HEADER MEMBRANE PROTEIN 29-AUG-18 6AK3 TITLE CRYSTAL STRUCTURE OF THE HUMAN PROSTAGLANDIN E RECEPTOR EP3 BOUND TO TITLE 2 PROSTAGLANDIN E2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROSTAGLANDIN E2 RECEPTOR EP3 SUBTYPE,SOLUBLE CYTOCHROME COMPND 3 B562; COMPND 4 CHAIN: B, A; COMPND 5 SYNONYM: PGE2 RECEPTOR EP3 SUBTYPE,PGE2-R,PROSTANOID EP3 RECEPTOR, COMPND 6 CYTOCHROME B-562; COMPND 7 ENGINEERED: YES; COMPND 8 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 562; SOURCE 5 GENE: PTGER3, CYBC; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS GPCR, LIPID, SIGNALING PROTEIN, PROSTANOID RECEPTOR, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR K.MORIMOTO,R.SUNO,S.IWATA,T.KOBAYASHI REVDAT 4 30-JAN-19 6AK3 1 JRNL REVDAT 3 19-DEC-18 6AK3 1 JRNL REVDAT 2 12-DEC-18 6AK3 1 TITLE REVDAT 1 05-DEC-18 6AK3 0 JRNL AUTH K.MORIMOTO,R.SUNO,Y.HOTTA,K.YAMASHITA,K.HIRATA,M.YAMAMOTO, JRNL AUTH 2 S.NARUMIYA,S.IWATA,T.KOBAYASHI JRNL TITL CRYSTAL STRUCTURE OF THE ENDOGENOUS AGONIST-BOUND PROSTANOID JRNL TITL 2 RECEPTOR EP3. JRNL REF NAT. CHEM. BIOL. V. 15 8 2019 JRNL REFN ESSN 1552-4469 JRNL PMID 30510192 JRNL DOI 10.1038/S41589-018-0171-8 REMARK 2 REMARK 2 RESOLUTION. 2.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.14_3260: ???) 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.38 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 20175 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.253 REMARK 3 R VALUE (WORKING SET) : 0.251 REMARK 3 FREE R VALUE : 0.295 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.790 REMARK 3 FREE R VALUE TEST SET COUNT : 967 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 48.3839 - 5.5453 1.00 2845 149 0.2793 0.3063 REMARK 3 2 5.5453 - 4.4024 1.00 2782 131 0.2518 0.2907 REMARK 3 3 4.4024 - 3.8462 1.00 2712 145 0.2247 0.2971 REMARK 3 4 3.8462 - 3.4947 1.00 2730 142 0.2200 0.2522 REMARK 3 5 3.4947 - 3.2442 1.00 2726 120 0.2361 0.2945 REMARK 3 6 3.2442 - 3.0530 1.00 2718 151 0.2672 0.3004 REMARK 3 7 3.0530 - 2.9001 1.00 2695 129 0.2941 0.3486 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL 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) : 0.370 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.590 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 : 0.002 4329 REMARK 3 ANGLE : 0.437 5830 REMARK 3 CHIRALITY : 0.035 702 REMARK 3 PLANARITY : 0.003 679 REMARK 3 DIHEDRAL : 11.924 2480 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 9 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 47 THROUGH 124 ) REMARK 3 ORIGIN FOR THE GROUP (A): 65.8964 55.2678 211.8119 REMARK 3 T TENSOR REMARK 3 T11: 0.1380 T22: 0.1105 REMARK 3 T33: 0.4316 T12: -0.0708 REMARK 3 T13: -0.0010 T23: 0.0597 REMARK 3 L TENSOR REMARK 3 L11: 4.0765 L22: 3.1433 REMARK 3 L33: 3.2029 L12: 1.4763 REMARK 3 L13: 0.2012 L23: 0.7465 REMARK 3 S TENSOR REMARK 3 S11: -0.0680 S12: -0.0003 S13: 0.1724 REMARK 3 S21: -0.0221 S22: -0.0463 S23: 0.1104 REMARK 3 S31: -0.3998 S32: 0.0930 S33: -0.0713 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 125 THROUGH 226 ) REMARK 3 ORIGIN FOR THE GROUP (A): 51.1737 53.8619 210.6267 REMARK 3 T TENSOR REMARK 3 T11: 0.1611 T22: 0.2226 REMARK 3 T33: 0.7294 T12: 0.0005 REMARK 3 T13: -0.0176 T23: 0.1361 REMARK 3 L TENSOR REMARK 3 L11: 3.9445 L22: 2.7074 REMARK 3 L33: 1.8476 L12: 0.7346 REMARK 3 L13: 0.4984 L23: 0.3946 REMARK 3 S TENSOR REMARK 3 S11: -0.0548 S12: 0.2403 S13: 0.7531 REMARK 3 S21: -0.2856 S22: 0.0559 S23: 0.5763 REMARK 3 S31: -0.3771 S32: -0.1006 S33: -0.1423 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 227 THROUGH 346 ) REMARK 3 ORIGIN FOR THE GROUP (A): 54.7739 39.6636 209.2063 REMARK 3 T TENSOR REMARK 3 T11: 0.0011 T22: 0.1943 REMARK 3 T33: 0.3490 T12: -0.0946 REMARK 3 T13: -0.1189 T23: 0.1357 REMARK 3 L TENSOR REMARK 3 L11: 3.7985 L22: 1.9232 REMARK 3 L33: 2.2476 L12: 1.1776 REMARK 3 L13: 0.3215 L23: 0.0564 REMARK 3 S TENSOR REMARK 3 S11: 0.0323 S12: 0.2765 S13: -0.0673 REMARK 3 S21: -0.0424 S22: 0.2005 S23: 0.0656 REMARK 3 S31: 0.3411 S32: -0.2258 S33: -0.2033 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 347 THROUGH 1106 ) REMARK 3 ORIGIN FOR THE GROUP (A): 67.5392 38.8477 190.9427 REMARK 3 T TENSOR REMARK 3 T11: 0.2990 T22: 0.5917 REMARK 3 T33: 0.4256 T12: -0.2382 REMARK 3 T13: -0.1104 T23: -0.1950 REMARK 3 L TENSOR REMARK 3 L11: 1.0013 L22: 1.2816 REMARK 3 L33: 1.7124 L12: -0.5649 REMARK 3 L13: 0.2595 L23: -0.8780 REMARK 3 S TENSOR REMARK 3 S11: -0.0258 S12: 0.5700 S13: -0.4380 REMARK 3 S21: -0.4733 S22: 0.0256 S23: 0.4411 REMARK 3 S31: 0.3363 S32: -0.2688 S33: -0.3113 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 47 THROUGH 116 ) REMARK 3 ORIGIN FOR THE GROUP (A): 80.6352 34.7430 208.8639 REMARK 3 T TENSOR REMARK 3 T11: 0.1886 T22: 0.1528 REMARK 3 T33: 0.3973 T12: -0.1120 REMARK 3 T13: -0.0249 T23: -0.1513 REMARK 3 L TENSOR REMARK 3 L11: 3.4172 L22: 2.7431 REMARK 3 L33: 3.3262 L12: 1.1692 REMARK 3 L13: 0.0556 L23: -0.2036 REMARK 3 S TENSOR REMARK 3 S11: -0.0519 S12: 0.1905 S13: -0.3683 REMARK 3 S21: -0.2794 S22: 0.1494 S23: -0.1597 REMARK 3 S31: 0.2958 S32: -0.0641 S33: -0.1379 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 117 THROUGH 202 ) REMARK 3 ORIGIN FOR THE GROUP (A): 95.0747 34.1800 210.3399 REMARK 3 T TENSOR REMARK 3 T11: 0.1368 T22: 0.2155 REMARK 3 T33: 0.6622 T12: 0.0346 REMARK 3 T13: -0.0228 T23: -0.1221 REMARK 3 L TENSOR REMARK 3 L11: 3.4405 L22: 2.6756 REMARK 3 L33: 1.5844 L12: 0.8793 REMARK 3 L13: 0.0934 L23: -0.2199 REMARK 3 S TENSOR REMARK 3 S11: 0.1771 S12: 0.0874 S13: -0.6133 REMARK 3 S21: -0.2623 S22: 0.2032 S23: -0.3748 REMARK 3 S31: 0.2892 S32: 0.1973 S33: -0.0682 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 203 THROUGH 263 ) REMARK 3 ORIGIN FOR THE GROUP (A): 96.5807 47.0508 210.7170 REMARK 3 T TENSOR REMARK 3 T11: -0.0012 T22: 0.3001 REMARK 3 T33: 0.3528 T12: -0.1318 REMARK 3 T13: -0.0119 T23: -0.0657 REMARK 3 L TENSOR REMARK 3 L11: 3.2932 L22: 1.9542 REMARK 3 L33: 0.9691 L12: 0.7375 REMARK 3 L13: 0.3626 L23: 0.1527 REMARK 3 S TENSOR REMARK 3 S11: -0.0681 S12: 0.1161 S13: -0.0773 REMARK 3 S21: -0.2064 S22: 0.0588 S23: -0.2869 REMARK 3 S31: -0.0046 S32: 0.2369 S33: -0.0270 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 264 THROUGH 346 ) REMARK 3 ORIGIN FOR THE GROUP (A): 88.1853 48.9576 210.4439 REMARK 3 T TENSOR REMARK 3 T11: 0.0683 T22: 0.1225 REMARK 3 T33: 0.2849 T12: -0.0449 REMARK 3 T13: 0.0509 T23: -0.0167 REMARK 3 L TENSOR REMARK 3 L11: 3.3107 L22: 2.7440 REMARK 3 L33: 0.5066 L12: 1.1747 REMARK 3 L13: -0.2149 L23: -0.0769 REMARK 3 S TENSOR REMARK 3 S11: 0.0986 S12: 0.0952 S13: 0.1842 REMARK 3 S21: -0.0575 S22: 0.0370 S23: 0.0751 REMARK 3 S31: -0.1455 S32: 0.0465 S33: -0.0415 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 347 THROUGH 1106 ) REMARK 3 ORIGIN FOR THE GROUP (A): 81.0460 52.2088 188.5217 REMARK 3 T TENSOR REMARK 3 T11: 0.2974 T22: 0.5794 REMARK 3 T33: 0.3680 T12: -0.1704 REMARK 3 T13: 0.0358 T23: 0.2688 REMARK 3 L TENSOR REMARK 3 L11: 1.1242 L22: 0.5967 REMARK 3 L33: 1.6152 L12: -0.5864 REMARK 3 L13: -0.7280 L23: 0.9568 REMARK 3 S TENSOR REMARK 3 S11: -0.1010 S12: 0.7775 S13: 0.5754 REMARK 3 S21: -0.4479 S22: 0.0154 S23: -0.4068 REMARK 3 S31: -0.3575 S32: 0.2051 S33: -0.1425 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 6AK3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-SEP-18. REMARK 100 THE DEPOSITION ID IS D_1300008457. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 22-JAN-18 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SPRING-8 REMARK 200 BEAMLINE : BL32XU REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20206 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 43.40 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 1.1500 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.08 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.07 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: BUFFER A (0.1 M MES-NAOH (PH 6.0), 35 REMARK 280 % PEG300, 400 MM NA2SO4, 1% 1,2,3-HEPTANETRIOL, 0.2 MM ONO-AE3- REMARK 280 240), BUFFER B (0.1 M MES-NAOH (PH 5.5-6.0), 30-40 % PEG300, 100 REMARK 280 MM NACL, 100 MM LI2SO4, 1% 1,2,3-HEPTANETRIOL, 0.2 MM ONO-AE3- REMARK 280 240), BUFFER C (0.1 M MES-NAOH (PH 6.1) OR 0.1 M TRIS-HCL (PH REMARK 280 7.5-8.0), 30 % PEG500MME, 200 MM (NH4)2SO4, 1% 1,2,3- REMARK 280 HEPTANETRIOL, 0.2 MM ONO-AE3-240), BUFFER D (0.1 M MES-NAOH (PH REMARK 280 5.8-6.1), 30 % PEG300, 100 MM MGSO4, 1% 1,2,3-HEPTANETRIOL, 0.2 REMARK 280 MM ONO-AE3-240), BUFFER E (0.1 M MES-NAOH (PH 5.5), 30 % PEG300, REMARK 280 100 MM K2SO4, 1% 1,2,3-HEPTANETRIOL, 0.2 MM ONO-AE3-240), REMARK 280 LIPIDIC CUBIC PHASE, TEMPERATURE 293K 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 21.14000 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: 2460 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 26250 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 GLY B 39 REMARK 465 PRO B 40 REMARK 465 THR B 41 REMARK 465 SER B 42 REMARK 465 SER B 43 REMARK 465 GLY B 44 REMARK 465 GLU B 45 REMARK 465 ASP B 46 REMARK 465 ARG B 79 REMARK 465 ARG B 80 REMARK 465 GLU B 81 REMARK 465 SER B 82 REMARK 465 LYS B 83 REMARK 465 ARG B 84 REMARK 465 LYS B 85 REMARK 465 GLN B 118 REMARK 465 ARG B 214 REMARK 465 GLY B 215 REMARK 465 GLY B 216 REMARK 465 GLN B 217 REMARK 465 GLY B 218 REMARK 465 THR B 219 REMARK 465 SER B 220 REMARK 465 SER B 221 REMARK 465 SER B 222 REMARK 465 HIS B 223 REMARK 465 ASN B 224 REMARK 465 TRP B 225 REMARK 465 THR B 265 REMARK 465 ALA B 266 REMARK 465 SER B 267 REMARK 465 GLN B 268 REMARK 465 SER B 269 REMARK 465 SER B 270 REMARK 465 GLN B 308 REMARK 465 GLN B 309 REMARK 465 THR B 310 REMARK 465 SER B 311 REMARK 465 VAL B 312 REMARK 465 GLU B 313 REMARK 465 HIS B 314 REMARK 465 CYS B 315 REMARK 465 LYS B 316 REMARK 465 THR B 317 REMARK 465 HIS B 318 REMARK 465 THR B 319 REMARK 465 GLU B 320 REMARK 465 LYS B 321 REMARK 465 GLN B 322 REMARK 465 LYS B 356 REMARK 465 PHE B 357 REMARK 465 CYS B 358 REMARK 465 GLN B 359 REMARK 465 LEU B 360 REMARK 465 GLU B 361 REMARK 465 LEU B 362 REMARK 465 GLU B 363 REMARK 465 VAL B 364 REMARK 465 LEU B 365 REMARK 465 PHE B 366 REMARK 465 GLN B 367 REMARK 465 ASP B 1002 REMARK 465 LEU B 1003 REMARK 465 GLU B 1004 REMARK 465 ASP B 1005 REMARK 465 ASN B 1006 REMARK 465 TRP B 1007 REMARK 465 GLU B 1008 REMARK 465 THR B 1009 REMARK 465 LEU B 1010 REMARK 465 ASN B 1011 REMARK 465 ASP B 1012 REMARK 465 ASN B 1013 REMARK 465 LEU B 1014 REMARK 465 LYS B 1015 REMARK 465 VAL B 1016 REMARK 465 ILE B 1017 REMARK 465 GLU B 1018 REMARK 465 LYS B 1019 REMARK 465 ALA B 1020 REMARK 465 ASP B 1021 REMARK 465 ASN B 1022 REMARK 465 ALA B 1023 REMARK 465 ALA B 1024 REMARK 465 GLN B 1025 REMARK 465 VAL B 1026 REMARK 465 LYS B 1027 REMARK 465 ASP B 1028 REMARK 465 ALA B 1029 REMARK 465 LEU B 1030 REMARK 465 THR B 1031 REMARK 465 LYS B 1032 REMARK 465 MET B 1033 REMARK 465 ARG B 1034 REMARK 465 ALA B 1035 REMARK 465 ALA B 1036 REMARK 465 ALA B 1037 REMARK 465 LEU B 1038 REMARK 465 ASP B 1039 REMARK 465 ALA B 1040 REMARK 465 GLY B 1041 REMARK 465 SER B 1042 REMARK 465 GLY B 1043 REMARK 465 SER B 1044 REMARK 465 GLY B 1045 REMARK 465 HIS B 1063 REMARK 465 GLY B 1064 REMARK 465 PHE B 1065 REMARK 465 ASP B 1066 REMARK 465 ILE B 1067 REMARK 465 LEU B 1068 REMARK 465 VAL B 1069 REMARK 465 GLY B 1070 REMARK 465 GLN B 1071 REMARK 465 ILE B 1072 REMARK 465 ASP B 1073 REMARK 465 ASP B 1074 REMARK 465 ALA B 1075 REMARK 465 LEU B 1076 REMARK 465 LYS B 1077 REMARK 465 LEU B 1078 REMARK 465 ALA B 1079 REMARK 465 ASN B 1080 REMARK 465 GLU B 1081 REMARK 465 GLY B 1082 REMARK 465 LYS B 1083 REMARK 465 VAL B 1084 REMARK 465 LYS B 1085 REMARK 465 GLU B 1086 REMARK 465 ALA B 1087 REMARK 465 GLN B 1088 REMARK 465 ALA B 1089 REMARK 465 ALA B 1090 REMARK 465 ALA B 1091 REMARK 465 GLU B 1092 REMARK 465 GLN B 1093 REMARK 465 LEU B 1094 REMARK 465 LYS B 1095 REMARK 465 THR B 1096 REMARK 465 THR B 1097 REMARK 465 ILE B 1098 REMARK 465 ASN B 1099 REMARK 465 ALA B 1100 REMARK 465 TYR B 1101 REMARK 465 ILE B 1102 REMARK 465 GLN B 1103 REMARK 465 GLY A 39 REMARK 465 PRO A 40 REMARK 465 THR A 41 REMARK 465 SER A 42 REMARK 465 SER A 43 REMARK 465 GLY A 44 REMARK 465 GLU A 45 REMARK 465 ASP A 46 REMARK 465 TYR A 77 REMARK 465 ARG A 79 REMARK 465 ARG A 80 REMARK 465 GLU A 81 REMARK 465 SER A 82 REMARK 465 LYS A 83 REMARK 465 ARG A 84 REMARK 465 LYS A 85 REMARK 465 GLN A 118 REMARK 465 SER A 126 REMARK 465 ARG A 214 REMARK 465 GLY A 215 REMARK 465 GLY A 216 REMARK 465 GLN A 217 REMARK 465 GLY A 218 REMARK 465 THR A 219 REMARK 465 SER A 220 REMARK 465 SER A 221 REMARK 465 SER A 222 REMARK 465 HIS A 223 REMARK 465 ASN A 224 REMARK 465 TRP A 225 REMARK 465 THR A 265 REMARK 465 ALA A 266 REMARK 465 SER A 267 REMARK 465 GLN A 268 REMARK 465 SER A 269 REMARK 465 SER A 270 REMARK 465 GLN A 308 REMARK 465 GLN A 309 REMARK 465 THR A 310 REMARK 465 SER A 311 REMARK 465 VAL A 312 REMARK 465 GLU A 313 REMARK 465 HIS A 314 REMARK 465 CYS A 315 REMARK 465 LYS A 316 REMARK 465 THR A 317 REMARK 465 HIS A 318 REMARK 465 THR A 319 REMARK 465 GLU A 320 REMARK 465 LYS A 321 REMARK 465 GLN A 322 REMARK 465 LYS A 356 REMARK 465 PHE A 357 REMARK 465 CYS A 358 REMARK 465 GLN A 359 REMARK 465 LEU A 360 REMARK 465 GLU A 361 REMARK 465 LEU A 362 REMARK 465 GLU A 363 REMARK 465 VAL A 364 REMARK 465 LEU A 365 REMARK 465 PHE A 366 REMARK 465 GLN A 367 REMARK 465 GLU A 1004 REMARK 465 ASP A 1005 REMARK 465 ASN A 1006 REMARK 465 TRP A 1007 REMARK 465 GLU A 1008 REMARK 465 THR A 1009 REMARK 465 LEU A 1010 REMARK 465 ASN A 1011 REMARK 465 ASP A 1012 REMARK 465 ASN A 1013 REMARK 465 LEU A 1014 REMARK 465 LYS A 1015 REMARK 465 VAL A 1016 REMARK 465 ILE A 1017 REMARK 465 GLU A 1018 REMARK 465 LYS A 1019 REMARK 465 ALA A 1020 REMARK 465 ASP A 1021 REMARK 465 ASN A 1022 REMARK 465 ALA A 1023 REMARK 465 ALA A 1024 REMARK 465 GLN A 1025 REMARK 465 VAL A 1026 REMARK 465 LYS A 1027 REMARK 465 ASP A 1028 REMARK 465 ALA A 1029 REMARK 465 LEU A 1030 REMARK 465 THR A 1031 REMARK 465 LYS A 1032 REMARK 465 MET A 1033 REMARK 465 ARG A 1034 REMARK 465 ALA A 1035 REMARK 465 ALA A 1036 REMARK 465 ALA A 1037 REMARK 465 LEU A 1038 REMARK 465 ASP A 1039 REMARK 465 ALA A 1040 REMARK 465 GLY A 1041 REMARK 465 SER A 1042 REMARK 465 GLY A 1043 REMARK 465 SER A 1044 REMARK 465 GLY A 1045 REMARK 465 HIS A 1063 REMARK 465 GLY A 1064 REMARK 465 PHE A 1065 REMARK 465 ASP A 1066 REMARK 465 ILE A 1067 REMARK 465 LEU A 1068 REMARK 465 VAL A 1069 REMARK 465 GLY A 1070 REMARK 465 GLN A 1071 REMARK 465 ILE A 1072 REMARK 465 ASP A 1073 REMARK 465 ASP A 1074 REMARK 465 ALA A 1075 REMARK 465 LEU A 1076 REMARK 465 LYS A 1077 REMARK 465 LEU A 1078 REMARK 465 ALA A 1079 REMARK 465 ASN A 1080 REMARK 465 GLU A 1081 REMARK 465 GLY A 1082 REMARK 465 LYS A 1083 REMARK 465 VAL A 1084 REMARK 465 LYS A 1085 REMARK 465 GLU A 1086 REMARK 465 ALA A 1087 REMARK 465 GLN A 1088 REMARK 465 ALA A 1089 REMARK 465 ALA A 1090 REMARK 465 ALA A 1091 REMARK 465 GLU A 1092 REMARK 465 GLN A 1093 REMARK 465 LEU A 1094 REMARK 465 LYS A 1095 REMARK 465 THR A 1096 REMARK 465 THR A 1097 REMARK 465 ILE A 1098 REMARK 465 ASN A 1099 REMARK 465 ALA A 1100 REMARK 465 TYR A 1101 REMARK 465 ILE A 1102 REMARK 465 GLN A 1103 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 CYS B 47 CB SG REMARK 470 TYR B 77 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR B 77 OH REMARK 470 SER B 126 CB OG REMARK 470 ARG B 160 CB CG CD NE CZ NH1 NH2 REMARK 470 TYR B 165 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR B 165 OH REMARK 470 ALA B 166 CB REMARK 470 SER B 167 CB OG REMARK 470 LYS B 170 CB CG CD CE NZ REMARK 470 ARG B 172 CB CG CD NE CZ NH1 NH2 REMARK 470 VAL B 193 CB CG1 CG2 REMARK 470 ARG B 259 CB CG CD NE CZ NH1 NH2 REMARK 470 ALA B 264 CB REMARK 470 TRP B 273 CB CG CD1 CD2 NE1 CE2 CE3 REMARK 470 TRP B 273 CZ2 CZ3 CH2 REMARK 470 ALA B1001 CB REMARK 470 LYS B1104 CB CG CD CE NZ REMARK 470 TYR B1105 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR B1105 OH