HEADER MEMBRANE PROTEIN/INHIBITOR 05-JAN-18 6C1R TITLE CRYSTAL STRUCTURE OF HUMAN C5A RECEPTOR IN COMPLEX WITH AN ORTHOSTERIC TITLE 2 ANTAGONIST PMX53 AND AN ALLOSTERIC ANTAGONIST AVACOPAN COMPND MOL_ID: 1; COMPND 2 MOLECULE: SOLUBLE CYTOCHROME B562, C5A ANAPHYLATOXIN CHEMOTACTIC COMPND 3 RECEPTOR 1 CHIMERA; COMPND 4 CHAIN: B; COMPND 5 FRAGMENT: CYTOCHROME (UNP RESIDUES 23-127) + C5A RECEPTOR (UNP COMPND 6 RESIDUES 30-331); COMPND 7 SYNONYM: CYTOCHROME B-562,C5A ANAPHYLATOXIN CHEMOTACTIC RECEPTOR, COMPND 8 C5AR; COMPND 9 ENGINEERED: YES; COMPND 10 MUTATION: YES; COMPND 11 MOL_ID: 2; COMPND 12 MOLECULE: PMX53; COMPND 13 CHAIN: L; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI, HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 562, 9606; SOURCE 5 GENE: CYBC, 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_CELL_LINE: SF9; SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC; SOURCE 12 MOL_ID: 2; SOURCE 13 SYNTHETIC: YES; SOURCE 14 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 15 ORGANISM_TAXID: 32630 KEYWDS GPCR, MEMBRANE PROTEIN-INHIBITOR COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR H.LIU,L.WANG,Z.WEI,C.ZHANG REVDAT 4 08-JAN-20 6C1R 1 REMARK REVDAT 3 05-SEP-18 6C1R 1 REMARK REVDAT 2 20-JUN-18 6C1R 1 JRNL REVDAT 1 30-MAY-18 6C1R 0 JRNL AUTH H.LIU,H.R.KIM,R.N.V.K.DEEPAK,L.WANG,K.Y.CHUNG,H.FAN,Z.WEI, JRNL AUTH 2 C.ZHANG JRNL TITL ORTHOSTERIC AND ALLOSTERIC ACTION OF THE C5A RECEPTOR JRNL TITL 2 ANTAGONISTS. JRNL REF NAT. STRUCT. MOL. BIOL. V. 25 472 2018 JRNL REFN ESSN 1545-9985 JRNL PMID 29867214 JRNL DOI 10.1038/S41594-018-0067-Z REMARK 2 REMARK 2 RESOLUTION. 2.20 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) : 2.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.36 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 3 NUMBER OF REFLECTIONS : 24988 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.194 REMARK 3 R VALUE (WORKING SET) : 0.192 REMARK 3 FREE R VALUE : 0.224 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060 REMARK 3 FREE R VALUE TEST SET COUNT : 1264 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 27.3613 - 4.5699 1.00 2725 143 0.1969 0.2048 REMARK 3 2 4.5699 - 3.6300 1.00 2645 143 0.1758 0.2198 REMARK 3 3 3.6300 - 3.1719 1.00 2671 139 0.1905 0.2348 REMARK 3 4 3.1719 - 2.8822 1.00 2616 143 0.1827 0.2239 REMARK 3 5 2.8822 - 2.6758 1.00 2654 134 0.1796 0.2234 REMARK 3 6 2.6758 - 2.5182 1.00 2617 142 0.1869 0.2182 REMARK 3 7 2.5182 - 2.3922 1.00 2618 145 0.2123 0.2332 REMARK 3 8 2.3922 - 2.2881 0.99 2617 132 0.2340 0.2747 REMARK 3 9 2.2881 - 2.2000 0.98 2561 143 0.2623 0.2896 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) : 0.210 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.970 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 41.20 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.60 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 : 0.005 3102 REMARK 3 ANGLE : 1.006 4200 REMARK 3 CHIRALITY : 0.028 500 REMARK 3 PLANARITY : 0.004 499 REMARK 3 DIHEDRAL : 16.969 1104 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 12 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 30 THROUGH 65 ) REMARK 3 ORIGIN FOR THE GROUP (A): -14.3664 3.6881 -37.2846 REMARK 3 T TENSOR REMARK 3 T11: 0.2155 T22: 0.3474 REMARK 3 T33: 0.4346 T12: -0.0325 REMARK 3 T13: -0.0244 T23: 0.0409 REMARK 3 L TENSOR REMARK 3 L11: 3.1277 L22: 9.9251 REMARK 3 L33: 6.3671 L12: 0.2268 REMARK 3 L13: 0.9486 L23: 7.3078 REMARK 3 S TENSOR REMARK 3 S11: -0.2125 S12: -0.2045 S13: -0.0845 REMARK 3 S21: 0.0837 S22: -0.3805 S23: 0.9026 REMARK 3 S31: 0.1342 S32: -0.6477 S33: 0.6712 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 66 THROUGH 97 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.4133 -2.6149 -42.2970 REMARK 3 T TENSOR REMARK 3 T11: 0.2239 T22: 0.2622 REMARK 3 T33: 0.3268 T12: -0.0272 REMARK 3 T13: -0.0504 T23: 0.0005 REMARK 3 L TENSOR REMARK 3 L11: 4.1667 L22: 1.8143 REMARK 3 L33: 6.2736 L12: 0.2231 REMARK 3 L13: -4.0679 L23: 0.2411 REMARK 3 S TENSOR REMARK 3 S11: -0.3418 S12: 0.3763 S13: -0.4630 REMARK 3 S21: -0.1778 S22: -0.1511 S23: 0.3396 REMARK 3 S31: 0.4013 S32: -0.6781 S33: 0.4188 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 98 THROUGH 139 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.6147 -0.3595 -37.2673 REMARK 3 T TENSOR REMARK 3 T11: 0.2402 T22: 0.2205 REMARK 3 T33: 0.3031 T12: -0.0027 REMARK 3 T13: -0.0331 T23: 0.0099 REMARK 3 L TENSOR REMARK 3 L11: 3.8379 L22: 1.8088 REMARK 3 L33: 8.1873 L12: 1.7358 REMARK 3 L13: -4.2006 L23: -1.7066 REMARK 3 S TENSOR REMARK 3 S11: -0.1357 S12: 0.1197 S13: -0.0611 REMARK 3 S21: -0.1520 S22: 0.0376 S23: 0.1429 REMARK 3 S31: 0.2027 S32: -0.4560 S33: 0.0489 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 140 THROUGH 149 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.0470 -2.2271 -62.8976 REMARK 3 T TENSOR REMARK 3 T11: 0.7084 T22: 0.6283 REMARK 3 T33: 0.6581 T12: -0.0051 REMARK 3 T13: 0.0629 T23: -0.0029 REMARK 3 L TENSOR REMARK 3 L11: 9.8847 L22: 7.9615 REMARK 3 L33: 2.0046 L12: -8.1057 REMARK 3 L13: -2.1080 L23: -2.3980 REMARK 3 S TENSOR REMARK 3 S11: -0.2643 S12: 0.1909 S13: -0.9075 REMARK 3 S21: -0.7611 S22: -0.3687 S23: 0.4228 REMARK 3 S31: 1.8763 S32: 0.2376 S33: 0.5100 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 150 THROUGH 180 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.3137 -6.5401 -33.5986 REMARK 3 T TENSOR REMARK 3 T11: 0.1984 T22: 0.1619 REMARK 3 T33: 0.2723 T12: -0.0229 REMARK 3 T13: 0.0004 T23: 0.0269 REMARK 3 L TENSOR REMARK 3 L11: 1.4370 L22: 3.6266 REMARK 3 L33: 9.9090 L12: -1.0429 REMARK 3 L13: -0.7632 L23: 1.8700 REMARK 3 S TENSOR REMARK 3 S11: -0.1725 S12: -0.1023 S13: -0.1266 REMARK 3 S21: 0.2467 S22: -0.0364 S23: 0.2929 REMARK 3 S31: 0.4797 S32: -0.0969 S33: 0.1777 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 181 THROUGH 211 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.9145 2.7249 -20.2858 REMARK 3 T TENSOR REMARK 3 T11: 0.4970 T22: 0.3558 REMARK 3 T33: 0.3359 T12: 0.0303 REMARK 3 T13: -0.0073 T23: 0.0697 REMARK 3 L TENSOR REMARK 3 L11: 7.1891 L22: 3.4340 REMARK 3 L33: 9.4054 L12: 3.5175 REMARK 3 L13: -5.1857 L23: -2.6602 REMARK 3 S TENSOR REMARK 3 S11: 0.1243 S12: -1.2552 S13: -0.5722 REMARK 3 S21: 0.8491 S22: -0.4552 S23: -0.2010 REMARK 3 S31: -0.2598 S32: 0.7640 S33: 0.2490 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 212 THROUGH 237 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.0981 13.2462 -53.2813 REMARK 3 T TENSOR REMARK 3 T11: 0.3192 T22: 0.3441 REMARK 3 T33: 0.2509 T12: -0.0488 REMARK 3 T13: 0.0233 T23: -0.0086 REMARK 3 L TENSOR REMARK 3 L11: 6.9298 L22: 5.4067 REMARK 3 L33: 2.1047 L12: -0.3105 REMARK 3 L13: 2.0275 L23: -0.8048 REMARK 3 S TENSOR REMARK 3 S11: -0.1306 S12: 0.9380 S13: 0.1906 REMARK 3 S21: -0.7645 S22: -0.1927 S23: -0.0553 REMARK 3 S31: 0.1605 S32: 0.1157 S33: 0.2669 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 238 THROUGH 305 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.2984 10.8855 -35.0153 REMARK 3 T TENSOR REMARK 3 T11: 0.1956 T22: 0.1873 REMARK 3 T33: 0.3328 T12: 0.0481 REMARK 3 T13: -0.0194 T23: 0.0347 REMARK 3 L TENSOR REMARK 3 L11: 1.3158 L22: 1.8069 REMARK 3 L33: 5.9045 L12: 0.3563 REMARK 3 L13: 0.0167 L23: 1.3114 REMARK 3 S TENSOR REMARK 3 S11: -0.1231 S12: -0.0519 S13: 0.0888 REMARK 3 S21: 0.0178 S22: -0.0336 S23: 0.2239 REMARK 3 S31: -0.1685 S32: -0.1207 S33: 0.1779 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 306 THROUGH 327 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.1019 2.7421 -59.6980 REMARK 3 T TENSOR REMARK 3 T11: 0.5055 T22: 0.7121 REMARK 3 T33: 0.6522 T12: 0.0241 REMARK 3 T13: -0.1758 T23: -0.0172 REMARK 3 L TENSOR REMARK 3 L11: 2.0246 L22: 3.1960 REMARK 3 L33: 9.5037 L12: 0.2562 REMARK 3 L13: -7.5728 L23: 1.3247 REMARK 3 S TENSOR REMARK 3 S11: 0.2235 S12: 1.0624 S13: -0.4686 REMARK 3 S21: -0.4094 S22: -0.0826 S23: 0.4131 REMARK 3 S31: -0.3321 S32: -0.4982 S33: -0.0293 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 12 THROUGH 68 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.3579 17.7385 -3.2386 REMARK 3 T TENSOR REMARK 3 T11: 0.9072 T22: 1.0657 REMARK 3 T33: 0.4423 T12: 0.0127 REMARK 3 T13: 0.1296 T23: -0.1939 REMARK 3 L TENSOR REMARK 3 L11: 7.0529 L22: 3.8290 REMARK 3 L33: 3.0745 L12: 1.4796 REMARK 3 L13: 3.6983 L23: -0.6062 REMARK 3 S TENSOR REMARK 3 S11: -0.0136 S12: 1.0447 S13: -0.2053 REMARK 3 S21: -1.1412 S22: 0.1771 S23: -0.1870 REMARK 3 S31: -0.3652 S32: -0.6067 S33: -0.1149 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 69 THROUGH 90 ) REMARK 3 ORIGIN FOR THE GROUP (A): -9.7187 16.0984 6.9900 REMARK 3 T TENSOR REMARK 3 T11: 0.7072 T22: 1.0935 REMARK 3 T33: 0.5194 T12: -0.0856 REMARK 3 T13: 0.1936 T23: -0.2642 REMARK 3 L TENSOR REMARK 3 L11: 2.0006 L22: 1.7833 REMARK 3 L33: 3.5130 L12: 0.8357 REMARK 3 L13: 5.5805 L23: -0.2536 REMARK 3 S TENSOR REMARK 3 S11: -0.1844 S12: -1.3103 S13: 0.3969 REMARK 3 S21: 0.3662 S22: -0.1571 S23: 0.5971 REMARK 3 S31: -0.1205 S32: -1.8260 S33: 0.3077 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 91 THROUGH 110 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.1971 8.8650 3.3397 REMARK 3 T TENSOR REMARK 3 T11: 0.9170 T22: 0.8016 REMARK 3 T33: 0.6033 T12: -0.1323 REMARK 3 T13: 0.1468 T23: -0.2809 REMARK 3 L TENSOR REMARK 3 L11: 2.0113 L22: 5.9137 REMARK 3 L33: 5.3497 L12: 3.2491 REMARK 3 L13: 7.3873 L23: 1.2503 REMARK 3 S TENSOR REMARK 3 S11: 0.1044 S12: -0.1261 S13: -0.6173 REMARK 3 S21: 0.6565 S22: 0.1077 S23: -0.0235 REMARK 3 S31: 0.5947 S32: -0.8169 S33: -0.2446 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 6C1R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JAN-18. REMARK 100 THE DEPOSITION ID IS D_1000231948. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 27-OCT-17 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL CRYO-COOLED REMARK 200 SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25865 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 200 DATA REDUNDANCY : 6.700 REMARK 200 R MERGE (I) : 0.12800 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.24 REMARK 200 COMPLETENESS FOR SHELL (%) : 94.8 REMARK 200 DATA REDUNDANCY IN SHELL : 4.10 REMARK 200 R MERGE FOR SHELL (I) : 0.99800 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 4ZUD REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.95 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 25-32% PEG300, 100 MM MES, PH6.5, 90 REMARK 280 -120 MM SODIUM MALONATE, 1% P400, 5 UM AVACOPAN, 5 UM PMX53, REMARK 280 LIPIDIC CUBIC PHASE, TEMPERATURE 283K 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 26.30400 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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3830 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19800 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, L 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 400 REMARK 400 COMPOUND REMARK 400 REMARK 400 THE PMX53 IS CYCLIC PEPTIDE, A MEMBER OF CLASS. REMARK 400 REMARK 400 GROUP: 1 REMARK 400 NAME: PMX53 REMARK 400 CHAIN: L REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER REMARK 400 DESCRIPTION: NULL 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 ASP B 1 REMARK 465 TYR B 2 REMARK 465 LYS B 3 REMARK 465 ASP B 4 REMARK 465 ASP B 5 REMARK 465 ASP B 6 REMARK 465 ASP B 7 REMARK 465 VAL B 8 REMARK 465 ASP B 9 REMARK 465 ALA B 10 REMARK 465 ASP B 11 REMARK 465 GLN B 50 REMARK 465 LYS B 51 REMARK 465 ALA B 52 REMARK 465 THR B 53 REMARK 465 PRO B 54 REMARK 465 PRO B 55 REMARK 465 LYS B 56 REMARK 465 LEU B 57 REMARK 465 GLU B 58 REMARK 465 ASP B 59 REMARK 465 LYS B 60 REMARK 465 SER B 61 REMARK 465 PRO B 62 REMARK 465 ASP B 63 REMARK 465 SER B 64 REMARK 465 PRO B 65 REMARK 465 GLU B 66 REMARK 465 MET B 67 REMARK 465 ILE B 111 REMARK 465 GLN B 112 REMARK 465 LYS B 113 REMARK 465 TYR B 114 REMARK 465 LEU B 115 REMARK 465 ALA B 320 REMARK 465 THR B 321 REMARK 465 ARG B 322 REMARK 465 GLN B 394 REMARK 465 GLY B 395 REMARK 465 ARG B 396 REMARK 465 LEU B 397 REMARK 465 ARG B 398 REMARK 465 VAL B 414 REMARK 465 VAL B 415 REMARK 465 ARG B 416 REMARK 465 GLU B 417 REMARK 465 ASN B 418 REMARK 465 LEU B 419 REMARK 465 TYR B 420 REMARK 465 PHE B 421 REMARK 465 GLN B 422 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLU B 13 CG CD OE1 OE2 REMARK 470 ASP B 14 CG OD1 OD2 REMARK 470 GLU B 17 CG CD OE1 OE2 REMARK 470 LYS B 24 CG CD CE NZ REMARK 470 GLU B 27 CG CD OE1 OE2 REMARK 470 LYS B 28 CG CD CE NZ REMARK 470 ASP B 30 CG OD1 OD2 REMARK 470 LYS B 68 CG CD CE NZ REMARK 470 ASP B 69 CG OD1 OD2 REMARK 470 PHE B 70 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG B 71 CG CD NE CZ NH1 NH2 REMARK 470 HIS B 72 CG ND1 CD2 CE1 NE2 REMARK 470 PHE B 74 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS B 94 CG CD CE NZ REMARK 470 GLU B 95 CG CD OE1 OE2 REMARK 470 GLU B 101 CG CD OE1 OE2 REMARK 470 LYS B 104 CG CD CE NZ REMARK 470 ARG B 107 CG CD NE CZ NH1 NH2 REMARK 470 ASN B 108 CG OD1 ND2 REMARK 470 TYR B 110 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ASN B 117 CG OD1 ND2 REMARK 470 GLU B 151 CG CD OE1 OE2 REMARK 470 ARG B 154 CG CD NE CZ NH1 NH2 REMARK 470 PHE B 268 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG B 283 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 319 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 325 CG CD CE NZ REMARK 470 LYS B 328 CG CD CE NZ REMARK 470 PHE B 393 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS B 399 CG CD CE NZ REMARK 470 ASN B 407 CG OD1 ND2 REMARK 470 GLU B 411 CG CD OE1 OE2 REMARK 470 GLU B 412 CG CD OE1 OE2 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 GLN B 184 31.34 -91.20 REMARK 500 PHE B 233 -63.10 -101.63 REMARK 500 ASP B 281 62.96 -152.71 REMARK 500 PHE B 297 -62.80 -139.13 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 PGE B 505 REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA B 504 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP B 168 OD2 REMARK 620 2 ASN B 378 O 80.4 REMARK 620 3 ASN B 382 OD1 86.5 94.0 REMARK 620 4 HOH B 626 O 94.1 84.1 177.9 REMARK 620 5 HOH B 635 O 95.2 171.5 93.0 88.9 REMARK 620 6 HOH B 617 O 171.2 94.5 86.6 92.6 90.6 REMARK 620 N 1 2 3 4 5 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EFD B 501 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue MLI B 502 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue MLI B 503 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 504 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 505 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC B 506 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC B 507 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA B 508 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA B 509 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA B 510 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA B 511 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6C1Q RELATED DB: PDB DBREF 6C1R B 10 115 UNP P0ABE7 C562_ECOLX 23 128 DBREF 6C1R B 116 417 UNP P21730 C5AR1_HUMAN 30 331 DBREF 6C1R L 0 6 PDB 6C1R 6C1R 0 6 SEQADV 6C1R ASP B 1 UNP P0ABE7 EXPRESSION TAG SEQADV 6C1R TYR B 2 UNP P0ABE7 EXPRESSION TAG SEQADV 6C1R LYS B 3 UNP P0ABE7 EXPRESSION TAG SEQADV 6C1R ASP B 4 UNP P0ABE7 EXPRESSION TAG SEQADV 6C1R ASP B 5 UNP P0ABE7 EXPRESSION TAG SEQADV 6C1R ASP B 6 UNP P0ABE7 EXPRESSION TAG SEQADV 6C1R ASP B 7 UNP P0ABE7 EXPRESSION TAG SEQADV 6C1R VAL B 8 UNP P0ABE7 EXPRESSION TAG SEQADV 6C1R ASP B 9 UNP P0ABE7 EXPRESSION TAG SEQADV 6C1R TRP B 16 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 6C1R ILE B 111 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 6C1R LEU B 115 UNP P0ABE7 ARG 128 ENGINEERED MUTATION SEQADV 6C1R ASN B 418 UNP P21730 EXPRESSION TAG SEQADV 6C1R LEU B 419 UNP P21730 EXPRESSION TAG SEQADV 6C1R TYR B 420 UNP P21730 EXPRESSION TAG SEQADV 6C1R PHE B 421 UNP P21730 EXPRESSION TAG SEQADV 6C1R GLN B 422 UNP P21730 EXPRESSION TAG SEQRES 1 B 422 ASP TYR LYS ASP ASP ASP ASP VAL ASP ALA ASP LEU GLU SEQRES 2 B 422 ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS VAL ILE SEQRES 3 B 422 GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP ALA LEU SEQRES 4 B 422 THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN LYS ALA SEQRES 5 B 422 THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SER PRO SEQRES 6 B 422 GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE LEU VAL SEQRES 7 B 422 GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN GLU GLY SEQRES 8 B 422 LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN LEU LYS SEQRES 9 B 422 THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU SER ASN SEQRES 10 B 422 THR LEU ARG VAL PRO ASP ILE LEU ALA LEU VAL ILE PHE SEQRES 11 B 422 ALA VAL VAL PHE LEU VAL GLY VAL LEU GLY ASN ALA LEU SEQRES 12 B 422 VAL VAL TRP VAL THR ALA PHE GLU ALA LYS ARG THR ILE SEQRES 13 B 422 ASN ALA ILE TRP PHE LEU ASN LEU ALA VAL ALA ASP PHE SEQRES 14 B 422 LEU SER CYS LEU ALA LEU PRO ILE LEU PHE THR SER ILE SEQRES 15 B 422 VAL GLN HIS HIS HIS TRP PRO PHE GLY GLY ALA ALA CYS SEQRES 16 B 422 SER ILE LEU PRO SER LEU ILE LEU LEU ASN MET TYR ALA SEQRES 17 B 422 SER ILE LEU LEU LEU ALA THR ILE SER ALA ASP ARG PHE SEQRES 18 B 422 LEU LEU VAL PHE LYS PRO ILE TRP YCM GLN ASN PHE ARG SEQRES 19 B 422 GLY ALA GLY LEU ALA TRP ILE ALA CYS ALA VAL ALA TRP SEQRES 20 B 422 GLY LEU ALA LEU LEU LEU THR ILE PRO SER PHE LEU TYR SEQRES 21 B 422 ARG VAL VAL ARG GLU GLU TYR PHE PRO PRO LYS VAL LEU SEQRES 22 B 422 CYS GLY VAL ASP TYR SER HIS ASP LYS ARG ARG GLU ARG SEQRES 23 B 422 ALA VAL ALA ILE VAL ARG LEU VAL LEU GLY PHE LEU TRP SEQRES 24 B 422 PRO LEU LEU THR LEU THR ILE CYS TYR THR PHE ILE LEU SEQRES 25 B 422 LEU ARG THR TRP SER ARG ARG ALA THR ARG SER THR LYS SEQRES 26 B 422 THR LEU LYS VAL VAL VAL ALA VAL VAL ALA SER PHE PHE SEQRES 27 B 422 ILE PHE TRP LEU PRO TYR GLN VAL THR GLY ILE MET MET SEQRES 28 B 422 SER PHE LEU GLU PRO SER SER PRO THR PHE LEU LEU LEU SEQRES 29 B 422 LYS LYS LEU ASP SER LEU CYS VAL SER PHE ALA TYR ILE SEQRES 30 B 422 ASN CYS CYS ILE ASN PRO ILE ILE TYR VAL VAL ALA GLY SEQRES 31 B 422 GLN GLY PHE GLN GLY ARG LEU ARG LYS SER LEU PRO SER SEQRES 32 B 422 LEU LEU ARG ASN VAL LEU THR GLU GLU SER VAL VAL ARG SEQRES 33 B 422 GLU ASN LEU TYR PHE GLN SEQRES 1 L 7 ACE PHE ORN PRO ZAL TRP ARG MODRES 6C1R YCM B 230 CYS MODIFIED RESIDUE HET YCM B 230 10 HET ACE L 0 3 HET ORN L 2 8 HET ZAL L 4 11 HET EFD B 501 42 HET MLI B 502 7 HET MLI B 503 7 HET NA B 504 1 HET PGE B 505 9 HET OLC B 506 25 HET OLC B 507 25 HET OLA B 508 20 HET OLA B 509 20 HET OLA B 510 20 HET OLA B 511 20 HETNAM YCM S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE HETNAM ACE ACETYL GROUP HETNAM ORN L-ORNITHINE HETNAM ZAL 3-CYCLOHEXYL-D-ALANINE HETNAM EFD AVACOPAN HETNAM MLI MALONATE ION HETNAM NA SODIUM ION HETNAM PGE TRIETHYLENE GLYCOL HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM OLA OLEIC ACID HETSYN YCM CYSTEINE-S-ACETAMIDE HETSYN EFD (2R,3S)-2-[4-(CYCLOPENTYLAMINO)PHENYL]-1-(2-FLUORO-6- HETSYN 2 EFD METHYLBENZENE-1-CARBONYL)-N-[4-METHYL-3- HETSYN 3 EFD (TRIFLUOROMETHYL)PHENYL]PIPERIDINE-3-CARBOXAMIDE HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 1 YCM C5 H10 N2 O3 S FORMUL 2 ACE C2 H4 O FORMUL 2 ORN C5 H12 N2 O2 FORMUL 2 ZAL C9 H17 N O2 FORMUL 3 EFD C33 H35 F4 N3 O2 FORMUL 4 MLI 2(C3 H2 O4 2-) FORMUL 6 NA NA 1+ FORMUL 7 PGE C6 H14 O4 FORMUL 8 OLC 2(C21 H40 O4) FORMUL 10 OLA 4(C18 H34 O2) FORMUL 14 HOH *45(H2 O) HELIX 1 AA1 LEU B 12 LYS B 28 1 17 HELIX 2 AA2 ASN B 31 ALA B 49 1 19 HELIX 3 AA3 ASP B 69 GLY B 91 1 23 HELIX 4 AA4 LYS B 92 ASN B 108 1 17 HELIX 5 AA5 ARG B 120 ALA B 152 1 33 HELIX 6 AA6 THR B 155 LEU B 173 1 19 HELIX 7 AA7 ALA B 174 GLN B 184 1 11 HELIX 8 AA8 GLY B 191 LEU B 198 1 8 HELIX 9 AA9 SER B 200 LYS B 226 1 27 HELIX 10 AB1 LYS B 226 PHE B 233 1 8 HELIX 11 AB2 GLY B 235 TYR B 260 1 26 HELIX 12 AB3 ASP B 281 PHE B 297 1 17 HELIX 13 AB4 PHE B 297 SER B 317 1 21 HELIX 14 AB5 THR B 324 PHE B 353 1 30 HELIX 15 AB6 SER B 358 LEU B 367 1 10 HELIX 16 AB7 LEU B 367 TYR B 376 1 10 HELIX 17 AB8 ILE B 377 GLY B 392 1 16 HELIX 18 AB9 SER B 400 THR B 410 1 11 SHEET 1 AA1 3 ARG B 261 GLU B 266 0 SHEET 2 AA1 3 LYS B 271 VAL B 276 -1 O LYS B 271 N GLU B 266 SHEET 3 AA1 3 ORN L 2 PRO L 3 -1 O ORN L 2 N VAL B 276 SSBOND 1 CYS B 195 CYS B 274 1555 1555 2.05 LINK OD2 ASP B 168 NA NA B 504 1555 1555 2.73 LINK C TRP B 229 N YCM B 230 1555 1555 1.33 LINK C YCM B 230 N GLN B 231 1555 1555 1.33 LINK O ASN B 378 NA NA B 504 1555 1555 2.40 LINK OD1 ASN B 382 NA NA B 504 1555 1555 2.31 LINK C ACE L 0 N PHE L 1 1555 1555 1.33 LINK C PHE L 1 N ORN L 2 1555 1555 1.33 LINK NE ORN L 2 C ARG L 6 1555 1555 1.33 LINK C ORN L 2 N PRO L 3 1555 1555 1.34 LINK C PRO L 3 N ZAL L 4 1555 1555 1.33 LINK C ZAL L 4 N TRP L 5 1555 1555 1.33 LINK NA NA B 504 O HOH B 626 1555 1555 2.62 LINK NA NA B 504 O HOH B 635 1555 1555 2.31 LINK NA NA B 504 O HOH B 617 1555 1555 2.79 CISPEP 1 PHE B 268 PRO B 269 0 -1.06 SITE 1 AC1 15 LEU B 211 ALA B 214 THR B 215 ALA B 218 SITE 2 AC1 15 PHE B 221 ALA B 242 LEU B 249 LEU B 295 SITE 3 AC1 15 TRP B 299 THR B 303 LEU B 304 CYS B 307 SITE 4 AC1 15 OLA B 509 OLA B 511 HOH B 608 SITE 1 AC2 7 ASN B 157 ARG B 220 SER B 323 LYS B 325 SITE 2 AC2 7 THR B 326 GLU B 411 SER B 413 SITE 1 AC3 5 TYR B 207 LEU B 253 ARG B 292 OLC B 506 SITE 2 AC3 5 HOH B 612 SITE 1 AC4 6 ASP B 168 ASN B 378 ASN B 382 HOH B 617 SITE 2 AC4 6 HOH B 626 HOH B 635 SITE 1 AC5 2 ARG B 234 GLY B 235 SITE 1 AC6 4 PRO B 256 ARG B 284 VAL B 288 MLI B 503 SITE 1 AC7 3 TRP B 316 LYS B 328 PHE B 340 SITE 1 AC8 4 ILE B 290 LEU B 298 LEU B 301 LEU B 302 SITE 1 AC9 3 VAL B 294 TRP B 299 EFD B 501 SITE 1 AD1 2 TRP B 240 TRP B 247 SITE 1 AD2 2 TRP B 299 EFD B 501 CRYST1 58.411 52.608 83.865 90.00 106.08 90.00 P 1 21 1 2 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 0.017120 0.000000 0.004935 0.00000 SCALE2 0.000000 0.019009 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012409 0.00000 ATOM 1 N LEU B 12 -18.891 21.606 -9.717 1.00111.41 N ANISOU 1 N LEU B 12 15187 18722 8422 952 -2026 -73 N ATOM 2 CA LEU B 12 -18.963 20.454 -8.825 1.00108.63 C ANISOU 2 CA LEU B 12 14551 18467 8256 911 -1871 -344 C ATOM 3 C LEU B 12 -18.187 19.267 -9.386 1.00108.50 C ANISOU 3 C LEU B 12 14746 18491 7989 597 -1703 -593 C ATOM 4 O LEU B 12 -17.391 18.645 -8.681 1.00106.23 O ANISOU 4 O LEU B 12 14393 18104 7867 539 -1413 -825 O ATOM 5 CB LEU B 12 -20.418 20.054 -8.579 1.00110.20 C ANISOU 5 CB LEU B 12 14376 18899 8598 989 -2201 -270 C ATOM 6 CG LEU B 12 -20.615 18.810 -7.710 1.00107.98 C ANISOU 6 CG LEU B 12 13769 18757 8501 882 -2119 -463 C ATOM 7 CD1 LEU B 12 -19.951 18.996 -6.357 1.00105.18 C ANISOU 7 CD1 LEU B 12 13231 18300 8431 1017 -1775 -590 C ATOM 8 CD2 LEU B 12 -22.093 18.492 -7.546 1.00109.92 C ANISOU 8 CD2 LEU B 12 13618 19275 8873 932 -2467 -322 C ATOM 9 N GLU B 13 -18.428 18.955 -10.654 1.00111.91 N ANISOU 9 N GLU B 13 15423 19067 8031 401 -1908 -565 N ATOM 10 CA GLU B 13 -17.734 17.859 -11.317 1.00112.41 C ANISOU 10 CA GLU B 13 15696 19189 7827 134 -1776 -872 C ATOM 11 C GLU B 13 -16.252 18.181 -11.493 1.00113.87 C ANISOU 11 C GLU B 13 16144 19248 7875 72 -1356 -988 C ATOM 12 O GLU B 13 -15.408 17.284 -11.504 1.00114.90 O ANISOU 12 O GLU B 13 16324 19342 7991 -62 -1114 -1327 O ATOM 13 CB GLU B 13 -18.376 17.557 -12.672 1.00113.66 C ANISOU 13 CB GLU B 13 16073 19575 7539 -52 -2113 -831 C ATOM 14 N ASP B 14 -15.943 19.468 -11.625 1.00113.78 N ANISOU 14 N ASP B 14 16274 19152 7804 168 -1300 -698 N ATOM 15 CA ASP B 14 -14.564 19.915 -11.778 1.00112.03 C ANISOU 15 CA ASP B 14 16271 18822 7473 96 -924 -722 C ATOM 16 C ASP B 14 -13.815 19.842 -10.449 1.00107.87 C ANISOU 16 C ASP B 14 15544 18031 7409 228 -615 -877 C ATOM 17 O ASP B 14 -12.635 19.491 -10.412 1.00107.65 O ANISOU 17 O ASP B 14 15599 17926 7375 120 -270 -1082 O ATOM 18 CB ASP B 14 -14.520 21.340 -12.334 1.00114.00 C ANISOU 18 CB ASP B 14 16723 19034 7556 122 -1044 -293 C ATOM 19 N ASN B 15 -14.503 20.177 -9.361 1.00104.25 N ANISOU 19 N ASN B 15 14805 17463 7342 457 -742 -786 N ATOM 20 CA ASN B 15 -13.920 20.074 -8.029 1.00 99.46 C ANISOU 20 CA ASN B 15 13992 16655 7142 566 -494 -925 C ATOM 21 C ASN B 15 -13.633 18.626 -7.654 1.00 94.94 C ANISOU 21 C ASN B 15 13275 16110 6688 407 -374 -1249 C ATOM 22 O ASN B 15 -12.690 18.342 -6.915 1.00 91.86 O ANISOU 22 O ASN B 15 12826 15540 6535 379 -108 -1401 O ATOM 23 CB ASN B 15 -14.842 20.705 -6.982 1.00101.43 C ANISOU 23 CB ASN B 15 13946 16879 7712 846 -667 -797 C ATOM 24 CG ASN B 15 -14.810 22.220 -7.010 1.00105.15 C ANISOU 24 CG ASN B 15 14531 17173 8250 1056 -751 -543 C ATOM 25 OD1 ASN B 15 -13.804 22.825 -7.381 1.00107.87 O ANISOU 25 OD1 ASN B 15 15134 17337 8515 986 -595 -450 O ATOM 26 ND2 ASN B 15 -15.915 22.843 -6.609 1.00105.18 N ANISOU 26 ND2 ASN B 15 14313 17218 8432 1317 -1020 -427 N ATOM 27 N TRP B 16 -14.452 17.713 -8.167 1.00 95.39 N ANISOU 27 N TRP B 16 13270 16359 6613 293 -621 -1339 N ATOM 28 CA TRP B 16 -14.298 16.294 -7.868 1.00 94.00 C ANISOU 28 CA TRP B 16 12944 16168 6602 130 -615 -1629 C ATOM 29 C TRP B 16 -13.024 15.741 -8.500 1.00 92.04 C ANISOU 29 C TRP B 16 12924 15820 6226 -30 -343 -1932 C ATOM 30 O TRP B 16 -12.355 14.881 -7.922 1.00 88.83 O ANISOU 30 O TRP B 16 12392 15247 6113 -109 -211 -2173 O ATOM 31 CB TRP B 16 -15.522 15.510 -8.351 1.00 97.76 C ANISOU 31 CB TRP B 16 13313 16850 6981 38 -1009 -1633 C ATOM 32 CG TRP B 16 -15.538 14.077 -7.908 1.00 97.84 C ANISOU 32 CG TRP B 16 13113 16801 7259 -130 -1111 -1869 C ATOM 33 CD1 TRP B 16 -15.320 12.976 -8.685 1.00101.74 C ANISOU 33 CD1 TRP B 16 13728 17270 7657 -319 -1222 -2178 C ATOM 34 CD2 TRP B 16 -15.781 13.590 -6.582 1.00 93.76 C ANISOU 34 CD2 TRP B 16 12223 16240 7163 -141 -1151 -1807 C ATOM 35 NE1 TRP B 16 -15.416 11.834 -7.926 1.00101.16 N ANISOU 35 NE1 TRP B 16 13377 17074 7984 -443 -1371 -2295 N ATOM 36 CE2 TRP B 16 -15.697 12.184 -6.630 1.00 96.10 C ANISOU 36 CE2 TRP B 16 12428 16442 7644 -362 -1326 -2035 C ATOM 37 CE3 TRP B 16 -16.062 14.206 -5.358 1.00 89.07 C ANISOU 37 CE3 TRP B 16 11356 15693 6793 6 -1070 -1591 C ATOM 38 CZ2 TRP B 16 -15.885 11.385 -5.505 1.00 93.41 C ANISOU 38 CZ2 TRP B 16 11731 16051 7711 -481 -1447 -1975 C ATOM 39 CZ3 TRP B 16 -16.248 13.412 -4.241 1.00 88.07 C ANISOU 39 CZ3 TRP B 16 10877 15586 6999 -109 -1140 -1562 C ATOM 40 CH2 TRP B 16 -16.158 12.018 -4.322 1.00 90.88 C ANISOU 40 CH2 TRP B 16 11147 15843 7541 -370 -1338 -1715 C ATOM 41 N GLU B 17 -12.690 16.247 -9.685 1.00 92.77 N ANISOU 41 N GLU B 17 13329 16035 5884 -85 -269 -1908 N ATOM 42 CA GLU B 17 -11.461 15.862 -10.373 1.00 91.44 C ANISOU 42 CA GLU B 17 13357 15863 5523 -219 42 -2201 C ATOM 43 C GLU B 17 -10.246 16.484 -9.689 1.00 86.70 C ANISOU 43 C GLU B 17 12746 15037 5158 -161 417 -2146 C ATOM 44 O GLU B 17 -9.155 15.913 -9.703 1.00 80.63 O ANISOU 44 O GLU B 17 11977 14171 4488 -240 698 -2438 O ATOM 45 CB GLU B 17 -11.511 16.274 -11.849 1.00 96.46 C ANISOU 45 CB GLU B 17 14312 16796 5544 -331 14 -2145 C ATOM 46 N THR B 18 -10.446 17.657 -9.093 1.00 86.98 N ANISOU 46 N THR B 18 12758 14974 5316 -12 393 -1789 N ATOM 47 CA THR B 18 -9.399 18.330 -8.330 1.00 86.86 C ANISOU 47 CA THR B 18 12726 14709 5569 52 678 -1702 C ATOM 48 C THR B 18 -8.993 17.491 -7.122 1.00 82.96 C ANISOU 48 C THR B 18 11973 13996 5550 58 775 -1921 C ATOM 49 O THR B 18 -7.814 17.406 -6.775 1.00 81.43 O ANISOU 49 O THR B 18 11773 13611 5557 10 1056 -2033 O ATOM 50 CB THR B 18 -9.853 19.725 -7.856 1.00 85.25 C ANISOU 50 CB THR B 18 12531 14405 5457 242 542 -1321 C ATOM 51 OG1 THR B 18 -10.127 20.551 -8.995 1.00 90.06 O ANISOU 51 OG1 THR B 18 13384 15171 5666 201 411 -1056 O ATOM 52 CG2 THR B 18 -8.776 20.383 -7.011 1.00 81.92 C ANISOU 52 CG2 THR B 18 12095 13689 5340 302 789 -1254 C ATOM 53 N LEU B 19 -9.981 16.863 -6.495 1.00 81.64 N ANISOU 53 N LEU B 19 11577 13875 5568 90 519 -1948 N ATOM 54 CA LEU B 19 -9.737 16.004 -5.344 1.00 78.33 C ANISOU 54 CA LEU B 19 10891 13290 5579 42 536 -2089 C ATOM 55 C LEU B 19 -8.931 14.776 -5.739 1.00 76.88 C ANISOU 55 C LEU B 19 10709 13001 5500 -134 633 -2448 C ATOM 56 O LEU B 19 -7.942 14.437 -5.088 1.00 75.16 O ANISOU 56 O LEU B 19 10398 12543 5617 -184 816 -2568 O ATOM 57 CB LEU B 19 -11.056 15.573 -4.706 1.00 80.50 C ANISOU 57 CB LEU B 19 10895 13719 5972 67 214 -1989 C ATOM 58 CG LEU B 19 -11.945 16.677 -4.142 1.00 81.96 C ANISOU 58 CG LEU B 19 10982 14028 6131 283 107 -1707 C ATOM 59 CD1 LEU B 19 -13.249 16.080 -3.646 1.00 83.26 C ANISOU 59 CD1 LEU B 19 10830 14427 6378 272 -188 -1632 C ATOM 60 CD2 LEU B 19 -11.228 17.412 -3.024 1.00 78.93 C ANISOU 60 CD2 LEU B 19 10544 13455 5991 396 319 -1643 C ATOM 61 N ASN B 20 -9.363 14.113 -6.807 1.00 78.35 N ANISOU 61 N ASN B 20 10995 13355 5419 -217 484 -2640 N ATOM 62 CA ASN B 20 -8.706 12.901 -7.278 1.00 80.06 C ANISOU 62 CA ASN B 20 11205 13475 5739 -347 527 -3066 C ATOM 63 C ASN B 20 -7.317 13.176 -7.848 1.00 78.74 C ANISOU 63 C ASN B 20 11200 13260 5458 -356 937 -3260 C ATOM 64 O ASN B 20 -6.404 12.367 -7.686 1.00 76.01 O ANISOU 64 O ASN B 20 10748 12709 5422 -409 1072 -3585 O ATOM 65 CB ASN B 20 -9.572 12.202 -8.330 1.00 85.83 C ANISOU 65 CB ASN B 20 12027 14418 6167 -420 236 -3253 C ATOM 66 CG ASN B 20 -9.148 10.766 -8.572 1.00 90.60 C ANISOU 66 CG ASN B 20 12549 14858 7017 -530 143 -3734 C ATOM 67 OD1 ASN B 20 -8.497 10.146 -7.729 1.00 90.39 O ANISOU 67 OD1 ASN B 20 12318 14531 7496 -566 181 -3855 O ATOM 68 ND2 ASN B 20 -9.519 10.227 -9.726 1.00 96.21 N ANISOU 68 ND2 ASN B 20 13418 15748 7389 -584 -17 -4022 N ATOM 69 N ASP B 21 -7.160 14.316 -8.516 1.00 79.14 N ANISOU 69 N ASP B 21 11479 13500 5090 -315 1114 -3042 N ATOM 70 CA ASP B 21 -5.865 14.702 -9.076 1.00 82.13 C ANISOU 70 CA ASP B 21 11984 13879 5341 -348 1509 -3120 C ATOM 71 C ASP B 21 -4.821 14.909 -7.982 1.00 79.88 C ANISOU 71 C ASP B 21 11543 13287 5520 -324 1747 -3082 C ATOM 72 O ASP B 21 -3.698 14.411 -8.074 1.00 80.35 O ANISOU 72 O ASP B 21 11530 13205 5793 -362 1994 -3335 O ATOM 73 CB ASP B 21 -5.995 15.974 -9.916 1.00 83.78 C ANISOU 73 CB ASP B 21 12448 14307 5078 -343 1565 -2744 C ATOM 74 CG ASP B 21 -6.380 15.689 -11.355 1.00 91.62 C ANISOU 74 CG ASP B 21 13635 15553 5624 -410 1470 -2825 C ATOM 75 OD1 ASP B 21 -7.035 14.657 -11.613 1.00 94.76 O ANISOU 75 OD1 ASP B 21 13990 15988 6026 -431 1238 -3109 O ATOM 76 OD2 ASP B 21 -6.024 16.502 -12.232 1.00 94.82 O ANISOU 76 OD2 ASP B 21 14233 16134 5659 -463 1608 -2598 O ATOM 77 N ASN B 22 -5.194 15.650 -6.946 1.00 76.01 N ANISOU 77 N ASN B 22 10985 12641 5252 -235 1635 -2733 N ATOM 78 CA ASN B 22 -4.287 15.889 -5.834 1.00 74.84 C ANISOU 78 CA ASN B 22 10705 12178 5555 -218 1798 -2655 C ATOM 79 C ASN B 22 -4.107 14.635 -4.988 1.00 70.55 C ANISOU 79 C ASN B 22 9902 11403 5503 -283 1695 -2905 C ATOM 80 O ASN B 22 -3.106 14.491 -4.290 1.00 67.72 O ANISOU 80 O ASN B 22 9423 10774 5535 -320 1849 -2951 O ATOM 81 CB ASN B 22 -4.787 17.048 -4.976 1.00 74.91 C ANISOU 81 CB ASN B 22 10724 12111 5627 -89 1682 -2267 C ATOM 82 CG ASN B 22 -4.632 18.386 -5.666 1.00 79.66 C ANISOU 82 CG ASN B 22 11565 12803 5899 -42 1771 -1978 C ATOM 83 OD1 ASN B 22 -3.584 19.025 -5.576 1.00 82.27 O ANISOU 83 OD1 ASN B 22 11956 12978 6325 -71 1996 -1864 O ATOM 84 ND2 ASN B 22 -5.675 18.815 -6.368 1.00 80.86 N ANISOU 84 ND2 ASN B 22 11844 13192 5689 8 1558 -1824 N ATOM 85 N LEU B 23 -5.074 13.724 -5.064 1.00 70.18 N ANISOU 85 N LEU B 23 9759 11445 5460 -320 1395 -3036 N ATOM 86 CA LEU B 23 -4.980 12.463 -4.342 1.00 68.77 C ANISOU 86 CA LEU B 23 9326 11036 5766 -425 1213 -3233 C ATOM 87 C LEU B 23 -3.863 11.618 -4.933 1.00 71.76 C ANISOU 87 C LEU B 23 9681 11254 6331 -482 1391 -3667 C ATOM 88 O LEU B 23 -3.109 10.971 -4.204 1.00 71.89 O ANISOU 88 O LEU B 23 9499 10952 6865 -547 1389 -3784 O ATOM 89 CB LEU B 23 -6.308 11.704 -4.386 1.00 70.33 C ANISOU 89 CB LEU B 23 9422 11375 5924 -478 808 -3236 C ATOM 90 CG LEU B 23 -6.374 10.428 -3.542 1.00 72.32 C ANISOU 90 CG LEU B 23 9385 11388 6707 -632 520 -3329 C ATOM 91 CD1 LEU B 23 -5.935 10.704 -2.111 1.00 69.35 C ANISOU 91 CD1 LEU B 23 8827 10826 6698 -675 566 -3067 C ATOM 92 CD2 LEU B 23 -7.773 9.839 -3.561 1.00 75.13 C ANISOU 92 CD2 LEU B 23 9626 11923 6997 -707 101 -3230 C ATOM 93 N LYS B 24 -3.759 11.640 -6.259 1.00 72.94 N ANISOU 93 N LYS B 24 10021 11645 6050 -455 1538 -3911 N ATOM 94 CA LYS B 24 -2.691 10.940 -6.965 1.00 76.20 C ANISOU 94 CA LYS B 24 10404 11997 6549 -469 1770 -4392 C ATOM 95 C LYS B 24 -1.342 11.581 -6.657 1.00 77.94 C ANISOU 95 C LYS B 24 10585 12082 6945 -453 2171 -4314 C ATOM 96 O LYS B 24 -0.330 10.891 -6.536 1.00 76.00 O ANISOU 96 O LYS B 24 10161 11595 7121 -459 2296 -4613 O ATOM 97 CB LYS B 24 -2.947 10.942 -8.474 1.00 80.67 C ANISOU 97 CB LYS B 24 11191 12892 6570 -435 1816 -4541 C ATOM 98 N VAL B 25 -1.344 12.905 -6.528 1.00 79.06 N ANISOU 98 N VAL B 25 10879 12343 6818 -426 2322 -3879 N ATOM 99 CA VAL B 25 -0.145 13.659 -6.171 1.00 77.95 C ANISOU 99 CA VAL B 25 10711 12053 6854 -429 2642 -3701 C ATOM 100 C VAL B 25 0.409 13.202 -4.828 1.00 73.17 C ANISOU 100 C VAL B 25 9860 11014 6927 -460 2560 -3690 C ATOM 101 O VAL B 25 1.618 13.009 -4.680 1.00 74.02 O ANISOU 101 O VAL B 25 9830 10921 7373 -488 2791 -3833 O ATOM 102 CB VAL B 25 -0.433 15.174 -6.121 1.00 75.96 C ANISOU 102 CB VAL B 25 10664 11931 6266 -398 2690 -3205 C ATOM 103 CG1 VAL B 25 0.706 15.923 -5.440 1.00 72.53 C ANISOU 103 CG1 VAL B 25 10176 11243 6139 -416 2914 -2977 C ATOM 104 CG2 VAL B 25 -0.682 15.709 -7.528 1.00 78.40 C ANISOU 104 CG2 VAL B 25 11199 12607 5982 -395 2756 -3096 C ATOM 105 N ILE B 26 -0.486 13.018 -3.860 1.00 69.11 N ANISOU 105 N ILE B 26 9271 10383 6604 -470 2219 -3499 N ATOM 106 CA ILE B 26 -0.113 12.537 -2.532 1.00 68.50 C ANISOU 106 CA ILE B 26 8962 9943 7121 -546 2068 -3429 C ATOM 107 C ILE B 26 0.457 11.122 -2.605 1.00 69.30 C ANISOU 107 C ILE B 26 8841 9795 7696 -621 1981 -3841 C ATOM 108 O ILE B 26 1.446 10.803 -1.941 1.00 65.38 O ANISOU 108 O ILE B 26 8163 8965 7715 -682 2026 -3880 O ATOM 109 CB ILE B 26 -1.319 12.552 -1.564 1.00 66.33 C ANISOU 109 CB ILE B 26 8625 9716 6861 -569 1717 -3147 C ATOM 110 CG1 ILE B 26 -1.884 13.967 -1.430 1.00 63.78 C ANISOU 110 CG1 ILE B 26 8488 9597 6147 -446 1776 -2798 C ATOM 111 CG2 ILE B 26 -0.921 12.014 -0.197 1.00 62.79 C ANISOU 111 CG2 ILE B 26 7935 8954 6971 -701 1547 -3045 C ATOM 112 CD1 ILE B 26 -3.170 14.031 -0.643 1.00 59.06 C ANISOU 112 CD1 ILE B 26 7803 9155 5483 -426 1477 -2582 C ATOM 113 N GLU B 27 -0.176 10.285 -3.422 1.00 74.08 N ANISOU 113 N GLU B 27 9458 10536 8152 -613 1818 -4156 N ATOM 114 CA GLU B 27 0.249 8.902 -3.609 1.00 76.86 C ANISOU 114 CA GLU B 27 9607 10629 8968 -654 1665 -4615 C ATOM 115 C GLU B 27 1.676 8.808 -4.145 1.00 83.81 C ANISOU 115 C GLU B 27 10412 11403 10030 -588 2048 -4974 C ATOM 116 O GLU B 27 2.428 7.907 -3.775 1.00 87.20 O ANISOU 116 O GLU B 27 10590 11457 11086 -616 1956 -5239 O ATOM 117 CB GLU B 27 -0.713 8.178 -4.554 1.00 76.77 C ANISOU 117 CB GLU B 27 9675 10820 8673 -636 1427 -4918 C ATOM 118 N LYS B 28 2.045 9.746 -5.014 1.00 87.57 N ANISOU 118 N LYS B 28 11077 12220 9974 -511 2461 -4958 N ATOM 119 CA LYS B 28 3.386 9.776 -5.592 1.00 90.74 C ANISOU 119 CA LYS B 28 11381 12609 10486 -452 2815 -5130 C ATOM 120 C LYS B 28 4.173 10.994 -5.113 1.00 92.21 C ANISOU 120 C LYS B 28 11602 12777 10656 -485 3122 -4724 C ATOM 121 O LYS B 28 4.856 11.650 -5.901 1.00 95.54 O ANISOU 121 O LYS B 28 12090 13434 10776 -453 3421 -4607 O ATOM 122 CB LYS B 28 3.312 9.770 -7.121 1.00 93.38 C ANISOU 122 CB LYS B 28 11871 13348 10261 -362 2943 -5273 C ATOM 123 N ALA B 29 4.075 11.288 -3.819 1.00 88.68 N ANISOU 123 N ALA B 29 11105 12039 10552 -558 2968 -4421 N ATOM 124 CA ALA B 29 4.743 12.447 -3.236 1.00 86.02 C ANISOU 124 CA ALA B 29 10815 11615 10251 -591 3162 -3998 C ATOM 125 C ALA B 29 6.101 12.080 -2.641 1.00 86.27 C ANISOU 125 C ALA B 29 10573 11263 10944 -639 3278 -4091 C ATOM 126 O ALA B 29 6.288 10.981 -2.116 1.00 82.91 O ANISOU 126 O ALA B 29 9912 10509 11083 -674 3045 -4323 O ATOM 127 CB ALA B 29 3.861 13.085 -2.176 1.00 81.51 C ANISOU 127 CB ALA B 29 10359 10969 9641 -617 2870 -3545 C ATOM 128 N ASP B 30 7.042 13.016 -2.720 1.00 90.78 N ANISOU 128 N ASP B 30 11162 11857 11475 -659 3598 -3876 N ATOM 129 CA ASP B 30 8.402 12.779 -2.254 1.00 95.07 C ANISOU 129 CA ASP B 30 11429 12064 12629 -706 3741 -3937 C ATOM 130 C ASP B 30 8.609 13.280 -0.828 1.00 96.11 C ANISOU 130 C ASP B 30 11551 11812 13153 -807 3512 -3500 C ATOM 131 O ASP B 30 9.431 12.741 -0.089 1.00100.96 O ANISOU 131 O ASP B 30 11915 12036 14410 -878 3421 -3542 O ATOM 132 CB ASP B 30 9.410 13.446 -3.195 1.00 97.01 C ANISOU 132 CB ASP B 30 11645 12581 12631 -700 4232 -3954 C ATOM 133 N ASN B 31 7.866 14.310 -0.441 1.00 92.14 N ANISOU 133 N ASN B 31 11314 11419 12276 -809 3399 -3100 N ATOM 134 CA ASN B 31 8.007 14.868 0.899 1.00 89.64 C ANISOU 134 CA ASN B 31 11017 10794 12248 -889 3184 -2729 C ATOM 135 C ASN B 31 6.704 15.432 1.455 1.00 84.58 C ANISOU 135 C ASN B 31 10600 10294 11241 -846 2916 -2483 C ATOM 136 O ASN B 31 5.675 15.435 0.780 1.00 83.32 O ANISOU 136 O ASN B 31 10580 10455 10624 -757 2887 -2559 O ATOM 137 CB ASN B 31 9.083 15.954 0.905 1.00 93.80 C ANISOU 137 CB ASN B 31 11580 11219 12839 -929 3425 -2457 C ATOM 138 CG ASN B 31 8.813 17.045 -0.109 1.00 99.54 C ANISOU 138 CG ASN B 31 12555 12307 12960 -867 3648 -2288 C ATOM 139 OD1 ASN B 31 8.283 16.787 -1.190 1.00104.00 O ANISOU 139 OD1 ASN B 31 13187 13233 13093 -804 3777 -2494 O ATOM 140 ND2 ASN B 31 9.178 18.273 0.234 1.00100.05 N ANISOU 140 ND2 ASN B 31 12759 12257 12997 -902 3652 -1898 N ATOM 141 N ALA B 32 6.764 15.912 2.693 1.00 81.66 N ANISOU 141 N ALA B 32 10249 9701 11076 -905 2719 -2208 N ATOM 142 CA ALA B 32 5.588 16.427 3.385 1.00 77.56 C ANISOU 142 CA ALA B 32 9882 9328 10258 -847 2473 -2021 C ATOM 143 C ALA B 32 5.073 17.717 2.753 1.00 73.30 C ANISOU 143 C ALA B 32 9618 9021 9214 -692 2578 -1858 C ATOM 144 O ALA B 32 3.873 17.986 2.770 1.00 72.66 O ANISOU 144 O ALA B 32 9646 9179 8781 -582 2429 -1820 O ATOM 145 CB ALA B 32 5.902 16.651 4.859 1.00 76.55 C ANISOU 145 CB ALA B 32 9700 8936 10448 -953 2259 -1812 C ATOM 146 N ALA B 33 5.985 18.510 2.200 1.00 71.35 N ANISOU 146 N ALA B 33 9454 8694 8960 -696 2809 -1736 N ATOM 147 CA ALA B 33 5.621 19.775 1.572 1.00 72.56 C ANISOU 147 CA ALA B 33 9859 9008 8700 -589 2859 -1518 C ATOM 148 C ALA B 33 4.634 19.565 0.425 1.00 73.10 C ANISOU 148 C ALA B 33 10025 9473 8276 -505 2900 -1641 C ATOM 149 O ALA B 33 3.635 20.276 0.317 1.00 73.70 O ANISOU 149 O ALA B 33 10275 9706 8022 -381 2744 -1507 O ATOM 150 CB ALA B 33 6.864 20.495 1.077 1.00 76.85 C ANISOU 150 CB ALA B 33 10425 9424 9351 -677 3096 -1333 C ATOM 151 N GLN B 34 4.913 18.582 -0.424 1.00 71.52 N ANISOU 151 N GLN B 34 9702 9425 8045 -565 3087 -1921 N ATOM 152 CA GLN B 34 4.026 18.271 -1.541 1.00 72.50 C ANISOU 152 CA GLN B 34 9922 9932 7694 -509 3108 -2077 C ATOM 153 C GLN B 34 2.704 17.693 -1.046 1.00 67.63 C ANISOU 153 C GLN B 34 9284 9399 7014 -438 2797 -2169 C ATOM 154 O GLN B 34 1.638 18.030 -1.565 1.00 65.01 O ANISOU 154 O GLN B 34 9099 9332 6271 -350 2683 -2107 O ATOM 155 CB GLN B 34 4.702 17.303 -2.511 1.00 77.77 C ANISOU 155 CB GLN B 34 10446 10738 8363 -575 3376 -2435 C ATOM 156 CG GLN B 34 5.911 17.903 -3.208 1.00 83.90 C ANISOU 156 CG GLN B 34 11214 11582 9083 -656 3735 -2335 C ATOM 157 CD GLN B 34 6.664 16.901 -4.057 1.00 89.68 C ANISOU 157 CD GLN B 34 11743 12475 9858 -692 4034 -2768 C ATOM 158 OE1 GLN B 34 6.419 15.699 -3.979 1.00 94.65 O ANISOU 158 OE1 GLN B 34 12225 13042 10698 -652 3930 -3164 O ATOM 159 NE2 GLN B 34 7.589 17.392 -4.874 1.00 90.54 N ANISOU 159 NE2 GLN B 34 11821 12800 9780 -771 4395 -2700 N ATOM 160 N VAL B 35 2.777 16.824 -0.043 1.00 65.16 N ANISOU 160 N VAL B 35 8768 8870 7120 -500 2640 -2280 N ATOM 161 CA VAL B 35 1.575 16.267 0.564 1.00 63.37 C ANISOU 161 CA VAL B 35 8471 8744 6864 -482 2334 -2302 C ATOM 162 C VAL B 35 0.691 17.382 1.116 1.00 61.70 C ANISOU 162 C VAL B 35 8396 8645 6401 -351 2187 -2032 C ATOM 163 O VAL B 35 -0.511 17.418 0.853 1.00 59.38 O ANISOU 163 O VAL B 35 8145 8620 5797 -260 2036 -2021 O ATOM 164 CB VAL B 35 1.911 15.276 1.696 1.00 63.09 C ANISOU 164 CB VAL B 35 8182 8444 7344 -628 2157 -2361 C ATOM 165 CG1 VAL B 35 0.637 14.776 2.355 1.00 61.84 C ANISOU 165 CG1 VAL B 35 7926 8458 7111 -652 1838 -2306 C ATOM 166 CG2 VAL B 35 2.725 14.107 1.158 1.00 63.48 C ANISOU 166 CG2 VAL B 35 8059 8330 7730 -722 2242 -2680 C ATOM 167 N LYS B 36 1.305 18.294 1.867 1.00 63.69 N ANISOU 167 N LYS B 36 8705 8679 6814 -330 2216 -1839 N ATOM 168 CA LYS B 36 0.596 19.415 2.478 1.00 63.29 C ANISOU 168 CA LYS B 36 8772 8679 6596 -170 2065 -1648 C ATOM 169 C LYS B 36 -0.034 20.331 1.431 1.00 62.19 C ANISOU 169 C LYS B 36 8844 8732 6052 -16 2076 -1544 C ATOM 170 O LYS B 36 -1.189 20.735 1.565 1.00 61.05 O ANISOU 170 O LYS B 36 8728 8778 5691 142 1893 -1502 O ATOM 171 CB LYS B 36 1.544 20.219 3.375 1.00 66.05 C ANISOU 171 CB LYS B 36 9166 8703 7228 -186 2078 -1500 C ATOM 172 CG LYS B 36 0.992 21.568 3.819 1.00 69.56 C ANISOU 172 CG LYS B 36 9770 9138 7522 20 1930 -1355 C ATOM 173 CD LYS B 36 2.027 22.369 4.595 1.00 71.22 C ANISOU 173 CD LYS B 36 10051 8980 8027 -9 1916 -1229 C ATOM 174 CE LYS B 36 1.525 23.774 4.907 1.00 73.19 C ANISOU 174 CE LYS B 36 10479 9163 8168 226 1733 -1132 C ATOM 175 NZ LYS B 36 0.279 23.758 5.724 1.00 74.10 N ANISOU 175 NZ LYS B 36 10503 9539 8114 402 1551 -1275 N ATOM 176 N ASP B 37 0.730 20.654 0.390 1.00 63.94 N ANISOU 176 N ASP B 37 9190 8926 6178 -76 2280 -1485 N ATOM 177 CA ASP B 37 0.238 21.520 -0.676 1.00 65.64 C ANISOU 177 CA ASP B 37 9612 9326 6004 7 2265 -1321 C ATOM 178 C ASP B 37 -0.957 20.891 -1.381 1.00 62.79 C ANISOU 178 C ASP B 37 9242 9311 5303 51 2160 -1454 C ATOM 179 O ASP B 37 -1.963 21.555 -1.630 1.00 63.75 O ANISOU 179 O ASP B 37 9466 9576 5181 192 1969 -1322 O ATOM 180 CB ASP B 37 1.345 21.815 -1.689 1.00 73.42 C ANISOU 180 CB ASP B 37 10687 10305 6905 -136 2531 -1217 C ATOM 181 CG ASP B 37 0.840 22.589 -2.895 1.00 83.61 C ANISOU 181 CG ASP B 37 12184 11842 7742 -120 2495 -1006 C ATOM 182 OD1 ASP B 37 0.038 23.529 -2.707 1.00 88.30 O ANISOU 182 OD1 ASP B 37 12898 12393 8260 31 2232 -803 O ATOM 183 OD2 ASP B 37 1.237 22.254 -4.032 1.00 86.64 O ANISOU 183 OD2 ASP B 37 12598 12477 7845 -258 2714 -1053 O ATOM 184 N ALA B 38 -0.833 19.604 -1.695 1.00 60.33 N ANISOU 184 N ALA B 38 8800 9103 5021 -67 2250 -1723 N ATOM 185 CA ALA B 38 -1.904 18.860 -2.346 1.00 61.15 C ANISOU 185 CA ALA B 38 8884 9502 4846 -55 2119 -1878 C ATOM 186 C ALA B 38 -3.145 18.798 -1.463 1.00 59.45 C ANISOU 186 C ALA B 38 8554 9365 4670 58 1829 -1831 C ATOM 187 O ALA B 38 -4.266 18.956 -1.946 1.00 60.65 O ANISOU 187 O ALA B 38 8752 9759 4532 147 1657 -1780 O ATOM 188 CB ALA B 38 -1.434 17.459 -2.700 1.00 61.79 C ANISOU 188 CB ALA B 38 8826 9592 5061 -193 2222 -2219 C ATOM 189 N LEU B 39 -2.936 18.572 -0.169 1.00 57.07 N ANISOU 189 N LEU B 39 8082 8889 4712 40 1775 -1835 N ATOM 190 CA LEU B 39 -4.030 18.490 0.793 1.00 55.88 C ANISOU 190 CA LEU B 39 7768 8883 4580 120 1543 -1789 C ATOM 191 C LEU B 39 -4.733 19.826 0.989 1.00 56.41 C ANISOU 191 C LEU B 39 7936 9025 4473 360 1441 -1619 C ATOM 192 O LEU B 39 -5.929 19.873 1.279 1.00 56.76 O ANISOU 192 O LEU B 39 7861 9315 4389 481 1258 -1602 O ATOM 193 CB LEU B 39 -3.516 17.985 2.141 1.00 55.52 C ANISOU 193 CB LEU B 39 7526 8669 4902 1 1519 -1807 C ATOM 194 CG LEU B 39 -3.335 16.476 2.289 1.00 56.62 C ANISOU 194 CG LEU B 39 7457 8769 5288 -227 1448 -1952 C ATOM 195 CD1 LEU B 39 -2.663 16.168 3.614 1.00 57.81 C ANISOU 195 CD1 LEU B 39 7442 8711 5810 -372 1407 -1895 C ATOM 196 CD2 LEU B 39 -4.680 15.773 2.187 1.00 55.30 C ANISOU 196 CD2 LEU B 39 7139 8915 4957 -246 1211 -1965 C ATOM 197 N THR B 40 -3.981 20.911 0.845 1.00 57.59 N ANISOU 197 N THR B 40 8278 8949 4656 430 1537 -1495 N ATOM 198 CA THR B 40 -4.542 22.245 0.995 1.00 62.65 C ANISOU 198 CA THR B 40 9024 9566 5213 673 1390 -1351 C ATOM 199 C THR B 40 -5.497 22.529 -0.155 1.00 66.40 C ANISOU 199 C THR B 40 9599 10267 5364 762 1262 -1264 C ATOM 200 O THR B 40 -6.578 23.087 0.042 1.00 68.35 O ANISOU 200 O THR B 40 9792 10642 5537 978 1053 -1227 O ATOM 201 CB THR B 40 -3.446 23.320 1.037 1.00 64.76 C ANISOU 201 CB THR B 40 9482 9482 5643 686 1464 -1199 C ATOM 202 OG1 THR B 40 -2.521 23.018 2.087 1.00 63.51 O ANISOU 202 OG1 THR B 40 9232 9102 5795 580 1562 -1270 O ATOM 203 CG2 THR B 40 -4.055 24.692 1.277 1.00 69.12 C ANISOU 203 CG2 THR B 40 10129 9939 6193 960 1236 -1084 C ATOM 204 N LYS B 41 -5.092 22.125 -1.356 1.00 65.95 N ANISOU 204 N LYS B 41 9671 10278 5111 594 1384 -1248 N ATOM 205 CA LYS B 41 -5.921 22.289 -2.544 1.00 70.23 C ANISOU 205 CA LYS B 41 10328 11059 5296 618 1254 -1154 C ATOM 206 C LYS B 41 -7.148 21.384 -2.489 1.00 72.72 C ANISOU 206 C LYS B 41 10459 11662 5508 645 1085 -1293 C ATOM 207 O LYS B 41 -8.211 21.739 -2.998 1.00 75.89 O ANISOU 207 O LYS B 41 10881 12246 5706 758 867 -1191 O ATOM 208 CB LYS B 41 -5.108 22.003 -3.807 1.00 69.59 C ANISOU 