HEADER MEMBRANE PROTEIN 19-JUN-17 5O9H TITLE CRYSTAL STRUCTURE OF THERMOSTABILISED HUMAN C5A ANAPHYLATOXIN TITLE 2 CHEMOTACTIC RECEPTOR 1 (C5AR) IN COMPLEX WITH NDT9513727 CAVEAT 5O9H TLA A 402 HAS WRONG CHIRALITY AT ATOM C2 TLA A 402 HAS WRONG CAVEAT 2 5O9H CHIRALITY AT ATOM C3 TLA A 403 HAS WRONG CHIRALITY AT ATOM CAVEAT 3 5O9H C2 TLA A 403 HAS WRONG CHIRALITY AT ATOM C3 TLA B 402 HAS CAVEAT 4 5O9H WRONG CHIRALITY AT ATOM C2 TLA B 402 HAS WRONG CHIRALITY AT CAVEAT 5 5O9H ATOM C3 COMPND MOL_ID: 1; COMPND 2 MOLECULE: C5A ANAPHYLATOXIN CHEMOTACTIC RECEPTOR 1; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: C5A ANAPHYLATOXIN CHEMOTACTIC RECEPTOR,C5AR; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: C5AR1, C5AR, C5R1; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: SF9; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC KEYWDS GPCR, 7TM, SIGNALLING PROTEIN, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR N.ROBERTSON,M.RAPPAS,A.S.DORE,J.BROWN,G.BOTTEGONI,M.KOGLIN, AUTHOR 2 J.CANSFIELD,A.JAZAYERI,R.M.COOKE,F.H.MARSHALL REVDAT 3 31-JAN-18 5O9H 1 SOURCE REVDAT 2 17-JAN-18 5O9H 1 JRNL REVDAT 1 10-JAN-18 5O9H 0 JRNL AUTH N.ROBERTSON,M.RAPPAS,A.S.DORE,J.BROWN,G.BOTTEGONI,M.KOGLIN, JRNL AUTH 2 J.CANSFIELD,A.JAZAYERI,R.M.COOKE,F.H.MARSHALL JRNL TITL STRUCTURE OF THE COMPLEMENT C5A RECEPTOR BOUND TO THE JRNL TITL 2 EXTRA-HELICAL ANTAGONIST NDT9513727. JRNL REF NATURE V. 553 111 2018 JRNL REFN ESSN 1476-4687 JRNL PMID 29300009 JRNL DOI 10.1038/NATURE25025 REMARK 2 REMARK 2 RESOLUTION. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.9_1692 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.89 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2 REMARK 3 NUMBER OF REFLECTIONS : 26440 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.210 REMARK 3 R VALUE (WORKING SET) : 0.208 REMARK 3 FREE R VALUE : 0.239 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110 REMARK 3 FREE R VALUE TEST SET COUNT : 1352 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 19.8949 - 5.7741 0.96 2542 126 0.1980 0.1848 REMARK 3 2 5.7741 - 4.6017 0.99 2521 141 0.1936 0.2212 REMARK 3 3 4.6017 - 4.0255 0.99 2526 142 0.1760 0.2156 REMARK 3 4 4.0255 - 3.6600 0.99 2518 128 0.1892 0.2066 REMARK 3 5 3.6600 - 3.3990 1.00 2496 140 0.2099 0.2695 REMARK 3 6 3.3990 - 3.1995 1.00 2492 135 0.2195 0.2541 REMARK 3 7 3.1995 - 3.0398 1.00 2525 132 0.2323 0.2716 REMARK 3 8 3.0398 - 2.9079 1.00 2496 145 0.2539 0.3103 REMARK 3 9 2.9079 - 2.7963 1.00 2485 137 0.2554 0.3098 REMARK 3 10 2.7963 - 2.7001 1.00 2487 126 0.2695 0.3211 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.320 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.760 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.24 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.004 5377 REMARK 3 ANGLE : 1.035 7173 REMARK 3 CHIRALITY : 0.030 800 REMARK 3 PLANARITY : 0.004 859 REMARK 3 DIHEDRAL : 12.326 1707 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 11 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 31 THROUGH 63 ) REMARK 3 ORIGIN FOR THE GROUP (A): 75.5756 -10.2788 22.7269 REMARK 3 T TENSOR REMARK 3 T11: 0.1313 T22: 0.4889 REMARK 3 T33: 0.2546 T12: 0.0295 REMARK 3 T13: -0.0375 T23: 0.0450 REMARK 3 L TENSOR REMARK 3 L11: 0.0280 L22: 0.0345 REMARK 3 L33: 0.0139 L12: 0.0016 REMARK 3 L13: 0.0032 L23: -0.0418 REMARK 3 S TENSOR REMARK 3 S11: -0.0987 S12: 0.2188 S13: 0.1162 REMARK 3 S21: 0.0029 S22: 0.2073 S23: 0.1530 REMARK 3 S31: -0.0618 S32: -0.1293 S33: 0.0000 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 64 THROUGH 104 ) REMARK 3 ORIGIN FOR THE GROUP (A): 83.0024 -4.5054 25.8745 REMARK 3 T TENSOR REMARK 3 T11: 0.0911 T22: 0.2097 REMARK 3 T33: 0.1315 T12: 0.1292 REMARK 3 T13: -0.0669 T23: 0.0778 REMARK 3 L TENSOR REMARK 3 L11: 0.0457 L22: 0.0547 REMARK 3 L33: 0.0157 L12: -0.0382 REMARK 3 L13: -0.0137 L23: -0.0343 REMARK 3 S TENSOR REMARK 3 S11: -0.0143 S12: -0.1019 S13: 0.3285 REMARK 3 S21: 0.1948 S22: -0.1647 S23: 0.3033 REMARK 3 S31: -0.1103 S32: -0.1153 S33: 0.0000 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 105 THROUGH 174 ) REMARK 3 ORIGIN FOR THE GROUP (A): 96.0239 -7.1966 33.3198 REMARK 3 T TENSOR REMARK 3 T11: 0.1180 T22: 0.0788 REMARK 3 T33: 0.1115 T12: -0.0125 REMARK 3 T13: 0.0088 T23: 0.0057 REMARK 3 L TENSOR REMARK 3 L11: 0.1451 L22: 0.0595 REMARK 3 L33: 0.0186 L12: 0.0098 REMARK 3 L13: -0.0590 L23: -0.0051 REMARK 3 S TENSOR REMARK 3 S11: -0.0364 S12: 0.0171 S13: -0.0070 REMARK 3 S21: -0.0220 S22: -0.0290 S23: -0.0042 REMARK 3 S31: -0.0207 S32: 0.0227 S33: 0.0000 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 175 THROUGH 195 ) REMARK 3 ORIGIN FOR THE GROUP (A): 89.7821 -8.1745 0.8123 REMARK 3 T TENSOR REMARK 3 T11: 0.4250 T22: 0.5323 REMARK 3 T33: 0.3309 T12: 0.2037 REMARK 3 T13: -0.0149 T23: 0.0836 REMARK 3 L TENSOR REMARK 3 L11: -0.0029 L22: -0.0016 REMARK 3 L33: 0.0019 L12: -0.0057 REMARK 3 L13: -0.0012 L23: -0.0024 REMARK 3 S TENSOR REMARK 3 S11: -0.1178 S12: -0.0101 S13: -0.0850 REMARK 3 S21: 0.0207 S22: -0.0712 S23: -0.0836 REMARK 3 S31: 0.0124 S32: 0.0454 S33: 0.0000 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 196 THROUGH 281 ) REMARK 3 ORIGIN FOR THE GROUP (A): 93.6305 -21.7826 26.9243 REMARK 3 T TENSOR REMARK 3 T11: 0.0932 T22: -0.0090 REMARK 3 T33: 0.0467 T12: -0.1195 REMARK 3 T13: -0.0937 T23: -0.0874 REMARK 3 L TENSOR REMARK 3 L11: 0.0841 L22: 0.0223 REMARK 3 L33: 0.0215 L12: 0.1035 REMARK 3 L13: 0.0299 L23: 0.0861 REMARK 3 S TENSOR REMARK 3 S11: -0.0947 S12: -0.1304 S13: -0.2067 REMARK 3 S21: 0.0402 S22: 0.2655 S23: 0.2677 REMARK 3 S31: 0.1164 S32: 0.1269 S33: 0.0000 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 282 THROUGH 330 ) REMARK 3 ORIGIN FOR THE GROUP (A): 79.7402 -12.4252 38.1172 REMARK 3 T TENSOR REMARK 3 T11: 0.1598 T22: 0.2518 REMARK 3 T33: 0.2428 T12: 0.0202 REMARK 3 T13: -0.0067 T23: 0.0382 REMARK 3 L TENSOR REMARK 3 L11: 0.0217 L22: 0.0873 REMARK 3 L33: 0.0093 L12: -0.0185 REMARK 3 L13: 0.0423 L23: -0.0246 REMARK 3 S TENSOR REMARK 3 S11: -0.0085 S12: -0.0939 S13: -0.0141 REMARK 3 S21: -0.1403 S22: 0.0280 S23: 0.0404 REMARK 3 S31: -0.0629 S32: -0.2008 S33: -0.0000 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 31 THROUGH 173 ) REMARK 3 ORIGIN FOR THE GROUP (A): 122.3792 -8.4153 29.5939 REMARK 3 T TENSOR REMARK 3 T11: 0.0656 T22: 0.0651 REMARK 3 T33: 0.0850 T12: 0.0156 REMARK 3 T13: 0.0192 T23: -0.0263 REMARK 3 L TENSOR REMARK 3 L11: 0.1452 L22: 0.2312 REMARK 3 L33: 0.0634 L12: 0.2206 REMARK 3 L13: 0.0420 L23: -0.0597 REMARK 3 S TENSOR REMARK 3 S11: -0.0218 S12: -0.0027 S13: -0.0636 REMARK 3 S21: -0.0060 S22: 0.0271 S23: -0.0174 REMARK 3 S31: 0.0843 S32: 0.1310 S33: 0.0000 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 174 THROUGH 190 ) REMARK 3 ORIGIN FOR THE GROUP (A): 118.3155 -8.4996 1.7192 REMARK 3 T TENSOR REMARK 3 T11: 0.5600 T22: 0.3842 REMARK 3 T33: 0.2337 T12: -0.0358 REMARK 3 T13: -0.0434 T23: -0.0136 REMARK 3 L TENSOR REMARK 3 L11: 0.0104 L22: -0.0038 REMARK 3 L33: 0.0071 L12: 0.0098 REMARK 3 L13: 0.0150 L23: 0.0045 REMARK 3 S TENSOR REMARK 3 S11: -0.0039 S12: -0.0440 S13: 0.0730 REMARK 3 S21: -0.1300 S22: -0.0543 S23: 0.0740 REMARK 3 S31: 0.0356 S32: -0.0781 S33: 0.0000 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 191 THROUGH 211 ) REMARK 3 ORIGIN FOR THE GROUP (A): 108.0934 1.7657 14.6525 REMARK 3 T TENSOR REMARK 3 T11: 0.1204 T22: 0.1374 REMARK 3 T33: 0.0985 T12: -0.0006 REMARK 3 T13: -0.0178 T23: -0.0156 REMARK 3 L TENSOR REMARK 3 L11: -0.0037 L22: 0.0015 REMARK 3 L33: 0.0053 L12: 0.0158 REMARK 3 L13: 0.0024 L23: -0.0176 REMARK 3 S TENSOR REMARK 3 S11: 0.0590 S12: 0.1209 S13: -0.0376 REMARK 3 S21: -0.0446 S22: 0.0257 S23: -0.0502 REMARK 3 S31: 0.0425 S32: 0.0492 S33: -0.0000 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 212 THROUGH 281 ) REMARK 3 ORIGIN FOR THE GROUP (A): 120.4287 7.3654 30.4197 REMARK 3 T TENSOR REMARK 3 T11: 0.1222 T22: 0.0653 REMARK 3 T33: 0.0793 T12: 0.0110 REMARK 3 T13: 0.0246 T23: 0.0140 REMARK 3 L TENSOR REMARK 3 L11: 0.1195 L22: 0.1823 REMARK 3 L33: 0.0111 L12: 0.0804 REMARK 3 L13: -0.0835 L23: 0.0374 REMARK 3 S TENSOR REMARK 3 S11: 0.0238 S12: -0.0483 S13: 0.1099 REMARK 3 S21: -0.0910 S22: 0.0059 S23: -0.0587 REMARK 3 S31: -0.0447 S32: 0.0828 S33: -0.0000 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 282 THROUGH 331 ) REMARK 3 ORIGIN FOR THE GROUP (A): 131.5627 -4.9917 38.1479 REMARK 3 T TENSOR REMARK 3 T11: 0.1363 T22: 0.1857 REMARK 3 T33: 0.2234 T12: 0.0832 REMARK 3 T13: -0.0124 T23: -0.0173 REMARK 3 L TENSOR REMARK 3 L11: 0.0415 L22: 0.1209 REMARK 3 L33: 0.0066 L12: 0.0124 REMARK 3 L13: 0.0203 L23: 0.0431 REMARK 3 S TENSOR REMARK 3 S11: -0.0038 S12: 0.0284 S13: -0.1941 REMARK 3 S21: -0.0646 S22: 0.2627 S23: -0.0368 REMARK 3 S31: 0.0433 S32: -0.0049 S33: -0.0000 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 5O9H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JUN-17. REMARK 100 THE DEPOSITION ID IS D_1200005426. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 06-AUG-15 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.5 - 6.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I24 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.96861 REMARK 200 MONOCHROMATOR : ACCEL FIXED EXIT DOUBLE CRYSTAL REMARK 200 SI(111) REMARK 200 OPTICS : OXFORD DANFYSIK/SESO TWO STAGE REMARK 200 DEMAGNIFICATION USING TWO K-B REMARK 200 PAIRS OF BIMORPH TYPE MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26541 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700 REMARK 200 RESOLUTION RANGE LOW (A) : 34.600 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 200 DATA REDUNDANCY : 5.000 REMARK 200 R MERGE (I) : 0.19000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.83 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6 REMARK 200 DATA REDUNDANCY IN SHELL : 5.10 REMARK 200 R MERGE FOR SHELL (I) : 0.92300 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.700 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: 4DKL REMARK 200 REMARK 200 REMARK: ELONGATED PLATES REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 66.51 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.67 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRI-SODIUM CITRATE PH 5.5, 200MM REMARK 280 NA/K TARTRATE, 35-45% (V/V) POLYETHYLENE GLYCOL 400, LIPIDIC REMARK 280 CUBIC PHASE, TEMPERATURE 295.65K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 25.54800 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 19400 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 28810 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 56.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 30 REMARK 465 TYR A 192 REMARK 465 SER A 193 REMARK 465 GLY A 309 REMARK 465 ARG A 310 REMARK 465 GLU A 311 REMARK 465 ARG A 312 REMARK 465 GLU A 331 REMARK 465 SER A 332 REMARK 465 LYS A 333 REMARK 465 ALA A 334 REMARK 465 ALA A 335 REMARK 465 ALA A 336 REMARK 465 HIS A 337 REMARK 465 HIS A 338 REMARK 465 HIS A 339 REMARK 465 HIS A 340 REMARK 465 HIS A 341 REMARK 465 HIS A 342 REMARK 465 HIS A 343 REMARK 465 HIS A 344 REMARK 465 HIS A 345 REMARK 465 HIS A 346 REMARK 465 MET B 30 REMARK 465 GLY B 306 REMARK 465 PHE B 307 REMARK 465 GLN B 308 REMARK 465 GLY B 309 REMARK 465 ARG B 310 REMARK 465 GLU B 311 REMARK 465 SER B 332 REMARK 465 LYS B 333 REMARK 465 ALA B 334 REMARK 465 ALA B 335 REMARK 465 ALA B 336 REMARK 465 HIS B 337 REMARK 465 HIS B 338 REMARK 465 HIS B 339 REMARK 465 HIS B 340 REMARK 465 HIS B 341 REMARK 465 HIS B 342 REMARK 465 HIS B 343 REMARK 465 HIS B 344 REMARK 465 HIS B 345 REMARK 465 HIS B 346 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O ARG A 320 OG1 THR A 324 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 NH1 ARG B 236 O11 TLA A 403 2856 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ARG A 68 -53.29 -122.95 REMARK 500 GLN A 98 30.45 -96.83 REMARK 500 ILE A 111 -61.25 -92.03 REMARK 500 PHE A 211 -66.34 -145.61 REMARK 500 ARG B 68 -53.49 -135.01 REMARK 500 PHE B 211 -64.41 -143.34 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLA A 404 REMARK 610 OLA A 406 REMARK 610 OLA A 407 REMARK 610 OLA A 408 REMARK 610 OLA A 409 REMARK 610 OLA A 410 REMARK 610 OLA A 411 REMARK 610 OLA A 413 REMARK 610 OLA A 414 REMARK 610 OLA A 415 REMARK 610 OLA A 418 REMARK 610 OLA B 403 REMARK 610 OLA B 404 REMARK 610 OLA B 405 REMARK 610 OLA B 406 REMARK 610 OLA B 407 REMARK 610 OLA B 408 REMARK 610 OLA B 409 REMARK 610 OLA B 411 REMARK 610 OLA B 413 REMARK 610 OLA B 414 REMARK 610 OLA B 417 REMARK 610 OLA B 418 REMARK 610 OLA B 419 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 9P2 A 401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue TLA A 402 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue TLA A 403 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 404 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 405 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 406 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 407 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 408 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 409 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 411 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 412 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 413 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 416 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 417 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 9P2 B 401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue TLA B 402 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA B 403 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA B 404 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA B 405 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA B 406 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA B 407 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA B 408 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA B 409 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA B 410 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA B 412 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA B 413 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA B 414 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA B 415 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA B 416 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA B 417 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA B 419 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CIT B 420 DBREF 5O9H A 31 333 UNP P21730 C5AR1_HUMAN 31 333 DBREF 5O9H B 31 333 UNP P21730 C5AR1_HUMAN 31 333 SEQADV 5O9H MET A 30 UNP P21730 INITIATING METHIONINE SEQADV 5O9H ALA A 85 UNP P21730 SER 85 ENGINEERED MUTATION SEQADV 5O9H ALA A 91 UNP P21730 ILE 91 ENGINEERED MUTATION SEQADV 5O9H ALA A 142 UNP P21730 ILE 142 ENGINEERED MUTATION SEQADV 5O9H ARG A 146 UNP P21730 ASN 146 ENGINEERED MUTATION SEQADV 5O9H LEU A 156 UNP P21730 ALA 156 ENGINEERED MUTATION SEQADV 5O9H ALA A 172 UNP P21730 PHE 172 ENGINEERED MUTATION SEQADV 5O9H ALA A 232 UNP P21730 ARG 232 ENGINEERED MUTATION SEQADV 5O9H GLU A 234 UNP P21730 ALA 234 ENGINEERED MUTATION SEQADV 5O9H GLU A 311 UNP P21730 LEU 311 ENGINEERED MUTATION SEQADV 5O9H GLU A 317 UNP P21730 SER 317 ENGINEERED MUTATION SEQADV 5O9H GLU A 321 UNP P21730 ASN 321 ENGINEERED MUTATION SEQADV 5O9H ALA A 334 UNP P21730 EXPRESSION TAG SEQADV 5O9H ALA A 335 UNP P21730 EXPRESSION TAG SEQADV 5O9H ALA A 336 UNP P21730 EXPRESSION TAG SEQADV 5O9H HIS A 337 UNP P21730 EXPRESSION TAG SEQADV 5O9H HIS A 338 UNP P21730 EXPRESSION TAG SEQADV 5O9H HIS A 339 UNP P21730 EXPRESSION TAG SEQADV 5O9H HIS A 340 UNP P21730 EXPRESSION TAG SEQADV 5O9H HIS A 341 UNP P21730 EXPRESSION TAG SEQADV 5O9H HIS A 342 UNP P21730 EXPRESSION TAG SEQADV 5O9H HIS A 343 UNP P21730 EXPRESSION TAG SEQADV 5O9H HIS A 344 UNP P21730 EXPRESSION TAG SEQADV 5O9H HIS A 345 UNP P21730 EXPRESSION TAG SEQADV 5O9H HIS A 346 UNP P21730 EXPRESSION TAG SEQADV 5O9H MET B 30 UNP P21730 INITIATING METHIONINE SEQADV 5O9H ALA B 85 UNP P21730 SER 85 ENGINEERED MUTATION SEQADV 5O9H ALA B 91 UNP P21730 ILE 91 ENGINEERED MUTATION SEQADV 5O9H ALA B 142 UNP P21730 ILE 142 ENGINEERED MUTATION SEQADV 5O9H ARG B 146 UNP P21730 ASN 146 ENGINEERED MUTATION SEQADV 5O9H LEU B 156 UNP P21730 ALA 156 ENGINEERED MUTATION SEQADV 5O9H ALA B 172 UNP P21730 PHE 172 ENGINEERED MUTATION SEQADV 5O9H ALA B 232 UNP P21730 ARG 232 ENGINEERED MUTATION SEQADV 5O9H GLU B 234 UNP P21730 ALA 234 ENGINEERED MUTATION SEQADV 5O9H GLU B 311 UNP P21730 LEU 311 ENGINEERED MUTATION SEQADV 5O9H GLU B 317 UNP P21730 SER 317 ENGINEERED MUTATION SEQADV 5O9H GLU B 321 UNP P21730 ASN 321 ENGINEERED MUTATION SEQADV 5O9H ALA B 334 UNP P21730 EXPRESSION TAG SEQADV 5O9H ALA B 335 UNP P21730 EXPRESSION TAG SEQADV 5O9H ALA B 336 UNP P21730 EXPRESSION TAG SEQADV 5O9H HIS B 337 UNP P21730 EXPRESSION TAG SEQADV 5O9H HIS B 338 UNP P21730 EXPRESSION TAG SEQADV 5O9H HIS B 339 UNP P21730 EXPRESSION TAG SEQADV 5O9H HIS B 340 UNP P21730 EXPRESSION TAG SEQADV 5O9H HIS B 341 UNP P21730 EXPRESSION TAG SEQADV 5O9H HIS B 342 UNP P21730 EXPRESSION TAG SEQADV 5O9H HIS B 343 UNP P21730 EXPRESSION TAG SEQADV 5O9H HIS B 344 UNP P21730 EXPRESSION TAG SEQADV 5O9H HIS B 345 UNP P21730 EXPRESSION TAG SEQADV 5O9H HIS B 346 UNP P21730 EXPRESSION TAG SEQRES 1 A 317 MET ASN THR LEU ARG VAL PRO ASP ILE LEU ALA LEU VAL SEQRES 2 A 317 ILE PHE ALA VAL VAL PHE LEU VAL GLY VAL LEU GLY ASN SEQRES 3 A 317 ALA LEU VAL VAL TRP VAL THR ALA PHE GLU ALA LYS ARG SEQRES 4 A 317 THR ILE ASN ALA ILE TRP PHE LEU ASN LEU ALA VAL ALA SEQRES 5 A 317 ASP PHE LEU ALA CYS LEU ALA LEU PRO ALA LEU PHE THR SEQRES 6 A 317 SER ILE VAL GLN HIS HIS HIS TRP PRO PHE GLY GLY ALA SEQRES 7 A 317 ALA CYS SER ILE LEU PRO SER LEU ILE LEU LEU ASN MET SEQRES 8 A 317 TYR ALA SER ILE LEU LEU LEU ALA THR ILE SER ALA ASP SEQRES 9 A 317 ARG PHE LEU LEU VAL PHE LYS PRO ALA TRP CYS GLN ARG SEQRES 10 A 317 PHE ARG GLY ALA GLY LEU ALA TRP ILE LEU CYS ALA VAL SEQRES 11 A 317 ALA TRP GLY LEU ALA LEU LEU LEU THR ILE PRO SER ALA SEQRES 12 A 317 LEU TYR ARG VAL VAL ARG GLU GLU TYR PHE PRO PRO LYS SEQRES 13 A 317 VAL LEU CYS GLY VAL ASP TYR SER HIS ASP LYS ARG ARG SEQRES 14 A 317 GLU ARG ALA VAL ALA ILE VAL ARG LEU VAL LEU GLY PHE SEQRES 15 A 317 LEU TRP PRO LEU LEU THR LEU THR ILE CYS TYR THR PHE SEQRES 16 A 317 ILE LEU LEU ARG THR TRP SER ALA ARG GLU THR ARG SER SEQRES 17 A 317 THR LYS THR LEU LYS VAL VAL VAL ALA VAL VAL ALA SER SEQRES 18 A 317 PHE PHE ILE PHE TRP LEU PRO TYR GLN VAL THR GLY ILE SEQRES 19 A 317 MET MET SER PHE LEU GLU PRO SER SER PRO THR PHE LEU SEQRES 20 A 317 LEU LEU LYS LYS LEU ASP SER LEU CYS VAL SER PHE ALA SEQRES 21 A 317 TYR ILE ASN CYS CYS ILE ASN PRO ILE ILE TYR VAL VAL SEQRES 22 A 317 ALA GLY GLN GLY PHE GLN GLY ARG GLU ARG LYS SER LEU SEQRES 23 A 317 PRO GLU LEU LEU ARG GLU VAL LEU THR GLU GLU SER VAL SEQRES 24 A 317 VAL ARG GLU SER LYS ALA ALA ALA HIS HIS HIS HIS HIS SEQRES 25 A 317 HIS HIS HIS HIS HIS SEQRES 1 B 317 MET ASN THR LEU ARG VAL PRO ASP ILE LEU ALA LEU VAL SEQRES 2 B 317 ILE PHE ALA VAL VAL PHE LEU VAL GLY VAL LEU GLY ASN SEQRES 3 B 317 ALA LEU VAL VAL TRP VAL THR ALA PHE GLU ALA LYS ARG SEQRES 4 B 317 THR ILE ASN ALA ILE TRP PHE LEU ASN LEU ALA VAL ALA SEQRES 5 B 317 ASP PHE LEU ALA CYS LEU ALA LEU PRO ALA LEU PHE THR SEQRES 6 B 317 SER ILE VAL GLN HIS HIS HIS TRP PRO PHE GLY GLY ALA SEQRES 7 B 317 ALA CYS SER ILE LEU PRO SER LEU ILE LEU LEU ASN MET SEQRES 8 B 317 TYR ALA SER ILE LEU LEU LEU ALA THR ILE SER ALA ASP SEQRES 9 B 317 ARG PHE LEU LEU VAL PHE LYS PRO ALA TRP CYS GLN ARG SEQRES 10 B 317 PHE ARG GLY ALA GLY LEU ALA TRP ILE LEU CYS ALA VAL SEQRES 11 B 317 ALA TRP GLY LEU ALA LEU LEU LEU THR ILE PRO SER ALA SEQRES 12 B 317 LEU TYR ARG VAL VAL ARG GLU GLU TYR PHE PRO PRO LYS SEQRES 13 B 317 VAL LEU CYS GLY VAL ASP TYR SER HIS ASP LYS ARG ARG SEQRES 14 B 317 GLU ARG ALA VAL ALA ILE VAL ARG LEU VAL LEU GLY PHE SEQRES 15 B 317 LEU TRP PRO LEU LEU THR LEU THR ILE CYS TYR THR PHE SEQRES 16 B 317 ILE LEU LEU ARG THR TRP SER ALA ARG GLU THR ARG SER SEQRES 17 B 317 THR LYS THR LEU LYS VAL VAL VAL ALA VAL VAL ALA SER SEQRES 18 B 317 PHE PHE ILE PHE TRP LEU PRO TYR GLN VAL THR GLY ILE SEQRES 19 B 317 MET MET SER PHE LEU GLU PRO SER SER PRO THR PHE LEU SEQRES 20 B 317 LEU LEU LYS LYS LEU ASP SER LEU CYS VAL SER PHE ALA SEQRES 21 B 317 TYR ILE ASN CYS CYS ILE ASN PRO ILE ILE TYR VAL VAL SEQRES 22 B 317 ALA GLY GLN GLY PHE GLN GLY ARG GLU ARG LYS SER LEU SEQRES 23 B 317 PRO GLU LEU LEU ARG GLU VAL LEU THR GLU GLU SER VAL SEQRES 24 B 317 VAL ARG GLU SER LYS ALA ALA ALA HIS HIS HIS HIS HIS SEQRES 25 B 317 HIS HIS HIS HIS HIS HET 9P2 A 401 43 HET TLA A 402 10 HET TLA A 403 10 HET OLA A 404 17 HET OLA A 405 20 HET OLA A 406 15 HET OLA A 407 14 HET OLA A 408 16 HET OLA A 409 12 HET OLA A 410 10 HET OLA A 411 18 HET OLA A 412 20 HET OLA A 413 13 HET OLA A 414 16 HET OLA A 415 15 HET OLA A 416 20 HET OLA A 417 20 HET OLA A 418 11 HET 9P2 B 401 43 HET TLA B 402 10 HET OLA B 403 13 HET OLA B 404 10 HET OLA B 405 15 HET OLA B 406 14 HET OLA B 407 13 HET OLA B 408 7 HET OLA B 409 16 HET OLA B 410 20 HET OLA B 411 14 HET OLA B 412 20 HET OLA B 413 14 HET OLA B 414 9 HET OLA B 415 20 HET OLA B 416 20 HET OLA B 417 16 HET OLA B 418 15 HET OLA B 419 14 HET CIT B 420 13 HETNAM 9P2 1-(1,3-BENZODIOXOL-5-YL)-~{N}-(1,3-BENZODIOXOL-5- HETNAM 2 9P2 YLMETHYL)-~{N}-[(3-BUTYL-2,5-DIPHENYL-IMIDAZOL-4-YL) HETNAM 3 9P2 METHYL]METHANAMINE HETNAM TLA L(+)-TARTARIC ACID HETNAM OLA OLEIC ACID HETNAM CIT CITRIC ACID FORMUL 3 9P2 2(C36 H35 N3 O4) FORMUL 4 TLA 3(C4 H6 O6) FORMUL 6 OLA 32(C18 H34 O2) FORMUL 40 CIT C6 H8 O7 FORMUL 41 HOH *71(H2 O) HELIX 1 AA1 ARG A 34 PHE A 64 1 31 HELIX 2 AA2 THR A 69 ALA A 88 1 20 HELIX 3 AA3 ALA A 88 GLN A 98 1 11 HELIX 4 AA4 PHE A 104 LEU A 112 1 9 HELIX 5 AA5 SER A 114 LYS A 140 1 27 HELIX 6 AA6 LYS A 140 ARG A 148 1 9 HELIX 7 AA7 GLY A 149 ARG A 175 1 27 HELIX 8 AA8 ASP A 195 PHE A 211 1 17 HELIX 9 AA9 PHE A 211 ALA A 232 1 22 HELIX 10 AB1 THR A 238 PHE A 267 1 30 HELIX 11 AB2 SER A 272 LEU A 281 1 10 HELIX 12 AB3 LEU A 281 ILE A 291 1 11 HELIX 13 AB4 CYS A 294 PHE A 307 1 14 HELIX 14 AB5 SER A 314 THR A 324 1 11 HELIX 15 AB6 ARG B 34 PHE B 64 1 31 HELIX 16 AB7 THR B 69 LEU B 87 1 19 HELIX 17 AB8 ALA B 88 GLN B 98 1 11 HELIX 18 AB9 PHE B 104 LEU B 112 1 9 HELIX 19 AC1 SER B 114 LYS B 140 1 27 HELIX 20 AC2 LYS B 140 ARG B 148 1 9 HELIX 21 AC3 GLY B 149 TYR B 174 1 26 HELIX 22 AC4 ARG B 197 PHE B 211 1 15 HELIX 23 AC5 PHE B 211 ALA B 232 1 22 HELIX 24 AC6 THR B 238 MET B 265 1 28 HELIX 25 AC7 SER B 272 LEU B 281 1 10 HELIX 26 AC8 LEU B 281 TYR B 290 1 10 HELIX 27 AC9 ILE B 291 GLN B 305 1 15 HELIX 28 AD1 SER B 314 THR B 324 1 11 SHEET 1 AA1 2 VAL A 176 GLU A 180 0 SHEET 2 AA1 2 LYS A 185 GLY A 189 -1 O LEU A 187 N ARG A 178 SHEET 1 AA2 2 ARG B 175 GLU B 180 0 SHEET 2 AA2 2 LYS B 185 VAL B 190 -1 O GLY B 189 N VAL B 176 SSBOND 1 CYS A 109 CYS A 188 1555 1555 2.03 SSBOND 2 CYS B 109 CYS B 188 1555 1555 2.03 CISPEP 1 PHE A 182 PRO A 183 0 -0.91 CISPEP 2 PHE B 182 PRO B 183 0 -2.48 SITE 1 AC1 14 ILE A 124 LEU A 125 ALA A 128 THR A 129 SITE 2 AC1 14 LEU A 156 VAL A 159 LEU A 163 LEU A 209 SITE 3 AC1 14 TRP A 213 PRO A 214 THR A 217 OLA A 406 SITE 4 AC1 14 ALA B 158 GLY B 162 SITE 1 AC2 9 THR A 69 ILE A 70 ASN A 71 ARG A 148 SITE 2 AC2 9 GLU A 325 GLU A 326 SER A 327 VAL A 328 SITE 3 AC2 9 ARG A 330 SITE 1 AC3 6 THR A 229 ALA A 232 ARG A 233 THR A 235 SITE 2 AC3 6 SER A 237 HOH A 509 SITE 1 AC4 2 ALA A 132 TRP A 143 SITE 1 AC5 4 PHE A 135 LYS A 140 OLA A 406 ILE B 155 SITE 1 AC6 4 LEU A 218 9P2 A 401 OLA A 405 OLA B 405 SITE 1 AC7 1 ALA A 63 SITE 1 AC8 2 THR A 94 GLN A 98 SITE 1 AC9 1 VAL A 42 SITE 1 AD1 7 LEU A 216 ILE A 220 THR A 223 PHE A 224 SITE 2 AD1 7 LEU A 227 ARG A 228 SER A 231 SITE 1 AD2 4 THR A 223 LEU A 226 TRP A 230 OLA A 417 SITE 1 AD3 3 LYS A 242 ILE A 253 ILE A 295 SITE 1 AD4 4 ALA A 158 GLY A 162 9P2 B 401 OLA B 406 SITE 1 AD5 3 VAL A 245 PHE A 252 OLA A 412 SITE 1 AD6 12 ILE A 155 OLA A 416 LEU B 125 ALA B 128 SITE 2 AD6 12 THR B 129 LEU B 156 LEU B 163 LEU B 209 SITE 3 AD6 12 TRP B 213 PRO B 214 THR B 217 OLA B 404 SITE 1 AD7 7 ARG B 68 THR B 69 ILE B 70 ARG B 148 SITE 2 AD7 7 GLU B 326 SER B 327 VAL B 328 SITE 1 AD8 2 TRP B 143 OLA B 404 SITE 1 AD9 4 TRP B 213 9P2 B 401 OLA B 403 OLA B 406 SITE 1 AE1 3 OLA A 406 GLY B 151 ILE B 155 SITE 1 AE2 4 OLA A 416 LEU B 209 TRP B 213 OLA B 404 SITE 1 AE3 4 TRP B 74 ALA B 132 LEU B 156 OLA B 408 SITE 1 AE4 6 TRP A 143 PHE A 147 LEU B 136 TRP B 143 SITE 2 AE4 6 ARG B 148 OLA B 407 SITE 1 AE5 1 ALA B 172 SITE 1 AE6 3 TRP B 154 TRP B 161 OLA B 417 SITE 1 AE7 5 LEU B 216 THR B 219 PHE B 224 LEU B 227 SITE 2 AE7 5 OLA B 414 SITE 1 AE8 1 TRP B 230 SITE 1 AE9 3 LEU B 215 ILE B 263 OLA B 412 SITE 1 AF1 3 VAL B 245 ALA B 246 OLA B 416 SITE 1 AF2 4 LYS B 242 VAL B 302 ALA B 303 OLA B 415 SITE 1 AF3 1 OLA B 410 SITE 1 AF4 6 LEU A 166 LEU A 167 LEU B 166 PRO B 170 SITE 2 AF4 6 TYR B 174 TYR B 192 SITE 1 AF5 1 TYR B 181 CRYST1 83.093 51.096 118.936 90.00 106.73 90.00 P 1 21 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.012035 0.000000 0.003616 0.00000 SCALE2 0.000000 0.019571 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008779 0.00000 ATOM 1 N ASN A 31 73.002 -15.622 -0.965 1.00 83.50 N ANISOU 1 N ASN A 31 9016 13048 9664 -810 -600 704 N ATOM 2 CA ASN A 31 71.658 -15.204 -0.585 1.00 90.82 C ANISOU 2 CA ASN A 31 9903 13986 10619 -788 -607 773 C ATOM 3 C ASN A 31 71.404 -15.436 0.902 1.00109.37 C ANISOU 3 C ASN A 31 12248 16309 12998 -737 -597 756 C ATOM 4 O ASN A 31 71.779 -14.617 1.736 1.00118.14 O ANISOU 4 O ASN A 31 13355 17400 14134 -699 -595 756 O ATOM 5 CB ASN A 31 70.611 -15.946 -1.418 1.00114.55 C ANISOU 5 CB ASN A 31 12895 17021 13610 -822 -612 807 C ATOM 6 CG ASN A 31 69.280 -15.220 -1.465 1.00118.29 C ANISOU 6 CG ASN A 31 13325 17513 14107 -812 -623 894 C ATOM 7 OD1 ASN A 31 68.576 -15.123 -0.460 1.00120.00 O ANISOU 7 OD1 ASN A 31 13522 17718 14355 -772 -619 916 O ATOM 8 ND2 ASN A 31 68.925 -14.711 -2.640 1.00112.30 N ANISOU 8 ND2 ASN A 31 12551 16783 13335 -847 -635 944 N ATOM 9 N THR A 32 70.755 -16.548 1.230 1.00104.25 N ANISOU 9 N THR A 32 11600 15661 12350 -735 -590 743 N ATOM 10 CA THR A 32 70.500 -16.894 2.625 1.00 95.70 C ANISOU 10 CA THR A 32 10514 14553 11294 -688 -580 724 C ATOM 11 C THR A 32 71.799 -17.247 3.351 1.00 90.22 C ANISOU 11 C THR A 32 9856 13828 10594 -671 -567 642 C ATOM 12 O THR A 32 72.718 -17.815 2.761 1.00 79.00 O ANISOU 12 O THR A 32 8469 12406 9144 -702 -563 589 O ATOM 13 CB THR A 32 69.507 -18.068 2.750 1.00 83.17 C ANISOU 13 CB THR A 32 8919 12974 9707 -693 -575 727 C ATOM 14 OG1 THR A 32 70.100 -19.263 2.227 1.00 99.36 O ANISOU 14 OG1 THR A 32 11003 15025 11724 -728 -569 666 O ATOM 15 CG2 THR A 32 68.222 -17.767 1.992 1.00 92.43 C ANISOU 15 CG2 THR A 32 10057 14178 10884 -712 -588 807 C ATOM 16 N LEU A 33 71.873 -16.893 4.630 1.00 77.72 N ANISOU 16 N LEU A 33 8269 12221 9042 -620 -560 633 N ATOM 17 CA LEU A 33 73.039 -17.200 5.452 1.00 60.73 C ANISOU 17 CA LEU A 33 6151 10038 6887 -599 -547 557 C ATOM 18 C LEU A 33 73.117 -18.679 5.825 1.00 61.32 C ANISOU 18 C LEU A 33 6250 10102 6949 -603 -534 498 C ATOM 19 O LEU A 33 72.100 -19.364 5.905 1.00 68.06 O ANISOU 19 O LEU A 33 7087 10966 7808 -604 -533 520 O ATOM 20 CB LEU A 33 73.026 -16.348 6.721 1.00 51.09 C ANISOU 20 CB LEU A 33 4914 8794 5702 -541 -543 569 C ATOM 21 CG LEU A 33 73.183 -14.844 6.498 1.00 66.23 C ANISOU 21 CG LEU A 33 6814 10715 7634 -530 -554 617 C ATOM 22 CD1 LEU A 33 72.881 -14.072 7.771 1.00 61.83 C ANISOU 22 CD1 LEU A 33 6236 10136 7119 -468 -548 641 C ATOM 23 CD2 LEU A 33 74.586 -14.533 6.001 1.00 65.95 C ANISOU 23 CD2 LEU A 33 6810 10673 7574 -552 -556 570 C ATOM 24 N ARG A 34 74.337 -19.156 6.049 1.00 65.07 N ANISOU 24 N ARG A 34 6762 10554 7406 -606 -523 424 N ATOM 25 CA ARG A 34 74.586 -20.515 6.524 1.00 55.82 C ANISOU 25 CA ARG A 34 5618 9367 6224 -606 -507 362 C ATOM 26 C ARG A 34 74.205 -20.658 7.993 1.00 59.69 C ANISOU 26 C ARG A 34 6100 9836 6745 -553 -498 352 C ATOM 27 O ARG A 34 74.055 -19.661 8.700 1.00 66.12 O ANISOU 27 O ARG A 34 6894 10643 7587 -514 -501 380 O ATOM 28 CB ARG A 34 76.053 -20.895 6.324 1.00 57.28 C ANISOU 28 CB ARG A 34 5848 9531 6384 -622 -496 288 C ATOM 29 CG ARG A 34 76.410 -21.296 4.903 1.00 54.84 C ANISOU 29 CG ARG A 34 5555 9238 6042 -675 -499 283 C ATOM 30 CD ARG A 34 77.911 -21.263 4.677 1.00 60.42 C ANISOU 30 CD ARG A 34 6301 9923 6731 -686 -489 224 C ATOM 31 NE ARG A 34 78.278 -21.850 3.393 1.00 89.03 N ANISOU 31 NE ARG A 34 9943 13559 10324 -734 -487 212 N ATOM 32 CZ ARG A 34 78.160 -21.228 2.225 1.00107.87 C ANISOU 32 CZ ARG A 34 12317 15971 12697 -766 -501 254 C ATOM 33 NH1 ARG A 34 77.673 -19.995 2.170 1.00106.88 N ANISOU 33 NH1 ARG A 34 12161 15862 12587 -756 -517 313 N ATOM 34 NH2 ARG A 34 78.524 -21.843 1.108 1.00109.02 N ANISOU 34 NH2 ARG A 34 12482 16126 12817 -806 -497 239 N ATOM 35 N VAL A 35 74.022 -21.898 8.436 1.00 62.13 N ANISOU 35 N VAL A 35 6422 10135 7049 -551 -486 313 N ATOM 36 CA VAL A 35 73.675 -22.177 9.828 1.00 66.08 C ANISOU 36 CA VAL A 35 6917 10615 7577 -502 -475 298 C ATOM 37 C VAL A 35 74.637 -21.527 10.846 1.00 50.28 C ANISOU 37 C VAL A 35 4930 8585 5589 -460 -466 260 C ATOM 38 O VAL A 35 74.172 -20.842 11.773 1.00 66.50 O ANISOU 38 O VAL A 35 6960 10631 7676 -413 -466 289 O ATOM 39 CB VAL A 35 73.627 -23.713 10.090 1.00 60.13 C ANISOU 39 CB VAL A 35 6186 9852 6810 -511 -461 247 C ATOM 40 CG1 VAL A 35 73.307 -24.010 11.545 1.00 65.77 C ANISOU 40 CG1 VAL A 35 6894 10543 7551 -459 -448 229 C ATOM 41 CG2 VAL A 35 72.627 -24.387 9.162 1.00 70.01 C ANISOU 41 CG2 VAL A 35 7422 11131 8049 -548 -469 284 C ATOM 42 N PRO A 36 75.966 -21.711 10.681 1.00 59.79 N ANISOU 42 N PRO A 36 6174 9774 6772 -475 -459 197 N ATOM 43 CA PRO A 36 76.864 -21.089 11.662 1.00 65.70 C ANISOU 43 CA PRO A 36 6936 10495 7533 -435 -451 161 C ATOM 44 C PRO A 36 76.734 -19.568 11.767 1.00 55.96 C ANISOU 44 C PRO A 36 5674 9266 6321 -411 -463 215 C ATOM 45 O PRO A 36 76.887 -19.024 12.857 1.00 58.34 O ANISOU 45 O PRO A 36 5970 9548 6647 -361 -458 208 O ATOM 46 CB PRO A 36 78.261 -21.457 11.148 1.00 74.99 C ANISOU 46 CB PRO A 36 8157 11657 8679 -465 -443 96 C ATOM 47 CG PRO A 36 78.061 -22.652 10.297 1.00 69.97 C ANISOU 47 CG PRO A 36 7535 11032 8018 -509 -438 83 C ATOM 48 CD PRO A 36 76.733 -22.451 9.653 1.00 58.71 C ANISOU 48 CD PRO A 36 6070 9639 6599 -525 -455 157 C ATOM 49 N ASP A 37 76.441 -18.898 10.653 1.00 48.75 N ANISOU 49 N ASP A 37 4743 8378 5400 -443 -480 268 N ATOM 50 CA ASP A 37 76.344 -17.439 10.649 1.00 57.77 C ANISOU 50 CA ASP A 37 5860 9526 6564 -422 -491 321 C ATOM 51 C ASP A 37 75.094 -16.942 11.378 1.00 51.59 C ANISOU 51 C ASP A 37 5036 8746 5821 -379 -493 385 C ATOM 52 O ASP A 37 75.140 -15.939 12.096 1.00 45.38 O ANISOU 52 O ASP A 37 4235 7945 5062 -335 -492 407 O ATOM 53 CB ASP A 37 76.371 -16.908 9.212 1.00 56.32 C ANISOU 53 CB ASP A 37 5671 9369 6360 -471 -507 360 C ATOM 54 CG ASP A 37 77.673 -17.231 8.496 1.00 73.83 C ANISOU 54 CG ASP A 37 7929 11579 8543 -508 -504 301 C ATOM 55 OD1 ASP A 37 78.175 -18.366 8.644 1.00 77.02 O ANISOU 55 OD1 ASP A 37 8364 11969 8929 -519 -490 239 O ATOM 56 OD2 ASP A 37 78.198 -16.346 7.788 1.00 78.33 O ANISOU 56 OD2 ASP A 37 8500 12156 9105 -526 -514 318 O ATOM 57 N ILE A 38 73.984 -17.653 11.206 1.00 52.79 N ANISOU 57 N ILE A 38 5170 8912 5976 -389 -493 415 N ATOM 58 CA ILE A 38 72.766 -17.330 11.940 1.00 54.15 C ANISOU 58 CA ILE A 38 5305 9083 6186 -347 -491 473 C ATOM 59 C ILE A 38 72.979 -17.572 13.431 1.00 54.42 C ANISOU 59 C ILE A 38 5347 9085 6244 -290 -473 433 C ATOM 60 O ILE A 38 72.565 -16.762 14.278 1.00 44.63 O ANISOU 60 O ILE A 38 4086 7830 5042 -237 -468 469 O ATOM 61 CB ILE A 38 71.569 -18.172 11.450 1.00 60.87 C ANISOU 61 CB ILE A 38 6139 9955 7033 -372 -494 507 C ATOM 62 CG1 ILE A 38 71.489 -18.148 9.921 1.00 67.20 C ANISOU 62 CG1 ILE A 38 6940 10789 7805 -432 -509 533 C ATOM 63 CG2 ILE A 38 70.271 -17.683 12.079 1.00 60.45 C ANISOU 63 CG2 ILE A 38 6046 9900 7022 -329 -492 577 C ATOM 64 CD1 ILE A 38 70.438 -19.076 9.345 1.00 71.54 C ANISOU 64 CD1 ILE A 38 7478 11360 8346 -462 -512 558 C ATOM 65 N LEU A 39 73.666 -18.670 13.746 1.00 52.49 N ANISOU 65 N LEU A 39 5138 8829 5979 -299 -462 357 N ATOM 66 CA LEU A 39 73.960 -18.974 15.141 1.00 49.30 C ANISOU 66 CA LEU A 39 4744 8393 5593 -247 -444 311 C ATOM 67 C LEU A 39 74.821 -17.873 15.747 1.00 53.46 C ANISOU 67 C LEU A 39 5278 8901 6135 -209 -442 299 C ATOM 68 O LEU A 39 74.621 -17.462 16.896 1.00 48.07 O ANISOU 68 O LEU A 39 4583 8195 5485 -149 -430 306 O ATOM 69 CB LEU A 39 74.672 -20.321 15.265 1.00 52.42 C ANISOU 69 CB LEU A 39 5179 8778 5959 -269 -433 229 C ATOM 70 CG LEU A 39 73.832 -21.579 15.058 1.00 49.16 C ANISOU 70 CG LEU A 39 4764 8377 5539 -291 -430 229 C ATOM 71 CD1 LEU A 39 74.724 -22.808 15.062 1.00 66.85 C ANISOU 71 CD1 LEU A 39 7048 10605 7749 -315 -418 147 C ATOM 72 CD2 LEU A 39 72.773 -21.681 16.143 1.00 60.97 C ANISOU 72 CD2 LEU A 39 6233 9862 7072 -240 -421 259 C ATOM 73 N ALA A 40 75.761 -17.378 14.949 1.00 40.32 N ANISOU 73 N ALA A 40 3631 7244 4446 -242 -452 284 N ATOM 74 CA ALA A 40 76.632 -16.301 15.386 1.00 39.29 C ANISOU 74 CA ALA A 40 3507 7096 4326 -212 -452 274 C ATOM 75 C ALA A 40 75.846 -15.016 15.604 1.00 52.30 C ANISOU 75 C ALA A 40 5115 8745 6011 -173 -458 354 C ATOM 76 O ALA A 40 76.140 -14.258 16.523 1.00 54.36 O ANISOU 76 O ALA A 40 5374 8983 6298 -120 -450 354 O ATOM 77 CB ALA A 40 77.747 -16.079 14.376 1.00 45.25 C ANISOU 77 CB ALA A 40 4289 7858 5046 -260 -462 244 C ATOM 78 N LEU A 41 74.831 -14.783 14.775 1.00 61.21 N ANISOU 78 N LEU A 41 6215 9899 7144 -198 -470 424 N ATOM 79 CA LEU A 41 74.005 -13.591 14.938 1.00 45.55 C ANISOU 79 CA LEU A 41 4194 7914 5198 -163 -473 506 C ATOM 80 C LEU A 41 73.231 -13.652 16.252 1.00 51.66 C ANISOU 80 C LEU A 41 4951 8662 6013 -97 -455 523 C ATOM 81 O LEU A 41 73.168 -12.664 17.004 1.00 53.05 O ANISOU 81 O LEU A 41 5116 8816 6225 -41 -447 552 O ATOM 82 CB LEU A 41 73.040 -13.435 13.762 1.00 46.60 C ANISOU 82 CB LEU A 41 4301 8079 5325 -205 -488 575 C ATOM 83 CG LEU A 41 73.642 -13.020 12.419 1.00 54.20 C ANISOU 83 CG LEU A 41 5272 9066 6255 -262 -506 580 C ATOM 84 CD1 LEU A 41 72.594 -13.097 11.321 1.00 50.17 C ANISOU 84 CD1 LEU A 41 4737 8588 5738 -304 -518 642 C ATOM 85 CD2 LEU A 41 74.224 -11.618 12.504 1.00 52.85 C ANISOU 85 CD2 LEU A 41 5096 8884 6099 -239 -511 602 C ATOM 86 N VAL A 42 72.681 -14.828 16.548 1.00 45.82 N ANISOU 86 N VAL A 42 4215 7925 5271 -101 -446 502 N ATOM 87 CA VAL A 42 71.920 -14.995 17.784 1.00 51.90 C ANISOU 87 CA VAL A 42 4972 8668 6080 -39 -427 515 C ATOM 88 C VAL A 42 72.816 -14.825 19.013 1.00 51.82 C ANISOU 88 C VAL A 42 4984 8622 6084 16 -409 459 C ATOM 89 O VAL A 42 72.472 -14.098 19.966 1.00 46.51 O ANISOU 89 O VAL A 42 4299 7921 5452 81 -394 490 O ATOM 90 CB VAL A 42 71.235 -16.376 17.838 1.00 51.90 C ANISOU 90 CB VAL A 42 4974 8677 6071 -58 -422 497 C ATOM 91 CG1 VAL A 42 70.514 -16.563 19.163 1.00 43.26 C ANISOU 91 CG1 VAL A 42 3869 7552 5016 7 -400 507 C ATOM 92 CG2 VAL A 42 70.269 -16.538 16.671 1.00 51.34 C ANISOU 92 CG2 VAL A 42 4880 8640 5988 -108 -438 555 C ATOM 93 N ILE A 43 73.983 -15.468 18.976 1.00 54.24 N ANISOU 93 N ILE A 43 5326 8928 6356 -9 -409 378 N ATOM 94 CA ILE A 43 74.916 -15.372 20.092 1.00 42.00 C ANISOU 94 CA ILE A 43 3799 7345 4814 40 -393 318 C ATOM 95 C ILE A 43 75.394 -13.936 20.283 1.00 38.28 C ANISOU 95 C ILE A 43 3323 6860 4363 75 -395 345 C ATOM 96 O ILE A 43 75.494 -13.454 21.410 1.00 31.21 O ANISOU 96 O ILE A 43 2429 5929 3499 142 -377 340 O ATOM 97 CB ILE A 43 76.143 -16.291 19.893 1.00 38.39 C ANISOU 97 CB ILE A 43 3383 6889 4312 0 -393 226 C ATOM 98 CG1 ILE A 43 75.716 -17.757 19.850 1.00 40.29 C ANISOU 98 CG1 ILE A 43 3635 7138 4537 -27 -387 195 C ATOM 99 CG2 ILE A 43 77.155 -16.090 21.009 1.00 41.96 C ANISOU 99 CG2 ILE A 43 3862 7308 4772 50 -377 163 C ATOM 100 CD1 ILE A 43 76.869 -18.723 19.703 1.00 27.62 C ANISOU 100 CD1 ILE A 43 2073 5528 2891 -63 -384 105 C ATOM 101 N PHE A 44 75.645 -13.241 19.178 1.00 35.57 N ANISOU 101 N PHE A 44 2973 6540 4003 32 -415 375 N ATOM 102 CA PHE A 44 76.077 -11.852 19.253 1.00 34.63 C ANISOU 102 CA PHE A 44 2847 6409 3901 61 -419 405 C ATOM 103 C PHE A 44 74.997 -10.979 19.875 1.00 40.41 C ANISOU 103 C PHE A 44 3549 7122 4684 121 -409 484 C ATOM 104 O PHE A 44 75.303 -10.042 20.617 1.00 31.03 O ANISOU 104 O PHE A 44 2362 5903 3524 178 -398 493 O ATOM 105 CB PHE A 44 76.442 -11.318 17.864 1.00 35.66 C ANISOU 105 CB PHE A 44 2976 6570 4003 0 -444 429 C ATOM 106 CG PHE A 44 77.792 -11.762 17.378 1.00 52.91 C ANISOU 106 CG PHE A 44 5199 8761 6144 -45 -451 352 C ATOM 107 CD1 PHE A 44 78.839 -11.939 18.266 1.00 52.59 C ANISOU 107 CD1 PHE A 44 5189 8695 6099 -15 -438 279 C ATOM 108 CD2 PHE A 44 78.015 -12.004 16.033 1.00 53.17 C ANISOU 108 CD2 PHE A 44 5240 8823 6141 -116 -468 352 C ATOM 109 CE1 PHE A 44 80.084 -12.344 17.820 1.00 49.16 C ANISOU 109 CE1 PHE A 44 4792 8261 5625 -56 -443 209 C ATOM 110 CE2 PHE A 44 79.255 -12.418 15.584 1.00 44.74 C ANISOU 110 CE2 PHE A 44 4210 7755 5035 -155 -471 283 C ATOM 111 CZ PHE A 44 80.290 -12.588 16.478 1.00 50.80 C ANISOU 111 CZ PHE A 44 5008 8494 5798 -126 -458 212 C ATOM 112 N ALA A 45 73.736 -11.305 19.595 1.00 50.96 N ANISOU 112 N ALA A 45 4859 8472 6033 111 -409 538 N ATOM 113 CA ALA A 45 72.629 -10.539 20.165 1.00 46.70 C ANISOU 113 CA ALA A 45 4293 7909 5543 166 -397 614 C ATOM 114 C ALA A 45 72.551 -10.727 21.680 1.00 42.74 C ANISOU 114 C ALA A 45 3803 7361 5075 242 -367 588 C ATOM 115 O ALA A 45 72.535 -9.743 22.450 1.00 48.32 O ANISOU 115 O ALA A 45 4510 8031 5819 306 -351 615 O ATOM 116 CB ALA A 45 71.318 -10.938 19.511 1.00 51.68 C ANISOU 116 CB ALA A 45 4896 8565 6176 135 -404 673 C ATOM 117 N VAL A 46 72.546 -11.991 22.104 1.00 37.32 N ANISOU 117 N VAL A 46 3130 6674 4375 236 -358 534 N ATOM 118 CA VAL A 46 72.453 -12.308 23.528 1.00 39.09 C ANISOU 118 CA VAL A 46 3369 6854 4629 305 -328 504 C ATOM 119 C VAL A 46 73.623 -11.706 24.306 1.00 36.87 C ANISOU 119 C VAL A 46 3115 6539 4354 352 -315 455 C ATOM 120 O VAL A 46 73.441 -11.087 25.365 1.00 47.53 O ANISOU 120 O VAL A 46 4472 7841 5745 426 -291 470 O ATOM 121 CB VAL A 46 72.432 -13.834 23.755 1.00 38.87 C ANISOU 121 CB VAL A 46 3356 6834 4579 283 -322 443 C ATOM 122 CG1 VAL A 46 72.394 -14.162 25.239 1.00 31.12 C ANISOU 122 CG1 VAL A 46 2393 5804 3628 354 -290 408 C ATOM 123 CG2 VAL A 46 71.259 -14.466 23.024 1.00 33.37 C ANISOU 123 CG2 VAL A 46 2634 6169 3877 239 -334 490 C ATOM 124 N VAL A 47 74.819 -11.867 23.747 1.00 29.81 N ANISOU 124 N VAL A 47 2240 5667 3419 309 -331 397 N ATOM 125 CA VAL A 47 76.037 -11.338 24.346 1.00 38.86 C ANISOU 125 CA VAL A 47 3414 6787 4565 344 -323 345 C ATOM 126 C VAL A 47 76.022 -9.810 24.397 1.00 44.07 C ANISOU 126 C VAL A 47 4062 7427 5254 384 -323 404 C ATOM 127 O VAL A 47 76.521 -9.216 25.356 1.00 35.97 O ANISOU 127 O VAL A 47 3056 6357 4253 448 -303 385 O ATOM 128 CB VAL A 47 77.291 -11.822 23.575 1.00 30.35 C ANISOU 128 CB VAL A 47 2359 5739 3433 279 -343 274 C ATOM 129 CG1 VAL A 47 78.533 -11.045 23.994 1.00 31.44 C ANISOU 129 CG1 VAL A 47 2521 5854 3569 310 -340 232 C ATOM 130 CG2 VAL A 47 77.500 -13.313 23.785 1.00 26.82 C ANISOU 130 CG2 VAL A 47 1934 5298 2960 254 -337 202 C ATOM 131 N PHE A 48 75.431 -9.170 23.391 1.00 29.72 N ANISOU 131 N PHE A 48 2217 5638 3438 348 -343 477 N ATOM 132 CA PHE A 48 75.380 -7.713 23.404 1.00 42.74 C ANISOU 132 CA PHE A 48 3855 7266 5116 383 -343 536 C ATOM 133 C PHE A 48 74.481 -7.222 24.525 1.00 47.52 C ANISOU 133 C PHE A 48 4459 7820 5777 464 -313 582 C ATOM 134 O PHE A 48 74.863 -6.327 25.283 1.00 38.80 O ANISOU 134 O PHE A 48 3370 6670 4700 525 -296 584 O ATOM 135 CB PHE A 48 74.897 -7.143 22.066 1.00 34.46 C ANISOU 135 CB PHE A 48 2778 6258 4056 326 -370 605 C ATOM 136 CG PHE A 48 74.764 -5.639 22.065 1.00 41.05 C ANISOU 136 CG PHE A 48 3602 7072 4924 362 -370 670 C ATOM 137 CD1 PHE A 48 75.883 -4.829 21.938 1.00 38.61 C ANISOU 137 CD1 PHE A 48 3308 6757 4605 366 -379 649 C ATOM 138 CD2 PHE A 48 73.523 -5.036 22.203 1.00 41.16 C ANISOU 138 CD2 PHE A 48 3592 7068 4978 393 -360 753 C ATOM 139 CE1 PHE A 48 75.765 -3.449 21.944 1.00 44.50 C ANISOU 139 CE1 PHE A 48 4046 7481 5381 400 -378 709 C ATOM 140 CE2 PHE A 48 73.399 -3.656 22.209 1.00 45.58 C ANISOU 140 CE2 PHE A 48 4145 7605 5568 426 -359 812 C ATOM 141 CZ PHE A 48 74.522 -2.862 22.079 1.00 46.04 C ANISOU 141 CZ PHE A 48 4218 7658 5616 429 -368 791 C ATOM 142 N LEU A 49 73.303 -7.826 24.654 1.00 44.07 N ANISOU 142 N LEU A 49 4006 7384 5356 465 -305 615 N ATOM 143 CA LEU A 49 72.365 -7.366 25.674 1.00 57.12 C ANISOU 143 CA LEU A 49 5658 8983 7061 537 -276 661 C ATOM 144 C LEU A 49 72.864 -7.655 27.093 1.00 53.41 C ANISOU 144 C LEU A 49 5227 8458 6610 605 -243 600 C ATOM 145 O LEU A 49 73.064 -6.724 27.904 1.00 50.81 O ANISOU 145 O LEU A 49 4919 8073 6315 670 -222 609 O ATOM 146 CB LEU A 49 70.998 -8.008 25.444 1.00 43.72 C ANISOU 146 CB LEU A 49 3936 7303 5373 518 -276 708 C ATOM 147 CG LEU A 49 70.421 -7.681 24.062 1.00 71.03 C ANISOU 147 CG LEU A 49 7360 10812 8815 454 -305 772 C ATOM 148 CD1 LEU A 49 69.245 -8.582 23.703 1.00 75.12 C ANISOU 148 CD1 LEU A 49 7856 11356 9330 422 -309 801 C ATOM 149 CD2 LEU A 49 70.017 -6.215 23.987 1.00 74.80 C ANISOU 149 CD2 LEU A 49 7826 11268 9328 485 -303 848 C ATOM 150 N VAL A 50 73.107 -8.935 27.374 1.00 39.97 N ANISOU 150 N VAL A 50 3537 6765 4885 589 -239 533 N ATOM 151 CA VAL A 50 73.532 -9.350 28.707 1.00 44.55 C ANISOU 151 CA VAL A 50 4155 7290 5480 649 -207 471 C ATOM 152 C VAL A 50 74.877 -8.731 29.065 1.00 49.58 C ANISOU 152 C VAL A 50 4824 7904 6110 676 -202 418 C ATOM 153 O VAL A 50 75.127 -8.362 30.215 1.00 47.30 O ANISOU 153 O VAL A 50 4575 7546 5851 743 -171 395 O ATOM 154 CB VAL A 50 73.636 -10.886 28.814 1.00 45.62 C ANISOU 154 CB VAL A 50 4299 7448 5587 617 -206 405 C ATOM 155 CG1 VAL A 50 74.143 -11.299 30.190 1.00 31.57 C ANISOU 155 CG1 VAL A 50 2564 5609 3823 678 -173 336 C ATOM 156 CG2 VAL A 50 72.292 -11.527 28.521 1.00 29.34 C ANISOU 156 CG2 VAL A 50 2209 5406 3533 594 -210 455 C ATOM 157 N GLY A 51 75.729 -8.587 28.056 1.00 41.23 N ANISOU 157 N GLY A 51 3767 6884 5013 616 -230 398 N ATOM 158 CA GLY A 51 77.054 -8.048 28.264 1.00 41.95 C ANISOU 158 CA GLY A 51 3909 6938 5094 624 -225 341 C ATOM 159 C GLY A 51 77.044 -6.570 28.581 1.00 45.28 C ANISOU 159 C GLY A 51 4341 7311 5552 674 -215 391 C ATOM 160 O GLY A 51 77.626 -6.148 29.587 1.00 54.96 O ANISOU 160 O GLY A 51 5614 8469 6798 731 -188 354 O ATOM 161 N VAL A 52 76.359 -5.781 27.755 1.00 41.02 N ANISOU 161 N VAL A 52 3759 6806 5023 656 -234 475 N ATOM 162 CA VAL A 52 76.334 -4.343 27.991 1.00 48.26 C ANISOU 162 CA VAL A 52 4683 7680 5974 702 -226 526 C ATOM 163 C VAL A 52 75.656 -4.040 29.320 1.00 51.42 C ANISOU 163 C VAL A 52 5098 8013 6426 787 -188 547 C ATOM 164 O VAL A 52 76.247 -3.375 30.184 1.00 45.22 O ANISOU 164 O VAL A 52 4358 7161 5662 841 -166 521 O ATOM 165 CB VAL A 52 75.615 -3.570 26.858 1.00 46.21 C ANISOU 165 CB VAL A 52 4369 7470 5717 667 -253 618 C ATOM 166 CG1 VAL A 52 75.316 -2.142 27.293 1.00 50.33 C ANISOU 166 CG1 VAL A 52 4896 7942 6284 726 -239 680 C ATOM 167 CG2 VAL A 52 76.459 -3.573 25.590 1.00 36.12 C ANISOU 167 CG2 VAL A 52 3084 6248 4391 589 -289 598 C ATOM 168 N LEU A 53 74.450 -4.569 29.518 1.00 50.12 N ANISOU 168 N LEU A 53 4899 7863 6279 800 -181 589 N ATOM 169 CA LEU A 53 73.711 -4.204 30.723 1.00 47.81 C ANISOU 169 CA LEU A 53 4634 7493 6037 871 -145 612 C ATOM 170 C LEU A 53 74.360 -4.775 31.983 1.00 52.36 C ANISOU 170 C LEU A 53 5263 8013 6619 918 -114 530 C ATOM 171 O LEU A 53 74.511 -4.077 32.997 1.00 40.67 O ANISOU 171 O LEU A 53 3825 6455 5172 980 -86 523 O ATOM 172 CB LEU A 53 72.256 -4.661 30.617 1.00 59.99 C ANISOU 172 CB LEU A 53 6149 9047 7596 859 -142 668 C ATOM 173 CG LEU A 53 71.394 -3.825 29.668 1.00 57.46 C ANISOU 173 CG LEU A 53 5788 8757 7286 831 -162 760 C ATOM 174 CD1 LEU A 53 69.959 -4.329 29.640 1.00 70.41 C ANISOU 174 CD1 LEU A 53 7405 10406 8943 822 -157 809 C ATOM 175 CD2 LEU A 53 71.438 -2.352 30.056 1.00 44.92 C ANISOU 175 CD2 LEU A 53 4218 7114 5734 881 -148 801 C ATOM 176 N GLY A 54 74.785 -6.031 31.900 1.00 40.26 N ANISOU 176 N GLY A 54 3731 6515 5052 886 -120 465 N ATOM 177 CA GLY A 54 75.350 -6.711 33.048 1.00 45.07 C ANISOU 177 CA GLY A 54 4390 7072 5664 924 -92 384 C ATOM 178 C GLY A 54 76.675 -6.119 33.476 1.00 44.00 C ANISOU 178 C GLY A 54 4303 6893 5523 949 -83 327 C ATOM 179 O GLY A 54 76.857 -5.779 34.648 1.00 47.63 O ANISOU 179 O GLY A 54 4809 7276 6012 1011 -51 304 O ATOM 180 N ASN A 55 77.598 -5.971 32.530 1.00 35.53 N ANISOU 180 N ASN A 55 3235 5854 4412 891 -110 302 N ATOM 181 CA ASN A 55 78.893 -5.399 32.863 1.00 42.56 C ANISOU 181 CA ASN A 55 4177 6698 5294 906 -103 246 C ATOM 182 C ASN A 55 78.792 -3.929 33.261 1.00 42.43 C ANISOU 182 C ASN A 55 4172 6630 5317 961 -91 298 C ATOM 183 O ASN A 55 79.568 -3.463 34.102 1.00 46.36 O ANISOU 183 O ASN A 55 4721 7065 5829 1007 -70 256 O ATOM 184 CB ASN A 55 79.874 -5.576 31.705 1.00 34.78 C ANISOU 184 CB ASN A 55 3192 5764 4259 829 -136 210 C ATOM 185 CG ASN A 55 80.422 -6.990 31.620 1.00 29.85 C ANISOU 185 CG ASN A 55 2580 5168 3594 786 -141 129 C ATOM 186 OD1 ASN A 55 80.755 -7.600 32.638 1.00 34.66 O ANISOU 186 OD1 ASN A 55 3226 5735 4209 822 -115 68 O ATOM 187 ND2 ASN A 55 80.508 -7.521 30.409 1.00 42.74 N ANISOU 187 ND2 ASN A 55 4180 6873 5185 709 -173 129 N ATOM 188 N ALA A 56 77.836 -3.198 32.687 1.00 36.86 N ANISOU 188 N ALA A 56 3421 5950 4632 959 -102 389 N ATOM 189 CA ALA A 56 77.649 -1.816 33.119 1.00 43.77 C ANISOU 189 CA ALA A 56 4307 6774 5549 1016 -89 442 C ATOM 190 C ALA A 56 77.190 -1.781 34.572 1.00 51.17 C ANISOU 190 C ALA A 56 5280 7633 6529 1091 -48 434 C ATOM 191 O ALA A 56 77.672 -0.962 35.364 1.00 49.40 O ANISOU 191 O ALA A 56 5105 7335 6328 1136 -28 418 O ATOM 192 CB ALA A 56 76.653 -1.095 32.233 1.00 49.07 C ANISOU 192 CB ALA A 56 4923 7489 6235 997 -108 542 C ATOM 193 N LEU A 57 76.282 -2.689 34.927 1.00 53.89 N ANISOU 193 N LEU A 57 5618 7976 6881 1087 -37 437 N ATOM 194 CA LEU A 57 75.824 -2.768 36.311 1.00 51.03 C ANISOU 194 CA LEU A 57 5308 7526 6557 1135 0 420 C ATOM 195 C LEU A 57 76.943 -3.181 37.263 1.00 50.51 C ANISOU 195 C LEU A 57 5305 7404 6482 1157 20 326 C ATOM 196 O LEU A 57 77.014 -2.687 38.391 1.00 44.44 O ANISOU 196 O LEU A 57 4593 6547 5745 1197 48 310 O ATOM 197 CB LEU A 57 74.655 -3.747 36.441 1.00 55.06 C ANISOU 197 CB LEU A 57 5795 8052 7074 1122 5 439 C ATOM 198 CG LEU A 57 74.113 -3.912 37.865 1.00 53.74 C ANISOU 198 CG LEU A 57 5679 7796 6943 1164 40 421 C ATOM 199 CD1 LEU A 57 73.564 -2.593 38.394 1.00 37.15 C ANISOU 199 CD1 LEU A 57 3600 5632 4885 1202 55 474 C ATOM 200 CD2 LEU A 57 73.060 -5.008 37.945 1.00 53.61 C ANISOU 200 CD2 LEU A 57 5639 7802 6927 1148 43 432 C ATOM 201 N VAL A 58 77.824 -4.070 36.807 1.00 51.71 N ANISOU 201 N VAL A 58 5449 7607 6590 1124 5 263 N ATOM 202 CA VAL A 58 78.955 -4.497 37.627 1.00 38.56 C ANISOU 202 CA VAL A 58 3846 5892 4914 1138 23 171 C ATOM 203 C VAL A 58 79.913 -3.332 37.858 1.00 33.71 C ANISOU 203 C VAL A 58 3270 5231 4308 1165 27 158 C ATOM 204 O VAL A 58 80.458 -3.170 38.959 1.00 34.20 O ANISOU 204 O VAL A 58 3400 5208 4387 1192 53 111 O ATOM 205 CB VAL A 58 79.719 -5.678 36.981 1.00 30.73 C ANISOU 205 CB VAL A 58 2836 4971 3870 1092 3 104 C ATOM 206 CG1 VAL A 58 81.019 -5.950 37.720 1.00 37.55 C ANISOU 206 CG1 VAL A 58 3765 5782 4719 1102 18 10 C ATOM 207 CG2 VAL A 58 78.851 -6.929 36.953 1.00 34.05 C ANISOU 207 CG2 VAL A 58 3230 5424 4283 1066 3 105 C ATOM 208 N VAL A 59 80.090 -2.503 36.831 1.00 36.84 N ANISOU 208 N VAL A 59 3624 5679 4693 1152 2 204 N ATOM 209 CA VAL A 59 80.911 -1.305 36.972 1.00 43.11 C ANISOU 209 CA VAL A 59 4452 6432 5498 1178 4 202 C ATOM 210 C VAL A 59 80.274 -0.367 37.990 1.00 40.42 C ANISOU 210 C VAL A 59 4152 5998 5210 1223 32 241 C ATOM 211 O VAL A 59 80.960 0.195 38.851 1.00 45.57 O ANISOU 211 O VAL A 59 4865 6572 5878 1250 51 204 O ATOM 212 CB VAL A 59 81.089 -0.569 35.621 1.00 47.93 C ANISOU 212 CB VAL A 59 5021 7102 6089 1133 -31 250 C ATOM 213 CG1 VAL A 59 81.680 0.817 35.830 1.00 26.93 C ANISOU 213 CG1 VAL A 59 2391 4393 3449 1167 -26 265 C ATOM 214 CG2 VAL A 59 81.960 -1.388 34.677 1.00 32.08 C ANISOU 214 CG2 VAL A 59 3013 5151 4026 1053 -59 192 C ATOM 215 N TRP A 60 78.951 -0.240 37.915 1.00 52.45 N ANISOU 215 N TRP A 60 5642 7528 6759 1225 34 312 N ATOM 216 CA TRP A 60 78.212 0.618 38.834 1.00 51.04 C ANISOU 216 CA TRP A 60 5496 7268 6628 1261 58 349 C ATOM 217 C TRP A 60 78.332 0.139 40.277 1.00 49.29 C ANISOU 217 C TRP A 60 5341 6961 6425 1280 88 288 C ATOM 218 O TRP A 60 78.402 0.942 41.206 1.00 52.35 O ANISOU 218 O TRP A 60 5779 7269 6844 1304 107 284 O ATOM 219 CB TRP A 60 76.737 0.677 38.424 1.00 63.52 C ANISOU 219 CB TRP A 60 7027 8880 8227 1254 52 431 C ATOM 220 CG TRP A 60 75.872 1.478 39.351 1.00 67.56 C ANISOU 220 CG TRP A 60 7569 9315 8785 1287 75 468 C ATOM 221 CD1 TRP A 60 74.911 1.001 40.195 1.00 63.98 C ANISOU 221 CD1 TRP A 60 7130 8824 8353 1297 94 470 C ATOM 222 CD2 TRP A 60 75.888 2.899 39.523 1.00 72.98 C ANISOU 222 CD2 TRP A 60 8274 9956 9497 1311 79 504 C ATOM 223 NE1 TRP A 60 74.327 2.039 40.882 1.00 73.62 N ANISOU 223 NE1 TRP A 60 8378 9983 9612 1324 109 504 N ATOM 224 CE2 TRP A 60 74.910 3.215 40.488 1.00 68.74 C ANISOU 224 CE2 TRP A 60 7764 9358 8997 1333 101 525 C ATOM 225 CE3 TRP A 60 76.635 3.936 38.956 1.00 87.22 C ANISOU 225 CE3 TRP A 60 10076 11767 11296 1314 66 520 C ATOM 226 CZ2 TRP A 60 74.661 4.523 40.897 1.00 83.24 C ANISOU 226 CZ2 TRP A 60 9623 11141 10862 1357 110 559 C ATOM 227 CZ3 TRP A 60 76.386 5.233 39.363 1.00 97.48 C ANISOU 227 CZ3 TRP A 60 11400 13011 12628 1339 76 556 C ATOM 228 CH2 TRP A 60 75.407 5.516 40.324 1.00 85.85 C ANISOU 228 CH2 TRP A 60 9952 11478 11188 1359 97 574 C ATOM 229 N VAL A 61 78.386 -1.176 40.452 1.00 47.41 N ANISOU 229 N VAL A 61 5105 6742 6167 1261 91 240 N ATOM 230 CA VAL A 61 78.468 -1.763 41.781 1.00 39.74 C ANISOU 230 CA VAL A 61 4194 5695 5212 1269 117 184 C ATOM 231 C VAL A 61 79.865 -1.611 42.374 1.00 40.46 C ANISOU 231 C VAL A 61 4346 5733 5293 1269 126 111 C ATOM 232 O VAL A 61 80.019 -1.236 43.540 1.00 44.45 O ANISOU 232 O VAL A 61 4907 6154 5827 1279 147 89 O ATOM 233 CB VAL A 61 78.071 -3.260 41.749 1.00 37.84 C ANISOU 233 CB VAL A 61 3934 5492 4951 1245 117 157 C ATOM 234 CG1 VAL A 61 78.858 -4.068 42.776 1.00 43.63 C ANISOU 234 CG1 VAL A 61 4729 6169 5679 1236 135 73 C ATOM 235 CG2 VAL A 61 76.571 -3.415 41.960 1.00 39.15 C ANISOU 235 CG2 VAL A 61 4073 5658 5146 1252 123 214 C ATOM 236 N THR A 62 80.883 -1.889 41.567 1.00 31.49 N ANISOU 236 N THR A 62 3197 4650 4116 1251 109 75 N ATOM 237 CA THR A 62 82.246 -1.914 42.081 1.00 39.75 C ANISOU 237 CA THR A 62 4304 5652 5149 1245 116 1 C ATOM 238 C THR A 62 82.935 -0.550 42.148 1.00 38.89 C ANISOU 238 C THR A 62 4222 5503 5053 1264 116 11 C ATOM 239 O THR A 62 83.874 -0.376 42.924 1.00 41.99 O ANISOU 239 O THR A 62 4675 5832 5449 1260 128 -41 O ATOM 240 CB THR A 62 83.128 -2.855 41.241 1.00 33.26 C ANISOU 240 CB THR A 62 3463 4902 4274 1215 97 -56 C ATOM 241 OG1 THR A 62 83.079 -2.456 39.866 1.00 41.57 O ANISOU 241 OG1 THR A 62 4448 6044 5303 1208 67 -15 O ATOM 242 CG2 THR A 62 82.636 -4.287 41.362 1.00 29.90 C ANISOU 242 CG2 THR A 62 3025 4502 3833 1192 100 -81 C ATOM 243 N ALA A 63 82.475 0.415 41.355 1.00 38.86 N ANISOU 243 N ALA A 63 4173 5534 5057 1279 101 79 N ATOM 244 CA ALA A 63 83.190 1.687 41.256 1.00 51.79 C ANISOU 244 CA ALA A 63 5832 7144 6704 1295 97 89 C ATOM 245 C ALA A 63 83.237 2.469 42.573 1.00 42.99 C ANISOU 245 C ALA A 63 4780 5924 5630 1312 122 81 C ATOM 246 O ALA A 63 84.229 3.137 42.864 1.00 46.48 O ANISOU 246 O ALA A 63 5264 6324 6073 1314 124 51 O ATOM 247 CB ALA A 63 82.569 2.550 40.166 1.00 44.23 C ANISOU 247 CB ALA A 63 4812 6244 5749 1303 76 172 C ATOM 248 N PHE A 64 82.174 2.384 43.366 1.00 57.43 N ANISOU 248 N PHE A 64 7240 7589 6993 1019 44 -412 N ATOM 249 CA PHE A 64 82.113 3.113 44.631 1.00 77.93 C ANISOU 249 CA PHE A 64 9872 10148 9590 1007 87 -504 C ATOM 250 C PHE A 64 83.053 2.542 45.689 1.00 71.34 C ANISOU 250 C PHE A 64 9127 9354 8625 952 126 -500 C ATOM 251 O PHE A 64 83.494 3.256 46.590 1.00 75.88 O ANISOU 251 O PHE A 64 9750 9897 9185 937 131 -542 O ATOM 252 CB PHE A 64 80.679 3.133 45.160 1.00 83.76 C ANISOU 252 CB PHE A 64 10561 10873 10390 1026 168 -617 C ATOM 253 CG PHE A 64 79.713 3.830 44.245 1.00103.04 C ANISOU 253 CG PHE A 64 12915 13267 12967 1081 132 -633 C ATOM 254 CD1 PHE A 64 79.683 5.213 44.171 1.00108.71 C ANISOU 254 CD1 PHE A 64 13615 13912 13777 1110 81 -658 C ATOM 255 CD2 PHE A 64 78.841 3.103 43.452 1.00 86.08 C ANISOU 255 CD2 PHE A 64 10704 11149 10854 1103 149 -622 C ATOM 256 CE1 PHE A 64 78.799 5.858 43.325 1.00 98.67 C ANISOU 256 CE1 PHE A 64 12264 12597 12630 1161 48 -672 C ATOM 257 CE2 PHE A 64 77.954 3.743 42.605 1.00 94.94 C ANISOU 257 CE2 PHE A 64 11745 12228 12099 1153 115 -636 C ATOM 258 CZ PHE A 64 77.934 5.122 42.543 1.00 97.73 C ANISOU 258 CZ PHE A 64 12081 12508 12543 1182 65 -661 C ATOM 259 N GLU A 65 83.359 1.255 45.574 1.00 64.52 N ANISOU 259 N GLU A 65 8286 8561 7666 923 154 -449 N ATOM 260 CA GLU A 65 84.233 0.593 46.534 1.00 58.76 C ANISOU 260 CA GLU A 65 7640 7877 6808 870 195 -441 C ATOM 261 C GLU A 65 85.636 0.359 45.981 1.00 59.79 C ANISOU 261 C GLU A 65 7820 8032 6866 848 121 -323 C ATOM 262 O GLU A 65 86.517 -0.113 46.695 1.00 66.93 O ANISOU 262 O GLU A 65 8797 8971 7663 804 142 -304 O ATOM 263 CB GLU A 65 83.616 -0.735 46.979 1.00 67.77 C ANISOU 263 CB GLU A 65 8782 9084 7883 849 289 -475 C ATOM 264 CG GLU A 65 82.477 -0.584 47.978 1.00 86.95 C ANISOU 264 CG GLU A 65 11192 11497 10348 855 379 -601 C ATOM 265 CD GLU A 65 81.182 -1.204 47.491 1.00 92.81 C ANISOU 265 CD GLU A 65 11860 12259 11145 881 425 -634 C ATOM 266 OE1 GLU A 65 81.014 -1.344 46.262 1.00 89.14 O ANISOU 266 OE1 GLU A 65 11343 11797 10729 909 372 -570 O ATOM 267 OE2 GLU A 65 80.334 -1.553 48.340 1.00 89.60 O ANISOU 267 OE2 GLU A 65 11447 11865 10733 875 515 -724 O ATOM 268 N ALA A 66 85.850 0.717 44.718 1.00 60.81 N ANISOU 268 N ALA A 66 7909 8141 7056 878 35 -244 N ATOM 269 CA ALA A 66 87.132 0.478 44.061 1.00 51.34 C ANISOU 269 CA ALA A 66 6749 6965 5794 861 -39 -126 C ATOM 270 C ALA A 66 88.229 1.366 44.644 1.00 58.09 C ANISOU 270 C ALA A 66 7667 7782 6621 841 -82 -114 C ATOM 271 O ALA A 66 89.418 1.137 44.417 1.00 55.72 O ANISOU 271 O ALA A 66 7417 7505 6250 816 -130 -26 O ATOM 272 CB ALA A 66 87.010 0.700 42.560 1.00 44.94 C ANISOU 272 CB ALA A 66 5875 6137 5062 902 -120 -50 C ATOM 273 N LYS A 67 87.816 2.397 45.372 1.00 65.80 N ANISOU 273 N LYS A 67 8641 8702 7659 853 -66 -202 N ATOM 274 CA LYS A 67 88.748 3.290 46.051 1.00 69.86 C ANISOU 274 CA LYS A 67 9214 9177 8151 835 -99 -207 C ATOM 275 C LYS A 67 89.524 2.605 47.182 1.00 73.63 C ANISOU 275 C LYS A 67 9777 9702 8498 780 -46 -214 C ATOM 276 O LYS A 67 90.675 2.956 47.447 1.00 57.92 O ANISOU 276 O LYS A 67 7847 7704 6457 755 -90 -169 O ATOM 277 CB LYS A 67 87.988 4.500 46.601 1.00 71.96 C ANISOU 277 CB LYS A 67 9453 9374 8517 862 -85 -309 C ATOM 278 CG LYS A 67 88.872 5.594 47.166 1.00 78.70 C ANISOU 278 CG LYS A 67 10357 10177 9369 851 -130 -314 C ATOM 279 CD LYS A 67 88.036 6.776 47.623 1.00104.24 C ANISOU 279 CD LYS A 67 13558 13341 12708 881 -117 -414 C ATOM 280 CE LYS A 67 88.908 7.890 48.176 1.00105.38 C ANISOU 280 CE LYS A 67 13753 13434 12855 871 -163 -420 C ATOM 281 NZ LYS A 67 88.095 9.048 48.639 1.00 95.73 N ANISOU 281 NZ LYS A 67 12498 12141 11733 901 -149 -519 N ATOM 282 N ARG A 68 88.911 1.617 47.830 1.00 69.75 N ANISOU 282 N ARG A 68 9291 9260 7951 760 46 -267 N ATOM 283 CA ARG A 68 89.517 1.012 49.016 1.00 54.01 C ANISOU 283 CA ARG A 68 7376 7307 5838 709 106 -288 C ATOM 284 C ARG A 68 89.727 -0.500 48.906 1.00 62.94 C ANISOU 284 C ARG A 68 8527 8521 6865 679 148 -238 C ATOM 285 O ARG A 68 90.836 -0.985 49.134 1.00 58.26 O ANISOU 285 O ARG A 68 8000 7966 6171 640 135 -176 O ATOM 286 CB ARG A 68 88.674 1.320 50.260 1.00 78.92 C ANISOU 286 CB ARG A 68 10535 10442 9011 707 191 -417 C ATOM 287 CG ARG A 68 88.722 2.780 50.704 1.00 97.54 C ANISOU 287 CG ARG A 68 12897 12723 11441 724 158 -472 C ATOM 288 CD ARG A 68 87.839 3.038 51.922 1.00102.19 C ANISOU 288 CD ARG A 68 13489 13293 12047 722 246 -600 C ATOM 289 NE ARG A 68 88.352 2.404 53.134 1.00107.76 N ANISOU 289 NE ARG A 68 14270 14041 12634 674 311 -629 N ATOM 290 CZ ARG A 68 87.740 2.444 54.315 1.00119.78 C ANISOU 290 CZ ARG A 68 15807 15558 14144 664 394 -734 C ATOM 291 NH1 ARG A 68 86.587 3.086 54.445 1.00 98.06 N ANISOU 291 NH1 ARG A 68 13002 12762 11494 699 423 -822 N ATOM 292 NH2 ARG A 68 88.279 1.840 55.365 1.00115.11 N ANISOU 292 NH2 ARG A 68 15287 15008 13442 619 449 -752 N ATOM 293 N THR A 69 88.674 -1.247 48.578 1.00 43.19 N ANISOU 293 N THR A 69 5972 6049 4389 695 199 -264 N ATOM 294 CA THR A 69 88.798 -2.703 48.516 1.00 51.06 C ANISOU 294 CA THR A 69 6982 7119 5299 660 242 -221 C ATOM 295 C THR A 69 89.328 -3.181 47.155 1.00 44.13 C ANISOU 295 C THR A 69 6074 6254 4439 657 166 -99 C ATOM 296 O THR A 69 88.851 -2.769 46.096 1.00 45.33 O ANISOU 296 O THR A 69 6177 6397 4651 716 119 -77 O ATOM 297 CB THR A 69 87.452 -3.410 48.851 1.00 45.74 C ANISOU 297 CB THR A 69 6256 6458 4664 655 330 -298 C ATOM 298 OG1 THR A 69 87.586 -4.824 48.662 1.00 65.62 O ANISOU 298 OG1 THR A 69 8748 8986 7197 568 338 -232 O ATOM 299 CG2 THR A 69 86.323 -2.901 47.988 1.00 47.57 C ANISOU 299 CG2 THR A 69 6410 6668 4995 727 318 -332 C ATOM 300 N ILE A 70 90.343 -4.041 47.212 1.00 29.77 N ANISOU 300 N ILE A 70 4256 4412 2642 549 146 -24 N ATOM 301 CA ILE A 70 91.070 -4.506 46.030 1.00 33.60 C ANISOU 301 CA ILE A 70 4707 4878 3181 515 78 76 C ATOM 302 C ILE A 70 90.260 -5.417 45.092 1.00 31.39 C ANISOU 302 C ILE A 70 4368 4619 2941 530 89 96 C ATOM 303 O ILE A 70 90.372 -5.314 43.858 1.00 35.26 O ANISOU 303 O ILE A 70 4820 5101 3475 558 33 155 O ATOM 304 CB ILE A 70 92.367 -5.239 46.470 1.00 30.62 C ANISOU 304 CB ILE A 70 4342 4459 2832 381 68 114 C ATOM 305 CG1 ILE A 70 93.424 -4.232 46.937 1.00 28.82 C ANISOU 305 CG1 ILE A 70 4157 4209 2586 367 29 127 C ATOM 306 CG2 ILE A 70 92.942 -6.081 45.356 1.00 30.25 C ANISOU 306 CG2 ILE A 70 4255 4378 2860 320 26 179 C ATOM 307 CD1 ILE A 70 93.463 -4.022 48.431 1.00 22.89 C ANISOU 307 CD1 ILE A 70 3452 3467 1779 342 81 61 C ATOM 308 N ASN A 71 89.422 -6.281 45.662 1.00 31.09 N ANISOU 308 N ASN A 71 4316 4600 2896 507 160 43 N ATOM 309 CA ASN A 71 88.649 -7.213 44.843 1.00 27.43 C ANISOU 309 CA ASN A 71 3799 4154 2471 516 172 59 C ATOM 310 C ASN A 71 87.697 -6.464 43.916 1.00 33.84 C ANISOU 310 C ASN A 71 4572 5010 3275 640 157 52 C ATOM 311 O ASN A 71 87.469 -6.869 42.765 1.00 24.36 O ANISOU 311 O ASN A 71 3324 3819 2114 662 124 104 O ATOM 312 CB ASN A 71 87.859 -8.189 45.721 1.00 20.90 C ANISOU 312 CB ASN A 71 2968 3330 1644 463 249 -3 C ATOM 313 CG ASN A 71 88.747 -9.202 46.422 1.00 46.06 C ANISOU 313 CG ASN A 71 6186 6470 4846 336 253 12 C ATOM 314 OD1 ASN A 71 89.750 -9.657 45.871 1.00 29.16 O ANISOU 314 OD1 ASN A 71 4044 4300 2735 295 203 73 O ATOM 315 ND2 ASN A 71 88.374 -9.564 47.645 1.00 40.72 N ANISOU 315 ND2 ASN A 71 5533 5787 4151 285 317 -51 N ATOM 316 N ALA A 72 87.174 -5.348 44.416 1.00 22.54 N ANISOU 316 N ALA A 72 3162 3599 1804 719 180 -23 N ATOM 317 CA ALA A 72 86.312 -4.490 43.620 1.00 35.43 C ANISOU 317 CA ALA A 72 4731 5204 3528 793 148 -47 C ATOM 318 C ALA A 72 87.087 -3.866 42.464 1.00 40.18 C ANISOU 318 C ALA A 72 5322 5777 4169 815 36 53 C ATOM 319 O ALA A 72 86.531 -3.644 41.393 1.00 34.80 O ANISOU 319 O ALA A 72 4573 5076 3574 855 -7 78 O ATOM 320 CB ALA A 72 85.687 -3.411 44.487 1.00 38.68 C ANISOU 320 CB ALA A 72 5132 5554 4009 807 177 -156 C ATOM 321 N ILE A 73 88.372 -3.596 42.681 1.00 32.49 N ANISOU 321 N ILE A 73 4413 4800 3130 788 -10 111 N ATOM 322 CA ILE A 73 89.229 -3.076 41.620 1.00 27.04 C ANISOU 322 CA ILE A 73 3715 4079 2481 795 -112 208 C ATOM 323 C ILE A 73 89.410 -4.127 40.532 1.00 31.74 C ANISOU 323 C ILE A 73 4252 4650 3159 722 -111 261 C ATOM 324 O ILE A 73 89.275 -3.831 39.329 1.00 23.79 O ANISOU 324 O ILE A 73 3195 3611 2233 734 -161 299 O ATOM 325 CB ILE A 73 90.609 -2.652 42.163 1.00 24.22 C ANISOU 325 CB ILE A 73 3407 3667 2129 716 -135 229 C ATOM 326 CG1 ILE A 73 90.445 -1.666 43.323 1.00 33.27 C ANISOU 326 CG1 ILE A 73 4612 4817 3211 766 -123 156 C ATOM 327 CG2 ILE A 73 91.473 -2.070 41.054 1.00 27.24 C ANISOU 327 CG2 ILE A 73 3757 3979 2614 673 -214 296 C ATOM 328 CD1 ILE A 73 91.744 -1.289 44.004 1.00 30.71 C ANISOU 328 CD1 ILE A 73 4348 4461 2860 704 -143 177 C ATOM 329 N TRP A 74 89.678 -5.361 40.962 1.00 27.90 N ANISOU 329 N TRP A 74 3772 4164 2664 637 -55 251 N ATOM 330 CA TRP A 74 89.843 -6.461 40.017 1.00 22.58 C ANISOU 330 CA TRP A 74 3057 3462 2061 568 -55 282 C ATOM 331 C TRP A 74 88.602 -6.613 39.138 1.00 25.71 C ANISOU 331 C TRP A 74 3394 3901 2472 648 -49 283 C ATOM 332 O TRP A 74 88.675 -6.548 37.898 1.00 27.97 O ANISOU 332 O TRP A 74 3644 4151 2832 632 -88 317 O ATOM 333 CB TRP A 74 90.094 -7.791 40.741 1.00 27.82 C ANISOU 333 CB TRP A 74 3738 4117 2717 481 -7 260 C ATOM 334 CG TRP A 74 91.337 -7.923 41.609 1.00 27.06 C ANISOU 334 CG TRP A 74 3691 3982 2610 397 -9 258 C ATOM 335 CD1 TRP A 74 91.445 -8.664 42.753 1.00 23.67 C ANISOU 335 CD1 TRP A 74 3287 3564 2142 361 38 227 C ATOM 336 CD2 TRP A 74 92.636 -7.344 41.389 1.00 22.78 C ANISOU 336 CD2 TRP A 74 3164 3408 2085 378 -53 292 C ATOM 337 NE1 TRP A 74 92.716 -8.578 43.260 1.00 26.09 N ANISOU 337 NE1 TRP A 74 3623 3850 2438 325 24 242 N ATOM 338 CE2 TRP A 74 93.467 -7.773 42.445 1.00 21.32 C ANISOU 338 CE2 TRP A 74 3013 3220 1865 334 -30 281 C ATOM 339 CE3 TRP A 74 93.175 -6.505 40.409 1.00 33.37 C ANISOU 339 CE3 TRP A 74 4491 4719 3469 390 -108 329 C ATOM 340 CZ2 TRP A 74 94.802 -7.388 42.551 1.00 25.77 C ANISOU 340 CZ2 TRP A 74 3600 3759 2433 305 -60 305 C ATOM 341 CZ3 TRP A 74 94.500 -6.124 40.517 1.00 37.78 C ANISOU 341 CZ3 TRP A 74 5072 5251 4031 358 -135 351 C ATOM 342 CH2 TRP A 74 95.298 -6.565 41.580 1.00 32.81 C ANISOU 342 CH2 TRP A 74 4478 4624 3364 317 -111 339 C ATOM 343 N PHE A 75 87.456 -6.779 39.797 1.00 24.52 N ANISOU 343 N PHE A 75 3241 3823 2254 723 3 236 N ATOM 344 CA PHE A 75 86.203 -7.010 39.087 1.00 26.73 C ANISOU 344 CA PHE A 75 3464 4155 2539 801 14 230 C ATOM 345 C PHE A 75 85.780 -5.808 38.240 1.00 27.16 C ANISOU 345 C PHE A 75 3479 4198 2642 893 -64 252 C ATOM 346 O PHE A 75 85.173 -5.975 37.180 1.00 25.55 O ANISOU 346 O PHE A 75 3212 3982 2515 910 -83 270 O ATOM 347 CB PHE A 75 85.102 -7.376 40.082 1.00 20.42 C ANISOU 347 CB PHE A 75 2670 3417 1669 833 107 141 C ATOM 348 CG PHE A 75 85.256 -8.752 40.666 1.00 35.49 C ANISOU 348 CG PHE A 75 4584 5297 3602 725 153 131 C ATOM 349 CD1 PHE A 75 85.431 -9.849 39.839 1.00 24.24 C ANISOU 349 CD1 PHE A 75 3125 3849 2236 676 133 181 C ATOM 350 CD2 PHE A 75 85.253 -8.948 42.039 1.00 27.35 C ANISOU 350 CD2 PHE A 75 3597 4249 2547 667 211 67 C ATOM 351 CE1 PHE A 75 85.580 -11.119 40.367 1.00 20.96 C ANISOU 351 CE1 PHE A 75 2724 3399 1841 581 161 167 C ATOM 352 CE2 PHE A 75 85.402 -10.215 42.572 1.00 17.90 C ANISOU 352 CE2 PHE A 75 2411 3017 1372 566 237 63 C ATOM 353 CZ PHE A 75 85.567 -11.301 41.735 1.00 21.21 C ANISOU 353 CZ PHE A 75 2803 3417 1840 526 209 113 C ATOM 354 N LEU A 76 86.124 -4.607 38.693 1.00 24.15 N ANISOU 354 N LEU A 76 3120 3767 2288 908 -100 229 N ATOM 355 CA LEU A 76 85.828 -3.403 37.929 1.00 25.89 C ANISOU 355 CA LEU A 76 3286 3921 2630 956 -172 232 C ATOM 356 C LEU A 76 86.597 -3.397 36.615 1.00 32.24 C ANISOU 356 C LEU A 76 4080 4670 3498 879 -224 307 C ATOM 357 O LEU A 76 86.012 -3.174 35.550 1.00 33.27 O ANISOU 357 O LEU A 76 4156 4763 3724 878 -250 313 O ATOM 358 CB LEU A 76 86.170 -2.148 38.735 1.00 30.88 C ANISOU 358 CB LEU A 76 3949 4492 3292 954 -186 181 C ATOM 359 CG LEU A 76 86.058 -0.807 38.007 1.00 44.97 C ANISOU 359 CG LEU A 76 5688 6204 5196 1000 -267 190 C ATOM 360 CD1 LEU A 76 84.610 -0.497 37.671 1.00 51.69 C ANISOU 360 CD1 LEU A 76 6454 7025 6161 1044 -243 118 C ATOM 361 CD2 LEU A 76 86.678 0.319 38.826 1.00 44.08 C ANISOU 361 CD2 LEU A 76 5621 6038 5089 989 -287 157 C ATOM 362 N ASN A 77 87.902 -3.658 36.687 1.00 30.14 N ANISOU 362 N ASN A 77 3866 4371 3215 774 -223 337 N ATOM 363 CA ASN A 77 88.705 -3.688 35.468 1.00 23.15 C ANISOU 363 CA ASN A 77 2973 3407 2417 665 -261 376 C ATOM 364 C ASN A 77 88.250 -4.801 34.522 1.00 28.43 C ANISOU 364 C ASN A 77 3610 4078 3115 626 -235 380 C ATOM 365 O ASN A 77 88.210 -4.615 33.295 1.00 25.73 O ANISOU 365 O ASN A 77 3243 3685 2848 593 -271 395 O ATOM 366 CB ASN A 77 90.190 -3.852 35.804 1.00 22.26 C ANISOU 366 CB ASN A 77 2912 3252 2293 563 -269 392 C ATOM 367 CG ASN A 77 90.829 -2.559 36.291 1.00 34.09 C ANISOU 367 CG ASN A 77 4437 4722 3795 575 -316 402 C ATOM 368 OD1 ASN A 77 91.648 -1.957 35.594 1.00 30.22 O ANISOU 368 OD1 ASN A 77 3946 4172 3364 521 -366 429 O ATOM 369 ND2 ASN A 77 90.459 -2.130 37.493 1.00 21.27 N ANISOU 369 ND2 ASN A 77 2839 3149 2095 663 -297 373 N ATOM 370 N LEU A 78 87.854 -5.935 35.097 1.00 30.84 N ANISOU 370 N LEU A 78 3916 4447 3356 641 -169 361 N ATOM 371 CA LEU A 78 87.346 -7.042 34.290 1.00 21.88 C ANISOU 371 CA LEU A 78 2749 3320 2244 615 -138 360 C ATOM 372 C LEU A 78 86.080 -6.633 33.542 1.00 28.80 C ANISOU 372 C LEU A 78 3573 4210 3161 683 -153 357 C ATOM 373 O LEU A 78 85.939 -6.878 32.335 1.00 36.93 O ANISOU 373 O LEU A 78 4583 5194 4254 635 -173 368 O ATOM 374 CB LEU A 78 87.060 -8.255 35.175 1.00 17.29 C ANISOU 374 CB LEU A 78 2169 2803 1596 625 -67 338 C ATOM 375 CG LEU A 78 87.888 -9.519 34.954 1.00 27.86 C ANISOU 375 CG LEU A 78 3509 4128 2949 554 -39 343 C ATOM 376 CD1 LEU A 78 89.346 -9.171 34.766 1.00 18.25 C ANISOU 376 CD1 LEU A 78 2313 2879 1742 518 -62 367 C ATOM 377 CD2 LEU A 78 87.715 -10.464 36.131 1.00 22.84 C ANISOU 377 CD2 LEU A 78 2886 3522 2271 545 6 316 C ATOM 378 N ALA A 79 85.173 -5.985 34.268 1.00 37.41 N ANISOU 378 N ALA A 79 4640 5350 4224 791 -151 331 N ATOM 379 CA ALA A 79 83.905 -5.547 33.700 1.00 29.56 C ANISOU 379 CA ALA A 79 3582 4350 3301 855 -168 309 C ATOM 380 C ALA A 79 84.089 -4.483 32.626 1.00 33.77 C ANISOU 380 C ALA A 79 4098 4785 3948 814 -240 328 C ATOM 381 O ALA A 79 83.372 -4.478 31.625 1.00 34.50 O ANISOU 381 O ALA A 79 4149 4843 4117 801 -257 327 O ATOM 382 CB ALA A 79 82.994 -5.027 34.799 1.00 26.96 C ANISOU 382 CB ALA A 79 3217 4067 2959 978 -150 248 C ATOM 383 N VAL A 80 85.058 -3.594 32.822 1.00 33.02 N ANISOU 383 N VAL A 80 4035 4645 3865 788 -284 345 N ATOM 384 CA VAL A 80 85.328 -2.569 31.823 1.00 33.89 C ANISOU 384 CA VAL A 80 4130 4665 4083 744 -353 366 C ATOM 385 C VAL A 80 85.857 -3.226 30.558 1.00 41.03 C ANISOU 385 C VAL A 80 5049 5540 5002 660 -361 395 C ATOM 386 O VAL A 80 85.422 -2.905 29.441 1.00 40.92 O ANISOU 386 O VAL A 80 5002 5497 5049 664 -387 403 O ATOM 387 CB VAL A 80 86.342 -1.520 32.329 1.00 29.66 C ANISOU 387 CB VAL A 80 3627 4094 3549 733 -394 381 C ATOM 388 CG1 VAL A 80 86.799 -0.619 31.190 1.00 28.66 C ANISOU 388 CG1 VAL A 80 3486 3878 3525 670 -463 412 C ATOM 389 CG2 VAL A 80 85.740 -0.698 33.457 1.00 26.06 C ANISOU 389 CG2 VAL A 80 3156 3667 3079 848 -389 337 C ATOM 390 N ALA A 81 86.767 -4.181 30.739 1.00 32.56 N ANISOU 390 N ALA A 81 4017 4506 3847 623 -317 409 N ATOM 391 CA ALA A 81 87.340 -4.868 29.593 1.00 33.48 C ANISOU 391 CA ALA A 81 4136 4634 3952 589 -298 432 C ATOM 392 C ALA A 81 86.276 -5.641 28.814 1.00 40.50 C ANISOU 392 C ALA A 81 4988 5547 4853 602 -270 425 C ATOM 393 O ALA A 81 86.303 -5.661 27.583 1.00 37.95 O ANISOU 393 O ALA A 81 4649 5210 4559 590 -281 442 O ATOM 394 CB ALA A 81 88.456 -5.801 30.038 1.00 31.62 C ANISOU 394 CB ALA A 81 3932 4434 3650 552 -249 440 C ATOM 395 N ASP A 82 85.326 -6.256 29.516 1.00 40.67 N ANISOU 395 N ASP A 82 4996 5604 4853 628 -235 400 N ATOM 396 CA ASP A 82 84.284 -7.012 28.820 1.00 31.99 C ANISOU 396 CA ASP A 82 3862 4527 3765 639 -208 392 C ATOM 397 C ASP A 82 83.196 -6.103 28.249 1.00 49.58 C ANISOU 397 C ASP A 82 6046 6710 6084 672 -258 378 C ATOM 398 O ASP A 82 82.461 -6.495 27.342 1.00 40.90 O ANISOU 398 O ASP A 82 4918 5614 5009 675 -252 379 O ATOM 399 CB ASP A 82 83.665 -8.058 29.749 1.00 28.05 C ANISOU 399 CB ASP A 82 3362 4085 3213 653 -150 368 C ATOM 400 CG ASP A 82 84.577 -9.254 29.972 1.00 51.09 C ANISOU 400 CG ASP A 82 6302 7049 6062 619 -89 379 C ATOM 401 OD1 ASP A 82 85.541 -9.424 29.198 1.00 50.08 O ANISOU 401 OD1 ASP A 82 6178 6913 5938 586 -86 404 O ATOM 402 OD2 ASP A 82 84.325 -10.032 30.917 1.00 48.89 O ANISOU 402 OD2 ASP A 82 6026 6811 5738 627 -44 358 O ATOM 403 N PHE A 83 83.110 -4.883 28.768 1.00 46.82 N ANISOU 403 N PHE A 83 5683 6314 5792 696 -305 365 N ATOM 404 CA PHE A 83 82.134 -3.919 28.277 1.00 38.75 C ANISOU 404 CA PHE A 83 4605 5240 4879 728 -347 347 C ATOM 405 C PHE A 83 82.607 -3.276 26.981 1.00 45.75 C ANISOU 405 C PHE A 83 5493 6085 5805 707 -395 378 C ATOM 406 O PHE A 83 81.812 -3.042 26.069 1.00 40.01 O ANISOU 406 O PHE A 83 4726 5333 5143 718 -414 373 O ATOM 407 CB PHE A 83 81.860 -2.844 29.332 1.00 40.14 C ANISOU 407 CB PHE A 83 4755 5402 5096 784 -359 319 C ATOM 408 CG PHE A 83 80.888 -1.788 28.888 1.00 38.00 C ANISOU 408 CG PHE A 83 4417 5076 4947 819 -388 297 C ATOM 409 CD1 PHE A 83 79.523 -1.995 28.997 1.00 45.80 C ANISOU 409 CD1 PHE A 83 5347 6083 5973 873 -350 251 C ATOM 410 CD2 PHE A 83 81.340 -0.584 28.371 1.00 42.57 C ANISOU 410 CD2 PHE A 83 4986 5581 5608 792 -447 324 C ATOM 411 CE1 PHE A 83 78.626 -1.023 28.593 1.00 49.63 C ANISOU 411 CE1 PHE A 83 5769 6512 6577 897 -366 232 C ATOM 412 CE2 PHE A 83 80.449 0.390 27.964 1.00 37.14 C ANISOU 412 CE2 PHE A 83 4232 4846 5034 820 -461 315 C ATOM 413 CZ PHE A 83 79.090 0.170 28.076 1.00 46.00 C ANISOU 413 CZ PHE A 83 5300 5986 6193 873 -419 269 C ATOM 414 N LEU A 84 83.903 -2.988 26.899 1.00 48.90 N ANISOU 414 N LEU A 84 5936 6476 6168 676 -412 407 N ATOM 415 CA LEU A 84 84.441 -2.344 25.703 1.00 38.81 C ANISOU 415 CA LEU A 84 4660 5158 4927 657 -458 431 C ATOM 416 C LEU A 84 84.292 -3.210 24.451 1.00 44.46 C ANISOU 416 C LEU A 84 5374 5895 5623 639 -435 444 C ATOM 417 O LEU A 84 84.074 -2.693 23.355 1.00 50.04 O ANISOU 417 O LEU A 84 6063 6568 6382 642 -472 449 O ATOM 418 CB LEU A 84 85.913 -1.986 25.907 1.00 48.18 C ANISOU 418 CB LEU A 84 5894 6335 6075 626 -473 455 C ATOM 419 CG LEU A 84 86.224 -0.928 26.967 1.00 51.52 C ANISOU 419 CG LEU A 84 6323 6728 6524 638 -506 451 C ATOM 420 CD1 LEU A 84 87.726 -0.765 27.123 1.00 48.12 C ANISOU 420 CD1 LEU A 84 5943 6293 6046 601 -515 475 C ATOM 421 CD2 LEU A 84 85.572 0.401 26.615 1.00 55.31 C ANISOU 421 CD2 LEU A 84 6754 7149 7114 664 -561 449 C ATOM 422 N ALA A 85 84.411 -4.523 24.619 1.00 40.11 N ANISOU 422 N ALA A 85 4838 5402 4998 622 -371 448 N ATOM 423 CA ALA A 85 84.326 -5.449 23.491 1.00 46.10 C ANISOU 423 CA ALA A 85 5592 6189 5737 603 -339 463 C ATOM 424 C ALA A 85 82.932 -5.483 22.876 1.00 41.81 C ANISOU 424 C ALA A 85 5007 5635 5244 629 -349 447 C ATOM 425 O ALA A 85 82.778 -5.681 21.670 1.00 39.23 O ANISOU 425 O ALA A 85 4670 5304 4932 619 -353 460 O ATOM 426 CB ALA A 85 84.739 -6.842 23.926 1.00 40.72 C ANISOU 426 CB ALA A 85 4926 5570 4976 580 -264 469 C ATOM 427 N CYS A 86 81.921 -5.290 23.715 1.00 37.88 N ANISOU 427 N CYS A 86 4481 5133 4776 663 -352 416 N ATOM 428 CA CYS A 86 80.535 -5.348 23.269 1.00 43.46 C ANISOU 428 CA CYS A 86 5142 5830 5542 689 -357 394 C ATOM 429 C CYS A 86 80.166 -4.153 22.400 1.00 41.68 C ANISOU 429 C CYS A 86 4884 5540 5412 704 -421 390 C ATOM 430 O CYS A 86 79.210 -4.210 21.629 1.00 38.04 O ANISOU 430 O CYS A 86 4387 5066 4999 717 -430 379 O ATOM 431 CB CYS A 86 79.593 -5.432 24.470 1.00 40.83 C ANISOU 431 CB CYS A 86 4778 5507 5227 723 -335 354 C ATOM 432 SG CYS A 86 79.782 -6.937 25.449 1.00 39.14 S ANISOU 432 SG CYS A 86 4598 5373 4901 711 -258 352 S ATOM 433 N LEU A 87 80.915 -3.065 22.541 1.00 41.37 N ANISOU 433 N LEU A 87 4856 5460 5403 702 -466 398 N ATOM 434 CA LEU A 87 80.631 -1.852 21.784 1.00 39.52 C ANISOU 434 CA LEU A 87 4591 5163 5262 717 -528 394 C ATOM 435 C LEU A 87 80.827 -2.057 20.283 1.00 38.20 C ANISOU 435 C LEU A 87 4437 4993 5083 703 -544 409 C ATOM 436 O LEU A 87 80.149 -1.426 19.474 1.00 54.42 O ANISOU 436 O LEU A 87 6461 7010 7204 721 -581 392 O ATOM 437 CB LEU A 87 81.506 -0.701 22.278 1.00 37.04 C ANISOU 437 CB LEU A 87 4290 4810 4973 714 -570 404 C ATOM 438 CG LEU A 87 81.297 -0.322 23.745 1.00 49.88 C ANISOU 438 CG LEU A 87 5896 6436 6620 733 -553 392 C ATOM 439 CD1 LEU A 87 82.143 0.884 24.121 1.00 38.06 C ANISOU 439 CD1 LEU A 87 4411 4902 5146 723 -584 409 C ATOM 440 CD2 LEU A 87 79.823 -0.061 24.028 1.00 36.12 C ANISOU 440 CD2 LEU A 87 4082 4679 4965 769 -533 364 C ATOM 441 N ALA A 88 81.750 -2.938 19.916 1.00 41.30 N ANISOU 441 N ALA A 88 4874 5429 5391 669 -506 437 N ATOM 442 CA ALA A 88 82.009 -3.226 18.509 1.00 53.69 C ANISOU 442 CA ALA A 88 6452 7003 6945 653 -506 456 C ATOM 443 C ALA A 88 81.043 -4.267 17.947 1.00 52.18 C ANISOU 443 C ALA A 88 6238 6844 6744 653 -467 455 C ATOM 444 O ALA A 88 80.996 -4.493 16.738 1.00 51.67 O ANISOU 444 O ALA A 88 6170 6782 6679 644 -467 469 O ATOM 445 CB ALA A 88 83.445 -3.691 18.324 1.00 51.92 C ANISOU 445 CB ALA A 88 6269 6807 6652 613 -475 489 C ATOM 446 N LEU A 89 80.281 -4.901 18.834 1.00 51.72 N ANISOU 446 N LEU A 89 6163 6812 6675 664 -434 439 N ATOM 447 CA LEU A 89 79.381 -5.992 18.452 1.00 42.61 C ANISOU 447 CA LEU A 89 4992 5694 5503 663 -392 436 C ATOM 448 C LEU A 89 78.329 -5.627 17.389 1.00 48.05 C ANISOU 448 C LEU A 89 5644 6352 6263 684 -428 422 C ATOM 449 O LEU A 89 78.139 -6.393 16.441 1.00 52.06 O ANISOU 449 O LEU A 89 6152 6882 6745 669 -404 438 O ATOM 450 CB LEU A 89 78.687 -6.553 19.694 1.00 35.60 C ANISOU 450 CB LEU A 89 4091 4835 4599 680 -356 412 C ATOM 451 CG LEU A 89 78.529 -8.072 19.739 1.00 36.67 C ANISOU 451 CG LEU A 89 4239 5035 4657 661 -288 423 C ATOM 452 CD1 LEU A 89 79.806 -8.747 19.269 1.00 27.79 C ANISOU 452 CD1 LEU A 89 3152 3944 3462 620 -251 461 C ATOM 453 CD2 LEU A 89 78.186 -8.514 21.148 1.00 49.27 C ANISOU 453 CD2 LEU A 89 5836 6663 6223 676 -252 398 C ATOM 454 N PRO A 90 77.628 -4.482 17.542 1.00 50.35 N ANISOU 454 N PRO A 90 5898 6589 6645 718 -481 389 N ATOM 455 CA PRO A 90 76.616 -4.177 16.520 1.00 48.72 C ANISOU 455 CA PRO A 90 5653 6354 6503 739 -511 369 C ATOM 456 C PRO A 90 77.184 -4.076 15.105 1.00 50.68 C ANISOU 456 C PRO A 90 5927 6600 6729 726 -530 393 C ATOM 457 O PRO A 90 76.500 -4.444 14.148 1.00 50.07 O ANISOU 457 O PRO A 90 5833 6528 6662 731 -527 391 O ATOM 458 CB PRO A 90 76.057 -2.822 16.971 1.00 50.87 C ANISOU 458 CB PRO A 90 5888 6569 6870 766 -553 331 C ATOM 459 CG PRO A 90 76.303 -2.784 18.430 1.00 50.63 C ANISOU 459 CG PRO A 90 5853 6545 6839 767 -532 331 C ATOM 460 CD PRO A 90 77.613 -3.480 18.623 1.00 49.63 C ANISOU 460 CD PRO A 90 5788 6462 6607 738 -508 367 C ATOM 461 N ALA A 91 78.416 -3.591 14.976 1.00 49.66 N ANISOU 461 N ALA A 91 5834 6465 6569 711 -543 414 N ATOM 462 CA ALA A 91 79.038 -3.468 13.665 1.00 36.62 C ANISOU 462 CA ALA A 91 4203 4815 4896 698 -550 439 C ATOM 463 C ALA A 91 79.341 -4.832 13.053 1.00 45.11 C ANISOU 463 C ALA A 91 5290 5938 5910 657 -490 479 C ATOM 464 O ALA A 91 79.117 -5.051 11.860 1.00 53.66 O ANISOU 