Browse entries in the PDBbind-CN Database
HEADER IMMUNE SYSTEM/DNA 05-JUL-16 5GKR TITLE CRYSTAL STRUCTURE OF SLE PATIENT-DERIVED ANTI-DNA ANTIBODY IN COMPLEX TITLE 2 WITH OLIGONUCLEOTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: IGG2, FAB (HEAVY CHAIN); COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: LAMBDA, FAB (LIGHT CHAIN); COMPND 7 CHAIN: B, D; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: DNA (5'-D(P*TP*TP*TP*T)-3'); COMPND 11 CHAIN: T; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 13 MOL_ID: 3; SOURCE 14 SYNTHETIC: YES; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_TAXID: 9606 KEYWDS ANTIBODY, LUPUS, DNA, FAB, IMMUNE SYSTEM-DNA COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR T.ARIMORI,S.SAKAKIBARA,H.KIKUTANI,J.TAKAGI REVDAT 2 06-DEC-17 5GKR 1 JRNL REVDAT 1 05-JUL-17 5GKR 0 JRNL AUTH S.SAKAKIBARA,T.ARIMORI,K.YAMASHITA,H.JINZAI,D.MOTOOKA, JRNL AUTH 2 S.NAKAMURA,S.LI,K.TAKEDA,J.KATAYAMA,M.A.EL HUSSIEN, JRNL AUTH 3 M.NARAZAKI,T.TANAKA,D.M.STANDLEY,J.TAKAGI,H.KIKUTANI JRNL TITL CLONAL EVOLUTION AND ANTIGEN RECOGNITION OF ANTI-NUCLEAR JRNL TITL 2 ANTIBODIES IN ACUTE SYSTEMIC LUPUS ERYTHEMATOSUS JRNL REF SCI REP V. 7 16428 2017 JRNL REFN ESSN 2045-2322 JRNL PMID 29180749 JRNL DOI 10.1038/S41598-017-16681-Y REMARK 2 REMARK 2 RESOLUTION. 2.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0124 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.33 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 50879 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) : 0.164 REMARK 3 R VALUE (WORKING SET) : 0.163 REMARK 3 FREE R VALUE : 0.185 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 2609 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3756 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.75 REMARK 3 BIN R VALUE (WORKING SET) : 0.2030 REMARK 3 BIN FREE R VALUE SET COUNT : 176 REMARK 3 BIN FREE R VALUE : 0.2360 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6239 REMARK 3 NUCLEIC ACID ATOMS : 64 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 156 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.75 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -2.08000 REMARK 3 B22 (A**2) : -2.08000 REMARK 3 B33 (A**2) : 4.16000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.037 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.030 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.082 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.593 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6478 ; 0.007 ; 0.019 REMARK 3 BOND LENGTHS OTHERS (A): 5853 ; 0.003 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8855 ; 1.295 ; 1.938 REMARK 3 BOND ANGLES OTHERS (DEGREES): 13575 ; 1.051 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 819 ; 6.646 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 227 ;32.268 ;24.097 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 968 ;13.369 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;13.916 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1003 ; 0.075 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7225 ; 0.005 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): 1416 ; 0.003 ; 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): 3303 ; 0.545 ; 2.281 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3302 ; 0.545 ; 2.281 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4113 ; 0.961 ; 3.414 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4114 ; 0.961 ; 3.414 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3175 ; 0.515 ; 2.366 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3171 ; 0.508 ; 2.364 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4740 ; 0.882 ; 3.529 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 6698 ; 2.927 ;18.153 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 6697 ; 2.927 ;18.151 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 NCS TYPE: LOCAL REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 2 REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT REMARK 3 1 A 2 215 C 2 215 20840 0.11 0.05 REMARK 3 2 B 3 212 D 3 212 20906 0.10 0.05 REMARK 3 REMARK 3 TWIN DETAILS REMARK 3 NUMBER OF TWIN DOMAINS : 2 REMARK 3 TWIN DOMAIN : 1 REMARK 3 TWIN OPERATOR : H, K, L REMARK 3 TWIN FRACTION : 0.670 REMARK 3 TWIN DOMAIN : 2 REMARK 3 TWIN OPERATOR : K, H, -L REMARK 3 TWIN FRACTION : 0.330 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 8 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 2 A 116 REMARK 3 ORIGIN FOR THE GROUP (A): -35.5970 135.1140 1.2570 REMARK 3 T TENSOR REMARK 3 T11: 0.1273 T22: 0.1649 REMARK 3 T33: 0.0114 T12: 0.0018 REMARK 3 T13: 0.0021 T23: 0.0026 REMARK 3 L TENSOR REMARK 3 L11: 1.0819 L22: 1.1930 REMARK 3 L33: 1.5858 L12: 0.1180 REMARK 3 L13: -0.0177 L23: 0.3585 REMARK 3 S TENSOR REMARK 3 S11: -0.0290 S12: 0.0151 S13: 0.0287 REMARK 3 S21: 0.0029 S22: 0.0422 S23: -0.0508 REMARK 3 S31: -0.0403 S32: 0.0258 S33: -0.0132 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 : B 2 B 110 REMARK 3 ORIGIN FOR THE GROUP (A): -34.6150 133.6820 22.7750 REMARK 3 T TENSOR REMARK 3 T11: 0.1622 T22: 0.1479 REMARK 3 T33: 0.0162 T12: 0.0002 REMARK 3 T13: -0.0272 T23: -0.0149 REMARK 3 L TENSOR REMARK 3 L11: 1.7193 L22: 0.5354 REMARK 3 L33: 1.5829 L12: 0.1505 REMARK 3 L13: -0.1296 L23: -0.0845 REMARK 3 S TENSOR REMARK 3 S11: 0.0260 S12: -0.0131 S13: 0.0008 REMARK 3 S21: 0.0632 S22: 0.0191 S23: -0.0273 REMARK 3 S31: -0.0023 S32: -0.0586 S33: -0.0451 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 : C 2 C 116 REMARK 3 ORIGIN FOR THE GROUP (A): 5.7880 111.3720 28.9960 REMARK 3 T TENSOR REMARK 3 T11: 0.2665 T22: 0.1618 REMARK 3 T33: 0.0547 T12: 0.0625 REMARK 3 T13: 0.0047 T23: -0.0622 REMARK 3 L TENSOR REMARK 3 L11: 2.1201 L22: 3.0455 REMARK 3 L33: 3.4839 L12: 0.1678 REMARK 3 L13: 1.3708 L23: 0.9125 REMARK 3 S TENSOR REMARK 3 S11: 0.1718 S12: 0.1665 S13: -0.2658 REMARK 3 S21: 0.2682 S22: -0.0875 S23: -0.0334 REMARK 3 S31: 0.6925 S32: 0.1657 S33: -0.0843 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 : D 3 D 108 REMARK 3 ORIGIN FOR THE GROUP (A): -2.5670 114.3910 9.4370 REMARK 3 T TENSOR REMARK 3 T11: 0.2807 T22: 0.3353 REMARK 3 T33: 0.0804 T12: 0.0604 REMARK 3 T13: -0.0087 T23: -0.1542 REMARK 3 L TENSOR REMARK 3 L11: 2.9045 L22: 2.3881 REMARK 3 L33: 3.0415 L12: -1.3233 REMARK 3 L13: 1.5664 L23: -1.1496 REMARK 3 S TENSOR REMARK 3 S11: 0.2595 S12: 0.4894 S13: -0.1998 REMARK 3 S21: -0.1445 S22: -0.2104 S23: 0.1340 REMARK 3 S31: 0.5779 S32: 0.2754 S33: -0.0491 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 : A 117 A 212 REMARK 3 ORIGIN FOR THE GROUP (A): -62.3930 112.3280 9.1090 REMARK 3 T TENSOR REMARK 3 T11: 0.1258 T22: 0.1609 REMARK 3 T33: 0.0222 T12: -0.0678 REMARK 3 T13: -0.0140 T23: -0.0364 REMARK 3 L TENSOR REMARK 3 L11: 2.4058 L22: 2.1838 REMARK 3 L33: 1.3029 L12: 0.9305 REMARK 3 L13: -0.8022 L23: -0.8631 REMARK 3 S TENSOR REMARK 3 S11: -0.0469 S12: -0.1243 S13: 0.0386 REMARK 3 S21: -0.0171 S22: -0.0488 S23: -0.0121 REMARK 3 S31: -0.1098 S32: 0.0245 S33: 0.0956 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 111 B 210 REMARK 3 ORIGIN FOR THE GROUP (A): -48.8210 108.1300 18.0560 REMARK 3 T TENSOR REMARK 3 T11: 0.1089 T22: 0.1976 REMARK 3 T33: 0.0896 T12: -0.0160 REMARK 3 T13: -0.0699 T23: -0.0090 REMARK 3 L TENSOR REMARK 3 L11: 0.9056 L22: 6.0558 REMARK 3 L33: 3.8167 L12: 1.0732 REMARK 3 L13: 0.5661 L23: 3.5406 REMARK 3 S TENSOR REMARK 3 S11: 0.1454 S12: 0.0814 S13: -0.2595 REMARK 3 S21: 0.4927 S22: 0.1600 S23: -0.4143 REMARK 3 S31: 0.2408 S32: 0.2356 S33: -0.3054 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 117 C 213 REMARK 3 ORIGIN FOR THE GROUP (A): 3.2580 146.9260 28.1790 REMARK 3 T TENSOR REMARK 3 T11: 0.0887 T22: 0.1746 REMARK 3 T33: 0.0196 T12: -0.0585 REMARK 3 T13: -0.0130 T23: -0.0000 REMARK 3 L TENSOR REMARK 3 L11: 1.8174 L22: 2.2246 REMARK 3 L33: 2.1351 L12: -0.3382 REMARK 3 L13: 0.1862 L23: -0.7121 REMARK 3 S TENSOR REMARK 3 S11: -0.0333 S12: 0.2448 S13: 0.0986 REMARK 3 S21: -0.0586 S22: 0.0308 S23: 0.0417 REMARK 3 S31: -0.0747 S32: -0.0417 S33: 0.0024 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 : D 113 D 209 REMARK 3 ORIGIN FOR THE GROUP (A): 10.1840 142.6410 13.6950 REMARK 3 T TENSOR REMARK 3 T11: 0.1184 T22: 0.2539 REMARK 3 T33: 0.0120 T12: -0.0785 REMARK 3 T13: 0.0251 T23: -0.0331 REMARK 3 L TENSOR REMARK 3 L11: 5.4032 L22: 4.1044 REMARK 3 L33: 3.2454 L12: 3.9602 REMARK 3 L13: 0.8849 L23: 0.6946 REMARK 3 S TENSOR REMARK 3 S11: -0.3659 S12: 0.5756 S13: -0.0498 REMARK 3 S21: -0.5114 S22: 0.4662 S23: -0.1189 REMARK 3 S31: -0.0298 S32: 0.1019 S33: -0.1002 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL 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 5GKR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-JUL-16. REMARK 100 THE DEPOSITION ID IS D_1300000949. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 09-AUG-15 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSRRC REMARK 200 BEAMLINE : BL15A1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300HE REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53509 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 5.800 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.11500 REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 5.60 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.85700 REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 4QHK, 4Y5Y, 4IDJ, AND 4LLW REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.12 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL (PH 7.0), 0.2 M NACL, 1 REMARK 280 M SODIUM CITRATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 X+2/3,Y+1/3,Z+1/3 REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3 REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3 REMARK 290 7555 X+1/3,Y+2/3,Z+2/3 REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3 REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 73.75750 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 42.58391 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 37.60233 REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 73.75750 REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 42.58391 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 37.60233 REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 73.75750 REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 42.58391 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 37.60233 REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 85.16782 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 75.20467 REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 85.16782 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 75.20467 REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 85.16782 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 75.20467 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, T 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: 3370 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18830 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 GLN A 1 REMARK 465 SER A 127 REMARK 465 SER A 128 REMARK 465 LYS A 129 REMARK 465 SER A 130 REMARK 465 THR A 131 REMARK 465 SER A 132 REMARK 465 GLY A 133 REMARK 465 ARG A 213 REMARK 465 LYS A 214 REMARK 465 CYS A 215 REMARK 465 GLU B 211 REMARK 465 CYS B 212 REMARK 465 SER B 213 REMARK 465 GLN C 1 REMARK 465 ILE C 29 REMARK 465 SER C 30 REMARK 465 SER C 31 REMARK 465 SER C 127 REMARK 465 SER C 128 REMARK 465 LYS C 129 REMARK 465 SER C 130 REMARK 465 THR C 131 REMARK 465 SER C 132 REMARK 465 GLY C 133 REMARK 465 GLY C 134 REMARK 465 SER C 188 REMARK 465 LEU C 189 REMARK 465 LYS C 214 REMARK 465 CYS C 215 REMARK 465 GLN D 1 REMARK 465 SER D 2 REMARK 465 GLN D 109 REMARK 465 PRO D 110 REMARK 465 LYS D 111 REMARK 465 ALA D 112 REMARK 465 THR D 210 REMARK 465 GLU D 211 REMARK 465 CYS D 212 REMARK 465 SER D 213 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 DT T 4 C5' C4' O4' C3' O3' C2' C1' REMARK 470 DT T 4 N1 C2 O2 N3 C4 O4 C5 REMARK 470 DT T 4 C7 C6 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 TYR A 32 -179.34 72.17 REMARK 500 THR A 191 -55.93 -130.40 REMARK 500 ASP B 29 -90.82 -137.84 REMARK 500 ASN B 31 49.03 -109.41 REMARK 500 TYR B 32 55.77 -117.39 REMARK 500 VAL B 51 -55.74 69.51 REMARK 500 ASN B 171 -0.81 77.38 REMARK 500 THR C 191 -55.10 -132.70 REMARK 500 ASP D 29 -90.77 -136.90 REMARK 500 ASN D 31 49.12 -109.25 REMARK 500 TYR D 32 55.95 -117.78 REMARK 500 VAL D 51 -55.86 69.97 REMARK 500 ASN D 171 -1.39 77.60 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5GKS RELATED DB: PDB DBREF 5GKR A 1 215 PDB 5GKR 5GKR 1 215 DBREF 5GKR B 1 213 PDB 5GKR 5GKR 1 213 DBREF 5GKR C 1 215 PDB 5GKR 5GKR 1 215 DBREF 5GKR D 1 213 PDB 5GKR 5GKR 1 213 DBREF 5GKR T 1 4 PDB 5GKR 5GKR 1 4 SEQRES 1 A 218 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 A 218 SER SER GLU THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 A 218 GLY SER ILE SER SER TYR PHE TRP SER TRP ILE ARG GLN SEQRES 4 A 218 PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE TYR SEQRES 5 A 218 TYR SER GLY SER THR ASN TYR ASN PRO SER LEU LYS SER SEQRES 6 A 218 ARG VAL THR ILE SER LEU HIS THR SER LYS ASN GLN PHE SEQRES 7 A 218 SER LEU LYS LEU SER SER VAL THR ALA ALA ASP THR ALA SEQRES 8 A 218 VAL TYR TYR CYS ALA ARG HIS ARG ASN TRP LEU PHE ASP SEQRES 9 A 218 TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SEQRES 10 A 218 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 11 A 218 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 12 A 218 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 13 A 218 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 14 A 218 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 15 A 218 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN SEQRES 16 A 218 THR TYR THR CYS ASN VAL ASP HIS LYS PRO SER ASN THR SEQRES 17 A 218 LYS VAL ASP LYS THR VAL GLU ARG LYS CYS SEQRES 1 B 216 GLN SER ALA LEU THR GLN PRO ARG SER VAL SER GLY SER SEQRES 2 B 216 PRO GLY GLN SER VAL THR ILE SER CYS THR GLY THR SER SEQRES 3 B 216 SER ASP VAL GLY GLY TYR ASN TYR VAL SER TRP TYR GLN SEQRES 4 B 216 GLN HIS PRO GLY LYS ALA PRO LYS VAL MET ILE TYR ASP SEQRES 5 B 216 VAL SER LYS ARG PRO SER GLY VAL PRO ASP ARG PHE SER SEQRES 6 B 216 GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER SEQRES 7 B 216 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS CYS SEQRES 8 B 216 SER TYR ALA GLY SER TYR THR TYR VAL PHE GLY THR GLY SEQRES 9 B 216 THR LYS VAL THR VAL LEU GLY GLN PRO LYS ALA ASN PRO SEQRES 10 B 216 THR VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 B 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 B 216 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP GLY SEQRES 13 B 216 SER PRO VAL LYS ALA GLY VAL GLU THR THR LYS PRO SER SEQRES 14 B 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 B 216 SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SEQRES 16 B 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 B 216 THR VAL ALA PRO THR GLU CYS SER SEQRES 1 C 218 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 C 218 SER SER GLU THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 C 218 GLY SER ILE SER SER TYR PHE TRP SER TRP ILE ARG GLN SEQRES 4 C 218 PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE TYR SEQRES 5 C 218 TYR SER GLY SER THR ASN TYR ASN PRO SER LEU LYS SER SEQRES 6 C 218 ARG VAL THR ILE SER LEU HIS THR SER LYS ASN GLN PHE SEQRES 7 C 218 SER LEU LYS LEU SER SER VAL THR ALA ALA ASP THR ALA SEQRES 8 C 218 VAL TYR TYR CYS ALA ARG HIS ARG ASN TRP LEU PHE ASP SEQRES 9 C 218 TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SEQRES 10 C 218 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 11 C 218 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 12 C 218 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 13 C 218 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 14 C 218 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 15 C 218 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN SEQRES 16 C 218 THR TYR THR CYS ASN VAL ASP HIS LYS PRO SER ASN THR SEQRES 17 C 218 LYS VAL ASP LYS THR VAL GLU ARG LYS CYS SEQRES 1 D 216 GLN SER ALA LEU THR GLN PRO ARG SER VAL SER GLY SER SEQRES 2 D 216 PRO GLY GLN SER VAL THR ILE SER CYS THR GLY THR SER SEQRES 3 D 216 SER ASP VAL GLY GLY TYR ASN TYR VAL SER TRP TYR GLN SEQRES 4 D 216 GLN HIS PRO GLY LYS ALA PRO LYS VAL MET ILE TYR ASP SEQRES 5 D 216 VAL SER LYS ARG PRO SER GLY VAL PRO ASP ARG PHE SER SEQRES 6 D 216 GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER SEQRES 7 D 216 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS CYS SEQRES 8 D 216 SER TYR ALA GLY SER TYR THR TYR VAL PHE GLY THR GLY SEQRES 9 D 216 THR LYS VAL THR VAL LEU GLY GLN PRO LYS ALA ASN PRO SEQRES 10 D 216 THR VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 D 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 D 216 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP GLY SEQRES 13 D 216 SER PRO VAL LYS ALA GLY VAL GLU THR THR LYS PRO SER SEQRES 14 D 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 D 216 SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SEQRES 16 D 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 D 216 THR VAL ALA PRO THR GLU CYS SER SEQRES 1 T 4 DT DT DT DT FORMUL 6 HOH *156(H2 O) HELIX 1 AA1 LEU A 63 SER A 65 5 3 HELIX 2 AA2 THR A 83 THR A 87 5 5 HELIX 3 AA3 SER A 156 ALA A 158 5 3 HELIX 4 AA4 SER A 187 LEU A 189 5 3 HELIX 5 AA5 LYS A 201 ASN A 204 5 4 HELIX 6 AA6 GLN B 79 GLU B 83 5 5 HELIX 7 AA7 SER B 122 ALA B 128 1 7 HELIX 8 AA8 THR B 182 HIS B 189 1 8 HELIX 9 AA9 LEU C 63 SER C 65 5 3 HELIX 10 AB1 THR C 83 THR C 87 5 5 HELIX 11 AB2 SER C 156 ALA C 158 5 3 HELIX 12 AB3 LYS C 201 ASN C 204 5 4 HELIX 13 AB4 GLN D 79 GLU D 83 5 5 HELIX 14 AB5 SER D 122 ALA D 128 1 7 HELIX 15 AB6 THR D 182 HIS D 189 1 8 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O THR A 21 N SER A 7 SHEET 3 AA1 4 GLN A 77 LEU A 82 -1 O PHE A 78 N CYS A 22 SHEET 4 AA1 4 VAL A 67 HIS A 72 -1 N HIS A 72 O GLN A 77 SHEET 1 AA2 6 LEU A 11 VAL A 12 0 SHEET 2 AA2 6 THR A 107 VAL A 111 1 O THR A 110 N VAL A 12 SHEET 3 AA2 6 ALA A 88 ARG A 96 -1 N ALA A 88 O VAL A 109 SHEET 4 AA2 6 PHE A 33 GLN A 39 -1 N ILE A 37 O TYR A 91 SHEET 5 AA2 6 GLU A 46 TYR A 52 -1 O GLU A 46 N ARG A 38 SHEET 6 AA2 6 THR A 57 TYR A 59 -1 O ASN A 58 N TYR A 50 SHEET 1 AA3 4 LEU A 11 VAL A 12 0 SHEET 2 AA3 4 THR A 107 VAL A 111 1 O THR A 110 N VAL A 12 SHEET 3 AA3 4 ALA A 88 ARG A 96 -1 N ALA A 88 O VAL A 109 SHEET 4 AA3 4 LEU A 99 TRP A 103 -1 O LEU A 99 N ARG A 96 SHEET 1 AA4 4 SER A 120 LEU A 124 0 SHEET 2 AA4 4 THR A 135 TYR A 145 -1 O LYS A 143 N SER A 120 SHEET 3 AA4 4 TYR A 176 PRO A 185 -1 O LEU A 178 N VAL A 142 SHEET 4 AA4 4 VAL A 163 THR A 165 -1 N HIS A 164 O VAL A 181 SHEET 1 AA5 4 SER A 120 LEU A 124 0 SHEET 2 AA5 4 THR A 135 TYR A 145 -1 O LYS A 143 N SER A 120 SHEET 3 AA5 4 TYR A 176 PRO A 185 -1 O LEU A 178 N VAL A 142 SHEET 4 AA5 4 VAL A 169 LEU A 170 -1 N VAL A 169 O SER A 177 SHEET 1 AA6 3 THR A 151 TRP A 154 0 SHEET 2 AA6 3 TYR A 194 HIS A 200 -1 O ASN A 197 N SER A 153 SHEET 3 AA6 3 THR A 205 VAL A 211 -1 O VAL A 207 N VAL A 198 SHEET 1 AA7 5 SER B 9 GLY B 13 0 SHEET 2 AA7 5 THR B 102 VAL B 106 1 O LYS B 103 N VAL B 11 SHEET 3 AA7 5 ALA B 84 TYR B 91 -1 N ALA B 84 O VAL B 104 SHEET 4 AA7 5 VAL B 33 GLN B 38 -1 N GLN B 38 O ASP B 85 SHEET 5 AA7 5 LYS B 45 ILE B 48 -1 O MET B 47 N TRP B 35 SHEET 1 AA8 4 SER B 9 GLY B 13 0 SHEET 2 AA8 4 THR B 102 VAL B 106 1 O LYS B 103 N VAL B 11 SHEET 3 AA8 4 ALA B 84 TYR B 91 -1 N ALA B 84 O VAL B 104 SHEET 4 AA8 4 TYR B 96 PHE B 98 -1 O VAL B 97 N SER B 90 SHEET 1 AA9 3 VAL B 19 THR B 24 0 SHEET 2 AA9 3 THR B 70 ILE B 75 -1 O LEU B 73 N ILE B 21 SHEET 3 AA9 3 PHE B 62 SER B 67 -1 N SER B 67 O THR B 70 SHEET 1 AB1 4 THR B 115 PHE B 119 0 SHEET 2 AB1 4 ALA B 131 PHE B 140 -1 O LEU B 136 N THR B 117 SHEET 3 AB1 4 TYR B 173 LEU B 181 -1 O SER B 177 N CYS B 135 SHEET 4 AB1 4 VAL B 160 THR B 162 -1 N GLU B 161 O TYR B 178 SHEET 1 AB2 4 THR B 115 PHE B 119 0 SHEET 2 AB2 4 ALA B 131 PHE B 140 -1 O LEU B 136 N THR B 117 SHEET 3 AB2 4 TYR B 173 LEU B 181 -1 O SER B 177 N CYS B 135 SHEET 4 AB2 4 SER B 166 LYS B 167 -1 N SER B 166 O ALA B 174 SHEET 1 AB3 4 SER B 154 VAL B 156 0 SHEET 2 AB3 4 THR B 146 ALA B 151 -1 N ALA B 151 O SER B 154 SHEET 3 AB3 4 TYR B 192 HIS B 198 -1 O GLN B 195 N ALA B 148 SHEET 4 AB3 4 SER B 201 VAL B 207 -1 O VAL B 203 N VAL B 196 SHEET 1 AB4 4 GLN C 3 SER C 7 0 SHEET 2 AB4 4 LEU C 18 SER C 25 -1 O THR C 21 N SER C 7 SHEET 3 AB4 4 GLN C 77 LEU C 82 -1 O PHE C 78 N CYS C 22 SHEET 4 AB4 4 VAL C 67 HIS C 72 -1 N HIS C 72 O GLN C 77 SHEET 1 AB5 6 LEU C 11 VAL C 12 0 SHEET 2 AB5 6 THR C 107 VAL C 111 1 O THR C 110 N VAL C 12 SHEET 3 AB5 6 ALA C 88 ARG C 96 -1 N ALA C 88 O VAL C 109 SHEET 4 AB5 6 PHE C 33 GLN C 39 -1 N ILE C 37 O TYR C 91 SHEET 5 AB5 6 GLU C 46 TYR C 52 -1 O GLU C 46 N ARG C 38 SHEET 6 AB5 6 THR C 57 TYR C 59 -1 O ASN C 58 N TYR C 50 SHEET 1 AB6 4 LEU C 11 VAL C 12 0 SHEET 2 AB6 4 THR C 107 VAL C 111 1 O THR C 110 N VAL C 12 SHEET 3 AB6 4 ALA C 88 ARG C 96 -1 N ALA C 88 O VAL C 109 SHEET 4 AB6 4 LEU C 99 TRP C 103 -1 O LEU C 99 N ARG C 96 SHEET 1 AB7 4 SER C 120 LEU C 124 0 SHEET 2 AB7 4 ALA C 136 TYR C 145 -1 O LYS C 143 N SER C 120 SHEET 3 AB7 4 TYR C 176 VAL C 184 -1 O VAL C 182 N LEU C 138 SHEET 4 AB7 4 VAL C 163 THR C 165 -1 N HIS C 164 O VAL C 181 SHEET 1 AB8 4 SER C 120 LEU C 124 0 SHEET 2 AB8 4 ALA C 136 TYR C 145 -1 O LYS C 143 N SER C 120 SHEET 3 AB8 4 TYR C 176 VAL C 184 -1 O VAL C 182 N LEU C 138 SHEET 4 AB8 4 VAL C 169 LEU C 170 -1 N VAL C 169 O SER C 177 SHEET 1 AB9 3 THR C 151 TRP C 154 0 SHEET 2 AB9 3 TYR C 194 HIS C 200 -1 O ASN C 197 N SER C 153 SHEET 3 AB9 3 THR C 205 VAL C 211 -1 O VAL C 207 N VAL C 198 SHEET 1 AC1 5 SER D 9 GLY D 13 0 SHEET 2 AC1 5 THR D 102 VAL D 106 1 O LYS D 103 N VAL D 11 SHEET 3 AC1 5 ALA D 84 TYR D 91 -1 N ALA D 84 O VAL D 104 SHEET 4 AC1 5 VAL D 33 GLN D 38 -1 N GLN D 38 O ASP D 85 SHEET 5 AC1 5 LYS D 45 ILE D 48 -1 O MET D 47 N TRP D 35 SHEET 1 AC2 4 SER D 9 GLY D 13 0 SHEET 2 AC2 4 THR D 102 VAL D 106 1 O LYS D 103 N VAL D 11 SHEET 3 AC2 4 ALA D 84 TYR D 91 -1 N ALA D 84 O VAL D 104 SHEET 4 AC2 4 TYR D 96 PHE D 98 -1 O VAL D 97 N SER D 90 SHEET 1 AC3 3 VAL D 19 THR D 24 0 SHEET 2 AC3 3 THR D 70 ILE D 75 -1 O LEU D 73 N ILE D 21 SHEET 3 AC3 3 PHE D 62 SER D 67 -1 N SER D 67 O THR D 70 SHEET 1 AC4 4 THR D 115 PHE D 119 0 SHEET 2 AC4 4 ALA D 131 PHE D 140 -1 O LEU D 136 N THR D 117 SHEET 3 AC4 4 TYR D 173 LEU D 181 -1 O SER D 177 N CYS D 135 SHEET 4 AC4 4 VAL D 160 THR D 162 -1 N GLU D 161 O TYR D 178 SHEET 1 AC5 4 THR D 115 PHE D 119 0 SHEET 2 AC5 4 ALA D 131 PHE D 140 -1 O LEU D 136 N THR D 117 SHEET 3 AC5 4 TYR D 173 LEU D 181 -1 O SER D 177 N CYS D 135 SHEET 4 AC5 4 SER D 166 LYS D 167 -1 N SER D 166 O ALA D 174 SHEET 1 AC6 4 SER D 154 VAL D 156 0 SHEET 2 AC6 4 THR D 146 ALA D 151 -1 N ALA D 151 O SER D 154 SHEET 3 AC6 4 TYR D 192 HIS D 198 -1 O GLN D 195 N ALA D 148 SHEET 4 AC6 4 SER D 201 VAL D 207 -1 O VAL D 203 N VAL D 196 SSBOND 1 CYS A 22 CYS A 92 1555 1555 2.09 SSBOND 2 CYS A 140 CYS A 196 1555 1555 2.05 SSBOND 3 CYS B 23 CYS B 88 1555 1555 2.04 SSBOND 4 CYS B 135 CYS B 194 1555 1555 2.03 SSBOND 5 CYS C 22 CYS C 92 1555 1555 2.06 SSBOND 6 CYS C 140 CYS C 196 1555 1555 2.03 SSBOND 7 CYS D 23 CYS D 88 1555 1555 2.03 SSBOND 8 CYS D 135 CYS D 194 1555 1555 2.03 CISPEP 1 PHE A 146 PRO A 147 0 -5.70 CISPEP 2 GLU A 148 PRO A 149 0 -1.68 CISPEP 3 TYR B 141 PRO B 142 0 0.74 CISPEP 4 PHE C 146 PRO C 147 0 -7.81 CISPEP 5 GLU C 148 PRO C 149 0 2.32 CISPEP 6 TYR D 141 PRO D 142 0 -0.30 CRYST1 147.515 147.515 112.807 90.00 90.00 120.00 H 3 18 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 0.006779 0.003914 0.000000 0.00000 SCALE2 0.000000 0.007828 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008865 0.00000 ATOM 1 N VAL A 2 -39.790 151.982 7.502 1.00 37.28 N ANISOU 1 N VAL A 2 5574 4560 4032 343 -8 -292 N ATOM 2 CA VAL A 2 -39.027 150.955 6.703 1.00 36.36 C ANISOU 2 CA VAL A 2 5407 4516 3894 265 -16 -227 C ATOM 3 C VAL A 2 -39.730 149.611 6.801 1.00 34.57 C ANISOU 3 C VAL A 2 5085 4415 3635 300 -8 -212 C ATOM 4 O VAL A 2 -40.156 149.192 7.877 1.00 34.49 O ANISOU 4 O VAL A 2 5040 4464 3599 325 10 -263 O ATOM 5 CB VAL A 2 -37.536 150.756 7.125 1.00 37.00 C ANISOU 5 CB VAL A 2 5487 4612 3959 151 -19 -252 C ATOM 6 CG1 VAL A 2 -36.808 149.939 6.058 1.00 36.55 C ANISOU 6 CG1 VAL A 2 5387 4606 3894 88 -23 -185 C ATOM 7 CG2 VAL A 2 -36.807 152.085 7.348 1.00 38.62 C ANISOU 7 CG2 VAL A 2 5782 4698 4195 98 -22 -292 C ATOM 8 N GLN A 3 -39.815 148.927 5.671 1.00 32.93 N ANISOU 8 N GLN A 3 4841 4246 3423 291 -18 -143 N ATOM 9 CA GLN A 3 -40.721 147.802 5.540 1.00 30.96 C ANISOU 9 CA GLN A 3 4513 4097 3155 331 -12 -125 C ATOM 10 C GLN A 3 -40.337 146.874 4.394 1.00 29.16 C ANISOU 10 C GLN A 3 4252 3916 2913 285 -23 -61 C ATOM 11 O GLN A 3 -40.008 147.338 3.297 1.00 29.00 O ANISOU 11 O GLN A 3 4271 3847 2902 267 -38 -13 O ATOM 12 CB GLN A 3 -42.105 148.379 5.329 1.00 31.70 C ANISOU 12 CB GLN A 3 4602 4171 3273 434 -17 -126 C ATOM 13 CG GLN A 3 -43.172 147.372 4.992 1.00 31.30 C ANISOU 13 CG GLN A 3 4464 4219 3211 473 -16 -106 C ATOM 14 CD GLN A 3 -44.556 147.966 5.093 1.00 32.01 C ANISOU 14 CD GLN A 3 4527 4306 3328 582 -18 -129 C ATOM 15 OE1 GLN A 3 -44.745 149.178 4.951 1.00 33.09 O ANISOU 15 OE1 GLN A 3 4723 4350 3498 642 -34 -135 O ATOM 16 NE2 GLN A 3 -45.531 147.119 5.349 1.00 31.58 N ANISOU 16 NE2 GLN A 3 4383 4353 3265 608 0 -145 N ATOM 17 N LEU A 4 -40.422 145.570 4.671 1.00 27.06 N ANISOU 17 N LEU A 4 3921 3742 2619 267 -12 -63 N ATOM 18 CA LEU A 4 -40.155 144.495 3.721 1.00 26.10 C ANISOU 18 CA LEU A 4 3762 3672 2481 229 -17 -18 C ATOM 19 C LEU A 4 -41.405 143.645 3.574 1.00 25.25 C ANISOU 19 C LEU A 4 3594 3634 2365 271 -14 -11 C ATOM 20 O LEU A 4 -42.084 143.381 4.565 1.00 25.45 O ANISOU 20 O LEU A 4 3589 3696 2384 298 5 -47 O ATOM 21 CB LEU A 4 -39.039 143.600 4.251 1.00 25.64 C ANISOU 21 CB LEU A 4 3685 3652 2404 166 -9 -32 C ATOM 22 CG LEU A 4 -37.603 144.118 4.151 1.00 25.85 C ANISOU 22 CG LEU A 4 3744 3638 2439 104 -13 -37 C ATOM 23 CD1 LEU A 4 -37.336 145.270 5.104 1.00 26.66 C ANISOU 23 CD1 LEU A 4 3893 3682 2555 103 -16 -83 C ATOM 24 CD2 LEU A 4 -36.625 142.987 4.426 1.00 25.41 C ANISOU 24 CD2 LEU A 4 3647 3639 2367 60 -13 -43 C ATOM 25 N GLN A 5 -41.715 143.226 2.351 1.00 24.75 N ANISOU 25 N GLN A 5 3512 3593 2297 270 -31 31 N ATOM 26 CA GLN A 5 -42.863 142.358 2.081 1.00 24.29 C ANISOU 26 CA GLN A 5 3391 3608 2232 294 -33 35 C ATOM 27 C GLN A 5 -42.598 141.410 0.915 1.00 23.86 C ANISOU 27 C GLN A 5 3321 3588 2156 250 -45 69 C ATOM 28 O GLN A 5 -42.106 141.826 -0.132 1.00 23.74 O ANISOU 28 O GLN A 5 3345 3544 2134 237 -63 104 O ATOM 29 CB GLN A 5 -44.103 143.207 1.795 1.00 25.06 C ANISOU 29 CB GLN A 5 3474 3698 2351 375 -55 36 C ATOM 30 CG GLN A 5 -44.689 143.957 2.988 1.00 25.42 C ANISOU 30 CG GLN A 5 3515 3726 2418 433 -35 -13 C ATOM 31 CD GLN A 5 -44.894 143.159 4.278 1.00 25.05 C ANISOU 31 CD GLN A 5 3426 3738 2355 411 9 -59 C ATOM 32 OE1 GLN A 5 -44.900 141.930 4.299 1.00 24.60 O ANISOU 32 OE1 GLN A 5 3330 3740 2276 362 23 -51 O ATOM 33 NE2 GLN A 5 -45.064 143.884 5.375 1.00 25.50 N ANISOU 33 NE2 GLN A 5 3500 3772 2418 447 33 -106 N ATOM 34 N GLU A 6 -42.981 140.145 1.094 1.00 23.57 N ANISOU 34 N GLU A 6 3235 3614 2109 226 -32 57 N ATOM 35 CA GLU A 6 -42.752 139.094 0.100 1.00 23.33 C ANISOU 35 CA GLU A 6 3191 3615 2058 182 -38 75 C ATOM 36 C GLU A 6 -43.899 139.067 -0.893 1.00 23.79 C ANISOU 36 C GLU A 6 3215 3714 2110 209 -70 88 C ATOM 37 O GLU A 6 -45.065 139.216 -0.494 1.00 24.37 O ANISOU 37 O GLU A 6 3239 3820 2199 249 -74 71 O ATOM 38 CB GLU A 6 -42.673 137.697 0.737 1.00 23.13 C ANISOU 38 CB GLU A 6 3138 3625 2025 142 -11 56 C ATOM 39 CG GLU A 6 -41.718 137.527 1.902 1.00 22.79 C ANISOU 39 CG GLU A 6 3120 3558 1981 125 11 42 C ATOM 40 CD GLU A 6 -42.269 138.053 3.219 1.00 23.19 C ANISOU 40 CD GLU A 6 3166 3611 2036 155 28 17 C ATOM 41 OE1 GLU A 6 -43.412 138.559 3.264 1.00 23.60 O ANISOU 41 OE1 GLU A 6 3188 3682 2098 194 28 7 O ATOM 42 OE2 GLU A 6 -41.547 137.993 4.223 1.00 22.72 O ANISOU 42 OE2 GLU A 6 3129 3537 1965 144 39 4 O ATOM 43 N SER A 7 -43.574 138.880 -2.174 1.00 23.70 N ANISOU 43 N SER A 7 3225 3707 2073 186 -91 115 N ATOM 44 CA SER A 7 -44.572 138.673 -3.225 1.00 24.14 C ANISOU 44 CA SER A 7 3249 3813 2110 201 -131 125 C ATOM 45 C SER A 7 -44.192 137.455 -4.088 1.00 24.01 C ANISOU 45 C SER A 7 3233 3830 2060 139 -127 120 C ATOM 46 O SER A 7 -43.019 137.055 -4.193 1.00 23.36 O ANISOU 46 O SER A 7 3187 3722 1968 97 -99 120 O ATOM 47 CB SER A 7 -44.753 139.955 -4.067 1.00 24.86 C ANISOU 47 CB SER A 7 3384 3874 2190 253 -174 167 C ATOM 48 OG SER A 7 -43.570 140.272 -4.791 1.00 25.10 O ANISOU 48 OG SER A 7 3486 3859 2190 216 -165 200 O ATOM 49 N GLY A 8 -45.196 136.817 -4.676 1.00 24.38 N ANISOU 49 N GLY A 8 3232 3938 2094 133 -155 107 N ATOM 50 CA GLY A 8 -44.913 135.690 -5.597 1.00 24.70 C ANISOU 50 CA GLY A 8 3279 4006 2099 75 -154 93 C ATOM 51 C GLY A 8 -45.865 134.557 -5.299 1.00 25.12 C ANISOU 51 C GLY A 8 3269 4110 2167 42 -151 53 C ATOM 52 O GLY A 8 -46.645 134.656 -4.349 1.00 24.74 O ANISOU 52 O GLY A 8 3169 4077 2153 60 -141 40 O ATOM 53 N PRO A 9 -45.806 133.474 -6.091 1.00 25.33 N ANISOU 53 N PRO A 9 3300 4160 2167 -13 -154 30 N ATOM 54 CA PRO A 9 -46.910 132.500 -5.955 1.00 26.22 C ANISOU 54 CA PRO A 9 3349 4323 2293 -54 -159 -10 C ATOM 55 C PRO A 9 -46.913 131.677 -4.688 1.00 26.44 C ANISOU 55 C PRO A 9 3363 4324 2359 -89 -105 -29 C ATOM 56 O PRO A 9 -45.858 131.376 -4.149 1.00 26.49 O ANISOU 56 O PRO A 9 3420 4272 2372 -96 -67 -21 O ATOM 57 CB PRO A 9 -46.760 131.596 -7.183 1.00 26.34 C ANISOU 57 CB PRO A 9 3386 4357 2264 -107 -177 -35 C ATOM 58 CG PRO A 9 -45.834 132.305 -8.119 1.00 26.30 C ANISOU 58 CG PRO A 9 3445 4334 2212 -81 -190 -4 C ATOM 59 CD PRO A 9 -45.026 133.297 -7.334 1.00 25.75 C ANISOU 59 CD PRO A 9 3406 4208 2168 -36 -163 35 C ATOM 60 N GLY A 10 -48.120 131.366 -4.225 1.00 27.17 N ANISOU 60 N GLY A 10 3383 4466 2473 -109 -104 -52 N ATOM 61 CA GLY A 10 -48.373 130.480 -3.107 1.00 27.46 C ANISOU 61 CA GLY A 10 3407 4489 2537 -159 -51 -69 C ATOM 62 C GLY A 10 -48.307 128.979 -3.408 1.00 27.87 C ANISOU 62 C GLY A 10 3484 4521 2586 -244 -32 -98 C ATOM 63 O GLY A 10 -48.247 128.186 -2.478 1.00 27.53 O ANISOU 63 O GLY A 10 3460 4441 2559 -286 16 -99 O ATOM 64 N LEU A 11 -48.383 128.587 -4.685 1.00 28.38 N ANISOU 64 N LEU A 11 3552 4607 2624 -271 -71 -121 N ATOM 65 CA LEU A 11 -48.322 127.180 -5.095 1.00 28.94 C ANISOU 65 CA LEU A 11 3654 4650 2690 -352 -56 -159 C ATOM 66 C LEU A 11 -47.289 127.010 -6.208 1.00 28.84 C ANISOU 66 C LEU A 11 3710 4607 2641 -342 -73 -167 C ATOM 67 O LEU A 11 -47.364 127.678 -7.238 1.00 28.26 O ANISOU 67 O LEU A 11 3627 4581 2529 -314 -119 -165 O ATOM 68 CB LEU A 11 -49.700 126.695 -5.577 1.00 30.21 C ANISOU 68 CB LEU A 11 3738 4887 2854 -418 -84 -204 C ATOM 69 CG LEU A 11 -49.833 125.256 -6.104 1.00 31.11 C ANISOU 69 CG LEU A 11 3882 4975 2965 -516 -76 -256 C ATOM 70 CD1 LEU A 11 -49.365 124.211 -5.097 1.00 30.99 C ANISOU 70 CD1 LEU A 11 3930 4863 2980 -563 -8 -250 C ATOM 71 CD2 LEU A 11 -51.278 124.971 -6.503 1.00 32.27 C ANISOU 71 CD2 LEU A 11 3931 5213 3117 -584 -109 -303 C ATOM 72 N VAL A 12 -46.303 126.153 -5.960 1.00 28.64 N ANISOU 72 N VAL A 12 3754 4503 2625 -357 -33 -174 N ATOM 73 CA VAL A 12 -45.304 125.770 -6.952 1.00 29.01 C ANISOU 73 CA VAL A 12 3861 4520 2642 -353 -34 -196 C ATOM 74 C VAL A 12 -45.358 124.259 -7.205 1.00 29.84 C ANISOU 74 C VAL A 12 4006 4577 2756 -422 -14 -249 C ATOM 75 O VAL A 12 -45.661 123.479 -6.296 1.00 29.95 O ANISOU 75 O VAL A 12 4029 4542 2807 -461 16 -249 O ATOM 76 CB VAL A 12 -43.896 126.160 -6.427 1.00 28.29 C ANISOU 76 CB VAL A 12 3815 4373 2562 -293 -4 -162 C ATOM 77 CG1 VAL A 12 -42.750 125.697 -7.333 1.00 28.49 C ANISOU 77 CG1 VAL A 12 3893 4369 2564 -285 11 -191 C ATOM 78 CG2 VAL A 12 -43.801 127.659 -6.178 1.00 27.82 C ANISOU 78 CG2 VAL A 12 3728 4347 2497 -235 -20 -115 C ATOM 79 N LYS A 13 -45.032 123.854 -8.433 1.00 30.42 N ANISOU 79 N LYS A 13 4111 4656 2790 -438 -27 -294 N ATOM 80 CA LYS A 13 -45.015 122.437 -8.794 1.00 31.62 C ANISOU 80 CA LYS A 13 4313 4752 2949 -500 -9 -355 C ATOM 81 C LYS A 13 -43.727 121.774 -8.322 1.00 30.96 C ANISOU 81 C LYS A 13 4301 4568 2896 -463 38 -354 C ATOM 82 O LYS A 13 -42.674 122.412 -8.239 1.00 29.99 O ANISOU 82 O LYS A 13 4187 4440 2769 -393 50 -324 O ATOM 83 CB LYS A 13 -45.173 122.247 -10.300 1.00 33.08 C ANISOU 83 CB LYS A 13 4509 4987 3074 -531 -41 -415 C ATOM 84 CG LYS A 13 -46.504 122.730 -10.855 1.00 34.59 C ANISOU 84 CG LYS A 13 4628 5282 3232 -569 -102 -425 C ATOM 85 CD LYS A 13 -46.680 122.258 -12.282 1.00 36.27 C ANISOU 85 CD LYS A 13 4866 5537 3380 -614 -136 -494 C ATOM 86 CE LYS A 13 -47.805 122.993 -12.999 1.00 37.62 C ANISOU 86 CE LYS A 13 4964 5828 3501 -626 -214 -494 C ATOM 87 NZ LYS A 13 -49.128 122.780 -12.342 1.00 38.25 N ANISOU 87 NZ LYS A 13 4958 5944 3629 -681 -236 -503 N ATOM 88 N SER A 14 -43.828 120.487 -8.010 1.00 31.20 N ANISOU 88 N SER A 14 4381 4516 2960 -510 62 -386 N ATOM 89 CA SER A 14 -42.682 119.676 -7.598 1.00 31.25 C ANISOU 89 CA SER A 14 4460 4415 2999 -468 99 -391 C ATOM 90 C SER A 14 -41.624 119.642 -8.711 1.00 31.28 C ANISOU 90 C SER A 14 4492 4422 2972 -423 107 -438 C ATOM 91 O SER A 14 -41.958 119.646 -9.899 1.00 31.40 O ANISOU 91 O SER A 14 4502 4490 2938 -458 90 -490 O ATOM 92 CB SER A 14 -43.132 118.249 -7.239 1.00 32.20 C ANISOU 92 CB SER A 14 4643 4437 3156 -536 120 -421 C ATOM 93 OG SER A 14 -42.202 117.639 -6.366 1.00 32.82 O ANISOU 93 OG SER A 14 4786 4408 3275 -482 148 -393 O ATOM 94 N SER A 15 -40.358 119.638 -8.300 1.00 31.08 N ANISOU 94 N SER A 15 4489 4349 2970 -345 132 -421 N ATOM 95 CA SER A 15 -39.191 119.639 -9.197 1.00 31.35 C ANISOU 95 CA SER A 15 4538 4391 2984 -293 153 -464 C ATOM 96 C SER A 15 -39.039 120.896 -10.068 1.00 30.94 C ANISOU 96 C SER A 15 4439 4448 2871 -283 143 -454 C ATOM 97 O SER A 15 -38.302 120.861 -11.037 1.00 30.74 O ANISOU 97 O SER A 15 4426 4444 2809 -265 166 -499 O ATOM 98 CB SER A 15 -39.144 118.386 -10.100 1.00 32.64 C ANISOU 98 CB SER A 15 4763 4499 3140 -322 171 -555 C ATOM 99 OG SER A 15 -39.326 117.214 -9.325 1.00 33.75 O ANISOU 99 OG SER A 15 4963 4523 3339 -336 181 -561 O ATOM 100 N GLU A 16 -39.698 121.997 -9.706 1.00 30.80 N ANISOU 100 N GLU A 16 4372 4493 2840 -292 113 -393 N ATOM 101 CA GLU A 16 -39.539 123.271 -10.406 1.00 30.76 C ANISOU 101 CA GLU A 16 4334 4573 2780 -278 100 -367 C ATOM 102 C GLU A 16 -38.867 124.247 -9.456 1.00 29.59 C ANISOU 102 C GLU A 16 4156 4424 2664 -224 107 -302 C ATOM 103 O GLU A 16 -38.442 123.854 -8.368 1.00 29.29 O ANISOU 103 O GLU A 16 4122 4327 2680 -195 120 -286 O ATOM 104 CB GLU A 16 -40.894 123.770 -10.915 1.00 31.69 C ANISOU 104 CB GLU A 16 4424 4761 2854 -325 51 -357 C ATOM 105 CG GLU A 16 -41.517 122.757 -11.861 1.00 33.03 C ANISOU 105 CG GLU A 16 4623 4938 2991 -387 39 -432 C ATOM 106 CD GLU A 16 -42.624 123.307 -12.743 1.00 34.24 C ANISOU 106 CD GLU A 16 4747 5184 3080 -426 -19 -435 C ATOM 107 OE1 GLU A 16 -43.129 124.421 -12.497 1.00 34.97 O ANISOU 107 OE1 GLU A 16 4793 5328 3164 -404 -53 -374 O ATOM 108 OE2 GLU A 16 -43.022 122.585 -13.671 1.00 36.07 O ANISOU 108 OE2 GLU A 16 5002 5435 3269 -477 -34 -502 O ATOM 109 N THR A 17 -38.725 125.494 -9.894 1.00 28.73 N ANISOU 109 N THR A 17 4025 4375 2515 -213 98 -267 N ATOM 110 CA THR A 17 -38.038 126.515 -9.144 1.00 27.70 C ANISOU 110 CA THR A 17 3871 4244 2409 -173 105 -214 C ATOM 111 C THR A 17 -39.045 127.441 -8.435 1.00 27.19 C ANISOU 111 C THR A 17 3778 4199 2354 -173 67 -160 C ATOM 112 O THR A 17 -39.956 127.988 -9.062 1.00 27.53 O ANISOU 112 O THR A 17 3812 4290 2358 -191 34 -148 O ATOM 113 CB THR A 17 -37.101 127.294 -10.087 1.00 27.84 C ANISOU 113 CB THR A 17 3893 4304 2382 -166 130 -213 C ATOM 114 OG1 THR A 17 -36.011 126.440 -10.471 1.00 27.65 O ANISOU 114 OG1 THR A 17 3880 4262 2366 -153 176 -268 O ATOM 115 CG2 THR A 17 -36.531 128.533 -9.406 1.00 27.18 C ANISOU 115 CG2 THR A 17 3786 4224 2320 -142 132 -158 C ATOM 116 N LEU A 18 -38.887 127.571 -7.118 1.00 26.72 N ANISOU 116 N LEU A 18 3705 4104 2343 -147 70 -132 N ATOM 117 CA LEU A 18 -39.675 128.507 -6.308 1.00 26.40 C ANISOU 117 CA LEU A 18 3636 4079 2315 -137 46 -87 C ATOM 118 C LEU A 18 -39.030 129.882 -6.394 1.00 25.91 C ANISOU 118 C LEU A 18 3571 4033 2242 -111 45 -53 C ATOM 119 O LEU A 18 -37.830 130.009 -6.153 1.00 25.18 O ANISOU 119 O LEU A 18 3482 3920 2164 -94 69 -54 O ATOM 120 CB LEU A 18 -39.699 128.031 -4.860 1.00 26.10 C ANISOU 120 CB LEU A 18 3598 3998 2323 -126 56 -76 C ATOM 121 CG LEU A 18 -40.323 128.730 -3.686 1.00 25.87 C ANISOU 121 CG LEU A 18 3545 3974 2311 -112 46 -42 C ATOM 122 CD1 LEU A 18 -40.485 127.739 -2.536 1.00 26.07 C ANISOU 122 CD1 LEU A 18 3586 3957 2361 -122 62 -41 C ATOM 123 CD2 LEU A 18 -39.522 129.937 -3.249 1.00 25.58 C ANISOU 123 CD2 LEU A 18 3504 3936 2278 -74 45 -16 C ATOM 124 N SER A 19 -39.829 130.887 -6.755 1.00 25.80 N ANISOU 124 N SER A 19 3547 4051 2204 -107 15 -24 N ATOM 125 CA SER A 19 -39.372 132.268 -6.917 1.00 25.84 C ANISOU 125 CA SER A 19 3563 4058 2197 -88 12 14 C ATOM 126 C SER A 19 -40.173 133.205 -6.052 1.00 25.15 C ANISOU 126 C SER A 19 3458 3965 2133 -58 -13 45 C ATOM 127 O SER A 19 -41.388 133.247 -6.179 1.00 25.35 O ANISOU 127 O SER A 19 3461 4019 2152 -51 -44 47 O ATOM 128 CB SER A 19 -39.585 132.746 -8.351 1.00 26.72 C ANISOU 128 CB SER A 19 3700 4206 2246 -101 -6 27 C ATOM 129 OG SER A 19 -38.599 132.240 -9.202 1.00 28.20 O ANISOU 129 OG SER A 19 3910 4401 2402 -126 30 2 O ATOM 130 N LEU A 20 -39.479 133.990 -5.236 1.00 24.36 N ANISOU 130 N LEU A 20 3363 3832 2059 -39 -1 61 N ATOM 131 CA LEU A 20 -40.098 135.041 -4.440 1.00 24.27 C ANISOU 131 CA LEU A 20 3345 3808 2069 -6 -19 84 C ATOM 132 C LEU A 20 -39.299 136.322 -4.535 1.00 24.05 C ANISOU 132 C LEU A 20 3351 3748 2041 0 -14 110 C ATOM 133 O LEU A 20 -38.096 136.302 -4.773 1.00 23.54 O ANISOU 133 O LEU A 20 3300 3672 1973 -27 12 106 O ATOM 134 CB LEU A 20 -40.186 134.628 -2.966 1.00 23.91 C ANISOU 134 CB LEU A 20 3279 3748 2059 4 -5 67 C ATOM 135 CG LEU A 20 -40.998 133.380 -2.657 1.00 23.93 C ANISOU 135 CG LEU A 20 3256 3770 2066 -13 -1 46 C ATOM 136 CD1 LEU A 20 -40.912 133.041 -1.180 1.00 23.92 C ANISOU 136 CD1 LEU A 20 3251 3750 2086 -7 18 41 C ATOM 137 CD2 LEU A 20 -42.438 133.583 -3.055 1.00 24.54 C ANISOU 137 CD2 LEU A 20 3300 3889 2136 -6 -26 47 C ATOM 138 N THR A 21 -40.003 137.437 -4.390 1.00 24.28 N ANISOU 138 N THR A 21 3391 3761 2075 34 -39 135 N ATOM 139 CA THR A 21 -39.393 138.744 -4.361 1.00 24.77 C ANISOU 139 CA THR A 21 3496 3775 2143 38 -36 160 C ATOM 140 C THR A 21 -39.775 139.465 -3.092 1.00 24.47 C ANISOU 140 C THR A 21 3451 3703 2142 76 -42 150 C ATOM 141 O THR A 21 -40.927 139.402 -2.666 1.00 24.48 O ANISOU 141 O THR A 21 3423 3724 2155 116 -59 142 O ATOM 142 CB THR A 21 -39.921 139.581 -5.534 1.00 25.51 C ANISOU 142 CB THR A 21 3630 3862 2200 54 -67 205 C ATOM 143 OG1 THR A 21 -39.796 138.821 -6.733 1.00 25.82 O ANISOU 143 OG1 THR A 21 3674 3946 2191 22 -65 208 O ATOM 144 CG2 THR A 21 -39.192 140.914 -5.667 1.00 26.25 C ANISOU 144 CG2 THR A 21 3787 3891 2296 44 -58 239 C ATOM 145 N CYS A 22 -38.807 140.168 -2.521 1.00 24.20 N ANISOU 145 N CYS A 22 3443 3624 2127 58 -25 146 N ATOM 146 CA CYS A 22 -39.033 141.051 -1.385 1.00 24.50 C ANISOU 146 CA CYS A 22 3492 3622 2195 89 -29 131 C ATOM 147 C CYS A 22 -38.888 142.488 -1.849 1.00 24.81 C ANISOU 147 C CYS A 22 3595 3594 2239 96 -39 161 C ATOM 148 O CYS A 22 -37.873 142.826 -2.446 1.00 24.57 O ANISOU 148 O CYS A 22 3597 3539 2198 44 -23 179 O ATOM 149 CB CYS A 22 -38.001 140.753 -0.307 1.00 24.86 C ANISOU 149 CB CYS A 22 3525 3664 2256 59 -9 97 C ATOM 150 SG CYS A 22 -38.295 141.625 1.238 1.00 25.51 S ANISOU 150 SG CYS A 22 3620 3710 2361 92 -13 63 S ATOM 151 N THR A 23 -39.894 143.324 -1.580 1.00 25.03 N ANISOU 151 N THR A 23 3639 3590 2283 158 -62 166 N ATOM 152 CA THR A 23 -39.844 144.744 -1.924 1.00 25.69 C ANISOU 152 CA THR A 23 3797 3590 2376 175 -75 197 C ATOM 153 C THR A 23 -39.687 145.553 -0.645 1.00 26.05 C ANISOU 153 C THR A 23 3863 3578 2458 191 -65 155 C ATOM 154 O THR A 23 -40.467 145.397 0.304 1.00 26.11 O ANISOU 154 O THR A 23 3832 3608 2481 241 -66 116 O ATOM 155 CB THR A 23 -41.103 145.184 -2.701 1.00 26.14 C ANISOU 155 CB THR A 23 3866 3642 2423 250 -117 235 C ATOM 156 OG1 THR A 23 -41.283 144.322 -3.833 1.00 25.77 O ANISOU 156 OG1 THR A 23 3797 3663 2333 231 -131 263 O ATOM 157 CG2 THR A 23 -40.998 146.633 -3.191 1.00 27.01 C ANISOU 157 CG2 THR A 23 4073 3650 2539 271 -135 280 C ATOM 158 N VAL A 24 -38.658 146.389 -0.636 1.00 26.36 N ANISOU 158 N VAL A 24 3961 3547 2508 138 -51 159 N ATOM 159 CA VAL A 24 -38.350 147.249 0.482 1.00 27.16 C ANISOU 159 CA VAL A 24 4094 3585 2641 137 -44 114 C ATOM 160 C VAL A 24 -38.960 148.614 0.195 1.00 28.11 C ANISOU 160 C VAL A 24 4296 3602 2783 191 -63 138 C ATOM 161 O VAL A 24 -38.772 149.158 -0.894 1.00 28.65 O ANISOU 161 O VAL A 24 4427 3619 2840 173 -71 198 O ATOM 162 CB VAL A 24 -36.832 147.359 0.697 1.00 26.97 C ANISOU 162 CB VAL A 24 4081 3545 2621 39 -21 95 C ATOM 163 CG1 VAL A 24 -36.512 148.259 1.885 1.00 27.49 C ANISOU 163 CG1 VAL A 24 4181 3548 2715 30 -19 39 C ATOM 164 CG2 VAL A 24 -36.237 145.976 0.884 1.00 26.25 C ANISOU 164 CG2 VAL A 24 3910 3553 2512 3 -9 76 C ATOM 165 N SER A 25 -39.684 149.151 1.174 1.00 28.47 N ANISOU 165 N SER A 25 4346 3615 2855 260 -69 92 N ATOM 166 CA SER A 25 -40.279 150.485 1.089 1.00 29.76 C ANISOU 166 CA SER A 25 4590 3668 3049 328 -87 101 C ATOM 167 C SER A 25 -39.898 151.314 2.304 1.00 30.39 C ANISOU 167 C SER A 25 4714 3674 3159 319 -70 31 C ATOM 168 O SER A 25 -39.690 150.773 3.397 1.00 30.15 O ANISOU 168 O SER A 25 4631 3703 3121 299 -52 -32 O ATOM 169 CB SER A 25 -41.799 150.393 0.976 1.00 29.89 C ANISOU 169 CB SER A 25 4564 3720 3073 449 -114 106 C ATOM 170 OG SER A 25 -42.335 149.619 2.033 1.00 29.44 O ANISOU 170 OG SER A 25 4418 3752 3015 475 -95 42 O ATOM 171 N GLY A 26 -39.812 152.626 2.097 1.00 31.57 N ANISOU 171 N GLY A 26 4967 3689 3338 331 -79 44 N ATOM 172 CA GLY A 26 -39.400 153.576 3.125 1.00 32.59 C ANISOU 172 CA GLY A 26 5159 3726 3498 313 -65 -26 C ATOM 173 C GLY A 26 -37.917 153.555 3.454 1.00 32.98 C ANISOU 173 C GLY A 26 5219 3770 3541 176 -43 -53 C ATOM 174 O GLY A 26 -37.494 154.142 4.451 1.00 33.84 O ANISOU 174 O GLY A 26 5362 3830 3668 146 -35 -126 O ATOM 175 N GLY A 27 -37.126 152.882 2.625 1.00 32.72 N ANISOU 175 N GLY A 27 5154 3796 3484 93 -36 -1 N ATOM 176 CA GLY A 27 -35.702 152.686 2.872 1.00 32.84 C ANISOU 176 CA GLY A 27 5148 3835 3494 -34 -16 -28 C ATOM 177 C GLY A 27 -35.068 152.128 1.610 1.00 32.49 C ANISOU 177 C GLY A 27 5082 3837 3426 -102 -2 43 C ATOM 178 O GLY A 27 -35.770 151.593 0.756 1.00 31.84 O ANISOU 178 O GLY A 27 4982 3798 3320 -47 -12 101 O ATOM 179 N SER A 28 -33.752 152.288 1.477 1.00 32.88 N ANISOU 179 N SER A 28 5131 3881 3480 -222 21 35 N ATOM 180 CA SER A 28 -33.014 151.784 0.314 1.00 32.92 C ANISOU 180 CA SER A 28 5110 3936 3460 -297 47 91 C ATOM 181 C SER A 28 -32.408 150.429 0.638 1.00 31.92 C ANISOU 181 C SER A 28 4862 3950 3318 -319 52 55 C ATOM 182 O SER A 28 -32.416 149.999 1.787 1.00 31.68 O ANISOU 182 O SER A 28 4777 3965 3293 -292 34 -7 O ATOM 183 CB SER A 28 -31.894 152.741 -0.069 1.00 33.96 C ANISOU 183 CB SER A 28 5305 3987 3610 -424 80 100 C ATOM 184 OG SER A 28 -30.930 152.778 0.961 1.00 34.62 O ANISOU 184 OG SER A 28 5338 4095 3719 -498 83 17 O ATOM 185 N ILE A 29 -31.854 149.790 -0.383 1.00 31.45 N ANISOU 185 N ILE A 29 4765 3952 3233 -367 78 96 N ATOM 186 CA ILE A 29 -31.107 148.548 -0.224 1.00 30.90 C ANISOU 186 CA ILE A 29 4585 4002 3154 -391 87 63 C ATOM 187 C ILE A 29 -29.609 148.746 -0.444 1.00 31.80 C ANISOU 187 C ILE A 29 4664 4135 3283 -512 123 42 C ATOM 188 O ILE A 29 -28.886 147.779 -0.751 1.00 31.42 O ANISOU 188 O ILE A 29 4528 4184 3225 -537 142 30 O ATOM 189 CB ILE A 29 -31.654 147.433 -1.137 1.00 30.19 C ANISOU 189 CB ILE A 29 4458 3986 3025 -340 91 107 C ATOM 190 CG1 ILE A 29 -31.508 147.788 -2.631 1.00 30.54 C ANISOU 190 CG1 ILE A 29 4558 4007 3038 -387 124 175 C ATOM 191 CG2 ILE A 29 -33.113 147.152 -0.793 1.00 29.58 C ANISOU 191 CG2 ILE A 29 4392 3907 2939 -229 55 115 C ATOM 192 CD1 ILE A 29 -31.994 146.680 -3.539 1.00 30.00 C ANISOU 192 CD1 ILE A 29 4455 4017 2925 -344 125 206 C ATOM 193 N SER A 30 -29.145 149.984 -0.242 1.00 32.81 N ANISOU 193 N SER A 30 4855 4172 3438 -587 134 30 N ATOM 194 CA SER A 30 -27.754 150.371 -0.486 1.00 33.85 C ANISOU 194 CA SER A 30 4958 4313 3589 -720 174 8 C ATOM 195 C SER A 30 -26.861 150.200 0.756 1.00 33.67 C ANISOU 195 C SER A 30 4848 4346 3599 -759 149 -83 C ATOM 196 O SER A 30 -25.703 150.625 0.755 1.00 34.18 O ANISOU 196 O SER A 30 4877 4420 3689 -874 173 -118 O ATOM 197 CB SER A 30 -27.703 151.826 -0.963 1.00 35.30 C ANISOU 197 CB SER A 30 5267 4360 3786 -797 200 46 C ATOM 198 OG SER A 30 -28.089 152.717 0.073 1.00 35.97 O ANISOU 198 OG SER A 30 5416 4348 3904 -776 165 3 O ATOM 199 N SER A 31 -27.410 149.606 1.816 1.00 32.57 N ANISOU 199 N SER A 31 4675 4245 3455 -667 99 -122 N ATOM 200 CA SER A 31 -26.622 149.121 2.952 1.00 32.28 C ANISOU 200 CA SER A 31 4546 4289 3431 -680 64 -200 C ATOM 201 C SER A 31 -27.121 147.763 3.409 1.00 30.73 C ANISOU 201 C SER A 31 4287 4182 3206 -573 32 -201 C ATOM 202 O SER A 31 -28.162 147.278 2.957 1.00 30.38 O ANISOU 202 O SER A 31 4273 4132 3138 -493 37 -151 O ATOM 203 CB SER A 31 -26.720 150.096 4.132 1.00 32.78 C ANISOU 203 CB SER A 31 4664 4281 3509 -696 30 -261 C ATOM 204 OG SER A 31 -26.172 151.345 3.807 1.00 34.20 O ANISOU 204 OG SER A 31 4905 4368 3720 -807 58 -268 O ATOM 205 N TYR A 32 -26.357 147.154 4.312 1.00 29.95 N ANISOU 205 N TYR A 32 4103 4166 3110 -575 -4 -257 N ATOM 206 CA TYR A 32 -26.806 145.998 5.093 1.00 28.75 C ANISOU 206 CA TYR A 32 3912 4081 2929 -478 -44 -265 C ATOM 207 C TYR A 32 -26.912 144.705 4.282 1.00 27.40 C ANISOU 207 C TYR A 32 3691 3974 2747 -427 -26 -221 C ATOM 208 O TYR A 32 -26.612 144.683 3.078 1.00 27.38 O ANISOU 208 O TYR A 32 3676 3973 2753 -465 20 -189 O ATOM 209 CB TYR A 32 -28.141 146.319 5.789 1.00 28.48 C ANISOU 209 CB TYR A 32 3962 3989 2871 -405 -60 -260 C ATOM 210 CG TYR A 32 -28.185 147.705 6.401 1.00 29.52 C ANISOU 210 CG TYR A 32 4166 4035 3016 -449 -68 -303 C ATOM 211 CD1 TYR A 32 -27.170 148.134 7.249 1.00 30.53 C ANISOU 211 CD1 TYR A 32 4264 4183 3154 -517 -99 -374 C ATOM 212 CD2 TYR A 32 -29.214 148.598 6.105 1.00 29.85 C ANISOU 212 CD2 TYR A 32 4304 3974 3063 -421 -48 -278 C ATOM 213 CE1 TYR A 32 -27.193 149.399 7.823 1.00 31.60 C ANISOU 213 CE1 TYR A 32 4471 4232 3302 -564 -106 -423 C ATOM 214 CE2 TYR A 32 -29.237 149.875 6.662 1.00 31.17 C ANISOU 214 CE2 TYR A 32 4546 4049 3248 -457 -53 -323 C ATOM 215 CZ TYR A 32 -28.225 150.266 7.527 1.00 31.90 C ANISOU 215 CZ TYR A 32 4615 4158 3349 -533 -80 -399 C ATOM 216 OH TYR A 32 -28.225 151.525 8.095 1.00 33.34 O ANISOU 216 OH TYR A 32 4877 4242 3548 -575 -85 -454 O ATOM 217 N PHE A 33 -27.331 143.643 4.965 1.00 26.05 N ANISOU 217 N PHE A 33 3497 3851 2551 -346 -59 -222 N ATOM 218 CA PHE A 33 -27.632 142.352 4.353 1.00 25.09 C ANISOU 218 CA PHE A 33 3344 3773 2417 -288 -46 -185 C ATOM 219 C PHE A 33 -29.133 142.163 4.216 1.00 24.13 C ANISOU 219 C PHE A 33 3288 3611 2269 -226 -38 -143 C ATOM 220 O PHE A 33 -29.918 142.751 4.943 1.00 23.68 O ANISOU 220 O PHE A 33 3284 3514 2199 -204 -51 -150 O ATOM 221 CB PHE A 33 -27.094 141.198 5.189 1.00 24.98 C ANISOU 221 CB PHE A 33 3267 3830 2394 -241 -89 -208 C ATOM 222 CG PHE A 33 -25.605 141.143 5.284 1.00 25.88 C ANISOU 222 CG PHE A 33 3290 4004 2537 -284 -106 -253 C ATOM 223 CD1 PHE A 33 -24.927 141.935 6.218 1.00 26.53 C ANISOU 223 CD1 PHE A 33 3356 4097 2628 -331 -145 -305 C ATOM 224 CD2 PHE A 33 -24.872 140.257 4.498 1.00 25.96 C ANISOU 224 CD2 PHE A 33 3226 4070 2569 -273 -86 -251 C ATOM 225 CE1 PHE A 33 -23.550 141.860 6.341 1.00 27.37 C ANISOU 225 CE1 PHE A 33 3362 4274 2765 -371 -168 -352 C ATOM 226 CE2 PHE A 33 -23.490 140.181 4.624 1.00 26.69 C ANISOU 226 CE2 PHE A 33 3217 4232 2694 -305 -103 -300 C ATOM 227 CZ PHE A 33 -22.834 140.988 5.538 1.00 27.58 C ANISOU 227 CZ PHE A 33 3304 4360 2816 -355 -145 -349 C ATOM 228 N TRP A 34 -29.505 141.318 3.261 1.00 23.79 N ANISOU 228 N TRP A 34 3235 3587 2218 -199 -14 -106 N ATOM 229 CA TRP A 34 -30.895 141.107 2.874 1.00 23.17 C ANISOU 229 CA TRP A 34 3204 3482 2119 -151 -4 -67 C ATOM 230 C TRP A 34 -31.110 139.617 2.783 1.00 22.63 C ANISOU 230 C TRP A 34 3102 3460 2037 -106 -6 -56 C ATOM 231 O TRP A 34 -30.424 138.940 2.025 1.00 23.13 O ANISOU 231 O TRP A 34 3125 3555 2107 -118 10 -56 O ATOM 232 CB TRP A 34 -31.153 141.854 1.571 1.00 23.25 C ANISOU 232 CB TRP A 34 3253 3453 2130 -183 28 -30 C ATOM 233 CG TRP A 34 -30.810 143.296 1.776 1.00 23.88 C ANISOU 233 CG TRP A 34 3374 3472 2227 -233 30 -42 C ATOM 234 CD1 TRP A 34 -29.625 143.921 1.471 1.00 24.71 C ANISOU 234 CD1 TRP A 34 3465 3571 2353 -314 49 -57 C ATOM 235 CD2 TRP A 34 -31.622 144.276 2.419 1.00 24.12 C ANISOU 235 CD2 TRP A 34 3467 3437 2261 -209 15 -47 C ATOM 236 NE1 TRP A 34 -29.671 145.239 1.864 1.00 25.17 N ANISOU 236 NE1 TRP A 34 3582 3554 2426 -348 45 -68 N ATOM 237 CE2 TRP A 34 -30.885 145.484 2.444 1.00 24.83 C ANISOU 237 CE2 TRP A 34 3591 3471 2374 -278 23 -64 C ATOM 238 CE3 TRP A 34 -32.914 144.261 2.961 1.00 23.89 C ANISOU 238 CE3 TRP A 34 3466 3391 2219 -136 0 -43 C ATOM 239 CZ2 TRP A 34 -31.394 146.656 2.992 1.00 25.51 C ANISOU 239 CZ2 TRP A 34 3748 3473 2472 -271 13 -78 C ATOM 240 CZ3 TRP A 34 -33.421 145.432 3.503 1.00 24.41 C ANISOU 240 CZ3 TRP A 34 3592 3386 2297 -122 -8 -60 C ATOM 241 CH2 TRP A 34 -32.661 146.614 3.513 1.00 25.17 C ANISOU 241 CH2 TRP A 34 3731 3416 2418 -185 -3 -78 C ATOM 242 N SER A 35 -32.044 139.110 3.578 1.00 22.23 N ANISOU 242 N SER A 35 3070 3410 1967 -58 -23 -52 N ATOM 243 CA SER A 35 -32.055 137.702 3.939 1.00 21.83 C ANISOU 243 CA SER A 35 2997 3393 1905 -22 -33 -49 C ATOM 244 C SER A 35 -33.399 137.031 3.700 1.00 21.26 C ANISOU 244 C SER A 35 2948 3316 1815 7 -20 -21 C ATOM 245 O SER A 35 -34.447 137.681 3.685 1.00 20.63 O ANISOU 245 O SER A 35 2895 3217 1728 15 -13 -12 O ATOM 246 CB SER A 35 -31.668 137.549 5.415 1.00 22.29 C ANISOU 246 CB SER A 35 3053 3468 1949 -4 -70 -71 C ATOM 247 OG SER A 35 -31.386 136.189 5.738 1.00 22.59 O ANISOU 247 OG SER A 35 3074 3531 1978 30 -86 -63 O ATOM 248 N TRP A 36 -33.326 135.713 3.530 1.00 21.31 N ANISOU 248 N TRP A 36 2940 3339 1818 25 -19 -14 N ATOM 249 CA TRP A 36 -34.479 134.828 3.444 1.00 20.99 C ANISOU 249 CA TRP A 36 2917 3296 1762 41 -8 5 C ATOM 250 C TRP A 36 -34.392 133.758 4.538 1.00 21.20 C ANISOU 250 C TRP A 36 2955 3326 1774 65 -23 9 C ATOM 251 O TRP A 36 -33.323 133.189 4.780 1.00 21.42 O ANISOU 251 O TRP A 36 2969 3359 1811 80 -42 1 O ATOM 252 CB TRP A 36 -34.538 134.186 2.064 1.00 20.94 C ANISOU 252 CB TRP A 36 2900 3293 1762 30 11 11 C ATOM 253 CG TRP A 36 -34.919 135.173 0.979 1.00 21.06 C ANISOU 253 CG TRP A 36 2920 3305 1775 9 24 20 C ATOM 254 CD1 TRP A 36 -34.073 135.830 0.139 1.00 21.09 C ANISOU 254 CD1 TRP A 36 2918 3311 1785 -17 35 18 C ATOM 255 CD2 TRP A 36 -36.232 135.630 0.658 1.00 21.16 C ANISOU 255 CD2 TRP A 36 2948 3315 1776 15 23 37 C ATOM 256 NE1 TRP A 36 -34.774 136.662 -0.689 1.00 21.24 N ANISOU 256 NE1 TRP A 36 2961 3319 1790 -28 40 40 N ATOM 257 CE2 TRP A 36 -36.105 136.542 -0.419 1.00 21.31 C ANISOU 257 CE2 TRP A 36 2980 3327 1790 -2 28 51 C ATOM 258 CE3 TRP A 36 -37.510 135.323 1.135 1.00 21.44 C ANISOU 258 CE3 TRP A 36 2985 3359 1804 31 21 42 C ATOM 259 CZ2 TRP A 36 -37.203 137.182 -1.000 1.00 21.51 C ANISOU 259 CZ2 TRP A 36 3021 3348 1804 10 18 72 C ATOM 260 CZ3 TRP A 36 -38.613 135.964 0.554 1.00 21.73 C ANISOU 260 CZ3 TRP A 36 3020 3400 1835 41 16 54 C ATOM 261 CH2 TRP A 36 -38.447 136.882 -0.502 1.00 21.70 C ANISOU 261 CH2 TRP A 36 3033 3386 1828 37 8 70 C ATOM 262 N ILE A 37 -35.513 133.535 5.218 1.00 21.29 N ANISOU 262 N ILE A 37 2992 3335 1762 69 -13 22 N ATOM 263 CA ILE A 37 -35.649 132.532 6.276 1.00 21.98 C ANISOU 263 CA ILE A 37 3109 3420 1824 83 -20 37 C ATOM 264 C ILE A 37 -36.972 131.833 5.981 1.00 22.01 C ANISOU 264 C ILE A 37 3124 3419 1821 65 12 53 C ATOM 265 O ILE A 37 -37.918 132.485 5.547 1.00 22.02 O ANISOU 265 O ILE A 37 3107 3433 1826 53 31 47 O ATOM 266 CB ILE A 37 -35.698 133.195 7.687 1.00 22.22 C ANISOU 266 CB ILE A 37 3161 3464 1819 91 -32 30 C ATOM 267 CG1 ILE A 37 -34.414 133.991 7.961 1.00 22.43 C ANISOU 267 CG1 ILE A 37 3170 3500 1854 97 -69 4 C ATOM 268 CG2 ILE A 37 -35.941 132.173 8.792 1.00 22.55 C ANISOU 268 CG2 ILE A 37 3247 3505 1818 100 -34 56 C ATOM 269 CD1 ILE A 37 -34.540 135.467 7.668 1.00 22.39 C ANISOU 269 CD1 ILE A 37 3153 3490 1864 79 -61 -22 C ATOM 270 N ARG A 38 -37.046 130.527 6.212 1.00 22.30 N ANISOU 270 N ARG A 38 3189 3435 1850 63 17 73 N ATOM 271 CA ARG A 38 -38.307 129.812 6.051 1.00 22.42 C ANISOU 271 CA ARG A 38 3214 3446 1858 30 50 85 C ATOM 272 C ARG A 38 -38.710 129.050 7.301 1.00 22.98 C ANISOU 272 C ARG A 38 3335 3505 1891 19 64 112 C ATOM 273 O ARG A 38 -37.906 128.849 8.228 1.00 23.13 O ANISOU 273 O ARG A 38 3390 3512 1885 47 38 128 O ATOM 274 CB ARG A 38 -38.259 128.870 4.846 1.00 22.51 C ANISOU 274 CB ARG A 38 3223 3432 1897 15 55 79 C ATOM 275 CG ARG A 38 -37.190 127.803 4.922 1.00 22.78 C ANISOU 275 CG ARG A 38 3291 3423 1941 42 37 87 C ATOM 276 CD ARG A 38 -37.259 126.888 3.722 1.00 22.89 C ANISOU 276 CD ARG A 38 3308 3409 1981 26 49 70 C ATOM 277 NE ARG A 38 -36.419 125.701 3.905 1.00 23.33 N ANISOU 277 NE ARG A 38 3407 3409 2049 58 36 76 N ATOM 278 CZ ARG A 38 -36.312 124.713 3.021 1.00 23.78 C ANISOU 278 CZ ARG A 38 3482 3425 2130 54 46 56 C ATOM 279 NH1 ARG A 38 -36.984 124.752 1.875 1.00 23.58 N ANISOU 279 NH1 ARG A 38 3435 3417 2109 12 67 27 N ATOM 280 NH2 ARG A 38 -35.526 123.673 3.280 1.00 24.46 N ANISOU 280 NH2 ARG A 38 3610 3451 2231 98 32 61 N ATOM 281 N GLN A 39 -39.978 128.652 7.321 1.00 23.30 N ANISOU 281 N GLN A 39 3375 3554 1924 -24 103 118 N ATOM 282 CA GLN A 39 -40.570 127.962 8.463 1.00 23.94 C ANISOU 282 CA GLN A 39 3504 3629 1963 -52 133 147 C ATOM 283 C GLN A 39 -41.639 126.995 7.951 1.00 24.74 C ANISOU 283 C GLN A 39 3605 3718 2079 -114 172 152 C ATOM 284 O GLN A 39 -42.726 127.440 7.566 1.00 24.64 O ANISOU 284 O GLN A 39 3534 3751 2078 -144 199 128 O ATOM 285 CB GLN A 39 -41.180 128.982 9.429 1.00 23.92 C ANISOU 285 CB GLN A 39 3487 3679 1924 -50 155 136 C ATOM 286 CG GLN A 39 -41.651 128.388 10.756 1.00 24.35 C ANISOU 286 CG GLN A 39 3598 3736 1916 -80 191 167 C ATOM 287 CD GLN A 39 -42.093 129.424 11.777 1.00 24.45 C ANISOU 287 CD GLN A 39 3601 3805 1884 -70 216 146 C ATOM 288 OE1 GLN A 39 -41.919 129.227 12.991 1.00 25.13 O ANISOU 288 OE1 GLN A 39 3748 3897 1903 -72 224 168 O ATOM 289 NE2 GLN A 39 -42.684 130.502 11.316 1.00 23.88 N ANISOU 289 NE2 GLN A 39 3461 3771 1842 -56 227 103 N ATOM 290 N PRO A 40 -41.327 125.677 7.900 1.00 25.46 N ANISOU 290 N PRO A 40 3757 3744 2174 -132 171 177 N ATOM 291 CA PRO A 40 -42.367 124.716 7.527 1.00 26.21 C ANISOU 291 CA PRO A 40 3859 3820 2281 -207 211 178 C ATOM 292 C PRO A 40 -43.548 124.773 8.520 1.00 26.99 C ANISOU 292 C PRO A 40 3955 3960 2340 -264 268 193 C ATOM 293 O PRO A 40 -43.323 125.089 9.694 1.00 27.73 O ANISOU 293 O PRO A 40 4084 4066 2384 -244 274 218 O ATOM 294 CB PRO A 40 -41.658 123.358 7.590 1.00 26.63 C ANISOU 294 CB PRO A 40 4001 3778 2338 -204 198 210 C ATOM 295 CG PRO A 40 -40.189 123.654 7.613 1.00 26.26 C ANISOU 295 CG PRO A 40 3966 3713 2297 -116 143 212 C ATOM 296 CD PRO A 40 -40.052 125.011 8.235 1.00 25.76 C ANISOU 296 CD PRO A 40 3859 3722 2207 -84 132 205 C ATOM 297 N PRO A 41 -44.787 124.494 8.057 1.00 27.53 N ANISOU 297 N PRO A 41 3976 4059 2428 -337 308 171 N ATOM 298 CA PRO A 41 -45.947 124.662 8.954 1.00 28.37 C ANISOU 298 CA PRO A 41 4056 4223 2501 -393 371 174 C ATOM 299 C PRO A 41 -45.817 123.863 10.254 1.00 29.31 C ANISOU 299 C PRO A 41 4277 4297 2561 -427 408 230 C ATOM 300 O PRO A 41 -45.536 122.670 10.223 1.00 30.04 O ANISOU 300 O PRO A 41 4453 4307 2655 -462 408 266 O ATOM 301 CB PRO A 41 -47.129 124.180 8.113 1.00 28.70 C ANISOU 301 CB PRO A 41 4032 4291 2580 -475 401 141 C ATOM 302 CG PRO A 41 -46.686 124.352 6.698 1.00 28.15 C ANISOU 302 CG PRO A 41 3927 4210 2557 -438 343 108 C ATOM 303 CD PRO A 41 -45.204 124.075 6.705 1.00 27.59 C ANISOU 303 CD PRO A 41 3940 4060 2482 -374 299 135 C ATOM 304 N GLY A 42 -45.950 124.552 11.384 1.00 29.82 N ANISOU 304 N GLY A 42 4347 4414 2570 -410 434 239 N ATOM 305 CA GLY A 42 -45.795 123.940 12.701 1.00 30.90 C ANISOU 305 CA GLY A 42 4588 4521 2631 -436 465 298 C ATOM 306 C GLY A 42 -44.383 123.568 13.145 1.00 31.10 C ANISOU 306 C GLY A 42 4718 4472 2627 -368 400 346 C ATOM 307 O GLY A 42 -44.224 122.896 14.161 1.00 31.79 O ANISOU 307 O GLY A 42 4907 4522 2648 -388 416 405 O ATOM 308 N LYS A 43 -43.359 124.027 12.423 1.00 30.77 N ANISOU 308 N LYS A 43 4647 4414 2629 -287 328 322 N ATOM 309 CA LYS A 43 -41.965 123.650 12.700 1.00 31.05 C ANISOU 309 CA LYS A 43 4757 4388 2651 -216 259 358 C ATOM 310 C LYS A 43 -41.125 124.908 12.962 1.00 29.79 C ANISOU 310 C LYS A 43 4556 4283 2481 -138 208 328 C ATOM 311 O LYS A 43 -41.682 125.989 13.093 1.00 29.56 O ANISOU 311 O LYS A 43 4463 4324 2443 -142 232 288 O ATOM 312 CB LYS A 43 -41.425 122.808 11.536 1.00 31.59 C ANISOU 312 CB LYS A 43 4834 4380 2790 -201 225 353 C ATOM 313 CG LYS A 43 -42.037 121.407 11.456 1.00 33.05 C ANISOU 313 CG LYS A 43 5093 4485 2980 -276 267 388 C ATOM 314 CD LYS A 43 -41.383 120.454 12.458 1.00 34.84 C ANISOU 314 CD LYS A 43 5454 4629 3156 -253 246 464 C ATOM 315 CE LYS A 43 -42.066 119.087 12.528 1.00 36.36 C ANISOU 315 CE LYS A 43 5740 4728 3346 -341 296 508 C ATOM 316 NZ LYS A 43 -42.913 118.906 13.746 1.00 37.67 N ANISOU 316 NZ LYS A 43 5969 4913 3430 -420 362 561 N ATOM 317 N GLY A 44 -39.800 124.763 13.057 1.00 29.02 N ANISOU 317 N GLY A 44 4492 4150 2384 -67 137 343 N ATOM 318 CA GLY A 44 -38.903 125.876 13.393 1.00 28.04 C ANISOU 318 CA GLY A 44 4332 4074 2246 -5 84 314 C ATOM 319 C GLY A 44 -38.399 126.692 12.221 1.00 26.48 C ANISOU 319 C GLY A 44 4044 3894 2123 26 56 259 C ATOM 320 O GLY A 44 -38.633 126.351 11.056 1.00 26.41 O ANISOU 320 O GLY A 44 4000 3860 2173 10 70 244 O ATOM 321 N LEU A 45 -37.701 127.777 12.542 1.00 25.42 N ANISOU 321 N LEU A 45 3878 3802 1979 64 19 229 N ATOM 322 CA LEU A 45 -37.117 128.672 11.530 1.00 24.07 C ANISOU 322 CA LEU A 45 3630 3647 1869 87 -6 182 C ATOM 323 C LEU A 45 -35.870 128.031 10.940 1.00 23.82 C ANISOU 323 C LEU A 45 3592 3580 1878 130 -55 186 C ATOM 324 O LEU A 45 -35.158 127.319 11.635 1.00 23.92 O ANISOU 324 O LEU A 45 3653 3572 1864 166 -96 217 O ATOM 325 CB LEU A 45 -36.758 130.030 12.152 1.00 23.79 C ANISOU 325 CB LEU A 45 3570 3658 1809 102 -27 145 C ATOM 326 CG LEU A 45 -37.885 130.814 12.832 1.00 23.76 C ANISOU 326 CG LEU A 45 3571 3693 1765 75 21 127 C ATOM 327 CD1 LEU A 45 -37.326 131.996 13.604 1.00 23.72 C ANISOU 327 CD1 LEU A 45 3564 3721 1729 96 -9 88 C ATOM 328 CD2 LEU A 45 -38.914 131.292 11.802 1.00 23.14 C ANISOU 328 CD2 LEU A 45 3434 3621 1737 52 67 103 C ATOM 329 N GLU A 46 -35.645 128.256 9.647 1.00 23.36 N ANISOU 329 N GLU A 46 3476 3518 1881 129 -51 156 N ATOM 330 CA GLU A 46 -34.466 127.769 8.940 1.00 23.57 C ANISOU 330 CA GLU A 46 3479 3524 1952 170 -85 145 C ATOM 331 C GLU A 46 -33.926 128.899 8.076 1.00 22.90 C ANISOU 331 C GLU A 46 3320 3475 1906 167 -89 101 C ATOM 332 O GLU A 46 -34.626 129.395 7.199 1.00 22.17 O ANISOU 332 O GLU A 46 3202 3391 1832 133 -54 85 O ATOM 333 CB GLU A 46 -34.789 126.555 8.058 1.00 23.86 C ANISOU 333 CB GLU A 46 3539 3507 2021 161 -61 155 C ATOM 334 CG GLU A 46 -33.538 125.942 7.447 1.00 24.40 C ANISOU 334 CG GLU A 46 3588 3551 2133 216 -92 139 C ATOM 335 CD GLU A 46 -33.773 124.728 6.556 1.00 25.00 C ANISOU 335 CD GLU A 46 3693 3565 2241 213 -68 137 C ATOM 336 OE1 GLU A 46 -34.759 124.694 5.783 1.00 24.45 O ANISOU 336 OE1 GLU A 46 3620 3491 2178 157 -25 124 O ATOM 337 OE2 GLU A 46 -32.926 123.813 6.608 1.00 25.65 O ANISOU 337 OE2 GLU A 46 3800 3603 2344 271 -96 142 O ATOM 338 N TRP A 47 -32.685 129.296 8.337 1.00 23.16 N ANISOU 338 N TRP A 47 3320 3532 1948 200 -134 82 N ATOM 339 CA TRP A 47 -32.019 130.339 7.566 1.00 22.89 C ANISOU 339 CA TRP A 47 3219 3529 1949 187 -134 42 C ATOM 340 C TRP A 47 -31.689 129.790 6.179 1.00 22.77 C ANISOU 340 C TRP A 47 3171 3500 1980 190 -110 27 C ATOM 341 O TRP A 47 -31.173 128.690 6.065 1.00 23.54 O ANISOU 341 O TRP A 47 3276 3574 2093 229 -123 32 O ATOM 342 CB TRP A 47 -30.757 130.782 8.295 1.00 23.55 C ANISOU 342 CB TRP A 47 3269 3648 2031 213 -189 21 C ATOM 343 CG TRP A 47 -30.059 131.944 7.682 1.00 23.52 C ANISOU 343 CG TRP A 47 3200 3676 2060 183 -185 -21 C ATOM 344 CD1 TRP A 47 -30.462 133.249 7.708 1.00 23.38 C ANISOU 344 CD1 TRP A 47 3183 3664 2036 139 -169 -38 C ATOM 345 CD2 TRP A 47 -28.825 131.916 6.975 1.00 23.70 C ANISOU 345 CD2 TRP A 47 3153 3724 2129 192 -195 -51 C ATOM 346 NE1 TRP A 47 -29.552 134.034 7.058 1.00 23.71 N ANISOU 346 NE1 TRP A 47 3168 3727 2115 111 -167 -71 N ATOM 347 CE2 TRP A 47 -28.534 133.242 6.597 1.00 23.67 C ANISOU 347 CE2 TRP A 47 3112 3741 2140 138 -180 -81 C ATOM 348 CE3 TRP A 47 -27.933 130.895 6.612 1.00 24.21 C ANISOU 348 CE3 TRP A 47 3180 3794 2224 242 -210 -59 C ATOM 349 CZ2 TRP A 47 -27.393 133.579 5.879 1.00 24.00 C ANISOU 349 CZ2 TRP A 47 3079 3817 2224 120 -174 -116 C ATOM 350 CZ3 TRP A 47 -26.789 131.233 5.891 1.00 24.43 C ANISOU 350 CZ3 TRP A 47 3123 3864 2297 234 -205 -102 C ATOM 351 CH2 TRP A 47 -26.532 132.567 5.534 1.00 24.33 C ANISOU 351 CH2 TRP A 47 3072 3878 2294 167 -184 -128 C ATOM 352 N ILE A 48 -32.027 130.542 5.139 1.00 21.97 N ANISOU 352 N ILE A 48 3043 3410 1895 151 -76 10 N ATOM 353 CA ILE A 48 -31.745 130.133 3.754 1.00 21.74 C ANISOU 353 CA ILE A 48 2989 3377 1895 146 -48 -8 C ATOM 354 C ILE A 48 -30.475 130.809 3.254 1.00 21.66 C ANISOU 354 C ILE A 48 2915 3404 1912 143 -51 -40 C ATOM 355 O ILE A 48 -29.606 130.155 2.700 1.00 21.92 O ANISOU 355 O ILE A 48 2915 3444 1971 169 -46 -63 O ATOM 356 CB ILE A 48 -32.924 130.453 2.816 1.00 21.10 C ANISOU 356 CB ILE A 48 2922 3291 1804 104 -12 -2 C ATOM 357 CG1 ILE A 48 -34.180 129.707 3.271 1.00 20.95 C ANISOU 357 CG1 ILE A 48 2949 3245 1765 97 -4 23 C ATOM 358 CG2 ILE A 48 -32.582 130.081 1.365 1.00 21.25 C ANISOU 358 CG2 ILE A 48 2920 3314 1839 94 16 -24 C ATOM 359 CD1 ILE A 48 -35.479 130.262 2.721 1.00 20.64 C ANISOU 359 CD1 ILE A 48 2911 3217 1713 60 19 28 C ATOM 360 N GLY A 49 -30.363 132.113 3.480 1.00 21.77 N ANISOU 360 N GLY A 49 2912 3438 1921 109 -54 -47 N ATOM 361 CA GLY A 49 -29.181 132.862 3.056 1.00 22.01 C ANISOU 361 CA GLY A 49 2883 3503 1976 87 -51 -78 C ATOM 362 C GLY A 49 -29.376 134.357 3.169 1.00 21.97 C ANISOU 362 C GLY A 49 2886 3497 1965 36 -46 -79 C ATOM 363 O GLY A 49 -30.444 134.834 3.561 1.00 21.72 O ANISOU 363 O GLY A 49 2902 3440 1910 30 -46 -59 O ATOM 364 N TYR A 50 -28.324 135.098 2.859 1.00 22.39 N ANISOU 364 N TYR A 50 2890 3577 2041 -1 -39 -106 N ATOM 365 CA TYR A 50 -28.441 136.540 2.695 1.00 22.53 C ANISOU 365 CA TYR A 50 2925 3578 2058 -60 -25 -106 C ATOM 366 C TYR A 50 -27.512 137.074 1.619 1.00 22.96 C ANISOU 366 C TYR A 50 2936 3654 2133 -117 15 -122 C ATOM 367 O TYR A 50 -26.596 136.390 1.177 1.00 22.92 O ANISOU 367 O TYR A 50 2869 3692 2148 -108 29 -146 O ATOM 368 CB TYR A 50 -28.300 137.316 4.026 1.00 22.84 C ANISOU 368 CB TYR A 50 2973 3614 2092 -67 -67 -124 C ATOM 369 CG TYR A 50 -27.024 137.197 4.845 1.00 23.55 C ANISOU 369 CG TYR A 50 3000 3751 2198 -65 -110 -164 C ATOM 370 CD1 TYR A 50 -25.886 136.512 4.394 1.00 24.00 C ANISOU 370 CD1 TYR A 50 2977 3856 2285 -54 -110 -187 C ATOM 371 CD2 TYR A 50 -26.953 137.806 6.100 1.00 23.87 C ANISOU 371 CD2 TYR A 50 3055 3792 2221 -71 -155 -186 C ATOM 372 CE1 TYR A 50 -24.738 136.436 5.176 1.00 24.84 C ANISOU 372 CE1 TYR A 50 3014 4016 2409 -44 -160 -226 C ATOM 373 CE2 TYR A 50 -25.799 137.739 6.878 1.00 24.51 C ANISOU 373 CE2 TYR A 50 3075 3925 2311 -69 -207 -225 C ATOM 374 CZ TYR A 50 -24.698 137.049 6.414 1.00 24.93 C ANISOU 374 CZ TYR A 50 3042 4031 2399 -54 -213 -244 C ATOM 375 OH TYR A 50 -23.550 136.974 7.176 1.00 25.72 O ANISOU 375 OH TYR A 50 3068 4193 2512 -45 -273 -286 O ATOM 376 N ILE A 51 -27.807 138.289 1.180 1.00 23.18 N ANISOU 376 N ILE A 51 3003 3649 2156 -172 39 -108 N ATOM 377 CA ILE A 51 -27.007 138.982 0.187 1.00 24.20 C ANISOU 377 CA ILE A 51 3109 3788 2296 -244 84 -114 C ATOM 378 C ILE A 51 -26.602 140.329 0.785 1.00 25.00 C ANISOU 378 C ILE A 51 3222 3863 2415 -306 73 -129 C ATOM 379 O ILE A 51 -27.426 141.017 1.378 1.00 25.17 O ANISOU 379 O ILE A 51 3307 3829 2425 -297 51 -116 O ATOM 380 CB ILE A 51 -27.758 139.130 -1.176 1.00 23.84 C ANISOU 380 CB ILE A 51 3120 3719 2219 -260 129 -70 C ATOM 381 CG1 ILE A 51 -26.859 139.767 -2.238 1.00 24.48 C ANISOU 381 CG1 ILE A 51 3185 3817 2301 -341 185 -72 C ATOM 382 CG2 ILE A 51 -29.044 139.940 -1.054 1.00 23.57 C ANISOU 382 CG2 ILE A 51 3170 3619 2164 -249 112 -30 C ATOM 383 CD1 ILE A 51 -27.302 139.508 -3.666 1.00 24.42 C ANISOU 383 CD1 ILE A 51 3215 3814 2249 -350 230 -38 C ATOM 384 N TYR A 52 -25.330 140.683 0.650 1.00 26.27 N ANISOU 384 N TYR A 52 3317 4062 2603 -370 91 -165 N ATOM 385 CA TYR A 52 -24.848 141.991 1.086 1.00 27.44 C ANISOU 385 CA TYR A 52 3475 4179 2771 -450 88 -186 C ATOM 386 C TYR A 52 -25.198 142.992 -0.010 1.00 27.90 C ANISOU 386 C TYR A 52 3610 4175 2816 -517 142 -142 C ATOM 387 O TYR A 52 -25.368 142.598 -1.153 1.00 28.05 O ANISOU 387 O TYR A 52 3638 4207 2812 -515 186 -109 O ATOM 388 CB TYR A 52 -23.335 141.945 1.330 1.00 28.50 C ANISOU 388 CB TYR A 52 3497 4389 2943 -502 86 -245 C ATOM 389 CG TYR A 52 -22.788 143.098 2.145 1.00 29.52 C ANISOU 389 CG TYR A 52 3623 4498 3095 -579 61 -285 C ATOM 390 CD1 TYR A 52 -23.369 143.457 3.366 1.00 29.28 C ANISOU 390 CD1 TYR A 52 3646 4427 3053 -547 1 -298 C ATOM 391 CD2 TYR A 52 -21.676 143.818 1.718 1.00 30.82 C ANISOU 391 CD2 TYR A 52 3731 4687 3292 -692 100 -317 C ATOM 392 CE1 TYR A 52 -22.879 144.501 4.119 1.00 30.21 C ANISOU 392 CE1 TYR A 52 3767 4523 3188 -620 -24 -345 C ATOM 393 CE2 TYR A 52 -21.167 144.865 2.479 1.00 31.83 C ANISOU 393 CE2 TYR A 52 3858 4793 3444 -774 75 -362 C ATOM 394 CZ TYR A 52 -21.770 145.192 3.682 1.00 31.47 C ANISOU 394 CZ TYR A 52 3871 4702 3384 -734 9 -378 C ATOM 395 OH TYR A 52 -21.300 146.234 4.446 1.00 32.65 O ANISOU 395 OH TYR A 52 4027 4825 3553 -817 -18 -431 O ATOM 396 N TYR A 53 -25.319 144.273 0.332 1.00 28.74 N ANISOU 396 N TYR A 53 3778 4209 2931 -572 138 -141 N ATOM 397 CA TYR A 53 -25.749 145.290 -0.647 1.00 29.44 C ANISOU 397 CA TYR A 53 3962 4218 3004 -626 181 -87 C ATOM 398 C TYR A 53 -24.825 145.379 -1.869 1.00 30.25 C ANISOU 398 C TYR A 53 4034 4356 3102 -716 252 -74 C ATOM 399 O TYR A 53 -25.254 145.798 -2.934 1.00 30.53 O ANISOU 399 O TYR A 53 4147 4349 3105 -740 292 -16 O ATOM 400 CB TYR A 53 -25.894 146.684 -0.016 1.00 30.10 C ANISOU 400 CB TYR A 53 4123 4206 3108 -674 165 -96 C ATOM 401 CG TYR A 53 -24.585 147.370 0.291 1.00 31.39 C ANISOU 401 CG TYR A 53 4238 4380 3310 -790 180 -148 C ATOM 402 CD1 TYR A 53 -23.940 147.135 1.492 1.00 31.68 C ANISOU 402 CD1 TYR A 53 4195 4470 3371 -789 132 -220 C ATOM 403 CD2 TYR A 53 -23.983 148.249 -0.623 1.00 32.48 C ANISOU 403 CD2 TYR A 53 4409 4477 3454 -907 242 -124 C ATOM 404 CE1 TYR A 53 -22.747 147.756 1.796 1.00 32.90 C ANISOU 404 CE1 TYR A 53 4293 4645 3562 -900 138 -277 C ATOM 405 CE2 TYR A 53 -22.768 148.870 -0.332 1.00 33.63 C ANISOU 405 CE2 TYR A 53 4500 4638 3639 -1028 260 -178 C ATOM 406 CZ TYR A 53 -22.160 148.616 0.882 1.00 33.93 C ANISOU 406 CZ TYR A 53 4448 4738 3708 -1024 205 -259 C ATOM 407 OH TYR A 53 -20.968 149.202 1.208 1.00 35.61 O ANISOU 407 OH TYR A 53 4593 4977 3960 -1145 213 -321 O ATOM 408 N SER A 54 -23.555 145.014 -1.690 1.00 31.18 N ANISOU 408 N SER A 54 4037 4558 3250 -764 268 -131 N ATOM 409 CA SER A 54 -22.571 145.003 -2.772 1.00 32.11 C ANISOU 409 CA SER A 54 4102 4731 3366 -851 345 -134 C ATOM 410 C SER A 54 -22.668 143.795 -3.722 1.00 31.38 C ANISOU 410 C SER A 54 3974 4709 3241 -793 380 -120 C ATOM 411 O SER A 54 -21.955 143.759 -4.730 1.00 32.05 O ANISOU 411 O SER A 54 4023 4842 3311 -860 454 -122 O ATOM 412 CB SER A 54 -21.163 145.046 -2.171 1.00 33.51 C ANISOU 412 CB SER A 54 4151 4985 3597 -920 346 -211 C ATOM 413 OG SER A 54 -20.873 143.812 -1.526 1.00 33.48 O ANISOU 413 OG SER A 54 4043 5068 3611 -824 298 -258 O ATOM 414 N GLY A 55 -23.498 142.801 -3.391 1.00 29.97 N ANISOU 414 N GLY A 55 3802 4538 3049 -676 331 -115 N ATOM 415 CA GLY A 55 -23.742 141.651 -4.276 1.00 29.28 C ANISOU 415 CA GLY A 55 3698 4499 2927 -619 358 -106 C ATOM 416 C GLY A 55 -23.267 140.290 -3.785 1.00 28.71 C ANISOU 416 C GLY A 55 3523 4502 2883 -539 333 -160 C ATOM 417 O GLY A 55 -23.740 139.270 -4.285 1.00 28.03 O ANISOU 417 O GLY A 55 3446 4433 2773 -473 338 -154 O ATOM 418 N SER A 56 -22.346 140.255 -2.819 1.00 29.02 N ANISOU 418 N SER A 56 3471 4583 2973 -542 301 -214 N ATOM 419 CA SER A 56 -21.862 138.982 -2.247 1.00 29.02 C ANISOU 419 CA SER A 56 3379 4646 3002 -452 263 -261 C ATOM 420 C SER A 56 -23.008 138.156 -1.667 1.00 27.48 C ANISOU 420 C SER A 56 3248 4408 2787 -348 205 -232 C ATOM 421 O SER A 56 -23.809 138.672 -0.901 1.00 26.90 O ANISOU 421 O SER A 56 3242 4277 2702 -339 161 -206 O ATOM 422 CB SER A 56 -20.836 139.235 -1.147 1.00 29.94 C ANISOU 422 CB SER A 56 3400 4809 3168 -468 216 -315 C ATOM 423 OG SER A 56 -19.723 139.939 -1.658 1.00 31.38 O ANISOU 423 OG SER A 56 3505 5041 3375 -574 274 -350 O ATOM 424 N THR A 57 -23.087 136.887 -2.057 1.00 26.81 N ANISOU 424 N THR A 57 3143 4348 2697 -275 212 -241 N ATOM 425 CA THR A 57 -24.128 135.987 -1.575 1.00 25.83 C ANISOU 425 CA THR A 57 3077 4182 2556 -188 166 -216 C ATOM 426 C THR A 57 -23.529 134.939 -0.645 1.00 25.84 C ANISOU 426 C THR A 57 3014 4213 2590 -106 113 -250 C ATOM 427 O THR A 57 -22.391 134.517 -0.823 1.00 26.28 O ANISOU 427 O THR A 57 2974 4330 2680 -92 126 -297 O ATOM 428 CB THR A 57 -24.850 135.285 -2.741 1.00 25.36 C ANISOU 428 CB THR A 57 3066 4108 2460 -170 208 -197 C ATOM 429 OG1 THR A 57 -23.895 134.620 -3.575 1.00 26.02 O ANISOU 429 OG1 THR A 57 3080 4250 2557 -164 259 -242 O ATOM 430 CG2 THR A 57 -25.614 136.281 -3.562 1.00 25.27 C ANISOU 430 CG2 THR A 57 3133 4062 2406 -234 241 -152 C ATOM 431 N ASN A 58 -24.290 134.570 0.384 1.00 25.20 N ANISOU 431 N ASN A 58 2985 4092 2496 -51 54 -225 N ATOM 432 CA ASN A 58 -23.899 133.514 1.321 1.00 25.32 C ANISOU 432 CA ASN A 58 2969 4121 2531 35 -4 -239 C ATOM 433 C ASN A 58 -25.148 132.736 1.697 1.00 24.57 C ANISOU 433 C ASN A 58 2966 3965 2405 86 -26 -196 C ATOM 434 O ASN A 58 -26.135 133.327 2.153 1.00 24.20 O ANISOU 434 O ASN A 58 2987 3882 2328 61 -36 -163 O ATOM 435 CB ASN A 58 -23.213 134.082 2.579 1.00 26.00 C ANISOU 435 CB ASN A 58 3011 4238 2630 31 -68 -259 C ATOM 436 CG ASN A 58 -22.335 135.303 2.278 1.00 26.68 C ANISOU 436 CG ASN A 58 3031 4368 2739 -61 -42 -295 C ATOM 437 OD1 ASN A 58 -21.127 135.185 2.074 1.00 27.53 O ANISOU 437 OD1 ASN A 58 3031 4544 2886 -66 -36 -342 O ATOM 438 ND2 ASN A 58 -22.954 136.481 2.235 1.00 26.46 N ANISOU 438 ND2 ASN A 58 3066 4297 2690 -135 -23 -273 N ATOM 439 N TYR A 59 -25.106 131.422 1.498 1.00 24.54 N ANISOU 439 N TYR A 59 2964 3949 2410 154 -27 -201 N ATOM 440 CA TYR A 59 -26.278 130.562 1.667 1.00 24.01 C ANISOU 440 CA TYR A 59 2983 3821 2317 187 -35 -163 C ATOM 441 C TYR A 59 -26.032 129.516 2.752 1.00 24.23 C ANISOU 441 C TYR A 59 3025 3830 2353 268 -93 -153 C ATOM 442 O TYR A 59 -24.891 129.244 3.124 1.00 24.66 O ANISOU 442 O TYR A 59 3013 3920 2438 317 -128 -181 O ATOM 443 CB TYR A 59 -26.605 129.849 0.350 1.00 24.00 C ANISOU 443 CB TYR A 59 3000 3803 2316 186 20 -175 C ATOM 444 CG TYR A 59 -26.710 130.757 -0.856 1.00 23.93 C ANISOU 444 CG TYR A 59 2982 3819 2290 113 78 -182 C ATOM 445 CD1 TYR A 59 -27.462 131.930 -0.808 1.00 23.44 C ANISOU 445 CD1 TYR A 59 2958 3747 2201 54 80 -149 C ATOM 446 CD2 TYR A 59 -26.060 130.436 -2.061 1.00 24.39 C ANISOU 446 CD2 TYR A 59 3001 3910 2357 107 132 -221 C ATOM 447 CE1 TYR A 59 -27.563 132.769 -1.909 1.00 23.37 C ANISOU 447 CE1 TYR A 59 2955 3752 2171 -8 126 -145 C ATOM 448 CE2 TYR A 59 -26.175 131.258 -3.182 1.00 24.40 C ANISOU 448 CE2 TYR A 59 3009 3935 2328 36 185 -219 C ATOM 449 CZ TYR A 59 -26.930 132.421 -3.102 1.00 23.95 C ANISOU 449 CZ TYR A 59 2997 3860 2243 -21 179 -176 C ATOM 450 OH TYR A 59 -27.042 133.261 -4.185 1.00 23.95 O ANISOU 450 OH TYR A 59 3017 3874 2209 -87 226 -163 O ATOM 451 N ASN A 60 -27.127 128.957 3.257 1.00 23.65 N ANISOU 451 N ASN A 60 3037 3700 2249 281 -105 -111 N ATOM 452 CA ASN A 60 -27.091 127.801 4.145 1.00 23.97 C ANISOU 452 CA ASN A 60 3119 3701 2286 352 -151 -87 C ATOM 453 C ASN A 60 -26.373 126.650 3.407 1.00 24.76 C ANISOU 453 C ASN A 60 3194 3784 2429 416 -139 -118 C ATOM 454 O ASN A 60 -26.805 126.291 2.300 1.00 23.93 O ANISOU 454 O ASN A 60 3105 3656 2330 394 -86 -134 O ATOM 455 CB ASN A 60 -28.531 127.410 4.488 1.00 23.57 C ANISOU 455 CB ASN A 60 3166 3592 2197 329 -138 -40 C ATOM 456 CG ASN A 60 -28.629 126.261 5.470 1.00 24.06 C ANISOU 456 CG ASN A 60 3295 3603 2245 387 -179 -2 C ATOM 457 OD1 ASN A 60 -27.843 125.325 5.435 1.00 24.58 O ANISOU 457 OD1 ASN A 60 3354 3647 2341 457 -203 -11 O ATOM 458 ND2 ASN A 60 -29.630 126.320 6.344 1.00 23.99 N ANISOU 458 ND2 ASN A 60 3355 3572 2189 359 -182 42 N ATOM 459 N PRO A 61 -25.297 126.078 4.003 1.00 25.84 N ANISOU 459 N PRO A 61 3290 3933 2593 499 -193 -130 N ATOM 460 CA PRO A 61 -24.529 124.999 3.344 1.00 26.93 C ANISOU 460 CA PRO A 61 3398 4055 2780 577 -183 -168 C ATOM 461 C PRO A 61 -25.344 123.791 2.874 1.00 27.30 C ANISOU 461 C PRO A 61 3540 4006 2826 596 -154 -153 C ATOM 462 O PRO A 61 -24.979 123.181 1.884 1.00 27.50 O ANISOU 462 O PRO A 61 3544 4021 2885 624 -115 -200 O ATOM 463 CB PRO A 61 -23.512 124.569 4.414 1.00 27.83 C ANISOU 463 CB PRO A 61 3476 4186 2914 675 -268 -164 C ATOM 464 CG PRO A 61 -23.382 125.741 5.315 1.00 27.64 C ANISOU 464 CG PRO A 61 3420 4225 2858 628 -309 -151 C ATOM 465 CD PRO A 61 -24.735 126.398 5.332 1.00 26.42 C ANISOU 465 CD PRO A 61 3345 4041 2652 533 -270 -113 C ATOM 466 N SER A 62 -26.438 123.458 3.559 1.00 27.61 N ANISOU 466 N SER A 62 3683 3982 2827 573 -167 -95 N ATOM 467 CA SER A 62 -27.261 122.312 3.162 1.00 28.29 C ANISOU 467 CA SER A 62 3863 3973 2913 574 -139 -82 C ATOM 468 C SER A 62 -28.175 122.635 1.949 1.00 27.69 C ANISOU 468 C SER A 62 3794 3903 2823 484 -69 -107 C ATOM 469 O SER A 62 -28.624 121.728 1.255 1.00 27.60 O ANISOU 469 O SER A 62 3835 3831 2822 480 -38 -125 O ATOM 470 CB SER A 62 -28.008 121.772 4.395 1.00 28.72 C ANISOU 470 CB SER A 62 4022 3961 2930 578 -176 -9 C ATOM 471 OG SER A 62 -29.040 122.644 4.774 1.00 28.32 O ANISOU 471 OG SER A 62 3992 3939 2831 490 -160 22 O ATOM 472 N LEU A 63 -28.401 123.925 1.669 1.00 27.29 N ANISOU 472 N LEU A 63 3693 3924 2750 415 -49 -111 N ATOM 473 CA LEU A 63 -29.234 124.374 0.540 1.00 26.86 C ANISOU 473 CA LEU A 63 3643 3886 2675 337 5 -128 C ATOM 474 C LEU A 63 -28.444 125.041 -0.606 1.00 27.03 C ANISOU 474 C LEU A 63 3587 3976 2708 321 44 -179 C ATOM 475 O LEU A 63 -29.018 125.333 -1.654 1.00 26.36 O ANISOU 475 O LEU A 63 3511 3906 2599 265 85 -193 O ATOM 476 CB LEU A 63 -30.301 125.339 1.051 1.00 26.40 C ANISOU 476 CB LEU A 63 3606 3847 2578 271 0 -85 C ATOM 477 CG LEU A 63 -31.181 124.802 2.191 1.00 26.43 C ANISOU 477 CG LEU A 63 3684 3799 2561 270 -24 -34 C ATOM 478 CD1 LEU A 63 -31.972 125.933 2.808 1.00 25.91 C ANISOU 478 CD1 LEU A 63 3616 3769 2460 220 -27 -5 C ATOM 479 CD2 LEU A 63 -32.099 123.685 1.697 1.00 26.86 C ANISOU 479 CD2 LEU A 63 3805 3787 2614 245 3 -34 C ATOM 480 N LYS A 64 -27.131 125.201 -0.412 1.00 27.63 N ANISOU 480 N LYS A 64 3587 4094 2816 370 30 -207 N ATOM 481 CA LYS A 64 -26.223 125.983 -1.271 1.00 28.28 C ANISOU 481 CA LYS A 64 3582 4254 2909 346 69 -252 C ATOM 482 C LYS A 64 -26.412 125.814 -2.792 1.00 28.22 C ANISOU 482 C LYS A 64 3580 4257 2883 309 138 -292 C ATOM 483 O LYS A 64 -26.607 126.800 -3.521 1.00 28.03 O ANISOU 483 O LYS A 64 3543 4278 2827 237 174 -289 O ATOM 484 CB LYS A 64 -24.778 125.612 -0.906 1.00 29.96 C ANISOU 484 CB LYS A 64 3710 4501 3172 426 46 -291 C ATOM 485 CG LYS A 64 -23.719 126.630 -1.277 1.00 30.83 C ANISOU 485 CG LYS A 64 3711 4704 3297 392 72 -329 C ATOM 486 CD LYS A 64 -22.405 126.292 -0.593 1.00 32.04 C ANISOU 486 CD LYS A 64 3772 4899 3504 475 27 -362 C ATOM 487 CE LYS A 64 -21.700 125.157 -1.265 1.00 33.35 C ANISOU 487 CE LYS A 64 3900 5060 3712 560 54 -421 C ATOM 488 NZ LYS A 64 -20.526 124.706 -0.475 1.00 34.64 N ANISOU 488 NZ LYS A 64 3977 5255 3929 665 -7 -447 N ATOM 489 N SER A 65 -26.385 124.570 -3.265 1.00 28.12 N ANISOU 489 N SER A 65 3598 4199 2887 358 154 -328 N ATOM 490 CA SER A 65 -26.466 124.295 -4.713 1.00 28.25 C ANISOU 490 CA SER A 65 3622 4230 2880 330 219 -379 C ATOM 491 C SER A 65 -27.837 124.613 -5.326 1.00 27.34 C ANISOU 491 C SER A 65 3578 4102 2707 247 232 -351 C ATOM 492 O SER A 65 -27.969 124.622 -6.547 1.00 27.25 O ANISOU 492 O SER A 65 3576 4119 2661 210 280 -387 O ATOM 493 CB SER A 65 -26.095 122.840 -5.015 1.00 29.04 C ANISOU 493 CB SER A 65 3744 4275 3016 409 231 -434 C ATOM 494 OG SER A 65 -27.125 121.959 -4.609 1.00 28.95 O ANISOU 494 OG SER A 65 3831 4168 3000 412 201 -406 O ATOM 495 N ARG A 66 -28.842 124.851 -4.479 1.00 26.69 N ANISOU 495 N ARG A 66 3543 3985 2614 223 189 -292 N ATOM 496 CA ARG A 66 -30.213 125.101 -4.915 1.00 26.27 C ANISOU 496 CA ARG A 66 3544 3922 2514 156 190 -266 C ATOM 497 C ARG A 66 -30.683 126.555 -4.810 1.00 25.04 C ANISOU 497 C ARG A 66 3374 3813 2328 101 181 -220 C ATOM 498 O ARG A 66 -31.721 126.893 -5.373 1.00 24.57 O ANISOU 498 O ARG A 66 3345 3761 2228 52 182 -203 O ATOM 499 CB ARG A 66 -31.165 124.244 -4.082 1.00 26.77 C ANISOU 499 CB ARG A 66 3671 3912 2588 163 157 -237 C ATOM 500 CG ARG A 66 -30.862 122.753 -4.082 1.00 28.22 C ANISOU 500 CG ARG A 66 3895 4023 2805 215 160 -274 C ATOM 501 CD ARG A 66 -31.713 122.044 -3.031 1.00 28.99 C ANISOU 501 CD ARG A 66 4059 4043 2911 214 128 -229 C ATOM 502 NE ARG A 66 -33.119 122.284 -3.304 1.00 29.07 N ANISOU 502 NE ARG A 66 4099 4061 2885 132 132 -211 N ATOM 503 CZ ARG A 66 -34.125 122.223 -2.429 1.00 29.12 C ANISOU 503 CZ ARG A 66 4140 4040 2884 98 114 -164 C ATOM 504 NH1 ARG A 66 -33.941 121.916 -1.149 1.00 29.21 N ANISOU 504 NH1 ARG A 66 4178 4008 2911 133 89 -121 N ATOM 505 NH2 ARG A 66 -35.349 122.485 -2.869 1.00 28.65 N ANISOU 505 NH2 ARG A 66 4086 4005 2796 27 120 -161 N ATOM 506 N VAL A 67 -29.941 127.396 -4.091 1.00 24.40 N ANISOU 506 N VAL A 67 3246 3759 2267 112 167 -202 N ATOM 507 CA VAL A 67 -30.391 128.750 -3.726 1.00 23.71 C ANISOU 507 CA VAL A 67 3156 3693 2159 69 152 -158 C ATOM 508 C VAL A 67 -29.711 129.820 -4.561 1.00 23.46 C ANISOU 508 C VAL A 67 3088 3713 2111 27 187 -166 C ATOM 509 O VAL A 67 -28.494 129.772 -4.774 1.00 23.91 O ANISOU 509 O VAL A 67 3091 3803 2191 39 213 -201 O ATOM 510 CB VAL A 67 -30.121 129.035 -2.232 1.00 23.67 C ANISOU 510 CB VAL A 67 3136 3675 2181 98 109 -133 C ATOM 511 CG1 VAL A 67 -30.389 130.493 -1.883 1.00 23.40 C ANISOU 511 CG1 VAL A 67 3098 3660 2132 57 98 -103 C ATOM 512 CG2 VAL A 67 -30.982 128.126 -1.366 1.00 23.63 C ANISOU 512 CG2 VAL A 67 3182 3618 2177 124 79 -110 C ATOM 513 N THR A 68 -30.512 130.768 -5.043 1.00 23.00 N ANISOU 513 N THR A 68 3063 3662 2015 -20 189 -132 N ATOM 514 CA THR A 68 -30.014 132.011 -5.626 1.00 23.02 C ANISOU 514 CA THR A 68 3052 3696 1997 -69 217 -119 C ATOM 515 C THR A 68 -30.692 133.177 -4.922 1.00 22.55 C ANISOU 515 C THR A 68 3018 3612 1936 -86 183 -72 C ATOM 516 O THR A 68 -31.920 133.207 -4.814 1.00 22.40 O ANISOU 516 O THR A 68 3039 3572 1899 -79 156 -45 O ATOM 517 CB THR A 68 -30.308 132.132 -7.134 1.00 23.16 C ANISOU 517 CB THR A 68 3103 3740 1957 -109 254 -119 C ATOM 518 OG1 THR A 68 -30.063 130.883 -7.788 1.00 23.55 O ANISOU 518 OG1 THR A 68 3147 3801 2000 -87 281 -170 O ATOM 519 CG2 THR A 68 -29.424 133.210 -7.754 1.00 23.72 C ANISOU 519 CG2 THR A 68 3159 3844 2010 -163 299 -111 C ATOM 520 N ILE A 69 -29.895 134.120 -4.429 1.00 22.59 N ANISOU 520 N ILE A 69 2996 3623 1963 -108 185 -69 N ATOM 521 CA ILE A 69 -30.414 135.391 -3.935 1.00 22.51 C ANISOU 521 CA ILE A 69 3018 3584 1951 -130 162 -32 C ATOM 522 C ILE A 69 -29.804 136.477 -4.805 1.00 23.36 C ANISOU 522 C ILE A 69 3135 3701 2041 -193 201 -19 C ATOM 523 O ILE A 69 -28.592 136.475 -5.039 1.00 23.97 O ANISOU 523 O ILE A 69 3162 3813 2134 -224 237 -48 O ATOM 524 CB ILE A 69 -30.122 135.604 -2.427 1.00 22.12 C ANISOU 524 CB ILE A 69 2945 3520 1939 -108 125 -41 C ATOM 525 CG1 ILE A 69 -30.787 134.489 -1.617 1.00 21.70 C ANISOU 525 CG1 ILE A 69 2899 3455 1890 -52 93 -44 C ATOM 526 CG2 ILE A 69 -30.649 136.964 -1.960 1.00 21.95 C ANISOU 526 CG2 ILE A 69 2964 3462 1915 -130 108 -14 C ATOM 527 CD1 ILE A 69 -30.363 134.412 -0.166 1.00 21.72 C ANISOU 527 CD1 ILE A 69 2882 3454 1916 -25 56 -55 C ATOM 528 N SER A 70 -30.650 137.374 -5.319 1.00 23.79 N ANISOU 528 N SER A 70 3253 3726 2062 -213 196 27 N ATOM 529 CA SER A 70 -30.211 138.435 -6.213 1.00 24.93 C ANISOU 529 CA SER A 70 3430 3864 2179 -277 233 55 C ATOM 530 C SER A 70 -30.770 139.786 -5.802 1.00 25.69 C ANISOU 530 C SER A 70 3584 3896 2280 -287 206 97 C ATOM 531 O SER A 70 -31.869 139.871 -5.257 1.00 25.30 O ANISOU 531 O SER A 70 3560 3817 2236 -236 161 112 O ATOM 532 CB SER A 70 -30.629 138.130 -7.653 1.00 25.20 C ANISOU 532 CB SER A 70 3504 3923 2147 -289 257 75 C ATOM 533 OG SER A 70 -30.190 136.847 -8.031 1.00 25.20 O ANISOU 533 OG SER A 70 3458 3974 2144 -274 283 27 O ATOM 534 N LEU A 71 -29.987 140.831 -6.056 1.00 27.34 N ANISOU 534 N LEU A 71 3812 4085 2492 -355 238 110 N ATOM 535 CA LEU A 71 -30.420 142.217 -5.836 1.00 28.59 C ANISOU 535 CA LEU A 71 4043 4165 2655 -372 220 152 C ATOM 536 C LEU A 71 -31.034 142.788 -7.097 1.00 29.45 C ANISOU 536 C LEU A 71 4238 4248 2704 -385 228 217 C ATOM 537 O LEU A 71 -30.534 142.541 -8.198 1.00 29.53 O ANISOU 537 O LEU A 71 4254 4299 2668 -431 275 228 O ATOM 538 CB LEU A 71 -29.254 143.131 -5.468 1.00 29.54 C ANISOU 538 CB LEU A 71 4152 4261 2809 -452 250 135 C ATOM 539 CG LEU A 71 -28.620 143.012 -4.103 1.00 29.51 C ANISOU 539 CG LEU A 71 4081 4270 2863 -448 227 76 C ATOM 540 CD1 LEU A 71 -27.388 143.899 -3.954 1.00 30.56 C ANISOU 540 CD1 LEU A 71 4193 4391 3025 -546 261 54 C ATOM 541 CD2 LEU A 71 -29.628 143.301 -3.012 1.00 29.19 C ANISOU 541 CD2 LEU A 71 4073 4177 2840 -382 170 76 C ATOM 542 N HIS A 72 -32.078 143.595 -6.927 1.00 30.00 N ANISOU 542 N HIS A 72 4376 4251 2771 -343 185 259 N ATOM 543 CA HIS A 72 -32.659 144.362 -8.031 1.00 31.38 C ANISOU 543 CA HIS A 72 4646 4385 2890 -347 179 331 C ATOM 544 C HIS A 72 -32.803 145.820 -7.600 1.00 32.07 C ANISOU 544 C HIS A 72 4812 4366 3007 -355 163 365 C ATOM 545 O HIS A 72 -33.874 146.245 -7.148 1.00 31.51 O ANISOU 545 O HIS A 72 4773 4247 2954 -277 111 380 O ATOM 546 CB HIS A 72 -33.998 143.746 -8.457 1.00 31.47 C ANISOU 546 CB HIS A 72 4663 4429 2866 -266 128 349 C ATOM 547 CG HIS A 72 -33.927 142.272 -8.679 1.00 31.14 C ANISOU 547 CG HIS A 72 4548 4476 2809 -257 139 303 C ATOM 548 ND1 HIS A 72 -33.420 141.717 -9.832 1.00 32.02 N ANISOU 548 ND1 HIS A 72 4663 4644 2861 -301 179 305 N ATOM 549 CD2 HIS A 72 -34.258 141.236 -7.874 1.00 30.69 C ANISOU 549 CD2 HIS A 72 4419 4455 2787 -212 120 252 C ATOM 550 CE1 HIS A 72 -33.462 140.400 -9.740 1.00 31.58 C ANISOU 550 CE1 HIS A 72 4542 4648 2809 -278 181 252 C ATOM 551 NE2 HIS A 72 -33.975 140.084 -8.566 1.00 30.90 N ANISOU 551 NE2 HIS A 72 4412 4547 2780 -226 144 224 N ATOM 552 N THR A 73 -31.715 146.580 -7.752 1.00 32.85 N ANISOU 552 N THR A 73 4940 4427 3113 -450 213 373 N ATOM 553 CA THR A 73 -31.640 147.943 -7.207 1.00 33.73 C ANISOU 553 CA THR A 73 5126 4426 3264 -474 206 390 C ATOM 554 C THR A 73 -32.570 148.953 -7.886 1.00 33.81 C ANISOU 554 C THR A 73 5264 4341 3241 -435 174 474 C ATOM 555 O THR A 73 -33.068 149.850 -7.217 1.00 33.94 O ANISOU 555 O THR A 73 5334 4261 3298 -394 140 478 O ATOM 556 CB THR A 73 -30.205 148.500 -7.225 1.00 35.14 C ANISOU 556 CB THR A 73 5301 4588 3462 -604 270 374 C ATOM 557 OG1 THR A 73 -29.681 148.453 -8.552 1.00 36.26 O ANISOU 557 OG1 THR A 73 5475 4763 3539 -678 328 421 O ATOM 558 CG2 THR A 73 -29.307 147.709 -6.284 1.00 35.00 C ANISOU 558 CG2 THR A 73 5155 4651 3493 -626 283 285 C ATOM 559 N SER A 74 -32.828 148.802 -9.185 1.00 33.94 N ANISOU 559 N SER A 74 5330 4384 3180 -439 180 538 N ATOM 560 CA SER A 74 -33.750 149.712 -9.878 1.00 34.63 C ANISOU 560 CA SER A 74 5543 4388 3229 -388 136 626 C ATOM 561 C SER A 74 -35.209 149.556 -9.422 1.00 33.77 C ANISOU 561 C SER A 74 5415 4276 3141 -247 53 620 C ATOM 562 O SER A 74 -36.025 150.436 -9.688 1.00 34.19 O ANISOU 562 O SER A 74 5560 4246 3186 -181 4 680 O ATOM 563 CB SER A 74 -33.634 149.593 -11.413 1.00 35.76 C ANISOU 563 CB SER A 74 5750 4568 3268 -431 159 699 C ATOM 564 OG SER A 74 -34.335 148.473 -11.909 1.00 35.44 O ANISOU 564 OG SER A 74 5652 4635 3180 -367 125 686 O ATOM 565 N LYS A 75 -35.528 148.443 -8.752 1.00 32.32 N ANISOU 565 N LYS A 75 5115 4183 2984 -201 38 550 N ATOM 566 CA LYS A 75 -36.840 148.233 -8.139 1.00 32.11 C ANISOU 566 CA LYS A 75 5048 4165 2986 -83 -27 529 C ATOM 567 C LYS A 75 -36.819 148.231 -6.604 1.00 30.81 C ANISOU 567 C LYS A 75 4823 3984 2900 -59 -25 454 C ATOM 568 O LYS A 75 -37.875 148.160 -5.989 1.00 30.68 O ANISOU 568 O LYS A 75 4774 3972 2910 33 -67 432 O ATOM 569 CB LYS A 75 -37.435 146.925 -8.654 1.00 32.25 C ANISOU 569 CB LYS A 75 4990 4301 2962 -50 -47 514 C ATOM 570 CG LYS A 75 -37.518 146.878 -10.173 1.00 33.64 C ANISOU 570 CG LYS A 75 5227 4506 3047 -70 -54 581 C ATOM 571 CD LYS A 75 -38.145 145.594 -10.687 1.00 34.09 C ANISOU 571 CD LYS A 75 5214 4677 3062 -42 -80 556 C ATOM 572 CE LYS A 75 -39.658 145.712 -10.855 1.00 34.98 C ANISOU 572 CE LYS A 75 5323 4802 3166 64 -165 579 C ATOM 573 NZ LYS A 75 -40.205 144.625 -11.720 1.00 35.33 N ANISOU 573 NZ LYS A 75 5325 4953 3147 69 -192 568 N ATOM 574 N ASN A 76 -35.633 148.324 -5.993 1.00 30.00 N ANISOU 574 N ASN A 76 4702 3868 2829 -142 22 413 N ATOM 575 CA ASN A 76 -35.471 148.262 -4.529 1.00 28.92 C ANISOU 575 CA ASN A 76 4510 3726 2752 -131 22 339 C ATOM 576 C ASN A 76 -35.963 146.912 -3.994 1.00 27.37 C ANISOU 576 C ASN A 76 4210 3633 2556 -81 9 292 C ATOM 577 O ASN A 76 -36.655 146.822 -2.970 1.00 26.48 O ANISOU 577 O ASN A 76 4065 3522 2473 -19 -13 252 O ATOM 578 CB ASN A 76 -36.172 149.464 -3.860 1.00 29.49 C ANISOU 578 CB ASN A 76 4651 3690 2865 -69 -8 338 C ATOM 579 CG ASN A 76 -35.449 149.948 -2.609 1.00 29.53 C ANISOU 579 CG ASN A 76 4650 3650 2919 -111 10 272 C ATOM 580 OD1 ASN A 76 -34.245 150.212 -2.634 1.00 29.59 O ANISOU 580 OD1 ASN A 76 4667 3641 2933 -214 46 261 O ATOM 581 ND2 ASN A 76 -36.179 150.062 -1.510 1.00 29.30 N ANISOU 581 ND2 ASN A 76 4602 3609 2921 -36 -14 222 N ATOM 582 N GLN A 77 -35.629 145.858 -4.740 1.00 26.70 N ANISOU 582 N GLN A 77 4080 3632 2434 -112 27 297 N ATOM 583 CA GLN A 77 -36.070 144.498 -4.422 1.00 25.98 C ANISOU 583 CA GLN A 77 3904 3628 2339 -76 17 260 C ATOM 584 C GLN A 77 -34.884 143.573 -4.321 1.00 25.30 C ANISOU 584 C GLN A 77 3758 3599 2255 -137 55 223 C ATOM 585 O GLN A 77 -33.818 143.853 -4.885 1.00 25.40 O ANISOU 585 O GLN A 77 3785 3608 2257 -208 92 231 O ATOM 586 CB GLN A 77 -36.993 143.945 -5.513 1.00 26.27 C ANISOU 586 CB GLN A 77 3942 3712 2329 -39 -8 296 C ATOM 587 CG GLN A 77 -38.271 144.721 -5.745 1.00 27.07 C ANISOU 587 CG GLN A 77 4086 3774 2425 37 -57 334 C ATOM 588 CD GLN A 77 -39.074 144.196 -6.922 1.00 27.65 C ANISOU 588 CD GLN A 77 4158 3905 2444 63 -90 368 C ATOM 589 OE1 GLN A 77 -38.537 143.562 -7.826 1.00 27.81 O ANISOU 589 OE1 GLN A 77 4179 3972 2416 11 -68 377 O ATOM 590 NE2 GLN A 77 -40.369 144.480 -6.925 1.00 28.17 N ANISOU 590 NE2 GLN A 77 4218 3971 2514 146 -143 382 N ATOM 591 N PHE A 78 -35.080 142.475 -3.593 1.00 24.16 N ANISOU 591 N PHE A 78 3547 3508 2124 -107 47 181 N ATOM 592 CA PHE A 78 -34.209 141.321 -3.683 1.00 23.76 C ANISOU 592 CA PHE A 78 3439 3518 2070 -137 72 150 C ATOM 593 C PHE A 78 -35.054 140.053 -3.811 1.00 23.53 C ANISOU 593 C PHE A 78 3376 3539 2026 -95 57 140 C ATOM 594 O PHE A 78 -36.187 139.986 -3.315 1.00 23.25 O ANISOU 594 O PHE A 78 3338 3500 1996 -46 29 142 O ATOM 595 CB PHE A 78 -33.180 141.264 -2.532 1.00 23.52 C ANISOU 595 CB PHE A 78 3366 3490 2079 -159 80 104 C ATOM 596 CG PHE A 78 -33.770 141.122 -1.155 1.00 23.02 C ANISOU 596 CG PHE A 78 3289 3420 2037 -111 50 78 C ATOM 597 CD1 PHE A 78 -34.367 142.209 -0.518 1.00 23.17 C ANISOU 597 CD1 PHE A 78 3350 3384 2069 -90 32 80 C ATOM 598 CD2 PHE A 78 -33.675 139.922 -0.464 1.00 22.39 C ANISOU 598 CD2 PHE A 78 3161 3385 1961 -87 42 50 C ATOM 599 CE1 PHE A 78 -34.887 142.083 0.767 1.00 22.93 C ANISOU 599 CE1 PHE A 78 3308 3356 2049 -49 14 50 C ATOM 600 CE2 PHE A 78 -34.198 139.788 0.817 1.00 22.15 C ANISOU 600 CE2 PHE A 78 3127 3352 1938 -51 21 31 C ATOM 601 CZ PHE A 78 -34.806 140.871 1.433 1.00 22.54 C ANISOU 601 CZ PHE A 78 3212 3358 1994 -33 10 28 C ATOM 602 N SER A 79 -34.513 139.059 -4.508 1.00 23.50 N ANISOU 602 N SER A 79 3345 3581 2002 -117 81 126 N ATOM 603 CA SER A 79 -35.272 137.859 -4.852 1.00 23.37 C ANISOU 603 CA SER A 79 3310 3603 1968 -92 70 115 C ATOM 604 C SER A 79 -34.632 136.588 -4.317 1.00 23.07 C ANISOU 604 C SER A 79 3225 3589 1951 -88 84 73 C ATOM 605 O SER A 79 -33.444 136.561 -3.974 1.00 22.94 O ANISOU 605 O SER A 79 3183 3577 1958 -105 104 51 O ATOM 606 CB SER A 79 -35.441 137.754 -6.364 1.00 23.85 C ANISOU 606 CB SER A 79 3398 3689 1973 -113 79 135 C ATOM 607 OG SER A 79 -34.181 137.846 -7.018 1.00 24.83 O ANISOU 607 OG SER A 79 3524 3827 2083 -162 125 129 O ATOM 608 N LEU A 80 -35.452 135.545 -4.256 1.00 22.52 N ANISOU 608 N LEU A 80 3145 3535 1877 -65 71 61 N ATOM 609 CA LEU A 80 -35.012 134.202 -3.936 1.00 22.58 C ANISOU 609 CA LEU A 80 3127 3553 1900 -57 81 27 C ATOM 610 C LEU A 80 -35.463 133.258 -5.033 1.00 22.70 C ANISOU 610 C LEU A 80 3151 3589 1885 -67 89 13 C ATOM 611 O LEU A 80 -36.612 133.302 -5.444 1.00 22.69 O ANISOU 611 O LEU A 80 3163 3598 1860 -68 68 26 O ATOM 612 CB LEU A 80 -35.628 133.747 -2.606 1.00 22.15 C ANISOU 612 CB LEU A 80 3065 3481 1869 -29 61 25 C ATOM 613 CG LEU A 80 -35.476 132.273 -2.201 1.00 22.17 C ANISOU 613 CG LEU A 80 3061 3478 1885 -17 65 2 C ATOM 614 CD1 LEU A 80 -34.026 131.953 -1.905 1.00 22.17 C ANISOU 614 CD1 LEU A 80 3040 3476 1907 -4 74 -19 C ATOM 615 CD2 LEU A 80 -36.366 131.969 -1.002 1.00 22.10 C ANISOU 615 CD2 LEU A 80 3058 3455 1883 -3 50 13 C ATOM 616 N LYS A 81 -34.552 132.400 -5.478 1.00 23.38 N ANISOU 616 N LYS A 81 3226 3686 1973 -72 117 -21 N ATOM 617 CA LYS A 81 -34.891 131.245 -6.279 1.00 24.04 C ANISOU 617 CA LYS A 81 3321 3779 2036 -78 126 -52 C ATOM 618 C LYS A 81 -34.397 129.998 -5.564 1.00 23.75 C ANISOU 618 C LYS A 81 3271 3713 2038 -50 132 -84 C ATOM 619 O LYS A 81 -33.230 129.917 -5.169 1.00 23.76 O ANISOU 619 O LYS A 81 3248 3712 2069 -29 146 -99 O ATOM 620 CB LYS A 81 -34.287 131.338 -7.678 1.00 25.42 C ANISOU 620 CB LYS A 81 3506 3988 2166 -105 160 -69 C ATOM 621 CG LYS A 81 -34.851 132.471 -8.505 1.00 26.54 C ANISOU 621 CG LYS A 81 3677 4151 2255 -131 148 -27 C ATOM 622 CD LYS A 81 -34.139 132.555 -9.849 1.00 28.38 C ANISOU 622 CD LYS A 81 3930 4422 2432 -164 191 -41 C ATOM 623 CE LYS A 81 -34.530 133.783 -10.648 1.00 29.15 C ANISOU 623 CE LYS A 81 4072 4533 2471 -190 180 14 C ATOM 624 NZ LYS A 81 -35.926 134.257 -10.426 1.00 29.43 N ANISOU 624 NZ LYS A 81 4126 4557 2501 -168 117 54 N ATOM 625 N LEU A 82 -35.303 129.045 -5.374 1.00 23.25 N ANISOU 625 N LEU A 82 3228 3629 1979 -51 118 -93 N ATOM 626 CA LEU A 82 -34.987 127.752 -4.787 1.00 23.04 C ANISOU 626 CA LEU A 82 3211 3558 1985 -26 122 -117 C ATOM 627 C LEU A 82 -35.344 126.686 -5.808 1.00 22.94 C ANISOU 627 C LEU A 82 3225 3536 1953 -46 136 -160 C ATOM 628 O LEU A 82 -36.520 126.469 -6.087 1.00 23.06 O ANISOU 628 O LEU A 82 3257 3557 1949 -82 121 -159 O ATOM 629 CB LEU A 82 -35.766 127.555 -3.490 1.00 22.70 C ANISOU 629 CB LEU A 82 3179 3485 1960 -21 98 -87 C ATOM 630 CG LEU A 82 -35.509 126.248 -2.727 1.00 22.84 C ANISOU 630 CG LEU A 82 3226 3444 2008 4 98 -95 C ATOM 631 CD1 LEU A 82 -34.111 126.217 -2.108 1.00 23.01 C ANISOU 631 CD1 LEU A 82 3230 3455 2057 59 93 -97 C ATOM 632 CD2 LEU A 82 -36.565 126.039 -1.663 1.00 22.74 C ANISOU 632 CD2 LEU A 82 3235 3410 1996 -14 86 -62 C ATOM 633 N SER A 82A -34.330 126.043 -6.382 1.00 22.78 N ANISOU 633 N SER A 82A 3206 3509 1941 -25 165 -205 N ATOM 634 CA SER A 82A -34.537 125.030 -7.416 1.00 23.20 C ANISOU 634 CA SER A 82A 3290 3551 1973 -42 184 -260 C ATOM 635 C SER A 82A -34.895 123.679 -6.792 1.00 23.35 C ANISOU 635 C SER A 82A 3349 3492 2030 -31 175 -276 C ATOM 636 O SER A 82A -34.763 123.501 -5.584 1.00 22.85 O ANISOU 636 O SER A 82A 3290 3388 2005 -1 159 -243 O ATOM 637 CB SER A 82A -33.271 124.887 -8.288 1.00 23.49 C ANISOU 637 CB SER A 82A 3311 3612 2002 -18 228 -310 C ATOM 638 OG SER A 82A -32.251 124.169 -7.605 1.00 23.65 O ANISOU 638 OG SER A 82A 3316 3590 2080 45 237 -331 O ATOM 639 N SER A 82B -35.355 122.746 -7.628 1.00 24.05 N ANISOU 639 N SER A 82B 3477 3559 2102 -61 186 -327 N ATOM 640 CA SER A 82B -35.479 121.323 -7.271 1.00 24.94 C ANISOU 640 CA SER A 82B 3643 3581 2252 -52 189 -357 C ATOM 641 C SER A 82B -36.403 121.097 -6.094 1.00 24.94 C ANISOU 641 C SER A 82B 3663 3537 2275 -78 164 -305 C ATOM 642 O SER A 82B -36.161 120.250 -5.251 1.00 25.23 O ANISOU 642 O SER A 82B 3740 3493 2351 -49 162 -293 O ATOM 643 CB SER A 82B -34.096 120.716 -6.958 1.00 25.60 C ANISOU 643 CB SER A 82B 3729 3616 2381 30 208 -381 C ATOM 644 OG SER A 82B -33.129 121.156 -7.882 1.00 26.21 O ANISOU 644 OG SER A 82B 3766 3754 2440 55 240 -422 O ATOM 645 N VAL A 82C -37.476 121.865 -6.051 1.00 24.83 N ANISOU 645 N VAL A 82C 3622 3577 2234 -130 145 -274 N ATOM 646 CA VAL A 82C -38.318 121.943 -4.881 1.00 25.15 C ANISOU 646 CA VAL A 82C 3663 3602 2290 -153 130 -222 C ATOM 647 C VAL A 82C -39.165 120.644 -4.764 1.00 25.73 C ANISOU 647 C VAL A 82C 3791 3606 2379 -210 137 -244 C ATOM 648 O VAL A 82C -39.555 120.066 -5.790 1.00 25.90 O ANISOU 648 O VAL A 82C 3829 3625 2386 -255 141 -300 O ATOM 649 CB VAL A 82C -39.081 123.295 -4.981 1.00 24.96 C ANISOU 649 CB VAL A 82C 3582 3666 2235 -175 111 -191 C ATOM 650 CG1 VAL A 82C -40.375 123.204 -5.773 1.00 25.23 C ANISOU 650 CG1 VAL A 82C 3603 3742 2242 -243 96 -216 C ATOM 651 CG2 VAL A 82C -39.257 123.930 -3.638 1.00 24.86 C ANISOU 651 CG2 VAL A 82C 3552 3657 2238 -156 103 -134 C ATOM 652 N THR A 83 -39.331 120.129 -3.538 1.00 25.88 N ANISOU 652 N THR A 83 3846 3563 2425 -211 141 -202 N ATOM 653 CA THR A 83 -40.223 118.987 -3.258 1.00 26.76 C ANISOU 653 CA THR A 83 4013 3604 2551 -282 154 -209 C ATOM 654 C THR A 83 -41.186 119.384 -2.142 1.00 26.52 C ANISOU 654 C THR A 83 3961 3600 2515 -325 157 -153 C ATOM 655 O THR A 83 -41.060 120.482 -1.600 1.00 25.67 O ANISOU 655 O THR A 83 3804 3554 2394 -287 147 -114 O ATOM 656 CB THR A 83 -39.434 117.720 -2.848 1.00 27.68 C ANISOU 656 CB THR A 83 4220 3593 2703 -243 165 -212 C ATOM 657 OG1 THR A 83 -38.735 117.960 -1.623 1.00 27.73 O ANISOU 657 OG1 THR A 83 4238 3577 2719 -174 155 -148 O ATOM 658 CG2 THR A 83 -38.423 117.327 -3.928 1.00 28.20 C ANISOU 658 CG2 THR A 83 4299 3636 2778 -188 169 -278 C ATOM 659 N ALA A 84 -42.110 118.493 -1.767 1.00 27.25 N ANISOU 659 N ALA A 84 4094 3643 2618 -406 177 -150 N ATOM 660 CA ALA A 84 -43.061 118.782 -0.670 1.00 27.52 C ANISOU 660 CA ALA A 84 4106 3706 2643 -456 193 -101 C ATOM 661 C ALA A 84 -42.413 119.212 0.655 1.00 27.37 C ANISOU 661 C ALA A 84 4109 3675 2616 -390 194 -34 C ATOM 662 O ALA A 84 -42.998 119.996 1.405 1.00 26.99 O ANISOU 662 O ALA A 84 4015 3691 2548 -402 203 -2 O ATOM 663 CB ALA A 84 -44.024 117.625 -0.442 1.00 28.47 C ANISOU 663 CB ALA A 84 4276 3764 2777 -564 225 -108 C ATOM 664 N ALA A 85 -41.206 118.715 0.937 1.00 27.80 N ANISOU 664 N ALA A 85 4228 3651 2683 -315 182 -17 N ATOM 665 CA ALA A 85 -40.415 119.156 2.099 1.00 27.36 C ANISOU 665 CA ALA A 85 4188 3592 2614 -241 168 40 C ATOM 666 C ALA A 85 -40.031 120.639 2.103 1.00 26.21 C ANISOU 666 C ALA A 85 3958 3548 2453 -189 146 41 C ATOM 667 O ALA A 85 -39.684 121.174 3.151 1.00 26.22 O ANISOU 667 O ALA A 85 3961 3567 2435 -150 136 82 O ATOM 668 CB ALA A 85 -39.154 118.308 2.223 1.00 28.11 C ANISOU 668 CB ALA A 85 4357 3592 2733 -161 148 46 C ATOM 669 N ASP A 86 -40.067 121.301 0.946 1.00 25.39 N ANISOU 669 N ASP A 86 3789 3506 2352 -189 138 -4 N ATOM 670 CA ASP A 86 -39.822 122.743 0.863 1.00 24.37 C ANISOU 670 CA ASP A 86 3590 3462 2209 -152 122 -2 C ATOM 671 C ASP A 86 -41.079 123.587 1.126 1.00 23.97 C ANISOU 671 C ASP A 86 3486 3482 2139 -198 131 8 C ATOM 672 O ASP A 86 -41.030 124.826 1.016 1.00 23.07 O ANISOU 672 O ASP A 86 3320 3430 2016 -169 117 10 O ATOM 673 CB ASP A 86 -39.221 123.083 -0.510 1.00 24.31 C ANISOU 673 CB ASP A 86 3549 3483 2206 -130 111 -46 C ATOM 674 CG ASP A 86 -37.864 122.430 -0.734 1.00 24.77 C ANISOU 674 CG ASP A 86 3639 3487 2285 -70 108 -64 C ATOM 675 OD1 ASP A 86 -36.943 122.684 0.075 1.00 24.58 O ANISOU 675 OD1 ASP A 86 3615 3455 2268 -12 93 -39 O ATOM 676 OD2 ASP A 86 -37.690 121.671 -1.727 1.00 25.28 O ANISOU 676 OD2 ASP A 86 3724 3522 2359 -78 118 -111 O ATOM 677 N THR A 87 -42.205 122.931 1.431 1.00 23.99 N ANISOU 677 N THR A 87 3499 3475 2140 -269 156 11 N ATOM 678 CA THR A 87 -43.434 123.641 1.802 1.00 23.89 C ANISOU 678 CA THR A 87 3426 3536 2115 -307 170 16 C ATOM 679 C THR A 87 -43.191 124.379 3.120 1.00 23.42 C ANISOU 679 C THR A 87 3371 3493 2036 -267 177 55 C ATOM 680 O THR A 87 -42.832 123.771 4.125 1.00 23.53 O ANISOU 680 O THR A 87 3449 3456 2037 -265 191 90 O ATOM 681 CB THR A 87 -44.638 122.676 1.901 1.00 24.76 C ANISOU 681 CB THR A 87 3541 3635 2231 -404 204 6 C ATOM 682 OG1 THR A 87 -44.951 122.193 0.582 1.00 24.95 O ANISOU 682 OG1 THR A 87 3549 3662 2269 -444 189 -43 O ATOM 683 CG2 THR A 87 -45.874 123.355 2.507 1.00 24.95 C ANISOU 683 CG2 THR A 87 3493 3742 2245 -439 228 10 C ATOM 684 N ALA A 88 -43.339 125.695 3.083 1.00 22.77 N ANISOU 684 N ALA A 88 3228 3476 1947 -230 164 49 N ATOM 685 CA ALA A 88 -42.990 126.519 4.213 1.00 22.72 C ANISOU 685 CA ALA A 88 3227 3485 1921 -187 166 73 C ATOM 686 C ALA A 88 -43.493 127.937 4.029 1.00 22.54 C ANISOU 686 C ALA A 88 3136 3529 1899 -159 157 56 C ATOM 687 O ALA A 88 -43.837 128.349 2.916 1.00 21.99 O ANISOU 687 O ALA A 88 3022 3489 1845 -158 138 34 O ATOM 688 CB ALA A 88 -41.474 126.514 4.420 1.00 22.29 C ANISOU 688 CB ALA A 88 3217 3386 1865 -129 137 87 C ATOM 689 N VAL A 89 -43.560 128.661 5.146 1.00 22.73 N ANISOU 689 N VAL A 89 3161 3574 1903 -135 170 66 N ATOM 690 CA VAL A 89 -43.703 130.117 5.116 1.00 22.60 C ANISOU 690 CA VAL A 89 3102 3597 1890 -89 157 50 C ATOM 691 C VAL A 89 -42.311 130.671 4.855 1.00 22.36 C ANISOU 691 C VAL A 89 3097 3533 1864 -44 120 54 C ATOM 692 O VAL A 89 -41.392 130.360 5.605 1.00 22.14 O ANISOU 692 O VAL A 89 3114 3476 1821 -32 114 69 O ATOM 693 CB VAL A 89 -44.255 130.673 6.437 1.00 22.99 C ANISOU 693 CB VAL A 89 3146 3676 1913 -80 189 48 C ATOM 694 CG1 VAL A 89 -44.243 132.196 6.425 1.00 23.05 C ANISOU 694 CG1 VAL A 89 3124 3704 1929 -23 173 27 C ATOM 695 CG2 VAL A 89 -45.677 130.160 6.665 1.00 23.53 C ANISOU 695 CG2 VAL A 89 3172 3790 1979 -131 236 38 C ATOM 696 N TYR A 90 -42.176 131.475 3.791 1.00 22.26 N ANISOU 696 N TYR A 90 3057 3530 1870 -24 96 43 N ATOM 697 CA TYR A 90 -40.917 132.114 3.426 1.00 22.04 C ANISOU 697 CA TYR A 90 3047 3480 1850 5 70 44 C ATOM 698 C TYR A 90 -40.959 133.580 3.821 1.00 22.50 C ANISOU 698 C TYR A 90 3096 3545 1908 38 63 37 C ATOM 699 O TYR A 90 -41.857 134.313 3.392 1.00 22.73 O ANISOU 699 O TYR A 90 3097 3594 1946 52 61 31 O ATOM 700 CB TYR A 90 -40.650 131.969 1.919 1.00 21.74 C ANISOU 700 CB TYR A 90 2998 3439 1822 -5 56 40 C ATOM 701 CG TYR A 90 -40.240 130.560 1.544 1.00 21.74 C ANISOU 701 CG TYR A 90 3020 3417 1825 -29 62 37 C ATOM 702 CD1 TYR A 90 -41.186 129.555 1.426 1.00 21.85 C ANISOU 702 CD1 TYR A 90 3031 3433 1837 -67 76 32 C ATOM 703 CD2 TYR A 90 -38.903 130.232 1.331 1.00 21.62 C ANISOU 703 CD2 TYR A 90 3024 3375 1817 -14 55 33 C ATOM 704 CE1 TYR A 90 -40.814 128.259 1.107 1.00 22.03 C ANISOU 704 CE1 TYR A 90 3086 3419 1865 -88 83 24 C ATOM 705 CE2 TYR A 90 -38.517 128.937 1.004 1.00 21.82 C ANISOU 705 CE2 TYR A 90 3072 3370 1849 -23 61 24 C ATOM 706 CZ TYR A 90 -39.479 127.950 0.899 1.00 21.94 C ANISOU 706 CZ TYR A 90 3099 3374 1862 -60 75 21 C ATOM 707 OH TYR A 90 -39.102 126.663 0.592 1.00 22.33 O ANISOU 707 OH TYR A 90 3184 3378 1922 -69 82 8 O ATOM 708 N TYR A 91 -40.000 133.982 4.660 1.00 22.47 N ANISOU 708 N TYR A 91 3118 3523 1897 52 55 34 N ATOM 709 CA TYR A 91 -39.877 135.352 5.131 1.00 22.83 C ANISOU 709 CA TYR A 91 3168 3561 1943 77 48 20 C ATOM 710 C TYR A 91 -38.657 136.002 4.521 1.00 23.32 C ANISOU 710 C TYR A 91 3240 3598 2022 74 26 18 C ATOM 711 O TYR A 91 -37.588 135.372 4.448 1.00 23.81 O ANISOU 711 O TYR A 91 3305 3656 2086 62 16 21 O ATOM 712 CB TYR A 91 -39.671 135.378 6.641 1.00 22.89 C ANISOU 712 CB TYR A 91 3201 3573 1922 83 54 8 C ATOM 713 CG TYR A 91 -40.801 134.877 7.495 1.00 22.67 C ANISOU 713 CG TYR A 91 3171 3575 1867 78 88 8 C ATOM 714 CD1 TYR A 91 -41.893 135.695 7.775 1.00 23.00 C ANISOU 714 CD1 TYR A 91 3190 3639 1910 98 111 -15 C ATOM 715 CD2 TYR A 91 -40.769 133.604 8.058 1.00 22.55 C ANISOU 715 CD2 TYR A 91 3179 3563 1825 53 100 30 C ATOM 716 CE1 TYR A 91 -42.913 135.269 8.596 1.00 23.31 C ANISOU 716 CE1 TYR A 91 3217 3716 1923 87 153 -21 C ATOM 717 CE2 TYR A 91 -41.790 133.161 8.873 1.00 23.03 C ANISOU 717 CE2 TYR A 91 3242 3652 1855 35 141 32 C ATOM 718 CZ TYR A 91 -42.856 133.995 9.150 1.00 23.42 C ANISOU 718 CZ TYR A 91 3257 3736 1904 48 172 4 C ATOM 719 OH TYR A 91 -43.870 133.552 9.961 1.00 23.90 O ANISOU 719 OH TYR A 91 3312 3836 1934 24 223 2 O ATOM 720 N CYS A 92 -38.794 137.256 4.106 1.00 23.30 N ANISOU 720 N CYS A 92 3242 3578 2033 86 20 14 N ATOM 721 CA CYS A 92 -37.639 138.097 3.875 1.00 23.44 C ANISOU 721 CA CYS A 92 3276 3566 2064 72 7 9 C ATOM 722 C CYS A 92 -37.407 138.928 5.121 1.00 23.20 C ANISOU 722 C CYS A 92 3267 3521 2029 81 1 -20 C ATOM 723 O CYS A 92 -38.329 139.173 5.898 1.00 22.80 O ANISOU 723 O CYS A 92 3222 3476 1966 108 12 -34 O ATOM 724 CB CYS A 92 -37.771 138.949 2.604 1.00 24.16 C ANISOU 724 CB CYS A 92 3378 3634 2169 69 4 28 C ATOM 725 SG CYS A 92 -39.105 140.163 2.485 1.00 25.97 S ANISOU 725 SG CYS A 92 3624 3838 2407 115 -2 33 S ATOM 726 N ALA A 93 -36.158 139.342 5.311 1.00 23.01 N ANISOU 726 N ALA A 93 3249 3482 2012 55 -14 -35 N ATOM 727 CA ALA A 93 -35.776 140.139 6.459 1.00 23.22 C ANISOU 727 CA ALA A 93 3298 3495 2031 53 -26 -72 C ATOM 728 C ALA A 93 -34.502 140.915 6.190 1.00 23.39 C ANISOU 728 C ALA A 93 3320 3491 2074 10 -40 -88 C ATOM 729 O ALA A 93 -33.640 140.468 5.437 1.00 22.96 O ANISOU 729 O ALA A 93 3237 3453 2035 -17 -41 -75 O ATOM 730 CB ALA A 93 -35.595 139.253 7.686 1.00 23.13 C ANISOU 730 CB ALA A 93 3283 3522 1983 63 -37 -83 C ATOM 731 N ARG A 94 -34.410 142.099 6.794 1.00 23.85 N ANISOU 731 N ARG A 94 3413 3512 2138 1 -46 -122 N ATOM 732 CA ARG A 94 -33.178 142.871 6.746 1.00 24.56 C ANISOU 732 CA ARG A 94 3503 3579 2249 -55 -59 -147 C ATOM 733 C ARG A 94 -32.290 142.337 7.859 1.00 24.68 C ANISOU 733 C ARG A 94 3490 3645 2242 -66 -92 -183 C ATOM 734 O ARG A 94 -32.766 142.059 8.959 1.00 24.04 O ANISOU 734 O ARG A 94 3425 3585 2123 -33 -104 -200 O ATOM 735 CB ARG A 94 -33.443 144.362 6.936 1.00 25.59 C ANISOU 735 CB ARG A 94 3691 3635 2396 -66 -55 -174 C ATOM 736 CG ARG A 94 -32.198 145.225 6.761 1.00 26.55 C ANISOU 736 CG ARG A 94 3818 3723 2545 -143 -62 -199 C ATOM 737 CD ARG A 94 -32.490 146.691 6.993 1.00 27.59 C ANISOU 737 CD ARG A 94 4023 3763 2695 -154 -58 -227 C ATOM 738 NE ARG A 94 -32.573 147.018 8.417 1.00 28.20 N ANISOU 738 NE ARG A 94 4121 3842 2750 -141 -78 -293 N ATOM 739 CZ ARG A 94 -32.592 148.249 8.931 1.00 29.55 C ANISOU 739 CZ ARG A 94 4355 3938 2934 -159 -80 -343 C ATOM 740 NH1 ARG A 94 -32.672 148.409 10.243 1.00 30.27 N ANISOU 740 NH1 ARG A 94 4463 4046 2992 -145 -97 -408 N ATOM 741 NH2 ARG A 94 -32.546 149.319 8.157 1.00 30.33 N ANISOU 741 NH2 ARG A 94 4510 3940 3074 -190 -64 -329 N ATOM 742 N HIS A 95 -31.012 142.164 7.548 1.00 25.07 N ANISOU 742 N HIS A 95 3494 3721 2312 -109 -107 -192 N ATOM 743 CA HIS A 95 -30.034 141.751 8.538 1.00 25.76 C ANISOU 743 CA HIS A 95 3546 3861 2382 -116 -152 -227 C ATOM 744 C HIS A 95 -29.005 142.864 8.675 1.00 26.62 C ANISOU 744 C HIS A 95 3642 3954 2516 -187 -167 -277 C ATOM 745 O HIS A 95 -28.340 143.218 7.696 1.00 26.95 O ANISOU 745 O HIS A 95 3656 3985 2598 -240 -145 -271 O ATOM 746 CB HIS A 95 -29.370 140.440 8.134 1.00 25.54 C ANISOU 746 CB HIS A 95 3456 3889 2360 -97 -163 -204 C ATOM 747 CG HIS A 95 -28.346 139.971 9.115 1.00 26.18 C ANISOU 747 CG HIS A 95 3495 4027 2426 -89 -219 -235 C ATOM 748 ND1 HIS A 95 -28.664 139.185 10.198 1.00 26.33 N ANISOU 748 ND1 HIS A 95 3538 4074 2394 -37 -253 -227 N ATOM 749 CD2 HIS A 95 -27.019 140.218 9.208 1.00 27.04 C ANISOU 749 CD2 HIS A 95 3540 4176 2559 -128 -252 -275 C ATOM 750 CE1 HIS A 95 -27.580 138.955 10.910 1.00 27.05 C ANISOU 750 CE1 HIS A 95 3586 4216 2475 -35 -313 -256 C ATOM 751 NE2 HIS A 95 -26.567 139.569 10.331 1.00 27.26 N ANISOU 751 NE2 HIS A 95 3551 4256 2551 -89 -315 -290 N ATOM 752 N ARG A 96 -28.906 143.422 9.877 1.00 27.31 N ANISOU 752 N ARG A 96 3757 4042 2577 -195 -201 -327 N ATOM 753 CA ARG A 96 -28.027 144.554 10.173 1.00 28.50 C ANISOU 753 CA ARG A 96 3907 4173 2750 -272 -220 -387 C ATOM 754 C ARG A 96 -27.421 144.388 11.566 1.00 28.80 C ANISOU 754 C ARG A 96 3927 4271 2744 -271 -285 -442 C ATOM 755 O ARG A 96 -28.133 144.072 12.514 1.00 27.75 O ANISOU 755 O ARG A 96 3838 4152 2555 -217 -299 -446 O ATOM 756 CB ARG A 96 -28.823 145.857 10.119 1.00 29.66 C ANISOU 756 CB ARG A 96 4140 4222 2909 -287 -189 -402 C ATOM 757 CG ARG A 96 -28.039 147.119 10.471 1.00 31.31 C ANISOU 757 CG ARG A 96 4369 4386 3140 -373 -204 -468 C ATOM 758 CD ARG A 96 -28.934 148.347 10.455 1.00 32.28 C ANISOU 758 CD ARG A 96 4593 4397 3276 -370 -174 -482 C ATOM 759 NE ARG A 96 -29.632 148.482 11.728 1.00 33.41 N ANISOU 759 NE ARG A 96 4782 4542 3369 -318 -192 -531 N ATOM 760 CZ ARG A 96 -29.235 149.219 12.769 1.00 34.41 C ANISOU 760 CZ ARG A 96 4942 4657 3477 -357 -222 -614 C ATOM 761 NH1 ARG A 96 -28.133 149.961 12.727 1.00 35.54 N ANISOU 761 NH1 ARG A 96 5073 4777 3653 -457 -242 -662 N ATOM 762 NH2 ARG A 96 -29.973 149.226 13.871 1.00 35.12 N ANISOU 762 NH2 ARG A 96 5076 4759 3510 -301 -229 -654 N ATOM 763 N ASN A 97 -26.119 144.644 11.680 1.00 29.48 N ANISOU 763 N ASN A 97 3949 4397 2853 -335 -322 -488 N ATOM 764 CA ASN A 97 -25.397 144.514 12.952 1.00 30.48 C ANISOU 764 CA ASN A 97 4049 4593 2937 -339 -398 -545 C ATOM 765 C ASN A 97 -25.697 143.197 13.686 1.00 29.57 C ANISOU 765 C ASN A 97 3933 4544 2760 -247 -437 -509 C ATOM 766 O ASN A 97 -26.014 143.188 14.875 1.00 29.38 O ANISOU 766 O ASN A 97 3956 4540 2665 -220 -474 -534 O ATOM 767 CB ASN A 97 -25.671 145.732 13.851 1.00 31.79 C ANISOU 767 CB ASN A 97 4290 4711 3077 -380 -410 -614 C ATOM 768 CG ASN A 97 -25.239 147.048 13.207 1.00 33.12 C ANISOU 768 CG ASN A 97 4471 4804 3310 -481 -379 -652 C ATOM 769 OD1 ASN A 97 -24.479 147.068 12.230 1.00 33.92 O ANISOU 769 OD1 ASN A 97 4507 4912 3469 -537 -358 -636 O ATOM 770 ND2 ASN A 97 -25.724 148.154 13.751 1.00 34.01 N ANISOU 770 ND2 ASN A 97 4671 4840 3411 -507 -371 -704 N ATOM 771 N TRP A 98 -25.604 142.096 12.935 1.00 28.80 N ANISOU 771 N TRP A 98 3786 4472 2685 -202 -423 -450 N ATOM 772 CA TRP A 98 -25.635 140.720 13.469 1.00 28.77 C ANISOU 772 CA TRP A 98 3773 4523 2635 -120 -463 -410 C ATOM 773 C TRP A 98 -26.998 140.270 14.007 1.00 28.38 C ANISOU 773 C TRP A 98 3815 4445 2523 -64 -436 -368 C ATOM 774 O TRP A 98 -27.083 139.390 14.869 1.00 28.25 O ANISOU 774 O TRP A 98 3822 4467 2446 -11 -475 -345 O ATOM 775 CB TRP A 98 -24.528 140.524 14.519 1.00 29.79 C ANISOU 775 CB TRP A 98 3854 4734 2731 -115 -558 -454 C ATOM 776 CG TRP A 98 -23.175 141.023 14.065 1.00 30.74 C ANISOU 776 CG TRP A 98 3868 4896 2916 -181 -584 -507 C ATOM 777 CD1 TRP A 98 -22.631 142.266 14.288 1.00 31.58 C ANISOU 777 CD1 TRP A 98 3960 4999 3041 -273 -597 -581 C ATOM 778 CD2 TRP A 98 -22.204 140.292 13.306 1.00 31.01 C ANISOU 778 CD2 TRP A 98 3793 4982 3007 -164 -594 -497 C ATOM 779 NE1 TRP A 98 -21.378 142.342 13.722 1.00 32.30 N ANISOU 779 NE1 TRP A 98 3933 5144 3197 -323 -613 -614 N ATOM 780 CE2 TRP A 98 -21.093 141.150 13.106 1.00 31.95 C ANISOU 780 CE2 TRP A 98 3824 5138 3177 -253 -609 -566 C ATOM 781 CE3 TRP A 98 -22.153 138.990 12.792 1.00 30.70 C ANISOU 781 CE3 TRP A 98 3720 4960 2983 -83 -589 -443 C ATOM 782 CZ2 TRP A 98 -19.946 140.747 12.405 1.00 32.34 C ANISOU 782 CZ2 TRP A 98 3742 5254 3291 -262 -615 -583 C ATOM 783 CZ3 TRP A 98 -21.015 138.592 12.081 1.00 31.33 C ANISOU 783 CZ3 TRP A 98 3679 5098 3128 -82 -596 -462 C ATOM 784 CH2 TRP A 98 -19.923 139.471 11.906 1.00 32.12 C ANISOU 784 CH2 TRP A 98 3682 5246 3276 -170 -608 -532 C ATOM 785 N LEU A 99 -28.063 140.857 13.468 1.00 27.96 N ANISOU 785 N LEU A 99 3811 4325 2486 -75 -367 -355 N ATOM 786 CA LEU A 99 -29.413 140.494 13.851 1.00 27.62 C ANISOU 786 CA LEU A 99 3837 4262 2395 -30 -329 -322 C ATOM 787 C LEU A 99 -30.385 140.746 12.698 1.00 26.94 C ANISOU 787 C LEU A 99 3763 4116 2356 -29 -258 -289 C ATOM 788 O LEU A 99 -30.096 141.528 11.803 1.00 26.20 O ANISOU 788 O LEU A 99 3652 3984 2319 -69 -239 -300 O ATOM 789 CB LEU A 99 -29.815 141.261 15.112 1.00 28.73 C ANISOU 789 CB LEU A 99 4041 4404 2472 -36 -341 -373 C ATOM 790 CG LEU A 99 -30.437 142.652 14.962 1.00 29.21 C ANISOU 790 CG LEU A 99 4144 4399 2557 -66 -298 -419 C ATOM 791 CD1 LEU A 99 -31.918 142.532 15.255 1.00 29.27 C ANISOU 791 CD1 LEU A 99 4206 4388 2528 -19 -242 -400 C ATOM 792 CD2 LEU A 99 -29.818 143.673 15.892 1.00 30.39 C ANISOU 792 CD2 LEU A 99 4317 4551 2680 -110 -340 -502 C ATOM 793 N PHE A 100 -31.527 140.073 12.761 1.00 26.34 N ANISOU 793 N PHE A 100 3719 4036 2252 13 -223 -248 N ATOM 794 CA PHE A 100 -32.590 140.180 11.762 1.00 26.15 C ANISOU 794 CA PHE A 100 3703 3971 2264 23 -165 -217 C ATOM 795 C PHE A 100 -33.712 141.070 12.308 1.00 27.00 C ANISOU 795 C PHE A 100 3859 4050 2349 36 -132 -246 C ATOM 796 O PHE A 100 -34.471 140.632 13.160 1.00 26.76 O ANISOU 796 O PHE A 100 3857 4047 2265 63 -117 -243 O ATOM 797 CB PHE A 100 -33.107 138.779 11.445 1.00 25.22 C ANISOU 797 CB PHE A 100 3575 3872 2135 55 -149 -161 C ATOM 798 CG PHE A 100 -32.060 137.858 10.874 1.00 25.25 C ANISOU 798 CG PHE A 100 3533 3896 2165 56 -177 -138 C ATOM 799 CD1 PHE A 100 -31.858 137.775 9.492 1.00 24.86 C ANISOU 799 CD1 PHE A 100 3448 3830 2170 42 -154 -121 C ATOM 800 CD2 PHE A 100 -31.288 137.058 11.701 1.00 25.48 C ANISOU 800 CD2 PHE A 100 3558 3964 2161 77 -226 -134 C ATOM 801 CE1 PHE A 100 -30.897 136.921 8.967 1.00 24.84 C ANISOU 801 CE1 PHE A 100 3399 3848 2191 49 -172 -111 C ATOM 802 CE2 PHE A 100 -30.312 136.210 11.179 1.00 25.64 C ANISOU 802 CE2 PHE A 100 3529 4000 2211 93 -253 -120 C ATOM 803 CZ PHE A 100 -30.123 136.137 9.810 1.00 25.18 C ANISOU 803 CZ PHE A 100 3430 3926 2212 78 -221 -112 C ATOM 804 N ASP A 101 -33.810 142.318 11.841 1.00 28.76 N ANISOU 804 N ASP A 101 4098 4217 2613 19 -118 -274 N ATOM 805 CA ASP A 101 -34.603 143.348 12.570 1.00 30.27 C ANISOU 805 CA ASP A 101 4340 4377 2786 36 -97 -323 C ATOM 806 C ASP A 101 -35.985 143.701 12.007 1.00 31.34 C ANISOU 806 C ASP A 101 4486 4476 2946 81 -49 -307 C ATOM 807 O ASP A 101 -36.892 144.005 12.795 1.00 33.34 O ANISOU 807 O ASP A 101 4764 4735 3168 116 -22 -341 O ATOM 808 CB ASP A 101 -33.785 144.625 12.839 1.00 31.43 C ANISOU 808 CB ASP A 101 4514 4476 2951 -8 -122 -384 C ATOM 809 CG ASP A 101 -33.255 145.288 11.587 1.00 31.68 C ANISOU 809 CG ASP A 101 4537 4448 3053 -49 -118 -367 C ATOM 810 OD1 ASP A 101 -33.478 144.804 10.457 1.00 31.47 O ANISOU 810 OD1 ASP A 101 4481 4419 3056 -39 -100 -308 O ATOM 811 OD2 ASP A 101 -32.579 146.326 11.739 1.00 32.95 O ANISOU 811 OD2 ASP A 101 4723 4562 3235 -98 -133 -414 O ATOM 812 N TYR A 102 -36.141 143.704 10.684 1.00 31.34 N ANISOU 812 N TYR A 102 4464 4447 2996 81 -39 -262 N ATOM 813 CA TYR A 102 -37.427 143.995 10.040 1.00 31.23 C ANISOU 813 CA TYR A 102 4451 4408 3008 129 -7 -243 C ATOM 814 C TYR A 102 -37.789 142.820 9.146 1.00 29.52 C ANISOU 814 C TYR A 102 4187 4232 2795 134 0 -183 C ATOM 815 O TYR A 102 -37.100 142.578 8.152 1.00 30.07 O ANISOU 815 O TYR A 102 4242 4294 2890 104 -13 -150 O ATOM 816 CB TYR A 102 -37.345 145.286 9.207 1.00 32.45 C ANISOU 816 CB TYR A 102 4641 4476 3213 127 -11 -244 C ATOM 817 CG TYR A 102 -37.339 146.554 10.042 1.00 34.29 C ANISOU 817 CG TYR A 102 4931 4650 3450 134 -11 -310 C ATOM 818 CD1 TYR A 102 -38.532 147.146 10.460 1.00 35.46 C ANISOU 818 CD1 TYR A 102 5099 4774 3599 204 15 -342 C ATOM 819 CD2 TYR A 102 -36.140 147.152 10.428 1.00 35.08 C ANISOU 819 CD2 TYR A 102 5060 4717 3552 72 -35 -349 C ATOM 820 CE1 TYR A 102 -38.535 148.307 11.230 1.00 36.60 C ANISOU 820 CE1 TYR A 102 5303 4856 3746 216 19 -412 C ATOM 821 CE2 TYR A 102 -36.128 148.303 11.206 1.00 36.58 C ANISOU 821 CE2 TYR A 102 5309 4846 3743 71 -35 -418 C ATOM 822 CZ TYR A 102 -37.326 148.882 11.597 1.00 37.30 C ANISOU 822 CZ TYR A 102 5432 4905 3835 146 -7 -450 C ATOM 823 OH TYR A 102 -37.315 150.025 12.360 1.00 39.12 O ANISOU 823 OH TYR A 102 5728 5067 4069 151 -5 -528 O ATOM 824 N TRP A 103 -38.846 142.090 9.507 1.00 27.24 N ANISOU 824 N TRP A 103 3878 3990 2483 165 26 -175 N ATOM 825 CA TRP A 103 -39.271 140.892 8.791 1.00 25.86 C ANISOU 825 CA TRP A 103 3662 3853 2309 161 35 -128 C ATOM 826 C TRP A 103 -40.545 141.194 8.009 1.00 25.50 C ANISOU 826 C TRP A 103 3592 3806 2292 200 52 -116 C ATOM 827 O TRP A 103 -41.397 141.946 8.482 1.00 25.65 O ANISOU 827 O TRP A 103 3614 3819 2314 242 70 -148 O ATOM 828 CB TRP A 103 -39.584 139.752 9.771 1.00 25.57 C ANISOU 828 CB TRP A 103 3620 3872 2224 155 53 -125 C ATOM 829 CG TRP A 103 -38.429 139.228 10.583 1.00 25.19 C ANISOU 829 CG TRP A 103 3595 3837 2139 129 26 -127 C ATOM 830 CD1 TRP A 103 -37.679 139.920 11.482 1.00 25.26 C ANISOU 830 CD1 TRP A 103 3635 3839 2124 123 3 -166 C ATOM 831 CD2 TRP A 103 -37.923 137.889 10.577 1.00 24.61 C ANISOU 831 CD2 TRP A 103 3515 3786 2047 113 13 -89 C ATOM 832 NE1 TRP A 103 -36.725 139.093 12.043 1.00 25.29 N ANISOU 832 NE1 TRP A 103 3645 3870 2094 106 -29 -154 N ATOM 833 CE2 TRP A 103 -36.863 137.837 11.511 1.00 24.80 C ANISOU 833 CE2 TRP A 103 3564 3822 2037 105 -23 -104 C ATOM 834 CE3 TRP A 103 -38.279 136.717 9.891 1.00 24.03 C ANISOU 834 CE3 TRP A 103 3423 3723 1986 105 26 -49 C ATOM 835 CZ2 TRP A 103 -36.146 136.666 11.761 1.00 24.59 C ANISOU 835 CZ2 TRP A 103 3542 3812 1989 103 -50 -73 C ATOM 836 CZ3 TRP A 103 -37.562 135.552 10.138 1.00 24.07 C ANISOU 836 CZ3 TRP A 103 3440 3734 1972 97 6 -22 C ATOM 837 CH2 TRP A 103 -36.508 135.532 11.068 1.00 24.17 C ANISOU 837 CH2 TRP A 103 3476 3755 1951 102 -33 -31 C ATOM 838 N GLY A 104 -40.676 140.609 6.823 1.00 24.73 N ANISOU 838 N GLY A 104 3468 3718 2212 189 44 -76 N ATOM 839 CA GLY A 104 -41.957 140.620 6.117 1.00 24.72 C ANISOU 839 CA GLY A 104 3429 3736 2228 224 51 -64 C ATOM 840 C GLY A 104 -42.973 139.740 6.818 1.00 24.68 C ANISOU 840 C GLY A 104 3383 3793 2202 226 85 -75 C ATOM 841 O GLY A 104 -42.632 138.988 7.738 1.00 24.73 O ANISOU 841 O GLY A 104 3402 3821 2174 196 102 -80 O ATOM 842 N GLN A 105 -44.223 139.849 6.400 1.00 24.97 N ANISOU 842 N GLN A 105 3370 3860 2257 259 93 -79 N ATOM 843 CA GLN A 105 -45.310 139.035 6.958 1.00 25.22 C ANISOU 843 CA GLN A 105 3349 3960 2274 250 133 -93 C ATOM 844 C GLN A 105 -45.215 137.554 6.606 1.00 24.97 C ANISOU 844 C GLN A 105 3304 3957 2228 187 138 -63 C ATOM 845 O GLN A 105 -45.817 136.710 7.277 1.00 24.91 O ANISOU 845 O GLN A 105 3274 3992 2198 156 178 -68 O ATOM 846 CB GLN A 105 -46.672 139.580 6.515 1.00 25.81 C ANISOU 846 CB GLN A 105 3357 4070 2380 305 135 -111 C ATOM 847 CG GLN A 105 -47.129 140.740 7.385 1.00 26.47 C ANISOU 847 CG GLN A 105 3443 4142 2471 371 157 -159 C ATOM 848 CD GLN A 105 -48.255 141.537 6.779 1.00 27.05 C ANISOU 848 CD GLN A 105 3460 4231 2589 450 141 -175 C ATOM 849 OE1 GLN A 105 -48.289 142.767 6.901 1.00 27.50 O ANISOU 849 OE1 GLN A 105 3545 4235 2668 520 129 -198 O ATOM 850 NE2 GLN A 105 -49.172 140.858 6.112 1.00 27.18 N ANISOU 850 NE2 GLN A 105 3396 4315 2618 443 135 -165 N ATOM 851 N GLY A 106 -44.485 137.249 5.541 1.00 24.45 N ANISOU 851 N GLY A 106 3254 3863 2172 167 103 -33 N ATOM 852 CA GLY A 106 -44.264 135.883 5.129 1.00 24.30 C ANISOU 852 CA GLY A 106 3235 3855 2144 114 105 -11 C ATOM 853 C GLY A 106 -45.303 135.486 4.100 1.00 24.89 C ANISOU 853 C GLY A 106 3253 3969 2235 104 96 -9 C ATOM 854 O GLY A 106 -46.377 136.080 4.018 1.00 24.71 O ANISOU 854 O GLY A 106 3178 3982 2227 139 97 -27 O ATOM 855 N THR A 107 -44.949 134.493 3.299 1.00 25.08 N ANISOU 855 N THR A 107 3286 3988 2257 62 85 6 N ATOM 856 CA THR A 107 -45.848 133.940 2.302 1.00 26.10 C ANISOU 856 CA THR A 107 3367 4157 2394 38 72 2 C ATOM 857 C THR A 107 -45.729 132.414 2.363 1.00 25.87 C ANISOU 857 C THR A 107 3353 4121 2355 -29 94 4 C ATOM 858 O THR A 107 -44.630 131.864 2.279 1.00 25.26 O ANISOU 858 O THR A 107 3329 3998 2271 -43 90 17 O ATOM 859 CB THR A 107 -45.548 134.518 0.886 1.00 26.55 C ANISOU 859 CB THR A 107 3430 4205 2453 61 24 15 C ATOM 860 OG1 THR A 107 -46.314 133.823 -0.107 1.00 28.41 O ANISOU 860 OG1 THR A 107 3625 4483 2685 31 5 6 O ATOM 861 CG2 THR A 107 -44.090 134.407 0.534 1.00 26.65 C ANISOU 861 CG2 THR A 107 3505 4166 2455 49 18 31 C ATOM 862 N LEU A 108 -46.861 131.745 2.549 1.00 26.41 N ANISOU 862 N LEU A 108 3373 4233 2428 -71 118 -12 N ATOM 863 CA LEU A 108 -46.887 130.287 2.535 1.00 26.38 C ANISOU 863 CA LEU A 108 3391 4213 2419 -144 140 -11 C ATOM 864 C LEU A 108 -46.666 129.841 1.116 1.00 25.84 C ANISOU 864 C LEU A 108 3326 4137 2355 -162 102 -19 C ATOM 865 O LEU A 108 -47.370 130.288 0.216 1.00 26.14 O ANISOU 865 O LEU A 108 3311 4224 2398 -152 70 -34 O ATOM 866 CB LEU A 108 -48.230 129.734 3.027 1.00 27.22 C ANISOU 866 CB LEU A 108 3439 4373 2531 -200 180 -29 C ATOM 867 CG LEU A 108 -48.363 128.202 2.990 1.00 27.57 C ANISOU 867 CG LEU A 108 3514 4388 2573 -290 206 -29 C ATOM 868 CD1 LEU A 108 -47.285 127.536 3.829 1.00 27.47 C ANISOU 868 CD1 LEU A 108 3600 4296 2540 -296 227 6 C ATOM 869 CD2 LEU A 108 -49.745 127.779 3.454 1.00 28.49 C ANISOU 869 CD2 LEU A 108 3562 4567 2697 -358 252 -50 C ATOM 870 N VAL A 109 -45.670 128.985 0.909 1.00 25.19 N ANISOU 870 N VAL A 109 3309 3996 2267 -182 104 -11 N ATOM 871 CA VAL A 109 -45.482 128.335 -0.391 1.00 24.91 C ANISOU 871 CA VAL A 109 3283 3951 2229 -210 80 -29 C ATOM 872 C VAL A 109 -45.694 126.850 -0.181 1.00 24.95 C ANISOU 872 C VAL A 109 3320 3919 2241 -280 108 -41 C ATOM 873 O VAL A 109 -45.022 126.234 0.649 1.00 24.41 O ANISOU 873 O VAL A 109 3310 3790 2173 -282 132 -20 O ATOM 874 CB VAL A 109 -44.091 128.578 -0.981 1.00 24.51 C ANISOU 874 CB VAL A 109 3281 3861 2171 -171 62 -21 C ATOM 875 CG1 VAL A 109 -43.952 127.879 -2.330 1.00 24.99 C ANISOU 875 CG1 VAL A 109 3355 3920 2220 -201 46 -49 C ATOM 876 CG2 VAL A 109 -43.835 130.068 -1.120 1.00 24.40 C ANISOU 876 CG2 VAL A 109 3251 3870 2152 -113 40 -5 C ATOM 877 N THR A 110 -46.652 126.305 -0.917 1.00 25.06 N ANISOU 877 N THR A 110 3296 3968 2258 -339 100 -73 N ATOM 878 CA THR A 110 -46.937 124.890 -0.914 1.00 25.56 C ANISOU 878 CA THR A 110 3391 3989 2330 -419 125 -91 C ATOM 879 C THR A 110 -46.314 124.315 -2.181 1.00 25.80 C ANISOU 879 C THR A 110 3462 3987 2353 -426 99 -122 C ATOM 880 O THR A 110 -46.519 124.837 -3.281 1.00 25.94 O ANISOU 880 O THR A 110 3442 4059 2353 -413 60 -145 O ATOM 881 CB THR A 110 -48.458 124.655 -0.923 1.00 26.08 C ANISOU 881 CB THR A 110 3380 4123 2407 -494 135 -119 C ATOM 882 OG1 THR A 110 -49.038 125.296 0.220 1.00 25.92 O ANISOU 882 OG1 THR A 110 3314 4144 2389 -479 166 -98 O ATOM 883 CG2 THR A 110 -48.789 123.177 -0.904 1.00 26.82 C ANISOU 883 CG2 THR A 110 3515 4164 2512 -595 165 -140 C ATOM 884 N VAL A 111 -45.549 123.248 -2.018 1.00 26.07 N ANISOU 884 N VAL A 111 3576 3933 2397 -440 120 -124 N ATOM 885 CA VAL A 111 -44.943 122.567 -3.149 1.00 26.42 C ANISOU 885 CA VAL A 111 3663 3939 2435 -446 106 -164 C ATOM 886 C VAL A 111 -45.729 121.308 -3.464 1.00 27.48 C ANISOU 886 C VAL A 111 3818 4042 2581 -542 119 -206 C ATOM 887 O VAL A 111 -45.698 120.339 -2.697 1.00 28.17 O ANISOU 887 O VAL A 111 3965 4048 2690 -580 153 -193 O ATOM 888 CB VAL A 111 -43.488 122.191 -2.875 1.00 26.22 C ANISOU 888 CB VAL A 111 3711 3832 2420 -386 118 -149 C ATOM 889 CG1 VAL A 111 -42.890 121.464 -4.082 1.00 26.37 C ANISOU 889 CG1 VAL A 111 3769 3816 2433 -388 113 -202 C ATOM 890 CG2 VAL A 111 -42.688 123.426 -2.548 1.00 25.55 C ANISOU 890 CG2 VAL A 111 3602 3781 2327 -305 106 -113 C ATOM 891 N SER A 112 -46.449 121.332 -4.581 1.00 28.09 N ANISOU 891 N SER A 112 3850 4181 2641 -586 89 -255 N ATOM 892 CA SER A 112 -47.089 120.143 -5.084 1.00 29.55 C ANISOU 892 CA SER A 112 4057 4337 2835 -684 94 -311 C ATOM 893 C SER A 112 -47.483 120.287 -6.540 1.00 30.40 C ANISOU 893 C SER A 112 4127 4516 2906 -707 46 -371 C ATOM 894 O SER A 112 -48.029 121.315 -6.934 1.00 30.14 O ANISOU 894 O SER A 112 4015 4587 2849 -682 6 -363 O ATOM 895 CB SER A 112 -48.349 119.883 -4.259 1.00 29.98 C ANISOU 895 CB SER A 112 4061 4417 2912 -769 118 -303 C ATOM 896 OG SER A 112 -48.975 118.696 -4.678 1.00 31.22 O ANISOU 896 OG SER A 112 4242 4537 3082 -880 127 -358 O ATOM 897 N SER A 113 -47.250 119.236 -7.323 1.00 31.76 N ANISOU 897 N SER A 113 4362 4631 3072 -754 48 -432 N ATOM 898 CA SER A 113 -47.787 119.163 -8.691 1.00 33.42 C ANISOU 898 CA SER A 113 4545 4913 3241 -799 2 -500 C ATOM 899 C SER A 113 -49.096 118.399 -8.756 1.00 35.33 C ANISOU 899 C SER A 113 4747 5176 3499 -924 -7 -552 C ATOM 900 O SER A 113 -49.509 118.014 -9.846 1.00 36.04 O ANISOU 900 O SER A 113 4832 5305 3557 -980 -44 -623 O ATOM 901 CB SER A 113 -46.801 118.458 -9.631 1.00 33.32 C ANISOU 901 CB SER A 113 4621 4835 3204 -784 10 -556 C ATOM 902 OG SER A 113 -45.487 118.883 -9.382 1.00 32.89 O ANISOU 902 OG SER A 113 4606 4739 3150 -682 34 -515 O ATOM 903 N ALA A 114 -49.718 118.150 -7.604 1.00 38.32 N ANISOU 903 N ALA A 114 5596 5176 3787 -1230 811 296 N ATOM 904 CA ALA A 114 -50.956 117.395 -7.547 1.00 38.65 C ANISOU 904 CA ALA A 114 5707 5257 3720 -1223 742 207 C ATOM 905 C ALA A 114 -52.088 118.127 -8.253 1.00 40.18 C ANISOU 905 C ALA A 114 5999 5505 3763 -1270 613 251 C ATOM 906 O ALA A 114 -52.216 119.339 -8.142 1.00 40.39 O ANISOU 906 O ALA A 114 5999 5512 3835 -1267 510 343 O ATOM 907 CB ALA A 114 -51.340 117.112 -6.105 1.00 37.08 C ANISOU 907 CB ALA A 114 5411 5033 3644 -1151 635 162 C ATOM 908 N SER A 115 -52.840 117.381 -9.054 1.00 42.36 N ANISOU 908 N SER A 115 6385 5846 3863 -1323 631 192 N ATOM 909 CA SER A 115 -54.143 117.810 -9.526 1.00 44.04 C ANISOU 909 CA SER A 115 6664 6128 3940 -1363 475 232 C ATOM 910 C SER A 115 -55.165 117.580 -8.421 1.00 42.88 C ANISOU 910 C SER A 115 6450 5967 3875 -1297 337 182 C ATOM 911 O SER A 115 -54.928 116.812 -7.478 1.00 42.04 O ANISOU 911 O SER A 115 6280 5818 3874 -1240 380 97 O ATOM 912 CB SER A 115 -54.544 117.019 -10.766 1.00 46.17 C ANISOU 912 CB SER A 115 7078 6487 3977 -1470 539 179 C ATOM 913 OG SER A 115 -55.756 117.491 -11.342 1.00 48.34 O ANISOU 913 OG SER A 115 7406 6851 4109 -1527 373 250 O ATOM 914 N THR A 116 -56.305 118.246 -8.559 1.00 43.36 N ANISOU 914 N THR A 116 6519 6066 3889 -1304 178 251 N ATOM 915 CA THR A 116 -57.427 118.080 -7.648 1.00 42.14 C ANISOU 915 CA THR A 116 6304 5907 3798 -1247 53 215 C ATOM 916 C THR A 116 -57.762 116.599 -7.469 1.00 41.36 C ANISOU 916 C THR A 116 6232 5836 3646 -1262 105 81 C ATOM 917 O THR A 116 -57.863 115.858 -8.447 1.00 40.72 O ANISOU 917 O THR A 116 6251 5816 3405 -1351 165 35 O ATOM 918 CB THR A 116 -58.678 118.804 -8.159 1.00 43.28 C ANISOU 918 CB THR A 116 6460 6107 3877 -1270 -105 321 C ATOM 919 OG1 THR A 116 -58.390 120.198 -8.296 1.00 44.82 O ANISOU 919 OG1 THR A 116 6626 6253 4149 -1248 -143 455 O ATOM 920 CG2 THR A 116 -59.834 118.630 -7.191 1.00 42.66 C ANISOU 920 CG2 THR A 116 6306 6017 3886 -1205 -214 286 C ATOM 921 N LYS A 117 -57.881 116.182 -6.210 1.00 39.90 N ANISOU 921 N LYS A 117 5963 5602 3595 -1184 93 17 N ATOM 922 CA LYS A 117 -58.169 114.793 -5.869 1.00 39.96 C ANISOU 922 CA LYS A 117 5977 5614 3590 -1185 147 -97 C ATOM 923 C LYS A 117 -58.964 114.724 -4.576 1.00 37.84 C ANISOU 923 C LYS A 117 5619 5326 3434 -1109 51 -119 C ATOM 924 O LYS A 117 -58.622 115.390 -3.596 1.00 37.08 O ANISOU 924 O LYS A 117 5444 5182 3464 -1041 23 -91 O ATOM 925 CB LYS A 117 -56.869 113.987 -5.731 1.00 40.60 C ANISOU 925 CB LYS A 117 6051 5641 3733 -1171 325 -155 C ATOM 926 CG LYS A 117 -57.067 112.492 -5.520 1.00 41.59 C ANISOU 926 CG LYS A 117 6192 5750 3860 -1175 412 -266 C ATOM 927 CD LYS A 117 -55.728 111.775 -5.402 1.00 42.09 C ANISOU 927 CD LYS A 117 6228 5743 4021 -1146 601 -293 C ATOM 928 CE LYS A 117 -55.786 110.323 -4.932 1.00 42.16 C ANISOU 928 CE LYS A 117 6221 5701 4098 -1123 701 -382 C ATOM 929 NZ LYS A 117 -56.899 109.904 -4.027 1.00 41.74 N ANISOU 929 NZ LYS A 117 6125 5660 4074 -1093 584 -410 N ATOM 930 N GLY A 118 -60.009 113.898 -4.581 1.00 36.74 N ANISOU 930 N GLY A 118 5496 5224 3240 -1134 9 -175 N ATOM 931 CA GLY A 118 -60.824 113.659 -3.403 1.00 35.16 C ANISOU 931 CA GLY A 118 5214 5011 3134 -1069 -60 -201 C ATOM 932 C GLY A 118 -60.182 112.644 -2.470 1.00 34.28 C ANISOU 932 C GLY A 118 5061 4851 3113 -1024 42 -272 C ATOM 933 O GLY A 118 -59.433 111.773 -2.925 1.00 34.41 O ANISOU 933 O GLY A 118 5120 4846 3109 -1055 169 -319 O ATOM 934 N PRO A 119 -60.477 112.732 -1.157 1.00 32.37 N ANISOU 934 N PRO A 119 4734 4590 2976 -953 -5 -273 N ATOM 935 CA PRO A 119 -59.805 111.887 -0.170 1.00 31.57 C ANISOU 935 CA PRO A 119 4577 4454 2964 -909 73 -304 C ATOM 936 C PRO A 119 -60.306 110.454 -0.112 1.00 31.72 C ANISOU 936 C PRO A 119 4607 4468 2978 -924 128 -369 C ATOM 937 O PRO A 119 -61.462 110.190 -0.432 1.00 31.66 O ANISOU 937 O PRO A 119 4626 4492 2910 -960 69 -397 O ATOM 938 CB PRO A 119 -60.135 112.582 1.159 1.00 31.08 C ANISOU 938 CB PRO A 119 4438 4392 2979 -849 -10 -283 C ATOM 939 CG PRO A 119 -61.460 113.209 0.913 1.00 30.94 C ANISOU 939 CG PRO A 119 4433 4400 2925 -853 -112 -273 C ATOM 940 CD PRO A 119 -61.450 113.639 -0.527 1.00 31.74 C ANISOU 940 CD PRO A 119 4605 4520 2936 -912 -124 -238 C ATOM 941 N SER A 120 -59.425 109.541 0.293 1.00 31.62 N ANISOU 941 N SER A 120 4562 4410 3041 -899 241 -380 N ATOM 942 CA SER A 120 -59.823 108.228 0.780 1.00 31.89 C ANISOU 942 CA SER A 120 4576 4418 3122 -889 295 -422 C ATOM 943 C SER A 120 -60.035 108.375 2.276 1.00 31.00 C ANISOU 943 C SER A 120 4367 4323 3088 -823 226 -379 C ATOM 944 O SER A 120 -59.234 109.017 2.953 1.00 31.40 O ANISOU 944 O SER A 120 4361 4381 3187 -787 206 -324 O ATOM 945 CB SER A 120 -58.744 107.185 0.517 1.00 32.88 C ANISOU 945 CB SER A 120 4703 4470 3319 -883 465 -434 C ATOM 946 OG SER A 120 -58.506 107.058 -0.866 1.00 34.07 O ANISOU 946 OG SER A 120 4959 4604 3383 -954 552 -490 O ATOM 947 N VAL A 121 -61.122 107.809 2.784 1.00 30.31 N ANISOU 947 N VAL A 121 4263 4249 3003 -820 189 -405 N ATOM 948 CA VAL A 121 -61.473 107.924 4.196 1.00 29.66 C ANISOU 948 CA VAL A 121 4103 4195 2970 -768 132 -371 C ATOM 949 C VAL A 121 -61.369 106.521 4.809 1.00 30.01 C ANISOU 949 C VAL A 121 4105 4205 3092 -750 215 -361 C ATOM 950 O VAL A 121 -62.061 105.609 4.379 1.00 30.28 O ANISOU 950 O VAL A 121 4171 4210 3124 -782 255 -410 O ATOM 951 CB VAL A 121 -62.886 108.522 4.370 1.00 29.30 C ANISOU 951 CB VAL A 121 4059 4193 2882 -772 29 -391 C ATOM 952 CG1 VAL A 121 -63.224 108.681 5.845 1.00 29.30 C ANISOU 952 CG1 VAL A 121 3991 4222 2922 -724 -5 -369 C ATOM 953 CG2 VAL A 121 -63.001 109.871 3.660 1.00 29.29 C ANISOU 953 CG2 VAL A 121 4092 4207 2829 -786 -42 -381 C ATOM 954 N PHE A 122 -60.498 106.364 5.800 1.00 29.54 N ANISOU 954 N PHE A 122 3971 4149 3102 -706 235 -290 N ATOM 955 CA PHE A 122 -60.267 105.076 6.456 1.00 29.86 C ANISOU 955 CA PHE A 122 3954 4155 3238 -678 313 -243 C ATOM 956 C PHE A 122 -60.671 105.170 7.923 1.00 29.54 C ANISOU 956 C PHE A 122 3846 4182 3196 -650 241 -187 C ATOM 957 O PHE A 122 -60.520 106.230 8.532 1.00 28.63 O ANISOU 957 O PHE A 122 3716 4131 3029 -649 157 -172 O ATOM 958 CB PHE A 122 -58.804 104.681 6.332 1.00 30.64 C ANISOU 958 CB PHE A 122 4005 4206 3432 -652 408 -172 C ATOM 959 CG PHE A 122 -58.358 104.483 4.912 1.00 31.08 C ANISOU 959 CG PHE A 122 4132 4188 3487 -681 516 -233 C ATOM 960 CD1 PHE A 122 -58.902 103.464 4.134 1.00 31.88 C ANISOU 960 CD1 PHE A 122 4302 4214 3595 -715 615 -315 C ATOM 961 CD2 PHE A 122 -57.421 105.318 4.344 1.00 31.49 C ANISOU 961 CD2 PHE A 122 4193 4247 3524 -687 523 -216 C ATOM 962 CE1 PHE A 122 -58.505 103.275 2.815 1.00 32.80 C ANISOU 962 CE1 PHE A 122 4507 4270 3687 -759 727 -388 C ATOM 963 CE2 PHE A 122 -57.027 105.145 3.021 1.00 32.40 C ANISOU 963 CE2 PHE A 122 4387 4303 3622 -721 636 -275 C ATOM 964 CZ PHE A 122 -57.559 104.116 2.256 1.00 32.76 C ANISOU 964 CZ PHE A 122 4511 4279 3657 -759 742 -366 C ATOM 965 N PRO A 123 -61.214 104.074 8.491 1.00 30.11 N ANISOU 965 N PRO A 123 3885 4236 3319 -638 281 -163 N ATOM 966 CA PRO A 123 -61.697 104.143 9.870 1.00 29.98 C ANISOU 966 CA PRO A 123 3816 4296 3281 -622 222 -112 C ATOM 967 C PRO A 123 -60.565 103.966 10.876 1.00 31.24 C ANISOU 967 C PRO A 123 3891 4497 3482 -598 217 15 C ATOM 968 O PRO A 123 -59.646 103.188 10.630 1.00 31.82 O ANISOU 968 O PRO A 123 3918 4512 3661 -576 295 88 O ATOM 969 CB PRO A 123 -62.680 102.971 9.957 1.00 30.67 C ANISOU 969 CB PRO A 123 3897 4340 3414 -625 276 -123 C ATOM 970 CG PRO A 123 -62.182 101.986 8.963 1.00 30.95 C ANISOU 970 CG PRO A 123 3955 4264 3540 -633 390 -139 C ATOM 971 CD PRO A 123 -61.547 102.780 7.856 1.00 30.60 C ANISOU 971 CD PRO A 123 3970 4207 3451 -652 388 -196 C ATOM 972 N LEU A 124 -60.642 104.706 11.978 1.00 31.31 N ANISOU 972 N LEU A 124 3880 4607 3410 -610 130 41 N ATOM 973 CA LEU A 124 -59.758 104.521 13.119 1.00 32.73 C ANISOU 973 CA LEU A 124 3978 4861 3596 -612 98 173 C ATOM 974 C LEU A 124 -60.635 103.909 14.202 1.00 33.28 C ANISOU 974 C LEU A 124 4027 4985 3634 -611 95 213 C ATOM 975 O LEU A 124 -61.305 104.624 14.952 1.00 33.44 O ANISOU 975 O LEU A 124 4081 5085 3540 -638 40 163 O ATOM 976 CB LEU A 124 -59.140 105.855 13.545 1.00 32.68 C ANISOU 976 CB LEU A 124 3982 4938 3498 -654 2 159 C ATOM 977 CG LEU A 124 -58.338 106.594 12.468 1.00 32.49 C ANISOU 977 CG LEU A 124 3981 4862 3503 -661 4 120 C ATOM 978 CD1 LEU A 124 -57.918 107.972 12.961 1.00 32.75 C ANISOU 978 CD1 LEU A 124 4033 4966 3444 -715 -91 89 C ATOM 979 CD2 LEU A 124 -57.108 105.799 12.035 1.00 33.27 C ANISOU 979 CD2 LEU A 124 3997 4912 3731 -634 70 233 C ATOM 980 N ALA A 125 -60.660 102.578 14.232 1.00 33.76 N ANISOU 980 N ALA A 125 4037 4988 3804 -580 173 297 N ATOM 981 CA ALA A 125 -61.628 101.823 15.030 1.00 34.55 C ANISOU 981 CA ALA A 125 4120 5110 3898 -577 195 333 C ATOM 982 C ALA A 125 -61.212 101.792 16.488 1.00 35.49 C ANISOU 982 C ALA A 125 4177 5359 3951 -596 136 473 C ATOM 983 O ALA A 125 -60.023 101.662 16.779 1.00 36.40 O ANISOU 983 O ALA A 125 4219 5507 4106 -595 108 603 O ATOM 984 CB ALA A 125 -61.760 100.399 14.503 1.00 34.94 C ANISOU 984 CB ALA A 125 4140 5031 4103 -545 310 375 C ATOM 985 N PRO A 126 -62.185 101.917 17.412 1.00 35.84 N ANISOU 985 N PRO A 126 4244 5485 3890 -620 116 455 N ATOM 986 CA PRO A 126 -61.869 101.805 18.828 1.00 37.20 C ANISOU 986 CA PRO A 126 4369 5796 3969 -656 64 590 C ATOM 987 C PRO A 126 -61.608 100.343 19.185 1.00 38.04 C ANISOU 987 C PRO A 126 4380 5869 4205 -621 120 780 C ATOM 988 O PRO A 126 -60.642 100.039 19.874 1.00 39.53 O ANISOU 988 O PRO A 126 4485 6132 4401 -632 73 958 O ATOM 989 CB PRO A 126 -63.145 102.302 19.506 1.00 37.08 C ANISOU 989 CB PRO A 126 4420 5848 3820 -685 68 489 C ATOM 990 CG PRO A 126 -64.229 101.913 18.568 1.00 36.27 C ANISOU 990 CG PRO A 126 4343 5621 3816 -645 145 387 C ATOM 991 CD PRO A 126 -63.638 102.026 17.185 1.00 35.57 C ANISOU 991 CD PRO A 126 4267 5418 3828 -619 152 328 C ATOM 992 N GLY A 134 -64.953 103.149 30.880 1.00 47.52 N ANISOU 992 N GLY A 134 6036 8582 3438 -1399 -17 890 N ATOM 993 CA GLY A 134 -64.453 104.507 30.694 1.00 47.08 C ANISOU 993 CA GLY A 134 6074 8532 3283 -1467 -73 691 C ATOM 994 C GLY A 134 -64.792 105.043 29.312 1.00 44.65 C ANISOU 994 C GLY A 134 5767 7999 3199 -1347 -20 511 C ATOM 995 O GLY A 134 -65.936 104.948 28.867 1.00 43.39 O ANISOU 995 O GLY A 134 5615 7716 3154 -1255 108 413 O ATOM 996 N THR A 135 -63.800 105.614 28.634 1.00 43.79 N ANISOU 996 N THR A 135 5644 7846 3150 -1354 -122 480 N ATOM 997 CA THR A 135 -64.017 106.224 27.325 1.00 42.10 C ANISOU 997 CA THR A 135 5439 7437 3121 -1257 -85 318 C ATOM 998 C THR A 135 -63.142 105.576 26.264 1.00 40.83 C ANISOU 998 C THR A 135 5162 7179 3173 -1178 -155 450 C ATOM 999 O THR A 135 -62.066 105.053 26.565 1.00 41.68 O ANISOU 999 O THR A 135 5189 7375 3272 -1218 -257 637 O ATOM 1000 CB THR A 135 -63.707 107.736 27.334 1.00 42.61 C ANISOU 1000 CB THR A 135 5614 7500 3074 -1337 -110 115 C ATOM 1001 OG1 THR A 135 -62.297 107.940 27.481 1.00 43.52 O ANISOU 1001 OG1 THR A 135 5699 7710 3127 -1430 -261 207 O ATOM 1002 CG2 THR A 135 -64.453 108.447 28.453 1.00 43.88 C ANISOU 1002 CG2 THR A 135 5906 7754 3013 -1432 -22 -33 C ATOM 1003 N ALA A 136 -63.599 105.655 25.020 1.00 38.73 N ANISOU 1003 N ALA A 136 4887 6734 3095 -1071 -97 351 N ATOM 1004 CA ALA A 136 -62.867 105.128 23.879 1.00 37.58 C ANISOU 1004 CA ALA A 136 4655 6475 3149 -997 -131 432 C ATOM 1005 C ALA A 136 -62.760 106.201 22.804 1.00 36.21 C ANISOU 1005 C ALA A 136 4534 6187 3038 -972 -136 263 C ATOM 1006 O ALA A 136 -63.698 106.973 22.584 1.00 35.17 O ANISOU 1006 O ALA A 136 4477 5996 2888 -954 -75 95 O ATOM 1007 CB ALA A 136 -63.562 103.892 23.336 1.00 36.92 C ANISOU 1007 CB ALA A 136 4507 6283 3238 -900 -45 506 C ATOM 1008 N ALA A 137 -61.599 106.249 22.158 1.00 35.91 N ANISOU 1008 N ALA A 137 4445 6119 3081 -968 -205 324 N ATOM 1009 CA ALA A 137 -61.354 107.152 21.057 1.00 34.95 C ANISOU 1009 CA ALA A 137 4360 5888 3031 -945 -212 198 C ATOM 1010 C ALA A 137 -61.623 106.408 19.754 1.00 34.08 C ANISOU 1010 C ALA A 137 4208 5629 3111 -842 -148 210 C ATOM 1011 O ALA A 137 -61.279 105.239 19.611 1.00 34.03 O ANISOU 1011 O ALA A 137 4121 5600 3208 -803 -128 348 O ATOM 1012 CB ALA A 137 -59.919 107.653 21.100 1.00 35.54 C ANISOU 1012 CB ALA A 137 4401 6019 3082 -1012 -314 258 C ATOM 1013 N LEU A 138 -62.266 107.085 18.818 1.00 33.66 N ANISOU 1013 N LEU A 138 4213 5474 3103 -805 -113 66 N ATOM 1014 CA LEU A 138 -62.416 106.568 17.462 1.00 32.97 C ANISOU 1014 CA LEU A 138 4106 5258 3163 -736 -69 56 C ATOM 1015 C LEU A 138 -62.333 107.745 16.513 1.00 32.48 C ANISOU 1015 C LEU A 138 4102 5129 3110 -735 -89 -62 C ATOM 1016 O LEU A 138 -62.460 108.900 16.933 1.00 32.86 O ANISOU 1016 O LEU A 138 4206 5207 3073 -772 -116 -150 O ATOM 1017 CB LEU A 138 -63.721 105.793 17.312 1.00 32.82 C ANISOU 1017 CB LEU A 138 4084 5191 3194 -693 3 34 C ATOM 1018 CG LEU A 138 -65.040 106.568 17.482 1.00 33.03 C ANISOU 1018 CG LEU A 138 4165 5216 3170 -689 29 -90 C ATOM 1019 CD1 LEU A 138 -65.576 107.081 16.156 1.00 32.38 C ANISOU 1019 CD1 LEU A 138 4110 5032 3162 -655 34 -185 C ATOM 1020 CD2 LEU A 138 -66.091 105.695 18.146 1.00 33.54 C ANISOU 1020 CD2 LEU A 138 4200 5306 3238 -676 90 -54 C ATOM 1021 N GLY A 139 -62.099 107.461 15.245 1.00 31.87 N ANISOU 1021 N GLY A 139 4017 4958 3135 -698 -66 -65 N ATOM 1022 CA GLY A 139 -61.927 108.522 14.280 1.00 31.83 C ANISOU 1022 CA GLY A 139 4062 4894 3139 -699 -87 -149 C ATOM 1023 C GLY A 139 -61.928 108.089 12.832 1.00 31.49 C ANISOU 1023 C GLY A 139 4025 4757 3182 -667 -48 -159 C ATOM 1024 O GLY A 139 -62.244 106.949 12.510 1.00 30.95 O ANISOU 1024 O GLY A 139 3934 4652 3173 -645 5 -129 O ATOM 1025 N CYS A 140 -61.573 109.039 11.975 1.00 32.00 N ANISOU 1025 N CYS A 140 4130 4782 3248 -676 -71 -207 N ATOM 1026 CA CYS A 140 -61.467 108.840 10.540 1.00 32.72 C ANISOU 1026 CA CYS A 140 4247 4799 3387 -666 -38 -224 C ATOM 1027 C CYS A 140 -60.168 109.462 10.061 1.00 32.15 C ANISOU 1027 C CYS A 140 4173 4713 3329 -685 -49 -198 C ATOM 1028 O CYS A 140 -59.883 110.607 10.390 1.00 31.25 O ANISOU 1028 O CYS A 140 4076 4619 3178 -710 -101 -220 O ATOM 1029 CB CYS A 140 -62.636 109.524 9.825 1.00 33.80 C ANISOU 1029 CB CYS A 140 4435 4906 3502 -660 -60 -301 C ATOM 1030 SG CYS A 140 -64.163 108.578 9.873 1.00 37.33 S ANISOU 1030 SG CYS A 140 4868 5351 3964 -646 -36 -323 S ATOM 1031 N LEU A 141 -59.408 108.693 9.284 1.00 31.65 N ANISOU 1031 N LEU A 141 4093 4606 3329 -677 14 -155 N ATOM 1032 CA LEU A 141 -58.216 109.168 8.601 1.00 31.20 C ANISOU 1032 CA LEU A 141 4029 4523 3301 -691 30 -126 C ATOM 1033 C LEU A 141 -58.635 109.596 7.194 1.00 30.79 C ANISOU 1033 C LEU A 141 4059 4419 3221 -701 51 -194 C ATOM 1034 O LEU A 141 -59.084 108.772 6.404 1.00 29.89 O ANISOU 1034 O LEU A 141 3980 4266 3113 -699 113 -224 O ATOM 1035 CB LEU A 141 -57.172 108.051 8.540 1.00 31.78 C ANISOU 1035 CB LEU A 141 4031 4571 3474 -670 113 -36 C ATOM 1036 CG LEU A 141 -55.889 108.273 7.742 1.00 32.25 C ANISOU 1036 CG LEU A 141 4066 4592 3595 -676 168 7 C ATOM 1037 CD1 LEU A 141 -55.120 109.476 8.244 1.00 32.70 C ANISOU 1037 CD1 LEU A 141 4090 4705 3630 -714 78 41 C ATOM 1038 CD2 LEU A 141 -55.010 107.036 7.799 1.00 33.11 C ANISOU 1038 CD2 LEU A 141 4086 4661 3835 -638 272 106 C ATOM 1039 N VAL A 142 -58.516 110.891 6.917 1.00 30.40 N ANISOU 1039 N VAL A 142 4044 4372 3137 -722 -3 -214 N ATOM 1040 CA VAL A 142 -58.891 111.485 5.633 1.00 30.65 C ANISOU 1040 CA VAL A 142 4147 4367 3130 -738 -2 -251 C ATOM 1041 C VAL A 142 -57.620 111.673 4.824 1.00 31.13 C ANISOU 1041 C VAL A 142 4209 4401 3217 -758 53 -212 C ATOM 1042 O VAL A 142 -56.857 112.609 5.067 1.00 30.95 O ANISOU 1042 O VAL A 142 4165 4382 3213 -775 20 -182 O ATOM 1043 CB VAL A 142 -59.590 112.843 5.834 1.00 30.21 C ANISOU 1043 CB VAL A 142 4119 4314 3045 -741 -84 -279 C ATOM 1044 CG1 VAL A 142 -59.984 113.473 4.494 1.00 30.28 C ANISOU 1044 CG1 VAL A 142 4189 4295 3021 -757 -97 -281 C ATOM 1045 CG2 VAL A 142 -60.803 112.673 6.729 1.00 30.00 C ANISOU 1045 CG2 VAL A 142 4079 4312 3008 -715 -117 -315 C ATOM 1046 N LYS A 143 -57.423 110.813 3.829 1.00 32.21 N ANISOU 1046 N LYS A 143 4377 4506 3356 -765 146 -220 N ATOM 1047 CA LYS A 143 -56.103 110.622 3.223 1.00 33.99 C ANISOU 1047 CA LYS A 143 4584 4699 3632 -772 244 -177 C ATOM 1048 C LYS A 143 -56.012 110.960 1.725 1.00 34.40 C ANISOU 1048 C LYS A 143 4726 4728 3618 -813 298 -203 C ATOM 1049 O LYS A 143 -56.907 110.641 0.941 1.00 34.72 O ANISOU 1049 O LYS A 143 4849 4770 3575 -841 304 -260 O ATOM 1050 CB LYS A 143 -55.675 109.170 3.436 1.00 35.07 C ANISOU 1050 CB LYS A 143 4671 4801 3854 -742 355 -157 C ATOM 1051 CG LYS A 143 -54.189 108.984 3.618 1.00 36.74 C ANISOU 1051 CG LYS A 143 4787 4992 4180 -722 430 -66 C ATOM 1052 CD LYS A 143 -53.826 107.530 3.838 1.00 38.01 C ANISOU 1052 CD LYS A 143 4886 5099 4455 -679 552 -28 C ATOM 1053 CE LYS A 143 -52.428 107.211 3.339 1.00 39.60 C ANISOU 1053 CE LYS A 143 5021 5245 4780 -658 693 43 C ATOM 1054 NZ LYS A 143 -52.284 105.752 3.085 1.00 40.96 N ANISOU 1054 NZ LYS A 143 5178 5323 5064 -617 864 42 N ATOM 1055 N ASP A 144 -54.896 111.582 1.349 1.00 34.59 N ANISOU 1055 N ASP A 144 4731 4738 3675 -826 337 -152 N ATOM 1056 CA ASP A 144 -54.488 111.770 -0.044 1.00 34.90 C ANISOU 1056 CA ASP A 144 4845 4757 3660 -866 425 -158 C ATOM 1057 C ASP A 144 -55.458 112.618 -0.877 1.00 34.19 C ANISOU 1057 C ASP A 144 4855 4696 3442 -910 342 -182 C ATOM 1058 O ASP A 144 -55.925 112.187 -1.934 1.00 34.97 O ANISOU 1058 O ASP A 144 5046 4804 3439 -956 388 -225 O ATOM 1059 CB ASP A 144 -54.200 110.410 -0.721 1.00 36.42 C ANISOU 1059 CB ASP A 144 5070 4904 3863 -869 592 -201 C ATOM 1060 CG ASP A 144 -53.071 109.642 -0.044 1.00 37.14 C ANISOU 1060 CG ASP A 144 5043 4952 4116 -816 695 -141 C ATOM 1061 OD1 ASP A 144 -52.191 110.268 0.582 1.00 37.67 O ANISOU 1061 OD1 ASP A 144 5011 5035 4268 -799 654 -55 O ATOM 1062 OD2 ASP A 144 -53.043 108.402 -0.161 1.00 38.45 O ANISOU 1062 OD2 ASP A 144 5210 5063 4334 -796 819 -174 O ATOM 1063 N TYR A 145 -55.739 113.826 -0.384 1.00 32.60 N ANISOU 1063 N TYR A 145 4630 4506 3249 -903 222 -148 N ATOM 1064 CA TYR A 145 -56.563 114.805 -1.102 1.00 31.70 C ANISOU 1064 CA TYR A 145 4583 4408 3053 -931 139 -131 C ATOM 1065 C TYR A 145 -55.751 116.049 -1.446 1.00 31.85 C ANISOU 1065 C TYR A 145 4599 4402 3101 -951 133 -62 C ATOM 1066 O TYR A 145 -54.677 116.280 -0.894 1.00 31.63 O ANISOU 1066 O TYR A 145 4505 4350 3162 -945 165 -35 O ATOM 1067 CB TYR A 145 -57.806 115.205 -0.299 1.00 30.40 C ANISOU 1067 CB TYR A 145 4398 4255 2900 -899 18 -148 C ATOM 1068 CG TYR A 145 -57.536 115.935 0.990 1.00 29.66 C ANISOU 1068 CG TYR A 145 4235 4137 2899 -865 -33 -143 C ATOM 1069 CD1 TYR A 145 -57.366 115.247 2.196 1.00 28.83 C ANISOU 1069 CD1 TYR A 145 4068 4044 2841 -838 -27 -174 C ATOM 1070 CD2 TYR A 145 -57.458 117.328 1.010 1.00 29.68 C ANISOU 1070 CD2 TYR A 145 4241 4102 2936 -871 -85 -106 C ATOM 1071 CE1 TYR A 145 -57.118 115.936 3.379 1.00 28.85 C ANISOU 1071 CE1 TYR A 145 4024 4041 2897 -831 -78 -178 C ATOM 1072 CE2 TYR A 145 -57.209 118.017 2.188 1.00 29.66 C ANISOU 1072 CE2 TYR A 145 4193 4071 3005 -862 -123 -125 C ATOM 1073 CZ TYR A 145 -57.038 117.319 3.365 1.00 28.97 C ANISOU 1073 CZ TYR A 145 4055 4015 2938 -849 -122 -166 C ATOM 1074 OH TYR A 145 -56.791 118.016 4.527 1.00 29.65 O ANISOU 1074 OH TYR A 145 4112 4088 3065 -863 -163 -192 O ATOM 1075 N PHE A 146 -56.289 116.823 -2.382 1.00 31.98 N ANISOU 1075 N PHE A 146 4680 4429 3042 -983 88 -20 N ATOM 1076 CA PHE A 146 -55.692 118.072 -2.816 1.00 32.61 C ANISOU 1076 CA PHE A 146 4765 4478 3149 -1005 79 60 C ATOM 1077 C PHE A 146 -56.739 118.883 -3.591 1.00 33.17 C ANISOU 1077 C PHE A 146 4890 4563 3150 -1022 -10 122 C ATOM 1078 O PHE A 146 -57.484 118.289 -4.371 1.00 33.19 O ANISOU 1078 O PHE A 146 4950 4626 3034 -1054 -23 114 O ATOM 1079 CB PHE A 146 -54.485 117.787 -3.715 1.00 33.26 C ANISOU 1079 CB PHE A 146 4872 4562 3202 -1048 210 88 C ATOM 1080 CG PHE A 146 -53.677 118.999 -4.029 1.00 34.29 C ANISOU 1080 CG PHE A 146 4990 4655 3385 -1074 217 175 C ATOM 1081 CD1 PHE A 146 -52.661 119.405 -3.172 1.00 34.04 C ANISOU 1081 CD1 PHE A 146 4869 4578 3487 -1065 229 189 C ATOM 1082 CD2 PHE A 146 -53.925 119.745 -5.186 1.00 35.30 C ANISOU 1082 CD2 PHE A 146 5191 4795 3425 -1118 205 254 C ATOM 1083 CE1 PHE A 146 -51.907 120.529 -3.456 1.00 35.13 C ANISOU 1083 CE1 PHE A 146 4992 4673 3683 -1100 237 268 C ATOM 1084 CE2 PHE A 146 -53.172 120.882 -5.468 1.00 36.16 C ANISOU 1084 CE2 PHE A 146 5286 4858 3596 -1144 218 345 C ATOM 1085 CZ PHE A 146 -52.162 121.275 -4.599 1.00 36.00 C ANISOU 1085 CZ PHE A 146 5177 4780 3721 -1135 237 345 C ATOM 1086 N PRO A 147 -56.827 120.205 -3.405 1.00 33.85 N ANISOU 1086 N PRO A 147 4954 4593 3313 -1008 -73 189 N ATOM 1087 CA PRO A 147 -56.079 121.001 -2.416 1.00 34.02 C ANISOU 1087 CA PRO A 147 4916 4539 3472 -991 -72 182 C ATOM 1088 C PRO A 147 -56.840 121.039 -1.093 1.00 34.03 C ANISOU 1088 C PRO A 147 4872 4515 3542 -939 -135 109 C ATOM 1089 O PRO A 147 -57.833 120.342 -0.956 1.00 33.40 O ANISOU 1089 O PRO A 147 4796 4478 3417 -911 -167 71 O ATOM 1090 CB PRO A 147 -56.071 122.391 -3.053 1.00 34.87 C ANISOU 1090 CB PRO A 147 5044 4587 3617 -1009 -101 288 C ATOM 1091 CG PRO A 147 -57.351 122.437 -3.819 1.00 35.07 C ANISOU 1091 CG PRO A 147 5107 4653 3563 -999 -170 346 C ATOM 1092 CD PRO A 147 -57.492 121.063 -4.404 1.00 34.98 C ANISOU 1092 CD PRO A 147 5140 4744 3406 -1030 -134 297 C ATOM 1093 N GLU A 148 -56.394 121.858 -0.142 1.00 35.05 N ANISOU 1093 N GLU A 148 4964 4577 3776 -939 -149 86 N ATOM 1094 CA GLU A 148 -57.204 122.183 1.038 1.00 35.45 C ANISOU 1094 CA GLU A 148 4992 4591 3886 -900 -197 17 C ATOM 1095 C GLU A 148 -58.425 123.023 0.594 1.00 35.92 C ANISOU 1095 C GLU A 148 5071 4597 3981 -860 -242 71 C ATOM 1096 O GLU A 148 -58.405 123.591 -0.499 1.00 36.60 O ANISOU 1096 O GLU A 148 5182 4665 4058 -874 -248 173 O ATOM 1097 CB GLU A 148 -56.366 122.942 2.086 1.00 36.90 C ANISOU 1097 CB GLU A 148 5150 4714 4155 -937 -194 -30 C ATOM 1098 CG GLU A 148 -55.118 122.170 2.571 1.00 37.51 C ANISOU 1098 CG GLU A 148 5181 4855 4218 -980 -167 -49 C ATOM 1099 CD GLU A 148 -54.759 122.240 4.075 1.00 38.74 C ANISOU 1099 CD GLU A 148 5299 5020 4401 -1014 -198 -128 C ATOM 1100 OE1 GLU A 148 -53.594 122.587 4.358 1.00 40.41 O ANISOU 1100 OE1 GLU A 148 5473 5228 4654 -1082 -199 -111 O ATOM 1101 OE2 GLU A 148 -55.548 121.936 5.006 1.00 39.05 O ANISOU 1101 OE2 GLU A 148 5341 5081 4415 -987 -222 -201 O ATOM 1102 N PRO A 149 -59.507 123.082 1.379 1.00 35.90 N ANISOU 1102 N PRO A 149 5049 4573 4019 -807 -269 20 N ATOM 1103 CA PRO A 149 -59.679 122.382 2.649 1.00 35.35 C ANISOU 1103 CA PRO A 149 4955 4537 3940 -793 -261 -91 C ATOM 1104 C PRO A 149 -60.605 121.165 2.582 1.00 34.53 C ANISOU 1104 C PRO A 149 4836 4519 3763 -760 -277 -107 C ATOM 1105 O PRO A 149 -61.278 120.915 1.580 1.00 35.07 O ANISOU 1105 O PRO A 149 4914 4623 3789 -752 -307 -42 O ATOM 1106 CB PRO A 149 -60.332 123.462 3.513 1.00 35.76 C ANISOU 1106 CB PRO A 149 5003 4486 4099 -761 -256 -137 C ATOM 1107 CG PRO A 149 -61.235 124.165 2.542 1.00 36.70 C ANISOU 1107 CG PRO A 149 5117 4550 4276 -715 -280 -29 C ATOM 1108 CD PRO A 149 -60.559 124.100 1.190 1.00 36.90 C ANISOU 1108 CD PRO A 149 5167 4616 4237 -758 -296 78 C ATOM 1109 N VAL A 150 -60.623 120.415 3.671 1.00 34.04 N ANISOU 1109 N VAL A 150 4752 4497 3684 -753 -263 -190 N ATOM 1110 CA VAL A 150 -61.676 119.452 3.934 1.00 34.61 C ANISOU 1110 CA VAL A 150 4802 4626 3722 -717 -273 -217 C ATOM 1111 C VAL A 150 -62.347 119.863 5.252 1.00 34.92 C ANISOU 1111 C VAL A 150 4821 4630 3818 -682 -262 -289 C ATOM 1112 O VAL A 150 -61.699 120.436 6.127 1.00 34.80 O ANISOU 1112 O VAL A 150 4817 4580 3824 -708 -242 -343 O ATOM 1113 CB VAL A 150 -61.133 118.001 3.893 1.00 34.29 C ANISOU 1113 CB VAL A 150 4758 4665 3608 -741 -247 -235 C ATOM 1114 CG1 VAL A 150 -60.652 117.526 5.245 1.00 34.00 C ANISOU 1114 CG1 VAL A 150 4691 4654 3576 -744 -226 -293 C ATOM 1115 CG2 VAL A 150 -62.185 117.059 3.352 1.00 34.81 C ANISOU 1115 CG2 VAL A 150 4821 4780 3627 -728 -262 -229 C ATOM 1116 N THR A 151 -63.655 119.643 5.355 1.00 35.17 N ANISOU 1116 N THR A 151 4823 4669 3871 -633 -272 -288 N ATOM 1117 CA THR A 151 -64.371 119.801 6.624 1.00 35.14 C ANISOU 1117 CA THR A 151 4799 4644 3909 -598 -237 -363 C ATOM 1118 C THR A 151 -64.849 118.412 7.056 1.00 34.16 C ANISOU 1118 C THR A 151 4646 4612 3723 -592 -234 -386 C ATOM 1119 O THR A 151 -65.251 117.590 6.215 1.00 34.01 O ANISOU 1119 O THR A 151 4610 4640 3671 -593 -264 -337 O ATOM 1120 CB THR A 151 -65.540 120.790 6.506 1.00 36.45 C ANISOU 1120 CB THR A 151 4937 4724 4190 -534 -226 -334 C ATOM 1121 OG1 THR A 151 -66.437 120.352 5.494 1.00 36.93 O ANISOU 1121 OG1 THR A 151 4952 4825 4253 -509 -281 -239 O ATOM 1122 CG2 THR A 151 -65.025 122.189 6.150 1.00 37.51 C ANISOU 1122 CG2 THR A 151 5101 4744 4406 -540 -216 -307 C ATOM 1123 N VAL A 152 -64.725 118.123 8.348 1.00 33.84 N ANISOU 1123 N VAL A 152 4605 4597 3656 -600 -196 -459 N ATOM 1124 CA VAL A 152 -65.213 116.865 8.919 1.00 33.25 C ANISOU 1124 CA VAL A 152 4498 4599 3535 -592 -183 -472 C ATOM 1125 C VAL A 152 -66.239 117.216 9.979 1.00 33.56 C ANISOU 1125 C VAL A 152 4521 4620 3610 -555 -133 -529 C ATOM 1126 O VAL A 152 -66.004 118.091 10.804 1.00 34.72 O ANISOU 1126 O VAL A 152 4702 4725 3763 -567 -93 -595 O ATOM 1127 CB VAL A 152 -64.085 116.002 9.532 1.00 32.78 C ANISOU 1127 CB VAL A 152 4444 4607 3403 -639 -179 -480 C ATOM 1128 CG1 VAL A 152 -64.626 114.637 9.958 1.00 32.65 C ANISOU 1128 CG1 VAL A 152 4391 4656 3358 -627 -161 -470 C ATOM 1129 CG2 VAL A 152 -62.948 115.813 8.536 1.00 32.60 C ANISOU 1129 CG2 VAL A 152 4434 4584 3368 -671 -200 -429 C ATOM 1130 N SER A 153 -67.387 116.551 9.930 1.00 32.79 N ANISOU 1130 N SER A 153 4372 4549 3538 -517 -126 -507 N ATOM 1131 CA SER A 153 -68.353 116.594 11.017 1.00 32.73 C ANISOU 1131 CA SER A 153 4338 4542 3557 -482 -58 -556 C ATOM 1132 C SER A 153 -68.675 115.156 11.413 1.00 31.84 C ANISOU 1132 C SER A 153 4190 4516 3391 -493 -53 -541 C ATOM 1133 O SER A 153 -68.237 114.212 10.750 1.00 31.00 O ANISOU 1133 O SER A 153 4080 4450 3250 -521 -98 -496 O ATOM 1134 CB SER A 153 -69.605 117.358 10.589 1.00 33.45 C ANISOU 1134 CB SER A 153 4375 4561 3775 -414 -40 -524 C ATOM 1135 OG SER A 153 -70.262 116.687 9.533 1.00 33.32 O ANISOU 1135 OG SER A 153 4298 4580 3782 -406 -109 -436 O ATOM 1136 N TRP A 154 -69.411 114.994 12.511 1.00 32.21 N ANISOU 1136 N TRP A 154 4217 4584 3438 -474 17 -581 N ATOM 1137 CA TRP A 154 -69.794 113.678 13.010 1.00 31.95 C ANISOU 1137 CA TRP A 154 4146 4626 3366 -484 34 -558 C ATOM 1138 C TRP A 154 -71.300 113.610 13.204 1.00 32.83 C ANISOU 1138 C TRP A 154 4184 4726 3562 -433 84 -549 C ATOM 1139 O TRP A 154 -71.894 114.515 13.797 1.00 33.08 O ANISOU 1139 O TRP A 154 4213 4713 3645 -395 159 -596 O ATOM 1140 CB TRP A 154 -69.056 113.362 14.307 1.00 31.95 C ANISOU 1140 CB TRP A 154 4188 4692 3259 -528 70 -593 C ATOM 1141 CG TRP A 154 -67.618 113.015 14.079 1.00 31.65 C ANISOU 1141 CG TRP A 154 4182 4686 3158 -578 10 -562 C ATOM 1142 CD1 TRP A 154 -66.565 113.881 14.003 1.00 31.76 C ANISOU 1142 CD1 TRP A 154 4246 4679 3144 -613 -21 -588 C ATOM 1143 CD2 TRP A 154 -67.076 111.708 13.884 1.00 31.24 C ANISOU 1143 CD2 TRP A 154 4103 4681 3086 -597 -15 -492 C ATOM 1144 NE1 TRP A 154 -65.400 113.194 13.791 1.00 31.40 N ANISOU 1144 NE1 TRP A 154 4194 4675 3062 -650 -67 -530 N ATOM 1145 CE2 TRP A 154 -65.683 111.858 13.703 1.00 31.23 C ANISOU 1145 CE2 TRP A 154 4126 4688 3050 -635 -57 -470 C ATOM 1146 CE3 TRP A 154 -67.631 110.425 13.837 1.00 31.46 C ANISOU 1146 CE3 TRP A 154 4083 4731 3137 -587 4 -443 C ATOM 1147 CZ2 TRP A 154 -64.832 110.768 13.476 1.00 31.39 C ANISOU 1147 CZ2 TRP A 154 4119 4735 3072 -651 -70 -395 C ATOM 1148 CZ3 TRP A 154 -66.786 109.337 13.617 1.00 31.54 C ANISOU 1148 CZ3 TRP A 154 4080 4759 3146 -607 -7 -379 C ATOM 1149 CH2 TRP A 154 -65.397 109.517 13.443 1.00 31.30 C ANISOU 1149 CH2 TRP A 154 4068 4732 3092 -633 -39 -352 C ATOM 1150 N ASN A 155 -71.906 112.541 12.684 1.00 33.25 N ANISOU 1150 N ASN A 155 4177 4813 3642 -438 53 -492 N ATOM 1151 CA ASN A 155 -73.358 112.321 12.747 1.00 34.09 C ANISOU 1151 CA ASN A 155 4191 4920 3842 -402 85 -462 C ATOM 1152 C ASN A 155 -74.133 113.540 12.261 1.00 35.30 C ANISOU 1152 C ASN A 155 4296 5002 4115 -343 86 -443 C ATOM 1153 O ASN A 155 -75.036 114.046 12.938 1.00 35.81 O ANISOU 1153 O ASN A 155 4308 5036 4263 -288 176 -458 O ATOM 1154 CB ASN A 155 -73.768 111.879 14.160 1.00 34.63 C ANISOU 1154 CB ASN A 155 4248 5029 3880 -396 189 -493 C ATOM 1155 CG ASN A 155 -73.216 110.513 14.519 1.00 34.00 C ANISOU 1155 CG ASN A 155 4185 5017 3716 -448 179 -468 C ATOM 1156 OD1 ASN A 155 -72.780 109.747 13.648 1.00 33.70 O ANISOU 1156 OD1 ASN A 155 4149 4981 3673 -482 110 -430 O ATOM 1157 ND2 ASN A 155 -73.219 110.201 15.804 1.00 33.77 N ANISOU 1157 ND2 ASN A 155 4170 5039 3623 -457 259 -485 N ATOM 1158 N SER A 156 -73.737 113.995 11.071 1.00 35.37 N ANISOU 1158 N SER A 156 4320 4983 4136 -354 -6 -402 N ATOM 1159 CA SER A 156 -74.306 115.159 10.390 1.00 36.63 C ANISOU 1159 CA SER A 156 4431 5074 4414 -302 -29 -349 C ATOM 1160 C SER A 156 -74.330 116.425 11.252 1.00 37.73 C ANISOU 1160 C SER A 156 4593 5121 4622 -241 83 -411 C ATOM 1161 O SER A 156 -75.275 117.204 11.199 1.00 38.95 O ANISOU 1161 O SER A 156 4667 5206 4925 -170 127 -370 O ATOM 1162 CB SER A 156 -75.713 114.827 9.870 1.00 37.53 C ANISOU 1162 CB SER A 156 4411 5210 4637 -281 -68 -254 C ATOM 1163 OG SER A 156 -75.675 113.663 9.065 1.00 37.30 O ANISOU 1163 OG SER A 156 4379 5259 4533 -360 -166 -218 O ATOM 1164 N GLY A 157 -73.278 116.618 12.043 1.00 37.93 N ANISOU 1164 N GLY A 157 4725 5144 4545 -275 130 -508 N ATOM 1165 CA GLY A 157 -73.178 117.769 12.936 1.00 38.80 C ANISOU 1165 CA GLY A 157 4885 5167 4690 -247 245 -600 C ATOM 1166 C GLY A 157 -73.888 117.632 14.273 1.00 39.76 C ANISOU 1166 C GLY A 157 4998 5299 4810 -227 384 -676 C ATOM 1167 O GLY A 157 -73.745 118.513 15.121 1.00 41.16 O ANISOU 1167 O GLY A 157 5241 5410 4987 -224 497 -780 O ATOM 1168 N ALA A 158 -74.631 116.542 14.487 1.00 39.27 N ANISOU 1168 N ALA A 158 4864 5316 4740 -223 388 -633 N ATOM 1169 CA ALA A 158 -75.321 116.311 15.760 1.00 40.34 C ANISOU 1169 CA ALA A 158 4989 5476 4863 -209 530 -694 C ATOM 1170 C ALA A 158 -74.359 115.993 16.904 1.00 40.19 C ANISOU 1170 C ALA A 158 5089 5532 4650 -290 566 -788 C ATOM 1171 O ALA A 158 -74.647 116.336 18.046 1.00 41.61 O ANISOU 1171 O ALA A 158 5312 5708 4789 -294 703 -878 O ATOM 1172 CB ALA A 158 -76.351 115.197 15.627 1.00 40.15 C ANISOU 1172 CB ALA A 158 4848 5518 4891 -193 517 -607 C ATOM 1173 N LEU A 159 -73.236 115.335 16.609 1.00 38.41 N ANISOU 1173 N LEU A 159 4912 5378 4305 -357 450 -760 N ATOM 1174 CA LEU A 159 -72.249 114.993 17.640 1.00 38.75 C ANISOU 1174 CA LEU A 159 5047 5508 4169 -440 456 -813 C ATOM 1175 C LEU A 159 -71.086 115.977 17.596 1.00 39.08 C ANISOU 1175 C LEU A 159 5183 5511 4156 -490 420 -879 C ATOM 1176 O LEU A 159 -70.303 115.971 16.651 1.00 38.70 O ANISOU 1176 O LEU A 159 5135 5449 4121 -502 313 -829 O ATOM 1177 CB LEU A 159 -71.743 113.563 17.452 1.00 37.39 C ANISOU 1177 CB LEU A 159 4846 5434 3925 -478 366 -721 C ATOM 1178 CG LEU A 159 -70.703 113.036 18.451 1.00 36.95 C ANISOU 1178 CG LEU A 159 4855 5485 3701 -561 350 -724 C ATOM 1179 CD1 LEU A 159 -71.277 112.993 19.865 1.00 38.42 C ANISOU 1179 CD1 LEU A 159 5068 5733 3795 -585 467 -776 C ATOM 1180 CD2 LEU A 159 -70.235 111.660 18.005 1.00 35.80 C ANISOU 1180 CD2 LEU A 159 4660 5395 3546 -575 269 -612 C ATOM 1181 N THR A 160 -70.993 116.831 18.612 1.00 41.12 N ANISOU 1181 N THR A 160 5525 5749 4351 -528 519 -999 N ATOM 1182 CA THR A 160 -69.906 117.816 18.717 1.00 41.90 C ANISOU 1182 CA THR A 160 5720 5807 4392 -598 492 -1079 C ATOM 1183 C THR A 160 -69.024 117.673 19.964 1.00 42.80 C ANISOU 1183 C THR A 160 5929 6038 4297 -723 491 -1147 C ATOM 1184 O THR A 160 -67.863 118.094 19.937 1.00 43.17 O ANISOU 1184 O THR A 160 6031 6097 4275 -805 413 -1170 O ATOM 1185 CB THR A 160 -70.466 119.249 18.670 1.00 43.14 C ANISOU 1185 CB THR A 160 5909 5803 4679 -552 609 -1178 C ATOM 1186 OG1 THR A 160 -71.416 119.427 19.722 1.00 44.58 O ANISOU 1186 OG1 THR A 160 6113 5973 4854 -536 776 -1270 O ATOM 1187 CG2 THR A 160 -71.141 119.512 17.329 1.00 42.41 C ANISOU 1187 CG2 THR A 160 5717 5606 4793 -441 575 -1078 C ATOM 1188 N SER A 161 -69.561 117.112 21.049 1.00 43.46 N ANISOU 1188 N SER A 161 6025 6212 4276 -748 572 -1171 N ATOM 1189 CA SER A 161 -68.791 116.924 22.284 1.00 44.38 C ANISOU 1189 CA SER A 161 6229 6466 4168 -881 560 -1217 C ATOM 1190 C SER A 161 -67.735 115.846 22.100 1.00 42.43 C ANISOU 1190 C SER A 161 5934 6345 3841 -928 400 -1073 C ATOM 1191 O SER A 161 -68.026 114.772 21.593 1.00 41.65 O ANISOU 1191 O SER A 161 5743 6272 3809 -861 361 -949 O ATOM 1192 CB SER A 161 -69.702 116.551 23.457 1.00 45.87 C ANISOU 1192 CB SER A 161 6443 6727 4259 -894 697 -1262 C ATOM 1193 OG SER A 161 -70.604 117.606 23.750 1.00 48.26 O ANISOU 1193 OG SER A 161 6795 6904 4636 -856 874 -1408 O ATOM 1194 N GLY A 162 -66.507 116.154 22.507 1.00 42.28 N ANISOU 1194 N GLY A 162 5975 6397 3694 -1047 313 -1090 N ATOM 1195 CA GLY A 162 -65.381 115.236 22.365 1.00 40.97 C ANISOU 1195 CA GLY A 162 5750 6343 3474 -1091 167 -942 C ATOM 1196 C GLY A 162 -64.800 115.120 20.962 1.00 38.92 C ANISOU 1196 C GLY A 162 5419 6001 3368 -1025 79 -857 C ATOM 1197 O GLY A 162 -63.892 114.322 20.751 1.00 38.37 O ANISOU 1197 O GLY A 162 5288 6002 3287 -1045 -19 -730 O ATOM 1198 N VAL A 163 -65.300 115.913 20.014 1.00 37.86 N ANISOU 1198 N VAL A 163 5288 5718 3378 -949 120 -917 N ATOM 1199 CA VAL A 163 -64.824 115.881 18.636 1.00 36.45 C ANISOU 1199 CA VAL A 163 5057 5465 3328 -895 48 -844 C ATOM 1200 C VAL A 163 -63.592 116.761 18.501 1.00 35.99 C ANISOU 1200 C VAL A 163 5041 5388 3245 -978 -19 -874 C ATOM 1201 O VAL A 163 -63.570 117.874 19.014 1.00 36.79 O ANISOU 1201 O VAL A 163 5223 5445 3312 -1038 23 -997 O ATOM 1202 CB VAL A 163 -65.906 116.374 17.649 1.00 36.21 C ANISOU 1202 CB VAL A 163 5006 5298 3456 -787 106 -869 C ATOM 1203 CG1 VAL A 163 -65.362 116.455 16.222 1.00 35.38 C ANISOU 1203 CG1 VAL A 163 4864 5127 3450 -752 31 -798 C ATOM 1204 CG2 VAL A 163 -67.118 115.463 17.714 1.00 36.04 C ANISOU 1204 CG2 VAL A 163 4923 5298 3472 -714 160 -827 C ATOM 1205 N HIS A 164 -62.572 116.262 17.801 1.00 34.86 N ANISOU 1205 N HIS A 164 4841 5272 3133 -985 -110 -766 N ATOM 1206 CA HIS A 164 -61.447 117.098 17.393 1.00 34.53 C ANISOU 1206 CA HIS A 164 4818 5194 3110 -1049 -170 -775 C ATOM 1207 C HIS A 164 -60.953 116.709 16.000 1.00 33.44 C ANISOU 1207 C HIS A 164 4616 5005 3086 -986 -209 -672 C ATOM 1208 O HIS A 164 -60.662 115.540 15.739 1.00 32.46 O ANISOU 1208 O HIS A 164 4422 4937 2972 -956 -234 -564 O ATOM 1209 CB HIS A 164 -60.303 117.017 18.410 1.00 35.45 C ANISOU 1209 CB HIS A 164 4938 5440 3092 -1183 -248 -753 C ATOM 1210 CG HIS A 164 -59.260 118.064 18.211 1.00 35.67 C ANISOU 1210 CG HIS A 164 4993 5429 3130 -1274 -301 -791 C ATOM 1211 ND1 HIS A 164 -59.454 119.381 18.561 1.00 36.50 N ANISOU 1211 ND1 HIS A 164 5198 5453 3218 -1339 -255 -944 N ATOM 1212 CD2 HIS A 164 -58.031 117.998 17.646 1.00 35.50 C ANISOU 1212 CD2 HIS A 164 4908 5425 3155 -1310 -383 -694 C ATOM 1213 CE1 HIS A 164 -58.378 120.078 18.244 1.00 37.17 C ANISOU 1213 CE1 HIS A 164 5282 5510 3330 -1421 -318 -941 C ATOM 1214 NE2 HIS A 164 -57.506 119.264 17.674 1.00 36.38 N ANISOU 1214 NE2 HIS A 164 5078 5473 3269 -1402 -398 -786 N ATOM 1215 N THR A 165 -60.881 117.696 15.110 1.00 33.07 N ANISOU 1215 N THR A 165 4596 4844 3126 -969 -202 -707 N ATOM 1216 CA THR A 165 -60.330 117.522 13.777 1.00 31.76 C ANISOU 1216 CA THR A 165 4389 4633 3046 -930 -230 -622 C ATOM 1217 C THR A 165 -58.960 118.208 13.721 1.00 32.34 C ANISOU 1217 C THR A 165 4463 4705 3119 -1019 -283 -608 C ATOM 1218 O THR A 165 -58.827 119.376 14.058 1.00 32.23 O ANISOU 1218 O THR A 165 4507 4635 3103 -1079 -278 -694 O ATOM 1219 CB THR A 165 -61.311 118.061 12.707 1.00 31.75 C ANISOU 1219 CB THR A 165 4406 4517 3142 -846 -190 -638 C ATOM 1220 OG1 THR A 165 -62.506 117.262 12.735 1.00 31.14 O ANISOU 1220 OG1 THR A 165 4304 4460 3070 -776 -156 -629 O ATOM 1221 CG2 THR A 165 -60.713 117.978 11.302 1.00 31.03 C ANISOU 1221 CG2 THR A 165 4292 4389 3111 -826 -216 -555 C ATOM 1222 N PHE A 166 -57.949 117.456 13.297 1.00 32.16 N ANISOU 1222 N PHE A 166 4371 4734 3113 -1028 -322 -500 N ATOM 1223 CA PHE A 166 -56.565 117.925 13.316 1.00 33.13 C ANISOU 1223 CA PHE A 166 4465 4878 3245 -1117 -376 -460 C ATOM 1224 C PHE A 166 -56.214 118.723 12.077 1.00 33.02 C ANISOU 1224 C PHE A 166 4466 4756 3324 -1101 -359 -450 C ATOM 1225 O PHE A 166 -56.855 118.554 11.050 1.00 32.55 O ANISOU 1225 O PHE A 166 4419 4634 3313 -1017 -316 -434 O ATOM 1226 CB PHE A 166 -55.624 116.740 13.466 1.00 32.92 C ANISOU 1226 CB PHE A 166 4336 4952 3219 -1125 -411 -328 C ATOM 1227 CG PHE A 166 -55.710 116.120 14.813 1.00 33.78 C ANISOU 1227 CG PHE A 166 4424 5183 3227 -1170 -450 -311 C ATOM 1228 CD1 PHE A 166 -54.956 116.631 15.856 1.00 35.18 C ANISOU 1228 CD1 PHE A 166 4598 5450 3320 -1300 -529 -319 C ATOM 1229 CD2 PHE A 166 -56.607 115.088 15.070 1.00 33.55 C ANISOU 1229 CD2 PHE A 166 4387 5184 3177 -1098 -410 -292 C ATOM 1230 CE1 PHE A 166 -55.044 116.092 17.119 1.00 36.08 C ANISOU 1230 CE1 PHE A 166 4700 5696 3314 -1358 -573 -294 C ATOM 1231 CE2 PHE A 166 -56.697 114.543 16.342 1.00 34.24 C ANISOU 1231 CE2 PHE A 166 4457 5390 3161 -1145 -443 -263 C ATOM 1232 CZ PHE A 166 -55.920 115.055 17.361 1.00 35.43 C ANISOU 1232 CZ PHE A 166 4607 5641 3212 -1275 -526 -262 C ATOM 1233 N PRO A 167 -55.192 119.598 12.174 1.00 34.71 N ANISOU 1233 N PRO A 167 4678 4956 3556 -1195 -398 -453 N ATOM 1234 CA PRO A 167 -54.712 120.272 10.960 1.00 34.88 C ANISOU 1234 CA PRO A 167 4701 4883 3670 -1185 -378 -417 C ATOM 1235 C PRO A 167 -54.103 119.275 9.975 1.00 34.78 C ANISOU 1235 C PRO A 167 4615 4898 3702 -1131 -354 -295 C ATOM 1236 O PRO A 167 -53.618 118.208 10.383 1.00 35.14 O ANISOU 1236 O PRO A 167 4585 5033 3733 -1129 -367 -226 O ATOM 1237 CB PRO A 167 -53.662 121.263 11.474 1.00 36.04 C ANISOU 1237 CB PRO A 167 4845 5025 3823 -1316 -429 -440 C ATOM 1238 CG PRO A 167 -53.274 120.782 12.831 1.00 36.65 C ANISOU 1238 CG PRO A 167 4889 5234 3802 -1401 -496 -447 C ATOM 1239 CD PRO A 167 -54.433 119.996 13.377 1.00 35.74 C ANISOU 1239 CD PRO A 167 4803 5163 3615 -1328 -466 -485 C ATOM 1240 N ALA A 168 -54.151 119.629 8.694 1.00 34.43 N ANISOU 1240 N ALA A 168 4594 4773 3714 -1090 -310 -268 N ATOM 1241 CA ALA A 168 -53.669 118.768 7.627 1.00 34.64 C ANISOU 1241 CA ALA A 168 4578 4810 3773 -1044 -258 -178 C ATOM 1242 C ALA A 168 -52.151 118.685 7.602 1.00 35.58 C ANISOU 1242 C ALA A 168 4608 4961 3948 -1102 -261 -90 C ATOM 1243 O ALA A 168 -51.460 119.626 7.986 1.00 37.08 O ANISOU 1243 O ALA A 168 4785 5141 4163 -1186 -308 -95 O ATOM 1244 CB ALA A 168 -54.180 119.246 6.275 1.00 34.36 C ANISOU 1244 CB ALA A 168 4606 4695 3753 -1003 -215 -172 C ATOM 1245 N VAL A 169 -51.658 117.524 7.184 1.00 35.48 N ANISOU 1245 N VAL A 169 4530 4983 3968 -1058 -205 -12 N ATOM 1246 CA VAL A 169 -50.248 117.297 6.910 1.00 36.35 C ANISOU 1246 CA VAL A 169 4537 5111 4163 -1088 -174 94 C ATOM 1247 C VAL A 169 -50.114 117.142 5.407 1.00 36.24 C ANISOU 1247 C VAL A 169 4557 5033 4179 -1043 -62 120 C ATOM 1248 O VAL A 169 -50.888 116.403 4.798 1.00 34.88 O ANISOU 1248 O VAL A 169 4442 4845 3967 -980 0 88 O ATOM 1249 CB VAL A 169 -49.759 116.007 7.597 1.00 37.05 C ANISOU 1249 CB VAL A 169 4514 5275 4289 -1062 -168 177 C ATOM 1250 CG1 VAL A 169 -48.386 115.588 7.080 1.00 38.06 C ANISOU 1250 CG1 VAL A 169 4520 5401 4540 -1062 -99 304 C ATOM 1251 CG2 VAL A 169 -49.729 116.201 9.108 1.00 37.73 C ANISOU 1251 CG2 VAL A 169 4563 5450 4323 -1132 -291 173 C ATOM 1252 N LEU A 170 -49.139 117.831 4.817 1.00 36.61 N ANISOU 1252 N LEU A 170 4572 5049 4288 -1089 -35 175 N ATOM 1253 CA LEU A 170 -48.773 117.613 3.419 1.00 36.97 C ANISOU 1253 CA LEU A 170 4639 5050 4358 -1060 91 215 C ATOM 1254 C LEU A 170 -47.680 116.540 3.332 1.00 38.49 C ANISOU 1254 C LEU A 170 4710 5264 4651 -1034 188 309 C ATOM 1255 O LEU A 170 -46.535 116.774 3.723 1.00 39.00 O ANISOU 1255 O LEU A 170 4653 5351 4814 -1078 171 398 O ATOM 1256 CB LEU A 170 -48.284 118.915 2.778 1.00 37.09 C ANISOU 1256 CB LEU A 170 4680 5014 4397 -1120 89 240 C ATOM 1257 CG LEU A 170 -47.889 118.819 1.296 1.00 37.35 C ANISOU 1257 CG LEU A 170 4748 5010 4433 -1106 224 287 C ATOM 1258 CD1 LEU A 170 -49.121 118.683 0.413 1.00 36.75 C ANISOU 1258 CD1 LEU A 170 4809 4917 4236 -1067 248 226 C ATOM 1259 CD2 LEU A 170 -47.052 120.014 0.863 1.00 37.98 C ANISOU 1259 CD2 LEU A 170 4808 5049 4573 -1175 228 348 C ATOM 1260 N GLN A 171 -48.021 115.393 2.750 1.00 39.17 N ANISOU 1260 N GLN A 171 4825 5334 4725 -966 300 294 N ATOM 1261 CA GLN A 171 -47.075 114.274 2.616 1.00 40.87 C ANISOU 1261 CA GLN A 171 4929 5541 5061 -923 428 378 C ATOM 1262 C GLN A 171 -46.088 114.486 1.456 1.00 40.79 C ANISOU 1262 C GLN A 171 4899 5483 5115 -934 573 432 C ATOM 1263 O GLN A 171 -46.270 115.390 0.631 1.00 40.50 O ANISOU 1263 O GLN A 171 4960 5424 5004 -974 579 399 O ATOM 1264 CB GLN A 171 -47.842 112.978 2.396 1.00 42.30 C ANISOU 1264 CB GLN A 171 5163 5697 5212 -855 515 323 C ATOM 1265 CG GLN A 171 -48.796 112.630 3.531 1.00 43.28 C ANISOU 1265 CG GLN A 171 5295 5868 5284 -839 394 283 C ATOM 1266 CD GLN A 171 -49.932 111.749 3.064 1.00 44.89 C ANISOU 1266 CD GLN A 171 5604 6039 5412 -798 455 190 C ATOM 1267 OE1 GLN A 171 -50.833 112.199 2.341 1.00 46.81 O ANISOU 1267 OE1 GLN A 171 5976 6271 5540 -817 439 103 O ATOM 1268 NE2 GLN A 171 -49.877 110.474 3.429 1.00 45.85 N ANISOU 1268 NE2 GLN A 171 5668 6143 5612 -746 528 220 N ATOM 1269 N SER A 172 -45.047 113.648 1.405 1.00 41.03 N ANISOU 1269 N SER A 172 4799 5496 5294 -896 699 527 N ATOM 1270 CA SER A 172 -44.036 113.676 0.328 1.00 42.16 C ANISOU 1270 CA SER A 172 4909 5589 5521 -897 878 584 C ATOM 1271 C SER A 172 -44.638 113.447 -1.063 1.00 41.61 C ANISOU 1271 C SER A 172 5016 5467 5326 -889 1027 479 C ATOM 1272 O SER A 172 -44.073 113.874 -2.065 1.00 42.34 O ANISOU 1272 O SER A 172 5139 5533 5415 -918 1144 499 O ATOM 1273 CB SER A 172 -42.911 112.671 0.606 1.00 43.53 C ANISOU 1273 CB SER A 172 4895 5740 5903 -839 1004 710 C ATOM 1274 OG SER A 172 -43.442 111.425 1.025 1.00 43.41 O ANISOU 1274 OG SER A 172 4878 5705 5912 -767 1043 686 O ATOM 1275 N SER A 173 -45.791 112.783 -1.110 1.00 40.40 N ANISOU 1275 N SER A 173 4979 5309 5062 -863 1016 373 N ATOM 1276 CA SER A 173 -46.561 112.630 -2.340 1.00 40.19 C ANISOU 1276 CA SER A 173 5134 5259 4876 -884 1108 264 C ATOM 1277 C SER A 173 -47.131 113.935 -2.946 1.00 39.52 C ANISOU 1277 C SER A 173 5168 5208 4639 -952 1002 240 C ATOM 1278 O SER A 173 -47.532 113.932 -4.104 1.00 40.39 O ANISOU 1278 O SER A 173 5415 5315 4615 -987 1082 186 O ATOM 1279 CB SER A 173 -47.719 111.678 -2.081 1.00 39.51 C ANISOU 1279 CB SER A 173 5125 5171 4717 -856 1083 166 C ATOM 1280 OG SER A 173 -48.568 112.214 -1.084 1.00 38.40 O ANISOU 1280 OG SER A 173 4979 5084 4527 -860 871 154 O ATOM 1281 N GLY A 174 -47.182 115.028 -2.180 1.00 38.22 N ANISOU 1281 N GLY A 174 4956 5073 4493 -976 828 281 N ATOM 1282 CA GLY A 174 -47.836 116.275 -2.626 1.00 37.46 C ANISOU 1282 CA GLY A 174 4962 4988 4283 -1026 722 268 C ATOM 1283 C GLY A 174 -49.324 116.325 -2.314 1.00 35.84 C ANISOU 1283 C GLY A 174 4847 4806 3964 -1015 589 188 C ATOM 1284 O GLY A 174 -50.017 117.267 -2.716 1.00 36.30 O ANISOU 1284 O GLY A 174 4986 4868 3940 -1044 506 187 O ATOM 1285 N LEU A 175 -49.813 115.328 -1.579 1.00 34.41 N ANISOU 1285 N LEU A 175 4640 4637 3796 -970 572 138 N ATOM 1286 CA LEU A 175 -51.219 115.244 -1.184 1.00 32.74 C ANISOU 1286 CA LEU A 175 4493 4449 3498 -955 458 66 C ATOM 1287 C LEU A 175 -51.350 115.402 0.329 1.00 31.92 C ANISOU 1287 C LEU A 175 4303 4363 3464 -932 337 67 C ATOM 1288 O LEU A 175 -50.433 115.051 1.080 1.00 32.05 O ANISOU 1288 O LEU A 175 4207 4387 3584 -922 354 117 O ATOM 1289 CB LEU A 175 -51.797 113.902 -1.615 1.00 32.41 C ANISOU 1289 CB LEU A 175 4509 4408 3399 -936 545 -3 C ATOM 1290 CG LEU A 175 -51.747 113.578 -3.111 1.00 33.09 C ANISOU 1290 CG LEU A 175 4706 4486 3381 -980 677 -32 C ATOM 1291 CD1 LEU A 175 -52.135 112.128 -3.374 1.00 33.25 C ANISOU 1291 CD1 LEU A 175 4773 4488 3373 -973 786 -117 C ATOM 1292 CD2 LEU A 175 -52.653 114.518 -3.885 1.00 33.13 C ANISOU 1292 CD2 LEU A 175 4817 4529 3243 -1031 579 -31 C ATOM 1293 N TYR A 176 -52.495 115.934 0.764 1.00 31.04 N ANISOU 1293 N TYR A 176 4238 4263 3293 -929 220 20 N ATOM 1294 CA TYR A 176 -52.754 116.173 2.180 1.00 30.70 C ANISOU 1294 CA TYR A 176 4139 4239 3285 -919 115 2 C ATOM 1295 C TYR A 176 -53.397 114.972 2.844 1.00 30.78 C ANISOU 1295 C TYR A 176 4132 4281 3283 -877 117 -36 C ATOM 1296 O TYR A 176 -54.055 114.164 2.186 1.00 30.16 O ANISOU 1296 O TYR A 176 4107 4197 3155 -857 170 -72 O ATOM 1297 CB TYR A 176 -53.675 117.371 2.391 1.00 30.02 C ANISOU 1297 CB TYR A 176 4109 4133 3164 -930 15 -34 C ATOM 1298 CG TYR A 176 -53.117 118.684 1.946 1.00 30.45 C ANISOU 1298 CG TYR A 176 4178 4141 3252 -974 1 8 C ATOM 1299 CD1 TYR A 176 -52.338 119.470 2.803 1.00 30.69 C ANISOU 1299 CD1 TYR A 176 4151 4156 3352 -1020 -44 18 C ATOM 1300 CD2 TYR A 176 -53.376 119.159 0.672 1.00 30.68 C ANISOU 1300 CD2 TYR A 176 4276 4143 3236 -983 30 42 C ATOM 1301 CE1 TYR A 176 -51.835 120.690 2.392 1.00 31.31 C ANISOU 1301 CE1 TYR A 176 4244 4177 3476 -1068 -51 54 C ATOM 1302 CE2 TYR A 176 -52.881 120.368 0.254 1.00 31.32 C ANISOU 1302 CE2 TYR A 176 4368 4174 3358 -1022 23 95 C ATOM 1303 CZ TYR A 176 -52.122 121.127 1.120 1.00 31.52 C ANISOU 1303 CZ TYR A 176 4337 4167 3472 -1062 -13 97 C ATOM 1304 OH TYR A 176 -51.660 122.305 0.672 1.00 32.34 O ANISOU 1304 OH TYR A 176 4453 4208 3627 -1107 -13 148 O ATOM 1305 N SER A 177 -53.200 114.881 4.157 1.00 31.10 N ANISOU 1305 N SER A 177 4098 4355 3362 -876 56 -26 N ATOM 1306 CA SER A 177 -53.935 113.949 4.992 1.00 31.11 C ANISOU 1306 CA SER A 177 4082 4390 3347 -840 37 -53 C ATOM 1307 C SER A 177 -54.300 114.621 6.314 1.00 30.71 C ANISOU 1307 C SER A 177 4017 4379 3271 -863 -71 -81 C ATOM 1308 O SER A 177 -53.560 115.459 6.820 1.00 31.09 O ANISOU 1308 O SER A 177 4033 4440 3341 -914 -121 -61 O ATOM 1309 CB SER A 177 -53.122 112.684 5.242 1.00 31.97 C ANISOU 1309 CB SER A 177 4102 4510 3534 -814 113 14 C ATOM 1310 OG SER A 177 -53.044 111.885 4.061 1.00 34.05 O ANISOU 1310 OG SER A 177 4403 4723 3812 -791 241 5 O ATOM 1311 N LEU A 178 -55.443 114.255 6.868 1.00 30.04 N ANISOU 1311 N LEU A 178 3961 4314 3140 -835 -97 -134 N ATOM 1312 CA LEU A 178 -55.781 114.670 8.226 1.00 30.59 C ANISOU 1312 CA LEU A 178 4020 4429 3176 -858 -171 -167 C ATOM 1313 C LEU A 178 -56.572 113.595 8.933 1.00 30.24 C ANISOU 1313 C LEU A 178 3959 4427 3105 -821 -163 -174 C ATOM 1314 O LEU A 178 -57.018 112.621 8.306 1.00 29.61 O ANISOU 1314 O LEU A 178 3885 4326 3040 -778 -105 -168 O ATOM 1315 CB LEU A 178 -56.516 116.022 8.236 1.00 30.97 C ANISOU 1315 CB LEU A 178 4140 4432 3196 -873 -211 -243 C ATOM 1316 CG LEU A 178 -57.926 116.262 7.682 1.00 31.00 C ANISOU 1316 CG LEU A 178 4205 4390 3182 -825 -203 -295 C ATOM 1317 CD1 LEU A 178 -59.020 115.526 8.447 1.00 30.92 C ANISOU 1317 CD1 LEU A 178 4189 4419 3141 -789 -203 -331 C ATOM 1318 CD2 LEU A 178 -58.202 117.765 7.722 1.00 31.76 C ANISOU 1318 CD2 LEU A 178 4346 4421 3299 -843 -230 -338 C ATOM 1319 N SER A 179 -56.738 113.781 10.237 1.00 30.07 N ANISOU 1319 N SER A 179 3924 4465 3038 -850 -216 -191 N ATOM 1320 CA SER A 179 -57.523 112.867 11.052 1.00 30.38 C ANISOU 1320 CA SER A 179 3947 4551 3043 -823 -209 -191 C ATOM 1321 C SER A 179 -58.542 113.674 11.851 1.00 30.10 C ANISOU 1321 C SER A 179 3970 4527 2939 -837 -237 -285 C ATOM 1322 O SER A 179 -58.353 114.868 12.122 1.00 29.97 O ANISOU 1322 O SER A 179 3993 4494 2900 -884 -268 -341 O ATOM 1323 CB SER A 179 -56.630 112.031 11.971 1.00 30.92 C ANISOU 1323 CB SER A 179 3927 4702 3121 -846 -229 -87 C ATOM 1324 OG SER A 179 -55.897 112.879 12.822 1.00 33.18 O ANISOU 1324 OG SER A 179 4199 5050 3358 -928 -305 -82 O ATOM 1325 N SER A 180 -59.662 113.033 12.149 1.00 29.67 N ANISOU 1325 N SER A 180 3923 4483 2867 -795 -209 -308 N ATOM 1326 CA SER A 180 -60.672 113.599 13.025 1.00 30.02 C ANISOU 1326 CA SER A 180 4009 4542 2857 -800 -207 -390 C ATOM 1327 C SER A 180 -61.014 112.508 14.019 1.00 30.21 C ANISOU 1327 C SER A 180 3996 4646 2837 -796 -194 -349 C ATOM 1328 O SER A 180 -61.103 111.345 13.636 1.00 30.19 O ANISOU 1328 O SER A 180 3949 4641 2879 -758 -167 -284 O ATOM 1329 CB SER A 180 -61.908 114.030 12.232 1.00 29.72 C ANISOU 1329 CB SER A 180 4005 4425 2861 -744 -178 -446 C ATOM 1330 OG SER A 180 -62.926 114.528 13.094 1.00 29.79 O ANISOU 1330 OG SER A 180 4040 4435 2844 -735 -151 -519 O ATOM 1331 N VAL A 181 -61.168 112.875 15.288 1.00 31.08 N ANISOU 1331 N VAL A 181 4129 4824 2857 -845 -205 -388 N ATOM 1332 CA VAL A 181 -61.336 111.898 16.367 1.00 31.63 C ANISOU 1332 CA VAL A 181 4164 4991 2863 -859 -200 -328 C ATOM 1333 C VAL A 181 -62.500 112.340 17.254 1.00 32.36 C ANISOU 1333 C VAL A 181 4311 5103 2881 -865 -152 -425 C ATOM 1334 O VAL A 181 -62.790 113.541 17.387 1.00 32.81 O ANISOU 1334 O VAL A 181 4434 5116 2916 -887 -134 -537 O ATOM 1335 CB VAL A 181 -60.028 111.671 17.201 1.00 32.59 C ANISOU 1335 CB VAL A 181 4241 5223 2919 -940 -271 -233 C ATOM 1336 CG1 VAL A 181 -58.850 111.341 16.284 1.00 32.53 C ANISOU 1336 CG1 VAL A 181 4165 5181 3013 -926 -298 -136 C ATOM 1337 CG2 VAL A 181 -59.719 112.888 18.074 1.00 33.53 C ANISOU 1337 CG2 VAL A 181 4426 5394 2920 -1044 -313 -323 C ATOM 1338 N VAL A 182 -63.174 111.356 17.835 1.00 32.63 N ANISOU 1338 N VAL A 182 4316 5189 2893 -842 -115 -379 N ATOM 1339 CA VAL A 182 -64.198 111.593 18.846 1.00 33.63 C ANISOU 1339 CA VAL A 182 4484 5355 2939 -854 -53 -451 C ATOM 1340 C VAL A 182 -63.943 110.654 20.024 1.00 34.85 C ANISOU 1340 C VAL A 182 4610 5643 2988 -904 -65 -354 C ATOM 1341 O VAL A 182 -63.644 109.473 19.833 1.00 34.79 O ANISOU 1341 O VAL A 182 4529 5655 3036 -875 -82 -224 O ATOM 1342 CB VAL A 182 -65.628 111.460 18.264 1.00 32.97 C ANISOU 1342 CB VAL A 182 4387 5187 2954 -767 22 -493 C ATOM 1343 CG1 VAL A 182 -65.916 110.054 17.758 1.00 32.50 C ANISOU 1343 CG1 VAL A 182 4254 5123 2972 -719 26 -391 C ATOM 1344 CG2 VAL A 182 -66.671 111.909 19.278 1.00 33.64 C ANISOU 1344 CG2 VAL A 182 4511 5295 2975 -773 109 -580 C ATOM 1345 N THR A 183 -64.019 111.207 21.231 1.00 36.47 N ANISOU 1345 N THR A 183 4878 5936 3041 -985 -52 -416 N ATOM 1346 CA THR A 183 -63.928 110.439 22.457 1.00 38.49 C ANISOU 1346 CA THR A 183 5121 6338 3164 -1046 -60 -326 C ATOM 1347 C THR A 183 -65.351 110.211 22.946 1.00 39.16 C ANISOU 1347 C THR A 183 5228 6418 3233 -1005 58 -379 C ATOM 1348 O THR A 183 -66.060 111.173 23.259 1.00 40.79 O ANISOU 1348 O THR A 183 5511 6590 3397 -1015 139 -529 O ATOM 1349 CB THR A 183 -63.111 111.195 23.524 1.00 39.76 C ANISOU 1349 CB THR A 183 5351 6623 3133 -1189 -121 -365 C ATOM 1350 OG1 THR A 183 -61.810 111.479 22.998 1.00 39.79 O ANISOU 1350 OG1 THR A 183 5319 6623 3176 -1227 -231 -313 O ATOM 1351 CG2 THR A 183 -62.965 110.370 24.799 1.00 41.09 C ANISOU 1351 CG2 THR A 183 5504 6970 3140 -1267 -147 -244 C ATOM 1352 N VAL A 184 -65.759 108.944 23.012 1.00 38.59 N ANISOU 1352 N VAL A 184 5083 6370 3210 -959 81 -255 N ATOM 1353 CA VAL A 184 -67.127 108.565 23.396 1.00 38.62 C ANISOU 1353 CA VAL A 184 5083 6366 3226 -916 195 -280 C ATOM 1354 C VAL A 184 -67.093 107.596 24.581 1.00 39.29 C ANISOU 1354 C VAL A 184 5147 6593 3189 -970 203 -150 C ATOM 1355 O VAL A 184 -66.035 107.052 24.890 1.00 39.75 O ANISOU 1355 O VAL A 184 5168 6737 3196 -1018 111 -12 O ATOM 1356 CB VAL A 184 -67.891 107.929 22.208 1.00 37.68 C ANISOU 1356 CB VAL A 184 4890 6119 3309 -810 225 -257 C ATOM 1357 CG1 VAL A 184 -67.902 108.883 21.022 1.00 36.85 C ANISOU 1357 CG1 VAL A 184 4803 5891 3306 -766 203 -360 C ATOM 1358 CG2 VAL A 184 -67.294 106.580 21.798 1.00 37.26 C ANISOU 1358 CG2 VAL A 184 4754 6063 3340 -790 175 -96 C ATOM 1359 N PRO A 185 -68.244 107.379 25.253 1.00 39.65 N ANISOU 1359 N PRO A 185 5205 6665 3195 -960 317 -176 N ATOM 1360 CA PRO A 185 -68.275 106.336 26.292 1.00 40.48 C ANISOU 1360 CA PRO A 185 5280 6900 3199 -1005 331 -25 C ATOM 1361 C PRO A 185 -68.136 104.943 25.667 1.00 39.17 C ANISOU 1361 C PRO A 185 5000 6681 3204 -938 299 150 C ATOM 1362 O PRO A 185 -68.828 104.640 24.697 1.00 37.51 O ANISOU 1362 O PRO A 185 4743 6337 3171 -855 341 117 O ATOM 1363 CB PRO A 185 -69.665 106.505 26.934 1.00 41.38 C ANISOU 1363 CB PRO A 185 5429 7023 3271 -994 485 -112 C ATOM 1364 CG PRO A 185 -70.148 107.848 26.504 1.00 41.24 C ANISOU 1364 CG PRO A 185 5476 6905 3289 -966 546 -317 C ATOM 1365 CD PRO A 185 -69.532 108.092 25.163 1.00 39.86 C ANISOU 1365 CD PRO A 185 5264 6611 3270 -911 444 -327 C ATOM 1366 N SER A 186 -67.253 104.117 26.220 1.00 40.05 N ANISOU 1366 N SER A 186 5065 6890 3263 -982 228 335 N ATOM 1367 CA SER A 186 -66.987 102.777 25.678 1.00 39.65 C ANISOU 1367 CA SER A 186 4905 6768 3390 -920 214 508 C ATOM 1368 C SER A 186 -68.187 101.824 25.793 1.00 39.68 C ANISOU 1368 C SER A 186 4866 6726 3485 -876 325 555 C ATOM 1369 O SER A 186 -68.285 100.853 25.030 1.00 39.01 O ANISOU 1369 O SER A 186 4708 6523 3592 -815 344 628 O ATOM 1370 CB SER A 186 -65.743 102.168 26.332 1.00 40.99 C ANISOU 1370 CB SER A 186 5020 7055 3501 -973 117 721 C ATOM 1371 OG SER A 186 -65.836 102.220 27.743 1.00 43.13 O ANISOU 1371 OG SER A 186 5329 7511 3546 -1068 113 788 O ATOM 1372 N SER A 187 -69.107 102.119 26.711 1.00 40.32 N ANISOU 1372 N SER A 187 4994 6890 3434 -912 408 503 N ATOM 1373 CA SER A 187 -70.342 101.344 26.849 1.00 40.51 C ANISOU 1373 CA SER A 187 4974 6874 3545 -876 523 536 C ATOM 1374 C SER A 187 -71.359 101.575 25.708 1.00 39.24 C ANISOU 1374 C SER A 187 4790 6554 3565 -802 579 393 C ATOM 1375 O SER A 187 -72.317 100.808 25.588 1.00 39.05 O ANISOU 1375 O SER A 187 4706 6474 3658 -774 656 432 O ATOM 1376 CB SER A 187 -71.003 101.632 28.197 1.00 42.12 C ANISOU 1376 CB SER A 187 5235 7221 3547 -941 612 523 C ATOM 1377 OG SER A 187 -71.429 102.981 28.289 1.00 42.39 O ANISOU 1377 OG SER A 187 5360 7260 3486 -955 661 313 O ATOM 1378 N SER A 188 -71.156 102.620 24.893 1.00 38.09 N ANISOU 1378 N SER A 188 4687 6343 3443 -779 534 244 N ATOM 1379 CA SER A 188 -72.038 102.935 23.761 1.00 37.22 C ANISOU 1379 CA SER A 188 4550 6099 3492 -718 561 129 C ATOM 1380 C SER A 188 -71.593 102.271 22.447 1.00 35.73 C ANISOU 1380 C SER A 188 4314 5791 3469 -684 494 164 C ATOM 1381 O SER A 188 -72.333 102.305 21.452 1.00 34.38 O ANISOU 1381 O SER A 188 4115 5522 3427 -651 503 95 O ATOM 1382 CB SER A 188 -72.124 104.454 23.562 1.00 37.18 C ANISOU 1382 CB SER A 188 4615 6080 3433 -711 559 -39 C ATOM 1383 OG SER A 188 -70.904 104.980 23.060 1.00 36.85 O ANISOU 1383 OG SER A 188 4614 6026 3361 -725 455 -61 O ATOM 1384 N LEU A 189 -70.403 101.665 22.447 1.00 35.64 N ANISOU 1384 N LEU A 189 4293 5792 3457 -698 434 275 N ATOM 1385 CA LEU A 189 -69.829 101.072 21.236 1.00 34.75 C ANISOU 1385 CA LEU A 189 4149 5560 3493 -670 395 297 C ATOM 1386 C LEU A 189 -70.645 99.881 20.758 1.00 34.57 C ANISOU 1386 C LEU A 189 4068 5440 3627 -656 457 338 C ATOM 1387 O LEU A 189 -71.068 99.042 21.554 1.00 35.25 O ANISOU 1387 O LEU A 189 4112 5557 3723 -668 516 444 O ATOM 1388 CB LEU A 189 -68.368 100.653 21.472 1.00 35.31 C ANISOU 1388 CB LEU A 189 4204 5664 3549 -681 338 427 C ATOM 1389 CG LEU A 189 -67.396 101.813 21.712 1.00 35.29 C ANISOU 1389 CG LEU A 189 4253 5743 3413 -711 256 383 C ATOM 1390 CD1 LEU A 189 -66.065 101.281 22.209 1.00 36.22 C ANISOU 1390 CD1 LEU A 189 4324 5925 3514 -732 197 555 C ATOM 1391 CD2 LEU A 189 -67.213 102.662 20.458 1.00 34.33 C ANISOU 1391 CD2 LEU A 189 4170 5528 3345 -686 221 244 C ATOM 1392 N GLY A 190 -70.877 99.826 19.452 1.00 33.71 N ANISOU 1392 N GLY A 190 3960 5217 3632 -643 444 253 N ATOM 1393 CA GLY A 190 -71.710 98.796 18.852 1.00 33.62 C ANISOU 1393 CA GLY A 190 3905 5107 3763 -653 494 258 C ATOM 1394 C GLY A 190 -73.205 98.921 19.115 1.00 33.75 C ANISOU 1394 C GLY A 190 3884 5145 3794 -664 538 217 C ATOM 1395 O GLY A 190 -73.947 97.983 18.834 1.00 34.28 O ANISOU 1395 O GLY A 190 3903 5147 3977 -688 581 240 O ATOM 1396 N THR A 191 -73.654 100.065 19.642 1.00 33.40 N ANISOU 1396 N THR A 191 3858 5184 3649 -648 536 154 N ATOM 1397 CA THR A 191 -75.089 100.356 19.787 1.00 33.69 C ANISOU 1397 CA THR A 191 3846 5232 3724 -645 587 109 C ATOM 1398 C THR A 191 -75.392 101.739 19.219 1.00 33.69 C ANISOU 1398 C THR A 191 3868 5228 3704 -616 546 -10 C ATOM 1399 O THR A 191 -76.239 101.874 18.332 1.00 33.35 O ANISOU 1399 O THR A 191 3777 5133 3761 -615 522 -53 O ATOM 1400 CB THR A 191 -75.565 100.222 21.250 1.00 34.62 C ANISOU 1400 CB THR A 191 3946 5446 3763 -649 682 175 C ATOM 1401 OG1 THR A 191 -74.769 101.040 22.112 1.00 34.40 O ANISOU 1401 OG1 THR A 191 3993 5514 3564 -649 675 162 O ATOM 1402 CG2 THR A 191 -75.473 98.771 21.697 1.00 35.21 C ANISOU 1402 CG2 THR A 191 3979 5508 3893 -677 726 316 C ATOM 1403 N GLN A 192 -74.697 102.760 19.722 1.00 33.89 N ANISOU 1403 N GLN A 192 3962 5308 3608 -600 534 -54 N ATOM 1404 CA GLN A 192 -74.624 104.058 19.049 1.00 33.77 C ANISOU 1404 CA GLN A 192 3982 5263 3586 -573 485 -156 C ATOM 1405 C GLN A 192 -73.802 103.908 17.785 1.00 32.96 C ANISOU 1405 C GLN A 192 3904 5095 3524 -582 389 -165 C ATOM 1406 O GLN A 192 -72.860 103.111 17.758 1.00 33.42 O ANISOU 1406 O GLN A 192 3980 5147 3570 -603 370 -106 O ATOM 1407 CB GLN A 192 -73.965 105.114 19.949 1.00 34.39 C ANISOU 1407 CB GLN A 192 4140 5406 3521 -572 502 -207 C ATOM 1408 CG GLN A 192 -74.789 105.482 21.169 1.00 36.02 C ANISOU 1408 CG GLN A 192 4346 5674 3665 -569 620 -231 C ATOM 1409 CD GLN A 192 -76.101 106.144 20.800 1.00 36.47 C ANISOU 1409 CD GLN A 192 4342 5674 3841 -519 680 -292 C ATOM 1410 OE1 GLN A 192 -76.124 107.110 20.035 1.00 36.87 O ANISOU 1410 OE1 GLN A 192 4401 5661 3947 -485 640 -357 O ATOM 1411 NE2 GLN A 192 -77.198 105.620 21.325 1.00 37.75 N ANISOU 1411 NE2 GLN A 192 4432 5856 4057 -511 777 -252 N ATOM 1412 N THR A 193 -74.161 104.656 16.741 1.00 32.53 N ANISOU 1412 N THR A 193 3846 4991 3524 -566 338 -228 N ATOM 1413 CA THR A 193 -73.367 104.708 15.514 1.00 31.52 C ANISOU 1413 CA THR A 193 3757 4811 3408 -581 255 -248 C ATOM 1414 C THR A 193 -72.619 106.030 15.451 1.00 31.00 C ANISOU 1414 C THR A 193 3753 4749 3275 -559 219 -301 C ATOM 1415 O THR A 193 -73.160 107.078 15.808 1.00 31.15 O ANISOU 1415 O THR A 193 3770 4775 3289 -527 243 -347 O ATOM 1416 CB THR A 193 -74.219 104.580 14.238 1.00 31.30 C ANISOU 1416 CB THR A 193 3687 4734 3471 -602 203 -265 C ATOM 1417 OG1 THR A 193 -75.124 105.684 14.154 1.00 31.46 O ANISOU 1417 OG1 THR A 193 3667 4760 3526 -564 194 -292 O ATOM 1418 CG2 THR A 193 -74.988 103.280 14.221 1.00 32.02 C ANISOU 1418 CG2 THR A 193 3717 4811 3637 -644 234 -225 C ATOM 1419 N TYR A 194 -71.389 105.970 14.953 1.00 30.55 N ANISOU 1419 N TYR A 194 3748 4676 3185 -575 172 -296 N ATOM 1420 CA TYR A 194 -70.526 107.133 14.815 1.00 30.21 C ANISOU 1420 CA TYR A 194 3762 4631 3086 -567 132 -338 C ATOM 1421 C TYR A 194 -70.046 107.216 13.361 1.00 30.15 C ANISOU 1421 C TYR A 194 3778 4566 3112 -579 71 -349 C ATOM 1422 O TYR A 194 -69.292 106.357 12.896 1.00 29.71 O ANISOU 1422 O TYR A 194 3734 4490 3066 -602 68 -318 O ATOM 1423 CB TYR A 194 -69.371 107.011 15.797 1.00 29.97 C ANISOU 1423 CB TYR A 194 3762 4658 2967 -588 138 -304 C ATOM 1424 CG TYR A 194 -69.858 106.967 17.234 1.00 30.51 C ANISOU 1424 CG TYR A 194 3823 4801 2968 -595 199 -295 C ATOM 1425 CD1 TYR A 194 -70.416 108.099 17.826 1.00 30.91 C ANISOU 1425 CD1 TYR A 194 3904 4866 2975 -585 238 -375 C ATOM 1426 CD2 TYR A 194 -69.789 105.792 17.994 1.00 30.46 C ANISOU 1426 CD2 TYR A 194 3783 4845 2945 -612 232 -203 C ATOM 1427 CE1 TYR A 194 -70.889 108.073 19.131 1.00 31.52 C ANISOU 1427 CE1 TYR A 194 3988 5014 2973 -600 314 -381 C ATOM 1428 CE2 TYR A 194 -70.250 105.762 19.303 1.00 31.25 C ANISOU 1428 CE2 TYR A 194 3884 5027 2962 -628 291 -189 C ATOM 1429 CZ TYR A 194 -70.800 106.906 19.868 1.00 31.80 C ANISOU 1429 CZ TYR A 194 3994 5119 2969 -626 335 -285 C ATOM 1430 OH TYR A 194 -71.259 106.893 21.171 1.00 32.42 O ANISOU 1430 OH TYR A 194 4088 5282 2947 -651 414 -285 O ATOM 1431 N THR A 195 -70.502 108.255 12.659 1.00 30.68 N ANISOU 1431 N THR A 195 3852 4604 3202 -562 34 -387 N ATOM 1432 CA THR A 195 -70.280 108.418 11.231 1.00 30.53 C ANISOU 1432 CA THR A 195 3855 4545 3200 -582 -27 -391 C ATOM 1433 C THR A 195 -69.591 109.745 10.982 1.00 31.09 C ANISOU 1433 C THR A 195 3972 4594 3245 -566 -58 -414 C ATOM 1434 O THR A 195 -70.118 110.789 11.367 1.00 31.62 O ANISOU 1434 O THR A 195 4030 4649 3335 -531 -49 -437 O ATOM 1435 CB THR A 195 -71.620 108.378 10.461 1.00 30.24 C ANISOU 1435 CB THR A 195 3765 4499 3224 -589 -62 -381 C ATOM 1436 OG1 THR A 195 -72.314 107.177 10.787 1.00 29.61 O ANISOU 1436 OG1 THR A 195 3637 4435 3178 -612 -28 -364 O ATOM 1437 CG2 THR A 195 -71.414 108.419 8.941 1.00 30.40 C ANISOU 1437 CG2 THR A 195 3819 4501 3230 -634 -133 -378 C ATOM 1438 N CYS A 196 -68.413 109.705 10.359 1.00 31.95 N ANISOU 1438 N CYS A 196 4129 4689 3322 -591 -79 -408 N ATOM 1439 CA CYS A 196 -67.730 110.931 9.958 1.00 32.86 C ANISOU 1439 CA CYS A 196 4286 4777 3422 -587 -111 -421 C ATOM 1440 C CYS A 196 -68.193 111.342 8.559 1.00 32.64 C ANISOU 1440 C CYS A 196 4266 4720 3416 -596 -164 -406 C ATOM 1441 O CYS A 196 -68.267 110.511 7.637 1.00 31.94 O ANISOU 1441 O CYS A 196 4186 4637 3313 -635 -179 -393 O ATOM 1442 CB CYS A 196 -66.210 110.799 10.032 1.00 34.38 C ANISOU 1442 CB CYS A 196 4512 4974 3577 -611 -106 -409 C ATOM 1443 SG CYS A 196 -65.455 109.742 8.795 1.00 37.07 S ANISOU 1443 SG CYS A 196 4873 5292 3921 -644 -93 -381 S ATOM 1444 N ASN A 197 -68.542 112.618 8.431 1.00 32.24 N ANISOU 1444 N ASN A 197 4213 4638 3399 -566 -188 -404 N ATOM 1445 CA ASN A 197 -69.039 113.181 7.186 1.00 32.88 C ANISOU 1445 CA ASN A 197 4288 4701 3504 -571 -250 -359 C ATOM 1446 C ASN A 197 -67.936 114.088 6.678 1.00 33.00 C ANISOU 1446 C ASN A 197 4362 4680 3497 -582 -264 -351 C ATOM 1447 O ASN A 197 -67.625 115.103 7.303 1.00 32.59 O ANISOU 1447 O ASN A 197 4320 4584 3477 -553 -241 -373 O ATOM 1448 CB ASN A 197 -70.334 113.970 7.405 1.00 33.69 C ANISOU 1448 CB ASN A 197 4321 4780 3699 -517 -258 -332 C ATOM 1449 CG ASN A 197 -71.217 113.357 8.476 1.00 33.95 C ANISOU 1449 CG ASN A 197 4296 4837 3767 -491 -203 -357 C ATOM 1450 OD1 ASN A 197 -71.298 113.865 9.598 1.00 34.53 O ANISOU 1450 OD1 ASN A 197 4367 4888 3866 -451 -133 -401 O ATOM 1451 ND2 ASN A 197 -71.861 112.252 8.148 1.00 33.85 N ANISOU 1451 ND2 ASN A 197 4244 4870 3750 -525 -227 -335 N ATOM 1452 N VAL A 198 -67.313 