208 CB LYS B 41 10420 11050 4972 403 1458 -1145 C ATOM 209 CG LYS B 41 -3.947 22.958 -4.011 1.00 69.83 C ANISOU 209 CG LYS B 41 10611 10857 5064 338 1612 -928 C ATOM 210 CD LYS B 41 -3.119 22.586 -5.227 1.00 71.65 C ANISOU 210 CD LYS B 41 10951 11263 5010 106 1871 -945 C ATOM 211 CE LYS B 41 -1.930 23.519 -5.367 1.00 75.41 C ANISOU 211 CE LYS B 41 11534 11546 5571 5 2030 -678 C ATOM 212 NZ LYS B 41 -1.122 23.224 -6.578 1.00 80.34 N ANISOU 212 NZ LYS B 41 12228 12439 5861 -230 2321 -681 N ATOM 213 N MET B 42 -6.997 20.216 -1.870 1.00 70.53 N ANISOU 213 N MET B 42 9985 11408 5405 522 1148 -1494 N ATOM 214 CA MET B 42 -8.118 19.296 -1.691 1.00 70.32 C ANISOU 214 CA MET B 42 9743 11637 5339 503 956 -1584 C ATOM 215 C MET B 42 -9.161 19.883 -0.747 1.00 71.05 C ANISOU 215 C MET B 42 9645 11864 5488 717 778 -1492 C ATOM 216 O MET B 42 -10.363 19.773 -0.989 1.00 73.76 O ANISOU 216 O MET B 42 9871 12469 5686 794 573 -1451 O ATOM 217 CB MET B 42 -7.643 17.944 -1.155 1.00 65.57 C ANISOU 217 CB MET B 42 8957 10974 4982 293 1011 -1772 C ATOM 218 CG MET B 42 -6.868 17.111 -2.152 1.00 62.68 C ANISOU 218 CG MET B 42 8704 10540 4573 115 1141 -1968 C ATOM 219 SD MET B 42 -6.580 15.425 -1.585 1.00 65.88 S ANISOU 219 SD MET B 42 8850 10833 5349 -108 1063 -2202 S ATOM 220 CE MET B 42 -8.227 14.737 -1.712 1.00 65.51 C ANISOU 220 CE MET B 42 8633 11100 5156 -130 697 -2165 C ATOM 221 N ARG B 43 -8.692 20.500 0.332 1.00 66.86 N ANISOU 221 N ARG B 43 9067 11171 5167 817 855 -1481 N ATOM 222 CA ARG B 43 -9.583 21.114 1.308 1.00 67.40 C ANISOU 222 CA ARG B 43 8937 11396 5276 1050 726 -1468 C ATOM 223 C ARG B 43 -10.401 22.229 0.667 1.00 70.85 C ANISOU 223 C ARG B 43 9470 11875 5574 1318 551 -1363 C ATOM 224 O ARG B 43 -11.617 22.305 0.848 1.00 71.96 O ANISOU 224 O ARG B 43 9397 12295 5651 1481 379 -1365 O ATOM 225 CB ARG B 43 -8.786 21.658 2.491 1.00 62.56 C ANISOU 225 CB ARG B 43 8315 10572 4884 1108 836 -1517 C ATOM 226 CG ARG B 43 -9.630 21.961 3.704 1.00 64.10 C ANISOU 226 CG ARG B 43 8238 11022 5095 1298 750 -1594 C ATOM 227 CD ARG B 43 -8.777 22.457 4.852 1.00 64.66 C ANISOU 227 CD ARG B 43 8333 10890 5345 1328 845 -1671 C ATOM 228 NE ARG B 43 -9.531 22.483 6.099 1.00 66.97 N ANISOU 228 NE ARG B 43 8324 11535 5588 1444 803 -1787 N ATOM 229 CZ ARG B 43 -10.317 23.485 6.474 1.00 71.83 C ANISOU 229 CZ ARG B 43 8850 12292 6148 1799 711 -1908 C ATOM 230 NH1 ARG B 43 -10.452 24.550 5.696 1.00 69.66 N ANISOU 230 NH1 ARG B 43 8779 11770 5918 2061 597 -1889 N ATOM 231 NH2 ARG B 43 -10.969 23.422 7.627 1.00 76.47 N ANISOU 231 NH2 ARG B 43 9126 13286 6643 1886 719 -2048 N ATOM 232 N ALA B 44 -9.721 23.085 -0.088 1.00 73.98 N ANISOU 232 N ALA B 44 10164 11998 5947 1346 574 -1243 N ATOM 233 CA ALA B 44 -10.370 24.198 -0.766 1.00 77.69 C ANISOU 233 CA ALA B 44 10752 12431 6335 1563 351 -1085 C ATOM 234 C ALA B 44 -11.409 23.693 -1.758 1.00 80.70 C ANISOU 234 C ALA B 44 11095 13105 6460 1514 181 -1015 C ATOM 235 O ALA B 44 -12.510 24.232 -1.841 1.00 85.79 O ANISOU 235 O ALA B 44 11626 13873 7095 1737 -65 -954 O ATOM 236 CB ALA B 44 -9.338 25.066 -1.470 1.00 79.15 C ANISOU 236 CB ALA B 44 11261 12285 6529 1498 392 -895 C ATOM 237 N ALA B 45 -11.055 22.647 -2.497 1.00 76.92 N ANISOU 237 N ALA B 45 10699 12730 5798 1232 293 -1052 N ATOM 238 CA ALA B 45 -11.944 22.074 -3.499 1.00 78.19 C ANISOU 238 CA ALA B 45 10860 13155 5692 1145 117 -1011 C ATOM 239 C ALA B 45 -13.128 21.362 -2.856 1.00 79.56 C ANISOU 239 C ALA B 45 10684 13615 5932 1205 -36 -1096 C ATOM 240 O ALA B 45 -14.216 21.310 -3.428 1.00 82.37 O ANISOU 240 O ALA B 45 10967 14183 6148 1252 -281 -1009 O ATOM 241 CB ALA B 45 -11.179 21.118 -4.392 1.00 76.03 C ANISOU 241 CB ALA B 45 10759 12909 5218 846 281 -1110 C ATOM 242 N ALA B 46 -12.913 20.811 -1.667 1.00 78.54 N ANISOU 242 N ALA B 46 10322 13509 6009 1174 93 -1231 N ATOM 243 CA ALA B 46 -13.965 20.085 -0.968 1.00 84.19 C ANISOU 243 CA ALA B 46 10663 14547 6777 1172 -35 -1264 C ATOM 244 C ALA B 46 -15.002 21.046 -0.389 1.00 89.70 C ANISOU 244 C ALA B 46 11133 15420 7528 1506 -172 -1218 C ATOM 245 O ALA B 46 -16.206 20.786 -0.444 1.00 95.46 O ANISOU 245 O ALA B 46 11601 16464 8207 1563 -366 -1164 O ATOM 246 CB ALA B 46 -13.371 19.214 0.130 1.00 82.33 C ANISOU 246 CB ALA B 46 10246 14307 6729 988 121 -1372 C ATOM 247 N LEU B 47 -14.526 22.155 0.166 1.00 86.22 N ANISOU 247 N LEU B 47 10775 14768 7218 1735 -87 -1258 N ATOM 248 CA LEU B 47 -15.410 23.170 0.723 1.00 85.62 C ANISOU 248 CA LEU B 47 10489 14806 7239 2110 -220 -1295 C ATOM 249 C LEU B 47 -16.097 23.966 -0.382 1.00 89.43 C ANISOU 249 C LEU B 47 11096 15213 7671 2285 -494 -1138 C ATOM 250 O LEU B 47 -17.220 24.437 -0.213 1.00 93.54 O ANISOU 250 O LEU B 47 11353 15927 8260 2559 -687 -1149 O ATOM 251 CB LEU B 47 -14.631 24.109 1.646 1.00 86.30 C ANISOU 251 CB LEU B 47 10651 14631 7510 2303 -92 -1429 C ATOM 252 CG LEU B 47 -14.099 23.480 2.936 1.00 82.79 C ANISOU 252 CG LEU B 47 10032 14306 7117 2166 131 -1578 C ATOM 253 CD1 LEU B 47 -13.276 24.479 3.734 1.00 82.74 C ANISOU 253 CD1 LEU B 47 10159 13998 7281 2350 216 -1713 C ATOM 254 CD2 LEU B 47 -15.247 22.938 3.772 1.00 83.39 C ANISOU 254 CD2 LEU B 47 9640 14920 7126 2215 105 -1650 C ATOM 255 N ASP B 48 -15.415 24.114 -1.512 1.00 90.90 N ANISOU 255 N ASP B 48 11663 15140 7734 2117 -517 -983 N ATOM 256 CA ASP B 48 -15.980 24.821 -2.655 1.00 96.25 C ANISOU 256 CA ASP B 48 12498 15749 8325 2204 -809 -766 C ATOM 257 C ASP B 48 -17.171 24.044 -3.211 1.00 95.72 C ANISOU 257 C ASP B 48 12237 16038 8096 2126 -1011 -703 C ATOM 258 O ASP B 48 -18.168 24.629 -3.630 1.00 97.75 O ANISOU 258 O ASP B 48 12394 16357 8389 2319 -1313 -575 O ATOM 259 CB ASP B 48 -14.921 25.030 -3.740 1.00 98.98 C ANISOU 259 CB ASP B 48 13278 15838 8490 1963 -752 -589 C ATOM 260 CG ASP B 48 -15.226 26.213 -4.638 1.00104.57 C ANISOU 260 CG ASP B 48 14179 16362 9191 2082 -1071 -308 C ATOM 261 OD1 ASP B 48 -16.417 26.541 -4.815 1.00107.66 O ANISOU 261 OD1 ASP B 48 14391 16872 9644 2280 -1382 -234 O ATOM 262 OD2 ASP B 48 -14.270 26.818 -5.167 1.00106.43 O ANISOU 262 OD2 ASP B 48 14724 16334 9380 1959 -1032 -131 O ATOM 263 N ALA B 49 -17.059 22.719 -3.199 1.00 91.96 N ANISOU 263 N ALA B 49 11694 15760 7486 1840 -881 -789 N ATOM 264 CA ALA B 49 -18.130 21.852 -3.673 1.00 90.73 C ANISOU 264 CA ALA B 49 11350 15921 7202 1722 -1095 -733 C ATOM 265 C ALA B 49 -19.308 21.851 -2.704 1.00 91.57 C ANISOU 265 C ALA B 49 10960 16344 7489 1941 -1194 -769 C ATOM 266 O ALA B 49 -19.126 21.958 -1.491 1.00 90.50 O ANISOU 266 O ALA B 49 10599 16275 7512 2061 -1001 -913 O ATOM 267 CB ALA B 49 -17.612 20.436 -3.878 1.00 87.37 C ANISOU 267 CB ALA B 49 10987 15556 6652 1358 -971 -840 C ATOM 268 N LYS B 68 -27.853 18.534 2.613 1.00108.23 N ANISOU 268 N LYS B 68 8720 22427 9975 2067 -1643 -313 N ATOM 269 CA LYS B 68 -27.603 18.151 3.998 1.00110.27 C ANISOU 269 CA LYS B 68 8648 23116 10136 1929 -1340 -364 C ATOM 270 C LYS B 68 -27.036 16.735 4.095 1.00110.31 C ANISOU 270 C LYS B 68 8758 23064 10092 1343 -1402 -132 C ATOM 271 O LYS B 68 -26.215 16.449 4.964 1.00108.90 O ANISOU 271 O LYS B 68 8626 22904 9848 1168 -1174 -191 O ATOM 272 CB LYS B 68 -28.880 18.267 4.828 1.00114.04 C ANISOU 272 CB LYS B 68 8355 24379 10596 2089 -1282 -323 C ATOM 273 N ASP B 69 -27.466 15.850 3.202 1.00118.80 N ANISOU 273 N ASP B 69 8843 23649 12645 -696 2276 -3345 N ATOM 274 CA ASP B 69 -26.826 14.547 3.121 1.00114.93 C ANISOU 274 CA ASP B 69 8658 22995 12015 -1275 2343 -2689 C ATOM 275 C ASP B 69 -25.513 14.648 2.348 1.00110.83 C ANISOU 275 C ASP B 69 8841 21459 11809 -1250 2160 -2636 C ATOM 276 O ASP B 69 -24.551 13.961 2.679 1.00108.39 O ANISOU 276 O ASP B 69 8871 20987 11326 -1525 2205 -2330 O ATOM 277 CB ASP B 69 -27.747 13.514 2.476 1.00114.07 C ANISOU 277 CB ASP B 69 8408 22970 11965 -1732 2282 -2123 C ATOM 278 N PHE B 70 -25.463 15.501 1.325 1.00109.97 N ANISOU 278 N PHE B 70 8970 20658 12157 -936 1918 -2925 N ATOM 279 CA PHE B 70 -24.209 15.704 0.603 1.00102.87 C ANISOU 279 CA PHE B 70 8716 18849 11522 -901 1729 -2891 C ATOM 280 C PHE B 70 -23.236 16.553 1.417 1.00102.05 C ANISOU 280 C PHE B 70 8728 18767 11281 -568 1763 -3293 C ATOM 281 O PHE B 70 -22.027 16.419 1.267 1.00101.19 O ANISOU 281 O PHE B 70 9091 18150 11208 -649 1711 -3150 O ATOM 282 CB PHE B 70 -24.451 16.350 -0.762 1.00 98.64 C ANISOU 282 CB PHE B 70 8409 17579 11491 -738 1423 -3038 C ATOM 283 N ARG B 71 -23.769 17.417 2.278 1.00103.73 N ANISOU 283 N ARG B 71 8502 19580 11329 -178 1831 -3796 N ATOM 284 CA ARG B 71 -22.940 18.268 3.126 1.00103.02 C ANISOU 284 CA ARG B 71 8508 19540 11095 182 1823 -4193 C ATOM 285 C ARG B 71 -22.183 17.433 4.142 1.00103.60 C ANISOU 285 C ARG B 71 8670 19930 10764 -117 2094 -3884 C ATOM 286 O ARG B 71 -21.020 17.706 4.434 1.00 99.17 O ANISOU 286 O ARG B 71 8484 19008 10188 -33 2047 -3928 O ATOM 287 CB ARG B 71 -23.795 19.314 3.840 1.00107.14 C ANISOU 287 CB ARG B 71 8511 20696 11500 702 1805 -4826 C ATOM 288 N HIS B 72 -22.857 16.417 4.676 1.00108.19 N ANISOU 288 N HIS B 72 8905 21182 11022 -494 2340 -3554 N ATOM 289 CA HIS B 72 -22.261 15.518 5.660 1.00106.40 C ANISOU 289 CA HIS B 72 8834 21150 10445 -860 2469 -3173 C ATOM 290 C HIS B 72 -21.069 14.766 5.085 1.00 99.82 C ANISOU 290 C HIS B 72 8529 19677 9722 -1196 2433 -2797 C ATOM 291 O HIS B 72 -20.025 14.660 5.726 1.00 96.16 O ANISOU 291 O HIS B 72 8339 19085 9112 -1246 2482 -2766 O ATOM 292 CB HIS B 72 -23.300 14.519 6.174 1.00108.60 C ANISOU 292 CB HIS B 72 8789 22033 10443 -1258 2534 -2771 C ATOM 293 N GLY B 73 -21.238 14.240 3.876 1.00 96.87 N ANISOU 293 N GLY B 73 8371 18788 9646 -1404 2263 -2482 N ATOM 294 CA GLY B 73 -20.182 13.507 3.203 1.00 89.78 C ANISOU 294 CA GLY B 73 8035 17174 8904 -1670 2123 -2111 C ATOM 295 C GLY B 73 -18.950 14.358 2.976 1.00 85.99 C ANISOU 295 C GLY B 73 7965 16082 8625 -1359 2020 -2379 C ATOM 296 O GLY B 73 -17.834 13.930 3.259 1.00 86.56 O ANISOU 296 O GLY B 73 8377 15895 8616 -1504 2028 -2216 O ATOM 297 N PHE B 74 -19.152 15.567 2.466 1.00 84.43 N ANISOU 297 N PHE B 74 7736 15651 8692 -946 1882 -2780 N ATOM 298 CA PHE B 74 -18.051 16.506 2.290 1.00 82.74 C ANISOU 298 CA PHE B 74 7876 14911 8651 -656 1724 -3028 C ATOM 299 C PHE B 74 -17.413 16.856 3.634 1.00 83.66 C ANISOU 299 C PHE B 74 7960 15349 8478 -498 1857 -3225 C ATOM 300 O PHE B 74 -16.197 17.021 3.733 1.00 81.29 O ANISOU 300 O PHE B 74 8032 14645 8211 -472 1794 -3188 O ATOM 301 CB PHE B 74 -18.535 17.777 1.592 1.00 86.60 C ANISOU 301 CB PHE B 74 8301 15150 9452 -268 1465 -3435 C ATOM 302 N ASP B 75 -18.246 16.965 4.664 1.00 88.26 N ANISOU 302 N ASP B 75 8085 16683 8768 -396 2039 -3428 N ATOM 303 CA ASP B 75 -17.783 17.263 6.016 1.00 88.04 C ANISOU 303 CA ASP B 75 7990 17039 8421 -247 2182 -3625 C ATOM 304 C ASP B 75 -16.863 16.170 6.555 1.00 84.34 C ANISOU 304 C ASP B 75 7795 16505 7747 -683 2324 -3212 C ATOM 305 O ASP B 75 -15.833 16.458 7.164 1.00 80.49 O ANISOU 305 O ASP B 75 7575 15812 7197 -587 2317 -3280 O ATOM 306 CB ASP B 75 -18.976 17.455 6.952 1.00 94.04 C ANISOU 306 CB ASP B 75 8225 18577 8930 -108 2285 -3817 C ATOM 307 CG ASP B 75 -19.470 18.888 6.978 1.00 98.01 C ANISOU 307 CG ASP B 75 8548 19113 9580 489 2065 -4377 C ATOM 308 OD1 ASP B 75 -18.674 19.796 6.659 1.00 98.76 O ANISOU 308 OD1 ASP B 75 8950 18693 9880 810 1839 -4637 O ATOM 309 OD2 ASP B 75 -20.649 19.110 7.324 1.00100.61 O ANISOU 309 OD2 ASP B 75 8443 19970 9812 631 2067 -4548 O ATOM 310 N ILE B 76 -17.243 14.917 6.326 1.00 85.70 N ANISOU 310 N ILE B 76 7913 16822 7826 -1164 2401 -2778 N ATOM 311 CA ILE B 76 -16.414 13.778 6.704 1.00 84.97 C ANISOU 311 CA ILE B 76 8109 16599 7577 -1612 2435 -2375 C ATOM 312 C ILE B 76 -15.119 13.789 5.901 1.00 81.12 C ANISOU 312 C ILE B 76 8168 15262 7391 -1582 2254 -2274 C ATOM 313 O ILE B 76 -14.060 13.399 6.396 1.00 81.55 O ANISOU 313 O ILE B 76 8519 15100 7366 -1729 2257 -2151 O ATOM 314 CB ILE B 76 -17.149 12.440 6.478 1.00 85.62 C ANISOU 314 CB ILE B 76 8051 16951 7529 -2131 2429 -1914 C ATOM 315 CG1 ILE B 76 -18.497 12.438 7.201 1.00 87.92 C ANISOU 315 CG1 ILE B 76 7829 17972 7604 -2144 2493 -1936 C ATOM 316 CG2 ILE B 76 -16.295 11.263 6.939 1.00 84.10 C ANISOU 316 CG2 ILE B 76 8176 16604 7175 -2591 2365 -1530 C ATOM 317 CD1 ILE B 76 -19.364 11.249 6.865 1.00 87.36 C ANISOU 317 CD1 ILE B 76 7608 18140 7443 -2617 2407 -1468 C ATOM 318 N LEU B 77 -15.212 14.253 4.659 1.00 76.82 N ANISOU 318 N LEU B 77 7740 14261 7186 -1399 2089 -2335 N ATOM 319 CA LEU B 77 -14.053 14.330 3.779 1.00 72.98 C ANISOU 319 CA LEU B 77 7716 13050 6964 -1366 1921 -2247 C ATOM 320 C LEU B 77 -13.059 15.383 4.261 1.00 69.53 C ANISOU 320 C LEU B 77 7464 12392 6564 -1045 1876 -2520 C ATOM 321 O LEU B 77 -11.859 15.121 4.346 1.00 64.00 O ANISOU 321 O LEU B 77 7098 11341 5877 -1136 1845 -2384 O ATOM 322 CB LEU B 77 -14.489 14.642 2.347 1.00 75.31 C ANISOU 322 CB LEU B 77 8063 12969 7583 -1273 1746 -2252 C ATOM 323 CG LEU B 77 -13.561 14.111 1.259 1.00 74.76 C ANISOU 323 CG LEU B 77 8412 12290 7703 -1425 1603 -1997 C ATOM 324 CD1 LEU B 77 -13.647 12.594 1.218 1.00 76.81 C ANISOU 324 CD1 LEU B 77 8745 12610 7830 -1823 1616 -1603 C ATOM 325 CD2 LEU B 77 -13.905 14.719 -0.091 1.00 73.99 C ANISOU 325 CD2 LEU B 77 8381 11814 7917 -1288 1420 -2073 C ATOM 326 N VAL B 78 -13.572 16.571 4.576 1.00 71.75 N ANISOU 326 N VAL B 78 7525 12874 6863 -658 1832 -2907 N ATOM 327 CA VAL B 78 -12.744 17.686 5.027 1.00 72.52 C ANISOU 327 CA VAL B 78 7800 12753 7002 -311 1700 -3173 C ATOM 328 C VAL B 78 -11.999 17.352 6.319 1.00 72.86 C ANISOU 328 C VAL B 78 7938 12969 6776 -397 1862 -3117 C ATOM 329 O VAL B 78 -10.801 17.618 6.437 1.00 72.31 O ANISOU 329 O VAL B 78 8210 12486 6778 -349 1765 -3066 O ATOM 330 CB VAL B 78 -13.588 18.961 5.237 1.00 76.04 C ANISOU 330 CB VAL B 78 7963 13445 7482 149 1558 -3641 C ATOM 331 CG1 VAL B 78 -12.770 20.045 5.926 1.00 76.11 C ANISOU 331 CG1 VAL B 78 8161 13281 7476 513 1374 -3900 C ATOM 332 CG2 VAL B 78 -14.128 19.457 3.903 1.00 73.82 C ANISOU 332 CG2 VAL B 78 7678 12839 7530 240 1307 -3719 C ATOM 333 N GLY B 79 -12.709 16.764 7.278 1.00 70.95 N ANISOU 333 N GLY B 79 7391 13347 6219 -554 2095 -3105 N ATOM 334 CA GLY B 79 -12.102 16.346 8.529 1.00 69.51 C ANISOU 334 CA GLY B 79 7295 13352 5763 -710 2243 -3026 C ATOM 335 C GLY B 79 -10.957 15.373 8.320 1.00 68.25 C ANISOU 335 C GLY B 79 7536 12726 5669 -1084 2217 -2658 C ATOM 336 O GLY B 79 -9.916 15.476 8.972 1.00 68.02 O ANISOU 336 O GLY B 79 7778 12460 5606 -1073 2205 -2646 O ATOM 337 N GLN B 80 -11.149 14.430 7.401 1.00 64.32 N ANISOU 337 N GLN B 80 7084 12078 5277 -1393 2176 -2369 N ATOM 338 CA GLN B 80 -10.107 13.472 7.044 1.00 64.71 C ANISOU 338 CA GLN B 80 7504 11671 5410 -1698 2089 -2061 C ATOM 339 C GLN B 80 -8.922 14.157 6.375 1.00 60.23 C ANISOU 339 C GLN B 80 7277 10492 5114 -1458 1942 -2121 C ATOM 340 O GLN B 80 -7.781 13.716 6.512 1.00 59.06 O ANISOU 340 O GLN B 80 7432 10012 4996 -1589 1896 -1980 O ATOM 341 CB GLN B 80 -10.667 12.392 6.120 1.00 63.61 C ANISOU 341 CB GLN B 80 7339 11505 5326 -2007 2014 -1774 C ATOM 342 CG GLN B 80 -11.519 11.354 6.820 1.00 68.56 C ANISOU 342 CG GLN B 80 7729 12664 5658 -2409 2080 -1559 C ATOM 343 CD GLN B 80 -12.118 10.358 5.851 1.00 69.61 C ANISOU 343 CD GLN B 80 7859 12724 5865 -2682 1929 -1254 C ATOM 344 OE1 GLN B 80 -12.279 10.651 4.669 1.00 72.46 O ANISOU 344 OE1 GLN B 80 8278 12771 6484 -2502 1843 -1278 O ATOM 345 NE2 GLN B 80 -12.444 9.174 6.344 1.00 70.69 N ANISOU 345 NE2 GLN B 80 7955 13133 5773 -3137 1851 -947 N ATOM 346 N ILE B 81 -9.202 15.230 5.642 1.00 58.56 N ANISOU 346 N ILE B 81 7005 10148 5096 -1129 1837 -2322 N ATOM 347 CA ILE B 81 -8.151 16.031 5.026 1.00 56.56 C ANISOU 347 CA ILE B 81 7035 9387 5067 -924 1654 -2363 C ATOM 348 C ILE B 81 -7.355 16.751 6.107 1.00 55.92 C ANISOU 348 C ILE B 81 7086 9251 4908 -729 1635 -2496 C ATOM 349 O ILE B 81 -6.130 16.777 6.069 1.00 57.26 O ANISOU 349 O ILE B 81 7553 9043 5161 -756 1555 -2375 O ATOM 350 CB ILE B 81 -8.726 17.058 4.022 1.00 59.70 C ANISOU 350 CB ILE B 81 7340 9663 5680 -664 1468 -2543 C ATOM 351 CG1 ILE B 81 -9.349 16.338 2.825 1.00 57.65 C ANISOU 351 CG1 ILE B 81 7029 9339 5536 -868 1461 -2373 C ATOM 352 CG2 ILE B 81 -7.647 18.025 3.552 1.00 57.64 C ANISOU 352 CG2 ILE B 81 7353 8947 5600 -482 1224 -2571 C ATOM 353 CD1 ILE B 81 -9.915 17.262 1.775 1.00 59.13 C ANISOU 353 CD1 ILE B 81 7157 9355 5955 -677 1255 -2528 C ATOM 354 N ASP B 82 -8.059 17.316 7.082 1.00 61.99 N ANISOU 354 N ASP B 82 7627 10419 5506 -522 1701 -2746 N ATOM 355 CA ASP B 82 -7.414 17.989 8.208 1.00 66.26 C ANISOU 355 CA ASP B 82 8298 10934 5945 -309 1669 -2887 C ATOM 356 C ASP B 82 -6.591 17.023 9.055 1.00 65.05 C ANISOU 356 C ASP B 82 8342 10728 5645 -631 1819 -2663 C ATOM 357 O ASP B 82 -5.532 17.387 9.563 1.00 56.31 O ANISOU 357 O ASP B 82 7514 9304 4578 -547 1736 -2638 O ATOM 358 CB ASP B 82 -8.455 18.687 9.084 1.00 73.07 C ANISOU 358 CB ASP B 82 8835 12323 6605 -4 1719 -3239 C ATOM 359 CG ASP B 82 -9.161 19.816 8.361 1.00 79.23 C ANISOU 359 CG ASP B 82 9460 13085 7558 383 1474 -3532 C ATOM 360 OD1 ASP B 82 -8.523 20.468 7.505 1.00 74.99 O ANISOU 360 OD1 ASP B 82 9167 12041 7284 495 1186 -3495 O ATOM 361 OD2 ASP B 82 -10.354 20.050 8.650 1.00 87.05 O ANISOU 361 OD2 ASP B 82 10073 14586 8414 557 1546 -3801 O ATOM 362 N ASP B 83 -7.087 15.800 9.215 1.00 64.24 N ANISOU 362 N ASP B 83 8108 10917 5383 -1016 1993 -2488 N ATOM 363 CA ASP B 83 -6.335 14.749 9.892 1.00 60.42 C ANISOU 363 CA ASP B 83 7835 10335 4788 -1390 2055 -2260 C ATOM 364 C ASP B 83 -5.014 14.486 9.173 1.00 56.28 C ANISOU 364 C ASP B 83 7678 9197 4511 -1457 1908 -2079 C ATOM 365 O ASP B 83 -3.950 14.483 9.786 1.00 52.19 O ANISOU 365 O ASP B 83 7425 8392 4012 -1488 1871 -2029 O ATOM 366 CB ASP B 83 -7.160 13.464 9.967 1.00 65.66 C ANISOU 366 CB ASP B 83 8304 11383 5260 -1825 2151 -2066 C ATOM 367 CG ASP B 83 -7.637 13.158 11.369 1.00 78.38 C ANISOU 367 CG ASP B 83 9738 13420 6622 -1980 2232 -2035 C ATOM 368 OD1 ASP B 83 -7.656 14.082 12.210 1.00 84.73 O ANISOU 368 OD1 ASP B 83 10482 14337 7374 -1664 2267 -2237 O ATOM 369 OD2 ASP B 83 -8.003 11.994 11.630 1.00 84.57 O ANISOU 369 OD2 ASP B 83 10452 14410 7269 -2416 2212 -1796 O ATOM 370 N ALA B 84 -5.096 14.272 7.863 1.00 52.07 N ANISOU 370 N ALA B 84 7144 8484 4157 -1473 1823 -1990 N ATOM 371 CA ALA B 84 -3.915 14.061 7.041 1.00 49.00 C ANISOU 371 CA ALA B 84 7037 7609 3970 -1502 1694 -1848 C ATOM 372 C ALA B 84 -3.039 15.309 7.029 1.00 48.79 C ANISOU 372 C ALA B 84 7170 7283 4085 -1192 1578 -1937 C ATOM 373 O ALA B 84 -1.811 15.217 7.044 1.00 48.35 O ANISOU 373 O ALA B 84 7365 6888 4118 -1229 1507 -1825 O ATOM 374 CB ALA B 84 -4.318 13.678 5.628 1.00 48.57 C ANISOU 374 CB ALA B 84 6922 7491 4042 -1550 1630 -1763 C ATOM 375 N LEU B 85 -3.682 16.472 7.011 1.00 49.58 N ANISOU 375 N LEU B 85 7122 7512 4204 -888 1513 -2137 N ATOM 376 CA LEU B 85 -2.976 17.748 6.957 1.00 53.23 C ANISOU 376 CA LEU B 85 7740 7690 4797 -592 1297 -2206 C ATOM 377 C LEU B 85 -2.189 17.987 8.242 1.00 53.02 C ANISOU 377 C LEU B 85 7907 7549 4688 -530 1295 -2210 C ATOM 378 O LEU B 85 -1.083 18.526 8.209 1.00 52.04 O ANISOU 378 O LEU B 85 8028 7059 4687 -444 1122 -2108 O ATOM 379 CB LEU B 85 -3.965 18.890 6.706 1.00 61.41 C ANISOU 379 CB LEU B 85 8576 8888 5867 -273 1145 -2461 C ATOM 380 CG LEU B 85 -3.433 20.202 6.128 1.00 64.13 C ANISOU 380 CG LEU B 85 9070 8902 6395 -18 782 -2497 C ATOM 381 CD1 LEU B 85 -2.424 19.936 5.028 1.00 58.35 C ANISOU 381 CD1 LEU B 85 8520 7838 5812 -222 700 -2223 C ATOM 382 CD2 LEU B 85 -4.587 21.035 5.595 1.00 68.12 C ANISOU 382 CD2 LEU B 85 9358 9558 6966 215 597 -2753 C ATOM 383 N LYS B 86 -2.761 17.578 9.372 1.00 53.73 N ANISOU 383 N LYS B 86 7887 7966 4561 -597 1477 -2307 N ATOM 384 CA LYS B 86 -2.068 17.659 10.654 1.00 52.04 C ANISOU 384 CA LYS B 86 7874 7649 4248 -588 1497 -2302 C ATOM 385 C LYS B 86 -0.806 16.797 10.657 1.00 54.72 C ANISOU 385 C LYS B 86 8503 7602 4686 -886 1500 -2046 C ATOM 386 O LYS B 86 0.246 17.230 11.128 1.00 54.02 O ANISOU 386 O LYS B 86 8682 7160 4683 -802 1384 -1976 O ATOM 387 CB LYS B 86 -2.993 17.233 11.797 1.00 55.99 C ANISOU 387 CB LYS B 86 8168 8658 4450 -686 1714 -2436 C ATOM 388 CG LYS B 86 -2.356 17.300 13.182 1.00 55.64 C ANISOU 388 CG LYS B 86 8339 8527 4274 -699 1740 -2442 C ATOM 389 CD LYS B 86 -3.305 16.783 14.250 1.00 66.17 C ANISOU 389 CD LYS B 86 9414 10401 5327 -841 1923 -2488 C ATOM 390 CE LYS B 86 -2.799 17.101 15.653 1.00 75.57 C ANISOU 390 CE LYS B 86 10793 11514 6404 -754 1904 -2515 C ATOM 391 NZ LYS B 86 -1.445 16.534 15.905 1.00 76.36 N ANISOU 391 NZ LYS B 86 11293 11077 6643 -1036 1840 -2290 N ATOM 392 N LEU B 87 -0.915 15.580 10.131 1.00 53.98 N ANISOU 392 N LEU B 87 8360 7563 4587 -1217 1593 -1912 N ATOM 393 CA LEU B 87 0.227 14.675 10.050 1.00 53.71 C ANISOU 393 CA LEU B 87 8575 7182 4651 -1474 1550 -1723 C ATOM 394 C LEU B 87 1.323 15.229 9.147 1.00 52.98 C ANISOU 394 C LEU B 87 8640 6705 4786 -1314 1395 -1629 C ATOM 395 O LEU B 87 2.507 15.164 9.480 1.00 55.61 O ANISOU 395 O LEU B 87 9212 6705 5213 -1356 1323 -1524 O ATOM 396 CB LEU B 87 -0.210 13.297 9.547 1.00 53.48 C ANISOU 396 CB LEU B 87 8458 7293 4568 -1809 1589 -1629 C ATOM 397 CG LEU B 87 -0.960 12.417 10.548 1.00 55.15 C ANISOU 397 CG LEU B 87 8582 7835 4538 -2130 1677 -1614 C ATOM 398 CD1 LEU B 87 -1.410 11.118 9.895 1.00 53.08 C ANISOU 398 CD1 LEU B 87 8256 7670 4242 -2447 1607 -1482 C ATOM 399 CD2 LEU B 87 -0.086 12.139 11.762 1.00 54.14 C ANISOU 399 CD2 LEU B 87 8717 7485 4370 -2304 1646 -1573 C ATOM 400 N ALA B 88 0.924 15.769 8.000 1.00 47.68 N ANISOU 400 N ALA B 88 7824 6096 4194 -1159 1333 -1653 N ATOM 401 CA ALA B 88 1.875 16.335 7.055 1.00 46.39 C ANISOU 401 CA ALA B 88 7764 5661 4200 -1054 1173 -1540 C ATOM 402 C ALA B 88 2.566 17.561 7.655 1.00 48.40 C ANISOU 402 C ALA B 88 8185 5688 4517 -828 994 -1517 C ATOM 403 O ALA B 88 3.768 17.750 7.473 1.00 53.05 O ANISOU 403 O ALA B 88 8946 5996 5214 -841 876 -1349 O ATOM 404 CB ALA B 88 1.178 16.689 5.744 1.00 45.33 C ANISOU 404 CB ALA B 88 7447 5659 4117 -978 1117 -1572 C ATOM 405 N ASN B 89 1.808 18.382 8.380 1.00 47.59 N ANISOU 405 N ASN B 89 8026 5721 4336 -609 947 -1686 N ATOM 406 CA ASN B 89 2.376 19.531 9.083 1.00 49.18 C ANISOU 406 CA ASN B 89 8420 5689 4578 -359 714 -1680 C ATOM 407 C ASN B 89 3.381 19.128 10.158 1.00 51.76 C ANISOU 407 C ASN B 89 9008 5756 4905 -470 763 -1560 C ATOM 408 O ASN B 89 4.310 19.871 10.452 1.00 50.28 O ANISOU 408 O ASN B 89 9048 5241 4816 -345 541 -1428 O ATOM 409 CB ASN B 89 1.269 20.375 9.714 1.00 56.53 C ANISOU 409 CB ASN B 89 9222 6864 5392 -58 645 -1955 C ATOM 410 CG ASN B 89 0.631 21.330 8.726 1.00 64.49 C ANISOU 410 CG ASN B 89 10086 7934 6483 155 394 -2065 C ATOM 411 OD1 ASN B 89 1.313 21.932 7.896 1.00 63.37 O ANISOU 411 OD1 ASN B 89 10057 7531 6490 167 121 -1898 O ATOM 412 ND2 ASN B 89 -0.686 21.474 8.809 1.00 70.46 N ANISOU 412 ND2 ASN B 89 10582 9053 7137 301 462 -2341 N ATOM 413 N GLU B 90 3.189 17.951 10.744 1.00 55.76 N ANISOU 413 N GLU B 90 9495 6387 5306 -730 1010 -1586 N ATOM 414 CA GLU B 90 4.120 17.430 11.739 1.00 60.59 C ANISOU 414 CA GLU B 90 10368 6720 5933 -898 1039 -1481 C ATOM 415 C GLU B 90 5.382 16.907 11.066 1.00 64.69 C ANISOU 415 C GLU B 90 11025 6919 6635 -1061 975 -1275 C ATOM 416 O GLU B 90 6.413 16.728 11.713 1.00 70.85 O ANISOU 416 O GLU B 90 12018 7383 7519 -1135 911 -1138 O ATOM 417 CB GLU B 90 3.471 16.316 12.564 1.00 64.73 C ANISOU 417 CB GLU B 90 10830 7494 6271 -1183 1255 -1567 C ATOM 418 CG GLU B 90 2.344 16.768 13.473 1.00 71.48 C ANISOU 418 CG GLU B 90 11536 8733 6891 -1045 1352 -1772 C ATOM 419 CD GLU B 90 1.599 15.598 14.089 1.00 78.40 C ANISOU 419 CD GLU B 90 12280 9965 7542 -1410 1553 -1806 C ATOM 420 OE1 GLU B 90 1.935 14.438 13.760 1.00 78.22 O ANISOU 420 OE1 GLU B 90 12305 9836 7579 -1756 1556 -1666 O ATOM 421 OE2 GLU B 90 0.678 15.836 14.901 1.00 83.30 O ANISOU 421 OE2 GLU B 90 12717 10990 7943 -1338 1654 -1949 O ATOM 422 N GLY B 91 5.288 16.657 9.763 1.00 74.99 N ANISOU 422 N GLY B 91 13238 6968 8287 524 -1303 -994 N ATOM 423 CA GLY B 91 6.413 16.158 8.993 1.00 72.29 C ANISOU 423 CA GLY B 91 12481 6650 8336 413 -1320 -1147 C ATOM 424 C GLY B 91 6.361 14.661 8.753 1.00 72.23 C ANISOU 424 C GLY B 91 12225 6545 8674 298 -1066 -1536 C ATOM 425 O GLY B 91 7.308 14.074 8.230 1.00 77.55 O ANISOU 425 O GLY B 91 12545 7184 9737 266 -1092 -1764 O ATOM 426 N LYS B 92 5.253 14.037 9.133 1.00 67.21 N ANISOU 426 N LYS B 92 11760 5887 7890 235 -857 -1631 N ATOM 427 CA LYS B 92 5.103 12.595 8.977 1.00 66.58 C ANISOU 427 CA LYS B 92 11543 5667 8089 99 -736 -1950 C ATOM 428 C LYS B 92 4.488 12.257 7.623 1.00 68.79 C ANISOU 428 C LYS B 92 11326 6542 8270 1 -388 -2273 C ATOM 429 O LYS B 92 3.270 12.151 7.494 1.00 69.40 O ANISOU 429 O LYS B 92 11417 6891 8062 -91 -150 -2297 O ATOM 430 CB LYS B 92 4.253 12.023 10.116 1.00 67.49 C ANISOU 430 CB LYS B 92 12136 5451 8055 -26 -745 -1835 C ATOM 431 CG LYS B 92 4.836 12.286 11.497 1.00 72.75 C ANISOU 431 CG LYS B 92 13393 5458 8791 11 -1105 -1515 C ATOM 432 CD LYS B 92 3.872 11.899 12.604 1.00 77.58 C ANISOU 432 CD LYS B 92 14418 5957 9100 -196 -1032 -1359 C ATOM 433 CE LYS B 92 4.438 12.264 13.968 1.00 78.48 C ANISOU 433 CE LYS B 92 14757 5839 9222 -166 -1284 -913 C ATOM 434 NZ LYS B 92 3.466 12.001 15.060 1.00 80.10 N ANISOU 434 NZ LYS B 92 15443 5974 9017 -408 -1192 -796 N ATOM 435 N VAL B 93 5.341 12.082 6.619 1.00 70.03 N ANISOU 435 N VAL B 93 11038 6905 8664 5 -359 -2532 N ATOM 436 CA VAL B 93 4.893 11.895 5.243 1.00 71.23 C ANISOU 436 CA VAL B 93 10756 7623 8686 -112 -45 -2828 C ATOM 437 C VAL B 93 4.130 10.589 5.030 1.00 71.26 C ANISOU 437 C VAL B 93 10727 7566 8783 -191 88 -3091 C ATOM 438 O VAL B 93 3.039 10.590 4.462 1.00 68.91 O ANISOU 438 O VAL B 93 10364 7603 8216 -307 327 -3117 O ATOM 439 CB VAL B 93 6.078 11.926 4.261 1.00 76.11 C ANISOU 439 CB VAL B 93 10897 8514 9507 -126 -17 -3095 C ATOM 440 CG1 VAL B 93 5.570 11.988 2.832 1.00 77.81 C ANISOU 440 CG1 VAL B 93 10759 9344 9461 -317 307 -3338 C ATOM 441 CG2 VAL B 93 6.981 13.113 4.558 1.00 76.31 C ANISOU 441 CG2 VAL B 93 10968 8549 9476 -98 -243 -2781 C ATOM 442 N LYS B 94 4.709 9.480 5.479 1.00 73.90 N ANISOU 442 N LYS B 94 11127 7433 9518 -139 -147 -3279 N ATOM 443 CA LYS B 94 4.094 8.170 5.276 1.00 77.35 C ANISOU 443 CA LYS B 94 11579 7754 10055 -228 -168 -3518 C ATOM 444 C LYS B 94 2.744 8.060 5.984 1.00 74.24 C ANISOU 444 C LYS B 94 11556 7326 9327 -418 -101 -3224 C ATOM 445 O LYS B 94 1.786 7.518 5.431 1.00 74.89 O ANISOU 445 O LYS B 94 11555 7642 9257 -553 60 -3301 O ATOM 446 CB LYS B 94 5.031 7.057 5.756 1.00 83.16 C ANISOU 446 CB LYS B 94 12393 7893 11310 -136 -611 -3777 C ATOM 447 N GLU B 95 2.670 8.585 7.203 1.00 73.34 N ANISOU 447 N GLU B 95 11842 6940 9083 -442 -218 -2891 N ATOM 448 CA GLU B 95 1.439 8.527 7.983 1.00 73.17 C ANISOU 448 CA GLU B 95 12137 6961 8701 -648 -111 -2647 C ATOM 449 C GLU B 95 0.353 9.406 7.362 1.00 72.04 C ANISOU 449 C GLU B 95 11759 7438 8175 -633 285 -2589 C ATOM 450 O GLU B 95 -0.828 9.054 7.372 1.00 77.71 O ANISOU 450 O GLU B 95 12472 8388 8666 -815 467 -2555 O ATOM 451 CB GLU B 95 1.705 8.945 9.431 1.00 69.40 C ANISOU 451 CB GLU B 95 12165 6061 8144 -672 -318 -2345 C ATOM 452 N ALA B 96 0.764 10.547 6.817 1.00 62.13 N ANISOU 452 N ALA B 96 10312 6434 6861 -446 352 -2577 N ATOM 453 CA ALA B 96 -0.156 11.450 6.135 1.00 58.53 C ANISOU 453 CA ALA B 96 9654 6485 6100 -431 583 -2566 C ATOM 454 C ALA B 96 -0.715 10.824 4.856 1.00 60.65 C ANISOU 454 C ALA B 96 9590 7048 6406 -573 776 -2803 C ATOM 455 O ALA B 96 -1.886 11.011 4.530 1.00 60.29 O ANISOU 455 O ALA B 96 9452 7294 6160 -657 952 -2796 O ATOM 456 CB ALA B 96 0.535 12.763 5.817 1.00 55.49 C ANISOU 456 CB ALA B 96 9213 6231 5638 -275 455 -2479 C ATOM 457 N GLN B 97 0.127 10.092 4.133 1.00 64.85 N ANISOU 457 N GLN B 97 9939 7492 7210 -583 723 -3037 N ATOM 458 CA GLN B 97 -0.295 9.417 2.908 1.00 68.69 C ANISOU 458 CA GLN B 97 10169 8201 7730 -702 873 -3280 C ATOM 459 C GLN B 97 -1.283 8.293 3.203 1.00 73.21 C ANISOU 459 C GLN B 97 10873 8644 8300 -850 869 -3247 C ATOM 460 O GLN B 97 -2.187 8.021 2.411 1.00 75.22 O ANISOU 460 O GLN B 97 11004 9117 8459 -978 1011 -3293 O ATOM 461 CB GLN B 97 0.913 8.861 2.154 1.00 69.28 C ANISOU 461 CB GLN B 97 10007 8232 8086 -632 810 -3609 C ATOM 462 CG GLN B 97 1.882 9.919 1.660 1.00 68.53 C ANISOU 462 CG GLN B 97 9706 8388 7943 -594 842 -3644 C ATOM 463 CD GLN B 97 2.974 9.335 0.791 1.00 72.20 C ANISOU 463 CD GLN B 97 9826 8960 8646 -556 874 -4053 C ATOM 464 OE1 GLN B 97 4.076 9.052 1.259 1.00 74.43 O ANISOU 464 OE1 GLN B 97 10036 9004 9240 -396 697 -4178 O ATOM 465 NE2 GLN B 97 2.670 9.147 -0.484 1.00 74.61 N ANISOU 465 NE2 GLN B 97 9912 9621 8816 -704 1091 -4294 N ATOM 466 N ALA B 98 -1.101 7.641 4.347 1.00 74.61 N ANISOU 466 N ALA B 98 11339 8438 8571 -885 650 -3138 N ATOM 467 CA ALA B 98 -2.011 6.589 4.777 1.00 74.04 C ANISOU 467 CA ALA B 98 11454 8249 8429 -1128 563 -3039 C ATOM 468 C ALA B 98 -3.390 7.165 5.060 1.00 73.28 C ANISOU 468 C ALA B 98 11341 8523 7978 -1272 846 -2814 C ATOM 469 O ALA B 98 -4.405 6.583 4.681 1.00 75.09 O ANISOU 469 O ALA B 98 11495 8923 8113 -1473 925 -2776 O ATOM 470 CB ALA B 98 -1.468 5.884 6.006 1.00 75.22 C ANISOU 470 CB ALA B 98 11990 7882 8707 -1227 191 -2948 C ATOM 471 N ALA B 99 -3.414 8.314 5.729 1.00 70.66 N ANISOU 471 N ALA B 99 11070 8311 7467 -1148 963 -2684 N ATOM 472 CA ALA B 99 -4.662 8.993 6.054 1.00 70.99 C ANISOU 472 CA ALA B 99 11038 8737 7199 -1197 1217 -2570 C ATOM 473 C ALA B 99 -5.353 9.499 4.790 1.00 71.48 C ANISOU 473 C ALA B 99 10753 9153 7252 -1149 1380 -2697 C ATOM 474 O ALA B 99 -6.573 9.655 4.759 1.00 74.77 O ANISOU 474 O ALA B 99 11017 9873 7520 -1241 1554 -2671 O ATOM 475 CB ALA B 99 -4.406 10.140 7.014 1.00 70.76 C ANISOU 475 CB ALA B 99 11183 8707 6997 -994 1218 -2465 C ATOM 476 N ALA B 100 -4.566 9.750 3.749 1.00 70.14 N ANISOU 476 N ALA B 100 10457 8948 7244 -1042 1308 -2848 N ATOM 477 CA ALA B 100 -5.112 10.206 2.478 1.00 70.54 C ANISOU 477 CA ALA B 100 10267 9257 7278 -1081 1392 -2965 C ATOM 478 C ALA B 100 -5.710 9.040 1.700 1.00 75.32 C ANISOU 478 C ALA B 100 10791 9844 7984 -1286 1440 -3021 C ATOM 479 O ALA B 100 -6.630 9.225 0.907 1.00 78.15 O ANISOU 479 O ALA B 100 11005 10377 8312 -1390 1516 -3043 O ATOM 480 CB ALA B 100 -4.038 10.902 1.656 1.00 69.03 C ANISOU 480 CB ALA B 100 10007 9085 7135 -1001 1295 -3089 C ATOM 481 N GLU B 101 -5.178 7.842 1.930 1.00 79.11 N ANISOU 481 N GLU B 101 11398 10055 8605 -1340 1313 -3045 N ATOM 482 CA GLU B 101 -5.685 6.637 1.276 1.00 81.82 C ANISOU 482 CA GLU B 101 11740 10316 9033 -1513 1243 -3076 C ATOM 483 C GLU B 101 -7.039 6.255 1.859 1.00 86.11 C ANISOU 483 C GLU B 101 12314 10981 9420 -1749 1297 -2828 C ATOM 484 O GLU B 101 -7.917 5.773 1.148 1.00 88.41 O ANISOU 484 O GLU B 101 12528 11346 9719 -1911 1307 -2776 O ATOM 485 CB GLU B 101 -4.695 5.480 1.422 1.00 81.06 C ANISOU 485 CB GLU B 101 11797 9853 9147 -1469 956 -3216 C ATOM 486 N GLN B 102 -7.200 6.488 3.159 1.00 87.79 N ANISOU 486 N GLN B 102 12644 11236 9476 -1795 1335 -2671 N ATOM 487 CA GLN B 102 -8.469 6.255 3.840 1.00 89.58 C ANISOU 487 CA GLN B 102 12841 11712 9483 -2064 1459 -2460 C ATOM 488 C GLN B 102 -9.543 7.213 3.327 1.00 85.44 C ANISOU 488 C GLN B 102 11983 11580 8899 -1996 1719 -2505 C ATOM 489 O GLN B 102 -10.737 6.951 3.454 1.00 88.21 O ANISOU 489 O GLN B 102 12173 12194 9148 -2216 1840 -2388 O ATOM 490 CB GLN B 102 -8.300 6.410 5.356 1.00 93.53 C ANISOU 490 CB GLN B 102 13563 12204 9771 -2142 1476 -2332 C ATOM 491 CG GLN B 102 -7.208 5.531 5.962 1.00 97.69 C ANISOU 491 CG GLN B 102 14475 12238 10403 -2232 1113 -2297 C ATOM 492 CD GLN B 102 -6.953 5.840 7.427 1.00104.53 C ANISOU 492 CD GLN B 102 15637 13021 11058 -2323 1107 -2165 C ATOM 493 OE1 GLN B 102 -7.619 6.691 8.016 1.00108.95 O ANISOU 493 OE1 GLN B 102 16097 13950 11350 -2299 1416 -2119 O ATOM 494 NE2 GLN B 102 -5.985 5.149 8.021 1.00105.72 N ANISOU 494 NE2 GLN B 102 16172 12657 11342 -2420 715 -2136 N ATOM 495 N LEU B 103 -9.106 8.324 2.744 1.00 81.92 N ANISOU 495 N LEU B 103 11435 11162 8529 -1718 1745 -2680 N ATOM 496 CA LEU B 103 -10.012 9.326 2.199 1.00 84.84 C ANISOU 496 CA LEU B 103 11540 11800 8897 -1634 1840 -2777 C ATOM 497 C LEU B 103 -10.739 8.776 0.974 1.00 83.96 C ANISOU 497 C LEU B 103 11306 11655 8939 -1825 1803 -2772 C ATOM 498 O LEU B 103 -11.844 9.207 0.645 1.00 83.66 O ANISOU 498 O LEU B 103 11039 11805 8944 -1865 1852 -2800 O ATOM 499 CB LEU B 103 -9.233 10.599 1.851 1.00 86.19 C ANISOU 499 CB LEU B 103 11734 11933 9080 -1369 1723 -2931 C ATOM 500 CG LEU B 103 -9.915 11.919 1.489 1.00 86.31 C ANISOU 500 CG LEU B 103 11574 12137 9081 -1225 1637 -3073 C ATOM 501 CD1 LEU B 103 -8.948 13.045 1.782 1.00 81.91 C ANISOU 501 CD1 LEU B 103 11171 11525 8428 -981 1442 -3120 C ATOM 502 CD2 LEU B 103 -10.330 11.956 0.020 1.00 85.81 C ANISOU 502 CD2 LEU B 103 11425 12002 9177 -1393 1514 -3157 C ATOM 503 N LYS B 104 -10.113 7.814 0.306 1.00 85.76 N ANISOU 503 N LYS B 104 11697 11616 9274 -1922 1679 -2761 N ATOM 504 CA LYS B 104 -10.706 7.193 -0.872 1.00 89.79 C ANISOU 504 CA LYS B 104 12184 12022 9911 -2100 1603 -2737 C ATOM 505 C LYS B 104 -11.863 6.276 -0.486 1.00 94.59 C ANISOU 505 C LYS B 104 12741 12714 10486 -2361 1603 -2486 C ATOM 506 O LYS B 104 -12.810 6.098 -1.255 1.00 94.37 O ANISOU 506 O LYS B 104 12611 12686 10559 -2512 1568 -2406 O ATOM 507 CB LYS B 104 -9.648 6.411 -1.653 1.00 88.59 C ANISOU 507 CB LYS B 104 12223 11586 9851 -2078 1456 -2859 C ATOM 508 N THR B 105 -11.779 5.696 0.708 1.00 97.68 N ANISOU 508 N THR B 105 13230 13161 10723 -2469 1603 -2337 N ATOM 509 CA THR B 105 -12.843 4.848 1.236 1.00101.13 C ANISOU 509 CA THR B 105 13626 13763 11036 -2823 1586 -2057 C ATOM 510 C THR B 105 -14.107 5.670 1.487 1.00101.72 C ANISOU 510 C THR B 105 13304 14284 11059 -2858 1867 -2057 C ATOM 511 O THR B 105 -15.227 5.181 1.323 1.00103.75 O ANISOU 511 O THR B 105 13386 14712 11322 -3133 1874 -1868 O ATOM 512 CB THR B 105 -12.410 4.153 2.546 1.00103.97 C ANISOU 512 CB THR B 105 14238 14091 11176 -3021 1483 -1906 C ATOM 513 OG1 THR B 105 -11.175 3.458 2.336 1.00103.53 O ANISOU 513 OG1 THR B 105 14514 13575 11248 -2919 1152 -1992 O ATOM 514 CG2 THR B 105 -13.468 3.162 3.007 1.00108.36 C ANISOU 514 CG2 THR B 105 14800 14834 11538 -3516 1389 -1569 C ATOM 515 N THR B 106 -13.913 6.927 1.875 1.00 99.68 N ANISOU 515 N THR B 106 12897 14209 10769 -2559 2048 -2289 N ATOM 516 CA THR B 106 -15.017 7.844 2.137 1.00 98.87 C ANISOU 516 CA THR B 106 12386 14524 10657 -2478 2259 -2420 C ATOM 517 C THR B 106 -15.678 8.303 0.835 1.00 98.96 C ANISOU 517 C THR B 106 12202 14426 10974 -2416 2133 -2533 C ATOM 518 O THR B 106 -16.882 8.561 0.796 1.00102.06 O ANISOU 518 O THR B 106 12224 15090 11466 -2473 2214 -2577 O ATOM 519 CB THR B 106 -14.536 9.079 2.936 1.00 94.11 C ANISOU 519 CB THR B 106 11755 14077 9925 -2120 2368 -2663 C ATOM 520 OG1 THR B 106 -13.956 8.653 4.176 1.00 94.00 O ANISOU 520 OG1 THR B 106 11982 14105 9630 -2221 2462 -2536 O ATOM 521 CG2 THR B 106 -15.691 10.032 3.226 1.00 94.58 C ANISOU 521 CG2 THR B 106 11364 14578 9994 -1961 2527 -2898 C ATOM 522 N ARG B 107 -14.884 8.384 -0.230 1.00 94.98 N ANISOU 522 N ARG B 107 11947 13524 10619 -2333 1920 -2595 N ATOM 523 CA ARG B 107 -15.356 8.880 -1.523 1.00 93.13 C ANISOU 523 CA ARG B 107 11651 13094 10640 -2338 1735 -2703 C ATOM 524 C ARG B 107 -16.479 8.026 -2.111 1.00 95.13 C ANISOU 524 C ARG B 107 11800 13284 11060 -2632 1675 -2485 C ATOM 525 O ARG B 107 -17.367 8.544 -2.789 1.00 97.29 O ANISOU 525 O ARG B 107 11884 13503 11577 -2657 1553 -2567 O ATOM 526 CB ARG B 107 -14.193 8.958 -2.515 1.00 90.35 C ANISOU 526 CB ARG B 107 11631 12384 10314 -2304 1562 -2789 C ATOM 527 N ASN B 108 -16.435 6.722 -1.851 1.00 94.49 N ANISOU 527 N ASN B 108 11874 13162 10866 -2866 1677 -2197 N ATOM 528 CA ASN B 108 -17.466 5.805 -2.331 1.00 95.72 C ANISOU 528 CA ASN B 108 11983 13248 11140 -3179 1555 -1905 C ATOM 529 C ASN B 108 -18.834 6.131 -1.741 1.00100.59 C ANISOU 529 C ASN B 108 12101 14314 11804 -3289 1730 -1871 C ATOM 530 O ASN B 108 -19.863 5.924 -2.383 1.00101.98 O ANISOU 530 O ASN B 108 12110 14424 12214 -3467 1611 -1734 O ATOM 531 CB ASN B 108 -17.089 4.359 -2.006 1.00 96.05 C ANISOU 531 CB ASN B 108 12333 13165 10995 -3418 1409 -1596 C ATOM 532 N ALA B 109 -18.833 6.641 -0.512 1.00103.28 N ANISOU 532 N ALA B 109 12197 15118 11925 -3181 2013 -2016 N ATOM 533 CA ALA B 109 -20.060 7.067 0.152 1.00105.55 C ANISOU 533 CA ALA B 109 11928 15958 12218 -3230 2253 -2108 C ATOM 534 C ALA B 109 -20.565 8.396 -0.412 1.00104.65 C ANISOU 534 C ALA B 109 11497 15818 12448 -2888 2171 -2513 C ATOM 535 O ALA B 109 -21.694 8.806 -0.140 1.00107.75 O ANISOU 535 O ALA B 109 11357 16599 12983 -2867 2289 -2679 O ATOM 536 CB ALA B 109 -19.838 7.179 1.655 1.00106.67 C ANISOU 536 CB ALA B 109 11968 16606 11957 -3232 2583 -2173 C ATOM 537 N TYR B 110 -19.724 9.065 -1.197 1.00 99.82 N ANISOU 537 N TYR B 110 11204 14757 11966 -2648 1922 -2692 N ATOM 538 CA TYR B 110 -20.099 10.324 -1.834 1.00 97.41 C ANISOU 538 CA TYR B 110 10731 14304 11976 -2391 1667 -3057 C ATOM 539 C TYR B 110 -20.702 10.086 -3.215 1.00 96.59 C ANISOU 539 C TYR B 110 10723 13727 12251 -2613 1331 -2942 C ATOM 540 O TYR B 110 -20.609 10.938 -4.100 1.00 94.21 O ANISOU 540 O TYR B 110 10570 13048 12178 -2528 970 -3159 O ATOM 541 CB TYR B 110 -18.889 11.254 -1.945 1.00 92.31 C ANISOU 541 CB TYR B 110 10418 13443 11214 -2114 1499 -3277 C ATOM 542 N SER B 116 -23.208 11.621 -10.370 1.00117.13 N ANISOU 542 N SER B 116 16224 16861 11420 -3552 6755 -4117 N ATOM 543 CA SER B 116 -23.315 11.908 -11.797 1.00110.81 C ANISOU 543 CA SER B 116 14523 16196 11385 -3288 6338 -4242 C ATOM 544 C SER B 116 -22.113 11.365 -12.566 1.00103.89 C ANISOU 544 C SER B 116 14069 15147 10256 -2893 5879 -3587 C ATOM 545 O SER B 116 -21.252 12.125 -13.007 1.00 92.84 O ANISOU 545 O SER B 116 12440 13891 8943 -2345 5331 -3466 O ATOM 546 CB SER B 116 -23.451 13.413 -12.029 1.00107.99 C ANISOU 546 CB SER B 116 13243 16188 11602 -2876 5920 -4709 C ATOM 547 OG SER B 116 -22.368 14.115 -11.447 1.00106.70 O ANISOU 547 OG SER B 116 13458 16101 10983 -2400 5580 -4460 O ATOM 548 N ASN B 117 -22.067 10.046 -12.726 1.00106.05 N ANISOU 548 N ASN B 117 14958 15087 10247 -3196 6100 -3213 N ATOM 549 CA ASN B 117 -20.948 9.386 -13.388 1.00100.24 C ANISOU 549 CA ASN B 117 14703 14140 9244 -2874 5680 -2600 C ATOM 550 C ASN B 117 -20.904 9.665 -14.886 1.00 97.33 C ANISOU 550 C ASN B 117 13485 13929 9567 -2611 5304 -2670 C ATOM 551 O ASN B 117 -21.210 8.791 -15.701 1.00 99.41 O ANISOU 551 O ASN B 117 13662 14032 10075 -2814 5381 -2568 O ATOM 552 CB ASN B 117 -21.008 7.876 -13.147 1.00103.64 C ANISOU 552 CB ASN B 117 16008 14117 9252 -3279 5990 -2230 C ATOM 553 N THR B 118 -20.516 10.885 -15.245 1.00 92.06 N ANISOU 553 N THR B 118 12215 13548 9217 -2151 4874 -2864 N ATOM 554 CA THR B 118 -20.396 11.270 -16.645 1.00 84.77 C ANISOU 554 CA THR B 118 10526 12747 8936 -1850 4444 -2934 C ATOM 555 C THR B 118 -18.937 11.219 -17.099 1.00 77.98 C ANISOU 555 C THR B 118 10054 11780 7794 -1402 3909 -2415 C ATOM 556 O THR B 118 -18.022 11.401 -16.294 1.00 79.78 O ANISOU 556 O THR B 118 10894 11920 7500 -1153 3664 -2152 O ATOM 557 CB THR B 118 -20.963 12.681 -16.892 1.00 86.22 C ANISOU 557 CB THR B 118 9754 13213 9793 -1590 4147 -3496 C ATOM 558 OG1 THR B 118 -20.845 13.011 -18.282 1.00 85.11 O ANISOU 558 OG1 THR B 118 8984 13100 10252 -1260 3635 -3508 O ATOM 559 CG2 THR B 118 -20.210 13.711 -16.064 1.00 84.37 C ANISOU 559 CG2 THR B 118 9675 13118 9263 -1236 3916 -3535 C ATOM 560 N LEU B 119 -18.725 10.969 -18.388 1.00 71.85 N ANISOU 560 N LEU B 119 8916 10906 7479 -1226 3499 -2195 N ATOM 561 CA LEU B 119 -17.374 10.838 -18.926 1.00 65.93 C ANISOU 561 CA LEU B 119 8466 9942 6644 -792 2821 -1638 C ATOM 562 C LEU B 119 -16.714 12.196 -19.169 1.00 62.02 C ANISOU 562 C LEU B 119 7522 9550 6491 -291 2187 -1704 C ATOM 563 O LEU B 119 -17.389 13.199 -19.414 1.00 64.65 O ANISOU 563 O LEU B 119 7185 10075 7305 -220 2128 -2123 O ATOM 564 CB LEU B 119 -17.385 10.029 -20.230 1.00 62.42 C ANISOU 564 CB LEU B 119 7844 9348 6524 -843 2685 -1403 C ATOM 565 CG LEU B 119 -17.816 8.561 -20.168 1.00 67.97 C ANISOU 565 CG LEU B 119 9050 9858 6917 -1307 3218 -1247 C ATOM 566 CD1 LEU B 119 -17.835 7.960 -21.565 1.00 62.56 C ANISOU 566 CD1 LEU B 119 8038 9071 6659 -1288 2995 -1089 C ATOM 567 CD2 LEU B 119 -16.906 7.760 -19.249 1.00 70.97 C ANISOU 567 CD2 LEU B 119 10501 9948 6517 -1285 3219 -806 C ATOM 568 N ARG B 120 -15.387 12.211 -19.086 1.00 57.44 N ANISOU 568 N ARG B 120 7331 8814 5679 55 1705 -1339 N ATOM 569 CA ARG B 120 -14.586 13.384 -19.422 1.00 54.81 C ANISOU 569 CA ARG B 120 6633 8513 5680 476 1130 -1371 C ATOM 570 C ARG B 120 -14.840 13.839 -20.852 1.00 51.38 C ANISOU 570 C ARG B 120 5582 8062 5877 544 871 -1405 C ATOM 571 O ARG B 120 -15.154 13.026 -21.724 1.00 48.09 O ANISOU 571 O ARG B 120 5123 7561 5587 378 962 -1256 O ATOM 572 CB ARG B 120 -13.094 13.081 -19.246 1.00 56.46 C ANISOU 572 CB ARG B 120 7310 8536 5604 781 693 -1044 C ATOM 573 CG ARG B 120 -12.451 13.738 -18.043 1.00 63.14 C ANISOU 573 CG ARG B 120 8425 9436 6129 1041 502 -1183 C ATOM 574 CD ARG B 120 -11.066 13.167 -17.777 1.00 67.26 C ANISOU 574 CD ARG B 120 9465 9754 6338 1349 66 -950 C ATOM 575 NE ARG B 120 -10.886 12.855 -16.363 1.00 74.16 N ANISOU 575 NE ARG B 120 11078 10581 6518 1433 111 -972 N ATOM 576 CZ ARG B 120 -10.605 11.645 -15.893 1.00 77.68 C ANISOU 576 CZ ARG B 120 12355 10783 6379 1421 121 -715 C ATOM 577 NH1 ARG B 120 -10.454 10.623 -16.726 1.00 75.85 N ANISOU 577 NH1 ARG B 120 12234 10355 6231 1331 95 -435 N ATOM 578 NH2 ARG B 120 -10.465 11.458 -14.588 1.00 81.76 N ANISOU 578 NH2 ARG B 120 13658 11214 6192 1516 127 -741 N ATOM 579 N VAL B 121 -14.684 15.135 -21.095 1.00 50.64 N ANISOU 579 N VAL B 121 5086 8010 6145 797 526 -1597 N ATOM 580 CA VAL B 121 -14.780 15.676 -22.451 1.00 47.38 C ANISOU 580 CA VAL B 121 4279 7491 6233 906 197 -1587 C ATOM 581 C VAL B 121 -13.861 14.960 -23.461 1.00 40.57 C ANISOU 581 C VAL B 121 3629 6426 5358 918 -2 -1172 C ATOM 582 O VAL B 121 -14.326 14.572 -24.531 1.00 37.15 O ANISOU 582 O VAL B 121 3053 5923 5141 823 -17 -1105 O ATOM 583 CB VAL B 121 -14.475 17.195 -22.471 1.00 43.56 C ANISOU 583 CB VAL B 121 3537 6974 6039 1184 -180 -1785 C ATOM 584 CG1 VAL B 121 -14.207 17.680 -23.893 1.00 40.95 C ANISOU 584 CG1 VAL B 121 3086 6409 6064 1289 -555 -1643 C ATOM 585 CG2 VAL B 121 -15.615 17.974 -21.834 1.00 49.44 C ANISOU 585 CG2 VAL B 121 3915 7905 6963 1197 -51 -2287 C ATOM 586 N PRO B 122 -12.564 14.772 -23.130 1.00 38.98 N ANISOU 586 N PRO B 122 3742 6139 4929 1050 -172 -963 N ATOM 587 CA PRO B 122 -11.708 14.094 -24.116 1.00 39.21 C ANISOU 587 CA PRO B 122 3893 5998 5007 1046 -332 -675 C ATOM 588 C PRO B 122 -12.136 12.652 -24.421 1.00 39.26 C ANISOU 588 C PRO B 122 4110 5967 4839 833 -85 -474 C ATOM 589 O PRO B 122 -11.972 12.190 -25.552 1.00 38.77 O ANISOU 589 O PRO B 122 3990 5799 4943 771 -162 -314 O ATOM 590 CB PRO B 122 -10.322 14.101 -23.451 1.00 36.16 C ANISOU 590 CB PRO B 122 3745 5562 4432 1253 -555 -647 C ATOM 591 CG PRO B 122 -10.384 15.157 -22.427 1.00 38.44 C ANISOU 591 CG PRO B 122 3953 5966 4685 1400 -608 -908 C ATOM 592 CD PRO B 122 -11.793 15.161 -21.934 1.00 38.62 C ANISOU 592 CD PRO B 122 3912 6143 4619 1234 -272 -1049 C ATOM 593 N ASP B 123 -12.659 11.948 -23.422 1.00 43.63 N ANISOU 593 N ASP B 123 4961 6581 5036 693 234 -490 N ATOM 594 CA ASP B 123 -13.116 10.579 -23.629 1.00 46.17 C ANISOU 594 CA ASP B 123 5544 6818 5180 438 524 -318 C ATOM 595 C ASP B 123 -14.345 10.558 -24.528 1.00 44.46 C ANISOU 595 C ASP B 123 4885 6674 5332 222 719 -479 C ATOM 596 O ASP B 123 -14.486 9.678 -25.371 1.00 44.24 O ANISOU 596 O ASP B 123 4871 6551 5389 90 765 -332 O ATOM 597 CB ASP B 123 -13.414 9.889 -22.292 1.00 50.11 C ANISOU 597 CB ASP B 123 6598 7299 5141 275 885 -308 C ATOM 598 CG ASP B 123 -12.153 9.371 -21.610 1.00 53.27 C ANISOU 598 CG ASP B 123 7621 7513 5105 525 594 -84 C ATOM 599 OD1 ASP B 123 -11.111 9.259 -22.296 1.00 54.72 O ANISOU 599 OD1 ASP B 123 7729 7593 5468 761 183 39 O ATOM 600 OD2 ASP B 123 -12.204 9.066 -20.399 1.00 57.76 O ANISOU 600 OD2 ASP B 123 8774 8026 5146 491 763 -77 O ATOM 601 N ILE B 124 -15.222 11.541 -24.367 1.00 43.13 N ANISOU 601 N ILE B 124 4302 6671 5416 226 776 -836 N ATOM 602 CA ILE B 124 -16.437 11.596 -25.166 1.00 41.97 C ANISOU 602 CA ILE B 124 3683 6593 5671 99 863 -1119 C ATOM 603 C ILE B 124 -16.119 11.866 -26.641 1.00 37.41 C ANISOU 603 C ILE B 124 2930 5877 5407 282 421 -976 C ATOM 604 O ILE B 124 -16.690 11.229 -27.525 1.00 37.45 O ANISOU 604 O ILE B 124 2798 5844 5589 168 450 -999 O ATOM 605 CB ILE B 124 -17.409 12.658 -24.621 1.00 48.15 C ANISOU 605 CB ILE B 124 4030 7569 6697 135 938 -1635 C ATOM 606 CG1 ILE B 124 -17.797 12.305 -23.183 1.00 50.20 C ANISOU 606 CG1 ILE B 124 4516 7969 6587 -135 1490 -1812 C ATOM 607 CG2 ILE B 124 -18.659 12.752 -25.495 1.00 51.34 C ANISOU 607 CG2 ILE B 124 3882 8030 7594 94 902 -2045 C ATOM 608 CD1 ILE B 124 -18.689 13.322 -22.512 1.00 51.18 C ANISOU 608 CD1 ILE B 124 4197 8317 6931 -124 1626 -2388 C ATOM 609 N LEU B 125 -15.203 12.794 -26.901 1.00 35.13 N ANISOU 609 N LEU B 125 2690 5496 5163 533 43 -849 N ATOM 610 CA LEU B 125 -14.742 13.052 -28.262 1.00 37.01 C ANISOU 610 CA LEU B 125 2930 5551 5582 640 -304 -676 C ATOM 611 C LEU B 125 -14.093 11.800 -28.863 1.00 34.56 C ANISOU 611 C LEU B 125 2870 5147 5116 508 -225 -354 C ATOM 612 O LEU B 125 -14.288 11.497 -30.039 1.00 33.13 O ANISOU 612 O LEU B 125 2650 4868 5069 475 -342 -286 O ATOM 613 CB LEU B 125 -13.757 14.225 -28.290 1.00 38.79 C ANISOU 613 CB LEU B 125 3239 5660 5838 832 -595 -619 C ATOM 614 CG LEU B 125 -14.328 15.591 -27.908 1.00 45.76 C ANISOU 614 CG LEU B 125 3901 6563 6925 1007 -774 -933 C ATOM 615 CD1 LEU B 125 -13.250 16.662 -27.925 1.00 45.19 C ANISOU 615 CD1 LEU B 125 3968 6329 6873 1135 -1005 -862 C ATOM 616 CD2 LEU B 125 -15.459 15.964 -28.850 1.00 50.52 C ANISOU 616 CD2 LEU B 125 4293 7080 7822 1094 -1009 -1148 C ATOM 617 N ALA B 126 -13.334 11.077 -28.044 1.00 33.98 N ANISOU 617 N ALA B 126 3082 5081 4746 466 -71 -188 N ATOM 618 CA ALA B 126 -12.705 9.826 -28.467 1.00 34.91 C ANISOU 618 CA ALA B 126 3450 5090 4723 380 -29 65 C ATOM 619 C ALA B 126 -13.760 8.825 -28.938 1.00 35.61 C ANISOU 619 C ALA B 126 3476 5183 4871 153 210 48 C ATOM 620 O ALA B 126 -13.581 8.158 -29.956 1.00 35.12 O ANISOU 620 O ALA B 126 3429 5026 4887 101 140 179 O ATOM 621 CB ALA B 126 -11.867 9.231 -27.325 1.00 36.70 C ANISOU 621 CB ALA B 126 4064 5283 4598 444 15 175 C ATOM 622 N LEU B 127 -14.864 8.744 -28.197 1.00 37.76 N ANISOU 622 N LEU B 127 3649 5572 5127 -8 523 -175 N ATOM 623 CA LEU B 127 -15.980 7.869 -28.554 1.00 38.20 C ANISOU 623 CA LEU B 127 3558 5646 5311 -277 818 -320 C ATOM 624 C LEU B 127 -16.590 8.230 -29.907 1.00 39.14 C ANISOU 624 C LEU B 127 3269 5770 5830 -190 547 -492 C ATOM 625 O LEU B 127 -16.818 7.357 -30.742 1.00 40.14 O ANISOU 625 O LEU B 127 3376 5828 6048 -303 570 -441 O ATOM 626 CB LEU B 127 -17.064 7.919 -27.479 1.00 40.31 C ANISOU 626 CB LEU B 127 3714 6058 5542 -512 1268 -664 C ATOM 627 CG LEU B 127 -16.708 7.294 -26.132 1.00 45.06 C ANISOU 627 CG LEU B 127 4889 6597 5634 -687 1632 -500 C ATOM 628 CD1 LEU B 127 -17.887 7.392 -25.186 1.00 47.15 C ANISOU 628 CD1 LEU B 127 5032 7015 5869 -1011 2182 -913 C ATOM 629 CD2 LEU B 127 -16.279 5.848 -26.324 1.00 44.28 C ANISOU 629 CD2 LEU B 127 5279 6262 5282 -849 1752 -165 C ATOM 630 N VAL B 128 -16.861 9.517 -30.111 1.00 38.98 N ANISOU 630 N VAL B 128 2981 5801 6028 34 251 -708 N ATOM 631 CA VAL B 128 -17.430 9.985 -31.370 1.00 40.94 C ANISOU 631 CA VAL B 128 2978 5986 6590 195 -123 -881 C ATOM 632 C VAL B 128 -16.526 9.626 -32.552 1.00 37.62 C ANISOU 632 C VAL B 128 2845 5383 6066 243 -360 -516 C ATOM 633 O VAL B 128 -16.988 9.102 -33.567 1.00 40.47 O ANISOU 633 O VAL B 128 3134 5688 6553 223 -473 -567 O ATOM 634 CB VAL B 128 -17.667 11.510 -31.351 1.00 43.72 C ANISOU 634 CB VAL B 128 3166 6323 7122 482 -488 -1116 C ATOM 635 CG1 VAL B 128 -18.004 12.014 -32.747 1.00 47.51 C ANISOU 635 CG1 VAL B 128 3634 6620 7800 712 -995 -1192 C ATOM 636 CG2 VAL B 128 -18.777 11.866 -30.368 1.00 43.36 C ANISOU 636 CG2 VAL B 128 2710 6486 7280 444 -274 -1627 C ATOM 637 N ILE B 129 -15.237 9.902 -32.400 1.00 35.56 N ANISOU 637 N ILE B 129 2880 5040 5589 295 -417 -213 N ATOM 638 CA ILE B 129 -14.249 9.625 -33.434 1.00 35.12 C ANISOU 638 CA ILE B 129 3073 4831 5439 288 -558 58 C ATOM 639 C ILE B 129 -14.133 8.120 -33.691 1.00 32.96 C ANISOU 639 C ILE B 129 2876 4558 5090 111 -352 194 C ATOM 640 O ILE B 129 -14.179 7.679 -34.836 1.00 33.81 O ANISOU 640 O ILE B 129 3017 4584 5244 78 -458 243 O ATOM 641 CB ILE B 129 -12.870 10.210 -33.048 1.00 32.73 C ANISOU 641 CB ILE B 129 2966 4472 4997 342 -593 213 C ATOM 642 CG1 ILE B 129 -12.934 11.744 -33.057 1.00 31.98 C ANISOU 642 CG1 ILE B 129 2857 4300 4994 492 -821 95 C ATOM 643 CG2 ILE B 129 -11.776 9.681 -33.984 1.00 29.99 C ANISOU 643 CG2 ILE B 129 2814 4007 4575 255 -607 397 C ATOM 644 CD1 ILE B 129 -11.732 12.407 -32.460 1.00 32.47 C ANISOU 644 CD1 ILE B 129 3019 4332 4987 523 -811 137 C ATOM 645 N PHE B 130 -13.994 7.351 -32.615 1.00 34.56 N ANISOU 645 N PHE B 130 3170 4816 5143 7 -78 250 N ATOM 646 CA PHE B 130 -14.013 5.891 -32.671 1.00 35.48 C ANISOU 646 CA PHE B 130 3429 4877 5176 -168 129 362 C ATOM 647 C PHE B 130 -15.175 5.346 -33.489 1.00 38.24 C ANISOU 647 C PHE B 130 3542 5241 5745 -302 193 188 C ATOM 648 O PHE B 130 -14.999 4.460 -34.325 1.00 35.86 O ANISOU 648 O PHE B 130 3305 4856 5466 -372 169 284 O ATOM 649 CB PHE B 130 -14.083 5.310 -31.257 1.00 37.80 C ANISOU 649 CB PHE B 130 3962 5171 5228 -280 431 396 C ATOM 650 CG PHE B 130 -12.757 5.237 -30.565 1.00 41.37 C ANISOU 650 CG PHE B 130 4758 5539 5422 -118 302 584 C ATOM 651 CD1 PHE B 130 -11.576 5.313 -31.288 1.00 36.00 C ANISOU 651 CD1 PHE B 130 4084 4794 4799 36 26 672 C ATOM 652 CD2 PHE B 130 -12.690 5.075 -29.190 1.00 49.23 C ANISOU 652 CD2 PHE B 130 6082 6510 6114 -123 456 611 C ATOM 653 CE1 PHE B 130 -10.351 5.225 -30.649 1.00 38.92 C ANISOU 653 CE1 PHE B 130 4678 5096 5015 220 -141 715 C ATOM 654 CE2 PHE B 130 -11.470 4.994 -28.543 1.00 50.83 C ANISOU 654 CE2 PHE B 130 6611 6615 6087 104 229 717 C ATOM 655 CZ PHE B 130 -10.296 5.072 -29.273 1.00 44.20 C ANISOU 655 CZ PHE B 130 5669 5731 5395 296 -94 734 C ATOM 656 N ALA B 131 -16.365 5.881 -33.241 1.00 40.86 N ANISOU 656 N ALA B 131 3557 5689 6278 -323 253 -141 N ATOM 657 CA ALA B 131 -17.563 5.395 -33.911 1.00 45.91 C ANISOU 657 CA ALA B 131 3876 6364 7204 -432 295 -451 C ATOM 658 C ALA B 131 -17.489 5.655 -35.416 1.00 46.22 C ANISOU 658 C ALA B 131 3883 6318 7361 -234 -149 -438 C ATOM 659 O ALA B 131 -17.695 4.742 -36.221 1.00 48.13 O ANISOU 659 O ALA B 131 4103 6509 7674 -324 -149 -448 O ATOM 660 CB ALA B 131 -18.798 6.036 -33.315 1.00 47.32 C ANISOU 660 CB ALA B 131 3637 6700 7641 -454 407 -937 C ATOM 661 N VAL B 132 -17.178 6.893 -35.791 1.00 39.68 N ANISOU 661 N VAL B 132 3126 5439 6510 21 -518 -411 N ATOM 662 CA VAL B 132 -17.091 7.255 -37.203 1.00 44.69 C ANISOU 662 CA VAL B 132 3909 5926 7143 196 -939 -376 C ATOM 663 C VAL B 132 -16.007 6.448 -37.923 1.00 43.78 C ANISOU 663 C VAL B 132 4111 5715 6807 73 -864 -33 C ATOM 664 O VAL B 132 -16.232 5.924 -39.017 1.00 45.16 O ANISOU 664 O VAL B 132 4334 5824 7000 74 -1011 -64 O ATOM 665 CB VAL B 132 -16.811 8.764 -37.388 1.00 45.39 C ANISOU 665 CB VAL B 132 4192 5889 7164 439 -1296 -353 C ATOM 666 CG1 VAL B 132 -16.680 9.103 -38.863 1.00 44.90 C ANISOU 666 CG1 VAL B 132 4485 5597 6979 577 -1700 -272 C ATOM 667 CG2 VAL B 132 -17.918 9.594 -36.747 1.00 48.09 C ANISOU 667 CG2 VAL B 132 4180 6316 7775 617 -1445 -770 C ATOM 668 N VAL B 133 -14.836 6.348 -37.302 1.00 39.23 N ANISOU 668 N VAL B 133 3723 5137 6045 -11 -662 226 N ATOM 669 CA VAL B 133 -13.729 5.599 -37.880 1.00 36.26 C ANISOU 669 CA VAL B 133 3568 4689 5522 -113 -588 445 C ATOM 670 C VAL B 133 -14.113 4.134 -38.087 1.00 38.55 C ANISOU 670 C VAL B 133 3774 4993 5881 -254 -428 427 C ATOM 671 O VAL B 133 -13.803 3.552 -39.125 1.00 40.77 O ANISOU 671 O VAL B 133 4149 5209 6132 -297 -493 472 O ATOM 672 CB VAL B 133 -12.474 5.694 -36.998 1.00 32.92 C ANISOU 672 CB VAL B 133 3264 4273 4971 -123 -451 589 C ATOM 673 CG1 VAL B 133 -11.412 4.707 -37.462 1.00 31.94 C ANISOU 673 CG1 VAL B 133 3259 4094 4782 -207 -378 688 C ATOM 674 CG2 VAL B 133 -11.936 7.125 -37.006 1.00 27.70 C ANISOU 674 CG2 VAL B 133 2698 3563 4265 -32 -586 588 C ATOM 675 N PHE B 134 -14.814 3.549 -37.119 1.00 34.00 N ANISOU 675 N PHE B 134 3056 4479 5385 -360 -188 336 N ATOM 676 CA PHE B 134 -15.253 2.164 -37.254 1.00 33.08 C ANISOU 676 CA PHE B 134 2904 4322 5344 -546 13 300 C ATOM 677 C PHE B 134 -16.198 1.944 -38.438 1.00 38.24 C ANISOU 677 C PHE B 134 3328 4987 6216 -542 -153 60 C ATOM 678 O PHE B 134 -16.030 0.995 -39.202 1.00 40.51 O ANISOU 678 O PHE B 134 3668 5205 6517 -616 -157 99 O ATOM 679 CB PHE B 134 -15.939 1.674 -35.982 1.00 32.90 C ANISOU 679 CB PHE B 134 2853 4318 5329 -744 387 211 C ATOM 680 CG PHE B 134 -16.517 0.294 -36.113 1.00 35.04 C ANISOU 680 CG PHE B 134 3123 4494 5696 -1004 652 136 C ATOM 681 CD1 PHE B 134 -15.691 -0.816 -36.097 1.00 33.54 C ANISOU 681 CD1 PHE B 134 3281 4121 5341 -1068 714 390 C ATOM 682 CD2 PHE B 134 -17.882 0.106 -36.276 1.00 35.99 C ANISOU 682 CD2 PHE B 134 2871 4689 6116 -1177 818 -252 C ATOM 683 CE1 PHE B 134 -16.215 -2.085 -36.227 1.00 34.14 C ANISOU 683 CE1 PHE B 134 3409 4056 5505 -1321 958 328 C ATOM 684 CE2 PHE B 134 -18.410 -1.162 -36.407 1.00 37.71 C ANISOU 684 CE2 PHE B 134 3077 4796 6455 -1466 1109 -361 C ATOM 685 CZ PHE B 134 -17.578 -2.256 -36.383 1.00 36.99 C ANISOU 685 CZ PHE B 134 3409 4490 6156 -1550 1188 -37 C ATOM 686 N LEU B 135 -17.202 2.802 -38.579 1.00 39.67 N ANISOU 686 N LEU B 135 3245 5245 6584 -419 -338 -240 N ATOM 687 CA LEU B 135 -18.191 2.604 -39.634 1.00 45.81 C ANISOU 687 CA LEU B 135 3782 6024 7599 -346 -586 -568 C ATOM 688 C LEU B 135 -17.571 2.835 -41.011 1.00 43.58 C ANISOU 688 C LEU B 135 3808 5625 7124 -175 -964 -403 C ATOM 689 O LEU B 135 -17.733 2.017 -41.924 1.00 44.58 O ANISOU 689 O LEU B 135 3932 5713 7292 -211 -1040 -471 O ATOM 690 CB LEU B 135 -19.396 3.523 -39.428 1.00 54.34 C ANISOU 690 CB LEU B 135 4488 7195 8964 -177 -792 -1028 C ATOM 691 CG LEU B 135 -20.236 3.269 -38.172 1.00 59.47 C ANISOU 691 CG LEU B 135 4761 7985 9849 -416 -341 -1346 C ATOM 692 CD1 LEU B 135 -21.505 4.112 -38.177 1.00 62.94 C ANISOU 692 CD1 LEU B 135 4924 8477 10511 -198 -558 -1863 C ATOM 693 CD2 LEU B 135 -20.573 1.795 -38.026 1.00 61.30 C ANISOU 693 CD2 LEU B 135 4912 8200 10180 -781 109 -1416 C ATOM 694 N VAL B 136 -16.851 3.943 -41.149 1.00 41.97 N ANISOU 694 N VAL B 136 3908 5348 6691 -29 -1157 -202 N ATOM 695 CA VAL B 136 -16.214 4.292 -42.412 1.00 43.68 C ANISOU 695 CA VAL B 136 4541 5413 6643 55 -1424 -45 C ATOM 696 C VAL B 136 -15.075 3.330 -42.747 1.00 44.04 C ANISOU 696 C VAL B 136 4760 5446 6526 -156 -1154 195 C ATOM 697 O VAL B 136 -14.907 2.932 -43.902 1.00 49.27 O ANISOU 697 O VAL B 136 5620 6037 7063 -174 -1269 196 O ATOM 698 CB VAL B 136 -15.666 5.739 -42.387 1.00 42.54 C ANISOU 698 CB VAL B 136 4739 5141 6285 177 -1596 99 C ATOM 699 CG1 VAL B 136 -14.947 6.066 -43.694 1.00 41.82 C ANISOU 699 CG1 VAL B 136 5205 4843 5843 155 -1749 267 C ATOM 700 CG2 VAL B 136 -16.792 6.735 -42.123 1.00 42.60 C ANISOU 700 CG2 VAL B 136 4591 5123 6473 450 -1955 -187 C ATOM 701 N GLY B 137 -14.302 2.953 -41.734 1.00 39.74 N ANISOU 701 N GLY B 137 4153 4962 5983 -286 -834 349 N ATOM 702 CA GLY B 137 -13.130 2.120 -41.936 1.00 37.45 C ANISOU 702 CA GLY B 137 3987 4649 5593 -422 -645 493 C ATOM 703 C GLY B 137 -13.444 0.673 -42.265 1.00 39.99 C ANISOU 703 C GLY B 137 4187 4968 6040 -521 -556 427 C ATOM 704 O GLY B 137 -12.794 0.064 -43.114 1.00 44.27 O ANISOU 704 O GLY B 137 4839 5471 6509 -583 -548 441 O ATOM 705 N VAL B 138 -14.437 0.110 -41.588 1.00 41.17 N ANISOU 705 N VAL B 138 4109 5147 6385 -572 -447 315 N ATOM 706 CA VAL B 138 -14.813 -1.273 -41.837 1.00 46.50 C ANISOU 706 CA VAL B 138 4687 5774 7205 -710 -324 231 C ATOM 707 C VAL B 138 -15.423 -1.430 -43.231 1.00 47.67 C ANISOU 707 C VAL B 138 4761 5929 7424 -656 -569 30 C ATOM 708 O VAL B 138 -14.989 -2.273 -44.007 1.00 50.39 O ANISOU 708 O VAL B 138 5185 6224 7739 -711 -574 40 O ATOM 709 CB VAL B 138 -15.793 -1.795 -40.761 1.00 48.06 C ANISOU 709 CB VAL B 138 4704 5969 7588 -871 -49 110 C ATOM 710 CG1 VAL B 138 -16.562 -3.010 -41.264 1.00 49.74 C ANISOU 710 CG1 VAL B 138 4753 6118 8026 -1042 55 -96 C ATOM 711 CG2 VAL B 138 -15.029 -2.136 -39.492 1.00 45.81 C ANISOU 711 CG2 VAL B 138 4676 5593 7138 -943 190 352 C ATOM 712 N LEU B 139 -16.411 -0.603 -43.552 1.00 44.46 N ANISOU 712 N LEU B 139 4218 5568 7105 -509 -824 -193 N ATOM 713 CA LEU B 139 -17.056 -0.669 -44.858 1.00 46.78 C ANISOU 713 CA LEU B 139 4500 5840 7434 -377 -1172 -432 C ATOM 714 C LEU B 139 -16.128 -0.193 -45.979 1.00 46.32 C ANISOU 714 C LEU B 139 4909 5695 6995 -297 -1373 -240 C ATOM 715 O LEU B 139 -16.069 -0.801 -47.048 1.00 41.35 O ANISOU 715 O LEU B 139 4400 5029 6282 -304 -1486 -312 O ATOM 716 CB LEU B 139 -18.343 0.157 -44.857 1.00 47.42 C ANISOU 716 CB LEU B 139 4331 5958 7727 -160 -1497 -798 C ATOM 717 CG LEU B 139 -19.423 -0.367 -43.908 1.00 54.91 C ANISOU 717 CG LEU B 139 4747 7011 9106 -313 -1228 -1146 C ATOM 718 CD1 LEU B 139 -20.709 0.432 -44.047 1.00 60.63 C ANISOU 718 CD1 LEU B 139 5170 7783 10082 -52 -1578 -1640 C ATOM 719 CD2 LEU B 139 -19.677 -1.852 -44.155 1.00 58.02 C ANISOU 719 CD2 LEU B 139 4957 7386 9702 -556 -980 -1277 C ATOM 720 N GLY B 140 -15.403 0.892 -45.724 1.00 43.50 N ANISOU 720 N GLY B 140 4834 5295 6398 -261 -1371 -26 N ATOM 721 CA GLY B 140 -14.517 1.460 -46.724 1.00 40.28 C ANISOU 721 CA GLY B 140 4932 4770 5601 -280 -1451 125 C ATOM 722 C GLY B 140 -13.381 0.538 -47.132 1.00 38.06 C ANISOU 722 C GLY B 140 4724 4513 5223 -503 -1149 211 C ATOM 723 O GLY B 140 -13.149 0.322 -48.318 1.00 42.75 O ANISOU 723 O GLY B 140 5606 5047 5590 -550 -1218 165 O ATOM 724 N ASN B 141 -12.671 -0.010 -46.151 1.00 32.82 N ANISOU 724 N ASN B 141 3826 3924 4721 -616 -847 294 N ATOM 725 CA ASN B 141 -11.531 -0.875 -46.430 1.00 31.93 C ANISOU 725 CA ASN B 141 3718 3825 4589 -770 -619 287 C ATOM 726 C ASN B 141 -11.950 -2.287 -46.862 1.00 32.83 C ANISOU 726 C ASN B 141 3652 3944 4876 -797 -633 159 C ATOM 727 O ASN B 141 -11.219 -2.951 -47.596 1.00 37.05 O ANISOU 727 O ASN B 141 4244 4477 5356 -893 -544 73 O ATOM 728 CB ASN B 141 -10.604 -0.949 -45.210 1.00 29.75 C ANISOU 728 CB ASN B 141 3296 3578 4429 -792 -419 361 C ATOM 729 CG ASN B 141 -9.864 0.361 -44.959 1.00 36.81 C ANISOU 729 CG ASN B 141 4350 4468 5170 -817 -354 418 C ATOM 730 OD1 ASN B 141 -9.027 0.778 -45.759 1.00 37.29 O ANISOU 730 OD1 ASN B 141 4619 4498 5051 -965 -233 349 O ATOM 731 ND2 ASN B 141 -10.171 1.011 -43.842 1.00 37.50 N ANISOU 731 ND2 ASN B 141 4351 4572 5324 -711 -388 510 N ATOM 732 N ALA B 142 -13.113 -2.748 -46.410 1.00 31.59 N ANISOU 732 N ALA B 142 3257 3790 4955 -742 -707 92 N ATOM 733 CA ALA B 142 -13.648 -4.010 -46.913 1.00 35.82 C ANISOU 733 CA ALA B 142 3629 4301 5678 -793 -722 -75 C ATOM 734 C ALA B 142 -13.884 -3.883 -48.408 1.00 39.38 C ANISOU 734 C ALA B 142 4259 4757 5947 -735 -965 -225 C ATOM 735 O ALA B 142 -13.584 -4.798 -49.170 1.00 42.68 O ANISOU 735 O ALA B 142 4685 5164 6367 -802 -939 -331 O ATOM 736 CB ALA B 142 -14.937 -4.396 -46.198 1.00 36.74 C ANISOU 736 CB ALA B 142 3446 4412 6101 -814 -693 -208 C ATOM 737 N LEU B 143 -14.405 -2.731 -48.823 1.00 41.33 N ANISOU 737 N LEU B 143 4709 4989 6004 -587 -1234 -243 N ATOM 738 CA LEU B 143 -14.664 -2.470 -50.236 1.00 40.78 C ANISOU 738 CA LEU B 143 4987 4860 5649 -484 -1544 -367 C ATOM 739 C LEU B 143 -13.363 -2.383 -51.034 1.00 39.47 C ANISOU 739 C LEU B 143 5245 4660 5092 -664 -1338 -251 C ATOM 740 O LEU B 143 -13.296 -2.843 -52.174 1.00 40.30 O ANISOU 740 O LEU B 143 5572 4742 4998 -693 -1416 -379 O ATOM 741 CB LEU B 143 -15.475 -1.183 -50.412 1.00 41.67 C ANISOU 741 CB LEU B 143 5338 4884 5610 -232 -1955 -410 C ATOM 742 CG LEU B 143 -15.891 -0.868 -51.851 1.00 49.60 C ANISOU 742 CG LEU B 143 6840 5752 6254 -44 -2406 -551 C ATOM 743 CD1 LEU B 143 -16.608 -2.058 -52.482 1.00 51.13 C ANISOU 743 CD1 LEU B 143 6730 6011 6684 19 -2575 -874 C ATOM 744 CD2 LEU B 143 -16.765 0.371 -51.907 1.00 55.01 C ANISOU 744 CD2 LEU B 143 7773 6290 6839 291 -2927 -639 C ATOM 745 N VAL B 144 -12.329 -1.803 -50.430 1.00 37.74 N ANISOU 745 N VAL B 144 5112 4445 4783 -803 -1049 -74 N ATOM 746 CA VAL B 144 -11.031 -1.722 -51.091 1.00 39.00 C ANISOU 746 CA VAL B 144 5570 4593 4655 -1045 -749 -78 C ATOM 747 C VAL B 144 -10.428 -3.113 -51.277 1.00 36.35 C ANISOU 747 C VAL B 144 4926 4352 4534 -1159 -547 -253 C ATOM 748 O VAL B 144 -10.003 -3.470 -52.376 1.00 39.17 O ANISOU 748 O VAL B 144 5500 4711 4670 -1295 -456 -405 O ATOM 749 CB VAL B 144 -10.045 -0.838 -50.307 1.00 39.92 C ANISOU 749 CB VAL B 144 5722 4706 4740 -1174 -474 40 C ATOM 750 CG1 VAL B 144 -8.662 -0.911 -50.933 1.00 40.57 C ANISOU 750 CG1 VAL B 144 5959 4807 4647 -1483 -78 -111 C ATOM 751 CG2 VAL B 144 -10.550 0.603 -50.266 1.00 41.49 C ANISOU 751 CG2 VAL B 144 6319 4762 4685 -1079 -675 202 C ATOM 752 N VAL B 145 -10.402 -3.893 -50.201 1.00 33.47 N ANISOU 752 N VAL B 145 4116 4031 4570 -1100 -490 -242 N ATOM 753 CA VAL B 145 -9.884 -5.259 -50.250 1.00 31.98 C ANISOU 753 CA VAL B 145 3666 3863 4623 -1149 -380 -410 C ATOM 754 C VAL B 145 -10.600 -6.042 -51.352 1.00 34.92 C ANISOU 754 C VAL B 145 4068 4228 4971 -1135 -539 -574 C ATOM 755 O VAL B 145 -9.963 -6.742 -52.132 1.00 40.10 O ANISOU 755 O VAL B 145 4730 4914 5593 -1236 -433 -774 O ATOM 756 CB VAL B 145 -10.039 -5.981 -48.884 1.00 37.62 C ANISOU 756 CB VAL B 145 4073 4520 5699 -1052 -381 -323 C ATOM 757 CG1 VAL B 145 -9.915 -7.507 -49.039 1.00 37.71 C ANISOU 757 CG1 VAL B 145 3910 4457 5961 -1056 -385 -483 C ATOM 758 CG2 VAL B 145 -9.023 -5.448 -47.868 1.00 31.76 C ANISOU 758 CG2 VAL B 145 3300 3785 4984 -1033 -256 -250 C ATOM 759 N TRP B 146 -11.920 -5.880 -51.422 1.00 35.05 N ANISOU 759 N TRP B 146 4071 4217 5028 -998 -808 -556 N ATOM 760 CA TRP B 146 -12.750 -6.506 -52.448 1.00 38.28 C ANISOU 760 CA TRP B 146 4485 4619 5439 -934 -1042 -771 C ATOM 761 C TRP B 146 -12.303 -6.121 -53.859 1.00 42.93 C ANISOU 761 C TRP B 146 5553 5211 5548 -989 -1088 -861 C ATOM 762 O TRP B 146 -12.071 -6.984 -54.703 1.00 44.59 O ANISOU 762 O TRP B 146 5765 5449 5729 -1055 -1058 -1064 O ATOM 763 CB TRP B 146 -14.216 -6.118 -52.238 1.00 41.46 C ANISOU 763 CB TRP B 146 4760 5002 5992 -744 -1364 -839 C ATOM 764 CG TRP B 146 -15.134 -6.534 -53.350 1.00 49.90 C ANISOU 764 CG TRP B 146 5844 6061 7053 -609 -1712 -1140 C ATOM 765 CD1 TRP B 146 -15.540 -5.771 -54.407 1.00 56.44 C ANISOU 765 CD1 TRP B 146 7108 6842 7495 -423 -2101 -1233 C ATOM 766 CD2 TRP B 146 -15.771 -7.808 -53.506 1.00 49.92 C ANISOU 766 CD2 TRP B 146 5456 6068 7445 -631 -1744 -1417 C ATOM 767 NE1 TRP B 146 -16.384 -6.495 -55.215 1.00 60.70 N ANISOU 767 NE1 TRP B 146 7511 7385 8166 -286 -2417 -1580 N ATOM 768 CE2 TRP B 146 -16.542 -7.747 -54.684 1.00 53.47 C ANISOU 768 CE2 TRP B 146 6046 6514 7757 -433 -2176 -1712 C ATOM 769 CE3 TRP B 146 -15.762 -8.995 -52.768 1.00 48.29 C ANISOU 769 CE3 TRP B 146 4861 5821 7667 -798 -1467 -1452 C ATOM 770 CZ2 TRP B 146 -17.297 -8.826 -55.138 1.00 56.20 C ANISOU 770 CZ2 TRP B 146 6048 6865 8441 -407 -2317 -2083 C ATOM 771 CZ3 TRP B 146 -16.510 -10.066 -53.223 1.00 50.90 C ANISOU 771 CZ3 TRP B 146 4909 6119 8313 -817 -1561 -1781 C ATOM 772 CH2 TRP B 146 -17.266 -9.973 -54.396 1.00 53.41 C ANISOU 772 CH2 TRP B 146 5266 6481 8547 -627 -1972 -2114 C ATOM 773 N VAL B 147 -12.180 -4.818 -54.098 1.00 41.63 N ANISOU 773 N VAL B 147 5853 4987 4976 -983 -1141 -712 N ATOM 774 CA VAL B 147 -11.801 -4.295 -55.404 1.00 46.54 C ANISOU 774 CA VAL B 147 7132 5535 5018 -1083 -1148 -753 C ATOM 775 C VAL B 147 -10.387 -4.719 -55.807 1.00 44.28 C ANISOU 775 C VAL B 147 6890 5326 4610 -1419 -650 -872 C ATOM 776 O VAL B 147 -10.164 -5.178 -56.924 1.00 46.49 O ANISOU 776 O VAL B 147 7430 5617 4618 -1531 -593 -1067 O ATOM 777 CB VAL B 147 -11.897 -2.753 -55.434 1.00 50.54 C ANISOU 777 CB VAL B 147 8226 5876 5100 -1043 -1271 -536 C ATOM 778 CG1 VAL B 147 -11.125 -2.191 -56.612 1.00 55.55 C ANISOU 778 CG1 VAL B 147 9663 6379 5064 -1302 -1060 -530 C ATOM 779 CG2 VAL B 147 -13.351 -2.307 -55.472 1.00 51.54 C ANISOU 779 CG2 VAL B 147 8423 5900 5260 -653 -1886 -565 C ATOM 780 N THR B 148 -9.432 -4.574 -54.893 1.00 42.01 N ANISOU 780 N THR B 148 6317 5099 4547 -1565 -305 -823 N ATOM 781 CA THR B 148 -8.034 -4.841 -55.221 1.00 42.64 C ANISOU 781 CA THR B 148 6357 5262 4583 -1876 165 -1060 C ATOM 782 C THR B 148 -7.697 -6.336 -55.256 1.00 42.23 C ANISOU 782 C THR B 148 5792 5316 4935 -1849 207 -1347 C ATOM 783 O THR B 148 -6.729 -6.735 -55.898 1.00 44.41 O ANISOU 783 O THR B 148 6043 5673 5156 -2079 524 -1671 O ATOM 784 CB THR B 148 -7.095 -4.152 -54.233 1.00 41.14 C ANISOU 784 CB THR B 148 5988 5095 4550 -1997 454 -1018 C ATOM 785 OG1 THR B 148 -7.462 -4.514 -52.897 1.00 37.63 O ANISOU 785 OG1 THR B 148 5056 4669 4573 -1733 242 -875 O ATOM 786 CG2 THR B 148 -7.178 -2.630 -54.387 1.00 42.53 C ANISOU 786 CG2 THR B 148 6758 5128 4273 -2116 511 -792 C ATOM 787 N ALA B 149 -8.486 -7.153 -54.562 1.00 42.11 N ANISOU 787 N ALA B 149 5389 5279 5332 -1597 -85 -1268 N ATOM 788 CA ALA B 149 -8.257 -8.600 -54.542 1.00 46.77 C ANISOU 788 CA ALA B 149 5573 5887 6310 -1549 -97 -1510 C ATOM 789 C ALA B 149 -8.295 -9.205 -55.944 1.00 49.53 C ANISOU 789 C ALA B 149 6084 6287 6451 -1643 -91 -1791 C ATOM 790 O ALA B 149 -7.505 -10.092 -56.263 1.00 51.94 O ANISOU 790 O ALA B 149 6155 6645 6934 -1724 68 -2116 O ATOM 791 CB ALA B 149 -9.279 -9.297 -53.646 1.00 44.77 C ANISOU 791 CB ALA B 149 5031 5531 6448 -1337 -364 -1353 C ATOM 792 N PHE B 150 -9.210 -8.719 -56.776 1.00 49.12 N ANISOU 792 N PHE B 150 6442 6204 6017 -1596 -308 -1710 N ATOM 793 CA PHE B 150 -9.357 -9.238 -58.132 1.00 55.51 C ANISOU 793 CA PHE B 150 7496 7046 6551 -1649 -364 -1971 C ATOM 794 C PHE B 150 -8.174 -8.896 -59.025 1.00 59.10 C ANISOU 794 C PHE B 150 8316 7573 6568 -1987 78 -2189 C ATOM 795 O PHE B 150 -7.776 -9.697 -59.866 1.00 64.59 O ANISOU 795 O PHE B 150 8972 8348 7221 -2103 212 -2531 O ATOM 796 CB PHE B 150 -10.640 -8.710 -58.769 1.00 58.31 C ANISOU 796 CB PHE B 150 8271 7313 6572 -1445 -807 -1868 C ATOM 797 CG PHE B 150 -11.886 -9.324 -58.213 1.00 60.68 C ANISOU 797 CG PHE B 150 8121 7578 7358 -1170 -1197 -1874 C ATOM 798 CD1 PHE B 150 -12.516 -8.766 -57.114 1.00 61.44 C ANISOU 798 CD1 PHE B 150 8019 7624 7702 -1037 -1324 -1645 C ATOM 799 CD2 PHE B 150 -12.429 -10.460 -58.787 1.00 65.26 C ANISOU 799 CD2 PHE B 150 8458 8172 8164 -1085 -1389 -2164 C ATOM 800 CE1 PHE B 150 -13.666 -9.327 -56.594 1.00 62.61 C ANISOU 800 CE1 PHE B 150 7733 7741 8314 -870 -1576 -1733 C ATOM 801 CE2 PHE B 150 -13.581 -11.025 -58.275 1.00 67.74 C ANISOU 801 CE2 PHE B 150 8335 8438 8965 -910 -1664 -2243 C ATOM 802 CZ PHE B 150 -14.202 -10.457 -57.176 1.00 64.88 C ANISOU 802 CZ PHE B 150 7776 8030 8845 -825 -1727 -2042 C ATOM 803 N GLU B 151 -7.614 -7.706 -58.850 1.00 56.20 N ANISOU 803 N GLU B 151 8302 7169 5881 -2184 347 -2034 N ATOM 804 CA GLU B 151 -6.529 -7.261 -59.715 1.00 62.43 C ANISOU 804 CA GLU B 151 9509 7997 6213 -2609 876 -2276 C ATOM 805 C GLU B 151 -5.167 -7.550 -59.097 1.00 65.49 C ANISOU 805 C GLU B 151 9320 8526 7039 -2823 1336 -2605 C ATOM 806 O GLU B 151 -4.132 -7.204 -59.669 1.00 70.79 O ANISOU 806 O GLU B 151 10174 9260 7462 -3240 1883 -2928 O ATOM 807 CB GLU B 151 -6.664 -5.768 -60.013 1.00 63.20 C ANISOU 807 CB GLU B 151 10437 7914 5664 -2768 955 -1980 C ATOM 808 N ALA B 152 -5.180 -8.200 -57.937 1.00 55.23 N ANISOU 808 N ALA B 152 7260 7929 5794 -2333 81 -2356 N ATOM 809 CA ALA B 152 -3.973 -8.393 -57.137 1.00 54.96 C ANISOU 809 CA ALA B 152 7485 7300 6097 -2079 304 -2072 C ATOM 810 C ALA B 152 -2.909 -9.208 -57.867 1.00 63.20 C ANISOU 810 C ALA B 152 8826 8005 7181 -2176 647 -2177 C ATOM 811 O ALA B 152 -1.717 -9.029 -57.631 1.00 68.63 O ANISOU 811 O ALA B 152 9676 8373 8026 -1887 730 -1894 O ATOM 812 CB ALA B 152 -4.322 -9.049 -55.812 1.00 51.15 C ANISOU 812 CB ALA B 152 7020 6499 5915 -2119 516 -2055 C ATOM 813 N LYS B 153 -3.331 -10.098 -58.756 1.00 67.02 N ANISOU 813 N LYS B 153 9346 8587 7530 -2548 858 -2543 N ATOM 814 CA LYS B 153 -2.373 -10.870 -59.533 1.00 71.85 C ANISOU 814 CA LYS B 153 10222 8897 8179 -2611 1203 -2613 C ATOM 815 C LYS B 153 -2.192 -10.281 -60.932 1.00 77.52 C ANISOU 815 C LYS B 153 10890 10011 8555 -2636 985 -2677 C ATOM 816 O LYS B 153 -1.430 -10.807 -61.742 1.00 80.89 O ANISOU 816 O LYS B 153 11509 10260 8964 -2701 1232 -2749 O ATOM 817 CB LYS B 153 -2.808 -12.334 -59.617 1.00 74.20 C ANISOU 817 CB LYS B 153 10591 9002 8599 -2912 1650 -2835 C ATOM 818 CG LYS B 153 -2.830 -13.043 -58.267 1.00 71.86 C ANISOU 818 CG LYS B 153 10404 8261 8638 -2835 1949 -2716 C ATOM 819 CD LYS B 153 -3.039 -14.531 -58.444 1.00 76.17 C ANISOU 819 CD LYS B 153 11098 8566 9278 -3103 2477 -2906 C ATOM 820 CE LYS B 153 -1.966 -15.118 -59.345 1.00 79.79 C ANISOU 820 CE LYS B 153 11804 8770 9743 -3100 2793 -2918 C ATOM 821 NZ LYS B 153 -2.196 -16.566 -59.608 1.00 86.28 N ANISOU 821 NZ LYS B 153 12782 9372 10627 -3396 3346 -3122 N ATOM 822 N ARG B 154 -2.883 -9.178 -61.204 1.00 78.04 N ANISOU 822 N ARG B 154 10694 10609 8347 -2542 538 -2608 N ATOM 823 CA ARG B 154 -2.791 -8.525 -62.506 1.00 76.63 C ANISOU 823 CA ARG B 154 10452 10842 7823 -2495 315 -2596 C ATOM 824 C ARG B 154 -2.023 -7.207 -62.427 1.00 73.32 C ANISOU 824 C ARG B 154 10101 10462 7296 -2135 44 -2279 C ATOM 825 O ARG B 154 -1.423 -6.775 -63.413 1.00 79.10 O ANISOU 825 O ARG B 154 10928 11317 7811 -2056 -9 -2220 O ATOM 826 CB ARG B 154 -4.187 -8.283 -63.084 1.00 76.71 C ANISOU 826 CB ARG B 154 10107 11471 7568 -2600 61 -2692 C ATOM 827 N THR B 155 -2.041 -6.570 -61.257 1.00 60.05 N ANISOU 827 N THR B 155 8340 8625 5852 -1837 -93 -1962 N ATOM 828 CA THR B 155 -1.374 -5.282 -61.080 1.00 54.89 C ANISOU 828 CA THR B 155 7705 7938 5212 -1426 -304 -1549 C ATOM 829 C THR B 155 -0.670 -5.144 -59.726 1.00 45.60 C ANISOU 829 C THR B 155 6596 6311 4417 -1192 -214 -1273 C ATOM 830 O THR B 155 -1.217 -5.527 -58.688 1.00 41.50 O ANISOU 830 O THR B 155 5989 5682 4096 -1232 -174 -1294 O ATOM 831 CB THR B 155 -2.369 -4.109 -61.230 1.00 64.50 C ANISOU 831 CB THR B 155 8681 9659 6166 -1246 -683 -1405 C ATOM 832 OG1 THR B 155 -3.529 -4.359 -60.429 1.00 70.83 O ANISOU 832 OG1 THR B 155 9256 10618 7039 -1347 -761 -1514 O ATOM 833 CG2 THR B 155 -2.795 -3.941 -62.682 1.00 73.03 C ANISOU 833 CG2 THR B 155 9690 11265 6793 -1353 -820 -1557 C ATOM 834 N ILE B 156 0.538 -4.581 -59.752 1.00 41.47 N ANISOU 834 N ILE B 156 6212 5575 3970 -964 -179 -1024 N ATOM 835 CA ILE B 156 1.307 -4.295 -58.543 1.00 38.46 C ANISOU 835 CA ILE B 156 5852 4881 3879 -742 -126 -755 C ATOM 836 C ILE B 156 0.586 -3.333 -57.596 1.00 38.80 C ANISOU 836 C ILE B 156 5731 5053 3958 -581 -372 -578 C ATOM 837 O ILE B 156 0.608 -3.519 -56.375 1.00 35.61 O ANISOU 837 O ILE B 156 5278 4466 3786 -522 -321 -486 O ATOM 838 CB ILE B 156 2.679 -3.684 -58.882 1.00 39.86 C ANISOU 838 CB ILE B 156 6159 4925 4061 -567 -75 -551 C ATOM 839 CG1 ILE B 156 3.458 -4.602 -59.822 1.00 41.78 C ANISOU 839 CG1 ILE B 156 6570 5028 4276 -696 194 -710 C ATOM 840 CG2 ILE B 156 3.472 -3.395 -57.600 1.00 34.57 C ANISOU 840 CG2 ILE B 156 5456 4033 3647 -378 -30 -306 C ATOM 841 CD1 ILE B 156 3.597 -6.007 -59.299 1.00 42.75 C ANISOU 841 CD1 ILE B 156 6759 4852 4634 -803 513 -840 C ATOM 842 N ASN B 157 -0.040 -2.299 -58.154 1.00 38.92 N ANISOU 842 N ASN B 157 5670 5384 3734 -485 -616 -512 N ATOM 843 CA ASN B 157 -0.727 -1.306 -57.329 1.00 36.75 C ANISOU 843 CA ASN B 157 5265 5211 3487 -300 -809 -332 C ATOM 844 C ASN B 157 -1.841 -1.929 -56.485 1.00 32.90 C ANISOU 844 C ASN B 157 4599 4795 3108 -420 -833 -471 C ATOM 845 O ASN B 157 -2.039 -1.547 -55.335 1.00 31.67 O ANISOU 845 O ASN B 157 4379 4533 3123 -307 -870 -338 O ATOM 846 CB ASN B 157 -1.292 -0.176 -58.196 1.00 38.36 C ANISOU 846 CB ASN B 157 5432 5753 3390 -132 -1016 -218 C ATOM 847 CG ASN B 157 -0.215 0.786 -58.678 1.00 41.07 C ANISOU 847 CG ASN B 157 5975 5953 3675 43 -972 -1 C ATOM 848 OD1 ASN B 157 0.904 0.785 -58.172 1.00 44.30 O ANISOU 848 OD1 ASN B 157 6502 6047 4284 45 -825 74 O ATOM 849 ND2 ASN B 157 -0.553 1.613 -59.663 1.00 41.34 N ANISOU 849 ND2 ASN B 157 6038 6251 3417 194 -1085 107 N ATOM 850 N ALA B 158 -2.551 -2.898 -57.059 1.00 33.44 N ANISOU 850 N ALA B 158 4592 5046 3069 -683 -788 -762 N ATOM 851 CA ALA B 158 -3.596 -3.606 -56.327 1.00 36.33 C ANISOU 851 CA ALA B 158 4796 5472 3535 -862 -758 -942 C ATOM 852 C ALA B 158 -3.036 -4.314 -55.093 1.00 33.45 C ANISOU 852 C ALA B 158 4536 4660 3513 -872 -525 -884 C ATOM 853 O ALA B 158 -3.685 -4.355 -54.054 1.00 33.34 O ANISOU 853 O ALA B 158 4409 4622 3636 -864 -543 -860 O ATOM 854 CB ALA B 158 -4.301 -4.605 -57.235 1.00 43.01 C ANISOU 854 CB ALA B 158 5572 6574 4195 -1223 -681 -1322 C ATOM 855 N ILE B 159 -1.831 -4.862 -55.209 1.00 34.32 N ANISOU 855 N ILE B 159 4852 4444 3745 -863 -298 -843 N ATOM 856 CA ILE B 159 -1.180 -5.521 -54.077 1.00 34.26 C ANISOU 856 CA ILE B 159 4934 4057 4024 -798 -65 -726 C ATOM 857 C ILE B 159 -0.869 -4.512 -52.966 1.00 32.55 C ANISOU 857 C ILE B 159 4644 3816 3907 -535 -222 -428 C ATOM 858 O ILE B 159 -1.116 -4.775 -51.790 1.00 32.58 O ANISOU 858 O ILE B 159 4596 3706 4076 -502 -165 -358 O ATOM 859 CB ILE B 159 0.116 -6.239 -54.509 1.00 31.95 C ANISOU 859 CB ILE B 159 4849 3475 3813 -776 215 -701 C ATOM 860 CG1 ILE B 159 -0.207 -7.320 -55.542 1.00 33.11 C ANISOU 860 CG1 ILE B 159 5109 3597 3876 -1079 439 -1038 C ATOM 861 CG2 ILE B 159 0.826 -6.844 -53.309 1.00 30.22 C ANISOU 861 CG2 ILE B 159 4690 2937 3856 -622 444 -507 C ATOM 862 CD1 ILE B 159 0.984 -8.125 -55.980 1.00 33.35 C ANISOU 862 CD1 ILE B 159 5364 3308 4001 -1053 776 -1032 C ATOM 863 N TRP B 160 -0.343 -3.354 -53.343 1.00 32.16 N ANISOU 863 N TRP B 160 4605 3872 3744 -374 -392 -270 N ATOM 864 CA TRP B 160 -0.042 -2.312 -52.369 1.00 30.68 C ANISOU 864 CA TRP B 160 4368 3665 3623 -183 -506 -40 C ATOM 865 C TRP B 160 -1.299 -1.866 -51.622 1.00 31.38 C ANISOU 865 C TRP B 160 4306 3896 3721 -167 -656 -46 C ATOM 866 O TRP B 160 -1.332 -1.844 -50.390 1.00 33.05 O ANISOU 866 O TRP B 160 4465 4013 4077 -117 -629 46 O ATOM 867 CB TRP B 160 0.596 -1.090 -53.036 1.00 30.88 C ANISOU 867 CB TRP B 160 4465 3762 3507 -60 -612 89 C ATOM 868 CG TRP B 160 1.901 -1.284 -53.770 1.00 32.12 C ANISOU 868 CG TRP B 160 4755 3810 3640 -60 -478 116 C ATOM 869 CD1 TRP B 160 2.292 -0.627 -54.900 1.00 32.68 C ANISOU 869 CD1 TRP B 160 4925 3957 3533 -32 -518 135 C ATOM 870 CD2 TRP B 160 2.991 -2.154 -53.419 1.00 31.52 C ANISOU 870 CD2 TRP B 160 4717 3547 3711 -56 -266 154 C ATOM 871 NE1 TRP B 160 3.541 -1.036 -55.284 1.00 33.94 N ANISOU 871 NE1 TRP B 160 5178 3987 3730 -46 -348 152 N ATOM 872 CE2 TRP B 160 3.995 -1.973 -54.393 1.00 32.96 C ANISOU 872 CE2 TRP B 160 5006 3713 3805 -44 -193 170 C ATOM 873 CE3 TRP B 160 3.214 -3.075 -52.389 1.00 30.03 C ANISOU 873 CE3 TRP B 160 4483 3218 3710 -30 -111 200 C ATOM 874 CZ2 TRP B 160 5.194 -2.670 -54.366 1.00 32.16 C ANISOU 874 CZ2 TRP B 160 4940 3479 3802 -3 20 223 C ATOM 875 CZ3 TRP B 160 4.407 -3.764 -52.364 1.00 30.07 C ANISOU 875 CZ3 TRP B 160 4533 3094 3800 45 105 283 C ATOM 876 CH2 TRP B 160 5.382 -3.559 -53.346 1.00 31.00 C ANISOU 876 CH2 TRP B 160 4730 3215 3833 59 166 289 C ATOM 877 N PHE B 161 -2.334 -1.508 -52.372 1.00 31.15 N ANISOU 877 N PHE B 161 4187 4133 3514 -196 -811 -147 N ATOM 878 CA PHE B 161 -3.535 -0.948 -51.771 1.00 30.02 C ANISOU 878 CA PHE B 161 3875 4173 3357 -134 -957 -131 C ATOM 879 C PHE B 161 -4.317 -1.994 -50.985 1.00 30.49 C ANISOU 879 C PHE B 161 3824 4204 3556 -312 -863 -289 C ATOM 880 O PHE B 161 -4.925 -1.677 -49.961 1.00 27.91 O ANISOU 880 O PHE B 161 3393 3889 3322 -251 -905 -228 O ATOM 881 CB PHE B 161 -4.403 -0.308 -52.848 1.00 29.79 C ANISOU 881 CB PHE B 161 3742 4512 3065 -69 -1142 -163 C ATOM 882 CG PHE B 161 -3.837 0.976 -53.383 1.00 34.56 C ANISOU 882 CG PHE B 161 4471 5116 3543 170 -1212 57 C ATOM 883 CD1 PHE B 161 -3.446 1.983 -52.518 1.00 32.12 C ANISOU 883 CD1 PHE B 161 4244 4611 3349 343 -1189 258 C ATOM 884 CD2 PHE B 161 -3.679 1.172 -54.747 1.00 36.33 C ANISOU 884 CD2 PHE B 161 4753 5526 3525 198 -1265 49 C ATOM 885 CE1 PHE B 161 -2.922 3.169 -53.003 1.00 36.56 C ANISOU 885 CE1 PHE B 161 4964 5120 3808 528 -1185 441 C ATOM 886 CE2 PHE B 161 -3.152 2.358 -55.236 1.00 39.59 C ANISOU 886 CE2 PHE B 161 5319 5899 3825 422 -1280 268 C ATOM 887 CZ PHE B 161 -2.773 3.356 -54.365 1.00 37.69 C ANISOU 887 CZ PHE B 161 5180 5417 3723 581 -1223 461 C ATOM 888 N LEU B 162 -4.285 -3.237 -51.458 1.00 31.54 N ANISOU 888 N LEU B 162 4004 4273 3706 -543 -694 -499 N ATOM 889 CA LEU B 162 -4.856 -4.359 -50.720 1.00 30.26 C ANISOU 889 CA LEU B 162 3809 3988 3701 -741 -507 -653 C ATOM 890 C LEU B 162 -4.256 -4.465 -49.318 1.00 30.11 C ANISOU 890 C LEU B 162 3861 3672 3908 -603 -384 -444 C ATOM 891 O LEU B 162 -4.980 -4.541 -48.325 1.00 30.94 O ANISOU 891 O LEU B 162 3869 3780 4109 -620 -374 -439 O ATOM 892 CB LEU B 162 -4.630 -5.670 -51.476 1.00 32.17 C ANISOU 892 CB LEU B 162 4182 4095 3947 -1005 -247 -898 C ATOM 893 CG LEU B 162 -5.012 -6.961 -50.758 1.00 41.29 C ANISOU 893 CG LEU B 162 5396 5001 5292 -1220 66 -1050 C ATOM 894 CD1 LEU B 162 -6.488 -6.940 -50.400 1.00 51.21 C ANISOU 894 CD1 LEU B 162 6419 6533 6507 -1397 -32 -1231 C ATOM 895 CD2 LEU B 162 -4.703 -8.153 -51.648 1.00 45.66 C ANISOU 895 CD2 LEU B 162 6134 5376 5838 -1482 377 -1304 C ATOM 896 N ASN B 163 -2.929 -4.476 -49.247 1.00 29.39 N ANISOU 896 N ASN B 163 3918 3371 3877 -466 -288 -271 N ATOM 897 CA ASN B 163 -2.235 -4.645 -47.976 1.00 28.84 C ANISOU 897 CA ASN B 163 3886 3105 3967 -324 -171 -61 C ATOM 898 C ASN B 163 -2.491 -3.489 -46.997 1.00 28.47 C ANISOU 898 C ASN B 163 3722 3182 3914 -188 -366 89 C ATOM 899 O ASN B 163 -2.603 -3.720 -45.789 1.00 26.01 O ANISOU 899 O ASN B 163 3375 2801 3706 -149 -294 179 O ATOM 900 CB ASN B 163 -0.732 -4.823 -48.216 1.00 25.85 C ANISOU 900 CB ASN B 163 3631 2583 3609 -195 -49 90 C ATOM 901 CG ASN B 163 -0.346 -6.279 -48.473 1.00 31.01 C ANISOU 901 CG ASN B 163 4434 2981 4368 -260 287 27 C ATOM 902 OD1 ASN B 163 0.253 -6.934 -47.618 1.00 30.91 O ANISOU 902 OD1 ASN B 163 4470 2794 4480 -125 495 201 O ATOM 903 ND2 ASN B 163 -0.698 -6.790 -49.644 1.00 28.46 N ANISOU 903 ND2 ASN B 163 4189 2644 3978 -458 366 -217 N ATOM 904 N LEU B 164 -2.597 -2.261 -47.509 1.00 26.55 N ANISOU 904 N LEU B 164 3441 3105 3540 -113 -575 117 N ATOM 905 CA LEU B 164 -2.887 -1.100 -46.656 1.00 24.12 C ANISOU 905 CA LEU B 164 3063 2874 3227 3 -705 231 C ATOM 906 C LEU B 164 -4.293 -1.204 -46.076 1.00 27.29 C ANISOU 906 C LEU B 164 3324 3378 3666 -49 -748 141 C ATOM 907 O LEU B 164 -4.529 -0.865 -44.920 1.00 30.80 O ANISOU 907 O LEU B 164 3720 3802 4182 0 -745 217 O ATOM 908 CB LEU B 164 -2.749 0.225 -47.429 1.00 24.44 C ANISOU 908 CB LEU B 164 3146 3013 3125 112 -845 290 C ATOM 909 CG LEU B 164 -1.374 0.704 -47.904 1.00 26.84 C ANISOU 909 CG LEU B 164 3584 3235 3380 158 -807 387 C ATOM 910 CD1 LEU B 164 -1.500 2.055 -48.619 1.00 24.56 C ANISOU 910 CD1 LEU B 164 3368 3011 2954 268 -899 447 C ATOM 911 CD2 LEU B 164 -0.403 0.802 -46.749 1.00 26.49 C ANISOU 911 CD2 LEU B 164 3538 3110 3418 169 -724 497 C ATOM 912 N ALA B 165 -5.226 -1.669 -46.898 1.00 26.92 N ANISOU 912 N ALA B 165 3194 3480 3552 -167 -782 -40 N ATOM 913 CA ALA B 165 -6.608 -1.825 -46.477 1.00 29.46 C ANISOU 913 CA ALA B 165 3336 3966 3891 -247 -818 -159 C ATOM 914 C ALA B 165 -6.747 -2.919 -45.414 1.00 29.79 C ANISOU 914 C ALA B 165 3393 3818 4106 -381 -611 -203 C ATOM 915 O ALA B 165 -7.456 -2.740 -44.425 1.00 32.79 O ANISOU 915 O ALA B 165 3674 4232 4554 -367 -614 -183 O ATOM 916 CB ALA B 165 -7.489 -2.131 -47.678 1.00 26.85 C ANISOU 916 CB ALA B 165 2874 3925 3402 -386 -897 -373 C ATOM 917 N VAL B 166 -6.065 -4.043 -45.621 1.00 30.86 N ANISOU 917 N VAL B 166 3674 3739 4313 -490 -400 -247 N ATOM 918 CA VAL B 166 -6.109 -5.148 -44.663 1.00 36.62 C ANISOU 918 CA VAL B 166 4472 4238 5205 -577 -137 -244 C ATOM 919 C VAL B 166 -5.590 -4.697 -43.291 1.00 34.09 C ANISOU 919 C VAL B 166 4163 3837 4953 -379 -141 10 C ATOM 920 O VAL B 166 -6.189 -4.999 -42.261 1.00 35.66 O ANISOU 920 O VAL B 166 4320 3997 5233 -411 -49 25 O ATOM 921 CB VAL B 166 -5.291 -6.376 -45.152 1.00 33.13 C ANISOU 921 CB VAL B 166 4233 3524 4830 -654 150 -279 C ATOM 922 CG1 VAL B 166 -5.197 -7.430 -44.050 1.00 33.85 C ANISOU 922 CG1 VAL B 166 4440 3334 5089 -651 469 -185 C ATOM 923 CG2 VAL B 166 -5.917 -6.980 -46.407 1.00 34.89 C ANISOU 923 CG2 VAL B 166 4452 3828 4975 -934 212 -598 C ATOM 924 N ALA B 167 -4.485 -3.959 -43.287 1.00 32.99 N ANISOU 924 N ALA B 167 4071 3707 4758 -203 -240 190 N ATOM 925 CA ALA B 167 -3.944 -3.415 -42.047 1.00 32.45 C ANISOU 925 CA ALA B 167 3981 3652 4697 -59 -264 391 C ATOM 926 C ALA B 167 -4.943 -2.461 -41.376 1.00 30.23 C ANISOU 926 C ALA B 167 3578 3512 4396 -58 -407 358 C ATOM 927 O ALA B 167 -5.114 -2.490 -40.157 1.00 30.28 O ANISOU 927 O ALA B 167 3551 3514 4441 -33 -351 437 O ATOM 928 CB ALA B 167 -2.624 -2.713 -42.309 1.00 27.53 C ANISOU 928 CB ALA B 167 3399 3072 3989 60 -342 525 C ATOM 929 N ASP B 168 -5.621 -1.642 -42.176 1.00 27.66 N ANISOU 929 N ASP B 168 3187 3322 4000 -62 -571 255 N ATOM 930 CA ASP B 168 -6.591 -0.688 -41.641 1.00 32.56 C ANISOU 930 CA ASP B 168 3697 4070 4605 -11 -676 241 C ATOM 931 C ASP B 168 -7.865 -1.370 -41.143 1.00 35.62 C ANISOU 931 C ASP B 168 3954 4511 5068 -126 -609 117 C ATOM 932 O ASP B 168 -8.384 -1.019 -40.085 1.00 38.66 O ANISOU 932 O ASP B 168 4278 4917 5494 -97 -591 152 O ATOM 933 CB ASP B 168 -6.934 0.369 -42.689 1.00 33.45 C ANISOU 933 CB ASP B 168 3781 4324 4604 88 -836 220 C ATOM 934 CG ASP B 168 -5.825 1.394 -42.867 1.00 38.67 C ANISOU 934 CG ASP B 168 4584 4910 5200 200 -866 348 C ATOM 935 OD1 ASP B 168 -4.908 1.428 -42.015 1.00 37.19 O ANISOU 935 OD1 ASP B 168 4462 4626 5042 184 -792 431 O ATOM 936 OD2 ASP B 168 -5.875 2.167 -43.852 1.00 36.94 O ANISOU 936 OD2 ASP B 168 4401 4753 4880 298 -948 366 O ATOM 937 N PHE B 169 -8.360 -2.344 -41.903 1.00 32.17 N ANISOU 937 N PHE B 169 3477 4103 4641 -290 -547 -51 N ATOM 938 CA PHE B 169 -9.536 -3.118 -41.509 1.00 30.38 C ANISOU 938 CA PHE B 169 3127 3931 4485 -471 -437 -216 C ATOM 939 C PHE B 169 -9.305 -3.834 -40.172 1.00 34.55 C ANISOU 939 C PHE B 169 3752 4233 5142 -496 -219 -117 C ATOM 940 O PHE B 169 -10.096 -3.700 -39.238 1.00 38.33 O ANISOU 940 O PHE B 169 4134 4762 5666 -514 -188 -125 O ATOM 941 CB PHE B 169 -9.888 -4.131 -42.604 1.00 31.17 C ANISOU 941 CB PHE B 169 3207 4078 4558 -712 -351 -454 C ATOM 942 CG PHE B 169 -11.174 -4.878 -42.363 1.00 35.15 C ANISOU 942 CG PHE B 169 3554 4693 5108 -970 -227 -689 C ATOM 943 CD1 PHE B 169 -12.375 -4.382 -42.842 1.00 35.08 C ANISOU 943 CD1 PHE B 169 3258 5087 4983 -1025 -402 -850 C ATOM 944 CD2 PHE B 169 -11.177 -6.080 -41.677 1.00 36.97 C ANISOU 944 CD2 PHE B 169 3917 4645 5484 -1150 90 -742 C ATOM 945 CE1 PHE B 169 -13.550 -5.056 -42.635 1.00 38.19 C ANISOU 945 CE1 PHE B 169 3466 5642 5404 -1297 -285 -1095 C ATOM 946 CE2 PHE B 169 -12.355 -6.763 -41.463 1.00 41.89 C ANISOU 946 CE2 PHE B 169 4408 5357 6151 -1434 245 -986 C ATOM 947 CZ PHE B 169 -13.544 -6.252 -41.943 1.00 42.51 C ANISOU 947 CZ PHE B 169 4165 5875 6111 -1532 48 -1183 C ATOM 948 N LEU B 170 -8.219 -4.594 -40.094 1.00 33.52 N ANISOU 948 N LEU B 170 3808 3873 5055 -470 -54 -3 N ATOM 949 CA LEU B 170 -7.875 -5.342 -38.887 1.00 36.95 C ANISOU 949 CA LEU B 170 4349 4115 5577 -432 176 151 C ATOM 950 C LEU B 170 -7.800 -4.442 -37.646 1.00 39.18 C ANISOU 950 C LEU B 170 4568 4501 5817 -285 71 315 C ATOM 951 O LEU B 170 -8.250 -4.811 -36.560 1.00 37.10 O ANISOU 951 O LEU B 170 4300 4195 5601 -305 209 364 O ATOM 952 CB LEU B 170 -6.543 -6.067 -39.085 1.00 38.44 C ANISOU 952 CB LEU B 170 4721 4105 5779 -323 338 315 C ATOM 953 CG LEU B 170 -5.930 -6.687 -37.829 1.00 50.53 C ANISOU 953 CG LEU B 170 6349 5506 7344 -169 552 574 C ATOM 954 CD1 LEU B 170 -6.719 -7.917 -37.380 1.00 52.75 C ANISOU 954 CD1 LEU B 170 6731 5558 7752 -308 890 511 C ATOM 955 CD2 LEU B 170 -4.461 -7.028 -38.054 1.00 56.26 C ANISOU 955 CD2 LEU B 170 7183 6161 8034 32 631 791 C ATOM 956 N SER B 171 -7.227 -3.258 -37.822 1.00 36.08 N ANISOU 956 N SER B 171 4146 4237 5327 -161 -141 384 N ATOM 957 CA SER B 171 -7.094 -2.298 -36.736 1.00 33.24 C ANISOU 957 CA SER B 171 3745 3979 4906 -71 -218 489 C ATOM 958 C SER B 171 -8.472 -1.841 -36.235 1.00 28.64 C ANISOU 958 C SER B 171 3039 3482 4360 -125 -245 372 C ATOM 959 O SER B 171 -8.685 -1.692 -35.034 1.00 28.74 O ANISOU 959 O SER B 171 3034 3517 4368 -114 -183 432 O ATOM 960 CB SER B 171 -6.255 -1.107 -37.203 1.00 38.45 C ANISOU 960 CB SER B 171 4428 4720 5462 15 -384 530 C ATOM 961 OG SER B 171 -6.052 -0.184 -36.157 1.00 43.22 O ANISOU 961 OG SER B 171 5016 5413 5994 47 -413 588 O ATOM 962 N CYS B 172 -9.405 -1.653 -37.168 1.00 26.77 N ANISOU 962 N CYS B 172 2698 3332 4141 -177 -332 210 N ATOM 963 CA CYS B 172 -10.764 -1.205 -36.856 1.00 31.24 C ANISOU 963 CA CYS B 172 3096 4040 4733 -197 -364 101 C ATOM 964 C CYS B 172 -11.565 -2.219 -36.038 1.00 37.25 C ANISOU 964 C CYS B 172 3804 4758 5589 -353 -174 29 C ATOM 965 O CYS B 172 -12.531 -1.858 -35.360 1.00 34.36 O ANISOU 965 O CYS B 172 3311 4493 5249 -360 -158 -22 O ATOM 966 CB CYS B 172 -11.531 -0.895 -38.146 1.00 34.15 C ANISOU 966 CB CYS B 172 3316 4605 5054 -196 -506 -36 C ATOM 967 SG CYS B 172 -11.109 0.679 -38.953 1.00 37.14 S ANISOU 967 SG CYS B 172 3734 5065 5314 50 -699 69 S ATOM 968 N LEU B 173 -11.168 -3.486 -36.112 1.00 38.14 N ANISOU 968 N LEU B 173 4033 4699 5759 -471 9 27 N ATOM 969 CA LEU B 173 -11.898 -4.554 -35.436 1.00 39.75 C ANISOU 969 CA LEU B 173 4239 4803 6062 -643 260 -47 C ATOM 970 C LEU B 173 -11.820 -4.430 -33.913 1.00 41.64 C ANISOU 970 C LEU B 173 4527 4992 6303 -556 361 123 C ATOM 971 O LEU B 173 -12.701 -4.905 -33.202 1.00 48.76 O ANISOU 971 O LEU B 173 5384 5872 7271 -676 530 56 O ATOM 972 CB LEU B 173 -11.370 -5.917 -35.882 1.00 36.49 C ANISOU 972 CB LEU B 173 4007 4144 5714 -761 505 -60 C ATOM 973 CG LEU B 173 -11.594 -6.271 -37.353 1.00 37.06 C ANISOU 973 CG LEU B 173 4037 4269 5775 -933 470 -292 C ATOM 974 CD1 LEU B 173 -11.123 -7.690 -37.643 1.00 37.83 C ANISOU 974 CD1 LEU B 173 4362 4053 5959 -1072 808 -325 C ATOM 975 CD2 LEU B 173 -13.059 -6.109 -37.714 1.00 39.69 C ANISOU 975 CD2 LEU B 173 4106 4879 6095 -1140 399 -571 C ATOM 976 N ALA B 174 -10.767 -3.780 -33.426 1.00 36.10 N ANISOU 976 N ALA B 174 3906 4305 5506 -372 264 323 N ATOM 977 CA ALA B 174 -10.582 -3.549 -31.996 1.00 32.40 C ANISOU 977 CA ALA B 174 3467 3868 4977 -295 331 476 C ATOM 978 C ALA B 174 -11.535 -2.486 -31.460 1.00 31.41 C ANISOU 978 C ALA B 174 3205 3891 4840 -305 239 372 C ATOM 979 O ALA B 174 -11.883 -2.499 -30.278 1.00 33.11 O ANISOU 979 O ALA B 174 3417 4129 5034 -317 350 419 O ATOM 980 CB ALA B 174 -9.144 -3.146 -31.711 1.00 28.98 C ANISOU 980 CB ALA B 174 3116 3493 4404 -142 248 676 C ATOM 981 N LEU B 175 -11.965 -1.583 -32.336 1.00 28.56 N ANISOU 981 N LEU B 175 2738 3630 4483 -276 62 248 N ATOM 982 CA LEU B 175 -12.696 -0.377 -31.925 1.00 33.55 C ANISOU 982 CA LEU B 175 3269 4382 5097 -207 -8 190 C ATOM 983 C LEU B 175 -13.959 -0.583 -31.071 1.00 37.72 C ANISOU 983 C LEU B 175 3672 4966 5695 -285 125 104 C ATOM 984 O LEU B 175 -14.149 0.159 -30.107 1.00 39.33 O ANISOU 984 O LEU B 175 3881 5202 5861 -233 163 128 O ATOM 985 CB LEU B 175 -13.062 0.452 -33.159 1.00 27.65 C ANISOU 985 CB LEU B 175 2426 3733 4345 -112 -177 110 C ATOM 986 CG LEU B 175 -11.856 1.190 -33.730 1.00 32.66 C ANISOU 986 CG LEU B 175 3205 4310 4892 -7 -289 203 C ATOM 987 CD1 LEU B 175 -12.225 1.955 -34.993 1.00 28.43 C ANISOU 987 CD1 LEU B 175 2603 3863 4336 119 -427 162 C ATOM 988 CD2 LEU B 175 -11.282 2.125 -32.668 1.00 35.95 C ANISOU 988 CD2 LEU B 175 3732 4692 5233 33 -242 271 C ATOM 989 N PRO B 176 -14.828 -1.563 -31.418 1.00 39.58 N ANISOU 989 N PRO B 176 3793 5220 6024 -437 219 -24 N ATOM 990 CA PRO B 176 -16.023 -1.767 -30.581 1.00 39.50 C ANISOU 990 CA PRO B 176 3650 5279 6079 -536 367 -119 C ATOM 991 C PRO B 176 -15.704 -2.073 -29.115 1.00 41.15 C ANISOU 991 C PRO B 176 4007 5370 6259 -551 550 14 C ATOM 992 O PRO B 176 -16.403 -1.598 -28.219 1.00 43.64 O ANISOU 992 O PRO B 176 4249 5756 6574 -543 618 -15 O ATOM 993 CB PRO B 176 -16.708 -2.968 -31.240 1.00 41.10 C ANISOU 993 CB PRO B 176 3754 5493 6369 -770 483 -294 C ATOM 994 CG PRO B 176 -16.275 -2.906 -32.662 1.00 41.80 C ANISOU 994 CG PRO B 176 3824 5640 6420 -747 307 -344 C ATOM 995 CD PRO B 176 -14.859 -2.421 -32.621 1.00 39.72 C ANISOU 995 CD PRO B 176 3781 5229 6082 -561 209 -133 C ATOM 996 N ILE B 177 -14.652 -2.848 -28.881 1.00 38.53 N ANISOU 996 N ILE B 177 3871 4884 5884 -548 637 175 N ATOM 997 CA ILE B 177 -14.266 -3.224 -27.525 1.00 43.23 C ANISOU 997 CA ILE B 177 4598 5426 6401 -524 808 348 C ATOM 998 C ILE B 177 -13.590 -2.067 -26.782 1.00 42.85 C ANISOU 998 C ILE B 177 4580 5512 6188 -398 680 441 C ATOM 999 O ILE B 177 -13.810 -1.876 -25.584 1.00 43.40 O ANISOU 999 O ILE B 177 4665 5649 6177 -408 782 484 O ATOM 1000 CB ILE B 177 -13.353 -4.462 -27.542 1.00 47.55 C ANISOU 1000 CB ILE B 177 5333 5798 6937 -500 971 533 C ATOM 1001 CG1 ILE B 177 -14.215 -5.717 -27.683 1.00 54.75 C ANISOU 1001 CG1 ILE B 177 6276 6523 8004 -689 1256 430 C ATOM 1002 CG2 ILE B 177 -12.503 -4.548 -26.283 1.00 48.59 C ANISOU 1002 CG2 ILE B 177 5582 5985 6894 -363 1051 797 C ATOM 1003 CD1 ILE B 177 -13.542 -6.984 -27.218 1.00 61.42 C ANISOU 1003 CD1 ILE B 177 7361 7133 8842 -635 1558 662 C ATOM 1004 N LEU B 178 -12.786 -1.288 -27.499 1.00 36.02 N ANISOU 1004 N LEU B 178 3731 4691 5263 -313 482 448 N ATOM 1005 CA LEU B 178 -12.198 -0.087 -26.932 1.00 31.83 C ANISOU 1005 CA LEU B 178 3232 4279 4582 -261 392 465 C ATOM 1006 C LEU B 178 -13.305 0.904 -26.571 1.00 36.11 C ANISOU 1006 C LEU B 178 3691 4856 5174 -271 420 311 C ATOM 1007 O LEU B 178 -13.335 1.450 -25.465 1.00 38.99 O ANISOU 1007 O LEU B 178 4090 5292 5433 -299 502 303 O ATOM 1008 CB LEU B 178 -11.202 0.532 -27.912 1.00 28.93 C ANISOU 1008 CB LEU B 178 2909 3916 4167 -200 218 474 C ATOM 1009 CG LEU B 178 -9.962 -0.307 -28.256 1.00 30.95 C ANISOU 1009 CG LEU B 178 3236 4168 4357 -160 194 637 C ATOM 1010 CD1 LEU B 178 -9.026 0.437 -29.202 1.00 28.56 C ANISOU 1010 CD1 LEU B 178 2964 3884 4004 -121 33 620 C ATOM 1011 CD2 LEU B 178 -9.214 -0.717 -26.994 1.00 28.59 C ANISOU 1011 CD2 LEU B 178 2972 4018 3872 -139 284 817 C ATOM 1012 N PHE B 179 -14.216 1.113 -27.515 1.00 34.25 N ANISOU 1012 N PHE B 179 3335 4599 5082 -236 364 192 N ATOM 1013 CA PHE B 179 -15.402 1.942 -27.321 1.00 35.14 C ANISOU 1013 CA PHE B 179 3326 4765 5263 -184 410 73 C ATOM 1014 C PHE B 179 -16.151 1.559 -26.042 1.00 39.34 C ANISOU 1014 C PHE B 179 3819 5328 5802 -277 600 49 C ATOM 1015 O PHE B 179 -16.429 2.408 -25.195 1.00 37.75 O ANISOU 1015 O PHE B 179 3642 5149 5551 -251 688 10 O ATOM 1016 CB PHE B 179 -16.331 1.810 -28.534 1.00 31.11 C ANISOU 1016 CB PHE B 179 2619 4329 4874 -135 323 -20 C ATOM 1017 CG PHE B 179 -17.468 2.791 -28.549 1.00 37.28 C ANISOU 1017 CG PHE B 179 3239 5218 5707 9 348 -97 C ATOM 1018 CD1 PHE B 179 -17.352 3.994 -29.231 1.00 40.66 C ANISOU 1018 CD1 PHE B 179 3698 5638 6112 222 268 -65 C ATOM 1019 CD2 PHE B 179 -18.660 2.505 -27.902 1.00 41.63 C ANISOU 1019 CD2 PHE B 179 3613 5875 6331 -48 481 -185 C ATOM 1020 CE1 PHE B 179 -18.400 4.895 -29.256 1.00 44.60 C ANISOU 1020 CE1 PHE B 179 4058 6230 6658 423 330 -90 C ATOM 1021 CE2 PHE B 179 -19.713 3.400 -27.924 1.00 46.11 C ANISOU 1021 CE2 PHE B 179 4005 6571 6944 129 519 -233 C ATOM 1022 CZ PHE B 179 -19.586 4.598 -28.600 1.00 45.34 C ANISOU 1022 CZ PHE B 179 3943 6462 6822 388 448 -171 C ATOM 1023 N THR B 180 -16.469 0.272 -25.922 1.00 37.43 N ANISOU 1023 N THR B 180 3541 5061 5621 -397 700 63 N ATOM 1024 CA THR B 180 -17.221 -0.256 -24.789 1.00 38.36 C ANISOU 1024 CA THR B 180 3633 5188 5754 -501 914 47 C ATOM 1025 C THR B 180 -16.554 0.036 -23.452 1.00 37.68 C ANISOU 1025 C THR B 180 3703 5127 5489 -496 998 162 C ATOM 1026 O THR B 180 -17.212 0.436 -22.491 1.00 42.47 O ANISOU 1026 O THR B 180 4282 5786 6069 -525 1128 105 O ATOM 1027 CB THR B 180 -17.408 -1.776 -24.917 1.00 44.23 C ANISOU 1027 CB THR B 180 4393 5831 6579 -648 1066 69 C ATOM 1028 OG1 THR B 180 -18.237 -2.056 -26.049 1.00 51.18 O ANISOU 1028 OG1 THR B 180 5084 6761 7601 -729 1019 -108 O ATOM 1029 CG2 THR B 180 -18.051 -2.349 -23.660 1.00 45.88 C ANISOU 1029 CG2 THR B 180 4628 6018 6785 -755 1329 87 C ATOM 1030 N SER B 181 -15.243 -0.166 -23.402 1.00 35.62 N ANISOU 1030 N SER B 181 3583 4869 5081 -460 925 317 N ATOM 1031 CA SER B 181 -14.489 0.009 -22.170 1.00 35.83 C ANISOU 1031 CA SER B 181 3717 5024 4874 -467 981 435 C ATOM 1032 C SER B 181 -14.505 1.469 -21.717 1.00 39.90 C ANISOU 1032 C SER B 181 4239 5630 5291 -484 949 295 C ATOM 1033 O SER B 181 -14.646 1.755 -20.527 1.00 40.48 O ANISOU 1033 O SER B 181 4347 5814 5220 -550 1073 277 O ATOM 1034 CB SER B 181 -13.054 -0.483 -22.352 1.00 34.54 C ANISOU 1034 CB SER B 181 3642 4922 4559 -401 890 632 C ATOM 1035 OG SER B 181 -12.336 -0.409 -21.132 1.00 39.35 O ANISOU 1035 OG SER B 181 4302 5759 4891 -404 936 760 O ATOM 1036 N ILE B 182 -14.377 2.387 -22.670 1.00 38.03 N ANISOU 1036 N ILE B 182 3993 5330 5128 -428 821 194 N ATOM 1037 CA ILE B 182 -14.442 3.810 -22.363 1.00 41.94 C ANISOU 1037 CA ILE B 182 4543 5827 5566 -438 863 50 C ATOM 1038 C ILE B 182 -15.846 4.181 -21.886 1.00 45.42 C ANISOU 1038 C ILE B 182 4905 6222 6130 -413 1029 -67 C ATOM 1039 O ILE B 182 -16.001 4.985 -20.967 1.00 48.22 O ANISOU 1039 O ILE B 182 5332 6598 6389 -470 1177 -165 O ATOM 1040 CB ILE B 182 -14.049 4.682 -23.581 1.00 39.73 C ANISOU 1040 CB ILE B 182 4302 5437 5354 -347 739 1 C ATOM 1041 CG1 ILE B 182 -12.585 4.446 -23.957 1.00 36.35 C ANISOU 1041 CG1 ILE B 182 3947 5080 4784 -394 597 94 C ATOM 1042 CG2 ILE B 182 -14.271 6.157 -23.282 1.00 39.69 C ANISOU 1042 CG2 ILE B 182 4401 5350 5328 -340 875 -148 C ATOM 1043 CD1 ILE B 182 -12.084 5.351 -25.073 1.00 35.85 C ANISOU 1043 CD1 ILE B 182 3956 4905 4762 -333 508 44 C ATOM 1044 N VAL B 183 -16.861 3.577 -22.500 1.00 42.72 N ANISOU 1044 N VAL B 183 4402 5843 5987 -347 1023 -74 N ATOM 1045 CA VAL B 183 -18.243 3.808 -22.095 1.00 47.05 C ANISOU 1045 CA VAL B 183 4815 6407 6656 -315 1179 -178 C ATOM 1046 C VAL B 183 -18.448 3.357 -20.651 1.00 46.60 C ANISOU 1046 C VAL B 183 4805 6409 6491 -454 1368 -170 C ATOM 1047 O VAL B 183 -19.166 3.996 -19.883 1.00 49.52 O ANISOU 1047 O VAL B 183 5161 6792 6862 -453 1537 -269 O ATOM 1048 CB VAL B 183 -19.243 3.078 -23.023 1.00 50.35 C ANISOU 1048 CB VAL B 183 4996 6868 7266 -278 1128 -209 C ATOM 1049 CG1 VAL B 183 -20.648 3.122 -22.444 1.00 54.81 C ANISOU 1049 CG1 VAL B 183 5376 7517 7932 -281 1307 -314 C ATOM 1050 CG2 VAL B 183 -19.229 3.701 -24.404 1.00 50.15 C ANISOU 1050 CG2 VAL B 183 4895 6846 7313 -104 954 -218 C ATOM 1051 N GLN B 184 -17.782 2.270 -20.280 1.00 54.93 N ANISOU 1051 N GLN B 184 4817 8765 7288 634 1696 200 N ATOM 1052 CA GLN B 184 -17.886 1.738 -18.930 1.00 54.24 C ANISOU 1052 CA GLN B 184 4838 8650 7121 364 1776 46 C ATOM 1053 C GLN B 184 -16.810 2.318 -18.004 1.00 52.75 C ANISOU 1053 C GLN B 184 5100 8024 6918 277 1920 -145 C ATOM 1054 O GLN B 184 -16.358 1.653 -17.073 1.00 53.89 O ANISOU 1054 O GLN B 184 5397 8119 6959 -46 1856 -272 O ATOM 1055 CB GLN B 184 -17.799 0.213 -18.965 1.00 51.26 C ANISOU 1055 CB GLN B 184 4388 8443 6645 -60 1490 0 C ATOM 1056 CG GLN B 184 -18.904 -0.438 -19.779 1.00 55.27 C ANISOU 1056 CG GLN B 184 4470 9438 7092 -124 1371 136 C ATOM 1057 CD GLN B 184 -18.906 -1.947 -19.657 1.00 59.70 C ANISOU 1057 CD GLN B 184 5051 10098 7533 -599 1196 52 C ATOM 1058 OE1 GLN B 184 -18.326 -2.508 -18.728 1.00 58.63 O ANISOU 1058 OE1 GLN B 184 5192 9716 7367 -813 1209 -62 O ATOM 1059 NE2 GLN B 184 -19.558 -2.614 -20.598 1.00 65.50 N ANISOU 1059 NE2 GLN B 184 5508 11206 8173 -784 1058 119 N ATOM 1060 N HIS B 185 -16.416 3.562 -18.270 1.00 49.53 N ANISOU 1060 N HIS B 185 4903 7331 6585 545 2130 -151 N ATOM 1061 CA HIS B 185 -15.419 4.277 -17.468 1.00 49.18 C ANISOU 1061 CA HIS B 185 5299 6908 6480 406 2313 -355 C ATOM 1062 C HIS B 185 -14.126 3.488 -17.296 1.00 45.17 C ANISOU 1062 C HIS B 185 4950 6346 5865 13 2005 -461 C ATOM 1063 O HIS B 185 -13.665 3.282 -16.171 1.00 45.58 O ANISOU 1063 O HIS B 185 5175 6374 5768 -280 2040 -598 O ATOM 1064 CB HIS B 185 -15.995 4.639 -16.098 1.00 46.83 C ANISOU 1064 CB HIS B 185 5117 6576 6099 354 2658 -478 C ATOM 1065 CG HIS B 185 -17.102 5.644 -16.158 1.00 62.13 C ANISOU 1065 CG HIS B 185 6981 8482 8143 806 3076 -367 C ATOM 1066 ND1 HIS B 185 -18.370 5.332 -16.604 1.00 66.35 N ANISOU 1066 ND1 HIS B 185 7057 9404 8750 1088 3064 -132 N ATOM 1067 CD2 HIS B 185 -17.130 6.959 -15.839 1.00 65.23 C ANISOU 1067 CD2 HIS B 185 7704 8513 8566 1039 3560 -434 C ATOM 1068 CE1 HIS B 185 -19.130 6.410 -16.552 1.00 71.57 C ANISOU 1068 CE1 HIS B 185 7724 9973 9494 1540 3511 -16 C ATOM 1069 NE2 HIS B 185 -18.403 7.411 -16.092 1.00 72.33 N ANISOU 1069 NE2 HIS B 185 8335 9566 9582 1532 3845 -202 N ATOM 1070 N HIS B 186 -13.575 3.041 -18.424 1.00 40.72 N ANISOU 1070 N HIS B 186 4304 5803 5363 27 1718 -369 N ATOM 1071 CA HIS B 186 -12.287 2.337 -18.501 1.00 40.08 C ANISOU 1071 CA HIS B 186 4347 5673 5207 -243 1449 -406 C ATOM 1072 C HIS B 186 -12.316 0.925 -17.905 1.00 41.60 C ANISOU 1072 C HIS B 186 4442 6052 5313 -501 1268 -376 C ATOM 1073 O HIS B 186 -11.285 0.259 -17.856 1.00 46.05 O ANISOU 1073 O HIS B 186 5096 6594 5808 -673 1089 -353 O ATOM 1074 CB HIS B 186 -11.173 3.152 -17.826 1.00 44.16 C ANISOU 1074 CB HIS B 186 5189 5988 5600 -413 1573 -561 C ATOM 1075 CG HIS B 186 -10.992 4.524 -18.393 1.00 51.68 C ANISOU 1075 CG HIS B 186 6339 6675 6620 -215 1800 -612 C ATOM 1076 ND1 HIS B 186 -10.133 5.451 -17.840 1.00 59.16 N ANISOU 1076 ND1 HIS B 186 7626 7419 7431 -413 1999 -792 N ATOM 1077 CD2 HIS B 186 -11.558 5.130 -19.465 1.00 53.98 C ANISOU 1077 CD2 HIS B 186 6554 6881 7077 146 1887 -493 C ATOM 1078 CE1 HIS B 186 -10.180 6.565 -18.544 1.00 63.68 C ANISOU 1078 CE1 HIS B 186 8371 7720 8102 -177 2230 -797 C ATOM 1079 NE2 HIS B 186 -11.036 6.399 -19.535 1.00 62.03 N ANISOU 1079 NE2 HIS B 186 7902 7581 8085 200 2161 -593 N ATOM 1080 N HIS B 187 -13.479 0.458 -17.465 1.00 41.05 N ANISOU 1080 N HIS B 187 4190 6169 5237 -512 1341 -350 N ATOM 1081 CA HIS B 187 -13.569 -0.911 -16.965 1.00 42.76 C ANISOU 1081 CA HIS B 187 4355 6522 5370 -762 1211 -311 C ATOM 1082 C HIS B 187 -13.281 -1.894 -18.090 1.00 42.76 C ANISOU 1082 C HIS B 187 4295 6528 5424 -807 986 -217 C ATOM 1083 O HIS B 187 -13.811 -1.760 -19.193 1.00 44.63 O ANISOU 1083 O HIS B 187 4366 6848 5744 -683 936 -173 O ATOM 1084 CB HIS B 187 -14.942 -1.199 -16.356 1.00 46.13 C ANISOU 1084 CB HIS B 187 4589 7170 5768 -798 1349 -312 C ATOM 1085 CG HIS B 187 -15.104 -2.614 -15.887 1.00 50.22 C ANISOU 1085 CG HIS B 187 5094 7793 6194 -1077 1257 -274 C ATOM 1086 ND1 HIS B 187 -14.265 -3.190 -14.957 1.00 53.60 N ANISOU 1086 ND1 HIS B 187 5724 8138 6503 -1264 1225 -264 N ATOM 1087 CD2 HIS B 187 -16.003 -3.569 -16.225 1.00 51.96 C ANISOU 1087 CD2 HIS B 187 5139 8204 6401 -1216 1219 -229 C ATOM 1088 CE1 HIS B 187 -14.642 -4.438 -14.740 1.00 54.64 C ANISOU 1088 CE1 HIS B 187 5840 8340 6580 -1458 1196 -200 C ATOM 1089 NE2 HIS B 187 -15.692 -4.694 -15.498 1.00 53.62 N ANISOU 1089 NE2 HIS B 187 5506 8360 6509 -1469 1199 -205 N ATOM 1090 N TRP B 188 -12.433 -2.878 -17.805 1.00 45.05 N ANISOU 1090 N TRP B 188 4728 6744 5647 -979 878 -169 N ATOM 1091 CA TRP B 188 -12.023 -3.865 -18.803 1.00 42.94 C ANISOU 1091 CA TRP B 188 4492 6401 5422 -1028 738 -90 C ATOM 1092 C TRP B 188 -12.424 -5.283 -18.391 1.00 47.60 C ANISOU 1092 C TRP B 188 5130 7016 5941 -1252 772 -38 C ATOM 1093 O TRP B 188 -11.719 -5.940 -17.621 1.00 50.31 O ANISOU 1093 O TRP B 188 5635 7274 6208 -1319 791 51 O ATOM 1094 CB TRP B 188 -10.512 -3.793 -19.027 1.00 36.50 C ANISOU 1094 CB TRP B 188 3842 5421 4605 -965 639 -31 C ATOM 1095 CG TRP B 188 -10.025 -4.627 -20.177 1.00 36.98 C ANISOU 1095 CG TRP B 188 3964 5358 4729 -959 545 42 C ATOM 1096 CD1 TRP B 188 -9.544 -5.905 -20.122 1.00 39.03 C ANISOU 1096 CD1 TRP B 188 4369 5504 4956 -1042 563 155 C ATOM 1097 CD2 TRP B 188 -9.965 -4.234 -21.550 1.00 36.80 C ANISOU 1097 CD2 TRP B 188 3892 5292 4801 -857 463 13 C ATOM 1098 NE1 TRP B 188 -9.191 -6.332 -21.378 1.00 39.87 N ANISOU 1098 NE1 TRP B 188 4543 5473 5134 -1015 521 169 N ATOM 1099 CE2 TRP B 188 -9.439 -5.325 -22.275 1.00 40.50 C ANISOU 1099 CE2 TRP B 188 4489 5619 5282 -922 435 77 C ATOM 1100 CE3 TRP B 188 -10.304 -3.067 -22.242 1.00 34.48 C ANISOU 1100 CE3 TRP B 188 3477 5052 4574 -701 442 -41 C ATOM 1101 CZ2 TRP B 188 -9.245 -5.282 -23.656 1.00 36.10 C ANISOU 1101 CZ2 TRP B 188 3930 5001 4784 -883 363 56 C ATOM 1102 CZ3 TRP B 188 -10.113 -3.026 -23.614 1.00 35.05 C ANISOU 1102 CZ3 TRP B 188 3524 5089 4705 -639 348 -26 C ATOM 1103 CH2 TRP B 188 -9.587 -4.128 -24.305 1.00 34.43 C ANISOU 1103 CH2 TRP B 188 3563 4898 4621 -754 297 6 C ATOM 1104 N PRO B 189 -13.569 -5.758 -18.899 1.00 48.64 N ANISOU 1104 N PRO B 189 5117 7293 6070 -1381 800 -76 N ATOM 1105 CA PRO B 189 -14.050 -7.096 -18.555 1.00 52.10 C ANISOU 1105 CA PRO B 189 5644 7732 6420 -1661 883 -59 C ATOM 1106 C PRO B 189 -13.732 -8.157 -19.609 1.00 50.26 C ANISOU 1106 C PRO B 189 5581 7327 6190 -1811 874 -43 C ATOM 1107 O PRO B 189 -14.404 -9.187 -19.635 1.00 52.96 O ANISOU 1107 O PRO B 189 5994 7684 6443 -2108 984 -78 O ATOM 1108 CB PRO B 189 -15.558 -6.886 -18.449 1.00 55.03 C ANISOU 1108 CB PRO B 189 5730 8439 6740 -1777 946 -132 C ATOM 1109 CG PRO B 189 -15.836 -5.860 -19.517 1.00 52.80 C ANISOU 1109 CG PRO B 189 5209 8318 6536 -1566 857 -141 C ATOM 1110 CD PRO B 189 -14.607 -4.965 -19.584 1.00 49.46 C ANISOU 1110 CD PRO B 189 4937 7643 6214 -1286 796 -119 C ATOM 1111 N PHE B 190 -12.728 -7.925 -20.448 1.00 44.61 N ANISOU 1111 N PHE B 190 4959 6435 5556 -1643 782 -7 N ATOM 1112 CA PHE B 190 -12.496 -8.797 -21.600 1.00 43.86 C ANISOU 1112 CA PHE B 190 5029 6177 5461 -1784 805 -23 C ATOM 1113 C PHE B 190 -11.326 -9.753 -21.404 1.00 42.80 C ANISOU 1113 C PHE B 190 5240 5680 5343 -1723 918 112 C ATOM 1114 O PHE B 190 -11.044 -10.580 -22.270 1.00 45.62 O ANISOU 1114 O PHE B 190 5818 5817 5700 -1829 1017 102 O ATOM 1115 CB PHE B 190 -12.276 -7.958 -22.859 1.00 40.82 C ANISOU 1115 CB PHE B 190 4504 5861 5145 -1642 654 -64 C ATOM 1116 CG PHE B 190 -13.382 -6.987 -23.130 1.00 41.96 C ANISOU 1116 CG PHE B 190 4292 6378 5274 -1608 575 -118 C ATOM 1117 CD1 PHE B 190 -14.586 -7.423 -23.654 1.00 46.87 C ANISOU 1117 CD1 PHE B 190 4726 7309 5774 -1894 591 -180 C ATOM 1118 CD2 PHE B 190 -13.223 -5.638 -22.849 1.00 41.29 C ANISOU 1118 CD2 PHE B 190 4061 6354 5271 -1297 519 -87 C ATOM 1119 CE1 PHE B 190 -15.614 -6.535 -23.900 1.00 50.68 C ANISOU 1119 CE1 PHE B 190 4817 8213 6226 -1801 531 -156 C ATOM 1120 CE2 PHE B 190 -14.246 -4.741 -23.094 1.00 46.46 C ANISOU 1120 CE2 PHE B 190 4403 7325 5924 -1182 511 -79 C ATOM 1121 CZ PHE B 190 -15.445 -5.190 -23.621 1.00 49.92 C ANISOU 1121 CZ PHE B 190 4591 8127 6249 -1399 506 -86 C ATOM 1122 N GLY B 191 -10.648 -9.636 -20.269 1.00 40.44 N ANISOU 1122 N GLY B 191 4985 5346 5035 -1551 929 255 N ATOM 1123 CA GLY B 191 -9.560 -10.541 -19.942 1.00 42.68 C ANISOU 1123 CA GLY B 191 5535 5371 5310 -1425 1054 470 C ATOM 1124 C GLY B 191 -8.179 -10.020 -20.289 1.00 42.58 C ANISOU 1124 C GLY B 191 5503 5319 5355 -1130 941 599 C ATOM 1125 O GLY B 191 -8.032 -8.995 -20.956 1.00 43.03 O ANISOU 1125 O GLY B 191 5398 5480 5471 -1056 775 488 O ATOM 1126 N GLY B 192 -7.160 -10.742 -19.837 1.00 41.22 N ANISOU 1126 N GLY B 192 5490 5017 5154 -950 1052 865 N ATOM 1127 CA GLY B 192 -5.783 -10.331 -20.030 1.00 35.99 C ANISOU 1127 CA GLY B 192 4763 4408 4506 -676 955 1038 C ATOM 1128 C GLY B 192 -5.333 -10.430 -21.468 1.00 37.03 C ANISOU 1128 C GLY B 192 4991 4327 4751 -599 969 981 C ATOM 1129 O GLY B 192 -4.622 -9.557 -21.956 1.00 36.59 O ANISOU 1129 O GLY B 192 4789 4386 4726 -475 804 962 O ATOM 1130 N ALA B 193 -5.752 -11.499 -22.142 1.00 40.10 N ANISOU 1130 N ALA B 193 5656 4400 5180 -715 1192 937 N ATOM 1131 CA ALA B 193 -5.374 -11.761 -23.527 1.00 37.40 C ANISOU 1131 CA ALA B 193 5469 3823 4917 -694 1264 866 C ATOM 1132 C ALA B 193 -5.826 -10.643 -24.458 1.00 38.05 C ANISOU 1132 C ALA B 193 5329 4094 5036 -814 1016 608 C ATOM 1133 O ALA B 193 -5.041 -10.128 -25.255 1.00 40.98 O ANISOU 1133 O ALA B 193 5648 4460 5463 -661 919 616 O ATOM 1134 CB ALA B 193 -5.950 -13.092 -23.983 1.00 41.54 C ANISOU 1134 CB ALA B 193 6378 3982 5425 -922 1596 800 C ATOM 1135 N ALA B 194 -7.096 -10.268 -24.347 1.00 34.09 N ANISOU 1135 N ALA B 194 4681 3780 4492 -1065 931 412 N ATOM 1136 CA ALA B 194 -7.651 -9.182 -25.142 1.00 34.88 C ANISOU 1136 CA ALA B 194 4537 4104 4611 -1124 723 232 C ATOM 1137 C ALA B 194 -7.000 -7.846 -24.779 1.00 36.56 C ANISOU 1137 C ALA B 194 4539 4484 4868 -877 530 280 C ATOM 1138 O ALA B 194 -6.828 -6.976 -25.638 1.00 37.47 O ANISOU 1138 O ALA B 194 4547 4660 5028 -802 402 211 O ATOM 1139 CB ALA B 194 -9.154 -9.108 -24.954 1.00 39.89 C ANISOU 1139 CB ALA B 194 5013 4972 5171 -1393 707 84 C ATOM 1140 N CYS B 195 -6.638 -7.689 -23.506 1.00 32.46 N ANISOU 1140 N CYS B 195 3982 4044 4306 -788 533 394 N ATOM 1141 CA CYS B 195 -5.976 -6.474 -23.046 1.00 30.01 C ANISOU 1141 CA CYS B 195 3526 3898 3980 -651 399 410 C ATOM 1142 C CYS B 195 -4.589 -6.329 -23.663 1.00 33.37 C ANISOU 1142 C CYS B 195 3987 4264 4429 -481 348 520 C ATOM 1143 O CYS B 195 -4.121 -5.215 -23.902 1.00 29.55 O ANISOU 1143 O CYS B 195 3407 3874 3945 -428 236 460 O ATOM 1144 CB CYS B 195 -5.873 -6.456 -21.520 1.00 30.83 C ANISOU 1144 CB CYS B 195 3592 4153 3970 -673 429 502 C ATOM 1145 SG CYS B 195 -4.850 -5.113 -20.844 1.00 38.54 S ANISOU 1145 SG CYS B 195 4449 5358 4837 -626 315 511 S ATOM 1146 N SER B 196 -3.933 -7.453 -23.925 1.00 31.96 N ANISOU 1146 N SER B 196 3964 3916 4264 -392 468 687 N ATOM 1147 CA SER B 196 -2.625 -7.411 -24.562 1.00 32.77 C ANISOU 1147 CA SER B 196 4079 3983 4389 -203 450 818 C ATOM 1148 C SER B 196 -2.729 -7.138 -26.068 1.00 31.91 C ANISOU 1148 C SER B 196 4019 3730 4375 -229 411 657 C ATOM 1149 O SER B 196 -1.928 -6.395 -26.628 1.00 33.38 O ANISOU 1149 O SER B 196 4129 3978 4576 -134 308 657 O ATOM 1150 CB SER B 196 -1.873 -8.718 -24.315 1.00 35.72 C ANISOU 1150 CB SER B 196 4611 4212 4749 -24 657 1102 C ATOM 1151 OG SER B 196 -1.525 -8.855 -22.950 1.00 41.69 O ANISOU 1151 OG SER B 196 5266 5194 5382 45 661 1323 O ATOM 1152 N ILE B 197 -3.741 -7.717 -26.707 1.00 31.33 N ANISOU 1152 N ILE B 197 4063 3509 4331 -401 494 515 N ATOM 1153 CA ILE B 197 -3.838 -7.741 -28.164 1.00 31.26 C ANISOU 1153 CA ILE B 197 4129 3386 4363 -472 492 388 C ATOM 1154 C ILE B 197 -4.580 -6.546 -28.773 1.00 33.70 C ANISOU 1154 C ILE B 197 4235 3895 4675 -548 298 223 C ATOM 1155 O ILE B 197 -4.029 -5.808 -29.599 1.00 31.23 O ANISOU 1155 O ILE B 197 3873 3598 4394 -453 199 204 O ATOM 1156 CB ILE B 197 -4.532 -9.044 -28.627 1.00 32.15 C ANISOU 1156 CB ILE B 197 4494 3281 4441 -702 713 311 C ATOM 1157 CG1 ILE B 197 -3.715 -10.260 -28.176 1.00 32.37 C ANISOU 1157 CG1 ILE B 197 4798 3018 4485 -554 992 517 C ATOM 1158 CG2 ILE B 197 -4.737 -9.039 -30.136 1.00 29.86 C ANISOU 1158 CG2 ILE B 197 4268 2945 4132 -864 705 149 C ATOM 1159 CD1 ILE B 197 -4.361 -11.590 -28.486 1.00 37.20 C ANISOU 1159 CD1 ILE B 197 5759 3328 5048 -812 1302 432 C ATOM 1160 N LEU B 198 -5.830 -6.358 -28.369 1.00 33.06 N ANISOU 1160 N LEU B 198 4030 3977 4556 -694 269 133 N ATOM 1161 CA LEU B 198 -6.683 -5.353 -28.996 1.00 35.07 C ANISOU 1161 CA LEU B 198 4074 4448 4802 -717 138 40 C ATOM 1162 C LEU B 198 -6.125 -3.912 -28.933 1.00 31.91 C ANISOU 1162 C LEU B 198 3569 4097 4457 -490 32 66 C ATOM 1163 O LEU B 198 -6.109 -3.223 -29.954 1.00 34.16 O ANISOU 1163 O LEU B 198 3797 4423 4760 -426 -44 47 O ATOM 1164 CB LEU B 198 -8.083 -5.424 -28.383 1.00 37.09 C ANISOU 1164 CB LEU B 198 4176 4919 4998 -866 159 -10 C ATOM 1165 CG LEU B 198 -8.710 -6.807 -28.579 1.00 38.04 C ANISOU 1165 CG LEU B 198 4425 5005 5025 -1182 286 -73 C ATOM 1166 CD1 LEU B 198 -10.132 -6.852 -28.050 1.00 39.94 C ANISOU 1166 CD1 LEU B 198 4463 5536 5176 -1370 297 -123 C ATOM 1167 CD2 LEU B 198 -8.662 -7.207 -30.051 1.00 36.18 C ANISOU 1167 CD2 LEU B 198 4272 4748 4726 -1354 287 -150 C ATOM 1168 N PRO B 199 -5.650 -3.452 -27.754 1.00 30.48 N ANISOU 1168 N PRO B 199 3389 3916 4276 -405 49 106 N ATOM 1169 CA PRO B 199 -5.072 -2.099 -27.774 1.00 28.50 C ANISOU 1169 CA PRO B 199 3111 3674 4043 -274 3 90 C ATOM 1170 C PRO B 199 -3.749 -2.027 -28.547 1.00 31.12 C ANISOU 1170 C PRO B 199 3528 3908 4387 -211 -46 134 C ATOM 1171 O PRO B 199 -3.281 -0.931 -28.869 1.00 30.37 O ANISOU 1171 O PRO B 199 3438 3802 4297 -146 -75 104 O ATOM 1172 CB PRO B 199 -4.855 -1.782 -26.287 1.00 26.79 C ANISOU 1172 CB PRO B 199 2901 3517 3760 -304 57 94 C ATOM 1173 CG PRO B 199 -5.742 -2.760 -25.543 1.00 26.76 C ANISOU 1173 CG PRO B 199 2869 3567 3730 -406 116 110 C ATOM 1174 CD PRO B 199 -5.731 -3.990 -26.384 1.00 27.67 C ANISOU 1174 CD PRO B 199 3058 3583 3871 -462 123 151 C ATOM 1175 N SER B 200 -3.164 -3.183 -28.852 1.00 31.53 N ANISOU 1175 N SER B 200 3668 3871 4441 -226 -16 209 N ATOM 1176 CA SER B 200 -1.911 -3.243 -29.599 1.00 28.43 C ANISOU 1176 CA SER B 200 3337 3403 4060 -140 -31 274 C ATOM 1177 C SER B 200 -2.105 -3.137 -31.113 1.00 27.48 C ANISOU 1177 C SER B 200 3253 3207 3981 -152 -66 201 C ATOM 1178 O SER B 200 -1.151 -2.880 -31.855 1.00 28.79 O ANISOU 1178 O SER B 200 3456 3325 4157 -82 -89 227 O ATOM 1179 CB SER B 200 -1.166 -4.545 -29.289 1.00 26.50 C ANISOU 1179 CB SER B 200 3190 3074 3805 -82 84 430 C ATOM 1180 OG SER B 200 -0.526 -4.506 -28.030 1.00 27.55 O ANISOU 1180 OG SER B 200 3245 3363 3858 -30 86 569 O ATOM 1181 N LEU B 201 -3.328 -3.359 -31.581 1.00 23.18 N ANISOU 1181 N LEU B 201 2675 2704 3427 -265 -71 120 N ATOM 1182 CA LEU B 201 -3.564 -3.399 -33.019 1.00 28.09 C ANISOU 1182 CA LEU B 201 3313 3330 4029 -333 -107 65 C ATOM 1183 C LEU B 201 -3.360 -2.025 -33.683 1.00 30.64 C ANISOU 1183 C LEU B 201 3550 3721 4371 -203 -212 72 C ATOM 1184 O LEU B 201 -3.035 -1.953 -34.865 1.00 27.75 O ANISOU 1184 O LEU B 201 3222 3334 3986 -214 -246 61 O ATOM 1185 CB LEU B 201 -4.967 -3.941 -33.317 1.00 24.46 C ANISOU 1185 CB LEU B 201 2780 3024 3489 -547 -99 -6 C ATOM 1186 CG LEU B 201 -5.187 -5.422 -32.951 1.00 27.56 C ANISOU 1186 CG LEU B 201 3346 3288 3837 -755 63 -45 C ATOM 1187 CD1 LEU B 201 -6.637 -5.853 -33.159 1.00 28.40 C ANISOU 1187 CD1 LEU B 201 3349 3626 3816 -1050 67 -137 C ATOM 1188 CD2 LEU B 201 -4.242 -6.331 -33.736 1.00 26.71 C ANISOU 1188 CD2 LEU B 201 3506 2912 3729 -793 207 -56 C ATOM 1189 N ILE B 202 -3.525 -0.941 -32.927 1.00 28.92 N ANISOU 1189 N ILE B 202 3256 3553 4178 -89 -224 88 N ATOM 1190 CA ILE B 202 -3.320 0.384 -33.504 1.00 26.64 C ANISOU 1190 CA ILE B 202 2960 3255 3907 43 -251 103 C ATOM 1191 C ILE B 202 -1.829 0.633 -33.708 1.00 26.71 C ANISOU 1191 C ILE B 202 3090 3140 3918 57 -253 104 C ATOM 1192 O ILE B 202 -1.436 1.304 -34.666 1.00 27.37 O ANISOU 1192 O ILE B 202 3214 3185 4003 109 -278 112 O ATOM 1193 CB ILE B 202 -3.957 1.519 -32.632 1.00 26.71 C ANISOU 1193 CB ILE B 202 2928 3285 3935 157 -171 107 C ATOM 1194 CG1 ILE B 202 -3.798 2.900 -33.297 1.00 25.63 C ANISOU 1194 CG1 ILE B 202 2855 3067 3817 316 -121 143 C ATOM 1195 CG2 ILE B 202 -3.385 1.533 -31.210 1.00 27.78 C ANISOU 1195 CG2 ILE B 202 3140 3366 4050 86 -104 58 C ATOM 1196 CD1 ILE B 202 -4.393 3.010 -34.685 1.00 23.19 C ANISOU 1196 CD1 ILE B 202 2437 2883 3493 407 -193 241 C ATOM 1197 N LEU B 203 -0.998 0.074 -32.830 1.00 24.67 N ANISOU 1197 N LEU B 203 2865 2867 3641 13 -225 123 N ATOM 1198 CA LEU B 203 0.449 0.218 -32.960 1.00 22.82 C ANISOU 1198 CA LEU B 203 2674 2623 3374 18 -230 161 C ATOM 1199 C LEU B 203 0.982 -0.664 -34.091 1.00 26.74 C ANISOU 1199 C LEU B 203 3220 3047 3895 46 -226 201 C ATOM 1200 O LEU B 203 1.860 -0.250 -34.854 1.00 26.86 O ANISOU 1200 O LEU B 203 3263 3046 3897 70 -242 210 O ATOM 1201 CB LEU B 203 1.146 -0.122 -31.644 1.00 31.19 C ANISOU 1201 CB LEU B 203 3688 3802 4362 -22 -202 230 C ATOM 1202 CG LEU B 203 2.631 0.250 -31.550 1.00 36.64 C ANISOU 1202 CG LEU B 203 4339 4628 4955 -54 -216 294 C ATOM 1203 CD1 LEU B 203 2.842 1.763 -31.666 1.00 35.08 C ANISOU 1203 CD1 LEU B 203 4207 4425 4697 -168 -210 171 C ATOM 1204 CD2 LEU B 203 3.208 -0.252 -30.256 1.00 39.91 C ANISOU 1204 CD2 LEU B 203 4642 5269 5254 -90 -205 420 C ATOM 1205 N LEU B 204 0.450 -1.883 -34.187 1.00 23.52 N ANISOU 1205 N LEU B 204 2854 2576 3507 16 -168 210 N ATOM 1206 CA LEU B 204 0.736 -2.759 -35.315 1.00 22.91 C ANISOU 1206 CA LEU B 204 2894 2376 3436 -4 -97 204 C ATOM 1207 C LEU B 204 0.414 -2.042 -36.622 1.00 30.36 C ANISOU 1207 C LEU B 204 3832 3347 4356 -53 -183 125 C ATOM 1208 O LEU B 204 1.193 -2.069 -37.580 1.00 31.92 O ANISOU 1208 O LEU B 204 4101 3481 4545 -36 -161 126 O ATOM 1209 CB LEU B 204 -0.072 -4.049 -35.218 1.00 22.89 C ANISOU 1209 CB LEU B 204 2998 2277 3423 -121 24 171 C ATOM 1210 CG LEU B 204 0.175 -5.059 -36.341 1.00 30.73 C ANISOU 1210 CG LEU B 204 4196 3086 4393 -205 180 124 C ATOM 1211 CD1 LEU B 204 1.645 -5.446 -36.396 1.00 32.53 C ANISOU 1211 CD1 LEU B 204 4508 3185 4668 4 315 262 C ATOM 1212 CD2 LEU B 204 -0.701 -6.288 -36.169 1.00 30.73 C ANISOU 1212 CD2 LEU B 204 4360 2966 4348 -404 349 55 C ATOM 1213 N ASN B 205 -0.742 -1.388 -36.640 1.00 27.76 N ANISOU 1213 N ASN B 205 3401 3140 4008 -91 -267 88 N ATOM 1214 CA ASN B 205 -1.171 -0.639 -37.805 1.00 27.78 C ANISOU 1214 CA ASN B 205 3355 3234 3965 -94 -348 81 C ATOM 1215 C ASN B 205 -0.183 0.478 -38.131 1.00 26.67 C ANISOU 1215 C ASN B 205 3256 3030 3850 27 -370 115 C ATOM 1216 O ASN B 205 0.044 0.783 -39.295 1.00 29.41 O ANISOU 1216 O ASN B 205 3634 3384 4157 22 -403 121 O ATOM 1217 CB ASN B 205 -2.578 -0.063 -37.593 1.00 30.94 C ANISOU 1217 CB ASN B 205 3587 3832 4337 -71 -403 113 C ATOM 1218 CG ASN B 205 -3.076 0.722 -38.805 1.00 37.48 C ANISOU 1218 CG ASN B 205 4321 4825 5094 -19 -479 184 C ATOM 1219 OD1 ASN B 205 -2.837 1.924 -38.920 1.00 39.47 O ANISOU 1219 OD1 ASN B 205 4585 5028 5385 168 -471 260 O ATOM 1220 ND2 ASN B 205 -3.761 0.038 -39.715 1.00 35.15 N ANISOU 1220 ND2 ASN B 205 3949 4741 4667 -209 -531 168 N ATOM 1221 N MET B 206 0.416 1.067 -37.101 1.00 23.71 N ANISOU 1221 N MET B 206 2891 2611 3508 87 -339 126 N ATOM 1222 CA MET B 206 1.362 2.163 -37.298 1.00 27.84 C ANISOU 1222 CA MET B 206 3478 3083 4017 120 -327 129 C ATOM 1223 C MET B 206 2.596 1.695 -38.060 1.00 27.68 C ANISOU 1223 C MET B 206 3503 3039 3975 92 -324 142 C ATOM 1224 O MET B 206 3.001 2.305 -39.051 1.00 25.95 O ANISOU 1224 O MET B 206 3339 2788 3733 96 -337 140 O ATOM 1225 CB MET B 206 1.787 2.762 -35.953 1.00 25.64 C ANISOU 1225 CB MET B 206 3211 2817 3715 81 -272 106 C ATOM 1226 CG MET B 206 2.676 3.988 -36.080 1.00 27.64 C ANISOU 1226 CG MET B 206 3569 3023 3908 21 -218 71 C ATOM 1227 SD MET B 206 3.308 4.532 -34.484 1.00 36.07 S ANISOU 1227 SD MET B 206 4658 4187 4861 -165 -139 5 S ATOM 1228 CE MET B 206 4.745 3.504 -34.374 1.00 28.74 C ANISOU 1228 CE MET B 206 3567 3500 3853 -227 -217 103 C ATOM 1229 N TYR B 207 3.194 0.610 -37.578 1.00 26.21 N ANISOU 1229 N TYR B 207 3295 2869 3796 93 -279 182 N ATOM 1230 CA TYR B 207 4.399 0.073 -38.188 1.00 26.44 C ANISOU 1230 CA TYR B 207 3348 2887 3812 128 -224 234 C ATOM 1231 C TYR B 207 4.108 -0.611 -39.518 1.00 22.05 C ANISOU 1231 C TYR B 207 2900 2216 3262 103 -183 188 C ATOM 1232 O TYR B 207 4.897 -0.493 -40.449 1.00 25.70 O ANISOU 1232 O TYR B 207 3408 2655 3701 112 -156 190 O ATOM 1233 CB TYR B 207 5.099 -0.886 -37.225 1.00 24.10 C ANISOU 1233 CB TYR B 207 2986 2656 3514 209 -139 358 C ATOM 1234 CG TYR B 207 5.772 -0.162 -36.082 1.00 26.56 C ANISOU 1234 CG TYR B 207 3159 3189 3743 169 -186 416 C ATOM 1235 CD1 TYR B 207 6.790 0.756 -36.328 1.00 25.18 C ANISOU 1235 CD1 TYR B 207 2933 3156 3480 92 -216 414 C ATOM 1236 CD2 TYR B 207 5.380 -0.373 -34.765 1.00 27.28 C ANISOU 1236 CD2 TYR B 207 3181 3376 3807 151 -191 456 C ATOM 1237 CE1 TYR B 207 7.408 1.439 -35.295 1.00 27.67 C ANISOU 1237 CE1 TYR B 207 3132 3725 3655 -48 -244 434 C ATOM 1238 CE2 TYR B 207 5.997 0.298 -33.716 1.00 31.12 C ANISOU 1238 CE2 TYR B 207 3546 4117 4161 40 -228 489 C ATOM 1239 CZ TYR B 207 7.011 1.203 -33.988 1.00 31.15 C ANISOU 1239 CZ TYR B 207 3503 4282 4052 -83 -252 469 C ATOM 1240 OH TYR B 207 7.617 1.873 -32.956 1.00 30.00 O ANISOU 1240 OH TYR B 207 3247 4436 3715 -292 -272 471 O ATOM 1241 N ALA B 208 2.977 -1.309 -39.614 1.00 20.57 N ANISOU 1241 N ALA B 208 2754 1986 3074 25 -168 132 N ATOM 1242 CA ALA B 208 2.624 -1.990 -40.857 1.00 24.11 C ANISOU 1242 CA ALA B 208 3323 2371 3466 -102 -111 53 C ATOM 1243 C ALA B 208 2.349 -0.968 -41.947 1.00 21.88 C ANISOU 1243 C ALA B 208 3001 2197 3116 -147 -238 30 C ATOM 1244 O ALA B 208 2.899 -1.068 -43.037 1.00 24.38 O ANISOU 1244 O ALA B 208 3407 2476 3381 -194 -200 1 O ATOM 1245 CB ALA B 208 1.420 -2.915 -40.659 1.00 23.07 C ANISOU 1245 CB ALA B 208 3234 2239 3293 -267 -63 -19 C ATOM 1246 N SER B 209 1.518 0.028 -41.642 1.00 21.91 N ANISOU 1246 N SER B 209 2880 2329 3116 -105 -359 66 N ATOM 1247 CA SER B 209 1.229 1.092 -42.604 1.00 24.37 C ANISOU 1247 CA SER B 209 3153 2742 3364 -75 -448 114 C ATOM 1248 C SER B 209 2.501 1.771 -43.108 1.00 26.24 C ANISOU 1248 C SER B 209 3480 2876 3613 -16 -423 129 C ATOM 1249 O SER B 209 2.689 1.919 -44.312 1.00 27.99 O ANISOU 1249 O SER B 209 3749 3129 3757 -66 -441 131 O ATOM 1250 CB SER B 209 0.296 2.140 -41.994 1.00 27.80 C ANISOU 1250 CB SER B 209 3470 3268 3824 60 -497 201 C ATOM 1251 OG SER B 209 -0.971 1.577 -41.705 1.00 38.97 O ANISOU 1251 OG SER B 209 4751 4860 5197 -5 -533 207 O ATOM 1252 N ILE B 210 3.385 2.160 -42.193 1.00 25.39 N ANISOU 1252 N ILE B 210 3386 2690 3571 48 -379 136 N ATOM 1253 CA ILE B 210 4.519 2.982 -42.589 1.00 23.78 C ANISOU 1253 CA ILE B 210 3245 2447 3345 52 -353 147 C ATOM 1254 C ILE B 210 5.575 2.158 -43.339 1.00 22.34 C ANISOU 1254 C ILE B 210 3099 2249 3140 16 -294 132 C ATOM 1255 O ILE B 210 6.272 2.684 -44.208 1.00 22.13 O ANISOU 1255 O ILE B 210 3126 2216 3065 -10 -284 134 O ATOM 1256 CB ILE B 210 5.146 3.707 -41.374 1.00 24.69 C ANISOU 1256 CB ILE B 210 3348 2564 3469 40 -314 144 C ATOM 1257 CG1 ILE B 210 6.009 4.882 -41.858 1.00 26.01 C ANISOU 1257 CG1 ILE B 210 3615 2694 3573 -26 -272 134 C ATOM 1258 CG2 ILE B 210 5.919 2.747 -40.467 1.00 22.01 C ANISOU 1258 CG2 ILE B 210 2911 2314 3137 30 -283 167 C ATOM 1259 CD1 ILE B 210 5.228 5.973 -42.592 1.00 25.61 C ANISOU 1259 CD1 ILE B 210 3687 2529 3514 43 -253 170 C ATOM 1260 N LEU B 211 5.670 0.869 -43.022 1.00 20.90 N ANISOU 1260 N LEU B 211 2913 2038 2991 30 -217 128 N ATOM 1261 CA LEU B 211 6.567 -0.030 -43.739 1.00 24.53 C ANISOU 1261 CA LEU B 211 3448 2434 3441 46 -81 130 C ATOM 1262 C LEU B 211 6.033 -0.328 -45.145 1.00 27.41 C ANISOU 1262 C LEU B 211 3941 2748 3724 -85 -66 39 C ATOM 1263 O LEU B 211 6.800 -0.418 -46.107 1.00 26.65 O ANISOU 1263 O LEU B 211 3926 2616 3585 -105 14 20 O ATOM 1264 CB LEU B 211 6.767 -1.326 -42.951 1.00 25.08 C ANISOU 1264 CB LEU B 211 3529 2430 3569 140 72 185 C ATOM 1265 CG LEU B 211 7.685 -1.175 -41.732 1.00 29.93 C ANISOU 1265 CG LEU B 211 3975 3188 4208 276 78 328 C ATOM 1266 CD1 LEU B 211 7.594 -2.381 -40.805 1.00 29.32 C ANISOU 1266 CD1 LEU B 211 3903 3055 4184 403 218 431 C ATOM 1267 CD2 LEU B 211 9.129 -0.923 -42.176 1.00 31.77 C ANISOU 1267 CD2 LEU B 211 4129 3542 4399 347 139 416 C ATOM 1268 N LEU B 212 4.716 -0.470 -45.258 1.00 25.01 N ANISOU 1268 N LEU B 212 3636 2497 3371 -202 -142 -13 N ATOM 1269 CA LEU B 212 4.092 -0.646 -46.561 1.00 25.42 C ANISOU 1269 CA LEU B 212 3758 2624 3277 -394 -163 -86 C ATOM 1270 C LEU B 212 4.275 0.620 -47.387 1.00 28.81 C ANISOU 1270 C LEU B 212 4141 3163 3644 -359 -286 -20 C ATOM 1271 O LEU B 212 4.663 0.548 -48.560 1.00 29.54 O ANISOU 1271 O LEU B 212 4324 3268 3631 -462 -250 -59 O ATOM 1272 CB LEU B 212 2.611 -0.996 -46.418 1.00 25.85 C ANISOU 1272 CB LEU B 212 3743 2835 3245 -553 -238 -122 C ATOM 1273 CG LEU B 212 2.309 -2.431 -45.957 1.00 28.30 C ANISOU 1273 CG LEU B 212 4185 3014 3556 -698 -64 -229 C ATOM 1274 CD1 LEU B 212 0.864 -2.573 -45.491 1.00 26.70 C ANISOU 1274 CD1 LEU B 212 3849 3017 3278 -845 -163 -243 C ATOM 1275 CD2 LEU B 212 2.615 -3.444 -47.067 1.00 26.59 C ANISOU 1275 CD2 LEU B 212 4221 2673 3209 -936 144 -375 C ATOM 1276 N LEU B 213 4.020 1.773 -46.767 1.00 26.42 N ANISOU 1276 N LEU B 213 3734 2907 3400 -216 -389 80 N ATOM 1277 CA LEU B 213 4.202 3.060 -47.445 1.00 28.64 C ANISOU 1277 CA LEU B 213 4026 3224 3633 -151 -446 170 C ATOM 1278 C LEU B 213 5.652 3.255 -47.869 1.00 29.16 C ANISOU 1278 C LEU B 213 4192 3180 3707 -162 -364 139 C ATOM 1279 O LEU B 213 5.920 3.804 -48.932 1.00 31.58 O ANISOU 1279 O LEU B 213 4561 3515 3924 -198 -375 169 O ATOM 1280 CB LEU B 213 3.752 4.220 -46.551 1.00 24.59 C ANISOU 1280 CB LEU B 213 3466 2683 3193 12 -470 268 C ATOM 1281 CG LEU B 213 2.237 4.305 -46.355 1.00 24.81 C ANISOU 1281 CG LEU B 213 3355 2880 3192 79 -544 360 C ATOM 1282 CD1 LEU B 213 1.859 5.435 -45.389 1.00 24.76 C ANISOU 1282 CD1 LEU B 213 3353 2779 3277 276 -487 452 C ATOM 1283 CD2 LEU B 213 1.536 4.466 -47.701 1.00 24.72 C ANISOU 1283 CD2 LEU B 213 3271 3113 3008 44 -629 472 C ATOM 1284 N ALA B 214 6.585 2.788 -47.044 1.00 27.96 N ANISOU 1284 N ALA B 214 4028 2953 3643 -128 -278 103 N ATOM 1285 CA ALA B 214 7.998 2.838 -47.406 1.00 28.64 C ANISOU 1285 CA ALA B 214 4144 3021 3716 -136 -188 99 C ATOM 1286 C ALA B 214 8.255 1.982 -48.654 1.00 30.06 C ANISOU 1286 C ALA B 214 4424 3172 3826 -209 -97 41 C ATOM 1287 O ALA B 214 9.006 2.379 -49.537 1.00 31.21 O ANISOU 1287 O ALA B 214 4622 3329 3907 -249 -62 40 O ATOM 1288 CB ALA B 214 8.875 2.384 -46.239 1.00 25.04 C ANISOU 1288 CB ALA B 214 3583 2601 3331 -62 -115 133 C ATOM 1289 N THR B 215 7.607 0.822 -48.734 1.00 27.33 N ANISOU 1289 N THR B 215 4136 2777 3473 -263 -32 -25 N ATOM 1290 CA THR B 215 7.791 -0.073 -49.873 1.00 28.22 C ANISOU 1290 CA THR B 215 4411 2822 3491 -391 120 -122 C ATOM 1291 C THR B 215 7.141 0.497 -51.123 1.00 29.05 C ANISOU 1291 C THR B 215 4552 3067 3418 -574 -1 -151 C ATOM 1292 O THR B 215 7.727 0.486 -52.207 1.00 31.74 O ANISOU 1292 O THR B 215 4997 3403 3660 -663 76 -194 O ATOM 1293 CB THR B 215 7.204 -1.472 -49.600 1.00 28.65 C ANISOU 1293 CB THR B 215 4587 2751 3548 -473 279 -214 C ATOM 1294 OG1 THR B 215 7.743 -1.989 -48.376 1.00 28.37 O ANISOU 1294 OG1 THR B 215 4501 2608 3669 -259 393 -130 O ATOM 1295 CG2 THR B 215 7.525 -2.410 -50.751 1.00 27.76 C ANISOU 1295 CG2 THR B 215 4720 2505 3322 -638 524 -347 C ATOM 1296 N ILE B 216 5.917 0.987 -50.964 1.00 29.23 N ANISOU 1296 N ILE B 216 4468 3252 3386 -613 -181 -98 N ATOM 1297 CA ILE B 216 5.213 1.650 -52.048 1.00 27.19 C ANISOU 1297 CA ILE B 216 4171 3223 2939 -727 -318 -37 C ATOM 1298 C ILE B 216 6.016 2.842 -52.572 1.00 31.38 C ANISOU 1298 C ILE B 216 4726 3728 3471 -614 -346 66 C ATOM 1299 O ILE B 216 6.109 3.061 -53.783 1.00 30.93 O ANISOU 1299 O ILE B 216 4725 3781 3246 -732 -360 79 O ATOM 1300 CB ILE B 216 3.818 2.121 -51.595 1.00 27.03 C ANISOU 1300 CB ILE B 216 3964 3425 2883 -681 -488 86 C ATOM 1301 CG1 ILE B 216 2.963 0.911 -51.197 1.00 28.11 C ANISOU 1301 CG1 ILE B 216 4079 3632 2969 -874 -457 -34 C ATOM 1302 CG2 ILE B 216 3.145 2.943 -52.702 1.00 28.41 C ANISOU 1302 CG2 ILE B 216 4042 3904 2847 -713 -625 247 C ATOM 1303 CD1 ILE B 216 1.838 1.232 -50.244 1.00 28.47 C ANISOU 1303 CD1 ILE B 216 3922 3829 3064 -764 -576 74 C ATOM 1304 N SER B 217 6.606 3.601 -51.653 1.00 30.82 N ANISOU 1304 N SER B 217 4628 3522 3559 -430 -336 126 N ATOM 1305 CA SER B 217 7.372 4.793 -52.022 1.00 29.83 C ANISOU 1305 CA SER B 217 4566 3345 3424 -373 -324 204 C ATOM 1306 C SER B 217 8.641 4.417 -52.778 1.00 28.77 C ANISOU 1306 C SER B 217 4520 3164 3247 -469 -205 118 C ATOM 1307 O SER B 217 9.042 5.115 -53.707 1.00 31.00 O ANISOU 1307 O SER B 217 4879 3469 3429 -517 -200 161 O ATOM 1308 CB SER B 217 7.726 5.620 -50.782 1.00 23.54 C ANISOU 1308 CB SER B 217 3754 2428 2761 -254 -298 240 C ATOM 1309 OG SER B 217 6.556 5.987 -50.078 1.00 29.09 O ANISOU 1309 OG SER B 217 4395 3148 3510 -141 -364 320 O ATOM 1310 N ALA B 218 9.270 3.316 -52.372 1.00 27.88 N ANISOU 1310 N ALA B 218 4399 2985 3210 -468 -82 22 N ATOM 1311 CA ALA B 218 10.453 2.825 -53.066 1.00 28.88 C ANISOU 1311 CA ALA B 218 4594 3075 3305 -506 83 -37 C ATOM 1312 C ALA B 218 10.082 2.428 -54.494 1.00 31.11 C ANISOU 1312 C ALA B 218 5015 3396 3410 -688 116 -113 C ATOM 1313 O ALA B 218 10.813 2.738 -55.435 1.00 35.00 O ANISOU 1313 O ALA B 218 5580 3908 3812 -754 178 -123 O ATOM 1314 CB ALA B 218 11.078 1.653 -52.308 1.00 28.30 C ANISOU 1314 CB ALA B 218 4483 2919 3349 -390 261 -62 C ATOM 1315 N ASP B 219 8.934 1.768 -54.642 1.00 28.86 N ANISOU 1315 N ASP B 219 4759 3162 3043 -813 73 -172 N ATOM 1316 CA ASP B 219 8.401 1.404 -55.952 1.00 31.94 C ANISOU 1316 CA ASP B 219 5261 3682 3193 -1078 82 -255 C ATOM 1317 C ASP B 219 8.147 2.655 -56.803 1.00 36.04 C ANISOU 1317 C ASP B 219 5726 4406 3563 -1101 -98 -109 C ATOM 1318 O ASP B 219 8.545 2.702 -57.968 1.00 34.87 O ANISOU 1318 O ASP B 219 5681 4323 3245 -1254 -45 -146 O ATOM 1319 CB ASP B 219 7.111 0.590 -55.804 1.00 31.85 C ANISOU 1319 CB ASP B 219 5242 3781 3078 -1269 43 -332 C ATOM 1320 CG ASP B 219 6.634 -0.004 -57.124 1.00 39.92 C ANISOU 1320 CG ASP B 219 6396 4981 3789 -1653 96 -467 C ATOM 1321 OD1 ASP B 219 7.478 -0.522 -57.892 1.00 42.22 O ANISOU 1321 OD1 ASP B 219 6899 5126 4018 -1769 321 -603 O ATOM 1322 OD2 ASP B 219 5.414 0.043 -57.394 1.00 39.30 O ANISOU 1322 OD2 ASP B 219 6200 5230 3504 -1859 -74 -433 O ATOM 1323 N ARG B 220 7.503 3.668 -56.217 1.00 37.12 N ANISOU 1323 N ARG B 220 5724 4621 3759 -930 -271 70 N ATOM 1324 CA ARG B 220 7.228 4.913 -56.945 1.00 36.88 C ANISOU 1324 CA ARG B 220 5671 4740 3603 -874 -386 270 C ATOM 1325 C ARG B 220 8.526 5.571 -57.386 1.00 34.79 C ANISOU 1325 C ARG B 220 5535 4319 3365 -850 -281 268 C ATOM 1326 O ARG B 220 8.643 6.036 -58.518 1.00 37.32 O ANISOU 1326 O ARG B 220 5921 4751 3506 -936 -295 340 O ATOM 1327 CB ARG B 220 6.420 5.909 -56.100 1.00 37.61 C ANISOU 1327 CB ARG B 220 5648 4846 3796 -625 -490 476 C ATOM 1328 CG ARG B 220 5.025 5.460 -55.698 1.00 37.37 C ANISOU 1328 CG ARG B 220 5435 5048 3716 -624 -610 533 C ATOM 1329 CD ARG B 220 4.280 4.809 -56.841 1.00 41.37 C ANISOU 1329 CD ARG B 220 5866 5935 3919 -899 -697 527 C ATOM 1330 NE ARG B 220 4.273 5.638 -58.040 1.00 47.48 N ANISOU 1330 NE ARG B 220 6640 6918 4482 -896 -755 723 N ATOM 1331 CZ ARG B 220 3.432 5.469 -59.052 1.00 50.90 C ANISOU 1331 CZ ARG B 220 6933 7817 4588 -1093 -878 833 C ATOM 1332 NH1 ARG B 220 3.495 6.266 -60.110 1.00 51.10 N ANISOU 1332 NH1 ARG B 220 6957 8040 4419 -1059 -924 1049 N ATOM 1333 NH2 ARG B 220 2.523 4.503 -59.000 1.00 51.05 N ANISOU 1333 NH2 ARG B 220 6809 8141 4445 -1357 -948 733 N ATOM 1334 N PHE B 221 9.493 5.610 -56.473 1.00 32.24 N ANISOU 1334 N PHE B 221 5225 3788 3238 -754 -179 198 N ATOM 1335 CA PHE B 221 10.801 6.178 -56.751 1.00 32.16 C ANISOU 1335 CA PHE B 221 5295 3687 3239 -774 -70 184 C ATOM 1336 C PHE B 221 11.469 5.480 -57.945 1.00 33.12 C ANISOU 1336 C PHE B 221 5502 3857 3226 -937 44 75 C ATOM 1337 O PHE B 221 11.989 6.137 -58.842 1.00 31.60 O ANISOU 1337 O PHE B 221 5396 3694 2916 -1013 72 116 O ATOM 1338 CB PHE B 221 11.687 6.081 -55.502 1.00 29.71 C ANISOU 1338 CB PHE B 221 4906 3276 3107 -696 12 129 C ATOM 1339 CG PHE B 221 12.951 6.893 -55.578 1.00 31.47 C ANISOU 1339 CG PHE B 221 5161 3485 3310 -760 105 135 C ATOM 1340 CD1 PHE B 221 12.987 8.182 -55.075 1.00 32.08 C ANISOU 1340 CD1 PHE B 221 5308 3487 3394 -773 97 204 C ATOM 1341 CD2 PHE B 221 14.104 6.370 -56.137 1.00 31.99 C ANISOU 1341 CD2 PHE B 221 5205 3615 3336 -826 238 68 C ATOM 1342 CE1 PHE B 221 14.143 8.936 -55.131 1.00 33.55 C ANISOU 1342 CE1 PHE B 221 5543 3683 3520 -919 203 183 C ATOM 1343 CE2 PHE B 221 15.262 7.124 -56.195 1.00 32.19 C ANISOU 1343 CE2 PHE B 221 5220 3699 3312 -925 319 78 C ATOM 1344 CZ PHE B 221 15.277 8.411 -55.691 1.00 34.03 C ANISOU 1344 CZ PHE B 221 5526 3878 3527 -1005 292 124 C ATOM 1345 N LEU B 222 11.440 4.149 -57.955 1.00 34.23 N ANISOU 1345 N LEU B 222 5655 3975 3376 -996 148 -68 N ATOM 1346 CA LEU B 222 12.116 3.384 -59.000 1.00 35.53 C ANISOU 1346 CA LEU B 222 5951 4124 3423 -1143 338 -199 C ATOM 1347 C LEU B 222 11.433 3.529 -60.362 1.00 36.71 C ANISOU 1347 C LEU B 222 6200 4453 3294 -1383 262 -205 C ATOM 1348 O LEU B 222 12.105 3.616 -61.387 1.00 34.29 O ANISOU 1348 O LEU B 222 6003 4173 2853 -1506 366 -248 O ATOM 1349 CB LEU B 222 12.206 1.905 -58.605 1.00 37.36 C ANISOU 1349 CB LEU B 222 6244 4213 3737 -1130 551 -345 C ATOM 1350 CG LEU B 222 13.093 1.583 -57.395 1.00 42.14 C ANISOU 1350 CG LEU B 222 6729 4703 4580 -868 675 -296 C ATOM 1351 CD1 LEU B 222 13.086 0.088 -57.076 1.00 42.85 C ANISOU 1351 CD1 LEU B 222 6929 4608 4743 -809 940 -392 C ATOM 1352 CD2 LEU B 222 14.517 2.084 -57.604 1.00 43.96 C ANISOU 1352 CD2 LEU B 222 6887 4984 4832 -786 781 -236 C ATOM 1353 N LEU B 223 10.103 3.563 -60.373 1.00 34.71 N ANISOU 1353 N LEU B 223 5880 4380 2927 -1459 81 -143 N ATOM 1354 CA LEU B 223 9.345 3.777 -61.609 1.00 35.89 C ANISOU 1354 CA LEU B 223 6045 4833 2757 -1693 -34 -85 C ATOM 1355 C LEU B 223 9.775 5.057 -62.326 1.00 37.55 C ANISOU 1355 C LEU B 223 6273 5113 2884 -1620 -101 106 C ATOM 1356 O LEU B 223 9.772 5.121 -63.558 1.00 39.10 O ANISOU 1356 O LEU B 223 6540 5505 2811 -1830 -103 116 O ATOM 1357 CB LEU B 223 7.845 3.834 -61.319 1.00 36.60 C ANISOU 1357 CB LEU B 223 5959 5204 2744 -1717 -249 41 C ATOM 1358 CG LEU B 223 7.140 2.510 -61.023 1.00 43.65 C ANISOU 1358 CG LEU B 223 6866 6146 3575 -1952 -190 -162 C ATOM 1359 CD1 LEU B 223 5.724 2.753 -60.512 1.00 44.13 C ANISOU 1359 CD1 LEU B 223 6680 6515 3573 -1915 -419 6 C ATOM 1360 CD2 LEU B 223 7.116 1.640 -62.272 1.00 46.83 C ANISOU 1360 CD2 LEU B 223 7443 6703 3646 -2398 -59 -369 C ATOM 1361 N VAL B 224 10.157 6.063 -61.543 1.00 37.25 N ANISOU 1361 N VAL B 224 6197 4903 3053 -1356 -128 246 N ATOM 1362 CA VAL B 224 10.518 7.377 -62.066 1.00 37.80 C ANISOU 1362 CA VAL B 224 6336 4964 3061 -1277 -145 439 C ATOM 1363 C VAL B 224 12.009 7.499 -62.388 1.00 39.92 C ANISOU 1363 C VAL B 224 6730 5068 3371 -1351 35 319 C ATOM 1364 O VAL B 224 12.383 8.053 -63.418 1.00 40.50 O ANISOU 1364 O VAL B 224 6908 5207 3273 -1449 65 387 O ATOM 1365 CB VAL B 224 10.136 8.497 -61.059 1.00 43.74 C ANISOU 1365 CB VAL B 224 7056 5576 3986 -1003 -196 637 C ATOM 1366 CG1 VAL B 224 10.713 9.842 -61.494 1.00 44.90 C ANISOU 1366 CG1 VAL B 224 7370 5597 4094 -943 -114 800 C ATOM 1367 CG2 VAL B 224 8.625 8.581 -60.895 1.00 40.26 C ANISOU 1367 CG2 VAL B 224 6463 5357 3478 -877 -360 833 C ATOM 1368 N PHE B 225 12.863 6.980 -61.511 1.00 41.86 N ANISOU 1368 N PHE B 225 6935 5147 3821 -1299 157 167 N ATOM 1369 CA PHE B 225 14.298 7.220 -61.642 1.00 45.28 C ANISOU 1369 CA PHE B 225 7409 5504 4292 -1340 321 102 C ATOM 1370 C PHE B 225 15.100 6.017 -62.127 1.00 51.28 C ANISOU 1370 C PHE B 225 8183 6270 5029 -1423 520 -78 C ATOM 1371 O PHE B 225 16.196 6.182 -62.654 1.00 55.79 O ANISOU 1371 O PHE B 225 8785 6858 5555 -1486 665 -111 O ATOM 1372 CB PHE B 225 14.867 7.705 -60.307 1.00 40.74 C ANISOU 1372 CB PHE B 225 6737 4826 3915 -1223 342 120 C ATOM 1373 CG PHE B 225 14.325 9.034 -59.878 1.00 38.41 C ANISOU 1373 CG PHE B 225 6518 4442 3635 -1164 256 273 C ATOM 1374 CD1 PHE B 225 14.784 10.206 -60.465 1.00 38.19 C ANISOU 1374 CD1 PHE B 225 6655 4356 3498 -1253 323 362 C ATOM 1375 CD2 PHE B 225 13.344 9.116 -58.904 1.00 35.06 C ANISOU 1375 CD2 PHE B 225 6036 3960 3326 -1014 155 334 C ATOM 1376 CE1 PHE B 225 14.281 11.432 -60.082 1.00 37.73 C ANISOU 1376 CE1 PHE B 225 6745 4137 3455 -1175 330 513 C ATOM 1377 CE2 PHE B 225 12.836 10.350 -58.513 1.00 36.46 C ANISOU 1377 CE2 PHE B 225 6329 4003 3521 -924 150 484 C ATOM 1378 CZ PHE B 225 13.306 11.506 -59.104 1.00 36.24 C ANISOU 1378 CZ PHE B 225 6507 3871 3392 -996 258 577 C ATOM 1379 N LYS B 226 14.566 4.813 -61.943 1.00 55.93 N ANISOU 1379 N LYS B 226 4642 8406 8204 41 -162 333 N ATOM 1380 CA LYS B 226 15.251 3.605 -62.402 1.00 55.75 C ANISOU 1380 CA LYS B 226 5096 8192 7894 321 72 468 C ATOM 1381 C LYS B 226 14.292 2.653 -63.117 1.00 55.42 C ANISOU 1381 C LYS B 226 5632 7964 7462 132 156 328 C ATOM 1382 O LYS B 226 14.129 1.510 -62.697 1.00 59.61 O ANISOU 1382 O LYS B 226 6584 8274 7790 115 239 271 O ATOM 1383 CB LYS B 226 15.918 2.884 -61.225 1.00 57.03 C ANISOU 1383 CB LYS B 226 5367 8329 7973 536 67 498 C ATOM 1384 CG LYS B 226 16.926 3.722 -60.439 1.00 58.98 C ANISOU 1384 CG LYS B 226 5033 8760 8617 773 -140 523 C ATOM 1385 CD LYS B 226 18.162 4.029 -61.264 1.00 62.37 C ANISOU 1385 CD LYS B 226 5174 9115 9407 1079 12 804 C ATOM 1386 CE LYS B 226 19.170 4.844 -60.470 1.00 66.76 C ANISOU 1386 CE LYS B 226 5055 9774 10538 1279 -265 774 C ATOM 1387 NZ LYS B 226 20.377 5.183 -61.279 1.00 71.50 N ANISOU 1387 NZ LYS B 226 5610 10154 11405 1453 -81 967 N ATOM 1388 N PRO B 227 13.663 3.118 -64.209 1.00 54.26 N ANISOU 1388 N PRO B 227 5470 7891 7255 27 129 262 N ATOM 1389 CA PRO B 227 12.610 2.327 -64.854 1.00 56.54 C ANISOU 1389 CA PRO B 227 6221 8015 7245 -189 61 -2 C ATOM 1390 C PRO B 227 13.131 1.029 -65.481 1.00 63.83 C ANISOU 1390 C PRO B 227 7734 8654 7864 108 219 -58 C ATOM 1391 O PRO B 227 12.352 0.097 -65.698 1.00 63.20 O ANISOU 1391 O PRO B 227 8054 8297 7663 -93 126 -355 O ATOM 1392 CB PRO B 227 12.070 3.278 -65.925 1.00 57.49 C ANISOU 1392 CB PRO B 227 6120 8397 7325 -199 -12 -25 C ATOM 1393 CG PRO B 227 13.221 4.161 -66.248 1.00 57.36 C ANISOU 1393 CG PRO B 227 5708 8561 7526 214 201 336 C ATOM 1394 CD PRO B 227 13.975 4.345 -64.966 1.00 55.21 C ANISOU 1394 CD PRO B 227 5126 8236 7613 188 186 449 C ATOM 1395 N ILE B 228 14.431 0.972 -65.759 1.00 64.90 N ANISOU 1395 N ILE B 228 7893 8813 7954 585 456 226 N ATOM 1396 CA ILE B 228 15.050 -0.243 -66.281 1.00 71.14 C ANISOU 1396 CA ILE B 228 9259 9329 8441 935 661 225 C ATOM 1397 C ILE B 228 15.065 -1.336 -65.215 1.00 70.83 C ANISOU 1397 C ILE B 228 9470 8981 8462 784 743 183 C ATOM 1398 O ILE B 228 14.871 -2.513 -65.520 1.00 72.53 O ANISOU 1398 O ILE B 228 10205 8835 8519 809 825 -12 O ATOM 1399 CB ILE B 228 16.487 0.015 -66.778 1.00 75.27 C ANISOU 1399 CB ILE B 228 9688 9955 8956 1531 963 661 C ATOM 1400 CG1 ILE B 228 16.480 1.070 -67.887 1.00 77.77 C ANISOU 1400 CG1 ILE B 228 9735 10558 9258 1804 1010 823 C ATOM 1401 CG2 ILE B 228 17.127 -1.275 -67.276 1.00 79.48 C ANISOU 1401 CG2 ILE B 228 10867 10197 9135 1932 1213 686 C ATOM 1402 CD1 ILE B 228 17.835 1.306 -68.519 1.00 80.90 C ANISOU 1402 CD1 ILE B 228 10015 11001 9723 2474 1397 1357 C ATOM 1403 N TRP B 229 15.293 -0.940 -63.964 1.00 68.73 N ANISOU 1403 N