464 O ALA A 91 6366 7025 6998 651 -488 492 O ATOM 465 CB ALA A 91 80.307 -2.638 13.761 1.00 32.37 C ANISOU 465 CB ALA A 91 3697 4261 4340 692 -573 451 C ATOM 466 N LEU A 92 79.848 -5.746 13.876 1.00 44.92 N ANISOU 466 N LEU A 92 5284 5953 5829 629 -439 495 N ATOM 467 CA LEU A 92 80.130 -7.104 13.428 1.00 52.02 C ANISOU 467 CA LEU A 92 6192 6904 6669 594 -375 525 C ATOM 468 C LEU A 92 78.842 -7.821 13.047 1.00 46.17 C ANISOU 468 C LEU A 92 5426 6178 5940 606 -359 515 C ATOM 469 O LEU A 92 78.808 -8.595 12.087 1.00 51.93 O ANISOU 469 O LEU A 92 6153 6931 6649 585 -329 537 O ATOM 470 CB LEU A 92 80.866 -7.888 14.521 1.00 48.62 C ANISOU 470 CB LEU A 92 5783 6516 6175 571 -322 535 C ATOM 471 CG LEU A 92 82.082 -7.197 15.143 1.00 42.82 C ANISOU 471 CG LEU A 92 5074 5767 5431 561 -338 540 C ATOM 472 CD1 LEU A 92 82.687 -8.042 16.260 1.00 39.56 C ANISOU 472 CD1 LEU A 92 4677 5397 4956 542 -283 543 C ATOM 473 CD2 LEU A 92 83.122 -6.886 14.081 1.00 36.10 C ANISOU 473 CD2 LEU A 92 4232 4904 4581 536 -347 567 C ATOM 474 N PHE A 93 77.779 -7.524 13.791 1.00 40.63 N ANISOU 474 N PHE A 93 4699 5459 5278 640 -380 479 N ATOM 475 CA PHE A 93 76.463 -8.090 13.535 1.00 45.40 C ANISOU 475 CA PHE A 93 5274 6072 5904 656 -370 461 C ATOM 476 C PHE A 93 75.974 -7.621 12.172 1.00 55.42 C ANISOU 476 C PHE A 93 6525 7311 7222 667 -408 460 C ATOM 477 O PHE A 93 75.558 -8.424 11.328 1.00 45.39 O ANISOU 477 O PHE A 93 5249 6062 5935 655 -384 474 O ATOM 478 CB PHE A 93 75.488 -7.670 14.644 1.00 45.40 C ANISOU 478 CB PHE A 93 5242 6052 5955 691 -388 417 C ATOM 479 CG PHE A 93 74.097 -8.227 14.495 1.00 61.73 C ANISOU 479 CG PHE A 93 7274 8127 8054 709 -376 393 C ATOM 480 CD1 PHE A 93 73.162 -7.597 13.688 1.00 53.24 C ANISOU 480 CD1 PHE A 93 6160 7011 7058 734 -420 368 C ATOM 481 CD2 PHE A 93 73.714 -9.363 15.189 1.00 59.71 C ANISOU 481 CD2 PHE A 93 7021 7918 7749 702 -322 391 C ATOM 482 CE1 PHE A 93 71.883 -8.103 13.558 1.00 52.03 C ANISOU 482 CE1 PHE A 93 5969 6861 6938 749 -409 344 C ATOM 483 CE2 PHE A 93 72.434 -9.872 15.064 1.00 50.62 C ANISOU 483 CE2 PHE A 93 5835 6771 6627 718 -311 367 C ATOM 484 CZ PHE A 93 71.518 -9.241 14.247 1.00 55.06 C ANISOU 484 CZ PHE A 93 6356 7290 7274 741 -354 344 C ATOM 485 N THR A 94 76.073 -6.312 11.956 1.00 41.90 N ANISOU 485 N THR A 94 4805 5552 5564 691 -467 441 N ATOM 486 CA THR A 94 75.619 -5.703 10.716 1.00 41.45 C ANISOU 486 CA THR A 94 4731 5468 5549 711 -506 432 C ATOM 487 C THR A 94 76.410 -6.241 9.533 1.00 61.41 C ANISOU 487 C THR A 94 7283 8020 8032 674 -479 479 C ATOM 488 O THR A 94 75.856 -6.480 8.457 1.00 53.05 O ANISOU 488 O THR A 94 6210 6961 6985 676 -481 485 O ATOM 489 CB THR A 94 75.765 -4.165 10.765 1.00 53.77 C ANISOU 489 CB THR A 94 6287 6987 7156 749 -566 402 C ATOM 490 OG1 THR A 94 74.975 -3.639 11.838 1.00 55.05 O ANISOU 490 OG1 THR A 94 6421 7125 7369 779 -583 353 O ATOM 491 CG2 THR A 94 75.324 -3.530 9.454 1.00 52.46 C ANISOU 491 CG2 THR A 94 6109 6811 7014 778 -595 393 C ATOM 492 N SER A 95 77.703 -6.459 9.747 1.00 53.19 N ANISOU 492 N SER A 95 6273 6996 6941 640 -453 512 N ATOM 493 CA SER A 95 78.556 -6.962 8.683 1.00 37.38 C ANISOU 493 CA SER A 95 4285 5015 4904 602 -424 554 C ATOM 494 C SER A 95 78.213 -8.406 8.337 1.00 47.52 C ANISOU 494 C SER A 95 5563 6341 6149 576 -367 573 C ATOM 495 O SER A 95 78.180 -8.772 7.162 1.00 42.51 O ANISOU 495 O SER A 95 4923 5714 5514 560 -356 595 O ATOM 496 CB SER A 95 80.030 -6.846 9.072 1.00 41.30 C ANISOU 496 CB SER A 95 4808 5519 5363 572 -407 577 C ATOM 497 OG SER A 95 80.864 -7.339 8.038 1.00 35.55 O ANISOU 497 OG SER A 95 4085 4810 4612 534 -377 614 O ATOM 498 N ILE A 96 77.951 -9.226 9.351 1.00 52.83 N ANISOU 498 N ILE A 96 6240 7046 6789 573 -328 566 N ATOM 499 CA ILE A 96 77.572 -10.609 9.082 1.00 55.24 C ANISOU 499 CA ILE A 96 6541 7396 7053 553 -272 581 C ATOM 500 C ILE A 96 76.209 -10.691 8.391 1.00 55.48 C ANISOU 500 C ILE A 96 6545 7412 7122 577 -293 565 C ATOM 501 O ILE A 96 75.989 -11.568 7.553 1.00 57.92 O ANISOU 501 O ILE A 96 6850 7746 7411 559 -262 584 O ATOM 502 CB ILE A 96 77.562 -11.454 10.372 1.00 51.25 C ANISOU 502 CB ILE A 96 6044 6930 6498 548 -224 573 C ATOM 503 CG1 ILE A 96 78.974 -11.515 10.955 1.00 52.26 C ANISOU 503 CG1 ILE A 96 6195 7077 6586 521 -196 590 C ATOM 504 CG2 ILE A 96 77.059 -12.865 10.097 1.00 38.53 C ANISOU 504 CG2 ILE A 96 4427 5366 4845 532 -167 584 C ATOM 505 CD1 ILE A 96 79.112 -12.441 12.133 1.00 46.52 C ANISOU 505 CD1 ILE A 96 5476 6396 5802 513 -141 584 C ATOM 506 N VAL A 97 75.307 -9.765 8.709 1.00 44.81 N ANISOU 506 N VAL A 97 5173 6021 5831 617 -346 526 N ATOM 507 CA VAL A 97 73.997 -9.762 8.058 1.00 53.87 C ANISOU 507 CA VAL A 97 6291 7153 7026 643 -370 504 C ATOM 508 C VAL A 97 74.143 -9.472 6.561 1.00 66.62 C ANISOU 508 C VAL A 97 7902 8753 8656 636 -389 524 C ATOM 509 O VAL A 97 73.370 -9.967 5.736 1.00 46.68 O ANISOU 509 O VAL A 97 5362 6234 6141 639 -385 526 O ATOM 510 CB VAL A 97 73.039 -8.736 8.706 1.00 49.79 C ANISOU 510 CB VAL A 97 5741 6594 6582 690 -422 451 C ATOM 511 CG1 VAL A 97 71.737 -8.634 7.925 1.00 54.20 C ANISOU 511 CG1 VAL A 97 6263 7134 7195 718 -448 424 C ATOM 512 CG2 VAL A 97 72.748 -9.123 10.146 1.00 53.02 C ANISOU 512 CG2 VAL A 97 6145 7019 6981 696 -398 431 C ATOM 513 N GLN A 98 75.171 -8.704 6.217 1.00 47.19 N ANISOU 513 N GLN A 98 5458 6276 6196 627 -408 541 N ATOM 514 CA GLN A 98 75.405 -8.306 4.836 1.00 41.81 C ANISOU 514 CA GLN A 98 4774 5581 5530 621 -426 561 C ATOM 515 C GLN A 98 76.424 -9.214 4.154 1.00 49.54 C ANISOU 515 C GLN A 98 5770 6593 6458 571 -376 609 C ATOM 516 O GLN A 98 77.157 -8.776 3.267 1.00 48.80 O ANISOU 516 O GLN A 98 5682 6490 6371 556 -385 631 O ATOM 517 CB GLN A 98 75.874 -6.852 4.778 1.00 35.47 C ANISOU 517 CB GLN A 98 3975 4742 4761 644 -476 548 C ATOM 518 CG GLN A 98 74.910 -5.871 5.429 1.00 46.49 C ANISOU 518 CG GLN A 98 5348 6108 6208 699 -524 495 C ATOM 519 CD GLN A 98 75.336 -4.426 5.259 1.00 50.02 C ANISOU 519 CD GLN A 98 5798 6530 6679 728 -567 485 C ATOM 520 OE1 GLN A 98 76.293 -4.127 4.545 1.00 52.56 O ANISOU 520 OE1 GLN A 98 6136 6849 6985 705 -565 519 O ATOM 521 NE2 GLN A 98 74.623 -3.518 5.917 1.00 51.94 N ANISOU 521 NE2 GLN A 98 6022 6758 6957 781 -600 437 N ATOM 522 N HIS A 99 76.461 -10.474 4.581 1.00 49.95 N ANISOU 522 N HIS A 99 5828 6687 6462 547 -320 621 N ATOM 523 CA HIS A 99 77.368 -11.476 4.023 1.00 43.18 C ANISOU 523 CA HIS A 99 4981 5868 5558 501 -264 660 C ATOM 524 C HIS A 99 78.824 -11.026 4.074 1.00 49.84 C ANISOU 524 C HIS A 99 5838 6709 6389 476 -260 680 C ATOM 525 O HIS A 99 79.543 -11.090 3.077 1.00 51.41 O ANISOU 525 O HIS A 99 6035 6911 6588 449 -250 706 O ATOM 526 CB HIS A 99 76.963 -11.817 2.588 1.00 53.86 C ANISOU 526 CB HIS A 99 6319 7221 6924 492 -262 678 C ATOM 527 CG HIS A 99 75.573 -12.357 2.474 1.00 61.51 C ANISOU 527 CG HIS A 99 7273 8195 7904 514 -263 660 C ATOM 528 ND1 HIS A 99 74.455 -11.567 2.635 1.00 65.98 N ANISOU 528 ND1 HIS A 99 7823 8725 8521 557 -316 624 N ATOM 529 CD2 HIS A 99 75.118 -13.610 2.237 1.00 57.85 C ANISOU 529 CD2 HIS A 99 6806 7767 7408 499 -218 671 C ATOM 530 CE1 HIS A 99 73.371 -12.308 2.492 1.00 70.53 C ANISOU 530 CE1 HIS A 99 8385 9314 9099 567 -304 614 C ATOM 531 NE2 HIS A 99 73.745 -13.552 2.250 1.00 64.99 N ANISOU 531 NE2 HIS A 99 7693 8655 8343 532 -245 643 N ATOM 532 N HIS A 100 79.232 -10.563 5.253 1.00 57.46 N ANISOU 532 N HIS A 100 6817 7669 7348 485 -269 664 N ATOM 533 CA HIS A 100 80.606 -10.151 5.534 1.00 39.27 C ANISOU 533 CA HIS A 100 4527 5362 5030 463 -265 678 C ATOM 534 C HIS A 100 81.087 -8.996 4.657 1.00 49.86 C ANISOU 534 C HIS A 100 5869 6665 6409 467 -312 686 C ATOM 535 O HIS A 100 82.284 -8.855 4.409 1.00 56.04 O ANISOU 535 O HIS A 100 6659 7452 7183 439 -302 707 O ATOM 536 CB HIS A 100 81.549 -11.349 5.390 1.00 45.47 C ANISOU 536 CB HIS A 100 5312 6196 5770 418 -198 705 C ATOM 537 CG HIS A 100 81.090 -12.563 6.135 1.00 58.43 C ANISOU 537 CG HIS A 100 6949 7880 7370 414 -145 698 C ATOM 538 ND1 HIS A 100 81.215 -12.688 7.502 1.00 50.86 N ANISOU 538 ND1 HIS A 100 6002 6936 6386 422 -130 681 N ATOM 539 CD2 HIS A 100 80.496 -13.701 5.706 1.00 59.83 C ANISOU 539 CD2 HIS A 100 7114 8091 7527 405 -103 705 C ATOM 540 CE1 HIS A 100 80.722 -13.853 7.882 1.00 60.20 C ANISOU 540 CE1 HIS A 100 7179 8160 7533 418 -79 678 C ATOM 541 NE2 HIS A 100 80.280 -14.487 6.812 1.00 63.20 N ANISOU 541 NE2 HIS A 100 7545 8553 7915 407 -62 692 N ATOM 542 N HIS A 101 80.148 -8.177 4.189 1.00 55.31 N ANISOU 542 N HIS A 101 6549 7322 7145 502 -362 668 N ATOM 543 CA HIS A 101 80.479 -6.893 3.576 1.00 48.99 C ANISOU 543 CA HIS A 101 5749 6484 6381 517 -411 668 C ATOM 544 C HIS A 101 80.831 -5.876 4.665 1.00 48.67 C ANISOU 544 C HIS A 101 5722 6419 6350 541 -444 645 C ATOM 545 O HIS A 101 80.205 -5.861 5.726 1.00 49.64 O ANISOU 545 O HIS A 101 5845 6540 6475 566 -452 616 O ATOM 546 CB HIS A 101 79.309 -6.401 2.718 1.00 41.10 C ANISOU 546 CB HIS A 101 4729 5461 5425 551 -448 652 C ATOM 547 CG HIS A 101 79.488 -5.017 2.179 1.00 40.75 C ANISOU 547 CG HIS A 101 4682 5383 5418 574 -496 648 C ATOM 548 ND1 HIS A 101 80.420 -4.708 1.211 1.00 48.52 N ANISOU 548 ND1 HIS A 101 5669 6363 6403 547 -495 680 N ATOM 549 CD2 HIS A 101 78.848 -3.859 2.467 1.00 47.11 C ANISOU 549 CD2 HIS A 101 5477 6161 6260 623 -542 615 C ATOM 550 CE1 HIS A 101 80.349 -3.419 0.930 1.00 44.18 C ANISOU 550 CE1 HIS A 101 5114 5784 5889 576 -538 671 C ATOM 551 NE2 HIS A 101 79.403 -2.881 1.678 1.00 49.88 N ANISOU 551 NE2 HIS A 101 5828 6494 6631 624 -565 632 N ATOM 552 N TRP A 102 81.818 -5.021 4.407 1.00 43.35 N ANISOU 552 N TRP A 102 5059 5729 5684 533 -464 658 N ATOM 553 CA TRP A 102 82.236 -4.040 5.409 1.00 49.84 C ANISOU 553 CA TRP A 102 5896 6530 6512 555 -494 638 C ATOM 554 C TRP A 102 82.062 -2.600 4.926 1.00 44.35 C ANISOU 554 C TRP A 102 5194 5800 5857 591 -545 627 C ATOM 555 O TRP A 102 82.841 -2.114 4.105 1.00 44.37 O ANISOU 555 O TRP A 102 5198 5795 5866 573 -551 653 O ATOM 556 CB TRP A 102 83.690 -4.279 5.826 1.00 36.11 C ANISOU 556 CB TRP A 102 4177 4805 4738 515 -467 662 C ATOM 557 CG TRP A 102 84.087 -3.481 7.033 1.00 40.34 C ANISOU 557 CG TRP A 102 4731 5323 5272 535 -492 641 C ATOM 558 CD1 TRP A 102 84.783 -2.307 7.046 1.00 48.60 C ANISOU 558 CD1 TRP A 102 5788 6344 6332 546 -526 641 C ATOM 559 CD2 TRP A 102 83.795 -3.789 8.403 1.00 38.08 C ANISOU 559 CD2 TRP A 102 4455 5044 4969 547 -485 618 C ATOM 560 NE1 TRP A 102 84.950 -1.870 8.338 1.00 54.31 N ANISOU 560 NE1 TRP A 102 6529 7059 7049 565 -541 618 N ATOM 561 CE2 TRP A 102 84.353 -2.762 9.190 1.00 50.30 C ANISOU 561 CE2 TRP A 102 6020 6569 6523 565 -518 604 C ATOM 562 CE3 TRP A 102 83.121 -4.836 9.040 1.00 45.22 C ANISOU 562 CE3 TRP A 102 5353 5975 5853 543 -452 609 C ATOM 563 CZ2 TRP A 102 84.257 -2.750 10.581 1.00 40.36 C ANISOU 563 CZ2 TRP A 102 4774 5309 5254 579 -521 580 C ATOM 564 CZ3 TRP A 102 83.027 -4.822 10.422 1.00 41.36 C ANISOU 564 CZ3 TRP A 102 4874 5487 5354 556 -452 587 C ATOM 565 CH2 TRP A 102 83.593 -3.786 11.177 1.00 33.81 C ANISOU 565 CH2 TRP A 102 3935 4503 4407 573 -488 573 C ATOM 566 N PRO A 103 81.031 -1.914 5.441 1.00 38.66 N ANISOU 566 N PRO A 103 4461 5063 5164 642 -579 588 N ATOM 567 CA PRO A 103 80.706 -0.538 5.056 1.00 39.76 C ANISOU 567 CA PRO A 103 4587 5180 5340 684 -618 576 C ATOM 568 C PRO A 103 81.255 0.536 6.000 1.00 46.27 C ANISOU 568 C PRO A 103 5424 5992 6165 709 -640 562 C ATOM 569 O PRO A 103 80.948 1.713 5.811 1.00 55.40 O ANISOU 569 O PRO A 103 6564 7136 7349 745 -664 555 O ATOM 570 CB PRO A 103 79.180 -0.539 5.094 1.00 40.62 C ANISOU 570 CB PRO A 103 4667 5290 5476 730 -631 540 C ATOM 571 CG PRO A 103 78.863 -1.468 6.225 1.00 38.77 C ANISOU 571 CG PRO A 103 4440 5067 5225 725 -614 517 C ATOM 572 CD PRO A 103 79.950 -2.526 6.234 1.00 43.70 C ANISOU 572 CD PRO A 103 5089 5709 5806 663 -573 556 C ATOM 573 N PHE A 104 82.035 0.144 7.003 1.00 53.60 N ANISOU 573 N PHE A 104 6377 6925 7062 687 -627 562 N ATOM 574 CA PHE A 104 82.465 1.088 8.034 1.00 39.03 C ANISOU 574 CA PHE A 104 4546 5070 5215 714 -647 545 C ATOM 575 C PHE A 104 83.840 1.720 7.807 1.00 50.67 C ANISOU 575 C PHE A 104 6039 6536 6679 687 -649 576 C ATOM 576 O PHE A 104 84.252 2.599 8.565 1.00 59.44 O ANISOU 576 O PHE A 104 7160 7637 7787 709 -665 567 O ATOM 577 CB PHE A 104 82.439 0.395 9.392 1.00 39.97 C ANISOU 577 CB PHE A 104 4681 5194 5312 710 -636 522 C ATOM 578 CG PHE A 104 81.125 -0.253 9.708 1.00 44.47 C ANISOU 578 CG PHE A 104 5229 5770 5899 730 -634 491 C ATOM 579 CD1 PHE A 104 80.044 0.511 10.117 1.00 33.85 C ANISOU 579 CD1 PHE A 104 3860 4418 4583 787 -655 447 C ATOM 580 CD2 PHE A 104 80.967 -1.623 9.587 1.00 40.66 C ANISOU 580 CD2 PHE A 104 4745 5306 5398 689 -597 508 C ATOM 581 CE1 PHE A 104 78.831 -0.081 10.405 1.00 36.73 C ANISOU 581 CE1 PHE A 104 4201 4785 4969 798 -649 415 C ATOM 582 CE2 PHE A 104 79.756 -2.222 9.875 1.00 44.93 C ANISOU 582 CE2 PHE A 104 5262 5851 5956 705 -592 483 C ATOM 583 CZ PHE A 104 78.686 -1.450 10.285 1.00 39.75 C ANISOU 583 CZ PHE A 104 4581 5178 5343 762 -628 434 C ATOM 584 N GLY A 105 84.547 1.284 6.771 1.00 50.49 N ANISOU 584 N GLY A 105 6633 6347 6203 -131 -134 -11 N ATOM 585 CA GLY A 105 85.822 1.888 6.422 1.00 44.64 C ANISOU 585 CA GLY A 105 5897 5608 5455 -136 -133 18 C ATOM 586 C GLY A 105 87.027 1.345 7.168 1.00 62.82 C ANISOU 586 C GLY A 105 8200 7901 7769 -140 -114 24 C ATOM 587 O GLY A 105 86.901 0.487 8.049 1.00 65.61 O ANISOU 587 O GLY A 105 8550 8244 8136 -139 -101 6 O ATOM 588 N GLY A 106 88.201 1.869 6.825 1.00 60.26 N ANISOU 588 N GLY A 106 7879 7578 7439 -144 -112 49 N ATOM 589 CA GLY A 106 89.457 1.349 7.333 1.00 72.01 C ANISOU 589 CA GLY A 106 9368 9060 8935 -149 -93 57 C ATOM 590 C GLY A 106 89.746 1.561 8.807 1.00 59.82 C ANISOU 590 C GLY A 106 7822 7492 7413 -147 -93 60 C ATOM 591 O GLY A 106 90.358 0.701 9.442 1.00 69.10 O ANISOU 591 O GLY A 106 8995 8661 8597 -150 -74 54 O ATOM 592 N ALA A 107 89.312 2.690 9.361 1.00 65.74 N ANISOU 592 N ALA A 107 8576 8230 8175 -144 -113 69 N ATOM 593 CA ALA A 107 89.555 2.964 10.774 1.00 65.34 C ANISOU 593 CA ALA A 107 8524 8157 8144 -144 -114 72 C ATOM 594 C ALA A 107 88.767 1.993 11.640 1.00 55.22 C ANISOU 594 C ALA A 107 7238 6868 6874 -140 -105 44 C ATOM 595 O ALA A 107 89.313 1.374 12.556 1.00 52.21 O ANISOU 595 O ALA A 107 6854 6478 6505 -142 -91 41 O ATOM 596 CB ALA A 107 89.192 4.402 11.115 1.00 40.91 C ANISOU 596 CB ALA A 107 5433 5051 5059 -141 -137 86 C ATOM 597 N ALA A 108 87.482 1.851 11.330 1.00 58.58 N ANISOU 597 N ALA A 108 7662 7298 7296 -136 -113 25 N ATOM 598 CA ALA A 108 86.637 0.903 12.040 1.00 48.74 C ANISOU 598 CA ALA A 108 6412 6047 6060 -132 -104 -2 C ATOM 599 C ALA A 108 87.123 -0.518 11.793 1.00 52.21 C ANISOU 599 C ALA A 108 6847 6495 6495 -135 -79 -14 C ATOM 600 O ALA A 108 87.027 -1.375 12.677 1.00 48.47 O ANISOU 600 O ALA A 108 6370 6013 6035 -133 -65 -29 O ATOM 601 CB ALA A 108 85.189 1.056 11.614 1.00 46.02 C ANISOU 601 CB ALA A 108 6066 5707 5712 -127 -118 -19 C ATOM 602 N CYS A 109 87.660 -0.757 10.598 1.00 51.21 N ANISOU 602 N CYS A 109 6720 6386 6349 -139 -72 -8 N ATOM 603 CA CYS A 109 88.211 -2.066 10.268 1.00 42.93 C ANISOU 603 CA CYS A 109 5669 5347 5297 -142 -47 -18 C ATOM 604 C CYS A 109 89.414 -2.400 11.145 1.00 53.09 C ANISOU 604 C CYS A 109 6953 6622 6595 -145 -31 -7 C ATOM 605 O CYS A 109 89.586 -3.543 11.562 1.00 45.11 O ANISOU 605 O CYS A 109 5938 5609 5592 -145 -10 -20 O ATOM 606 CB CYS A 109 88.610 -2.120 8.790 1.00 53.80 C ANISOU 606 CB CYS A 109 7046 6744 6650 -146 -44 -12 C ATOM 607 SG CYS A 109 89.327 -3.690 8.245 1.00 46.48 S ANISOU 607 SG CYS A 109 6115 5830 5717 -152 -12 -24 S ATOM 608 N SER A 110 90.225 -1.392 11.450 1.00 42.97 N ANISOU 608 N SER A 110 5677 5333 5318 -147 -41 19 N ATOM 609 CA SER A 110 91.409 -1.598 12.277 1.00 46.71 C ANISOU 609 CA SER A 110 6149 5797 5803 -150 -29 32 C ATOM 610 C SER A 110 91.068 -1.685 13.762 1.00 44.91 C ANISOU 610 C SER A 110 5918 5551 5595 -146 -29 24 C ATOM 611 O SER A 110 91.715 -2.416 14.514 1.00 45.63 O ANISOU 611 O SER A 110 6005 5636 5695 -147 -12 24 O ATOM 612 CB SER A 110 92.425 -0.478 12.038 1.00 44.15 C ANISOU 612 CB SER A 110 5829 5471 5474 -154 -39 62 C ATOM 613 OG SER A 110 92.995 -0.575 10.743 1.00 68.20 O ANISOU 613 OG SER A 110 8876 8534 8502 -158 -33 71 O ATOM 614 N ILE A 111 90.042 -0.952 14.181 1.00 33.53 N ANISOU 614 N ILE A 111 4479 4102 4159 -142 -48 18 N ATOM 615 CA ILE A 111 89.724 -0.863 15.600 1.00 34.06 C ANISOU 615 CA ILE A 111 4544 4152 4245 -139 -51 11 C ATOM 616 C ILE A 111 88.711 -1.900 16.083 1.00 50.16 C ANISOU 616 C ILE A 111 6579 6189 6292 -134 -41 -17 C ATOM 617 O ILE A 111 89.024 -2.717 16.949 1.00 44.23 O ANISOU 617 O ILE A 111 5823 5430 5551 -134 -25 -22 O ATOM 618 CB ILE A 111 89.190 0.532 15.955 1.00 35.85 C ANISOU 618 CB ILE A 111 4775 4368 4477 -137 -76 20 C ATOM 619 CG1 ILE A 111 90.254 1.589 15.667 1.00 30.96 C ANISOU 619 CG1 ILE A 111 4161 3749 3854 -142 -85 48 C ATOM 620 CG2 ILE A 111 88.780 0.591 17.417 1.00 42.07 C ANISOU 620 CG2 ILE A 111 5562 5139 5283 -134 -79 11 C ATOM 621 CD1 ILE A 111 89.800 2.992 15.964 1.00 47.88 C ANISOU 621 CD1 ILE A 111 6308 5882 6004 -141 -109 57 C ATOM 622 N LEU A 112 87.501 -1.864 15.530 1.00 55.15 N ANISOU 622 N LEU A 112 7212 6826 6919 -131 -51 -33 N ATOM 623 CA LEU A 112 86.391 -2.642 16.090 1.00 50.65 C ANISOU 623 CA LEU A 112 6637 6250 6358 -126 -45 -60 C ATOM 624 C LEU A 112 86.605 -4.168 16.173 1.00 40.29 C ANISOU 624 C LEU A 112 5318 4941 5048 -126 -18 -75 C ATOM 625 O LEU A 112 86.358 -4.752 17.228 1.00 56.86 O ANISOU 625 O LEU A 112 7413 7029 7162 -123 -8 -87 O ATOM 626 CB LEU A 112 85.110 -2.343 15.303 1.00 41.88 C ANISOU 626 CB LEU A 112 5527 5146 5239 -122 -60 -74 C ATOM 627 CG LEU A 112 84.707 -0.869 15.288 1.00 52.47 C ANISOU 627 CG LEU A 112 6874 6482 6581 -121 -86 -61 C ATOM 628 CD1 LEU A 112 83.419 -0.676 14.509 1.00 51.78 C ANISOU 628 CD1 LEU A 112 6786 6403 6485 -117 -100 -75 C ATOM 629 CD2 LEU A 112 84.570 -0.338 16.708 1.00 49.87 C ANISOU 629 CD2 LEU A 112 6546 6134 6270 -119 -94 -59 C ATOM 630 N PRO A 113 87.057 -4.820 15.080 1.00 45.97 N ANISOU 630 N PRO A 113 6037 5676 5755 -129 -5 -76 N ATOM 631 CA PRO A 113 87.321 -6.264 15.163 1.00 47.22 C ANISOU 631 CA PRO A 113 6188 5837 5917 -130 23 -91 C ATOM 632 C PRO A 113 88.365 -6.648 16.214 1.00 48.16 C ANISOU 632 C PRO A 113 6304 5945 6049 -131 38 -78 C ATOM 633 O PRO A 113 88.318 -7.760 16.742 1.00 55.98 O ANISOU 633 O PRO A 113 7288 6931 7051 -129 58 -92 O ATOM 634 CB PRO A 113 87.818 -6.605 13.753 1.00 45.93 C ANISOU 634 CB PRO A 113 6025 5692 5736 -135 31 -88 C ATOM 635 CG PRO A 113 87.218 -5.566 12.889 1.00 53.29 C ANISOU 635 CG PRO A 113 6962 6632 6653 -135 8 -84 C ATOM 636 CD PRO A 113 87.293 -4.322 13.714 1.00 52.44 C ANISOU 636 CD PRO A 113 6859 6511 6554 -133 -13 -66 C ATOM 637 N SER A 114 89.321 -5.760 16.464 1.00 38.37 N ANISOU 637 N SER A 114 5069 4702 4810 -134 29 -53 N ATOM 638 CA SER A 114 90.420 -6.040 17.386 1.00 34.42 C ANISOU 638 CA SER A 114 4565 4194 4320 -135 41 -39 C ATOM 639 C SER A 114 90.101 -5.777 18.865 1.00 46.70 C ANISOU 639 C SER A 114 6120 5733 5892 -132 35 -40 C ATOM 640 O SER A 114 90.907 -6.106 19.744 1.00 38.93 O ANISOU 640 O SER A 114 5132 4743 4918 -132 46 -30 O ATOM 641 CB SER A 114 91.650 -5.227 16.976 1.00 36.89 C ANISOU 641 CB SER A 114 4882 4510 4624 -141 35 -11 C ATOM 642 OG SER A 114 92.157 -5.674 15.729 1.00 50.82 O ANISOU 642 OG SER A 114 6646 6289 6375 -145 47 -8 O ATOM 643 N LEU A 115 88.940 -5.186 19.146 1.00 32.98 N ANISOU 643 N LEU A 115 4385 3990 4157 -128 18 -52 N ATOM 644 CA LEU A 115 88.555 -4.917 20.531 1.00 41.73 C ANISOU 644 CA LEU A 115 5492 5083 5280 -124 11 -55 C ATOM 645 C LEU A 115 88.385 -6.213 21.317 1.00 37.26 C ANISOU 645 C LEU A 115 4918 4512 4726 -120 34 -70 C ATOM 646 O LEU A 115 88.625 -6.251 22.523 1.00 35.09 O ANISOU 646 O LEU A 115 4642 4228 4464 -119 36 -66 O ATOM 647 CB LEU A 115 87.263 -4.096 20.598 1.00 29.41 C ANISOU 647 CB LEU A 115 3935 3517 3721 -120 -10 -66 C ATOM 648 CG LEU A 115 87.347 -2.624 20.187 1.00 32.08 C ANISOU 648 CG LEU A 115 4281 3856 4053 -123 -35 -50 C ATOM 649 CD1 LEU A 115 86.013 -1.919 20.401 1.00 30.08 C ANISOU 649 CD1 LEU A 115 4031 3595 3805 -118 -54 -63 C ATOM 650 CD2 LEU A 115 88.458 -1.914 20.946 1.00 30.50 C ANISOU 650 CD2 LEU A 115 4082 3648 3858 -127 -39 -27 C ATOM 651 N ILE A 116 87.968 -7.270 20.631 1.00 38.11 N ANISOU 651 N ILE A 116 5022 4627 4831 -119 49 -88 N ATOM 652 CA ILE A 116 87.863 -8.583 21.251 1.00 36.59 C ANISOU 652 CA ILE A 116 4822 4431 4651 -115 73 -101 C ATOM 653 C ILE A 116 89.249 -9.155 21.579 1.00 38.73 C ANISOU 653 C ILE A 116 5088 4702 4925 -118 92 -84 C ATOM 654 O ILE A 116 89.404 -9.925 22.532 1.00 32.96 O ANISOU 654 O ILE A 116 4351 3965 4207 -115 108 -87 O ATOM 655 CB ILE A 116 87.071 -9.566 20.350 1.00 35.28 C ANISOU 655 CB ILE A 116 4652 4272 4481 -114 86 -126 C ATOM 656 CG1 ILE A 116 86.618 -10.789 21.150 1.00 29.01 C ANISOU 656 CG1 ILE A 116 3850 3471 3703 -109 107 -144 C ATOM 657 CG2 ILE A 116 87.877 -9.959 19.115 1.00 18.93 C ANISOU 657 CG2 ILE A 116 2580 2215 2397 -119 98 -119 C ATOM 658 CD1 ILE A 116 85.746 -10.442 22.336 1.00 25.28 C ANISOU 658 CD1 ILE A 116 3377 2984 3242 -103 96 -152 C ATOM 659 N LEU A 117 90.256 -8.767 20.798 1.00 33.19 N ANISOU 659 N LEU A 117 4389 4009 4212 -124 91 -65 N ATOM 660 CA LEU A 117 91.624 -9.211 21.047 1.00 32.89 C ANISOU 660 CA LEU A 117 4346 3972 4177 -128 108 -47 C ATOM 661 C LEU A 117 92.210 -8.461 22.237 1.00 33.50 C ANISOU 661 C LEU A 117 4426 4041 4263 -128 97 -28 C ATOM 662 O LEU A 117 92.893 -9.046 23.096 1.00 32.77 O ANISOU 662 O LEU A 117 4327 3945 4180 -127 112 -21 O ATOM 663 CB LEU A 117 92.490 -9.008 19.803 1.00 36.72 C ANISOU 663 CB LEU A 117 4834 4469 4647 -134 109 -33 C ATOM 664 CG LEU A 117 92.070 -9.813 18.570 1.00 58.15 C ANISOU 664 CG LEU A 117 7548 7195 7353 -135 122 -51 C ATOM 665 CD1 LEU A 117 92.881 -9.397 17.353 1.00 71.45 C ANISOU 665 CD1 LEU A 117 9236 8891 9021 -141 120 -36 C ATOM 666 CD2 LEU A 117 92.210 -11.308 18.827 1.00 52.76 C ANISOU 666 CD2 LEU A 117 6855 6510 6681 -133 152 -63 C ATOM 667 N LEU A 118 91.916 -7.163 22.294 1.00 23.68 N ANISOU 667 N LEU A 118 3189 2794 3014 -129 72 -22 N ATOM 668 CA LEU A 118 92.313 -6.356 23.437 1.00 38.12 C ANISOU 668 CA LEU A 118 5019 4614 4851 -130 60 -8 C ATOM 669 C LEU A 118 91.629 -6.899 24.681 1.00 37.27 C ANISOU 669 C LEU A 118 4907 4497 4757 -124 65 -22 C ATOM 670 O LEU A 118 92.206 -6.912 25.772 1.00 29.17 O ANISOU 670 O LEU A 118 3878 3467 3740 -124 69 -12 O ATOM 671 CB LEU A 118 91.950 -4.886 23.221 1.00 26.10 C ANISOU 671 CB LEU A 118 3505 3089 3322 -132 32 -2 C ATOM 672 CG LEU A 118 92.130 -3.962 24.428 1.00 27.15 C ANISOU 672 CG LEU A 118 3640 3213 3464 -133 17 8 C ATOM 673 CD1 LEU A 118 93.598 -3.870 24.821 1.00 24.21 C ANISOU 673 CD1 LEU A 118 3264 2841 3092 -138 24 31 C ATOM 674 CD2 LEU A 118 91.547 -2.580 24.156 1.00 18.72 C ANISOU 674 CD2 LEU A 118 2579 2140 2392 -134 -9 10 C ATOM 675 N ASN A 119 90.404 -7.379 24.499 1.00 24.17 N ANISOU 675 N ASN A 119 3248 2837 3100 -119 67 -46 N ATOM 676 CA ASN A 119 89.690 -8.023 25.584 1.00 32.12 C ANISOU 676 CA ASN A 119 4250 3836 4120 -113 76 -61 C ATOM 677 C ASN A 119 90.373 -9.314 26.007 1.00 27.70 C ANISOU 677 C ASN A 119 3681 3276 3568 -112 103 -58 C ATOM 678 O ASN A 119 90.439 -9.617 27.195 1.00 23.23 O ANISOU 678 O ASN A 119 3109 2703 3012 -109 109 -57 O ATOM 679 CB ASN A 119 88.244 -8.309 25.190 1.00 27.29 C ANISOU 679 CB ASN A 119 3638 3221 3509 -108 73 -87 C ATOM 680 CG ASN A 119 87.506 -9.095 26.252 1.00 43.17 C ANISOU 680 CG ASN A 119 5644 5224 5535 -102 84 -103 C ATOM 681 OD1 ASN A 119 87.431 -10.323 26.193 1.00 45.31 O ANISOU 681 OD1 ASN A 119 5907 5496 5811 -99 107 -114 O ATOM 682 ND2 ASN A 119 86.971 -8.392 27.242 1.00 27.99 N ANISOU 682 ND2 ASN A 119 3724 3292 3618 -100 69 -105 N ATOM 683 N MET A 120 90.918 -10.049 25.041 1.00 23.27 N ANISOU 683 N MET A 120 3116 2723 3001 -114 120 -57 N ATOM 684 CA MET A 120 91.607 -11.296 25.357 1.00 29.49 C ANISOU 684 CA MET A 120 3895 3512 3798 -113 147 -54 C ATOM 685 C MET A 120 92.831 -11.038 26.225 1.00 24.99 C ANISOU 685 C MET A 120 3322 2941 3232 -115 148 -29 C ATOM 686 O MET A 120 92.973 -11.614 27.317 1.00 23.52 O ANISOU 686 O MET A 120 3129 2749 3057 -111 160 -27 O ATOM 687 CB MET A 120 92.027 -12.024 24.075 1.00 28.47 C ANISOU 687 CB MET A 120 3763 3392 3662 -116 164 -56 C ATOM 688 CG MET A 120 92.828 -13.299 24.313 1.00 38.04 C ANISOU 688 CG MET A 120 4965 4604 4884 -115 194 -51 C ATOM 689 SD MET A 120 93.409 -14.096 22.799 1.00 43.07 S ANISOU 689 SD MET A 120 5599 5252 5512 -120 214 -54 S ATOM 690 CE MET A 120 94.469 -12.823 22.119 1.00 46.96 C ANISOU 690 CE MET A 120 6100 5752 5989 -128 195 -28 C ATOM 691 N TYR A 121 93.699 -10.146 25.756 1.00 23.54 N ANISOU 691 N TYR A 121 3143 2761 3038 -121 136 -10 N ATOM 692 CA TYR A 121 94.946 -9.899 26.472 1.00 23.93 C ANISOU 692 CA TYR A 121 3191 2812 3092 -125 137 15 C ATOM 693 C TYR A 121 94.715 -9.213 27.820 1.00 27.75 C ANISOU 693 C TYR A 121 3674 3287 3581 -123 123 18 C ATOM 694 O TYR A 121 95.304 -9.609 28.836 1.00 26.92 O ANISOU 694 O TYR A 121 3563 3181 3485 -122 132 28 O ATOM 695 CB TYR A 121 95.897 -9.075 25.603 1.00 22.53 C ANISOU 695 CB TYR A 121 3018 2640 2902 -132 128 34 C ATOM 696 CG TYR A 121 96.502 -9.876 24.473 1.00 39.89 C ANISOU 696 CG TYR A 121 5213 4847 5095 -134 147 36 C ATOM 697 CD1 TYR A 121 97.146 -11.081 24.722 1.00 27.62 C ANISOU 697 CD1 TYR A 121 3650 3294 3550 -133 173 39 C ATOM 698 CD2 TYR A 121 96.409 -9.442 23.158 1.00 45.36 C ANISOU 698 CD2 TYR A 121 5913 5548 5775 -138 139 34 C ATOM 699 CE1 TYR A 121 97.696 -11.824 23.693 1.00 34.98 C ANISOU 699 CE1 TYR A 121 4580 4234 4479 -136 192 40 C ATOM 700 CE2 TYR A 121 96.955 -10.179 22.122 1.00 39.43 C ANISOU 700 CE2 TYR A 121 5159 4804 5019 -141 157 35 C ATOM 701 CZ TYR A 121 97.598 -11.370 22.395 1.00 40.33 C ANISOU 701 CZ TYR A 121 5264 4918 5142 -140 184 38 C ATOM 702 OH TYR A 121 98.142 -12.107 21.368 1.00 50.39 O ANISOU 702 OH TYR A 121 6535 6200 6412 -143 203 38 O ATOM 703 N ALA A 122 93.835 -8.213 27.838 1.00 30.99 N ANISOU 703 N ALA A 122 4093 3693 3988 -123 100 9 N ATOM 704 CA ALA A 122 93.554 -7.496 29.078 1.00 24.64 C ANISOU 704 CA ALA A 122 3291 2883 3190 -122 85 10 C ATOM 705 C ALA A 122 92.923 -8.421 30.106 1.00 32.08 C ANISOU 705 C ALA A 122 4226 3819 4144 -115 99 -3 C ATOM 706 O ALA A 122 93.281 -8.390 31.294 1.00 32.74 O ANISOU 706 O ALA A 122 4306 3901 4234 -114 100 5 O ATOM 707 CB ALA A 122 92.646 -6.304 28.817 1.00 20.84 C ANISOU 707 CB ALA A 122 2818 2396 2704 -122 60 2 C ATOM 708 N SER A 123 92.019 -9.278 29.641 1.00 27.84 N ANISOU 708 N SER A 123 3687 3281 3610 -110 111 -24 N ATOM 709 CA SER A 123 91.371 -10.206 30.550 1.00 27.86 C ANISOU 709 CA SER A 123 3683 3278 3624 -103 125 -37 C ATOM 710 C SER A 123 92.375 -11.186 31.126 1.00 24.64 C ANISOU 710 C SER A 123 3265 2873 3223 -102 148 -24 C ATOM 711 O SER A 123 92.415 -11.373 32.337 1.00 25.95 O ANISOU 711 O SER A 123 3427 3036 3397 -99 151 -20 O ATOM 712 CB SER A 123 90.240 -10.970 29.860 1.00 16.57 C ANISOU 712 CB SER A 123 2253 1847 2197 -98 134 -62 C ATOM 713 OG SER A 123 89.094 -10.152 29.701 1.00 44.07 O ANISOU 713 OG SER A 123 5743 5325 5677 -97 114 -77 O ATOM 714 N ILE A 124 93.190 -11.808 30.277 1.00 18.46 N ANISOU 714 N ILE A 124 2479 2097 2438 -104 164 -15 N ATOM 715 CA ILE A 124 94.083 -12.834 30.800 1.00 13.73 C ANISOU 715 CA ILE A 124 1870 1500 1848 -103 188 -3 C ATOM 716 C ILE A 124 95.175 -12.236 31.692 1.00 22.73 C ANISOU 716 C ILE A 124 3007 2642 2986 -106 180 22 C ATOM 717 O ILE A 124 95.622 -12.885 32.644 1.00 22.00 O ANISOU 717 O ILE A 124 2907 2549 2903 -103 194 31 O ATOM 718 CB ILE A 124 94.706 -13.687 29.666 1.00 17.65 C ANISOU 718 CB ILE A 124 2362 2002 2343 -105 208 0 C ATOM 719 CG1 ILE A 124 95.164 -15.043 30.213 1.00 29.17 C ANISOU 719 CG1 ILE A 124 3808 3459 3814 -100 238 4 C ATOM 720 CG2 ILE A 124 95.838 -12.954 28.959 1.00 17.93 C ANISOU 720 CG2 ILE A 124 2401 2044 2367 -113 199 20 C ATOM 721 CD1 ILE A 124 94.084 -15.799 30.975 1.00 13.15 C ANISOU 721 CD1 ILE A 124 1775 1424 1799 -92 248 -15 C ATOM 722 N LEU A 125 95.569 -10.993 31.422 1.00 17.14 N ANISOU 722 N LEU A 125 2307 1936 2269 -113 158 33 N ATOM 723 CA LEU A 125 96.562 -10.337 32.268 1.00 17.23 C ANISOU 723 CA LEU A 125 2317 1950 2279 -117 149 54 C ATOM 724 C LEU A 125 95.980 -10.018 33.638 1.00 22.81 C ANISOU 724 C LEU A 125 3023 2651 2991 -113 139 49 C ATOM 725 O LEU A 125 96.602 -10.297 34.675 1.00 27.42 O ANISOU 725 O LEU A 125 3600 3237 3580 -113 146 61 O ATOM 726 CB LEU A 125 97.086 -9.067 31.601 1.00 17.02 C ANISOU 726 CB LEU A 125 2299 1925 2241 -124 128 66 C ATOM 727 CG LEU A 125 98.092 -9.338 30.484 1.00 22.29 C ANISOU 727 CG LEU A 125 2965 2600 2903 -129 138 79 C ATOM 728 CD1 LEU A 125 98.608 -8.047 29.863 1.00 21.50 C ANISOU 728 CD1 LEU A 125 2873 2502 2793 -136 118 92 C ATOM 729 CD2 LEU A 125 99.233 -10.167 31.033 1.00 15.20 C ANISOU 729 CD2 LEU A 125 2057 1706 2012 -129 158 97 C ATOM 730 N LEU A 126 94.771 -9.459 33.638 1.00 32.29 N ANISOU 730 N LEU A 126 4232 3846 4191 -111 124 30 N ATOM 731 CA LEU A 126 94.106 -9.146 34.894 1.00 28.36 C ANISOU 731 CA LEU A 126 3734 3343 3699 -108 115 22 C ATOM 732 C LEU A 126 93.838 -10.413 35.700 1.00 30.89 C ANISOU 732 C LEU A 126 4045 3663 4030 -101 137 16 C ATOM 733 O LEU A 126 94.011 -10.431 36.917 1.00 19.31 O ANISOU 733 O LEU A 126 2574 2196 2568 -99 138 23 O ATOM 734 CB LEU A 126 92.795 -8.405 34.635 1.00 24.57 C ANISOU 734 CB LEU A 126 3263 2855 3217 -107 97 2 C ATOM 735 CG LEU A 126 92.889 -6.971 34.114 1.00 28.16 C ANISOU 735 CG LEU A 126 3726 3309 3663 -114 72 7 C ATOM 736 CD1 LEU A 126 91.537 -6.487 33.610 1.00 23.51 C ANISOU 736 CD1 LEU A 126 3146 2714 3074 -111 58 -14 C ATOM 737 CD2 LEU A 126 93.416 -6.052 35.201 1.00 25.61 C ANISOU 737 CD2 LEU A 126 3405 2986 3341 -118 58 19 C ATOM 738 N LEU A 127 93.452 -11.484 35.011 1.00 23.02 N ANISOU 738 N LEU A 127 3045 2665 3038 -96 157 5 N ATOM 739 CA LEU A 127 93.208 -12.764 35.666 1.00 23.76 C ANISOU 739 CA LEU A 127 3129 2757 3144 -89 181 0 C ATOM 740 C LEU A 127 94.501 -13.351 36.216 1.00 21.17 C ANISOU 740 C LEU A 127 2791 2435 2819 -89 196 23 C ATOM 741 O LEU A 127 94.486 -14.085 37.205 1.00 27.90 O ANISOU 741 O LEU A 127 3634 3286 3680 -84 210 26 O ATOM 742 CB LEU A 127 92.549 -13.753 34.704 1.00 24.61 C ANISOU 742 CB LEU A 127 3234 2862 3256 -85 198 -18 C ATOM 743 CG LEU A 127 91.107 -13.464 34.278 1.00 27.13 C ANISOU 743 CG LEU A 127 3560 3174 3573 -82 187 -44 C ATOM 744 CD1 LEU A 127 90.622 -14.533 33.313 1.00 19.07 C ANISOU 744 CD1 LEU A 127 2536 2153 2558 -79 207 -60 C ATOM 745 CD2 LEU A 127 90.180 -13.360 35.481 1.00 13.14 C ANISOU 745 CD2 LEU A 127 1789 1396 1810 -77 182 -55 C ATOM 746 N ALA A 128 95.618 -13.027 35.572 1.00 22.25 N ANISOU 746 N ALA A 128 2928 2578 2948 -96 194 41 N ATOM 747 CA ALA A 128 96.916 -13.456 36.072 1.00 20.48 C ANISOU 747 CA ALA A 128 2695 2361 2728 -97 207 65 C ATOM 748 C ALA A 128 97.245 -12.745 37.381 1.00 19.24 C ANISOU 748 C ALA A 128 2536 2206 2568 -99 192 77 C ATOM 749 O ALA A 128 97.645 -13.388 38.360 1.00 21.50 O ANISOU 749 O ALA A 128 2812 2495 2860 -95 205 87 O ATOM 750 CB ALA A 128 98.003 -13.199 35.035 1.00 20.57 C ANISOU 750 CB ALA A 128 2708 2378 2732 -104 207 81 C ATOM 751 N THR A 129 97.068 -11.424 37.414 1.00 14.00 N ANISOU 751 N THR A 129 1883 1542 1896 -104 166 75 N ATOM 752 CA THR A 129 97.359 -10.696 38.650 1.00 22.50 C ANISOU 752 CA THR A 129 2958 2621 2971 -107 152 84 C ATOM 753 C THR A 129 96.411 -11.108 39.776 1.00 30.37 C ANISOU 753 C THR A 129 3952 3614 3974 -100 156 71 C ATOM 754 O THR A 129 96.811 -11.211 40.941 1.00 20.87 O ANISOU 754 O THR A 129 2742 2415 2772 -99 158 82 O ATOM 755 CB THR A 129 97.254 -9.175 38.463 1.00 23.38 C ANISOU 755 CB THR A 129 3080 2730 3073 -114 123 83 C ATOM 756 OG1 THR A 129 95.877 -8.783 38.494 1.00 52.45 O ANISOU 756 OG1 THR A 129 6770 6403 6756 -111 112 60 O ATOM 757 CG2 THR A 129 97.871 -8.751 37.142 1.00 20.50 C ANISOU 757 CG2 THR A 129 2720 2367 2702 -120 119 91 C ATOM 758 N ILE A 130 95.157 -11.364 39.414 1.00 32.51 N ANISOU 758 N ILE A 130 4227 3876 4248 -94 157 48 N ATOM 759 CA ILE A 130 94.156 -11.776 40.386 1.00 17.30 C ANISOU 759 CA ILE A 130 2299 1945 2330 -87 162 34 C ATOM 760 C ILE A 130 94.485 -13.152 40.941 1.00 29.08 C ANISOU 760 C ILE A 130 3778 3441 3832 -80 189 41 C ATOM 761 O ILE A 130 94.335 -13.404 42.138 1.00 28.88 O ANISOU 761 O ILE A 130 3747 3416 3809 -76 193 43 O ATOM 762 CB ILE A 130 92.747 -11.805 39.767 1.00 18.11 C ANISOU 762 CB ILE A 130 2408 2038 2435 -83 159 7 C ATOM 763 CG1 ILE A 130 92.290 -10.390 39.419 1.00 26.06 C ANISOU 763 CG1 ILE A 130 3427 3041 3434 -89 131 0 C ATOM 764 CG2 ILE A 130 91.751 -12.448 40.720 1.00 14.65 C ANISOU 764 CG2 ILE A 130 1966 1594 2006 -75 169 -7 C ATOM 765 CD1 ILE A 130 91.133 -10.357 38.445 1.00 21.89 C ANISOU 765 CD1 ILE A 130 2906 2506 2907 -87 127 -23 C ATOM 766 N SER A 131 94.950 -14.040 40.068 1.00 19.42 N ANISOU 766 N SER A 131 2550 2218 2612 -79 209 46 N ATOM 767 CA SER A 131 95.336 -15.371 40.507 1.00 28.18 C ANISOU 767 CA SER A 131 3646 3329 3732 -72 236 55 C ATOM 768 C SER A 131 96.550 -15.298 41.420 1.00 26.33 C ANISOU 768 C SER A 131 3403 3105 3495 -75 237 81 C ATOM 769 O SER A 131 96.660 -16.060 42.382 1.00 20.10 O ANISOU 769 O SER A 131 2605 2319 2714 -69 252 89 O ATOM 770 CB SER A 131 95.623 -16.272 39.308 1.00 16.51 C ANISOU 770 CB SER A 131 2165 1851 2259 -72 257 54 C ATOM 771 OG SER A 131 94.482 -16.374 38.477 1.00 20.82 O ANISOU 771 OG SER A 131 2716 2388 2806 -70 256 29 O ATOM 772 N ALA A 132 97.451 -14.364 41.124 1.00 22.87 N ANISOU 772 N ALA A 132 2970 2673 3048 -83 221 96 N ATOM 773 CA ALA A 132 98.611 -14.151 41.980 1.00 19.79 C ANISOU 773 CA ALA A 132 2572 2293 2654 -87 218 120 C ATOM 774 C ALA A 132 98.167 -13.638 43.344 1.00 28.77 C ANISOU 774 C ALA A 132 3709 3432 3788 -86 205 117 C ATOM 775 O ALA A 132 98.771 -13.958 44.370 1.00 22.04 O ANISOU 775 O ALA A 132 2848 2588 2938 -84 211 133 O ATOM 776 CB ALA A 132 99.583 -13.180 41.332 1.00 17.60 C ANISOU 776 CB ALA A 132 2300 2020 2366 -97 202 134 C ATOM 777 N ASP A 133 97.091 -12.857 43.348 1.00 22.95 N ANISOU 777 N ASP A 133 2984 2688 3049 -86 187 97 N ATOM 778 CA ASP A 133 96.546 -12.327 44.589 1.00 22.56 C ANISOU 778 CA ASP A 133 2936 2640 2997 -86 175 90 C ATOM 779 C ASP A 133 95.916 -13.437 45.429 1.00 27.55 C ANISOU 779 C ASP A 133 3560 3270 3639 -75 194 85 C ATOM 780 O ASP A 133 96.163 -13.534 46.637 1.00 26.11 O ANISOU 780 O ASP A 133 3370 3095 3455 -74 196 94 O ATOM 781 CB ASP A 133 95.518 -11.236 44.294 1.00 31.71 C ANISOU 781 CB ASP A 133 4107 3789 4151 -89 152 69 C ATOM 782 CG ASP A 133 95.079 -10.499 45.540 1.00 24.84 C ANISOU 782 CG ASP A 133 3239 2920 3277 -90 137 64 C ATOM 783 OD1 ASP A 133 95.899 -10.362 46.471 1.00 44.17 O ANISOU 783 OD1 ASP A 133 5682 5379 5722 -93 135 80 O ATOM 784 OD2 ASP A 133 93.912 -10.058 45.590 1.00 27.69 O ANISOU 784 OD2 ASP A 133 3608 3272 3640 -89 127 42 O ATOM 785 N ARG A 134 95.121 -14.283 44.779 1.00 24.64 N ANISOU 785 N ARG A 134 3190 2892 3278 -69 210 70 N ATOM 786 CA ARG A 134 94.484 -15.401 45.463 1.00 23.68 C ANISOU 786 CA ARG A 134 3061 2768 3168 -58 231 63 C ATOM 787 C ARG A 134 95.542 -16.360 45.989 1.00 29.00 C ANISOU 787 C ARG A 134 3720 3451 3847 -55 252 88 C ATOM 788 O ARG A 134 95.357 -17.001 47.025 1.00 27.67 O ANISOU 788 O ARG A 134 3543 3284 3684 -48 264 92 O ATOM 789 CB ARG A 134 93.520 -16.149 44.533 1.00 16.08 C ANISOU 789 CB ARG A 134 2101 1794 2216 -53 245 42 C ATOM 790 CG ARG A 134 92.410 -15.308 43.906 1.00 22.77 C ANISOU 790 CG ARG A 134 2961 2632 3059 -55 226 18 C ATOM 791 CD ARG A 134 91.721 -14.389 44.906 1.00 27.82 C ANISOU 791 CD ARG A 134 3607 3270 3694 -56 206 9 C ATOM 792 NE ARG A 134 91.413 -15.064 46.161 1.00 32.92 N ANISOU 792 NE ARG A 134 4245 3918 4347 -49 219 10 N ATOM 793 CZ ARG A 134 90.876 -14.462 47.215 1.00 28.19 C ANISOU 793 CZ ARG A 134 3648 3318 3744 -49 206 4 C ATOM 794 NH1 ARG A 134 90.578 -13.172 47.163 1.00 29.82 N ANISOU 794 NH1 ARG A 134 3866 3523 3942 -56 180 -5 N ATOM 795 NH2 ARG A 134 90.640 -15.149 48.322 1.00 46.74 N ANISOU 795 NH2 ARG A 134 5990 5670 6099 -41 219 6 N ATOM 796 N PHE A 135 96.653 -16.452 45.269 1.00 23.66 N ANISOU 796 N PHE A 135 3041 2780 3169 -60 257 105 N ATOM 797 CA PHE A 135 97.749 -17.305 45.696 1.00 28.25 C ANISOU 797 CA PHE A 135 3609 3370 3756 -57 276 130 C ATOM 798 C PHE A 135 98.426 -16.735 46.936 1.00 24.76 C ANISOU 798 C PHE A 135 3161 2940 3305 -60 263 147 C ATOM 799 O PHE A 135 98.643 -17.445 47.925 1.00 23.91 O ANISOU 799 O PHE A 135 3043 2839 3202 -54 277 160 O ATOM 800 CB PHE A 135 98.770 -17.467 44.567 1.00 22.03 C ANISOU 800 CB PHE A 135 2819 2584 2968 -62 283 143 C ATOM 801 CG PHE A 135 99.885 -18.418 44.891 1.00 23.95 C ANISOU 801 CG PHE A 135 3046 2834 3218 -59 305 168 C ATOM 802 CD1 PHE A 135 101.027 -17.975 45.541 1.00 23.54 C ANISOU 802 CD1 PHE A 135 2990 2796 3159 -64 296 192 C ATOM 803 CD2 PHE A 135 99.793 -19.754 44.544 1.00 31.48 C ANISOU 803 CD2 PHE A 135 3992 3783 4187 -51 334 168 C ATOM 804 CE1 PHE A 135 102.050 -18.848 45.843 1.00 24.08 C ANISOU 804 CE1 PHE A 135 3044 2872 3236 -60 316 217 C ATOM 805 CE2 PHE A 135 100.816 -20.632 44.841 1.00 34.92 C ANISOU 805 CE2 PHE A 135 4412 4225 4631 -48 355 192 C ATOM 806 CZ PHE A 135 101.946 -20.178 45.490 1.00 25.76 C ANISOU 806 CZ PHE A 135 3247 3078 3464 -52 346 217 C ATOM 807 N LEU A 136 98.757 -15.449 46.875 1.00 23.10 N ANISOU 807 N LEU A 136 2960 2733 3082 -70 238 149 N ATOM 808 CA LEU A 136 99.474 -14.800 47.964 1.00 26.61 C ANISOU 808 CA LEU A 136 3401 3191 3517 -74 224 165 C ATOM 809 C LEU A 136 98.644 -14.750 49.244 1.00 31.83 C ANISOU 809 C LEU A 136 4062 3854 4178 -70 220 155 C ATOM 810 O LEU A 136 99.190 -14.838 50.341 1.00 21.02 O ANISOU 810 O LEU A 136 2684 2497 2805 -69 221 171 O ATOM 811 CB LEU A 136 99.902 -13.388 47.551 1.00 20.29 C ANISOU 811 CB LEU A 136 2611 2393 2706 -86 197 165 C ATOM 812 CG LEU A 136 101.009 -13.306 46.491 1.00 35.98 C ANISOU 812 CG LEU A 136 4597 4381 4691 -92 199 180 C ATOM 813 CD1 LEU A 136 101.140 -11.893 45.939 1.00 30.01 C ANISOU 813 CD1 LEU A 136 3854 3624 3926 -103 173 175 C ATOM 814 CD2 LEU A 136 102.341 -13.788 47.050 1.00 18.39 C ANISOU 814 CD2 LEU A 136 2355 2167 2464 -93 209 209 C ATOM 815 N LEU A 137 97.327 -14.624 49.107 1.00 30.05 N ANISOU 815 N LEU A 137 3845 3617 3956 -66 216 130 N ATOM 816 CA LEU A 137 96.462 -14.594 50.283 1.00 28.45 C ANISOU 816 CA LEU A 137 3643 3415 3753 -62 213 119 C ATOM 817 C LEU A 137 96.485 -15.912 51.045 1.00 33.97 C ANISOU 817 C LEU A 137 4328 4118 4461 -51 239 130 C ATOM 818 O LEU A 137 96.403 -15.936 52.274 1.00 32.21 O ANISOU 818 O LEU A 137 4099 3903 4235 -48 238 134 O ATOM 819 CB LEU A 137 95.030 -14.262 49.881 1.00 20.25 C ANISOU 819 CB LEU A 137 2615 2361 2717 -60 206 90 C ATOM 820 CG LEU A 137 94.762 -12.823 49.463 1.00 25.66 C ANISOU 820 CG LEU A 137 3315 3043 3394 -69 178 77 C ATOM 821 CD1 LEU A 137 93.440 -12.777 48.735 1.00 19.87 C ANISOU 821 CD1 LEU A 137 2591 2294 2666 -66 176 51 C ATOM 822 CD2 LEU A 137 94.753 -11.906 50.678 1.00 14.05 C ANISOU 822 CD2 LEU A 137 1845 1578 1913 -74 159 78 C ATOM 823 N VAL A 138 96.608 -17.007 50.306 1.00 29.14 N ANISOU 823 N VAL A 138 3710 3501 3861 -45 263 133 N ATOM 824 CA VAL A 138 96.632 -18.331 50.904 1.00 25.63 C ANISOU 824 CA VAL A 138 3252 3059 3429 -34 290 143 C ATOM 825 C VAL A 138 98.023 -18.685 51.433 1.00 29.13 C ANISOU 825 C VAL A 138 3682 3517 3870 -35 298 175 C ATOM 826 O VAL A 138 98.154 -19.235 52.525 1.00 37.70 O ANISOU 826 O VAL A 138 4756 4611 4956 -29 308 188 O ATOM 827 CB VAL A 138 96.160 -19.394 49.884 1.00 24.26 C ANISOU 827 CB VAL A 138 3076 2872 3270 -28 313 133 C ATOM 828 CG1 VAL A 138 96.447 -20.801 50.380 1.00 27.34 C ANISOU 828 CG1 VAL A 138 3450 3264 3674 -18 344 148 C ATOM 829 CG2 VAL A 138 94.675 -19.217 49.590 1.00 19.88 C ANISOU 829 CG2 VAL A 138 2532 2303 2719 -25 308 102 C ATOM 830 N PHE A 139 99.059 -18.345 50.671 1.00 35.44 N ANISOU 830 N PHE A 139 4481 4320 4664 -43 292 188 N ATOM 831 CA PHE A 139 100.411 -18.789 51.006 1.00 37.16 C ANISOU 831 CA PHE A 139 4685 4551 4882 -43 302 219 C ATOM 832 C PHE A 139 101.303 -17.728 51.665 1.00 39.73 C ANISOU 832 C PHE A 139 5011 4892 5193 -53 279 234 C ATOM 833 O PHE A 139 102.294 -18.071 52.309 1.00 28.69 O ANISOU 833 O PHE A 139 3600 3507 3793 -52 286 259 O ATOM 834 CB PHE A 139 101.087 -19.340 49.748 1.00 21.88 C ANISOU 834 CB PHE A 139 2747 2611 2956 -44 317 226 C ATOM 835 CG PHE A 139 100.482 -20.631 49.260 1.00 39.53 C ANISOU 835 CG PHE A 139 4977 4834 5208 -34 346 218 C ATOM 836 CD1 PHE A 139 100.754 -21.825 49.909 1.00 26.35 C ANISOU 836 CD1 PHE A 139 3293 3169 3552 -25 372 234 C ATOM 837 CD2 PHE A 139 99.635 -20.650 48.161 1.00 32.12 C ANISOU 837 CD2 PHE A 139 4049 3881 4274 -35 347 193 C ATOM 838 CE1 PHE A 139 100.199 -23.017 49.471 1.00 26.54 C ANISOU 838 CE1 PHE A 139 3311 3180 3593 -16 399 225 C ATOM 839 CE2 PHE A 139 99.077 -21.841 47.716 1.00 28.54 C ANISOU 839 CE2 PHE A 139 3589 3416 3837 -26 374 184 C ATOM 840 CZ PHE A 139 99.360 -23.025 48.373 1.00 35.43 C ANISOU 840 CZ PHE A 139 4447 4292 4723 -17 400 200 C ATOM 841 N LYS A 140 100.969 -16.450 51.512 1.00 43.69 N ANISOU 841 N LYS A 140 5526 5391 5682 -61 253 219 N ATOM 842 CA LYS A 140 101.743 -15.394 52.166 1.00 25.29 C ANISOU 842 CA LYS A 140 3196 3075 3339 -71 230 230 C ATOM 843 C LYS A 140 100.852 -14.365 52.860 1.00 26.40 C ANISOU 843 C LYS A 140 3347 3215 3470 -75 208 210 C ATOM 844 O LYS A 140 100.773 -13.218 52.420 1.00 22.43 O ANISOU 844 O LYS A 140 2856 2708 2960 -84 186 200 O ATOM 845 CB LYS A 140 102.635 -14.684 51.148 1.00 27.60 C ANISOU 845 CB LYS A 140 3494 3367 3627 -81 219 237 C ATOM 846 CG LYS A 140 103.523 -15.602 50.323 1.00 26.33 C ANISOU 846 CG LYS A 140 3324 3206 3475 -78 240 255 C ATOM 847 CD LYS A 140 104.679 -16.139 51.144 1.00 34.90 C ANISOU 847 CD LYS A 140 4393 4308 4561 -77 250 285 C ATOM 848 CE LYS A 140 105.641 -16.934 50.280 1.00 39.43 C ANISOU 848 CE LYS A 140 4958 4880 5143 -76 269 303 C ATOM 849 NZ LYS A 140 106.805 -17.429 51.066 1.00 55.54 N ANISOU 849 NZ LYS A 140 6982 6937 7185 -74 278 333 N ATOM 850 N PRO A 141 100.179 -14.765 53.956 1.00 33.43 N ANISOU 850 N PRO A 141 4233 4108 4360 -68 214 206 N ATOM 851 CA PRO A 141 99.301 -13.834 54.678 1.00 33.57 C ANISOU 851 CA PRO A 141 4260 4124 4369 -71 194 186 C ATOM 852 C PRO A 141 100.025 -12.595 55.207 1.00 28.48 C ANISOU 852 C PRO A 141 3618 3493 3711 -83 169 192 C ATOM 853 O PRO A 141 99.471 -11.489 55.180 1.00 28.97 O ANISOU 853 O PRO A 141 3692 3549 3767 -90 148 174 O ATOM 854 CB PRO A 141 98.785 -14.677 55.845 1.00 23.96 C ANISOU 854 CB PRO A 141 3034 2913 3156 -61 209 188 C ATOM 855 CG PRO A 141 98.979 -16.094 55.425 1.00 29.31 C ANISOU 855 CG PRO A 141 3702 3588 3848 -51 238 200 C ATOM 856 CD PRO A 141 100.217 -16.090 54.591 1.00 33.73 C ANISOU 856 CD PRO A 141 4258 4152 4408 -56 239 219 C ATOM 857 N ALA A 142 101.269 -12.774 55.642 1.00 35.27 N ANISOU 857 N ALA A 142 4466 4370 4566 -86 172 218 N ATOM 858 CA ALA A 142 102.018 -11.690 56.270 1.00 28.96 C ANISOU 858 CA ALA A 142 3666 3584 3753 -97 150 225 C ATOM 859 C ALA A 142 102.386 -10.621 55.254 1.00 34.39 C ANISOU 859 C ALA A 142 4364 4264 4438 -108 132 220 C ATOM 860 O ALA A 142 102.354 -9.427 55.552 1.00 29.86 O ANISOU 860 O ALA A 142 3797 3692 3856 -118 110 211 O ATOM 861 CB ALA A 142 103.262 -12.234 56.949 1.00 28.63 C ANISOU 861 CB ALA A 142 3608 3562 3708 -97 158 255 C ATOM 862 N TRP A 143 102.739 -11.061 54.053 1.00 33.08 N ANISOU 862 N TRP A 143 4199 4089 4280 -107 143 226 N ATOM 863 CA TRP A 143 103.064 -10.143 52.974 1.00 31.97 C ANISOU 863 CA TRP A 143 4068 3941 4138 -116 128 222 C ATOM 864 C TRP A 143 101.827 -9.362 52.537 1.00 35.30 C ANISOU 864 C TRP A 143 4505 4346 4560 -117 114 194 C ATOM 865 O TRP A 143 101.899 -8.164 52.236 1.00 30.80 O ANISOU 865 O TRP A 143 3944 3774 3985 -127 93 187 O ATOM 866 CB TRP A 143 103.660 -10.919 51.799 1.00 29.52 C ANISOU 866 CB TRP A 143 3754 3625 3836 -113 145 235 C ATOM 867 CG TRP A 143 104.247 -10.063 50.733 1.00 36.26 C ANISOU 867 CG TRP A 143 4616 4474 4688 -122 132 237 C ATOM 868 CD1 TRP A 143 105.547 -9.669 50.623 1.00 40.40 C ANISOU 868 CD1 TRP A 143 5134 5008 5207 -130 126 257 C ATOM 869 CD2 TRP A 143 103.559 -9.498 49.614 1.00 37.29 C ANISOU 869 CD2 TRP A 143 4760 4589 4820 -124 124 218 C ATOM 870 NE1 TRP A 143 105.712 -8.889 49.505 1.00 37.24 N ANISOU 870 NE1 TRP A 143 4744 4599 4807 -137 115 252 N ATOM 871 CE2 TRP A 143 104.505 -8.769 48.868 1.00 37.14 C ANISOU 871 CE2 TRP A 143 4743 4571 4796 -134 113 229 C ATOM 872 CE3 TRP A 143 102.233 -9.536 49.172 1.00 23.52 C ANISOU 872 CE3 TRP A 143 3026 2831 3081 -119 124 194 C ATOM 873 CZ2 TRP A 143 104.167 -8.083 47.703 1.00 56.15 C ANISOU 873 CZ2 TRP A 143 7163 6967 7205 -138 103 217 C ATOM 874 CZ3 TRP A 143 101.900 -8.856 48.017 1.00 30.03 C ANISOU 874 CZ3 TRP A 143 3862 3644 3904 -124 113 182 C ATOM 875 CH2 TRP A 143 102.862 -8.139 47.295 1.00 45.13 C ANISOU 875 CH2 TRP A 143 5777 5558 5813 -133 103 194 C ATOM 876 N CYS A 144 100.688 -10.049 52.527 1.00 25.25 N ANISOU 876 N CYS A 144 3235 3064 3294 -108 126 178 N ATOM 877 CA CYS A 144 99.417 -9.428 52.183 1.00 21.94 C ANISOU 877 CA CYS A 144 2829 2630 2877 -108 115 151 C ATOM 878 C CYS A 144 99.013 -8.396 53.222 1.00 34.65 C ANISOU 878 C CYS A 144 4443 4243 4479 -114 95 140 C ATOM 879 O CYS A 144 98.339 -7.416 52.905 1.00 31.99 O ANISOU 879 O CYS A 144 4118 3896 4141 -119 78 122 O ATOM 880 CB CYS A 144 98.317 -10.482 52.051 1.00 29.86 C ANISOU 880 CB CYS A 144 3832 3622 3890 -96 134 138 C ATOM 881 SG CYS A 144 98.506 -11.601 50.654 1.00 28.68 S ANISOU 881 SG CYS A 144 3680 3464 3751 -90 157 143 S ATOM 882 N GLN A 145 99.419 -8.629 54.470 1.00 39.35 N ANISOU 882 N GLN A 145 5029 4854 5068 -113 97 151 N ATOM 883 CA GLN A 145 99.094 -7.701 55.548 1.00 29.98 C ANISOU 883 CA GLN A 145 3845 3673 3872 -119 80 141 C ATOM 884 C GLN A 145 99.712 -6.326 55.342 1.00 34.87 C ANISOU 884 C GLN A 145 4470 4294 4485 -133 56 141 C ATOM 885 O GLN A 145 99.113 -5.310 55.696 1.00 44.90 O ANISOU 885 O GLN A 145 5748 5560 5752 -139 39 123 O ATOM 886 CB GLN A 145 99.556 -8.262 56.894 1.00 41.63 C ANISOU 886 CB GLN A 145 5308 5168 5342 -116 88 155 C ATOM 887 CG GLN A 145 98.690 -9.380 57.428 1.00 50.51 C ANISOU 887 CG GLN A 145 6428 6290 6473 -104 107 150 C ATOM 888 CD GLN A 145 97.281 -8.922 57.733 1.00 64.90 C ANISOU 888 CD GLN A 145 8261 8100 8296 -102 99 122 C ATOM 889 OE1 GLN A 145 97.050 -7.757 58.063 1.00 52.90 O ANISOU 889 OE1 GLN A 145 6749 6581 6771 -111 79 109 O ATOM 890 NE2 GLN A 145 96.326 -9.838 57.623 1.00 53.85 N ANISOU 890 NE2 GLN A 145 6862 6691 6907 -91 116 112 N ATOM 891 N ARG A 146 100.907 -6.294 54.764 1.00 24.70 N ANISOU 891 N ARG A 146 3177 3012 3195 -138 57 160 N ATOM 892 CA ARG A 146 101.638 -5.040 54.627 1.00 34.58 C ANISOU 892 CA ARG A 146 4432 4266 4441 -151 36 163 C ATOM 893 C ARG A 146 101.519 -4.424 53.235 1.00 31.29 C ANISOU 893 C ARG A 146 4025 3833 4029 -155 28 157 C ATOM 894 O ARG A 146 101.451 -3.200 53.104 1.00 39.13 O ANISOU 894 O ARG A 146 5027 4822 5020 -164 9 147 O ATOM 895 CB ARG A 146 103.118 -5.249 54.979 1.00 34.33 C ANISOU 895 CB ARG A 146 4387 4253 4404 -155 39 190 C ATOM 896 CG ARG A 146 103.972 -3.979 54.924 1.00 44.80 C ANISOU 896 CG ARG A 146 5715 5583 5723 -169 18 195 C ATOM 897 CD ARG A 146 103.372 -2.850 55.763 1.00 64.51 C ANISOU 897 CD ARG A 146 8217 8079 8214 -177 -2 175 C ATOM 898 NE ARG A 146 104.175 -1.628 55.717 1.00 75.84 N ANISOU 898 NE ARG A 146 9653 9518 9645 -191 -21 178 N ATOM 899 CZ ARG A 146 103.799 -0.463 56.238 1.00 86.06 C ANISOU 899 CZ ARG A 146 10953 10810 10936 -199 -39 162 C ATOM 900 NH1 ARG A 146 102.625 -0.353 56.844 1.00 99.82 N ANISOU 900 NH1 ARG A 146 12701 12547 12678 -196 -41 141 N ATOM 901 NH2 ARG A 146 104.594 0.596 56.150 1.00 81.75 N ANISOU 901 NH2 ARG A 146 10408 10267 10388 -212 -55 165 N ATOM 902 N PHE A 147 101.488 -5.256 52.196 1.00 32.46 N ANISOU 902 N PHE A 147 4175 3975 4185 -148 44 161 N ATOM 903 CA PHE A 147 101.602 -4.719 50.839 1.00 46.64 C ANISOU 903 CA PHE A 147 5979 5758 5983 -152 37 159 C ATOM 904 C PHE A 147 100.345 -4.767 49.964 1.00 50.80 C ANISOU 904 C PHE A 147 6517 6267 6516 -146 38 138 C ATOM 905 O PHE A 147 100.344 -4.215 48.863 1.00 52.80 O ANISOU 905 O PHE A 147 6778 6511 6771 -150 31 135 O ATOM 906 CB PHE A 147 102.740 -5.431 50.108 1.00 44.62 C ANISOU 906 CB PHE A 147 5716 5508 5730 -151 51 182 C ATOM 907 CG PHE A 147 104.071 -5.292 50.786 1.00 35.93 C ANISOU 907 CG PHE A 147 4604 4424 4623 -157 48 204 C ATOM 908 CD1 PHE A 147 104.756 -4.089 50.759 1.00 36.26 C ANISOU 908 CD1 PHE A 147 4648 4469 4659 -169 29 208 C ATOM 909 CD2 PHE A 147 104.641 -6.367 51.448 1.00 40.26 C ANISOU 909 CD2 PHE A 147 5140 4986 5172 -152 65 221 C ATOM 910 CE1 PHE A 147 105.982 -3.959 51.381 1.00 35.49 C ANISOU 910 CE1 PHE A 147 4541 4388 4557 -176 26 228 C ATOM 911 CE2 PHE A 147 105.868 -6.243 52.070 1.00 35.26 C ANISOU 911 CE2 PHE A 147 4495 4369 4533 -157 62 242 C ATOM 912 CZ PHE A 147 106.539 -5.038 52.037 1.00 40.07 C ANISOU 912 CZ PHE A 147 5107 4981 5136 -170 42 245 C ATOM 913 N ARG A 148 99.276 -5.400 50.431 1.00 38.03 N ANISOU 913 N ARG A 148 4900 4646 4903 -137 47 124 N ATOM 914 CA ARG A 148 98.085 -5.487 49.593 1.00 26.88 C ANISOU 914 CA ARG A 148 3498 3217 3497 -132 49 104 C ATOM 915 C ARG A 148 97.258 -4.207 49.686 1.00 31.48 C ANISOU 915 C ARG A 148 4091 3791 4079 -138 27 85 C ATOM 916 O ARG A 148 96.201 -4.183 50.320 1.00 43.29 O ANISOU 916 O ARG A 148 5590 5281 5577 -134 25 67 O ATOM 917 CB ARG A 148 97.230 -6.697 49.968 1.00 18.74 C ANISOU 917 CB ARG A 148 2463 2184 2472 -120 68 96 C ATOM 918 CG ARG A 148 96.412 -7.209 48.796 1.00 22.27 C ANISOU 918 CG ARG A 148 2916 2618 2927 -114 77 83 C ATOM 919 CD ARG A 148 95.267 -8.095 49.230 1.00 26.64 C ANISOU 919 CD ARG A 148 3468 3165 3488 -103 91 67 C ATOM 920 NE ARG A 148 94.029 -7.723 48.553 1.00 42.12 N ANISOU 920 NE ARG A 148 5439 5111 5452 -101 84 44 N ATOM 921 CZ ARG A 148 92.970 -8.516 48.462 1.00 36.81 C ANISOU 921 CZ ARG A 148 4767 4430 4788 -92 97 28 C ATOM 922 NH1 ARG A 148 93.013 -9.719 48.998 1.00 61.25 N ANISOU 922 NH1 ARG A 148 7853 7531 7889 -84 118 34 N ATOM 923 NH2 ARG A 148 91.877 -8.114 47.833 1.00 44.90 N ANISOU 923 NH2 ARG A 148 5801 5442 5816 -91 88 7 N ATOM 924 N GLY A 149 97.752 -3.146 49.050 1.00 28.60 N ANISOU 924 N GLY A 149 3733 3423 3712 -147 11 88 N ATOM 925 CA GLY A 149 97.062 -1.867 49.030 1.00 31.91 C ANISOU 925 CA GLY A 149 4161 3832 4130 -153 -10 72 C ATOM 926 C GLY A 149 96.377 -1.552 47.710 1.00 42.45 C ANISOU 926 C GLY A 149 5506 5152 5470 -151 -14 61 C ATOM 927 O GLY A 149 96.688 -2.146 46.676 1.00 31.56 O ANISOU 927 O GLY A 149 4127 3773 4093 -148 -4 69 O ATOM 928 N ALA A 150 95.438 -0.609 47.749 1.00 29.14 N ANISOU 928 N ALA A 150 3830 3456 3788 -153 -30 43 N ATOM 929 CA ALA A 150 94.669 -0.241 46.564 1.00 23.17 C ANISOU 929 CA ALA A 150 3082 2686 3035 -152 -36 32 C ATOM 930 C ALA A 150 95.519 0.428 45.488 1.00 33.98 C ANISOU 930 C ALA A 150 4455 4055 4402 -159 -44 46 C ATOM 931 O ALA A 150 95.257 0.257 44.291 1.00 36.55 O ANISOU 931 O ALA A 150 4784 4374 4728 -156 -41 45 O ATOM 932 CB ALA A 150 93.513 0.672 46.954 1.00 24.45 C ANISOU 932 CB ALA A 150 3252 2836 3202 -153 -50 11 C ATOM 933 N GLY A 151 96.534 1.181 45.901 1.00 35.26 N ANISOU 933 N GLY A 151 4613 4223 4560 -168 -53 59 N ATOM 934 CA GLY A 151 97.349 1.894 44.936 1.00 35.70 C ANISOU 934 CA GLY A 151 4672 4277 4614 -175 -62 72 C ATOM 935 C GLY A 151 98.207 0.951 44.121 1.00 30.19 C ANISOU 935 C GLY A 151 3970 3587 3914 -172 -46 89 C ATOM 936 O GLY A 151 98.389 1.142 42.917 1.00 38.33 O ANISOU 936 O GLY A 151 5006 4614 4945 -173 -48 94 O ATOM 937 N LEU A 152 98.698 -0.098 44.770 1.00 28.70 N ANISOU 937 N LEU A 152 3771 3409 3723 -168 -31 98 N ATOM 938 CA LEU A 152 99.470 -1.112 44.074 1.00 28.31 C ANISOU 938 CA LEU A 152 3717 3367 3673 -165 -13 114 C ATOM 939 C LEU A 152 98.590 -1.874 43.096 1.00 32.42 C ANISOU 939 C LEU A 152 4242 3879 4197 -156 -2 102 C ATOM 940 O LEU A 152 99.009 -2.180 41.980 1.00 36.04 O ANISOU 940 O LEU A 152 4701 4338 4654 -156 5 111 O ATOM 941 CB LEU A 152 100.108 -2.081 45.067 1.00 23.75 C ANISOU 941 CB LEU A 152 3127 2801 3094 -162 2 125 C ATOM 942 CG LEU A 152 100.944 -3.183 44.420 1.00 22.00 C ANISOU 942 CG LEU A 152 2899 2586 2873 -158 22 142 C ATOM 943 CD1 LEU A 152 102.118 -2.570 43.678 1.00 31.26 C ANISOU 943 CD1 LEU A 152 4072 3762 4043 -167 15 160 C ATOM 944 CD2 LEU A 152 101.419 -4.196 45.450 1.00 26.65 C ANISOU 944 CD2 LEU A 152 3476 3188 3463 -154 37 153 C ATOM 945 N ALA A 153 97.360 -2.162 43.514 1.00 30.42 N ANISOU 945 N ALA A 153 3991 3619 3947 -150 0 83 N ATOM 946 CA ALA A 153 96.434 -2.898 42.665 1.00 32.52 C ANISOU 946 CA ALA A 153 4260 3878 4216 -142 10 70 C ATOM 947 C ALA A 153 96.082 -2.076 41.432 1.00 26.85 C ANISOU 947 C ALA A 153 3553 3153 3498 -145 -3 65 C ATOM 948 O ALA A 153 95.998 -2.605 40.318 1.00 21.58 O ANISOU 948 O ALA A 153 2887 2484 2829 -142 6 65 O ATOM 949 CB ALA A 153 95.178 -3.269 43.441 1.00 25.19 C ANISOU 949 CB ALA A 153 3334 2945 3294 -135 13 50 C ATOM 950 N TRP A 154 95.899 -0.773 41.632 1.00 24.50 N ANISOU 950 N TRP A 154 3261 2850 3200 -151 -23 61 N ATOM 951 CA TRP A 154 95.650 0.123 40.511 1.00 29.41 C ANISOU 951 CA TRP A 154 3891 3463 3820 -154 -37 59 C ATOM 952 C TRP A 154 96.866 0.251 39.590 1.00 32.43 C ANISOU 952 C TRP A 154 4273 3851 4198 -160 -35 79 C ATOM 953 O TRP A 154 96.721 0.371 38.365 1.00 26.67 O ANISOU 953 O TRP A 154 3548 3119 3466 -159 -37 80 O ATOM 954 CB TRP A 154 95.217 1.502 41.018 1.00 28.27 C ANISOU 954 CB TRP A 154 3752 3310 3678 -160 -58 51 C ATOM 955 CG TRP A 154 93.748 1.571 41.313 1.00 25.23 C ANISOU 955 CG TRP A 154 3372 2916 3299 -154 -63 28 C ATOM 956 CD1 TRP A 154 93.160 1.703 42.537 1.00 35.75 C ANISOU 956 CD1 TRP A 154 4703 4246 4634 -154 -66 15 C ATOM 957 CD2 TRP A 154 92.681 1.486 40.362 1.00 28.25 C ANISOU 957 CD2 TRP A 154 3761 3291 3683 -149 -64 14 C ATOM 958 NE1 TRP A 154 91.792 1.716 42.405 1.00 34.01 N ANISOU 958 NE1 TRP A 154 4488 4015 4419 -148 -69 -5 N ATOM 959 CE2 TRP A 154 91.472 1.583 41.079 1.00 24.71 C ANISOU 959 CE2 TRP A 154 3315 2834 3241 -145 -68 -6 C ATOM 960 CE3 TRP A 154 92.631 1.341 38.971 1.00 30.36 C ANISOU 960 CE3 TRP A 154 4032 3557 3947 -147 -62 17 C ATOM 961 CZ2 TRP A 154 90.227 1.540 40.453 1.00 29.74 C ANISOU 961 CZ2 TRP A 154 3957 3462 3882 -139 -71 -23 C ATOM 962 CZ3 TRP A 154 91.393 1.299 38.351 1.00 27.37 C ANISOU 962 CZ3 TRP A 154 3658 3171 3571 -141 -65 0 C ATOM 963 CH2 TRP A 154 90.208 1.398 39.092 1.00 32.97 C ANISOU 963 CH2 TRP A 154 4370 3872 4287 -137 -69 -19 C ATOM 964 N ILE A 155 98.062 0.195 40.171 1.00 23.32 N ANISOU 964 N ILE A 155 3112 2707 3042 -165 -32 96 N ATOM 965 CA ILE A 155 99.274 0.240 39.363 1.00 22.97 C ANISOU 965 CA ILE A 155 3065 2668 2994 -169 -29 117 C ATOM 966 C ILE A 155 99.361 -1.003 38.481 1.00 27.72 C ANISOU 966 C ILE A 155 3664 3273 3594 -163 -8 120 C ATOM 967 O ILE A 155 99.657 -0.912 37.283 1.00 34.50 O ANISOU 967 O ILE A 155 4527 4132 4450 -165 -8 126 O ATOM 968 CB ILE A 155 100.538 0.356 40.242 1.00 32.68 C ANISOU 968 CB ILE A 155 4287 3907 4222 -176 -28 134 C ATOM 969 CG1 ILE A 155 100.655 1.770 40.815 1.00 44.38 C ANISOU 969 CG1 ILE A 155 5771 5385 5704 -184 -49 133 C ATOM 970 CG2 ILE A 155 101.786 0.019 39.444 1.00 14.44 C ANISOU 970 CG2 ILE A 155 1973 1604 1909 -179 -19 155 C ATOM 971 CD1 ILE A 155 101.843 1.962 41.729 1.00 45.23 C ANISOU 971 CD1 ILE A 155 5871 5504 5811 -191 -51 149 C ATOM 972 N LEU A 156 99.064 -2.157 39.074 1.00 23.87 N ANISOU 972 N LEU A 156 3170 2789 3109 -156 8 114 N ATOM 973 CA LEU A 156 99.094 -3.419 38.345 1.00 28.90 C ANISOU 973 CA LEU A 156 3804 3429 3747 -150 29 115 C ATOM 974 C LEU A 156 98.029 -3.453 37.252 1.00 30.81 C ANISOU 974 C LEU A 156 4055 3664 3989 -146 28 98 C ATOM 975 O LEU A 156 98.255 -4.008 36.171 1.00 24.25 O ANISOU 975 O LEU A 156 3224 2835 3156 -145 39 102 O ATOM 976 CB LEU A 156 98.910 -4.595 39.312 1.00 19.33 C ANISOU 976 CB LEU A 156 2584 2221 2541 -143 47 112 C ATOM 977 CG LEU A 156 100.010 -4.758 40.368 1.00 30.44 C ANISOU 977 CG LEU A 156 3980 3637 3947 -146 51 130 C ATOM 978 CD1 LEU A 156 99.602 -5.738 41.464 1.00 27.53 C ANISOU 978 CD1 LEU A 156 3604 3271 3583 -138 65 125 C ATOM 979 CD2 LEU A 156 101.313 -5.196 39.720 1.00 25.75 C ANISOU 979 CD2 LEU A 156 3381 3051 3352 -149 63 152 C ATOM 980 N CYS A 157 96.878 -2.840 37.523 1.00 25.22 N ANISOU 980 N CYS A 157 3352 2947 3282 -144 14 81 N ATOM 981 CA CYS A 157 95.841 -2.728 36.505 1.00 24.88 C ANISOU 981 CA CYS A 157 3318 2898 3239 -141 10 65 C ATOM 982 C CYS A 157 96.310 -1.849 35.351 1.00 28.42 C ANISOU 982 C CYS A 157 3772 3346 3681 -147 -2 75 C ATOM 983 O CYS A 157 96.034 -2.138 34.180 1.00 24.07 O ANISOU 983 O CYS A 157 3224 2796 3127 -145 2 71 O ATOM 984 CB CYS A 157 94.553 -2.165 37.105 1.00 25.88 C ANISOU 984 CB CYS A 157 3449 3015 3370 -138 -3 45 C ATOM 985 SG CYS A 157 93.678 -3.314 38.196 1.00 27.22 S ANISOU 985 SG CYS A 157 3613 3184 3547 -129 12 29 S ATOM 986 N ALA A 158 97.052 -0.796 35.683 1.00 24.61 N ANISOU 986 N ALA A 158 3290 2864 3197 -155 -16 88 N ATOM 987 CA ALA A 158 97.573 0.096 34.657 1.00 27.02 C ANISOU 987 CA ALA A 158 3601 3168 3498 -160 -27 100 C ATOM 988 C ALA A 158 98.564 -0.648 33.770 1.00 31.58 C ANISOU 988 C ALA A 158 4175 3754 4071 -161 -11 115 C ATOM 989 O ALA A 158 98.535 -0.521 32.539 1.00 31.58 O ANISOU 989 O ALA A 158 4179 3754 4065 -162 -12 117 O ATOM 990 CB ALA A 158 98.230 1.313 35.288 1.00 22.96 C ANISOU 990 CB ALA A 158 3087 2652 2985 -169 -44 111 C ATOM 991 N VAL A 159 99.421 -1.447 34.400 1.00 34.35 N ANISOU 991 N VAL A 159 4516 4111 4422 -161 3 126 N ATOM 992 CA VAL A 159 100.387 -2.244 33.652 1.00 27.62 C ANISOU 992 CA VAL A 159 3660 3268 3568 -162 21 140 C ATOM 993 C VAL A 159 99.696 -3.276 32.761 1.00 31.66 C ANISOU 993 C VAL A 159 4172 3779 4078 -155 36 127 C ATOM 994 O VAL A 159 100.104 -3.493 31.615 1.00 24.89 O ANISOU 994 O VAL A 159 3316 2925 3215 -157 43 133 O ATOM 995 CB VAL A 159 101.364 -2.967 34.597 1.00 24.08 C ANISOU 995 CB VAL A 159 3201 2826 3123 -162 34 153 C ATOM 996 CG1 VAL A 159 102.323 -3.848 33.808 1.00 22.19 C ANISOU 996 CG1 VAL A 159 2957 2594 2883 -162 54 168 C ATOM 997 CG2 VAL A 159 102.128 -1.956 35.437 1.00 38.02 C ANISOU 997 CG2 VAL A 159 4965 4592 4889 -169 19 166 C ATOM 998 N ALA A 160 98.625 -3.879 33.270 1.00 32.52 N ANISOU 998 N ALA A 160 4280 3884 4192 -148 41 108 N ATOM 999 CA ALA A 160 97.908 -4.886 32.496 1.00 30.20 C ANISOU 999 CA ALA A 160 3986 3590 3898 -142 56 94 C ATOM 1000 C ALA A 160 97.245 -4.259 31.276 1.00 26.83 C ANISOU 1000 C ALA A 160 3569 3161 3464 -143 44 85 C ATOM 1001 O ALA A 160 97.307 -4.810 30.174 1.00 25.97 O ANISOU 1001 O ALA A 160 3460 3056 3351 -142 54 84 O ATOM 1002 CB ALA A 160 96.873 -5.588 33.359 1.00 17.82 C ANISOU 1002 CB ALA A 160 2415 2018 2337 -135 63 76 C ATOM 1003 N TRP A 161 96.635 -3.093 31.467 1.00 31.58 N ANISOU 1003 N TRP A 161 4177 3757 4066 -145 22 80 N ATOM 1004 CA TRP A 161 95.980 -2.411 30.356 1.00 27.99 C ANISOU 1004 CA TRP A 161 3731 3300 3605 -146 9 73 C ATOM 1005 C TRP A 161 96.983 -1.949 29.306 1.00 26.36 C ANISOU 1005 C TRP A 161 3527 3100 3390 -152 7 92 C ATOM 1006 O TRP A 161 96.757 -2.115 28.102 1.00 36.03 O ANISOU 1006 O TRP A 161 4754 4327 4607 -151 9 89 O ATOM 1007 CB TRP A 161 95.170 -1.214 30.857 1.00 28.90 C ANISOU 1007 CB TRP A 161 3851 3406 3722 -146 -14 65 C ATOM 1008 CG TRP A 161 93.795 -1.574 31.319 1.00 28.45 C ANISOU 1008 CG TRP A 161 3795 3343 3671 -140 -14 42 C ATOM 1009 CD1 TRP A 161 93.337 -1.589 32.604 1.00 21.16 C ANISOU 1009 CD1 TRP A 161 2870 2415 2756 -137 -16 33 C ATOM 1010 CD2 TRP A 161 92.696 -1.978 30.496 1.00 24.90 C ANISOU 1010 CD2 TRP A 161 3349 2893 3220 -134 -12 25 C ATOM 1011 NE1 TRP A 161 92.019 -1.975 32.632 1.00 22.89 N ANISOU 1011 NE1 TRP A 161 3090 2628 2978 -131 -15 12 N ATOM 1012 CE2 TRP A 161 91.601 -2.219 31.350 1.00 29.65 C ANISOU 1012 CE2 TRP A 161 3950 3487 3829 -129 -13 6 C ATOM 1013 CE3 TRP A 161 92.530 -2.158 29.120 1.00 22.94 C ANISOU 1013 CE3 TRP A 161 3103 2649 2963 -134 -10 23 C ATOM 1014 CZ2 TRP A 161 90.359 -2.631 30.872 1.00 27.85 C ANISOU 1014 CZ2 TRP A 161 3724 3257 3602 -123 -12 -15 C ATOM 1015 CZ3 TRP A 161 91.298 -2.566 28.648 1.00 25.58 C ANISOU 1015 CZ3 TRP A 161 3440 2983 3298 -128 -9 2 C ATOM 1016 CH2 TRP A 161 90.228 -2.797 29.521 1.00 27.17 C ANISOU 1016 CH2 TRP A 161 3639 3176 3507 -123 -10 -17 C ATOM 1017 N GLY A 162 98.106 -1.396 29.760 1.00 26.66 N ANISOU 1017 N GLY A 162 3563 3139 3429 -158 2 111 N ATOM 1018 CA GLY A 162 99.098 -0.893 28.829 1.00 28.00 C ANISOU 1018 CA GLY A 162 3735 3313 3592 -164 0 130 C ATOM 1019 C GLY A 162 99.741 -2.012 28.034 1.00 27.86 C ANISOU 1019 C GLY A 162 3712 3303 3569 -163 21 136 C ATOM 1020 O GLY A 162 99.905 -1.910 26.812 1.00 35.96 O ANISOU 1020 O GLY A 162 4741 4333 4587 -164 22 140 O ATOM 1021 N LEU A 163 100.074 -3.102 28.719 1.00 28.17 N ANISOU 1021 N LEU A 163 3743 3345 3614 -160 40 135 N ATOM 1022 CA LEU A 163 100.637 -4.258 28.037 1.00 36.91 C ANISOU 1022 CA LEU A 163 4845 4459 4720 -159 63 139 C ATOM 1023 C LEU A 163 99.631 -4.885 27.074 1.00 29.75 C ANISOU 1023 C LEU A 163 3942 3554 3809 -154 70 120 C ATOM 1024 O LEU A 163 100.007 -5.373 26.007 1.00 25.84 O ANISOU 1024 O LEU A 163 3446 3064 3308 -155 82 123 O ATOM 1025 CB LEU A 163 101.118 -5.299 29.047 1.00 21.95 C ANISOU 1025 CB LEU A 163 2940 2565 2834 -156 81 143 C ATOM 1026 CG LEU A 163 101.879 -6.469 28.424 1.00 34.22 C ANISOU 1026 CG LEU A 163 4487 4126 4388 -156 106 150 C ATOM 1027 CD1 LEU A 163 103.091 -5.977 27.639 1.00 14.38 C ANISOU 1027 CD1 LEU A 163 1976 1619 1870 -163 105 171 C ATOM 1028 CD2 LEU A 163 102.293 -7.458 29.492 1.00 28.77 C ANISOU 1028 CD2 LEU A 163 3786 3436 3708 -152 124 155 C ATOM 1029 N ALA A 164 98.352 -4.860 27.442 1.00 28.43 N ANISOU 1029 N ALA A 164 3777 3381 3645 -149 63 100 N ATOM 1030 CA ALA A 164 97.325 -5.423 26.571 1.00 26.70 C ANISOU 1030 CA ALA A 164 3560 3163 3422 -145 68 80 C ATOM 1031 C ALA A 164 97.184 -4.600 25.294 1.00 28.76 C ANISOU 1031 C ALA A 164 3829 3427 3671 -148 55 83 C ATOM 1032 O ALA A 164 97.088 -5.157 24.196 1.00 26.79 O ANISOU 1032 O ALA A 164 3581 3185 3415 -148 65 77 O ATOM 1033 CB ALA A 164 95.992 -5.508 27.297 1.00 24.98 C ANISOU 1033 CB ALA A 164 3343 2938 3211 -139 63 59 C ATOM 1034 N LEU A 165 97.199 -3.276 25.435 1.00 29.11 N ANISOU 1034 N LEU A 165 3879 3467 3713 -152 32 91 N ATOM 1035 CA LEU A 165 97.130 -2.402 24.269 1.00 38.51 C ANISOU 1035 CA LEU A 165 5077 4661 4893 -155 18 97 C ATOM 1036 C LEU A 165 98.333 -2.632 23.367 1.00 37.01 C ANISOU 1036 C LEU A 165 4886 4480 4696 -160 30 114 C ATOM 1037 O LEU A 165 98.211 -2.735 22.134 1.00 41.75 O ANISOU 1037 O LEU A 165 5490 5088 5286 -160 32 112 O ATOM 1038 CB LEU A 165 97.080 -0.935 24.698 1.00 29.38 C ANISOU 1038 CB LEU A 165 3926 3498 3739 -158 -6 105 C ATOM 1039 CG LEU A 165 95.722 -0.343 25.062 1.00 46.12 C ANISOU 1039 CG LEU A 165 6050 5610 5863 -154 -22 88 C ATOM 1040 CD1 LEU A 165 95.909 0.910 25.899 1.00 24.60 C ANISOU 1040 CD1 LEU A 165 3327 2876 3144 -157 -41 97 C ATOM 1041 CD2 LEU A 165 94.952 -0.028 23.792 1.00 36.65 C ANISOU 1041 CD2 LEU A 165 4857 4415 4654 -152 -31 81 C ATOM 1042 N LEU A 166 99.489 -2.762 24.011 1.00 44.06 N ANISOU 1042 N LEU A 166 5774 5373 5594 -163 37 131 N ATOM 1043 CA LEU A 166 100.747 -2.957 23.311 1.00 38.18 C ANISOU 1043 CA LEU A 166 5028 4636 4845 -168 49 149 C ATOM 1044 C LEU A 166 100.746 -4.270 22.533 1.00 33.68 C ANISOU 1044 C LEU A 166 4453 4072 4271 -166 72 141 C ATOM 1045 O LEU A 166 101.324 -4.362 21.450 1.00 42.20 O ANISOU 1045 O LEU A 166 5534 5159 5341 -169 78 149 O ATOM 1046 CB LEU A 166 101.901 -2.934 24.315 1.00 42.02 C ANISOU 1046 CB LEU A 166 5507 5119 5339 -171 53 167 C ATOM 1047 CG LEU A 166 103.310 -2.708 23.777 1.00 43.42 C ANISOU 1047 CG LEU A 166 5683 5301 5512 -177 58 191 C ATOM 1048 CD1 LEU A 166 103.427 -1.331 23.147 1.00 49.24 C ANISOU 1048 CD1 LEU A 166 6428 6038 6243 -182 37 201 C ATOM 1049 CD2 LEU A 166 104.334 -2.887 24.885 1.00 50.94 C ANISOU 1049 CD2 LEU A 166 6627 6252 6474 -180 64 205 C ATOM 1050 N LEU A 167 100.089 -5.282 23.093 1.00 37.01 N ANISOU 1050 N LEU A 167 4870 4492 4700 -160 85 124 N ATOM 1051 CA LEU A 167 99.968 -6.578 22.432 1.00 34.40 C ANISOU 1051 CA LEU A 167 4535 4168 4368 -158 108 112 C ATOM 1052 C LEU A 167 98.948 -6.556 21.299 1.00 32.70 C ANISOU 1052 C LEU A 167 4326 3957 4143 -156 103 95 C ATOM 1053 O LEU A 167 99.075 -7.299 20.326 1.00 40.07 O ANISOU 1053 O LEU A 167 5257 4898 5069 -157 118 90 O ATOM 1054 CB LEU A 167 99.588 -7.658 23.448 1.00 34.28 C ANISOU 1054 CB LEU A 167 4511 4147 4365 -152 124 100 C ATOM 1055 CG LEU A 167 100.656 -8.068 24.463 1.00 30.49 C ANISOU 1055 CG LEU A 167 4023 3666 3896 -153 136 116 C ATOM 1056 CD1 LEU A 167 100.018 -8.725 25.675 1.00 25.04 C ANISOU 1056 CD1 LEU A 167 3327 2969 3217 -147 143 104 C ATOM 1057 CD2 LEU A 167 101.653 -9.007 23.821 1.00 27.81 C ANISOU 1057 CD2 LEU A 167 3677 3332 3556 -155 160 126 C ATOM 1058 N THR A 168 97.931 -5.710 21.432 1.00 36.33 N ANISOU 1058 N THR A 168 4791 4412 4600 -154 82 85 N ATOM 1059 CA THR A 168 96.862 -5.659 20.437 1.00 39.24 C ANISOU 1059 CA THR A 168 5165 4786 4959 -152 75 68 C ATOM 1060 C THR A 168 97.219 -4.822 19.202 1.00 47.91 C ANISOU 1060 C THR A 168 6269 5892 6042 -157 64 81 C ATOM 1061 O THR A 168 96.704 -5.076 18.111 1.00 42.91 O ANISOU 1061 O THR A 168 5638 5267 5398 -157 66 70 O ATOM 1062 CB THR A 168 95.557 -5.114 21.056 1.00 28.97 C ANISOU 1062 CB THR A 168 3868 3478 3663 -148 57 52 C ATOM 1063 OG1 THR A 168 95.224 -5.886 22.214 1.00 23.85 O ANISOU 1063 OG1 THR A 168 3213 2822 3028 -143 68 41 O ATOM 1064 CG2 THR A 168 94.400 -5.195 20.065 1.00 36.47 C ANISOU 1064 CG2 THR A 168 4820 4433 4603 -145 52 33 C ATOM 1065 N ILE A 169 98.118 -3.850 19.360 1.00 54.63 N ANISOU 1065 N ILE A 169 7124 6741 6893 -161 53 103 N ATOM 1066 CA ILE A 169 98.454 -2.952 18.244 1.00 57.90 C ANISOU 1066 CA ILE A 169 7543 7161 7294 -166 41 117 C ATOM 1067 C ILE A 169 98.899 -3.645 16.931 1.00 65.08 C ANISOU 1067 C ILE A 169 8452 8084 8191 -168 57 118 C ATOM 1068 O ILE A 169 98.363 -3.320 15.853 1.00 52.36 O ANISOU 1068 O ILE A 169 6846 6481 6566 -168 49 113 O ATOM 1069 CB ILE A 169 99.564 -1.951 18.667 1.00 55.29 C ANISOU 1069 CB ILE A 169 7215 6826 6967 -171 31 143 C ATOM 1070 CG1 ILE A 169 98.996 -0.895 19.614 1.00 65.76 C ANISOU 1070 CG1 ILE A 169 8543 8141 8301 -169 9 142 C ATOM 1071 CG2 ILE A 169 100.190 -1.284 17.449 1.00 56.79 C ANISOU 1071 CG2 ILE A 169 7409 7024 7144 -175 26 159 C ATOM 1072 CD1 ILE A 169 100.038 0.074 20.139 1.00 70.40 C ANISOU 1072 CD1 ILE A 169 9131 8723 8894 -174 0 165 C ATOM 1073 N PRO A 170 99.856 -4.601 17.004 1.00 60.67 N ANISOU 1073 N PRO A 170 7887 7528 7636 -170 80 123 N ATOM 1074 CA PRO A 170 100.302 -5.227 15.751 1.00 71.92 C ANISOU 1074 CA PRO A 170 9312 8965 9050 -174 96 124 C ATOM 1075 C PRO A 170 99.178 -5.910 14.977 1.00 69.45 C ANISOU 1075 C PRO A 170 9000 8660 8728 -171 101 99 C ATOM 1076 O PRO A 170 99.200 -5.910 13.746 1.00 78.54 O ANISOU 1076 O PRO A 170 10153 9822 9864 -173 103 98 O ATOM 1077 CB PRO A 170 101.337 -6.260 16.225 1.00 70.67 C ANISOU 1077 CB PRO A 170 9146 8805 8901 -175 121 131 C ATOM 1078 CG PRO A 170 100.986 -6.522 17.644 1.00 65.47 C ANISOU 1078 CG PRO A 170 8482 8136 8258 -171 121 124 C ATOM 1079 CD PRO A 170 100.530 -5.204 18.169 1.00 63.45 C ANISOU 1079 CD PRO A 170 8232 7873 8003 -170 93 129 C ATOM 1080 N SER A 171 98.214 -6.483 15.688 1.00 57.94 N ANISOU 1080 N SER A 171 7538 7196 7279 -165 104 78 N ATOM 1081 CA SER A 171 97.080 -7.122 15.035 1.00 58.90 C ANISOU 1081 CA SER A 171 7659 7324 7395 -162 108 53 C ATOM 1082 C SER A 171 96.211 -6.099 14.316 1.00 70.22 C ANISOU 1082 C SER A 171 9102 8764 8816 -162 84 49 C ATOM 1083 O SER A 171 95.719 -6.351 13.214 1.00 82.27 O ANISOU 1083 O SER A 171 10628 10301 10328 -163 85 38 O ATOM 1084 CB SER A 171 96.239 -7.892 16.054 1.00 72.98 C ANISOU 1084 CB SER A 171 9437 9098 9193 -157 115 32 C ATOM 1085 OG SER A 171 97.024 -8.844 16.750 1.00 90.78 O ANISOU 1085 OG SER A 171 11684 11349 11461 -157 138 36 O ATOM 1086 N ALA A 172 96.032 -4.941 14.942 1.00 59.04 N ANISOU 1086 N ALA A 172 7690 7339 7404 -161 61 60 N ATOM 1087 CA ALA A 172 95.214 -3.888 14.360 1.00 54.08 C ANISOU 1087 CA ALA A 172 7068 6714 6766 -159 38 59 C ATOM 1088 C ALA A 172 95.850 -3.305 13.106 1.00 70.51 C ANISOU 1088 C ALA A 172 9154 8807 8830 -164 33 76 C ATOM 1089 O ALA A 172 95.151 -2.989 12.144 1.00 78.20 O ANISOU 1089 O ALA A 172 10131 9790 9790 -164 23 70 O ATOM 1090 CB ALA A 172 94.963 -2.789 15.383 1.00 57.06 C ANISOU 1090 CB ALA A 172 7449 7078 7154 -157 17 67 C ATOM 1091 N LEU A 173 97.173 -3.163 13.112 1.00 76.17 N ANISOU 1091 N LEU A 173 9870 9523 9548 -169 40 98 N ATOM 1092 CA LEU A 173 97.838 -2.574 11.953 1.00 66.44 C ANISOU 1092 CA LEU A 173 8642 8301 8300 -173 37 116 C ATOM 1093 C LEU A 173 97.752 -3.455 10.706 1.00 80.13 C ANISOU 1093 C LEU A 173 10375 10052 10019 -175 52 104 C ATOM 1094 O LEU A 173 97.612 -2.951 9.591 1.00 84.75 O ANISOU 1094 O LEU A 173 10965 10650 10587 -177 43 109 O ATOM 1095 CB LEU A 173 99.299 -2.278 12.282 1.00 65.02 C ANISOU 1095 CB LEU A 173 8462 8117 8126 -178 42 141 C ATOM 1096 CG LEU A 173 99.481 -1.292 13.436 1.00 64.93 C ANISOU 1096 CG LEU A 173 8452 8091 8129 -178 26 154 C ATOM 1097 CD1 LEU A 173 100.954 -1.070 13.715 1.00 70.35 C ANISOU 1097 CD1 LEU A 173 9136 8773 8820 -183 33 178 C ATOM 1098 CD2 LEU A 173 98.778 0.026 13.136 1.00 67.21 C ANISOU 1098 CD2 LEU A 173 8747 8378 8412 -176 0 159 C ATOM 1099 N TYR A 174 97.838 -4.768 10.899 1.00 71.48 N ANISOU 1099 N TYR A 174 9274 8958 8929 -175 75 89 N ATOM 1100 CA TYR A 174 97.768 -5.714 9.788 1.00 69.56 C ANISOU 1100 CA TYR A 174 9028 8729 8673 -178 93 75 C ATOM 1101 C TYR A 174 96.364 -5.813 9.196 1.00 64.67 C ANISOU 1101 C TYR A 174 8410 8119 8043 -174 83 52 C ATOM 1102 O TYR A 174 96.197 -6.194 8.038 1.00 76.98 O ANISOU 1102 O TYR A 174 9969 9694 9586 -177 90 43 O ATOM 1103 CB TYR A 174 98.256 -7.095 10.237 1.00 78.29 C ANISOU 1103 CB TYR A 174 10125 9831 9790 -178 121 66 C ATOM 1104 CG TYR A 174 99.767 -7.225 10.260 1.00 91.83 C ANISOU 1104 CG TYR A 174 11838 11545 11509 -183 136 88 C ATOM 1105 CD1 TYR A 174 100.545 -6.378 11.038 1.00 89.56 C ANISOU 1105 CD1 TYR A 174 11552 11246 11229 -184 125 112 C ATOM 1106 CD2 TYR A 174 100.413 -8.197 9.506 1.00 90.47 C ANISOU 1106 CD2 TYR A 174 11662 11382 11331 -187 160 85 C ATOM 1107 CE1 TYR A 174 101.922 -6.490 11.065 1.00 92.27 C ANISOU 1107 CE1 TYR A 174 11893 11588 11576 -188 138 132 C ATOM 1108 CE2 TYR A 174 101.792 -8.319 9.527 1.00 92.57 C ANISOU 1108 CE2 TYR A 174 11926 11646 11601 -192 174 106 C ATOM 1109 CZ TYR A 174 102.541 -7.462 10.307 1.00 95.16 C ANISOU 1109 CZ TYR A 174 12255 11964 11938 -192 162 129 C ATOM 1110 OH TYR A 174 103.912 -7.576 10.333 1.00 85.58 O ANISOU 1110 OH TYR A 174 11040 10749 10729 -196 175 150 O ATOM 1111 N ARG A 175 95.357 -5.479 9.995 1.00 68.77 N ANISOU 1111 N ARG A 175 8634 9773 7722 2104 -447 1221 N ATOM 1112 CA ARG A 175 93.981 -5.485 9.516 1.00 83.56 C ANISOU 1112 CA ARG A 175 10527 11646 9578 2097 -435 1151 C ATOM 1113 C ARG A 175 93.784 -4.390 8.465 1.00 80.82 C ANISOU 1113 C ARG A 175 10187 11311 9212 2079 -478 1125 C ATOM 1114 O ARG A 175 94.295 -3.277 8.611 1.00 76.97 O ANISOU 1114 O ARG A 175 9699 10836 8710 2072 -542 1148 O ATOM 1115 CB ARG A 175 93.005 -5.305 10.680 1.00 58.93 C ANISOU 1115 CB ARG A 175 7428 8527 6437 2103 -458 1124 C ATOM 1116 CG ARG A 175 91.552 -5.518 10.301 1.00 72.30 C ANISOU 1116 CG ARG A 175 9139 10217 8115 2099 -436 1053 C ATOM 1117 CD ARG A 175 91.182 -6.989 10.189 1.00 69.09 C ANISOU 1117 CD ARG A 175 8728 9794 7731 2109 -354 1037 C ATOM 1118 NE ARG A 175 90.710 -7.536 11.458 1.00 70.68 N ANISOU 1118 NE ARG A 175 8937 9988 7931 2123 -342 1035 N ATOM 1119 CZ ARG A 175 90.030 -8.673 11.573 1.00 62.53 C ANISOU 1119 CZ ARG A 175 7908 8943 6910 2131 -280 1008 C ATOM 1120 NH1 ARG A 175 89.737 -9.384 10.493 1.00 71.94 N ANISOU 1120 NH1 ARG A 175 9095 10126 8114 2127 -225 980 N ATOM 1121 NH2 ARG A 175 89.639 -9.099 12.766 1.00 60.53 N ANISOU 1121 NH2 ARG A 175 7661 8683 6654 2144 -273 1009 N ATOM 1122 N VAL A 176 93.034 -4.712 7.414 1.00 63.38 N ANISOU 1122 N VAL A 176 7983 9098 7002 2071 -442 1076 N ATOM 1123 CA VAL A 176 92.890 -3.829 6.262 1.00 73.11 C ANISOU 1123 CA VAL A 176 9219 10339 8219 2054 -472 1051 C ATOM 1124 C VAL A 176 91.626 -4.136 5.449 1.00 68.06 C ANISOU 1124 C VAL A 176 8593 9696 7570 2047 -440 982 C ATOM 1125 O VAL A 176 91.135 -5.276 5.424 1.00 56.24 O ANISOU 1125 O VAL A 176 7096 8186 6088 2055 -376 961 O ATOM 1126 CB VAL A 176 94.126 -3.927 5.334 1.00 63.42 C ANISOU 1126 CB VAL A 176 7969 9112 7014 2050 -458 1093 C ATOM 1127 CG1 VAL A 176 94.092 -5.219 4.529 1.00 51.60 C ANISOU 1127 CG1 VAL A 176 6461 7602 5544 2053 -377 1082 C ATOM 1128 CG2 VAL A 176 94.215 -2.718 4.409 1.00 76.07 C ANISOU 1128 CG2 VAL A 176 9575 10729 8600 2033 -510 1081 C ATOM 1129 N VAL A 177 91.090 -3.092 4.821 1.00 57.95 N ANISOU 1129 N VAL A 177 7326 8426 6265 2033 -484 946 N ATOM 1130 CA VAL A 177 89.987 -3.197 3.870 1.00 73.20 C ANISOU 1130 CA VAL A 177 9270 10356 8186 2023 -461 882 C ATOM 1131 C VAL A 177 90.464 -3.766 2.524 1.00 74.44 C ANISOU 1131 C VAL A 177 9410 10507 8365 2018 -412 885 C ATOM 1132 O VAL A 177 91.585 -3.498 2.089 1.00 74.57 O ANISOU 1132 O VAL A 177 9411 10528 8395 2014 -424 929 O ATOM 1133 CB VAL A 177 89.320 -1.812 3.677 1.00 73.09 C ANISOU 1133 CB VAL A 177 9275 10357 8138 2009 -530 847 C ATOM 1134 CG1 VAL A 177 88.320 -1.822 2.535 1.00 70.28 C ANISOU 1134 CG1 VAL A 177 8930 10000 7772 1998 -509 785 C ATOM 1135 CG2 VAL A 177 88.649 -1.376 4.973 1.00 64.81 C ANISOU 1135 CG2 VAL A 177 8244 9312 7067 2015 -570 835 C ATOM 1136 N ARG A 178 89.602 -4.541 1.869 1.00 58.73 N ANISOU 1136 N ARG A 178 7427 8509 6381 2017 -358 838 N ATOM 1137 CA ARG A 178 89.952 -5.245 0.638 1.00 63.12 C ANISOU 1137 CA ARG A 178 7968 9057 6959 2013 -304 836 C ATOM 1138 C ARG A 178 88.744 -5.385 -0.292 1.00 60.53 C ANISOU 1138 C ARG A 178 7653 8726 6619 2004 -278 768 C ATOM 1139 O ARG A 178 87.759 -6.040 0.051 1.00 61.02 O ANISOU 1139 O ARG A 178 7727 8780 6678 2010 -244 730 O ATOM 1140 CB ARG A 178 90.525 -6.625 0.969 1.00 72.54 C ANISOU 1140 CB ARG A 178 9144 10235 8185 2028 -237 870 C ATOM 1141 CG ARG A 178 90.778 -7.510 -0.239 1.00 73.82 C ANISOU 1141 CG ARG A 178 9291 10387 8370 2026 -172 865 C ATOM 1142 CD ARG A 178 91.239 -8.901 0.178 1.00 82.30 C ANISOU 1142 CD ARG A 178 10350 11446 9475 2041 -106 895 C ATOM 1143 NE ARG A 178 92.508 -8.872 0.900 1.00109.91 N ANISOU 1143 NE ARG A 178 13831 14944 12986 2049 -122 963 N ATOM 1144 CZ ARG A 178 93.115 -9.951 1.387 1.00114.86 C ANISOU 1144 CZ ARG A 178 14443 15559 13640 2063 -74 1000 C ATOM 1145 NH1 ARG A 178 92.568 -11.149 1.231 1.00103.91 N ANISOU 1145 NH1 ARG A 178 13055 14158 12267 2070 -5 975 N ATOM 1146 NH2 ARG A 178 94.268 -9.832 2.031 1.00111.72 N ANISOU 1146 NH2 ARG A 178 14032 15164 13255 2070 -94 1061 N ATOM 1147 N GLU A 179 88.821 -4.753 -1.461 1.00 81.47 N ANISOU 1147 N GLU A 179 10304 11385 9264 1990 -295 753 N ATOM 1148 CA GLU A 179 87.724 -4.764 -2.429 1.00 65.73 C ANISOU 1148 CA GLU A 179 8324 9391 7259 1980 -276 689 C ATOM 1149 C GLU A 179 87.686 -6.042 -3.274 1.00 58.13 C ANISOU 1149 C GLU A 179 7350 8415 6324 1983 -195 677 C ATOM 1150 O GLU A 179 88.731 -6.569 -3.657 1.00 72.93 O ANISOU 1150 O GLU A 179 9203 10283 8223 1986 -165 719 O ATOM 1151 CB GLU A 179 87.835 -3.533 -3.332 1.00 64.65 C ANISOU 1151 CB GLU A 179 8190 9268 7104 1963 -329 678 C ATOM 1152 CG GLU A 179 86.605 -3.234 -4.171 1.00 73.41 C ANISOU 1152 CG GLU A 179 9317 10380 8194 1951 -328 609 C ATOM 1153 CD GLU A 179 86.596 -1.807 -4.684 1.00 84.80 C ANISOU 1153 CD GLU A 179 10769 11840 9613 1936 -397 599 C ATOM 1154 OE1 GLU A 179 87.145 -0.923 -3.992 1.00 81.10 O ANISOU 1154 OE1 GLU A 179 10301 11381 9133 1936 -456 632 O ATOM 1155 OE2 GLU A 179 86.045 -1.568 -5.779 1.00 85.03 O ANISOU 1155 OE2 GLU A 179 10804 11871 9634 1924 -391 557 O ATOM 1156 N GLU A 180 86.481 -6.511 -3.596 1.00 70.02 N ANISOU 1156 N GLU A 180 8870 9914 7822 1981 -161 618 N ATOM 1157 CA GLU A 180 86.315 -7.705 -4.430 1.00 78.23 C ANISOU 1157 CA GLU A 180 9900 10939 8884 1984 -85 600 C ATOM 1158 C GLU A 180 85.126 -7.548 -5.378 1.00 68.90 C ANISOU 1158 C GLU A 180 8734 9758 7686 1972 -75 532 C ATOM 1159 O GLU A 180 84.178 -6.826 -5.073 1.00 67.05 O ANISOU 1159 O GLU A 180 8520 9532 7423 1967 -114 492 O ATOM 1160 CB GLU A 180 86.147 -8.952 -3.561 1.00 52.06 C ANISOU 1160 CB GLU A 180 6582 7610 5586 2000 -30 608 C ATOM 1161 CG GLU A 180 87.170 -10.035 -3.857 1.00 81.07 C ANISOU 1161 CG GLU A 180 10232 11273 9296 2009 28 652 C ATOM 1162 CD GLU A 180 87.159 -11.144 -2.828 1.00 93.37 C ANISOU 1162 CD GLU A 180 11787 12819 10871 2026 73 669 C ATOM 1163 OE1 GLU A 180 88.241 -11.697 -2.539 1.00 99.49 O ANISOU 1163 OE1 GLU A 180 12543 13588 11670 2035 94 723 O ATOM 1164 OE2 GLU A 180 86.069 -11.464 -2.309 1.00 82.33 O ANISOU 1164 OE2 GLU A 180 10404 11416 9461 2030 86 627 O ATOM 1165 N TYR A 181 85.176 -8.229 -6.523 1.00 65.40 N ANISOU 1165 N TYR A 181 8281 9308 7260 1969 -22 518 N ATOM 1166 CA TYR A 181 84.272 -7.919 -7.633 1.00 67.97 C ANISOU 1166 CA TYR A 181 8619 9637 7572 1956 -19 460 C ATOM 1167 C TYR A 181 83.329 -9.035 -8.100 1.00 76.81 C ANISOU 1167 C TYR A 181 9742 10742 8699 1959 51 412 C ATOM 1168 O TYR A 181 82.457 -8.790 -8.934 1.00 82.31 O ANISOU 1168 O TYR A 181 10451 11441 9382 1948 53 360 O ATOM 1169 CB TYR A 181 85.099 -7.451 -8.832 1.00 51.47 C ANISOU 1169 CB TYR A 181 6516 7553 5489 1944 -29 479 C ATOM 1170 CG TYR A 181 86.066 -6.343 -8.494 1.00 57.94 C ANISOU 1170 CG TYR A 181 7329 8385 6300 1940 -97 526 C ATOM 1171 CD1 TYR A 181 85.617 -5.046 -8.292 1.00 59.77 C ANISOU 1171 CD1 TYR A 181 7578 8632 6502 1931 -167 506 C ATOM 1172 CD2 TYR A 181 87.427 -6.593 -8.372 1.00 54.99 C ANISOU 1172 CD2 TYR A 181 6933 8009 5950 1946 -90 590 C ATOM 1173 CE1 TYR A 181 86.493 -4.027 -7.979 1.00 72.52 C ANISOU 1173 CE1 TYR A 181 9187 10258 8108 1927 -230 549 C ATOM 1174 CE2 TYR A 181 88.313 -5.578 -8.059 1.00 71.05 C ANISOU 1174 CE2 TYR A 181 8962 10056 7977 1943 -152 633 C ATOM 1175 CZ TYR A 181 87.839 -4.297 -7.864 1.00 70.91 C ANISOU 1175 CZ TYR A 181 8962 10053 7929 1933 -222 612 C ATOM 1176 OH TYR A 181 88.710 -3.279 -7.552 1.00 57.84 O ANISOU 1176 OH TYR A 181 7302 8410 6266 1929 -284 655 O ATOM 1177 N PHE A 182 83.491 -10.248 -7.582 1.00 87.10 N ANISOU 1177 N PHE A 182 11037 12032 10026 1973 108 429 N ATOM 1178 CA PHE A 182 82.664 -11.367 -8.037 1.00 79.11 C ANISOU 1178 CA PHE A 182 10028 11007 9024 1976 177 387 C ATOM 1179 C PHE A 182 82.046 -12.161 -6.887 1.00 81.18 C ANISOU 1179 C PHE A 182 10297 11259 9287 1990 205 378 C ATOM 1180 O PHE A 182 82.557 -13.221 -6.524 1.00 96.25 O ANISOU 1180 O PHE A 182 12193 13156 11222 2002 254 408 O ATOM 1181 CB PHE A 182 83.476 -12.314 -8.924 1.00 83.90 C ANISOU 1181 CB PHE A 182 10612 11603 9663 1978 237 412 C ATOM 1182 CG PHE A 182 84.211 -11.628 -10.039 1.00 90.71 C ANISOU 1182 CG PHE A 182 11465 12474 10528 1966 214 428 C ATOM 1183 CD1 PHE A 182 85.593 -11.682 -10.107 1.00 92.01 C ANISOU 1183 CD1 PHE A 182 11608 12639 10712 1969 213 490 C ATOM 1184 CD2 PHE A 182 83.524 -10.926 -11.016 1.00 93.25 C ANISOU 1184 CD2 PHE A 182 11798 12803 10830 1951 194 381 C ATOM 1185 CE1 PHE A 182 86.276 -11.054 -11.129 1.00 93.87 C ANISOU 1185 CE1 PHE A 182 11834 12882 10951 1957 192 505 C ATOM 1186 CE2 PHE A 182 84.203 -10.293 -12.041 1.00 94.67 C ANISOU 1186 CE2 PHE A 182 11969 12991 11012 1940 172 395 C ATOM 1187 CZ PHE A 182 85.581 -10.358 -12.097 1.00105.38 C ANISOU 1187 CZ PHE A 182 13303 14347 12389 1943 172 457 C ATOM 1188 N PRO A 183 80.944 -11.659 -6.308 1.00 65.82 N ANISOU 1188 N PRO A 183 8374 9318 7315 1988 174 335 N ATOM 1189 CA PRO A 183 80.230 -10.415 -6.610 1.00 61.10 C ANISOU 1189 CA PRO A 183 7795 8735 6686 1974 114 296 C ATOM 1190 C PRO A 183 80.907 -9.220 -5.948 1.00 73.68 C ANISOU 1190 C PRO A 183 9389 10342 8264 1972 38 335 C ATOM 1191 O PRO A 183 81.865 -9.431 -5.203 1.00 86.71 O ANISOU 1191 O PRO A 183 11025 11990 9929 1981 35 390 O ATOM 1192 CB PRO A 183 78.828 -10.657 -6.025 1.00 64.81 C ANISOU 1192 CB PRO A 183 8287 9201 7138 1978 124 242 C ATOM 1193 CG PRO A 183 78.889 -11.999 -5.314 1.00 46.62 C ANISOU 1193 CG PRO A 183 5975 6882 4858 1994 185 257 C ATOM 1194 CD PRO A 183 80.329 -12.355 -5.168 1.00 78.55 C ANISOU 1194 CD PRO A 183 9995 10922 8928 2001 196 326 C ATOM 1195 N PRO A 184 80.448 -7.986 -6.233 1.00 61.77 N ANISOU 1195 N PRO A 184 7895 8847 6727 1959 -22 307 N ATOM 1196 CA PRO A 184 81.080 -6.881 -5.507 1.00 60.66 C ANISOU 1196 CA PRO A 184 7756 8720 6573 1957 -94 345 C ATOM 1197 C PRO A 184 80.885 -7.008 -4.001 1.00 70.51 C ANISOU 1197 C PRO A 184 9011 9966 7815 1970 -108 359 C ATOM 1198 O PRO A 184 79.796 -7.368 -3.549 1.00 68.30 O ANISOU 1198 O PRO A 184 8746 9681 7524 1974 -92 317 O ATOM 1199 CB PRO A 184 80.354 -5.645 -6.045 1.00 56.97 C ANISOU 1199 CB PRO A 184 7306 8266 6074 1942 -149 302 C ATOM 1200 CG PRO A 184 79.863 -6.052 -7.390 1.00 61.60 C ANISOU 1200 CG PRO A 184 7892 8848 6666 1933 -106 260 C ATOM 1201 CD PRO A 184 79.526 -7.511 -7.279 1.00 61.57 C ANISOU 1201 CD PRO A 184 7882 8826 6683 1945 -28 249 C ATOM 1202 N LYS A 185 81.929 -6.693 -3.243 1.00 70.94 N ANISOU 1202 N LYS A 185 9054 10025 7875 1976 -140 417 N ATOM 1203 CA LYS A 185 81.885 -6.780 -1.790 1.00 59.76 C ANISOU 1203 CA LYS A 185 7643 8607 6454 1988 -157 437 C ATOM 1204 C LYS A 185 83.139 -6.161 -1.189 1.00 52.51 C ANISOU 1204 C LYS A 185 6713 7697 5540 1991 -203 502 C ATOM 1205 O LYS A 185 84.204 -6.158 -1.812 1.00 51.79 O ANISOU 1205 O LYS A 185 6604 7607 5468 1988 -198 541 O ATOM 1206 CB LYS A 185 81.740 -8.237 -1.328 1.00 51.22 C ANISOU 1206 CB LYS A 185 6556 7509 5397 2003 -85 440 C ATOM 1207 CG LYS A 185 80.846 -8.406 -0.104 1.00 62.46 C ANISOU 1207 CG LYS A 185 7995 8930 6806 2012 -91 418 C ATOM 1208 CD LYS A 185 80.808 -9.847 0.395 1.00 53.88 C ANISOU 1208 CD LYS A 185 6901 7826 5743 2028 -21 426 C ATOM 1209 CE LYS A 185 80.151 -10.788 -0.606 1.00 61.35 C ANISOU 1209 CE LYS A 185 7846 8761 6701 2025 47 383 C ATOM 1210 NZ LYS A 185 80.045 -12.178 -0.072 1.00 54.91 N ANISOU 1210 NZ LYS A 185 7025 7930 5909 2041 114 389 N ATOM 1211 N VAL A 186 83.006 -5.640 0.025 1.00 44.39 N ANISOU 1211 N VAL A 186 5694 6674 4496 1996 -248 513 N ATOM 1212 CA VAL A 186 84.140 -5.087 0.750 1.00 61.96 C ANISOU 1212 CA VAL A 186 7910 8907 6726 2000 -293 574 C ATOM 1213 C VAL A 186 84.451 -5.950 1.970 1.00 52.94 C ANISOU 1213 C VAL A 186 6761 7755 5599 2018 -265 608 C ATOM 1214 O VAL A 186 83.592 -6.155 2.828 1.00 54.72 O ANISOU 1214 O VAL A 186 7001 7977 5813 2025 -264 582 O ATOM 1215 CB VAL A 186 83.874 -3.642 1.190 1.00 53.62 C ANISOU 1215 CB VAL A 186 6870 7867 5637 1992 -375 566 C ATOM 1216 CG1 VAL A 186 85.054 -3.109 1.975 1.00 44.65 C ANISOU 1216 CG1 VAL A 186 5722 6737 4505 1997 -420 630 C ATOM 1217 CG2 VAL A 186 83.595 -2.768 -0.023 1.00 38.12 C ANISOU 1217 CG2 VAL A 186 4912 5913 3658 1974 -403 534 C ATOM 1218 N LEU A 187 85.679 -6.457 2.037 1.00 51.39 N ANISOU 1218 N LEU A 187 6543 7554 5430 2025 -244 666 N ATOM 1219 CA LEU A 187 86.069 -7.388 3.093 1.00 47.70 C ANISOU 1219 CA LEU A 187 6067 7077 4982 2042 -211 701 C ATOM 1220 C LEU A 187 87.076 -6.789 4.073 1.00 47.22 C ANISOU 1220 C LEU A 187 5998 7022 4920 2047 -261 760 C ATOM 1221 O LEU A 187 88.010 -6.105 3.667 1.00 38.59 O ANISOU 1221 O LEU A 187 4895 5938 3829 2040 -295 795 O ATOM 1222 CB LEU A 187 86.655 -8.655 2.472 1.00 56.90 C ANISOU 1222 CB LEU A 187 7212 8227 6180 2048 -136 720 C ATOM 1223 CG LEU A 187 85.799 -9.320 1.396 1.00 47.97 C ANISOU 1223 CG LEU A 187 6085 7088 5053 2043 -81 666 C ATOM 1224 CD1 LEU A 187 86.552 -10.470 0.753 1.00 54.69 C ANISOU 1224 CD1 LEU A 187 6915 7927 5938 2048 -13 693 C ATOM 1225 CD2 LEU A 187 84.492 -9.802 1.997 1.00 39.97 C ANISOU 1225 CD2 LEU A 187 5091 6069 4028 2048 -60 617 C ATOM 1226 N CYS A 188 86.884 -7.054 5.362 1.00 59.45 N ANISOU 1226 N CYS A 188 7554 8569 6467 2060 -265 771 N ATOM 1227 CA CYS A 188 87.854 -6.661 6.383 1.00 44.16 C ANISOU 1227 CA CYS A 188 5609 6637 4533 2067 -304 829 C ATOM 1228 C CYS A 188 88.718 -7.865 6.755 1.00 44.81 C ANISOU 1228 C CYS A 188 5671 6707 4649 2082 -248 876 C ATOM 1229 O CYS A 188 88.188 -8.907 7.142 1.00 51.80 O ANISOU 1229 O CYS A 188 6559 7580 5545 2092 -196 859 O ATOM 1230 CB CYS A 188 87.135 -6.108 7.617 1.00 45.79 C ANISOU 1230 CB CYS A 188 5835 6849 4715 2071 -349 814 C ATOM 1231 SG CYS A 188 88.196 -5.277 8.822 1.00 62.56 S ANISOU 1231 SG CYS A 188 7953 8983 6834 2077 -415 879 S ATOM 1232 N GLY A 189 90.040 -7.738 6.655 1.00 53.25 N ANISOU 1232 N GLY A 189 6720 7777 5734 2082 -258 934 N ATOM 1233 CA GLY A 189 90.881 -8.899 6.903 1.00 60.42 C ANISOU 1233 CA GLY A 189 7608 8673 6674 2096 -203 978 C ATOM 1234 C GLY A 189 92.355 -8.650 7.151 1.00 70.94 C ANISOU 1234 C GLY A 189 8921 10010 8022 2099 -225 1048 C ATOM 1235 O GLY A 189 92.843 -7.538 6.989 1.00 71.82 O ANISOU 1235 O GLY A 189 9033 10135 8121 2090 -284 1066 O ATOM 1236 N VAL A 190 93.067 -9.704 7.539 1.00 80.35 N ANISOU 1236 N VAL A 190 10096 11190 9241 2112 -176 1088 N ATOM 1237 CA VAL A 190 94.483 -9.609 7.887 1.00 78.13 C ANISOU 1237 CA VAL A 190 9797 10912 8978 2117 -192 1157 C ATOM 1238 C VAL A 190 95.370 -9.435 6.649 1.00 87.99 C ANISOU 1238 C VAL A 190 11028 12163 10240 2107 -186 1179 C ATOM 1239 O VAL A 190 95.025 -9.896 5.560 1.00 85.00 O ANISOU 1239 O VAL A 190 10648 11779 9869 2101 -144 1148 O ATOM 1240 CB VAL A 190 94.943 -10.860 8.674 1.00 83.74 C ANISOU 1240 CB VAL A 190 10494 11609 9715 2135 -137 1192 C ATOM 1241 CG1 VAL A 190 96.267 -10.599 9.381 1.00 93.74 C ANISOU 1241 CG1 VAL A 190 11744 12879 10992 2141 -166 1262 C ATOM 1242 CG2 VAL A 190 93.882 -11.272 9.684 1.00 88.50 C ANISOU 1242 CG2 VAL A 190 11113 12206 10307 2144 -126 1159 C ATOM 1243 N ASP A 191 96.509 -8.767 6.823 1.00102.68 N ANISOU 1243 N ASP A 191 12877 14033 12104 2106 -229 1232 N ATOM 1244 CA ASP A 191 97.467 -8.567 5.738 1.00 94.52 C ANISOU 1244 CA ASP A 191 11826 13002 11084 2097 -227 1259 C ATOM 1245 C ASP A 191 98.313 -9.820 5.521 1.00 92.22 C ANISOU 1245 C ASP A 191 11513 12698 10829 2107 -160 1297 C ATOM 1246 O ASP A 191 99.446 -9.909 5.997 1.00 89.25 O ANISOU 1246 O ASP A 191 11121 12321 10468 2114 -166 1355 O ATOM 1247 CB ASP A 191 98.373 -7.365 6.032 1.00 92.81 C ANISOU 1247 CB ASP A 191 11605 12799 10857 2092 -299 1302 C ATOM 1248 CG ASP A 191 98.959 -6.751 4.773 1.00107.29 C ANISOU 1248 CG ASP A 191 13430 14641 12693 2078 -316 1310 C ATOM 1249 OD1 ASP A 191 98.937 -7.414 3.715 1.00 99.34 O ANISOU 1249 OD1 ASP A 191 12416 13627 11702 2075 -265 1294 O ATOM 1250 OD2 ASP A 191 99.445 -5.602 4.840 1.00106.36 O ANISOU 1250 OD2 ASP A 191 13314 14537 12562 2070 -380 1331 O ATOM 1251 N HIS A 194 101.512 -14.289 2.733 1.00 98.97 N ANISOU 1251 N HIS A 194 12279 13505 11818 2127 109 1409 N ATOM 1252 CA HIS A 194 102.785 -13.587 2.619 1.00 95.77 C ANISOU 1252 CA HIS A 194 11860 13110 11419 2123 69 1464 C ATOM 1253 C HIS A 194 103.958 -14.568 2.638 1.00 96.93 C ANISOU 1253 C HIS A 194 11982 13247 11599 2134 117 1520 C ATOM 1254 O HIS A 194 104.350 -15.105 1.602 1.00 92.67 O ANISOU 1254 O HIS A 194 11430 12702 11079 2131 160 1524 O ATOM 1255 CB HIS A 194 102.927 -12.547 3.742 1.00102.73 C ANISOU 1255 CB HIS A 194 12750 14003 12279 2124 -4 1485 C ATOM 1256 CG HIS A 194 102.467 -13.024 5.088 1.00110.00 C ANISOU 1256 CG HIS A 194 13680 14919 13198 2138 4 1485 C ATOM 1257 ND1 HIS A 194 103.340 -13.466 6.059 1.00109.72 N ANISOU 1257 ND1 HIS A 194 13631 14879 13179 2152 11 1540 N ATOM 1258 CD2 HIS A 194 101.229 -13.110 5.630 1.00113.89 C ANISOU 1258 CD2 HIS A 194 14192 15408 13673 2141 5 1437 C ATOM 1259 CE1 HIS A 194 102.660 -13.813 7.137 1.00102.79 C ANISOU 1259 CE1 HIS A 194 12765 13997 12295 2162 16 1525 C ATOM 1260 NE2 HIS A 194 101.377 -13.608 6.903 1.00111.96 N ANISOU 1260 NE2 HIS A 194 13946 15158 13435 2156 13 1463 N ATOM 1261 N ASP A 195 104.516 -14.777 3.825 1.00110.66 N ANISOU 1261 N ASP A 195 13716 14985 13346 2146 109 1563 N ATOM 1262 CA ASP A 195 105.535 -15.789 4.069 1.00104.73 C ANISOU 1262 CA ASP A 195 12943 14223 12626 2159 157 1615 C ATOM 1263 C ASP A 195 104.916 -16.899 4.915 1.00 91.19 C ANISOU 1263 C ASP A 195 11233 12495 10919 2173 206 1601 C ATOM 1264 O ASP A 195 104.617 -16.685 6.090 1.00 88.26 O ANISOU 1264 O ASP A 195 10872 12126 10536 2181 179 1604 O ATOM 1265 CB ASP A 195 106.745 -15.163 4.773 1.00 87.94 C ANISOU 1265 CB ASP A 195 10805 12105 10502 2162 108 1679 C ATOM 1266 CG ASP A 195 107.913 -16.122 4.912 1.00 83.90 C ANISOU 1266 CG ASP A 195 10271 11585 10024 2174 154 1736 C ATOM 1267 OD1 ASP A 195 107.863 -17.221 4.323 1.00 98.20 O ANISOU 1267 OD1 ASP A 195 12073 13383 11856 2177 222 1727 O ATOM 1268 OD2 ASP A 195 108.894 -15.765 5.599 1.00 71.17 O ANISOU 1268 OD2 ASP A 195 8648 9977 8416 2178 121 1790 O ATOM 1269 N LYS A 196 104.717 -18.073 4.319 1.00 82.98 N ANISOU 1269 N LYS A 196 10707 10530 10291 -627 -299 -469 N ATOM 1270 CA LYS A 196 104.070 -19.187 5.012 1.00 89.39 C ANISOU 1270 CA LYS A 196 11518 11308 11138 -602 -332 -469 C ATOM 1271 C LYS A 196 104.813 -19.511 6.307 1.00 83.54 C ANISOU 1271 C LYS A 196 10763 10577 10399 -571 -329 -489 C ATOM 1272 O LYS A 196 104.223 -19.616 7.398 1.00 73.76 O ANISOU 1272 O LYS A 196 9524 9327 9173 -553 -332 -477 O ATOM 1273 CB LYS A 196 104.033 -20.432 4.113 1.00 85.34 C ANISOU 1273 CB LYS A 196 11003 10770 10652 -603 -368 -488 C ATOM 1274 CG LYS A 196 103.595 -20.186 2.668 1.00 98.87 C ANISOU 1274 CG LYS A 196 12729 12479 12360 -635 -372 -474 C ATOM 1275 CD LYS A 196 103.786 -21.439 1.807 1.00 82.90 C ANISOU 1275 CD LYS A 196 10699 10436 10362 -636 -403 -498 C ATOM 1276 CE LYS A 196 103.198 -21.269 0.408 1.00 87.68 C ANISOU 1276 CE LYS A 196 11319 11032 10964 -668 -409 -481 C ATOM 1277 NZ LYS A 196 103.389 -22.488 -0.431 1.00 89.97 N ANISOU 1277 NZ LYS A 196 11600 11305 11279 -670 -437 -506 N ATOM 1278 N ARG A 197 106.130 -19.599 6.163 1.00 84.94 N ANISOU 1278 N ARG A 197 10932 10779 10562 -567 -320 -518 N ATOM 1279 CA ARG A 197 107.037 -20.005 7.223 1.00 82.62 C ANISOU 1279 CA ARG A 197 10628 10497 10266 -540 -318 -539 C ATOM 1280 C ARG A 197 106.995 -19.044 8.410 1.00 76.35 C ANISOU 1280 C ARG A 197 9828 9727 9455 -533 -283 -524 C ATOM 1281 O ARG A 197 107.143 -19.453 9.562 1.00 62.05 O ANISOU 1281 O ARG A 197 8013 7912 7651 -507 -289 -529 O ATOM 1282 CB ARG A 197 108.451 -20.091 6.645 1.00 79.32 C ANISOU 1282 CB ARG A 197 10199 10108 9829 -546 -305 -569 C ATOM 1283 CG ARG A 197 109.455 -20.898 7.432 1.00 87.22 C ANISOU 1283 CG ARG A 197 11194 11116 10831 -520 -314 -595 C ATOM 1284 CD ARG A 197 110.681 -21.154 6.565 1.00 93.84 C ANISOU 1284 CD ARG A 197 12022 11978 11655 -530 -307 -625 C ATOM 1285 NE ARG A 197 111.086 -19.954 5.834 1.00 97.95 N ANISOU 1285 NE ARG A 197 12527 12538 12150 -559 -263 -625 N ATOM 1286 CZ ARG A 197 111.927 -19.953 4.804 1.00 95.18 C ANISOU 1286 CZ ARG A 197 12167 12209 11789 -577 -253 -647 C ATOM 1287 NH1 ARG A 197 112.238 -18.814 4.199 1.00 94.27 N ANISOU 1287 NH1 ARG A 197 12038 12129 11650 -603 -213 -645 N ATOM 1288 NH2 ARG A 197 112.453 -21.092 4.375 1.00 95.76 N ANISOU 1288 NH2 ARG A 197 12244 12268 11872 -569 -283 -670 N ATOM 1289 N ARG A 198 106.771 -17.767 8.115 1.00 78.33 N ANISOU 1289 N ARG A 198 10078 10001 9684 -557 -247 -505 N ATOM 1290 CA ARG A 198 106.695 -16.729 9.138 1.00 64.15 C ANISOU 1290 CA ARG A 198 8273 8230 7872 -554 -211 -491 C ATOM 1291 C ARG A 198 105.318 -16.700 9.794 1.00 53.17 C ANISOU 1291 C ARG A 198 6897 6809 6497 -548 -225 -460 C ATOM 1292 O ARG A 198 105.188 -16.557 11.020 1.00 70.87 O ANISOU 1292 O ARG A 198 9132 9054 8740 -530 -215 -454 O ATOM 1293 CB ARG A 198 107.020 -15.366 8.518 1.00 77.02 C ANISOU 1293 CB ARG A 198 9894 9896 9473 -584 -166 -484 C ATOM 1294 CG ARG A 198 107.324 -14.264 9.516 1.00 78.56 C ANISOU 1294 CG ARG A 198 10069 10127 9652 -582 -122 -478 C ATOM 1295 CD ARG A 198 108.436 -13.356 9.004 1.00 78.40 C ANISOU 1295 CD ARG A 198 10024 10155 9609 -602 -79 -495 C ATOM 1296 NE ARG A 198 109.662 -14.097 8.715 1.00 71.59 N ANISOU 1296 NE ARG A 198 9145 9309 8749 -593 -84 -532 N ATOM 1297 CZ ARG A 198 110.539 -14.487 9.637 1.00 94.01 C ANISOU 1297 CZ ARG A 198 11960 12166 11592 -569 -78 -555 C ATOM 1298 NH1 ARG A 198 110.327 -14.215 10.918 1.00 81.33 N ANISOU 1298 NH1 ARG A 198 10345 10566 9990 -551 -67 -546 N ATOM 1299 NH2 ARG A 198 111.626 -15.156 9.277 1.00 86.10 N ANISOU 1299 NH2 ARG A 198 10945 11179 10591 -562 -84 -588 N ATOM 1300 N GLU A 199 104.294 -16.860 8.963 1.00 61.06 N ANISOU 1300 N GLU A 199 7913 7780 7509 -563 -247 -440 N ATOM 1301 CA GLU A 199 102.914 -16.808 9.417 1.00 53.80 C ANISOU 1301 CA GLU A 199 7004 6833 6603 -561 -258 -409 C ATOM 1302 C GLU A 199 102.637 -17.917 10.418 1.00 51.05 C ANISOU 1302 C GLU A 199 6652 6460 6284 -532 -285 -417 C ATOM 1303 O GLU A 199 101.898 -17.719 11.395 1.00 47.67 O ANISOU 1303 O GLU A 199 6226 6025 5861 -523 -281 -397 O ATOM 1304 CB GLU A 199 101.970 -16.921 8.218 1.00 75.70 C ANISOU 1304 CB GLU A 199 9796 9583 9386 -584 -279 -389 C ATOM 1305 CG GLU A 199 100.504 -16.711 8.526 1.00 71.87 C ANISOU 1305 CG GLU A 199 9324 9072 8910 -589 -288 -351 C ATOM 1306 CD GLU A 199 99.649 -16.769 7.276 1.00108.93 C ANISOU 1306 CD GLU A 199 14035 13745 13608 -613 -307 -329 C ATOM 1307 OE1 GLU A 199 100.216 -16.914 6.171 1.00132.74 O ANISOU 1307 OE1 GLU A 199 17051 16766 16617 -627 -311 -345 O ATOM 1308 OE2 GLU A 199 98.411 -16.670 7.395 1.00112.48 O ANISOU 1308 OE2 GLU A 199 14499 14172 14066 -618 -320 -295 O ATOM 1309 N ARG A 200 103.273 -19.067 10.201 1.00 43.90 N ANISOU 1309 N ARG A 200 5739 5545 5396 -517 -312 -446 N ATOM 1310 CA ARG A 200 103.095 -20.184 11.121 1.00 52.84 C ANISOU 1310 CA ARG A 200 6864 6655 6556 -489 -337 -458 C ATOM 1311 C ARG A 200 103.641 -19.855 12.508 1.00 60.61 C ANISOU 1311 C ARG A 200 7844 7659 7527 -467 -320 -462 C ATOM 1312 O ARG A 200 102.979 -20.095 13.528 1.00 48.32 O ANISOU 1312 O ARG A 200 6286 6089 5984 -452 -325 -452 O ATOM 1313 CB ARG A 200 103.771 -21.441 10.572 1.00 43.07 C ANISOU 1313 CB ARG A 200 5620 5405 5338 -478 -368 -492 C ATOM 1314 CG ARG A 200 103.192 -21.912 9.249 1.00 58.10 C ANISOU 1314 CG ARG A 200 7526 7290 7259 -500 -384 -490 C ATOM 1315 CD ARG A 200 103.048 -23.422 9.214 1.00 70.23 C ANISOU 1315 CD ARG A 200 9049 8805 8831 -489 -412 -513 C ATOM 1316 NE ARG A 200 102.112 -23.852 8.181 1.00 76.02 N ANISOU 1316 NE ARG A 200 9788 9517 9578 -517 -420 -496 N ATOM 1317 CZ ARG A 200 102.458 -24.531 7.095 1.00 75.36 C ANISOU 1317 CZ ARG A 200 9699 9428 9505 -527 -435 -517 C ATOM 1318 NH1 ARG A 200 101.535 -24.875 6.208 1.00 75.21 N ANISOU 1318 NH1 ARG A 200 9692 9389 9496 -554 -444 -493 N ATOM 1319 NH2 ARG A 200 103.725 -24.871 6.898 1.00 83.38 N ANISOU 1319 NH2 ARG A 200 10704 10455 10520 -509 -447 -556 N ATOM 1320 N ALA A 201 104.840 -19.279 12.540 1.00 57.39 N ANISOU 1320 N ALA A 201 7431 7285 7091 -468 -295 -477 N ATOM 1321 CA ALA A 201 105.469 -18.918 13.801 1.00 47.92 C ANISOU 1321 CA ALA A 201 6222 6110 5874 -451 -271 -482 C ATOM 1322 C ALA A 201 104.676 -17.835 14.524 1.00 47.61 C ANISOU 1322 C ALA A 201 6183 6082 5827 -458 -241 -453 C ATOM 1323 O ALA A 201 104.540 -17.873 15.753 1.00 41.24 O ANISOU 1323 O ALA A 201 5372 5275 5022 -439 -237 -449 O ATOM 1324 CB ALA A 201 106.903 -18.459 13.565 1.00 48.35 C ANISOU 1324 CB ALA A 201 6261 6208 5903 -456 -240 -505 C ATOM 1325 N VAL A 202 104.121 -16.892 13.766 1.00 32.85 N ANISOU 1325 N VAL A 202 4317 4217 3946 -485 -223 -432 N ATOM 1326 CA VAL A 202 103.326 -15.840 14.393 1.00 38.80 C ANISOU 1326 CA VAL A 202 5073 4980 4691 -493 -196 -403 C ATOM 1327 C VAL A 202 102.055 -16.423 15.014 1.00 45.26 C ANISOU 1327 C VAL A 202 5903 5761 5533 -482 -223 -383 C ATOM 1328 O VAL A 202 101.671 -16.054 16.135 1.00 45.87 O ANISOU 1328 O VAL A 202 5978 5842 5609 -472 -209 -370 O ATOM 1329 CB VAL A 202 102.957 -14.729 13.387 1.00 21.74 C ANISOU 1329 CB VAL A 202 2918 2830 2511 -525 -174 -384 C ATOM 1330 CG1 VAL A 202 102.083 -13.679 14.047 1.00 35.71 C ANISOU 1330 CG1 VAL A 202 4693 4606 4272 -532 -150 -353 C ATOM 1331 CG2 VAL A 202 104.214 -14.088 12.829 1.00 37.33 C ANISOU 1331 CG2 VAL A 202 4876 4846 4463 -539 -141 -405 C ATOM 1332 N ALA A 203 101.429 -17.365 14.310 1.00 45.09 N ANISOU 1332 N ALA A 203 5890 5705 5536 -484 -259 -381 N ATOM 1333 CA ALA A 203 100.235 -18.006 14.850 1.00 38.10 C ANISOU 1333 CA ALA A 203 5011 4788 4677 -477 -280 -363 C ATOM 1334 C ALA A 203 100.548 -18.817 16.107 1.00 38.51 C ANISOU 1334 C ALA A 203 5052 4836 4743 -447 -290 -381 C ATOM 1335 O ALA A 203 99.748 -18.847 17.055 1.00 33.20 O ANISOU 1335 O ALA A 203 4382 4153 4080 -441 -288 -363 O ATOM 1336 CB ALA A 203 99.595 -18.893 13.803 1.00 37.84 C ANISOU 1336 CB ALA A 203 4985 4725 4667 -490 -310 -359 C ATOM 1337 N ILE A 204 101.717 -19.455 16.124 1.00 34.33 N ANISOU 1337 N ILE A 204 4514 4315 4213 -429 -300 -415 N ATOM 1338 CA ILE A 204 102.132 -20.215 17.299 1.00 31.81 C ANISOU 1338 CA ILE A 204 4188 3993 3903 -398 -313 -433 C ATOM 1339 C ILE A 204 102.381 -19.287 18.488 1.00 40.74 C ANISOU 1339 C ILE A 204 5319 5150 5010 -390 -282 -422 C ATOM 1340 O ILE A 204 102.032 -19.609 19.630 1.00 33.74 O ANISOU 1340 O ILE A 204 4431 4256 4133 -372 -286 -418 O ATOM 1341 CB ILE A 204 103.398 -21.047 17.012 1.00 35.41 C ANISOU 1341 CB ILE A 204 4643 4452 4359 -381 -335 -468 C ATOM 1342 CG1 ILE A 204 103.063 -22.207 16.073 1.00 32.53 C ANISOU 1342 CG1 ILE A 204 4271 4063 4027 -384 -365 -485 C ATOM 1343 CG2 ILE A 204 104.005 -21.577 18.301 1.00 35.47 C ANISOU 1343 CG2 ILE A 204 4653 4461 4362 -350 -344 -480 C ATOM 1344 CD1 ILE A 204 104.229 -23.134 15.806 1.00 37.45 C ANISOU 1344 CD1 ILE A 204 4895 4682 4651 -364 -391 -514 C ATOM 1345 N VAL A 205 102.949 -18.116 18.207 1.00 45.94 N ANISOU 1345 N VAL A 205 5973 5842 5640 -407 -246 -418 N ATOM 1346 CA VAL A 205 103.175 -17.123 19.250 1.00 37.62 C ANISOU 1346 CA VAL A 205 4908 4819 4565 -405 -206 -409 C ATOM 1347 C VAL A 205 101.844 -16.625 19.811 1.00 43.47 C ANISOU 1347 C VAL A 205 5657 5546 5312 -411 -200 -377 C ATOM 1348 O VAL A 205 101.713 -16.412 21.023 1.00 41.37 O ANISOU 1348 O VAL A 205 5386 5289 5043 -399 -186 -371 O ATOM 1349 CB VAL A 205 104.012 -15.930 18.722 1.00 29.00 C ANISOU 1349 CB VAL A 205 3800 3772 3447 -425 -163 -414 C ATOM 1350 CG1 VAL A 205 103.943 -14.739 19.670 1.00 22.63 C ANISOU 1350 CG1 VAL A 205 2976 2996 2625 -429 -119 -401 C ATOM 1351 CG2 VAL A 205 105.454 -16.353 18.499 1.00 45.37 C ANISOU 1351 CG2 VAL A 205 5859 5868 5511 -416 -161 -448 C ATOM 1352 N ARG A 206 100.841 -16.486 18.946 1.00 30.23 N ANISOU 1352 N ARG A 206 3993 3848 3645 -431 -210 -356 N ATOM 1353 CA ARG A 206 99.524 -16.083 19.430 1.00 38.67 C ANISOU 1353 CA ARG A 206 5071 4902 4721 -438 -207 -323 C ATOM 1354 C ARG A 206 98.916 -17.166 20.316 1.00 45.34 C ANISOU 1354 C ARG A 206 5917 5718 5591 -419 -233 -322 C ATOM 1355 O ARG A 206 98.344 -16.869 21.372 1.00 35.71 O ANISOU 1355 O ARG A 206 4698 4498 4371 -413 -222 -306 O ATOM 1356 CB ARG A 206 98.578 -15.773 18.270 1.00 34.82 C ANISOU 1356 CB ARG A 206 4599 4396 4236 -464 -216 -299 C ATOM 1357 CG ARG A 206 99.019 -14.622 17.385 1.00 50.10 C ANISOU 1357 CG ARG A 206 6533 6357 6143 -486 -189 -296 C ATOM 1358 CD ARG A 206 97.869 -14.152 16.512 1.00 62.58 C ANISOU 1358 CD ARG A 206 8134 7920 7725 -508 -198 -264 C ATOM 1359 NE ARG A 206 98.329 -13.473 15.305 1.00 73.67 N ANISOU 1359 NE ARG A 206 9541 9342 9109 -530 -185 -267 N ATOM 1360 CZ ARG A 206 98.510 -14.076 14.136 1.00 52.98 C ANISOU 1360 CZ ARG A 206 6926 6708 6496 -539 -208 -276 C ATOM 1361 NH1 ARG A 206 98.269 -15.375 14.014 1.00 53.16 N ANISOU 1361 NH1 ARG A 206 6949 6701 6547 -529 -243 -284 N ATOM 1362 NH2 ARG A 206 98.929 -13.383 13.087 1.00 65.63 N ANISOU 1362 NH2 ARG A 206 8531 8327 8078 -560 -193 -278 N ATOM 1363 N LEU A 207 99.055 -18.421 19.894 1.00 40.42 N ANISOU 1363 N LEU A 207 5292 5074 4991 -411 -264 -341 N ATOM 1364 CA LEU A 207 98.497 -19.533 20.658 1.00 31.72 C ANISOU 1364 CA LEU A 207 4188 3949 3915 -398 -284 -341 C ATOM 1365 C LEU A 207 99.160 -19.685 22.025 1.00 44.48 C ANISOU 1365 C LEU A 207 5796 5581 5525 -369 -278 -360 C ATOM 1366 O LEU A 207 98.506 -20.041 23.007 1.00 33.06 O ANISOU 1366 O LEU A 207 4350 4123 4090 -363 -279 -349 O ATOM 1367 CB LEU A 207 98.621 -20.840 19.873 1.00 33.08 C ANISOU 1367 CB LEU A 207 4358 4102 4110 -400 -310 -360 C ATOM 1368 CG LEU A 207 98.161 -22.108 20.597 1.00 25.77 C ANISOU 1368 CG LEU A 207 3431 3154 3205 -394 -324 -359 C ATOM 1369 CD1 LEU A 207 96.704 -21.989 21.019 1.00 29.93 C ANISOU 1369 CD1 LEU A 207 3976 3655 3743 -408 -327 -310 C ATOM 1370 CD2 LEU A 207 98.372 -23.333 19.723 1.00 33.24 C ANISOU 1370 CD2 LEU A 207 4377 4086 4168 -402 -344 -374 C ATOM 1371 N VAL A 208 100.457 -19.404 22.093 1.00 38.76 N ANISOU 1371 N VAL A 208 5066 4880 4779 -355 -271 -383 N ATOM 1372 CA VAL A 208 101.167 -19.533 23.360 1.00 37.29 C ANISOU 1372 CA VAL A 208 4878 4709 4580 -328 -267 -397 C ATOM 1373 C VAL A 208 100.882 -18.358 24.292 1.00 34.31 C ANISOU 1373 C VAL A 208 4499 4355 4183 -334 -229 -374 C ATOM 1374 O VAL A 208 100.534 -18.552 25.458 1.00 27.83 O ANISOU 1374 O VAL A 208 3678 3530 3365 -319 -229 -369 O ATOM 1375 CB VAL A 208 102.691 -19.650 23.144 1.00 35.19 C ANISOU 1375 CB VAL A 208 4614 4465 4293 -317 -267 -422 C ATOM 1376 CG1 VAL A 208 103.436 -19.469 24.458 1.00 20.48 C ANISOU 1376 CG1 VAL A 208 2749 2626 2407 -299 -248 -427 C ATOM 1377 CG2 VAL A 208 103.034 -20.990 22.506 1.00 21.20 C ANISOU 1377 CG2 VAL A 208 2848 2666 2541 -304 -311 -446 C ATOM 1378 N LEU A 209 101.018 -17.142 23.772 1.00 39.93 N ANISOU 1378 N LEU A 209 5204 5091 4875 -357 -195 -363 N ATOM 1379 CA LEU A 209 100.819 -15.948 24.588 1.00 25.82 C ANISOU 1379 CA LEU A 209 3407 3332 3071 -364 -154 -346 C ATOM 1380 C LEU A 209 99.374 -15.773 25.040 1.00 33.86 C ANISOU 1380 C LEU A 209 4438 4328 4102 -371 -157 -316 C ATOM 1381 O LEU A 209 99.117 -15.212 26.107 1.00 44.89 O ANISOU 1381 O LEU A 209 5828 5738 5491 -368 -134 -304 O ATOM 1382 CB LEU A 209 101.275 -14.704 23.826 1.00 26.30 C ANISOU 1382 CB LEU A 209 3455 3427 3113 -388 -116 -344 C ATOM 1383 CG LEU A 209 102.775 -14.606 23.533 1.00 33.43 C ANISOU 1383 CG LEU A 209 4335 4364 4002 -385 -100 -374 C ATOM 1384 CD1 LEU A 209 103.121 -13.248 22.941 1.00 29.82 C ANISOU 1384 CD1 LEU A 209 3857 3943 3529 -410 -57 -370 C ATOM 1385 CD2 LEU A 209 103.596 -14.878 24.786 1.00 26.38 C ANISOU 1385 CD2 LEU A 209 3425 3493 3105 -360 -92 -392 C ATOM 1386 N GLY A 210 98.433 -16.246 24.230 1.00 34.97 N ANISOU 1386 N GLY A 210 4592 4435 4262 -383 -184 -301 N ATOM 1387 CA GLY A 210 97.030 -16.044 24.535 1.00 24.86 C ANISOU 1387 CA GLY A 210 3322 3132 2992 -393 -187 -268 C ATOM 1388 C GLY A 210 96.310 -17.197 25.210 1.00 21.96 C ANISOU 1388 C GLY A 210 2958 2733 2652 -382 -214 -264 C ATOM 1389 O GLY A 210 95.203 -17.018 25.720 1.00 24.08 O ANISOU 1389 O GLY A 210 3235 2987 2929 -388 -214 -235 O ATOM 1390 N PHE A 211 96.924 -18.376 25.238 1.00 26.08 N ANISOU 1390 N PHE A 211 3475 3247 3188 -366 -236 -291 N ATOM 1391 CA PHE A 211 96.197 -19.558 25.693 1.00 25.67 C ANISOU 1391 CA PHE A 211 3426 3164 3162 -363 -258 -283 C ATOM 1392 C PHE A 211 97.053 -20.570 26.450 1.00 24.86 C ANISOU 1392 C PHE A 211 3314 3069 3064 -337 -266 -318 C ATOM 1393 O PHE A 211 96.844 -20.786 27.643 1.00 25.23 O ANISOU 1393 O PHE A 211 3359 3114 3111 -325 -262 -315 O ATOM 1394 CB PHE A 211 95.527 -20.246 24.498 1.00 23.42 C ANISOU 1394 CB PHE A 211 3152 2848 2898 -384 -282 -267 C ATOM 1395 CG PHE A 211 94.438 -21.210 24.882 1.00 23.36 C ANISOU 1395 CG PHE A 211 3156 2803 2917 -390 -303 -237 C ATOM 1396 CD1 PHE A 211 93.154 -20.757 25.141 1.00 22.19 C ANISOU 1396 CD1 PHE A 211 3017 2635 2777 -400 -307 -195 C ATOM 1397 CD2 PHE A 211 94.694 -22.568 24.976 1.00 22.73 C ANISOU 1397 CD2 PHE A 211 3078 2706 2853 -384 -322 -247 C ATOM 1398 CE1 PHE A 211 92.147 -21.641 25.492 1.00 19.65 C ANISOU 1398 CE1 PHE A 211 2705 2277 2485 -403 -331 -162 C ATOM 1399 CE2 PHE A 211 93.691 -23.456 25.327 1.00 30.40 C ANISOU 1399 CE2 PHE A 211 4062 3639 3851 -388 -346 -212 C ATOM 1400 CZ PHE A 211 92.417 -22.991 25.585 1.00 24.44 C ANISOU 1400 CZ PHE A 211 3314 2864 3109 -397 -352 -169 C ATOM 1401 N LEU A 212 98.004 -21.193 25.761 1.00 20.36 N ANISOU 1401 N LEU A 212 2736 2505 2495 -329 -280 -351 N ATOM 1402 CA LEU A 212 98.726 -22.327 26.330 1.00 21.17 C ANISOU 1402 CA LEU A 212 2827 2613 2602 -306 -291 -385 C ATOM 1403 C LEU A 212 99.535 -21.966 27.574 1.00 30.08 C ANISOU 1403 C LEU A 212 3953 3765 3711 -270 -287 -403 C ATOM 1404 O LEU A 212 99.446 -22.653 28.598 1.00 37.46 O ANISOU 1404 O LEU A 212 4884 4703 4648 -257 -284 -408 O ATOM 1405 CB LEU A 212 99.650 -22.949 25.280 1.00 29.33 C ANISOU 1405 CB LEU A 212 3852 3653 3639 -303 -306 -420 C ATOM 1406 CG LEU A 212 98.950 -23.638 24.105 1.00 40.79 C ANISOU 1406 CG LEU A 212 5313 5077 5108 -337 -315 -401 C ATOM 1407 CD1 LEU A 212 99.967 -24.297 23.191 1.00 21.28 C ANISOU 1407 CD1 LEU A 212 2829 2618 2637 -334 -326 -441 C ATOM 1408 CD2 LEU A 212 97.932 -24.653 24.610 1.00 30.47 C ANISOU 1408 CD2 LEU A 212 4026 3733 3817 -350 -327 -366 C ATOM 1409 N TRP A 213 100.330 -20.904 27.489 1.00 24.25 N ANISOU 1409 N TRP A 213 3226 3045 2944 -263 -279 -399 N ATOM 1410 CA TRP A 213 101.098 -20.450 28.648 1.00 27.20 C ANISOU 1410 CA TRP A 213 3610 3439 3284 -243 -265 -398 C ATOM 1411 C TRP A 213 100.188 -20.059 29.828 1.00 27.72 C ANISOU 1411 C TRP A 213 3672 3507 3352 -243 -247 -378 C ATOM 1412 O TRP A 213 100.411 -20.531 30.956 1.00 31.72 O ANISOU 1412 O TRP A 213 4186 4014 3850 -217 -254 -385 O ATOM 1413 CB TRP A 213 102.022 -19.286 28.262 1.00 27.58 C ANISOU 1413 CB TRP A 213 3651 3525 3302 -259 -228 -396 C ATOM 1414 CG TRP A 213 102.789 -18.698 29.410 1.00 29.15 C ANISOU 1414 CG TRP A 213 3838 3763 3474 -249 -193 -400 C ATOM 1415 CD1 TRP A 213 102.606 -17.470 29.972 1.00 21.24 C ANISOU 1415 CD1 TRP A 213 2812 2793 2464 -260 -150 -388 C ATOM 1416 CD2 TRP A 213 103.857 -19.318 30.139 1.00 32.54 C ANISOU 1416 CD2 TRP A 213 4272 4206 3885 -225 -197 -419 C ATOM 1417 NE1 TRP A 213 103.495 -17.282 31.002 1.00 22.48 N ANISOU 1417 NE1 TRP A 213 2951 2986 2605 -242 -129 -402 N ATOM 1418 CE2 TRP A 213 104.274 -18.402 31.126 1.00 24.71 C ANISOU 1418 CE2 TRP A 213 3251 3259 2880 -220 -156 -421 C ATOM 1419 CE3 TRP A 213 104.500 -20.556 30.052 1.00 28.69 C ANISOU 1419 CE3 TRP A 213 3810 3699 3391 -211 -229 -434 C ATOM 1420 CZ2 TRP A 213 105.305 -18.686 32.021 1.00 17.36 C ANISOU 1420 CZ2 TRP A 213 2309 2357 1932 -196 -148 -439 C ATOM 1421 CZ3 TRP A 213 105.522 -20.836 30.939 1.00 26.14 C ANISOU 1421 CZ3 TRP A 213 3480 3405 3045 -192 -215 -450 C ATOM 1422 CH2 TRP A 213 105.914 -19.906 31.912 1.00 23.84 C ANISOU 1422 CH2 TRP A 213 3153 3161 2745 -182 -176 -454 C ATOM 1423 N PRO A 214 99.152 -19.224 29.583 1.00 28.37 N ANISOU 1423 N PRO A 214 3750 3587 3442 -272 -224 -349 N ATOM 1424 CA PRO A 214 98.244 -18.955 30.701 1.00 24.01 C ANISOU 1424 CA PRO A 214 3199 3032 2892 -273 -210 -328 C ATOM 1425 C PRO A 214 97.590 -20.217 31.249 1.00 25.46 C ANISOU 1425 C PRO A 214 3384 3190 3102 -266 -232 -332 C ATOM 1426 O PRO A 214 97.371 -20.321 32.458 1.00 29.56 O ANISOU 1426 O PRO A 214 3904 3712 3615 -252 -226 -329 O ATOM 1427 CB PRO A 214 97.193 -18.032 30.081 1.00 21.47 C ANISOU 1427 CB PRO A 214 2879 2703 2575 -306 -193 -295 C ATOM 1428 CG PRO A 214 97.918 -17.330 28.994 1.00 22.53 C ANISOU 1428 CG PRO A 214 3009 2857 2695 -318 -180 -302 C ATOM 1429 CD PRO A 214 98.822 -18.379 28.413 1.00 23.43 C ANISOU 1429 CD PRO A 214 3123 2964 2815 -302 -210 -333 C ATOM 1430 N LEU A 215 97.312 -21.177 30.371 1.00 22.64 N ANISOU 1430 N LEU A 215 3025 2809 2767 -280 -251 -336 N ATOM 1431 CA LEU A 215 96.655 -22.409 30.785 1.00 27.95 C ANISOU 1431 CA LEU A 215 3706 3454 3460 -289 -262 -325 C ATOM 1432 C LEU A 215 97.542 -23.195 31.737 1.00 33.10 C ANISOU 1432 C LEU A 215 4350 4128 4099 -261 -263 -362 C ATOM 1433 O LEU A 215 97.101 -23.608 32.811 1.00 31.91 O ANISOU 1433 O LEU A 215 4208 3967 3947 -257 -260 -349 O ATOM 1434 CB LEU A 215 96.298 -23.264 29.567 1.00 25.41 C ANISOU 1434 CB LEU A 215 3394 3101 3160 -312 -283 -313 C ATOM 1435 CG LEU A 215 95.540 -24.562 29.849 1.00 25.19 C ANISOU 1435 CG LEU A 215 3386 3029 3157 -321 -306 -283 C ATOM 1436 CD1 LEU A 215 94.211 -24.265 30.524 1.00 22.96 C ANISOU 1436 CD1 LEU A 215 3114 2718 2893 -330 -308 -237 C ATOM 1437 CD2 LEU A 215 95.335 -25.354 28.564 1.00 23.32 C ANISOU 1437 CD2 LEU A 215 3159 2762 2940 -336 -333 -270 C ATOM 1438 N LEU A 216 98.803 -23.367 31.353 1.00 21.86 N ANISOU 1438 N LEU A 216 2911 2733 2662 -237 -266 -400 N ATOM 1439 CA LEU A 216 99.753 -24.111 32.168 1.00 29.91 C ANISOU 1439 CA LEU A 216 3920 3783 3661 -210 -256 -425 C ATOM 1440 C LEU A 216 99.992 -23.429 33.511 1.00 32.68 C ANISOU 1440 C LEU A 216 4276 4149 3994 -165 -255 -420 C ATOM 1441 O LEU A 216 99.851 -24.053 34.578 1.00 28.68 O ANISOU 1441 O LEU A 216 3765 3661 3472 -171 -233 -424 O ATOM 1442 CB LEU A 216 101.075 -24.265 31.412 1.00 23.81 C ANISOU 1442 CB LEU A 216 3131 3034 2883 -184 -262 -454 C ATOM 1443 CG LEU A 216 102.241 -24.931 32.140 1.00 26.30 C ANISOU 1443 CG LEU A 216 3508 3387 3097 -280 -193 -421 C ATOM 1444 CD1 LEU A 216 101.911 -26.376 32.464 1.00 22.27 C ANISOU 1444 CD1 LEU A 216 2994 2852 2614 -251 -230 -446 C ATOM 1445 CD2 LEU A 216 103.510 -24.839 31.306 1.00 28.06 C ANISOU 1445 CD2 LEU A 216 3844 3519 3299 -238 -284 -382 C ATOM 1446 N THR A 217 100.302 -22.136 33.460 1.00 22.75 N ANISOU 1446 N THR A 217 3056 2876 2713 -156 -266 -392 N ATOM 1447 CA THR A 217 100.641 -21.413 34.679 1.00 20.26 C ANISOU 1447 CA THR A 217 2769 2575 2356 -147 -248 -377 C ATOM 1448 C THR A 217 99.467 -21.347 35.657 1.00 33.32 C ANISOU 1448 C THR A 217 4405 4230 4024 -145 -236 -370 C ATOM 1449 O THR A 217 99.617 -21.664 36.846 1.00 30.81 O ANISOU 1449 O THR A 217 4101 3918 3686 -117 -233 -367 O ATOM 1450 CB THR A 217 101.109 -19.986 34.363 1.00 22.39 C ANISOU 1450 CB THR A 217 3025 2879 2604 -174 -211 -375 C ATOM 1451 OG1 THR A 217 100.079 -19.298 33.643 1.00 36.11 O ANISOU 1451 OG1 THR A 217 4744 4610 4368 -203 -199 -359 O ATOM 1452 CG2 THR A 217 102.371 -20.022 33.520 1.00 33.67 C ANISOU 1452 CG2 THR A 217 4450 4324 4018 -179 -207 -392 C ATOM 1453 N LEU A 218 98.297 -20.956 35.159 1.00 19.63 N ANISOU 1453 N LEU A 218 2656 2485 2319 -184 -228 -359 N ATOM 1454 CA LEU A 218 97.121 -20.862 36.018 1.00 20.67 C ANISOU 1454 CA LEU A 218 2787 2605 2461 -200 -213 -333 C ATOM 1455 C LEU A 218 96.708 -22.234 36.541 1.00 26.23 C ANISOU 1455 C LEU A 218 3494 3293 3180 -203 -222 -340 C ATOM 1456 O LEU A 218 96.229 -22.356 37.679 1.00 33.74 O ANISOU 1456 O LEU A 218 4454 4242 4125 -197 -214 -329 O ATOM 1457 CB LEU A 218 95.957 -20.200 35.279 1.00 12.87 C ANISOU 1457 CB LEU A 218 1800 1593 1496 -244 -202 -295 C ATOM 1458 CG LEU A 218 96.174 -18.723 34.939 1.00 20.51 C ANISOU 1458 CG LEU A 218 2764 2586 2443 -255 -174 -283 C ATOM 1459 CD1 LEU A 218 94.973 -18.128 34.219 1.00 21.96 C ANISOU 1459 CD1 LEU A 218 2950 2748 2645 -290 -168 -248 C ATOM 1460 CD2 LEU A 218 96.490 -17.933 36.194 1.00 20.54 C ANISOU 1460 CD2 LEU A 218 2764 2623 2418 -241 -144 -282 C ATOM 1461 N THR A 219 96.922 -23.268 35.729 1.00 21.76 N ANISOU 1461 N THR A 219 2927 2711 2629 -217 -236 -350 N ATOM 1462 CA THR A 219 96.594 -24.618 36.169 1.00 31.80 C ANISOU 1462 CA THR A 219 4220 3952 3910 -225 -248 -339 C ATOM 1463 C THR A 219 97.452 -25.005 37.363 1.00 29.34 C ANISOU 1463 C THR A 219 3908 3683 3556 -194 -235 -370 C ATOM 1464 O THR A 219 96.938 -25.511 38.365 1.00 29.27 O ANISOU 1464 O THR A 219 3921 3655 3546 -188 -237 -352 O ATOM 1465 CB THR A 219 96.788 -25.658 35.052 1.00 31.38 C ANISOU 1465 CB THR A 219 4177 3871 3876 -241 -271 -337 C ATOM 1466 OG1 THR A 219 95.929 -25.341 33.949 1.00 39.62 O ANISOU 1466 OG1 THR A 219 5222 4880 4952 -268 -283 -304 O ATOM 1467 CG2 THR A 219 96.460 -27.051 35.558 1.00 22.67 C ANISOU 1467 CG2 THR A 219 3101 2723 2790 -238 -295 -318 C ATOM 1468 N ILE A 220 98.752 -24.738 37.272 1.00 30.75 N ANISOU 1468 N ILE A 220 4063 3918 3703 -173 -215 -399 N ATOM 1469 CA ILE A 220 99.634 -25.046 38.392 1.00 25.08 C ANISOU 1469 CA ILE A 220 3355 3242 2932 -165 -185 -404 C ATOM 1470 C ILE A 220 99.257 -24.228 39.632 1.00 30.91 C ANISOU 1470 C ILE A 220 4081 4007 3655 -139 -164 -395 C ATOM 1471 O ILE A 220 99.201 -24.754 40.764 1.00 34.44 O ANISOU 1471 O ILE A 220 4562 4454 4068 -135 -154 -384 O ATOM 1472 CB ILE A 220 101.101 -24.784 38.015 1.00 26.12 C ANISOU 1472 CB ILE A 220 3539 3374 3011 -200 -167 -382 C ATOM 1473 CG1 ILE A 220 101.496 -25.676 36.837 1.00 23.78 C ANISOU 1473 CG1 ILE A 220 3232 3069 2735 -204 -191 -407 C ATOM 1474 CG2 ILE A 220 102.012 -25.024 39.199 1.00 18.97 C ANISOU 1474 CG2 ILE A 220 2678 2468 2062 -155 -174 -384 C ATOM 1475 CD1 ILE A 220 102.910 -25.469 36.357 1.00 23.47 C ANISOU 1475 CD1 ILE A 220 3241 3012 2663 -194 -210 -401 C ATOM 1476 N CYS A 221 98.917 -22.963 39.392 1.00 23.97 N ANISOU 1476 N CYS A 221 3198 3105 2806 -81 -199 -387 N ATOM 1477 CA CYS A 221 98.590 -22.027 40.464 1.00 33.36 C ANISOU 1477 CA CYS A 221 4431 4280 3965 -55 -196 -355 C ATOM 1478 C CYS A 221 97.399 -22.506 41.293 1.00 27.45 C ANISOU 1478 C CYS A 221 3662 3546 3222 -83 -172 -356 C ATOM 1479 O CYS A 221 97.483 -22.652 42.526 1.00 24.20 O ANISOU 1479 O CYS A 221 3249 3172 2774 -58 -146 -353 O ATOM 1480 CB CYS A 221 98.301 -20.643 39.866 1.00 32.45 C ANISOU 1480 CB CYS A 221 4320 4157 3851 -97 -183 -338 C ATOM 1481 SG CYS A 221 97.761 -19.362 41.026 1.00 34.41 S ANISOU 1481 SG CYS A 221 4567 4432 4076 -104 -140 -317 S ATOM 1482 N TYR A 222 96.299 -22.792 40.608 1.00 25.26 N ANISOU 1482 N TYR A 222 3396 3215 2987 -138 -188 -342 N ATOM 1483 CA TYR A 222 95.105 -23.226 41.315 1.00 27.50 C ANISOU 1483 CA TYR A 222 3704 3454 3290 -160 -188 -308 C ATOM 1484 C TYR A 222 95.183 -24.689 41.738 1.00 28.55 C ANISOU 1484 C TYR A 222 3906 3538 3403 -165 -217 -297 C ATOM 1485 O TYR A 222 94.401 -25.130 42.578 1.00 32.05 O ANISOU 1485 O TYR A 222 4450 3899 3829 -181 -248 -253 O ATOM 1486 CB TYR A 222 93.864 -22.958 40.466 1.00 27.06 C ANISOU 1486 CB TYR A 222 3649 3330 3302 -215 -199 -264 C ATOM 1487 CG TYR A 222 93.543 -21.483 40.424 1.00 30.17 C ANISOU 1487 CG TYR A 222 4030 3744 3687 -223 -178 -250 C ATOM 1488 CD1 TYR A 222 92.933 -20.861 41.505 1.00 25.71 C ANISOU 1488 CD1 TYR A 222 3483 3182 3106 -232 -158 -229 C ATOM 1489 CD2 TYR A 222 93.885 -20.705 39.326 1.00 24.26 C ANISOU 1489 CD2 TYR A 222 3269 3011 2938 -233 -176 -251 C ATOM 1490 CE1 TYR A 222 92.652 -19.511 41.487 1.00 25.45 C ANISOU 1490 CE1 TYR A 222 3429 3172 3069 -236 -133 -217 C ATOM 1491 CE2 TYR A 222 93.607 -19.352 39.299 1.00 27.56 C ANISOU 1491 CE2 TYR A 222 3680 3447 3344 -246 -152 -234 C ATOM 1492 CZ TYR A 222 92.990 -18.761 40.383 1.00 17.65 C ANISOU 1492 CZ TYR A 222 2428 2198 2080 -248 -129 -216 C ATOM 1493 OH TYR A 222 92.710 -17.416 40.365 1.00 19.95 O ANISOU 1493 OH TYR A 222 2709 2511 2360 -265 -98 -199 O ATOM 1494 N THR A 223 96.132 -25.438 41.182 1.00 25.08 N ANISOU 1494 N THR A 223 3427 3134 2966 -149 -213 -332 N ATOM 1495 CA THR A 223 96.392 -26.774 41.705 1.00 32.15 C ANISOU 1495 CA THR A 223 4398 3981 3836 -127 -253 -321 C ATOM 1496 C THR A 223 96.917 -26.644 43.129 1.00 35.45 C ANISOU 1496 C THR A 223 4849 4448 4171 -70 -227 -328 C ATOM 1497 O THR A 223 96.369 -27.249 44.069 1.00 27.14 O ANISOU 1497 O THR A 223 3900 3330 3080 -28 -260 -297 O ATOM 1498 CB THR A 223 97.405 -27.553 40.848 1.00 28.36 C ANISOU 1498 CB THR A 223 3870 3538 3368 -130 -242 -353 C ATOM 1499 OG1 THR A 223 96.875 -27.738 39.530 1.00 35.84 O ANISOU 1499 OG1 THR A 223 4807 4434 4376 -165 -267 -338 O ATOM 1500 CG2 THR A 223 97.687 -28.914 41.464 1.00 37.02 C ANISOU 1500 CG2 THR A 223 5042 4580 4442 -86 -293 -345 C ATOM 1501 N PHE A 224 97.939 -25.805 43.297 1.00 32.43 N ANISOU 1501 N PHE A 224 4377 4181 3763 -79 -158 -358 N ATOM 1502 CA PHE A 224 98.476 -25.569 44.634 1.00 31.95 C ANISOU 1502 CA PHE A 224 4334 4166 3641 -47 -117 -346 C ATOM 1503 C PHE A 224 97.410 -24.999 45.569 1.00 35.00 C ANISOU 1503 C PHE A 224 4767 4536 3995 -4 -113 -315 C ATOM 1504 O PHE A 224 97.222 -25.490 46.699 1.00 27.57 O ANISOU 1504 O PHE A 224 3890 3585 2999 71 -102 -283 O ATOM 1505 CB PHE A 224 99.673 -24.618 44.577 1.00 32.61 C ANISOU 1505 CB PHE A 224 4413 4267 3711 -65 -88 -343 C ATOM 1506 CG PHE A 224 100.962 -25.283 44.191 1.00 38.46 C ANISOU 1506 CG PHE A 224 5168 5004 4439 -45 -108 -365 C ATOM 1507 CD1 PHE A 224 101.765 -25.874 45.153 1.00 50.40 C ANISOU 1507 CD1 PHE A 224 6685 6537 5927 16 -104 -368 C ATOM 1508 CD2 PHE A 224 101.379 -25.309 42.871 1.00 41.59 C ANISOU 1508 CD2 PHE A 224 5559 5383 4861 -75 -131 -378 C ATOM 1509 CE1 PHE A 224 102.956 -26.482 44.804 1.00 56.10 C ANISOU 1509 CE1 PHE A 224 7402 7264 6649 42 -124 -389 C ATOM 1510 CE2 PHE A 224 102.568 -25.917 42.517 1.00 50.23 C ANISOU 1510 CE2 PHE A 224 6653 6481 5951 -49 -149 -399 C ATOM 1511 CZ PHE A 224 103.356 -26.505 43.484 1.00 60.66 C ANISOU 1511 CZ PHE A 224 7974 7825 7250 10 -147 -406 C ATOM 1512 N ILE A 225 96.684 -23.991 45.084 1.00 33.92 N ANISOU 1512 N ILE A 225 4600 4398 3889 -40 -111 -315 N ATOM 1513 CA ILE A 225 95.705 -23.319 45.938 1.00 29.37 C ANISOU 1513 CA ILE A 225 4082 3801 3276 -27 -85 -271 C ATOM 1514 C ILE A 225 94.582 -24.248 46.390 1.00 31.60 C ANISOU 1514 C ILE A 225 4410 3985 3612 -16 -85 -170 C ATOM 1515 O ILE A 225 94.307 -24.366 47.587 1.00 28.76 O ANISOU 1515 O ILE A 225 4038 3641 3247 40 -30 -104 O ATOM 1516 CB ILE A 225 95.069 -22.110 45.234 1.00 24.45 C ANISOU 1516 CB ILE A 225 3415 3170 2703 -78 -87 -272 C ATOM 1517 CG1 ILE A 225 96.101 -21.007 45.021 1.00 26.68 C ANISOU 1517 CG1 ILE A 225 3601 3514 3023 -5 -88 -291 C ATOM 1518 CG2 ILE A 225 93.907 -21.569 46.053 1.00 25.52 C ANISOU 1518 CG2 ILE A 225 3605 3276 2817 -105 -41 -209 C ATOM 1519 CD1 ILE A 225 95.533 -19.789 44.330 1.00 28.69 C ANISOU 1519 CD1 ILE A 225 3861 3735 3302 -53 -91 -281 C ATOM 1520 N LEU A 226 93.940 -24.914 45.435 1.00 32.08 N ANISOU 1520 N LEU A 226 4472 3952 3766 -67 -136 -142 N ATOM 1521 CA LEU A 226 92.826 -25.792 45.765 1.00 34.07 C ANISOU 1521 CA LEU A 226 4711 4113 4121 -61 -128 -27 C ATOM 1522 C LEU A 226 93.258 -26.987 46.610 1.00 34.56 C ANISOU 1522 C LEU A 226 4786 4175 4168 17 -118 7 C ATOM 1523 O LEU A 226 92.511 -27.423 47.493 1.00 27.75 O ANISOU 1523 O LEU A 226 3912 3280 3354 50 -79 104 O ATOM 1524 CB LEU A 226 92.127 -26.271 44.492 1.00 30.32 C ANISOU 1524 CB LEU A 226 4237 3540 3745 -133 -188 -12 C ATOM 1525 CG LEU A 226 91.380 -25.185 43.713 1.00 40.18 C ANISOU 1525 CG LEU A 226 5468 4766 5033 -214 -197 -18 C ATOM 1526 CD1 LEU A 226 90.687 -25.770 42.492 1.00 39.39 C ANISOU 1526 CD1 LEU A 226 5368 4565 5033 -282 -257 3 C ATOM 1527 CD2 LEU A 226 90.383 -24.470 44.612 1.00 22.24 C ANISOU 1527 CD2 LEU A 226 3166 2492 2791 -208 -133 65 C ATOM 1528 N LEU A 227 94.462 -27.508 46.364 1.00 28.40 N ANISOU 1528 N LEU A 227 4033 3435 3324 46 -151 -73 N ATOM 1529 CA LEU A 227 94.947 -28.601 47.201 1.00 28.39 C ANISOU 1529 CA LEU A 227 4045 3439 3302 123 -141 -45 C ATOM 1530 C LEU A 227 95.154 -28.136 48.640 1.00 35.62 C ANISOU 1530 C LEU A 227 4953 4432 4151 190 -69 -18 C ATOM 1531 O LEU A 227 94.855 -28.871 49.591 1.00 34.97 O ANISOU 1531 O LEU A 227 4868 4330 4090 243 -40 60 O ATOM 1532 CB LEU A 227 96.246 -29.185 46.644 1.00 36.08 C ANISOU 1532 CB LEU A 227 5048 4446 4216 141 -192 -143 C ATOM 1533 CG LEU A 227 96.087 -30.148 45.465 1.00 40.84 C ANISOU 1533 CG LEU A 227 5662 4964 4893 97 -263 -151 C ATOM 1534 CD1 LEU A 227 97.443 -30.589 44.937 1.00 39.33 C ANISOU 1534 CD1 LEU A 227 5496 4814 4632 114 -310 -259 C ATOM 1535 CD2 LEU A 227 95.248 -31.352 45.868 1.00 35.59 C ANISOU 1535 CD2 LEU A 227 4992 4210 4320 120 -262 -42 C ATOM 1536 N ARG A 228 95.624 -26.901 48.804 1.00 32.24 N ANISOU 1536 N ARG A 228 4519 4089 3643 186 -40 -80 N ATOM 1537 CA ARG A 228 95.817 -26.373 50.151 1.00 24.38 C ANISOU 1537 CA ARG A 228 3514 3169 2582 246 30 -57 C ATOM 1538 C ARG A 228 94.488 -26.119 50.862 1.00 34.50 C ANISOU 1538 C ARG A 228 4766 4408 3935 239 81 55 C ATOM 1539 O ARG A 228 94.316 -26.501 52.022 1.00 25.71 O ANISOU 1539 O ARG A 228 3647 3306 2817 297 127 122 O ATOM 1540 CB ARG A 228 96.641 -25.084 50.114 1.00 25.92 C ANISOU 1540 CB ARG A 228 3704 3463 2680 237 49 -152 C ATOM 1541 CG ARG A 228 96.618 -24.296 51.417 1.00 29.33 C ANISOU 1541 CG ARG A 228 4083 3949 3113 252 115 -114 C ATOM 1542 CD ARG A 228 97.195 -25.084 52.588 1.00 28.51 C ANISOU 1542 CD ARG A 228 3977 3867 2988 324 137 -86 C ATOM 1543 NE ARG A 228 98.636 -25.278 52.466 1.00 33.30 N ANISOU 1543 NE ARG A 228 4552 4491 3610 295 102 -152 N ATOM 1544 CZ ARG A 228 99.540 -24.352 52.771 1.00 26.62 C ANISOU 1544 CZ ARG A 228 3658 3662 2795 232 111 -183 C ATOM 1545 NH1 ARG A 228 99.151 -23.163 53.212 1.00 24.09 N ANISOU 1545 NH1 ARG A 228 3315 3352 2485 213 138 -170 N ATOM 1546 NH2 ARG A 228 100.831 -24.613 52.630 1.00 23.75 N ANISOU 1546 NH2 ARG A 228 3287 3307 2430 248 84 -217 N ATOM 1547 N THR A 229 93.550 -25.477 50.170 1.00 31.45 N ANISOU 1547 N THR A 229 4362 3974 3615 168 72 76 N ATOM 1548 CA THR A 229 92.266 -25.157 50.786 1.00 29.02 C ANISOU 1548 CA THR A 229 4024 3626 3377 157 120 178 C ATOM 1549 C THR A 229 91.459 -26.414 51.074 1.00 30.98 C ANISOU 1549 C THR A 229 4271 3785 3716 173 114 280 C ATOM 1550 O THR A 229 90.618 -26.419 51.965 1.00 46.93 O ANISOU 1550 O THR A 229 6271 5786 5775 192 163 369 O ATOM 1551 CB THR A 229 91.427 -24.209 49.914 1.00 30.55 C ANISOU 1551 CB THR A 229 4198 3783 3626 74 107 176 C ATOM 1552 OG1 THR A 229 91.080 -24.862 48.688 1.00 44.33 O ANISOU 1552 OG1 THR A 229 5953 5442 5448 19 41 174 O ATOM 1553 CG2 THR A 229 92.202 -22.935 49.617 1.00 34.34 C ANISOU 1553 CG2 THR A 229 4679 4351 4016 55 112 76 C ATOM 1554 N TRP A 230 91.709 -27.477 50.317 1.00 30.56 N ANISOU 1554 N TRP A 230 4238 3676 3697 166 55 266 N ATOM 1555 CA TRP A 230 91.055 -28.748 50.596 1.00 29.94 C ANISOU 1555 CA TRP A 230 4162 3515 3699 187 47 357 C ATOM 1556 C TRP A 230 91.708 -29.476 51.774 1.00 43.18 C ANISOU 1556 C TRP A 230 5851 5235 5320 273 77 378 C ATOM 1557 O TRP A 230 91.015 -30.065 52.603 1.00 37.42 O ANISOU 1557 O TRP A 230 5112 4467 4637 304 108 473 O ATOM 1558 CB TRP A 230 91.062 -29.644 49.355 1.00 35.61 C ANISOU 1558 CB TRP A 230 4897 4157 4478 146 -27 337 C ATOM 1559 CG TRP A 230 90.550 -31.029 49.612 1.00 39.10 C ANISOU 1559 CG TRP A 230 5344 4519 4994 172 -40 421 C ATOM 1560 CD1 TRP A 230 89.245 -31.426 49.661 1.00 49.94 C ANISOU 1560 CD1 TRP A 230 6700 5803 6472 147 -32 523 C ATOM 1561 CD2 TRP A 230 91.335 -32.202 49.855 1.00 45.91 C ANISOU 1561 CD2 TRP A 230 6231 5382 5832 228 -63 410 C ATOM 1562 NE1 TRP A 230 89.170 -32.774 49.922 1.00 55.83 N ANISOU 1562 NE1 TRP A 230 7459 6496 7260 184 -48 577 N ATOM 1563 CE2 TRP A 230 90.440 -33.273 50.045 1.00 43.61 C ANISOU 1563 CE2 TRP A 230 5936 5000 5634 234 -68 510 C ATOM 1564 CE3 TRP A 230 92.709 -32.449 49.931 1.00 44.12 C ANISOU 1564 CE3 TRP A 230 6028 5223 5514 274 -81 326 C ATOM 1565 CZ2 TRP A 230 90.874 -34.572 50.306 1.00 56.30 C ANISOU 1565 CZ2 TRP A 230 7563 6583 7246 284 -91 528 C ATOM 1566 CZ3 TRP A 230 93.138 -33.738 50.191 1.00 50.09 C ANISOU 1566 CZ3 TRP A 230 6803 5955 6276 323 -104 343 C ATOM 1567 CH2 TRP A 230 92.224 -34.783 50.375 1.00 49.16 C ANISOU 1567 CH2 TRP A 230 6681 5745 6252 328 -109 444 C ATOM 1568 N SER A 231 93.037 -29.438 51.848 1.00 38.68 N ANISOU 1568 N SER A 231 5302 4743 4651 312 67 289 N ATOM 1569 CA SER A 231 93.747 -30.171 52.897 1.00 29.96 C ANISOU 1569 CA SER A 231 4213 3681 3491 395 89 302 C ATOM 1570 C SER A 231 93.554 -29.593 54.303 1.00 43.03 C ANISOU 1570 C SER A 231 5850 5395 5103 441 166 351 C ATOM 1571 O SER A 231 93.340 -30.336 55.262 1.00 32.58 O ANISOU 1571 O SER A 231 4528 4058 3793 493 194 425 O ATOM 1572 CB SER A 231 95.241 -30.227 52.580 1.00 31.38 C ANISOU 1572 CB SER A 231 4418 3930 3573 422 57 188 C ATOM 1573 OG SER A 231 95.469 -30.806 51.309 1.00 63.67 O ANISOU 1573 OG SER A 231 8524 7968 7700 381 -15 139 O ATOM 1574 N ALA A 232 93.615 -28.270 54.420 1.00 33.57 N ANISOU 1574 N ALA A 232 4636 4262 3855 422 202 312 N ATOM 1575 CA ALA A 232 93.646 -27.619 55.728 1.00 18.20 C ANISOU 1575 CA ALA A 232 2676 2390 1851 469 275 340 C ATOM 1576 C ALA A 232 92.317 -26.970 56.102 1.00 29.30 C ANISOU 1576 C ALA A 232 4048 3761 3324 435 321 424 C ATOM 1577 O ALA A 232 91.802 -26.125 55.369 1.00 43.10 O ANISOU 1577 O ALA A 232 5781 5493 5104 372 312 405 O ATOM 1578 CB ALA A 232 94.757 -26.580 55.763 1.00 26.70 C ANISOU 1578 CB ALA A 232 3758 3575 2813 481 289 235 C ATOM 1579 N ARG A 233 91.771 -27.368 57.248 1.00 29.30 N ANISOU 1579 N ARG A 233 4036 3752 3344 477 369 514 N ATOM 1580 CA ARG A 233 90.539 -26.780 57.759 1.00 38.41 C ANISOU 1580 CA ARG A 233 5157 4880 4556 452 419 596 C ATOM 1581 C ARG A 233 90.710 -25.314 58.134 1.00 37.14 C ANISOU 1581 C ARG A 233 4976 4806 4330 444 468 553 C ATOM 1582 O ARG A 233 89.771 -24.525 58.020 1.00 31.44 O ANISOU 1582 O ARG A 233 4221 4059 3666 393 482 574 O ATOM 1583 CB ARG A 233 90.038 -27.568 58.970 1.00 29.39 C ANISOU 1583 CB ARG A 233 4005 3718 3444 499 457 689 C ATOM 1584 CG ARG A 233 89.052 -28.665 58.618 1.00 54.17 C ANISOU 1584 CG ARG A 233 7135 6747 6699 467 418 753 C ATOM 1585 CD ARG A 233 87.745 -28.090 58.099 1.00 60.53 C ANISOU 1585 CD ARG A 233 7904 7498 7599 388 410 771 C ATOM 1586 NE ARG A 233 87.075 -27.272 59.106 1.00 66.54 N ANISOU 1586 NE ARG A 233 8621 8297 8364 384 462 784 N ATOM 1587 CZ ARG A 233 86.003 -26.523 58.869 1.00 64.57 C ANISOU 1587 CZ ARG A 233 8336 8022 8174 326 462 787 C ATOM 1588 NH1 ARG A 233 85.461 -25.810 59.847 1.00 56.40 N ANISOU 1588 NH1 ARG A 233 7266 7024 7141 332 505 795 N ATOM 1589 NH2 ARG A 233 85.474 -26.482 57.654 1.00 77.00 N ANISOU 1589 NH2 ARG A 233 9913 9536 9808 263 414 777 N ATOM 1590 N GLU A 234 91.908 -24.953 58.583 1.00 29.91 N ANISOU 1590 N GLU A 234 4059 3977 3327 479 466 460 N ATOM 1591 CA GLU A 234 92.188 -23.574 58.965 1.00 34.63 C ANISOU 1591 CA GLU A 234 4615 4630 3912 446 462 380 C ATOM 1592 C GLU A 234 92.178 -22.655 57.748 1.00 28.53 C ANISOU 1592 C GLU A 234 3843 3858 3139 380 434 319 C ATOM 1593 O GLU A 234 91.910 -21.462 57.866 1.00 22.20 O ANISOU 1593 O GLU A 234 3007 3072 2356 333 432 286 O ATOM 1594 CB GLU A 234 93.527 -23.477 59.698 1.00 27.34 C ANISOU 1594 CB GLU A 234 3683 3764 2941 470 434 300 C ATOM 1595 CG GLU A 234 93.762 -24.582 60.717 1.00 42.51 C ANISOU 1595 CG GLU A 234 5616 5688 4849 543 455 352 C ATOM 1596 CD GLU A 234 92.682 -24.657 61.780 1.00 40.39 C ANISOU 1596 CD GLU A 234 5324 5397 4626 562 504 442 C ATOM 1597 OE1 GLU A 234 92.145 -23.599 62.171 1.00 45.49 O ANISOU 1597 OE1 GLU A 234 5936 6049 5300 524 513 434 O ATOM 1598 OE2 GLU A 234 92.369 -25.782 62.224 1.00 36.74 O ANISOU 1598 OE2 GLU A 234 4876 4907 4176 610 529 518 O ATOM 1599 N THR A 235 92.472 -23.213 56.578 1.00 28.65 N ANISOU 1599 N THR A 235 3901 3854 3130 374 408 303 N ATOM 1600 CA THR A 235 92.402 -22.445 55.341 1.00 32.44 C ANISOU 1600 CA THR A 235 4388 4329 3609 311 380 249 C ATOM 1601 C THR A 235 91.017 -22.561 54.706 1.00 26.63 C ANISOU 1601 C THR A 235 3638 3491 2988 251 368 326 C ATOM 1602 O THR A 235 90.562 -23.661 54.388 1.00 25.84 O ANISOU 1602 O THR A 235 3547 3309 2963 246 333 378 O ATOM 1603 CB THR A 235 93.467 -22.904 54.330 1.00 31.88 C ANISOU 1603 CB THR A 235 4354 4268 3489 309 320 159 C ATOM 1604 OG1 THR A 235 94.770 -22.784 54.917 1.00 28.35 O ANISOU 1604 OG1 THR A 235 3878 3874 3021 316 290 76 O ATOM 1605 CG2 THR A 235 93.400 -22.055 53.073 1.00 20.83 C ANISOU 1605 CG2 THR A 235 2953 2859 2101 233 281 93 C ATOM 1606 N ARG A 236 90.355 -21.423 54.523 1.00 31.56 N ANISOU 1606 N ARG A 236 4237 4119 3635 203 389 329 N ATOM 1607 CA ARG A 236 89.004 -21.390 53.962 1.00 41.27 C ANISOU 1607 CA ARG A 236 5446 5254 4981 140 375 397 C ATOM 1608 C ARG A 236 88.969 -21.152 52.450 1.00 37.44 C ANISOU 1608 C ARG A 236 4970 4725 4531 66 309 340 C ATOM 1609 O ARG A 236 89.733 -20.343 51.921 1.00 36.47 O ANISOU 1609 O ARG A 236 4856 4662 4340 47 294 247 O ATOM 1610 CB ARG A 236 88.174 -20.312 54.676 1.00 41.15 C ANISOU 1610 CB ARG A 236 5394 5260 4980 128 438 442 C ATOM 1611 CG ARG A 236 87.024 -19.730 53.855 1.00 41.32 C ANISOU 1611 CG ARG A 236 5392 5211 5096 49 416 466 C ATOM 1612 CD ARG A 236 85.970 -19.091 54.747 1.00 40.94 C ANISOU 1612 CD ARG A 236 5295 5163 5099 41 431 488 C ATOM 1613 NE ARG A 236 86.571 -18.267 55.791 1.00 50.71 N ANISOU 1613 NE ARG A 236 6517 6489 6263 78 457 435 N ATOM 1614 CZ ARG A 236 86.204 -18.297 57.068 1.00 49.95 C ANISOU 1614 CZ ARG A 236 6398 6405 6177 116 481 462 C ATOM 1615 NH1 ARG A 236 85.231 -19.106 57.462 1.00 70.72 N ANISOU 1615 NH1 ARG A 236 9017 8976 8879 126 491 539 N ATOM 1616 NH2 ARG A 236 86.808 -17.515 57.952 1.00 44.88 N ANISOU 1616 NH2 ARG A 236 5744 5829 5479 135 486 405 N ATOM 1617 N SER A 237 88.076 -21.858 51.761 1.00 46.05 N ANISOU 1617 N SER A 237 6059 5712 5726 25 270 396 N ATOM 1618 CA SER A 237 87.780 -21.555 50.366 1.00 41.98 C ANISOU 1618 CA SER A 237 5545 5145 5259 -54 213 358 C ATOM 1619 C SER A 237 86.707 -20.472 50.331 1.00 33.32 C ANISOU 1619 C SER A 237 4416 4029 4216 -105 241 395 C ATOM 1620 O SER A 237 85.518 -20.752 50.453 1.00 47.06 O ANISOU 1620 O SER A 237 6136 5693 6052 -125 251 485 O ATOM 1621 CB SER A 237 87.324 -22.801 49.604 1.00 38.48 C ANISOU 1621 CB SER A 237 5115 4600 4905 -77 157 398 C ATOM 1622 OG SER A 237 87.203 -22.540 48.217 1.00 54.12 O ANISOU 1622 OG SER A 237 7101 6538 6923 -151 98 351 O ATOM 1623 N THR A 238 87.153 -19.231 50.187 1.00 46.05 N ANISOU 1623 N THR A 238 6021 5711 5764 -124 253 325 N ATOM 1624 CA THR A 238 86.285 -18.062 50.223 1.00 35.19 C ANISOU 1624 CA THR A 238 4614 4333 4424 -168 283 348 C ATOM 1625 C THR A 238 85.461 -17.918 48.950 1.00 35.40 C ANISOU 1625 C THR A 238 4635 4275 4542 -252 229 355 C ATOM 1626 O THR A 238 85.793 -18.498 47.917 1.00 38.20 O ANISOU 1626 O THR A 238 5013 4591 4911 -281 168 317 O ATOM 1627 CB THR A 238 87.098 -16.780 50.439 1.00 40.58 C ANISOU 1627 CB THR A 238 5294 5121 5004 -162 310 265 C ATOM 1628 OG1 THR A 238 86.211 -15.673 50.627 1.00 80.49 O ANISOU 1628 OG1 THR A 238 10307 10180 10097 -193 328 287 O ATOM 1629 CG2 THR A 238 87.979 -16.512 49.242 1.00 43.57 C ANISOU 1629 CG2 THR A 238 5698 5521 5336 -201 251 160 C ATOM 1630 N LYS A 239 84.376 -17.155 49.045 1.00 40.32 N ANISOU 1630 N LYS A 239 5228 4901 5189 -276 210 350 N ATOM 1631 CA LYS A 239 83.463 -16.955 47.926 1.00 34.35 C ANISOU 1631 CA LYS A 239 4488 4095 4470 -313 172 299 C ATOM 1632 C LYS A 239 84.167 -16.344 46.714 1.00 35.84 C ANISOU 1632 C LYS A 239 4623 4285 4710 -302 161 245 C ATOM 1633 O LYS A 239 83.919 -16.737 45.561 1.00 42.31 O ANISOU 1633 O LYS A 239 5448 5069 5560 -316 128 206 O ATOM 1634 CB LYS A 239 82.306 -16.049 48.358 1.00 43.14 C ANISOU 1634 CB LYS A 239 5582 5225 5586 -319 178 301 C ATOM 1635 CG LYS A 239 81.542 -16.531 49.590 1.00 64.12 C ANISOU 1635 CG LYS A 239 8214 7877 8274 -279 201 366 C ATOM 1636 CD LYS A 239 80.494 -15.512 50.033 1.00 67.94 C ANISOU 1636 CD LYS A 239 8665 8376 8774 -277 214 368 C ATOM 1637 CE LYS A 239 79.638 -16.040 51.181 1.00 59.35 C ANISOU 1637 CE LYS A 239 7547 7276 7729 -235 242 428 C ATOM 1638 NZ LYS A 239 80.431 -16.309 52.415 1.00 73.07 N ANISOU 1638 NZ LYS A 239 9282 9053 9428 -194 283 451 N ATOM 1639 N THR A 240 85.075 -15.411 46.986 1.00 31.96 N ANISOU 1639 N THR A 240 4137 3873 4134 -324 154 218 N ATOM 1640 CA THR A 240 85.805 -14.724 45.932 1.00 26.92 C ANISOU 1640 CA THR A 240 3519 3269 3440 -358 109 122 C ATOM 1641 C THR A 240 86.660 -15.709 45.143 1.00 32.31 C ANISOU 1641 C THR A 240 4248 3935 4092 -385 63 78 C ATOM 1642 O THR A 240 86.783 -15.603 43.920 1.00 27.95 O ANISOU 1642 O THR A 240 3685 3383 3553 -378 10 30 O ATOM 1643 CB THR A 240 86.700 -13.607 46.512 1.00 23.54 C ANISOU 1643 CB THR A 240 3110 2936 2898 -366 149 60 C ATOM 1644 OG1 THR A 240 85.882 -12.612 47.138 1.00 24.01 O ANISOU 1644 OG1 THR A 240 3122 3006 2994 -329 174 95 O ATOM 1645 CG2 THR A 240 87.533 -12.951 45.421 1.00 19.31 C ANISOU 1645 CG2 THR A 240 2598 2443 2295 -393 104 -40 C ATOM 1646 N LEU A 241 87.219 -16.692 45.842 1.00 29.79 N ANISOU 1646 N LEU A 241 3972 3610 3735 -382 87 104 N ATOM 1647 CA LEU A 241 88.053 -17.691 45.188 1.00 22.19 C ANISOU 1647 CA LEU A 241 3044 2638 2751 -374 33 55 C ATOM 1648 C LEU A 241 87.236 -18.567 44.249 1.00 24.98 C ANISOU 1648 C LEU A 241 3377 2900 3214 -388 -18 94 C ATOM 1649 O LEU A 241 87.679 -18.896 43.149 1.00 28.00 O ANISOU 1649 O LEU A 241 3757 3288 3594 -384 -68 37 O ATOM 1650 CB LEU A 241 88.763 -18.561 46.225 1.00 20.70 C ANISOU 1650 CB LEU A 241 2868 2490 2507 -287 63 66 C ATOM 1651 CG LEU A 241 89.534 -19.767 45.682 1.00 18.04 C ANISOU 1651 CG LEU A 241 2564 2133 2158 -270 9 30 C ATOM 1652 CD1 LEU A 241 90.661 -19.335 44.751 1.00 23.53 C ANISOU 1652 CD1 LEU A 241 3283 2882 2776 -298 -36 -91 C ATOM 1653 CD2 LEU A 241 90.070 -20.611 46.822 1.00 34.34 C ANISOU 1653 CD2 LEU A 241 4637 4232 4178 -183 44 56 C ATOM 1654 N LYS A 242 86.030 -18.920 44.681 1.00 29.81 N ANISOU 1654 N LYS A 242 3947 3463 3915 -356 16 176 N ATOM 1655 CA LYS A 242 85.155 -19.761 43.879 1.00 34.21 C ANISOU 1655 CA LYS A 242 4482 3971 4544 -339 10 183 C ATOM 1656 C LYS A 242 84.727 -19.022 42.618 1.00 33.46 C ANISOU 1656 C LYS A 242 4354 3899 4461 -342 0 123 C ATOM 1657 O LYS A 242 84.747 -19.582 41.507 1.00 28.34 O ANISOU 1657 O LYS A 242 3711 3243 3813 -354 -48 105 O ATOM 1658 CB LYS A 242 83.939 -20.190 44.702 1.00 29.50 C ANISOU 1658 CB LYS A 242 3895 3340 3975 -316 61 247 C ATOM 1659 CG LYS A 242 84.299 -21.032 45.919 1.00 26.16 C ANISOU 1659 CG LYS A 242 3499 2900 3540 -290 72 317 C ATOM 1660 CD LYS A 242 83.179 -21.052 46.950 1.00 46.85 C ANISOU 1660 CD LYS A 242 6116 5521 6164 -270 100 370 C ATOM 1661 CE LYS A 242 83.593 -21.825 48.193 1.00 38.41 C ANISOU 1661 CE LYS A 242 5049 4455 5090 -223 118 439 C ATOM 1662 NZ LYS A 242 82.678 -21.581 49.342 1.00 57.87 N ANISOU 1662 NZ LYS A 242 7484 6940 7563 -198 153 481 N ATOM 1663 N VAL A 243 84.392 -17.744 42.791 1.00 21.73 N ANISOU 1663 N VAL A 243 2847 2442 2967 -346 14 117 N ATOM 1664 CA VAL A 243 84.012 -16.906 41.660 1.00 37.59 C ANISOU 1664 CA VAL A 243 4846 4473 4964 -361 -24 89 C ATOM 1665 C VAL A 243 85.154 -16.772 40.650 1.00 28.07 C ANISOU 1665 C VAL A 243 3658 3308 3700 -366 -73 34 C ATOM 1666 O VAL A 243 84.963 -16.971 39.439 1.00 21.47 O ANISOU 1666 O VAL A 243 2828 2468 2862 -374 -106 28 O ATOM 1667 CB VAL A 243 83.586 -15.499 42.131 1.00 32.85 C ANISOU 1667 CB VAL A 243 4225 3898 4357 -359 1 91 C ATOM 1668 CG1 VAL A 243 83.429 -14.557 40.948 1.00 23.21 C ANISOU 1668 CG1 VAL A 243 3005 2704 3109 -370 -37 62 C ATOM 1669 CG2 VAL A 243 82.303 -15.576 42.942 1.00 29.87 C ANISOU 1669 CG2 VAL A 243 3845 3486 4019 -358 51 140 C ATOM 1670 N VAL A 244 86.344 -16.456 41.157 1.00 27.09 N ANISOU 1670 N VAL A 244 3549 3228 3516 -358 -70 -1 N ATOM 1671 CA VAL A 244 87.506 -16.258 40.299 1.00 25.36 C ANISOU 1671 CA VAL A 244 3356 3058 3224 -354 -94 -50 C ATOM 1672 C VAL A 244 87.882 -17.538 39.559 1.00 28.70 C ANISOU 1672 C VAL A 244 3788 3454 3663 -353 -125 -58 C ATOM 1673 O VAL A 244 88.224 -17.501 38.370 1.00 28.21 O ANISOU 1673 O VAL A 244 3734 3404 3581 -354 -144 -73 O ATOM 1674 CB VAL A 244 88.715 -15.754 41.114 1.00 16.26 C ANISOU 1674 CB VAL A 244 2220 1965 1994 -341 -70 -87 C ATOM 1675 CG1 VAL A 244 89.985 -15.805 40.289 1.00 21.07 C ANISOU 1675 CG1 VAL A 244 2840 2612 2555 -327 -75 -122 C ATOM 1676 CG2 VAL A 244 88.462 -14.340 41.611 1.00 13.29 C ANISOU 1676 CG2 VAL A 244 1837 1629 1584 -345 -33 -83 C ATOM 1677 N VAL A 245 87.777 -18.674 40.244 1.00 20.53 N ANISOU 1677 N VAL A 245 2753 2378 2670 -350 -122 -42 N ATOM 1678 CA VAL A 245 88.055 -19.950 39.599 1.00 30.05 C ANISOU 1678 CA VAL A 245 3970 3556 3891 -349 -150 -46 C ATOM 1679 C VAL A 245 87.057 -20.194 38.469 1.00 22.55 C ANISOU 1679 C VAL A 245 3012 2577 2978 -363 -171 -15 C ATOM 1680 O VAL A 245 87.434 -20.648 37.376 1.00 27.10 O ANISOU 1680 O VAL A 245 3598 3156 3541 -364 -201 -29 O ATOM 1681 CB VAL A 245 88.009 -21.119 40.609 1.00 25.47 C ANISOU 1681 CB VAL A 245 3411 2925 3341 -351 -145 -13 C ATOM 1682 CG1 VAL A 245 87.915 -22.456 39.891 1.00 32.80 C ANISOU 1682 CG1 VAL A 245 4341 3816 4305 -346 -167 -4 C ATOM 1683 CG2 VAL A 245 89.234 -21.085 41.511 1.00 23.24 C ANISOU 1683 CG2 VAL A 245 3187 2671 2972 -359 -160 -46 C ATOM 1684 N ALA A 246 85.797 -19.831 38.706 1.00 18.77 N ANISOU 1684 N ALA A 246 2516 2074 2543 -371 -154 27 N ATOM 1685 CA ALA A 246 84.788 -20.010 37.666 1.00 26.11 C ANISOU 1685 CA ALA A 246 3437 2981 3502 -381 -181 54 C ATOM 1686 C ALA A 246 85.106 -19.153 36.437 1.00 30.57 C ANISOU 1686 C ALA A 246 4008 3580 4027 -386 -204 27 C ATOM 1687 O ALA A 246 85.030 -19.629 35.291 1.00 31.40 O ANISOU 1687 O ALA A 246 4119 3675 4135 -390 -236 30 O ATOM 1688 CB ALA A 246 83.407 -19.677 38.202 1.00 25.52 C ANISOU 1688 CB ALA A 246 3342 2881 3472 -384 -158 99 C ATOM 1689 N VAL A 247 85.507 -17.907 36.674 1.00 19.75 N ANISOU 1689 N VAL A 247 2637 2249 2616 -383 -183 4 N ATOM 1690 CA VAL A 247 85.812 -17.004 35.566 1.00 26.89 C ANISOU 1690 CA VAL A 247 3551 3184 3481 -386 -193 -13 C ATOM 1691 C VAL A 247 87.018 -17.494 34.760 1.00 29.51 C ANISOU 1691 C VAL A 247 3902 3534 3779 -382 -207 -42 C ATOM 1692 O VAL A 247 86.998 -17.515 33.510 1.00 26.36 O ANISOU 1692 O VAL A 247 3508 3131 3376 -388 -226 -40 O ATOM 1693 CB VAL A 247 86.088 -15.575 36.073 1.00 19.42 C ANISOU 1693 CB VAL A 247 2604 2280 2494 -382 -164 -28 C ATOM 1694 CG1 VAL A 247 86.615 -14.697 34.949 1.00 22.23 C ANISOU 1694 CG1 VAL A 247 2973 2667 2805 -385 -165 -43 C ATOM 1695 CG2 VAL A 247 84.831 -14.976 36.688 1.00 12.65 C ANISOU 1695 CG2 VAL A 247 1725 1405 1676 -387 -152 -1 C ATOM 1696 N VAL A 248 88.048 -17.930 35.480 1.00 29.82 N ANISOU 1696 N VAL A 248 3947 3589 3795 -369 -195 -67 N ATOM 1697 CA VAL A 248 89.262 -18.412 34.839 1.00 26.48 C ANISOU 1697 CA VAL A 248 3535 3183 3344 -361 -203 -98 C ATOM 1698 C VAL A 248 88.965 -19.647 33.995 1.00 29.95 C ANISOU 1698 C VAL A 248 3979 3584 3817 -368 -236 -85 C ATOM 1699 O VAL A 248 89.512 -19.801 32.901 1.00 43.84 O ANISOU 1699 O VAL A 248 5744 5349 5564 -369 -248 -99 O ATOM 1700 CB VAL A 248 90.364 -18.743 35.877 1.00 25.54 C ANISOU 1700 CB VAL A 248 3418 3087 3199 -342 -188 -130 C ATOM 1701 CG1 VAL A 248 91.518 -19.497 35.228 1.00 11.17 C ANISOU 1701 CG1 VAL A 248 1602 1277 1365 -329 -201 -163 C ATOM 1702 CG2 VAL A 248 90.865 -17.471 36.546 1.00 19.24 C ANISOU 1702 CG2 VAL A 248 2617 2336 2357 -333 -153 -143 C ATOM 1703 N ALA A 249 88.072 -20.510 34.475 1.00 29.04 N ANISOU 1703 N ALA A 249 3859 3427 3747 -372 -250 -55 N ATOM 1704 CA ALA A 249 87.702 -21.671 33.672 1.00 35.81 C ANISOU 1704 CA ALA A 249 4720 4248 4638 -377 -284 -35 C ATOM 1705 C ALA A 249 86.939 -21.247 32.413 1.00 33.28 C ANISOU 1705 C ALA A 249 4397 3921 4328 -389 -304 -14 C ATOM 1706 O ALA A 249 87.174 -21.778 31.310 1.00 36.27 O ANISOU 1706 O ALA A 249 4783 4291 4706 -392 -329 -17 O ATOM 1707 CB ALA A 249 86.877 -22.644 34.496 1.00 30.74 C ANISOU 1707 CB ALA A 249 4070 3562 4047 -377 -289 1 C ATOM 1708 N SER A 250 86.065 -20.252 32.570 1.00 25.05 N ANISOU 1708 N SER A 250 3342 2882 3293 -395 -293 4 N ATOM 1709 CA SER A 250 85.244 -19.803 31.451 1.00 28.60 C ANISOU 1709 CA SER A 250 3789 3324 3754 -405 -314 24 C ATOM 1710 C SER A 250 86.109 -19.240 30.330 1.00 28.45 C ANISOU 1710 C SER A 250 3785 3332 3691 -408 -313 -2 C ATOM 1711 O SER A 250 85.795 -19.411 29.142 1.00 33.60 O ANISOU 1711 O SER A 250 4441 3972 4352 -416 -339 10 O ATOM 1712 CB SER A 250 84.233 -18.748 31.906 1.00 33.33 C ANISOU 1712 CB SER A 250 4372 3926 4366 -409 -299 43 C ATOM 1713 OG SER A 250 84.881 -17.537 32.254 1.00 31.17 O ANISOU 1713 OG SER A 250 4104 3691 4047 -407 -268 16 O ATOM 1714 N PHE A 251 87.221 -18.611 30.711 1.00 32.97 N ANISOU 1714 N PHE A 251 4364 3942 4222 -401 -283 -36 N ATOM 1715 CA PHE A 251 88.126 -18.033 29.719 1.00 30.43 C ANISOU 1715 CA PHE A 251 4051 3647 3863 -404 -274 -60 C ATOM 1716 C PHE A 251 88.582 -19.079 28.702 1.00 30.25 C ANISOU 1716 C PHE A 251 4035 3608 3849 -406 -299 -67 C ATOM 1717 O PHE A 251 88.378 -18.922 27.487 1.00 26.29 O ANISOU 1717 O PHE A 251 3539 3101 3348 -416 -315 -58 O ATOM 1718 CB PHE A 251 89.345 -17.413 30.414 1.00 16.62 C ANISOU 1718 CB PHE A 251 2301 1939 2075 -392 -239 -94 C ATOM 1719 CG PHE A 251 90.386 -16.871 29.468 1.00 27.97 C ANISOU 1719 CG PHE A 251 3742 3406 3482 -393 -226 -118 C ATOM 1720 CD1 PHE A 251 90.326 -15.557 29.031 1.00 20.80 C ANISOU 1720 CD1 PHE A 251 2835 2520 2549 -402 -206 -113 C ATOM 1721 CD2 PHE A 251 91.435 -17.668 29.030 1.00 26.52 C ANISOU 1721 CD2 PHE A 251 3556 3224 3294 -387 -233 -146 C ATOM 1722 CE1 PHE A 251 91.283 -15.053 28.166 1.00 20.92 C ANISOU 1722 CE1 PHE A 251 2850 2559 2539 -406 -192 -132 C ATOM 1723 CE2 PHE A 251 92.392 -17.170 28.162 1.00 18.38 C ANISOU 1723 CE2 PHE A 251 2524 2218 2241 -388 -221 -168 C ATOM 1724 CZ PHE A 251 92.316 -15.861 27.733 1.00 18.07 C ANISOU 1724 CZ PHE A 251 2486 2200 2179 -399 -200 -159 C ATOM 1725 N PHE A 252 89.177 -20.156 29.205 1.00 20.14 N ANISOU 1725 N PHE A 252 2756 2320 2576 -396 -304 -81 N ATOM 1726 CA PHE A 252 89.684 -21.208 28.337 1.00 29.59 C ANISOU 1726 CA PHE A 252 3959 3502 3781 -397 -327 -91 C ATOM 1727 C PHE A 252 88.554 -21.941 27.634 1.00 33.60 C ANISOU 1727 C PHE A 252 4469 3970 4328 -406 -365 -52 C ATOM 1728 O PHE A 252 88.691 -22.318 26.458 1.00 33.51 O ANISOU 1728 O PHE A 252 4463 3949 4319 -413 -385 -52 O ATOM 1729 CB PHE A 252 90.545 -22.186 29.136 1.00 29.94 C ANISOU 1729 CB PHE A 252 4005 3548 3824 -383 -324 -115 C ATOM 1730 CG PHE A 252 91.708 -21.532 29.827 1.00 28.26 C ANISOU 1730 CG PHE A 252 3784 3378 3575 -368 -291 -156 C ATOM 1731 CD1 PHE A 252 92.819 -21.127 29.106 1.00 18.37 C ANISOU 1731 CD1 PHE A 252 2525 2156 2297 -364 -279 -191 C ATOM 1732 CD2 PHE A 252 91.684 -21.311 31.194 1.00 27.83 C ANISOU 1732 CD2 PHE A 252 3726 3334 3515 -358 -273 -159 C ATOM 1733 CE1 PHE A 252 93.887 -20.517 29.737 1.00 24.75 C ANISOU 1733 CE1 PHE A 252 3322 3005 3078 -346 -254 -226 C ATOM 1734 CE2 PHE A 252 92.751 -20.703 31.830 1.00 21.67 C ANISOU 1734 CE2 PHE A 252 2937 2595 2702 -340 -247 -195 C ATOM 1735 CZ PHE A 252 93.852 -20.306 31.101 1.00 27.18 C ANISOU 1735 CZ PHE A 252 3627 3323 3377 -333 -239 -227 C ATOM 1736 N ILE A 253 87.426 -22.099 28.329 1.00 34.43 N ANISOU 1736 N ILE A 253 4566 4051 4466 -407 -375 -18 N ATOM 1737 CA ILE A 253 86.291 -22.790 27.725 1.00 31.72 C ANISOU 1737 CA ILE A 253 4216 3671 4167 -412 -413 21 C ATOM 1738 C ILE A 253 85.821 -22.088 26.456 1.00 32.91 C ANISOU 1738 C ILE A 253 4368 3824 4312 -424 -426 31 C ATOM 1739 O ILE A 253 85.590 -22.736 25.433 1.00 40.75 O ANISOU 1739 O ILE A 253 5364 4798 5322 -428 -456 44 O ATOM 1740 CB ILE A 253 85.096 -22.896 28.693 1.00 36.60 C ANISOU 1740 CB ILE A 253 4814 4266 4825 -411 -416 55 C ATOM 1741 CG1 ILE A 253 85.408 -23.873 29.825 1.00 30.81 C ANISOU 1741 CG1 ILE A 253 4080 3520 4109 -402 -409 53 C ATOM 1742 CG2 ILE A 253 83.842 -23.341 27.951 1.00 20.04 C ANISOU 1742 CG2 ILE A 253 2703 2138 2774 -417 -452 94 C ATOM 1743 CD1 ILE A 253 84.302 -23.985 30.846 1.00 35.17 C ANISOU 1743 CD1 ILE A 253 4610 4048 4704 -401 -403 87 C ATOM 1744 N PHE A 254 85.719 -20.763 26.497 1.00 28.14 N ANISOU 1744 N PHE A 254 3765 3245 3683 -428 -403 26 N ATOM 1745 CA PHE A 254 85.178 -20.062 25.337 1.00 32.32 C ANISOU 1745 CA PHE A 254 4296 3774 4208 -439 -417 40 C ATOM 1746 C PHE A 254 86.227 -19.662 24.306 1.00 36.16 C ANISOU 1746 C PHE A 254 4798 4283 4656 -445 -405 12 C ATOM 1747 O PHE A 254 85.903 -19.502 23.128 1.00 39.59 O ANISOU 1747 O PHE A 254 5238 4711 5093 -455 -424 23 O ATOM 1748 CB PHE A 254 84.386 -18.837 25.786 1.00 22.46 C ANISOU 1748 CB PHE A 254 3039 2537 2958 -441 -402 52 C ATOM 1749 CG PHE A 254 83.135 -19.189 26.524 1.00 34.86 C ANISOU 1749 CG PHE A 254 4588 4081 4576 -438 -417 85 C ATOM 1750 CD1 PHE A 254 82.131 -19.910 25.897 1.00 36.66 C ANISOU 1750 CD1 PHE A 254 4805 4277 4849 -441 -456 117 C ATOM 1751 CD2 PHE A 254 82.969 -18.827 27.845 1.00 42.36 C ANISOU 1751 CD2 PHE A 254 5527 5037 5530 -432 -391 83 C ATOM 1752 CE1 PHE A 254 80.980 -20.252 26.574 1.00 41.64 C ANISOU 1752 CE1 PHE A 254 5410 4884 5530 -438 -466 148 C ATOM 1753 CE2 PHE A 254 81.823 -19.165 28.525 1.00 39.26 C ANISOU 1753 CE2 PHE A 254 5112 4620 5187 -430 -400 114 C ATOM 1754 CZ PHE A 254 80.826 -19.879 27.891 1.00 41.67 C ANISOU 1754 CZ PHE A 254 5402 4893 5538 -433 -436 147 C ATOM 1755 N TRP A 255 87.477 -19.502 24.728 1.00 23.99 N ANISOU 1755 N TRP A 255 3260 2770 3084 -439 -375 -25 N ATOM 1756 CA TRP A 255 88.515 -19.202 23.750 1.00 22.71 C ANISOU 1756 CA TRP A 255 3106 2630 2893 -445 -363 -52 C ATOM 1757 C TRP A 255 89.044 -20.451 23.042 1.00 25.24 C ANISOU 1757 C TRP A 255 3430 2933 3226 -445 -384 -63 C ATOM 1758 O TRP A 255 89.734 -20.332 22.030 1.00 38.35 O ANISOU 1758 O TRP A 255 5095 4606 4871 -452 -381 -82 O ATOM 1759 CB TRP A 255 89.678 -18.447 24.401 1.00 28.24 C ANISOU 1759 CB TRP A 255 3802 3370 3558 -437 -322 -88 C ATOM 1760 CG TRP A 255 89.453 -16.965 24.509 1.00 26.79 C ANISOU 1760 CG TRP A 255 3618 3210 3350 -441 -298 -83 C ATOM 1761 CD1 TRP A 255 89.273 -16.245 25.654 1.00 38.11 C ANISOU 1761 CD1 TRP A 255 5046 4660 4775 -434 -274 -81 C ATOM 1762 CD2 TRP A 255 89.382 -16.022 23.429 1.00 25.77 C ANISOU 1762 CD2 TRP A 255 3496 3092 3204 -455 -294 -77 C ATOM 1763 NE1 TRP A 255 89.096 -14.915 25.356 1.00 29.55 N ANISOU 1763 NE1 TRP A 255 3965 3596 3667 -442 -256 -75 N ATOM 1764 CE2 TRP A 255 89.158 -14.752 23.997 1.00 23.28 C ANISOU 1764 CE2 TRP A 255 3179 2799 2867 -455 -268 -72 C ATOM 1765 CE3 TRP A 255 89.488 -16.130 22.039 1.00 29.48 C ANISOU 1765 CE3 TRP A 255 3974 3555 3672 -467 -310 -76 C ATOM 1766 CZ2 TRP A 255 89.036 -13.598 23.225 1.00 32.48 C ANISOU 1766 CZ2 TRP A 255 4351 3979 4011 -467 -258 -65 C ATOM 1767 CZ3 TRP A 255 89.367 -14.981 21.272 1.00 21.77 C ANISOU 1767 CZ3 TRP A 255 3005 2594 2675 -480 -300 -69 C ATOM 1768 CH2 TRP A 255 89.145 -13.733 21.867 1.00 29.57 C ANISOU 1768 CH2 TRP A 255 3991 3603 3642 -479 -274 -64 C ATOM 1769 N LEU A 256 88.735 -21.640 23.561 1.00 29.42 N ANISOU 1769 N LEU A 256 3958 3437 3785 -437 -406 -51 N ATOM 1770 CA LEU A 256 89.313 -22.858 22.982 1.00 34.24 C ANISOU 1770 CA LEU A 256 4572 4032 4407 -436 -425 -63 C ATOM 1771 C LEU A 256 89.005 -23.123 21.485 1.00 41.92 C ANISOU 1771 C LEU A 256 5550 4988 5389 -449 -452 -50 C ATOM 1772 O LEU A 256 89.945 -23.312 20.700 1.00 35.44 O ANISOU 1772 O LEU A 256 4733 4180 4554 -453 -447 -79 O ATOM 1773 CB LEU A 256 88.872 -24.071 23.808 1.00 32.49 C ANISOU 1773 CB LEU A 256 4346 3780 4218 -426 -447 -45 C ATOM 1774 CG LEU A 256 89.386 -25.435 23.351 1.00 31.67 C ANISOU 1774 CG LEU A 256 4246 3657 4130 -422 -470 -54 C ATOM 1775 CD1 LEU A 256 90.898 -25.493 23.463 1.00 29.82 C ANISOU 1775 CD1 LEU A 256 4013 3452 3864 -415 -444 -105 C ATOM 1776 CD2 LEU A 256 88.737 -26.541 24.165 1.00 39.09 C ANISOU 1776 CD2 LEU A 256 5181 4564 5108 -413 -494 -28 C ATOM 1777 N PRO A 257 87.716 -23.119 21.075 1.00 39.76 N ANISOU 1777 N PRO A 257 5275 4689 5142 -455 -481 -10 N ATOM 1778 CA PRO A 257 87.473 -23.400 19.648 1.00 37.53 C ANISOU 1778 CA PRO A 257 4998 4393 4869 -467 -507 1 C ATOM 1779 C PRO A 257 88.125 -22.404 18.686 1.00 39.69 C ANISOU 1779 C PRO A 257 5280 4693 5107 -479 -487 -21 C ATOM 1780 O PRO A 257 88.595 -22.795 17.617 1.00 41.91 O ANISOU 1780 O PRO A 257 5566 4972 5385 -487 -496 -33 O ATOM 1781 CB PRO A 257 85.944 -23.343 19.530 1.00 28.69 C ANISOU 1781 CB PRO A 257 3870 3247 3782 -469 -538 47 C ATOM 1782 CG PRO A 257 85.486 -22.584 20.703 1.00 38.51 C ANISOU 1782 CG PRO A 257 5107 4502 5025 -463 -519 55 C ATOM 1783 CD PRO A 257 86.458 -22.859 21.799 1.00 33.41 C ANISOU 1783 CD PRO A 257 4461 3871 4364 -452 -491 26 C ATOM 1784 N TYR A 258 88.188 -21.140 19.089 1.00 39.66 N ANISOU 1784 N TYR A 258 5277 4716 5078 -480 -458 -27 N ATOM 1785 CA TYR A 258 88.769 -20.099 18.251 1.00 24.14 C ANISOU 1785 CA TYR A 258 3317 2777 3079 -492 -437 -45 C ATOM 1786 C TYR A 258 90.272 -20.299 18.100 1.00 38.07 C ANISOU 1786 C TYR A 258 5078 4566 4822 -489 -413 -91 C ATOM 1787 O TYR A 258 90.820 -20.195 16.997 1.00 41.44 O ANISOU 1787 O TYR A 258 5508 5001 5238 -500 -412 -106 O ATOM 1788 CB TYR A 258 88.464 -18.722 18.848 1.00 34.36 C ANISOU 1788 CB TYR A 258 4610 4092 4352 -492 -412 -39 C ATOM 1789 CG TYR A 258 89.214 -17.570 18.224 1.00 41.15 C ANISOU 1789 CG TYR A 258 5475 4985 5177 -501 -384 -59 C ATOM 1790 CD1 TYR A 258 88.714 -16.911 17.111 1.00 57.28 C ANISOU 1790 CD1 TYR A 258 7527 7024 7212 -517 -395 -42 C ATOM 1791 CD2 TYR A 258 90.412 -17.124 18.763 1.00 40.10 C ANISOU 1791 CD2 TYR A 258 5334 4885 5018 -494 -347 -94 C ATOM 1792 CE1 TYR A 258 89.396 -15.848 16.543 1.00 53.53 C ANISOU 1792 CE1 TYR A 258 7056 6578 6704 -527 -369 -57 C ATOM 1793 CE2 TYR A 258 91.101 -16.065 18.202 1.00 46.86 C ANISOU 1793 CE2 TYR A 258 6192 5770 5844 -503 -322 -109 C ATOM 1794 CZ TYR A 258 90.588 -15.431 17.094 1.00 60.41 C ANISOU 1794 CZ TYR A 258 7919 7482 7551 -520 -332 -90 C ATOM 1795 OH TYR A 258 91.272 -14.375 16.537 1.00 75.04 O ANISOU 1795 OH TYR A 258 9774 9364 9373 -530 -305 -102 O ATOM 1796 N GLN A 259 90.931 -20.607 19.213 1.00 35.37 N ANISOU 1796 N GLN A 259 4726 4235 4477 -474 -395 -113 N ATOM 1797 CA GLN A 259 92.372 -20.812 19.208 1.00 40.69 C ANISOU 1797 CA GLN A 259 5391 4934 5134 -468 -375 -159 C ATOM 1798 C GLN A 259 92.738 -22.036 18.384 1.00 34.91 C ANISOU 1798 C GLN A 259 4661 4186 4419 -471 -398 -171 C ATOM 1799 O GLN A 259 93.702 -22.012 17.605 1.00 40.74 O ANISOU 1799 O GLN A 259 5392 4942 5144 -475 -390 -203 O ATOM 1800 CB GLN A 259 92.903 -20.960 20.638 1.00 30.76 C ANISOU 1800 CB GLN A 259 4123 3692 3873 -449 -356 -179 C ATOM 1801 CG GLN A 259 92.916 -19.672 21.448 1.00 22.96 C ANISOU 1801 CG GLN A 259 3131 2731 2863 -444 -325 -179 C ATOM 1802 CD GLN A 259 93.999 -18.703 21.004 1.00 41.63 C ANISOU 1802 CD GLN A 259 5488 5132 5199 -444 -299 -207 C ATOM 1803 OE1 GLN A 259 94.826 -19.020 20.146 1.00 47.65 O ANISOU 1803 OE1 GLN A 259 6246 5902 5958 -446 -303 -232 O ATOM 1804 NE2 GLN A 259 94.000 -17.512 21.592 1.00 36.99 N ANISOU 1804 NE2 GLN A 259 4898 4568 4590 -443 -272 -202 N ATOM 1805 N VAL A 260 91.945 -23.093 18.534 1.00 40.62 N ANISOU 1805 N VAL A 260 5389 4873 5171 -469 -429 -144 N ATOM 1806 CA VAL A 260 92.208 -24.324 17.804 1.00 49.32 C ANISOU 1806 CA VAL A 260 6492 5955 6291 -471 -453 -150 C ATOM 1807 C VAL A 260 91.982 -24.142 16.304 1.00 38.62 C ANISOU 