REMARK 470 CYS A 47 CB SG REMARK 470 TYR A 165 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR A 165 OH REMARK 470 ALA A 166 CB REMARK 470 SER A 167 CB OG REMARK 470 LYS A 170 CB CG CD CE NZ REMARK 470 ARG A 172 CB CG CD NE CZ NH1 NH2 REMARK 470 GLU A 324 CB CG CD OE1 OE2 REMARK 470 LEU A1003 CB CG CD1 CD2 REMARK 470 TYR A1105 CB CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR A1105 OH 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 SER B 126 -4.28 75.81 REMARK 500 PRO B 204 45.25 -97.39 REMARK 500 PRO A 204 45.08 -97.44 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 POV B 1202 REMARK 610 POV A 1202 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue P2E B 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue POV B 1202 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue P2E A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue POV A 1202 DBREF 6AK3 B 43 359 UNP P43115 PE2R3_HUMAN 43 359 DBREF 6AK3 B 1001 1040 UNP P0ABE7 C562_ECOLX 23 62 DBREF 6AK3 B 1063 1105 UNP P0ABE7 C562_ECOLX 85 127 DBREF 6AK3 A 43 359 UNP P43115 PE2R3_HUMAN 43 359 DBREF 6AK3 A 1001 1040 UNP P0ABE7 C562_ECOLX 23 62 DBREF 6AK3 A 1063 1105 UNP P0ABE7 C562_ECOLX 85 127 SEQADV 6AK3 GLY B 39 UNP P43115 EXPRESSION TAG SEQADV 6AK3 PRO B 40 UNP P43115 EXPRESSION TAG SEQADV 6AK3 THR B 41 UNP P43115 EXPRESSION TAG SEQADV 6AK3 SER B 42 UNP P43115 EXPRESSION TAG SEQADV 6AK3 ILE B 173 UNP P43115 ALA 173 ENGINEERED MUTATION SEQADV 6AK3 SER B 185 UNP P43115 VAL 185 ENGINEERED MUTATION SEQADV 6AK3 GLN B 217 UNP P43115 ASN 217 ENGINEERED MUTATION SEQADV 6AK3 ASP B 258 UNP P43115 SER 258 ENGINEERED MUTATION SEQADV 6AK3 LEU B 289 UNP P43115 CYS 289 ENGINEERED MUTATION SEQADV 6AK3 GLN B 308 UNP P43115 ASN 308 ENGINEERED MUTATION SEQADV 6AK3 LEU B 360 UNP P43115 LINKER SEQADV 6AK3 GLU B 361 UNP P43115 LINKER SEQADV 6AK3 LEU B 362 UNP P43115 LINKER SEQADV 6AK3 GLU B 363 UNP P43115 LINKER SEQADV 6AK3 VAL B 364 UNP P43115 LINKER SEQADV 6AK3 LEU B 365 UNP P43115 LINKER SEQADV 6AK3 PHE B 366 UNP P43115 LINKER SEQADV 6AK3 GLN B 367 UNP P43115 LINKER SEQADV 6AK3 TRP B 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 6AK3 GLY B 1041 UNP P0ABE7 LINKER SEQADV 6AK3 SER B 1042 UNP P0ABE7 LINKER SEQADV 6AK3 GLY B 1043 UNP P0ABE7 LINKER SEQADV 6AK3 SER B 1044 UNP P0ABE7 LINKER SEQADV 6AK3 GLY B 1045 UNP P0ABE7 LINKER SEQADV 6AK3 ILE B 1098 UNP P0ABE7 ARG 120 ENGINEERED MUTATION SEQADV 6AK3 ILE B 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 6AK3 GLY B 1106 UNP P0ABE7 EXPRESSION TAG SEQADV 6AK3 GLY A 39 UNP P43115 EXPRESSION TAG SEQADV 6AK3 PRO A 40 UNP P43115 EXPRESSION TAG SEQADV 6AK3 THR A 41 UNP P43115 EXPRESSION TAG SEQADV 6AK3 SER A 42 UNP P43115 EXPRESSION TAG SEQADV 6AK3 ILE A 173 UNP P43115 ALA 173 ENGINEERED MUTATION SEQADV 6AK3 SER A 185 UNP P43115 VAL 185 ENGINEERED MUTATION SEQADV 6AK3 GLN A 217 UNP P43115 ASN 217 ENGINEERED MUTATION SEQADV 6AK3 ASP A 258 UNP P43115 SER 258 ENGINEERED MUTATION SEQADV 6AK3 LEU A 289 UNP P43115 CYS 289 ENGINEERED MUTATION SEQADV 6AK3 GLN A 308 UNP P43115 ASN 308 ENGINEERED MUTATION SEQADV 6AK3 LEU A 360 UNP P43115 LINKER SEQADV 6AK3 GLU A 361 UNP P43115 LINKER SEQADV 6AK3 LEU A 362 UNP P43115 LINKER SEQADV 6AK3 GLU A 363 UNP P43115 LINKER SEQADV 6AK3 VAL A 364 UNP P43115 LINKER SEQADV 6AK3 LEU A 365 UNP P43115 LINKER SEQADV 6AK3 PHE A 366 UNP P43115 LINKER SEQADV 6AK3 GLN A 367 UNP P43115 LINKER SEQADV 6AK3 TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 6AK3 GLY A 1041 UNP P0ABE7 LINKER SEQADV 6AK3 SER A 1042 UNP P0ABE7 LINKER SEQADV 6AK3 GLY A 1043 UNP P0ABE7 LINKER SEQADV 6AK3 SER A 1044 UNP P0ABE7 LINKER SEQADV 6AK3 GLY A 1045 UNP P0ABE7 LINKER SEQADV 6AK3 ILE A 1098 UNP P0ABE7 ARG 120 ENGINEERED MUTATION SEQADV 6AK3 ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 6AK3 GLY A 1106 UNP P0ABE7 EXPRESSION TAG SEQRES 1 B 418 GLY PRO THR SER SER GLY GLU ASP CYS GLY SER VAL SER SEQRES 2 B 418 VAL ALA PHE PRO ILE THR MET LEU LEU THR GLY PHE VAL SEQRES 3 B 418 GLY ASN ALA LEU ALA MET LEU LEU VAL SER ARG SER TYR SEQRES 4 B 418 ARG ARG ARG GLU SER LYS ARG LYS LYS SER PHE LEU LEU SEQRES 5 B 418 CYS ILE GLY TRP LEU ALA LEU THR ASP LEU VAL GLY GLN SEQRES 6 B 418 LEU LEU THR THR PRO VAL VAL ILE VAL VAL TYR LEU SER SEQRES 7 B 418 LYS GLN ARG TRP GLU HIS ILE ASP PRO SER GLY ARG LEU SEQRES 8 B 418 CYS THR PHE PHE GLY LEU THR MET THR VAL PHE GLY LEU SEQRES 9 B 418 SER SER LEU PHE ILE ALA SER ALA MET ALA VAL GLU ARG SEQRES 10 B 418 ALA LEU ALA ILE ARG ALA PRO HIS TRP TYR ALA SER HIS SEQRES 11 B 418 MET LYS THR ARG ILE THR ARG ALA VAL LEU LEU GLY VAL SEQRES 12 B 418 TRP LEU ALA SER LEU ALA PHE ALA LEU LEU PRO VAL LEU SEQRES 13 B 418 GLY VAL GLY GLN TYR THR VAL GLN TRP PRO GLY THR TRP SEQRES 14 B 418 CYS PHE ILE SER THR GLY ARG GLY GLY GLN GLY THR SER SEQRES 15 B 418 SER SER HIS ASN TRP GLY ASN LEU PHE PHE ALA SER ALA SEQRES 16 B 418 PHE ALA PHE LEU GLY LEU LEU ALA LEU THR VAL THR PHE SEQRES 17 B 418 SER CYS ASN LEU ALA THR ILE LYS ALA LEU VAL ASP ARG SEQRES 18 B 418 CYS ARG ALA LYS ALA THR ALA SER GLN SER SER ALA GLN SEQRES 19 B 418 TRP GLY ARG ILE THR THR GLU THR ALA ILE GLN LEU MET SEQRES 20 B 418 GLY ILE MET LEU VAL LEU SER VAL CYS TRP SER PRO LEU SEQRES 21 B 418 LEU ILE MET MET LEU LYS MET ILE PHE GLN GLN THR SER SEQRES 22 B 418 VAL GLU HIS CYS LYS THR HIS THR GLU LYS GLN LYS GLU SEQRES 23 B 418 CYS ASN PHE PHE LEU ILE ALA VAL ARG LEU ALA SER LEU SEQRES 24 B 418 ASN GLN ILE LEU ASP PRO TRP VAL TYR LEU LEU LEU ARG SEQRES 25 B 418 LYS ILE LEU LEU ARG LYS PHE CYS GLN LEU GLU LEU GLU SEQRES 26 B 418 VAL LEU PHE GLN ALA ASP LEU GLU ASP ASN TRP GLU THR SEQRES 27 B 418 LEU ASN ASP ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN SEQRES 28 B 418 ALA ALA GLN VAL LYS ASP ALA LEU THR LYS MET ARG ALA SEQRES 29 B 418 ALA ALA LEU ASP ALA GLY SER GLY SER GLY HIS GLY PHE SEQRES 30 B 418 ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU SEQRES 31 B 418 ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA SEQRES 32 B 418 GLU GLN LEU LYS THR THR ILE ASN ALA TYR ILE GLN LYS SEQRES 33 B 418 TYR GLY SEQRES 1 A 418 GLY PRO THR SER SER GLY GLU ASP CYS GLY SER VAL SER SEQRES 2 A 418 VAL ALA PHE PRO ILE THR MET LEU LEU THR GLY PHE VAL SEQRES 3 A 418 GLY ASN ALA LEU ALA MET LEU LEU VAL SER ARG SER TYR SEQRES 4 A 418 ARG ARG ARG GLU SER LYS ARG LYS LYS SER PHE LEU LEU SEQRES 5 A 418 CYS ILE GLY TRP LEU ALA LEU THR ASP LEU VAL GLY GLN SEQRES 6 A 418 LEU LEU THR THR PRO VAL VAL ILE VAL VAL TYR LEU SER SEQRES 7 A 418 LYS GLN ARG TRP GLU HIS ILE ASP PRO SER GLY ARG LEU SEQRES 8 A 418 CYS THR PHE PHE GLY LEU THR MET THR VAL PHE GLY LEU SEQRES 9 A 418 SER SER LEU PHE ILE ALA SER ALA MET ALA VAL GLU ARG SEQRES 10 A 418 ALA LEU ALA ILE ARG ALA PRO HIS TRP TYR ALA SER HIS SEQRES 11 A 418 MET LYS THR ARG ILE THR ARG ALA VAL LEU LEU GLY VAL SEQRES 12 A 418 TRP LEU ALA SER LEU ALA PHE ALA LEU LEU PRO VAL LEU SEQRES 13 A 418 GLY VAL GLY GLN TYR THR VAL GLN TRP PRO GLY THR TRP SEQRES 14 A 418 CYS PHE ILE SER THR GLY ARG GLY GLY GLN GLY THR SER SEQRES 15 A 418 SER SER HIS ASN TRP GLY ASN LEU PHE PHE ALA SER ALA SEQRES 16 A 418 PHE ALA PHE LEU GLY LEU LEU ALA LEU THR VAL THR PHE SEQRES 17 A 418 SER CYS ASN LEU ALA THR ILE LYS ALA LEU VAL ASP ARG SEQRES 18 A 418 CYS ARG ALA LYS ALA THR ALA SER GLN SER SER ALA GLN SEQRES 19 A 418 TRP GLY ARG ILE THR THR GLU THR ALA ILE GLN LEU MET SEQRES 20 A 418 GLY ILE MET LEU VAL LEU SER VAL CYS TRP SER PRO LEU SEQRES 21 A 418 LEU ILE MET MET LEU LYS MET ILE PHE GLN GLN THR SER SEQRES 22 A 418 VAL GLU HIS CYS LYS THR HIS THR GLU LYS GLN LYS GLU SEQRES 23 A 418 CYS ASN PHE PHE LEU ILE ALA VAL ARG LEU ALA SER LEU SEQRES 24 A 418 ASN GLN ILE LEU ASP PRO TRP VAL TYR LEU LEU LEU ARG SEQRES 25 A 418 LYS ILE LEU LEU ARG LYS PHE CYS GLN LEU GLU LEU GLU SEQRES 26 A 418 VAL LEU PHE GLN ALA ASP LEU GLU ASP ASN TRP GLU THR SEQRES 27 A 418 LEU ASN ASP ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN SEQRES 28 A 418 ALA ALA GLN VAL LYS ASP ALA LEU THR LYS MET ARG ALA SEQRES 29 A 418 ALA ALA LEU ASP ALA GLY SER GLY SER GLY HIS GLY PHE SEQRES 30 A 418 ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU SEQRES 31 A 418 ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA SEQRES 32 A 418 GLU GLN LEU LYS THR THR ILE ASN ALA TYR ILE GLN LYS SEQRES 33 A 418 TYR GLY HET P2E B1201 25 HET POV B1202 46 HET P2E A1201 25 HET POV A1202 46 HETNAM P2E (Z)-7-[(1R,2R,3R)-3-HYDROXY-2-[(E,3S)-3-HYDROXYOCT-1- HETNAM 2 P2E ENYL]-5-OXO-CYCLOPENTYL]HEPT-5-ENOIC ACID HETNAM POV (2S)-3-(HEXADECANOYLOXY)-2-[(9Z)-OCTADEC-9- HETNAM 2 POV ENOYLOXY]PROPYL 2-(TRIMETHYLAMMONIO)ETHYL PHOSPHATE HETSYN P2E PROSTAGLANDIN E2 HETSYN POV POPC FORMUL 3 P2E 2(C20 H32 O5) FORMUL 4 POV 2(C42 H82 N O8 P) HELIX 1 AA1 VAL B 52 TYR B 77 1 26 HELIX 2 AA2 SER B 87 LEU B 105 1 19 HELIX 3 AA3 THR B 106 LYS B 117 1 12 HELIX 4 AA4 TRP B 120 ASP B 124 1 5 HELIX 5 AA5 GLY B 127 ALA B 161 1 35 HELIX 6 AA6 ALA B 161 MET B 169 1 9 HELIX 7 AA7 LYS B 170 LEU B 190 1 21 HELIX 8 AA8 LEU B 190 GLY B 195 1 6 HELIX 9 AA9 ASN B 227 ALA B 264 1 38 HELIX 10 AB1 GLN B 272 PHE B 307 1 36 HELIX 11 AB2 GLU B 324 LEU B 347 1 24 HELIX 12 AB3 LEU B 347 LEU B 353 1 7 HELIX 13 AB4 VAL A 52 SER A 76 1 25 HELIX 14 AB5 SER A 87 LEU A 105 1 19 HELIX 15 AB6 THR A 106 LYS A 117 1 12 HELIX 16 AB7 TRP A 120 ASP A 124 1 5 HELIX 17 AB8 ARG A 128 ALA A 161 1 34 HELIX 18 AB9 ALA A 161 MET A 169 1 9 HELIX 19 AC1 LYS A 170 LEU A 190 1 21 HELIX 20 AC2 LEU A 190 GLY A 195 1 6 HELIX 21 AC3 ASN A 227 ALA A 264 1 38 HELIX 22 AC4 GLN A 272 PHE A 307 1 36 HELIX 23 AC5 GLU A 324 LEU A 347 1 24 HELIX 24 AC6 LEU A 347 LEU A 353 1 7 SHEET 1 AA1 2 TYR B 199 GLN B 202 0 SHEET 2 AA1 2 TRP B 207 ILE B 210 -1 O TRP B 207 N GLN B 202 SHEET 1 AA2 2 TYR A 199 GLN A 202 0 SHEET 2 AA2 2 TRP A 207 ILE A 210 -1 O TRP A 207 N GLN A 202 SSBOND 1 CYS B 130 CYS B 208 1555 1555 2.04 SSBOND 2 CYS A 130 CYS A 208 1555 1555 2.04 CISPEP 1 TRP B 203 PRO B 204 0 2.82 CISPEP 2 TRP A 203 PRO A 204 0 2.98 SITE 1 AC1 12 MET B 58 GLN B 103 THR B 106 THR B 107 SITE 2 AC1 12 VAL B 110 TYR B 114 MET B 137 THR B 206 SITE 3 AC1 12 TRP B 207 ARG B 333 SER B 336 GLN B 339 SITE 1 AC2 10 SER A 49 ILE A 330 ARG A 333 LEU A 341 SITE 2 AC2 10 VAL B 50 SER B 51 VAL B 52 ALA B 53 SITE 3 AC2 10 THR B 57 TYR B 114 SITE 1 AC3 13 MET A 58 GLN A 103 THR A 106 THR A 107 SITE 2 AC3 13 VAL A 110 TYR A 114 MET A 137 THR A 206 SITE 3 AC3 13 TRP A 207 LEU A 329 ARG A 333 SER A 336 SITE 4 AC3 13 GLN A 339 SITE 1 AC4 10 VAL A 50 SER A 51 VAL A 52 ALA A 53 SITE 2 AC4 10 THR A 57 LEU A 60 GLY B 48 SER B 49 SITE 3 AC4 10 ILE B 330 ARG B 333 CRYST1 66.090 42.280 161.300 90.00 96.09 90.00 P 1 21 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.015131 0.000000 0.001614 0.00000 SCALE2 0.000000 0.023652 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006235 0.00000 ATOM 1 N CYS B 47 70.403 43.582 234.081 1.00 70.58 N ANISOU 1 N CYS B 47 9047 9709 8061 -2354 -1508 3569 N ATOM 2 CA CYS B 47 70.378 44.745 233.202 1.00 68.58 C ANISOU 2 CA CYS B 47 8669 9450 7938 -2287 -1351 3231 C ATOM 3 C CYS B 47 71.116 44.460 231.899 1.00 76.58 C ANISOU 3 C CYS B 47 9468 10184 9443 -1980 -1439 3210 C ATOM 4 O CYS B 47 71.848 45.310 231.391 1.00 78.17 O ANISOU 4 O CYS B 47 9525 10424 9752 -1888 -1481 3004 O ATOM 5 N GLY B 48 70.919 43.254 231.362 1.00 80.07 N ANISOU 5 N GLY B 48 9891 10350 10184 -1832 -1450 3393 N ATOM 6 CA GLY B 48 71.569 42.894 230.114 1.00 78.35 C ANISOU 6 CA GLY B 48 9471 9873 10425 -1551 -1502 3346 C ATOM 7 C GLY B 48 71.032 43.646 228.913 1.00 79.82 C ANISOU 7 C GLY B 48 9562 9968 10798 -1468 -1244 2993 C ATOM 8 O GLY B 48 71.779 43.935 227.974 1.00 79.29 O ANISOU 8 O GLY B 48 9318 9819 10990 -1294 -1280 2859 O ATOM 9 N SER B 49 69.738 43.971 228.921 1.00 79.85 N ANISOU 9 N SER B 49 9668 9999 10673 -1590 -982 2826 N ATOM 10 CA SER B 49 69.134 44.684 227.803 1.00 75.92 C ANISOU 10 CA SER B 49 9083 9418 10346 -1503 -756 2497 C ATOM 11 C SER B 49 69.354 46.189 227.874 1.00 73.82 C ANISOU 11 C SER B 49 8791 9335 9921 -1558 -708 2225 C ATOM 12 O SER B 49 69.193 46.873 226.857 1.00 75.65 O ANISOU 12 O SER B 49 8936 9483 10325 -1458 -589 1987 O ATOM 13 CB SER B 49 67.634 44.386 227.737 1.00 78.98 C ANISOU 13 CB SER B 49 9556 9761 10691 -1557 -508 2375 C ATOM 14 OG SER B 49 66.977 44.810 228.919 1.00 81.27 O ANISOU 14 OG SER B 49 9982 10275 10622 -1808 -417 2389 O ATOM 15 N VAL B 50 69.714 46.718 229.042 1.00 65.83 N ANISOU 15 N VAL B 50 7866 8564 8581 -1728 -803 2258 N ATOM 16 CA VAL B 50 69.933 48.153 229.216 1.00 53.70 C ANISOU 16 CA VAL B 50 6326 7187 6890 -1807 -759 1986 C ATOM 17 C VAL B 50 71.337 48.468 228.704 1.00 46.06 C ANISOU 17 C VAL B 50 5208 6203 6088 -1697 -956 1991 C ATOM 18 O VAL B 50 72.321 48.315 229.428 1.00 43.47 O ANISOU 18 O VAL B 50 4862 6020 5634 -1754 -1191 2156 O ATOM 19 CB VAL B 50 69.751 48.583 230.673 1.00 48.00 C ANISOU 19 CB VAL B 50 5758 6745 5734 -2058 -768 1981 C ATOM 20 CG1 VAL B 50 69.639 50.100 230.771 1.00 39.22 C ANISOU 20 CG1 VAL B 50 4661 5741 4500 -2140 -646 1624 C ATOM 21 CG2 VAL B 50 68.529 47.905 231.273 1.00 53.44 C ANISOU 21 CG2 VAL B 50 6579 7469 6254 -2184 -603 2068 C ATOM 22 N SER B 51 71.431 48.917 227.453 1.00 44.18 N ANISOU 22 N SER B 51 4854 5810 6124 -1553 -866 1814 N ATOM 23 CA SER B 51 72.715 49.234 226.838 1.00 33.60 C ANISOU 23 CA SER B 51 3352 4459 4957 -1466 -1007 1792 C ATOM 24 C SER B 51 72.462 50.097 225.611 1.00 34.14 C ANISOU 24 C SER B 51 3366 4399 5207 -1393 -837 1541 C ATOM 25 O SER B 51 71.570 49.791 224.813 1.00 46.77 O ANISOU 25 O SER B 51 4977 5839 6954 -1299 -679 1489 O ATOM 26 CB SER B 51 73.479 47.960 226.454 1.00 43.12 C ANISOU 26 CB SER B 51 4421 5552 6409 -1300 -1169 2033 C ATOM 27 OG SER B 51 74.681 48.268 225.768 1.00 34.09 O ANISOU 27 OG SER B 51 3083 4412 5456 -1212 -1268 1975 O ATOM 28 N VAL B 52 73.251 51.164 225.461 1.00 38.91 N ANISOU 28 N VAL B 52 3916 5074 5795 -1453 -880 1398 N ATOM 29 CA VAL B 52 73.117 52.088 224.338 1.00 28.91 C ANISOU 29 CA VAL B 52 2622 3687 4677 -1413 -743 1192 C ATOM 30 C VAL B 52 73.678 51.478 223.058 1.00 27.72 C ANISOU 30 C VAL B 52 2315 3413 4806 -1249 -746 1240 C ATOM 31 O VAL B 52 73.559 52.067 221.978 1.00 26.18 O ANISOU 31 O VAL B 52 2158 3123 4665 -1151 -612 1065 O ATOM 32 CB VAL B 52 73.804 53.431 224.651 1.00 37.67 C ANISOU 32 CB VAL B 52 3744 4896 5672 -1565 -787 1031 C ATOM 33 CG1 VAL B 52 75.299 53.348 224.374 1.00 30.67 C ANISOU 33 CG1 VAL B 52 2672 4088 4893 -1565 -954 1101 C ATOM 34 CG2 VAL B 52 73.157 54.564 223.861 1.00 45.02 C ANISOU 34 CG2 VAL B 52 4750 5678 6677 -1567 -615 814 C ATOM 35 N ALA B 53 74.281 50.291 223.162 1.00 32.51 N ANISOU 35 N ALA B 53 2806 4023 5525 -1160 -876 1435 N ATOM 36 CA ALA B 53 74.835 49.643 221.976 1.00 36.14 C ANISOU 36 CA ALA B 53 3140 4369 6224 -971 -847 1424 C ATOM 37 C ALA B 53 73.747 49.236 220.992 1.00 35.49 C ANISOU 37 C ALA B 53 3155 4118 6212 -839 -658 1331 C ATOM 38 O ALA B 53 74.001 49.171 219.784 1.00 25.14 O ANISOU 38 O ALA B 53 1817 2737 4997 -716 -569 1214 O ATOM 39 CB ALA B 53 75.666 48.423 222.376 1.00 33.50 C ANISOU 39 CB ALA B 53 2628 4044 6055 -898 -1045 1657 C ATOM 40 N PHE B 54 72.537 48.969 221.482 1.00 35.90 N ANISOU 40 N PHE B 54 3326 4131 6185 -879 -594 1367 N ATOM 41 CA PHE B 54 71.437 48.546 220.622 1.00 33.53 C ANISOU 41 CA PHE B 54 3106 3711 5925 -756 -438 1261 C ATOM 42 C PHE B 54 70.848 49.712 219.828 1.00 26.97 C ANISOU 42 C PHE B 54 2370 2882 4996 -737 -305 1030 C ATOM 43 O PHE B 54 70.726 49.600 218.601 1.00 22.25 O ANISOU 43 O PHE B 54 1772 2225 4457 -622 -237 933 O ATOM 44 CB PHE B 54 70.352 47.842 221.444 1.00 38.18 C ANISOU 44 CB PHE B 54 3781 4278 6446 -811 -406 1364 C ATOM 45 CG PHE B 54 70.796 46.536 222.037 1.00 43.56 C ANISOU 45 CG PHE B 54 4406 4905 7241 -812 -539 1628 C ATOM 46 CD1 PHE B 54 70.926 45.408 221.243 1.00 48.54 C ANISOU 46 CD1 PHE B 54 4963 5383 8097 -658 -538 1658 C ATOM 47 CD2 PHE B 54 71.089 46.436 223.387 1.00 49.39 C ANISOU 47 CD2 PHE B 54 5183 5744 7839 -964 -674 