TRP B 229 8822 8855 8438 688 729 357 N ATOM 1404 CA TRP B 229 15.196 -1.866 -62.839 1.00 69.24 C ANISOU 1404 CA TRP B 229 9061 8716 8532 631 854 393 C ATOM 1405 C TRP B 229 13.798 -2.473 -62.790 1.00 69.51 C ANISOU 1405 C TRP B 229 9315 8442 8654 204 776 115 C ATOM 1406 O TRP B 229 13.639 -3.673 -62.573 1.00 73.94 O ANISOU 1406 O TRP B 229 10233 8599 9262 206 985 95 O ATOM 1407 CB TRP B 229 15.496 -1.170 -61.503 1.00 67.36 C ANISOU 1407 CB TRP B 229 8354 8790 8450 680 761 554 C ATOM 1408 CG TRP B 229 16.887 -0.621 -61.342 1.00 67.04 C ANISOU 1408 CG TRP B 229 7982 8991 8499 1074 768 788 C ATOM 1409 CD1 TRP B 229 17.809 -0.400 -62.324 1.00 69.97 C ANISOU 1409 CD1 TRP B 229 8313 9359 8915 1351 884 966 C ATOM 1410 CD2 TRP B 229 17.509 -0.221 -60.111 1.00 63.76 C ANISOU 1410 CD2 TRP B 229 7186 8845 8196 1287 634 872 C ATOM 1411 NE1 TRP B 229 18.965 0.114 -61.782 1.00 69.76 N ANISOU 1411 NE1 TRP B 229 7838 9518 9147 1651 841 1186 N ATOM 1412 CE2 TRP B 229 18.806 0.232 -60.426 1.00 64.90 C ANISOU 1412 CE2 TRP B 229 7012 9087 8560 1609 632 1068 C ATOM 1413 CE3 TRP B 229 17.093 -0.202 -58.775 1.00 60.71 C ANISOU 1413 CE3 TRP B 229 6691 8639 7737 1309 510 803 C ATOM 1414 CZ2 TRP B 229 19.691 0.699 -59.453 1.00 63.11 C ANISOU 1414 CZ2 TRP B 229 6323 9109 8546 1883 417 1105 C ATOM 1415 CZ3 TRP B 229 17.975 0.262 -57.810 1.00 60.53 C ANISOU 1415 CZ3 TRP B 229 6285 8935 7779 1667 299 820 C ATOM 1416 CH2 TRP B 229 19.258 0.705 -58.155 1.00 61.72 C ANISOU 1416 CH2 TRP B 229 6086 9155 8211 1915 210 925 C HETATM 1417 N YCM B 230 12.789 -1.629 -62.995 1.00 65.78 N ANISOU 1417 N YCM B 230 8576 8126 8292 -157 499 -67 N HETATM 1418 CA YCM B 230 11.409 -2.052 -62.936 1.00 63.31 C ANISOU 1418 CA YCM B 230 8342 7530 8182 -592 382 -295 C HETATM 1419 CB YCM B 230 10.414 -0.888 -62.896 1.00 58.95 C ANISOU 1419 CB YCM B 230 7377 7267 7753 -947 107 -371 C HETATM 1420 SG YCM B 230 10.728 0.358 -61.679 1.00 53.54 S ANISOU 1420 SG YCM B 230 6177 7038 7127 -866 84 -102 S HETATM 1421 CD YCM B 230 9.850 -0.183 -60.246 1.00 53.37 C ANISOU 1421 CD YCM B 230 6149 6840 7290 -990 226 63 C HETATM 1422 CE YCM B 230 10.633 -1.120 -59.351 1.00 59.72 C ANISOU 1422 CE YCM B 230 7160 7525 8007 -588 535 301 C HETATM 1423 OZ1 YCM B 230 11.770 -1.527 -59.676 1.00 63.42 O ANISOU 1423 OZ1 YCM B 230 7807 7982 8308 -279 642 333 O HETATM 1424 NZ2 YCM B 230 10.072 -1.515 -58.168 1.00 60.06 N ANISOU 1424 NZ2 YCM B 230 7181 7494 8146 -494 748 548 N HETATM 1425 C YCM B 230 11.008 -3.030 -64.035 1.00 69.58 C ANISOU 1425 C YCM B 230 9578 7902 8956 -665 314 -657 C HETATM 1426 O YCM B 230 10.169 -3.919 -63.878 1.00 76.22 O ANISOU 1426 O YCM B 230 10566 8275 10119 -942 313 -834 O ATOM 1427 N GLN B 231 11.631 -2.858 -65.195 1.00 68.56 N ANISOU 1427 N GLN B 231 9647 7920 8484 -355 252 -776 N ATOM 1428 CA GLN B 231 11.358 -3.738 -66.325 1.00 73.12 C ANISOU 1428 CA GLN B 231 10703 8162 8918 -280 117 -1211 C ATOM 1429 C GLN B 231 12.031 -5.097 -66.137 1.00 74.58 C ANISOU 1429 C GLN B 231 11343 7858 9135 -48 427 -1187 C ATOM 1430 O GLN B 231 11.539 -6.113 -66.625 1.00 81.02 O ANISOU 1430 O GLN B 231 12520 8171 10094 -142 323 -1608 O ATOM 1431 CB GLN B 231 11.810 -3.081 -67.630 1.00 75.32 C ANISOU 1431 CB GLN B 231 11077 8825 8716 144 5 -1285 C ATOM 1432 CG GLN B 231 10.916 -1.923 -68.059 1.00 77.17 C ANISOU 1432 CG GLN B 231 10926 9468 8927 -76 -305 -1396 C ATOM 1433 CD GLN B 231 11.552 -1.048 -69.123 1.00 81.30 C ANISOU 1433 CD GLN B 231 11398 10465 9029 471 -236 -1218 C ATOM 1434 OE1 GLN B 231 12.725 -0.687 -69.027 1.00 81.06 O ANISOU 1434 OE1 GLN B 231 11256 10587 8955 869 97 -765 O ATOM 1435 NE2 GLN B 231 10.778 -0.704 -70.146 1.00 84.85 N ANISOU 1435 NE2 GLN B 231 11886 11150 9205 544 -532 -1537 N ATOM 1436 N ASN B 232 13.146 -5.110 -65.412 1.00 72.03 N ANISOU 1436 N ASN B 232 10968 7664 8734 260 791 -716 N ATOM 1437 CA ASN B 232 13.875 -6.348 -65.143 1.00 75.95 C ANISOU 1437 CA ASN B 232 11860 7753 9243 532 1170 -583 C ATOM 1438 C ASN B 232 13.367 -7.086 -63.905 1.00 75.29 C ANISOU 1438 C ASN B 232 11680 7310 9616 279 1409 -423 C ATOM 1439 O ASN B 232 13.249 -8.313 -63.906 1.00 79.68 O ANISOU 1439 O ASN B 232 12567 7285 10424 281 1635 -528 O ATOM 1440 CB ASN B 232 15.373 -6.056 -64.985 1.00 75.76 C ANISOU 1440 CB ASN B 232 11800 8059 8926 1054 1464 -104 C ATOM 1441 CG ASN B 232 16.090 -5.906 -66.319 1.00 78.99 C ANISOU 1441 CG ASN B 232 12500 8587 8924 1513 1468 -144 C ATOM 1442 OD1 ASN B 232 16.686 -6.857 -66.825 1.00 83.20 O ANISOU 1442 OD1 ASN B 232 13539 8818 9255 1876 1706 -159 O ATOM 1443 ND2 ASN B 232 16.040 -4.705 -66.892 1.00 77.22 N ANISOU 1443 ND2 ASN B 232 11958 8800 8581 1568 1259 -111 N ATOM 1444 N PHE B 233 13.060 -6.326 -62.856 1.00 72.81 N ANISOU 1444 N PHE B 233 10905 7329 9429 124 1389 -151 N ATOM 1445 CA PHE B 233 12.729 -6.880 -61.543 1.00 74.63 C ANISOU 1445 CA PHE B 233 11008 7369 9981 93 1710 167 C ATOM 1446 C PHE B 233 11.240 -6.909 -61.222 1.00 83.09 C ANISOU 1446 C PHE B 233 11859 8154 11555 -389 1593 45 C ATOM 1447 O PHE B 233 10.663 -7.980 -61.019 1.00 94.57 O ANISOU 1447 O PHE B 233 13429 8990 13514 -521 1840 50 O ATOM 1448 CB PHE B 233 13.444 -6.082 -60.454 1.00 67.95 C ANISOU 1448 CB PHE B 233 9822 7112 8885 405 1782 570 C ATOM 1449 CG PHE B 233 14.758 -6.655 -60.057 1.00 67.64 C ANISOU 1449 CG PHE B 233 9948 7146 8606 932 2134 901 C ATOM 1450 CD1 PHE B 233 14.870 -8.002 -59.757 1.00 69.30 C ANISOU 1450 CD1 PHE B 233 10475 6882 8972 1111 2608 1092 C ATOM 1451 CD2 PHE B 233 15.887 -5.858 -59.996 1.00 66.64 C ANISOU 1451 CD2 PHE B 233 9611 7524 8185 1255 2010 1045 C ATOM 1452 CE1 PHE B 233 16.079 -8.543 -59.391 1.00 73.58 C ANISOU 1452 CE1 PHE B 233 11165 7522 9271 1626 2965 1441 C ATOM 1453 CE2 PHE B 233 17.105 -6.396 -59.631 1.00 71.39 C ANISOU 1453 CE2 PHE B 233 10321 8203 8600 1749 2312 1371 C ATOM 1454 CZ PHE B 233 17.198 -7.742 -59.329 1.00 74.12 C ANISOU 1454 CZ PHE B 233 11028 8142 8993 1945 2797 1578 C ATOM 1455 N ARG B 234 10.648 -5.717 -61.155 1.00 79.17 N ANISOU 1455 N ARG B 234 11004 8079 10999 -630 1255 -14 N ATOM 1456 CA ARG B 234 9.271 -5.500 -60.707 1.00 77.94 C ANISOU 1456 CA ARG B 234 10552 7778 11283 -1042 1158 -6 C ATOM 1457 C ARG B 234 8.283 -6.546 -61.215 1.00 83.27 C ANISOU 1457 C ARG B 234 11348 7703 12587 -1413 1141 -289 C ATOM 1458 O ARG B 234 7.974 -6.612 -62.406 1.00 85.38 O ANISOU 1458 O ARG B 234 11764 7809 12867 -1637 753 -812 O ATOM 1459 CB ARG B 234 8.810 -4.105 -61.133 1.00 71.71 C ANISOU 1459 CB ARG B 234 9458 7486 10301 -1288 719 -188 C ATOM 1460 CG ARG B 234 7.458 -3.669 -60.598 1.00 69.79 C ANISOU 1460 CG ARG B 234 8868 7209 10439 -1667 630 -96 C ATOM 1461 CD ARG B 234 7.123 -2.283 -61.126 1.00 62.91 C ANISOU 1461 CD ARG B 234 7722 6845 9338 -1868 237 -269 C ATOM 1462 NE ARG B 234 6.115 -1.597 -60.328 1.00 56.38 N ANISOU 1462 NE ARG B 234 6535 6161 8727 -2084 226 -43 N ATOM 1463 CZ ARG B 234 4.877 -1.362 -60.739 1.00 61.50 C ANISOU 1463 CZ ARG B 234 6985 6680 9702 -2526 6 -174 C ATOM 1464 NH1 ARG B 234 4.490 -1.760 -61.943 1.00 65.10 N ANISOU 1464 NH1 ARG B 234 7561 6887 10288 -2786 -292 -609 N ATOM 1465 NH2 ARG B 234 4.026 -0.728 -59.945 1.00 64.98 N ANISOU 1465 NH2 ARG B 234 7113 7261 10317 -2657 64 117 N ATOM 1466 N GLY B 235 7.809 -7.372 -60.290 1.00 86.71 N ANISOU 1466 N GLY B 235 11693 7674 13579 -1411 1568 66 N ATOM 1467 CA GLY B 235 6.816 -8.387 -60.581 1.00 93.62 C ANISOU 1467 CA GLY B 235 12542 7711 15318 -1783 1603 -133 C ATOM 1468 C GLY B 235 5.938 -8.565 -59.360 1.00 94.55 C ANISOU 1468 C GLY B 235 12279 7583 16061 -1819 2031 453 C ATOM 1469 O GLY B 235 6.232 -8.014 -58.300 1.00 90.23 O ANISOU 1469 O GLY B 235 11605 7553 15126 -1445 2313 976 O ATOM 1470 N ALA B 236 4.859 -9.325 -59.500 1.00 48.69 N ANISOU 1470 N ALA B 236 8800 5221 4477 1104 -995 -379 N ATOM 1471 CA ALA B 236 3.939 -9.530 -58.389 1.00 43.12 C ANISOU 1471 CA ALA B 236 7782 4560 4040 932 -1146 -472 C ATOM 1472 C ALA B 236 4.621 -10.293 -57.258 1.00 39.94 C ANISOU 1472 C ALA B 236 7209 4125 3841 799 -948 -419 C ATOM 1473 O ALA B 236 4.345 -10.046 -56.083 1.00 38.69 O ANISOU 1473 O ALA B 236 6783 4010 3906 664 -943 -390 O ATOM 1474 CB ALA B 236 2.694 -10.265 -58.855 1.00 42.52 C ANISOU 1474 CB ALA B 236 7721 4510 3925 884 -1439 -718 C ATOM 1475 N GLY B 237 5.520 -11.205 -57.625 1.00 43.05 N ANISOU 1475 N GLY B 237 7788 4448 4121 888 -788 -410 N ATOM 1476 CA GLY B 237 6.210 -12.051 -56.665 1.00 40.58 C ANISOU 1476 CA GLY B 237 7396 4098 3924 869 -620 -373 C ATOM 1477 C GLY B 237 7.066 -11.295 -55.666 1.00 38.78 C ANISOU 1477 C GLY B 237 6886 4016 3831 851 -437 -208 C ATOM 1478 O GLY B 237 7.014 -11.571 -54.468 1.00 36.30 O ANISOU 1478 O GLY B 237 6397 3698 3699 762 -415 -193 O ATOM 1479 N LEU B 238 7.858 -10.344 -56.157 1.00 37.56 N ANISOU 1479 N LEU B 238 6716 3991 3564 907 -297 -94 N ATOM 1480 CA LEU B 238 8.683 -9.513 -55.283 1.00 36.41 C ANISOU 1480 CA LEU B 238 6301 4010 3521 818 -127 34 C ATOM 1481 C LEU B 238 7.834 -8.597 -54.410 1.00 34.77 C ANISOU 1481 C LEU B 238 5933 3771 3509 642 -258 56 C ATOM 1482 O LEU B 238 8.173 -8.336 -53.257 1.00 35.48 O ANISOU 1482 O LEU B 238 5785 3942 3754 546 -190 110 O ATOM 1483 CB LEU B 238 9.674 -8.680 -56.100 1.00 36.80 C ANISOU 1483 CB LEU B 238 6413 4198 3373 825 83 128 C ATOM 1484 CG LEU B 238 10.874 -9.461 -56.641 1.00 44.93 C ANISOU 1484 CG LEU B 238 7458 5393 4221 1012 299 120 C ATOM 1485 CD1 LEU B 238 11.809 -8.564 -57.441 1.00 51.37 C ANISOU 1485 CD1 LEU B 238 8303 6385 4830 941 550 203 C ATOM 1486 CD2 LEU B 238 11.617 -10.122 -55.494 1.00 44.40 C ANISOU 1486 CD2 LEU B 238 7099 5501 4272 1089 385 115 C ATOM 1487 N ALA B 239 6.731 -8.107 -54.963 1.00 34.24 N ANISOU 1487 N ALA B 239 5998 3608 3405 641 -456 3 N ATOM 1488 CA ALA B 239 5.840 -7.219 -54.225 1.00 31.72 C ANISOU 1488 CA ALA B 239 5546 3280 3227 555 -592 6 C ATOM 1489 C ALA B 239 5.226 -7.943 -53.021 1.00 30.17 C ANISOU 1489 C ALA B 239 5106 3093 3265 451 -665 -69 C ATOM 1490 O ALA B 239 5.133 -7.376 -51.933 1.00 31.01 O ANISOU 1490 O ALA B 239 5024 3238 3522 362 -644 -19 O ATOM 1491 CB ALA B 239 4.751 -6.669 -55.146 1.00 29.87 C ANISOU 1491 CB ALA B 239 5497 3000 2852 675 -819 -68 C ATOM 1492 N TRP B 240 4.834 -9.204 -53.217 1.00 30.58 N ANISOU 1492 N TRP B 240 5214 3086 3319 441 -730 -189 N ATOM 1493 CA TRP B 240 4.261 -10.010 -52.138 1.00 29.46 C ANISOU 1493 CA TRP B 240 4929 2908 3354 293 -755 -261 C ATOM 1494 C TRP B 240 5.292 -10.379 -51.075 1.00 29.68 C ANISOU 1494 C TRP B 240 4886 2932 3459 304 -560 -152 C ATOM 1495 O TRP B 240 4.965 -10.483 -49.897 1.00 32.85 O ANISOU 1495 O TRP B 240 5140 3329 4013 193 -546 -146 O ATOM 1496 CB TRP B 240 3.623 -11.279 -52.693 1.00 32.71 C ANISOU 1496 CB TRP B 240 5518 3208 3701 222 -849 -429 C ATOM 1497 CG TRP B 240 2.231 -11.069 -53.216 1.00 33.69 C ANISOU 1497 CG TRP B 240 5560 3423 3816 127 -1092 -604 C ATOM 1498 CD1 TRP B 240 1.813 -11.190 -54.512 1.00 35.21 C ANISOU 1498 CD1 TRP B 240 5919 3632 3826 202 -1257 -729 C ATOM 1499 CD2 TRP B 240 1.077 -10.692 -52.456 1.00 31.50 C ANISOU 1499 CD2 TRP B 240 4981 3294 3694 -27 -1209 -696 C ATOM 1500 NE1 TRP B 240 0.465 -10.933 -54.599 1.00 36.83 N ANISOU 1500 NE1 TRP B 240 5914 4018 4061 109 -1493 -908 N ATOM 1501 CE2 TRP B 240 -0.007 -10.617 -53.352 1.00 39.72 C ANISOU 1501 CE2 TRP B 240 5972 4484 4635 -28 -1457 -892 C ATOM 1502 CE3 TRP B 240 0.854 -10.416 -51.107 1.00 34.00 C ANISOU 1502 CE3 TRP B 240 5054 3664 4201 -142 -1130 -644 C ATOM 1503 CZ2 TRP B 240 -1.289 -10.269 -52.941 1.00 41.22 C ANISOU 1503 CZ2 TRP B 240 5824 4926 4913 -127 -1621 -1048 C ATOM 1504 CZ3 TRP B 240 -0.421 -10.074 -50.701 1.00 36.22 C ANISOU 1504 CZ3 TRP B 240 5040 4151 4571 -253 -1268 -783 C ATOM 1505 CH2 TRP B 240 -1.473 -10.003 -51.614 1.00 37.86 C ANISOU 1505 CH2 TRP B 240 5152 4554 4680 -239 -1509 -988 C ATOM 1506 N ILE B 241 6.535 -10.586 -51.495 1.00 28.57 N ANISOU 1506 N ILE B 241 4839 2830 3187 462 -410 -79 N ATOM 1507 CA ILE B 241 7.607 -10.838 -50.543 1.00 28.50 C ANISOU 1507 CA ILE B 241 4711 2911 3208 541 -251 6 C ATOM 1508 C ILE B 241 7.899 -9.578 -49.712 1.00 24.76 C ANISOU 1508 C ILE B 241 3970 2592 2848 432 -212 97 C ATOM 1509 O ILE B 241 8.034 -9.657 -48.498 1.00 29.37 O ANISOU 1509 O ILE B 241 4407 3212 3541 401 -186 125 O ATOM 1510 CB ILE B 241 8.895 -11.312 -51.247 1.00 31.35 C ANISOU 1510 CB ILE B 241 5164 3378 3370 775 -99 32 C ATOM 1511 CG1 ILE B 241 8.651 -12.660 -51.942 1.00 35.10 C ANISOU 1511 CG1 ILE B 241 5984 3648 3706 915 -131 -65 C ATOM 1512 CG2 ILE B 241 10.036 -11.440 -50.238 1.00 30.11 C ANISOU 1512 CG2 ILE B 241 4797 3425 3218 903 35 94 C ATOM 1513 CD1 ILE B 241 9.785 -13.110 -52.836 1.00 34.49 C ANISOU 1513 CD1 ILE B 241 6037 3677 3392 1201 11 -59 C ATOM 1514 N ALA B 242 7.988 -8.423 -50.370 1.00 24.88 N ANISOU 1514 N ALA B 242 3984 2663 2804 372 -206 139 N ATOM 1515 CA ALA B 242 8.216 -7.172 -49.658 1.00 25.53 C ANISOU 1515 CA ALA B 242 3913 2829 2958 230 -166 211 C ATOM 1516 C ALA B 242 7.091 -6.932 -48.641 1.00 26.15 C ANISOU 1516 C ALA B 242 3901 2821 3213 150 -301 182 C ATOM 1517 O ALA B 242 7.348 -6.526 -47.507 1.00 28.60 O ANISOU 1517 O ALA B 242 4053 3193 3620 73 -261 221 O ATOM 1518 CB ALA B 242 8.332 -6.014 -50.632 1.00 25.05 C ANISOU 1518 CB ALA B 242 4016 2746 2755 172 -130 259 C ATOM 1519 N CYS B 243 5.854 -7.217 -49.040 1.00 28.06 N ANISOU 1519 N CYS B 243 4220 2962 3480 167 -459 95 N ATOM 1520 CA CYS B 243 4.713 -7.092 -48.133 1.00 27.69 C ANISOU 1520 CA CYS B 243 4036 2902 3582 94 -567 38 C ATOM 1521 C CYS B 243 4.801 -8.049 -46.933 1.00 30.28 C ANISOU 1521 C CYS B 243 4261 3215 4027 26 -494 33 C ATOM 1522 O CYS B 243 4.444 -7.684 -45.808 1.00 25.92 O ANISOU 1522 O CYS B 243 3570 2690 3588 -42 -489 47 O ATOM 1523 CB CYS B 243 3.404 -7.329 -48.890 1.00 27.62 C ANISOU 1523 CB CYS B 243 4061 2885 3548 111 -751 -99 C ATOM 1524 SG CYS B 243 2.947 -5.989 -50.029 1.00 35.18 S ANISOU 1524 SG CYS B 243 5171 3859 4338 279 -895 -99 S ATOM 1525 N ALA B 244 5.266 -9.270 -47.182 1.00 26.10 N ANISOU 1525 N ALA B 244 3863 2618 3436 76 -431 14 N ATOM 1526 CA ALA B 244 5.435 -10.261 -46.123 1.00 25.15 C ANISOU 1526 CA ALA B 244 3775 2426 3357 65 -348 23 C ATOM 1527 C ALA B 244 6.439 -9.784 -45.077 1.00 27.30 C ANISOU 1527 C ALA B 244 3901 2822 3650 139 -257 126 C ATOM 1528 O ALA B 244 6.183 -9.853 -43.874 1.00 30.37 O ANISOU 1528 O ALA B 244 4228 3193 4119 87 -236 144 O ATOM 1529 CB ALA B 244 5.879 -11.601 -46.711 1.00 22.90 C ANISOU 1529 CB ALA B 244 3765 2005 2933 181 -294 -11 C ATOM 1530 N VAL B 245 7.582 -9.306 -45.552 1.00 28.00 N ANISOU 1530 N VAL B 245 3928 3064 3647 241 -198 178 N ATOM 1531 CA VAL B 245 8.618 -8.752 -44.692 1.00 27.28 C ANISOU 1531 CA VAL B 245 3641 3172 3551 267 -128 237 C ATOM 1532 C VAL B 245 8.095 -7.538 -43.917 1.00 29.28 C ANISOU 1532 C VAL B 245 3769 3433 3922 87 -176 256 C ATOM 1533 O VAL B 245 8.322 -7.417 -42.720 1.00 30.58 O ANISOU 1533 O VAL B 245 3825 3662 4131 77 -164 275 O ATOM 1534 CB VAL B 245 9.863 -8.352 -45.516 1.00 27.98 C ANISOU 1534 CB VAL B 245 3642 3484 3505 321 -33 255 C ATOM 1535 CG1 VAL B 245 10.871 -7.609 -44.658 1.00 27.10 C ANISOU 1535 CG1 VAL B 245 3266 3644 3387 252 26 275 C ATOM 1536 CG2 VAL B 245 10.494 -9.587 -46.165 1.00 33.17 C ANISOU 1536 CG2 VAL B 245 4417 4172 4012 581 27 230 C ATOM 1537 N ALA B 246 7.385 -6.650 -44.606 1.00 28.19 N ANISOU 1537 N ALA B 246 3689 3221 3802 -11 -238 246 N ATOM 1538 CA ALA B 246 6.806 -5.473 -43.967 1.00 28.36 C ANISOU 1538 CA ALA B 246 3671 3212 3893 -116 -289 256 C ATOM 1539 C ALA B 246 5.874 -5.871 -42.816 1.00 30.83 C ANISOU 1539 C ALA B 246 3912 3475 4328 -124 -331 224 C ATOM 1540 O ALA B 246 5.972 -5.334 -41.708 1.00 29.78 O ANISOU 1540 O ALA B 246 3700 3376 4238 -166 -315 246 O ATOM 1541 CB ALA B 246 6.068 -4.631 -44.987 1.00 22.71 C ANISOU 1541 CB ALA B 246 3105 2401 3121 -111 -370 241 C ATOM 1542 N TRP B 247 4.992 -6.831 -43.076 1.00 30.85 N ANISOU 1542 N TRP B 247 3954 3402 4367 -115 -369 160 N ATOM 1543 CA TRP B 247 4.110 -7.353 -42.037 1.00 27.58 C ANISOU 1543 CA TRP B 247 3483 2952 4044 -185 -358 121 C ATOM 1544 C TRP B 247 4.889 -7.989 -40.895 1.00 29.45 C ANISOU 1544 C TRP B 247 3747 3177 4266 -147 -256 183 C ATOM 1545 O TRP B 247 4.557 -7.786 -39.732 1.00 26.70 O ANISOU 1545 O TRP B 247 3341 2836 3967 -186 -226 195 O ATOM 1546 CB TRP B 247 3.137 -8.370 -42.613 1.00 30.29 C ANISOU 1546 CB TRP B 247 3884 3226 4398 -269 -388 17 C ATOM 1547 CG TRP B 247 1.936 -7.779 -43.240 1.00 29.07 C ANISOU 1547 CG TRP B 247 3612 3162 4271 -302 -519 -90 C ATOM 1548 CD1 TRP B 247 1.690 -7.641 -44.573 1.00 26.99 C ANISOU 1548 CD1 TRP B 247 3402 2921 3933 -242 -637 -152 C ATOM 1549 CD2 TRP B 247 0.797 -7.249 -42.563 1.00 28.36 C ANISOU 1549 CD2 TRP B 247 3324 3195 4258 -349 -557 -164 C ATOM 1550 NE1 TRP B 247 0.463 -7.061 -44.771 1.00 29.99 N ANISOU 1550 NE1 TRP B 247 3620 3446 4328 -222 -771 -267 N ATOM 1551 CE2 TRP B 247 -0.106 -6.803 -43.552 1.00 32.75 C ANISOU 1551 CE2 TRP B 247 3792 3878 4774 -280 -720 -281 C ATOM 1552 CE3 TRP B 247 0.451 -7.102 -41.217 1.00 31.18 C ANISOU 1552 CE3 TRP B 247 3569 3592 4688 -409 -470 -150 C ATOM 1553 CZ2 TRP B 247 -1.333 -6.228 -43.239 1.00 34.74 C ANISOU 1553 CZ2 TRP B 247 3806 4339 5055 -240 -803 -397 C ATOM 1554 CZ3 TRP B 247 -0.767 -6.527 -40.907 1.00 35.64 C ANISOU 1554 CZ3 TRP B 247 3911 4339 5291 -402 -525 -256 C ATOM 1555 CH2 TRP B 247 -1.645 -6.098 -41.916 1.00 35.42 C ANISOU 1555 CH2 TRP B 247 3758 4479 5222 -304 -694 -385 C ATOM 1556 N GLY B 248 5.922 -8.757 -41.231 1.00 26.92 N ANISOU 1556 N GLY B 248 3528 2857 3845 -22 -207 216 N ATOM 1557 CA GLY B 248 6.705 -9.455 -40.230 1.00 22.95 C ANISOU 1557 CA GLY B 248 3086 2366 3270 114 -137 264 C ATOM 1558 C GLY B 248 7.439 -8.489 -39.325 1.00 25.02 C ANISOU 1558 C GLY B 248 3159 2814 3533 134 -149 302 C ATOM 1559 O GLY B 248 7.444 -8.633 -38.102 1.00 27.25 O ANISOU 1559 O GLY B 248 3455 3095 3806 172 -129 325 O ATOM 1560 N LEU B 249 8.052 -7.491 -39.944 1.00 27.51 N ANISOU 1560 N LEU B 249 3334 3280 3838 80 -172 301 N ATOM 1561 CA LEU B 249 8.810 -6.472 -39.233 1.00 26.23 C ANISOU 1561 CA LEU B 249 3006 3302 3658 13 -180 306 C ATOM 1562 C LEU B 249 7.911 -5.654 -38.320 1.00 24.35 C ANISOU 1562 C LEU B 249 2780 2963 3510 -107 -217 303 C ATOM 1563 O LEU B 249 8.273 -5.355 -37.187 1.00 27.20 O ANISOU 1563 O LEU B 249 3079 3409 3848 -107 -225 302 O ATOM 1564 CB LEU B 249 9.526 -5.568 -40.231 1.00 28.91 C ANISOU 1564 CB LEU B 249 3270 3770 3946 -112 -155 296 C ATOM 1565 CG LEU B 249 10.732 -4.825 -39.665 1.00 44.51 C ANISOU 1565 CG LEU B 249 5044 6020 5846 -222 -131 268 C ATOM 1566 CD1 LEU B 249 11.754 -5.835 -39.158 1.00 48.59 C ANISOU 1566 CD1 LEU B 249 5393 6808 6261 18 -125 242 C ATOM 1567 CD2 LEU B 249 11.341 -3.900 -40.717 1.00 46.72 C ANISOU 1567 CD2 LEU B 249 5307 6389 6057 -442 -54 256 C ATOM 1568 N ALA B 250 6.731 -5.310 -38.823 1.00 23.82 N ANISOU 1568 N ALA B 250 2787 2744 3520 -173 -247 287 N ATOM 1569 CA ALA B 250 5.732 -4.599 -38.044 1.00 23.45 C ANISOU 1569 CA ALA B 250 2744 2629 3539 -219 -275 268 C ATOM 1570 C ALA B 250 5.367 -5.390 -36.796 1.00 25.22 C ANISOU 1570 C ALA B 250 2966 2832 3785 -181 -224 273 C ATOM 1571 O ALA B 250 5.293 -4.837 -35.703 1.00 23.33 O ANISOU 1571 O ALA B 250 2711 2612 3539 -187 -219 276 O ATOM 1572 CB ALA B 250 4.503 -4.334 -38.882 1.00 22.00 C ANISOU 1572 CB ALA B 250 2590 2368 3400 -216 -332 221 C ATOM 1573 N LEU B 251 5.168 -6.694 -36.961 1.00 24.23 N ANISOU 1573 N LEU B 251 2916 2637 3653 -148 -172 276 N ATOM 1574 CA LEU B 251 4.810 -7.537 -35.836 1.00 26.48 C ANISOU 1574 CA LEU B 251 3300 2845 3916 -137 -85 293 C ATOM 1575 C LEU B 251 5.920 -7.512 -34.789 1.00 29.63 C ANISOU 1575 C LEU B 251 3720 3331 4208 5 -86 344 C ATOM 1576 O LEU B 251 5.653 -7.321 -33.606 1.00 31.67 O ANISOU 1576 O LEU B 251 4007 3580 4445 9 -54 356 O ATOM 1577 CB LEU B 251 4.531 -8.967 -36.290 1.00 26.93 C ANISOU 1577 CB LEU B 251 3547 2749 3935 -153 -13 285 C ATOM 1578 CG LEU B 251 4.203 -9.935 -35.156 1.00 31.18 C ANISOU 1578 CG LEU B 251 4309 3138 4399 -170 120 317 C ATOM 1579 CD1 LEU B 251 2.927 -9.504 -34.452 1.00 30.33 C ANISOU 1579 CD1 LEU B 251 4091 3051 4381 -368 189 271 C ATOM 1580 CD2 LEU B 251 4.093 -11.380 -35.663 1.00 33.86 C ANISOU 1580 CD2 LEU B 251 4962 3254 4648 -199 206 310 C ATOM 1581 N LEU B 252 7.163 -7.668 -35.234 1.00 26.60 N ANISOU 1581 N LEU B 252 3295 3076 3737 135 -129 356 N ATOM 1582 CA LEU B 252 8.305 -7.659 -34.322 1.00 28.32 C ANISOU 1582 CA LEU B 252 3459 3478 3823 301 -165 366 C ATOM 1583 C LEU B 252 8.442 -6.329 -33.581 1.00 29.42 C ANISOU 1583 C LEU B 252 3451 3740 3987 173 -225 333 C ATOM 1584 O LEU B 252 8.849 -6.305 -32.421 1.00 26.39 O ANISOU 1584 O LEU B 252 3072 3447 3506 268 -256 329 O ATOM 1585 CB LEU B 252 9.604 -7.961 -35.071 1.00 27.35 C ANISOU 1585 CB LEU B 252 3219 3578 3595 458 -199 347 C ATOM 1586 CG LEU B 252 9.729 -9.341 -35.716 1.00 24.82 C ANISOU 1586 CG LEU B 252 3106 3142 3182 676 -147 372 C ATOM 1587 CD1 LEU B 252 11.064 -9.467 -36.456 1.00 21.63 C ANISOU 1587 CD1 LEU B 252 2521 3040 2656 868 -173 334 C ATOM 1588 CD2 LEU B 252 9.569 -10.449 -34.665 1.00 22.52 C ANISOU 1588 CD2 LEU B 252 3126 2678 2753 898 -103 420 C ATOM 1589 N LEU B 253 8.101 -5.229 -34.250 1.00 29.50 N ANISOU 1589 N LEU B 253 3389 3728 4091 -25 -246 305 N ATOM 1590 CA LEU B 253 8.186 -3.906 -33.627 1.00 26.25 C ANISOU 1590 CA LEU B 253 2941 3360 3674 -165 -292 266 C ATOM 1591 C LEU B 253 7.093 -3.683 -32.594 1.00 23.75 C ANISOU 1591 C LEU B 253 2734 2898 3390 -148 -269 271 C ATOM 1592 O LEU B 253 7.193 -2.788 -31.762 1.00 26.70 O ANISOU 1592 O LEU B 253 3134 3293 3718 -201 -304 237 O ATOM 1593 CB LEU B 253 8.124 -2.804 -34.688 1.00 21.78 C ANISOU 1593 CB LEU B 253 2391 2742 3143 -348 -302 245 C ATOM 1594 CG LEU B 253 9.404 -2.654 -35.512 1.00 23.44 C ANISOU 1594 CG LEU B 253 2475 3152 3280 -450 -293 222 C ATOM 1595 CD1 LEU B 253 9.222 -1.709 -36.697 1.00 22.95 C ANISOU 1595 CD1 LEU B 253 2535 2965 3220 -626 -264 226 C ATOM 1596 CD2 LEU B 253 10.544 -2.198 -34.610 1.00 26.14 C ANISOU 1596 CD2 LEU B 253 2665 3752 3517 -550 -331 151 C ATOM 1597 N THR B 254 6.056 -4.512 -32.649 1.00 30.24 N ANISOU 1597 N THR B 254 3624 3589 4275 -97 -195 299 N ATOM 1598 CA THR B 254 4.876 -4.352 -31.804 1.00 31.74 C ANISOU 1598 CA THR B 254 3869 3693 4498 -104 -130 289 C ATOM 1599 C THR B 254 4.964 -5.199 -30.519 1.00 30.64 C ANISOU 1599 C THR B 254 3849 3533 4260 -12 -52 329 C ATOM 1600 O THR B 254 4.414 -4.830 -29.482 1.00 30.69 O ANISOU 1600 O THR B 254 3908 3521 4234 -3 -2 320 O ATOM 1601 CB THR B 254 3.593 -4.707 -32.606 1.00 26.00 C ANISOU 1601 CB THR B 254 3100 2900 3879 -166 -78 260 C ATOM 1602 OG1 THR B 254 3.541 -3.908 -33.799 1.00 27.56 O ANISOU 1602 OG1 THR B 254 3243 3108 4120 -187 -170 228 O ATOM 1603 CG2 THR B 254 2.332 -4.462 -31.784 1.00 24.51 C ANISOU 1603 CG2 THR B 254 2881 2718 3714 -179 6 219 C ATOM 1604 N ILE B 255 5.678 -6.318 -30.592 1.00 30.18 N ANISOU 1604 N ILE B 255 3880 3469 4118 96 -37 374 N ATOM 1605 CA ILE B 255 5.799 -7.245 -29.463 1.00 30.43 C ANISOU 1605 CA ILE B 255 4134 3431 3998 238 42 429 C ATOM 1606 C ILE B 255 6.275 -6.605 -28.138 1.00 27.45 C ANISOU 1606 C ILE B 255 3774 3160 3494 341 -19 419 C ATOM 1607 O ILE B 255 5.653 -6.842 -27.105 1.00 28.20 O ANISOU 1607 O ILE B 255 4046 3154 3515 363 89 449 O ATOM 1608 CB ILE B 255 6.746 -8.425 -29.808 1.00 33.99 C ANISOU 1608 CB ILE B 255 4728 3872 4315 449 25 471 C ATOM 1609 CG1 ILE B 255 6.263 -9.158 -31.061 1.00 41.93 C ANISOU 1609 CG1 ILE B 255 5790 4732 5410 346 91 472 C ATOM 1610 CG2 ILE B 255 6.876 -9.385 -28.617 1.00 28.09 C ANISOU 1610 CG2 ILE B 255 4321 3003 3348 659 104 540 C ATOM 1611 CD1 ILE B 255 4.920 -9.820 -30.898 1.00 50.47 C ANISOU 1611 CD1 ILE B 255 7061 5580 6535 142 266 479 C ATOM 1612 N PRO B 256 7.360 -5.795 -28.158 1.00 26.62 N ANISOU 1612 N PRO B 256 3495 3272 3349 371 -180 361 N ATOM 1613 CA PRO B 256 7.821 -5.218 -26.883 1.00 27.01 C ANISOU 1613 CA PRO B 256 3571 3438 3254 446 -260 322 C ATOM 1614 C PRO B 256 6.736 -4.487 -26.083 1.00 26.85 C ANISOU 1614 C PRO B 256 3653 3283 3266 349 -180 313 C ATOM 1615 O PRO B 256 6.640 -4.694 -24.869 1.00 28.89 O ANISOU 1615 O PRO B 256 4085 3518 3375 473 -145 331 O ATOM 1616 CB PRO B 256 8.915 -4.242 -27.320 1.00 28.28 C ANISOU 1616 CB PRO B 256 3483 3849 3413 332 -418 223 C ATOM 1617 CG PRO B 256 9.460 -4.838 -28.545 1.00 28.51 C ANISOU 1617 CG PRO B 256 3380 3963 3491 357 -420 238 C ATOM 1618 CD PRO B 256 8.276 -5.436 -29.261 1.00 25.87 C ANISOU 1618 CD PRO B 256 3181 3351 3298 315 -281 315 C ATOM 1619 N SER B 257 5.921 -3.674 -26.746 1.00 25.68 N ANISOU 1619 N SER B 257 3424 3057 3276 181 -147 282 N ATOM 1620 CA SER B 257 4.877 -2.937 -26.040 1.00 26.03 C ANISOU 1620 CA SER B 257 3547 3018 3326 158 -72 255 C ATOM 1621 C SER B 257 3.750 -3.889 -25.665 1.00 30.95 C ANISOU 1621 C SER B 257 4251 3545 3962 177 132 309 C ATOM 1622 O SER B 257 3.147 -3.761 -24.599 1.00 35.88 O ANISOU 1622 O SER B 257 4988 4146 4500 223 238 308 O ATOM 1623 CB SER B 257 4.344 -1.781 -26.886 1.00 24.68 C ANISOU 1623 CB SER B 257 3303 2806 3270 58 -112 198 C ATOM 1624 OG SER B 257 3.634 -2.269 -28.013 1.00 29.13 O ANISOU 1624 OG SER B 257 3755 3338 3974 16 -54 216 O ATOM 1625 N PHE B 258 3.472 -4.837 -26.559 1.00 25.19 N ANISOU 1625 N PHE B 258 3481 2766 3324 108 201 344 N ATOM 1626 CA PHE B 258 2.501 -5.897 -26.308 1.00 26.29 C ANISOU 1626 CA PHE B 258 3724 2806 3458 28 417 380 C ATOM 1627 C PHE B 258 2.786 -6.614 -24.980 1.00 28.58 C ANISOU 1627 C PHE B 258 4317 3008 3535 141 524 454 C ATOM 1628 O PHE B 258 1.871 -6.891 -24.200 1.00 29.13 O ANISOU 1628 O PHE B 258 4501 3022 3546 64 733 466 O ATOM 1629 CB PHE B 258 2.517 -6.886 -27.484 1.00 32.16 C ANISOU 1629 CB PHE B 258 4461 3477 4281 -68 436 397 C ATOM 1630 CG PHE B 258 1.916 -8.230 -27.178 1.00 32.38 C ANISOU 1630 CG PHE B 258 4730 3338 4235 -188 658 441 C ATOM 1631 CD1 PHE B 258 0.551 -8.436 -27.285 1.00 33.98 C ANISOU 1631 CD1 PHE B 258 4829 3561 4522 -445 840 377 C ATOM 1632 CD2 PHE B 258 2.722 -9.302 -26.824 1.00 35.17 C ANISOU 1632 CD2 PHE B 258 5433 3526 4406 -47 690 532 C ATOM 1633 CE1 PHE B 258 0.001 -9.687 -27.021 1.00 39.91 C ANISOU 1633 CE1 PHE B 258 5842 4137 5184 -656 1081 402 C ATOM 1634 CE2 PHE B 258 2.178 -10.547 -26.553 1.00 38.46 C ANISOU 1634 CE2 PHE B 258 6196 3708 4710 -184 921 579 C ATOM 1635 CZ PHE B 258 0.817 -10.737 -26.654 1.00 39.97 C ANISOU 1635 CZ PHE B 258 6301 3890 4996 -538 1130 514 C ATOM 1636 N LEU B 259 4.060 -6.891 -24.718 1.00 29.74 N ANISOU 1636 N LEU B 259 4587 3174 3537 342 384 494 N ATOM 1637 CA LEU B 259 4.441 -7.651 -23.529 1.00 35.91 C ANISOU 1637 CA LEU B 259 5715 3868 4061 537 450 568 C ATOM 1638 C LEU B 259 4.301 -6.835 -22.243 1.00 34.77 C ANISOU 1638 C LEU B 259 5627 3788 3795 609 446 542 C ATOM 1639 O LEU B 259 4.245 -7.392 -21.159 1.00 34.30 O ANISOU 1639 O LEU B 259 5890 3629 3514 737 559 606 O ATOM 1640 CB LEU B 259 5.877 -8.166 -23.661 1.00 38.64 C ANISOU 1640 CB LEU B 259 6130 4299 4254 817 262 590 C ATOM 1641 CG LEU B 259 6.125 -9.270 -24.694 1.00 36.87 C ANISOU 1641 CG LEU B 259 6003 3962 4045 855 294 635 C ATOM 1642 CD1 LEU B 259 7.611 -9.556 -24.837 1.00 36.39 C ANISOU 1642 CD1 LEU B 259 5908 4096 3820 1199 83 622 C ATOM 1643 CD2 LEU B 259 5.373 -10.526 -24.292 1.00 38.77 C ANISOU 1643 CD2 LEU B 259 6707 3874 4149 816 552 731 C ATOM 1644 N TYR B 260 4.236 -5.516 -22.366 1.00 34.22 N ANISOU 1644 N TYR B 260 5311 3852 3840 537 327 448 N ATOM 1645 CA TYR B 260 4.160 -4.658 -21.189 1.00 35.57 C ANISOU 1645 CA TYR B 260 5569 4068 3877 616 303 403 C ATOM 1646 C TYR B 260 2.729 -4.232 -20.843 1.00 36.19 C ANISOU 1646 C TYR B 260 5635 4099 4016 511 521 381 C ATOM 1647 O TYR B 260 2.514 -3.445 -19.925 1.00 37.37 O ANISOU 1647 O TYR B 260 5869 4274 4055 590 525 334 O ATOM 1648 CB TYR B 260 5.053 -3.429 -21.380 1.00 35.31 C ANISOU 1648 CB TYR B 260 5368 4185 3863 604 44 294 C ATOM 1649 CG TYR B 260 6.468 -3.675 -20.910 1.00 38.09 C ANISOU 1649 CG TYR B 260 5752 4700 4021 768 -161 270 C ATOM 1650 CD1 TYR B 260 6.887 -3.247 -19.654 1.00 43.32 C ANISOU 1650 CD1 TYR B 260 6564 5443 4454 897 -261 212 C ATOM 1651 CD2 TYR B 260 7.372 -4.370 -21.700 1.00 39.45 C ANISOU 1651 CD2 TYR B 260 5795 4986 4209 830 -262 286 C ATOM 1652 CE1 TYR B 260 8.173 -3.489 -19.209 1.00 47.45 C ANISOU 1652 CE1 TYR B 260 7062 6195 4770 1078 -479 157 C ATOM 1653 CE2 TYR B 260 8.663 -4.613 -21.264 1.00 42.75 C ANISOU 1653 CE2 TYR B 260 6176 5646 4420 1038 -462 236 C ATOM 1654 CZ TYR B 260 9.055 -4.169 -20.018 1.00 49.35 C ANISOU 1654 CZ TYR B 260 7121 6599 5031 1159 -580 165 C ATOM 1655 OH TYR B 260 10.331 -4.406 -19.574 1.00 58.00 O ANISOU 1655 OH TYR B 260 8129 8013 5896 1392 -810 82 O ATOM 1656 N ARG B 261 1.752 -4.772 -21.563 1.00 33.99 N ANISOU 1656 N ARG B 261 5240 3785 3891 344 700 396 N ATOM 1657 CA ARG B 261 0.355 -4.517 -21.235 1.00 33.99 C ANISOU 1657 CA ARG B 261 5150 3837 3926 251 928 351 C ATOM 1658 C ARG B 261 -0.120 -5.495 -20.165 1.00 36.13 C ANISOU 1658 C ARG B 261 5701 4015 4010 207 1215 427 C ATOM 1659 O ARG B 261 0.135 -6.693 -20.254 1.00 38.19 O ANISOU 1659 O ARG B 261 6183 4123 4203 134 1311 516 O ATOM 1660 CB ARG B 261 -0.530 -4.620 -22.481 1.00 32.56 C ANISOU 1660 CB ARG B 261 4659 3741 3970 69 980 291 C ATOM 1661 CG ARG B 261 -0.111 -3.702 -23.626 1.00 31.47 C ANISOU 1661 CG ARG B 261 4319 3654 3983 119 723 233 C ATOM 1662 CD ARG B 261 -1.269 -3.463 -24.569 1.00 31.20 C ANISOU 1662 CD ARG B 261 3984 3763 4108 39 768 141 C ATOM 1663 NE ARG B 261 -2.412 -2.934 -23.837 1.00 32.26 N ANISOU 1663 NE ARG B 261 4013 4057 4186 111 927 60 N ATOM 1664 CZ ARG B 261 -2.575 -1.652 -23.529 1.00 33.06 C ANISOU 1664 CZ ARG B 261 4127 4207 4228 339 837 -5 C ATOM 1665 NH1 ARG B 261 -1.675 -0.756 -23.908 1.00 32.10 N ANISOU 1665 NH1 ARG B 261 4142 3955 4099 445 598 0 N ATOM 1666 NH2 ARG B 261 -3.646 -1.272 -22.847 1.00 34.29 N ANISOU 1666 NH2 ARG B 261 4180 4542 4309 449 1005 -86 N ATOM 1667 N VAL B 262 -0.797 -4.975 -19.148 1.00 36.99 N ANISOU 1667 N VAL B 262 5860 4193 4002 264 1368 393 N ATOM 1668 CA VAL B 262 -1.342 -5.810 -18.084 1.00 38.97 C ANISOU 1668 CA VAL B 262 6402 4361 4045 192 1692 464 C ATOM 1669 C VAL B 262 -2.725 -5.320 -17.686 1.00 40.85 C ANISOU 1669 C VAL B 262 6420 4803 4299 99 1957 370 C ATOM 1670 O VAL B 262 -3.079 -4.164 -17.933 1.00 40.79 O ANISOU 1670 O VAL B 262 6132 4976 4391 230 1836 257 O ATOM 1671 CB VAL B 262 -0.443 -5.814 -16.819 1.00 46.57 C ANISOU 1671 CB VAL B 262 7785 5202 4707 457 1618 539 C ATOM 1672 CG1 VAL B 262 0.929 -6.379 -17.123 1.00 48.70 C ANISOU 1672 CG1 VAL B 262 8236 5356 4912 610 1361 610 C ATOM 1673 CG2 VAL B 262 -0.325 -4.408 -16.241 1.00 44.54 C ANISOU 1673 CG2 VAL B 262 7450 5071 4403 661 1452 440 C ATOM 1674 N VAL B 263 -3.510 -6.195 -17.064 1.00 41.75 N ANISOU 1674 N VAL B 263 6686 4895 4282 -118 2335 410 N ATOM 1675 CA VAL B 263 -4.726 -5.741 -16.407 1.00 44.90 C ANISOU 1675 CA VAL B 263 6894 5543 4622 -166 2623 317 C ATOM 1676 C VAL B 263 -4.429 -5.483 -14.939 1.00 48.16 C ANISOU 1676 C VAL B 263 7714 5855 4729 69 2710 382 C ATOM 1677 O VAL B 263 -3.499 -6.056 -14.367 1.00 46.23 O ANISOU 1677 O VAL B 263 7939 5340 4285 173 2647 513 O ATOM 1678 CB VAL B 263 -5.885 -6.740 -16.539 1.00 49.38 C ANISOU 1678 CB VAL B 263 7330 6226 5207 -614 3040 283 C ATOM 1679 CG1 VAL B 263 -6.148 -7.041 -18.002 1.00 43.44 C ANISOU 1679 CG1 VAL B 263 6195 5577 4733 -851 2924 200 C ATOM 1680 CG2 VAL B 263 -5.596 -8.007 -15.756 1.00 50.75 C ANISOU 1680 CG2 VAL B 263 8054 6067 5163 -779 3218 430 C ATOM 1681 N ARG B 264 -5.217 -4.597 -14.342 1.00 45.33 N ANISOU 1681 N ARG B 264 7183 5733 4307 203 2836 277 N ATOM 1682 CA ARG B 264 -5.000 -4.168 -12.973 1.00 48.00 C ANISOU 1682 CA ARG B 264 7890 6002 4346 462 2897 310 C ATOM 1683 C ARG B 264 -6.351 -4.013 -12.287 1.00 52.11 C ANISOU 1683 C ARG B 264 8235 6805 4759 391 3309 224 C ATOM 1684 O ARG B 264 -7.233 -3.325 -12.802 1.00 54.91 O ANISOU 1684 O ARG B 264 8108 7493 5262 429 3348 69 O ATOM 1685 CB ARG B 264 -4.213 -2.855 -12.956 1.00 50.42 C ANISOU 1685 CB ARG B 264 8215 6283 4658 823 2486 240 C ATOM 1686 CG ARG B 264 -4.043 -2.229 -11.592 1.00 59.34 C ANISOU 1686 CG ARG B 264 9701 7368 5477 1104 2508 228 C ATOM 1687 CD ARG B 264 -2.993 -2.959 -10.783 1.00 65.55 C ANISOU 1687 CD ARG B 264 11000 7901 6006 1172 2434 365 C ATOM 1688 NE ARG B 264 -1.663 -2.910 -11.391 1.00 63.08 N ANISOU 1688 NE ARG B 264 10712 7470 5785 1239 2004 381 N ATOM 1689 CZ ARG B 264 -0.734 -2.010 -11.083 1.00 57.63 C ANISOU 1689 CZ ARG B 264 10133 6761 5002 1452 1653 305 C ATOM 1690 NH1 ARG B 264 -0.992 -1.070 -10.185 1.00 56.77 N ANISOU 1690 NH1 ARG B 264 10180 6687 4704 1640 1664 214 N ATOM 1691 NH2 ARG B 264 0.452 -2.046 -11.672 1.00 55.02 N ANISOU 1691 NH2 ARG B 264 9755 6397 4752 1458 1302 302 N ATOM 1692 N GLU B 265 -6.530 -4.660 -11.140 1.00 53.54 N ANISOU 1692 N GLU B 265 8724 6880 4740 300 3485 304 N ATOM 1693 CA GLU B 265 -7.815 -4.599 -10.456 1.00 59.10 C ANISOU 1693 CA GLU B 265 9193 7890 5372 185 3800 216 C ATOM 1694 C GLU B 265 -7.860 -3.433 -9.471 1.00 62.49 C ANISOU 1694 C GLU B 265 9730 8407 5607 592 3752 148 C ATOM 1695 O GLU B 265 -6.944 -3.241 -8.673 1.00 62.25 O ANISOU 1695 O GLU B 265 10171 8094 5389 832 3574 232 O ATOM 1696 CB GLU B 265 -8.113 -5.921 -9.745 1.00 65.93 C ANISOU 1696 CB GLU B 265 10346 8592 6112 -156 4057 329 C ATOM 1697 CG GLU B 265 -9.545 -6.023 -9.243 1.00 78.61 C ANISOU 1697 CG GLU B 265 11616 10590 7662 -382 4416 236 C ATOM 1698 CD GLU B 265 -9.943 -7.435 -8.854 1.00 87.40 C ANISOU 1698 CD GLU B 265 12975 11531 8703 -820 4686 331 C ATOM 1699 OE1 GLU B 265 -9.073 -8.332 -8.874 1.00 87.15 O ANISOU 1699 OE1 GLU B 265 13447 11029 8637 -887 4587 463 O ATOM 1700 OE2 GLU B 265 -11.132 -7.644 -8.533 1.00 93.87 O ANISOU 1700 OE2 GLU B 265 13494 12688 9484 -1074 4996 261 O ATOM 1701 N GLU B 266 -8.934 -2.652 -9.556 1.00 67.52 N ANISOU 1701 N GLU B 266 9914 9460 6283 688 3878 -25 N ATOM 1702 CA GLU B 266 -9.144 -1.474 -8.717 1.00 71.97 C ANISOU 1702 CA GLU B 266 10548 10124 6674 1091 3829 -125 C ATOM 1703 C GLU B 266 -10.188 -1.799 -7.643 1.00 74.88 C ANISOU 1703 C GLU B 266 10845 10753 6855 960 4195 -161 C ATOM 1704 O GLU B 266 -10.870 -2.818 -7.741 1.00 76.96 O ANISOU 1704 O GLU B 266 10898 11195 7148 552 4471 -133 O ATOM 1705 CB GLU B 266 -9.584 -0.286 -9.585 1.00 77.37 C ANISOU 1705 CB GLU B 266 10821 11069 7508 1386 3667 -311 C ATOM 1706 CG GLU B 266 -9.661 1.063 -8.881 1.00 84.33 C ANISOU 1706 CG GLU B 266 11866 11948 8229 1850 3519 -413 C ATOM 1707 CD GLU B 266 -10.186 2.160 -9.788 1.00 86.31 C ANISOU 1707 CD GLU B 266 11763 12412 8621 2155 3338 -584 C ATOM 1708 OE1 GLU B 266 -9.757 2.219 -10.959 1.00 84.46 O ANISOU 1708 OE1 GLU B 266 11407 12106 8578 2146 3126 -576 O ATOM 1709 OE2 GLU B 266 -11.031 2.957 -9.328 1.00 90.46 O ANISOU 1709 OE2 GLU B 266 12159 13159 9053 2424 3398 -719 O ATOM 1710 N TYR B 267 -10.317 -0.950 -6.624 1.00 71.46 N ANISOU 1710 N TYR B 267 11230 10515 5406 -1074 2975 745 N ATOM 1711 CA TYR B 267 -11.212 -1.256 -5.507 1.00 76.95 C ANISOU 1711 CA TYR B 267 11898 11471 5868 -1237 3165 761 C ATOM 1712 C TYR B 267 -12.150 -0.123 -5.071 1.00 80.41 C ANISOU 1712 C TYR B 267 12325 11975 6254 -1136 3503 346 C ATOM 1713 O TYR B 267 -13.130 -0.373 -4.367 1.00 83.91 O ANISOU 1713 O TYR B 267 12677 12607 6597 -1195 3716 342 O ATOM 1714 CB TYR B 267 -10.387 -1.715 -4.301 1.00 84.99 C ANISOU 1714 CB TYR B 267 13063 12745 6485 -1523 2930 1045 C ATOM 1715 CG TYR B 267 -9.596 -2.972 -4.568 1.00 88.79 C ANISOU 1715 CG TYR B 267 13503 13159 7076 -1541 2657 1585 C ATOM 1716 CD1 TYR B 267 -10.240 -4.167 -4.859 1.00 89.91 C ANISOU 1716 CD1 TYR B 267 13541 13152 7470 -1519 2770 1853 C ATOM 1717 CD2 TYR B 267 -8.208 -2.966 -4.534 1.00 91.76 C ANISOU 1717 CD2 TYR B 267 13922 13602 7340 -1569 2313 1841 C ATOM 1718 CE1 TYR B 267 -9.525 -5.320 -5.113 1.00 91.72 C ANISOU 1718 CE1 TYR B 267 13773 13192 7885 -1485 2609 2354 C ATOM 1719 CE2 TYR B 267 -7.483 -4.117 -4.783 1.00 92.97 C ANISOU 1719 CE2 TYR B 267 13999 13645 7679 -1480 2113 2401 C ATOM 1720 CZ TYR B 267 -8.147 -5.290 -5.073 1.00 92.73 C ANISOU 1720 CZ TYR B 267 13930 13358 7944 -1419 2295 2654 C ATOM 1721 OH TYR B 267 -7.428 -6.435 -5.324 1.00 93.52 O ANISOU 1721 OH TYR B 267 14003 13221 8310 -1278 2195 3202 O ATOM 1722 N PHE B 268 -11.864 1.112 -5.474 1.00 81.70 N ANISOU 1722 N PHE B 268 12588 11948 6509 -969 3580 22 N ATOM 1723 CA PHE B 268 -12.698 2.242 -5.060 1.00 87.30 C ANISOU 1723 CA PHE B 268 13320 12617 7235 -825 3953 -332 C ATOM 1724 C PHE B 268 -12.817 3.317 -6.143 1.00 90.71 C ANISOU 1724 C PHE B 268 13687 12724 8053 -440 4098 -542 C ATOM 1725 O PHE B 268 -12.034 4.268 -6.157 1.00 93.79 O ANISOU 1725 O PHE B 268 14339 12886 8409 -471 4078 -764 O ATOM 1726 CB PHE B 268 -12.145 2.864 -3.774 1.00 89.87 C ANISOU 1726 CB PHE B 268 13980 13033 7134 -1158 3977 -541 C ATOM 1727 N PRO B 269 -13.801 3.172 -7.053 1.00 89.92 N ANISOU 1727 N PRO B 269 13211 12635 8318 -104 4231 -438 N ATOM 1728 CA PRO B 269 -14.757 2.059 -7.109 1.00 85.98 C ANISOU 1728 CA PRO B 269 12374 12441 7854 -148 4255 -194 C ATOM 1729 C PRO B 269 -14.108 0.814 -7.705 1.00 76.10 C ANISOU 1729 C PRO B 269 11101 11181 6634 -339 3932 89 C ATOM 1730 O PRO B 269 -13.175 0.944 -8.495 1.00 70.81 O ANISOU 1730 O PRO B 269 10533 10277 6093 -268 3729 107 O ATOM 1731 CB PRO B 269 -15.865 2.596 -8.018 1.00 88.46 C ANISOU 1731 CB PRO B 269 12262 12808 8540 253 4471 -194 C ATOM 1732 CG PRO B 269 -15.143 3.513 -8.957 1.00 87.04 C ANISOU 1732 CG PRO B 269 12175 12278 8618 522 4386 -283 C ATOM 1733 CD PRO B 269 -14.013 4.130 -8.156 1.00 88.96 C ANISOU 1733 CD PRO B 269 12939 12263 8600 315 4340 -519 C ATOM 1734 N PRO B 270 -14.579 -0.379 -7.318 1.00 74.16 N ANISOU 1734 N PRO B 270 10749 11144 6285 -582 3908 315 N ATOM 1735 CA PRO B 270 -13.967 -1.604 -7.838 1.00 71.63 C ANISOU 1735 CA PRO B 270 10461 10708 6046 -775 3660 597 C ATOM 1736 C PRO B 270 -14.159 -1.760 -9.347 1.00 71.40 C ANISOU 1736 C PRO B 270 10144 10570 6413 -614 3587 614 C ATOM 1737 O PRO B 270 -15.275 -1.623 -9.848 1.00 78.01 O ANISOU 1737 O PRO B 270 10627 11636 7375 -520 3788 572 O ATOM 1738 CB PRO B 270 -14.695 -2.714 -7.072 1.00 73.64 C ANISOU 1738 CB PRO B 270 10645 11175 6161 -1047 3730 800 C ATOM 1739 CG PRO B 270 -15.991 -2.106 -6.666 1.00 76.00 C ANISOU 1739 CG PRO B 270 10699 11764 6413 -927 4028 624 C ATOM 1740 CD PRO B 270 -15.697 -0.660 -6.403 1.00 74.40 C ANISOU 1740 CD PRO B 270 10641 11479 6150 -686 4135 332 C ATOM 1741 N LYS B 271 -13.066 -2.019 -10.057 1.00 62.70 N ANISOU 1741 N LYS B 271 9133 9185 5506 -584 3256 693 N ATOM 1742 CA LYS B 271 -13.132 -2.384 -11.466 1.00 62.15 C ANISOU 1742 CA LYS B 271 8812 9015 5788 -534 3125 712 C ATOM 1743 C LYS B 271 -11.815 -2.976 -11.941 1.00 57.91 C ANISOU 1743 C LYS B 271 8458 8129 5415 -568 2822 844 C ATOM 1744 O LYS B 271 -10.862 -3.100 -11.176 1.00 53.22 O ANISOU 1744 O LYS B 271 8122 7429 4668 -598 2686 984 O ATOM 1745 CB LYS B 271 -13.505 -1.180 -12.339 1.00 63.76 C ANISOU 1745 CB LYS B 271 8764 9296 6166 -204 3176 536 C ATOM 1746 CG LYS B 271 -12.481 -0.062 -12.393 1.00 63.63 C ANISOU 1746 CG LYS B 271 8979 9026 6172 39 3051 397 C ATOM 1747 CD LYS B 271 -12.972 1.042 -13.317 1.00 67.18 C ANISOU 1747 CD LYS B 271 9174 9516 6838 392 3166 302 C ATOM 1748 CE LYS B 271 -12.279 2.355 -13.026 1.00 72.76 C ANISOU 1748 CE LYS B 271 10186 9960 7501 611 3241 110 C ATOM 1749 NZ LYS B 271 -13.159 3.507 -13.359 1.00 77.62 N ANISOU 1749 NZ LYS B 271 10611 10616 8264 1013 3599 62 N ATOM 1750 N VAL B 272 -11.782 -3.350 -13.213 1.00 50.88 N ANISOU 1750 N VAL B 272 7400 7118 4813 -580 2736 822 N ATOM 1751 CA VAL B 272 -10.582 -3.882 -13.829 1.00 48.80 C ANISOU 1751 CA VAL B 272 7280 6498 4763 -570 2523 921 C ATOM 1752 C VAL B 272 -10.122 -2.939 -14.938 1.00 51.95 C ANISOU 1752 C VAL B 272 7551 6840 5348 -344 2347 745 C ATOM 1753 O VAL B 272 -10.870 -2.655 -15.875 1.00 49.95 O ANISOU 1753 O VAL B 272 7021 6760 5196 -340 2398 623 O ATOM 1754 CB VAL B 272 -10.817 -5.292 -14.403 1.00 49.86 C ANISOU 1754 CB VAL B 272 7426 6445 5073 -862 2653 1016 C ATOM 1755 CG1 VAL B 272 -9.539 -5.834 -15.025 1.00 48.42 C ANISOU 1755 CG1 VAL B 272 7411 5831 5155 -789 2527 1126 C ATOM 1756 CG2 VAL B 272 -11.336 -6.227 -13.322 1.00 53.34 C ANISOU 1756 CG2 VAL B 272 8015 6912 5339 -1102 2869 1216 C ATOM 1757 N LEU B 273 -8.893 -2.448 -14.816 1.00 44.21 N ANISOU 1757 N LEU B 273 6743 5680 4376 -184 2136 770 N ATOM 1758 CA LEU B 273 -8.308 -1.582 -15.830 1.00 41.52 C ANISOU 1758 CA LEU B 273 6328 5245 4202 4 1968 624 C ATOM 1759 C LEU B 273 -7.353 -2.355 -16.735 1.00 39.87 C ANISOU 1759 C LEU B 273 6141 4759 4250 -34 1825 709 C ATOM 1760 O LEU B 273 -6.718 -3.317 -16.303 1.00 40.97 O ANISOU 1760 O LEU B 273 6424 4716 4425 -100 1823 934 O ATOM 1761 CB LEU B 273 -7.576 -0.410 -15.173 1.00 41.41 C ANISOU 1761 CB LEU B 273 6496 5233 4003 142 1870 540 C ATOM 1762 CG LEU B 273 -8.477 0.538 -14.380 1.00 48.89 C ANISOU 1762 CG LEU B 273 7485 6363 4727 206 2118 380 C ATOM 1763 CD1 LEU B 273 -7.664 1.539 -13.577 1.00 50.97 C ANISOU 1763 CD1 LEU B 273 8043 6592 4732 187 2089 249 C ATOM 1764 CD2 LEU B 273 -9.438 1.257 -15.316 1.00 43.29 C ANISOU 1764 CD2 LEU B 273 6512 5727 4208 428 2276 266 C ATOM 1765 N CYS B 274 -7.279 -1.933 -17.993 1.00 37.83 N ANISOU 1765 N CYS B 274 5731 4472 4173 26 1748 561 N ATOM 1766 CA CYS B 274 -6.318 -2.472 -18.947 1.00 37.06 C ANISOU 1766 CA CYS B 274 5662 4109 4313 2 1649 579 C ATOM 1767 C CYS B 274 -5.362 -1.357 -19.359 1.00 38.16 C ANISOU 1767 C CYS B 274 5806 4209 4484 209 1423 501 C ATOM 1768 O CYS B 274 -5.799 -0.272 -19.757 1.00 39.29 O ANISOU 1768 O CYS B 274 5842 4498 4588 319 1399 358 O ATOM 1769 CB CYS B 274 -7.029 -3.051 -20.171 1.00 38.31 C ANISOU 1769 CB CYS B 274 5650 4307 4599 -233 1774 445 C ATOM 1770 SG CYS B 274 -5.935 -3.515 -21.531 1.00 45.33 S ANISOU 1770 SG CYS B 274 6585 4879 5758 -292 1728 364 S ATOM 1771 N GLY B 275 -4.061 -1.608 -19.254 1.00 36.26 N ANISOU 1771 N GLY B 275 5675 3785 4317 274 1284 634 N ATOM 1772 CA GLY B 275 -3.101 -0.550 -19.505 1.00 34.58 C ANISOU 1772 CA GLY B 275 5477 3580 4079 399 1071 563 C ATOM 1773 C GLY B 275 -1.666 -0.995 -19.676 1.00 33.93 C ANISOU 1773 C GLY B 275 5407 3360 4125 455 929 744 C ATOM 1774 O GLY B 275 -1.397 -2.175 -19.900 1.00 33.12 O ANISOU 1774 O GLY B 275 5299 3057 4228 457 1047 917 O ATOM 1775 N VAL B 276 -0.745 -0.036 -19.586 1.00 34.66 N ANISOU 1775 N VAL B 276 5517 3550 4100 494 723 712 N ATOM 1776 CA VAL B 276 0.682 -0.322 -19.702 1.00 34.22 C ANISOU 1776 CA VAL B 276 5391 3483 4126 554 563 927 C ATOM 1777 C VAL B 276 1.312 -0.288 -18.314 1.00 37.31 C ANISOU 1777 C VAL B 276 5808 4167 4202 492 422 1203 C ATOM 1778 O VAL B 276 0.825 0.412 -17.427 1.00 39.38 O ANISOU 1778 O VAL B 276 6205 4626 4134 346 417 1079 O ATOM 1779 CB VAL B 276 1.403 0.683 -20.637 1.00 33.46 C ANISOU 1779 CB VAL B 276 5252 3384 4077 558 408 728 C ATOM 1780 CG1 VAL B 276 0.798 0.644 -22.039 1.00 29.46 C ANISOU 1780 CG1 VAL B 276 4686 2685 3822 578 524 505 C ATOM 1781 CG2 VAL B 276 1.347 2.100 -20.063 1.00 35.40 C ANISOU 1781 CG2 VAL B 276 5646 3800 4005 440 320 528 C ATOM 1782 N ASP B 277 2.384 -1.051 -18.121 1.00 38.02 N ANISOU 1782 N ASP B 277 5751 4320 4376 597 340 1601 N ATOM 1783 CA ASP B 277 3.043 -1.108 -16.817 1.00 41.68 C ANISOU 1783 CA ASP B 277 6148 5201 4488 512 167 1975 C ATOM 1784 C ASP B 277 4.561 -1.001 -16.920 1.00 42.53 C ANISOU 1784 C ASP B 277 6001 5592 4567 558 -70 2277 C ATOM 1785 O ASP B 277 5.255 -2.000 -17.096 1.00 45.17 O ANISOU 1785 O ASP B 277 6126 5860 5178 825 -15 2725 O ATOM 1786 CB ASP B 277 2.667 -2.400 -16.084 1.00 48.17 C ANISOU 1786 CB ASP B 277 6967 5960 5378 628 337 2395 C ATOM 1787 CG ASP B 277 3.142 -2.418 -14.633 1.00 59.73 C ANISOU 1787 CG ASP B 277 8352 7959 6384 490 149 2814 C ATOM 1788 OD1 ASP B 277 3.336 -1.334 -14.048 1.00 60.43 O ANISOU 1788 OD1 ASP B 277 8491 8456 6015 184 -52 2611 O ATOM 1789 OD2 ASP B 277 3.315 -3.522 -14.074 1.00 67.63 O ANISOU 1789 OD2 ASP B 277 9256 8976 7462 657 233 3357 O ATOM 1790 N TYR B 278 5.067 0.219 -16.798 1.00 43.94 N ANISOU 1790 N TYR B 278 6200 6083 4412 290 -289 2043 N ATOM 1791 CA TYR B 278 6.500 0.441 -16.703 1.00 44.39 C ANISOU 1791 CA TYR B 278 5976 6583 4307 213 -553 2335 C ATOM 1792 C TYR B 278 6.859 0.892 -15.294 1.00 58.40 C ANISOU 1792 C TYR B 278 7725 9021 5445 -178 -773 2514 C ATOM 1793 O TYR B 278 7.719 1.751 -15.113 1.00 60.14 O ANISOU 1793 O TYR B 278 7866 9687 5298 -524 -998 2446 O ATOM 1794 CB TYR B 278 6.962 1.477 -17.728 1.00 42.89 C ANISOU 1794 CB TYR B 278 5822 6293 4180 98 -629 1932 C ATOM 1795 CG TYR B 278 6.718 1.056 -19.155 1.00 40.17 C ANISOU 1795 CG TYR B 278 5469 5407 4386 408 -439 1773 C ATOM 1796 CD1 TYR B 278 7.587 0.189 -19.799 1.00 42.14 C ANISOU 1796 CD1 TYR B 278 5436 5584 4990 694 -397 2107 C ATOM 1797 CD2 TYR B 278 5.611 1.516 -19.855 1.00 38.71 C ANISOU 1797 CD2 TYR B 278 5540 4826 4342 402 -269 1312 C ATOM 1798 CE1 TYR B 278 7.365 -0.206 -21.103 1.00 42.78 C ANISOU 1798 CE1 TYR B 278 5553 5186 5515 887 -177 1904 C ATOM 1799 CE2 TYR B 278 5.380 1.130 -21.157 1.00 40.84 C