113.678 5.578 1.00 32.61 N ANISOU 1452 N VAL A 198 4355 4645 3390 -631 -288 -329 N ATOM 1453 CA VAL A 198 -66.158 114.373 5.024 1.00 32.90 C ANISOU 1453 CA VAL A 198 4445 4654 3403 -650 -289 -315 C ATOM 1454 C VAL A 198 -66.612 115.118 3.784 1.00 33.70 C ANISOU 1454 C VAL A 198 4555 4747 3501 -664 -352 -247 C ATOM 1455 O VAL A 198 -67.265 114.545 2.921 1.00 33.10 O ANISOU 1455 O VAL A 198 4477 4716 3382 -703 -396 -218 O ATOM 1456 CB VAL A 198 -65.044 113.372 4.679 1.00 32.97 C ANISOU 1456 CB VAL A 198 4492 4681 3353 -694 -246 -331 C ATOM 1457 CG1 VAL A 198 -63.868 114.074 4.020 1.00 33.16 C ANISOU 1457 CG1 VAL A 198 4562 4679 3359 -717 -238 -306 C ATOM 1458 CG2 VAL A 198 -64.603 112.642 5.942 1.00 32.87 C ANISOU 1458 CG2 VAL A 198 4453 4681 3356 -678 -195 -364 C ATOM 1459 N ASP A 199 -66.276 116.402 3.716 1.00 34.33 N ANISOU 1459 N ASP A 199 4645 4772 3627 -640 -361 -215 N ATOM 1460 CA ASP A 199 -66.690 117.263 2.615 1.00 35.57 C ANISOU 1460 CA ASP A 199 4801 4916 3799 -645 -423 -121 C ATOM 1461 C ASP A 199 -65.439 117.865 1.992 1.00 35.07 C ANISOU 1461 C ASP A 199 4800 4824 3702 -678 -408 -97 C ATOM 1462 O ASP A 199 -64.683 118.556 2.674 1.00 34.63 O ANISOU 1462 O ASP A 199 4754 4707 3697 -660 -367 -129 O ATOM 1463 CB ASP A 199 -67.604 118.359 3.162 1.00 37.46 C ANISOU 1463 CB ASP A 199 4978 5087 4169 -571 -429 -87 C ATOM 1464 CG ASP A 199 -68.123 119.298 2.093 1.00 39.76 C ANISOU 1464 CG ASP A 199 5243 5356 4506 -563 -498 44 C ATOM 1465 OD1 ASP A 199 -68.438 118.852 0.976 1.00 41.27 O ANISOU 1465 OD1 ASP A 199 5439 5627 4616 -618 -573 118 O ATOM 1466 OD2 ASP A 199 -68.218 120.507 2.379 1.00 42.07 O ANISOU 1466 OD2 ASP A 199 5515 5551 4920 -507 -475 77 O ATOM 1467 N HIS A 200 -65.193 117.551 0.722 1.00 34.07 N ANISOU 1467 N HIS A 200 4719 4747 3480 -740 -436 -47 N ATOM 1468 CA HIS A 200 -64.053 118.102 -0.011 1.00 33.85 C ANISOU 1468 CA HIS A 200 4748 4699 3415 -777 -413 -10 C ATOM 1469 C HIS A 200 -64.579 118.808 -1.248 1.00 35.14 C ANISOU 1469 C HIS A 200 4922 4884 3547 -804 -487 113 C ATOM 1470 O HIS A 200 -64.693 118.205 -2.315 1.00 34.69 O ANISOU 1470 O HIS A 200 4910 4906 3363 -877 -514 141 O ATOM 1471 CB HIS A 200 -63.059 116.993 -0.372 1.00 33.04 C ANISOU 1471 CB HIS A 200 4700 4638 3217 -833 -344 -67 C ATOM 1472 CG HIS A 200 -61.848 117.470 -1.112 1.00 32.64 C ANISOU 1472 CG HIS A 200 4699 4569 3133 -871 -299 -30 C ATOM 1473 ND1 HIS A 200 -61.023 118.480 -0.666 1.00 32.27 N ANISOU 1473 ND1 HIS A 200 4637 4454 3168 -849 -279 -10 N ATOM 1474 CD2 HIS A 200 -61.306 117.027 -2.264 1.00 32.63 C ANISOU 1474 CD2 HIS A 200 4766 4610 3023 -939 -258 -15 C ATOM 1475 CE1 HIS A 200 -60.038 118.646 -1.531 1.00 32.24 C ANISOU 1475 CE1 HIS A 200 4678 4453 3118 -896 -233 30 C ATOM 1476 NE2 HIS A 200 -60.186 117.775 -2.508 1.00 32.76 N ANISOU 1476 NE2 HIS A 200 4798 4585 3065 -948 -212 26 N ATOM 1477 N LYS A 201 -64.898 120.090 -1.072 1.00 36.09 N ANISOU 1477 N LYS A 201 5002 4927 3782 -750 -514 188 N ATOM 1478 CA LYS A 201 -65.500 120.907 -2.125 1.00 38.22 C ANISOU 1478 CA LYS A 201 5258 5208 4058 -760 -594 343 C ATOM 1479 C LYS A 201 -64.657 121.045 -3.392 1.00 39.03 C ANISOU 1479 C LYS A 201 5439 5355 4037 -840 -597 415 C ATOM 1480 O LYS A 201 -65.213 120.964 -4.485 1.00 39.78 O ANISOU 1480 O LYS A 201 5546 5536 4031 -897 -676 519 O ATOM 1481 CB LYS A 201 -65.858 122.295 -1.603 1.00 39.77 C ANISOU 1481 CB LYS A 201 5394 5279 4439 -676 -592 408 C ATOM 1482 CG LYS A 201 -67.017 122.294 -0.626 1.00 40.54 C ANISOU 1482 CG LYS A 201 5404 5338 4660 -596 -592 376 C ATOM 1483 CD LYS A 201 -67.239 123.692 -0.068 1.00 42.01 C ANISOU 1483 CD LYS A 201 5547 5371 5043 -513 -549 416 C ATOM 1484 CE LYS A 201 -68.222 123.750 1.081 1.00 42.40 C ANISOU 1484 CE LYS A 201 5523 5361 5225 -430 -502 352 C ATOM 1485 NZ LYS A 201 -69.377 122.817 0.987 1.00 42.66 N ANISOU 1485 NZ LYS A 201 5483 5499 5227 -424 -562 380 N ATOM 1486 N PRO A 202 -63.328 121.239 -3.262 1.00 38.63 N ANISOU 1486 N PRO A 202 5437 5256 3984 -856 -512 366 N ATOM 1487 CA PRO A 202 -62.504 121.358 -4.469 1.00 39.38 C ANISOU 1487 CA PRO A 202 5606 5393 3962 -933 -492 434 C ATOM 1488 C PRO A 202 -62.662 120.214 -5.483 1.00 40.01 C ANISOU 1488 C PRO A 202 5755 5603 3845 -1026 -501 416 C ATOM 1489 O PRO A 202 -62.665 120.478 -6.681 1.00 41.39 O ANISOU 1489 O PRO A 202 5981 5841 3902 -1097 -535 520 O ATOM 1490 CB PRO A 202 -61.074 121.441 -3.901 1.00 38.74 C ANISOU 1490 CB PRO A 202 5544 5246 3929 -931 -386 355 C ATOM 1491 CG PRO A 202 -61.257 122.092 -2.580 1.00 38.18 C ANISOU 1491 CG PRO A 202 5410 5074 4023 -855 -386 307 C ATOM 1492 CD PRO A 202 -62.514 121.452 -2.048 1.00 37.92 C ANISOU 1492 CD PRO A 202 5333 5079 3997 -814 -435 263 C ATOM 1493 N SER A 203 -62.832 118.972 -5.015 1.00 39.30 N ANISOU 1493 N SER A 203 5669 5549 3715 -1034 -468 289 N ATOM 1494 CA SER A 203 -63.096 117.822 -5.906 1.00 40.24 C ANISOU 1494 CA SER A 203 5860 5773 3655 -1133 -467 245 C ATOM 1495 C SER A 203 -64.582 117.451 -6.056 1.00 40.95 C ANISOU 1495 C SER A 203 5910 5939 3709 -1158 -589 275 C ATOM 1496 O SER A 203 -64.894 116.413 -6.629 1.00 41.04 O ANISOU 1496 O SER A 203 5978 6031 3582 -1250 -592 214 O ATOM 1497 CB SER A 203 -62.328 116.588 -5.405 1.00 39.33 C ANISOU 1497 CB SER A 203 5776 5638 3531 -1137 -340 93 C ATOM 1498 OG SER A 203 -62.915 116.045 -4.237 1.00 37.77 O ANISOU 1498 OG SER A 203 5506 5413 3431 -1074 -354 21 O ATOM 1499 N ASN A 204 -65.478 118.289 -5.535 1.00 41.59 N ANISOU 1499 N ASN A 204 5891 5985 3925 -1080 -679 365 N ATOM 1500 CA ASN A 204 -66.917 118.005 -5.463 1.00 42.43 C ANISOU 1500 CA ASN A 204 5920 6150 4050 -1082 -791 407 C ATOM 1501 C ASN A 204 -67.252 116.644 -4.832 1.00 41.04 C ANISOU 1501 C ASN A 204 5741 5996 3856 -1097 -753 260 C ATOM 1502 O ASN A 204 -68.120 115.925 -5.328 1.00 41.43 O ANISOU 1502 O ASN A 204 5788 6136 3817 -1178 -827 262 O ATOM 1503 CB ASN A 204 -67.568 118.101 -6.849 1.00 45.07 C ANISOU 1503 CB ASN A 204 6280 6612 4234 -1193 -916 540 C ATOM 1504 CG ASN A 204 -67.325 119.428 -7.530 1.00 47.01 C ANISOU 1504 CG ASN A 204 6522 6843 4498 -1181 -962 718 C ATOM 1505 OD1 ASN A 204 -67.405 120.485 -6.909 1.00 48.36 O ANISOU 1505 OD1 ASN A 204 6612 6905 4859 -1068 -958 792 O ATOM 1506 ND2 ASN A 204 -67.023 119.378 -8.816 1.00 48.63 N ANISOU 1506 ND2 ASN A 204 6820 7152 4504 -1304 -994 785 N ATOM 1507 N THR A 205 -66.577 116.317 -3.728 1.00 38.96 N ANISOU 1507 N THR A 205 5472 5650 3680 -1028 -644 145 N ATOM 1508 CA THR A 205 -66.690 115.001 -3.087 1.00 37.82 C ANISOU 1508 CA THR A 205 5329 5512 3530 -1037 -587 16 C ATOM 1509 C THR A 205 -67.230 115.109 -1.667 1.00 36.54 C ANISOU 1509 C THR A 205 5069 5293 3522 -933 -578 -12 C ATOM 1510 O THR A 205 -66.809 115.986 -0.895 1.00 34.74 O ANISOU 1510 O THR A 205 4811 4991 3399 -852 -545 -3 O ATOM 1511 CB THR A 205 -65.317 114.292 -3.021 1.00 37.35 C ANISOU 1511 CB THR A 205 5348 5417 3428 -1056 -451 -87 C ATOM 1512 OG1 THR A 205 -64.773 114.180 -4.340 1.00 38.68 O ANISOU 1512 OG1 THR A 205 5617 5632 3447 -1154 -428 -75 O ATOM 1513 CG2 THR A 205 -65.442 112.885 -2.433 1.00 36.72 C ANISOU 1513 CG2 THR A 205 5266 5331 3354 -1066 -386 -200 C ATOM 1514 N LYS A 206 -68.155 114.208 -1.336 1.00 36.00 N ANISOU 1514 N LYS A 206 4957 5260 3459 -949 -601 -51 N ATOM 1515 CA LYS A 206 -68.593 113.981 0.049 1.00 35.71 C ANISOU 1515 CA LYS A 206 4844 5182 3542 -866 -563 -100 C ATOM 1516 C LYS A 206 -68.511 112.489 0.350 1.00 34.68 C ANISOU 1516 C LYS A 206 4738 5067 3371 -910 -502 -200 C ATOM 1517 O LYS A 206 -68.960 111.675 -0.459 1.00 34.57 O ANISOU 1517 O LYS A 206 4754 5107 3272 -1003 -534 -216 O ATOM 1518 CB LYS A 206 -70.032 114.458 0.260 1.00 36.97 C ANISOU 1518 CB LYS A 206 4895 5358 3795 -827 -646 -20 C ATOM 1519 CG LYS A 206 -70.215 115.967 0.148 1.00 38.72 C ANISOU 1519 CG LYS A 206 5072 5533 4109 -760 -686 88 C ATOM 1520 CD LYS A 206 -71.683 116.340 -0.019 1.00 40.08 C ANISOU 1520 CD LYS A 206 5124 5733 4372 -736 -779 203 C ATOM 1521 CE LYS A 206 -71.861 117.809 -0.378 1.00 41.72 C ANISOU 1521 CE LYS A 206 5284 5885 4681 -675 -820 341 C ATOM 1522 NZ LYS A 206 -71.627 118.702 0.793 1.00 41.42 N ANISOU 1522 NZ LYS A 206 5223 5718 4796 -560 -716 295 N ATOM 1523 N VAL A 207 -67.956 112.141 1.512 1.00 33.46 N ANISOU 1523 N VAL A 207 4569 4865 3278 -850 -416 -261 N ATOM 1524 CA VAL A 207 -67.878 110.749 1.965 1.00 32.83 C ANISOU 1524 CA VAL A 207 4496 4784 3194 -873 -347 -334 C ATOM 1525 C VAL A 207 -68.450 110.650 3.379 1.00 32.19 C ANISOU 1525 C VAL A 207 4334 4690 3206 -801 -328 -342 C ATOM 1526 O VAL A 207 -68.073 111.429 4.253 1.00 31.16 O ANISOU 1526 O VAL A 207 4183 4532 3125 -734 -307 -336 O ATOM 1527 CB VAL A 207 -66.425 110.229 2.000 1.00 32.55 C ANISOU 1527 CB VAL A 207 4521 4710 3138 -878 -245 -378 C ATOM 1528 CG1 VAL A 207 -66.366 108.764 2.441 1.00 32.34 C ANISOU 1528 CG1 VAL A 207 4491 4662 3134 -894 -164 -434 C ATOM 1529 CG2 VAL A 207 -65.765 110.395 0.643 1.00 33.60 C ANISOU 1529 CG2 VAL A 207 4740 4851 3176 -946 -236 -375 C ATOM 1530 N ASP A 208 -69.352 109.691 3.589 1.00 32.58 N ANISOU 1530 N ASP A 208 4344 4760 3273 -827 -329 -360 N ATOM 1531 CA ASP A 208 -69.781 109.294 4.933 1.00 32.50 C ANISOU 1531 CA ASP A 208 4268 4742 3336 -773 -284 -373 C ATOM 1532 C ASP A 208 -69.182 107.929 5.258 1.00 32.12 C ANISOU 1532 C ASP A 208 4247 4673 3283 -799 -200 -416 C ATOM 1533 O ASP A 208 -69.369 106.970 4.496 1.00 31.60 O ANISOU 1533 O ASP A 208 4213 4603 3190 -874 -190 -446 O ATOM 1534 CB ASP A 208 -71.304 109.207 5.034 1.00 34.05 C ANISOU 1534 CB ASP A 208 4380 4972 3586 -777 -335 -343 C ATOM 1535 CG ASP A 208 -71.997 110.525 4.718 1.00 35.49 C ANISOU 1535 CG ASP A 208 4511 5163 3809 -738 -410 -276 C ATOM 1536 OD1 ASP A 208 -71.469 111.592 5.096 1.00 35.66 O ANISOU 1536 OD1 ASP A 208 4546 5148 3855 -675 -390 -268 O ATOM 1537 OD2 ASP A 208 -73.086 110.490 4.100 1.00 37.39 O ANISOU 1537 OD2 ASP A 208 4691 5444 4071 -776 -489 -223 O ATOM 1538 N LYS A 209 -68.504 107.843 6.402 1.00 31.41 N ANISOU 1538 N LYS A 209 4142 4569 3223 -744 -140 -413 N ATOM 1539 CA LYS A 209 -67.885 106.601 6.862 1.00 31.85 C ANISOU 1539 CA LYS A 209 4201 4600 3302 -751 -57 -420 C ATOM 1540 C LYS A 209 -68.313 106.291 8.293 1.00 31.73 C ANISOU 1540 C LYS A 209 4122 4606 3329 -707 -29 -394 C ATOM 1541 O LYS A 209 -67.946 107.016 9.220 1.00 30.50 O ANISOU 1541 O LYS A 209 3952 4475 3161 -663 -31 -378 O ATOM 1542 CB LYS A 209 -66.371 106.738 6.793 1.00 31.75 C ANISOU 1542 CB LYS A 209 4225 4561 3278 -736 -15 -409 C ATOM 1543 CG LYS A 209 -65.586 105.475 7.103 1.00 31.96 C ANISOU 1543 CG LYS A 209 4242 4546 3354 -736 79 -392 C ATOM 1544 CD LYS A 209 -65.840 104.423 6.047 1.00 32.84 C ANISOU 1544 CD LYS A 209 4401 4604 3474 -799 132 -442 C ATOM 1545 CE LYS A 209 -64.734 103.397 6.017 1.00 33.18 C ANISOU 1545 CE LYS A 209 4450 4572 3584 -791 252 -427 C ATOM 1546 NZ LYS A 209 -65.024 102.314 5.047 1.00 33.99 N ANISOU 1546 NZ LYS A 209 4612 4602 3699 -862 330 -500 N ATOM 1547 N THR A 210 -69.098 105.229 8.472 1.00 32.63 N ANISOU 1547 N THR A 210 4203 4713 3483 -731 0 -394 N ATOM 1548 CA THR A 210 -69.480 104.780 9.818 1.00 33.37 C ANISOU 1548 CA THR A 210 4238 4830 3611 -698 42 -357 C ATOM 1549 C THR A 210 -68.358 103.899 10.374 1.00 34.85 C ANISOU 1549 C THR A 210 4428 4993 3819 -686 111 -313 C ATOM 1550 O THR A 210 -67.968 102.912 9.761 1.00 34.31 O ANISOU 1550 O THR A 210 4379 4862 3794 -716 162 -316 O ATOM 1551 CB THR A 210 -70.844 104.061 9.830 1.00 33.60 C ANISOU 1551 CB THR A 210 4216 4861 3691 -729 46 -359 C ATOM 1552 OG1 THR A 210 -71.840 104.924 9.263 1.00 33.71 O ANISOU 1552 OG1 THR A 210 4204 4902 3701 -736 -28 -375 O ATOM 1553 CG2 THR A 210 -71.270 103.697 11.251 1.00 33.65 C ANISOU 1553 CG2 THR A 210 4163 4899 3723 -694 98 -313 C ATOM 1554 N VAL A 211 -67.849 104.277 11.544 1.00 28.54 N ATOM 1555 CA VAL A 211 -66.672 103.647 12.154 1.00 30.11 C ATOM 1556 C VAL A 211 -67.122 102.727 13.284 1.00 31.91 C ATOM 1557 O VAL A 211 -67.860 103.163 14.159 1.00 31.74 O ATOM 1558 CB VAL A 211 -65.729 104.726 12.721 1.00 30.26 C ATOM 1559 CG1 VAL A 211 -64.478 104.101 13.331 1.00 30.73 C ATOM 1560 CG2 VAL A 211 -65.366 105.726 11.626 1.00 30.52 C ATOM 1561 N GLU A 212 -66.665 101.472 13.271 1.00 35.46 N ATOM 1562 CA GLU A 212 -67.095 100.468 14.260 1.00 39.08 C ATOM 1563 C GLU A 212 -65.987 99.480 14.633 1.00 39.67 C ATOM 1564 O GLU A 212 -64.886 99.523 14.086 1.00 38.54 O ATOM 1565 CB GLU A 212 -68.323 99.707 13.742 1.00 41.73 C ATOM 1566 CG GLU A 212 -68.144 99.055 12.377 1.00 44.13 C ATOM 1567 CD GLU A 212 -69.384 98.320 11.892 1.00 46.05 C ATOM 1568 OE1 GLU A 212 -70.507 98.646 12.338 1.00 49.36 O ATOM 1569 OE2 GLU A 212 -69.238 97.417 11.039 1.00 48.01 O TER 1570 GLU A 212 ATOM 1571 N GLN B 1 -25.333 122.764 8.928 1.00 45.35 N ATOM 1572 CA GLN B 1 -25.018 122.582 10.379 1.00 44.07 C ATOM 1573 C GLN B 1 -26.247 122.094 11.147 1.00 42.11 C ATOM 1574 O GLN B 1 -27.344 122.014 10.590 1.00 42.21 O ATOM 1575 CB GLN B 1 -24.505 123.890 10.999 1.00 44.36 C ATOM 1576 CG GLN B 1 -23.352 124.560 10.252 1.00 44.50 C ATOM 1577 CD GLN B 1 -23.756 125.804 9.467 1.00 44.40 C ATOM 1578 OE1 GLN B 1 -24.854 125.887 8.920 1.00 43.03 O ATOM 1579 NE2 GLN B 1 -22.854 126.781 9.408 1.00 43.63 N ATOM 1580 N SER B 2 -26.045 121.772 12.423 1.00 53.32 N ANISOU 1580 N SER B 2 7191 6987 6082 306 -182 -844 N ATOM 1581 CA SER B 2 -27.117 121.302 13.309 1.00 50.34 C ANISOU 1581 CA SER B 2 6883 6501 5744 262 -209 -799 C ATOM 1582 C SER B 2 -27.867 122.483 13.955 1.00 45.69 C ANISOU 1582 C SER B 2 6285 5965 5108 200 -232 -701 C ATOM 1583 O SER B 2 -27.232 123.435 14.416 1.00 45.25 O ANISOU 1583 O SER B 2 6191 5967 5035 219 -240 -640 O ATOM 1584 CB SER B 2 -26.524 120.387 14.395 1.00 51.61 C ANISOU 1584 CB SER B 2 7080 6534 5996 333 -227 -763 C ATOM 1585 OG SER B 2 -27.432 120.177 15.469 1.00 52.26 O ANISOU 1585 OG SER B 2 7217 6535 6104 288 -256 -687 O ATOM 1586 N ALA B 3 -29.204 122.412 13.987 1.00 41.33 N ANISOU 1586 N ALA B 3 5769 5396 4539 127 -241 -692 N ATOM 1587 CA ALA B 3 -30.045 123.395 14.697 1.00 37.96 C ANISOU 1587 CA ALA B 3 5339 5005 4078 78 -259 -604 C ATOM 1588 C ALA B 3 -29.672 123.469 16.178 1.00 35.41 C ANISOU 1588 C ALA B 3 5034 4625 3796 109 -284 -522 C ATOM 1589 O ALA B 3 -29.294 122.463 16.775 1.00 35.70 O ANISOU 1589 O ALA B 3 5104 4566 3893 145 -293 -518 O ATOM 1590 CB ALA B 3 -31.519 123.046 14.553 1.00 37.79 C ANISOU 1590 CB ALA B 3 5346 4971 4040 2 -264 -612 C ATOM 1591 N LEU B 4 -29.778 124.659 16.759 1.00 32.78 N ANISOU 1591 N LEU B 4 4678 4349 3427 95 -293 -456 N ATOM 1592 CA LEU B 4 -29.413 124.872 18.169 1.00 30.89 C ANISOU 1592 CA LEU B 4 4449 4081 3208 117 -317 -385 C ATOM 1593 C LEU B 4 -30.502 124.252 19.044 1.00 30.31 C ANISOU 1593 C LEU B 4 4425 3943 3150 79 -330 -345 C ATOM 1594 O LEU B 4 -31.698 124.420 18.761 1.00 29.63 O ANISOU 1594 O LEU B 4 4346 3878 3036 22 -323 -347 O ATOM 1595 CB LEU B 4 -29.224 126.359 18.477 1.00 30.17 C ANISOU 1595 CB LEU B 4 4324 4065 3073 106 -318 -344 C ATOM 1596 CG LEU B 4 -28.385 127.196 17.493 1.00 30.05 C ANISOU 1596 CG LEU B 4 4259 4127 3033 117 -300 -372 C ATOM 1597 CD1 LEU B 4 -28.290 128.635 17.952 1.00 29.54 C ANISOU 1597 CD1 LEU B 4 4176 4109 2940 95 -302 -326 C ATOM 1598 CD2 LEU B 4 -26.993 126.599 17.295 1.00 30.62 C ANISOU 1598 CD2 LEU B 4 4301 4197 3135 175 -298 -404 C ATOM 1599 N THR B 5 -30.097 123.513 20.082 1.00 29.26 N ANISOU 1599 N THR B 5 4318 3740 3058 110 -350 -302 N ATOM 1600 CA THR B 5 -31.040 122.739 20.891 1.00 29.14 C ANISOU 1600 CA THR B 5 4351 3658 3063 72 -360 -256 C ATOM 1601 C THR B 5 -31.750 123.613 21.928 1.00 28.13 C ANISOU 1601 C THR B 5 4217 3586 2885 35 -369 -190 C ATOM 1602 O THR B 5 -31.099 124.286 22.727 1.00 27.79 O ANISOU 1602 O THR B 5 4156 3583 2822 64 -383 -153 O ATOM 1603 CB THR B 5 -30.331 121.560 21.601 1.00 30.13 C ANISOU 1603 CB THR B 5 4511 3684 3253 123 -378 -221 C ATOM 1604 OG1 THR B 5 -29.666 120.753 20.625 1.00 30.83 O ANISOU 1604 OG1 THR B 5 4606 3716 3393 169 -364 -293 O ATOM 1605 CG2 THR B 5 -31.333 120.679 22.362 1.00 30.66 C ANISOU 1605 CG2 THR B 5 4632 3673 3343 72 -385 -165 C ATOM 1606 N GLN B 6 -33.081 123.619 21.890 1.00 27.40 N ANISOU 1606 N GLN B 6 4136 3506 2770 -30 -359 -184 N ATOM 1607 CA GLN B 6 -33.895 124.316 22.882 1.00 26.87 C ANISOU 1607 CA GLN B 6 4063 3491 2657 -61 -361 -128 C ATOM 1608 C GLN B 6 -34.883 123.332 23.497 1.00 27.63 C ANISOU 1608 C GLN B 6 4192 3540 2764 -115 -362 -84 C ATOM 1609 O GLN B 6 -35.234 122.346 22.858 1.00 27.70 O ANISOU 1609 O GLN B 6 4226 3486 2812 -147 -358 -114 O ATOM 1610 CB GLN B 6 -34.677 125.463 22.249 1.00 25.96 C ANISOU 1610 CB GLN B 6 3912 3459 2492 -86 -342 -152 C ATOM 1611 CG GLN B 6 -33.841 126.528 21.563 1.00 25.32 C ANISOU 1611 CG GLN B 6 3799 3423 2397 -47 -336 -185 C ATOM 1612 CD GLN B 6 -34.686 127.661 20.992 1.00 24.66 C ANISOU 1612 CD GLN B 6 3686 3412 2272 -65 -319 -191 C ATOM 1613 OE1 GLN B 6 -34.550 128.017 19.817 1.00 24.46 O ANISOU 1613 OE1 GLN B 6 3638 3418 2238 -61 -308 -224 O ATOM 1614 NE2 GLN B 6 -35.567 128.222 21.806 1.00 24.37 N ANISOU 1614 NE2 GLN B 6 3647 3406 2207 -80 -313 -155 N ATOM 1615 N PRO B 7 -35.329 123.592 24.742 1.00 27.81 N ANISOU 1615 N PRO B 7 4218 3597 2753 -132 -367 -18 N ATOM 1616 CA PRO B 7 -36.418 122.775 25.268 1.00 28.84 C ANISOU 1616 CA PRO B 7 4370 3704 2884 -198 -363 29 C ATOM 1617 C PRO B 7 -37.716 123.041 24.487 1.00 29.33 C ANISOU 1617 C PRO B 7 4404 3819 2919 -260 -341 -8 C ATOM 1618 O PRO B 7 -37.912 124.156 23.975 1.00 28.05 O ANISOU 1618 O PRO B 7 4203 3737 2720 -242 -331 -42 O ATOM 1619 CB PRO B 7 -36.525 123.222 26.727 1.00 28.85 C ANISOU 1619 CB PRO B 7 4365 3762 2834 -194 -368 102 C ATOM 1620 CG PRO B 7 -35.969 124.607 26.760 1.00 28.15 C ANISOU 1620 CG PRO B 7 4242 3748 2705 -146 -367 69 C ATOM 1621 CD PRO B 7 -34.954 124.687 25.657 1.00 27.66 C ANISOU 1621 CD PRO B 7 4176 3650 2685 -101 -373 9 C ATOM 1622 N ARG B 8 -38.563 122.024 24.351 1.00 31.02 N ANISOU 1622 N ARG B 8 4638 3991 3157 -332 -337 1 N ATOM 1623 CA ARG B 8 -39.818 122.185 23.592 1.00 32.26 C ANISOU 1623 CA ARG B 8 4758 4214 3285 -398 -322 -34 C ATOM 1624 C ARG B 8 -40.800 123.105 24.338 1.00 31.30 C ANISOU 1624 C ARG B 8 4589 4209 3095 -413 -307 10 C ATOM 1625 O ARG B 8 -41.494 123.904 23.699 1.00 30.09 O ANISOU 1625 O ARG B 8 4385 4144 2902 -416 -295 -20 O ATOM 1626 CB ARG B 8 -40.458 120.843 23.152 1.00 35.17 C ANISOU 1626 CB ARG B 8 5157 4508 3697 -487 -322 -51 C ATOM 1627 CG ARG B 8 -40.031 120.417 21.735 1.00 37.35 C ANISOU 1627 CG ARG B 8 5445 4736 4009 -484 -324 -148 C ATOM 1628 CD ARG B 8 -40.850 119.261 21.183 1.00 40.18 C ANISOU 1628 CD ARG B 8 5826 5040 4401 -587 -321 -187 C ATOM 1629 NE ARG B 8 -40.423 118.862 19.832 1.00 42.71 N ANISOU 1629 NE ARG B 8 6158 5323 4746 -584 -321 -296 N ATOM 1630 CZ ARG B 8 -39.295 118.196 19.542 1.00 44.47 C ANISOU 1630 CZ ARG B 8 6433 5428 5034 -529 -323 -339 C ATOM 1631 NH1 ARG B 8 -38.427 117.824 20.493 1.00 45.54 N ANISOU 1631 NH1 ARG B 8 6615 5467 5223 -466 -330 -275 N ATOM 1632 NH2 ARG B 8 -39.022 117.896 18.275 1.00 45.58 N ANISOU 1632 NH2 ARG B 8 6576 5558 5183 -530 -317 -448 N ATOM 1633 N SER B 9 -40.790 123.036 25.676 1.00 30.78 N ANISOU 1633 N SER B 9 4537 4148 3011 -412 -307 82 N ATOM 1634 CA SER B 9 -41.786 123.685 26.533 1.00 30.60 C ANISOU 1634 CA SER B 9 4472 4233 2922 -432 -287 123 C ATOM 1635 C SER B 9 -41.144 124.292 27.781 1.00 30.15 C ANISOU 1635 C SER B 9 4424 4203 2829 -378 -290 163 C ATOM 1636 O SER B 9 -40.364 123.641 28.462 1.00 30.10 O ANISOU 1636 O SER B 9 4459 4136 2843 -367 -308 207 O ATOM 1637 CB SER B 9 -42.823 122.656 26.996 1.00 31.61 C ANISOU 1637 CB SER B 9 4601 4361 3048 -530 -279 177 C ATOM 1638 OG SER B 9 -43.820 123.250 27.818 1.00 32.07 O ANISOU 1638 OG SER B 9 4608 4540 3036 -549 -254 215 O ATOM 1639 N VAL B 11 -41.500 125.538 28.065 1.00 29.63 N ANISOU 1639 N VAL B 11 4317 4232 2709 -342 -271 145 N ATOM 1640 CA VAL B 11 -41.186 126.199 29.329 1.00 29.92 C ANISOU 1640 CA VAL B 11 4354 4321 2694 -306 -266 170 C ATOM 1641 C VAL B 11 -42.490 126.867 29.794 1.00 29.83 C ANISOU 1641 C VAL B 11 4290 4425 2619 -321 -230 174 C ATOM 1642 O VAL B 11 -43.313 127.264 28.956 1.00 29.23 O ANISOU 1642 O VAL B 11 4173 4387 2545 -325 -214 143 O ATOM 1643 CB VAL B 11 -39.953 127.137 29.145 1.00 29.53 C ANISOU 1643 CB VAL B 11 4316 4248 2656 -232 -280 121 C ATOM 1644 CG1 VAL B 11 -39.884 128.187 30.222 1.00 29.63 C ANISOU 1644 CG1 VAL B 11 4317 4334 2607 -200 -268 114 C ATOM 1645 CG2 VAL B 11 -38.664 126.303 29.118 1.00 29.66 C ANISOU 1645 CG2 VAL B 11 4374 4174 2720 -217 -315 138 C ATOM 1646 N SER B 12 -42.738 126.902 31.105 1.00 29.80 N ANISOU 1646 N SER B 12 4281 4486 2555 -332 -218 216 N ATOM 1647 CA SER B 12 -43.982 127.477 31.621 1.00 30.28 C ANISOU 1647 CA SER B 12 4286 4667 2551 -341 -178 218 C ATOM 1648 C SER B 12 -43.856 128.096 33.007 1.00 30.86 C ANISOU 1648 C SER B 12 4355 4820 2548 -314 -161 223 C ATOM 1649 O SER B 12 -42.967 127.739 33.792 1.00 31.19 O ANISOU 1649 O SER B 12 4435 4840 2574 -314 -185 256 O ATOM 1650 CB SER B 12 -45.102 126.436 31.634 1.00 30.96 C ANISOU 1650 CB SER B 12 4346 4788 2631 -432 -165 276 C ATOM 1651 OG SER B 12 -44.796 125.342 32.499 1.00 31.49 O ANISOU 1651 OG SER B 12 4451 4822 2691 -486 -180 355 O ATOM 1652 N GLY B 13 -44.751 129.043 33.271 1.00 30.92 N ANISOU 1652 N GLY B 13 4313 4928 2506 -285 -120 188 N ATOM 1653 CA GLY B 13 -44.859 129.682 34.568 1.00 31.70 C ANISOU 1653 CA GLY B 13 4400 5123 2522 -261 -94 176 C ATOM 1654 C GLY B 13 -46.174 130.424 34.689 1.00 32.22 C ANISOU 1654 C GLY B 13 4398 5302 2543 -237 -40 146 C ATOM 1655 O GLY B 13 -46.799 130.765 33.691 1.00 31.64 O ANISOU 1655 O GLY B 13 4290 5223 2509 -215 -29 123 O ATOM 1656 N SER B 14 -46.605 130.655 35.923 1.00 33.45 N ANISOU 1656 N SER B 14 4528 5571 2609 -238 -7 149 N ATOM 1657 CA SER B 14 -47.761 131.507 36.203 1.00 34.11 C ANISOU 1657 CA SER B 14 4544 5773 2642 -195 51 107 C ATOM 1658 C SER B 14 -47.400 132.971 35.959 1.00 33.76 C ANISOU 1658 C SER B 14 4516 5689 2624 -92 66 4 C ATOM 1659 O SER B 14 -46.216 133.318 35.957 1.00 32.71 O ANISOU 1659 O SER B 14 4445 5465 2518 -72 35 -32 O ATOM 1660 CB SER B 14 -48.198 131.345 37.660 1.00 35.44 C ANISOU 1660 CB SER B 14 4685 6082 2699 -223 86 131 C ATOM 1661 OG SER B 14 -48.600 130.014 37.910 1.00 36.44 O ANISOU 1661 OG SER B 14 4797 6244 2804 -324 76 238 O ATOM 1662 N PRO B 15 -48.415 133.841 35.770 1.00 34.28 N ANISOU 1662 N PRO B 15 4523 5820 2681 -28 114 -40 N ATOM 1663 CA PRO B 15 -48.148 135.278 35.684 1.00 34.50 C ANISOU 1663 CA PRO B 15 4572 5802 2735 73 137 -135 C ATOM 1664 C PRO B 15 -47.357 135.789 36.884 1.00 34.97 C ANISOU 1664 C PRO B 15 4680 5871 2737 84 143 -199 C ATOM 1665 O PRO B 15 -47.648 135.406 38.026 1.00 35.35 O ANISOU 1665 O PRO B 15 4706 6035 2691 49 164 -185 O ATOM 1666 CB PRO B 15 -49.550 135.895 35.677 1.00 35.14 C ANISOU 1666 CB PRO B 15 4570 5991 2792 136 197 -156 C ATOM 1667 CG PRO B 15 -50.418 134.833 35.094 1.00 35.18 C ANISOU 1667 CG PRO B 15 4510 6058 2797 68 187 -68 C ATOM 1668 CD PRO B 15 -49.851 133.544 35.609 1.00 35.02 C ANISOU 1668 CD PRO B 15 4527 6031 2748 -43 151 -1 C ATOM 1669 N GLY B 16 -46.351 136.615 36.619 1.00 34.85 N ANISOU 1669 N GLY B 16 4725 5742 2773 124 124 -264 N ATOM 1670 CA GLY B 16 -45.462 137.122 37.668 1.00 35.62 C ANISOU 1670 CA GLY B 16 4871 5843 2820 123 121 -335 C ATOM 1671 C GLY B 16 -44.216 136.286 37.925 1.00 35.50 C ANISOU 1671 C GLY B 16 4901 5792 2795 51 58 -289 C ATOM 1672 O GLY B 16 -43.269 136.788 38.529 1.00 35.85 O ANISOU 1672 O GLY B 16 4987 5819 2816 50 42 -350 O ATOM 1673 N GLN B 17 -44.196 135.027 37.479 1.00 35.30 N ANISOU 1673 N GLN B 17 4867 5754 2790 -7 23 -186 N ATOM 1674 CA GLN B 17 -43.022 134.159 37.657 1.00 35.32 C ANISOU 1674 CA GLN B 17 4910 5715 2796 -60 -36 -133 C ATOM 1675 C GLN B 17 -41.965 134.392 36.577 1.00 34.38 C ANISOU 1675 C GLN B 17 4831 5457 2774 -44 -76 -152 C ATOM 1676 O GLN B 17 -42.187 135.129 35.616 1.00 32.96 O ANISOU 1676 O GLN B 17 4651 5212 2661 -1 -61 -192 O ATOM 1677 CB GLN B 17 -43.440 132.683 37.659 1.00 36.07 C ANISOU 1677 CB GLN B 17 4987 5838 2880 -127 -52 -16 C ATOM 1678 CG GLN B 17 -44.421 132.332 38.766 1.00 37.59 C ANISOU 1678 CG GLN B 17 5135 6179 2969 -159 -14 22 C ATOM 1679 CD GLN B 17 -44.674 130.839 38.892 1.00 38.32 C ANISOU 1679 CD GLN B 17 5221 6285 3053 -240 -34 148 C ATOM 1680 OE1 GLN B 17 -44.779 130.122 37.893 1.00 38.71 O ANISOU 1680 OE1 GLN B 17 5277 6248 3184 -267 -54 195 O ATOM 1681 NE2 GLN B 17 -44.807 130.370 40.121 1.00 39.41 N ANISOU 1681 NE2 GLN B 17 5348 6536 3092 -281 -26 204 N ATOM 1682 N SER B 18 -40.808 133.764 36.775 1.00 34.55 N ANISOU 1682 N SER B 18 4884 5446 2799 -77 -127 -117 N ATOM 1683 CA SER B 18 -39.713 133.798 35.823 1.00 34.20 C ANISOU 1683 CA SER B 18 4870 5289 2838 -69 -167 -125 C ATOM 1684 C SER B 18 -39.565 132.466 35.117 1.00 33.42 C ANISOU 1684 C SER B 18 4773 5136 2788 -101 -200 -38 C ATOM 1685 O SER B 18 -39.850 131.411 35.685 1.00 34.79 O ANISOU 1685 O SER B 18 4941 5351 2927 -139 -208 38 O ATOM 1686 CB SER B 18 -38.402 134.137 36.517 1.00 34.62 C ANISOU 1686 CB SER B 18 4947 5345 2861 -76 -202 -162 C ATOM 1687 OG SER B 18 -38.507 135.386 37.156 1.00 35.99 O ANISOU 1687 OG SER B 18 5125 5557 2992 -54 -171 -259 O ATOM 1688 N VAL B 19 -39.121 132.532 33.870 1.00 31.57 N ANISOU 1688 N VAL B 19 4550 4809 2638 -85 -215 -50 N ATOM 1689 CA VAL B 19 -38.714 131.355 33.123 1.00 30.90 C ANISOU 1689 CA VAL B 19 4475 4657 2607 -107 -247 8 C ATOM 1690 C VAL B 19 -37.415 131.635 32.408 1.00 29.85 C ANISOU 1690 C VAL B 19 4361 4450 2531 -85 -277 -24 C ATOM 1691 O VAL B 19 -37.139 132.779 32.053 1.00 29.44 O ANISOU 1691 O VAL B 19 4310 4380 2495 -59 -265 -86 O ATOM 1692 CB VAL B 19 -39.768 130.897 32.087 1.00 30.72 C ANISOU 1692 CB VAL B 19 4433 4613 2625 -122 -228 29 C ATOM 1693 CG1 VAL B 19 -40.963 130.275 32.796 1.00 31.50 C ANISOU 1693 CG1 VAL B 19 4507 4789 2672 -163 -205 80 C ATOM 1694 CG2 VAL B 19 -40.209 132.023 31.161 1.00 30.22 C ANISOU 1694 CG2 VAL B 19 4352 4539 2591 -82 -202 -28 C ATOM 1695 N THR B 20 -36.650 130.571 32.177 1.00 29.35 N ANISOU 1695 N THR B 20 4310 4339 2501 -95 -313 23 N ATOM 1696 CA THR B 20 -35.404 130.630 31.435 1.00 28.90 C ANISOU 1696 CA THR B 20 4260 4221 2497 -73 -340 0 C ATOM 1697 C THR B 20 -35.439 129.592 30.315 1.00 28.14 C ANISOU 1697 C THR B 20 4170 4054 2466 -77 -348 26 C ATOM 1698 O THR B 20 -35.791 128.440 30.552 1.00 28.28 O ANISOU 1698 O THR B 20 4199 4055 2490 -100 -356 82 O ATOM 1699 CB THR B 20 -34.214 130.322 32.358 1.00 29.59 C ANISOU 1699 CB THR B 20 4351 4332 2558 -68 -380 24 C ATOM 1700 OG1 THR B 20 -34.251 131.206 33.486 1.00 30.58 O ANISOU 1700 OG1 THR B 20 4472 4538 2611 -75 -374 -8 O ATOM 1701 CG2 THR B 20 -32.900 130.495 31.627 1.00 29.54 C ANISOU 1701 CG2 THR B 20 4339 4283 2603 -44 -405 -5 C ATOM 1702 N ILE B 21 -35.057 130.015 29.113 1.00 26.93 N ANISOU 1702 N ILE B 21 4011 3860 2360 -59 -344 -17 N ATOM 1703 CA ILE B 21 -35.009 129.163 27.931 1.00 26.68 C ANISOU 1703 CA ILE B 21 3983 3770 2384 -61 -348 -15 C ATOM 1704 C ILE B 21 -33.543 128.992 27.535 1.00 26.58 C ANISOU 1704 C ILE B 21 3970 3722 2408 -31 -373 -29 C ATOM 1705 O ILE B 21 -32.866 129.970 27.250 1.00 25.72 O ANISOU 1705 O ILE B 21 3846 3627 2299 -15 -372 -67 O ATOM 1706 CB ILE B 21 -35.770 129.793 26.744 1.00 26.23 C ANISOU 1706 CB ILE B 21 3910 3719 2340 -64 -321 -50 C ATOM 1707 CG1 ILE B 21 -37.224 130.085 27.127 1.00 26.48 C ANISOU 1707 CG1 ILE B 21 3927 3802 2333 -84 -295 -37 C ATOM 1708 CG2 ILE B 21 -35.732 128.869 25.526 1.00 26.44 C ANISOU 1708 CG2 ILE B 21 3938 3699 2410 -73 -326 -60 C ATOM 1709 CD1 ILE B 21 -37.907 131.073 26.212 1.00 26.45 C ANISOU 1709 CD1 ILE B 21 3898 3822 2330 -68 -270 -65 C ATOM 1710 N SER B 22 -33.080 127.745 27.488 1.00 27.16 N ANISOU 1710 N SER B 22 4057 3747 2516 -22 -393 1 N ATOM 1711 CA SER B 22 -31.717 127.426 27.072 1.00 27.38 C ANISOU 1711 CA SER B 22 4076 3746 2583 18 -415 -12 C ATOM 1712 C SER B 22 -31.617 127.203 25.564 1.00 27.79 C ANISOU 1712 C SER B 22 4122 3759 2679 26 -399 -60 C ATOM 1713 O SER B 22 -32.593 126.826 24.904 1.00 27.69 O ANISOU 1713 O SER B 22 4120 3725 2675 -2 -381 -71 O ATOM 1714 CB SER B 22 -31.227 126.179 27.811 1.00 28.12 C ANISOU 1714 CB SER B 22 4187 3801 2696 39 -443 48 C ATOM 1715 OG SER B 22 -32.057 125.073 27.519 1.00 27.94 O ANISOU 1715 OG SER B 22 4196 3711 2707 16 -433 71 O ATOM 1716 N CYS B 23 -30.420 127.434 25.032 1.00 28.16 N ANISOU 1716 N CYS B 23 4143 3810 2745 61 -406 -89 N ATOM 1717 CA CYS B 23 -30.130 127.329 23.611 1.00 28.46 C ANISOU 1717 CA CYS B 23 4168 3834 2813 72 -390 -139 C ATOM 1718 C CYS B 23 -28.707 126.819 23.456 1.00 28.68 C ANISOU 1718 C CYS B 23 4173 3852 2874 125 -405 -148 C ATOM 1719 O CYS B 23 -27.759 127.601 23.502 1.00 28.53 O ANISOU 1719 O CYS B 23 4116 3882 2841 137 -411 -158 O ATOM 1720 CB CYS B 23 -30.293 128.704 22.945 1.00 28.31 C ANISOU 1720 CB CYS B 23 4124 3866 2765 53 -369 -168 C ATOM 1721 SG CYS B 23 -29.671 128.825 21.256 1.00 29.18 S ANISOU 1721 SG CYS B 23 4203 3993 2891 66 -348 -219 S ATOM 1722 N THR B 24 -28.573 125.509 23.268 1.00 29.34 N ANISOU 1722 N THR B 24 4277 3868 3002 154 -410 -147 N ATOM 1723 CA THR B 24 -27.278 124.846 23.272 1.00 30.27 C ANISOU 1723 CA THR B 24 4374 3968 3159 221 -425 -147 C ATOM 1724 C THR B 24 -26.750 124.634 21.854 1.00 30.30 C ANISOU 1724 C THR B 24 4354 3970 3189 249 -400 -219 C ATOM 1725 O THR B 24 -27.371 123.951 21.035 1.00 29.85 O ANISOU 1725 O THR B 24 4326 3862 3154 237 -381 -261 O ATOM 1726 CB THR B 24 -27.363 123.507 24.017 1.00 31.48 C ANISOU 1726 CB THR B 24 4568 4037 3356 251 -445 -94 C ATOM 1727 OG1 THR B 24 -27.830 123.759 25.344 1.00 32.05 O ANISOU 1727 OG1 THR B 24 4655 4134 3388 222 -466 -23 O ATOM 1728 CG2 THR B 24 -25.995 122.825 24.096 1.00 32.40 C ANISOU 1728 CG2 THR B 24 4657 4136 3516 339 -463 -85 C ATOM 1729 N GLY B 25 -25.594 125.241 21.585 1.00 30.21 N ANISOU 1729 N GLY B 25 4286 4026 3167 279 -401 -237 N ATOM 1730 CA GLY B 25 -24.914 125.115 20.307 1.00 30.23 C ANISOU 1730 CA GLY B 25 4252 4053 3183 309 -374 -302 C ATOM 1731 C GLY B 25 -23.580 124.417 20.476 1.00 30.67 C ANISOU 1731 C GLY B 25 4268 4108 3277 394 -386 -303 C ATOM 1732 O GLY B 25 -23.440 123.518 21.308 1.00 31.10 O ANISOU 1732 O GLY B 25 4346 4100 3370 440 -411 -259 O ATOM 1733 N THR B 26 -22.608 124.846 19.677 1.00 30.04 N ANISOU 1733 N THR B 26 4124 4106 3186 416 -368 -344 N ATOM 1734 CA THR B 26 -21.249 124.308 19.678 1.00 30.55 C ANISOU 1734 CA THR B 26 4128 4198 3281 503 -373 -352 C ATOM 1735 C THR B 26 -20.278 125.469 19.796 1.00 30.09 C ANISOU 1735 C THR B 26 3989 4263 3180 481 -380 -339 C ATOM 1736 O THR B 26 -20.691 126.627 19.719 1.00 29.37 O ANISOU 1736 O THR B 26 3900 4215 3044 400 -374 -332 O ATOM 1737 CB THR B 26 -20.912 123.574 18.369 1.00 31.01 C ANISOU 1737 CB THR B 26 4171 4245 3366 555 -333 -437 C ATOM 1738 OG1 THR B 26 -21.032 124.482 17.273 1.00 30.54 O ANISOU 1738 OG1 THR B 26 4082 4270 3253 497 -299 -482 O ATOM 1739 CG2 THR B 26 -21.840 122.397 18.159 1.00 31.43 C ANISOU 1739 CG2 THR B 26 4307 4169 3466 567 -324 -467 C ATOM 1740 N SER B 27 -18.993 125.154 19.918 1.00 30.52 N ANISOU 1740 N SER B 27 3972 4374 3252 552 -390 -337 N ATOM 1741 CA SER B 27 -17.935 126.161 19.906 1.00 30.94 C ANISOU 1741 CA SER B 27 3933 4555 3267 527 -393 -332 C ATOM 1742 C SER B 27 -17.761 126.912 18.572 1.00 31.17 C ANISOU 1742 C SER B 27 3924 4657 3264 480 -346 -385 C ATOM 1743 O SER B 27 -17.109 127.948 18.551 1.00 31.29 O ANISOU 1743 O SER B 27 3877 4767 3244 427 -346 -374 O ATOM 1744 CB SER B 27 -16.594 125.544 20.349 1.00 31.83 C ANISOU 1744 CB SER B 27 3964 4725 3406 622 -416 -314 C ATOM 1745 OG SER B 27 -16.117 124.608 19.409 1.00 32.44 O ANISOU 1745 OG SER B 27 4015 4788 3522 714 -381 -369 O ATOM 1746 N SER B 28 -18.319 126.393 17.474 1.00 31.76 N ANISOU 1746 N SER B 28 4031 4691 3346 494 -307 -441 N ATOM 1747 CA SER B 28 -18.310 127.089 16.174 1.00 31.99 C ANISOU 1747 CA SER B 28 4029 4795 3330 445 -262 -482 C ATOM 1748 C SER B 28 -19.552 127.974 15.888 1.00 30.96 C ANISOU 1748 C SER B 28 3961 4640 3164 350 -254 -465 C ATOM 1749 O SER B 28 -19.666 128.554 14.800 1.00 31.28 O ANISOU 1749 O SER B 28 3981 4741 3163 308 -219 -485 O ATOM 1750 CB SER B 28 -18.063 126.064 15.054 1.00 33.08 C ANISOU 1750 CB SER B 28 4152 4936 3483 517 -222 -562 C ATOM 1751 OG SER B 28 -19.189 125.242 14.835 1.00 33.85 O ANISOU 1751 OG SER B 28 4336 4923 3602 523 -217 -596 O ATOM 1752 N ASP B 29 -20.463 128.102 16.859 1.00 30.27 N ANISOU 1752 N ASP B 29 3940 4474 3086 320 -285 -423 N ATOM 1753 CA ASP B 29 -21.594 129.029 16.746 1.00 29.46 C ANISOU 1753 CA ASP B 29 3886 4354 2953 241 -280 -399 C ATOM 1754 C ASP B 29 -21.849 129.787 18.068 1.00 28.66 C ANISOU 1754 C ASP B 29 3811 4228 2851 201 -314 -344 C ATOM 1755 O ASP B 29 -21.221 130.824 18.283 1.00 28.76 O ANISOU 1755 O ASP B 29 3787 4295 2847 159 -317 -325 O ATOM 1756 CB ASP B 29 -22.850 128.336 16.151 1.00 29.45 C ANISOU 1756 CB ASP B 29 3946 4291 2953 240 -266 -428 C ATOM 1757 CG ASP B 29 -23.163 127.007 16.806 1.00 29.93 C ANISOU 1757 CG ASP B 29 4053 4257 3061 290 -286 -437 C ATOM 1758 OD1 ASP B 29 -23.564 127.021 17.984 1.00 29.73 O ANISOU 1758 OD1 ASP B 29 4064 4183 3049 281 -316 -388 O ATOM 1759 OD2 ASP B 29 -23.031 125.952 16.161 1.00 31.07 O ANISOU 1759 OD2 ASP B 29 4201 4373 3230 338 -269 -493 O ATOM 1760 N VAL B 30 -22.695 129.273 18.964 1.00 27.85 N ANISOU 1760 N VAL B 30 3768 4051 2764 209 -337 -323 N ATOM 1761 CA VAL B 30 -23.084 129.993 20.187 1.00 27.10 C ANISOU 1761 CA VAL B 30 3700 3941 2655 169 -363 -282 C ATOM 1762 C VAL B 30 -21.861 130.324 21.050 1.00 27.33 C ANISOU 1762 C VAL B 30 3677 4027 2680 173 -392 -266 C ATOM 1763 O VAL B 30 -21.703 131.459 21.489 1.00 26.83 O ANISOU 1763 O VAL B 30 3606 3994 2594 116 -398 -257 O ATOM 1764 CB VAL B 30 -24.110 129.200 21.034 1.00 26.89 C ANISOU 1764 CB VAL B 30 3736 3840 2640 181 -382 -258 C ATOM 1765 CG1 VAL B 30 -24.330 129.862 22.399 1.00 26.75 C ANISOU 1765 CG1 VAL B 30 3736 3829 2598 149 -408 -222 C ATOM 1766 CG2 VAL B 30 -25.436 129.056 20.286 1.00 26.43 C ANISOU 1766 CG2 VAL B 30 3723 3741 2577 157 -357 -273 C ATOM 1767 N GLY B 30A -20.989 129.337 21.245 1.00 27.42 N ANISOU 1767 N GLY B 30A 3651 4052 2715 241 -409 -265 N ATOM 1768 CA GLY B 30A -19.743 129.537 21.992 1.00 27.80 C ANISOU 1768 CA GLY B 30A 3632 4177 2755 253 -441 -247 C ATOM 1769 C GLY B 30A -18.545 130.005 21.178 1.00 27.97 C ANISOU 1769 C GLY B 30A 3566 4291 2770 248 -422 -273 C ATOM 1770 O GLY B 30A -17.433 130.032 21.696 1.00 28.19 O ANISOU 1770 O GLY B 30A 3523 4397 2793 264 -448 -261 O ATOM 1771 N GLY B 30B -18.755 130.362 19.911 1.00 27.67 N ANISOU 1771 N GLY B 30B 3526 4260 2727 223 -378 -304 N ATOM 1772 CA GLY B 30B -17.691 130.912 19.062 1.00 27.89 C ANISOU 1772 CA GLY B 30B 3469 4386 2740 203 -353 -322 C ATOM 1773 C GLY B 30B -17.726 132.422 18.910 1.00 27.57 C ANISOU 1773 C GLY B 30B 3427 4375 2672 98 -341 -308 C ATOM 1774 O GLY B 30B -16.711 133.028 18.584 1.00 28.10 O ANISOU 1774 O GLY B 30B 3419 4530 2726 60 -331 -309 O ATOM 1775 N TYR B 30C -18.896 133.028 19.103 1.00 26.46 N ANISOU 1775 N TYR B 30C 3367 4158 2527 51 -338 -295 N ATOM 1776 CA TYR B 30C -19.068 134.472 18.927 1.00 26.34 C ANISOU 1776 CA TYR B 30C 3367 4143 2500 -41 -322 -279 C ATOM 1777 C TYR B 30C -20.031 134.973 19.990 1.00 25.89 C ANISOU 1777 C TYR B 30C 3385 4007 2444 -70 -343 -267 C ATOM 1778 O TYR B 30C -20.646 134.178 20.699 1.00 25.39 O ANISOU 1778 O TYR B 30C 3361 3901 2385 -24 -365 -267 O ATOM 1779 CB TYR B 30C -19.630 134.797 17.518 1.00 26.03 C ANISOU 1779 CB TYR B 30C 3341 4099 2448 -57 -276 -273 C ATOM 1780 CG TYR B 30C -18.922 134.081 16.392 1.00 26.49 C ANISOU 1780 CG TYR B 30C 3333 4236 2494 -15 -249 -297 C ATOM 1781 CD1 TYR B 30C -17.839 134.661 15.728 1.00 27.05 C ANISOU 1781 CD1 TYR B 30C 3326 4404 2548 -55 -226 -290 C ATOM 1782 CD2 TYR B 30C -19.322 132.803 16.005 1.00 26.47 C ANISOU 1782 CD2 TYR B 30C 3346 4213 2497 63 -244 -331 C ATOM 1783 CE1 TYR B 30C -17.172 133.981 14.717 1.00 27.60 C ANISOU 1783 CE1 TYR B 30C 3328 4560 2598 -10 -195 -320 C ATOM 1784 CE2 TYR B 30C -18.664 132.120 14.988 1.00 27.14 C ANISOU 1784 CE2 TYR B 30C 3372 4369 2570 109 -215 -368 C ATOM 1785 CZ TYR B 30C -17.581 132.713 14.357 1.00 27.58 C ANISOU 1785 CZ TYR B 30C 3344 4534 2602 76 -190 -364 C ATOM 1786 OH TYR B 30C -16.926 132.059 13.332 1.00 28.67 O ANISOU 1786 OH TYR B 30C 3417 4757 2720 124 -154 -407 O ATOM 1787 N ASN B 31 -20.155 136.291 20.094 1.00 26.26 N ANISOU 1787 N ASN B 31 3454 4034 2490 -146 -333 -259 N ATOM 1788 CA ASN B 31 -21.230 136.912 20.893 1.00 26.20 C ANISOU 1788 CA ASN B 31 3523 3946 2485 -169 -339 -257 C ATOM 1789 C ASN B 31 -22.250 137.575 19.960 1.00 25.82 C ANISOU 1789 C ASN B 31 3523 3844 2445 -182 -301 -234 C ATOM 1790 O ASN B 31 -22.641 138.729 20.147 1.00 25.66 O ANISOU 1790 O ASN B 31 3542 3771 2436 -229 -289 -226 O ATOM 1791 CB ASN B 31 -20.632 137.882 21.914 1.00 26.74 C ANISOU 1791 CB ASN B 31 3587 4022 2550 -239 -360 -275 C ATOM 1792 CG ASN B 31 -19.856 137.153 23.002 1.00 27.33 C ANISOU 1792 CG ASN B 31 3619 4162 2605 -217 -406 -289 C ATOM 1793 OD1 ASN B 31 -20.367 136.211 23.593 1.00 27.21 O ANISOU 1793 OD1 ASN B 31 3626 4133 2580 -157 -426 -282 O ATOM 1794 ND2 ASN B 31 -18.617 137.560 23.245 1.00 28.11 N ANISOU 1794 ND2 ASN B 31 3650 4335 2695 -267 -424 -302 N ATOM 1795 N TYR B 32 -22.674 136.807 18.956 1.00 25.80 N ANISOU 1795 N TYR B 32 3514 3854 2435 -136 -284 -226 N ATOM 1796 CA TYR B 32 -23.670 137.234 17.981 1.00 25.93 C ANISOU 1796 CA TYR B 32 3562 3843 2446 -138 -253 -198 C ATOM 1797 C TYR B 32 -24.891 136.320 18.100 1.00 25.47 C ANISOU 1797 C TYR B 32 3543 3753 2382 -86 -260 -205 C ATOM 1798 O TYR B 32 -25.326 135.700 17.129 1.00 25.05 O ANISOU 1798 O TYR B 32 3482 3722 2313 -61 -245 -206 O ATOM 1799 CB TYR B 32 -23.075 137.220 16.565 1.00 26.51 C ANISOU 1799 CB TYR B 32 3584 3987 2503 -146 -225 -185 C ATOM 1800 CG TYR B 32 -21.908 138.174 16.380 1.00 27.64 C ANISOU 1800 CG TYR B 32 3683 4168 2650 -211 -213 -169 C ATOM 1801 CD1 TYR B 32 -21.972 139.487 16.851 1.00 28.25 C ANISOU 1801 CD1 TYR B 32 3795 4186 2751 -274 -210 -145 C ATOM 1802 CD2 TYR B 32 -20.747 137.777 15.715 1.00 28.45 C ANISOU 1802 CD2 TYR B 32 3708 4365 2736 -213 -202 -179 C ATOM 1803 CE1 TYR B 32 -20.919 140.374 16.668 1.00 29.33 C ANISOU 1803 CE1 TYR B 32 3895 4351 2898 -349 -199 -129 C ATOM 1804 CE2 TYR B 32 -19.684 138.661 15.529 1.00 29.44 C ANISOU 1804 CE2 TYR B 32 3786 4538 2864 -285 -190 -159 C ATOM 1805 CZ TYR B 32 -19.781 139.954 16.005 1.00 29.79 C ANISOU 1805 CZ TYR B 32 3870 4516 2934 -359 -190 -132 C ATOM 1806 OH TYR B 32 -18.753 140.836 15.842 1.00 31.07 O ANISOU 1806 OH TYR B 32 3988 4715 3103 -444 -178 -113 O ATOM 1807 N VAL B 33 -25.429 136.257 19.320 1.00 25.05 N ANISOU 1807 N VAL B 33 3529 3654 2335 -79 -281 -213 N ATOM 1808 CA VAL B 33 -26.634 135.495 19.637 1.00 24.67 C ANISOU 1808 CA VAL B 33 3517 3574 2280 -44 -287 -213 C ATOM 1809 C VAL B 33 -27.819 136.459 19.721 1.00 24.32 C ANISOU 1809 C VAL B 33 3515 3491 2236 -55 -270 -192 C ATOM 1810 O VAL B 33 -27.765 137.482 20.424 1.00 23.87 O ANISOU 1810 O VAL B 33 3479 3402 2188 -79 -268 -193 O ATOM 1811 CB VAL B 33 -26.491 134.738 20.974 1.00 24.93 C ANISOU 1811 CB VAL B 33 3561 3596 2313 -27 -319 -225 C ATOM 1812 CG1 VAL B 33 -27.762 133.960 21.302 1.00 24.62 C ANISOU 1812 CG1 VAL B 33 3559 3528 2268 -4 -321 -217 C ATOM 1813 CG2 VAL B 33 -25.300 133.786 20.921 1.00 25.39 C ANISOU 1813 CG2 VAL B 33 3575 3691 2380 0 -337 -238 C ATOM 1814 N SER B 34 -28.879 136.133 18.992 1.00 23.67 N ANISOU 1814 N SER B 34 3440 3412 2141 -36 -257 -177 N ATOM 1815 CA SER B 34 -30.102 136.902 19.017 1.00 23.43 C ANISOU 1815 CA SER B 34 3437 3357 2109 -30 -241 -151 C ATOM 1816 C SER B 34 -31.279 135.984 19.281 1.00 23.29 C ANISOU 1816 C SER B 34 3430 3345 2075 -8 -248 -155 C ATOM 1817 O SER B 34 -31.195 134.781 19.051 1.00 23.22 O ANISOU 1817 O SER B 34 3410 3354 2060 -3 -260 -172 O ATOM 1818 CB SER B 34 -30.285 137.684 17.708 1.00 23.60 C ANISOU 1818 CB SER B 34 3445 3397 2125 -34 -218 -112 C ATOM 1819 OG SER B 34 -30.239 136.829 16.574 1.00 23.41 O ANISOU 1819 OG SER B 34 3388 3433 2075 -29 -216 -115 O ATOM 1820 N TRP B 35 -32.352 136.562 19.825 1.00 23.73 N ANISOU 1820 N TRP B 35 3506 3381 2127 4 -239 -140 N ATOM 1821 CA TRP B 35 -33.558 135.830 20.210 1.00 23.56 C ANISOU 1821 CA TRP B 35 3488 3374 2087 16 -242 -138 C ATOM 1822 C TRP B 35 -34.774 136.477 19.550 1.00 23.53 C ANISOU 1822 C TRP B 35 3474 3393 2073 35 -222 -106 C ATOM 1823 O TRP B 35 -34.828 137.700 19.418 1.00 23.70 O ANISOU 1823 O TRP B 35 3503 3391 2110 51 -205 -84 O ATOM 1824 CB TRP B 35 -33.728 135.853 21.729 1.00 23.73 C ANISOU 1824 CB TRP B 35 3535 3376 2106 16 -248 -153 C ATOM 1825 CG TRP B 35 -32.739 135.016 22.492 1.00 23.82 C ANISOU 1825 CG TRP B 35 3550 3381 2118 3 -274 -171 C ATOM 1826 CD1 TRP B 35 -31.504 135.396 22.950 1.00 24.14 C ANISOU 1826 CD1 TRP B 35 3591 3413 2168 -8 -287 -189 C ATOM 1827 CD2 TRP B 35 -32.924 133.665 22.918 1.00 23.88 C ANISOU 1827 CD2 TRP B 35 3560 3394 2118 1 -292 -167 C ATOM 1828 NE1 TRP B 35 -30.905 134.357 23.629 1.00 24.14 N ANISOU 1828 NE1 TRP B 35 3588 3423 2163 -7 -314 -191 N ATOM 1829 CE2 TRP B 35 -31.758 133.284 23.630 1.00 24.03 C ANISOU 1829 CE2 TRP B 35 3580 3407 2142 0 -316 -175 C ATOM 1830 CE3 TRP B 35 -33.966 132.739 22.786 1.00 23.98 C ANISOU 1830 CE3 TRP B 35 3574 3416 2122 -5 -290 -154 C ATOM 1831 CZ2 TRP B 35 -31.605 132.007 24.189 1.00 24.08 C ANISOU 1831 CZ2 TRP B 35 3593 3407 2149 5 -338 -160 C ATOM 1832 CZ3 TRP B 35 -33.811 131.467 23.355 1.00 24.01 C ANISOU 1832 CZ3 TRP B 35 3589 3403 2130 -13 -310 -145 C ATOM 1833 CH2 TRP B 35 -32.640 131.120 24.042 1.00 24.16 C ANISOU 1833 CH2 TRP B 35 3614 3408 2159 -2 -333 -144 C ATOM 1834 N TYR B 36 -35.735 135.649 19.146 1.00 23.35 N ANISOU 1834 N TYR B 36 3430 3414 2027 33 -226 -100 N ATOM 1835 CA TYR B 36 -36.910 136.089 18.385 1.00 23.45 C ANISOU 1835 CA TYR B 36 3416 3475 2020 52 -213 -65 C ATOM 1836 C TYR B 36 -38.170 135.546 19.020 1.00 23.43 C ANISOU 1836 C TYR B 36 3401 3504 1997 52 -214 -64 C ATOM 1837 O TYR B 36 -38.192 134.404 19.464 1.00 23.49 O ANISOU 1837 O TYR B 36 3414 3511 1999 20 -227 -88 O ATOM 1838 CB TYR B 36 -36.811 135.647 16.907 1.00 23.47 C ANISOU 1838 CB TYR B 36 3387 3535 1997 36 -219 -59 C ATOM 1839 CG TYR B 36 -35.583 136.223 16.285 1.00 23.60 C ANISOU 1839 CG TYR B 36 3407 3534 2026 34 -213 -53 C ATOM 1840 CD1 TYR B 36 -34.362 135.587 16.424 1.00 23.61 C ANISOU 1840 CD1 TYR B 36 3417 3512 2040 13 -223 -93 C ATOM 1841 CD2 TYR B 36 -35.613 137.468 15.662 1.00 24.06 C ANISOU 1841 CD2 TYR B 36 3459 3595 2087 54 -197 1 C ATOM 1842 CE1 TYR B 36 -33.205 136.148 15.928 1.00 23.78 C ANISOU 1842 CE1 TYR B 36 3433 3529 2071 6 -215 -86 C ATOM 1843 CE2 TYR B 36 -34.463 138.035 15.156 1.00 24.45 C ANISOU 1843 CE2 TYR B 36 3512 3630 2149 39 -189 13 C ATOM 1844 CZ TYR B 36 -33.258 137.374 15.293 1.00 24.33 C ANISOU 1844 CZ TYR B 36 3497 3606 2140 12 -198 -33 C ATOM 1845 OH TYR B 36 -32.108 137.934 14.795 1.00 24.66 O ANISOU 1845 OH TYR B 36 3532 3648 2191 -8 -187 -20 O ATOM 1846 N GLN B 37 -39.199 136.392 19.083 1.00 23.44 N ANISOU 1846 N GLN B 37 3384 3530 1992 89 -196 -33 N ATOM 1847 CA GLN B 37 -40.504 136.044 19.633 1.00 23.59 C ANISOU 1847 CA GLN B 37 3376 3601 1987 93 -191 -26 C ATOM 1848 C GLN B 37 -41.466 135.895 18.465 1.00 23.81 C ANISOU 1848 C GLN B 37 3347 3716 1983 93 -195 5 C ATOM 1849 O GLN B 37 -41.461 136.718 17.540 1.00 23.96 O ANISOU 1849 O GLN B 37 3350 3753 2002 127 -191 41 O ATOM 1850 CB GLN B 37 -40.982 137.149 20.585 1.00 23.88 C ANISOU 1850 CB GLN B 37 3423 3615 2036 146 -164 -20 C ATOM 1851 CG GLN B 37 -42.345 136.907 21.222 1.00 24.16 C ANISOU 1851 CG GLN B 37 3420 3718 2042 158 -151 -13 C ATOM 1852 CD GLN B 37 -42.876 138.146 21.925 1.00 24.65 C ANISOU 1852 CD GLN B 37 3484 3764 2116 229 -117 -11 C ATOM 1853 OE1 GLN B 37 -43.179 139.153 21.288 1.00 25.13 O ANISOU 1853 OE1 GLN B 37 3533 3819 2197 288 -103 20 O ATOM 1854 NE2 GLN B 37 -42.990 138.077 23.243 1.00 24.86 N ANISOU 1854 NE2 GLN B 37 3529 3787 2131 227 -103 -45 N ATOM 1855 N GLN B 38 -42.272 134.841 18.492 1.00 24.14 N ANISOU 1855 N GLN B 38 3358 3817 1996 50 -206 -6 N ATOM 1856 CA GLN B 38 -43.261 134.598 17.439 1.00 24.95 C ANISOU 1856 CA GLN B 38 3398 4023 2059 36 -215 16 C ATOM 1857 C GLN B 38 -44.624 134.219 18.025 1.00 25.46 C ANISOU 1857 C GLN B 38 3415 4161 2097 22 -210 26 C ATOM 1858 O GLN B 38 -44.778 133.153 18.629 1.00 25.12 O ANISOU 1858 O GLN B 38 3382 4110 2051 -40 -216 -1 O ATOM 1859 CB GLN B 38 -42.791 133.518 16.466 1.00 25.00 C ANISOU 1859 CB GLN B 38 3405 4046 2049 -27 -238 -21 C ATOM 1860 CG GLN B 38 -43.642 133.474 15.195 1.00 25.89 C ANISOU 1860 CG GLN B 38 3450 4278 2108 -41 -250 -3 C ATOM 1861 CD GLN B 38 -43.199 132.453 14.175 1.00 26.16 C ANISOU 1861 CD GLN B 38 3485 4336 2118 -105 -269 -56 C ATOM 1862 OE1 GLN B 38 -43.353 132.674 12.969 1.00 27.44 O ANISOU 1862 OE1 GLN B 38 3606 4586 2234 -106 -278 -44 O ATOM 1863 NE2 GLN B 38 -42.649 131.345 14.628 1.00 25.96 N ANISOU 1863 NE2 GLN B 38 3505 4237 2121 -154 -274 -113 N ATOM 1864 N HIS B 39 -45.598 135.107 17.832 1.00 26.18 N ANISOU 1864 N HIS B 39 3451 4324 2170 80 -197 71 N ATOM 1865 CA HIS B 39 -46.991 134.820 18.131 1.00 27.01 C ANISOU 1865 CA HIS B 39 3487 4535 2242 70 -191 87 C ATOM 1866 C HIS B 39 -47.657 134.146 16.922 1.00 27.93 C ANISOU 1866 C HIS B 39 3536 4766 2309 14 -219 92 C ATOM 1867 O HIS B 39 -47.128 134.230 15.801 1.00 27.43 O ANISOU 1867 O HIS B 39 3476 4711 2235 11 -236 94 O ATOM 1868 CB HIS B 39 -47.722 136.099 18.519 1.00 27.64 C ANISOU 1868 CB HIS B 39 3532 4644 2327 171 -162 129 C ATOM 1869 CG HIS B 39 -47.367 136.594 19.887 1.00 27.49 C ANISOU 1869 CG HIS B 39 3566 4539 2340 209 -132 105 C ATOM 1870 ND1 HIS B 39 -46.366 137.514 20.115 1.00 27.37 N ANISOU 1870 ND1 HIS B 39 3619 4411 2370 259 -120 95 N ATOM 1871 CD2 HIS B 39 -47.878 136.282 21.104 1.00 27.86 C ANISOU 1871 CD2 HIS B 39 3605 4606 2374 197 -112 86 C ATOM 1872 CE1 HIS B 39 -46.283 137.754 21.415 1.00 27.45 C ANISOU 1872 CE1 HIS B 39 3663 4377 2392 276 -96 63 C ATOM 1873 NE2 HIS B 39 -47.185 137.014 22.036 1.00 27.61 N ANISOU 1873 NE2 HIS B 39 3637 4481 2373 242 -90 59 N ATOM 1874 N PRO B 40 -48.795 133.456 17.141 1.00 28.78 N ANISOU 1874 N PRO B 40 3580 4972 2382 -39 -222 92 N ATOM 1875 CA PRO B 40 -49.437 132.727 16.047 1.00 29.51 C ANISOU 1875 CA PRO B 40 3609 5181 2425 -111 -251 83 C ATOM 1876 C PRO B 40 -49.736 133.594 14.823 1.00 30.38 C ANISOU 1876 C PRO B 40 3658 5388 2497 -50 -265 132 C ATOM 1877 O PRO B 40 -50.272 134.698 14.955 1.00 30.64 O ANISOU 1877 O PRO B 40 3650 5461 2531 48 -248 192 O ATOM 1878 CB PRO B 40 -50.730 132.220 16.687 1.00 30.19 C ANISOU 1878 CB PRO B 40 3622 5365 2482 -159 -245 92 C ATOM 1879 CG PRO B 40 -50.368 132.040 18.127 1.00 29.71 C ANISOU 1879 CG PRO B 40 3625 5202 2461 -159 -218 79 C ATOM 1880 CD PRO B 40 -49.472 133.196 18.431 1.00 29.02 C ANISOU 1880 CD PRO B 40 3598 5016 2414 -53 -200 92 C ATOM 1881 N GLY B 41 -49.339 133.101 13.651 1.00 30.48 N ANISOU 1881 N GLY B 41 3669 5435 2478 -103 -292 105 N ATOM 1882 CA GLY B 41 -49.621 133.761 12.386 1.00 31.53 C ANISOU 1882 CA GLY B 41 3739 5683 2558 -62 -310 155 C ATOM 1883 C GLY B 41 -48.780 134.988 12.086 1.00 31.34 C ANISOU 1883 C GLY B 41 3757 5587 2563 37 -297 210 C ATOM 1884 O GLY B 41 -48.995 135.615 11.065 1.00 32.30 O ANISOU 1884 O GLY B 41 3829 5802 2642 78 -310 269 O ATOM 1885 N LYS B 42 -47.822 135.318 12.961 1.00 30.52 N ANISOU 1885 N LYS B 42 3742 5325 2528 69 -271 194 N ATOM 1886 CA LYS B 42 -47.025 136.541 12.847 1.00 30.09 C ANISOU 1886 CA LYS B 42 3734 5186 2514 154 -254 244 C ATOM 1887 C LYS B 42 -45.581 136.216 12.473 1.00 28.66 C ANISOU 1887 C LYS B 42 3623 4916 2349 111 -257 200 C ATOM 1888 O LYS B 42 -45.117 135.090 12.661 1.00 28.08 O ANISOU 1888 O LYS B 42 3580 4810 2277 35 -266 124 O ATOM 1889 CB LYS B 42 -47.024 137.287 14.178 1.00 29.93 C ANISOU 1889 CB LYS B 42 3754 5059 2557 221 -221 252 C ATOM 1890 CG LYS B 42 -48.376 137.807 14.638 1.00 31.08 C ANISOU 1890 CG LYS B 42 3831 5284 2695 287 -207 295 C ATOM 1891 CD LYS B 42 -48.473 139.326 14.553 1.00 32.04 C ANISOU 1891 CD LYS B 42 3955 5364 2853 410 -184 370 C ATOM 1892 CE LYS B 42 -47.599 140.005 15.588 1.00 31.75 C ANISOU 1892 CE LYS B 42 4013 5160 2891 447 -152 340 C ATOM 1893 NZ LYS B 42 -47.891 141.461 15.709 1.00 32.66 N ANISOU 1893 NZ LYS B 42 4135 5221 3054 568 -123 400 N ATOM 1894 N ALA B 43 -44.880 137.222 11.962 1.00 28.07 N ANISOU 1894 N ALA B 43 3572 4802 2290 164 -248 252 N ATOM 1895 CA ALA B 43 -43.444 137.141 11.732 1.00 27.62 C ANISOU 1895 CA ALA B 43 3577 4660 2256 136 -243 220 C ATOM 1896 C ALA B 43 -42.687 137.132 13.062 1.00 26.93 C ANISOU 1896 C ALA B 43 3564 4429 2239 136 -225 174 C ATOM 1897 O ALA B 43 -43.159 137.708 14.034 1.00 26.58 O ANISOU 1897 O ALA B 43 3531 4339 2231 183 -209 190 O ATOM 1898 CB ALA B 43 -42.978 138.328 10.904 1.00 28.02 C ANISOU 1898 CB ALA B 43 3630 4710 2307 186 -234 303 C ATOM 1899 N PRO B 44 -41.496 136.508 13.097 1.00 27.16 N ANISOU 1899 N PRO B 44 3638 4397 2285 90 -228 117 N ATOM 1900 CA PRO B 44 -40.649 136.634 14.275 1.00 26.61 C ANISOU 1900 CA PRO B 44 3632 4206 2275 94 -215 84 C ATOM 1901 C PRO B 44 -40.237 138.082 14.523 1.00 27.04 C ANISOU 1901 C PRO B 44 3715 4188 2371 150 -194 134 C ATOM 1902 O PRO B 44 -40.095 138.862 13.571 1.00 27.12 O ANISOU 1902 O PRO B 44 3710 4221 2371 172 -190 194 O ATOM 1903 CB PRO B 44 -39.425 135.775 13.933 1.00 26.39 C ANISOU 1903 CB PRO B 44 3628 4152 2247 45 -224 28 C ATOM 1904 CG PRO B 44 -39.905 134.814 12.909 1.00 26.52 C ANISOU 1904 CG PRO B 44 3602 4266 2208 3 -241 1 C ATOM 1905 CD PRO B 44 -40.937 135.553 12.120 1.00 27.07 C ANISOU 1905 CD PRO B 44 3617 4437 2233 32 -243 69 C ATOM 1906 N LYS B 45 -40.084 138.425 15.801 1.00 27.13 N ANISOU 1906 N LYS B 45 3768 4113 2427 167 -181 111 N ATOM 1907 CA LYS B 45 -39.739 139.776 16.235 1.00 27.94 C ANISOU 1907 CA LYS B 45 3908 4128 2578 212 -159 139 C ATOM 1908 C LYS B 45 -38.526 139.692 17.151 1.00 27.44 C ANISOU 1908 C LYS B 45 3898 3977 2549 178 -159 82 C ATOM 1909 O LYS B 45 -38.560 138.983 18.162 1.00 26.78 O ANISOU 1909 O LYS B 45 3828 3885 2463 159 -165 32 O ATOM 1910 CB LYS B 45 -40.931 140.402 16.980 1.00 28.91 C ANISOU 1910 CB LYS B 45 4022 4248 2714 275 -140 155 C ATOM 1911 CG LYS B 45 -40.583 141.581 17.895 1.00 29.53 C ANISOU 1911 CG LYS B 45 4156 4213 2851 315 -113 144 C ATOM 1912 CD LYS B 45 -41.812 142.159 18.568 1.00 30.55 C ANISOU 1912 CD LYS B 45 4269 4349 2989 389 -89 151 C ATOM 1913 CE LYS B 45 -41.413 143.188 19.616 1.00 31.06 C ANISOU 1913 CE LYS B 45 4397 4296 3108 419 -60 110 C ATOM 1914 NZ LYS B 45 -42.597 143.617 20.399 1.00 32.28 N ANISOU 1914 NZ LYS B 45 4533 4466 3265 494 -32 98 N ATOM 1915 N VAL B 46 -37.473 140.428 16.818 1.00 27.59 N ANISOU 1915 N VAL B 46 3945 3941 2598 167 -152 96 N ATOM 1916 CA VAL B 46 -36.248 140.432 17.627 1.00 27.32 C ANISOU 1916 CA VAL B 46 3950 3838 2592 130 -155 45 C ATOM 1917 C VAL B 46 -36.475 140.980 19.052 1.00 27.47 C ANISOU 1917 C VAL B 46 4007 3791 2639 150 -142 7 C ATOM 1918 O VAL B 46 -37.036 142.054 19.233 1.00 28.10 O ANISOU 1918 O VAL B 46 4105 3824 2748 194 -119 28 O ATOM 1919 CB VAL B 46 -35.072 141.166 16.926 1.00 27.55 C ANISOU 1919 CB VAL B 46 3991 3832 2645 103 -148 72 C ATOM 1920 CG1 VAL B 46 -35.349 142.660 16.710 1.00 28.59 C ANISOU 1920 CG1 VAL B 46 4148 3897 2818 137 -122 130 C ATOM 1921 CG2 VAL B 46 -33.775 140.960 17.698 1.00 27.45 C ANISOU 1921 CG2 VAL B 46 3999 3779 2650 57 -157 15 C ATOM 1922 N MET B 47 -36.064 140.198 20.048 1.00 26.93 N ANISOU 1922 N MET B 47 3949 3723 2559 121 -158 -48 N ATOM 1923 CA MET B 47 -36.156 140.595 21.466 1.00 27.18 C ANISOU 1923 CA MET B 47 4015 3714 2600 129 -149 -94 C ATOM 1924 C MET B 47 -34.788 140.864 22.112 1.00 26.56 C ANISOU 1924 C MET B 47 3965 3587 2539 84 -159 -138 C ATOM 1925 O MET B 47 -34.697 141.669 23.049 1.00 26.71 O ANISOU 1925 O MET B 47 4018 3557 2573 86 -147 -178 O ATOM 1926 CB MET B 47 -36.882 139.509 22.266 1.00 27.41 C ANISOU 1926 CB MET B 47 4026 3798 2588 128 -159 -114 C ATOM 1927 CG MET B 47 -38.250 139.116 21.714 1.00 27.78 C ANISOU 1927 CG MET B 47 4033 3910 2612 156 -152 -77 C ATOM 1928 SD MET B 47 -39.468 140.448 21.678 1.00 29.58 S ANISOU 1928 SD MET B 47 4254 4129 2858 234 -115 -50 S ATOM 1929 CE MET B 47 -39.780 140.641 23.426 1.00 29.79 C ANISOU 1929 CE MET B 47 4305 4142 2871 247 -96 -111 C ATOM 1930 N ILE B 48 -33.753 140.145 21.665 1.00 25.31 N ANISOU 1930 N ILE B 48 3790 3453 2374 45 -183 -138 N ATOM 1931 CA ILE B 48 -32.392 140.292 22.180 1.00 24.93 C ANISOU 1931 CA ILE B 48 3752 3384 2337 0 -198 -173 C ATOM 1932 C ILE B 48 -31.417 140.163 21.017 1.00 24.31 C ANISOU 1932 C ILE B 48 3646 3322 2267 -26 -203 -148 C ATOM 1933 O ILE B 48 -31.646 139.373 20.111 1.00 24.10 O ANISOU 1933 O ILE B 48 3591 3343 2223 -14 -207 -124 O ATOM 1934 CB ILE B 48 -32.051 139.195 23.235 1.00 24.77 C ANISOU 1934 CB ILE B 48 3725 3403 2285 -13 -226 -207 C ATOM 1935 CG1 ILE B 48 -32.951 139.296 24.478 1.00 25.09 C ANISOU 1935 CG1 ILE B 48 3786 3444 2301 6 -219 -232 C ATOM 1936 CG2 ILE B 48 -30.583 139.267 23.664 1.00 24.99 C ANISOU 1936 CG2 ILE B 48 3746 3431 2317 -55 -248 -236 C ATOM 1937 CD1 ILE B 48 -32.727 140.518 25.352 1.00 25.59 C ANISOU 1937 CD1 ILE B 48 3885 3463 2376 -5 -205 -280 C ATOM 1938 N TYR B 49 -30.334 140.927 21.050 1.00 24.13 N ANISOU 1938 N TYR B 49 3630 3270 2269 -68 -202 -159 N ATOM 1939 CA TYR B 49 -29.218 140.739 20.109 1.00 24.06 C ANISOU 1939 CA TYR B 49 3584 3296 2262 -101 -207 -141 C ATOM 1940 C TYR B 49 -27.879 140.889 20.845 1.00 24.25 C ANISOU 1940 C TYR B 49 3598 3323 2293 -152 -225 -181 C ATOM 1941 O TYR B 49 -27.840 141.398 21.966 1.00 24.46 O ANISOU 1941 O TYR B 49 3653 3315 2325 -169 -231 -221 O ATOM 1942 CB TYR B 49 -29.335 141.721 18.942 1.00 24.15 C ANISOU 1942 CB TYR B 49 3599 3284 2295 -107 -179 -83 C ATOM 1943 CG TYR B 49 -29.068 143.160 19.310 1.00 24.72 C ANISOU 1943 CG TYR B 49 3711 3268 2412 -140 -161 -82 C ATOM 1944 CD1 TYR B 49 -30.046 143.937 19.934 1.00 24.80 C ANISOU 1944 CD1 TYR B 49 3771 3204 2449 -106 -144 -90 C ATOM 1945 CD2 TYR B 49 -27.839 143.751 19.027 1.00 25.10 C ANISOU 1945 CD2 TYR B 49 3748 3307 2481 -207 -157 -77 C ATOM 1946 CE1 TYR B 49 -29.793 145.250 20.281 1.00 25.57 C ANISOU 1946 CE1 TYR B 49 3915 3203 2597 -136 -125 -100 C ATOM 1947 CE2 TYR B 49 -27.588 145.067 19.353 1.00 25.84 C ANISOU 1947 CE2 TYR B 49 3887 3307 2625 -250 -140 -79 C ATOM 1948 CZ TYR B 49 -28.569 145.812 19.982 1.00 26.15 C ANISOU 1948 CZ TYR B 49 3985 3256 2696 -212 -124 -94 C ATOM 1949 OH TYR B 49 -28.313 147.119 20.321 1.00 27.28 O ANISOU 1949 OH TYR B 49 4180 3287 2896 -254 -103 -108 O ATOM 1950 N ASP B 50 -26.798 140.434 20.209 1.00 24.11 N ANISOU 1950 N ASP B 50 3533 3361 2269 -175 -233 -175 N ATOM 1951 CA ASP B 50 -25.463 140.415 20.824 1.00 24.68 C ANISOU 1951 CA ASP B 50 3574 3464 2340 -220 -255 -209 C ATOM 1952 C ASP B 50 -25.491 139.814 22.244 1.00 24.47 C ANISOU 1952 C ASP B 50 3556 3449 2293 -206 -287 -251 C ATOM 1953 O ASP B 50 -25.016 140.424 23.200 1.00 24.64 O ANISOU 1953 O ASP B 50 3587 3462 2313 -248 -300 -287 O ATOM 1954 CB ASP B 50 -24.834 141.820 20.852 1.00 25.55 C ANISOU 1954 CB ASP B 50 3697 3529 2481 -291 -241 -210 C ATOM 1955 CG ASP B 50 -24.474 142.349 19.466 1.00 26.17 C ANISOU 1955 CG ASP B 50 3754 3616 2574 -318 -212 -155 C ATOM 1956 OD1 ASP B 50 -24.493 141.594 18.467 1.00 26.20 O ANISOU 1956 OD1 ASP B 50 3720 3681 2554 -286 -205 -127 O ATOM 1957 OD2 ASP B 50 -24.132 143.540 19.385 1.00 27.14 O ANISOU 1957 OD2 ASP B 50 3897 3683 2730 -379 -195 -142 O ATOM 1958 N VAL B 51 -26.115 138.643 22.366 1.00 24.11 N ANISOU 1958 N VAL B 51 3509 3424 2227 -152 -299 -245 N ATOM 1959 CA VAL B 51 -26.271 137.911 23.630 1.00 24.21 C ANISOU 1959 CA VAL B 51 3531 3455 2215 -133 -328 -264 C ATOM 1960 C VAL B 51 -27.229 138.571 24.645 1.00 24.50 C ANISOU 1960 C VAL B 51 3617 3453 2239 -136 -320 -285 C ATOM 1961 O VAL B 51 -28.141 137.907 25.129 1.00 23.81 O ANISOU 1961 O VAL B 51 3547 3370 2131 -103 -322 -277 O ATOM 1962 CB VAL B 51 -24.910 137.627 24.327 1.00 24.88 C ANISOU 1962 CB VAL B 51 3572 3596 2286 -155 -363 -283 C ATOM 1963 CG1 VAL B 51 -25.101 136.779 25.580 1.00 24.98 C ANISOU 1963 CG1 VAL B 51 3590 3636 2265 -130 -395 -285 C ATOM 1964 CG2 VAL B 51 -23.945 136.941 23.366 1.00 25.08 C ANISOU 1964 CG2 VAL B 51 3540 3668 2323 -140 -366 -268 C ATOM 1965 N SER B 52 -26.975 139.832 25.003 1.00 25.11 N ANISOU 1965 N SER B 52 3716 3497 2330 -179 -309 -316 N ATOM 1966 CA SER B 52 -27.651 140.494 26.121 1.00 25.85 C ANISOU 1966 CA SER B 52 3854 3561 2407 -184 -302 -358 C ATOM 1967 C SER B 52 -28.312 141.854 25.837 1.00 26.50 C ANISOU 1967 C SER B 52 3983 3556 2528 -188 -262 -371 C ATOM 1968 O SER B 52 -29.007 142.360 26.700 1.00 26.37 O ANISOU 1968 O SER B 52 4003 3514 2501 -177 -248 -412 O ATOM 1969 CB SER B 52 -26.646 140.668 27.252 1.00 26.34 C ANISOU 1969 CB SER B 52 3901 3667 2439 -234 -333 -408 C ATOM 1970 OG SER B 52 -25.523 141.419 26.820 1.00 27.16 O ANISOU 1970 OG SER B 52 3985 3761 2571 -296 -336 -423 O ATOM 1971 N LYS B 53 -28.125 142.435 24.650 1.00 27.30 N ANISOU 1971 N LYS B 53 4083 3615 2673 -198 -241 -334 N ATOM 1972 CA LYS B 53 -28.696 143.765 24.374 1.00 28.55 C ANISOU 1972 CA LYS B 53 4291 3678 2879 -197 -203 -333 C ATOM 1973 C LYS B 53 -30.157 143.680 23.936 1.00 28.78 C ANISOU 1973 C LYS B 53 4334 3689 2911 -120 -178 -293 C ATOM 1974 O LYS B 53 -30.541 142.760 23.199 1.00 27.24 O ANISOU 1974 O LYS B 53 4106 3548 2696 -88 -184 -245 O ATOM 1975 CB LYS B 53 -27.868 144.494 23.318 1.00 29.26 C ANISOU 1975 CB LYS B 53 4373 3731 3012 -246 -191 -296 C ATOM 1976 CG LYS B 53 -26.457 144.799 23.792 1.00 30.27 C ANISOU 1976 CG LYS B 53 4483 3876 3142 -333 -212 -340 C ATOM 1977 CD LYS B 53 -25.658 145.483 22.706 1.00 31.45 C ANISOU 1977 CD LYS B 53 4619 4000 3332 -390 -196 -293 C ATOM 1978 CE LYS B 53 -24.198 145.618 23.090 1.00 32.31 C ANISOU 1978 CE LYS B 53 4688 4154 3435 -482 -220 -332 C ATOM 1979 NZ LYS B 53 -23.423 146.144 21.939 1.00 33.21 N ANISOU 1979 NZ LYS B 53 4776 4264 3580 -540 -201 -275 N ATOM 1980 N ARG B 54 -30.957 144.638 24.399 1.00 29.85 N ANISOU 1980 N ARG B 54 4517 3753 3072 -92 -149 -318 N ATOM 1981 CA ARG B 54 -32.369 144.735 24.038 1.00 30.76 C ANISOU 1981 CA ARG B 54 4639 3855 3193 -14 -122 -280 C ATOM 1982 C ARG B 54 -32.556 145.808 22.965 1.00 31.16 C ANISOU 1982 C ARG B 54 4711 3823 3304 4 -93 -220 C ATOM 1983 O ARG B 54 -32.014 146.903 23.099 1.00 31.62 O ANISOU 1983 O ARG B 54 4813 3789 3413 -32 -77 -242 O ATOM 1984 CB ARG B 54 -33.227 145.111 25.250 1.00 32.36 C ANISOU 1984 CB ARG B 54 4873 4039 3384 24 -102 -343 C ATOM 1985 CG ARG B 54 -33.854 143.926 25.957 1.00 32.94 C ANISOU 1985 CG ARG B 54 4915 4211 3390 47 -118 -354 C ATOM 1986 CD ARG B 54 -34.630 144.385 27.174 1.00 34.50 C ANISOU 1986 CD ARG B 54 5139 4404 3568 80 -93 -420 C ATOM 1987 NE ARG B 54 -33.725 144.812 28.237 1.00 36.09 N ANISOU 1987 NE ARG B 54 5368 4589 3754 22 -103 -505 N ATOM 1988 CZ ARG B 54 -33.614 146.045 28.735 1.00 38.25 C ANISOU 1988 CZ ARG B 54 5693 4778 4062 14 -77 -577 C ATOM 1989 NH1 ARG B 54 -34.370 147.064 28.304 1.00 39.40 N ANISOU 1989 NH1 ARG B 54 5872 4827 4269 73 -33 -571 N ATOM 1990 NH2 ARG B 54 -32.729 146.264 29.702 1.00 39.40 N ANISOU 1990 NH2 ARG B 54 5855 4935 4181 -53 -95 -659 N ATOM 1991 N PRO B 55 -33.330 145.503 21.909 1.00 30.64 N ANISOU 1991 N PRO B 55 4616 3794 3232 54 -87 -143 N ATOM 1992 CA PRO B 55 -33.763 146.570 21.004 1.00 31.54 C ANISOU 1992 CA PRO B 55 4751 3836 3398 91 -58 -73 C ATOM 1993 C PRO B 55 -34.667 147.568 21.709 1.00 32.45 C ANISOU 1993 C PRO B 55 4913 3861 3556 154 -25 -102 C ATOM 1994 O PRO B 55 -35.273 147.255 22.742 1.00 31.70 O ANISOU 1994 O PRO B 55 4819 3793 3432 184 -21 -167 O ATOM 1995 CB PRO B 55 -34.562 145.825 19.924 1.00 30.92 C ANISOU 1995 CB PRO B 55 4618 3850 3281 136 -66 4 C ATOM 1996 CG PRO B 55 -34.062 144.429 19.971 1.00 29.95 C ANISOU 1996 CG PRO B 55 4453 3827 3101 95 -99 -25 C ATOM 1997 CD PRO B 55 -33.729 144.176 21.410 1.00 29.91 C ANISOU 1997 CD PRO B 55 4470 3810 3086 71 -109 -112 C ATOM 1998 N SER B 56 -34.772 148.758 21.142 1.00 33.98 N ANISOU 1998 N SER B 56 5145 3949 3817 178 3 -51 N ATOM 1999 CA SER B 56 -35.660 149.783 21.685 1.00 35.37 C ANISOU 1999 CA SER B 56 5369 4023 4047 256 41 -75 C ATOM 2000 C SER B 56 -37.090 149.270 21.681 1.00 35.06 C ANISOU 2000 C SER B 56 5283 4070 3968 355 48 -49 C ATOM 2001 O SER B 56 -37.507 148.634 20.712 1.00 34.49 O ANISOU 2001 O SER B 56 5154 4092 3859 376 31 33 O ATOM 2002 CB SER B 56 -35.570 151.022 20.819 1.00 36.61 C ANISOU 2002 CB SER B 56 5569 4054 4287 273 67 8 C ATOM 2003 OG SER B 56 -36.476 152.020 21.238 1.00 38.50 O ANISOU 2003 OG SER B 56 5856 4183 4589 366 107 -7 O ATOM 2004 N GLY B 57 -37.819 149.526 22.765 1.00 35.24 N ANISOU 2004 N GLY B 57 5323 4073 3992 410 72 -126 N ATOM 2005 CA GLY B 57 -39.218 149.093 22.890 1.00 35.34 C ANISOU 2005 CA GLY B 57 5284 4177 3967 503 83 -109 C ATOM 2006 C GLY B 57 -39.427 147.732 23.521 1.00 34.44 C ANISOU 2006 C GLY B 57 5118 4203 3764 469 58 -151 C ATOM 2007 O GLY B 57 -40.534 147.437 23.969 1.00 34.62 O ANISOU 2007 O GLY B 57 5104 4298 3754 531 73 -162 O ATOM 2008 N VAL B 58 -38.388 146.894 23.548 1.00 33.63 N ANISOU 2008 N VAL B 58 5010 4142 3626 375 21 -169 N ATOM 2009 CA VAL B 58 -38.480 145.578 24.181 1.00 32.80 C ANISOU 2009 CA VAL B 58 4866 4152 3445 339 -4 -201 C ATOM 2010 C VAL B 58 -38.423 145.777 25.703 1.00 33.06 C ANISOU 2010 C VAL B 58 4930 4173 3457 331 10 -303 C ATOM 2011 O VAL B 58 -37.488 146.411 26.194 1.00 33.26 O ANISOU 2011 O VAL B 58 5006 4123 3510 286 11 -362 O ATOM 2012 CB VAL B 58 -37.358 144.632 23.707 1.00 32.13 C ANISOU 2012 CB VAL B 58 4765 4107 3336 255 -46 -184 C ATOM 2013 CG1 VAL B 58 -37.339 143.345 24.525 1.00 31.38 C ANISOU 2013 CG1 VAL B 58 4644 4102 3175 220 -71 -219 C ATOM 2014 CG2 VAL B 58 -37.537 144.326 22.222 1.00 32.10 C ANISOU 2014 CG2 VAL B 58 4723 4141 3334 264 -58 -94 C ATOM 2015 N PRO B 59 -39.423 145.252 26.446 1.00 33.14 N ANISOU 2015 N PRO B 59 4908 4269 3416 368 23 -325 N ATOM 2016 CA PRO B 59 -39.454 145.463 27.905 1.00 33.98 C ANISOU 2016 CA PRO B 59 5039 4383 3487 364 41 -422 C ATOM 2017 C PRO B 59 -38.247 144.871 28.633 1.00 33.72 C ANISOU 2017 C PRO B 59 5022 4375 3413 271 4 -468 C ATOM 2018 O PRO B 59 -37.695 143.854 28.207 1.00 33.16 O ANISOU 2018 O PRO B 59 4924 4353 3320 221 -36 -421 O ATOM 2019 CB PRO B 59 -40.751 144.759 28.343 1.00 33.90 C ANISOU 2019 CB PRO B 59 4972 4491 3417 409 57 -409 C ATOM 2020 CG PRO B 59 -41.585 144.646 27.118 1.00 33.69 C ANISOU 2020 CG PRO B 59 4898 4487 3414 461 59 -317 C ATOM 2021 CD PRO B 59 -40.629 144.539 25.974 1.00 33.18 C ANISOU 2021 CD PRO B 59 4847 4373 3387 413 24 -263 C ATOM 2022 N ASP B 60 -37.847 145.516 29.719 1.00 34.59 N ANISOU 2022 N ASP B 60 5175 4456 3514 252 17 -564 N ATOM 2023 CA ASP B 60 -36.663 145.101 30.474 1.00 34.59 C ANISOU 2023 CA ASP B 60 5184 4487 3470 165 -21 -611 C ATOM 2024 C ASP B 60 -36.802 143.759 31.211 1.00 33.16 C ANISOU 2024 C ASP B 60 4961 4439 3199 141 -48 -592 C ATOM 2025 O ASP B 60 -35.806 143.232 31.700 1.00 32.16 O ANISOU 2025 O ASP B 60 4833 4352 3036 77 -88 -605 O ATOM 2026 CB ASP B 60 -36.202 146.206 31.438 1.00 36.62 C ANISOU 2026 CB ASP B 60 5497 4685 3734 142 -1 -727 C ATOM 2027 CG ASP B 60 -37.261 146.594 32.460 1.00 38.34 C ANISOU 2027 CG ASP B 60 5721 4936 3910 202 45 -802 C ATOM 2028 OD1 ASP B 60 -38.269 145.863 32.630 1.00 39.24 O ANISOU 2028 OD1 ASP B 60 5789 5148 3974 248 56 -761 O ATOM 2029 OD2 ASP B 60 -37.085 147.657 33.091 1.00 40.56 O ANISOU 2029 OD2 ASP B 60 6053 5146 4210 201 73 -906 O ATOM 2030 N ARG B 61 -38.016 143.211 31.280 1.00 32.10 N ANISOU 2030 N ARG B 61 4791 4375 3032 189 -28 -556 N ATOM 2031 CA ARG B 61 -38.219 141.857 31.812 1.00 31.28 C ANISOU 2031 CA ARG B 61 4647 4384 2853 160 -53 -515 C ATOM 2032 C ARG B 61 -37.585 140.744 30.958 1.00 29.42 C ANISOU 2032 C ARG B 61 4390 4154 2633 119 -99 -436 C ATOM 2033 O ARG B 61 -37.397 139.635 31.463 1.00 28.40 O ANISOU 2033 O ARG B 61 4243 4093 2454 85 -127 -406 O ATOM 2034 CB ARG B 61 -39.705 141.570 32.086 1.00 32.02 C ANISOU 2034 CB ARG B 61 4702 4556 2909 211 -16 -495 C ATOM 2035 CG ARG B 61 -40.612 141.436 30.871 1.00 32.26 C ANISOU 2035 CG ARG B 61 4697 4578 2984 256 -5 -424 C ATOM 2036 CD ARG B 61 -42.031 141.041 31.276 1.00 32.86 C ANISOU 2036 CD ARG B 61 4719 4756 3009 292 28 -405 C ATOM 2037 NE ARG B 61 -42.918 140.978 30.117 1.00 33.17 N ANISOU 2037 NE ARG B 61 4715 4802 3085 333 36 -341 N ATOM 2038 CZ ARG B 61 -43.575 142.003 29.577 1.00 33.68 C ANISOU 2038 CZ ARG B 61 4772 4829 3195 414 70 -343 C ATOM 2039 NH1 ARG B 61 -43.478 143.232 30.067 1.00 34.82 N ANISOU 2039 NH1 ARG B 61 4957 4904 3368 467 105 -413 N ATOM 2040 NH2 ARG B 61 -44.338 141.786 28.510 1.00 33.86 N ANISOU 2040 NH2 ARG B 61 4744 4883 3237 443 67 -273 N ATOM 2041 N PHE B 62 -37.267 141.040 29.687 1.00 28.18 N ANISOU 2041 N PHE B 62 4238 3927 2544 127 -105 -402 N ATOM 2042 CA PHE B 62 -36.489 140.147 28.824 1.00 27.12 C ANISOU 2042 CA PHE B 62 4087 3790 2427 91 -144 -348 C ATOM 2043 C PHE B 62 -34.986 140.409 28.944 1.00 26.89 C ANISOU 2043 C PHE B 62 4078 3725 2412 42 -173 -378 C ATOM 2044 O PHE B 62 -34.535 141.538 28.732 1.00 27.08 O ANISOU 2044 O PHE B 62 4130 3682 2479 37 -159 -414 O ATOM 2045 CB PHE B 62 -36.901 140.325 27.352 1.00 26.93 C ANISOU 2045 CB PHE B 62 4048 3730 2452 120 -134 -296 C ATOM 2046 CG PHE B 62 -38.315 139.911 27.065 1.00 26.92 C ANISOU 2046 CG PHE B 62 4012 3784 2435 158 -115 -257 C ATOM 2047 CD1 PHE B 62 -39.363 140.816 27.195 1.00 27.66 C ANISOU 2047 CD1 PHE B 62 4101 3873 2535 219 -75 -268 C ATOM 2048 CD2 PHE B 62 -38.602 138.613 26.683 1.00 26.78 C ANISOU 2048 CD2 PHE B 62 3962 3820 2394 134 -137 -212 C ATOM 2049 CE1 PHE B 62 -40.674 140.431 26.939 1.00 27.83 C ANISOU 2049 CE1 PHE B 62 4075 3963 2536 253 -59 -230 C ATOM 2050 CE2 PHE B 62 -39.910 138.216 26.432 1.00 26.79 C ANISOU 2050 CE2 PHE B 62 3923 3881 2375 154 -121 -180 C ATOM 2051 CZ PHE B 62 -40.946 139.126 26.557 1.00 27.30 C ANISOU 2051 CZ PHE B 62 3971 3960 2440 213 -84 -186 C ATOM 2052 N SER B 63 -34.216 139.371 29.278 1.00 26.43 N ANISOU 2052 N SER B 63 4004 3715 2325 7 -212 -361 N ATOM 2053 CA SER B 63 -32.758 139.468 29.348 1.00 26.27 C ANISOU 2053 CA SER B 63 3984 3684 2313 -37 -244 -381 C ATOM 2054 C SER B 63 -32.110 138.252 28.691 1.00 25.36 C ANISOU 2054 C SER B 63 3838 3590 2206 -45 -278 -326 C ATOM 2055 O SER B 63 -32.672 137.170 28.668 1.00 24.80 O ANISOU 2055 O SER B 63 3755 3550 2120 -30 -284 -284 O ATOM 2056 CB SER B 63 -32.255 139.587 30.798 1.00 27.24 C ANISOU 2056 CB SER B 63 4114 3859 2378 -68 -262 -434 C ATOM 2057 OG SER B 63 -32.801 138.557 31.590 1.00 27.75 O ANISOU 2057 OG SER B 63 4163 3997 2382 -59 -273 -402 O ATOM 2058 N GLY B 64 -30.902 138.456 28.185 1.00 24.89 N ANISOU 2058 N GLY B 64 3768 3515 2176 -71 -296 -332 N ATOM 2059 CA GLY B 64 -30.136 137.411 27.540 1.00 24.03 C ANISOU 2059 CA GLY B 64 3627 3425 2079 -71 -323 -293 C ATOM 2060 C GLY B 64 -28.808 137.187 28.245 1.00 24.18 C ANISOU 2060 C GLY B 64 3621 3488 2077 -99 -362 -308 C ATOM 2061 O GLY B 64 -28.216 138.125 28.805 1.00 23.94 O ANISOU 2061 O GLY B 64 3596 3463 2038 -137 -366 -355 O ATOM 2062 N SER B 65 -28.330 135.953 28.189 1.00 23.73 N ANISOU 2062 N SER B 65 3538 3462 2017 -80 -390 -270 N ATOM 2063 CA SER B 65 -27.041 135.579 28.774 1.00 24.08 C ANISOU 2063 CA SER B 65 3546 3561 2042 -91 -432 -269 C ATOM 2064 C SER B 65 -26.421 134.419 28.018 1.00 24.15 C ANISOU 2064 C SER B 65 3523 3572 2082 -54 -448 -229 C ATOM 2065 O SER B 65 -27.040 133.848 27.113 1.00 23.49 O ANISOU 2065 O SER B 65 3450 3446 2028 -28 -428 -209 O ATOM 2066 CB SER B 65 -27.221 135.210 30.241 1.00 24.67 C ANISOU 2066 CB SER B 65 3627 3692 2055 -93 -457 -261 C ATOM 2067 OG SER B 65 -28.151 134.163 30.379 1.00 24.32 O ANISOU 2067 OG SER B 65 3600 3637 2003 -60 -453 -211 O ATOM 2068 N LYS B 66 -25.180 134.098 28.377 1.00 24.62 N ANISOU 2068 N LYS B 66 3537 3685 2132 -52 -484 -223 N ATOM 2069 CA LYS B 66 -24.460 132.995 27.763 1.00 24.71 C ANISOU 2069 CA LYS B 66 3513 3702 2176 -5 -499 -191 C ATOM 2070 C LYS B 66 -23.514 132.324 28.747 1.00 24.83 C ANISOU 2070 C LYS B 66 3487 3784 2164 19 -547 -161 C ATOM 2071 O LYS B 66 -22.914 132.995 29.592 1.00 25.04 O ANISOU 2071 O LYS B 66 3489 3879 2148 -19 -572 -180 O ATOM 2072 CB LYS B 66 -23.667 133.487 26.549 1.00 25.06 C ANISOU 2072 CB LYS B 66 3519 3748 2255 -16 -480 -217 C ATOM 2073 CG LYS B 66 -23.255 132.358 25.619 1.00 25.43 C ANISOU 2073 CG LYS B 66 3539 3785 2339 42 -477 -200 C ATOM 2074 CD LYS B 66 -22.650 132.877 24.314 1.00 25.64 C ANISOU 2074 CD LYS B 66 3528 3825 2388 28 -449 -226 C ATOM 2075 CE LYS B 66 -21.138 132.893 24.368 1.00 26.44 C ANISOU 2075 CE LYS B 66 3551 4005 2488 32 -471 -231 C ATOM 2076 NZ LYS B 66 -20.554 133.402 23.098 1.00 26.51 N ANISOU 2076 NZ LYS B 66 3519 4040 2512 11 -439 -251 N ATOM 2077 N SER B 67 -23.389 131.005 28.603 1.00 24.60 N ANISOU 2077 N SER B 67 3451 3734 2160 82 -560 -113 N ATOM 2078 CA SER B 67 -22.525 130.161 29.428 1.00 25.24 C ANISOU 2078 CA SER B 67 3493 3869 2226 127 -607 -63 C ATOM 2079 C SER B 67 -21.986 129.041 28.557 1.00 25.62 C ANISOU 2079 C SER B 67 3519 3878 2336 202 -604 -42 C ATOM 2080 O SER B 67 -22.760 128.221 28.067 1.00 25.42 O ANISOU 2080 O SER B 67 3541 3767 2351 230 -583 -28 O ATOM 2081 CB SER B 67 -23.334 129.566 30.593 1.00 25.41 C ANISOU 2081 CB SER B 67 3557 3888 2208 132 -625 -7 C ATOM 2082 OG SER B 67 -22.518 128.779 31.428 1.00 26.15 O ANISOU 2082 OG SER B 67 3613 4040 2283 178 -673 57 O ATOM 2083 N GLY B 68 -20.673 129.024 28.332 1.00 26.40 N ANISOU 2083 N GLY B 68 3544 4041 2445 231 -623 -49 N ATOM 2084 CA GLY B 68 -20.047 128.079 27.407 1.00 26.76 C ANISOU 2084 CA GLY B 68 3559 4058 2551 310 -613 -46 C ATOM 2085 C GLY B 68 -20.689 128.121 26.026 1.00 26.17 C ANISOU 2085 C GLY B 68 3519 3908 2515 300 -560 -97 C ATOM 2086 O GLY B 68 -20.690 129.171 25.361 1.00 25.88 O ANISOU 2086 O GLY B 68 3471 3896 2466 242 -534 -143 O ATOM 2087 N ASN B 69 -21.254 126.988 25.605 1.00 26.11 N ANISOU 2087 N ASN B 69 3558 3810 2554 350 -546 -86 N ATOM 2088 CA ASN B 69 -21.984 126.899 24.330 1.00 25.77 C ANISOU 2088 CA ASN B 69 3549 3703 2538 337 -500 -136 C ATOM 2089 C ASN B 69 -23.504 127.019 24.484 1.00 25.19 C ANISOU 2089 C ASN B 69 3551 3568 2451 283 -485 -129 C ATOM 2090 O ASN B 69 -24.245 126.648 23.569 1.00 24.90 O ANISOU 2090 O ASN B 69 3547 3476 2437 276 -455 -160 O ATOM 2091 CB ASN B 69 -21.662 125.578 23.624 1.00 26.42 C ANISOU 2091 CB ASN B 69 3633 3724 2681 419 -488 -150 C ATOM 2092 CG ASN B 69 -20.182 125.387 23.379 1.00 27.28 C ANISOU 2092 CG ASN B 69 3658 3899 2807 487 -496 -161 C ATOM 2093 OD1 ASN B 69 -19.495 126.298 22.930 1.00 27.46 O ANISOU 2093 OD1 ASN B 69 3620 4012 2802 458 -485 -192 O ATOM 2094 ND2 ASN B 69 -19.683 124.191 23.661 1.00 28.31 N ANISOU 2094 ND2 ASN B 69 3784 3986 2986 581 -512 -131 N ATOM 2095 N THR B 70 -23.970 127.548 25.614 1.00 24.89 N ANISOU 2095 N THR B 70 3532 3553 2370 242 -505 -95 N ATOM 2096 CA THR B 70 -25.396 127.685 25.870 1.00 24.77 C ANISOU 2096 CA THR B 70 3576 3498 2337 195 -489 -85 C ATOM 2097 C THR B 70 -25.771 129.146 26.087 1.00 24.32 C ANISOU 2097 C THR B 70 3518 3488 2235 135 -478 -110 C ATOM 2098 O THR B 70 -25.227 129.810 26.965 1.00 24.93 O ANISOU 2098 O THR B 70 3573 3623 2275 117 -500 -106 O ATOM 2099 CB THR B 70 -25.817 126.831 27.084 1.00 25.19 C ANISOU 2099 CB THR B 70 3663 3529 2381 207 -516 -17 C ATOM 2100 OG1 THR B 70 -25.426 125.471 26.855 1.00 26.04 O ANISOU 2100 OG1 THR B 70 3778 3571 2545 269 -525 10 O ATOM 2101 CG2 THR B 70 -27.305 126.874 27.316 1.00 24.89 C ANISOU 2101 CG2 THR B 70 3675 3459 2323 158 -496 -5 C ATOM 2102 N ALA B 71 -26.709 129.630 25.282 1.00 23.94 N ANISOU 2102 N ALA B 71 3493 3414 2189 105 -444 -138 N ATOM 2103 CA ALA B 71 -27.334 130.922 25.489 1.00 23.83 C ANISOU 2103 CA ALA B 71 3491 3419 2142 59 -427 -155 C ATOM 2104 C ALA B 71 -28.634 130.707 26.250 1.00 23.99 C ANISOU 2104 C ALA B 71 3553 3424 2139 44 -422 -130 C ATOM 2105 O ALA B 71 -29.228 129.622 26.192 1.00 24.59 O ANISOU 2105 O ALA B 71 3650 3464 2230 55 -422 -103 O ATOM 2106 CB ALA B 71 -27.607 131.604 24.161 1.00 23.44 C ANISOU 2106 CB ALA B 71 3438 3361 2109 44 -393 -185 C ATOM 2107 N SER B 72 -29.054 131.727 26.982 1.00 24.00 N ANISOU 2107 N SER B 72 3564 3452 2102 16 -415 -141 N ATOM 2108 CA SER B 72 -30.302 131.682 27.737 1.00 24.29 C ANISOU 2108 CA SER B 72 3630 3494 2107 3 -404 -123 C ATOM 2109 C SER B 72 -31.098 132.967 27.556 1.00 24.14 C ANISOU 2109 C SER B 72 3620 3477 2076 -14 -371 -158 C ATOM 2110 O SER B 72 -30.534 134.063 27.589 1.00 24.08 O ANISOU 2110 O SER B 72 3608 3475 2068 -25 -367 -193 O ATOM 2111 CB SER B 72 -30.034 131.439 29.221 1.00 24.80 C ANISOU 2111 CB SER B 72 3695 3605 2123 -2 -431 -97 C ATOM 2112 OG SER B 72 -29.376 130.203 29.433 1.00 25.52 O ANISOU 2112 OG SER B 72 3778 3688 2229 24 -463 -49 O ATOM 2113 N LEU B 73 -32.409 132.824 27.363 1.00 24.38 N ANISOU 2113 N LEU B 73 3662 3500 2100 -15 -346 -145 N ATOM 2114 CA LEU B 73 -33.347 133.943 27.419 1.00 24.49 C ANISOU 2114 CA LEU B 73 3683 3522 2099 -15 -314 -168 C ATOM 2115 C LEU B 73 -34.158 133.799 28.696 1.00 25.25 C ANISOU 2115 C LEU B 73 3789 3662 2145 -21 -308 -158 C ATOM 2116 O LEU B 73 -34.761 132.747 28.919 1.00 25.36 O ANISOU 2116 O LEU B 73 3800 3688 2146 -30 -312 -116 O ATOM 2117 CB LEU B 73 -34.287 133.915 26.223 1.00 24.26 C ANISOU 2117 CB LEU B 73 3646 3479 2093 -6 -291 -157 C ATOM 2118 CG LEU B 73 -35.348 135.016 26.130 1.00 24.29 C ANISOU 2118 CG LEU B 73 3649 3492 2089 10 -256 -168 C ATOM 2119 CD1 LEU B 73 -34.690 136.358 25.833 1.00 24.50 C ANISOU 2119 CD1 LEU B 73 3686 3484 2140 19 -246 -198 C ATOM 2120 CD2 LEU B 73 -36.376 134.694 25.065 1.00 24.17 C ANISOU 2120 CD2 LEU B 73 3612 3489 2081 17 -242 -144 C ATOM 2121 N THR B 74 -34.155 134.841 29.526 1.00 25.88 N ANISOU 2121 N THR B 74 3877 3763 2194 -22 -296 -197 N ATOM 2122 CA THR B 74 -34.894 134.855 30.785 1.00 26.85 C ANISOU 2122 CA THR B 74 4003 3943 2255 -27 -284 -200 C ATOM 2123 C THR B 74 -35.979 135.916 30.697 1.00 27.31 C ANISOU 2123 C THR B 74 4063 4001 2311 -2 -238 -236 C ATOM 2124 O THR B 74 -35.722 137.040 30.243 1.00 27.12 O ANISOU 2124 O THR B 74 4051 3931 2321 12 -223 -279 O ATOM 2125 CB THR B 74 -33.965 135.136 31.979 1.00 27.47 C ANISOU 2125 CB THR B 74 4088 4064 2286 -45 -308 -229 C ATOM 2126 OG1 THR B 74 -32.927 134.149 31.994 1.00 27.86 O ANISOU 2126 OG1 THR B 74 4127 4117 2343 -53 -352 -185 O ATOM 2127 CG2 THR B 74 -34.724 135.082 33.309 1.00 28.01 C ANISOU 2127 CG2 THR B 74 4156 4212 2274 -52 -294 -230 C ATOM 2128 N ILE B 75 -37.198 135.524 31.051 1.00 27.90 N ANISOU 2128 N ILE B 75 4123 4125 2352 3 -216 -211 N ATOM 2129 CA ILE B 75 -38.340 136.433 31.117 1.00 28.81 C ANISOU 2129 CA ILE B 75 4230 4260 2458 38 -170 -242 C ATOM 2130 C ILE B 75 -38.777 136.487 32.571 1.00 29.97 C ANISOU 2130 C ILE B 75 4373 4487 2527 33 -153 -264 C ATOM 2131 O ILE B 75 -39.263 135.501 33.102 1.00 30.67 O ANISOU 2131 O ILE B 75 4443 4639 2571 7 -157 -214 O ATOM 2132 CB ILE B 75 -39.538 135.989 30.237 1.00 28.81 C ANISOU 2132 CB ILE B 75 4196 4276 2476 50 -152 -196 C ATOM 2133 CG1 ILE B 75 -39.088 135.613 28.823 1.00 28.45 C ANISOU 2133 CG1 ILE B 75 4148 4172 2488 43 -174 -169 C ATOM 2134 CG2 ILE B 75 -40.578 137.105 30.177 1.00 29.37 C ANISOU 2134 CG2 ILE B 75 4251 4362 2548 105 -106 -227 C ATOM 2135 CD1 ILE B 75 -40.171 135.000 27.949 1.00 28.40 C ANISOU 2135 CD1 ILE B 75 4105 4195 2488 39 -166 -129 C ATOM 2136 N SER B 76 -38.591 137.637 33.205 1.00 31.01 N ANISOU 2136 N SER B 76 4524 4616 2642 52 -132 -340 N ATOM 2137 CA SER B 76 -39.053 137.851 34.574 1.00 32.99 C ANISOU 2137 CA SER B 76 4770 4955 2809 52 -108 -380 C ATOM 2138 C SER B 76 -40.470 138.352 34.514 1.00 33.53 C ANISOU 2138 C SER B 76 4813 5055 2872 103 -53 -395 C ATOM 2139 O SER B 76 -40.892 138.879 33.478 1.00 34.56 O ANISOU 2139 O SER B 76 4939 5124 3070 145 -35 -391 O ATOM 2140 CB SER B 76 -38.175 138.878 35.275 1.00 33.74 C ANISOU 2140 CB SER B 76 4899 5032 2887 45 -110 -473 C ATOM 2141 OG SER B 76 -36.824 138.488 35.174 1.00 34.53 O ANISOU 2141 OG SER B 76 5011 5107 3000 1 -163 -456 O ATOM 2142 N GLY B 77 -41.215 138.163 35.591 1.00 33.92 N ANISOU 2142 N GLY B 77 4838 5212 2839 101 -25 -404 N ATOM 2143 CA GLY B 77 -42.561 138.711 35.698 1.00 34.53 C ANISOU 2143 CA GLY B 77 4880 5339 2900 158 34 -429 C ATOM 2144 C GLY B 77 -43.377 138.474 34.452 1.00 33.84 C ANISOU 2144 C GLY B 77 4757 5227 2875 185 41 -367 C ATOM 2145 O GLY B 77 -43.743 139.426 33.760 1.00 34.30 O ANISOU 2145 O GLY B 77 4814 5228 2990 250 67 -396 O ATOM 2146 N LEU B 78 -43.632 137.200 34.155 1.00 33.36 N ANISOU 2146 N LEU B 78 4667 5205 2804 132 16 -281 N ATOM 2147 CA LEU B 78 -44.401 136.813 32.971 1.00 33.09 C ANISOU 2147 CA LEU B 78 4593 5163 2815 139 15 -224 C ATOM 2148 C LEU B 78 -45.745 137.523 32.925 1.00 33.78 C ANISOU 2148 C LEU B 78 4625 5317 2892 206 69 -242 C ATOM 2149 O LEU B 78 -46.442 137.626 33.937 1.00 33.94 O ANISOU 2149 O LEU B 78 4614 5437 2845 218 108 -264 O ATOM 2150 CB LEU B 78 -44.658 135.297 32.934 1.00 32.95 C ANISOU 2150 CB LEU B 78 4552 5192 2775 61 -10 -142 C ATOM 2151 CG LEU B 78 -43.503 134.403 32.496 1.00 32.27 C ANISOU 2151 CG LEU B 78 4509 5024 2726 8 -65 -106 C ATOM 2152 CD1 LEU B 78 -43.814 132.955 32.838 1.00 32.59 C ANISOU 2152 CD1 LEU B 78 4537 5108 2738 -66 -81 -31 C ATOM 2153 CD2 LEU B 78 -43.241 134.552 30.997 1.00 31.89 C ANISOU 2153 CD2 LEU B 78 4466 4894 2757 25 -84 -103 C ATOM 2154 N GLN B 79 -46.092 138.007 31.741 1.00 33.76 N ANISOU 2154 N GLN B 79 4605 5270 2953 254 71 -228 N ATOM 2155 CA GLN B 79 -47.405 138.576 31.484 1.00 34.87 C ANISOU 2155 CA GLN B 79 4679 5479 3091 326 115 -226 C ATOM 2156 C GLN B 79 -48.055 137.744 30.387 1.00 33.92 C ANISOU 2156 C GLN B 79 4502 5401 2985 291 92 -150 C ATOM 2157 O GLN B 79 -47.353 137.123 29.580 1.00 32.66 O ANISOU 2157 O GLN B 79 4372 5179 2860 237 47 -118 O ATOM 2158 CB GLN B 79 -47.271 140.043 31.086 1.00 36.04 C ANISOU 2158 CB GLN B 79 4856 5537 3300 425 139 -275 C ATOM 2159 CG GLN B 79 -46.460 140.853 32.096 1.00 37.40 C ANISOU 2159 CG GLN B 79 5097 5648 3467 441 156 -365 C ATOM 2160 CD GLN B 79 -46.399 142.335 31.784 1.00 38.83 C ANISOU 2160 CD GLN B 79 5313 5724 3716 535 187 -419 C ATOM 2161 OE1 GLN B 79 -46.996 142.810 30.820 1.00 40.40 O ANISOU 2161 OE1 GLN B 79 5483 5899 3967 603 198 -378 O ATOM 2162 NE2 GLN B 79 -45.678 143.080 32.611 1.00 40.15 N ANISOU 2162 NE2 GLN B 79 5544 5827 3883 539 201 -509 N ATOM 2163 N ALA B 80 -49.386 137.740 30.362 1.00 34.18 N ANISOU 2163 N ALA B 80 4450 5549 2988 320 124 -127 N ATOM 2164 CA ALA B 80 -50.170 136.878 29.456 1.00 34.19 C ANISOU 2164 CA ALA B 80 4382 5623 2986 270 104 -61 C ATOM 2165 C ALA B 80 -49.691 136.946 28.000 1.00 33.11 C ANISOU 2165 C ALA B 80 4264 5407 2910 273 63 -36 C ATOM 2166 O ALA B 80 -49.567 135.920 27.321 1.00 33.73 O ANISOU 2166 O ALA B 80 4337 5488 2991 191 25 -1 O ATOM 2167 CB ALA B 80 -51.651 137.238 29.549 1.00 35.07 C ANISOU 2167 CB ALA B 80 4390 5874 3063 328 148 -48 C ATOM 2168 N GLU B 81 -49.391 138.157 27.542 1.00 32.46 N ANISOU 2168 N GLU B 81 4207 5251 2876 366 73 -56 N ATOM 2169 CA GLU B 81 -48.878 138.395 26.185 1.00 31.77 C ANISOU 2169 CA GLU B 81 4138 5092 2840 377 40 -28 C ATOM 2170 C GLU B 81 -47.466 137.800 25.891 1.00 30.23 C ANISOU 2170 C GLU B 81 4021 4794 2670 301 -2 -37 C ATOM 2171 O GLU B 81 -47.072 137.746 24.730 1.00 30.51 O ANISOU 2171 O GLU B 81 4062 4796 2734 292 -31 -12 O ATOM 2172 CB GLU B 81 -48.952 139.910 25.833 1.00 32.29 C ANISOU 2172 CB GLU B 81 4214 5099 2955 498 67 -35 C ATOM 2173 CG GLU B 81 -47.993 140.840 26.663 1.00 32.39 C ANISOU 2173 CG GLU B 81 4316 4988 3001 533 88 -102 C ATOM 2174 CD GLU B 81 -48.621 141.542 27.880 1.00 33.32 C ANISOU 2174 CD GLU B 81 4425 5138 3098 603 143 -160 C ATOM 2175 OE1 GLU B 81 -49.635 141.061 28.438 1.00 33.68 O ANISOU 2175 OE1 GLU B 81 4399 5311 3086 602 166 -154 O ATOM 2176 OE2 GLU B 81 -48.053 142.578 28.322 1.00 33.70 O ANISOU 2176 OE2 GLU B 81 4538 5081 3184 654 166 -218 O ATOM 2177 N ASP B 82 -46.720 137.350 26.904 1.00 29.14 N ANISOU 2177 N ASP B 82 3935 4621 2517 253 -7 -69 N ATOM 2178 CA ASP B 82 -45.425 136.663 26.683 1.00 28.03 C ANISOU 2178 CA ASP B 82 3855 4399 2397 187 -48 -73 C ATOM 2179 C ASP B 82 -45.566 135.236 26.153 1.00 27.59 C ANISOU 2179 C ASP B 82 3779 4375 2330 102 -80 -37 C ATOM 2180 O ASP B 82 -44.580 134.654 25.700 1.00 27.21 O ANISOU 2180 O ASP B 82 3772 4261 2308 62 -112 -39 O ATOM 2181 CB ASP B 82 -44.576 136.646 27.966 1.00 27.89 C ANISOU 2181 CB ASP B 82 3891 4343 2361 167 -48 -112 C ATOM 2182 CG ASP B 82 -44.304 138.041 28.511 1.00 27.94 C ANISOU 2182 CG ASP B 82 3930 4305 2382 237 -18 -167 C ATOM 2183 OD1 ASP B 82 -44.202 139.001 27.726 1.00 27.73 O ANISOU 2183 OD1 ASP B 82 3913 4219 2404 291 -10 -170 O ATOM 2184 OD2 ASP B 82 -44.177 138.178 29.745 1.00 28.56 O ANISOU 2184 OD2 ASP B 82 4026 4403 2421 233 -2 -207 O ATOM 2185 N GLU B 83 -46.768 134.668 26.222 1.00 28.08 N ANISOU 2185 N GLU B 83 3776 4536 2355 75 -69 -10 N ATOM 2186 CA GLU B 83 -47.045 133.353 25.651 1.00 27.94 C ANISOU 2186 CA GLU B 83 3738 4546 2331 -14 -96 17 C ATOM 2187 C GLU B 83 -46.866 133.382 24.123 1.00 27.52 C ANISOU 2187 C GLU B 83 3675 4476 2307 -12 -121 20 C ATOM 2188 O GLU B 83 -47.600 134.061 23.411 1.00 27.25 O ANISOU 2188 O GLU B 83 3584 4503 2265 36 -112 36 O ATOM 2189 CB GLU B 83 -48.455 132.887 26.033 1.00 29.05 C ANISOU 2189 CB GLU B 83 3802 4810 2425 -50 -75 45 C ATOM 2190 CG GLU B 83 -48.857 131.553 25.408 1.00 29.27 C ANISOU 2190 CG GLU B 83 3806 4864 2450 -155 -101 67 C ATOM 2191 CD GLU B 83 -49.914 130.795 26.192 1.00 30.09 C ANISOU 2191 CD GLU B 83 3858 5065 2509 -226 -83 99 C ATOM 2192 OE1 GLU B 83 -49.916 130.814 27.448 1.00 30.43 O ANISOU 2192 OE1 GLU B 83 3915 5124 2524 -225 -59 109 O ATOM 2193 OE2 GLU B 83 -50.762 130.166 25.546 1.00 30.58 O ANISOU 2193 OE2 GLU B 83 3861 5198 2559 -293 -92 115 O ATOM 2194 N ALA B 84 -45.848 132.670 23.651 1.00 26.82 N ANISOU 2194 N ALA B 84 3637 4308 2246 -57 -152 7 N ATOM 2195 CA ALA B 84 -45.436 132.692 22.247 1.00 26.50 C ANISOU 2195 CA ALA B 84 3595 4248 2224 -57 -174 0 C ATOM 2196 C ALA B 84 -44.354 131.642 22.049 1.00 26.23 C ANISOU 2196 C ALA B 84 3617 4132 2218 -113 -201 -23 C ATOM 2197 O ALA B 84 -43.926 131.000 23.015 1.00 26.15 O ANISOU 2197 O ALA B 84 3647 4074 2216 -142 -204 -24 O ATOM 2198 CB ALA B 84 -44.886 134.064 21.888 1.00 26.07 C ANISOU 2198 CB ALA B 84 3556 4157 2192 27 -164 0 C ATOM 2199 N ASP B 85 -43.899 131.480 20.811 1.00 25.98 N ANISOU 2199 N ASP B 85 3586 4087 2197 -121 -219 -40 N ATOM 2200 CA ASP B 85 -42.708 130.681 20.540 1.00 25.64 C ANISOU 2200 CA ASP B 85 3596 3961 2186 -149 -238 -71 C ATOM 2201 C ASP B 85 -41.501 131.599 20.535 1.00 25.04 C ANISOU 2201 C ASP B 85 3553 3827 2133 -91 -236 -78 C ATOM 2202 O ASP B 85 -41.614 132.778 20.170 1.00 25.23 O ANISOU 2202 O ASP B 85 3558 3875 2152 -41 -224 -62 O ATOM 2203 CB ASP B 85 -42.839 129.913 19.222 1.00 26.33 C ANISOU 2203 CB ASP B 85 3664 4074 2267 -197 -255 -99 C ATOM 2204 CG ASP B 85 -43.859 128.787 19.304 1.00 27.11 C ANISOU 2204 CG ASP B 85 3741 4208 2351 -279 -261 -104 C ATOM 2205 OD1 ASP B 85 -43.970 128.134 20.371 1.00 28.04 O ANISOU 2205 OD1 ASP B 85 3885 4285 2483 -312 -258 -89 O ATOM 2206 OD2 ASP B 85 -44.546 128.544 18.297 1.00 27.51 O ANISOU 2206 OD2 ASP B 85 3746 4333 2374 -317 -270 -120 O ATOM 2207 N TYR B 86 -40.365 131.068 20.971 1.00 24.39 N ANISOU 2207 N TYR B 86 3518 3670 2080 -99 -248 -96 N ATOM 2208 CA TYR B 86 -39.117 131.815 21.052 1.00 24.30 C ANISOU 2208 CA TYR B 86 3533 3610 2090 -58 -249 -105 C ATOM 2209 C TYR B 86 -37.998 131.023 20.400 1.00 24.27 C ANISOU 2209 C TYR B 86 3548 3562 2110 -71 -266 -135 C ATOM 2210 O TYR B 86 -37.843 129.833 20.668 1.00 24.71 O ANISOU 2210 O TYR B 86 3623 3582 2182 -100 -279 -145 O ATOM 2211 CB TYR B 86 -38.753 132.125 22.512 1.00 24.39 C ANISOU 2211 CB TYR B 86 3572 3592 2102 -43 -247 -99 C ATOM 2212 CG TYR B 86 -39.704 133.106 23.153 1.00 24.68 C ANISOU 2212 CG TYR B 86 3592 3669 2115 -16 -222 -85 C ATOM 2213 CD1 TYR B 86 -40.900 132.670 23.721 1.00 25.01 C ANISOU 2213 CD1 TYR B 86 3610 3764 2128 -36 -212 -66 C ATOM 2214 CD2 TYR B 86 -39.411 134.471 23.196 1.00 24.63 C ANISOU 2214 CD2 TYR B 86 3593 3647 2119 30 -207 -92 C ATOM 2215 CE1 TYR B 86 -41.788 133.566 24.292 1.00 25.38 C ANISOU 2215 CE1 TYR B 86 3634 3859 2151 0 -184 -60 C ATOM 2216 CE2 TYR B 86 -40.290 135.374 23.788 1.00 25.03 C ANISOU 2216 CE2 TYR B 86 3631 3725 2154 67 -179 -89 C ATOM 2217 CZ TYR B 86 -41.478 134.913 24.327 1.00 25.25 C ANISOU 2217 CZ TYR B 86 3629 3817 2149 57 -167 -75 C ATOM 2218 OH TYR B 86 -42.360 135.783 24.918 1.00 26.08 O ANISOU 2218 OH TYR B 86 3713 3959 2236 103 -136 -77 O ATOM 2219 N TYR B 87 -37.234 131.695 19.541 1.00 23.81 N ANISOU 2219 N TYR B 87 3483 3507 2058 -48 -263 -145 N ATOM 2220 CA TYR B 87 -36.141 131.084 18.810 1.00 23.70 C ANISOU 2220 CA TYR B 87 3474 3469 2060 -51 -272 -178 C ATOM 2221 C TYR B 87 -34.861 131.832 19.098 1.00 23.68 C ANISOU 2221 C TYR B 87 3481 3439 2077 -24 -272 -177 C ATOM 2222 O TYR B 87 -34.827 133.052 19.013 1.00 23.57 O ANISOU 2222 O TYR B 87 3461 3437 2058 -8 -260 -157 O ATOM 2223 CB TYR B 87 -36.410 131.137 17.307 1.00 23.63 C ANISOU 2223 CB TYR B 87 3434 3518 2027 -60 -266 -192 C ATOM 2224 CG TYR B 87 -37.569 130.284 16.871 1.00 23.64 C ANISOU 2224 CG TYR B 87 3419 3558 2006 -101 -271 -206 C ATOM 2225 CD1 TYR B 87 -37.396 128.931 16.602 1.00 23.92 C ANISOU 2225 CD1 TYR B 87 3472 3562 2056 -135 -280 -255 C ATOM 2226 CD2 TYR B 87 -38.846 130.827 16.725 1.00 23.65 C ANISOU 2226 CD2 TYR B 87 3385 3627 1973 -107 -266 -173 C ATOM 2227 CE1 TYR B 87 -38.460 128.135 16.197 1.00 24.13 C ANISOU 2227 CE1 TYR B 87 3485 3620 2064 -189 -285 -276 C ATOM 2228 CE2 TYR B 87 -39.921 130.037 16.330 1.00 24.04 C ANISOU 2228 CE2 TYR B 87 3409 3727 1997 -156 -273 -188 C ATOM 2229 CZ TYR B 87 -39.725 128.690 16.076 1.00 24.22 C ANISOU 2229 CZ TYR B 87 3454 3714 2035 -205 -283 -242 C ATOM 2230 OH TYR B 87 -40.793 127.911 15.677 1.00 24.66 O ANISOU 2230 OH TYR B 87 3486 3817 2067 -268 -290 -264 O ATOM 2231 N CYS B 88 -33.810 131.105 19.446 1.00 24.38 N ANISOU 2231 N CYS B 88 3584 3490 2190 -18 -286 -197 N ATOM 2232 CA CYS B 88 -32.476 131.698 19.456 1.00 24.97 C ANISOU 2232 CA CYS B 88 3652 3559 2278 -1 -287 -203 C ATOM 2233 C CYS B 88 -31.906 131.582 18.057 1.00 24.69 C ANISOU 2233 C CYS B 88 3589 3554 2237 2 -277 -228 C ATOM 2234 O CYS B 88 -32.402 130.821 17.222 1.00 24.70 O ANISOU 2234 O CYS B 88 3584 3572 2227 -8 -273 -252 O ATOM 2235 CB CYS B 88 -31.562 131.017 20.460 1.00 25.88 C ANISOU 2235 CB CYS B 88 3779 3638 2415 12 -308 -207 C ATOM 2236 SG CYS B 88 -31.327 129.260 20.154 1.00 27.70 S ANISOU 2236 SG CYS B 88 4020 3829 2674 23 -320 -231 S ATOM 2237 N CYS B 89 -30.870 132.361 17.809 1.00 24.34 N ANISOU 2237 N CYS B 89 3526 3525 2197 8 -271 -225 N ATOM 2238 CA CYS B 89 -30.168 132.359 16.538 1.00 24.40 C ANISOU 2238 CA CYS B 89 3501 3578 2192 9 -257 -243 C ATOM 2239 C CYS B 89 -28.726 132.727 16.823 1.00 23.92 C ANISOU 2239 C CYS B 89 3419 3521 2149 15 -259 -247 C ATOM 2240 O CYS B 89 -28.461 133.565 17.684 1.00 23.29 O ANISOU 2240 O CYS B 89 3349 3421 2080 4 -266 -224 O ATOM 2241 CB CYS B 89 -30.773 133.400 15.610 1.00 24.99 C ANISOU 2241 CB CYS B 89 3561 3698 2237 -6 -238 -209 C ATOM 2242 SG CYS B 89 -30.001 133.516 13.991 1.00 26.54 S ANISOU 2242 SG CYS B 89 3710 3975 2397 -13 -216 -220 S ATOM 2243 N SER B 90 -27.798 132.089 16.121 1.00 23.67 N ANISOU 2243 N SER B 90 3356 3521 2118 31 -253 -281 N ATOM 2244 CA SER B 90 -26.396 132.444 16.261 1.00 23.50 C ANISOU 2244 CA SER B 90 3297 3526 2106 34 -253 -283 C ATOM 2245 C SER B 90 -25.705 132.469 14.919 1.00 23.67 C ANISOU 2245 C SER B 90 3270 3621 2103 34 -226 -302 C ATOM 2246 O SER B 90 -26.000 131.666 14.019 1.00 23.60 O ANISOU 2246 O SER B 90 3255 3637 2076 50 -213 -341 O ATOM 2247 CB SER B 90 -25.684 131.482 17.221 1.00 23.66 C ANISOU 2247 CB SER B 90 3315 3516 2158 71 -278 -302 C ATOM 2248 OG SER B 90 -24.289 131.748 17.287 1.00 23.83 O ANISOU 2248 OG SER B 90 3286 3583 2185 78 -280 -306 O ATOM 2249 N TYR B 91 -24.762 133.397 14.802 1.00 23.58 N ANISOU 2249 N TYR B 91 3222 3651 2088 8 -216 -279 N ATOM 2250 CA TYR B 91 -23.767 133.352 13.743 1.00 23.90 C ANISOU 2250 CA TYR B 91 3200 3776 2104 9 -191 -297 C ATOM 2251 C TYR B 91 -23.003 132.049 13.882 1.00 24.19 C ANISOU 2251 C TYR B 91 3210 3820 2160 67 -197 -355 C ATOM 2252 O TYR B 91 -22.695 131.624 14.996 1.00 24.24 O ANISOU 2252 O TYR B 91 3228 3780 2203 94 -225 -357 O ATOM 2253 CB TYR B 91 -22.813 134.533 13.879 1.00 24.03 C ANISOU 2253 CB TYR B 91 3181 3826 2123 -38 -184 -259 C ATOM 2254 CG TYR B 91 -21.874 134.696 12.725 1.00 24.45 C ANISOU 2254 CG TYR B 91 3165 3983 2142 -52 -151 -261 C ATOM 2255 CD1 TYR B 91 -22.370 134.947 11.459 1.00 24.50 C ANISOU 2255 CD1 TYR B 91 3166 4044 2101 -68 -121 -244 C ATOM 2256 CD2 TYR B 91 -20.488 134.629 12.899 1.00 24.82 C ANISOU 2256 CD2 TYR B 91 3145 4090 2197 -52 -149 -277 C ATOM 2257 CE1 TYR B 91 -21.529 135.124 10.385 1.00 25.13 C ANISOU 2257 CE1 TYR B 91 3178 4233 2137 -86 -87 -241 C ATOM 2258 CE2 TYR B 91 -19.625 134.806 11.826 1.00 25.47 C ANISOU 2258 CE2 TYR B 91 3155 4282 2241 -68 -113 -278 C ATOM 2259 CZ TYR B 91 -20.156 135.044 10.566 1.00 25.56 C ANISOU 2259 CZ TYR B 91 3165 4345 2201 -86 -80 -260 C ATOM 2260 OH TYR B 91 -19.349 135.220 9.480 1.00 26.33 O ANISOU 2260 OH TYR B 91 3190 4566 2249 -106 -41 -257 O ATOM 2261 N ALA B 92 -22.727 131.396 12.758 1.00 24.61 N ANISOU 2261 N ALA B 92 3230 3933 2187 93 -170 -403 N ATOM 2262 CA ALA B 92 -22.114 130.072 12.769 1.00 25.05 C ANISOU 2262 CA ALA B 92 3268 3982 2270 162 -170 -468 C ATOM 2263 C ALA B 92 -20.883 129.995 11.872 1.00 25.84 C ANISOU 2263 C ALA B 92 3286 4189 2344 184 -136 -504 C ATOM 2264 O ALA B 92 -20.515 128.919 11.410 1.00 25.97 O ANISOU 2264 O ALA B 92 3283 4215 2368 246 -120 -574 O ATOM 2265 CB ALA B 92 -23.147 129.023 12.364 1.00 25.09 C ANISOU 2265 CB ALA B 92 3324 3933 2276 182 -167 -519 C ATOM 2266 N GLY B 93 -20.233 131.138 11.657 1.00 26.06 N ANISOU 2266 N GLY B 93 3263 4294 2345 133 -124 -457 N ATOM 2267 CA GLY B 93 -19.003 131.201 10.878 1.00 26.81 C ANISOU 2267 CA GLY B 93 3267 4509 2409 143 -89 -478 C ATOM 2268 C GLY B 93 -19.234 131.297 9.386 1.00 27.28 C ANISOU 2268 C GLY B 93 3304 4663 2400 123 -45 -500 C ATOM 2269 O GLY B 93 -20.253 130.820 8.870 1.00 26.86 O ANISOU 2269 O GLY B 93 3298 4581 2325 129 -42 -532 O ATOM 2270 N SER B 94 -18.259 131.905 8.703 1.00 28.17 N ANISOU 2270 N SER B 94 3334 4898 2470 93 -12 -482 N ATOM 2271 CA SER B 94 -18.223 132.034 7.244 1.00 28.93 C ANISOU 2271 CA SER B 94 3387 5120 2484 72 36 -498 C ATOM 2272 C SER B 94 -19.563 132.453 6.655 1.00 28.54 C ANISOU 2272 C SER B 94 3400 5053 2393 28 34 -462 C ATOM 2273 O SER B 94 -20.095 131.793 5.773 1.00 28.15 O ANISOU 2273 O SER B 94 3357 5046 2293 48 51 -521 O ATOM 2274 CB SER B 94 -17.757 130.722 6.597 1.00 29.86 C ANISOU 2274 CB SER B 94 3465 5294 2585 156 65 -612 C ATOM 2275 OG SER B 94 -16.410 130.413 6.941 1.00 31.04 O ANISOU 2275 OG SER B 94 3535 5496 2764 206 75 -638 O ATOM 2276 N TYR B 95 -20.113 133.532 7.205 1.00 28.48 N ANISOU 2276 N TYR B 95 3437 4978 2407 -30 10 -370 N ATOM 2277 CA TYR B 95 -21.338 134.153 6.709 1.00 28.63 C ANISOU 2277 CA TYR B 95 3504 4985 2389 -70 7 -312 C ATOM 2278 C TYR B 95 -22.550 133.208 6.701 1.00 27.95 C ANISOU 2278 C TYR B 95 3475 4843 2303 -32 -13 -370 C ATOM 2279 O TYR B 95 -23.266 133.107 5.706 1.00 28.52 O ANISOU 2279 O TYR B 95 3547 4983 2308 -44 -1 -377 O ATOM 2280 CB TYR B 95 -21.090 134.759 5.327 1.00 30.09 C ANISOU 2280 CB TYR B 95 3633 5315 2485 -113 48 -269 C ATOM 2281 CG TYR B 95 -19.897 135.687 5.277 1.00 31.52 C ANISOU 2281 CG TYR B 95 3753 5558 2665 -165 72 -206 C ATOM 2282 CD1 TYR B 95 -20.027 137.031 5.599 1.00 32.25 C ANISOU 2282 CD1 TYR B 95 3873 5597 2784 -233 65 -96 C ATOM 2283 CD2 TYR B 95 -18.637 135.221 4.907 1.00 32.85 C ANISOU 2283 CD2 TYR B 95 3835 5837 2809 -148 104 -260 C ATOM 2284 CE1 TYR B 95 -18.936 137.890 5.555 1.00 33.39 C ANISOU 2284 CE1 TYR B 95 3963 5791 2932 -296 86 -39 C ATOM 2285 CE2 TYR B 95 -17.547 136.070 4.854 1.00 34.03 C ANISOU 2285 CE2 TYR B 95 3920 6055 2955 -207 126 -200 C ATOM 2286 CZ TYR B 95 -17.708 137.407 5.184 1.00 34.41 C ANISOU 2286 CZ TYR B 95 4000 6042 3031 -289 116 -89 C ATOM 2287 OH TYR B 95 -16.641 138.268 5.145 1.00 36.21 O ANISOU 2287 OH TYR B 95 4168 6331 3261 -364 137 -30 O ATOM 2288 N THR B 95A -22.758 