1845 C ATOM 48 CE1 PHE B 54 71.339 44.202 221.785 1.00 54.23 C ANISOU 48 CE1 PHE B 54 5645 6006 8954 -636 -671 1905 C ATOM 49 CE2 PHE B 54 71.502 45.234 223.936 1.00 58.94 C ANISOU 49 CE2 PHE B 54 6389 6896 9112 -923 -823 2100 C ATOM 50 CZ PHE B 54 71.627 44.116 223.133 1.00 56.81 C ANISOU 50 CZ PHE B 54 6036 6410 9140 -766 -826 2162 C ATOM 51 N PRO B 55 70.463 50.837 220.456 1.00 22.67 N ANISOU 51 N PRO B 55 1900 2395 4316 -858 -274 950 N ATOM 52 CA PRO B 55 69.914 51.943 219.649 1.00 21.48 C ANISOU 52 CA PRO B 55 1825 2205 4131 -830 -174 769 C ATOM 53 C PRO B 55 70.901 52.511 218.643 1.00 21.09 C ANISOU 53 C PRO B 55 1750 2157 4108 -795 -191 711 C ATOM 54 O PRO B 55 70.502 52.864 217.526 1.00 20.09 O ANISOU 54 O PRO B 55 1669 1981 3985 -723 -128 630 O ATOM 55 CB PRO B 55 69.512 52.984 220.705 1.00 32.21 C ANISOU 55 CB PRO B 55 3241 3599 5397 -991 -154 708 C ATOM 56 CG PRO B 55 70.305 52.642 221.909 1.00 23.99 C ANISOU 56 CG PRO B 55 2151 2671 4292 -1131 -275 847 C ATOM 57 CD PRO B 55 70.424 51.157 221.895 1.00 24.17 C ANISOU 57 CD PRO B 55 2114 2683 4386 -1044 -330 1025 C ATOM 58 N ILE B 56 72.182 52.611 219.006 1.00 34.67 N ANISOU 58 N ILE B 56 3389 3948 5837 -862 -282 763 N ATOM 59 CA ILE B 56 73.179 53.129 218.072 1.00 33.02 C ANISOU 59 CA ILE B 56 3143 3759 5643 -858 -274 701 C ATOM 60 C ILE B 56 73.331 52.193 216.879 1.00 29.93 C ANISOU 60 C ILE B 56 2696 3328 5347 -724 -232 708 C ATOM 61 O ILE B 56 73.373 52.633 215.724 1.00 32.84 O ANISOU 61 O ILE B 56 3100 3685 5691 -710 -163 628 O ATOM 62 CB ILE B 56 74.523 53.355 218.787 1.00 30.96 C ANISOU 62 CB ILE B 56 2774 3609 5381 -966 -385 743 C ATOM 63 CG1 ILE B 56 74.378 54.427 219.869 1.00 29.81 C ANISOU 63 CG1 ILE B 56 2697 3506 5122 -1135 -422 694 C ATOM 64 CG2 ILE B 56 75.601 53.748 217.785 1.00 24.09 C ANISOU 64 CG2 ILE B 56 1840 2778 4534 -973 -353 672 C ATOM 65 CD1 ILE B 56 75.645 54.676 220.656 1.00 26.56 C ANISOU 65 CD1 ILE B 56 2179 3235 4677 -1265 -560 726 C ATOM 66 N THR B 57 73.413 50.886 217.140 1.00 21.94 N ANISOU 66 N THR B 57 1597 2285 4453 -644 -277 812 N ATOM 67 CA THR B 57 73.526 49.921 216.052 1.00 21.68 C ANISOU 67 CA THR B 57 1508 2187 4544 -529 -226 795 C ATOM 68 C THR B 57 72.292 49.945 215.159 1.00 33.43 C ANISOU 68 C THR B 57 3106 3618 5977 -476 -129 709 C ATOM 69 O THR B 57 72.404 49.865 213.930 1.00 26.38 O ANISOU 69 O THR B 57 2209 2718 5096 -446 -66 632 O ATOM 70 CB THR B 57 73.749 48.517 216.615 1.00 27.16 C ANISOU 70 CB THR B 57 2089 2809 5422 -458 -301 937 C ATOM 71 OG1 THR B 57 74.896 48.520 217.474 1.00 24.46 O ANISOU 71 OG1 THR B 57 1620 2543 5130 -507 -431 1042 O ATOM 72 CG2 THR B 57 73.958 47.512 215.492 1.00 26.00 C ANISOU 72 CG2 THR B 57 1871 2564 5443 -349 -234 886 C ATOM 73 N MET B 58 71.104 50.063 215.758 1.00 32.69 N ANISOU 73 N MET B 58 3100 3504 5819 -481 -119 716 N ATOM 74 CA MET B 58 69.874 50.031 214.973 1.00 25.05 C ANISOU 74 CA MET B 58 2203 2498 4817 -429 -49 641 C ATOM 75 C MET B 58 69.697 51.293 214.135 1.00 21.06 C ANISOU 75 C MET B 58 1767 2015 4221 -464 -20 559 C ATOM 76 O MET B 58 69.101 51.235 213.053 1.00 20.64 O ANISOU 76 O MET B 58 1734 1943 4165 -428 16 514 O ATOM 77 CB MET B 58 68.676 49.812 215.897 1.00 22.85 C ANISOU 77 CB MET B 58 1969 2205 4507 -440 -36 663 C ATOM 78 CG MET B 58 68.642 48.416 216.511 1.00 32.06 C ANISOU 78 CG MET B 58 3083 3330 5770 -416 -59 767 C ATOM 79 SD MET B 58 67.190 48.080 217.531 1.00 39.77 S ANISOU 79 SD MET B 58 4121 4310 6681 -474 -11 790 S ATOM 80 CE MET B 58 67.462 49.219 218.886 1.00 46.42 C ANISOU 80 CE MET B 58 5000 5231 7404 -618 -35 820 C ATOM 81 N LEU B 59 70.201 52.435 214.608 1.00 20.96 N ANISOU 81 N LEU B 59 1786 2033 4146 -551 -43 551 N ATOM 82 CA LEU B 59 70.093 53.662 213.823 1.00 31.62 C ANISOU 82 CA LEU B 59 3204 3369 5440 -598 -25 502 C ATOM 83 C LEU B 59 71.002 53.621 212.600 1.00 30.77 C ANISOU 83 C LEU B 59 3066 3302 5324 -625 -3 490 C ATOM 84 O LEU B 59 70.616 54.082 211.518 1.00 35.12 O ANISOU 84 O LEU B 59 3665 3835 5843 -643 20 474 O ATOM 85 CB LEU B 59 70.420 54.876 214.694 1.00 35.43 C ANISOU 85 CB LEU B 59 3737 3846 5880 -704 -49 485 C ATOM 86 CG LEU B 59 70.461 56.243 214.001 1.00 30.19 C ANISOU 86 CG LEU B 59 3159 3129 5185 -773 -41 454 C ATOM 87 CD1 LEU B 59 69.152 56.542 213.282 1.00 19.11 C ANISOU 87 CD1 LEU B 59 1805 1638 3818 -700 -32 450 C ATOM 88 CD2 LEU B 59 70.787 57.341 215.002 1.00 27.77 C ANISOU 88 CD2 LEU B 59 2905 2787 4858 -890 -60 417 C ATOM 89 N LEU B 60 72.208 53.066 212.747 1.00 32.92 N ANISOU 89 N LEU B 60 3242 3631 5634 -644 -9 503 N ATOM 90 CA LEU B 60 73.159 53.067 211.639 1.00 35.60 C ANISOU 90 CA LEU B 60 3527 4033 5966 -700 37 469 C ATOM 91 C LEU B 60 72.764 52.064 210.562 1.00 31.31 C ANISOU 91 C LEU B 60 2951 3476 5470 -635 90 438 C ATOM 92 O LEU B 60 72.828 52.373 209.366 1.00 22.78 O ANISOU 92 O LEU B 60 1888 2436 4331 -707 142 403 O ATOM 93 CB LEU B 60 74.567 52.774 212.154 1.00 38.41 C ANISOU 93 CB LEU B 60 3749 4464 6381 -736 15 475 C ATOM 94 CG LEU B 60 75.152 53.769 213.159 1.00 33.25 C ANISOU 94 CG LEU B 60 3105 3850 5678 -842 -40 487 C ATOM 95 CD1 LEU B 60 76.548 53.338 213.588 1.00 27.04 C ANISOU 95 CD1 LEU B 60 2143 3163 4968 -870 -80 495 C ATOM 96 CD2 LEU B 60 75.170 55.178 212.579 1.00 24.02 C ANISOU 96 CD2 LEU B 60 2047 2679 4401 -974 0 444 C ATOM 97 N THR B 61 72.351 50.858 210.961 1.00 32.01 N ANISOU 97 N THR B 61 2993 3503 5665 -524 80 454 N ATOM 98 CA THR B 61 71.939 49.866 209.975 1.00 19.44 C ANISOU 98 CA THR B 61 1371 1880 4137 -475 137 402 C ATOM 99 C THR B 61 70.641 50.269 209.286 1.00 22.72 C ANISOU 99 C THR B 61 1885 2281 4467 -487 145 384 C ATOM 100 O THR B 61 70.462 49.993 208.095 1.00 30.77 O ANISOU 100 O THR B 61 2892 3326 5474 -525 195 330 O ATOM 101 CB THR B 61 71.789 48.492 210.629 1.00 21.86 C ANISOU 101 CB THR B 61 1612 2086 4610 -368 122 431 C ATOM 102 OG1 THR B 61 70.778 48.548 211.642 1.00 41.08 O ANISOU 102 OG1 THR B 61 4117 4477 7015 -334 72 496 O ATOM 103 CG2 THR B 61 73.101 48.050 211.254 1.00 20.90 C ANISOU 103 CG2 THR B 61 1360 1960 4618 -351 91 472 C ATOM 104 N GLY B 62 69.730 50.917 210.014 1.00 24.12 N ANISOU 104 N GLY B 62 2139 2425 4599 -466 98 424 N ATOM 105 CA GLY B 62 68.502 51.388 209.394 1.00 17.58 C ANISOU 105 CA GLY B 62 1370 1576 3732 -469 90 416 C ATOM 106 C GLY B 62 68.741 52.504 208.395 1.00 22.90 C ANISOU 106 C GLY B 62 2093 2278 4330 -575 88 430 C ATOM 107 O GLY B 62 68.103 52.550 207.339 1.00 21.86 O ANISOU 107 O GLY B 62 1975 2147 4186 -612 88 429 O ATOM 108 N PHE B 63 69.659 53.421 208.713 1.00 23.87 N ANISOU 108 N PHE B 63 2244 2420 4403 -647 81 451 N ATOM 109 CA PHE B 63 69.965 54.517 207.797 1.00 23.05 C ANISOU 109 CA PHE B 63 2208 2324 4227 -776 86 481 C ATOM 110 C PHE B 63 70.584 54.000 206.504 1.00 29.85 C ANISOU 110 C PHE B 63 3019 3278 5043 -878 156 451 C ATOM 111 O PHE B 63 70.167 54.385 205.406 1.00 20.95 O ANISOU 111 O PHE B 63 1941 2152 3869 -971 161 485 O ATOM 112 CB PHE B 63 70.896 55.525 208.474 1.00 19.97 C ANISOU 112 CB PHE B 63 1857 1933 3800 -854 78 493 C ATOM 113 CG PHE B 63 71.320 56.658 207.577 1.00 36.35 C ANISOU 113 CG PHE B 63 4017 3993 5802 -1008 96 530 C ATOM 114 CD1 PHE B 63 70.538 57.796 207.458 1.00 40.87 C ANISOU 114 CD1 PHE B 63 4710 4435 6384 -1018 39 597 C ATOM 115 CD2 PHE B 63 72.501 56.586 206.854 1.00 30.42 C ANISOU 115 CD2 PHE B 63 3221 3349 4988 -1149 176 502 C ATOM 116 CE1 PHE B 63 70.924 58.839 206.634 1.00 32.25 C ANISOU 116 CE1 PHE B 63 3720 3296 5238 -1159 51 660 C ATOM 117 CE2 PHE B 63 72.891 57.625 206.027 1.00 31.14 C ANISOU 117 CE2 PHE B 63 3400 3416 5014 -1311 219 542 C ATOM 118 CZ PHE B 63 72.102 58.752 205.918 1.00 24.28 C ANISOU 118 CZ PHE B 63 2678 2393 4155 -1311 150 637 C ATOM 119 N VAL B 64 71.590 53.129 206.615 1.00 27.68 N ANISOU 119 N VAL B 64 2636 3084 4798 -873 212 391 N ATOM 120 CA VAL B 64 72.310 52.659 205.433 1.00 25.96 C ANISOU 120 CA VAL B 64 2335 2981 4546 -984 302 335 C ATOM 121 C VAL B 64 71.384 51.857 204.527 1.00 23.76 C ANISOU 121 C VAL B 64 2041 2700 4286 -971 325 298 C ATOM 122 O VAL B 64 71.353 52.058 203.306 1.00 22.84 O ANISOU 122 O VAL B 64 1929 2663 4085 -1123 374 296 O ATOM 123 CB VAL B 64 73.546 51.839 205.847 1.00 25.68 C ANISOU 123 CB VAL B 64 2147 3011 4598 -940 347 272 C ATOM 124 CG1 VAL B 64 74.204 51.217 204.628 1.00 23.88 C ANISOU 124 CG1 VAL B 64 1796 2907 4369 -1024 459 190 C ATOM 125 CG2 VAL B 64 74.539 52.715 206.594 1.00 25.36 C ANISOU 125 CG2 VAL B 64 2100 3010 4525 -1004 322 303 C ATOM 126 N GLY B 65 70.618 50.934 205.111 1.00 24.78 N ANISOU 126 N GLY B 65 2151 2743 4519 -816 295 271 N ATOM 127 CA GLY B 65 69.721 50.116 204.309 1.00 29.67 C ANISOU 127 CA GLY B 65 2748 3356 5169 -815 317 213 C ATOM 128 C GLY B 65 68.666 50.934 203.588 1.00 34.42 C ANISOU 128 C GLY B 65 3430 3955 5692 -905 259 279 C ATOM 129 O GLY B 65 68.409 50.732 202.398 1.00 34.40 O ANISOU 129 O GLY B 65 3401 4024 5647 -1031 292 247 O ATOM 130 N ASN B 66 68.044 51.878 204.299 1.00 30.66 N ANISOU 130 N ASN B 66 3038 3392 5219 -846 169 374 N ATOM 131 CA ASN B 66 66.967 52.663 203.704 1.00 23.94 C ANISOU 131 CA ASN B 66 2242 2492 4360 -892 80 465 C ATOM 132 C ASN B 66 67.491 53.709 202.728 1.00 31.18 C ANISOU 132 C ASN B 66 3234 3440 5174 -1072 72 566 C ATOM 133 O ASN B 66 66.776 54.093 201.796 1.00 31.68 O ANISOU 133 O ASN B 66 3333 3498 5207 -1165 -16 673 O ATOM 134 CB ASN B 66 66.136 53.328 204.801 1.00 22.07 C ANISOU 134 CB ASN B 66 2044 2139 4203 -757 -9 524 C ATOM 135 CG ASN B 66 65.243 52.346 205.528 1.00 34.24 C ANISOU 135 CG ASN B 66 3519 3657 5832 -625 -6 455 C ATOM 136 OD1 ASN B 66 64.667 51.447 204.917 1.00 39.35 O ANISOU 136 OD1 ASN B 66 4112 4336 6502 -640 5 398 O ATOM 137 ND2 ASN B 66 65.125 52.508 206.841 1.00 41.90 N ANISOU 137 ND2 ASN B 66 4497 4581 6843 -523 -10 454 N ATOM 138 N ALA B 67 68.726 54.181 202.917 1.00 39.24 N ANISOU 138 N ALA B 67 4282 4498 6129 -1138 144 557 N ATOM 139 CA ALA B 67 69.275 55.172 201.997 1.00 24.25 C ANISOU 139 CA ALA B 67 2471 2625 4118 -1324 160 658 C ATOM 140 C ALA B 67 69.640 54.540 200.660 1.00 25.72 C ANISOU 140 C ALA B 67 2594 2971 4210 -1501 262 617 C ATOM 141 O ALA B 67 69.432 55.148 199.603 1.00 27.42 O ANISOU 141 O ALA B 67 2911 3243 4265 -1663 205 759 O ATOM 142 CB ALA B 67 70.491 55.857 202.619 1.00 24.44 C ANISOU 142 CB ALA B 67 2524 2647 4116 -1358 225 634 C ATOM 143 N LEU B 68 70.188 53.323 200.685 1.00 25.45 N ANISOU 143 N LEU B 68 2409 3040 4220 -1489 395 431 N ATOM 144 CA LEU B 68 70.498 52.630 199.439 1.00 36.88 C ANISOU 144 CA LEU B 68 3753 4641 5619 -1620 497 373 C ATOM 145 C LEU B 68 69.231 52.318 198.653 1.00 35.84 C ANISOU 145 C LEU B 68 3685 4573 5361 -1702 410 376 C ATOM 146 O LEU B 68 69.234 52.354 197.416 1.00 37.28 O ANISOU 146 O LEU B 68 3941 4932 5291 -1869 439 356 O ATOM 147 CB LEU B 68 71.278 51.347 199.729 1.00 43.82 C ANISOU 147 CB LEU B 68 4470 5602 6576 -1512 590 197 C ATOM 148 CG LEU B 68 72.666 51.500 200.356 1.00 27.13 C ANISOU 148 CG LEU B 68 2284 3529 4497 -1469 633 194 C ATOM 149 CD1 LEU B 68 73.299 50.138 200.589 1.00 28.99 C ANISOU 149 CD1 LEU B 68 2366 3782 4865 -1327 737 -11 C ATOM 150 CD2 LEU B 68 73.555 52.364 199.479 1.00 29.18 C ANISOU 150 CD2 LEU B 68 2559 3889 4639 -1647 733 237 C ATOM 151 N ALA B 69 68.139 52.003 199.354 1.00 34.42 N ANISOU 151 N ALA B 69 3488 4249 5342 -1524 289 389 N ATOM 152 CA ALA B 69 66.871 51.744 198.679 1.00 27.36 C ANISOU 152 CA ALA B 69 2646 3395 4354 -1512 168 384 C ATOM 153 C ALA B 69 66.359 52.998 197.981 1.00 29.38 C ANISOU 153 C ALA B 69 3081 3675 4408 -1601 -6 607 C ATOM 154 O ALA B 69 65.975 52.957 196.806 1.00 38.06 O ANISOU 154 O ALA B 69 4254 4934 5272 -1725 -62 615 O ATOM 155 CB ALA B 69 65.840 51.224 199.681 1.00 24.89 C ANISOU 155 CB ALA B 69 2255 2928 4276 -1317 89 355 C ATOM 156 N MET B 70 66.348 54.128 198.694 1.00 31.33 N ANISOU 156 N MET B 70 3406 3755 4744 -1544 -103 792 N ATOM 157 CA MET B 70 65.897 55.381 198.098 1.00 37.18 C ANISOU 157 CA MET B 70 4328 4457 5341 -1609 -285 1029 C ATOM 158 C MET B 70 66.815 55.829 196.969 1.00 47.15 C ANISOU 158 C MET B 70 5715 5886 6314 -1870 -216 1110 C ATOM 159 O MET B 70 66.378 56.545 196.060 1.00 53.96 O ANISOU 159 O MET B 70 6742 6790 6970 -1974 -370 1300 O ATOM 160 CB MET B 70 65.803 56.468 199.169 1.00 35.97 C ANISOU 160 CB MET B 70 4230 4056 5382 -1494 -373 1169 C ATOM 161 CG MET B 70 64.778 56.182 200.252 1.00 45.20 C ANISOU 161 CG MET B 70 5290 5080 6803 -1257 -440 1100 C ATOM 162 SD MET B 70 64.650 57.523 201.449 1.00 50.08 S ANISOU 162 SD MET B 70 5984 5428 7615 -1127 -521 1207 S ATOM 163 CE MET B 70 66.359 57.672 201.964 1.00 50.66 C ANISOU 163 CE MET B 70 6089 5579 7581 -1186 -311 1085 C ATOM 164 N LEU B 71 68.088 55.425 197.010 1.00 44.59 N ANISOU 164 N LEU B 71 5309 5665 5968 -1984 9 976 N ATOM 165 CA LEU B 71 69.023 55.807 195.957 1.00 42.31 C ANISOU 165 CA LEU B 71 5113 5568 5396 -2260 119 1024 C ATOM 166 C LEU B 71 68.724 55.069 194.657 1.00 42.88 C ANISOU 166 C LEU B 71 5202 5901 5191 -2393 155 914 C ATOM 167 O LEU B 71 68.840 55.644 193.569 1.00 47.02 O ANISOU 167 O LEU B 71 5890 6579 5397 -2623 123 1054 O ATOM 168 CB LEU B 71 70.458 55.546 196.419 1.00 48.07 C ANISOU 168 CB LEU B 71 5706 6338 6219 -2251 351 850 C ATOM 169 CG LEU B 71 71.629 56.146 195.629 1.00 43.54 C ANISOU 169 CG LEU B 71 5203 5917 5422 -2451 479 871 C ATOM 170 CD1 LEU B 71 72.065 55.238 194.485 1.00 48.78 C ANISOU 170 CD1 LEU B 71 5797 6882 5856 -2633 666 677 C ATOM 171 CD2 LEU B 71 71.277 57.535 195.113 1.00 42.13 C ANISOU 171 CD2 LEU B 71 5283 5668 5058 -2583 307 1167 C ATOM 172 N LEU B 72 68.336 53.794 194.749 1.00 38.91 N ANISOU 172 N LEU B 72 4543 5449 4792 -2273 219 664 N ATOM 173 CA LEU B 72 68.091 53.011 193.541 1.00 45.27 C ANISOU 173 CA LEU B 72 5355 6506 5340 -2413 273 502 C ATOM 174 C LEU B 72 66.778 53.403 192.875 1.00 48.14 C ANISOU 174 C LEU B 72 5863 6903 5526 -2424 0 676 C ATOM 175 O LEU B 72 66.681 53.411 191.642 1.00 51.12 O ANISOU 175 O LEU B 72 6351 7521 5552 -2638 -22 688 O ATOM 176 CB LEU B 72 68.098 51.517 193.869 1.00 47.77 C ANISOU 176 CB LEU B 72 5466 6825 5858 -2285 425 170 C ATOM 177 CG LEU B 72 69.413 50.920 194.374 1.00 48.56 C ANISOU 177 CG LEU B 72 5390 6920 6140 -2260 687 -34 C ATOM 178 CD1 LEU B 72 69.297 49.408 194.500 1.00 44.93 C ANISOU 178 CD1 LEU B 72 4761 6442 5870 -2141 809 -349 C ATOM 179 CD2 LEU B 72 70.568 51.300 193.459 1.00 52.22 C ANISOU 179 CD2 LEU B 72 5883 7623 6336 -2523 877 -70 C ATOM 180 N VAL B 73 65.752 53.723 193.669 1.00 41.76 N ANISOU 180 N VAL B 73 5044 5874 4948 -2201 -211 803 N ATOM 181 CA VAL B 73 64.461 54.068 193.081 1.00 43.92 C ANISOU 181 CA VAL B 73 5408 6179 5101 -2179 -492 959 C ATOM 182 C VAL B 73 64.521 55.427 192.395 1.00 46.43 C ANISOU 182 C VAL B 73 5956 6505 5179 -2323 -665 1297 C ATOM 183 O VAL B 73 63.861 55.641 191.371 1.00 44.12 O ANISOU 183 O VAL B 73 5779 6367 4617 -2431 -858 1427 O ATOM 184 CB VAL B 73 63.346 54.015 194.144 1.00 52.67 C ANISOU 184 CB VAL B 73 6402 7061 6548 -1896 -646 973 C ATOM 185 CG1 VAL B 73 63.168 52.594 194.655 1.00 42.77 C ANISOU 185 CG1 VAL B 73 4949 5815 5485 -1800 -496 666 C ATOM 186 CG2 VAL B 73 63.646 54.966 195.292 1.00 65.30 C ANISOU 186 CG2 VAL B 73 8025 8391 8396 -1755 -660 1126 C ATOM 187 N SER B 74 65.300 56.368 192.939 1.00 50.53 N ANISOU 187 N SER B 74 6556 6856 5789 -2339 -615 1456 N ATOM 188 CA SER B 74 65.468 57.655 192.273 1.00 48.65 C ANISOU 188 CA SER B 74 6560 6594 5331 -2508 -760 1789 C ATOM 189 C SER B 74 66.187 57.504 190.939 1.00 58.71 C ANISOU 189 C SER B 74 7951 8195 6162 -2852 -636 1786 C ATOM 190 O SER B 74 65.928 58.269 190.004 1.00 64.16 O ANISOU 190 O SER B 74 8859 8962 6559 -3023 -819 2064 O ATOM 191 CB SER B 74 66.235 58.620 193.179 1.00 42.69 C ANISOU 191 CB SER B 74 5856 5580 4782 -2482 -699 1915 C ATOM 192 OG SER B 74 65.563 58.808 194.412 1.00 43.49 O ANISOU 192 OG SER B 74 5863 5398 5262 -2183 -802 1901 O ATOM 193 N ARG B 75 67.085 56.523 190.835 1.00 66.11 N ANISOU 193 N ARG B 75 8744 9328 7044 -2957 -327 1474 N ATOM 