1807 C VAL A 260 5145 4594 4936 -489 -468 -142 C ATOM 1808 O VAL A 260 92.818 -24.547 15.495 1.00 44.03 O ANISOU 1808 O VAL A 260 5827 5287 5616 -494 -467 -171 O ATOM 1809 CB VAL A 260 91.333 -25.484 18.319 1.00 41.45 C ANISOU 1809 CB VAL A 260 5499 4919 5330 -463 -486 -117 C ATOM 1810 CG1 VAL A 260 91.531 -26.720 17.463 1.00 43.05 C ANISOU 1810 CG1 VAL A 260 5705 5100 5553 -466 -514 -120 C ATOM 1811 CG2 VAL A 260 91.664 -25.790 19.772 1.00 32.28 C ANISOU 1811 CG2 VAL A 260 4333 3764 4168 -446 -473 -128 C ATOM 1812 N THR A 261 90.867 -23.521 15.929 1.00 38.09 N ANISOU 1812 N THR A 261 5085 4514 4874 -498 -481 -104 N ATOM 1813 CA THR A 261 90.596 -23.299 14.511 1.00 36.34 C ANISOU 1813 CA THR A 261 4871 4286 4651 -516 -496 -94 C ATOM 1814 C THR A 261 91.609 -22.355 13.872 1.00 40.06 C ANISOU 1814 C THR A 261 5341 4793 5089 -525 -466 -128 C ATOM 1815 O THR A 261 91.962 -22.520 12.705 1.00 49.15 O ANISOU 1815 O THR A 261 6494 5944 6236 -538 -473 -139 O ATOM 1816 CB THR A 261 89.186 -22.732 14.276 1.00 33.67 C ANISOU 1816 CB THR A 261 4539 3930 4324 -522 -517 -47 C ATOM 1817 OG1 THR A 261 89.010 -21.541 15.054 1.00 40.41 O ANISOU 1817 OG1 THR A 261 5392 4804 5159 -519 -492 -44 O ATOM 1818 CG2 THR A 261 88.130 -23.756 14.661 1.00 25.90 C ANISOU 1818 CG2 THR A 261 3552 2909 3382 -514 -554 -12 C ATOM 1819 N GLY A 262 92.087 -21.376 14.636 1.00 32.60 N ANISOU 1819 N GLY A 262 4389 3876 4119 -519 -433 -144 N ATOM 1820 CA GLY A 262 93.074 -20.450 14.112 1.00 30.85 C ANISOU 1820 CA GLY A 262 4164 3690 3869 -525 -405 -174 C ATOM 1821 C GLY A 262 94.415 -21.119 13.877 1.00 34.15 C ANISOU 1821 C GLY A 262 4568 4123 4285 -519 -397 -220 C ATOM 1822 O GLY A 262 94.996 -21.009 12.783 1.00 40.65 O ANISOU 1822 O GLY A 262 5390 4956 5099 -531 -397 -238 O ATOM 1823 N ILE A 263 94.898 -21.838 14.891 1.00 32.32 N ANISOU 1823 N ILE A 263 4325 3894 4062 -501 -394 -241 N ATOM 1824 CA ILE A 263 96.184 -22.514 14.765 1.00 43.93 C ANISOU 1824 CA ILE A 263 5780 5381 5532 -491 -389 -288 C ATOM 1825 C ILE A 263 96.098 -23.596 13.687 1.00 51.90 C ANISOU 1825 C ILE A 263 6794 6367 6559 -503 -415 -289 C ATOM 1826 O ILE A 263 97.090 -23.901 13.027 1.00 55.83 O ANISOU 1826 O ILE A 263 7280 6880 7053 -504 -413 -326 O ATOM 1827 CB ILE A 263 96.664 -23.118 16.112 1.00 44.94 C ANISOU 1827 CB ILE A 263 5895 5516 5665 -469 -382 -309 C ATOM 1828 CG1 ILE A 263 98.123 -23.579 16.017 1.00 27.73 C ANISOU 1828 CG1 ILE A 263 3695 3362 3480 -454 -376 -364 C ATOM 1829 CG2 ILE A 263 95.771 -24.266 16.557 1.00 44.93 C ANISOU 1829 CG2 ILE A 263 5906 5477 5689 -468 -407 -279 C ATOM 1830 CD1 ILE A 263 99.099 -22.478 15.662 1.00 35.30 C ANISOU 1830 CD1 ILE A 263 4643 4353 4417 -448 -359 -389 C ATOM 1831 N MET A 264 94.906 -24.158 13.491 1.00 51.57 N ANISOU 1831 N MET A 264 6767 6288 6538 -512 -443 -246 N ATOM 1832 CA MET A 264 94.712 -25.141 12.431 1.00 53.06 C ANISOU 1832 CA MET A 264 6962 6453 6746 -523 -471 -240 C ATOM 1833 C MET A 264 94.748 -24.501 11.049 1.00 56.97 C ANISOU 1833 C MET A 264 7462 6955 7228 -543 -471 -241 C ATOM 1834 O MET A 264 95.390 -25.020 10.135 1.00 40.35 O ANISOU 1834 O MET A 264 5352 4854 5126 -551 -476 -266 O ATOM 1835 CB MET A 264 93.390 -25.888 12.615 1.00 37.00 C ANISOU 1835 CB MET A 264 4940 4376 4741 -522 -505 -191 C ATOM 1836 CG MET A 264 93.475 -27.064 13.566 1.00 49.10 C ANISOU 1836 CG MET A 264 6469 5891 6294 -505 -517 -192 C ATOM 1837 SD MET A 264 92.053 -28.160 13.416 1.00 60.44 S ANISOU 1837 SD MET A 264 7914 7275 7773 -504 -566 -137 S ATOM 1838 CE MET A 264 90.726 -27.059 13.900 1.00 42.31 C ANISOU 1838 CE MET A 264 5623 4973 5479 -505 -568 -91 C ATOM 1839 N MET A 265 94.055 -23.378 10.892 1.00 42.49 N ANISOU 1839 N MET A 265 5638 5124 5381 -552 -466 -212 N ATOM 1840 CA MET A 265 94.015 -22.709 9.599 1.00 42.40 C ANISOU 1840 CA MET A 265 5635 5119 5356 -572 -466 -208 C ATOM 1841 C MET A 265 95.384 -22.170 9.189 1.00 44.54 C ANISOU 1841 C MET A 265 5893 5427 5604 -574 -440 -254 C ATOM 1842 O MET A 265 95.693 -22.104 8.000 1.00 48.58 O ANISOU 1842 O MET A 265 6406 5942 6109 -589 -444 -263 O ATOM 1843 CB MET A 265 92.984 -21.580 9.605 1.00 43.26 C ANISOU 1843 CB MET A 265 5758 5226 5455 -580 -466 -168 C ATOM 1844 CG MET A 265 91.541 -22.061 9.557 1.00 54.70 C ANISOU 1844 CG MET A 265 7218 6637 6930 -581 -502 -120 C ATOM 1845 SD MET A 265 90.375 -20.705 9.333 1.00 64.58 S ANISOU 1845 SD MET A 265 8483 7887 8169 -592 -506 -78 S ATOM 1846 CE MET A 265 90.798 -19.670 10.734 1.00 43.47 C ANISOU 1846 CE MET A 265 5801 5243 5472 -578 -466 -92 C ATOM 1847 N SER A 266 96.209 -21.789 10.161 1.00 58.96 N ANISOU 1847 N SER A 266 7705 7280 7418 -556 -414 -281 N ATOM 1848 CA SER A 266 97.557 -21.334 9.822 1.00 53.72 C ANISOU 1848 CA SER A 266 7027 6649 6736 -553 -395 -323 C ATOM 1849 C SER A 266 98.443 -22.461 9.280 1.00 51.87 C ANISOU 1849 C SER A 266 6779 6415 6516 -549 -407 -362 C ATOM 1850 O SER A 266 99.398 -22.206 8.547 1.00 52.21 O ANISOU 1850 O SER A 266 6815 6477 6547 -552 -402 -390 O ATOM 1851 CB SER A 266 98.226 -20.684 11.033 1.00 60.39 C ANISOU 1851 CB SER A 266 7861 7520 7566 -532 -370 -339 C ATOM 1852 OG SER A 266 97.668 -19.406 11.286 1.00 59.43 O ANISOU 1852 OG SER A 266 7751 7408 7424 -541 -351 -309 O ATOM 1853 N PHE A 267 98.127 -23.701 9.647 1.00 56.15 N ANISOU 1853 N PHE A 267 7319 6934 7082 -543 -425 -362 N ATOM 1854 CA PHE A 267 98.908 -24.856 9.208 1.00 49.01 C ANISOU 1854 CA PHE A 267 6401 6030 6191 -539 -436 -399 C ATOM 1855 C PHE A 267 98.236 -25.640 8.077 1.00 69.12 C ANISOU 1855 C PHE A 267 8961 8548 8755 -560 -461 -379 C ATOM 1856 O PHE A 267 98.678 -26.734 7.726 1.00 72.26 O ANISOU 1856 O PHE A 267 9350 8939 9165 -561 -473 -402 O ATOM 1857 CB PHE A 267 99.184 -25.787 10.391 1.00 51.78 C ANISOU 1857 CB PHE A 267 6741 6380 6554 -519 -436 -416 C ATOM 1858 CG PHE A 267 100.365 -25.375 11.227 1.00 64.29 C ANISOU 1858 CG PHE A 267 8303 7998 8126 -493 -417 -458 C ATOM 1859 CD1 PHE A 267 100.247 -24.370 12.173 1.00 51.27 C ANISOU 1859 CD1 PHE A 267 6656 6361 6463 -480 -401 -445 C ATOM 1860 CD2 PHE A 267 101.592 -25.999 11.070 1.00 60.50 C ANISOU 1860 CD2 PHE A 267 7801 7536 7648 -478 -420 -510 C ATOM 1861 CE1 PHE A 267 101.332 -23.992 12.941 1.00 51.92 C ANISOU 1861 CE1 PHE A 267 6723 6469 6534 -452 -392 -477 C ATOM 1862 CE2 PHE A 267 102.680 -25.626 11.837 1.00 58.10 C ANISOU 1862 CE2 PHE A 267 7483 7257 7337 -444 -416 -541 C ATOM 1863 CZ PHE A 267 102.550 -24.620 12.772 1.00 53.91 C ANISOU 1863 CZ PHE A 267 6958 6733 6790 -432 -406 -523 C ATOM 1864 N LEU A 268 97.164 -25.085 7.519 1.00 65.75 N ANISOU 1864 N LEU A 268 8554 8103 8326 -577 -471 -335 N ATOM 1865 CA LEU A 268 96.440 -25.737 6.429 1.00 55.65 C ANISOU 1865 CA LEU A 268 7288 6795 7063 -595 -499 -310 C ATOM 1866 C LEU A 268 96.508 -24.950 5.122 1.00 60.23 C ANISOU 1866 C LEU A 268 7873 7384 7626 -617 -497 -309 C ATOM 1867 O LEU A 268 96.640 -23.725 5.131 1.00 65.37 O ANISOU 1867 O LEU A 268 8528 8056 8253 -620 -477 -306 O ATOM 1868 CB LEU A 268 94.973 -25.954 6.816 1.00 46.62 C ANISOU 1868 CB LEU A 268 6161 5615 5937 -595 -524 -254 C ATOM 1869 CG LEU A 268 94.644 -27.148 7.715 1.00 42.18 C ANISOU 1869 CG LEU A 268 5598 5027 5401 -579 -542 -242 C ATOM 1870 CD1 LEU A 268 93.159 -27.186 8.053 1.00 36.69 C ANISOU 1870 CD1 LEU A 268 4916 4298 4726 -576 -568 -185 C ATOM 1871 CD2 LEU A 268 95.077 -28.448 7.059 1.00 45.07 C ANISOU 1871 CD2 LEU A 268 5959 5380 5786 -582 -560 -262 C ATOM 1872 N GLU A 269 96.439 -25.668 4.004 1.00 67.78 N ANISOU 1872 N GLU A 269 8833 8325 8594 -632 -516 -311 N ATOM 1873 CA GLU A 269 96.304 -25.061 2.682 1.00 61.75 C ANISOU 1873 CA GLU A 269 8080 7566 7818 -655 -520 -303 C ATOM 1874 C GLU A 269 94.879 -24.585 2.420 1.00 68.93 C ANISOU 1874 C GLU A 269 9011 8450 8729 -666 -539 -246 C ATOM 1875 O GLU A 269 93.921 -25.247 2.814 1.00 70.03 O ANISOU 1875 O GLU A 269 9157 8560 8893 -659 -563 -213 O ATOM 1876 CB GLU A 269 96.724 -26.051 1.597 1.00 62.93 C ANISOU 1876 CB GLU A 269 8223 7707 7981 -666 -535 -326 C ATOM 1877 CG GLU A 269 98.217 -26.293 1.536 1.00 81.27 C ANISOU 1877 CG GLU A 269 10522 10059 10298 -658 -518 -386 C ATOM 1878 CD GLU A 269 98.577 -27.424 0.596 1.00107.33 C ANISOU 1878 CD GLU A 269 13815 13351 13616 -668 -534 -410 C ATOM 1879 OE1 GLU A 269 97.822 -28.420 0.544 1.00113.57 O ANISOU 1879 OE1 GLU A 269 14613 14109 14429 -671 -558 -386 O ATOM 1880 OE2 GLU A 269 99.614 -27.320 -0.091 1.00118.41 O ANISOU 1880 OE2 GLU A 269 15204 14776 15011 -671 -526 -451 O ATOM 1881 N PRO A 270 94.738 -23.430 1.744 1.00 74.84 N ANISOU 1881 N PRO A 270 9771 9212 9453 -682 -530 -233 N ATOM 1882 CA PRO A 270 93.423 -22.914 1.344 1.00 68.67 C ANISOU 1882 CA PRO A 270 9010 8410 8672 -694 -550 -182 C ATOM 1883 C PRO A 270 92.650 -23.880 0.440 1.00 77.13 C ANISOU 1883 C PRO A 270 10089 9449 9769 -704 -587 -159 C ATOM 1884 O PRO A 270 91.421 -23.931 0.510 1.00 70.13 O ANISOU 1884 O PRO A 270 9212 8535 8898 -703 -613 -115 O ATOM 1885 CB PRO A 270 93.777 -21.627 0.587 1.00 65.96 C ANISOU 1885 CB PRO A 270 8675 8093 8294 -712 -530 -186 C ATOM 1886 CG PRO A 270 95.101 -21.215 1.136 1.00 55.97 C ANISOU 1886 CG PRO A 270 7394 6862 7010 -703 -495 -229 C ATOM 1887 CD PRO A 270 95.826 -22.495 1.425 1.00 55.83 C ANISOU 1887 CD PRO A 270 7357 6840 7015 -688 -500 -266 C ATOM 1888 N SER A 271 93.365 -24.640 -0.376 1.00 74.20 N ANISOU 1888 N SER A 271 9709 9079 9404 -713 -590 -189 N ATOM 1889 CA SER A 271 92.752 -25.602 -1.291 1.00 73.82 C ANISOU 1889 CA SER A 271 9667 9002 9380 -723 -624 -171 C ATOM 1890 C SER A 271 92.105 -26.773 -0.549 1.00 69.65 C ANISOU 1890 C SER A 271 9134 8443 8888 -705 -649 -151 C ATOM 1891 O SER A 271 91.250 -27.469 -1.096 1.00 76.26 O ANISOU 1891 O SER A 271 9977 9250 9750 -710 -682 -122 O ATOM 1892 CB SER A 271 93.788 -26.123 -2.292 1.00 57.83 C ANISOU 1892 CB SER A 271 7631 6989 7352 -737 -617 -214 C ATOM 1893 OG SER A 271 94.886 -26.733 -1.634 1.00 66.76 O ANISOU 1893 OG SER A 271 8742 8136 8487 -721 -600 -260 O ATOM 1894 N SER A 272 92.535 -26.996 0.689 1.00 63.48 N ANISOU 1894 N SER A 272 8342 7668 8110 -685 -634 -168 N ATOM 1895 CA SER A 272 92.007 -28.070 1.523 1.00 61.54 C ANISOU 1895 CA SER A 272 8092 7394 7896 -666 -656 -149 C ATOM 1896 C SER A 272 90.555 -27.830 1.938 1.00 62.07 C ANISOU 1896 C SER A 272 8168 7435 7979 -660 -681 -93 C ATOM 1897 O SER A 272 90.203 -26.730 2.368 1.00 56.20 O ANISOU 1897 O SER A 272 7431 6705 7219 -659 -668 -78 O ATOM 1898 CB SER A 272 92.877 -28.241 2.771 1.00 64.85 C ANISOU 1898 CB SER A 272 8499 7831 8310 -647 -631 -181 C ATOM 1899 OG SER A 272 92.337 -29.211 3.648 1.00 65.20 O ANISOU 1899 OG SER A 272 8541 7848 8383 -629 -652 -160 O ATOM 1900 N PRO A 273 89.702 -28.863 1.798 1.00 57.24 N ANISOU 1900 N PRO A 273 7556 6789 7404 -654 -718 -63 N ATOM 1901 CA PRO A 273 88.287 -28.764 2.177 1.00 57.06 C ANISOU 1901 CA PRO A 273 7536 6741 7405 -646 -747 -10 C ATOM 1902 C PRO A 273 88.051 -28.418 3.646 1.00 54.82 C ANISOU 1902 C PRO A 273 7247 6461 7121 -626 -736 -1 C ATOM 1903 O PRO A 273 87.135 -27.646 3.953 1.00 50.06 O ANISOU 1903 O PRO A 273 6647 5855 6519 -624 -742 31 O ATOM 1904 CB PRO A 273 87.752 -30.173 1.877 1.00 48.52 C ANISOU 1904 CB PRO A 273 6446 5624 6365 -640 -785 9 C ATOM 1905 CG PRO A 273 88.720 -30.763 0.903 1.00 43.98 C ANISOU 1905 CG PRO A 273 5871 5056 5783 -654 -778 -28 C ATOM 1906 CD PRO A 273 90.049 -30.193 1.277 1.00 50.48 C ANISOU 1906 CD PRO A 273 6693 5916 6571 -656 -735 -77 C ATOM 1907 N THR A 274 88.890 -28.940 4.533 1.00 50.58 N ANISOU 1907 N THR A 274 6703 5932 6584 -612 -718 -30 N ATOM 1908 CA THR A 274 88.725 -28.684 5.967 1.00 63.09 C ANISOU 1908 CA THR A 274 8283 7520 8169 -594 -706 -22 C ATOM 1909 C THR A 274 89.062 -27.232 6.298 1.00 54.66 C ANISOU 1909 C THR A 274 7219 6485 7063 -598 -671 -35 C ATOM 1910 O THR A 274 88.496 -26.648 7.226 1.00 48.89 O ANISOU 1910 O THR A 274 6488 5756 6332 -588 -666 -16 O ATOM 1911 CB THR A 274 89.580 -29.648 6.832 1.00 40.63 C ANISOU 1911 CB THR A 274 5428 4675 5332 -578 -697 -51 C ATOM 1912 OG1 THR A 274 89.456 -29.296 8.216 1.00 55.33 O ANISOU 1912 OG1 THR A 274 7288 6544 7192 -562 -683 -45 O ATOM 1913 CG2 THR A 274 91.043 -29.602 6.433 1.00 58.61 C ANISOU 1913 CG2 THR A 274 7704 6982 7582 -586 -667 -106 C ATOM 1914 N PHE A 275 89.964 -26.650 5.515 1.00 46.92 N ANISOU 1914 N PHE A 275 6243 5530 6053 -613 -647 -68 N ATOM 1915 CA PHE A 275 90.291 -25.238 5.645 1.00 50.45 C ANISOU 1915 CA PHE A 275 6694 6009 6465 -619 -616 -79 C ATOM 1916 C PHE A 275 89.075 -24.398 5.305 1.00 53.97 C ANISOU 1916 C PHE A 275 7151 6445 6911 -627 -632 -35 C ATOM 1917 O PHE A 275 88.768 -23.426 5.991 1.00 57.20 O ANISOU 1917 O PHE A 275 7563 6866 7306 -622 -618 -24 O ATOM 1918 CB PHE A 275 91.460 -24.874 4.727 1.00 50.28 C ANISOU 1918 CB PHE A 275 6671 6015 6417 -635 -592 -120 C ATOM 1919 CG PHE A 275 91.811 -23.408 4.725 1.00 51.60 C ANISOU 1919 CG PHE A 275 6842 6214 6549 -642 -561 -129 C ATOM 1920 CD1 PHE A 275 91.128 -22.510 3.916 1.00 58.58 C ANISOU 1920 CD1 PHE A 275 7741 7097 7421 -658 -569 -101 C ATOM 1921 CD2 PHE A 275 92.846 -22.935 5.512 1.00 65.08 C ANISOU 1921 CD2 PHE A 275 8538 7952 8237 -631 -526 -165 C ATOM 1922 CE1 PHE A 275 91.457 -21.170 3.911 1.00 65.78 C ANISOU 1922 CE1 PHE A 275 8657 8037 8299 -665 -541 -108 C ATOM 1923 CE2 PHE A 275 93.181 -21.596 5.509 1.00 60.45 C ANISOU 1923 CE2 PHE A 275 7954 7394 7619 -637 -499 -171 C ATOM 1924 CZ PHE A 275 92.486 -20.712 4.707 1.00 51.47 C ANISOU 1924 CZ PHE A 275 6833 6255 6468 -655 -506 -141 C ATOM 1925 N LEU A 276 88.388 -24.784 4.235 1.00 57.20 N ANISOU 1925 N LEU A 276 7565 6831 7336 -639 -664 -11 N ATOM 1926 CA LEU A 276 87.192 -24.085 3.792 1.00 59.48 C ANISOU 1926 CA LEU A 276 7863 7109 7629 -646 -686 30 C ATOM 1927 C LEU A 276 86.098 -24.196 4.843 1.00 51.87 C ANISOU 1927 C LEU A 276 6892 6126 6692 -628 -705 65 C ATOM 1928 O LEU A 276 85.384 -23.222 5.129 1.00 56.52 O ANISOU 1928 O LEU A 276 7483 6719 7273 -627 -705 87 O ATOM 1929 CB LEU A 276 86.718 -24.659 2.453 1.00 75.37 C ANISOU 1929 CB LEU A 276 9879 9100 9657 -661 -719 47 C ATOM 1930 CG LEU A 276 85.326 -24.310 1.925 1.00 65.13 C ANISOU 1930 CG LEU A 276 8587 7783 8376 -666 -753 93 C ATOM 1931 CD1 LEU A 276 85.230 -22.838 1.566 1.00 64.26 C ANISOU 1931 CD1 LEU A 276 8491 7695 8232 -679 -737 98 C ATOM 1932 CD2 LEU A 276 84.980 -25.186 0.727 1.00 60.28 C ANISOU 1932 CD2 LEU A 276 7973 7146 7784 -677 -786 105 C ATOM 1933 N LEU A 277 86.001 -25.377 5.448 1.00 46.90 N ANISOU 1933 N LEU A 277 6250 5476 6092 -613 -720 68 N ATOM 1934 CA LEU A 277 85.010 -25.593 6.492 1.00 50.44 C ANISOU 1934 CA LEU A 277 6687 5907 6570 -595 -738 99 C ATOM 1935 C LEU A 277 85.300 -24.720 7.709 1.00 55.87 C ANISOU 1935 C LEU A 277 7374 6617 7236 -586 -705 88 C ATOM 1936 O LEU A 277 84.384 -24.136 8.286 1.00 51.11 O ANISOU 1936 O LEU A 277 6767 6011 6642 -579 -712 114 O ATOM 1937 CB LEU A 277 84.962 -27.066 6.899 1.00 39.28 C ANISOU 1937 CB LEU A 277 5262 4469 5194 -582 -759 103 C ATOM 1938 CG LEU A 277 84.082 -27.367 8.115 1.00 43.06 C ANISOU 1938 CG LEU A 277 5725 4931 5705 -563 -773 131 C ATOM 1939 CD1 LEU A 277 82.645 -26.925 7.873 1.00 44.74 C ANISOU 1939 CD1 LEU A 277 5929 5129 5940 -564 -802 174 C ATOM 1940 CD2 LEU A 277 84.144 -28.842 8.469 1.00 41.35 C ANISOU 1940 CD2 LEU A 277 5496 4691 5523 -550 -793 132 C ATOM 1941 N LEU A 278 86.572 -24.613 8.085 1.00 44.91 N ANISOU 1941 N LEU A 278 5989 5254 5821 -584 -669 47 N ATOM 1942 CA LEU A 278 86.939 -23.746 9.198 1.00 44.76 C ANISOU 1942 CA LEU A 278 5968 5259 5779 -576 -635 33 C ATOM 1943 C LEU A 278 86.700 -22.285 8.851 1.00 42.67 C ANISOU 1943 C LEU A 278 5712 5014 5485 -587 -620 40 C ATOM 1944 O LEU A 278 86.353 -21.480 9.714 1.00 47.61 O ANISOU 1944 O LEU A 278 6335 5650 6103 -580 -606 48 O ATOM 1945 CB LEU A 278 88.400 -23.959 9.594 1.00 47.24 C ANISOU 1945 CB LEU A 278 6279 5598 6072 -572 -601 -15 C ATOM 1946 CG LEU A 278 88.736 -25.329 10.182 1.00 43.72 C ANISOU 1946 CG LEU A 278 5825 5136 5652 -558 -612 -26 C ATOM 1947 CD1 LEU A 278 90.167 -25.353 10.687 1.00 42.52 C ANISOU 1947 CD1 LEU A 278 5668 5013 5477 -552 -577 -75 C ATOM 1948 CD2 LEU A 278 87.761 -25.693 11.290 1.00 30.55 C ANISOU 1948 CD2 LEU A 278 4149 3446 4011 -542 -630 7 C ATOM 1949 N LYS A 279 86.881 -21.947 7.579 1.00 57.67 N ANISOU 1949 N LYS A 279 7623 6920 7371 -605 -623 36 N ATOM 1950 CA LYS A 279 86.656 -20.587 7.121 1.00 55.60 C ANISOU 1950 CA LYS A 279 7370 6674 7081 -618 -612 44 C ATOM 1951 C LYS A 279 85.180 -20.218 7.250 1.00 56.65 C ANISOU 1951 C LYS A 279 7503 6788 7235 -615 -641 89 C ATOM 1952 O LYS A 279 84.847 -19.080 7.580 1.00 51.08 O ANISOU 1952 O LYS A 279 6800 6096 6512 -615 -628 98 O ATOM 1953 CB LYS A 279 87.131 -20.430 5.674 1.00 50.64 C ANISOU 1953 CB LYS A 279 6752 6053 6435 -639 -612 33 C ATOM 1954 CG LYS A 279 87.229 -18.996 5.176 1.00 67.55 C ANISOU 1954 CG LYS A 279 8906 8218 8541 -654 -593 34 C ATOM 1955 CD LYS A 279 87.663 -18.974 3.716 1.00 95.14 C ANISOU 1955 CD LYS A 279 12411 11717 12022 -676 -597 24 C ATOM 1956 CE LYS A 279 87.998 -17.572 3.236 1.00 94.28 C ANISOU 1956 CE LYS A 279 12313 11635 11875 -691 -572 19 C ATOM 1957 NZ LYS A 279 88.468 -17.568 1.819 1.00 65.70 N ANISOU 1957 NZ LYS A 279 8702 8020 8240 -714 -575 9 N ATOM 1958 N LYS A 280 84.297 -21.183 7.003 1.00 54.70 N ANISOU 1958 N LYS A 280 7249 6510 7027 -610 -681 116 N ATOM 1959 CA LYS A 280 82.863 -20.947 7.186 1.00 53.29 C ANISOU 1959 CA LYS A 280 7061 6311 6874 -605 -712 158 C ATOM 1960 C LYS A 280 82.452 -20.802 8.653 1.00 49.22 C ANISOU 1960 C LYS A 280 6532 5797 6373 -586 -703 165 C ATOM 1961 O LYS A 280 81.487 -20.107 8.970 1.00 59.27 O ANISOU 1961 O LYS A 280 7798 7066 7655 -583 -713 190 O ATOM 1962 CB LYS A 280 82.056 -22.071 6.539 1.00 64.60 C ANISOU 1962 CB LYS A 280 8486 7711 8350 -604 -756 184 C ATOM 1963 CG LYS A 280 82.208 -22.143 5.031 1.00 63.63 C ANISOU 1963 CG LYS A 280 8376 7585 8217 -623 -770 184 C ATOM 1964 CD LYS A 280 81.521 -23.372 4.465 1.00 70.58 C ANISOU 1964 CD LYS A 280 9244 8432 9139 -621 -812 206 C ATOM 1965 CE LYS A 280 81.741 -23.476 2.966 1.00 71.18 C ANISOU 1965 CE LYS A 280 9334 8507 9205 -642 -823 203 C ATOM 1966 NZ LYS A 280 81.161 -24.727 2.408 1.00 79.14 N ANISOU 1966 NZ LYS A 280 10332 9485 10255 -640 -862 222 N ATOM 1967 N LEU A 281 83.194 -21.457 9.541 1.00 54.53 N ANISOU 1967 N LEU A 281 7199 6474 7046 -575 -685 142 N ATOM 1968 CA LEU A 281 82.839 -21.523 10.959 1.00 54.12 C ANISOU 1968 CA LEU A 281 7133 6420 7011 -558 -678 149 C ATOM 1969 C LEU A 281 83.374 -20.349 11.777 1.00 55.43 C ANISOU 1969 C LEU A 281 7303 6616 7140 -556 -637 129 C ATOM 1970 O LEU A 281 83.132 -20.266 12.982 1.00 49.10 O ANISOU 1970 O LEU A 281 6491 5817 6348 -543 -627 132 O ATOM 1971 CB LEU A 281 83.343 -22.834 11.567 1.00 40.60 C ANISOU 1971 CB LEU A 281 5413 4696 5318 -546 -680 136 C ATOM 1972 CG LEU A 281 82.684 -24.126 11.081 1.00 53.63 C ANISOU 1972 CG LEU A 281 7052 6313 7013 -543 -722 160 C ATOM 1973 CD1 LEU A 281 83.374 -25.339 11.687 1.00 31.65 C ANISOU 1973 CD1 LEU A 281 4263 3521 4242 -532 -719 143 C ATOM 1974 CD2 LEU A 281 81.200 -24.128 11.414 1.00 63.11 C ANISOU 1974 CD2 LEU A 281 8233 7493 8254 -536 -752 201 C ATOM 1975 N ASP A 282 84.099 -19.449 11.119 1.00 51.41 N ANISOU 1975 N ASP A 282 7233 5651 6650 -189 -148 387 N ATOM 1976 CA ASP A 282 84.838 -18.394 11.809 1.00 51.62 C ANISOU 1976 CA ASP A 282 7257 5673 6685 -161 -115 369 C ATOM 1977 C ASP A 282 83.956 -17.472 12.659 1.00 45.08 C ANISOU 1977 C ASP A 282 6374 4908 5846 -122 -133 364 C ATOM 1978 O ASP A 282 84.305 -17.154 13.803 1.00 42.24 O ANISOU 1978 O ASP A 282 5969 4579 5501 -112 -114 360 O ATOM 1979 CB ASP A 282 85.619 -17.568 10.780 1.00 46.08 C ANISOU 1979 CB ASP A 282 6639 4897 5973 -144 -92 349 C ATOM 1980 CG ASP A 282 86.243 -16.323 11.377 1.00 57.76 C ANISOU 1980 CG ASP A 282 8119 6370 7456 -109 -64 329 C ATOM 1981 OD1 ASP A 282 87.339 -16.428 11.968 1.00 65.00 O ANISOU 1981 OD1 ASP A 282 9031 7269 8396 -121 -26 325 O ATOM 1982 OD2 ASP A 282 85.642 -15.236 11.242 1.00 61.17 O ANISOU 1982 OD2 ASP A 282 8557 6815 7868 -70 -79 318 O ATOM 1983 N SER A 283 82.810 -17.066 12.121 1.00 31.44 N ANISOU 1983 N SER A 283 4652 3201 4094 -100 -171 365 N ATOM 1984 CA SER A 283 81.926 -16.161 12.852 1.00 40.51 C ANISOU 1984 CA SER A 283 5752 4409 5232 -62 -191 360 C ATOM 1985 C SER A 283 81.369 -16.811 14.112 1.00 36.69 C ANISOU 1985 C SER A 283 5181 3999 4762 -74 -202 376 C ATOM 1986 O SER A 283 81.222 -16.159 15.153 1.00 34.31 O ANISOU 1986 O SER A 283 4830 3742 4463 -48 -197 371 O ATOM 1987 CB SER A 283 80.775 -15.695 11.959 1.00 35.21 C ANISOU 1987 CB SER A 283 5104 3743 4532 -39 -231 359 C ATOM 1988 OG SER A 283 81.225 -14.768 10.988 1.00 44.90 O ANISOU 1988 OG SER A 283 6406 4910 5745 -17 -220 340 O ATOM 1989 N LEU A 284 81.081 -18.104 14.020 1.00 34.21 N ANISOU 1989 N LEU A 284 4845 3697 4455 -112 -218 397 N ATOM 1990 CA LEU A 284 80.557 -18.834 15.163 1.00 41.46 C ANISOU 1990 CA LEU A 284 5681 4685 5387 -128 -229 415 C ATOM 1991 C LEU A 284 81.608 -18.939 16.264 1.00 43.57 C ANISOU 1991 C LEU A 284 5918 4956 5680 -137 -190 412 C ATOM 1992 O LEU A 284 81.289 -18.823 17.451 1.00 31.20 O ANISOU 1992 O LEU A 284 4284 3449 4120 -127 -191 416 O ATOM 1993 CB LEU A 284 80.082 -20.227 14.741 1.00 30.12 C ANISOU 1993 CB LEU A 284 4235 3255 3955 -169 -254 438 C ATOM 1994 CG LEU A 284 79.387 -21.054 15.825 1.00 43.15 C ANISOU 1994 CG LEU A 284 5799 4979 5617 -187 -272 459 C ATOM 1995 CD1 LEU A 284 78.217 -20.284 16.418 1.00 32.90 C ANISOU 1995 CD1 LEU A 284 4450 3746 4304 -149 -300 459 C ATOM 1996 CD2 LEU A 284 78.924 -22.393 15.271 1.00 37.92 C ANISOU 1996 CD2 LEU A 284 5134 4317 4957 -227 -298 481 C ATOM 1997 N CYS A 285 82.865 -19.127 15.866 1.00 31.93 N ANISOU 1997 N CYS A 285 4494 3419 4218 -156 -154 404 N ATOM 1998 CA CYS A 285 83.962 -19.189 16.823 1.00 39.50 C ANISOU 1998 CA CYS A 285 5432 4374 5203 -166 -115 399 C ATOM 1999 C CYS A 285 84.175 -17.841 17.494 1.00 39.27 C ANISOU 1999 C CYS A 285 5393 4357 5170 -122 -98 380 C ATOM 2000 O CYS A 285 84.437 -17.770 18.699 1.00 37.83 O ANISOU 2000 O CYS A 285 5158 4212 5003 -119 -83 380 O ATOM 2001 CB CYS A 285 85.255 -19.639 16.139 1.00 32.97 C ANISOU 2001 CB CYS A 285 4666 3472 4390 -194 -81 394 C ATOM 2002 SG CYS A 285 85.305 -21.390 15.694 1.00 44.85 S ANISOU 2002 SG CYS A 285 6171 4965 5907 -251 -91 418 S ATOM 2003 N VAL A 286 84.049 -16.771 16.714 1.00 30.34 N ANISOU 2003 N VAL A 286 4313 3195 4019 -89 -103 363 N ATOM 2004 CA VAL A 286 84.178 -15.433 17.273 1.00 30.78 C ANISOU 2004 CA VAL A 286 4363 3263 4070 -45 -90 345 C ATOM 2005 C VAL A 286 83.046 -15.159 18.266 1.00 38.26 C ANISOU 2005 C VAL A 286 5236 4292 5010 -22 -117 351 C ATOM 2006 O VAL A 286 83.256 -14.514 19.295 1.00 41.54 O ANISOU 2006 O VAL A 286 5615 4736 5432 0 -102 342 O ATOM 2007 CB VAL A 286 84.197 -14.357 16.160 1.00 24.13 C ANISOU 2007 CB VAL A 286 3592 2371 3206 -14 -93 326 C ATOM 2008 CG1 VAL A 286 84.165 -12.956 16.749 1.00 22.61 C ANISOU 2008 CG1 VAL A 286 3389 2196 3006 33 -86 308 C ATOM 2009 CG2 VAL A 286 85.429 -14.528 15.278 1.00 27.22 C ANISOU 2009 CG2 VAL A 286 4056 2679 3605 -34 -61 319 C ATOM 2010 N SER A 287 81.860 -15.694 17.986 1.00 26.34 N ANISOU 2010 N SER A 287 3701 2819 3487 -29 -157 366 N ATOM 2011 CA SER A 287 80.723 -15.498 18.885 1.00 41.66 C ANISOU 2011 CA SER A 287 5570 4838 5420 -9 -184 374 C ATOM 2012 C SER A 287 80.908 -16.262 20.195 1.00 32.39 C ANISOU 2012 C SER A 287 4325 3713 4269 -31 -172 388 C ATOM 2013 O SER A 287 80.705 -15.722 21.301 1.00 28.33 O ANISOU 2013 O SER A 287 3759 3248 3757 -7 -168 384 O ATOM 2014 CB SER A 287 79.423 -15.928 18.199 1.00 37.24 C ANISOU 2014 CB SER A 287 5004 4303 4842 -13 -229 389 C ATOM 2015 OG SER A 287 79.477 -17.288 17.803 1.00 33.90 O ANISOU 2015 OG SER A 287 4583 3868 4429 -60 -236 408 O ATOM 2016 N PHE A 288 81.319 -17.517 20.059 1.00 35.98 N ANISOU 2016 N PHE A 288 4779 4152 4740 -76 -166 403 N ATOM 2017 CA PHE A 288 81.531 -18.373 21.212 1.00 34.51 C ANISOU 2017 CA PHE A 288 4529 4007 4576 -102 -155 417 C ATOM 2018 C PHE A 288 82.644 -17.802 22.086 1.00 37.51 C ANISOU 2018 C PHE A 288 4904 4375 4973 -91 -114 403 C ATOM 2019 O PHE A 288 82.588 -17.890 23.310 1.00 35.86 O ANISOU 2019 O PHE A 288 4632 4217 4775 -89 -108 408 O ATOM 2020 CB PHE A 288 81.870 -19.793 20.755 1.00 28.41 C ANISOU 2020 CB PHE A 288 3768 3210 3818 -154 -155 435 C ATOM 2021 CG PHE A 288 81.783 -20.820 21.843 1.00 33.43 C ANISOU 2021 CG PHE A 288 4332 3897 4473 -183 -155 454 C ATOM 2022 CD1 PHE A 288 80.565 -21.377 22.190 1.00 30.56 C ANISOU 2022 CD1 PHE A 288 3911 3597 4104 -188 -191 474 C ATOM 2023 CD2 PHE A 288 82.921 -21.240 22.509 1.00 31.01 C ANISOU 2023 CD2 PHE A 288 4017 3573 4191 -205 -119 453 C ATOM 2024 CE1 PHE A 288 80.482 -22.328 23.187 1.00 31.09 C ANISOU 2024 CE1 PHE A 288 3913 3712 4189 -216 -191 492 C ATOM 2025 CE2 PHE A 288 82.845 -22.194 23.505 1.00 37.66 C ANISOU 2025 CE2 PHE A 288 4795 4463 5053 -233 -119 471 C ATOM 2026 CZ PHE A 288 81.623 -22.737 23.846 1.00 26.64 C ANISOU 2026 CZ PHE A 288 3341 3131 3650 -238 -155 490 C ATOM 2027 N ALA A 289 83.646 -17.198 21.453 1.00 38.61 N ANISOU 2027 N ALA A 289 5109 4448 5114 -83 -87 384 N ATOM 2028 CA ALA A 289 84.666 -16.472 22.203 1.00 38.83 C ANISOU 2028 CA ALA A 289 5138 4461 5156 -66 -50 368 C ATOM 2029 C ALA A 289 84.091 -15.206 22.834 1.00 36.47 C ANISOU 2029 C ALA A 289 4812 4204 4843 -17 -58 355 C ATOM 2030 O ALA A 289 84.562 -14.756 23.878 1.00 38.86 O ANISOU 2030 O ALA A 289 5083 4525 5157 -2 -37 348 O ATOM 2031 CB ALA A 289 85.845 -16.124 21.308 1.00 34.94 C ANISOU 2031 CB ALA A 289 4723 3884 4667 -70 -20 353 C ATOM 2032 N TYR A 290 83.073 -14.637 22.195 1.00 34.36 N ANISOU 2032 N TYR A 290 4557 3949 4550 9 -90 352 N ATOM 2033 CA TYR A 290 82.481 -13.389 22.668 1.00 30.34 C ANISOU 2033 CA TYR A 290 4027 3475 4025 58 -100 339 C ATOM 2034 C TYR A 290 81.612 -13.608 23.893 1.00 33.05 C ANISOU 2034 C TYR A 290 4286 3903 4370 65 -118 352 C ATOM 2035 O TYR A 290 81.280 -12.658 24.606 1.00 33.81 O ANISOU 2035 O TYR A 290 4354 4035 4458 103 -120 341 O ATOM 2036 CB TYR A 290 81.662 -12.720 21.566 1.00 30.38 C ANISOU 2036 CB TYR A 290 4075 3467 4003 83 -129 332 C ATOM 2037 CG TYR A 290 82.157 -11.340 21.203 1.00 32.27 C ANISOU 2037 CG TYR A 290 4365 3665 4232 122 -114 307 C ATOM 2038 CD1 TYR A 290 81.914 -10.254 22.034 1.00 28.87 C ANISOU 2038 CD1 TYR A 290 3902 3271 3795 164 -113 294 C ATOM 2039 CD2 TYR A 290 82.873 -11.123 20.031 1.00 26.81 C ANISOU 2039 CD2 TYR A 290 3752 2898 3537 117 -100 297 C ATOM 2040 CE1 TYR A 290 82.367 -8.989 21.707 1.00 37.68 C ANISOU 2040 CE1 TYR A 290 5064 4349 4902 200 -100 272 C ATOM 2041 CE2 TYR A 290 83.329 -9.863 19.695 1.00 27.23 C ANISOU 2041 CE2 TYR A 290 3851 2915 3582 153 -86 274 C ATOM 2042 CZ TYR A 290 83.073 -8.800 20.535 1.00 38.87 C ANISOU 2042 CZ TYR A 290 5292 4425 5050 194 -86 262 C ATOM 2043 OH TYR A 290 83.527 -7.544 20.202 1.00 33.93 O ANISOU 2043 OH TYR A 290 4713 3763 4416 229 -73 240 O ATOM 2044 N ILE A 291 81.257 -14.864 24.148 1.00 32.43 N ANISOU 2044 N ILE A 291 4167 3854 4301 28 -130 374 N ATOM 2045 CA ILE A 291 80.492 -15.187 25.353 1.00 38.60 C ANISOU 2045 CA ILE A 291 4866 4715 5086 30 -144 388 C ATOM 2046 C ILE A 291 81.281 -14.816 26.627 1.00 41.90 C ANISOU 2046 C ILE A 291 5250 5150 5522 40 -112 379 C ATOM 2047 O ILE A 291 80.690 -14.566 27.684 1.00 39.47 O ANISOU 2047 O ILE A 291 4880 4906 5212 60 -121 383 O ATOM 2048 CB ILE A 291 80.093 -16.680 25.377 1.00 37.37 C ANISOU 2048 CB ILE A 291 4675 4583 4940 -16 -160 414 C ATOM 2049 CG1 ILE A 291 79.223 -17.010 24.165 1.00 24.69 C ANISOU 2049 CG1 ILE A 291 3100 2965 3317 -23 -195 423 C ATOM 2050 CG2 ILE A 291 79.325 -17.025 26.640 1.00 35.59 C ANISOU 2050 CG2 ILE A 291 4363 4439 4719 -14 -174 430 C ATOM 2051 CD1 ILE A 291 78.573 -18.375 24.237 1.00 37.29 C ANISOU 2051 CD1 ILE A 291 4653 4595 4919 -62 -219 450 C ATOM 2052 N ASN A 292 82.606 -14.739 26.514 1.00 27.86 N ANISOU 2052 N ASN A 292 3514 3314 3760 29 -76 368 N ATOM 2053 CA ASN A 292 83.462 -14.321 27.628 1.00 33.38 C ANISOU 2053 CA ASN A 292 4189 4018 4475 40 -44 358 C ATOM 2054 C ASN A 292 83.117 -12.923 28.129 1.00 35.85 C ANISOU 2054 C ASN A 292 4491 4357 4773 93 -47 340 C ATOM 2055 O ASN A 292 83.376 -12.586 29.284 1.00 49.32 O ANISOU 2055 O ASN A 292 6155 6095 6488 107 -32 336 O ATOM 2056 CB ASN A 292 84.936 -14.349 27.214 1.00 37.73 C ANISOU 2056 CB ASN A 292 4798 4493 5044 22 -6 347 C ATOM 2057 CG ASN A 292 85.657 -15.597 27.681 1.00 40.73 C ANISOU 2057 CG ASN A 292 5156 4868 5451 -25 13 361 C ATOM 2058 OD1 ASN A 292 85.568 -15.986 28.846 1.00 37.23 O ANISOU 2058 OD1 ASN A 292 4651 4476 5020 -32 16 370 O ATOM 2059 ND2 ASN A 292 86.388 -16.226 26.771 1.00 40.26 N ANISOU 2059 ND2 ASN A 292 5149 4748 5401 -57 26 363 N ATOM 2060 N CYS A 293 82.546 -12.112 27.246 1.00 33.46 N ANISOU 2060 N CYS A 293 4226 4039 4447 121 -66 330 N ATOM 2061 CA CYS A 293 82.205 -10.731 27.563 1.00 30.85 C ANISOU 2061 CA CYS A 293 3892 3727 4101 173 -71 312 C ATOM 2062 C CYS A 293 80.842 -10.581 28.235 1.00 36.32 C ANISOU 2062 C CYS A 293 4520 4501 4779 195 -103 321 C ATOM 2063 O CYS A 293 80.412 -9.462 28.519 1.00 43.69 O ANISOU 2063 O CYS A 293 5446 5457 5698 239 -111 307 O ATOM 2064 CB CYS A 293 82.247 -9.877 26.295 1.00 39.93 C ANISOU 2064 CB CYS A 293 5116 4823 5234 194 -76 296 C ATOM 2065 SG CYS A 293 83.850 -9.880 25.465 1.00 46.16 S ANISOU 2065 SG CYS A 293 5986 5515 6039 174 -37 283 S ATOM 2066 N CYS A 294 80.144 -11.690 28.458 1.00 27.31 N ANISOU 2066 N CYS A 294 3333 3403 3641 166 -123 344 N ATOM 2067 CA CYS A 294 78.846 -11.615 29.122 1.00 40.81 C ANISOU 2067 CA CYS A 294 4978 5191 5338 186 -153 354 C ATOM 2068 C CYS A 294 78.632 -12.692 30.183 1.00 38.97 C ANISOU 2068 C CYS A 294 4672 5013 5120 157 -153 376 C ATOM 2069 O CYS A 294 77.690 -12.602 30.969 1.00 49.38 O ANISOU 2069 O CYS A 294 5931 6400 6432 175 -172 384 O ATOM 2070 CB CYS A 294 77.717 -11.699 28.093 1.00 42.99 C ANISOU 2070 CB CYS A 294 5270 5473 5594 189 -191 362 C ATOM 2071 SG CYS A 294 77.397 -13.367 27.479 1.00 49.27 S ANISOU 2071 SG CYS A 294 6060 6265 6397 133 -209 390 S ATOM 2072 N ILE A 295 79.470 -13.724 30.192 1.00 35.83 N ANISOU 2072 N ILE A 295 4282 4587 4745 114 -133 386 N ATOM 2073 CA ILE A 295 79.288 -14.799 31.163 1.00 34.34 C ANISOU 2073 CA ILE A 295 4027 4449 4572 84 -134 407 C ATOM 2074 C ILE A 295 79.679 -14.394 32.594 1.00 35.38 C ANISOU 2074 C ILE A 295 4110 4618 4713 102 -112 401 C ATOM 2075 O ILE A 295 79.221 -15.011 33.559 1.00 34.51 O ANISOU 2075 O ILE A 295 3934 4568 4611 90 -119 417 O ATOM 2076 CB ILE A 295 80.081 -16.072 30.770 1.00 34.04 C ANISOU 2076 CB ILE A 295 4009 4370 4554 30 -120 419 C ATOM 2077 CG1 ILE A 295 79.527 -17.287 31.524 1.00 33.68 C ANISOU 2077 CG1 ILE A 295 3894 4383 4520 -2 -133 446 C ATOM 2078 CG2 ILE A 295 81.576 -15.882 30.999 1.00 23.42 C ANISOU 2078 CG2 ILE A 295 2697 2972 3229 23 -78 405 C ATOM 2079 CD1 ILE A 295 80.413 -18.504 31.505 1.00 41.93 C ANISOU 2079 CD1 ILE A 295 4945 5397 5589 -52 -114 457 C ATOM 2080 N ASN A 296 80.521 -13.370 32.736 1.00 30.12 N ANISOU 2080 N ASN A 296 3477 3917 4049 129 -87 378 N ATOM 2081 CA ASN A 296 80.947 -12.939 34.069 1.00 28.37 C ANISOU 2081 CA ASN A 296 3214 3728 3839 147 -66 371 C ATOM 2082 C ASN A 296 79.788 -12.520 34.993 1.00 33.08 C ANISOU 2082 C ASN A 296 3744 4405 4420 179 -88 376 C ATOM 2083 O ASN A 296 79.698 -13.020 36.120 1.00 34.04 O ANISOU 2083 O ASN A 296 3805 4577 4553 169 -83 387 O ATOM 2084 CB ASN A 296 81.972 -11.796 33.961 1.00 28.70 C ANISOU 2084 CB ASN A 296 3306 3716 3882 174 -38 345 C ATOM 2085 CG ASN A 296 83.374 -12.291 33.657 1.00 39.77 C ANISOU 2085 CG ASN A 296 4753 5051 5308 141 -5 341 C ATOM 2086 OD1 ASN A 296 83.662 -12.741 32.548 1.00 40.77 O ANISOU 2086 OD1 ASN A 296 4929 5126 5435 116 -5 343 O ATOM 2087 ND2 ASN A 296 84.260 -12.191 34.641 1.00 31.30 N ANISOU 2087 ND2 ASN A 296 3661 3977 4253 140 24 335 N ATOM 2088 N PRO A 297 78.888 -11.619 34.524 1.00 34.08 N ANISOU 2088 N PRO A 297 3880 4546 4522 217 -112 367 N ATOM 2089 CA PRO A 297 77.739 -11.305 35.386 1.00 29.67 C ANISOU 2089 CA PRO A 297 3256 4066 3950 245 -134 374 C ATOM 2090 C PRO A 297 76.893 -12.530 35.715 1.00 32.39 C ANISOU 2090 C PRO A 297 3542 4465 4298 214 -156 402 C ATOM 2091 O PRO A 297 76.379 -12.651 36.829 1.00 36.61 O ANISOU 2091 O PRO A 297 4011 5065 4834 223 -160 411 O ATOM 2092 CB PRO A 297 76.937 -10.302 34.549 1.00 39.70 C ANISOU 2092 CB PRO A 297 4557 5332 5194 284 -159 362 C ATOM 2093 CG PRO A 297 77.929 -9.701 33.629 1.00 42.77 C ANISOU 2093 CG PRO A 297 5025 5641 5584 288 -140 342 C ATOM 2094 CD PRO A 297 78.867 -10.814 33.291 1.00 39.77 C ANISOU 2094 CD PRO A 297 4668 5216 5227 237 -120 351 C ATOM 2095 N ILE A 298 76.785 -13.444 34.754 1.00 31.09 N ANISOU 2095 N ILE A 298 3403 4273 4137 178 -168 416 N ATOM 2096 CA ILE A 298 76.007 -14.655 34.949 1.00 29.69 C ANISOU 2096 CA ILE A 298 3176 4142 3964 145 -190 443 C ATOM 2097 C ILE A 298 76.613 -15.485 36.069 1.00 37.91 C ANISOU 2097 C ILE A 298 4170 5206 5028 116 -168 455 C ATOM 2098 O ILE A 298 75.903 -16.008 36.932 1.00 40.64 O ANISOU 2098 O ILE A 298 4449 5617 5376 111 -180 472 O ATOM 2099 CB ILE A 298 75.945 -15.494 33.660 1.00 32.06 C ANISOU 2099 CB ILE A 298 3519 4398 4265 109 -205 454 C ATOM 2100 CG1 ILE A 298 75.248 -14.709 32.546 1.00 40.46 C ANISOU 2100 CG1 ILE A 298 4626 5442 5305 137 -229 444 C ATOM 2101 CG2 ILE A 298 75.243 -16.818 33.912 1.00 36.81 C ANISOU 2101 CG2 ILE A 298 4067 5044 4874 72 -225 483 C ATOM 2102 CD1 ILE A 298 75.153 -15.465 31.241 1.00 28.74 C ANISOU 2102 CD1 ILE A 298 3187 3913 3819 105 -245 454 C ATOM 2103 N ILE A 299 77.938 -15.559 36.067 1.00 37.24 N ANISOU 2103 N ILE A 299 4122 5067 4961 100 -135 444 N ATOM 2104 CA ILE A 299 78.664 -16.295 37.085 1.00 36.07 C ANISOU 2104 CA ILE A 299 3937 4932 4836 72 -111 452 C ATOM 2105 C ILE A 299 78.465 -15.646 38.447 1.00 47.66 C ANISOU 2105 C ILE A 299 5350 6457 6302 105 -104 447 C ATOM 2106 O ILE A 299 78.236 -16.335 39.444 1.00 41.71 O ANISOU 2106 O ILE A 299 4535 5756 5558 89 -104 464 O ATOM 2107 CB ILE A 299 80.170 -16.366 36.757 1.00 32.90 C ANISOU 2107 CB ILE A 299 3591 4455 4453 51 -76 440 C ATOM 2108 CG1 ILE A 299 80.408 -17.270 35.545 1.00 31.30 C ANISOU 2108 CG1 ILE A 299 3435 4202 4257 11 -81 449 C ATOM 2109 CG2 ILE A 299 80.970 -16.855 37.957 1.00 27.97 C ANISOU 2109 CG2 ILE A 299 2929 3847 3853 33 -49 444 C ATOM 2110 CD1 ILE A 299 81.859 -17.388 35.150 1.00 35.69 C ANISOU 2110 CD1 ILE A 299 4047 4682 4832 -11 -47 437 C ATOM 2111 N TYR A 300 78.518 -14.317 38.480 1.00 43.28 N ANISOU 2111 N TYR A 300 4816 5894 5733 151 -98 425 N ATOM 2112 CA TYR A 300 78.382 -13.603 39.744 1.00 34.48 C ANISOU 2112 CA TYR A 300 3655 4829 4616 186 -91 417 C ATOM 2113 C TYR A 300 77.000 -13.816 40.349 1.00 43.43 C ANISOU 2113 C TYR A 300 4719 6046 5736 198 -120 435 C ATOM 2114 O TYR A 300 76.860 -14.015 41.561 1.00 49.70 O ANISOU 2114 O TYR A 300 5453 6893 6536 200 -114 443 O ATOM 2115 CB TYR A 300 78.631 -12.106 39.550 1.00 36.74 C ANISOU 2115 CB TYR A 300 3981 5089 4888 235 -83 390 C ATOM 2116 CG TYR A 300 79.966 -11.759 38.933 1.00 35.12 C ANISOU 2116 CG TYR A 300 3846 4802 4695 228 -55 372 C ATOM 2117 CD1 TYR A 300 81.070 -12.587 39.093 1.00 29.68 C ANISOU 2117 CD1 TYR A 300 3168 4078 4032 188 -28 376 C ATOM 2118 CD2 TYR A 300 80.121 -10.597 38.189 1.00 25.14 C ANISOU 2118 CD2 TYR A 300 2638 3497 3417 262 -54 349 C ATOM 2119 CE1 TYR A 300 82.290 -12.265 38.527 1.00 27.28 C ANISOU 2119 CE1 TYR A 300 2928 3699 3739 182 -2 360 C ATOM 2120 CE2 TYR A 300 81.333 -10.268 37.621 1.00 33.77 C ANISOU 2120 CE2 TYR A 300 3795 4516 4521 257 -28 333 C ATOM 2121 CZ TYR A 300 82.415 -11.103 37.792 1.00 22.67 C ANISOU 2121 CZ TYR A 300 2398 3075 3141 217 -2 339 C ATOM 2122 OH TYR A 300 83.624 -10.773 37.225 1.00 27.86 O ANISOU 2122 OH TYR A 300 3118 3658 3810 212 25 323 O ATOM 2123 N VAL A 301 75.981 -13.800 39.495 1.00 45.59 N ANISOU 2123 N VAL A 301 5001 6329 5993 204 -151 442 N ATOM 2124 CA VAL A 301 74.613 -13.985 39.962 1.00 41.38 C ANISOU 2124 CA VAL A 301 4405 5872 5447 216 -181 459 C ATOM 2125 C VAL A 301 74.371 -15.423 40.410 1.00 37.85 C ANISOU 2125 C VAL A 301 3907 5460 5015 170 -187 487 C ATOM 2126 O VAL A 301 73.710 -15.663 41.426 1.00 47.56 O ANISOU 2126 O VAL A 301 5068 6758 6244 176 -194 501 O ATOM 2127 CB VAL A 301 73.593 -13.603 38.874 1.00 41.75 C ANISOU 2127 CB VAL A 301 4475 5916 5471 233 -214 459 C ATOM 2128 CG1 VAL A 301 72.176 -13.888 39.346 1.00 63.07 C ANISOU 2128 CG1 VAL A 301 7108 8694 8160 242 -245 478 C ATOM 2129 CG2 VAL A 301 73.745 -12.138 38.510 1.00 41.93 C ANISOU 2129 CG2 VAL A 301 4542 5910 5478 281 -210 431 C ATOM 2130 N VAL A 302 74.923 -16.379 39.667 1.00 35.81 N ANISOU 2130 N VAL A 302 3681 5155 4770 126 -183 496 N ATOM 2131 CA VAL A 302 74.756 -17.781 40.029 1.00 34.52 C ANISOU 2131 CA VAL A 302 3473 5020 4622 80 -188 523 C ATOM 2132 C VAL A 302 75.434 -18.086 41.360 1.00 47.53 C ANISOU 2132 C VAL A 302 5077 6693 6288 70 -162 525 C ATOM 2133 O VAL A 302 74.874 -18.785 42.206 1.00 50.91 O ANISOU 2133 O VAL A 302 5441 7181 6721 57 -170 546 O ATOM 2134 CB VAL A 302 75.317 -18.721 38.941 1.00 33.72 C ANISOU 2134 CB VAL A 302 3421 4858 4533 34 -187 530 C ATOM 2135 CG1 VAL A 302 75.454 -20.139 39.474 1.00 36.04 C ANISOU 2135 CG1 VAL A 302 3672 5174 4848 -14 -185 554 C ATOM 2136 CG2 VAL A 302 74.423 -18.700 37.712 1.00 30.87 C ANISOU 2136 CG2 VAL A 302 3089 4485 4155 37 -220 534 C ATOM 2137 N ALA A 303 76.632 -17.544 41.553 1.00 48.88 N ANISOU 2137 N ALA A 303 5284 6818 6469 77 -129 505 N ATOM 2138 CA ALA A 303 77.340 -17.743 42.809 1.00 41.77 C ANISOU 2138 CA ALA A 303 4347 5938 5586 70 -103 505 C ATOM 2139 C ALA A 303 76.623 -17.049 43.965 1.00 53.61 C ANISOU 2139 C ALA A 303 5788 7508 7072 111 -108 504 C ATOM 2140 O ALA A 303 76.553 -17.582 45.079 1.00 57.09 O ANISOU 2140 O ALA A 303 6171 7998 7524 100 -103 517 O ATOM 2141 CB ALA A 303 78.770 -17.244 42.694 1.00 49.72 C ANISOU 2141 CB ALA A 303 5409 6876 6605 71 -69 483 C ATOM 2142 N GLY A 304 76.064 -15.873 43.688 1.00 50.25 N ANISOU 2142 N GLY A 304 5378 7089 6625 157 -120 488 N ATOM 2143 CA GLY A 304 75.396 -15.110 44.726 1.00 58.28 C ANISOU 2143 CA GLY A 304 6345 8171 7630 200 -125 484 C ATOM 2144 C GLY A 304 74.115 -15.770 45.190 1.00 67.54 C ANISOU 2144 C GLY A 304 7449 9419 8795 194 -152 510 C ATOM 2145 O GLY A 304 73.781 -15.730 46.375 1.00 74.77 O ANISOU 2145 O GLY A 304 8305 10394 9710 208 -149 516 O ATOM 2146 N GLN A 305 73.391 -16.376 44.253 1.00 71.86 N ANISOU 2146 N GLN A 305 8004 9964 9338 174 -179 525 N ATOM 2147 CA GLN A 305 72.256 -17.221 44.604 1.00 66.32 C ANISOU 2147 CA GLN A 305 7237 9327 8633 158 -205 553 C ATOM 2148 C GLN A 305 72.713 -18.503 45.292 1.00 73.99 C ANISOU 2148 C GLN A 305 8172 10314 9628 112 -192 573 C ATOM 2149 O GLN A 305 72.005 -19.052 46.139 1.00 88.14 O ANISOU 2149 O GLN A 305 9896 12172 11421 106 -202 593 O ATOM 2150 CB GLN A 305 71.435 -17.565 43.360 1.00 68.67 C ANISOU 2150 CB GLN A 305 7557 9612 8920 147 -237 563 C ATOM 2151 CG GLN A 305 70.630 -16.408 42.797 1.00 81.67 C ANISOU 2151 CG GLN A 305 9225 11265 10543 193 -257 549 C ATOM 2152 CD GLN A 305 69.861 -16.791 41.546 1.00 93.93 C ANISOU 2152 CD GLN A 305 10802 12801 12087 179 -289 560 C ATOM 2153 OE1 GLN A 305 70.083 -17.855 40.967 1.00 96.42 O ANISOU 2153 OE1 GLN A 305 11131 13090 12415 135 -293 575 O ATOM 2154 NE2 GLN A 305 68.948 -15.923 41.123 1.00 93.80 N ANISOU 2154 NE2 GLN A 305 10790 12801 12049 218 -312 553 N ATOM 2155 N GLY A 306 73.902 -18.972 44.927 1.00 80.21 N ANISOU 2155 N GLY A 306 9003 11040 10434 79 -170 567 N ATOM 2156 CA GLY A 306 74.400 -20.242 45.421 1.00 88.65 C ANISOU 2156 CA GLY A 306 10043 12113 11525 31 -159 586 C ATOM 2157 C GLY A 306 74.773 -20.198 46.888 1.00 86.63 C ANISOU 2157 C GLY A 306 9737 11898 11279 38 -137 586 C ATOM 2158 O GLY A 306 74.565 -21.169 47.618 1.00 86.88 O ANISOU 2158 O GLY A 306 9715 11972 11322 10 -139 608 O ATOM 2159 N PHE A 307 75.318 -19.065 47.323 1.00 87.25 N ANISOU 2159 N PHE A 307 9834 11964 11352 76 -117 562 N ATOM 2160 CA PHE A 307 75.580 -18.853 48.745 1.00 89.52 C ANISOU 2160 CA PHE A 307 10074 12294 11645 90 -98 560 C ATOM 2161 C PHE A 307 74.259 -18.638 49.477 1.00 96.67 C ANISOU 2161 C PHE A 307 10913 13283 12533 119 -120 572 C ATOM 2162 O PHE A 307 74.178 -18.784 50.699 1.00106.07 O ANISOU 2162 O PHE A 307 12096 14489 13719 119 -108 560 O ATOM 2163 CB PHE A 307 76.507 -17.655 48.962 1.00 88.29 C ANISOU 2163 CB PHE A 307 9958 12100 11488 125 -72 530 C ATOM 2164 CG PHE A 307 77.725 -17.664 48.086 1.00 73.38 C ANISOU 2164 CG PHE A 307 8142 10126 9614 104 -52 516 C ATOM 2165 CD1 PHE A 307 78.405 -18.842 47.824 1.00 66.92 C ANISOU 2165 CD1 PHE A 307 7334 9275 8818 52 -42 529 C ATOM 2166 CD2 PHE A 307 78.183 -16.490 47.514 1.00 62.53 C ANISOU 2166 CD2 PHE A 307 6824 8703 8230 138 -43 489 C ATOM 2167 CE1 PHE A 307 79.523 -18.846 47.009 1.00 74.04 C ANISOU 2167 CE1 PHE A 307 8303 10098 9733 33 -24 515 C ATOM 2168 CE2 PHE A 307 79.297 -16.488 46.700 1.00 71.45 C ANISOU 2168 CE2 PHE A 307 8021 9754 9373 119 -24 476 C ATOM 2169 CZ PHE A 307 79.968 -17.667 46.446 1.00 72.97 C ANISOU 2169 CZ PHE A 307 8223 9915 9588 67 -14 489 C ATOM 2170 N GLN A 308 73.235 -18.285 48.703 1.00100.29 N ANISOU 2170 N GLN A 308 11379 13754 12973 138 -148 574 N ATOM 2171 CA GLN A 308 71.913 -17.927 49.216 1.00 97.38 C ANISOU 2171 CA GLN A 308 10971 13446 12582 168 -169 577 C ATOM 2172 C GLN A 308 72.000 -16.704 50.126 1.00 95.35 C ANISOU 2172 C GLN A 308 10716 13202 12312 216 -154 551 C ATOM 2173 O GLN A 308 71.699 -16.777 51.317 1.00 97.02 O ANISOU 2173 O GLN A 308 10921 13429 12515 218 -144 538 O ATOM 2174 CB GLN A 308 71.267 -19.103 49.961 1.00107.68 C ANISOU 2174 CB GLN A 308 12265 14764 13884 133 -173 582 C ATOM 2175 CG GLN A 308 71.092 -20.370 49.130 1.00 95.62 C ANISOU 2175 CG GLN A 308 10739 13225 12369 85 -189 607 C ATOM 2176 CD GLN A 308 70.084 -21.328 49.742 1.00119.90 C ANISOU 2176 CD GLN A 308 13800 16322 15434 64 -200 612 C ATOM 2177 OE1 GLN A 308 69.325 -20.956 50.636 1.00121.34 O ANISOU 2177 OE1 GLN A 308 13970 16533 15600 88 -200 601 O ATOM 2178 NE2 GLN A 308 70.071 -22.568 49.260 1.00108.70 N ANISOU 2178 NE2 GLN A 308 12385 14889 14027 19 -209 630 N ATOM 2179 N LYS A 313 67.060 -10.719 47.786 1.00 84.14 N ANISOU 2179 N LYS A 313 9314 11891 10764 480 -273 498 N ATOM 2180 CA LYS A 313 68.041 -9.649 47.631 1.00 83.36 C ANISOU 2180 CA LYS A 313 9271 11739 10663 506 -251 468 C ATOM 2181 C LYS A 313 68.051 -9.077 46.216 1.00 77.10 C ANISOU 2181 C LYS A 313 8547 10886 9860 515 -264 453 C ATOM 2182 O LYS A 313 67.889 -9.807 45.239 1.00 76.04 O ANISOU 2182 O LYS A 313 8437 10725 9731 482 -279 465 O ATOM 2183 CB LYS A 313 69.441 -10.149 47.987 1.00 85.70 C ANISOU 2183 CB LYS A 313 9587 11992 10981 474 -218 464 C ATOM 2184 CG LYS A 313 69.661 -10.398 49.466 1.00 84.20 C ANISOU 2184 CG LYS A 313 9339 11852 10800 475 -200 470 C ATOM 2185 CD LYS A 313 71.117 -10.724 49.751 1.00 92.49 C ANISOU 2185 CD LYS A 313 10417 12854 11872 448 -166 463 C ATOM 2186 CE LYS A 313 71.360 -10.898 51.240 1.00 96.72 C ANISOU 2186 CE LYS A 313 10916 13420 12414 446 -146 461 C ATOM 2187 NZ LYS A 313 72.789 -11.177 51.551 1.00101.80 N ANISOU 2187 NZ LYS A 313 11572 14028 13080 426 -115 457 N ATOM 2188 N SER A 314 68.254 -7.766 46.118 1.00 66.58 N ANISOU 2188 N SER A 314 7249 9534 8515 559 -259 427 N ATOM 2189 CA SER A 314 68.329 -7.086 44.827 1.00 64.30 C ANISOU 2189 CA SER A 314 7028 9188 8216 572 -270 410 C ATOM 2190 C SER A 314 69.575 -7.498 44.049 1.00 70.33 C ANISOU 2190 C SER A 314 7855 9871 8996 536 -250 403 C ATOM 2191 O SER A 314 70.576 -7.904 44.635 1.00 77.53 O ANISOU 2191 O SER A 314 8765 10766 9925 514 -222 403 O ATOM 2192 CB SER A 314 68.305 -5.567 45.018 1.00 58.55 C ANISOU 2192 CB SER A 314 6318 8459 7471 629 -267 383 C ATOM 2193 OG SER A 314 68.861 -5.195 46.267 1.00 75.59 O ANISOU 2193 OG SER A 314 8448 10640 9634 647 -243 374 O ATOM 2194 N LEU A 315 69.493 -7.416 42.724 1.00 68.08 N ANISOU 2194 N LEU A 315 7626 9538 8705 528 -264 399 N ATOM 2195 CA LEU A 315 70.619 -7.761 41.861 1.00 65.45 C ANISOU 2195 CA LEU A 315 7357 9126 8386 496 -246 392 C ATOM 2196 C LEU A 315 71.896 -6.966 42.200 1.00 64.67 C ANISOU 2196 C LEU A 315 7295 8982 8294 513 -213 367 C ATOM 2197 O LEU A 315 72.966 -7.570 42.373 1.00 64.92 O ANISOU 2197 O LEU A 315 7341 8978 8346 480 -188 369 O ATOM 2198 CB LEU A 315 70.223 -7.557 40.393 1.00 70.00 C ANISOU 2198 CB LEU A 315 7988 9659 8950 496 -269 388 C ATOM 2199 CG LEU A 315 71.177 -8.021 39.296 1.00 74.64 C ANISOU 2199 CG LEU A 315 8644 10167 9549 460 -257 385 C ATOM 2200 CD1 LEU A 315 71.431 -9.511 39.412 1.00 82.07 C ANISOU 2200 CD1 LEU A 315 9562 11110 10510 406 -252 409 C ATOM 2201 CD2 LEU A 315 70.589 -7.679 37.940 1.00 91.63 C ANISOU 2201 CD2 LEU A 315 10843 12287 11684 469 -283 381 C ATOM 2202 N PRO A 316 71.800 -5.617 42.312 1.00 59.92 N ANISOU 2202 N PRO A 316 6709 8381 7678 563 -213 345 N ATOM 2203 CA PRO A 316 72.997 -4.889 42.749 1.00 65.88 C ANISOU 2203 CA PRO A 316 7493 9097 8440 579 -182 322 C ATOM 2204 C PRO A 316 73.489 -5.339 44.119 1.00 63.77 C ANISOU 2204 C PRO A 316 7176 8866 8189 569 -160 329 C ATOM 2205 O PRO A 316 74.689 -5.316 44.366 1.00 60.34 O ANISOU 2205 O PRO A 316 6767 8389 7771 558 -131 319 O ATOM 2206 CB PRO A 316 72.529 -3.428 42.786 1.00 47.52 C ANISOU 2206 CB PRO A 316 5177 6784 6093 637 -192 301 C ATOM 2207 CG PRO A 316 71.059 -3.502 42.907 1.00 47.77 C ANISOU 2207 CG PRO A 316 5159 6883 6109 653 -224 315 C ATOM 2208 CD PRO A 316 70.666 -4.700 42.110 1.00 62.00 C ANISOU 2208 CD PRO A 316 6963 8678 7916 607 -241 338 C ATOM 2209 N GLU A 317 72.565 -5.729 44.994 1.00 63.58 N ANISOU 2209 N GLU A 317 7081 8916 8160 573 -173 346 N ATOM 2210 CA GLU A 317 72.918 -6.178 46.336 1.00 56.14 C ANISOU 2210 CA GLU A 317 6086 8013 7230 564 -154 354 C ATOM 2211 C GLU A 317 73.740 -7.460 46.295 1.00 50.35 C ANISOU 2211 C GLU A 317 5357 7251 6522 507 -137 370 C ATOM 2212 O GLU A 317 74.753 -7.593 46.995 1.00 39.99 O ANISOU 2212 O GLU A 317 4044 5923 5227 497 -109 365 O ATOM 2213 CB GLU A 317 71.650 -6.398 47.168 1.00 73.35 C ANISOU 2213 CB GLU A 317 8190 10280 9399 578 -174 372 C ATOM 2214 CG GLU A 317 71.893 -6.858 48.595 1.00 86.79 C ANISOU 2214 CG GLU A 317 9834 12030 11113 571 -157 382 C ATOM 2215 CD GLU A 317 72.287 -5.720 49.511 1.00116.86 C ANISOU 2215 CD GLU A 317 13637 15849 14915 616 -140 360 C ATOM 2216 OE1 GLU A 317 72.265 -4.556 49.058 1.00114.17 O ANISOU 2216 OE1 GLU A 317 13335 15485 14561 655 -144 338 O ATOM 2217 OE2 GLU A 317 72.615 -5.988 50.685 1.00127.85 O ANISOU 2217 OE2 GLU A 317 14988 17273 16317 613 -123 364 O ATOM 2218 N LEU A 318 73.304 -8.389 45.453 1.00 47.33 N ANISOU 2218 N LEU A 318 4980 6860 6142 472 -154 388 N ATOM 2219 CA LEU A 318 73.983 -9.663 45.294 1.00 53.20 C ANISOU 2219 CA LEU A 318 5729 7577 6908 417 -142 404 C ATOM 2220 C LEU A 318 75.364 -9.438 44.701 1.00 47.84 C ANISOU 2220 C LEU A 318 5120 6816 6243 404 -116 386 C ATOM 2221 O LEU A 318 76.359 -10.012 45.164 1.00 46.89 O ANISOU 2221 O LEU A 318 5000 6674 6144 376 -90 388 O ATOM 2222 CB LEU A 318 73.162 -10.596 44.403 1.00 48.51 C ANISOU 2222 CB LEU A 318 5132 6989 6312 385 -169 426 C ATOM 2223 CG LEU A 318 73.384 -12.098 44.572 1.00 69.86 C ANISOU 2223 CG LEU A 318 7809 9698 9035 330 -166 450 C ATOM 2224 CD1 LEU A 318 73.177 -12.492 46.023 1.00 71.22 C ANISOU 2224 CD1 LEU A 318 7908 9938 9215 329 -158 463 C ATOM 2225 CD2 LEU A 318 72.451 -12.884 43.662 1.00 69.74 C ANISOU 2225 CD2 LEU A 318 7791 9692 9014 306 -197 471 C ATOM 2226 N LEU A 319 75.428 -8.572 43.694 1.00 41.27 N ANISOU 2226 N LEU A 319 4346 5936 5398 427 -121 368 N ATOM 2227 CA LEU A 319 76.709 -8.277 43.075 1.00 47.38 C ANISOU 2227 CA LEU A 319 5187 6630 6184 418 -97 350 C ATOM 2228 C LEU A 319 77.647 -7.585 44.057 1.00 45.89 C ANISOU 2228 C LEU A 319 4997 6434 6004 439 -68 333 C ATOM 2229 O LEU A 319 78.853 -7.808 44.028 1.00 51.40 O ANISOU 2229 O LEU A 319 5727 7081 6723 417 -41 327 O ATOM 2230 CB LEU A 319 76.520 -7.415 41.830 1.00 44.88 C ANISOU 2230 CB LEU A 319 4932 6269 5851 441 -110 334 C ATOM 2231 CG LEU A 319 75.713 -8.050 40.697 1.00 32.22 C ANISOU 2231 CG LEU A 319 3343 4660 4239 419 -138 349 C ATOM 2232 CD1 LEU A 319 75.735 -7.154 39.473 1.00 52.96 C ANISOU 2232 CD1 LEU A 319 6038 7234 6851 441 -146 331 C ATOM 2233 CD2 LEU A 319 76.244 -9.435 40.366 1.00 40.50 C ANISOU 2233 CD2 LEU A 319 4398 5682 5307 362 -130 367 C ATOM 2234 N ARG A 320 77.094 -6.752 44.932 1.00 42.11 N ANISOU 2234 N ARG A 320 4480 6008 5512 483 -73 325 N ATOM 2235 CA ARG A 320 77.909 -6.061 45.923 1.00 47.29 C ANISOU 2235 CA ARG A 320 5132 6662 6176 506 -48 309 C ATOM 2236 C ARG A 320 78.444 -7.023 46.972 1.00 51.06 C ANISOU 2236 C ARG A 320 5565 7160 6674 474 -29 323 C ATOM 2237 O ARG A 320 79.578 -6.878 47.424 1.00 60.03 O ANISOU 2237 O ARG A 320 6718 8263 7827 469 -1 312 O ATOM 2238 CB ARG A 320 77.119 -4.932 46.595 1.00 65.46 C ANISOU 2238 CB ARG A 320 7401 9014 8455 562 -60 297 C ATOM 2239 CG ARG A 320 76.988 -3.687 45.736 1.00 87.01 C ANISOU 2239 CG ARG A 320 10183 11709 11167 601 -70 275 C ATOM 2240 CD ARG A 320 76.208 -2.574 46.412 1.00105.14 C ANISOU 2240 CD ARG A 320 12448 14057 13442 656 -83 263 C ATOM 2241 NE ARG A 320 75.961 -1.474 45.481 1.00 92.24 N ANISOU 2241 NE ARG A 320 10865 12393 11792 691 -96 244 N ATOM 2242 CZ ARG A 320 75.308 -0.358 45.789 1.00101.91 C ANISOU 2242 CZ ARG A 320 12076 13649 12995 742 -109 230 C ATOM 2243 NH1 ARG A 320 75.133 0.585 44.872 1.00 87.35 N ANISOU 2243 NH1 ARG A 320 10280 11771 11136 769 -121 214 N ATOM 2244 NH2 ARG A 320 74.829 -0.179 47.013 1.00109.34 N ANISOU 2244 NH2 ARG A 320 12957 14656 13931 765 -110 233 N ATOM 2245 N GLU A 321 77.643 -8.010 47.361 1.00 51.48 N ANISOU 2245 N GLU A 321 5563 7270 6728 450 -44 348 N ATOM 2246 CA GLU A 321 78.151 -8.999 48.301 1.00 45.34 C ANISOU 2246 CA GLU A 321 4745 6512 5972 416 -26 362 C ATOM 2247 C GLU A 321 79.223 -9.873 47.658 1.00 62.24 C ANISOU 2247 C GLU A 321 6927 8586 8135 367 -8 367 C ATOM 2248 O GLU A 321 80.210 -10.225 48.302 1.00 78.11 O ANISOU 2248 O GLU A 321 8933 10580 10166 347 17 366 O ATOM 2249 CB GLU A 321 77.030 -9.881 48.844 1.00 56.04 C ANISOU 2249 CB GLU A 321 6029 7941 7321 402 -47 389 C ATOM 2250 CG GLU A 321 77.498 -10.798 49.961 1.00 69.44 C ANISOU 2250 CG GLU A 321 7680 9666 9039 372 -29 403 C ATOM 2251 CD GLU A 321 76.678 -12.064 50.063 1.00 98.63 C ANISOU 2251 CD GLU A 321 11326 13410 12738 336 -47 433 C ATOM 2252 OE1 GLU A 321 75.717 -12.211 49.280 1.00 97.59 O ANISOU 2252 OE1 GLU A 321 11195 13292 12593 336 -74 443 O ATOM 2253 OE2 GLU A 321 76.998 -12.914 50.921 1.00105.68 O ANISOU 2253 OE2 GLU A 321 12180 14327 13648 308 -35 448 O ATOM 2254 N VAL A 322 79.046 -10.199 46.381 1.00 51.83 N ANISOU 2254 N VAL A 322 5649 7230 6813 347 -21 371 N ATOM 2255 CA VAL A 322 79.965 -11.128 45.726 1.00 45.08 C ANISOU 2255 CA VAL A 322 4832 6317 5980 298 -7 377 C ATOM 2256 C VAL A 322 81.285 -10.479 45.292 1.00 47.14 C ANISOU 2256 C VAL A 322 5159 6500 6252 303 21 354 C ATOM 2257 O VAL A 322 82.350 -11.091 45.396 1.00 40.10 O ANISOU 2257 O VAL A 322 4283 5569 5383 269 45 356 O ATOM 2258 CB VAL A 322 79.293 -11.789 44.503 1.00 41.56 C ANISOU 2258 CB VAL A 322 4406 5858 5527 273 -31 391 C ATOM 2259 CG1 VAL A 322 80.293 -12.610 43.710 1.00 55.34 C ANISOU 2259 CG1 VAL A 322 6199 7535 7292 227 -15 394 C ATOM 2260 CG2 VAL A 322 78.137 -12.665 44.954 1.00 52.09 C ANISOU 2260 CG2 VAL A 322 5672 7263 6855 258 -56 417 C ATOM 2261 N LEU A 323 81.221 -9.235 44.831 1.00 39.32 N ANISOU 2261 N LEU A 323 4207 5487 5245 345 17 333 N ATOM 2262 CA LEU A 323 82.378 -8.603 44.202 1.00 36.16 C ANISOU 2262 CA LEU A 323 3876 5010 4854 349 40 312 C ATOM 2263 C LEU A 323 83.145 -7.608 45.080 1.00 42.18 C ANISOU 2263 C LEU A 323 4640 5764 5621 383 62 292 C ATOM 2264 O LEU A 323 84.161 -7.064 44.647 1.00 44.95 O ANISOU 2264 O LEU A 323 5046 6051 5981 387 82 274 O ATOM 2265 CB LEU A 323 81.938 -7.897 42.918 1.00 30.51 C ANISOU 2265 CB LEU A 323 3212 4261 4119 370 22 301 C ATOM 2266 CG LEU A 323 81.116 -8.734 41.934 1.00 33.77 C ANISOU 2266 CG LEU A 323 3630 4678 4524 343 -4 319 C ATOM 2267 CD1 LEU A 323 80.594 -7.859 40.809 1.00 36.49 C ANISOU 2267 CD1 LEU A 323 4021 4997 4846 372 -23 307 C ATOM 2268 CD2 LEU A 323 81.923 -9.899 41.380 1.00 30.33 C ANISOU 2268 CD2 LEU A 323 3220 4194 4110 288 11 331 C ATOM 2269 N THR A 324 82.674 -7.361 46.298 1.00 40.75 N ANISOU 2269 N THR A 324 4401 5647 5435 406 59 294 N ATOM 2270 CA THR A 324 83.345 -6.396 47.169 1.00 40.19 C ANISOU 2270 CA THR A 324 4330 5571 5368 440 79 274 C ATOM 2271 C THR A 324 83.775 -6.997 48.500 1.00 32.09 C ANISOU 2271 C THR A 324 3254 4580 4361 424 96 283 C ATOM 2272 O THR A 324 83.915 -6.285 49.495 1.00 42.17 O ANISOU 2272 O THR A 324 4507 5881 5634 456 104 272 O ATOM 2273 CB THR A 324 82.457 -5.175 47.456 1.00 37.72 C ANISOU 2273 CB THR A 324 4002 5301 5029 497 60 261 C ATOM 2274 OG1 THR A 324 81.230 -5.605 48.057 1.00 49.57 O ANISOU 2274 OG1 THR A 324 5438 6881 6517 501 38 279 O ATOM 2275 CG2 THR A 324 82.157 -4.424 46.173 1.00 53.14 C ANISOU 2275 CG2 THR A 324 6010 7215 6965 517 46 249 C ATOM 2276 N GLU A 325 83.968 -8.311 48.514 1.00 42.45 N ANISOU 2276 N GLU A 325 4548 5893 5689 374 100 304 N ATOM 2277 CA GLU A 325 84.446 -8.998 49.704 1.00 31.68 C ANISOU 2277 CA GLU A 325 3139 4555 4344 352 117 314 C ATOM 2278 C GLU A 325 85.846 -8.519 50.077 1.00 28.19 C ANISOU 2278 C GLU A 325 2729 4060 3922 356 148 296 C ATOM 2279 O GLU A 325 86.699 -8.328 49.208 1.00 28.60 O ANISOU 2279 O GLU A 325 2841 4040 3983 346 162 285 O ATOM 2280 CB GLU A 325 84.445 -10.512 49.482 1.00 25.76 C ANISOU 2280 CB GLU A 325 2371 3806 3609 296 115 338 C ATOM 2281 CG GLU A 325 84.779 -11.323 50.721 1.00 59.80 C ANISOU 2281 CG GLU A 325 6630 8153 7939 272 129 352 C ATOM 2282 CD GLU A 325 85.196 -12.742 50.393 1.00 58.06 C ANISOU 2282 CD GLU A 325 6410 7912 7740 212 135 371 C ATOM 2283 OE1 GLU A 325 84.339 -13.648 50.465 1.00 67.90 O ANISOU 2283 OE1 GLU A 325 7612 9204 8982 190 116 393 O ATOM 2284 OE2 GLU A 325 86.383 -12.954 50.065 1.00 53.18 O ANISOU 2284 OE2 GLU A 325 5833 7230 7143 188 158 364 O ATOM 2285 N GLU A 326 86.075 -8.331 51.374 1.00 45.38 N ANISOU 2285 N GLU A 326 4866 6272 6105 370 160 293 N ATOM 2286 CA GLU A 326 87.374 -7.903 51.882 1.00 38.41 C ANISOU 2286 CA GLU A 326 4007 5345 5242 374 189 278 C ATOM 2287 C GLU A 326 88.168 -9.102 52.396 1.00 38.23 C ANISOU 2287 C GLU A 326 3965 5312 5247 325 208 292 C ATOM 2288 O GLU A 326 87.728 -9.796 53.313 1.00 59.24 O ANISOU 2288 O GLU A 326 6567 8030 7910 312 204 308 O ATOM 2289 CB GLU A 326 87.197 -6.866 52.994 1.00 41.05 C ANISOU 2289 CB GLU A 326 4312 5720 5566 423 190 264 C ATOM 2290 CG GLU A 326 86.330 -5.676 52.604 1.00 61.23 C ANISOU 2290 CG GLU A 326 6880 8293 8093 475 169 250 C ATOM 2291 CD GLU A 326 86.140 -4.687 53.741 1.00 90.51 C ANISOU 2291 CD GLU A 326 10557 12043 11790 523 170 237 C ATOM 2292 OE1 GLU A 326 86.181 -5.106 54.917 1.00 66.75 O ANISOU 2292 OE1 GLU A 326 7498 9076 8788 517 177 245 O ATOM 2293 OE2 GLU A 326 85.952 -3.485 53.456 1.00 96.73 O ANISOU 2293 OE2 GLU A 326 11371 12820 12560 567 163 218 O ATOM 2294 N SER A 327 89.328 -9.352 51.796 1.00 28.80 N ANISOU 2294 N SER A 327 2821 4045 4075 297 229 287 N ATOM 2295 CA SER A 327 90.140 -10.510 52.163 1.00 31.09 C ANISOU 2295 CA SER A 327 3100 4319 4394 248 248 300 C ATOM 2296 C SER A 327 91.090 -10.252 53.333 1.00 30.66 C ANISOU 2296 C SER A 327 3032 4260 4359 254 272 291 C ATOM 2297 O SER A 327 91.626 -11.192 53.918 1.00 26.43 O ANISOU 2297 O SER A 327 2472 3727 3845 218 285 303 O ATOM 2298 CB SER A 327 90.935 -10.993 50.952 1.00 21.24 C ANISOU 2298 CB SER A 327 1911 2996 3162 212 260 300 C ATOM 2299 OG SER A 327 90.072 -11.438 49.918 1.00 24.20 O ANISOU 2299 OG SER A 327 2296 3378 3523 198 237 311 O ATOM 2300 N VAL A 328 91.292 -8.984 53.679 1.00 31.18 N ANISOU 2300 N VAL A 328 3112 4320 4417 301 277 270 N ATOM 2301 CA VAL A 328 92.109 -8.634 54.838 1.00 28.26 C ANISOU 2301 CA VAL A 328 2726 3948 4061 313 297 260 C ATOM 2302 C VAL A 328 91.395 -7.595 55.691 1.00 40.94 C ANISOU 2302 C VAL A 328 4300 5610 5645 367 285 250 C ATOM 2303 O VAL A 328 91.129 -6.481 55.239 1.00 47.42 O ANISOU 2303 O VAL A 328 5150 6420 6448 408 277 233 O ATOM 2304 CB VAL A 328 93.494 -8.091 54.436 1.00 31.27 C ANISOU 2304 CB VAL A 328 3170 4248 4464 313 323 242 C ATOM 2305 CG1 VAL A 328 94.272 -7.667 55.674 1.00 42.87 C ANISOU 2305 CG1 VAL A 328 4621 5719 5948 328 341 232 C ATOM 2306 CG2 VAL A 328 94.271 -9.135 53.653 1.00 20.04 C ANISOU 2306 CG2 VAL A 328 1778 2769 3066 259 337 252 C ATOM 2307 N VAL A 329 91.086 -7.970 56.928 1.00 29.47 N ANISOU 2307 N VAL A 329 2788 4218 4193 367 284 260 N ATOM 2308 CA VAL A 329 90.321 -7.109 57.819 1.00 38.17 C ANISOU 2308 CA VAL A 329 3851 5379 5272 416 272 253 C ATOM 2309 C VAL A 329 91.217 -6.110 58.539 1.00 41.76 C ANISOU 2309 C VAL A 329 4323 5809 5736 448 290 231 C ATOM 2310 O VAL A 329 92.247 -6.479 59.104 1.00 52.25 O ANISOU 2310 O VAL A 329 5653 7111 7090 426 312 231 O ATOM 2311 CB VAL A 329 89.547 -7.938 58.855 1.00 33.16 C ANISOU 2311 CB VAL A 329 3148 4819 4631 402 261 271 C ATOM 2312 CG1 VAL A 329 88.663 -7.039 59.703 1.00 30.85 C ANISOU 2312 CG1 VAL A 329 2846 4570 4306 440 240 252 C ATOM 2313 CG2 VAL A 329 88.719 -9.008 58.156 1.00 26.10 C ANISOU 2313 CG2 VAL A 329 2233 3952 3734 368 245 296 C ATOM 2314 N ARG A 330 90.813 -4.843 58.523 1.00 53.65 N ANISOU 2314 N ARG A 330 5840 7323 7220 500 280 213 N ATOM 2315 CA ARG A 330 91.589 -3.778 59.148 1.00 56.89 C ANISOU 2315 CA ARG A 330 6269 7710 7636 536 294 192 C ATOM 2316 C ARG A 330 90.675 -2.771 59.841 1.00 57.70 C ANISOU 2316 C ARG A 330 6352 7864 7708 584 273 177 C ATOM 2317 O ARG A 330 91.057 -2.149 60.833 1.00 60.70 O ANISOU 2317 O ARG A 330 6742 8236 8084 594 274 156 O ATOM 2318 CB ARG A 330 92.466 -3.072 58.108 1.00 63.17 C ANISOU 2318 CB ARG A 330 7138 8424 8441 542 305 173 C ATOM 2319 CG ARG A 330 93.535 -3.964 57.485 1.00 59.94 C ANISOU 2319 CG ARG A 330 6764 7950 8062 490 325 180 C ATOM 2320 CD ARG A 330 94.245 -3.290 56.321 1.00 44.17 C ANISOU 2320 CD ARG A 330 4838 5874 6071 496 334 164 C ATOM 2321 NE ARG A 330 95.122 -4.220 55.615 1.00 32.44 N ANISOU 2321 NE ARG A 330 3384 4330 4610 444 351 173 N ATOM 2322 CZ ARG A 330 95.860 -3.900 54.557 1.00 58.24 C ANISOU 2322 CZ ARG A 330 6716 7525 7889 438 362 162 C ATOM 2323 NH1 ARG A 330 95.831 -2.665 54.074 1.00 65.17 N ANISOU 2323 NH1 ARG A 330 7631 8378 8752 480 357 143 N ATOM 2324 NH2 ARG A 330 96.626 -4.816 53.979 1.00 40.76 N ANISOU 2324 NH2 ARG A 330 4526 5262 5698 391 378 172 N TER 2325 ARG A 330 ATOM 2326 N ASN B 31 134.819 -0.615 -2.310 1.00 73.67 N ANISOU 2326 N ASN B 31 9177 9788 9025 -646 337 -583 N ATOM 2327 CA ASN B 31 135.906 -1.576 -2.154 1.00 93.88 C ANISOU 2327 CA ASN B 31 11724 12352 11592 -619 353 -628 C ATOM 2328 C ASN B 31 136.264 -1.815 -0.689 1.00 96.80 C ANISOU 2328 C ASN B 31 12076 12722 11982 -558 343 -637 C ATOM 2329 O ASN B 31 135.740 -2.728 -0.052 1.00 96.79 O ANISOU 2329 O ASN B 31 12094 12687 11995 -521 348 -640 O ATOM 2330 CB ASN B 31 137.151 -1.111 -2.918 1.00 94.94 C ANISOU 2330 CB ASN B 31 11833 12527 11712 -644 362 -647 C ATOM 2331 CG ASN B 31 137.081 -1.422 -4.401 1.00 94.11 C ANISOU 2331 CG ASN B 31 11751 12418 11589 -693 384 -654 C ATOM 2332 OD1 ASN B 31 136.247 -2.212 -4.842 1.00107.84 O ANISOU 2332 OD1 ASN B 31 13526 14122 13327 -703 395 -653 O ATOM 2333 ND2 ASN B 31 137.971 -0.813 -5.176 1.00 98.97 N ANISOU 2333 ND2 ASN B 31 12346 13068 12189 -725 391 -663 N ATOM 2334 N THR B 32 137.179 -1.000 -0.170 1.00 85.65 N ANISOU 2334 N THR B 32 10626 11347 10569 -546 330 -637 N ATOM 2335 CA THR B 32 137.603 -1.097 1.224 1.00 74.92 C ANISOU 2335 CA THR B 32 9249 9992 9225 -487 320 -639 C ATOM 2336 C THR B 32 136.560 -0.527 2.186 1.00 70.45 C ANISOU 2336 C THR B 32 8683 9413 8670 -482 297 -609 C ATOM 2337 O THR B 32 135.751 0.324 1.814 1.00 62.74 O ANISOU 2337 O THR B 32 7712 8438 7689 -521 287 -581 O ATOM 2338 CB THR B 32 138.948 -0.378 1.455 1.00 76.28 C ANISOU 2338 CB THR B 32 9383 10210 9391 -477 312 -646 C ATOM 2339 OG1 THR B 32 139.417 -0.647 2.783 1.00 82.65 O ANISOU 2339 OG1 THR B 32 10176 11017 10211 -415 308 -644 O ATOM 2340 CG2 THR B 32 138.797 1.124 1.267 1.00 70.38 C ANISOU 2340 CG2 THR B 32 8612 9492 8635 -522 289 -621 C ATOM 2341 N LEU B 33 136.586 -1.009 3.424 1.00 63.17 N ANISOU 2341 N LEU B 33 7758 8479 7763 -427 294 -610 N ATOM 2342 CA LEU B 33 135.635 -0.586 4.449 1.00 64.01 C ANISOU 2342 CA LEU B 33 7867 8572 7883 -417 274 -586 C ATOM 2343 C LEU B 33 135.803 0.873 4.868 1.00 57.69 C ANISOU 2343 C LEU B 33 7035 7805 7079 -434 250 -565 C ATOM 2344 O LEU B 33 136.913 1.405 4.884 1.00 67.40 O ANISOU 2344 O LEU B 33 8236 9072 8301 -432 245 -572 O ATOM 2345 CB LEU B 33 135.761 -1.489 5.677 1.00 47.60 C ANISOU 2345 CB LEU B 33 5791 6475 5821 -351 280 -590 C ATOM 2346 CG LEU B 33 135.198 -2.902 5.523 1.00 60.10 C ANISOU 2346 CG LEU B 33 7407 8014 7414 -328 303 -600 C ATOM 2347 CD1 LEU B 33 135.732 -3.813 6.614 1.00 63.71 C ANISOU 2347 CD1 LEU B 33 7858 8461 7888 -258 316 -601 C ATOM 2348 CD2 LEU B 33 133.678 -2.867 5.549 1.00 57.00 C ANISOU 2348 CD2 LEU B 33 7042 7587 7028 -353 292 -584 C ATOM 2349 N ARG B 34 134.685 1.511 5.201 1.00 41.83 N ANISOU 2349 N ARG B 34 5035 5782 5076 -447 240 -534 N ATOM 2350 CA ARG B 34 134.684 2.879 5.713 1.00 50.14 C ANISOU 2350 CA ARG B 34 6069 6859 6124 -448 228 -504 C ATOM 2351 C ARG B 34 135.219 2.945 7.137 1.00 52.37 C ANISOU 2351 C ARG B 34 6325 7155 6420 -409 210 -511 C ATOM 2352 O ARG B 34 135.180 1.953 7.866 1.00 51.05 O ANISOU 2352 O ARG B 34 6165 6968 6265 -375 209 -529 O ATOM 2353 CB ARG B 34 133.277 3.476 5.671 1.00 61.02 C ANISOU 2353 CB ARG B 34 7488 8201 7496 -451 219 -464 C ATOM 2354 CG ARG B 34 132.726 3.689 4.280 1.00 62.46 C ANISOU 2354 CG ARG B 34 7707 8364 7661 -482 218 -445 C ATOM 2355 CD ARG B 34 131.435 4.482 4.329 1.00 62.37 C ANISOU 2355 CD ARG B 34 7734 8310 7655 -475 188 -398 C ATOM 2356 NE ARG B 34 130.786 4.531 3.025 1.00 77.27 N ANISOU 2356 NE ARG B 34 9653 10174 9532 -502 181 -380 N ATOM 2357 CZ ARG B 34 129.932 3.613 2.586 1.00 71.37 C ANISOU 2357 CZ ARG B 34 8931 9394 8792 -513 183 -381 C ATOM 2358 NH1 ARG B 34 129.622 2.576 3.353 1.00 67.30 N ANISOU 2358 NH1 ARG B 34 8412 8863 8294 -499 192 -401 N ATOM 2359 NH2 ARG B 34 129.387 3.731 1.384 1.00 71.92 N ANISOU 2359 NH2 ARG B 34 9028 9447 8850 -536 174 -363 N ATOM 2360 N VAL B 35 135.720 4.115 7.524 1.00 55.76 N ANISOU 2360 N VAL B 35 6749 7598 6838 -393 193 -484 N ATOM 2361 CA VAL B 35 136.240 4.325 8.872 1.00 59.86 C ANISOU 2361 CA VAL B 35 7248 8129 7366 -358 173 -484 C ATOM 2362 C VAL B 35 135.223 4.013 9.987 1.00 54.13 C ANISOU 2362 C VAL B 35 6531 7378 6658 -339 168 -477 C ATOM 2363 O VAL B 35 135.575 3.321 10.941 1.00 44.19 O ANISOU 2363 O VAL B 35 5255 6128 5407 -313 162 -501 O ATOM 2364 CB VAL B 35 136.758 5.779 9.050 1.00 62.05 C ANISOU 2364 CB VAL B 35 7531 8418 7627 -346 163 -449 C ATOM 2365 CG1 VAL B 35 137.248 6.004 10.472 1.00 52.22 C ANISOU 2365 CG1 VAL B 35 6268 7182 6390 -314 142 -444 C ATOM 2366 CG2 VAL B 35 137.867 6.073 8.048 1.00 54.08 C ANISOU 2366 CG2 VAL B 35 6509 7435 6603 -363 166 -456 C ATOM 2367 N PRO B 36 133.977 4.526 9.899 1.00 53.75 N ANISOU 2367 N PRO B 36 6515 7300 6607 -347 173 -448 N ATOM 2368 CA PRO B 36 133.044 4.158 10.976 1.00 49.88 C ANISOU 2368 CA PRO B 36 6031 6787 6136 -330 170 -446 C ATOM 2369 C PRO B 36 132.811 2.654 11.137 1.00 50.23 C ANISOU 2369 C PRO B 36 6069 6816 6200 -326 178 -480 C ATOM 2370 O PRO B 36 132.669 2.171 12.263 1.00 59.63 O ANISOU 2370 O PRO B 36 7263 7991 7402 -289 173 -483 O ATOM 2371 CB PRO B 36 131.746 4.865 10.584 1.00 34.48 C ANISOU 2371 CB PRO B 36 4120 4798 4182 -345 163 -411 C ATOM 2372 CG PRO B 36 131.880 5.151 9.128 1.00 50.03 C ANISOU 2372 CG PRO B 36 6104 6769 6134 -373 166 -403 C ATOM 2373 CD PRO B 36 133.331 5.424 8.919 1.00 61.38 C ANISOU 2373 CD PRO B 36 7512 8255 7555 -372 176 -421 C ATOM 2374 N ASP B 37 132.786 1.923 10.024 1.00 55.13 N ANISOU 2374 N ASP B 37 6710 7423 6816 -341 192 -493 N ATOM 2375 CA ASP B 37 132.598 0.478 10.078 1.00 55.34 C ANISOU 2375 CA ASP B 37 6761 7415 6849 -311 208 -511 C ATOM 2376 C ASP B 37 133.825 -0.216 10.670 1.00 49.51 C ANISOU 2376 C ASP B 37 6009 6691 6112 -256 220 -522 C ATOM 2377 O ASP B 37 133.705 -1.208 11.397 1.00 50.87 O ANISOU 2377 O ASP B 37 6192 6838 6299 -211 232 -520 O ATOM 2378 CB ASP B 37 132.292 -0.074 8.680 1.00 60.14 C ANISOU 2378 CB ASP B 37 7394 8006 7450 -343 222 -520 C ATOM 2379 CG ASP B 37 130.995 0.476 8.101 1.00 71.65 C ANISOU 2379 CG ASP B 37 8877 9439 8909 -383 213 -492 C ATOM 2380 OD1 ASP B 37 130.993 1.638 7.641 1.00 77.28 O ANISOU 2380 OD1 ASP B 37 9586 10168 9609 -405 204 -467 O ATOM 2381 OD2 ASP B 37 129.982 -0.256 8.093 1.00 65.65 O ANISOU 2381 OD2 ASP B 37 8147 8635 8160 -381 214 -489 O ATOM 2382 N ILE B 38 135.002 0.325 10.364 1.00 41.92 N ANISOU 2382 N ILE B 38 5023 5768 5137 -261 216 -527 N ATOM 2383 CA ILE B 38 136.261 -0.209 10.871 1.00 52.55 C ANISOU 2383 CA ILE B 38 6354 7128 6485 -212 226 -531 C ATOM 2384 C ILE B 38 136.331 -0.030 12.382 1.00 48.63 C ANISOU 2384 C ILE B 38 5846 6633 6000 -172 215 -511 C ATOM 2385 O ILE B 38 136.672 -0.957 13.128 1.00 53.38 O ANISOU 2385 O ILE B 38 6448 7220 6615 -123 228 -507 O ATOM 2386 CB ILE B 38 137.472 0.492 10.210 1.00 66.23 C ANISOU 2386 CB ILE B 38 8063 8902 8198 -231 221 -540 C ATOM 2387 CG1 ILE B 38 137.596 0.085 8.739 1.00 58.24 C ANISOU 2387 CG1 ILE B 38 7063 7888 7177 -263 239 -561 C ATOM 2388 CG2 ILE B 38 138.756 0.182 10.964 1.00 58.63 C ANISOU 2388 CG2 ILE B 38 7081 7956 7239 -181 227 -537 C ATOM 2389 CD1 ILE B 38 138.638 0.878 7.967 1.00 47.65 C ANISOU 2389 CD1 ILE B 38 5699 6588 5817 -292 232 -570 C ATOM 2390 N LEU B 39 135.976 1.173 12.818 1.00 38.80 N ANISOU 2390 N LEU B 39 4590 5403 4749 -197 189 -498 N ATOM 2391 CA LEU B 39 135.951 1.521 14.226 1.00 49.28 C ANISOU 2391 CA LEU B 39 5908 6731 6083 -168 176 -478 C ATOM 2392 C LEU B 39 134.929 0.662 14.954 1.00 53.65 C ANISOU 2392 C LEU B 39 6481 7245 6658 -142 186 -471 C ATOM 2393 O LEU B 39 135.150 0.232 16.093 1.00 38.89 O ANISOU 2393 O LEU B 39 4608 5368 4800 -100 188 -457 O ATOM 2394 CB LEU B 39 135.626 3.008 14.385 1.00 40.71 C ANISOU 2394 CB LEU B 39 4814 5668 4988 -207 147 -469 C ATOM 2395 CG LEU B 39 135.822 3.672 15.746 1.00 54.29 C ANISOU 2395 CG LEU B 39 6525 7396 6707 -185 129 -448 C ATOM 2396 CD1 LEU B 39 137.253 3.499 16.212 1.00 53.11 C ANISOU 2396 CD1 LEU B 39 6358 7271 6551 -150 131 -443 C ATOM 2397 CD2 LEU B 39 135.456 5.148 15.666 1.00 47.70 C ANISOU 2397 CD2 LEU B 39 5698 6573 5854 -222 104 -441 C ATOM 2398 N ALA B 40 133.824 0.377 14.269 1.00 35.26 N ANISOU 2398 N ALA B 40 4174 4889 4334 -169 193 -479 N ATOM 2399 CA ALA B 40 132.812 -0.512 14.816 1.00 37.20 C ANISOU 2399 CA ALA B 40 4443 5093 4599 -147 203 -475 C ATOM 2400 C ALA B 40 133.370 -1.923 14.974 1.00 41.18 C ANISOU 2400 C ALA B 40 4954 5580 5114 -98 225 -480 C ATOM 2401 O ALA B 40 133.028 -2.626 15.925 1.00 35.75 O ANISOU 2401 O ALA B 40 4273 4867 4442 -61 230 -469 O ATOM 2402 CB ALA B 40 131.575 -0.519 13.933 1.00 34.05 C ANISOU 2402 CB ALA B 40 4069 4667 4202 -190 204 -483 C ATOM 2403 N LEU B 41 134.238 -2.333 14.053 1.00 42.53 N ANISOU 2403 N LEU B 41 5122 5763 5274 -99 238 -495 N ATOM 2404 CA LEU B 41 134.875 -3.642 14.165 1.00 40.87 C ANISOU 2404 CA LEU B 41 4916 5538 5076 -53 260 -501 C ATOM 2405 C LEU B 41 135.836 -3.704 15.351 1.00 46.47 C ANISOU 2405 C LEU B 41 5602 6264 5792 -8 257 -485 C ATOM 2406 O LEU B 41 135.889 -4.709 16.076 1.00 37.55 O ANISOU 2406 O LEU B 41 4477 5111 4680 35 268 -479 O ATOM 2407 CB LEU B 41 135.613 -3.989 12.873 1.00 43.28 C ANISOU 2407 CB LEU B 41 5222 5854 5369 -67 277 -522 C ATOM 2408 CG LEU B 41 134.736 -4.276 11.655 1.00 47.37 C ANISOU 2408 CG LEU B 41 5769 6350 5881 -106 286 -538 C ATOM 2409 CD1 LEU B 41 135.593 -4.435 10.412 1.00 52.02 C ANISOU 2409 CD1 LEU B 41 6354 6955 6455 -125 301 -558 C ATOM 2410 CD2 LEU B 41 133.898 -5.519 11.891 1.00 38.23 C ANISOU 2410 CD2 LEU B 41 4640 5146 4741 -80 299 -537 C ATOM 2411 N VAL B 42 136.572 -2.615 15.566 1.00 40.69 N ANISOU 2411 N VAL B 42 4845 5569 5046 -21 241 -479 N ATOM 2412 CA VAL B 42 137.520 -2.555 16.676 1.00 37.92 C ANISOU 2412 CA VAL B 42 4473 5236 4701 15 236 -462 C ATOM 2413 C VAL B 42 136.790 -2.638 18.012 1.00 43.58 C ANISOU 2413 C VAL B 42 5194 5933 5431 36 226 -442 C ATOM 2414 O VAL B 42 137.129 -3.456 18.892 1.00 38.06 O ANISOU 2414 O VAL B 42 4491 5222 4746 78 234 -432 O ATOM 2415 CB VAL B 42 138.352 -1.257 16.639 1.00 45.57 C ANISOU 2415 CB VAL B 42 5418 6248 5650 -7 217 -458 C ATOM 2416 CG1 VAL B 42 139.354 -1.231 17.782 1.00 31.14 C ANISOU 2416 CG1 VAL B 42 3570 4437 3826 28 212 -441 C ATOM 2417 CG2 VAL B 42 139.055 -1.109 15.297 1.00 46.81 C ANISOU 2417 CG2 VAL B 42 5569 6424 5791 -32 225 -479 C ATOM 2418 N ILE B 43 135.757 -1.808 18.141 1.00 40.08 N ANISOU 2418 N ILE B 43 4759 5485 4984 5 211 -436 N ATOM 2419 CA ILE B 43 134.967 -1.791 19.361 1.00 33.91 C ANISOU 2419 CA ILE B 43 3983 4685 4215 19 203 -419 C ATOM 2420 C ILE B 43 134.284 -3.139 19.561 1.00 39.45 C ANISOU 2420 C ILE B 43 4707 5345 4936 48 219 -421 C ATOM 2421 O ILE B 43 134.179 -3.627 20.687 1.00 47.18 O ANISOU 2421 O ILE B 43 5687 6311 5929 80 219 -406 O ATOM 2422 CB ILE B 43 133.908 -0.672 19.332 1.00 26.77 C ANISOU 2422 CB ILE B 43 3085 3780 3306 -23 186 -415 C ATOM 2423 CG1 ILE B 43 134.568 0.696 19.167 1.00 31.75 C ANISOU 2423 CG1 ILE B 43 3696 4451 3918 -52 166 -412 C ATOM 2424 CG2 ILE B 43 133.050 -0.701 20.587 1.00 23.69 C ANISOU 2424 CG2 ILE B 43 2702 3368 2932 -9 181 -398 C ATOM 2425 CD1 ILE B 43 133.578 1.822 18.956 1.00 33.21 C ANISOU 2425 CD1 ILE B 43 3885 4634 4099 -97 150 -411 C ATOM 2426 N PHE B 44 133.869 -3.766 18.464 1.00 37.67 N ANISOU 2426 N PHE B 44 4500 5099 4712 36 233 -438 N ATOM 2427 CA PHE B 44 133.225 -5.072 18.552 1.00 36.19 C ANISOU 2427 CA PHE B 44 4337 4871 4542 62 248 -441 C ATOM 2428 C PHE B 44 134.175 -6.123 19.105 1.00 40.16 C ANISOU 2428 C PHE B 44 4831 5371 5057 112 260 -436 C ATOM 2429 O PHE B 44 133.787 -6.942 19.945 1.00 35.64 O ANISOU 2429 O PHE B 44 4268 4771 4501 143 263 -426 O ATOM 2430 CB PHE B 44 132.710 -5.519 17.183 1.00 40.21 C ANISOU 2430 CB PHE B 44 4869 5361 5048 37 260 -461 C ATOM 2431 CG PHE B 44 131.294 -5.109 16.901 1.00 40.42 C ANISOU 2431 CG PHE B 44 4917 5364 5076 0 253 -462 C ATOM 2432 CD1 PHE B 44 130.477 -4.633 17.913 1.00 43.09 C ANISOU 2432 CD1 PHE B 44 5255 5691 5424 0 239 -447 C ATOM 2433 CD2 PHE B 44 130.775 -5.212 15.622 1.00 41.88 C ANISOU 2433 CD2 PHE B 44 5123 5537 5254 -36 259 -479 C ATOM 2434 CE1 PHE B 44 129.170 -4.261 17.652 1.00 43.08 C ANISOU 2434 CE1 PHE B 44 5274 5666 5429 -35 234 -448 C ATOM 2435 CE2 PHE B 44 129.470 -4.842 15.357 1.00 48.97 C ANISOU 2435 CE2 PHE B 44 6042 6411 6155 -73 251 -478 C ATOM 2436 CZ PHE B 44 128.668 -4.365 16.371 1.00 54.81 C ANISOU 2436 CZ PHE B 44 6780 7137 6907 -72 239 -463 C ATOM 2437 N ALA B 45 135.426 -6.082 18.655 1.00 42.11 N ANISOU 2437 N ALA B 45 5058 5645 5296 118 267 -444 N ATOM 2438 CA ALA B 45 136.409 -7.057 19.112 1.00 43.50 C ANISOU 2438 CA ALA B 45 5222 5819 5486 163 280 -440 C ATOM 2439 C ALA B 45 136.704 -6.874 20.597 1.00 39.79 C ANISOU 2439 C ALA B 45 4736 5357 5024 189 266 -417 C ATOM 2440 O ALA B 45 136.678 -7.843 21.383 1.00 40.66 O ANISOU 2440 O ALA B 45 4849 5445 5154 225 271 -407 O ATOM 2441 CB ALA B 45 137.687 -6.944 18.298 1.00 35.68 C ANISOU 2441 CB ALA B 45 4214 4857 4487 160 290 -453 C ATOM 2442 N VAL B 46 136.955 -5.624 20.986 1.00 35.25 N ANISOU 2442 N VAL B 46 4144 4815 4434 167 248 -407 N ATOM 2443 CA VAL B 46 137.286 -5.344 22.380 1.00 34.01 C ANISOU 2443 CA VAL B 46 3971 4670 4282 187 235 -385 C ATOM 2444 C VAL B 46 136.135 -5.728 23.310 1.00 38.93 C ANISOU 2444 C VAL B 46 4611 5261 4918 197 230 -373 C ATOM 2445 O VAL B 46 136.341 -6.386 24.342 1.00 28.62 O ANISOU 2445 O VAL B 46 3301 3947 3627 230 229 -360 O ATOM 2446 CB VAL B 46 137.631 -3.857 22.584 1.00 42.94 C ANISOU 2446 CB VAL B 46 5085 5838 5392 157 215 -377 C ATOM 2447 CG1 VAL B 46 137.803 -3.545 24.064 1.00 24.73 C ANISOU 2447 CG1 VAL B 46 2767 3541 3087 173 201 -354 C ATOM 2448 CG2 VAL B 46 138.882 -3.492 21.800 1.00 31.01 C ANISOU 2448 CG2 VAL B 46 3555 4359 3869 150 218 -387 C ATOM 2449 N VAL B 47 134.919 -5.359 22.910 1.00 29.84 N ANISOU 2449 N VAL B 47 3481 4093 3763 169 227 -379 N ATOM 2450 CA VAL B 47 133.726 -5.668 23.689 1.00 36.62 C ANISOU 2450 CA VAL B 47 4359 4920 4635 174 223 -370 C ATOM 2451 C VAL B 47 133.496 -7.178 23.753 1.00 36.76 C ANISOU 2451 C VAL B 47 4394 4901 4672 209 237 -372 C ATOM 2452 O VAL B 47 132.981 -7.693 24.747 1.00 38.44 O ANISOU 2452 O VAL B 47 4615 5092 4899 230 233 -360 O ATOM 2453 CB VAL B 47 132.469 -4.963 23.108 1.00 32.40 C ANISOU 2453 CB VAL B 47 3842 4372 4096 133 218 -377 C ATOM 2454 CG1 VAL B 47 131.192 -5.506 23.733 1.00 25.82 C ANISOU 2454 CG1 VAL B 47 3032 3499 3280 141 219 -371 C ATOM 2455 CG2 VAL B 47 132.554 -3.457 23.317 1.00 23.75 C ANISOU 2455 CG2 VAL B 47 2730 3309 2985 101 202 -370 C ATOM 2456 N PHE B 48 133.895 -7.901 22.710 1.00 33.82 N ANISOU 2456 N PHE B 48 4028 4522 4302 215 253 -388 N ATOM 2457 CA PHE B 48 133.722 -9.345 22.751 1.00 34.17 C ANISOU 2457 CA PHE B 48 4089 4530 4366 248 265 -389 C ATOM 2458 C PHE B 48 134.670 -9.973 23.758 1.00 40.59 C ANISOU 2458 C PHE B 48 4882 5348 5193 289 265 -376 C ATOM 2459 O PHE B 48 134.252 -10.798 24.572 1.00 44.56 O ANISOU 2459 O PHE B 48 5394 5823 5712 315 263 -365 O ATOM 2460 CB PHE B 48 133.930 -9.982 21.377 1.00 45.13 C ANISOU 2460 CB PHE B 48 5489 5908 5752 244 284 -410 C ATOM 2461 CG PHE B 48 133.689 -11.469 21.365 1.00 43.26 C ANISOU 2461 CG PHE B 48 5272 5631 5534 276 297 -412 C ATOM 2462 CD1 PHE B 48 132.409 -11.977 21.207 1.00 29.97 C ANISOU 2462 CD1 PHE B 48 3622 3909 3856 269 296 -412 C ATOM 2463 CD2 PHE B 48 134.739 -12.358 21.528 1.00 41.66 C ANISOU 2463 CD2 PHE B 48 5055 5428 5345 312 309 -411 C ATOM 2464 CE1 PHE B 48 132.183 -13.343 21.203 1.00 37.70 C ANISOU 2464 CE1 PHE B 48 4621 4851 4850 298 306 -412 C ATOM 2465 CE2 PHE B 48 134.519 -13.724 21.526 1.00 46.74 C ANISOU 2465 CE2 PHE B 48 5717 6034 6006 342 320 -411 C ATOM 2466 CZ PHE B 48 133.239 -14.217 21.362 1.00 45.15 C ANISOU 2466 CZ PHE B 48 5551 5797 5807 334 318 -411 C ATOM 2467 N LEU B 49 135.941 -9.582 23.719 1.00 39.15 N ANISOU 2467 N LEU B 49 4670 5200 5005 294 266 -375 N ATOM 2468 CA LEU B 49 136.901 -10.207 24.625 1.00 35.03 C ANISOU 2468 CA LEU B 49 4127 4684 4500 332 265 -362 C ATOM 2469 C LEU B 49 136.605 -9.851 26.082 1.00 40.89 C ANISOU 2469 C LEU B 49 4862 5431 5244 339 246 -341 C ATOM 2470 O LEU B 49 136.394 -10.739 26.932 1.00 41.83 O ANISOU 2470 O LEU B 49 4986 5527 5383 369 243 -329 O ATOM 2471 CB LEU B 49 138.327 -9.792 24.260 1.00 37.05 C ANISOU 2471 CB LEU B 49 4351 4976 4749 333 269 -366 C ATOM 2472 CG LEU B 49 138.813 -10.174 22.861 1.00 48.13 C ANISOU 2472 CG LEU B 49 5757 6377 6151 328 291 -389 C ATOM 2473 CD1 LEU B 49 140.235 -9.681 22.634 1.00 54.49 C ANISOU 2473 CD1 LEU B 49 6532 7221 6951 329 293 -391 C ATOM 2474 CD2 LEU B 49 138.721 -11.679 22.643 1.00 48.94 C ANISOU 2474 CD2 LEU B 49 5875 6442 6278 360 309 -395 C ATOM 2475 N VAL B 50 136.540 -8.548 26.348 1.00 38.64 N ANISOU 2475 N VAL B 50 4568 5175 4939 311 232 -335 N ATOM 2476 CA VAL B 50 136.338 -8.052 27.703 1.00 37.72 C ANISOU 2476 CA VAL