132.519 7.822 1.00 27.16 N ANISOU 2288 N THR B 95A 3420 4626 2273 6 -45 -408 N ATOM 2289 CA THR B 95A -23.930 131.661 8.016 1.00 26.54 C ANISOU 2289 CA THR B 95A 3401 4476 2207 28 -67 -453 C ATOM 2290 C THR B 95A -24.554 131.877 9.389 1.00 25.45 C ANISOU 2290 C THR B 95A 3324 4210 2134 26 -105 -411 C ATOM 2291 O THR B 95A -23.882 132.293 10.336 1.00 25.22 O ANISOU 2291 O THR B 95A 3293 4139 2151 27 -118 -381 O ATOM 2292 CB THR B 95A -23.593 130.161 7.841 1.00 26.99 C ANISOU 2292 CB THR B 95A 3454 4523 2278 86 -59 -567 C ATOM 2293 OG1 THR B 95A -22.748 129.713 8.906 1.00 26.87 O ANISOU 2293 OG1 THR B 95A 3437 4435 2335 133 -74 -580 O ATOM 2294 CG2 THR B 95A -22.887 129.902 6.504 1.00 27.90 C ANISOU 2294 CG2 THR B 95A 3503 4775 2324 95 -14 -626 C ATOM 2295 N TYR B 96 -25.854 131.599 9.470 1.00 25.09 N ANISOU 2295 N TYR B 96 3326 4120 2085 19 -122 -412 N ATOM 2296 CA TYR B 96 -26.622 131.606 10.712 1.00 24.23 C ANISOU 2296 CA TYR B 96 3274 3903 2029 20 -154 -384 C ATOM 2297 C TYR B 96 -27.350 130.280 10.874 1.00 24.38 C ANISOU 2297 C TYR B 96 3330 3869 2065 39 -167 -449 C ATOM 2298 O TYR B 96 -27.706 129.636 9.889 1.00 24.78 O ANISOU 2298 O TYR B 96 3371 3969 2076 34 -154 -506 O ATOM 2299 CB TYR B 96 -27.640 132.752 10.711 1.00 23.78 C ANISOU 2299 CB TYR B 96 3237 3847 1953 -14 -159 -306 C ATOM 2300 CG TYR B 96 -26.965 134.063 10.931 1.00 23.62 C ANISOU 2300 CG TYR B 96 3203 3828 1943 -36 -150 -238 C ATOM 2301 CD1 TYR B 96 -26.410 134.759 9.868 1.00 24.01 C ANISOU 2301 CD1 TYR B 96 3208 3965 1948 -61 -123 -204 C ATOM 2302 CD2 TYR B 96 -26.792 134.572 12.223 1.00 23.08 C ANISOU 2302 CD2 TYR B 96 3164 3677 1928 -39 -168 -213 C ATOM 2303 CE1 TYR B 96 -25.735 135.952 10.064 1.00 24.07 C ANISOU 2303 CE1 TYR B 96 3206 3966 1974 -94 -114 -140 C ATOM 2304 CE2 TYR B 96 -26.112 135.763 12.429 1.00 23.06 C ANISOU 2304 CE2 TYR B 96 3152 3669 1940 -71 -160 -164 C ATOM 2305 CZ TYR B 96 -25.581 136.448 11.343 1.00 23.63 C ANISOU 2305 CZ TYR B 96 3184 3816 1977 -101 -132 -126 C ATOM 2306 OH TYR B 96 -24.902 137.637 11.524 1.00 23.80 O ANISOU 2306 OH TYR B 96 3199 3823 2019 -145 -122 -73 O ATOM 2307 N VAL B 97 -27.576 129.903 12.125 1.00 24.25 N ANISOU 2307 N VAL B 97 3354 3756 2104 53 -193 -440 N ATOM 2308 CA VAL B 97 -28.349 128.719 12.476 1.00 24.51 C ANISOU 2308 CA VAL B 97 3430 3719 2163 59 -207 -481 C ATOM 2309 C VAL B 97 -29.341 129.123 13.554 1.00 24.04 C ANISOU 2309 C VAL B 97 3409 3604 2121 37 -230 -422 C ATOM 2310 O VAL B 97 -28.976 129.805 14.519 1.00 23.64 O ANISOU 2310 O VAL B 97 3363 3526 2092 44 -241 -374 O ATOM 2311 CB VAL B 97 -27.437 127.585 12.977 1.00 25.03 C ANISOU 2311 CB VAL B 97 3505 3721 2285 110 -212 -529 C ATOM 2312 CG1 VAL B 97 -28.256 126.386 13.434 1.00 25.35 C ANISOU 2312 CG1 VAL B 97 3601 3668 2364 108 -227 -558 C ATOM 2313 CG2 VAL B 97 -26.449 127.170 11.889 1.00 25.70 C ANISOU 2313 CG2 VAL B 97 3545 3868 2351 142 -183 -598 C ATOM 2314 N PHE B 98 -30.599 128.715 13.384 1.00 24.33 N ANISOU 2314 N PHE B 98 3468 3634 2143 8 -235 -431 N ATOM 2315 CA PHE B 98 -31.653 129.018 14.357 1.00 23.94 C ANISOU 2315 CA PHE B 98 3446 3547 2103 -12 -252 -380 C ATOM 2316 C PHE B 98 -31.828 127.841 15.287 1.00 24.05 C ANISOU 2316 C PHE B 98 3501 3473 2164 -9 -268 -396 C ATOM 2317 O PHE B 98 -31.556 126.696 14.914 1.00 24.77 O ANISOU 2317 O PHE B 98 3606 3529 2278 -2 -266 -454 O ATOM 2318 CB PHE B 98 -32.985 129.314 13.664 1.00 23.94 C ANISOU 2318 CB PHE B 98 3433 3608 2055 -48 -249 -368 C ATOM 2319 CG PHE B 98 -33.079 130.698 13.088 1.00 23.84 C ANISOU 2319 CG PHE B 98 3389 3666 2002 -46 -238 -314 C ATOM 2320 CD1 PHE B 98 -33.547 131.754 13.857 1.00 23.35 C ANISOU 2320 CD1 PHE B 98 3336 3586 1950 -38 -240 -249 C ATOM 2321 CD2 PHE B 98 -32.730 130.942 11.758 1.00 24.09 C ANISOU 2321 CD2 PHE B 98 3383 3783 1986 -51 -222 -327 C ATOM 2322 CE1 PHE B 98 -33.646 133.029 13.328 1.00 23.56 C ANISOU 2322 CE1 PHE B 98 3341 3658 1952 -32 -228 -193 C ATOM 2323 CE2 PHE B 98 -32.817 132.217 11.225 1.00 24.10 C ANISOU 2323 CE2 PHE B 98 3359 3844 1954 -50 -212 -260 C ATOM 2324 CZ PHE B 98 -33.270 133.266 12.011 1.00 24.00 C ANISOU 2324 CZ PHE B 98 3362 3792 1965 -38 -215 -191 C ATOM 2325 N GLY B 99 -32.316 128.113 16.492 1.00 23.43 N ANISOU 2325 N GLY B 99 3445 3358 2099 -15 -281 -345 N ATOM 2326 CA GLY B 99 -32.683 127.041 17.410 1.00 23.65 C ANISOU 2326 CA GLY B 99 3511 3311 2163 -23 -296 -340 C ATOM 2327 C GLY B 99 -34.000 126.376 17.045 1.00 23.74 C ANISOU 2327 C GLY B 99 3535 3324 2162 -75 -295 -357 C ATOM 2328 O GLY B 99 -34.747 126.876 16.199 1.00 23.68 O ANISOU 2328 O GLY B 99 3498 3389 2110 -102 -287 -365 O ATOM 2329 N THR B 100 -34.286 125.252 17.691 1.00 24.45 N ANISOU 2329 N THR B 100 3663 3336 2291 -93 -305 -357 N ATOM 2330 CA THR B 100 -35.472 124.425 17.374 1.00 24.96 C ANISOU 2330 CA THR B 100 3741 3391 2353 -158 -305 -380 C ATOM 2331 C THR B 100 -36.790 125.014 17.881 1.00 24.73 C ANISOU 2331 C THR B 100 3692 3419 2285 -201 -305 -328 C ATOM 2332 O THR B 100 -37.859 124.586 17.459 1.00 25.29 O ANISOU 2332 O THR B 100 3753 3519 2338 -262 -305 -345 O ATOM 2333 CB THR B 100 -35.343 123.006 17.969 1.00 25.69 C ANISOU 2333 CB THR B 100 3888 3365 2510 -170 -313 -386 C ATOM 2334 OG1 THR B 100 -35.079 123.104 19.376 1.00 25.77 O ANISOU 2334 OG1 THR B 100 3916 3337 2537 -145 -325 -309 O ATOM 2335 CG2 THR B 100 -34.223 122.229 17.272 1.00 26.41 C ANISOU 2335 CG2 THR B 100 3997 3394 2645 -125 -307 -456 C ATOM 2336 N GLY B 101 -36.719 125.981 18.790 1.00 24.38 N ANISOU 2336 N GLY B 101 3639 3398 2226 -171 -306 -269 N ATOM 2337 CA GLY B 101 -37.906 126.712 19.248 1.00 24.42 C ANISOU 2337 CA GLY B 101 3618 3469 2192 -193 -300 -225 C ATOM 2338 C GLY B 101 -38.456 126.201 20.564 1.00 25.00 C ANISOU 2338 C GLY B 101 3714 3511 2275 -220 -304 -179 C ATOM 2339 O GLY B 101 -38.457 125.003 20.817 1.00 25.64 O ANISOU 2339 O GLY B 101 3828 3524 2389 -254 -311 -181 O ATOM 2340 N THR B 102 -38.926 127.123 21.402 1.00 25.22 N ANISOU 2340 N THR B 102 3724 3588 2271 -204 -295 -136 N ATOM 2341 CA THR B 102 -39.538 126.793 22.688 1.00 25.65 C ANISOU 2341 CA THR B 102 3789 3642 2316 -230 -293 -88 C ATOM 2342 C THR B 102 -40.875 127.491 22.780 1.00 26.35 C ANISOU 2342 C THR B 102 3830 3824 2357 -246 -275 -70 C ATOM 2343 O THR B 102 -40.970 128.703 22.527 1.00 25.84 O ANISOU 2343 O THR B 102 3738 3809 2272 -200 -263 -74 O ATOM 2344 CB THR B 102 -38.644 127.265 23.849 1.00 25.36 C ANISOU 2344 CB THR B 102 3774 3584 2277 -185 -299 -61 C ATOM 2345 OG1 THR B 102 -37.348 126.673 23.713 1.00 25.10 O ANISOU 2345 OG1 THR B 102 3772 3478 2286 -159 -318 -75 O ATOM 2346 CG2 THR B 102 -39.235 126.880 25.212 1.00 25.60 C ANISOU 2346 CG2 THR B 102 3813 3629 2283 -213 -296 -7 C ATOM 2347 N LYS B 103 -41.904 126.733 23.148 1.00 27.48 N ANISOU 2347 N LYS B 103 3961 3990 2489 -309 -270 -45 N ATOM 2348 CA LYS B 103 -43.206 127.303 23.471 1.00 28.66 C ANISOU 2348 CA LYS B 103 4057 4242 2592 -322 -250 -20 C ATOM 2349 C LYS B 103 -43.165 127.771 24.925 1.00 28.42 C ANISOU 2349 C LYS B 103 4035 4227 2536 -294 -236 17 C ATOM 2350 O LYS B 103 -42.928 126.970 25.828 1.00 28.66 O ANISOU 2350 O LYS B 103 4099 4219 2572 -326 -243 51 O ATOM 2351 CB LYS B 103 -44.313 126.254 23.286 1.00 30.02 C ANISOU 2351 CB LYS B 103 4206 4445 2758 -415 -250 -10 C ATOM 2352 CG LYS B 103 -45.740 126.694 23.692 1.00 31.26 C ANISOU 2352 CG LYS B 103 4292 4725 2862 -436 -227 22 C ATOM 2353 CD LYS B 103 -46.481 127.506 22.647 1.00 32.22 C ANISOU 2353 CD LYS B 103 4343 4946 2954 -410 -223 2 C ATOM 2354 CE LYS B 103 -47.807 128.042 23.188 1.00 33.34 C ANISOU 2354 CE LYS B 103 4407 5214 3045 -407 -197 37 C ATOM 2355 NZ LYS B 103 -48.856 126.992 23.335 1.00 34.41 N ANISOU 2355 NZ LYS B 103 4504 5407 3163 -517 -196 56 N ATOM 2356 N VAL B 104 -43.397 129.063 25.150 1.00 28.46 N ANISOU 2356 N VAL B 104 4013 4290 2513 -233 -217 11 N ATOM 2357 CA VAL B 104 -43.583 129.589 26.506 1.00 28.83 C ANISOU 2357 CA VAL B 104 4057 4375 2521 -209 -197 31 C ATOM 2358 C VAL B 104 -45.076 129.639 26.764 1.00 29.29 C ANISOU 2358 C VAL B 104 4053 4539 2536 -234 -170 54 C ATOM 2359 O VAL B 104 -45.802 130.287 26.012 1.00 29.25 O ANISOU 2359 O VAL B 104 3998 4593 2525 -206 -157 42 O ATOM 2360 CB VAL B 104 -42.965 130.989 26.670 1.00 28.87 C ANISOU 2360 CB VAL B 104 4073 4370 2525 -130 -187 -1 C ATOM 2361 CG1 VAL B 104 -43.362 131.630 28.001 1.00 29.37 C ANISOU 2361 CG1 VAL B 104 4128 4491 2541 -105 -159 1 C ATOM 2362 CG2 VAL B 104 -41.455 130.896 26.560 1.00 28.53 C ANISOU 2362 CG2 VAL B 104 4081 4239 2518 -116 -214 -19 C ATOM 2363 N THR B 105 -45.527 128.960 27.817 1.00 29.73 N ANISOU 2363 N THR B 105 4107 4630 2561 -285 -160 93 N ATOM 2364 CA THR B 105 -46.922 128.997 28.237 1.00 30.63 C ANISOU 2364 CA THR B 105 4152 4861 2625 -312 -129 118 C ATOM 2365 C THR B 105 -47.047 129.804 29.529 1.00 30.74 C ANISOU 2365 C THR B 105 4157 4938 2585 -262 -97 118 C ATOM 2366 O THR B 105 -46.367 129.523 30.527 1.00 30.80 O ANISOU 2366 O THR B 105 4209 4918 2574 -272 -103 134 O ATOM 2367 CB THR B 105 -47.482 127.573 28.414 1.00 31.44 C ANISOU 2367 CB THR B 105 4250 4970 2726 -423 -136 167 C ATOM 2368 OG1 THR B 105 -47.519 126.924 27.127 1.00 31.94 O ANISOU 2368 OG1 THR B 105 4314 4986 2834 -470 -161 147 O ATOM 2369 CG2 THR B 105 -48.903 127.595 28.984 1.00 32.27 C ANISOU 2369 CG2 THR B 105 4275 5215 2770 -461 -100 200 C ATOM 2370 N VAL B 106 -47.902 130.825 29.499 1.00 31.09 N ANISOU 2370 N VAL B 106 4142 5070 2601 -203 -63 96 N ATOM 2371 CA VAL B 106 -48.259 131.566 30.707 1.00 31.58 C ANISOU 2371 CA VAL B 106 4184 5209 2605 -157 -22 82 C ATOM 2372 C VAL B 106 -49.463 130.834 31.293 1.00 32.84 C ANISOU 2372 C VAL B 106 4278 5490 2708 -226 3 132 C ATOM 2373 O VAL B 106 -50.566 130.897 30.740 1.00 32.47 O ANISOU 2373 O VAL B 106 4154 5530 2653 -231 20 141 O ATOM 2374 CB VAL B 106 -48.557 133.042 30.417 1.00 31.65 C ANISOU 2374 CB VAL B 106 4166 5239 2621 -49 7 31 C ATOM 2375 CG1 VAL B 106 -49.020 133.762 31.685 1.00 32.48 C ANISOU 2375 CG1 VAL B 106 4248 5429 2664 0 55 2 C ATOM 2376 CG2 VAL B 106 -47.315 133.724 29.858 1.00 31.04 C ANISOU 2376 CG2 VAL B 106 4156 5037 2601 2 -18 -9 C ATOM 2377 N LEU B 107 -49.227 130.135 32.403 1.00 33.73 N ANISOU 2377 N LEU B 107 4418 5618 2781 -283 5 170 N ATOM 2378 CA LEU B 107 -50.180 129.168 32.955 1.00 35.66 C ANISOU 2378 CA LEU B 107 4615 5958 2978 -378 22 237 C ATOM 2379 C LEU B 107 -51.488 129.829 33.369 1.00 37.36 C ANISOU 2379 C LEU B 107 4731 6336 3127 -346 78 227 C ATOM 2380 O LEU B 107 -51.481 130.733 34.209 1.00 37.54 O ANISOU 2380 O LEU B 107 4747 6417 3101 -272 113 187 O ATOM 2381 CB LEU B 107 -49.585 128.446 34.167 1.00 35.80 C ANISOU 2381 CB LEU B 107 4682 5963 2955 -429 15 290 C ATOM 2382 CG LEU B 107 -48.331 127.593 33.952 1.00 35.26 C ANISOU 2382 CG LEU B 107 4705 5745 2948 -462 -38 319 C ATOM 2383 CD1 LEU B 107 -47.834 127.096 35.303 1.00 35.66 C ANISOU 2383 CD1 LEU B 107 4792 5817 2943 -492 -41 379 C ATOM 2384 CD2 LEU B 107 -48.575 126.430 32.999 1.00 35.41 C ANISOU 2384 CD2 LEU B 107 4732 5690 3031 -549 -63 356 C ATOM 2385 N GLY B 108 -52.587 129.389 32.746 1.00 40.74 N ANISOU 2385 N GLY B 108 7159 5032 3289 -988 634 -150 N ATOM 2386 CA GLY B 108 -53.945 129.805 33.116 1.00 43.00 C ANISOU 2386 CA GLY B 108 7413 5275 3649 -948 840 -311 C ATOM 2387 C GLY B 108 -54.875 128.654 33.492 1.00 44.93 C ANISOU 2387 C GLY B 108 7589 5557 3924 -1015 1013 -397 C ATOM 2388 O GLY B 108 -56.043 128.888 33.774 1.00 46.48 O ANISOU 2388 O GLY B 108 7699 5737 4224 -1003 1219 -589 O ATOM 2389 N GLN B 109 -54.367 127.419 33.481 1.00 45.29 N ANISOU 2389 N GLN B 109 7671 5644 3894 -1091 935 -284 N ATOM 2390 CA GLN B 109 -55.092 126.237 33.942 1.00 47.17 C ANISOU 2390 CA GLN B 109 7939 5884 4099 -1211 1104 -343 C ATOM 2391 C GLN B 109 -54.091 125.354 34.669 1.00 47.81 C ANISOU 2391 C GLN B 109 8315 5905 3947 -1345 968 -197 C ATOM 2392 O GLN B 109 -52.884 125.523 34.468 1.00 46.76 O ANISOU 2392 O GLN B 109 8217 5779 3773 -1290 711 -75 O ATOM 2393 CB GLN B 109 -55.614 125.412 32.770 1.00 47.21 C ANISOU 2393 CB GLN B 109 7655 5985 4298 -1101 1075 -355 C ATOM 2394 CG GLN B 109 -56.469 126.131 31.746 1.00 47.59 C ANISOU 2394 CG GLN B 109 7405 6081 4598 -903 1078 -483 C ATOM 2395 CD GLN B 109 -56.514 125.382 30.424 1.00 47.03 C ANISOU 2395 CD GLN B 109 7110 6094 4665 -776 933 -427 C ATOM 2396 OE1 GLN B 109 -56.431 125.988 29.359 1.00 47.09 O ANISOU 2396 OE1 GLN B 109 7004 6113 4776 -603 774 -403 O ATOM 2397 NE2 GLN B 109 -56.624 124.057 30.489 1.00 47.07 N ANISOU 2397 NE2 GLN B 109 7103 6135 4646 -876 985 -401 N ATOM 2398 N PRO B 110 -54.576 124.379 35.472 1.00 49.54 N ANISOU 2398 N PRO B 110 8754 6051 4018 -1523 1125 -230 N ATOM 2399 CA PRO B 110 -53.665 123.347 35.972 1.00 49.94 C ANISOU 2399 CA PRO B 110 9108 6010 3855 -1602 917 -85 C ATOM 2400 C PRO B 110 -53.185 122.455 34.837 1.00 48.21 C ANISOU 2400 C PRO B 110 8655 5880 3783 -1459 698 12 C ATOM 2401 O PRO B 110 -53.901 122.288 33.843 1.00 47.15 O ANISOU 2401 O PRO B 110 8201 5854 3859 -1374 799 -42 O ATOM 2402 CB PRO B 110 -54.533 122.540 36.954 1.00 52.56 C ANISOU 2402 CB PRO B 110 9767 6217 3988 -1850 1195 -163 C ATOM 2403 CG PRO B 110 -55.685 123.425 37.286 1.00 53.90 C ANISOU 2403 CG PRO B 110 9830 6410 4241 -1933 1565 -376 C ATOM 2404 CD PRO B 110 -55.925 124.242 36.051 1.00 51.85 C ANISOU 2404 CD PRO B 110 9077 6311 4314 -1682 1502 -429 C ATOM 2405 N LYS B 111 -51.994 121.880 34.978 1.00 48.12 N ANISOU 2405 N LYS B 111 8794 5816 3673 -1422 386 128 N ATOM 2406 CA LYS B 111 -51.483 121.009 33.933 1.00 47.05 C ANISOU 2406 CA LYS B 111 8433 5758 3685 -1290 187 190 C ATOM 2407 C LYS B 111 -52.348 119.752 33.815 1.00 46.68 C ANISOU 2407 C LYS B 111 8440 5677 3620 -1365 328 183 C ATOM 2408 O LYS B 111 -52.933 119.290 34.798 1.00 47.54 O ANISOU 2408 O LYS B 111 8895 5646 3522 -1552 493 159 O ATOM 2409 CB LYS B 111 -49.995 120.689 34.123 1.00 48.35 C ANISOU 2409 CB LYS B 111 8696 5873 3802 -1213 -195 253 C ATOM 2410 CG LYS B 111 -49.615 119.694 35.206 1.00 51.57 C ANISOU 2410 CG LYS B 111 9556 6076 3961 -1285 -391 301 C ATOM 2411 CD LYS B 111 -48.298 119.027 34.826 1.00 52.23 C ANISOU 2411 CD LYS B 111 9547 6154 4143 -1119 -807 313 C ATOM 2412 CE LYS B 111 -47.691 118.232 35.968 1.00 55.24 C ANISOU 2412 CE LYS B 111 10423 6291 4276 -1134 -1131 346 C ATOM 2413 NZ LYS B 111 -46.228 118.063 35.749 1.00 56.11 N ANISOU 2413 NZ LYS B 111 10368 6410 4539 -939 -1584 279 N ATOM 2414 N ALA B 112 -52.458 119.240 32.595 1.00 44.27 N ANISOU 2414 N ALA B 112 7813 5490 3519 -1246 291 191 N ATOM 2415 CA ALA B 112 -53.231 118.031 32.321 1.00 44.29 C ANISOU 2415 CA ALA B 112 7818 5474 3537 -1309 410 175 C ATOM 2416 C ALA B 112 -52.364 117.070 31.525 1.00 43.34 C ANISOU 2416 C ALA B 112 7595 5375 3495 -1174 129 257 C ATOM 2417 O ALA B 112 -51.718 117.474 30.558 1.00 41.34 O ANISOU 2417 O ALA B 112 7044 5248 3415 -1020 -11 266 O ATOM 2418 CB ALA B 112 -54.492 118.382 31.555 1.00 43.62 C ANISOU 2418 CB ALA B 112 7397 5517 3660 -1292 675 48 C ATOM 2419 N ASN B 113 -52.349 115.806 31.939 1.00 44.89 N ANISOU 2419 N ASN B 113 8069 5432 3555 -1248 63 299 N ATOM 2420 CA ASN B 113 -51.541 114.787 31.289 1.00 44.68 C ANISOU 2420 CA ASN B 113 7977 5395 3603 -1113 -218 353 C ATOM 2421 C ASN B 113 -52.240 114.319 30.010 1.00 43.06 C ANISOU 2421 C ASN B 113 7418 5334 3609 -1062 -81 317 C ATOM 2422 O ASN B 113 -53.471 114.267 29.962 1.00 43.35 O ANISOU 2422 O ASN B 113 7407 5398 3666 -1180 210 249 O ATOM 2423 CB ASN B 113 -51.288 113.597 32.221 1.00 47.05 C ANISOU 2423 CB ASN B 113 8774 5445 3657 -1195 -380 413 C ATOM 2424 CG ASN B 113 -50.706 113.995 33.577 1.00 49.40 C ANISOU 2424 CG ASN B 113 9517 5558 3696 -1258 -539 445 C ATOM 2425 OD1 ASN B 113 -50.052 115.028 33.726 1.00 49.63 O ANISOU 2425 OD1 ASN B 113 9423 5659 3776 -1181 -648 425 O ATOM 2426 ND2 ASN B 113 -50.938 113.150 34.576 1.00 52.07 N ANISOU 2426 ND2 ASN B 113 10421 5632 3731 -1416 -558 492 N ATOM 2427 N PRO B 114 -51.460 113.976 28.968 1.00 41.81 N ANISOU 2427 N PRO B 114 7002 5267 3618 -894 -287 330 N ATOM 2428 CA PRO B 114 -52.103 113.565 27.723 1.00 40.47 C ANISOU 2428 CA PRO B 114 6528 5223 3625 -846 -175 296 C ATOM 2429 C PRO B 114 -52.696 112.156 27.802 1.00 41.51 C ANISOU 2429 C PRO B 114 6824 5250 3698 -932 -125 303 C ATOM 2430 O PRO B 114 -52.086 111.264 28.392 1.00 42.44 O ANISOU 2430 O PRO B 114 7242 5201 3683 -938 -318 356 O ATOM 2431 CB PRO B 114 -50.957 113.611 26.708 1.00 39.16 C ANISOU 2431 CB PRO B 114 6105 5159 3616 -679 -392 293 C ATOM 2432 CG PRO B 114 -49.719 113.388 27.508 1.00 40.64 C ANISOU 2432 CG PRO B 114 6483 5232 3725 -633 -671 304 C ATOM 2433 CD PRO B 114 -49.995 113.791 28.926 1.00 41.75 C ANISOU 2433 CD PRO B 114 6984 5233 3647 -755 -629 340 C ATOM 2434 N THR B 115 -53.885 111.978 27.225 1.00 41.27 N ANISOU 2434 N THR B 115 6615 5300 3767 -996 112 232 N ATOM 2435 CA THR B 115 -54.402 110.647 26.908 1.00 41.87 C ANISOU 2435 CA THR B 115 6743 5319 3849 -1063 161 217 C ATOM 2436 C THR B 115 -53.861 110.300 25.524 1.00 39.80 C ANISOU 2436 C THR B 115 6174 5177 3772 -875 -14 228 C ATOM 2437 O THR B 115 -54.091 111.055 24.573 1.00 39.01 O ANISOU 2437 O THR B 115 5758 5238 3828 -782 28 184 O ATOM 2438 CB THR B 115 -55.944 110.620 26.869 1.00 43.05 C ANISOU 2438 CB THR B 115 6781 5514 4063 -1226 500 79 C ATOM 2439 OG1 THR B 115 -56.469 111.139 28.091 1.00 45.57 O ANISOU 2439 OG1 THR B 115 7335 5746 4233 -1417 720 24 O ATOM 2440 CG2 THR B 115 -56.465 109.204 26.664 1.00 44.38 C ANISOU 2440 CG2 THR B 115 7047 5600 4215 -1344 574 51 C ATOM 2441 N VAL B 116 -53.137 109.181 25.418 1.00 39.25 N ANISOU 2441 N VAL B 116 6232 5007 3672 -820 -217 275 N ATOM 2442 CA VAL B 116 -52.539 108.733 24.157 1.00 37.81 C ANISOU 2442 CA VAL B 116 5784 4924 3660 -659 -367 260 C ATOM 2443 C VAL B 116 -53.254 107.478 23.652 1.00 37.79 C ANISOU 2443 C VAL B 116 5795 4880 3686 -715 -298 236 C ATOM 2444 O VAL B 116 -53.348 106.481 24.371 1.00 39.51 O ANISOU 2444 O VAL B 116 6341 4907 3763 -810 -327 267 O ATOM 2445 CB VAL B 116 -51.032 108.412 24.310 1.00 38.12 C ANISOU 2445 CB VAL B 116 5886 4890 3706 -515 -685 273 C ATOM 2446 CG1 VAL B 116 -50.395 108.114 22.951 1.00 37.32 C ANISOU 2446 CG1 VAL B 116 5462 4915 3802 -375 -777 208 C ATOM 2447 CG2 VAL B 116 -50.304 109.558 24.998 1.00 37.97 C ANISOU 2447 CG2 VAL B 116 5896 4885 3647 -490 -765 277 C ATOM 2448 N THR B 117 -53.759 107.545 22.422 1.00 36.26 N ANISOU 2448 N THR B 117 5285 4841 3652 -665 -216 179 N ATOM 2449 CA THR B 117 -54.314 106.380 21.722 1.00 36.30 C ANISOU 2449 CA THR B 117 5243 4832 3717 -694 -180 140 C ATOM 2450 C THR B 117 -53.487 106.166 20.464 1.00 34.79 C ANISOU 2450 C THR B 117 4826 4736 3656 -524 -342 127 C ATOM 2451 O THR B 117 -53.288 107.102 19.679 1.00 33.59 O ANISOU 2451 O THR B 117 4452 4727 3584 -444 -337 105 O ATOM 2452 CB THR B 117 -55.782 106.596 21.315 1.00 36.50 C ANISOU 2452 CB THR B 117 5082 4954 3831 -793 57 37 C ATOM 2453 OG1 THR B 117 -56.518 107.108 22.422 1.00 38.01 O ANISOU 2453 OG1 THR B 117 5406 5097 3940 -954 255 -5 O ATOM 2454 CG2 THR B 117 -56.431 105.288 20.842 1.00 37.19 C ANISOU 2454 CG2 THR B 117 5173 4997 3961 -875 115 -21 C ATOM 2455 N LEU B 118 -53.020 104.935 20.278 1.00 35.09 N ANISOU 2455 N LEU B 118 4959 4674 3700 -484 -474 128 N ATOM 2456 CA LEU B 118 -52.275 104.545 19.085 1.00 34.23 C ANISOU 2456 CA LEU B 118 4641 4642 3721 -347 -594 77 C ATOM 2457 C LEU B 118 -53.140 103.584 18.282 1.00 34.38 C ANISOU 2457 C LEU B 118 4607 4668 3789 -395 -511 39 C ATOM 2458 O LEU B 118 -53.552 102.541 18.796 1.00 35.68 O ANISOU 2458 O LEU B 118 4989 4680 3885 -481 -503 52 O ATOM 2459 CB LEU B 118 -50.964 103.874 19.481 1.00 35.13 C ANISOU 2459 CB LEU B 118 4871 4629 3847 -227 -849 61 C ATOM 2460 CG LEU B 118 -50.086 103.267 18.384 1.00 34.86 C ANISOU 2460 CG LEU B 118 4628 4645 3970 -91 -968 -45 C ATOM 2461 CD1 LEU B 118 -49.718 104.298 17.326 1.00 33.57 C ANISOU 2461 CD1 LEU B 118 4163 4689 3903 -72 -862 -113 C ATOM 2462 CD2 LEU B 118 -48.838 102.670 19.015 1.00 36.42 C ANISOU 2462 CD2 LEU B 118 4933 4693 4213 53 -1264 -108 C ATOM 2463 N PHE B 119 -53.425 103.953 17.037 1.00 33.10 N ANISOU 2463 N PHE B 119 4195 4660 3722 -353 -453 -13 N ATOM 2464 CA PHE B 119 -54.207 103.121 16.128 1.00 33.37 C ANISOU 2464 CA PHE B 119 4147 4716 3815 -382 -403 -70 C ATOM 2465 C PHE B 119 -53.257 102.429 15.150 1.00 33.52 C ANISOU 2465 C PHE B 119 4088 4745 3902 -273 -523 -115 C ATOM 2466 O PHE B 119 -52.390 103.084 14.573 1.00 33.12 O ANISOU 2466 O PHE B 119 3916 4781 3885 -196 -559 -144 O ATOM 2467 CB PHE B 119 -55.186 103.968 15.329 1.00 32.46 C ANISOU 2467 CB PHE B 119 3841 4739 3752 -389 -309 -122 C ATOM 2468 CG PHE B 119 -56.266 104.594 16.153 1.00 32.73 C ANISOU 2468 CG PHE B 119 3881 4778 3779 -486 -176 -146 C ATOM 2469 CD1 PHE B 119 -57.416 103.879 16.467 1.00 33.82 C ANISOU 2469 CD1 PHE B 119 4025 4874 3953 -625 -46 -232 C ATOM 2470 CD2 PHE B 119 -56.149 105.905 16.602 1.00 31.96 C ANISOU 2470 CD2 PHE B 119 3768 4723 3651 -456 -157 -117 C ATOM 2471 CE1 PHE B 119 -58.420 104.456 17.233 1.00 34.52 C ANISOU 2471 CE1 PHE B 119 4078 4974 4065 -736 118 -315 C ATOM 2472 CE2 PHE B 119 -57.154 106.482 17.368 1.00 32.76 C ANISOU 2472 CE2 PHE B 119 3853 4827 3767 -542 -21 -177 C ATOM 2473 CZ PHE B 119 -58.290 105.757 17.676 1.00 33.97 C ANISOU 2473 CZ PHE B 119 3982 4949 3975 -683 125 -291 C ATOM 2474 N PRO B 120 -53.428 101.110 14.941 1.00 34.59 N ANISOU 2474 N PRO B 120 4300 4786 4058 -288 -559 -143 N ATOM 2475 CA PRO B 120 -52.657 100.456 13.884 1.00 35.03 C ANISOU 2475 CA PRO B 120 4251 4862 4197 -188 -646 -220 C ATOM 2476 C PRO B 120 -53.263 100.766 12.517 1.00 34.49 C ANISOU 2476 C PRO B 120 4010 4936 4159 -203 -557 -273 C ATOM 2477 O PRO B 120 -54.343 101.359 12.451 1.00 33.36 O ANISOU 2477 O PRO B 120 3826 4854 3994 -266 -474 -260 O ATOM 2478 CB PRO B 120 -52.795 98.968 14.216 1.00 36.35 C ANISOU 2478 CB PRO B 120 4607 4849 4355 -206 -719 -226 C ATOM 2479 CG PRO B 120 -54.103 98.858 14.925 1.00 36.86 C ANISOU 2479 CG PRO B 120 4815 4856 4334 -382 -578 -177 C ATOM 2480 CD PRO B 120 -54.384 100.186 15.580 1.00 36.01 C ANISOU 2480 CD PRO B 120 4668 4832 4181 -425 -488 -130 C ATOM 2481 N PRO B 121 -52.575 100.374 11.427 1.00 35.11 N ANISOU 2481 N PRO B 121 4000 5053 4289 -141 -588 -358 N ATOM 2482 CA PRO B 121 -53.196 100.492 10.108 1.00 34.81 C ANISOU 2482 CA PRO B 121 3885 5105 4237 -165 -532 -406 C ATOM 2483 C PRO B 121 -54.517 99.727 10.071 1.00 35.59 C ANISOU 2483 C PRO B 121 4008 5167 4350 -233 -518 -412 C ATOM 2484 O PRO B 121 -54.592 98.614 10.591 1.00 36.49 O ANISOU 2484 O PRO B 121 4212 5164 4487 -264 -538 -414 O ATOM 2485 CB PRO B 121 -52.169 99.841 9.170 1.00 35.56 C ANISOU 2485 CB PRO B 121 3928 5203 4382 -115 -548 -517 C ATOM 2486 CG PRO B 121 -50.872 99.913 9.901 1.00 36.06 C ANISOU 2486 CG PRO B 121 3959 5229 4513 -47 -603 -556 C ATOM 2487 CD PRO B 121 -51.236 99.764 11.350 1.00 35.93 C ANISOU 2487 CD PRO B 121 4072 5104 4473 -45 -683 -446 C ATOM 2488 N SER B 122 -55.557 100.334 9.504 1.00 35.47 N ANISOU 2488 N SER B 122 3924 5229 4323 -258 -498 -435 N ATOM 2489 CA SER B 122 -56.815 99.617 9.288 1.00 36.28 C ANISOU 2489 CA SER B 122 3984 5318 4482 -326 -487 -508 C ATOM 2490 C SER B 122 -56.595 98.538 8.236 1.00 36.88 C ANISOU 2490 C SER B 122 4072 5370 4570 -314 -530 -573 C ATOM 2491 O SER B 122 -55.784 98.704 7.325 1.00 36.80 O ANISOU 2491 O SER B 122 4074 5394 4516 -252 -559 -589 O ATOM 2492 CB SER B 122 -57.915 100.569 8.829 1.00 36.34 C ANISOU 2492 CB SER B 122 3882 5412 4514 -307 -521 -568 C ATOM 2493 OG SER B 122 -57.566 101.179 7.602 1.00 36.53 O ANISOU 2493 OG SER B 122 3938 5481 4460 -221 -614 -574 O ATOM 2494 N SER B 123 -57.327 97.438 8.358 1.00 38.20 N ANISOU 2494 N SER B 123 4250 5471 4793 -399 -506 -630 N ATOM 2495 CA SER B 123 -57.302 96.390 7.341 1.00 39.17 C ANISOU 2495 CA SER B 123 4383 5566 4932 -397 -547 -707 C ATOM 2496 C SER B 123 -57.734 96.940 5.974 1.00 39.20 C ANISOU 2496 C SER B 123 4314 5671 4909 -347 -624 -778 C ATOM 2497 O SER B 123 -57.251 96.484 4.950 1.00 39.25 O ANISOU 2497 O SER B 123 4366 5673 4874 -317 -657 -821 O ATOM 2498 CB SER B 123 -58.192 95.219 7.750 1.00 40.31 C ANISOU 2498 CB SER B 123 4565 5615 5135 -532 -493 -769 C ATOM 2499 OG SER B 123 -59.489 95.683 8.088 1.00 41.36 O ANISOU 2499 OG SER B 123 4574 5808 5335 -630 -431 -845 O ATOM 2500 N GLU B 124 -58.632 97.921 5.963 1.00 39.48 N ANISOU 2500 N GLU B 124 4264 5776 4960 -333 -668 -804 N ATOM 2501 CA GLU B 124 -58.993 98.596 4.722 1.00 40.34 C ANISOU 2501 CA GLU B 124 4384 5937 5007 -256 -807 -859 C ATOM 2502 C GLU B 124 -57.815 99.332 4.076 1.00 39.47 C ANISOU 2502 C GLU B 124 4430 5833 4734 -203 -804 -782 C ATOM 2503 O GLU B 124 -57.623 99.223 2.863 1.00 39.92 O ANISOU 2503 O GLU B 124 4604 5878 4683 -193 -860 -826 O ATOM 2504 CB GLU B 124 -60.191 99.508 4.949 1.00 41.38 C ANISOU 2504 CB GLU B 124 4391 6112 5218 -216 -902 -933 C ATOM 2505 CG GLU B 124 -60.683 100.269 3.734 1.00 43.10 C ANISOU 2505 CG GLU B 124 4675 6338 5363 -100 -1128 -999 C ATOM 2506 CD GLU B 124 -62.022 100.959 3.955 1.00 44.68 C ANISOU 2506 CD GLU B 124 4694 6566 5716 -24 -1279 -1145 C ATOM 2507 OE1 GLU B 124 -62.522 101.004 5.103 1.00 45.32 O ANISOU 2507 OE1 GLU B 124 4584 6680 5954 -86 -1151 -1196 O ATOM 2508 OE2 GLU B 124 -62.578 101.465 2.961 1.00 46.08 O ANISOU 2508 OE2 GLU B 124 4935 6718 5857 100 -1538 -1233 O ATOM 2509 N GLU B 125 -57.029 100.050 4.878 1.00 38.48 N ANISOU 2509 N GLU B 125 4320 5717 4583 -195 -720 -687 N ATOM 2510 CA GLU B 125 -55.836 100.745 4.372 1.00 38.40 C ANISOU 2510 CA GLU B 125 4435 5716 4440 -191 -663 -651 C ATOM 2511 C GLU B 125 -54.768 99.760 3.877 1.00 38.24 C ANISOU 2511 C GLU B 125 4428 5675 4425 -224 -572 -715 C ATOM 2512 O GLU B 125 -54.172 99.978 2.822 1.00 38.52 O ANISOU 2512 O GLU B 125 4583 5714 4340 -261 -520 -771 O ATOM 2513 CB GLU B 125 -55.232 101.684 5.424 1.00 37.52 C ANISOU 2513 CB GLU B 125 4304 5622 4331 -185 -595 -565 C ATOM 2514 CG GLU B 125 -54.170 102.615 4.846 1.00 38.04 C ANISOU 2514 CG GLU B 125 4499 5699 4258 -217 -517 -560 C ATOM 2515 CD GLU B 125 -53.376 103.393 5.885 1.00 37.97 C ANISOU 2515 CD GLU B 125 4446 5708 4272 -225 -440 -503 C ATOM 2516 OE1 GLU B 125 -53.276 102.978 7.061 1.00 37.68 O ANISOU 2516 OE1 GLU B 125 4295 5665 4355 -199 -443 -470 O ATOM 2517 OE2 GLU B 125 -52.818 104.434 5.504 1.00 39.58 O ANISOU 2517 OE2 GLU B 125 4769 5915 4352 -274 -376 -497 O ATOM 2518 N LEU B 126 -54.549 98.681 4.629 1.00 37.81 N ANISOU 2518 N LEU B 126 4282 5581 4503 -217 -553 -726 N ATOM 2519 CA LEU B 126 -53.650 97.595 4.194 1.00 38.32 C ANISOU 2519 CA LEU B 126 4338 5606 4618 -211 -510 -823 C ATOM 2520 C LEU B 126 -54.068 96.977 2.850 1.00 39.21 C ANISOU 2520 C LEU B 126 4517 5712 4668 -244 -526 -914 C ATOM 2521 O LEU B 126 -53.220 96.693 2.005 1.00 39.42 O ANISOU 2521 O LEU B 126 4580 5739 4661 -265 -445 -1020 O ATOM 2522 CB LEU B 126 -53.550 96.510 5.265 1.00 38.41 C ANISOU 2522 CB LEU B 126 4315 5521 4758 -179 -552 -809 C ATOM 2523 CG LEU B 126 -52.825 96.942 6.543 1.00 38.01 C ANISOU 2523 CG LEU B 126 4246 5442 4754 -132 -564 -746 C ATOM 2524 CD1 LEU B 126 -53.130 95.984 7.683 1.00 38.35 C ANISOU 2524 CD1 LEU B 126 4377 5344 4849 -129 -636 -694 C ATOM 2525 CD2 LEU B 126 -51.326 97.055 6.313 1.00 38.48 C ANISOU 2525 CD2 LEU B 126 4229 5519 4873 -72 -535 -858 C ATOM 2526 N GLN B 127 -55.369 96.793 2.648 1.00 38.92 N ANISOU 2526 N GLN B 127 4489 5672 4628 -258 -625 -904 N ATOM 2527 CA GLN B 127 -55.872 96.358 1.348 1.00 39.77 C ANISOU 2527 CA GLN B 127 4682 5771 4658 -283 -684 -992 C ATOM 2528 C GLN B 127 -55.613 97.375 0.235 1.00 40.87 C ANISOU 2528 C GLN B 127 5008 5929 4591 -300 -690 -1003 C ATOM 2529 O GLN B 127 -55.492 96.985 -0.914 1.00 41.12 O ANISOU 2529 O GLN B 127 5179 5934 4512 -342 -686 -1087 O ATOM 2530 CB GLN B 127 -57.351 96.053 1.424 1.00 40.19 C ANISOU 2530 CB GLN B 127 4666 5823 4783 -290 -814 -1020 C ATOM 2531 CG GLN B 127 -57.969 95.238 0.291 1.00 41.36 C ANISOU 2531 CG GLN B 127 4864 5945 4905 -315 -906 -1135 C ATOM 2532 CD GLN B 127 -57.145 94.038 -0.138 1.00 41.84 C ANISOU 2532 CD GLN B 127 4974 5949 4972 -347 -809 -1195 C ATOM 2533 OE1 GLN B 127 -56.635 93.939 -1.273 1.00 42.51 O ANISOU 2533 OE1 GLN B 127 5196 6024 4930 -363 -786 -1263 O ATOM 2534 NE2 GLN B 127 -56.994 93.123 0.786 1.00 41.64 N ANISOU 2534 NE2 GLN B 127 4870 5867 5085 -362 -750 -1184 N ATOM 2535 N ALA B 128 -55.550 98.666 0.572 1.00 40.99 N ANISOU 2535 N ALA B 128 5074 5969 4531 -284 -698 -920 N ATOM 2536 CA ALA B 128 -55.083 99.701 -0.371 1.00 42.59 C ANISOU 2536 CA ALA B 128 5537 6148 4497 -335 -665 -919 C ATOM 2537 C ALA B 128 -53.553 99.755 -0.556 1.00 43.46 C ANISOU 2537 C ALA B 128 5679 6271 4561 -436 -414 -983 C ATOM 2538 O ALA B 128 -53.048 100.709 -1.148 1.00 43.96 O ANISOU 2538 O ALA B 128 5970 6310 4424 -531 -319 -988 O ATOM 2539 CB ALA B 128 -55.605 101.073 0.051 1.00 42.32 C ANISOU 2539 CB ALA B 128 5574 6108 4398 -281 -776 -820 C ATOM 2540 N ASN B 129 -52.825 98.740 -0.078 1.00 44.36 N ANISOU 2540 N ASN B 129 5581 6408 4864 -424 -311 -1060 N ATOM 2541 CA ASN B 129 -51.355 98.681 -0.155 1.00 45.88 C ANISOU 2541 CA ASN B 129 5705 6625 5103 -492 -92 -1195 C ATOM 2542 C ASN B 129 -50.643 99.857 0.523 1.00 46.00 C ANISOU 2542 C ASN B 129 5686 6680 5113 -527 4 -1159 C ATOM 2543 O ASN B 129 -49.630 100.357 0.029 1.00 46.77 O ANISOU 2543 O ASN B 129 5836 6795 5140 -657 215 -1286 O ATOM 2544 CB ASN B 129 -50.863 98.539 -1.610 1.00 48.12 C ANISOU 2544 CB ASN B 129 6188 6884 5212 -635 73 -1351 C ATOM 2545 CG ASN B 129 -49.433 98.043 -1.682 1.00 49.71 C ANISOU 2545 CG ASN B 129 6210 7117 5562 -693 307 -1581 C ATOM 2546 OD1 ASN B 129 -49.190 96.891 -1.387 1.00 50.44 O ANISOU 2546 OD1 ASN B 129 6100 7200 5866 -593 263 -1674 O ATOM 2547 ND2 ASN B 129 -48.474 98.920 -2.027 1.00 51.24 N ANISOU 2547 ND2 ASN B 129 6469 7337 5661 -855 551 -1698 N ATOM 2548 N LYS B 130 -51.184 100.288 1.657 1.00 45.28 N ANISOU 2548 N LYS B 130 5509 6600 5095 -434 -127 -1009 N ATOM 2549 CA LYS B 130 -50.591 101.363 2.448 1.00 45.53 C ANISOU 2549 CA LYS B 130 5498 6664 5136 -451 -65 -963 C ATOM 2550 C LYS B 130 -50.749 101.023 3.926 1.00 43.57 C ANISOU 2550 C LYS B 130 5059 6417 5077 -330 -184 -879 C ATOM 2551 O LYS B 130 -51.515 100.126 4.299 1.00 42.71 O ANISOU 2551 O LYS B 130 4905 6273 5050 -259 -304 -832 O ATOM 2552 CB LYS B 130 -51.252 102.713 2.123 1.00 46.69 C ANISOU 2552 CB LYS B 130 5890 6788 5063 -496 -105 -844 C ATOM 2553 CG LYS B 130 -51.110 103.202 0.671 1.00 50.04 C ANISOU 2553 CG LYS B 130 6639 7155 5217 -640 -7 -905 C ATOM 2554 CD LYS B 130 -52.197 104.196 0.250 1.00 51.42 C ANISOU 2554 CD LYS B 130 7118 7247 5173 -607 -194 -775 C ATOM 2555 CE LYS B 130 -52.488 104.160 -1.251 1.00 54.22 C ANISOU 2555 CE LYS B 130 7844 7499 5257 -692 -226 -823 C ATOM 2556 NZ LYS B 130 -53.559 105.121 -1.649 1.00 55.69 N ANISOU 2556 NZ LYS B 130 8353 7568 5241 -612 -494 -716 N ATOM 2557 N ALA B 131 -49.985 101.715 4.762 1.00 43.28 N ANISOU 2557 N ALA B 131 4940 6407 5098 -330 -139 -875 N ATOM 2558 CA ALA B 131 -50.045 101.511 6.203 1.00 41.84 C ANISOU 2558 CA ALA B 131 4649 6201 5048 -231 -257 -793 C ATOM 2559 C ALA B 131 -49.656 102.796 6.920 1.00 41.15 C ANISOU 2559 C ALA B 131 4564 6146 4925 -259 -220 -736 C ATOM 2560 O ALA B 131 -48.559 103.332 6.702 1.00 42.39 O ANISOU 2560 O ALA B 131 4667 6343 5098 -326 -98 -857 O ATOM 2561 CB ALA B 131 -49.133 100.360 6.616 1.00 42.63 C ANISOU 2561 CB ALA B 131 4604 6256 5338 -147 -309 -924 C ATOM 2562 N THR B 132 -50.557 103.282 7.772 1.00 38.98 N ANISOU 2562 N THR B 132 4342 5856 4615 -225 -304 -581 N ATOM 2563 CA THR B 132 -50.309 104.467 8.583 1.00 38.14 C ANISOU 2563 CA THR B 132 4250 5767 4474 -241 -285 -514 C ATOM 2564 C THR B 132 -50.666 104.138 10.030 1.00 37.24 C ANISOU 2564 C THR B 132 4112 5604 4435 -175 -390 -424 C ATOM 2565 O THR B 132 -51.783 103.698 10.304 1.00 36.58 O ANISOU 2565 O THR B 132 4069 5486 4344 -164 -436 -355 O ATOM 2566 CB THR B 132 -51.146 105.669 8.104 1.00 37.75 C ANISOU 2566 CB THR B 132 4355 5726 4264 -280 -269 -427 C ATOM 2567 OG1 THR B 132 -51.088 105.771 6.678 1.00 38.32 O ANISOU 2567 OG1 THR B 132 4557 5793 4209 -348 -207 -491 O ATOM 2568 CG2 THR B 132 -50.639 106.970 8.721 1.00 37.65 C ANISOU 2568 CG2 THR B 132 4381 5723 4200 -320 -216 -388 C ATOM 2569 N LEU B 133 -49.706 104.304 10.936 1.00 37.19 N ANISOU 2569 N LEU B 133 4052 5581 4496 -148 -425 -452 N ATOM 2570 CA LEU B 133 -49.989 104.279 12.372 1.00 37.08 C ANISOU 2570 CA LEU B 133 4105 5498 4487 -114 -518 -353 C ATOM 2571 C LEU B 133 -50.336 105.697 12.772 1.00 35.81 C ANISOU 2571 C LEU B 133 3993 5379 4234 -163 -454 -269 C ATOM 2572 O LEU B 133 -49.647 106.635 12.376 1.00 34.64 O ANISOU 2572 O LEU B 133 3813 5287 4060 -202 -384 -315 O ATOM 2573 CB LEU B 133 -48.795 103.806 13.198 1.00 38.93 C ANISOU 2573 CB LEU B 133 4299 5665 4827 -34 -653 -432 C ATOM 2574 CG LEU B 133 -48.468 102.314 13.145 1.00 40.50 C ANISOU 2574 CG LEU B 133 4499 5762 5127 57 -787 -513 C ATOM 2575 CD1 LEU B 133 -47.803 101.947 11.825 1.00 41.80 C ANISOU 2575 CD1 LEU B 133 4489 6000 5391 65 -713 -692 C ATOM 2576 CD2 LEU B 133 -47.564 101.944 14.305 1.00 41.74 C ANISOU 2576 CD2 LEU B 133 4704 5796 5360 171 -1009 -560 C ATOM 2577 N VAL B 134 -51.407 105.833 13.550 1.00 35.32 N ANISOU 2577 N VAL B 134 4015 5280 4125 -178 -458 -169 N ATOM 2578 CA VAL B 134 -51.936 107.125 13.951 1.00 34.68 C ANISOU 2578 CA VAL B 134 3976 5227 3973 -207 -404 -106 C ATOM 2579 C VAL B 134 -51.892 107.208 15.471 1.00 34.60 C ANISOU 2579 C VAL B 134 4055 5149 3944 -223 -430 -48 C ATOM 2580 O VAL B 134 -52.605 106.487 16.171 1.00 34.36 O ANISOU 2580 O VAL B 134 4108 5045 3904 -258 -426 -20 O ATOM 2581 CB VAL B 134 -53.386 107.332 13.452 1.00 34.64 C ANISOU 2581 CB VAL B 134 3966 5242 3953 -209 -374 -99 C ATOM 2582 CG1 VAL B 134 -53.867 108.741 13.784 1.00 34.73 C ANISOU 2582 CG1 VAL B 134 4013 5268 3915 -204 -348 -67 C ATOM 2583 CG2 VAL B 134 -53.489 107.063 11.955 1.00 35.17 C ANISOU 2583 CG2 VAL B 134 4010 5344 4011 -189 -393 -154 C ATOM 2584 N CYS B 135 -51.047 108.100 15.969 1.00 34.51 N ANISOU 2584 N CYS B 135 4054 5148 3910 -222 -444 -42 N ATOM 2585 CA CYS B 135 -50.913 108.331 17.381 1.00 35.07 C ANISOU 2585 CA CYS B 135 4244 5147 3935 -240 -486 9 C ATOM 2586 C CYS B 135 -51.643 109.616 17.742 1.00 34.55 C ANISOU 2586 C CYS B 135 4215 5110 3801 -283 -384 57 C ATOM 2587 O CYS B 135 -51.227 110.704 17.359 1.00 34.99 O ANISOU 2587 O CYS B 135 4236 5220 3839 -283 -354 48 O ATOM 2588 CB CYS B 135 -49.447 108.433 17.744 1.00 36.68 C ANISOU 2588 CB CYS B 135 4414 5337 4186 -196 -605 -53 C ATOM 2589 SG CYS B 135 -49.171 108.593 19.505 1.00 38.46 S ANISOU 2589 SG CYS B 135 4848 5437 4330 -199 -728 6 S ATOM 2590 N LEU B 136 -52.757 109.467 18.447 1.00 34.27 N ANISOU 2590 N LEU B 136 4258 5029 3733 -334 -313 84 N ATOM 2591 CA LEU B 136 -53.565 110.581 18.898 1.00 34.14 C ANISOU 2591 CA LEU B 136 4257 5030 3686 -365 -214 87 C ATOM 2592 C LEU B 136 -53.234 110.935 20.328 1.00 34.40 C ANISOU 2592 C LEU B 136 4456 4986 3628 -425 -204 129 C ATOM 2593 O LEU B 136 -53.315 110.085 21.193 1.00 34.43 O ANISOU 2593 O LEU B 136 4620 4890 3572 -493 -207 149 O ATOM 2594 CB LEU B 136 -55.032 110.161 18.837 1.00 35.19 C ANISOU 2594 CB LEU B 136 4333 5165 3874 -407 -110 21 C ATOM 2595 CG LEU B 136 -56.025 110.964 19.711 1.00 36.55 C ANISOU 2595 CG LEU B 136 4515 5326 4048 -467 25 -37 C ATOM 2596 CD1 LEU B 136 -56.258 112.256 18.972 1.00 36.60 C ANISOU 2596 CD1 LEU B 136 4416 5391 4099 -353 -23 -68 C ATOM 2597 CD2 LEU B 136 -57.341 110.252 20.003 1.00 37.98 C ANISOU 2597 CD2 LEU B 136 4639 5492 4301 -574 177 -159 C ATOM 2598 N ILE B 137 -52.953 112.216 20.556 1.00 34.23 N ANISOU 2598 N ILE B 137 4440 4992 3575 -413 -190 142 N ATOM 2599 CA ILE B 137 -52.596 112.753 21.851 1.00 35.04 C ANISOU 2599 CA ILE B 137 4703 5027 3582 -468 -189 175 C ATOM 2600 C ILE B 137 -53.670 113.792 22.192 1.00 35.61 C ANISOU 2600 C ILE B 137 4771 5113 3647 -499 -41 140 C ATOM 2601 O ILE B 137 -53.873 114.741 21.430 1.00 34.27 O ANISOU 2601 O ILE B 137 4498 4999 3524 -430 -37 117 O ATOM 2602 CB ILE B 137 -51.203 113.414 21.788 1.00 35.00 C ANISOU 2602 CB ILE B 137 4679 5045 3573 -429 -304 181 C ATOM 2603 CG1 ILE B 137 -50.192 112.500 21.079 1.00 35.22 C ANISOU 2603 CG1 ILE B 137 4603 5095 3685 -372 -434 140 C ATOM 2604 CG2 ILE B 137 -50.696 113.751 23.178 1.00 36.01 C ANISOU 2604 CG2 ILE B 137 4993 5088 3602 -474 -363 207 C ATOM 2605 CD1 ILE B 137 -48.943 113.210 20.615 1.00 35.70 C ANISOU 2605 CD1 ILE B 137 4548 5218 3799 -363 -477 70 C ATOM 2606 N SER B 138 -54.359 113.610 23.319 1.00 36.56 N ANISOU 2606 N SER B 138 5028 5161 3702 -607 81 118 N ATOM 2607 CA SER B 138 -55.504 114.474 23.681 1.00 37.41 C ANISOU 2607 CA SER B 138 5085 5283 3847 -642 251 21 C ATOM 2608 C SER B 138 -55.469 114.956 25.131 1.00 38.07 C ANISOU 2608 C SER B 138 5393 5280 3794 -762 354 25 C ATOM 2609 O SER B 138 -54.860 114.316 25.992 1.00 38.27 O ANISOU 2609 O SER B 138 5667 5202 3670 -852 309 98 O ATOM 2610 CB SER B 138 -56.819 113.740 23.401 1.00 38.94 C ANISOU 2610 CB SER B 138 5144 5498 4153 -694 392 -108 C ATOM 2611 OG SER B 138 -56.825 112.471 24.016 1.00 40.41 O ANISOU 2611 OG SER B 138 5508 5598 4249 -842 457 -87 O ATOM 2612 N ASP B 139 -56.099 116.111 25.371 1.00 38.17 N ANISOU 2612 N ASP B 139 5341 5313 3850 -749 462 -61 N ATOM 2613 CA ASP B 139 -56.381 116.636 26.709 1.00 39.90 C ANISOU 2613 CA ASP B 139 5748 5456 3958 -881 624 -108 C ATOM 2614 C ASP B 139 -55.123 116.907 27.525 1.00 38.70 C ANISOU 2614 C ASP B 139 5859 5226 3618 -912 492 27 C ATOM 2615 O ASP B 139 -55.009 116.471 28.673 1.00 39.31 O ANISOU 2615 O ASP B 139 6230 5187 3520 -1060 546 51 O ATOM 2616 CB ASP B 139 -57.343 115.708 27.484 1.00 42.69 C ANISOU 2616 CB ASP B 139 6210 5744 4268 -1089 868 -218 C ATOM 2617 CG ASP B 139 -58.758 115.757 26.948 1.00 44.75 C ANISOU 2617 CG ASP B 139 6160 6088 4756 -1082 1046 -444 C ATOM 2618 OD1 ASP B 139 -59.345 116.862 26.902 1.00 46.64 O ANISOU 2618 OD1 ASP B 139 6227 6371 5124 -997 1100 -581 O ATOM 2619 OD2 ASP B 139 -59.296 114.690 26.596 1.00 46.05 O ANISOU 2619 OD2 ASP B 139 6249 6263 4985 -1156 1118 -508 O ATOM 2620 N PHE B 140 -54.179 117.635 26.929 1.00 36.45 N ANISOU 2620 N PHE B 140 5492 4991 3365 -786 315 97 N ATOM 2621 CA PHE B 140 -52.979 118.033 27.658 1.00 35.86 C ANISOU 2621 CA PHE B 140 5603 4860 3162 -807 177 173 C ATOM 2622 C PHE B 140 -52.814 119.547 27.735 1.00 35.31 C ANISOU 2622 C PHE B 140 5512 4808 3095 -775 200 153 C ATOM 2623 O PHE B 140 -53.308 120.293 26.890 1.00 34.71 O ANISOU 2623 O PHE B 140 5274 4788 3128 -689 244 110 O ATOM 2624 CB PHE B 140 -51.720 117.346 27.117 1.00 34.95 C ANISOU 2624 CB PHE B 140 5442 4764 3075 -735 -57 234 C ATOM 2625 CG PHE B 140 -51.430 117.625 25.667 1.00 33.59 C ANISOU 2625 CG PHE B 140 5010 4705 3047 -632 -98 221 C ATOM 2626 CD1 PHE B 140 -51.962 116.823 24.673 1.00 32.83 C ANISOU 2626 CD1 PHE B 140 4766 4661 3048 -583 -77 208 C ATOM 2627 CD2 PHE B 140 -50.593 118.676 25.300 1.00 33.00 C ANISOU 2627 CD2 PHE B 140 4880 4668 2989 -611 -148 213 C ATOM 2628 CE1 PHE B 140 -51.679 117.072 23.333 1.00 31.94 C ANISOU 2628 CE1 PHE B 140 4483 4628 3024 -510 -112 196 C ATOM 2629 CE2 PHE B 140 -50.305 118.928 23.971 1.00 32.31 C ANISOU 2629 CE2 PHE B 140 4637 4654 2986 -564 -153 196 C ATOM 2630 CZ PHE B 140 -50.860 118.132 22.985 1.00 31.83 C ANISOU 2630 CZ PHE B 140 4461 4635 2998 -510 -139 192 C ATOM 2631 N TYR B 141 -52.133 119.977 28.791 1.00 35.09 N ANISOU 2631 N TYR B 141 5695 4707 2931 -844 148 180 N ATOM 2632 CA TYR B 141 -51.813 121.382 29.031 1.00 34.84 C ANISOU 2632 CA TYR B 141 5692 4670 2874 -839 158 165 C ATOM 2633 C TYR B 141 -50.590 121.379 29.944 1.00 35.48 C ANISOU 2633 C TYR B 141 5965 4687 2830 -894 -17 203 C ATOM 2634 O TYR B 141 -50.583 120.620 30.918 1.00 36.72 O ANISOU 2634 O TYR B 141 6359 4744 2849 -967 -58 224 O ATOM 2635 CB TYR B 141 -52.985 122.116 29.693 1.00 35.16 C ANISOU 2635 CB TYR B 141 5799 4668 2890 -888 378 79 C ATOM 2636 CG TYR B 141 -52.730 123.606 29.904 1.00 35.04 C ANISOU 2636 CG TYR B 141 5831 4629 2853 -869 386 58 C ATOM 2637 CD1 TYR B 141 -52.994 124.535 28.892 1.00 34.16 C ANISOU 2637 CD1 TYR B 141 5575 4548 2858 -751 380 29 C ATOM 2638 CD2 TYR B 141 -52.199 124.080 31.105 1.00 35.47 C ANISOU 2638 CD2 TYR B 141 6124 4603 2749 -971 376 68 C ATOM 2639 CE1 TYR B 141 -52.738 125.900 29.084 1.00 34.44 C ANISOU 2639 CE1 TYR B 141 5704 4528 2853 -744 380 13 C ATOM 2640 CE2 TYR B 141 -51.947 125.436 31.308 1.00 35.81 C ANISOU 2640 CE2 TYR B 141 6221 4616 2770 -966 387 43 C ATOM 2641 CZ TYR B 141 -52.217 126.344 30.305 1.00 35.16 C ANISOU 2641 CZ TYR B 141 5995 4558 2805 -856 398 17 C ATOM 2642 OH TYR B 141 -51.944 127.683 30.527 1.00 35.62 O ANISOU 2642 OH TYR B 141 6158 4556 2821 -862 404 -4 O ATOM 2643 N PRO B 142 -49.547 122.163 29.660 1.00 35.00 N ANISOU 2643 N PRO B 142 5832 4659 2805 -870 -133 194 N ATOM 2644 CA PRO B 142 -49.436 123.088 28.521 1.00 34.16 C ANISOU 2644 CA PRO B 142 5546 4627 2806 -825 -81 174 C ATOM 2645 C PRO B 142 -49.383 122.417 27.145 1.00 33.24 C ANISOU 2645 C PRO B 142 5221 4594 2816 -756 -104 178 C ATOM 2646 O PRO B 142 -49.132 121.220 27.056 1.00 32.65 O ANISOU 2646 O PRO B 142 5091 4538 2775 -733 -196 187 O ATOM 2647 CB PRO B 142 -48.105 123.785 28.787 1.00 34.82 C ANISOU 2647 CB PRO B 142 5649 4707 2874 -881 -199 136 C ATOM 2648 CG PRO B 142 -47.956 123.756 30.261 1.00 35.97 C ANISOU 2648 CG PRO B 142 6025 4761 2882 -936 -273 138 C ATOM 2649 CD PRO B 142 -48.680 122.557 30.784 1.00 36.23 C ANISOU 2649 CD PRO B 142 6185 4739 2843 -932 -266 183 C ATOM 2650 N GLY B 143 -49.625 123.207 26.102 1.00 32.66 N ANISOU 2650 N GLY B 143 5079 4543 2786 -725 -32 170 N ATOM 2651 CA GLY B 143 -49.722 122.727 24.731 1.00 32.44 C ANISOU 2651 CA GLY B 143 4914 4572 2839 -671 -36 173 C ATOM 2652 C GLY B 143 -48.391 122.561 24.033 1.00 32.84 C ANISOU 2652 C GLY B 143 4868 4678 2933 -733 -91 130 C ATOM 2653 O GLY B 143 -48.082 123.277 23.073 1.00 33.45 O ANISOU 2653 O GLY B 143 4965 4751 2995 -780 -29 108 O ATOM 2654 N ALA B 144 -47.608 121.601 24.510 1.00 33.24 N ANISOU 2654 N ALA B 144 4833 4761 3036 -738 -207 93 N ATOM 2655 CA ALA B 144 -46.297 121.326 23.950 1.00 34.21 C ANISOU 2655 CA ALA B 144 4793 4946 3257 -788 -265 -18 C ATOM 2656 C ALA B 144 -45.879 119.912 24.350 1.00 35.45 C ANISOU 2656 C ALA B 144 4856 5115 3500 -710 -445 -54 C ATOM 2657 O ALA B 144 -45.953 119.531 25.517 1.00 35.83 O ANISOU 2657 O ALA B 144 5033 5091 3490 -674 -576 -20 O ATOM 2658 CB ALA B 144 -45.285 122.357 24.418 1.00 35.26 C ANISOU 2658 CB ALA B 144 4941 5072 3385 -899 -270 -111 C ATOM 2659 N VAL B 145 -45.471 119.131 23.358 1.00 36.06 N ANISOU 2659 N VAL B 145 4753 5257 3693 -686 -453 -126 N ATOM 2660 CA VAL B 145 -45.252 117.712 23.544 1.00 36.98 C ANISOU 2660 CA VAL B 145 4799 5360 3892 -584 -628 -155 C ATOM 2661 C VAL B 145 -44.120 117.268 22.607 1.00 38.25 C ANISOU 2661 C VAL B 145 4692 5606 4237 -591 -653 -345 C ATOM 2662 O VAL B 145 -43.891 117.914 21.580 1.00 38.42 O ANISOU 2662 O VAL B 145 4627 5694 4276 -701 -461 -409 O ATOM 2663 CB VAL B 145 -46.617 116.997 23.331 1.00 35.86 C ANISOU 2663 CB VAL B 145 4757 5188 3678 -531 -559 -14 C ATOM 2664 CG1 VAL B 145 -46.893 116.642 21.869 1.00 35.15 C ANISOU 2664 CG1 VAL B 145 4529 5173 3654 -522 -448 -30 C ATOM 2665 CG2 VAL B 145 -46.748 115.795 24.227 1.00 36.61 C ANISOU 2665 CG2 VAL B 145 4977 5188 3744 -462 -732 22 C ATOM 2666 N THR B 146 -43.365 116.238 23.000 1.00 39.76 N ANISOU 2666 N THR B 146 4776 5772 4559 -486 -891 -461 N ATOM 2667 CA THR B 146 -42.369 115.617 22.114 1.00 40.94 C ANISOU 2667 CA THR B 146 4628 6001 4928 -467 -918 -688 C ATOM 2668 C THR B 146 -42.867 114.224 21.792 1.00 40.57 C ANISOU 2668 C THR B 146 4598 5914 4904 -339 -1010 -628 C ATOM 2669 O THR B 146 -43.275 113.491 22.691 1.00 40.81 O ANISOU 2669 O THR B 146 4824 5823 4859 -231 -1211 -519 O ATOM 2670 CB THR B 146 -40.967 115.503 22.756 1.00 43.48 C ANISOU 2670 CB THR B 146 4749 6318 5452 -409 -1171 -951 C ATOM 2671 OG1 THR B 146 -40.632 116.729 23.403 1.00 44.27 O ANISOU 2671 OG1 THR B 146 4898 6422 5499 -516 -1139 -976 O ATOM 2672 CG2 THR B 146 -39.902 115.167 21.703 1.00 45.10 C ANISOU 2672 CG2 THR B 146 4575 6638 5925 -443 -1101 -1263 C ATOM 2673 N VAL B 147 -42.835 113.873 20.510 1.00 40.67 N ANISOU 2673 N VAL B 147 4447 6009 4997 -375 -850 -701 N ATOM 2674 CA VAL B 147 -43.265 112.565 20.043 1.00 40.44 C ANISOU 2674 CA VAL B 147 4412 5950 5003 -269 -915 -667 C ATOM 2675 C VAL B 147 -42.070 111.849 19.416 1.00 42.04 C ANISOU 2675 C VAL B 147 4307 6206 5461 -216 -991 -956 C ATOM 2676 O VAL B 147 -41.370 112.412 18.574 1.00 42.38 O ANISOU 2676 O VAL B 147 4141 6359 5604 -348 -792 -1148 O ATOM 2677 CB VAL B 147 -44.424 112.673 19.036 1.00 38.72 C ANISOU 2677 CB VAL B 147 4287 5772 4653 -341 -676 -510 C ATOM 2678 CG1 VAL B 147 -44.845 111.291 18.556 1.00 38.89 C ANISOU 2678 CG1 VAL B 147 4294 5764 4720 -244 -742 -492 C ATOM 2679 CG2 VAL B 147 -45.607 113.393 19.673 1.00 37.47 C ANISOU 2679 CG2 VAL B 147 4371 5564 4300 -372 -612 -292 C ATOM 2680 N ALA B 148 -41.843 110.616 19.860 1.00 43.01 N ANISOU 2680 N ALA B 148 4427 6232 5684 -33 -1275 -1006 N ATOM 2681 CA ALA B 148 -40.805 109.748 19.322 1.00 45.31 C ANISOU 2681 CA ALA B 148 4419 6548 6249 71 -1398 -1304 C ATOM 2682 C ALA B 148 -41.449 108.410 18.979 1.00 45.31 C ANISOU 2682 C ALA B 148 4531 6462 6221 188 -1480 -1204 C ATOM 2683 O ALA B 148 -42.318 107.930 19.710 1.00 44.67 O ANISOU 2683 O ALA B 148 4767 6244 5962 247 -1607 -968 O ATOM 2684 CB ALA B 148 -39.696 109.559 20.342 1.00 47.86 C ANISOU 2684 CB ALA B 148 4631 6792 6762 232 -1774 -1524 C ATOM 2685 N TRP B 149 -41.030 107.826 17.860 1.00 46.51 N ANISOU 2685 N TRP B 149 4439 6691 6543 190 -1376 -1400 N ATOM 2686 CA TRP B 149 -41.550 106.542 17.398 1.00 46.59 C ANISOU 2686 CA TRP B 149 4526 6627 6551 292 -1439 -1341 C ATOM 2687 C TRP B 149 -40.472 105.470 17.540 1.00 49.88 C ANISOU 2687 C TRP B 149 4739 6961 7253 512 -1757 -1637 C ATOM 2688 O TRP B 149 -39.288 105.753 17.354 1.00 51.54 O ANISOU 2688 O TRP B 149 4602 7256 7726 529 -1780 -1975 O ATOM 2689 CB TRP B 149 -41.989 106.648 15.940 1.00 45.55 C ANISOU 2689 CB TRP B 149 4311 6624 6372 135 -1086 -1339 C ATOM 2690 CG TRP B 149 -43.275 107.379 15.752 1.00 43.14 C ANISOU 2690 CG TRP B 149 4254 6345 5793 -6 -873 -1041 C ATOM 2691 CD1 TRP B 149 -43.441 108.721 15.571 1.00 42.18 C ANISOU 2691 CD1 TRP B 149 4175 6302 5548 -168 -660 -977 C ATOM 2692 CD2 TRP B 149 -44.582 106.801 15.710 1.00 41.68 C ANISOU 2692 CD2 TRP B 149 4296 6093 5446 12 -869 -804 C ATOM 2693 NE1 TRP B 149 -44.776 109.019 15.425 1.00 40.41 N ANISOU 2693 NE1 TRP B 149 4180 6060 5112 -217 -561 -724 N ATOM 2694 CE2 TRP B 149 -45.500 107.856 15.502 1.00 39.80 C ANISOU 2694 CE2 TRP B 149 4191 5909 5023 -117 -673 -629 C ATOM 2695 CE3 TRP B 149 -45.067 105.492 15.830 1.00 41.99 C ANISOU 2695 CE3 TRP B 149 4441 6022 5489 120 -1014 -746 C ATOM 2696 CZ2 TRP B 149 -46.877 107.644 15.415 1.00 38.44 C ANISOU 2696 CZ2 TRP B 149 4191 5704 4710 -130 -625 -437 C ATOM 2697 CZ3 TRP B 149 -46.442 105.278 15.738 1.00 40.28 C ANISOU 2697 CZ3 TRP B 149 4420 5776 5108 65 -924 -538 C ATOM 2698 CH2 TRP B 149 -47.329 106.352 15.526 1.00 38.86 C ANISOU 2698 CH2 TRP B 149 4307 5673 4786 -54 -734 -404 C ATOM 2699 N LYS B 150 -40.894 104.248 17.863 1.00 50.59 N ANISOU 2699 N LYS B 150 5046 6874 7300 675 -1999 -1535 N ATOM 2700 CA LYS B 150 -39.991 103.106 17.976 1.00 54.03 C ANISOU 2700 CA LYS B 150 5351 7182 7995 926 -2355 -1803 C ATOM 2701 C LYS B 150 -40.548 101.882 17.249 1.00 54.08 C ANISOU 2701 C LYS B 150 5448 7116 7982 978 -2329 -1750 C ATOM 2702 O LYS B 150 -41.757 101.665 17.224 1.00 51.07 O ANISOU 2702 O LYS B 150 5376 6687 7342 875 -2193 -1444 O ATOM 2703 CB LYS B 150 -39.723 102.780 19.450 1.00 56.07 C ANISOU 2703 CB LYS B 150 5897 7198 8210 1129 -2836 -1756 C ATOM 2704 CG LYS B 150 -38.828 103.795 20.147 1.00 57.39 C ANISOU 2704 CG LYS B 150 5891 7422 8494 1143 -2965 -1927 C ATOM 2705 CD LYS B 150 -38.617 103.445 21.612 1.00 59.79 C ANISOU 2705 CD LYS B 150 6559 7452 8707 1348 -3479 -1865 C ATOM 2706 CE LYS B 150 -37.577 104.348 22.263 1.00 61.84 C ANISOU 2706 CE LYS B 150 6592 7763 9140 1398 -3676 -2105 C ATOM 2707 NZ LYS B 150 -37.055 103.769 23.538 1.00 65.33 N ANISOU 2707 NZ LYS B 150 7336 7904 9581 1681 -4304 -2164 N ATOM 2708 N ALA B 151 -39.646 101.103 16.650 1.00 57.45 N ANISOU 2708 N ALA B 151 5577 7540 8711 1132 -2449 -2087 N ATOM 2709 CA ALA B 151 -39.971 99.823 16.017 1.00 58.68 C ANISOU 2709 CA ALA B 151 5802 7598 8896 1224 -2490 -2096 C ATOM 2710 C ALA B 151 -39.133 98.751 16.700 1.00 62.78 C ANISOU 2710 C ALA B 151 6346 7873 9635 1560 -3020 -2318 C ATOM 2711 O ALA B 151 -37.911 98.738 16.549 1.00 65.78 O ANISOU 2711 O ALA B 151 6320 8302 10372 1712 -3175 -2731 O ATOM 2712 CB ALA B 151 -39.666 99.873 14.529 1.00 58.77 C ANISOU 2712 CB ALA B 151 5442 7821 9068 1095 -2123 -2331 C ATOM 2713 N ASP B 152 -39.789 97.873 17.461 1.00 63.94 N ANISOU 2713 N ASP B 152 6985 7741 9570 1668 -3301 -2070 N ATOM 2714 CA ASP B 152 -39.125 96.875 18.306 1.00 68.54 C ANISOU 2714 CA ASP B 152 7767 8005 10269 2001 -3886 -2212 C ATOM 2715 C ASP B 152 -38.102 97.493 19.277 1.00 71.16 C ANISOU 2715 C ASP B 152 7988 8290 10759 2170 -4254 -2414 C ATOM 2716 O ASP B 152 -36.987 96.986 19.436 1.00 75.58 O ANISOU 2716 O ASP B 152 8324 8738 11656 2476 -4681 -2789 O ATOM 2717 CB ASP B 152 -38.467 95.796 17.461 1.00 71.42 C ANISOU 2717 CB ASP B 152 7854 8327 10957 2211 -4019 -2550 C ATOM 2718 CG ASP B 152 -39.454 94.961 16.669 1.00 70.08 C ANISOU 2718 CG ASP B 152 7885 8125 10616 2091 -3770 -2352 C ATOM 2719 OD1 ASP B 152 -40.630 94.811 17.060 1.00 69.14 O ANISOU 2719 OD1 ASP B 152 8239 7896 10135 1929 -3668 -1965 O ATOM 2720 OD2 ASP B 152 -39.035 94.405 15.644 1.00 71.59 O ANISOU 2720 OD2 ASP B 152 7748 8397 11055 2155 -3676 -2622 O ATOM 2721 N GLY B 153 -38.497 98.593 19.912 1.00 69.52 N ANISOU 2721 N GLY B 153 7924 8166 10325 1980 -4101 -2188 N ATOM 2722 CA GLY B 153 -37.640 99.304 20.868 1.00 72.07 C ANISOU 2722 CA GLY B 153 8175 8456 10752 2098 -4418 -2343 C ATOM 2723 C GLY B 153 -36.530 100.163 20.275 1.00 73.39 C ANISOU 2723 C GLY B 153 7663 8912 11310 2076 -4270 -2761 C ATOM 2724 O GLY B 153 -35.703 100.686 21.017 1.00 75.71 O ANISOU 2724 O GLY B 153 7828 9184 11756 2193 -4564 -2964 O ATOM 2725 N SER B 154 -36.526 100.331 18.950 1.00 72.66 N ANISOU 2725 N SER B 154 7167 9080 11360 1898 -3799 -2899 N ATOM 2726 CA SER B 154 -35.467 101.034 18.226 1.00 74.16 C ANISOU 2726 CA SER B 154 6725 9534 11917 1817 -3572 -3344 C ATOM 2727 C SER B 154 -36.053 102.288 17.575 1.00 70.50 C ANISOU 2727 C SER B 154 6215 9334 11238 1421 -2963 -3146 C ATOM 2728 O SER B 154 -37.044 102.180 16.849 1.00 67.03 O ANISOU 2728 O SER B 154 5967 8947 10555 1246 -2624 -2869 O ATOM 2729 CB SER B 154 -34.895 100.118 17.143 1.00 76.55 C ANISOU 2729 CB SER B 154 6646 9885 12556 1922 -3516 -3722 C ATOM 2730 OG SER B 154 -33.748 100.690 16.543 1.00 79.58 O ANISOU 2730 OG SER B 154 6406 10494 13336 1845 -3318 -4238 O ATOM 2731 N PRO B 155 -35.455 103.477 17.825 1.00 71.07 N ANISOU 2731 N PRO B 155 6053 9553 11396 1284 -2845 -3299 N ATOM 2732 CA PRO B 155 -35.976 104.727 17.247 1.00 68.00 C ANISOU 2732 CA PRO B 155 5683 9371 10783 916 -2303 -3115 C ATOM 2733 C PRO B 155 -36.204 104.695 15.729 1.00 66.87 C ANISOU 2733 C PRO B 155 5388 9392 10630 689 -1806 -3178 C ATOM 2734 O PRO B 155 -35.361 104.184 14.993 1.00 69.20 O ANISOU 2734 O PRO B 155 5297 9754 11242 723 -1745 -3592 O ATOM 2735 CB PRO B 155 -34.888 105.748 17.584 1.00 70.32 C ANISOU 2735 CB PRO B 155 5623 9785 11310 838 -2293 -3452 C ATOM 2736 CG PRO B 155 -34.263 105.233 18.829 1.00 73.31 C ANISOU 2736 CG PRO B 155 6016 9972 11866 1179 -2919 -3594 C ATOM 2737 CD PRO B 155 -34.329 103.737 18.747 1.00 74.46 C ANISOU 2737 CD PRO B 155 6250 9931 12108 1473 -3255 -3632 C ATOM 2738 N VAL B 156 -37.341 105.235 15.287 1.00 63.35 N ANISOU 2738 N VAL B 156 5254 8993 9821 467 -1474 -2794 N ATOM 2739 CA VAL B 156 -37.672 105.360 13.865 1.00 62.28 C ANISOU 2739 CA VAL B 156 5083 8986 9594 229 -1019 -2803 C ATOM 2740 C VAL B 156 -37.869 106.839 13.545 1.00 60.66 C ANISOU 2740 C VAL B 156 4965 8900 9181 -83 -641 -2698 C ATOM 2741 O VAL B 156 -38.817 107.457 14.034 1.00 58.10 O ANISOU 2741 O VAL B 156 4972 8533 8568 -126 -644 -2324 O ATOM 2742 CB VAL B 156 -38.962 104.589 13.501 1.00 59.99 C ANISOU 2742 CB VAL B 156 5134 8609 9049 270 -1013 -2447 C ATOM 2743 CG1 VAL B 156 -39.267 104.715 12.007 1.00 59.62 C ANISOU 2743 CG1 VAL B 156 5082 8676 8897 39 -590 -2475 C ATOM 2744 CG2 VAL B 156 -38.839 103.126 13.898 1.00 61.42 C ANISOU 2744 CG2 VAL B 156 5319 8627 9390 567 -1399 -2514 C ATOM 2745 N LYS B 157 -36.982 107.390 12.717 1.00 62.56 N ANISOU 2745 N LYS B 157 4928 9275 9567 -312 -306 -3048 N ATOM 2746 CA LYS B 157 -37.062 108.800 12.305 1.00 61.92 C ANISOU 2746 CA LYS B 157 4979 9275 9273 -644 77 -2984 C ATOM 2747 C LYS B 157 -37.812 108.980 10.959 1.00 60.12 C ANISOU 2747 C LYS B 157 5028 9064 8751 -877 456 -2823 C ATOM 2748 O LYS B 157 -38.653 109.882 10.834 1.00 58.81 O ANISOU 2748 O LYS B 157 5221 8867 8257 -1015 587 -2507 O ATOM 2749 CB LYS B 157 -35.679 109.481 12.379 1.00 65.53 C ANISOU 2749 CB LYS B 157 5046 9838 10015 -807 227 -3450 C ATOM 2750 CG LYS B 157 -35.447 110.150 13.733 1.00 65.74 C ANISOU 2750 CG LYS B 157 5060 9833 10085 -706 -55 -3391 C ATOM 2751 CD LYS B 157 -34.014 110.620 13.919 1.00 69.89 C ANISOU 2751 CD LYS B 157 5120 10460 10974 -814 6 -3917 C ATOM 2752 CE LYS B 157 -33.760 111.026 15.364 1.00 70.20 C ANISOU 2752 CE LYS B 157 5139 10445 11091 -634 -393 -3876 C ATOM 2753 NZ LYS B 157 -32.554 111.884 15.516 1.00 73.77 N ANISOU 2753 NZ LYS B 157 5209 11006 11813 -830 -254 -4330 N ATOM 2754 N ALA B 158 -37.584 108.075 10.004 1.00 59.89 N ANISOU 2754 N ALA B 158 4866 9058 8830 -886 576 -3028 N ATOM 2755 CA ALA B 158 -38.179 108.171 8.662 1.00 58.13 C ANISOU 2755 CA ALA B 158 4920 8837 8331 -1111 916 -2926 C ATOM 2756 C ALA B 158 -39.694 107.920 8.634 1.00 53.56 C ANISOU 2756 C ALA B 158 4742 8165 7445 -984 753 -2449 C ATOM 2757 O ALA B 158 -40.213 107.070 9.361 1.00 51.48 O ANISOU 2757 O ALA B 158 4472 7840 7247 -709 417 -2283 O ATOM 2758 CB ALA B 158 -37.484 107.206 7.710 1.00 60.57 C ANISOU 2758 CB ALA B 158 4963 9193 8858 -1149 1082 -3306 C ATOM 2759 N GLY B 159 -40.383 108.660 7.768 1.00 51.65 N ANISOU 2759 N GLY B 159 4862 7895 6867 -1197 992 -2263 N ATOM 2760 CA GLY B 159 -41.824 108.518 7.577 1.00 48.29 C ANISOU 2760 CA GLY B 159 4785 7390 6174 -1097 856 -1879 C ATOM 2761 C GLY B 159 -42.685 109.049 8.711 1.00 45.43 C ANISOU 2761 C GLY B 159 4567 6979 5716 -948 610 -1559 C ATOM 2762 O GLY B 159 -43.833 108.629 8.853 1.00 42.51 O ANISOU 2762 O GLY B 159 4354 6555 5241 -803 435 -1306 O ATOM 2763 N VAL B 160 -42.148 109.984 9.498 1.00 45.14 N ANISOU 2763 N VAL B 160 4471 6961 5720 -1004 621 -1595 N ATOM 2764 CA VAL B 160 -42.860 110.548 10.653 1.00 42.80 C ANISOU 2764 CA VAL B 160 4302 6618 5341 -881 415 -1328 C ATOM 2765 C VAL B 160 -43.333 111.961 10.324 1.00 42.30 C ANISOU 2765 C VAL B 160 4554 6513 5006 -1055 577 -1177 C ATOM 2766 O VAL B 160 -42.584 112.770 9.777 1.00 43.00 O ANISOU 2766 O VAL B 160 4688 6614 5035 -1293 830 -1338 O ATOM 2767 CB VAL B 160 -41.979 110.583 11.923 1.00 43.48 C ANISOU 2767 CB VAL B 160 4138 6728 5656 -786 245 -1460 C ATOM 2768 CG1 VAL B 160 -42.727 111.217 13.095 1.00 41.69 C ANISOU 2768 CG1 VAL B 160 4092 6443 5307 -695 73 -1190 C ATOM 2769 CG2 VAL B 160 -41.526 109.173 12.290 1.00 44.39 C ANISOU 2769 CG2 VAL B 160 4004 6834 6030 -572 9 -1611 C ATOM 2770 N GLU B 161 -44.586 112.239 10.665 1.00 40.46 N ANISOU 2770 N GLU B 161 4545 6215 4613 -941 431 -892 N ATOM 2771 CA GLU B 161 -45.164 113.565 10.514 1.00 40.72 C ANISOU 2771 CA GLU B 161 4888 6175 4407 -1034 498 -738 C ATOM 2772 C GLU B 161 -45.999 113.847 11.753 1.00 38.50 C ANISOU 2772 C GLU B 161 4629 5865 4132 -864 292 -540 C ATOM 2773 O GLU B 161 -46.845 113.030 12.131 1.00 37.36 O ANISOU 2773 O GLU B 161 4438 5717 4040 -697 129 -433 O ATOM 2774 CB GLU B 161 -46.051 113.631 9.274 1.00 41.49 C ANISOU 2774 CB GLU B 161 5289 6195 4280 -1067 534 -637 C ATOM 2775 CG GLU B 161 -45.350 113.592 7.910 1.00 44.35 C ANISOU 2775 CG GLU B 161 5775 6544 4533 -1297 787 -813 C ATOM 2776 CD GLU B 161 -44.421 114.765 7.620 1.00 47.05 C ANISOU 2776 CD GLU B 161 6281 6848 4749 -1585 1059 -943 C ATOM 2777 OE1 GLU B 161 -44.557 115.794 8.297 1.00 47.44 O ANISOU 2777 OE1 GLU B 161 6447 6849 4729 -1590 1017 -839 O ATOM 2778 OE2 GLU B 161 -43.555 114.673 6.709 1.00 50.31 O ANISOU 2778 OE2 GLU B 161 6718 7272 5126 -1831 1341 -1169 O ATOM 2779 N THR B 162 -45.764 114.999 12.370 1.00 37.87 N ANISOU 2779 N THR B 162 4634 5760 3994 -933 328 -512 N ATOM 2780 CA THR B 162 -46.393 115.347 13.635 1.00 36.68 C ANISOU 2780 CA THR B 162 4500 5584 3854 -804 172 -365 C ATOM 2781 C THR B 162 -46.984 116.747 13.540 1.00 35.91 C ANISOU 2781 C THR B 162 4685 5398 3563 -856 216 -250 C ATOM 2782 O THR B 162 -46.348 117.646 12.994 1.00 36.64 O ANISOU 2782 O THR B 162 4926 5452 3544 -1036 374 -318 O ATOM 2783 CB THR B 162 -45.366 115.255 14.779 1.00 37.65 C ANISOU 2783 CB THR B 162 4410 5752 4141 -800 112 -477 C ATOM 2784 OG1 THR B 162 -44.864 113.912 14.848 1.00 38.00 O ANISOU 2784 OG1 THR B 162 4225 5842 4371 -708 10 -594 O ATOM 2785 CG2 THR B 162 -45.990 115.635 16.121 1.00 36.72 C ANISOU 2785 CG2 THR B 162 4367 5590 3994 -698 -27 -329 C ATOM 2786 N THR B 163 -48.199 116.918 14.064 1.00 33.98 N ANISOU 2786 N THR B 163 4522 5107 3284 -708 84 -103 N ATOM 2787 CA THR B 163 -48.877 118.204 14.022 1.00 33.80 C ANISOU 2787 CA THR B 163 4755 4980 3109 -701 72 -13 C ATOM 2788 C THR B 163 -48.548 119.000 15.272 1.00 33.51 C ANISOU 2788 C THR B 163 4700 4937 3093 -723 77 1 C ATOM 2789 O THR B 163 -48.425 118.435 16.374 1.00 32.27 O ANISOU 2789 O THR B 163 4364 4838 3059 -665 16 -1 O ATOM 2790 CB THR B 163 -50.409 118.066 13.920 1.00 33.64 C ANISOU 2790 CB THR B 163 4788 4912 3084 -518 -78 73 C ATOM 2791 OG1 THR B 163 -50.907 117.249 14.987 1.00 32.88 O ANISOU 2791 OG1 THR B 163 4475 4882 3138 -419 -139 88 O ATOM 2792 CG2 THR B 163 -50.804 117.467 12.592 1.00 34.66 C ANISOU 2792 CG2 THR B 163 4990 5020 3159 -495 -116 58 C ATOM 2793 N LYS B 164 -48.446 120.313 15.092 1.00 33.89 N ANISOU 2793 N LYS B 164 4990 4889 2997 -809 137 21 N ATOM 2794 CA LYS B 164 -48.269 121.242 16.193 1.00 34.32 C ANISOU 2794 CA LYS B 164 5081 4915 3045 -829 140 40 C ATOM 2795 C LYS B 164 -49.534 121.170 17.067 1.00 33.12 C ANISOU 2795 C LYS B 164 4891 4747 2946 -638 11 125 C ATOM 2796 O LYS B 164 -50.641 121.103 16.525 1.00 32.14 O ANISOU 2796 O LYS B 164 4832 4574 2806 -511 -73 160 O ATOM 2797 CB LYS B 164 -48.083 122.651 15.643 1.00 36.16 C ANISOU 2797 CB LYS B 164 5644 5010 3085 -955 225 51 C ATOM 2798 CG LYS B 164 -47.593 123.661 16.661 1.00 37.12 C ANISOU 2798 CG LYS B 164 5809 5103 3193 -1035 268 39 C ATOM 2799 CD LYS B 164 -47.693 125.072 16.095 1.00 38.85 C ANISOU 2799 CD LYS B 164 6431 5136 3194 -1130 322 74 C ATOM 2800 CE LYS B 164 -47.456 126.100 17.186 1.00 39.46 C ANISOU 2800 CE LYS B 164 6564 5170 3260 -1171 339 76 C ATOM 2801 NZ LYS B 164 -46.001 126.214 17.456 1.00 40.54 N ANISOU 2801 NZ LYS B 164 6572 5388 3445 -1418 506 -63 N ATOM 2802 N PRO B 165 -49.382 121.164 18.410 1.00 32.94 N ANISOU 2802 N PRO B 165 4767 4759 2991 -628 -4 127 N ATOM 2803 CA PRO B 165 -50.594 121.074 19.239 1.00 32.26 C ANISOU 2803 CA PRO B 165 4657 4653 2946 -498 -62 169 C ATOM 2804 C PRO B 165 -51.564 122.217 18.981 1.00 33.00 C ANISOU 2804 C PRO B 165 4921 4638 2978 -411 -91 183 C ATOM 2805 O PRO B 165 -51.133 123.351 18.841 1.00 33.42 O ANISOU 2805 O PRO B 165 5165 4607 2924 -473 -66 192 O ATOM 2806 CB PRO B 165 -50.049 121.134 20.668 1.00 31.98 C ANISOU 2806 CB PRO B 165 4591 4635 2926 -552 -53 165 C ATOM 2807 CG PRO B 165 -48.674 120.594 20.559 1.00 32.26 C ANISOU 2807 CG PRO B 165 4520 4732 3004 -644 -65 107 C ATOM 2808 CD PRO B 165 -48.162 121.098 19.237 1.00 32.87 C ANISOU 2808 CD PRO B 165 4653 4803 3033 -732 17 65 C ATOM 2809 N SER B 166 -52.853 121.898 18.875 1.00 33.93 N ANISOU 2809 N SER B 166 4970 4748 3176 -266 -156 157 N ATOM 2810 CA SER B 166 -53.913 122.908 18.680 1.00 35.60 C ANISOU 2810 CA SER B 166 5294 4846 3387 -125 -243 116 C ATOM 2811 C SER B 166 -54.974 122.740 19.762 1.00 35.43 C ANISOU 2811 C SER B 166 5101 4854 3506 -50 -207 28 C ATOM 2812 O SER B 166 -55.214 121.623 20.219 1.00 34.00 O ANISOU 2812 O SER B 166 4741 4765 3410 -89 -138 4 O ATOM 2813 CB SER B 166 -54.561 122.751 17.308 1.00 36.69 C ANISOU 2813 CB SER B 166 5495 4927 3520 -3 -390 94 C ATOM 2814 OG SER B 166 -55.112 121.449 17.146 1.00 37.22 O ANISOU 2814 OG SER B 166 5323 5099 3718 38 -399 50 O ATOM 2815 N LYS B 167 -55.596 123.850 20.158 1.00 36.91 N ANISOU 2815 N LYS B 167 5365 4948 3711 41 -236 -38 N ATOM 2816 CA LYS B 167 -56.616 123.859 21.209 1.00 38.53 C ANISOU 2816 CA LYS B 167 5408 5173 4058 87 -153 -175 C ATOM 2817 C LYS B 167 -57.841 123.042 20.804 1.00 38.94 C ANISOU 2817 C LYS B 167 5216 5276 4302 197 -192 -325 C ATOM 2818 O LYS B 167 -58.329 123.168 19.685 1.00 38.84 O ANISOU 2818 O LYS B 167 5207 5212 4337 355 -383 -370 O ATOM 2819 CB LYS B 167 -57.081 125.286 21.519 1.00 40.75 C ANISOU 2819 CB LYS B 167 5808 5328 4349 199 -204 -256 C ATOM 2820 CG LYS B 167 -56.071 126.169 22.242 1.00 41.18 C ANISOU 2820 CG LYS B 167 6076 5331 4241 70 -124 -155 C ATOM 2821 CD LYS B 167 -56.401 126.366 23.718 1.00 42.10 C ANISOU 2821 CD LYS B 167 6131 5466 4399 3 43 -242 C ATOM 2822 CE LYS B 167 -55.950 127.730 24.212 1.00 43.20 C ANISOU 2822 CE LYS B 167 6493 5491 4430 -14 45 -219 C ATOM 2823 NZ LYS B 167 -56.475 128.021 25.575 1.00 44.45 N ANISOU 2823 NZ LYS B 167 6606 5648 4634 -58 206 -340 N ATOM 2824 N GLN B 168 -58.326 122.220 21.734 1.00 39.39 N ANISOU 2824 N GLN B 168 5095 5416 4453 96 -12 -414 N ATOM 2825 CA GLN B 168 -59.605 121.524 21.597 1.00 40.65 C ANISOU 2825 CA GLN B 168 4988 5629 4830 153 18 -623 C ATOM 2826 C GLN B 168 -60.725 122.483 21.994 1.00 43.38 C ANISOU 2826 C GLN B 168 5205 5920 5357 287 20 -873 C ATOM 2827 O GLN B 168 -60.463 123.579 22.507 1.00 43.90 O ANISOU 2827 O GLN B 168 5419 5907 5353 313 25 -855 O ATOM 2828 CB GLN B 168 -59.652 120.299 22.515 1.00 40.44 C ANISOU 2828 CB GLN B 168 4887 5680 4798 -64 259 -636 C ATOM 2829 CG GLN B 168 -58.557 119.260 22.303 1.00 38.79 C ANISOU 2829 CG GLN B 168 4795 5506 4436 -180 242 -424 C ATOM 2830 CD GLN B 168 -58.571 118.170 23.377 1.00 38.83 C ANISOU 2830 CD GLN B 168 4842 5525 4388 -391 447 -426 C ATOM 2831 OE1 GLN B 168 -58.822 118.447 24.544 1.00 40.13 O ANISOU 2831 OE1 GLN B 168 5088 5652 4509 -510 623 -491 O ATOM 2832 NE2 GLN B 168 -58.317 116.930 22.982 1.00 38.04 N ANISOU 2832 NE2 GLN B 168 4730 5452 4270 -446 423 -360 N ATOM 2833 N SER B 169 -61.972 122.058 21.798 1.00 45.21 N ANISOU 2833 N SER B 169 5139 6195 5843 367 25 -1140 N ATOM 2834 CA SER B 169 -63.134 122.854 22.218 1.00 48.08 C ANISOU 2834 CA SER B 169 5292 6522 6454 500 42 -1467 C ATOM 2835 C SER B 169 -63.221 123.078 23.733 1.00 48.61 C ANISOU 2835 C SER B 169 5364 6605 6501 296 383 -1560 C ATOM 2836 O SER B 169 -63.804 124.076 24.178 1.00 50.84 O ANISOU 2836 O SER B 169 5572 6828 6918 404 397 -1772 O ATOM 2837 CB SER B 169 -64.435 122.205 21.738 1.00 50.27 C ANISOU 2837 CB SER B 169 5183 6866 7052 594 3 -1795 C ATOM 2838 OG SER B 169 -64.442 122.048 20.334 1.00 49.95 O ANISOU 2838 OG SER B 169 5165 6791 7024 799 -344 -1731 O ATOM 2839 N ASN B 170 -62.657 122.157 24.519 1.00 47.02 N ANISOU 2839 N ASN B 170 5280 6460 6124 10 640 -1416 N ATOM 2840 CA ASN B 170 -62.618 122.298 25.990 1.00 47.40 C ANISOU 2840 CA ASN B 170 5445 6492 6073 -222 961 -1467 C ATOM 2841 C ASN B 170 -61.414 123.087 26.548 1.00 45.81 C ANISOU 2841 C ASN B 170 5589 6216 5600 -263 917 -1205 C ATOM 2842 O ASN B 170 -61.202 123.107 27.761 1.00 46.17 O ANISOU 2842 O ASN B 170 5805 6234 5503 -469 1147 -1199 O ATOM 2843 CB ASN B 170 -62.730 120.916 26.668 1.00 47.79 C ANISOU 2843 CB ASN B 170 5524 6589 6043 -525 1250 -1477 C ATOM 2844 CG ASN B 170 -61.485 120.054 26.500 1.00 45.21 C ANISOU 2844 CG ASN B 170 5468 6257 5455 -618 1145 -1127 C ATOM 2845 OD1 ASN B 170 -60.578 120.378 25.734 1.00 43.38 O ANISOU 2845 OD1 ASN B 170 5328 6017 5136 -468 881 -907 O ATOM 2846 ND2 ASN B 170 -61.447 118.932 27.215 1.00 45.51 N ANISOU 2846 ND2 ASN B 170 5646 6280 5365 -877 1359 -1102 N ATOM 2847 N ASN B 171 -60.631 123.713 25.664 1.00 44.12 N ANISOU 2847 N ASN B 171 5501 5960 5303 -92 634 -1007 N ATOM 2848 CA ASN B 171 -59.474 124.568 26.017 1.00 42.81 C ANISOU 2848 CA ASN B 171 5628 5724 4914 -124 572 -795 C ATOM 2849 C ASN B 171 -58.163 123.876 26.433 1.00 40.22 C ANISOU 2849 C ASN B 171 5512 5422 4348 -315 598 -543 C ATOM 2850 O ASN B 171 -57.163 124.559 26.675 1.00 39.33 O ANISOU 2850 O ASN B 171 5600 5263 4082 -345 533 -401 O ATOM 2851 CB ASN B 171 -59.861 125.688 27.017 1.00 44.74 C ANISOU 2851 CB ASN B 171 5928 5895 5177 -128 701 -944 C ATOM 2852 CG ASN B 171 -59.930 127.057 26.365 1.00 46.02 C ANISOU 2852 CG ASN B 171 6150 5946 5391 111 476 -972 C ATOM 2853 OD1 ASN B 171 -60.251 127.183 25.177 1.00 47.30 O ANISOU 2853 OD1 ASN B 171 6243 6075 5654 317 238 -994 O ATOM 2854 ND2 ASN B 171 -59.634 128.099 27.142 1.00 46.75 N ANISOU 2854 ND2 ASN B 171 6418 5954 5391 81 534 -972 N ATOM 2855 N LYS B 172 -58.148 122.543 26.468 1.00 39.03 N ANISOU 2855 N LYS B 172 5315 5332 4183 -429 664 -508 N ATOM 2856 CA LYS B 172 -56.897 121.781 26.508 1.00 36.77 C ANISOU 2856 CA LYS B 172 5187 5059 3726 -528 584 -292 C ATOM 2857 C LYS B 172 -56.406 121.560 25.074 1.00 34.90 C ANISOU 2857 C LYS B 172 4864 4865 3532 -401 383 -196 C ATOM 2858 O LYS B 172 -57.113 121.889 24.111 1.00 35.38 O ANISOU 2858 O LYS B 172 4790 4931 3723 -250 300 -279 O ATOM 2859 CB LYS B 172 -57.092 120.446 27.234 1.00 37.40 C ANISOU 2859 CB LYS B 172 5326 5139 3745 -706 727 -301 C ATOM 2860 CG LYS B 172 -57.462 120.619 28.703 1.00 39.32 C ANISOU 2860 CG LYS B 172 5755 5309 3877 -888 956 -388 C ATOM 2861 CD LYS B 172 -57.800 119.295 29.361 1.00 40.55 C ANISOU 2861 CD LYS B 172 6045 5422 3939 -1097 1123 -413 C ATOM 2862 CE LYS B 172 -58.501 119.514 30.687 1.00 43.22 C ANISOU 2862 CE LYS B 172 6561 5680 4179 -1314 1429 -567 C ATOM 2863 NZ LYS B 172 -58.813 118.215 31.340 1.00 44.87 N ANISOU 2863 NZ LYS B 172 6998 5807 4243 -1567 1617 -588 N ATOM 2864 N TYR B 173 -55.205 121.006 24.935 1.00 32.50 N ANISOU 2864 N TYR B 173 4648 4580 3122 -460 293 -46 N ATOM 2865 CA TYR B 173 -54.597 120.780 23.621 1.00 31.13 C ANISOU 2865 CA TYR B 173 4415 4446 2969 -386 149 26 C ATOM 2866 C TYR B 173 -54.689 119.324 23.150 1.00 30.28 C ANISOU 2866 C TYR B 173 4199 4393 2913 -399 131 37 C ATOM 2867 O TYR B 173 -54.788 118.384 23.947 1.00 29.36 O ANISOU 2867 O TYR B 173 4119 4268 2770 -494 199 36 O ATOM 2868 CB TYR B 173 -53.133 121.228 23.623 1.00 30.38 C ANISOU 2868 CB TYR B 173 4434 4343 2767 -443 76 121 C ATOM 2869 CG TYR B 173 -52.961 122.736 23.665 1.00 30.92 C ANISOU 2869 CG TYR B 173 4623 4346 2778 -429 76 117 C ATOM 2870 CD1 TYR B 173 -53.072 123.434 24.865 1.00 31.61 C ANISOU 2870 CD1 TYR B 173 4816 4382 2811 -478 147 92 C ATOM 2871 CD2 TYR B 173 -52.698 123.461 22.498 1.00 30.99 C ANISOU 2871 CD2 TYR B 173 4693 4321 2762 -384 13 135 C ATOM 2872 CE1 TYR B 173 -52.915 124.816 24.911 1.00 32.30 C ANISOU 2872 CE1 TYR B 173 5031 4395 2846 -466 145 84 C ATOM 2873 CE2 TYR B 173 -52.543 124.842 22.527 1.00 31.90 C ANISOU 2873 CE2 TYR B 173 4980 4339 2800 -385 11 135 C ATOM 2874 CZ TYR B 173 -52.651 125.516 23.733 1.00 32.54 C ANISOU 2874 CZ TYR B 173 5129 4380 2853 -417 72 109 C ATOM 2875 OH TYR B 173 -52.504 126.877 23.761 1.00 33.85 O ANISOU 2875 OH TYR B 173 5480 4437 2943 -417 66 105 O ATOM 2876 N ALA B 174 -54.615 119.166 21.836 1.00 29.56 N ANISOU 2876 N ALA B 174 4028 4334 2869 -315 35 50 N ATOM 2877 CA ALA B 174 -54.442 117.859 21.207 1.00 29.15 C ANISOU 2877 CA ALA B 174 3887 4332 2855 -323 -4 70 C ATOM 2878 C ALA B 174 -53.405 117.961 20.109 1.00 28.84 C ANISOU 2878 C ALA B 174 3867 4314 2776 -308 -93 124 C ATOM 2879 O ALA B 174 -53.214 119.030 19.518 1.00 28.17 O ANISOU 2879 O ALA B 174 3870 4194 2639 -281 -120 132 O ATOM 2880 CB ALA B 174 -55.760 117.378 20.633 1.00 29.91 C ANISOU 2880 CB ALA B 174 3836 4450 3077 -253 7 -33 C ATOM 2881 N ALA B 175 -52.746 116.838 19.839 1.00 28.70 N ANISOU 2881 N ALA B 175 3791 4336 2778 -340 -125 142 N ATOM 2882 CA ALA B 175 -51.793 116.724 18.745 1.00 29.00 C ANISOU 2882 CA ALA B 175 3809 4407 2805 -353 -163 142 C ATOM 2883 C ALA B 175 -51.875 115.329 18.158 1.00 29.34 C ANISOU 2883 C ALA B 175 3744 4487 2917 -331 -196 123 C ATOM 2884 O ALA B 175 -52.455 114.417 18.762 1.00 29.42 O ANISOU 2884 O ALA B 175 3721 4487 2969 -325 -196 124 O ATOM 2885 CB ALA B 175 -50.376 117.014 19.234 1.00 29.32 C ANISOU 2885 CB ALA B 175 3864 4454 2820 -433 -169 131 C ATOM 2886 N SER B 176 -51.311 115.176 16.968 1.00 30.27 N ANISOU 2886 N SER B 176 3839 4633 3028 -341 -202 96 N ATOM 2887 CA SER B 176 -51.358 113.912 16.256 1.00 31.21 C ANISOU 2887 CA SER B 176 3864 4784 3210 -318 -230 66 C ATOM 2888 C SER B 176 -50.013 113.639 15.605 1.00 32.12 C ANISOU 2888 C SER B 176 3926 4937 3344 -378 -207 -6 C ATOM 2889 O SER B 176 -49.311 114.564 15.185 1.00 32.61 O ANISOU 2889 O SER B 176 4047 4999 3343 -459 -135 -41 O ATOM 2890 CB SER B 176 -52.477 113.931 15.206 1.00 31.82 C ANISOU 2890 CB SER B 176 3964 4853 3275 -256 -255 59 C ATOM 2891 OG SER B 176 -52.216 114.873 14.178 1.00 33.45 O ANISOU 2891 OG SER B 176 4313 5025 3370 -276 -250 57 O ATOM 2892 N SER B 177 -49.649 112.365 15.551 1.00 32.80 N ANISOU 2892 N SER B 177 3900 5042 3522 -351 -255 -53 N ATOM 2893 CA SER B 177 -48.454 111.936 14.839 1.00 33.80 C ANISOU 2893 CA SER B 177 3917 5209 3715 -393 -227 -181 C ATOM 2894 C SER B 177 -48.777 110.734 13.973 1.00 34.61 C ANISOU 2894 C SER B 177 3964 5322 3865 -352 -245 -213 C ATOM 2895 O SER B 177 -49.548 109.844 14.379 1.00 34.37 O ANISOU 2895 O SER B 177 3935 5258 3865 -282 -324 -155 O ATOM 2896 CB SER B 177 -47.330 111.606 15.811 1.00 34.47 C ANISOU 2896 CB SER B 177 3890 5291 3915 -372 -320 -268 C ATOM 2897 OG SER B 177 -46.099 111.537 15.122 1.00 35.68 O ANISOU 2897 OG SER B 177 3888 5501 4169 -433 -258 -458 O ATOM 2898 N TYR B 178 -48.194 110.723 12.778 1.00 35.95 N ANISOU 2898 N TYR B 178 4108 5528 4024 -423 -145 -318 N ATOM 2899 CA TYR B 178 -48.410 109.669 11.803 1.00 37.62 C ANISOU 2899 CA TYR B 178 4283 5749 4264 -401 -142 -367 C ATOM 2900 C TYR B 178 -47.068 109.036 11.467 1.00 38.81 C ANISOU 2900 C TYR B 178 4255 5939 4552 -436 -93 -570 C ATOM 2901 O TYR B 178 -46.098 109.742 11.204 1.00 39.19 O ANISOU 2901 O TYR B 178 4258 6023 4608 -554 40 -701 O ATOM 2902 CB TYR B 178 -49.055 110.236 10.534 1.00 38.89 C ANISOU 2902 CB TYR B 178 4626 5891 4258 -463 -67 -334 C ATOM 2903 CG TYR B 178 -50.240 111.159 10.793 1.00 39.38 C ANISOU 2903 CG TYR B 178 4845 5905 4213 -412 -138 -195 C ATOM 2904 CD1 TYR B 178 -50.064 112.544 10.859 1.00 40.90 C ANISOU 2904 CD1 TYR B 178 5198 6058 4285 -476 -86 -162 C ATOM 2905 CD2 TYR B 178 -51.529 110.659 10.988 1.00 40.04 C ANISOU 2905 CD2 TYR B 178 4905 5974 4336 -304 -253 -133 C ATOM 2906 CE1 TYR B 178 -51.132 113.405 11.098 1.00 41.31 C ANISOU 2906 CE1 TYR B 178 5382 6049 4264 -398 -178 -67 C ATOM 2907 CE2 TYR B 178 -52.610 111.516 11.231 1.00 40.67 C ANISOU 2907 CE2 TYR B 178 5069 6012 4369 -240 -324 -72 C ATOM 2908 CZ TYR B 178 -52.409 112.890 11.279 1.00 41.67 C ANISOU 2908 CZ TYR B 178 5356 6092 4384 -269 -303 -38 C ATOM 2909 OH TYR B 178 -53.473 113.757 11.504 1.00 42.89 O ANISOU 2909 OH TYR B 178 5590 6190 4517 -174 -402 -6 O ATOM 2910 N LEU B 179 -47.012 107.709 11.532 1.00 39.73 N ANISOU 2910 N LEU B 179 4263 6039 4794 -336 -198 -621 N ATOM 2911 CA LEU B 179 -45.885 106.943 11.017 1.00 41.62 C ANISOU 2911 CA LEU B 179 4310 6307 5196 -336 -167 -854 C ATOM 2912 C LEU B 179 -46.370 106.211 9.774 1.00 41.98 C ANISOU 2912 C LEU B 179 4405 6355 5189 -360 -93 -875 C ATOM 2913 O LEU B 179 -47.259 105.357 9.867 1.00 41.20 O ANISOU 2913 O LEU B 179 4364 6208 5081 -269 -209 -765 O ATOM 2914 CB LEU B 179 -45.377 105.948 12.066 1.00 42.52 C ANISOU 2914 CB LEU B 179 4300 6360 5495 -171 -400 -916 C ATOM 2915 CG LEU B 179 -44.258 104.987 11.643 1.00 44.66 C ANISOU 2915 CG LEU B 179 4337 6637 5993 -104 -441 -1196 C ATOM 2916 CD1 LEU B 179 -43.095 105.729 10.995 1.00 46.37 C ANISOU 2916 CD1 LEU B 179 4351 6960 6306 -249 -227 -1465 C ATOM 2917 CD2 LEU B 179 -43.782 104.179 12.843 1.00 45.60 C ANISOU 2917 CD2 LEU B 179 4409 6646 6271 96 -756 -1242 C ATOM 2918 N SER B 180 -45.814 106.569 8.618 1.00 43.08 N ANISOU 2918 N SER B 180 4551 6541 5277 -511 119 -1023 N ATOM 2919 CA SER B 180 -46.193 105.953 7.345 1.00 44.21 C ANISOU 2919 CA SER B 180 4784 6676 5337 -559 204 -1060 C ATOM 2920 C SER B 180 -45.245 104.815 7.006 1.00 46.00 C ANISOU 2920 C SER B 180 4777 6926 5777 -526 234 -1317 C ATOM 2921 O SER B 180 -44.036 105.023 6.940 1.00 47.86 O ANISOU 2921 O SER B 180 4821 7212 6152 -605 366 -1568 O ATOM 2922 CB SER B 180 -46.156 106.992 6.231 1.00 45.30 C ANISOU 2922 CB SER B 180 5158 6811 5242 -770 428 -1080 C ATOM 2923 OG SER B 180 -47.073 108.032 6.512 1.00 44.90 O ANISOU 2923 OG SER B 180 5339 6714 5008 -761 352 -859 O ATOM 2924 N LEU B 181 -45.799 103.621 6.806 1.00 46.03 N ANISOU 2924 N LEU B 181 4779 6886 5824 -411 111 -1282 N ATOM 2925 CA LEU B 181 -45.029 102.423 6.472 1.00 47.71 C ANISOU 2925 CA LEU B 181 4791 7093 6245 -342 100 -1522 C ATOM 2926 C LEU B 181 -45.619 101.754 5.238 1.00 48.29 C ANISOU 2926 C LEU B 181 4994 7150 6204 -397 185 -1527 C ATOM 2927 O LEU B 181 -46.738 102.065 4.830 1.00 46.47 O ANISOU 2927 O LEU B 181 4997 6900 5760 -441 172 -1324 O ATOM 2928 CB LEU B 181 -45.076 101.425 7.632 1.00 47.48 C ANISOU 2928 CB LEU B 181 4676 6975 6389 -117 -194 -1476 C ATOM 2929 CG LEU B 181 -44.705 101.926 9.028 1.00 46.78 C ANISOU 2929 CG LEU B 181 4538 6858 6376 -29 -361 -1424 C ATOM 2930 CD1 LEU B 181 -45.035 100.863 10.065 1.00 46.56 C ANISOU 2930 CD1 LEU B 181 4588 6685 6415 163 -658 -1324 C ATOM 2931 CD2 LEU B 181 -43.230 102.307 9.093 1.00 49.28 C ANISOU 2931 CD2 LEU B 181 4578 7239 6906 -43 -304 -1734 C ATOM 2932 N THR B 182 -44.860 100.835 4.649 1.00 50.69 N ANISOU 2932 N THR B 182 5135 7458 6668 -383 252 -1785 N ATOM 2933 CA THR B 182 -45.427 99.890 3.691 1.00 51.31 C ANISOU 2933 CA THR B 182 5318 7499 6680 -386 267 -1792 C ATOM 2934 C THR B 182 -46.038 98.744 4.502 1.00 50.86 C ANISOU 2934 C THR B 182 5245 7346 6734 -176 -18 -1666 C ATOM 2935 O THR B 182 -45.618 98.511 5.643 1.00 49.87 O ANISOU 2935 O THR B 182 5002 7171 6774 -30 -202 -1672 O ATOM 2936 CB THR B 182 -44.376 99.321 2.723 1.00 53.93 C ANISOU 2936 CB THR B 182 5489 7861 7142 -466 477 -2147 C ATOM 2937 OG1 THR B 182 -43.424 98.528 3.446 1.00 55.38 O ANISOU 2937 OG1 THR B 182 5355 8023 7665 -279 333 -2375 O ATOM 2938 CG2 THR B 182 -43.658 100.444 1.975 1.00 55.52 C ANISOU 2938 CG2 THR B 182 5732 8139 7225 -734 821 -2315 C ATOM 2939 N PRO B 183 -47.036 98.031 3.931 1.00 51.35 N ANISOU 2939 N PRO B 183 5461 7362 6690 -174 -64 -1560 N ATOM 2940 CA PRO B 183 -47.600 96.850 4.611 1.00 51.67 C ANISOU 2940 CA PRO B 183 5524 7288 6820 -25 -288 -1470 C ATOM 2941 C PRO B 183 -46.561 95.805 5.038 1.00 54.34 C ANISOU 2941 C PRO B 183 5696 7538 7413 138 -417 -1680 C ATOM 2942 O PRO B 183 -46.707 95.187 6.100 1.00 53.98 O ANISOU 2942 O PRO B 183 5708 7363 7438 276 -646 -1592 O ATOM 2943 CB PRO B 183 -48.540 96.259 3.558 1.00 51.48 C ANISOU 2943 CB PRO B 183 5641 7250 6668 -93 -250 -1433 C ATOM 2944 CG PRO B 183 -48.955 97.427 2.740 1.00 50.86 C ANISOU 2944 CG PRO B 183 5695 7258 6371 -243 -106 -1368 C ATOM 2945 CD PRO B 183 -47.745 98.315 2.668 1.00 51.54 C ANISOU 2945 CD PRO B 183 5685 7413 6484 -320 68 -1515 C ATOM 2946 N GLU B 184 -45.524 95.630 4.218 1.00 57.94 N ANISOU 2946 N GLU B 184 5970 8045 7998 117 -272 -1977 N ATOM 2947 CA GLU B 184 -44.441 94.687 4.509 1.00 61.22 C ANISOU 2947 CA GLU B 184 6171 8379 8709 301 -410 -2255 C ATOM 2948 C GLU B 184 -43.619 95.105 5.725 1.00 62.11 C ANISOU 2948 C GLU B 184 6134 8468 8997 439 -594 -2317 C ATOM 2949 O GLU B 184 -43.296 94.268 6.568 1.00 63.41 O ANISOU 2949 O GLU B 184 6293 8476 9326 662 -900 -2364 O ATOM 2950 CB GLU B 184 -43.519 94.524 3.293 1.00 64.41 C ANISOU 2950 CB GLU B 184 6372 8868 9234 213 -154 -2620 C ATOM 2951 CG GLU B 184 -44.184 93.820 2.120 1.00 65.50 C ANISOU 2951 CG GLU B 184 6670 8988 9231 120 -31 -2609 C ATOM 2952 CD GLU B 184 -43.424 93.991 0.813 1.00 68.47 C ANISOU 2952 CD GLU B 184 6934 9462 9617 -64 317 -2933 C ATOM 2953 OE1 GLU B 184 -43.137 95.148 0.429 1.00 68.99 O ANISOU 2953 OE1 GLU B 184 7020 9639 9554 -276 575 -2969 O ATOM 2954 OE2 GLU B 184 -43.121 92.968 0.162 1.00 70.68 O ANISOU 2954 OE2 GLU B 184 7141 9694 10020 -17 352 -3160 O ATOM 2955 N GLN B 185 -43.276 96.393 5.802 1.00 62.21 N ANISOU 2955 N GLN B 185 6064 8613 8960 305 -429 -2325 N ATOM 2956 CA GLN B 185 -42.598 96.953 6.983 1.00 62.96 C ANISOU 2956 CA GLN B 185 6036 8696 9189 411 -603 -2360 C ATOM 2957 C GLN B 185 -43.414 96.729 8.253 1.00 61.42 C ANISOU 2957 C GLN B 185 6103 8356 8880 535 -898 -2038 C ATOM 2958 O GLN B 185 -42.881 96.303 9.281 1.00 62.34 O ANISOU 2958 O GLN B 185 6204 8338 9144 735 -1204 -2096 O ATOM 2959 CB GLN B 185 -42.345 98.453 6.817 1.00 62.73 C ANISOU 2959 CB GLN B 185 5951 8824 9060 200 -344 -2361 C ATOM 2960 CG GLN B 185 -41.206 98.802 5.877 1.00 65.65 C ANISOU 2960 CG GLN B 185 6043 9319 9584 49 -41 -2757 C ATOM 2961 CD GLN B 185 -41.105 100.294 5.616 1.00 65.42 C ANISOU 2961 CD GLN B 185 6069 9409 9380 -215 252 -2720 C ATOM 2962 OE1 GLN B 185 -42.112 100.972 5.414 1.00 63.37 O ANISOU 2962 OE1 GLN B 185 6117 9153 8809 -339 329 -2404 O ATOM 2963 NE2 GLN B 185 -39.882 100.813 5.612 1.00 68.37 N ANISOU 2963 NE2 GLN B 185 6144 9869 9966 -304 408 -3073 N ATOM 2964 N TRP B 186 -44.708 97.030 8.159 1.00 58.89 N ANISOU 2964 N TRP B 186 6035 8048 8292 405 -805 -1727 N ATOM 2965 CA TRP B 186 -45.658 96.822 9.255 1.00 57.78 C ANISOU 2965 CA TRP B 186 6161 7778 8015 449 -992 -1441 C ATOM 2966 C TRP B 186 -45.655 95.367 9.754 1.00 59.85 C ANISOU 2966 C TRP B 186 6563 7819 8358 620 -1260 -1460 C ATOM 2967 O TRP B 186 -45.565 95.129 10.961 1.00 61.09 O ANISOU 2967 O TRP B 186 6891 7813 8509 731 -1509 -1378 O ATOM 2968 CB TRP B 186 -47.067 97.264 8.814 1.00 55.02 C ANISOU 2968 CB TRP B 186 5981 7496 7427 278 -818 -1201 C ATOM 2969 CG TRP B 186 -48.181 96.797 9.688 1.00 53.44 C ANISOU 2969 CG TRP B 186 6027 7168 7109 273 -931 -978 C ATOM 2970 CD1 TRP B 186 -49.197 95.967 9.333 1.00 53.04 C ANISOU 2970 CD1 TRP B 186 6109 7056 6987 219 -912 -903 C ATOM 2971 CD2 TRP B 186 -48.399 97.135 11.061 1.00 53.21 C ANISOU 2971 CD2 TRP B 186 6153 7050 7014 287 -1047 -829 C ATOM 2972 NE1 TRP B 186 -50.040 95.762 10.397 1.00 52.37 N ANISOU 2972 NE1 TRP B 186 6241 6853 6803 175 -977 -734 N ATOM 2973 CE2 TRP B 186 -49.572 96.465 11.474 1.00 52.79 C ANISOU 2973 CE2 TRP B 186 6333 6881 6843 214 -1056 -679 C ATOM 2974 CE3 TRP B 186 -47.719 97.937 11.983 1.00 53.24 C ANISOU 2974 CE3 TRP B 186 6133 7057 7040 335 -1131 -824 C ATOM 2975 CZ2 TRP B 186 -50.082 96.572 12.772 1.00 52.74 C ANISOU 2975 CZ2 TRP B 186 6562 6754 6723 165 -1114 -530 C ATOM 2976 CZ3 TRP B 186 -48.226 98.042 13.281 1.00 53.20 C ANISOU 2976 CZ3 TRP B 186 6372 6929 6914 315 -1229 -654 C ATOM 2977 CH2 TRP B 186 -49.396 97.362 13.659 1.00 52.80 C ANISOU 2977 CH2 TRP B 186 6576 6757 6728 221 -1204 -511 C ATOM 2978 N LYS B 187 -45.735 94.417 8.821 1.00 61.23 N ANISOU 2978 N LYS B 187 6712 7967 8586 634 -1216 -1572 N ATOM 2979 CA LYS B 187 -45.739 92.980 9.146 1.00 63.10 C ANISOU 2979 CA LYS B 187 7115 7970 8891 790 -1463 -1604 C ATOM 2980 C LYS B 187 -44.378 92.417 9.576 1.00 66.09 C ANISOU 2980 C LYS B 187 7352 8218 9541 1051 -1752 -1882 C ATOM 2981 O LYS B 187 -44.331 91.444 10.332 1.00 67.76 O ANISOU 2981 O LYS B 187 7806 8168 9772 1219 -2066 -1857 O ATOM 2982 CB LYS B 187 -46.254 92.147 7.958 1.00 63.61 C ANISOU 2982 CB LYS B 187 7190 8046 8934 722 -1324 -1655 C ATOM 2983 CG LYS B 187 -47.774 92.061 7.840 1.00 62.28 C ANISOU 2983 CG LYS B 187 7255 7876 8532 541 -1207 -1395 C ATOM 2984 CD LYS B 187 -48.241 90.937 6.856 1.00 63.57 C ANISOU 2984 CD LYS B 187 7475 7984 8694 511 -1159 -1462 C ATOM 2985 CE LYS B 187 -47.756 89.577 7.289 1.00 65.96 C ANISOU 2985 CE LYS B 187 7916 8030 9118 692 -1414 -1563 C ATOM 2986 NZ LYS B 187 -48.685 88.465 6.964 1.00 66.39 N ANISOU 2986 NZ LYS B 187 8195 7948 9082 615 -1410 -1494 N ATOM 2987 N SER B 188 -43.286 92.996 9.078 1.00 67.17 N ANISOU 2987 N SER B 188 7115 8515 9891 1081 -1654 -2173 N ATOM 2988 CA SER B 188 -41.941 92.483 9.364 1.00 70.34 C ANISOU 2988 CA SER B 188 7281 8819 10626 1345 -1928 -2532 C ATOM 2989 C SER B 188 -41.541 92.629 10.835 1.00 71.13 C ANISOU 2989 C SER B 188 7519 8749 10759 1533 -2318 -2475 C ATOM 2990 O SER B 188 -40.890 91.739 11.387 1.00 74.75 O ANISOU 2990 O SER B 188 8026 8975 11400 1814 -2720 -2646 O ATOM 2991 CB SER B 188 -40.896 93.161 8.468 1.00 71.96 C ANISOU 2991 CB SER B 188 7018 9260 11065 1271 -1660 -2907 C ATOM 2992 OG SER B 188 -40.821 94.552 8.726 1.00 71.23 O ANISOU 2992 OG SER B 188 6841 9340 10881 1103 -1479 -2826 O ATOM 2993 N HIS B 189 -41.932 93.741 11.461 1.00 68.34 N ANISOU 2993 N HIS B 189 7257 8489 10221 1388 -2224 -2246 N ATOM 2994 CA HIS B 189 -41.565 94.028 12.855 1.00 68.50 C ANISOU 2994 CA HIS B 189 7432 8360 10234 1532 -2567 -2185 C ATOM 2995 C HIS B 189 -42.556 93.447 13.862 1.00 67.09 C ANISOU 2995 C HIS B 189 7813 7915 9761 1531 -2767 -1835 C ATOM 2996 O HIS B 189 -43.751 93.348 13.585 1.00 65.32 O ANISOU 2996 O HIS B 189 7808 7714 9297 1325 -2525 -1577 O ATOM 2997 CB HIS B 189 -41.423 95.537 13.076 1.00 67.16 C ANISOU 2997 CB HIS B 189 7092 8410 10015 1369 -2359 -2140 C ATOM 2998 CG HIS B 189 -40.195 96.122 12.455 1.00 69.06 C ANISOU 2998 CG HIS B 189 6826 8849 10565 1379 -2235 -2539 C ATOM 2999 ND1 HIS B 189 -38.964 96.095 13.073 1.00 72.25 N ANISOU 2999 ND1 HIS B 189 6987 9191 11274 1608 -2560 -2866 N ATOM 3000 CD2 HIS B 189 -40.006 96.743 11.267 1.00 68.64 C ANISOU 3000 CD2 HIS B 189 6479 9041 10560 1166 -1811 -2695 C ATOM 3001 CE1 HIS B 189 -38.071 96.681 12.296 1.00 73.82 C ANISOU 3001 CE1 HIS B 189 6712 9611 11724 1516 -2303 -3230 C ATOM 3002 NE2 HIS B 189 -38.679 97.085 11.194 1.00 71.57 N ANISOU 3002 NE2 HIS B 189 6424 9505 11264 1231 -1831 -3120 N ATOM 3003 N ARG B 190 -42.040 93.084 15.035 1.00 68.91 N ANISOU 3003 N ARG B 190 8287 7883 10012 1750 -3211 -1855 N ATOM 3004 CA ARG B 190 -42.849 92.523 16.128 1.00 68.80 C ANISOU 3004 CA ARG B 190 8894 7560 9686 1727 -3415 -1550 C ATOM 3005 C ARG B 190 -43.773 93.560 16.776 1.00 65.11 C ANISOU 3005 C ARG B 190 8629 7190 8922 1460 -3166 -1239 C ATOM 3006 O ARG B 190 -44.914 93.243 17.116 1.00 64.47 O ANISOU 3006 O ARG B 190 8946 6992 8559 1272 -3034 -977 O ATOM 3007 CB ARG B 190 -41.954 91.866 17.205 1.00 73.45 C ANISOU 3007 CB ARG B 190 9759 7795 10352 2052 -4015 -1676 C ATOM 3008 CG ARG B 190 -41.925 90.350 17.166 1.00 76.55 C ANISOU 3008 CG ARG B 190 10482 7847 10757 2243 -4329 -1731 C ATOM 3009 CD ARG B 190 -40.581 89.827 17.636 1.00 81.58 C ANISOU 3009 CD ARG B 190 11065 8245 11686 2667 -4932 -2063 C ATOM 3010 NE ARG B 190 -39.398 90.339 16.924 1.00 82.99 N ANISOU 3010 NE ARG B 190 10506 8703 12324 2829 -4918 -2496 N ATOM 3011 CZ ARG B 190 -38.137 90.071 17.272 1.00 87.31 C ANISOU 3011 CZ ARG B 190 10845 9109 13219 3205 -5424 -2880 C ATOM 3012 NH1 ARG B 190 -37.870 89.294 18.321 1.00 91.40 N ANISOU 3012 NH1 ARG B 190 11884 9185 13657 3496 -6048 -2861 N ATOM 3013 NH2 ARG B 190 -37.129 90.581 16.568 1.00 88.34 N ANISOU 3013 NH2 ARG B 190 10258 9527 13781 3285 -5315 -3313 N ATOM 3014 N SER B 191 -43.287 94.791 16.928 1.00 62.98 N ANISOU 3014 N SER B 191 8070 7130 8729 1431 -3081 -1300 N ATOM 3015 CA SER B 191 -44.017 95.830 17.676 1.00 60.34 C ANISOU 3015 CA SER B 191 7924 6863 8140 1222 -2901 -1042 C ATOM 3016 C SER B 191 -43.646 97.245 17.214 1.00 57.79 C ANISOU 3016 C SER B 191 7163 6865 7931 1124 -2641 -1129 C ATOM 3017 O SER B 191 -42.582 97.472 16.620 1.00 58.89 O ANISOU 3017 O SER B 191 6886 7139 8350 1233 -2668 -1419 O ATOM 3018 CB SER B 191 -43.814 95.662 19.195 1.00 62.29 C ANISOU 3018 CB SER B 191 8642 6803 8221 1325 -3286 -942 C ATOM 3019 OG SER B 191 -42.502 96.027 19.586 1.00 64.29 O ANISOU 3019 OG SER B 191 8673 7048 8705 1561 -3621 -1186 O ATOM 3020 N TYR B 192 -44.565 98.176 17.456 1.00 54.89 N ANISOU 3020 N TYR B 192 6900 6611 7345 901 -2366 -897 N ATOM 3021 CA TYR B 192 -44.361 99.599 17.185 1.00 52.63 C ANISOU 3021 CA TYR B 192 6322 6580 7096 787 -2131 -926 C ATOM 3022 C TYR B 192 -44.890 100.410 18.360 1.00 50.92 C ANISOU 3022 C TYR B 192 6381 6312 6657 685 -2126 -714 C ATOM 3023 O TYR B 192 -45.946 100.086 18.903 1.00 51.27 O ANISOU 3023 O TYR B 192 6775 6230 6474 575 -2068 -502 O ATOM 3024 CB TYR B 192 -45.091 100.024 15.907 1.00 50.23 C ANISOU 3024 CB TYR B 192 5827 6499 6758 605 -1737 -882 C ATOM 3025 CG TYR B 192 -44.374 99.678 14.629 1.00 50.99 C ANISOU 3025 CG TYR B 192 5590 6712 7070 650 -1651 -1134 C ATOM 3026 CD1 TYR B 192 -43.455 100.561 14.064 1.00 51.59 C ANISOU 3026 CD1 TYR B 192 5334 6970 7299 608 -1510 -1348 C ATOM 3027 CD2 TYR B 192 -44.624 98.472 13.966 1.00 51.79 C ANISOU 3027 CD2 TYR B 192 5728 6737 7215 703 -1676 -1178 C ATOM 3028 CE1 TYR B 192 -42.794 100.249 12.882 1.00 52.83 C ANISOU 3028 CE1 TYR B 192 5204 7228 7639 603 -1374 -1614 C ATOM 3029 CE2 TYR B 192 -43.972 98.153 12.781 1.00 52.80 C ANISOU 3029 CE2 TYR B 192 5562 6969 7532 727 -1569 -1430 C ATOM 3030 CZ TYR B 192 -43.056 99.042 12.244 1.00 53.33 C ANISOU 3030 CZ TYR B 192 5303 7216 7742 670 -1406 -1655 C ATOM 3031 OH TYR B 192 -42.397 98.727 11.078 1.00 54.99 O ANISOU 3031 OH TYR B 192 5242 7523 8128 652 -1249 -1938 O ATOM 3032 N SER B 193 -44.175 101.469 18.731 1.00 49.40 N ANISOU 3032 N SER B 193 6022 6216 6530 695 -2154 -795 N ATOM 3033 CA SER B 193 -44.564 102.304 19.870 1.00 48.26 C ANISOU 3033 CA SER B 193 6129 6023 6185 606 -2158 -620 C ATOM 3034 C SER B 193 -44.612 103.787 19.519 1.00 45.97 C ANISOU 3034 C SER B 193 5601 5971 5896 460 -1872 -612 C ATOM 3035 O SER B 193 -43.825 104.257 18.694 1.00 45.56 O ANISOU 3035 O SER B 193 5194 6084 6032 465 -1781 -807 O ATOM 3036 CB SER B 193 -43.599 102.085 21.036 1.00 50.75 C ANISOU 3036 CB SER B 193 6613 6135 6535 790 -2588 -713 C ATOM 3037 OG SER B 193 -43.841 100.840 21.656 1.00 52.59 O ANISOU 3037 OG SER B 193 7269 6070 6643 886 -2861 -634 O ATOM 3038 N CYS B 194 -45.566 104.496 20.131 1.00 44.18 N ANISOU 3038 N CYS B 194 5593 5743 5451 315 -1714 -404 N ATOM 3039 CA CYS B 194 -45.634 105.955 20.105 1.00 42.74 C ANISOU 3039 CA CYS B 194 5286 5721 5233 198 -1510 -375 C ATOM 3040 C CYS B 194 -45.329 106.449 21.515 1.00 43.27 C ANISOU 3040 C CYS B 194 5576 5669 5196 214 -1692 -327 C ATOM 3041 O CYS B 194 -46.056 106.125 22.449 1.00 43.39 O ANISOU 3041 O CYS B 194 5951 5524 5011 167 -1732 -172 O ATOM 3042 CB CYS B 194 -47.025 106.440 19.693 1.00 40.93 C ANISOU 3042 CB CYS B 194 5118 5575 4859 43 -1206 -209 C ATOM 3043 SG CYS B 194 -47.177 108.248 19.688 1.00 39.95 S ANISOU 3043 SG CYS B 194 4908 5598 4675 -73 -996 -168 S ATOM 3044 N GLN B 195 -44.269 107.242 21.647 1.00 43.55 N ANISOU 3044 N GLN B 195 5409 5780 5358 253 -1777 -478 N ATOM 3045 CA GLN B 195 -43.787 107.713 22.938 1.00 45.04 C ANISOU 3045 CA GLN B 195 5780 5858 5474 289 -2001 -475 C ATOM 3046 C GLN B 195 -44.003 109.225 23.047 1.00 43.08 C ANISOU 3046 C GLN B 195 5471 5746 5151 136 -1759 -417 C ATOM 3047 O GLN B 195 -43.437 109.989 22.269 1.00 41.94 O ANISOU 3047 O GLN B 195 5018 5769 5148 84 -1611 -553 O ATOM 3048 CB GLN B 195 -42.305 107.356 23.067 1.00 48.36 C ANISOU 3048 CB GLN B 195 5989 6239 6146 480 -2353 -752 C ATOM 3049 CG GLN B 195 -41.804 107.262 24.492 1.00 51.42 C ANISOU 3049 CG GLN B 195 6674 6413 6452 600 -2754 -759 C ATOM 3050 CD GLN B 195 -40.444 106.581 24.598 1.00 55.19 C ANISOU 3050 CD GLN B 195 6957 6801 7210 857 -3202 -1068 C ATOM 3051 OE1 GLN B 195 -40.157 105.609 23.889 1.00 57.00 O ANISOU 3051 OE1 GLN B 195 7022 7015 7622 985 -3291 -1207 O ATOM 3052 NE2 GLN B 195 -39.607 107.075 25.493 1.00 57.53 N ANISOU 3052 NE2 GLN B 195 7265 7032 7563 947 -3509 -1203 N ATOM 3053 N VAL B 196 -44.843 109.637 23.994 1.00 42.25 N ANISOU 3053 N VAL B 196 5687 5554 4813 46 -1698 -231 N ATOM 3054 CA VAL B 196 -45.242 111.034 24.160 1.00 40.90 C ANISOU 3054 CA VAL B 196 5507 5483 4551 -90 -1467 -161 C ATOM 3055 C VAL B 196 -44.628 111.544 25.449 1.00 42.35 C ANISOU 3055 C VAL B 196 5873 5560 4656 -73 -1681 -180 C ATOM 3056 O VAL B 196 -44.874 110.975 26.504 1.00 43.81 O ANISOU 3056 O VAL B 196 6422 5551 4672 -52 -1855 -93 O ATOM 3057 CB VAL B 196 -46.780 111.174 24.255 1.00 39.49 C ANISOU 3057 CB VAL B 196 5522 5292 4190 -212 -1204 23 C ATOM 3058 CG1 VAL B 196 -47.192 112.631 24.398 1.00 38.68 C ANISOU 3058 CG1 VAL B 196 5402 5274 4019 -317 -997 68 C ATOM 3059 CG2 VAL B 196 -47.456 110.565 23.036 1.00 38.76 C ANISOU 3059 CG2 VAL B 196 5275 5282 4171 -216 -1045 34 C ATOM 3060 N THR B 197 -43.841 112.614 25.360 1.00 42.20 N ANISOU 3060 N THR B 197 5642 5651 4739 -102 -1660 -300 N ATOM 3061 CA THR B 197 -43.233 113.245 26.519 1.00 43.63 C ANISOU 3061 CA THR B 197 5965 5751 4861 -96 -1857 -340 C ATOM 3062 C THR B 197 -43.938 114.579 26.762 1.00 42.14 C ANISOU 3062 C THR B 197 5868 5624 4520 -256 -1574 -219 C ATOM 3063 O THR B 197 -44.005 115.415 25.863 1.00 40.89 O ANISOU 3063 O THR B 197 5490 5615 4434 -341 -1325 -248 O ATOM 3064 CB THR B 197 -41.730 113.485 26.267 1.00 45.27 C ANISOU 3064 CB THR B 197 5823 6039 5338 -19 -2051 -626 C ATOM 3065 OG1 THR B 197 -41.053 112.226 26.188 1.00 47.12 O ANISOU 3065 OG1 THR B 197 5978 6188 5738 171 -2375 -776 O ATOM 3066 CG2 THR B 197 -41.093 114.333 27.363 1.00 46.77 C ANISOU 3066 CG2 THR B 197 6109 6173 5487 -32 -2236 -694 C ATOM 3067 N HIS B 198 -44.434 114.772 27.983 1.00 42.84 N ANISOU 3067 N HIS B 198 6318 5571 4386 -301 -1621 -99 N ATOM 3068 CA HIS B 198 -45.168 115.976 28.363 1.00 41.89 C ANISOU 3068 CA HIS B 198 6313 5482 4122 -438 -1368 -3 C ATOM 3069 C HIS B 198 -44.824 116.392 29.787 1.00 44.54 C ANISOU 3069 C HIS B 198 6954 5676 4293 -463 -1551 5 C ATOM 3070 O HIS B 198 -45.207 115.715 30.744 1.00 45.25 O ANISOU 3070 O HIS B 198 7427 5581 4183 -472 -1665 90 O ATOM 3071 CB HIS B 198 -46.669 115.720 28.269 1.00 40.73 C ANISOU 3071 CB HIS B 198 6316 5315 3844 -516 -1101 142 C ATOM 3072 CG HIS B 198 -47.503 116.911 28.613 1.00 39.71 C ANISOU 3072 CG HIS B 198 6268 5213 3609 -628 -847 197 C ATOM 3073 ND1 HIS B 198 -48.070 117.081 29.856 1.00 40.48 N ANISOU 3073 ND1 HIS B 198 6705 5179 3498 -722 -797 254 N ATOM 3074 CD2 HIS B 198 -47.844 118.003 27.889 1.00 38.30 C ANISOU 3074 CD2 HIS B 198 5904 5152 3497 -657 -641 186 C ATOM 3075 CE1 HIS B 198 -48.736 118.220 29.880 1.00 39.81 C ANISOU 3075 CE1 HIS B 198 6584 5150 3390 -792 -562 258 C ATOM 3076 NE2 HIS B 198 -48.616 118.799 28.699 1.00 38.20 N ANISOU 3076 NE2 HIS B 198 6077 5086 3350 -739 -489 224 N ATOM 3077 N GLU B 199 -44.101 117.506 29.917 1.00 45.91 N ANISOU 3077 N GLU B 199 6995 5917 4529 -496 -1568 -91 N ATOM 3078 CA GLU B 199 -43.748 118.085 31.218 1.00 48.36 C ANISOU 3078 CA GLU B 199 7579 6107 4687 -530 -1733 -98 C ATOM 3079 C GLU B 199 -43.017 117.062 32.096 1.00 51.36 C ANISOU 3079 C GLU B 199 8200 6297 5017 -400 -2182 -152 C ATOM 3080 O GLU B 199 -43.440 116.764 33.217 1.00 52.17 O ANISOU 3080 O GLU B 199 8775 6198 4849 -436 -2283 -44 O ATOM 3081 CB GLU B 199 -45.000 118.649 31.919 1.00 48.08 C ANISOU 3081 CB GLU B 199 7866 6004 4398 -669 -1460 60 C ATOM 3082 CG GLU B 199 -45.779 119.663 31.084 1.00 46.57 C ANISOU 3082 CG GLU B 199 7464 5963 4267 -749 -1086 93 C ATOM 3083 CD GLU B 199 -45.078 121.003 30.957 1.00 46.67 C ANISOU 3083 CD GLU B 199 7323 6056 4355 -796 -1055 5 C ATOM 3084 OE1 GLU B 199 -44.990 121.739 31.960 1.00 48.63 O ANISOU 3084 OE1 GLU B 199 7784 6226 4468 -861 -1084 6 O ATOM 3085 OE2 GLU B 199 -44.630 121.332 29.846 1.00 46.80 O ANISOU 3085 OE2 GLU B 199 7037 6200 4546 -793 -980 -71 O ATOM 3086 N GLY B 200 -41.940 116.500 31.548 1.00 53.13 N ANISOU 3086 N GLY B 200 8119 6568 5500 -249 -2451 -338 N ATOM 3087 CA GLY B 200 -41.104 115.537 32.262 1.00 56.94 C ANISOU 3087 CA GLY B 200 8780 6857 5997 -65 -2964 -444 C ATOM 3088 C GLY B 200 -41.564 114.091 32.174 1.00 58.22 C ANISOU 3088 C GLY B 200 9176 6866 6078 31 -3085 -346 C ATOM 3089 O GLY B 200 -40.729 113.189 32.108 1.00 61.49 O ANISOU 3089 O GLY B 200 9521 7190 6653 235 -3481 -499 O ATOM 3090 N SER B 201 -42.880 113.867 32.178 1.00 56.66 N ANISOU 3090 N SER B 201 9247 6632 5652 -114 -2752 -122 N ATOM 3091 CA SER B 201 -43.459 112.523 32.185 1.00 57.50 C