194 CA ARG B 75 67.836 56.302 189.605 1.00 78.59 C ANISOU 194 CA ARG B 75 10404 11250 8206 -3294 -151 1404 C ATOM 195 C ARG B 75 66.991 55.616 188.536 1.00 81.44 C ANISOU 195 C ARG B 75 10799 11874 8270 -3381 -257 1312 C ATOM 196 O ARG B 75 67.111 55.935 187.348 1.00 90.54 O ANISOU 196 O ARG B 75 12133 13286 8984 -3673 -285 1434 O ATOM 197 CB ARG B 75 69.093 55.483 189.910 1.00 82.90 C ANISOU 197 CB ARG B 75 10746 11901 8850 -3344 224 1067 C ATOM 198 CG ARG B 75 69.798 54.900 188.693 1.00 93.49 C ANISOU 198 CG ARG B 75 12090 13628 9806 -3652 469 856 C ATOM 199 CD ARG B 75 69.548 53.402 188.575 1.00 98.65 C ANISOU 199 CD ARG B 75 12546 14400 10535 -3549 605 445 C ATOM 200 NE ARG B 75 70.230 52.819 187.424 1.00102.09 N ANISOU 200 NE ARG B 75 12972 15205 10615 -3838 867 187 N ATOM 201 CZ ARG B 75 70.139 51.540 187.072 1.00 98.13 C ANISOU 201 CZ ARG B 75 12327 14844 10115 -3818 1023 -207 C ATOM 202 NH1 ARG B 75 69.392 50.707 187.783 1.00 90.96 N ANISOU 202 NH1 ARG B 75 11283 13729 9547 -3534 933 -357 N ATOM 203 NH2 ARG B 75 70.794 51.094 186.009 1.00 99.63 N ANISOU 203 NH2 ARG B 75 12512 15377 9965 -4096 1281 -461 N ATOM 204 N SER B 76 66.124 54.684 188.936 1.00 80.57 N ANISOU 204 N SER B 76 10526 11712 8375 -3157 -322 1103 N ATOM 205 CA SER B 76 65.398 53.874 187.962 1.00 75.86 C ANISOU 205 CA SER B 76 9927 11380 7515 -3259 -391 942 C ATOM 206 C SER B 76 64.193 54.613 187.388 1.00 77.39 C ANISOU 206 C SER B 76 10283 11594 7528 -3260 -791 1267 C ATOM 207 O SER B 76 64.127 54.867 186.181 1.00 79.89 O ANISOU 207 O SER B 76 10776 12186 7395 -3527 -885 1389 O ATOM 208 CB SER B 76 64.964 52.553 188.603 1.00 72.37 C ANISOU 208 CB SER B 76 9246 10865 7388 -3046 -297 584 C ATOM 209 OG SER B 76 66.089 51.762 188.949 1.00 76.34 O ANISOU 209 OG SER B 76 9600 11377 8029 -3056 55 275 O ATOM 210 N TYR B 77 63.226 54.964 188.234 1.00 81.76 N ANISOU 210 N TYR B 77 10771 11871 8422 -2967 -1034 1411 N ATOM 211 CA TYR B 77 61.987 55.548 187.739 1.00 91.12 C ANISOU 211 CA TYR B 77 12048 13068 9504 -2917 -1432 1684 C ATOM 212 C TYR B 77 61.380 56.467 188.788 1.00 91.53 C ANISOU 212 C TYR B 77 12075 12744 9959 -2611 -1642 1924 C ATOM 213 O TYR B 77 61.421 56.170 189.985 1.00 86.52 O ANISOU 213 O TYR B 77 11271 11886 9718 -2386 -1510 1765 O ATOM 214 N ARG B 78 60.815 57.578 188.318 1.00 97.20 N ANISOU 214 N ARG B 78 12966 13396 10569 -2610 -1973 2307 N ATOM 215 CA ARG B 78 60.083 58.527 189.154 1.00 96.38 C ANISOU 215 CA ARG B 78 12844 12936 10841 -2311 -2216 2537 C ATOM 216 C ARG B 78 60.940 59.054 190.302 1.00 92.21 C ANISOU 216 C ARG B 78 12317 12098 10619 -2210 -2003 2529 C ATOM 217 O ARG B 78 60.944 60.252 190.585 1.00 95.60 O ANISOU 217 O ARG B 78 12886 12256 11181 -2135 -2151 2813 O ATOM 218 CB ARG B 78 58.808 57.879 189.702 1.00 96.13 C ANISOU 218 CB ARG B 78 12551 12867 11105 -2037 -2353 2360 C ATOM 219 CG ARG B 78 57.575 58.772 189.647 1.00 99.09 C ANISOU 219 CG ARG B 78 12926 13091 11634 -1822 -2770 2650 C ATOM 220 CD ARG B 78 57.614 59.857 190.711 1.00101.96 C ANISOU 220 CD ARG B 78 13312 13037 12391 -1578 -2803 2809 C ATOM 221 NE ARG B 78 56.295 60.441 190.937 1.00104.53 N ANISOU 221 NE ARG B 78 13526 13193 12997 -1287 -3148 2958 N ATOM 222 CZ ARG B 78 55.992 61.224 191.967 1.00105.20 C ANISOU 222 CZ ARG B 78 13551 12920 13499 -1010 -3188 3007 C ATOM 223 NH1 ARG B 78 54.764 61.710 192.093 1.00104.19 N ANISOU 223 NH1 ARG B 78 13281 12672 13636 -738 -3373 3001 N ATOM 224 NH2 ARG B 78 56.914 61.522 192.872 1.00104.90 N ANISOU 224 NH2 ARG B 78 13572 12663 13620 -1006 -2922 2933 N ATOM 225 N LYS B 86 57.664 52.030 187.277 1.00 69.28 N ANISOU 225 N LYS B 86 8622 10723 6977 -2633 -1934 889 N ATOM 226 CA LYS B 86 56.499 51.271 187.715 1.00 75.40 C ANISOU 226 CA LYS B 86 9162 11468 8020 -2483 -2043 704 C ATOM 227 C LYS B 86 56.050 51.714 189.103 1.00 85.54 C ANISOU 227 C LYS B 86 10299 12404 9798 -2152 -2079 809 C ATOM 228 O LYS B 86 56.798 52.369 189.829 1.00 81.51 O ANISOU 228 O LYS B 86 9859 11665 9446 -2046 -1950 940 O ATOM 229 CB LYS B 86 56.802 49.770 187.712 1.00 68.67 C ANISOU 229 CB LYS B 86 8195 10700 7196 -2596 -1742 251 C ATOM 230 CG LYS B 86 57.062 49.194 186.330 1.00 64.68 C ANISOU 230 CG LYS B 86 7801 10562 6212 -2927 -1702 63 C ATOM 231 CD LYS B 86 55.940 49.544 185.365 1.00 67.05 C ANISOU 231 CD LYS B 86 8132 11127 6217 -3031 -2107 228 C ATOM 232 CE LYS B 86 56.340 49.249 183.927 1.00 65.53 C ANISOU 232 CE LYS B 86 8113 11333 5451 -3398 -2081 111 C ATOM 233 NZ LYS B 86 55.692 50.183 182.966 1.00 67.00 N ANISOU 233 NZ LYS B 86 8445 11758 5255 -3512 -2500 477 N ATOM 234 N SER B 87 54.817 51.352 189.466 1.00 94.98 N ANISOU 234 N SER B 87 11282 13581 11226 -2008 -2247 734 N ATOM 235 CA SER B 87 54.280 51.732 190.767 1.00 96.79 C ANISOU 235 CA SER B 87 11351 13519 11906 -1711 -2268 799 C ATOM 236 C SER B 87 54.917 50.953 191.910 1.00 92.76 C ANISOU 236 C SER B 87 10754 12811 11678 -1641 -1908 560 C ATOM 237 O SER B 87 54.926 51.443 193.045 1.00 88.07 O ANISOU 237 O SER B 87 10105 11967 11391 -1433 -1854 641 O ATOM 238 CB SER B 87 52.763 51.539 190.787 1.00 97.99 C ANISOU 238 CB SER B 87 11270 13746 12218 -1601 -2536 768 C ATOM 239 OG SER B 87 52.137 52.331 189.793 1.00100.29 O ANISOU 239 OG SER B 87 11624 14203 12277 -1630 -2918 1028 O ATOM 240 N PHE B 88 55.443 49.755 191.642 1.00 92.00 N ANISOU 240 N PHE B 88 10648 12818 11488 -1810 -1670 266 N ATOM 241 CA PHE B 88 56.120 48.996 192.690 1.00 83.46 C ANISOU 241 CA PHE B 88 9500 11537 10675 -1741 -1352 71 C ATOM 242 C PHE B 88 57.391 49.700 193.149 1.00 79.78 C ANISOU 242 C PHE B 88 9171 10922 10219 -1699 -1189 209 C ATOM 243 O PHE B 88 57.711 49.694 194.343 1.00 81.35 O ANISOU 243 O PHE B 88 9310 10895 10703 -1545 -1048 204 O ATOM 244 CB PHE B 88 56.434 47.582 192.201 1.00 83.77 C ANISOU 244 CB PHE B 88 9507 11692 10630 -1922 -1150 -273 C ATOM 245 CG PHE B 88 55.278 46.629 192.322 1.00 90.93 C ANISOU 245 CG PHE B 88 10230 12626 11692 -1930 -1213 -473 C ATOM 246 CD1 PHE B 88 54.389 46.730 193.379 1.00 87.95 C ANISOU 246 CD1 PHE B 88 9687 12088 11643 -1744 -1283 -411 C ATOM 247 CD2 PHE B 88 55.083 45.630 191.382 1.00 95.39 C ANISOU 247 CD2 PHE B 88 10784 13389 12073 -2145 -1189 -744 C ATOM 248 CE1 PHE B 88 53.325 45.855 193.497 1.00 87.54 C ANISOU 248 CE1 PHE B 88 9453 12072 11735 -1781 -1327 -595 C ATOM 249 CE2 PHE B 88 54.019 44.752 191.493 1.00 88.07 C ANISOU 249 CE2 PHE B 88 9685 12480 11297 -2181 -1246 -936 C ATOM 250 CZ PHE B 88 53.140 44.865 192.552 1.00 86.91 C ANISOU 250 CZ PHE B 88 9366 12174 11483 -2004 -1315 -852 C ATOM 251 N LEU B 89 58.130 50.306 192.218 1.00 74.78 N ANISOU 251 N LEU B 89 8722 10429 9263 -1857 -1207 333 N ATOM 252 CA LEU B 89 59.296 51.095 192.605 1.00 67.56 C ANISOU 252 CA LEU B 89 7931 9387 8352 -1843 -1075 483 C ATOM 253 C LEU B 89 58.887 52.323 193.407 1.00 62.26 C ANISOU 253 C LEU B 89 7279 8489 7888 -1639 -1248 763 C ATOM 254 O LEU B 89 59.602 52.736 194.328 1.00 63.58 O ANISOU 254 O LEU B 89 7463 8460 8235 -1547 -1113 812 O ATOM 255 CB LEU B 89 60.091 51.505 191.366 1.00 72.17 C ANISOU 255 CB LEU B 89 8708 10193 8520 -2096 -1056 565 C ATOM 256 CG LEU B 89 60.897 50.405 190.673 1.00 72.78 C ANISOU 256 CG LEU B 89 8777 10474 8401 -2304 -791 251 C ATOM 257 CD1 LEU B 89 61.534 50.934 189.398 1.00 68.47 C ANISOU 257 CD1 LEU B 89 8428 10193 7396 -2580 -789 352 C ATOM 258 CD2 LEU B 89 61.954 49.846 191.613 1.00 63.55 C ANISOU 258 CD2 LEU B 89 7513 9133 7502 -2217 -482 71 C ATOM 259 N LEU B 90 57.743 52.922 193.070 1.00 58.59 N ANISOU 259 N LEU B 90 6802 8049 7409 -1564 -1553 935 N ATOM 260 CA LEU B 90 57.291 54.109 193.788 1.00 60.28 C ANISOU 260 CA LEU B 90 7024 8028 7852 -1350 -1723 1174 C ATOM 261 C LEU B 90 56.907 53.777 195.224 1.00 60.97 C ANISOU 261 C LEU B 90 6922 7912 8332 -1134 -1604 1033 C ATOM 262 O LEU B 90 57.220 54.537 196.148 1.00 64.02 O ANISOU 262 O LEU B 90 7338 8072 8913 -1000 -1558 1127 O ATOM 263 CB LEU B 90 56.113 54.750 193.054 1.00 63.84 C ANISOU 263 CB LEU B 90 7473 8556 8229 -1297 -2095 1378 C ATOM 264 CG LEU B 90 56.461 55.921 192.137 1.00 76.93 C ANISOU 264 CG LEU B 90 9379 10231 9619 -1402 -2296 1713 C ATOM 265 CD1 LEU B 90 55.210 56.473 191.473 1.00 84.22 C ANISOU 265 CD1 LEU B 90 10272 11220 10508 -1315 -2703 1924 C ATOM 266 CD2 LEU B 90 57.181 57.005 192.923 1.00 78.15 C ANISOU 266 CD2 LEU B 90 9658 10084 9952 -1302 -2223 1887 C ATOM 267 N CYS B 91 56.227 52.648 195.435 1.00 55.88 N ANISOU 267 N CYS B 91 6091 7348 7794 -1120 -1550 802 N ATOM 268 CA CYS B 91 55.788 52.299 196.781 1.00 44.40 C ANISOU 268 CA CYS B 91 4464 5727 6680 -948 -1436 682 C ATOM 269 C CYS B 91 56.956 51.886 197.666 1.00 38.48 C ANISOU 269 C CYS B 91 3754 4849 6019 -961 -1144 584 C ATOM 270 O CYS B 91 56.937 52.148 198.874 1.00 39.46 O ANISOU 270 O CYS B 91 3822 4796 6375 -819 -1066 590 O ATOM 271 CB CYS B 91 54.745 51.184 196.719 1.00 50.22 C ANISOU 271 CB CYS B 91 4999 6585 7497 -969 -1455 476 C ATOM 272 SG CYS B 91 53.814 50.967 198.250 1.00 58.78 S ANISOU 272 SG CYS B 91 5852 7509 8973 -773 -1381 380 S ATOM 273 N ILE B 92 57.975 51.243 197.092 1.00 43.64 N ANISOU 273 N ILE B 92 4491 5601 6490 -1130 -984 484 N ATOM 274 CA ILE B 92 59.140 50.843 197.876 1.00 34.97 C ANISOU 274 CA ILE B 92 3407 4392 5488 -1131 -732 400 C ATOM 275 C ILE B 92 59.975 52.061 198.250 1.00 31.80 C ANISOU 275 C ILE B 92 3135 3872 5077 -1098 -729 593 C ATOM 276 O ILE B 92 60.549 52.126 199.345 1.00 35.91 O ANISOU 276 O ILE B 92 3633 4246 5767 -1019 -601 581 O ATOM 277 CB ILE B 92 59.966 49.797 197.104 1.00 31.97 C ANISOU 277 CB ILE B 92 3045 4151 4950 -1303 -560 207 C ATOM 278 CG1 ILE B 92 59.168 48.501 196.947 1.00 31.33 C ANISOU 278 CG1 ILE B 92 2835 4127 4940 -1334 -537 -18 C ATOM 279 CG2 ILE B 92 61.285 49.515 197.808 1.00 27.79 C ANISOU 279 CG2 ILE B 92 2520 3517 4523 -1291 -331 148 C ATOM 280 CD1 ILE B 92 59.846 47.473 196.072 1.00 36.25 C ANISOU 280 CD1 ILE B 92 3477 4880 5417 -1502 -379 -248 C ATOM 281 N GLY B 93 60.046 53.051 197.357 1.00 36.90 N ANISOU 281 N GLY B 93 3924 4577 5519 -1173 -880 781 N ATOM 282 CA GLY B 93 60.835 54.239 197.645 1.00 38.33 C ANISOU 282 CA GLY B 93 4244 4626 5693 -1174 -880 968 C ATOM 283 C GLY B 93 60.313 55.012 198.840 1.00 46.43 C ANISOU 283 C GLY B 93 5231 5417 6992 -968 -949 1046 C ATOM 284 O GLY B 93 61.082 55.436 199.707 1.00 59.63 O ANISOU 284 O GLY B 93 6938 6949 8769 -941 -836 1061 O ATOM 285 N TRP B 94 58.995 55.210 198.901 1.00 39.63 N ANISOU 285 N TRP B 94 4283 4523 6249 -825 -1133 1076 N ATOM 286 CA TRP B 94 58.400 55.929 200.019 1.00 38.16 C ANISOU 286 CA TRP B 94 4036 4128 6334 -621 -1180 1106 C ATOM 287 C TRP B 94 58.261 55.066 201.266 1.00 27.21 C ANISOU 287 C TRP B 94 2489 2707 5143 -543 -994 905 C ATOM 288 O TRP B 94 58.106 55.611 202.365 1.00 26.52 O ANISOU 288 O TRP B 94 2371 2461 5243 -416 -959 895 O ATOM 289 CB TRP B 94 57.038 56.493 199.613 1.00 49.54 C ANISOU 289 CB TRP B 94 5411 5555 7857 -483 -1446 1203 C ATOM 290 CG TRP B 94 57.138 57.553 198.557 1.00 57.91 C ANISOU 290 CG TRP B 94 6656 6591 8755 -534 -1669 1462 C ATOM 291 CD1 TRP B 94 56.971 57.390 197.212 1.00 57.65 C ANISOU 291 CD1 TRP B 94 6694 6757 8456 -672 -1826 1564 C ATOM 292 CD2 TRP B 94 57.437 58.941 198.758 1.00 59.87 C ANISOU 292 CD2 TRP B 94 7065 6598 9086 -469 -1763 1663 C ATOM 293 NE1 TRP B 94 57.145 58.589 196.564 1.00 63.64 N ANISOU 293 NE1 TRP B 94 7653 7417 9112 -699 -2022 1848 N ATOM 294 CE2 TRP B 94 57.432 59.557 197.491 1.00 61.71 C ANISOU 294 CE2 TRP B 94 7467 6881 9097 -572 -1986 1914 C ATOM 295 CE3 TRP B 94 57.707 59.722 199.887 1.00 59.30 C ANISOU 295 CE3 TRP B 94 7019 6267 9245 -348 -1682 1650 C ATOM 296 CZ2 TRP B 94 57.686 60.918 197.320 1.00 56.74 C ANISOU 296 CZ2 TRP B 94 7041 6022 8497 -553 -2133 2173 C ATOM 297 CZ3 TRP B 94 57.959 61.072 199.715 1.00 59.92 C ANISOU 297 CZ3 TRP B 94 7288 6115 9363 -328 -1819 1871 C ATOM 298 CH2 TRP B 94 57.946 61.656 198.442 1.00 51.68 C ANISOU 298 CH2 TRP B 94 6419 5097 8122 -427 -2044 2140 C ATOM 299 N LEU B 95 58.309 53.740 201.126 1.00 26.37 N ANISOU 299 N LEU B 95 2291 2737 4992 -627 -875 744 N ATOM 300 CA LEU B 95 58.365 52.884 202.306 1.00 33.53 C ANISOU 300 CA LEU B 95 3085 3594 6062 -585 -693 595 C ATOM 301 C LEU B 95 59.713 53.010 203.003 1.00 37.50 C ANISOU 301 C LEU B 95 3675 4013 6562 -623 -535 609 C ATOM 302 O LEU B 95 59.777 53.087 204.236 1.00 30.19 O ANISOU 302 O LEU B 95 2715 2985 5771 -545 -452 579 O ATOM 303 CB LEU B 95 58.091 51.429 201.920 1.00 24.41 C ANISOU 303 CB LEU B 95 1829 2565 4882 -672 -618 432 C ATOM 304 CG LEU B 95 58.245 50.402 203.045 1.00 22.84 C ANISOU 304 CG LEU B 95 1596 2314 4768 -626 -419 300 C ATOM 305 CD1 LEU B 95 57.254 50.670 204.170 1.00 22.61 C ANISOU 305 CD1 LEU B 95 1505 2218 4870 -487 -416 288 C ATOM 306 CD2 LEU B 95 58.094 48.984 202.515 1.00 23.22 C ANISOU 306 CD2 LEU B 95 1618 2458 4746 -707 -341 143 C ATOM 307 N ALA B 96 60.801 53.033 202.228 1.00 42.30 N ANISOU 307 N ALA B 96 4387 4686 7000 -753 -492 645 N ATOM 308 CA ALA B 96 62.122 53.245 202.809 1.00 27.74 C ANISOU 308 CA ALA B 96 2602 2786 5154 -795 -362 660 C ATOM 309 C ALA B 96 62.231 54.630 203.430 1.00 22.35 C ANISOU 309 C ALA B 96 2011 1954 4525 -735 -430 787 C ATOM 310 O ALA B 96 62.880 54.805 204.468 1.00 21.30 O ANISOU 310 O ALA B 96 1919 1800 4375 -657 -330 729 O ATOM 311 CB ALA B 96 63.202 53.044 201.746 1.00 23.00 C ANISOU 311 CB ALA B 96 2064 2312 4363 -961 -292 656 C ATOM 312 N LEU B 97 61.604 55.631 202.804 1.00 29.45 N ANISOU 312 N LEU B 97 2992 2803 5394 -712 -600 920 N ATOM 313 CA LEU B 97 61.604 56.974 203.375 1.00 24.49 C ANISOU 313 CA LEU B 97 2459 1984 4862 -644 -673 1026 C ATOM 314 C LEU B 97 60.791 57.029 204.660 1.00 32.71 C ANISOU 314 C LEU B 97 3391 2915 6120 -475 -652 925 C ATOM 315 O LEU B 97 61.142 57.771 205.584 1.00 23.55 O ANISOU 315 O LEU B 97 2283 1658 5007 -423 -605 898 O ATOM 316 CB LEU B 97 61.070 57.980 202.353 1.00 26.85 C ANISOU 316 CB LEU B 97 2877 2229 5097 -638 -884 1210 C ATOM 317 CG LEU B 97 61.416 59.464 202.542 1.00 48.69 C ANISOU 317 CG LEU B 97 5809 4771 7921 -631 -966 1363 C ATOM 318 CD1 LEU B 97 61.408 60.180 201.200 1.00 52.34 C ANISOU 318 CD1 LEU B 97 6438 5233 8215 -730 -1144 1593 C ATOM 319 CD2 LEU B 97 60.457 60.152 203.504 1.00 44.90 C ANISOU 319 CD2 LEU B 97 5269 4103 7689 -410 -1031 1306 C ATOM 320 N THR B 98 59.708 56.254 204.741 1.00 37.93 N ANISOU 320 N THR B 98 3902 3654 6857 -389 -666 829 N ATOM 321 CA THR B 98 58.912 56.218 205.963 1.00 42.84 C ANISOU 321 CA THR B 98 4402 4211 7663 -258 -612 715 C ATOM 322 C THR B 98 59.716 55.636 207.119 1.00 33.22 C ANISOU 322 C THR B 98 3179 3015 6427 -302 -425 623 C ATOM 323 O THR B 98 59.751 56.206 208.216 1.00 33.30 O ANISOU 323 O THR B 98 3205 2961 6486 -238 -369 571 O ATOM 324 CB THR B 98 57.635 55.407 205.736 1.00 44.22 C ANISOU 324 CB THR B 98 4402 4496 7905 -198 -651 629 C ATOM 325 OG1 THR B 98 56.921 55.941 204.613 1.00 34.31 O ANISOU 325 OG1 THR B 98 3148 3259 6630 -150 -859 726 O ATOM 326 CG2 THR B 98 56.745 55.460 206.970 1.00 42.61 C ANISOU 326 CG2 THR B 98 4059 4246 7884 -79 -577 506 C ATOM 327 N ASP B 99 60.371 54.495 206.890 1.00 22.03 N ANISOU 327 N ASP B 99 1779 1753 4837 -356 -327 573 N ATOM 328 CA ASP B 99 61.130 53.842 207.952 1.00 26.48 C ANISOU 328 CA ASP B 99 2386 2390 5286 -329 -187 492 C ATOM 329 C ASP B 99 62.311 54.685 208.416 1.00 29.30 C ANISOU 329 C ASP B 99 2847 2734 5553 -357 -168 523 C ATOM 330 O ASP B 99 62.661 54.660 209.601 1.00 24.86 O ANISOU 330 O ASP B 99 2298 2184 4963 -332 -106 477 O ATOM 331 CB ASP B 99 61.610 52.469 207.484 1.00 28.03 C ANISOU 331 CB ASP B 99 2593 2695 5363 -367 -118 438 C ATOM 332 CG ASP B 99 60.465 51.542 207.131 1.00 38.19 C ANISOU 332 CG ASP B 99 3795 4008 6707 -359 -123 377 C ATOM 333 OD1 ASP B 99 59.297 51.919 207.370 1.00 36.02 O ANISOU 333 OD1 ASP B 99 3436 3690 6562 -316 -173 371 O ATOM 334 OD2 ASP B 99 60.731 50.438 206.613 1.00 40.07 O ANISOU 334 OD2 ASP B 99 4040 4310 6876 -402 -75 318 O ATOM 335 N LEU B 100 62.937 55.437 207.506 1.00 28.47 N ANISOU 335 N LEU