B 50 4443 5069 4819 313 215 -316 C ATOM 2477 C VAL B 50 134.968 -8.463 28.231 1.00 42.82 C ANISOU 2477 C VAL B 50 5116 5679 5474 315 213 -312 C ATOM 2478 O VAL B 50 134.806 -8.762 29.416 1.00 38.29 O ANISOU 2478 O VAL B 50 4540 5100 4909 334 204 -297 O ATOM 2479 CB VAL B 50 136.483 -6.514 27.759 1.00 41.86 C ANISOU 2479 CB VAL B 50 4956 5631 5319 278 203 -312 C ATOM 2480 CG1 VAL B 50 136.311 -6.002 29.179 1.00 31.18 C ANISOU 2480 CG1 VAL B 50 3596 4291 3962 279 187 -292 C ATOM 2481 CG2 VAL B 50 137.834 -6.092 27.200 1.00 30.62 C ANISOU 2481 CG2 VAL B 50 3507 4242 3885 275 204 -316 C ATOM 2482 N GLY B 51 133.990 -8.513 27.332 1.00 40.65 N ANISOU 2482 N GLY B 51 4866 5380 5198 295 221 -325 N ATOM 2483 CA GLY B 51 132.633 -8.846 27.717 1.00 41.98 C ANISOU 2483 CA GLY B 51 5062 5512 5376 293 219 -323 C ATOM 2484 C GLY B 51 132.451 -10.311 28.038 1.00 44.22 C ANISOU 2484 C GLY B 51 5360 5759 5681 329 224 -319 C ATOM 2485 O GLY B 51 131.890 -10.657 29.079 1.00 43.69 O ANISOU 2485 O GLY B 51 5302 5675 5624 343 215 -306 O ATOM 2486 N VAL B 52 132.942 -11.176 27.155 1.00 43.84 N ANISOU 2486 N VAL B 52 5316 5700 5642 343 238 -329 N ATOM 2487 CA VAL B 52 132.792 -12.605 27.371 1.00 53.04 C ANISOU 2487 CA VAL B 52 6496 6828 6830 376 243 -325 C ATOM 2488 C VAL B 52 133.565 -13.018 28.612 1.00 47.92 C ANISOU 2488 C VAL B 52 5825 6188 6194 409 232 -308 C ATOM 2489 O VAL B 52 132.989 -13.588 29.548 1.00 50.47 O ANISOU 2489 O VAL B 52 6160 6488 6529 426 222 -295 O ATOM 2490 CB VAL B 52 133.278 -13.422 26.154 1.00 42.20 C ANISOU 2490 CB VAL B 52 5128 5443 5462 384 262 -341 C ATOM 2491 CG1 VAL B 52 133.478 -14.883 26.529 1.00 36.76 C ANISOU 2491 CG1 VAL B 52 4446 4723 4799 423 267 -334 C ATOM 2492 CG2 VAL B 52 132.295 -13.288 25.000 1.00 46.67 C ANISOU 2492 CG2 VAL B 52 5725 5992 6018 355 270 -357 C ATOM 2493 N LEU B 53 134.852 -12.677 28.651 1.00 47.35 N ANISOU 2493 N LEU B 53 5721 6152 6119 416 232 -306 N ATOM 2494 CA LEU B 53 135.674 -13.130 29.765 1.00 48.41 C ANISOU 2494 CA LEU B 53 5832 6295 6268 448 220 -289 C ATOM 2495 C LEU B 53 135.252 -12.474 31.081 1.00 49.25 C ANISOU 2495 C LEU B 53 5934 6415 6364 444 200 -271 C ATOM 2496 O LEU B 53 135.138 -13.147 32.116 1.00 49.17 O ANISOU 2496 O LEU B 53 5926 6391 6367 470 188 -254 O ATOM 2497 CB LEU B 53 137.154 -12.869 29.474 1.00 40.04 C ANISOU 2497 CB LEU B 53 4737 5269 5208 455 224 -290 C ATOM 2498 CG LEU B 53 137.746 -13.728 28.348 1.00 53.71 C ANISOU 2498 CG LEU B 53 6467 6985 6954 468 246 -306 C ATOM 2499 CD1 LEU B 53 139.213 -13.399 28.097 1.00 35.16 C ANISOU 2499 CD1 LEU B 53 4083 4671 4607 473 251 -308 C ATOM 2500 CD2 LEU B 53 137.574 -15.212 28.650 1.00 48.11 C ANISOU 2500 CD2 LEU B 53 5770 6235 6276 502 249 -301 C ATOM 2501 N GLY B 54 134.967 -11.176 31.029 1.00 41.59 N ANISOU 2501 N GLY B 54 4961 5471 5369 411 197 -274 N ATOM 2502 CA GLY B 54 134.632 -10.441 32.233 1.00 33.78 C ANISOU 2502 CA GLY B 54 3972 4495 4368 398 180 -254 C ATOM 2503 C GLY B 54 133.303 -10.867 32.818 1.00 52.94 C ANISOU 2503 C GLY B 54 6434 6879 6800 391 174 -243 C ATOM 2504 O GLY B 54 133.214 -11.179 34.009 1.00 49.71 O ANISOU 2504 O GLY B 54 6031 6462 6395 398 160 -219 O ATOM 2505 N ASN B 55 132.270 -10.897 31.981 1.00 45.80 N ANISOU 2505 N ASN B 55 5555 5949 5897 374 185 -258 N ATOM 2506 CA ASN B 55 130.959 -11.302 32.462 1.00 38.12 C ANISOU 2506 CA ASN B 55 4616 4935 4932 366 181 -248 C ATOM 2507 C ASN B 55 130.946 -12.760 32.903 1.00 38.35 C ANISOU 2507 C ASN B 55 4658 4932 4983 402 178 -239 C ATOM 2508 O ASN B 55 130.245 -13.109 33.856 1.00 39.31 O ANISOU 2508 O ASN B 55 4799 5030 5108 401 167 -220 O ATOM 2509 CB ASN B 55 129.895 -11.055 31.391 1.00 41.27 C ANISOU 2509 CB ASN B 55 5038 5312 5330 341 192 -266 C ATOM 2510 CG ASN B 55 129.726 -9.579 31.074 1.00 43.05 C ANISOU 2510 CG ASN B 55 5256 5564 5537 301 191 -271 C ATOM 2511 OD1 ASN B 55 129.611 -8.749 31.976 1.00 36.36 O ANISOU 2511 OD1 ASN B 55 4404 4731 4680 283 181 -256 O ATOM 2512 ND2 ASN B 55 129.720 -9.245 29.788 1.00 48.10 N ANISOU 2512 ND2 ASN B 55 5893 6210 6172 285 201 -292 N ATOM 2513 N ALA B 56 131.728 -13.610 32.236 1.00 37.89 N ANISOU 2513 N ALA B 56 4587 4873 4939 433 187 -252 N ATOM 2514 CA ALA B 56 131.808 -14.999 32.678 1.00 49.49 C ANISOU 2514 CA ALA B 56 6063 6311 6430 469 183 -243 C ATOM 2515 C ALA B 56 132.443 -15.068 34.063 1.00 43.45 C ANISOU 2515 C ALA B 56 5282 5560 5667 482 163 -214 C ATOM 2516 O ALA B 56 132.004 -15.844 34.925 1.00 40.22 O ANISOU 2516 O ALA B 56 4890 5124 5269 493 150 -195 O ATOM 2517 CB ALA B 56 132.597 -15.843 31.686 1.00 40.66 C ANISOU 2517 CB ALA B 56 4935 5187 5329 491 198 -258 C ATOM 2518 N LEU B 57 133.448 -14.225 34.290 1.00 42.77 N ANISOU 2518 N LEU B 57 5165 5517 5569 476 158 -210 N ATOM 2519 CA LEU B 57 134.086 -14.176 35.598 1.00 38.44 C ANISOU 2519 CA LEU B 57 4601 4986 5020 482 137 -181 C ATOM 2520 C LEU B 57 133.107 -13.682 36.661 1.00 40.32 C ANISOU 2520 C LEU B 57 4864 5214 5241 453 125 -162 C ATOM 2521 O LEU B 57 133.120 -14.157 37.803 1.00 38.44 O ANISOU 2521 O LEU B 57 4631 4967 5008 460 108 -137 O ATOM 2522 CB LEU B 57 135.323 -13.275 35.563 1.00 46.46 C ANISOU 2522 CB LEU B 57 5579 6051 6023 479 136 -181 C ATOM 2523 CG LEU B 57 136.154 -13.240 36.847 1.00 53.26 C ANISOU 2523 CG LEU B 57 6421 6932 6883 485 113 -150 C ATOM 2524 CD1 LEU B 57 136.648 -14.636 37.197 1.00 47.08 C ANISOU 2524 CD1 LEU B 57 5632 6125 6132 525 104 -137 C ATOM 2525 CD2 LEU B 57 137.319 -12.272 36.714 1.00 36.31 C ANISOU 2525 CD2 LEU B 57 4238 4835 4722 479 112 -150 C ATOM 2526 N VAL B 58 132.235 -12.752 36.273 1.00 35.01 N ANISOU 2526 N VAL B 58 4208 4543 4553 419 134 -174 N ATOM 2527 CA VAL B 58 131.244 -12.226 37.206 1.00 34.49 C ANISOU 2527 CA VAL B 58 4164 4466 4474 390 126 -159 C ATOM 2528 C VAL B 58 130.216 -13.291 37.569 1.00 36.37 C ANISOU 2528 C VAL B 58 4434 4657 4727 399 123 -151 C ATOM 2529 O VAL B 58 129.827 -13.419 38.735 1.00 35.97 O ANISOU 2529 O VAL B 58 4398 4597 4673 391 111 -130 O ATOM 2530 CB VAL B 58 130.511 -10.995 36.636 1.00 37.81 C ANISOU 2530 CB VAL B 58 4592 4895 4879 352 137 -174 C ATOM 2531 CG1 VAL B 58 129.388 -10.566 37.569 1.00 27.13 C ANISOU 2531 CG1 VAL B 58 3264 3524 3519 324 132 -161 C ATOM 2532 CG2 VAL B 58 131.483 -9.849 36.414 1.00 34.28 C ANISOU 2532 CG2 VAL B 58 4114 4495 4414 339 136 -179 C ATOM 2533 N VAL B 59 129.793 -14.069 36.576 1.00 38.26 N ANISOU 2533 N VAL B 59 4687 4869 4982 415 135 -168 N ATOM 2534 CA VAL B 59 128.834 -15.134 36.834 1.00 42.72 C ANISOU 2534 CA VAL B 59 5282 5388 5561 425 132 -161 C ATOM 2535 C VAL B 59 129.454 -16.178 37.754 1.00 40.94 C ANISOU 2535 C VAL B 59 5051 5155 5349 454 116 -140 C ATOM 2536 O VAL B 59 128.801 -16.666 38.684 1.00 40.66 O ANISOU 2536 O VAL B 59 5038 5097 5316 451 104 -122 O ATOM 2537 CB VAL B 59 128.358 -15.807 35.527 1.00 31.30 C ANISOU 2537 CB VAL B 59 3851 3914 4129 436 148 -184 C ATOM 2538 CG1 VAL B 59 127.524 -17.040 35.828 1.00 31.44 C ANISOU 2538 CG1 VAL B 59 3898 3885 4162 452 143 -175 C ATOM 2539 CG2 VAL B 59 127.567 -14.825 34.682 1.00 29.45 C ANISOU 2539 CG2 VAL B 59 3626 3681 3883 402 160 -200 C ATOM 2540 N TRP B 60 130.733 -16.473 37.527 1.00 47.66 N ANISOU 2540 N TRP B 60 5872 6027 6210 481 114 -142 N ATOM 2541 CA TRP B 60 131.430 -17.468 38.336 1.00 46.53 C ANISOU 2541 CA TRP B 60 5719 5876 6083 510 96 -121 C ATOM 2542 C TRP B 60 131.572 -17.011 39.784 1.00 48.36 C ANISOU 2542 C TRP B 60 5949 6125 6300 492 75 -91 C ATOM 2543 O TRP B 60 131.366 -17.791 40.715 1.00 41.30 O ANISOU 2543 O TRP B 60 5068 5211 5415 499 58 -69 O ATOM 2544 CB TRP B 60 132.808 -17.770 37.739 1.00 44.12 C ANISOU 2544 CB TRP B 60 5378 5592 5795 542 100 -129 C ATOM 2545 CG TRP B 60 133.702 -18.572 38.640 1.00 60.97 C ANISOU 2545 CG TRP B 60 7493 7725 7947 569 79 -104 C ATOM 2546 CD1 TRP B 60 134.725 -18.100 39.410 1.00 66.67 C ANISOU 2546 CD1 TRP B 60 8187 8482 8665 567 63 -84 C ATOM 2547 CD2 TRP B 60 133.650 -19.987 38.867 1.00 60.77 C ANISOU 2547 CD2 TRP B 60 7476 7663 7951 600 69 -95 C ATOM 2548 NE1 TRP B 60 135.314 -19.131 40.100 1.00 84.54 N ANISOU 2548 NE1 TRP B 60 10439 10730 10952 594 43 -61 N ATOM 2549 CE2 TRP B 60 134.673 -20.300 39.784 1.00 69.93 C ANISOU 2549 CE2 TRP B 60 8611 8836 9124 616 47 -68 C ATOM 2550 CE3 TRP B 60 132.839 -21.019 38.383 1.00 69.25 C ANISOU 2550 CE3 TRP B 60 8578 8694 9042 616 77 -105 C ATOM 2551 CZ2 TRP B 60 134.906 -21.600 40.228 1.00 79.19 C ANISOU 2551 CZ2 TRP B 60 9782 9979 10326 646 30 -51 C ATOM 2552 CZ3 TRP B 60 133.073 -22.310 38.825 1.00 70.95 C ANISOU 2552 CZ3 TRP B 60 8793 8880 9285 647 61 -90 C ATOM 2553 CH2 TRP B 60 134.098 -22.589 39.738 1.00 74.12 C ANISOU 2553 CH2 TRP B 60 9167 9295 9701 662 38 -63 C ATOM 2554 N VAL B 61 131.903 -15.738 39.969 1.00 52.34 N ANISOU 2554 N VAL B 61 6438 6666 6781 465 76 -91 N ATOM 2555 CA VAL B 61 132.076 -15.193 41.310 1.00 40.74 C ANISOU 2555 CA VAL B 61 4968 5216 5294 443 58 -65 C ATOM 2556 C VAL B 61 130.755 -15.089 42.076 1.00 42.33 C ANISOU 2556 C VAL B 61 5205 5393 5484 415 56 -56 C ATOM 2557 O VAL B 61 130.681 -15.417 43.263 1.00 51.05 O ANISOU 2557 O VAL B 61 6320 6491 6584 407 39 -31 O ATOM 2558 CB VAL B 61 132.748 -13.805 41.250 1.00 41.65 C ANISOU 2558 CB VAL B 61 5060 5377 5387 420 62 -69 C ATOM 2559 CG1 VAL B 61 132.597 -13.073 42.565 1.00 37.74 C ANISOU 2559 CG1 VAL B 61 4573 4897 4868 388 48 -46 C ATOM 2560 CG2 VAL B 61 134.217 -13.951 40.878 1.00 39.96 C ANISOU 2560 CG2 VAL B 61 4807 5191 5184 448 58 -68 C ATOM 2561 N THR B 62 129.706 -14.648 41.391 1.00 37.53 N ANISOU 2561 N THR B 62 4617 4771 4873 397 74 -76 N ATOM 2562 CA THR B 62 128.430 -14.419 42.057 1.00 34.48 C ANISOU 2562 CA THR B 62 4262 4363 4477 368 76 -71 C ATOM 2563 C THR B 62 127.528 -15.646 42.182 1.00 41.65 C ANISOU 2563 C THR B 62 5199 5225 5401 382 73 -65 C ATOM 2564 O THR B 62 126.546 -15.608 42.922 1.00 41.40 O ANISOU 2564 O THR B 62 5193 5175 5363 359 71 -56 O ATOM 2565 CB THR B 62 127.637 -13.327 41.337 1.00 36.64 C ANISOU 2565 CB THR B 62 4542 4639 4741 339 95 -92 C ATOM 2566 OG1 THR B 62 127.561 -13.640 39.941 1.00 42.13 O ANISOU 2566 OG1 THR B 62 5235 5323 5450 356 108 -114 O ATOM 2567 CG2 THR B 62 128.318 -11.982 41.514 1.00 27.13 C ANISOU 2567 CG2 THR B 62 3314 3477 3515 317 96 -93 C ATOM 2568 N ALA B 63 127.839 -16.724 41.467 1.00 42.35 N ANISOU 2568 N ALA B 63 5284 5295 5511 417 73 -72 N ATOM 2569 CA ALA B 63 126.945 -17.883 41.470 1.00 46.20 C ANISOU 2569 CA ALA B 63 5801 5739 6015 430 70 -68 C ATOM 2570 C ALA B 63 126.840 -18.571 42.832 1.00 46.99 C ANISOU 2570 C ALA B 63 5914 5826 6115 430 48 -40 C ATOM 2571 O ALA B 63 125.756 -18.988 43.244 1.00 58.03 O ANISOU 2571 O ALA B 63 7341 7193 7513 419 47 -34 O ATOM 2572 CB ALA B 63 127.389 -18.891 40.421 1.00 42.48 C ANISOU 2572 CB ALA B 63 5322 5251 5567 468 75 -82 C ATOM 2573 N PHE B 64 127.966 -18.689 43.527 1.00 64.22 N ANISOU 2573 N PHE B 64 8074 8031 8297 440 31 -21 N ATOM 2574 CA PHE B 64 128.003 -19.372 44.817 1.00 64.98 C ANISOU 2574 CA PHE B 64 8180 8117 8393 438 6 8 C ATOM 2575 C PHE B 64 127.308 -18.584 45.921 1.00 49.53 C ANISOU 2575 C PHE B 64 6242 6168 6409 395 4 20 C ATOM 2576 O PHE B 64 126.819 -19.157 46.894 1.00 68.91 O ANISOU 2576 O PHE B 64 8718 8604 8861 385 -10 40 O ATOM 2577 CB PHE B 64 129.450 -19.663 45.209 1.00 68.34 C ANISOU 2577 CB PHE B 64 8573 8565 8827 459 -14 26 C ATOM 2578 CG PHE B 64 130.154 -20.577 44.252 1.00 79.91 C ANISOU 2578 CG PHE B 64 10020 10019 10323 504 -12 16 C ATOM 2579 CD1 PHE B 64 129.517 -21.704 43.759 1.00 78.74 C ANISOU 2579 CD1 PHE B 64 9891 9831 10196 527 -9 8 C ATOM 2580 CD2 PHE B 64 131.441 -20.299 43.825 1.00 69.39 C ANISOU 2580 CD2 PHE B 64 8649 8716 8999 522 -11 12 C ATOM 2581 CE1 PHE B 64 130.156 -22.547 42.869 1.00 70.38 C ANISOU 2581 CE1 PHE B 64 8815 8759 9166 567 -4 -4 C ATOM 2582 CE2 PHE B 64 132.085 -21.138 42.934 1.00 85.11 C ANISOU 2582 CE2 PHE B 64 10622 10696 11019 562 -6 -1 C ATOM 2583 CZ PHE B 64 131.442 -22.263 42.456 1.00 91.25 C ANISOU 2583 CZ PHE B 64 11421 11433 11819 585 -2 -9 C ATOM 2584 N GLU B 65 127.272 -17.267 45.767 1.00 47.07 N ANISOU 2584 N GLU B 65 5922 5883 6078 368 19 8 N ATOM 2585 CA GLU B 65 126.660 -16.399 46.763 1.00 51.44 C ANISOU 2585 CA GLU B 65 6493 6446 6608 325 21 16 C ATOM 2586 C GLU B 65 125.245 -15.987 46.368 1.00 53.00 C ANISOU 2586 C GLU B 65 6715 6620 6804 304 43 -3 C ATOM 2587 O GLU B 65 124.600 -15.204 47.066 1.00 52.67 O ANISOU 2587 O GLU B 65 6687 6582 6745 268 50 -1 O ATOM 2588 CB GLU B 65 127.525 -15.161 46.977 1.00 46.68 C ANISOU 2588 CB GLU B 65 5866 5887 5985 306 22 16 C ATOM 2589 CG GLU B 65 129.010 -15.457 47.110 1.00 59.41 C ANISOU 2589 CG GLU B 65 7446 7524 7601 330 3 32 C ATOM 2590 CD GLU B 65 129.561 -15.114 48.481 1.00 82.52 C ANISOU 2590 CD GLU B 65 10372 10475 10507 305 -17 59 C ATOM 2591 OE1 GLU B 65 128.766 -14.741 49.369 1.00 73.25 O ANISOU 2591 OE1 GLU B 65 9223 9295 9314 269 -14 66 O ATOM 2592 OE2 GLU B 65 130.792 -15.215 48.670 1.00 90.52 O ANISOU 2592 OE2 GLU B 65 11359 11512 11524 319 -34 75 O ATOM 2593 N ALA B 66 124.772 -16.512 45.241 1.00 58.89 N ANISOU 2593 N ALA B 66 7466 7341 7569 326 53 -20 N ATOM 2594 CA ALA B 66 123.477 -16.126 44.687 1.00 45.19 C ANISOU 2594 CA ALA B 66 5751 5582 5836 308 73 -37 C ATOM 2595 C ALA B 66 122.292 -16.758 45.414 1.00 46.62 C ANISOU 2595 C ALA B 66 5966 5729 6020 295 71 -26 C ATOM 2596 O ALA B 66 121.151 -16.339 45.224 1.00 47.49 O ANISOU 2596 O ALA B 66 6093 5821 6132 274 86 -36 O ATOM 2597 CB ALA B 66 123.421 -16.479 43.208 1.00 38.70 C ANISOU 2597 CB ALA B 66 4925 4747 5032 332 84 -57 C ATOM 2598 N LYS B 67 122.552 -17.771 46.233 1.00 57.60 N ANISOU 2598 N LYS B 67 7364 7109 7412 308 51 -5 N ATOM 2599 CA LYS B 67 121.468 -18.457 46.929 1.00 57.10 C ANISOU 2599 CA LYS B 67 7333 7013 7350 297 46 7 C ATOM 2600 C LYS B 67 120.995 -17.714 48.177 1.00 52.89 C ANISOU 2600 C LYS B 67 6812 6490 6795 255 49 16 C ATOM 2601 O LYS B 67 119.951 -18.045 48.739 1.00 61.81 O ANISOU 2601 O LYS B 67 7969 7594 7923 238 51 22 O ATOM 2602 CB LYS B 67 121.889 -19.884 47.294 1.00 68.85 C ANISOU 2602 CB LYS B 67 8827 8484 8850 326 22 26 C ATOM 2603 CG LYS B 67 123.378 -20.072 47.540 1.00 70.16 C ANISOU 2603 CG LYS B 67 8964 8678 9017 346 3 39 C ATOM 2604 CD LYS B 67 123.719 -21.553 47.644 1.00 66.06 C ANISOU 2604 CD LYS B 67 8449 8135 8518 380 -19 55 C ATOM 2605 CE LYS B 67 125.219 -21.785 47.696 1.00 65.63 C ANISOU 2605 CE LYS B 67 8361 8104 8472 405 -37 66 C ATOM 2606 NZ LYS B 67 125.558 -23.234 47.647 1.00 81.14 N ANISOU 2606 NZ LYS B 67 10325 10041 10462 441 -57 79 N ATOM 2607 N ARG B 68 121.748 -16.701 48.600 1.00 47.56 N ANISOU 2607 N ARG B 68 6119 5851 6102 237 50 18 N ATOM 2608 CA ARG B 68 121.402 -15.962 49.813 1.00 49.71 C ANISOU 2608 CA ARG B 68 6402 6135 6350 195 54 26 C ATOM 2609 C ARG B 68 121.511 -14.445 49.646 1.00 47.88 C ANISOU 2609 C ARG B 68 6156 5931 6106 169 72 10 C ATOM 2610 O ARG B 68 120.566 -13.718 49.949 1.00 53.66 O ANISOU 2610 O ARG B 68 6902 6655 6832 137 91 0 O ATOM 2611 CB ARG B 68 122.282 -16.415 50.984 1.00 65.55 C ANISOU 2611 CB ARG B 68 8407 8157 8341 191 28 53 C ATOM 2612 CG ARG B 68 122.013 -17.838 51.460 1.00 86.63 C ANISOU 2612 CG ARG B 68 11096 10798 11021 206 7 72 C ATOM 2613 CD ARG B 68 122.880 -18.203 52.661 1.00111.28 C ANISOU 2613 CD ARG B 68 14216 13938 14129 196 -21 102 C ATOM 2614 NE ARG B 68 122.705 -19.598 53.061 1.00109.33 N ANISOU 2614 NE ARG B 68 13985 13662 13892 212 -44 121 N ATOM 2615 CZ ARG B 68 123.377 -20.186 54.046 1.00119.77 C ANISOU 2615 CZ ARG B 68 15307 14991 15208 208 -74 150 C ATOM 2616 NH1 ARG B 68 124.276 -19.502 54.741 1.00114.39 N ANISOU 2616 NH1 ARG B 68 14612 14345 14507 187 -84 164 N ATOM 2617 NH2 ARG B 68 123.151 -21.461 54.338 1.00127.45 N ANISOU 2617 NH2 ARG B 68 16295 15936 16193 222 -96 168 N ATOM 2618 N THR B 69 122.667 -13.968 49.191 1.00 43.23 N ANISOU 2618 N THR B 69 5538 5374 5513 182 67 7 N ATOM 2619 CA THR B 69 122.884 -12.531 49.020 1.00 30.67 C ANISOU 2619 CA THR B 69 3931 3812 3909 158 82 -7 C ATOM 2620 C THR B 69 122.107 -11.959 47.830 1.00 34.55 C ANISOU 2620 C THR B 69 4421 4290 4416 157 104 -32 C ATOM 2621 O THR B 69 122.174 -12.490 46.721 1.00 38.15 O ANISOU 2621 O THR B 69 4870 4734 4890 187 104 -41 O ATOM 2622 CB THR B 69 124.379 -12.221 48.841 1.00 33.36 C ANISOU 2622 CB THR B 69 4241 4192 4242 173 69 -1 C ATOM 2623 OG1 THR B 69 125.128 -12.873 49.873 1.00 39.33 O ANISOU 2623 OG1 THR B 69 4997 4957 4988 176 45 26 O ATOM 2624 CG2 THR B 69 124.626 -10.724 48.911 1.00 30.31 C ANISOU 2624 CG2 THR B 69 3842 3837 3838 143 81 -11 C ATOM 2625 N ILE B 70 121.401 -10.854 48.062 1.00 34.12 N ANISOU 2625 N ILE B 70 4372 4237 4355 123 123 -43 N ATOM 2626 CA ILE B 70 120.527 -10.256 47.052 1.00 25.53 C ANISOU 2626 CA ILE B 70 3284 3133 3285 116 142 -65 C ATOM 2627 C ILE B 70 121.306 -9.537 45.948 1.00 26.33 C ANISOU 2627 C ILE B 70 3356 3260 3387 126 144 -78 C ATOM 2628 O ILE B 70 121.007 -9.683 44.747 1.00 28.44 O ANISOU 2628 O ILE B 70 3620 3513 3672 141 149 -92 O ATOM 2629 CB ILE B 70 119.543 -9.250 47.696 1.00 32.22 C ANISOU 2629 CB ILE B 70 4142 3972 4128 74 161 -72 C ATOM 2630 CG1 ILE B 70 118.972 -9.808 49.004 1.00 22.61 C ANISOU 2630 CG1 ILE B 70 2951 2738 2902 58 160 -58 C ATOM 2631 CG2 ILE B 70 118.432 -8.882 46.722 1.00 19.36 C ANISOU 2631 CG2 ILE B 70 2517 2316 2524 68 178 -89 C ATOM 2632 CD1 ILE B 70 118.128 -11.043 48.834 1.00 35.68 C ANISOU 2632 CD1 ILE B 70 4629 4355 4575 75 157 -52 C ATOM 2633 N ASN B 71 122.312 -8.769 46.359 1.00 20.11 N ANISOU 2633 N ASN B 71 2550 2511 2580 117 138 -75 N ATOM 2634 CA ASN B 71 123.117 -8.000 45.421 1.00 26.58 C ANISOU 2634 CA ASN B 71 3342 3360 3397 123 139 -87 C ATOM 2635 C ASN B 71 123.810 -8.930 44.436 1.00 29.11 C ANISOU 2635 C ASN B 71 3650 3680 3730 163 129 -88 C ATOM 2636 O ASN B 71 123.957 -8.607 43.250 1.00 25.83 O ANISOU 2636 O ASN B 71 3221 3271 3323 170 135 -104 O ATOM 2637 CB ASN B 71 124.149 -7.146 46.167 1.00 21.41 C ANISOU 2637 CB ASN B 71 2670 2747 2717 107 132 -79 C ATOM 2638 CG ASN B 71 123.517 -5.993 46.938 1.00 36.69 C ANISOU 2638 CG ASN B 71 4614 4685 4640 64 146 -83 C ATOM 2639 OD1 ASN B 71 122.641 -5.294 46.428 1.00 35.94 O ANISOU 2639 OD1 ASN B 71 4523 4576 4558 47 162 -99 O ATOM 2640 ND2 ASN B 71 123.968 -5.787 48.173 1.00 34.50 N ANISOU 2640 ND2 ASN B 71 4342 4427 4340 46 139 -68 N ATOM 2641 N ALA B 72 124.200 -10.102 44.930 1.00 22.67 N ANISOU 2641 N ALA B 72 2840 2856 2916 186 115 -72 N ATOM 2642 CA ALA B 72 124.810 -11.119 44.086 1.00 29.72 C ANISOU 2642 CA ALA B 72 3724 3745 3824 226 107 -74 C ATOM 2643 C ALA B 72 123.834 -11.605 43.020 1.00 30.48 C ANISOU 2643 C ALA B 72 3834 3805 3941 235 118 -89 C ATOM 2644 O ALA B 72 124.231 -11.864 41.887 1.00 25.47 O ANISOU 2644 O ALA B 72 3189 3172 3317 257 121 -102 O ATOM 2645 CB ALA B 72 125.295 -12.287 44.930 1.00 27.60 C ANISOU 2645 CB ALA B 72 3461 3469 3557 247 88 -51 C ATOM 2646 N ILE B 73 122.555 -11.700 43.378 1.00 25.32 N ANISOU 2646 N ILE B 73 3208 3120 3294 217 126 -88 N ATOM 2647 CA ILE B 73 121.528 -12.090 42.418 1.00 23.70 C ANISOU 2647 CA ILE B 73 3018 2880 3108 222 136 -100 C ATOM 2648 C ILE B 73 121.383 -11.016 41.346 1.00 26.25 C ANISOU 2648 C ILE B 73 3327 3213 3433 206 149 -120 C ATOM 2649 O ILE B 73 121.310 -11.325 40.142 1.00 22.30 O ANISOU 2649 O ILE B 73 2826 2702 2946 219 152 -132 O ATOM 2650 CB ILE B 73 120.166 -12.328 43.110 1.00 21.98 C ANISOU 2650 CB ILE B 73 2830 2627 2896 202 141 -94 C ATOM 2651 CG1 ILE B 73 120.294 -13.419 44.175 1.00 20.95 C ANISOU 2651 CG1 ILE B 73 2713 2485 2760 215 127 -73 C ATOM 2652 CG2 ILE B 73 119.093 -12.693 42.092 1.00 17.27 C ANISOU 2652 CG2 ILE B 73 2248 1993 2320 205 150 -104 C ATOM 2653 CD1 ILE B 73 119.026 -13.664 44.962 1.00 20.98 C ANISOU 2653 CD1 ILE B 73 2746 2457 2767 195 132 -66 C ATOM 2654 N TRP B 74 121.399 -9.754 41.778 1.00 19.93 N ANISOU 2654 N TRP B 74 2517 2434 2621 176 154 -122 N ATOM 2655 CA TRP B 74 121.294 -8.650 40.824 1.00 21.95 C ANISOU 2655 CA TRP B 74 2759 2703 2880 158 164 -139 C ATOM 2656 C TRP B 74 122.430 -8.685 39.800 1.00 28.11 C ANISOU 2656 C TRP B 74 3515 3509 3656 179 159 -149 C ATOM 2657 O TRP B 74 122.198 -8.752 38.577 1.00 28.38 O ANISOU 2657 O TRP B 74 3549 3533 3702 183 164 -162 O ATOM 2658 CB TRP B 74 121.323 -7.292 41.538 1.00 22.97 C ANISOU 2658 CB TRP B 74 2878 2855 2996 125 169 -140 C ATOM 2659 CG TRP B 74 120.249 -7.018 42.572 1.00 29.91 C ANISOU 2659 CG TRP B 74 3776 3711 3876 98 178 -134 C ATOM 2660 CD1 TRP B 74 120.396 -6.278 43.712 1.00 23.91 C ANISOU 2660 CD1 TRP B 74 3016 2970 3101 74 180 -128 C ATOM 2661 CD2 TRP B 74 118.877 -7.443 42.548 1.00 20.46 C ANISOU 2661 CD2 TRP B 74 2603 2471 2700 90 187 -134 C ATOM 2662 NE1 TRP B 74 119.210 -6.224 44.401 1.00 24.15 N ANISOU 2662 NE1 TRP B 74 3067 2970 3139 52 192 -127 N ATOM 2663 CE2 TRP B 74 118.262 -6.932 43.710 1.00 22.28 C ANISOU 2663 CE2 TRP B 74 2844 2695 2925 62 196 -130 C ATOM 2664 CE3 TRP B 74 118.111 -8.209 41.664 1.00 20.31 C ANISOU 2664 CE3 TRP B 74 2598 2418 2702 103 188 -138 C ATOM 2665 CZ2 TRP B 74 116.922 -7.164 44.008 1.00 23.03 C ANISOU 2665 CZ2 TRP B 74 2961 2752 3038 48 207 -129 C ATOM 2666 CZ3 TRP B 74 116.785 -8.439 41.963 1.00 27.07 C ANISOU 2666 CZ3 TRP B 74 3476 3235 3575 89 197 -135 C ATOM 2667 CH2 TRP B 74 116.202 -7.919 43.125 1.00 30.80 C ANISOU 2667 CH2 TRP B 74 3957 3703 4044 63 206 -131 C ATOM 2668 N PHE B 75 123.658 -8.680 40.312 1.00 23.89 N ANISOU 2668 N PHE B 75 2963 3009 3107 192 150 -141 N ATOM 2669 CA PHE B 75 124.835 -8.623 39.452 1.00 26.34 C ANISOU 2669 CA PHE B 75 3247 3349 3412 211 146 -149 C ATOM 2670 C PHE B 75 124.958 -9.875 38.588 1.00 28.77 C ANISOU 2670 C PHE B 75 3560 3636 3735 244 146 -155 C ATOM 2671 O PHE B 75 125.445 -9.815 37.454 1.00 24.30 O ANISOU 2671 O PHE B 75 2980 3081 3172 253 151 -170 O ATOM 2672 CB PHE B 75 126.099 -8.423 40.292 1.00 18.32 C ANISOU 2672 CB PHE B 75 2212 2372 2379 218 135 -136 C ATOM 2673 CG PHE B 75 126.171 -7.078 40.963 1.00 21.91 C ANISOU 2673 CG PHE B 75 2658 2852 2815 184 136 -134 C ATOM 2674 CD1 PHE B 75 126.027 -5.912 40.227 1.00 20.98 C ANISOU 2674 CD1 PHE B 75 2529 2749 2694 162 144 -149 C ATOM 2675 CD2 PHE B 75 126.368 -6.979 42.332 1.00 28.41 C ANISOU 2675 CD2 PHE B 75 3486 3685 3624 173 128 -115 C ATOM 2676 CE1 PHE B 75 126.089 -4.673 40.843 1.00 20.04 C ANISOU 2676 CE1 PHE B 75 2403 2653 2559 131 145 -147 C ATOM 2677 CE2 PHE B 75 126.428 -5.746 42.953 1.00 25.65 C ANISOU 2677 CE2 PHE B 75 3132 3359 3257 141 130 -114 C ATOM 2678 CZ PHE B 75 126.288 -4.591 42.208 1.00 29.58 C ANISOU 2678 CZ PHE B 75 3617 3870 3753 121 139 -131 C ATOM 2679 N LEU B 76 124.485 -11.000 39.117 1.00 23.81 N ANISOU 2679 N LEU B 76 2953 2977 3118 260 142 -144 N ATOM 2680 CA LEU B 76 124.483 -12.248 38.369 1.00 23.96 C ANISOU 2680 CA LEU B 76 2980 2971 3153 291 142 -149 C ATOM 2681 C LEU B 76 123.569 -12.148 37.154 1.00 29.02 C ANISOU 2681 C LEU B 76 3634 3587 3804 280 154 -166 C ATOM 2682 O LEU B 76 123.974 -12.491 36.034 1.00 27.85 O ANISOU 2682 O LEU B 76 3479 3440 3662 296 160 -181 O ATOM 2683 CB LEU B 76 124.047 -13.407 39.266 1.00 26.39 C ANISOU 2683 CB LEU B 76 3309 3248 3468 307 133 -131 C ATOM 2684 CG LEU B 76 123.805 -14.764 38.608 1.00 22.54 C ANISOU 2684 CG LEU B 76 2838 2727 3000 336 133 -135 C ATOM 2685 CD1 LEU B 76 125.099 -15.338 38.066 1.00 37.59 C ANISOU 2685 CD1 LEU B 76 4721 4651 4912 370 130 -141 C ATOM 2686 CD2 LEU B 76 123.161 -15.725 39.592 1.00 32.73 C ANISOU 2686 CD2 LEU B 76 4153 3987 4297 343 123 -116 C ATOM 2687 N ASN B 77 122.348 -11.659 37.363 1.00 24.41 N ANISOU 2687 N ASN B 77 3068 2981 3223 252 159 -164 N ATOM 2688 CA ASN B 77 121.423 -11.526 36.242 1.00 21.44 C ANISOU 2688 CA ASN B 77 2706 2582 2860 238 168 -177 C ATOM 2689 C ASN B 77 121.910 -10.513 35.205 1.00 32.65 C ANISOU 2689 C ASN B 77 4104 4029 4273 222 173 -194 C ATOM 2690 O ASN B 77 121.806 -10.756 33.988 1.00 26.90 O ANISOU 2690 O ASN B 77 3379 3290 3551 224 178 -207 O ATOM 2691 CB ASN B 77 120.029 -11.145 36.743 1.00 16.00 C ANISOU 2691 CB ASN B 77 2036 1863 2179 210 172 -170 C ATOM 2692 CG ASN B 77 119.238 -12.346 37.233 1.00 23.70 C ANISOU 2692 CG ASN B 77 3040 2799 3166 224 169 -158 C ATOM 2693 OD1 ASN B 77 118.257 -12.752 36.611 1.00 33.55 O ANISOU 2693 OD1 ASN B 77 4307 4012 4428 219 173 -161 O ATOM 2694 ND2 ASN B 77 119.671 -12.926 38.347 1.00 31.30 N ANISOU 2694 ND2 ASN B 77 4004 3767 4121 239 160 -144 N ATOM 2695 N LEU B 78 122.495 -9.411 35.675 1.00 26.39 N ANISOU 2695 N LEU B 78 3289 3271 3466 206 171 -193 N ATOM 2696 CA LEU B 78 123.037 -8.426 34.744 1.00 28.84 C ANISOU 2696 CA LEU B 78 3579 3611 3768 191 174 -207 C ATOM 2697 C LEU B 78 124.161 -9.046 33.920 1.00 30.37 C ANISOU 2697 C LEU B 78 3758 3824 3959 219 175 -218 C ATOM 2698 O LEU B 78 124.304 -8.770 32.721 1.00 25.84 O ANISOU 2698 O LEU B 78 3178 3257 3384 211 180 -234 O ATOM 2699 CB LEU B 78 123.559 -7.195 35.489 1.00 22.54 C ANISOU 2699 CB LEU B 78 2761 2850 2955 172 171 -203 C ATOM 2700 CG LEU B 78 122.538 -6.223 36.079 1.00 21.96 C ANISOU 2700 CG LEU B 78 2695 2764 2884 137 174 -199 C ATOM 2701 CD1 LEU B 78 123.239 -5.072 36.788 1.00 24.70 C ANISOU 2701 CD1 LEU B 78 3022 3150 3214 120 171 -196 C ATOM 2702 CD2 LEU B 78 121.625 -5.701 34.987 1.00 33.15 C ANISOU 2702 CD2 LEU B 78 4118 4162 4317 112 179 -210 C ATOM 2703 N ALA B 79 124.930 -9.918 34.568 1.00 29.95 N ANISOU 2703 N ALA B 79 3699 3776 3903 251 170 -209 N ATOM 2704 CA ALA B 79 126.056 -10.570 33.917 1.00 31.96 C ANISOU 2704 CA ALA B 79 3938 4047 4159 281 172 -219 C ATOM 2705 C ALA B 79 125.610 -11.569 32.857 1.00 35.38 C ANISOU 2705 C ALA B 79 4389 4447 4606 295 180 -232 C ATOM 2706 O ALA B 79 126.212 -11.647 31.785 1.00 29.48 O ANISOU 2706 O ALA B 79 3631 3713 3858 301 188 -249 O ATOM 2707 CB ALA B 79 126.929 -11.256 34.946 1.00 26.30 C ANISOU 2707 CB ALA B 79 3211 3341 3442 310 162 -203 C ATOM 2708 N VAL B 80 124.559 -12.330 33.152 1.00 28.29 N ANISOU 2708 N VAL B 80 3520 3508 3721 298 179 -223 N ATOM 2709 CA VAL B 80 124.044 -13.278 32.171 1.00 36.79 C ANISOU 2709 CA VAL B 80 4617 4551 4810 308 186 -234 C ATOM 2710 C VAL B 80 123.481 -12.529 30.970 1.00 39.12 C ANISOU 2710 C VAL B 80 4917 4844 5102 276 194 -249 C ATOM 2711 O VAL B 80 123.714 -12.915 29.812 1.00 35.06 O ANISOU 2711 O VAL B 80 4405 4326 4589 281 203 -266 O ATOM 2712 CB VAL B 80 122.958 -14.187 32.780 1.00 24.40 C ANISOU 2712 CB VAL B 80 3079 2938 3254 315 182 -219 C ATOM 2713 CG1 VAL B 80 122.326 -15.070 31.713 1.00 26.30 C ANISOU 2713 CG1 VAL B 80 3344 3143 3506 320 189 -230 C ATOM 2714 CG2 VAL B 80 123.543 -15.031 33.901 1.00 23.15 C ANISOU 2714 CG2 VAL B 80 2917 2780 3099 345 172 -204 C ATOM 2715 N ALA B 81 122.781 -11.429 31.246 1.00 39.12 N ANISOU 2715 N ALA B 81 4918 4847 5099 242 191 -243 N ATOM 2716 CA ALA B 81 122.203 -10.636 30.170 1.00 27.62 C ANISOU 2716 CA ALA B 81 3464 3387 3643 208 195 -254 C ATOM 2717 C ALA B 81 123.289 -10.055 29.268 1.00 30.42 C ANISOU 2717 C ALA B 81 3794 3781 3983 204 199 -272 C ATOM 2718 O ALA B 81 123.162 -10.078 28.042 1.00 30.27 O ANISOU 2718 O ALA B 81 3780 3756 3963 191 204 -286 O ATOM 2719 CB ALA B 81 121.335 -9.527 30.736 1.00 28.35 C ANISOU 2719 CB ALA B 81 3557 3476 3738 174 190 -244 C ATOM 2720 N ASP B 82 124.363 -9.552 29.870 1.00 34.88 N ANISOU 2720 N ASP B 82 4332 4385 4536 213 196 -270 N ATOM 2721 CA ASP B 82 125.477 -9.032 29.081 1.00 32.40 C ANISOU 2721 CA ASP B 82 3992 4111 4207 211 200 -286 C ATOM 2722 C ASP B 82 126.225 -10.132 28.327 1.00 40.69 C ANISOU 2722 C ASP B 82 5041 5160 5261 242 210 -301 C ATOM 2723 O ASP B 82 126.754 -9.898 27.239 1.00 35.66 O ANISOU 2723 O ASP B 82 4393 4541 4615 234 218 -319 O ATOM 2724 CB ASP B 82 126.446 -8.256 29.974 1.00 28.62 C ANISOU 2724 CB ASP B 82 3484 3674 3715 215 193 -278 C ATOM 2725 CG ASP B 82 125.963 -6.848 30.270 1.00 50.88 C ANISOU 2725 CG ASP B 82 6298 6506 6527 177 186 -273 C ATOM 2726 OD1 ASP B 82 125.112 -6.340 29.509 1.00 41.14 O ANISOU 2726 OD1 ASP B 82 5076 5257 5299 147 187 -279 O ATOM 2727 OD2 ASP B 82 126.440 -6.244 31.254 1.00 62.83 O ANISOU 2727 OD2 ASP B 82 7797 8045 8032 176 180 -262 O ATOM 2728 N PHE B 83 126.265 -11.330 28.901 1.00 45.23 N ANISOU 2728 N PHE B 83 5626 5712 5847 276 210 -293 N ATOM 2729 CA PHE B 83 126.991 -12.433 28.284 1.00 40.97 C ANISOU 2729 CA PHE B 83 5085 5168 5315 308 221 -307 C ATOM 2730 C PHE B 83 126.277 -12.946 27.043 1.00 47.64 C ANISOU 2730 C PHE B 83 5957 5983 6162 295 230 -318 C ATOM 2731 O PHE B 83 126.919 -13.274 26.042 1.00 47.67 O ANISOU 2731 O PHE B 83 5958 5995 6159 298 240 -331 O ATOM 2732 CB PHE B 83 127.192 -13.577 29.283 1.00 43.89 C ANISOU 2732 CB PHE B 83 5458 5519 5698 347 216 -292 C ATOM 2733 CG PHE B 83 127.983 -14.738 28.735 1.00 34.53 C ANISOU 2733 CG PHE B 83 4272 4327 4521 377 225 -297 C ATOM 2734 CD1 PHE B 83 129.369 -14.701 28.710 1.00 39.84 C ANISOU 2734 CD1 PHE B 83 4912 5032 5192 394 229 -301 C ATOM 2735 CD2 PHE B 83 127.340 -15.871 28.261 1.00 33.37 C ANISOU 2735 CD2 PHE B 83 4156 4139 4384 385 231 -296 C ATOM 2736 CE1 PHE B 83 130.098 -15.769 28.212 1.00 32.14 C ANISOU 2736 CE1 PHE B 83 3935 4047 4229 419 240 -305 C ATOM 2737 CE2 PHE B 83 128.063 -16.941 27.763 1.00 26.70 C ANISOU 2737 CE2 PHE B 83 3311 3286 3548 410 242 -300 C ATOM 2738 CZ PHE B 83 129.443 -16.890 27.739 1.00 29.93 C ANISOU 2738 CZ PHE B 83 3687 3726 3960 427 247 -305 C ATOM 2739 N LEU B 84 124.949 -13.020 27.104 1.00 34.86 N ANISOU 2739 N LEU B 84 4366 4328 4551 277 225 -310 N ATOM 2740 CA LEU B 84 124.204 -13.556 25.969 1.00 38.58 C ANISOU 2740 CA LEU B 84 4867 4770 5023 262 229 -316 C ATOM 2741 C LEU B 84 124.332 -12.682 24.724 1.00 34.84 C ANISOU 2741 C LEU B 84 4386 4316 4537 228 236 -334 C ATOM 2742 O LEU B 84 124.403 -13.190 23.605 1.00 39.96 O ANISOU 2742 O LEU B 84 5047 4955 5180 223 244 -347 O ATOM 2743 CB LEU B 84 122.730 -13.725 26.328 1.00 41.95 C ANISOU 2743 CB LEU B 84 5323 5156 5460 247 220 -299 C ATOM 2744 CG LEU B 84 122.423 -14.751 27.418 1.00 55.60 C ANISOU 2744 CG LEU B 84 7066 6861 7198 277 211 -281 C ATOM 2745 CD1 LEU B 84 120.922 -14.882 27.618 1.00 64.84 C ANISOU 2745 CD1 LEU B 84 8265 7994 8376 255 200 -264 C ATOM 2746 CD2 LEU B 84 123.047 -16.098 27.082 1.00 62.23 C ANISOU 2746 CD2 LEU B 84 7912 7693 8037 311 214 -285 C ATOM 2747 N ALA B 85 124.372 -11.369 24.923 1.00 29.34 N ANISOU 2747 N ALA B 85 3669 3645 3836 202 232 -337 N ATOM 2748 CA ALA B 85 124.479 -10.439 23.805 1.00 28.21 C ANISOU 2748 CA ALA B 85 3518 3522 3679 165 234 -352 C ATOM 2749 C ALA B 85 125.832 -10.542 23.102 1.00 30.87 C ANISOU 2749 C ALA B 85 3835 3895 4001 177 244 -369 C ATOM 2750 O ALA B 85 125.932 -10.316 21.897 1.00 38.32 O ANISOU 2750 O ALA B 85 4781 4846 4935 153 250 -385 O ATOM 2751 CB ALA B 85 124.234 -9.014 24.281 1.00 31.23 C ANISOU 2751 CB ALA B 85 3884 3924 4056 135 221 -340 C ATOM 2752 N CYS B 86 126.868 -10.886 23.861 1.00 33.63 N ANISOU 2752 N CYS B 86 4163 4265 4350 213 245 -363 N ATOM 2753 CA CYS B 86 128.216 -11.003 23.312 1.00 41.94 C ANISOU 2753 CA CYS B 86 5195 5349 5391 226 254 -374 C ATOM 2754 C CYS B 86 128.355 -12.162 22.333 1.00 34.74 C ANISOU 2754 C CYS B 86 4303 4417 4482 238 268 -386 C ATOM 2755 O CYS B 86 129.211 -12.136 21.451 1.00 39.14 O ANISOU 2755 O CYS B 86 4848 4995 5028 234 279 -401 O ATOM 2756 CB CYS B 86 129.237 -11.148 24.442 1.00 36.60 C ANISOU 2756 CB CYS B 86 4492 4695 4718 260 251 -362 C ATOM 2757 SG CYS B 86 129.640 -9.577 25.234 1.00 41.88 S ANISOU 2757 SG CYS B 86 5130 5409 5373 241 237 -354 S ATOM 2758 N LEU B 87 127.512 -13.176 22.493 1.00 31.19 N ANISOU 2758 N LEU B 87 3882 3925 4045 252 268 -379 N ATOM 2759 CA LEU B 87 127.561 -14.350 21.631 1.00 43.96 C ANISOU 2759 CA LEU B 87 5520 5519 5664 265 280 -389 C ATOM 2760 C LEU B 87 127.226 -14.009 20.180 1.00 38.00 C ANISOU 2760 C LEU B 87 4779 4763 4896 226 288 -408 C ATOM 2761 O LEU B 87 127.697 -14.671 19.257 1.00 44.45 O ANISOU 2761 O LEU B 87 5602 5578 5707 230 301 -423 O ATOM 2762 CB LEU B 87 126.605 -15.426 22.146 1.00 41.02 C ANISOU 2762 CB LEU B 87 5178 5101 5305 283 274 -374 C ATOM 2763 CG LEU B 87 126.761 -15.848 23.608 1.00 45.84 C ANISOU 2763 CG LEU B 87 5781 5708 5930 318 265 -354 C ATOM 2764 CD1 LEU B 87 125.836 -17.014 23.923 1.00 34.65 C ANISOU 2764 CD1 LEU B 87 4396 4247 4522 334 257 -341 C ATOM 2765 CD2 LEU B 87 128.206 -16.203 23.920 1.00 41.09 C ANISOU 2765 CD2 LEU B 87 5151 5130 5332 351 274 -355 C ATOM 2766 N ALA B 88 126.409 -12.979 19.988 1.00 35.41 N ANISOU 2766 N ALA B 88 4455 4436 4564 185 279 -408 N ATOM 2767 CA ALA B 88 125.994 -12.558 18.653 1.00 36.78 C ANISOU 2767 CA ALA B 88 4642 4607 4726 141 283 -424 C ATOM 2768 C ALA B 88 127.060 -11.733 17.937 1.00 34.17 C ANISOU 2768 C ALA B 88 4285 4322 4377 123 290 -441 C ATOM 2769 O ALA B 88 126.976 -11.510 16.729 1.00 34.80 O ANISOU 2769 O ALA B 88 4374 4404 4443 88 296 -456 O ATOM 2770 CB ALA B 88 124.699 -11.769 18.736 1.00 32.47 C ANISOU 2770 CB ALA B 88 4110 4041 4186 103 270 -414 C ATOM 2771 N LEU B 89 128.057 -11.281 18.689 1.00 26.93 N ANISOU 2771 N LEU B 89 3336 3440 3457 144 287 -436 N ATOM 2772 CA LEU B 89 129.098 -10.407 18.154 1.00 32.09 C ANISOU 2772 CA LEU B 89 3961 4138 4093 127 290 -447 C ATOM 2773 C LEU B 89 129.902 -10.978 16.972 1.00 46.92 C ANISOU 2773 C LEU B 89 5841 6025 5961 127 308 -467 C ATOM 2774 O LEU B 89 130.124 -10.259 15.999 1.00 41.50 O ANISOU 2774 O LEU B 89 5149 5360 5257 90 310 -481 O ATOM 2775 CB LEU B 89 130.058 -9.996 19.276 1.00 34.38 C ANISOU 2775 CB LEU B 89 4218 4460 4384 155 283 -435 C ATOM 2776 CG LEU B 89 129.500 -8.903 20.188 1.00 39.75 C ANISOU 2776 CG LEU B 89 4888 5151 5065 139 265 -420 C ATOM 2777 CD1 LEU B 89 130.435 -8.629 21.352 1.00 26.60 C ANISOU 2777 CD1 LEU B 89 3194 3513 3400 167 259 -406 C ATOM 2778 CD2 LEU B 89 129.250 -7.634 19.388 1.00 33.84 C ANISOU 2778 CD2 LEU B 89 4133 4423 4300 88 258 -430 C ATOM 2779 N PRO B 90 130.375 -12.239 17.054 1.00 38.42 N ANISOU 2779 N PRO B 90 4771 4931 4894 167 321 -469 N ATOM 2780 CA PRO B 90 131.149 -12.728 15.902 1.00 38.77 C ANISOU 2780 CA PRO B 90 4817 4984 4930 164 340 -489 C ATOM 2781 C PRO B 90 130.396 -12.696 14.563 1.00 48.38 C ANISOU 2781 C PRO B 90 6062 6185 6134 119 346 -506 C ATOM 2782 O PRO B 90 131.011 -12.434 13.522 1.00 59.14 O ANISOU 2782 O PRO B 90 7419 7570 7482 96 356 -524 O ATOM 2783 CB PRO B 90 131.478 -14.175 16.291 1.00 50.72 C ANISOU 2783 CB PRO B 90 6338 6471 6461 213 352 -486 C ATOM 2784 CG PRO B 90 131.407 -14.201 17.775 1.00 32.43 C ANISOU 2784 CG PRO B 90 4011 4152 4160 244 339 -462 C ATOM 2785 CD PRO B 90 130.331 -13.233 18.147 1.00 38.40 C ANISOU 2785 CD PRO B 90 4774 4905 4913 213 320 -452 C ATOM 2786 N ALA B 91 129.092 -12.951 14.588 1.00 43.96 N ANISOU 2786 N ALA B 91 5532 5589 5581 105 338 -498 N ATOM 2787 CA ALA B 91 128.300 -12.930 13.363 1.00 46.72 C ANISOU 2787 CA ALA B 91 5910 5921 5919 60 340 -510 C ATOM 2788 C ALA B 91 128.140 -11.516 12.812 1.00 42.11 C ANISOU 2788 C ALA B 91 5316 5364 5319 6 330 -514 C ATOM 2789 O ALA B 91 128.210 -11.304 11.601 1.00 48.51 O ANISOU 2789 O ALA B 91 6136 6183 6113 -33 336 -529 O ATOM 2790 CB ALA B 91 126.938 -13.557 13.603 1.00 37.38 C ANISOU 2790 CB ALA B 91 4762 4691 4750 58 332 -497 C ATOM 2791 N LEU B 92 127.918 -10.555 13.705 1.00 46.78 N ANISOU 2791 N LEU B 92 5889 5969 5915 3 313 -500 N ATOM 2792 CA LEU B 92 127.813 -9.157 13.308 1.00 53.94 C ANISOU 2792 CA LEU B 92 6782 6904 6807 -46 301 -503 C ATOM 2793 C LEU B 92 129.140 -8.656 12.753 1.00 44.77 C ANISOU 2793 C LEU B 92 5594 5790 5628 -52 307 -516 C ATOM 2794 O LEU B 92 129.175 -7.855 11.817 1.00 42.70 O ANISOU 2794 O LEU B 92 5330 5547 5348 -99 303 -525 O ATOM 2795 CB LEU B 92 127.376 -8.292 14.494 1.00 33.34 C ANISOU 2795 CB LEU B 92 4158 4301 4209 -42 283 -485 C ATOM 2796 CG LEU B 92 126.084 -8.675 15.222 1.00 32.21 C ANISOU 2796 CG LEU B 92 4039 4112 4087 -35 275 -470 C ATOM 2797 CD1 LEU B 92 125.789 -7.690 16.347 1.00 33.33 C ANISOU 2797 CD1 LEU B 92 4162 4265 4238 -35 258 -454 C ATOM 2798 CD2 LEU B 92 124.909 -8.754 14.261 1.00 24.21 C ANISOU 2798 CD2 LEU B 92 3062 3064 3075 -80 270 -470 C ATOM 2799 N PHE B 93 130.228 -9.159 13.326 1.00 43.83 N ANISOU 2799 N PHE B 93 5454 5686 5514 -5 317 -516 N ATOM 2800 CA PHE B 93 131.571 -8.794 12.904 1.00 48.53 C ANISOU 2800 CA PHE B 93 6021 6321 6095 -4 324 -527 C ATOM 2801 C PHE B 93 131.806 -9.304 11.493 1.00 45.34 C ANISOU 2801 C PHE B 93 5634 5914 5679 -27 342 -548 C ATOM 2802 O PHE B 93 132.229 -8.556 10.603 1.00 44.80 O ANISOU 2802 O PHE B 93 5556 5873 5592 -65 341 -559 O ATOM 2803 CB PHE B 93 132.603 -9.377 13.874 1.00 38.68 C ANISOU 2803 CB PHE B 93 4753 5084 4861 53 331 -519 C ATOM 2804 CG PHE B 93 134.008 -8.902 13.638 1.00 51.13 C ANISOU 2804 CG PHE B 93 6298 6702 6427 56 335 -526 C ATOM 2805 CD1 PHE B 93 134.808 -9.506 12.682 1.00 61.92 C ANISOU 2805 CD1 PHE B 93 7665 8073 7788 59 357 -545 C ATOM 2806 CD2 PHE B 93 134.540 -7.872 14.394 1.00 54.78 C ANISOU 2806 CD2 PHE B 93 6731 7198 6885 56 319 -513 C ATOM 2807 CE1 PHE B 93 136.104 -9.077 12.471 1.00 53.55 C ANISOU 2807 CE1 PHE B 93 6577 7050 6721 61 361 -551 C ATOM 2808 CE2 PHE B 93 135.837 -7.439 14.188 1.00 54.80 C ANISOU 2808 CE2 PHE B 93 6706 7238 6878 59 322 -517 C ATOM 2809 CZ PHE B 93 136.619 -8.043 13.225 1.00 57.83 C ANISOU 2809 CZ PHE B 93 7090 7625 7258 62 343 -537 C ATOM 2810 N THR B 94 131.484 -10.577 11.288 1.00 44.31 N ANISOU 2810 N THR B 94 5530 5748 5559 -5 357 -553 N ATOM 2811 CA THR B 94 131.651 -11.201 9.985 1.00 48.17 C ANISOU 2811 CA THR B 94 6038 6228 6038 -24 376 -573 C ATOM 2812 C THR B 94 130.773 -10.519 8.940 1.00 55.47 C ANISOU 2812 C THR B 94 6983 7149 6945 -90 367 -578 C ATOM 2813 O THR B 94 131.174 -10.359 7.783 1.00 47.82 O ANISOU 2813 O THR B 94 6017 6195 5959 -124 377 -593 O ATOM 2814 CB THR B 94 131.304 -12.701 10.046 1.00 51.53 C ANISOU 2814 CB THR B 94 6490 6612 6478 11 390 -575 C ATOM 2815 OG1 THR B 94 132.162 -13.351 10.991 1.00 50.22 O ANISOU 2815 OG1 THR B 94 6304 6449 6329 69 397 -569 O ATOM 2816 CG2 THR B 94 131.465 -13.359 8.684 1.00 64.58 C ANISOU 2816 CG2 THR B 94 8164 8255 8119 -11 411 -597 C ATOM 2817 N SER B 95 129.590 -10.081 9.358 1.00 40.33 N ANISOU 2817 N SER B 95 5080 5212 5034 -109 348 -562 N ATOM 2818 CA SER B 95 128.687 -9.402 8.440 1.00 36.97 C ANISOU 2818 CA SER B 95 4674 4780 4595 -172 336 -559 C ATOM 2819 C SER B 95 129.238 -8.038 8.046 1.00 43.20 C ANISOU 2819 C SER B 95 5436 5613 5366 -211 324 -561 C ATOM 2820 O SER B 95 129.170 -7.652 6.880 1.00 44.09 O ANISOU 2820 O SER B 95 5558 5735 5461 -261 323 -567 O ATOM 2821 CB SER B 95 127.295 -9.250 9.055 1.00 47.07 C ANISOU 2821 CB SER B 95 5973 6024 5888 -182 317 -539 C ATOM 2822 OG SER B 95 126.430 -8.542 8.182 1.00 38.31 O ANISOU 2822 OG SER B 95 4881 4906 4768 -244 301 -530 O ATOM 2823 N ILE B 96 129.792 -7.310 9.011 1.00 42.01 N ANISOU 2823 N ILE B 96 5253 5491 5219 -189 314 -554 N ATOM 2824 CA ILE B 96 130.363 -6.005 8.702 1.00 37.74 C ANISOU 2824 CA ILE B 96 4684 4993 4661 -223 301 -554 C ATOM 2825 C ILE B 96 131.587 -6.130 7.794 1.00 44.94 C ANISOU 2825 C ILE B 96 5582 5934 5557 -228 318 -573 C ATOM 2826 O ILE B 96 131.783 -5.308 6.897 1.00 44.91 O ANISOU 2826 O ILE B 96 5572 5955 5536 -276 311 -577 O ATOM 2827 CB ILE B 96 130.747 -5.237 9.981 1.00 42.06 C ANISOU 2827 CB ILE B 96 5199 5565 5215 -197 287 -542 C ATOM 2828 CG1 ILE B 96 129.497 -4.894 10.787 1.00 46.67 C ANISOU 2828 CG1 ILE B 96 5795 6124 5814 -202 269 -524 C ATOM 2829 CG2 ILE B 96 131.491 -3.954 9.643 1.00 49.78 C ANISOU 2829 CG2 ILE B 96 6147 6590 6176 -228 274 -542 C ATOM 2830 CD1 ILE B 96 129.776 -4.032 11.990 1.00 46.89 C ANISOU 2830 CD1 ILE B 96 5793 6176 5847 -184 255 -512 C ATOM 2831 N VAL B 97 132.389 -7.174 8.000 1.00 52.04 N ANISOU 2831 N VAL B 97 6479 6830 6465 -180 339 -584 N ATOM 2832 CA VAL B 97 133.561 -7.392 7.151 1.00 56.03 C ANISOU 2832 CA VAL B 97 6972 7357 6958 -182 358 -604 C ATOM 2833 C VAL B 97 133.134 -7.720 5.719 1.00 56.45 C ANISOU 2833 C VAL B 97 7054 7396 6997 -228 369 -618 C ATOM 2834 O VAL B 97 133.812 -7.362 4.753 1.00 46.81 O ANISOU 2834 O VAL B 97 5825 6200 5759 -260 376 -631 O ATOM 2835 CB VAL B 97 134.464 -8.523 7.702 1.00 54.28 C ANISOU 2835 CB VAL B 97 6742 7130 6753 -118 379 -610 C ATOM 2836 CG1 VAL B 97 135.635 -8.792 6.763 1.00 42.25 C ANISOU 2836 CG1 VAL B 97 5209 5627 5219 -121 401 -632 C ATOM 2837 CG2 VAL B 97 134.977 -8.164 9.087 1.00 42.38 C ANISOU 2837 CG2 VAL B 97 5205 5639 5257 -76 367 -593 C ATOM 2838 N GLN B 98 131.981 -8.365 5.589 1.00 49.09 N ANISOU 2838 N GLN B 98 6157 6423 6072 -236 369 -612 N ATOM 2839 CA GLN B 98 131.466 -8.756 4.284 1.00 38.64 C ANISOU 2839 CA GLN B 98 4865 5081 4736 -281 379 -621 C ATOM 2840 C GLN B 98 130.460 -7.734 3.761 1.00 35.22 C ANISOU 2840 C GLN B 98 4443 4647 4291 -344 355 -603 C ATOM 2841 O GLN B 98 129.565 -8.077 2.990 1.00 40.30 O ANISOU 2841 O GLN B 98 5120 5262 4930 -377 354 -596 O ATOM 2842 CB GLN B 98 130.826 -10.145 4.351 1.00 37.42 C ANISOU 2842 CB GLN B 98 4744 4880 4595 -253 393 -623 C ATOM 2843 CG GLN B 98 131.790 -11.255 4.745 1.00 34.74 C ANISOU 2843 CG GLN B 98 4395 4537 4267 -192 417 -638 C ATOM 2844 CD GLN B 98 131.155 -12.631 4.687 1.00 53.60 C ANISOU 2844 CD GLN B 98 6818 6881 6669 -169 431 -640 C ATOM 2845 OE1 GLN B 98 130.078 -12.806 4.116 1.00 55.58 O ANISOU 2845 OE1 GLN B 98 7101 7103 6914 -204 425 -634 O ATOM 2846 NE2 GLN B 98 131.820 -13.617 5.279 1.00 61.09 N ANISOU 2846 NE2 GLN B 98 7758 7821 7634 -110 447 -645 N ATOM 2847 N HIS B 99 130.613 -6.485 4.196 1.00 36.78 N ANISOU 2847 N HIS B 99 4613 4874 4486 -358 333 -590 N ATOM 2848 CA HIS B 99 129.760 -5.380 3.756 1.00 46.97 C ANISOU 2848 CA HIS B 99 5909 6169 5770 -412 309 -566 C ATOM 2849 C HIS B 99 128.276 -5.669 3.976 1.00 45.47 C ANISOU 2849 C HIS B 99 5752 5932 5592 -419 295 -542 C ATOM 2850 O HIS B 99 127.471 -5.582 3.047 1.00 56.78 O ANISOU 2850 O HIS B 99 7209 7347 7016 -459 287 -523 O ATOM 2851 CB HIS B 99 130.025 -5.055 2.285 1.00 47.97 C ANISOU 2851 CB HIS B 99 6041 6311 5873 -465 315 -568 C ATOM 2852 CG HIS B 99 131.453 -4.715 1.993 1.00 60.70 C ANISOU 2852 CG HIS B 99 7622 7968 7475 -463 327 -589 C ATOM 2853 ND1 HIS B 99 132.381 -5.658 1.606 1.00 59.99 N ANISOU 2853 ND1 HIS B 99 7532 7881 7381 -441 354 -619 N ATOM 2854 CD2 HIS B 99 132.117 -3.535 2.046 1.00 53.99 C ANISOU 2854 CD2 HIS B 99 6739 7160 6617 -478 314 -583 C ATOM 2855 CE1 HIS B 99 133.552 -5.074 1.426 1.00 60.79 C ANISOU 2855 CE1 HIS B 99 7602 8023 7473 -443 357 -631 C ATOM 2856 NE2 HIS B 99 133.419 -3.786 1.687 1.00 66.88 N ANISOU 2856 NE2 HIS B 99 8352 8818 8240 -467 332 -610 N ATOM 2857 N HIS B 100 127.941 -6.034 5.212 1.00 50.54 N ANISOU 2857 N HIS B 100 6393 6556 6255 -377 291 -540 N ATOM 2858 CA HIS B 100 126.570 -6.310 5.644 1.00 60.07 C ANISOU 2858 CA HIS B 100 7627 7719 7479 -376 276 -517 C ATOM 2859 C HIS B 100 125.901 -7.456 4.877 1.00 55.36 C ANISOU 2859 C HIS B 100 7071 7082 6882 -384 288 -518 C ATOM 2860 O HIS B 100 124.674 -7.543 4.828 1.00 50.20 O ANISOU 2860 O HIS B 100 6442 6394 6238 -399 271 -492 O ATOM 2861 CB HIS B 100 125.719 -5.039 5.529 1.00 51.85 C ANISOU 2861 CB HIS B 100 6582 6678 6439 -413 244 -479 C ATOM 2862 CG HIS B 100 126.329 -3.843 6.192 1.00 46.92 C ANISOU 2862 CG HIS B 100 5920 6092 5813 -409 232 -475 C ATOM 2863 ND1 HIS B 100 126.770 -2.745 5.487 1.00 51.53 N ANISOU 2863 ND1 HIS B 100 6489 6711 6381 -438 223 -461 N ATOM 2864 CD2 HIS B 100 126.579 -3.578 7.497 1.00 57.86 C ANISOU 2864 CD2 HIS B 100 7284 7488 7213 -376 227 -480 C ATOM 2865 CE1 HIS B 100 127.261 -1.852 6.328 1.00 62.29 C ANISOU 2865 CE1 HIS B 100 7820 8102 7746 -424 213 -458 C ATOM 2866 NE2 HIS B 100 127.157 -2.333 7.554 1.00 42.65 N ANISOU 2866 NE2 HIS B 100 5327 5601 5277 -389 215 -470 N ATOM 2867 N HIS B 101 126.710 -8.332 4.287 1.00 48.99 N ANISOU 2867 N HIS B 101 6269 6281 6065 -372 315 -545 N ATOM 2868 CA HIS B 101 126.209 -9.587 3.731 1.00 55.16 C ANISOU 2868 CA HIS B 101 7087 7025 6848 -369 330 -550 C ATOM 2869 C HIS B 101 125.853 -10.540 4.871 1.00 46.83 C ANISOU 2869 C HIS B 101 6041 5936 5816 -313 334 -549 C ATOM 2870 O HIS B 101 126.552 -10.584 5.882 1.00 56.56 O ANISOU 2870 O HIS B 101 7247 7183 7059 -265 340 -557 O ATOM 2871 CB HIS B 101 127.252 -10.213 2.798 1.00 62.86 C ANISOU 2871 CB HIS B 101 8062 8015 7807 -369 359 -579 C ATOM 2872 CG HIS B 101 126.821 -11.505 2.179 1.00 42.23 C ANISOU 2872 CG HIS B 101 5485 5366 5194 -367 376 -586 C ATOM 2873 ND1 HIS B 101 125.899 -11.570 1.156 1.00 44.14 N ANISOU 2873 ND1 HIS B 101 5760 5587 5425 -417 369 -570 N ATOM 2874 CD2 HIS B 101 127.194 -12.782 2.431 1.00 37.67 C ANISOU 2874 CD2 HIS B 101 4916 4769 4627 -319 399 -603 C ATOM 2875 CE1 HIS B 101 125.721 -12.832 0.807 1.00 54.32 C ANISOU 2875 CE1 HIS B 101 7077 6846 6715 -402 388 -581 C ATOM 2876 NE2 HIS B 101 126.493 -13.588 1.567 1.00 52.81 N ANISOU 2876 NE2 HIS B 101 6872 6655 6539 -343 406 -601 N ATOM 2877 N TRP B 102 124.776 -11.306 4.713 1.00 41.20 N ANISOU 2877 N TRP B 102 5363 5180 5111 -317 331 -536 N ATOM 2878 CA TRP B 102 124.317 -12.195 5.782 1.00 51.61 C ANISOU 2878 CA TRP B 102 6692 6465 6453 -267 332 -530 C ATOM 2879 C TRP B 102 124.182 -13.642 5.316 1.00 46.96 C ANISOU 2879 C TRP B 102 6133 5845 5866 -248 350 -539 C ATOM 2880 O TRP B 102 123.148 -14.029 4.770 1.00 55.01 O ANISOU 2880 O TRP B 102 7185 6832 6883 -275 342 -523 O ATOM 2881 CB TRP B 102 122.985 -11.706 6.356 1.00 57.83 C ANISOU 2881 CB TRP B 102 7490 7225 7256 -282 303 -497 C ATOM 2882 CG TRP B 102 122.594 -12.408 7.626 1.00 41.58 C ANISOU 2882 CG TRP B 102 5436 5139 5223 -230 302 -489 C ATOM 2883 CD1 TRP B 102 121.727 -13.455 7.754 1.00 45.36 C ANISOU 2883 CD1 TRP B 102 5945 5574 5714 -214 300 -476 C ATOM 2884 CD2 TRP B 102 123.068 -12.117 8.948 1.00 41.84 C ANISOU 2884 CD2 TRP B 102 5441 5186 5270 -187 301 -491 C ATOM 2885 NE1 TRP B 102 121.627 -13.829 9.072 1.00 51.00 N ANISOU 2885 NE1 TRP B 102 6651 6275 6450 -165 298 -469 N ATOM 2886 CE2 TRP B 102 122.440 -13.023 9.826 1.00 56.55 C ANISOU 2886 CE2 TRP B 102 7318 7012 7154 -147 299 -477 C ATOM 2887 CE3 TRP B 102 123.959 -11.176 9.473 1.00 45.43 C ANISOU 2887 CE3 TRP B 102 5858 5683 5721 -178 301 -499 C ATOM 2888 CZ2 TRP B 102 122.674 -13.016 11.200 1.00 50.47 C ANISOU 2888 CZ2 TRP B 102 6529 6247 6402 -101 297 -471 C ATOM 2889 CZ3 TRP B 102 124.190 -11.171 10.838 1.00 52.79 C ANISOU 2889 CZ3 TRP B 102 6769 6619 6669 -132 299 -493 C ATOM 2890 CH2 TRP B 102 123.550 -12.085 11.685 1.00 50.71 C ANISOU 2890 CH2 TRP B 102 6522 6318 6427 -94 297 -479 C ATOM 2891 N PRO B 103 125.236 -14.442 5.523 1.00 44.37 N ANISOU 2891 N PRO B 103 5793 5527 5540 -202 374 -561 N ATOM 2892 CA PRO B 103 125.283 -15.838 5.083 1.00 49.56 C ANISOU 2892 CA PRO B 103 6474 6158 6199 -181 394 -572 C ATOM 2893 C PRO B 103 124.872 -16.842 6.160 1.00 54.19 C ANISOU 2893 C PRO B 103 7068 6711 6809 -125 391 -560 C ATOM 2894 O PRO B 103 125.196 -18.022 6.032 1.00 60.71 O ANISOU 2894 O PRO B 103 7905 7523 7641 -94 407 -572 O ATOM 2895 CB PRO B 103 126.756 -16.020 4.733 1.00 59.60 C ANISOU 2895 CB PRO B 103 7721 7462 7463 -161 419 -599 C ATOM 2896 CG PRO B 103 127.453 -15.182 5.769 1.00 51.73 C ANISOU 2896 CG PRO B 103 6684 6497 6473 -133 410 -596 C ATOM 2897 CD PRO B 103 126.535 -14.005 6.065 1.00 46.61 C ANISOU 2897 CD PRO B 103 6036 5851 5824 -171 383 -575 C ATOM 2898 N PHE B 104 124.184 -16.385 7.202 1.00 54.83 N ANISOU 2898 N PHE B 104 7145 6782 6906 -115 369 -538 N ATOM 2899 CA PHE B 104 123.893 -17.246 8.348 1.00 40.73 C ANISOU 2899 CA PHE B 104 5362 4972 5143 -61 364 -525 C ATOM 2900 C PHE B 104 122.471 -17.808 8.380 1.00 49.11 C ANISOU 2900 C PHE B 104 6459 5987 6213 -72 349 -502 C ATOM 2901 O PHE B 104 122.141 -18.614 9.249 1.00 56.89 O ANISOU 2901 O PHE B 104 7450 6950 7217 -31 343 -490 O ATOM 2902 CB PHE B 104 124.165 -16.485 9.644 1.00 45.43 C ANISOU 2902 CB PHE B 104 5926 5586 5751 -34 353 -514 C ATOM 2903 CG PHE B 104 125.585 -16.027 9.787 1.00 39.61 C ANISOU 2903 CG PHE B 104 5150 4892 5006 -15 365 -531 C ATOM 2904 CD1 PHE B 104 126.591 -16.934 10.073 1.00 41.51 C ANISOU 2904 CD1 PHE B 104 5378 5140 5254 35 381 -542 C ATOM 2905 CD2 PHE B 104 125.914 -14.690 9.637 1.00 44.21 C ANISOU 2905 CD2 PHE B 104 5709 5510 5577 -47 359 -534 C ATOM 2906 CE1 PHE B 104 127.900 -16.518 10.205 1.00 39.96 C ANISOU 2906 CE1 PHE B 104 5146 4983 5053 53 392 -554 C ATOM 2907 CE2 PHE B 104 127.221 -14.267 9.769 1.00 45.75 C ANISOU 2907 CE2 PHE B 104 5869 5747 5766 -30 369 -547 C ATOM 2908 CZ PHE B 104 128.216 -15.182 10.053 1.00 41.11 C ANISOU 2908 CZ PHE B 104 5270 5165 5186 20 385 -556 C ATOM 2909 N GLY B 105 121.632 -17.388 7.441 1.00 48.76 N ANISOU 2909 N GLY B 105 6438 5933 6158 -128 339 -493 N ATOM 2910 CA GLY B 105 120.276 -17.901 7.362 1.00 41.34 C ANISOU 2910 CA GLY B 105 5530 4952 5225 -142 322 -467 C ATOM 2911 C GLY B 105 119.255 -17.164 8.212 1.00 42.04 C ANISOU 2911 C GLY B 105 5615 5029 5330 -150 294 -436 C ATOM 2912 O GLY B 105 119.598 -16.305 9.033 1.00 44.94 O ANISOU 2912 O GLY B 105 5955 5415 5705 -139 289 -435 O ATOM 2913 N GLY B 106 117.988 -17.522 8.017 1.00 45.36 N ANISOU 2913 N GLY B 106 6061 5418 5757 -167 276 -408 N ATOM 2914 CA GLY B 106 116.877 -16.808 8.621 1.00 33.11 C ANISOU 2914 CA GLY B 106 4505 3855 4222 -180 246 -373 C ATOM 2915 C GLY B 106 116.749 -16.950 10.124 1.00 44.15 C ANISOU 2915 C GLY B 106 5890 5244 5642 -135 239 -362 C ATOM 2916 O GLY B 106 116.311 -16.018 10.799 1.00 48.41 O ANISOU 2916 O GLY B 106 6412 5788 6193 -142 222 -344 O ATOM 2917 N ALA B 107 117.136 -18.106 10.656 1.00 54.86 N ANISOU 2917 N ALA B 107 7251 6589 7004 -88 252 -373 N ATOM 2918 CA ALA B 107 117.065 -18.330 12.095 1.00 48.87 C ANISOU 2918 CA ALA B 107 6479 5826 6265 -43 244 -360 C ATOM 2919 C ALA B 107 118.047 -17.421 12.822 1.00 51.40 C ANISOU 2919 C ALA B 107 6766 6177 6586 -27 252 -374 C ATOM 2920 O ALA B 107 117.687 -16.744 13.790 1.00 50.16 O ANISOU 2920 O ALA B 107 6594 6021 6442 -22 239 -358 O ATOM 2921 CB ALA B 107 117.343 -19.789 12.424 1.00 44.43 C ANISOU 2921 CB ALA B 107 5926 5248 5707 3 252 -367 C ATOM 2922 N ALA B 108 119.286 -17.398 12.337 1.00 48.19 N ANISOU 2922 N ALA B 108 6346 5798 6166 -20 274 -404 N ATOM 2923 CA ALA B 108 120.301 -16.513 12.891 1.00 38.40 C ANISOU 2923 CA ALA B 108 5072 4595 4924 -7 281 -418 C ATOM 2924 C ALA B 108 119.915 -15.059 12.662 1.00 47.27 C ANISOU 2924 C ALA B 108 6185 5731 6044 -56 269 -412 C ATOM 2925 O ALA B 108 120.197 -14.197 13.495 1.00 52.43 O ANISOU 2925 O ALA B 108 6813 6405 6704 -48 264 -410 O ATOM 2926 CB ALA B 108 121.659 -16.806 12.276 1.00 35.89 C ANISOU 2926 CB ALA B 108 4740 4306 4592 7 305 -448 C ATOM 2927 N CYS B 109 119.255 -14.798 11.536 1.00 41.21 N ANISOU 2927 N CYS B 109 5438 4954 5266 -105 262 -406 N ATOM 2928 CA CYS B 109 118.786 -13.451 11.226 1.00 43.25 C ANISOU 2928 CA CYS B 109 5687 5223 5522 -154 243 -394 C ATOM 2929 C CYS B 109 117.718 -12.971 12.208 1.00 42.02 C ANISOU 2929 C CYS B 109 5527 5048 5389 -153 219 -361 C ATOM 2930 O CYS B 109 117.633 -11.782 12.514 1.00 25.18 O ANISOU 2930 O CYS B 109 3373 2932 3261 -173 206 -352 O ATOM 2931 CB CYS B 109 118.238 -13.394 9.800 1.00 31.82 C ANISOU 2931 CB CYS B 109 4260 3770 4060 -204 235 -385 C ATOM 2932 SG CYS B 109 117.429 -11.832 9.390 1.00 42.94 S ANISOU 2932 SG CYS B 109 5654 5191 5468 -257 202 -352 S ATOM 2933 N SER B 110 116.907 -13.902 12.699 1.00 33.19 N ANISOU 2933 N SER B 110 4428 3898 4285 -129 212 -341 N ATOM 2934 CA SER B 110 115.857 -13.571 13.656 1.00 37.88 C ANISOU 2934 CA SER B 110 5017 4475 4900 -124 190 -308 C ATOM 2935 C SER B 110 116.390 -13.473 15.082 1.00 48.62 C ANISOU 2935 C SER B 110 6357 5844 6272 -83 197 -314 C ATOM 2936 O SER B 110 115.952 -12.625 15.860 1.00 46.39 O ANISOU 2936 O SER B 110 6059 5564 6003 -89 184 -297 O ATOM 2937 CB SER B 110 114.732 -14.610 13.597 1.00 33.14 C ANISOU 2937 CB SER B 110 4442 3844 4308 -116 176 -283 C ATOM 2938 OG SER B 110 113.987 -14.495 12.398 1.00 51.63 O ANISOU 2938 OG SER B 110 6796 6181 6642 -156 160 -268 O ATOM 2939 N ILE B 111 117.341 -14.337 15.422 1.00 36.38 N ANISOU 2939 N ILE B 111 4805 4301 4717 -41 217 -335 N ATOM 2940 CA ILE B 111 117.795 -14.432 16.803 1.00 33.17 C ANISOU 2940 CA ILE B 111 4379 3903 4320 3 220 -333 C ATOM 2941 C ILE B 111 118.994 -13.537 17.121 1.00 40.05 C ANISOU 2941 C ILE B 111 5217 4815 5185 10 232 -354 C ATOM 2942 O ILE B 111 118.933 -12.735 18.054 1.00 39.87 O ANISOU 2942 O ILE B 111 5175 4801 5172 12 225 -346 O ATOM 2943 CB ILE B 111 118.146 -15.889 17.166 1.00 41.36 C ANISOU 2943 CB ILE B 111 5426 4929 5358 50 226 -335 C ATOM 2944 CG1 ILE B 111 116.904 -16.772 17.039 1.00 37.08 C ANISOU 2944 CG1 ILE B 111 4914 4352 4823 45 210 -312 C ATOM 2945 CG2 ILE B 111 118.698 -15.973 18.579 1.00 35.51 C ANISOU 2945 CG2 ILE B 111 4665 4203 4626 93 226 -330 C ATOM 2946 CD1 ILE B 111 117.158 -18.228 17.347 1.00 55.50 C ANISOU 2946 CD1 ILE B 111 7257 6674 7158 87 213 -314 C ATOM 2947 N LEU B 112 120.079 -13.674 16.363 1.00 47.41 N ANISOU 2947 N LEU B 112 6141 5772 6100 13 249 -381 N ATOM 2948 CA LEU B 112 121.331 -12.997 16.722 1.00 37.86 C ANISOU 2948 CA LEU B 112 4896 4608 4883 28 258 -398 C ATOM 2949 C LEU B 112 121.256 -11.457 16.815 1.00 29.81 C ANISOU 2949 C LEU B 112 3855 3611 3862 -8 249 -399 C ATOM 2950 O LEU B 112 121.713 -10.894 17.810 1.00 31.64 O ANISOU 2950 O LEU B 112 4059 3865 4097 11 247 -397 O ATOM 2951 CB LEU B 112 122.438 -13.406 15.743 1.00 33.69 C ANISOU 2951 CB LEU B 112 4362 4104 4336 32 276 -423 C ATOM 2952 CG LEU B 112 122.688 -14.913 15.664 1.00 48.66 C ANISOU 2952 CG LEU B 112 6274 5980 6234 71 286 -425 C ATOM 2953 CD1 LEU B 112 123.857 -15.210 14.745 1.00 49.74 C ANISOU 2953 CD1 LEU B 112 6402 6143 6355 75 305 -451 C ATOM 2954 CD2 LEU B 112 122.924 -15.497 17.051 1.00 50.87 C ANISOU 2954 CD2 LEU B 112 6544 6257 6529 123 281 -411 C ATOM 2955 N PRO B 113 120.687 -10.768 15.802 1.00 33.07 N ANISOU 2955 N PRO B 113 4278 4019 4268 -62 241 -401 N ATOM 2956 CA PRO B 113 120.528 -9.315 15.955 1.00 31.79 C ANISOU 2956 CA PRO B 113 4094 3878 4106 -96 224 -391 C ATOM 2957 C PRO B 113 119.660 -8.899 17.152 1.00 34.01 C ANISOU 2957 C PRO B 113 4372 4140 4411 -89 208 -364 C ATOM 2958 O PRO B 113 119.893 -7.832 17.725 1.00 32.29 O ANISOU 2958 O PRO B 113 4127 3949 4194 -96 198 -357 O ATOM 2959 CB PRO B 113 119.859 -8.896 14.639 1.00 33.37 C ANISOU 2959 CB PRO B 113 4314 4066 4300 -154 213 -389 C ATOM 2960 CG PRO B 113 120.248 -9.946 13.671 1.00 31.43 C ANISOU 2960 CG PRO B 113 4088 3816 4038 -148 229 -405 C ATOM 2961 CD PRO B 113 120.258 -11.214 14.463 1.00 34.04 C ANISOU 2961 CD PRO B 113 4429 4123 4380 -94 241 -403 C ATOM 2962 N SER B 114 118.681 -9.724 17.512 1.00 30.26 N ANISOU 2962 N SER B 114 3923 3621 3954 -77 206 -350 N ATOM 2963 CA SER B 114 117.724 -9.404 18.577 1.00 31.11 C ANISOU 2963 CA SER B 114 4029 3707 4084 -74 192 -322 C ATOM 2964 C SER B 114 118.299 -9.522 19.989 1.00 40.02 C ANISOU 2964 C SER B 114 5139 4850 5216 -30 198 -321 C ATOM 2965 O SER B 114 117.686 -9.054 20.957 1.00 34.50 O ANISOU 2965 O SER B 114 4433 4141 4532 -30 189 -303 O ATOM 2966 CB SER B 114 116.495 -10.312 18.467 1.00 27.08 C ANISOU 2966 CB SER B 114 3549 3158 3583 -73 180 -293 C ATOM 2967 OG SER B 114 115.593 -9.851 17.478 1.00 26.94 O ANISOU 2967 OG SER B 114 3540 3131 3564 -116 161 -273 O ATOM 2968 N LEU B 115 119.460 -10.161 20.111 1.00 34.87 N ANISOU 2968 N LEU B 115 4477 4222 4550 7 213 -338 N ATOM 2969 CA LEU B 115 120.035 -10.429 21.424 1.00 32.72 C ANISOU 2969 CA LEU B 115 4188 3964 4281 50 216 -333 C ATOM 2970 C LEU B 115 120.374 -9.150 22.189 1.00 32.26 C ANISOU 2970 C LEU B 115 4099 3939 4220 41 207 -325 C ATOM 2971 O LEU B 115 120.265 -9.116 23.414 1.00 40.21 O ANISOU 2971 O LEU B 115 5099 4944 5235 60 204 -312 O ATOM 2972 CB LEU B 115 121.288 -11.303 21.294 1.00 37.07 C ANISOU 2972 CB LEU B 115 4730 4534 4819 89 232 -352 C ATOM 2973 CG LEU B 115 121.082 -12.777 20.926 1.00 50.17 C ANISOU 2973 CG LEU B 115 6417 6165 6480 112 235 -348 C ATOM 2974 CD1 LEU B 115 122.401 -13.540 20.986 1.00 27.57 C ANISOU 2974 CD1 LEU B 115 3541 3327 3609 152 247 -360 C ATOM 2975 CD2 LEU B 115 120.045 -13.424 21.832 1.00 32.16 C ANISOU 2975 CD2 LEU B 115 4157 3849 4214 126 223 -321 C ATOM 2976 N ILE B 116 120.770 -8.099 21.478 1.00 27.24 N ANISOU 2976 N ILE B 116 3445 3332 3571 9 203 -334 N ATOM 2977 CA ILE B 116 121.113 -6.850 22.148 1.00 32.47 C ANISOU 2977 CA ILE B 116 4079 4027 4230 -2 194 -328 C ATOM 2978 C ILE B 116 119.870 -6.035 22.517 1.00 34.19 C ANISOU 2978 C ILE B 116 4303 4220 4468 -34 180 -309 C ATOM 2979 O ILE B 116 119.905 -5.234 23.450 1.00 29.49 O ANISOU 2979 O ILE B 116 3690 3639 3876 -35 175 -300 O ATOM 2980 CB ILE B 116 122.063 -5.988 21.289 1.00 23.89 C ANISOU 2980 CB ILE B 116 2970 2984 3123 -25 193 -344 C ATOM 2981 CG1 ILE B 116 122.645 -4.839 22.121 1.00 21.79 C ANISOU 2981 CG1 ILE B 116 2673 2756 2851 -27 186 -339 C ATOM 2982 CG2 ILE B 116 121.360 -5.487 20.037 1.00 21.27 C ANISOU 2982 CG2 ILE B 116 2651 2639 2792 -74 185 -346 C ATOM 2983 CD1 ILE B 116 123.435 -3.839 21.315 1.00 39.60 C ANISOU 2983 CD1 ILE B 116 4907 5053 5087 -54 182 -352 C ATOM 2984 N LEU B 117 118.774 -6.240 21.793 1.00 29.13 N ANISOU 2984 N LEU B 117 3686 3541 3841 -60 175 -303 N ATOM 2985 CA LEU B 117 117.512 -5.602 22.148 1.00 30.83 C ANISOU 2985 CA LEU B 117 3907 3727 4081 -88 163 -284 C ATOM 2986 C LEU B 117 116.966 -6.270 23.402 1.00 26.44 C ANISOU 2986 C LEU B 117 3362 3145 3540 -57 167 -270 C ATOM 2987 O LEU B 117 116.465 -5.607 24.334 1.00 27.84 O ANISOU 2987 O LEU B 117 3530 3316 3731 -63 163 -258 O ATOM 2988 CB LEU B 117 116.523 -5.692 20.985 1.00 31.45 C ANISOU 2988 CB LEU B 117 4007 3774 4169 -124 153 -275 C ATOM 2989 CG LEU B 117 117.073 -5.046 19.709 1.00 40.42 C ANISOU 2989 CG LEU B 117 5134 4937 5287 -157 147 -287 C ATOM 2990 CD1 LEU B 117 116.266 -5.428 18.488 1.00 34.39 C ANISOU 2990 CD1 LEU B 117 4394 4157 4518 -177 133 -265 C ATOM 2991 CD2 LEU B 117 117.126 -3.533 19.855 1.00 40.32 C ANISOU 2991 CD2 LEU B 117 5093 4952 5274 -182 132 -275 C ATOM 2992 N LEU B 118 117.115 -7.592 23.432 1.00 21.84 N ANISOU 2992 N LEU B 118 2798 2546 2953 -24 177 -274 N ATOM 2993 CA LEU B 118 116.782 -8.367 24.614 1.00 28.11 C ANISOU 2993 CA LEU B 118 3603 3321 3757 8 181 -262 C ATOM 2994 C LEU B 118 117.649 -7.915 25.778 1.00 28.09 C ANISOU 2994 C LEU B 118 3575 3353 3744 29 183 -262 C ATOM 2995 O LEU B 118 117.177 -7.809 26.910 1.00 33.51 O ANISOU 2995 O LEU B 118 4262 4029 4441 35 182 -249 O ATOM 2996 CB LEU B 118 116.987 -9.861 24.354 1.00 22.31 C ANISOU 2996 CB LEU B 118 2889 2574 3013 40 185 -262 C ATOM 2997 CG LEU B 118 116.935 -10.785 25.574 1.00 26.69 C ANISOU 2997 CG LEU B 118 3451 3120 3569 77 184 -248 C ATOM 2998 CD1 LEU B 118 115.559 -10.734 26.216 1.00 25.28 C ANISOU 2998 CD1 LEU B 118 3286 2917 3403 62 170 -220 C ATOM 2999 CD2 LEU B 118 117.317 -12.216 25.208 1.00 23.97 C ANISOU 2999 CD2 LEU B 118 3124 2768 3216 108 186 -251 C ATOM 3000 N ASN B 119 118.909 -7.613 25.485 1.00 27.17 N ANISOU 3000 N ASN B 119 3437 3280 3608 37 186 -277 N ATOM 3001 CA ASN B 119 119.824 -7.114 26.500 1.00 37.36 C ANISOU 3001 CA ASN B 119 4702 4607 4887 54 187 -276 C ATOM 3002 C ASN B 119 119.379 -5.755 27.013 1.00 31.75 C ANISOU 3002 C ASN B 119 3977 3905 4183 23 179 -267 C ATOM 3003 O ASN B 119 119.515 -5.454 28.198 1.00 31.66 O ANISOU 3003 O ASN B 119 3957 3903 4170 33 179 -259 O ATOM 3004 CB ASN B 119 121.245 -7.017 25.943 1.00 21.84 C ANISOU 3004 CB ASN B 119 2714 2684 2899 66 191 -293 C ATOM 3005 CG ASN B 119 122.205 -6.339 26.904 1.00 29.28 C ANISOU 3005 CG ASN B 119 3629 3668 3829 77 189 -290 C ATOM 3006 OD1 ASN B 119 122.361 -5.118 26.885 1.00 24.53 O ANISOU 3006 OD1 ASN B 119 3008 3090 3220 51 183 -291 O ATOM 3007 ND2 ASN B 119 122.854 -7.131 27.752 1.00 27.54 N ANISOU 3007 ND2 ASN B 119 3405 3454 3605 115 193 -286 N ATOM 3008 N MET B 120 118.813 -4.955 26.116 1.00 17.21 N ANISOU 3008 N MET B 120 2135 2056 2349 -15 172 -269 N ATOM 3009 CA MET B 120 118.382 -3.612 26.458 1.00 22.55 C ANISOU 3009 CA MET B 120 2796 2738 3034 -47 165 -262 C ATOM 3010 C MET B 120 117.240 -3.680 27.459 1.00 26.88 C ANISOU 3010 C MET B 120 3357 3250 3606 -48 166 -247 C ATOM 3011 O MET B 120 117.324 -3.116 28.564 1.00 25.19 O ANISOU 3011 O MET B 120 3131 3047 3392 -46 168 -242 O ATOM 3012 CB MET B 120 117.949 -2.856 25.198 1.00 21.48 C ANISOU 3012 CB MET B 120 2658 2597 2905 -89 155 -265 C ATOM 3013 CG MET B 120 117.474 -1.431 25.433 1.00 24.26 C ANISOU 3013 CG MET B 120 2994 2953 3272 -124 145 -258 C ATOM 3014 SD MET B 120 116.475 -0.798 24.066 1.00 28.11 S ANISOU 3014 SD MET B 120 3488 3426 3767 -162 125 -238 S ATOM 3015 CE MET B 120 116.682 0.962 24.307 1.00 52.90 C ANISOU 3015 CE MET B 120 6605 6601 6894 -174 110 -222 C ATOM 3016 N TYR B 121 116.190 -4.412 27.092 1.00 29.57 N ANISOU 3016 N TYR B 121 3723 3547 3966 -52 166 -239 N ATOM 3017 CA TYR B 121 115.035 -4.505 27.981 1.00 28.26 C ANISOU 3017 CA TYR B 121 3568 3349 3819 -54 166 -220 C ATOM 3018 C TYR B 121 115.344 -5.257 29.280 1.00 29.03 C ANISOU 3018 C TYR B 121 3672 3445 3913 -19 177 -220 C ATOM 3019 O TYR B 121 114.896 -4.850 30.358 1.00 22.66 O ANISOU 3019 O TYR B 121 2862 2634 3112 -23 179 -210 O ATOM 3020 CB TYR B 121 113.860 -5.162 27.254 1.00 21.16 C ANISOU 3020 CB TYR B 121 2690 2429 2922 -61 152 -195 C ATOM 3021 CG TYR B 121 113.203 -4.238 26.257 1.00 23.17 C ANISOU 3021 CG TYR B 121 2937 2692 3175 -93 135 -180 C ATOM 3022 CD1 TYR B 121 112.616 -3.050 26.671 1.00 30.49 C ANISOU 3022 CD1 TYR B 121 3848 3631 4104 -107 125 -164 C ATOM 3023 CD2 TYR B 121 113.169 -4.548 24.903 1.00 25.79 C ANISOU 3023 CD2 TYR B 121 3279 3021 3499 -104 126 -179 C ATOM 3024 CE1 TYR B 121 112.014 -2.196 25.768 1.00 24.44 C ANISOU 3024 CE1 TYR B 121 3080 2877 3329 -125 104 -146 C ATOM 3025 CE2 TYR B 121 112.567 -3.699 23.992 1.00 31.99 C ANISOU 3025 CE2 TYR B 121 4060 3817 4276 -127 105 -161 C ATOM 3026 CZ TYR B 121 111.992 -2.525 24.431 1.00 37.33 C ANISOU 3026 CZ TYR B 121 4724 4507 4952 -135 92 -143 C ATOM 3027 OH TYR B 121 111.391 -1.673 23.531 1.00 49.97 O ANISOU 3027 OH TYR B 121 6328 6119 6540 -152 66 -121 O ATOM 3028 N ALA B 122 116.136 -6.322 29.189 1.00 29.30 N ANISOU 3028 N ALA B 122 3713 3489 3929 14 180 -226 N ATOM 3029 CA ALA B 122 116.453 -7.111 30.374 1.00 22.62 C ANISOU 3029 CA ALA B 122 2873 2645 3076 47 184 -220 C ATOM 3030 C ALA B 122 117.299 -6.309 31.359 1.00 29.64 C ANISOU 3030 C ALA B 122 3739 3573 3950 50 185 -220 C ATOM 3031 O ALA B 122 117.025 -6.295 32.565 1.00 23.50 O ANISOU 3031 O ALA B 122 2964 2790 3174 54 188 -211 O ATOM 3032 CB ALA B 122 117.168 -8.397 29.984 1.00 18.76 C ANISOU 3032 CB ALA B 122 2394 2158 2576 82 186 -226 C ATOM 3033 N SER B 123 118.312 -5.621 30.842 1.00 35.63 N ANISOU 3033 N SER B 123 4475 4371 4693 45 182 -231 N ATOM 3034 CA SER B 123 119.185 -4.845 31.707 1.00 30.11 C ANISOU 3034 CA SER B 123 3753 3711 3977 47 182 -231 C ATOM 3035 C SER B 123 118.448 -3.657 32.311 1.00 19.27 C ANISOU 3035 C SER B 123 2374 2332 2615 15 182 -226 C ATOM 3036 O SER B 123 118.633 -3.360 33.487 1.00 21.65 O ANISOU 3036 O SER B 123 2671 2646 2910 17 185 -220 O ATOM 3037 CB SER B 123 120.427 -4.364 30.949 1.00 15.72 C ANISOU 3037 CB SER B 123 1907 1932 2135 47 179 -244 C ATOM 3038 OG SER B 123 120.092 -3.416 29.951 1.00 35.11 O ANISOU 3038 OG SER B 123 4355 4390 4596 13 174 -251 O ATOM 3039 N ILE B 124 117.615 -2.974 31.528 1.00 19.41 N ANISOU 3039 N ILE B 124 2393 2332 2652 -17 179 -227 N ATOM 3040 CA ILE B 124 116.897 -1.836 32.097 1.00 10.74 C ANISOU 3040 CA ILE B 124 1287 1225 1569 -47 181 -223 C ATOM 3041 C ILE B 124 115.847 -2.278 33.125 1.00 18.31 C ANISOU 3041 C ILE B 124 2264 2147 2546 -44 189 -212 C ATOM 3042 O ILE B 124 115.592 -1.571 34.107 1.00 17.50 O ANISOU 3042 O ILE B 124 2156 2046 2447 -57 196 -210 O ATOM 3043 CB ILE B 124 116.236 -0.964 31.004 1.00 18.35 C ANISOU 3043 CB ILE B 124 2243 2175 2553 -83 174 -226 C ATOM 3044 CG1 ILE B 124 115.935 0.429 31.558 1.00 13.29 C ANISOU 3044 CG1 ILE B 124 1585 1540 1923 -112 174 -225 C ATOM 3045 CG2 ILE B 124 114.981 -1.619 30.440 1.00 10.48 C ANISOU 3045 CG2 ILE B 124 1269 1130 1583 -90 173 -218 C ATOM 3046 CD1 ILE B 124 117.126 1.078 32.233 1.00 15.26 C ANISOU 3046 CD1 ILE B 124 1815 1838 2145 -105 175 -231 C ATOM 3047 N LEU B 125 115.274 -3.463 32.928 1.00 15.85 N ANISOU 3047 N LEU B 125 1976 1804 2244 -28 191 -207 N ATOM 3048 CA LEU B 125 114.293 -3.983 33.871 1.00 16.15 C ANISOU 3048 CA LEU B 125 2032 1808 2295 -25 197 -195 C ATOM 3049 C LEU B 125 114.956 -4.375 35.186 1.00 32.03 C ANISOU 3049 C LEU B 125 4045 3837 4286 -3 203 -193 C ATOM 3050 O LEU B 125 114.476 -4.025 36.279 1.00 24.99 O ANISOU 3050 O LEU B 125 3157 2939 3401 -14 211 -188 O ATOM 3051 CB LEU B 125 113.559 -5.182 33.268 1.00 21.87 C ANISOU 3051 CB LEU B 125 2778 2513 3019 -14 186 -178 C ATOM 3052 CG LEU B 125 112.356 -4.814 32.399 1.00 22.77 C ANISOU 3052 CG LEU B 125 2891 2621 3140 -38 171 -159 C ATOM 3053 CD1 LEU B 125 111.833 -6.006 31.605 1.00 16.76 C ANISOU 3053 CD1 LEU B 125 2151 1845 2372 -27 160 -148 C ATOM 3054 CD2 LEU B 125 111.276 -4.257 33.296 1.00 24.58 C ANISOU 3054 CD2 LEU B 125 3117 2851 3373 -51 171 -143 C ATOM 3055 N LEU B 126 116.066 -5.099 35.072 1.00 24.36 N ANISOU 3055 N LEU B 126 3071 2891 3292 26 198 -195 N ATOM 3056 CA LEU B 126 116.815 -5.505 36.249 1.00 19.99 C ANISOU 3056 CA LEU B 126 2518 2359 2720 47 198 -189 C ATOM 3057 C LEU B 126 117.352 -4.290 36.988 1.00 27.00 C ANISOU 3057 C LEU B 126 3385 3280 3594 28 200 -191 C ATOM 3058 O LEU B 126 117.326 -4.250 38.214 1.00 24.34 O ANISOU 3058 O LEU B 126 3053 2946 3249 26 204 -184 O ATOM 3059 CB LEU B 126 117.961 -6.435 35.858 1.00 21.92 C ANISOU 3059 CB LEU B 126 2758 2624 2946 81 191 -191 C ATOM 3060 CG LEU B 126 117.540 -7.824 35.382 1.00 31.70 C ANISOU 3060 CG LEU B 126 4019 3829 4195 104 190 -188 C ATOM 3061 CD1 LEU B 126 118.701 -8.528 34.705 1.00 28.69 C ANISOU 3061 CD1 LEU B 126 3629 3469 3801 134 185 -196 C ATOM 3062 CD2 LEU B 126 117.006 -8.652 36.546 1.00 29.38 C ANISOU 3062 CD2 LEU B 126 3746 3512 3904 115 190 -175 C ATOM 3063 N LEU B 127 117.802 -3.289 36.241 1.00 17.67 N ANISOU 3063 N LEU B 127 2183 2122 2408 13 197 -201 N ATOM 3064 CA LEU B 127 118.306 -2.062 36.844 1.00 21.71 C ANISOU 3064 CA LEU B 127 2675 2665 2907 -7 198 -203 C ATOM 3065 C LEU B 127 117.191 -1.294 37.541 1.00 18.96 C ANISOU 3065 C LEU B 127 2333 2293 2578 -36 209 -202 C ATOM 3066 O LEU B 127 117.429 -0.625 38.547 1.00 23.52 O ANISOU 3066 O LEU B 127 2904 2887 3145 -48 214 -201 O ATOM 3067 CB LEU B 127 118.985 -1.175 35.793 1.00 14.69 C ANISOU 3067 CB LEU B 127 1763 1806 2012 -18 191 -214 C ATOM 3068 CG LEU B 127 120.402 -1.584 35.376 1.00 17.00 C ANISOU 3068 CG LEU B 127 2043 2137 2280 7 183 -217 C ATOM 3069 CD1 LEU B 127 120.936 -0.663 34.290 1.00 18.70 C ANISOU 3069 CD1 LEU B 127 2237 2380 2490 -9 177 -228 C ATOM 3070 CD2 LEU B 127 121.336 -1.600 36.577 1.00 13.94 C ANISOU 3070 CD2 LEU B 127 1648 1780 1869 20 182 -210 C ATOM 3071 N ALA B 128 115.972 -1.394 37.018 1.00 15.83 N ANISOU 3071 N ALA B 128 1948 1856 2212 -49 212 -201 N ATOM 3072 CA ALA B 128 114.845 -0.767 37.694 1.00 19.21 C ANISOU 3072 CA ALA B 128 2380 2256 2663 -75 224 -200 C ATOM 3073 C ALA B 128 114.566 -1.475 39.018 1.00 23.45 C ANISOU 3073 C ALA B 128 2936 2780 3193 -65 234 -192 C ATOM 3074 O ALA B 128 114.315 -0.826 40.042 1.00 18.02 O ANISOU 3074 O ALA B 128 2248 2094 2505 -83 246 -193 O ATOM 3075 CB ALA B 128 113.615 -0.779 36.811 1.00 11.17 C ANISOU 3075 CB ALA B 128 1368 1199 1677 -89 223 -196 C ATOM 3076 N THR B 129 114.641 -2.805 39.002 1.00 14.26 N ANISOU 3076 N THR B 129 1790 1606 2023 -37 229 -185 N ATOM 3077 CA THR B 129 114.402 -3.575 40.219 1.00 17.74 C ANISOU 3077 CA THR B 129 2250 2036 2456 -28 235 -176 C ATOM 3078 C THR B 129 115.475 -3.293 41.273 1.00 31.81 C ANISOU 3078 C THR B 129 4024 3856 4206 -26 234 -173 C ATOM 3079 O THR B 129 115.179 -3.124 42.463 1.00 18.03 O ANISOU 3079 O THR B 129 2287 2108 2455 -40 244 -170 O ATOM 3080 CB THR B 129 114.370 -5.082 39.922 1.00 21.54 C ANISOU 3080 CB THR B 129 2749 2498 2935 3 227 -167 C ATOM 3081 OG1 THR B 129 113.523 -5.328 38.793 1.00 18.72 O ANISOU 3081 OG1 THR B 129 2399 2109 2604 0 226 -169 O ATOM 3082 CG2 THR B 129 113.854 -5.856 41.123 1.00 20.94 C ANISOU 3082 CG2 THR B 129 2695 2403 2857 7 232 -157 C ATOM 3083 N ILE B 130 116.721 -3.220 40.814 1.00 29.58 N ANISOU 3083 N ILE B 130 3725 3611 3903 -10 222 -176 N ATOM 3084 CA ILE B 130 117.854 -2.930 41.678 1.00 14.79 C ANISOU 3084 CA ILE B 130 1841 1777 2000 -8 218 -172 C ATOM 3085 C ILE B 130 117.720 -1.531 42.249 1.00 22.99 C ANISOU 3085 C ILE B 130 2869 2829 3036 -42 228 -178 C ATOM 3086 O ILE B 130 118.063 -1.285 43.405 1.00 14.98 O ANISOU 3086 O ILE B 130 1858 1830 2002 -52 232 -173 O ATOM 3087 CB ILE B 130 119.189 -3.048 40.909 1.00 11.12 C ANISOU 3087 CB ILE B 130 1357 1349 1519 14 204 -174 C ATOM 3088 CG1 ILE B 130 119.415 -4.485 40.451 1.00 13.74 C ANISOU 3088 CG1 ILE B 130 1700 1668 1853 49 196 -168 C ATOM 3089 CG2 ILE B 130 120.357 -2.597 41.767 1.00 11.27 C ANISOU 3089 CG2 ILE B 130 1364 1410 1509 13 198 -168 C ATOM 3090 CD1 ILE B 130 120.401 -4.601 39.314 1.00 25.62 C ANISOU 3090 CD1 ILE B 130 3186 3197 3352 69 187 -176 C ATOM 3091 N SER B 131 117.196 -0.618 41.437 1.00 23.13 N ANISOU 3091 N SER B 131 2875 2837 3074 -61 232 -189 N ATOM 3092 CA SER B 131 116.997 0.752 41.886 1.00 24.44 C ANISOU 3092 CA SER B 131 3031 3012 3244 -94 243 -196 C ATOM 3093 C SER B 131 115.916 0.824 42.955 1.00 21.63 C ANISOU 3093 C SER B 131 2692 2625 2901 -113 261 -195 C ATOM 3094 O SER B 131 116.031 1.594 43.912 1.00 24.29 O ANISOU 3094 O SER B 131 3028 2976 3227 -135 271 -198 O ATOM 3095 CB SER B 131 116.642 1.657 40.707 1.00 20.21 C ANISOU 3095 CB SER B 131 2477 2470 2730 -110 240 -206 C ATOM 3096 OG SER B 131 117.682 1.657 39.745 1.00 20.11 O ANISOU 3096 OG SER B 131 2449 2489 2702 -95 225 -208 O ATOM 3097 N ALA B 132 114.879 0.004 42.804 1.00 13.49 N ANISOU 3097 N ALA B 132 1679 1555 1894 -107 266 -192 N ATOM 3098 CA ALA B 132 113.847 -0.076 43.830 1.00 23.93 C ANISOU 3098 CA ALA B 132 3018 2847 3228 -124 285 -191 C ATOM 3099 C ALA B 132 114.440 -0.641 45.116 1.00 23.50 C ANISOU 3099 C ALA B 132 2979 2811 3141 -118 285 -182 C ATOM 3100 O ALA B 132 114.067 -0.231 46.218 1.00 18.41 O ANISOU 3100 O ALA B 132 2342 2162 2492 -142 301 -185 O ATOM 3101 CB ALA B 132 112.684 -0.930 43.356 1.00 17.06 C ANISOU 3101 CB ALA B 132 2163 1931 2387 -116 287 -187 C ATOM 3102 N ASP B 133 115.389 -1.559 44.962 1.00 18.63 N ANISOU 3102 N ASP B 133 2364 2215 2502 -89 267 -172 N ATOM 3103 CA ASP B 133 116.071 -2.148 46.106 1.00 12.57 C ANISOU 3103 CA ASP B 133 1607 1465 1703 -83 262 -161 C ATOM 3104 C ASP B 133 116.894 -1.097 46.853 1.00 25.39 C ANISOU 3104 C ASP B 133 3219 3126 3301 -104 264 -163 C ATOM 3105 O ASP B 133 116.789 -0.966 48.078 1.00 29.29 O ANISOU 3105 O ASP B 133 3727 3623 3780 -124 274 -160 O ATOM 3106 CB ASP B 133 116.964 -3.303 45.648 1.00 19.60 C ANISOU 3106 CB ASP B 133 2497 2369 2581 -45 240 -150 C ATOM 3107 CG ASP B 133 117.620 -4.034 46.802 1.00 21.34 C ANISOU 3107 CG ASP B 133 2730 2604 2774 -38 231 -134 C ATOM 3108 OD1 ASP B 133 116.934 -4.301 47.808 1.00 31.45 O ANISOU 3108 OD1 ASP B 133 4030 3866 4052 -54 241 -129 O ATOM 3109 OD2 ASP B 133 118.824 -4.350 46.701 1.00 31.25 O ANISOU 3109 OD2 ASP B 133 3973 3889 4011 -17 214 -126 O ATOM 3110 N ARG B 134 117.692 -0.335 46.106 1.00 20.10 N ANISOU 3110 N ARG B 134 2525 2485 2625 -102 256 -169 N ATOM 3111 CA ARG B 134 118.529 0.706 46.697 1.00 19.73 C ANISOU 3111 CA ARG B 134 2466 2475 2553 -121 256 -171 C ATOM 3112 C ARG B 134 117.676 1.787 47.349 1.00 24.62 C ANISOU 3112 C ARG B 134 3090 3081 3184 -159 279 -183 C ATOM 3113 O ARG B 134 118.053 2.358 48.374 1.00 26.62 O ANISOU 3113 O ARG B 134 3347 3354 3414 -181 286 -182 O ATOM 3114 CB ARG B 134 119.448 1.345 45.646 1.00 10.14 C ANISOU 3114 CB ARG B 134 1226 1293 1335 -113 243 -176 C ATOM 3115 CG ARG B 134 120.338 0.380 44.868 1.00 17.76 C ANISOU 3115 CG ARG B 134 2183 2274 2293 -75 223 -168 C ATOM 3116 CD ARG B 134 120.999 -0.656 45.764 1.00 22.79 C ANISOU 3116 CD ARG B 134 2832 2921 2907 -58 213 -151 C ATOM 3117 NE ARG B 134 121.706 -0.050 46.887 1.00 33.40 N ANISOU 3117 NE ARG B 134 4174 4295 4222 -77 212 -144 N ATOM 3118 CZ ARG B 134 122.247 -0.742 47.883 1.00 33.70 C ANISOU 3118 CZ ARG B 134 4222 4343 4238 -72 202 -127 C ATOM 3119 NH1 ARG B 134 122.869 -0.112 48.869 1.00 36.28 N ANISOU 3119 NH1 ARG B 134 4549 4698 4537 -94 201 -120 N ATOM 3120 NH2 ARG B 134 122.167 -2.065 47.892 1.00 40.85 N ANISOU 3120 NH2 ARG B 134 5140 5230 5150 -46 193 -116 N ATOM 3121 N PHE B 135 116.519 2.059 46.753 1.00 25.35 N ANISOU 3121 N PHE B 135 3182 3138 3313 -168 292 -193 N ATOM 3122 CA PHE B 135 115.613 3.066 47.289 1.00 18.25 C ANISOU 3122 CA PHE B 135 2284 2219 2432 -203 316 -206 C ATOM 3123 C PHE B 135 115.028 2.605 48.616 1.00 27.61 C ANISOU 3123 C PHE B 135 3495 3387 3609 -217 333 -203 C ATOM 3124 O PHE B 135 115.051 3.335 49.615 1.00 21.24 O ANISOU 3124 O PHE B 135 2692 2589 2788 -246 348 -209 O ATOM 3125 CB PHE B 135 114.492 3.356 46.286 1.00 16.84 C ANISOU 3125 CB PHE B 135 2097 2002 2297 -207 322 -215 C ATOM 3126 CG PHE B 135 113.564 4.463 46.706 1.00 19.39 C ANISOU 3126 CG PHE B 135 2425 2315 2629 -215 327 -222 C ATOM 3127 CD1 PHE B 135 112.507 4.216 47.569 1.00 15.07 C ANISOU 3127 CD1 PHE B 135 1895 1747 2085 -214 340 -220 C ATOM 3128 CD2 PHE B 135 113.740 5.748 46.222 1.00 29.20 C ANISOU 3128 CD2 PHE B 135 3654 3574 3869 -212 312 -227 C ATOM 3129 CE1 PHE B 135 111.654 5.230 47.953 1.00 15.83 C ANISOU 3129 CE1 PHE B 135 1991 1842 2184 -211 342 -225 C ATOM 3130 CE2 PHE B 135 112.889 6.768 46.600 1.00 29.61 C ANISOU 3130 CE2 PHE B 135 3709 3620 3924 -209 313 -229 C ATOM 3131 CZ PHE B 135 111.844 6.509 47.467 1.00 11.93 C ANISOU 3131 CZ PHE B 135 1483 1362 1690 -208 329 -229 C ATOM 3132 N LEU B 136 114.508 1.382 48.617 1.00 25.54 N ANISOU 3132 N LEU B 136 3249 3099 3354 -199 330 -194 N ATOM 3133 CA LEU B 136 113.855 0.845 49.798 1.00 22.34 C ANISOU 3133 CA LEU B 136 2869 2674 2943 -213 345 -190 C ATOM 3134 C LEU B 136 114.840 0.636 50.943 1.00 29.70 C ANISOU 3134 C LEU B 136 3812 3640 3831 -219 338 -180 C ATOM 3135 O LEU B 136 114.472 0.774 52.107 1.00 21.79 O ANISOU 3135 O LEU B 136 2829 2634 2818 -246 355 -182 O ATOM 3136 CB LEU B 136 113.139 -0.463 49.461 1.00 19.41 C ANISOU 3136 CB LEU B 136 2514 2271 2589 -190 339 -181 C ATOM 3137 CG LEU B 136 111.865 -0.296 48.628 1.00 22.36 C ANISOU 3137 CG LEU B 136 2884 2603 3009 -193 351 -190 C ATOM 3138 CD1 LEU B 136 111.260 -1.652 48.307 1.00 23.49 C ANISOU 3138 CD1 LEU B 136 3044 2716 3164 -169 343 -179 C ATOM 3139 CD2 LEU B 136 110.853 0.595 49.342 1.00 14.04 C ANISOU 3139 CD2 LEU B 136 1827 1548 1959 -209 367 -196 C ATOM 3140 N LEU B 137 116.091 0.321 50.624 1.00 31.38 N ANISOU 3140 N LEU B 137 4016 3888 4020 -196 313 -168 N ATOM 3141 CA LEU B 137 117.089 0.163 51.678 1.00 22.51 C ANISOU 3141 CA LEU B 137 2901 2797 2856 -203 302 -155 C ATOM 3142 C LEU B 137 117.344 1.479 52.402 1.00 30.38 C ANISOU 3142 C LEU B 137 3893 3815 3835 -240 317 -165 C ATOM 3143 O LEU B 137 117.635 1.494 53.598 1.00 25.70 O ANISOU 3143 O LEU B 137 3316 3235 3213 -263 321 -158 O ATOM 3144 CB LEU B 137 118.395 -0.385 51.110 1.00 17.28 C ANISOU 3144 CB LEU B 137 2223 2165 2176 -170 273 -141 C ATOM 3145 CG LEU B 137 118.360 -1.877 50.790 1.00 27.38 C ANISOU 3145 CG LEU B 137 3512 3429 3463 -136 256 -127 C ATOM 3146 CD1 LEU B 137 119.523 -2.254 49.894 1.00 23.30 C ANISOU 3146 CD1 LEU B 137 2974 2937 2940 -101 232 -120 C ATOM 3147 CD2 LEU B 137 118.382 -2.689 52.078 1.00 25.18 C ANISOU 3147 CD2 LEU B 137 3257 