ANISOU 3091 CA SER B 201 9647 6568 5632 -82 -2810 -16 C ATOM 3092 C SER B 201 -43.634 111.977 30.768 1.00 55.64 C ANISOU 3092 C SER B 201 8988 6510 5642 -33 -2628 -56 C ATOM 3093 O SER B 201 -43.913 112.736 29.835 1.00 52.84 O ANISOU 3093 O SER B 201 8250 6395 5431 -112 -2292 -71 O ATOM 3094 CB SER B 201 -44.808 112.549 32.907 1.00 57.41 C ANISOU 3094 CB SER B 201 10111 6433 5270 -306 -2498 190 C ATOM 3095 OG SER B 201 -45.400 111.264 32.939 1.00 59.25 O ANISOU 3095 OG SER B 201 10661 6488 5362 -326 -2511 281 O ATOM 3096 N THR B 202 -43.476 110.662 30.624 1.00 57.14 N ANISOU 3096 N THR B 202 9300 6555 5856 98 -2868 -72 N ATOM 3097 CA THR B 202 -43.613 109.982 29.338 1.00 56.52 C ANISOU 3097 CA THR B 202 8874 6611 5991 153 -2734 -117 C ATOM 3098 C THR B 202 -44.736 108.948 29.384 1.00 56.62 C ANISOU 3098 C THR B 202 9241 6476 5798 64 -2594 54 C ATOM 3099 O THR B 202 -44.816 108.150 30.317 1.00 59.02 O ANISOU 3099 O THR B 202 10065 6490 5870 76 -2833 127 O ATOM 3100 CB THR B 202 -42.300 109.294 28.913 1.00 58.37 C ANISOU 3100 CB THR B 202 8826 6829 6522 406 -3138 -360 C ATOM 3101 OG1 THR B 202 -41.286 110.286 28.740 1.00 58.91 O ANISOU 3101 OG1 THR B 202 8489 7070 6825 441 -3192 -572 O ATOM 3102 CG2 THR B 202 -42.465 108.539 27.596 1.00 57.20 C ANISOU 3102 CG2 THR B 202 8358 6805 6572 448 -2981 -412 C ATOM 3103 N VAL B 203 -45.594 108.988 28.367 1.00 54.95 N ANISOU 3103 N VAL B 203 8769 6448 5661 -39 -2211 104 N ATOM 3104 CA VAL B 203 -46.636 107.995 28.147 1.00 55.23 C ANISOU 3104 CA VAL B 203 9009 6395 5580 -131 -2042 212 C ATOM 3105 C VAL B 203 -46.264 107.247 26.872 1.00 55.04 C ANISOU 3105 C VAL B 203 8620 6479 5814 8 -2093 110 C ATOM 3106 O VAL B 203 -45.990 107.874 25.845 1.00 54.38 O ANISOU 3106 O VAL B 203 8079 6638 5947 34 -1947 19 O ATOM 3107 CB VAL B 203 -48.025 108.658 27.991 1.00 53.70 C ANISOU 3107 CB VAL B 203 8783 6330 5292 -356 -1569 308 C ATOM 3108 CG1 VAL B 203 -49.089 107.627 27.617 1.00 54.02 C ANISOU 3108 CG1 VAL B 203 8938 6314 5273 -463 -1374 362 C ATOM 3109 CG2 VAL B 203 -48.416 109.386 29.271 1.00 54.58 C ANISOU 3109 CG2 VAL B 203 9254 6331 5152 -510 -1481 378 C ATOM 3110 N GLU B 204 -46.257 105.917 26.943 1.00 56.32 N ANISOU 3110 N GLU B 204 9031 6440 5929 81 -2290 121 N ATOM 3111 CA GLU B 204 -45.960 105.063 25.794 1.00 56.71 C ANISOU 3111 CA GLU B 204 8786 6558 6204 210 -2343 19 C ATOM 3112 C GLU B 204 -47.145 104.133 25.507 1.00 55.33 C ANISOU 3112 C GLU B 204 8818 6304 5899 73 -2124 136 C ATOM 3113 O GLU B 204 -47.713 103.548 26.428 1.00 56.89 O ANISOU 3113 O GLU B 204 9528 6254 5834 -40 -2148 248 O ATOM 3114 CB GLU B 204 -44.696 104.238 26.050 1.00 60.59 C ANISOU 3114 CB GLU B 204 9333 6865 6822 474 -2847 -136 C ATOM 3115 CG GLU B 204 -44.134 103.565 24.805 1.00 61.53 C ANISOU 3115 CG GLU B 204 9036 7097 7246 630 -2900 -315 C ATOM 3116 CD GLU B 204 -42.818 102.851 25.059 1.00 65.74 C ANISOU 3116 CD GLU B 204 9544 7461 7972 925 -3423 -539 C ATOM 3117 OE1 GLU B 204 -42.788 101.915 25.893 1.00 69.14 O ANISOU 3117 OE1 GLU B 204 10473 7560 8236 1030 -3776 -482 O ATOM 3118 OE2 GLU B 204 -41.814 103.218 24.412 1.00 66.86 O ANISOU 3118 OE2 GLU B 204 9180 7787 8438 1047 -3484 -798 O ATOM 3119 N LYS B 205 -47.531 104.042 24.236 1.00 52.45 N ANISOU 3119 N LYS B 205 8080 6144 5704 57 -1894 96 N ATOM 3120 CA LYS B 205 -48.511 103.055 23.772 1.00 51.81 C ANISOU 3120 CA LYS B 205 8110 6007 5567 -43 -1727 154 C ATOM 3121 C LYS B 205 -47.862 102.211 22.690 1.00 51.76 C ANISOU 3121 C LYS B 205 7842 6041 5785 132 -1875 28 C ATOM 3122 O LYS B 205 -47.024 102.704 21.936 1.00 50.08 O ANISOU 3122 O LYS B 205 7227 6009 5792 252 -1914 -108 O ATOM 3123 CB LYS B 205 -49.770 103.733 23.232 1.00 49.29 C ANISOU 3123 CB LYS B 205 7598 5891 5239 -234 -1310 203 C ATOM 3124 CG LYS B 205 -50.606 104.426 24.294 1.00 49.74 C ANISOU 3124 CG LYS B 205 7912 5898 5090 -431 -1110 289 C ATOM 3125 CD LYS B 205 -51.435 103.444 25.109 1.00 51.71 C ANISOU 3125 CD LYS B 205 8641 5900 5108 -620 -1027 353 C ATOM 3126 CE LYS B 205 -51.878 104.058 26.427 1.00 52.73 C ANISOU 3126 CE LYS B 205 9127 5912 4995 -808 -895 411 C ATOM 3127 NZ LYS B 205 -52.794 103.148 27.168 1.00 54.98 N ANISOU 3127 NZ LYS B 205 9903 5957 5032 -1069 -718 445 N ATOM 3128 N THR B 206 -48.272 100.947 22.619 1.00 53.58 N ANISOU 3128 N THR B 206 8318 6093 5949 118 -1926 59 N ATOM 3129 CA THR B 206 -47.646 99.950 21.751 1.00 55.03 C ANISOU 3129 CA THR B 206 8337 6249 6323 297 -2109 -68 C ATOM 3130 C THR B 206 -48.715 99.199 20.958 1.00 54.71 C ANISOU 3130 C THR B 206 8292 6236 6258 161 -1859 -23 C ATOM 3131 O THR B 206 -49.816 98.974 21.459 1.00 54.17 O ANISOU 3131 O THR B 206 8522 6070 5989 -51 -1665 95 O ATOM 3132 CB THR B 206 -46.825 98.945 22.584 1.00 58.48 C ANISOU 3132 CB THR B 206 9162 6349 6708 485 -2566 -108 C ATOM 3133 OG1 THR B 206 -45.986 99.655 23.503 1.00 60.32 O ANISOU 3133 OG1 THR B 206 9466 6526 6926 591 -2822 -144 O ATOM 3134 CG2 THR B 206 -45.950 98.068 21.697 1.00 59.83 C ANISOU 3134 CG2 THR B 206 9076 6509 7146 726 -2799 -305 C ATOM 3135 N VAL B 207 -48.379 98.822 19.725 1.00 54.81 N ANISOU 3135 N VAL B 207 7962 6382 6483 265 -1848 -146 N ATOM 3136 CA VAL B 207 -49.288 98.068 18.861 1.00 55.24 C ANISOU 3136 CA VAL B 207 7984 6467 6539 161 -1652 -132 C ATOM 3137 C VAL B 207 -48.494 97.098 17.969 1.00 57.28 C ANISOU 3137 C VAL B 207 8082 6693 6990 350 -1834 -287 C ATOM 3138 O VAL B 207 -47.324 97.352 17.653 1.00 58.35 O ANISOU 3138 O VAL B 207 7949 6903 7319 533 -1995 -449 O ATOM 3139 CB VAL B 207 -50.181 99.033 18.038 1.00 52.61 C ANISOU 3139 CB VAL B 207 7339 6416 6235 14 -1306 -109 C ATOM 3140 CG1 VAL B 207 -49.405 99.685 16.899 1.00 51.24 C ANISOU 3140 CG1 VAL B 207 6747 6470 6251 122 -1280 -235 C ATOM 3141 CG2 VAL B 207 -51.421 98.323 17.525 1.00 52.43 C ANISOU 3141 CG2 VAL B 207 7368 6387 6167 -141 -1108 -81 C ATOM 3142 N ALA B 208 -49.130 95.989 17.587 1.00 58.25 N ANISOU 3142 N ALA B 208 8361 6702 7072 292 -1791 -268 N ATOM 3143 CA ALA B 208 -48.477 94.915 16.823 1.00 59.78 C ANISOU 3143 CA ALA B 208 8467 6819 7429 466 -1968 -417 C ATOM 3144 C ALA B 208 -49.433 94.279 15.800 1.00 59.31 C ANISOU 3144 C ALA B 208 8340 6828 7367 332 -1736 -410 C ATOM 3145 O ALA B 208 -50.635 94.202 16.057 1.00 58.56 O ANISOU 3145 O ALA B 208 8431 6707 7112 112 -1532 -288 O ATOM 3146 CB ALA B 208 -47.959 93.853 17.780 1.00 62.62 C ANISOU 3146 CB ALA B 208 9271 6808 7713 610 -2343 -416 C ATOM 3147 N PRO B 209 -48.903 93.808 14.645 1.00 60.05 N ANISOU 3147 N PRO B 209 8161 7006 7649 452 -1758 -573 N ATOM 3148 CA PRO B 209 -49.765 93.205 13.612 1.00 60.40 C ANISOU 3148 CA PRO B 209 8143 7116 7691 334 -1563 -581 C ATOM 3149 C PRO B 209 -50.516 91.964 14.103 1.00 62.42 C ANISOU 3149 C PRO B 209 8813 7099 7806 236 -1609 -499 C ATOM 3150 O PRO B 209 -49.908 91.063 14.678 1.00 65.02 O ANISOU 3150 O PRO B 209 9431 7150 8123 374 -1885 -525 O ATOM 3151 CB PRO B 209 -48.785 92.870 12.475 1.00 60.55 C ANISOU 3151 CB PRO B 209 7856 7223 7928 504 -1624 -799 C ATOM 3152 CG PRO B 209 -47.446 92.813 13.122 1.00 62.29 C ANISOU 3152 CG PRO B 209 8057 7324 8285 737 -1925 -930 C ATOM 3153 CD PRO B 209 -47.490 93.826 14.226 1.00 61.16 C ANISOU 3153 CD PRO B 209 8019 7192 8025 687 -1947 -795 C ATOM 3154 N THR B 210 -51.832 91.958 13.890 1.00 62.55 N ANISOU 3154 N THR B 210 8864 7181 7720 -4 -1348 -423 N ATOM 3155 CA THR B 210 -52.732 90.951 14.458 1.00 65.07 C ANISOU 3155 CA THR B 210 9587 7257 7879 -192 -1296 -353 C ATOM 3156 C THR B 210 -54.119 91.038 13.815 1.00 64.29 C ANISOU 3156 C THR B 210 9327 7325 7776 -435 -986 -368 C ATOM 3157 O THR B 210 -54.574 90.102 13.155 1.00 65.90 O ANISOU 3157 O THR B 210 9558 7476 8006 -501 -941 -431 O ATOM 3158 CB THR B 210 -52.871 91.119 15.994 1.00 66.81 C ANISOU 3158 CB THR B 210 10237 7262 7888 -300 -1335 -224 C ATOM 3159 OG1 THR B 210 -53.652 90.044 16.530 1.00 69.78 O ANISOU 3159 OG1 THR B 210 11079 7356 8079 -520 -1263 -177 O ATOM 3160 CG2 THR B 210 -53.533 92.453 16.360 1.00 65.04 C ANISOU 3160 CG2 THR B 210 9833 7257 7621 -454 -1092 -166 C TER 3161 THR B 210 ATOM 3162 N VAL C 2 -8.743 103.577 29.650 1.00 71.87 N ANISOU 3162 N VAL C 2 10494 8269 8543 -2185 522 -912 N ATOM 3163 CA VAL C 2 -9.323 104.588 28.713 1.00 70.62 C ANISOU 3163 CA VAL C 2 9962 8354 8516 -2060 507 -1058 C ATOM 3164 C VAL C 2 -9.332 106.060 29.219 1.00 68.90 C ANISOU 3164 C VAL C 2 9487 8396 8295 -1926 652 -1069 C ATOM 3165 O VAL C 2 -10.049 106.893 28.659 1.00 68.77 O ANISOU 3165 O VAL C 2 9157 8575 8398 -1876 655 -1185 O ATOM 3166 CB VAL C 2 -10.746 104.178 28.258 1.00 73.26 C ANISOU 3166 CB VAL C 2 10093 8741 9004 -2338 508 -1166 C ATOM 3167 CG1 VAL C 2 -10.739 102.917 27.395 1.00 74.77 C ANISOU 3167 CG1 VAL C 2 10501 8684 9226 -2410 303 -1201 C ATOM 3168 CG2 VAL C 2 -11.688 104.010 29.445 1.00 75.91 C ANISOU 3168 CG2 VAL C 2 10347 9154 9343 -2696 736 -1119 C ATOM 3169 N GLN C 3 -8.584 106.388 30.279 1.00 67.42 N ANISOU 3169 N GLN C 3 9438 8202 7978 -1865 753 -959 N ATOM 3170 CA GLN C 3 -8.263 107.790 30.580 1.00 65.29 C ANISOU 3170 CA GLN C 3 8986 8126 7694 -1662 825 -974 C ATOM 3171 C GLN C 3 -6.891 107.915 31.243 1.00 62.70 C ANISOU 3171 C GLN C 3 8901 7704 7217 -1489 805 -854 C ATOM 3172 O GLN C 3 -6.582 107.197 32.200 1.00 63.91 O ANISOU 3172 O GLN C 3 9311 7720 7252 -1614 852 -745 O ATOM 3173 CB GLN C 3 -9.324 108.450 31.461 1.00 67.52 C ANISOU 3173 CB GLN C 3 9029 8614 8010 -1834 1038 -1024 C ATOM 3174 CG GLN C 3 -8.964 109.858 31.921 1.00 66.96 C ANISOU 3174 CG GLN C 3 8821 8708 7914 -1626 1103 -1044 C ATOM 3175 CD GLN C 3 -10.136 110.587 32.533 1.00 69.35 C ANISOU 3175 CD GLN C 3 8828 9238 8282 -1744 1290 -1153 C ATOM 3176 OE1 GLN C 3 -11.073 109.969 33.046 1.00 72.61 O ANISOU 3176 OE1 GLN C 3 9186 9699 8705 -2029 1438 -1174 O ATOM 3177 NE2 GLN C 3 -10.090 111.912 32.485 1.00 68.33 N ANISOU 3177 NE2 GLN C 3 8506 9253 8201 -1529 1284 -1230 N ATOM 3178 N LEU C 4 -6.093 108.837 30.707 1.00 58.94 N ANISOU 3178 N LEU C 4 8342 7303 6749 -1211 723 -872 N ATOM 3179 CA LEU C 4 -4.745 109.136 31.170 1.00 56.33 C ANISOU 3179 CA LEU C 4 8172 6921 6308 -1018 682 -782 C ATOM 3180 C LEU C 4 -4.699 110.604 31.592 1.00 54.63 C ANISOU 3180 C LEU C 4 7765 6890 6103 -911 760 -803 C ATOM 3181 O LEU C 4 -5.275 111.432 30.910 1.00 53.64 O ANISOU 3181 O LEU C 4 7397 6900 6083 -854 751 -892 O ATOM 3182 CB LEU C 4 -3.751 108.894 30.025 1.00 54.68 C ANISOU 3182 CB LEU C 4 8029 6641 6105 -792 507 -794 C ATOM 3183 CG LEU C 4 -3.347 107.450 29.698 1.00 55.30 C ANISOU 3183 CG LEU C 4 8368 6497 6148 -807 389 -776 C ATOM 3184 CD1 LEU C 4 -4.477 106.660 29.052 1.00 57.21 C ANISOU 3184 CD1 LEU C 4 8583 6681 6473 -998 363 -852 C ATOM 3185 CD2 LEU C 4 -2.125 107.426 28.795 1.00 54.04 C ANISOU 3185 CD2 LEU C 4 8254 6316 5963 -532 250 -798 C ATOM 3186 N GLN C 5 -4.008 110.919 32.690 1.00 53.55 N ANISOU 3186 N GLN C 5 7752 6739 5855 -875 810 -725 N ATOM 3187 CA GLN C 5 -3.845 112.314 33.162 1.00 52.74 C ANISOU 3187 CA GLN C 5 7505 6780 5752 -763 861 -748 C ATOM 3188 C GLN C 5 -2.475 112.522 33.816 1.00 49.97 C ANISOU 3188 C GLN C 5 7333 6363 5292 -624 797 -655 C ATOM 3189 O GLN C 5 -2.052 111.713 34.645 1.00 49.90 O ANISOU 3189 O GLN C 5 7565 6231 5164 -691 800 -572 O ATOM 3190 CB GLN C 5 -4.941 112.675 34.176 1.00 55.54 C ANISOU 3190 CB GLN C 5 7761 7252 6090 -936 1050 -800 C ATOM 3191 CG GLN C 5 -6.227 113.316 33.629 1.00 57.68 C ANISOU 3191 CG GLN C 5 7716 7687 6512 -973 1110 -943 C ATOM 3192 CD GLN C 5 -6.161 114.849 33.499 1.00 57.53 C ANISOU 3192 CD GLN C 5 7506 7791 6561 -777 1077 -1018 C ATOM 3193 OE1 GLN C 5 -5.247 115.520 33.993 1.00 56.99 O ANISOU 3193 OE1 GLN C 5 7529 7704 6421 -649 1043 -967 O ATOM 3194 NE2 GLN C 5 -7.152 115.404 32.823 1.00 59.26 N ANISOU 3194 NE2 GLN C 5 7464 8125 6926 -756 1065 -1143 N ATOM 3195 N GLU C 6 -1.813 113.621 33.452 1.00 46.61 N ANISOU 3195 N GLU C 6 6790 6013 4905 -441 728 -668 N ATOM 3196 CA GLU C 6 -0.467 113.945 33.936 1.00 45.27 C ANISOU 3196 CA GLU C 6 6735 5803 4661 -303 647 -595 C ATOM 3197 C GLU C 6 -0.581 114.705 35.236 1.00 44.76 C ANISOU 3197 C GLU C 6 6695 5789 4521 -342 732 -595 C ATOM 3198 O GLU C 6 -1.449 115.567 35.377 1.00 45.40 O ANISOU 3198 O GLU C 6 6614 5983 4654 -375 820 -677 O ATOM 3199 CB GLU C 6 0.328 114.839 32.966 1.00 43.50 C ANISOU 3199 CB GLU C 6 6371 5646 4511 -125 540 -602 C ATOM 3200 CG GLU C 6 0.414 114.363 31.526 1.00 43.29 C ANISOU 3200 CG GLU C 6 6287 5617 4545 -64 465 -624 C ATOM 3201 CD GLU C 6 -0.841 114.634 30.716 1.00 43.22 C ANISOU 3201 CD GLU C 6 6111 5679 4630 -129 497 -706 C ATOM 3202 OE1 GLU C 6 -1.815 115.210 31.244 1.00 43.91 O ANISOU 3202 OE1 GLU C 6 6096 5830 4757 -211 582 -757 O ATOM 3203 OE2 GLU C 6 -0.869 114.275 29.531 1.00 43.91 O ANISOU 3203 OE2 GLU C 6 6162 5769 4751 -86 430 -732 O ATOM 3204 N SER C 7 0.311 114.397 36.169 1.00 44.23 N ANISOU 3204 N SER C 7 6835 5639 4332 -318 688 -517 N ATOM 3205 CA SER C 7 0.500 115.188 37.371 1.00 43.94 C ANISOU 3205 CA SER C 7 6851 5642 4202 -315 727 -517 C ATOM 3206 C SER C 7 1.916 115.693 37.336 1.00 41.99 C ANISOU 3206 C SER C 7 6626 5369 3959 -143 566 -472 C ATOM 3207 O SER C 7 2.818 114.878 37.186 1.00 41.75 O ANISOU 3207 O SER C 7 6720 5243 3901 -78 455 -408 O ATOM 3208 CB SER C 7 0.340 114.331 38.611 1.00 45.83 C ANISOU 3208 CB SER C 7 7349 5801 4264 -457 797 -453 C ATOM 3209 OG SER C 7 0.723 115.065 39.758 1.00 46.73 O ANISOU 3209 OG SER C 7 7549 5945 4261 -427 803 -452 O ATOM 3210 N GLY C 8 2.097 116.990 37.592 1.00 40.54 N ANISOU 3210 N GLY C 8 6335 5263 3806 -77 550 -515 N ATOM 3211 CA GLY C 8 3.356 117.691 37.382 1.00 39.19 C ANISOU 3211 CA GLY C 8 6120 5093 3677 61 401 -484 C ATOM 3212 C GLY C 8 3.623 118.905 38.266 1.00 38.60 C ANISOU 3212 C GLY C 8 6045 5048 3572 91 371 -517 C ATOM 3213 O GLY C 8 2.686 119.408 38.907 1.00 39.30 O ANISOU 3213 O GLY C 8 6129 5180 3622 31 481 -591 O ATOM 3214 N PRO C 9 4.897 119.393 38.288 1.00 37.96 N ANISOU 3214 N PRO C 9 5957 4953 3514 185 219 -476 N ATOM 3215 CA PRO C 9 5.314 120.462 39.189 1.00 38.36 C ANISOU 3215 CA PRO C 9 6041 5005 3531 210 151 -505 C ATOM 3216 C PRO C 9 5.051 121.903 38.668 1.00 37.45 C ANISOU 3216 C PRO C 9 5755 4934 3542 234 129 -563 C ATOM 3217 O PRO C 9 5.049 122.863 39.450 1.00 37.69 O ANISOU 3217 O PRO C 9 5821 4952 3547 245 92 -620 O ATOM 3218 CB PRO C 9 6.829 120.202 39.374 1.00 38.73 C ANISOU 3218 CB PRO C 9 6139 5011 3564 286 -21 -434 C ATOM 3219 CG PRO C 9 7.264 119.381 38.209 1.00 38.16 C ANISOU 3219 CG PRO C 9 5977 4953 3571 332 -41 -387 C ATOM 3220 CD PRO C 9 6.033 118.952 37.449 1.00 37.99 C ANISOU 3220 CD PRO C 9 5904 4950 3580 270 104 -415 C ATOM 3221 N GLY C 10 4.868 122.059 37.356 1.00 36.37 N ANISOU 3221 N GLY C 10 5458 4833 3530 247 132 -548 N ATOM 3222 CA GLY C 10 4.607 123.356 36.725 1.00 35.99 C ANISOU 3222 CA GLY C 10 5277 4799 3598 267 86 -582 C ATOM 3223 C GLY C 10 5.876 124.138 36.433 1.00 35.75 C ANISOU 3223 C GLY C 10 5202 4755 3627 288 -65 -514 C ATOM 3224 O GLY C 10 6.054 124.641 35.319 1.00 35.80 O ANISOU 3224 O GLY C 10 5094 4782 3725 284 -107 -469 O ATOM 3225 N LEU C 11 6.759 124.218 37.428 1.00 35.44 N ANISOU 3225 N LEU C 11 5256 4683 3526 296 -148 -503 N ATOM 3226 CA LEU C 11 8.001 124.971 37.331 1.00 35.33 C ANISOU 3226 CA LEU C 11 5189 4662 3574 292 -299 -449 C ATOM 3227 C LEU C 11 9.179 124.135 37.821 1.00 35.37 C ANISOU 3227 C LEU C 11 5237 4682 3522 321 -373 -403 C ATOM 3228 O LEU C 11 9.164 123.628 38.944 1.00 35.74 O ANISOU 3228 O LEU C 11 5439 4686 3454 341 -383 -432 O ATOM 3229 CB LEU C 11 7.874 126.247 38.163 1.00 36.26 C ANISOU 3229 CB LEU C 11 5370 4708 3701 282 -385 -517 C ATOM 3230 CG LEU C 11 9.070 127.204 38.257 1.00 37.27 C ANISOU 3230 CG LEU C 11 5462 4801 3899 246 -562 -475 C ATOM 3231 CD1 LEU C 11 9.541 127.684 36.890 1.00 36.78 C ANISOU 3231 CD1 LEU C 11 5241 4775 3958 188 -596 -380 C ATOM 3232 CD2 LEU C 11 8.695 128.395 39.130 1.00 38.38 C ANISOU 3232 CD2 LEU C 11 5705 4841 4038 250 -645 -571 C ATOM 3233 N VAL C 12 10.187 123.985 36.966 1.00 35.58 N ANISOU 3233 N VAL C 12 5123 4774 3620 327 -426 -337 N ATOM 3234 CA VAL C 12 11.487 123.414 37.357 1.00 36.91 C ANISOU 3234 CA VAL C 12 5276 4972 3776 376 -536 -311 C ATOM 3235 C VAL C 12 12.604 124.436 37.168 1.00 37.61 C ANISOU 3235 C VAL C 12 5219 5106 3966 323 -663 -278 C ATOM 3236 O VAL C 12 12.570 125.270 36.250 1.00 37.38 O ANISOU 3236 O VAL C 12 5069 5113 4021 245 -641 -238 O ATOM 3237 CB VAL C 12 11.860 122.099 36.636 1.00 37.36 C ANISOU 3237 CB VAL C 12 5278 5090 3825 453 -490 -289 C ATOM 3238 CG1 VAL C 12 10.989 120.955 37.136 1.00 37.73 C ANISOU 3238 CG1 VAL C 12 5516 5057 3761 489 -413 -312 C ATOM 3239 CG2 VAL C 12 11.779 122.226 35.132 1.00 37.24 C ANISOU 3239 CG2 VAL C 12 5092 5172 3884 428 -402 -258 C ATOM 3240 N LYS C 13 13.586 124.380 38.052 1.00 38.61 N ANISOU 3240 N LYS C 13 5365 5223 4080 351 -809 -290 N ATOM 3241 CA LYS C 13 14.780 125.198 37.921 1.00 40.17 C ANISOU 3241 CA LYS C 13 5399 5480 4385 286 -942 -263 C ATOM 3242 C LYS C 13 15.695 124.604 36.854 1.00 40.18 C ANISOU 3242 C LYS C 13 5169 5639 4456 312 -907 -225 C ATOM 3243 O LYS C 13 15.697 123.387 36.616 1.00 39.28 O ANISOU 3243 O LYS C 13 5064 5563 4297 429 -850 -242 O ATOM 3244 CB LYS C 13 15.532 125.282 39.245 1.00 42.63 C ANISOU 3244 CB LYS C 13 5798 5738 4662 317 -1132 -304 C ATOM 3245 CG LYS C 13 14.786 126.009 40.351 1.00 43.64 C ANISOU 3245 CG LYS C 13 6148 5729 4706 290 -1178 -361 C ATOM 3246 CD LYS C 13 15.724 126.277 41.518 1.00 46.23 C ANISOU 3246 CD LYS C 13 6539 6016 5009 302 -1400 -400 C ATOM 3247 CE LYS C 13 14.974 126.677 42.779 1.00 47.40 C ANISOU 3247 CE LYS C 13 6957 6039 5012 313 -1433 -478 C ATOM 3248 NZ LYS C 13 14.194 127.936 42.597 1.00 47.69 N ANISOU 3248 NZ LYS C 13 7014 6008 5098 233 -1390 -517 N ATOM 3249 N SER C 14 16.464 125.482 36.218 1.00 40.77 N ANISOU 3249 N SER C 14 5047 5805 4638 195 -940 -177 N ATOM 3250 CA SER C 14 17.451 125.077 35.223 1.00 41.98 C ANISOU 3250 CA SER C 14 4946 6150 4855 199 -893 -153 C ATOM 3251 C SER C 14 18.481 124.114 35.828 1.00 42.91 C ANISOU 3251 C SER C 14 4988 6334 4982 346 -1006 -218 C ATOM 3252 O SER C 14 18.858 124.241 36.996 1.00 43.67 O ANISOU 3252 O SER C 14 5169 6349 5074 373 -1178 -254 O ATOM 3253 CB SER C 14 18.143 126.305 34.622 1.00 43.26 C ANISOU 3253 CB SER C 14 4921 6396 5119 2 -917 -81 C ATOM 3254 OG SER C 14 18.659 126.009 33.338 1.00 44.35 O ANISOU 3254 OG SER C 14 4839 6734 5278 -27 -783 -44 O ATOM 3255 N SER C 15 18.894 123.135 35.028 1.00 43.39 N ANISOU 3255 N SER C 15 4907 6532 5047 457 -922 -245 N ATOM 3256 CA SER C 15 19.847 122.090 35.421 1.00 44.77 C ANISOU 3256 CA SER C 15 4998 6771 5241 642 -1033 -323 C ATOM 3257 C SER C 15 19.370 121.105 36.511 1.00 44.77 C ANISOU 3257 C SER C 15 5287 6585 5139 802 -1135 -364 C ATOM 3258 O SER C 15 20.182 120.411 37.108 1.00 46.30 O ANISOU 3258 O SER C 15 5463 6781 5347 953 -1295 -421 O ATOM 3259 CB SER C 15 21.188 122.726 35.775 1.00 46.92 C ANISOU 3259 CB SER C 15 5030 7165 5635 584 -1187 -342 C ATOM 3260 OG SER C 15 21.234 123.157 37.126 1.00 47.40 O ANISOU 3260 OG SER C 15 5255 7072 5681 567 -1387 -351 O ATOM 3261 N GLU C 16 18.060 121.029 36.751 1.00 43.86 N ANISOU 3261 N GLU C 16 5433 6314 4917 767 -1046 -334 N ATOM 3262 CA GLU C 16 17.488 120.064 37.700 1.00 44.40 C ANISOU 3262 CA GLU C 16 5795 6213 4863 875 -1102 -351 C ATOM 3263 C GLU C 16 16.682 118.990 36.936 1.00 43.38 C ANISOU 3263 C GLU C 16 5752 6052 4679 942 -952 -356 C ATOM 3264 O GLU C 16 16.708 118.976 35.707 1.00 42.79 O ANISOU 3264 O GLU C 16 5498 6099 4659 934 -828 -360 O ATOM 3265 CB GLU C 16 16.695 120.822 38.772 1.00 44.30 C ANISOU 3265 CB GLU C 16 6007 6060 4763 767 -1127 -330 C ATOM 3266 CG GLU C 16 17.586 121.832 39.503 1.00 45.77 C ANISOU 3266 CG GLU C 16 6117 6267 5008 710 -1307 -342 C ATOM 3267 CD GLU C 16 17.043 122.336 40.826 1.00 46.45 C ANISOU 3267 CD GLU C 16 6466 6208 4977 663 -1387 -355 C ATOM 3268 OE1 GLU C 16 15.862 122.120 41.143 1.00 46.00 O ANISOU 3268 OE1 GLU C 16 6626 6055 4797 643 -1265 -351 O ATOM 3269 OE2 GLU C 16 17.823 122.964 41.566 1.00 48.23 O ANISOU 3269 OE2 GLU C 16 6670 6426 5229 643 -1574 -379 O ATOM 3270 N THR C 17 16.046 118.053 37.646 1.00 43.85 N ANISOU 3270 N THR C 17 6088 5949 4623 1003 -974 -355 N ATOM 3271 CA THR C 17 15.319 116.926 37.014 1.00 43.70 C ANISOU 3271 CA THR C 17 6176 5871 4558 1057 -865 -363 C ATOM 3272 C THR C 17 13.813 117.178 37.019 1.00 42.04 C ANISOU 3272 C THR C 17 6114 5583 4275 910 -701 -329 C ATOM 3273 O THR C 17 13.229 117.436 38.070 1.00 41.72 O ANISOU 3273 O THR C 17 6265 5444 4144 835 -710 -307 O ATOM 3274 CB THR C 17 15.637 115.575 37.708 1.00 45.42 C ANISOU 3274 CB THR C 17 6612 5943 4702 1213 -1013 -380 C ATOM 3275 OG1 THR C 17 16.988 115.225 37.426 1.00 47.86 O ANISOU 3275 OG1 THR C 17 6729 6348 5106 1390 -1156 -443 O ATOM 3276 CG2 THR C 17 14.731 114.414 37.218 1.00 44.97 C ANISOU 3276 CG2 THR C 17 6729 5772 4587 1231 -916 -380 C ATOM 3277 N LEU C 18 13.200 117.099 35.841 1.00 40.61 N ANISOU 3277 N LEU C 18 5837 5462 4131 876 -553 -337 N ATOM 3278 CA LEU C 18 11.747 117.192 35.696 1.00 39.77 C ANISOU 3278 CA LEU C 18 5835 5297 3980 756 -406 -324 C ATOM 3279 C LEU C 18 11.148 115.815 35.932 1.00 40.26 C ANISOU 3279 C LEU C 18 6117 5222 3959 785 -391 -329 C ATOM 3280 O LEU C 18 11.532 114.866 35.253 1.00 40.14 O ANISOU 3280 O LEU C 18 6088 5200 3965 893 -420 -358 O ATOM 3281 CB LEU C 18 11.394 117.708 34.293 1.00 39.09 C ANISOU 3281 CB LEU C 18 5556 5328 3966 711 -290 -330 C ATOM 3282 CG LEU C 18 9.917 117.848 33.784 1.00 38.58 C ANISOU 3282 CG LEU C 18 5529 5238 3892 609 -153 -335 C ATOM 3283 CD1 LEU C 18 9.551 116.663 32.901 1.00 38.95 C ANISOU 3283 CD1 LEU C 18 5608 5267 3924 658 -103 -367 C ATOM 3284 CD2 LEU C 18 8.839 118.039 34.859 1.00 38.30 C ANISOU 3284 CD2 LEU C 18 5653 5103 3794 515 -107 -339 C ATOM 3285 N SER C 19 10.194 115.725 36.862 1.00 40.05 N ANISOU 3285 N SER C 19 6291 5089 3835 680 -340 -305 N ATOM 3286 CA SER C 19 9.469 114.491 37.152 1.00 41.44 C ANISOU 3286 CA SER C 19 6698 5124 3922 644 -308 -290 C ATOM 3287 C SER C 19 7.954 114.656 36.911 1.00 40.72 C ANISOU 3287 C SER C 19 6611 5042 3821 482 -125 -301 C ATOM 3288 O SER C 19 7.341 115.590 37.428 1.00 39.66 O ANISOU 3288 O SER C 19 6448 4956 3667 388 -46 -310 O ATOM 3289 CB SER C 19 9.755 114.050 38.588 1.00 43.16 C ANISOU 3289 CB SER C 19 7182 5213 4005 646 -415 -243 C ATOM 3290 OG SER C 19 9.202 112.774 38.818 1.00 45.24 O ANISOU 3290 OG SER C 19 7692 5318 4180 603 -406 -208 O ATOM 3291 N LEU C 20 7.371 113.771 36.097 1.00 40.49 N ANISOU 3291 N LEU C 20 6600 4971 3815 462 -70 -317 N ATOM 3292 CA LEU C 20 5.920 113.733 35.873 1.00 41.01 C ANISOU 3292 CA LEU C 20 6662 5040 3881 304 84 -337 C ATOM 3293 C LEU C 20 5.407 112.315 36.031 1.00 42.06 C ANISOU 3293 C LEU C 20 7014 5017 3949 232 90 -315 C ATOM 3294 O LEU C 20 6.133 111.364 35.747 1.00 42.61 O ANISOU 3294 O LEU C 20 7186 4986 4017 344 -31 -308 O ATOM 3295 CB LEU C 20 5.547 114.270 34.476 1.00 40.44 C ANISOU 3295 CB LEU C 20 6353 5087 3926 319 139 -390 C ATOM 3296 CG LEU C 20 5.925 115.716 34.154 1.00 39.42 C ANISOU 3296 CG LEU C 20 6020 5092 3866 358 132 -398 C ATOM 3297 CD1 LEU C 20 5.551 116.078 32.731 1.00 39.48 C ANISOU 3297 CD1 LEU C 20 5850 5191 3958 367 168 -431 C ATOM 3298 CD2 LEU C 20 5.226 116.665 35.097 1.00 39.79 C ANISOU 3298 CD2 LEU C 20 6072 5156 3889 266 197 -409 C ATOM 3299 N THR C 21 4.160 112.186 36.486 1.00 42.73 N ANISOU 3299 N THR C 21 7166 5084 3986 43 226 -310 N ATOM 3300 CA THR C 21 3.472 110.882 36.546 1.00 44.63 C ANISOU 3300 CA THR C 21 7604 5178 4177 -88 252 -282 C ATOM 3301 C THR C 21 2.169 110.936 35.763 1.00 44.82 C ANISOU 3301 C THR C 21 7468 5276 4287 -227 387 -346 C ATOM 3302 O THR C 21 1.468 111.951 35.777 1.00 44.89 O ANISOU 3302 O THR C 21 7285 5431 4338 -283 501 -396 O ATOM 3303 CB THR C 21 3.169 110.357 37.972 1.00 46.20 C ANISOU 3303 CB THR C 21 8087 5262 4205 -241 288 -198 C ATOM 3304 OG1 THR C 21 2.238 111.213 38.644 1.00 46.39 O ANISOU 3304 OG1 THR C 21 8025 5419 4183 -391 468 -221 O ATOM 3305 CG2 THR C 21 4.449 110.211 38.768 1.00 46.51 C ANISOU 3305 CG2 THR C 21 8313 5207 4152 -95 115 -135 C ATOM 3306 N CYS C 22 1.880 109.842 35.070 1.00 45.94 N ANISOU 3306 N CYS C 22 7689 5304 4461 -265 348 -356 N ATOM 3307 CA CYS C 22 0.623 109.644 34.366 1.00 46.13 C ANISOU 3307 CA CYS C 22 7595 5367 4564 -418 445 -417 C ATOM 3308 C CYS C 22 -0.164 108.567 35.105 1.00 48.29 C ANISOU 3308 C CYS C 22 8096 5496 4757 -659 507 -360 C ATOM 3309 O CYS C 22 0.357 107.477 35.323 1.00 48.64 O ANISOU 3309 O CYS C 22 8409 5336 4736 -648 392 -297 O ATOM 3310 CB CYS C 22 0.897 109.194 32.934 1.00 45.67 C ANISOU 3310 CB CYS C 22 7467 5286 4599 -292 340 -482 C ATOM 3311 SG CYS C 22 -0.583 109.110 31.899 1.00 46.51 S ANISOU 3311 SG CYS C 22 7393 5460 4817 -447 414 -576 S ATOM 3312 N THR C 23 -1.405 108.869 35.487 1.00 49.25 N ANISOU 3312 N THR C 23 8110 5720 4882 -876 683 -385 N ATOM 3313 CA THR C 23 -2.284 107.882 36.130 1.00 52.08 C ANISOU 3313 CA THR C 23 8651 5973 5166 -1162 776 -329 C ATOM 3314 C THR C 23 -3.358 107.449 35.129 1.00 53.03 C ANISOU 3314 C THR C 23 8614 6112 5424 -1301 808 -413 C ATOM 3315 O THR C 23 -4.047 108.284 34.535 1.00 52.04 O ANISOU 3315 O THR C 23 8180 6176 5416 -1286 878 -520 O ATOM 3316 CB THR C 23 -2.916 108.395 37.456 1.00 53.63 C ANISOU 3316 CB THR C 23 8855 6285 5236 -1345 977 -298 C ATOM 3317 OG1 THR C 23 -4.110 109.141 37.196 1.00 54.49 O ANISOU 3317 OG1 THR C 23 8642 6613 5449 -1449 1147 -415 O ATOM 3318 CG2 THR C 23 -1.939 109.262 38.250 1.00 52.38 C ANISOU 3318 CG2 THR C 23 8749 6175 4976 -1164 941 -267 C ATOM 3319 N VAL C 24 -3.471 106.136 34.940 1.00 55.10 N ANISOU 3319 N VAL C 24 9104 6159 5673 -1427 727 -367 N ATOM 3320 CA VAL C 24 -4.448 105.540 34.043 1.00 56.49 C ANISOU 3320 CA VAL C 24 9180 6312 5971 -1585 724 -441 C ATOM 3321 C VAL C 24 -5.658 105.093 34.864 1.00 59.73 C ANISOU 3321 C VAL C 24 9621 6735 6339 -1963 907 -399 C ATOM 3322 O VAL C 24 -5.501 104.432 35.894 1.00 61.91 O ANISOU 3322 O VAL C 24 10197 6864 6462 -2123 940 -268 O ATOM 3323 CB VAL C 24 -3.844 104.333 33.295 1.00 57.06 C ANISOU 3323 CB VAL C 24 9496 6122 6061 -1501 508 -433 C ATOM 3324 CG1 VAL C 24 -4.861 103.715 32.342 1.00 58.12 C ANISOU 3324 CG1 VAL C 24 9539 6222 6322 -1669 483 -523 C ATOM 3325 CG2 VAL C 24 -2.587 104.757 32.554 1.00 54.73 C ANISOU 3325 CG2 VAL C 24 9157 5849 5787 -1132 358 -481 C ATOM 3326 N SER C 25 -6.851 105.470 34.404 1.00 61.23 N ANISOU 3326 N SER C 25 9497 7108 6659 -2107 1023 -511 N ATOM 3327 CA SER C 25 -8.120 105.067 35.025 1.00 65.06 C ANISOU 3327 CA SER C 25 9929 7656 7136 -2487 1217 -502 C ATOM 3328 C SER C 25 -9.058 104.473 33.976 1.00 67.04 C ANISOU 3328 C SER C 25 10025 7886 7561 -2644 1159 -601 C ATOM 3329 O SER C 25 -9.006 104.848 32.809 1.00 65.70 O ANISOU 3329 O SER C 25 9665 7770 7528 -2439 1027 -716 O ATOM 3330 CB SER C 25 -8.788 106.265 35.703 1.00 64.89 C ANISOU 3330 CB SER C 25 9607 7942 7109 -2520 1449 -576 C ATOM 3331 OG SER C 25 -8.921 107.347 34.797 1.00 62.88 O ANISOU 3331 OG SER C 25 9009 7870 7014 -2279 1398 -725 O ATOM 3332 N GLY C 26 -9.906 103.541 34.408 1.00 71.46 N ANISOU 3332 N GLY C 26 10681 8366 8104 -3023 1252 -548 N ATOM 3333 CA GLY C 26 -10.807 102.806 33.511 1.00 73.71 C ANISOU 3333 CA GLY C 26 10860 8595 8551 -3226 1179 -631 C ATOM 3334 C GLY C 26 -10.130 101.778 32.610 1.00 74.38 C ANISOU 3334 C GLY C 26 11235 8363 8662 -3117 898 -614 C ATOM 3335 O GLY C 26 -10.742 101.282 31.658 1.00 75.12 O ANISOU 3335 O GLY C 26 11236 8408 8900 -3210 787 -713 O ATOM 3336 N GLY C 27 -8.880 101.438 32.924 1.00 73.84 N ANISOU 3336 N GLY C 27 11517 8081 8458 -2916 774 -504 N ATOM 3337 CA GLY C 27 -8.081 100.508 32.126 1.00 73.69 C ANISOU 3337 CA GLY C 27 11781 7766 8451 -2745 504 -508 C ATOM 3338 C GLY C 27 -6.764 100.222 32.826 1.00 73.56 C ANISOU 3338 C GLY C 27 12126 7552 8271 -2548 408 -378 C ATOM 3339 O GLY C 27 -6.459 100.858 33.844 1.00 73.08 O ANISOU 3339 O GLY C 27 12072 7604 8090 -2527 543 -290 O ATOM 3340 N SER C 28 -5.978 99.296 32.270 1.00 73.88 N ANISOU 3340 N SER C 28 12456 7306 8310 -2382 162 -383 N ATOM 3341 CA SER C 28 -4.718 98.845 32.875 1.00 73.94 C ANISOU 3341 CA SER C 28 12824 7086 8182 -2179 20 -276 C ATOM 3342 C SER C 28 -3.590 98.874 31.854 1.00 71.59 C ANISOU 3342 C SER C 28 12517 6751 7934 -1748 -185 -396 C ATOM 3343 O SER C 28 -3.836 99.008 30.658 1.00 70.73 O ANISOU 3343 O SER C 28 12203 6731 7938 -1650 -235 -546 O ATOM 3344 CB SER C 28 -4.875 97.430 33.439 1.00 77.51 C ANISOU 3344 CB SER C 28 13729 7160 8562 -2440 -94 -146 C ATOM 3345 OG SER C 28 -5.827 97.404 34.486 1.00 80.09 O ANISOU 3345 OG SER C 28 14085 7539 8807 -2858 123 -15 O ATOM 3346 N TYR C 32 0.145 96.893 26.250 1.00 63.40 N ANISOU 3346 N TYR C 32 11651 5378 7059 -176 -1092 -1169 N ATOM 3347 CA TYR C 32 0.383 98.033 25.359 1.00 60.98 C ANISOU 3347 CA TYR C 32 10978 5436 6756 7 -975 -1265 C ATOM 3348 C TYR C 32 1.633 98.811 25.762 1.00 58.75 C ANISOU 3348 C TYR C 32 10573 5333 6418 280 -919 -1225 C ATOM 3349 O TYR C 32 2.333 98.432 26.711 1.00 59.68 O ANISOU 3349 O TYR C 32 10885 5290 6499 353 -989 -1139 O ATOM 3350 CB TYR C 32 -0.846 98.961 25.322 1.00 59.72 C ANISOU 3350 CB TYR C 32 10536 5507 6648 -274 -793 -1217 C ATOM 3351 CG TYR C 32 -2.151 98.212 25.168 1.00 62.34 C ANISOU 3351 CG TYR C 32 10962 5672 7052 -602 -836 -1235 C ATOM 3352 CD1 TYR C 32 -2.316 97.281 24.142 1.00 64.29 C ANISOU 3352 CD1 TYR C 32 11356 5745 7328 -556 -1017 -1389 C ATOM 3353 CD2 TYR C 32 -3.216 98.421 26.046 1.00 62.92 C ANISOU 3353 CD2 TYR C 32 10974 5769 7166 -964 -696 -1112 C ATOM 3354 CE1 TYR C 32 -3.503 96.580 23.987 1.00 66.71 C ANISOU 3354 CE1 TYR C 32 11743 5890 7713 -876 -1076 -1410 C ATOM 3355 CE2 TYR C 32 -4.411 97.723 25.899 1.00 65.20 C ANISOU 3355 CE2 TYR C 32 11318 5922 7533 -1291 -730 -1133 C ATOM 3356 CZ TYR C 32 -4.551 96.807 24.864 1.00 67.22 C ANISOU 3356 CZ TYR C 32 11718 5992 7829 -1253 -929 -1278 C ATOM 3357 OH TYR C 32 -5.724 96.104 24.694 1.00 69.45 O ANISOU 3357 OH TYR C 32 12052 6133 8203 -1593 -982 -1305 O ATOM 3358 N PHE C 33 1.916 99.873 25.003 1.00 56.31 N ANISOU 3358 N PHE C 33 9951 5343 6101 424 -811 -1288 N ATOM 3359 CA PHE C 33 2.986 100.820 25.310 1.00 54.22 C ANISOU 3359 CA PHE C 33 9505 5297 5798 629 -731 -1245 C ATOM 3360 C PHE C 33 2.414 102.076 25.952 1.00 51.83 C ANISOU 3360 C PHE C 33 8981 5203 5510 433 -547 -1113 C ATOM 3361 O PHE C 33 1.249 102.426 25.752 1.00 51.66 O ANISOU 3361 O PHE C 33 8849 5248 5530 208 -465 -1103 O ATOM 3362 CB PHE C 33 3.743 101.236 24.053 1.00 53.56 C ANISOU 3362 CB PHE C 33 9227 5441 5681 900 -721 -1390 C ATOM 3363 CG PHE C 33 4.502 100.129 23.393 1.00 55.52 C ANISOU 3363 CG PHE C 33 9652 5540 5903 1162 -885 -1557 C ATOM 3364 CD1 PHE C 33 3.854 99.242 22.540 1.00 57.22 C ANISOU 3364 CD1 PHE C 33 10019 5599 6124 1126 -992 -1687 C ATOM 3365 CD2 PHE C 33 5.874 99.997 23.586 1.00 55.94 C ANISOU 3365 CD2 PHE C 33 9701 5621 5931 1460 -941 -1605 C ATOM 3366 CE1 PHE C 33 4.554 98.224 21.907 1.00 59.51 C ANISOU 3366 CE1 PHE C 33 10481 5745 6385 1393 -1152 -1868 C ATOM 3367 CE2 PHE C 33 6.580 98.985 22.954 1.00 58.43 C ANISOU 3367 CE2 PHE C 33 10160 5813 6228 1737 -1094 -1790 C ATOM 3368 CZ PHE C 33 5.920 98.096 22.115 1.00 60.05 C ANISOU 3368 CZ PHE C 33 10540 5847 6429 1710 -1198 -1925 C ATOM 3369 N TRP C 34 3.265 102.761 26.708 1.00 50.33 N ANISOU 3369 N TRP C 34 8716 5116 5290 538 -499 -1031 N ATOM 3370 CA TRP C 34 2.872 103.915 27.507 1.00 48.02 C ANISOU 3370 CA TRP C 34 8259 4986 5002 382 -347 -912 C ATOM 3371 C TRP C 34 3.906 105.000 27.275 1.00 45.80 C ANISOU 3371 C TRP C 34 7748 4946 4706 586 -300 -917 C ATOM 3372 O TRP C 34 5.090 104.787 27.509 1.00 46.67 O ANISOU 3372 O TRP C 34 7905 5036 4791 792 -379 -928 O ATOM 3373 CB TRP C 34 2.757 103.483 28.963 1.00 49.07 C ANISOU 3373 CB TRP C 34 8617 4930 5096 236 -358 -782 C ATOM 3374 CG TRP C 34 1.778 102.356 29.050 1.00 51.24 C ANISOU 3374 CG TRP C 34 9123 4964 5382 12 -406 -774 C ATOM 3375 CD1 TRP C 34 2.058 101.017 29.047 1.00 53.47 C ANISOU 3375 CD1 TRP C 34 9717 4952 5649 59 -580 -797 C ATOM 3376 CD2 TRP C 34 0.354 102.467 29.030 1.00 51.59 C ANISOU 3376 CD2 TRP C 34 9089 5041 5471 -291 -292 -760 C ATOM 3377 NE1 TRP C 34 0.893 100.291 29.070 1.00 55.13 N ANISOU 3377 NE1 TRP C 34 10066 4996 5886 -230 -579 -778 N ATOM 3378 CE2 TRP C 34 -0.168 101.155 29.064 1.00 53.99 C ANISOU 3378 CE2 TRP C 34 9667 5064 5781 -452 -395 -759 C ATOM 3379 CE3 TRP C 34 -0.534 103.550 29.011 1.00 50.26 C ANISOU 3379 CE3 TRP C 34 8639 5109 5347 -439 -124 -756 C ATOM 3380 CZ2 TRP C 34 -1.540 100.896 29.084 1.00 55.21 C ANISOU 3380 CZ2 TRP C 34 9800 5189 5987 -782 -318 -750 C ATOM 3381 CZ3 TRP C 34 -1.901 103.294 29.036 1.00 51.39 C ANISOU 3381 CZ3 TRP C 34 8748 5233 5545 -734 -52 -762 C ATOM 3382 CH2 TRP C 34 -2.390 101.975 29.071 1.00 53.84 C ANISOU 3382 CH2 TRP C 34 9312 5283 5863 -915 -140 -757 C ATOM 3383 N SER C 35 3.450 106.152 26.793 1.00 43.23 N ANISOU 3383 N SER C 35 7177 4844 4405 523 -186 -913 N ATOM 3384 CA SER C 35 4.326 107.089 26.095 1.00 41.19 C ANISOU 3384 CA SER C 35 6704 4815 4131 696 -151 -940 C ATOM 3385 C SER C 35 4.237 108.507 26.628 1.00 38.45 C ANISOU 3385 C SER C 35 6174 4634 3803 616 -47 -846 C ATOM 3386 O SER C 35 3.228 108.910 27.218 1.00 37.12 O ANISOU 3386 O SER C 35 5989 4451 3665 430 19 -795 O ATOM 3387 CB SER C 35 3.989 107.090 24.598 1.00 41.48 C ANISOU 3387 CB SER C 35 6649 4954 4155 739 -153 -1046 C ATOM 3388 OG SER C 35 4.993 107.759 23.849 1.00 41.43 O ANISOU 3388 OG SER C 35 6481 5158 4104 911 -122 -1074 O ATOM 3389 N TRP C 36 5.324 109.242 26.402 1.00 37.10 N ANISOU 3389 N TRP C 36 5861 4622 3614 760 -36 -836 N ATOM 3390 CA TRP C 36 5.418 110.662 26.687 1.00 35.31 C ANISOU 3390 CA TRP C 36 5459 4552 3405 709 38 -759 C ATOM 3391 C TRP C 36 5.761 111.410 25.393 1.00 34.80 C ANISOU 3391 C TRP C 36 5217 4686 3321 777 70 -787 C ATOM 3392 O TRP C 36 6.634 110.982 24.629 1.00 35.05 O ANISOU 3392 O TRP C 36 5225 4788 3306 927 49 -852 O ATOM 3393 CB TRP C 36 6.480 110.916 27.766 1.00 35.35 C ANISOU 3393 CB TRP C 36 5475 4553 3405 780 8 -699 C ATOM 3394 CG TRP C 36 6.045 110.446 29.126 1.00 35.34 C ANISOU 3394 CG TRP C 36 5661 4375 3392 679 -12 -643 C ATOM 3395 CD1 TRP C 36 6.364 109.259 29.726 1.00 36.70 C ANISOU 3395 CD1 TRP C 36 6053 4361 3531 730 -105 -645 C ATOM 3396 CD2 TRP C 36 5.185 111.139 30.042 1.00 34.71 C ANISOU 3396 CD2 TRP C 36 5582 4289 3316 507 65 -580 C ATOM 3397 NE1 TRP C 36 5.771 109.177 30.967 1.00 36.68 N ANISOU 3397 NE1 TRP C 36 6203 4239 3493 577 -84 -566 N ATOM 3398 CE2 TRP C 36 5.037 110.313 31.184 1.00 35.73 C ANISOU 3398 CE2 TRP C 36 5940 4243 3393 441 34 -536 C ATOM 3399 CE3 TRP C 36 4.531 112.378 30.015 1.00 33.64 C ANISOU 3399 CE3 TRP C 36 5288 4276 3217 411 150 -563 C ATOM 3400 CZ2 TRP C 36 4.266 110.690 32.291 1.00 35.72 C ANISOU 3400 CZ2 TRP C 36 5998 4217 3358 272 115 -480 C ATOM 3401 CZ3 TRP C 36 3.754 112.751 31.114 1.00 33.63 C ANISOU 3401 CZ3 TRP C 36 5331 4242 3205 271 217 -529 C ATOM 3402 CH2 TRP C 36 3.632 111.905 32.237 1.00 34.65 C ANISOU 3402 CH2 TRP C 36 5676 4226 3264 197 214 -490 C ATOM 3403 N ILE C 37 5.051 112.511 25.162 1.00 33.89 N ANISOU 3403 N ILE C 37 4988 4658 3230 668 119 -743 N ATOM 3404 CA ILE C 37 5.254 113.395 24.015 1.00 34.12 C ANISOU 3404 CA ILE C 37 4880 4858 3224 691 142 -733 C ATOM 3405 C ILE C 37 5.220 114.809 24.577 1.00 33.55 C ANISOU 3405 C ILE C 37 4705 4845 3197 611 167 -637 C ATOM 3406 O ILE C 37 4.455 115.081 25.506 1.00 33.45 O ANISOU 3406 O ILE C 37 4719 4748 3244 520 175 -616 O ATOM 3407 CB ILE C 37 4.123 113.224 22.967 1.00 34.35 C ANISOU 3407 CB ILE C 37 4923 4887 3241 638 121 -792 C ATOM 3408 CG1 ILE C 37 4.080 111.778 22.448 1.00 35.69 C ANISOU 3408 CG1 ILE C 37 5222 4968 3372 709 76 -903 C ATOM 3409 CG2 ILE C 37 4.268 114.201 21.802 1.00 34.59 C ANISOU 3409 CG2 ILE C 37 4852 5082 3210 650 129 -762 C ATOM 3410 CD1 ILE C 37 3.058 110.912 23.148 1.00 36.10 C ANISOU 3410 CD1 ILE C 37 5397 4830 3491 598 44 -933 C ATOM 3411 N ARG C 38 6.044 115.705 24.044 1.00 33.90 N ANISOU 3411 N ARG C 38 4641 5031 3210 637 183 -583 N ATOM 3412 CA ARG C 38 6.010 117.105 24.485 1.00 33.51 C ANISOU 3412 CA ARG C 38 4516 5011 3207 556 182 -493 C ATOM 3413 C ARG C 38 5.803 118.063 23.328 1.00 33.32 C ANISOU 3413 C ARG C 38 4430 5086 3145 514 173 -445 C ATOM 3414 O ARG C 38 5.959 117.698 22.154 1.00 33.59 O ANISOU 3414 O ARG C 38 4465 5208 3090 553 186 -472 O ATOM 3415 CB ARG C 38 7.266 117.480 25.285 1.00 34.23 C ANISOU 3415 CB ARG C 38 4553 5140 3312 582 181 -441 C ATOM 3416 CG ARG C 38 8.570 117.322 24.526 1.00 35.87 C ANISOU 3416 CG ARG C 38 4666 5502 3459 660 209 -442 C ATOM 3417 CD ARG C 38 9.744 117.771 25.372 1.00 36.33 C ANISOU 3417 CD ARG C 38 4641 5604 3560 670 189 -397 C ATOM 3418 NE ARG C 38 10.965 117.885 24.576 1.00 37.95 N ANISOU 3418 NE ARG C 38 4697 6004 3720 711 236 -394 N ATOM 3419 CZ ARG C 38 12.145 118.275 25.055 1.00 38.76 C ANISOU 3419 CZ ARG C 38 4671 6195 3861 715 222 -367 C ATOM 3420 NH1 ARG C 38 12.287 118.588 26.341 1.00 38.35 N ANISOU 3420 NH1 ARG C 38 4648 6037 3885 693 144 -339 N ATOM 3421 NH2 ARG C 38 13.191 118.361 24.240 1.00 40.37 N ANISOU 3421 NH2 ARG C 38 4708 6609 4021 736 290 -375 N ATOM 3422 N GLN C 39 5.439 119.290 23.685 1.00 32.30 N ANISOU 3422 N GLN C 39 4271 4930 3073 439 140 -378 N ATOM 3423 CA GLN C 39 5.158 120.337 22.720 1.00 32.42 C ANISOU 3423 CA GLN C 39 4265 4995 3059 389 97 -312 C ATOM 3424 C GLN C 39 5.565 121.685 23.324 1.00 32.45 C ANISOU 3424 C GLN C 39 4235 4975 3119 324 59 -217 C ATOM 3425 O GLN C 39 4.853 122.199 24.189 1.00 31.14 O ANISOU 3425 O GLN C 39 4084 4702 3045 307 17 -237 O ATOM 3426 CB GLN C 39 3.671 120.330 22.372 1.00 31.98 C ANISOU 3426 CB GLN C 39 4240 4867 3043 380 37 -371 C ATOM 3427 CG GLN C 39 3.285 121.248 21.222 1.00 32.65 C ANISOU 3427 CG GLN C 39 4339 4985 3081 354 -45 -312 C ATOM 3428 CD GLN C 39 1.830 121.087 20.816 1.00 33.04 C ANISOU 3428 CD GLN C 39 4399 4976 3177 368 -128 -396 C ATOM 3429 OE1 GLN C 39 0.959 120.826 21.646 1.00 32.36 O ANISOU 3429 OE1 GLN C 39 4277 4815 3203 366 -126 -479 O ATOM 3430 NE2 GLN C 39 1.563 121.238 19.530 1.00 33.95 N ANISOU 3430 NE2 GLN C 39 4559 5139 3200 375 -200 -377 N ATOM 3431 N PRO C 40 6.708 122.259 22.875 1.00 33.36 N ANISOU 3431 N PRO C 40 4304 5192 3178 279 77 -122 N ATOM 3432 CA PRO C 40 7.053 123.611 23.331 1.00 33.55 C ANISOU 3432 CA PRO C 40 4316 5172 3260 190 16 -24 C ATOM 3433 C PRO C 40 5.977 124.616 22.911 1.00 34.11 C ANISOU 3433 C PRO C 40 4457 5142 3361 155 -90 11 C ATOM 3434 O PRO C 40 5.340 124.414 21.866 1.00 35.00 O ANISOU 3434 O PRO C 40 4609 5280 3408 173 -111 3 O ATOM 3435 CB PRO C 40 8.395 123.904 22.638 1.00 34.90 C ANISOU 3435 CB PRO C 40 4414 5499 3347 119 70 72 C ATOM 3436 CG PRO C 40 8.907 122.588 22.146 1.00 35.02 C ANISOU 3436 CG PRO C 40 4379 5650 3278 212 173 -8 C ATOM 3437 CD PRO C 40 7.696 121.734 21.911 1.00 34.41 C ANISOU 3437 CD PRO C 40 4388 5493 3192 297 157 -109 C ATOM 3438 N PRO C 41 5.747 125.676 23.712 1.00 34.41 N ANISOU 3438 N PRO C 41 4519 5057 3497 122 -178 34 N ATOM 3439 CA PRO C 41 4.637 126.590 23.383 1.00 34.91 C ANISOU 3439 CA PRO C 41 4649 5005 3611 131 -306 37 C ATOM 3440 C PRO C 41 4.728 127.165 21.959 1.00 36.38 C ANISOU 3440 C PRO C 41 4902 5224 3697 68 -370 158 C ATOM 3441 O PRO C 41 5.767 127.699 21.568 1.00 36.43 O ANISOU 3441 O PRO C 41 4921 5286 3636 -44 -356 290 O ATOM 3442 CB PRO C 41 4.756 127.693 24.438 1.00 35.02 C ANISOU 3442 CB PRO C 41 4687 4891 3729 105 -389 50 C ATOM 3443 CG PRO C 41 5.478 127.051 25.578 1.00 34.24 C ANISOU 3443 CG PRO C 41 4534 4830 3646 114 -295 1 C ATOM 3444 CD PRO C 41 6.439 126.085 24.948 1.00 34.14 C ANISOU 3444 CD PRO C 41 4462 4975 3534 95 -186 40 C ATOM 3445 N GLY C 42 3.653 127.005 21.194 1.00 37.11 N ANISOU 3445 N GLY C 42 5035 5294 3770 128 -439 113 N ATOM 3446 CA GLY C 42 3.599 127.462 19.803 1.00 39.20 C ANISOU 3446 CA GLY C 42 5398 5584 3911 80 -519 223 C ATOM 3447 C GLY C 42 4.405 126.663 18.785 1.00 39.93 C ANISOU 3447 C GLY C 42 5487 5865 3819 36 -391 270 C ATOM 3448 O GLY C 42 4.545 127.100 17.649 1.00 42.23 O ANISOU 3448 O GLY C 42 5876 6200 3969 -31 -435 382 O ATOM 3449 N LYS C 43 4.907 125.488 19.168 1.00 39.23 N ANISOU 3449 N LYS C 43 5301 5885 3720 82 -241 178 N ATOM 3450 CA LYS C 43 5.772 124.674 18.303 1.00 40.05 C ANISOU 3450 CA LYS C 43 5381 6179 3659 73 -109 186 C ATOM 3451 C LYS C 43 5.145 123.285 18.106 1.00 38.92 C ANISOU 3451 C LYS C 43 5229 6061 3498 194 -72 27 C ATOM 3452 O LYS C 43 4.002 123.072 18.498 1.00 37.83 O ANISOU 3452 O LYS C 43 5102 5804 3466 251 -152 -63 O ATOM 3453 CB LYS C 43 7.186 124.608 18.907 1.00 40.50 C ANISOU 3453 CB LYS C 43 5324 6339 3723 23 14 222 C ATOM 3454 CG LYS C 43 7.948 125.929 18.819 1.00 42.50 C ANISOU 3454 CG LYS C 43 5588 6598 3963 -141 -13 394 C ATOM 3455 CD LYS C 43 8.548 126.136 17.430 1.00 45.50 C ANISOU 3455 CD LYS C 43 6005 7149 4134 -248 57 507 C ATOM 3456 CE LYS C 43 9.188 127.510 17.247 1.00 47.82 C ANISOU 3456 CE LYS C 43 6342 7424 4402 -455 16 705 C ATOM 3457 NZ LYS C 43 8.360 128.449 16.430 1.00 49.23 N ANISOU 3457 NZ LYS C 43 6728 7472 4507 -522 -142 827 N ATOM 3458 N GLY C 44 5.872 122.363 17.471 1.00 39.13 N ANISOU 3458 N GLY C 44 5233 6244 3393 230 44 -16 N ATOM 3459 CA GLY C 44 5.352 121.034 17.142 1.00 38.62 C ANISOU 3459 CA GLY C 44 5190 6188 3294 338 60 -167 C ATOM 3460 C GLY C 44 5.519 119.980 18.223 1.00 37.01 C ANISOU 3460 C GLY C 44 4929 5930 3202 417 117 -281 C ATOM 3461 O GLY C 44 6.173 120.204 19.245 1.00 36.49 O ANISOU 3461 O GLY C 44 4796 5844 3224 403 155 -249 O ATOM 3462 N LEU C 45 4.921 118.821 17.979 1.00 36.44 N ANISOU 3462 N LEU C 45 4906 5822 3119 494 105 -411 N ATOM 3463 CA LEU C 45 5.011 117.676 18.891 1.00 35.67 C ANISOU 3463 CA LEU C 45 4803 5646 3105 562 139 -515 C ATOM 3464 C LEU C 45 6.385 117.025 18.770 1.00 36.52 C ANISOU 3464 C LEU C 45 4870 5875 3133 649 234 -548 C ATOM 3465 O LEU C 45 6.959 116.994 17.688 1.00 38.36 O ANISOU 3465 O LEU C 45 5092 6264 3219 678 286 -555 O ATOM 3466 CB LEU C 45 3.918 116.648 18.580 1.00 35.54 C ANISOU 3466 CB LEU C 45 4867 5535 3103 592 79 -639 C ATOM 3467 CG LEU C 45 2.465 117.129 18.626 1.00 35.31 C ANISOU 3467 CG LEU C 45 4840 5408 3166 521 -21 -645 C ATOM 3468 CD1 LEU C 45 1.536 116.071 18.041 1.00 36.12 C ANISOU 3468 CD1 LEU C 45 5006 5455 3261 536 -86 -773 C ATOM 3469 CD2 LEU C 45 2.049 117.478 20.044 1.00 34.13 C ANISOU 3469 CD2 LEU C 45 4639 5153 3175 468 -10 -626 C ATOM 3470 N GLU C 46 6.908 116.529 19.889 1.00 36.77 N ANISOU 3470 N GLU C 46 4874 5842 3254 695 254 -575 N ATOM 3471 CA GLU C 46 8.180 115.808 19.926 1.00 38.12 C ANISOU 3471 CA GLU C 46 4992 6109 3385 813 314 -635 C ATOM 3472 C GLU C 46 8.003 114.571 20.784 1.00 37.92 C ANISOU 3472 C GLU C 46 5057 5916 3434 902 266 -732 C ATOM 3473 O GLU C 46 7.688 114.678 21.971 1.00 37.85 O ANISOU 3473 O GLU C 46 5080 5774 3529 851 231 -691 O ATOM 3474 CB GLU C 46 9.305 116.674 20.497 1.00 38.71 C ANISOU 3474 CB GLU C 46 4929 6285 3495 775 358 -541 C ATOM 3475 CG GLU C 46 10.671 116.000 20.402 1.00 40.61 C ANISOU 3475 CG GLU C 46 5063 6668 3699 910 418 -620 C ATOM 3476 CD GLU C 46 11.804 116.834 20.966 1.00 41.57 C ANISOU 3476 CD GLU C 46 5019 6904 3873 858 449 -537 C ATOM 3477 OE1 GLU C 46 12.961 116.613 20.558 1.00 43.75 O ANISOU 3477 OE1 GLU C 46 5147 7376 4102 934 523 -589 O ATOM 3478 OE2 GLU C 46 11.549 117.698 21.830 1.00 40.75 O ANISOU 3478 OE2 GLU C 46 4922 6701 3861 746 396 -436 O ATOM 3479 N TRP C 47 8.229 113.407 20.187 1.00 39.06 N ANISOU 3479 N TRP C 47 5262 6065 3513 1033 262 -861 N ATOM 3480 CA TRP C 47 8.158 112.134 20.898 1.00 39.76 C ANISOU 3480 CA TRP C 47 5474 5972 3661 1124 195 -952 C ATOM 3481 C TRP C 47 9.349 112.023 21.852 1.00 39.88 C ANISOU 3481 C TRP C 47 5425 5999 3729 1219 189 -941 C ATOM 3482 O TRP C 47 10.479 112.290 21.467 1.00 40.58 O ANISOU 3482 O TRP C 47 5366 6276 3777 1304 245 -959 O ATOM 3483 CB TRP C 47 8.161 110.986 19.885 1.00 41.24 C ANISOU 3483 CB TRP C 47 5753 6157 3760 1257 171 -1108 C ATOM 3484 CG TRP C 47 7.928 109.645 20.463 1.00 42.16 C ANISOU 3484 CG TRP C 47 6043 6044 3932 1333 74 -1200 C ATOM 3485 CD1 TRP C 47 6.745 109.144 20.933 1.00 42.06 C ANISOU 3485 CD1 TRP C 47 6182 5814 3985 1213 4 -1192 C ATOM 3486 CD2 TRP C 47 8.900 108.607 20.628 1.00 43.75 C ANISOU 3486 CD2 TRP C 47 6294 6199 4130 1540 24 -1314 C ATOM 3487 NE1 TRP C 47 6.924 107.856 21.385 1.00 43.32 N ANISOU 3487 NE1 TRP C 47 6511 5775 4171 1309 -88 -1274 N ATOM 3488 CE2 TRP C 47 8.237 107.503 21.211 1.00 44.25 C ANISOU 3488 CE2 TRP C 47 6580 5981 4251 1528 -92 -1355 C ATOM 3489 CE3 TRP C 47 10.269 108.502 20.342 1.00 45.13 C ANISOU 3489 CE3 TRP C 47 6337 6546 4263 1735 62 -1394 C ATOM 3490 CZ2 TRP C 47 8.896 106.305 21.511 1.00 45.92 C ANISOU 3490 CZ2 TRP C 47 6924 6045 4479 1718 -197 -1464 C ATOM 3491 CZ3 TRP C 47 10.926 107.307 20.639 1.00 46.89 C ANISOU 3491 CZ3 TRP C 47 6656 6647 4513 1950 -38 -1527 C ATOM 3492 CH2 TRP C 47 10.234 106.224 21.219 1.00 47.10 C ANISOU 3492 CH2 TRP C 47 6942 6357 4595 1946 -179 -1557 C ATOM 3493 N ILE C 48 9.087 111.668 23.104 1.00 39.83 N ANISOU 3493 N ILE C 48 5523 5802 3807 1192 122 -910 N ATOM 3494 CA ILE C 48 10.146 111.513 24.109 1.00 40.44 C ANISOU 3494 CA ILE C 48 5572 5860 3933 1288 77 -899 C ATOM 3495 C ILE C 48 10.520 110.044 24.243 1.00 41.99 C ANISOU 3495 C ILE C 48 5911 5916 4127 1469 -19 -1019 C ATOM 3496 O ILE C 48 11.698 109.704 24.256 1.00 42.87 O ANISOU 3496 O ILE C 48 5939 6106 4243 1650 -52 -1091 O ATOM 3497 CB ILE C 48 9.725 112.084 25.482 1.00 39.32 C ANISOU 3497 CB ILE C 48 5484 5596 3858 1154 48 -784 C ATOM 3498 CG1 ILE C 48 9.428 113.586 25.355 1.00 38.37 C ANISOU 3498 CG1 ILE C 48 5230 5598 3751 1003 118 -682 C ATOM 3499 CG2 ILE C 48 10.810 111.849 26.537 1.00 39.93 C ANISOU 3499 CG2 ILE C 48 5562 5639 3972 1262 -33 -778 C ATOM 3500 CD1 ILE C 48 8.599 114.161 26.487 1.00 37.16 C ANISOU 3500 CD1 ILE C 48 5148 5322 3648 862 106 -603 C ATOM 3501 N GLY C 49 9.517 109.181 24.369 1.00 42.17 N ANISOU 3501 N GLY C 49 6146 5724 4154 1419 -76 -1045 N ATOM 3502 CA GLY C 49 9.757 107.745 24.496 1.00 43.67 C ANISOU 3502 CA GLY C 49 6525 5724 4343 1574 -196 -1152 C ATOM 3503 C GLY C 49 8.501 106.979 24.854 1.00 43.54 C ANISOU 3503 C GLY C 49 6753 5449 4342 1430 -252 -1134 C ATOM 3504 O GLY C 49 7.435 107.562 25.049 1.00 42.27 O ANISOU 3504 O GLY C 49 6584 5279 4197 1216 -187 -1049 O ATOM 3505 N TYR C 50 8.631 105.662 24.935 1.00 45.26 N ANISOU 3505 N TYR C 50 7182 5454 4559 1546 -380 -1221 N ATOM 3506 CA TYR C 50 7.580 104.837 25.520 1.00 45.81 C ANISOU 3506 CA TYR C 50 7514 5244 4648 1384 -450 -1180 C ATOM 3507 C TYR C 50 8.136 103.635 26.269 1.00 47.63 C ANISOU 3507 C TYR C 50 8003 5208 4884 1515 -623 -1203 C ATOM 3508 O TYR C 50 9.307 103.286 26.132 1.00 48.48 O ANISOU 3508 O TYR C 50 8082 5346 4994 1780 -709 -1296 O ATOM 3509 CB TYR C 50 6.492 104.436 24.499 1.00 46.27 C ANISOU 3509 CB TYR C 50 7623 5260 4697 1277 -439 -1257 C ATOM 3510 CG TYR C 50 6.877 103.633 23.259 1.00 47.96 C ANISOU 3510 CG TYR C 50 7878 5477 4869 1481 -509 -1441 C ATOM 3511 CD1 TYR C 50 8.162 103.111 23.053 1.00 49.55 C ANISOU 3511 CD1 TYR C 50 8079 5701 5048 1776 -582 -1558 C ATOM 3512 CD2 TYR C 50 5.910 103.358 22.289 1.00 48.70 C ANISOU 3512 CD2 TYR C 50 8010 5548 4944 1385 -514 -1518 C ATOM 3513 CE1 TYR C 50 8.464 102.374 21.918 1.00 51.44 C ANISOU 3513 CE1 TYR C 50 8357 5951 5236 1972 -636 -1752 C ATOM 3514 CE2 TYR C 50 6.210 102.617 21.153 1.00 50.21 C ANISOU 3514 CE2 TYR C 50 8263 5738 5078 1569 -583 -1701 C ATOM 3515 CZ TYR C 50 7.490 102.126 20.972 1.00 51.83 C ANISOU 3515 CZ TYR C 50 8471 5973 5249 1867 -635 -1822 C ATOM 3516 OH TYR C 50 7.802 101.392 19.848 1.00 53.82 O ANISOU 3516 OH TYR C 50 8780 6237 5431 2072 -694 -2030 O ATOM 3517 N ILE C 51 7.280 103.044 27.094 1.00 48.23 N ANISOU 3517 N ILE C 51 8328 5032 4964 1321 -674 -1113 N ATOM 3518 CA ILE C 51 7.614 101.851 27.868 1.00 50.34 C ANISOU 3518 CA ILE C 51 8913 4988 5224 1395 -860 -1102 C ATOM 3519 C ILE C 51 6.562 100.789 27.559 1.00 51.88 C ANISOU 3519 C ILE C 51 9362 4925 5425 1236 -926 -1130 C ATOM 3520 O ILE C 51 5.372 101.087 27.523 1.00 51.09 O ANISOU 3520 O ILE C 51 9229 4848 5334 957 -812 -1070 O ATOM 3521 CB ILE C 51 7.724 102.155 29.391 1.00 49.86 C ANISOU 3521 CB ILE C 51 8961 4849 5134 1284 -871 -931 C ATOM 3522 CG1 ILE C 51 8.183 100.915 30.167 1.00 52.18 C ANISOU 3522 CG1 ILE C 51 9616 4807 5403 1386 -1098 -910 C ATOM 3523 CG2 ILE C 51 6.412 102.669 29.983 1.00 48.81 C ANISOU 3523 CG2 ILE C 51 8842 4723 4981 930 -718 -797 C ATOM 3524 CD1 ILE C 51 8.777 101.219 31.527 1.00 52.25 C ANISOU 3524 CD1 ILE C 51 9712 4777 5363 1398 -1160 -780 C ATOM 3525 N TYR C 52 7.008 99.563 27.296 1.00 54.63 N ANISOU 3525 N TYR C 52 9947 5031 5778 1420 -1121 -1238 N ATOM 3526 CA TYR C 52 6.093 98.440 27.086 1.00 56.64 C ANISOU 3526 CA TYR C 52 10492 4984 6043 1264 -1225 -1263 C ATOM 3527 C TYR C 52 5.659 97.953 28.460 1.00 58.09 C ANISOU 3527 C TYR C 52 10981 4892 6200 1033 -1288 -1076 C ATOM 3528 O TYR C 52 6.380 98.167 29.432 1.00 58.05 O ANISOU 3528 O TYR C 52 11024 4872 6159 1118 -1329 -981 O ATOM 3529 CB TYR C 52 6.788 97.325 26.298 1.00 58.89 C ANISOU 3529 CB TYR C 52 10940 5094 6341 1570 -1431 -1462 C ATOM 3530 CG TYR C 52 5.852 96.299 25.686 1.00 60.67 C ANISOU 3530 CG TYR C 52 11407 5059 6587 1431 -1534 -1540 C ATOM 3531 CD1 TYR C 52 4.763 96.695 24.913 1.00 59.48 C ANISOU 3531 CD1 TYR C 52 11104 5046 6449 1204 -1403 -1563 C ATOM 3532 CD2 TYR C 52 6.075 94.929 25.850 1.00 63.91 C ANISOU 3532 CD2 TYR C 52 12202 5073 7010 1536 -1790 -1600 C ATOM 3533 CE1 TYR C 52 3.909 95.765 24.345 1.00 61.27 C ANISOU 3533 CE1 TYR C 52 11538 5037 6703 1065 -1515 -1644 C ATOM 3534 CE2 TYR C 52 5.226 93.987 25.278 1.00 65.70 C ANISOU 3534 CE2 TYR C 52 12660 5041 7262 1393 -1903 -1676 C ATOM 3535 CZ TYR C 52 4.144 94.413 24.524 1.00 64.55 C ANISOU 3535 CZ TYR C 52 12338 5056 7132 1150 -1761 -1700 C ATOM 3536 OH TYR C 52 3.290 93.505 23.947 1.00 66.41 O ANISOU 3536 OH TYR C 52 12786 5045 7402 993 -1885 -1784 O ATOM 3537 N TYR C 53 4.497 97.307 28.555 1.00 59.42 N ANISOU 3537 N TYR C 53 11354 4847 6375 730 -1296 -1020 N ATOM 3538 CA TYR C 53 3.965 96.887 29.866 1.00 60.97 C ANISOU 3538 CA TYR C 53 11842 4806 6519 447 -1315 -822 C ATOM 3539 C TYR C 53 4.914 95.956 30.640 1.00 63.46 C ANISOU 3539 C TYR C 53 12525 4801 6787 637 -1565 -777 C ATOM 3540 O TYR C 53 4.860 95.899 31.866 1.00 64.12 O ANISOU 3540 O TYR C 53 12815 4759 6788 481 -1576 -596 O ATOM 3541 CB TYR C 53 2.584 96.216 29.742 1.00 62.63 C ANISOU 3541 CB TYR C 53 12212 4830 6753 73 -1293 -784 C ATOM 3542 CG TYR C 53 2.595 94.817 29.140 1.00 65.79 C ANISOU 3542 CG TYR C 53 12936 4871 7190 139 -1539 -891 C ATOM 3543 CD1 TYR C 53 2.834 93.677 29.928 1.00 69.00 C ANISOU 3543 CD1 TYR C 53 13801 4863 7553 106 -1756 -796 C ATOM 3544 CD2 TYR C 53 2.358 94.628 27.781 1.00 66.00 C ANISOU 3544 CD2 TYR C 53 12839 4954 7285 236 -1573 -1089 C ATOM 3545 CE1 TYR C 53 2.847 92.405 29.369 1.00 72.21 C ANISOU 3545 CE1 TYR C 53 14525 4910 8001 177 -2006 -903 C ATOM 3546 CE2 TYR C 53 2.365 93.355 27.218 1.00 69.00 C ANISOU 3546 CE2 TYR C 53 13526 4994 7697 307 -1812 -1209 C ATOM 3547 CZ TYR C 53 2.609 92.251 28.017 1.00 72.00 C ANISOU 3547 CZ TYR C 53 14354 4952 8051 279 -2030 -1118 C ATOM 3548 OH TYR C 53 2.624 90.989 27.479 1.00 75.50 O ANISOU 3548 OH TYR C 53 15130 5025 8532 358 -2291 -1242 O ATOM 3549 N SER C 54 5.748 95.210 29.913 1.00 65.17 N ANISOU 3549 N SER C 54 12833 4881 7046 977 -1775 -951 N ATOM 3550 CA SER C 54 6.738 94.302 30.501 1.00 68.00 C ANISOU 3550 CA SER C 54 13522 4931 7382 1233 -2057 -951 C ATOM 3551 C SER C 54 8.006 94.983 31.043 1.00 67.17 C ANISOU 3551 C SER C 54 13243 5017 7260 1531 -2083 -949 C ATOM 3552 O SER C 54 8.834 94.315 31.663 1.00 69.35 O ANISOU 3552 O SER C 54 13780 5052 7519 1746 -2331 -937 O ATOM 3553 CB SER C 54 7.152 93.262 29.460 1.00 70.30 C ANISOU 3553 CB SER C 54 13950 5021 7739 1521 -2277 -1180 C ATOM 3554 OG SER C 54 7.920 93.875 28.438 1.00 68.94 O ANISOU 3554 OG SER C 54 13396 5190 7609 1847 -2198 -1387 O ATOM 3555 N GLY C 55 8.179 96.282 30.781 1.00 64.22 N ANISOU 3555 N GLY C 55 12440 5062 6899 1550 -1854 -967 N ATOM 3556 CA GLY C 55 9.294 97.054 31.336 1.00 63.34 C ANISOU 3556 CA GLY C 55 12132 5156 6780 1770 -1860 -951 C ATOM 3557 C GLY C 55 10.315 97.597 30.347 1.00 62.46 C ANISOU 3557 C GLY C 55 11636 5360 6737 2110 -1820 -1151 C ATOM 3558 O GLY C 55 11.048 98.527 30.685 1.00 61.53 O ANISOU 3558 O GLY C 55 11260 5495 6625 2205 -1753 -1128 O ATOM 3559 N SER C 56 10.378 97.038 29.138 1.00 63.17 N ANISOU 3559 N SER C 56 11686 5445 6871 2279 -1857 -1349 N ATOM 3560 CA SER C 56 11.305 97.527 28.103 1.00 62.57 C ANISOU 3560 CA SER C 56 11241 5698 6834 2581 -1786 -1549 C ATOM 3561 C SER C 56 11.074 99.006 27.792 1.00 59.44 C ANISOU 3561 C SER C 56 10451 5709 6426 2413 -1500 -1484 C ATOM 3562 O SER C 56 9.948 99.414 27.544 1.00 57.55 O ANISOU 3562 O SER C 56 10185 5515 6164 2122 -1344 -1406 O ATOM 3563 CB SER C 56 11.151 96.721 26.812 1.00 63.99 C ANISOU 3563 CB SER C 56 11471 5814 7027 2728 -1836 -1767 C ATOM 3564 OG SER C 56 11.413 95.350 27.034 1.00 67.20 O ANISOU 3564 OG SER C 56 12253 5823 7456 2912 -2125 -1848 O ATOM 3565 N THR C 57 12.144 99.798 27.815 1.00 59.15 N ANISOU 3565 N THR C 57 10110 5954 6409 2598 -1448 -1521 N ATOM 3566 CA THR C 57 12.068 101.228 27.524 1.00 56.70 C ANISOU 3566 CA THR C 57 9442 6010 6090 2456 -1205 -1458 C ATOM 3567 C THR C 57 12.729 101.543 26.182 1.00 57.02 C ANISOU 3567 C THR C 57 9174 6360 6132 2657 -1099 -1642 C ATOM 3568 O THR C 57 13.711 100.908 25.800 1.00 58.65 O ANISOU 3568 O THR C 57 9343 6582 6361 2974 -1209 -1820 O ATOM 3569 CB THR C 57 12.737 102.058 28.632 1.00 56.14 C ANISOU 3569 CB THR C 57 9253 6043 6034 2445 -1209 -1333 C ATOM 3570 OG1 THR C 57 14.083 101.616 28.836 1.00 58.62 O ANISOU 3570 OG1 THR C 57 9519 6358 6394 2779 -1386 -1448 O ATOM 3571 CG2 THR C 57 11.972 101.922 29.929 1.00 55.96 C ANISOU 3571 CG2 THR C 57 9524 5768 5970 2202 -1264 -1140 C ATOM 3572 N ASN C 58 12.165 102.510 25.464 1.00 55.20 N ANISOU 3572 N ASN C 58 8733 6374 5867 2473 -887 -1602 N ATOM 3573 CA ASN C 58 12.745 103.004 24.210 1.00 55.61 C ANISOU 3573 CA ASN C 58 8490 6755 5882 2605 -750 -1737 C ATOM 3574 C ASN C 58 12.513 104.512 24.147 1.00 52.96 C ANISOU 3574 C ASN C 58 7900 6691 5531 2381 -551 -1592 C ATOM 3575 O ASN C 58 11.372 104.972 24.273 1.00 51.31 O ANISOU 3575 O ASN C 58 7758 6425 5311 2120 -483 -1469 O ATOM 3576 CB ASN C 58 12.132 102.321 22.970 1.00 56.67 C ANISOU 3576 CB ASN C 58 8725 6850 5955 2639 -739 -1884 C ATOM 3577 CG ASN C 58 11.870 100.834 23.162 1.00 58.98 C ANISOU 3577 CG ASN C 58 9369 6768 6272 2750 -956 -1981 C ATOM 3578 OD1 ASN C 58 10.737 100.426 23.418 1.00 59.19 O ANISOU 3578 OD1 ASN C 58 9637 6547 6304 2529 -1005 -1899 O ATOM 3579 ND2 ASN C 58 12.911 100.017 23.024 1.00 61.52 N ANISOU 3579 ND2 ASN C 58 9717 7045 6613 3090 -1093 -2163 N ATOM 3580 N TYR C 59 13.593 105.270 23.959 1.00 52.97 N ANISOU 3580 N TYR C 59 7607 6980 5538 2484 -469 -1615 N ATOM 3581 CA TYR C 59 13.553 106.731 24.017 1.00 50.67 C ANISOU 3581 CA TYR C 59 7091 6919 5243 2282 -315 -1471 C ATOM 3582 C TYR C 59 13.967 107.348 22.687 1.00 51.06 C ANISOU 3582 C TYR C 59 6888 7297 5216 2307 -146 -1541 C ATOM 3583 O TYR C 59 14.595 106.697 21.849 1.00 52.90 O ANISOU 3583 O TYR C 59 7062 7637 5402 2523 -137 -1720 O ATOM 3584 CB TYR C 59 14.490 107.244 25.118 1.00 50.60 C ANISOU 3584 CB TYR C 59 6960 6958 5309 2318 -372 -1398 C ATOM 3585 CG TYR C 59 14.298 106.584 26.476 1.00 50.56 C ANISOU 3585 CG TYR C 59 7218 6642 5349 2326 -555 -1334 C ATOM 3586 CD1 TYR C 59 13.027 106.438 27.026 1.00 49.12 C ANISOU 3586 CD1 TYR C 59 7290 6228 5146 2110 -565 -1218 C ATOM 3587 CD2 TYR C 59 15.392 106.117 27.212 1.00 52.03 C ANISOU 3587 CD2 TYR C 59 7399 6780 5592 2544 -719 -1389 C ATOM 3588 CE1 TYR C 59 12.845 105.843 28.263 1.00 49.62 C ANISOU 3588 CE1 TYR C 59 7616 6020 5218 2087 -712 -1143 C ATOM 3589 CE2 TYR C 59 15.222 105.518 28.453 1.00 52.64 C ANISOU 3589 CE2 TYR C 59 7756 6562 5681 2544 -901 -1313 C ATOM 3590 CZ TYR C 59 13.946 105.391 28.976 1.00 51.40 C ANISOU 3590 CZ TYR C 59 7871 6182 5478 2303 -886 -1182 C ATOM 3591 OH TYR C 59 13.747 104.806 30.203 1.00 52.28 O ANISOU 3591 OH TYR C 59 8282 6012 5570 2270 -1045 -1091 O ATOM 3592 N ASN C 60 13.608 108.617 22.515 1.00 48.90 N ANISOU 3592 N ASN C 60 6483 7178 4920 2084 -17 -1400 N ATOM 3593 CA ASN C 60 14.085 109.438 21.406 1.00 49.08 C ANISOU 3593 CA ASN C 60 6269 7523 4857 2054 148 -1411 C ATOM 3594 C ASN C 60 15.615 109.511 21.476 1.00 50.99 C ANISOU 3594 C ASN C 60 6253 7989 5130 2225 175 -1492 C ATOM 3595 O ASN C 60 16.146 109.897 22.523 1.00 50.72 O ANISOU 3595 O ASN C 60 6143 7931 5199 2207 109 -1417 O ATOM 3596 CB ASN C 60 13.475 110.843 21.537 1.00 46.71 C ANISOU 3596 CB ASN C 60 5910 7280 4558 1779 228 -1215 C ATOM 3597 CG ASN C 60 13.831 111.769 20.382 1.00 46.99 C ANISOU 3597 CG ASN C 60 5756 7612 4486 1697 388 -1185 C ATOM 3598 OD1 ASN C 60 14.950 111.752 19.870 1.00 48.61 O ANISOU 3598 OD1 ASN C 60 5765 8058 4647 1808 471 -1268 O ATOM 3599 ND2 ASN C 60 12.886 112.614 19.997 1.00 45.00 N ANISOU 3599 ND2 ASN C 60 5559 7350 4190 1495 428 -1063 N ATOM 3600 N PRO C 61 16.326 109.130 20.384 1.00 53.33 N ANISOU 3600 N PRO C 61 6407 8516 5337 2394 269 -1659 N ATOM 3601 CA PRO C 61 17.798 109.117 20.400 1.00 55.89 C ANISOU 3601 CA PRO C 61 6444 9089 5702 2574 305 -1772 C ATOM 3602 C PRO C 61 18.480 110.430 20.815 1.00 55.63 C ANISOU 3602 C PRO C 61 6145 9268 5726 2393 389 -1622 C ATOM 3603 O PRO C 61 19.567 110.372 21.387 1.00 57.02 O ANISOU 3603 O PRO C 61 6121 9542 6003 2521 336 -1684 O ATOM 3604 CB PRO C 61 18.176 108.758 18.949 1.00 58.12 C ANISOU 3604 CB PRO C 61 6616 9635 5832 2708 458 -1952 C ATOM 3605 CG PRO C 61 16.987 108.054 18.406 1.00 57.31 C ANISOU 3605 CG PRO C 61 6822 9311 5642 2708 405 -1995 C ATOM 3606 CD PRO C 61 15.798 108.683 19.077 1.00 54.13 C ANISOU 3606 CD PRO C 61 6602 8675 5291 2432 346 -1769 C ATOM 3607 N SER C 62 17.866 111.584 20.540 1.00 54.15 N ANISOU 3607 N SER C 62 5959 9134 5482 2106 494 -1437 N ATOM 3608 CA SER C 62 18.458 112.877 20.940 1.00 54.34 C ANISOU 3608 CA SER C 62 5765 9319 5564 1908 552 -1285 C ATOM 3609 C SER C 62 18.316 113.154 22.435 1.00 52.96 C ANISOU 3609 C SER C 62 5674 8910 5538 1848 384 -1177 C ATOM 3610 O SER C 62 19.044 113.983 22.963 1.00 52.81 O ANISOU 3610 O SER C 62 5466 9003 5598 1751 380 -1102 O ATOM 3611 CB SER C 62 17.828 114.067 20.198 1.00 53.67 C ANISOU 3611 CB SER C 62 5694 9325 5373 1623 686 -1114 C ATOM 3612 OG SER C 62 17.699 113.835 18.808 1.00 55.34 O ANISOU 3612 OG SER C 62 5907 9713 5407 1648 828 -1188 O ATOM 3613 N LEU C 63 17.353 112.504 23.091 1.00 51.76 N ANISOU 3613 N LEU C 63 5811 8443 5411 1883 252 -1165 N ATOM 3614 CA LEU C 63 17.093 112.701 24.521 1.00 50.65 C ANISOU 3614 CA LEU C 63 5797 8075 5372 1820 104 -1065 C ATOM 3615 C LEU C 63 17.517 111.518 25.404 1.00 52.05 C ANISOU 3615 C LEU C 63 6088 8072 5616 2057 -79 -1171 C ATOM 3616 O LEU C 63 17.463 111.620 26.628 1.00 51.28 O ANISOU 3616 O LEU C 63 6098 7804 5581 2023 -211 -1095 O ATOM 3617 CB LEU C 63 15.607 112.992 24.721 1.00 48.65 C ANISOU 3617 CB LEU C 63 5790 7607 5087 1635 104 -946 C ATOM 3618 CG LEU C 63 15.055 114.163 23.899 1.00 47.72 C ANISOU 3618 CG LEU C 63 5608 7616 4909 1417 238 -835 C ATOM 3619 CD1 LEU C 63 13.538 114.170 23.940 1.00 46.31 C ANISOU 3619 CD1 LEU C 63 5657 7232 4706 1298 223 -776 C ATOM 3620 CD2 LEU C 63 15.625 115.490 24.388 1.00 47.60 C ANISOU 3620 CD2 LEU C 63 5428 7705 4953 1257 250 -711 C ATOM 3621 N LYS C 64 17.985 110.440 24.771 1.00 54.19 N ANISOU 3621 N LYS C 64 6340 8385 5865 2302 -96 -1351 N ATOM 3622 CA LYS C 64 18.252 109.126 25.392 1.00 56.40 C ANISOU 3622 CA LYS C 64 6790 8447 6194 2559 -294 -1471 C ATOM 3623 C LYS C 64 18.941 109.158 26.765 1.00 56.94 C ANISOU 3623 C LYS C 64 6855 8415 6365 2625 -481 -1432 C ATOM 3624 O LYS C 64 18.438 108.586 27.739 1.00 56.64 O ANISOU 3624 O LYS C 64 7109 8075 6335 2635 -643 -1377 O ATOM 3625 CB LYS C 64 19.103 108.290 24.415 1.00 59.42 C ANISOU 3625 CB LYS C 64 7019 9002 6557 2845 -268 -1703 C ATOM 3626 CG LYS C 64 19.069 106.780 24.607 1.00 61.40 C ANISOU 3626 CG LYS C 64 7517 8987 6826 3121 -461 -1857 C ATOM 3627 CD LYS C 64 19.712 106.068 23.414 1.00 63.91 C ANISOU 3627 CD LYS C 64 7689 9497 7099 3389 -396 -2106 C ATOM 3628 CE LYS C 64 21.269 106.089 23.457 1.00 67.15 C ANISOU 3628 CE LYS C 64 7734 10185 7597 3636 -415 -2264 C ATOM 3629 NZ LYS C 64 21.835 104.763 23.850 1.00 69.68 N ANISOU 3629 NZ LYS C 64 8170 10308 7996 4013 -663 -2464 N ATOM 3630 N SER C 65 20.077 109.844 26.846 1.00 58.20 N ANISOU 3630 N SER C 65 6690 8830 6594 2651 -461 -1454 N ATOM 3631 CA SER C 65 20.876 109.864 28.081 1.00 59.64 C ANISOU 3631 CA SER C 65 6835 8947 6879 2742 -665 -1444 C ATOM 3632 C SER C 65 20.224 110.633 29.238 1.00 57.31 C ANISOU 3632 C SER C 65 6723 8471 6581 2502 -728 -1245 C ATOM 3633 O SER C 65 20.695 110.541 30.368 1.00 58.74 O ANISOU 3633 O SER C 65 6964 8539 6815 2571 -924 -1226 O ATOM 3634 CB SER C 65 22.276 110.433 27.813 1.00 61.56 C ANISOU 3634 CB SER C 65 6639 9539 7211 2813 -625 -1532 C ATOM 3635 OG SER C 65 22.223 111.831 27.605 1.00 60.71 O ANISOU 3635 OG SER C 65 6350 9622 7098 2514 -462 -1391 O ATOM 3636 N ARG C 66 19.161 111.386 28.949 1.00 54.86 N ANISOU 3636 N ARG C 66 6500 8140 6203 2239 -572 -1113 N ATOM 3637 CA ARG C 66 18.478 112.227 29.930 1.00 52.90 C ANISOU 3637 CA ARG C 66 6399 7755 5945 2012 -597 -948 C ATOM 3638 C ARG C 66 17.116 111.703 30.398 1.00 50.86 C ANISOU 3638 C ARG C 66 6507 7208 5610 1926 -614 -877 C ATOM 3639 O ARG C 66 16.588 112.210 31.384 1.00 48.60 O ANISOU 3639 O ARG C 66 6366 6794 5304 1779 -651 -767 O ATOM 3640 CB ARG C 66 18.253 113.607 29.320 1.00 51.77 C ANISOU 3640 CB ARG C 66 6072 7803 5797 1771 -419 -853 C ATOM 3641 CG ARG C 66 19.509 114.291 28.798 1.00 53.80 C ANISOU 3641 CG ARG C 66 5957 8366 6119 1773 -363 -892 C ATOM 3642 CD ARG C 66 19.139 115.528 27.998 1.00 52.92 C ANISOU 3642 CD ARG C 66 5730 8405 5973 1520 -183 -784 C ATOM 3643 NE ARG C 66 18.374 116.432 28.836 1.00 51.34 N ANISOU 3643 NE ARG C 66 5689 8039 5780 1322 -227 -646 N ATOM 3644 CZ ARG C 66 17.518 117.363 28.423 1.00 49.51 C ANISOU 3644 CZ ARG C 66 5510 7792 5508 1116 -125 -538 C ATOM 3645 NH1 ARG C 66 17.264 117.583 27.130 1.00 49.70 N ANISOU 3645 NH1 ARG C 66 5461 7955 5468 1051 28 -526 N ATOM 3646 NH2 ARG C 66 16.902 118.089 29.341 1.00 47.67 N ANISOU 3646 NH2 ARG C 66 5420 7400 5294 986 -190 -449 N ATOM 3647 N VAL C 67 16.556 110.716 29.694 1.00 51.25 N ANISOU 3647 N VAL C 67 6695 7166 5614 2008 -582 -948 N ATOM 3648 CA VAL C 67 15.173 110.275 29.894 1.00 49.89 C ANISOU 3648 CA VAL C 67 6822 6760 5375 1879 -559 -884 C ATOM 3649 C VAL C 67 15.111 108.954 30.657 1.00 50.98 C ANISOU 3649 C VAL C 67 7260 6617 5492 2011 -740 -912 C ATOM 3650 O VAL C 67 15.844 108.008 30.349 1.00 52.48 O ANISOU 3650 O VAL C 67 7453 6778 5708 2253 -852 -1037 O ATOM 3651 CB VAL C 67 14.439 110.103 28.538 1.00 49.96 C ANISOU 3651 CB VAL C 67 6805 6834 5342 1836 -412 -935 C ATOM 3652 CG1 VAL C 67 13.071 109.445 28.710 1.00 49.38 C ANISOU 3652 CG1 VAL C 67 7022 6517 5222 1719 -413 -898 C ATOM 3653 CG2 VAL C 67 14.273 111.454 27.858 1.00 48.86 C ANISOU 3653 CG2 VAL C 67 6445 6921 5199 1664 -248 -869 C ATOM 3654 N THR C 68 14.207 108.903 31.633 1.00 49.78 N ANISOU 3654 N THR C 68 7369 6258 5287 1846 -765 -797 N ATOM 3655 CA THR C 68 13.796 107.658 32.272 1.00 50.91 C ANISOU 3655 CA THR C 68 7862 6101 5379 1884 -903 -784 C ATOM 3656 C THR C 68 12.275 107.572 32.220 1.00 49.33 C ANISOU 3656 C THR C 68 7841 5782 5121 1636 -774 -709 C ATOM 3657 O THR C 68 11.586 108.514 32.609 1.00 46.85 O ANISOU 3657 O THR C 68 7483 5533 4785 1429 -653 -619 O ATOM 3658 CB THR C 68 14.234 107.582 33.751 1.00 52.41 C ANISOU 3658 CB THR C 68 8236 6145 5532 1905 -1076 -702 C ATOM 3659 OG1 THR C 68 15.580 108.052 33.891 1.00 53.76 O ANISOU 3659 OG1 THR C 68 8168 6484 5775 2081 -1178 -759 O ATOM 3660 CG2 THR C 68 14.146 106.144 34.261 1.00 54.27 C ANISOU 3660 CG2 THR C 68 8839 6066 5716 2005 -1267 -701 C ATOM 3661 N ILE C 69 11.761 106.444 31.734 1.00 50.36 N ANISOU 3661 N ILE C 69 8159 5739 5236 1663 -811 -761 N ATOM 3662 CA ILE C 69 10.340 106.131 31.835 1.00 49.78 C ANISOU 3662 CA ILE C 69 8283 5516 5117 1421 -725 -695 C ATOM 3663 C ILE C 69 10.235 104.859 32.666 1.00 52.36 C ANISOU 3663 C ILE C 69 8988 5519 5387 1431 -895 -652 C ATOM 3664 O ILE C 69 10.957 103.894 32.415 1.00 54.11 O ANISOU 3664 O ILE C 69 9317 5610 5630 1658 -1067 -739 O ATOM 3665 CB ILE C 69 9.669 105.987 30.449 1.00 48.83 C ANISOU 3665 CB ILE C 69 8059 5470 5026 1388 -619 -785 C ATOM 3666 CG1 ILE C 69 9.798 107.307 29.679 1.00 47.06 C ANISOU 3666 CG1 ILE C 69 7496 5550 4833 1365 -468 -800 C ATOM 3667 CG2 ILE C 69 8.192 105.619 30.593 1.00 48.45 C ANISOU 3667 CG2 ILE C 69 8190 5269 4949 1127 -549 -726 C ATOM 3668 CD1 ILE C 69 9.430 107.232 28.213 1.00 46.84 C ANISOU 3668 CD1 ILE C 69 7351 5632 4812 1386 -389 -899 C ATOM 3669 N SER C 70 9.357 104.882 33.669 1.00 53.51 N ANISOU 3669 N SER C 70 9338 5539 5454 1187 -848 -520 N ATOM 3670 CA SER C 70 9.186 103.760 34.587 1.00 56.85 C ANISOU 3670 CA SER C 70 10162 5647 5793 1136 -997 -437 C ATOM 3671 C SER C 70 7.718 103.426 34.784 1.00 58.00 C ANISOU 3671 C SER C 70 10482 5673 5882 811 -866 -355 C ATOM 3672 O SER C 70 6.853 104.296 34.743 1.00 56.29 O ANISOU 3672 O SER C 70 10088 5631 5669 609 -660 -329 O ATOM 3673 CB SER C 70 9.825 104.067 35.941 1.00 57.22 C ANISOU 3673 CB SER C 70 10333 5655 5754 1164 -1100 -336 C ATOM 3674 OG SER C 70 11.176 104.459 35.767 1.00 57.46 O ANISOU 3674 OG SER C 70 10151 5824 5856 1448 -1219 -421 O ATOM 3675 N LEU C 71 7.457 102.145 34.986 1.00 61.53 N ANISOU 3675 N LEU C 71 11273 5817 6287 765 -998 -321 N ATOM 3676 CA LEU C 71 6.129 101.635 35.262 1.00 63.69 C ANISOU 3676 CA LEU C 71 11749 5945 6505 431 -897 -233 C ATOM 3677 C LEU C 71 5.917 101.470 36.773 1.00 66.27 C ANISOU 3677 C LEU C 71 12385 6124 6670 239 -909 -56 C ATOM 3678 O LEU C 71 6.844 101.114 37.514 1.00 67.82 O ANISOU 3678 O LEU C 71 12801 6173 6796 402 -1108 -4 O ATOM 3679 CB LEU C 71 5.966 100.342 34.463 1.00 66.10 C ANISOU 3679 CB LEU C 71 12250 6000 6864 475 -1040 -307 C ATOM 3680 CG LEU C 71 4.605 99.624 34.294 1.00 67.65 C ANISOU 3680 CG LEU C 71 12615 6033 7056 143 -965 -265 C ATOM 3681 CD1 LEU C 71 3.859 100.300 33.155 1.00 65.54 C ANISOU 3681 CD1 LEU C 71 11986 6021 6894 74 -783 -380 C ATOM 3682 CD2 LEU C 71 4.781 98.135 34.003 1.00 70.62 C ANISOU 3682 CD2 LEU C 71 13348 6038 7445 214 -1208 -297 C ATOM 3683 N HIS C 72 4.714 101.813 37.231 1.00 66.93 N ANISOU 3683 N HIS C 72 12462 6280 6690 -98 -689 25 N ATOM 3684 CA HIS C 72 4.318 101.624 38.628 1.00 69.77 C ANISOU 3684 CA HIS C 72 13123 6522 6862 -338 -650 194 C ATOM 3685 C HIS C 72 2.973 100.891 38.642 1.00 71.70 C ANISOU 3685 C HIS C 72 13527 6641 7074 -707 -522 260 C ATOM 3686 O HIS C 72 1.913 101.510 38.762 1.00 71.25 O ANISOU 3686 O HIS C 72 13280 6782 7010 -962 -267 263 O ATOM 3687 CB HIS C 72 4.265 102.974 39.367 1.00 68.57 C ANISOU 3687 CB HIS C 72 12765 6647 6641 -384 -474 216 C ATOM 3688 CG HIS C 72 5.490 103.818 39.166 1.00 67.42 C ANISOU 3688 CG HIS C 72 12391 6660 6567 -59 -579 134 C ATOM 3689 ND1 HIS C 72 6.662 103.605 39.859 1.00 69.03 N ANISOU 3689 ND1 HIS C 72 12781 6746 6699 149 -806 176 N ATOM 3690 CD2 HIS C 72 5.732 104.859 38.332 1.00 65.14 C ANISOU 3690 CD2 HIS C 72 11703 6632 6417 80 -498 16 C ATOM 3691 CE1 HIS C 72 7.570 104.484 39.469 1.00 67.14 C ANISOU 3691 CE1 HIS C 72 12240 6706 6563 390 -848 80 C ATOM 3692 NE2 HIS C 72 7.031 105.256 38.543 1.00 64.91 N ANISOU 3692 NE2 HIS C 72 11612 6649 6400 343 -657 -9 N ATOM 3693 N THR C 73 3.035 99.565 38.507 1.00 73.98 N ANISOU 3693 N THR C 73 14159 6596 7354 -730 -714 301 N ATOM 3694 CA THR C 73 1.837 98.738 38.310 1.00 76.15 C ANISOU 3694 CA THR C 73 14581 6718 7635 -1076 -634 347 C ATOM 3695 C THR C 73 0.905 98.672 39.521 1.00 78.30 C ANISOU 3695 C THR C 73 15056 6975 7721 -1490 -446 524 C ATOM 3696 O THR C 73 -0.307 98.600 39.343 1.00 79.15 O ANISOU 3696 O THR C 73 15059 7155 7858 -1819 -246 526 O ATOM 3697 CB THR C 73 2.184 97.295 37.885 1.00 78.73 C ANISOU 3697 CB THR C 73 15270 6647 7998 -996 -919 347 C ATOM 3698 OG1 THR C 73 3.069 96.707 38.845 1.00 80.98 O ANISOU 3698 OG1 THR C 73 15964 6664 8140 -876 -1151 472 O ATOM 3699 CG2 THR C 73 2.831 97.284 36.517 1.00 76.88 C ANISOU 3699 CG2 THR C 73 14802 6461 7948 -641 -1049 138 C ATOM 3700 N SER C 74 1.443 98.731 40.739 1.00 79.60 N ANISOU 3700 N SER C 74 15488 7068 7687 -1481 -500 662 N ATOM 3701 CA SER C 74 0.590 98.737 41.940 1.00 81.93 C ANISOU 3701 CA SER C 74 15979 7386 7763 -1876 -293 829 C ATOM 3702 C SER C 74 -0.243 100.025 42.085 1.00 79.83 C ANISOU 3702 C SER C 74 15291 7536 7505 -2022 55 756 C ATOM 3703 O SER C 74 -1.197 100.051 42.860 1.00 82.24 O ANISOU 3703 O SER C 74 15662 7923 7662 -2381 290 847 O ATOM 3704 CB SER C 74 1.402 98.467 43.220 1.00 83.99 C ANISOU 3704 CB SER C 74 16672 7461 7781 -1820 -461 997 C ATOM 3705 OG SER C 74 2.088 99.621 43.670 1.00 82.51 O ANISOU 3705 OG SER C 74 16281 7520 7548 -1589 -431 945 O ATOM 3706 N LYS C 75 0.128 101.085 41.360 1.00 76.06 N ANISOU 3706 N LYS C 75 14392 7318 7191 -1743 84 589 N ATOM 3707 CA LYS C 75 -0.660 102.321 41.302 1.00 73.57 C ANISOU 3707 CA LYS C 75 13657 7370 6925 -1832 372 489 C ATOM 3708 C LYS C 75 -1.319 102.572 39.941 1.00 70.75 C ANISOU 3708 C LYS C 75 12912 7157 6812 -1818 445 329 C ATOM 3709 O LYS C 75 -2.072 103.533 39.799 1.00 69.87 O ANISOU 3709 O LYS C 75 12453 7330 6766 -1890 661 236 O ATOM 3710 CB LYS C 75 0.227 103.510 41.680 1.00 71.59 C ANISOU 3710 CB LYS C 75 13248 7308 6645 -1552 349 439 C ATOM 3711 CG LYS C 75 0.884 103.346 43.044 1.00 73.77 C ANISOU 3711 CG LYS C 75 13898 7460 6670 -1552 258 584 C ATOM 3712 CD LYS C 75 1.721 104.549 43.444 1.00 72.16 C ANISOU 3712 CD LYS C 75 13530 7442 6443 -1299 226 524 C ATOM 3713 CE LYS C 75 0.918 105.590 44.212 1.00 72.61 C ANISOU 3713 CE LYS C 75 13431 7770 6386 -1476 509 495 C ATOM 3714 NZ LYS C 75 1.807 106.550 44.925 1.00 72.00 N ANISOU 3714 NZ LYS C 75 13343 7792 6219 -1268 430 474 N ATOM 3715 N ASN C 76 -1.043 101.720 38.952 1.00 69.49 N ANISOU 3715 N ASN C 76 12823 6798 6781 -1713 253 287 N ATOM 3716 CA ASN C 76 -1.544 101.891 37.589 1.00 66.80 C ANISOU 3716 CA ASN C 76 12157 6572 6653 -1667 277 132 C ATOM 3717 C ASN C 76 -1.038 103.217 36.990 1.00 62.30 C ANISOU 3717 C ASN C 76 11204 6279 6187 -1373 305 4 C ATOM 3718 O ASN C 76 -1.780 103.952 36.328 1.00 60.46 O ANISOU 3718 O ASN C 76 10628 6270 6074 -1412 440 -103 O ATOM 3719 CB ASN C 76 -3.082 101.774 37.567 1.00 68.35 C ANISOU 3719 CB ASN C 76 12218 6865 6886 -2053 498 121 C ATOM 3720 CG ASN C 76 -3.608 101.132 36.292 1.00 68.90 C ANISOU 3720 CG ASN C 76 12193 6852 7133 -2096 414 17 C ATOM 3721 OD1 ASN C 76 -3.177 100.039 35.908 1.00 70.07 O ANISOU 3721 OD1 ASN C 76 12622 6706 7294 -2046 201 39 O ATOM 3722 ND2 ASN C 76 -4.565 101.790 35.645 1.00 67.98 N ANISOU 3722 ND2 ASN C 76 11694 6982 7153 -2183 563 -105 N ATOM 3723 N GLN C 77 0.242 103.500 37.241 1.00 60.36 N ANISOU 3723 N GLN C 77 11030 6007 5895 -1087 160 21 N ATOM 3724 CA GLN C 77 0.889 104.732 36.799 1.00 56.89 C ANISOU 3724 CA GLN C 77 10277 5804 5535 -827 169 -72 C ATOM 3725 C GLN C 77 2.149 104.424 36.020 1.00 55.33 C ANISOU 3725 C GLN C 77 10094 5522 5408 -500 -53 -129 C ATOM 3726 O GLN C 77 2.742 103.352 36.175 1.00 56.59 O ANISOU 3726 O GLN C 77 10549 5430 5524 -423 -238 -87 O ATOM 3727 CB GLN C 77 1.296 105.604 37.991 1.00 56.99 C ANISOU 3727 CB GLN C 77 10308 5924 5420 -803 228 -8 C ATOM 3728 CG GLN C 77 0.156 106.036 38.892 1.00 58.32 C ANISOU 3728 CG GLN C 77 10451 6217 5489 -1094 469 29 C ATOM 3729 CD GLN C 77 0.627 106.773 40.133 1.00 58.62 C ANISOU 3729 CD GLN C 77 10574 6331 5368 -1059 503 85 C ATOM 3730 OE1 GLN C 77 1.768 106.620 40.569 1.00 59.39 O ANISOU 3730 OE1 GLN C 77 10861 6314 5393 -877 318 141 O ATOM 3731 NE2 GLN C 77 -0.257 107.571 40.716 1.00 59.07 N ANISOU 3731 NE2 GLN C 77 10488 6585 5369 -1223 730 54 N ATOM 3732 N PHE C 78 2.546 105.379 35.186 1.00 52.26 N ANISOU 3732 N PHE C 78 9385 5346 5124 -310 -34 -230 N ATOM 3733 CA PHE C 78 3.896 105.421 34.632 1.00 51.03 C ANISOU 3733 CA PHE C 78 9175 5200 5014 8 -198 -286 C ATOM 3734 C PHE C 78 4.456 106.843 34.727 1.00 48.73 C ANISOU 3734 C PHE C 78 8614 5154 4746 125 -138 -305 C ATOM 3735 O PHE C 78 3.705 107.823 34.709 1.00 47.28 O ANISOU 3735 O PHE C 78 8230 5145 4590 4 21 -318 O ATOM 3736 CB PHE C 78 3.965 104.838 33.206 1.00 50.40 C ANISOU 3736 CB PHE C 78 9020 5093 5037 131 -272 -403 C ATOM 3737 CG PHE C 78 3.160 105.583 32.173 1.00 48.64 C ANISOU 3737 CG PHE C 78 8500 5076 4905 64 -137 -485 C ATOM 3738 CD1 PHE C 78 1.771 105.460 32.120 1.00 48.99 C ANISOU 3738 CD1 PHE C 78 8524 5116 4973 -200 -20 -484 C ATOM 3739 CD2 PHE C 78 3.797 106.355 31.202 1.00 46.94 C ANISOU 3739 CD2 PHE C 78 8030 5056 4750 263 -139 -567 C ATOM 3740 CE1 PHE C 78 1.035 106.123 31.147 1.00 47.72 C ANISOU 3740 CE1 PHE C 78 8095 5135 4902 -238 66 -568 C ATOM 3741 CE2 PHE C 78 3.064 107.020 30.229 1.00 45.40 C ANISOU 3741 CE2 PHE C 78 7601 5029 4622 207 -45 -631 C ATOM 3742 CZ PHE C 78 1.683 106.905 30.203 1.00 45.86 C ANISOU 3742 CZ PHE C 78 7644 5071 4711 -28 43 -636 C ATOM 3743 N SER C 79 5.774 106.940 34.870 1.00 48.70 N ANISOU 3743 N SER C 79 8613 5153 4739 358 -279 -310 N ATOM 3744 CA SER C 79 6.434 108.217 35.146 1.00 47.16 C ANISOU 3744 CA SER C 79 8208 5153 4557 448 -254 -310 C ATOM 3745 C SER C 79 7.471 108.585 34.092 1.00 45.52 C ANISOU 3745 C SER C 79 7761 5088 4449 679 -318 -397 C ATOM 3746 O SER C 79 7.945 107.736 33.336 1.00 45.66 O ANISOU 3746 O SER C 79 7808 5038 4501 828 -414 -464 O ATOM 3747 CB SER C 79 7.090 108.185 36.529 1.00 48.57 C ANISOU 3747 CB SER C 79 8590 5240 4625 476 -358 -226 C ATOM 3748 OG SER C 79 7.929 107.050 36.664 1.00 51.22 O ANISOU 3748 OG SER C 79 9146 5378 4936 637 -564 -220 O ATOM 3749 N LEU C 80 7.806 109.872 34.070 1.00 43.61 N ANISOU 3749 N LEU C 80 7286 5042 4243 698 -261 -399 N ATOM 3750 CA LEU C 80 8.886 110.412 33.262 1.00 42.78 C ANISOU 3750 CA LEU C 80 6940 5101 4213 876 -303 -456 C ATOM 3751 C LEU C 80 9.847 111.184 34.159 1.00 42.57 C ANISOU 3751 C LEU C 80 6859 5137 4178 936 -379 -418 C ATOM 3752 O LEU C 80 9.413 111.977 34.983 1.00 41.50 O ANISOU 3752 O LEU C 80 6745 5019 4005 809 -325 -364 O ATOM 3753 CB LEU C 80 8.321 111.356 32.197 1.00 41.39 C ANISOU 3753 CB LEU C 80 6524 5105 4098 804 -166 -486 C ATOM 3754 CG LEU C 80 9.306 112.207 31.391 1.00 40.88 C ANISOU 3754 CG LEU C 80 6200 5243 4090 915 -166 -515 C ATOM 3755 CD1 LEU C 80 10.155 111.325 30.495 1.00 42.46 C ANISOU 3755 CD1 LEU C 80 6361 5469 4303 1105 -230 -601 C ATOM 3756 CD2 LEU C 80 8.551 113.246 30.572 1.00 39.55 C ANISOU 3756 CD2 LEU C 80 5865 5208 3955 802 -47 -509 C ATOM 3757 N LYS C 81 11.145 110.942 33.993 1.00 43.39 N ANISOU 3757 N LYS C 81 6884 5282 4321 1136 -509 -462 N ATOM 3758 CA LYS C 81 12.184 111.812 34.537 1.00 43.31 C ANISOU 3758 CA LYS C 81 6732 5384 4340 1198 -586 -448 C ATOM 3759 C LYS C 81 13.028 112.318 33.382 1.00 42.60 C ANISOU 3759 C LYS C 81 6328 5513 4344 1297 -552 -515 C ATOM 3760 O LYS C 81 13.495 111.523 32.552 1.00 42.87 O ANISOU 3760 O LYS C 81 6309 5574 4406 1451 -579 -598 O ATOM 3761 CB LYS C 81 13.064 111.090 35.552 1.00 45.83 C ANISOU 3761 CB LYS C 81 7226 5568 4621 1341 -794 -441 C ATOM 3762 CG LYS C 81 12.320 110.693 36.814 1.00 47.54 C ANISOU 3762 CG LYS C 81 7778 5578 4705 1216 -825 -352 C ATOM 3763 CD LYS C 81 13.235 109.904 37.753 1.00 50.34 C ANISOU 3763 CD LYS C 81 8344 5777 5008 1376 -1069 -338 C ATOM 3764 CE LYS C 81 12.539 109.291 38.984 1.00 52.12 C ANISOU 3764 CE LYS C 81 8969 5772 5063 1248 -1114 -232 C ATOM 3765 NZ LYS C 81 11.079 109.577 39.181 1.00 51.40 N ANISOU 3765 NZ LYS C 81 8972 5670 4887 977 -889 -171 N ATOM 3766 N LEU C 82 13.189 113.639 33.320 1.00 40.85 N ANISOU 3766 N LEU C 82 5912 5447 4164 1201 -490 -481 N ATOM 3767 CA LEU C 82 14.041 114.286 32.335 1.00 40.98 C ANISOU 3767 CA LEU C 82 5632 5685 4254 1243 -448 -515 C ATOM 3768 C LEU C 82 15.092 115.089 33.099 1.00 41.66 C ANISOU 3768 C LEU C 82 5591 5848 4390 1251 -554 -494 C ATOM 3769 O LEU C 82 14.768 116.093 33.726 1.00 41.07 O ANISOU 3769 O LEU C 82 5535 5757 4311 1110 -548 -430 O ATOM 3770 CB LEU C 82 13.205 115.192 31.425 1.00 39.08 C ANISOU 3770 CB LEU C 82 5291 5541 4018 1086 -288 -479 C ATOM 3771 CG LEU C 82 13.957 115.910 30.298 1.00 39.23 C ANISOU 3771 CG LEU C 82 5036 5790 4080 1082 -219 -489 C ATOM 3772 CD1 LEU C 82 14.417 114.936 29.211 1.00 40.29 C ANISOU 3772 CD1 LEU C 82 5093 6018 4197 1237 -183 -586 C ATOM 3773 CD2 LEU C 82 13.100 117.006 29.702 1.00 37.64 C ANISOU 3773 CD2 LEU C 82 4794 5633 3874 907 -111 -421 C ATOM 3774 N SER C 82A 16.340 114.634 33.051 1.00 43.52 N ANISOU 3774 N SER C 82A 5692 6167 4677 1423 -664 -563 N ATOM 3775 CA SER C 82A 17.440 115.290 33.773 1.00 44.82 C ANISOU 3775 CA SER C 82A 5711 6413 4907 1441 -795 -559 C ATOM 3776 C SER C 82A 17.984 116.474 32.978 1.00 44.53 C ANISOU 3776 C SER C 82A 5361 6613 4946 1323 -695 -542 C ATOM 3777 O SER C 82A 17.636 116.651 31.808 1.00 44.55 O ANISOU 3777 O SER C 82A 5263 6727 4938 1264 -532 -539 O ATOM 3778 CB SER C 82A 18.562 114.284 34.039 1.00 46.89 C ANISOU 3778 CB SER C 82A 5931 6675 5210 1689 -972 -656 C ATOM 3779 OG SER C 82A 19.303 114.007 32.860 1.00 48.39 O ANISOU 3779 OG SER C 82A 5847 7076 5465 1810 -900 -757 O ATOM 3780 N SER C 82B 18.816 117.287 33.633 1.00 45.01 N ANISOU 3780 N SER C 82B 5289 6739 5074 1272 -804 -524 N ATOM 3781 CA SER C 82B 19.634 118.315 32.965 1.00 45.65 C ANISOU 3781 CA SER C 82B 5049 7052 5242 1158 -744 -510 C ATOM 3782 C SER C 82B 18.801 119.338 32.188 1.00 43.45 C ANISOU 3782 C SER C 82B 4768 6804 4937 939 -574 -416 C ATOM 3783 O SER C 82B 19.193 119.764 31.096 1.00 43.45 O ANISOU 3783 O SER C 82B 4550 6999 4958 863 -451 -402 O ATOM 3784 CB SER C 82B 20.646 117.653 32.015 1.00 47.89 C ANISOU 3784 CB SER C 82B 5059 7561 5577 1311 -697 -615 C ATOM 3785 OG SER C 82B 21.222 116.504 32.599 1.00 49.98 O ANISOU 3785 OG SER C 82B 5370 7759 5860 1563 -863 -719 O ATOM 3786 N VAL C 82C 17.666 119.746 32.761 1.00 41.35 N ANISOU 3786 N VAL C 82C 4742 6350 4617 841 -572 -355 N ATOM 3787 CA VAL C 82C 16.692 120.558 32.008 1.00 39.63 C ANISOU 3787 CA VAL C 82C 4558 6125 4373 680 -435 -283 C ATOM 3788 C VAL C 82C 17.238 121.976 31.785 1.00 39.94 C ANISOU 3788 C VAL C 82C 4431 6260 4482 496 -444 -210 C ATOM 3789 O VAL C 82C 17.888 122.523 32.666 1.00 40.53 O ANISOU 3789 O VAL C 82C 4470 6314 4616 454 -578 -206 O ATOM 3790 CB VAL C 82C 15.264 120.640 32.658 1.00 37.94 C ANISOU 3790 CB VAL C 82C 4615 5703 4096 636 -423 -262 C ATOM 3791 CG1 VAL C 82C 14.620 119.261 32.738 1.00 37.79 C ANISOU 3791 CG1 VAL C 82C 4767 5586 4004 764 -393 -314 C ATOM 3792 CG2 VAL C 82C 15.290 121.323 34.020 1.00 37.86 C ANISOU 3792 CG2 VAL C 82C 4716 5577 4094 583 -550 -249 C ATOM 3793 N THR C 83 16.972 122.547 30.612 1.00 39.51 N ANISOU 3793 N THR C 83 4299 6299 4414 378 -319 -149 N ATOM 3794 CA THR C 83 17.249 123.964 30.312 1.00 39.99 C ANISOU 3794 CA THR C 83 4269 6402 4525 165 -327 -50 C ATOM 3795 C THR C 83 15.972 124.609 29.750 1.00 38.08 C ANISOU 3795 C THR C 83 4187 6045 4236 71 -266 17 C ATOM 3796 O THR C 83 14.956 123.933 29.612 1.00 36.28 O ANISOU 3796 O THR C 83 4099 5737 3947 168 -211 -23 O ATOM 3797 CB THR C 83 18.393 124.117 29.292 1.00 42.06 C ANISOU 3797 CB THR C 83 4253 6923 4807 88 -240 -24 C ATOM 3798 OG1 THR C 83 17.998 123.545 28.042 1.00 42.20 O ANISOU 3798 OG1 THR C 83 4260 7046 4729 133 -78 -30 O ATOM 3799 CG2 THR C 83 19.661 123.429 29.786 1.00 43.77 C ANISOU 3799 CG2 THR C 83 4266 7275 5089 212 -307 -120 C ATOM 3800 N ALA C 84 16.008 125.912 29.454 1.00 38.69 N ANISOU 3800 N ALA C 84 4250 6102 4348 -117 -294 117 N ATOM 3801 CA ALA C 84 14.818 126.631 28.930 1.00 38.10 C ANISOU 3801 CA ALA C 84 4333 5901 4242 -190 -278 178 C ATOM 3802 C ALA C 84 14.209 125.986 27.670 1.00 37.42 C ANISOU 3802 C ALA C 84 4259 5899 4060 -139 -142 182 C ATOM 3803 O ALA C 84 12.993 126.079 27.460 1.00 37.21 O ANISOU 3803 O ALA C 84 4379 5753 4007 -111 -141 177 O ATOM 3804 CB ALA C 84 15.132 128.111 28.680 1.00 39.46 C ANISOU 3804 CB ALA C 84 4496 6032 4465 -406 -351 298 C ATOM 3805 N ALA C 85 15.044 125.325 26.864 1.00 38.15 N ANISOU 3805 N ALA C 85 4189 6204 4103 -115 -36 173 N ATOM 3806 CA ALA C 85 14.589 124.543 25.702 1.00 37.56 C ANISOU 3806 CA ALA C 85 4127 6224 3919 -41 88 147 C ATOM 3807 C ALA C 85 13.675 123.365 26.038 1.00 35.53 C ANISOU 3807 C ALA C 85 3998 5862 3640 144 92 33 C ATOM 3808 O ALA C 85 12.955 122.887 25.166 1.00 34.72 O ANISOU 3808 O ALA C 85 3960 5773 3459 188 156 12 O ATOM 3809 CB ALA C 85 15.778 124.041 24.898 1.00 39.61 C ANISOU 3809 CB ALA C 85 4173 6750 4128 -31 204 127 C ATOM 3810 N ASP C 86 13.702 122.899 27.284 1.00 34.20 N ANISOU 3810 N ASP C 86 3879 5586 3530 236 16 -35 N ATOM 3811 CA ASP C 86 12.780 121.856 27.744 1.00 32.53 C ANISOU 3811 CA ASP C 86 3818 5248 3295 366 15 -121 C ATOM 3812 C ASP C 86 11.422 122.382 28.241 1.00 30.94 C ANISOU 3812 C ASP C 86 3776 4869 3110 317 -19 -112 C ATOM 3813 O ASP C 86 10.564 121.582 28.634 1.00 29.96 O ANISOU 3813 O ASP C 86 3767 4649 2966 386 -4 -176 O ATOM 3814 CB ASP C 86 13.446 121.019 28.832 1.00 32.44 C ANISOU 3814 CB ASP C 86 3813 5202 3310 485 -52 -190 C ATOM 3815 CG ASP C 86 14.704 120.328 28.345 1.00 33.82 C ANISOU 3815 CG ASP C 86 3814 5554 3481 585 -28 -240 C ATOM 3816 OD1 ASP C 86 14.611 119.559 27.368 1.00 33.13 O ANISOU 3816 OD1 ASP C 86 3706 5548 3334 665 57 -291 O ATOM 3817 OD2 ASP C 86 15.786 120.535 28.948 1.00 34.62 O ANISOU 3817 OD2 ASP C 86 3794 5718 3644 595 -103 -245 O ATOM 3818 N THR C 87 11.205 123.700 28.171 1.00 31.26 N ANISOU 3818 N THR C 87 3820 4869 3189 197 -63 -38 N ATOM 3819 CA THR C 87 9.895 124.291 28.464 1.00 30.59 C ANISOU 3819 CA THR C 87 3856 4638 3128 174 -97 -51 C ATOM 3820 C THR C 87 8.884 123.813 27.435 1.00 30.59 C ANISOU 3820 C THR C 87 3890 4651 3083 206 -37 -74 C ATOM 3821 O THR C 87 9.036 124.063 26.237 1.00 31.38 O ANISOU 3821 O THR C 87 3948 4837 3138 163 -14 -15 O ATOM 3822 CB THR C 87 9.939 125.841 28.510 1.00 30.80 C ANISOU 3822 CB THR C 87 3894 4597 3212 58 -190 26 C ATOM 3823 OG1 THR C 87 10.726 126.239 29.631 1.00 30.93 O ANISOU 3823 OG1 THR C 87 3901 4575 3277 32 -266 22 O ATOM 3824 CG2 THR C 87 8.531 126.477 28.657 1.00 30.13 C ANISOU 3824 CG2 THR C 87 3917 4368 3162 71 -236 -13 C ATOM 3825 N ALA C 88 7.845 123.125 27.903 1.00 29.94 N ANISOU 3825 N ALA C 88 3885 4487 3003 266 -13 -159 N ATOM 3826 CA ALA C 88 6.880 122.504 26.997 1.00 30.06 C ANISOU 3826 CA ALA C 88 3923 4514 2986 295 30 -201 C ATOM 3827 C ALA C 88 5.663 121.994 27.741 1.00 29.58 C ANISOU 3827 C ALA C 88 3929 4356 2954 318 52 -291 C ATOM 3828 O ALA C 88 5.683 121.849 28.963 1.00 28.95 O ANISOU 3828 O ALA C 88 3898 4215 2885 321 59 -322 O ATOM 3829 CB ALA C 88 7.553 121.361 26.239 1.00 30.62 C ANISOU 3829 CB ALA C 88 3961 4689 2982 355 90 -218 C ATOM 3830 N VAL C 89 4.598 121.748 26.983 1.00 29.83 N ANISOU 3830 N VAL C 89 3961 4384 2988 321 61 -334 N ATOM 3831 CA VAL C 89 3.474 120.961 27.459 1.00 29.69 C ANISOU 3831 CA VAL C 89 3978 4311 2992 320 107 -426 C ATOM 3832 C VAL C 89 3.886 119.509 27.310 1.00 30.11 C ANISOU 3832 C VAL C 89 4082 4373 2984 351 153 -449 C ATOM 3833 O VAL C 89 4.239 119.088 26.203 1.00 30.64 O ANISOU 3833 O VAL C 89 4135 4503 3004 386 148 -443 O ATOM 3834 CB VAL C 89 2.187 121.231 26.653 1.00 29.75 C ANISOU 3834 CB VAL C 89 3942 4317 3043 312 75 -477 C ATOM 3835 CG1 VAL C 89 1.074 120.275 27.068 1.00 29.92 C ANISOU 3835 CG1 VAL C 89 3970 4307 3093 282 136 -577 C ATOM 3836 CG2 VAL C 89 1.748 122.669 26.846 1.00 30.19 C ANISOU 3836 CG2 VAL C 89 3963 4337 3172 312 1 -470 C ATOM 3837 N TYR C 90 3.840 118.761 28.412 1.00 29.89 N ANISOU 3837 N TYR C 90 4135 4276 2945 340 191 -478 N ATOM 3838 CA TYR C 90 4.163 117.330 28.422 1.00 30.55 C ANISOU 3838 CA TYR C 90 4309 4319 2978 373 207 -502 C ATOM 3839 C TYR C 90 2.874 116.514 28.480 1.00 31.24 C ANISOU 3839 C TYR C 90 4452 4339 3081 299 249 -566 C ATOM 3840 O TYR C 90 2.070 116.685 29.405 1.00 30.90 O ANISOU 3840 O TYR C 90 4425 4256 3058 218 299 -586 O ATOM 3841 CB TYR C 90 5.074 116.990 29.605 1.00 30.63 C ANISOU 3841 CB TYR C 90 4408 4277 2954 404 191 -471 C ATOM 3842 CG TYR C 90 6.487 117.488 29.406 1.00 30.19 C ANISOU 3842 CG TYR C 90 4274 4303 2894 480 140 -424 C ATOM 3843 CD1 TYR C 90 6.801 118.832 29.586 1.00 29.70 C ANISOU 3843 CD1 TYR C 90 4126 4290 2867 445 115 -377 C ATOM 3844 CD2 TYR C 90 7.504 116.620 29.005 1.00 30.48 C ANISOU 3844 CD2 TYR C 90 4312 4371 2899 585 111 -439 C ATOM 3845 CE1 TYR C 90 8.091 119.301 29.383 1.00 30.22 C ANISOU 3845 CE1 TYR C 90 4101 4443 2939 478 73 -330 C ATOM 3846 CE2 TYR C 90 8.795 117.078 28.803 1.00 30.91 C ANISOU 3846 CE2 TYR C 90 4250 4535 2960 644 79 -410 C ATOM 3847 CZ TYR C 90 9.082 118.416 28.981 1.00 30.59 C ANISOU 3847 CZ TYR C 90 4115 4552 2956 573 65 -349 C ATOM 3848 OH TYR C 90 10.354 118.878 28.780 1.00 31.46 O ANISOU 3848 OH TYR C 90 4092 4779 3081 596 38 -316 O ATOM 3849 N TYR C 91 2.687 115.650 27.480 1.00 31.54 N ANISOU 3849 N TYR C 91 4509 4373 3103 321 232 -608 N ATOM 3850 CA TYR C 91 1.538 114.766 27.384 1.00 32.66 C ANISOU 3850 CA TYR C 91 4699 4445 3267 234 252 -672 C ATOM 3851 C TYR C 91 1.953 113.329 27.640 1.00 34.68 C ANISOU 3851 C TYR C 91 5121 4583 3473 248 235 -683 C ATOM 3852 O TYR C 91 2.986 112.880 27.126 1.00 35.50 O ANISOU 3852 O TYR C 91 5264 4693 3532 373 185 -685 O ATOM 3853 CB TYR C 91 0.952 114.791 25.974 1.00 32.37 C ANISOU 3853 CB TYR C 91 4587 4464 3248 247 208 -725 C ATOM 3854 CG TYR C 91 0.356 116.101 25.528 1.00 31.42 C ANISOU 3854 CG TYR C 91 4329 4430 3181 239 185 -722 C ATOM 3855 CD1 TYR C 91 -0.937 116.459 25.895 1.00 31.54 C ANISOU 3855 CD1 TYR C 91 4260 4441 3282 156 203 -778 C ATOM 3856 CD2 TYR C 91 1.057 116.951 24.672 1.00 31.05 C ANISOU 3856 CD2 TYR C 91 4234 4468 3095 314 138 -669 C ATOM 3857 CE1 TYR C 91 -1.506 117.651 25.458 1.00 31.39 C ANISOU 3857 CE1 TYR C 91 4122 4480 3323 181 147 -790 C ATOM 3858 CE2 TYR C 91 0.496 118.144 24.220 1.00 30.95 C ANISOU 3858 CE2 TYR C 91 4135 4499 3126 310 83 -655 C ATOM 3859 CZ TYR C 91 -0.780 118.490 24.616 1.00 31.33 C ANISOU 3859 CZ TYR C 91 4111 4522 3273 260 74 -721 C ATOM 3860 OH TYR C 91 -1.333 119.670 24.171 1.00 32.10 O ANISOU 3860 OH TYR C 91 4130 4642 3423 286 -12 -720 O ATOM 3861 N CYS C 92 1.137 112.597 28.395 1.00 36.40 N ANISOU 3861 N CYS C 92 5438 4694 3697 120 275 -695 N ATOM 3862 CA CYS C 92 1.209 111.145 28.390 1.00 38.85 C ANISOU 3862 CA CYS C 92 5931 4855 3974 103 232 -713 C ATOM 3863 C CYS C 92 0.157 110.616 27.421 1.00 39.69 C ANISOU 3863 C CYS C 92 6007 4946 4129 21 214 -794 C ATOM 3864 O CYS C 92 -0.838 111.298 27.131 1.00 39.81 O ANISOU 3864 O CYS C 92 5864 5053 4208 -61 251 -829 O ATOM 3865 CB CYS C 92 1.075 110.539 29.790 1.00 40.91 C ANISOU 3865 CB CYS C 92 6371 4984 4189 -12 268 -655 C ATOM 3866 SG CYS C 92 -0.457 110.803 30.726 1.00 43.16 S ANISOU 3866 SG CYS C 92 6612 5291 4498 -265 412 -654 S ATOM 3867 N ALA C 93 0.412 109.427 26.882 1.00 40.70 N ANISOU 3867 N ALA C 93 6280 4955 4231 63 134 -837 N ATOM 3868 CA ALA C 93 -0.487 108.801 25.926 1.00 41.88 C ANISOU 3868 CA ALA C 93 6427 5066 4418 -10 86 -926 C ATOM 3869 C ALA C 93 -0.296 107.294 25.902 1.00 43.92 C ANISOU 3869 C ALA C 93 6925 5112 4649 -16 -1 -959 C ATOM 3870 O ALA C 93 0.816 106.800 26.102 1.00 44.39 O ANISOU 3870 O ALA C 93 7122 5092 4651 137 -59 -944 O ATOM 3871 CB ALA C 93 -0.275 109.381 24.529 1.00 41.29 C ANISOU 3871 CB ALA C 93 6222 5135 4331 126 38 -986 C ATOM 3872 N ARG C 94 -1.384 106.570 25.653 1.00 45.08 N ANISOU 3872 N ARG C 94 7119 5163 4847 -189 -27 -1011 N ATOM 3873 CA ARG C 94 -1.303 105.136 25.410 1.00 46.92 C ANISOU 3873 CA ARG C 94 7593 5169 5064 -201 -143 -1060 C ATOM 3874 C ARG C 94 -0.938 104.936 23.947 1.00 47.14 C ANISOU 3874 C ARG C 94 7602 5242 5067 -16 -247 -1185 C ATOM 3875 O ARG C 94 -1.464 105.620 23.069 1.00 45.98 O ANISOU 3875 O ARG C 94 7275 5256 4942 -16 -240 -1238 O ATOM 3876 CB ARG C 94 -2.626 104.438 25.728 1.00 48.45 C ANISOU 3876 CB ARG C 94 7844 5238 5326 -497 -132 -1065 C ATOM 3877 CG ARG C 94 -2.550 102.919 25.650 1.00 50.82 C ANISOU 3877 CG ARG C 94 8445 5252 5613 -545 -268 -1095 C ATOM 3878 CD ARG C 94 -3.886 102.263 25.955 1.00 52.66 C ANISOU 3878 CD ARG C 94 8720 5368 5919 -886 -250 -1089 C ATOM 3879 NE ARG C 94 -4.850 102.369 24.860 1.00 52.90 N ANISOU 3879 NE ARG C 94 8570 5491 6038 -961 -295 -1214 N ATOM 3880 CZ ARG C 94 -6.020 101.716 24.816 1.00 55.01 C ANISOU 3880 CZ ARG C 94 8843 5666 6392 -1247 -317 -1250 C ATOM 3881 NH1 ARG C 94 -6.384 100.886 25.793 1.00 56.79 N ANISOU 3881 NH1 ARG C 94 9261 5698 6617 -1509 -282 -1158 N ATOM 3882 NH2 ARG C 94 -6.844 101.876 23.785 1.00 55.40 N ANISOU 3882 NH2 ARG C 94 8711 5814 6525 -1289 -384 -1375 N ATOM 3883 N HIS C 95 -0.023 104.007 23.698 1.00 48.73 N ANISOU 3883 N HIS C 95 7999 5303 5213 155 -353 -1236 N ATOM 3884 CA HIS C 95 0.348 103.632 22.344 1.00 49.77 C ANISOU 3884 CA HIS C 95 8150 5464 5297 338 -448 -1379 C ATOM 3885 C HIS C 95 -0.010 102.164 22.139 1.00 52.48 C ANISOU 3885 C HIS C 95 8754 5529 5658 284 -595 -1469 C ATOM 3886 O HIS C 95 0.505 101.295 22.848 1.00 53.73 O ANISOU 3886 O HIS C 95 9138 5467 5809 321 -666 -1442 O ATOM 3887 CB HIS C 95 1.834 103.873 22.100 1.00 49.41 C ANISOU 3887 CB HIS C 95 8076 5528 5168 629 -442 -1402 C ATOM 3888 CG HIS C 95 2.274 103.503 20.724 1.00 50.06 C ANISOU 3888 CG HIS C 95 8173 5676 5172 826 -510 -1561 C ATOM 3889 ND1 HIS C 95 2.212 104.386 19.668 1.00 49.69 N ANISOU 3889 ND1 HIS C 95 7944 5873 5062 872 -454 -1595 N ATOM 3890 CD2 HIS C 95 2.740 102.337 20.216 1.00 52.35 C ANISOU 3890 CD2 HIS C 95 8655 5813 5423 989 -635 -1703 C ATOM 3891 CE1 HIS C 95 2.631 103.782 18.572 1.00 51.01 C ANISOU 3891 CE1 HIS C 95 8186 6057 5137 1047 -523 -1750 C ATOM 3892 NE2 HIS C 95 2.969 102.544 18.879 1.00 52.37 N ANISOU 3892 NE2 HIS C 95 8576 5994 5328 1133 -632 -1830 N ATOM 3893 N ARG C 96 -0.898 101.908 21.179 1.00 53.35 N ANISOU 3893 N ARG C 96 8844 5635 5793 196 -663 -1574 N ATOM 3894 CA ARG C 96 -1.407 100.564 20.895 1.00 56.24 C ANISOU 3894 CA ARG C 96 9450 5728 6190 103 -820 -1671 C ATOM 3895 C ARG C 96 -1.584 100.392 19.392 1.00 56.67 C ANISOU 3895 C ARG C 96 9486 5848 6197 217 -924 -1849 C ATOM 3896 O ARG C 96 -2.127 101.275 18.729 1.00 54.85 O ANISOU 3896 O ARG C 96 9041 5837 5963 182 -878 -1865 O ATOM 3897 CB ARG C 96 -2.752 100.362 21.597 1.00 57.40 C ANISOU 3897 CB ARG C 96 9591 5770 6448 -264 -792 -1594 C ATOM 3898 CG ARG C 96 -3.426 99.018 21.335 1.00 60.62 C ANISOU 3898 CG ARG C 96 10237 5886 6908 -431 -957 -1677 C ATOM 3899 CD ARG C 96 -4.784 98.945 22.013 1.00 61.93 C ANISOU 3899 CD ARG C 96 10335 6008 7188 -829 -893 -1598 C ATOM 3900 NE ARG C 96 -5.812 99.579 21.189 1.00 62.14 N ANISOU 3900 NE ARG C 96 10087 6239 7286 -929 -885 -1684 N ATOM 3901 CZ ARG C 96 -6.614 98.956 20.320 1.00 64.21 C ANISOU 3901 CZ ARG C 96 10378 6413 7608 -1046 -1036 -1817 C ATOM 3902 NH1 ARG C 96 -6.560 97.635 20.127 1.00 67.07 N ANISOU 3902 NH1 ARG C 96 11045 6466 7972 -1096 -1207 -1886 N ATOM 3903 NH2 ARG C 96 -7.497 99.671 19.631 1.00 64.05 N ANISOU 3903 NH2 ARG C 96 10084 6604 7650 -1110 -1037 -1889 N ATOM 3904 N ASN C 97 -1.149 99.245 18.869 1.00 58.99 N ANISOU 3904 N ASN C 97 10025 5939 6449 358 -1081 -1988 N ATOM 3905 CA ASN C 97 -1.241 98.944 17.435 1.00 60.28 C ANISOU 3905 CA ASN C 97 10220 6145 6537 489 -1195 -2182 C ATOM 3906 C ASN C 97 -0.735 100.083 16.536 1.00 58.30 C ANISOU 3906 C ASN C 97 9743 6245 6165 679 -1089 -2209 C ATOM 3907 O ASN C 97 -1.415 100.509 15.597 1.00 57.71 O ANISOU 3907 O ASN C 97 9566 6305 6055 629 -1119 -2271 O ATOM 3908 CB ASN C 97 -2.676 98.533 17.068 1.00 62.31 C ANISOU 3908 CB ASN C 97 10500 6288 6887 207 -1306 -2236 C ATOM 3909 CG ASN C 97 -3.146 97.289 17.820 1.00 64.89 C ANISOU 3909 CG ASN C 97 11088 6247 7319 -6 -1423 -2217 C ATOM 3910 OD1 ASN C 97 -2.347 96.553 18.408 1.00 66.22 O ANISOU 3910 OD1 ASN C 97 11488 6204 7470 107 -1474 -2198 O ATOM 3911 ND2 ASN C 97 -4.454 97.056 17.809 1.00 66.10 N ANISOU 3911 ND2 ASN C 97 11207 6323 7586 -325 -1478 -2218 N ATOM 3912 N TRP C 98 0.462 100.572 16.868 1.00 57.09 N ANISOU 3912 N TRP C 98 9516 6228 5946 883 -975 -2153 N ATOM 3913 CA TRP C 98 1.232 101.514 16.044 1.00 56.09 C ANISOU 3913 CA TRP C 98 9213 6417 5682 1080 -868 -2176 C ATOM 3914 C TRP C 98 0.625 102.929 15.956 1.00 54.06 C ANISOU 3914 C TRP C 98 8709 6398 5435 933 -757 -2044 C ATOM 3915 O TRP C 98 0.858 103.661 14.989 1.00 53.76 O ANISOU 3915 O TRP C 98 8564 6591 5271 1025 -713 -2070 O ATOM 3916 CB TRP C 98 1.491 100.921 