B 100 2823 2608 5388 -434 -224 603 N ATOM 336 CA LEU B 100 64.101 56.231 207.887 1.00 25.50 C ANISOU 336 CA LEU B 100 2548 2226 4913 -486 -197 617 C ATOM 337 C LEU B 100 63.707 57.416 208.761 1.00 30.11 C ANISOU 337 C LEU B 100 3168 2681 5590 -440 -232 612 C ATOM 338 O LEU B 100 64.383 57.711 209.753 1.00 20.88 O ANISOU 338 O LEU B 100 2037 1522 4374 -459 -180 561 O ATOM 339 CB LEU B 100 64.844 56.706 206.639 1.00 35.49 C ANISOU 339 CB LEU B 100 3902 3505 6078 -611 -226 705 C ATOM 340 CG LEU B 100 66.097 57.549 206.891 1.00 45.68 C ANISOU 340 CG LEU B 100 5292 4794 7269 -698 -189 714 C ATOM 341 CD1 LEU B 100 67.075 56.804 207.785 1.00 49.49 C ANISOU 341 CD1 LEU B 100 5725 5385 7695 -693 -94 618 C ATOM 342 CD2 LEU B 100 66.758 57.934 205.579 1.00 39.06 C ANISOU 342 CD2 LEU B 100 4535 3982 6324 -851 -193 805 C ATOM 343 N VAL B 101 62.622 58.108 208.407 1.00 37.97 N ANISOU 343 N VAL B 101 4152 3543 6732 -382 -331 657 N ATOM 344 CA VAL B 101 62.170 59.245 209.207 1.00 32.73 C ANISOU 344 CA VAL B 101 3523 2728 6186 -315 -355 617 C ATOM 345 C VAL B 101 61.793 58.792 210.612 1.00 28.51 C ANISOU 345 C VAL B 101 2893 2217 5722 -267 -251 484 C ATOM 346 O VAL B 101 62.098 59.470 211.602 1.00 27.90 O ANISOU 346 O VAL B 101 2870 2079 5652 -280 -205 412 O ATOM 347 CB VAL B 101 60.999 59.960 208.505 1.00 34.12 C ANISOU 347 CB VAL B 101 3688 2750 6526 -217 -499 682 C ATOM 348 CG1 VAL B 101 60.420 61.047 209.399 1.00 32.30 C ANISOU 348 CG1 VAL B 101 3473 2359 6442 -110 -503 589 C ATOM 349 CG2 VAL B 101 61.455 60.547 207.177 1.00 28.44 C ANISOU 349 CG2 VAL B 101 3107 1996 5704 -294 -615 850 C ATOM 350 N GLY B 102 61.129 57.639 210.722 1.00 29.38 N ANISOU 350 N GLY B 102 2871 2409 5882 -236 -207 448 N ATOM 351 CA GLY B 102 60.777 57.114 212.031 1.00 20.70 C ANISOU 351 CA GLY B 102 1698 1344 4825 -223 -94 342 C ATOM 352 C GLY B 102 61.980 56.801 212.897 1.00 29.95 C ANISOU 352 C GLY B 102 2952 2618 5811 -300 -25 331 C ATOM 353 O GLY B 102 61.917 56.929 214.123 1.00 20.21 O ANISOU 353 O GLY B 102 1713 1371 4594 -329 45 256 O ATOM 354 N GLN B 103 63.089 56.388 212.280 1.00 32.86 N ANISOU 354 N GLN B 103 3383 3084 6017 -346 -46 396 N ATOM 355 CA GLN B 103 64.303 56.102 213.036 1.00 36.02 C ANISOU 355 CA GLN B 103 3836 3569 6279 -413 -12 394 C ATOM 356 C GLN B 103 65.052 57.370 213.432 1.00 29.89 C ANISOU 356 C GLN B 103 3151 2726 5479 -488 -32 382 C ATOM 357 O GLN B 103 65.682 57.403 214.495 1.00 25.21 O ANISOU 357 O GLN B 103 2579 2167 4832 -556 -6 351 O ATOM 358 CB GLN B 103 65.216 55.182 212.225 1.00 33.52 C ANISOU 358 CB GLN B 103 3522 3357 5856 -426 -16 437 C ATOM 359 CG GLN B 103 64.631 53.801 211.977 1.00 29.82 C ANISOU 359 CG GLN B 103 2990 2937 5404 -367 11 428 C ATOM 360 CD GLN B 103 65.270 53.100 210.795 1.00 30.75 C ANISOU 360 CD GLN B 103 3105 3105 5474 -380 10 442 C ATOM 361 OE1 GLN B 103 66.142 53.655 210.126 1.00 32.67 O ANISOU 361 OE1 GLN B 103 3384 3364 5664 -441 -1 463 O ATOM 362 NE2 GLN B 103 64.836 51.874 210.528 1.00 31.46 N ANISOU 362 NE2 GLN B 103 3153 3214 5587 -343 36 419 N ATOM 363 N LEU B 104 64.997 58.417 212.604 1.00 27.56 N ANISOU 363 N LEU B 104 2921 2329 5222 -494 -85 413 N ATOM 364 CA LEU B 104 65.691 59.660 212.927 1.00 36.00 C ANISOU 364 CA LEU B 104 4102 3306 6270 -576 -102 397 C ATOM 365 C LEU B 104 64.954 60.479 213.979 1.00 40.32 C ANISOU 365 C LEU B 104 4666 3704 6949 -551 -83 292 C ATOM 366 O LEU B 104 65.585 61.246 214.715 1.00 24.35 O ANISOU 366 O LEU B 104 2725 1626 4902 -642 -72 233 O ATOM 367 CB LEU B 104 65.891 60.500 211.664 1.00 26.30 C ANISOU 367 CB LEU B 104 2967 1998 5028 -605 -164 481 C ATOM 368 CG LEU B 104 66.776 59.909 210.565 1.00 27.80 C ANISOU 368 CG LEU B 104 3157 2317 5089 -676 -156 556 C ATOM 369 CD1 LEU B 104 66.814 60.835 209.357 1.00 26.30 C ANISOU 369 CD1 LEU B 104 3077 2029 4887 -733 -214 655 C ATOM 370 CD2 LEU B 104 68.179 59.637 211.084 1.00 29.24 C ANISOU 370 CD2 LEU B 104 3334 2616 5158 -778 -101 521 C ATOM 371 N LEU B 105 63.630 60.343 214.059 1.00 42.66 N ANISOU 371 N LEU B 105 4876 3928 7404 -438 -73 245 N ATOM 372 CA LEU B 105 62.837 61.077 215.037 1.00 42.60 C ANISOU 372 CA LEU B 105 4860 3768 7560 -396 -25 95 C ATOM 373 C LEU B 105 62.809 60.410 216.405 1.00 42.52 C ANISOU 373 C LEU B 105 4786 3841 7528 -470 88 -16 C ATOM 374 O LEU B 105 62.364 61.038 217.372 1.00 44.25 O ANISOU 374 O LEU B 105 5011 3950 7854 -483 163 -193 O ATOM 375 CB LEU B 105 61.400 61.236 214.533 1.00 33.92 C ANISOU 375 CB LEU B 105 3665 2557 6667 -235 -55 65 C ATOM 376 CG LEU B 105 61.137 62.225 213.399 1.00 33.50 C ANISOU 376 CG LEU B 105 3686 2368 6673 -153 -186 155 C ATOM 377 CD1 LEU B 105 59.713 62.072 212.896 1.00 28.05 C ANISOU 377 CD1 LEU B 105 2857 1632 6166 9 -240 142 C ATOM 378 CD2 LEU B 105 61.387 63.647 213.868 1.00 40.86 C ANISOU 378 CD2 LEU B 105 4757 3113 7655 -153 -196 74 C ATOM 379 N THR B 106 63.277 59.169 216.511 1.00 40.59 N ANISOU 379 N THR B 106 4494 3790 7140 -524 106 71 N ATOM 380 CA THR B 106 63.079 58.360 217.706 1.00 39.23 C ANISOU 380 CA THR B 106 4256 3722 6926 -600 202 15 C ATOM 381 C THR B 106 64.381 58.001 218.405 1.00 38.19 C ANISOU 381 C THR B 106 4180 3724 6607 -737 176 75 C ATOM 382 O THR B 106 64.493 58.172 219.625 1.00 23.96 O ANISOU 382 O THR B 106 2381 1947 4777 -866 233 -15 O ATOM 383 CB THR B 106 62.317 57.080 217.331 1.00 26.64 C ANISOU 383 CB THR B 106 2555 2231 5335 -531 231 79 C ATOM 384 OG1 THR B 106 61.053 57.430 216.754 1.00 45.81 O ANISOU 384 OG1 THR B 106 4891 4541 7974 -424 244 12 O ATOM 385 CG2 THR B 106 62.085 56.224 218.550 1.00 25.97 C ANISOU 385 CG2 THR B 106 2423 2272 5173 -628 331 54 C ATOM 386 N THR B 107 65.369 57.509 217.664 1.00 39.20 N ANISOU 386 N THR B 107 4333 3944 6619 -723 99 201 N ATOM 387 CA THR B 107 66.612 56.990 218.225 1.00 41.42 C ANISOU 387 CA THR B 107 4620 4352 6766 -824 60 266 C ATOM 388 C THR B 107 67.465 58.056 218.915 1.00 44.37 C ANISOU 388 C THR B 107 5054 4697 7108 -974 31 203 C ATOM 389 O THR B 107 68.015 57.778 219.989 1.00 32.98 O ANISOU 389 O THR B 107 3585 3349 5596 -1105 13 208 O ATOM 390 CB THR B 107 67.431 56.297 217.133 1.00 39.52 C ANISOU 390 CB THR B 107 4362 4184 6470 -755 12 360 C ATOM 391 OG1 THR B 107 66.556 55.537 216.291 1.00 30.31 O ANISOU 391 OG1 THR B 107 3156 3011 5348 -630 33 382 O ATOM 392 CG2 THR B 107 68.458 55.363 217.760 1.00 31.04 C ANISOU 392 CG2 THR B 107 3236 3226 5330 -806 -24 432 C ATOM 393 N PRO B 108 67.634 59.262 218.349 1.00 22.88 N ANISOU 393 N PRO B 108 2415 1851 4429 -979 11 151 N ATOM 394 CA PRO B 108 68.464 60.264 219.042 1.00 24.36 C ANISOU 394 CA PRO B 108 2672 2004 4581 -1143 -16 69 C ATOM 395 C PRO B 108 67.973 60.613 220.436 1.00 25.82 C ANISOU 395 C PRO B 108 2861 2152 4799 -1254 35 -95 C ATOM 396 O PRO B 108 68.786 60.978 221.295 1.00 27.07 O ANISOU 396 O PRO B 108 3039 2367 4880 -1434 0 -165 O ATOM 397 CB PRO B 108 68.402 61.476 218.103 1.00 26.54 C ANISOU 397 CB PRO B 108 3056 2108 4919 -1105 -32 49 C ATOM 398 CG PRO B 108 68.181 60.886 216.765 1.00 25.96 C ANISOU 398 CG PRO B 108 2948 2073 4844 -969 -42 173 C ATOM 399 CD PRO B 108 67.251 59.735 217.004 1.00 23.00 C ANISOU 399 CD PRO B 108 2468 1765 4504 -864 -5 186 C ATOM 400 N VAL B 109 66.667 60.516 220.691 1.00 37.99 N ANISOU 400 N VAL B 109 4375 3626 6433 -1164 133 -195 N ATOM 401 CA VAL B 109 66.156 60.771 222.034 1.00 39.70 C ANISOU 401 CA VAL B 109 4632 3931 6523 -1220 225 -389 C ATOM 402 C VAL B 109 66.606 59.676 222.994 1.00 34.00 C ANISOU 402 C VAL B 109 3871 3476 5571 -1332 209 -295 C ATOM 403 O VAL B 109 66.979 59.951 224.141 1.00 31.70 O ANISOU 403 O VAL B 109 3639 3317 5087 -1480 212 -400 O ATOM 404 CB VAL B 109 64.622 60.904 222.004 1.00 36.44 C ANISOU 404 CB VAL B 109 4181 3436 6229 -1064 349 -525 C ATOM 405 CG1 VAL B 109 64.077 61.116 223.407 1.00 34.97 C ANISOU 405 CG1 VAL B 109 4021 3376 5891 -1140 482 -754 C ATOM 406 CG2 VAL B 109 64.207 62.045 221.090 1.00 35.10 C ANISOU 406 CG2 VAL B 109 4054 2980 6302 -938 325 -594 C ATOM 407 N VAL B 110 66.581 58.420 222.541 1.00 31.32 N ANISOU 407 N VAL B 110 3442 3212 5247 -1268 179 -93 N ATOM 408 CA VAL B 110 66.957 57.302 223.403 1.00 26.42 C ANISOU 408 CA VAL B 110 2795 2805 4440 -1354 143 39 C ATOM 409 C VAL B 110 68.425 57.398 223.795 1.00 48.65 C ANISOU 409 C VAL B 110 5617 5725 7144 -1488 -3 115 C ATOM 410 O VAL B 110 68.801 57.101 224.936 1.00 37.85 O ANISOU 410 O VAL B 110 4277 4544 5558 -1616 -51 140 O ATOM 411 CB VAL B 110 66.644 55.964 222.706 1.00 24.83 C ANISOU 411 CB VAL B 110 2500 2599 4336 -1246 137 232 C ATOM 412 CG1 VAL B 110 67.029 54.793 223.597 1.00 25.55 C ANISOU 412 CG1 VAL B 110 2581 2863 4264 -1327 82 401 C ATOM 413 CG2 VAL B 110 65.173 55.893 222.325 1.00 24.43 C ANISOU 413 CG2 VAL B 110 2419 2469 4395 -1134 271 143 C ATOM 414 N ILE B 111 69.276 57.821 222.857 1.00 47.70 N ANISOU 414 N ILE B 111 5462 5503 7159 -1474 -81 156 N ATOM 415 CA ILE B 111 70.710 57.896 223.117 1.00 37.70 C ANISOU 415 CA ILE B 111 4155 4348 5822 -1600 -220 223 C ATOM 416 C ILE B 111 71.016 58.955 224.170 1.00 42.99 C ANISOU 416 C ILE B 111 4924 5084 6327 -1778 -236 39 C ATOM 417 O ILE B 111 71.884 58.761 225.030 1.00 45.09 O ANISOU 417 O ILE B 111 5168 5543 6422 -1914 -354 81 O ATOM 418 CB ILE B 111 71.468 58.158 221.803 1.00 36.22 C ANISOU 418 CB ILE B 111 3923 4067 5773 -1523 -238 261 C ATOM 419 CG1 ILE B 111 71.220 57.016 220.814 1.00 31.61 C ANISOU 419 CG1 ILE B 111 3285 3481 5244 -1313 -202 381 C ATOM 420 CG2 ILE B 111 72.958 58.326 222.063 1.00 43.37 C ANISOU 420 CG2 ILE B 111 4763 5102 6612 -1630 -352 284 C ATOM 421 CD1 ILE B 111 71.863 57.222 219.461 1.00 23.50 C ANISOU 421 CD1 ILE B 111 2257 2423 4248 -1221 -187 384 C ATOM 422 N VAL B 112 70.311 60.089 224.124 1.00 44.96 N ANISOU 422 N VAL B 112 5280 5168 6633 -1777 -129 -174 N ATOM 423 CA VAL B 112 70.550 61.159 225.091 1.00 42.28 C ANISOU 423 CA VAL B 112 5048 4859 6159 -1950 -123 -398 C ATOM 424 C VAL B 112 70.234 60.688 226.506 1.00 46.06 C ANISOU 424 C VAL B 112 5563 5581 6356 -2050 -99 -454 C ATOM 425 O VAL B 112 70.978 60.976 227.452 1.00 50.83 O ANISOU 425 O VAL B 112 6205 6358 6749 -2244 -184 -523 O ATOM 426 CB VAL B 112 69.736 62.411 224.714 1.00 37.90 C ANISOU 426 CB VAL B 112 4598 4028 5774 -1890 -3 -622 C ATOM 427 CG1 VAL B 112 69.808 63.451 225.821 1.00 41.90 C ANISOU 427 CG1 VAL B 112 5223 4550 6145 -2061 37 -907 C ATOM 428 CG2 VAL B 112 70.237 62.995 223.405 1.00 31.85 C ANISOU 428 CG2 VAL B 112 3832 3038 5234 -1855 -55 -539 C ATOM 429 N VAL B 113 69.129 59.956 226.673 1.00 42.79 N ANISOU 429 N VAL B 113 5139 5203 5917 -1943 14 -423 N ATOM 430 CA VAL B 113 68.740 59.481 227.999 1.00 43.98 C ANISOU 430 CA VAL B 113 5339 5598 5773 -2063 61 -461 C ATOM 431 C VAL B 113 69.794 58.534 228.562 1.00 48.01 C ANISOU 431 C VAL B 113 5809 6346 6086 -2174 -133 -210 C ATOM 432 O VAL B 113 70.076 58.540 229.767 1.00 53.84 O ANISOU 432 O VAL B 113 6616 7317 6522 -2362 -182 -250 O ATOM 433 CB VAL B 113 67.350 58.820 227.940 1.00 45.64 C ANISOU 433 CB VAL B 113 5524 5795 6023 -1938 230 -455 C ATOM 434 CG1 VAL B 113 66.942 58.302 229.312 1.00 36.68 C ANISOU 434 CG1 VAL B 113 4450 4931 4555 -2098 300 -478 C ATOM 435 CG2 VAL B 113 66.318 59.802 227.408 1.00 34.34 C ANISOU 435 CG2 VAL B 113 4101 4134 4812 -1806 394 -708 C ATOM 436 N TYR B 114 70.397 57.711 227.700 1.00 33.83 N ANISOU 436 N TYR B 114 3898 4497 4459 -2058 -253 45 N ATOM 437 CA TYR B 114 71.450 56.807 228.152 1.00 36.77 C ANISOU 437 CA TYR B 114 4202 5059 4710 -2121 -461 292 C ATOM 438 C TYR B 114 72.681 57.580 228.615 1.00 38.63 C ANISOU 438 C TYR B 114 4427 5416 4834 -2295 -618 217 C ATOM 439 O TYR B 114 73.185 57.359 229.722 1.00 38.82 O ANISOU 439 O TYR B 114 4478 5685 4587 -2454 -753 273 O ATOM 440 CB TYR B 114 71.825 55.834 227.033 1.00 37.86 C ANISOU 440 CB TYR B 114 4198 5082 5105 -1938 -530 526 C ATOM 441 CG TYR B 114 71.016 54.555 227.008 1.00 39.12 C ANISOU 441 CG TYR B 114 4352 5223 5288 -1829 -477 706 C ATOM 442 CD1 TYR B 114 71.379 53.464 227.786 1.00 36.40 C ANISOU 442 CD1 TYR B 114 4000 5027 4802 -1871 -617 948 C ATOM 443 CD2 TYR B 114 69.900 54.434 226.190 1.00 42.20 C ANISOU 443 CD2 TYR B 114 4743 5438 5853 -1693 -304 646 C ATOM 444 CE1 TYR B 114 70.646 52.291 227.760 1.00 32.98 C ANISOU 444 CE1 TYR B 114 3580 4546 4407 -1794 -566 1121 C ATOM 445 CE2 TYR B 114 69.162 53.267 226.157 1.00 29.54 C ANISOU 445 CE2 TYR B 114 3130 3814 4280 -1622 -252 796 C ATOM 446 CZ TYR B 114 69.539 52.199 226.942 1.00 31.04 C ANISOU 446 CZ TYR B 114 3331 4129 4335 -1679 -375 1031 C ATOM 447 OH TYR B 114 68.804 51.036 226.909 1.00 49.92 O ANISOU 447 OH TYR B 114 5729 6468 6771 -1629 -320 1189 O ATOM 448 N LEU B 115 73.178 58.493 227.776 1.00 35.67 N ANISOU 448 N LEU B 115 4015 4882 4655 -2288 -612 98 N ATOM 449 CA LEU B 115 74.417 59.202 228.080 1.00 46.20 C ANISOU 449 CA LEU B 115 5311 6320 5923 -2468 -762 30 C ATOM 450 C LEU B 115 74.266 60.190 229.231 1.00 54.40 C ANISOU 450 C LEU B 115 6500 7466 6706 -2689 -731 -236 C ATOM 451 O LEU B 115 75.275 60.581 229.828 1.00 50.77 O ANISOU 451 O LEU B 115 6014 7175 6101 -2884 -887 -281 O ATOM 452 CB LEU B 115 74.923 59.935 226.837 1.00 36.12 C ANISOU 452 CB LEU B 115 3971 4831 4921 -2432 -735 -23 C ATOM 453 CG LEU B 115 75.180 59.073 225.599 1.00 42.71 C ANISOU 453 CG LEU B 115 4652 5576 5999 -2242 -748 192 C ATOM 454 CD1 LEU B 115 75.697 59.923 224.449 1.00 33.15 C ANISOU 454 CD1 LEU B 115 3429 4184 4981 -2161 -668 106 C ATOM 455 CD2 LEU B 115 76.152 57.947 225.919 1.00 42.87 C ANISOU 455 CD2 LEU B 115 4503 5808 5980 -2217 -938 417 C ATOM 456 N SER B 116 73.042 60.604 229.554 1.00 56.15 N ANISOU 456 N SER B 116 6861 7601 6872 -2668 -529 -435 N ATOM 457 CA SER B 116 72.827 61.557 230.635 1.00 46.92 C ANISOU 457 CA SER B 116 5836 6523 5469 -2872 -463 -741 C ATOM 458 C SER B 116 72.667 60.889 231.993 1.00 55.09 C ANISOU 458 C SER B 116 6929 7891 6110 -3018 -505 -696 C ATOM 459 O SER B 116 72.954 61.518 233.018 1.00 51.40 O ANISOU 459 O SER B 116 6556 7605 5368 -3253 -534 -903 O ATOM 460 CB SER B 116 71.591 62.412 230.344 1.00 44.63 C ANISOU 460 CB SER B 116 5649 5973 5335 -2772 -212 -1020 C ATOM 461 OG SER B 116 70.434 61.603 230.231 1.00 41.47 O ANISOU 461 OG SER B 116 5232 5565 4959 -2603 -74 -933 O ATOM 462 N LYS B 117 72.213 59.637 232.019 1.00 66.13 N ANISOU 462 N LYS B 117 8288 9374 7465 -2905 -509 -430 N ATOM 463 CA LYS B 117 71.949 58.910 233.261 1.00 75.36 C ANISOU 463 CA LYS B 117 9535 10847 8251 -3049 -539 -335 C ATOM 464 C LYS B 117 70.983 59.668 234.170 1.00 79.20 C ANISOU 464 C LYS B 117 10176 11419 8498 -3197 -307 -689 C ATOM 465 O LYS B 117 70.033 60.294 233.700 1.00 78.11 O ANISOU 465 O LYS B 117 10058 11058 8561 -3080 -73 -931 O ATOM 466 CB LYS B 117 73.255 58.621 234.007 1.00 77.31 C ANISOU 466 CB LYS B 117 9747 11373 8252 -3231 -841 -162 C ATOM 467 CG LYS B 117 74.210 57.714 233.250 1.00 75.06 C ANISOU 467 CG LYS B 117 9279 11042 8198 -3075 -1071 190 C ATOM 468 CD LYS B 117 75.428 57.372 234.090 1.00 75.86 C ANISOU 468 CD LYS B 117 9323 11444 8058 -3239 -1391 372 C ATOM 469 CE LYS B 117 76.442 56.568 233.294 1.00 72.67 C ANISOU 469 CE LYS B 117 8694 10977 7940 -3061 -1610 674 C ATOM 470 NZ LYS B 117 77.679 56.304 234.079 1.00 75.79 N ANISOU 470 NZ LYS B 117 8991 11664 8142 -3201 -1950 842 N ATOM 471 N ARG B 119 67.606 60.695 234.360 1.00 55.96 N ANISOU 471 N ARG B 119 7348 8243 5673 -3044 442 -1381 N ATOM 472 CA ARG B 119 66.209 60.291 234.458 1.00 63.13 C ANISOU 472 CA ARG B 119 8232 9163 6591 -2962 699 -1456 C ATOM 473 C ARG B 119 65.377 60.991 233.392 1.00 72.65 C ANISOU 473 C ARG B 119 9353 10012 8240 -2698 858 -1654 C ATOM 474 O ARG B 119 65.625 62.152 233.068 1.00 72.59 O ANISOU 474 O ARG B 119 9373 9789 8419 -2658 859 -1895 O ATOM 475 CB ARG B 119 65.650 60.606 235.848 1.00 62.93 C ANISOU 475 CB ARG B 119 8317 9431 6163 -3207 895 -1754 C ATOM 476 CG ARG B 119 66.547 60.184 237.001 1.00 65.11 C ANISOU 476 CG ARG B 119 8709 10080 5951 -3510 714 -1606 C ATOM 477 CD ARG B 119 67.337 61.367 237.546 1.00 65.64 C