ANISOU 1799 CE2 TYR B 278 5782 4716 5020 584 -114 1170 C ATOM 1800 CZ TYR B 278 6.259 0.267 -21.775 1.00 44.41 C ANISOU 1800 CZ TYR B 278 6014 5079 5780 786 -61 1426 C ATOM 1801 OH TYR B 278 6.021 -0.117 -23.070 1.00 48.08 O ANISOU 1801 OH TYR B 278 6495 5179 6594 879 138 1225 O ATOM 1802 N SER B 279 6.186 0.313 -14.300 1.00 58.49 N ANISOU 1802 N SER B 279 7814 9130 5280 -193 -693 2725 N ATOM 1803 CA SER B 279 6.414 0.667 -12.902 1.00 66.52 C ANISOU 1803 CA SER B 279 8827 10825 5623 -630 -875 2890 C ATOM 1804 C SER B 279 7.817 0.283 -12.468 1.00 70.09 C ANISOU 1804 C SER B 279 8792 11833 6008 -636 -1126 3381 C ATOM 1805 O SER B 279 8.300 -0.800 -12.799 1.00 72.54 O ANISOU 1805 O SER B 279 8787 11997 6779 -183 -1070 3834 O ATOM 1806 CB SER B 279 5.384 -0.007 -11.992 1.00 71.59 C ANISOU 1806 CB SER B 279 9626 11416 6159 -601 -703 3033 C ATOM 1807 OG SER B 279 5.589 -1.409 -11.939 1.00 77.56 O ANISOU 1807 OG SER B 279 10120 12042 7306 -177 -639 3613 O ATOM 1808 N HIS B 280 8.461 1.182 -11.727 1.00 72.48 N ANISOU 1808 N HIS B 280 9033 12699 5809 -1165 -1318 3200 N ATOM 1809 CA HIS B 280 9.843 1.007 -11.287 1.00 77.73 C ANISOU 1809 CA HIS B 280 9167 13979 6387 -1279 -1540 3596 C ATOM 1810 C HIS B 280 10.789 0.881 -12.479 1.00 76.02 C ANISOU 1810 C HIS B 280 8648 13658 6580 -971 -1586 3750 C ATOM 1811 O HIS B 280 11.854 0.270 -12.376 1.00 84.52 O ANISOU 1811 O HIS B 280 9210 15093 7810 -797 -1657 4246 O ATOM 1812 CB HIS B 280 9.985 -0.216 -10.370 1.00 81.56 C ANISOU 1812 CB HIS B 280 9318 14721 6951 -1037 -1536 4218 C ATOM 1813 CG HIS B 280 9.142 -0.146 -9.135 1.00 84.84 C ANISOU 1813 CG HIS B 280 9981 15312 6943 -1361 -1504 4111 C ATOM 1814 ND1 HIS B 280 8.101 -1.016 -8.894 1.00 84.35 N ANISOU 1814 ND1 HIS B 280 10130 14856 7065 -1049 -1304 4254 N ATOM 1815 CD2 HIS B 280 9.183 0.695 -8.075 1.00 89.89 C ANISOU 1815 CD2 HIS B 280 10704 16460 6991 -2005 -1604 3848 C ATOM 1816 CE1 HIS B 280 7.540 -0.718 -7.735 1.00 87.44 C ANISOU 1816 CE1 HIS B 280 10704 15539 6981 -1456 -1305 4104 C ATOM 1817 NE2 HIS B 280 8.178 0.318 -7.218 1.00 91.12 N ANISOU 1817 NE2 HIS B 280 11104 16540 6980 -2039 -1476 3843 N ATOM 1818 N ASP B 281 10.402 1.472 -13.603 1.00 65.67 N ANISOU 1818 N ASP B 281 7640 11877 5434 -911 -1518 3338 N ATOM 1819 CA ASP B 281 11.249 1.480 -14.781 1.00 64.28 C ANISOU 1819 CA ASP B 281 7219 11590 5615 -675 -1553 3405 C ATOM 1820 C ASP B 281 10.935 2.705 -15.629 1.00 59.95 C ANISOU 1820 C ASP B 281 7057 10788 4935 -958 -1570 2808 C ATOM 1821 O ASP B 281 10.479 2.589 -16.767 1.00 54.99 O ANISOU 1821 O ASP B 281 6578 9541 4772 -620 -1403 2600 O ATOM 1822 CB ASP B 281 11.056 0.194 -15.587 1.00 69.62 C ANISOU 1822 CB ASP B 281 7773 11709 6970 18 -1317 3740 C ATOM 1823 CG ASP B 281 12.302 -0.206 -16.357 1.00 80.19 C ANISOU 1823 CG ASP B 281 8667 13125 8676 301 -1295 4021 C ATOM 1824 OD1 ASP B 281 12.437 -1.401 -16.702 1.00 84.35 O ANISOU 1824 OD1 ASP B 281 9031 13303 9716 807 -1027 4347 O ATOM 1825 OD2 ASP B 281 13.150 0.676 -16.613 1.00 83.38 O ANISOU 1825 OD2 ASP B 281 8916 13917 8847 -19 -1490 3880 O ATOM 1826 N LYS B 282 11.174 3.882 -15.058 1.00 58.37 N ANISOU 1826 N LYS B 282 7037 10909 4230 -1584 -1652 2404 N ATOM 1827 CA LYS B 282 10.908 5.142 -15.740 1.00 59.67 C ANISOU 1827 CA LYS B 282 7641 10763 4269 -1904 -1581 1776 C ATOM 1828 C LYS B 282 11.864 5.331 -16.916 1.00 58.22 C ANISOU 1828 C LYS B 282 7204 10572 4345 -1803 -1689 1814 C ATOM 1829 O LYS B 282 11.556 6.046 -17.870 1.00 56.08 O ANISOU 1829 O LYS B 282 7240 9784 4286 -1797 -1548 1353 O ATOM 1830 CB LYS B 282 11.020 6.309 -14.753 1.00 59.45 C ANISOU 1830 CB LYS B 282 7877 10969 3741 -2594 -1513 1338 C ATOM 1831 CG LYS B 282 10.676 7.680 -15.319 1.00 57.49 C ANISOU 1831 CG LYS B 282 8161 10236 3445 -2896 -1290 663 C ATOM 1832 CD LYS B 282 9.212 7.792 -15.743 1.00 65.93 C ANISOU 1832 CD LYS B 282 9751 10624 4677 -2611 -1011 323 C ATOM 1833 CE LYS B 282 8.910 9.196 -16.265 1.00 65.41 C ANISOU 1833 CE LYS B 282 10179 9998 4676 -2817 -699 -286 C ATOM 1834 NZ LYS B 282 7.579 9.340 -16.929 1.00 56.33 N ANISOU 1834 NZ LYS B 282 9365 8094 3943 -2350 -368 -543 N ATOM 1835 N ARG B 283 13.021 4.678 -16.852 1.00 57.37 N ANISOU 1835 N ARG B 283 6516 10908 4374 -1649 -1822 2313 N ATOM 1836 CA ARG B 283 14.000 4.761 -17.931 1.00 56.71 C ANISOU 1836 CA ARG B 283 6135 10860 4552 -1525 -1882 2391 C ATOM 1837 C ARG B 283 13.507 4.025 -19.174 1.00 56.00 C ANISOU 1837 C ARG B 283 6058 10160 5061 -898 -1751 2470 C ATOM 1838 O ARG B 283 13.763 4.453 -20.305 1.00 56.14 O ANISOU 1838 O ARG B 283 6125 9867 5339 -858 -1683 2183 O ATOM 1839 CB ARG B 283 15.348 4.193 -17.484 1.00 63.85 C ANISOU 1839 CB ARG B 283 6402 12402 5457 -1491 -1967 2939 C ATOM 1840 N ARG B 284 12.798 2.920 -18.963 1.00 53.28 N ANISOU 1840 N ARG B 284 5714 9488 5043 -428 -1576 2737 N ATOM 1841 CA ARG B 284 12.293 2.120 -20.075 1.00 51.70 C ANISOU 1841 CA ARG B 284 5581 8548 5514 115 -1273 2671 C ATOM 1842 C ARG B 284 11.116 2.816 -20.745 1.00 43.80 C ANISOU 1842 C ARG B 284 5097 6916 4628 17 -1098 1994 C ATOM 1843 O ARG B 284 11.003 2.830 -21.967 1.00 44.01 O ANISOU 1843 O ARG B 284 5185 6513 5022 185 -951 1750 O ATOM 1844 CB ARG B 284 11.885 0.720 -19.601 1.00 56.51 C ANISOU 1844 CB ARG B 284 6083 8980 6407 569 -1084 3153 C ATOM 1845 CG ARG B 284 11.180 -0.109 -20.668 1.00 54.36 C ANISOU 1845 CG ARG B 284 5997 7904 6753 983 -699 2976 C ATOM 1846 CD ARG B 284 11.389 -1.598 -20.455 1.00 62.58 C ANISOU 1846 CD ARG B 284 6844 8761 8172 1427 -415 3468 C ATOM 1847 NE ARG B 284 12.619 -2.071 -21.085 1.00 67.61 N ANISOU 1847 NE ARG B 284 7128 9461 9099 1649 -279 3670 N ATOM 1848 CZ ARG B 284 13.657 -2.576 -20.424 1.00 76.76 C ANISOU 1848 CZ ARG B 284 7885 11078 10204 1751 -290 4156 C ATOM 1849 NH1 ARG B 284 13.621 -2.687 -19.100 1.00 82.00 N ANISOU 1849 NH1 ARG B 284 8433 12191 10533 1625 -455 4470 N ATOM 1850 NH2 ARG B 284 14.730 -2.979 -21.091 1.00 79.33 N ANISOU 1850 NH2 ARG B 284 7910 11429 10801 1972 -110 4347 N ATOM 1851 N GLU B 285 10.242 3.391 -19.930 1.00 42.74 N ANISOU 1851 N GLU B 285 5305 6774 4160 -253 -1095 1731 N ATOM 1852 CA GLU B 285 9.115 4.159 -20.429 1.00 41.14 C ANISOU 1852 CA GLU B 285 5540 6060 4032 -314 -912 1180 C ATOM 1853 C GLU B 285 9.603 5.256 -21.377 1.00 42.45 C ANISOU 1853 C GLU B 285 5803 6129 4199 -514 -949 842 C ATOM 1854 O GLU B 285 9.078 5.431 -22.479 1.00 38.78 O ANISOU 1854 O GLU B 285 5462 5218 4054 -337 -801 597 O ATOM 1855 CB GLU B 285 8.337 4.760 -19.259 1.00 45.39 C ANISOU 1855 CB GLU B 285 6404 6696 4147 -612 -870 980 C ATOM 1856 CG GLU B 285 7.255 5.737 -19.659 0.68 48.03 C ANISOU 1856 CG GLU B 285 7162 6556 4530 -653 -638 470 C ATOM 1857 CD GLU B 285 6.666 6.460 -18.465 0.74 55.61 C ANISOU 1857 CD GLU B 285 8470 7614 5047 -982 -521 242 C ATOM 1858 OE1 GLU B 285 6.516 5.824 -17.398 0.88 55.38 O ANISOU 1858 OE1 GLU B 285 8370 7886 4786 -1043 -568 475 O ATOM 1859 OE2 GLU B 285 6.364 7.666 -18.591 1.00 59.84 O ANISOU 1859 OE2 GLU B 285 9369 7903 5466 -1182 -339 -162 O ATOM 1860 N ARG B 286 10.630 5.979 -20.940 1.00 46.15 N ANISOU 1860 N ARG B 286 6194 7074 4265 -931 -1149 860 N ATOM 1861 CA ARG B 286 11.231 7.041 -21.743 1.00 44.66 C ANISOU 1861 CA ARG B 286 6107 6837 4025 -1199 -1179 568 C ATOM 1862 C ARG B 286 11.899 6.466 -23.000 1.00 41.31 C ANISOU 1862 C ARG B 286 5342 6325 4029 -882 -1199 736 C ATOM 1863 O ARG B 286 11.838 7.049 -24.084 1.00 36.79 O ANISOU 1863 O ARG B 286 4913 5427 3639 -882 -1113 462 O ATOM 1864 CB ARG B 286 12.240 7.830 -20.893 1.00 52.42 C ANISOU 1864 CB ARG B 286 7056 8449 4412 -1826 -1382 564 C ATOM 1865 CG ARG B 286 12.796 9.073 -21.562 1.00 53.91 C ANISOU 1865 CG ARG B 286 7460 8557 4466 -2231 -1361 201 C ATOM 1866 CD ARG B 286 13.132 10.137 -20.529 1.00 56.93 C ANISOU 1866 CD ARG B 286 8104 9218 4310 -2895 -1308 -43 C ATOM 1867 NE ARG B 286 13.760 9.567 -19.337 1.00 65.95 N ANISOU 1867 NE ARG B 286 8850 11050 5158 -3073 -1478 332 N ATOM 1868 CZ ARG B 286 15.050 9.247 -19.234 0.60 72.05 C ANISOU 1868 CZ ARG B 286 9078 12439 5857 -3183 -1669 710 C ATOM 1869 NH1 ARG B 286 15.871 9.427 -20.261 1.00 77.57 N ANISOU 1869 NH1 ARG B 286 9571 13160 6741 -3141 -1719 741 N ATOM 1870 NH2 ARG B 286 15.522 8.739 -18.099 0.68 70.98 N ANISOU 1870 NH2 ARG B 286 8587 12916 5466 -3331 -1784 1080 N ATOM 1871 N ALA B 287 12.518 5.301 -22.849 1.00 41.14 N ANISOU 1871 N ALA B 287 4878 6579 4176 -594 -1265 1215 N ATOM 1872 CA ALA B 287 13.215 4.656 -23.951 1.00 38.29 C ANISOU 1872 CA ALA B 287 4192 6128 4228 -276 -1198 1391 C ATOM 1873 C ALA B 287 12.229 4.211 -25.020 1.00 39.31 C ANISOU 1873 C ALA B 287 4542 5585 4809 42 -921 1137 C ATOM 1874 O ALA B 287 12.474 4.394 -26.214 1.00 35.06 O ANISOU 1874 O ALA B 287 3990 4847 4486 73 -840 954 O ATOM 1875 CB ALA B 287 14.029 3.470 -23.439 1.00 42.22 C ANISOU 1875 CB ALA B 287 4185 7015 4841 37 -1232 2026 C ATOM 1876 N VAL B 288 11.113 3.634 -24.585 1.00 35.69 N ANISOU 1876 N VAL B 288 4272 4845 4443 217 -779 1126 N ATOM 1877 CA VAL B 288 10.081 3.179 -25.507 1.00 33.62 C ANISOU 1877 CA VAL B 288 4194 4061 4521 417 -528 893 C ATOM 1878 C VAL B 288 9.468 4.360 -26.252 1.00 33.12 C ANISOU 1878 C VAL B 288 4405 3806 4373 217 -535 470 C ATOM 1879 O VAL B 288 9.247 4.300 -27.461 1.00 31.80 O ANISOU 1879 O VAL B 288 4249 3406 4427 273 -418 302 O ATOM 1880 CB VAL B 288 8.972 2.399 -24.768 1.00 34.04 C ANISOU 1880 CB VAL B 288 4383 3933 4618 563 -385 973 C ATOM 1881 CG1 VAL B 288 7.809 2.097 -25.699 1.00 31.20 C ANISOU 1881 CG1 VAL B 288 4202 3155 4498 631 -154 689 C ATOM 1882 CG2 VAL B 288 9.528 1.114 -24.167 1.00 36.11 C ANISOU 1882 CG2 VAL B 288 4393 4285 5041 831 -301 1460 C ATOM 1883 N ALA B 289 9.203 5.438 -25.519 1.00 33.82 N ANISOU 1883 N ALA B 289 4725 3995 4128 -26 -633 320 N ATOM 1884 CA ALA B 289 8.587 6.618 -26.099 1.00 32.09 C ANISOU 1884 CA ALA B 289 4797 3541 3856 -146 -568 -2 C ATOM 1885 C ALA B 289 9.473 7.197 -27.190 1.00 32.92 C ANISOU 1885 C ALA B 289 4831 3662 4015 -271 -630 -87 C ATOM 1886 O ALA B 289 8.981 7.571 -28.248 1.00 30.72 O ANISOU 1886 O ALA B 289 4640 3149 3883 -214 -538 -232 O ATOM 1887 CB ALA B 289 8.311 7.658 -25.025 1.00 32.87 C ANISOU 1887 CB ALA B 289 5209 3684 3595 -399 -560 -151 C ATOM 1888 N ILE B 290 10.777 7.255 -26.929 1.00 32.97 N ANISOU 1888 N ILE B 290 4636 4015 3874 -459 -793 43 N ATOM 1889 CA ILE B 290 11.733 7.833 -27.873 1.00 33.17 C ANISOU 1889 CA ILE B 290 4572 4122 3908 -634 -856 -30 C ATOM 1890 C ILE B 290 11.875 6.982 -29.131 1.00 32.66 C ANISOU 1890 C ILE B 290 4274 3922 4213 -375 -751 21 C ATOM 1891 O ILE B 290 11.875 7.503 -30.249 1.00 30.83 O ANISOU 1891 O ILE B 290 4116 3544 4056 -446 -703 -148 O ATOM 1892 CB ILE B 290 13.125 8.014 -27.230 1.00 36.34 C ANISOU 1892 CB ILE B 290 4723 5058 4025 -932 -1062 145 C ATOM 1893 CG1 ILE B 290 13.081 9.088 -26.138 1.00 35.72 C ANISOU 1893 CG1 ILE B 290 4959 5132 3479 -1385 -1126 -24 C ATOM 1894 CG2 ILE B 290 14.167 8.371 -28.289 1.00 37.06 C ANISOU 1894 CG2 ILE B 290 4630 5276 4177 -1072 -1106 115 C ATOM 1895 CD1 ILE B 290 14.308 9.083 -25.233 1.00 38.79 C ANISOU 1895 CD1 ILE B 290 5041 6224 3473 -1758 -1365 205 C ATOM 1896 N VAL B 291 11.989 5.673 -28.944 1.00 33.66 N ANISOU 1896 N VAL B 291 4152 4080 4560 -96 -670 256 N ATOM 1897 CA VAL B 291 12.135 4.756 -30.067 1.00 33.58 C ANISOU 1897 CA VAL B 291 3980 3883 4897 110 -463 260 C ATOM 1898 C VAL B 291 10.895 4.791 -30.955 1.00 31.28 C ANISOU 1898 C VAL B 291 3925 3255 4704 109 -314 -12 C ATOM 1899 O VAL B 291 11.002 4.748 -32.174 1.00 30.62 O ANISOU 1899 O VAL B 291 3812 3087 4736 51 -207 -157 O ATOM 1900 CB VAL B 291 12.399 3.310 -29.580 1.00 32.99 C ANISOU 1900 CB VAL B 291 3673 3791 5072 437 -293 584 C ATOM 1901 CG1 VAL B 291 12.342 2.328 -30.731 1.00 31.37 C ANISOU 1901 CG1 VAL B 291 3434 3255 5231 604 54 491 C ATOM 1902 CG2 VAL B 291 13.750 3.237 -28.888 1.00 34.80 C ANISOU 1902 CG2 VAL B 291 3530 4484 5210 476 -446 969 C ATOM 1903 N ARG B 292 9.724 4.881 -30.326 1.00 30.05 N ANISOU 1903 N ARG B 292 3969 2983 4466 143 -309 -57 N ATOM 1904 CA ARG B 292 8.453 4.980 -31.034 1.00 27.65 C ANISOU 1904 CA ARG B 292 3811 2499 4196 130 -201 -235 C ATOM 1905 C ARG B 292 8.375 6.299 -31.813 1.00 26.98 C ANISOU 1905 C ARG B 292 3842 2428 3980 -23 -289 -365 C ATOM 1906 O ARG B 292 7.816 6.371 -32.906 1.00 27.32 O ANISOU 1906 O ARG B 292 3872 2448 4061 -72 -223 -448 O ATOM 1907 CB ARG B 292 7.287 4.875 -30.049 1.00 24.35 C ANISOU 1907 CB ARG B 292 3529 2021 3700 220 -174 -202 C ATOM 1908 CG ARG B 292 5.927 4.772 -30.707 1.00 27.72 C ANISOU 1908 CG ARG B 292 3996 2379 4156 218 -55 -306 C ATOM 1909 CD ARG B 292 4.879 4.326 -29.712 1.00 28.46 C ANISOU 1909 CD ARG B 292 4155 2445 4215 315 19 -247 C ATOM 1910 NE ARG B 292 5.211 3.036 -29.110 1.00 29.74 N ANISOU 1910 NE ARG B 292 4261 2535 4504 385 122 -130 N ATOM 1911 CZ ARG B 292 4.661 2.572 -27.992 1.00 30.01 C ANISOU 1911 CZ ARG B 292 4354 2556 4492 464 167 -18 C ATOM 1912 NH1 ARG B 292 3.749 3.293 -27.343 1.00 34.53 N ANISOU 1912 NH1 ARG B 292 5039 3194 4888 471 130 -53 N ATOM 1913 NH2 ARG B 292 5.031 1.392 -27.515 1.00 30.50 N ANISOU 1913 NH2 ARG B 292 4369 2522 4696 557 291 156 N ATOM 1914 N LEU B 293 8.949 7.342 -31.234 1.00 24.96 N ANISOU 1914 N LEU B 293 3708 2233 3543 -139 -418 -363 N ATOM 1915 CA LEU B 293 8.985 8.631 -31.901 1.00 25.62 C ANISOU 1915 CA LEU B 293 3960 2249 3524 -283 -440 -455 C ATOM 1916 C LEU B 293 9.859 8.527 -33.146 1.00 29.84 C ANISOU 1916 C LEU B 293 4321 2879 4136 -402 -459 -487 C ATOM 1917 O LEU B 293 9.469 8.962 -34.225 1.00 29.69 O ANISOU 1917 O LEU B 293 4335 2817 4128 -445 -420 -523 O ATOM 1918 CB LEU B 293 9.505 9.726 -30.965 1.00 23.27 C ANISOU 1918 CB LEU B 293 3900 1951 2989 -483 -498 -504 C ATOM 1919 CG LEU B 293 9.722 11.079 -31.649 1.00 26.56 C ANISOU 1919 CG LEU B 293 4552 2218 3320 -664 -453 -593 C ATOM 1920 CD1 LEU B 293 8.412 11.637 -32.168 1.00 25.50 C ANISOU 1920 CD1 LEU B 293 4585 1826 3279 -443 -289 -548 C ATOM 1921 CD2 LEU B 293 10.398 12.066 -30.697 1.00 26.21 C ANISOU 1921 CD2 LEU B 293 4789 2171 3001 -997 -453 -709 C ATOM 1922 N VAL B 294 11.032 7.921 -32.997 1.00 30.55 N ANISOU 1922 N VAL B 294 4192 3143 4274 -442 -503 -431 N ATOM 1923 CA VAL B 294 11.978 7.858 -34.104 1.00 30.74 C ANISOU 1923 CA VAL B 294 4039 3275 4367 -558 -482 -469 C ATOM 1924 C VAL B 294 11.534 6.889 -35.206 1.00 31.29 C ANISOU 1924 C VAL B 294 4003 3258 4628 -481 -288 -548 C ATOM 1925 O VAL B 294 11.390 7.296 -36.361 1.00 33.16 O ANISOU 1925 O VAL B 294 4269 3510 4819 -633 -258 -650 O ATOM 1926 CB VAL B 294 13.384 7.465 -33.613 1.00 31.48 C ANISOU 1926 CB VAL B 294 3852 3640 4470 -579 -545 -325 C ATOM 1927 CG1 VAL B 294 14.350 7.385 -34.776 1.00 30.87 C ANISOU 1927 CG1 VAL B 294 3570 3680 4481 -677 -472 -367 C ATOM 1928 CG2 VAL B 294 13.881 8.479 -32.602 1.00 31.45 C ANISOU 1928 CG2 VAL B 294 3951 3832 4167 -825 -742 -291 C ATOM 1929 N LEU B 295 11.312 5.623 -34.852 1.00 24.81 N ANISOU 1929 N LEU B 295 3085 2352 3990 -294 -129 -503 N ATOM 1930 CA LEU B 295 10.995 4.605 -35.852 1.00 23.58 C ANISOU 1930 CA LEU B 295 2885 2083 3993 -317 144 -642 C ATOM 1931 C LEU B 295 9.597 4.805 -36.437 1.00 26.53 C ANISOU 1931 C LEU B 295 3394 2449 4236 -458 150 -765 C ATOM 1932 O LEU B 295 9.349 4.520 -37.607 1.00 25.83 O ANISOU 1932 O LEU B 295 3285 2419 4111 -671 288 -923 O ATOM 1933 CB LEU B 295 11.103 3.191 -35.252 1.00 26.73 C ANISOU 1933 CB LEU B 295 3211 2302 4642 -86 397 -548 C ATOM 1934 CG LEU B 295 12.446 2.712 -34.693 1.00 31.80 C ANISOU 1934 CG LEU B 295 3612 3007 5464 147 458 -298 C ATOM 1935 CD1 LEU B 295 12.352 1.246 -34.258 1.00 30.21 C ANISOU 1935 CD1 LEU B 295 3388 2530 5561 425 811 -159 C ATOM 1936 CD2 LEU B 295 13.568 2.902 -35.705 1.00 36.38 C ANISOU 1936 CD2 LEU B 295 4017 3708 6098 54 546 -364 C ATOM 1937 N GLY B 296 8.684 5.295 -35.607 1.00 24.88 N ANISOU 1937 N GLY B 296 3296 2228 3928 -359 13 -672 N ATOM 1938 CA GLY B 296 7.295 5.424 -35.994 1.00 27.60 C ANISOU 1938 CA GLY B 296 3680 2648 4159 -427 23 -692 C ATOM 1939 C GLY B 296 6.905 6.757 -36.604 1.00 27.37 C ANISOU 1939 C GLY B 296 3687 2755 3958 -484 -124 -606 C ATOM 1940 O GLY B 296 5.835 6.871 -37.200 1.00 26.23 O ANISOU 1940 O GLY B 296 3471 2794 3700 -549 -118 -546 O ATOM 1941 N PHE B 297 7.759 7.768 -36.456 1.00 23.00 N ANISOU 1941 N PHE B 297 3230 2137 3371 -474 -236 -562 N ATOM 1942 CA PHE B 297 7.415 9.108 -36.939 1.00 24.95 C ANISOU 1942 CA PHE B 297 3583 2402 3496 -483 -304 -435 C ATOM 1943 C PHE B 297 8.580 9.836 -37.613 1.00 24.60 C ANISOU 1943 C PHE B 297 3581 2364 3400 -670 -357 -467 C ATOM 1944 O PHE B 297 8.513 10.143 -38.805 1.00 29.09 O ANISOU 1944 O PHE B 297 4082 3086 3886 -814 -360 -419 O ATOM 1945 CB PHE B 297 6.870 9.975 -35.796 1.00 25.61 C ANISOU 1945 CB PHE B 297 3890 2280 3562 -273 -297 -331 C ATOM 1946 CG PHE B 297 6.114 11.191 -36.275 1.00 26.41 C ANISOU 1946 CG PHE B 297 4097 2329 3608 -158 -244 -121 C ATOM 1947 CD1 PHE B 297 4.747 11.124 -36.487 1.00 26.25 C ANISOU 1947 CD1 PHE B 297 3930 2461 3581 30 -190 83 C ATOM 1948 CD2 PHE B 297 6.771 12.381 -36.549 1.00 26.08 C ANISOU 1948 CD2 PHE B 297 4276 2110 3524 -237 -221 -79 C ATOM 1949 CE1 PHE B 297 4.040 12.217 -36.948 1.00 31.06 C ANISOU 1949 CE1 PHE B 297 4568 3059 4173 223 -108 393 C ATOM 1950 CE2 PHE B 297 6.065 13.490 -37.018 1.00 32.09 C ANISOU 1950 CE2 PHE B 297 5150 2760 4283 -64 -103 193 C ATOM 1951 CZ PHE B 297 4.695 13.406 -37.213 1.00 30.79 C ANISOU 1951 CZ PHE B 297 4794 2761 4143 209 -44 464 C ATOM 1952 N LEU B 298 9.642 10.104 -36.862 1.00 25.20 N ANISOU 1952 N LEU B 298 3237 3831 2505 -670 370 -83 N ATOM 1953 CA LEU B 298 10.697 10.995 -37.336 1.00 32.14 C ANISOU 1953 CA LEU B 298 4150 4538 3523 -594 186 -190 C ATOM 1954 C LEU B 298 11.509 10.429 -38.507 1.00 32.33 C ANISOU 1954 C LEU B 298 4139 4313 3831 -628 158 -73 C ATOM 1955 O LEU B 298 11.720 11.117 -39.508 1.00 25.41 O ANISOU 1955 O LEU B 298 3225 3321 3110 -583 125 -164 O ATOM 1956 CB LEU B 298 11.641 11.364 -36.181 1.00 27.63 C ANISOU 1956 CB LEU B 298 3681 4031 2787 -560 4 -182 C ATOM 1957 CG LEU B 298 11.139 12.399 -35.162 1.00 30.93 C ANISOU 1957 CG LEU B 298 4159 4672 2921 -463 -35 -431 C ATOM 1958 CD1 LEU B 298 12.279 12.898 -34.265 1.00 31.97 C ANISOU 1958 CD1 LEU B 298 4403 4796 2949 -422 -308 -472 C ATOM 1959 CD2 LEU B 298 10.433 13.569 -35.849 1.00 29.93 C ANISOU 1959 CD2 LEU B 298 3951 4485 2936 -367 -19 -707 C ATOM 1960 N TRP B 299 11.984 9.195 -38.377 1.00 22.57 N ANISOU 1960 N TRP B 299 2910 3002 2666 -697 173 134 N ATOM 1961 CA TRP B 299 12.749 8.562 -39.450 1.00 22.58 C ANISOU 1961 CA TRP B 299 2867 2779 2933 -698 176 199 C ATOM 1962 C TRP B 299 11.912 8.332 -40.731 1.00 26.85 C ANISOU 1962 C TRP B 299 3366 3271 3565 -704 299 88 C ATOM 1963 O TRP B 299 12.415 8.548 -41.836 1.00 29.12 O ANISOU 1963 O TRP B 299 3635 3457 3973 -656 308 28 O ATOM 1964 CB TRP B 299 13.366 7.241 -38.958 1.00 23.62 C ANISOU 1964 CB TRP B 299 2996 2805 3174 -756 142 425 C ATOM 1965 CG TRP B 299 14.076 6.454 -40.020 1.00 26.72 C ANISOU 1965 CG TRP B 299 3328 2965 3860 -729 171 442 C ATOM 1966 CD1 TRP B 299 13.686 5.258 -40.551 1.00 30.63 C ANISOU 1966 CD1 TRP B 299 3791 3325 4520 -767 241 463 C ATOM 1967 CD2 TRP B 299 15.297 6.806 -40.681 1.00 26.68 C ANISOU 1967 CD2 TRP B 299 3269 2836 4033 -646 138 419 C ATOM 1968 NE1 TRP B 299 14.590 4.840 -41.494 1.00 30.75 N ANISOU 1968 NE1 TRP B 299 3757 3154 4772 -688 262 408 N ATOM 1969 CE2 TRP B 299 15.590 5.771 -41.594 1.00 30.05 C ANISOU 1969 CE2 TRP B 299 3641 3089 4686 -614 226 399 C ATOM 1970 CE3 TRP B 299 16.175 7.890 -40.586 1.00 30.17 C ANISOU 1970 CE3 TRP B 299 3682 3288 4495 -595 41 413 C ATOM 1971 CZ2 TRP B 299 16.721 5.792 -42.409 1.00 28.86 C ANISOU 1971 CZ2 TRP B 299 3405 2826 4733 -518 270 373 C ATOM 1972 CZ3 TRP B 299 17.300 7.907 -41.397 1.00 30.41 C ANISOU 1972 CZ3 TRP B 299 3606 3185 4764 -529 70 441 C ATOM 1973 CH2 TRP B 299 17.559 6.866 -42.297 1.00 26.23 C ANISOU 1973 CH2 TRP B 299 3021 2535 4412 -483 209 420 C ATOM 1974 N PRO B 300 10.640 7.908 -40.599 1.00 26.29 N ANISOU 1974 N PRO B 300 3271 3287 3429 -767 387 72 N ATOM 1975 CA PRO B 300 9.820 7.866 -41.823 1.00 24.46 C ANISOU 1975 CA PRO B 300 3003 3010 3282 -769 439 -60 C ATOM 1976 C PRO B 300 9.544 9.249 -42.420 1.00 23.14 C ANISOU 1976 C PRO B 300 2829 2907 3058 -696 407 -216 C ATOM 1977 O PRO B 300 9.461 9.382 -43.639 1.00 26.68 O ANISOU 1977 O PRO B 300 3278 3297 3564 -675 399 -289 O ATOM 1978 CB PRO B 300 8.509 7.238 -41.352 1.00 27.40 C ANISOU 1978 CB PRO B 300 3309 3464 3639 -863 515 -14 C ATOM 1979 CG PRO B 300 8.834 6.546 -40.093 1.00 30.49 C ANISOU 1979 CG PRO B 300 3711 3903 3972 -926 527 201 C ATOM 1980 CD PRO B 300 9.939 7.301 -39.452 1.00 25.67 C ANISOU 1980 CD PRO B 300 3181 3343 3231 -850 442 209 C ATOM 1981 N LEU B 301 9.377 10.253 -41.565 1.00 26.88 N ANISOU 1981 N LEU B 301 3298 3499 3416 -654 372 -268 N ATOM 1982 CA LEU B 301 9.114 11.608 -42.031 1.00 27.69 C ANISOU 1982 CA LEU B 301 3373 3611 3536 -582 302 -406 C ATOM 1983 C LEU B 301 10.281 12.096 -42.880 1.00 27.82 C ANISOU 1983 C LEU B 301 3410 3500 3661 -547 220 -355 C ATOM 1984 O LEU B 301 10.089 12.578 -43.987 1.00 27.32 O ANISOU 1984 O LEU B 301 3325 3402 3654 -532 199 -375 O ATOM 1985 CB LEU B 301 8.871 12.560 -40.851 1.00 26.40 C ANISOU 1985 CB LEU B 301 3204 3565 3260 -518 258 -519 C ATOM 1986 CG LEU B 301 8.485 13.991 -41.232 1.00 28.38 C ANISOU 1986 CG LEU B 301 3400 3778 3606 -431 153 -683 C ATOM 1987 CD1 LEU B 301 7.346 13.971 -42.230 1.00 28.25 C ANISOU 1987 CD1 LEU B 301 3300 3756 3679 -447 196 -717 C ATOM 1988 CD2 LEU B 301 8.105 14.804 -39.999 1.00 27.90 C ANISOU 1988 CD2 LEU B 301 3331 3836 3433 -340 124 -874 C ATOM 1989 N LEU B 302 11.489 11.930 -42.354 1.00 25.48 N ANISOU 1989 N LEU B 302 3139 3146 3395 -542 174 -258 N ATOM 1990 CA LEU B 302 12.698 12.328 -43.049 1.00 23.17 C ANISOU 1990 CA LEU B 302 2818 2741 3244 -516 125 -168 C ATOM 1991 C LEU B 302 12.822 11.621 -44.400 1.00 27.19 C ANISOU 1991 C LEU B 302 3323 3221 3787 -520 249 -130 C ATOM 1992 O LEU B 302 12.973 12.268 -45.442 1.00 23.54 O ANISOU 1992 O LEU B 302 2834 2760 3349 -499 255 -105 O ATOM 1993 CB LEU B 302 13.924 12.033 -42.181 1.00 24.30 C ANISOU 1993 CB LEU B 302 2959 2819 3453 -517 48 -59 C ATOM 1994 CG LEU B 302 15.292 12.432 -42.739 1.00 29.94 C ANISOU 1994 CG LEU B 302 3588 3412 4376 -495 1 67 C ATOM 1995 CD1 LEU B 302 15.364 13.944 -42.962 1.00 24.95 C ANISOU 1995 CD1 LEU B 302 2902 2739 3841 -478 -133 46 C ATOM 1996 CD2 LEU B 302 16.421 11.961 -41.819 1.00 34.74 C ANISOU 1996 CD2 LEU B 302 4172 3942 5087 -501 -103 181 C ATOM 1997 N THR B 303 12.739 10.293 -44.374 1.00 24.08 N ANISOU 1997 N THR B 303 2956 2802 3389 -546 336 -127 N ATOM 1998 CA THR B 303 13.040 9.481 -45.552 1.00 26.98 C ANISOU 1998 CA THR B 303 3332 3123 3795 -521 441 -150 C ATOM 1999 C THR B 303 11.987 9.603 -46.662 1.00 25.75 C ANISOU 1999 C THR B 303 3217 3041 3527 -527 461 -270 C ATOM 2000 O THR B 303 12.337 9.721 -47.835 1.00 23.80 O ANISOU 2000 O THR B 303 2987 2832 3224 -483 518 -286 O ATOM 2001 CB THR B 303 13.217 7.987 -45.169 1.00 29.66 C ANISOU 2001 CB THR B 303 3678 3353 4236 -540 480 -137 C ATOM 2002 OG1 THR B 303 12.070 7.532 -44.444 1.00 27.84 O ANISOU 2002 OG1 THR B 303 3467 3149 3963 -621 450 -149 O ATOM 2003 CG2 THR B 303 14.461 7.806 -44.298 1.00 28.73 C ANISOU 2003 CG2 THR B 303 3511 3149 4256 -523 435 11 C ATOM 2004 N LEU B 304 10.707 9.577 -46.303 1.00 25.96 N ANISOU 2004 N LEU B 304 3247 3107 3511 -580 414 -341 N ATOM 2005 CA LEU B 304 9.646 9.749 -47.297 1.00 26.39 C ANISOU 2005 CA LEU B 304 3318 3215 3493 -594 376 -444 C ATOM 2006 C LEU B 304 9.565 11.176 -47.868 1.00 26.73 C ANISOU 2006 C LEU B 304 3345 3328 3484 -561 302 -407 C ATOM 2007 O LEU B 304 9.209 11.347 -49.030 1.00 28.56 O ANISOU 2007 O LEU B 304 3613 3614 3625 -555 267 -433 O ATOM 2008 CB LEU B 304 8.297 9.361 -46.706 1.00 24.42 C ANISOU 2008 CB LEU B 304 3020 2976 3282 -664 345 -502 C ATOM 2009 CG LEU B 304 8.164 7.882 -46.328 1.00 28.63 C ANISOU 2009 CG LEU B 304 3549 3410 3917 -727 386 -497 C ATOM 2010 CD1 LEU B 304 6.774 7.591 -45.772 1.00 29.07 C ANISOU 2010 CD1 LEU B 304 3509 3496 4040 -816 372 -498 C ATOM 2011 CD2 LEU B 304 8.471 6.974 -47.524 1.00 26.98 C ANISOU 2011 CD2 LEU B 304 3411 3104 3736 -703 377 -611 C ATOM 2012 N THR B 305 9.889 12.191 -47.063 1.00 23.36 N ANISOU 2012 N THR B 305 2865 2890 3120 -542 248 -344 N ATOM 2013 CA THR B 305 9.880 13.564 -47.567 1.00 27.45 C ANISOU 2013 CA THR B 305 3343 3412 3674 -517 142 -282 C ATOM 2014 C THR B 305 11.007 13.732 -48.584 1.00 27.78 C ANISOU 2014 C THR B 305 3398 3468 3688 -501 195 -129 C ATOM 2015 O THR B 305 10.841 14.424 -49.582 1.00 29.89 O ANISOU 2015 O THR B 305 3663 3786 3910 -503 143 -38 O ATOM 2016 CB THR B 305 10.017 14.620 -46.432 1.00 21.44 C ANISOU 2016 CB THR B 305 2518 2591 3038 -488 36 -296 C ATOM 2017 OG1 THR B 305 8.910 14.503 -45.534 1.00 24.97 O ANISOU 2017 OG1 THR B 305 2940 3085 3463 -481 36 -448 O ATOM 2018 CG2 THR B 305 10.022 16.052 -47.001 1.00 23.14 C ANISOU 2018 CG2 THR B 305 2668 2742 3382 -466 -117 -216 C ATOM 2019 N ILE B 306 12.148 13.091 -48.333 1.00 28.85 N ANISOU 2019 N ILE B 306 3531 3573 3858 -485 305 -77 N ATOM 2020 CA ILE B 306 13.248 13.081 -49.298 1.00 30.71 C ANISOU 2020 CA ILE B 306 3744 3855 4069 -456 423 61 C ATOM 2021 C ILE B 306 12.799 12.398 -50.584 1.00 33.48 C ANISOU 2021 C ILE B 306 4192 4335 4194 -435 517 -27 C ATOM 2022 O ILE B 306 13.028 12.907 -51.691 1.00 33.17 O ANISOU 2022 O ILE B 306 4161 4424 4019 -422 561 91 O ATOM 2023 CB ILE B 306 14.501 12.346 -48.766 1.00 32.33 C ANISOU 2023 CB ILE B 306 3897 3987 4401 -424 529 102 C ATOM 2024 CG1 ILE B 306 15.134 13.105 -47.596 1.00 28.55 C ANISOU 2024 CG1 ILE B 306 3328 3390 4130 -446 392 202 C ATOM 2025 CG2 ILE B 306 15.534 12.150 -49.893 1.00 30.13 C ANISOU 2025 CG2 ILE B 306 3569 3796 4082 -369 719 207 C ATOM 2026 CD1 ILE B 306 16.279 12.366 -46.924 1.00 25.92 C ANISOU 2026 CD1 ILE B 306 2933 2966 3949 -424 432 256 C ATOM 2027 N CYS B 307 12.162 11.241 -50.418 1.00 27.01 N ANISOU 2027 N CYS B 307 3444 3485 3334 -436 533 -224 N ATOM 2028 CA CYS B 307 11.681 10.429 -51.529 1.00 27.18 C ANISOU 2028 CA CYS B 307 3572 3590 3165 -411 571 -383 C ATOM 2029 C CYS B 307 10.769 11.202 -52.473 1.00 26.23 C ANISOU 2029 C CYS B 307 3505 3597 2863 -439 446 -361 C ATOM 2030 O CYS B 307 10.944 11.160 -53.691 1.00 28.10 O ANISOU 2030 O CYS B 307 3825 3993 2858 -400 497 -365 O ATOM 2031 CB CYS B 307 10.939 9.193 -50.998 1.00 27.42 C ANISOU 2031 CB CYS B 307 3634 3497 3286 -442 528 -576 C ATOM 2032 SG CYS B 307 10.274 8.081 -52.281 1.00 36.17 S ANISOU 2032 SG CYS B 307 4875 4638 4229 -415 495 -846 S ATOM 2033 N TYR B 308 9.797 11.912 -51.907 1.00 25.73 N ANISOU 2033 N TYR B 308 3389 3479 2909 -495 281 -336 N ATOM 2034 CA TYR B 308 8.804 12.588 -52.726 1.00 27.77 C ANISOU 2034 CA TYR B 308 3672 3817 3063 -522 114 -311 C ATOM 2035 C TYR B 308 9.252 13.979 -53.165 1.00 30.11 C ANISOU 2035 C TYR B 308 3916 4167 3355 -523 60 -50 C ATOM 2036 O TYR B 308 8.725 14.513 -54.138 1.00 31.32 O ANISOU 2036 O TYR B 308 4109 4421 3371 -540 -67 41 O ATOM 2037 CB TYR B 308 7.468 12.622 -51.988 1.00 27.98 C ANISOU 2037 CB TYR B 308 3624 3749 3258 -568 -31 -421 C ATOM 2038 CG TYR B 308 6.861 11.235 -51.959 1.00 31.18 C ANISOU 2038 CG TYR B 308 4073 4113 3662 -598 -21 -625 C ATOM 2039 CD1 TYR B 308 6.933 10.435 -50.818 1.00 29.96 C ANISOU 2039 CD1 TYR B 308 3865 3851 3666 -621 73 -681 C ATOM 2040 CD2 TYR B 308 6.271 10.701 -53.094 1.00 33.41 C ANISOU 2040 CD2 TYR B 308 4451 4455 3788 -609 -130 -747 C ATOM 2041 CE1 TYR B 308 6.400 9.152 -50.806 1.00 29.95 C ANISOU 2041 CE1 TYR B 308 3879 3770 3732 -667 59 -822 C ATOM 2042 CE2 TYR B 308 5.733 9.424 -53.091 1.00 38.35 C ANISOU 2042 CE2 TYR B 308 5102 4991 4480 -644 -166 -946 C ATOM 2043 CZ TYR B 308 5.804 8.656 -51.948 1.00 36.68 C ANISOU 2043 CZ TYR B 308 4810 4639 4488 -678 -68 -967 C ATOM 2044 OH TYR B 308 5.271 7.394 -51.959 1.00 41.75 O ANISOU 2044 OH TYR B 308 5452 5152 5260 -731 -129 -1122 O ATOM 2045 N THR B 309 10.248 14.547 -52.491 1.00 29.87 N ANISOU 2045 N THR B 309 3794 4059 3494 -513 128 93 N ATOM 2046 CA THR B 309 10.896 15.739 -53.020 1.00 32.16 C ANISOU 2046 CA THR B 309 4016 4379 3824 -528 92 385 C ATOM 2047 C THR B 309 11.556 15.387 -54.368 1.00 33.21 C ANISOU 2047 C THR B 309 4229 4743 3646 -508 260 506 C ATOM 2048 O THR B 309 11.349 16.076 -55.369 1.00 34.71 O ANISOU 2048 O THR B 309 4442 5066 3680 -536 186 712 O ATOM 2049 CB THR B 309 11.939 16.316 -52.031 1.00 29.96 C ANISOU 2049 CB THR B 309 3607 3948 3830 -528 109 500 C ATOM 2050 OG1 THR B 309 11.268 16.797 -50.856 1.00 29.24 O ANISOU 2050 OG1 THR B 309 3462 3688 3960 -528 -59 364 O ATOM 2051 CG2 THR B 309 12.723 17.467 -52.670 1.00 28.82 C ANISOU 2051 CG2 THR B 309 3357 3810 3782 -565 77 850 C ATOM 2052 N PHE B 310 12.329 14.304 -54.382 1.00 30.89 N ANISOU 2052 N PHE B 310 3974 4505 3258 -450 486 378 N ATOM 2053 CA PHE B 310 12.907 13.765 -55.608 1.00 32.50 C ANISOU 2053 CA PHE B 310 4263 4956 3130 -390 692 389 C ATOM 2054 C PHE B 310 11.840 13.552 -56.688 1.00 32.68 C ANISOU 2054 C PHE B 310 4459 5153 2804 -393 570 272 C ATOM 2055 O PHE B 310 11.986 14.018 -57.812 1.00 34.40 O ANISOU 2055 O PHE B 310 4734 5613 2722 -392 604 460 O ATOM 2056 CB PHE B 310 13.624 12.440 -55.325 1.00 33.23 C ANISOU 2056 CB PHE B 310 4369 5015 3242 -301 907 152 C ATOM 2057 CG PHE B 310 15.104 12.578 -55.047 1.00 33.29 C ANISOU 2057 CG PHE B 310 4213 5009 3429 -262 1120 338 C ATOM 2058 CD1 PHE B 310 15.559 13.032 -53.818 1.00 30.98 C ANISOU 2058 CD1 PHE B 310 3773 4490 3510 -309 1034 454 C ATOM 2059 CD2 PHE B 310 16.040 12.228 -56.007 1.00 35.36 C ANISOU 2059 CD2 PHE B 310 4457 5494 3485 -169 1405 378 C ATOM 2060 CE1 PHE B 310 16.921 13.148 -53.556 1.00 33.72 C ANISOU 2060 CE1 PHE B 310 3943 4800 4070 -283 1186 632 C ATOM 2061 CE2 PHE B 310 17.401 12.341 -55.750 1.00 34.87 C ANISOU 2061 CE2 PHE B 310 4191 5410 3646 -132 1608 565 C ATOM 2062 CZ PHE B 310 17.839 12.799 -54.519 1.00 36.56 C ANISOU 2062 CZ PHE B 310 4247 5363 4283 -198 1477 702 C ATOM 2063 N ILE B 311 10.762 12.861 -56.330 1.00 32.29 N ANISOU 2063 N ILE B 311 4482 4985 2801 -406 413 -12 N ATOM 2064 CA ILE B 311 9.734 12.472 -57.293 1.00 33.06 C ANISOU 2064 CA ILE B 311 4738 5209 2613 -410 253 -177 C ATOM 2065 C ILE B 311 8.925 13.664 -57.819 1.00 33.23 C ANISOU 2065 C ILE B 311 4750 5297 2579 -482 1 63 C ATOM 2066 O ILE B 311 8.648 13.757 -59.019 1.00 35.91 O ANISOU 2066 O ILE B 311 5224 5866 2554 -479 -80 112 O ATOM 2067 CB ILE B 311 8.764 11.430 -56.675 1.00 33.64 C ANISOU 2067 CB ILE B 311 4834 5090 2859 -429 124 -506 C ATOM 2068 CG1 ILE B 311 9.505 10.116 -56.392 1.00 34.15 C ANISOU 2068 CG1 ILE B 311 4928 5080 2966 -355 327 -744 C ATOM 2069 CG2 ILE B 311 7.560 11.179 -57.594 1.00 33.15 C ANISOU 2069 CG2 ILE B 311 4897 5110 2589 -458 -129 -660 C ATOM 2070 CD1 ILE B 311 8.647 9.042 -55.756 1.00 30.17 C ANISOU 2070 CD1 ILE B 311 4420 4357 2687 -395 203 -1003 C ATOM 2071 N LEU B 312 8.539 14.568 -56.926 1.00 32.96 N ANISOU 2071 N LEU B 312 4560 5060 2903 -537 -140 200 N ATOM 2072 CA LEU B 312 7.686 15.688 -57.320 1.00 34.42 C ANISOU 2072 CA LEU B 312 4700 5236 3144 -592 -417 407 C ATOM 2073 C LEU B 312 8.428 16.726 -58.158 1.00 35.51 C ANISOU 2073 C LEU B 312 4825 5529 3138 -617 -397 817 C ATOM 2074 O LEU B 312 7.875 17.268 -59.117 1.00 38.48 O ANISOU 2074 O LEU B 312 5259 6038 3325 -655 -596 1006 O ATOM 2075 CB LEU B 312 7.071 16.352 -56.088 1.00 33.34 C ANISOU 2075 CB LEU B 312 4383 4825 3461 -612 -558 383 C ATOM 2076 CG LEU B 312 5.968 15.503 -55.449 1.00 34.26 C ANISOU 2076 CG LEU B 312 4482 4833 3702 -613 -628 62 C ATOM 2077 CD1 LEU B 312 5.293 16.238 -54.302 1.00 36.82 C ANISOU 2077 CD1 LEU B 312 4619 4953 4420 -609 -734 32 C ATOM 2078 CD2 LEU B 312 4.954 15.095 -56.502 1.00 36.54 C ANISOU 2078 CD2 LEU B 312 4871 5230 3782 -641 -834 -24 C ATOM 2079 N LEU B 313 9.677 17.002 -57.801 1.00 35.15 N ANISOU 2079 N LEU B 313 4685 5466 3202 -606 -176 988 N ATOM 2080 CA LEU B 313 10.472 17.945 -58.570 1.00 42.12 C ANISOU 2080 CA LEU B 313 5513 6496 3993 -648 -123 1430 C ATOM 2081 C LEU B 313 10.771 17.377 -59.951 1.00 40.18 C ANISOU 2081 C LEU B 313 5447 6649 3170 -615 47 1476 C ATOM 2082 O LEU B 313 10.827 18.111 -60.931 1.00 43.53 O ANISOU 2082 O LEU B 313 5894 7283 3362 -666 -9 1844 O ATOM 2083 CB LEU B 313 11.765 18.293 -57.833 1.00 41.62 C ANISOU 2083 CB LEU B 313 5274 6305 4234 -651 68 1592 C ATOM 2084 CG LEU B 313 11.541 19.196 -56.615 1.00 43.36 C ANISOU 2084 CG LEU B 313 5322 6159 4992 -687 -156 1610 C ATOM 2085 CD1 LEU B 313 12.841 19.437 -55.863 1.00 38.60 C ANISOU 2085 CD1 LEU B 313 4559 5420 4686 -692 -13 1727 C ATOM 2086 CD2 LEU B 313 10.909 20.521 -57.050 1.00 47.14 C ANISOU 2086 CD2 LEU B 313 5724 6544 5642 -757 -464 1923 C ATOM 2087 N ARG B 314 10.951 16.064 -60.027 1.00 39.90 N ANISOU 2087 N ARG B 314 5542 6720 2897 -523 246 1099 N ATOM 2088 CA ARG B 314 11.132 15.420 -61.320 1.00 47.25 C ANISOU 2088 CA ARG B 314 6673 8037 3243 -456 395 1023 C ATOM 2089 C ARG B 314 9.873 15.576 -62.168 1.00 46.35 C ANISOU 2089 C ARG B 314 6730 8047 2836 -499 58 1002 C ATOM 2090 O ARG B 314 9.941 15.982 -63.325 1.00 49.93 O ANISOU 2090 O ARG B 314 7294 8833 2845 -514 47 1257 O ATOM 2091 CB ARG B 314 11.480 13.943 -61.143 1.00 47.85 C ANISOU 2091 CB ARG B 314 6841 8118 3221 -333 617 550 C ATOM 2092 CG ARG B 314 11.501 13.154 -62.437 1.00 47.44 C ANISOU 2092 CG ARG B 314 7025 8436 2562 -231 727 328 C ATOM 2093 CD ARG B 314 12.534 13.687 -63.399 1.00 51.53 C ANISOU 2093 CD ARG B 314 7533 9356 2689 -196 1027 680 C ATOM 2094 NE ARG B 314 12.557 12.909 -64.632 1.00 59.19 N ANISOU 2094 NE ARG B 314 8759 10567 3164 -67 1124 395 N ATOM 2095 CZ ARG B 314 13.215 13.268 -65.729 1.00 67.18 C ANISOU 2095 CZ ARG B 314 9838 11824 3864 -35 1325 617 C ATOM 2096 NH1 ARG B 314 13.908 14.398 -65.747 1.00 71.39 N ANISOU 2096 NH1 ARG B 314 10175 12401 4547 -125 1444 1145 N ATOM 2097 NH2 ARG B 314 13.177 12.497 -66.806 1.00 69.47 N ANISOU 2097 NH2 ARG B 314 10387 12297 3711 74 1395 306 N ATOM 2098 N THR B 315 8.726 15.265 -61.573 1.00 45.80 N ANISOU 2098 N THR B 315 6662 7717 3023 -526 -220 726 N ATOM 2099 CA THR B 315 7.434 15.366 -62.246 1.00 48.64 C ANISOU 2099 CA THR B 315 7139 8129 3214 -572 -594 680 C ATOM 2100 C THR B 315 7.095 16.799 -62.675 1.00 51.10 C ANISOU 2100 C THR B 315 7369 8466 3580 -665 -844 1171 C ATOM 2101 O THR B 315 6.635 17.025 -63.793 1.00 55.25 O ANISOU 2101 O THR B 315 8042 9242 3707 -693 -1045 1323 O ATOM 2102 CB THR B 315 6.301 14.838 -61.335 1.00 46.79 C ANISOU 2102 CB THR B 315 6832 7566 3379 -593 -815 340 C ATOM 2103 OG1 THR B 315 6.665 13.559 -60.801 1.00 49.04 O ANISOU 2103 OG1 THR B 315 7154 7767 3710 -526 -599 -47 O ATOM 2104 CG2 THR B 315 4.993 14.718 -62.107 1.00 44.86 C ANISOU 2104 CG2 THR B 315 6698 7379 2969 -634 -1205 237 C ATOM 2105 N TRP B 316 7.327 17.761 -61.784 1.00 53.11 N ANISOU 2105 N TRP B 316 7392 8447 4339 -711 -859 1416 N ATOM 2106 CA TRP B 316 6.976 19.161 -62.033 1.00 56.91 C ANISOU 2106 CA TRP B 316 7750 8844 5029 -796 -1140 1869 C ATOM 2107 C TRP B 316 7.905 19.864 -63.014 1.00 61.64 C ANISOU 2107 C TRP B 316 8372 9734 5312 -845 -1016 2385 C ATOM 2108 O TRP B 316 7.587 20.945 -63.506 1.00 67.85 O ANISOU 2108 O TRP B 316 9094 10506 6180 -929 -1281 2821 O ATOM 2109 CB TRP B 316 6.968 19.948 -60.723 1.00 54.67 C ANISOU 2109 CB TRP B 316 7210 8147 5416 -808 -1207 1902 C ATOM 2110 CG TRP B 316 5.909 19.519 -59.773 1.00 53.51 C ANISOU 2110 CG TRP B 316 6998 7741 5593 -771 -1348 1494 C ATOM 2111 CD1 TRP B 316 4.769 18.832 -60.072 1.00 55.71 C ANISOU 2111 CD1 TRP B 316 7364 8056 5747 -765 -1535 1226 C ATOM 2112 CD2 TRP B 316 5.890 19.736 -58.359 1.00 50.68 C ANISOU 2112 CD2 TRP B 316 6458 7069 5730 -738 -1308 1316 C ATOM 2113 NE1 TRP B 316 4.037 18.613 -58.929 1.00 53.63 N ANISOU 2113 NE1 TRP B 316 6955 7526 5896 -737 -1580 931 N ATOM 2114 CE2 TRP B 316 4.704 19.160 -57.863 1.00 52.58 C ANISOU 2114 CE2 TRP B 316 6672 7199 6107 -712 -1431 971 C ATOM 2115 CE3 TRP B 316 6.762 20.367 -57.463 1.00 50.06 C ANISOU 2115 CE3 TRP B 316 6234 6801 5985 -729 -1193 1414 C ATOM 2116 CZ2 TRP B 316 4.366 19.193 -56.507 1.00 52.27 C ANISOU 2116 CZ2 TRP B 316 6474 6918 6467 -669 -1393 736 C ATOM 2117 CZ3 TRP B 316 6.425 20.400 -56.119 1.00 50.68 C ANISOU 2117 CZ3 TRP B 316 6187 6626 6443 -679 -1201 1138 C ATOM 2118 CH2 TRP B 316 5.237 19.815 -55.654 1.00 52.02 C ANISOU 2118 CH2 TRP B 316 6342 6741 6684 -645 -1277 809 C ATOM 2119 N SER B 317 9.059 19.269 -63.284 1.00 61.11 N ANISOU 2119 N SER B 317 8370 9926 4922 -793 -609 2365 N ATOM 2120 CA SER B 317 10.004 19.870 -64.216 1.00 65.09 C ANISOU 2120 CA SER B 317 8862 10718 5152 -823 -409 2832 C ATOM 2121 C SER B 317 9.809 19.312 -65.622 1.00 70.40 C ANISOU 2121 C SER B 317 9807 11761 5179 -743 -354 2702 C ATOM 2122 O SER B 317 10.433 19.774 -66.579 1.00 69.57 O ANISOU 2122 O SER B 317 9727 11857 4849 -737 -194 2992 O ATOM 2123 CB SER B 317 11.444 19.641 -63.749 1.00 65.43 C ANISOU 2123 CB SER B 317 8764 10766 5331 -778 29 2852 C ATOM 2124 OG SER B 317 11.735 18.259 -63.635 1.00 63.58 O ANISOU 2124 OG SER B 317 8667 10695 4797 -658 306 2386 O ATOM 2125 N ARG B 318 8.935 18.317 -65.735 1.00 74.56 N ANISOU 2125 N ARG B 318 10540 12358 5432 -687 -506 2251 N ATOM 2126 CA ARG B 318 8.676 17.663 -67.012 1.00 79.56 C ANISOU 2126 CA ARG B 318 11466 13289 5472 -588 -503 2034 C ATOM 2127 C ARG B 318 7.215 17.793 -67.429 1.00 80.42 C ANISOU 2127 C ARG B 318 11688 13344 5524 -628 -1007 1968 C ATOM 2128 O ARG B 318 6.360 18.195 -66.635 1.00 78.65 O ANISOU 2128 O ARG B 318 11307 12835 5743 -725 -1334 2000 O ATOM 2129 CB ARG B 318 9.084 16.189 -66.947 1.00 78.96 C ANISOU 2129 CB ARG B 318 11546 13311 5143 -446 -221 1469 C ATOM 2130 CG ARG B 318 10.582 15.981 -67.073 1.00 79.50 C ANISOU 2130 CG ARG B 318 11559 13516 5133 -363 297 1526 C ATOM 2131 CD ARG B 318 11.087 16.530 -68.402 1.00 87.10 C ANISOU 2131 CD ARG B 318 12635 14770 5690 -352 435 1851 C ATOM 2132 NE ARG B 318 12.388 17.181 -68.270 1.00 88.72 N ANISOU 2132 NE ARG B 318 12604 15001 6105 -387 790 2235 N ATOM 2133 CZ ARG B 318 13.552 16.544 -68.335 1.00 90.13 C ANISOU 2133 CZ ARG B 318 12747 15287 6210 -291 1230 2076 C ATOM 2134 NH1 ARG B 318 13.573 15.235 -68.533 1.00 93.31 N ANISOU 2134 NH1 ARG B 318 13347 15765 6341 -147 1374 1529 N ATOM 2135 NH2 ARG B 318 14.690 17.213 -68.201 1.00 88.59 N ANISOU 2135 NH2 ARG B 318 12298 15092 6271 -341 1500 2451 N ATOM 2136 N ARG B 319 6.939 17.452 -68.683 1.00 84.53 N ANISOU 2136 N ARG B 319 12478 14120 5520 -546 -1077 1867 N ATOM 2137 CA ARG B 319 5.614 17.642 -69.256 1.00 85.81 C ANISOU 2137 CA ARG B 319 12739 14253 5611 -567 -1569 1850 C ATOM 2138 C ARG B 319 4.809 16.346 -69.289 1.00 88.23 C ANISOU 2138 C ARG B 319 13224 14529 5770 -480 -1759 1237 C ATOM 2139 O ARG B 319 4.038 16.062 -68.368 1.00 86.47 O ANISOU 2139 O ARG B 319 12851 14031 5973 -545 -1980 1011 O ATOM 2140 CB ARG B 319 5.737 18.225 -70.662 1.00 90.05 C ANISOU 2140 CB ARG B 319 13458 15079 5677 -539 -1601 2185 C ATOM 2141 N SER B 323 0.990 9.909 -64.936 1.00 84.81 N ANISOU 2141 N SER B 323 12367 12484 7375 -623 -2424 -1558 N ATOM 2142 CA SER B 323 0.965 8.904 -63.880 1.00 82.58 C ANISOU 2142 CA SER B 323 11971 11850 7556 -652 -2300 -1833 C ATOM 2143 C SER B 323 0.530 9.504 -62.553 1.00 77.68 C ANISOU 2143 C SER B 323 11092 10936 7487 -731 -2326 -1623 C ATOM 2144 O SER B 323 0.435 8.793 -61.549 1.00 76.91 O ANISOU 2144 O SER B 323 10837 10568 7819 -758 -2203 -1769 O ATOM 2145 CB SER B 323 2.342 8.262 -63.710 1.00 85.26 C ANISOU 2145 CB SER B 323 12451 12245 7699 -537 -1885 -1998 C ATOM 2146 OG SER B 323 3.095 8.967 -62.734 1.00 84.63 O ANISOU 2146 OG SER B 323 12221 12115 7819 -515 -1587 -1714 O ATOM 2147 N THR B 324 0.267 10.810 -62.556 1.00 58.62 N ANISOU 2147 N THR B 324 8852 7345 6075 -1128 -885 748 N ATOM 2148 CA THR B 324 0.047 11.557 -61.319 1.00 58.19 C ANISOU 2148 CA THR B 324 8773 7160 6178 -1012 -936 808 C ATOM 2149 C THR B 324 -1.116 11.044 -60.477 1.00 55.90 C ANISOU 2149 C THR B 324 8273 6853 6113 -776 -1039 757 C ATOM 2150 O THR B 324 -1.137 11.262 -59.270 1.00 56.07 O ANISOU 2150 O THR B 324 8187 6816 6302 -684 -1018 759 O ATOM 2151 CB THR B 324 -0.191 13.051 -61.604 1.00 60.63 C ANISOU 2151 CB THR B 324 9420 7287 6330 -1027 -1082 962 C ATOM 2152 OG1 THR B 324 -1.326 13.202 -62.466 1.00 63.80 O ANISOU 2152 OG1 THR B 324 9955 7656 6628 -896 -1297 1006 O ATOM 2153 CG2 THR B 324 1.033 13.658 -62.260 1.00 63.76 C ANISOU 2153 CG2 THR B 324 10043 7689 6492 -1323 -951 1015 C ATOM 2154 N LYS B 325 -2.069 10.363 -61.110 1.00 53.77 N ANISOU 2154 N LYS B 325 7942 6656 5831 -705 -1142 702 N ATOM 2155 CA LYS B 325 -3.256 9.866 -60.411 1.00 54.47 C ANISOU 2155 CA LYS B 325 7822 6775 6101 -528 -1236 637 C ATOM 2156 C LYS B 325 -2.911 9.014 -59.185 1.00 52.25 C ANISOU 2156 C LYS B 325 7313 6508 6032 -511 -1074 551 C ATOM 2157 O LYS B 325 -3.252 9.369 -58.056 1.00 50.73 O ANISOU 2157 O LYS B 325 7029 6259 5988 -396 -1095 566 O ATOM 2158 CB LYS B 325 -4.134 9.061 -61.367 1.00 56.58 C ANISOU 2158 CB LYS B 325 8038 7167 6295 -534 -1330 557 C ATOM 2159 N THR B 326 -2.235 7.892 -59.412 1.00 49.91 N ANISOU 2159 N THR B 326 6949 6281 5733 -610 -915 460 N ATOM 2160 CA THR B 326 -1.807 7.023 -58.321 1.00 43.17 C ANISOU 2160 CA THR B 326 5934 5424 5047 -576 -766 385 C ATOM 2161 C THR B 326 -0.838 7.756 -57.392 1.00 40.25 C ANISOU 2161 C THR B 326 5557 5006 4729 -566 -684 446 C ATOM 2162 O THR B 326 -0.937 7.656 -56.170 1.00 41.26 O ANISOU 2162 O THR B 326 5570 5093 5014 -476 -653 437 O ATOM 2163 CB THR B 326 -1.141 5.740 -58.854 1.00 43.51 C ANISOU 2163 CB THR B 326 5963 5530 5038 -648 -619 274 C ATOM 2164 OG1 THR B 326 -2.057 5.043 -59.710 1.00 45.38 O ANISOU 2164 OG1 THR B 326 6222 5806 5213 -688 -693 206 O ATOM 2165 CG2 THR B 326 -0.731 4.831 -57.704 1.00 42.23 C ANISOU 2165 CG2 THR B 326 5683 5336 5028 -570 -485 206 C ATOM 2166 N LEU B 327 0.087 8.502 -57.990 1.00 39.09 N ANISOU 2166 N LEU B 327 5542 4878 4433 -685 -645 502 N ATOM 2167 CA LEU B 327 1.064 9.289 -57.242 1.00 37.15 C ANISOU 2167 CA LEU B 327 5303 4617 4197 -735 -567 549 C ATOM 2168 C LEU B 327 0.395 10.284 -56.291 1.00 37.43 C ANISOU 2168 C LEU B 327 5374 4515 4334 -634 -682 629 C ATOM 2169 O LEU B 327 0.804 10.427 -55.141 1.00 36.51 O ANISOU 2169 O LEU B 327 5164 4381 4329 -598 -620 623 O ATOM 2170 CB LEU B 327 1.994 10.028 -58.208 1.00 39.02 C ANISOU 2170 CB LEU B 327 5710 4903 4212 -940 -518 595 C ATOM 2171 CG LEU B 327 2.996 11.014 -57.604 1.00 40.77 C ANISOU 2171 CG LEU B 327 5975 5122 4391 -1069 -442 642 C ATOM 2172 CD1 LEU B 327 3.922 10.306 -56.618 1.00 41.01 C ANISOU 2172 CD1 LEU B 327 5754 5291 4538 -1030 -291 543 C ATOM 2173 CD2 LEU B 327 3.793 11.705 -58.704 1.00 39.61 C ANISOU 2173 CD2 LEU B 327 6027 5033 3988 -1327 -386 682 C ATOM 2174 N LYS B 328 -0.641 10.961 -56.772 1.00 35.81 N ANISOU 2174 N LYS B 328 5306 4222 4078 -566 -856 695 N ATOM 2175 CA LYS B 328 -1.346 11.944 -55.964 1.00 35.32 C ANISOU 2175 CA LYS B 328 5299 4029 4092 -427 -978 757 C ATOM 2176 C LYS B 328 -2.066 11.271 -54.797 1.00 34.37 C ANISOU 2176 C LYS B 328 4937 3938 4186 -272 -970 683 C ATOM 2177 O LYS B 328 -2.173 11.844 -53.708 1.00 34.73 O ANISOU 2177 O LYS B 328 4958 3908 4330 -186 -978 701 O ATOM 2178 CB LYS B 328 -2.338 12.739 -56.822 1.00 32.97 C ANISOU 2178 CB LYS B 328 5201 3655 3672 -333 -1186 830 C ATOM 2179 N VAL B 329 -2.557 10.055 -55.034 1.00 32.83 N ANISOU 2179 N VAL B 329 4586 3846 4043 -259 -945 595 N ATOM 2180 CA VAL B 329 -3.249 9.277 -54.007 1.00 32.42 C ANISOU 2180 CA VAL B 329 4329 3827 4163 -167 -915 518 C ATOM 2181 C VAL B 329 -2.290 8.855 -52.896 1.00 32.40 C ANISOU 2181 C VAL B 329 4245 3806 4257 -187 -754 497 C ATOM 2182 O VAL B 329 -2.597 8.988 -51.707 1.00 35.39 O ANISOU 2182 O VAL B 329 4537 4152 4758 -102 -744 491 O ATOM 2183 CB VAL B 329 -3.921 8.013 -54.609 1.00 36.49 C ANISOU 2183 CB VAL B 329 4749 4441 4675 -209 -911 421 C ATOM 2184 CG1 VAL B 329 -4.217 6.986 -53.527 1.00 34.07 C ANISOU 2184 CG1 VAL B 329 4286 4146 4514 -195 -810 340 C ATOM 2185 CG2 VAL B 329 -5.187 8.389 -55.370 1.00 38.08 C ANISOU 2185 CG2 VAL B 329 4948 4709 4811 -147 -1099 416 C ATOM 2186 N VAL B 330 -1.126 8.353 -53.296 1.00 31.33 N ANISOU 2186 N VAL B 330 4135 3715 4054 -285 -633 478 N ATOM 2187 CA VAL B 330 -0.150 7.841 -52.347 1.00 29.77 C ANISOU 2187 CA VAL B 330 3849 3540 3924 -272 -494 444 C ATOM 2188 C VAL B 330 0.417 8.978 -51.497 1.00 30.66 C ANISOU 2188 C VAL B 330 3981 3616 4053 -276 -494 505 C ATOM 2189 O VAL B 330 0.554 8.832 -50.280 1.00 29.00 O ANISOU 2189 O VAL B 330 3680 3393 3948 -205 -450 491 O ATOM 2190 CB VAL B 330 0.993 7.095 -53.057 1.00 33.17 C ANISOU 2190 CB VAL B 330 4280 4068 4253 -340 -374 388 C ATOM 2191 CG1 VAL B 330 2.058 6.695 -52.055 1.00 33.54 C ANISOU 2191 CG1 VAL B 330 4224 4170 4349 -282 -257 350 C ATOM 2192 CG2 VAL B 330 0.453 5.864 -53.781 1.00 33.45 C ANISOU 2192 CG2 VAL B 330 4326 4112 4273 -334 -361 310 C ATOM 2193 N VAL B 331 0.717 10.112 -52.131 1.00 30.87 N ANISOU 2193 N VAL B 331 4156 3613 3960 -373 -546 574 N ATOM 