14.649 1.00 58.09 C ANISOU 3916 CB TRP C 98 9575 6706 5789 1273 -962 -2394 C ATOM 3917 CG TRP C 98 1.993 99.489 14.690 1.00 60.65 C ANISOU 3917 CG TRP C 98 10164 6764 6118 1435 -1104 -2555 C ATOM 3918 CD1 TRP C 98 1.239 98.349 14.606 1.00 62.83 C ANISOU 3918 CD1 TRP C 98 10677 6734 6461 1333 -1293 -2658 C ATOM 3919 CD2 TRP C 98 3.352 99.057 14.830 1.00 61.54 C ANISOU 3919 CD2 TRP C 98 10327 6881 6175 1731 -1088 -2639 C ATOM 3920 NE1 TRP C 98 2.045 97.237 14.678 1.00 65.00 N ANISOU 3920 NE1 TRP C 98 11178 6799 6721 1557 -1407 -2797 N ATOM 3921 CE2 TRP C 98 3.347 97.641 14.817 1.00 64.26 C ANISOU 3921 CE2 TRP C 98 10964 6897 6555 1819 -1286 -2796 C ATOM 3922 CE3 TRP C 98 4.574 99.727 14.961 1.00 60.60 C ANISOU 3922 CE3 TRP C 98 10026 7011 5990 1929 -936 -2604 C ATOM 3923 CZ2 TRP C 98 4.521 96.883 14.932 1.00 65.92 C ANISOU 3923 CZ2 TRP C 98 11290 7017 6738 2132 -1346 -2931 C ATOM 3924 CZ3 TRP C 98 5.744 98.973 15.078 1.00 62.50 C ANISOU 3924 CZ3 TRP C 98 10348 7190 6209 2226 -982 -2740 C ATOM 3925 CH2 TRP C 98 5.705 97.563 15.057 1.00 64.95 C ANISOU 3925 CH2 TRP C 98 10954 7168 6557 2341 -1191 -2908 C ATOM 3926 N LEU C 99 -0.123 103.321 16.983 1.00 53.33 N ANISOU 3926 N LEU C 99 8537 6246 5481 710 -714 -1903 N ATOM 3927 CA LEU C 99 -0.711 104.661 17.048 1.00 52.12 C ANISOU 3927 CA LEU C 99 8155 6288 5362 589 -625 -1788 C ATOM 3928 C LEU C 99 -0.900 105.102 18.496 1.00 50.82 C ANISOU 3928 C LEU C 99 7912 6082 5317 442 -524 -1634 C ATOM 3929 O LEU C 99 -0.942 104.269 19.401 1.00 51.77 O ANISOU 3929 O LEU C 99 8171 5999 5501 361 -542 -1611 O ATOM 3930 CB LEU C 99 -2.037 104.686 16.281 1.00 53.20 C ANISOU 3930 CB LEU C 99 8250 6425 5537 442 -732 -1860 C ATOM 3931 CG LEU C 99 -3.343 104.351 17.031 1.00 53.88 C ANISOU 3931 CG LEU C 99 8308 6364 5800 167 -768 -1837 C ATOM 3932 CD1 LEU C 99 -4.124 105.636 17.240 1.00 52.70 C ANISOU 3932 CD1 LEU C 99 7907 6389 5729 56 -703 -1751 C ATOM 3933 CD2 LEU C 99 -4.197 103.347 16.275 1.00 56.32 C ANISOU 3933 CD2 LEU C 99 8734 6525 6137 72 -943 -1988 C ATOM 3934 N PHE C 100 -1.025 106.415 18.690 1.00 49.19 N ANISOU 3934 N PHE C 100 7504 6059 5126 407 -430 -1530 N ATOM 3935 CA PHE C 100 -1.219 107.028 20.004 1.00 47.87 C ANISOU 3935 CA PHE C 100 7245 5891 5053 285 -326 -1399 C ATOM 3936 C PHE C 100 -2.688 107.422 20.171 1.00 47.79 C ANISOU 3936 C PHE C 100 7101 5895 5161 73 -330 -1398 C ATOM 3937 O PHE C 100 -3.114 108.431 19.620 1.00 46.90 O ANISOU 3937 O PHE C 100 6828 5935 5056 83 -337 -1394 O ATOM 3938 CB PHE C 100 -0.309 108.260 20.128 1.00 46.38 C ANISOU 3938 CB PHE C 100 6924 5889 4810 403 -230 -1302 C ATOM 3939 CG PHE C 100 1.155 107.946 19.988 1.00 46.22 C ANISOU 3939 CG PHE C 100 6975 5897 4689 607 -213 -1313 C ATOM 3940 CD1 PHE C 100 1.748 107.865 18.731 1.00 46.64 C ANISOU 3940 CD1 PHE C 100 7036 6065 4618 764 -239 -1400 C ATOM 3941 CD2 PHE C 100 1.943 107.728 21.110 1.00 45.71 C ANISOU 3941 CD2 PHE C 100 6964 5757 4647 646 -173 -1249 C ATOM 3942 CE1 PHE C 100 3.098 107.577 18.603 1.00 47.37 C ANISOU 3942 CE1 PHE C 100 7155 6217 4627 959 -207 -1434 C ATOM 3943 CE2 PHE C 100 3.293 107.433 20.984 1.00 45.85 C ANISOU 3943 CE2 PHE C 100 7013 5814 4593 850 -172 -1279 C ATOM 3944 CZ PHE C 100 3.873 107.361 19.734 1.00 46.58 C ANISOU 3944 CZ PHE C 100 7079 6042 4578 1008 -180 -1378 C ATOM 3945 N ASP C 101 -3.457 106.653 20.945 1.00 48.87 N ANISOU 3945 N ASP C 101 7301 5877 5391 -122 -327 -1401 N ATOM 3946 CA ASP C 101 -4.936 106.738 20.877 1.00 49.68 C ANISOU 3946 CA ASP C 101 7264 5997 5615 -332 -351 -1450 C ATOM 3947 C ASP C 101 -5.665 107.501 21.994 1.00 49.02 C ANISOU 3947 C ASP C 101 7000 5993 5633 -490 -219 -1379 C ATOM 3948 O ASP C 101 -6.685 108.142 21.723 1.00 49.53 O ANISOU 3948 O ASP C 101 6855 6174 5790 -564 -232 -1430 O ATOM 3949 CB ASP C 101 -5.571 105.351 20.670 1.00 52.11 C ANISOU 3949 CB ASP C 101 7725 6107 5969 -486 -455 -1538 C ATOM 3950 CG ASP C 101 -5.235 104.349 21.767 1.00 52.94 C ANISOU 3950 CG ASP C 101 8047 5997 6072 -592 -413 -1469 C ATOM 3951 OD1 ASP C 101 -4.504 104.672 22.725 1.00 52.20 O ANISOU 3951 OD1 ASP C 101 7989 5911 5935 -538 -307 -1358 O ATOM 3952 OD2 ASP C 101 -5.721 103.207 21.660 1.00 55.05 O ANISOU 3952 OD2 ASP C 101 8469 6071 6377 -738 -506 -1525 O ATOM 3953 N TYR C 102 -5.159 107.436 23.225 1.00 48.40 N ANISOU 3953 N TYR C 102 7001 5857 5530 -527 -102 -1278 N ATOM 3954 CA TYR C 102 -5.738 108.172 24.356 1.00 47.85 C ANISOU 3954 CA TYR C 102 6783 5876 5523 -657 42 -1220 C ATOM 3955 C TYR C 102 -4.667 109.059 24.983 1.00 45.78 C ANISOU 3955 C TYR C 102 6525 5682 5186 -500 117 -1123 C ATOM 3956 O TYR C 102 -3.705 108.548 25.547 1.00 46.03 O ANISOU 3956 O TYR C 102 6745 5608 5138 -444 128 -1054 O ATOM 3957 CB TYR C 102 -6.297 107.199 25.404 1.00 49.84 C ANISOU 3957 CB TYR C 102 7149 5989 5800 -911 120 -1187 C ATOM 3958 CG TYR C 102 -7.590 106.530 24.980 1.00 51.91 C ANISOU 3958 CG TYR C 102 7335 6218 6171 -1135 74 -1282 C ATOM 3959 CD1 TYR C 102 -8.822 107.150 25.199 1.00 52.93 C ANISOU 3959 CD1 TYR C 102 7184 6508 6420 -1288 155 -1340 C ATOM 3960 CD2 TYR C 102 -7.587 105.284 24.354 1.00 53.78 C ANISOU 3960 CD2 TYR C 102 7768 6263 6401 -1190 -62 -1330 C ATOM 3961 CE1 TYR C 102 -10.012 106.544 24.816 1.00 55.15 C ANISOU 3961 CE1 TYR C 102 7358 6777 6819 -1506 107 -1437 C ATOM 3962 CE2 TYR C 102 -8.773 104.670 23.960 1.00 56.04 C ANISOU 3962 CE2 TYR C 102 7980 6512 6799 -1417 -121 -1421 C ATOM 3963 CZ TYR C 102 -9.983 105.303 24.194 1.00 56.70 C ANISOU 3963 CZ TYR C 102 7760 6776 7009 -1584 -33 -1471 C ATOM 3964 OH TYR C 102 -11.159 104.703 23.809 1.00 59.03 O ANISOU 3964 OH TYR C 102 7947 7053 7430 -1820 -97 -1571 O ATOM 3965 N TRP C 103 -4.839 110.378 24.881 1.00 43.90 N ANISOU 3965 N TRP C 103 6088 5609 4982 -427 146 -1122 N ATOM 3966 CA TRP C 103 -3.866 111.350 25.377 1.00 42.05 C ANISOU 3966 CA TRP C 103 5843 5442 4691 -289 196 -1037 C ATOM 3967 C TRP C 103 -4.398 112.016 26.644 1.00 42.34 C ANISOU 3967 C TRP C 103 5784 5533 4771 -391 323 -1012 C ATOM 3968 O TRP C 103 -5.590 112.271 26.748 1.00 43.41 O ANISOU 3968 O TRP C 103 5756 5736 5000 -506 363 -1083 O ATOM 3969 CB TRP C 103 -3.623 112.445 24.328 1.00 40.66 C ANISOU 3969 CB TRP C 103 5544 5392 4511 -135 120 -1046 C ATOM 3970 CG TRP C 103 -3.000 111.993 23.035 1.00 40.60 C ANISOU 3970 CG TRP C 103 5623 5380 4423 -15 16 -1072 C ATOM 3971 CD1 TRP C 103 -3.517 111.112 22.127 1.00 41.69 C ANISOU 3971 CD1 TRP C 103 5811 5467 4562 -46 -75 -1163 C ATOM 3972 CD2 TRP C 103 -1.754 112.443 22.487 1.00 39.41 C ANISOU 3972 CD2 TRP C 103 5508 5295 4171 148 0 -1019 C ATOM 3973 NE1 TRP C 103 -2.661 110.970 21.060 1.00 41.32 N ANISOU 3973 NE1 TRP C 103 5845 5452 4403 106 -141 -1177 N ATOM 3974 CE2 TRP C 103 -1.571 111.775 21.256 1.00 40.20 C ANISOU 3974 CE2 TRP C 103 5684 5394 4197 220 -84 -1087 C ATOM 3975 CE3 TRP C 103 -0.765 113.337 22.926 1.00 38.25 C ANISOU 3975 CE3 TRP C 103 5332 5215 3986 229 50 -926 C ATOM 3976 CZ2 TRP C 103 -0.441 111.976 20.451 1.00 39.87 C ANISOU 3976 CZ2 TRP C 103 5676 5441 4032 370 -93 -1067 C ATOM 3977 CZ3 TRP C 103 0.352 113.541 22.128 1.00 37.98 C ANISOU 3977 CZ3 TRP C 103 5319 5260 3850 359 32 -897 C ATOM 3978 CH2 TRP C 103 0.507 112.860 20.904 1.00 38.68 C ANISOU 3978 CH2 TRP C 103 5471 5371 3854 428 -26 -968 C ATOM 3979 N GLY C 104 -3.512 112.332 27.589 1.00 41.81 N ANISOU 3979 N GLY C 104 5803 5450 4633 -339 383 -927 N ATOM 3980 CA GLY C 104 -3.863 113.223 28.705 1.00 41.59 C ANISOU 3980 CA GLY C 104 5684 5496 4621 -387 493 -916 C ATOM 3981 C GLY C 104 -4.060 114.656 28.244 1.00 40.77 C ANISOU 3981 C GLY C 104 5389 5518 4585 -273 454 -952 C ATOM 3982 O GLY C 104 -3.742 114.996 27.100 1.00 39.84 O ANISOU 3982 O GLY C 104 5236 5426 4476 -160 344 -953 O ATOM 3983 N GLN C 105 -4.593 115.493 29.136 1.00 40.96 N ANISOU 3983 N GLN C 105 5307 5613 4644 -303 540 -984 N ATOM 3984 CA GLN C 105 -4.802 116.920 28.855 1.00 40.83 C ANISOU 3984 CA GLN C 105 5132 5682 4699 -185 485 -1024 C ATOM 3985 C GLN C 105 -3.497 117.707 28.708 1.00 38.37 C ANISOU 3985 C GLN C 105 4901 5348 4328 -43 410 -929 C ATOM 3986 O GLN C 105 -3.486 118.788 28.131 1.00 36.96 O ANISOU 3986 O GLN C 105 4641 5206 4197 54 319 -933 O ATOM 3987 CB GLN C 105 -5.683 117.572 29.937 1.00 43.06 C ANISOU 3987 CB GLN C 105 5288 6042 5030 -235 601 -1111 C ATOM 3988 CG GLN C 105 -7.166 117.350 29.698 1.00 46.07 C ANISOU 3988 CG GLN C 105 5467 6509 5529 -332 639 -1245 C ATOM 3989 CD GLN C 105 -8.036 117.691 30.902 1.00 48.96 C ANISOU 3989 CD GLN C 105 5706 6979 5919 -413 806 -1345 C ATOM 3990 OE1 GLN C 105 -7.644 118.476 31.774 1.00 49.49 O ANISOU 3990 OE1 GLN C 105 5810 7061 5933 -342 857 -1341 O ATOM 3991 NE2 GLN C 105 -9.224 117.090 30.961 1.00 51.81 N ANISOU 3991 NE2 GLN C 105 5910 7421 6354 -570 898 -1446 N ATOM 3992 N GLY C 106 -2.412 117.173 29.262 1.00 37.24 N ANISOU 3992 N GLY C 106 4920 5143 4086 -41 437 -842 N ATOM 3993 CA GLY C 106 -1.102 117.798 29.185 1.00 35.51 C ANISOU 3993 CA GLY C 106 4757 4919 3818 69 373 -756 C ATOM 3994 C GLY C 106 -0.872 118.698 30.383 1.00 34.40 C ANISOU 3994 C GLY C 106 4624 4781 3666 79 409 -746 C ATOM 3995 O GLY C 106 -1.820 119.142 31.037 1.00 35.07 O ANISOU 3995 O GLY C 106 4637 4898 3792 37 474 -824 O ATOM 3996 N THR C 107 0.398 118.946 30.684 1.00 32.70 N ANISOU 3996 N THR C 107 4488 4543 3395 138 366 -665 N ATOM 3997 CA THR C 107 0.794 119.837 31.777 1.00 31.86 C ANISOU 3997 CA THR C 107 4409 4426 3269 155 367 -655 C ATOM 3998 C THR C 107 1.962 120.697 31.289 1.00 30.74 C ANISOU 3998 C THR C 107 4247 4295 3140 230 260 -579 C ATOM 3999 O THR C 107 2.975 120.177 30.792 1.00 29.90 O ANISOU 3999 O THR C 107 4168 4197 2996 262 224 -515 O ATOM 4000 CB THR C 107 1.157 119.045 33.070 1.00 32.27 C ANISOU 4000 CB THR C 107 4617 4426 3217 106 429 -632 C ATOM 4001 OG1 THR C 107 1.715 119.922 34.063 1.00 32.49 O ANISOU 4001 OG1 THR C 107 4689 4445 3211 136 402 -623 O ATOM 4002 CG2 THR C 107 2.155 117.930 32.798 1.00 31.86 C ANISOU 4002 CG2 THR C 107 4675 4323 3108 135 383 -561 C ATOM 4003 N LEU C 108 1.812 122.015 31.393 1.00 30.18 N ANISOU 4003 N LEU C 108 4120 4223 3125 254 206 -594 N ATOM 4004 CA LEU C 108 2.884 122.928 31.018 1.00 29.67 C ANISOU 4004 CA LEU C 108 4045 4156 3074 284 103 -511 C ATOM 4005 C LEU C 108 3.976 122.824 32.063 1.00 29.54 C ANISOU 4005 C LEU C 108 4107 4116 3001 283 90 -473 C ATOM 4006 O LEU C 108 3.695 122.973 33.245 1.00 30.04 O ANISOU 4006 O LEU C 108 4235 4142 3035 274 117 -525 O ATOM 4007 CB LEU C 108 2.390 124.381 30.956 1.00 29.90 C ANISOU 4007 CB LEU C 108 4031 4147 3183 304 21 -540 C ATOM 4008 CG LEU C 108 3.458 125.436 30.594 1.00 29.85 C ANISOU 4008 CG LEU C 108 4032 4115 3195 294 -96 -439 C ATOM 4009 CD1 LEU C 108 4.117 125.143 29.249 1.00 29.36 C ANISOU 4009 CD1 LEU C 108 3932 4119 3103 271 -111 -338 C ATOM 4010 CD2 LEU C 108 2.848 126.830 30.596 1.00 30.38 C ANISOU 4010 CD2 LEU C 108 4098 4100 3346 321 -202 -476 C ATOM 4011 N VAL C 109 5.203 122.572 31.622 1.00 28.85 N ANISOU 4011 N VAL C 109 4006 4064 2892 296 47 -394 N ATOM 4012 CA VAL C 109 6.365 122.677 32.482 1.00 29.02 C ANISOU 4012 CA VAL C 109 4068 4074 2886 305 -9 -359 C ATOM 4013 C VAL C 109 7.241 123.819 31.948 1.00 29.12 C ANISOU 4013 C VAL C 109 3995 4115 2953 276 -100 -288 C ATOM 4014 O VAL C 109 7.679 123.795 30.799 1.00 28.56 O ANISOU 4014 O VAL C 109 3841 4120 2889 265 -96 -231 O ATOM 4015 CB VAL C 109 7.167 121.367 32.534 1.00 29.56 C ANISOU 4015 CB VAL C 109 4171 4164 2896 351 3 -340 C ATOM 4016 CG1 VAL C 109 8.375 121.527 33.457 1.00 30.45 C ANISOU 4016 CG1 VAL C 109 4311 4267 2992 374 -88 -314 C ATOM 4017 CG2 VAL C 109 6.267 120.210 32.975 1.00 29.71 C ANISOU 4017 CG2 VAL C 109 4304 4126 2858 346 82 -389 C ATOM 4018 N THR C 110 7.488 124.809 32.800 1.00 29.14 N ANISOU 4018 N THR C 110 4032 4058 2982 251 -178 -294 N ATOM 4019 CA THR C 110 8.381 125.930 32.494 1.00 29.32 C ANISOU 4019 CA THR C 110 3996 4082 3062 190 -282 -221 C ATOM 4020 C THR C 110 9.706 125.671 33.181 1.00 29.82 C ANISOU 4020 C THR C 110 4039 4180 3111 188 -341 -197 C ATOM 4021 O THR C 110 9.727 125.351 34.376 1.00 29.50 O ANISOU 4021 O THR C 110 4095 4089 3027 227 -365 -252 O ATOM 4022 CB THR C 110 7.764 127.241 33.013 1.00 29.71 C ANISOU 4022 CB THR C 110 4110 4015 3165 170 -365 -261 C ATOM 4023 OG1 THR C 110 6.483 127.420 32.408 1.00 29.20 O ANISOU 4023 OG1 THR C 110 4046 3924 3126 201 -327 -304 O ATOM 4024 CG2 THR C 110 8.620 128.458 32.689 1.00 30.58 C ANISOU 4024 CG2 THR C 110 4190 4089 3341 78 -493 -175 C ATOM 4025 N VAL C 111 10.803 125.787 32.434 1.00 30.58 N ANISOU 4025 N VAL C 111 4009 4375 3237 140 -365 -120 N ATOM 4026 CA VAL C 111 12.151 125.648 32.985 1.00 31.14 C ANISOU 4026 CA VAL C 111 4008 4501 3322 137 -441 -107 C ATOM 4027 C VAL C 111 12.770 127.039 33.122 1.00 32.24 C ANISOU 4027 C VAL C 111 4106 4607 3538 9 -559 -53 C ATOM 4028 O VAL C 111 13.182 127.634 32.128 1.00 33.24 O ANISOU 4028 O VAL C 111 4128 4800 3703 -97 -549 33 O ATOM 4029 CB VAL C 111 13.046 124.742 32.107 1.00 31.62 C ANISOU 4029 CB VAL C 111 3917 4727 3372 176 -378 -83 C ATOM 4030 CG1 VAL C 111 14.430 124.587 32.729 1.00 32.64 C ANISOU 4030 CG1 VAL C 111 3940 4926 3537 195 -474 -93 C ATOM 4031 CG2 VAL C 111 12.400 123.378 31.912 1.00 30.78 C ANISOU 4031 CG2 VAL C 111 3880 4619 3196 298 -285 -140 C ATOM 4032 N SER C 112 12.832 127.544 34.355 1.00 32.27 N ANISOU 4032 N SER C 112 4208 4501 3551 9 -672 -102 N ATOM 4033 CA SER C 112 13.490 128.824 34.672 1.00 33.39 C ANISOU 4033 CA SER C 112 4333 4581 3772 -114 -820 -68 C ATOM 4034 C SER C 112 13.938 128.802 36.128 1.00 34.07 C ANISOU 4034 C SER C 112 4504 4603 3838 -70 -946 -145 C ATOM 4035 O SER C 112 13.169 128.402 36.996 1.00 33.47 O ANISOU 4035 O SER C 112 4586 4453 3678 29 -924 -228 O ATOM 4036 CB SER C 112 12.566 130.039 34.461 1.00 33.00 C ANISOU 4036 CB SER C 112 4393 4384 3762 -172 -863 -62 C ATOM 4037 OG SER C 112 13.215 131.256 34.815 1.00 34.01 O ANISOU 4037 OG SER C 112 4536 4418 3969 -297 -1028 -32 O ATOM 4038 N SER C 113 15.169 129.233 36.381 1.00 35.79 N ANISOU 4038 N SER C 113 4616 4858 4124 -155 -1078 -117 N ATOM 4039 CA SER C 113 15.656 129.457 37.745 1.00 37.14 C ANISOU 4039 CA SER C 113 4879 4952 4282 -134 -1247 -188 C ATOM 4040 C SER C 113 15.517 130.932 38.164 1.00 37.79 C ANISOU 4040 C SER C 113 5061 4873 4423 -245 -1392 -204 C ATOM 4041 O SER C 113 16.092 131.341 39.164 1.00 38.47 O ANISOU 4041 O SER C 113 5205 4896 4517 -265 -1563 -258 O ATOM 4042 CB SER C 113 17.092 128.929 37.905 1.00 38.80 C ANISOU 4042 CB SER C 113 4908 5297 4538 -133 -1339 -177 C ATOM 4043 OG SER C 113 18.021 129.669 37.131 1.00 41.16 O ANISOU 4043 OG SER C 113 4991 5685 4962 -305 -1378 -98 O ATOM 4044 N ALA C 114 14.716 131.712 37.430 1.00 32.46 N ANISOU 4044 N ALA C 114 4191 4411 3733 171 -177 -10 N ATOM 4045 CA ALA C 114 14.477 133.117 37.768 1.00 32.11 C ANISOU 4045 CA ALA C 114 4108 4458 3635 69 -224 -3 C ATOM 4046 C ALA C 114 13.737 133.275 39.100 1.00 32.00 C ANISOU 4046 C ALA C 114 4188 4411 3561 22 -276 41 C ATOM 4047 O ALA C 114 12.804 132.536 39.395 1.00 32.07 O ANISOU 4047 O ALA C 114 4297 4332 3558 11 -240 48 O ATOM 4048 CB ALA C 114 13.693 133.820 36.667 1.00 31.21 C ANISOU 4048 CB ALA C 114 3991 4372 3496 -13 -166 -75 C ATOM 4049 N SER C 115 14.202 134.219 39.906 1.00 32.29 N ANISOU 4049 N SER C 115 4191 4519 3558 -6 -360 75 N ATOM 4050 CA SER C 115 13.436 134.786 41.012 1.00 32.34 C ANISOU 4050 CA SER C 115 4290 4522 3477 -61 -397 93 C ATOM 4051 C SER C 115 12.411 135.786 40.501 1.00 30.94 C ANISOU 4051 C SER C 115 4128 4360 3267 -150 -349 34 C ATOM 4052 O SER C 115 12.570 136.324 39.407 1.00 30.30 O ANISOU 4052 O SER C 115 3971 4316 3224 -180 -322 -9 O ATOM 4053 CB SER C 115 14.387 135.516 41.970 1.00 33.12 C ANISOU 4053 CB SER C 115 4358 4688 3537 -59 -521 130 C ATOM 4054 OG SER C 115 15.373 134.633 42.415 1.00 34.60 O ANISOU 4054 OG SER C 115 4512 4874 3760 31 -577 195 O ATOM 4055 N THR C 116 11.390 136.063 41.312 1.00 31.08 N ANISOU 4055 N THR C 116 4240 4357 3211 -183 -336 43 N ATOM 4056 CA THR C 116 10.399 137.103 41.014 1.00 30.21 C ANISOU 4056 CA THR C 116 4145 4265 3069 -250 -296 -2 C ATOM 4057 C THR C 116 11.086 138.405 40.647 1.00 29.88 C ANISOU 4057 C THR C 116 4039 4280 3033 -288 -354 -35 C ATOM 4058 O THR C 116 11.987 138.857 41.365 1.00 31.27 O ANISOU 4058 O THR C 116 4210 4483 3186 -283 -449 -19 O ATOM 4059 CB THR C 116 9.458 137.365 42.207 1.00 30.92 C ANISOU 4059 CB THR C 116 4341 4342 3066 -255 -279 22 C ATOM 4060 OG1 THR C 116 8.771 136.162 42.535 1.00 31.22 O ANISOU 4060 OG1 THR C 116 4429 4325 3107 -236 -216 72 O ATOM 4061 CG2 THR C 116 8.413 138.446 41.882 1.00 30.25 C ANISOU 4061 CG2 THR C 116 4262 4273 2958 -302 -230 -20 C ATOM 4062 N LYS C 117 10.654 139.004 39.541 1.00 28.43 N ANISOU 4062 N LYS C 117 3809 4111 2881 -331 -308 -74 N ATOM 4063 CA LYS C 117 11.226 140.253 39.054 1.00 28.32 C ANISOU 4063 CA LYS C 117 3735 4139 2886 -377 -350 -92 C ATOM 4064 C LYS C 117 10.178 141.066 38.298 1.00 27.13 C ANISOU 4064 C LYS C 117 3592 3985 2730 -421 -294 -122 C ATOM 4065 O LYS C 117 9.444 140.517 37.473 1.00 26.35 O ANISOU 4065 O LYS C 117 3482 3882 2649 -420 -225 -133 O ATOM 4066 CB LYS C 117 12.422 139.963 38.142 1.00 29.10 C ANISOU 4066 CB LYS C 117 3717 4281 3057 -364 -357 -78 C ATOM 4067 CG LYS C 117 13.176 141.197 37.676 1.00 29.65 C ANISOU 4067 CG LYS C 117 3707 4397 3160 -422 -401 -72 C ATOM 4068 CD LYS C 117 14.330 140.805 36.767 1.00 30.72 C ANISOU 4068 CD LYS C 117 3712 4593 3367 -397 -381 -44 C ATOM 4069 CE LYS C 117 14.953 141.948 35.988 1.00 31.18 C ANISOU 4069 CE LYS C 117 3674 4703 3470 -465 -389 -20 C ATOM 4070 NZ LYS C 117 14.052 143.030 35.486 1.00 30.45 N ANISOU 4070 NZ LYS C 117 3631 4587 3350 -531 -365 -41 N ATOM 4071 N GLY C 118 10.114 142.361 38.598 1.00 26.64 N ANISOU 4071 N GLY C 118 3558 3920 2646 -458 -335 -134 N ATOM 4072 CA GLY C 118 9.211 143.292 37.927 1.00 26.55 C ANISOU 4072 CA GLY C 118 3551 3899 2635 -487 -293 -152 C ATOM 4073 C GLY C 118 9.795 143.729 36.595 1.00 26.75 C ANISOU 4073 C GLY C 118 3484 3962 2717 -525 -288 -141 C ATOM 4074 O GLY C 118 11.021 143.749 36.425 1.00 26.57 O ANISOU 4074 O GLY C 118 3394 3970 2733 -540 -330 -120 O ATOM 4075 N PRO C 119 8.927 144.092 35.643 1.00 27.06 N ANISOU 4075 N PRO C 119 3512 4009 2759 -538 -235 -144 N ATOM 4076 CA PRO C 119 9.382 144.406 34.299 1.00 27.74 C ANISOU 4076 CA PRO C 119 3523 4142 2877 -566 -215 -124 C ATOM 4077 C PRO C 119 10.001 145.786 34.169 1.00 28.24 C ANISOU 4077 C PRO C 119 3567 4195 2968 -619 -261 -95 C ATOM 4078 O PRO C 119 9.648 146.710 34.912 1.00 28.51 O ANISOU 4078 O PRO C 119 3669 4170 2994 -633 -301 -105 O ATOM 4079 CB PRO C 119 8.082 144.372 33.481 1.00 27.53 C ANISOU 4079 CB PRO C 119 3509 4124 2829 -561 -163 -132 C ATOM 4080 CG PRO C 119 7.040 144.791 34.450 1.00 27.08 C ANISOU 4080 CG PRO C 119 3520 4018 2752 -546 -164 -142 C ATOM 4081 CD PRO C 119 7.461 144.211 35.763 1.00 27.39 C ANISOU 4081 CD PRO C 119 3605 4029 2773 -522 -189 -154 C ATOM 4082 N SER C 120 10.914 145.918 33.219 1.00 29.13 N ANISOU 4082 N SER C 120 3593 4361 3115 -646 -249 -57 N ATOM 4083 CA SER C 120 11.283 147.237 32.713 1.00 30.21 C ANISOU 4083 CA SER C 120 3703 4488 3287 -710 -270 -9 C ATOM 4084 C SER C 120 10.312 147.533 31.588 1.00 29.76 C ANISOU 4084 C SER C 120 3660 4450 3199 -701 -211 6 C ATOM 4085 O SER C 120 10.043 146.648 30.773 1.00 30.33 O ANISOU 4085 O SER C 120 3708 4581 3234 -666 -154 -6 O ATOM 4086 CB SER C 120 12.714 147.229 32.204 1.00 31.56 C ANISOU 4086 CB SER C 120 3758 4722 3511 -745 -271 46 C ATOM 4087 OG SER C 120 13.601 146.917 33.257 1.00 33.03 O ANISOU 4087 OG SER C 120 3919 4902 3731 -750 -343 39 O ATOM 4088 N VAL C 121 9.788 148.764 31.548 1.00 29.77 N ANISOU 4088 N VAL C 121 3707 4394 3212 -730 -234 31 N ATOM 4089 CA VAL C 121 8.834 149.199 30.539 1.00 29.73 C ANISOU 4089 CA VAL C 121 3714 4403 3180 -717 -195 60 C ATOM 4090 C VAL C 121 9.490 150.282 29.680 1.00 30.32 C ANISOU 4090 C VAL C 121 3753 4480 3288 -776 -197 145 C ATOM 4091 O VAL C 121 9.876 151.347 30.177 1.00 30.10 O ANISOU 4091 O VAL C 121 3752 4369 3315 -827 -249 171 O ATOM 4092 CB VAL C 121 7.532 149.747 31.160 1.00 29.55 C ANISOU 4092 CB VAL C 121 3772 4307 3148 -679 -208 35 C ATOM 4093 CG1 VAL C 121 6.524 150.120 30.075 1.00 29.61 C ANISOU 4093 CG1 VAL C 121 3773 4343 3133 -657 -179 77 C ATOM 4094 CG2 VAL C 121 6.936 148.720 32.107 1.00 29.24 C ANISOU 4094 CG2 VAL C 121 3763 4267 3081 -630 -196 -30 C ATOM 4095 N PHE C 122 9.626 149.989 28.391 1.00 30.57 N ANISOU 4095 N PHE C 122 3732 4603 3281 -773 -140 190 N ATOM 4096 CA PHE C 122 10.284 150.882 27.455 1.00 31.44 C ANISOU 4096 CA PHE C 122 3799 4737 3410 -827 -120 291 C ATOM 4097 C PHE C 122 9.261 151.357 26.427 1.00 31.67 C ANISOU 4097 C PHE C 122 3866 4785 3382 -802 -99 337 C ATOM 4098 O PHE C 122 8.398 150.568 26.025 1.00 29.96 O ANISOU 4098 O PHE C 122 3667 4622 3095 -747 -81 290 O ATOM 4099 CB PHE C 122 11.448 150.157 26.787 1.00 32.33 C ANISOU 4099 CB PHE C 122 3816 4960 3510 -832 -58 319 C ATOM 4100 CG PHE C 122 12.528 149.734 27.746 1.00 33.14 C ANISOU 4100 CG PHE C 122 3858 5055 3679 -851 -88 294 C ATOM 4101 CD1 PHE C 122 13.261 150.689 28.435 1.00 33.90 C ANISOU 4101 CD1 PHE C 122 3931 5081 3869 -935 -157 337 C ATOM 4102 CD2 PHE C 122 12.826 148.378 27.953 1.00 32.73 C ANISOU 4102 CD2 PHE C 122 3777 5059 3602 -788 -59 229 C ATOM 4103 CE1 PHE C 122 14.265 150.309 29.322 1.00 34.67 C ANISOU 4103 CE1 PHE C 122 3965 5182 4026 -957 -207 320 C ATOM 4104 CE2 PHE C 122 13.836 147.994 28.830 1.00 33.38 C ANISOU 4104 CE2 PHE C 122 3796 5140 3748 -795 -96 220 C ATOM 4105 CZ PHE C 122 14.555 148.962 29.518 1.00 34.08 C ANISOU 4105 CZ PHE C 122 3850 5176 3923 -882 -175 267 C ATOM 4106 N PRO C 123 9.340 152.645 26.004 1.00 32.64 N ANISOU 4106 N PRO C 123 4003 4857 3540 -847 -111 434 N ATOM 4107 CA PRO C 123 8.390 153.151 25.012 1.00 33.56 C ANISOU 4107 CA PRO C 123 4155 4994 3601 -815 -100 496 C ATOM 4108 C PRO C 123 8.712 152.704 23.584 1.00 34.79 C ANISOU 4108 C PRO C 123 4269 5291 3660 -809 -34 554 C ATOM 4109 O PRO C 123 9.880 152.621 23.200 1.00 35.53 O ANISOU 4109 O PRO C 123 4300 5442 3757 -850 18 604 O ATOM 4110 CB PRO C 123 8.539 154.673 25.123 1.00 34.46 C ANISOU 4110 CB PRO C 123 4308 4987 3797 -867 -136 589 C ATOM 4111 CG PRO C 123 9.954 154.870 25.545 1.00 35.02 C ANISOU 4111 CG PRO C 123 4325 5034 3945 -956 -140 613 C ATOM 4112 CD PRO C 123 10.336 153.670 26.373 1.00 33.83 C ANISOU 4112 CD PRO C 123 4137 4928 3787 -935 -143 500 C ATOM 4113 N LEU C 124 7.665 152.406 22.820 1.00 35.21 N ANISOU 4113 N LEU C 124 4354 5404 3620 -755 -37 547 N ATOM 4114 CA LEU C 124 7.765 152.151 21.395 1.00 36.62 C ANISOU 4114 CA LEU C 124 4527 5711 3677 -741 11 603 C ATOM 4115 C LEU C 124 7.115 153.367 20.737 1.00 38.12 C ANISOU 4115 C LEU C 124 4756 5874 3855 -741 -18 725 C ATOM 4116 O LEU C 124 5.903 153.411 20.530 1.00 38.10 O ANISOU 4116 O LEU C 124 4787 5873 3816 -693 -72 716 O ATOM 4117 CB LEU C 124 7.070 150.837 21.020 1.00 36.04 C ANISOU 4117 CB LEU C 124 4471 5722 3500 -687 5 495 C ATOM 4118 CG LEU C 124 7.580 149.575 21.726 1.00 35.22 C ANISOU 4118 CG LEU C 124 4345 5621 3416 -675 29 373 C ATOM 4119 CD1 LEU C 124 6.694 148.379 21.395 1.00 35.25 C ANISOU 4119 CD1 LEU C 124 4385 5672 3336 -635 3 269 C ATOM 4120 CD2 LEU C 124 9.028 149.271 21.370 1.00 35.93 C ANISOU 4120 CD2 LEU C 124 4384 5777 3492 -683 115 398 C ATOM 4121 N ALA C 125 7.946 154.360 20.433 1.00 40.31 N ANISOU 4121 N ALA C 125 5021 6121 4175 -797 14 851 N ATOM 4122 CA ALA C 125 7.481 155.678 20.006 1.00 42.01 C ANISOU 4122 CA ALA C 125 5280 6265 4414 -805 -17 985 C ATOM 4123 C ALA C 125 7.043 155.665 18.545 1.00 43.85 C ANISOU 4123 C ALA C 125 5538 6628 4495 -767 3 1074 C ATOM 4124 O ALA C 125 7.692 155.021 17.723 1.00 45.22 O ANISOU 4124 O ALA C 125 5688 6937 4557 -769 75 1083 O ATOM 4125 CB ALA C 125 8.581 156.711 20.209 1.00 42.84 C ANISOU 4125 CB ALA C 125 5366 6280 4631 -898 6 1095 C ATOM 4126 N PRO C 126 5.956 156.393 18.210 1.00 45.01 N ANISOU 4126 N PRO C 126 5735 6737 4631 -722 -61 1143 N ATOM 4127 CA PRO C 126 5.530 156.504 16.809 1.00 46.35 C ANISOU 4127 CA PRO C 126 5936 7030 4647 -686 -61 1247 C ATOM 4128 C PRO C 126 6.432 157.418 15.989 1.00 47.75 C ANISOU 4128 C PRO C 126 6123 7218 4802 -738 8 1431 C ATOM 4129 O PRO C 126 7.062 158.313 16.551 1.00 48.35 O ANISOU 4129 O PRO C 126 6190 7160 5021 -803 22 1502 O ATOM 4130 CB PRO C 126 4.131 157.104 16.925 1.00 46.54 C ANISOU 4130 CB PRO C 126 5992 6986 4705 -619 -160 1275 C ATOM 4131 CG PRO C 126 4.195 157.941 18.157 1.00 46.11 C ANISOU 4131 CG PRO C 126 5947 6738 4837 -635 -176 1267 C ATOM 4132 CD PRO C 126 5.134 157.237 19.097 1.00 44.68 C ANISOU 4132 CD PRO C 126 5726 6534 4716 -693 -131 1142 C ATOM 4133 N THR C 135 -2.831 156.702 10.068 1.00 56.02 N ANISOU 4133 N THR C 135 7289 9015 4980 -252 -875 1673 N ATOM 4134 CA THR C 135 -2.703 156.171 11.426 1.00 54.16 C ANISOU 4134 CA THR C 135 6985 8665 4930 -284 -817 1513 C ATOM 4135 C THR C 135 -1.248 155.889 11.798 1.00 52.75 C ANISOU 4135 C THR C 135 6849 8435 4759 -348 -658 1445 C ATOM 4136 O THR C 135 -0.413 155.618 10.932 1.00 53.82 O ANISOU 4136 O THR C 135 7056 8668 4725 -375 -595 1462 O ATOM 4137 CB THR C 135 -3.490 154.859 11.602 1.00 53.57 C ANISOU 4137 CB THR C 135 6852 8670 4832 -311 -911 1339 C ATOM 4138 OG1 THR C 135 -2.854 153.811 10.858 1.00 54.07 O ANISOU 4138 OG1 THR C 135 6995 8849 4701 -363 -892 1231 O ATOM 4139 CG2 THR C 135 -4.933 155.017 11.140 1.00 55.16 C ANISOU 4139 CG2 THR C 135 6987 8952 5019 -261 -1085 1407 C ATOM 4140 N ALA C 136 -0.968 155.923 13.100 1.00 51.20 N ANISOU 4140 N ALA C 136 6604 8094 4754 -367 -594 1367 N ATOM 4141 CA ALA C 136 0.360 155.623 13.633 1.00 49.60 C ANISOU 4141 CA ALA C 136 6417 7838 4590 -428 -463 1297 C ATOM 4142 C ALA C 136 0.252 154.577 14.735 1.00 47.36 C ANISOU 4142 C ALA C 136 6081 7512 4401 -451 -457 1108 C ATOM 4143 O ALA C 136 -0.697 154.592 15.528 1.00 47.10 O ANISOU 4143 O ALA C 136 5992 7416 4487 -421 -517 1067 O ATOM 4144 CB ALA C 136 1.013 156.886 14.163 1.00 49.62 C ANISOU 4144 CB ALA C 136 6430 7687 4735 -440 -394 1417 C ATOM 4145 N ALA C 137 1.225 153.670 14.769 1.00 45.81 N ANISOU 4145 N ALA C 137 5900 7354 4150 -495 -378 1003 N ATOM 4146 CA ALA C 137 1.315 152.652 15.803 1.00 43.99 C ANISOU 4146 CA ALA C 137 5633 7076 4005 -519 -360 837 C ATOM 4147 C ALA C 137 2.259 153.143 16.892 1.00 42.29 C ANISOU 4147 C ALA C 137 5397 6731 3939 -546 -274 840 C ATOM 4148 O ALA C 137 3.288 153.749 16.608 1.00 42.48 O ANISOU 4148 O ALA C 137 5438 6745 3957 -573 -200 928 O ATOM 4149 CB ALA C 137 1.822 151.346 15.213 1.00 44.29 C ANISOU 4149 CB ALA C 137 5707 7220 3900 -538 -331 718 C ATOM 4150 N LEU C 138 1.890 152.905 18.142 1.00 41.17 N ANISOU 4150 N LEU C 138 5219 6494 3931 -543 -288 752 N ATOM 4151 CA LEU C 138 2.785 153.153 19.271 1.00 39.85 C ANISOU 4151 CA LEU C 138 5042 6211 3889 -573 -225 723 C ATOM 4152 C LEU C 138 2.525 152.080 20.310 1.00 38.47 C ANISOU 4152 C LEU C 138 4840 6010 3768 -573 -231 577 C ATOM 4153 O LEU C 138 1.499 151.395 20.256 1.00 39.06 O ANISOU 4153 O LEU C 138 4894 6128 3818 -553 -286 520 O ATOM 4154 CB LEU C 138 2.577 154.558 19.835 1.00 40.09 C ANISOU 4154 CB LEU C 138 5087 6107 4040 -557 -240 818 C ATOM 4155 CG LEU C 138 1.213 154.895 20.453 1.00 40.36 C ANISOU 4155 CG LEU C 138 5106 6079 4149 -488 -301 808 C ATOM 4156 CD1 LEU C 138 1.195 154.649 21.957 1.00 39.29 C ANISOU 4156 CD1 LEU C 138 4963 5841 4124 -483 -281 700 C ATOM 4157 CD2 LEU C 138 0.832 156.342 20.175 1.00 41.71 C ANISOU 4157 CD2 LEU C 138 5311 6167 4370 -445 -326 949 C ATOM 4158 N GLY C 139 3.452 151.923 21.241 1.00 36.73 N ANISOU 4158 N GLY C 139 4613 5720 3621 -602 -181 526 N ATOM 4159 CA GLY C 139 3.326 150.861 22.223 1.00 35.42 C ANISOU 4159 CA GLY C 139 4431 5531 3497 -601 -180 401 C ATOM 4160 C GLY C 139 4.289 150.923 23.378 1.00 34.46 C ANISOU 4160 C GLY C 139 4307 5322 3464 -626 -144 364 C ATOM 4161 O GLY C 139 5.005 151.912 23.554 1.00 33.90 O ANISOU 4161 O GLY C 139 4245 5190 3445 -653 -131 432 O ATOM 4162 N CYS C 140 4.289 149.843 24.154 1.00 33.92 N ANISOU 4162 N CYS C 140 4230 5246 3412 -623 -138 262 N ATOM 4163 CA CYS C 140 5.166 149.661 25.299 1.00 33.92 C ANISOU 4163 CA CYS C 140 4228 5180 3479 -640 -119 217 C ATOM 4164 C CYS C 140 5.757 148.259 25.252 1.00 32.58 C ANISOU 4164 C CYS C 140 4042 5064 3272 -640 -89 140 C ATOM 4165 O CYS C 140 5.032 147.282 25.067 1.00 31.60 O ANISOU 4165 O CYS C 140 3926 4971 3110 -623 -100 79 O ATOM 4166 CB CYS C 140 4.376 149.819 26.594 1.00 35.38 C ANISOU 4166 CB CYS C 140 4436 5278 3730 -613 -143 177 C ATOM 4167 SG CYS C 140 4.084 151.545 27.044 1.00 38.95 S ANISOU 4167 SG CYS C 140 4931 5619 4249 -599 -167 246 S ATOM 4168 N LEU C 141 7.074 148.176 25.403 1.00 32.22 N ANISOU 4168 N LEU C 141 3971 5024 3248 -659 -55 147 N ATOM 4169 CA LEU C 141 7.785 146.906 25.530 1.00 31.78 C ANISOU 4169 CA LEU C 141 3898 5001 3177 -640 -21 79 C ATOM 4170 C LEU C 141 7.936 146.623 27.026 1.00 30.93 C ANISOU 4170 C LEU C 141 3795 4814 3145 -639 -49 34 C ATOM 4171 O LEU C 141 8.611 147.373 27.721 1.00 31.28 O ANISOU 4171 O LEU C 141 3824 4812 3248 -667 -70 68 O ATOM 4172 CB LEU C 141 9.159 147.001 24.861 1.00 32.43 C ANISOU 4172 CB LEU C 141 3927 5150 3246 -648 38 128 C ATOM 4173 CG LEU C 141 10.151 145.839 24.999 1.00 32.97 C ANISOU 4173 CG LEU C 141 3960 5252 3316 -610 85 76 C ATOM 4174 CD1 LEU C 141 9.571 144.547 24.462 1.00 33.35 C ANISOU 4174 CD1 LEU C 141 4061 5326 3284 -558 102 -16 C ATOM 4175 CD2 LEU C 141 11.454 146.162 24.279 1.00 34.04 C ANISOU 4175 CD2 LEU C 141 4018 5468 3447 -614 157 152 C ATOM 4176 N VAL C 142 7.317 145.539 27.487 1.00 30.03 N ANISOU 4176 N VAL C 142 3707 4681 3022 -612 -56 -37 N ATOM 4177 CA VAL C 142 7.346 145.103 28.874 1.00 29.59 C ANISOU 4177 CA VAL C 142 3669 4560 3014 -602 -75 -74 C ATOM 4178 C VAL C 142 8.350 143.953 29.016 1.00 29.80 C ANISOU 4178 C VAL C 142 3677 4601 3046 -575 -52 -110 C ATOM 4179 O VAL C 142 8.055 142.813 28.668 1.00 30.08 O ANISOU 4179 O VAL C 142 3732 4643 3053 -550 -32 -160 O ATOM 4180 CB VAL C 142 5.949 144.638 29.323 1.00 28.92 C ANISOU 4180 CB VAL C 142 3618 4442 2926 -591 -88 -107 C ATOM 4181 CG1 VAL C 142 5.961 144.223 30.791 1.00 28.97 C ANISOU 4181 CG1 VAL C 142 3653 4388 2965 -575 -95 -130 C ATOM 4182 CG2 VAL C 142 4.922 145.737 29.080 1.00 28.99 C ANISOU 4182 CG2 VAL C 142 3630 4448 2936 -595 -105 -65 C ATOM 4183 N LYS C 143 9.515 144.257 29.574 1.00 30.28 N ANISOU 4183 N LYS C 143 3698 4657 3150 -581 -62 -82 N ATOM 4184 CA LYS C 143 10.687 143.393 29.425 1.00 31.31 C ANISOU 4184 CA LYS C 143 3779 4825 3292 -544 -31 -90 C ATOM 4185 C LYS C 143 11.245 142.803 30.730 1.00 30.61 C ANISOU 4185 C LYS C 143 3689 4692 3249 -520 -69 -103 C ATOM 4186 O LYS C 143 11.336 143.503 31.748 1.00 29.51 O ANISOU 4186 O LYS C 143 3561 4512 3137 -552 -130 -84 O ATOM 4187 CB LYS C 143 11.781 144.189 28.734 1.00 33.10 C ANISOU 4187 CB LYS C 143 3922 5117 3537 -569 -6 -21 C ATOM 4188 CG LYS C 143 12.658 143.342 27.832 1.00 35.09 C ANISOU 4188 CG LYS C 143 4120 5447 3766 -511 73 -25 C ATOM 4189 CD LYS C 143 13.725 144.196 27.177 1.00 36.74 C ANISOU 4189 CD LYS C 143 4228 5734 3999 -541 113 66 C ATOM 4190 CE LYS C 143 14.972 143.384 26.869 1.00 38.64 C ANISOU 4190 CE LYS C 143 4376 6048 4259 -471 184 77 C ATOM 4191 NZ LYS C 143 16.157 144.273 26.754 1.00 39.98 N ANISOU 4191 NZ LYS C 143 4410 6281 4500 -522 199 187 N ATOM 4192 N ASP C 144 11.636 141.526 30.655 1.00 30.20 N ANISOU 4192 N ASP C 144 3634 4644 3197 -458 -38 -136 N ATOM 4193 CA ASP C 144 12.430 140.835 31.675 1.00 30.32 C ANISOU 4193 CA ASP C 144 3630 4634 3255 -415 -68 -130 C ATOM 4194 C ASP C 144 11.728 140.760 33.031 1.00 29.26 C ANISOU 4194 C ASP C 144 3573 4427 3118 -428 -126 -140 C ATOM 4195 O ASP C 144 12.264 141.198 34.041 1.00 29.75 O ANISOU 4195 O ASP C 144 3625 4478 3199 -441 -189 -112 O ATOM 4196 CB ASP C 144 13.828 141.479 31.799 1.00 31.36 C ANISOU 4196 CB ASP C 144 3651 4822 3441 -428 -93 -68 C ATOM 4197 CG ASP C 144 14.650 141.349 30.526 1.00 32.49 C ANISOU 4197 CG ASP C 144 3705 5052 3587 -394 -9 -45 C ATOM 4198 OD1 ASP C 144 14.413 140.422 29.724 1.00 33.04 O ANISOU 4198 OD1 ASP C 144 3810 5131 3614 -329 63 -93 O ATOM 4199 OD2 ASP C 144 15.546 142.181 30.324 1.00 33.62 O ANISOU 4199 OD2 ASP C 144 3746 5254 3774 -435 -14 23 O ATOM 4200 N TYR C 145 10.530 140.180 33.028 1.00 28.21 N ANISOU 4200 N TYR C 145 3514 4249 2956 -426 -103 -176 N ATOM 4201 CA TYR C 145 9.770 139.924 34.257 1.00 27.65 C ANISOU 4201 CA TYR C 145 3514 4117 2875 -428 -129 -175 C ATOM 4202 C TYR C 145 9.593 138.433 34.486 1.00 27.01 C ANISOU 4202 C TYR C 145 3476 3984 2805 -385 -106 -191 C ATOM 4203 O TYR C 145 9.771 137.615 33.575 1.00 27.12 O ANISOU 4203 O TYR C 145 3482 3992 2828 -358 -70 -223 O ATOM 4204 CB TYR C 145 8.408 140.632 34.241 1.00 27.27 C ANISOU 4204 CB TYR C 145 3503 4057 2800 -471 -118 -181 C ATOM 4205 CG TYR C 145 7.457 140.142 33.195 1.00 27.66 C ANISOU 4205 CG TYR C 145 3555 4112 2842 -487 -80 -208 C ATOM 4206 CD1 TYR C 145 7.409 140.731 31.935 1.00 27.74 C ANISOU 4206 CD1 TYR C 145 3530 4174 2835 -507 -69 -214 C ATOM 4207 CD2 TYR C 145 6.574 139.098 33.473 1.00 28.15 C ANISOU 4207 CD2 TYR C 145 3657 4126 2912 -490 -63 -222 C ATOM 4208 CE1 TYR C 145 6.517 140.270 30.973 1.00 28.61 C ANISOU 4208 CE1 TYR C 145 3650 4295 2925 -526 -55 -244 C ATOM 4209 CE2 TYR C 145 5.687 138.631 32.521 1.00 28.75 C ANISOU 4209 CE2 TYR C 145 3734 4204 2988 -521 -52 -251 C ATOM 4210 CZ TYR C 145 5.654 139.221 31.272 1.00 28.87 C ANISOU 4210 CZ TYR C 145 3719 4277 2974 -537 -54 -268 C ATOM 4211 OH TYR C 145 4.759 138.758 30.332 1.00 30.14 O ANISOU 4211 OH TYR C 145 3886 4444 3120 -572 -63 -302 O ATOM 4212 N PHE C 146 9.259 138.094 35.722 1.00 26.04 N ANISOU 4212 N PHE C 146 3408 3813 2673 -376 -126 -167 N ATOM 4213 CA PHE C 146 8.982 136.718 36.121 1.00 25.89 C ANISOU 4213 CA PHE C 146 3442 3725 2670 -345 -107 -161 C ATOM 4214 C PHE C 146 8.244 136.730 37.459 1.00 25.59 C ANISOU 4214 C PHE C 146 3469 3655 2600 -355 -113 -119 C ATOM 4215 O PHE C 146 8.583 137.542 38.317 1.00 24.96 O ANISOU 4215 O PHE C 146 3400 3603 2481 -349 -153 -98 O ATOM 4216 CB PHE C 146 10.289 135.944 36.260 1.00 26.49 C ANISOU 4216 CB PHE C 146 3496 3791 2778 -270 -125 -147 C ATOM 4217 CG PHE C 146 10.104 134.476 36.470 1.00 27.32 C ANISOU 4217 CG PHE C 146 3664 3804 2913 -229 -103 -142 C ATOM 4218 CD1 PHE C 146 9.977 133.617 35.383 1.00 27.73 C ANISOU 4218 CD1 PHE C 146 3732 3810 2994 -213 -62 -198 C ATOM 4219 CD2 PHE C 146 10.053 133.944 37.757 1.00 27.67 C ANISOU 4219 CD2 PHE C 146 3766 3798 2950 -204 -127 -82 C ATOM 4220 CE1 PHE C 146 9.811 132.258 35.575 1.00 28.48 C ANISOU 4220 CE1 PHE C 146 3901 3794 3128 -180 -48 -197 C ATOM 4221 CE2 PHE C 146 9.882 132.592 37.953 1.00 28.48 C ANISOU 4221 CE2 PHE C 146 3933 3799 3090 -170 -107 -63 C ATOM 4222 CZ PHE C 146 9.760 131.747 36.859 1.00 28.92 C ANISOU 4222 CZ PHE C 146 4006 3792 3192 -161 -69 -123 C ATOM 4223 N PRO C 147 7.244 135.869 37.668 1.00 25.51 N ANISOU 4223 N PRO C 147 3505 3587 2602 -373 -73 -104 N ATOM 4224 CA PRO C 147 6.635 134.971 36.671 1.00 25.53 C ANISOU 4224 CA PRO C 147 3508 3541 2650 -404 -42 -139 C ATOM 4225 C PRO C 147 5.531 135.693 35.900 1.00 24.92 C ANISOU 4225 C PRO C 147 3395 3507 2567 -470 -26 -165 C ATOM 4226 O PRO C 147 5.349 136.887 36.071 1.00 23.92 O ANISOU 4226 O PRO C 147 3242 3440 2408 -477 -30 -156 O ATOM 4227 CB PRO C 147 6.034 133.874 37.549 1.00 26.11 C ANISOU 4227 CB PRO C 147 3645 3529 2745 -411 -20 -86 C ATOM 4228 CG PRO C 147 5.660 134.590 38.800 1.00 26.00 C ANISOU 4228 CG PRO C 147 3651 3554 2675 -408 -11 -27 C ATOM 4229 CD PRO C 147 6.774 135.570 39.030 1.00 25.66 C ANISOU 4229 CD PRO C 147 3589 3574 2587 -364 -62 -42 C ATOM 4230 N GLU C 148 4.777 134.970 35.086 1.00 25.63 N ANISOU 4230 N GLU C 148 3488 3560 2691 -517 -17 -196 N ATOM 4231 CA GLU C 148 3.512 135.500 34.539 1.00 25.95 C ANISOU 4231 CA GLU C 148 3486 3640 2735 -584 -14 -200 C ATOM 4232 C GLU C 148 2.493 135.687 35.676 1.00 26.01 C ANISOU 4232 C GLU C 148 3486 3647 2750 -606 22 -127 C ATOM 4233 O GLU C 148 2.648 135.041 36.712 1.00 25.48 O ANISOU 4233 O GLU C 148 3466 3528 2686 -586 44 -80 O ATOM 4234 CB GLU C 148 2.967 134.558 33.481 1.00 27.25 C ANISOU 4234 CB GLU C 148 3661 3759 2933 -640 -34 -251 C ATOM 4235 CG GLU C 148 3.798 134.585 32.229 1.00 27.72 C ANISOU 4235 CG GLU C 148 3731 3846 2958 -609 -53 -328 C ATOM 4236 CD GLU C 148 3.223 135.574 31.276 1.00 27.83 C ANISOU 4236 CD GLU C 148 3692 3949 2934 -645 -74 -343 C ATOM 4237 OE1 GLU C 148 3.215 136.766 31.595 1.00 27.47 O ANISOU 4237 OE1 GLU C 148 3602 3969 2869 -630 -65 -300 O ATOM 4238 OE2 GLU C 148 2.736 135.146 30.246 1.00 29.52 O ANISOU 4238 OE2 GLU C 148 3919 4159 3137 -688 -107 -396 O ATOM 4239 N PRO C 149 1.461 136.533 35.506 1.00 25.96 N ANISOU 4239 N PRO C 149 3422 3699 2743 -636 36 -108 N ATOM 4240 CA PRO C 149 1.168 137.293 34.281 1.00 25.66 C ANISOU 4240 CA PRO C 149 3330 3722 2697 -658 4 -147 C ATOM 4241 C PRO C 149 1.447 138.778 34.436 1.00 25.30 C ANISOU 4241 C PRO C 149 3269 3735 2609 -611 7 -137 C ATOM 4242 O PRO C 149 1.773 139.257 35.536 1.00 24.87 O ANISOU 4242 O PRO C 149 3250 3674 2526 -566 30 -112 O ATOM 4243 CB PRO C 149 -0.337 137.091 34.125 1.00 26.58 C ANISOU 4243 CB PRO C 149 3382 3852 2864 -724 11 -111 C ATOM 4244 CG PRO C 149 -0.828 137.077 35.546 1.00 26.60 C ANISOU 4244 CG PRO C 149 3389 3844 2875 -703 80 -36 C ATOM 4245 CD PRO C 149 0.272 136.454 36.373 1.00 26.39 C ANISOU 4245 CD PRO C 149 3451 3756 2820 -660 89 -36 C ATOM 4246 N VAL C 150 1.352 139.485 33.319 1.00 25.49 N ANISOU 4246 N VAL C 150 3255 3809 2622 -622 -22 -159 N ATOM 4247 CA VAL C 150 1.254 140.944 33.303 1.00 25.32 C ANISOU 4247 CA VAL C 150 3213 3829 2578 -591 -21 -138 C ATOM 4248 C VAL C 150 -0.060 141.300 32.634 1.00 25.77 C ANISOU 4248 C VAL C 150 3201 3932 2659 -616 -29 -112 C ATOM 4249 O VAL C 150 -0.504 140.580 31.744 1.00 25.85 O ANISOU 4249 O VAL C 150 3182 3957 2684 -668 -63 -131 O ATOM 4250 CB VAL C 150 2.441 141.566 32.522 1.00 25.14 C ANISOU 4250 CB VAL C 150 3200 3827 2524 -579 -51 -163 C ATOM 4251 CG1 VAL C 150 2.106 142.875 31.801 1.00 25.27 C ANISOU 4251 CG1 VAL C 150 3186 3886 2530 -575 -66 -139 C ATOM 4252 CG2 VAL C 150 3.636 141.773 33.428 1.00 25.12 C ANISOU 4252 CG2 VAL C 150 3239 3795 2509 -547 -52 -165 C ATOM 4253 N THR C 151 -0.676 142.398 33.078 1.00 25.94 N ANISOU 4253 N THR C 151 3200 3972 2684 -574 -3 -72 N ATOM 4254 CA THR C 151 -1.788 143.031 32.360 1.00 26.34 C ANISOU 4254 CA THR C 151 3173 4075 2759 -574 -18 -35 C ATOM 4255 C THR C 151 -1.302 144.385 31.870 1.00 26.51 C ANISOU 4255 C THR C 151 3216 4104 2753 -533 -39 -29 C ATOM 4256 O THR C 151 -0.628 145.109 32.612 1.00 25.92 O ANISOU 4256 O THR C 151 3203 3984 2659 -491 -18 -36 O ATOM 4257 CB THR C 151 -3.002 143.307 33.281 1.00 26.96 C ANISOU 4257 CB THR C 151 3200 4167 2878 -534 45 22 C ATOM 4258 OG1 THR C 151 -3.543 142.079 33.757 1.00 27.01 O ANISOU 4258 OG1 THR C 151 3175 4167 2922 -585 71 38 O ATOM 4259 CG2 THR C 151 -4.133 144.090 32.567 1.00 27.67 C ANISOU 4259 CG2 THR C 151 3193 4318 3004 -513 27 73 C ATOM 4260 N VAL C 152 -1.670 144.733 30.645 1.00 26.99 N ANISOU 4260 N VAL C 152 3231 4215 2808 -550 -87 -10 N ATOM 4261 CA VAL C 152 -1.432 146.067 30.107 1.00 27.47 C ANISOU 4261 CA VAL C 152 3305 4280 2853 -512 -105 22 C ATOM 4262 C VAL C 152 -2.770 146.671 29.732 1.00 28.45 C ANISOU 4262 C VAL C 152 3350 4448 3011 -478 -118 84 C ATOM 4263 O VAL C 152 -3.610 146.015 29.112 1.00 28.88 O ANISOU 4263 O VAL C 152 3330 4564 3080 -518 -158 96 O ATOM 4264 CB VAL C 152 -0.511 146.052 28.870 1.00 27.42 C ANISOU 4264 CB VAL C 152 3320 4304 2793 -550 -147 8 C ATOM 4265 CG1 VAL C 152 -0.152 147.474 28.460 1.00 27.24 C ANISOU 4265 CG1 VAL C 152 3319 4269 2761 -519 -156 60 C ATOM 4266 CG2 VAL C 152 0.753 145.259 29.164 1.00 26.77 C ANISOU 4266 CG2 VAL C 152 3288 4194 2689 -575 -130 -48 C ATOM 4267 N SER C 153 -2.988 147.906 30.160 1.00 29.02 N ANISOU 4267 N SER C 153 3439 4483 3103 -402 -91 122 N ATOM 4268 CA SER C 153 -4.119 148.681 29.685 1.00 30.60 C ANISOU 4268 CA SER C 153 3565 4720 3340 -347 -107 193 C ATOM 4269 C SER C 153 -3.579 150.008 29.176 1.00 30.87 C ANISOU 4269 C SER C 153 3661 4709 3359 -308 -129 228 C ATOM 4270 O SER C 153 -2.392 150.299 29.337 1.00 30.40 O ANISOU 4270 O SER C 153 3689 4590 3273 -332 -125 196 O ATOM 4271 CB SER C 153 -5.149 148.859 30.802 1.00 31.59 C ANISOU 4271 CB SER C 153 3646 4837 3521 -268 -32 218 C ATOM 4272 OG SER C 153 -4.605 149.612 31.856 1.00 32.56 O ANISOU 4272 OG SER C 153 3875 4868 3630 -202 27 188 O ATOM 4273 N TRP C 154 -4.437 150.784 28.526 1.00 31.68 N ANISOU 4273 N TRP C 154 3708 4841 3487 -253 -158 304 N ATOM 4274 CA TRP C 154 -4.061 152.079 27.988 1.00 32.25 C ANISOU 4274 CA TRP C 154 3837 4859 3555 -212 -180 359 C ATOM 4275 C TRP C 154 -5.014 153.153 28.499 1.00 33.62 C ANISOU 4275 C TRP C 154 3997 4980 3796 -86 -145 412 C ATOM 4276 O TRP C 154 -6.232 152.971 28.464 1.00 34.38 O ANISOU 4276 O TRP C 154 3982 5147 3934 -34 -142 456 O ATOM 4277 CB TRP C 154 -4.048 152.043 26.464 1.00 32.49 C ANISOU 4277 CB TRP C 154 3834 4975 3535 -258 -259 415 C ATOM 4278 CG TRP C 154 -2.864 151.315 25.918 1.00 31.76 C ANISOU 4278 CG TRP C 154 3790 4910 3367 -354 -273 364 C ATOM 4279 CD1 TRP C 154 -2.766 149.973 25.680 1.00 31.04 C ANISOU 4279 CD1 TRP C 154 3673 4887 3234 -423 -288 298 C ATOM 4280 CD2 TRP C 154 -1.601 151.878 25.575 1.00 31.51 C ANISOU 4280 CD2 TRP C 154 3837 4834 3301 -386 -264 376 C ATOM 4281 NE1 TRP C 154 -1.525 149.670 25.195 1.00 30.59 N ANISOU 4281 NE1 TRP C 154 3676 4835 3112 -477 -282 265 N ATOM 4282 CE2 TRP C 154 -0.786 150.820 25.117 1.00 30.91 C ANISOU 4282 CE2 TRP C 154 3768 4817 3158 -460 -264 319 C ATOM 4283 CE3 TRP C 154 -1.074 153.178 25.603 1.00 31.85 C ANISOU 4283 CE3 TRP C 154 3942 4786 3372 -362 -254 436 C ATOM 4284 CZ2 TRP C 154 0.530 151.017 24.692 1.00 30.98 C ANISOU 4284 CZ2 TRP C 154 3825 4819 3127 -502 -244 327 C ATOM 4285 CZ3 TRP C 154 0.238 153.376 25.183 1.00 31.94 C ANISOU 4285 CZ3 TRP C 154 4002 4783 3352 -427 -246 449 C ATOM 4286 CH2 TRP C 154 1.024 152.298 24.726 1.00 31.57 C ANISOU 4286 CH2 TRP C 154 3940 4818 3237 -492 -235 399 C ATOM 4287 N ASN C 155 -4.441 154.258 28.978 1.00 34.43 N ANISOU 4287 N ASN C 155 4211 4956 3913 -38 -121 408 N ATOM 4288 CA ASN C 155 -5.199 155.382 29.541 1.00 36.22 C ANISOU 4288 CA ASN C 155 4464 5098 4201 101 -79 442 C ATOM 4289 C ASN C 155 -6.210 154.917 30.593 1.00 36.59 C ANISOU 4289 C ASN C 155 4447 5181 4276 182 4 415 C ATOM 4290 O ASN C 155 -7.404 155.241 30.534 1.00 37.35 O ANISOU 4290 O ASN C 155 4447 5318 4427 289 29 481 O ATOM 4291 CB ASN C 155 -5.850 156.203 28.420 1.00 37.43 C ANISOU 4291 CB ASN C 155 4565 5272 4384 160 -132 559 C ATOM 4292 CG ASN C 155 -4.829 156.909 27.544 1.00 38.41 C ANISOU 4292 CG ASN C 155 4779 5335 4481 97 -189 603 C ATOM 4293 OD1 ASN C 155 -4.831 156.733 26.330 1.00 39.85 O ANISOU 4293 OD1 ASN C 155 4909 5608 4622 48 -252 673 O ATOM 4294 ND2 ASN C 155 -3.957 157.719 28.149 1.00 38.84 N ANISOU 4294 ND2 ASN C 155 4969 5235 4553 93 -170 568 N ATOM 4295 N SER C 156 -5.691 154.131 31.541 1.00 36.09 N ANISOU 4295 N SER C 156 4428 5109 4174 132 47 328 N ATOM 4296 CA SER C 156 -6.453 153.534 32.640 1.00 36.36 C ANISOU 4296 CA SER C 156 4418 5182 4216 188 140 303 C ATOM 4297 C SER C 156 -7.688 152.749 32.186 1.00 36.82 C ANISOU 4297 C SER C 156 4286 5380 4323 184 143 374 C ATOM 4298 O SER C 156 -8.732 152.787 32.834 1.00 37.94 O ANISOU 4298 O SER C 156 4350 5558 4509 282 228 408 O ATOM 4299 CB SER C 156 -6.835 154.618 33.655 1.00 37.85 C ANISOU 4299 CB SER C 156 4697 5267 4416 343 225 285 C ATOM 4300 OG SER C 156 -5.680 155.319 34.086 1.00 37.73 O ANISOU 4300 OG SER C 156 4863 5113 4360 325 199 212 O ATOM 4301 N GLY C 157 -7.559 152.039 31.069 1.00 36.35 N ANISOU 4301 N GLY C 157 4155 5402 4256 70 50 395 N ATOM 4302 CA GLY C 157 -8.664 151.269 30.498 1.00 36.95 C ANISOU 4302 CA GLY C 157 4055 5606 4379 36 16 456 C ATOM 4303 C GLY C 157 -9.630 152.043 29.615 1.00 37.91 C ANISOU 4303 C GLY C 157 4067 5783 4554 112 -37 559 C ATOM 4304 O GLY C 157 -10.517 151.436 29.015 1.00 38.37 O ANISOU 4304 O GLY C 157 3970 5956 4652 69 -96 614 O ATOM 4305 N ALA C 158 -9.488 153.368 29.539 1.00 38.75 N ANISOU 4305 N ALA C 158 4250 5805 4668 222 -28 590 N ATOM 4306 CA ALA C 158 -10.383 154.195 28.719 1.00 40.54 C ANISOU 4306 CA ALA C 158 4383 6073 4949 315 -80 702 C ATOM 4307 C ALA C 158 -10.161 153.993 27.222 1.00 40.68 C ANISOU 4307 C ALA C 158 4374 6166 4917 217 -221 746 C ATOM 4308 O ALA C 158 -11.102 154.120 26.449 1.00 42.76 O ANISOU 4308 O ALA C 158 4506 6525 5216 249 -295 840 O ATOM 4309 CB ALA C 158 -10.233 155.668 29.074 1.00 41.48 C ANISOU 4309 CB ALA C 158 4617 6052 5091 463 -30 722 C ATOM 4310 N LEU C 159 -8.927 153.698 26.815 1.00 39.62 N ANISOU 4310 N LEU C 159 4361 5996 4696 105 -257 682 N ATOM 4311 CA LEU C 159 -8.614 153.478 25.398 1.00 39.57 C ANISOU 4311 CA LEU C 159 4355 6066 4614 18 -373 715 C ATOM 4312 C LEU C 159 -8.528 151.979 25.115 1.00 39.00 C ANISOU 4312 C LEU C 159 4237 6087 4494 -119 -418 643 C ATOM 4313 O LEU C 159 -7.599 151.316 25.582 1.00 37.54 O ANISOU 4313 O LEU C 159 4135 5857 4271 -191 -374 549 O ATOM 4314 CB LEU C 159 -7.299 154.168 25.033 1.00 39.12 C ANISOU 4314 CB LEU C 159 4455 5916 4492 -7 -371 706 C ATOM 4315 CG LEU C 159 -6.813 154.039 23.587 1.00 39.27 C ANISOU 4315 CG LEU C 159 4500 6012 4410 -85 -464 745 C ATOM 4316 CD1 LEU C 159 -7.803 154.677 22.615 1.00 40.96 C ANISOU 4316 CD1 LEU C 159 4636 6299 4628 -15 -553 874 C ATOM 4317 CD2 LEU C 159 -5.435 154.667 23.464 1.00 38.78 C ANISOU 4317 CD2 LEU C 159 4578 5854 4305 -117 -430 741 C ATOM 4318 N THR C 160 -9.511 151.458 24.380 1.00 40.24 N ANISOU 4318 N THR C 160 4263 6365 4660 -152 -514 688 N ATOM 4319 CA THR C 160 -9.553 150.040 23.999 1.00 40.58 C ANISOU 4319 CA THR C 160 4270 6485 4665 -288 -579 619 C ATOM 4320 C THR C 160 -9.542 149.775 22.485 1.00 41.37 C ANISOU 4320 C THR C 160 4379 6680 4660 -358 -723 633 C ATOM 4321 O THR C 160 -9.097 148.703 22.063 1.00 41.12 O ANISOU 4321 O THR C 160 4396 6673 4554 -468 -767 543 O ATOM 4322 CB THR C 160 -10.780 149.341 24.607 1.00 41.37 C ANISOU 4322 CB THR C 160 4202 6643 4873 -304 -575 639 C ATOM 4323 OG1 THR C 160 -11.971 150.008 24.182 1.00 43.01 O ANISOU 4323 OG1 THR C 160 4261 6932 5147 -226 -637 758 O ATOM 4324 CG2 THR C 160 -10.700 149.360 26.136 1.00 41.08 C ANISOU 4324 CG2 THR C 160 4178 6523 4907 -248 -421 610 C ATOM 4325 N SER C 161 -10.025 150.723 21.678 1.00 42.70 N ANISOU 4325 N SER C 161 4513 6899 4812 -287 -795 742 N ATOM 4326 CA SER C 161 -10.021 150.571 20.214 1.00 43.55 C ANISOU 4326 CA SER C 161 4646 7109 4794 -340 -936 765 C ATOM 4327 C SER C 161 -8.603 150.645 19.658 1.00 42.13 C ANISOU 4327 C SER C 161 4642 6889 4475 -374 -901 716 C ATOM 4328 O SER C 161 -7.839 151.540 20.008 1.00 41.55 O ANISOU 4328 O SER C 161 4652 6723 4413 -314 -808 746 O ATOM 4329 CB SER C 161 -10.881 151.645 19.542 1.00 45.46 C ANISOU 4329 CB SER C 161 4808 7412 5052 -240 -1020 916 C ATOM 4330 OG SER C 161 -12.239 151.513 19.924 1.00 46.86 O ANISOU 4330 OG SER C 161 4793 7654 5360 -208 -1063 973 O ATOM 4331 N GLY C 162 -8.258 149.684 18.806 1.00 42.23 N ANISOU 4331 N GLY C 162 4713 6971 4363 -471 -973 638 N ATOM 4332 CA GLY C 162 -6.929 149.592 18.217 1.00 41.56 C ANISOU 4332 CA GLY C 162 4781 6872 4139 -501 -929 588 C ATOM 4333 C GLY C 162 -5.840 149.054 19.134 1.00 40.02 C ANISOU 4333 C GLY C 162 4655 6576 3975 -531 -801 482 C ATOM 4334 O GLY C 162 -4.677 149.012 18.733 1.00 39.48 O ANISOU 4334 O GLY C 162 4693 6498 3810 -546 -747 450 O ATOM 4335 N VAL C 163 -6.199 148.641 20.352 1.00 39.15 N ANISOU 4335 N VAL C 163 4480 6401 3993 -536 -749 438 N ATOM 4336 CA VAL C 163 -5.234 148.121 21.317 1.00 37.60 C ANISOU 4336 CA VAL C 163 4344 6112 3829 -559 -639 347 C ATOM 4337 C VAL C 163 -5.005 146.637 21.055 1.00 37.71 C ANISOU 4337 C VAL C 163 4393 6148 3789 -649 -671 229 C ATOM 4338 O VAL C 163 -5.959 145.896 20.839 1.00 38.18 O ANISOU 4338 O VAL C 163 4386 6253 3867 -703 -759 206 O ATOM 4339 CB VAL C 163 -5.729 148.305 22.769 1.00 36.94 C ANISOU 4339 CB VAL C 163 4193 5953 3888 -517 -566 356 C ATOM 4340 CG1 VAL C 163 -4.777 147.653 23.775 1.00 36.02 C ANISOU 4340 CG1 VAL C 163 4143 5752 3792 -545 -473 265 C ATOM 4341 CG2 VAL C 163 -5.896 149.782 23.080 1.00 37.02 C ANISOU 4341 CG2 VAL C 163 4197 5916 3952 -415 -528 455 C ATOM 4342 N HIS C 164 -3.742 146.207 21.087 1.00 36.50 N ANISOU 4342 N HIS C 164 4338 5953 3577 -664 -602 156 N ATOM 4343 CA HIS C 164 -3.427 144.787 21.124 1.00 35.96 C ANISOU 4343 CA HIS C 164 4315 5866 3484 -728 -605 36 C ATOM 4344 C HIS C 164 -2.232 144.514 22.031 1.00 33.89 C ANISOU 4344 C HIS C 164 4106 5516 3254 -712 -492 -14 C ATOM 4345 O HIS C 164 -1.178 145.133 21.872 1.00 32.47 O ANISOU 4345 O HIS C 164 3974 5331 3031 -676 -430 10 O ATOM 4346 CB HIS C 164 -3.166 144.231 19.729 1.00 37.80 C ANISOU 4346 CB HIS C 164 4629 6173 3562 -759 -673 -21 C ATOM 4347 CG HIS C 164 -3.184 142.735 19.690 1.00 38.67 C ANISOU 4347 CG HIS C 164 4786 6250 3657 -826 -707 -149 C ATOM 4348 ND1 HIS C 164 -2.048 141.971 19.839 1.00 38.74 N ANISOU 4348 ND1 HIS C 164 4886 6201 3631 -817 -628 -240 N ATOM 4349 CD2 HIS C 164 -4.213 141.863 19.600 1.00 39.84 C ANISOU 4349 CD2 HIS C 164 4897 6399 3842 -905 -813 -196 C ATOM 4350 CE1 HIS C 164 -2.372 140.691 19.802 1.00 38.96 C ANISOU 4350 CE1 HIS C 164 4951 6185 3666 -879 -681 -343 C ATOM 4351 NE2 HIS C 164 -3.680 140.599 19.653 1.00 40.33 N ANISOU 4351 NE2 HIS C 164 5050 6390 3884 -944 -798 -319 N ATOM 4352 N THR C 165 -2.425 143.607 22.992 1.00 32.76 N ANISOU 4352 N THR C 165 3946 5308 3194 -742 -470 -69 N ATOM 4353 CA THR C 165 -1.368 143.150 23.873 1.00 31.90 C ANISOU 4353 CA THR C 165 3886 5121 3114 -729 -383 -119 C ATOM 4354 C THR C 165 -1.004 141.733 23.469 1.00 31.70 C ANISOU 4354 C THR C 165 3926 5074 3043 -771 -400 -224 C ATOM 4355 O THR C 165 -1.864 140.851 23.382 1.00 32.26 O ANISOU 4355 O THR C 165 3982 5134 3141 -832 -464 -264 O ATOM 4356 CB THR C 165 -1.783 143.250 25.349 1.00 31.78 C ANISOU 4356 CB THR C 165 3821 5040 3213 -715 -335 -90 C ATOM 4357 OG1 THR C 165 -1.966 144.631 25.673 1.00 31.96 O ANISOU 4357 OG1 THR C 165 3813 5067 3265 -658 -311 -8 O ATOM 4358 CG2 THR C 165 -0.709 142.669 26.279 1.00 31.03 C ANISOU 4358 CG2 THR C 165 3782 4870 3139 -703 -264 -138 C ATOM 4359 N PHE C 166 0.278 141.532 23.194 1.00 31.14 N ANISOU 4359 N PHE C 166 3925 4997 2911 -737 -343 -266 N ATOM 4360 CA PHE C 166 0.756 140.274 22.635 1.00 31.55 C ANISOU 4360 CA PHE C 166 4059 5027 2901 -749 -348 -372 C ATOM 4361 C PHE C 166 1.008 139.245 23.719 1.00 31.36 C ANISOU 4361 C PHE C 166 4052 4898 2967 -756 -312 -419 C ATOM 4362 O PHE C 166 1.254 139.615 24.864 1.00 30.60 O ANISOU 4362 O PHE C 166 3914 4761 2950 -734 -261 -369 O ATOM 4363 CB PHE C 166 2.026 140.523 21.830 1.00 31.30 C ANISOU 4363 CB PHE C 166 4083 5047 2764 -690 -284 -384 C ATOM 4364 CG PHE C 166 1.769 141.269 20.570 1.00 31.97 C ANISOU 4364 CG PHE C 166 4180 5238 2730 -687 -323 -344 C ATOM 4365 CD1 PHE C 166 1.396 140.579 19.424 1.00 33.26 C ANISOU 4365 CD1 PHE C 166 4419 5446 2772 -707 -389 -421 C ATOM 4366 CD2 PHE C 166 1.825 142.655 20.530 1.00 31.17 C ANISOU 4366 CD2 PHE C 166 4026 5182 2634 -668 -305 -228 C ATOM 4367 CE1 PHE C 166 1.134 141.257 18.248 1.00 34.18 C ANISOU 4367 CE1 PHE C 166 4558 5671 2759 -700 -434 -378 C ATOM 4368 CE2 PHE C 166 1.556 143.339 19.356 1.00 32.14 C ANISOU 4368 CE2 PHE C 166 4166 5401 2644 -662 -344 -174 C ATOM 4369 CZ PHE C 166 1.207 142.635 18.214 1.00 33.53 C ANISOU 4369 CZ PHE C 166 4415 5640 2685 -676 -409 -245 C ATOM 4370 N PRO C 167 0.958 137.947 23.361 1.00 32.80 N ANISOU 4370 N PRO C 167 4306 5027 3130 -784 -343 -517 N ATOM 4371 CA PRO C 167 1.358 136.931 24.332 1.00 32.65 C ANISOU 4371 CA PRO C 167 4318 4896 3193 -778 -302 -553 C ATOM 4372 C PRO C 167 2.838 137.045 24.686 1.00 32.28 C ANISOU 4372 C PRO C 167 4290 4839 3134 -689 -208 -550 C ATOM 4373 O PRO C 167 3.638 137.551 23.882 1.00 32.13 O ANISOU 4373 O PRO C 167 4283 4894 3029 -638 -172 -552 O ATOM 4374 CB PRO C 167 1.050 135.603 23.624 1.00 34.17 C ANISOU 4374 CB PRO C 167 4605 5024 3355 -823 -363 -666 C ATOM 4375 CG PRO C 167 0.968 135.926 22.172 1.00 35.27 C ANISOU 4375 CG PRO C 167 4788 5258 3355 -821 -413 -710 C ATOM 4376 CD PRO C 167 0.579 137.369 22.055 1.00 34.19 C ANISOU 4376 CD PRO C 167 4555 5234 3203 -818 -421 -600 C ATOM 4377 N ALA C 168 3.185 136.592 25.886 1.00 31.59 N ANISOU 4377 N ALA C 168 4198 4672 3134 -671 -171 -533 N ATOM 4378 CA ALA C 168 4.546 136.688 26.377 1.00 31.44 C ANISOU 4378 CA ALA C 168 4175 4647 3124 -592 -100 -516 C ATOM 4379 C ALA C 168 5.462 135.709 25.661 1.00 32.30 C ANISOU 4379 C ALA C 168 4358 4730 3184 -528 -65 -601 C ATOM 4380 O ALA C 168 5.038 134.635 25.239 1.00 32.89 O ANISOU 4380 O ALA C 168 4513 4735 3249 -548 -97 -684 O ATOM 4381 CB ALA C 168 4.593 136.440 27.878 1.00 31.00 C ANISOU 4381 CB ALA C 168 4101 4517 3160 -588 -86 -471 C ATOM 4382 N VAL C 169 6.721 136.111 25.531 1.00 32.39 N ANISOU 4382 N VAL C 169 4339 4796 3172 -452 1 -578 N ATOM 4383 CA VAL C 169 7.793 135.236 25.091 1.00 33.75 C ANISOU 4383 CA VAL C 169 4558 4949 3317 -358 62 -640 C ATOM 4384 C VAL C 169 8.683 134.968 26.303 1.00 33.19 C ANISOU 4384 C VAL C 169 4442 4827 3340 -303 92 -592 C ATOM 4385 O VAL C 169 9.031 135.911 27.011 1.00 32.22 O ANISOU 4385 O VAL C 169 4235 4751 3257 -317 91 -507 O ATOM 4386 CB VAL C 169 8.614 135.923 23.996 1.00 34.81 C ANISOU 4386 CB VAL C 169 4664 5207 3355 -306 126 -628 C ATOM 4387 CG1 VAL C 169 9.896 135.158 23.724 1.00 36.53 C ANISOU 4387 CG1 VAL C 169 4896 5422 3561 -185 216 -668 C ATOM 4388 CG2 VAL C 169 7.785 136.055 22.728 1.00 35.68 C ANISOU 4388 CG2 VAL C 169 4841 5371 3347 -346 90 -679 C ATOM 4389 N LEU C 170 9.031 133.696 26.538 1.00 33.87 N ANISOU 4389 N LEU C 170 4595 4813 3463 -243 108 -647 N ATOM 4390 CA LEU C 170 10.038 133.309 27.534 1.00 34.02 C ANISOU 4390 CA LEU C 170 4575 4791 3559 -164 135 -601 C ATOM 4391 C LEU C 170 11.417 133.254 26.876 1.00 35.12 C ANISOU 4391 C LEU C 170 4671 5002 3672 -45 219 -609 C ATOM 4392 O LEU C 170 11.683 132.382 26.046 1.00 36.06 O ANISOU 4392 O LEU C 170 4867 5088 3747 34 267 -695 O ATOM 4393 CB LEU C 170 9.717 131.944 28.166 1.00 34.14 C ANISOU 4393 CB LEU C 170 4683 4650 3638 -149 112 -637 C ATOM 4394 CG LEU C 170 10.721 131.463 29.231 1.00 34.07 C ANISOU 4394 CG LEU C 170 4643 4596 3707 -58 129 -578 C ATOM 4395 CD1 LEU C 170 10.584 132.271 30.515 1.00 33.09 C ANISOU 4395 CD1 LEU C 170 4448 4505 3622 -114 84 -475 C ATOM 4396 CD2 LEU C 170 10.578 129.971 29.508 1.00 35.23 C ANISOU 4396 CD2 LEU C 170 4904 4576 3907 -14 124 -623 C ATOM 4397 N GLN C 171 12.285 134.189 27.247 1.00 35.17 N ANISOU 4397 N GLN C 171 4553 5105 3706 -32 237 -518 N ATOM 4398 CA GLN C 171 13.623 134.288 26.653 1.00 36.58 C ANISOU 4398 CA GLN C 171 4649 5377 3874 70 325 -497 C ATOM 4399 C GLN C 171 14.548 133.215 27.243 1.00 37.25 C ANISOU 4399 C GLN C 171 4722 5396 4034 195 352 -497 C ATOM 4400 O GLN C 171 14.233 132.609 28.254 1.00 37.58 O ANISOU 4400 O GLN C 171 4809 5331 4139 188 292 -490 O ATOM 4401 CB GLN C 171 14.202 135.691 26.873 1.00 36.47 C ANISOU 4401 CB GLN C 171 4493 5479 3883 17 319 -388 C ATOM 4402 CG GLN C 171 13.377 136.823 26.256 1.00 36.09 C ANISOU 4402 CG GLN C 171 4454 5490 3767 -90 298 -372 C ATOM 4403 CD GLN C 171 13.555 138.156 26.975 1.00 36.07 C ANISOU 4403 CD GLN C 171 4357 5529 3821 -175 247 -272 C ATOM 4404 OE1 GLN C 171 13.066 138.342 28.099 1.00 36.11 O ANISOU 4404 OE1 GLN C 171 4378 5468 3875 -227 169 -256 O ATOM 4405 NE2 GLN C 171 14.220 139.103 26.323 1.00 36.75 N ANISOU 4405 NE2 GLN C 171 4354 5717 3892 -192 292 -204 N ATOM 4406 N SER C 172 15.695 133.001 26.616 1.00 38.29 N ANISOU 4406 N SER C 172 4788 5600 4160 317 448 -493 N ATOM 4407 CA SER C 172 16.707 132.046 27.111 1.00 39.05 C ANISOU 4407 CA SER C 172 4848 5651 4338 462 482 -478 C ATOM 4408 C SER C 172 17.241 132.412 28.511 1.00 37.90 C ANISOU 4408 C SER C 172 4586 5516 4300 438 400 -364 C ATOM 4409 O SER C 172 17.718 131.541 29.240 1.00 38.08 O ANISOU 4409 O SER C 172 4610 5463 4395 532 383 -345 O ATOM 4410 CB SER C 172 17.860 131.950 26.112 1.00 41.05 C ANISOU 4410 CB SER C 172 5021 6015 4564 602 617 -478 C ATOM 4411 OG SER C 172 18.251 133.238 25.673 1.00 41.47 O ANISOU 4411 OG SER C 172 4938 6228 4591 534 649 -396 O ATOM 4412 N SER C 173 17.134 133.694 28.887 1.00 36.19 N ANISOU 4412 N SER C 173 4282 5381 4088 314 342 -291 N ATOM 4413 CA SER C 173 17.428 134.156 30.247 1.00 35.16 C ANISOU 4413 CA SER C 173 4078 5251 4032 263 238 -203 C ATOM 4414 C SER C 173 16.529 133.560 31.342 1.00 33.83 C ANISOU 4414 C SER C 173 4033 4949 3872 229 155 -219 C ATOM 4415 O SER C 173 16.850 133.683 32.519 1.00 33.27 O ANISOU 4415 O SER C 173 3925 4869 3847 220 74 -152 O ATOM 4416 CB SER C 173 17.316 135.692 30.307 1.00 34.13 C ANISOU 4416 CB SER C 173 3871 5208 3889 127 192 -146 C ATOM 4417 OG SER C 173 16.001 136.116 29.975 1.00 33.16 O ANISOU 4417 OG SER C 173 3859 5048 3694 29 178 -198 O ATOM 4418 N GLY C 174 15.386 132.979 30.964 1.00 32.86 N ANISOU 4418 N GLY C 174 4054 4731 3702 199 169 -301 N ATOM 4419 CA GLY C 174 14.397 132.511 31.937 1.00 31.61 C ANISOU 4419 CA GLY C 174 4002 4456 3554 144 104 -301 C ATOM 4420 C GLY C 174 13.402 133.580 32.362 1.00 29.67 C ANISOU 4420 C GLY C 174 3765 4236 3271 7 50 -281 C ATOM 4421 O GLY C 174 12.586 133.337 33.249 1.00 28.89 O ANISOU 4421 O GLY C 174 3738 4064 3176 -40 8 -265 O ATOM 4422 N LEU C 175 13.453 134.757 31.725 1.00 29.14 N ANISOU 4422 N LEU C 175 3630 4271 3169 -50 61 -275 N ATOM 4423 CA LEU C 175 12.537 135.869 31.997 1.00 27.90 C ANISOU 4423 CA LEU C 175 3483 4137 2981 -162 18 -258 C ATOM 4424 C LEU C 175 11.604 136.096 30.809 1.00 27.20 C ANISOU 4424 C LEU C 175 3436 4065 2835 -212 52 -314 C ATOM 4425 O LEU C 175 11.980 135.840 29.666 1.00 27.95 O ANISOU 4425 O LEU C 175 3524 4198 2898 -169 108 -354 O ATOM 4426 CB LEU C 175 13.320 137.160 32.283 1.00 28.28 C ANISOU 4426 CB LEU C 175 3428 4273 3044 -197 -16 -195 C ATOM 4427 CG LEU C 175 14.302 137.118 33.463 1.00 28.91 C ANISOU 4427 CG LEU C 175 3454 4356 3174 -164 -79 -135 C ATOM 4428 CD1 LEU C 175 15.169 138.368 33.499 1.00 29.42 C ANISOU 4428 CD1 LEU C 175 3407 4507 3266 -214 -119 -80 C ATOM 4429 CD2 LEU C 175 13.552 136.956 34.771 1.00 28.84 C ANISOU 4429 CD2 LEU C 175 3537 4274 3149 -190 -140 -125 C ATOM 4430 N TYR C 176 10.409 136.614 31.082 1.00 25.89 N ANISOU 4430 N TYR C 176 3308 3880 2651 -295 18 -313 N ATOM 4431 CA TYR C 176 9.410 136.887 30.042 1.00 25.76 C ANISOU 4431 CA TYR C 176 3320 3885 2583 -348 27 -353 C ATOM 4432 C TYR C 176 9.533 138.306 29.487 1.00 25.84 C ANISOU 4432 C TYR C 176 3269 3986 2562 -386 29 -313 C ATOM 4433 O TYR C 176 10.017 139.221 30.157 1.00 25.42 O ANISOU 4433 O TYR C 176 3165 3956 2537 -402 6 -257 O ATOM 4434 CB TYR C 176 7.986 136.712 30.574 1.00 24.94 C ANISOU 4434 CB TYR C 176 3266 3720 2489 -413 -7 -356 C ATOM 4435 CG TYR C 176 7.641 135.307 31.024 1.00 25.11 C ANISOU 4435 CG TYR C 176 3357 3636 2547 -401 -9 -384 C ATOM 4436 CD1 TYR C 176 7.120 134.367 30.133 1.00 25.66 C ANISOU 4436 CD1 TYR C 176 3489 3656 2606 -416 -8 -456 C ATOM 4437 CD2 TYR C 176 7.816 134.927 32.354 1.00 24.84 C ANISOU 4437 CD2 TYR C 176 3338 3545 2554 -381 -19 -335 C ATOM 4438 CE1 TYR C 176 6.795 133.068 30.566 1.00 26.22 C ANISOU 4438 CE1 TYR C 176 3632 3605 2726 -418 -16 -477 C ATOM 4439 CE2 TYR C 176 7.494 133.648 32.796 1.00 25.26 C ANISOU 4439 CE2 TYR C 176 3460 3491 2647 -375 -18 -342 C ATOM 4440 CZ TYR C 176 6.993 132.715 31.912 1.00 26.04 C ANISOU 4440 CZ TYR C 176 3616 3523 2754 -396 -15 -410 C ATOM 4441 OH TYR C 176 6.697 131.448 32.396 1.00 26.25 O ANISOU 4441 OH TYR C 176 3718 3420 2835 -399 -19 -409 O ATOM 4442 N SER C 177 9.064 138.481 28.259 1.00 26.64 N ANISOU 4442 N SER C 177 3386 4133 2602 -404 46 -342 N ATOM 4443 CA SER C 177 8.860 139.811 27.682 1.00 27.17 C ANISOU 4443 CA SER C 177 3415 4273 2637 -448 41 -294 C ATOM 4444 C SER C 177 7.576 139.827 26.877 1.00 27.63 C ANISOU 4444 C SER C 177 3517 4340 2640 -489 15 -325 C ATOM 4445 O SER C 177 7.206 138.815 26.282 1.00 28.13 O ANISOU 4445 O SER C 177 3637 4384 2667 -480 14 -395 O ATOM 4446 CB SER C 177 10.034 140.216 26.773 1.00 27.85 C ANISOU 4446 CB SER C 177 3445 4445 2690 -414 99 -265 C ATOM 4447 OG SER C 177 11.170 140.535 27.551 1.00 28.57 O ANISOU 4447 OG SER C 177 3462 4543 2850 -399 102 -211 O ATOM 4448 N LEU C 178 6.917 140.981 26.841 1.00 27.74 N ANISOU 4448 N LEU C 178 3507 4381 2651 -532 -13 -271 N ATOM 4449 CA LEU C 178 5.790 141.169 25.941 1.00 28.67 C ANISOU 4449 CA LEU C 178 3645 4533 2715 -565 -47 -280 C ATOM 4450 C LEU C 178 5.701 142.613 25.474 1.00 28.85 C ANISOU 4450 C LEU C 178 3633 4611 2716 -581 -53 -201 C ATOM 4451 O LEU C 178 6.390 143.508 25.985 1.00 28.00 O ANISOU 4451 O LEU C 178 3493 4495 2651 -582 -37 -143 O ATOM 4452 CB LEU C 178 4.474 140.695 26.579 1.00 28.76 C ANISOU 4452 CB LEU C 178 3668 4489 2771 -602 -93 -299 C ATOM 4453 CG LEU C 178 3.764 141.381 27.757 1.00 28.52 C ANISOU 4453 CG LEU C 178 3607 4422 2808 -616 -106 -246 C ATOM 4454 CD1 LEU C 178 3.262 142.780 27.430 1.00 29.00 C ANISOU 4454 CD1 LEU C 178 3635 4525 2860 -621 -122 -181 C ATOM 4455 CD2 LEU C 178 2.585 140.497 28.183 1.00 29.11 C ANISOU 4455 CD2 LEU C 178 3684 4455 2922 -651 -130 -268 C ATOM 4456 N SER C 179 4.844 142.824 24.493 1.00 29.62 N ANISOU 4456 N SER C 179 3745 4759 2751 -599 -86 -196 N ATOM 4457 CA SER C 179 4.588 144.144 23.951 1.00 30.80 C ANISOU 4457 CA SER C 179 3872 4953 2876 -609 -100 -110 C ATOM 4458 C SER C 179 3.107 144.393 23.922 1.00 30.63 C ANISOU 4458 C SER C 179 3839 4931 2867 -628 -167 -94 C ATOM 4459 O SER C 179 2.319 143.452 23.828 1.00 30.88 O ANISOU 4459 O SER C 179 3881 4960 2893 -649 -207 -153 O ATOM 4460 CB SER C 179 5.110 144.231 22.526 1.00 32.28 C ANISOU 4460 CB SER C 179 4083 5234 2950 -595 -73 -96 C ATOM 4461 OG SER C 179 6.513 144.244 22.509 1.00 33.95 O ANISOU 4461 OG SER C 179 4275 5463 3162 -572 3 -80 O ATOM 4462 N SER C 180 2.741 145.668 23.983 1.00 30.46 N ANISOU 4462 N SER C 180 3793 4909 2872 -622 -180 -9 N ATOM 4463 CA SER C 180 1.367 146.096 23.789 1.00 31.25 C ANISOU 4463 CA SER C 180 3863 5026 2983 -622 -240 29 C ATOM 4464 C SER C 180 1.407 147.288 22.847 1.00 32.71 C ANISOU 4464 C SER C 180 4052 5258 3119 -607 -254 124 C ATOM 4465 O SER C 180 2.293 148.135 22.972 1.00 32.30 O ANISOU 4465 O SER C 180 4011 5176 3084 -601 -211 177 O ATOM 4466 CB SER C 180 0.736 146.470 25.130 1.00 30.42 C ANISOU 4466 CB SER C 180 3727 4847 2983 -603 -231 44 C ATOM 4467 OG SER C 180 -0.592 146.933 24.955 1.00 30.93 O ANISOU 4467 OG SER C 180 3743 4937 3072 -587 -277 94 O ATOM 4468 N VAL C 181 0.463 147.345 21.909 1.00 34.20 N ANISOU 4468 N VAL C 181 4228 5517 3249 -607 -320 152 N ATOM 4469 CA VAL C 181 0.459 148.365 20.868 1.00 36.27 C ANISOU 4469 CA VAL C 181 4503 5834 3442 -589 -341 253 C ATOM 4470 C VAL C 181 -0.917 148.960 20.724 1.00 37.51 C ANISOU 4470 C VAL C 181 4610 6010 3631 -563 -419 321 C ATOM 4471 O VAL C 181 -1.913 148.278 20.960 1.00 37.31 O ANISOU 4471 O VAL C 181 4536 6002 3638 -576 -473 277 O ATOM 4472 CB VAL C 181 0.880 147.769 19.508 1.00 37.72 C ANISOU 4472 CB VAL C 181 4740 6123 3469 -603 -351 227 C ATOM 4473 CG1 VAL C 181 -0.199 146.887 18.886 1.00 38.35 C ANISOU 4473 CG1 VAL C 181 4820 6267 3484 -626 -451 166 C ATOM 4474 CG2 VAL C 181 1.352 148.843 18.525 1.00 39.20 C ANISOU 4474 CG2 VAL C 181 4956 6363 3573 -585 -331 347 C ATOM 4475 N VAL C 182 -0.951 150.221 20.311 1.00 38.78 N ANISOU 4475 N VAL C 182 4778 6166 3789 -527 -425 437 N ATOM 4476 CA VAL C 182 -2.184 150.888 19.957 1.00 40.74 C ANISOU 4476 CA VAL C 182 4978 6444 4055 -483 -502 524 C ATOM 4477 C VAL C 182 -1.987 151.612 18.627 1.00 42.62 C ANISOU 4477 C VAL C 182 5259 6754 4179 -470 -535 632 C ATOM 4478 O VAL C 182 -0.956 152.250 18.404 1.00 42.17 O ANISOU 4478 O VAL C 182 5258 6666 4098 -475 -470 688 O ATOM 4479 CB VAL C 182 -2.676 151.825 21.086 1.00 40.76 C ANISOU 4479 CB VAL C 182 4946 6338 4202 -421 -473 570 C ATOM 4480 CG1 VAL C 182 -1.699 152.964 21.358 1.00 41.06 C ANISOU 4480 CG1 VAL C 182 5051 6273 4276 -407 -410 629 C ATOM 4481 CG2 VAL C 182 -4.070 152.354 20.778 1.00 42.11 C ANISOU 4481 CG2 VAL C 182 5043 6550 4409 -358 -549 656 C ATOM 4482 N THR C 183 -2.964 151.459 17.735 1.00 44.74 N ANISOU 4482 N THR C 183 5500 7124 4374 -460 -640 667 N ATOM 4483 CA THR C 183 -3.001 152.174 16.466 1.00 46.62 C ANISOU 4483 CA THR C 183 5780 7443 4492 -435 -690 788 C ATOM 4484 C THR C 183 -3.940 153.353 16.652 1.00 48.61 C ANISOU 4484 C THR C 183 5976 7652 4844 -358 -737 919 C ATOM 4485 O THR C 183 -5.127 153.162 16.915 1.00 49.45 O ANISOU 4485 O THR C 183 5989 7784 5018 -330 -813 916 O ATOM 4486 CB THR C 183 -3.505 151.267 15.329 1.00 47.71 C ANISOU 4486 CB THR C 183 5933 7726 4468 -468 -798 742 C ATOM 4487 OG1 THR C 183 -2.667 150.111 15.239 1.00 47.02 O ANISOU 4487 OG1 THR C 183 5908 7658 4298 -524 -747 603 O ATOM 4488 CG2 THR C 183 -3.499 152.000 13.987 1.00 48.69 C ANISOU 4488 CG2 THR C 183 6116 7947 4437 -437 -850 874 C ATOM 4489 N VAL C 184 -3.403 154.563 16.512 1.00 50.68 N ANISOU 4489 N VAL C 184 6289 7843 5124 -321 -688 1041 N ATOM 4490 CA VAL C 184 -4.159 155.803 16.739 1.00 52.88 C ANISOU 4490 CA VAL C 184 6538 8044 5509 -230 -717 1170 C ATOM 4491 C VAL C 184 -4.089 156.696 15.498 1.00 55.99 C ANISOU 4491 C VAL C 184 6988 8486 5799 -200 -760 1338 C ATOM 4492 O VAL C 184 -3.247 156.463 14.630 1.00 56.82 O ANISOU 4492 O VAL C 184 7165 8667 5758 -254 -736 1354 O ATOM 4493 CB VAL C 184 -3.637 156.569 17.981 1.00 51.71 C ANISOU 4493 CB VAL C 184 6418 7711 5517 -208 -618 1159 C ATOM 4494 CG1 VAL C 184 -3.688 155.674 19.207 1.00 50.26 C ANISOU 4494 CG1 VAL C 184 6191 7492 5413 -233 -574 1003 C ATOM 4495 CG2 VAL C 184 -2.219 157.105 17.776 1.00 51.60 C ANISOU 4495 CG2 VAL C 184 6500 7631 5475 -265 -540 1202 C ATOM 4496 N PRO C 185 -4.969 157.717 15.404 1.00 59.05 N ANISOU 4496 N PRO C 185 7346 8833 6258 -103 -818 1473 N ATOM 4497 CA PRO C 185 -4.826 158.688 14.309 1.00 61.67 C ANISOU 4497 CA PRO C 185 7745 9184 6503 -68 -851 1657 C ATOM 4498 C PRO C 185 -3.566 159.536 14.484 1.00 62.60 C ANISOU 4498 C PRO C 185 7963 9162 6659 -105 -737 1720 C ATOM 4499 O PRO C 185 -3.317 160.033 15.589 1.00 62.20 O ANISOU 4499 O PRO C 185 7922 8942 6769 -94 -672 1682 O ATOM 4500 CB PRO C 185 -6.084 159.567 14.437 1.00 63.01 C ANISOU 4500 CB PRO C 185 7848 9309 6785 61 -930 1775 C ATOM 4501 CG PRO C 185 -7.021 158.807 15.314 1.00 61.98 C ANISOU 4501 CG PRO C 185 7591 9203 6755 83 -957 1650 C ATOM 4502 CD PRO C 185 -6.154 158.005 16.234 1.00 59.50 C ANISOU 4502 CD PRO C 185 7302 8833 6470 -9 -851 1475 C ATOM 4503 N SER C 186 -2.795 159.720 13.410 1.00 64.54 N ANISOU 4503 N SER C 186 8285 9480 6759 -151 -715 1820 N ATOM 4504 CA SER C 186 -1.506 160.413 13.510 1.00 65.51 C ANISOU 4504 CA SER C 186 8483 9489 6919 -213 -603 1888 C ATOM 4505 C SER C 186 -1.627 161.906 13.864 1.00 67.21 C ANISOU 4505 C SER C 186 8742 9504 7289 -159 -599 2036 C ATOM 4506 O SER C 186 -0.618 162.536 14.190 1.00 68.55 O ANISOU 4506 O SER C 186 8967 9541 7539 -224 -518 2078 O ATOM 4507 CB SER C 186 -0.689 160.226 12.226 1.00 66.61 C ANISOU 4507 CB SER C 186 8682 9773 6855 -268 -564 1976 C ATOM 4508 OG SER C 186 -1.324 160.825 11.115 1.00 68.57 O ANISOU 4508 OG SER C 186 8967 10098 6989 -205 -645 2152 O ATOM 4509 N SER C 187 -2.843 162.461 13.796 1.00 68.68 N ANISOU 4509 N SER C 187 8903 9666 7527 -41 -690 2115 N ATOM 4510 CA SER C 187 -3.119 163.826 14.255 1.00 69.63 C ANISOU 4510 CA SER C 187 9071 9574 7813 40 -689 2232 C ATOM 4511 C SER C 187 -3.547 163.829 15.721 1.00 68.55 C ANISOU 4511 C SER C 187 8898 9293 7855 92 -666 2084 C ATOM 4512 O SER C 187 -3.704 164.891 16.329 1.00 69.33 O ANISOU 4512 O SER C 187 9053 9187 8101 162 -651 2134 O ATOM 4513 CB SER C 187 -4.199 164.476 13.383 1.00 71.45 C ANISOU 4513 CB SER C 187 9291 9851 8005 165 -794 2412 C ATOM 4514 OG SER C 187 -5.467 163.871 13.569 1.00 71.23 O ANISOU 4514 OG SER C 187 9146 9932 7986 253 -882 2339 O ATOM 4515 N GLY C 190 0.150 164.306 18.926 1.00 63.92 N ANISOU 4515 N GLY C 190 8496 8205 7585 -236 -421 1768 N ATOM 4516 CA GLY C 190 0.608 165.604 19.467 1.00 65.40 C ANISOU 4516 CA GLY C 190 8794 8134 7919 -254 -416 1825 C ATOM 4517 C GLY C 190 -0.405 166.436 20.257 1.00 66.39 C ANISOU 4517 C GLY C 190 8983 8073 8167 -105 -445 1802 C ATOM 4518 O GLY C 190 -0.134 167.598 20.571 1.00 68.03 O ANISOU 4518 O GLY C 190 9308 8049 8493 -105 -452 1860 O ATOM 4519 N THR C 191 -1.559 165.852 20.586 1.00 66.16 N ANISOU 4519 N THR C 191 8880 8141 8117 22 -458 1720 N ATOM 4520 CA THR C 191 -2.566 166.487 21.453 1.00 66.87 C ANISOU 4520 CA THR C 191 9009 8082 8317 186 -460 1677 C ATOM 4521 C THR C 191 -3.046 165.503 22.531 1.00 64.98 C ANISOU 4521 C THR C 191 8698 7920 8071 227 -426 1486 C ATOM 4522 O THR C 191 -2.979 165.806 23.727 1.00 66.01 O ANISOU 4522 O THR C 191 8906 7896 8278 262 -392 1368 O ATOM 4523 CB THR C 191 -3.757 167.037 20.638 1.00 68.94 C ANISOU 4523 CB THR C 191 9234 8378 8583 344 -508 1836 C ATOM 4524 OG1 THR C 191 -4.307 166.008 19.808 1.00 68.69 O ANISOU 4524 OG1 THR C 191 9061 8615 8424 342 -545 1858 O ATOM 4525 CG2 THR C 191 -3.307 168.195 19.756 1.00 70.69 C ANISOU 4525 CG2 THR C 191 9559 8471 8831 321 -535 2035 C ATOM 4526 N GLN C 192 -3.525 164.332 22.106 1.00 62.63 N ANISOU 4526 N GLN C 192 8264 7857 7676 219 -438 1457 N ATOM 4527 CA GLN C 192 -3.789 163.210 23.024 1.00 59.91 C ANISOU 4527 CA GLN C 192 7844 7604 7313 215 -402 1289 C ATOM 4528 C GLN C 192 -2.517 162.638 23.660 1.00 56.21 C ANISOU 4528 C GLN C 192 7421 7113 6823 68 -367 1165 C ATOM 4529 O GLN C 192 -1.453 162.607 23.032 1.00 55.97 O ANISOU 4529 O GLN C 192 7415 7103 6749 -58 -374 1210 O ATOM 4530 CB GLN C 192 -4.514 162.074 22.287 1.00 60.27 C ANISOU 4530 CB GLN C 192 7741 7893 7265 212 -440 1298 C ATOM 4531 CG GLN C 192 -5.945 162.387 21.881 1.00 62.84 C ANISOU 4531 CG GLN C 192 7976 8279 7622 362 -486 1397 C ATOM 4532 CD GLN C 192 -6.847 162.619 23.081 1.00 63.76 C ANISOU 4532 CD GLN C 192 8066 8313 7846 505 -431 1330 C ATOM 4533 OE1 GLN C 192 -6.899 161.797 23.993 1.00 63.65 O ANISOU 4533 OE1 GLN C 192 8014 8338 7834 482 -379 1197 O ATOM 4534 NE2 GLN C 192 -7.555 163.744 23.089 1.00 66.12 N ANISOU 4534 NE2 GLN C 192 8392 8498 8234 663 -433 1427 N ATOM 4535 N THR C 193 -2.642 162.191 24.910 1.00 52.41 N ANISOU 4535 N THR C 193 6946 6597 6370 93 -325 1019 N ATOM 4536 CA THR C 193 -1.580 161.444 25.584 1.00 49.57 C ANISOU 4536 CA THR C 193 6606 6247 5981 -30 -302 895 C ATOM 4537 C THR C 193 -1.954 159.969 25.614 1.00 47.03 C ANISOU 4537 C THR C 193 6165 6118 5586 -50 -288 819 C ATOM 4538 O THR C 193 -3.112 159.623 25.819 1.00 45.95 O ANISOU 4538 O THR C 193 5954 6049 5458 46 -278 807 O ATOM 4539 CB THR C 193 -1.349 161.921 27.028 1.00 49.27 C ANISOU 4539 CB THR C 193 6680 6033 6007 1 -275 780 C ATOM 4540 OG1 THR C 193 -2.540 161.730 27.797 1.00 49.14 O ANISOU 4540 OG1 THR C 193 6634 6031 6006 144 -232 721 O ATOM 4541 CG2 THR C 193 -0.943 163.384 27.057 1.00 50.67 C ANISOU 4541 CG2 THR C 193 6997 5987 6268 7 -300 840 C ATOM 4542 N TYR C 194 -0.955 159.115 25.424 1.00 45.28 N ANISOU 4542 N TYR C 194 5924 5978 5304 -175 -286 772 N ATOM 4543 CA TYR C 194 -1.136 157.673 25.392 1.00 43.00 C ANISOU 4543 CA TYR C 194 5543 5848 4948 -209 -277 697 C ATOM 4544 C TYR C 194 -0.208 157.053 26.441 1.00 41.01 C ANISOU 4544 C TYR C 194 5324 5559 4698 -277 -246 577 C ATOM 4545 O TYR C 194 1.024 157.097 26.310 1.00 40.79 O ANISOU 4545 O TYR C 194 5328 5509 4662 -371 -248 577 O ATOM 4546 CB TYR C 194 -0.851 157.156 23.987 1.00 43.66 C ANISOU 4546 CB TYR C 194 5577 6075 4939 -274 -307 762 C ATOM 4547 CG TYR C 194 -1.812 157.741 22.969 1.00 45.16 C ANISOU 4547 CG TYR C 194 5736 6313 5111 -203 -355 886 C ATOM 4548 CD1 TYR C 194 -3.157 157.373 22.969 1.00 45.62 C ANISOU 4548 CD1 TYR C 194 5708 6449 5178 -123 -386 886 C ATOM 4549 CD2 TYR C 194 -1.387 158.676 22.020 1.00 46.51 C ANISOU 4549 CD2 TYR C 194 5956 6454 5262 -217 -375 1018 C ATOM 4550 CE1 TYR C 194 -4.056 157.909 22.052 1.00 47.21 C ANISOU 4550 CE1 TYR C 194 5868 6703 5368 -52 -446 1008 C ATOM 4551 CE2 TYR C 194 -2.279 159.213 21.098 1.00 47.63 C ANISOU 4551 CE2 TYR C 194 6074 6642 5381 -143 -429 1143 C ATOM 4552 CZ TYR C 194 -3.610 158.826 21.117 1.00 48.05 C ANISOU 4552 CZ TYR C 194 6037 6778 5442 -58 -471 1135 C ATOM 4553 OH TYR C 194 -4.508 159.342 20.213 1.00 49.57 O ANISOU 4553 OH TYR C 194 6192 7028 5615 20 -540 1266 O ATOM 4554 N THR C 195 -0.814 156.479 27.478 1.00 38.75 N ANISOU 4554 N THR C 195 5021 5276 4425 -227 -216 488 N ATOM 4555 CA THR C 195 -0.098 155.979 28.642 1.00 37.77 C ANISOU 4555 CA THR C 195 4943 5108 4300 -267 -192 381 C ATOM 4556 C THR C 195 -0.423 154.511 28.812 1.00 36.66 C ANISOU 4556 C THR C 195 4722 5091 4116 -285 -172 321 C ATOM 4557 O THR C 195 -1.599 154.149 28.941 1.00 36.02 O ANISOU 4557 O THR C 195 4578 5064 4043 -221 -153 324 O ATOM 4558 CB THR C 195 -0.499 156.758 29.909 1.00 37.91 C ANISOU 4558 CB THR C 195 5052 4989 4365 -178 -165 331 C ATOM 4559 OG1 THR C 195 -0.286 158.152 29.686 1.00 38.62 O ANISOU 4559 OG1 THR C 195 5229 4940 4506 -158 -192 388 O ATOM 4560 CG2 THR C 195 0.329 156.325 31.133 1.00 37.21 C ANISOU 4560 CG2 THR C 195 5029 4853 4256 -223 -157 223 C ATOM 4561 N CYS C 196 0.608 153.661 28.796 1.00 36.06 N ANISOU 4561 N CYS C 196 4641 5057 4004 -372 -175 274 N ATOM 4562 CA CYS C 196 0.405 152.242 29.093 1.00 35.41 C ANISOU 4562 CA CYS C 196 4507 5059 3890 -391 -156 210 C ATOM 4563 C CYS C 196 0.524 152.017 30.597 1.00 34.16 C ANISOU 4563 C CYS C 196 4399 4835 3744 -367 -124 136 C ATOM 4564 O CYS C 196 1.464 152.494 31.250 1.00 34.29 O ANISOU 4564 O CYS C 196 4491 4771 3768 -390 -137 106 O ATOM 4565 CB CYS C 196 1.359 151.335 28.307 1.00 35.87 C ANISOU 4565 CB CYS C 196 4537 5195 3898 -471 -168 196 C ATOM 4566 SG CYS C 196 3.083 151.371 28.802 1.00 37.72 S ANISOU 4566 SG CYS C 196 4814 5378 4140 -536 -167 164 S ATOM 4567 N ASN C 197 -0.444 151.287 31.137 1.00 33.23 N ANISOU 4567 N ASN C 197 4240 4758 3626 -327 -88 114 N ATOM 4568 CA ASN C 197 -0.496 150.979 32.560 1.00 32.32 C ANISOU 4568 CA ASN C 197 4176 4601 3504 -293 -45 57 C ATOM 4569 C ASN C 197 -0.168 149.506 32.672 1.00 30.35 C ANISOU 4569 C ASN C 197 3889 4414 3229 -353 -41 22 C ATOM 4570 O ASN C 197 -0.939 148.666 32.216 1.00 29.67 O ANISOU 4570 O ASN C 197 3723 4399 3151 -367 -33 38 O ATOM 4571 CB ASN C 197 -1.881 151.291 33.140 1.00 32.89 C ANISOU 4571 CB ASN C 197 4224 4673 3599 -192 15 78 C ATOM 4572 CG ASN C 197 -2.527 152.505 32.494 1.00 34.02 C ANISOU 4572 CG ASN C 197 4355 4788 3782 -124 4 140 C ATOM 4573 OD1 ASN C 197 -3.439 152.378 31.668 1.00 33.64 O ANISOU 4573 OD1 ASN C 197 4203 4817 3761 -107 -6 201 O ATOM 4574 ND2 ASN C 197 -2.043 153.687 32.845 1.00 34.69 N ANISOU 4574 ND2 ASN C 197 4550 4756 3876 -87 -5 126 N ATOM 4575 N VAL C 198 0.991 149.206 33.246 1.00 29.57 N ANISOU 4575 N VAL C 198 3848 4282 3107 -391 -56 -22 N ATOM 4576 CA VAL C 198 1.489 147.841 33.351 1.00 28.89 C ANISOU 4576 CA VAL C 198 3739 4235 3003 -437 -56 -52 C ATOM 4577 C VAL C 198 1.325 147.394 34.785 1.00 28.82 C ANISOU 4577 C VAL C 198 3781 4197 2971 -402 -19 -80 C ATOM 4578 O VAL C 198 1.743 148.084 35.701 1.00 28.86 O ANISOU 4578 O VAL C 198 3869 4143 2953 -373 -27 -105 O ATOM 4579 CB VAL C 198 2.967 147.756 32.927 1.00 28.66 C ANISOU 4579 CB VAL C 198 3719 4205 2966 -492 -98 -65 C ATOM 4580 CG1 VAL C 198 3.526 146.348 33.109 1.00 28.21 C ANISOU 4580 CG1 VAL C 198 3647 4176 2896 -516 -94 -96 C ATOM 4581 CG2 VAL C 198 3.094 148.204 31.481 1.00 28.82 C ANISOU 4581 CG2 VAL C 198 3694 4266 2989 -520 -117 -24 C ATOM 4582 N ASP C 199 0.735 146.222 34.961 1.00 28.43 N ANISOU 4582 N ASP C 199 3691 4186 2925 -411 15 -75 N ATOM 4583 CA ASP C 199 0.477 145.662 36.270 1.00 28.31 C ANISOU 4583 CA ASP C 199 3720 4155 2883 -380 63 -81 C ATOM 4584 C ASP C 199 1.156 144.302 36.339 1.00 26.64 C ANISOU 4584 C ASP C 199 3507 3948 2668 -428 47 -93 C ATOM 4585 O ASP C 199 0.818 143.409 35.567 1.00 25.96 O ANISOU 4585 O ASP C 199 3359 3889 2614 -471 44 -85 O ATOM 4586 CB ASP C 199 -1.039 145.542 36.455 1.00 29.97 C ANISOU 4586 CB ASP C 199 3868 4401 3119 -344 134 -37 C ATOM 4587 CG ASP C 199 -1.427 145.011 37.812 1.00 31.54 C ANISOU 4587 CG ASP C 199 4108 4594 3281 -305 207 -23 C ATOM 4588 OD1 ASP C 199 -0.777 145.381 38.819 1.00 33.48 O ANISOU 4588 OD1 ASP C 199 4462 4799 3460 -265 209 -55 O ATOM 4589 OD2 ASP C 199 -2.401 144.238 37.872 1.00 32.93 O ANISOU 4589 OD2 ASP C 199 4209 4810 3494 -320 261 25 O ATOM 4590 N HIS C 200 2.130 144.156 37.240 1.00 25.36 N ANISOU 4590 N HIS C 200 3418 3754 2466 -417 26 -115 N ATOM 4591 CA HIS C 200 2.783 142.874 37.487 1.00 24.75 C ANISOU 4591 CA HIS C 200 3348 3670 2386 -439 13 -116 C ATOM 4592 C HIS C 200 2.620 142.515 38.966 1.00 24.35 C ANISOU 4592 C HIS C 200 3371 3599 2281 -399 48 -98 C ATOM 4593 O HIS C 200 3.468 142.835 39.806 1.00 24.05 O ANISOU 4593 O HIS C 200 3408 3542 2190 -375 7 -115 O ATOM 4594 CB HIS C 200 4.258 142.915 37.092 1.00 24.39 C ANISOU 4594 CB HIS C 200 3302 3620 2345 -459 -54 -141 C ATOM 4595 CG HIS C 200 4.951 141.586 37.199 1.00 24.42 C ANISOU 4595 CG HIS C 200 3304 3615 2359 -463 -64 -140 C ATOM 4596 ND1 HIS C 200 5.974 141.362 38.088 1.00 24.83 N ANISOU 4596 ND1 HIS C 200 3397 3651 2386 -440 -106 -137 N ATOM 4597 CD2 HIS C 200 4.757 140.414 36.550 1.00 24.47 C ANISOU 4597 CD2 HIS C 200 3280 3617 2400 -481 -45 -142 C ATOM 4598 CE1 HIS C 200 6.393 140.116 37.973 1.00 25.03 C ANISOU 4598 CE1 HIS C 200 3412 3664 2436 -433 -104 -128 C ATOM 4599 NE2 HIS C 200 5.668 139.517 37.049 1.00 24.75 N ANISOU 4599 NE2 HIS C 200 3341 3626 2436 -458 -64 -137 N ATOM 4600 N LYS C 201 1.515 141.847 39.262 1.00 24.45 N ANISOU 4600 N LYS C 201 3361 3623 2305 -396 120 -56 N ATOM 4601 CA LYS C 201 1.147 141.487 40.632 1.00 25.12 C ANISOU 4601 CA LYS C 201 3512 3702 2329 -354 179 -18 C ATOM 4602 C LYS C 201 2.170 140.617 41.374 1.00 25.05 C ANISOU 4602 C LYS C 201 3573 3665 2280 -350 140 -9 C ATOM 4603 O LYS C 201 2.413 140.856 42.542 1.00 25.23 O ANISOU 4603 O LYS C 201 3688 3685 2212 -301 144 -3 O ATOM 4604 CB LYS C 201 -0.219 140.800 40.665 1.00 25.78 C ANISOU 4604 CB LYS C 201 3529 3809 2458 -372 269 47 C ATOM 4605 CG LYS C 201 -1.367 141.733 40.347 1.00 26.05 C ANISOU 4605 CG LYS C 201 3496 3885 2517 -344 323 59 C ATOM 4606 CD LYS C 201 -2.676 140.975 40.224 1.00 26.82 C ANISOU 4606 CD LYS C 201 3488 4016 2685 -382 396 135 C ATOM 4607 CE LYS C 201 -3.732 141.889 39.605 1.00 27.09 C ANISOU 4607 CE LYS C 201 3422 4102 2768 -357 423 150 C ATOM 4608 NZ LYS C 201 -4.987 141.135 39.408 1.00 28.02 N ANISOU 4608 NZ LYS C 201 3409 4264 2974 -411 475 230 N ATOM 4609 N PRO C 202 2.766 139.607 40.706 1.00 24.98 N ANISOU 4609 N PRO C 202 3527 3633 2330 -392 100 -9 N ATOM 4610 CA PRO C 202 3.736 138.750 41.412 1.00 25.44 C ANISOU 4610 CA PRO C 202 3645 3662 2361 -372 61 11 C ATOM 4611 C PRO C 202 4.897 139.508 42.074 1.00 25.71 C ANISOU 4611 C PRO C 202 3738 3705 2325 -335 -19 -18 C ATOM 4612 O PRO C 202 5.302 139.141 43.169 1.00 27.00 O ANISOU 4612 O PRO C 202 3978 3862 2419 -298 -39 14 O ATOM 4613 CB PRO C 202 4.231 137.821 40.303 1.00 25.18 C ANISOU 4613 CB PRO C 202 3555 3600 2413 -407 31 -6 C ATOM 4614 CG PRO C 202 3.057 137.707 39.394 1.00 24.95 C ANISOU 4614 CG PRO C 202 3461 3577 2443 -460 77 -10 C ATOM 4615 CD PRO C 202 2.514 139.103 39.344 1.00 24.60 C ANISOU 4615 CD PRO C 202 3396 3583 2369 -448 91 -26 C ATOM 4616 N SER C 203 5.389 140.577 41.441 1.00 26.00 N ANISOU 4616 N SER C 203 3744 3758 2378 -350 -70 -71 N ATOM 4617 CA SER C 203 6.410 141.445 42.055 1.00 26.47 C ANISOU 4617 CA SER C 203 3854 3819 2384 -338 -160 -101 C ATOM 4618 C SER C 203 5.841 142.690 42.762 1.00 27.33 C ANISOU 4618 C SER C 203 4049 3921 2416 -313 -149 -133 C ATOM 4619 O SER C 203 6.614 143.550 43.176 1.00 27.49 O ANISOU 4619 O SER C 203 4121 3928 2398 -318 -236 -173 O ATOM 4620 CB SER C 203 7.423 141.898 41.002 1.00 25.99 C ANISOU 4620 CB SER C 203 3710 3770 2394 -379 -227 -128 C ATOM 4621 OG SER C 203 6.848 142.864 40.121 1.00 25.20 O ANISOU 4621 OG SER C 203 3575 3673 2327 -406 -199 -153 O ATOM 4622 N ASN C 204 4.519 142.770 42.916 1.00 28.18 N ANISOU 4622 N ASN C 204 4169 4033 2504 -284 -45 -117 N ATOM 4623 CA ASN C 204 3.823 143.942 43.470 1.00 29.52 C ANISOU 4623 CA ASN C 204 4416 4193 2608 -236 -7 -150 C ATOM 4624 C ASN C 204 4.183 145.254 42.786 1.00 29.61 C ANISOU 4624 C ASN C 204 4419 4172 2660 -259 -68 -205 C ATOM 4625 O ASN C 204 4.400 146.269 43.459 1.00 30.00 O ANISOU 4625 O ASN C 204 4575 4181 2642 -232 -110 -257 O ATOM 4626 CB ASN C 204 4.075 144.061 44.979 1.00 30.95 C ANISOU 4626 CB ASN C 204 4744 4368 2648 -180 -25 -163 C ATOM 4627 CG ASN C 204 3.703 142.808 45.739 1.00 31.89 C ANISOU 4627 CG ASN C 204 4884 4516 2717 -153 44 -89 C ATOM 4628 OD1 ASN C 204 2.651 142.225 45.519 1.00 32.00 O ANISOU 4628 OD1 ASN C 204 4836 4551 2773 -149 156 -32 O ATOM 4629 ND2 ASN C 204 4.560 142.410 46.669 1.00 32.90 N ANISOU 4629 ND2 ASN C 204 5100 4645 2756 -137 -30 -80 N ATOM 4630 N THR C 205 4.259 145.219 41.453 1.00 29.64 N ANISOU 4630 N THR C 205 4309 4187 2765 -311 -77 -193 N ATOM 4631 CA THR C 205 4.730 146.344 40.659 1.00 29.76 C ANISOU 4631 CA THR C 205 4304 4175 2830 -347 -136 -221 C ATOM 4632 C THR C 205 3.633 146.860 39.724 1.00 29.93 C ANISOU 4632 C THR C 205 4264 4203 2905 -334 -70 -203 C ATOM 4633 O THR C 205 2.946 146.073 39.056 1.00 28.97 O ANISOU 4633 O THR C 205 4055 4128 2823 -343 -17 -167 O ATOM 4634 CB THR C 205 5.964 145.949 39.801 1.00 29.62 C ANISOU 4634 CB THR C 205 4200 4177 2876 -416 -208 -210 C ATOM 4635 OG1 THR C 205 7.003 145.433 40.643 1.00 30.63 O ANISOU 4635 OG1 THR C 205 4362 4307 2968 -421 -278 -215 O ATOM 4636 CG2 THR C 205 6.512 147.146 39.054 1.00 29.78 C ANISOU 4636 CG2 THR C 205 4199 4169 2946 -462 -263 -220 C ATOM 4637 N LYS C 206 3.499 148.182 39.674 1.00 30.69 N ANISOU 4637 N LYS C 206 4410 4246 3003 -314 -87 -228 N ATOM 4638 CA LYS C 206 2.708 148.874 38.658 1.00 31.39 C ANISOU 4638 CA LYS C 206 4441 4335 3152 -302 -53 -201 C ATOM 4639 C LYS C 206 3.563 149.974 38.038 1.00 31.15 C ANISOU 4639 C LYS C 206 4426 4246 3162 -352 -133 -210 C ATOM 4640 O LYS C 206 4.241 150.711 38.765 1.00 31.12 O ANISOU 4640 O LYS C 206 4522 4169 3132 -360 -194 -254 O ATOM 4641 CB LYS C 206 1.453 149.501 39.268 1.00 33.32 C ANISOU 4641 CB LYS C 206 4736 4557 3368 -202 29 -205 C ATOM 4642 CG LYS C 206 0.430 148.498 39.765 1.00 34.79 C ANISOU 4642 CG LYS C 206 4877 4811 3531 -158 127 -170 C ATOM 4643 CD LYS C 206 -0.604 149.164 40.669 1.00 37.39 C ANISOU 4643 CD LYS C 206 5272 5122 3812 -41 221 -178 C ATOM 4644 CE LYS C 206 -1.491 148.145 41.366 1.00 38.89 C ANISOU 4644 CE LYS C 206 5421 5383 3971 -5 329 -130 C ATOM 4645 NZ LYS C 206 -2.491 147.554 40.432 1.00 39.49 N ANISOU 4645 NZ LYS C 206 5330 5532 4144 -33 373 -56 N ATOM 4646 N VAL C 207 3.561 150.057 36.708 1.00 30.52 N ANISOU 4646 N VAL C 207 4253 4199 3143 -392 -137 -164 N ATOM 4647 CA VAL C 207 4.296 151.089 35.976 1.00 31.03 C ANISOU 4647 CA VAL C 207 4320 4217 3254 -446 -196 -145 C ATOM 4648 C VAL C 207 3.327 151.786 35.017 1.00 31.84 C ANISOU 4648 C VAL C 207 4388 4318 3393 -410 -161 -95 C ATOM 4649 O VAL C 207 2.625 151.113 34.257 1.00 30.50 O ANISOU 4649 O VAL C 207 4130 4231 3227 -400 -123 -60 O ATOM 4650 CB VAL C 207 5.480 150.500 35.165 1.00 30.41 C ANISOU 4650 CB VAL C 207 4155 4197 3202 -531 -234 -118 C ATOM 4651 CG1 VAL C 207 6.258 151.599 34.435 1.00 31.20 C ANISOU 4651 CG1 VAL C 207 4247 4254 3356 -595 -283 -77 C ATOM 4652 CG2 VAL C 207 6.426 149.710 36.063 1.00 30.25 C ANISOU 4652 CG2 VAL C 207 4148 4190 3157 -553 -273 -153 C ATOM 4653 N ASP C 208 3.288 153.119 35.064 1.00 32.98 N ANISOU 4653 N ASP C 208 4605 4362 3564 -392 -186 -90 N ATOM 4654 CA ASP C 208 2.639 153.930 34.029 1.00 34.33 C ANISOU 4654 CA ASP C 208 4746 4519 3779 -366 -174 -23 C ATOM 4655 C ASP C 208 3.714 154.595 33.187 1.00 34.88 C ANISOU 4655 C ASP C 208 4808 4553 3892 -459 -233 27 C ATOM 4656 O ASP C 208 4.611 155.258 33.726 1.00 34.98 O ANISOU 4656 O ASP C 208 4895 4469 3926 -512 -290 1 O ATOM 4657 CB ASP C 208 1.742 155.013 34.626 1.00 35.90 C ANISOU 4657 CB ASP C 208 5039 4613 3988 -261 -147 -38 C ATOM 4658 CG ASP C 208 0.634 154.450 35.487 1.00 37.09 C ANISOU 4658 CG ASP C 208 5188 4807 4098 -158 -67 -72 C ATOM 4659 OD1 ASP C 208 0.084 153.379 35.144 1.00 37.14 O ANISOU 4659 OD1 ASP C 208 5083 4931 4096 -162 -28 -44 O ATOM 4660 OD2 ASP C 208 0.322 155.075 36.523 1.00 39.55 O ANISOU 4660 OD2 ASP C 208 5614 5032 4383 -75 -40 -127 O ATOM 4661 N LYS C 209 3.628 154.407 31.871 1.00 35.05 N ANISOU 4661 N LYS C 209 4739 4656 3921 -485 -221 102 N ATOM 4662 CA LYS C 209 4.590 154.966 30.926 1.00 35.98 C ANISOU 4662 CA LYS C 209 4834 4767 4071 -570 -254 174 C ATOM 4663 C LYS C 209 3.848 155.717 29.824 1.00 36.84 C ANISOU 4663 C LYS C 209 4929 4876 4193 -535 -243 267 C ATOM 4664 O LYS C 209 3.167 155.097 29.008 1.00 35.93 O ANISOU 4664 O LYS C 209 4743 4872 4038 -506 -219 297 O ATOM 4665 CB LYS C 209 5.430 153.833 30.322 1.00 36.02 C ANISOU 4665 CB LYS C 209 4745 4898 4045 -634 -242 179 C ATOM 4666 CG LYS C 209 6.566 154.279 29.425 1.00 37.06 C ANISOU 4666 CG LYS C 209 4833 5044 4202 -721 -254 259 C ATOM 4667 CD LYS C 209 7.605 155.026 30.233 1.00 38.05 C ANISOU 4667 CD LYS C 209 5002 5062 4394 -794 -312 249 C ATOM 4668 CE LYS C 209 8.940 155.023 29.536 1.00 39.33 C ANISOU 4668 CE LYS C 209 5077 5278 4588 -893 -313 322 C ATOM 4669 NZ LYS C 209 9.927 155.854 30.272 1.00 40.88 N ANISOU 4669 NZ LYS C 209 5302 5363 4867 -986 -390 325 N ATOM 4670 N THR C 210 3.983 157.044 29.800 1.00 38.77 N ANISOU 4670 N THR C 210 5248 4989 4494 -541 -273 314 N ATOM 4671 CA THR C 210 3.414 157.853 28.718 1.00 40.87 C ANISOU 4671 CA THR C 210 5509 5243 4778 -509 -271 425 C ATOM 4672 C THR C 210 4.383 157.848 27.532 1.00 42.88 C ANISOU 4672 C THR C 210 5705 5568 5022 -609 -273 522 C ATOM 4673 O THR C 210 5.552 158.192 27.675 1.00 42.75 O ANISOU 4673 O THR C 210 5698 5497 5047 -707 -295 537 O ATOM 4674 CB THR C 210 3.070 159.285 29.174 1.00 41.71 C ANISOU 4674 CB THR C 210 5733 5160 4956 -458 -295 443 C ATOM 4675 OG1 THR C 210 2.191 159.218 30.299 1.00 41.14 O ANISOU 4675 OG1 THR C 210 5715 5040 4876 -348 -271 347 O ATOM 4676 CG2 THR C 210 2.375 160.071 28.060 1.00 42.62 C ANISOU 4676 CG2 THR C 210 5840 5265 5090 -405 -294 572 C ATOM 4677 N VAL C 211 3.878 157.432 26.370 1.00 45.85 N ANISOU 4677 N VAL C 211 6015 6073 5335 -584 -252 588 N ATOM 4678 CA VAL C 211 4.686 157.211 25.174 1.00 48.62 C ANISOU 4678 CA VAL C 211 6309 6527 5636 -657 -232 672 C ATOM 4679 C VAL C 211 4.476 158.371 24.206 1.00 53.32 C ANISOU 4679 C VAL C 211 6936 7078 6244 -652 -243 819 C ATOM 4680 O VAL C 211 3.337 158.687 23.874 1.00 52.19 O ANISOU 4680 O VAL C 211 6808 6936 6088 -564 -260 857 O ATOM 4681 CB VAL C 211 4.274 155.888 24.490 1.00 47.82 C ANISOU 4681 CB VAL C 211 6137 6602 5430 -630 -208 636 C ATOM 4682 CG1 VAL C 211 5.133 155.616 23.257 1.00 48.71 C ANISOU 4682 CG1 VAL C 211 6208 6831 5467 -687 -172 710 C ATOM 4683 CG2 VAL C 211 4.369 154.730 25.479 1.00 46.31 C ANISOU 4683 CG2 VAL C 211 5924 6436 5236 -627 -198 502 C ATOM 4684 N GLU C 212 5.568 158.978 23.737 1.00 44.68 N ATOM 4685 CA GLU C 212 5.495 160.162 22.863 1.00 49.56 C ATOM 4686 C GLU C 212 6.578 160.188 21.776 1.00 52.58 C ATOM 4687 O GLU C 212 7.495 159.364 21.792 1.00 53.34 O ATOM 4688 CB GLU C 212 5.519 161.443 23.713 1.00 51.42 C ATOM 4689 CG GLU C 212 6.698 161.561 24.670 1.00 53.12 C ATOM 4690 CD GLU C 212 6.665 162.831 25.506 1.00 54.62 C ATOM 4691 OE1 GLU C 212 7.745 163.423 25.729 1.00 56.60 O ATOM 4692 OE2 GLU C 212 5.566 163.240 25.947 1.00 55.27 O ATOM 4693 N ARG C 213 6.424 161.146 20.852 1.00 56.71 N ATOM 4694 CA ARG C 213 7.201 161.350 19.600 1.00 58.41 C ATOM 4695 C ARG C 213 6.420 160.811 18.410 1.00 58.81 C ATOM 4696 O ARG C 213 5.606 161.522 17.821 1.00 60.78 O ATOM 4697 CB ARG C 213 8.645 160.795 19.585 1.00 59.58 C ATOM 4698 CG ARG C 213 9.692 161.731 20.181 1.00 60.86 C ATOM 4699 CD ARG C 213 11.006 161.674 19.411 1.00 62.14 C ATOM 4700 NE ARG C 213 11.839 162.856 19.641 1.00 63.56 N ATOM 4701 CZ ARG C 213 12.926 163.184 18.934 1.00 64.74 C ATOM 4702 NH1 ARG C 213 13.352 162.423 17.924 1.00 65.00 N ATOM 4703 NH2 ARG C 213 13.600 164.292 19.240 1.00 65.49 N TER 4704 ARG C 213 ATOM 4705 N ALA D 3 12.485 115.719 12.068 1.00 50.91 N ANISOU 4705 N ALA D 3 5457 9093 4792 1563 45 -215 N ATOM 4706 CA ALA D 3 10.998 115.895 11.985 1.00 48.94 C ANISOU 4706 CA ALA D 3 5431 8615 4549 1425 47 -374 C ATOM 4707 C ALA D 3 10.481 115.781 10.548 1.00 49.23 C ANISOU 4707 C ALA D 3 5452 8811 4442 1556 159 -407 C ATOM 4708 O ALA D 3 11.137 116.218 9.607 1.00 50.75 O ANISOU 4708 O ALA D 3 5405 9301 4575 1646 239 -229 O ATOM 4709 CB ALA D 3 10.577 117.231 12.583 1.00 47.84 C ANISOU 4709 CB ALA D 3 5251 8339 4586 1127 -35 -282 C ATOM 4710 N LEU D 4 9.285 115.218 10.395 1.00 48.13 N ANISOU 4710 N LEU D 4 5560 8480 4249 1558 155 -618 N ATOM 4711 CA LEU D 4 8.682 115.027 9.070 1.00 48.35 C ANISOU 4711 CA LEU D 4 5616 8626 4131 1686 226 -688 C ATOM 4712 C LEU D 4 8.191 116.387 8.556 1.00 47.81 C ANISOU 4712 C LEU D 4 5401 8629 4134 1494 253 -538 C ATOM 4713 O LEU D 4 7.578 117.154 9.311 1.00 46.29 O ANISOU 4713 O LEU D 4 5248 8239 4102 1248 191 -522 O ATOM 4714 CB LEU D 4 7.538 114.001 9.122 1.00 47.72 C ANISOU 4714 CB LEU D 4 5838 8289 4004 1716 175 -951 C ATOM 4715 CG LEU D 4 7.787 112.689 9.889 1.00 48.11 C ANISOU 4715 CG LEU D 4 6086 8157 4038 1837 110 -1101 C ATOM 4716 CD1 LEU D 4 6.562 111.790 9.834 1.00 47.75 C ANISOU 4716 CD1 LEU D 4 6315 7849 3980 1820 41 -1320 C ATOM 4717 CD2 LEU D 4 9.012 111.956 9.357 1.00 50.49 C ANISOU 4717 CD2 LEU D 4 6312 8684 4186 2161 148 -1090 C ATOM 4718 N THR D 5 8.470 116.690 7.288 1.00 48.92 N ANISOU 4718 N THR D 5 5382 9060 4147 1626 343 -423 N ATOM 4719 CA THR D 5 8.191 118.019 6.732 1.00 49.00 C ANISOU 4719 CA THR D 5 5223 9169 4226 1460 368 -228 C ATOM 4720 C THR D 5 6.712 118.169 6.342 1.00 47.64 C ANISOU 4720 C THR D 5 5224 8833 4045 1371 343 -378 C ATOM 4721 O THR D 5 6.191 117.378 5.557 1.00 47.99 O ANISOU 4721 O THR D 5 5399 8914 3921 1544 364 -543 O ATOM 4722 CB THR D 5 9.092 118.314 5.513 1.00 51.54 C ANISOU 4722 CB THR D 5 5282 9898 4401 1638 488 -1 C ATOM 4723 OG1 THR D 5 10.465 118.148 5.889 1.00 52.99 O ANISOU 4723 OG1 THR D 5 5274 10255 4604 1724 512 155 O ATOM 4724 CG2 THR D 5 8.888 119.741 4.993 1.00 51.67 C ANISOU 4724 CG2 THR D 5 5111 10006 4514 1443 501 250 C ATOM 4725 N GLN D 6 6.051 119.184 6.900 1.00 46.32 N ANISOU 4725 N GLN D 6 5058 8484 4059 1113 283 -326 N ATOM 4726 CA GLN D 6 4.681 119.548 6.527 1.00 45.41 C ANISOU 4726 CA GLN D 6 5051 8244 3959 1016 262 -419 C ATOM 4727 C GLN D 6 4.630 121.019 6.114 1.00 45.84 C ANISOU 4727 C GLN D 6 4928 8376 4112 865 260 -189 C ATOM 4728 O GLN D 6 5.474 121.799 6.542 1.00 46.22 O ANISOU 4728 O GLN D 6 4817 8455 4287 757 232 10 O ATOM 4729 CB GLN D 6 3.728 119.340 7.702 1.00 43.28 C ANISOU 4729 CB GLN D 6 4980 7648 3816 864 186 -595 C ATOM 4730 CG GLN D 6 3.676 117.925 8.261 1.00 42.95 C ANISOU 4730 CG GLN D 6 5128 7475 3715 967 167 -797 C ATOM 4731 CD GLN D 6 2.675 117.781 9.401 1.00 41.45 C ANISOU 4731 CD GLN D 6 5108 6997 3645 808 112 -923 C ATOM 4732 OE1 GLN D 6 3.011 117.275 10.472 1.00 41.41 O ANISOU 4732 OE1 GLN D 6 5188 6864 3681 792 83 -966 O ATOM 4733 NE2 GLN D 6 1.448 118.248 9.187 1.00 40.51 N ANISOU 4733 NE2 GLN D 6 5025 6793 3573 700 102 -965 N ATOM 4734 N PRO D 7 3.642 121.407 5.278 1.00 46.18 N ANISOU 4734 N PRO D 7 4998 8436 4111 851 268 -208 N ATOM 4735 CA PRO D 7 3.449 122.841 5.038 1.00 46.66 C ANISOU 4735 CA PRO D 7 4927 8503 4299 688 241 1 C ATOM 4736 C PRO D 7 2.956 123.535 6.316 1.00 45.40 C ANISOU 4736 C PRO D 7 4851 8036 4362 473 136 -45 C ATOM 4737 O PRO D 7 2.278 122.917 7.137 1.00 43.93 O ANISOU 4737 O PRO D 7 4845 7650 4197 456 109 -260 O ATOM 4738 CB PRO D 7 2.398 122.883 3.924 1.00 46.83 C ANISOU 4738 CB PRO D 7 4997 8594 4200 753 263 -57 C ATOM 4739 CG PRO D 7 1.660 121.596 4.036 1.00 45.96 C ANISOU 4739 CG PRO D 7 5098 8375 3990 857 250 -352 C ATOM 4740 CD PRO D 7 2.613 120.588 4.616 1.00 45.90 C ANISOU 4740 CD PRO D 7 5127 8379 3935 965 271 -423 C ATOM 4741 N ARG D 8 3.332 124.793 6.505 1.00 46.26 N ANISOU 4741 N ARG D 8 4834 8110 4634 321 71 165 N ATOM 4742 CA ARG D 8 2.920 125.535 7.698 1.00 45.94 C ANISOU 4742 CA ARG D 8 4889 7780 4786 151 -48 111 C ATOM 4743 C ARG D 8 1.422 125.824 7.725 1.00 44.15 C ANISOU 4743 C ARG D 8 4804 7389 4582 117 -65 -39 C ATOM 4744 O ARG D 8 0.791 125.768 8.785 1.00 43.49 O ANISOU 4744 O ARG D 8 4870 7091 4564 69 -110 -202 O ATOM 4745 CB ARG D 8 3.668 