ANISOU 477 CD ARG B 119 8868 10197 5875 -3694 645 -1919 C ATOM 478 NE ARG B 119 68.057 61.030 238.770 1.00 73.24 N ANISOU 478 NE ARG B 119 9945 11568 6316 -4013 483 -1824 N ATOM 479 CZ ARG B 119 67.517 61.055 239.985 1.00 80.93 C ANISOU 479 CZ ARG B 119 11040 12869 6842 -4266 652 -2025 C ATOM 480 NH1 ARG B 119 66.246 61.401 240.140 1.00 75.25 N ANISOU 480 NH1 ARG B 119 10319 12113 6161 -4226 1010 -2358 N ATOM 481 NH2 ARG B 119 68.247 60.734 241.044 1.00 87.76 N ANISOU 481 NH2 ARG B 119 12015 14115 7213 -4564 460 -1897 N ATOM 482 N TRP B 120 64.386 60.280 232.846 1.00 73.86 N ANISOU 482 N TRP B 120 9404 10097 8562 -2528 976 -1540 N ATOM 483 CA TRP B 120 63.504 60.887 231.855 1.00 71.99 C ANISOU 483 CA TRP B 120 9071 9550 8733 -2272 1104 -1709 C ATOM 484 C TRP B 120 62.709 62.044 232.447 1.00 76.00 C ANISOU 484 C TRP B 120 9603 10018 9255 -2286 1341 -2182 C ATOM 485 O TRP B 120 62.406 63.014 231.743 1.00 77.54 O ANISOU 485 O TRP B 120 9766 9902 9793 -2101 1376 -2375 O ATOM 486 CB TRP B 120 62.557 59.833 231.276 1.00 62.74 C ANISOU 486 CB TRP B 120 7771 8368 7699 -2124 1181 -1513 C ATOM 487 CG TRP B 120 61.766 60.309 230.088 1.00 55.95 C ANISOU 487 CG TRP B 120 6791 7200 7266 -1847 1240 -1604 C ATOM 488 CD1 TRP B 120 60.719 61.185 230.094 1.00 51.78 C ANISOU 488 CD1 TRP B 120 6199 6551 6923 -1727 1436 -1947 C ATOM 489 CD2 TRP B 120 61.960 59.928 228.720 1.00 56.02 C ANISOU 489 CD2 TRP B 120 6726 6995 7565 -1655 1089 -1346 C ATOM 490 NE1 TRP B 120 60.253 61.377 228.817 1.00 48.85 N ANISOU 490 NE1 TRP B 120 5721 5901 6938 -1468 1386 -1888 N ATOM 491 CE2 TRP B 120 60.997 60.616 227.954 1.00 50.33 C ANISOU 491 CE2 TRP B 120 5909 6040 7173 -1435 1180 -1524 C ATOM 492 CE3 TRP B 120 62.855 59.074 228.068 1.00 49.94 C ANISOU 492 CE3 TRP B 120 5952 6215 6810 -1646 887 -996 C ATOM 493 CZ2 TRP B 120 60.903 60.475 226.571 1.00 47.39 C ANISOU 493 CZ2 TRP B 120 5460 5449 7097 -1235 1065 -1346 C ATOM 494 CZ3 TRP B 120 62.760 58.936 226.695 1.00 41.79 C ANISOU 494 CZ3 TRP B 120 4837 4964 6078 -1449 806 -856 C ATOM 495 CH2 TRP B 120 61.792 59.633 225.962 1.00 43.28 C ANISOU 495 CH2 TRP B 120 4953 4945 6546 -1259 889 -1021 C ATOM 496 N GLU B 121 62.374 61.964 233.737 1.00 76.07 N ANISOU 496 N GLU B 121 9673 10332 8897 -2505 1504 -2375 N ATOM 497 CA GLU B 121 61.538 62.986 234.359 1.00 80.23 C ANISOU 497 CA GLU B 121 10203 10846 9435 -2519 1772 -2870 C ATOM 498 C GLU B 121 62.268 64.322 234.447 1.00 81.12 C ANISOU 498 C GLU B 121 10430 10767 9627 -2561 1707 -3150 C ATOM 499 O GLU B 121 61.719 65.365 234.073 1.00 73.21 O ANISOU 499 O GLU B 121 9394 9467 8955 -2387 1824 -3465 O ATOM 500 CB GLU B 121 61.087 62.521 235.745 1.00 88.26 C ANISOU 500 CB GLU B 121 11270 12284 9980 -2791 1973 -3005 C ATOM 501 CG GLU B 121 60.200 61.279 235.738 1.00 93.82 C ANISOU 501 CG GLU B 121 11866 13166 10616 -2780 2089 -2776 C ATOM 502 CD GLU B 121 60.974 59.997 235.481 1.00 94.13 C ANISOU 502 CD GLU B 121 11945 13297 10523 -2840 1829 -2237 C ATOM 503 OE1 GLU B 121 62.075 59.842 236.050 1.00 98.79 O ANISOU 503 OE1 GLU B 121 12673 14050 10811 -3038 1630 -2077 O ATOM 504 OE2 GLU B 121 60.485 59.150 234.704 1.00 92.05 O ANISOU 504 OE2 GLU B 121 11565 12935 10473 -2686 1815 -1984 O ATOM 505 N HIS B 122 63.509 64.312 234.939 1.00 85.43 N ANISOU 505 N HIS B 122 11104 11466 9888 -2793 1509 -3038 N ATOM 506 CA HIS B 122 64.269 65.551 235.053 1.00 85.74 C ANISOU 506 CA HIS B 122 11255 11335 9988 -2879 1438 -3303 C ATOM 507 C HIS B 122 64.705 66.091 233.698 1.00 75.57 C ANISOU 507 C HIS B 122 9933 9621 9157 -2660 1276 -3165 C ATOM 508 O HIS B 122 65.014 67.282 233.589 1.00 75.10 O ANISOU 508 O HIS B 122 9955 9304 9274 -2672 1272 -3427 O ATOM 509 CB HIS B 122 65.487 65.343 235.956 1.00 88.97 C ANISOU 509 CB HIS B 122 11784 12064 9955 -3206 1250 -3209 C ATOM 510 CG HIS B 122 65.148 65.247 237.411 1.00 96.76 C ANISOU 510 CG HIS B 122 12860 13449 10454 -3482 1417 -3459 C ATOM 511 ND1 HIS B 122 65.916 64.539 238.311 1.00 99.43 N ANISOU 511 ND1 HIS B 122 13281 14193 10305 -3768 1253 -3249 N ATOM 512 CD2 HIS B 122 64.124 65.773 238.124 1.00100.81 C ANISOU 512 CD2 HIS B 122 13390 14032 10882 -3524 1735 -3905 C ATOM 513 CE1 HIS B 122 65.379 64.632 239.514 1.00100.86 C ANISOU 513 CE1 HIS B 122 13548 14691 10085 -3997 1463 -3541 C ATOM 514 NE2 HIS B 122 64.290 65.375 239.428 1.00102.31 N ANISOU 514 NE2 HIS B 122 13686 14683 10503 -3857 1775 -3961 N ATOM 515 N ILE B 123 64.741 65.246 232.668 1.00 71.96 N ANISOU 515 N ILE B 123 9373 9085 8885 -2482 1149 -2766 N ATOM 516 CA ILE B 123 65.021 65.724 231.319 1.00 71.54 C ANISOU 516 CA ILE B 123 9289 8648 9243 -2279 1023 -2632 C ATOM 517 C ILE B 123 63.761 66.297 230.679 1.00 73.99 C ANISOU 517 C ILE B 123 9527 8655 9932 -2002 1188 -2821 C ATOM 518 O ILE B 123 63.819 67.293 229.949 1.00 65.56 O ANISOU 518 O ILE B 123 8497 7221 9191 -1877 1145 -2910 O ATOM 519 CB ILE B 123 65.623 64.589 230.470 1.00 65.18 C ANISOU 519 CB ILE B 123 8400 7900 8463 -2215 824 -2157 C ATOM 520 CG1 ILE B 123 66.981 64.164 231.028 1.00 62.20 C ANISOU 520 CG1 ILE B 123 8071 7780 7784 -2458 624 -1977 C ATOM 521 CG2 ILE B 123 65.758 65.012 229.014 1.00 58.47 C ANISOU 521 CG2 ILE B 123 7516 6690 8010 -2012 726 -2018 C ATOM 522 CD1 ILE B 123 67.591 62.996 230.294 1.00 56.82 C ANISOU 522 CD1 ILE B 123 7290 7163 7137 -2387 442 -1543 C ATOM 523 N ASP B 124 62.604 65.693 230.956 1.00 82.09 N ANISOU 523 N ASP B 124 10442 9826 10924 -1910 1371 -2879 N ATOM 524 CA ASP B 124 61.335 66.056 230.327 1.00 84.74 C ANISOU 524 CA ASP B 124 10651 9920 11626 -1626 1510 -3026 C ATOM 525 C ASP B 124 60.336 66.484 231.396 1.00 82.89 C ANISOU 525 C ASP B 124 10380 9808 11308 -1657 1800 -3474 C ATOM 526 O ASP B 124 59.530 65.666 231.867 1.00 87.93 O ANISOU 526 O ASP B 124 10906 10718 11785 -1682 1964 -3482 O ATOM 527 CB ASP B 124 60.786 64.889 229.510 1.00 79.08 C ANISOU 527 CB ASP B 124 9783 9264 11002 -1471 1468 -2690 C ATOM 528 CG ASP B 124 59.535 65.253 228.734 1.00 76.52 C ANISOU 528 CG ASP B 124 9304 8697 11073 -1172 1559 -2804 C ATOM 529 OD1 ASP B 124 59.224 66.458 228.624 1.00 79.23 O ANISOU 529 OD1 ASP B 124 9668 8754 11682 -1043 1606 -3084 O ATOM 530 OD2 ASP B 124 58.857 64.330 228.238 1.00 76.77 O ANISOU 530 OD2 ASP B 124 9189 8816 11163 -1065 1572 -2615 O ATOM 531 N PRO B 125 60.351 67.750 231.809 1.00 77.97 N ANISOU 531 N PRO B 125 7832 7842 13950 -981 1196 -3921 N ATOM 532 CA PRO B 125 59.321 68.225 232.740 1.00 76.79 C ANISOU 532 CA PRO B 125 7636 7740 13800 -894 1363 -4280 C ATOM 533 C PRO B 125 57.982 68.384 232.037 1.00 79.39 C ANISOU 533 C PRO B 125 7880 7875 14411 -700 1452 -4124 C ATOM 534 O PRO B 125 57.906 68.871 230.906 1.00 77.51 O ANISOU 534 O PRO B 125 7612 7358 14481 -626 1359 -3824 O ATOM 535 CB PRO B 125 59.869 69.575 233.216 1.00 74.43 C ANISOU 535 CB PRO B 125 7323 7310 13648 -941 1316 -4516 C ATOM 536 CG PRO B 125 60.739 70.035 232.095 1.00 70.11 C ANISOU 536 CG PRO B 125 6792 6508 13338 -968 1152 -4184 C ATOM 537 CD PRO B 125 61.345 68.792 231.500 1.00 65.03 C ANISOU 537 CD PRO B 125 6202 6019 12489 -1040 1070 -3871 C ATOM 538 N SER B 126 56.919 67.964 232.721 1.00 85.71 N ANISOU 538 N SER B 126 8634 8864 15068 -623 1627 -4311 N ATOM 539 CA SER B 126 55.544 67.997 232.234 1.00 94.23 C ANISOU 539 CA SER B 126 9608 9835 16359 -450 1713 -4183 C ATOM 540 C SER B 126 55.225 66.911 231.215 1.00 91.28 C ANISOU 540 C SER B 126 9238 9462 15983 -379 1682 -3792 C ATOM 541 O SER B 126 54.066 66.795 230.798 1.00 99.92 O ANISOU 541 O SER B 126 10243 10513 17209 -250 1732 -3652 O ATOM 542 N GLY B 127 56.204 66.111 230.801 1.00 78.61 N ANISOU 542 N GLY B 127 7730 7991 14147 -482 1552 -3506 N ATOM 543 CA GLY B 127 55.953 65.036 229.858 1.00 62.53 C ANISOU 543 CA GLY B 127 5702 6038 12019 -434 1490 -3069 C ATOM 544 C GLY B 127 55.714 65.481 228.433 1.00 51.29 C ANISOU 544 C GLY B 127 4243 4253 10991 -341 1387 -2787 C ATOM 545 O GLY B 127 55.009 64.793 227.687 1.00 49.43 O ANISOU 545 O GLY B 127 3975 4042 10765 -252 1376 -2510 O ATOM 546 N ARG B 128 56.286 66.617 228.030 1.00 52.73 N ANISOU 546 N ARG B 128 4435 4128 11473 -373 1299 -2824 N ATOM 547 CA ARG B 128 56.091 67.104 226.667 1.00 56.22 C ANISOU 547 CA ARG B 128 4854 4348 12160 -300 1170 -2454 C ATOM 548 C ARG B 128 56.747 66.180 225.646 1.00 53.00 C ANISOU 548 C ARG B 128 4521 4001 11617 -354 1062 -2077 C ATOM 549 O ARG B 128 56.146 65.858 224.615 1.00 49.05 O ANISOU 549 O ARG B 128 3998 3455 11184 -266 1007 -1773 O ATOM 550 CB ARG B 128 56.631 68.529 226.542 1.00 68.38 C ANISOU 550 CB ARG B 128 6393 5672 13915 -328 1089 -2503 C ATOM 551 CG ARG B 128 56.812 69.023 225.112 1.00 71.70 C ANISOU 551 CG ARG B 128 6832 5904 14508 -297 940 -2106 C ATOM 552 CD ARG B 128 58.284 69.203 224.762 1.00 62.34 C ANISOU 552 CD ARG B 128 5744 4718 13224 -431 845 -1981 C ATOM 553 NE ARG B 128 58.465 69.762 223.425 1.00 67.12 N ANISOU 553 NE ARG B 128 6378 5161 13964 -411 721 -1624 N ATOM 554 CZ ARG B 128 58.687 69.038 222.333 1.00 69.40 C ANISOU 554 CZ ARG B 128 6721 5537 14110 -417 651 -1273 C ATOM 555 NH1 ARG B 128 58.762 67.716 222.413 1.00 66.63 N ANISOU 555 NH1 ARG B 128 6395 5415 13507 -434 687 -1223 N ATOM 556 NH2 ARG B 128 58.839 69.635 221.158 1.00 68.78 N ANISOU 556 NH2 ARG B 128 6676 5325 14131 -414 546 -979 N ATOM 557 N LEU B 129 57.980 65.743 225.917 1.00 50.98 N ANISOU 557 N LEU B 129 4342 3885 11144 -509 1019 -2089 N ATOM 558 CA LEU B 129 58.698 64.899 224.968 1.00 45.00 C ANISOU 558 CA LEU B 129 3640 3241 10216 -567 915 -1729 C ATOM 559 C LEU B 129 58.167 63.470 224.955 1.00 60.78 C ANISOU 559 C LEU B 129 5638 5524 11932 -518 946 -1576 C ATOM 560 O LEU B 129 58.214 62.803 223.915 1.00 50.81 O ANISOU 560 O LEU B 129 4393 4289 10624 -501 876 -1263 O ATOM 561 CB LEU B 129 60.192 64.911 225.297 1.00 49.19 C ANISOU 561 CB LEU B 129 4228 3902 10561 -722 848 -1769 C ATOM 562 CG LEU B 129 61.147 64.135 224.390 1.00 48.56 C ANISOU 562 CG LEU B 129 4206 3974 10272 -768 748 -1437 C ATOM 563 CD1 LEU B 129 61.089 64.664 222.966 1.00 48.62 C ANISOU 563 CD1 LEU B 129 4248 3812 10412 -693 680 -1129 C ATOM 564 CD2 LEU B 129 62.565 64.207 224.935 1.00 43.04 C ANISOU 564 CD2 LEU B 129 3533 3404 9416 -912 691 -1542 C ATOM 565 N CYS B 130 57.658 62.985 226.091 1.00 62.77 N ANISOU 565 N CYS B 130 5873 6007 11970 -497 1051 -1785 N ATOM 566 CA CYS B 130 57.186 61.605 226.168 1.00 59.89 C ANISOU 566 CA CYS B 130 5512 5923 11320 -462 1078 -1627 C ATOM 567 C CYS B 130 55.947 61.386 225.309 1.00 55.65 C ANISOU 567 C CYS B 130 4911 5274 10960 -326 1095 -1444 C ATOM 568 O CYS B 130 55.820 60.347 224.650 1.00 56.49 O ANISOU 568 O CYS B 130 5031 5497 10936 -310 1044 -1184 O ATOM 569 CB CYS B 130 56.905 61.233 227.623 1.00 64.37 C ANISOU 569 CB CYS B 130 6078 6762 11616 -492 1196 -1884 C ATOM 570 SG CYS B 130 56.304 59.548 227.902 1.00 68.92 S ANISOU 570 SG CYS B 130 6661 7678 11848 -476 1239 -1692 S ATOM 571 N THR B 131 55.022 62.349 225.303 1.00 62.59 N ANISOU 571 N THR B 131 5708 5920 12152 -225 1155 -1589 N ATOM 572 CA THR B 131 53.829 62.219 224.471 1.00 57.66 C ANISOU 572 CA THR B 131 5002 5178 11730 -90 1147 -1417 C ATOM 573 C THR B 131 54.191 62.219 222.990 1.00 60.24 C ANISOU 573 C THR B 131 5372 5345 12173 -90 988 -1074 C ATOM 574 O THR B 131 53.605 61.470 222.198 1.00 39.14 O ANISOU 574 O THR B 131 2678 2727 9466 -34 937 -839 O ATOM 575 CB THR B 131 52.844 63.345 224.787 1.00 61.13 C ANISOU 575 CB THR B 131 5333 5384 12509 21 1225 -1652 C ATOM 576 OG1 THR B 131 52.544 63.337 226.188 1.00 66.06 O ANISOU 576 OG1 THR B 131 5916 6188 12997 13 1400 -2004 O ATOM 577 CG2 THR B 131 51.553 63.162 224.002 1.00 61.33 C ANISOU 577 CG2 THR B 131 5315 5380 12608 99 1160 -1431 C ATOM 578 N PHE B 132 55.156 63.054 222.597 1.00 58.71 N ANISOU 578 N PHE B 132 5236 4963 12106 -167 909 -1046 N ATOM 579 CA PHE B 132 55.623 63.056 221.215 1.00 50.62 C ANISOU 579 CA PHE B 132 4268 3900 11066 -178 768 -703 C ATOM 580 C PHE B 132 56.346 61.762 220.862 1.00 46.19 C ANISOU 580 C PHE B 132 3783 3586 10181 -252 730 -524 C ATOM 581 O PHE B 132 56.253 61.292 219.723 1.00 45.00 O ANISOU 581 O PHE B 132 3673 3484 9941 -208 641 -254 O ATOM 582 CB PHE B 132 56.541 64.256 220.976 1.00 50.02 C ANISOU 582 CB PHE B 132 4242 3698 11065 -231 702 -701 C ATOM 583 CG PHE B 132 57.305 64.191 219.683 1.00 49.38 C ANISOU 583 CG PHE B 132 4249 3659 10856 -267 583 -382 C ATOM 584 CD1 PHE B 132 56.708 64.557 218.489 1.00 53.93 C ANISOU 584 CD1 PHE B 132 4813 4146 11530 -201 487 -131 C ATOM 585 CD2 PHE B 132 58.624 63.764 219.664 1.00 44.78 C ANISOU 585 CD2 PHE B 132 3756 3223 10037 -380 567 -345 C ATOM 586 CE1 PHE B 132 57.409 64.497 217.301 1.00 50.48 C ANISOU 586 CE1 PHE B 132 4465 3762 10953 -253 395 137 C ATOM 587 CE2 PHE B 132 59.330 63.700 218.479 1.00 42.44 C ANISOU 587 CE2 PHE B 132 3535 2978 9612 -421 483 -84 C ATOM 588 CZ PHE B 132 58.722 64.067 217.296 1.00 46.13 C ANISOU 588 CZ PHE B 132 4002 3353 10172 -363 406 151 C ATOM 589 N PHE B 133 57.063 61.175 221.822 1.00 36.70 N ANISOU 589 N PHE B 133 2599 2583 8762 -355 785 -674 N ATOM 590 CA PHE B 133 57.799 59.945 221.552 1.00 34.43 C ANISOU 590 CA PHE B 133 2395 2559 8126 -389 730 -510 C ATOM 591 C PHE B 133 56.847 58.781 221.312 1.00 38.67 C ANISOU 591 C PHE B 133 2928 3238 8526 -304 735 -383 C ATOM 592 O PHE B 133 57.014 58.017 220.355 1.00 43.20 O ANISOU 592 O PHE B 133 3585 3890 8940 -276 649 -165 O ATOM 593 CB PHE B 133 58.747 59.646 222.714 1.00 46.53 C ANISOU 593 CB PHE B 133 3933 4277 9470 -504 762 -696 C ATOM 594 CG PHE B 133 59.740 58.552 222.430 1.00 44.33 C ANISOU 594 CG PHE B 133 3739 4218 8885 -539 682 -537 C ATOM 595 CD1 PHE B 133 59.406 57.222 222.627 1.00 43.92 C ANISOU 595 CD1 PHE B 133 3704 4373 8612 -504 681 -452 C ATOM 596 CD2 PHE B 133 61.016 58.857 221.983 1.00 46.97 C ANISOU 596 CD2 PHE B 133 4129 4548 9168 -604 610 -479 C ATOM 597 CE1 PHE B 133 60.320 56.215 222.373 1.00 37.72 C ANISOU 597 CE1 PHE B 133 2984 3756 7593 -528 601 -325 C ATOM 598 CE2 PHE B 133 61.936 57.854 221.728 1.00 42.40 C ANISOU 598 CE2 PHE B 133 3600 4163 8348 -629 546 -362 C ATOM 599 CZ PHE B 133 61.586 56.532 221.926 1.00 32.73 C ANISOU 599 CZ PHE B 133 2386 3115 6934 -585 537 -291 C ATOM 600 N GLY B 134 55.842 58.630 222.178 1.00 33.69 N ANISOU 600 N GLY B 134 2208 2657 7935 -263 838 -536 N ATOM 601 CA GLY B 134 54.888 57.545 222.011 1.00 32.59 C ANISOU 601 CA GLY B 134 2096 2650 7637 -189 834 -417 C ATOM 602 C GLY B 134 54.077 57.665 220.735 1.00 32.38 C ANISOU 602 C GLY B 134 2075 2465 7762 -100 749 -223 C ATOM 603 O GLY B 134 53.750 56.661 220.098 1.00 30.97 O ANISOU 603 O GLY B 134 1967 2386 7413 -75 681 -54 O ATOM 604 N LEU B 135 53.731 58.895 220.350 1.00 34.03 N ANISOU 604 N LEU B 135 2196 2418 8316 -58 743 -250 N ATOM 605 CA LEU B 135 52.971 59.103 219.121 1.00 34.24 C ANISOU 605 CA LEU B 135 2209 2290 8512 6 640 -43 C ATOM 606 C LEU B 135 53.788 58.709 217.896 1.00 32.83 C ANISOU 606 C LEU B 135 2118 2155 8199 -14 520 204 C ATOM 607 O LEU B 135 53.284 58.025 216.997 1.00 31.98 O ANISOU 607 O LEU B 135 2050 2097 8004 14 438 382 O ATOM 608 CB LEU B 135 52.516 60.562 219.030 1.00 41.03 C ANISOU 608 CB LEU B 135 2956 2900 9733 31 633 -108 C ATOM 609 CG LEU B 135 51.769 61.020 217.773 1.00 44.35 C ANISOU 609 CG LEU B 135 3344 3248 10259 64 492 117 C ATOM 610 CD1 LEU B 135 50.663 61.993 218.148 1.00 40.21 C ANISOU 610 CD1 LEU B 135 2738 2584 9956 132 506 -18 C ATOM 611 CD2 LEU B 135 52.717 61.664 216.767 1.00 37.88 C ANISOU 611 CD2 LEU B 135 2571 2385 9435 45 382 304 C ATOM 612 N THR B 136 55.054 59.130 217.846 1.00 45.43 N ANISOU 612 N THR B 136 3771 3774 9718 -85 508 200 N ATOM 613 CA THR B 136 55.904 58.797 216.707 1.00 40.18 C ANISOU 613 CA THR B 136 3205 3209 8852 -123 414 402 C ATOM 614 C THR B 136 56.114 57.291 216.594 1.00 36.74 C ANISOU 614 C THR B 136 2854 3001 8103 -133 401 449 C ATOM 615 O THR B 136 56.164 56.744 215.486 1.00 39.25 O ANISOU 615 O THR B 136 3215 3390 8307 -128 325 616 O ATOM 616 CB THR B 136 57.244 59.523 216.827 1.00 43.04 C ANISOU 616 CB THR B 136 