2194 CA VAL B 331 1.190 11.283 -51.392 1.00 32.93 C ANISOU 2194 CA VAL B 331 4489 3809 4213 -414 -552 629 C ATOM 2195 C VAL B 331 0.181 11.680 -50.315 1.00 32.47 C ANISOU 2195 C VAL B 331 4404 3643 4291 -256 -635 642 C ATOM 2196 O VAL B 331 0.556 11.917 -49.167 1.00 34.04 O ANISOU 2196 O VAL B 331 4546 3829 4559 -235 -589 634 O ATOM 2197 CB VAL B 331 1.457 12.485 -52.322 1.00 38.65 C ANISOU 2197 CB VAL B 331 5460 4464 4761 -561 -609 710 C ATOM 2198 CG1 VAL B 331 1.735 13.747 -51.500 1.00 39.59 C ANISOU 2198 CG1 VAL B 331 5712 4463 4869 -606 -631 763 C ATOM 2199 CG2 VAL B 331 2.623 12.179 -53.255 1.00 38.67 C ANISOU 2199 CG2 VAL B 331 5469 4613 4610 -757 -492 682 C ATOM 2200 N ALA B 332 -1.097 11.711 -50.685 1.00 34.12 N ANISOU 2200 N ALA B 332 4631 3807 4525 -142 -757 648 N ATOM 2201 CA ALA B 332 -2.169 12.013 -49.737 1.00 34.21 C ANISOU 2201 CA ALA B 332 4576 3767 4655 24 -832 634 C ATOM 2202 C ALA B 332 -2.183 11.036 -48.556 1.00 30.79 C ANISOU 2202 C ALA B 332 3943 3395 4361 63 -725 566 C ATOM 2203 O ALA B 332 -2.330 11.440 -47.406 1.00 34.67 O ANISOU 2203 O ALA B 332 4398 3846 4930 135 -715 561 O ATOM 2204 CB ALA B 332 -3.529 12.003 -50.447 1.00 31.90 C ANISOU 2204 CB ALA B 332 4271 3499 4350 141 -977 619 C ATOM 2205 N VAL B 333 -2.025 9.749 -48.844 1.00 29.07 N ANISOU 2205 N VAL B 333 3632 3257 4156 16 -644 513 N ATOM 2206 CA VAL B 333 -2.051 8.734 -47.793 1.00 26.33 C ANISOU 2206 CA VAL B 333 3161 2935 3910 50 -545 459 C ATOM 2207 C VAL B 333 -0.837 8.887 -46.875 1.00 29.27 C ANISOU 2207 C VAL B 333 3526 3305 4291 42 -456 475 C ATOM 2208 O VAL B 333 -0.957 8.797 -45.657 1.00 30.39 O ANISOU 2208 O VAL B 333 3609 3429 4510 103 -421 463 O ATOM 2209 CB VAL B 333 -2.102 7.310 -48.390 1.00 25.86 C ANISOU 2209 CB VAL B 333 3073 2918 3833 1 -480 398 C ATOM 2210 CG1 VAL B 333 -1.794 6.261 -47.332 1.00 24.31 C ANISOU 2210 CG1 VAL B 333 2834 2704 3700 31 -366 360 C ATOM 2211 CG2 VAL B 333 -3.461 7.058 -49.041 1.00 25.82 C ANISOU 2211 CG2 VAL B 333 3033 2950 3828 -11 -567 358 C ATOM 2212 N VAL B 334 0.324 9.132 -47.473 1.00 28.40 N ANISOU 2212 N VAL B 334 3466 3241 4085 -43 -419 492 N ATOM 2213 CA VAL B 334 1.539 9.401 -46.716 1.00 27.97 C ANISOU 2213 CA VAL B 334 3375 3242 4009 -71 -348 492 C ATOM 2214 C VAL B 334 1.362 10.631 -45.822 1.00 30.05 C ANISOU 2214 C VAL B 334 3688 3428 4302 -69 -399 531 C ATOM 2215 O VAL B 334 1.640 10.576 -44.625 1.00 27.39 O ANISOU 2215 O VAL B 334 3283 3105 4018 -21 -361 514 O ATOM 2216 CB VAL B 334 2.747 9.606 -47.650 1.00 30.72 C ANISOU 2216 CB VAL B 334 3748 3702 4221 -203 -299 486 C ATOM 2217 CG1 VAL B 334 3.953 10.099 -46.855 1.00 29.11 C ANISOU 2217 CG1 VAL B 334 3480 3603 3979 -264 -240 471 C ATOM 2218 CG2 VAL B 334 3.062 8.305 -48.406 1.00 27.64 C ANISOU 2218 CG2 VAL B 334 3305 3400 3797 -171 -231 424 C ATOM 2219 N ALA B 335 0.875 11.726 -46.401 1.00 31.15 N ANISOU 2219 N ALA B 335 3971 3471 4392 -106 -491 580 N ATOM 2220 CA ALA B 335 0.638 12.954 -45.648 1.00 29.54 C ANISOU 2220 CA ALA B 335 3872 3153 4200 -86 -548 611 C ATOM 2221 C ALA B 335 -0.304 12.709 -44.470 1.00 30.69 C ANISOU 2221 C ALA B 335 3915 3270 4477 74 -560 576 C ATOM 2222 O ALA B 335 -0.018 13.117 -43.346 1.00 33.96 O ANISOU 2222 O ALA B 335 4320 3664 4921 87 -532 565 O ATOM 2223 CB ALA B 335 0.078 14.047 -46.563 1.00 29.53 C ANISOU 2223 CB ALA B 335 4091 3018 4111 -94 -667 671 C ATOM 2224 N SER B 336 -1.409 12.019 -44.723 1.00 31.33 N ANISOU 2224 N SER B 336 3912 3372 4621 171 -592 548 N ATOM 2225 CA SER B 336 -2.392 11.746 -43.674 1.00 30.56 C ANISOU 2225 CA SER B 336 3700 3282 4627 289 -588 501 C ATOM 2226 C SER B 336 -1.822 10.908 -42.521 1.00 30.87 C ANISOU 2226 C SER B 336 3644 3369 4715 274 -471 475 C ATOM 2227 O SER B 336 -2.303 11.007 -41.396 1.00 32.14 O ANISOU 2227 O SER B 336 3755 3522 4933 340 -451 448 O ATOM 2228 CB SER B 336 -3.621 11.047 -44.257 1.00 34.86 C ANISOU 2228 CB SER B 336 4149 3892 5205 338 -629 457 C ATOM 2229 OG SER B 336 -3.302 9.737 -44.698 1.00 43.24 O ANISOU 2229 OG SER B 336 5159 5012 6259 252 -551 436 O ATOM 2230 N PHE B 337 -0.805 10.091 -42.790 1.00 29.64 N ANISOU 2230 N PHE B 337 3472 3269 4520 208 -398 478 N ATOM 2231 CA PHE B 337 -0.190 9.284 -41.735 1.00 27.94 C ANISOU 2231 CA PHE B 337 3197 3093 4324 236 -309 459 C ATOM 2232 C PHE B 337 0.428 10.188 -40.666 1.00 31.11 C ANISOU 2232 C PHE B 337 3609 3495 4717 236 -308 469 C ATOM 2233 O PHE B 337 0.194 10.003 -39.476 1.00 28.50 O ANISOU 2233 O PHE B 337 3246 3157 4425 293 -277 454 O ATOM 2234 CB PHE B 337 0.870 8.334 -42.314 1.00 24.75 C ANISOU 2234 CB PHE B 337 2781 2762 3859 216 -250 448 C ATOM 2235 CG PHE B 337 1.643 7.556 -41.270 1.00 21.19 C ANISOU 2235 CG PHE B 337 2295 2357 3400 293 -183 432 C ATOM 2236 CD1 PHE B 337 1.248 6.278 -40.896 1.00 20.83 C ANISOU 2236 CD1 PHE B 337 2280 2260 3374 362 -133 415 C ATOM 2237 CD2 PHE B 337 2.784 8.094 -40.686 1.00 23.77 C ANISOU 2237 CD2 PHE B 337 2575 2780 3676 290 -177 430 C ATOM 2238 CE1 PHE B 337 1.965 5.566 -39.937 1.00 22.26 C ANISOU 2238 CE1 PHE B 337 2476 2460 3522 466 -88 411 C ATOM 2239 CE2 PHE B 337 3.507 7.392 -39.734 1.00 25.69 C ANISOU 2239 CE2 PHE B 337 2780 3089 3893 395 -139 413 C ATOM 2240 CZ PHE B 337 3.100 6.125 -39.362 1.00 26.69 C ANISOU 2240 CZ PHE B 337 2965 3139 4035 503 -101 411 C ATOM 2241 N PHE B 338 1.218 11.165 -41.096 1.00 30.15 N ANISOU 2241 N PHE B 338 3549 3383 4524 145 -337 490 N ATOM 2242 CA PHE B 338 1.897 12.049 -40.155 1.00 28.37 C ANISOU 2242 CA PHE B 338 3348 3166 4266 99 -334 486 C ATOM 2243 C PHE B 338 0.949 13.059 -39.514 1.00 28.75 C ANISOU 2243 C PHE B 338 3485 3081 4358 153 -389 486 C ATOM 2244 O PHE B 338 1.136 13.424 -38.357 1.00 33.32 O ANISOU 2244 O PHE B 338 4061 3657 4942 166 -371 465 O ATOM 2245 CB PHE B 338 3.055 12.770 -40.838 1.00 24.72 C ANISOU 2245 CB PHE B 338 2939 2767 3688 -71 -331 494 C ATOM 2246 CG PHE B 338 4.097 11.841 -41.391 1.00 26.92 C ANISOU 2246 CG PHE B 338 3095 3225 3907 -104 -268 467 C ATOM 2247 CD1 PHE B 338 4.960 11.164 -40.540 1.00 22.64 C ANISOU 2247 CD1 PHE B 338 2415 2836 3351 -43 -219 423 C ATOM 2248 CD2 PHE B 338 4.203 11.626 -42.762 1.00 24.33 C ANISOU 2248 CD2 PHE B 338 2796 2923 3526 -169 -263 476 C ATOM 2249 CE1 PHE B 338 5.914 10.304 -41.035 1.00 22.85 C ANISOU 2249 CE1 PHE B 338 2324 3043 3313 -18 -170 381 C ATOM 2250 CE2 PHE B 338 5.161 10.772 -43.267 1.00 24.44 C ANISOU 2250 CE2 PHE B 338 2693 3116 3477 -174 -198 431 C ATOM 2251 CZ PHE B 338 6.023 10.105 -42.395 1.00 23.49 C ANISOU 2251 CZ PHE B 338 2425 3154 3347 -83 -152 378 C ATOM 2252 N ILE B 339 -0.071 13.491 -40.249 1.00 27.34 N ANISOU 2252 N ILE B 339 3381 2807 4199 207 -461 501 N ATOM 2253 CA ILE B 339 -1.057 14.416 -39.688 1.00 26.41 C ANISOU 2253 CA ILE B 339 3338 2579 4117 319 -522 482 C ATOM 2254 C ILE B 339 -1.777 13.807 -38.481 1.00 28.93 C ANISOU 2254 C ILE B 339 3518 2953 4522 425 -470 429 C ATOM 2255 O ILE B 339 -1.916 14.445 -37.439 1.00 27.96 O ANISOU 2255 O ILE B 339 3429 2788 4406 472 -464 398 O ATOM 2256 CB ILE B 339 -2.097 14.848 -40.748 1.00 31.01 C ANISOU 2256 CB ILE B 339 3996 3091 4695 413 -629 496 C ATOM 2257 CG1 ILE B 339 -1.480 15.878 -41.698 1.00 35.50 C ANISOU 2257 CG1 ILE B 339 4801 3541 5146 312 -693 558 C ATOM 2258 CG2 ILE B 339 -3.324 15.449 -40.084 1.00 33.47 C ANISOU 2258 CG2 ILE B 339 4303 3354 5058 604 -686 444 C ATOM 2259 CD1 ILE B 339 -2.224 16.038 -42.996 1.00 39.28 C ANISOU 2259 CD1 ILE B 339 5363 3978 5585 382 -799 591 C ATOM 2260 N PHE B 340 -2.196 12.554 -38.609 1.00 28.83 N ANISOU 2260 N PHE B 340 3372 3027 4554 438 -421 415 N ATOM 2261 CA PHE B 340 -3.032 11.941 -37.590 1.00 29.60 C ANISOU 2261 CA PHE B 340 3362 3174 4709 498 -361 364 C ATOM 2262 C PHE B 340 -2.245 11.247 -36.467 1.00 27.68 C ANISOU 2262 C PHE B 340 3101 2967 4450 461 -269 370 C ATOM 2263 O PHE B 340 -2.819 10.929 -35.428 1.00 28.75 O ANISOU 2263 O PHE B 340 3191 3127 4606 492 -212 335 O ATOM 2264 CB PHE B 340 -4.017 10.968 -38.255 1.00 33.12 C ANISOU 2264 CB PHE B 340 3708 3688 5188 496 -351 335 C ATOM 2265 CG PHE B 340 -5.052 11.662 -39.104 1.00 33.72 C ANISOU 2265 CG PHE B 340 3763 3775 5274 579 -458 306 C ATOM 2266 CD1 PHE B 340 -5.956 12.546 -38.528 1.00 32.71 C ANISOU 2266 CD1 PHE B 340 3601 3657 5169 715 -503 248 C ATOM 2267 CD2 PHE B 340 -5.109 11.456 -40.474 1.00 34.10 C ANISOU 2267 CD2 PHE B 340 3830 3832 5294 548 -521 330 C ATOM 2268 CE1 PHE B 340 -6.898 13.206 -39.300 1.00 38.01 C ANISOU 2268 CE1 PHE B 340 4256 4353 5833 848 -623 216 C ATOM 2269 CE2 PHE B 340 -6.053 12.113 -41.251 1.00 34.97 C ANISOU 2269 CE2 PHE B 340 3931 3964 5392 653 -642 307 C ATOM 2270 CZ PHE B 340 -6.946 12.982 -40.662 1.00 37.14 C ANISOU 2270 CZ PHE B 340 4168 4255 5689 818 -700 250 C ATOM 2271 N TRP B 341 -0.942 11.041 -36.653 1.00 28.55 N ANISOU 2271 N TRP B 341 3241 3099 4506 403 -257 407 N ATOM 2272 CA TRP B 341 -0.115 10.453 -35.592 1.00 25.01 C ANISOU 2272 CA TRP B 341 2778 2705 4021 410 -199 411 C ATOM 2273 C TRP B 341 0.588 11.503 -34.734 1.00 25.45 C ANISOU 2273 C TRP B 341 2866 2772 4031 384 -220 400 C ATOM 2274 O TRP B 341 1.018 11.207 -33.617 1.00 25.08 O ANISOU 2274 O TRP B 341 2805 2776 3950 409 -187 392 O ATOM 2275 CB TRP B 341 0.932 9.501 -36.174 1.00 24.42 C ANISOU 2275 CB TRP B 341 2685 2697 3896 402 -178 432 C ATOM 2276 CG TRP B 341 0.408 8.126 -36.345 1.00 24.24 C ANISOU 2276 CG TRP B 341 2675 2646 3890 440 -127 434 C ATOM 2277 CD1 TRP B 341 0.123 7.499 -37.521 1.00 23.35 C ANISOU 2277 CD1 TRP B 341 2571 2513 3787 416 -125 432 C ATOM 2278 CD2 TRP B 341 0.069 7.201 -35.300 1.00 26.51 C ANISOU 2278 CD2 TRP B 341 3006 2901 4165 483 -64 436 C ATOM 2279 NE1 TRP B 341 -0.366 6.234 -37.274 1.00 27.61 N ANISOU 2279 NE1 TRP B 341 3166 3002 4324 430 -63 426 N ATOM 2280 CE2 TRP B 341 -0.404 6.026 -35.918 1.00 27.66 C ANISOU 2280 CE2 TRP B 341 3207 2993 4312 467 -22 434 C ATOM 2281 CE3 TRP B 341 0.131 7.250 -33.901 1.00 26.45 C ANISOU 2281 CE3 TRP B 341 3024 2899 4128 518 -36 438 C ATOM 2282 CZ2 TRP B 341 -0.819 4.912 -35.188 1.00 25.86 C ANISOU 2282 CZ2 TRP B 341 3084 2694 4049 467 51 439 C ATOM 2283 CZ3 TRP B 341 -0.281 6.138 -33.174 1.00 27.88 C ANISOU 2283 CZ3 TRP B 341 3298 3023 4272 533 34 451 C ATOM 2284 CH2 TRP B 341 -0.749 4.986 -33.821 1.00 27.01 C ANISOU 2284 CH2 TRP B 341 3267 2838 4157 499 79 453 C ATOM 2285 N LEU B 342 0.704 12.720 -35.264 1.00 26.98 N ANISOU 2285 N LEU B 342 3133 2910 4207 325 -278 399 N ATOM 2286 CA LEU B 342 1.460 13.783 -34.604 1.00 28.34 C ANISOU 2286 CA LEU B 342 3374 3079 4315 248 -296 380 C ATOM 2287 C LEU B 342 1.035 14.042 -33.143 1.00 26.67 C ANISOU 2287 C LEU B 342 3173 2847 4112 310 -272 339 C ATOM 2288 O LEU B 342 1.895 14.059 -32.258 1.00 28.16 O ANISOU 2288 O LEU B 342 3343 3121 4237 266 -256 323 O ATOM 2289 CB LEU B 342 1.375 15.080 -35.423 1.00 28.59 C ANISOU 2289 CB LEU B 342 3563 2985 4314 171 -360 389 C ATOM 2290 CG LEU B 342 2.191 16.237 -34.852 1.00 32.85 C ANISOU 2290 CG LEU B 342 4225 3494 4762 35 -372 363 C ATOM 2291 CD1 LEU B 342 3.656 15.849 -34.749 1.00 30.88 C ANISOU 2291 CD1 LEU B 342 3862 3444 4426 -111 -335 352 C ATOM 2292 CD2 LEU B 342 2.017 17.475 -35.707 1.00 36.53 C ANISOU 2292 CD2 LEU B 342 4924 3780 5175 -42 -434 383 C ATOM 2293 N PRO B 343 -0.275 14.224 -32.877 1.00 26.22 N ANISOU 2293 N PRO B 343 3129 2712 4120 416 -270 311 N ATOM 2294 CA PRO B 343 -0.642 14.471 -31.475 1.00 30.63 C ANISOU 2294 CA PRO B 343 3695 3274 4671 466 -232 259 C ATOM 2295 C PRO B 343 -0.271 13.307 -30.561 1.00 33.17 C ANISOU 2295 C PRO B 343 3938 3703 4963 468 -164 274 C ATOM 2296 O PRO B 343 0.186 13.528 -29.438 1.00 28.75 O ANISOU 2296 O PRO B 343 3402 3180 4340 455 -148 251 O ATOM 2297 CB PRO B 343 -2.162 14.649 -31.533 1.00 29.90 C ANISOU 2297 CB PRO B 343 3575 3138 4649 590 -230 211 C ATOM 2298 CG PRO B 343 -2.431 15.080 -32.947 1.00 29.25 C ANISOU 2298 CG PRO B 343 3538 2985 4592 610 -310 237 C ATOM 2299 CD PRO B 343 -1.451 14.306 -33.763 1.00 27.25 C ANISOU 2299 CD PRO B 343 3254 2783 4316 498 -305 306 C ATOM 2300 N TYR B 344 -0.462 12.084 -31.046 1.00 28.51 N ANISOU 2300 N TYR B 344 3285 3149 4400 487 -130 311 N ATOM 2301 CA TYR B 344 -0.063 10.914 -30.287 1.00 24.47 C ANISOU 2301 CA TYR B 344 2764 2697 3836 506 -76 339 C ATOM 2302 C TYR B 344 1.415 11.021 -29.933 1.00 24.68 C ANISOU 2302 C TYR B 344 2789 2815 3774 492 -115 353 C ATOM 2303 O TYR B 344 1.789 10.887 -28.773 1.00 25.69 O ANISOU 2303 O TYR B 344 2937 2996 3829 518 -104 347 O ATOM 2304 CB TYR B 344 -0.347 9.634 -31.078 1.00 21.98 C ANISOU 2304 CB TYR B 344 2437 2369 3547 516 -43 375 C ATOM 2305 CG TYR B 344 0.223 8.379 -30.461 1.00 24.76 C ANISOU 2305 CG TYR B 344 2849 2739 3821 561 -3 415 C ATOM 2306 CD1 TYR B 344 -0.525 7.622 -29.568 1.00 26.64 C ANISOU 2306 CD1 TYR B 344 3159 2936 4025 554 76 420 C ATOM 2307 CD2 TYR B 344 1.502 7.943 -30.782 1.00 23.25 C ANISOU 2307 CD2 TYR B 344 2655 2611 3570 618 -44 443 C ATOM 2308 CE1 TYR B 344 -0.007 6.464 -29.002 1.00 28.81 C ANISOU 2308 CE1 TYR B 344 3559 3186 4204 611 103 470 C ATOM 2309 CE2 TYR B 344 2.026 6.790 -30.235 1.00 26.53 C ANISOU 2309 CE2 TYR B 344 3155 3029 3898 717 -28 479 C ATOM 2310 CZ TYR B 344 1.270 6.053 -29.340 1.00 30.77 C ANISOU 2310 CZ TYR B 344 3819 3477 4396 717 41 501 C ATOM 2311 OH TYR B 344 1.793 4.904 -28.785 1.00 29.26 O ANISOU 2311 OH TYR B 344 3778 3248 4092 830 48 549 O ATOM 2312 N GLN B 345 2.244 11.296 -30.935 1.00 23.88 N ANISOU 2312 N GLN B 345 2654 2758 3663 442 -162 362 N ATOM 2313 CA GLN B 345 3.691 11.346 -30.740 1.00 27.00 C ANISOU 2313 CA GLN B 345 2992 3307 3960 414 -196 352 C ATOM 2314 C GLN B 345 4.116 12.488 -29.807 1.00 33.27 C ANISOU 2314 C GLN B 345 3810 4141 4689 327 -223 304 C ATOM 2315 O GLN B 345 4.973 12.289 -28.950 1.00 34.21 O ANISOU 2315 O GLN B 345 3880 4404 4714 344 -241 285 O ATOM 2316 CB GLN B 345 4.412 11.462 -32.093 1.00 24.78 C ANISOU 2316 CB GLN B 345 2655 3092 3669 341 -220 354 C ATOM 2317 CG GLN B 345 4.273 10.221 -32.997 1.00 21.80 C ANISOU 2317 CG GLN B 345 2253 2707 3325 432 -196 387 C ATOM 2318 CD GLN B 345 5.144 9.058 -32.537 1.00 26.97 C ANISOU 2318 CD GLN B 345 2858 3487 3901 573 -192 388 C ATOM 2319 OE1 GLN B 345 5.822 9.145 -31.511 1.00 29.78 O ANISOU 2319 OE1 GLN B 345 3179 3959 4178 614 -218 369 O ATOM 2320 NE2 GLN B 345 5.137 7.965 -33.301 1.00 27.60 N ANISOU 2320 NE2 GLN B 345 2953 3544 3990 665 -171 406 N ATOM 2321 N VAL B 346 3.515 13.670 -29.964 1.00 26.50 N ANISOU 2321 N VAL B 346 3045 3153 3869 246 -233 278 N ATOM 2322 CA VAL B 346 3.852 14.812 -29.109 1.00 29.15 C ANISOU 2322 CA VAL B 346 3456 3485 4135 149 -254 221 C ATOM 2323 C VAL B 346 3.515 14.568 -27.639 1.00 28.04 C ANISOU 2323 C VAL B 346 3326 3364 3963 231 -226 196 C ATOM 2324 O VAL B 346 4.337 14.815 -26.757 1.00 33.96 O ANISOU 2324 O VAL B 346 4063 4233 4609 175 -247 159 O ATOM 2325 CB VAL B 346 3.131 16.099 -29.557 1.00 32.54 C ANISOU 2325 CB VAL B 346 4047 3715 4600 94 -273 197 C ATOM 2326 CG1 VAL B 346 3.350 17.211 -28.530 1.00 33.31 C ANISOU 2326 CG1 VAL B 346 4270 3769 4619 9 -284 126 C ATOM 2327 CG2 VAL B 346 3.605 16.525 -30.939 1.00 30.56 C ANISOU 2327 CG2 VAL B 346 3840 3436 4336 -30 -305 225 C ATOM 2328 N THR B 347 2.309 14.079 -27.376 1.00 28.42 N ANISOU 2328 N THR B 347 3393 3321 4084 346 -175 209 N ATOM 2329 CA THR B 347 1.885 13.835 -26.002 1.00 30.09 C ANISOU 2329 CA THR B 347 3631 3551 4252 402 -129 185 C ATOM 2330 C THR B 347 2.664 12.682 -25.390 1.00 33.34 C ANISOU 2330 C THR B 347 4000 4096 4574 454 -130 231 C ATOM 2331 O THR B 347 2.980 12.695 -24.195 1.00 32.07 O ANISOU 2331 O THR B 347 3871 4005 4311 463 -131 211 O ATOM 2332 CB THR B 347 0.385 13.529 -25.919 1.00 34.49 C ANISOU 2332 CB THR B 347 4195 4021 4890 481 -57 173 C ATOM 2333 OG1 THR B 347 0.074 12.435 -26.787 1.00 32.35 O ANISOU 2333 OG1 THR B 347 3867 3747 4678 511 -35 232 O ATOM 2334 CG2 THR B 347 -0.425 14.753 -26.335 1.00 35.50 C ANISOU 2334 CG2 THR B 347 4372 4033 5084 497 -75 109 C ATOM 2335 N GLY B 348 2.979 11.692 -26.223 1.00 33.01 N ANISOU 2335 N GLY B 348 3906 4083 4554 505 -137 290 N ATOM 2336 CA GLY B 348 3.744 10.537 -25.787 1.00 30.45 C ANISOU 2336 CA GLY B 348 3574 3862 4135 608 -154 335 C ATOM 2337 C GLY B 348 5.104 10.935 -25.251 1.00 34.11 C ANISOU 2337 C GLY B 348 3964 4521 4475 595 -234 299 C ATOM 2338 O GLY B 348 5.493 10.543 -24.148 1.00 34.63 O ANISOU 2338 O GLY B 348 4061 4673 4424 672 -258 305 O ATOM 2339 N ILE B 349 5.826 11.732 -26.032 1.00 34.96 N ANISOU 2339 N ILE B 349 3978 4716 4590 480 -276 255 N ATOM 2340 CA ILE B 349 7.168 12.151 -25.658 1.00 37.28 C ANISOU 2340 CA ILE B 349 4159 5252 4756 419 -347 196 C ATOM 2341 C ILE B 349 7.154 13.055 -24.425 1.00 35.59 C ANISOU 2341 C ILE B 349 4008 5053 4463 324 -360 138 C ATOM 2342 O ILE B 349 8.021 12.944 -23.554 1.00 33.28 O ANISOU 2342 O ILE B 349 3648 4965 4032 349 -420 103 O ATOM 2343 CB ILE B 349 7.857 12.855 -26.838 1.00 36.89 C ANISOU 2343 CB ILE B 349 4013 5289 4716 251 -363 154 C ATOM 2344 CG1 ILE B 349 8.389 11.805 -27.811 1.00 35.46 C ANISOU 2344 CG1 ILE B 349 3713 5218 4543 373 -368 183 C ATOM 2345 CG2 ILE B 349 8.994 13.743 -26.358 1.00 39.56 C ANISOU 2345 CG2 ILE B 349 4258 5857 4917 74 -414 61 C ATOM 2346 CD1 ILE B 349 9.547 10.983 -27.242 1.00 33.24 C ANISOU 2346 CD1 ILE B 349 3285 5219 4124 537 -434 155 C ATOM 2347 N MET B 350 6.149 13.925 -24.349 1.00 34.86 N ANISOU 2347 N MET B 350 4046 4752 4448 239 -311 119 N ATOM 2348 CA MET B 350 6.014 14.857 -23.233 1.00 36.89 C ANISOU 2348 CA MET B 350 4397 4986 4634 153 -311 49 C ATOM 2349 C MET B 350 5.801 14.130 -21.910 1.00 37.84 C ANISOU 2349 C MET B 350 4552 5155 4671 283 -300 68 C ATOM 2350 O MET B 350 6.469 14.419 -20.918 1.00 40.08 O ANISOU 2350 O MET B 350 4830 5583 4816 241 -346 17 O ATOM 2351 CB MET B 350 4.857 15.833 -23.485 1.00 36.99 C ANISOU 2351 CB MET B 350 4558 4748 4748 106 -260 19 C ATOM 2352 CG MET B 350 5.195 16.976 -24.438 1.00 39.34 C ANISOU 2352 CG MET B 350 4918 4968 5059 -69 -288 -17 C ATOM 2353 SD MET B 350 3.792 18.043 -24.863 1.00 51.08 S ANISOU 2353 SD MET B 350 6614 6139 6654 -34 -256 -43 S ATOM 2354 CE MET B 350 3.317 18.699 -23.269 1.00 49.46 C ANISOU 2354 CE MET B 350 6533 5883 6375 -7 -226 -139 C ATOM 2355 N MET B 351 4.855 13.197 -21.902 1.00 35.55 N ANISOU 2355 N MET B 351 4312 4747 4446 416 -235 137 N ATOM 2356 CA MET B 351 4.541 12.432 -20.703 1.00 33.74 C ANISOU 2356 CA MET B 351 4166 4533 4122 515 -205 169 C ATOM 2357 C MET B 351 5.750 11.666 -20.175 1.00 33.51 C ANISOU 2357 C MET B 351 4092 4705 3936 618 -297 202 C ATOM 2358 O MET B 351 5.938 11.565 -18.967 1.00 34.10 O ANISOU 2358 O MET B 351 4233 4854 3867 652 -319 195 O ATOM 2359 CB MET B 351 3.394 11.456 -20.978 1.00 33.17 C ANISOU 2359 CB MET B 351 4162 4310 4132 592 -110 239 C ATOM 2360 CG MET B 351 2.053 12.126 -21.231 1.00 39.25 C ANISOU 2360 CG MET B 351 4952 4936 5026 531 -20 188 C ATOM 2361 SD MET B 351 0.752 10.969 -21.718 1.00 36.56 S ANISOU 2361 SD MET B 351 4636 4485 4771 566 91 244 S ATOM 2362 CE MET B 351 0.712 9.913 -20.265 1.00 30.43 C ANISOU 2362 CE MET B 351 4012 3735 3814 595 148 296 C ATOM 2363 N SER B 352 6.567 11.124 -21.074 1.00 32.48 N ANISOU 2363 N SER B 352 3847 4678 3816 688 -357 230 N ATOM 2364 CA SER B 352 7.726 10.340 -20.648 1.00 33.94 C ANISOU 2364 CA SER B 352 3969 5082 3845 848 -461 248 C ATOM 2365 C SER B 352 8.762 11.218 -19.942 1.00 38.83 C ANISOU 2365 C SER B 352 4468 5960 4326 751 -553 150 C ATOM 2366 O SER B 352 9.485 10.749 -19.066 1.00 41.53 O ANISOU 2366 O SER B 352 4792 6490 4498 884 -644 150 O ATOM 2367 CB SER B 352 8.367 9.627 -21.836 1.00 32.39 C ANISOU 2367 CB SER B 352 3654 4963 3690 960 -497 272 C ATOM 2368 OG SER B 352 8.949 10.558 -22.729 1.00 38.36 O ANISOU 2368 OG SER B 352 4233 5843 4499 789 -513 194 O ATOM 2369 N PHE B 353 8.825 12.492 -20.323 1.00 40.45 N ANISOU 2369 N PHE B 353 4613 6169 4586 515 -536 64 N ATOM 2370 CA PHE B 353 9.794 13.413 -19.730 1.00 46.32 C ANISOU 2370 CA PHE B 353 5256 7152 5190 354 -612 -48 C ATOM 2371 C PHE B 353 9.225 14.164 -18.522 1.00 48.18 C ANISOU 2371 C PHE B 353 5654 7289 5365 256 -583 -95 C ATOM 2372 O PHE B 353 9.897 15.016 -17.947 1.00 47.78 O ANISOU 2372 O PHE B 353 5563 7400 5191 88 -636 -198 O ATOM 2373 CB PHE B 353 10.300 14.408 -20.786 1.00 43.91 C ANISOU 2373 CB PHE B 353 4845 6904 4936 107 -605 -125 C ATOM 2374 CG PHE B 353 11.381 13.850 -21.675 1.00 40.61 C ANISOU 2374 CG PHE B 353 4191 6754 4484 158 -660 -138 C ATOM 2375 CD1 PHE B 353 12.715 13.966 -21.321 1.00 37.74 C ANISOU 2375 CD1 PHE B 353 3605 6790 3945 106 -758 -239 C ATOM 2376 CD2 PHE B 353 11.062 13.203 -22.861 1.00 40.98 C ANISOU 2376 CD2 PHE B 353 4222 6686 4662 259 -614 -67 C ATOM 2377 CE1 PHE B 353 13.709 13.452 -22.127 1.00 36.35 C ANISOU 2377 CE1 PHE B 353 3178 6908 3727 172 -802 -275 C ATOM 2378 CE2 PHE B 353 12.058 12.683 -23.679 1.00 38.29 C ANISOU 2378 CE2 PHE B 353 3663 6607 4281 321 -655 -95 C ATOM 2379 CZ PHE B 353 13.380 12.809 -23.312 1.00 36.90 C ANISOU 2379 CZ PHE B 353 3248 6842 3930 286 -745 -203 C ATOM 2380 N LEU B 354 7.996 13.832 -18.136 1.00 46.93 N ANISOU 2380 N LEU B 354 5671 6884 5276 346 -492 -32 N ATOM 2381 CA LEU B 354 7.344 14.467 -16.994 1.00 44.43 C ANISOU 2381 CA LEU B 354 5507 6475 4899 278 -444 -84 C ATOM 2382 C LEU B 354 7.218 13.511 -15.813 1.00 45.96 C ANISOU 2382 C LEU B 354 5793 6720 4950 439 -453 -23 C ATOM 2383 O LEU B 354 7.094 12.302 -15.996 1.00 45.00 O ANISOU 2383 O LEU B 354 5698 6568 4831 614 -450 85 O ATOM 2384 CB LEU B 354 5.955 14.980 -17.382 1.00 42.04 C ANISOU 2384 CB LEU B 354 5327 5885 4763 239 -319 -91 C ATOM 2385 CG LEU B 354 5.890 16.189 -18.319 1.00 46.90 C ANISOU 2385 CG LEU B 354 5949 6384 5485 79 -311 -160 C ATOM 2386 CD1 LEU B 354 4.532 16.274 -19.007 1.00 43.81 C ANISOU 2386 CD1 LEU B 354 5631 5745 5270 144 -216 -135 C ATOM 2387 CD2 LEU B 354 6.185 17.468 -17.550 1.00 50.61 C ANISOU 2387 CD2 LEU B 354 6521 6863 5847 -95 -330 -286 C ATOM 2388 N GLU B 355 7.247 14.060 -14.602 1.00 45.96 N ANISOU 2388 N GLU B 355 5877 6780 4807 370 -463 -92 N ATOM 2389 CA GLU B 355 6.944 13.279 -13.411 1.00 47.11 C ANISOU 2389 CA GLU B 355 6165 6936 4800 492 -451 -33 C ATOM 2390 C GLU B 355 5.453 12.974 -13.381 1.00 45.92 C ANISOU 2390 C GLU B 355 6162 6532 4755 508 -285 12 C ATOM 2391 O GLU B 355 4.638 13.837 -13.705 1.00 43.73 O ANISOU 2391 O GLU B 355 5893 6114 4610 404 -191 -63 O ATOM 2392 CB GLU B 355 7.359 14.023 -12.140 1.00 52.05 C ANISOU 2392 CB GLU B 355 6840 7706 5231 393 -501 -134 C ATOM 2393 CG GLU B 355 8.842 14.342 -12.049 1.00 63.31 C ANISOU 2393 CG GLU B 355 8092 9446 6518 346 -669 -205 C ATOM 2394 CD GLU B 355 9.712 13.100 -11.964 1.00 75.83 C ANISOU 2394 CD GLU B 355 9595 11241 7974 588 -801 -110 C ATOM 2395 OE1 GLU B 355 9.196 12.027 -11.585 1.00 80.70 O ANISOU 2395 OE1 GLU B 355 10377 11739 8545 778 -771 13 O ATOM 2396 OE2 GLU B 355 10.917 13.197 -12.279 1.00 80.22 O ANISOU 2396 OE2 GLU B 355 9932 12087 8460 588 -935 -168 O ATOM 2397 N PRO B 356 5.092 11.743 -12.991 1.00 48.64 N ANISOU 2397 N PRO B 356 6632 6826 5023 636 -249 126 N ATOM 2398 CA PRO B 356 3.694 11.298 -12.941 1.00 50.76 C ANISOU 2398 CA PRO B 356 7025 6901 5361 613 -79 164 C ATOM 2399 C PRO B 356 2.828 12.075 -11.939 1.00 53.93 C ANISOU 2399 C PRO B 356 7511 7274 5706 502 36 63 C ATOM 2400 O PRO B 356 1.602 11.985 -12.007 1.00 55.99 O ANISOU 2400 O PRO B 356 7807 7421 6047 457 189 45 O ATOM 2401 CB PRO B 356 3.812 9.824 -12.529 1.00 48.38 C ANISOU 2401 CB PRO B 356 6897 6576 4911 745 -91 306 C ATOM 2402 CG PRO B 356 5.147 9.718 -11.872 1.00 50.40 C ANISOU 2402 CG PRO B 356 7149 7033 4968 861 -269 320 C ATOM 2403 CD PRO B 356 6.024 10.666 -12.620 1.00 49.69 C ANISOU 2403 CD PRO B 356 6808 7090 4981 814 -373 223 C ATOM 2404 N SER B 357 3.452 12.823 -11.032 1.00 54.00 N ANISOU 2404 N SER B 357 7540 7409 5570 456 -34 -19 N ATOM 2405 CA SER B 357 2.706 13.637 -10.078 1.00 55.85 C ANISOU 2405 CA SER B 357 7861 7621 5738 360 72 -137 C ATOM 2406 C SER B 357 2.545 15.084 -10.550 1.00 54.75 C ANISOU 2406 C SER B 357 7646 7421 5736 272 81 -285 C ATOM 2407 O SER B 357 1.958 15.910 -9.850 1.00 56.88 O ANISOU 2407 O SER B 357 7992 7657 5960 217 162 -409 O ATOM 2408 CB SER B 357 3.387 13.612 -8.709 1.00 61.06 C ANISOU 2408 CB SER B 357 8635 8435 6128 353 -1 -150 C ATOM 2409 OG SER B 357 4.716 14.096 -8.791 1.00 66.23 O ANISOU 2409 OG SER B 357 9187 9255 6723 339 -180 -189 O ATOM 2410 N SER B 358 3.062 15.389 -11.737 1.00 48.88 N ANISOU 2410 N SER B 358 6781 6650 5141 263 1 -275 N ATOM 2411 CA SER B 358 2.999 16.749 -12.261 1.00 49.61 C ANISOU 2411 CA SER B 358 6864 6648 5340 171 -4 -397 C ATOM 2412 C SER B 358 1.652 17.030 -12.920 1.00 50.15 C ANISOU 2412 C SER B 358 6932 6531 5590 228 119 -431 C ATOM 2413 O SER B 358 1.058 16.142 -13.535 1.00 51.25 O ANISOU 2413 O SER B 358 7003 6635 5833 304 173 -340 O ATOM 2414 CB SER B 358 4.134 16.997 -13.260 1.00 51.48 C ANISOU 2414 CB SER B 358 6988 6945 5629 105 -134 -376 C ATOM 2415 OG SER B 358 3.890 16.337 -14.488 1.00 52.97 O ANISOU 2415 OG SER B 358 7078 7063 5984 183 -122 -277 O ATOM 2416 N PRO B 359 1.162 18.273 -12.781 1.00 50.37 N ANISOU 2416 N PRO B 359 7048 6447 5644 201 157 -571 N ATOM 2417 CA PRO B 359 -0.104 18.719 -13.373 1.00 48.28 C ANISOU 2417 CA PRO B 359 6779 6031 5534 300 250 -633 C ATOM 2418 C PRO B 359 -0.169 18.548 -14.892 1.00 43.60 C ANISOU 2418 C PRO B 359 6088 5351 5127 340 205 -552 C ATOM 2419 O PRO B 359 -1.240 18.259 -15.428 1.00 43.75 O ANISOU 2419 O PRO B 359 6032 5324 5266 444 279 -549 O ATOM 2420 CB PRO B 359 -0.160 20.203 -12.996 1.00 50.71 C ANISOU 2420 CB PRO B 359 7250 6220 5797 272 243 -796 C ATOM 2421 CG PRO B 359 0.625 20.295 -11.744 1.00 54.24 C ANISOU 2421 CG PRO B 359 7781 6791 6036 157 215 -838 C ATOM 2422 CD PRO B 359 1.744 19.301 -11.899 1.00 54.09 C ANISOU 2422 CD PRO B 359 7647 6939 5965 91 114 -695 C ATOM 2423 N THR B 360 0.952 18.732 -15.578 1.00 43.41 N ANISOU 2423 N THR B 360 6051 5330 5111 245 88 -501 N ATOM 2424 CA THR B 360 0.965 18.595 -17.028 1.00 42.39 C ANISOU 2424 CA THR B 360 5845 5125 5136 266 47 -427 C ATOM 2425 C THR B 360 0.826 17.126 -17.414 1.00 42.35 C ANISOU 2425 C THR B 360 5698 5209 5182 333 71 -297 C ATOM 2426 O THR B 360 0.159 16.802 -18.397 1.00 40.05 O ANISOU 2426 O THR B 360 5339 4849 5029 399 97 -256 O ATOM 2427 CB THR B 360 2.247 19.180 -17.651 1.00 47.40 C ANISOU 2427 CB THR B 360 6500 5769 5739 110 -66 -419 C ATOM 2428 OG1 THR B 360 2.401 20.542 -17.235 1.00 53.47 O ANISOU 2428 OG1 THR B 360 7456 6428 6432 7 -83 -543 O ATOM 2429 CG2 THR B 360 2.176 19.134 -19.175 1.00 43.70 C ANISOU 2429 CG2 THR B 360 5980 5209 5416 124 -96 -349 C ATOM 2430 N PHE B 361 1.439 16.241 -16.628 1.00 41.62 N ANISOU 2430 N PHE B 361 5589 5261 4964 323 58 -237 N ATOM 2431 CA PHE B 361 1.339 14.806 -16.885 1.00 40.91 C ANISOU 2431 CA PHE B 361 5437 5217 4889 393 82 -114 C ATOM 2432 C PHE B 361 -0.100 14.344 -16.708 1.00 39.54 C ANISOU 2432 C PHE B 361 5273 4983 4767 438 222 -124 C ATOM 2433 O PHE B 361 -0.639 13.633 -17.556 1.00 37.81 O ANISOU 2433 O PHE B 361 4991 4722 4654 468 259 -65 O ATOM 2434 CB PHE B 361 2.266 14.006 -15.963 1.00 41.04 C ANISOU 2434 CB PHE B 361 5489 5379 4724 410 26 -51 C ATOM 2435 CG PHE B 361 2.263 12.518 -16.232 1.00 39.67 C ANISOU 2435 CG PHE B 361 5323 5209 4540 501 37 80 C ATOM 2436 CD1 PHE B 361 3.198 11.951 -17.087 1.00 38.02 C ANISOU 2436 CD1 PHE B 361 5034 5054 4356 562 -61 152 C ATOM 2437 CD2 PHE B 361 1.335 11.683 -15.621 1.00 40.67 C ANISOU 2437 CD2 PHE B 361 5557 5284 4613 515 154 122 C ATOM 2438 CE1 PHE B 361 3.207 10.578 -17.332 1.00 38.34 C ANISOU 2438 CE1 PHE B 361 5128 5064 4373 668 -54 265 C ATOM 2439 CE2 PHE B 361 1.337 10.311 -15.869 1.00 40.79 C ANISOU 2439 CE2 PHE B 361 5645 5258 4597 578 167 243 C ATOM 2440 CZ PHE B 361 2.275 9.762 -16.724 1.00 38.66 C ANISOU 2440 CZ PHE B 361 5322 5010 4358 671 58 315 C ATOM 2441 N LEU B 362 -0.713 14.748 -15.599 1.00 41.07 N ANISOU 2441 N LEU B 362 5535 5198 4871 426 306 -213 N ATOM 2442 CA LEU B 362 -2.096 14.389 -15.315 1.00 44.23 C ANISOU 2442 CA LEU B 362 5914 5600 5292 442 459 -256 C ATOM 2443 C LEU B 362 -3.033 14.871 -16.420 1.00 44.66 C ANISOU 2443 C LEU B 362 5852 5586 5531 503 483 -316 C ATOM 2444 O LEU B 362 -3.964 14.163 -16.802 1.00 49.53 O ANISOU 2444 O LEU B 362 6381 6232 6207 503 572 -304 O ATOM 2445 CB LEU B 362 -2.529 14.958 -13.965 1.00 47.42 C ANISOU 2445 CB LEU B 362 6397 6060 5560 423 545 -373 C ATOM 2446 CG LEU B 362 -1.781 14.385 -12.758 1.00 49.66 C ANISOU 2446 CG LEU B 362 6811 6429 5629 367 531 -313 C ATOM 2447 CD1 LEU B 362 -2.148 15.130 -11.484 1.00 53.71 C ANISOU 2447 CD1 LEU B 362 7409 6996 6003 340 608 -448 C ATOM 2448 CD2 LEU B 362 -2.057 12.895 -12.611 1.00 46.38 C ANISOU 2448 CD2 LEU B 362 6444 6036 5142 336 603 -185 C ATOM 2449 N LEU B 363 -2.776 16.064 -16.945 1.00 41.28 N ANISOU 2449 N LEU B 363 5441 5069 5176 546 398 -381 N ATOM 2450 CA LEU B 363 -3.597 16.601 -18.026 1.00 43.66 C ANISOU 2450 CA LEU B 363 5666 5292 5631 642 390 -431 C ATOM 2451 C LEU B 363 -3.426 15.797 -19.317 1.00 44.57 C ANISOU 2451 C LEU B 363 5689 5389 5856 628 340 -312 C ATOM 2452 O LEU B 363 -4.407 15.480 -19.990 1.00 47.29 O ANISOU 2452 O LEU B 363 5921 5752 6296 680 384 -327 O ATOM 2453 CB LEU B 363 -3.264 18.069 -18.281 1.00 46.93 C ANISOU 2453 CB LEU B 363 6201 5567 6063 684 301 -513 C ATOM 2454 CG LEU B 363 -3.905 18.674 -19.533 1.00 53.80 C ANISOU 2454 CG LEU B 363 7049 6322 7071 805 250 -538 C ATOM 2455 CD1 LEU B 363 -5.422 18.529 -19.498 1.00 55.30 C ANISOU 2455 CD1 LEU B 363 7098 6598 7316 956 346 -635 C ATOM 2456 CD2 LEU B 363 -3.506 20.139 -19.689 1.00 58.24 C ANISOU 2456 CD2 LEU B 363 7821 6696 7610 830 163 -609 C ATOM 2457 N LEU B 364 -2.183 15.470 -19.657 1.00 42.49 N ANISOU 2457 N LEU B 364 5459 5116 5569 559 249 -209 N ATOM 2458 CA LEU B 364 -1.906 14.695 -20.861 1.00 40.23 C ANISOU 2458 CA LEU B 364 5099 4816 5370 551 205 -104 C ATOM 2459 C LEU B 364 -2.492 13.287 -20.758 1.00 40.49 C ANISOU 2459 C LEU B 364 5086 4906 5393 538 296 -43 C ATOM 2460 O LEU B 364 -3.007 12.759 -21.739 1.00 41.43 O ANISOU 2460 O LEU B 364 5129 5005 5607 545 308 -11 O ATOM 2461 CB LEU B 364 -0.401 14.630 -21.127 1.00 39.03 C ANISOU 2461 CB LEU B 364 4972 4691 5168 491 99 -33 C ATOM 2462 CG LEU B 364 0.259 15.949 -21.548 1.00 42.37 C ANISOU 2462 CG LEU B 364 5452 5050 5596 434 11 -84 C ATOM 2463 CD1 LEU B 364 1.754 15.775 -21.723 1.00 43.45 C ANISOU 2463 CD1 LEU B 364 5560 5291 5656 342 -74 -35 C ATOM 2464 CD2 LEU B 364 -0.368 16.504 -22.822 1.00 40.64 C ANISOU 2464 CD2 LEU B 364 5232 4704 5506 474 -12 -92 C ATOM 2465 N LYS B 365 -2.430 12.697 -19.568 1.00 38.71 N ANISOU 2465 N LYS B 365 4933 4741 5034 503 362 -28 N ATOM 2466 CA LYS B 365 -3.012 11.377 -19.323 1.00 39.49 C ANISOU 2466 CA LYS B 365 5059 4863 5083 452 466 30 C ATOM 2467 C LYS B 365 -4.490 11.317 -19.698 1.00 37.82 C ANISOU 2467 C LYS B 365 4731 4685 4955 422 578 -49 C ATOM 2468 O LYS B 365 -4.949 10.348 -20.303 1.00 39.50 O ANISOU 2468 O LYS B 365 4918 4891 5198 360 627 -3 O ATOM 2469 CB LYS B 365 -2.851 10.980 -17.853 1.00 45.73 C ANISOU 2469 CB LYS B 365 5986 5703 5685 410 527 44 C ATOM 2470 CG LYS B 365 -1.926 9.804 -17.626 1.00 54.86 C ANISOU 2470 CG LYS B 365 7286 6835 6721 422 479 181 C ATOM 2471 CD LYS B 365 -2.069 9.263 -16.213 1.00 59.88 C ANISOU 2471 CD LYS B 365 8095 7502 7153 372 560 205 C ATOM 2472 CE LYS B 365 -3.425 8.595 -16.018 1.00 64.23 C ANISOU 2472 CE LYS B 365 8679 8046 7678 236 744 182 C ATOM 2473 NZ LYS B 365 -3.588 8.042 -14.644 1.00 67.87 N ANISOU 2473 NZ LYS B 365 9346 8530 7912 153 840 211 N ATOM 2474 N LYS B 366 -5.232 12.358 -19.332 1.00 36.30 N ANISOU 2474 N LYS B 366 4465 4543 4785 471 617 -184 N ATOM 2475 CA LYS B 366 -6.662 12.418 -19.612 1.00 38.71 C ANISOU 2475 CA LYS B 366 4610 4945 5154 477 715 -295 C ATOM 2476 C LYS B 366 -6.940 12.505 -21.109 1.00 36.89 C ANISOU 2476 C LYS B 366 4260 4679 5077 537 634 -284 C ATOM 2477 O LYS B 366 -8.037 12.189 -21.565 1.00 37.51 O ANISOU 2477 O LYS B 366 4184 4865 5203 518 699 -350 O ATOM 2478 CB LYS B 366 -7.290 13.611 -18.894 1.00 40.78 C ANISOU 2478 CB LYS B 366 4828 5271 5397 580 754 -457 C ATOM 2479 CG LYS B 366 -7.146 13.563 -17.385 1.00 45.59 C ANISOU 2479 CG LYS B 366 5549 5936 5839 512 848 -488 C ATOM 2480 CD LYS B 366 -7.411 14.922 -16.768 1.00 49.93 C ANISOU 2480 CD LYS B 366 6107 6495 6369 642 848 -644 C ATOM 2481 CE LYS B 366 -6.970 14.959 -15.316 1.00 57.42 C ANISOU 2481 CE LYS B 366 7203 7475 7139 569 908 -660 C ATOM 2482 NZ LYS B 366 -6.875 16.359 -14.820 1.00 65.00 N ANISOU 2482 NZ LYS B 366 8236 8384 8077 690 869 -796 N ATOM 2483 N LEU B 367 -5.930 12.931 -21.865 1.00 35.66 N ANISOU 2483 N LEU B 367 4170 4399 4980 592 493 -209 N ATOM 2484 CA LEU B 367 -6.066 13.147 -23.302 1.00 34.50 C ANISOU 2484 CA LEU B 367 3947 4202 4959 651 402 -191 C ATOM 2485 C LEU B 367 -5.645 11.929 -24.118 1.00 34.06 C ANISOU 2485 C LEU B 367 3897 4121 4925 560 390 -73 C ATOM 2486 O LEU B 367 -5.758 11.936 -25.341 1.00 38.65 O ANISOU 2486 O LEU B 367 4418 4673 5595 586 324 -53 O ATOM 2487 CB LEU B 367 -5.236 14.361 -23.735 1.00 31.91 C ANISOU 2487 CB LEU B 367 3714 3748 4663 732 269 -185 C ATOM 2488 CG LEU B 367 -5.582 15.717 -23.104 1.00 34.04 C ANISOU 2488 CG LEU B 367 4043 3981 4910 843 258 -307 C ATOM 2489 CD1 LEU B 367 -4.625 16.796 -23.580 1.00 37.04 C ANISOU 2489 CD1 LEU B 367 4582 4201 5292 855 134 -283 C ATOM 2490 CD2 LEU B 367 -7.012 16.104 -23.421 1.00 33.11 C ANISOU 2490 CD2 LEU B 367 3791 3935 4853 992 285 -428 C ATOM 2491 N ASP B 368 -5.158 10.894 -23.437 1.00 31.33 N ANISOU 2491 N ASP B 368 3649 3774 4481 468 449 3 N ATOM 2492 CA ASP B 368 -4.559 9.735 -24.104 1.00 33.59 C ANISOU 2492 CA ASP B 368 4000 4001 4761 418 428 116 C ATOM 2493 C ASP B 368 -5.508 9.071 -25.099 1.00 34.50 C ANISOU 2493 C ASP B 368 4023 4137 4947 352 470 100 C ATOM 2494 O ASP B 368 -5.142 8.833 -26.251 1.00 34.36 O ANISOU 2494 O ASP B 368 3993 4068 4996 369 398 148 O ATOM 2495 CB ASP B 368 -4.088 8.703 -23.069 1.00 31.39 C ANISOU 2495 CB ASP B 368 3888 3703 4335 362 489 191 C ATOM 2496 CG ASP B 368 -3.398 7.496 -23.709 1.00 39.05 C ANISOU 2496 CG ASP B 368 4971 4587 5281 361 457 301 C ATOM 2497 OD1 ASP B 368 -3.747 6.345 -23.349 1.00 36.23 O ANISOU 2497 OD1 ASP B 368 4755 4180 4830 274 548 345 O ATOM 2498 OD2 ASP B 368 -2.504 7.696 -24.565 1.00 40.07 O ANISOU 2498 OD2 ASP B 368 5066 4691 5467 442 348 338 O ATOM 2499 N SER B 369 -6.727 8.785 -24.658 1.00 33.43 N ANISOU 2499 N SER B 369 3812 4106 4786 260 592 18 N ATOM 2500 CA SER B 369 -7.705 8.129 -25.520 1.00 34.62 C ANISOU 2500 CA SER B 369 3851 4321 4981 158 641 -22 C ATOM 2501 C SER B 369 -8.050 8.983 -26.737 1.00 32.75 C ANISOU 2501 C SER B 369 3447 4123 4875 277 528 -75 C ATOM 2502 O SER B 369 -8.159 8.460 -27.850 1.00 29.28 O ANISOU 2502 O SER B 369 2976 3668 4483 234 491 -49 O ATOM 2503 CB SER B 369 -8.970 7.786 -24.736 1.00 36.46 C ANISOU 2503 CB SER B 369 3995 4719 5140 10 804 -129 C ATOM 2504 OG SER B 369 -8.749 6.642 -23.925 1.00 43.76 O ANISOU 2504 OG SER B 369 5132 5573 5922 -160 917 -55 O ATOM 2505 N LEU B 370 -8.209 10.291 -26.526 1.00 34.48 N ANISOU 2505 N LEU B 370 3594 4374 5134 432 469 -149 N ATOM 2506 CA LEU B 370 -8.481 11.218 -27.625 1.00 36.37 C ANISOU 2506 CA LEU B 370 3737 4611 5470 580 343 -188 C ATOM 2507 C LEU B 370 -7.368 11.198 -28.669 1.00 38.67 C ANISOU 2507 C LEU B 370 4142 4749 5800 592 227 -68 C ATOM 2508 O LEU B 370 -7.637 11.139 -29.866 1.00 40.81 O ANISOU 2508 O LEU B 370 4353 5026 6127 609 158 -62 O ATOM 2509 CB LEU B 370 -8.665 12.643 -27.100 1.00 33.29 C ANISOU 2509 CB LEU B 370 3345 4216 5087 761 296 -276 C ATOM 2510 CG LEU B 370 -9.004 13.679 -28.175 1.00 33.94 C ANISOU 2510 CG LEU B 370 3392 4264 5242 947 155 -314 C ATOM 2511 CD1 LEU B 370 -10.235 13.240 -28.961 1.00 32.54 C ANISOU 2511 CD1 LEU B 370 2990 4272 5101 963 157 -394 C ATOM 2512 CD2 LEU B 370 -9.209 15.066 -27.564 1.00 32.15 C ANISOU 2512 CD2 LEU B 370 3225 3991 4999 1144 115 -409 C ATOM 2513 N CYS B 371 -6.122 11.239 -28.206 1.00 33.87 N ANISOU 2513 N CYS B 371 3684 4035 5148 577 207 15 N ATOM 2514 CA CYS B 371 -4.964 11.228 -29.092 1.00 31.14 C ANISOU 2514 CA CYS B 371 3421 3592 4818 574 114 110 C ATOM 2515 C CYS B 371 -4.876 9.940 -29.922 1.00 29.79 C ANISOU 2515 C CYS B 371 3248 3417 4654 491 135 170 C ATOM 2516 O CYS B 371 -4.534 9.982 -31.099 1.00 30.37 O ANISOU 2516 O CYS B 371 3319 3455 4766 500 62 205 O ATOM 2517 CB CYS B 371 -3.681 11.428 -28.278 1.00 29.59 C ANISOU 2517 CB CYS B 371 3340 3354 4550 565 99 159 C ATOM 2518 SG CYS B 371 -3.465 13.123 -27.647 1.00 46.78 S ANISOU 2518 SG CYS B 371 5578 5486 6710 632 42 93 S ATOM 2519 N VAL B 372 -5.184 8.804 -29.304 1.00 26.52 N ANISOU 2519 N VAL B 372 2867 3025 4184 401 241 178 N ATOM 2520 CA VAL B 372 -5.215 7.530 -30.017 1.00 31.01 C ANISOU 2520 CA VAL B 372 3482 3559 4741 312 274 221 C ATOM 2521 C VAL B 372 -6.382 7.490 -31.015 1.00 30.69 C ANISOU 2521 C VAL B 372 3300 3597 4764 259 270 151 C ATOM 2522 O VAL B 372 -6.251 6.966 -32.125 1.00 29.26 O ANISOU 2522 O VAL B 372 3131 3381 4604 226 234 178 O ATOM 2523 CB VAL B 372 -5.319 6.344 -29.028 1.00 29.07 C ANISOU 2523 CB VAL B 372 3375 3282 4390 208 394 249 C ATOM 2524 CG1 VAL B 372 -5.569 5.033 -29.763 1.00 29.03 C ANISOU 2524 CG1 VAL B 372 3460 3212 4358 91 443 273 C ATOM 2525 CG2 VAL B 372 -4.060 6.262 -28.166 1.00 25.46 C ANISOU 2525 CG2 VAL B 372 3065 2759 3851 295 368 326 C ATOM 2526 N SER B 373 -7.516 8.063 -30.623 1.00 29.09 N ANISOU 2526 N SER B 373 2948 3524 4581 265 302 48 N ATOM 2527 CA SER B 373 -8.675 8.109 -31.508 1.00 33.36 C ANISOU 2527 CA SER B 373 3309 4198 5167 243 281 -41 C ATOM 2528 C SER B 373 -8.351 8.929 -32.756 1.00 31.48 C ANISOU 2528 C SER B 373 3052 3914 4997 379 126 -14 C ATOM 2529 O SER B 373 -8.778 8.590 -33.860 1.00 31.09 O ANISOU 2529 O SER B 373 2935 3911 4967 342 80 -30 O ATOM 2530 CB SER B 373 -9.899 8.686 -30.789 1.00 35.78 C ANISOU 2530 CB SER B 373 3428 4699 5470 275 335 -179 C ATOM 2531 OG SER B 373 -9.839 10.101 -30.686 1.00 38.54 O ANISOU 2531 OG SER B 373 3745 5036 5862 496 236 -212 O ATOM 2532 N PHE B 374 -7.577 9.996 -32.571 1.00 29.95 N ANISOU 2532 N PHE B 374 2940 3622 4816 513 48 25 N ATOM 2533 CA PHE B 374 -7.157 10.834 -33.685 1.00 31.16 C ANISOU 2533 CA PHE B 374 3138 3700 5002 611 -88 64 C ATOM 2534 C PHE B 374 -6.216 10.041 -34.592 1.00 29.63 C ANISOU 2534 C PHE B 374 3033 3430 4796 518 -103 156 C ATOM 2535 O PHE B 374 -6.296 10.127 -35.816 1.00 32.33 O ANISOU 2535 O PHE B 374 3366 3767 5151 527 -181 171 O ATOM 2536 CB PHE B 374 -6.485 12.113 -33.179 1.00 30.80 C ANISOU 2536 CB PHE B 374 3207 3551 4946 716 -146 81 C ATOM 2537 CG PHE B 374 -6.347 13.184 -34.223 1.00 33.22 C ANISOU 2537 CG PHE B 374 3593 3768 5260 814 -281 103 C ATOM 2538 CD1 PHE B 374 -7.463 13.840 -34.719 1.00 33.67 C ANISOU 2538 CD1 PHE B 374 3581 3875 5337 968 -363 32 C ATOM 2539 CD2 PHE B 374 -5.101 13.555 -34.694 1.00 33.01 C ANISOU 2539 CD2 PHE B 374 3720 3622 5201 755 -328 189 C ATOM 2540 CE1 PHE B 374 -7.333 14.832 -35.674 1.00 31.54 C ANISOU 2540 CE1 PHE B 374 3447 3490 5049 1072 -499 66 C ATOM 2541 CE2 PHE B 374 -4.973 14.555 -35.649 1.00 30.11 C ANISOU 2541 CE2 PHE B 374 3478 3151 4812 809 -442 217 C ATOM 2542 CZ PHE B 374 -6.087 15.186 -36.135 1.00 27.86 C ANISOU 2542 CZ PHE B 374 3174 2869 4540 974 -531 165 C ATOM 2543 N ALA B 375 -5.331 9.260 -33.986 1.00 26.31 N ANISOU 2543 N ALA B 375 2704 2959 4335 449 -31 212 N ATOM 2544 CA ALA B 375 -4.448 8.388 -34.751 1.00 23.81 C ANISOU 2544 CA ALA B 375 2466 2588 3994 396 -32 278 C ATOM 2545 C ALA B 375 -5.250 7.337 -35.511 1.00 27.59 C ANISOU 2545 C ALA B 375 2909 3097 4476 302 4 249 C ATOM 2546 O ALA B 375 -4.892 6.955 -36.621 1.00 29.92 O ANISOU 2546 O ALA B 375 3237 3364 4766 280 -33 274 O ATOM 2547 CB ALA B 375 -3.431 7.725 -33.837 1.00 25.61 C ANISOU 2547 CB ALA B 375 2797 2773 4161 394 26 328 C ATOM 2548 N TYR B 376 -6.348 6.887 -34.915 1.00 27.17 N ANISOU 2548 N TYR B 376 2789 3117 4417 224 83 184 N ATOM 2549 CA TYR B 376 -7.163 5.839 -35.513 1.00 25.59 C ANISOU 2549 CA TYR B 376 2563 2962 4198 78 134 138 C ATOM 2550 C TYR B 376 -7.833 6.293 -36.815 1.00 26.55 C ANISOU 2550 C TYR B 376 2549 3179 4360 98 31 89 C ATOM 2551 O TYR B 376 -8.328 5.475 -37.582 1.00 28.37 O ANISOU 2551 O TYR B 376 2763 3448 4568 -27 47 53 O ATOM 2552 CB TYR B 376 -8.216 5.356 -34.512 1.00 27.80 C ANISOU 2552 CB TYR B 376 2784 3339 4440 -55 256 62 C ATOM 2553 CG TYR B 376 -8.067 3.898 -34.121 1.00 30.48 C ANISOU 2553 CG TYR B 376 3320 3571 4691 -230 380 93 C ATOM 2554 CD1 TYR B 376 -7.642 3.533 -32.845 1.00 29.52 C ANISOU 2554 CD1 TYR B 376 3355 3362 4498 -242 467 142 C ATOM 2555 CD2 TYR B 376 -8.351 2.886 -35.031 1.00 29.25 C ANISOU 2555 CD2 TYR B 376 3231 3381 4501 -381 404 74 C ATOM 2556 CE1 TYR B 376 -7.512 2.190 -32.490 1.00 28.69 C ANISOU 2556 CE1 TYR B 376 3496 3119 4286 -386 571 181 C ATOM 2557 CE2 TYR B 376 -8.219 1.558 -34.690 1.00 29.10 C ANISOU 2557 CE2 TYR B 376 3458 3218 4382 -538 516 103 C ATOM 2558 CZ TYR B 376 -7.796 1.211 -33.424 1.00 28.87 C ANISOU 2558 CZ TYR B 376 3611 3081 4277 -532 596 161 C ATOM 2559 OH TYR B 376 -7.680 -0.131 -33.105 1.00 28.80 O ANISOU 2559 OH TYR B 376 3911 2890 4144 -676 699 199 O ATOM 2560 N ILE B 377 -7.828 7.597 -37.073 1.00 28.86 N ANISOU 2560 N ILE B 377 2776 3497 4693 256 -80 89 N ATOM 2561 CA ILE B 377 -8.412 8.137 -38.300 1.00 27.31 C ANISOU 2561 CA ILE B 377 2489 3376 4512 318 -204 57 C ATOM 2562 C ILE B 377 -7.632 7.645 -39.527 1.00 29.60 C ANISOU 2562 C ILE B 377 2892 3577 4776 263 -244 124 C ATOM 2563 O ILE B 377 -8.172 7.564 -40.623 1.00 33.57 O ANISOU 2563 O ILE B 377 3338 4151 5265 243 -317 93 O ATOM 2564 CB ILE B 377 -8.472 9.680 -38.239 1.00 30.08 C ANISOU 2564 CB ILE B 377 2830 3713 4886 521 -318 57 C ATOM 2565 CG1 ILE B 377 -9.430 10.100 -37.118 1.00 26.91 C ANISOU 2565 CG1 ILE B 377 2288 3435 4501 595 -275 -44 C ATOM 2566 CG2 ILE B 377 -8.927 10.291 -39.564 1.00 28.06 C ANISOU 2566 CG2 ILE B 377 2547 3496 4618 619 -470 49 C ATOM 2567 CD1 ILE B 377 -9.708 11.574 -37.064 1.00 27.65 C ANISOU 2567 CD1 ILE B 377 2388 3512 4605 829 -391 -71 C ATOM 2568 N ASN B 378 -6.371 7.276 -39.323 1.00 27.63 N ANISOU 2568 N ASN B 378 2791 3199 4508 243 -196 202 N ATOM 2569 CA ASN B 378 -5.590 6.601 -40.357 1.00 31.64 C ANISOU 2569 CA ASN B 378 3399 3646 4979 191 -200 244 C ATOM 2570 C ASN B 378 -6.241 5.330 -40.890 1.00 32.40 C ANISOU 2570 C ASN B 378 3498 3768 5046 51 -147 191 C ATOM 2571 O ASN B 378 -5.986 4.932 -42.021 1.00 37.86 O ANISOU 2571 O ASN B 378 4239 4442 5703 12 -177 195 O ATOM 2572 CB ASN B 378 -4.200 6.255 -39.828 1.00 33.13 C ANISOU 2572 CB ASN B 378 3708 3742 5139 218 -143 307 C ATOM 2573 CG ASN B 378 -3.228 7.405 -39.957 1.00 40.02 C ANISOU 2573 CG ASN B 378 4601 4600 6004 292 -209 357 C ATOM 2574 OD1 ASN B 378 -3.038 7.952 -41.049 1.00 45.33 O ANISOU 2574 OD1 ASN B 378 5289 5279 6657 287 -282 374 O ATOM 2575 ND2 ASN B 378 -2.622 7.798 -38.840 1.00 35.04 N ANISOU 2575 ND2 ASN B 378 3986 3955 5372 337 -183 377 N ATOM 2576 N CYS B 379 -7.076 4.694 -40.076 1.00 27.29 N ANISOU 2576 N CYS B 379 2811 3163 4395 -50 -58 134 N ATOM 2577 CA CYS B 379 -7.663 3.410 -40.447 1.00 30.68 C ANISOU 2577 CA CYS B 379 3288 3595 4773 -239 16 77 C ATOM 2578 C CYS B 379 -8.999 3.557 -41.179 1.00 35.37 C ANISOU 2578 C CYS B 379 3687 4385 5367 -330 -42 -27 C ATOM 2579 O CYS B 379 -9.680 2.564 -41.436 1.00 37.20 O ANISOU 2579 O CYS B 379 3927 4662 5546 -535 23 -101 O ATOM 2580 CB CYS B 379 -7.834 2.534 -39.199 1.00 30.53 C ANISOU 2580 CB CYS B 379 3374 3513 4713 -354 159 69 C ATOM 2581 SG CYS B 379 -6.298 2.339 -38.256 1.00 36.71 S ANISOU 2581 SG CYS B 379 4374 4101 5472 -205 200 183 S ATOM 2582 N CYS B 380 -9.374 4.791 -41.513 1.00 34.24 N ANISOU 2582 N CYS B 380 3383 4360 5265 -177 -169 -39 N ATOM 2583 CA CYS B 380 -10.561 5.017 -42.334 1.00 35.64 C ANISOU 2583 CA CYS B 380 3363 4751 5427 -201 -263 -138 C ATOM 2584 C CYS B 380 -10.335 6.084 -43.408 1.00 34.72 C ANISOU 2584 C CYS B 380 3243 4637 5313 -14 -438 -91 C ATOM 2585 O CYS B 380 -11.169 6.265 -44.295 1.00 35.83 O ANISOU 2585 O CYS B 380 3253 4942 5419 0 -548 -157 O ATOM 2586 CB CYS B 380 -11.758 5.409 -41.461 1.00 38.71 C ANISOU 2586 CB CYS B 380 3515 5359 5833 -189 -241 -248 C ATOM 2587 SG CYS B 380 -11.857 7.156 -41.010 1.00 40.02 S ANISOU 2587 SG CYS B 380 3584 5564 6056 139 -366 -234 S ATOM 2588 N ILE B 381 -9.199 6.769 -43.347 1.00 32.89 N ANISOU 2588 N ILE B 381 3165 4231 5098 112 -464 20 N ATOM 2589 CA ILE B 381 -8.964 7.903 -44.236 1.00 33.64 C ANISOU 2589 CA ILE B 381 3311 4299 5173 267 -618 75 C ATOM 2590 C ILE B 381 -8.645 7.505 -45.687 1.00 33.60 C ANISOU 2590 C ILE B 381 3392 4278 5098 192 -675 101 C ATOM 2591 O ILE B 381 -8.975 8.247 -46.609 1.00 37.69 O ANISOU 2591 O ILE B 381 3914 4841 5567 288 -821 113 O ATOM 2592 CB ILE B 381 -7.826 8.802 -43.691 1.00 29.85 C ANISOU 2592 CB ILE B 381 2982 3650 4711 368 -613 175 C ATOM 2593 CG1 ILE B 381 -7.819 10.165 -44.395 1.00 31.90 C ANISOU 2593 CG1 ILE B 381 3327 3863 4931 522 -771 223 C ATOM 2594 CG2 ILE B 381 -6.472 8.095 -43.764 1.00 24.46 C ANISOU 2594 CG2 ILE B 381 2441 2844 4007 262 -515 