126.867 7.766 1.00 48.06 C ANISOU 4745 CB ARG D 8 4997 8028 5235 -2 -152 375 C ATOM 4746 CG ARG D 8 5.170 126.732 7.982 1.00 50.43 C ANISOU 4746 CG ARG D 8 5128 8462 5570 -12 -168 549 C ATOM 4747 CD ARG D 8 5.863 128.085 8.087 1.00 52.84 C ANISOU 4747 CD ARG D 8 5269 8712 6096 -204 -310 827 C ATOM 4748 NE ARG D 8 7.317 127.963 8.228 1.00 55.29 N ANISOU 4748 NE ARG D 8 5371 9181 6456 -226 -331 1029 N ATOM 4749 CZ ARG D 8 7.973 127.693 9.362 1.00 56.11 C ANISOU 4749 CZ ARG D 8 5513 9169 6640 -267 -432 958 C ATOM 4750 NH1 ARG D 8 7.329 127.500 10.518 1.00 54.90 N ANISOU 4750 NH1 ARG D 8 5611 8739 6509 -284 -515 687 N ATOM 4751 NH2 ARG D 8 9.305 127.615 9.345 1.00 58.14 N ANISOU 4751 NH2 ARG D 8 5538 9608 6946 -283 -449 1176 N ATOM 4752 N SER D 9 0.878 126.126 6.550 1.00 43.58 N ANISOU 4752 N SER D 9 4672 7444 4443 156 -25 31 N ATOM 4753 CA SER D 9 -0.471 126.652 6.407 1.00 42.75 C ANISOU 4753 CA SER D 9 4647 7216 4381 118 -56 -49 C ATOM 4754 C SER D 9 -1.163 126.059 5.187 1.00 42.48 C ANISOU 4754 C SER D 9 4613 7349 4176 239 14 -106 C ATOM 4755 O SER D 9 -0.567 125.993 4.114 1.00 43.41 O ANISOU 4755 O SER D 9 4618 7706 4171 326 67 34 O ATOM 4756 CB SER D 9 -0.415 128.175 6.234 1.00 43.59 C ANISOU 4756 CB SER D 9 4662 7255 4644 1 -148 160 C ATOM 4757 OG SER D 9 -1.716 128.703 6.071 1.00 43.77 O ANISOU 4757 OG SER D 9 4757 7169 4706 -9 -178 85 O ATOM 4758 N VAL D 11 -2.414 125.636 5.370 1.00 41.01 N ANISOU 4758 N VAL D 11 4551 7051 3981 247 7 -304 N ATOM 4759 CA VAL D 11 -3.355 125.448 4.265 1.00 41.11 C ANISOU 4759 CA VAL D 11 4566 7166 3887 319 16 -350 C ATOM 4760 C VAL D 11 -4.706 126.007 4.650 1.00 39.95 C ANISOU 4760 C VAL D 11 4471 6851 3859 244 -34 -429 C ATOM 4761 O VAL D 11 -5.039 126.112 5.835 1.00 39.00 O ANISOU 4761 O VAL D 11 4421 6543 3854 175 -51 -515 O ATOM 4762 CB VAL D 11 -3.590 123.972 3.866 1.00 41.22 C ANISOU 4762 CB VAL D 11 4672 7250 3739 438 43 -541 C ATOM 4763 CG1 VAL D 11 -2.430 123.447 3.048 1.00 42.48 C ANISOU 4763 CG1 VAL D 11 4773 7647 3721 587 99 -466 C ATOM 4764 CG2 VAL D 11 -3.867 123.095 5.081 1.00 40.15 C ANISOU 4764 CG2 VAL D 11 4665 6921 3668 392 37 -722 C ATOM 4765 N SER D 12 -5.499 126.305 3.630 1.00 39.97 N ANISOU 4765 N SER D 12 4436 6942 3810 282 -55 -402 N ATOM 4766 CA SER D 12 -6.804 126.895 3.843 1.00 39.49 C ANISOU 4766 CA SER D 12 4391 6756 3855 235 -102 -455 C ATOM 4767 C SER D 12 -7.802 126.574 2.741 1.00 40.24 C ANISOU 4767 C SER D 12 4472 6964 3852 299 -130 -510 C ATOM 4768 O SER D 12 -7.429 126.243 1.609 1.00 40.54 O ANISOU 4768 O SER D 12 4482 7194 3729 391 -126 -464 O ATOM 4769 CB SER D 12 -6.656 128.410 4.018 1.00 39.86 C ANISOU 4769 CB SER D 12 4383 6717 4044 172 -154 -281 C ATOM 4770 OG SER D 12 -6.091 129.017 2.875 1.00 41.15 O ANISOU 4770 OG SER D 12 4444 7044 4149 196 -163 -67 O ATOM 4771 N GLY D 13 -9.076 126.664 3.107 1.00 39.60 N ANISOU 4771 N GLY D 13 4408 6777 3863 263 -164 -609 N ATOM 4772 CA GLY D 13 -10.181 126.532 2.172 1.00 40.63 C ANISOU 4772 CA GLY D 13 4506 6988 3944 303 -221 -653 C ATOM 4773 C GLY D 13 -11.463 127.066 2.785 1.00 40.49 C ANISOU 4773 C GLY D 13 4459 6848 4078 257 -247 -695 C ATOM 4774 O GLY D 13 -11.583 127.157 4.005 1.00 39.92 O ANISOU 4774 O GLY D 13 4418 6635 4114 209 -205 -743 O ATOM 4775 N SER D 14 -12.410 127.445 1.934 1.00 41.52 N ANISOU 4775 N SER D 14 4524 7049 4200 291 -313 -671 N ATOM 4776 CA SER D 14 -13.761 127.804 2.370 1.00 41.72 C ANISOU 4776 CA SER D 14 4494 7002 4355 273 -338 -716 C ATOM 4777 C SER D 14 -14.522 126.561 2.821 1.00 41.28 C ANISOU 4777 C SER D 14 4443 6921 4322 219 -336 -870 C ATOM 4778 O SER D 14 -14.150 125.449 2.433 1.00 41.30 O ANISOU 4778 O SER D 14 4502 6964 4225 209 -360 -951 O ATOM 4779 CB SER D 14 -14.531 128.465 1.229 1.00 43.15 C ANISOU 4779 CB SER D 14 4595 7287 4515 330 -427 -639 C ATOM 4780 OG SER D 14 -13.894 129.651 0.823 1.00 43.89 O ANISOU 4780 OG SER D 14 4679 7389 4609 366 -438 -464 O ATOM 4781 N PRO D 15 -15.596 126.741 3.626 1.00 40.91 N ANISOU 4781 N PRO D 15 4331 6808 4405 192 -312 -900 N ATOM 4782 CA PRO D 15 -16.458 125.614 3.968 1.00 41.12 C ANISOU 4782 CA PRO D 15 4319 6825 4478 118 -321 -996 C ATOM 4783 C PRO D 15 -16.958 124.885 2.719 1.00 42.14 C ANISOU 4783 C PRO D 15 4419 7048 4544 105 -458 -1046 C ATOM 4784 O PRO D 15 -17.350 125.531 1.742 1.00 42.32 O ANISOU 4784 O PRO D 15 4383 7164 4533 166 -537 -996 O ATOM 4785 CB PRO D 15 -17.632 126.276 4.700 1.00 41.69 C ANISOU 4785 CB PRO D 15 4274 6882 4685 133 -277 -965 C ATOM 4786 CG PRO D 15 -17.046 127.513 5.289 1.00 41.13 C ANISOU 4786 CG PRO D 15 4257 6739 4631 213 -216 -906 C ATOM 4787 CD PRO D 15 -16.056 127.987 4.269 1.00 40.92 C ANISOU 4787 CD PRO D 15 4288 6744 4516 241 -279 -838 C ATOM 4788 N GLY D 16 -16.907 123.558 2.753 1.00 42.26 N ANISOU 4788 N GLY D 16 4492 7025 4538 35 -502 -1147 N ATOM 4789 CA GLY D 16 -17.293 122.734 1.615 1.00 43.74 C ANISOU 4789 CA GLY D 16 4695 7268 4657 29 -669 -1230 C ATOM 4790 C GLY D 16 -16.152 122.366 0.674 1.00 44.14 C ANISOU 4790 C GLY D 16 4885 7383 4501 132 -713 -1281 C ATOM 4791 O GLY D 16 -16.299 121.433 -0.110 1.00 45.13 O ANISOU 4791 O GLY D 16 5078 7525 4544 147 -858 -1395 O ATOM 4792 N GLN D 17 -15.028 123.086 0.733 1.00 43.46 N ANISOU 4792 N GLN D 17 4839 7341 4331 211 -602 -1194 N ATOM 4793 CA GLN D 17 -13.870 122.788 -0.123 1.00 44.27 C ANISOU 4793 CA GLN D 17 5043 7552 4226 331 -610 -1207 C ATOM 4794 C GLN D 17 -13.012 121.672 0.460 1.00 44.06 C ANISOU 4794 C GLN D 17 5139 7440 4162 326 -573 -1308 C ATOM 4795 O GLN D 17 -13.232 121.215 1.588 1.00 43.16 O ANISOU 4795 O GLN D 17 5037 7175 4186 218 -532 -1346 O ATOM 4796 CB GLN D 17 -13.017 124.040 -0.338 1.00 43.93 C ANISOU 4796 CB GLN D 17 4956 7606 4130 399 -513 -1029 C ATOM 4797 CG GLN D 17 -13.770 125.177 -1.004 1.00 44.91 C ANISOU 4797 CG GLN D 17 4977 7808 4281 424 -562 -912 C ATOM 4798 CD GLN D 17 -12.876 126.342 -1.396 1.00 45.10 C ANISOU 4798 CD GLN D 17 4965 7922 4248 484 -497 -710 C ATOM 4799 OE1 GLN D 17 -11.956 126.717 -0.667 1.00 44.44 O ANISOU 4799 OE1 GLN D 17 4892 7775 4220 450 -404 -630 O ATOM 4800 NE2 GLN D 17 -13.158 126.936 -2.548 1.00 46.57 N ANISOU 4800 NE2 GLN D 17 5105 8255 4335 564 -562 -609 N ATOM 4801 N SER D 18 -12.039 121.232 -0.334 1.00 45.44 N ANISOU 4801 N SER D 18 5402 7726 4136 463 -586 -1342 N ATOM 4802 CA SER D 18 -11.069 120.228 0.084 1.00 45.67 C ANISOU 4802 CA SER D 18 5551 7698 4102 506 -553 -1430 C ATOM 4803 C SER D 18 -9.696 120.849 0.305 1.00 45.26 C ANISOU 4803 C SER D 18 5472 7742 3982 577 -406 -1292 C ATOM 4804 O SER D 18 -9.333 121.826 -0.351 1.00 46.20 O ANISOU 4804 O SER D 18 5507 8021 4025 640 -362 -1142 O ATOM 4805 CB SER D 18 -10.956 119.133 -0.969 1.00 47.48 C ANISOU 4805 CB SER D 18 5912 7988 4142 647 -691 -1595 C ATOM 4806 OG SER D 18 -12.214 118.515 -1.169 1.00 48.78 O ANISOU 4806 OG SER D 18 6100 8039 4395 558 -866 -1721 O ATOM 4807 N VAL D 19 -8.943 120.262 1.229 1.00 44.17 N ANISOU 4807 N VAL D 19 5398 7504 3881 557 -343 -1327 N ATOM 4808 CA VAL D 19 -7.532 120.580 1.413 1.00 43.78 C ANISOU 4808 CA VAL D 19 5324 7549 3760 632 -231 -1214 C ATOM 4809 C VAL D 19 -6.755 119.287 1.604 1.00 43.93 C ANISOU 4809 C VAL D 19 5469 7536 3688 728 -239 -1344 C ATOM 4810 O VAL D 19 -7.299 118.294 2.087 1.00 43.89 O ANISOU 4810 O VAL D 19 5572 7356 3750 672 -313 -1494 O ATOM 4811 CB VAL D 19 -7.275 121.510 2.617 1.00 42.81 C ANISOU 4811 CB VAL D 19 5130 7323 3814 500 -144 -1086 C ATOM 4812 CG1 VAL D 19 -7.755 122.926 2.318 1.00 42.98 C ANISOU 4812 CG1 VAL D 19 5035 7388 3907 450 -141 -936 C ATOM 4813 CG2 VAL D 19 -7.920 120.975 3.895 1.00 41.89 C ANISOU 4813 CG2 VAL D 19 5076 6988 3851 374 -149 -1188 C ATOM 4814 N THR D 20 -5.493 119.310 1.195 1.00 44.47 N ANISOU 4814 N THR D 20 5513 7778 3607 878 -166 -1269 N ATOM 4815 CA THR D 20 -4.582 118.177 1.340 1.00 45.17 C ANISOU 4815 CA THR D 20 5708 7866 3590 1014 -160 -1374 C ATOM 4816 C THR D 20 -3.331 118.652 2.053 1.00 44.15 C ANISOU 4816 C THR D 20 5482 7793 3499 1008 -39 -1215 C ATOM 4817 O THR D 20 -2.771 119.680 1.684 1.00 43.99 O ANISOU 4817 O THR D 20 5312 7946 3455 1016 35 -1015 O ATOM 4818 CB THR D 20 -4.172 117.606 -0.025 1.00 47.33 C ANISOU 4818 CB THR D 20 6037 8354 3591 1274 -195 -1450 C ATOM 4819 OG1 THR D 20 -5.347 117.271 -0.765 1.00 48.67 O ANISOU 4819 OG1 THR D 20 6293 8475 3723 1276 -340 -1596 O ATOM 4820 CG2 THR D 20 -3.304 116.358 0.132 1.00 48.28 C ANISOU 4820 CG2 THR D 20 6291 8451 3602 1449 -207 -1590 C ATOM 4821 N ILE D 21 -2.902 117.888 3.053 1.00 43.76 N ANISOU 4821 N ILE D 21 5518 7593 3516 987 -36 -1292 N ATOM 4822 CA ILE D 21 -1.713 118.190 3.848 1.00 43.65 C ANISOU 4822 CA ILE D 21 5426 7610 3550 977 49 -1163 C ATOM 4823 C ILE D 21 -0.671 117.108 3.564 1.00 45.03 C ANISOU 4823 C ILE D 21 5664 7885 3560 1200 62 -1238 C ATOM 4824 O ILE D 21 -0.924 115.933 3.813 1.00 45.22 O ANISOU 4824 O ILE D 21 5860 7754 3570 1252 -12 -1425 O ATOM 4825 CB ILE D 21 -2.031 118.205 5.361 1.00 41.93 C ANISOU 4825 CB ILE D 21 5260 7141 3530 791 39 -1186 C ATOM 4826 CG1 ILE D 21 -3.157 119.203 5.678 1.00 40.90 C ANISOU 4826 CG1 ILE D 21 5083 6912 3547 611 26 -1140 C ATOM 4827 CG2 ILE D 21 -0.787 118.564 6.168 1.00 41.57 C ANISOU 4827 CG2 ILE D 21 5137 7126 3530 781 94 -1059 C ATOM 4828 CD1 ILE D 21 -3.820 118.976 7.021 1.00 39.87 C ANISOU 4828 CD1 ILE D 21 5034 6553 3564 469 14 -1206 C ATOM 4829 N SER D 22 0.496 117.515 3.072 1.00 46.03 N ANISOU 4829 N SER D 22 5645 8268 3576 1333 152 -1078 N ATOM 4830 CA SER D 22 1.607 116.593 2.814 1.00 47.76 C ANISOU 4830 CA SER D 22 5888 8628 3628 1581 187 -1122 C ATOM 4831 C SER D 22 2.493 116.415 4.053 1.00 47.28 C ANISOU 4831 C SER D 22 5801 8471 3690 1524 210 -1070 C ATOM 4832 O SER D 22 2.577 117.306 4.914 1.00 46.03 O ANISOU 4832 O SER D 22 5546 8232 3712 1316 223 -931 O ATOM 4833 CB SER D 22 2.453 117.102 1.653 1.00 49.43 C ANISOU 4833 CB SER D 22 5920 9214 3645 1773 290 -943 C ATOM 4834 OG SER D 22 2.955 118.395 1.943 1.00 48.98 O ANISOU 4834 OG SER D 22 5637 9251 3721 1606 361 -661 O ATOM 4835 N CYS D 23 3.161 115.265 4.111 1.00 48.57 N ANISOU 4835 N CYS D 23 6065 8645 3746 1729 199 -1189 N ATOM 4836 CA CYS D 23 4.030 114.885 5.225 1.00 48.51 C ANISOU 4836 CA CYS D 23 6056 8551 3825 1720 205 -1163 C ATOM 4837 C CYS D 23 5.209 114.080 4.682 1.00 50.90 C ANISOU 4837 C CYS D 23 6334 9074 3932 2043 252 -1179 C ATOM 4838 O CYS D 23 5.091 112.875 4.461 1.00 52.19 O ANISOU 4838 O CYS D 23 6698 9145 3985 2234 185 -1393 O ATOM 4839 CB CYS D 23 3.238 114.059 6.237 1.00 47.73 C ANISOU 4839 CB CYS D 23 6182 8101 3850 1597 104 -1344 C ATOM 4840 SG CYS D 23 4.237 113.247 7.514 1.00 48.18 S ANISOU 4840 SG CYS D 23 6304 8036 3965 1646 85 -1357 S ATOM 4841 N THR D 24 6.329 114.759 4.446 1.00 51.61 N ANISOU 4841 N THR D 24 6171 9455 3982 2110 359 -946 N ATOM 4842 CA THR D 24 7.467 114.174 3.743 1.00 54.10 C ANISOU 4842 CA THR D 24 6400 10072 4082 2450 439 -915 C ATOM 4843 C THR D 24 8.526 113.681 4.725 1.00 54.18 C ANISOU 4843 C THR D 24 6370 10052 4164 2505 436 -880 C ATOM 4844 O THR D 24 9.084 114.460 5.504 1.00 53.18 O ANISOU 4844 O THR D 24 6062 9937 4208 2312 450 -679 O ATOM 4845 CB THR D 24 8.075 115.184 2.755 1.00 55.70 C ANISOU 4845 CB THR D 24 6310 10673 4180 2513 574 -637 C ATOM 4846 OG1 THR D 24 7.061 115.597 1.834 1.00 55.74 O ANISOU 4846 OG1 THR D 24 6372 10701 4105 2479 565 -677 O ATOM 4847 CG2 THR D 24 9.238 114.568 1.966 1.00 58.77 C ANISOU 4847 CG2 THR D 24 6586 11432 4311 2907 685 -590 C ATOM 4848 N GLY D 25 8.785 112.377 4.675 1.00 55.16 N ANISOU 4848 N GLY D 25 6678 10123 4157 2775 395 -1085 N ATOM 4849 CA GLY D 25 9.799 111.735 5.498 1.00 55.30 C ANISOU 4849 CA GLY D 25 6681 10121 4209 2889 383 -1076 C ATOM 4850 C GLY D 25 10.913 111.169 4.638 1.00 58.32 C ANISOU 4850 C GLY D 25 6955 10857 4346 3308 478 -1052 C ATOM 4851 O GLY D 25 11.270 111.746 3.611 1.00 59.28 O ANISOU 4851 O GLY D 25 6870 11337 4316 3436 602 -897 O ATOM 4852 N THR D 26 11.451 110.035 5.081 1.00 59.42 N ANISOU 4852 N THR D 26 7236 10900 4441 3531 421 -1196 N ATOM 4853 CA THR D 26 12.571 109.344 4.443 1.00 62.71 C ANISOU 4853 CA THR D 26 7573 11628 4626 3976 501 -1201 C ATOM 4854 C THR D 26 12.149 107.874 4.266 1.00 63.66 C ANISOU 4854 C THR D 26 8078 11491 4619 4249 363 -1555 C ATOM 4855 O THR D 26 11.091 107.454 4.764 1.00 62.14 O ANISOU 4855 O THR D 26 8165 10886 4559 4042 210 -1741 O ATOM 4856 CB THR D 26 13.838 109.484 5.346 1.00 63.33 C ANISOU 4856 CB THR D 26 7409 11831 4821 3974 541 -991 C ATOM 4857 OG1 THR D 26 14.020 110.858 5.702 1.00 62.32 O ANISOU 4857 OG1 THR D 26 6984 11815 4880 3632 597 -690 O ATOM 4858 CG2 THR D 26 15.127 108.985 4.685 1.00 66.97 C ANISOU 4858 CG2 THR D 26 7688 12704 5054 4433 661 -920 C ATOM 4859 N SER D 27 12.955 107.101 3.539 1.00 66.74 N ANISOU 4859 N SER D 27 8479 12124 4754 4718 409 -1641 N ATOM 4860 CA SER D 27 12.741 105.657 3.403 1.00 68.30 C ANISOU 4860 CA SER D 27 9050 12066 4835 5023 251 -1979 C ATOM 4861 C SER D 27 12.871 104.849 4.715 1.00 67.67 C ANISOU 4861 C SER D 27 9150 11603 4958 4932 108 -2060 C ATOM 4862 O SER D 27 12.447 103.697 4.754 1.00 68.67 O ANISOU 4862 O SER D 27 9626 11406 5061 5078 -68 -2332 O ATOM 4863 CB SER D 27 13.696 105.088 2.360 1.00 72.13 C ANISOU 4863 CB SER D 27 9487 12937 4981 5593 345 -2040 C ATOM 4864 OG SER D 27 13.431 103.719 2.131 1.00 74.02 O ANISOU 4864 OG SER D 27 10123 12903 5098 5908 161 -2395 O ATOM 4865 N SER D 28 13.468 105.432 5.759 1.00 66.14 N ANISOU 4865 N SER D 28 8729 11444 4957 4703 165 -1823 N ATOM 4866 CA SER D 28 13.529 104.800 7.089 1.00 65.43 C ANISOU 4866 CA SER D 28 8799 11000 5063 4573 33 -1866 C ATOM 4867 C SER D 28 12.373 105.147 8.047 1.00 62.08 C ANISOU 4867 C SER D 28 8513 10185 4891 4091 -65 -1867 C ATOM 4868 O SER D 28 12.383 104.706 9.202 1.00 61.17 O ANISOU 4868 O SER D 28 8518 9795 4928 3962 -161 -1871 O ATOM 4869 CB SER D 28 14.860 105.124 7.769 1.00 66.32 C ANISOU 4869 CB SER D 28 8612 11356 5229 4627 119 -1628 C ATOM 4870 OG SER D 28 15.007 104.395 8.976 1.00 66.40 O ANISOU 4870 OG SER D 28 8795 11051 5383 4574 -14 -1682 O ATOM 4871 N ASP D 29 11.396 105.931 7.589 1.00 60.03 N ANISOU 4871 N ASP D 29 8227 9917 4663 3844 -37 -1851 N ATOM 4872 CA ASP D 29 10.189 106.205 8.383 1.00 57.52 C ANISOU 4872 CA ASP D 29 8047 9251 4559 3431 -122 -1869 C ATOM 4873 C ASP D 29 8.910 106.135 7.525 1.00 57.05 C ANISOU 4873 C ASP D 29 8156 9063 4458 3360 -184 -2033 C ATOM 4874 O ASP D 29 8.370 105.038 7.361 1.00 58.04 O ANISOU 4874 O ASP D 29 8573 8919 4561 3464 -336 -2255 O ATOM 4875 CB ASP D 29 10.323 107.507 9.213 1.00 55.05 C ANISOU 4875 CB ASP D 29 7480 9021 4417 3093 -39 -1618 C ATOM 4876 CG ASP D 29 10.856 108.679 8.408 1.00 55.35 C ANISOU 4876 CG ASP D 29 7190 9458 4384 3108 109 -1419 C ATOM 4877 OD1 ASP D 29 10.121 109.157 7.523 1.00 55.15 O ANISOU 4877 OD1 ASP D 29 7155 9500 4298 3055 144 -1442 O ATOM 4878 OD2 ASP D 29 11.994 109.128 8.645 1.00 56.01 O ANISOU 4878 OD2 ASP D 29 7017 9786 4478 3163 182 -1223 O ATOM 4879 N VAL D 30 8.460 107.245 6.934 1.00 56.16 N ANISOU 4879 N VAL D 30 7867 9134 4336 3202 -91 -1926 N ATOM 4880 CA VAL D 30 7.186 107.281 6.193 1.00 55.85 C ANISOU 4880 CA VAL D 30 7966 8976 4279 3101 -161 -2062 C ATOM 4881 C VAL D 30 7.181 106.258 5.052 1.00 58.68 C ANISOU 4881 C VAL D 30 8530 9356 4411 3470 -253 -2304 C ATOM 4882 O VAL D 30 6.219 105.509 4.899 1.00 59.11 O ANISOU 4882 O VAL D 30 8849 9109 4501 3427 -426 -2510 O ATOM 4883 CB VAL D 30 6.872 108.695 5.633 1.00 54.86 C ANISOU 4883 CB VAL D 30 7596 9097 4152 2927 -37 -1887 C ATOM 4884 CG1 VAL D 30 5.660 108.667 4.697 1.00 55.18 C ANISOU 4884 CG1 VAL D 30 7770 9063 4133 2891 -116 -2035 C ATOM 4885 CG2 VAL D 30 6.642 109.688 6.768 1.00 52.34 C ANISOU 4885 CG2 VAL D 30 7138 8680 4068 2554 4 -1699 C ATOM 4886 N GLY D 30A 8.261 106.231 4.271 1.00 60.81 N ANISOU 4886 N GLY D 30A 8672 9985 4449 3835 -146 -2273 N ATOM 4887 CA GLY D 30A 8.411 105.267 3.175 1.00 64.21 C ANISOU 4887 CA GLY D 30A 9303 10480 4615 4263 -225 -2515 C ATOM 4888 C GLY D 30A 9.031 103.929 3.545 1.00 66.12 C ANISOU 4888 C GLY D 30A 9769 10536 4816 4557 -345 -2692 C ATOM 4889 O GLY D 30A 9.332 103.136 2.662 1.00 69.33 O ANISOU 4889 O GLY D 30A 10340 11020 4982 4973 -408 -2898 O ATOM 4890 N GLY D 30B 9.234 103.676 4.838 1.00 64.55 N ANISOU 4890 N GLY D 30B 9591 10097 4837 4368 -383 -2618 N ATOM 4891 CA GLY D 30B 9.739 102.391 5.324 1.00 66.48 C ANISOU 4891 CA GLY D 30B 10070 10106 5082 4608 -520 -2771 C ATOM 4892 C GLY D 30B 8.676 101.455 5.868 1.00 66.28 C ANISOU 4892 C GLY D 30B 10397 9545 5242 4412 -767 -2953 C ATOM 4893 O GLY D 30B 8.886 100.250 5.909 1.00 68.81 O ANISOU 4893 O GLY D 30B 10989 9626 5531 4658 -936 -3142 O ATOM 4894 N TYR D 30C 7.549 102.005 6.320 1.00 63.83 N ANISOU 4894 N TYR D 30C 10075 9043 5136 3970 -791 -2878 N ATOM 4895 CA TYR D 30C 6.471 101.214 6.928 1.00 63.62 C ANISOU 4895 CA TYR D 30C 10326 8528 5319 3721 -1007 -2984 C ATOM 4896 C TYR D 30C 5.137 101.813 6.505 1.00 62.41 C ANISOU 4896 C TYR D 30C 10155 8312 5247 3414 -1039 -2991 C ATOM 4897 O TYR D 30C 5.099 102.890 5.910 1.00 61.41 O ANISOU 4897 O TYR D 30C 9802 8502 5031 3375 -885 -2896 O ATOM 4898 CB TYR D 30C 6.583 101.217 8.472 1.00 61.59 C ANISOU 4898 CB TYR D 30C 10034 8082 5284 3451 -981 -2802 C ATOM 4899 CG TYR D 30C 7.976 100.908 9.004 1.00 62.35 C ANISOU 4899 CG TYR D 30C 10068 8308 5315 3713 -917 -2734 C ATOM 4900 CD1 TYR D 30C 8.955 101.897 9.029 1.00 61.26 C ANISOU 4900 CD1 TYR D 30C 9604 8579 5095 3775 -706 -2547 C ATOM 4901 CD2 TYR D 30C 8.321 99.630 9.471 1.00 64.28 C ANISOU 4901 CD2 TYR D 30C 10571 8261 5591 3894 -1084 -2844 C ATOM 4902 CE1 TYR D 30C 10.237 101.639 9.488 1.00 62.29 C ANISOU 4902 CE1 TYR D 30C 9642 8851 5173 4012 -656 -2471 C ATOM 4903 CE2 TYR D 30C 9.607 99.364 9.941 1.00 65.11 C ANISOU 4903 CE2 TYR D 30C 10603 8504 5633 4151 -1028 -2777 C ATOM 4904 CZ TYR D 30C 10.560 100.374 9.945 1.00 64.06 C ANISOU 4904 CZ TYR D 30C 10121 8803 5416 4209 -812 -2590 C ATOM 4905 OH TYR D 30C 11.836 100.143 10.402 1.00 65.21 O ANISOU 4905 OH TYR D 30C 10159 9106 5510 4453 -764 -2507 O ATOM 4906 N ASN D 31 4.049 101.112 6.815 1.00 62.88 N ANISOU 4906 N ASN D 31 10441 7964 5486 3193 -1245 -3085 N ATOM 4907 CA ASN D 31 2.700 101.672 6.706 1.00 61.42 C ANISOU 4907 CA ASN D 31 10208 7688 5439 2837 -1276 -3047 C ATOM 4908 C ASN D 31 2.109 101.907 8.098 1.00 59.29 C ANISOU 4908 C ASN D 31 9876 7219 5432 2435 -1234 -2848 C ATOM 4909 O ASN D 31 0.976 101.519 8.389 1.00 59.45 O ANISOU 4909 O ASN D 31 10006 6946 5637 2170 -1374 -2856 O ATOM 4910 CB ASN D 31 1.827 100.771 5.833 1.00 64.14 C ANISOU 4910 CB ASN D 31 10824 7767 5778 2894 -1552 -3296 C ATOM 4911 CG ASN D 31 2.272 100.784 4.382 1.00 66.27 C ANISOU 4911 CG ASN D 31 11132 8300 5746 3288 -1568 -3486 C ATOM 4912 OD1 ASN D 31 2.441 101.853 3.795 1.00 65.60 O ANISOU 4912 OD1 ASN D 31 10814 8591 5521 3321 -1378 -3392 O ATOM 4913 ND2 ASN D 31 2.485 99.611 3.803 1.00 69.61 N ANISOU 4913 ND2 ASN D 31 11855 8535 6060 3603 -1797 -3748 N ATOM 4914 N TYR D 32 2.908 102.561 8.944 1.00 57.29 N ANISOU 4914 N TYR D 32 9435 7147 5185 2404 -1042 -2660 N ATOM 4915 CA TYR D 32 2.522 102.907 10.306 1.00 55.30 C ANISOU 4915 CA TYR D 32 9112 6773 5126 2079 -973 -2467 C ATOM 4916 C TYR D 32 2.524 104.427 10.437 1.00 52.32 C ANISOU 4916 C TYR D 32 8446 6694 4741 1923 -765 -2299 C ATOM 4917 O TYR D 32 3.214 104.994 11.279 1.00 50.76 O ANISOU 4917 O TYR D 32 8114 6615 4558 1885 -643 -2150 O ATOM 4918 CB TYR D 32 3.468 102.236 11.315 1.00 56.06 C ANISOU 4918 CB TYR D 32 9292 6766 5243 2188 -984 -2411 C ATOM 4919 CG TYR D 32 3.430 100.713 11.285 1.00 59.06 C ANISOU 4919 CG TYR D 32 9981 6798 5660 2329 -1213 -2564 C ATOM 4920 CD1 TYR D 32 2.211 100.021 11.258 1.00 60.06 C ANISOU 4920 CD1 TYR D 32 10291 6582 5945 2121 -1401 -2623 C ATOM 4921 CD2 TYR D 32 4.608 99.961 11.301 1.00 60.90 C ANISOU 4921 CD2 TYR D 32 10319 7034 5786 2666 -1260 -2637 C ATOM 4922 CE1 TYR D 32 2.169 98.636 11.233 1.00 62.97 C ANISOU 4922 CE1 TYR D 32 10957 6594 6376 2231 -1645 -2753 C ATOM 4923 CE2 TYR D 32 4.572 98.570 11.279 1.00 63.75 C ANISOU 4923 CE2 TYR D 32 10987 7043 6190 2808 -1493 -2784 C ATOM 4924 CZ TYR D 32 3.350 97.915 11.246 1.00 64.70 C ANISOU 4924 CZ TYR D 32 11304 6798 6481 2581 -1694 -2842 C ATOM 4925 OH TYR D 32 3.293 96.544 11.221 1.00 67.66 O ANISOU 4925 OH TYR D 32 11995 6785 6926 2700 -1960 -2978 O ATOM 4926 N VAL D 33 1.752 105.065 9.558 1.00 51.77 N ANISOU 4926 N VAL D 33 8294 6730 4647 1844 -751 -2332 N ATOM 4927 CA VAL D 33 1.580 106.513 9.535 1.00 49.52 C ANISOU 4927 CA VAL D 33 7759 6688 4368 1691 -586 -2185 C ATOM 4928 C VAL D 33 0.238 106.842 10.180 1.00 47.94 C ANISOU 4928 C VAL D 33 7547 6316 4352 1353 -596 -2114 C ATOM 4929 O VAL D 33 -0.805 106.276 9.813 1.00 48.55 O ANISOU 4929 O VAL D 33 7739 6206 4502 1257 -728 -2205 O ATOM 4930 CB VAL D 33 1.615 107.081 8.097 1.00 50.05 C ANISOU 4930 CB VAL D 33 7727 7017 4273 1844 -553 -2244 C ATOM 4931 CG1 VAL D 33 1.391 108.591 8.096 1.00 48.06 C ANISOU 4931 CG1 VAL D 33 7228 6978 4054 1668 -404 -2075 C ATOM 4932 CG2 VAL D 33 2.939 106.748 7.424 1.00 51.98 C ANISOU 4932 CG2 VAL D 33 7961 7481 4310 2210 -520 -2296 C ATOM 4933 N SER D 34 0.272 107.748 11.151 1.00 46.29 N ANISOU 4933 N SER D 34 7197 6174 4218 1184 -467 -1950 N ATOM 4934 CA SER D 34 -0.935 108.212 11.809 1.00 44.93 C ANISOU 4934 CA SER D 34 6982 5898 4190 904 -439 -1866 C ATOM 4935 C SER D 34 -0.975 109.729 11.777 1.00 43.09 C ANISOU 4935 C SER D 34 6537 5886 3949 822 -304 -1759 C ATOM 4936 O SER D 34 0.062 110.376 11.642 1.00 42.60 O ANISOU 4936 O SER D 34 6364 6016 3805 936 -232 -1705 O ATOM 4937 CB SER D 34 -1.014 107.669 13.240 1.00 45.27 C ANISOU 4937 CB SER D 34 7118 5748 4335 784 -440 -1779 C ATOM 4938 OG SER D 34 0.145 107.992 13.995 1.00 44.91 O ANISOU 4938 OG SER D 34 7027 5802 4233 873 -364 -1702 O ATOM 4939 N TRP D 35 -2.185 110.277 11.886 1.00 42.18 N ANISOU 4939 N TRP D 35 6361 5735 3929 627 -283 -1719 N ATOM 4940 CA TRP D 35 -2.425 111.716 11.835 1.00 40.51 C ANISOU 4940 CA TRP D 35 5974 5690 3729 545 -181 -1629 C ATOM 4941 C TRP D 35 -3.210 112.143 13.065 1.00 39.46 C ANISOU 4941 C TRP D 35 5819 5470 3706 359 -119 -1536 C ATOM 4942 O TRP D 35 -4.088 111.410 13.534 1.00 40.04 O ANISOU 4942 O TRP D 35 5968 5383 3862 247 -154 -1534 O ATOM 4943 CB TRP D 35 -3.210 112.079 10.574 1.00 40.98 C ANISOU 4943 CB TRP D 35 5969 5832 3770 538 -216 -1683 C ATOM 4944 CG TRP D 35 -2.439 111.960 9.290 1.00 41.82 C ANISOU 4944 CG TRP D 35 6069 6097 3724 751 -247 -1756 C ATOM 4945 CD1 TRP D 35 -2.291 110.842 8.510 1.00 43.62 C ANISOU 4945 CD1 TRP D 35 6437 6270 3864 908 -361 -1902 C ATOM 4946 CD2 TRP D 35 -1.730 113.010 8.620 1.00 41.39 C ANISOU 4946 CD2 TRP D 35 5859 6293 3575 843 -164 -1675 C ATOM 4947 NE1 TRP D 35 -1.525 111.133 7.405 1.00 44.17 N ANISOU 4947 NE1 TRP D 35 6447 6572 3762 1119 -334 -1924 N ATOM 4948 CE2 TRP D 35 -1.167 112.457 7.448 1.00 42.96 C ANISOU 4948 CE2 TRP D 35 6097 6616 3608 1070 -206 -1766 C ATOM 4949 CE3 TRP D 35 -1.515 114.367 8.897 1.00 40.21 C ANISOU 4949 CE3 TRP D 35 5544 6267 3467 759 -70 -1527 C ATOM 4950 CZ2 TRP D 35 -0.402 113.218 6.548 1.00 43.25 C ANISOU 4950 CZ2 TRP D 35 5988 6933 3512 1211 -129 -1682 C ATOM 4951 CZ3 TRP D 35 -0.751 115.125 7.997 1.00 40.49 C ANISOU 4951 CZ3 TRP D 35 5439 6543 3403 870 -19 -1441 C ATOM 4952 CH2 TRP D 35 -0.204 114.544 6.845 1.00 41.81 C ANISOU 4952 CH2 TRP D 35 5624 6864 3398 1091 -35 -1503 C ATOM 4953 N TYR D 36 -2.894 113.334 13.580 1.00 38.31 N ANISOU 4953 N TYR D 36 5567 5430 3557 332 -34 -1451 N ATOM 4954 CA TYR D 36 -3.478 113.851 14.821 1.00 37.25 C ANISOU 4954 CA TYR D 36 5425 5244 3484 212 31 -1375 C ATOM 4955 C TYR D 36 -4.006 115.253 14.608 1.00 36.49 C ANISOU 4955 C TYR D 36 5197 5251 3415 160 81 -1337 C ATOM 4956 O TYR D 36 -3.365 116.056 13.939 1.00 35.72 O ANISOU 4956 O TYR D 36 5014 5271 3288 217 75 -1321 O ATOM 4957 CB TYR D 36 -2.443 113.820 15.957 1.00 36.95 C ANISOU 4957 CB TYR D 36 5445 5186 3406 261 46 -1331 C ATOM 4958 CG TYR D 36 -1.982 112.414 16.168 1.00 37.60 C ANISOU 4958 CG TYR D 36 5666 5153 3469 322 -11 -1362 C ATOM 4959 CD1 TYR D 36 -2.727 111.531 16.943 1.00 37.98 C ANISOU 4959 CD1 TYR D 36 5819 5044 3566 234 -15 -1332 C ATOM 4960 CD2 TYR D 36 -0.857 111.924 15.505 1.00 38.00 C ANISOU 4960 CD2 TYR D 36 5735 5251 3454 477 -64 -1412 C ATOM 4961 CE1 TYR D 36 -2.335 110.214 17.094 1.00 39.04 C ANISOU 4961 CE1 TYR D 36 6096 5038 3700 287 -91 -1354 C ATOM 4962 CE2 TYR D 36 -0.458 110.606 15.658 1.00 39.00 C ANISOU 4962 CE2 TYR D 36 6005 5250 3563 560 -133 -1456 C ATOM 4963 CZ TYR D 36 -1.203 109.752 16.447 1.00 39.47 C ANISOU 4963 CZ TYR D 36 6189 5118 3688 458 -158 -1430 C ATOM 4964 OH TYR D 36 -0.817 108.440 16.590 1.00 40.40 O ANISOU 4964 OH TYR D 36 6467 5079 3807 536 -248 -1464 O ATOM 4965 N GLN D 37 -5.176 115.523 15.187 1.00 36.32 N ANISOU 4965 N GLN D 37 5156 5188 3454 59 130 -1306 N ATOM 4966 CA GLN D 37 -5.815 116.829 15.151 1.00 35.83 C ANISOU 4966 CA GLN D 37 4989 5201 3424 27 174 -1275 C ATOM 4967 C GLN D 37 -5.650 117.481 16.525 1.00 35.95 C ANISOU 4967 C GLN D 37 5044 5197 3420 35 226 -1236 C ATOM 4968 O GLN D 37 -5.845 116.821 17.555 1.00 36.60 O ANISOU 4968 O GLN D 37 5208 5216 3482 18 265 -1211 O ATOM 4969 CB GLN D 37 -7.300 116.663 14.814 1.00 36.13 C ANISOU 4969 CB GLN D 37 4966 5230 3533 -60 191 -1272 C ATOM 4970 CG GLN D 37 -8.086 117.959 14.756 1.00 35.75 C ANISOU 4970 CG GLN D 37 4806 5257 3519 -71 236 -1244 C ATOM 4971 CD GLN D 37 -9.578 117.740 14.667 1.00 36.21 C ANISOU 4971 CD GLN D 37 4782 5322 3655 -153 264 -1218 C ATOM 4972 OE1 GLN D 37 -10.203 118.204 13.727 1.00 36.56 O ANISOU 4972 OE1 GLN D 37 4729 5426 3737 -165 231 -1229 O ATOM 4973 NE2 GLN D 37 -10.155 117.035 15.633 1.00 36.57 N ANISOU 4973 NE2 GLN D 37 4852 5319 3725 -213 322 -1163 N ATOM 4974 N GLN D 38 -5.289 118.765 16.536 1.00 35.72 N ANISOU 4974 N GLN D 38 4966 5216 3392 66 212 -1225 N ATOM 4975 CA GLN D 38 -5.118 119.510 17.778 1.00 36.20 C ANISOU 4975 CA GLN D 38 5085 5245 3424 96 223 -1217 C ATOM 4976 C GLN D 38 -5.786 120.878 17.702 1.00 36.75 C ANISOU 4976 C GLN D 38 5095 5337 3532 107 224 -1221 C ATOM 4977 O GLN D 38 -5.362 121.750 16.943 1.00 36.39 O ANISOU 4977 O GLN D 38 4982 5313 3531 107 158 -1205 O ATOM 4978 CB GLN D 38 -3.636 119.662 18.138 1.00 36.03 C ANISOU 4978 CB GLN D 38 5110 5209 3371 138 143 -1210 C ATOM 4979 CG GLN D 38 -3.420 120.135 19.568 1.00 36.63 C ANISOU 4979 CG GLN D 38 5291 5231 3395 178 126 -1223 C ATOM 4980 CD GLN D 38 -1.949 120.316 19.933 1.00 36.56 C ANISOU 4980 CD GLN D 38 5313 5204 3373 205 15 -1210 C ATOM 4981 OE1 GLN D 38 -1.145 120.784 19.128 1.00 36.56 O ANISOU 4981 OE1 GLN D 38 5216 5244 3433 187 -57 -1171 O ATOM 4982 NE2 GLN D 38 -1.604 119.976 21.164 1.00 37.12 N ANISOU 4982 NE2 GLN D 38 5508 5231 3367 248 -1 -1225 N ATOM 4983 N HIS D 39 -6.832 121.051 18.505 1.00 38.13 N ANISOU 4983 N HIS D 39 5290 5511 3687 128 302 -1227 N ATOM 4984 CA HIS D 39 -7.442 122.358 18.712 1.00 39.15 C ANISOU 4984 CA HIS D 39 5397 5646 3831 186 300 -1249 C ATOM 4985 C HIS D 39 -6.670 123.105 19.805 1.00 41.05 C ANISOU 4985 C HIS D 39 5764 5820 4014 266 230 -1291 C ATOM 4986 O HIS D 39 -5.971 122.478 20.612 1.00 41.28 O ANISOU 4986 O HIS D 39 5890 5823 3971 278 221 -1294 O ATOM 4987 CB HIS D 39 -8.930 122.212 19.049 1.00 39.67 C ANISOU 4987 CB HIS D 39 5409 5775 3890 204 423 -1232 C ATOM 4988 CG HIS D 39 -9.769 121.816 17.872 1.00 39.34 C ANISOU 4988 CG HIS D 39 5227 5786 3933 123 442 -1199 C ATOM 4989 ND1 HIS D 39 -10.053 120.504 17.559 1.00 39.26 N ANISOU 4989 ND1 HIS D 39 5189 5780 3948 29 468 -1164 N ATOM 4990 CD2 HIS D 39 -10.372 122.567 16.921 1.00 39.16 C ANISOU 4990 CD2 HIS D 39 5097 5803 3980 124 414 -1199 C ATOM 4991 CE1 HIS D 39 -10.796 120.466 16.466 1.00 39.28 C ANISOU 4991 CE1 HIS D 39 5073 5824 4027 -26 445 -1156 C ATOM 4992 NE2 HIS D 39 -11.010 121.703 16.065 1.00 39.41 N ANISOU 4992 NE2 HIS D 39 5035 5875 4065 34 422 -1172 N ATOM 4993 N PRO D 40 -6.789 124.449 19.839 1.00 43.06 N ANISOU 4993 N PRO D 40 6029 6030 4301 324 155 -1328 N ATOM 4994 CA PRO D 40 -6.058 125.230 20.841 1.00 44.67 C ANISOU 4994 CA PRO D 40 6373 6140 4462 400 39 -1388 C ATOM 4995 C PRO D 40 -6.254 124.759 22.286 1.00 46.49 C ANISOU 4995 C PRO D 40 6741 6386 4539 501 108 -1435 C ATOM 4996 O PRO D 40 -7.389 124.542 22.729 1.00 48.67 O ANISOU 4996 O PRO D 40 7007 6743 4741 574 251 -1435 O ATOM 4997 CB PRO D 40 -6.616 126.646 20.651 1.00 45.30 C ANISOU 4997 CB PRO D 40 6451 6159 4600 468 -33 -1430 C ATOM 4998 CG PRO D 40 -7.018 126.687 19.217 1.00 44.23 C ANISOU 4998 CG PRO D 40 6151 6079 4574 381 -6 -1356 C ATOM 4999 CD PRO D 40 -7.583 125.326 18.951 1.00 43.17 C ANISOU 4999 CD PRO D 40 5942 6061 4401 329 147 -1319 C ATOM 5000 N GLY D 41 -5.140 124.559 22.988 1.00 47.39 N ANISOU 5000 N GLY D 41 6963 6442 4600 507 9 -1454 N ATOM 5001 CA GLY D 41 -5.153 124.175 24.394 1.00 49.14 C ANISOU 5001 CA GLY D 41 7338 6679 4654 616 48 -1494 C ATOM 5002 C GLY D 41 -5.531 122.736 24.697 1.00 49.51 C ANISOU 5002 C GLY D 41 7368 6818 4624 586 215 -1412 C ATOM 5003 O GLY D 41 -5.611 122.370 25.866 1.00 52.32 O ANISOU 5003 O GLY D 41 7844 7208 4828 680 267 -1415 O ATOM 5004 N LYS D 42 -5.754 121.920 23.667 1.00 48.58 N ANISOU 5004 N LYS D 42 7117 6732 4608 462 283 -1336 N ATOM 5005 CA LYS D 42 -6.249 120.551 23.826 1.00 48.47 C ANISOU 5005 CA LYS D 42 7082 6769 4563 410 415 -1249 C ATOM 5006 C LYS D 42 -5.167 119.549 23.477 1.00 46.39 C ANISOU 5006 C LYS D 42 6839 6453 4335 335 347 -1219 C ATOM 5007 O LYS D 42 -4.191 119.887 22.807 1.00 44.22 O ANISOU 5007 O LYS D 42 6535 6142 4127 309 230 -1248 O ATOM 5008 CB LYS D 42 -7.434 120.312 22.891 1.00 49.18 C ANISOU 5008 CB LYS D 42 7017 6916 4752 331 513 -1200 C ATOM 5009 CG LYS D 42 -8.670 121.152 23.193 1.00 51.15 C ANISOU 5009 CG LYS D 42 7213 7249 4973 418 607 -1208 C ATOM 5010 CD LYS D 42 -9.812 120.321 23.766 1.00 53.47 C ANISOU 5010 CD LYS D 42 7448 7648 5221 408 780 -1094 C ATOM 5011 CE LYS D 42 -10.409 119.384 22.720 1.00 53.80 C ANISOU 5011 CE LYS D 42 7343 7689 5409 239 803 -1011 C ATOM 5012 NZ LYS D 42 -11.696 118.788 23.180 1.00 56.26 N ANISOU 5012 NZ LYS D 42 7546 8111 5721 206 958 -873 N ATOM 5013 N ALA D 43 -5.365 118.309 23.924 1.00 45.58 N ANISOU 5013 N ALA D 43 6777 6350 4191 306 423 -1145 N ATOM 5014 CA ALA D 43 -4.509 117.195 23.538 1.00 44.10 C ANISOU 5014 CA ALA D 43 6614 6101 4040 253 366 -1118 C ATOM 5015 C ALA D 43 -4.738 116.818 22.074 1.00 42.71 C ANISOU 5015 C ALA D 43 6322 5914 3991 167 351 -1125 C ATOM 5016 O ALA D 43 -5.845 116.992 21.567 1.00 41.78 O ANISOU 5016 O ALA D 43 6111 5833 3932 115 414 -1111 O ATOM 5017 CB ALA D 43 -4.789 115.987 24.415 1.00 45.28 C ANISOU 5017 CB ALA D 43 6852 6228 4126 243 439 -1023 C ATOM 5018 N PRO D 44 -3.699 116.287 21.398 1.00 41.33 N ANISOU 5018 N PRO D 44 6152 5706 3846 170 264 -1147 N ATOM 5019 CA PRO D 44 -3.913 115.731 20.063 1.00 40.82 C ANISOU 5019 CA PRO D 44 6012 5634 3862 122 244 -1165 C ATOM 5020 C PRO D 44 -4.904 114.567 20.087 1.00 41.47 C ANISOU 5020 C PRO D 44 6121 5649 3986 44 287 -1120 C ATOM 5021 O PRO D 44 -4.978 113.835 21.082 1.00 42.55 O ANISOU 5021 O PRO D 44 6351 5729 4086 34 319 -1054 O ATOM 5022 CB PRO D 44 -2.517 115.251 19.645 1.00 40.62 C ANISOU 5022 CB PRO D 44 6015 5601 3819 190 157 -1191 C ATOM 5023 CG PRO D 44 -1.570 116.052 20.467 1.00 40.24 C ANISOU 5023 CG PRO D 44 5989 5580 3721 244 113 -1182 C ATOM 5024 CD PRO D 44 -2.272 116.278 21.771 1.00 41.16 C ANISOU 5024 CD PRO D 44 6191 5670 3779 238 171 -1160 C ATOM 5025 N LYS D 45 -5.653 114.430 19.000 1.00 40.88 N ANISOU 5025 N LYS D 45 5962 5579 3992 -19 275 -1144 N ATOM 5026 CA LYS D 45 -6.666 113.390 18.838 1.00 41.78 C ANISOU 5026 CA LYS D 45 6076 5613 4184 -124 275 -1098 C ATOM 5027 C LYS D 45 -6.402 112.653 17.527 1.00 41.28 C ANISOU 5027 C LYS D 45 6030 5489 4167 -119 156 -1184 C ATOM 5028 O LYS D 45 -6.342 113.279 16.469 1.00 40.22 O ANISOU 5028 O LYS D 45 5816 5435 4030 -84 126 -1252 O ATOM 5029 CB LYS D 45 -8.064 114.029 18.824 1.00 42.20 C ANISOU 5029 CB LYS D 45 5996 5744 4295 -202 356 -1047 C ATOM 5030 CG LYS D 45 -9.163 113.173 18.201 1.00 43.48 C ANISOU 5030 CG LYS D 45 6096 5844 4580 -335 314 -1008 C ATOM 5031 CD LYS D 45 -10.509 113.866 18.242 1.00 44.06 C ANISOU 5031 CD LYS D 45 6006 6026 4710 -397 402 -940 C ATOM 5032 CE LYS D 45 -11.538 113.088 17.437 1.00 45.38 C ANISOU 5032 CE LYS D 45 6088 6134 5022 -543 319 -908 C ATOM 5033 NZ LYS D 45 -12.810 113.849 17.330 1.00 46.12 N ANISOU 5033 NZ LYS D 45 5989 6359 5176 -588 395 -844 N ATOM 5034 N VAL D 46 -6.260 111.332 17.599 1.00 42.28 N ANISOU 5034 N VAL D 46 6271 5469 4325 -141 82 -1179 N ATOM 5035 CA VAL D 46 -6.012 110.513 16.396 1.00 42.93 C ANISOU 5035 CA VAL D 46 6410 5469 4431 -101 -55 -1287 C ATOM 5036 C VAL D 46 -7.173 110.585 15.383 1.00 43.38 C ANISOU 5036 C VAL D 46 6375 5533 4576 -197 -109 -1321 C ATOM 5037 O VAL D 46 -8.328 110.368 15.735 1.00 44.82 O ANISOU 5037 O VAL D 46 6500 5666 4864 -349 -94 -1231 O ATOM 5038 CB VAL D 46 -5.652 109.040 16.742 1.00 44.30 C ANISOU 5038 CB VAL D 46 6755 5441 4634 -94 -155 -1282 C ATOM 5039 CG1 VAL D 46 -6.795 108.297 17.443 1.00 45.71 C ANISOU 5039 CG1 VAL D 46 6947 5480 4939 -281 -159 -1149 C ATOM 5040 CG2 VAL D 46 -5.198 108.293 15.489 1.00 45.37 C ANISOU 5040 CG2 VAL D 46 6980 5502 4756 14 -309 -1434 C ATOM 5041 N MET D 47 -6.841 110.914 14.134 1.00 43.01 N ANISOU 5041 N MET D 47 6300 5566 4476 -102 -170 -1435 N ATOM 5042 CA MET D 47 -7.811 110.955 13.026 1.00 43.80 C ANISOU 5042 CA MET D 47 6330 5678 4633 -162 -253 -1491 C ATOM 5043 C MET D 47 -7.607 109.847 11.980 1.00 45.12 C ANISOU 5043 C MET D 47 6630 5726 4786 -91 -438 -1631 C ATOM 5044 O MET D 47 -8.575 109.406 11.348 1.00 46.16 O ANISOU 5044 O MET D 47 6756 5775 5006 -187 -564 -1670 O ATOM 5045 CB MET D 47 -7.737 112.311 12.326 1.00 42.88 C ANISOU 5045 CB MET D 47 6078 5765 4449 -97 -187 -1506 C ATOM 5046 CG MET D 47 -7.889 113.516 13.249 1.00 42.03 C ANISOU 5046 CG MET D 47 5863 5757 4347 -133 -38 -1401 C ATOM 5047 SD MET D 47 -9.469 113.606 14.120 1.00 43.06 S ANISOU 5047 SD MET D 47 5896 5860 4604 -305 34 -1285 S ATOM 5048 CE MET D 47 -10.560 113.997 12.762 1.00 43.20 C ANISOU 5048 CE MET D 47 5780 5949 4686 -354 -45 -1327 C ATOM 5049 N ILE D 48 -6.356 109.431 11.774 1.00 45.03 N ANISOU 5049 N ILE D 48 6735 5714 4659 92 -467 -1713 N ATOM 5050 CA ILE D 48 -6.008 108.364 10.823 1.00 46.61 C ANISOU 5050 CA ILE D 48 7095 5807 4810 225 -644 -1872 C ATOM 5051 C ILE D 48 -4.893 107.511 11.424 1.00 47.25 C ANISOU 5051 C ILE D 48 7328 5781 4842 356 -663 -1891 C ATOM 5052 O ILE D 48 -4.025 108.035 12.112 1.00 45.92 O ANISOU 5052 O ILE D 48 7110 5724 4611 419 -532 -1815 O ATOM 5053 CB ILE D 48 -5.504 108.945 9.475 1.00 46.30 C ANISOU 5053 CB ILE D 48 7009 5977 4607 418 -649 -1980 C ATOM 5054 CG1 ILE D 48 -6.590 109.773 8.768 1.00 46.03 C ANISOU 5054 CG1 ILE D 48 6833 6047 4609 310 -652 -1966 C ATOM 5055 CG2 ILE D 48 -5.006 107.846 8.542 1.00 48.36 C ANISOU 5055 CG2 ILE D 48 7456 6152 4765 622 -822 -2165 C ATOM 5056 CD1 ILE D 48 -7.771 108.977 8.238 1.00 47.76 C ANISOU 5056 CD1 ILE D 48 7117 6091 4938 192 -848 -2046 C ATOM 5057 N TYR D 49 -4.927 106.205 11.172 1.00 49.86 N ANISOU 5057 N TYR D 49 7850 5883 5210 397 -847 -1993 N ATOM 5058 CA TYR D 49 -3.814 105.318 11.513 1.00 51.16 C ANISOU 5058 CA TYR D 49 8182 5943 5314 576 -896 -2043 C ATOM 5059 C TYR D 49 -3.585 104.314 10.390 1.00 53.65 C ANISOU 5059 C TYR D 49 8689 6136 5560 774 -1108 -2257 C ATOM 5060 O TYR D 49 -4.441 104.143 9.517 1.00 54.64 O ANISOU 5060 O TYR D 49 8842 6197 5720 720 -1248 -2356 O ATOM 5061 CB TYR D 49 -4.074 104.616 12.850 1.00 52.07 C ANISOU 5061 CB TYR D 49 8379 5834 5573 411 -907 -1906 C ATOM 5062 CG TYR D 49 -5.168 103.572 12.802 1.00 54.40 C ANISOU 5062 CG TYR D 49 8789 5832 6049 228 -1103 -1907 C ATOM 5063 CD1 TYR D 49 -6.514 103.938 12.841 1.00 54.47 C ANISOU 5063 CD1 TYR D 49 8660 5836 6199 -29 -1095 -1807 C ATOM 5064 CD2 TYR D 49 -4.857 102.215 12.727 1.00 56.89 C ANISOU 5064 CD2 TYR D 49 9344 5862 6410 309 -1312 -1996 C ATOM 5065 CE1 TYR D 49 -7.518 102.980 12.795 1.00 56.89 C ANISOU 5065 CE1 TYR D 49 9042 5872 6700 -225 -1292 -1778 C ATOM 5066 CE2 TYR D 49 -5.853 101.250 12.685 1.00 59.22 C ANISOU 5066 CE2 TYR D 49 9746 5851 6903 114 -1527 -1979 C ATOM 5067 CZ TYR D 49 -7.180 101.639 12.721 1.00 59.21 C ANISOU 5067 CZ TYR D 49 9582 5862 7053 -166 -1516 -1860 C ATOM 5068 OH TYR D 49 -8.163 100.687 12.673 1.00 62.02 O ANISOU 5068 OH TYR D 49 10015 5920 7631 -384 -1745 -1816 O ATOM 5069 N ASP D 50 -2.423 103.663 10.409 1.00 54.64 N ANISOU 5069 N ASP D 50 8949 6235 5578 1022 -1141 -2336 N ATOM 5070 CA ASP D 50 -2.001 102.749 9.338 1.00 56.71 C ANISOU 5070 CA ASP D 50 9410 6413 5723 1296 -1330 -2564 C ATOM 5071 C ASP D 50 -2.212 103.371 7.948 1.00 56.83 C ANISOU 5071 C ASP D 50 9349 6655 5588 1417 -1334 -2686 C ATOM 5072 O ASP D 50 -2.845 102.768 7.071 1.00 58.53 O ANISOU 5072 O ASP D 50 9709 6728 5803 1450 -1547 -2855 O ATOM 5073 CB ASP D 50 -2.735 101.396 9.436 1.00 59.42 C ANISOU 5073 CB ASP D 50 9999 6343 6236 1192 -1605 -2646 C ATOM 5074 CG ASP D 50 -2.321 100.570 10.647 1.00 59.97 C ANISOU 5074 CG ASP D 50 10194 6177 6416 1150 -1631 -2543 C ATOM 5075 OD1 ASP D 50 -1.332 100.903 11.339 1.00 58.89 O ANISOU 5075 OD1 ASP D 50 9986 6192 6195 1259 -1461 -2450 O ATOM 5076 OD2 ASP D 50 -2.996 99.552 10.896 1.00 62.14 O ANISOU 5076 OD2 ASP D 50 10641 6100 6870 1003 -1844 -2546 O ATOM 5077 N VAL D 51 -1.717 104.597 7.774 1.00 54.65 N ANISOU 5077 N VAL D 51 8848 6722 5193 1468 -1116 -2588 N ATOM 5078 CA VAL D 51 -1.815 105.362 6.513 1.00 54.54 C ANISOU 5078 CA VAL D 51 8728 6976 5019 1585 -1078 -2649 C ATOM 5079 C VAL D 51 -3.228 105.851 6.157 1.00 54.04 C ANISOU 5079 C VAL D 51 8590 6873 5069 1334 -1137 -2633 C ATOM 5080 O VAL D 51 -3.417 107.044 5.930 1.00 51.87 O ANISOU 5080 O VAL D 51 8111 6832 4764 1263 -991 -2523 O ATOM 5081 CB VAL D 51 -1.227 104.596 5.298 1.00 57.08 C ANISOU 5081 CB VAL D 51 9225 7346 5116 1953 -1212 -2878 C ATOM 5082 CG1 VAL D 51 -1.259 105.465 4.044 1.00 57.26 C ANISOU 5082 CG1 VAL D 51 9120 7694 4942 2087 -1143 -2903 C ATOM 5083 CG2 VAL D 51 0.196 104.131 5.587 1.00 57.80 C ANISOU 5083 CG2 VAL D 51 9365 7514 5083 2240 -1145 -2890 C ATOM 5084 N SER D 52 -4.193 104.932 6.077 1.00 56.02 N ANISOU 5084 N SER D 52 9001 6826 5457 1206 -1365 -2733 N ATOM 5085 CA SER D 52 -5.529 105.222 5.546 1.00 56.70 C ANISOU 5085 CA SER D 52 9026 6873 5643 1004 -1470 -2746 C ATOM 5086 C SER D 52 -6.737 104.855 6.425 1.00 57.24 C ANISOU 5086 C SER D 52 9076 6672 6000 650 -1557 -2633 C ATOM 5087 O SER D 52 -7.859 105.203 6.067 1.00 57.17 O ANISOU 5087 O SER D 52 8967 6665 6090 469 -1622 -2609 O ATOM 5088 CB SER D 52 -5.670 104.513 4.197 1.00 59.59 C ANISOU 5088 CB SER D 52 9585 7182 5873 1212 -1720 -2999 C ATOM 5089 OG SER D 52 -5.460 103.121 4.339 1.00 62.04 O ANISOU 5089 OG SER D 52 10166 7172 6233 1297 -1945 -3147 O ATOM 5090 N LYS D 53 -6.544 104.159 7.546 1.00 57.79 N ANISOU 5090 N LYS D 53 9226 6528 6201 553 -1557 -2546 N ATOM 5091 CA LYS D 53 -7.685 103.720 8.361 1.00 58.85 C ANISOU 5091 CA LYS D 53 9335 6423 6604 223 -1637 -2407 C ATOM 5092 C LYS D 53 -8.163 104.825 9.300 1.00 56.72 C ANISOU 5092 C LYS D 53 8810 6331 6411 18 -1382 -2171 C ATOM 5093 O LYS D 53 -7.353 105.567 9.862 1.00 54.88 O ANISOU 5093 O LYS D 53 8494 6286 6071 109 -1163 -2093 O ATOM 5094 CB LYS D 53 -7.341 102.461 9.154 1.00 60.80 C ANISOU 5094 CB LYS D 53 9786 6357 6959 203 -1759 -2389 C ATOM 5095 CG LYS D 53 -7.066 101.261 8.268 1.00 64.19 C ANISOU 5095 CG LYS D 53 10499 6540 7349 390 -2065 -2635 C ATOM 5096 CD LYS D 53 -6.690 100.048 9.093 1.00 66.25 C ANISOU 5096 CD LYS D 53 10971 6472 7730 377 -2190 -2603 C ATOM 5097 CE LYS D 53 -6.222 98.906 8.215 1.00 69.40 C ANISOU 5097 CE LYS D 53 11683 6631 8056 636 -2493 -2879 C ATOM 5098 NZ LYS D 53 -5.705 97.797 9.057 1.00 71.31 N ANISOU 5098 NZ LYS D 53 12134 6561 8400 660 -2599 -2839 N ATOM 5099 N ARG D 54 -9.483 104.919 9.462 1.00 57.27 N ANISOU 5099 N ARG D 54 8755 6338 6667 -248 -1426 -2062 N ATOM 5100 CA ARG D 54 -10.109 105.874 10.374 1.00 55.80 C ANISOU 5100 CA ARG D 54 8336 6306 6560 -429 -1202 -1844 C ATOM 5101 C ARG D 54 -10.507 105.171 11.671 1.00 56.45 C ANISOU 5101 C ARG D 54 8431 6202 6816 -631 -1182 -1651 C ATOM 5102 O ARG D 54 -11.108 104.098 11.625 1.00 58.40 O ANISOU 5102 O ARG D 54 8766 6189 7233 -779 -1392 -1636 O ATOM 5103 CB ARG D 54 -11.363 106.492 9.748 1.00 56.48 C ANISOU 5103 CB ARG D 54 8238 6490 6733 -574 -1238 -1818 C ATOM 5104 CG ARG D 54 -11.124 107.821 9.061 1.00 54.92 C ANISOU 5104 CG ARG D 54 7911 6585 6371 -432 -1102 -1867 C ATOM 5105 CD ARG D 54 -12.402 108.323 8.419 1.00 56.00 C ANISOU 5105 CD ARG D 54 7879 6796 6602 -567 -1168 -1844 C ATOM 5106 NE ARG D 54 -12.742 107.532 7.236 1.00 58.59 N ANISOU 5106 NE ARG D 54 8330 6990 6942 -546 -1457 -2019 N ATOM 5107 CZ ARG D 54 -13.819 106.753 7.083 1.00 61.58 C ANISOU 5107 CZ ARG D 54 8703 7173 7523 -752 -1682 -2006 C ATOM 5108 NH1 ARG D 54 -14.753 106.633 8.032 1.00 62.60 N ANISOU 5108 NH1 ARG D 54 8675 7236 7874 -1013 -1632 -1791 N ATOM 5109 NH2 ARG D 54 -13.977 106.096 5.937 1.00 63.64 N ANISOU 5109 NH2 ARG D 54 9110 7311 7759 -690 -1971 -2204 N ATOM 5110 N PRO D 55 -10.196 105.779 12.832 1.00 54.37 N ANISOU 5110 N PRO D 55 8079 6068 6510 -641 -942 -1494 N ATOM 5111 CA PRO D 55 -10.807 105.311 14.079 1.00 55.24 C ANISOU 5111 CA PRO D 55 8149 6072 6769 -845 -883 -1266 C ATOM 5112 C PRO D 55 -12.329 105.486 14.078 1.00 56.29 C ANISOU 5112 C PRO D 55 8075 6232 7082 -1090 -891 -1119 C ATOM 5113 O PRO D 55 -12.849 106.323 13.331 1.00 55.42 O ANISOU 5113 O PRO D 55 7822 6285 6952 -1082 -873 -1179 O ATOM 5114 CB PRO D 55 -10.172 106.216 15.147 1.00 53.07 C ANISOU 5114 CB PRO D 55 7811 5998 6356 -754 -618 -1168 C ATOM 5115 CG PRO D 55 -8.912 106.709 14.538 1.00 51.43 C ANISOU 5115 CG PRO D 55 7678 5901 5961 -505 -600 -1348 C ATOM 5116 CD PRO D 55 -9.204 106.840 13.076 1.00 51.92 C ANISOU 5116 CD PRO D 55 7722 5993 6014 -458 -737 -1513 C ATOM 5117 N SER D 56 -13.020 104.717 14.921 1.00 58.47 N ANISOU 5117 N SER D 56 8322 6363 7532 -1303 -913 -906 N ATOM 5118 CA SER D 56 -14.480 104.826 15.058 1.00 60.16 C ANISOU 5118 CA SER D 56 8299 6626 7934 -1549 -903 -712 C ATOM 5119 C SER D 56 -14.811 106.257 15.542 1.00 58.15 C ANISOU 5119 C SER D 56 7820 6709 7566 -1488 -612 -628 C ATOM 5120 O SER D 56 -14.083 106.838 16.367 1.00 56.63 O ANISOU 5120 O SER D 56 7661 6646 7209 -1345 -407 -605 O ATOM 5121 CB SER D 56 -15.069 103.720 15.981 1.00 63.21 C ANISOU 5121 CB SER D 56 8678 6812 8524 -1791 -958 -446 C ATOM 5122 OG SER D 56 -15.003 104.092 17.347 1.00 62.85 O ANISOU 5122 OG SER D 56 8552 6931 8399 -1783 -681 -226 O ATOM 5123 N GLY D 57 -15.847 106.852 14.953 1.00 58.29 N ANISOU 5123 N GLY D 57 7627 6857 7665 -1572 -620 -609 N ATOM 5124 CA GLY D 57 -16.264 108.222 15.282 1.00 56.45 C ANISOU 5124 CA GLY D 57 7187 6924 7339 -1497 -378 -549 C ATOM 5125 C GLY D 57 -15.639 109.336 14.448 1.00 53.83 C ANISOU 5125 C GLY D 57 6881 6736 6835 -1285 -346 -765 C ATOM 5126 O GLY D 57 -16.176 110.446 14.415 1.00 53.26 O ANISOU 5126 O GLY D 57 6635 6873 6730 -1241 -217 -737 O ATOM 5127 N VAL D 58 -14.514 109.065 13.782 1.00 52.23 N ANISOU 5127 N VAL D 58 6887 6433 6523 -1143 -461 -964 N ATOM 5128 CA VAL D 58 -13.881 110.049 12.901 1.00 49.70 C ANISOU 5128 CA VAL D 58 6582 6257 6047 -954 -441 -1137 C ATOM 5129 C VAL D 58 -14.690 110.121 11.600 1.00 50.08 C ANISOU 5129 C VAL D 58 6545 6318 6164 -1004 -612 -1224 C ATOM 5130 O VAL D 58 -14.900 109.088 10.960 1.00 51.60 O ANISOU 5130 O VAL D 58 6832 6328 6445 -1079 -842 -1297 O ATOM 5131 CB VAL D 58 -12.403 109.701 12.619 1.00 48.79 C ANISOU 5131 CB VAL D 58 6686 6069 5782 -772 -492 -1291 C ATOM 5132 CG1 VAL D 58 -11.813 110.616 11.548 1.00 47.40 C ANISOU 5132 CG1 VAL D 58 6500 6051 5459 -595 -490 -1436 C ATOM 5133 CG2 VAL D 58 -11.600 109.795 13.914 1.00 47.87 C ANISOU 5133 CG2 VAL D 58 6633 5966 5589 -714 -327 -1204 C ATOM 5134 N PRO D 59 -15.150 111.331 11.209 1.00 48.58 N ANISOU 5134 N PRO D 59 6190 6332 5935 -955 -523 -1220 N ATOM 5135 CA PRO D 59 -15.963 111.454 9.990 1.00 49.42 C ANISOU 5135 CA PRO D 59 6207 6472 6099 -996 -689 -1290 C ATOM 5136 C PRO D 59 -15.240 111.003 8.710 1.00 49.55 C ANISOU 5136 C PRO D 59 6408 6417 6003 -868 -888 -1505 C ATOM 5137 O PRO D 59 -14.022 111.150 8.590 1.00 47.97 O ANISOU 5137 O PRO D 59 6346 6246 5633 -688 -832 -1598 O ATOM 5138 CB PRO D 59 -16.295 112.952 9.924 1.00 47.95 C ANISOU 5138 CB PRO D 59 5846 6519 5852 -913 -527 -1247 C ATOM 5139 CG PRO D 59 -16.084 113.467 11.304 1.00 46.89 C ANISOU 5139 CG PRO D 59 5674 6452 5691 -890 -291 -1120 C ATOM 5140 CD PRO D 59 -15.009 112.625 11.905 1.00 46.67 C ANISOU 5140 CD PRO D 59 5846 6281 5605 -861 -289 -1148 C ATOM 5141 N ASP D 60 -16.007 110.468 7.764 1.00 51.59 N ANISOU 5141 N ASP D 60 6658 6597 6348 -950 -1124 -1578 N ATOM 5142 CA ASP D 60 -15.441 109.940 6.514 1.00 52.45 C ANISOU 5142 CA ASP D 60 6960 6638 6331 -807 -1341 -1800 C ATOM 5143 C ASP D 60 -14.849 111.000 5.569 1.00 51.15 C ANISOU 5143 C ASP D 60 6787 6704 5944 -584 -1269 -1893 C ATOM 5144 O ASP D 60 -14.181 110.649 4.603 1.00 51.95 O ANISOU 5144 O ASP D 60 7053 6804 5884 -410 -1395 -2064 O ATOM 5145 CB ASP D 60 -16.461 109.058 5.777 1.00 55.46 C ANISOU 5145 CB ASP D 60 7353 6852 6867 -958 -1654 -1864 C ATOM 5146 CG ASP D 60 -17.741 109.800 5.392 1.00 55.99 C ANISOU 5146 CG ASP D 60 7168 7064 7043 -1080 -1677 -1775 C ATOM 5147 OD1 ASP D 60 -17.782 111.048 5.444 1.00 54.29 O ANISOU 5147 OD1 ASP D 60 6800 7083 6746 -998 -1471 -1705 O ATOM 5148 OD2 ASP D 60 -18.717 109.116 5.038 1.00 58.52 O ANISOU 5148 OD2 ASP D 60 7442 7249 7545 -1260 -1923 -1772 O ATOM 5149 N ARG D 61 -15.087 112.285 5.843 1.00 49.65 N ANISOU 5149 N ARG D 61 6413 6712 5740 -576 -1072 -1773 N ATOM 5150 CA ARG D 61 -14.425 113.365 5.094 1.00 48.42 C ANISOU 5150 CA ARG D 61 6242 6764 5391 -382 -983 -1811 C ATOM 5151 C ARG D 61 -12.901 113.438 5.301 1.00 47.14 C ANISOU 5151 C ARG D 61 6210 6641 5060 -206 -861 -1845 C ATOM 5152 O ARG D 61 -12.212 114.070 4.498 1.00 46.28 O ANISOU 5152 O ARG D 61 6111 6693 4780 -38 -827 -1879 O ATOM 5153 CB ARG D 61 -15.088 114.724 5.368 1.00 47.45 C ANISOU 5153 CB ARG D 61 5904 6804 5321 -421 -831 -1672 C ATOM 5154 CG ARG D 61 -14.910 115.300 6.765 1.00 46.11 C ANISOU 5154 CG ARG D 61 5666 6648 5208 -460 -607 -1536 C ATOM 5155 CD ARG D 61 -15.525 116.691 6.872 1.00 45.65 C ANISOU 5155 CD ARG D 61 5427 6741 5177 -445 -489 -1436 C ATOM 5156 NE ARG D 61 -15.433 117.220 8.234 1.00 44.41 N ANISOU 5156 NE ARG D 61 5226 6589 5059 -458 -297 -1331 N ATOM 5157 CZ ARG D 61 -16.312 116.968 9.214 1.00 45.14 C ANISOU 5157 CZ ARG D 61 5219 6654 5277 -573 -228 -1231 C ATOM 5158 NH1 ARG D 61 -16.127 117.504 10.417 1.00 44.48 N ANISOU 5158 NH1 ARG D 61 5124 6597 5180 -538 -52 -1155 N ATOM 5159 NH2 ARG D 61 -17.372 116.177 9.022 1.00 46.86 N ANISOU 5159 NH2 ARG D 61 5345 6826 5634 -720 -338 -1198 N ATOM 5160 N PHE D 62 -12.392 112.811 6.369 1.00 47.07 N ANISOU 5160 N PHE D 62 6284 6500 5101 -248 -797 -1813 N ATOM 5161 CA PHE D 62 -10.950 112.636 6.583 1.00 46.62 C ANISOU 5161 CA PHE D 62 6355 6456 4903 -86 -720 -1852 C ATOM 5162 C PHE D 62 -10.451 111.344 5.939 1.00 48.55 C ANISOU 5162 C PHE D 62 6805 6571 5071 23 -904 -2019 C ATOM 5163 O PHE D 62 -10.955 110.260 6.252 1.00 49.92 O ANISOU 5163 O PHE D 62 7071 6523 5373 -93 -1046 -2054 O ATOM 5164 CB PHE D 62 -10.629 112.604 8.080 1.00 45.64 C ANISOU 5164 CB PHE D 62 6229 6257 4856 -165 -573 -1738 C ATOM 5165 CG PHE D 62 -10.910 113.896 8.782 1.00 44.14 C ANISOU 5165 CG PHE D 62 5878 6190 4701 -214 -396 -1603 C ATOM 5166 CD1 PHE D 62 -12.165 114.150 9.327 1.00 44.71 C ANISOU 5166 CD1 PHE D 62 5821 6251 4918 -368 -361 -1507 C ATOM 5167 CD2 PHE D 62 -9.923 114.866 8.896 1.00 42.77 C ANISOU 5167 CD2 PHE D 62 5682 6145 4423 -98 -276 -1568 C ATOM 5168 CE1 PHE D 62 -12.427 115.350 9.972 1.00 43.53 C ANISOU 5168 CE1 PHE D 62 5545 6212 4782 -371 -206 -1407 C ATOM 5169 CE2 PHE D 62 -10.176 116.067 9.541 1.00 41.57 C ANISOU 5169 CE2 PHE D 62 5414 6071 4309 -131 -150 -1466 C ATOM 5170 CZ PHE D 62 -11.428 116.308 10.083 1.00 42.23 C ANISOU 5170 CZ PHE D 62 5395 6138 4513 -250 -114 -1399 C ATOM 5171 N SER D 63 -9.460 111.459 5.056 1.00 48.81 N ANISOU 5171 N SER D 63 6909 6741 4896 255 -904 -2112 N ATOM 5172 CA SER D 63 -8.834 110.294 4.431 1.00 50.89 C ANISOU 5172 CA SER D 63 7384 6909 5041 431 -1064 -2291 C ATOM 5173 C SER D 63 -7.304 110.436 4.403 1.00 50.55 C ANISOU 5173 C SER D 63 7382 7017 4809 669 -931 -2293 C ATOM 5174 O SER D 63 -6.764 111.548 4.409 1.00 49.06 O ANISOU 5174 O SER D 63 7047 7048 4548 715 -755 -2171 O ATOM 5175 CB SER D 63 -9.413 110.063 3.033 1.00 52.88 C ANISOU 5175 CB SER D 63 7697 7196 5200 516 -1266 -2444 C ATOM 5176 OG SER D 63 -10.757 109.608 3.107 1.00 54.26 O ANISOU 5176 OG SER D 63 7858 7179 5578 288 -1445 -2457 O ATOM 5177 N GLY D 64 -6.614 109.297 4.424 1.00 51.68 N ANISOU 5177 N GLY D 64 7716 7028 4890 813 -1027 -2418 N ATOM 5178 CA GLY D 64 -5.157 109.253 4.442 1.00 51.74 C ANISOU 5178 CA GLY D 64 7757 7173 4729 1054 -916 -2420 C ATOM 5179 C GLY D 64 -4.622 108.464 3.260 1.00 54.25 C ANISOU 5179 C GLY D 64 8246 7539 4826 1359 -1053 -2624 C ATOM 5180 O GLY D 64 -5.267 107.529 2.785 1.00 56.39 O ANISOU 5180 O GLY D 64 8696 7609 5119 1369 -1284 -2798 O ATOM 5181 N SER D 65 -3.446 108.856 2.784 1.00 54.50 N ANISOU 5181 N SER D 65 8219 7845 4644 1616 -917 -2595 N ATOM 5182 CA SER D 65 -2.785 108.183 1.673 1.00 57.48 C ANISOU 5182 CA SER D 65 8744 8336 4759 1972 -1004 -2776 C ATOM 5183 C SER D 65 -1.276 108.298 1.795 1.00 57.15 C ANISOU 5183 C SER D 65 8631 8523 4560 2219 -827 -2696 C ATOM 5184 O SER D 65 -0.768 109.013 2.659 1.00 55.28 O ANISOU 5184 O SER D 65 8218 8364 4423 2091 -652 -2495 O ATOM 5185 CB SER D 65 -3.257 108.775 0.337 1.00 58.85 C ANISOU 5185 CB SER D 65 8867 8734 4757 2070 -1035 -2816 C ATOM 5186 OG SER D 65 -3.007 110.172 0.295 1.00 57.92 O ANISOU 5186 OG SER D 65 8488 8901 4619 2002 -815 -2581 O ATOM 5187 N LYS D 66 -0.573 107.587 0.918 1.00 59.37 N ANISOU 5187 N LYS D 66 9048 8917 4591 2585 -886 -2859 N ATOM 5188 CA LYS D 66 0.881 107.627 0.875 1.00 60.15 C ANISOU 5188 CA LYS D 66 9060 9282 4512 2870 -720 -2784 C ATOM 5189 C LYS D 66 1.419 107.451 -0.539 1.00 62.69 C ANISOU 5189 C LYS D 66 9428 9910 4483 3285 -716 -2899 C ATOM 5190 O LYS D 66 0.849 106.709 -1.342 1.00 65.30 O ANISOU 5190 O LYS D 66 9990 10128 4694 3437 -922 -3146 O ATOM 5191 CB LYS D 66 1.468 106.541 1.772 1.00 60.61 C ANISOU 5191 CB LYS D 66 9278 9098 4652 2943 -788 -2868 C ATOM 5192 CG LYS D 66 2.924 106.782 2.123 1.00 60.44 C ANISOU 5192 CG LYS D 66 9092 9332 4539 3132 -592 -2717 C ATOM 5193 CD LYS D 66 3.429 105.797 3.168 1.00 60.65 C ANISOU 5193 CD LYS D 66 9263 9099 4681 3161 -661 -2771 C ATOM 5194 CE LYS D 66 4.154 104.626 2.531 1.00 63.98 C ANISOU 5194 CE LYS D 66 9897 9531 4883 3602 -764 -2992 C ATOM 5195 NZ LYS D 66 4.643 103.665 3.553 1.00 64.36 N ANISOU 5195 NZ LYS D 66 10092 9309 5052 3635 -844 -3035 N ATOM 5196 N SER D 67 2.521 108.147 -0.814 1.00 62.81 N ANISOU 5196 N SER D 67 9214 10317 4335 3464 -488 -2707 N ATOM 5197 CA SER D 67 3.209 108.119 -2.102 1.00 65.67 C ANISOU 5197 CA SER D 67 9555 11064 4331 3885 -417 -2745 C ATOM 5198 C SER D 67 4.703 108.269 -1.837 1.00 65.97 C ANISOU 5198 C SER D 67 9392 11400 4274 4097 -202 -2561 C ATOM 5199 O SER D 67 5.136 109.317 -1.351 1.00 64.09 O ANISOU 5199 O SER D 67 8863 11328 4161 3893 -20 -2263 O ATOM 5200 CB SER D 67 2.721 109.273 -2.986 1.00 65.51 C ANISOU 5200 CB SER D 67 9359 11318 4213 3808 -328 -2592 C ATOM 5201 OG SER D 67 3.347 109.247 -4.260 1.00 68.90 O ANISOU 5201 OG SER D 67 9770 12149 4260 4229 -250 -2612 O ATOM 5202 N GLY D 68 5.479 107.227 -2.145 1.00 68.76 N ANISOU 5202 N GLY D 68 9898 11811 4417 4507 -240 -2738 N ATOM 5203 CA GLY D 68 6.912 107.199 -1.839 1.00 69.60 C ANISOU 5203 CA GLY D 68 9817 12186 4442 4736 -56 -2580 C ATOM 5204 C GLY D 68 7.176 107.469 -0.364 1.00 66.94 C ANISOU 5204 C GLY D 68 9353 11642 4439 4393 -15 -2405 C ATOM 5205 O GLY D 68 6.686 106.739 0.499 1.00 65.49 O ANISOU 5205 O GLY D 68 9385 11040 4456 4232 -180 -2557 O ATOM 5206 N ASN D 69 7.910 108.545 -0.082 1.00 66.08 N ANISOU 5206 N ASN D 69 8896 11820 4392 4270 192 -2077 N ATOM 5207 CA ASN D 69 8.174 108.984 1.294 1.00 63.85 C ANISOU 5207 CA ASN D 69 8476 11372 4414 3937 225 -1896 C ATOM 5208 C ASN D 69 7.239 110.102 1.783 1.00 60.60 C ANISOU 5208 C ASN D 69 7966 10810 4249 3472 223 -1751 C ATOM 5209 O ASN D 69 7.545 110.770 2.770 1.00 59.04 O ANISOU 5209 O ASN D 69 7603 10564 4264 3214 276 -1558 O ATOM 5210 CB ASN D 69 9.627 109.453 1.426 1.00 65.09 C ANISOU 5210 CB ASN D 69 8308 11902 4521 4076 413 -1623 C ATOM 5211 CG ASN D 69 10.629 108.393 1.010 1.00 68.57 C ANISOU 5211 CG ASN D 69 8810 12528 4716 4565 436 -1744 C ATOM 5212 OD1 ASN D 69 10.504 107.227 1.380 1.00 69.54 O ANISOU 5212 OD1 ASN D 69 9220 12358 4844 4701 285 -2002 O ATOM 5213 ND2 ASN D 69 11.639 108.797 0.251 1.00 70.85 N ANISOU 5213 ND2 ASN D 69 8820 13307 4791 4838 626 -1541 N ATOM 5214 N THR D 70 6.107 110.306 1.109 1.00 60.24 N ANISOU 5214 N THR D 70 8027 10689 4171 3381 150 -1853 N ATOM 5215 CA THR D 70 5.170 111.369 1.470 1.00 57.59 C ANISOU 5215 CA THR D 70 7602 10231 4049 2986 149 -1727 C ATOM 5216 C THR D 70 3.806 110.789 1.813 1.00 56.45 C ANISOU 5216 C THR D 70 7717 9686 4046 2793 -37 -1951 C ATOM 5217 O THR D 70 3.200 110.086 1.004 1.00 58.90 O ANISOU 5217 O THR D 70 8226 9931 4222 2944 -165 -2169 O ATOM 5218 CB THR D 70 5.036 112.399 0.332 1.00 58.36 C ANISOU 5218 CB THR D 70 7518 10652 4004 3017 249 -1567 C ATOM 5219 OG1 THR D 70 6.332 112.913 0.017 1.00 59.73 O ANISOU 5219 OG1 THR D 70 7421 11214 4058 3185 427 -1317 O ATOM 5220 CG2 THR D 70 4.137 113.563 0.733 1.00 55.76 C ANISOU 5220 CG2 THR D 70 7089 10195 3904 2629 246 -1425 C ATOM 5221 N ALA D 71 3.339 111.083 3.019 1.00 53.93 N ANISOU 5221 N ALA D 71 7390 9109 3994 2466 -60 -1888 N ATOM 5222 CA ALA D 71 1.969 110.801 3.420 1.00 52.61 C ANISOU 5222 CA ALA D 71 7388 8608 3994 2223 -200 -2018 C ATOM 5223 C ALA D 71 1.128 112.053 3.187 1.00 51.00 C ANISOU 5223 C ALA D 71 7033 8470 3874 1990 -153 -1885 C ATOM 5224 O ALA D 71 1.649 113.171 3.203 1.00 50.37 O ANISOU 5224 O ALA D 71 6733 8598 3808 1932 -21 -1669 O ATOM 5225 CB ALA D 71 1.919 110.386 4.882 1.00 51.06 C ANISOU 5225 CB ALA D 71 7267 8123 4012 2031 -235 -2011 C ATOM 5226 N SER D 72 -0.170 111.857 2.976 1.00 50.52 N ANISOU 5226 N SER D 72 7088 8224 3884 1854 -277 -2008 N ATOM 5227 CA SER D 72 -1.112 112.967 2.812 1.00 49.23 C ANISOU 5227 CA SER D 72 6797 8089 3817 1637 -252 -1901 C ATOM 5228 C SER D 72 -2.377 112.753 3.630 1.00 47.81 C ANISOU 5228 C SER D 72 6699 7604 3863 1366 -348 -1960 C ATOM 5229 O SER D 72 -2.905 111.642 3.683 1.00 48.17 O ANISOU 5229 O SER D 72 6928 7434 3941 1367 -495 -2130 O ATOM 5230 CB SER D 72 -1.479 113.157 1.340 1.00 50.88 C ANISOU 5230 CB SER D 72 7005 8496 3831 1792 -294 -1954 C ATOM 5231 OG SER D 72 -0.331 113.456 0.570 1.00 52.34 O ANISOU 5231 OG SER D 72 7081 9014 3792 2047 -174 -1854 O ATOM 5232 N LEU D 73 -2.842 113.821 4.278 1.00 46.28 N ANISOU 5232 N LEU D 73 6364 7395 3826 1142 -270 -1809 N ATOM 5233 CA LEU D 73 -4.160 113.861 4.903 1.00 45.52 C ANISOU 5233 CA LEU D 73 6288 7087 3920 902 -328 -1828 C ATOM 5234 C LEU D 73 -5.025 114.775 4.060 1.00 45.71 C ANISOU 5234 C LEU D 73 6205 7228 3937 848 -339 -1784 C ATOM 5235 O LEU D 73 -4.672 115.936 3.843 1.00 45.26 O ANISOU 5235 O LEU D 73 5999 7344 3854 850 -239 -1635 O ATOM 5236 CB LEU D 73 -4.079 114.422 6.326 1.00 43.69 C ANISOU 5236 CB LEU D 73 5989 6762 3850 728 -230 -1701 C ATOM 5237 CG LEU D 73 -5.386 114.524 7.124 1.00 42.91 C ANISOU 5237 CG LEU D 73 5885 6487 3933 504 -250 -1688 C ATOM 5238 CD1 LEU D 73 -5.911 113.141 7.480 1.00 43.80 C ANISOU 5238 CD1 LEU D 73 6153 6377 4112 453 -364 -1800 C ATOM 5239 CD2 LEU D 73 -5.188 115.350 8.388 1.00 41.36 C ANISOU 5239 CD2 LEU D 73 5614 6266 3836 393 -138 -1561 C ATOM 5240 N THR D 74 -6.165 114.262 3.613 1.00 46.57 N ANISOU 5240 N THR D 74 6383 7226 4084 788 -478 -1901 N ATOM 5241 CA THR D 74 -7.115 115.043 2.836 1.00 46.75 C ANISOU 5241 CA THR D 74 6308 7343 4111 733 -514 -1869 C ATOM 5242 C THR D 74 -8.385 115.211 3.660 1.00 45.85 C ANISOU 5242 C THR D 74 6139 7059 4223 490 -537 -1835 C ATOM 5243 O THR D 74 -8.902 114.234 4.218 1.00 46.60 O ANISOU 5243 O THR D 74 6324 6951 4430 389 -625 -1911 O ATOM 5244 CB THR D 74 -7.410 114.360 1.488 1.00 48.67 C ANISOU 5244 CB THR D 74 6662 7641 4191 889 -678 -2033 C ATOM 5245 OG1 THR D 74 -6.178 114.173 0.783 1.00 49.87 O ANISOU 5245 OG1 THR D 74 6860 7984 4104 1154 -630 -2057 O ATOM 5246 CG2 THR D 74 -8.350 115.203 0.619 1.00 49.04 C ANISOU 5246 CG2 THR D 74 6602 7807 4222 849 -724 -1990 C ATOM 5247 N ILE D 75 -8.875 116.450 3.729 1.00 44.70 N ANISOU 5247 N ILE D 75 5840 7001 4144 406 -458 -1707 N ATOM 5248 CA ILE D 75 -10.163 116.757 4.345 1.00 44.17 C ANISOU 5248 CA ILE D 75 5687 6832 4263 220 -467 -1664 C ATOM 5249 C ILE D 75 -11.084 117.289 3.260 1.00 44.83 C ANISOU 5249 C ILE D 75 5687 7020 4326 225 -554 -1667 C ATOM 5250 O ILE D 75 -10.855 118.369 2.724 1.00 43.88 O ANISOU 5250 O ILE D 75 5479 7056 4137 292 -496 -1574 O ATOM 5251 CB ILE D 75 -10.061 117.806 5.473 1.00 42.91 C ANISOU 5251 CB ILE D 75 5430 6670 4206 141 -312 -1525 C ATOM 5252 CG1 ILE D 75 -8.915 117.464 6.432 1.00 42.35 C ANISOU 5252 CG1 ILE D 75 5438 6538 4117 169 -230 -1510 C ATOM 5253 CG2 ILE D 75 -11.387 117.883 6.229 1.00 42.83 C ANISOU 5253 CG2 ILE D 75 5342 6564 4367 -16 -307 -1493 C ATOM 5254 CD1 ILE D 75 -8.627 118.535 7.462 1.00 41.23 C ANISOU 5254 CD1 ILE D 75 5228 6395 4042 123 -111 -1395 C ATOM 5255 N SER D 76 -12.117 116.522 2.933 1.00 46.56 N ANISOU 5255 N SER D 76 5930 7145 4614 147 -712 -1761 N ATOM 5256 CA SER D 76 -13.126 116.954 1.967 1.00 47.78 C ANISOU 5256 CA SER D 76 5999 7387 4769 137 -823 -1768 C ATOM 5257 C SER D 76 -14.196 117.701 2.716 1.00 46.74 C ANISOU 5257 C SER D 76 5696 7233 4831 -18 -756 -1649 C ATOM 5258 O SER D 76 -14.334 117.529 3.923 1.00 46.98 O ANISOU 5258 O SER D 76 5703 7156 4992 -127 -664 -1597 O ATOM 5259 CB SER D 76 -13.741 115.753 1.268 1.00 50.02 C ANISOU 5259 CB SER D 76 6386 7567 5051 119 -1061 -1930 C ATOM 5260 OG SER D 76 -12.729 114.955 0.706 1.00 51.25 O ANISOU 5260 OG SER D 76 6729 7725 5020 294 -1124 -2064 O ATOM 5261 N GLY D 77 -14.932 118.555 2.015 1.00 46.68 N ANISOU 5261 N GLY D 77 5569 7343 4825 -4 -794 -1600 N ATOM 5262 CA GLY D 77 -16.071 119.246 2.604 1.00 46.19 C ANISOU 5262 CA GLY D 77 5332 7279 4938 -117 -746 -1498 C ATOM 5263 C GLY D 77 -15.758 119.830 3.970 1.00 44.19 C ANISOU 5263 C GLY D 77 5044 6982 4766 -149 -549 -1400 C ATOM 5264 O GLY D 77 -16.328 119.395 4.970 1.00 44.44 O ANISOU 5264 O GLY D 77 5031 6925 4930 -262 -504 -1373 O ATOM 5265 N LEU D 78 -14.825 120.779 4.002 1.00 42.38 N ANISOU 5265 N LEU D 78 4837 6816 4450 -48 -444 -1340 N ATOM 5266 CA LEU D 78 -14.398 121.423 5.244 1.00 40.95 C ANISOU 5266 CA LEU D 78 4652 6583 4324 -56 -291 -1267 C ATOM 5267 C LEU D 78 -15.582 121.996 6.016 1.00 40.96 C ANISOU 5267 C LEU D 78 4522 6572 4467 -110 -234 -1206 C ATOM 5268 O LEU D 78 -16.476 122.598 5.430 1.00 41.23 O ANISOU 5268 O LEU D 78 4441 6680 4543 -95 -284 -1173 O ATOM 5269 CB LEU D 78 -13.402 122.555 4.974 1.00 40.15 C ANISOU 5269 CB LEU D 78 4564 6547 4143 41 -238 -1189 C ATOM 5270 CG LEU D 78 -11.954 122.175 4.662 1.00 39.61 C ANISOU 5270 CG LEU D 78 4598 6510 3942 109 -226 -1200 C ATOM 5271 CD1 LEU D 78 -11.215 123.380 4.107 1.00 39.38 C ANISOU 5271 CD1 LEU D 78 4525 6580 3857 182 -201 -1074 C ATOM 5272 CD2 LEU D 78 -11.252 121.641 5.910 1.00 38.79 C ANISOU 5272 CD2 LEU D 78 4578 6294 3868 73 -148 -1224 C ATOM 5273 N GLN D 79 -15.582 121.762 7.321 1.00 40.63 N ANISOU 5273 N GLN D 79 4499 6455 4484 -153 -128 -1190 N ATOM 5274 CA GLN D 79 -16.555 122.342 8.235 1.00 41.44 C ANISOU 5274 CA GLN D 79 4488 6574 4685 -159 -36 -1127 C ATOM 5275 C GLN D 79 -15.782 123.161 9.258 1.00 40.59 C ANISOU 5275 C GLN D 79 4462 6422 4540 -78 76 -1108 C ATOM 5276 O GLN D 79 -14.606 122.895 9.502 1.00 39.48 O ANISOU 5276 O GLN D 79 4448 6221 4329 -70 86 -1135 O ATOM 5277 CB GLN D 79 -17.383 121.245 8.900 1.00 42.65 C ANISOU 5277 CB GLN D 79 4580 6698 4929 -279 -16 -1108 C ATOM 5278 CG GLN D 79 -18.025 120.300 7.887 1.00 44.40 C ANISOU 5278 CG GLN D 79 4749 6917 5204 -384 -179 -1141 C ATOM 5279 CD GLN D 79 -18.964 119.282 8.510 1.00 46.17 C ANISOU 5279 CD GLN D 79 4876 7102 5564 -537 -184 -1080 C ATOM 5280 OE1 GLN D 79 -19.197 119.284 9.719 1.00 46.68 O ANISOU 5280 OE1 GLN D 79 4896 7172 5667 -554 -37 -995 O ATOM 5281 NE2 GLN D 79 -19.499 118.395 7.682 1.00 47.56 N ANISOU 5281 NE2 GLN D 79 5022 7238 5811 -649 -366 -1115 N ATOM 5282 N ALA D 80 -16.445 124.157 9.840 1.00 41.12 N ANISOU 5282 N ALA D 80 4456 6516 4651 -4 143 -1069 N ATOM 5283 CA ALA D 80 -15.800 125.138 10.723 1.00 40.86 C ANISOU 5283 CA ALA D 80 4515 6423 4585 97 203 -1071 C ATOM 5284 C ALA D 80 -14.934 124.483 11.813 1.00 40.38 C ANISOU 5284 C ALA D 80 4587 6288 4469 73 268 -1099 C ATOM 5285 O ALA D 80 -13.822 124.935 12.093 1.00 39.56 O ANISOU 5285 O ALA D 80 4598 6114 4318 110 249 -1116 O ATOM 5286 CB ALA D 80 -16.856 126.044 11.348 1.00 42.04 C ANISOU 5286 CB ALA D 80 4578 6615 4781 205 269 -1049 C ATOM 5287 N GLU D 81 -15.445 123.395 12.381 1.00 41.11 N ANISOU 5287 N GLU D 81 4650 6395 4575 -1 330 -1087 N ATOM 5288 CA GLU D 81 -14.732 122.604 13.388 1.00 41.08 C ANISOU 5288 CA GLU D 81 4766 6326 4518 -30 388 -1097 C ATOM 5289 C GLU D 81 -13.445 121.910 12.939 1.00 39.56 C ANISOU 5289 C GLU D 81 4695 6061 4274 -76 313 -1139 C ATOM 5290 O GLU D 81 -12.666 121.480 13.792 1.00 38.85 O ANISOU 5290 O GLU D 81 4718 5911 4132 -71 348 -1149 O ATOM 5291 CB GLU D 81 -15.666 121.541 13.966 1.00 43.08 C ANISOU 5291 CB GLU D 81 4939 6611 4817 -120 459 -1035 C ATOM 5292 CG GLU D 81 -16.787 122.041 14.808 1.00 45.33 C ANISOU 5292 CG GLU D 81 5105 6999 5120 -51 584 -968 C ATOM 5293 CD GLU D 81 -17.834 120.976 15.094 1.00 47.66 C ANISOU 5293 CD GLU D 81 5258 7355 5496 -176 638 -857 C ATOM 5294 OE1 GLU D 81 -17.552 119.759 14.917 1.00 48.32 O ANISOU 5294 OE1 GLU D 81 5387 7353 5618 -321 575 -841 O ATOM 5295 OE2 GLU D 81 -18.940 121.374 15.505 1.00 49.63 O ANISOU 5295 OE2 GLU D 81 5343 7735 5777 -123 738 -776 O ATOM 5296 N ASP D 82 -13.215 121.795 11.628 1.00 39.00 N ANISOU 5296 N ASP D 82 4603 6014 4203 -97 213 -1162 N ATOM 5297 CA ASP D 82 -11.955 121.237 11.113 1.00 38.33 C ANISOU 5297 CA ASP D 82 4620 5899 4047 -93 154 -1199 C ATOM 5298 C ASP D 82 -10.751 122.178 11.255 1.00 37.32 C ANISOU 5298 C ASP D 82 4546 5764 3870 -21 154 -1179 C ATOM 5299 O ASP D 82 -9.609 121.741 11.097 1.00 37.03 O ANISOU 5299 O ASP D 82 4577 5718 3773 -6 129 -1189 O ATOM 5300 CB ASP D 82 -12.097 120.826 9.639 1.00 39.00 C ANISOU 5300 CB ASP D 82 4668 6039 4110 -102 50 -1232 C ATOM 5301 CG ASP D 82 -13.220 119.830 9.409 1.00 40.27 C ANISOU 5301 CG ASP D 82 4781 6179 4340 -195 -3 -1257 C ATOM 5302 OD1 ASP D 82 -13.520 119.025 10.313 1.00 41.25 O ANISOU 5302 OD1 ASP D 82 4930 6229 4515 -269 36 -1243 O ATOM 5303 OD2 ASP D 82 -13.828 119.867 8.328 1.00 41.28 O ANISOU 5303 OD2 ASP D 82 4841 6365 4478 -201 -96 -1277 O ATOM 5304 N GLU D 83 -10.992 123.458 11.537 1.00 37.16 N ANISOU 5304 N GLU D 83 4492 5742 3886 25 165 -1145 N ATOM 5305 CA GLU D 83 -9.914 124.409 11.801 1.00 36.52 C ANISOU 5305 CA GLU D 83 4463 5618 3796 66 132 -1112 C ATOM 5306 C GLU D 83 -9.135 124.013 13.068 1.00 36.01 C ANISOU 5306 C GLU D 83 4512 5476 3694 70 163 -1142 C ATOM 5307 O GLU D 83 -9.670 124.039 14.169 1.00 35.81 O ANISOU 5307 O GLU D 83 4531 5412 3665 96 220 -1172 O ATOM 5308 CB GLU D 83 -10.472 125.833 11.936 1.00 37.29 C ANISOU 5308 CB GLU D 83 4528 5685 3956 121 109 -1086 C ATOM 5309 CG GLU D 83 -9.420 126.882 12.292 1.00 37.74 C ANISOU 5309 CG GLU D 83 4650 5653 4037 143 34 -1049 C ATOM 5310 CD GLU D 83 -9.779 128.293 11.852 1.00 38.98 C ANISOU 5310 CD GLU D 83 4769 5767 4272 184 -43 -996 C ATOM 5311 OE1 GLU D 83 -10.371 128.485 10.763 1.00 39.43 O ANISOU 5311 OE1 GLU D 83 4729 5903 4348 182 -56 -947 O ATOM 5312 OE2 GLU D 83 -9.420 129.224 12.605 1.00 40.45 O ANISOU 5312 OE2 GLU D 83 5039 5827 4502 222 -112 -1006 O ATOM 5313 N ALA D 84 -7.870 123.643 12.875 1.00 35.41 N ANISOU 5313 N ALA D 84 4474 5400 3578 60 126 -1125 N ATOM 5314 CA ALA D 84 -7.025 123.099 13.929 1.00 35.00 C ANISOU 5314 CA ALA D 84 4524 5288 3485 65 137 -1148 C ATOM 5315 C ALA D 84 -5.610 122.910 13.383 1.00 34.98 C ANISOU 5315 C ALA D 84 4512 5326 3454 69 84 -1103 C ATOM 5316 O ALA D 84 -5.370 123.127 12.196 1.00 35.07 O ANISOU 5316 O ALA D 84 4437 5426 3461 75 58 -1050 O ATOM 5317 CB ALA D 84 -7.585 121.762 14.399 1.00 35.22 C ANISOU 5317 CB ALA D 84 4598 5302 3480 40 203 -1192 C ATOM 5318 N ASP D 85 -4.687 122.486 14.242 1.00 35.00 N ANISOU 5318 N ASP D 85 4591 5283 3424 80 73 -1112 N ATOM 5319 CA ASP D 85 -3.377 122.027 13.790 1.00 35.68 C ANISOU 5319 CA ASP D 85 4652 5433 3474 103 41 -1068 C ATOM 5320 C ASP D 85 -3.443 120.519 13.556 1.00 35.64 C ANISOU 5320 C ASP D 85 4699 5444 3400 134 81 -1131 C ATOM 5321 O ASP D 85 -4.196 119.806 14.239 1.00 36.04 O ANISOU 5321 O ASP D 85 4831 5416 3447 112 119 -1189 O ATOM 5322 CB ASP D 85 -2.274 122.410 14.787 1.00 36.37 C ANISOU 5322 CB ASP D 85 4780 5462 3575 102 -22 -1037 C ATOM 5323 CG ASP D 85 -1.989 123.921 14.801 1.00 37.04 C ANISOU 5323 CG ASP D 85 4812 5509 3752 62 -115 -962 C ATOM 5324 OD1 ASP D 85 -2.098 124.564 13.747 1.00 37.47 O ANISOU 5324 OD1 ASP D 85 4759 5629 3849 42 -128 -882 O ATOM 5325 OD2 ASP D 85 -1.650 124.482 15.856 1.00 37.97 O ANISOU 5325 OD2 ASP D 85 5006 5522 3900 54 -192 -980 O ATOM 5326 N TYR D 86 -2.683 120.048 12.571 1.00 35.85 N ANISOU 5326 N TYR D 86 4677 5574 3370 195 69 -1111 N ATOM 5327 CA TYR D 86 -2.644 118.631 12.208 1.00 36.27 C ANISOU 5327 CA TYR D 86 4802 5627 3353 256 74 -1190 C ATOM 5328 C TYR D 86 -1.207 118.158 12.125 1.00 36.71 C ANISOU 5328 C TYR D 86 4850 5754 3342 357 60 -1162 C ATOM 5329 O TYR D 86 -0.371 118.817 11.512 1.00 37.00 O ANISOU 5329 O TYR D 86 4768 5930 3361 398 58 -1066 O ATOM 5330 CB TYR D 86 -3.354 118.388 10.875 1.00 36.69 C ANISOU 5330 CB TYR D 86 4818 5753 3369 283 62 -1232 C ATOM 5331 CG TYR D 86 -4.848 118.601 10.950 1.00 36.69 C ANISOU 5331 CG TYR D 86 4815 5684 3442 188 66 -1264 C ATOM 5332 CD1 TYR D 86 -5.390 119.874 10.819 1.00 36.34 C ANISOU 5332 CD1 TYR D 86 4678 5675 3454 143 78 -1202 C ATOM 5333 CD2 TYR D 86 -5.722 117.529 11.170 1.00 37.07 C ANISOU 5333 CD2 TYR D 86 4940 5627 3515 142 49 -1341 C ATOM 5334 CE1 TYR D 86 -6.756 120.079 10.895 1.00 36.31 C ANISOU 5334 CE1 TYR D 86 4649 5631 3515 79 88 -1224 C ATOM 5335 CE2 TYR D 86 -7.091 117.728 11.249 1.00 37.31 C ANISOU 5335 CE2 TYR D 86 4929 5622 3625 49 56 -1342 C ATOM 5336 CZ TYR D 86 -7.599 119.006 11.114 1.00 36.87 C ANISOU 5336 CZ TYR D 86 4770 5629 3609 30 84 -1288 C ATOM 5337 OH TYR D 86 -8.948 119.222 11.197 1.00 37.80 O ANISOU 5337 OH TYR D 86 4826 5735 3804 -38 97 -1282 O ATOM 5338 N TYR D 87 -0.930 117.015 12.750 1.00 37.09 N ANISOU 5338 N TYR D 87 5017 5716 3361 398 51 -1225 N ATOM 5339 CA TYR D 87 0.405 116.440 12.802 1.00 37.57 C ANISOU 5339 CA TYR D 87 5080 5837 3359 516 35 -1207 C ATOM 5340 C TYR D 87 0.367 115.035 12.249 1.00 38.67 C ANISOU 5340 C TYR D 87 5327 5944 3421 632 12 -1316 C ATOM 5341 O TYR D 87 -0.476 114.236 12.640 1.00 38.85 O ANISOU 5341 O TYR D 87 5479 5805 3477 578 -13 -1394 O ATOM 5342 CB TYR D 87 0.908 116.384 14.242 1.00 37.02 C ANISOU 5342 CB TYR D 87 5076 5665 3323 481 17 -1183 C ATOM 5343 CG TYR D 87 1.156 117.737 14.844 1.00 36.61 C ANISOU 5343 CG TYR D 87 4946 5625 3340 394 -3 -1096 C ATOM 5344 CD1 TYR D 87 2.367 118.398 14.652 1.00 36.96 C ANISOU 5344 CD1 TYR D 87 4857 5785 3400 417 -42 -988 C ATOM 5345 CD2 TYR D 87 0.180 118.366 15.612 1.00 36.01 C ANISOU 5345 CD2 TYR D 87 4924 5442 3315 294 5 -1117 C ATOM 5346 CE1 TYR D 87 2.603 119.648 15.209 1.00 37.06 C ANISOU 5346 CE1 TYR D 87 4813 5769 3501 322 -105 -912 C ATOM 5347 CE2 TYR D 87 0.406 119.616 16.174 1.00 36.17 C ANISOU 5347 CE2 TYR D 87 4905 5442 3394 237 -45 -1064 C ATOM 5348 CZ TYR D 87 1.618 120.258 15.974 1.00 36.49 C ANISOU 5348 CZ TYR D 87 4834 5560 3471 240 -116 -966 C ATOM 5349 OH TYR D 87 1.834 121.506 16.539 1.00 36.52 O ANISOU 5349 OH TYR D 87 4816 5503 3556 168 -209 -919 O ATOM 5350 N CYS D 88 1.276 114.731 11.337 1.00 40.33 N ANISOU 5350 N CYS D 88 5485 6307 3530 799 12 -1316 N ATOM 5351 CA CYS D 88 1.509 113.339 10.966 1.00 42.03 C ANISOU 5351 CA CYS D 88 5834 6475 3659 960 -34 -1437 C ATOM 5352 C CYS D 88 2.508 112.754 11.951 1.00 41.77 C ANISOU 5352 C CYS D 88 5855 6387 3628 1027 -48 -1416 C ATOM 5353 O CYS D 88 3.201 113.481 12.663 1.00 40.41 O ANISOU 5353 O CYS D 88 5583 6272 3497 976 -24 -1302 O ATOM 5354 CB CYS D 88 2.025 113.215 9.540 1.00 43.81 C ANISOU 5354 CB CYS D 88 5996 6912 3738 1163 -23 -1462 C ATOM 5355 SG CYS D 88 3.580 114.079 9.247 1.00 45.74 S ANISOU 5355 SG CYS D 88 6002 7459 3919 1277 61 -1275 S ATOM 5356 N CYS D 89 2.560 111.432 11.975 1.00 42.91 N ANISOU 5356 N CYS D 89 6167 6404 3732 1140 -111 -1528 N ATOM 5357 CA CYS D 89 3.489 110.695 12.811 1.00 43.64 C ANISOU 5357 CA CYS D 89 6334 6434 3815 1238 -140 -1520 C ATOM 5358 C CYS D 89 3.821 109.405 12.092 1.00 45.30 C ANISOU 5358 C CYS D 89 6681 6605 3926 1471 -209 -1656 C ATOM 5359 O CYS D 89 2.952 108.814 11.456 1.00 45.55 O ANISOU 5359 O CYS D 89 6836 6518 3951 1472 -277 -1778 O ATOM 5360 CB CYS D 89 2.838 110.383 14.146 1.00 43.11 C ANISOU 5360 CB CYS D 89 6397 6133 3852 1067 -166 -1505 C ATOM 5361 SG CYS D 89 3.881 109.485 15.312 1.00 43.97 S ANISOU 5361 SG CYS D 89 6616 6142 3948 1170 -215 -1478 S ATOM 5362 N SER D 90 5.072 108.975 12.177 1.00 46.51 N ANISOU 5362 N SER D 90 6813 6856 4004 1680 -209 -1640 N ATOM 5363 CA SER D 90 5.464 107.703 11.593 1.00 48.65 C ANISOU 5363 CA SER D 90 7239 7075 4171 1946 -287 -1785 C ATOM 5364 C SER D 90 6.410 106.946 12.503 1.00 49.56 C ANISOU 5364 C SER D 90 7427 7110 4292 2068 -329 -1764 C ATOM 5365 O SER D 90 7.248 107.533 13.199 1.00 48.85 O ANISOU 5365 O SER D 90 7187 7147 4226 2043 -274 -1625 O ATOM 5366 CB SER D 90 6.104 107.905 10.217 1.00 50.08 C ANISOU 5366 CB SER D 90 7297 7553 4179 2202 -232 -1812 C ATOM 5367 OG SER D 90 6.581 106.676 9.680 1.00 52.53 O ANISOU 5367 OG SER D 90 7771 7827 4362 2515 -312 -1971 O ATOM 5368 N TYR D 91 6.250 105.627 12.490 1.00 51.37 N ANISOU 5368 N TYR D 91 7898 7110 4510 2196 -449 -1904 N ATOM 5369 CA TYR D 91 7.255 104.722 13.023 1.00 52.93 C ANISOU 5369 CA TYR D 91 8186 7249 4675 2408 -506 -1917 C ATOM 5370 C TYR D 91 8.539 104.975 12.250 1.00 54.17 C ANISOU 5370 C TYR D 91 8155 7751 4676 2711 -426 -1894 C ATOM 5371 O TYR D 91 8.501 105.166 11.038 1.00 54.90 O ANISOU 5371 O TYR D 91 8186 8027 4646 2856 -385 -1962 O ATOM 5372 CB TYR D 91 6.800 103.276 12.847 1.00 54.79 C ANISOU 5372 CB TYR D 91 8729 7170 4921 2522 -674 -2092 C ATOM 5373 CG TYR D 91 7.674 102.269 13.545 1.00 56.53 C ANISOU 5373 CG TYR D 91 9083 7258 5135 2716 -757 -2100 C ATOM 5374 CD1 TYR D 91 7.808 102.305 14.922 1.00 55.64 C ANISOU 5374 CD1 TYR D 91 8978 7035 5128 2549 -753 -1955 C ATOM 5375 CD2 TYR D 91 8.339 101.269 12.840 1.00 58.98 C ANISOU 5375 CD2 TYR D 91 9532 7553 5327 3085 -850 -2258 C ATOM 5376 CE1 TYR D 91 8.597 101.395 15.598 1.00 57.23 C ANISOU 5376 CE1 TYR D 91 9305 7115 5326 2724 -837 -1948 C ATOM 5377 CE2 TYR D 91 9.136 100.343 13.503 1.00 60.81 C ANISOU 5377 CE2 TYR D 91 9892 7652 5561 3277 -935 -2262 C ATOM 5378 CZ TYR D 91 9.257 100.411 14.885 1.00 59.78 C ANISOU 5378 CZ TYR D 91 9755 7411 5549 3084 -930 -2098 C ATOM 5379 OH TYR D 91 10.028 99.517 15.575 1.00 61.52 O ANISOU 5379 OH TYR D 91 10102 7500 5773 3267 -1021 -2086 O ATOM 5380 N ALA D 92 9.667 104.996 12.953 1.00 54.92 N ANISOU 5380 N ALA D 92 8142 7955 4771 2808 -401 -1783 N ATOM 5381 CA ALA D 92 10.952 105.342 12.344 1.00 56.51 C ANISOU 5381 CA ALA D 92 8098 8525 4847 3068 -308 -1702 C ATOM 5382 C ALA D 92 12.032 104.291 12.619 1.00 59.17 C ANISOU 5382 C ALA D 92 8505 8861 5117 3392 -367 -1743 C ATOM 5383 O ALA D 92 13.218 104.605 12.607 1.00 60.60 O ANISOU 5383 O ALA D 92 8447 9332 5245 3555 -297 -1615 O ATOM 5384 CB ALA D 92 11.390 106.721 12.825 1.00 55.15 C ANISOU 5384 CB ALA D 92 7628 8569 4758 2851 -214 -1475 C ATOM 5385 N GLY D 93 11.614 103.048 12.859 1.00 60.35 N ANISOU 5385 N GLY D 93 8971 8679 5280 3481 -507 -1908 N ATOM 5386 CA GLY D 93 12.535 101.940 13.102 1.00 62.89 C ANISOU 5386 CA GLY D 93 9409 8944 5542 3810 -591 -1970 C ATOM 5387 C GLY D 93 13.036 101.836 14.532 1.00 62.43 C ANISOU 5387 C GLY D 93 9348 8773 5600 3699 -637 -1834 C ATOM 5388 O GLY D 93 13.081 102.838 15.260 1.00 60.56 O ANISOU 5388 O GLY D 93 8926 8632 5453 3432 -574 -1662 O ATOM 5389 N SER D 94 13.396 100.607 14.918 1.00 64.54 N ANISOU 5389 N SER D 94 9841 8823 5860 3920 -767 -1921 N ATOM 5390 CA SER D 94 13.963 100.263 16.235 1.00 64.81 C ANISOU 5390 CA SER D 94 9915 8737 5975 3891 -837 -1807 C ATOM 5391 C SER D 94 13.239 100.976 17.385 1.00 62.01 C ANISOU 5391 C SER D 94 9552 8249 5760 3462 -825 -1666 C ATOM 5392 O SER D 94 13.853 101.667 18.192 1.00 61.07 O ANISOU 5392 O SER D 94 9250 8281 5674 3363 -791 -1508 O ATOM 5393 CB SER D 94 15.487 100.495 16.270 1.00 66.48 C ANISOU 5393 CB SER D 94 9851 9299 6108 4160 -778 -1695 C ATOM 5394 OG SER D 94 15.791 101.876 16.199 1.00 65.48 O ANISOU 5394 OG SER D 94 9378 9502 6000 3977 -645 -1526 O ATOM 5395 N TYR D 95 11.919 100.805 17.420 1.00 60.82 N ANISOU 5395 N TYR D 95 9597 7825 5685 3221 -862 -1727 N ATOM 5396 CA TYR D 95 11.066 101.300 18.501 1.00 58.75 C ANISOU 5396 CA TYR D 95 9373 7413 5537 2851 -850 -1609 C ATOM 5397 C TYR D 95 11.152 102.821 18.710 1.00 56.09 C ANISOU 5397 C TYR D 95 8755 7346 5211 2643 -723 -1483 C ATOM 5398 O TYR D 95 11.311 103.300 19.837 1.00 54.83 O ANISOU 5398 O TYR D 95 8553 7189 5091 2490 -724 -1357 O ATOM 5399 CB TYR D 95 11.379 100.548 19.801 1.00 60.00 C ANISOU 5399 CB TYR D 95 9696 7364 5739 2857 -950 -1524 C ATOM 5400 CG TYR D 95 11.326 99.047 19.664 1.00 62.98 C ANISOU 5400 CG TYR D 95 10365 7435 6129 3054 -1102 -1630 C ATOM 5401 CD1 TYR D 95 10.123 98.358 19.813 1.00 63.61 C ANISOU 5401 CD1 TYR D 95 10694 7165 6311 2868 -1189 -1658 C ATOM 5402 CD2 TYR D 95 12.476 98.309 19.383 1.00 65.63 C ANISOU 5402 CD2 TYR D 95 10725 7824 6386 3432 -1172 -1695 C ATOM 5403 CE1 TYR D 95 10.065 96.977 19.685 1.00 66.39 C ANISOU 5403 CE1 TYR D 95 11331 7193 6702 3031 -1366 -1750 C ATOM 5404 CE2 TYR D 95 12.426 96.927 19.254 1.00 68.44 C ANISOU 5404 CE2 TYR D 95 11378 7865 6760 3631 -1338 -1808 C ATOM 5405 CZ TYR D 95 11.216 96.269 19.407 1.00 68.79 C ANISOU 5405 CZ TYR D 95 11686 7529 6923 3419 -1446 -1836 C ATOM 5406 OH TYR D 95 11.143 94.901 19.282 1.00 72.11 O ANISOU 5406 OH TYR D 95 12416 7593 7389 3594 -1646 -1941 O ATOM 5407 N THR D 95A 11.054 103.570 17.612 1.00 54.97 N ANISOU 5407 N THR D 95A 8437 7421 5027 2650 -631 -1518 N ATOM 5408 CA THR D 95A 11.013 105.037 17.664 1.00 52.59 C ANISOU 5408 CA THR D 95A 7886 7338 4756 2440 -531 -1402 C ATOM 5409 C THR D 95A 9.919 105.595 16.757 1.00 50.97 C ANISOU 5409 C THR D 95A 7662 7143 4561 2292 -465 -1463 C ATOM 5410 O THR D 95A 9.516 104.956 15.779 1.00 51.51 O ANISOU 5410 O THR D 95A 7838 7158 4577 2421 -484 -1599 O ATOM 5411 CB THR D 95A 12.368 105.676 17.280 1.00 53.35 C ANISOU 5411 CB THR D 95A 7685 7785 4802 2604 -479 -1300 C ATOM 5412 OG1 THR D 95A 12.636 105.451 15.894 1.00 55.01 O ANISOU 5412 OG1 THR D 95A 7818 8179 4903 2846 -421 -1377 O ATOM 5413 CG2 THR D 95A 13.512 105.096 18.110 1.00 54.79 C ANISOU 5413 CG2 THR D 95A 7862 7982 4975 2776 -558 -1237 C ATOM 5414 N TYR D 96 9.442 106.786 17.117 1.00 48.35 N ANISOU 5414 N TYR D 96 7206 6870 4294 2033 -406 -1371 N ATOM 5415 CA TYR D 96 8.474 107.544 16.336 1.00 46.83 C ANISOU 5415 CA TYR D 96 6952 6722 4119 1881 -339 -1398 C ATOM 5416 C TYR D 96 8.989 108.955 16.127 1.00 45.73 C ANISOU 5416 C TYR D 96 6538 6843 3996 1800 -269 -1270 C ATOM 5417 O TYR D 96 9.725 109.483 16.957 1.00 45.32 O ANISOU 5417 O TYR D 96 6380 6854 3983 1750 -293 -1158 O ATOM 5418 CB TYR D 96 7.115 107.580 17.049 1.00 45.47 C ANISOU 5418 CB TYR D 96 6933 6310 4035 1623 -349 -1411 C ATOM 5419 CG TYR D 96 6.417 106.250 16.957 1.00 46.39 C ANISOU 5419 CG TYR D 96 7296 6165 4165 1662 -428 -1519 C ATOM 5420 CD1 TYR D 96 5.650 105.933 15.845 1.00 46.62 C ANISOU 5420 CD1 TYR D 96 7383 6146 4185 1680 -448 -1638 C ATOM 5421 CD2 TYR D 96 6.564 105.284 17.958 1.00 47.24 C ANISOU 5421 CD2 TYR D 96 7585 6065 4300 1684 -506 -1498 C ATOM 5422 CE1 TYR D 96 5.028 104.701 15.730 1.00 48.00 C ANISOU 5422 CE1 TYR D 96 7791 6052 4397 1703 -562 -1739 C ATOM 5423 CE2 TYR D 96 5.943 104.048 17.855 1.00 48.44 C ANISOU 5423 CE2 TYR D 96 7966 5947 4491 1704 -605 -1577 C ATOM 5424 CZ TYR D 96 5.181 103.760 16.733 1.00 49.04 C ANISOU 5424 CZ TYR D 96 8096 5961 4577 1708 -643 -1702 C ATOM 5425 OH TYR D 96 4.557 102.542 16.602 1.00 50.63 O ANISOU 5425 OH TYR D 96 8530 5865 4842 1710 -781 -1783 O ATOM 5426 N VAL D 97 8.604 109.548 15.003 1.00 45.35 N ANISOU 5426 N VAL D 97 6378 6933 3919 1787 -202 -1280 N ATOM 5427 CA VAL D 97 8.928 110.932 14.689 1.00 44.76 C ANISOU 5427 CA VAL D 97 6050 7078 3880 1680 -144 -1140 C ATOM 5428 C VAL D 97 7.636 111.612 14.244 1.00 43.55 C ANISOU 5428 C VAL D 97 5919 6862 3766 1493 -107 -1175 C ATOM 5429 O VAL D 97 6.894 111.061 13.425 1.00 43.72 O ANISOU 5429 O VAL D 97 6046 6834 3732 1552 -98 -1292 O ATOM 5430 CB VAL D 97 10.001 111.014 13.585 1.00 46.42 C ANISOU 5430 CB VAL D 97 6044 7603 3991 1907 -83 -1068 C ATOM 5431 CG1 VAL D 97 10.267 112.462 13.191 1.00 46.11 C ANISOU 5431 CG1 VAL D 97 5734 7777 4010 1766 -32 -886 C ATOM 5432 CG2 VAL D 97 11.290 110.342 14.047 1.00 48.02 C ANISOU 5432 CG2 VAL D 97 6199 7887 4160 2111 -119 -1025 C ATOM 5433 N PHE D 98 7.374 112.799 14.786 1.00 42.52 N ANISOU 5433 N PHE D 98 5699 6725 3732 1280 -106 -1080 N ATOM 5434 CA PHE D 98 6.188 113.585 14.418 1.00 41.27 C ANISOU 5434 CA PHE D 98 5540 6521 3621 1111 -73 -1096 C ATOM 5435 C PHE D 98 6.560 114.597 13.347 1.00 41.18 C ANISOU 5435 C PHE D 98 5301 6744 3600 1117 -24 -981 C ATOM 5436 O PHE D 98 7.710 115.032 13.261 1.00 41.79 O ANISOU 5436 O PHE D 98 5193 7002 3685 1168 -25 -843 O ATOM 5437 CB PHE D 98 5.623 114.331 15.627 1.00 40.53 C ANISOU 5437 CB PHE D 98 5498 6275 3625 905 -105 -1069 C ATOM 5438 CG PHE D 98 4.814 113.470 16.553 1.00 40.49 C ANISOU 5438 CG PHE D 98 5714 6048 3622 861 -120 -1160 C ATOM 5439 CD1 PHE D 98 3.451 113.288 16.334 1.00 40.01 C ANISOU 5439 CD1 PHE D 98 5747 5875 3581 770 -87 -1231 C ATOM 5440 CD2 PHE D 98 5.408 112.850 17.647 1.00 41.13 C ANISOU 5440 CD2 PHE D 98 5894 6044 3689 905 -170 -1151 C ATOM 5441 CE1 PHE D 98 2.695 112.495 17.183 1.00 40.21 C ANISOU 5441 CE1 PHE D 98 5944 5713 3622 712 -95 -1271 C ATOM 5442 CE2 PHE D 98 4.656 112.057 18.502 1.00 41.41 C ANISOU 5442 CE2 PHE D 98 6123 5887 3724 858 -177 -1196 C ATOM 5443 CZ PHE D 98 3.299 111.879 18.271 1.00 40.89 C ANISOU 5443 CZ PHE D 98 6133 5716 3686 756 -134 -1246 C ATOM 5444 N GLY D 99 5.576 114.987 12.543 1.00 40.13 N ANISOU 5444 N GLY D 99 5170 6617 3459 1056 13 -1017 N ATOM 5445 CA GLY D 99 5.765 116.077 11.596 1.00 40.12 C ANISOU 5445 CA GLY D 99 4964 6818 3460 1029 56 -883 C ATOM 5446 C GLY D 99 5.763 117.444 12.256 1.00 39.20 C ANISOU 5446 C GLY D 99 4748 6656 3489 821 14 -755 C ATOM 5447 O GLY D 99 5.400 117.576 13.427 1.00 38.33 O ANISOU 5447 O GLY D 99 4753 6354 3457 706 -41 -804 O ATOM 5448 N THR D 100 6.148 118.466 11.492 1.00 39.56 N ANISOU 5448 N THR D 100 4590 6876 3564 784 33 -588 N ATOM 5449 CA THR D 100 6.289 119.841 12.013 1.00 39.21 C ANISOU 5449 CA THR D 100 4444 6776 3676 591 -43 -449 C ATOM 5450 C THR D 100 4.960 120.563 12.264 1.00 37.81 C ANISOU 5450 C THR D 100 4381 6414 3573 445 -68 -524 C ATOM 5451 O THR D 100 4.935 121.585 12.936 1.00 38.02 O ANISOU 5451 O THR D 100 4395 6327 3725 305 -157 -468 O ATOM 5452 CB THR D 100 7.127 120.715 11.059 1.00 40.55 C ANISOU 5452 CB THR D 100 4345 7186 3875 581 -25 -205 C ATOM 5453 OG1 THR D 100 6.555 120.671 9.746 1.00 40.75 O ANISOU 5453 OG1 THR D 100 4339 7356 3790 666 71 -202 O ATOM 5454 CG2 THR D 100 8.575 120.226 11.014 1.00 41.98 C ANISOU 5454 CG2 THR D 100 4361 7572 4017 708 -10 -82 C ATOM 5455 N GLY D 101 3.874 120.049 11.696 1.00 37.09 N ANISOU 5455 N GLY D 101 4393 6295 3405 489 -5 -651 N ATOM 5456 CA GLY D 101 2.533 120.570 11.945 1.00 35.84 C ANISOU 5456 CA GLY D 101 4332 5979 3305 378 -15 -730 C ATOM 5457 C GLY D 101 2.042 121.517 10.870 1.00 35.62 C ANISOU 5457 C GLY D 101 4193 6042 3299 338 0 -639 C ATOM 5458 O GLY D 101 2.810 122.307 10.336 1.00 36.37 O ANISOU 5458 O GLY D 101 4123 6267 3430 318 -16 -461 O ATOM 5459 N THR D 102 0.748 121.442 10.575 1.00 35.11 N ANISOU 5459 N THR D 102 4209 5910 3221 320 24 -743 N ATOM 5460 CA THR D 102 0.094 122.322 9.613 1.00 35.04 C ANISOU 5460 CA THR D 102 4118 5967 3231 286 28 -672 C ATOM 5461 C THR D 102 -1.150 122.930 10.238 1.00 34.40 C ANISOU 5461 C THR D 102 4117 5710 3244 190 1 -745 C ATOM 5462 O THR D 102 -1.966 122.215 10.822 1.00 33.91 O ANISOU 5462 O THR D 102 4173 5544 3169 188 24 -884 O ATOM 5463 CB THR D 102 -0.326 121.535 8.360 1.00 35.37 C ANISOU 5463 CB THR D 102 4162 6146 3132 403 78 -734 C ATOM 5464 OG1 THR D 102 0.823 120.886 7.811 1.00 36.36 O ANISOU 5464 OG1 THR D 102 4226 6451 3138 543 115 -688 O ATOM 5465 CG2 THR D 102 -0.957 122.451 7.305 1.00 35.75 C ANISOU 5465 CG2 THR D 102 4118 6284 3180 382 77 -646 C ATOM 5466 N LYS D 103 -1.283 124.249 10.117 1.00 34.72 N ANISOU 5466 N LYS D 103 4087 5723 3382 117 -49 -637 N ATOM 5467 CA LYS D 103 -2.501 124.945 10.510 1.00 34.63 C ANISOU 5467 CA LYS D 103 4135 5577 3447 67 -72 -698 C ATOM 5468 C LYS D 103 -3.493 124.883 9.355 1.00 34.34 C ANISOU 5468 C LYS D 103 4054 5631 3363 99 -35 -711 C ATOM 5469 O LYS D 103 -3.181 125.330 8.255 1.00 34.65 O ANISOU 5469 O LYS D 103 3987 5804 3376 117 -42 -585 O ATOM 5470 CB LYS D 103 -2.204 126.402 10.866 1.00 35.72 C ANISOU 5470 CB LYS D 103 4239 5614 3718 -6 -174 -589 C ATOM 5471 CG LYS D 103 -3.372 127.132 11.479 1.00 36.07 C ANISOU 5471 CG LYS D 103 4369 5504 3830 -15 -205 -675 C ATOM 5472 CD LYS D 103 -2.964 128.355 12.279 1.00 37.52 C ANISOU 5472 CD LYS D 103 4598 5521 4138 -63 -341 -634 C ATOM 5473 CE LYS D 103 -4.124 128.863 13.127 1.00 37.97 C ANISOU 5473 CE LYS D 103 4776 5432 4217 -13 -354 -769 C ATOM 5474 NZ LYS D 103 -5.183 129.545 12.329 1.00 38.85 N ANISOU 5474 NZ LYS D 103 4838 5555 4370 11 -348 -743 N ATOM 5475 N VAL D 104 -4.664 124.304 9.607 1.00 33.89 N ANISOU 5475 N VAL D 104 4069 5515 3293 104 -2 -846 N ATOM 5476 CA VAL D 104 -5.771 124.336 8.651 1.00 33.99 C ANISOU 5476 CA VAL D 104 4039 5589 3286 119 2 -867 C ATOM 5477 C VAL D 104 -6.698 125.485 9.050 1.00 33.91 C ANISOU 5477 C VAL D 104 4016 5483 3384 85 -24 -852 C ATOM 5478 O VAL D 104 -7.194 125.502 10.170 1.00 33.42 O ANISOU 5478 O VAL D 104 4022 5307 3368 72 -5 -926 O ATOM 5479 CB VAL D 104 -6.546 123.000 8.638 1.00 33.93 C ANISOU 5479 CB VAL D 104 4096 5571 3226 130 29 -1006 C ATOM 5480 CG1 VAL D 104 -7.824 123.116 7.807 1.00 34.59 C ANISOU 5480 CG1 VAL D 104 4126 5696 3318 126 5 -1032 C ATOM 5481 CG2 VAL D 104 -5.662 121.877 8.097 1.00 34.15 C ANISOU 5481 CG2 VAL D 104 4158 5681 3137 201 31 -1041 C ATOM 5482 N THR D 105 -6.911 126.445 8.145 1.00 34.34 N ANISOU 5482 N THR D 105 3990 5592 3467 90 -66 -748 N ATOM 5483 CA THR D 105 -7.862 127.544 8.364 1.00 34.51 C ANISOU 5483 CA THR D 105 4001 5524 3588 88 -103 -737 C ATOM 5484 C THR D 105 -9.108 127.314 7.499 1.00 35.03 C ANISOU 5484 C THR D 105 4008 5675 3627 116 -93 -773 C ATOM 5485 O THR D 105 -9.003 127.148 6.277 1.00 35.28 O ANISOU 5485 O THR D 105 3980 5841 3583 138 -111 -716 O ATOM 5486 CB THR D 105 -7.232 128.930 8.053 1.00 35.33 C ANISOU 5486 CB THR D 105 4063 5585 3777 66 -191 -575 C ATOM 5487 OG1 THR D 105 -6.174 129.197 8.972 1.00 35.41 O ANISOU 5487 OG1 THR D 105 4124 5488 3840 24 -235 -550 O ATOM 5488 CG2 THR D 105 -8.263 130.055 8.158 1.00 35.73 C ANISOU 5488 CG2 THR D 105 4119 5531 3928 94 -247 -573 C ATOM 5489 N VAL D 106 -10.279 127.286 8.135 1.00 35.18 N ANISOU 5489 N VAL D 106 4036 5633 3697 126 -68 -861 N ATOM 5490 CA VAL D 106 -11.549 127.271 7.419 1.00 35.88 C ANISOU 5490 CA VAL D 106 4043 5793 3796 145 -81 -878 C ATOM 5491 C VAL D 106 -11.934 128.725 7.210 1.00 36.75 C ANISOU 5491 C VAL D 106 4115 5862 3987 191 -137 -794 C ATOM 5492 O VAL D 106 -12.313 129.417 8.163 1.00 36.83 O ANISOU 5492 O VAL D 106 4162 5762 4072 232 -131 -824 O ATOM 5493 CB VAL D 106 -12.647 126.510 8.186 1.00 36.05 C ANISOU 5493 CB VAL D 106 4055 5796 3847 129 -21 -978 C ATOM 5494 CG1 VAL D 106 -13.983 126.600 7.453 1.00 37.02 C ANISOU 5494 CG1 VAL D 106 4061 5998 4007 141 -54 -975 C ATOM 5495 CG2 VAL D 106 -12.238 125.056 8.346 1.00 35.61 C ANISOU 5495 CG2 VAL D 106 4054 5748 3730 73 7 -1046 C ATOM 5496 N LEU D 107 -11.830 129.169 5.957 1.00 37.61 N ANISOU 5496 N LEU D 107 4162 6060 4068 204 -196 -689 N ATOM 5497 CA LEU D 107 -11.912 130.589 5.611 1.00 38.60 C ANISOU 5497 CA LEU D 107 4261 6131 4273 237 -272 -567 C ATOM 5498 C LEU D 107 -13.269 131.205 5.953 1.00 39.37 C ANISOU 5498 C LEU D 107 4329 6173 4456 308 -287 -618 C ATOM 5499 O LEU D 107 -14.285 130.754 5.446 1.00 39.87 O ANISOU 5499 O LEU D 107 4311 6340 4498 328 -278 -658 O ATOM 5500 CB LEU D 107 -11.621 130.807 4.123 1.00 39.28 C ANISOU 5500 CB LEU D 107 4276 6362 4287 244 -319 -424 C ATOM 5501 CG LEU D 107 -10.244 130.398 3.584 1.00 39.19 C ANISOU 5501 CG LEU D 107 4262 6457 4173 213 -297 -327 C ATOM 5502 CD1 LEU D 107 -10.235 130.563 2.069 1.00 40.36 C ANISOU 5502 CD1 LEU D 107 4333 6793 4210 259 -326 -193 C ATOM 5503 CD2 LEU D 107 -9.118 131.200 4.224 1.00 39.36 C ANISOU 5503 CD2 LEU D 107 4310 6355 4292 155 -327 -210 C ATOM 5504 N GLY D 108 -13.262 132.208 6.831 1.00 56.63 N ANISOU 5504 N GLY D 108 6109 10872 4537 -3927 -2139 1138 N ATOM 5505 CA GLY D 108 -14.445 133.010 7.163 1.00 58.67 C ANISOU 5505 CA GLY D 108 5900 11273 5119 -3784 -2366 1341 C ATOM 5506 C GLY D 108 -14.194 134.500 7.012 1.00 59.06 C ANISOU 5506 C GLY D 108 5754 11225 5461 -3493 -2548 1550 C ATOM 5507 O GLY D 108 -15.092 135.308 7.260 1.00 61.34 O ANISOU 5507 O GLY D 108 5621 11569 6115 -3318 -2749 1708 O ATOM 5508 N ASN D 113 -2.358 140.066 4.260 1.00 60.71 N ANISOU 5508 N ASN D 113 7864 10317 4887 -3121 -1689 1350 N ATOM 5509 CA ASN D 113 -2.527 141.512 4.360 1.00 61.70 C ANISOU 5509 CA ASN D 113 7858 10316 5269 -2968 -1967 1686 C ATOM 5510 C ASN D 113 -2.054 142.104 5.711 1.00 58.56 C ANISOU 5510 C ASN D 113 7323 9648 5278 -2487 -1807 1564 C ATOM 5511 O ASN D 113 -2.753 142.934 6.306 1.00 58.69 O ANISOU 5511 O ASN D 113 7111 9514 5676 -2221 -1993 1738 O ATOM 5512 CB ASN D 113 -4.020 141.857 4.137 1.00 64.07 C ANISOU 5512 CB ASN D 113 7937 10659 5747 -2990 -2367 2029 C ATOM 5513 CG ASN D 113 -4.961 140.951 4.935 1.00 62.92 C ANISOU 5513 CG ASN D 113 7608 10529 5771 -2807 -2274 1861 C ATOM 5514 OD1 ASN D 113 -4.565 139.883 5.408 1.00 60.84 O ANISOU 5514 OD1 ASN D 113 7446 10276 5394 -2773 -1952 1526 O ATOM 5515 ND2 ASN D 113 -6.210 141.376 5.087 1.00 64.32 N ANISOU 5515 ND2 ASN D 113 7499 10697 6244 -2698 -2568 2098 N ATOM 5516 N PRO D 114 -0.869 141.686 6.203 1.00 56.07 N ANISOU 5516 N PRO D 114 7128 9273 4902 -2386 -1465 1252 N ATOM 5517 CA PRO D 114 -0.424 142.214 7.499 1.00 53.59 C ANISOU 5517 CA PRO D 114 6696 8737 4928 -1984 -1328 1144 C ATOM 5518 C PRO D 114 0.081 143.655 7.410 1.00 54.47 C ANISOU 5518 C PRO D 114 6803 8715 5179 -1921 -1463 1342 C ATOM 5519 O PRO D 114 0.730 144.009 6.433 1.00 56.53 O ANISOU 5519 O PRO D 114 7233 9062 5183 -2205 -1516 1446 O ATOM 5520 CB PRO D 114 0.719 141.273 7.890 1.00 51.46 C ANISOU 5520 CB PRO D 114 6559 8459 4536 -1951 -979 794 C ATOM 5521 CG PRO D 114 1.248 140.744 6.605 1.00 53.08 C ANISOU 5521 CG PRO D 114 6963 8847 4357 -2338 -915 720 C ATOM 5522 CD PRO D 114 0.159 140.835 5.573 1.00 56.03 C ANISOU 5522 CD PRO D 114 7349 9394 4548 -2643 -1203 985 C ATOM 5523 N THR D 115 -0.264 144.477 8.401 1.00 54.05 N ANISOU 5523 N THR D 115 6557 8458 5522 -1590 -1515 1385 N ATOM 5524 CA THR D 115 0.397 145.764 8.628 1.00 53.66 C ANISOU 5524 CA THR D 115 6511 8217 5661 -1471 -1564 1480 C ATOM 5525 C THR D 115 1.588 145.470 9.534 1.00 50.47 C ANISOU 5525 C THR D 115 6177 7767 5232 -1319 -1223 1170 C ATOM 5526 O THR D 115 1.414 144.919 10.623 1.00 48.13 O ANISOU 5526 O THR D 115 5779 7438 5069 -1104 -1051 962 O ATOM 5527 CB THR D 115 -0.529 146.783 9.324 1.00 55.10 C ANISOU 5527 CB THR D 115 6433 8173 6331 -1179 -1751 1607 C ATOM 5528 OG1 THR D 115 -1.742 146.927 8.577 1.00 58.38 O ANISOU 5528 OG1 THR D 115 6718 8626 6839 -1283 -2091 1893 O ATOM 5529 CG2 THR D 115 0.142 148.154 9.446 1.00 56.17 C ANISOU 5529 CG2 THR D 115 6596 8070 6675 -1091 -1828 1716 C ATOM 5530 N VAL D 116 2.788 145.822 9.076 1.00 49.87 N ANISOU 5530 N VAL D 116 6268 7709 4973 -1466 -1142 1154 N ATOM 5531 CA VAL D 116 4.029 145.572 9.814 1.00 46.87 C ANISOU 5531 CA VAL D 116 5936 7301 4571 -1352 -851 885 C ATOM 5532 C VAL D 116 4.609 146.893 10.308 1.00 46.63 C ANISOU 5532 C VAL D 116 5888 7087 4744 -1226 -882 953 C ATOM 5533 O VAL D 116 4.833 147.806 9.507 1.00 48.36 O ANISOU 5533 O VAL D 116 6194 7275 4906 -1406 -1051 1172 O ATOM 5534 CB VAL D 116 5.084 144.856 8.934 1.00 47.29 C ANISOU 5534 CB VAL D 116 6158 7538 4273 -1628 -676 735 C ATOM 5535 CG1 VAL D 116 6.300 144.457 9.766 1.00 45.43 C ANISOU 5535 CG1 VAL D 116 5910 7261 4090 -1471 -399 452 C ATOM 5536 CG2 VAL D 116 4.484 143.630 8.256 1.00 47.78 C ANISOU 5536 CG2 VAL D 116 6264 7767 4122 -1813 -658 663 C ATOM 5537 N THR D 117 4.840 146.986 11.621 1.00 43.78 N ANISOU 5537 N THR D 117 5427 6608 4599 -959 -732 775 N ATOM 5538 CA THR D 117 5.553 148.102 12.229 1.00 43.57 C ANISOU 5538 CA THR D 117 5397 6418 4741 -854 -701 763 C ATOM 5539 C THR D 117 6.801 147.555 12.914 1.00 41.08 C ANISOU 5539 C THR D 117 5121 6169 4320 -816 -442 516 C ATOM 5540 O THR D 117 6.715 146.612 13.706 1.00 40.05 O ANISOU 5540 O THR D 117 4932 6085 4202 -700 -314 347 O ATOM 5541 CB THR D 117 4.704 148.832 13.288 1.00 43.71 C ANISOU 5541 CB THR D 117 5236 6237 5133 -594 -750 743 C ATOM 5542 OG1 THR D 117 3.396 149.068 12.774 1.00 46.16 O ANISOU 5542 OG1 THR D 117 5435 6494 5610 -579 -987 935 O ATOM 5543 CG2 THR D 117 5.347 150.172 13.673 1.00 44.81 C ANISOU 5543 CG2 THR D 117 5395 6170 5461 -537 -763 760 C ATOM 5544 N LEU D 118 7.948 148.149 12.598 1.00 40.54 N ANISOU 5544 N LEU D 118 5144 6102 4157 -935 -393 519 N ATOM 5545 CA LEU D 118 9.224 147.789 13.203 1.00 38.79 C ANISOU 5545 CA LEU D 118 4923 5936 3880 -903 -182 309 C ATOM 5546 C LEU D 118 9.686 148.956 14.061 1.00 38.03 C ANISOU 5546 C LEU D 118 4804 5687 3958 -806 -178 307 C ATOM 5547 O LEU D 118 9.829 150.074 13.566 1.00 39.90 O ANISOU 5547 O LEU D 118 5109 5828 4225 -911 -289 459 O ATOM 5548 CB LEU D 118 10.257 147.488 12.119 1.00 40.31 C ANISOU 5548 CB LEU D 118 5207 6295 3813 -1155 -88 260 C ATOM 5549 CG LEU D 118 11.705 147.212 12.536 1.00 40.26 C ANISOU 5549 CG LEU D 118 5158 6355 3783 -1145 115 48 C ATOM 5550 CD1 LEU D 118 11.792 146.056 13.522 1.00 38.97 C ANISOU 5550 CD1 LEU D 118 4888 6178 3739 -936 216 -133 C ATOM 5551 CD2 LEU D 118 12.540 146.932 11.299 1.00 42.00 C ANISOU 5551 CD2 LEU D 118 5437 6767 3755 -1430 230 -37 C ATOM 5552 N PHE D 119 9.898 148.692 15.347 1.00 35.39 N ANISOU 5552 N PHE D 119 4389 5328 3731 -641 -65 144 N ATOM 5553 CA PHE D 119 10.389 149.690 16.287 1.00 34.88 C ANISOU 5553 CA PHE D 119 4304 5145 3801 -580 -28 89 C ATOM 5554 C PHE D 119 11.867 149.445 16.566 1.00 33.86 C ANISOU 5554 C PHE D 119 4184 5123 3556 -648 101 -27 C ATOM 5555 O PHE D 119 12.257 148.310 16.830 1.00 32.60 O ANISOU 5555 O PHE D 119 3976 5079 3334 -614 179 -131 O ATOM 5556 CB PHE D 119 9.630 149.602 17.602 1.00 34.44 C ANISOU 5556 CB PHE D 119 4147 5034 3904 -416 14 -28 C ATOM 5557 CG PHE D 119 8.180 149.974 17.493 1.00 35.47 C ANISOU 5557 CG PHE D 119 4202 5048 4225 -323 -92 38 C ATOM 5558 CD1 PHE D 119 7.783 151.312 17.533 1.00 37.05 C ANISOU 5558 CD1 PHE D 119 4372 5028 4678 -271 -175 84 C ATOM 5559 CD2 PHE D 119 7.208 148.993 17.369 1.00 35.07 C ANISOU 5559 CD2 PHE D 119 4090 5091 4144 -285 -116 48 C ATOM 5560 CE1 PHE D 119 6.440 151.657 17.452 1.00 38.64 C ANISOU 5560 CE1 PHE D 119 4446 5099 5137 -155 -285 130 C ATOM 5561 CE2 PHE D 119 5.866 149.336 17.286 1.00 36.38 C ANISOU 5561 CE2 PHE D 119 4138 5167 4516 -198 -217 100 C ATOM 5562 CZ PHE D 119 5.483 150.667 17.325 1.00 38.32 C ANISOU 5562 CZ PHE D 119 4318 5190 5053 -120 -305 138 C ATOM 5563 N PRO D 120 12.692 150.505 16.533 1.00 33.95 N ANISOU 5563 N PRO D 120 4243 5080 3574 -743 107 -6 N ATOM 5564 CA PRO D 120 14.082 150.340 16.965 1.00 33.33 C ANISOU 5564 CA PRO D 120 4128 5113 3424 -798 222 -126 C