3626 3558 9170 -218 420 357 C ATOM 617 OG1 THR B 136 57.015 60.935 216.919 1.00 38.51 O ANISOU 617 OG1 THR B 136 2997 2762 8875 -209 419 308 O ATOM 618 CG2 THR B 136 58.126 59.235 215.622 1.00 44.13 C ANISOU 618 CG2 THR B 136 3852 3801 9114 -273 350 549 C ATOM 619 N MET B 137 56.233 56.604 217.733 1.00 39.54 N ANISOU 619 N MET B 137 3228 3484 8309 -156 468 300 N ATOM 620 CA MET B 137 56.342 55.149 217.713 1.00 27.30 C ANISOU 620 CA MET B 137 1753 2136 6482 -158 443 345 C ATOM 621 C MET B 137 55.110 54.515 217.081 1.00 41.52 C ANISOU 621 C MET B 137 3550 3929 8295 -92 402 446 C ATOM 622 O MET B 137 55.222 53.562 216.302 1.00 47.69 O ANISOU 622 O MET B 137 4391 4807 8922 -90 338 550 O ATOM 623 CB MET B 137 56.544 54.620 219.133 1.00 27.12 C ANISOU 623 CB MET B 137 1727 2249 6328 -197 513 193 C ATOM 624 CG MET B 137 57.868 55.011 219.767 1.00 45.48 C ANISOU 624 CG MET B 137 4057 4622 8603 -281 530 93 C ATOM 625 SD MET B 137 59.274 54.113 219.082 1.00 26.06 S ANISOU 625 SD MET B 137 1682 2306 5914 -321 447 200 S ATOM 626 CE MET B 137 59.063 52.519 219.865 1.00 25.06 C ANISOU 626 CE MET B 137 1573 2367 5582 -312 439 201 C ATOM 627 N THR B 138 53.925 55.038 217.400 1.00 41.14 N ANISOU 627 N THR B 138 3424 3765 8443 -45 437 400 N ATOM 628 CA THR B 138 52.688 54.445 216.904 1.00 38.32 C ANISOU 628 CA THR B 138 3056 3409 8094 -1 394 480 C ATOM 629 C THR B 138 52.465 54.769 215.431 1.00 35.82 C ANISOU 629 C THR B 138 2727 2989 7896 17 280 668 C ATOM 630 O THR B 138 51.991 53.918 214.668 1.00 32.72 O ANISOU 630 O THR B 138 2363 2669 7401 19 209 767 O ATOM 631 CB THR B 138 51.504 54.925 217.746 1.00 45.52 C ANISOU 631 CB THR B 138 3877 4254 9165 34 473 353 C ATOM 632 OG1 THR B 138 51.762 54.657 219.131 1.00 36.49 O ANISOU 632 OG1 THR B 138 2728 3238 7899 5 587 184 O ATOM 633 CG2 THR B 138 50.225 54.210 217.331 1.00 54.15 C ANISOU 633 CG2 THR B 138 4957 5385 10235 64 430 421 C ATOM 634 N VAL B 139 52.801 55.993 215.013 1.00 39.68 N ANISOU 634 N VAL B 139 3156 3311 8611 22 256 725 N ATOM 635 CA VAL B 139 52.573 56.404 213.628 1.00 40.18 C ANISOU 635 CA VAL B 139 3179 3321 8767 25 133 931 C ATOM 636 C VAL B 139 53.381 55.531 212.675 1.00 44.67 C ANISOU 636 C VAL B 139 3818 4050 9105 -2 72 1055 C ATOM 637 O VAL B 139 52.832 54.886 211.773 1.00 44.50 O ANISOU 637 O VAL B 139 3802 4079 9028 -8 -14 1176 O ATOM 638 CB VAL B 139 52.916 57.893 213.442 1.00 32.42 C ANISOU 638 CB VAL B 139 2073 2233 8013 21 114 959 C ATOM 639 CG1 VAL B 139 52.908 58.256 211.967 1.00 33.09 C ANISOU 639 CG1 VAL B 139 2169 2320 8084 -15 -26 1196 C ATOM 640 CG2 VAL B 139 51.939 58.764 214.204 1.00 44.98 C ANISOU 640 CG2 VAL B 139 3559 3668 9864 20 162 829 C ATOM 641 N PHE B 140 54.700 55.500 212.863 1.00 28.41 N ANISOU 641 N PHE B 140 1831 2093 6873 -64 122 998 N ATOM 642 CA PHE B 140 55.568 54.790 211.932 1.00 35.67 C ANISOU 642 CA PHE B 140 2824 3170 7559 -130 89 1080 C ATOM 643 C PHE B 140 55.492 53.279 212.098 1.00 36.98 C ANISOU 643 C PHE B 140 3045 3486 7518 -120 97 1010 C ATOM 644 O PHE B 140 55.825 52.549 211.159 1.00 41.75 O ANISOU 644 O PHE B 140 3674 4204 7984 -158 56 1076 O ATOM 645 CB PHE B 140 57.005 55.285 212.094 1.00 36.50 C ANISOU 645 CB PHE B 140 2985 3312 7573 -209 144 1033 C ATOM 646 CG PHE B 140 57.192 56.719 211.686 1.00 29.50 C ANISOU 646 CG PHE B 140 2078 2281 6848 -247 123 1126 C ATOM 647 CD1 PHE B 140 56.943 57.744 212.583 1.00 30.51 C ANISOU 647 CD1 PHE B 140 2158 2247 7188 -216 157 1028 C ATOM 648 CD2 PHE B 140 57.598 57.042 210.403 1.00 30.47 C ANISOU 648 CD2 PHE B 140 2240 2429 6907 -325 70 1308 C ATOM 649 CE1 PHE B 140 57.102 59.065 212.211 1.00 32.43 C ANISOU 649 CE1 PHE B 140 2397 2341 7584 -251 126 1106 C ATOM 650 CE2 PHE B 140 57.762 58.362 210.025 1.00 40.73 C ANISOU 650 CE2 PHE B 140 3552 3591 8334 -368 40 1411 C ATOM 651 CZ PHE B 140 57.514 59.374 210.931 1.00 46.24 C ANISOU 651 CZ PHE B 140 4205 4112 9252 -325 62 1308 C ATOM 652 N GLY B 141 55.067 52.794 213.265 1.00 35.00 N ANISOU 652 N GLY B 141 2812 3244 7243 -85 151 875 N ATOM 653 CA GLY B 141 54.844 51.365 213.417 1.00 34.80 C ANISOU 653 CA GLY B 141 2836 3339 7045 -80 143 832 C ATOM 654 C GLY B 141 53.689 50.873 212.564 1.00 36.30 C ANISOU 654 C GLY B 141 2998 3517 7276 -59 67 919 C ATOM 655 O GLY B 141 53.804 49.866 211.859 1.00 38.60 O ANISOU 655 O GLY B 141 3314 3905 7448 -78 21 943 O ATOM 656 N LEU B 142 52.558 51.580 212.617 1.00 31.65 N ANISOU 656 N LEU B 142 2346 2807 6874 -27 50 954 N ATOM 657 CA LEU B 142 51.403 51.196 211.813 1.00 26.24 C ANISOU 657 CA LEU B 142 1621 2113 6237 -20 -38 1034 C ATOM 658 C LEU B 142 51.631 51.467 210.332 1.00 34.54 C ANISOU 658 C LEU B 142 2637 3177 7311 -49 -151 1204 C ATOM 659 O LEU B 142 51.117 50.729 209.484 1.00 37.19 O ANISOU 659 O LEU B 142 2957 3589 7584 -64 -240 1254 O ATOM 660 CB LEU B 142 50.156 51.937 212.294 1.00 27.49 C ANISOU 660 CB LEU B 142 1705 2148 6594 12 -26 1011 C ATOM 661 CG LEU B 142 49.671 51.633 213.712 1.00 35.43 C ANISOU 661 CG LEU B 142 2710 3176 7576 34 86 852 C ATOM 662 CD1 LEU B 142 48.573 52.604 214.119 1.00 28.95 C ANISOU 662 CD1 LEU B 142 1789 2234 6977 68 112 809 C ATOM 663 CD2 LEU B 142 49.184 50.196 213.815 1.00 34.74 C ANISOU 663 CD2 LEU B 142 2655 3210 7336 25 77 826 C ATOM 664 N SER B 143 52.384 52.521 210.004 1.00 31.45 N ANISOU 664 N SER B 143 2216 2723 7010 -67 -157 1299 N ATOM 665 CA SER B 143 52.617 52.867 208.604 1.00 30.52 C ANISOU 665 CA SER B 143 2047 2640 6909 -121 -269 1504 C ATOM 666 C SER B 143 53.317 51.733 207.865 1.00 33.64 C ANISOU 666 C SER B 143 2486 3238 7056 -188 -275 1487 C ATOM 667 O SER B 143 52.873 51.309 206.792 1.00 40.78 O ANISOU 667 O SER B 143 3341 4233 7921 -223 -391 1593 O ATOM 668 CB SER B 143 53.435 54.156 208.513 1.00 32.89 C ANISOU 668 CB SER B 143 2347 2854 7295 -161 -246 1589 C ATOM 669 OG SER B 143 52.694 55.265 208.992 1.00 40.06 O ANISOU 669 OG SER B 143 3165 3587 8467 -96 -266 1595 O ATOM 670 N SER B 144 54.417 51.227 208.427 1.00 29.35 N ANISOU 670 N SER B 144 2021 2776 6354 -206 -164 1345 N ATOM 671 CA SER B 144 55.115 50.106 207.807 1.00 31.03 C ANISOU 671 CA SER B 144 2257 3160 6374 -260 -154 1294 C ATOM 672 C SER B 144 54.222 48.873 207.727 1.00 26.83 C ANISOU 672 C SER B 144 1715 2674 5806 -220 -213 1222 C ATOM 673 O SER B 144 54.290 48.111 206.755 1.00 30.72 O ANISOU 673 O SER B 144 2170 3289 6212 -266 -272 1233 O ATOM 674 CB SER B 144 56.394 49.791 208.583 1.00 36.09 C ANISOU 674 CB SER B 144 2965 3850 6896 -266 -40 1146 C ATOM 675 OG SER B 144 57.051 48.655 208.045 1.00 37.77 O ANISOU 675 OG SER B 144 3176 4206 6969 -302 -27 1075 O ATOM 676 N LEU B 145 53.372 48.666 208.735 1.00 25.17 N ANISOU 676 N LEU B 145 1533 2374 5658 -151 -194 1142 N ATOM 677 CA LEU B 145 52.531 47.473 208.761 1.00 29.26 C ANISOU 677 CA LEU B 145 2054 2922 6140 -133 -234 1071 C ATOM 678 C LEU B 145 51.487 47.496 207.651 1.00 33.82 C ANISOU 678 C LEU B 145 2557 3516 6778 -143 -373 1172 C ATOM 679 O LEU B 145 51.162 46.449 207.078 1.00 31.83 O ANISOU 679 O LEU B 145 2286 3343 6467 -160 -440 1126 O ATOM 680 CB LEU B 145 51.855 47.333 210.125 1.00 31.78 C ANISOU 680 CB LEU B 145 2409 3161 6504 -89 -166 987 C ATOM 681 CG LEU B 145 52.711 46.795 211.271 1.00 29.24 C ANISOU 681 CG LEU B 145 2156 2868 6086 -86 -71 882 C ATOM 682 CD1 LEU B 145 51.930 46.816 212.578 1.00 26.63 C ANISOU 682 CD1 LEU B 145 1829 2488 5801 -61 -10 831 C ATOM 683 CD2 LEU B 145 53.197 45.388 210.955 1.00 23.21 C ANISOU 683 CD2 LEU B 145 1414 2183 5222 -106 -93 827 C ATOM 684 N PHE B 146 50.949 48.675 207.332 1.00 33.86 N ANISOU 684 N PHE B 146 2510 3441 6915 -131 -435 1307 N ATOM 685 CA PHE B 146 49.864 48.770 206.365 1.00 39.50 C ANISOU 685 CA PHE B 146 3157 4168 7685 -128 -597 1414 C ATOM 686 C PHE B 146 50.316 49.174 204.968 1.00 30.20 C ANISOU 686 C PHE B 146 1924 3100 6450 -180 -739 1598 C ATOM 687 O PHE B 146 49.587 48.913 204.005 1.00 31.53 O ANISOU 687 O PHE B 146 2056 3344 6579 -187 -909 1671 O ATOM 688 CB PHE B 146 48.790 49.743 206.867 1.00 36.86 C ANISOU 688 CB PHE B 146 2790 3677 7537 -78 -605 1451 C ATOM 689 CG PHE B 146 47.868 49.135 207.887 1.00 36.16 C ANISOU 689 CG PHE B 146 2710 3546 7485 -46 -526 1300 C ATOM 690 CD1 PHE B 146 46.749 48.420 207.488 1.00 30.03 C ANISOU 690 CD1 PHE B 146 1889 2806 6714 -42 -617 1278 C ATOM 691 CD2 PHE B 146 48.131 49.256 209.241 1.00 34.29 C ANISOU 691 CD2 PHE B 146 2514 3249 7265 -27 -371 1188 C ATOM 692 CE1 PHE B 146 45.904 47.849 208.421 1.00 29.80 C ANISOU 692 CE1 PHE B 146 1848 2747 6727 -24 -540 1164 C ATOM 693 CE2 PHE B 146 47.289 48.687 210.179 1.00 28.09 C ANISOU 693 CE2 PHE B 146 1722 2454 6498 -8 -303 1079 C ATOM 694 CZ PHE B 146 46.175 47.983 209.768 1.00 28.86 C ANISOU 694 CZ PHE B 146 1767 2581 6617 -9 -381 1075 C ATOM 695 N ILE B 147 51.483 49.806 204.827 1.00 35.73 N ANISOU 695 N ILE B 147 2678 3821 7078 -233 -665 1661 N ATOM 696 CA ILE B 147 52.070 49.955 203.498 1.00 36.23 C ANISOU 696 CA ILE B 147 2847 4028 6893 -320 -724 1770 C ATOM 697 C ILE B 147 52.414 48.585 202.926 1.00 39.70 C ANISOU 697 C ILE B 147 3313 4659 7114 -364 -720 1618 C ATOM 698 O ILE B 147 52.224 48.325 201.731 1.00 32.71 O ANISOU 698 O ILE B 147 2476 3921 6030 -414 -833 1664 O ATOM 699 CB ILE B 147 53.300 50.882 203.547 1.00 31.61 C ANISOU 699 CB ILE B 147 2338 3419 6255 -387 -604 1843 C ATOM 700 CG1 ILE B 147 52.871 52.326 203.813 1.00 36.83 C ANISOU 700 CG1 ILE B 147 2984 3872 7137 -353 -650 2016 C ATOM 701 CG2 ILE B 147 54.085 50.803 202.248 1.00 32.98 C ANISOU 701 CG2 ILE B 147 2614 3792 6126 -500 -611 1919 C ATOM 702 CD1 ILE B 147 54.023 53.307 203.863 1.00 33.12 C ANISOU 702 CD1 ILE B 147 2583 3347 6652 -434 -544 2098 C ATOM 703 N ALA B 148 52.907 47.681 203.777 1.00 36.49 N ANISOU 703 N ALA B 148 2872 4248 6743 -345 -599 1429 N ATOM 704 CA ALA B 148 53.173 46.315 203.339 1.00 32.67 C ANISOU 704 CA ALA B 148 2396 3898 6118 -368 -600 1261 C ATOM 705 C ALA B 148 51.880 45.580 203.008 1.00 45.25 C ANISOU 705 C ALA B 148 3932 5495 7767 -342 -755 1228 C ATOM 706 O ALA B 148 51.830 44.805 202.045 1.00 60.33 O ANISOU 706 O ALA B 148 5871 7542 9511 -383 -833 1146 O ATOM 707 CB ALA B 148 53.959 45.562 204.412 1.00 27.58 C ANISOU 707 CB ALA B 148 1721 3210 5547 -343 -459 1099 C ATOM 708 N SER B 149 50.825 45.805 203.797 1.00 54.89 N ANISOU 708 N SER B 149 5058 6574 9223 -279 -797 1272 N ATOM 709 CA SER B 149 49.540 45.175 203.510 1.00 30.38 C ANISOU 709 CA SER B 149 1906 3464 6174 -260 -933 1237 C ATOM 710 C SER B 149 48.969 45.670 202.189 1.00 32.53 C ANISOU 710 C SER B 149 2173 3838 6349 -290 -1137 1381 C ATOM 711 O SER B 149 48.347 44.902 201.446 1.00 33.68 O ANISOU 711 O SER B 149 2296 4075 6424 -319 -1278 1318 O ATOM 712 CB SER B 149 48.555 45.439 204.649 1.00 29.81 C ANISOU 712 CB SER B 149 1867 3219 6243 -190 -853 1210 C ATOM 713 OG SER B 149 48.954 44.777 205.835 1.00 29.80 O ANISOU 713 OG SER B 149 1930 3154 6239 -173 -688 1074 O ATOM 714 N ALA B 150 49.172 46.952 201.878 1.00 33.35 N ANISOU 714 N ALA B 150 2328 3919 6425 -290 -1156 1570 N ATOM 715 CA ALA B 150 48.710 47.484 200.602 1.00 35.73 C ANISOU 715 CA ALA B 150 2675 4320 6581 -325 -1351 1739 C ATOM 716 C ALA B 150 49.433 46.823 199.436 1.00 44.74 C ANISOU 716 C ALA B 150 3933 5699 7369 -426 -1367 1666 C ATOM 717 O ALA B 150 48.805 46.443 198.442 1.00 43.04 O ANISOU 717 O ALA B 150 3726 5619 7009 -464 -1548 1673 O ATOM 718 CB ALA B 150 48.900 49.000 200.564 1.00 36.59 C ANISOU 718 CB ALA B 150 2825 4326 6750 -312 -1358 1976 C ATOM 719 N MET B 151 50.757 46.669 199.544 1.00 45.98 N ANISOU 719 N MET B 151 4168 5920 7383 -473 -1179 1577 N ATOM 720 CA MET B 151 51.521 46.026 198.479 1.00 42.74 C ANISOU 720 CA MET B 151 3851 5746 6642 -565 -1156 1468 C ATOM 721 C MET B 151 51.107 44.574 198.285 1.00 38.52 C ANISOU 721 C MET B 151 3272 5279 6087 -561 -1214 1219 C ATOM 722 O MET B 151 51.175 44.055 197.165 1.00 38.91 O ANISOU 722 O MET B 151 3381 5533 5871 -632 -1288 1132 O ATOM 723 CB MET B 151 53.018 46.114 198.774 1.00 47.26 C ANISOU 723 CB MET B 151 4475 6355 7125 -602 -926 1397 C ATOM 724 CG MET B 151 53.613 47.489 198.532 1.00 58.12 C ANISOU 724 CG MET B 151 5922 7730 8429 -659 -876 1636 C ATOM 725 SD MET B 151 55.401 47.544 198.763 1.00 61.78 S ANISOU 725 SD MET B 151 6421 8270 8782 -724 -611 1538 S ATOM 726 CE MET B 151 55.524 47.203 200.517 1.00 51.28 C ANISOU 726 CE MET B 151 4985 6702 7799 -610 -502 1393 C ATOM 727 N ALA B 152 50.684 43.901 199.358 1.00 35.28 N ANISOU 727 N ALA B 152 2759 4699 5946 -490 -1180 1100 N ATOM 728 CA ALA B 152 50.213 42.527 199.226 1.00 38.40 C ANISOU 728 CA ALA B 152 3103 5113 6373 -494 -1247 880 C ATOM 729 C ALA B 152 48.975 42.454 198.342 1.00 49.39 C ANISOU 729 C ALA B 152 4465 6583 7718 -522 -1491 927 C ATOM 730 O ALA B 152 48.830 41.525 197.538 1.00 61.74 O ANISOU 730 O ALA B 152 6045 8274 9138 -574 -1582 753 O ATOM 731 CB ALA B 152 49.927 41.935 200.606 1.00 38.08 C ANISOU 731 CB ALA B 152 2960 4866 6643 -428 -1168 802 C ATOM 732 N VAL B 153 48.072 43.429 198.473 1.00 50.01 N ANISOU 732 N VAL B 153 4489 6582 7931 -484 -1609 1150 N ATOM 733 CA VAL B 153 46.897 43.471 197.611 1.00 40.35 C ANISOU 733 CA VAL B 153 3221 5438 6672 -504 -1868 1223 C ATOM 734 C VAL B 153 47.292 43.846 196.189 1.00 60.96 C ANISOU 734 C VAL B 153 5969 8294 8898 -593 -1972 1306 C ATOM 735 O VAL B 153 46.657 43.404 195.223 1.00 60.38 O ANISOU 735 O VAL B 153 5899 8376 8668 -647 -2175 1259 O ATOM 736 CB VAL B 153 45.852 44.444 198.190 1.00 40.38 C ANISOU 736 CB VAL B 153 3105 5273 6964 -421 -1962 1436 C ATOM 737 CG1 VAL B 153 44.573 44.418 197.365 1.00 42.89 C ANISOU 737 CG1 VAL B 153 3342 5663 7291 -432 -2253 1507 C ATOM 738 CG2 VAL B 153 45.561 44.104 199.644 1.00 38.15 C ANISOU 738 CG2 VAL B 153 2715 4780 7000 -349 -1800 1337 C ATOM 739 N GLU B 154 48.341 44.659 196.032 1.00 57.07 N ANISOU 739 N GLU B 154 5592 7856 8238 -622 -1837 1430 N ATOM 740 CA GLU B 154 48.812 45.017 194.697 1.00 56.79 C ANISOU 740 CA GLU B 154 5696 8079 7803 -729 -1902 1523 C ATOM 741 C GLU B 154 49.306 43.789 193.942 1.00 62.47 C ANISOU 741 C GLU B 154 6471 9021 8245 -807 -1865 1224 C ATOM 742 O GLU B 154 48.949 43.575 192.779 1.00 66.42 O ANISOU 742 O GLU B 154 7030 9749 8459 -889 -2035 1209 O ATOM 743 CB GLU B 154 49.921 46.068 194.793 1.00 62.75 C ANISOU 743 CB GLU B 154 6547 8830 8466 -760 -1726 1702 C ATOM 744 CG GLU B 154 49.536 47.335 195.539 1.00 61.71 C ANISOU 744 CG GLU B 154 6367 8455 8624 -683 -1749 1971 C ATOM 745 CD GLU B 154 48.646 48.251 194.728 1.00 68.62 C ANISOU 745 CD GLU B 154 7262 9357 9452 -696 -2011 2272 C ATOM 746 OE1 GLU B 154 48.519 48.031 193.506 1.00 79.18 O ANISOU 746 OE1 GLU B 154 8684 10944 10456 -790 -2160 2310 O ATOM 747 OE2 GLU B 154 48.072 49.193 195.316 1.00 69.41 O ANISOU 747 OE2 GLU B 154 7292 9231 9851 -609 -2074 2466 O ATOM 748 N ARG B 155 50.130 42.965 194.595 1.00 71.21 N ANISOU 748 N ARG B 155 7556 10064 9437 -781 -1652 975 N ATOM 749 CA ARG B 155 50.657 41.772 193.938 1.00 77.92 C ANISOU 749 CA ARG B 155 8442 11090 10074 -837 -1601 656 C ATOM 750 C ARG B 155 49.561 40.750 193.657 1.00 71.39 C ANISOU 750 C ARG B 155 7544 10258 9323 -840 -1804 474 C ATOM 751 O ARG B 155 49.635 40.025 192.658 1.00 69.97 O ANISOU 751 O ARG B 155 7415 10287 8882 -915 -1867 261 O ATOM 752 CB ARG B 155 51.761 41.145 194.792 1.00 80.17 C ANISOU 752 CB ARG B 155 8698 11265 10500 -787 -1347 451 C ATOM 753 CG ARG B 155 52.922 42.082 195.089 1.00 85.10 C ANISOU 753 CG ARG B 155 9373 11900 11062 -796 -1143 596 C ATOM 754 CD ARG B 155 53.957 41.427 195.994 1.00 92.24 C ANISOU 754 CD ARG B 155 10225 12689 12134 -736 -926 395 C ATOM 755 NE ARG B 155 55.050 42.340 196.319 1.00 98.25 N ANISOU 755 NE ARG B 155 11015 13458 12859 -752 -743 529 N ATOM 756 CZ ARG B 155 56.249 41.955 196.744 1.00100.66 C ANISOU 756 CZ ARG B 155 11288 13758 13199 -731 -545 369 C ATOM 757 NH1 ARG B 155 57.180 42.860 197.014 1.00102.53 N ANISOU 757 NH1 ARG B 155 11540 14006 13412 -760 -396 502 N ATOM 758 NH2 ARG B 155 56.522 40.667 196.893 1.00100.61 N ANISOU 758 NH2 ARG B 155 