3147 3162 -145 252 -111 C ATOM 3148 N VAL B 138 117.222 2.583 51.674 1.00 26.72 N ANISOU 3148 N VAL B 138 3409 3353 3390 -248 325 -180 N ATOM 3149 CA VAL B 138 117.481 3.896 52.248 1.00 30.27 C ANISOU 3149 CA VAL B 138 3853 3823 3826 -282 339 -191 C ATOM 3150 C VAL B 138 116.269 4.480 52.968 1.00 26.37 C ANISOU 3150 C VAL B 138 3372 3297 3350 -317 373 -208 C ATOM 3151 O VAL B 138 116.395 5.017 54.069 1.00 48.93 O ANISOU 3151 O VAL B 138 6244 6165 6184 -341 379 -211 O ATOM 3152 CB VAL B 138 117.946 4.888 51.160 1.00 29.31 C ANISOU 3152 CB VAL B 138 3703 3719 3715 -277 331 -200 C ATOM 3153 CG1 VAL B 138 117.907 6.316 51.674 1.00 13.96 C ANISOU 3153 CG1 VAL B 138 1755 1783 1766 -309 344 -214 C ATOM 3154 CG2 VAL B 138 119.345 4.529 50.684 1.00 21.76 C ANISOU 3154 CG2 VAL B 138 2732 2803 2733 -250 301 -185 C ATOM 3155 N PHE B 139 115.095 4.368 52.355 1.00 28.55 N ANISOU 3155 N PHE B 139 3648 3533 3666 -305 378 -217 N ATOM 3156 CA PHE B 139 113.908 5.019 52.900 1.00 28.62 C ANISOU 3156 CA PHE B 139 3671 3515 3689 -307 385 -231 C ATOM 3157 C PHE B 139 112.989 4.094 53.699 1.00 27.06 C ANISOU 3157 C PHE B 139 3497 3291 3494 -311 400 -229 C ATOM 3158 O PHE B 139 112.187 4.568 54.504 1.00 43.49 O ANISOU 3158 O PHE B 139 5589 5361 5573 -316 411 -240 O ATOM 3159 CB PHE B 139 113.118 5.688 51.773 1.00 31.38 C ANISOU 3159 CB PHE B 139 4003 3847 4073 -282 376 -240 C ATOM 3160 CG PHE B 139 113.848 6.828 51.117 1.00 29.46 C ANISOU 3160 CG PHE B 139 3741 3627 3827 -280 360 -244 C ATOM 3161 CD1 PHE B 139 113.982 8.046 51.764 1.00 25.25 C ANISOU 3161 CD1 PHE B 139 3210 3106 3279 -291 360 -253 C ATOM 3162 CD2 PHE B 139 114.403 6.682 49.856 1.00 32.28 C ANISOU 3162 CD2 PHE B 139 4079 3994 4194 -266 344 -238 C ATOM 3163 CE1 PHE B 139 114.655 9.098 51.165 1.00 35.32 C ANISOU 3163 CE1 PHE B 139 4469 4401 4550 -289 344 -255 C ATOM 3164 CE2 PHE B 139 115.076 7.731 49.251 1.00 35.66 C ANISOU 3164 CE2 PHE B 139 4490 4444 4617 -265 328 -240 C ATOM 3165 CZ PHE B 139 115.202 8.940 49.907 1.00 34.59 C ANISOU 3165 CZ PHE B 139 4358 4320 4467 -276 327 -248 C ATOM 3166 N LYS B 140 113.086 2.786 53.480 1.00 28.74 N ANISOU 3166 N LYS B 140 3717 3494 3710 -307 402 -215 N ATOM 3167 CA LYS B 140 112.287 1.839 54.260 1.00 31.41 C ANISOU 3167 CA LYS B 140 4080 3807 4047 -311 413 -210 C ATOM 3168 C LYS B 140 113.108 0.661 54.781 1.00 29.29 C ANISOU 3168 C LYS B 140 3828 3554 3748 -311 402 -189 C ATOM 3169 O LYS B 140 112.915 -0.471 54.340 1.00 36.75 O ANISOU 3169 O LYS B 140 4779 4483 4701 -283 386 -176 O ATOM 3170 CB LYS B 140 111.130 1.299 53.413 1.00 32.63 C ANISOU 3170 CB LYS B 140 4230 3929 4238 -282 410 -209 C ATOM 3171 CG LYS B 140 110.195 2.353 52.843 1.00 24.95 C ANISOU 3171 CG LYS B 140 3237 2955 3288 -263 408 -221 C ATOM 3172 CD LYS B 140 109.255 2.894 53.901 1.00 26.07 C ANISOU 3172 CD LYS B 140 3388 3094 3425 -271 424 -231 C ATOM 3173 CE LYS B 140 108.189 3.784 53.284 1.00 30.13 C ANISOU 3173 CE LYS B 140 3879 3603 3964 -249 423 -236 C ATOM 3174 NZ LYS B 140 107.204 4.257 54.296 1.00 32.84 N ANISOU 3174 NZ LYS B 140 4230 3941 4305 -256 442 -248 N ATOM 3175 N PRO B 141 114.024 0.920 55.731 1.00 34.33 N ANISOU 3175 N PRO B 141 4474 4225 4344 -331 397 -182 N ATOM 3176 CA PRO B 141 114.824 -0.170 56.308 1.00 39.27 C ANISOU 3176 CA PRO B 141 5115 4871 4936 -319 371 -158 C ATOM 3177 C PRO B 141 113.969 -1.253 56.971 1.00 40.82 C ANISOU 3177 C PRO B 141 5339 5038 5134 -323 377 -151 C ATOM 3178 O PRO B 141 114.312 -2.441 56.926 1.00 36.94 O ANISOU 3178 O PRO B 141 4856 4547 4634 -298 352 -132 O ATOM 3179 CB PRO B 141 115.699 0.550 57.344 1.00 23.49 C ANISOU 3179 CB PRO B 141 3122 2907 2896 -351 373 -156 C ATOM 3180 CG PRO B 141 114.987 1.823 57.634 1.00 35.90 C ANISOU 3180 CG PRO B 141 4692 4468 4481 -387 408 -181 C ATOM 3181 CD PRO B 141 114.312 2.213 56.363 1.00 28.07 C ANISOU 3181 CD PRO B 141 3677 3452 3535 -367 415 -196 C ATOM 3182 N ALA B 142 112.863 -0.832 57.574 1.00 43.00 N ANISOU 3182 N ALA B 142 5628 5288 5423 -355 410 -168 N ATOM 3183 CA ALA B 142 111.991 -1.743 58.302 1.00 33.90 C ANISOU 3183 CA ALA B 142 4502 4108 4271 -366 420 -163 C ATOM 3184 C ALA B 142 111.358 -2.777 57.379 1.00 38.71 C ANISOU 3184 C ALA B 142 5109 4687 4911 -329 407 -156 C ATOM 3185 O ALA B 142 111.172 -3.931 57.768 1.00 41.11 O ANISOU 3185 O ALA B 142 5433 4980 5206 -321 395 -141 O ATOM 3186 CB ALA B 142 110.917 -0.962 59.039 1.00 29.47 C ANISOU 3186 CB ALA B 142 3947 3534 3716 -387 445 -187 C ATOM 3187 N TRP B 143 111.044 -2.368 56.153 1.00 34.25 N ANISOU 3187 N TRP B 143 4522 4109 4382 -308 409 -166 N ATOM 3188 CA TRP B 143 110.485 -3.290 55.168 1.00 30.47 C ANISOU 3188 CA TRP B 143 4042 3602 3933 -274 396 -159 C ATOM 3189 C TRP B 143 111.528 -4.309 54.760 1.00 38.15 C ANISOU 3189 C TRP B 143 5014 4595 4887 -237 359 -138 C ATOM 3190 O TRP B 143 111.241 -5.497 54.635 1.00 36.95 O ANISOU 3190 O TRP B 143 4875 4425 4739 -216 346 -125 O ATOM 3191 CB TRP B 143 109.994 -2.548 53.921 1.00 35.19 C ANISOU 3191 CB TRP B 143 4615 4183 4572 -263 404 -173 C ATOM 3192 CG TRP B 143 108.726 -1.780 54.101 1.00 35.19 C ANISOU 3192 CG TRP B 143 4600 4187 4582 -257 413 -183 C ATOM 3193 CD1 TRP B 143 108.033 -1.600 55.260 1.00 37.57 C ANISOU 3193 CD1 TRP B 143 4914 4491 4870 -273 428 -190 C ATOM 3194 CD2 TRP B 143 107.994 -1.085 53.082 1.00 46.86 C ANISOU 3194 CD2 TRP B 143 6049 5668 6086 -234 407 -187 C ATOM 3195 NE1 TRP B 143 106.917 -0.834 55.029 1.00 34.83 N ANISOU 3195 NE1 TRP B 143 4546 4145 4542 -260 434 -198 N ATOM 3196 CE2 TRP B 143 106.869 -0.505 53.700 1.00 35.94 C ANISOU 3196 CE2 TRP B 143 4661 4287 4706 -236 420 -195 C ATOM 3197 CE3 TRP B 143 108.182 -0.896 51.709 1.00 38.02 C ANISOU 3197 CE3 TRP B 143 4907 4550 4987 -213 391 -183 C ATOM 3198 CZ2 TRP B 143 105.935 0.251 52.993 1.00 37.05 C ANISOU 3198 CZ2 TRP B 143 4776 4431 4870 -218 416 -196 C ATOM 3199 CZ3 TRP B 143 107.254 -0.145 51.009 1.00 30.79 C ANISOU 3199 CZ3 TRP B 143 3968 3641 4091 -197 386 -183 C ATOM 3200 CH2 TRP B 143 106.145 0.419 51.652 1.00 33.72 C ANISOU 3200 CH2 TRP B 143 4335 4013 4465 -200 398 -189 C ATOM 3201 N CYS B 144 112.746 -3.826 54.548 1.00 35.46 N ANISOU 3201 N CYS B 144 4656 4292 4526 -229 344 -135 N ATOM 3202 CA CYS B 144 113.832 -4.678 54.096 1.00 30.16 C ANISOU 3202 CA CYS B 144 3978 3641 3840 -194 310 -117 C ATOM 3203 C CYS B 144 114.245 -5.703 55.142 1.00 33.70 C ANISOU 3203 C CYS B 144 4449 4098 4259 -195 293 -96 C ATOM 3204 O CYS B 144 114.632 -6.818 54.798 1.00 31.88 O ANISOU 3204 O CYS B 144 4221 3865 4029 -163 269 -80 O ATOM 3205 CB CYS B 144 115.037 -3.825 53.702 1.00 31.15 C ANISOU 3205 CB CYS B 144 4079 3806 3950 -189 300 -119 C ATOM 3206 SG CYS B 144 114.690 -2.621 52.401 1.00 42.78 S ANISOU 3206 SG CYS B 144 5525 5273 5456 -187 313 -141 S ATOM 3207 N GLN B 145 114.146 -5.338 56.419 1.00 37.04 N ANISOU 3207 N GLN B 145 4888 4528 4657 -235 307 -96 N ATOM 3208 CA GLN B 145 114.555 -6.259 57.478 1.00 30.01 C ANISOU 3208 CA GLN B 145 4020 3646 3737 -242 289 -75 C ATOM 3209 C GLN B 145 113.639 -7.478 57.527 1.00 35.50 C ANISOU 3209 C GLN B 145 4735 4306 4447 -231 286 -67 C ATOM 3210 O GLN B 145 114.070 -8.576 57.877 1.00 47.89 O ANISOU 3210 O GLN B 145 6315 5877 6002 -217 259 -45 O ATOM 3211 CB GLN B 145 114.571 -5.553 58.837 1.00 34.81 C ANISOU 3211 CB GLN B 145 4644 4269 4314 -293 306 -78 C ATOM 3212 CG GLN B 145 115.832 -5.811 59.665 1.00 46.65 C ANISOU 3212 CG GLN B 145 6148 5803 5773 -302 279 -55 C ATOM 3213 CD GLN B 145 115.875 -7.200 60.283 1.00 53.73 C ANISOU 3213 CD GLN B 145 7067 6692 6658 -296 255 -30 C ATOM 3214 OE1 GLN B 145 114.838 -7.780 60.605 1.00 43.60 O ANISOU 3214 OE1 GLN B 145 5804 5378 5383 -305 266 -33 O ATOM 3215 NE2 GLN B 145 117.080 -7.738 60.453 1.00 35.69 N ANISOU 3215 NE2 GLN B 145 4776 4432 4353 -281 220 -6 N ATOM 3216 N ARG B 146 112.380 -7.278 57.152 1.00 27.75 N ANISOU 3216 N ARG B 146 3757 3291 3495 -236 311 -84 N ATOM 3217 CA ARG B 146 111.371 -8.327 57.243 1.00 34.29 C ANISOU 3217 CA ARG B 146 4606 4084 4339 -230 312 -78 C ATOM 3218 C ARG B 146 111.110 -9.060 55.917 1.00 41.47 C ANISOU 3218 C ARG B 146 5506 4971 5279 -186 298 -75 C ATOM 3219 O ARG B 146 110.772 -10.245 55.920 1.00 50.35 O ANISOU 3219 O ARG B 146 6647 6076 6408 -169 283 -61 O ATOM 3220 CB ARG B 146 110.065 -7.723 57.780 1.00 30.57 C ANISOU 3220 CB ARG B 146 4146 3587 3881 -267 350 -96 C ATOM 3221 CG ARG B 146 108.872 -8.670 57.823 1.00 45.04 C ANISOU 3221 CG ARG B 146 5999 5381 5732 -264 355 -93 C ATOM 3222 CD ARG B 146 109.121 -9.867 58.726 1.00 52.29 C ANISOU 3222 CD ARG B 146 6943 6302 6622 -266 333 -71 C ATOM 3223 NE ARG B 146 107.964 -10.757 58.774 1.00 73.85 N ANISOU 3223 NE ARG B 146 9692 8996 9370 -264 338 -67 N ATOM 3224 CZ ARG B 146 107.728 -11.727 57.895 1.00 69.46 C ANISOU 3224 CZ ARG B 146 9137 8420 8835 -227 318 -57 C ATOM 3225 NH1 ARG B 146 108.570 -11.935 56.893 1.00 55.06 N ANISOU 3225 NH1 ARG B 146 7294 6608 7018 -188 295 -50 N ATOM 3226 NH2 ARG B 146 106.649 -12.488 58.018 1.00 71.46 N ANISOU 3226 NH2 ARG B 146 9409 8640 9102 -229 324 -53 N ATOM 3227 N PHE B 147 111.288 -8.377 54.788 1.00 29.53 N ANISOU 3227 N PHE B 147 3969 3463 3788 -169 301 -87 N ATOM 3228 CA PHE B 147 110.822 -8.923 53.510 1.00 39.78 C ANISOU 3228 CA PHE B 147 5261 4736 5118 -135 293 -88 C ATOM 3229 C PHE B 147 111.857 -9.042 52.384 1.00 38.75 C ANISOU 3229 C PHE B 147 5109 4625 4990 -99 271 -84 C ATOM 3230 O PHE B 147 111.538 -9.548 51.308 1.00 51.23 O ANISOU 3230 O PHE B 147 6686 6185 6594 -72 264 -85 O ATOM 3231 CB PHE B 147 109.647 -8.084 52.999 1.00 31.07 C ANISOU 3231 CB PHE B 147 4151 3606 4050 -151 322 -106 C ATOM 3232 CG PHE B 147 108.397 -8.237 53.813 1.00 33.97 C ANISOU 3232 CG PHE B 147 4540 3943 4426 -179 344 -110 C ATOM 3233 CD1 PHE B 147 107.675 -9.418 53.775 1.00 31.77 C ANISOU 3233 CD1 PHE B 147 4280 3635 4158 -165 337 -98 C ATOM 3234 CD2 PHE B 147 107.940 -7.202 54.612 1.00 36.81 C ANISOU 3234 CD2 PHE B 147 4900 4303 4785 -218 375 -125 C ATOM 3235 CE1 PHE B 147 106.524 -9.567 54.522 1.00 37.83 C ANISOU 3235 CE1 PHE B 147 5055 4394 4924 -183 348 -98 C ATOM 3236 CE2 PHE B 147 106.786 -7.344 55.359 1.00 30.63 C ANISOU 3236 CE2 PHE B 147 4120 3520 3999 -228 383 -125 C ATOM 3237 CZ PHE B 147 106.078 -8.528 55.315 1.00 36.99 C ANISOU 3237 CZ PHE B 147 4938 4306 4809 -211 369 -111 C ATOM 3238 N ARG B 148 113.085 -8.590 52.617 1.00 39.35 N ANISOU 3238 N ARG B 148 5171 4739 5041 -98 260 -81 N ATOM 3239 CA ARG B 148 114.098 -8.606 51.561 1.00 27.20 C ANISOU 3239 CA ARG B 148 3609 3221 3504 -66 242 -80 C ATOM 3240 C ARG B 148 114.811 -9.958 51.500 1.00 33.31 C ANISOU 3240 C ARG B 148 4389 3998 4270 -32 213 -61 C ATOM 3241 O ARG B 148 115.924 -10.110 52.009 1.00 39.08 O ANISOU 3241 O ARG B 148 5113 4758 4977 -27 195 -49 O ATOM 3242 CB ARG B 148 115.104 -7.472 51.772 1.00 29.84 C ANISOU 3242 CB ARG B 148 3924 3596 3819 -81 242 -85 C ATOM 3243 CG ARG B 148 116.037 -7.213 50.602 1.00 24.29 C ANISOU 3243 CG ARG B 148 3195 2915 3121 -53 229 -89 C ATOM 3244 CD ARG B 148 116.853 -5.950 50.835 1.00 29.94 C ANISOU 3244 CD ARG B 148 3891 3668 3818 -73 234 -96 C ATOM 3245 NE ARG B 148 117.879 -5.753 49.815 1.00 29.49 N ANISOU 3245 NE ARG B 148 3808 3636 3760 -48 219 -97 N ATOM 3246 CZ ARG B 148 119.130 -6.186 49.921 1.00 29.25 C ANISOU 3246 CZ ARG B 148 3768 3635 3711 -28 197 -84 C ATOM 3247 NH1 ARG B 148 119.516 -6.846 51.005 1.00 32.73 N ANISOU 3247 NH1 ARG B 148 4223 4082 4132 -31 185 -65 N ATOM 3248 NH2 ARG B 148 119.998 -5.960 48.944 1.00 36.92 N ANISOU 3248 NH2 ARG B 148 4715 4628 4685 -6 188 -88 N ATOM 3249 N GLY B 149 114.155 -10.937 50.881 1.00 28.17 N ANISOU 3249 N GLY B 149 3749 3316 3640 -9 208 -58 N ATOM 3250 CA GLY B 149 114.697 -12.280 50.771 1.00 21.70 C ANISOU 3250 CA GLY B 149 2936 2492 2818 24 182 -42 C ATOM 3251 C GLY B 149 115.126 -12.648 49.364 1.00 26.36 C ANISOU 3251 C GLY B 149 3510 3081 3426 61 173 -47 C ATOM 3252 O GLY B 149 114.759 -11.979 48.397 1.00 34.37 O ANISOU 3252 O GLY B 149 4513 4088 4456 60 186 -62 O ATOM 3253 N ALA B 150 115.905 -13.721 49.253 1.00 28.16 N ANISOU 3253 N ALA B 150 3738 3312 3651 93 150 -33 N ATOM 3254 CA ALA B 150 116.440 -14.163 47.967 1.00 25.92 C ANISOU 3254 CA ALA B 150 3439 3028 3382 130 141 -39 C ATOM 3255 C ALA B 150 115.364 -14.644 46.998 1.00 30.05 C ANISOU 3255 C ALA B 150 3976 3513 3930 140 149 -47 C ATOM 3256 O ALA B 150 115.493 -14.472 45.781 1.00 34.23 O ANISOU 3256 O ALA B 150 4492 4041 4472 155 153 -59 O ATOM 3257 CB ALA B 150 117.465 -15.268 48.186 1.00 18.57 C ANISOU 3257 CB ALA B 150 2506 2105 2445 160 116 -22 C ATOM 3258 N GLY B 151 114.302 -15.240 47.534 1.00 18.16 N ANISOU 3258 N GLY B 151 2495 1975 2429 130 152 -40 N ATOM 3259 CA GLY B 151 113.262 -15.804 46.694 1.00 23.52 C ANISOU 3259 CA GLY B 151 3189 2616 3131 139 157 -44 C ATOM 3260 C GLY B 151 112.472 -14.738 45.967 1.00 39.54 C ANISOU 3260 C GLY B 151 5211 4636 5176 118 178 -60 C ATOM 3261 O GLY B 151 112.146 -14.893 44.787 1.00 42.25 O ANISOU 3261 O GLY B 151 5554 4963 5538 131 179 -67 O ATOM 3262 N LEU B 152 112.207 -13.632 46.656 1.00 26.47 N ANISOU 3262 N LEU B 152 3549 2993 3515 85 193 -66 N ATOM 3263 CA LEU B 152 111.543 -12.498 46.032 1.00 29.82 C ANISOU 3263 CA LEU B 152 3963 3411 3957 64 212 -81 C ATOM 3264 C LEU B 152 112.423 -11.904 44.944 1.00 21.55 C ANISOU 3264 C LEU B 152 2890 2388 2910 76 208 -91 C ATOM 3265 O LEU B 152 111.937 -11.491 43.890 1.00 33.94 O ANISOU 3265 O LEU B 152 4454 3944 4499 73 214 -101 O ATOM 3266 CB LEU B 152 111.212 -11.428 47.074 1.00 26.99 C ANISOU 3266 CB LEU B 152 3602 3062 3592 27 230 -86 C ATOM 3267 CG LEU B 152 110.618 -10.138 46.510 1.00 25.35 C ANISOU 3267 CG LEU B 152 3379 2850 3404 3 249 -101 C ATOM 3268 CD1 LEU B 152 109.299 -10.425 45.813 1.00 22.09 C ANISOU 3268 CD1 LEU B 152 2965 2418 3009 0 243 -95 C ATOM 3269 CD2 LEU B 152 110.441 -9.096 47.600 1.00 21.86 C ANISOU 3269 CD2 LEU B 152 2933 2419 2952 -32 268 -108 C ATOM 3270 N ALA B 153 113.729 -11.893 45.193 1.00 18.20 N ANISOU 3270 N ALA B 153 2452 1998 2464 90 197 -89 N ATOM 3271 CA ALA B 153 114.663 -11.349 44.224 1.00 21.38 C ANISOU 3271 CA ALA B 153 2831 2429 2865 101 193 -99 C ATOM 3272 C ALA B 153 114.665 -12.199 42.958 1.00 29.30 C ANISOU 3272 C ALA B 153 3836 3414 3882 130 185 -102 C ATOM 3273 O ALA B 153 114.629 -11.671 41.841 1.00 20.59 O ANISOU 3273 O ALA B 153 2722 2313 2790 127 190 -114 O ATOM 3274 CB ALA B 153 116.058 -11.267 44.819 1.00 18.25 C ANISOU 3274 CB ALA B 153 2419 2073 2444 111 181 -93 C ATOM 3275 N TRP B 154 114.685 -13.518 43.135 1.00 27.36 N ANISOU 3275 N TRP B 154 3607 3152 3637 154 173 -91 N ATOM 3276 CA TRP B 154 114.647 -14.421 41.989 1.00 33.15 C ANISOU 3276 CA TRP B 154 4347 3866 4384 181 167 -94 C ATOM 3277 C TRP B 154 113.326 -14.325 41.228 1.00 33.39 C ANISOU 3277 C TRP B 154 4391 3860 4435 166 177 -99 C ATOM 3278 O TRP B 154 113.301 -14.430 39.997 1.00 22.90 O ANISOU 3278 O TRP B 154 3054 2539 3107 168 166 -104 O ATOM 3279 CB TRP B 154 114.899 -15.866 42.427 1.00 32.19 C ANISOU 3279 CB TRP B 154 4241 3730 4259 209 152 -80 C ATOM 3280 CG TRP B 154 116.357 -16.190 42.577 1.00 36.99 C ANISOU 3280 CG TRP B 154 4831 4369 4854 235 139 -77 C ATOM 3281 CD1 TRP B 154 117.017 -16.485 43.732 1.00 38.19 C ANISOU 3281 CD1 TRP B 154 4981 4537 4992 239 127 -62 C ATOM 3282 CD2 TRP B 154 117.338 -16.235 41.532 1.00 36.52 C ANISOU 3282 CD2 TRP B 154 4752 4327 4797 258 137 -88 C ATOM 3283 NE1 TRP B 154 118.346 -16.718 43.472 1.00 34.61 N ANISOU 3283 NE1 TRP B 154 4506 4110 4534 264 116 -62 N ATOM 3284 CE2 TRP B 154 118.569 -16.569 42.129 1.00 36.35 C ANISOU 3284 CE2 TRP B 154 4715 4332 4764 277 124 -79 C ATOM 3285 CE3 TRP B 154 117.293 -16.027 40.149 1.00 34.81 C ANISOU 3285 CE3 TRP B 154 4529 4107 4590 262 145 -105 C ATOM 3286 CZ2 TRP B 154 119.746 -16.701 41.391 1.00 40.73 C ANISOU 3286 CZ2 TRP B 154 5247 4909 5319 303 120 -87 C ATOM 3287 CZ3 TRP B 154 118.461 -16.158 39.419 1.00 30.12 C ANISOU 3287 CZ3 TRP B 154 3914 3536 3993 286 143 -114 C ATOM 3288 CH2 TRP B 154 119.671 -16.491 40.041 1.00 36.64 C ANISOU 3288 CH2 TRP B 154 4724 4387 4810 307 131 -106 C ATOM 3289 N ILE B 155 112.234 -14.102 41.955 1.00 27.90 N ANISOU 3289 N ILE B 155 3705 3154 3741 138 179 -91 N ATOM 3290 CA ILE B 155 110.934 -13.968 41.309 1.00 23.10 C ANISOU 3290 CA ILE B 155 3094 2547 3137 114 167 -86 C ATOM 3291 C ILE B 155 110.891 -12.700 40.461 1.00 29.37 C ANISOU 3291 C ILE B 155 3868 3357 3936 94 173 -96 C ATOM 3292 O ILE B 155 110.457 -12.732 39.305 1.00 30.81 O ANISOU 3292 O ILE B 155 4046 3543 4119 89 160 -95 O ATOM 3293 CB ILE B 155 109.785 -13.942 42.336 1.00 28.57 C ANISOU 3293 CB ILE B 155 3796 3230 3830 91 169 -76 C ATOM 3294 CG1 ILE B 155 109.610 -15.320 42.976 1.00 28.61 C ANISOU 3294 CG1 ILE B 155 3822 3218 3831 107 158 -65 C ATOM 3295 CG2 ILE B 155 108.485 -13.529 41.672 1.00 20.25 C ANISOU 3295 CG2 ILE B 155 2732 2183 2780 67 159 -72 C ATOM 3296 CD1 ILE B 155 108.555 -15.357 44.057 1.00 40.97 C ANISOU 3296 CD1 ILE B 155 5397 4775 5395 85 161 -56 C ATOM 3297 N LEU B 156 111.367 -11.592 41.024 1.00 21.32 N ANISOU 3297 N LEU B 156 2836 2345 2918 81 192 -106 N ATOM 3298 CA LEU B 156 111.412 -10.335 40.283 1.00 21.47 C ANISOU 3298 CA LEU B 156 2835 2380 2943 61 197 -115 C ATOM 3299 C LEU B 156 112.334 -10.423 39.064 1.00 27.39 C ANISOU 3299 C LEU B 156 3575 3141 3691 80 192 -125 C ATOM 3300 O LEU B 156 112.036 -9.856 38.005 1.00 19.49 O ANISOU 3300 O LEU B 156 2563 2147 2695 65 186 -127 O ATOM 3301 CB LEU B 156 111.866 -9.195 41.198 1.00 20.05 C ANISOU 3301 CB LEU B 156 2645 2208 2764 45 218 -127 C ATOM 3302 CG LEU B 156 110.929 -8.835 42.353 1.00 33.50 C ANISOU 3302 CG LEU B 156 4355 3905 4469 19 228 -120 C ATOM 3303 CD1 LEU B 156 111.607 -7.880 43.324 1.00 27.14 C ANISOU 3303 CD1 LEU B 156 3544 3111 3658 5 247 -132 C ATOM 3304 CD2 LEU B 156 109.641 -8.234 41.821 1.00 36.48 C ANISOU 3304 CD2 LEU B 156 4718 4288 4854 -4 220 -111 C ATOM 3305 N CYS B 157 113.443 -11.149 39.205 1.00 23.12 N ANISOU 3305 N CYS B 157 3037 2602 3144 112 194 -131 N ATOM 3306 CA CYS B 157 114.355 -11.330 38.079 1.00 29.85 C ANISOU 3306 CA CYS B 157 3879 3468 3993 132 190 -142 C ATOM 3307 C CYS B 157 113.704 -12.160 36.976 1.00 33.42 C ANISOU 3307 C CYS B 157 4343 3910 4445 134 172 -134 C ATOM 3308 O CYS B 157 113.878 -11.884 35.782 1.00 22.04 O ANISOU 3308 O CYS B 157 2893 2476 3004 129 169 -142 O ATOM 3309 CB CYS B 157 115.655 -11.995 38.534 1.00 23.25 C ANISOU 3309 CB CYS B 157 3037 2658 3140 164 182 -139 C ATOM 3310 SG CYS B 157 116.764 -10.913 39.464 1.00 28.45 S ANISOU 3310 SG CYS B 157 3669 3366 3776 153 182 -140 S ATOM 3311 N ALA B 158 112.932 -13.164 37.384 1.00 33.30 N ANISOU 3311 N ALA B 158 4346 3877 4428 138 160 -120 N ATOM 3312 CA ALA B 158 112.240 -14.012 36.426 1.00 28.64 C ANISOU 3312 CA ALA B 158 3767 3277 3837 138 142 -114 C ATOM 3313 C ALA B 158 111.179 -13.215 35.673 1.00 33.11 C ANISOU 3313 C ALA B 158 4328 3845 4406 105 138 -109 C ATOM 3314 O ALA B 158 111.030 -13.352 34.451 1.00 27.84 O ANISOU 3314 O ALA B 158 3662 3177 3737 102 129 -111 O ATOM 3315 CB ALA B 158 111.615 -15.207 37.130 1.00 23.01 C ANISOU 3315 CB ALA B 158 3072 2548 3122 147 130 -101 C ATOM 3316 N VAL B 159 110.459 -12.364 36.402 1.00 24.01 N ANISOU 3316 N VAL B 159 3170 2695 3258 82 143 -103 N ATOM 3317 CA VAL B 159 109.449 -11.514 35.781 1.00 28.00 C ANISOU 3317 CA VAL B 159 3666 3204 3767 53 138 -96 C ATOM 3318 C VAL B 159 110.104 -10.537 34.805 1.00 25.86 C ANISOU 3318 C VAL B 159 3379 2946 3501 44 145 -107 C ATOM 3319 O VAL B 159 109.574 -10.273 33.716 1.00 23.40 O ANISOU 3319 O VAL B 159 3065 2636 3190 29 135 -103 O ATOM 3320 CB VAL B 159 108.636 -10.732 36.844 1.00 26.65 C ANISOU 3320 CB VAL B 159 3487 3037 3601 32 146 -90 C ATOM 3321 CG1 VAL B 159 107.726 -9.701 36.187 1.00 21.93 C ANISOU 3321 CG1 VAL B 159 2875 2450 3009 7 141 -84 C ATOM 3322 CG2 VAL B 159 107.823 -11.692 37.699 1.00 33.72 C ANISOU 3322 CG2 VAL B 159 4399 3922 4493 38 138 -79 C ATOM 3323 N ALA B 160 111.287 -10.048 35.173 1.00 24.03 N ANISOU 3323 N ALA B 160 3136 2722 3270 52 160 -122 N ATOM 3324 CA ALA B 160 112.009 -9.121 34.312 1.00 22.47 C ANISOU 3324 CA ALA B 160 2922 2539 3077 44 166 -136 C ATOM 3325 C ALA B 160 112.425 -9.800 33.009 1.00 24.10 C ANISOU 3325 C ALA B 160 3135 2744 3278 56 159 -142 C ATOM 3326 O ALA B 160 112.248 -9.239 31.920 1.00 14.89 O ANISOU 3326 O ALA B 160 1962 1581 2116 37 155 -144 O ATOM 3327 CB ALA B 160 113.227 -8.564 35.035 1.00 14.07 C ANISOU 3327 CB ALA B 160 1844 1489 2012 54 182 -153 C ATOM 3328 N TRP B 161 112.958 -11.017 33.119 1.00 25.79 N ANISOU 3328 N TRP B 161 3362 2952 3484 87 157 -145 N ATOM 3329 CA TRP B 161 113.346 -11.766 31.925 1.00 27.53 C ANISOU 3329 CA TRP B 161 3591 3171 3699 100 152 -152 C ATOM 3330 C TRP B 161 112.143 -12.076 31.042 1.00 21.38 C ANISOU 3330 C TRP B 161 2825 2378 2921 80 137 -138 C ATOM 3331 O TRP B 161 112.237 -12.035 29.807 1.00 27.04 O ANISOU 3331 O TRP B 161 3543 3094 3637 72 135 -144 O ATOM 3332 CB TRP B 161 114.050 -13.071 32.304 1.00 18.37 C ANISOU 3332 CB TRP B 161 2441 2008 2532 138 150 -155 C ATOM 3333 CG TRP B 161 115.488 -12.906 32.674 1.00 24.96 C ANISOU 3333 CG TRP B 161 3259 2863 3363 163 164 -170 C ATOM 3334 CD1 TRP B 161 116.012 -12.890 33.932 1.00 26.80 C ANISOU 3334 CD1 TRP B 161 3485 3102 3595 179 170 -169 C ATOM 3335 CD2 TRP B 161 116.591 -12.738 31.776 1.00 25.08 C ANISOU 3335 CD2 TRP B 161 3259 2898 3373 174 172 -189 C ATOM 3336 NE1 TRP B 161 117.373 -12.719 33.875 1.00 29.90 N ANISOU 3336 NE1 TRP B 161 3857 3520 3984 201 181 -183 N ATOM 3337 CE2 TRP B 161 117.754 -12.623 32.563 1.00 31.95 C ANISOU 3337 CE2 TRP B 161 4111 3790 4240 199 181 -197 C ATOM 3338 CE3 TRP B 161 116.708 -12.671 30.385 1.00 26.97 C ANISOU 3338 CE3 TRP B 161 3499 3140 3610 164 173 -200 C ATOM 3339 CZ2 TRP B 161 119.018 -12.445 32.005 1.00 32.79 C ANISOU 3339 CZ2 TRP B 161 4194 3927 4336 213 187 -213 C ATOM 3340 CZ3 TRP B 161 117.964 -12.494 29.833 1.00 26.53 C ANISOU 3340 CZ3 TRP B 161 3424 3109 3546 178 183 -220 C ATOM 3341 CH2 TRP B 161 119.102 -12.384 30.642 1.00 30.14 C ANISOU 3341 CH2 TRP B 161 3860 3593 4000 204 191 -227 C ATOM 3342 N GLY B 162 111.008 -12.356 31.676 1.00 22.04 N ANISOU 3342 N GLY B 162 2917 2452 3005 72 126 -121 N ATOM 3343 CA GLY B 162 109.807 -12.701 30.937 1.00 30.39 C ANISOU 3343 CA GLY B 162 3985 3500 4060 57 108 -107 C ATOM 3344 C GLY B 162 109.287 -11.524 30.139 1.00 31.79 C ANISOU 3344 C GLY B 162 4151 3686 4242 27 106 -103 C ATOM 3345 O GLY B 162 108.992 -11.646 28.943 1.00 32.41 O ANISOU 3345 O GLY B 162 4235 3761 4317 16 96 -101 O ATOM 3346 N LEU B 163 109.188 -10.373 30.796 1.00 18.08 N ANISOU 3346 N LEU B 163 2397 1961 2512 12 114 -102 N ATOM 3347 CA LEU B 163 108.735 -9.174 30.110 1.00 27.26 C ANISOU 3347 CA LEU B 163 3544 3134 3679 -14 110 -98 C ATOM 3348 C LEU B 163 109.722 -8.742 29.028 1.00 18.07 C ANISOU 3348 C LEU B 163 2373 1975 2517 -20 116 -113 C ATOM 3349 O LEU B 163 109.318 -8.230 27.982 1.00 22.58 O ANISOU 3349 O LEU B 163 2941 2551 3087 -39 105 -108 O ATOM 3350 CB LEU B 163 108.511 -8.043 31.112 1.00 23.36 C ANISOU 3350 CB LEU B 163 3032 2652 3193 -26 118 -96 C ATOM 3351 CG LEU B 163 107.930 -6.743 30.563 1.00 20.78 C ANISOU 3351 CG LEU B 163 2689 2339 2869 -49 111 -89 C ATOM 3352 CD1 LEU B 163 106.785 -7.018 29.601 1.00 16.40 C ANISOU 3352 CD1 LEU B 163 2138 1776 2317 -58 102 -77 C ATOM 3353 CD2 LEU B 163 107.458 -5.889 31.716 1.00 18.78 C ANISOU 3353 CD2 LEU B 163 2419 2093 2622 -55 120 -86 C ATOM 3354 N ALA B 164 111.012 -8.972 29.268 1.00 19.93 N ANISOU 3354 N ALA B 164 2607 2213 2754 -2 131 -132 N ATOM 3355 CA ALA B 164 112.029 -8.591 28.296 1.00 22.43 C ANISOU 3355 CA ALA B 164 2914 2537 3070 -6 139 -152 C ATOM 3356 C ALA B 164 111.912 -9.432 27.027 1.00 26.54 C ANISOU 3356 C ALA B 164 3453 3048 3585 -5 132 -152 C ATOM 3357 O ALA B 164 111.906 -8.897 25.910 1.00 23.42 O ANISOU 3357 O ALA B 164 3054 2657 3189 -27 127 -156 O ATOM 3358 CB ALA B 164 113.419 -8.722 28.896 1.00 16.96 C ANISOU 3358 CB ALA B 164 2213 1855 2375 20 156 -174 C ATOM 3359 N LEU B 165 111.795 -10.748 27.200 1.00 25.43 N ANISOU 3359 N LEU B 165 3332 2894 3437 19 128 -149 N ATOM 3360 CA LEU B 165 111.624 -11.637 26.057 1.00 29.84 C ANISOU 3360 CA LEU B 165 3909 3440 3989 20 121 -149 C ATOM 3361 C LEU B 165 110.330 -11.307 25.325 1.00 35.09 C ANISOU 3361 C LEU B 165 4578 4100 4653 -9 101 -129 C ATOM 3362 O LEU B 165 110.271 -11.339 24.086 1.00 37.84 O ANISOU 3362 O LEU B 165 4933 4446 4998 -24 95 -131 O ATOM 3363 CB LEU B 165 111.615 -13.099 26.506 1.00 23.84 C ANISOU 3363 CB LEU B 165 3166 2668 3223 50 117 -147 C ATOM 3364 CG LEU B 165 112.936 -13.646 27.046 1.00 45.68 C ANISOU 3364 CG LEU B 165 5929 5441 5984 86 132 -165 C ATOM 3365 CD1 LEU B 165 112.716 -14.897 27.888 1.00 48.07 C ANISOU 3365 CD1 LEU B 165 6245 5735 6285 112 123 -156 C ATOM 3366 CD2 LEU B 165 113.882 -13.934 25.894 1.00 46.96 C ANISOU 3366 CD2 LEU B 165 6094 5609 6141 93 143 -186 C ATOM 3367 N LEU B 166 109.309 -10.948 26.099 1.00 32.08 N ANISOU 3367 N LEU B 166 4193 3722 4274 -16 90 -110 N ATOM 3368 CA LEU B 166 108.017 -10.614 25.522 1.00 21.14 C ANISOU 3368 CA LEU B 166 2811 2338 2885 -39 68 -90 C ATOM 3369 C LEU B 166 108.134 -9.391 24.622 1.00 31.57 C ANISOU 3369 C LEU B 166 4117 3670 4207 -64 66 -91 C ATOM 3370 O LEU B 166 107.586 -9.366 23.518 1.00 35.94 O ANISOU 3370 O LEU B 166 4675 4219 4760 -81 56 -84 O ATOM 3371 CB LEU B 166 106.983 -10.364 26.622 1.00 18.88 C ANISOU 3371 CB LEU B 166 2515 2051 2607 -41 72 -77 C ATOM 3372 CG LEU B 166 105.545 -10.109 26.165 1.00 26.49 C ANISOU 3372 CG LEU B 166 3475 3011 3579 -59 67 -62 C ATOM 3373 CD1 LEU B 166 104.900 -11.394 25.663 1.00 33.57 C ANISOU 3373 CD1 LEU B 166 4394 3890 4472 -55 58 -55 C ATOM 3374 CD2 LEU B 166 104.718 -9.486 27.282 1.00 26.62 C ANISOU 3374 CD2 LEU B 166 3476 3033 3606 -62 75 -55 C ATOM 3375 N LEU B 167 108.866 -8.383 25.086 1.00 21.79 N ANISOU 3375 N LEU B 167 2858 2446 2974 -67 78 -101 N ATOM 3376 CA LEU B 167 109.071 -7.183 24.286 1.00 27.93 C ANISOU 3376 CA LEU B 167 3622 3239 3751 -91 72 -101 C ATOM 3377 C LEU B 167 109.982 -7.422 23.081 1.00 36.83 C ANISOU 3377 C LEU B 167 4753 4364 4875 -98 77 -118 C ATOM 3378 O LEU B 167 109.880 -6.721 22.074 1.00 31.78 O ANISOU 3378 O LEU B 167 4111 3734 4230 -120 63 -112 O ATOM 3379 CB LEU B 167 109.635 -6.061 25.157 1.00 27.13 C ANISOU 3379 CB LEU B 167 3496 3154 3659 -92 85 -110 C ATOM 3380 CG LEU B 167 108.658 -5.544 26.214 1.00 25.36 C ANISOU 3380 CG LEU B 167 3264 2934 3438 -91 82 -95 C ATOM 3381 CD1 LEU B 167 109.280 -4.427 27.038 1.00 24.98 C ANISOU 3381 CD1 LEU B 167 3193 2901 3397 -94 93 -104 C ATOM 3382 CD2 LEU B 167 107.366 -5.081 25.553 1.00 15.36 C ANISOU 3382 CD2 LEU B 167 1992 1664 2180 -107 74 -80 C ATOM 3383 N THR B 168 110.876 -8.403 23.185 1.00 35.95 N ANISOU 3383 N THR B 168 4651 4243 4766 -78 97 -139 N ATOM 3384 CA THR B 168 111.812 -8.678 22.097 1.00 27.97 C ANISOU 3384 CA THR B 168 3645 3232 3749 -83 107 -162 C ATOM 3385 C THR B 168 111.222 -9.579 21.000 1.00 37.35 C ANISOU 3385 C THR B 168 4857 4405 4929 -89 94 -153 C ATOM 3386 O THR B 168 111.720 -9.586 19.871 1.00 36.47 O ANISOU 3386 O THR B 168 4750 4298 4811 -104 97 -166 O ATOM 3387 CB THR B 168 113.115 -9.312 22.642 1.00 24.25 C ANISOU 3387 CB THR B 168 3173 2763 3278 -53 133 -191 C ATOM 3388 OG1 THR B 168 113.622 -8.501 23.707 1.00 30.43 O ANISOU 3388 OG1 THR B 168 3934 3561 4068 -47 141 -199 O ATOM 3389 CG2 THR B 168 114.183 -9.416 21.559 1.00 23.46 C ANISOU 3389 CG2 THR B 168 3074 2672 3167 -58 146 -220 C ATOM 3390 N ILE B 169 110.146 -10.301 21.311 1.00 37.65 N ANISOU 3390 N ILE B 169 4909 4430 4967 -80 77 -131 N ATOM 3391 CA ILE B 169 109.577 -11.245 20.340 1.00 36.88 C ANISOU 3391 CA ILE B 169 4832 4318 4863 -83 63 -124 C ATOM 3392 C ILE B 169 109.211 -10.637 18.965 1.00 36.99 C ANISOU 3392 C ILE B 169 4844 4337 4873 -115 43 -114 C ATOM 3393 O ILE B 169 109.599 -11.196 17.926 1.00 30.39 O ANISOU 3393 O ILE B 169 4019 3495 4033 -121 49 -126 O ATOM 3394 CB ILE B 169 108.317 -11.945 20.921 1.00 29.03 C ANISOU 3394 CB ILE B 169 3847 3312 3870 -73 43 -101 C ATOM 3395 CG1 ILE B 169 108.717 -12.982 21.966 1.00 35.53 C ANISOU 3395 CG1 ILE B 169 4678 4127 4695 -41 57 -110 C ATOM 3396 CG2 ILE B 169 107.524 -12.623 19.819 1.00 36.08 C ANISOU 3396 CG2 ILE B 169 4752 4191 4765 -87 32 -91 C ATOM 3397 CD1 ILE B 169 107.538 -13.631 22.652 1.00 43.79 C ANISOU 3397 CD1 ILE B 169 5730 5164 5745 -34 46 -91 C ATOM 3398 N PRO B 170 108.482 -9.498 18.937 1.00 44.55 N ANISOU 3398 N PRO B 170 5787 5306 5833 -135 28 -95 N ATOM 3399 CA PRO B 170 108.164 -8.929 17.618 1.00 41.78 C ANISOU 3399 CA PRO B 170 5433 4959 5483 -163 14 -87 C ATOM 3400 C PRO B 170 109.406 -8.582 16.800 1.00 44.89 C ANISOU 3400 C PRO B 170 5822 5367 5868 -173 18 -106 C ATOM 3401 O PRO B 170 109.391 -8.697 15.575 1.00 48.78 O ANISOU 3401 O PRO B 170 6318 5859 6359 -190 12 -107 O ATOM 3402 CB PRO B 170 107.374 -7.660 17.961 1.00 45.66 C ANISOU 3402 CB PRO B 170 5910 5461 5979 -177 5 -70 C ATOM 3403 CG PRO B 170 107.775 -7.325 19.351 1.00 30.09 C ANISOU 3403 CG PRO B 170 3927 3498 4008 -160 21 -77 C ATOM 3404 CD PRO B 170 107.967 -8.641 20.024 1.00 39.09 C ANISOU 3404 CD PRO B 170 5081 4623 5147 -134 31 -85 C ATOM 3405 N SER B 171 110.471 -8.173 17.481 1.00 52.38 N ANISOU 3405 N SER B 171 6761 6329 6815 -165 41 -127 N ATOM 3406 CA SER B 171 111.710 -7.828 16.801 1.00 37.66 C ANISOU 3406 CA SER B 171 4889 4479 4941 -179 61 -155 C ATOM 3407 C SER B 171 112.344 -9.042 16.128 1.00 45.32 C ANISOU 3407 C SER B 171 5880 5436 5901 -174 83 -181 C ATOM 3408 O SER B 171 113.004 -8.919 15.096 1.00 48.68 O ANISOU 3408 O SER B 171 6309 5875 6314 -194 90 -198 O ATOM 3409 CB SER B 171 112.698 -7.200 17.781 1.00 41.80 C ANISOU 3409 CB SER B 171 5394 5020 5469 -171 83 -178 C ATOM 3410 OG SER B 171 113.898 -6.849 17.120 1.00 64.82 O ANISOU 3410 OG SER B 171 8300 7955 8372 -185 99 -207 O ATOM 3411 N ALA B 172 112.140 -10.215 16.717 1.00 40.53 N ANISOU 3411 N ALA B 172 5291 4808 5299 -147 93 -184 N ATOM 3412 CA ALA B 172 112.656 -11.446 16.138 1.00 31.90 C ANISOU 3412 CA ALA B 172 4220 3703 4196 -136 112 -205 C ATOM 3413 C ALA B 172 111.777 -11.914 14.984 1.00 46.97 C ANISOU 3413 C ALA B 172 6146 5601 6102 -155 93 -187 C ATOM 3414 O ALA B 172 112.282 -12.377 13.961 1.00 53.78 O ANISOU 3414 O ALA B 172 7022 6463 6949 -167 106 -205 O ATOM 3415 CB ALA B 172 112.763 -12.531 17.200 1.00 30.68 C ANISOU 3415 CB ALA B 172 4076 3533 4048 -94 125 -210 C ATOM 3416 N LEU B 173 110.463 -11.792 15.151 1.00 40.82 N ANISOU 3416 N LEU B 173 5360 4814 5334 -157 61 -153 N ATOM 3417 CA LEU B 173 109.528 -12.257 14.127 1.00 45.83 C ANISOU 3417 CA LEU B 173 6001 5439 5973 -171 39 -135 C ATOM 3418 C LEU B 173 109.580 -11.469 12.818 1.00 57.34 C ANISOU 3418 C LEU B 173 7448 6911 7426 -202 28 -132 C ATOM 3419 O LEU B 173 109.352 -12.025 11.745 1.00 47.12 O ANISOU 3419 O LEU B 173 6167 5611 6126 -216 30 -133 O ATOM 3420 CB LEU B 173 108.099 -12.223 14.669 1.00 35.16 C ANISOU 3420 CB LEU B 173 4641 4078 4639 -168 18 -105 C ATOM 3421 CG LEU B 173 107.769 -13.264 15.736 1.00 47.79 C ANISOU 3421 CG LEU B 173 6252 5663 6242 -139 22 -103 C ATOM 3422 CD1 LEU B 173 106.338 -13.102 16.223 1.00 46.86 C ANISOU 3422 CD1 LEU B 173 6128 5539 6138 -143 8 -77 C ATOM 3423 CD2 LEU B 173 107.998 -14.661 15.185 1.00 56.73 C ANISOU 3423 CD2 LEU B 173 7404 6780 7369 -128 32 -116 C ATOM 3424 N TYR B 174 109.881 -10.178 12.904 1.00 54.75 N ANISOU 3424 N TYR B 174 8086 7232 5484 -538 -464 -433 N ATOM 3425 CA TYR B 174 109.718 -9.295 11.751 1.00 49.63 C ANISOU 3425 CA TYR B 174 7461 6551 4845 -516 -492 -429 C ATOM 3426 C TYR B 174 111.023 -8.943 11.038 1.00 56.44 C ANISOU 3426 C TYR B 174 8367 7380 5698 -495 -475 -397 C ATOM 3427 O TYR B 174 111.057 -8.027 10.218 1.00 65.27 O ANISOU 3427 O TYR B 174 9499 8472 6828 -474 -494 -393 O ATOM 3428 CB TYR B 174 108.992 -8.020 12.181 1.00 65.45 C ANISOU 3428 CB TYR B 174 9415 8569 6886 -506 -516 -460 C ATOM 3429 CG TYR B 174 107.611 -8.293 12.734 1.00 88.27 C ANISOU 3429 CG TYR B 174 12264 11489 9786 -524 -538 -493 C ATOM 3430 CD1 TYR B 174 106.781 -9.237 12.144 1.00 88.97 C ANISOU 3430 CD1 TYR B 174 12376 11575 9854 -537 -554 -494 C ATOM 3431 CD2 TYR B 174 107.148 -7.627 13.858 1.00 87.79 C ANISOU 3431 CD2 TYR B 174 12143 11459 9753 -528 -541 -523 C ATOM 3432 CE1 TYR B 174 105.519 -9.497 12.651 1.00 91.60 C ANISOU 3432 CE1 TYR B 174 12672 11936 10197 -554 -574 -524 C ATOM 3433 CE2 TYR B 174 105.890 -7.880 14.372 1.00 89.38 C ANISOU 3433 CE2 TYR B 174 12307 11689 9963 -545 -561 -553 C ATOM 3434 CZ TYR B 174 105.080 -8.815 13.766 1.00 93.73 C ANISOU 3434 CZ TYR B 174 12881 12237 10494 -558 -577 -553 C ATOM 3435 OH TYR B 174 103.828 -9.065 14.281 1.00 95.22 O ANISOU 3435 OH TYR B 174 13033 12454 10692 -574 -596 -583 O ATOM 3436 N ARG B 175 112.100 -9.650 11.362 1.00 49.73 N ANISOU 3436 N ARG B 175 7537 6530 4828 -502 -439 -373 N ATOM 3437 CA ARG B 175 113.328 -9.510 10.590 1.00 48.93 C ANISOU 3437 CA ARG B 175 7483 6395 4713 -485 -422 -340 C ATOM 3438 C ARG B 175 113.433 -10.639 9.572 1.00 52.10 C ANISOU 3438 C ARG B 175 7942 6774 5080 -490 -421 -316 C ATOM 3439 O ARG B 175 113.215 -11.805 9.902 1.00 54.76 O ANISOU 3439 O ARG B 175 8283 7127 5396 -511 -410 -315 O ATOM 3440 CB ARG B 175 114.555 -9.501 11.499 1.00 43.00 C ANISOU 3440 CB ARG B 175 6722 5656 3962 -485 -383 -327 C ATOM 3441 CG ARG B 175 115.489 -8.332 11.237 1.00 48.64 C ANISOU 3441 CG ARG B 175 7442 6348 4691 -460 -377 -315 C ATOM 3442 CD ARG B 175 116.826 -8.526 11.922 1.00 38.88 C ANISOU 3442 CD ARG B 175 6209 5117 3447 -461 -336 -295 C ATOM 3443 NE ARG B 175 116.669 -9.059 13.271 1.00 44.59 N ANISOU 3443 NE ARG B 175 6890 5879 4173 -482 -316 -311 N ATOM 3444 CZ ARG B 175 116.402 -8.319 14.341 1.00 40.44 C ANISOU 3444 CZ ARG B 175 6308 5381 3676 -484 -316 -336 C ATOM 3445 NH1 ARG B 175 116.258 -7.005 14.227 1.00 51.91 N ANISOU 3445 NH1 ARG B 175 7741 6827 5157 -465 -335 -349 N ATOM 3446 NH2 ARG B 175 116.277 -8.893 15.527 1.00 44.65 N ANISOU 3446 NH2 ARG B 175 6806 5949 4209 -504 -298 -349 N ATOM 3447 N VAL B 176 113.779 -10.294 8.337 1.00 65.92 N ANISOU 3447 N VAL B 176 9737 8487 6823 -472 -432 -296 N ATOM 3448 CA VAL B 176 113.872 -11.287 7.276 1.00 60.64 C ANISOU 3448 CA VAL B 176 9125 7795 6122 -475 -434 -272 C ATOM 3449 C VAL B 176 115.166 -11.169 6.479 1.00 52.55 C ANISOU 3449 C VAL B 176 8149 6735 5081 -458 -416 -237 C ATOM 3450 O VAL B 176 115.847 -10.135 6.499 1.00 56.00 O ANISOU 3450 O VAL B 176 8580 7161 5535 -439 -411 -233 O ATOM 3451 CB VAL B 176 112.693 -11.182 6.290 1.00 36.34 C ANISOU 3451 CB VAL B 176 6059 4703 3046 -472 -474 -284 C ATOM 3452 CG1 VAL B 176 111.366 -11.343 7.017 1.00 54.50 C ANISOU 3452 CG1 VAL B 176 8312 7035 5359 -489 -493 -318 C ATOM 3453 CG2 VAL B 176 112.747 -9.857 5.554 1.00 54.16 C ANISOU 3453 CG2 VAL B 176 8321 6935 5324 -446 -496 -284 C ATOM 3454 N VAL B 177 115.500 -12.259 5.798 1.00 41.96 N ANISOU 3454 N VAL B 177 6856 5378 3708 -465 -405 -214 N ATOM 3455 CA VAL B 177 116.618 -12.294 4.870 1.00 50.09 C ANISOU 3455 CA VAL B 177 7940 6373 4719 -449 -391 -180 C ATOM 3456 C VAL B 177 116.131 -12.035 3.445 1.00 43.97 C ANISOU 3456 C VAL B 177 7202 5565 3939 -436 -423 -173 C ATOM 3457 O VAL B 177 115.294 -12.774 2.925 1.00 60.28 O ANISOU 3457 O VAL B 177 9284 7629 5991 -447 -441 -177 O ATOM 3458 CB VAL B 177 117.348 -13.653 4.940 1.00 40.62 C ANISOU 3458 CB VAL B 177 6774 5174 3486 -464 -360 -156 C ATOM 3459 CG1 VAL B 177 118.194 -13.877 3.707 1.00 45.77 C ANISOU 3459 CG1 VAL B 177 7488 5787 4115 -450 -354 -122 C ATOM 3460 CG2 VAL B 177 118.192 -13.739 6.201 1.00 41.79 C ANISOU 3460 CG2 VAL B 177 6894 5346 3638 -472 -324 -154 C ATOM 3461 N ARG B 178 116.657 -10.988 2.814 1.00 56.97 N ANISOU 3461 N ARG B 178 8863 7186 5597 -412 -431 -163 N ATOM 3462 CA ARG B 178 116.278 -10.651 1.445 1.00 52.64 C ANISOU 3462 CA ARG B 178 8350 6605 5046 -398 -460 -156 C ATOM 3463 C ARG B 178 117.486 -10.634 0.515 1.00 59.05 C ANISOU 3463 C ARG B 178 9216 7381 5838 -382 -445 -120 C ATOM 3464 O ARG B 178 118.600 -10.307 0.929 1.00 53.37 O ANISOU 3464 O ARG B 178 8496 6661 5122 -374 -418 -106 O ATOM 3465 CB ARG B 178 115.566 -9.296 1.397 1.00 52.15 C ANISOU 3465 CB ARG B 178 8255 6543 5018 -383 -492 -179 C ATOM 3466 CG ARG B 178 116.410 -8.127 1.886 1.00 63.27 C ANISOU 3466 CG ARG B 178 9640 7950 6448 -367 -479 -178 C ATOM 3467 CD ARG B 178 115.592 -6.848 1.961 1.00 95.78 C ANISOU 3467 CD ARG B 178 13719 12072 10601 -355 -510 -205 C ATOM 3468 NE ARG B 178 116.314 -5.765 2.626 1.00116.59 N ANISOU 3468 NE ARG B 178 16327 14713 13261 -341 -497 -208 N ATOM 3469 CZ ARG B 178 116.884 -4.743 1.995 1.00102.00 C ANISOU 3469 CZ ARG B 178 14494 12839 11423 -318 -504 -197 C ATOM 3470 NH1 ARG B 178 116.817 -4.655 0.674 1.00 99.76 N ANISOU 3470 NH1 ARG B 178 14254 12521 11128 -306 -524 -181 N ATOM 3471 NH2 ARG B 178 117.517 -3.805 2.686 1.00 84.28 N ANISOU 3471 NH2 ARG B 178 12220 10602 9200 -308 -491 -200 N ATOM 3472 N GLU B 179 117.253 -10.996 -0.743 1.00 71.65 N ANISOU 3472 N GLU B 179 10858 8949 7416 -377 -463 -106 N ATOM 3473 CA GLU B 179 118.304 -11.009 -1.753 1.00 62.11 C ANISOU 3473 CA GLU B 179 9704 7706 6189 -362 -452 -73 C ATOM 3474 C GLU B 179 118.235 -9.779 -2.658 1.00 58.58 C ANISOU 3474 C GLU B 179 9268 7232 5760 -338 -478 -72 C ATOM 3475 O GLU B 179 117.165 -9.418 -3.148 1.00 84.26 O ANISOU 3475 O GLU B 179 12512 10480 9024 -336 -513 -89 O ATOM 3476 CB GLU B 179 118.206 -12.288 -2.588 1.00 65.91 C ANISOU 3476 CB GLU B 179 10234 8172 6636 -373 -451 -54 C ATOM 3477 CG GLU B 179 119.302 -12.455 -3.624 1.00 77.77 C ANISOU 3477 CG GLU B 179 11795 9639 8116 -359 -438 -19 C ATOM 3478 CD GLU B 179 119.287 -13.828 -4.270 1.00 85.06 C ANISOU 3478 CD GLU B 179 12763 10552 9003 -372 -432 -1 C ATOM 3479 OE1 GLU B 179 118.423 -14.651 -3.899 1.00 91.98 O ANISOU 3479 OE1 GLU B 179 13626 11449 9874 -391 -438 -16 O ATOM 3480 OE2 GLU B 179 120.141 -14.084 -5.144 1.00 88.47 O ANISOU 3480 OE2 GLU B 179 13245 10956 9415 -362 -421 28 O ATOM 3481 N GLU B 180 119.383 -9.146 -2.883 1.00 63.83 N ANISOU 3481 N GLU B 180 9950 7878 6426 -321 -462 -52 N ATOM 3482 CA GLU B 180 119.475 -8.007 -3.794 1.00 74.57 C ANISOU 3482 CA GLU B 180 11325 9209 7801 -297 -484 -47 C ATOM 3483 C GLU B 180 120.527 -8.283 -4.862 1.00 66.11 C ANISOU 3483 C GLU B 180 10314 8103 6704 -285 -471 -11 C ATOM 3484 O GLU B 180 121.423 -9.097 -4.651 1.00 64.00 O ANISOU 3484 O GLU B 180 10067 7835 6413 -292 -439 10 O ATOM 3485 CB GLU B 180 119.803 -6.720 -3.035 1.00 74.12 C ANISOU 3485 CB GLU B 180 11225 9162 7775 -284 -481 -60 C ATOM 3486 CG GLU B 180 118.632 -6.146 -2.252 1.00 82.89 C ANISOU 3486 CG GLU B 180 12278 10301 8916 -290 -504 -97 C ATOM 3487 CD GLU B 180 118.876 -4.716 -1.814 1.00101.32 C ANISOU 3487 CD GLU B 180 14578 12638 11283 -273 -509 -108 C ATOM 3488 OE1 GLU B 180 120.031 -4.252 -1.912 1.00102.15 O ANISOU 3488 OE1 GLU B 180 14698 12727 11387 -259 -489 -88 O ATOM 3489 OE2 GLU B 180 117.911 -4.052 -1.377 1.00110.15 O ANISOU 3489 OE2 GLU B 180 15652 13772 12427 -274 -532 -138 O ATOM 3490 N TYR B 181 120.414 -7.613 -6.007 1.00 74.52 N ANISOU 3490 N TYR B 181 11406 9137 7772 -268 -496 -3 N ATOM 3491 CA TYR B 181 121.237 -7.956 -7.166 1.00 76.30 C ANISOU 3491 CA TYR B 181 11692 9328 7972 -258 -489 30 C ATOM 3492 C TYR B 181 122.116 -6.832 -7.709 1.00 78.06 C ANISOU 3492 C TYR B 181 11931 9525 8205 -233 -488 46 C ATOM 3493 O TYR B 181 122.915 -7.058 -8.618 1.00 70.13 O ANISOU 3493 O TYR B 181 10975 8492 7179 -224 -480 74 O ATOM 3494 CB TYR B 181 120.341 -8.468 -8.295 1.00 61.74 C ANISOU 3494 CB TYR B 181 9880 7466 6112 -260 -518 31 C ATOM 3495 CG TYR B 181 119.489 -9.644 -7.893 1.00 64.52 C ANISOU 3495 CG TYR B 181 10223 7841 6452 -284 -519 18 C ATOM 3496 CD1 TYR B 181 120.063 -10.876 -7.618 1.00 60.71 C ANISOU 3496 CD1 TYR B 181 9761 7365 5941 -299 -489 34 C ATOM 3497 CD2 TYR B 181 118.111 -9.524 -7.786 1.00 58.35 C ANISOU 3497 CD2 TYR B 181 9411 7073 5685 -292 -550 -11 C ATOM 3498 CE1 TYR B 181 119.290 -11.957 -7.247 1.00 64.83 C ANISOU 3498 CE1 TYR B 181 10274 7908 6450 -322 -490 23 C ATOM 3499 CE2 TYR B 181 117.330 -10.600 -7.416 1.00 72.00 C ANISOU 3499 CE2 TYR B 181 11131 8823 7401 -314 -551 -23 C ATOM 3500 CZ TYR B 181 117.924 -11.814 -7.147 1.00 70.39 C ANISOU 3500 CZ TYR B 181 10949 8627 7170 -329 -521 -6 C ATOM 3501 OH TYR B 181 117.149 -12.888 -6.778 1.00 77.16 O ANISOU 3501 OH TYR B 181 11798 9505 8015 -351 -522 -17 O ATOM 3502 N PHE B 182 121.980 -5.627 -7.167 1.00 85.18 N ANISOU 3502 N PHE B 182 12791 10436 9139 -222 -498 27 N ATOM 3503 CA PHE B 182 122.748 -4.496 -7.681 1.00 79.53 C ANISOU 3503 CA PHE B 182 12088 9695 8434 -199 -500 41 C ATOM 3504 C PHE B 182 123.451 -3.702 -6.585 1.00 71.26 C ANISOU 3504 C PHE B 182 11001 8665 7409 -193 -479 35 C ATOM 3505 O PHE B 182 122.967 -2.645 -6.178 1.00 85.23 O ANISOU 3505 O PHE B 182 12731 10444 9209 -185 -497 12 O ATOM 3506 CB PHE B 182 121.844 -3.569 -8.495 1.00 79.05 C ANISOU 3506 CB PHE B 182 12025 9618 8393 -186 -542 27 C ATOM 3507 CG PHE B 182 121.121 -4.262 -9.612 1.00 71.97 C ANISOU 3507 CG PHE B 182 11165 8703 7476 -190 -565 32 C ATOM 3508 CD1 PHE B 182 121.786 -4.611 -10.776 1.00 73.22 C ANISOU 3508 CD1 PHE B 182 11382 8829 7609 -182 -561 62 C ATOM 3509 CD2 PHE B 182 119.777 -4.569 -9.495 1.00 78.27 C ANISOU 3509 CD2 PHE B 182 11941 9517 8281 -203 -590 7 C ATOM 3510 CE1 PHE B 182 121.120 -5.254 -11.804 1.00 66.12 C ANISOU 3510 CE1 PHE B 182 10517 7913 6692 -186 -582 67 C ATOM 3511 CE2 PHE B 182 119.107 -5.210 -10.517 1.00 69.88 C ANISOU 3511 CE2 PHE B 182 10914 8438 7200 -207 -611 12 C ATOM 3512 CZ PHE B 182 119.778 -5.553 -11.674 1.00 66.10 C ANISOU 3512 CZ PHE B 182 10492 7927 6696 -199 -607 42 C ATOM 3513 N PRO B 183 124.599 -4.202 -6.101 1.00 64.23 N ANISOU 3513 N PRO B 183 10123 7779 6504 -196 -441 54 N ATOM 3514 CA PRO B 183 125.261 -5.463 -6.457 1.00 69.56 C ANISOU 3514 CA PRO B 183 10842 8445 7142 -206 -416 81 C ATOM 3515 C PRO B 183 124.612 -6.650 -5.763 1.00 70.89 C ANISOU 3515 C PRO B 183 10995 8641 7299 -231 -409 68 C ATOM 3516 O PRO B 183 123.795 -6.432 -4.867 1.00 77.28 O ANISOU 3516 O PRO B 183 11754 9479 8129 -241 -418 39 O ATOM 3517 CB PRO B 183 126.687 -5.249 -5.963 1.00 75.96 C ANISOU 3517 CB PRO B 183 11657 9254 7950 -199 -380 101 C ATOM 3518 CG PRO B 183 126.509 -4.407 -4.754 1.00 68.90 C ANISOU 3518 CG PRO B 183 10704 8388 7088 -199 -378 76 C ATOM 3519 CD PRO B 183 125.338 -3.492 -5.042 1.00 68.86 C ANISOU 3519 CD PRO B 183 10673 8382 7109 -191 -418 50 C ATOM 3520 N PRO B 184 124.937 -7.884 -6.184 1.00 72.91 N ANISOU 3520 N PRO B 184 11291 8889 7521 -242 -393 88 N ATOM 3521 CA PRO B 184 124.357 -8.998 -5.430 1.00 73.44 C ANISOU 3521 CA PRO B 184 11340 8985 7578 -267 -384 76 C ATOM 3522 C PRO B 184 124.798 -8.970 -3.971 1.00 68.40 C ANISOU 3522 C PRO B 184 10658 8378 6952 -276 -356 66 C ATOM 3523 O PRO B 184 125.961 -8.683 -3.678 1.00 61.70 O ANISOU 3523 O PRO B 184 9816 7526 6103 -267 -329 82 O ATOM 3524 CB PRO B 184 124.895 -10.240 -6.153 1.00 70.36 C ANISOU 3524 CB PRO B 184 11005 8578 7151 -274 -368 104 C ATOM 3525 CG PRO B 184 126.032 -9.749 -7.003 1.00 53.33 C ANISOU 3525 CG PRO B 184 8890 6388 4985 -253 -359 133 C ATOM 3526 CD PRO B 184 125.691 -8.341 -7.362 1.00 66.45 C ANISOU 3526 CD PRO B 184 10535 8038 6676 -234 -386 121 C ATOM 3527 N LYS B 185 123.868 -9.282 -3.074 1.00 60.61 N ANISOU 3527 N LYS B 185 9630 7424 5976 -293 -362 39 N ATOM 3528 CA LYS B 185 124.115 -9.233 -1.638 1.00 52.92 C ANISOU 3528 CA LYS B 185 8608 6483 5015 -303 -338 25 C ATOM 3529 C LYS B 185 122.919 -9.832 -0.912 1.00 54.15 C ANISOU 3529 C LYS B 185 8728 6671 5177 -325 -349 -3 C ATOM 3530 O LYS B 185 121.800 -9.799 -1.422 1.00 43.39 O ANISOU 3530 O LYS B 185 7363 5305 3818 -327 -381 -18 O ATOM 3531 CB LYS B 185 124.361 -7.793 -1.174 1.00 61.80 C ANISOU 3531 CB LYS B 185 9698 7611 6173 -286 -342 14 C ATOM 3532 CG LYS B 185 124.918 -7.664 0.238 1.00 38.42 C ANISOU 3532 CG LYS B 185 6694 4679 3224 -293 -312 6 C ATOM 3533 CD LYS B 185 126.315 -7.066 0.226 1.00 35.06 C ANISOU 3533 CD LYS B 185 6284 4238 2800 -277 -287 29 C ATOM 3534 CE LYS B 185 126.313 -5.668 -0.371 1.00 41.15 C ANISOU 3534 CE LYS B 185 7053 4988 3593 -253 -310 26 C ATOM 3535 NZ LYS B 185 127.691 -5.119 -0.482 1.00 53.20 N ANISOU 3535 NZ LYS B 185 8599 6498 5119 -236 -287 50 N ATOM 3536 N VAL B 186 123.154 -10.374 0.278 1.00 54.19 N ANISOU 3536 N VAL B 186 8704 6705 5180 -341 -323 -9 N ATOM 3537 CA VAL B 186 122.078 -10.935 1.086 1.00 58.25 C ANISOU 3537 CA VAL B 186 9181 7253 5700 -362 -331 -36 C ATOM 3538 C VAL B 186 121.936 -10.159 2.392 1.00 56.05 C ANISOU 3538 C VAL B 186 8841 7005 5452 -364 -325 -61 C ATOM 3539 O VAL B 186 122.783 -10.257 3.280 1.00 43.86 O ANISOU 3539 O VAL B 186 7282 5476 3908 -368 -293 -55 O ATOM 3540 CB VAL B 186 122.319 -12.422 1.387 1.00 53.42 C ANISOU 3540 CB VAL B 186 8587 6652 5058 -384 -306 -24 C ATOM 3541 CG1 VAL B 186 121.245 -12.949 2.305 1.00 48.72 C ANISOU 3541 CG1 VAL B 186 7949 6092 4469 -406 -313 -52 C ATOM 3542 CG2 VAL B 186 122.359 -13.225 0.094 1.00 41.96 C ANISOU 3542 CG2 VAL B 186 7195 5171 3576 -383 -313 -1 C ATOM 3543 N LEU B 187 120.864 -9.382 2.500 1.00 55.14 N ANISOU 3543 N LEU B 187 8690 6899 5363 -361 -356 -89 N ATOM 3544 CA LEU B 187 120.677 -8.501 3.647 1.00 49.37 C ANISOU 3544 CA LEU B 187 7900 6195 4663 -361 -355 -114 C ATOM 3545 C LEU B 187 119.724 -9.066 4.696 1.00 47.22 C ANISOU 3545 C LEU B 187 7583 5961 4397 -384 -357 -142 C ATOM 3546 O LEU B 187 118.660 -9.592 4.371 1.00 36.20 O ANISOU 3546 O LEU B 187 6188 4569 2995 -395 -380 -154 O ATOM 3547 CB LEU B 187 120.174 -7.134 3.178 1.00 60.84 C ANISOU 3547 CB LEU B 187 9337 7635 6144 -341 -387 -128 C ATOM 3548 CG LEU B 187 121.194 -6.262 2.443 1.00 63.94 C ANISOU 3548 CG LEU B 187 9759 7995 6539 -316 -383 -106 C ATOM 3549 CD1 LEU B 187 120.524 -5.042 1.832 1.00 54.25 C ANISOU 3549 CD1 LEU B 187 8522 6754 5337 -299 -420 -120 C ATOM 3550 CD2 LEU B 187 122.310 -5.841 3.385 1.00 57.65 C ANISOU 3550 CD2 LEU B 187 8942 7210 5752 -312 -350 -99 C ATOM 3551 N CYS B 188 120.121 -8.950 5.959 1.00 55.76 N ANISOU 3551 N CYS B 188 8625 7070 5490 -391 -333 -151 N ATOM 3552 CA CYS B 188 119.248 -9.278 7.077 1.00 47.80 C ANISOU 3552 CA CYS B 188 7567 6101 4494 -411 -335 -180 C ATOM 3553 C CYS B 188 118.659 -7.989 7.632 1.00 45.03 C ANISOU 3553 C CYS B 188 7165 5765 4181 -402 -355 -208 C ATOM 3554 O CYS B 188 119.385 -7.166 8.190 1.00 41.99 O ANISOU 3554 O CYS B 188 6759 5384 3813 -391 -340 -207 O ATOM 3555 CB CYS B 188 120.014 -10.035 8.164 1.00 43.72 C ANISOU 3555 CB CYS B 188 7038 5608 3966 -427 -296 -172 C ATOM 3556 SG CYS B 188 119.006 -10.565 9.574 1.00 53.43 S ANISOU 3556 SG CYS B 188 8208 6885 5206 -454 -295 -206 S ATOM 3557 N GLY B 189 117.353 -7.800 7.478 1.00 42.15 N ANISOU 3557 N GLY B 189 6778 5407 3828 -406 -389 -234 N ATOM 3558 CA GLY B 189 116.755 -6.554 7.921 1.00 45.21 C ANISOU 3558 CA GLY B 189 7118 5807 4252 -397 -410 -261 C ATOM 3559 C GLY B 189 115.278 -6.603 8.243 1.00 54.56 C ANISOU 3559 C GLY B 189 8266 7015 5450 -410 -439 -294 C ATOM 3560 O GLY B 189 114.582 -7.558 7.903 1.00 58.84 O ANISOU 3560 O GLY B 189 8824 7560 5974 -424 -449 -296 O ATOM 3561 N VAL B 190 114.800 -5.560 8.913 1.00 62.27 N ANISOU 3561 N VAL B 190 9192 8009 6460 -404 -453 -321 N ATOM 3562 CA VAL B 190 113.392 -5.461 9.265 1.00 78.20 C ANISOU 3562 CA VAL B 190 11170 10049 8493 -415 -481 -355 C ATOM 3563 C VAL B 190 112.536 -5.336 8.010 1.00 69.73 C ANISOU 3563 C VAL B 190 10125 8952 7418 -407 -518 -357 C ATOM 3564 O VAL B 190 112.897 -4.628 7.070 1.00 63.13 O ANISOU 3564 O VAL B 190 9317 8085 6585 -386 -530 -343 O ATOM 3565 CB VAL B 190 113.124 -4.259 10.186 1.00 87.31 C ANISOU 3565 CB VAL B 190 12265 11225 9684 -408 -489 -382 C ATOM 3566 CG1 VAL B 190 111.778 -4.413 10.874 1.00 88.34 C ANISOU 3566 CG1 VAL B 190 12350 11388 9829 -425 -509 -417 C ATOM 3567 CG2 VAL B 190 114.232 -4.128 11.218 1.00 81.92 C ANISOU 3567 CG2 VAL B 190 11563 10557 9005 -409 -451 -374 C ATOM 3568 N ASP B 191 111.401 -6.028 8.003 1.00 83.28 N ANISOU 3568 N ASP B 191 10547 10829 10265 124 -286 -428 N ATOM 3569 CA ASP B 191 110.477 -5.960 6.879 1.00 88.93 C ANISOU 3569 CA ASP B 191 11270 11566 10952 122 -282 -416 C ATOM 3570 C ASP B 191 109.088 -5.535 7.328 1.00 93.96 C ANISOU 3570 C ASP B 191 11923 12190 11589 105 -287 -377 C ATOM 3571 O ASP B 191 108.359 -6.299 7.962 1.00 90.46 O ANISOU 3571 O ASP B 191 11494 11721 11155 103 -317 -375 O ATOM 3572 CB ASP B 191 110.394 -7.304 6.158 1.00 75.57 C ANISOU 3572 CB ASP B 191 9586 9877 9251 137 -309 -447 C ATOM 3573 CG ASP B 191 109.472 -7.260 4.954 1.00 91.89 C ANISOU 3573 CG ASP B 191 11659 11966 11288 136 -304 -436 C ATOM 3574 OD1 ASP B 191 109.427 -6.212 4.277 1.00 99.26 O ANISOU 3574 OD1 ASP B 191 12585 12925 12204 129 -273 -418 O ATOM 3575 OD2 ASP B 191 108.789 -8.272 4.687 1.00 96.95 O ANISOU 3575 OD2 ASP B 191 12315 12600 11923 140 -333 -446 O ATOM 3576 N TYR B 192 108.735 -4.304 6.984 1.00102.25 N ANISOU 3576 N TYR B 192 12968 13258 12625 94 -256 -346 N ATOM 3577 CA TYR B 192 107.421 -3.750 7.265 1.00102.27 C ANISOU 3577 CA TYR B 192 12984 13252 12623 77 -255 -307 C ATOM 3578 C TYR B 192 106.910 -3.036 6.021 1.00117.34 C ANISOU 3578 C TYR B 192 14890 15193 14502 73 -231 -290 C ATOM 3579 O TYR B 192 107.497 -2.042 5.598 1.00134.64 O ANISOU 3579 O TYR B 192 17066 17406 16684 71 -197 -284 O ATOM 3580 CB TYR B 192 107.487 -2.776 8.441 1.00108.03 C ANISOU 3580 CB TYR B 192 13710 13964 13372 63 -241 -280 C ATOM 3581 CG TYR B 192 107.141 -3.357 9.795 1.00115.00 C ANISOU 3581 CG TYR B 192 14605 14809 14281 58 -271 -277 C ATOM 3582 CD1 TYR B 192 108.099 -3.987 10.580 1.00111.99 C ANISOU 3582 CD1 TYR B 192 14218 14409 13923 67 -286 -304 C ATOM 3583 CD2 TYR B 192 105.859 -3.246 10.299 1.00101.67 C ANISOU 3583 CD2 TYR B 192 12932 13103 12594 45 -283 -246 C ATOM 3584 CE1 TYR B 192 107.772 -4.501 11.827 1.00111.32 C ANISOU 3584 CE1 TYR B 192 14145 14290 13863 62 -313 -300 C ATOM 3585 CE2 TYR B 192 105.524 -3.750 11.536 1.00100.16 C ANISOU 3585 CE2 TYR B 192 12753 12878 12427 40 -309 -242 C ATOM 3586 CZ TYR B 192 106.479 -4.377 12.296 1.00111.40 C ANISOU 3586 CZ TYR B 192 14171 14283 13873 48 -324 -269 C ATOM 3587 OH TYR B 192 106.126 -4.873 13.528 1.00 92.07 O ANISOU 3587 OH TYR B 192 11733 11800 11448 43 -351 -265 O ATOM 3588 N SER B 193 105.829 -3.537 5.430 1.00113.82 N ANISOU 3588 N SER B 193 14458 14749 14039 72 -246 -283 N ATOM 3589 CA SER B 193 105.299 -2.939 4.207 1.00109.63 C ANISOU 3589 CA SER B 193 13926 14250 13480 68 -225 -267 C ATOM 3590 C SER B 193 104.831 -1.503 4.439 1.00118.66 C ANISOU 3590 C SER B 193 15066 15398 14620 51 -195 -226 C ATOM 3591 O SER B 193 104.964 -0.649 3.562 1.00112.18 O ANISOU 3591 O SER B 193 14235 14606 13781 49 -165 -217 O ATOM 3592 CB SER B 193 104.149 -3.783 3.653 1.00104.04 C ANISOU 3592 CB SER B 193 13234 13539 12756 69 -250 -265 C ATOM 3593 OG SER B 193 104.618 -5.034 3.179 1.00110.29 O ANISOU 3593 OG SER B 193 14027 14332 13545 85 -273 -304 O ATOM 3594 N HIS B 194 104.295 -1.244 5.628 1.00130.48 N ANISOU 3594 N HIS B 194 16571 16868 16136 39 -204 -203 N ATOM 3595 CA HIS B 194 103.934 0.111 6.035 1.00122.66 C ANISOU 3595 CA HIS B 194 15578 15879 15147 22 -176 -164 C ATOM 3596 C HIS B 194 105.129 0.782 6.705 1.00118.56 C ANISOU 3596 C HIS B 194 15043 15358 14645 23 -156 -170 C ATOM 3597 O HIS B 194 105.154 0.944 7.926 1.00115.11 O ANISOU 3597 O HIS B 194 14610 14895 14232 15 -163 -159 O ATOM 3598 CB HIS B 194 102.727 0.094 6.979 1.00105.75 C ANISOU 3598 CB HIS B 194 13454 13709 13016 8 -195 -134 C ATOM 3599 CG HIS B 194 101.447 -0.327 6.323 1.00128.34 C ANISOU 3599 CG HIS B 194 16330 16574 15858 5 -209 -121 C ATOM 3600 ND1 HIS B 194 101.317 -1.515 5.636 1.00129.08 N ANISOU 3600 ND1 HIS B 194 16431 16672 15942 17 -234 -148 N ATOM 3601 CD2 HIS B 194 100.239 0.281 6.252 1.00127.40 C ANISOU 3601 CD2 HIS B 194 16221 16456 15728 -9 -203 -84 C ATOM 3602 CE1 HIS B 194 100.086 -1.619 5.168 1.00122.45 C ANISOU 3602 CE1 HIS B 194 15604 15835 15085 11 -243 -128 C ATOM 3603 NE2 HIS B 194 99.411 -0.543 5.528 1.00137.45 N ANISOU 3603 NE2 HIS B 194 17507 17733 16985 -6 -224 -89 N ATOM 3604 N ASP B 195 106.118 1.164 5.898 1.00126.41 N ANISOU 3604 N ASP B 195 16021 16380 15629 31 -132 -187 N ATOM 3605 CA ASP B 195 107.376 1.691 6.419 1.00127.35 C ANISOU 3605 CA ASP B 195 16124 16499 15763 34 -113 -197 C ATOM 3606 C ASP B 195 107.166 2.978 7.209 1.00111.68 C ANISOU 3606 C ASP B 195 14137 14508 13789 17 -90 -161 C ATOM 3607 O ASP B 195 107.855 3.235 8.196 1.00113.92 O ANISOU 3607 O ASP B 195 14415 14776 14095 15 -87 -163 O ATOM 3608 CB ASP B 195 108.370 1.960 5.279 1.00141.94 C ANISOU 3608 CB ASP B 195 17955 18381 17595 45 -89 -219 C ATOM 3609 CG ASP B 195 108.518 0.783 4.326 1.00132.26 C ANISOU 3609 CG ASP B 195 16731 17166 16355 61 -108 -253 C ATOM 3610 OD1 ASP B 195 109.276 -0.158 4.645 1.00124.73 O ANISOU 3610 OD1 ASP B 195 15776 16201 15416 74 -128 -285 O ATOM 3611 OD2 ASP B 195 107.896 0.811 3.243 1.00120.04 O ANISOU 3611 OD2 ASP B 195 15187 15641 14784 61 -103 -247 O ATOM 3612 N LYS B 196 106.208 3.786 6.772 1.00104.82 N ANISOU 3612 N LYS B 196 13272 13651 12903 5 -74 -128 N ATOM 3613 CA LYS B 196 105.975 5.078 7.399 1.00103.58 C ANISOU 3613 CA LYS B 196 13112 13490 12752 -11 -49 -92 C ATOM 3614 C LYS B 196 105.139 4.962 8.670 1.00104.21 C ANISOU 3614 C LYS B 196 13207 13535 12851 -23 -69 -70 C ATOM 3615 O LYS B 196 105.421 5.623 9.666 1.00 96.34 O ANISOU 3615 O LYS B 196 12208 12524 11874 -32 -59 -55 O ATOM 3616 CB LYS B 196 105.306 6.029 6.404 1.00 98.55 C ANISOU 3616 CB LYS B 196 12474 12882 12089 -20 -22 -65 C ATOM 3617 CG LYS B 196 106.102 6.209 5.116 1.00107.22 C ANISOU 3617 CG LYS B 196 13556 14015 13166 -9 0 -86 C ATOM 3618 CD LYS B 196 105.528 7.304 4.233 1.00 97.58 C ANISOU 3618 CD LYS B 196 12333 12822 11922 -19 30 -57 C ATOM 3619 CE LYS B 196 106.361 7.484 2.971 1.00 99.20 C ANISOU 3619 CE LYS B 196 12522 13063 12107 -8 51 -78 C ATOM 3620 NZ LYS B 196 105.846 8.584 2.110 1.00 99.50 N ANISOU 3620 NZ LYS B 196 12556 13128 12122 -17 82 -50 N ATOM 3621 N ARG B 197 104.121 4.110 8.645 1.00101.17 N ANISOU 3621 N ARG B 197 12840 13137 12464 -23 -98 -68 N ATOM 3622 CA ARG B 197 103.210 4.018 9.778 1.00 90.41 C ANISOU 3622 CA ARG B 197 11491 11742 11117 -35 -117 -44 C ATOM 3623 C ARG B 197 103.745 3.155 10.921 1.00 92.93 C ANISOU 3623 C ARG B 197 11815 12031 11465 -30 -144 -66 C ATOM 3624 O ARG B 197 103.827 3.610 12.062 1.00 94.89 O ANISOU 3624 O ARG B 197 12063 12257 11733 -39 -142 -50 O ATOM 3625 CB ARG B 197 101.855 3.472 9.325 1.00 82.61 C ANISOU 3625 CB ARG B 197 10521 10752 10115 -39 -137 -31 C ATOM 3626 CG ARG B 197 100.860 3.319 10.460 1.00 74.76 C ANISOU 3626 CG ARG B 197 9544 9725 9137 -51 -159 -7 C ATOM 3627 CD ARG B 197 99.828 2.253 10.152 1.00 81.41 C ANISOU 3627 CD ARG B 197 10403 10559 9971 -48 -191 -11 C ATOM 3628 NE ARG B 197 98.596 2.806 9.600 1.00 71.61 N ANISOU 3628 NE ARG B 197 9171 9329 8710 -59 -182 23 N ATOM 3629 CZ ARG B 197 97.551 2.070 9.242 1.00 71.83 C ANISOU 3629 CZ ARG B 197 9213 9352 8727 -59 -205 27 C ATOM 3630 NH1 ARG B 197 97.595 0.751 9.373 1.00 71.61 N ANISOU 3630 NH1 ARG B 197 9193 9309 8705 -48 -240 -1 N ATOM 3631 NH2 ARG B 197 96.463 2.647 8.750 1.00 96.91 N ANISOU 3631 NH2 ARG B 197 12397 12539 11886 -70 -195 58 N ATOM 3632 N ARG B 198 104.112 1.915 10.614 1.00 83.76 N ANISOU 3632 N ARG B 198 10654 10866 10303 -15 -170 -101 N ATOM 3633 CA ARG B 198 104.429 0.940 11.656 1.00 83.19 C ANISOU 3633 CA ARG B 198 10588 10763 10256 -9 -201 -121 C ATOM 3634 C ARG B 198 105.856 1.045 12.209 1.00 88.18 C ANISOU 3634 C ARG B 198 11205 11391 10907 -2 -192 -143 C ATOM 3635 O ARG B 198 106.073 0.904 13.421 1.00 85.98 O ANISOU 3635 O ARG B 198 10930 11085 10654 -6 -205 -143 O ATOM 3636 CB ARG B 198 104.190 -0.475 11.125 1.00 77.91 C ANISOU 3636 CB ARG B 198 9929 10092 9581 4 -234 -149 C ATOM 3637 CG ARG B 198 102.786 -0.733 10.582 1.00 93.76 C ANISOU 3637 CG ARG B 198 11953 12102 11571 -2 -247 -130 C ATOM 3638 CD ARG B 198 102.660 -2.162 10.060 1.00 94.67 C ANISOU 3638 CD ARG B 198 12076 12215 11679 12 -279 -161 C ATOM 3639 NE ARG B 198 101.388 -2.427 9.392 1.00 99.42 N ANISOU 3639 NE ARG B 198 12692 12822 12261 8 -290 -145 N ATOM 3640 CZ ARG B 198 101.132 -3.529 8.694 1.00 94.85 C ANISOU 3640 CZ ARG B 198 12120 12247 11670 19 -314 -167 C ATOM 3641 NH1 ARG B 198 102.062 -4.466 8.566 1.00 86.63 N ANISOU 3641 NH1 ARG B 198 11074 11206 10636 35 -329 -207 N ATOM 3642 NH2 ARG B 198 99.949 -3.693 8.117 1.00 96.75 N ANISOU 3642 NH2 ARG B 198 12374 12493 11893 14 -322 -150 N ATOM 3643 N GLU B 199 106.823 1.296 11.331 1.00 88.44 N ANISOU 3643 N GLU B 199 11222 11452 10928 8 -171 -163 N ATOM 3644 CA GLU B 199 108.220 1.355 11.751 1.00 75.49 C ANISOU 3644 CA GLU B 199 9567 9811 9304 15 -162 -186 C ATOM 3645 C GLU B 199 108.451 2.487 12.737 1.00 73.84 C ANISOU 3645 C GLU B 199 9352 9591 9111 2 -140 -160 C ATOM 3646 O GLU B 199 109.210 2.344 13.704 1.00 77.56 O ANISOU 3646 O GLU B 199 9820 10043 9606 3 -147 -171 O ATOM 3647 CB GLU B 199 109.137 1.533 10.542 1.00 86.43 C ANISOU 3647 CB GLU B 199 10937 11232 10672 27 -140 -208 C ATOM 3648 CG GLU B 199 109.273 0.297 9.676 1.00106.84 C ANISOU 3648 CG GLU B 199 13524 13825 13245 44 -162 -242 C ATOM 3649 CD GLU B 199 110.193 -0.739 10.288 1.00103.05 C ANISOU 3649 CD GLU B 199 13042 13326 12787 57 -185 -278 C ATOM 3650 OE1 GLU B 199 110.894 -0.409 11.268 1.00 87.71 O ANISOU 3650 OE1 GLU B 199 11092 11368 10866 54 -180 -278 O ATOM 3651 OE2 GLU B 199 110.220 -1.881 9.785 1.00102.08 O ANISOU 3651 OE2 GLU B 199 12923 13203 12658 69 -209 -306 O ATOM 3652 N ARG B 200 107.766 3.602 12.504 1.00 69.04 N ANISOU 3652 N ARG B 200 8745 8995 8491 -12 -116 -125 N ATOM 3653 CA ARG B 200 107.840 4.727 13.418 1.00 60.82 C ANISOU 3653 CA ARG B 200 7701 7944 7464 -26 -95 -97 C ATOM 3654 C ARG B 200 107.249 4.346 14.767 1.00 62.37 C ANISOU 3654 C ARG B 200 7912 8103 7684 -35 -121 -84 C ATOM 3655 O ARG B 200 107.729 4.792 15.802 1.00 50.69 O ANISOU 3655 O ARG B 200 6428 6606 6225 -41 -115 -77 O ATOM 3656 CB ARG B 200 107.114 5.944 12.845 1.00 60.82 C ANISOU 3656 CB ARG B 200 7701 7965 7444 -39 -65 -61 C ATOM 3657 CG ARG B 200 107.784 6.551 11.624 1.00 82.71 C ANISOU 3657 CG ARG B 200 10457 10775 10195 -32 -35 -69 C ATOM 3658 CD ARG B 200 107.060 7.807 11.168 1.00 91.64 C ANISOU 3658 CD ARG B 200 11588 11924 11308 -46 -5 -31 C ATOM 3659 NE ARG B 200 107.524 8.256 9.859 1.00102.33 N ANISOU 3659 NE ARG B 200 12928 13315 12638 -39 21 -40 N ATOM 3660 CZ ARG B 200 106.958 9.235 9.161 1.00 99.43 C ANISOU 3660 CZ ARG B 200 12559 12969 12250 -48 47 -13 C ATOM 3661 NH1 ARG B 200 105.900 9.872 9.644 1.00104.05 N ANISOU 3661 NH1 ARG B 200 13155 13544 12837 -64 51 25 N ATOM 3662 NH2 ARG B 200 107.450 9.575 7.978 1.00 84.58 N ANISOU 3662 NH2 ARG B 200 10666 11123 10349 -41 69 -23 N ATOM 3663 N ALA B 201 106.218 3.506 14.755 1.00 61.94 N ANISOU 3663 N ALA B 201 7874 8035 7627 -35 -150 -82 N ATOM 3664 CA ALA B 201 105.610 3.054 16.000 1.00 50.70 C ANISOU 3664 CA ALA B 201 6464 6575 6225 -43 -177 -72 C ATOM 3665 C ALA B 201 106.578 2.175 16.785 1.00 54.27 C ANISOU 3665 C ALA B 201 6913 7007 6702 -33 -198 -104 C ATOM 3666 O ALA B 201 106.674 2.281 18.015 1.00 52.53 O ANISOU 3666 O ALA B 201 6695 6759 6504 -40 -205 -96 O ATOM 3667 CB ALA B 201 104.313 2.309 15.722 1.00 54.34 C ANISOU 3667 CB ALA B 201 6943 7028 6676 -44 -203 -64 C ATOM 3668 N VAL B 202 107.322 1.333 16.071 1.00 49.97 N ANISOU 3668 N VAL B 202 6362 6475 6151 -16 -207 -141 N ATOM 3669 CA VAL B 202 108.331 0.512 16.729 1.00 45.62 C ANISOU 3669 CA VAL B 202 5806 5907 5622 -5 -226 -173 C ATOM 3670 C VAL B 202 109.417 1.398 17.337 1.00 44.77 C ANISOU 3670 C VAL B 202 5682 5799 5528 -9 -200 -171 C ATOM 3671 O VAL B 202 109.844 1.184 18.478 1.00 46.62 O ANISOU 3671 O VAL B 202 5917 6007 5788 -11 -213 -176 O ATOM 3672 CB VAL B 202 108.971 -0.497 15.751 1.00 51.47 C ANISOU 3672 CB VAL B 202 6541 6663 6351 14 -238 -213 C ATOM 3673 CG1 VAL B 202 110.085 -1.273 16.435 1.00 36.22 C ANISOU 3673 CG1 VAL B 202 4603 4716 4443 25 -254 -246 C ATOM 3674 CG2 VAL B 202 107.915 -1.444 15.199 1.00 51.90 C ANISOU 3674 CG2 VAL B 202 6611 6717 6392 17 -265 -217 C ATOM 3675 N ALA B 203 109.830 2.421 16.590 1.00 48.29 N ANISOU 3675 N ALA B 203 6116 6274 5958 -10 -165 -162 N ATOM 3676 CA ALA B 203 110.859 3.338 17.074 1.00 47.41 C ANISOU 3676 CA ALA B 203 5990 6166 5859 -13 -138 -159 C ATOM 3677 C ALA B 203 110.392 4.133 18.293 1.00 42.38 C ANISOU 3677 C ALA B 203 5358 5505 5239 -31 -133 -125 C ATOM 3678 O ALA B 203 111.182 4.426 19.194 1.00 32.16 O ANISOU 3678 O ALA B 203 4057 4198 3965 -34 -127 -128 O ATOM 3679 CB ALA B 203 111.285 4.284 15.962 1.00 33.99 C ANISOU 3679 CB ALA B 203 4276 4503 4136 -12 -102 -155 C ATOM 3680 N ILE B 204 109.104 4.466 18.323 1.00 42.24 N ANISOU 3680 N ILE B 204 5354 5483 5213 -44 -134 -94 N ATOM 3681 CA ILE B 204 108.536 5.210 19.441 1.00 35.77 C ANISOU 3681 CA ILE B 204 4542 4641 4408 -61 -130 -60 C ATOM 3682 C ILE B 204 108.491 4.333 20.681 1.00 38.04 C ANISOU 3682 C ILE B 204 4839 4891 4723 -62 -163 -69 C ATOM 3683 O ILE B 204 108.890 4.756 21.772 1.00 37.94 O ANISOU 3683 O ILE B 204 4824 4860 4732 -70 -158 -61 O ATOM 3684 CB ILE B 204 107.113 5.720 19.132 1.00 41.83 C ANISOU 3684 CB ILE B 204 5322 5412 5160 -74 -125 -24 C ATOM 3685 CG1 ILE B 204 107.142 6.772 18.023 1.00 42.95 C ANISOU 3685 CG1 ILE B 204 5454 5590 5277 -76 -88 -10 C ATOM 3686 CG2 ILE B 204 106.476 6.316 20.376 1.00 28.05 C ANISOU 3686 CG2 ILE B 204 3586 3640 3433 -91 -125 9 C ATOM 3687 CD1 ILE B 204 105.781 7.043 17.414 1.00 53.77 C ANISOU 3687 CD1 ILE B 204 6836 6969 6627 -84 -87 18 C ATOM 3688 N VAL B 205 108.023 3.101 20.504 1.00 36.76 N ANISOU 3688 N VAL B 205 4688 4720 4560 -53 -196 -88 N ATOM 3689 CA VAL B 205 107.911 2.184 21.629 1.00 34.87 C ANISOU 3689 CA VAL B 205 4458 4445 4345 -53 -230 -98 C ATOM 3690 C VAL B 205 109.285 1.885 22.214 1.00 34.22 C ANISOU 3690 C VAL B 205 4364 4354 4283 -45 -232 -126 C ATOM 3691 O VAL B 205 109.463 1.868 23.437 1.00 35.82 O ANISOU 3691 O VAL B 205 4569 4529 4511 -52 -242 -122 O ATOM 3692 CB VAL B 205 107.227 0.866 21.214 1.00 40.89 C ANISOU 3692 CB VAL B 205 5234 5202 5101 -44 -265 -115 C ATOM 3693 CG1 VAL B 205 107.381 -0.186 22.301 1.00 36.85 C ANISOU 3693 CG1 VAL B 205 4729 4656 4615 -41 -300 -133 C ATOM 3694 CG2 VAL B 205 105.760 1.107 20.904 1.00 32.93 C ANISOU 3694 CG2 VAL B 205 4240 4195 4077 -55 -268 -84 C ATOM 3695 N ARG B 206 110.265 1.689 21.339 1.00 36.01 N ANISOU 3695 N ARG B 206 4577 4605 4500 -31 -222 -154 N ATOM 3696 CA ARG B 206 111.618 1.419 21.802 1.00 25.89 C ANISOU 3696 CA ARG B 206 3283 3318 3237 -22 -222 -182 C ATOM 3697 C ARG B 206 112.228 2.636 22.491 1.00 27.06 C ANISOU 3697 C ARG B 206 3420 3464 3396 -33 -193 -163 C ATOM 3698 O ARG B 206 112.907 2.502 23.510 1.00 32.07 O ANISOU 3698 O ARG B 206 4053 4078 4056 -34 -200 -171 O ATOM 3699 CB ARG B 206 112.503 0.976 20.638 1.00 32.61 C ANISOU 3699 CB ARG B 206 4121 4196 4072 -4 -216 -216 C ATOM 3700 CG ARG B 206 113.905 0.572 21.050 1.00 46.36 C ANISOU 3700 CG ARG B 206 5850 5933 5832 7 -219 -247 C ATOM 3701 CD ARG B 206 114.718 0.185 19.836 1.00 61.70 C ANISOU 3701 CD ARG B 206 7781 7904 7758 24 -212 -279 C ATOM 3702 NE ARG B 206 114.075 -0.890 19.088 1.00 71.10 N ANISOU 3702 NE ARG B 206 8982 9099 8935 33 -237 -295 N ATOM 3703 CZ ARG B 206 114.425 -1.258 17.860 1.00 64.33 C ANISOU 3703 CZ ARG B 206 8118 8268 8057 47 -232 -318 C ATOM 3704 NH1 ARG B 206 115.410 -0.629 17.235 1.00 56.28 N ANISOU 3704 NH1 ARG B 206 7081 7274 7029 53 -203 -327 N ATOM 3705 NH2 ARG B 206 113.786 -2.250 17.254 1.00 56.00 N ANISOU 3705 NH2 ARG B 206 7073 7214 6991 55 -257 -331 N ATOM 3706 N LEU B 207 111.977 3.822 21.939 1.00 27.00 N ANISOU 3706 N LEU B 207 3409 3479 3372 -41 -160 -137 N ATOM 3707 CA LEU B 207 112.522 5.049 22.512 1.00 25.99 C ANISOU 3707 CA LEU B 207 3270 3352 3252 -52 -130 -117 C ATOM 3708 C LEU B 207 111.952 5.337 23.896 1.00 38.40 C ANISOU 3708 C LEU B 207 4854 4892 4847 -68 -139 -91 C ATOM 3709 O LEU B 207 112.660 5.813 24.786 1.00 20.83 O ANISOU 3709 O LEU B 207 2621 2653 2640 -73 -129 -88 O ATOM 3710 CB LEU B 207 112.250 6.238 21.591 1.00 23.26 C ANISOU 3710 CB LEU B 207 2919 3038 2883 -58 -94 -93 C ATOM 3711 CG LEU B 207 112.661 7.611 22.130 1.00 29.73 C ANISOU 3711 CG LEU B 207 3729 3859 3708 -70 -61 -68 C ATOM 3712 CD1 LEU B 207 114.178 7.752 22.184 1.00 30.41 C ANISOU 3712 CD1 LEU B 207 3797 3954 3803 -61 -47 -92 C ATOM 3713 CD2 LEU B 207 112.038 8.727 21.307 1.00 32.03 C ANISOU 3713 CD2 LEU B 207 4018 4176 3975 -79 -31 -38 C ATOM 3714 N VAL B 208 110.678 5.016 24.084 1.00 37.31 N ANISOU 3714 N VAL B 208 4732 4739 4706 -75 -158 -73 N ATOM 3715 CA VAL B 208 110.015 5.324 25.342 1.00 28.27 C ANISOU 3715 CA VAL B 208 3598 3563 3580 -91 -166 -46 C ATOM 3716 C VAL B 208 110.304 4.257 26.390 1.00 30.02 C ANISOU 3716 C VAL B 208 3826 3753 3828 -87 -200 -67 C ATOM 3717 O VAL B 208 110.842 4.555 27.458 1.00 32.07 O ANISOU 3717 O VAL B 208 4082 3993 4110 -93 -198 -63 O ATOM 3718 CB VAL B 208 108.492 5.467 25.156 1.00 25.23 C ANISOU 3718 CB VAL B 208 3229 3176 3182 -101 -172 -16 C ATOM 3719 CG1 VAL B 208 107.794 5.577 26.504 1.00 21.43 C ANISOU 3719 CG1 VAL B 208 2761 2659 2721 -116 -186 9 C ATOM 3720 CG2 VAL B 208 108.178 6.676 24.287 1.00 12.57 C ANISOU 3720 CG2 VAL B 208 1620 1601 1555 -107 -137 10 C ATOM 3721 N LEU B 209 109.948 3.015 26.082 1.00 22.51 N ANISOU 3721 N LEU B 209 2883 2795 2874 -77 -232 -89 N ATOM 3722 CA LEU B 209 110.128 1.925 27.031 1.00 24.73 C ANISOU 3722 CA LEU B 209 3171 3047 3180 -73 -267 -109 C ATOM 3723 C LEU B 209 111.601 1.632 27.302 1.00 26.56 C ANISOU 3723 C LEU B 209 3388 3277 3426 -62 -265 -140 C ATOM 3724 O LEU B 209 111.961 1.165 28.381 1.00 34.10 O ANISOU 3724 O LEU B 209 4345 4205 4407 -64 -284 -150 O ATOM 3725 CB LEU B 209 109.431 0.659 26.524 1.00 33.37 C ANISOU 3725 CB LEU B 209 4277 4137 4265 -63 -300 -126 C ATOM 3726 CG LEU B 209 107.905 0.694 26.411 1.00 27.19 C ANISOU 3726 CG LEU B 209 3512 3349 3471 -73 -310 -98 C ATOM 3727 CD1 LEU B 209 107.387 -0.644 25.912 1.00 23.73 C ANISOU 3727 CD1 LEU B 209 3083 2907 3025 -62 -344 -120 C ATOM 3728 CD2 LEU B 209 107.262 1.057 27.740 1.00 29.74 C ANISOU 3728 CD2 LEU B 209 3845 3640 3814 -90 -317 -69 C ATOM 3729 N GLY B 210 112.456 1.896 26.323 1.00 26.54 N ANISOU 3729 N GLY B 210 3370 3304 3409 -52 -243 -157 N ATOM 3730 CA GLY B 210 113.859 1.565 26.470 1.00 28.69 C ANISOU 3730 CA GLY B 210 3628 3578 3694 -40 -242 -188 C ATOM 3731 C GLY B 210 114.763 2.673 26.973 1.00 28.73 C ANISOU 3731 C GLY B 210 3621 3587 3710 -47 -211 -178 C ATOM 3732 O GLY B 210 115.896 2.409 27.373 1.00 26.34 O ANISOU 3732 O GLY B 210 3308 3279 3423 -41 -213 -201 O ATOM 3733 N PHE B 211 114.277 3.910 26.970 1.00 30.86 N ANISOU 3733 N PHE B 211 3890 3865 3970 -61 -184 -143 N ATOM 3734 CA PHE B 211 115.159 5.037 27.249 1.00 30.76 C ANISOU 3734 CA PHE B 211 3863 3861 3962 -67 -151 -133 C ATOM 3735 C PHE B 211 114.500 6.154 28.054 1.00 22.57 C ANISOU 3735 C PHE B 211 2832 2811 2931 -87 -135 -91 C ATOM 3736 O PHE B 211 114.910 6.429 29.180 1.00 25.77 O ANISOU 3736 O PHE B 211 3237 3195 3360 -95 -134 -85 O ATOM 3737 CB PHE B 211 115.706 5.607 25.934 1.00 28.76 C ANISOU 3737 CB PHE B 211 3596 3646 3684 -59 -121 -139 C ATOM 3738 CG PHE B 211 116.922 6.473 26.107 1.00 25.72 C ANISOU 3738 CG PHE B 211 3194 3272 3305 -59 -92 -141 C ATOM 3739 CD1 PHE B 211 118.188 5.911 26.157 1.00 22.82 C ANISOU 3739 CD1 PHE B 211 2814 2906 2949 -46 -97 -175 C ATOM 3740 CD2 PHE B 211 116.801 7.846 26.220 1.00 28.00 C ANISOU 3740 CD2 PHE B 211 3479 3571 3589 -73 -59 -109 C ATOM 3741 CE1 PHE B 211 119.309 6.704 26.318 1.00 22.29 C ANISOU 3741 CE1 PHE B 211 2733 2850 2888 -47 -70 -177 C ATOM 3742 CE2 PHE B 211 117.919 8.646 26.381 1.00 22.08 C ANISOU 3742 CE2 PHE B 211 2714 2831 2844 -74 -32 -111 C ATOM 3743 CZ PHE B 211 119.174 8.074 26.430 1.00 30.10 C ANISOU 3743 CZ PHE B 211 3717 3847 3870 -61 -38 -145 C ATOM 3744 N LEU B 212 113.490 6.799 27.478 1.00 23.26 N ANISOU 3744 N LEU B 212 3401 2619 2819 161 136 207 N ATOM 3745 CA LEU B 212 112.954 8.032 28.055 1.00 20.60 C ANISOU 3745 CA LEU B 212 3066 2253 2508 152 135 201 C ATOM 3746 C LEU B 212 112.290 7.841 29.418 1.00 24.56 C ANISOU 3746 C LEU B 212 3559 2760 3014 161 120 187 C ATOM 3747 O LEU B 212 112.616 8.542 30.380 1.00 29.24 O ANISOU 3747 O LEU B 212 4150 3337 3625 155 133 175 O ATOM 3748 CB LEU B 212 111.955 8.673 27.090 1.00 20.69 C ANISOU 3748 CB LEU B 212 3075 2253 2534 143 120 205 C ATOM 3749 CG LEU B 212 112.531 9.241 25.793 1.00 31.68 C ANISOU 3749 CG LEU B 212 4478 3631 3928 133 135 218 C ATOM 3750 CD1 LEU B 212 111.425 9.849 24.947 1.00 34.33 C ANISOU 3750 CD1 LEU B 212 4809 3957 4277 126 116 223 C ATOM 3751 CD2 LEU B 212 113.611 10.268 26.093 1.00 32.16 C ANISOU 3751 CD2 LEU B 212 4549 3663 4006 122 169 219 C ATOM 3752 N TRP B 213 111.353 6.901 29.495 1.00 24.24 N ANISOU 3752 N TRP B 213 3505 2746 2959 169 94 181 N ATOM 3753 CA TRP B 213 110.700 6.576 30.762 1.00 24.09 C ANISOU 3753 CA TRP B 213 3477 2735 2940 178 78 166 C ATOM 3754 C TRP B 213 111.696 6.103 31.837 1.00 21.93 C ANISOU 3754 C TRP B 213 3208 2472 2652 190 89 164 C ATOM 3755 O TRP B 213 111.660 6.616 32.969 1.00 25.97 O ANISOU 3755 O TRP B 213 3692 2995 3182 178 87 137 O ATOM 3756 CB TRP B 213 109.600 5.536 30.539 1.00 20.66 C ANISOU 3756 CB TRP B 213 3026 2330 2494 183 53 160 C ATOM 3757 CG TRP B 213 108.978 5.028 31.803 1.00 33.10 C ANISOU 3757 CG TRP B 213 4591 3919 4065 191 38 144 C ATOM 3758 CD1 TRP B 213 109.168 3.805 32.375 1.00 26.97 C ANISOU 3758 CD1 TRP B 213 3806 3174 3267 203 32 138 C ATOM 3759 CD2 TRP B 213 108.059 5.727 32.649 1.00 25.46 C ANISOU 3759 CD2 TRP B 213 3620 2935 3118 188 27 132 C ATOM 3760 NE1 TRP B 213 108.424 3.696 33.522 1.00 24.04 N ANISOU 3760 NE1 TRP B 213 3428 2808 2899 208 17 123 N ATOM 3761 CE2 TRP B 213 107.734 4.864 33.714 1.00 32.65 C ANISOU 3761 CE2 TRP B 213 4522 3868 4015 198 15 118 C ATOM 3762 CE3 TRP B 213 107.480 6.998 32.610 1.00 23.36 C ANISOU 3762 CE3 TRP B 213 3355 2638 2883 175 28 129 C ATOM 3763 CZ2 TRP B 213 106.854 5.231 34.730 1.00 33.28 C ANISOU 3763 CZ2 TRP B 213 4596 3939 4110 197 3 102 C ATOM 3764 CZ3 TRP B 213 106.608 7.360 33.619 1.00 25.33 C ANISOU 3764 CZ3 TRP B 213 3596 2879 3150 173 17 112 C ATOM 3765 CH2 TRP B 213 106.304 6.481 34.665 1.00 26.95 C ANISOU 3765 CH2 TRP B 213 3795 3106 3340 184 5 98 C ATOM 3766 N PRO B 214 112.579 5.135 31.503 1.00 23.01 N ANISOU 3766 N PRO B 214 3344 2635 2765 198 97 173 N ATOM 3767 CA PRO B 214 113.599 4.798 32.500 1.00 22.46 C ANISOU 3767 CA PRO B 214 3238 2604 2692 192 103 153 C ATOM 3768 C PRO B 214 114.457 5.988 32.912 1.00 26.06 C ANISOU 3768 C PRO B 214 3667 3059 3175 166 122 133 C ATOM 3769 O PRO B 214 114.819 6.104 34.079 1.00 27.72 O ANISOU 3769 O PRO B 214 3843 3297 3392 156 119 107 O ATOM 3770 CB PRO B 214 114.453 3.745 31.785 1.00 21.08 C ANISOU 3770 CB PRO B 214 3071 2447 2491 204 113 172 C ATOM 3771 CG PRO B 214 113.545 3.134 30.790 1.00 18.46 C ANISOU 3771 CG PRO B 214 2751 2110 2151 210 99 181 C ATOM 3772 CD PRO B 214 112.681 4.263 30.314 1.00 25.67 C ANISOU 3772 CD PRO B 214 3674 2993 3088 198 94 180 C ATOM 3773 N LEU B 215 114.745 6.882 31.967 1.00 17.13 N ANISOU 3773 N LEU B 215 2551 1897 2059 155 141 144 N ATOM 3774 CA LEU B 215 115.585 8.033 32.270 1.00 28.02 C ANISOU 3774 CA LEU B 215 3907 3274 3466 131 162 125 C ATOM 3775 C LEU B 215 114.900 8.929 33.289 1.00 35.30 C ANISOU 3775 C LEU B 215 4811 4189 4413 117 153 100 C ATOM 3776 O LEU B 215 115.499 9.318 34.295 1.00 33.78 O ANISOU 3776 O LEU B 215 4583 4019 4232 101 159 72 O ATOM 3777 CB LEU B 215 115.905 8.822 31.000 1.00 30.07 C ANISOU 3777 CB LEU B 215 4192 3497 3736 122 184 143 C ATOM 3778 CG LEU B 215 116.698 10.118 31.178 1.00 37.35 C ANISOU 3778 CG LEU B 215 5093 4409 4689 97 208 125 C ATOM 3779 CD1 LEU B 215 118.048 9.848 31.826 1.00 18.94 C ANISOU 3779 CD1 LEU B 215 2725 2116 2356 87 221 106 C ATOM 3780 CD2 LEU B 215 116.869 10.809 29.837 1.00 36.57 C ANISOU 3780 CD2 LEU B 215 5026 4272 4599 91 228 147 C ATOM 3781 N LEU B 216 113.625 9.209 33.045 1.00 24.33 N ANISOU 3781 N LEU B 216 3444 2769 3031 124 139 108 N ATOM 3782 CA LEU B 216 112.850 10.065 33.928 1.00 26.36 C ANISOU 3782 CA LEU B 216 3687 3015 3315 112 132 86 C ATOM 3783 C LEU B 216 112.724 9.471 35.329 1.00 30.85 C ANISOU 3783 C LEU B 216 4226 3620 3874 112 116 60 C ATOM 3784 O LEU B 216 113.100 10.104 36.335 1.00 25.53 O ANISOU 3784 O LEU B 216 3521 2962 3218 92 122 32 O ATOM 3785 CB LEU B 216 111.464 10.293 33.327 1.00 22.68 C ANISOU 3785 CB LEU B 216 3252 2509 2855 122 117 103 C ATOM 3786 CG LEU B 216 110.444 11.119 34.103 1.00 22.73 C ANISOU 3786 CG LEU B 216 3248 2496 2891 113 108 84 C ATOM 3787 CD1 LEU B 216 110.896 12.563 34.201 1.00 38.62 C ANISOU 3787 CD1 LEU B 216 5246 4489 4939 87 131 69 C ATOM 3788 CD2 LEU B 216 109.087 11.019 33.426 1.00 23.57 C ANISOU 3788 CD2 LEU B 216 3388 2568 2998 129 90 106 C ATOM 3789 N THR B 217 112.232 8.235 35.391 1.00 25.82 N ANISOU 3789 N THR B 217 3601 3001 3209 135 96 71 N ATOM 3790 CA THR B 217 111.959 7.621 36.684 1.00 28.65 C ANISOU 3790 CA THR B 217 3936 3391 3558 137 79 49 C ATOM 3791 C THR B 217 113.229 7.372 37.496 1.00 34.99 C ANISOU 3791 C THR B 217 4705 4238 4354 126 88 31 C ATOM 3792 O THR B 217 113.271 7.661 38.695 1.00 33.90 O ANISOU 3792 O THR B 217 4538 4119 4223 112 84 3 O ATOM 3793 CB THR B 217 111.198 6.301 36.519 1.00 19.76 C ANISOU 3793 CB THR B 217 2831 2274 2403 164 58 66 C ATOM 3794 OG1 THR B 217 111.822 5.520 35.494 1.00 32.96 O ANISOU 3794 OG1 THR B 217 4520 3951 4052 179 65 92 O ATOM 3795 CG2 THR B 217 109.761 6.576 36.121 1.00 19.46 C ANISOU 3795 CG2 THR B 217 2820 2198 2375 173 45 75 C ATOM 3796 N LEU B 218 114.268 6.849 36.848 1.00 27.93 N ANISOU 3796 N LEU B 218 3811 3357 3444 132 99 46 N ATOM 3797 CA LEU B 218 115.523 6.611 37.552 1.00 28.87 C ANISOU 3797 CA LEU B 218 3896 3516 3558 122 107 30 C ATOM 3798 C LEU B 218 116.201 7.912 37.976 1.00 29.00 C ANISOU 3798 C LEU B 218 3886 3528 3603 93 125 6 C ATOM 3799 O LEU B 218 116.838 7.963 39.037 1.00 29.83 O ANISOU 3799 O LEU B 218 3958 3666 3710 80 125 -18 O ATOM 3800 CB LEU B 218 116.475 5.781 36.693 1.00 27.73 C ANISOU 3800 CB LEU B 218 3759 3384 3394 134 117 52 C ATOM 3801 CG LEU B 218 116.006 4.357 36.385 1.00 32.20 C ANISOU 3801 CG LEU B 218 4345 3961 3929 162 101 73 C ATOM 3802 CD1 LEU B 218 117.104 3.575 35.682 1.00 31.01 C ANISOU 3802 CD1 LEU B 218 4194 3825 3762 170 114 90 C ATOM 3803 CD2 LEU B 218 115.545 3.642 37.648 1.00 30.00 C ANISOU 3803 CD2 LEU B 218 4048 3713 3637 169 78 57 C ATOM 3804 N THR B 219 116.046 8.966 37.175 1.00 20.75 N ANISOU 3804 N THR B 219 2858 2445 2582 83 141 13 N ATOM 3805 CA THR B 219 116.620 10.253 37.554 1.00 22.49 C ANISOU 3805 CA THR B 219 3054 2658 2832 56 161 -10 C ATOM 3806 C THR B 219 115.944 10.759 38.821 1.00 28.49 C ANISOU 3806 C THR B 219 3793 3425 3606 42 150 -40 C ATOM 3807 O THR B 219 116.616 11.229 39.746 1.00 25.98 O ANISOU 3807 O THR B 219 3442 3130 3299 21 157 -67 O ATOM 3808 CB THR B 219 116.483 11.315 36.441 1.00 23.42 C ANISOU 3808 CB THR B 219 3195 2730 2973 48 180 4 C ATOM 3809 OG1 THR B 219 117.156 10.864 35.259 1.00 23.24 O ANISOU 3809 OG1 THR B 219 3193 2702 2937 59 192 30 O ATOM 3810 CG2 THR B 219 117.097 12.632 36.883 1.00 22.26 C ANISOU 3810 CG2 THR B 219 3023 2578 2859 19 202 -22 C ATOM 3811 N ILE B 220 114.620 10.627 38.884 1.00 29.17 N ANISOU 3811 N ILE B 220 3899 3491 3692 52 132 -35 N ATOM 3812 CA ILE B 220 113.910 11.049 40.089 1.00 29.39 C ANISOU 3812 CA ILE B 220 3909 3524 3734 39 122 -63 C ATOM 3813 C ILE B 220 114.327 10.208 41.298 1.00 38.60 C ANISOU 3813 C ILE B 220 5049 4740 4878 39 109 -82 C ATOM 3814 O ILE B 220 114.571 10.732 42.404 1.00 33.90 O ANISOU 3814 O ILE B 220 4424 4163 4294 17 111 -112 O ATOM 3815 CB ILE B 220 112.387 10.956 39.897 1.00 28.08 C ANISOU 3815 CB ILE B 220 3771 3328 3571 53 106 -53 C ATOM 3816 CG1 ILE B 220 111.942 11.924 38.800 1.00 29.39 C ANISOU 3816 CG1 ILE B 220 3961 3444 3763 51 118 -36 C ATOM 3817 CG2 ILE B 220 111.662 11.251 41.200 1.00 21.47 C ANISOU 3817 CG2 ILE B 220 2915 2497 2746 40 95 -83 C ATOM 3818 CD1 ILE B 220 110.469 11.864 38.490 1.00 26.50 C ANISOU 3818 CD1 ILE B 220 3622 3045 3403 65 101 -23 C ATOM 3819 N CYS B 221 114.471 8.908 41.056 1.00 27.66 N ANISOU 3819 N CYS B 221 3673 3376 3460 62 96 -63 N ATOM 3820 CA CYS B 221 114.770 7.952 42.113 1.00 30.67 C ANISOU 3820 CA CYS B 221 4033 3803 3818 67 80 -75 C ATOM 3821 C CYS B 221 116.119 8.236 42.768 1.00 30.89 C ANISOU 3821 C CYS B 221 4024 3864 3848 47 91 -95 C ATOM 3822 O CYS B 221 116.224 8.385 43.999 1.00 21.54 O ANISOU 3822 O CYS B 221 2813 2707 2665 31 85 -123 O ATOM 3823 CB CYS B 221 114.748 6.530 41.541 1.00 26.92 C ANISOU 3823 CB CYS B 221 3578 3341 3311 97 68 -48 C ATOM 3824 SG CYS B 221 115.310 5.230 42.663 1.00 39.47 S ANISOU 3824 SG CYS B 221 5141 4987 4869 105 50 -56 S ATOM 3825 N TYR B 222 117.150 8.339 41.937 1.00 28.56 N ANISOU 3825 N TYR B 222 3728 3567 3556 46 109 -82 N ATOM 3826 CA TYR B 222 118.482 8.594 42.455 1.00 26.38 C ANISOU 3826 CA TYR B 222 3417 3322 3285 28 120 -100 C ATOM 3827 C TYR B 222 118.652 10.043 42.896 1.00 30.67 C ANISOU 3827 C TYR B 222 3941 3852 3860 -2 137 -127 C ATOM 3828 O TYR B 222 119.551 10.348 43.676 1.00 32.03 O ANISOU 3828 O TYR B 222 4080 4053 4038 -22 142 -150 O ATOM 3829 CB TYR B 222 119.536 8.191 41.424 1.00 13.75 C ANISOU 3829 CB TYR B 222 1822 1723 1679 38 135 -78 C ATOM 3830 CG TYR B 222 119.672 6.690 41.361 1.00 19.68 C ANISOU 3830 CG TYR B 222 2579 2502 2398 63 119 -59 C ATOM 3831 CD1 TYR B 222 120.484 6.011 42.262 1.00 15.73 C ANISOU 3831 CD1 TYR B 222 2048 2047 1884 62 109 -70 C ATOM 3832 CD2 TYR B 222 118.948 5.945 40.440 1.00 22.38 C ANISOU 3832 CD2 TYR B 222 2956 2823 2724 88 112 -30 C ATOM 3833 CE1 TYR B 222 120.593 4.633 42.229 1.00 13.43 C ANISOU 3833 CE1 TYR B 222 1760 1779 1564 86 95 -52 C ATOM 3834 CE2 TYR B 222 119.050 4.568 40.398 1.00 20.68 C ANISOU 3834 CE2 TYR B 222 2745 2632 2481 111 99 -13 C ATOM 3835 CZ TYR B 222 119.872 3.918 41.294 1.00 15.79 C ANISOU 3835 CZ TYR B 222 2093 2056 1848 110 91 -24 C ATOM 3836 OH TYR B 222 119.969 2.549 41.250 1.00 19.89 O ANISOU 3836 OH TYR B 222 2617 2599 2342 134 79 -7 O ATOM 3837 N THR B 223 117.778 10.933 42.434 1.00 28.67 N ANISOU 3837 N THR B 223 3708 3556 3629 -8 145 -126 N ATOM 3838 CA THR B 223 117.771 12.280 42.993 1.00 37.29 C ANISOU 3838 CA THR B 223 4780 4635 4752 -37 159 -154 C ATOM 3839 C THR B 223 117.376 12.205 44.470 1.00 34.43 C ANISOU 3839 C THR B 223 4395 4301 4386 -50 144 -184 C ATOM 3840 O THR B 223 118.088 12.735 45.341 1.00 28.95 O ANISOU 3840 O THR B 223 3669 3631 3701 -74 151 -212 O ATOM 3841 CB THR B 223 116.812 13.216 42.232 1.00 30.44 C ANISOU 3841 CB THR B 223 3939 3716 3912 -39 169 -145 C ATOM 3842 OG1 THR B 223 117.162 13.236 40.842 1.00 38.13 O ANISOU 3842 OG1 THR B 223 4937 4664 4886 -27 183 -116 O ATOM 3843 CG2 THR B 223 116.890 14.629 42.786 1.00 33.13 C ANISOU 3843 CG2 THR B 223 4259 4043 4288 -70 188 -175 C ATOM 3844 N PHE B 224 116.283 11.493 44.752 1.00 32.14 N ANISOU 3844 N PHE B 224 4121 4009 4079 -33 122 -177 N ATOM 3845 CA PHE B 224 115.856 11.289 46.138 1.00 21.57 C ANISOU 3845 CA PHE B 224 2766 2698 2734 -44 106 -204 C ATOM 3846 C PHE B 224 116.950 10.632 46.979 1.00 32.66 C ANISOU 3846 C PHE B 224 4140 4155 4115 -49 98 -216 C ATOM 3847 O PHE B 224 117.335 11.140 48.053 1.00 26.30 O ANISOU 3847 O PHE B 224 3304 3372 3316 -74 101 -246 O ATOM 3848 CB PHE B 224 114.601 10.415 46.194 1.00 32.45 C ANISOU 3848 CB PHE B 224 4169 4068 4094 -21 84 -191 C ATOM 3849 CG PHE B 224 113.319 11.170 46.011 1.00 39.69 C ANISOU 3849 CG PHE B 224 5104 4940 5036 -24 86 -194 C ATOM 3850 CD1 PHE B 224 112.826 11.977 47.022 1.00 63.49 C ANISOU 3850 CD1 PHE B 224 8102 7950 8070 -49 89 -226 C ATOM 3851 CD2 PHE B 224 112.591 11.051 44.840 1.00 35.68 C ANISOU 3851 CD2 PHE B 224 4630 4395 4531 -3 84 -165 C ATOM 3852 CE1 PHE B 224 111.639 12.666 46.860 1.00 73.44 C ANISOU 3852 CE1 PHE B 224 9379 9169 9357 -52 91 -229 C ATOM 3853 CE2 PHE B 224 111.404 11.736 44.674 1.00 50.67 C ANISOU 3853 CE2 PHE B 224 6545 6252 6455 -6 85 -167 C ATOM 3854 CZ PHE B 224 110.927 12.545 45.684 1.00 62.41 C ANISOU 3854 CZ PHE B 224 8014 7734 7964 -30 88 -199 C ATOM 3855 N ILE B 225 117.473 9.520 46.462 1.00 30.08 N ANISOU 3855 N ILE B 225 3820 3846 3763 -25 90 -191 N ATOM 3856 CA ILE B 225 118.460 8.736 47.200 1.00 33.67 C ANISOU 3856 CA ILE B 225 4247 4350 4195 -25 80 -197 C ATOM 3857 C ILE B 225 119.726 9.535 47.501 1.00 27.77 C ANISOU 3857 C ILE B 225 3467 3621 3465 -51 97 -217 C ATOM 3858 O ILE B 225 120.179 9.578 48.645 1.00 27.70 O ANISOU 3858 O ILE B 225 3428 3647 3450 -69 90 -242 O ATOM 3859 CB ILE B 225 118.858 7.455 46.433 1.00 23.56 C ANISOU 3859 CB ILE B 225 2981 3082 2889 5 72 -165 C ATOM 3860 CG1 ILE B 225 117.657 6.521 46.279 1.00 17.65 C ANISOU 3860 CG1 ILE B 225 2261 2323 2120 31 53 -147 C ATOM 3861 CG2 ILE B 225 120.002 6.738 47.138 1.00 16.29 C ANISOU 3861 CG2 ILE B 225 2028 2210 1949 4 64 -171 C ATOM 3862 CD1 ILE B 225 117.959 5.272 45.473 1.00 17.46 C ANISOU 3862 CD1 ILE B 225 2253 2308 2073 61 48 -115 C ATOM 3863 N LEU B 226 120.290 10.173 46.479 1.00 28.91 N ANISOU 3863 N LEU B 226 3616 3740 3628 -54 120 -208 N ATOM 3864 CA LEU B 226 121.523 10.932 46.664 1.00 29.45 C ANISOU 3864 CA LEU B 226 3654 3822 3714 -78 138 -226 C ATOM 3865 C LEU B 226 121.330 12.160 47.550 1.00 34.03 C ANISOU 3865 C LEU B 226 4213 4399 4318 -111 148 -262 C ATOM 3866 O LEU B 226 122.238 12.527 48.305 1.00 32.03 O ANISOU 3866 O LEU B 226 3926 4175 4069 -133 152 -286 O ATOM 3867 CB LEU B 226 122.105 11.354 45.311 1.00 22.43 C ANISOU 3867 CB LEU B 226 2778 2903 2841 -74 163 -207 C ATOM 3868 CG LEU B 226 122.589 10.204 44.421 1.00 28.18 C ANISOU 3868 CG LEU B 226 3521 3638 3547 -46 159 -175 C ATOM 3869 CD1 LEU B 226 123.304 10.723 43.181 1.00 44.54 C ANISOU 3869 CD1 LEU B 226 5603 5683 5638 -47 187 -161 C ATOM 3870 CD2 LEU B 226 123.480 9.255 45.203 1.00 24.30 C ANISOU 3870 CD2 LEU B 226 3001 3197 3035 -43 144 -180 C ATOM 3871 N LEU B 227 120.155 12.785 47.484 1.00 29.93 N ANISOU 3871 N LEU B 227 3714 3844 3814 -114 150 -266 N ATOM 3872 CA LEU B 227 119.908 13.921 48.366 1.00 26.29 C ANISOU 3872 CA LEU B 227 3233 3379 3376 -146 160 -300 C ATOM 3873 C LEU B 227 119.894 13.453 49.816 1.00 26.17 C ANISOU 3873 C LEU B 227 3194 3407 3341 -157 140 -325 C ATOM 3874 O LEU B 227 120.528 14.071 50.685 1.00 33.46 O ANISOU 3874 O LEU B 227 4087 4354 4274 -186 146 -355 O ATOM 3875 CB LEU B 227 118.596 14.627 48.018 1.00 23.02 C ANISOU 3875 CB LEU B 227 2845 2917 2985 -147 166 -299 C ATOM 3876 CG LEU B 227 118.621 15.564 46.804 1.00 29.66 C ANISOU 3876 CG LEU B 227 3702 3712 3856 -148 191 -285 C ATOM 3877 CD1 LEU B 227 117.249 16.177 46.556 1.00 31.57 C ANISOU 3877 CD1 LEU B 227 3967 3908 4119 -147 192 -282 C ATOM 3878 CD2 LEU B 227 119.667 16.652 46.979 1.00 27.69 C ANISOU 3878 CD2 LEU B 227 3423 3466 3631 -177 217 -308 C ATOM 3879 N ARG B 228 119.208 12.341 50.075 1.00 29.20 N ANISOU 3879 N ARG B 228 3594 3803 3697 -135 115 -311 N ATOM 3880 CA ARG B 228 119.185 11.808 51.435 1.00 21.87 C ANISOU 3880 CA ARG B 228 2647 2918 2747 -145 94 -332 C ATOM 3881 C ARG B 228 120.570 11.351 51.905 1.00 38.35 C ANISOU 3881 C ARG B 228 4702 5052 4817 -150 89 -337 C ATOM 3882 O ARG B 228 120.932 11.551 53.068 1.00 42.71 O ANISOU 3882 O ARG B 228 5226 5637 5364 -173 83 -365 O ATOM 3883 CB ARG B 228 118.189 10.650 51.539 1.00 20.88 C ANISOU 3883 CB ARG B 228 2546 2794 2594 -118 70 -314 C ATOM 3884 CG ARG B 228 118.444 9.699 52.703 1.00 32.83 C ANISOU 3884 CG ARG B 228 4042 4357 4075 -117 46 -324 C ATOM 3885 CD ARG B 228 118.232 10.363 54.057 1.00 31.46 C ANISOU 3885 CD ARG B 228 3847 4200 3907 -150 45 -362 C ATOM 3886 NE ARG B 228 116.864 10.839 54.205 1.00 39.91 N ANISOU 3886 NE ARG B 228 4938 5236 4992 -155 47 -372 N ATOM 3887 CZ ARG B 228 115.864 10.088 54.648 1.00 49.64 C ANISOU 3887 CZ ARG B 228 6187 6469 6205 -142 29 -369 C ATOM 3888 NH1 ARG B 228 114.643 10.596 54.748 1.00 36.25 N ANISOU 3888 NH1 ARG B 228 4508 4738 4527 -148 33 -380 N ATOM 3889 NH2 ARG B 228 116.086 8.827 54.993 1.00 38.99 N ANISOU 3889 NH2 ARG B 228 4838 5155 4821 -123 7 -356 N ATOM 3890 N THR B 229 121.356 10.776 51.000 1.00 35.91 N ANISOU 3890 N THR B 229 4396 4746 4501 -130 92 -311 N ATOM 3891 CA THR B 229 122.669 10.260 51.376 1.00 35.13 C ANISOU 3891 CA THR B 229 4268 4691 4389 -132 86 -313 C ATOM 3892 C THR B 229 123.635 11.389 51.707 1.00 33.84 C ANISOU 3892 C THR B 229 4072 4536 4249 -165 105 -341 C ATOM 3893 O THR B 229 124.361 11.322 52.699 1.00 36.36 O ANISOU 3893 O THR B 229 4359 4896 4559 -182 96 -361 O ATOM 3894 CB THR B 229 123.285 9.391 50.264 1.00 27.32 C ANISOU 3894 CB THR B 229 3290 3700 3389 -104 87 -278 C ATOM 3895 OG1 THR B 229 122.376 8.344 49.910 1.00 39.73 O ANISOU 3895 OG1 THR B 229 4893 5264 4940 -73 71 -253 O ATOM 3896 CG2 THR B 229 124.586 8.774 50.741 1.00 41.48 C ANISOU 3896 CG2 THR B 229 5051 5540 5170 -105 78 -280 C ATOM 3897 N TRP B 230 123.638 12.426 50.874 1.00 34.80 N ANISOU 3897 N TRP B 230 4202 4618 4401 -174 132 -342 N ATOM 3898 CA TRP B 230 124.479 13.591 51.117 1.00 30.06 C ANISOU 3898 CA TRP B 230 3573 4020 3827 -205 154 -369 C ATOM 3899 C TRP B 230 124.049 14.360 52.365 1.00 44.22 C ANISOU 3899 C TRP B 230 5349 5825 5629 -236 153 -407 C ATOM 3900 O TRP B 230 124.888 14.917 53.077 1.00 27.59 O ANISOU 3900 O TRP B 230 3208 3744 3530 -263 160 -434 O ATOM 3901 CB TRP B 230 124.462 14.524 49.899 1.00 36.57 C ANISOU 3901 CB TRP B 230 4415 4796 4683 -206 184 -360 C ATOM 3902 CG TRP B 230 124.932 15.921 50.197 1.00 46.42 C ANISOU 3902 CG TRP B 230 5639 6036 5963 -240 210 -391 C ATOM 3903 CD1 TRP B 230 126.224 16.360 50.244 1.00 46.12 C ANISOU 3903 CD1 TRP B 230 5571 6016 5938 -257 226 -406 C ATOM 3904 CD2 TRP B 230 124.111 17.060 50.487 1.00 46.50 C ANISOU 3904 CD2 TRP B 230 5652 6017 5999 -262 224 -413 C ATOM 3905 NE1 TRP B 230 126.257 17.701 50.549 1.00 54.40 N ANISOU 3905 NE1 TRP B 230 6604 7048 7016 -288 249 -435 N ATOM 3906 CE2 TRP B 230 124.973 18.153 50.703 1.00 45.77 C ANISOU 3906 CE2 TRP B 230 5531 5926 5932 -292 249 -440 C ATOM 3907 CE3 TRP B 230 122.731 17.260 50.587 1.00 43.23 C ANISOU 3907 CE3 TRP B 230 5262 5575 5590 -259 219 -412 C ATOM 3908 CZ2 TRP B 230 124.500 19.428 51.012 1.00 55.74 C ANISOU 3908 CZ2 TRP B 230 6788 7164 7226 -319 269 -466 C ATOM 3909 CZ3 TRP B 230 122.263 18.526 50.894 1.00 50.80 C ANISOU 3909 CZ3 TRP B 230 6214 6507 6580 -286 239 -438 C ATOM 3910 CH2 TRP B 230 123.145 19.593 51.103 1.00 41.18 C ANISOU 3910 CH2 TRP B 230 4968 5293 5387 -316 264 -464 C ATOM 3911 N SER B 231 122.746 14.372 52.641 1.00 47.68 N ANISOU 3911 N SER B 231 5808 6243 6064 -234 145 -408 N ATOM 3912 CA SER B 231 122.223 15.200 53.728 1.00 34.07 C ANISOU 3912 CA SER B 231 4070 4521 4352 -265 148 -444 C ATOM 3913 C SER B 231 122.409 14.619 55.133 1.00 43.65 C ANISOU 3913 C SER B 231 5261 5786 5537 -277 124 -465 C ATOM 3914 O SER B 231 122.736 15.348 56.072 1.00 41.59 O ANISOU 3914 O SER B 231 4974 5543 5285 -310 130 -499 O ATOM 3915 CB SER B 231 120.738 15.474 53.503 1.00 27.34 C ANISOU 3915 CB SER B 231 3249 3627 3512 -259 149 -440 C ATOM 3916 OG SER B 231 120.208 16.230 54.574 1.00 62.90 O ANISOU 3916 OG SER B 231 7739 8132 8026 -289 153 -475 O ATOM 3917 N ALA B 232 122.193 13.315 55.280 1.00 43.85 N ANISOU 3917 N ALA B 232 5299 5834 5530 -251 97 -444 N ATOM 3918 CA ALA B 232 122.216 12.688 56.601 1.00 38.10 C ANISOU 3918 CA ALA B 232 4554 5151 4772 -261 72 -460 C ATOM 3919 C ALA B 232 123.492 11.890 56.845 1.00 37.30 C ANISOU 3919 C ALA B 232 4428 5096 4648 -254 57 -452 C ATOM 3920 O ALA B 232 123.845 11.006 56.065 1.00 34.42 O ANISOU 3920 O ALA B 232 4072 4733 4272 -224 51 -421 O ATOM 3921 CB ALA B 232 120.998 11.791 56.776 1.00 28.13 C ANISOU 3921 CB ALA B 232 3320 3881 3487 -239 52 -446 C ATOM 3922 N ARG B 233 124.179 12.214 57.936 1.00 31.21 N ANISOU 3922 N ARG B 233 3623 4363 3872 -283 53 -481 N ATOM 3923 CA ARG B 233 125.384 11.498 58.332 1.00 23.77 C ANISOU 3923 CA ARG B 233 2653 3468 2909 -280 36 -477 C ATOM 3924 C ARG B 233 125.093 10.053 58.749 1.00 34.53 C ANISOU 3924 C ARG B 233 4026 4859 4234 -255 4 -456 C ATOM 3925 O ARG B 233 125.919 9.165 58.539 1.00 37.73 O ANISOU 3925 O ARG B 233 4422 5291 4625 -236 -9 -435 O ATOM 3926 CB ARG B 233 126.078 12.241 59.474 1.00 23.84 C ANISOU 3926 CB ARG B 233 2626 3512 2922 -320 37 -515 C ATOM 3927 CG ARG B 233 127.486 11.760 59.773 1.00 62.55 C ANISOU 3927 CG ARG B 233 7495 8460 7813 -321 24 -514 C ATOM 3928 CD ARG B 233 128.480 12.285 58.751 1.00 28.41 C ANISOU 3928 CD ARG B 233 3159 4120 3518 -319 48 -507 C ATOM 3929 NE ARG B 233 129.825 11.770 58.989 1.00 51.98 N ANISOU 3929 NE ARG B 233 6111 7146 6493 -318 35 -504 N ATOM 3930 CZ ARG B 233 130.361 10.754 58.321 1.00 48.91 C ANISOU 3930 CZ ARG B 233 5725 6764 6094 -287 26 -472 C ATOM 3931 NH1 ARG B 233 131.592 10.347 58.600 1.00 71.66 N ANISOU 3931 NH1 ARG B 233 8574 9683 8971 -289 15 -471 N ATOM 3932 NH2 ARG B 233 129.666 10.151 57.368 1.00 63.77 N ANISOU 3932 NH2 ARG B 233 7643 8615 7973 -256 28 -440 N ATOM 3933 N GLU B 234 123.920 9.821 59.332 1.00 32.26 N ANISOU 3933 N GLU B 234 3759 4566 3932 -254 -8 -461 N ATOM 3934 CA GLU B 234 123.541 8.483 59.785 1.00 32.39 C ANISOU 3934 CA GLU B 234 3787 4608 3913 -231 -37 -443 C ATOM 3935 C GLU B 234 123.344 7.499 58.628 1.00 31.82 C ANISOU 3935 C GLU B 234 3740 4516 3834 -189 -40 -402 C ATOM 3936 O GLU B 234 123.584 6.300 58.778 1.00 32.84 O ANISOU 3936 O GLU B 234 3870 4673 3936 -166 -61 -382 O ATOM 3937 CB GLU B 234 122.270 8.546 60.635 1.00 26.23 C ANISOU 3937 CB GLU B 234 3024 3821 3121 -242 -45 -461 C ATOM 3938 CG GLU B 234 122.320 9.576 61.754 1.00 55.44 C ANISOU 3938 CG GLU B 234 6701 7535 6829 -286 -38 -503 C ATOM 3939 CD GLU B 234 123.566 9.461 62.619 1.00 41.81 C ANISOU 3939 CD GLU B 234 4937 5861 5087 -305 -52 -517 C ATOM 3940 OE1 GLU B 234 123.966 8.328 62.955 1.00 38.91 O ANISOU 3940 OE1 GLU B 234 4566 5530 4690 -287 -78 -499 O ATOM 3941 OE2 GLU B 234 124.148 10.510 62.968 1.00 41.05 O ANISOU 3941 OE2 GLU B 234 4816 5771 5009 -338 -37 -546 O ATOM 3942 N THR B 235 122.905 8.002 57.476 1.00 25.13 N ANISOU 3942 N THR B 235 2915 3622 3011 -179 -18 -391 N ATOM 3943 CA THR B 235 122.760 7.155 56.296 1.00 27.10 C ANISOU 3943 CA THR B 235 3190 3852 3256 -141 -19 -353 C ATOM 3944 C THR B 235 123.990 7.287 55.399 1.00 30.68 C ANISOU 3944 C THR B 235 3629 4305 3725 -136 -4 -339 C ATOM 3945 O THR B 235 124.357 8.388 54.990 1.00 31.27 O ANISOU 3945 O THR B 235 3695 4358 3827 -155 20 -352 O ATOM 3946 CB THR B 235 121.481 7.494 55.496 1.00 37.98 C ANISOU 3946 CB THR B 235 4605 5177 4649 -130 -7 -343 C ATOM 3947 OG1 THR B 235 121.548 8.840 55.011 1.00 51.48 O ANISOU 3947 OG1 THR B 235 6312 6855 6394 -151 20 -358 O ATOM 3948 CG2 THR B 235 120.244 7.333 56.373 1.00 44.76 C ANISOU 3948 CG2 THR B 235 5478 6035 5494 -134 -21 -357 C ATOM 3949 N ARG B 236 124.630 6.159 55.105 1.00 23.47 N ANISOU 3949 N ARG B 236 2711 3413 2792 -112 -16 -314 N ATOM 3950 CA ARG B 236 125.878 6.172 54.351 1.00 38.43 C ANISOU 3950 CA ARG B 236 4589 5311 4700 -108 -3 -302 C ATOM 3951 C ARG B 236 125.707 5.799 52.885 1.00 31.97 C ANISOU 3951 C ARG B 236 3801 4458 3890 -79 11 -270 C ATOM 3952 O ARG B 236 124.713 5.185 52.496 1.00 39.93 O ANISOU 3952 O ARG B 236 4840 5447 4885 -57 4 -251 O ATOM 3953 CB ARG B 236 126.895 5.227 54.990 1.00 35.99 C ANISOU 3953 CB ARG B 236 4251 5052 4371 -102 -24 -296 C ATOM 3954 CG ARG B 236 126.836 3.802 54.473 1.00 33.09 C ANISOU 3954 CG ARG B 236 3900 4691 3982 -65 -38 -261 C ATOM 3955 CD ARG B 236 128.202 3.147 54.562 1.00 33.12 C ANISOU 3955 CD ARG B 236 3873 4731 3982 -59 -45 -251 C ATOM 3956 NE ARG B 236 128.827 3.387 55.858 1.00 54.33 N ANISOU 3956 NE ARG B 236 6523 7459 6662 -84 -61 -277 N ATOM 3957 CZ ARG B 236 128.576 2.670 56.946 1.00 46.42 C ANISOU 3957 CZ ARG B 236 5513 6492 5631 -83 -89 -279 C ATOM 3958 NH1 ARG B 236 127.709 1.669 56.892 1.00 48.63 N ANISOU 3958 NH1 ARG B 236 5821 6769 5889 -57 -103 -258 N ATOM 3959 NH2 ARG B 236 129.188 2.953 58.088 1.00 56.70 N ANISOU 3959 NH2 ARG B 236 6783 7833 6927 -108 -103 -303 N ATOM 3960 N SER B 237 126.694 6.180 52.081 1.00 40.05 N ANISOU 3960 N SER B 237 4813 5472 4933 -82 31 -264 N ATOM 3961 CA SER B 237 126.782 5.735 50.698 1.00 27.45 C ANISOU 3961 CA SER B 237 3240 3847 3341 -56 44 -233 C ATOM 3962 C SER B 237 127.600 4.448 50.614 1.00 33.17 C ANISOU 3962 C SER B 237 3953 4603 4048 -34 31 -211 C ATOM 3963 O SER B 237 128.828 4.475 50.707 1.00 46.71 O ANISOU 3963 O SER B 237 5637 6339 5770 -42 35 -216 O ATOM 3964 CB SER B 237 127.405 6.821 49.818 1.00 24.50 C ANISOU 3964 CB SER B 237 2864 3445 3000 -71 75 -238 C ATOM 3965 OG SER B 237 127.367 6.456 48.450 1.00 47.05 O ANISOU 3965 OG SER B 237 5747 6269 5858 -48 89 -208 O ATOM 3966 N THR B 238 126.910 3.324 50.454 1.00 30.72 N ANISOU 3966 N THR B 238 3666 4293 3714 -6 15 -187 N ATOM 3967 CA THR B 238 127.560 2.023 50.320 1.00 34.47 C ANISOU 3967 CA THR B 238 4132 4793 4172 17 4 -163 C ATOM 3968 C THR B 238 128.239 1.881 48.961 1.00 36.85 C ANISOU 3968 C THR B 238 4442 5072 4488 30 27 -141 C ATOM 3969 O THR B 238 127.884 2.571 48.004 1.00 33.77 O ANISOU 3969 O THR B 238 4076 4642 4114 28 48 -137 O ATOM 3970 CB THR B 238 126.562 0.862 50.509 1.00 39.01 C ANISOU 3970 CB THR B 238 4731 5373 4718 44 -17 -145 C ATOM 3971 OG1 THR B 238 125.446 1.033 49.627 1.00 36.50 O ANISOU 3971 OG1 THR B 238 4453 5012 4403 55 -7 -133 O ATOM 3972 CG2 THR B 238 126.063 0.815 51.945 1.00 38.55 C ANISOU 3972 CG2 THR B 238 4661 5344 4642 31 -41 -166 C ATOM 3973 N LYS B 239 129.229 0.996 48.884 1.00 39.89 N ANISOU 3973 N LYS B 239 4807 5481 4867 43 22 -127 N ATOM 3974 CA LYS B 239 129.948 0.763 47.638 1.00 47.28 C ANISOU 3974 CA LYS B 239 5749 6398 5817 55 45 -106 C ATOM 3975 C LYS B 239 128.993 0.261 46.554 1.00 46.88 C ANISOU 3975 C LYS B 239 5744 6313 5757 79 52 -80 C ATOM 3976 O LYS B 239 129.140 0.589 45.367 1.00 53.85 O ANISOU 3976 O LYS B 239 6646 7162 6654 82 76 -68 O ATOM 3977 CB LYS B 239 131.075 -0.248 47.863 1.00 48.85 C ANISOU 3977 CB LYS B 239 5918 6631 6010 66 35 -95 C ATOM 3978 CG LYS B 239 132.255 -0.086 46.930 1.00 52.03 C ANISOU 3978 CG LYS B 239 6309 7023 6437 64 61 -88 C ATOM 3979 CD LYS B 239 132.857 1.297 47.077 1.00 69.13 C ANISOU 3979 CD LYS B 239 8454 9182 8629 33 77 -116 C ATOM 3980 CE LYS B 239 134.019 1.498 46.126 1.00 73.81 C ANISOU 3980 CE LYS B 239 9037 9762 9247 30 105 -111 C ATOM 3981 NZ LYS B 239 134.550 2.886 46.201 1.00 75.65 N ANISOU 3981 NZ LYS B 239 9252 9985 9506 0 124 -139 N ATOM 3982 N THR B 240 127.994 -0.508 46.979 1.00 30.99 N ANISOU 3982 N THR B 240 3748 4307 3720 96 31 -71 N ATOM 3983 CA THR B 240 127.005 -1.049 46.057 1.00 32.05 C ANISOU 3983 CA THR B 240 3924 4411 3843 119 34 -47 C ATOM 3984 C THR B 240 126.213 0.067 45.386 1.00 28.53 C ANISOU 3984 C THR B 240 3506 3921 3412 108 51 -53 C ATOM 3985 O THR B 240 125.896 -0.010 44.198 1.00 34.60 O ANISOU 3985 O THR B 240 4306 4658 4184 121 66 -34 O ATOM 3986 CB THR B 240 126.033 -2.002 46.780 1.00 23.75 C ANISOU 3986 CB THR B 240 2883 3377 2764 137 8 -41 C ATOM 3987 OG1 THR B 240 126.769 -3.093 47.345 1.00 33.91 O ANISOU 3987 OG1 THR B 240 4145 4703 4037 149 -7 -33 O ATOM 3988 CG2 THR B 240 124.995 -2.549 45.814 1.00 23.91 C ANISOU 3988 CG2 THR B 240 2946 3365 2773 160 12 -18 C ATOM 3989 N LEU B 241 125.938 1.127 46.137 1.00 26.02 N ANISOU 3989 N LEU B 241 3178 3604 3105 84 48 -81 N ATOM 3990 CA LEU B 241 125.194 2.251 45.592 1.00 29.46 C ANISOU 3990 CA LEU B 241 3638 3999 3559 72 63 -88 C ATOM 3991 C LEU B 241 125.990 2.965 44.507 1.00 33.44 C ANISOU 3991 C LEU B 241 4143 4477 4086 63 93 -83 C ATOM 3992 O LEU B 241 125.451 3.302 43.454 1.00 26.97 O ANISOU 3992 O LEU B 241 3356 3618 3274 69 107 -69 O ATOM 3993 CB LEU B 241 124.824 3.236 46.699 1.00 12.97 C ANISOU 3993 CB LEU B 241 1532 1916 1479 46 57 -120 C ATOM 3994 CG LEU B 241 124.248 4.568 46.217 1.00 19.18 C ANISOU 3994 CG LEU B 241 2335 2662 2290 29 75 -131 C ATOM 3995 CD1 LEU B 241 122.927 4.354 45.492 1.00 23.79 C ANISOU 3995 CD1 LEU B 241 2962 3211 2868 48 73 -112 C ATOM 3996 CD2 LEU B 241 124.086 5.544 47.371 1.00 18.98 C ANISOU 3996 CD2 LEU B 241 2289 2648 2276 0 72 -166 C ATOM 3997 N LYS B 242 127.278 3.177 44.761 1.00 26.62 N ANISOU 3997 N LYS B 242 3245 3635 3234 50 101 -94 N ATOM 3998 CA LYS B 242 128.127 3.872 43.805 1.00 34.89 C ANISOU 3998 CA LYS B 242 4292 4660 4306 40 130 -93 C ATOM 3999 C LYS B 242 128.261 3.043 42.536 1.00 40.66 C ANISOU 3999 C LYS B 242 5049 5372 5030 63 142 -61 C ATOM 4000 O LYS B 242 128.198 3.572 41.411 1.00 31.92 O ANISOU 4000 O LYS B 242 3966 4228 3935 62 164 -50 O ATOM 4001 CB LYS B 242 129.506 4.147 44.413 1.00 40.85 C ANISOU 4001 CB LYS B 242 5002 5446 5075 21 135 -112 C ATOM 4002 CG LYS B 242 129.467 4.804 45.794 1.00 39.99 C ANISOU 4002 CG LYS B 242 4863 5362 4968 -2 121 -144 C ATOM 4003 CD LYS B 242 130.857 4.885 46.423 1.00 51.64 C ANISOU 4003 CD LYS B 242 6294 6874 6454 -18 121 -161 C ATOM 4004 CE LYS B 242 130.812 5.430 47.850 1.00 37.22 C ANISOU 4004 CE LYS B 242 4438 5077 4626 -42 104 -193 C ATOM 4005 NZ LYS B 242 130.359 6.846 47.917 1.00 44.00 N ANISOU 4005 NZ LYS B 242 5302 5910 5506 -67 121 -217 N ATOM 4006 N VAL B 243 128.395 1.731 42.724 1.00 25.15 N ANISOU 4006 N VAL B 243 3080 3433 3044 84 126 -44 N ATOM 4007 CA VAL B 243 128.524 0.823 41.592 1.00 33.40 C ANISOU 4007 CA VAL B 243 4147 4463 4080 107 136 -14 C ATOM 4008 C VAL B 243 127.268 0.851 40.726 1.00 27.45 C ANISOU 4008 C VAL B 243 3440 3672 3317 120 139 3 C ATOM 4009 O VAL B 243 127.338 0.999 39.494 1.00 30.26 O ANISOU 4009 O VAL B 243 3822 3996 3680 123 160 19 O ATOM 4010 CB VAL B 243 128.792 -0.620 42.059 1.00 34.35 C ANISOU 4010 CB VAL B 243 4254 4620 4180 128 117 -1 C ATOM 4011 CG1 VAL B 243 128.548 -1.603 40.926 1.00 34.20 C ANISOU 4011 CG1 VAL B 243 4265 4582 4148 153 126 30 C ATOM 4012 CG2 VAL B 243 130.209 -0.747 42.588 1.00 26.53 C ANISOU 4012 CG2 VAL B 243 3219 3661 3201 118 119 -11 C ATOM 4013 N VAL B 244 126.116 0.745 41.381 1.00 21.77 N ANISOU 4013 N VAL B 244 2733 2956 2585 125 117 -2 N ATOM 4014 CA VAL B 244 124.852 0.739 40.664 1.00 30.44 C ANISOU 4014 CA VAL B 244 3873 4020 3675 137 116 13 C ATOM 4015 C VAL B 244 124.612 2.073 39.960 1.00 37.56 C ANISOU 4015 C VAL B 244 4792 4881 4598 120 136 8 C ATOM 4016 O VAL B 244 124.108 2.104 38.835 1.00 29.26 O ANISOU 4016 O VAL B 244 3775 3796 3546 129 146 27 O ATOM 4017 CB VAL B 244 123.675 0.430 41.611 1.00 20.35 C ANISOU 4017 CB VAL B 244 2600 2753 2381 144 89 6 C ATOM 4018 CG1 VAL B 244 122.355 0.570 40.884 1.00 30.99 C ANISOU 4018 CG1 VAL B 244 3989 4063 3724 155 88 19 C ATOM 4019 CG2 VAL B 244 123.808 -0.974 42.171 1.00 20.02 C ANISOU 4019 CG2 VAL B 244 2547 2746 2314 164 70 15 C ATOM 4020 N VAL B 245 125.021 3.170 40.591 1.00 25.36 N ANISOU 4020 N VAL B 245 3222 3340 3074 95 142 -19 N ATOM 4021 CA VAL B 245 124.865 4.478 39.966 1.00 30.05 C ANISOU 4021 CA VAL B 245 3830 3897 3692 78 162 -25 C ATOM 4022 C VAL B 245 125.708 4.565 38.695 1.00 24.74 C ANISOU 4022 C VAL B 245 3168 3202 3028 78 190 -8 C ATOM 4023 O VAL B 245 125.242 5.062 37.660 1.00 36.14 O ANISOU 4023 O VAL B 245 4645 4607 4479 79 204 6 O ATOM 4024 CB VAL B 245 125.248 5.622 40.930 1.00 25.49 C ANISOU 4024 CB VAL B 245 3219 3329 3135 49 166 -58 C ATOM 4025 CG1 VAL B 245 125.469 6.919 40.170 1.00 30.54 C ANISOU 4025 CG1 VAL B 245 3869 3933 3803 31 194 -63 C ATOM 4026 CG2 VAL B 245 124.171 5.803 41.983 1.00 30.04 C ANISOU 4026 CG2 VAL B 245 3794 3913 3706 45 144 -75 C ATOM 4027 N ALA B 246 126.930 4.039 38.754 1.00 27.73 N ANISOU 4027 N ALA B 246 3522 3607 3408 79 197 -8 N ATOM 4028 CA ALA B 246 127.790 4.070 37.577 1.00 27.15 C ANISOU 4028 CA ALA B 246 3458 3514 3343 78 224 6 C ATOM 4029 C ALA B 246 127.214 3.223 36.439 1.00 35.59 C ANISOU 4029 C ALA B 246 4568 4562 4394 102 226 38 C ATOM 4030 O ALA B 246 127.234 3.633 35.268 1.00 22.88 O ANISOU 4030 O ALA B 246 2986 2917 2790 100 248 52 O ATOM 4031 CB ALA B 246 129.190 3.598 37.931 1.00 32.52 C ANISOU 4031 CB ALA B 246 4100 4227 4029 75 230 0 C ATOM 4032 N VAL B 247 126.664 2.062 36.786 1.00 26.11 N ANISOU 4032 N VAL B 247 3372 3381 3169 123 204 50 N ATOM 4033 CA VAL B 247 126.083 1.195 35.764 1.00 24.93 C ANISOU 4033 CA VAL B 247 3259 3212 2999 145 205 79 C ATOM 4034 C VAL B 247 124.863 1.851 35.111 1.00 30.13 C ANISOU 4034 C VAL B 247 3959 3832 3658 145 204 88 C ATOM 4035 O VAL B 247 124.706 1.842 33.875 1.00 34.81 O ANISOU 4035 O VAL B 247 4585 4394 4248 150 219 108 O ATOM 4036 CB VAL B 247 125.681 -0.169 36.355 1.00 28.18 C ANISOU 4036 CB VAL B 247 3667 3654 3386 167 180 88 C ATOM 4037 CG1 VAL B 247 124.945 -1.003 35.322 1.00 25.68 C ANISOU 4037 CG1 VAL B 247 3390 3316 3049 189 181 116 C ATOM 4038 CG2 VAL B 247 126.909 -0.905 36.869 1.00 26.99 C ANISOU 4038 CG2 VAL B 247 3479 3540 3236 169 181 84 C ATOM 4039 N VAL B 248 124.021 2.450 35.950 1.00 29.78 N ANISOU 4039 N VAL B 248 3910 3788 3618 138 187 71 N ATOM 4040 CA VAL B 248 122.809 3.102 35.476 1.00 27.81 C ANISOU 4040 CA VAL B 248 3694 3502 3371 139 184 77 C ATOM 4041 C VAL B 248 123.144 4.272 34.558 1.00 32.49 C ANISOU 4041 C VAL B 248 4300 4059 3986 122 210 79 C ATOM 4042 O VAL B 248 122.488 4.470 33.533 1.00 26.41 O ANISOU 4042 O VAL B 248 3567 3253 3213 127 216 98 O ATOM 4043 CB VAL B 248 121.939 3.592 36.657 1.00 22.32 C ANISOU 4043 CB VAL B 248 2985 2813 2680 131 163 55 C ATOM 4044 CG1 VAL B 248 120.858 4.550 36.181 1.00 17.04 C ANISOU 4044 CG1 VAL B 248 2345 2103 2025 126 164 58 C ATOM 4045 CG2 VAL B 248 121.320 2.408 37.384 1.00 24.00 C ANISOU 4045 CG2 VAL B 248 3196 3054 2869 151 137 58 C ATOM 4046 N ALA B 249 124.191 5.019 34.895 1.00 26.79 N ANISOU 4046 N ALA B 249 3549 3345 3285 101 227 59 N ATOM 4047 CA ALA B 249 124.609 6.115 34.030 1.00 29.24 C ANISOU 4047 CA ALA B 249 3870 3622 3617 84 254 60 C ATOM 4048 C ALA B 249 125.145 5.585 32.700 1.00 28.51 C ANISOU 4048 C ALA B 249 3803 3514 3516 93 274 86 C ATOM 4049 O ALA B 249 124.835 6.127 31.624 1.00 24.86 O ANISOU 4049 O ALA B 249 3375 3014 3058 91 289 101 O ATOM 4050 CB ALA B 249 125.657 6.968 34.726 1.00 19.46 C ANISOU 4050 CB ALA B 249 2592 2398 2403 60 268 32 C ATOM 4051 N SER B 250 125.914 4.499 32.773 1.00 27.06 N ANISOU 4051 N SER B 250 3604 3357 3319 104 274 91 N ATOM 4052 CA SER B 250 126.532 3.946 31.572 1.00 27.65 C ANISOU 4052 CA SER B 250 3699 3419 3387 111 295 113 C ATOM 4053 C SER B 250 125.473 3.475 30.587 1.00 29.38 C ANISOU 4053 C SER B 250 3966 3612 3585 128 289 141 C ATOM 4054 O SER B 250 125.652 3.592 29.369 1.00 35.18 O ANISOU 4054 O SER B 250 4731 4319 4319 126 310 159 O ATOM 4055 CB SER B 250 127.469 2.788 31.920 1.00 25.02 C ANISOU 4055 CB SER B 250 3340 3123 3045 120 294 114 C ATOM 4056 OG SER B 250 126.739 1.648 32.339 1.00 31.34 O ANISOU 4056 OG SER B 250 4144 3943 3821 142 268 124 O ATOM 4057 N PHE B 251 124.353 2.987 31.121 1.00 26.75 N ANISOU 4057 N PHE B 251 3640 3287 3236 142 261 144 N ATOM 4058 CA PHE B 251 123.258 2.520 30.273 1.00 29.24 C ANISOU 4058 CA PHE B 251 3999 3580 3532 159 252 169 C ATOM 4059 C PHE B 251 122.813 3.605 29.295 1.00 30.73 C ANISOU 4059 C PHE B 251 4220 3723 3731 148 266 178 C ATOM 4060 O PHE B 251 122.827 3.408 28.072 1.00 31.92 O ANISOU 4060 O PHE B 251 4406 3851 3873 152 280 201 O ATOM 4061 CB PHE B 251 122.071 2.076 31.141 1.00 26.39 C ANISOU 4061 CB PHE B 251 3637 3232 3157 173 220 164 C ATOM 4062 CG PHE B 251 120.843 1.679 30.358 1.00 18.25 C ANISOU 4062 CG PHE B 251 2649 2176 2108 189 208 187 C ATOM 4063 CD1 PHE B 251 120.660 0.368 29.952 1.00 23.87 C ANISOU 4063 CD1 PHE B 251 3376 2899 2795 210 203 206 C ATOM 4064 CD2 PHE B 251 119.859 2.612 30.055 1.00 21.99 C ANISOU 4064 CD2 PHE B 251 3146 2617 2592 184 203 190 C ATOM 4065 CE1 PHE B 251 119.529 -0.005 29.243 1.00 20.64 C ANISOU 4065 CE1 PHE B 251 3004 2468 2368 225 191 225 C ATOM 4066 CE2 PHE B 251 118.728 2.245 29.343 1.00 16.17 C ANISOU 4066 CE2 PHE B 251 2447 1858 1839 199 191 210 C ATOM 4067 CZ PHE B 251 118.564 0.935 28.940 1.00 10.96 C ANISOU 4067 CZ PHE B 251 1795 1213 1157 216 182 222 C ATOM 4068 N PHE B 252 122.443 4.758 29.838 1.00 29.09 N ANISOU 4068 N PHE B 252 4003 3504 3544 134 262 161 N ATOM 4069 CA PHE B 252 121.959 5.852 29.012 1.00 41.45 C ANISOU 4069 CA PHE B 252 5599 5028 5124 123 273 169 C ATOM 4070 C PHE B 252 123.062 6.456 28.159 1.00 27.16 C ANISOU 4070 C PHE B 252 3793 3201 3327 108 307 173 C ATOM 4071 O PHE B 252 122.822 6.828 27.000 1.00 27.65 O ANISOU 4071 O PHE B 252 3891 3227 3387 106 319 192 O ATOM 4072 CB PHE B 252 121.314 6.924 29.885 1.00 30.43 C ANISOU 4072 CB PHE B 252 4187 3625 3750 111 262 149 C ATOM 4073 CG PHE B 252 120.141 6.423 30.669 1.00 23.40 C ANISOU 4073 CG PHE B 252 3297 2747 2848 125 231 145 C ATOM 4074 CD1 PHE B 252 118.934 6.165 30.040 1.00 21.36 C ANISOU 4074 CD1 PHE B 252 3075 2463 2576 140 216 166 C ATOM 4075 CD2 PHE B 252 120.246 6.196 32.031 1.00 25.21 C ANISOU 4075 CD2 PHE B 252 3489 3010 3079 123 216 121 C ATOM 4076 CE1 PHE B 252 117.851 5.697 30.756 1.00 27.61 C ANISOU 4076 CE1 PHE B 252 3866 3264 3359 153 188 162 C ATOM 4077 CE2 PHE B 252 119.166 5.729 32.754 1.00 19.97 C ANISOU 4077 CE2 PHE B 252 2826 2356 2405 136 189 117 C ATOM 4078 CZ PHE B 252 117.968 5.478 32.115 1.00 28.13 C ANISOU 4078 CZ PHE B 252 3896 3365 3427 151 175 137 C ATOM 4079 N ILE B 253 124.272 6.526 28.713 1.00 27.18 N ANISOU 4079 N ILE B 253 3757 3226 3342 96 321 153 N ATOM 4080 CA ILE B 253 125.367 7.132 27.967 1.00 34.86 C ANISOU 4080 CA ILE B 253 4731 4183 4330 80 354 153 C ATOM 4081 C ILE B 253 125.642 6.346 26.693 1.00 40.52 C ANISOU 4081 C ILE B 253 5481 4886 5028 90 369 180 C ATOM 4082 O ILE B 253 125.811 6.930 25.623 1.00 35.93 O ANISOU 4082 O ILE B 253 4928 4272 4451 81 392 193 O ATOM 4083 CB ILE B 253 126.669 7.216 28.797 1.00 32.61 C ANISOU 4083 CB ILE B 253 4399 3929 4063 67 366 127 C ATOM 4084 CG1 ILE B 253 126.522 8.236 29.927 1.00 32.47 C ANISOU 4084 CG1 ILE B 253 4350 3919 4067 51 359 98 C ATOM 4085 CG2 ILE B 253 127.843 7.606 27.909 1.00 29.23 C ANISOU 4085 CG2 ILE B 253 3974 3485 3648 53 402 129 C ATOM 4086 CD1 ILE B 253 127.744 8.335 30.824 1.00 27.94 C ANISOU 4086 CD1 ILE B 253 3727 3378 3509 38 367 72 C ATOM 4087 N PHE B 254 125.654 5.021 26.792 1.00 31.31 N ANISOU 4087 N PHE B 254 4312 3745 3839 108 357 189 N ATOM 4088 CA PHE B 254 125.965 4.230 25.610 1.00 27.82 C ANISOU 4088 CA PHE B 254 3900 3292 3379 115 373 213 C ATOM 4089 C PHE B 254 124.745 3.885 24.757 1.00 35.00 C ANISOU 4089 C PHE B 254 4856 4177 4264 129 360 240 C ATOM 4090 O PHE B 254 124.901 3.448 23.616 1.00 31.37 O ANISOU 4090 O PHE B 254 4428 3701 3790 132 376 261 O ATOM 4091 CB PHE B 254 126.710 2.960 26.012 1.00 19.17 C ANISOU 4091 CB PHE B 254 2779 2233 2273 127 372 212 C ATOM 4092 CG PHE B 254 128.079 3.223 26.564 1.00 37.30 C ANISOU 4092 CG PHE B 254 5032 4548 4591 113 390 190 C ATOM 4093 CD1 PHE B 254 129.091 3.694 25.743 1.00 40.93 C ANISOU 4093 CD1 PHE B 254 5497 4989 5066 97 424 190 C ATOM 4094 CD2 PHE B 254 128.354 3.013 27.904 1.00 43.37 C ANISOU 4094 CD2 PHE B 254 5756 5354 5367 114 372 169 C ATOM 4095 CE1 PHE B 254 130.352 3.947 26.248 1.00 37.11 C ANISOU 4095 CE1 PHE B 254 4973 4522 4605 84 440 169 C ATOM 4096 CE2 PHE B 254 129.613 3.262 28.415 1.00 38.73 C ANISOU 4096 CE2 PHE B 254 5129 4786 4801 100 387 149 C ATOM 4097 CZ PHE B 254 130.614 3.730 27.585 1.00 44.85 C ANISOU 4097 CZ PHE B 254 5908 5541 5592 86 421 149 C ATOM 4098 N TRP B 255 123.538 4.076 25.285 1.00 36.27 N ANISOU 4098 N TRP B 255 5023 4336 4423 137 332 239 N ATOM 4099 CA TRP B 255 122.351 3.863 24.455 1.00 25.54 C ANISOU 4099 CA TRP B 255 3704 2953 3045 149 317 260 C ATOM 4100 C TRP B 255 121.870 5.116 23.722 1.00 29.96 C ANISOU 4100 C TRP B 255 4282 3480 3622 134 318 260 C ATOM 4101 O TRP B 255 121.054 5.014 22.804 1.00 29.04 O ANISOU 4101 O TRP B 255 4172 3361 3501 135 295 258 O ATOM 4102 CB TRP B 255 121.202 3.294 25.288 1.00 23.60 C ANISOU 4102 CB TRP B 255 3448 2727 2790 165 280 253 C ATOM 4103 CG TRP B 255 121.269 1.805 25.454 1.00 24.57 C ANISOU 4103 CG TRP B 255 3554 2886 2897 180 264 250 C ATOM 4104 CD1 TRP B 255 121.542 1.121 26.602 1.00 24.07 C ANISOU 4104 CD1 TRP B 255 3472 2851 2822 193 261 248 C ATOM 4105 CD2 TRP B 255 121.068 0.815 24.436 1.00 28.36 C ANISOU 4105 CD2 TRP B 255 4030 3375 3370 183 251 246 C ATOM 4106 NE1 TRP B 255 121.518 -0.231 26.365 1.00 32.07 N ANISOU 4106 NE1 TRP B 255 4471 3890 3826 203 245 244 N ATOM 4107 CE2 TRP B 255 121.230 -0.446 25.043 1.00 20.27 C ANISOU 4107 CE2 TRP B 255 2985 2382 2335 196 241 242 C ATOM 4108 CE3 TRP B 255 120.764 0.873 23.072 1.00 26.03 C ANISOU 4108 CE3 TRP B 255 3746 3066 3078 174 247 246 C ATOM 4109 CZ2 TRP B 255 121.101 -1.638 24.334 1.00 22.29 C ANISOU 4109 CZ2 TRP B 255 3231 2650 2587 200 229 237 C ATOM 4110 CZ3 TRP B 255 120.634 -0.313 22.370 1.00 21.07 C ANISOU 4110 CZ3 TRP B 255 3109 2453 2442 178 236 242 C ATOM 4111 CH2 TRP B 255 120.803 -1.551 23.002 1.00 22.12 C ANISOU 4111 CH2 TRP B 255 3223 2614 2569 190 228 237 C ATOM 4112 N LEU B 256 122.366 6.291 24.108 1.00 28.15 N ANISOU 4112 N LEU B 256 4047 3232 3415 118 340 253 N ATOM 4113 CA LEU B 256 121.871 7.535 23.509 1.00 27.51 C ANISOU 4113 CA LEU B 256 3990 3113 3351 105 346 259 C ATOM 4114 C LEU B 256 122.006 7.651 21.969 1.00 29.98 C ANISOU 4114 C LEU B 256 4315 3417 3659 99 348 263 C ATOM 4115 O LEU B 256 121.009 7.939 21.285 1.00 37.33 O ANISOU 4115 O LEU B 256 5253 4342 4588 99 322 264 O ATOM 4116 CB LEU B 256 122.567 8.733 24.172 1.00 28.80 C ANISOU 4116 CB LEU B 256 4122 3273 3547 84 363 234 C ATOM 4117 CG LEU B 256 122.184 10.139 23.713 1.00 31.23 C ANISOU 4117 CG LEU B 256 4448 3541 3877 70 373 237 C ATOM 4118 CD1 LEU B 256 120.732 10.432 24.049 1.00 27.54 C ANISOU 4118 CD1 LEU B 256 3992 3061 3412 78 344 241 C ATOM 4119 CD2 LEU B 256 123.100 11.175 24.348 1.00 17.37 C ANISOU 4119 CD2 LEU B 256 2657 1790 2154 48 395 209 C ATOM 4120 N PRO B 257 123.224 7.441 21.415 1.00 41.14 N ANISOU 4120 N PRO B 257 5730 4829 5071 91 378 266 N ATOM 4121 CA PRO B 257 123.321 7.603 19.955 1.00 33.69 C ANISOU 4121 CA PRO B 257 4802 3876 4124 84 380 269 C ATOM 4122 C PRO B 257 122.433 6.662 19.133 1.00 27.89 C ANISOU 4122 C PRO B 257 4069 3160 3368 96 345 271 C ATOM 4123 O PRO B 257 121.860 7.084 18.120 1.00 37.22 O ANISOU 4123 O PRO B 257 5261 4331 4549 91 333 274 O ATOM 4124 CB PRO B 257 124.805 7.321 19.670 1.00 36.04 C ANISOU 4124 CB PRO B 257 5098 4174 4423 76 418 270 C ATOM 4125 CG PRO B 257 125.289 6.548 20.833 1.00 41.11 C ANISOU 4125 CG PRO B 257 5722 4838 5062 84 426 268 C ATOM 4126 CD PRO B 257 124.512 7.036 22.008 1.00 36.58 C ANISOU 4126 CD PRO B 257 5141 4261 4496 87 412 266 C ATOM 4127 N TYR B 258 122.281 5.423 19.594 1.00 34.23 N ANISOU 4127 N TYR B 258 4859 3990 4158 110 330 268 N ATOM 4128 CA TYR B 258 121.497 4.432 18.863 1.00 35.50 C ANISOU 4128 CA TYR B 258 5017 4168 4304 118 300 266 C ATOM 4129 C TYR B 258 120.023 4.800 18.849 1.00 35.34 C ANISOU 4129 C TYR B 258 4995 4147 4285 120 267 265 C ATOM 4130 O TYR B 258 119.319 4.566 17.866 1.00 36.16 O ANISOU 4130 O TYR B 258 5102 4253 4384 119 249 266 O ATOM 4131 CB TYR B 258 121.688 3.039 19.473 1.00 39.29 C ANISOU 4131 CB TYR B 258 5480 4677 4773 132 293 262 C ATOM 4132 CG TYR B 258 120.818 1.964 18.856 1.00 48.15 C ANISOU 4132 CG TYR B 258 6595 5818 5884 139 265 257 C ATOM 4133 CD1 TYR B 258 121.221 1.287 17.713 1.00 55.91 C ANISOU 4133 CD1 TYR B 258 7582 6802 6859 136 271 258 C ATOM 4134 CD2 TYR B 258 119.595 1.620 19.423 1.00 53.60 C ANISOU 4134 CD2 TYR B 258 7272 6520 6572 147 234 250 C ATOM 4135 CE1 TYR B 258 120.431 0.302 17.148 1.00 58.76 C ANISOU 4135 CE1 TYR B 258 7936 7179 7213 140 248 254 C ATOM 4136 CE2 TYR B 258 118.797 0.637 18.865 1.00 56.41 C ANISOU 4136 CE2 TYR B 258 7619 6892 6922 151 211 245 C ATOM 4137 CZ TYR B 258 119.221 -0.019 17.729 1.00 50.82 C ANISOU 4137 CZ TYR B 258 6916 6185 6208 147 219 247 C ATOM 4138 OH TYR B 258 118.434 -0.998 17.167 1.00 62.86 O ANISOU 4138 OH TYR B 258 8431 7724 7728 148 199 241 O ATOM 4139 N GLN B 259 119.566 5.392 19.947 1.00 32.40 N ANISOU 4139 N GLN B 259 4618 3770 3923 123 261 262 N ATOM 4140 CA GLN B 259 118.175 5.790 20.069 1.00 36.21 C ANISOU 4140 CA GLN B 259 5096 4250 4411 124 231 259 C ATOM 4141 C GLN B 259 117.888 7.015 19.213 1.00 33.19 C ANISOU 4141 C GLN B 259 4728 3843 4041 112 233 266 C ATOM 4142 O GLN B 259 116.907 7.041 18.450 1.00 44.56 O ANISOU 4142 O GLN B 259 6167 5283 5479 110 210 269 O ATOM 4143 CB GLN B 259 117.827 6.062 21.537 1.00 30.30 C ANISOU 4143 CB GLN B 259 4339 3503 3672 131 225 253 C ATOM 4144 CG GLN B 259 117.593 4.809 22.372 1.00 16.36 C ANISOU 4144 CG GLN B 259 2557 1767 1893 145 209 246 C ATOM 4145 CD GLN B 259 116.204 4.224 22.174 1.00 27.04 C ANISOU 4145 CD GLN B 259 3898 3133 3242 150 175 239 C ATOM 4146 OE1 GLN B 259 115.675 4.200 21.064 1.00 43.93 O ANISOU 4146 OE1 GLN B 259 6041 5271 5381 145 165 242 O ATOM 4147 NE2 GLN B 259 115.602 3.760 23.259 1.00 42.56 N ANISOU 4147 NE2 GLN B 259 5850 5114 5206 160 159 230 N ATOM 4148 N VAL B 260 118.767 8.011 19.314 1.00 23.56 N ANISOU 4148 N VAL B 260 3518 2600 2834 101 262 269 N ATOM 4149 CA VAL B 260 118.597 9.241 18.545 1.00 40.29 C ANISOU 4149 CA VAL B 260 5649 4694 4967 89 267 276 C ATOM 4150 C VAL B 260 118.598 8.959 17.041 1.00 35.41 C ANISOU 4150 C VAL B 260 5041 4077 4335 85 263 283 C ATOM 4151 O VAL B 260 117.636 9.294 16.325 1.00 43.33 O ANISOU 4151 O VAL B 260 6047 5077 5340 83 241 289 O ATOM 4152 CB VAL B 260 119.706 10.260 18.881 1.00 44.73 C ANISOU 4152 CB VAL B 260 6218 5231 5546 76 305 275 C ATOM 4153 CG1 VAL B 260 119.653 11.448 17.938 1.00 44.78 C ANISOU 4153 CG1 VAL B 260 6236 5212 5564 63 312 281 C ATOM 4154 CG2 VAL B 260 119.587 10.710 20.331 1.00 40.36 C ANISOU 4154 CG2 VAL B 260 5654 4671 5010 77 309 267 C ATOM 4155 N THR B 261 119.650 8.294 16.571 1.00 36.78 N ANISOU 4155 N THR B 261 5220 4257 4497 84 284 283 N ATOM 4156 CA THR B 261 119.736 7.959 15.157 1.00 40.92 C ANISOU 4156 CA THR B 261 5756 4783 5010 80 283 289 C ATOM 4157 C THR B 261 118.600 7.023 14.765 1.00 46.55 C ANISOU 4157 C THR B 261 6460 5517 5711 88 249 288 C ATOM 4158 O THR B 261 118.075 7.092 13.650 1.00 55.40 O ANISOU 4158 O THR B 261 7587 6634 6826 83 237 295 O ATOM 4159 CB THR B 261 121.076 7.300 14.815 1.00 34.36 C ANISOU 4159 CB THR B 261 4929 3955 4170 77 312 287 C ATOM 4160 OG1 THR B 261 121.194 6.066 15.533 1.00 40.81 O ANISOU 4160 OG1 THR B 261 5731 4796 4977 90 306 281 O ATOM 4161 CG2 THR B 261 122.227 8.217 15.195 1.00 32.11 C ANISOU 4161 CG2 THR B 261 4651 3650 3900 67 349 286 C ATOM 4162 N GLY B 262 118.201 6.173 15.708 1.00 42.29 N ANISOU 4162 N GLY B 262 5903 4997 5167 99 234 280 N ATOM 4163 CA GLY B 262 117.170 5.190 15.450 1.00 39.40 C ANISOU 4163 CA GLY B 262 5525 4652 4793 106 206 277 C ATOM 4164 C GLY B 262 115.817 5.788 15.121 1.00 39.05 C ANISOU 4164 C GLY B 262 5479 4602 4757 104 180 281 C ATOM 4165 O GLY B 262 115.185 5.365 14.152 1.00 57.90 O ANISOU 4165 O GLY B 262 7875 6990 7132 106 171 283 O ATOM 4166 N ILE B 263 115.358 6.758 15.912 1.00 39.32 N ANISOU 4166 N ILE B 263 5509 4624 4806 103 175 281 N ATOM 4167 CA ILE B 263 114.093 7.419 15.584 1.00 43.02 C ANISOU 4167 CA ILE B 263 5975 5085 5286 100 151 287 C ATOM 4168 C ILE B 263 114.264 8.369 14.394 1.00 47.13 C ANISOU 4168 C ILE B 263 6512 5584 5810 89 159 300 C ATOM 4169 O ILE B 263 113.339 8.536 13.567 1.00 49.55 O ANISOU 4169 O ILE B 263 6833 5883 6111 91 148 306 O ATOM 4170 CB ILE B 263 113.517 8.181 16.795 1.00 25.70 C ANISOU 4170 CB ILE B 263 3772 2883 3110 102 143 282 C ATOM 4171 CG1 ILE B 263 114.548 9.171 17.342 1.00 38.03 C ANISOU 4171 CG1 ILE B 263 5344 4423 4683 96 170 283 C ATOM 4172 CG2 ILE B 263 113.066 7.191 17.869 1.00 55.36 C ANISOU 4172 CG2 ILE B 263 7510 6662 6862 113 130 270 C ATOM 4173 CD1 ILE B 263 114.086 9.954 18.541 1.00 75.42 C ANISOU 4173 CD1 ILE B 263 10072 9148 9438 97 166 278 C ATOM 4174 N MET B 264 115.455 8.960 14.285 1.00 43.91 N ANISOU 4174 N MET B 264 6119 5161 5404 82 188 303 N ATOM 4175 CA MET B 264 115.723 9.879 13.185 1.00 47.05 C ANISOU 4175 CA MET B 264 6533 5537 5804 71 198 315 C ATOM 4176 C MET B 264 115.591 9.179 11.838 1.00 53.23 C ANISOU 4176 C MET B 264 7328 6329 6570 70 193 321 C ATOM 4177 O MET B 264 115.126 9.770 10.868 1.00 57.57 O ANISOU 4177 O MET B 264 7895 6862 7116 67 190 331 O ATOM 4178 CB MET B 264 117.115 10.489 13.315 1.00 36.87 C ANISOU 4178 CB MET B 264 5259 4232 4520 63 234 314 C ATOM 4179 CG MET B 264 117.191 11.695 14.228 1.00 30.62 C ANISOU 4179 CG MET B 264 4465 3420 3751 59 244 312 C ATOM 4180 SD MET B 264 118.841 12.423 14.197 1.00 59.17 S ANISOU 4180 SD MET B 264 8095 7014 7374 47 291 310 S ATOM 4181 CE MET B 264 118.616 13.820 15.292 1.00 54.41 C ANISOU 4181 CE MET B 264 7484 6387 6802 41 298 306 C ATOM 4182 N MET B 265 115.955 7.902 11.792 1.00 50.01 N ANISOU 4182 N MET B 265 6919 5939 6144 77 198 312 N ATOM 4183 CA MET B 265 115.865 7.150 10.546 1.00 56.22 C ANISOU 4183 CA MET B 265 7727 6726 6907 80 201 314 C ATOM 4184 C MET B 265 114.442 6.658 10.286 1.00 60.05 C ANISOU 4184 C MET B 265 8217 7216 7382 90 177 312 C ATOM 4185 O MET B 265 114.156 6.094 9.229 1.00 76.65 O ANISOU 4185 O MET B 265 10339 9318 9467 92 176 313 O ATOM 4186 CB MET B 265 116.846 5.978 10.553 1.00 42.21 C ANISOU 4186 CB MET B 265 5949 4968 5122 83 216 305 C ATOM 4187 CG MET B 265 118.302 6.417 10.530 1.00 45.97 C ANISOU 4187 CG MET B 265 6424 5437 5606 71 242 308 C ATOM 4188 SD MET B 265 119.464 5.056 10.321 1.00 71.04 S ANISOU 4188 SD MET B 265 9597 8627 8768 74 262 300 S ATOM 4189 CE MET B 265 118.946 3.965 11.643 1.00 69.45 C ANISOU 4189 CE MET B 265 9370 8451 8567 89 244 289 C ATOM 4190 N SER B 266 113.557 6.848 11.260 1.00 57.32 N ANISOU 4190 N SER B 266 7856 6876 7048 96 159 307 N ATOM 4191 CA SER B 266 112.140 6.576 11.051 1.00 70.65 C ANISOU 4191 CA SER B 266 9549 8566 8731 104 136 306 C ATOM 4192 C SER B 266 111.404 7.815 10.555 1.00 66.83 C ANISOU 4192 C SER B 266 9074 8061 8257 98 127 319 C ATOM 4193 O SER B 266 110.407 7.703 9.839 1.00 66.87 O ANISOU 4193 O SER B 266 9091 8062 8253 101 113 323 O ATOM 4194 CB SER B 266 111.489 6.061 12.336 1.00 63.02 C ANISOU 4194 CB SER B 266 8559 7614 7769 114 122 293 C ATOM 4195 OG SER B 266 111.931 4.748 12.635 1.00 78.74 O ANISOU 4195 OG SER B 266 10545 9625 9748 122 127 280 O ATOM 4196 N PHE B 267 111.884 8.996 10.938 1.00 68.28 N ANISOU 4196 N PHE B 267 9251 8231 8462 89 134 327 N ATOM 4197 CA PHE B 267 111.212 10.221 10.495 1.00 71.30 C ANISOU 4197 CA PHE B 267 9641 8592 8858 84 126 340 C ATOM 4198 C PHE B 267 111.835 10.881 9.258 1.00 76.82 C ANISOU 4198 C PHE B 267 10362 9273 9553 73 140 354 C ATOM 4199 O PHE B 267 111.430 11.976 8.868 1.00 68.93 O ANISOU 4199 O PHE B 267 9369 8254 8567 67 136 367 O ATOM 4200 CB PHE B 267 111.145 11.225 11.648 1.00 64.33 C ANISOU 4200 CB PHE B 267 8737 7700 8005 80 123 340 C ATOM 4201 CG PHE B 267 110.085 10.898 12.659 1.00 73.74 C ANISOU 4201 CG PHE B 267 9911 8902 9205 89 102 330 C ATOM 4202 CD1 PHE B 267 110.235 9.813 13.505 1.00 72.39 C ANISOU 4202 CD1 PHE B 267 9727 8754 9025 98 101 315 C ATOM 4203 CD2 PHE B 267 108.933 11.663 12.754 1.00 80.14 C ANISOU 4203 CD2 PHE B 267 10717 9700 10032 90 85 336 C ATOM 4204 CE1 PHE B 267 109.264 9.497 14.430 1.00 73.65 C ANISOU 4204 CE1 PHE B 267 9871 8923 9190 106 84 305 C ATOM 4205 CE2 PHE B 267 107.955 11.352 13.683 1.00 81.05 C ANISOU 4205 CE2 PHE B 267 10817 9825 10155 99 68 326 C ATOM 4206 CZ PHE B 267 108.122 10.268 14.521 1.00 85.63 C ANISOU 4206 CZ PHE B 267 11384 10426 10723 106 68 310 C ATOM 4207 N LEU B 268 112.814 10.222 8.644 1.00 76.56 N ANISOU 4207 N LEU B 268 10342 9246 9502 70 159 352 N ATOM 4208 CA LEU B 268 113.458 10.767 7.446 1.00 54.10 C ANISOU 4208 CA LEU B 268 7519 6385 6651 60 175 364 C ATOM 4209 C LEU B 268 113.114 10.006 6.167 1.00 74.41 C ANISOU 4209 C LEU B 268 10117 8960 9197 62 172 367 C ATOM 4210 O LEU B 268 112.823 8.810 6.202 1.00 67.64 O ANISOU 4210 O LEU B 268 9257 8118 8323 71 165 356 O ATOM 4211 CB LEU B 268 114.976 10.785 7.622 1.00 49.97 C ANISOU 4211 CB LEU B 268 6994 5863 6131 52 202 359 C ATOM 4212 CG LEU B 268 115.551 11.805 8.600 1.00 52.38 C ANISOU 4212 CG LEU B 268 7280 6159 6463 45 211 359 C ATOM 4213 CD1 LEU B 268 117.041 11.574 8.764 1.00 54.15 C ANISOU 4213 CD1 LEU B 268 7501 6387 6687 38 237 352 C ATOM 4214 CD2 LEU B 268 115.271 13.223 8.138 1.00 54.63 C ANISOU 4214 CD2 LEU B 268 7574 6419 6764 36 210 373 C ATOM 4215 N GLU B 269 113.149 10.714 5.041 1.00 82.25 N ANISOU 4215 N GLU B 269 11131 9934 10185 54 176 381 N ATOM 4216 CA GLU B 269 113.034 10.090 3.726 1.00 67.86 C ANISOU 4216 CA GLU B 269 9336 8111 8338 53 178 385 C ATOM 4217 C GLU B 269 114.302 9.306 3.409 1.00 63.72 C ANISOU 4217 C GLU B 269 8818 7594 7800 49 202 376 C ATOM 4218 O GLU B 269 115.404 9.770 3.705 1.00 72.18 O ANISOU 4218 O GLU B 269 9883 8659 8881 42 223 375 O ATOM 4219 CB GLU B 269 112.801 11.140 2.636 1.00 83.53 C ANISOU 4219 CB GLU B 269 11343 10073 10322 43 177 403 C ATOM 4220 CG GLU B 269 111.737 12.185 2.947 1.00 91.53 C ANISOU 4220 CG GLU B 269 12348 11074 11355 45 157 415 C ATOM 4221 CD GLU B 269 110.377 11.831 2.376 1.00109.83 C ANISOU 4221 CD GLU B 269 14675 13393 13662 52 132 421 C ATOM 4222 OE1 GLU B 269 109.564 12.755 2.160 1.00110.68 O ANISOU 4222 OE1 GLU B 269 14785 13487 13783 50 118 436 O ATOM 4223 OE2 GLU B 269 110.117 10.633 2.143 1.00110.43 O ANISOU 4223 OE2 GLU B 269 14756 13484 13717 58 127 411 O ATOM 4224 N PRO B 270 114.154 8.111 2.820 1.00 62.19 N ANISOU 4224 N PRO B 270 8636 7410 7584 54 201 369 N ATOM 4225 CA PRO B 270 115.317 7.298 2.444 1.00 66.92 C ANISOU 4225 CA PRO B 270 9241 8014 8170 50 224 361 C ATOM 4226 C PRO B 270 116.258 8.020 1.482 1.00 71.51 C ANISOU 4226 C PRO B 270 9845 8578 8749 36 247 370 C ATOM 4227 O PRO B 270 117.472 7.820 1.538 1.00 64.79 O ANISOU 4227 O PRO B 270 8991 7727 7899 31 271 364 O ATOM 4228 CB PRO B 270 114.685 6.066 1.780 1.00 80.57 C ANISOU 4228 CB PRO B 270 10983 9753 9877 57 214 355 C ATOM 4229 CG PRO B 270 113.320 5.983 2.378 1.00 60.04 C ANISOU 4229 CG PRO B 270 8370 7160 7282 67 186 353 C ATOM 4230 CD PRO B 270 112.883 7.405 2.584 1.00 65.00 C ANISOU 4230 CD PRO B 270 8995 7773 7927 63 177 367 C ATOM 4231 N SER B 271 115.695 8.853 0.612 1.00 81.63 N ANISOU 4231 N SER B 271 11146 9843 10027 30 239 385 N ATOM 4232 CA SER B 271 116.479 9.599 -0.369 1.00 78.58 C ANISOU 4232 CA SER B 271 10783 9438 9637 17 260 395 C ATOM 4233 C SER B 271 117.379 10.660 0.262 1.00 73.82 C ANISOU 4233 C SER B 271 10167 8825 9057 9 278 397 C ATOM 4234 O SER B 271 118.391 11.048 -0.322 1.00 80.79 O ANISOU 4234 O SER B 271 11063 9695 9938 -2 302 398 O ATOM 4235 CB SER B 271 115.553 10.261 -1.389 1.00 77.41 C ANISOU 4235 CB SER B 271 10658 9274 9481 13 245 412 C ATOM 4236 OG SER B 271 114.758 11.263 -0.778 1.00 78.52 O ANISOU 4236 OG SER B 271 10785 9408 9642 16 227 421 O ATOM 4237 N SER B 272 117.001 11.136 1.446 1.00 67.04 N ANISOU 4237 N SER B 272 9283 7971 8220 15 266 395 N ATOM 4238 CA SER B 272 117.684 12.270 2.073 1.00 64.58 C ANISOU 4238 CA SER B 272 8958 7647 7932 7 279 397 C ATOM 4239 C SER B 272 119.123 11.955 2.489 1.00 48.68 C ANISOU 4239 C SER B 272 6935 5639 5923 2 307 385 C ATOM 4240 O SER B 272 119.411 10.855 2.963 1.00 44.13 O ANISOU 4240 O SER B 272 6347 5080 5340 9 309 373 O ATOM 4241 CB SER B 272 116.885 12.762 3.284 1.00 66.13 C ANISOU 4241 CB SER B 272 9128 7846 8150 14 259 397 C ATOM 4242 OG SER B 272 116.638 11.717 4.211 1.00 59.65 O ANISOU 4242 OG SER B 272 8288 7049 7328 25 248 384 O ATOM 4243 N PRO B 273 120.033 12.925 2.300 1.00 47.91 N ANISOU 4243 N PRO B 273 6841 5523 5837 -11 330 389 N ATOM 4244 CA PRO B 273 121.446 12.799 2.681 1.00 57.51 C ANISOU 4244 CA PRO B 273 8048 6742 7061 -17 359 378 C ATOM 4245 C PRO B 273 121.668 12.534 4.176 1.00 56.10 C ANISOU 4245 C PRO B 273 7842 6575 6897 -11 359 366 C ATOM 4246 O PRO B 273 122.620 11.830 4.530 1.00 51.97 O ANISOU 4246 O PRO B 273 7317 6060 6370 -9 381 353 O ATOM 4247 CB PRO B 273 122.034 14.169 2.291 1.00 47.86 C ANISOU 4247 CB PRO B 273 6837 5495 5853 -31 378 385 C ATOM 4248 CG PRO B 273 121.107 14.708 1.264 1.00 48.48 C ANISOU 4248 CG PRO B 273 6939 5560 5922 -32 364 401 C ATOM 4249 CD PRO B 273 119.747 14.213 1.639 1.00 41.23 C ANISOU 4249 CD PRO B 273 6012 4654 4999 -19 330 404 C ATOM 4250 N THR B 274 120.819 13.094 5.033 1.00 48.81 N ANISOU 4250 N THR B 274 6904 5652 5989 -5 339 368 N ATOM 4251 CA THR B 274 120.936 12.873 6.473 1.00 56.00 C ANISOU 4251 CA THR B 274 7796 6571 6911 2 341 356 C ATOM 4252 C THR B 274 120.701 11.403 6.801 1.00 47.84 C ANISOU 4252 C THR B 274 6749 5565 5864 14 327 348 C ATOM 4253 O THR B 274 121.411 10.799 7.617 1.00 40.62 O ANISOU 4253 O THR B 274 5825 4659 4949 18 342 336 O ATOM 4254 CB THR B 274 119.930 13.742 7.270 1.00 53.02 C ANISOU 4254 CB THR B 274 7406 6187 6553 5 320 360 C ATOM 4255 OG1 THR B 274 120.118 15.124 6.943 1.00 69.02 O ANISOU 4255 OG1 THR B 274 9443 8186 8594 -5 334 368 O ATOM 4256 CG2 THR B 274 120.121 13.553 8.770 1.00 54.00 C ANISOU 4256 CG2 THR B 274 7512 6318 6688 12 325 347 C ATOM 4257 N PHE B 275 119.711 10.829 6.125 1.00 53.66 N ANISOU 4257 N PHE B 275 7487 6313 6587 18 300 354 N ATOM 4258 CA PHE B 275 119.372 9.423 6.274 1.00 55.10 C ANISOU 4258 CA PHE B 275 7665 6517 6753 30 289 346 C ATOM 4259 C PHE B 275 120.531 8.548 5.812 1.00 53.11 C ANISOU 4259 C PHE B 275 7420 6271 6490 27 313 339 C ATOM 4260 O PHE B 275 120.829 7.511 6.416 1.00 49.57 O ANISOU 4260 O PHE B 275 6956 5841 6038 35 314 329 O ATOM 4261 CB PHE B 275 118.105 9.118 5.468 1.00 48.42 C ANISOU 4261 CB PHE B 275 6836 5670 5890 37 268 351 C ATOM 4262 CG PHE B 275 117.619 7.703 5.589 1.00 56.75 C ANISOU 4262 CG PHE B 275 7887 6745 6929 50 256 341 C ATOM 4263 CD1 PHE B 275 118.085 6.720 4.732 1.00 59.66 C ANISOU 4263 CD1 PHE B 275 8271 7118 7279 50 268 337 C ATOM 4264 CD2 PHE B 275 116.671 7.363 6.540 1.00 58.89 C ANISOU 4264 CD2 PHE B 275 8140 7029 7206 61 233 336 C ATOM 4265 CE1 PHE B 275 117.632 5.420 4.835 1.00 61.45 C ANISOU 4265 CE1 PHE B 275 8493 7361 7493 61 257 328 C ATOM 4266 CE2 PHE B 275 116.213 6.066 6.646 1.00 58.18 C ANISOU 4266 CE2 PHE B 275 8047 6957 7103 72 223 326 C ATOM 4267 CZ PHE B 275 116.694 5.093 5.793 1.00 56.59 C ANISOU 4267 CZ PHE B 275 7859 6759 6882 72 235 322 C ATOM 4268 N LEU B 276 121.196 8.993 4.751 1.00 50.59 N ANISOU 4268 N LEU B 276 7122 5936 6165 16 333 344 N ATOM 4269 CA LEU B 276 122.333 8.273 4.197 1.00 44.37 C ANISOU 4269 CA LEU B 276 6341 5149 5367 11 358 338 C ATOM 4270 C LEU B 276 123.494 8.288 5.177 1.00 44.43 C ANISOU 4270 C LEU B 276 6335 5157 5388 10 384 328 C ATOM 4271 O LEU B 276 124.182 7.279 5.365 1.00 50.58 O ANISOU 4271 O LEU B 276 7108 5947 6162 14 396 319 O ATOM 4272 CB LEU B 276 122.751 8.894 2.862 1.00 55.11 C ANISOU 4272 CB LEU B 276 7731 6488 6719 -1 376 346 C ATOM 4273 CG LEU B 276 124.049 8.424 2.204 1.00 41.63 C ANISOU 4273 CG LEU B 276 6034 4777 5006 -9 407 339 C ATOM 4274 CD1 LEU B 276 123.920 6.991 1.719 1.00 34.49 C ANISOU 4274 CD1 LEU B 276 5137 3885 4081 -2 404 333 C ATOM 4275 CD2 LEU B 276 124.434 9.351 1.060 1.00 38.81 C ANISOU 4275 CD2 LEU B 276 5705 4397 4646 -23 425 347 C ATOM 4276 N LEU B 277 123.682 9.433 5.827 1.00 37.86 N ANISOU 4276 N LEU B 277 5502 4309 4572 6 395 329 N ATOM 4277 CA LEU B 277 124.765 9.591 6.789 1.00 43.63 C ANISOU 4277 CA LEU B 277 6226 5035 5316 5 425 318 C ATOM 4278 C LEU B 277 124.542 8.708 8.006 1.00 41.85 C ANISOU 4278 C LEU B 277 5978 4831 5092 18 413 311 C ATOM 4279 O LEU B 277 125.449 7.984 8.441 1.00 46.60 O ANISOU 4279 O LEU B 277 6572 5440 5694 20 433 303 O ATOM 4280 CB LEU B 277 124.890 11.056 7.216 1.00 34.06 C ANISOU 4280 CB LEU B 277 5017 3800 4123 -3 439 320 C ATOM 4281 CG LEU B 277 125.898 11.417 8.312 1.00 40.91 C ANISOU 4281 CG LEU B 277 5874 4660 5009 -6 471 309 C ATOM 4282 CD1 LEU B 277 127.304 10.968 7.942 1.00 31.39 C ANISOU 4282 CD1 LEU B 277 4674 3451 3803 -13 508 301 C ATOM 4283 CD2 LEU B 277 125.865 12.916 8.577 1.00 43.24 C ANISOU 4283 CD2 LEU B 277 6173 4932 5326 -16 482 311 C ATOM 4284 N LEU B 278 123.328 8.760 8.547 1.00 38.78 N ANISOU 4284 N LEU B 278 5578 4451 4705 26 380 314 N ATOM 4285 CA LEU B 278 123.013 7.965 9.724 1.00 51.49 C ANISOU 4285 CA LEU B 278 7167 6081 6315 39 366 307 C ATOM 4286 C LEU B 278 123.076 6.471 9.422 1.00 45.01 C ANISOU 4286 C LEU B 278 6340 5283 5480 47 359 303 C ATOM 4287 O LEU B 278 123.550 5.683 10.250 1.00 42.37 O ANISOU 4287 O LEU B 278 5991 4962 5145 54 365 295 O ATOM 4288 CB LEU B 278 121.632 8.340 10.262 1.00 53.44 C ANISOU 4288 CB LEU B 278 7404 6334 6569 46 333 311 C ATOM 4289 CG LEU B 278 121.486 9.789 10.731 1.00 40.45 C ANISOU 4289 CG LEU B 278 5762 4666 4942 39 338 314 C ATOM 4290 CD1 LEU B 278 120.118 10.014 11.348 1.00 34.94 C ANISOU 4290 CD1 LEU B 278 5050 3974 4250 46 304 316 C ATOM 4291 CD2 LEU B 278 122.590 10.155 11.713 1.00 32.16 C ANISOU 4291 CD2 LEU B 278 4706 3607 3905 36 371 306 C ATOM 4292 N LYS B 279 122.628 6.080 8.231 1.00 49.94 N ANISOU 4292 N LYS B 279 6973 5910 6091 44 346 308 N ATOM 4293 CA LYS B 279 122.719 4.677 7.844 1.00 51.46 C ANISOU 4293 CA LYS B 279 7160 6121 6271 50 341 303 C ATOM 4294 C LYS B 279 124.174 4.260 7.670 1.00 46.02 C ANISOU 4294 C LYS B 279 6476 5427 5581 45 376 298 C ATOM 4295 O LYS B 279 124.531 3.106 7.914 1.00 50.12 O ANISOU 4295 O LYS B 279 6984 5962 6097 52 378 291 O ATOM 4296 CB LYS B 279 121.937 4.395 6.560 1.00 43.53 C ANISOU 4296 CB LYS B 279 6177 5113 5250 50 329 307 C ATOM 4297 CG LYS B 279 121.889 2.911 6.218 1.00 61.83 C ANISOU 4297 CG LYS B 279 8497 7443 7552 59 329 300 C ATOM 4298 CD LYS B 279 121.074 2.612 4.973 1.00 78.66 C ANISOU 4298 CD LYS B 279 10656 9567 9664 60 320 302 C ATOM 4299 CE LYS B 279 121.011 1.109 4.722 1.00 81.62 C ANISOU 4299 CE LYS B 279 11031 9954 10027 69 320 293 C ATOM 4300 NZ LYS B 279 120.185 0.765 3.532 1.00 72.59 N ANISOU 4300 NZ LYS B 279 9913 8803 8864 69 312 295 N ATOM 4301 N LYS B 280 125.019 5.198 7.258 1.00 45.79 N ANISOU 4301 N LYS B 280 6463 5376 5558 33 404 300 N ATOM 4302 CA LYS B 280 126.444 4.906 7.169 1.00 51.50 C ANISOU 4302 CA LYS B 280 7189 6093 6285 28 440 293 C ATOM 4303 C LYS B 280 127.089 4.872 8.558 1.00 50.23 C ANISOU 4303 C LYS B 280 7011 5936 6138 33 456 287 C ATOM 4304 O LYS B 280 128.193 4.351 8.716 1.00 64.19 O ANISOU 4304 O LYS B 280 8773 7705 7910 32 483 281 O ATOM 4305 CB LYS B 280 127.154 5.919 6.262 1.00 55.24 C ANISOU 4305 CB LYS B 280 7686 6541 6762 12 467 296 C ATOM 4306 CG LYS B 280 126.942 5.648 4.773 1.00 64.64 C ANISOU 4306 CG LYS B 280 8895 7728 7937 6 462 301 C ATOM 4307 CD LYS B 280 127.873 6.468 3.889 1.00 67.83 C ANISOU 4307 CD LYS B 280 9321 8107 8343 -9 494 301 C ATOM 4308 CE LYS B 280 127.415 7.912 3.767 1.00 75.18 C ANISOU 4308 CE LYS B 280 10263 9020 9281 -16 490 310 C ATOM 4309 NZ LYS B 280 128.266 8.670 2.806 1.00 65.07 N ANISOU 4309 NZ LYS B 280 9006 7717 8002 -31 521 310 N ATOM 4310 N LEU B 281 126.406 5.426 9.559 1.00 42.08 N ANISOU 4310 N LEU B 281 5968 4907 5114 39 440 288 N ATOM 4311 CA LEU B 281 126.907 5.379 10.937 1.00 52.16 C ANISOU 4311 CA LEU B 281 7227 6189 6403 44 453 283 C ATOM 4312 C LEU B 281 126.246 4.299 11.810 1.00 46.75 C ANISOU 4312 C LEU B 281 6522 5530 5711 60 426 281 C ATOM 4313 O LEU B 281 126.582 4.153 12.998 1.00 47.80 O ANISOU 4313 O LEU B 281 6639 5672 5852 66 433 277 O ATOM 4314 CB LEU B 281 126.738 6.748 11.597 1.00 40.93 C ANISOU 4314 CB LEU B 281 5806 4750 4996 38 459 284 C ATOM 4315 CG LEU B 281 127.652 7.852 11.060 1.00 41.92 C ANISOU 4315 CG LEU B 281 5946 4849 5134 21 494 283 C ATOM 4316 CD1 LEU B 281 127.232 9.208 11.600 1.00 26.80 C ANISOU 4316 CD1 LEU B 281 4032 2917 3236 15 494 285 C ATOM 4317 CD2 LEU B 281 129.107 7.560 11.405 1.00 39.15 C ANISOU 4317 CD2 LEU B 281 5585 4495 4794 15 533 275 C ATOM 4318 N ASP B 282 125.326 3.538 11.220 1.00 42.18 N ANISOU 4318 N ASP B 282 5519 5555 4952 -478 276 -448 N ATOM 4319 CA ASP B 282 124.547 2.545 11.968 1.00 47.85 C ANISOU 4319 CA ASP B 282 6205 6254 5723 -445 215 -362 C ATOM 4320 C ASP B 282 125.392 1.521 12.737 1.00 41.38 C ANISOU 4320 C ASP B 282 5348 5411 4964 -404 188 -420 C ATOM 4321 O ASP B 282 125.165 1.297 13.933 1.00 48.62 O ANISOU 4321 O ASP B 282 6234 6327 5911 -347 169 -362 O ATOM 4322 CB ASP B 282 123.605 1.801 11.016 1.00 38.19 C ANISOU 4322 CB ASP B 282 4994 5009 4506 -494 166 -314 C ATOM 4323 CG ASP B 282 122.947 0.595 11.667 1.00 63.57 C ANISOU 4323 CG ASP B 282 8175 8199 7781 -464 100 -243 C ATOM 4324 OD1 ASP B 282 121.920 0.772 12.357 1.00 64.20 O ANISOU 4324 OD1 ASP B 282 8244 8287 7864 -436 83 -128 O ATOM 4325 OD2 ASP B 282 123.452 -0.533 11.483 1.00 62.69 O ANISOU 4325 OD2 ASP B 282 8048 8058 7714 -470 64 -303 O ATOM 4326 N SER B 283 126.367 0.914 12.065 1.00 36.84 N ANISOU 4326 N SER B 283 4775 4816 4405 -432 186 -535 N ATOM 4327 CA SER B 283 127.201 -0.101 12.705 1.00 39.24 C ANISOU 4327 CA SER B 283 5045 5096 4768 -397 158 -597 C ATOM 4328 C SER B 283 128.001 0.491 13.857 1.00 40.37 C ANISOU 4328 C SER B 283 5168 5256 4914 -338 194 -627 C ATOM 4329 O SER B 283 128.233 -0.169 14.872 1.00 43.31 O ANISOU 4329 O SER B 283 5507 5616 5335 -288 166 -620 O ATOM 4330 CB SER B 283 128.149 -0.745 11.691 1.00 42.04 C ANISOU 4330 CB SER B 283 5409 5429 5136 -441 156 -722 C ATOM 4331 OG SER B 283 127.436 -1.501 10.730 1.00 68.32 O ANISOU 4331 OG SER B 283 8749 8736 8472 -490 113 -695 O ATOM 4332 N LEU B 284 128.407 1.747 13.696 1.00 37.63 N ANISOU 4332 N LEU B 284 4844 4939 4515 -345 257 -659 N ATOM 4333 CA LEU B 284 129.144 2.448 14.736 1.00 36.45 C ANISOU 4333 CA LEU B 284 4679 4808 4361 -292 297 -687 C ATOM 4334 C LEU B 284 128.266 2.690 15.958 1.00 40.01 C ANISOU 4334 C LEU B 284 5110 5272 4820 -237 283 -565 C ATOM 4335 O LEU B 284 128.722 2.553 17.098 1.00 31.09 O ANISOU 4335 O LEU B 284 3951 4141 3719 -180 281 -570 O ATOM 4336 CB LEU B 284 129.682 3.779 14.204 1.00 33.19 C ANISOU 4336 CB LEU B 284 4298 4424 3887 -316 367 -742 C ATOM 4337 CG LEU B 284 130.568 4.586 15.153 1.00 27.74 C ANISOU 4337 CG LEU B 284 3596 3756 3189 -267 415 -786 C ATOM 4338 CD1 LEU B 284 131.847 3.823 15.439 1.00 40.90 C ANISOU 4338 CD1 LEU B 284 5238 5400 4902 -247 408 -899 C ATOM 4339 CD2 LEU B 284 130.873 5.957 14.571 1.00 38.01 C ANISOU 4339 CD2 LEU B 284 4930 5086 4425 -295 483 -822 C ATOM 4340 N CYS B 285 127.001 3.030 15.720 1.00 33.80 N ANISOU 4340 N CYS B 285 4338 4496 4007 -254 272 -456 N ATOM 4341 CA CYS B 285 126.077 3.255 16.829 1.00 32.34 C ANISOU 4341 CA CYS B 285 4135 4323 3829 -205 258 -335 C ATOM 4342 C CYS B 285 125.751 1.962 17.574 1.00 34.59 C ANISOU 4342 C CYS B 285 4385 4579 4178 -171 194 -291 C ATOM 4343 O CYS B 285 125.700 1.942 18.811 1.00 31.51 O ANISOU 4343 O CYS B 285 3968 4193 3810 -112 187 -246 O ATOM 4344 CB CYS B 285 124.788 3.910 16.331 1.00 30.24 C ANISOU 4344 CB CYS B 285 3895 4075 3522 -235 261 -231 C ATOM 4345 SG CYS B 285 124.952 5.667 15.941 1.00 41.75 S ANISOU 4345 SG CYS B 285 5389 5574 4902 -254 339 -245 S ATOM 4346 N VAL B 286 125.544 0.881 16.827 1.00 35.92 N ANISOU 4346 N VAL B 286 4554 4719 4376 -207 148 -304 N ATOM 4347 CA VAL B 286 125.296 -0.411 17.454 1.00 39.13 C ANISOU 4347 CA VAL B 286 4927 5096 4846 -178 86 -271 C ATOM 4348 C VAL B 286 126.522 -0.827 18.260 1.00 40.05 C ANISOU 4348 C VAL B 286 5017 5202 5000 -134 88 -357 C ATOM 4349 O VAL B 286 126.414 -1.371 19.367 1.00 30.26 O ANISOU 4349 O VAL B 286 3745 3951 3801 -81 58 -315 O ATOM 4350 CB VAL B 286 124.958 -1.489 16.404 1.00 23.33 C ANISOU 4350 CB VAL B 286 2932 3064 2868 -229 37 -283 C ATOM 4351 CG1 VAL B 286 124.791 -2.849 17.055 1.00 29.97 C ANISOU 4351 CG1 VAL B 286 3737 3873 3775 -198 -26 -256 C ATOM 4352 CG2 VAL B 286 123.704 -1.103 15.643 1.00 39.77 C ANISOU 4352 CG2 VAL B 286 5040 5155 4914 -271 32 -193 C ATOM 4353 N SER B 287 127.691 -0.511 17.712 1.00 44.73 N ANISOU 4353 N SER B 287 5621 5797 5577 -154 127 -479 N ATOM 4354 CA SER B 287 128.954 -0.833 18.355 1.00 31.46 C ANISOU 4354 CA SER B 287 3918 4106 3929 -117 134 -574 C ATOM 4355 C SER B 287 129.120 -0.069 19.663 1.00 33.92 C ANISOU 4355 C SER B 287 4214 4441 4233 -54 163 -541 C ATOM 4356 O SER B 287 129.620 -0.609 20.649 1.00 26.64 O ANISOU 4356 O SER B 287 3262 3506 3354 -4 144 -557 O ATOM 4357 CB SER B 287 130.111 -0.518 17.407 1.00 30.94 C ANISOU 4357 CB SER B 287 3873 4042 3842 -157 175 -709 C ATOM 4358 OG SER B 287 131.294 -1.180 17.804 1.00 63.50 O ANISOU 4358 OG SER B 287 7972 8146 8009 -132 167 -809 O ATOM 4359 N PHE B 288 128.683 1.186 19.668 1.00 28.52 N ANISOU 4359 N PHE B 288 3551 3791 3496 -56 208 -492 N ATOM 4360 CA PHE B 288 128.740 2.002 20.871 1.00 28.30 C ANISOU 4360 CA PHE B 288 3511 3786 3455 2 238 -452 C ATOM 4361 C PHE B 288 127.758 1.476 21.914 1.00 42.09 C ANISOU 4361 C PHE B 288 5232 5526 5234 46 193 -332 C ATOM 4362 O PHE B 288 128.034 1.501 23.116 1.00 27.07 O ANISOU 4362 O PHE B 288 3306 3627 3352 105 193 -317 O ATOM 4363 CB PHE B 288 128.440 3.464 20.533 1.00 25.89 C ANISOU 4363 CB PHE B 288 3235 3517 3083 -16 296 -425 C ATOM 4364 CG PHE B 288 128.967 4.444 21.543 1.00 27.15 C ANISOU 4364 CG PHE B 288 3387 3704 3224 35 343 -433 C ATOM 4365 CD1 PHE B 288 130.328 4.675 21.658 1.00 29.89 C ANISOU 4365 CD1 PHE B 288 3730 4052 3573 47 377 -551 C ATOM 4366 CD2 PHE B 288 128.101 5.146 22.365 1.00 24.26 C ANISOU 4366 CD2 PHE B 288 3017 3360 2838 69 352 -323 C ATOM 4367 CE1 PHE B 288 130.817 5.579 22.583 1.00 31.89 C ANISOU 4367 CE1 PHE B 288 3976 4329 3810 94 420 -559 C ATOM 4368 CE2 PHE B 288 128.584 6.053 23.290 1.00 23.84 C ANISOU 4368 CE2 PHE B 288 2957 3332 2768 116 395 -331 C ATOM 4369 CZ PHE B 288 129.943 6.269 23.399 1.00 34.69 C ANISOU 4369 CZ PHE B 288 4328 4707 4144 129 428 -449 C ATOM 4370 N ALA B 289 126.614 0.987 21.442 1.00 33.37 N ANISOU 4370 N ALA B 289 4134 4411 4135 18 153 -248 N ATOM 4371 CA ALA B 289 125.617 0.401 22.331 1.00 27.14 C ANISOU 4371 CA ALA B 289 3321 3613 3379 55 107 -133 C ATOM 4372 C ALA B 289 126.120 -0.891 22.967 1.00 34.40 C ANISOU 4372 C ALA B 289 4208 4500 4364 88 58 -166 C ATOM 4373 O ALA B 289 125.757 -1.216 24.097 1.00 27.71 O ANISOU 4373 O ALA B 289 3336 3648 3545 139 33 -98 O ATOM 4374 CB ALA B 289 124.323 0.147 21.581 1.00 30.64 C ANISOU 4374 CB ALA B 289 3779 4051 3814 12 75 -43 C ATOM 4375 N TYR B 290 126.982 -1.613 22.255 1.00 33.24 N ANISOU 4375 N TYR B 290 4061 4329 4240 59 45 -272 N ATOM 4376 CA TYR B 290 127.443 -2.910 22.745 1.00 31.43 C ANISOU 4376 CA TYR B 290 3801 4066 4074 84 -5 -306 C ATOM 4377 C TYR B 290 128.419 -2.771 23.903 1.00 30.33 C ANISOU 4377 C TYR B 290 3640 3930 3954 144 12 -354 C ATOM 4378 O TYR B 290 128.716 -3.748 24.590 1.00 22.37 O ANISOU 4378 O TYR B 290 2604 2897 2998 179 -29 -364 O ATOM 4379 CB TYR B 290 128.077 -3.728 21.624 1.00 23.92 C ANISOU 4379 CB TYR B 290 2857 3089 3143 35 -24 -406 C ATOM 4380 CG TYR B 290 127.294 -4.975 21.293 1.00 24.67 C ANISOU 4380 CG TYR B 290 2942 3153 3279 15 -90 -355 C ATOM 4381 CD1 TYR B 290 127.345 -6.092 22.117 1.00 32.59 C ANISOU 4381 CD1 TYR B 290 3912 4129 4341 54 -142 -339 C ATOM 4382 CD2 TYR B 290 126.499 -5.032 20.159 1.00 30.02 C ANISOU 4382 CD2 TYR B 290 3642 3829 3935 -43 -101 -321 C ATOM 4383 CE1 TYR B 290 126.624 -7.233 21.816 1.00 31.33 C ANISOU 4383 CE1 TYR B 290 3744 3941 4221 36 -202 -292 C ATOM 4384 CE2 TYR B 290 125.777 -6.164 19.850 1.00 26.03 C ANISOU 4384 CE2 TYR B 290 3128 3296 3468 -61 -161 -275 C ATOM 4385 CZ TYR B 290 125.843 -7.262 20.678 1.00 35.38 C ANISOU 4385 CZ TYR B 290 4280 4453 4712 -21 -211 -260 C ATOM 4386 OH TYR B 290 125.120 -8.388 20.360 1.00 27.42 O ANISOU 4386 OH TYR B 290 3261 3416 3741 -40 -272 -213 O ATOM 4387 N ILE B 291 128.907 -1.552 24.117 1.00 28.41 N ANISOU 4387 N ILE B 291 3409 3717 3667 157 72 -383 N ATOM 4388 CA ILE B 291 129.835 -1.270 25.205 1.00 33.61 C ANISOU 4388 CA ILE B 291 4049 4383 4339 214 93 -429 C ATOM 4389 C ILE B 291 129.154 -1.542 26.548 1.00 35.16 C ANISOU 4389 C ILE B 291 4220 4577 4561 274 63 -325 C ATOM 4390 O ILE B 291 129.817 -1.816 27.541 1.00 34.70 O ANISOU 4390 O ILE B 291 4139 4512 4533 325 56 -353 O ATOM 4391 CB ILE B 291 130.357 0.187 25.138 1.00 39.37 C ANISOU 4391 CB ILE B 291 4798 5147 5011 214 165 -470 C ATOM 4392 CG1 ILE B 291 131.035 0.447 23.790 1.00 25.56 C ANISOU 4392 CG1 ILE B 291 3076 3400 3237 154 196 -574 C ATOM 4393 CG2 ILE B 291 131.333 0.479 26.272 1.00 31.01 C ANISOU 4393 CG2 ILE B 291 3720 4095 3966 274 188 -519 C ATOM 4394 CD1 ILE B 291 131.559 1.861 23.622 1.00 31.57 C ANISOU 4394 CD1 ILE B 291 3859 4195 3942 149 267 -618 C ATOM 4395 N ASN B 292 127.825 -1.501 26.565 1.00 33.67 N ANISOU 4395 N ASN B 292 4037 4395 4362 267 43 -204 N ATOM 4396 CA ASN B 292 127.060 -1.866 27.754 1.00 36.16 C ANISOU 4396 CA ASN B 292 4329 4707 4704 318 10 -97 C ATOM 4397 C ASN B 292 127.333 -3.295 28.205 1.00 31.03 C ANISOU 4397 C ASN B 292 3651 4019 4120 340 -50 -115 C ATOM 4398 O ASN B 292 127.214 -3.617 29.387 1.00 47.38 O ANISOU 4398 O ASN B 292 5699 6084 6220 395 -71 -67 O ATOM 4399 CB ASN B 292 125.561 -1.712 27.502 1.00 40.31 C ANISOU 4399 CB ASN B 292 4865 5240 5210 297 -6 30 C ATOM 4400 CG ASN B 292 125.085 -0.290 27.653 1.00 37.66 C ANISOU 4400 CG ASN B 292 4548 4943 4817 302 47 86 C ATOM 4401 OD1 ASN B 292 125.002 0.456 26.679 1.00 49.47 O ANISOU 4401 OD1 ASN B 292 6071 6456 6268 256 81 66 O ATOM 4402 ND2 ASN B 292 124.757 0.092 28.878 1.00 42.46 N ANISOU 4402 ND2 ASN B 292 5141 5565 5425 357 54 158 N ATOM 4403 N CYS B 293 127.685 -4.148 27.250 1.00 31.27 N ANISOU 4403 N CYS B 293 3684 4024 4174 298 -77 -184 N ATOM 4404 CA CYS B 293 127.885 -5.568 27.511 1.00 28.93 C ANISOU 4404 CA CYS B 293 3363 3690 3941 311 -137 -202 C ATOM 4405 C CYS B 293 129.274 -5.888 28.065 1.00 40.54 C ANISOU 4405 C CYS B 293 4814 5146 5442 345 -133 -311 C ATOM 4406 O CYS B 293 129.556 -7.041 28.393 1.00 54.50 O ANISOU 4406 O CYS B 293 6561 6884 7265 362 -182 -333 O ATOM 4407 CB CYS B 293 127.641 -6.376 26.235 1.00 41.19 C ANISOU 4407 CB CYS B 293 4925 5219 5507 249 -170 -228 C ATOM 4408 SG CYS B 293 125.984 -6.178 25.546 1.00 48.16 S ANISOU 4408 SG CYS B 293 5827 6111 6361 207 -184 -101 S ATOM 4409 N CYS B 294 130.146 -4.886 28.149 1.00 31.21 N ANISOU 4409 N CYS B 294 3643 3988 4228 355 -77 -382 N ATOM 4410 CA CYS B 294 131.476 -5.101 28.715 1.00 38.82 C ANISOU 4410 CA CYS B 294 4589 4941 5219 390 -70 -485 C ATOM 4411 C CYS B 294 131.889 -4.014 29.708 1.00 42.06 C ANISOU 4411 C CYS B 294 4998 5381 5603 440 -22 -483 C ATOM 4412 O CYS B 294 132.947 -4.110 30.330 1.00 46.88 O ANISOU 4412 O CYS B 294 5593 5984 6235 476 -15 -559 O ATOM 4413 CB CYS B 294 132.524 -5.198 27.599 1.00 37.16 C ANISOU 4413 CB CYS B 294 4390 4721 5006 344 -51 -619 C ATOM 4414 SG CYS B 294 133.075 -3.611 26.928 1.00 40.00 S ANISOU 4414 SG CYS B 294 4782 5120 5296 315 32 -683 S ATOM 4415 N ILE B 295 131.074 -2.972 29.836 1.00 34.62 N ANISOU 4415 N ILE B 295 4072 4470 4613 441 11 -398 N ATOM 4416 CA ILE B 295 131.405 -1.848 30.709 1.00 44.33 C ANISOU 4416 CA ILE B 295 5302 5730 5812 485 60 -392 C ATOM 4417 C ILE B 295 131.283 -2.194 32.195 1.00 40.48 C ANISOU 4417 C ILE B 295 4788 5237 5357 554 33 -333 C ATOM 4418 O ILE B 295 132.024 -1.661 33.024 1.00 36.24 O ANISOU 4418 O ILE B 295 4243 4711 4816 598 62 -370 O ATOM 4419 CB ILE B 295 130.521 -0.609 30.387 1.00 32.75 C ANISOU 4419 CB ILE B 295 3860 4299 4284 464 103 -315 C ATOM 4420 CG1 ILE B 295 131.030 0.630 31.127 1.00 36.89 C ANISOU 4420 CG1 ILE B 295 4387 4855 4772 503 160 -329 C ATOM 4421 CG2 ILE B 295 129.053 -0.875 30.693 1.00 33.31 C ANISOU 4421 CG2 ILE B 295 3928 4371 4358 469 68 -173 C ATOM 4422 CD1 ILE B 295 132.404 1.078 30.686 1.00 27.57 C ANISOU 4422 CD1 ILE B 295 3216 3680 3581 491 202 -466 C ATOM 4423 N ASN B 296 130.356 -3.090 32.525 1.00 38.69 N ANISOU 4423 N ASN B 296 4548 4991 5163 562 -21 -243 N ATOM 4424 CA ASN B 296 130.133 -3.474 33.916 1.00 34.41 C ANISOU 4424 CA ASN B 296 3982 4441 4652 626 -49 -178 C ATOM 4425 C ASN B 296 131.368 -4.068 34.614 1.00 32.75 C ANISOU 4425 C ASN B 296 3750 4209 4484 667 -63 -270 C ATOM 4426 O ASN B 296 131.695 -3.641 35.720 1.00 25.74 O ANISOU 4426 O ASN B 296 2852 3333 3596 721 -47 -260 O ATOM 4427 CB ASN B 296 128.956 -4.448 34.022 1.00 26.53 C ANISOU 4427 CB ASN B 296 2973 3422 3685 622 -107 -73 C ATOM 4428 CG ASN B 296 127.617 -3.778 33.773 1.00 42.41 C ANISOU 4428 CG ASN B 296 5001 5457 5656 601 -94 43 C ATOM 4429 OD1 ASN B 296 127.530 -2.788 33.050 1.00 51.32 O ANISOU 4429 OD1 ASN B 296 6152 6611 6735 568 -48 32 O ATOM 4430 ND2 ASN B 296 126.565 -4.314 34.383 1.00 47.20 N ANISOU 4430 ND2 ASN B 296 5595 6054 6285 622 -134 156 N ATOM 4431 N PRO B 297 132.059 -5.047 33.985 1.00 36.42 N ANISOU 4431 N PRO B 297 4207 4643 4987 642 -94 -359 N ATOM 4432 CA PRO B 297 133.272 -5.542 34.654 1.00 35.06 C ANISOU 4432 CA PRO B 297 4015 4452 4855 681 -105 -450 C ATOM 4433 C PRO B 297 134.312 -4.448 34.889 1.00 33.11 C ANISOU 4433 C PRO B 297 3775 4229 4577 700 -45 -532 C ATOM 4434 O PRO B 297 135.009 -4.463 35.909 1.00 36.75 O ANISOU 4434 O PRO B 297 4220 4687 5058 753 -45 -561 O ATOM 4435 CB PRO B 297 133.806 -6.593 33.675 1.00 36.07 C ANISOU 4435 CB PRO B 297 4140 4547 5019 638 -138 -539 C ATOM 4436 CG PRO B 297 132.610 -7.043 32.924 1.00 34.20 C ANISOU 4436 CG PRO B 297 3912 4304 4780 595 -168 -457 C ATOM 4437 CD PRO B 297 131.776 -5.812 32.755 1.00 39.47 C ANISOU 4437 CD PRO B 297 4601 5008 5386 582 -123 -380 C ATOM 4438 N ILE B 298 134.396 -3.497 33.963 1.00 28.28 N ANISOU 4438 N ILE B 298 3187 3642 3916 658 6 -565 N ATOM 4439 CA ILE B 298 135.328 -2.389 34.105 1.00 34.28 C ANISOU 4439 CA ILE B 298 3956 4427 4643 672 66 -640 C ATOM 4440 C ILE B 298 134.957 -1.536 35.310 1.00 35.31 C ANISOU 4440 C ILE B 298 4082 4583 4750 727 90 -561 C ATOM 4441 O ILE B 298 135.817 -1.157 36.105 1.00 39.15 O ANISOU 4441 O ILE B 298 4572 5071 5233 749 111 -591 O ATOM 4442 CB ILE B 298 135.346 -1.505 32.844 1.00 42.93 C ANISOU 4442 CB ILE B 298 5080 5544 5687 612 115 -679 C ATOM 4443 CG1 ILE B 298 135.758 -2.323 31.619 1.00 37.08 C ANISOU 4443 CG1 ILE B 298 4344 4777 4967 556 94 -763 C ATOM 4444 CG2 ILE B 298 136.280 -0.321 33.030 1.00 44.60 C ANISOU 4444 CG2 ILE B 298 5300 5782 5863 628 179 -752 C ATOM 4445 CD1 ILE B 298 135.778 -1.522 30.340 1.00 29.08 C ANISOU 4445 CD1 ILE B 298 3361 3784 3904 496 140 -803 C ATOM 4446 N ILE B 299 133.664 -1.262 35.450 1.00 41.06 N ANISOU 4446 N ILE B 299 4818 5327 5456 724 85 -436 N ATOM 4447 CA ILE B 299 133.168 -0.464 36.561 1.00 33.21 C ANISOU 4447 CA ILE B 299 3821 4358 4438 774 106 -349 C ATOM 4448 C ILE B 299 133.394 -1.173 37.891 1.00 39.95 C ANISOU 4448 C ILE B 299 4648 5193 5337 837 68 -329 C ATOM 4449 O ILE B 299 133.776 -0.546 38.881 1.00 34.95 O ANISOU 4449 O ILE B 299 4026 4562 4690 842 95 -308 O ATOM 4450 CB ILE B 299 131.665 -0.154 36.397 1.00 28.14 C ANISOU 4450 CB ILE B 299 3191 3733 3768 755 102 -216 C ATOM 4451 CG1 ILE B 299 131.430 0.702 35.150 1.00 31.46 C ANISOU 4451 CG1 ILE B 299 3640 4175 4138 695 144 -232 C ATOM 4452 CG2 ILE B 299 131.119 0.546 37.631 1.00 24.42 C ANISOU 4452 CG2 ILE B 299 2715 3285 3279 810 118 -122 C ATOM 4453 CD1 ILE B 299 129.971 0.989 34.870 1.00 26.46 C ANISOU 4453 CD1 ILE B 299 3019 3556 3477 672 139 -107 C ATOM 4454 N TYR B 300 133.203 -2.489 37.897 1.00 34.95 N ANISOU 4454 N TYR B 300 4000 4525 4755 835 7 -318 N ATOM 4455 CA TYR B 300 133.366 -3.265 39.119 1.00 38.74 C ANISOU 4455 CA TYR B 300 4463 4980 5276 874 -30 -287 C ATOM 4456 C TYR B 300 134.824 -3.257 39.548 1.00 35.05 C ANISOU 4456 C TYR B 300 4011 4497 4811 852 -9 -373 C ATOM 4457 O TYR B 300 135.142 -3.029 40.719 1.00 41.85 O ANISOU 4457 O TYR B 300 4881 5352 5666 855 4 -335 O ATOM 4458 CB TYR B 300 132.891 -4.710 38.928 1.00 38.85 C ANISOU 4458 CB TYR B 300 4455 4960 5345 879 -102 -266 C ATOM 4459 CG TYR B 300 131.446 -4.868 38.506 1.00 27.69 C ANISOU 4459 CG TYR B 300 3050 3551 3921 848 -122 -149 C ATOM 4460 CD1 TYR B 300 130.512 -3.865 38.740 1.00 25.08 C ANISOU 4460 CD1 TYR B 300 2732 3253 3544 853 -90 -52 C ATOM 4461 CD2 TYR B 300 131.016 -6.028 37.871 1.00 34.59 C ANISOU 4461 CD2 TYR B 300 3918 4394 4830 815 -175 -138 C ATOM 4462 CE1 TYR B 300 129.192 -4.015 38.349 1.00 24.20 C ANISOU 4462 CE1 TYR B 300 2628 3143 3424 825 -109 54 C ATOM 4463 CE2 TYR B 300 129.701 -6.187 37.479 1.00 33.64 C ANISOU 4463 CE2 TYR B 300 3805 4276 4701 786 -194 -32 C ATOM 4464 CZ TYR B 300 128.794 -5.178 37.721 1.00 27.55 C ANISOU 4464 CZ TYR B 300 3046 3536 3884 792 -161 63 C ATOM 4465 OH TYR B 300 127.484 -5.333 37.330 1.00 34.90 O ANISOU 4465 OH TYR B 300 3983 4468 4807 764 -181 167 O ATOM 4466 N VAL B 301 135.712 -3.484 38.585 1.00 42.63 N ANISOU 4466 N VAL B 301 4973 5448 5775 822 -6 -486 N ATOM 4467 CA VAL B 301 137.133 -3.534 38.889 1.00 43.89 C ANISOU 4467 CA VAL B 301 5150 5594 5931 795 7 -559 C ATOM 4468 C VAL B 301 137.649 -2.176 39.346 1.00 51.01 C ANISOU 4468 C VAL B 301 6081 6518 6783 778 67 -547 C ATOM 4469 O VAL B 301 138.384 -2.087 40.332 1.00 43.10 O ANISOU 4469 O VAL B 301 5090 5507 5779 777 72 -539 O ATOM 4470 CB VAL B 301 137.946 -4.011 37.676 1.00 40.26 C ANISOU 4470 CB VAL B 301 4691 5121 5485 754 -1 -673 C ATOM 4471 CG1 VAL B 301 139.433 -3.821 37.920 1.00 42.73 C ANISOU 4471 CG1 VAL B 301 5025 5430 5781 719 16 -733 C ATOM 4472 CG2 VAL B 301 137.634 -5.464 37.385 1.00 33.87 C ANISOU 4472 CG2 VAL B 301 3853 4280 4736 766 -65 -691 C ATOM 4473 N VAL B 302 137.237 -1.116 38.654 1.00 38.88 N ANISOU 4473 N VAL B 302 4557 5009 5208 763 109 -542 N ATOM 4474 CA VAL B 302 137.656 0.227 39.035 1.00 31.03 C ANISOU 4474 CA VAL B 302 3590 4029 4169 742 163 -524 C ATOM 4475 C VAL B 302 137.138 0.581 40.428 1.00 49.78 C ANISOU 4475 C VAL B 302 5961 6405 6548 770 166 -433 C ATOM 4476 O VAL B 302 137.844 1.206 41.225 1.00 53.08 O ANISOU 4476 O VAL B 302 6396 6817 6957 755 189 -427 O ATOM 4477 CB VAL B 302 137.166 1.279 38.014 1.00 43.07 C ANISOU 4477 CB VAL B 302 5130 5583 5652 719 207 -527 C ATOM 4478 CG1 VAL B 302 137.332 2.690 38.564 1.00 27.98 C ANISOU 4478 CG1 VAL B 302 3244 3682 3704 701 256 -486 C ATOM 4479 CG2 VAL B 302 137.915 1.124 36.697 1.00 34.38 C ANISOU 4479 CG2 VAL B 302 4043 4478 4543 672 213 -621 C ATOM 4480 N ALA B 303 135.917 0.148 40.732 1.00 51.97 N ANISOU 4480 N ALA B 303 6216 6686 6844 805 137 -358 N ATOM 4481 CA ALA B 303 135.334 0.390 42.045 1.00 43.23 C ANISOU 4481 CA ALA B 303 5105 5576 5745 820 130 -270 C ATOM 4482 C ALA B 303 136.076 -0.370 43.136 1.00 48.87 C ANISOU 4482 C ALA B 303 5815 6260 6492 825 107 -275 C ATOM 4483 O ALA B 303 136.184 0.100 44.267 1.00 38.77 O ANISOU 4483 O ALA B 303 4541 4976 5214 820 116 -240 O ATOM 4484 CB ALA B 303 133.861 0.012 42.050 1.00 41.17 C ANISOU 4484 CB ALA B 303 4827 5325 5492 846 96 -180 C ATOM 4485 N GLY B 304 136.594 -1.545 42.791 1.00 47.14 N ANISOU 4485 N GLY B 304 5588 6023 6300 832 74 -324 N ATOM 4486 CA GLY B 304 137.290 -2.363 43.766 1.00 43.41 C ANISOU 4486 CA GLY B 304 5114 5526 5854 838 50 -329 C ATOM 4487 C GLY B 304 