ATOM 5565 C PRO D 120 14.184 150.312 18.494 1.00 32.19 C ANISOU 5565 C PRO D 120 3914 4943 3374 -687 263 -240 C ATOM 5566 O PRO D 120 13.183 150.559 19.177 1.00 31.36 O ANISOU 5566 O PRO D 120 3799 4738 3377 -591 237 -255 O ATOM 5567 CB PRO D 120 14.772 151.581 16.394 1.00 35.18 C ANISOU 5567 CB PRO D 120 4451 5297 3620 -978 198 -45 C ATOM 5568 CG PRO D 120 13.704 152.616 16.341 1.00 36.51 C ANISOU 5568 CG PRO D 120 4688 5233 3951 -937 56 92 C ATOM 5569 CD PRO D 120 12.380 151.907 16.202 1.00 35.68 C ANISOU 5569 CD PRO D 120 4538 5111 3909 -800 -12 133 C ATOM 5570 N PRO D 121 15.383 150.012 19.037 1.00 31.79 N ANISOU 5570 N PRO D 121 3798 5001 3279 -726 325 -325 N ATOM 5571 CA PRO D 121 15.577 150.130 20.483 1.00 31.71 C ANISOU 5571 CA PRO D 121 3746 4996 3306 -701 334 -401 C ATOM 5572 C PRO D 121 15.275 151.553 20.959 1.00 32.46 C ANISOU 5572 C PRO D 121 3912 4947 3474 -747 342 -428 C ATOM 5573 O PRO D 121 15.659 152.512 20.283 1.00 33.27 O ANISOU 5573 O PRO D 121 4082 4967 3591 -839 330 -376 O ATOM 5574 CB PRO D 121 17.071 149.809 20.665 1.00 32.07 C ANISOU 5574 CB PRO D 121 3700 5175 3310 -774 357 -442 C ATOM 5575 CG PRO D 121 17.449 149.019 19.464 1.00 32.14 C ANISOU 5575 CG PRO D 121 3658 5257 3297 -770 392 -445 C ATOM 5576 CD PRO D 121 16.613 149.576 18.352 1.00 32.44 C ANISOU 5576 CD PRO D 121 3820 5221 3284 -817 387 -367 C ATOM 5577 N SER D 122 14.554 151.689 22.074 1.00 31.93 N ANISOU 5577 N SER D 122 3831 4840 3459 -708 367 -521 N ATOM 5578 CA SER D 122 14.334 153.001 22.679 1.00 33.22 C ANISOU 5578 CA SER D 122 4038 4853 3730 -755 413 -625 C ATOM 5579 C SER D 122 15.647 153.513 23.253 1.00 34.11 C ANISOU 5579 C SER D 122 4170 5038 3751 -917 444 -679 C ATOM 5580 O SER D 122 16.496 152.720 23.674 1.00 33.75 O ANISOU 5580 O SER D 122 4064 5185 3575 -974 426 -664 O ATOM 5581 CB SER D 122 13.292 152.925 23.797 1.00 33.48 C ANISOU 5581 CB SER D 122 4024 4880 3815 -718 485 -783 C ATOM 5582 OG SER D 122 13.734 152.065 24.828 1.00 32.33 O ANISOU 5582 OG SER D 122 3848 4950 3485 -814 503 -825 O ATOM 5583 N SER D 123 15.825 154.829 23.249 1.00 35.65 N ANISOU 5583 N SER D 123 4439 5063 4043 -997 467 -730 N ATOM 5584 CA SER D 123 17.000 155.439 23.870 1.00 36.88 C ANISOU 5584 CA SER D 123 4621 5284 4110 -1184 502 -800 C ATOM 5585 C SER D 123 17.064 155.098 25.366 1.00 37.09 C ANISOU 5585 C SER D 123 4604 5468 4019 -1276 558 -952 C ATOM 5586 O SER D 123 18.151 154.958 25.909 1.00 37.49 O ANISOU 5586 O SER D 123 4626 5693 3926 -1430 534 -947 O ATOM 5587 CB SER D 123 17.008 156.955 23.669 1.00 38.70 C ANISOU 5587 CB SER D 123 4960 5251 4494 -1263 515 -845 C ATOM 5588 OG SER D 123 15.786 157.513 24.093 1.00 39.94 O ANISOU 5588 OG SER D 123 5122 5181 4873 -1156 563 -985 O ATOM 5589 N GLU D 124 15.907 154.944 26.015 1.00 37.89 N ANISOU 5589 N GLU D 124 4691 5535 4171 -1214 624 -1077 N ATOM 5590 CA GLU D 124 15.872 154.455 27.398 1.00 38.69 C ANISOU 5590 CA GLU D 124 4765 5841 4093 -1363 671 -1199 C ATOM 5591 C GLU D 124 16.489 153.062 27.551 1.00 37.61 C ANISOU 5591 C GLU D 124 4564 5944 3782 -1382 539 -1017 C ATOM 5592 O GLU D 124 17.274 152.829 28.477 1.00 38.27 O ANISOU 5592 O GLU D 124 4634 6212 3694 -1579 484 -1006 O ATOM 5593 CB GLU D 124 14.453 154.487 28.012 1.00 40.15 C ANISOU 5593 CB GLU D 124 4925 5979 4350 -1325 796 -1395 C ATOM 5594 CG GLU D 124 14.161 155.853 28.582 1.00 43.24 C ANISOU 5594 CG GLU D 124 5351 6197 4882 -1416 957 -1682 C ATOM 5595 CD GLU D 124 12.792 155.989 29.197 1.00 45.61 C ANISOU 5595 CD GLU D 124 5575 6451 5303 -1384 1127 -1952 C ATOM 5596 OE1 GLU D 124 12.069 154.984 29.359 1.00 44.91 O ANISOU 5596 OE1 GLU D 124 5420 6522 5123 -1346 1124 -1912 O ATOM 5597 OE2 GLU D 124 12.420 157.129 29.544 1.00 49.46 O ANISOU 5597 OE2 GLU D 124 6056 6734 6004 -1409 1280 -2234 O ATOM 5598 N GLU D 125 16.124 152.145 26.653 1.00 36.27 N ANISOU 5598 N GLU D 125 4350 5753 3676 -1192 471 -872 N ATOM 5599 CA GLU D 125 16.659 150.777 26.691 1.00 35.96 C ANISOU 5599 CA GLU D 125 4236 5868 3559 -1171 338 -713 C ATOM 5600 C GLU D 125 18.163 150.755 26.403 1.00 36.18 C ANISOU 5600 C GLU D 125 4192 5969 3586 -1221 259 -628 C ATOM 5601 O GLU D 125 18.909 150.040 27.074 1.00 36.31 O ANISOU 5601 O GLU D 125 4127 6125 3543 -1303 133 -542 O ATOM 5602 CB GLU D 125 15.917 149.847 25.720 1.00 34.86 C ANISOU 5602 CB GLU D 125 4072 5666 3507 -970 310 -622 C ATOM 5603 CG GLU D 125 16.266 148.378 25.929 1.00 35.20 C ANISOU 5603 CG GLU D 125 4045 5810 3520 -946 175 -491 C ATOM 5604 CD GLU D 125 15.752 147.445 24.850 1.00 34.54 C ANISOU 5604 CD GLU D 125 3940 5655 3529 -769 158 -428 C ATOM 5605 OE1 GLU D 125 15.485 147.875 23.702 1.00 34.31 O ANISOU 5605 OE1 GLU D 125 3935 5538 3563 -681 227 -449 O ATOM 5606 OE2 GLU D 125 15.623 146.245 25.160 1.00 35.26 O ANISOU 5606 OE2 GLU D 125 3999 5776 3621 -748 57 -345 O ATOM 5607 N LEU D 126 18.594 151.538 25.415 1.00 36.11 N ANISOU 5607 N LEU D 126 4199 5868 3652 -1192 316 -642 N ATOM 5608 CA LEU D 126 20.027 151.711 25.128 1.00 37.56 C ANISOU 5608 CA LEU D 126 4296 6144 3832 -1279 283 -607 C ATOM 5609 C LEU D 126 20.816 152.244 26.339 1.00 39.34 C ANISOU 5609 C LEU D 126 4510 6487 3949 -1501 244 -648 C ATOM 5610 O LEU D 126 21.925 151.775 26.596 1.00 40.55 O ANISOU 5610 O LEU D 126 4521 6789 4096 -1565 137 -577 O ATOM 5611 CB LEU D 126 20.234 152.611 23.904 1.00 37.43 C ANISOU 5611 CB LEU D 126 4337 6023 3862 -1288 363 -615 C ATOM 5612 CG LEU D 126 19.769 152.011 22.572 1.00 36.48 C ANISOU 5612 CG LEU D 126 4211 5856 3795 -1147 381 -555 C ATOM 5613 CD1 LEU D 126 19.618 153.093 21.512 1.00 37.01 C ANISOU 5613 CD1 LEU D 126 4400 5796 3866 -1220 424 -523 C ATOM 5614 CD2 LEU D 126 20.725 150.922 22.097 1.00 36.89 C ANISOU 5614 CD2 LEU D 126 4085 6057 3874 -1107 365 -545 C ATOM 5615 N GLN D 127 20.233 153.193 27.077 1.00 40.45 N ANISOU 5615 N GLN D 127 4782 6563 4025 -1625 327 -778 N ATOM 5616 CA GLN D 127 20.796 153.675 28.361 1.00 42.80 C ANISOU 5616 CA GLN D 127 5099 6995 4166 -1893 308 -853 C ATOM 5617 C GLN D 127 20.911 152.542 29.414 1.00 43.28 C ANISOU 5617 C GLN D 127 5089 7266 4091 -1988 153 -745 C ATOM 5618 O GLN D 127 21.841 152.526 30.223 1.00 44.47 O ANISOU 5618 O GLN D 127 5185 7592 4118 -2208 33 -688 O ATOM 5619 CB GLN D 127 19.980 154.894 28.921 1.00 44.59 C ANISOU 5619 CB GLN D 127 5480 7081 4381 -2007 476 -1087 C ATOM 5620 CG GLN D 127 20.433 156.282 28.454 1.00 46.21 C ANISOU 5620 CG GLN D 127 5769 7113 4678 -2085 559 -1180 C ATOM 5621 CD GLN D 127 21.942 156.491 28.488 1.00 47.63 C ANISOU 5621 CD GLN D 127 5887 7451 4759 -2274 476 -1101 C ATOM 5622 OE1 GLN D 127 22.499 156.622 29.559 1.00 49.42 O ANISOU 5622 OE1 GLN D 127 6109 7849 4819 -2521 443 -1157 O ATOM 5623 NE2 GLN D 127 22.605 156.533 27.321 1.00 47.95 N ANISOU 5623 NE2 GLN D 127 5873 7461 4885 -2195 445 -980 N ATOM 5624 N ALA D 128 19.996 151.571 29.363 1.00 42.32 N ANISOU 5624 N ALA D 128 4965 7123 3994 -1845 124 -683 N ATOM 5625 CA ALA D 128 20.110 150.345 30.175 1.00 43.82 C ANISOU 5625 CA ALA D 128 5093 7469 4088 -1924 -74 -514 C ATOM 5626 C ALA D 128 21.104 149.292 29.635 1.00 44.42 C ANISOU 5626 C ALA D 128 4984 7558 4335 -1774 -276 -305 C ATOM 5627 O ALA D 128 21.112 148.167 30.125 1.00 45.37 O ANISOU 5627 O ALA D 128 5047 7728 4462 -1783 -475 -132 O ATOM 5628 CB ALA D 128 18.731 149.714 30.366 1.00 42.68 C ANISOU 5628 CB ALA D 128 5023 7293 3901 -1865 -26 -534 C ATOM 5629 N ASN D 129 21.931 149.654 28.647 1.00 45.13 N ANISOU 5629 N ASN D 129 4972 7596 4579 -1656 -225 -335 N ATOM 5630 CA ASN D 129 22.899 148.756 28.011 1.00 46.77 C ANISOU 5630 CA ASN D 129 4957 7808 5006 -1501 -351 -227 C ATOM 5631 C ASN D 129 22.274 147.516 27.366 1.00 46.08 C ANISOU 5631 C ASN D 129 4830 7599 5080 -1257 -382 -171 C ATOM 5632 O ASN D 129 22.809 146.406 27.447 1.00 48.31 O ANISOU 5632 O ASN D 129 4943 7867 5547 -1165 -566 -48 O ATOM 5633 CB ASN D 129 24.039 148.413 28.978 1.00 49.54 C ANISOU 5633 CB ASN D 129 5144 8313 5365 -1663 -601 -76 C ATOM 5634 CG ASN D 129 24.853 149.630 29.364 1.00 51.26 C ANISOU 5634 CG ASN D 129 5369 8661 5448 -1904 -556 -151 C ATOM 5635 OD1 ASN D 129 24.777 150.161 30.492 1.00 53.33 O ANISOU 5635 OD1 ASN D 129 5748 9043 5473 -2185 -605 -149 O ATOM 5636 ND2 ASN D 129 25.643 150.091 28.412 1.00 51.25 N ANISOU 5636 ND2 ASN D 129 5247 8653 5575 -1835 -448 -238 N ATOM 5637 N LYS D 130 21.118 147.719 26.738 1.00 44.04 N ANISOU 5637 N LYS D 130 4722 7233 4777 -1159 -215 -261 N ATOM 5638 CA LYS D 130 20.408 146.663 26.017 1.00 42.52 C ANISOU 5638 CA LYS D 130 4524 6929 4704 -958 -213 -237 C ATOM 5639 C LYS D 130 19.795 147.236 24.757 1.00 40.43 C ANISOU 5639 C LYS D 130 4345 6576 4440 -861 -13 -354 C ATOM 5640 O LYS D 130 19.693 148.451 24.608 1.00 38.52 O ANISOU 5640 O LYS D 130 4197 6325 4113 -945 97 -427 O ATOM 5641 CB LYS D 130 19.343 146.023 26.901 1.00 43.16 C ANISOU 5641 CB LYS D 130 4714 7007 4679 -1009 -301 -152 C ATOM 5642 CG LYS D 130 19.989 145.270 28.052 1.00 45.68 C ANISOU 5642 CG LYS D 130 4954 7407 4995 -1140 -562 32 C ATOM 5643 CD LYS D 130 19.028 144.511 28.932 1.00 46.56 C ANISOU 5643 CD LYS D 130 5179 7539 4970 -1254 -678 151 C ATOM 5644 CE LYS D 130 19.818 143.882 30.064 1.00 49.40 C ANISOU 5644 CE LYS D 130 5470 7986 5312 -1442 -992 387 C ATOM 5645 NZ LYS D 130 18.971 143.011 30.918 1.00 50.65 N ANISOU 5645 NZ LYS D 130 5749 8174 5320 -1609 -1148 553 N ATOM 5646 N ALA D 131 19.402 146.348 23.851 1.00 39.30 N ANISOU 5646 N ALA D 131 4174 6357 4400 -706 10 -360 N ATOM 5647 CA ALA D 131 18.776 146.752 22.604 1.00 38.51 C ANISOU 5647 CA ALA D 131 4160 6198 4274 -655 156 -430 C ATOM 5648 C ALA D 131 17.850 145.649 22.097 1.00 37.60 C ANISOU 5648 C ALA D 131 4071 6010 4204 -533 145 -415 C ATOM 5649 O ALA D 131 18.274 144.509 21.927 1.00 38.67 O ANISOU 5649 O ALA D 131 4094 6120 4478 -449 91 -419 O ATOM 5650 CB ALA D 131 19.842 147.080 21.578 1.00 39.56 C ANISOU 5650 CB ALA D 131 4197 6383 4450 -687 251 -511 C ATOM 5651 N THR D 132 16.581 145.995 21.898 1.00 35.92 N ANISOU 5651 N THR D 132 3991 5748 3907 -525 187 -404 N ATOM 5652 CA THR D 132 15.581 145.075 21.368 1.00 35.23 C ANISOU 5652 CA THR D 132 3942 5610 3833 -444 180 -387 C ATOM 5653 C THR D 132 14.863 145.764 20.220 1.00 34.26 C ANISOU 5653 C THR D 132 3906 5459 3654 -456 257 -397 C ATOM 5654 O THR D 132 14.320 146.854 20.397 1.00 34.23 O ANISOU 5654 O THR D 132 3967 5417 3622 -487 269 -378 O ATOM 5655 CB THR D 132 14.542 144.663 22.440 1.00 34.77 C ANISOU 5655 CB THR D 132 3936 5548 3728 -455 109 -330 C ATOM 5656 OG1 THR D 132 15.207 144.325 23.661 1.00 35.12 O ANISOU 5656 OG1 THR D 132 3933 5642 3769 -524 1 -275 O ATOM 5657 CG2 THR D 132 13.721 143.455 21.974 1.00 34.81 C ANISOU 5657 CG2 THR D 132 3960 5506 3761 -391 77 -303 C ATOM 5658 N LEU D 133 14.885 145.139 19.046 1.00 34.20 N ANISOU 5658 N LEU D 133 3893 5460 3643 -449 298 -430 N ATOM 5659 CA LEU D 133 14.027 145.545 17.937 1.00 34.31 C ANISOU 5659 CA LEU D 133 4001 5466 3571 -500 317 -390 C ATOM 5660 C LEU D 133 12.730 144.780 18.078 1.00 33.07 C ANISOU 5660 C LEU D 133 3874 5273 3418 -436 261 -348 C ATOM 5661 O LEU D 133 12.747 143.567 18.301 1.00 32.23 O ANISOU 5661 O LEU D 133 3731 5159 3353 -389 248 -387 O ATOM 5662 CB LEU D 133 14.650 145.235 16.572 1.00 35.81 C ANISOU 5662 CB LEU D 133 4184 5733 3690 -604 405 -466 C ATOM 5663 CG LEU D 133 15.817 146.119 16.129 1.00 37.26 C ANISOU 5663 CG LEU D 133 4347 5991 3820 -736 482 -506 C ATOM 5664 CD1 LEU D 133 17.089 145.768 16.877 1.00 38.22 C ANISOU 5664 CD1 LEU D 133 4309 6144 4067 -677 521 -613 C ATOM 5665 CD2 LEU D 133 16.036 145.971 14.631 1.00 38.67 C ANISOU 5665 CD2 LEU D 133 4561 6284 3847 -922 580 -572 C ATOM 5666 N VAL D 134 11.617 145.491 17.912 1.00 32.76 N ANISOU 5666 N VAL D 134 3887 5197 3365 -440 215 -268 N ATOM 5667 CA VAL D 134 10.286 144.932 18.088 1.00 32.06 C ANISOU 5667 CA VAL D 134 3796 5097 3287 -395 165 -232 C ATOM 5668 C VAL D 134 9.517 145.052 16.773 1.00 32.40 C ANISOU 5668 C VAL D 134 3887 5151 3273 -460 112 -148 C ATOM 5669 O VAL D 134 9.206 146.153 16.314 1.00 31.41 O ANISOU 5669 O VAL D 134 3783 4975 3177 -491 49 -52 O ATOM 5670 CB VAL D 134 9.515 145.655 19.211 1.00 32.07 C ANISOU 5670 CB VAL D 134 3756 5058 3369 -344 155 -239 C ATOM 5671 CG1 VAL D 134 8.177 144.971 19.451 1.00 32.08 C ANISOU 5671 CG1 VAL D 134 3721 5088 3378 -322 126 -230 C ATOM 5672 CG2 VAL D 134 10.346 145.703 20.490 1.00 31.97 C ANISOU 5672 CG2 VAL D 134 3722 5071 3353 -357 195 -308 C ATOM 5673 N CYS D 135 9.215 143.903 16.176 1.00 33.36 N ANISOU 5673 N CYS D 135 4029 5325 3321 -501 115 -173 N ATOM 5674 CA CYS D 135 8.473 143.846 14.932 1.00 34.36 C ANISOU 5674 CA CYS D 135 4210 5502 3345 -616 53 -92 C ATOM 5675 C CYS D 135 7.041 143.417 15.232 1.00 34.83 C ANISOU 5675 C CYS D 135 4227 5560 3447 -571 -29 -34 C ATOM 5676 O CYS D 135 6.796 142.263 15.587 1.00 34.33 O ANISOU 5676 O CYS D 135 4160 5514 3370 -557 1 -104 O ATOM 5677 CB CYS D 135 9.142 142.867 13.978 1.00 35.67 C ANISOU 5677 CB CYS D 135 4425 5747 3381 -742 145 -210 C ATOM 5678 SG CYS D 135 8.370 142.825 12.348 1.00 37.16 S ANISOU 5678 SG CYS D 135 4712 6056 3353 -989 74 -119 S ATOM 5679 N LEU D 136 6.108 144.361 15.103 1.00 36.06 N ANISOU 5679 N LEU D 136 4335 5680 3688 -550 -144 94 N ATOM 5680 CA LEU D 136 4.674 144.087 15.307 1.00 36.81 C ANISOU 5680 CA LEU D 136 4337 5793 3855 -513 -225 142 C ATOM 5681 C LEU D 136 3.968 143.852 13.967 1.00 38.09 C ANISOU 5681 C LEU D 136 4537 6031 3905 -664 -360 280 C ATOM 5682 O LEU D 136 4.090 144.642 13.035 1.00 39.46 O ANISOU 5682 O LEU D 136 4759 6193 4042 -764 -475 426 O ATOM 5683 CB LEU D 136 3.969 145.153 16.172 1.00 37.66 C ANISOU 5683 CB LEU D 136 4300 5806 4201 -373 -254 145 C ATOM 5684 CG LEU D 136 4.686 145.544 17.468 1.00 36.99 C ANISOU 5684 CG LEU D 136 4198 5673 4185 -288 -118 -1 C ATOM 5685 CD1 LEU D 136 3.902 146.525 18.330 1.00 38.51 C ANISOU 5685 CD1 LEU D 136 4234 5781 4618 -179 -97 -76 C ATOM 5686 CD2 LEU D 136 5.065 144.321 18.286 1.00 36.00 C ANISOU 5686 CD2 LEU D 136 4111 5637 3930 -320 -18 -105 C ATOM 5687 N ILE D 137 3.254 142.732 13.889 1.00 38.10 N ANISOU 5687 N ILE D 137 4531 6116 3827 -719 -360 245 N ATOM 5688 CA ILE D 137 2.536 142.292 12.693 1.00 39.63 C ANISOU 5688 CA ILE D 137 4767 6417 3873 -906 -481 351 C ATOM 5689 C ILE D 137 1.060 142.258 13.067 1.00 40.43 C ANISOU 5689 C ILE D 137 4703 6545 4113 -848 -594 425 C ATOM 5690 O ILE D 137 0.695 141.570 14.019 1.00 39.51 O ANISOU 5690 O ILE D 137 4527 6443 4042 -779 -500 308 O ATOM 5691 CB ILE D 137 3.004 140.879 12.272 1.00 39.17 C ANISOU 5691 CB ILE D 137 4838 6430 3616 -1044 -358 196 C ATOM 5692 CG1 ILE D 137 4.537 140.794 12.252 1.00 38.56 C ANISOU 5692 CG1 ILE D 137 4846 6309 3496 -1036 -194 44 C ATOM 5693 CG2 ILE D 137 2.448 140.502 10.908 1.00 41.14 C ANISOU 5693 CG2 ILE D 137 5166 6816 3650 -1307 -457 275 C ATOM 5694 CD1 ILE D 137 5.076 139.385 12.249 1.00 38.71 C ANISOU 5694 CD1 ILE D 137 4927 6309 3472 -1072 -53 -164 C ATOM 5695 N SER D 138 0.222 142.998 12.334 1.00 42.31 N ANISOU 5695 N SER D 138 4855 6795 4427 -897 -810 630 N ATOM 5696 CA SER D 138 -1.190 143.162 12.689 1.00 43.91 C ANISOU 5696 CA SER D 138 4828 7012 4845 -812 -930 694 C ATOM 5697 C SER D 138 -2.147 142.993 11.518 1.00 45.81 C ANISOU 5697 C SER D 138 5034 7369 5004 -1003 -1175 907 C ATOM 5698 O SER D 138 -1.779 143.211 10.374 1.00 47.08 O ANISOU 5698 O SER D 138 5339 7570 4980 -1202 -1309 1069 O ATOM 5699 CB SER D 138 -1.432 144.551 13.277 1.00 45.07 C ANISOU 5699 CB SER D 138 4785 6986 5352 -594 -993 732 C ATOM 5700 OG SER D 138 -0.571 144.810 14.357 1.00 44.37 O ANISOU 5700 OG SER D 138 4731 6809 5319 -457 -779 539 O ATOM 5701 N ASP D 139 -3.380 142.601 11.840 1.00 47.06 N ANISOU 5701 N ASP D 139 4994 7605 5281 -977 -1232 904 N ATOM 5702 CA ASP D 139 -4.518 142.604 10.909 1.00 49.85 C ANISOU 5702 CA ASP D 139 5225 8067 5647 -1125 -1511 1131 C ATOM 5703 C ASP D 139 -4.299 141.696 9.700 1.00 49.91 C ANISOU 5703 C ASP D 139 5477 8248 5239 -1468 -1566 1200 C ATOM 5704 O ASP D 139 -4.495 142.113 8.554 1.00 52.96 O ANISOU 5704 O ASP D 139 5906 8696 5520 -1674 -1823 1453 O ATOM 5705 CB ASP D 139 -4.876 144.035 10.464 1.00 52.98 C ANISOU 5705 CB ASP D 139 5456 8316 6357 -1028 -1803 1394 C ATOM 5706 CG ASP D 139 -5.504 144.855 11.571 1.00 54.40 C ANISOU 5706 CG ASP D 139 5310 8335 7026 -704 -1768 1289 C ATOM 5707 OD1 ASP D 139 -6.545 144.429 12.110 1.00 55.83 O ANISOU 5707 OD1 ASP D 139 5246 8613 7353 -646 -1730 1182 O ATOM 5708 OD2 ASP D 139 -4.976 145.941 11.885 1.00 55.68 O ANISOU 5708 OD2 ASP D 139 5450 8276 7428 -531 -1768 1292 O ATOM 5709 N PHE D 140 -3.901 140.453 9.955 1.00 47.07 N ANISOU 5709 N PHE D 140 5278 7958 4650 -1556 -1335 973 N ATOM 5710 CA PHE D 140 -3.760 139.475 8.875 1.00 47.30 C ANISOU 5710 CA PHE D 140 5522 8139 4312 -1890 -1337 955 C ATOM 5711 C PHE D 140 -4.651 138.259 9.061 1.00 46.80 C ANISOU 5711 C PHE D 140 5426 8189 4167 -2004 -1302 860 C ATOM 5712 O PHE D 140 -5.041 137.920 10.185 1.00 46.04 O ANISOU 5712 O PHE D 140 5205 8049 4241 -1833 -1192 745 O ATOM 5713 CB PHE D 140 -2.305 139.063 8.649 1.00 45.65 C ANISOU 5713 CB PHE D 140 5567 7881 3898 -1956 -1103 754 C ATOM 5714 CG PHE D 140 -1.635 138.450 9.845 1.00 43.18 C ANISOU 5714 CG PHE D 140 5276 7429 3700 -1737 -846 504 C ATOM 5715 CD1 PHE D 140 -0.985 139.247 10.783 1.00 41.53 C ANISOU 5715 CD1 PHE D 140 4999 7077 3702 -1471 -766 475 C ATOM 5716 CD2 PHE D 140 -1.611 137.069 10.011 1.00 42.80 C ANISOU 5716 CD2 PHE D 140 5331 7382 3549 -1826 -707 312 C ATOM 5717 CE1 PHE D 140 -0.342 138.680 11.871 1.00 39.57 C ANISOU 5717 CE1 PHE D 140 4779 6722 3534 -1317 -574 286 C ATOM 5718 CE2 PHE D 140 -0.977 136.498 11.098 1.00 40.69 C ANISOU 5718 CE2 PHE D 140 5090 6967 3405 -1650 -533 141 C ATOM 5719 CZ PHE D 140 -0.338 137.305 12.029 1.00 39.55 C ANISOU 5719 CZ PHE D 140 4872 6713 3442 -1405 -476 141 C ATOM 5720 N TYR D 141 -4.968 137.631 7.932 1.00 47.70 N ANISOU 5720 N TYR D 141 5664 8466 3993 -2343 -1400 910 N ATOM 5721 CA TYR D 141 -5.788 136.423 7.880 1.00 48.05 C ANISOU 5721 CA TYR D 141 5721 8629 3907 -2532 -1385 826 C ATOM 5722 C TYR D 141 -5.505 135.709 6.539 1.00 49.66 C ANISOU 5722 C TYR D 141 6179 8974 3718 -2941 -1384 772 C ATOM 5723 O TYR D 141 -5.475 136.398 5.519 1.00 51.53 O ANISOU 5723 O TYR D 141 6454 9329 3797 -3144 -1571 968 O ATOM 5724 CB TYR D 141 -7.262 136.805 7.978 1.00 49.44 C ANISOU 5724 CB TYR D 141 5599 8927 4258 -2521 -1638 1042 C ATOM 5725 CG TYR D 141 -8.179 135.631 8.010 1.00 50.06 C ANISOU 5725 CG TYR D 141 5661 9145 4213 -2725 -1630 968 C ATOM 5726 CD1 TYR D 141 -8.497 135.007 9.214 1.00 48.38 C ANISOU 5726 CD1 TYR D 141 5364 8882 4136 -2586 -1459 803 C ATOM 5727 CD2 TYR D 141 -8.733 135.130 6.837 1.00 52.26 C ANISOU 5727 CD2 TYR D 141 6025 9624 4207 -3108 -1799 1068 C ATOM 5728 CE1 TYR D 141 -9.342 133.932 9.250 1.00 49.43 C ANISOU 5728 CE1 TYR D 141 5495 9139 4148 -2806 -1459 747 C ATOM 5729 CE2 TYR D 141 -9.576 134.053 6.865 1.00 53.27 C ANISOU 5729 CE2 TYR D 141 6145 9876 4218 -3318 -1792 994 C ATOM 5730 CZ TYR D 141 -9.878 133.465 8.072 1.00 51.74 C ANISOU 5730 CZ TYR D 141 5864 9609 4186 -3158 -1623 838 C ATOM 5731 OH TYR D 141 -10.716 132.415 8.095 1.00 53.22 O ANISOU 5731 OH TYR D 141 6054 9917 4249 -3397 -1626 780 O ATOM 5732 N PRO D 142 -5.291 134.380 6.501 1.00 49.38 N ANISOU 5732 N PRO D 142 6320 8920 3522 -3095 -1186 509 N ATOM 5733 CA PRO D 142 -5.292 133.483 7.669 1.00 47.63 C ANISOU 5733 CA PRO D 142 6090 8538 3469 -2910 -1007 318 C ATOM 5734 C PRO D 142 -4.173 133.746 8.686 1.00 45.16 C ANISOU 5734 C PRO D 142 5790 7994 3373 -2572 -819 193 C ATOM 5735 O PRO D 142 -3.198 134.441 8.379 1.00 44.13 O ANISOU 5735 O PRO D 142 5714 7816 3238 -2499 -765 179 O ATOM 5736 CB PRO D 142 -5.106 132.092 7.046 1.00 48.93 C ANISOU 5736 CB PRO D 142 6491 8696 3406 -3207 -870 75 C ATOM 5737 CG PRO D 142 -5.675 132.198 5.665 1.00 52.01 C ANISOU 5737 CG PRO D 142 6934 9345 3482 -3603 -1038 188 C ATOM 5738 CD PRO D 142 -5.510 133.641 5.238 1.00 52.26 C ANISOU 5738 CD PRO D 142 6866 9469 3523 -3545 -1218 451 C ATOM 5739 N GLY D 143 -4.334 133.186 9.884 1.00 44.16 N ANISOU 5739 N GLY D 143 5616 7750 3414 -2413 -735 120 N ATOM 5740 CA GLY D 143 -3.415 133.417 11.003 1.00 42.74 C ANISOU 5740 CA GLY D 143 5427 7378 3434 -2124 -601 43 C ATOM 5741 C GLY D 143 -2.168 132.553 10.962 1.00 42.84 C ANISOU 5741 C GLY D 143 5640 7188 3449 -2114 -427 -181 C ATOM 5742 O GLY D 143 -1.965 131.684 11.813 1.00 42.50 O ANISOU 5742 O GLY D 143 5650 6980 3516 -2055 -365 -264 O ATOM 5743 N ALA D 144 -1.319 132.810 9.978 1.00 43.80 N ANISOU 5743 N ALA D 144 5856 7319 3467 -2186 -358 -275 N ATOM 5744 CA ALA D 144 -0.073 132.065 9.813 1.00 44.52 C ANISOU 5744 CA ALA D 144 6082 7222 3611 -2167 -168 -539 C ATOM 5745 C ALA D 144 0.897 132.892 8.975 1.00 45.14 C ANISOU 5745 C ALA D 144 6182 7373 3596 -2196 -85 -600 C ATOM 5746 O ALA D 144 0.545 133.379 7.900 1.00 46.14 O ANISOU 5746 O ALA D 144 6342 7710 3480 -2437 -153 -524 O ATOM 5747 CB ALA D 144 -0.341 130.705 9.174 1.00 46.31 C ANISOU 5747 CB ALA D 144 6455 7400 3742 -2417 -103 -739 C ATOM 5748 N VAL D 145 2.107 133.066 9.498 1.00 44.58 N ANISOU 5748 N VAL D 145 6087 7144 3707 -1979 39 -713 N ATOM 5749 CA VAL D 145 3.106 133.951 8.908 1.00 45.00 C ANISOU 5749 CA VAL D 145 6136 7270 3694 -1990 126 -762 C ATOM 5750 C VAL D 145 4.489 133.388 9.185 1.00 45.79 C ANISOU 5750 C VAL D 145 6228 7170 3999 -1845 328 -1040 C ATOM 5751 O VAL D 145 4.680 132.652 10.158 1.00 44.63 O ANISOU 5751 O VAL D 145 6051 6800 4106 -1650 327 -1084 O ATOM 5752 CB VAL D 145 3.049 135.402 9.490 1.00 43.24 C ANISOU 5752 CB VAL D 145 5801 7094 3533 -1808 -3 -497 C ATOM 5753 CG1 VAL D 145 1.817 136.143 8.995 1.00 43.88 C ANISOU 5753 CG1 VAL D 145 5846 7355 3470 -1947 -219 -227 C ATOM 5754 CG2 VAL D 145 3.105 135.401 11.014 1.00 41.12 C ANISOU 5754 CG2 VAL D 145 5437 6661 3528 -1510 -25 -440 C ATOM 5755 N THR D 146 5.452 133.769 8.347 1.00 47.48 N ANISOU 5755 N THR D 146 6454 7474 4113 -1958 484 -1211 N ATOM 5756 CA THR D 146 6.866 133.484 8.594 1.00 48.40 C ANISOU 5756 CA THR D 146 6495 7430 4465 -1798 675 -1473 C ATOM 5757 C THR D 146 7.596 134.810 8.792 1.00 47.80 C ANISOU 5757 C THR D 146 6343 7447 4374 -1704 667 -1343 C ATOM 5758 O THR D 146 7.388 135.756 8.028 1.00 47.95 O ANISOU 5758 O THR D 146 6413 7683 4121 -1910 624 -1211 O ATOM 5759 CB THR D 146 7.510 132.723 7.414 1.00 51.96 C ANISOU 5759 CB THR D 146 6988 7920 4834 -2042 935 -1884 C ATOM 5760 OG1 THR D 146 6.638 131.672 6.975 1.00 53.12 O ANISOU 5760 OG1 THR D 146 7248 8038 4899 -2228 932 -1988 O ATOM 5761 CG2 THR D 146 8.864 132.139 7.808 1.00 52.82 C ANISOU 5761 CG2 THR D 146 6958 7791 5321 -1818 1123 -2197 C ATOM 5762 N VAL D 147 8.436 134.874 9.823 1.00 47.53 N ANISOU 5762 N VAL D 147 6194 7238 4629 -1420 680 -1355 N ATOM 5763 CA VAL D 147 9.225 136.068 10.127 1.00 47.15 C ANISOU 5763 CA VAL D 147 6070 7252 4595 -1327 681 -1257 C ATOM 5764 C VAL D 147 10.702 135.732 9.986 1.00 49.00 C ANISOU 5764 C VAL D 147 6186 7419 5014 -1269 892 -1564 C ATOM 5765 O VAL D 147 11.174 134.731 10.530 1.00 49.93 O ANISOU 5765 O VAL D 147 6217 7314 5442 -1092 928 -1724 O ATOM 5766 CB VAL D 147 8.932 136.612 11.540 1.00 45.06 C ANISOU 5766 CB VAL D 147 5748 6884 4488 -1074 505 -996 C ATOM 5767 CG1 VAL D 147 9.779 137.846 11.841 1.00 44.39 C ANISOU 5767 CG1 VAL D 147 5597 6851 4420 -1002 516 -921 C ATOM 5768 CG2 VAL D 147 7.454 136.940 11.670 1.00 44.19 C ANISOU 5768 CG2 VAL D 147 5697 6847 4245 -1124 329 -749 C ATOM 5769 N ALA D 148 11.410 136.569 9.230 1.00 50.06 N ANISOU 5769 N ALA D 148 6306 7742 4971 -1437 1015 -1637 N ATOM 5770 CA ALA D 148 12.850 136.458 9.042 1.00 51.55 C ANISOU 5770 CA ALA D 148 6341 7926 5318 -1412 1236 -1939 C ATOM 5771 C ALA D 148 13.464 137.821 9.327 1.00 50.08 C ANISOU 5771 C ALA D 148 6115 7853 5061 -1398 1195 -1762 C ATOM 5772 O ALA D 148 12.891 138.855 8.965 1.00 50.00 O ANISOU 5772 O ALA D 148 6233 7994 4771 -1566 1082 -1512 O ATOM 5773 CB ALA D 148 13.163 136.017 7.623 1.00 54.94 C ANISOU 5773 CB ALA D 148 6799 8533 5544 -1744 1501 -2296 C ATOM 5774 N TRP D 149 14.620 137.819 9.982 1.00 49.37 N ANISOU 5774 N TRP D 149 5839 7669 5249 -1203 1262 -1879 N ATOM 5775 CA TRP D 149 15.333 139.047 10.320 1.00 47.86 C ANISOU 5775 CA TRP D 149 5596 7572 5015 -1197 1237 -1746 C ATOM 5776 C TRP D 149 16.596 139.159 9.478 1.00 50.87 C ANISOU 5776 C TRP D 149 5843 8122 5362 -1380 1508 -2066 C ATOM 5777 O TRP D 149 17.228 138.147 9.172 1.00 53.40 O ANISOU 5777 O TRP D 149 6005 8388 5898 -1345 1704 -2427 O ATOM 5778 CB TRP D 149 15.695 139.051 11.806 1.00 45.77 C ANISOU 5778 CB TRP D 149 5211 7114 5065 -875 1084 -1608 C ATOM 5779 CG TRP D 149 14.544 139.322 12.703 1.00 42.58 C ANISOU 5779 CG TRP D 149 4933 6620 4626 -762 848 -1290 C ATOM 5780 CD1 TRP D 149 13.683 138.407 13.239 1.00 42.07 C ANISOU 5780 CD1 TRP D 149 4913 6408 4664 -648 733 -1223 C ATOM 5781 CD2 TRP D 149 14.128 140.600 13.193 1.00 40.59 C ANISOU 5781 CD2 TRP D 149 4760 6416 4244 -767 717 -1026 C ATOM 5782 NE1 TRP D 149 12.749 139.040 14.029 1.00 39.79 N ANISOU 5782 NE1 TRP D 149 4710 6113 4296 -597 560 -952 N ATOM 5783 CE2 TRP D 149 13.000 140.386 14.019 1.00 39.03 C ANISOU 5783 CE2 TRP D 149 4628 6120 4082 -651 553 -844 C ATOM 5784 CE3 TRP D 149 14.593 141.909 13.009 1.00 40.06 C ANISOU 5784 CE3 TRP D 149 4714 6456 4051 -873 728 -941 C ATOM 5785 CZ2 TRP D 149 12.336 141.436 14.670 1.00 37.70 C ANISOU 5785 CZ2 TRP D 149 4513 5954 3859 -618 429 -628 C ATOM 5786 CZ3 TRP D 149 13.932 142.953 13.653 1.00 38.83 C ANISOU 5786 CZ3 TRP D 149 4636 6260 3859 -828 576 -699 C ATOM 5787 CH2 TRP D 149 12.817 142.709 14.476 1.00 37.34 C ANISOU 5787 CH2 TRP D 149 4480 5970 3738 -691 442 -568 C ATOM 5788 N LYS D 150 16.949 140.388 9.101 1.00 50.80 N ANISOU 5788 N LYS D 150 5890 8309 5102 -1589 1522 -1949 N ATOM 5789 CA LYS D 150 18.164 140.658 8.336 1.00 53.83 C ANISOU 5789 CA LYS D 150 6146 8905 5401 -1821 1785 -2234 C ATOM 5790 C LYS D 150 18.941 141.830 8.932 1.00 52.54 C ANISOU 5790 C LYS D 150 5919 8784 5258 -1789 1720 -2068 C ATOM 5791 O LYS D 150 18.348 142.776 9.449 1.00 49.54 O ANISOU 5791 O LYS D 150 5692 8346 4784 -1750 1490 -1708 O ATOM 5792 CB LYS D 150 17.826 140.936 6.869 1.00 56.02 C ANISOU 5792 CB LYS D 150 6605 9465 5217 -2298 1911 -2297 C ATOM 5793 CG LYS D 150 17.405 139.693 6.100 1.00 58.38 C ANISOU 5793 CG LYS D 150 6921 9782 5479 -2414 2077 -2605 C ATOM 5794 CD LYS D 150 17.060 140.017 4.657 1.00 61.18 C ANISOU 5794 CD LYS D 150 7475 10462 5307 -2961 2180 -2642 C ATOM 5795 CE LYS D 150 16.815 138.759 3.836 1.00 64.19 C ANISOU 5795 CE LYS D 150 7859 10895 5634 -3136 2411 -3043 C ATOM 5796 NZ LYS D 150 16.898 139.029 2.369 1.00 68.12 N ANISOU 5796 NZ LYS D 150 8497 11790 5594 -3759 2611 -3207 N ATOM 5797 N ALA D 151 20.268 141.737 8.860 1.00 54.88 N ANISOU 5797 N ALA D 151 5970 9172 5709 -1807 1934 -2361 N ATOM 5798 CA ALA D 151 21.176 142.813 9.253 1.00 54.62 C ANISOU 5798 CA ALA D 151 5856 9232 5666 -1852 1921 -2266 C ATOM 5799 C ALA D 151 22.037 143.163 8.050 1.00 57.86 C ANISOU 5799 C ALA D 151 6208 9966 5812 -2271 2215 -2539 C ATOM 5800 O ALA D 151 22.866 142.351 7.634 1.00 61.22 O ANISOU 5800 O ALA D 151 6375 10476 6411 -2291 2496 -2973 O ATOM 5801 CB ALA D 151 22.045 142.364 10.416 1.00 54.40 C ANISOU 5801 CB ALA D 151 5538 9037 6097 -1495 1881 -2351 C ATOM 5802 N ASP D 152 21.823 144.352 7.479 1.00 57.75 N ANISOU 5802 N ASP D 152 6426 10125 5392 -2623 2150 -2294 N ATOM 5803 CA ASP D 152 22.496 144.779 6.240 1.00 61.08 C ANISOU 5803 CA ASP D 152 6862 10900 5446 -3138 2404 -2493 C ATOM 5804 C ASP D 152 22.248 143.775 5.087 1.00 63.33 C ANISOU 5804 C ASP D 152 7154 11357 5553 -3393 2660 -2848 C ATOM 5805 O ASP D 152 23.166 143.441 4.329 1.00 66.24 O ANISOU 5805 O ASP D 152 7335 11984 5848 -3665 3017 -3287 O ATOM 5806 CB ASP D 152 24.037 145.014 6.463 1.00 63.70 C ANISOU 5806 CB ASP D 152 6878 11379 5948 -3164 2627 -2768 C ATOM 5807 CG ASP D 152 24.626 146.043 5.499 1.00 67.76 C ANISOU 5807 CG ASP D 152 7492 12243 6011 -3733 2769 -2766 C ATOM 5808 OD1 ASP D 152 23.996 146.311 4.449 1.00 69.68 O ANISOU 5808 OD1 ASP D 152 8010 12661 5805 -4159 2764 -2657 O ATOM 5809 OD2 ASP D 152 25.741 146.563 5.776 1.00 69.86 O ANISOU 5809 OD2 ASP D 152 7560 12626 6358 -3790 2875 -2866 O ATOM 5810 N GLY D 153 21.005 143.306 4.960 1.00 60.94 N ANISOU 5810 N GLY D 153 7054 10923 5176 -3329 2493 -2683 N ATOM 5811 CA GLY D 153 20.627 142.345 3.911 1.00 63.30 C ANISOU 5811 CA GLY D 153 7400 11367 5285 -3588 2705 -2997 C ATOM 5812 C GLY D 153 21.042 140.894 4.135 1.00 64.04 C ANISOU 5812 C GLY D 153 7208 11309 5816 -3288 2950 -3491 C ATOM 5813 O GLY D 153 20.856 140.064 3.248 1.00 65.81 O ANISOU 5813 O GLY D 153 7445 11648 5911 -3520 3182 -3839 O ATOM 5814 N SER D 154 21.567 140.582 5.323 1.00 62.27 N ANISOU 5814 N SER D 154 6736 10808 6117 -2792 2875 -3507 N ATOM 5815 CA SER D 154 22.116 139.266 5.646 1.00 63.91 C ANISOU 5815 CA SER D 154 6628 10807 6848 -2469 3052 -3935 C ATOM 5816 C SER D 154 21.278 138.626 6.754 1.00 60.49 C ANISOU 5816 C SER D 154 6251 9979 6755 -2008 2733 -3659 C ATOM 5817 O SER D 154 21.088 139.258 7.793 1.00 57.48 O ANISOU 5817 O SER D 154 5923 9465 6452 -1777 2440 -3256 O ATOM 5818 CB SER D 154 23.563 139.423 6.121 1.00 65.62 C ANISOU 5818 CB SER D 154 6465 11043 7424 -2312 3194 -4161 C ATOM 5819 OG SER D 154 24.188 138.164 6.273 1.00 68.80 O ANISOU 5819 OG SER D 154 6517 11242 8382 -2031 3376 -4614 O ATOM 5820 N PRO D 155 20.775 137.382 6.547 1.00 61.51 N ANISOU 5820 N PRO D 155 6375 9927 7069 -1909 2796 -3888 N ATOM 5821 CA PRO D 155 19.941 136.714 7.561 1.00 59.07 C ANISOU 5821 CA PRO D 155 6137 9258 7048 -1532 2494 -3622 C ATOM 5822 C PRO D 155 20.551 136.674 8.967 1.00 57.66 C ANISOU 5822 C PRO D 155 5746 8820 7344 -1105 2277 -3446 C ATOM 5823 O PRO D 155 21.738 136.399 9.113 1.00 59.30 O ANISOU 5823 O PRO D 155 5626 8984 7921 -975 2416 -3726 O ATOM 5824 CB PRO D 155 19.798 135.290 7.017 1.00 61.90 C ANISOU 5824 CB PRO D 155 6425 9458 7638 -1517 2688 -4046 C ATOM 5825 CG PRO D 155 19.912 135.440 5.545 1.00 65.09 C ANISOU 5825 CG PRO D 155 6898 10219 7615 -2009 3034 -4398 C ATOM 5826 CD PRO D 155 20.855 136.583 5.308 1.00 65.63 C ANISOU 5826 CD PRO D 155 6867 10592 7478 -2213 3155 -4398 C ATOM 5827 N VAL D 156 19.729 136.959 9.976 1.00 54.65 N ANISOU 5827 N VAL D 156 5536 8290 6939 -923 1941 -2993 N ATOM 5828 CA VAL D 156 20.133 136.886 11.384 1.00 53.97 C ANISOU 5828 CA VAL D 156 5303 7976 7226 -581 1691 -2773 C ATOM 5829 C VAL D 156 19.242 135.876 12.099 1.00 53.21 C ANISOU 5829 C VAL D 156 5302 7578 7336 -370 1464 -2611 C ATOM 5830 O VAL D 156 18.033 136.097 12.228 1.00 51.21 O ANISOU 5830 O VAL D 156 5313 7345 6800 -439 1321 -2343 O ATOM 5831 CB VAL D 156 20.007 138.253 12.094 1.00 51.12 C ANISOU 5831 CB VAL D 156 5067 7741 6617 -610 1503 -2382 C ATOM 5832 CG1 VAL D 156 20.462 138.146 13.550 1.00 50.59 C ANISOU 5832 CG1 VAL D 156 4855 7481 6887 -324 1254 -2177 C ATOM 5833 CG2 VAL D 156 20.812 139.316 11.361 1.00 52.47 C ANISOU 5833 CG2 VAL D 156 5188 8204 6544 -868 1701 -2497 C ATOM 5834 N LYS D 157 19.841 134.781 12.566 1.00 55.55 N ANISOU 5834 N LYS D 157 5370 7588 8148 -124 1417 -2765 N ATOM 5835 CA LYS D 157 19.121 133.743 13.310 1.00 55.21 C ANISOU 5835 CA LYS D 157 5409 7224 8345 57 1172 -2593 C ATOM 5836 C LYS D 157 19.151 133.960 14.814 1.00 53.09 C ANISOU 5836 C LYS D 157 5134 6833 8205 235 820 -2179 C ATOM 5837 O LYS D 157 18.143 133.751 15.487 1.00 51.43 O ANISOU 5837 O LYS D 157 5131 6535 7875 240 603 -1886 O ATOM 5838 CB LYS D 157 19.763 132.376 13.055 1.00 59.77 C ANISOU 5838 CB LYS D 157 5742 7486 9481 227 1259 -2956 C ATOM 5839 CG LYS D 157 18.762 131.240 12.986 1.00 60.54 C ANISOU 5839 CG LYS D 157 6017 7323 9661 240 1176 -2956 C ATOM 5840 CD LYS D 157 19.424 129.912 12.650 1.00 65.47 C ANISOU 5840 CD LYS D 157 6394 7589 10894 407 1283 -3365 C ATOM 5841 CE LYS D 157 18.374 128.860 12.330 1.00 66.31 C ANISOU 5841 CE LYS D 157 6720 7473 11002 340 1265 -3428 C ATOM 5842 NZ LYS D 157 18.902 127.473 12.430 1.00 71.07 N ANISOU 5842 NZ LYS D 157 7107 7582 12314 572 1228 -3694 N ATOM 5843 N ALA D 158 20.326 134.315 15.332 1.00 53.80 N ANISOU 5843 N ALA D 158 4971 6932 8539 349 771 -2176 N ATOM 5844 CA ALA D 158 20.556 134.413 16.772 1.00 52.70 C ANISOU 5844 CA ALA D 158 4788 6681 8555 483 427 -1812 C ATOM 5845 C ALA D 158 19.802 135.580 17.409 1.00 48.79 C ANISOU 5845 C ALA D 158 4548 6408 7582 340 319 -1475 C ATOM 5846 O ALA D 158 19.669 136.651 16.808 1.00 47.14 O ANISOU 5846 O ALA D 158 4437 6456 7020 181 500 -1524 O ATOM 5847 CB ALA D 158 22.041 134.536 17.060 1.00 55.29 C ANISOU 5847 CB ALA D 158 4754 6994 9259 611 407 -1914 C ATOM 5848 N GLY D 159 19.322 135.355 18.631 1.00 47.31 N ANISOU 5848 N GLY D 159 4462 6109 7404 377 20 -1143 N ATOM 5849 CA GLY D 159 18.621 136.377 19.408 1.00 44.10 C ANISOU 5849 CA GLY D 159 4262 5888 6606 246 -76 -867 C ATOM 5850 C GLY D 159 17.218 136.708 18.935 1.00 41.60 C ANISOU 5850 C GLY D 159 4209 5678 5919 120 26 -838 C ATOM 5851 O GLY D 159 16.724 137.799 19.214 1.00 39.75 O ANISOU 5851 O GLY D 159 4100 5618 5386 19 41 -717 O ATOM 5852 N VAL D 160 16.576 135.775 18.228 1.00 41.99 N ANISOU 5852 N VAL D 160 4326 5609 6018 126 88 -956 N ATOM 5853 CA VAL D 160 15.240 135.991 17.672 1.00 40.13 C ANISOU 5853 CA VAL D 160 4308 5481 5460 -3 167 -931 C ATOM 5854 C VAL D 160 14.213 135.212 18.498 1.00 39.71 C ANISOU 5854 C VAL D 160 4384 5303 5400 -14 -29 -728 C ATOM 5855 O VAL D 160 14.424 134.046 18.830 1.00 42.07 O ANISOU 5855 O VAL D 160 4639 5367 5980 61 -159 -716 O ATOM 5856 CB VAL D 160 15.151 135.562 16.182 1.00 41.40 C ANISOU 5856 CB VAL D 160 4477 5659 5595 -72 395 -1220 C ATOM 5857 CG1 VAL D 160 13.732 135.744 15.643 1.00 39.86 C ANISOU 5857 CG1 VAL D 160 4494 5578 5073 -223 419 -1146 C ATOM 5858 CG2 VAL D 160 16.141 136.357 15.336 1.00 42.18 C ANISOU 5858 CG2 VAL D 160 4458 5929 5638 -135 608 -1425 C ATOM 5859 N GLU D 161 13.103 135.868 18.811 1.00 37.80 N ANISOU 5859 N GLU D 161 4290 5212 4860 -119 -51 -576 N ATOM 5860 CA GLU D 161 11.974 135.245 19.492 1.00 37.28 C ANISOU 5860 CA GLU D 161 4348 5100 4716 -189 -189 -412 C ATOM 5861 C GLU D 161 10.687 135.750 18.857 1.00 35.79 C ANISOU 5861 C GLU D 161 4270 5073 4255 -293 -89 -421 C ATOM 5862 O GLU D 161 10.514 136.963 18.707 1.00 34.74 O ANISOU 5862 O GLU D 161 4136 5102 3962 -316 -15 -407 O ATOM 5863 CB GLU D 161 11.980 135.614 20.974 1.00 37.18 C ANISOU 5863 CB GLU D 161 4345 5140 4641 -237 -354 -192 C ATOM 5864 CG GLU D 161 13.064 134.980 21.854 1.00 38.92 C ANISOU 5864 CG GLU D 161 4470 5198 5119 -183 -559 -79 C ATOM 5865 CD GLU D 161 12.932 133.466 21.997 1.00 41.34 C ANISOU 5865 CD GLU D 161 4806 5238 5665 -170 -735 -7 C ATOM 5866 OE1 GLU D 161 13.861 132.761 22.467 1.00 44.02 O ANISOU 5866 OE1 GLU D 161 5037 5362 6325 -89 -933 78 O ATOM 5867 OE2 GLU D 161 11.862 132.964 21.637 1.00 41.62 O ANISOU 5867 OE2 GLU D 161 4966 5258 5587 -248 -696 -24 O ATOM 5868 N THR D 162 9.798 134.827 18.486 1.00 35.81 N ANISOU 5868 N THR D 162 4358 5013 4235 -360 -107 -435 N ATOM 5869 CA THR D 162 8.590 135.144 17.714 1.00 35.05 C ANISOU 5869 CA THR D 162 4337 5064 3916 -467 -37 -446 C ATOM 5870 C THR D 162 7.373 134.456 18.336 1.00 34.93 C ANISOU 5870 C THR D 162 4399 5045 3828 -568 -144 -322 C ATOM 5871 O THR D 162 7.449 133.291 18.722 1.00 36.27 O ANISOU 5871 O THR D 162 4613 5040 4129 -588 -241 -295 O ATOM 5872 CB THR D 162 8.757 134.703 16.244 1.00 36.19 C ANISOU 5872 CB THR D 162 4504 5190 4056 -519 94 -650 C ATOM 5873 OG1 THR D 162 9.883 135.383 15.672 1.00 36.94 O ANISOU 5873 OG1 THR D 162 4519 5333 4183 -476 217 -779 O ATOM 5874 CG2 THR D 162 7.507 135.006 15.414 1.00 35.72 C ANISOU 5874 CG2 THR D 162 4521 5298 3752 -668 116 -618 C ATOM 5875 N THR D 163 6.257 135.175 18.422 1.00 34.05 N ANISOU 5875 N THR D 163 4287 5115 3534 -639 -133 -248 N ATOM 5876 CA THR D 163 5.024 134.626 19.003 1.00 34.51 C ANISOU 5876 CA THR D 163 4384 5227 3501 -766 -204 -155 C ATOM 5877 C THR D 163 4.141 134.011 17.920 1.00 35.27 C ANISOU 5877 C THR D 163 4533 5347 3522 -870 -187 -208 C ATOM 5878 O THR D 163 4.090 134.515 16.787 1.00 35.12 O ANISOU 5878 O THR D 163 4501 5402 3440 -872 -121 -277 O ATOM 5879 CB THR D 163 4.204 135.700 19.741 1.00 33.37 C ANISOU 5879 CB THR D 163 4158 5276 3245 -793 -183 -94 C ATOM 5880 OG1 THR D 163 3.933 136.803 18.862 1.00 32.59 O ANISOU 5880 OG1 THR D 163 3991 5270 3123 -731 -118 -132 O ATOM 5881 CG2 THR D 163 4.946 136.190 20.952 1.00 33.61 C ANISOU 5881 CG2 THR D 163 4162 5310 3300 -765 -198 -53 C ATOM 5882 N LYS D 164 3.456 132.922 18.278 1.00 36.37 N ANISOU 5882 N LYS D 164 4743 5431 3646 -997 -262 -161 N ATOM 5883 CA LYS D 164 2.468 132.282 17.405 1.00 37.65 C ANISOU 5883 CA LYS D 164 4958 5637 3710 -1142 -260 -200 C ATOM 5884 C LYS D 164 1.331 133.288 17.210 1.00 37.29 C ANISOU 5884 C LYS D 164 4800 5847 3520 -1184 -247 -142 C ATOM 5885 O LYS D 164 0.945 133.953 18.170 1.00 36.28 O ANISOU 5885 O LYS D 164 4577 5828 3381 -1160 -249 -75 O ATOM 5886 CB LYS D 164 1.939 130.982 18.036 1.00 39.86 C ANISOU 5886 CB LYS D 164 5336 5804 4003 -1294 -360 -133 C ATOM 5887 CG LYS D 164 1.130 130.071 17.115 1.00 41.62 C ANISOU 5887 CG LYS D 164 5646 6013 4156 -1465 -362 -202 C ATOM 5888 CD LYS D 164 0.439 128.948 17.892 1.00 43.73 C ANISOU 5888 CD LYS D 164 6010 6199 4408 -1654 -476 -96 C ATOM 5889 CE LYS D 164 -0.637 128.203 17.106 1.00 45.61 C ANISOU 5889 CE LYS D 164 6315 6492 4523 -1872 -480 -143 C ATOM 5890 NZ LYS D 164 -0.180 126.969 16.402 1.00 47.90 N ANISOU 5890 NZ LYS D 164 6762 6485 4954 -1927 -483 -287 N ATOM 5891 N PRO D 165 0.798 133.419 15.977 1.00 38.04 N ANISOU 5891 N PRO D 165 4894 6037 3522 -1261 -239 -175 N ATOM 5892 CA PRO D 165 -0.285 134.395 15.786 1.00 38.48 C ANISOU 5892 CA PRO D 165 4805 6300 3516 -1279 -279 -86 C ATOM 5893 C PRO D 165 -1.497 134.138 16.685 1.00 39.49 C ANISOU 5893 C PRO D 165 4836 6547 3622 -1371 -314 -28 C ATOM 5894 O PRO D 165 -1.884 132.988 16.853 1.00 39.86 O ANISOU 5894 O PRO D 165 4972 6562 3609 -1527 -340 -32 O ATOM 5895 CB PRO D 165 -0.664 134.216 14.318 1.00 39.08 C ANISOU 5895 CB PRO D 165 4931 6451 3468 -1425 -316 -97 C ATOM 5896 CG PRO D 165 0.577 133.705 13.672 1.00 39.36 C ANISOU 5896 CG PRO D 165 5112 6341 3502 -1427 -225 -244 C ATOM 5897 CD PRO D 165 1.208 132.809 14.698 1.00 39.06 C ANISOU 5897 CD PRO D 165 5133 6101 3608 -1348 -195 -302 C ATOM 5898 N SER D 166 -2.037 135.201 17.282 1.00 40.19 N ANISOU 5898 N SER D 166 4737 6758 3777 -1287 -300 0 N ATOM 5899 CA SER D 166 -3.232 135.126 18.138 1.00 42.12 C ANISOU 5899 CA SER D 166 4828 7164 4010 -1387 -287 0 C ATOM 5900 C SER D 166 -4.274 136.119 17.641 1.00 43.70 C ANISOU 5900 C SER D 166 4781 7507 4317 -1331 -331 25 C ATOM 5901 O SER D 166 -3.920 137.174 17.121 1.00 43.54 O ANISOU 5901 O SER D 166 4700 7432 4411 -1173 -365 56 O ATOM 5902 CB SER D 166 -2.880 135.444 19.594 1.00 41.92 C ANISOU 5902 CB SER D 166 4770 7151 4008 -1359 -193 -50 C ATOM 5903 OG SER D 166 -2.310 136.735 19.714 1.00 42.04 O ANISOU 5903 OG SER D 166 4696 7130 4149 -1162 -142 -90 O ATOM 5904 N LYS D 167 -5.552 135.781 17.821 1.00 45.83 N ANISOU 5904 N LYS D 167 4894 7948 4572 -1468 -349 21 N ATOM 5905 CA LYS D 167 -6.665 136.623 17.370 1.00 48.08 C ANISOU 5905 CA LYS D 167 4884 8362 5023 -1413 -426 52 C ATOM 5906 C LYS D 167 -6.687 137.973 18.087 1.00 48.85 C ANISOU 5906 C LYS D 167 4749 8441 5372 -1200 -343 -40 C ATOM 5907 O LYS D 167 -6.531 138.029 19.305 1.00 48.44 O ANISOU 5907 O LYS D 167 4669 8424 5311 -1211 -177 -182 O ATOM 5908 CB LYS D 167 -8.009 135.927 17.620 1.00 50.53 C ANISOU 5908 CB LYS D 167 5032 8883 5284 -1616 -431 28 C ATOM 5909 CG LYS D 167 -8.301 134.720 16.739 1.00 51.09 C ANISOU 5909 CG LYS D 167 5280 8987 5146 -1849 -541 117 C ATOM 5910 CD LYS D 167 -9.323 135.021 15.647 1.00 53.69 C ANISOU 5910 CD LYS D 167 5410 9452 5539 -1901 -723 230 C ATOM 5911 CE LYS D 167 -10.153 133.792 15.313 1.00 55.39 C ANISOU 5911 CE LYS D 167 5680 9810 5557 -2206 -779 253 C ATOM 5912 NZ LYS D 167 -11.305 134.132 14.437 1.00 58.32 N ANISOU 5912 NZ LYS D 167 5789 10363 6007 -2279 -973 372 N ATOM 5913 N GLN D 168 -6.893 139.040 17.317 1.00 50.35 N ANISOU 5913 N GLN D 168 4780 8569 5782 -1038 -470 44 N ATOM 5914 CA GLN D 168 -7.165 140.376 17.850 1.00 52.43 C ANISOU 5914 CA GLN D 168 4765 8776 6379 -826 -422 -53 C ATOM 5915 C GLN D 168 -8.648 140.467 18.214 1.00 56.14 C ANISOU 5915 C GLN D 168 4855 9419 7057 -850 -403 -153 C ATOM 5916 O GLN D 168 -9.426 139.560 17.895 1.00 56.83 O ANISOU 5916 O GLN D 168 4912 9674 7006 -1037 -468 -97 O ATOM 5917 CB GLN D 168 -6.851 141.449 16.802 1.00 52.91 C ANISOU 5917 CB GLN D 168 4808 8662 6636 -663 -622 123 C ATOM 5918 CG GLN D 168 -5.418 141.453 16.277 1.00 50.55 C ANISOU 5918 CG GLN D 168 4846 8224 6138 -665 -638 214 C ATOM 5919 CD GLN D 168 -5.157 142.461 15.167 1.00 51.38 C ANISOU 5919 CD GLN D 168 4958 8191 6373 -590 -856 422 C ATOM 5920 OE1 GLN D 168 -4.014 142.876 14.945 1.00 50.12 O ANISOU 5920 OE1 GLN D 168 4994 7909 6141 -556 -835 453 O ATOM 5921 NE2 GLN D 168 -6.202 142.888 14.488 1.00 53.67 N ANISOU 5921 NE2 GLN D 168 5024 8503 6863 -584 -1083 582 N ATOM 5922 N SER D 169 -9.043 141.571 18.855 1.00 58.72 N ANISOU 5922 N SER D 169 4872 9699 7738 -666 -308 -326 N ATOM 5923 CA SER D 169 -10.459 141.800 19.205 1.00 62.58 C ANISOU 5923 CA SER D 169 4917 10342 8517 -654 -266 -478 C ATOM 5924 C SER D 169 -11.368 141.955 17.970 1.00 64.68 C ANISOU 5924 C SER D 169 4965 10609 9002 -609 -583 -238 C ATOM 5925 O SER D 169 -12.560 141.661 18.053 1.00 67.28 O ANISOU 5925 O SER D 169 4977 11132 9455 -687 -592 -303 O ATOM 5926 CB SER D 169 -10.622 142.993 20.165 1.00 64.84 C ANISOU 5926 CB SER D 169 4899 10545 9193 -455 -62 -780 C ATOM 5927 OG SER D 169 -10.179 144.203 19.585 1.00 66.06 O ANISOU 5927 OG SER D 169 5016 10396 9688 -185 -225 -671 O ATOM 5928 N ASN D 170 -10.805 142.374 16.829 1.00 63.97 N ANISOU 5928 N ASN D 170 5047 10333 8926 -531 -851 48 N ATOM 5929 CA ASN D 170 -11.558 142.460 15.558 1.00 66.04 C ANISOU 5929 CA ASN D 170 5168 10613 9310 -566 -1209 344 C ATOM 5930 C ASN D 170 -11.591 141.169 14.703 1.00 64.47 C ANISOU 5930 C ASN D 170 5245 10601 8649 -879 -1327 525 C ATOM 5931 O ASN D 170 -12.055 141.197 13.558 1.00 66.54 O ANISOU 5931 O ASN D 170 5465 10900 8917 -974 -1638 795 O ATOM 5932 CB ASN D 170 -11.063 143.654 14.715 1.00 67.04 C ANISOU 5932 CB ASN D 170 5320 10464 9689 -387 -1478 588 C ATOM 5933 CG ASN D 170 -9.679 143.440 14.114 1.00 64.14 C ANISOU 5933 CG ASN D 170 5438 10010 8922 -497 -1495 733 C ATOM 5934 OD1 ASN D 170 -8.979 142.483 14.439 1.00 61.37 O ANISOU 5934 OD1 ASN D 170 5387 9754 8176 -642 -1284 615 O ATOM 5935 ND2 ASN D 170 -9.279 144.345 13.227 1.00 65.19 N ANISOU 5935 ND2 ASN D 170 5634 9954 9180 -440 -1757 992 N ATOM 5936 N ASN D 171 -11.103 140.057 15.260 1.00 61.11 N ANISOU 5936 N ASN D 171 5101 10277 7839 -1056 -1096 382 N ATOM 5937 CA ASN D 171 -11.118 138.718 14.629 1.00 59.77 C ANISOU 5937 CA ASN D 171 5202 10248 7261 -1357 -1148 474 C ATOM 5938 C ASN D 171 -10.073 138.422 13.538 1.00 57.32 C ANISOU 5938 C ASN D 171 5286 9834 6658 -1464 -1257 636 C ATOM 5939 O ASN D 171 -10.022 137.300 13.030 1.00 56.88 O ANISOU 5939 O ASN D 171 5461 9866 6286 -1716 -1265 655 O ATOM 5940 CB ASN D 171 -12.545 138.296 14.181 1.00 62.79 C ANISOU 5940 CB ASN D 171 5305 10858 7693 -1527 -1316 558 C ATOM 5941 CG ASN D 171 -13.156 137.236 15.085 1.00 63.07 C ANISOU 5941 CG ASN D 171 5299 11096 7568 -1725 -1107 365 C ATOM 5942 OD1 ASN D 171 -12.867 137.178 16.283 1.00 62.50 O ANISOU 5942 OD1 ASN D 171 5239 11019 7490 -1682 -846 150 O ATOM 5943 ND2 ASN D 171 -14.013 136.393 14.515 1.00 64.80 N ANISOU 5943 ND2 ASN D 171 5479 11511 7630 -1987 -1235 454 N ATOM 5944 N LYS D 172 -9.231 139.399 13.203 1.00 56.19 N ANISOU 5944 N LYS D 172 5220 9508 6620 -1298 -1317 719 N ATOM 5945 CA LYS D 172 -8.002 139.137 12.445 1.00 53.82 C ANISOU 5945 CA LYS D 172 5298 9121 6030 -1399 -1313 778 C ATOM 5946 C LYS D 172 -6.883 138.772 13.424 1.00 49.87 C ANISOU 5946 C LYS D 172 5002 8508 5439 -1308 -1033 565 C ATOM 5947 O LYS D 172 -7.074 138.845 14.641 1.00 49.07 O ANISOU 5947 O LYS D 172 4767 8404 5472 -1193 -872 410 O ATOM 5948 CB LYS D 172 -7.616 140.352 11.600 1.00 55.43 C ANISOU 5948 CB LYS D 172 5495 9205 6360 -1320 -1524 991 C ATOM 5949 CG LYS D 172 -8.641 140.684 10.528 1.00 59.06 C ANISOU 5949 CG LYS D 172 5781 9768 6892 -1455 -1876 1273 C ATOM 5950 CD LYS D 172 -8.310 141.984 9.818 1.00 61.00 C ANISOU 5950 CD LYS D 172 6007 9859 7311 -1383 -2130 1530 C ATOM 5951 CE LYS D 172 -9.498 142.483 9.017 1.00 65.20 C ANISOU 5951 CE LYS D 172 6268 10452 8054 -1457 -2537 1845 C ATOM 5952 NZ LYS D 172 -9.164 143.745 8.308 1.00 67.56 N ANISOU 5952 NZ LYS D 172 6573 10566 8530 -1421 -2839 2151 N ATOM 5953 N TYR D 173 -5.731 138.365 12.889 1.00 47.40 N ANISOU 5953 N TYR D 173 4995 8118 4897 -1387 -979 551 N ATOM 5954 CA TYR D 173 -4.599 137.920 13.706 1.00 44.23 C ANISOU 5954 CA TYR D 173 4778 7597 4428 -1313 -761 381 C ATOM 5955 C TYR D 173 -3.502 138.965 13.835 1.00 42.85 C ANISOU 5955 C TYR D 173 4647 7277 4357 -1131 -715 379 C ATOM 5956 O TYR D 173 -3.355 139.857 12.994 1.00 44.15 O ANISOU 5956 O TYR D 173 4800 7412 4561 -1120 -850 518 O ATOM 5957 CB TYR D 173 -3.995 136.627 13.149 1.00 43.68 C ANISOU 5957 CB TYR D 173 4982 7511 4103 -1505 -699 306 C ATOM 5958 CG TYR D 173 -4.870 135.421 13.363 1.00 44.62 C ANISOU 5958 CG TYR D 173 5110 7720 4125 -1685 -695 263 C ATOM 5959 CD1 TYR D 173 -5.950 135.166 12.523 1.00 46.48 C ANISOU 5959 CD1 TYR D 173 5273 8119 4269 -1884 -844 361 C ATOM 5960 CD2 TYR D 173 -4.627 134.533 14.413 1.00 44.01 C ANISOU 5960 CD2 TYR D 173 5116 7566 4037 -1691 -570 152 C ATOM 5961 CE1 TYR D 173 -6.761 134.060 12.713 1.00 47.76 C ANISOU 5961 CE1 TYR D 173 5446 8370 4331 -2078 -840 320 C ATOM 5962 CE2 TYR D 173 -5.435 133.422 14.613 1.00 45.14 C ANISOU 5962 CE2 TYR D 173 5287 7778 4083 -1893 -582 133 C ATOM 5963 CZ TYR D 173 -6.497 133.192 13.757 1.00 46.77 C ANISOU 5963 CZ TYR D 173 5421 8151 4199 -2083 -702 203 C ATOM 5964 OH TYR D 173 -7.298 132.101 13.960 1.00 48.68 O ANISOU 5964 OH TYR D 173 5693 8467 4337 -2308 -711 181 O ATOM 5965 N ALA D 174 -2.744 138.839 14.919 1.00 40.46 N ANISOU 5965 N ALA D 174 4400 6888 4084 -1022 -545 240 N ATOM 5966 CA ALA D 174 -1.526 139.601 15.126 1.00 38.46 C ANISOU 5966 CA ALA D 174 4223 6505 3885 -886 -475 209 C ATOM 5967 C ALA D 174 -0.436 138.674 15.645 1.00 36.43 C ANISOU 5967 C ALA D 174 4147 6176 3518 -903 -341 90 C ATOM 5968 O ALA D 174 -0.722 137.668 16.297 1.00 35.88 O ANISOU 5968 O ALA D 174 4109 6126 3397 -975 -299 35 O ATOM 5969 CB ALA D 174 -1.764 140.728 16.113 1.00 38.71 C ANISOU 5969 CB ALA D 174 4063 6493 4153 -708 -433 166 C ATOM 5970 N ALA D 175 0.807 139.028 15.344 1.00 35.33 N ANISOU 5970 N ALA D 175 4114 5945 3364 -849 -295 64 N ATOM 5971 CA ALA D 175 1.980 138.328 15.857 1.00 34.10 C ANISOU 5971 CA ALA D 175 4076 5692 3189 -820 -192 -42 C ATOM 5972 C ALA D 175 3.083 139.339 16.128 1.00 33.29 C ANISOU 5972 C ALA D 175 3966 5521 3161 -697 -141 -59 C ATOM 5973 O ALA D 175 3.021 140.483 15.666 1.00 33.70 O ANISOU 5973 O ALA D 175 3970 5583 3253 -664 -184 10 O ATOM 5974 CB ALA D 175 2.438 137.268 14.874 1.00 34.91 C ANISOU 5974 CB ALA D 175 4319 5763 3184 -943 -168 -115 C ATOM 5975 N SER D 176 4.080 138.920 16.899 1.00 32.86 N ANISOU 5975 N SER D 176 3955 5387 3143 -644 -76 -131 N ATOM 5976 CA SER D 176 5.192 139.790 17.281 1.00 32.00 C ANISOU 5976 CA SER D 176 3832 5229 3098 -549 -28 -155 C ATOM 5977 C SER D 176 6.506 139.028 17.197 1.00 32.80 C ANISOU 5977 C SER D 176 3992 5244 3228 -534 19 -240 C ATOM 5978 O SER D 176 6.541 137.817 17.444 1.00 33.97 O ANISOU 5978 O SER D 176 4177 5322 3407 -557 -1 -271 O ATOM 5979 CB SER D 176 4.988 140.342 18.696 1.00 31.45 C ANISOU 5979 CB SER D 176 3688 5175 3087 -497 -13 -154 C ATOM 5980 OG SER D 176 5.012 139.309 19.676 1.00 30.79 O ANISOU 5980 OG SER D 176 3636 5086 2978 -551 -27 -158 O ATOM 5981 N SER D 177 7.572 139.743 16.829 1.00 32.63 N ANISOU 5981 N SER D 177 3961 5212 3225 -500 73 -280 N ATOM 5982 CA SER D 177 8.925 139.190 16.824 1.00 32.71 C ANISOU 5982 CA SER D 177 3959 5148 3323 -461 130 -387 C ATOM 5983 C SER D 177 9.912 140.179 17.451 1.00 31.81 C ANISOU 5983 C SER D 177 3788 5038 3260 -398 149 -377 C ATOM 5984 O SER D 177 9.810 141.395 17.248 1.00 31.31 O ANISOU 5984 O SER D 177 3728 5027 3141 -417 162 -331 O ATOM 5985 CB SER D 177 9.359 138.839 15.401 1.00 33.70 C ANISOU 5985 CB SER D 177 4115 5298 3391 -552 225 -520 C ATOM 5986 OG SER D 177 10.484 137.986 15.440 1.00 35.04 O ANISOU 5986 OG SER D 177 4228 5364 3722 -494 292 -677 O ATOM 5987 N TYR D 178 10.856 139.640 18.215 1.00 32.40 N ANISOU 5987 N TYR D 178 3808 5039 3462 -335 126 -406 N ATOM 5988 CA TYR D 178 11.867 140.423 18.909 1.00 32.05 C ANISOU 5988 CA TYR D 178 3700 5011 3467 -301 125 -395 C ATOM 5989 C TYR D 178 13.234 139.969 18.464 1.00 32.95 C ANISOU 5989 C TYR D 178 3715 5079 3725 -258 176 -516 C ATOM 5990 O TYR D 178 13.507 138.774 18.441 1.00 33.61 O ANISOU 5990 O TYR D 178 3753 5048 3969 -205 142 -572 O ATOM 5991 CB TYR D 178 11.745 140.257 20.428 1.00 32.84 C ANISOU 5991 CB TYR D 178 3793 5100 3585 -304 13 -290 C ATOM 5992 CG TYR D 178 10.357 140.504 20.937 1.00 32.95 C ANISOU 5992 CG TYR D 178 3865 5176 3478 -364 0 -231 C ATOM 5993 CD1 TYR D 178 9.911 141.796 21.171 1.00 33.52 C ANISOU 5993 CD1 TYR D 178 3931 5316 3488 -381 59 -244 C ATOM 5994 CD2 TYR D 178 9.480 139.450 21.167 1.00 34.03 C ANISOU 5994 CD2 TYR D 178 4044 5292 3593 -411 -63 -183 C ATOM 5995 CE1 TYR D 178 8.628 142.040 21.641 1.00 33.85 C ANISOU 5995 CE1 TYR D 178 3971 5415 3478 -422 73 -242 C ATOM 5996 CE2 TYR D 178 8.184 139.680 21.631 1.00 34.33 C ANISOU 5996 CE2 TYR D 178 4097 5422 3527 -485 -51 -159 C ATOM 5997 CZ TYR D 178 7.764 140.978 21.869 1.00 34.50 C ANISOU 5997 CZ TYR D 178 4073 5520 3515 -480 27 -204 C ATOM 5998 OH TYR D 178 6.485 141.228 22.321 1.00 36.47 O ANISOU 5998 OH TYR D 178 4281 5856 3719 -538 65 -231 O ATOM 5999 N LEU D 179 14.076 140.927 18.085 1.00 32.95 N ANISOU 5999 N LEU D 179 3670 5155 3695 -288 260 -570 N ATOM 6000 CA LEU D 179 15.494 140.691 17.861 1.00 34.31 C ANISOU 6000 CA LEU D 179 3693 5320 4023 -255 322 -703 C ATOM 6001 C LEU D 179 16.259 141.378 18.989 1.00 34.48 C ANISOU 6001 C LEU D 179 3643 5367 4090 -238 239 -613 C ATOM 6002 O LEU D 179 16.224 142.604 19.103 1.00 32.84 O ANISOU 6002 O LEU D 179 3494 5242 3742 -312 268 -565 O ATOM 6003 CB LEU D 179 15.929 141.249 16.505 1.00 34.88 C ANISOU 6003 CB LEU D 179 3763 5509 3981 -375 499 -847 C ATOM 6004 CG LEU D 179 17.422 141.170 16.152 1.00 36.67 C ANISOU 6004 CG LEU D 179 3800 5782 4351 -379 620 -1038 C ATOM 6005 CD1 LEU D 179 17.972 139.767 16.362 1.00 38.34 C ANISOU 6005 CD1 LEU D 179 3840 5843 4886 -228 602 -1178 C ATOM 6006 CD2 LEU D 179 17.640 141.625 14.712 1.00 38.00 C ANISOU 6006 CD2 LEU D 179 4003 6110 4326 -582 816 -1191 C ATOM 6007 N SER D 180 16.937 140.584 19.815 1.00 36.52 N ANISOU 6007 N SER D 180 3780 5540 4557 -156 113 -580 N ATOM 6008 CA SER D 180 17.732 141.108 20.928 1.00 37.83 C ANISOU 6008 CA SER D 180 3867 5751 4756 -178 -1 -479 C ATOM 6009 C SER D 180 19.188 141.282 20.513 1.00 39.51 C ANISOU 6009 C SER D 180 3872 6005 5137 -152 66 -610 C ATOM 6010 O SER D 180 19.824 140.324 20.094 1.00 40.95 O ANISOU 6010 O SER D 180 3881 6092 5585 -47 74 -730 O ATOM 6011 CB SER D 180 17.654 140.167 22.122 1.00 39.23 C ANISOU 6011 CB SER D 180 4025 5827 5052 -153 -237 -310 C ATOM 6012 OG SER D 180 16.316 140.041 22.552 1.00 38.84 O ANISOU 6012 OG SER D 180 4156 5782 4821 -220 -274 -210 O ATOM 6013 N LEU D 181 19.704 142.505 20.645 1.00 39.83 N ANISOU 6013 N LEU D 181 3913 6178 5045 -255 121 -607 N ATOM 6014 CA LEU D 181 21.097 142.838 20.310 1.00 42.02 C ANISOU 6014 CA LEU D 181 3982 6541 5442 -277 196 -729 C ATOM 6015 C LEU D 181 21.767 143.543 21.478 1.00 42.52 C ANISOU 6015 C LEU D 181 3996 6681 5480 -355 59 -602 C ATOM 6016 O LEU D 181 21.094 143.982 22.415 1.00 42.30 O ANISOU 6016 O LEU D 181 4129 6659 5283 -428 -41 -456 O ATOM 6017 CB LEU D 181 21.136 143.780 19.110 1.00 41.90 C ANISOU 6017 CB LEU D 181 4040 6647 5232 -411 419 -858 C ATOM 6018 CG LEU D 181 20.353 143.364 17.870 1.00 42.20 C ANISOU 6018 CG LEU D 181 4184 6669 5181 -429 558 -964 C ATOM 6019 CD1 LEU D 181 20.312 144.516 16.881 1.00 42.35 C ANISOU 6019 CD1 LEU D 181 4326 6821 4945 -634 701 -991 C ATOM 6020 CD2 LEU D 181 20.973 142.125 17.245 1.00 44.32 C ANISOU 6020 CD2 LEU D 181 4244 6892 5702 -337 651 -1188 C ATOM 6021 N THR D 182 23.093 143.646 21.428 1.00 44.30 N ANISOU 6021 N THR D 182 3982 6982 5869 -364 67 -680 N ATOM 6022 CA THR D 182 23.814 144.582 22.290 1.00 44.84 C ANISOU 6022 CA THR D 182 4014 7172 5852 -502 -18 -592 C ATOM 6023 C THR D 182 23.760 145.953 21.603 1.00 43.78 C ANISOU 6023 C THR D 182 4025 7144 5465 -667 184 -676 C ATOM 6024 O THR D 182 23.605 146.011 20.380 1.00 42.59 O ANISOU 6024 O THR D 182 3904 7009 5269 -680 369 -809 O ATOM 6025 CB THR D 182 25.287 144.178 22.516 1.00 47.75 C ANISOU 6025 CB THR D 182 4033 7590 6520 -460 -115 -629 C ATOM 6026 OG1 THR D 182 26.006 144.247 21.280 1.00 49.30 O ANISOU 6026 OG1 THR D 182 4051 7863 6819 -453 125 -882 O ATOM 6027 CG2 THR D 182 25.383 142.765 23.096 1.00 49.31 C ANISOU 6027 CG2 THR D 182 4066 7618 7051 -280 -362 -519 C ATOM 6028 N PRO D 183 23.888 147.053 22.376 1.00 43.80 N ANISOU 6028 N PRO D 183 4129 7214 5298 -826 140 -597 N ATOM 6029 CA PRO D 183 23.955 148.394 21.777 1.00 43.73 C ANISOU 6029 CA PRO D 183 4254 7261 5102 -996 293 -654 C ATOM 6030 C PRO D 183 25.027 148.549 20.692 1.00 45.67 C ANISOU 6030 C PRO D 183 4326 7633 5394 -1077 448 -801 C ATOM 6031 O PRO D 183 24.805 149.261 19.714 1.00 44.72 O ANISOU 6031 O PRO D 183 4342 7531 5117 -1205 591 -845 O ATOM 6032 CB PRO D 183 24.275 149.296 22.977 1.00 43.93 C ANISOU 6032 CB PRO D 183 4334 7335 5022 -1152 196 -581 C ATOM 6033 CG PRO D 183 23.693 148.578 24.143 1.00 43.53 C ANISOU 6033 CG PRO D 183 4313 7242 4986 -1087 23 -467 C ATOM 6034 CD PRO D 183 23.910 147.119 23.854 1.00 44.16 C ANISOU 6034 CD PRO D 183 4199 7281 5300 -896 -61 -449 C ATOM 6035 N GLU D 184 26.169 147.888 20.884 1.00 48.31 N ANISOU 6035 N GLU D 184 4349 8055 5951 -1025 407 -871 N ATOM 6036 CA GLU D 184 27.280 147.934 19.938 1.00 50.97 C ANISOU 6036 CA GLU D 184 4449 8548 6369 -1111 582 -1066 C ATOM 6037 C GLU D 184 26.923 147.246 18.618 1.00 51.18 C ANISOU 6037 C GLU D 184 4463 8563 6420 -1058 778 -1244 C ATOM 6038 O GLU D 184 27.217 147.781 17.553 1.00 51.73 O ANISOU 6038 O GLU D 184 4555 8771 6330 -1257 985 -1376 O ATOM 6039 CB GLU D 184 28.534 147.319 20.564 1.00 53.78 C ANISOU 6039 CB GLU D 184 4417 8978 7039 -1031 464 -1105 C ATOM 6040 CG GLU D 184 29.814 147.504 19.763 1.00 57.33 C ANISOU 6040 CG GLU D 184 4559 9630 7593 -1149 657 -1337 C ATOM 6041 CD GLU D 184 31.070 147.293 20.598 1.00 60.33 C ANISOU 6041 CD GLU D 184 4561 10101 8259 -1118 488 -1319 C ATOM 6042 OE1 GLU D 184 31.203 147.942 21.662 1.00 60.61 O ANISOU 6042 OE1 GLU D 184 4685 10171 8174 -1231 292 -1116 O ATOM 6043 OE2 GLU D 184 31.932 146.484 20.193 1.00 63.03 O ANISOU 6043 OE2 GLU D 184 4500 10484 8964 -992 550 -1520 O ATOM 6044 N GLN D 185 26.281 146.077 18.696 1.00 50.48 N ANISOU 6044 N GLN D 185 4358 8320 6502 -835 711 -1244 N ATOM 6045 CA GLN D 185 25.758 145.389 17.502 1.00 50.84 C ANISOU 6045 CA GLN D 185 4439 8339 6537 -806 890 -1416 C ATOM 6046 C GLN D 185 24.780 146.273 16.733 1.00 49.14 C ANISOU 6046 C GLN D 185 4565 8154 5951 -996 978 -1337 C ATOM 6047 O GLN D 185 24.870 146.389 15.510 1.00 50.33 O ANISOU 6047 O GLN D 185 4740 8429 5953 -1174 1178 -1489 O ATOM 6048 CB GLN D 185 25.052 144.082 17.877 1.00 50.50 C ANISOU 6048 CB GLN D 185 4387 8087 6714 -556 759 -1379 C ATOM 6049 CG GLN D 185 25.990 142.943 18.248 1.00 53.40 C ANISOU 6049 CG GLN D 185 4385 8366 7537 -353 680 -1494 C ATOM 6050 CD GLN D 185 25.244 141.730 18.781 1.00 53.24 C ANISOU 6050 CD GLN D 185 4405 8095 7728 -135 487 -1384 C ATOM 6051 OE1 GLN D 185 24.303 141.857 19.567 1.00 51.37 O ANISOU 6051 OE1 GLN D 185 4415 7784 7320 -135 309 -1130 O ATOM 6052 NE2 GLN D 185 25.662 140.545 18.355 1.00 56.00 N ANISOU 6052 NE2 GLN D 185 4504 8307 8466 34 533 -1595 N ATOM 6053 N TRP D 186 23.856 146.884 17.471 1.00 46.77 N ANISOU 6053 N TRP D 186 4513 7741 5518 -976 818 -1104 N ATOM 6054 CA TRP D 186 22.869 147.817 16.917 1.00 45.60 C ANISOU 6054 CA TRP D 186 4663 7561 5102 -1118 833 -982 C ATOM 6055 C TRP D 186 23.534 148.964 16.144 1.00 47.23 C ANISOU 6055 C TRP D 186 4919 7908 5116 -1407 947 -1004 C ATOM 6056 O TRP D 186 23.152 149.248 15.009 1.00 47.35 O ANISOU 6056 O TRP D 186 5076 7977 4938 -1588 1030 -1000 O ATOM 6057 CB TRP D 186 21.957 148.344 18.041 1.00 43.14 C ANISOU 6057 CB TRP D 186 4529 7098 4766 -1033 661 -787 C ATOM 6058 CG TRP D 186 21.147 149.543 17.698 1.00 42.40 C ANISOU 6058 CG TRP D 186 4681 6925 4502 -1157 643 -662 C ATOM 6059 CD1 TRP D 186 21.225 150.777 18.276 1.00 42.58 C ANISOU 6059 CD1 TRP D 186 4808 6887 4481 -1256 593 -584 C ATOM 6060 CD2 TRP D 186 20.135 149.632 16.693 1.00 42.33 C ANISOU 6060 CD2 TRP D 186 4835 6864 4383 -1202 648 -593 C ATOM 6061 NE1 TRP D 186 20.315 151.629 17.700 1.00 42.89 N ANISOU 6061 NE1 TRP D 186 5053 6798 4444 -1327 557 -469 N ATOM 6062 CE2 TRP D 186 19.640 150.956 16.716 1.00 42.69 C ANISOU 6062 CE2 TRP D 186 5064 6790 4368 -1303 573 -450 C ATOM 6063 CE3 TRP D 186 19.596 148.722 15.774 1.00 42.46 C ANISOU 6063 CE3 TRP D 186 4859 6915 4357 -1183 695 -638 C ATOM 6064 CZ2 TRP D 186 18.627 151.392 15.858 1.00 42.78 C ANISOU 6064 CZ2 TRP D 186 5243 6706 4306 -1368 504 -311 C ATOM 6065 CZ3 TRP D 186 18.587 149.158 14.918 1.00 42.75 C ANISOU 6065 CZ3 TRP D 186 5081 6902 4259 -1283 642 -505 C ATOM 6066 CH2 TRP D 186 18.113 150.480 14.971 1.00 42.97 C ANISOU 6066 CH2 TRP D 186 5268 6803 4256 -1366 529 -324 C ATOM 6067 N LYS D 187 24.541 149.587 16.757 1.00 49.02 N ANISOU 6067 N LYS D 187 5035 8211 5381 -1487 935 -1013 N ATOM 6068 CA LYS D 187 25.284 150.692 16.137 1.00 51.64 C ANISOU 6068 CA LYS D 187 5407 8682 5534 -1795 1033 -1027 C ATOM 6069 C LYS D 187 26.251 150.289 15.020 1.00 54.57 C ANISOU 6069 C LYS D 187 5571 9297 5866 -1976 1261 -1264 C ATOM 6070 O LYS D 187 26.526 151.097 14.130 1.00 56.28 O ANISOU 6070 O LYS D 187 5897 9646 5842 -2301 1364 -1261 O ATOM 6071 CB LYS D 187 26.073 151.474 17.192 1.00 52.66 C ANISOU 6071 CB LYS D 187 5473 8827 5708 -1851 952 -978 C ATOM 6072 CG LYS D 187 25.237 152.477 17.958 1.00 51.66 C ANISOU 6072 CG LYS D 187 5617 8497 5513 -1853 806 -790 C ATOM 6073 CD LYS D 187 26.099 153.353 18.831 1.00 53.28 C ANISOU 6073 CD LYS D 187 5786 8746 5712 -1995 761 -779 C ATOM 6074 CE LYS D 187 25.613 153.382 20.304 1.00 52.18 C ANISOU 6074 CE LYS D 187 5699 8480 5648 -1855 614 -715 C ATOM 6075 NZ LYS D 187 24.384 154.200 20.507 1.00 51.45 N ANISOU 6075 NZ LYS D 187 5894 8149 5506 -1841 569 -628 N ATOM 6076 N SER D 188 26.800 149.076 15.091 1.00 55.70 N ANISOU 6076 N SER D 188 5407 9496 6261 -1790 1340 -1479 N ATOM 6077 CA SER D 188 27.804 148.621 14.121 1.00 58.94 C ANISOU 6077 CA SER D 188 5545 10142 6705 -1942 1601 -1793 C ATOM 6078 C SER D 188 27.236 148.459 12.708 1.00 59.68 C ANISOU 6078 C SER D 188 5803 10336 6537 -2164 1784 -1897 C ATOM 6079 O SER D 188 27.916 148.785 11.732 1.00 62.70 O ANISOU 6079 O SER D 188 6122 10975 6725 -2501 2008 -2077 O ATOM 6080 CB SER D 188 28.447 147.308 14.577 1.00 60.20 C ANISOU 6080 CB SER D 188 5312 10264 7298 -1642 1616 -2009 C ATOM 6081 OG SER D 188 27.491 146.264 14.640 1.00 58.80 O ANISOU 6081 OG SER D 188 5208 9881 7252 -1389 1542 -1994 O ATOM 6082 N HIS D 189 25.996 147.976 12.607 1.00 57.65 N ANISOU 6082 N HIS D 189 5755 9905 6244 -2020 1684 -1781 N ATOM 6083 CA HIS D 189 25.353 147.724 11.312 1.00 58.51 C ANISOU 6083 CA HIS D 189 6029 10110 6093 -2240 1818 -1856 C ATOM 6084 C HIS D 189 24.606 148.942 10.765 1.00 57.77 C ANISOU 6084 C HIS D 189 6305 10020 5625 -2539 1698 -1550 C ATOM 6085 O HIS D 189 24.089 149.762 11.519 1.00 55.02 O ANISOU 6085 O HIS D 189 6130 9481 5294 -2442 1471 -1261 O ATOM 6086 CB HIS D 189 24.396 146.531 11.405 1.00 57.36 C ANISOU 6086 CB HIS D 189 5907 9784 6104 -1963 1762 -1889 C ATOM 6087 CG HIS D 189 25.092 145.207 11.457 1.00 59.39 C ANISOU 6087 CG HIS D 189 5818 10034 6714 -1758 1920 -2242 C ATOM 6088 ND1 HIS D 189 24.950 144.329 12.509 1.00 58.69 N ANISOU 6088 ND1 HIS D 189 5595 9703 7003 -1370 1755 -2204 N ATOM 6089 CD2 HIS D 189 25.949 144.618 10.590 1.00 62.73 C ANISOU 6089 CD2 HIS D 189 5987 10646 7202 -1898 2224 -2649 C ATOM 6090 CE1 HIS D 189 25.682 143.253 12.285 1.00 60.89 C ANISOU 6090 CE1 HIS D 189 5551 9976 7610 -1248 1917 -2546 C ATOM 6091 NE2 HIS D 189 26.297 143.403 11.127 1.00 63.68 N ANISOU 6091 NE2 HIS D 189 5810 10589 7798 -1549 2225 -2853 N ATOM 6092 N ARG D 190 24.566 149.039 9.438 1.00 59.95 N ANISOU 6092 N ARG D 190 6690 10512 5578 -2923 1848 -1627 N ATOM 6093 CA ARG D 190 23.894 150.147 8.747 1.00 60.62 C ANISOU 6093 CA ARG D 190 7121 10603 5308 -3265 1695 -1303 C ATOM 6094 C ARG D 190 22.383 150.072 8.879 1.00 57.84 C ANISOU 6094 C ARG D 190 7002 10004 4973 -3077 1441 -1022 C ATOM 6095 O ARG D 190 21.718 151.099 8.988 1.00 56.70 O ANISOU 6095 O ARG D 190 7089 9691 4762 -3133 1198 -681 O ATOM 6096 CB ARG D 190 24.247 150.162 7.246 1.00 64.93 C ANISOU 6096 CB ARG D 190 7725 11491 5452 -3798 1911 -1451 C ATOM 6097 CG ARG D 190 24.660 151.531 6.690 1.00 67.76 C ANISOU 6097 CG ARG D 190 8282 11985 5479 -4282 1852 -1225 C ATOM 6098 CD ARG D 190 25.637 151.513 5.507 1.00 72.86 C ANISOU 6098 CD ARG D 190 8849 13067 5768 -4840 2172 -1505 C ATOM 6099 NE ARG D 190 25.343 150.456 4.531 1.00 75.19 N ANISOU 6099 NE ARG D 190 9110 13574 5885 -5005 2391 -1788 N ATOM 6100 CZ ARG D 190 24.516 150.539 3.479 1.00 77.02 C ANISOU 6100 CZ ARG D 190 9630 13916 5718 -5389 2305 -1611 C ATOM 6101 NH1 ARG D 190 23.834 151.650 3.184 1.00 77.63 N ANISOU 6101 NH1 ARG D 190 10059 13890 5548 -5650 1963 -1102 N ATOM 6102 NH2 ARG D 190 24.370 149.473 2.696 1.00 78.85 N ANISOU 6102 NH2 ARG D 190 9790 14355 5816 -5528 2552 -1953 N ATOM 6103 N SER D 191 21.852 148.854 8.831 1.00 56.63 N ANISOU 6103 N SER D 191 6767 9818 4930 -2866 1500 -1182 N ATOM 6104 CA SER D 191 20.425 148.645 8.734 1.00 55.25 C ANISOU 6104 CA SER D 191 6786 9480 4726 -2758 1298 -962 C ATOM 6105 C SER D 191 19.977 147.311 9.309 1.00 53.23 C ANISOU 6105 C SER D 191 6392 9099 4734 -2386 1327 -1129 C ATOM 6106 O SER D 191 20.748 146.358 9.349 1.00 54.07 O ANISOU 6106 O SER D 191 6268 9278 4998 -2294 1537 -1458 O ATOM 6107 CB SER D 191 20.069 148.677 7.256 1.00 58.01 C ANISOU 6107 CB SER D 191 7312 10049 4680 -3208 1342 -932 C ATOM 6108 OG SER D 191 18.701 148.434 7.057 1.00 57.53 O ANISOU 6108 OG SER D 191 7415 9863 4582 -3139 1137 -718 O ATOM 6109 N TYR D 192 18.713 147.259 9.724 1.00 51.02 N ANISOU 6109 N TYR D 192 6244 8619 4521 -2189 1109 -899 N ATOM 6110 CA TYR D 192 18.074 146.025 10.176 1.00 49.55 C ANISOU 6110 CA TYR D 192 5984 8314 4530 -1901 1100 -1000 C ATOM 6111 C TYR D 192 16.683 145.938 9.582 1.00 49.16 C ANISOU 6111 C TYR D 192 6126 8234 4319 -1984 950 -809 C ATOM 6112 O TYR D 192 15.983 146.949 9.510 1.00 49.83 O ANISOU 6112 O TYR D 192 6366 8249 4320 -2058 744 -508 O ATOM 6113 CB TYR D 192 17.973 145.999 11.700 1.00 47.13 C ANISOU 6113 CB TYR D 192 5591 7792 4524 -1532 970 -916 C ATOM 6114 CG TYR D 192 19.247 145.604 12.390 1.00 47.92 C ANISOU 6114 CG TYR D 192 5452 7907 4848 -1396 1084 -1121 C ATOM 6115 CD1 TYR D 192 19.526 144.267 12.662 1.00 48.07 C ANISOU 6115 CD1 TYR D 192 5290 7869 5105 -1201 1156 -1333 C ATOM 6116 CD2 TYR D 192 20.177 146.571 12.783 1.00 48.82 C ANISOU 6116 CD2 TYR D 192 5511 8073 4967 -1467 1092 -1088 C ATOM 6117 CE1 TYR D 192 20.697 143.899 13.307 1.00 49.63 C ANISOU 6117 CE1 TYR D 192 5232 8054 5570 -1061 1208 -1487 C ATOM 6118 CE2 TYR D 192 21.352 146.212 13.424 1.00 50.10 C ANISOU 6118 CE2 TYR D 192 5422 8262 5350 -1350 1164 -1256 C ATOM 6119 CZ TYR D 192 21.608 144.874 13.682 1.00 50.58 C ANISOU 6119 CZ TYR D 192 5281 8261 5676 -1139 1209 -1445 C ATOM 6120 OH TYR D 192 22.769 144.520 14.325 1.00 52.94 O ANISOU 6120 OH TYR D 192 5300 8564 6252 -1011 1230 -1576 O ATOM 6121 N SER D 193 16.275 144.734 9.187 1.00 48.54 N ANISOU 6121 N SER D 193 6021 8184 4238 -1963 1036 -982 N ATOM 6122 CA SER D 193 14.973 144.528 8.565 1.00 48.04 C ANISOU 6122 CA SER D 193 6119 8127 4008 -2073 897 -821 C ATOM 6123 C SER D 193 14.182 143.409 9.235 1.00 45.73 C ANISOU 6123 C SER D 193 5774 7676 3925 -1784 851 -872 C ATOM 6124 O SER D 193 14.757 142.425 9.696 1.00 45.09 O ANISOU 6124 O SER D 193 5547 7529 4055 -1605 989 -1121 O ATOM 6125 CB SER D 193 15.151 144.228 7.072 1.00 50.98 C ANISOU 6125 CB SER D 193 6575 8764 4032 -2506 1053 -975 C ATOM 6126 OG SER D 193 15.500 145.406 6.362 1.00 52.67 O ANISOU 6126 OG SER D 193 6911 9131 3972 -2858 1003 -799 O ATOM 6127 N CYS D 194 12.860 143.589 9.288 1.00 44.84 N ANISOU 6127 N CYS D 194 5768 7492 3776 -1751 637 -620 N ATOM 6128 CA CYS D 194 11.911 142.547 9.666 1.00 43.64 C ANISOU 6128 CA CYS D 194 5603 7244 3734 -1585 584 -643 C ATOM 6129 C CYS D 194 11.115 142.180 8.419 1.00 45.33 C ANISOU 6129 C CYS D 194 5943 7607 3673 -1883 554 -617 C ATOM 6130 O CYS D 194 10.436 143.032 7.850 1.00 45.85 O ANISOU 6130 O CYS D 194 6115 7738 3570 -2065 367 -347 O ATOM 6131 CB CYS D 194 10.955 143.036 10.752 1.00 41.37 C ANISOU 6131 CB CYS D 194 5304 6794 3623 -1339 377 -402 C ATOM 6132 SG CYS D 194 9.723 141.797 11.233 1.00 40.56 S ANISOU 6132 SG CYS D 194 5186 6610 3617 -1194 310 -412 S ATOM 6133 N GLN D 195 11.204 140.919 8.008 1.00 46.54 N ANISOU 6133 N GLN D 195 6081 7799 3803 -1944 719 -892 N ATOM 6134 CA GLN D 195 10.598 140.440 6.771 1.00 48.99 C ANISOU 6134 CA GLN D 195 6515 8286 3814 -2288 738 -941 C ATOM 6135 C GLN D 195 9.463 139.474 7.111 1.00 47.76 C ANISOU 6135 C GLN D 195 6371 8021 3753 -2160 640 -916 C ATOM 6136 O GLN D 195 9.699 138.418 7.694 1.00 47.49 O ANISOU 6136 O GLN D 195 6259 7835 3949 -1959 754 -1136 O ATOM 6137 CB GLN D 195 11.668 139.753 5.920 1.00 52.46 C ANISOU 6137 CB GLN D 195 6924 8872 4139 -2521 1062 -1360 C ATOM 6138 CG GLN D 195 11.354 139.694 4.434 1.00 56.45 C ANISOU 6138 CG GLN D 195 7587 9662 4201 -3034 1118 -1415 C ATOM 6139 CD GLN D 195 12.565 139.334 3.576 1.00 60.19 C ANISOU 6139 CD GLN D 195 8010 10335 4524 -3326 1486 -1861 C ATOM 6140 OE1 GLN D 195 13.685 139.769 3.846 1.00 61.17 O ANISOU 6140 OE1 GLN D 195 8008 10467 4768 -3250 1630 -1986 O ATOM 6141 NE2 GLN D 195 12.342 138.552 2.530 1.00 63.00 N ANISOU 6141 NE2 GLN D 195 8451 10872 4613 -3689 1653 -2128 N ATOM 6142 N VAL D 196 8.239 139.849 6.740 1.00 47.59 N ANISOU 6142 N VAL D 196 6439 8070 3575 -2292 407 -629 N ATOM 6143 CA VAL D 196 7.039 139.088 7.061 1.00 47.15 C ANISOU 6143 CA VAL D 196 6382 7945 3588 -2203 286 -562 C ATOM 6144 C VAL D 196 6.488 138.487 5.770 1.00 50.62 C ANISOU 6144 C VAL D 196 6947 8586 3699 -2602 295 -628 C ATOM 6145 O VAL D 196 6.185 139.235 4.840 1.00 52.72 O ANISOU 6145 O VAL D 196 7305 9042 3684 -2914 154 -421 O ATOM 6146 CB VAL D 196 5.961 139.999 7.690 1.00 45.67 C ANISOU 6146 CB VAL D 196 6143 7690 3521 -2037 0 -194 C ATOM 6147 CG1 VAL D 196 4.725 139.197 8.064 1.00 45.07 C ANISOU 6147 CG1 VAL D 196 6034 7576 3516 -1964 -102 -147 C ATOM 6148 CG2 VAL D 196 6.509 140.722 8.920 1.00 43.06 C ANISOU 6148 CG2 VAL D 196 5706 7189 3467 -1708 7 -151 C ATOM 6149 N THR D 197 6.352 137.159 5.721 1.00 51.11 N ANISOU 6149 N THR D 197 7025 8600 3795 -2618 437 -898 N ATOM 6150 CA THR D 197 5.776 136.481 4.549 1.00 54.76 C ANISOU 6150 CA THR D 197 7616 9252 3937 -3021 464 -1002 C ATOM 6151 C THR D 197 4.392 135.962 4.933 1.00 53.78 C ANISOU 6151 C THR D 197 7488 9072 3872 -2952 259 -823 C ATOM 6152 O THR D 197 4.252 135.270 5.947 1.00 52.08 O ANISOU 6152 O THR D 197 7202 8638 3946 -2654 285 -895 O ATOM 6153 CB THR D 197 6.649 135.320 4.021 1.00 57.27 C ANISOU 6153 CB THR D 197 7960 9561 4239 -3163 813 -1511 C ATOM 6154 OG1 THR D 197 6.738 134.305 5.017 1.00 56.93 O ANISOU 6154 OG1 THR D 197 7830 9217 4583 -2813 882 -1681 O ATOM 6155 CG2 THR D 197 8.055 135.783 3.646 1.00 58.36 C ANISOU 6155 CG2 THR D 197 8052 9784 4339 -3243 1056 -1743 C ATOM 6156 N HIS D 198 3.386 136.324 4.134 1.00 55.50 N ANISOU 6156 N HIS D 198 7775 9497 3814 -3253 35 -569 N ATOM 6157 CA HIS D 198 1.993 135.966 4.385 1.00 55.18 C ANISOU 6157 CA HIS D 198 7698 9457 3809 -3233 -186 -370 C ATOM 6158 C HIS D 198 1.272 135.639 3.076 1.00 59.34 C ANISOU 6158 C HIS D 198 8356 10256 3935 -3733 -286 -328 C ATOM 6159 O HIS D 198 1.013 136.539 2.273 1.00 60.90 O ANISOU 6159 O HIS D 198 8595 10653 3891 -4005 -498 -47 O ATOM 6160 CB HIS D 198 1.273 137.114 5.088 1.00 53.38 C ANISOU 6160 CB HIS D 198 7322 9175 3786 -2980 -473 27 C ATOM 6161 CG HIS D 198 -0.160 136.817 5.399 1.00 53.22 C ANISOU 6161 CG HIS D 198 7204 9174 3843 -2946 -684 210 C ATOM 6162 ND1 HIS D 198 -1.198 137.241 4.599 1.00 55.36 N ANISOU 6162 ND1 HIS D 198 7454 9634 3946 -3205 -976 505 N ATOM 6163 CD2 HIS D 198 -0.726 136.114 6.407 1.00 51.55 C ANISOU 6163 CD2 HIS D 198 6899 8836 3850 -2719 -653 145 C ATOM 6164 CE1 HIS D 198 -2.342 136.825 5.109 1.00 54.76 C ANISOU 6164 CE1 HIS D 198 7247 9549 4008 -3111 -1098 588 C ATOM 6165 NE2 HIS D 198 -2.084 136.141 6.208 1.00 52.39 N ANISOU 6165 NE2 HIS D 198 6913 9070 3925 -2832 -894 367 N ATOM 6166 N GLU D 199 0.953 134.357 2.878 1.00 60.76 N ANISOU 6166 N GLU D 199 8608 10431 4048 -3875 -155 -589 N ATOM 6167 CA GLU D 199 0.193 133.885 1.711 1.00 64.56 C ANISOU 6167 CA GLU D 199 9220 11175 4135 -4379 -239 -585 C ATOM 6168 C GLU D 199 0.883 134.296 0.405 1.00 67.88 C ANISOU 6168 C GLU D 199 9793 11870 4130 -4856 -147 -673 C ATOM 6169 O GLU D 199 0.293 134.967 -0.447 1.00 70.23 O ANISOU 6169 O GLU D 199 10150 12432 4102 -5225 -420 -348 O ATOM 6170 CB GLU D 199 -1.263 134.383 1.772 1.00 64.82 C ANISOU 6170 CB GLU D 199 9152 11318 4159 -4405 -643 -129 C ATOM 6171 CG GLU D 199 -2.002 134.001 3.056 1.00 62.44 C ANISOU 6171 CG GLU D 199 8685 10803 4237 -3997 -706 -66 C ATOM 6172 CD GLU D 199 -2.357 132.521 3.138 1.00 63.01 C ANISOU 6172 CD GLU D 199 8839 10812 4288 -4104 -554 -352 C ATOM 6173 OE1 GLU D 199 -2.176 131.929 4.222 1.00 60.45 O ANISOU 6173 OE1 GLU D 199 8465 10233 4272 -3776 -428 -492 O ATOM 6174 OE2 GLU D 199 -2.818 131.940 2.131 1.00 66.40 O ANISOU 6174 OE2 GLU D 199 9398 11442 4389 -4543 -575 -427 O ATOM 6175 N GLY D 200 2.161 133.936 0.291 1.00 68.43 N ANISOU 6175 N GLY D 200 9904 11877 4221 -4851 223 -1100 N ATOM 6176 CA GLY D 200 2.964 134.227 -0.898 1.00 72.21 C ANISOU 6176 CA GLY D 200 10514 12636 4287 -5333 401 -1286 C ATOM 6177 C GLY D 200 3.638 135.592 -0.919 1.00 71.74 C ANISOU 6177 C GLY D 200 10424 12645 4191 -5300 307 -1027 C ATOM 6178 O GLY D 200 4.764 135.711 -1.397 1.00 73.36 O ANISOU 6178 O GLY D 200 10667 12957 4248 -5489 591 -1318 O ATOM 6179 N SER D 201 2.955 136.616 -0.406 1.00 70.23 N ANISOU 6179 N SER D 201 10151 12382 4152 -5073 -77 -506 N ATOM 6180 CA SER D 201 3.437 137.995 -0.445 1.00 70.52 C ANISOU 6180 CA SER D 201 10176 12447 4170 -5064 -234 -196 C ATOM 6181 C SER D 201 4.326 138.319 0.761 1.00 66.92 C ANISOU 6181 C SER D 201 9570 11696 4160 -4513 -73 -309 C ATOM 6182 O SER D 201 4.107 137.809 1.865 1.00 64.31 O ANISOU 6182 O SER D 201 9111 11107 4216 -4058 -32 -391 O ATOM 6183 CB SER D 201 2.245 138.957 -0.486 1.00 71.18 C ANISOU 6183 CB SER D 201 10221 12548 4276 -5074 -745 404 C ATOM 6184 OG SER D 201 2.673 140.306 -0.529 1.00 72.10 O ANISOU 6184 OG SER D 201 10339 12639 4418 -5069 -929 723 O ATOM 6185 N THR D 202 5.319 139.181 0.540 1.00 67.63 N ANISOU 6185 N THR D 202 9685 11846 4165 -4605 2 -294 N ATOM 6186 CA THR D 202 6.262 139.585 1.586 1.00 65.02 C ANISOU 6186 CA THR D 202 9220 11280 4205 -4156 147 -392 C ATOM 6187 C THR D 202 6.198 141.090 1.827 1.00 64.94 C ANISOU 6187 C THR D 202 9196 11204 4273 -4071 -149 55 C ATOM 6188 O THR D 202 6.215 141.875 0.880 1.00 67.22 O ANISOU 6188 O THR D 202 9615 11691 4236 -4489 -314 300 O ATOM 6189 CB THR D 202 7.705 139.180 1.231 1.00 66.13 C ANISOU 6189 CB THR D 202 9360 11515 4253 -4298 569 -869 C ATOM 6190 OG1 THR D 202 7.781 137.757 1.134 1.00 66.93 O ANISOU 6190 OG1 THR D 202 9442 11586 4404 -4300 847 -1319 O ATOM 6191 CG2 THR D 202 8.694 139.648 2.296 1.00 63.48 C ANISOU 6191 CG2 THR D 202 8870 10959 4291 -3863 678 -933 C ATOM 6192 N VAL D 203 6.121 141.466 3.105 1.00 62.09 N ANISOU 6192 N VAL D 203 8686 10560 4346 -3556 -219 153 N ATOM 6193 CA VAL D 203 6.216 142.853 3.546 1.00 62.00 C ANISOU 6193 CA VAL D 203 8636 10411 4510 -3397 -434 480 C ATOM 6194 C VAL D 203 7.513 142.978 4.336 1.00 59.96 C ANISOU 6194 C VAL D 203 8301 10035 4449 -3140 -162 222 C ATOM 6195 O VAL D 203 7.773 142.178 5.239 1.00 57.96 O ANISOU 6195 O VAL D 203 7935 9644 4444 -2812 27 -40 O ATOM 6196 CB VAL D 203 5.020 143.246 4.443 1.00 60.80 C ANISOU 6196 CB VAL D 203 8347 10037 4717 -3028 -718 763 C ATOM 6197 CG1 VAL D 203 5.201 144.652 5.019 1.00 60.85 C ANISOU 6197 CG1 VAL D 203 8295 9842 4983 -2819 -890 1017 C ATOM 6198 CG2 VAL D 203 3.722 143.157 3.654 1.00 63.00 C ANISOU 6198 CG2 VAL D 203 8658 10440 4841 -3279 -1023 1043 C ATOM 6199 N GLU D 204 8.320 143.978 3.989 1.00 61.46 N ANISOU 6199 N GLU D 204 8550 10280 4522 -3317 -169 321 N ATOM 6200 CA GLU D 204 9.581 144.251 4.674 1.00 60.18 C ANISOU 6200 CA GLU D 204 8305 10033 4527 -3120 57 113 C ATOM 6201 C GLU D 204 9.563 145.671 5.249 1.00 58.95 C ANISOU 6201 C GLU D 204 8141 9690 4569 -2962 -173 440 C ATOM 6202 O GLU D 204 9.167 146.616 4.569 1.00 61.09 O ANISOU 6202 O GLU D 204 8526 9987 4699 -3219 -440 785 O ATOM 6203 CB GLU D 204 10.757 144.078 3.702 1.00 63.52 C ANISOU 6203 CB GLU D 204 8792 10725 4617 -3528 337 -161 C ATOM 6204 CG GLU D 204 12.117 144.021 4.384 1.00 63.17 C ANISOU 6204 CG GLU D 204 8602 10624 4775 -3317 623 -471 C ATOM 6205 CD GLU D 204 13.252 143.728 3.417 1.00 66.69 C ANISOU 6205 CD GLU D 204 9053 11358 4928 -3717 951 -822 C ATOM 6206 OE1 GLU D 204 13.471 144.529 2.480 1.00 69.70 O ANISOU 6206 OE1 GLU D 204 9579 11961 4944 -4178 899 -666 O ATOM 6207 OE2 GLU D 204 13.939 142.701 3.604 1.00 66.64 O ANISOU 6207 OE2 GLU D 204 8892 11350 5076 -3584 1260 -1260 O ATOM 6208 N LYS D 205 9.983 145.806 6.505 1.00 56.15 N ANISOU 6208 N LYS D 205 7653 9131 4549 -2560 -85 335 N ATOM 6209 CA LYS D 205 10.226 147.111 7.121 1.00 55.15 C ANISOU 6209 CA LYS D 205 7515 8823 4618 -2422 -221 538 C ATOM 6210 C LYS D 205 11.667 147.159 7.582 1.00 53.64 C ANISOU 6210 C LYS D 205 7262 8660 4459 -2372 40 282 C ATOM 6211 O LYS D 205 12.234 146.134 7.963 1.00 51.48 O ANISOU 6211 O LYS D 205 6882 8432 4247 -2236 279 -34 O ATOM 6212 CB LYS D 205 9.290 147.352 8.299 1.00 53.58 C ANISOU 6212 CB LYS D 205 7201 8366 4792 -2016 -371 647 C ATOM 6213 CG LYS D 205 7.840 147.540 7.902 1.00 55.14 C ANISOU 6213 CG LYS D 205 7404 8511 5036 -2040 -666 931 C ATOM 6214 CD LYS D 205 7.571 148.932 7.355 1.00 58.36 C ANISOU 6214 CD LYS D 205 7889 8805 5481 -2199 -972 1302 C ATOM 6215 CE LYS D 205 6.287 148.964 6.542 1.00 61.05 C ANISOU 6215 CE LYS D 205 8244 9171 5782 -2353 -1296 1609 C ATOM 6216 NZ LYS D 205 5.948 150.348 6.114 1.00 64.48 N ANISOU 6216 NZ LYS D 205 8726 9417 6356 -2461 -1663 2019 N ATOM 6217 N THR D 206 12.246 148.358 7.537 1.00 54.45 N ANISOU 6217 N THR D 206 7423 8718 4547 -2487 -31 435 N ATOM 6218 CA THR D 206 13.671 148.567 7.777 1.00 54.08 C ANISOU 6218 CA THR D 206 7323 8747 4480 -2533 194 226 C ATOM 6219 C THR D 206 13.861 149.706 8.771 1.00 53.11 C ANISOU 6219 C THR D 206 7179 8388 4612 -2326 81 368 C ATOM 6220 O THR D 206 13.083 150.662 8.783 1.00 53.55 O ANISOU 6220 O THR D 206 7318 8255 4773 -2313 -182 667 O ATOM 6221 CB THR D 206 14.403 148.902 6.455 1.00 57.47 C ANISOU 6221 CB THR D 206 7875 9446 4515 -3050 273 229 C ATOM 6222 OG1 THR D 206 14.035 147.953 5.449 1.00 58.72 O ANISOU 6222 OG1 THR D 206 8082 9826 4400 -3305 355 112 O ATOM 6223 CG2 THR D 206 15.910 148.858 6.634 1.00 57.59 C ANISOU 6223 CG2 THR D 206 7773 9597 4510 -3108 567 -72 C ATOM 6224 N VAL D 207 14.892 149.592 9.606 1.00 51.89 N ANISOU 6224 N VAL D 207 6899 8232 4583 -2170 271 143 N ATOM 6225 CA VAL D 207 15.219 150.624 10.590 1.00 51.68 C ANISOU 6225 CA VAL D 207 6856 8015 4766 -2018 204 220 C ATOM 6226 C VAL D 207 16.741 150.703 10.781 1.00 52.48 C ANISOU 6226 C VAL D 207 6868 8257 4815 -2114 415 13 C ATOM 6227 O VAL D 207 17.450 149.706 10.589 1.00 52.42 O ANISOU 6227 O VAL D 207 6730 8435 4753 -2130 628 -251 O ATOM 6228 CB VAL D 207 14.464 150.372 11.920 1.00 49.35 C ANISOU 6228 CB VAL D 207 6463 7515 4771 -1621 150 192 C ATOM 6229 CG1 VAL D 207 15.081 149.220 12.706 1.00 47.55 C ANISOU 6229 CG1 VAL D 207 6075 7369 4622 -1429 337 -78 C ATOM 6230 CG2 VAL D 207 14.405 151.638 12.761 1.00 49.64 C ANISOU 6230 CG2 VAL D 207 6525 7323 5012 -1520 40 303 C ATOM 6231 N ALA D 208 17.230 151.891 11.138 1.00 53.53 N ANISOU 6231 N ALA D 208 7054 8289 4998 -2183 351 122 N ATOM 6232 CA ALA D 208 18.667 152.156 11.248 1.00 54.56 C ANISOU 6232 CA ALA D 208 7101 8567 5062 -2331 523 -37 C ATOM 6233 C ALA D 208 18.983 153.106 12.412 1.00 54.03 C ANISOU 6233 C ALA D 208 7026 8307 5196 -2193 456 9 C ATOM 6234 O ALA D 208 18.174 153.981 12.722 1.00 54.55 O ANISOU 6234 O ALA D 208 7215 8117 5393 -2123 268 207 O ATOM 6235 CB ALA D 208 19.176 152.743 9.942 1.00 57.87 C ANISOU 6235 CB ALA D 208 7651 9173 5163 -2798 545 53 C ATOM 6236 N PRO D 209 20.159 152.942 13.059 1.00 53.26 N ANISOU 6236 N PRO D 209 6766 8326 5146 -2164 609 -190 N ATOM 6237 CA PRO D 209 20.521 153.803 14.206 1.00 53.11 C ANISOU 6237 CA PRO D 209 6741 8158 5279 -2080 556 -172 C ATOM 6238 C PRO D 209 20.653 155.290 13.865 1.00 54.63 C ANISOU 6238 C PRO D 209 7126 8220 5412 -2340 448 17 C ATOM 6239 O PRO D 209 21.251 155.634 12.846 1.00 57.09 O ANISOU 6239 O PRO D 209 7504 8685 5503 -2677 487 70 O ATOM 6240 CB PRO D 209 21.876 153.240 14.660 1.00 53.20 C ANISOU 6240 CB PRO D 209 6520 8386 5308 -2079 725 -401 C ATOM 6241 CG PRO D 209 22.410 152.506 13.476 1.00 54.58 C ANISOU 6241 CG PRO D 209 6602 8816 5322 -2260 890 -538 C ATOM 6242 CD PRO D 209 21.206 151.941 12.784 1.00 53.96 C ANISOU 6242 CD PRO D 209 6641 8679 5181 -2207 829 -457 C TER 6243 PRO D 209 ATOM 6244 P DT T 1 -14.804 137.092 -3.437 1.00 70.52 P ATOM 6245 OP1 DT T 1 -15.929 136.203 -3.050 1.00 70.26 O ATOM 6246 OP2 DT T 1 -14.646 137.498 -4.858 1.00 69.53 O ATOM 6247 O5' DT T 1 -14.881 138.408 -2.541 1.00 66.55 O ATOM 6248 C5' DT T 1 -13.785 139.341 -2.493 1.00 63.76 C ATOM 6249 C4' DT T 1 -14.300 140.742 -2.257 1.00 61.39 C ATOM 6250 O4' DT T 1 -15.235 141.100 -3.303 1.00 60.65 O ATOM 6251 C3' DT T 1 -15.040 140.943 -0.930 1.00 58.74 C ATOM 6252 O3' DT T 1 -14.608 142.151 -0.290 1.00 55.25 O ATOM 6253 C2' DT T 1 -16.499 141.038 -1.340 1.00 59.11 C ATOM 6254 C1' DT T 1 -16.410 141.646 -2.726 1.00 59.69 C ATOM 6255 N1 DT T 1 -17.552 141.324 -3.614 1.00 58.90 N ATOM 6256 C2 DT T 1 -18.453 142.322 -3.918 1.00 58.89 C ATOM 6257 O2 DT T 1 -18.352 143.464 -3.501 1.00 58.10 O ATOM 6258 N3 DT T 1 -19.483 141.932 -4.741 1.00 58.21 N ATOM 6259 C4 DT T 1 -19.698 140.673 -5.270 1.00 58.79 C ATOM 6260 O4 DT T 1 -20.668 140.472 -5.996 1.00 58.76 O ATOM 6261 C5 DT T 1 -18.716 139.674 -4.906 1.00 58.86 C ATOM 6262 C7 DT T 1 -18.865 138.282 -5.434 1.00 59.18 C ATOM 6263 C6 DT T 1 -17.708 140.045 -4.106 1.00 59.10 C ATOM 6264 P DT T 2 -14.295 142.176 1.285 0.88 51.63 P ATOM 6265 OP1 DT T 2 -13.758 143.520 1.625 0.88 51.61 O ATOM 6266 OP2 DT T 2 -13.508 140.962 1.624 0.88 51.45 O1- ATOM 6267 O5' DT T 2 -15.739 142.051 1.945 0.88 46.82 O ATOM 6268 C5' DT T 2 -16.619 143.185 2.032 0.88 41.94 C ATOM 6269 C4' DT T 2 -17.995 142.759 2.490 0.88 39.43 C ATOM 6270 O4' DT T 2 -18.549 141.777 1.586 0.88 36.12 O ATOM 6271 C3' DT T 2 -18.061 142.095 3.861 0.88 37.77 C ATOM 6272 O3' DT T 2 -18.091 143.068 4.909 0.88 38.49 O ATOM 6273 C2' DT T 2 -19.362 141.320 3.773 0.88 35.97 C ATOM 6274 C1' DT T 2 -19.418 140.901 2.305 0.88 35.16 C ATOM 6275 N1 DT T 2 -18.978 139.508 2.060 0.88 32.92 N ATOM 6276 C2 DT T 2 -19.937 138.520 2.031 0.88 31.85 C ATOM 6277 O2 DT T 2 -21.129 138.741 2.172 0.88 32.37 O ATOM 6278 N3 DT T 2 -19.449 137.256 1.807 0.88 31.92 N ATOM 6279 C4 DT T 2 -18.129 136.889 1.627 0.88 31.67 C ATOM 6280 O4 DT T 2 -17.842 135.710 1.444 0.88 32.19 O ATOM 6281 C5 DT T 2 -17.174 137.973 1.690 0.88 32.33 C ATOM 6282 C7 DT T 2 -15.720 137.671 1.512 0.88 32.60 C ATOM 6283 C6 DT T 2 -17.640 139.211 1.903 0.88 32.50 C ATOM 6284 P DT T 3 -17.860 142.628 6.440 0.88 38.36 P ATOM 6285 OP1 DT T 3 -16.716 143.409 6.970 0.88 41.06 O ATOM 6286 OP2 DT T 3 -17.838 141.147 6.517 0.88 38.09 O1- ATOM 6287 O5' DT T 3 -19.182 143.149 7.155 0.88 36.41 O ATOM 6288 C5' DT T 3 -19.663 144.483 6.919 0.88 35.97 C ATOM 6289 C4' DT T 3 -20.449 144.973 8.111 0.88 35.29 C ATOM 6290 O4' DT T 3 -21.548 144.065 8.362 0.88 33.50 O ATOM 6291 C3' DT T 3 -19.662 145.044 9.419 0.88 34.93 C ATOM 6292 O3' DT T 3 -20.139 146.125 10.221 0.88 38.64 O ATOM 6293 C2' DT T 3 -19.996 143.733 10.100 0.88 33.85 C ATOM 6294 C1' DT T 3 -21.443 143.534 9.673 0.88 32.52 C ATOM 6295 N1 DT T 3 -21.927 142.143 9.632 0.88 30.09 N ATOM 6296 C2 DT T 3 -23.185 141.888 10.129 0.88 28.31 C ATOM 6297 O2 DT T 3 -23.897 142.748 10.623 0.88 27.65 O ATOM 6298 N3 DT T 3 -23.577 140.577 10.043 0.88 27.21 N ATOM 6299 C4 DT T 3 -22.864 139.523 9.503 0.88 27.29 C ATOM 6300 O4 DT T 3 -23.351 138.395 9.498 0.88 25.34 O ATOM 6301 C5 DT T 3 -21.556 139.864 8.991 0.88 27.23 C ATOM 6302 C7 DT T 3 -20.706 138.789 8.393 0.88 27.52 C ATOM 6303 C6 DT T 3 -21.164 141.141 9.069 0.88 28.58 C ATOM 6304 P DT T 4 -19.134 147.263 10.703 0.88 41.34 P ATOM 6305 OP1 DT T 4 -18.438 147.795 9.499 0.88 43.35 O1- ATOM 6306 OP2 DT T 4 -18.337 146.715 11.828 0.88 44.17 O ATOM 6307 O5' DT T 4 -20.114 148.384 11.267 0.88 44.53 O TER 6308 DT T 4 HETATM 6309 O HOH A 501 -33.635 146.219 -11.014 1.00 33.42 O HETATM 6310 O HOH A 502 -31.519 128.799 -7.354 1.00 20.20 O HETATM 6311 O HOH A 503 -74.078 107.544 12.683 1.00 30.14 O HETATM 6312 O HOH A 504 -36.497 119.200 -1.160 1.00 22.13 O HETATM 6313 O HOH A 505 -49.824 127.769 -0.056 1.00 25.78 O HETATM 6314 O HOH A 506 -46.228 134.618 9.607 1.00 34.90 O HETATM 6315 O HOH A 507 -41.978 141.855 -3.306 1.00 29.91 O HETATM 6316 O HOH A 508 -70.422 103.099 14.785 1.00 26.11 O HETATM 6317 O HOH A 509 -37.874 142.140 14.413 1.00 30.57 O HETATM 6318 O HOH A 510 -33.404 121.782 4.923 1.00 33.63 O HETATM 6319 O HOH A 511 -26.028 132.360 -6.520 1.00 28.47 O HETATM 6320 O HOH A 512 -19.084 147.342 3.358 1.00 39.72 O HETATM 6321 O HOH A 513 -60.544 105.674 -2.012 1.00 48.92 O HETATM 6322 O HOH A 514 -27.553 140.581 -7.245 1.00 34.09 O HETATM 6323 O HOH A 515 -42.552 116.440 -3.945 1.00 33.04 O HETATM 6324 O HOH A 516 -54.170 123.415 -0.449 1.00 37.75 O HETATM 6325 O HOH A 517 -23.880 147.936 5.205 1.00 37.51 O HETATM 6326 O HOH A 518 -49.328 132.996 2.629 1.00 25.43 O HETATM 6327 O HOH A 519 -42.451 121.136 4.896 1.00 35.39 O HETATM 6328 O HOH A 520 -35.643 123.039 -10.383 1.00 21.72 O HETATM 6329 O HOH A 521 -44.613 125.719 -10.470 1.00 37.67 O HETATM 6330 O HOH A 522 -26.732 136.812 -7.118 1.00 24.38 O HETATM 6331 O HOH A 523 -40.536 148.993 -5.580 1.00 32.54 O HETATM 6332 O HOH A 524 -64.055 121.600 1.155 1.00 41.00 O HETATM 6333 O HOH A 525 -44.160 126.808 14.165 1.00 38.06 O HETATM 6334 O HOH A 526 -58.000 120.834 9.821 1.00 30.99 O HETATM 6335 O HOH A 527 -37.168 124.359 9.675 1.00 35.86 O HETATM 6336 O HOH A 528 -44.884 128.331 9.178 1.00 28.65 O HETATM 6337 O HOH A 529 -59.164 101.015 12.394 1.00 40.15 O HETATM 6338 O HOH A 530 -30.368 123.903 7.844 1.00 25.91 O HETATM 6339 O HOH A 531 -41.056 144.714 7.318 1.00 28.33 O HETATM 6340 O HOH A 532 -43.212 130.888 -5.128 1.00 26.52 O HETATM 6341 O HOH A 533 -70.143 102.161 17.918 1.00 34.00 O HETATM 6342 O HOH A 534 -40.740 149.986 -2.835 1.00 24.86 O HETATM 6343 O HOH A 535 -45.863 127.399 11.866 1.00 36.79 O HETATM 6344 O HOH A 536 -71.566 105.631 6.462 1.00 31.17 O HETATM 6345 O HOH A 537 -42.688 127.963 -10.067 1.00 38.66 O HETATM 6346 O HOH A 538 -72.354 116.162 21.103 1.00 35.37 O HETATM 6347 O HOH A 539 -57.217 121.725 14.697 1.00 45.73 O HETATM 6348 O HOH A 540 -50.401 121.584 -8.655 1.00 35.26 O HETATM 6349 O HOH A 541 -38.303 142.128 -10.374 1.00 52.19 O HETATM 6350 O HOH A 542 -32.441 149.868 4.729 1.00 36.88 O HETATM 6351 O HOH A 543 -31.155 127.837 10.401 1.00 25.29 O HETATM 6352 O HOH A 544 -30.155 146.103 13.423 1.00 32.37 O HETATM 6353 O HOH A 545 -24.065 127.941 -4.572 1.00 27.29 O HETATM 6354 O HOH A 546 -74.178 111.052 9.586 1.00 22.36 O HETATM 6355 O HOH A 547 -39.480 126.579 -12.573 1.00 29.08 O HETATM 6356 O HOH A 548 -45.140 117.563 -3.650 1.00 32.21 O HETATM 6357 O HOH A 549 -43.650 119.433 -12.354 1.00 53.31 O HETATM 6358 O HOH A 550 -22.859 130.063 0.052 1.00 27.73 O HETATM 6359 O HOH A 551 -46.169 116.672 -6.168 1.00 27.95 O HETATM 6360 O HOH A 552 -35.212 121.005 1.911 1.00 33.51 O HETATM 6361 O HOH A 553 -42.601 130.434 -7.963 1.00 23.37 O HETATM 6362 O HOH A 554 -25.190 153.798 5.406 1.00 46.45 O HETATM 6363 O HOH A 555 -36.756 117.955 -7.246 1.00 30.91 O HETATM 6364 O HOH A 556 -45.625 143.619 8.450 1.00 38.25 O HETATM 6365 O HOH A 557 -29.669 147.458 16.496 1.00 35.05 O HETATM 6366 O HOH A 558 -40.328 115.642 0.147 1.00 38.44 O HETATM 6367 O HOH A 559 -68.740 99.028 17.048 1.00 32.99 O HETATM 6368 O HOH A 560 -44.773 119.627 4.350 1.00 38.96 O HETATM 6369 O HOH A 561 -60.639 98.896 11.121 1.00 45.19 O HETATM 6370 O HOH A 562 -51.736 129.765 0.784 1.00 34.41 O HETATM 6371 O HOH B 301 -17.451 129.618 13.406 1.00 24.46 O HETATM 6372 O HOH B 302 -61.249 95.362 6.289 1.00 36.45 O HETATM 6373 O HOH B 303 -26.852 130.580 29.363 1.00 25.91 O HETATM 6374 O HOH B 304 -43.196 129.136 15.795 1.00 22.58 O HETATM 6375 O HOH B 305 -35.061 138.707 32.843 1.00 28.95 O HETATM 6376 O HOH B 306 -31.231 123.633 25.492 1.00 30.09 O HETATM 6377 O HOH B 307 -45.259 125.594 26.829 1.00 29.28 O HETATM 6378 O HOH B 308 -30.018 148.443 21.849 1.00 39.70 O HETATM 6379 O HOH B 309 -30.947 135.067 30.476 1.00 31.64 O HETATM 6380 O HOH B 310 -30.103 141.171 28.811 1.00 25.50 O HETATM 6381 O HOH B 311 -27.736 136.596 15.669 1.00 24.00 O HETATM 6382 O HOH B 312 -30.254 128.151 30.922 1.00 28.09 O HETATM 6383 O HOH B 313 -41.527 125.720 17.052 1.00 37.82 O HETATM 6384 O HOH B 314 -37.396 122.518 20.972 1.00 26.55 O HETATM 6385 O HOH B 315 -58.245 96.764 10.818 1.00 40.45 O HETATM 6386 O HOH B 316 -16.252 132.883 10.243 1.00 34.54 O HETATM 6387 O HOH B 317 -44.384 138.998 18.863 1.00 27.11 O HETATM 6388 O HOH B 318 -49.870 125.925 26.211 1.00 35.16 O HETATM 6389 O HOH B 319 -43.001 141.828 22.403 1.00 39.30 O HETATM 6390 O HOH B 320 -50.449 141.944 16.510 1.00 26.15 O HETATM 6391 O HOH B 321 -52.578 119.199 16.207 1.00 39.05 O HETATM 6392 O HOH B 322 -60.384 98.266 8.268 1.00 40.15 O HETATM 6393 O HOH B 323 -28.547 135.214 24.777 1.00 20.02 O HETATM 6394 O HOH B 324 -26.412 139.443 17.661 1.00 30.13 O HETATM 6395 O HOH B 325 -22.126 124.795 27.055 1.00 41.57 O HETATM 6396 O HOH B 326 -40.193 141.518 12.784 1.00 30.83 O HETATM 6397 O HOH B 327 -55.877 103.039 8.781 1.00 37.69 O HETATM 6398 O HOH B 328 -22.913 133.797 18.605 1.00 23.71 O HETATM 6399 O HOH B 329 -40.399 132.439 39.216 1.00 47.00 O HETATM 6400 O HOH B 330 -46.555 132.670 12.534 1.00 38.01 O HETATM 6401 O HOH B 331 -26.726 127.898 7.892 1.00 28.39 O HETATM 6402 O HOH B 332 -22.286 125.268 13.524 1.00 38.38 O HETATM 6403 O HOH B 333 -34.581 126.051 29.650 1.00 30.80 O HETATM 6404 O HOH B 334 -37.637 119.477 25.160 1.00 36.40 O HETATM 6405 O HOH B 335 -30.052 119.726 13.559 1.00 46.41 O HETATM 6406 O HOH B 336 -44.798 137.460 16.422 1.00 24.33 O HETATM 6407 O HOH B 337 -32.067 125.785 12.249 1.00 29.82 O HETATM 6408 O HOH B 338 -50.093 135.378 23.905 1.00 32.66 O HETATM 6409 O HOH B 339 -37.876 144.648 18.294 1.00 34.36 O HETATM 6410 O HOH B 340 -45.460 120.249 20.696 1.00 33.57 O HETATM 6411 O HOH B 341 -44.208 140.042 24.983 1.00 30.72 O HETATM 6412 O HOH B 342 -51.242 133.623 28.010 1.00 44.92 O HETATM 6413 O HOH B 343 -18.400 138.192 18.696 1.00 44.34 O HETATM 6414 O HOH B 344 -18.728 131.224 26.140 1.00 28.87 O HETATM 6415 O HOH B 345 -50.366 102.073 28.474 1.00 52.10 O HETATM 6416 O HOH B 346 -46.735 131.054 17.823 1.00 46.72 O HETATM 6417 O HOH B 347 -50.490 139.252 32.687 1.00 28.38 O HETATM 6418 O HOH B 348 -39.242 121.077 27.318 1.00 30.17 O HETATM 6419 O HOH B 349 -46.162 139.802 11.091 1.00 22.17 O HETATM 6420 O HOH B 350 -33.213 149.643 18.721 1.00 49.04 O HETATM 6421 O HOH B 351 -33.405 149.095 24.650 1.00 41.61 O HETATM 6422 O HOH B 352 -37.528 127.985 33.543 1.00 28.91 O HETATM 6423 O HOH B 353 -40.095 122.964 19.212 1.00 40.48 O HETATM 6424 O HOH B 354 -45.142 141.248 17.111 1.00 37.06 O HETATM 6425 O HOH B 355 -41.006 144.657 31.691 1.00 39.18 O HETATM 6426 O HOH B 356 -33.355 121.409 25.862 1.00 41.27 O HETATM 6427 O HOH B 357 -18.958 124.338 27.223 1.00 51.42 O HETATM 6428 O HOH B 358 -20.425 141.444 23.097 1.00 39.06 O HETATM 6429 O HOH B 359 -32.194 147.025 17.699 1.00 46.50 O HETATM 6430 O HOH C 501 -2.547 141.484 36.024 1.00 23.68 O HETATM 6431 O HOH C 502 3.749 120.556 35.485 1.00 26.12 O HETATM 6432 O HOH C 503 0.974 90.399 25.450 1.00 47.68 O HETATM 6433 O HOH C 504 -3.696 156.297 32.498 1.00 27.71 O HETATM 6434 O HOH C 505 18.109 127.087 30.892 1.00 36.82 O HETATM 6435 O HOH C 506 16.081 133.923 24.076 1.00 35.65 O HETATM 6436 O HOH C 507 1.468 135.825 27.886 1.00 34.54 O HETATM 6437 O HOH C 508 -3.218 120.675 25.903 1.00 44.25 O HETATM 6438 O HOH C 509 9.038 113.133 17.557 1.00 25.17 O HETATM 6439 O HOH C 510 1.573 125.277 21.790 1.00 43.18 O HETATM 6440 O HOH C 511 5.941 122.996 42.097 1.00 46.78 O HETATM 6441 O HOH C 512 -0.067 140.589 37.290 1.00 20.07 O HETATM 6442 O HOH C 513 2.481 121.193 41.128 1.00 49.33 O HETATM 6443 O HOH C 514 16.714 129.964 34.038 1.00 31.62 O HETATM 6444 O HOH C 515 -11.402 153.098 22.883 1.00 42.41 O HETATM 6445 O HOH C 516 5.070 132.078 34.818 1.00 25.96 O HETATM 6446 O HOH C 517 1.701 124.909 18.842 1.00 32.85 O HETATM 6447 O HOH C 518 3.824 132.666 28.931 1.00 34.65 O HETATM 6448 O HOH C 519 -6.527 145.933 29.884 1.00 28.35 O HETATM 6449 O HOH C 520 18.927 111.013 33.497 1.00 46.86 O HETATM 6450 O HOH C 521 -2.173 140.733 29.056 1.00 50.34 O HETATM 6451 O HOH C 522 20.666 131.120 38.440 1.00 40.25 O HETATM 6452 O HOH C 523 -5.940 143.101 29.151 1.00 36.50 O HETATM 6453 O HOH D 301 -8.557 131.656 11.699 1.00 42.84 O HETATM 6454 O HOH D 302 -0.152 122.928 17.586 1.00 38.20 O HETATM 6455 O HOH D 303 -11.172 131.312 10.530 1.00 42.48 O HETATM 6456 O HOH D 304 -11.896 122.130 -2.960 1.00 39.75 O HETATM 6457 O HOH D 305 -12.973 118.113 12.886 1.00 29.10 O HETATM 6458 O HOH D 306 -7.628 118.552 20.075 1.00 36.79 O HETATM 6459 O HOH D 307 11.022 133.775 13.682 1.00 44.16 O HETATM 6460 O HOH D 308 -6.877 123.473 28.142 1.00 37.08 O HETATM 6461 O HOH D 309 2.626 147.791 6.978 1.00 50.33 O HETATM 6462 O HOH D 310 0.253 132.648 20.736 1.00 44.30 O HETATM 6463 O HOH D 311 -14.314 129.807 10.578 1.00 50.83 O HETATM 6464 O HOH D 312 3.874 131.973 21.307 1.00 37.45 O CONECT 150 725 CONECT 725 150 CONECT 1030 1443 CONECT 1443 1030 CONECT 1721 2236 CONECT 2236 1721 CONECT 2589 3043 CONECT 3043 2589 CONECT 3311 3866 CONECT 3866 3311 CONECT 4167 4566 CONECT 4566 4167 CONECT 4840 5355 CONECT 5355 4840 CONECT 5678 6132 CONECT 6132 5678 MASTER 511 0 0 15 98 0 0 6 6459 5 16 69 END
Display Options:
Goto PDB code:
3D presentation of molecule is powered by
3Dmol
, which supports all modern browsers and mobile devices via WebGL.
Hold mouse button:
left to rotate,middle to shift,right to zoom
Related entries of code: 5gkr
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
Check Database
Protein Sequence Similarity
3gjf
RCSB PDB
PDBbind
212aa, >3GJF_4|Chains... at 94%
3hae
RCSB PDB
PDBbind
212aa, >3HAE_4|Chains... at 94%
Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
No complexes with the same small molecule ligand are found!
Entry Information
PDB ID
5gkr
Complex Type
Protein-Nucleic Acid
PDBbind Subset
general set
Protein Name
71F12 fragment antigen binding (Fab)
Ligand Name
ssDNA (5-TTTTT-3)
EC.Number
E.C.-.-.-.-
Resolution
2.1(Å)
Affinity (Kd/Ki/IC50)
Kd=4.61nM
Release Year
2017
Protein/NA Sequence
Check fasta file
Primary Reference
(2017) Sci Rep Vol. 7: pp. 16428-16428
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
No matched UniProt accession number (AC) found!
Entrez Gene ID
No matched NCBI Entrez Gene ID found!
ASD
Information of known allosteric effects of PDB entries
This site has been visited
times since Nov 2007.
Copyright ©2007-2024 涓婃捣鐩堣禌鎬濅俊鎭鎶鏈夐檺鍏徃 缃戠珯澶囨鍙凤細
娌狪CP澶2021015625鍙-3
娌叕缃戝畨澶囷細
姝ｅ湪鐢宠涓
Technical Support锛堟妧鏈敮鎸侊級:
yingsaisi@foxmail.com
times since Nov 2007. 
娌叕缃戝畨澶囷細姝ｅ湪鐢宠涓