242 C ATOM 2595 CD1 ILE B 381 -9.007 11.036 -44.030 1.00 32.13 C ANISOU 2595 CD1 ILE B 381 3239 3992 4978 712 -872 154 C ATOM 2596 N ASN B 382 -8.026 6.344 -45.894 1.00 27.67 N ANISOU 2596 N ASN B 382 2731 3457 4324 39 -567 106 N ATOM 2597 CA ASN B 382 -7.659 5.914 -47.244 1.00 29.47 C ANISOU 2597 CA ASN B 382 3052 3669 4475 -34 -603 117 C ATOM 2598 C ASN B 382 -8.860 5.819 -48.198 1.00 32.49 C ANISOU 2598 C ASN B 382 3314 4225 4805 -77 -714 35 C ATOM 2599 O ASN B 382 -8.827 6.428 -49.265 1.00 35.31 O ANISOU 2599 O ASN B 382 3717 4604 5095 -13 -841 69 O ATOM 2600 CB ASN B 382 -6.906 4.572 -47.212 1.00 29.12 C ANISOU 2600 CB ASN B 382 3132 3521 4409 -164 -460 109 C ATOM 2601 CG ASN B 382 -5.563 4.669 -46.502 1.00 33.07 C ANISOU 2601 CG ASN B 382 3742 3891 4932 -88 -380 186 C ATOM 2602 OD1 ASN B 382 -5.462 5.234 -45.414 1.00 38.86 O ANISOU 2602 OD1 ASN B 382 4437 4606 5723 -12 -363 215 O ATOM 2603 ND2 ASN B 382 -4.522 4.138 -47.131 1.00 32.57 N ANISOU 2603 ND2 ASN B 382 3799 3763 4812 -103 -334 205 N ATOM 2604 N PRO B 383 -9.924 5.071 -47.828 1.00 34.24 N ANISOU 2604 N PRO B 383 3385 4590 5037 -199 -669 -78 N ATOM 2605 CA PRO B 383 -11.067 5.053 -48.754 1.00 36.11 C ANISOU 2605 CA PRO B 383 3465 5047 5208 -238 -793 -174 C ATOM 2606 C PRO B 383 -11.671 6.435 -49.029 1.00 35.50 C ANISOU 2606 C PRO B 383 3273 5094 5122 8 -985 -163 C ATOM 2607 O PRO B 383 -12.129 6.674 -50.145 1.00 39.37 O ANISOU 2607 O PRO B 383 3731 5700 5526 49 -1135 -185 O ATOM 2608 CB PRO B 383 -12.086 4.149 -48.046 1.00 41.00 C ANISOU 2608 CB PRO B 383 3915 5827 5838 -433 -690 -308 C ATOM 2609 CG PRO B 383 -11.624 4.033 -46.639 1.00 41.08 C ANISOU 2609 CG PRO B 383 3984 5701 5924 -430 -542 -266 C ATOM 2610 CD PRO B 383 -10.140 4.161 -46.687 1.00 35.96 C ANISOU 2610 CD PRO B 383 3579 4790 5293 -339 -508 -130 C ATOM 2611 N ILE B 384 -11.665 7.325 -48.043 1.00 33.20 N ANISOU 2611 N ILE B 384 2947 4767 4901 183 -989 -132 N ATOM 2612 CA ILE B 384 -12.114 8.701 -48.265 1.00 34.13 C ANISOU 2612 CA ILE B 384 3033 4937 4998 461 -1174 -113 C ATOM 2613 C ILE B 384 -11.251 9.381 -49.327 1.00 34.30 C ANISOU 2613 C ILE B 384 3313 4778 4940 537 -1281 18 C ATOM 2614 O ILE B 384 -11.761 9.997 -50.258 1.00 40.10 O ANISOU 2614 O ILE B 384 4061 5589 5585 676 -1463 22 O ATOM 2615 CB ILE B 384 -12.080 9.530 -46.968 1.00 34.77 C ANISOU 2615 CB ILE B 384 3097 4955 5161 627 -1138 -100 C ATOM 2616 CG1 ILE B 384 -13.118 9.000 -45.976 1.00 36.40 C ANISOU 2616 CG1 ILE B 384 3023 5391 5416 565 -1046 -246 C ATOM 2617 CG2 ILE B 384 -12.332 11.001 -47.262 1.00 39.05 C ANISOU 2617 CG2 ILE B 384 3713 5463 5662 936 -1330 -61 C ATOM 2618 CD1 ILE B 384 -13.159 9.758 -44.675 1.00 38.55 C ANISOU 2618 CD1 ILE B 384 3266 5627 5757 723 -1000 -254 C ATOM 2619 N ILE B 385 -9.939 9.250 -49.181 1.00 31.98 N ANISOU 2619 N ILE B 385 3223 4265 4663 441 -1165 120 N ATOM 2620 CA ILE B 385 -8.988 9.787 -50.143 1.00 34.47 C ANISOU 2620 CA ILE B 385 3782 4428 4888 443 -1221 234 C ATOM 2621 C ILE B 385 -9.224 9.212 -51.545 1.00 41.29 C ANISOU 2621 C ILE B 385 4662 5385 5641 345 -1291 211 C ATOM 2622 O ILE B 385 -9.221 9.951 -52.535 1.00 42.25 O ANISOU 2622 O ILE B 385 4922 5482 5649 427 -1436 272 O ATOM 2623 CB ILE B 385 -7.538 9.511 -49.680 1.00 33.07 C ANISOU 2623 CB ILE B 385 3745 4080 4742 322 -1057 306 C ATOM 2624 CG1 ILE B 385 -7.204 10.381 -48.463 1.00 31.53 C ANISOU 2624 CG1 ILE B 385 3582 3780 4618 427 -1026 345 C ATOM 2625 CG2 ILE B 385 -6.536 9.750 -50.801 1.00 29.12 C ANISOU 2625 CG2 ILE B 385 3451 3488 4126 246 -1072 390 C ATOM 2626 CD1 ILE B 385 -5.836 10.113 -47.875 1.00 29.74 C ANISOU 2626 CD1 ILE B 385 3442 3442 4416 321 -877 395 C ATOM 2627 N TYR B 386 -9.455 7.901 -51.619 1.00 41.81 N ANISOU 2627 N TYR B 386 4617 5545 5724 163 -1191 120 N ATOM 2628 CA TYR B 386 -9.634 7.220 -52.899 1.00 39.80 C ANISOU 2628 CA TYR B 386 4388 5374 5360 36 -1236 80 C ATOM 2629 C TYR B 386 -10.886 7.712 -53.616 1.00 41.76 C ANISOU 2629 C TYR B 386 4507 5833 5527 151 -1447 22 C ATOM 2630 O TYR B 386 -10.880 7.907 -54.833 1.00 41.41 O ANISOU 2630 O TYR B 386 4566 5816 5351 157 -1567 51 O ATOM 2631 CB TYR B 386 -9.719 5.703 -52.713 1.00 38.04 C ANISOU 2631 CB TYR B 386 4104 5186 5164 -189 -1081 -21 C ATOM 2632 CG TYR B 386 -8.538 5.065 -52.013 1.00 33.44 C ANISOU 2632 CG TYR B 386 3652 4410 4642 -262 -888 21 C ATOM 2633 CD1 TYR B 386 -7.311 5.714 -51.929 1.00 34.83 C ANISOU 2633 CD1 TYR B 386 3974 4438 4820 -179 -857 132 C ATOM 2634 CD2 TYR B 386 -8.653 3.804 -51.435 1.00 33.50 C ANISOU 2634 CD2 TYR B 386 3650 4394 4686 -417 -742 -57 C ATOM 2635 CE1 TYR B 386 -6.230 5.125 -51.285 1.00 30.91 C ANISOU 2635 CE1 TYR B 386 3561 3816 4366 -213 -698 154 C ATOM 2636 CE2 TYR B 386 -7.579 3.209 -50.792 1.00 33.79 C ANISOU 2636 CE2 TYR B 386 3823 4255 4759 -432 -588 -19 C ATOM 2637 CZ TYR B 386 -6.369 3.877 -50.721 1.00 32.55 C ANISOU 2637 CZ TYR B 386 3763 3995 4610 -312 -574 82 C ATOM 2638 OH TYR B 386 -5.297 3.301 -50.080 1.00 32.48 O ANISOU 2638 OH TYR B 386 3854 3860 4625 -295 -440 106 O ATOM 2639 N VAL B 387 -11.957 7.911 -52.855 1.00 40.34 N ANISOU 2639 N VAL B 387 4091 5826 5411 252 -1493 -67 N ATOM 2640 CA VAL B 387 -13.217 8.362 -53.430 1.00 45.98 C ANISOU 2640 CA VAL B 387 4623 6802 6045 403 -1704 -150 C ATOM 2641 C VAL B 387 -13.118 9.813 -53.903 1.00 47.53 C ANISOU 2641 C VAL B 387 4997 6900 6163 703 -1903 -36 C ATOM 2642 O VAL B 387 -13.603 10.144 -54.982 1.00 45.65 O ANISOU 2642 O VAL B 387 4785 6771 5787 805 -2096 -37 O ATOM 2643 CB VAL B 387 -14.381 8.209 -52.431 1.00 49.67 C ANISOU 2643 CB VAL B 387 4756 7526 6591 440 -1686 -300 C ATOM 2644 CG1 VAL B 387 -15.613 8.960 -52.920 1.00 51.79 C ANISOU 2644 CG1 VAL B 387 4817 8088 6774 697 -1931 -387 C ATOM 2645 CG2 VAL B 387 -14.700 6.730 -52.223 1.00 48.97 C ANISOU 2645 CG2 VAL B 387 4522 7563 6521 97 -1517 -427 C ATOM 2646 N VAL B 388 -12.476 10.671 -53.113 1.00 48.17 N ANISOU 2646 N VAL B 388 5232 6759 6311 834 -1861 62 N ATOM 2647 CA VAL B 388 -12.286 12.062 -53.524 1.00 50.40 C ANISOU 2647 CA VAL B 388 5769 6881 6499 1087 -2032 180 C ATOM 2648 C VAL B 388 -11.422 12.136 -54.787 1.00 54.37 C ANISOU 2648 C VAL B 388 6571 7232 6856 967 -2065 301 C ATOM 2649 O VAL B 388 -11.776 12.821 -55.747 1.00 57.28 O ANISOU 2649 O VAL B 388 7087 7606 7070 1123 -2268 350 O ATOM 2650 CB VAL B 388 -11.650 12.911 -52.409 1.00 44.40 C ANISOU 2650 CB VAL B 388 5154 5888 5828 1187 -1954 255 C ATOM 2651 CG1 VAL B 388 -11.245 14.277 -52.939 1.00 45.59 C ANISOU 2651 CG1 VAL B 388 5670 5801 5850 1370 -2103 393 C ATOM 2652 CG2 VAL B 388 -12.617 13.060 -51.250 1.00 44.88 C ANISOU 2652 CG2 VAL B 388 4944 6111 5999 1361 -1953 133 C ATOM 2653 N ALA B 389 -10.307 11.411 -54.791 1.00 51.57 N ANISOU 2653 N ALA B 389 6304 6757 6533 702 -1868 340 N ATOM 2654 CA ALA B 389 -9.430 11.362 -55.958 1.00 48.65 C ANISOU 2654 CA ALA B 389 6183 6282 6020 555 -1861 429 C ATOM 2655 C ALA B 389 -10.161 10.770 -57.154 1.00 55.40 C ANISOU 2655 C ALA B 389 6963 7336 6752 511 -1981 362 C ATOM 2656 O ALA B 389 -9.905 11.141 -58.299 1.00 58.35 O ANISOU 2656 O ALA B 389 7556 7664 6951 500 -2082 438 O ATOM 2657 CB ALA B 389 -8.183 10.560 -55.655 1.00 42.51 C ANISOU 2657 CB ALA B 389 5442 5405 5306 313 -1621 441 C ATOM 2658 N GLY B 390 -11.073 9.846 -56.877 1.00 56.97 N ANISOU 2658 N GLY B 390 6861 7761 7024 460 -1966 214 N ATOM 2659 CA GLY B 390 -11.896 9.249 -57.910 1.00 56.21 C ANISOU 2659 CA GLY B 390 6650 7896 6810 399 -2086 119 C ATOM 2660 C GLY B 390 -12.877 10.234 -58.518 1.00 60.33 C ANISOU 2660 C GLY B 390 7162 8559 7202 681 -2373 127 C ATOM 2661 O GLY B 390 -13.140 10.183 -59.719 1.00 61.62 O ANISOU 2661 O GLY B 390 7397 8821 7193 670 -2517 128 O ATOM 2662 N GLN B 391 -13.415 11.131 -57.692 1.00 61.59 N ANISOU 2662 N GLN B 391 7244 8727 7430 956 -2463 129 N ATOM 2663 CA GLN B 391 -14.378 12.130 -58.159 1.00 65.75 C ANISOU 2663 CA GLN B 391 7769 9383 7830 1305 -2752 128 C ATOM 2664 C GLN B 391 -13.783 13.006 -59.256 1.00 66.53 C ANISOU 2664 C GLN B 391 8294 9254 7728 1390 -2888 303 C ATOM 2665 O GLN B 391 -14.494 13.457 -60.152 1.00 70.94 O ANISOU 2665 O GLN B 391 8889 9924 8141 1528 -3023 312 O ATOM 2666 CB GLN B 391 -14.864 13.014 -57.003 1.00 68.73 C ANISOU 2666 CB GLN B 391 8062 9727 8324 1562 -2727 117 C ATOM 2667 CG GLN B 391 -15.583 12.283 -55.869 1.00 72.64 C ANISOU 2667 CG GLN B 391 8142 10471 8988 1499 -2605 -58 C ATOM 2668 CD GLN B 391 -16.901 11.660 -56.288 1.00 83.07 C ANISOU 2668 CD GLN B 391 9113 12189 10263 1453 -2660 -223 C ATOM 2669 OE1 GLN B 391 -16.933 10.692 -57.049 1.00 87.99 O ANISOU 2669 OE1 GLN B 391 9649 12966 10816 1224 -2684 -291 O ATOM 2670 NE2 GLN B 391 -18.001 12.209 -55.782 1.00 86.68 N ANISOU 2670 NE2 GLN B 391 9375 12811 10748 1656 -2675 -304 N ATOM 2671 N GLY B 392 -12.474 13.234 -59.185 1.00 77.72 N ANISOU 2671 N GLY B 392 11767 9616 8147 1495 1340 2120 N ATOM 2672 CA GLY B 392 -11.780 14.046 -60.168 1.00 80.22 C ANISOU 2672 CA GLY B 392 12605 9871 8004 1634 1788 2101 C ATOM 2673 C GLY B 392 -11.378 13.279 -61.416 1.00 85.53 C ANISOU 2673 C GLY B 392 12981 10918 8598 1766 1299 1823 C ATOM 2674 O GLY B 392 -10.511 13.720 -62.171 1.00 91.29 O ANISOU 2674 O GLY B 392 14097 11563 9026 1721 1603 1671 O ATOM 2675 N PHE B 393 -12.006 12.127 -61.634 1.00 84.69 N ANISOU 2675 N PHE B 393 12226 11197 8755 1882 601 1725 N ATOM 2676 CA PHE B 393 -11.747 11.324 -62.824 1.00 84.36 C ANISOU 2676 CA PHE B 393 11900 11517 8638 1971 152 1463 C ATOM 2677 C PHE B 393 -12.887 11.460 -63.826 1.00 87.99 C ANISOU 2677 C PHE B 393 12227 12414 8793 2620 -38 1699 C ATOM 2678 O PHE B 393 -12.991 12.465 -64.531 1.00 93.66 O ANISOU 2678 O PHE B 393 13419 13113 9054 3088 357 1961 O ATOM 2679 CB PHE B 393 -11.544 9.853 -62.452 1.00 82.45 C ANISOU 2679 CB PHE B 393 11065 11424 8838 1574 -410 1119 C ATOM 2680 N LYS B 399 -18.205 5.559 -62.480 1.00 70.17 N ANISOU 2680 N LYS B 399 6497 12157 8006 1880 -2384 517 N ATOM 2681 CA LYS B 399 -19.629 5.344 -62.255 1.00 78.95 C ANISOU 2681 CA LYS B 399 7084 13752 9160 1976 -2537 464 C ATOM 2682 C LYS B 399 -19.909 4.974 -60.800 1.00 78.92 C ANISOU 2682 C LYS B 399 7091 13206 9688 1668 -2386 404 C ATOM 2683 O LYS B 399 -19.914 5.836 -59.921 1.00 78.32 O ANISOU 2683 O LYS B 399 7332 12679 9748 1846 -2116 795 O ATOM 2684 CB LYS B 399 -20.161 4.254 -63.189 1.00 83.91 C ANISOU 2684 CB LYS B 399 7159 15104 9619 1720 -2876 -43 C ATOM 2685 N SER B 400 -20.135 3.688 -60.546 1.00 80.03 N ANISOU 2685 N SER B 400 6949 13351 10107 1188 -2494 -95 N ATOM 2686 CA SER B 400 -20.428 3.220 -59.194 1.00 77.96 C ANISOU 2686 CA SER B 400 6736 12550 10335 900 -2325 -201 C ATOM 2687 C SER B 400 -19.215 3.356 -58.278 1.00 68.94 C ANISOU 2687 C SER B 400 6151 10596 9448 764 -2095 -25 C ATOM 2688 O SER B 400 -18.121 3.697 -58.723 1.00 65.13 O ANISOU 2688 O SER B 400 5962 10004 8781 823 -2068 101 O ATOM 2689 CB SER B 400 -20.906 1.764 -59.217 1.00 81.91 C ANISOU 2689 CB SER B 400 6899 13207 11016 412 -2380 -824 C ATOM 2690 OG SER B 400 -19.906 0.894 -59.719 1.00 79.30 O ANISOU 2690 OG SER B 400 6752 12722 10654 120 -2364 -1115 O ATOM 2691 N LEU B 401 -19.423 3.088 -56.994 1.00 66.43 N ANISOU 2691 N LEU B 401 5956 9757 9525 574 -1925 -38 N ATOM 2692 CA LEU B 401 -18.361 3.191 -56.000 1.00 61.72 C ANISOU 2692 CA LEU B 401 5821 8500 9132 440 -1728 119 C ATOM 2693 C LEU B 401 -17.244 2.149 -56.194 1.00 59.74 C ANISOU 2693 C LEU B 401 5676 8108 8913 204 -1752 -173 C ATOM 2694 O LEU B 401 -16.063 2.508 -56.164 1.00 55.66 O ANISOU 2694 O LEU B 401 5428 7429 8290 224 -1697 -11 O ATOM 2695 CB LEU B 401 -18.953 3.080 -54.591 1.00 64.32 C ANISOU 2695 CB LEU B 401 6254 8335 9851 307 -1546 159 C ATOM 2696 CG LEU B 401 -18.151 3.688 -53.440 1.00 65.42 C ANISOU 2696 CG LEU B 401 6854 7896 10108 245 -1323 469 C ATOM 2697 CD1 LEU B 401 -18.007 5.191 -53.632 1.00 65.66 C ANISOU 2697 CD1 LEU B 401 7108 7971 9869 479 -1169 922 C ATOM 2698 CD2 LEU B 401 -18.820 3.377 -52.112 1.00 65.47 C ANISOU 2698 CD2 LEU B 401 6960 7411 10504 87 -1159 442 C ATOM 2699 N PRO B 402 -17.596 0.859 -56.391 1.00 60.90 N ANISOU 2699 N PRO B 402 5628 8326 9185 -29 -1768 -615 N ATOM 2700 CA PRO B 402 -16.491 -0.085 -56.603 1.00 58.42 C ANISOU 2700 CA PRO B 402 5483 7843 8873 -172 -1699 -816 C ATOM 2701 C PRO B 402 -15.775 0.138 -57.931 1.00 57.07 C ANISOU 2701 C PRO B 402 5269 8054 8362 -91 -1848 -809 C ATOM 2702 O PRO B 402 -14.565 -0.062 -58.020 1.00 55.37 O ANISOU 2702 O PRO B 402 5259 7674 8107 -90 -1790 -767 O ATOM 2703 CB PRO B 402 -17.184 -1.454 -56.578 1.00 61.01 C ANISOU 2703 CB PRO B 402 5685 8130 9367 -459 -1551 -1305 C ATOM 2704 CG PRO B 402 -18.587 -1.177 -56.944 1.00 64.25 C ANISOU 2704 CG PRO B 402 5693 9000 9718 -503 -1679 -1449 C ATOM 2705 CD PRO B 402 -18.896 0.163 -56.345 1.00 62.71 C ANISOU 2705 CD PRO B 402 5533 8739 9554 -208 -1755 -973 C ATOM 2706 N SER B 403 -16.518 0.556 -58.947 1.00 60.27 N ANISOU 2706 N SER B 403 5398 8996 8504 3 -2034 -845 N ATOM 2707 CA SER B 403 -15.935 0.821 -60.253 1.00 63.39 C ANISOU 2707 CA SER B 403 5791 9747 8547 101 -2169 -837 C ATOM 2708 C SER B 403 -15.020 2.040 -60.211 1.00 61.40 C ANISOU 2708 C SER B 403 5856 9327 8146 354 -2117 -430 C ATOM 2709 O SER B 403 -14.057 2.128 -60.970 1.00 63.53 O ANISOU 2709 O SER B 403 6278 9635 8226 370 -2120 -439 O ATOM 2710 CB SER B 403 -17.031 1.022 -61.294 1.00 71.00 C ANISOU 2710 CB SER B 403 6368 11410 9199 198 -2387 -948 C ATOM 2711 OG SER B 403 -16.465 1.216 -62.573 1.00 76.89 O ANISOU 2711 OG SER B 403 7158 12472 9584 290 -2506 -955 O ATOM 2712 N LEU B 404 -15.323 2.975 -59.317 1.00 59.05 N ANISOU 2712 N LEU B 404 5691 8817 7929 505 -2005 -106 N ATOM 2713 CA LEU B 404 -14.512 4.177 -59.169 1.00 55.93 C ANISOU 2713 CA LEU B 404 5656 8228 7368 652 -1827 232 C ATOM 2714 C LEU B 404 -13.195 3.857 -58.476 1.00 50.92 C ANISOU 2714 C LEU B 404 5233 7234 6880 418 -1704 182 C ATOM 2715 O LEU B 404 -12.147 4.397 -58.829 1.00 51.08 O ANISOU 2715 O LEU B 404 5465 7242 6700 411 -1599 243 O ATOM 2716 CB LEU B 404 -15.272 5.247 -58.385 1.00 61.53 C ANISOU 2716 CB LEU B 404 6493 8784 8101 833 -1644 589 C ATOM 2717 CG LEU B 404 -14.561 6.595 -58.280 1.00 65.76 C ANISOU 2717 CG LEU B 404 7482 9107 8397 939 -1317 915 C ATOM 2718 CD1 LEU B 404 -14.270 7.141 -59.670 1.00 70.25 C ANISOU 2718 CD1 LEU B 404 8161 9989 8540 1206 -1312 958 C ATOM 2719 CD2 LEU B 404 -15.392 7.582 -57.474 1.00 66.95 C ANISOU 2719 CD2 LEU B 404 7815 9043 8582 1102 -1039 1282 C ATOM 2720 N LEU B 405 -13.260 2.973 -57.486 1.00 49.30 N ANISOU 2720 N LEU B 405 4964 6773 6995 247 -1692 60 N ATOM 2721 CA LEU B 405 -12.070 2.533 -56.772 1.00 48.45 C ANISOU 2721 CA LEU B 405 4985 6436 6988 112 -1601 32 C ATOM 2722 C LEU B 405 -11.150 1.739 -57.692 1.00 50.90 C ANISOU 2722 C LEU B 405 5236 6905 7199 91 -1658 -182 C ATOM 2723 O LEU B 405 -9.929 1.874 -57.617 1.00 50.26 O ANISOU 2723 O LEU B 405 5242 6831 7022 64 -1592 -144 O ATOM 2724 CB LEU B 405 -12.453 1.695 -55.550 1.00 51.62 C ANISOU 2724 CB LEU B 405 5378 6521 7714 29 -1540 -31 C ATOM 2725 CG LEU B 405 -13.194 2.407 -54.416 1.00 51.28 C ANISOU 2725 CG LEU B 405 5450 6214 7821 5 -1437 188 C ATOM 2726 CD1 LEU B 405 -13.499 1.436 -53.295 1.00 53.33 C ANISOU 2726 CD1 LEU B 405 5752 6122 8390 -68 -1356 78 C ATOM 2727 CD2 LEU B 405 -12.385 3.577 -53.897 1.00 50.37 C ANISOU 2727 CD2 LEU B 405 5568 6041 7530 -59 -1291 453 C ATOM 2728 N ARG B 406 -11.745 0.918 -58.558 1.00 54.60 N ANISOU 2728 N ARG B 406 5542 7532 7672 68 -1751 -427 N ATOM 2729 CA ARG B 406 -10.994 0.129 -59.535 1.00 57.53 C ANISOU 2729 CA ARG B 406 5900 8013 7947 16 -1749 -635 C ATOM 2730 C ARG B 406 -10.109 1.008 -60.407 1.00 57.80 C ANISOU 2730 C ARG B 406 6044 8217 7700 88 -1779 -534 C ATOM 2731 O ARG B 406 -8.942 0.696 -60.630 1.00 58.69 O ANISOU 2731 O ARG B 406 6223 8296 7781 62 -1702 -580 O ATOM 2732 CB ARG B 406 -11.942 -0.688 -60.424 1.00 62.26 C ANISOU 2732 CB ARG B 406 6320 8822 8513 -109 -1810 -943 C ATOM 2733 CG ARG B 406 -12.639 -1.824 -59.703 1.00 67.15 C ANISOU 2733 CG ARG B 406 6894 9223 9396 -271 -1650 -1175 C ATOM 2734 CD ARG B 406 -13.436 -2.724 -60.634 1.00 74.15 C ANISOU 2734 CD ARG B 406 7614 10364 10197 -529 -1617 -1584 C ATOM 2735 NE ARG B 406 -13.904 -3.917 -59.929 1.00 76.94 N ANISOU 2735 NE ARG B 406 8041 10405 10790 -737 -1306 -1868 N ATOM 2736 CZ ARG B 406 -15.087 -4.021 -59.329 1.00 76.69 C ANISOU 2736 CZ ARG B 406 7867 10372 10901 -865 -1270 -2027 C ATOM 2737 NH1 ARG B 406 -15.938 -3.004 -59.353 1.00 77.16 N ANISOU 2737 NH1 ARG B 406 7653 10775 10888 -763 -1556 -1885 N ATOM 2738 NH2 ARG B 406 -15.421 -5.146 -58.708 1.00 76.24 N ANISOU 2738 NH2 ARG B 406 7971 9952 11046 -1072 -889 -2326 N ATOM 2739 N ASN B 407 -10.670 2.108 -60.897 1.00 58.65 N ANISOU 2739 N ASN B 407 6193 8502 7590 212 -1841 -392 N ATOM 2740 CA ASN B 407 -9.934 3.013 -61.772 1.00 61.44 C ANISOU 2740 CA ASN B 407 6747 8957 7639 298 -1781 -314 C ATOM 2741 C ASN B 407 -8.770 3.692 -61.063 1.00 57.34 C ANISOU 2741 C ASN B 407 6429 8258 7100 213 -1570 -199 C ATOM 2742 O ASN B 407 -7.728 3.949 -61.664 1.00 59.85 O ANISOU 2742 O ASN B 407 6876 8611 7252 162 -1470 -274 O ATOM 2743 CB ASN B 407 -10.875 4.073 -62.349 1.00 66.40 C ANISOU 2743 CB ASN B 407 7445 9791 7992 550 -1803 -130 C ATOM 2744 N VAL B 408 -8.958 3.976 -59.779 1.00 55.18 N ANISOU 2744 N VAL B 408 6170 7818 6976 153 -1485 -51 N ATOM 2745 CA VAL B 408 -7.971 4.701 -58.992 1.00 55.40 C ANISOU 2745 CA VAL B 408 6353 7770 6927 -9 -1266 29 C ATOM 2746 C VAL B 408 -6.863 3.788 -58.471 1.00 54.61 C ANISOU 2746 C VAL B 408 6070 7731 6948 -118 -1307 -99 C ATOM 2747 O VAL B 408 -5.691 4.166 -58.461 1.00 56.39 O ANISOU 2747 O VAL B 408 6316 8100 7008 -253 -1178 -163 O ATOM 2748 CB VAL B 408 -8.646 5.421 -57.803 1.00 54.74 C ANISOU 2748 CB VAL B 408 6389 7495 6915 -62 -1125 251 C ATOM 2749 CG1 VAL B 408 -7.611 5.943 -56.814 1.00 55.53 C ANISOU 2749 CG1 VAL B 408 6587 7583 6930 -340 -907 266 C ATOM 2750 CG2 VAL B 408 -9.535 6.549 -58.303 1.00 56.49 C ANISOU 2750 CG2 VAL B 408 6852 7674 6937 118 -962 454 C ATOM 2751 N LEU B 409 -7.236 2.577 -58.069 1.00 55.03 N ANISOU 2751 N LEU B 409 5950 7702 7256 -37 -1439 -148 N ATOM 2752 CA LEU B 409 -6.339 1.705 -57.314 1.00 56.86 C ANISOU 2752 CA LEU B 409 6047 7970 7587 -12 -1420 -171 C ATOM 2753 C LEU B 409 -5.650 0.621 -58.143 1.00 61.44 C ANISOU 2753 C LEU B 409 6533 8628 8184 100 -1420 -320 C ATOM 2754 O LEU B 409 -4.665 0.029 -57.697 1.00 62.24 O ANISOU 2754 O LEU B 409 6519 8846 8283 204 -1357 -298 O ATOM 2755 CB LEU B 409 -7.110 1.041 -56.168 1.00 52.32 C ANISOU 2755 CB LEU B 409 5459 7158 7261 55 -1429 -99 C ATOM 2756 CG LEU B 409 -7.807 1.976 -55.176 1.00 49.65 C ANISOU 2756 CG LEU B 409 5236 6670 6957 -61 -1390 70 C ATOM 2757 CD1 LEU B 409 -8.563 1.167 -54.133 1.00 48.38 C ANISOU 2757 CD1 LEU B 409 5094 6218 7071 10 -1379 97 C ATOM 2758 CD2 LEU B 409 -6.814 2.942 -54.521 1.00 48.56 C ANISOU 2758 CD2 LEU B 409 5136 6721 6593 -247 -1277 162 C ATOM 2759 N THR B 410 -6.162 0.352 -59.338 1.00 62.91 N ANISOU 2759 N THR B 410 6764 8782 8357 96 -1465 -455 N ATOM 2760 CA THR B 410 -5.640 -0.756 -60.132 1.00 66.24 C ANISOU 2760 CA THR B 410 7163 9195 8810 151 -1393 -602 C ATOM 2761 C THR B 410 -5.135 -0.330 -61.510 1.00 70.36 C ANISOU 2761 C THR B 410 7755 9844 9135 81 -1405 -714 C ATOM 2762 O THR B 410 -5.168 -1.118 -62.456 1.00 71.51 O ANISOU 2762 O THR B 410 7941 9943 9288 54 -1360 -866 O ATOM 2763 CB THR B 410 -6.707 -1.856 -60.317 1.00 66.35 C ANISOU 2763 CB THR B 410 7202 9021 8989 127 -1347 -751 C ATOM 2764 OG1 THR B 410 -7.816 -1.336 -61.061 1.00 64.17 O ANISOU 2764 OG1 THR B 410 6909 8850 8622 9 -1504 -845 O ATOM 2765 CG2 THR B 410 -7.197 -2.352 -58.965 1.00 66.92 C ANISOU 2765 CG2 THR B 410 7280 8881 9266 205 -1263 -674 C ATOM 2766 N GLU B 411 -4.673 0.912 -61.623 1.00 73.94 N ANISOU 2766 N GLU B 411 8279 10422 9393 18 -1401 -661 N ATOM 2767 CA GLU B 411 -4.050 1.373 -62.860 1.00 77.75 C ANISOU 2767 CA GLU B 411 8897 10972 9672 -36 -1345 -778 C ATOM 2768 C GLU B 411 -2.665 0.751 -62.978 1.00 80.71 C ANISOU 2768 C GLU B 411 9163 11424 10079 -31 -1221 -857 C ATOM 2769 O GLU B 411 -2.019 0.464 -61.968 1.00 80.43 O ANISOU 2769 O GLU B 411 8934 11512 10113 30 -1177 -776 O ATOM 2770 CB GLU B 411 -3.960 2.901 -62.903 1.00 76.25 C ANISOU 2770 CB GLU B 411 8910 10825 9235 -110 -1241 -724 C ATOM 2771 N GLU B 412 -2.217 0.528 -64.209 1.00 81.89 N ANISOU 2771 N GLU B 412 9426 11534 10156 -64 -1158 -999 N ATOM 2772 CA GLU B 412 -0.905 -0.066 -64.440 1.00 84.22 C ANISOU 2772 CA GLU B 412 9617 11895 10487 -32 -1003 -1063 C ATOM 2773 C GLU B 412 0.072 1.003 -64.915 1.00 87.90 C ANISOU 2773 C GLU B 412 10163 12490 10745 -183 -881 -1192 C ATOM 2774 O GLU B 412 -0.318 1.933 -65.624 1.00 89.40 O ANISOU 2774 O GLU B 412 10634 12582 10753 -281 -861 -1264 O ATOM 2775 CB GLU B 412 -0.995 -1.205 -65.459 1.00 83.20 C ANISOU 2775 CB GLU B 412 9599 11563 10451 -11 -920 -1155 C ATOM 2776 N SER B 413 1.337 0.878 -64.519 1.00 88.33 N ANISOU 2776 N SER B 413 9975 12794 10791 -181 -758 -1230 N ATOM 2777 CA SER B 413 2.354 1.844 -64.932 1.00 86.62 C ANISOU 2777 CA SER B 413 9805 12737 10369 -402 -572 -1439 C ATOM 2778 C SER B 413 3.135 1.366 -66.153 1.00 87.94 C ANISOU 2778 C SER B 413 10064 12781 10567 -400 -428 -1592 C ATOM 2779 O SER B 413 3.707 2.173 -66.890 1.00 89.82 O ANISOU 2779 O SER B 413 10509 12979 10642 -604 -242 -1815 O ATOM 2780 CB SER B 413 3.325 2.140 -63.788 1.00 85.46 C ANISOU 2780 CB SER B 413 9267 13079 10126 -486 -511 -1466 C ATOM 2781 OG SER B 413 4.313 3.064 -64.214 1.00 85.07 O ANISOU 2781 OG SER B 413 9255 13212 9857 -791 -263 -1757 O TER 2782 SER B 413 HETATM 2783 C ACE L 0 3.009 2.665 -14.095 1.00 46.95 C HETATM 2784 O ACE L 0 3.110 2.623 -15.320 1.00 47.77 O HETATM 2785 CH3 ACE L 0 4.058 3.286 -13.222 1.00 46.78 C ATOM 2786 N PHE L 1 1.969 2.137 -13.461 1.00 44.58 N ATOM 2787 CA PHE L 1 0.853 1.616 -14.234 1.00 39.65 C ATOM 2788 C PHE L 1 0.017 2.758 -14.790 1.00 39.98 C ATOM 2789 O PHE L 1 -0.151 3.789 -14.143 1.00 44.47 O ATOM 2790 CB PHE L 1 -0.040 0.695 -13.399 1.00 36.02 C ATOM 2791 CG PHE L 1 -1.294 0.288 -14.110 1.00 38.39 C ATOM 2792 CD1 PHE L 1 -1.269 -0.712 -15.071 1.00 36.88 C ATOM 2793 CD2 PHE L 1 -2.490 0.935 -13.857 1.00 36.77 C ATOM 2794 CE1 PHE L 1 -2.413 -1.071 -15.741 1.00 34.68 C ATOM 2795 CE2 PHE L 1 -3.638 0.577 -14.528 1.00 36.29 C ATOM 2796 CZ PHE L 1 -3.600 -0.429 -15.468 1.00 36.39 C HETATM 2797 N ORN L 2 -0.532 2.549 -15.979 1.00 37.35 N HETATM 2798 CA ORN L 2 -1.305 3.576 -16.653 1.00 37.26 C HETATM 2799 CB ORN L 2 -0.351 4.498 -17.414 1.00 39.50 C HETATM 2800 CG ORN L 2 -0.894 5.879 -17.702 1.00 42.84 C HETATM 2801 CD ORN L 2 0.120 6.804 -18.366 1.00 42.65 C HETATM 2802 NE ORN L 2 0.465 6.359 -19.715 1.00 37.45 N HETATM 2803 C ORN L 2 -2.297 2.922 -17.613 1.00 36.69 C HETATM 2804 O ORN L 2 -1.892 2.252 -18.564 1.00 39.20 O ATOM 2805 N PRO L 3 -3.603 3.113 -17.368 1.00 38.74 N ATOM 2806 CA PRO L 3 -4.646 2.539 -18.231 1.00 39.90 C ATOM 2807 C PRO L 3 -4.565 3.047 -19.669 1.00 38.80 C ATOM 2808 O PRO L 3 -4.103 4.165 -19.889 1.00 38.33 O ATOM 2809 CB PRO L 3 -5.952 2.997 -17.565 1.00 43.07 C ATOM 2810 CG PRO L 3 -5.576 4.185 -16.742 1.00 42.23 C ATOM 2811 CD PRO L 3 -4.173 3.919 -16.272 1.00 40.92 C HETATM 2812 C1 ZAL L 4 -7.328 1.674 -22.266 1.00 38.83 C HETATM 2813 C2 ZAL L 4 -7.844 3.108 -22.203 1.00 42.72 C HETATM 2814 C3 ZAL L 4 -9.344 3.263 -22.035 1.00 42.93 C HETATM 2815 C4 ZAL L 4 -10.138 2.028 -22.417 1.00 45.03 C HETATM 2816 C5 ZAL L 4 -9.492 1.276 -23.562 1.00 44.29 C HETATM 2817 C6 ZAL L 4 -8.130 0.746 -23.172 1.00 41.42 C HETATM 2818 N ZAL L 4 -5.000 2.233 -20.626 1.00 34.05 N HETATM 2819 CA ZAL L 4 -4.996 2.611 -21.998 1.00 33.21 C HETATM 2820 CB ZAL L 4 -5.896 1.695 -22.801 1.00 30.84 C HETATM 2821 C ZAL L 4 -3.616 2.467 -22.589 1.00 33.57 C HETATM 2822 O ZAL L 4 -2.969 1.393 -22.450 1.00 37.71 O ATOM 2823 N TRP L 5 -3.144 3.517 -23.249 1.00 27.50 N ATOM 2824 CA TRP L 5 -1.927 3.426 -24.051 1.00 30.48 C ATOM 2825 C TRP L 5 -0.727 4.120 -23.409 1.00 33.94 C ATOM 2826 O TRP L 5 0.395 3.631 -23.493 1.00 33.48 O ATOM 2827 CB TRP L 5 -2.189 3.999 -25.449 1.00 31.37 C ATOM 2828 CG TRP L 5 -3.140 3.148 -26.247 1.00 34.33 C ATOM 2829 CD1 TRP L 5 -2.814 2.097 -27.053 1.00 31.96 C ATOM 2830 CD2 TRP L 5 -4.567 3.263 -26.298 1.00 34.84 C ATOM 2831 NE1 TRP L 5 -3.946 1.552 -27.605 1.00 32.06 N ATOM 2832 CE2 TRP L 5 -5.037 2.249 -27.161 1.00 35.66 C ATOM 2833 CE3 TRP L 5 -5.495 4.125 -25.703 1.00 32.93 C ATOM 2834 CZ2 TRP L 5 -6.388 2.075 -27.446 1.00 33.65 C ATOM 2835 CZ3 TRP L 5 -6.834 3.952 -25.985 1.00 32.94 C ATOM 2836 CH2 TRP L 5 -7.270 2.932 -26.850 1.00 35.55 C ATOM 2837 N ARG L 6 -0.960 5.265 -22.780 1.00 35.85 N ATOM 2838 CA ARG L 6 0.110 5.964 -22.076 1.00 37.87 C ATOM 2839 C ARG L 6 -0.376 6.499 -20.733 1.00 37.78 C ATOM 2840 O ARG L 6 -1.480 7.040 -20.627 1.00 39.58 O ATOM 2841 CB ARG L 6 0.675 7.114 -22.925 1.00 39.14 C ATOM 2842 CG ARG L 6 1.555 6.678 -24.101 1.00 42.90 C ATOM 2843 CD ARG L 6 0.728 6.459 -25.367 1.00 40.60 C ATOM 2844 NE ARG L 6 -0.170 7.588 -25.618 1.00 38.57 N ATOM 2845 CZ ARG L 6 0.133 8.635 -26.382 1.00 39.84 C ATOM 2846 NH1 ARG L 6 -0.745 9.616 -26.542 1.00 40.84 N ATOM 2847 NH2 ARG L 6 1.311 8.696 -26.993 1.00 34.27 N TER 2848 ARG L 6 HETATM 2849 C10 EFD B 501 15.024 4.162 -48.197 1.00 34.77 C HETATM 2850 C11 EFD B 501 13.277 3.758 -46.663 1.00 36.06 C HETATM 2851 C01 EFD B 501 13.046 6.072 -50.778 1.00 38.20 C HETATM 2852 C02 EFD B 501 13.511 6.839 -51.838 1.00 34.20 C HETATM 2853 C03 EFD B 501 14.424 7.859 -51.611 1.00 35.91 C HETATM 2854 C04 EFD B 501 14.870 8.108 -50.322 1.00 36.81 C HETATM 2855 C05 EFD B 501 14.406 7.338 -49.262 1.00 39.39 C HETATM 2856 C06 EFD B 501 13.497 6.311 -49.490 1.00 37.49 C HETATM 2857 C07 EFD B 501 12.984 5.484 -48.325 1.00 37.90 C HETATM 2858 O08 EFD B 501 11.877 5.735 -47.882 1.00 37.79 O HETATM 2859 N09 EFD B 501 13.770 4.443 -47.736 1.00 35.32 N HETATM 2860 C12 EFD B 501 15.927 4.107 -47.134 1.00 35.18 C HETATM 2861 C13 EFD B 501 15.447 3.378 -46.071 1.00 38.10 C HETATM 2862 C14 EFD B 501 14.240 3.882 -45.657 1.00 38.64 C HETATM 2863 C15 EFD B 501 12.791 2.336 -46.997 1.00 34.66 C HETATM 2864 C16 EFD B 501 11.947 2.150 -48.085 1.00 36.95 C HETATM 2865 C17 EFD B 501 11.468 0.894 -48.423 1.00 37.72 C HETATM 2866 C18 EFD B 501 11.805 -0.222 -47.676 1.00 37.42 C HETATM 2867 C19 EFD B 501 12.640 -0.062 -46.578 1.00 35.10 C HETATM 2868 C20 EFD B 501 13.125 1.205 -46.245 1.00 33.48 C HETATM 2869 C21 EFD B 501 12.048 4.965 -51.023 1.00 35.62 C HETATM 2870 F22 EFD B 501 14.843 7.590 -48.020 1.00 41.42 F HETATM 2871 C23 EFD B 501 13.787 3.340 -44.308 1.00 37.77 C HETATM 2872 N24 EFD B 501 11.282 -1.496 -48.058 1.00 34.51 N HETATM 2873 C25 EFD B 501 11.452 -2.469 -47.031 1.00 38.10 C HETATM 2874 C26 EFD B 501 11.238 -3.845 -47.633 1.00 40.79 C HETATM 2875 C27 EFD B 501 10.153 -4.555 -46.850 1.00 38.57 C HETATM 2876 C28 EFD B 501 9.835 -3.685 -45.655 1.00 40.67 C HETATM 2877 C29 EFD B 501 10.400 -2.310 -45.953 1.00 39.33 C HETATM 2878 O30 EFD B 501 14.593 2.828 -43.550 1.00 36.74 O HETATM 2879 N31 EFD B 501 12.406 3.438 -43.977 1.00 37.07 N HETATM 2880 C32 EFD B 501 11.791 2.987 -42.773 1.00 38.97 C HETATM 2881 C33 EFD B 501 12.375 2.036 -41.947 1.00 38.55 C HETATM 2882 C34 EFD B 501 11.740 1.616 -40.785 1.00 38.69 C HETATM 2883 C35 EFD B 501 10.495 2.147 -40.453 1.00 36.61 C HETATM 2884 C36 EFD B 501 9.907 3.093 -41.280 1.00 36.97 C HETATM 2885 C37 EFD B 501 10.549 3.509 -42.436 1.00 38.34 C HETATM 2886 C38 EFD B 501 9.766 1.718 -39.197 1.00 33.77 C HETATM 2887 C39 EFD B 501 12.428 0.577 -39.912 1.00 42.02 C HETATM 2888 F40 EFD B 501 12.680 1.085 -38.704 1.00 43.26 F HETATM 2889 F41 EFD B 501 11.654 -0.505 -39.764 1.00 41.36 F HETATM 2890 F42 EFD B 501 13.585 0.218 -40.483 1.00 45.14 F HETATM 2891 C1 MLI B 502 -0.569 4.338 -62.559 1.00 81.93 C HETATM 2892 C2 MLI B 502 -1.273 5.640 -62.893 1.00 82.54 C HETATM 2893 C3 MLI B 502 0.683 4.473 -61.711 1.00 79.62 C HETATM 2894 O6 MLI B 502 -1.122 6.107 -64.041 1.00 86.16 O HETATM 2895 O7 MLI B 502 -1.994 6.199 -62.039 1.00 80.24 O HETATM 2896 O8 MLI B 502 1.203 5.599 -61.542 1.00 79.91 O HETATM 2897 O9 MLI B 502 1.173 3.434 -61.210 1.00 77.94 O HETATM 2898 C1 MLI B 503 8.771 -0.184 -30.843 1.00 61.24 C HETATM 2899 C2 MLI B 503 7.702 0.576 -30.068 1.00 51.01 C HETATM 2900 C3 MLI B 503 9.869 -0.758 -29.971 1.00 70.12 C HETATM 2901 O6 MLI B 503 7.130 1.539 -30.631 1.00 48.05 O HETATM 2902 O7 MLI B 503 7.387 0.227 -28.909 1.00 37.83 O HETATM 2903 O8 MLI B 503 10.506 -1.763 -30.361 1.00 68.53 O HETATM 2904 O9 MLI B 503 10.126 -0.199 -28.888 1.00 71.10 O HETATM 2905 NA NA B 504 -4.288 4.371 -43.618 1.00 43.31 NA HETATM 2906 C1 PGE B 505 8.236 -4.632 -57.168 1.00 73.99 C HETATM 2907 O1 PGE B 505 7.904 -5.881 -57.756 1.00 74.87 O HETATM 2908 C2 PGE B 505 8.704 -4.859 -55.746 1.00 75.49 C HETATM 2909 O2 PGE B 505 9.013 -3.609 -55.164 1.00 78.00 O HETATM 2910 C3 PGE B 505 9.646 -3.706 -53.904 1.00 78.49 C HETATM 2911 C4 PGE B 505 10.188 -2.340 -53.533 1.00 78.16 C HETATM 2912 C6 PGE B 505 13.067 -1.823 -51.300 1.00 75.54 C HETATM 2913 C5 PGE B 505 12.316 -1.845 -52.616 1.00 77.60 C HETATM 2914 O3 PGE B 505 11.066 -2.481 -52.434 1.00 79.92 O HETATM 2915 C18 OLC B 506 19.074 -9.764 -41.244 1.00 56.12 C HETATM 2916 C10 OLC B 506 18.347 -12.812 -33.085 1.00 59.21 C HETATM 2917 C9 OLC B 506 18.086 -12.269 -31.885 1.00 57.31 C HETATM 2918 C17 OLC B 506 20.210 -9.515 -40.263 1.00 57.31 C HETATM 2919 C11 OLC B 506 17.556 -12.351 -34.296 1.00 57.42 C HETATM 2920 C8 OLC B 506 17.021 -11.187 -31.835 1.00 54.80 C HETATM 2921 C24 OLC B 506 11.762 -0.881 -26.326 1.00 73.20 C HETATM 2922 C16 OLC B 506 19.656 -9.203 -38.874 1.00 58.42 C HETATM 2923 C12 OLC B 506 18.193 -11.162 -35.028 1.00 54.92 C HETATM 2924 C7 OLC B 506 16.806 -10.697 -30.416 1.00 52.67 C HETATM 2925 C15 OLC B 506 19.299 -10.470 -38.088 1.00 58.20 C HETATM 2926 C13 OLC B 506 19.423 -11.568 -35.836 1.00 55.61 C HETATM 2927 C6 OLC B 506 16.416 -9.224 -30.508 1.00 53.54 C HETATM 2928 C14 OLC B 506 19.920 -10.398 -36.694 1.00 56.73 C HETATM 2929 C5 OLC B 506 16.082 -8.753 -29.102 1.00 54.42 C HETATM 2930 C4 OLC B 506 16.047 -7.239 -29.035 1.00 58.05 C HETATM 2931 C3 OLC B 506 14.647 -6.836 -28.570 1.00 64.43 C HETATM 2932 C2 OLC B 506 14.718 -6.030 -27.279 1.00 70.80 C HETATM 2933 C21 OLC B 506 12.263 -3.260 -26.492 1.00 75.54 C HETATM 2934 C1 OLC B 506 13.801 -4.851 -27.465 1.00 75.62 C HETATM 2935 C22 OLC B 506 12.243 -2.077 -25.530 1.00 75.53 C HETATM 2936 O19 OLC B 506 13.191 -4.674 -28.499 1.00 78.05 O HETATM 2937 O25 OLC B 506 12.798 0.141 -26.322 1.00 70.27 O HETATM 2938 O23 OLC B 506 11.306 -2.335 -24.442 1.00 71.17 O HETATM 2939 O20 OLC B 506 13.562 -3.869 -26.450 1.00 74.27 O HETATM 2940 C18 OLC B 507 -7.474 19.336 -37.394 1.00 62.35 C HETATM 2941 C10 OLC B 507 -6.470 14.306 -45.370 1.00 62.00 C HETATM 2942 C9 OLC B 507 -5.674 14.092 -46.435 1.00 61.36 C HETATM 2943 C17 OLC B 507 -7.739 17.964 -37.991 1.00 64.09 C HETATM 2944 C11 OLC B 507 -5.865 15.031 -44.191 1.00 61.84 C HETATM 2945 C8 OLC B 507 -4.245 14.586 -46.314 1.00 62.92 C HETATM 2946 C24 OLC B 507 0.609 15.913 -57.506 1.00 77.90 C HETATM 2947 C16 OLC B 507 -7.408 18.149 -39.461 1.00 65.49 C HETATM 2948 C12 OLC B 507 -6.944 15.496 -43.218 1.00 61.31 C HETATM 2949 C7 OLC B 507 -3.944 15.345 -47.603 1.00 63.86 C HETATM 2950 C15 OLC B 507 -7.616 16.898 -40.297 1.00 66.51 C HETATM 2951 C13 OLC B 507 -6.449 16.766 -42.542 1.00 62.87 C HETATM 2952 C6 OLC B 507 -2.944 16.474 -47.361 1.00 64.27 C HETATM 2953 C14 OLC B 507 -7.561 17.423 -41.730 1.00 66.58 C HETATM 2954 C5 OLC B 507 -2.596 17.032 -48.747 1.00 62.56 C HETATM 2955 C4 OLC B 507 -2.068 15.890 -49.605 1.00 59.83 C HETATM 2956 C3 OLC B 507 -2.720 15.905 -50.992 1.00 63.40 C HETATM 2957 C2 OLC B 507 -1.749 16.563 -51.956 1.00 70.63 C HETATM 2958 C21 OLC B 507 -0.539 15.532 -55.332 1.00 78.32 C HETATM 2959 C1 OLC B 507 -1.454 15.599 -53.064 1.00 76.36 C HETATM 2960 C22 OLC B 507 0.777 15.888 -56.006 1.00 75.96 C HETATM 2961 O19 OLC B 507 -2.149 14.609 -53.267 1.00 78.34 O HETATM 2962 O25 OLC B 507 0.839 17.306 -57.874 1.00 77.86 O HETATM 2963 O23 OLC B 507 1.018 17.229 -55.550 1.00 72.03 O HETATM 2964 O20 OLC B 507 -0.337 15.833 -53.952 1.00 78.40 O HETATM 2965 C1 OLA B 508 17.958 10.590 -25.460 1.00 79.41 C HETATM 2966 O1 OLA B 508 18.879 11.447 -25.524 1.00 81.67 O HETATM 2967 O2 OLA B 508 17.560 10.149 -24.351 1.00 81.95 O HETATM 2968 C2 OLA B 508 17.364 10.126 -26.735 1.00 73.41 C HETATM 2969 C3 OLA B 508 18.035 10.910 -27.862 1.00 65.25 C HETATM 2970 C4 OLA B 508 17.262 10.598 -29.139 1.00 59.80 C HETATM 2971 C5 OLA B 508 18.186 10.641 -30.346 1.00 56.36 C HETATM 2972 C6 OLA B 508 17.361 10.883 -31.604 1.00 53.58 C HETATM 2973 C7 OLA B 508 18.024 10.218 -32.804 1.00 53.76 C HETATM 2974 C8 OLA B 508 17.630 10.961 -34.086 1.00 53.02 C HETATM 2975 C9 OLA B 508 17.440 9.948 -35.195 1.00 53.86 C HETATM 2976 C10 OLA B 508 17.016 10.453 -36.519 1.00 54.39 C HETATM 2977 C11 OLA B 508 16.241 11.759 -36.468 1.00 57.91 C HETATM 2978 C12 OLA B 508 15.657 12.072 -37.846 1.00 52.01 C HETATM 2979 C13 OLA B 508 15.191 13.515 -37.796 1.00 45.36 C HETATM 2980 C14 OLA B 508 14.414 13.797 -39.062 1.00 42.35 C HETATM 2981 C15 OLA B 508 13.084 14.417 -38.680 1.00 39.88 C HETATM 2982 C16 OLA B 508 13.221 15.901 -38.950 1.00 43.49 C HETATM 2983 C17 OLA B 508 12.397 16.227 -40.177 1.00 44.46 C HETATM 2984 C18 OLA B 508 11.018 16.606 -39.682 1.00 47.16 C HETATM 2985 C1 OLA B 509 18.178 4.980 -23.858 1.00 78.24 C HETATM 2986 O1 OLA B 509 18.362 3.764 -24.130 1.00 81.21 O HETATM 2987 O2 OLA B 509 18.618 5.415 -22.751 1.00 79.96 O HETATM 2988 C2 OLA B 509 17.469 5.874 -24.838 1.00 70.09 C HETATM 2989 C3 OLA B 509 17.339 5.099 -26.153 1.00 63.93 C HETATM 2990 C4 OLA B 509 17.369 6.055 -27.357 1.00 61.00 C HETATM 2991 C5 OLA B 509 17.287 5.262 -28.674 1.00 60.76 C HETATM 2992 C6 OLA B 509 17.802 6.015 -29.907 1.00 60.74 C HETATM 2993 C7 OLA B 509 16.841 5.758 -31.062 1.00 60.33 C HETATM 2994 C8 OLA B 509 17.582 5.287 -32.326 1.00 62.01 C HETATM 2995 C9 OLA B 509 16.732 4.260 -33.056 1.00 64.66 C HETATM 2996 C10 OLA B 509 17.052 4.121 -34.491 1.00 69.67 C HETATM 2997 C11 OLA B 509 17.742 5.319 -35.131 1.00 70.44 C HETATM 2998 C12 OLA B 509 17.027 5.703 -36.441 1.00 69.22 C HETATM 2999 C13 OLA B 509 17.724 5.151 -37.671 1.00 68.30 C HETATM 3000 C14 OLA B 509 16.739 4.233 -38.403 1.00 68.67 C HETATM 3001 C15 OLA B 509 17.435 2.968 -38.902 1.00 67.41 C HETATM 3002 C16 OLA B 509 16.557 2.320 -39.978 1.00 65.56 C HETATM 3003 C17 OLA B 509 17.244 1.093 -40.570 1.00 63.55 C HETATM 3004 C18 OLA B 509 16.977 1.068 -42.079 1.00 63.09 C HETATM 3005 C1 OLA B 510 1.101 -14.861 -55.974 1.00 80.89 C HETATM 3006 O1 OLA B 510 1.164 -14.121 -57.003 1.00 83.94 O HETATM 3007 O2 OLA B 510 0.996 -16.096 -56.136 1.00 83.85 O HETATM 3008 C2 OLA B 510 1.140 -14.347 -54.578 1.00 70.07 C HETATM 3009 C3 OLA B 510 0.110 -15.172 -53.819 1.00 62.43 C HETATM 3010 C4 OLA B 510 0.494 -15.349 -52.350 1.00 61.70 C HETATM 3011 C5 OLA B 510 0.630 -14.026 -51.602 1.00 59.81 C HETATM 3012 C6 OLA B 510 1.665 -14.187 -50.480 1.00 61.12 C HETATM 3013 C7 OLA B 510 0.992 -14.392 -49.134 1.00 64.55 C HETATM 3014 C8 OLA B 510 1.716 -13.670 -47.980 1.00 67.92 C HETATM 3015 C9 OLA B 510 1.669 -12.164 -48.178 1.00 67.24 C HETATM 3016 C10 OLA B 510 1.909 -11.362 -46.948 1.00 65.18 C HETATM 3017 C11 OLA B 510 1.669 -12.129 -45.657 1.00 61.19 C HETATM 3018 C12 OLA B 510 2.342 -11.451 -44.445 1.00 55.67 C HETATM 3019 C13 OLA B 510 2.877 -12.525 -43.487 1.00 50.33 C HETATM 3020 C14 OLA B 510 3.405 -11.894 -42.198 1.00 47.61 C HETATM 3021 C15 OLA B 510 3.016 -12.737 -40.994 1.00 50.55 C HETATM 3022 C16 OLA B 510 3.675 -12.222 -39.713 1.00 56.16 C HETATM 3023 C17 OLA B 510 2.961 -10.955 -39.215 1.00 61.47 C HETATM 3024 C18 OLA B 510 1.549 -11.248 -38.667 1.00 61.56 C HETATM 3025 C1 OLA B 511 18.706 8.849 -58.672 1.00 78.58 C HETATM 3026 O1 OLA B 511 18.490 8.519 -59.858 1.00 77.49 O HETATM 3027 O2 OLA B 511 18.817 10.068 -58.405 1.00 80.50 O HETATM 3028 C2 OLA B 511 18.861 7.853 -57.570 1.00 74.80 C HETATM 3029 C3 OLA B 511 19.351 8.739 -56.427 1.00 69.46 C HETATM 3030 C4 OLA B 511 19.150 8.064 -55.069 1.00 67.35 C HETATM 3031 C5 OLA B 511 19.198 9.180 -54.032 1.00 65.38 C HETATM 3032 C6 OLA B 511 18.871 8.619 -52.648 1.00 63.94 C HETATM 3033 C7 OLA B 511 18.892 9.794 -51.669 1.00 64.44 C HETATM 3034 C8 OLA B 511 18.857 9.256 -50.228 1.00 67.56 C HETATM 3035 C9 OLA B 511 19.247 7.793 -50.298 1.00 69.18 C HETATM 3036 C10 OLA B 511 18.817 6.957 -49.159 1.00 68.00 C HETATM 3037 C11 OLA B 511 18.520 7.789 -47.942 1.00 67.22 C HETATM 3038 C12 OLA B 511 18.485 6.880 -46.708 1.00 65.82 C HETATM 3039 C13 OLA B 511 18.767 7.773 -45.508 1.00 66.72 C HETATM 3040 C14 OLA B 511 18.132 9.162 -45.635 1.00 67.04 C HETATM 3041 C15 OLA B 511 18.734 10.085 -44.562 1.00 66.51 C HETATM 3042 C16 OLA B 511 20.138 10.479 -45.050 1.00 68.87 C HETATM 3043 C17 OLA B 511 20.796 11.536 -44.156 1.00 71.48 C HETATM 3044 C18 OLA B 511 21.720 12.335 -45.087 1.00 71.29 C HETATM 3045 O HOH B 601 -1.253 -4.555 -13.078 1.00 77.30 O HETATM 3046 O HOH B 602 -5.964 6.000 -22.279 1.00 43.54 O HETATM 3047 O HOH B 603 3.898 7.619 -35.828 1.00 23.82 O HETATM 3048 O HOH B 604 -9.010 -11.800 -23.166 1.00 40.24 O HETATM 3049 O HOH B 605 4.236 0.744 -24.681 1.00 34.21 O HETATM 3050 O HOH B 606 -2.371 1.105 -43.800 1.00 34.39 O HETATM 3051 O HOH B 607 5.930 7.418 -58.885 1.00 51.35 O HETATM 3052 O HOH B 608 10.799 5.453 -45.276 1.00 29.78 O HETATM 3053 O HOH B 609 1.053 -2.144 -27.621 1.00 30.23 O HETATM 3054 O HOH B 610 -7.975 3.724 -44.032 1.00 33.45 O HETATM 3055 O HOH B 611 4.227 7.924 -20.090 1.00 38.86 O HETATM 3056 O HOH B 612 6.254 -2.143 -29.393 1.00 34.88 O HETATM 3057 O HOH B 613 -9.025 10.992 -23.703 1.00 38.03 O HETATM 3058 O HOH B 614 2.817 -1.304 -23.673 1.00 30.37 O HETATM 3059 O HOH B 615 -5.772 0.917 -49.023 1.00 29.01 O HETATM 3060 O HOH B 616 0.465 2.813 -27.835 1.00 35.08 O HETATM 3061 O HOH B 617 -3.018 6.849 -43.470 1.00 51.71 O HETATM 3062 O HOH B 618 -2.731 11.411 -32.810 1.00 29.89 O HETATM 3063 O HOH B 619 -6.036 -0.807 -31.112 1.00 27.97 O HETATM 3064 O HOH B 620 -8.826 0.251 -18.902 1.00 39.69 O HETATM 3065 O HOH B 621 -6.555 1.468 -46.504 1.00 29.66 O HETATM 3066 O HOH B 622 7.597 4.477 -15.338 1.00 35.74 O HETATM 3067 O HOH B 623 1.065 -8.499 -22.201 1.00 53.45 O HETATM 3068 O HOH B 624 -0.719 0.086 -28.823 1.00 30.16 O HETATM 3069 O HOH B 625 -1.425 4.279 -39.204 1.00 34.84 O HETATM 3070 O HOH B 626 -3.005 3.454 -41.525 1.00 34.94 O HETATM 3071 O HOH B 627 -3.493 2.659 -59.280 1.00 59.46 O HETATM 3072 O HOH B 628 0.781 -0.808 -25.278 1.00 33.24 O HETATM 3073 O HOH B 629 9.589 -8.875 -31.461 1.00 37.76 O HETATM 3074 O HOH B 630 4.979 8.214 -22.581 1.00 35.48 O HETATM 3075 O HOH B 631 6.021 8.152 -28.824 1.00 37.65 O HETATM 3076 O HOH B 632 -2.528 -8.907 -17.283 1.00 43.03 O HETATM 3077 O HOH B 633 0.443 -1.378 -60.859 1.00 44.39 O HETATM 3078 O HOH B 634 7.457 -2.530 -15.012 1.00 76.71 O HETATM 3079 O HOH B 635 -2.591 3.553 -44.962 1.00 32.41 O HETATM 3080 O HOH B 636 4.984 5.165 -25.386 1.00 45.31 O HETATM 3081 O HOH B 637 -7.638 8.908 -21.822 1.00 40.22 O HETATM 3082 O HOH B 638 12.720 -3.559 -57.614 1.00 53.37 O HETATM 3083 O HOH B 639 6.049 5.702 -23.448 1.00 47.97 O HETATM 3084 O HOH L 101 -3.892 7.037 -19.496 1.00 44.79 O HETATM 3085 O HOH L 102 1.160 2.018 -25.604 1.00 27.06 O HETATM 3086 O HOH L 103 3.125 5.368 -19.785 1.00 40.96 O HETATM 3087 O HOH L 104 3.778 7.238 -27.201 1.00 35.21 O HETATM 3088 O HOH L 105 3.276 3.649 -23.506 1.00 52.89 O HETATM 3089 O HOH L 106 4.231 4.249 -21.598 1.00 43.57 O CONECT 936 2905 CONECT 1145 1770 CONECT 1405 1417 CONECT 1417 1405 1418 CONECT 1418 1417 1419 1425 CONECT 1419 1418 1420 CONECT 1420 1419 1421 CONECT 1421 1420 1422 CONECT 1422 1421 1423 1424 CONECT 1423 1422 CONECT 1424 1422 CONECT 1425 1418 1426 1427 CONECT 1426 1425 CONECT 1427 1425 CONECT 1770 1145 CONECT 2571 2905 CONECT 2602 2905 CONECT 2783 2784 2785 2786 CONECT 2784 2783 CONECT 2785 2783 CONECT 2786 2783 CONECT 2788 2797 CONECT 2797 2788 2798 CONECT 2798 2797 2799 2803 CONECT 2799 2798 2800 CONECT 2800 2799 2801 CONECT 2801 2800 2802 CONECT 2802 2801 2839 CONECT 2803 2798 2804 2805 CONECT 2804 2803 CONECT 2805 2803 CONECT 2807 2818 CONECT 2812 2813 2817 2820 CONECT 2813 2812 2814 CONECT 2814 2813 2815 CONECT 2815 2814 2816 CONECT 2816 2815 2817 CONECT 2817 2812 2816 CONECT 2818 2807 2819 CONECT 2819 2818 2820 2821 CONECT 2820 2812 2819 CONECT 2821 2819 2822 2823 CONECT 2822 2821 CONECT 2823 2821 CONECT 2839 2802 CONECT 2849 2859 2860 CONECT 2850 2859 2862 2863 CONECT 2851 2852 2856 2869 CONECT 2852 2851 2853 CONECT 2853 2852 2854 CONECT 2854 2853 2855 CONECT 2855 2854 2856 2870 CONECT 2856 2851 2855 2857 CONECT 2857 2856 2858 2859 CONECT 2858 2857 CONECT 2859 2849 2850 2857 CONECT 2860 2849 2861 CONECT 2861 2860 2862 CONECT 2862 2850 2861 2871 CONECT 2863 2850 2864 2868 CONECT 2864 2863 2865 CONECT 2865 2864 2866 CONECT 2866 2865 2867 2872 CONECT 2867 2866 2868 CONECT 2868 2863 2867 CONECT 2869 2851 CONECT 2870 2855 CONECT 2871 2862 2878 2879 CONECT 2872 2866 2873 CONECT 2873 2872 2874 2877 CONECT 2874 2873 2875 CONECT 2875 2874 2876 CONECT 2876 2875 2877 CONECT 2877 2873 2876 CONECT 2878 2871 CONECT 2879 2871 2880 CONECT 2880 2879 2881 2885 CONECT 2881 2880 2882 CONECT 2882 2881 2883 2887 CONECT 2883 2882 2884 2886 CONECT 2884 2883 2885 CONECT 2885 2880 2884 CONECT 2886 2883 CONECT 2887 2882 2888 2889 2890 CONECT 2888 2887 CONECT 2889 2887 CONECT 2890 2887 CONECT 2891 2892 2893 CONECT 2892 2891 2894 2895 CONECT 2893 2891 2896 2897 CONECT 2894 2892 CONECT 2895 2892 CONECT 2896 2893 CONECT 2897 2893 CONECT 2898 2899 2900 CONECT 2899 2898 2901 2902 CONECT 2900 2898 2903 2904 CONECT 2901 2899 CONECT 2902 2899 CONECT 2903 2900 CONECT 2904 2900 CONECT 2905 936 2571 2602 3061 CONECT 2905 3070 3079 CONECT 2906 2907 2908 CONECT 2907 2906 CONECT 2908 2906 2909 CONECT 2909 2908 2910 CONECT 2910 2909 2911 CONECT 2911 2910 2914 CONECT 2912 2913 CONECT 2913 2912 2914 CONECT 2914 2911 2913 CONECT 2915 2918 CONECT 2916 2917 2919 CONECT 2917 2916 2920 CONECT 2918 2915 2922 CONECT 2919 2916 2923 CONECT 2920 2917 2924 CONECT 2921 2935 2937 CONECT 2922 2918 2925 CONECT 2923 2919 2926 CONECT 2924 2920 2927 CONECT 2925 2922 2928 CONECT 2926 2923 2928 CONECT 2927 2924 2929 CONECT 2928 2925 2926 CONECT 2929 2927 2930 CONECT 2930 2929 2931 CONECT 2931 2930 2932 CONECT 2932 2931 2934 CONECT 2933 2935 2939 CONECT 2934 2932 2936 2939 CONECT 2935 2921 2933 2938 CONECT 2936 2934 CONECT 2937 2921 CONECT 2938 2935 CONECT 2939 2933 2934 CONECT 2940 2943 CONECT 2941 2942 2944 CONECT 2942 2941 2945 CONECT 2943 2940 2947 CONECT 2944 2941 2948 CONECT 2945 2942 2949 CONECT 2946 2960 2962 CONECT 2947 2943 2950 CONECT 2948 2944 2951 CONECT 2949 2945 2952 CONECT 2950 2947 2953 CONECT 2951 2948 2953 CONECT 2952 2949 2954 CONECT 2953 2950 2951 CONECT 2954 2952 2955 CONECT 2955 2954 2956 CONECT 2956 2955 2957 CONECT 2957 2956 2959 CONECT 2958 2960 2964 CONECT 2959 2957 2961 2964 CONECT 2960 2946 2958 2963 CONECT 2961 2959 CONECT 2962 2946 CONECT 2963 2960 CONECT 2964 2958 2959 CONECT 2965 2966 2967 2968 CONECT 2966 2965 CONECT 2967 2965 CONECT 2968 2965 2969 CONECT 2969 2968 2970 CONECT 2970 2969 2971 CONECT 2971 2970 2972 CONECT 2972 2971 2973 CONECT 2973 2972 2974 CONECT 2974 2973 2975 CONECT 2975 2974 2976 CONECT 2976 2975 2977 CONECT 2977 2976 2978 CONECT 2978 2977 2979 CONECT 2979 2978 2980 CONECT 2980 2979 2981 CONECT 2981 2980 2982 CONECT 2982 2981 2983 CONECT 2983 2982 2984 CONECT 2984 2983 CONECT 2985 2986 2987 2988 CONECT 2986 2985 CONECT 2987 2985 CONECT 2988 2985 2989 CONECT 2989 2988 2990 CONECT 2990 2989 2991 CONECT 2991 2990 2992 CONECT 2992 2991 2993 CONECT 2993 2992 2994 CONECT 2994 2993 2995 CONECT 2995 2994 2996 CONECT 2996 2995 2997 CONECT 2997 2996 2998 CONECT 2998 2997 2999 CONECT 2999 2998 3000 CONECT 3000 2999 3001 CONECT 3001 3000 3002 CONECT 3002 3001 3003 CONECT 3003 3002 3004 CONECT 3004 3003 CONECT 3005 3006 3007 3008 CONECT 3006 3005 CONECT 3007 3005 CONECT 3008 3005 3009 CONECT 3009 3008 3010 CONECT 3010 3009 3011 CONECT 3011 3010 3012 CONECT 3012 3011 3013 CONECT 3013 3012 3014 CONECT 3014 3013 3015 CONECT 3015 3014 3016 CONECT 3016 3015 3017 CONECT 3017 3016 3018 CONECT 3018 3017 3019 CONECT 3019 3018 3020 CONECT 3020 3019 3021 CONECT 3021 3020 3022 CONECT 3022 3021 3023 CONECT 3023 3022 3024 CONECT 3024 3023 CONECT 3025 3026 3027 3028 CONECT 3026 3025 CONECT 3027 3025 CONECT 3028 3025 3029 CONECT 3029 3028 3030 CONECT 3030 3029 3031 CONECT 3031 3030 3032 CONECT 3032 3031 3033 CONECT 3033 3032 3034 CONECT 3034 3033 3035 CONECT 3035 3034 3036 CONECT 3036 3035 3037 CONECT 3037 3036 3038 CONECT 3038 3037 3039 CONECT 3039 3038 3040 CONECT 3040 3039 3041 CONECT 3041 3040 3042 CONECT 3042 3041 3043 CONECT 3043 3042 3044 CONECT 3044 3043 CONECT 3061 2905 CONECT 3070 2905 CONECT 3079 2905 MASTER 572 0 15 18 3 0 17 6 3087 2 245 34 END