138.651 -1.801 44.121 1.00 51.45 C ANISOU 4487 C GLY B 304 6154 6543 6851 814 80 -385 C ATOM 4488 O GLY B 304 139.157 -2.013 45.223 1.00 53.59 O ANISOU 4488 O GLY B 304 6428 6802 7134 818 75 -369 O ATOM 4489 N GLN B 305 139.240 -1.064 43.185 1.00 56.48 N ANISOU 4489 N GLN B 305 6808 7194 7458 786 110 -445 N ATOM 4490 CA GLN B 305 140.553 -0.472 43.395 1.00 49.39 C ANISOU 4490 CA GLN B 305 5933 6294 6539 758 137 -489 C ATOM 4491 C GLN B 305 140.440 0.778 44.261 1.00 58.34 C ANISOU 4491 C GLN B 305 7080 7434 7654 750 177 -435 C ATOM 4492 O GLN B 305 141.008 0.843 45.350 1.00 70.26 O ANISOU 4492 O GLN B 305 8591 8939 9166 758 170 -430 O ATOM 4493 CB GLN B 305 141.217 -0.132 42.056 1.00 56.82 C ANISOU 4493 CB GLN B 305 6890 7243 7457 722 153 -563 C ATOM 4494 CG GLN B 305 141.380 -1.311 41.101 1.00 58.05 C ANISOU 4494 CG GLN B 305 7028 7389 7638 716 111 -630 C ATOM 4495 CD GLN B 305 142.514 -2.245 41.487 1.00 81.62 C ANISOU 4495 CD GLN B 305 10007 10356 10648 710 76 -680 C ATOM 4496 OE1 GLN B 305 143.268 -1.974 42.422 1.00 84.07 O ANISOU 4496 OE1 GLN B 305 10329 10663 10951 709 85 -667 O ATOM 4497 NE2 GLN B 305 142.642 -3.351 40.761 1.00 94.08 N ANISOU 4497 NE2 GLN B 305 11567 11921 12258 703 36 -737 N ATOM 4498 N ARG B 312 146.776 -6.567 46.980 1.00 85.68 N ANISOU 4498 N ARG B 312 10471 10802 11283 774 -118 -771 N ATOM 4499 CA ARG B 312 146.929 -7.631 47.966 1.00 92.49 C ANISOU 4499 CA ARG B 312 11324 11647 12173 796 -159 -765 C ATOM 4500 C ARG B 312 145.723 -8.563 47.954 1.00101.52 C ANISOU 4500 C ARG B 312 12464 12768 13340 815 -171 -704 C ATOM 4501 O ARG B 312 145.539 -9.378 48.859 1.00106.64 O ANISOU 4501 O ARG B 312 13107 13403 14008 836 -199 -676 O ATOM 4502 CB ARG B 312 147.138 -7.039 49.360 1.00106.95 C ANISOU 4502 CB ARG B 312 13162 13488 13985 818 -152 -735 C ATOM 4503 CG ARG B 312 148.391 -6.188 49.463 1.00107.05 C ANISOU 4503 CG ARG B 312 13175 13522 13979 802 -146 -793 C ATOM 4504 CD ARG B 312 148.734 -5.846 50.901 1.00114.59 C ANISOU 4504 CD ARG B 312 14134 14483 14921 825 -150 -773 C ATOM 4505 NE ARG B 312 150.063 -5.249 51.000 1.00112.68 N ANISOU 4505 NE ARG B 312 13886 14259 14670 808 -156 -835 N ATOM 4506 CZ ARG B 312 150.658 -4.928 52.144 1.00113.16 C ANISOU 4506 CZ ARG B 312 13948 14327 14720 823 -164 -836 C ATOM 4507 NH1 ARG B 312 150.043 -5.145 53.298 1.00108.75 N ANISOU 4507 NH1 ARG B 312 13399 13760 14160 854 -166 -780 N ATOM 4508 NH2 ARG B 312 151.870 -4.390 52.135 1.00122.02 N ANISOU 4508 NH2 ARG B 312 15060 15465 15837 806 -169 -892 N ATOM 4509 N LYS B 313 144.904 -8.427 46.916 1.00 84.55 N ANISOU 4509 N LYS B 313 10317 10618 11189 805 -152 -683 N ATOM 4510 CA LYS B 313 143.778 -9.323 46.685 1.00 73.25 C ANISOU 4510 CA LYS B 313 8870 9172 9788 825 -184 -650 C ATOM 4511 C LYS B 313 143.680 -9.615 45.191 1.00 72.66 C ANISOU 4511 C LYS B 313 8782 9094 9730 805 -203 -714 C ATOM 4512 O LYS B 313 143.940 -8.743 44.363 1.00 73.23 O ANISOU 4512 O LYS B 313 8862 9183 9778 783 -171 -748 O ATOM 4513 CB LYS B 313 142.470 -8.714 47.204 1.00 80.25 C ANISOU 4513 CB LYS B 313 9762 10068 10660 849 -156 -547 C ATOM 4514 CG LYS B 313 142.455 -8.439 48.701 1.00106.00 C ANISOU 4514 CG LYS B 313 13033 13332 13911 865 -136 -478 C ATOM 4515 CD LYS B 313 141.139 -7.829 49.155 1.00 94.95 C ANISOU 4515 CD LYS B 313 11631 11941 12505 880 -109 -374 C ATOM 4516 CE LYS B 313 141.168 -7.526 50.647 1.00106.16 C ANISOU 4516 CE LYS B 313 13053 13365 13918 898 -107 -335 C ATOM 4517 NZ LYS B 313 139.854 -7.035 51.150 1.00106.84 N ANISOU 4517 NZ LYS B 313 13131 13455 14007 906 -88 -234 N ATOM 4518 N SER B 314 143.314 -10.846 44.853 1.00 73.32 N ANISOU 4518 N SER B 314 8848 9155 9857 811 -252 -728 N ATOM 4519 CA SER B 314 143.180 -11.257 43.459 1.00 54.26 C ANISOU 4519 CA SER B 314 6417 6731 7466 791 -274 -789 C ATOM 4520 C SER B 314 141.926 -10.662 42.830 1.00 65.62 C ANISOU 4520 C SER B 314 7857 8180 8895 801 -255 -740 C ATOM 4521 O SER B 314 141.006 -10.249 43.534 1.00 78.19 O ANISOU 4521 O SER B 314 9456 9781 10472 828 -238 -648 O ATOM 4522 CB SER B 314 143.153 -12.781 43.340 1.00 51.58 C ANISOU 4522 CB SER B 314 6058 6360 7181 793 -336 -815 C ATOM 4523 OG SER B 314 141.938 -13.312 43.839 1.00 76.18 O ANISOU 4523 OG SER B 314 9169 9462 10313 822 -357 -729 O ATOM 4524 N LEU B 315 141.906 -10.602 41.502 1.00 64.21 N ANISOU 4524 N LEU B 315 7669 8001 8724 777 -255 -800 N ATOM 4525 CA LEU B 315 140.770 -10.053 40.765 1.00 63.33 C ANISOU 4525 CA LEU B 315 7557 7900 8605 784 -239 -763 C ATOM 4526 C LEU B 315 139.415 -10.705 41.116 1.00 58.98 C ANISOU 4526 C LEU B 315 6992 7335 8082 817 -274 -671 C ATOM 4527 O LEU B 315 138.441 -9.983 41.374 1.00 61.08 O ANISOU 4527 O LEU B 315 7264 7620 8325 836 -250 -587 O ATOM 4528 CB LEU B 315 141.040 -10.166 39.259 1.00 61.34 C ANISOU 4528 CB LEU B 315 7296 7644 8367 749 -242 -852 C ATOM 4529 CG LEU B 315 139.960 -9.701 38.287 1.00 54.40 C ANISOU 4529 CG LEU B 315 6412 6772 7484 750 -229 -834 C ATOM 4530 CD1 LEU B 315 139.600 -8.256 38.560 1.00 61.00 C ANISOU 4530 CD1 LEU B 315 7269 7644 8265 759 -171 -781 C ATOM 4531 CD2 LEU B 315 140.449 -9.872 36.860 1.00 46.12 C ANISOU 4531 CD2 LEU B 315 5360 5718 6446 706 -228 -932 C ATOM 4532 N PRO B 316 139.334 -12.057 41.128 1.00 50.15 N ANISOU 4532 N PRO B 316 5858 6185 7012 819 -331 -679 N ATOM 4533 CA PRO B 316 138.059 -12.651 41.556 1.00 51.56 C ANISOU 4533 CA PRO B 316 6027 6352 7210 842 -362 -574 C ATOM 4534 C PRO B 316 137.644 -12.248 42.967 1.00 59.51 C ANISOU 4534 C PRO B 316 7048 7376 8186 866 -336 -470 C ATOM 4535 O PRO B 316 136.452 -12.112 43.241 1.00 54.46 O ANISOU 4535 O PRO B 316 6407 6745 7539 879 -335 -366 O ATOM 4536 CB PRO B 316 138.332 -14.157 41.489 1.00 51.31 C ANISOU 4536 CB PRO B 316 5981 6283 7231 835 -422 -608 C ATOM 4537 CG PRO B 316 139.435 -14.295 40.514 1.00 60.81 C ANISOU 4537 CG PRO B 316 7177 7477 8451 806 -427 -737 C ATOM 4538 CD PRO B 316 140.302 -13.099 40.741 1.00 60.43 C ANISOU 4538 CD PRO B 316 7148 7461 8352 797 -369 -772 C ATOM 4539 N GLU B 317 138.623 -12.075 43.848 1.00 64.21 N ANISOU 4539 N GLU B 317 7656 7975 8764 867 -317 -496 N ATOM 4540 CA GLU B 317 138.366 -11.663 45.225 1.00 50.75 C ANISOU 4540 CA GLU B 317 5964 6285 7033 885 -288 -408 C ATOM 4541 C GLU B 317 137.818 -10.240 45.266 1.00 50.79 C ANISOU 4541 C GLU B 317 5979 6320 6999 890 -234 -355 C ATOM 4542 O GLU B 317 136.914 -9.922 46.050 1.00 56.01 O ANISOU 4542 O GLU B 317 6641 6991 7649 902 -216 -250 O ATOM 4543 CB GLU B 317 139.654 -11.772 46.044 1.00 56.19 C ANISOU 4543 CB GLU B 317 6664 6970 7716 881 -282 -459 C ATOM 4544 CG GLU B 317 139.514 -11.514 47.531 1.00 93.08 C ANISOU 4544 CG GLU B 317 11347 11651 12370 897 -257 -378 C ATOM 4545 CD GLU B 317 140.811 -11.775 48.277 1.00110.99 C ANISOU 4545 CD GLU B 317 13622 13911 14637 893 -260 -434 C ATOM 4546 OE1 GLU B 317 141.795 -12.198 47.632 1.00108.26 O ANISOU 4546 OE1 GLU B 317 13273 13555 14306 876 -284 -532 O ATOM 4547 OE2 GLU B 317 140.848 -11.559 49.506 1.00116.42 O ANISOU 4547 OE2 GLU B 317 14319 14604 15312 903 -239 -379 O ATOM 4548 N LEU B 318 138.353 -9.401 44.383 1.00 56.36 N ANISOU 4548 N LEU B 318 6691 7039 7684 874 -208 -427 N ATOM 4549 CA LEU B 318 137.921 -8.018 44.260 1.00 53.10 C ANISOU 4549 CA LEU B 318 6288 6654 7233 875 -157 -391 C ATOM 4550 C LEU B 318 136.466 -7.978 43.824 1.00 48.10 C ANISOU 4550 C LEU B 318 5642 6027 6607 886 -167 -310 C ATOM 4551 O LEU B 318 135.636 -7.275 44.420 1.00 49.22 O ANISOU 4551 O LEU B 318 5786 6183 6732 893 -141 -218 O ATOM 4552 CB LEU B 318 138.803 -7.277 43.252 1.00 46.23 C ANISOU 4552 CB LEU B 318 5428 5797 6340 849 -129 -490 C ATOM 4553 CG LEU B 318 138.901 -5.754 43.308 1.00 57.01 C ANISOU 4553 CG LEU B 318 6812 7190 7658 840 -68 -477 C ATOM 4554 CD1 LEU B 318 139.808 -5.323 44.450 1.00 53.97 C ANISOU 4554 CD1 LEU B 318 6444 6806 7256 836 -44 -473 C ATOM 4555 CD2 LEU B 318 139.407 -5.210 41.981 1.00 61.44 C ANISOU 4555 CD2 LEU B 318 7381 7763 8200 809 -47 -562 C ATOM 4556 N LEU B 319 136.154 -8.758 42.792 1.00 44.29 N ANISOU 4556 N LEU B 319 5145 5530 6153 881 -208 -343 N ATOM 4557 CA LEU B 319 134.783 -8.824 42.310 1.00 52.84 C ANISOU 4557 CA LEU B 319 6215 6617 7244 888 -227 -264 C ATOM 4558 C LEU B 319 133.863 -9.386 43.382 1.00 48.12 C ANISOU 4558 C LEU B 319 5614 6013 6655 899 -244 -141 C ATOM 4559 O LEU B 319 132.721 -8.954 43.519 1.00 50.09 O ANISOU 4559 O LEU B 319 5861 6276 6895 900 -234 -41 O ATOM 4560 CB LEU B 319 134.686 -9.683 41.049 1.00 38.80 C ANISOU 4560 CB LEU B 319 4420 4817 5506 876 -275 -324 C ATOM 4561 CG LEU B 319 135.327 -9.184 39.755 1.00 39.25 C ANISOU 4561 CG LEU B 319 4475 4879 5560 857 -257 -439 C ATOM 4562 CD1 LEU B 319 134.941 -10.108 38.612 1.00 47.28 C ANISOU 4562 CD1 LEU B 319 5468 5869 6626 844 -309 -473 C ATOM 4563 CD2 LEU B 319 134.914 -7.754 39.457 1.00 38.41 C ANISOU 4563 CD2 LEU B 319 4379 4811 5405 860 -203 -415 C ATOM 4564 N ARG B 320 134.371 -10.338 44.156 1.00 45.36 N ANISOU 4564 N ARG B 320 5264 5644 6325 901 -266 -149 N ATOM 4565 CA ARG B 320 133.562 -10.962 45.191 1.00 50.14 C ANISOU 4565 CA ARG B 320 5868 6247 6937 907 -275 -39 C ATOM 4566 C ARG B 320 133.221 -9.967 46.288 1.00 50.74 C ANISOU 4566 C ARG B 320 5947 6338 6993 907 -225 42 C ATOM 4567 O ARG B 320 132.129 -10.009 46.853 1.00 54.27 O ANISOU 4567 O ARG B 320 6383 6785 7451 899 -223 151 O ATOM 4568 CB ARG B 320 134.277 -12.177 45.783 1.00 56.37 C ANISOU 4568 CB ARG B 320 6656 7012 7749 910 -307 -76 C ATOM 4569 CG ARG B 320 133.332 -13.236 46.328 1.00 45.69 C ANISOU 4569 CG ARG B 320 5298 5655 6407 913 -334 17 C ATOM 4570 CD ARG B 320 133.930 -13.935 47.531 1.00 62.02 C ANISOU 4570 CD ARG B 320 7370 7714 8480 921 -337 18 C ATOM 4571 NE ARG B 320 134.137 -13.004 48.636 1.00 68.44 N ANISOU 4571 NE ARG B 320 8190 8543 9271 926 -284 59 N ATOM 4572 CZ ARG B 320 134.617 -13.349 49.825 1.00 77.47 C ANISOU 4572 CZ ARG B 320 9337 9683 10417 932 -276 71 C ATOM 4573 NH1 ARG B 320 134.769 -12.432 50.771 1.00 79.48 N ANISOU 4573 NH1 ARG B 320 9592 9944 10662 929 -231 107 N ATOM 4574 NH2 ARG B 320 134.945 -14.610 50.069 1.00 84.84 N ANISOU 4574 NH2 ARG B 320 10270 10598 11366 937 -315 46 N ATOM 4575 N GLU B 321 134.142 -9.055 46.580 1.00 49.16 N ANISOU 4575 N GLU B 321 5758 6145 6776 906 -189 -15 N ATOM 4576 CA GLU B 321 133.847 -8.040 47.579 1.00 57.44 C ANISOU 4576 CA GLU B 321 6806 7195 7824 894 -152 45 C ATOM 4577 C GLU B 321 132.878 -7.001 47.037 1.00 60.36 C ANISOU 4577 C GLU B 321 7171 7572 8190 878 -145 79 C ATOM 4578 O GLU B 321 131.922 -6.624 47.717 1.00 51.72 O ANISOU 4578 O GLU B 321 6073 6462 7117 853 -169 135 O ATOM 4579 CB GLU B 321 135.125 -7.360 48.061 1.00 52.42 C ANISOU 4579 CB GLU B 321 6187 6565 7165 894 -119 -27 C ATOM 4580 CG GLU B 321 135.989 -8.251 48.923 1.00 77.95 C ANISOU 4580 CG GLU B 321 9425 9786 10407 903 -132 -51 C ATOM 4581 CD GLU B 321 137.208 -7.533 49.450 1.00 93.31 C ANISOU 4581 CD GLU B 321 11387 11736 12331 898 -101 -111 C ATOM 4582 OE1 GLU B 321 137.308 -6.303 49.250 1.00 96.62 O ANISOU 4582 OE1 GLU B 321 11814 12169 12727 887 -65 -125 O ATOM 4583 OE2 GLU B 321 138.066 -8.199 50.063 1.00109.20 O ANISOU 4583 OE2 GLU B 321 13406 13739 14348 904 -114 -144 O ATOM 4584 N VAL B 322 133.128 -6.528 45.819 1.00 46.41 N ANISOU 4584 N VAL B 322 5414 5828 6393 886 -132 19 N ATOM 4585 CA VAL B 322 132.284 -5.478 45.255 1.00 30.47 C ANISOU 4585 CA VAL B 322 3398 3826 4353 876 -122 43 C ATOM 4586 C VAL B 322 130.848 -5.934 44.962 1.00 32.71 C ANISOU 4586 C VAL B 322 3674 4099 4657 865 -171 121 C ATOM 4587 O VAL B 322 129.899 -5.162 45.117 1.00 33.47 O ANISOU 4587 O VAL B 322 3790 4211 4716 853 -178 159 O ATOM 4588 CB VAL B 322 132.910 -4.916 43.963 1.00 48.61 C ANISOU 4588 CB VAL B 322 5706 6152 6614 886 -93 -42 C ATOM 4589 CG1 VAL B 322 132.027 -3.835 43.361 1.00 55.03 C ANISOU 4589 CG1 VAL B 322 6526 6994 7390 881 -74 -9 C ATOM 4590 CG2 VAL B 322 134.289 -4.358 44.261 1.00 36.77 C ANISOU 4590 CG2 VAL B 322 4222 4658 5092 882 -53 -126 C ATOM 4591 N LEU B 323 130.684 -7.199 44.588 1.00 39.85 N ANISOU 4591 N LEU B 323 4561 4986 5593 871 -202 143 N ATOM 4592 CA LEU B 323 129.404 -7.668 44.061 1.00 35.11 C ANISOU 4592 CA LEU B 323 3958 4373 5007 852 -253 201 C ATOM 4593 C LEU B 323 128.580 -8.495 45.046 1.00 40.14 C ANISOU 4593 C LEU B 323 4616 4976 5659 821 -320 230 C ATOM 4594 O LEU B 323 127.512 -8.998 44.691 1.00 32.27 O ANISOU 4594 O LEU B 323 3657 3990 4616 832 -375 240 O ATOM 4595 CB LEU B 323 129.636 -8.484 42.787 1.00 23.23 C ANISOU 4595 CB LEU B 323 2444 2888 3495 879 -257 178 C ATOM 4596 CG LEU B 323 130.421 -7.778 41.678 1.00 40.25 C ANISOU 4596 CG LEU B 323 4606 5062 5623 892 -239 65 C ATOM 4597 CD1 LEU B 323 130.614 -8.698 40.481 1.00 30.50 C ANISOU 4597 CD1 LEU B 323 3361 3809 4421 887 -290 -9 C ATOM 4598 CD2 LEU B 323 129.738 -6.481 41.267 1.00 33.91 C ANISOU 4598 CD2 LEU B 323 3813 4289 4782 888 -208 101 C ATOM 4599 N THR B 324 129.070 -8.641 46.275 1.00 35.68 N ANISOU 4599 N THR B 324 4047 4395 5113 810 -309 230 N ATOM 4600 CA THR B 324 128.382 -9.472 47.260 1.00 42.15 C ANISOU 4600 CA THR B 324 4904 5192 5919 801 -381 222 C ATOM 4601 C THR B 324 128.317 -8.817 48.643 1.00 50.49 C ANISOU 4601 C THR B 324 5982 6255 6948 802 -372 227 C ATOM 4602 O THR B 324 128.413 -9.491 49.670 1.00 43.50 O ANISOU 4602 O THR B 324 5103 5349 6075 795 -397 221 O ATOM 4603 CB THR B 324 129.051 -10.855 47.391 1.00 41.70 C ANISOU 4603 CB THR B 324 4786 5168 5891 800 -268 358 C ATOM 4604 OG1 THR B 324 129.536 -11.279 46.111 1.00 47.05 O ANISOU 4604 OG1 THR B 324 5478 5898 6499 878 -267 304 O ATOM 4605 CG2 THR B 324 128.053 -11.880 47.909 1.00 71.20 C ANISOU 4605 CG2 THR B 324 8687 8992 9373 933 -389 200 C ATOM 4606 N GLU B 325 128.158 -7.500 48.669 1.00 46.46 N ANISOU 4606 N GLU B 325 5479 5774 6399 812 -332 243 N ATOM 4607 CA GLU B 325 127.936 -6.801 49.927 1.00 37.93 C ANISOU 4607 CA GLU B 325 4416 4709 5288 821 -315 268 C ATOM 4608 C GLU B 325 126.579 -7.197 50.515 1.00 32.62 C ANISOU 4608 C GLU B 325 3776 4051 4566 822 -327 337 C ATOM 4609 O GLU B 325 125.585 -7.273 49.793 1.00 33.40 O ANISOU 4609 O GLU B 325 3891 4162 4640 809 -329 376 O ATOM 4610 CB GLU B 325 128.018 -5.287 49.715 1.00 33.09 C ANISOU 4610 CB GLU B 325 3813 4135 4623 814 -250 274 C ATOM 4611 CG GLU B 325 127.956 -4.466 50.990 1.00 55.58 C ANISOU 4611 CG GLU B 325 6681 7016 7422 823 -208 304 C ATOM 4612 CD GLU B 325 127.942 -2.973 50.718 1.00 61.06 C ANISOU 4612 CD GLU B 325 7390 7751 8060 817 -148 312 C ATOM 4613 OE1 GLU B 325 129.014 -2.338 50.808 1.00 64.85 O ANISOU 4613 OE1 GLU B 325 7862 8236 8541 824 -120 263 O ATOM 4614 OE2 GLU B 325 126.856 -2.435 50.413 1.00 59.76 O ANISOU 4614 OE2 GLU B 325 7243 7613 7851 803 -125 369 O ATOM 4615 N GLU B 326 126.543 -7.466 51.819 1.00 45.08 N ANISOU 4615 N GLU B 326 5360 5629 6139 834 -327 357 N ATOM 4616 CA GLU B 326 125.275 -7.671 52.513 1.00 41.52 C ANISOU 4616 CA GLU B 326 4930 5196 5650 828 -316 431 C ATOM 4617 C GLU B 326 124.700 -6.312 52.870 1.00 38.24 C ANISOU 4617 C GLU B 326 4524 4824 5180 814 -248 482 C ATOM 4618 O GLU B 326 125.390 -5.483 53.455 1.00 54.24 O ANISOU 4618 O GLU B 326 6551 6866 7193 823 -215 464 O ATOM 4619 CB GLU B 326 125.449 -8.517 53.781 1.00 49.61 C ANISOU 4619 CB GLU B 326 5954 6204 6692 847 -341 432 C ATOM 4620 CG GLU B 326 125.706 -10.004 53.554 1.00 62.26 C ANISOU 4620 CG GLU B 326 7554 7769 8334 864 -409 395 C ATOM 4621 CD GLU B 326 125.909 -10.771 54.857 1.00 69.81 C ANISOU 4621 CD GLU B 326 8511 8711 9304 884 -431 396 C ATOM 4622 OE1 GLU B 326 125.099 -10.599 55.794 1.00 56.11 O ANISOU 4622 OE1 GLU B 326 6786 6995 7539 878 -402 457 O ATOM 4623 OE2 GLU B 326 126.886 -11.545 54.946 1.00 56.70 O ANISOU 4623 OE2 GLU B 326 6843 7027 7675 885 -459 336 O ATOM 4624 N SER B 327 123.443 -6.078 52.518 1.00 31.24 N ANISOU 4624 N SER B 327 3647 3958 4265 792 -225 545 N ATOM 4625 CA SER B 327 122.805 -4.816 52.855 1.00 40.84 C ANISOU 4625 CA SER B 327 4869 5216 5433 778 -159 594 C ATOM 4626 C SER B 327 122.072 -4.917 54.191 1.00 36.34 C ANISOU 4626 C SER B 327 4299 4661 4849 778 -136 647 C ATOM 4627 O SER B 327 121.900 -3.921 54.893 1.00 19.28 O ANISOU 4627 O SER B 327 2140 2533 2653 777 -84 672 O ATOM 4628 CB SER B 327 121.852 -4.391 51.737 1.00 40.58 C ANISOU 4628 CB SER B 327 4839 5199 5382 751 -141 630 C ATOM 4629 OG SER B 327 122.579 -4.011 50.580 1.00 36.03 O ANISOU 4629 OG SER B 327 4262 4616 4810 751 -149 582 O ATOM 4630 N VAL B 328 121.661 -6.130 54.543 1.00 26.24 N ANISOU 4630 N VAL B 328 3017 3358 3596 780 -175 661 N ATOM 4631 CA VAL B 328 120.995 -6.380 55.814 1.00 30.46 C ANISOU 4631 CA VAL B 328 3548 3902 4124 781 -159 708 C ATOM 4632 C VAL B 328 121.697 -7.513 56.551 1.00 45.55 C ANISOU 4632 C VAL B 328 5460 5779 6068 805 -209 674 C ATOM 4633 O VAL B 328 121.596 -8.673 56.157 1.00 48.16 O ANISOU 4633 O VAL B 328 5790 6081 6428 808 -258 664 O ATOM 4634 CB VAL B 328 119.509 -6.749 55.622 1.00 36.39 C ANISOU 4634 CB VAL B 328 4291 4661 4874 755 -150 774 C ATOM 4635 CG1 VAL B 328 118.838 -6.976 56.967 1.00 35.54 C ANISOU 4635 CG1 VAL B 328 4176 4566 4764 756 -130 819 C ATOM 4636 CG2 VAL B 328 118.783 -5.670 54.836 1.00 26.12 C ANISOU 4636 CG2 VAL B 328 2987 3393 3546 730 -103 805 C ATOM 4637 N VAL B 329 122.438 -7.175 57.600 1.00 44.48 N ANISOU 4637 N VAL B 329 5326 5649 5927 825 -197 655 N ATOM 4638 CA VAL B 329 123.069 -8.200 58.424 1.00 40.40 C ANISOU 4638 CA VAL B 329 4807 5101 5440 848 -242 626 C ATOM 4639 C VAL B 329 122.034 -8.988 59.238 1.00 41.24 C ANISOU 4639 C VAL B 329 4914 5207 5550 843 -246 681 C ATOM 4640 O VAL B 329 121.083 -8.416 59.773 1.00 46.27 O ANISOU 4640 O VAL B 329 5546 5874 6160 829 -199 739 O ATOM 4641 CB VAL B 329 124.107 -7.580 59.362 1.00 34.70 C ANISOU 4641 CB VAL B 329 4087 4387 4712 867 -225 594 C ATOM 4642 CG1 VAL B 329 124.936 -8.669 60.022 1.00 51.77 C ANISOU 4642 CG1 VAL B 329 6244 6511 6915 890 -279 553 C ATOM 4643 CG2 VAL B 329 125.008 -6.641 58.575 1.00 22.26 C ANISOU 4643 CG2 VAL B 329 2510 2819 3129 867 -208 547 C ATOM 4644 N ARG B 330 122.220 -10.303 59.327 1.00 46.39 N ANISOU 4644 N ARG B 330 5567 5825 6235 856 -302 661 N ATOM 4645 CA ARG B 330 121.257 -11.167 60.005 1.00 62.01 C ANISOU 4645 CA ARG B 330 7543 7800 8219 852 -309 711 C ATOM 4646 C ARG B 330 121.946 -12.188 60.908 1.00 68.94 C ANISOU 4646 C ARG B 330 8425 8649 9122 880 -354 680 C ATOM 4647 O ARG B 330 121.349 -12.690 61.862 1.00 72.97 O ANISOU 4647 O ARG B 330 8933 9159 9632 882 -352 719 O ATOM 4648 CB ARG B 330 120.368 -11.875 58.977 1.00 49.56 C ANISOU 4648 CB ARG B 330 5964 6214 6651 833 -328 736 C ATOM 4649 CG ARG B 330 119.635 -10.907 58.064 1.00 54.60 C ANISOU 4649 CG ARG B 330 6598 6880 7268 804 -286 768 C ATOM 4650 CD ARG B 330 118.513 -11.546 57.270 1.00 59.48 C ANISOU 4650 CD ARG B 330 7211 7495 7895 779 -295 808 C ATOM 4651 NE ARG B 330 117.572 -10.522 56.823 1.00 37.58 N ANISOU 4651 NE ARG B 330 4427 4753 5098 749 -244 854 N ATOM 4652 CZ ARG B 330 116.672 -10.692 55.861 1.00 62.74 C ANISOU 4652 CZ ARG B 330 7608 7943 8289 723 -244 884 C ATOM 4653 NH1 ARG B 330 116.585 -11.852 55.226 1.00 72.97 N ANISOU 4653 NH1 ARG B 330 8907 9211 9609 723 -290 875 N ATOM 4654 NH2 ARG B 330 115.861 -9.696 55.530 1.00 61.11 N ANISOU 4654 NH2 ARG B 330 7391 7767 8061 698 -197 923 N ATOM 4655 N GLU B 331 123.204 -12.487 60.603 1.00 66.53 N ANISOU 4655 N GLU B 331 8122 8318 8839 903 -395 609 N ATOM 4656 CA GLU B 331 123.990 -13.419 61.404 1.00 79.61 C ANISOU 4656 CA GLU B 331 9781 9947 10522 932 -441 570 C ATOM 4657 C GLU B 331 125.383 -12.867 61.683 1.00 80.01 C ANISOU 4657 C GLU B 331 9823 9987 10591 946 -447 509 C ATOM 4658 O GLU B 331 126.144 -12.583 60.759 1.00 98.14 O ANISOU 4658 O GLU B 331 12111 12273 12905 945 -459 459 O ATOM 4659 CB GLU B 331 124.094 -14.775 60.705 1.00 90.87 C ANISOU 4659 CB GLU B 331 11213 11347 11965 950 -496 539 C ATOM 4660 CG GLU B 331 122.788 -15.547 60.655 1.00 86.35 C ANISOU 4660 CG GLU B 331 10643 10780 11385 935 -491 602 C ATOM 4661 CD GLU B 331 122.935 -16.898 59.987 1.00 90.69 C ANISOU 4661 CD GLU B 331 11199 11315 11944 957 -533 576 C ATOM 4662 OE1 GLU B 331 123.916 -17.089 59.238 1.00110.48 O ANISOU 4662 OE1 GLU B 331 13710 13819 14449 981 -553 511 O ATOM 4663 OE2 GLU B 331 122.070 -17.770 60.214 1.00 97.99 O ANISOU 4663 OE2 GLU B 331 12123 12238 12873 950 -537 622 O TER 4664 GLU B 331 HETATM 4665 C15 9P2 A 401 102.111 -11.354 29.647 1.00 27.38 C HETATM 4666 C16 9P2 A 401 102.308 -12.603 29.052 1.00 21.68 C HETATM 4667 C17 9P2 A 401 103.477 -13.254 29.206 1.00 27.15 C HETATM 4668 C18 9P2 A 401 104.570 -12.648 30.018 1.00 21.05 C HETATM 4669 C20 9P2 A 401 102.003 -14.652 28.081 1.00 44.96 C HETATM 4670 C01 9P2 A 401 102.449 -14.099 32.942 1.00 21.68 C HETATM 4671 N02 9P2 A 401 103.606 -14.892 32.779 1.00 22.85 N HETATM 4672 C03 9P2 A 401 104.697 -14.142 33.026 1.00 31.47 C HETATM 4673 C04 9P2 A 401 104.238 -12.834 33.376 1.00 28.06 C HETATM 4674 N05 9P2 A 401 102.844 -12.857 33.290 1.00 20.47 N HETATM 4675 C06 9P2 A 401 102.017 -11.757 33.584 1.00 24.74 C HETATM 4676 C07 9P2 A 401 101.884 -11.731 35.112 1.00 18.84 C HETATM 4677 C08 9P2 A 401 100.798 -10.764 35.661 1.00 23.85 C HETATM 4678 C09 9P2 A 401 100.709 -10.876 37.220 1.00 18.00 C HETATM 4679 C10 9P2 A 401 105.126 -11.573 33.743 1.00 30.94 C HETATM 4680 N11 9P2 A 401 104.836 -10.501 32.810 1.00 29.38 N HETATM 4681 C12 9P2 A 401 105.454 -10.742 31.467 1.00 26.33 C HETATM 4682 C13 9P2 A 401 104.374 -11.397 30.608 1.00 33.00 C HETATM 4683 C14 9P2 A 401 103.189 -10.750 30.453 1.00 43.98 C HETATM 4684 O19 9P2 A 401 103.400 -14.503 28.487 1.00 51.24 O HETATM 4685 O21 9P2 A 401 101.413 -13.376 28.233 1.00 29.01 O HETATM 4686 C22 9P2 A 401 105.152 -9.203 33.363 1.00 37.76 C HETATM 4687 C23 9P2 A 401 103.802 -8.524 33.793 1.00 28.45 C HETATM 4688 C24 9P2 A 401 103.611 -8.084 35.074 1.00 19.35 C HETATM 4689 C25 9P2 A 401 102.304 -7.448 35.451 1.00 35.96 C HETATM 4690 O26 9P2 A 401 101.849 -6.930 36.623 1.00 50.37 O HETATM 4691 C27 9P2 A 401 100.668 -6.225 36.311 1.00 26.98 C HETATM 4692 O28 9P2 A 401 100.223 -6.708 35.106 1.00 27.28 O HETATM 4693 C29 9P2 A 401 101.298 -7.310 34.513 1.00 30.54 C HETATM 4694 C30 9P2 A 401 101.498 -7.776 33.171 1.00 32.04 C HETATM 4695 C31 9P2 A 401 102.746 -8.382 32.815 1.00 40.89 C HETATM 4696 C32 9P2 A 401 105.985 -14.593 32.977 1.00 32.08 C HETATM 4697 C33 9P2 A 401 106.464 -15.248 31.845 1.00 20.01 C HETATM 4698 C34 9P2 A 401 107.801 -15.726 31.822 1.00 21.53 C HETATM 4699 C35 9P2 A 401 108.637 -15.554 32.932 1.00 19.51 C HETATM 4700 C36 9P2 A 401 108.147 -14.896 34.092 1.00 26.66 C HETATM 4701 C37 9P2 A 401 106.834 -14.429 34.115 1.00 33.80 C HETATM 4702 C38 9P2 A 401 101.076 -14.591 32.744 1.00 21.30 C HETATM 4703 C39 9P2 A 401 100.160 -13.894 31.936 1.00 24.80 C HETATM 4704 C40 9P2 A 401 98.869 -14.366 31.751 1.00 21.74 C HETATM 4705 C41 9P2 A 401 98.479 -15.533 32.347 1.00 26.01 C HETATM 4706 C42 9P2 A 401 99.398 -16.242 33.149 1.00 23.77 C HETATM 4707 C43 9P2 A 401 100.691 -15.758 33.331 1.00 23.02 C HETATM 4708 O1 TLA A 402 91.562 -2.837 52.938 1.00 60.77 O HETATM 4709 O11 TLA A 402 92.733 -4.670 52.940 1.00 59.87 O HETATM 4710 C1 TLA A 402 91.671 -4.059 52.698 1.00 58.48 C HETATM 4711 C2 TLA A 402 90.498 -4.788 52.105 1.00 52.31 C HETATM 4712 O2 TLA A 402 89.206 -4.200 52.271 1.00 87.57 O HETATM 4713 C3 TLA A 402 90.712 -6.090 51.315 1.00 38.23 C HETATM 4714 O3 TLA A 402 91.276 -7.245 51.934 1.00 69.19 O HETATM 4715 C4 TLA A 402 90.360 -6.134 49.851 1.00 59.65 C HETATM 4716 O4 TLA A 402 90.617 -5.127 49.171 1.00 71.71 O HETATM 4717 O41 TLA A 402 89.830 -7.132 49.312 1.00 49.89 O HETATM 4718 O1 TLA A 403 88.885 -25.998 53.898 1.00 47.20 O HETATM 4719 O11 TLA A 403 87.429 -24.985 55.126 1.00 77.67 O HETATM 4720 C1 TLA A 403 87.774 -25.453 54.026 1.00 71.83 C HETATM 4721 C2 TLA A 403 86.830 -25.361 52.861 1.00 43.25 C HETATM 4722 O2 TLA A 403 86.577 -24.076 52.302 1.00 53.75 O HETATM 4723 C3 TLA A 403 86.148 -26.620 52.307 1.00 65.07 C HETATM 4724 O3 TLA A 403 85.095 -27.264 53.027 1.00101.65 O HETATM 4725 C4 TLA A 403 86.571 -27.213 50.990 1.00 74.24 C HETATM 4726 O4 TLA A 403 85.850 -28.068 50.434 1.00 76.80 O HETATM 4727 O41 TLA A 403 87.646 -26.863 50.462 1.00 85.52 O HETATM 4728 C1 OLA A 404 105.765 -11.481 45.474 1.00 64.35 C HETATM 4729 O1 OLA A 404 106.120 -12.626 45.119 1.00 55.95 O HETATM 4730 O2 OLA A 404 105.418 -11.271 46.659 1.00 51.21 O HETATM 4731 C2 OLA A 404 105.759 -10.354 44.473 1.00 36.54 C HETATM 4732 C3 OLA A 404 105.326 -10.882 43.103 1.00 59.32 C HETATM 4733 C4 OLA A 404 105.907 -10.002 41.995 1.00 69.23 C HETATM 4734 C5 OLA A 404 105.022 -8.773 41.788 1.00 61.34 C HETATM 4735 C6 OLA A 404 104.599 -8.686 40.322 1.00 48.29 C HETATM 4736 C7 OLA A 404 103.179 -9.230 40.171 1.00 51.41 C HETATM 4737 C8 OLA A 404 102.392 -8.989 41.461 1.00 47.64 C HETATM 4738 C9 OLA A 404 101.443 -10.136 41.687 1.00 44.08 C HETATM 4739 C10 OLA A 404 100.563 -10.109 42.658 1.00 44.32 C HETATM 4740 C11 OLA A 404 100.464 -8.929 43.589 1.00 35.70 C HETATM 4741 C12 OLA A 404 99.009 -8.771 44.031 1.00 25.21 C HETATM 4742 C13 OLA A 404 98.931 -7.758 45.172 1.00 33.08 C HETATM 4743 C14 OLA A 404 97.573 -7.056 45.133 1.00 25.27 C HETATM 4744 C15 OLA A 404 97.759 -5.576 45.466 1.00 25.16 C HETATM 4745 C1 OLA A 405 104.625 -22.223 48.420 1.00 77.14 C HETATM 4746 O1 OLA A 405 105.559 -22.215 49.251 1.00 81.57 O HETATM 4747 O2 OLA A 405 103.996 -23.280 48.185 1.00 57.44 O HETATM 4748 C2 OLA A 405 104.262 -20.952 47.703 1.00 72.80 C HETATM 4749 C3 OLA A 405 105.114 -19.801 48.243 1.00 73.39 C HETATM 4750 C4 OLA A 405 106.307 -19.568 47.317 1.00 55.20 C HETATM 4751 C5 OLA A 405 105.810 -19.059 45.963 1.00 60.86 C HETATM 4752 C6 OLA A 405 105.605 -17.542 46.008 1.00 68.34 C HETATM 4753 C7 OLA A 405 105.513 -16.976 44.586 1.00 54.74 C HETATM 4754 C8 OLA A 405 104.046 -16.871 44.152 1.00 61.87 C HETATM 4755 C9 OLA A 405 103.867 -15.878 43.029 1.00 52.85 C HETATM 4756 C10 OLA A 405 102.869 -16.007 42.184 1.00 40.70 C HETATM 4757 C11 OLA A 405 101.893 -17.149 42.327 1.00 49.70 C HETATM 4758 C12 OLA A 405 101.870 -18.010 41.060 1.00 51.20 C HETATM 4759 C13 OLA A 405 101.812 -19.495 41.432 1.00 53.43 C HETATM 4760 C14 OLA A 405 102.891 -20.279 40.680 1.00 56.85 C HETATM 4761 C15 OLA A 405 102.438 -20.571 39.250 1.00 56.16 C HETATM 4762 C16 OLA A 405 103.263 -19.730 38.275 1.00 48.39 C HETATM 4763 C17 OLA A 405 104.421 -20.567 37.728 1.00 48.08 C HETATM 4764 C18 OLA A 405 105.028 -19.876 36.507 1.00 54.24 C HETATM 4765 C4 OLA A 406 105.760 -20.515 41.946 1.00 65.03 C HETATM 4766 C5 OLA A 406 106.428 -19.437 42.794 1.00 69.82 C HETATM 4767 C6 OLA A 406 107.784 -19.067 42.197 1.00 72.95 C HETATM 4768 C7 OLA A 406 107.643 -18.815 40.696 1.00 65.85 C HETATM 4769 C8 OLA A 406 107.241 -17.361 40.446 1.00 50.37 C HETATM 4770 C9 OLA A 406 107.894 -16.877 39.178 1.00 56.15 C HETATM 4771 C10 OLA A 406 107.162 -16.367 38.221 1.00 57.09 C HETATM 4772 C11 OLA A 406 105.670 -16.264 38.388 1.00 76.38 C HETATM 4773 C12 OLA A 406 105.071 -15.567 37.167 1.00 71.30 C HETATM 4774 C13 OLA A 406 104.482 -16.608 36.214 1.00 59.08 C HETATM 4775 C14 OLA A 406 103.086 -17.017 36.689 1.00 57.47 C HETATM 4776 C15 OLA A 406 102.071 -15.918 36.374 1.00 48.12 C HETATM 4777 C16 OLA A 406 101.359 -15.503 37.663 1.00 53.29 C HETATM 4778 C17 OLA A 406 100.745 -16.740 38.319 1.00 45.85 C HETATM 4779 C18 OLA A 406 99.629 -17.271 37.422 1.00 33.31 C HETATM 4780 C1 OLA A 407 86.742 5.301 41.115 1.00 71.77 C HETATM 4781 O1 OLA A 407 87.837 4.697 41.163 1.00 58.36 O HETATM 4782 O2 OLA A 407 86.361 5.969 42.101 1.00 72.88 O HETATM 4783 C2 OLA A 407 85.883 5.224 39.878 1.00 58.54 C HETATM 4784 C3 OLA A 407 86.754 4.965 38.646 1.00 44.78 C HETATM 4785 C4 OLA A 407 85.881 4.957 37.389 1.00 53.72 C HETATM 4786 C5 OLA A 407 86.630 4.275 36.245 1.00 68.12 C HETATM 4787 C6 OLA A 407 85.722 4.187 35.016 1.00 57.41 C HETATM 4788 C7 OLA A 407 86.430 3.397 33.914 1.00 71.21 C HETATM 4789 C8 OLA A 407 85.572 3.393 32.648 1.00 76.50 C HETATM 4790 C9 OLA A 407 85.850 4.641 31.854 1.00 73.37 C HETATM 4791 C10 OLA A 407 86.497 4.580 30.715 1.00 61.55 C HETATM 4792 C11 OLA A 407 86.979 3.260 30.170 1.00 71.07 C HETATM 4793 C12 OLA A 407 87.441 3.444 28.723 1.00 53.62 C HETATM 4794 C1 OLA A 408 71.577 -4.210 7.689 1.00 71.53 C HETATM 4795 O1 OLA A 408 72.606 -3.953 7.026 1.00 62.68 O HETATM 4796 O2 OLA A 408 70.594 -4.755 7.139 1.00 74.08 O HETATM 4797 C2 OLA A 408 71.522 -3.862 9.152 1.00 65.20 C HETATM 4798 C3 OLA A 408 70.319 -4.550 9.800 1.00 65.90 C HETATM 4799 C4 OLA A 408 70.714 -5.045 11.190 1.00 63.16 C HETATM 4800 C5 OLA A 408 71.241 -3.873 12.016 1.00 71.82 C HETATM 4801 C6 OLA A 408 71.071 -4.182 13.504 1.00 71.66 C HETATM 4802 C7 OLA A 408 72.181 -3.500 14.304 1.00 61.32 C HETATM 4803 C8 OLA A 408 71.628 -2.251 14.992 1.00 71.72 C HETATM 4804 C9 OLA A 408 71.258 -2.580 16.414 1.00 82.82 C HETATM 4805 C10 OLA A 408 71.829 -1.941 17.405 1.00 77.99 C HETATM 4806 C11 OLA A 408 72.858 -0.878 17.122 1.00 72.24 C HETATM 4807 C12 OLA A 408 72.899 0.126 18.274 1.00 61.17 C HETATM 4808 C13 OLA A 408 73.332 1.494 17.745 1.00 75.29 C HETATM 4809 C14 OLA A 408 74.505 1.326 16.779 1.00 58.57 C HETATM 4810 C4 OLA A 409 67.839 -8.525 9.898 1.00 58.49 C HETATM 4811 C5 OLA A 409 68.119 -10.017 10.082 1.00 61.17 C HETATM 4812 C6 OLA A 409 67.955 -10.377 11.559 1.00 65.40 C HETATM 4813 C7 OLA A 409 68.385 -11.824 11.818 1.00 55.78 C HETATM 4814 C8 OLA A 409 68.302 -12.084 13.323 1.00 67.30 C HETATM 4815 C9 OLA A 409 68.607 -13.523 13.645 1.00 60.71 C HETATM 4816 C10 OLA A 409 68.994 -13.828 14.859 1.00 57.31 C HETATM 4817 C11 OLA A 409 69.125 -12.738 15.894 1.00 63.03 C HETATM 4818 C12 OLA A 409 67.767 -12.467 16.546 1.00 77.58 C HETATM 4819 C13 OLA A 409 67.710 -11.028 17.068 1.00 74.56 C HETATM 4820 C14 OLA A 409 66.979 -10.988 18.414 1.00 80.04 C HETATM 4821 C15 OLA A 409 66.850 -9.540 18.891 1.00 71.09 C HETATM 4822 C4 OLA A 410 108.366 -22.129 14.620 1.00 66.27 C HETATM 4823 C5 OLA A 410 108.903 -22.416 16.021 1.00 59.19 C HETATM 4824 C6 OLA A 410 108.773 -21.166 16.893 1.00 64.04 C HETATM 4825 C7 OLA A 410 109.661 -21.322 18.127 1.00 73.43 C HETATM 4826 C8 OLA A 410 109.179 -20.380 19.230 1.00 68.69 C HETATM 4827 C9 OLA A 410 107.694 -20.543 19.406 1.00 68.03 C HETATM 4828 C10 OLA A 410 107.146 -20.269 20.562 1.00 56.82 C HETATM 4829 C11 OLA A 410 108.007 -19.795 21.702 1.00 56.33 C HETATM 4830 C12 OLA A 410 107.529 -18.410 22.138 1.00 62.40 C HETATM 4831 C13 OLA A 410 108.325 -17.956 23.362 1.00 46.37 C HETATM 4832 C1 OLA A 411 98.693 -29.454 49.873 1.00 63.89 C HETATM 4833 O1 OLA A 411 98.496 -30.687 49.789 1.00 54.77 O HETATM 4834 O2 OLA A 411 98.404 -28.842 50.926 1.00 60.67 O HETATM 4835 C2 OLA A 411 99.277 -28.707 48.702 1.00 61.44 C HETATM 4836 C3 OLA A 411 100.291 -29.604 47.986 1.00 66.14 C HETATM 4837 C4 OLA A 411 100.731 -28.953 46.675 1.00 60.76 C HETATM 4838 C5 OLA A 411 101.233 -30.027 45.712 1.00 51.33 C HETATM 4839 C6 OLA A 411 101.563 -29.377 44.367 1.00 59.47 C HETATM 4840 C7 OLA A 411 101.302 -30.366 43.232 1.00 67.75 C HETATM 4841 C8 OLA A 411 101.462 -29.659 41.885 1.00 58.32 C HETATM 4842 C9 OLA A 411 102.165 -30.591 40.936 1.00 71.92 C HETATM 4843 C10 OLA A 411 101.641 -30.885 39.772 1.00 61.74 C HETATM 4844 C11 OLA A 411 100.323 -30.293 39.352 1.00 56.93 C HETATM 4845 C12 OLA A 411 100.201 -30.396 37.832 1.00 62.90 C HETATM 4846 C13 OLA A 411 99.305 -29.266 37.330 1.00 52.88 C HETATM 4847 C14 OLA A 411 99.895 -28.674 36.051 1.00 51.60 C HETATM 4848 C15 OLA A 411 100.186 -29.797 35.057 1.00 56.38 C HETATM 4849 C16 OLA A 411 101.256 -29.326 34.071 1.00 53.00 C HETATM 4850 C1 OLA A 412 89.901 -29.782 45.917 1.00 68.03 C HETATM 4851 O1 OLA A 412 90.296 -30.826 46.480 1.00 69.59 O HETATM 4852 O2 OLA A 412 89.275 -28.911 46.565 1.00 49.69 O HETATM 4853 C2 OLA A 412 90.186 -29.585 44.453 1.00 68.32 C HETATM 4854 C3 OLA A 412 91.600 -30.092 44.152 1.00 54.29 C HETATM 4855 C4 OLA A 412 91.913 -29.898 42.667 1.00 57.82 C HETATM 4856 C5 OLA A 412 93.422 -29.948 42.432 1.00 43.73 C HETATM 4857 C6 OLA A 412 93.695 -29.794 40.935 1.00 62.65 C HETATM 4858 C7 OLA A 412 93.322 -28.380 40.487 1.00 54.65 C HETATM 4859 C8 OLA A 412 92.599 -28.441 39.140 1.00 49.49 C HETATM 4860 C9 OLA A 412 92.721 -27.116 38.436 1.00 59.79 C HETATM 4861 C10 OLA A 412 92.859 -27.083 37.134 1.00 59.06 C HETATM 4862 C11 OLA A 412 92.895 -28.366 36.344 1.00 56.28 C HETATM 4863 C12 OLA A 412 92.402 -28.099 34.922 1.00 59.89 C HETATM 4864 C13 OLA A 412 93.140 -29.000 33.930 1.00 48.97 C HETATM 4865 C14 OLA A 412 92.415 -28.958 32.582 1.00 56.47 C HETATM 4866 C15 OLA A 412 92.303 -30.374 32.014 1.00 81.44 C HETATM 4867 C16 OLA A 412 91.699 -30.333 30.608 1.00 78.08 C HETATM 4868 C17 OLA A 412 90.182 -30.141 30.693 1.00 69.22 C HETATM 4869 C18 OLA A 412 89.496 -31.480 30.960 1.00 38.53 C HETATM 4870 C3 OLA A 413 83.401 -23.130 43.055 1.00 55.61 C HETATM 4871 C4 OLA A 413 84.073 -22.990 41.690 1.00 48.23 C HETATM 4872 C5 OLA A 413 83.484 -24.027 40.734 1.00 62.95 C HETATM 4873 C6 OLA A 413 84.144 -23.898 39.361 1.00 51.73 C HETATM 4874 C7 OLA A 413 83.140 -24.289 38.276 1.00 50.76 C HETATM 4875 C8 OLA A 413 83.407 -23.468 37.013 1.00 40.95 C HETATM 4876 C9 OLA A 413 83.067 -24.284 35.794 1.00 43.03 C HETATM 4877 C10 OLA A 413 82.403 -23.729 34.810 1.00 47.50 C HETATM 4878 C11 OLA A 413 81.982 -22.286 34.907 1.00 51.29 C HETATM 4879 C12 OLA A 413 82.323 -21.559 33.606 1.00 38.82 C HETATM 4880 C13 OLA A 413 81.756 -22.339 32.419 1.00 54.45 C HETATM 4881 C14 OLA A 413 80.282 -21.979 32.220 1.00 44.40 C HETATM 4882 C15 OLA A 413 79.794 -22.515 30.873 1.00 40.12 C HETATM 4883 C1 OLA A 414 79.218 -21.024 38.717 1.00 60.16 C HETATM 4884 O1 OLA A 414 79.350 -22.268 38.696 1.00 74.22 O HETATM 4885 O2 OLA A 414 79.507 -20.380 39.751 1.00 43.54 O HETATM 4886 C2 OLA A 414 78.710 -20.310 37.490 1.00 40.55 C HETATM 4887 C3 OLA A 414 78.219 -21.334 36.461 1.00 37.74 C HETATM 4888 C4 OLA A 414 77.272 -20.656 35.467 1.00 56.80 C HETATM 4889 C5 OLA A 414 76.960 -21.593 34.299 1.00 39.99 C HETATM 4890 C6 OLA A 414 76.501 -20.761 33.098 1.00 48.65 C HETATM 4891 C7 OLA A 414 75.960 -21.687 32.009 1.00 60.97 C HETATM 4892 C8 OLA A 414 75.557 -20.864 30.784 1.00 50.99 C HETATM 4893 C9 OLA A 414 76.386 -21.299 29.604 1.00 54.60 C HETATM 4894 C10 OLA A 414 76.274 -20.671 28.460 1.00 59.14 C HETATM 4895 C11 OLA A 414 75.315 -19.517 28.328 1.00 63.82 C HETATM 4896 C12 OLA A 414 75.786 -18.575 27.220 1.00 63.55 C HETATM 4897 C13 OLA A 414 75.344 -17.146 27.537 1.00 58.14 C HETATM 4898 C14 OLA A 414 73.850 -16.992 27.250 1.00 67.61 C HETATM 4899 C2 OLA A 415 90.876 -31.783 16.684 1.00 43.08 C HETATM 4900 C3 OLA A 415 92.373 -31.520 16.855 1.00 71.79 C HETATM 4901 C4 OLA A 415 93.065 -31.547 15.492 1.00 66.26 C HETATM 4902 C5 OLA A 415 94.431 -30.869 15.588 1.00 64.04 C HETATM 4903 C6 OLA A 415 94.312 -29.606 16.442 1.00 69.08 C HETATM 4904 C7 OLA A 415 95.689 -29.164 16.942 1.00 58.90 C HETATM 4905 C8 OLA A 415 95.548 -28.541 18.333 1.00 62.55 C HETATM 4906 C9 OLA A 415 96.776 -27.736 18.666 1.00 65.45 C HETATM 4907 C10 OLA A 415 96.712 -26.824 19.603 1.00 57.64 C HETATM 4908 C11 OLA A 415 95.408 -26.601 20.323 1.00 52.62 C HETATM 4909 C12 OLA A 415 95.654 -26.415 21.821 1.00 41.74 C HETATM 4910 C13 OLA A 415 94.848 -27.450 22.609 1.00 36.99 C HETATM 4911 C14 OLA A 415 95.115 -27.273 24.107 1.00 46.93 C HETATM 4912 C15 OLA A 415 95.102 -28.631 24.809 1.00 43.00 C HETATM 4913 C16 OLA A 415 95.847 -28.523 26.142 1.00 45.18 C HETATM 4914 C1 OLA A 416 95.633 5.760 42.650 1.00 86.63 C HETATM 4915 O1 OLA A 416 96.325 5.410 43.632 1.00 67.95 O HETATM 4916 O2 OLA A 416 94.404 5.950 42.788 1.00 71.63 O HETATM 4917 C2 OLA A 416 96.276 5.968 41.302 1.00 70.22 C HETATM 4918 C3 OLA A 416 97.452 5.006 41.112 1.00 47.31 C HETATM 4919 C4 OLA A 416 98.265 5.428 39.888 1.00 54.12 C HETATM 4920 C5 OLA A 416 97.950 4.489 38.726 1.00 58.74 C HETATM 4921 C6 OLA A 416 97.940 5.282 37.420 1.00 54.01 C HETATM 4922 C7 OLA A 416 99.231 5.001 36.650 1.00 41.41 C HETATM 4923 C8 OLA A 416 98.912 4.828 35.164 1.00 43.92 C HETATM 4924 C9 OLA A 416 100.055 5.358 34.340 1.00 49.37 C HETATM 4925 C10 OLA A 416 100.432 4.752 33.240 1.00 45.72 C HETATM 4926 C11 OLA A 416 99.733 3.504 32.761 1.00 45.77 C HETATM 4927 C12 OLA A 416 100.475 2.928 31.552 1.00 39.81 C HETATM 4928 C13 OLA A 416 101.334 1.742 31.995 1.00 40.83 C HETATM 4929 C14 OLA A 416 102.436 1.477 30.966 1.00 42.98 C HETATM 4930 C15 OLA A 416 102.056 0.288 30.083 1.00 49.26 C HETATM 4931 C16 OLA A 416 102.867 -0.944 30.492 1.00 38.93 C HETATM 4932 C17 OLA A 416 103.780 -1.376 29.342 1.00 29.64 C HETATM 4933 C18 OLA A 416 104.820 -2.372 29.856 1.00 19.96 C HETATM 4934 C1 OLA A 417 85.850 -27.104 42.468 1.00 95.34 C HETATM 4935 O1 OLA A 417 84.978 -27.751 43.088 1.00 89.41 O HETATM 4936 O2 OLA A 417 86.155 -25.950 42.844 1.00 95.35 O HETATM 4937 C2 OLA A 417 86.538 -27.719 41.276 1.00 58.54 C HETATM 4938 C3 OLA A 417 86.695 -26.677 40.165 1.00 54.08 C HETATM 4939 C4 OLA A 417 87.445 -27.279 38.976 1.00 64.40 C HETATM 4940 C5 OLA A 417 87.393 -26.297 37.806 1.00 53.96 C HETATM 4941 C6 OLA A 417 87.672 -27.042 36.500 1.00 56.72 C HETATM 4942 C7 OLA A 417 86.463 -26.931 35.572 1.00 62.81 C HETATM 4943 C8 OLA A 417 86.834 -27.509 34.205 1.00 59.05 C HETATM 4944 C9 OLA A 417 86.741 -26.436 33.152 1.00 67.51 C HETATM 4945 C10 OLA A 417 87.830 -25.935 32.622 1.00 70.09 C HETATM 4946 C11 OLA A 417 89.185 -26.425 33.064 1.00 80.07 C HETATM 4947 C12 OLA A 417 90.266 -25.919 32.109 1.00 55.76 C HETATM 4948 C13 OLA A 417 90.841 -24.602 32.629 1.00 50.60 C HETATM 4949 C14 OLA A 417 91.019 -24.672 34.146 1.00 37.91 C HETATM 4950 C15 OLA A 417 92.228 -23.831 34.553 1.00 47.29 C HETATM 4951 C16 OLA A 417 92.285 -23.732 36.078 1.00 43.66 C HETATM 4952 C17 OLA A 417 90.938 -23.223 36.593 1.00 50.64 C HETATM 4953 C18 OLA A 417 90.526 -24.016 37.833 1.00 49.00 C HETATM 4954 C1 OLA A 418 94.357 10.891 43.324 1.00 92.89 C HETATM 4955 O1 OLA A 418 94.651 11.962 43.900 1.00 91.42 O HETATM 4956 O2 OLA A 418 94.490 9.803 43.926 1.00 99.07 O HETATM 4957 C2 OLA A 418 93.841 10.907 41.908 1.00 71.52 C HETATM 4958 C3 OLA A 418 94.212 9.593 41.216 1.00 68.27 C HETATM 4959 C4 OLA A 418 94.059 9.741 39.701 1.00 56.93 C HETATM 4960 C5 OLA A 418 95.327 9.249 39.004 1.00 61.71 C HETATM 4961 C6 OLA A 418 95.096 9.195 37.492 1.00 65.31 C HETATM 4962 C7 OLA A 418 96.320 8.581 36.811 1.00 66.56 C HETATM 4963 C8 OLA A 418 96.169 8.657 35.289 1.00 61.56 C HETATM 4964 C9 OLA A 418 97.529 8.560 34.648 1.00 52.35 C HETATM 4965 C15 9P2 B 401 109.075 -2.215 31.845 1.00 29.90 C HETATM 4966 C16 9P2 B 401 109.120 -0.932 31.302 1.00 26.88 C HETATM 4967 C17 9P2 B 401 108.105 -0.071 31.509 1.00 35.42 C HETATM 4968 C18 9P2 B 401 106.924 -0.482 32.323 1.00 22.54 C HETATM 4969 C20 9P2 B 401 109.858 1.073 30.565 1.00 37.62 C HETATM 4970 C01 9P2 B 401 108.969 0.479 35.240 1.00 25.61 C HETATM 4971 N02 9P2 B 401 107.856 1.347 35.154 1.00 35.85 N HETATM 4972 C03 9P2 B 401 106.729 0.668 35.439 1.00 27.63 C HETATM 4973 C04 9P2 B 401 107.127 -0.676 35.724 1.00 23.58 C HETATM 4974 N05 9P2 B 401 108.515 -0.746 35.569 1.00 25.97 N HETATM 4975 C06 9P2 B 401 109.289 -1.908 35.773 1.00 33.85 C HETATM 4976 C07 9P2 B 401 109.435 -2.143 37.284 1.00 30.37 C HETATM 4977 C08 9P2 B 401 110.769 -2.830 37.699 1.00 24.31 C HETATM 4978 C09 9P2 B 401 110.795 -3.161 39.229 1.00 18.46 C HETATM 4979 C10 9P2 B 401 106.189 -1.896 36.083 1.00 30.82 C HETATM 4980 N11 9P2 B 401 106.284 -2.827 34.973 1.00 19.86 N HETATM 4981 C12 9P2 B 401 105.707 -2.246 33.718 1.00 33.06 C HETATM 4982 C13 9P2 B 401 106.879 -1.771 32.859 1.00 26.70 C HETATM 4983 C14 9P2 B 401 107.913 -2.627 32.653 1.00 41.50 C HETATM 4984 O19 9P2 B 401 108.427 1.162 30.835 1.00 39.19 O HETATM 4985 O21 9P2 B 401 110.133 -0.311 30.496 1.00 20.51 O HETATM 4986 C22 9P2 B 401 105.703 -4.104 35.305 1.00 23.23 C HETATM 4987 C23 9P2 B 401 106.702 -4.896 36.221 1.00 33.17 C HETATM 4988 C24 9P2 B 401 107.917 -5.294 35.732 1.00 26.68 C HETATM 4989 C25 9P2 B 401 108.864 -6.046 36.619 1.00 35.42 C HETATM 4990 O26 9P2 B 401 110.107 -6.555 36.400 1.00 30.02 O HETATM 4991 C27 9P2 B 401 110.622 -6.874 37.673 1.00 31.24 C HETATM 4992 O28 9P2 B 401 109.541 -7.019 38.510 1.00 38.85 O HETATM 4993 C29 9P2 B 401 108.512 -6.332 37.925 1.00 26.42 C HETATM 4994 C30 9P2 B 401 107.238 -5.910 38.436 1.00 30.65 C HETATM 4995 C31 9P2 B 401 106.333 -5.192 37.589 1.00 28.83 C HETATM 4996 C32 9P2 B 401 105.468 1.204 35.456 1.00 24.27 C HETATM 4997 C33 9P2 B 401 105.030 1.979 34.381 1.00 28.60 C HETATM 4998 C34 9P2 B 401 103.729 2.550 34.388 1.00 25.90 C HETATM 4999 C35 9P2 B 401 102.877 2.344 35.479 1.00 25.17 C HETATM 5000 C36 9P2 B 401 103.321 1.563 36.580 1.00 27.67 C HETATM 5001 C37 9P2 B 401 104.600 1.005 36.573 1.00 28.92 C HETATM 5002 C38 9P2 B 401 110.353 0.892 34.968 1.00 29.42 C HETATM 5003 C39 9P2 B 401 110.925 1.972 35.656 1.00 28.07 C HETATM 5004 C40 9P2 B 401 112.225 2.369 35.378 1.00 32.43 C HETATM 5005 C41 9P2 B 401 112.956 1.719 34.420 1.00 19.71 C HETATM 5006 C42 9P2 B 401 112.382 0.640 33.717 1.00 17.78 C HETATM 5007 C43 9P2 B 401 111.076 0.252 33.999 1.00 21.62 C HETATM 5008 O1 TLA B 402 120.124 -13.052 53.505 1.00 68.27 O HETATM 5009 O11 TLA B 402 121.323 -13.095 55.302 1.00 61.92 O HETATM 5010 C1 TLA B 402 120.931 -12.500 54.277 1.00 61.24 C HETATM 5011 C2 TLA B 402 121.455 -11.125 53.947 1.00 59.45 C HETATM 5012 O2 TLA B 402 122.695 -10.722 54.518 1.00 81.26 O HETATM 5013 C3 TLA B 402 120.707 -10.166 53.009 1.00 51.22 C HETATM 5014 O3 TLA B 402 119.284 -10.032 53.025 1.00 67.54 O HETATM 5015 C4 TLA B 402 121.481 -9.376 51.995 1.00 42.36 C HETATM 5016 O4 TLA B 402 121.575 -9.834 50.840 1.00 40.17 O HETATM 5017 O41 TLA B 402 122.014 -8.291 52.308 1.00 43.87 O HETATM 5018 C1 OLA B 403 110.133 6.764 42.032 1.00 70.41 C HETATM 5019 O1 OLA B 403 109.759 7.009 40.862 1.00 49.93 O HETATM 5020 O2 OLA B 403 109.626 7.372 43.001 1.00 65.35 O HETATM 5021 C2 OLA B 403 111.205 5.736 42.281 1.00 57.72 C HETATM 5022 C3 OLA B 403 110.887 4.957 43.561 1.00 62.10 C HETATM 5023 C4 OLA B 403 111.050 3.455 43.321 1.00 55.89 C HETATM 5024 C5 OLA B 403 110.760 2.698 44.616 1.00 53.24 C HETATM 5025 C6 OLA B 403 109.323 2.179 44.595 1.00 60.60 C HETATM 5026 C7 OLA B 403 108.386 3.269 45.112 1.00 65.72 C HETATM 5027 C8 OLA B 403 108.123 3.067 46.604 1.00 41.94 C HETATM 5028 C9 OLA B 403 107.349 4.252 47.119 1.00 57.32 C HETATM 5029 C10 OLA B 403 106.868 4.259 48.336 1.00 49.03 C HETATM 5030 C11 OLA B 403 107.085 3.077 49.243 1.00 54.35 C HETATM 5031 C1 OLA B 404 104.586 4.710 38.615 1.00 64.10 C HETATM 5032 O1 OLA B 404 103.758 5.403 37.982 1.00 68.89 O HETATM 5033 O2 OLA B 404 104.281 4.234 39.731 1.00 79.42 O HETATM 5034 C2 OLA B 404 105.952 4.453 38.033 1.00 50.26 C HETATM 5035 C3 OLA B 404 106.661 3.344 38.814 1.00 54.41 C HETATM 5036 C4 OLA B 404 108.116 3.247 38.354 1.00 40.71 C HETATM 5037 C5 OLA B 404 108.903 2.360 39.316 1.00 33.91 C HETATM 5038 C6 OLA B 404 110.392 2.510 39.008 1.00 41.21 C HETATM 5039 C7 OLA B 404 111.220 1.873 40.123 1.00 41.95 C HETATM 5040 C8 OLA B 404 112.556 2.611 40.224 1.00 41.27 C HETATM 5041 C1 OLA B 405 111.171 -18.871 44.570 1.00 78.98 C HETATM 5042 O1 OLA B 405 112.347 -18.826 44.993 1.00 75.32 O HETATM 5043 O2 OLA B 405 110.219 -19.037 45.365 1.00 85.43 O HETATM 5044 C2 OLA B 405 110.914 -18.724 43.094 1.00 61.38 C HETATM 5045 C3 OLA B 405 112.238 -18.869 42.340 1.00 57.94 C HETATM 5046 C4 OLA B 405 111.981 -18.826 40.833 1.00 49.59 C HETATM 5047 C5 OLA B 405 113.296 -19.019 40.079 1.00 57.63 C HETATM 5048 C6 OLA B 405 113.246 -18.262 38.749 1.00 60.16 C HETATM 5049 C7 OLA B 405 114.669 -18.072 38.220 1.00 57.44 C HETATM 5050 C8 OLA B 405 114.643 -17.324 36.885 1.00 41.93 C HETATM 5051 C9 OLA B 405 114.886 -18.298 35.761 1.00 66.17 C HETATM 5052 C10 OLA B 405 114.406 -18.067 34.563 1.00 72.63 C HETATM 5053 C11 OLA B 405 113.603 -16.823 34.281 1.00 46.64 C HETATM 5054 C12 OLA B 405 112.472 -17.143 33.302 1.00 40.86 C HETATM 5055 C13 OLA B 405 112.940 -16.881 31.869 1.00 40.35 C HETATM 5056 C1 OLA B 406 101.103 8.534 39.132 1.00 80.91 C HETATM 5057 O1 OLA B 406 101.903 7.574 39.178 1.00 69.59 O HETATM 5058 O2 OLA B 406 100.537 8.930 40.176 1.00 84.58 O HETATM 5059 C2 OLA B 406 100.821 9.208 37.816 1.00 82.17 C HETATM 5060 C3 OLA B 406 101.982 8.949 36.853 1.00 79.07 C HETATM 5061 C4 OLA B 406 101.442 8.469 35.504 1.00 67.12 C HETATM 5062 C5 OLA B 406 102.535 8.600 34.444 1.00 66.89 C HETATM 5063 C6 OLA B 406 102.276 7.616 33.301 1.00 55.21 C HETATM 5064 C7 OLA B 406 103.465 7.650 32.338 1.00 53.61 C HETATM 5065 C8 OLA B 406 103.656 6.291 31.658 1.00 42.67 C HETATM 5066 C9 OLA B 406 104.687 6.445 30.571 1.00 42.09 C HETATM 5067 C10 OLA B 406 105.295 5.401 30.064 1.00 47.93 C HETATM 5068 C11 OLA B 406 104.974 4.014 30.556 1.00 46.71 C HETATM 5069 C12 OLA B 406 104.668 3.120 29.354 1.00 58.15 C HETATM 5070 C1 OLA B 407 113.566 -5.705 46.072 1.00 52.10 C HETATM 5071 O1 OLA B 407 114.077 -5.934 44.954 1.00 64.62 O HETATM 5072 O2 OLA B 407 113.905 -6.379 47.071 1.00 50.03 O HETATM 5073 C2 OLA B 407 112.542 -4.611 46.213 1.00 33.94 C HETATM 5074 C3 OLA B 407 111.766 -4.473 44.902 1.00 35.67 C HETATM 5075 C4 OLA B 407 110.665 -3.427 45.072 1.00 37.67 C HETATM 5076 C5 OLA B 407 109.512 -3.749 44.122 1.00 32.93 C HETATM 5077 C6 OLA B 407 108.921 -2.448 43.577 1.00 34.98 C HETATM 5078 C7 OLA B 407 107.460 -2.678 43.186 1.00 62.08 C HETATM 5079 C8 OLA B 407 107.379 -3.180 41.741 1.00 57.98 C HETATM 5080 C9 OLA B 407 105.945 -3.440 41.360 1.00 47.51 C HETATM 5081 C10 OLA B 407 105.322 -2.631 40.537 1.00 51.79 C HETATM 5082 C11 OLA B 407 106.030 -1.429 39.965 1.00 36.97 C HETATM 5083 C1 OLA B 408 111.418 -5.188 50.386 1.00 52.43 C HETATM 5084 O1 OLA B 408 112.619 -5.517 50.261 1.00 47.58 O HETATM 5085 O2 OLA B 408 111.106 -4.134 50.986 1.00 38.92 O HETATM 5086 C2 OLA B 408 110.340 -6.067 49.814 1.00 44.22 C HETATM 5087 C3 OLA B 408 109.163 -5.200 49.372 1.00 32.40 C HETATM 5088 C4 OLA B 408 108.020 -6.101 48.908 1.00 29.83 C HETATM 5089 C5 OLA B 408 107.087 -5.296 48.005 1.00 27.76 C HETATM 5090 C1 OLA B 409 111.292 -18.201 13.738 1.00 97.50 C HETATM 5091 O1 OLA B 409 110.997 -18.031 12.534 1.00 95.82 O HETATM 5092 O2 OLA B 409 111.790 -19.283 14.122 1.00103.88 O HETATM 5093 C2 OLA B 409 111.041 -17.104 14.739 1.00 59.77 C HETATM 5094 C3 OLA B 409 112.134 -17.134 15.811 1.00 63.57 C HETATM 5095 C4 OLA B 409 111.828 -16.112 16.908 1.00 69.43 C HETATM 5096 C5 OLA B 409 110.636 -16.596 17.733 1.00 69.82 C HETATM 5097 C6 OLA B 409 110.207 -15.526 18.738 1.00 58.38 C HETATM 5098 C7 OLA B 409 110.754 -15.865 20.124 1.00 54.08 C HETATM 5099 C8 OLA B 409 112.212 -15.411 20.216 1.00 63.44 C HETATM 5100 C9 OLA B 409 112.269 -13.941 20.541 1.00 59.71 C HETATM 5101 C10 OLA B 409 113.230 -13.472 21.298 1.00 53.63 C HETATM 5102 C11 OLA B 409 114.278 -14.405 21.848 1.00 60.25 C HETATM 5103 C12 OLA B 409 115.668 -13.940 21.415 1.00 38.96 C HETATM 5104 C13 OLA B 409 116.664 -15.086 21.589 1.00 51.04 C HETATM 5105 C14 OLA B 409 116.415 -15.789 22.925 1.00 46.80 C HETATM 5106 C1 OLA B 410 116.731 -19.593 45.995 1.00 77.33 C HETATM 5107 O1 OLA B 410 115.975 -19.247 46.930 1.00 80.14 O HETATM 5108 O2 OLA B 410 117.755 -18.923 45.737 1.00 68.56 O HETATM 5109 C2 OLA B 410 116.414 -20.821 45.184 1.00 69.54 C HETATM 5110 C3 OLA B 410 116.032 -20.417 43.758 1.00 65.59 C HETATM 5111 C4 OLA B 410 117.278 -20.375 42.871 1.00 55.86 C HETATM 5112 C5 OLA B 410 116.836 -20.288 41.411 1.00 51.18 C HETATM 5113 C6 OLA B 410 118.051 -20.077 40.508 1.00 53.68 C HETATM 5114 C7 OLA B 410 117.728 -20.588 39.104 1.00 54.45 C HETATM 5115 C8 OLA B 410 118.246 -19.599 38.057 1.00 62.93 C HETATM 5116 C9 OLA B 410 119.752 -19.562 38.083 1.00 71.30 C HETATM 5117 C10 OLA B 410 120.434 -19.350 36.984 1.00 65.11 C HETATM 5118 C11 OLA B 410 119.719 -19.142 35.674 1.00 72.02 C HETATM 5119 C12 OLA B 410 119.876 -17.688 35.225 1.00 70.60 C HETATM 5120 C13 OLA B 410 118.504 -17.077 34.932 1.00 71.20 C HETATM 5121 C14 OLA B 410 118.618 -16.088 33.769 1.00 53.56 C HETATM 5122 C15 OLA B 410 118.549 -16.846 32.442 1.00 52.65 C HETATM 5123 C16 OLA B 410 117.668 -16.081 31.451 1.00 40.58 C HETATM 5124 C17 OLA B 410 117.954 -16.567 30.028 1.00 37.42 C HETATM 5125 C18 OLA B 410 116.866 -16.055 29.083 1.00 49.52 C HETATM 5126 C1 OLA B 411 109.090 -23.633 46.362 1.00 89.67 C HETATM 5127 O1 OLA B 411 108.450 -24.674 46.098 1.00 91.28 O HETATM 5128 O2 OLA B 411 109.379 -23.362 47.548 1.00 84.89 O HETATM 5129 C2 OLA B 411 109.514 -22.706 45.253 1.00 74.82 C HETATM 5130 C3 OLA B 411 109.235 -23.355 43.894 1.00 73.01 C HETATM 5131 C4 OLA B 411 110.404 -23.090 42.946 1.00 68.69 C HETATM 5132 C5 OLA B 411 109.900 -23.066 41.504 1.00 71.71 C HETATM 5133 C6 OLA B 411 110.822 -23.916 40.631 1.00 81.52 C HETATM 5134 C7 OLA B 411 111.881 -23.024 39.986 1.00 77.54 C HETATM 5135 C8 OLA B 411 113.144 -22.987 40.850 1.00 76.76 C HETATM 5136 C9 OLA B 411 113.884 -24.297 40.776 1.00 73.55 C HETATM 5137 C10 OLA B 411 114.462 -24.691 39.666 1.00 66.54 C HETATM 5138 C11 OLA B 411 114.392 -23.846 38.418 1.00 64.89 C HETATM 5139 C12 OLA B 411 115.746 -23.842 37.710 1.00 63.29 C HETATM 5140 C1 OLA B 412 113.654 16.142 47.559 1.00 93.66 C HETATM 5141 O1 OLA B 412 114.225 15.033 47.459 1.00 98.71 O HETATM 5142 O2 OLA B 412 113.667 16.755 48.651 1.00 87.82 O HETATM 5143 C2 OLA B 412 112.952 16.733 46.363 1.00 70.28 C HETATM 5144 C3 OLA B 412 113.102 15.800 45.155 1.00 60.44 C HETATM 5145 C4 OLA B 412 113.085 16.613 43.857 1.00 74.37 C HETATM 5146 C5 OLA B 412 112.774 15.707 42.663 1.00 66.59 C HETATM 5147 C6 OLA B 412 113.330 16.325 41.376 1.00 71.18 C HETATM 5148 C7 OLA B 412 113.186 15.322 40.229 1.00 69.35 C HETATM 5149 C8 OLA B 412 113.617 15.937 38.893 1.00 52.80 C HETATM 5150 C9 OLA B 412 114.512 14.948 38.194 1.00 56.50 C HETATM 5151 C10 OLA B 412 114.550 14.843 36.887 1.00 66.54 C HETATM 5152 C11 OLA B 412 113.704 15.705 35.988 1.00 58.35 C HETATM 5153 C12 OLA B 412 114.239 15.614 34.555 1.00 63.10 C HETATM 5154 C13 OLA B 412 114.118 14.181 34.032 1.00 63.90 C HETATM 5155 C14 OLA B 412 115.221 13.894 33.007 1.00 58.56 C HETATM 5156 C15 OLA B 412 114.764 14.303 31.604 1.00 52.42 C HETATM 5157 C16 OLA B 412 114.050 13.135 30.918 1.00 51.33 C HETATM 5158 C17 OLA B 412 112.537 13.366 30.953 1.00 68.86 C HETATM 5159 C18 OLA B 412 111.888 12.758 29.708 1.00 38.53 C HETATM 5160 C1 OLA B 413 124.157 17.767 46.625 1.00 64.72 C HETATM 5161 O1 OLA B 413 124.899 18.055 45.660 1.00 82.85 O HETATM 5162 O2 OLA B 413 124.030 18.564 47.582 1.00 52.52 O HETATM 5163 C2 OLA B 413 123.418 16.455 46.631 1.00 50.37 C HETATM 5164 C3 OLA B 413 123.646 15.732 45.301 1.00 40.41 C HETATM 5165 C4 OLA B 413 122.317 15.175 44.789 1.00 51.00 C HETATM 5166 C5 OLA B 413 122.351 15.073 43.264 1.00 57.98 C HETATM 5167 C6 OLA B 413 120.989 14.620 42.738 1.00 39.38 C HETATM 5168 C7 OLA B 413 121.065 14.467 41.219 1.00 48.37 C HETATM 5169 C8 OLA B 413 121.421 13.025 40.848 1.00 52.90 C HETATM 5170 C9 OLA B 413 120.653 12.628 39.614 1.00 54.73 C HETATM 5171 C10 OLA B 413 121.095 11.680 38.824 1.00 40.71 C HETATM 5172 C11 OLA B 413 122.386 10.971 39.141 1.00 55.86 C HETATM 5173 C12 OLA B 413 122.526 9.727 38.262 1.00 39.56 C HETATM 5174 C10 OLA B 414 115.084 13.174 19.612 1.00 54.44 C HETATM 5175 C11 OLA B 414 114.490 12.387 20.751 1.00 52.21 C HETATM 5176 C12 OLA B 414 115.600 11.666 21.523 1.00 57.69 C HETATM 5177 C13 OLA B 414 115.643 12.189 22.960 1.00 50.27 C HETATM 5178 C14 OLA B 414 116.878 11.631 23.669 1.00 48.15 C HETATM 5179 C15 OLA B 414 117.392 12.639 24.698 1.00 64.02 C HETATM 5180 C16 OLA B 414 116.389 12.761 25.846 1.00 56.65 C HETATM 5181 C17 OLA B 414 116.911 13.768 26.874 1.00 46.61 C HETATM 5182 C18 OLA B 414 115.953 13.823 28.065 1.00 58.23 C HETATM 5183 C1 OLA B 415 128.293 8.386 43.137 1.00 73.68 C HETATM 5184 O1 OLA B 415 127.452 9.210 42.715 1.00 74.30 O HETATM 5185 O2 OLA B 415 128.542 8.325 44.362 1.00 70.65 O HETATM 5186 C2 OLA B 415 128.999 7.472 42.169 1.00 57.37 C HETATM 5187 C3 OLA B 415 128.807 7.989 40.740 1.00 63.37 C HETATM 5188 C4 OLA B 415 129.725 7.227 39.780 1.00 60.74 C HETATM 5189 C5 OLA B 415 129.915 8.023 38.487 1.00 61.16 C HETATM 5190 C6 OLA B 415 130.268 7.071 37.341 1.00 59.84 C HETATM 5191 C7 OLA B 415 130.246 7.828 36.011 1.00 43.64 C HETATM 5192 C8 OLA B 415 129.774 6.896 34.890 1.00 33.03 C HETATM 5193 C9 OLA B 415 130.659 5.679 34.857 1.00 52.95 C HETATM 5194 C10 OLA B 415 130.967 5.095 33.723 1.00 50.86 C HETATM 5195 C11 OLA B 415 130.436 5.627 32.418 1.00 51.79 C HETATM 5196 C12 OLA B 415 131.550 5.676 31.371 1.00 55.63 C HETATM 5197 C13 OLA B 415 131.251 6.822 30.402 1.00 64.51 C HETATM 5198 C14 OLA B 415 132.257 6.829 29.248 1.00 64.24 C HETATM 5199 C15 OLA B 415 131.957 8.015 28.328 1.00 55.01 C HETATM 5200 C16 OLA B 415 132.374 7.679 26.894 1.00 58.50 C HETATM 5201 C17 OLA B 415 131.745 8.676 25.917 1.00 56.29 C HETATM 5202 C18 OLA B 415 132.818 9.240 24.984 1.00 51.21 C HETATM 5203 C1 OLA B 416 133.282 3.851 42.272 1.00 77.71 C HETATM 5204 O1 OLA B 416 132.162 3.519 42.718 1.00 69.40 O HETATM 5205 O2 OLA B 416 133.989 4.666 42.906 1.00 62.74 O HETATM 5206 C2 OLA B 416 133.788 3.250 40.986 1.00 60.59 C HETATM 5207 C3 OLA B 416 133.251 3.985 39.754 1.00 44.67 C HETATM 5208 C4 OLA B 416 133.779 3.270 38.506 1.00 58.67 C HETATM 5209 C5 OLA B 416 133.787 4.212 37.302 1.00 56.41 C HETATM 5210 C6 OLA B 416 134.330 3.479 36.072 1.00 50.56 C HETATM 5211 C7 OLA B 416 134.590 4.486 34.950 1.00 40.11 C HETATM 5212 C8 OLA B 416 135.255 3.798 33.752 1.00 55.42 C HETATM 5213 C9 OLA B 416 135.726 4.852 32.782 1.00 82.10 C HETATM 5214 C10 OLA B 416 136.180 4.566 31.583 1.00 79.92 C HETATM 5215 C11 OLA B 416 136.270 3.152 31.069 1.00 60.42 C HETATM 5216 C12 OLA B 416 135.645 3.061 29.674 1.00 55.47 C HETATM 5217 C13 OLA B 416 135.850 4.364 28.897 1.00 68.51 C HETATM 5218 C14 OLA B 416 134.807 4.449 27.779 1.00 61.07 C HETATM 5219 C15 OLA B 416 135.206 5.512 26.753 1.00 65.90 C HETATM 5220 C16 OLA B 416 134.199 5.514 25.600 1.00 56.88 C HETATM 5221 C17 OLA B 416 134.895 5.054 24.320 1.00 67.00 C HETATM 5222 C18 OLA B 416 135.455 3.650 24.545 1.00 55.30 C HETATM 5223 C1 OLA B 417 122.162 -20.496 42.027 1.00 73.30 C HETATM 5224 O1 OLA B 417 122.984 -21.337 42.453 1.00 80.75 O HETATM 5225 O2 OLA B 417 121.480 -19.824 42.832 1.00 74.98 O HETATM 5226 C2 OLA B 417 121.990 -20.293 40.545 1.00 63.96 C HETATM 5227 C3 OLA B 417 123.304 -20.589 39.821 1.00 55.57 C HETATM 5228 C4 OLA B 417 123.022 -20.761 38.328 1.00 45.26 C HETATM 5229 C5 OLA B 417 124.323 -20.617 37.540 1.00 55.68 C HETATM 5230 C6 OLA B 417 124.015 -20.056 36.152 1.00 54.76 C HETATM 5231 C7 OLA B 417 125.088 -20.525 35.168 1.00 46.76 C HETATM 5232 C8 OLA B 417 124.557 -20.405 33.738 1.00 60.69 C HETATM 5233 C9 OLA B 417 123.950 -19.042 33.539 1.00 60.09 C HETATM 5234 C10 OLA B 417 123.048 -18.842 32.606 1.00 70.32 C HETATM 5235 C11 OLA B 417 122.603 -19.975 31.715 1.00 67.03 C HETATM 5236 C12 OLA B 417 121.278 -19.631 31.030 1.00 60.89 C HETATM 5237 C13 OLA B 417 120.271 -20.761 31.247 1.00 72.44 C HETATM 5238 C14 OLA B 417 120.240 -21.158 32.724 1.00 46.87 C HETATM 5239 C1 OLA B 418 140.070 -5.783 11.481 1.00 87.53 C HETATM 5240 O1 OLA B 418 139.467 -6.618 10.773 1.00 81.45 O HETATM 5241 O2 OLA B 418 140.066 -4.574 11.161 1.00 94.39 O HETATM 5242 C2 OLA B 418 140.811 -6.239 12.712 1.00 62.83 C HETATM 5243 C3 OLA B 418 140.390 -5.413 13.930 1.00 40.61 C HETATM 5244 C4 OLA B 418 140.684 -6.220 15.195 1.00 52.08 C HETATM 5245 C5 OLA B 418 141.065 -5.275 16.334 1.00 46.96 C HETATM 5246 C6 OLA B 418 141.894 -6.030 17.374 1.00 55.05 C HETATM 5247 C7 OLA B 418 141.565 -5.505 18.772 1.00 46.13 C HETATM 5248 C8 OLA B 418 142.236 -4.145 18.978 1.00 63.19 C HETATM 5249 C9 OLA B 418 142.780 -4.035 20.378 1.00 62.94 C HETATM 5250 C10 OLA B 418 143.149 -2.871 20.855 1.00 64.84 C HETATM 5251 C11 OLA B 418 143.041 -1.622 20.018 1.00 58.06 C HETATM 5252 C12 OLA B 418 142.416 -0.493 20.840 1.00 60.04 C HETATM 5253 C13 OLA B 418 143.230 -0.262 22.114 1.00 52.23 C HETATM 5254 C5 OLA B 419 104.419 -4.195 16.619 1.00 45.50 C HETATM 5255 C6 OLA B 419 104.499 -2.936 17.482 1.00 51.32 C HETATM 5256 C7 OLA B 419 105.908 -2.815 18.061 1.00 51.86 C HETATM 5257 C8 OLA B 419 106.088 -3.859 19.163 1.00 59.50 C HETATM 5258 C9 OLA B 419 105.594 -3.280 20.460 1.00 65.87 C HETATM 5259 C10 OLA B 419 105.024 -4.040 21.358 1.00 61.28 C HETATM 5260 C11 OLA B 419 104.837 -5.517 21.143 1.00 51.19 C HETATM 5261 C12 OLA B 419 105.068 -6.238 22.471 1.00 35.39 C HETATM 5262 C13 OLA B 419 105.493 -7.681 22.204 1.00 46.38 C HETATM 5263 C14 OLA B 419 104.256 -8.514 21.867 1.00 32.90 C HETATM 5264 C15 OLA B 419 104.633 -9.679 20.953 1.00 45.51 C HETATM 5265 C16 OLA B 419 104.221 -9.342 19.519 1.00 44.23 C HETATM 5266 C17 OLA B 419 103.833 -10.625 18.780 1.00 47.52 C HETATM 5267 C18 OLA B 419 103.447 -10.283 17.340 1.00 45.13 C HETATM 5268 C1 CIT B 420 117.948 -14.587 -10.714 1.00 86.84 C HETATM 5269 O1 CIT B 420 117.611 -13.827 -11.635 1.00 92.72 O HETATM 5270 O2 CIT B 420 119.006 -14.455 -10.086 1.00 83.98 O HETATM 5271 C2 CIT B 420 117.038 -15.736 -10.362 1.00 86.93 C HETATM 5272 C3 CIT B 420 116.007 -15.362 -9.312 1.00102.85 C HETATM 5273 O7 CIT B 420 115.736 -13.965 -9.382 1.00118.13 O HETATM 5274 C4 CIT B 420 114.692 -16.097 -9.546 1.00102.27 C HETATM 5275 C5 CIT B 420 113.485 -15.379 -8.984 1.00100.43 C HETATM 5276 O3 CIT B 420 112.490 -15.228 -9.719 1.00 95.01 O HETATM 5277 O4 CIT B 420 113.512 -14.982 -7.808 1.00 82.80 O HETATM 5278 C6 CIT B 420 116.592 -15.731 -7.980 1.00102.50 C HETATM 5279 O5 CIT B 420 117.786 -15.464 -7.764 1.00 89.94 O HETATM 5280 O6 CIT B 420 115.878 -16.296 -7.132 1.00 96.11 O HETATM 5281 O HOH A 501 97.695 -17.187 10.445 1.00 38.46 O HETATM 5282 O HOH A 502 85.245 -14.615 30.939 1.00 37.39 O HETATM 5283 O HOH A 503 84.961 -10.412 46.259 1.00 29.86 O HETATM 5284 O HOH A 504 85.719 -19.500 20.169 1.00 38.74 O HETATM 5285 O HOH A 505 112.588 -16.899 2.359 1.00 68.36 O HETATM 5286 O HOH A 506 87.234 0.223 -7.524 1.00 58.32 O HETATM 5287 O HOH A 507 81.092 -19.658 50.574 1.00 57.91 O HETATM 5288 O HOH A 508 92.745 -17.351 24.452 1.00 24.70 O HETATM 5289 O HOH A 509 89.317 -28.602 54.840 1.00 31.82 O HETATM 5290 O HOH A 510 98.248 -1.876 52.877 1.00 37.82 O HETATM 5291 O HOH A 511 87.094 -24.677 46.348 1.00 53.57 O HETATM 5292 O HOH A 512 87.919 3.599 4.565 1.00 61.70 O HETATM 5293 O HOH A 513 82.769 -20.640 57.069 1.00 52.79 O HETATM 5294 O HOH A 514 86.752 -16.630 60.780 1.00 19.96 O HETATM 5295 O HOH A 515 95.037 -13.831 53.984 1.00 41.65 O HETATM 5296 O HOH A 516 93.842 -5.080 0.759 1.00 46.99 O HETATM 5297 O HOH A 517 96.076 -22.899 57.735 1.00 26.64 O HETATM 5298 O HOH A 518 101.242 -20.463 54.012 1.00 36.47 O HETATM 5299 O HOH A 519 103.341 -15.062 55.042 1.00 29.32 O HETATM 5300 O HOH A 520 87.978 -2.093 -10.448 1.00 55.29 O HETATM 5301 O HOH A 521 86.476 -9.686 10.725 1.00 54.79 O HETATM 5302 O HOH A 522 83.257 5.977 48.462 1.00 56.77 O HETATM 5303 O HOH A 523 86.807 -10.596 13.731 1.00 47.84 O HETATM 5304 O HOH A 524 103.336 -22.548 53.472 1.00 45.39 O HETATM 5305 O HOH A 525 77.992 -12.797 54.129 1.00 51.52 O HETATM 5306 O HOH A 526 74.056 -0.197 6.412 1.00 42.31 O HETATM 5307 O HOH A 527 83.905 -28.577 3.394 1.00 38.34 O HETATM 5308 O HOH A 528 107.466 -13.452 48.489 1.00 38.82 O HETATM 5309 O HOH A 529 91.121 -6.705 -6.247 1.00 56.41 O HETATM 5310 O HOH A 530 80.644 -7.532 50.975 1.00 50.37 O HETATM 5311 O HOH A 531 97.938 -30.119 8.542 1.00 56.11 O HETATM 5312 O HOH A 532 88.817 -14.282 9.432 1.00 49.17 O HETATM 5313 O HOH A 533 94.702 -14.949 18.085 1.00 55.51 O HETATM 5314 O HOH A 534 97.371 -28.803 54.833 1.00 43.47 O HETATM 5315 O HOH A 535 107.009 -0.091 59.140 1.00 41.53 O HETATM 5316 O HOH A 536 84.270 -15.278 6.061 1.00 44.67 O HETATM 5317 O HOH A 537 84.310 7.259 45.688 1.00 39.22 O HETATM 5318 O HOH A 538 107.716 -12.912 51.776 1.00 63.03 O HETATM 5319 O HOH A 539 107.848 -25.928 51.756 1.00 54.20 O HETATM 5320 O HOH B 501 102.081 3.876 13.544 1.00 77.31 O HETATM 5321 O HOH B 502 120.734 -1.879 54.516 1.00 28.05 O HETATM 5322 O HOH B 503 125.761 10.454 54.624 1.00 26.94 O HETATM 5323 O HOH B 504 124.682 3.456 20.510 1.00 38.24 O HETATM 5324 O HOH B 505 127.039 -7.634 36.454 1.00 22.28 O HETATM 5325 O HOH B 506 114.498 1.784 17.038 1.00 58.50 O HETATM 5326 O HOH B 507 122.218 -8.667 19.338 1.00 36.08 O HETATM 5327 O HOH B 508 122.422 -7.703 6.484 1.00 47.22 O HETATM 5328 O HOH B 509 104.964 5.505 53.439 1.00 52.23 O HETATM 5329 O HOH B 510 125.814 -0.700 31.301 1.00 31.32 O HETATM 5330 O HOH B 511 93.989 2.547 9.911 1.00 39.81 O HETATM 5331 O HOH B 512 125.029 -3.452 31.067 1.00 41.44 O HETATM 5332 O HOH B 513 127.351 -5.603 46.303 1.00 31.55 O HETATM 5333 O HOH B 514 127.485 -7.576 33.492 1.00 30.69 O HETATM 5334 O HOH B 515 114.871 -12.188 -5.124 1.00 60.98 O HETATM 5335 O HOH B 516 124.924 -6.408 9.678 1.00 54.12 O HETATM 5336 O HOH B 517 124.277 -3.467 12.084 1.00 46.98 O HETATM 5337 O HOH B 518 116.758 -11.003 60.071 1.00 35.69 O HETATM 5338 O HOH B 519 116.879 -19.273 5.439 1.00 50.31 O HETATM 5339 O HOH B 520 111.810 -13.645 49.960 1.00 44.96 O HETATM 5340 O HOH B 521 133.411 7.754 57.519 1.00 60.48 O HETATM 5341 O HOH B 522 131.553 -8.746 50.749 1.00 37.12 O HETATM 5342 O HOH B 523 111.175 2.192 57.849 1.00 37.36 O HETATM 5343 O HOH B 524 119.412 -4.319 16.044 1.00 21.88 O HETATM 5344 O HOH B 525 113.087 -12.909 54.475 1.00 41.35 O HETATM 5345 O HOH B 526 119.360 2.133 14.728 1.00 52.62 O HETATM 5346 O HOH B 527 104.917 5.538 57.089 1.00 71.37 O HETATM 5347 O HOH B 528 132.414 3.354 49.775 1.00 55.05 O HETATM 5348 O HOH B 529 117.617 -14.522 62.124 1.00 58.23 O HETATM 5349 O HOH B 530 122.522 -6.760 11.152 1.00 55.29 O HETATM 5350 O HOH B 531 122.284 -5.135 14.593 1.00 42.57 O HETATM 5351 O HOH B 532 116.310 -15.050 59.636 1.00 55.78 O CONECT 607 1231 CONECT 1231 607 CONECT 2932 3556 CONECT 3556 2932 CONECT 4665 4666 4683 CONECT 4666 4665 4667 4685 CONECT 4667 4666 4668 4684 CONECT 4668 4667 4682 CONECT 4669 4684 4685 CONECT 4670 4671 4674 4702 CONECT 4671 4670 4672 CONECT 4672 4671 4673 4696 CONECT 4673 4672 4674 4679 CONECT 4674 4670 4673 4675 CONECT 4675 4674 4676 CONECT 4676 4675 4677 CONECT 4677 4676 4678 CONECT 4678 4677 CONECT 4679 4673 4680 CONECT 4680 4679 4681 4686 CONECT 4681 4680 4682 CONECT 4682 4668 4681 4683 CONECT 4683 4665 4682 CONECT 4684 4667 4669 CONECT 4685 4666 4669 CONECT 4686 4680 4687 CONECT 4687 4686 4688 4695 CONECT 4688 4687 4689 CONECT 4689 4688 4690 4693 CONECT 4690 4689 4691 CONECT 4691 4690 4692 CONECT 4692 4691 4693 CONECT 4693 4689 4692 4694 CONECT 4694 4693 4695 CONECT 4695 4687 4694 CONECT 4696 4672 4697 4701 CONECT 4697 4696 4698 CONECT 4698 4697 4699 CONECT 4699 4698 4700 CONECT 4700 4699 4701 CONECT 4701 4696 4700 CONECT 4702 4670 4703 4707 CONECT 4703 4702 4704 CONECT 4704 4703 4705 CONECT 4705 4704 4706 CONECT 4706 4705 4707 CONECT 4707 4702 4706 CONECT 4708 4710 CONECT 4709 4710 CONECT 4710 4708 4709 4711 CONECT 4711 4710 4712 4713 CONECT 4712 4711 CONECT 4713 4711 4714 4715 CONECT 4714 4713 CONECT 4715 4713 4716 4717 CONECT 4716 4715 CONECT 4717 4715 CONECT 4718 4720 CONECT 4719 4720 CONECT 4720 4718 4719 4721 CONECT 4721 4720 4722 4723 CONECT 4722 4721 CONECT 4723 4721 4724 4725 CONECT 4724 4723 CONECT 4725 4723 4726 4727 CONECT 4726 4725 CONECT 4727 4725 CONECT 4728 4729 4730 4731 CONECT 4729 4728 CONECT 4730 4728 CONECT 4731 4728 4732 CONECT 4732 4731 4733 CONECT 4733 4732 4734 CONECT 4734 4733 4735 CONECT 4735 4734 4736 CONECT 4736 4735 4737 CONECT 4737 4736 4738 CONECT 4738 4737 4739 CONECT 4739 4738 4740 CONECT 4740 4739 4741 CONECT 4741 4740 4742 CONECT 4742 4741 4743 CONECT 4743 4742 4744 CONECT 4744 4743 CONECT 4745 4746 4747 4748 CONECT 4746 4745 CONECT 4747 4745 CONECT 4748 4745 4749 CONECT 4749 4748 4750 CONECT 4750 4749 4751 CONECT 4751 4750 4752 CONECT 4752 4751 4753 CONECT 4753 4752 4754 CONECT 4754 4753 4755 CONECT 4755 4754 4756 CONECT 4756 4755 4757 CONECT 4757 4756 4758 CONECT 4758 4757 4759 CONECT 4759 4758 4760 CONECT 4760 4759 4761 CONECT 4761 4760 4762 CONECT 4762 4761 4763 CONECT 4763 4762 4764 CONECT 4764 4763 CONECT 4765 4766 CONECT 4766 4765 4767 CONECT 4767 4766 4768 CONECT 4768 4767 4769 CONECT 4769 4768 4770 CONECT 4770 4769 4771 CONECT 4771 4770 4772 CONECT 4772 4771 4773 CONECT 4773 4772 4774 CONECT 4774 4773 4775 CONECT 4775 4774 4776 CONECT 4776 4775 4777 CONECT 4777 4776 4778 CONECT 4778 4777 4779 CONECT 4779 4778 CONECT 4780 4781 4782 4783 CONECT 4781 4780 CONECT 4782 4780 CONECT 4783 4780 4784 CONECT 4784 4783 4785 CONECT 4785 4784 4786 CONECT 4786 4785 4787 CONECT 4787 4786 4788 CONECT 4788 4787 4789 CONECT 4789 4788 4790 CONECT 4790 4789 4791 CONECT 4791 4790 4792 CONECT 4792 4791 4793 CONECT 4793 4792 CONECT 4794 4795 4796 4797 CONECT 4795 4794 CONECT 4796 4794 CONECT 4797 4794 4798 CONECT 4798 4797 4799 CONECT 4799 4798 4800 CONECT 4800 4799 4801 CONECT 4801 4800 4802 CONECT 4802 4801 4803 CONECT 4803 4802 4804 CONECT 4804 4803 4805 CONECT 4805 4804 4806 CONECT 4806 4805 4807 CONECT 4807 4806 4808 CONECT 4808 4807 4809 CONECT 4809 4808 CONECT 4810 4811 CONECT 4811 4810 4812 CONECT 4812 4811 4813 CONECT 4813 4812 4814 CONECT 4814 4813 4815 CONECT 4815 4814 4816 CONECT 4816 4815 4817 CONECT 4817 4816 4818 CONECT 4818 4817 4819 CONECT 4819 4818 4820 CONECT 4820 4819 4821 CONECT 4821 4820 CONECT 4822 4823 CONECT 4823 4822 4824 CONECT 4824 4823 4825 CONECT 4825 4824 4826 CONECT 4826 4825 4827 CONECT 4827 4826 4828 CONECT 4828 4827 4829 CONECT 4829 4828 4830 CONECT 4830 4829 4831 CONECT 4831 4830 CONECT 4832 4833 4834 4835 CONECT 4833 4832 CONECT 4834 4832 CONECT 4835 4832 4836 CONECT 4836 4835 4837 CONECT 4837 4836 4838 CONECT 4838 4837 4839 CONECT 4839 4838 4840 CONECT 4840 4839 4841 CONECT 4841 4840 4842 CONECT 4842 4841 4843 CONECT 4843 4842 4844 CONECT 4844 4843 4845 CONECT 4845 4844 4846 CONECT 4846 4845 4847 CONECT 4847 4846 4848 CONECT 4848 4847 4849 CONECT 4849 4848 CONECT 4850 4851 4852 4853 CONECT 4851 4850 CONECT 4852 4850 CONECT 4853 4850 4854 CONECT 4854 4853 4855 CONECT 4855 4854 4856 CONECT 4856 4855 4857 CONECT 4857 4856 4858 CONECT 4858 4857 4859 CONECT 4859 4858 4860 CONECT 4860 4859 4861 CONECT 4861 4860 4862 CONECT 4862 4861 4863 CONECT 4863 4862 4864 CONECT 4864 4863 4865 CONECT 4865 4864 4866 CONECT 4866 4865 4867 CONECT 4867 4866 4868 CONECT 4868 4867 4869 CONECT 4869 4868 CONECT 4870 4871 CONECT 4871 4870 4872 CONECT 4872 4871 4873 CONECT 4873 4872 4874 CONECT 4874 4873 4875 CONECT 4875 4874 4876 CONECT 4876 4875 4877 CONECT 4877 4876 4878 CONECT 4878 4877 4879 CONECT 4879 4878 4880 CONECT 4880 4879 4881 CONECT 4881 4880 4882 CONECT 4882 4881 CONECT 4883 4884 4885 4886 CONECT 4884 4883 CONECT 4885 4883 CONECT 4886 4883 4887 CONECT 4887 4886 4888 CONECT 4888 4887 4889 CONECT 4889 4888 4890 CONECT 4890 4889 4891 CONECT 4891 4890 4892 CONECT 4892 4891 4893 CONECT 4893 4892 4894 CONECT 4894 4893 4895 CONECT 4895 4894 4896 CONECT 4896 4895 4897 CONECT 4897 4896 4898 CONECT 4898 4897 CONECT 4899 4900 CONECT 4900 4899 4901 CONECT 4901 4900 4902 CONECT 4902 4901 4903 CONECT 4903 4902 4904 CONECT 4904 4903 4905 CONECT 4905 4904 4906 CONECT 4906 4905 4907 CONECT 4907 4906 4908 CONECT 4908 4907 4909 CONECT 4909 4908 4910 CONECT 4910 4909 4911 CONECT 4911 4910 4912 CONECT 4912 4911 4913 CONECT 4913 4912 CONECT 4914 4915 4916 4917 CONECT 4915 4914 CONECT 4916 4914 CONECT 4917 4914 4918 CONECT 4918 4917 4919 CONECT 4919 4918 4920 CONECT 4920 4919 4921 CONECT 4921 4920 4922 CONECT 4922 4921 4923 CONECT 4923 4922 4924 CONECT 4924 4923 4925 CONECT 4925 4924 4926 CONECT 4926 4925 4927 CONECT 4927 4926 4928 CONECT 4928 4927 4929 CONECT 4929 4928 4930 CONECT 4930 4929 4931 CONECT 4931 4930 4932 CONECT 4932 4931 4933 CONECT 4933 4932 CONECT 4934 4935 4936 4937 CONECT 4935 4934 CONECT 4936 4934 CONECT 4937 4934 4938 CONECT 4938 4937 4939 CONECT 4939 4938 4940 CONECT 4940 4939 4941 CONECT 4941 4940 4942 CONECT 4942 4941 4943 CONECT 4943 4942 4944 CONECT 4944 4943 4945 CONECT 4945 4944 4946 CONECT 4946 4945 4947 CONECT 4947 4946 4948 CONECT 4948 4947 4949 CONECT 4949 4948 4950 CONECT 4950 4949 4951 CONECT 4951 4950 4952 CONECT 4952 4951 4953 CONECT 4953 4952 CONECT 4954 4955 4956 4957 CONECT 4955 4954 CONECT 4956 4954 CONECT 4957 4954 4958 CONECT 4958 4957 4959 CONECT 4959 4958 4960 CONECT 4960 4959 4961 CONECT 4961 4960 4962 CONECT 4962 4961 4963 CONECT 4963 4962 4964 CONECT 4964 4963 CONECT 4965 4966 4983 CONECT 4966 4965 4967 4985 CONECT 4967 4966 4968 4984 CONECT 4968 4967 4982 CONECT 4969 4984 4985 CONECT 4970 4971 4974 5002 CONECT 4971 4970 4972 CONECT 4972 4971 4973 4996 CONECT 4973 4972 4974 4979 CONECT 4974 4970 4973 4975 CONECT 4975 4974 4976 CONECT 4976 4975 4977 CONECT 4977 4976 4978 CONECT 4978 4977 CONECT 4979 4973 4980 CONECT 4980 4979 4981 4986 CONECT 4981 4980 4982 CONECT 4982 4968 4981 4983 CONECT 4983 4965 4982 CONECT 4984 4967 4969 CONECT 4985 4966 4969 CONECT 4986 4980 4987 CONECT 4987 4986 4988 4995 CONECT 4988 4987 4989 CONECT 4989 4988 4990 4993 CONECT 4990 4989 4991 CONECT 4991 4990 4992 CONECT 4992 4991 4993 CONECT 4993 4989 4992 4994 CONECT 4994 4993 4995 CONECT 4995 4987 4994 CONECT 4996 4972 4997 5001 CONECT 4997 4996 4998 CONECT 4998 4997 4999 CONECT 4999 4998 5000 CONECT 5000 4999 5001 CONECT 5001 4996 5000 CONECT 5002 4970 5003 5007 CONECT 5003 5002 5004 CONECT 5004 5003 5005 CONECT 5005 5004 5006 CONECT 5006 5005 5007 CONECT 5007 5002 5006 CONECT 5008 5010 CONECT 5009 5010 CONECT 5010 5008 5009 5011 CONECT 5011 5010 5012 5013 CONECT 5012 5011 CONECT 5013 5011 5014 5015 CONECT 5014 5013 CONECT 5015 5013 5016 5017 CONECT 5016 5015 CONECT 5017 5015 CONECT 5018 5019 5020 5021 CONECT 5019 5018 CONECT 5020 5018 CONECT 5021 5018 5022 CONECT 5022 5021 5023 CONECT 5023 5022 5024 CONECT 5024 5023 5025 CONECT 5025 5024 5026 CONECT 5026 5025 5027 CONECT 5027 5026 5028 CONECT 5028 5027 5029 CONECT 5029 5028 5030 CONECT 5030 5029 CONECT 5031 5032 5033 5034 CONECT 5032 5031 CONECT 5033 5031 CONECT 5034 5031 5035 CONECT 5035 5034 5036 CONECT 5036 5035 5037 CONECT 5037 5036 5038 CONECT 5038 5037 5039 CONECT 5039 5038 5040 CONECT 5040 5039 CONECT 5041 5042 5043 5044 CONECT 5042 5041 CONECT 5043 5041 CONECT 5044 5041 5045 CONECT 5045 5044 5046 CONECT 5046 5045 5047 CONECT 5047 5046 5048 CONECT 5048 5047 5049 CONECT 5049 5048 5050 CONECT 5050 5049 5051 CONECT 5051 5050 5052 CONECT 5052 5051 5053 CONECT 5053 5052 5054 CONECT 5054 5053 5055 CONECT 5055 5054 CONECT 5056 5057 5058 5059 CONECT 5057 5056 CONECT 5058 5056 CONECT 5059 5056 5060 CONECT 5060 5059 5061 CONECT 5061 5060 5062 CONECT 5062 5061 5063 CONECT 5063 5062 5064 CONECT 5064 5063 5065 CONECT 5065 5064 5066 CONECT 5066 5065 5067 CONECT 5067 5066 5068 CONECT 5068 5067 5069 CONECT 5069 5068 CONECT 5070 5071 5072 5073 CONECT 5071 5070 CONECT 5072 5070 CONECT 5073 5070 5074 CONECT 5074 5073 5075 CONECT 5075 5074 5076 CONECT 5076 5075 5077 CONECT 5077 5076 5078 CONECT 5078 5077 5079 CONECT 5079 5078 5080 CONECT 5080 5079 5081 CONECT 5081 5080 5082 CONECT 5082 5081 CONECT 5083 5084 5085 5086 CONECT 5084 5083 CONECT 5085 5083 CONECT 5086 5083 5087 CONECT 5087 5086 5088 CONECT 5088 5087 5089 CONECT 5089 5088 CONECT 5090 5091 5092 5093 CONECT 5091 5090 CONECT 5092 5090 CONECT 5093 5090 5094 CONECT 5094 5093 5095 CONECT 5095 5094 5096 CONECT 5096 5095 5097 CONECT 5097 5096 5098 CONECT 5098 5097 5099 CONECT 5099 5098 5100 CONECT 5100 5099 5101 CONECT 5101 5100 5102 CONECT 5102 5101 5103 CONECT 5103 5102 5104 CONECT 5104 5103 5105 CONECT 5105 5104 CONECT 5106 5107 5108 5109 CONECT 5107 5106 CONECT 5108 5106 CONECT 5109 5106 5110 CONECT 5110 5109 5111 CONECT 5111 5110 5112 CONECT 5112 5111 5113 CONECT 5113 5112 5114 CONECT 5114 5113 5115 CONECT 5115 5114 5116 CONECT 5116 5115 5117 CONECT 5117 5116 5118 CONECT 5118 5117 5119 CONECT 5119 5118 5120 CONECT 5120 5119 5121 CONECT 5121 5120 5122 CONECT 5122 5121 5123 CONECT 5123 5122 5124 CONECT 5124 5123 5125 CONECT 5125 5124 CONECT 5126 5127 5128 5129 CONECT 5127 5126 CONECT 5128 5126 CONECT 5129 5126 5130 CONECT 5130 5129 5131 CONECT 5131 5130 5132 CONECT 5132 5131 5133 CONECT 5133 5132 5134 CONECT 5134 5133 5135 CONECT 5135 5134 5136 CONECT 5136 5135 5137 CONECT 5137 5136 5138 CONECT 5138 5137 5139 CONECT 5139 5138 CONECT 5140 5141 5142 5143 CONECT 5141 5140 CONECT 5142 5140 CONECT 5143 5140 5144 CONECT 5144 5143 5145 CONECT 5145 5144 5146 CONECT 5146 5145 5147 CONECT 5147 5146 5148 CONECT 5148 5147 5149 CONECT 5149 5148 5150 CONECT 5150 5149 5151 CONECT 5151 5150 5152 CONECT 5152 5151 5153 CONECT 5153 5152 5154 CONECT 5154 5153 5155 CONECT 5155 5154 5156 CONECT 5156 5155 5157 CONECT 5157 5156 5158 CONECT 5158 5157 5159 CONECT 5159 5158 CONECT 5160 5161 5162 5163 CONECT 5161 5160 CONECT 5162 5160 CONECT 5163 5160 5164 CONECT 5164 5163 5165 CONECT 5165 5164 5166 CONECT 5166 5165 5167 CONECT 5167 5166 5168 CONECT 5168 5167 5169 CONECT 5169 5168 5170 CONECT 5170 5169 5171 CONECT 5171 5170 5172 CONECT 5172 5171 5173 CONECT 5173 5172 CONECT 5174 5175 CONECT 5175 5174 5176 CONECT 5176 5175 5177 CONECT 5177 5176 5178 CONECT 5178 5177 5179 CONECT 5179 5178 5180 CONECT 5180 5179 5181 CONECT 5181 5180 5182 CONECT 5182 5181 CONECT 5183 5184 5185 5186 CONECT 5184 5183 CONECT 5185 5183 CONECT 5186 5183 5187 CONECT 5187 5186 5188 CONECT 5188 5187 5189 CONECT 5189 5188 5190 CONECT 5190 5189 5191 CONECT 5191 5190 5192 CONECT 5192 5191 5193 CONECT 5193 5192 5194 CONECT 5194 5193 5195 CONECT 5195 5194 5196 CONECT 5196 5195 5197 CONECT 5197 5196 5198 CONECT 5198 5197 5199 CONECT 5199 5198 5200 CONECT 5200 5199 5201 CONECT 5201 5200 5202 CONECT 5202 5201 CONECT 5203 5204 5205 5206 CONECT 5204 5203 CONECT 5205 5203 CONECT 5206 5203 5207 CONECT 5207 5206 5208 CONECT 5208 5207 5209 CONECT 5209 5208 5210 CONECT 5210 5209 5211 CONECT 5211 5210 5212 CONECT 5212 5211 5213 CONECT 5213 5212 5214 CONECT 5214 5213 5215 CONECT 5215 5214 5216 CONECT 5216 5215 5217 CONECT 5217 5216 5218 CONECT 5218 5217 5219 CONECT 5219 5218 5220 CONECT 5220 5219 5221 CONECT 5221 5220 5222 CONECT 5222 5221 CONECT 5223 5224 5225 5226 CONECT 5224 5223 CONECT 5225 5223 CONECT 5226 5223 5227 CONECT 5227 5226 5228 CONECT 5228 5227 5229 CONECT 5229 5228 5230 CONECT 5230 5229 5231 CONECT 5231 5230 5232 CONECT 5232 5231 5233 CONECT 5233 5232 5234 CONECT 5234 5233 5235 CONECT 5235 5234 5236 CONECT 5236 5235 5237 CONECT 5237 5236 5238 CONECT 5238 5237 CONECT 5239 5240 5241 5242 CONECT 5240 5239 CONECT 5241 5239 CONECT 5242 5239 5243 CONECT 5243 5242 5244 CONECT 5244 5243 5245 CONECT 5245 5244 5246 CONECT 5246 5245 5247 CONECT 5247 5246 5248 CONECT 5248 5247 5249 CONECT 5249 5248 5250 CONECT 5250 5249 5251 CONECT 5251 5250 5252 CONECT 5252 5251 5253 CONECT 5253 5252 CONECT 5254 5255 CONECT 5255 5254 5256 CONECT 5256 5255 5257 CONECT 5257 5256 5258 CONECT 5258 5257 5259 CONECT 5259 5258 5260 CONECT 5260 5259 5261 CONECT 5261 5260 5262 CONECT 5262 5261 5263 CONECT 5263 5262 5264 CONECT 5264 5263 5265 CONECT 5265 5264 5266 CONECT 5266 5265 5267 CONECT 5267 5266 CONECT 5268 5269 5270 5271 CONECT 5269 5268 CONECT 5270 5268 CONECT 5271 5268 5272 CONECT 5272 5271 5273 5274 5278 CONECT 5273 5272 CONECT 5274 5272 5275 CONECT 5275 5274 5276 5277 CONECT 5276 5275 CONECT 5277 5275 CONECT 5278 5272 5279 5280 CONECT 5279 5278 CONECT 5280 5278 MASTER 624 0 38 28 4 0 45 6 5349 2 620 50 END