11227 13724 13276 -682 -505 76 N ATOM 759 N ALA B 156 48.546 40.674 194.520 1.00 62.52 N ANISOU 759 N ALA B 156 6297 8905 8555 -767 -1899 537 N ATOM 760 CA ALA B 156 47.455 39.730 194.302 1.00 61.68 C ANISOU 760 CA ALA B 156 6099 8776 8559 -783 -2095 377 C ATOM 761 C ALA B 156 46.633 40.114 193.078 1.00 66.21 C ANISOU 761 C ALA B 156 6707 9564 8887 -855 -2368 485 C ATOM 762 O ALA B 156 46.315 39.265 192.238 1.00 69.27 O ANISOU 762 O ALA B 156 7106 10104 9111 -928 -2505 268 O ATOM 763 CB ALA B 156 46.570 39.653 195.546 1.00 44.29 C ANISOU 763 CB ALA B 156 3741 6294 6792 -701 -2110 447 C ATOM 764 N LEU B 157 46.278 41.395 192.962 1.00 66.50 N ANISOU 764 N LEU B 157 6757 9608 8900 -836 -2463 819 N ATOM 765 CA LEU B 157 45.488 41.864 191.831 1.00 65.36 C ANISOU 765 CA LEU B 157 6643 9661 8530 -898 -2751 979 C ATOM 766 C LEU B 157 46.308 42.023 190.557 1.00 70.37 C ANISOU 766 C LEU B 157 7462 10626 8651 -1018 -2743 973 C ATOM 767 O LEU B 157 45.724 42.138 189.474 1.00 78.40 O ANISOU 767 O LEU B 157 8524 11866 9399 -1096 -2993 1043 O ATOM 768 CB LEU B 157 44.811 43.190 192.181 1.00 62.07 C ANISOU 768 CB LEU B 157 6167 9104 8314 -823 -2867 1353 C ATOM 769 CG LEU B 157 43.800 43.113 193.327 1.00 59.49 C ANISOU 769 CG LEU B 157 5635 8494 8476 -713 -2899 1363 C ATOM 770 CD1 LEU B 157 43.192 44.477 193.607 1.00 62.88 C ANISOU 770 CD1 LEU B 157 5999 8787 9106 -627 -3004 1705 C ATOM 771 CD2 LEU B 157 42.716 42.092 193.013 1.00 53.98 C ANISOU 771 CD2 LEU B 157 4812 7834 7865 -746 -3114 1174 C ATOM 772 N ALA B 158 47.638 42.032 190.657 1.00 68.77 N ANISOU 772 N ALA B 158 7357 10477 8297 -1040 -2466 892 N ATOM 773 CA ALA B 158 48.470 42.151 189.464 1.00 77.64 C ANISOU 773 CA ALA B 158 8642 11938 8919 -1167 -2417 867 C ATOM 774 C ALA B 158 48.533 40.833 188.701 1.00 85.17 C ANISOU 774 C ALA B 158 9617 13100 9645 -1240 -2445 463 C ATOM 775 O ALA B 158 48.330 40.802 187.482 1.00 85.15 O ANISOU 775 O ALA B 158 9708 13407 9239 -1354 -2604 445 O ATOM 776 CB ALA B 158 49.875 42.620 189.842 1.00 76.05 C ANISOU 776 CB ALA B 158 8509 11727 8661 -1170 -2100 907 C ATOM 777 N ILE B 159 48.810 39.734 189.403 1.00 83.81 N ANISOU 777 N ILE B 159 9360 12756 9726 -1178 -2302 134 N ATOM 778 CA ILE B 159 48.885 38.435 188.743 1.00 84.11 C ANISOU 778 CA ILE B 159 9407 12942 9611 -1236 -2323 -284 C ATOM 779 C ILE B 159 47.488 37.899 188.438 1.00 80.05 C ANISOU 779 C ILE B 159 8812 12408 9196 -1258 -2640 -356 C ATOM 780 O ILE B 159 47.314 37.102 187.509 1.00 80.28 O ANISOU 780 O ILE B 159 8876 12645 8982 -1346 -2754 -641 O ATOM 781 CB ILE B 159 49.701 37.452 189.601 1.00 80.62 C ANISOU 781 CB ILE B 159 8899 12291 9441 -1156 -2073 -592 C ATOM 782 CG1 ILE B 159 49.961 36.149 188.840 1.00 83.56 C ANISOU 782 CG1 ILE B 159 9287 12811 9650 -1212 -2067 -1054 C ATOM 783 CG2 ILE B 159 48.998 37.178 190.925 1.00 78.50 C ANISOU 783 CG2 ILE B 159 8486 11645 9696 -1048 -2107 -532 C ATOM 784 CD1 ILE B 159 50.674 36.343 187.519 1.00 87.12 C ANISOU 784 CD1 ILE B 159 9878 13675 9550 -1332 -2006 -1158 C ATOM 785 N ARG B 160 46.477 38.330 189.196 1.00 74.35 N ANISOU 785 N ARG B 160 7971 11448 8832 -1184 -2784 -117 N ATOM 786 CA ARG B 160 45.111 37.894 188.926 1.00 65.83 C ANISOU 786 CA ARG B 160 6785 10352 7876 -1210 -3092 -163 C ATOM 787 C ARG B 160 44.611 38.436 187.593 1.00 71.15 C ANISOU 787 C ARG B 160 7547 11357 8130 -1315 -3366 -23 C ATOM 788 O ARG B 160 43.860 37.758 186.883 1.00 82.93 O ANISOU 788 O ARG B 160 9007 12982 9521 -1390 -3607 -213 O ATOM 789 N ALA B 161 45.014 39.654 187.238 1.00 71.47 N ANISOU 789 N ALA B 161 7700 11532 7923 -1330 -3348 317 N ATOM 790 CA ALA B 161 44.632 40.273 185.969 1.00 80.78 C ANISOU 790 CA ALA B 161 8985 13038 8668 -1438 -3609 515 C ATOM 791 C ALA B 161 45.791 41.113 185.455 1.00 88.67 C ANISOU 791 C ALA B 161 10170 14251 9268 -1505 -3420 704 C ATOM 792 O ALA B 161 45.792 42.344 185.574 1.00 87.02 O ANISOU 792 O ALA B 161 9997 13987 9079 -1480 -3449 1118 O ATOM 793 CB ALA B 161 43.367 41.119 186.128 1.00 77.90 C ANISOU 793 CB ALA B 161 8508 12549 8542 -1377 -3916 879 C ATOM 794 N PRO B 162 46.813 40.472 184.877 1.00 90.47 N ANISOU 794 N PRO B 162 10510 14719 9147 -1594 -3214 401 N ATOM 795 CA PRO B 162 47.923 41.243 184.294 1.00 87.74 C ANISOU 795 CA PRO B 162 10330 14620 8386 -1686 -3023 573 C ATOM 796 C PRO B 162 47.509 42.085 183.102 1.00 91.11 C ANISOU 796 C PRO B 162 10890 15372 8355 -1817 -3282 901 C ATOM 797 O PRO B 162 48.192 43.069 182.792 1.00 91.20 O ANISOU 797 O PRO B 162 11023 15508 8120 -1885 -3174 1211 O ATOM 798 CB PRO B 162 48.932 40.160 183.884 1.00 87.88 C ANISOU 798 CB PRO B 162 10399 14839 8154 -1749 -2772 95 C ATOM 799 CG PRO B 162 48.539 38.941 184.669 1.00 85.92 C ANISOU 799 CG PRO B 162 9998 14308 8341 -1644 -2766 -277 C ATOM 800 CD PRO B 162 47.051 39.022 184.800 1.00 89.74 C ANISOU 800 CD PRO B 162 10380 14654 9063 -1610 -3121 -121 C ATOM 801 N HIS B 163 46.417 41.728 182.423 1.00 97.88 N ANISOU 801 N HIS B 163 11726 16371 9092 -1864 -3631 855 N ATOM 802 CA HIS B 163 45.954 42.510 181.282 1.00103.89 C ANISOU 802 CA HIS B 163 12613 17450 9411 -1988 -3924 1191 C ATOM 803 C HIS B 163 45.424 43.869 181.723 1.00107.46 C ANISOU 803 C HIS B 163 13030 17667 10133 -1905 -4083 1747 C ATOM 804 O HIS B 163 45.827 44.908 181.186 1.00106.45 O ANISOU 804 O HIS B 163 13047 17661 9738 -1973 -4064 2115 O ATOM 805 CB HIS B 163 44.879 41.728 180.526 1.00101.94 C ANISOU 805 CB HIS B 163 12331 17365 9038 -2033 -4255 966 C ATOM 806 CG HIS B 163 44.030 40.869 181.410 1.00 93.97 C ANISOU 806 CG HIS B 163 11099 16047 8557 -1923 -4366 712 C ATOM 807 ND1 HIS B 163 44.347 39.559 181.701 1.00 89.63 N ANISOU 807 ND1 HIS B 163 10491 15431 8135 -1912 -4188 194 N ATOM 808 CD2 HIS B 163 42.879 41.133 182.072 1.00 91.51 C ANISOU 808 CD2 HIS B 163 10620 15397 8754 -1777 -4555 885 C ATOM 809 CE1 HIS B 163 43.426 39.053 182.502 1.00 89.10 C ANISOU 809 CE1 HIS B 163 10228 15044 8582 -1810 -4312 98 C ATOM 810 NE2 HIS B 163 42.524 39.987 182.742 1.00 90.38 N ANISOU 810 NE2 HIS B 163 10309 15072 8960 -1742 -4547 511 N ATOM 811 N TRP B 164 44.517 43.881 182.701 1.00106.81 N ANISOU 811 N TRP B 164 12753 17207 10623 -1744 -4204 1793 N ATOM 812 CA TRP B 164 43.941 45.136 183.171 1.00110.35 C ANISOU 812 CA TRP B 164 13150 17359 11419 -1618 -4305 2243 C ATOM 813 C TRP B 164 44.899 45.903 184.073 1.00106.59 C ANISOU 813 C TRP B 164 12687 16675 11139 -1572 -4022 2441 C ATOM 814 O TRP B 164 44.856 47.137 184.108 1.00106.54 O ANISOU 814 O TRP B 164 12723 16541 11217 -1540 -4068 2857 O ATOM 815 CB TRP B 164 42.628 44.866 183.908 1.00109.67 C ANISOU 815 CB TRP B 164 12842 16939 11888 -1449 -4463 2166 C ATOM 816 CG TRP B 164 41.892 46.108 184.313 1.00110.83 C ANISOU 816 CG TRP B 164 12925 16777 12409 -1300 -4541 2545 C ATOM 817 CD1 TRP B 164 40.992 46.807 183.561 1.00111.93 C ANISOU 817 CD1 TRP B 164 13091 16930 12508 -1266 -4774 2780 C ATOM 818 CD2 TRP B 164 41.994 46.801 185.564 1.00108.74 C ANISOU 818 CD2 TRP B 164 12555 16141 12622 -1164 -4377 2702 C ATOM 819 NE1 TRP B 164 40.526 47.890 184.266 1.00111.62 N ANISOU 819 NE1 TRP B 164 12964 16544 12904 -1120 -4761 3059 N ATOM 820 CE2 TRP B 164 41.126 47.910 185.498 1.00108.34 C ANISOU 820 CE2 TRP B 164 12471 15888 12804 -1055 -4510 3005 C ATOM 821 CE3 TRP B 164 42.734 46.593 186.731 1.00105.53 C ANISOU 821 CE3 TRP B 164 12074 15555 12469 -1122 -4130 2599 C ATOM 822 CZ2 TRP B 164 40.977 48.806 186.555 1.00105.58 C ANISOU 822 CZ2 TRP B 164 12026 15166 12924 -913 -4385 3173 C ATOM 823 CZ3 TRP B 164 42.585 47.484 187.780 1.00103.39 C ANISOU 823 CZ3 TRP B 164 11712 14919 12650 -977 -4012 2785 C ATOM 824 CH2 TRP B 164 41.714 48.576 187.684 1.00104.10 C ANISOU 824 CH2 TRP B 164 11780 14816 12956 -877 -4131 3052 C ATOM 825 N TYR B 165 45.764 45.196 184.804 1.00102.13 N ANISOU 825 N TYR B 165 12096 16002 10705 -1538 -3671 2105 N ATOM 826 CA TYR B 165 46.683 45.868 185.717 1.00 96.69 C ANISOU 826 CA TYR B 165 11415 15077 10244 -1475 -3361 2232 C ATOM 827 C TYR B 165 47.783 46.602 184.960 1.00 97.08 C ANISOU 827 C TYR B 165 11659 15377 9848 -1620 -3210 2443 C ATOM 828 O TYR B 165 48.190 47.700 185.358 1.00 98.71 O ANISOU 828 O TYR B 165 11896 15416 10193 -1600 -3118 2768 O ATOM 829 N ALA B 166 48.279 46.015 183.871 1.00 97.56 N ANISOU 829 N ALA B 166 11848 15842 9377 -1777 -3173 2252 N ATOM 830 CA ALA B 166 49.360 46.626 183.109 1.00 97.23 C ANISOU 830 CA ALA B 166 11984 16084 8874 -1940 -2996 2427 C ATOM 831 C ALA B 166 48.908 47.804 182.256 1.00100.61 C ANISOU 831 C ALA B 166 12535 16652 9040 -2040 -3270 2951 C ATOM 832 O ALA B 166 49.757 48.471 181.656 1.00100.19 O ANISOU 832 O ALA B 166 12632 16810 8626 -2191 -3134 3181 O ATOM 833 N SER B 167 47.604 48.077 182.186 1.00101.15 N ANISOU 833 N SER B 167 12535 16605 9294 -1965 -3654 3157 N ATOM 834 CA SER B 167 47.085 49.159 181.364 1.00109.94 C ANISOU 834 CA SER B 167 13754 17692 10325 -1981 -3822 3545 C ATOM 835 C SER B 167 46.287 50.206 182.126 1.00109.33 C ANISOU 835 C SER B 167 13566 17150 10826 -1803 -3952 3863 C ATOM 836 O SER B 167 46.141 51.325 181.621 1.00112.84 O ANISOU 836 O SER B 167 14098 17520 11257 -1822 -4027 4224 O ATOM 837 N HIS B 168 45.766 49.886 183.312 1.00101.91 N ANISOU 837 N HIS B 168 12429 15892 10401 -1632 -3966 3718 N ATOM 838 CA HIS B 168 44.935 50.814 184.064 1.00 93.32 C ANISOU 838 CA HIS B 168 11215 14365 9877 -1451 -4057 3940 C ATOM 839 C HIS B 168 45.550 51.264 185.381 1.00 92.98 C ANISOU 839 C HIS B 168 11090 13999 10241 -1361 -3824 3983 C ATOM 840 O HIS B 168 44.995 52.161 186.025 1.00 94.46 O ANISOU 840 O HIS B 168 11187 13819 10885 -1221 -3849 4149 O ATOM 841 CB HIS B 168 43.558 50.191 184.340 1.00 86.41 C ANISOU 841 CB HIS B 168 10158 13355 9318 -1307 -4271 3736 C ATOM 842 CG HIS B 168 42.760 49.921 183.103 1.00 87.97 C ANISOU 842 CG HIS B 168 10414 13808 9202 -1365 -4541 3728 C ATOM 843 ND1 HIS B 168 43.109 48.951 182.188 1.00 88.80 N ANISOU 843 ND1 HIS B 168 10627 14323 8791 -1517 -4568 3492 N ATOM 844 CD2 HIS B 168 41.628 50.495 182.629 1.00 92.78 C ANISOU 844 CD2 HIS B 168 10984 14328 9939 -1288 -4795 3910 C ATOM 845 CE1 HIS B 168 42.227 48.939 181.204 1.00 97.45 C ANISOU 845 CE1 HIS B 168 11753 15568 9704 -1533 -4833 3535 C ATOM 846 NE2 HIS B 168 41.318 49.866 181.448 1.00 98.58 N ANISOU 846 NE2 HIS B 168 11806 15419 10232 -1394 -4984 3800 N ATOM 847 N MET B 169 46.667 50.675 185.800 1.00 92.31 N ANISOU 847 N MET B 169 11026 14045 10004 -1435 -3596 3817 N ATOM 848 CA MET B 169 47.326 51.115 187.022 1.00 90.60 C ANISOU 848 CA MET B 169 10746 13505 10173 -1344 -3319 3809 C ATOM 849 C MET B 169 47.982 52.470 186.792 1.00 93.11 C ANISOU 849 C MET B 169 11191 13756 10431 -1422 -3262 4224 C ATOM 850 O MET B 169 48.722 52.657 185.820 1.00 99.73 O ANISOU 850 O MET B 169 12202 14888 10803 -1604 -3195 4344 O ATOM 851 CB MET B 169 48.365 50.088 187.468 1.00 89.38 C ANISOU 851 CB MET B 169 10593 13435 9932 -1373 -2960 3376 C ATOM 852 CG MET B 169 49.082 50.438 188.764 1.00 90.78 C ANISOU 852 CG MET B 169 10703 13297 10494 -1281 -2666 3320 C ATOM 853 SD MET B 169 47.986 50.456 190.197 1.00 90.91 S ANISOU 853 SD MET B 169 10494 12880 11168 -1051 -2744 3249 S ATOM 854 CE MET B 169 49.147 50.833 191.507 1.00 86.35 C ANISOU 854 CE MET B 169 9893 12046 10869 -1002 -2368 3162 C ATOM 855 N LYS B 170 47.708 53.418 187.683 1.00 88.72 N ANISOU 855 N LYS B 170 10548 12782 10380 -1285 -3222 4359 N ATOM 856 CA LYS B 170 48.221 54.772 187.559 1.00 83.67 C ANISOU 856 CA LYS B 170 10005 11978 9809 -1336 -3133 4663 C ATOM 857 C LYS B 170 48.978 55.157 188.821 1.00 73.49 C ANISOU 857 C LYS B 170 8650 10400 8874 -1272 -2880 4623 C ATOM 858 O LYS B 170 48.699 54.652 189.913 1.00 65.96 O ANISOU 858 O LYS B 170 7546 9261 8256 -1129 -2828 4406 O ATOM 859 N THR B 171 49.945 56.061 188.657 1.00 70.66 N ANISOU 859 N THR B 171 8401 10005 8440 -1387 -2714 4818 N ATOM 860 CA THR B 171 50.740 56.521 189.789 1.00 67.61 C ANISOU 860 CA THR B 171 7964 9348 8376 -1347 -2466 4773 C ATOM 861 C THR B 171 49.931 57.378 190.753 1.00 65.31 C ANISOU 861 C THR B 171 7536 8613 8667 -1156 -2521 4757 C ATOM 862 O THR B 171 50.311 57.498 191.922 1.00 62.28 O ANISOU 862 O THR B 171 7066 7995 8603 -1075 -2341 4612 O ATOM 863 CB THR B 171 51.959 57.300 189.294 1.00 73.17 C ANISOU 863 CB THR B 171 8808 10135 8859 -1534 -2276 4957 C ATOM 864 OG1 THR B 171 51.536 58.332 188.393 1.00 80.46 O ANISOU 864 OG1 THR B 171 9813 11023 9734 -1581 -2445 5230 O ATOM 865 CG2 THR B 171 52.926 56.370 188.574 1.00 68.41 C ANISOU 865 CG2 THR B 171 8313 9984 7696 -1727 -2122 4883 C ATOM 866 N ARG B 172 48.828 57.974 190.293 1.00 79.94 N ANISOU 866 N ARG B 172 9364 10361 10650 -1087 -2755 4884 N ATOM 867 CA ARG B 172 47.983 58.762 191.182 1.00 80.22 C ANISOU 867 CA ARG B 172 9256 10009 11216 -909 -2797 4835 C ATOM 868 C ARG B 172 47.259 57.898 192.205 1.00 78.27 C ANISOU 868 C ARG B 172 8836 9662 11243 -747 -2775 4530 C ATOM 869 O ARG B 172 46.877 58.403 193.267 1.00 72.68 O ANISOU 869 O ARG B 172 8002 8653 10959 -616 -2696 4402 O ATOM 870 N ILE B 173 47.061 56.612 191.910 1.00 79.29 N ANISOU 870 N ILE B 173 8951 10046 11128 -763 -2837 4392 N ATOM 871 CA ILE B 173 46.500 55.700 192.901 1.00 86.85 C ANISOU 871 CA ILE B 173 9745 10922 12332 -629 -2788 4088 C ATOM 872 C ILE B 173 47.545 55.355 193.955 1.00 83.63 C ANISOU 872 C ILE B 173 9313 10448 12013 -623 -2523 3933 C ATOM 873 O ILE B 173 47.236 55.259 195.149 1.00 82.43 O ANISOU 873 O ILE B 173 9027 10080 12213 -498 -2403 3721 O ATOM 874 CB ILE B 173 45.938 54.441 192.210 1.00 91.07 C ANISOU 874 CB ILE B 173 10262 11747 12595 -654 -2957 3969 C ATOM 875 CG1 ILE B 173 44.452 54.620 191.876 1.00 92.98 C ANISOU 875 CG1 ILE B 173 10416 11911 13003 -563 -3180 3974 C ATOM 876 CG2 ILE B 173 46.143 53.200 193.072 1.00 88.82 C ANISOU 876 CG2 ILE B 173 9866 11502 12379 -605 -2830 3661 C ATOM 877 CD1 ILE B 173 44.163 55.706 190.861 1.00100.44 C ANISOU 877 CD1 ILE B 173 11462 12856 13846 -613 -3359 4285 C ATOM 878 N THR B 174 48.801 55.178 193.532 1.00 77.57 N ANISOU 878 N THR B 174 8679 9879 10914 -768 -2414 4031 N ATOM 879 CA THR B 174 49.870 54.868 194.477 1.00 72.21 C ANISOU 879 CA THR B 174 7992 9149 10295 -779 -2088 3777 C ATOM 880 C THR B 174 50.059 55.992 195.488 1.00 72.87 C ANISOU 880 C THR B 174 8026 8877 10785 -705 -1995 3871 C ATOM 881 O THR B 174 50.250 55.737 196.683 1.00 74.16 O ANISOU 881 O THR B 174 8095 8891 11190 -620 -1814 3621 O ATOM 882 CB THR B 174 51.173 54.597 193.722 1.00 75.29 C ANISOU 882 CB THR B 174 8534 9829 10245 -967 -1912 3763 C ATOM 883 OG1 THR B 174 51.010 53.446 192.883 1.00 76.49 O ANISOU 883 OG1 THR B 174 8720 10309 10034 -1024 -1973 3595 O ATOM 884 CG2 THR B 174 52.319 54.348 194.694 1.00 70.49 C ANISOU 884 CG2 THR B 174 7900 9158 9725 -974 -1593 3515 C ATOM 885 N ARG B 175 50.003 57.246 195.030 1.00 70.78 N ANISOU 885 N ARG B 175 7824 8497 10572 -746 -2056 4085 N ATOM 886 CA ARG B 175 50.109 58.371 195.953 1.00 65.06 C ANISOU 886 CA ARG B 175 7043 7456 10220 -677 -1941 4033 C ATOM 887 C ARG B 175 48.912 58.444 196.894 1.00 65.57 C ANISOU 887 C ARG B 175 6939 7302 10673 -496 -1983 3832 C ATOM 888 O ARG B 175 49.054 58.884 198.040 1.00 60.56 O ANISOU 888 O ARG B 175 6225 6460 10325 -423 -1830 3660 O ATOM 889 CB ARG B 175 50.255 59.682 195.180 1.00 68.74 C ANISOU 889 CB ARG B 175 7606 7854 10659 -757 -2023 4299 C ATOM 890 CG ARG B 175 51.550 59.800 194.393 1.00 84.76 C ANISOU 890 CG ARG B 175 9797 10082 12327 -958 -1916 4473 C ATOM 891 CD ARG B 175 51.726 61.197 193.817 1.00 92.58 C ANISOU 891 CD ARG B 175 10867 10951 13358 -1028 -1974 4719 C ATOM 892 NE ARG B 175 50.699 61.529 192.834 1.00 99.24 N ANISOU 892 NE ARG B 175 11738 11831 14137 -1014 -2241 4932 N ATOM 893 CZ ARG B 175 50.822 61.321 191.527 1.00103.08 C ANISOU 893 CZ ARG B 175 12358 12602 14206 -1157 -2348 5149 C ATOM 894 NH1 ARG B 175 51.931 60.781 191.041 1.00100.08 N ANISOU 894 NH1 ARG B 175 12090 12506 13430 -1330 -2190 5171 N ATOM 895 NH2 ARG B 175 49.836 61.655 190.705 1.00107.66 N ANISOU 895 NH2 ARG B 175 12954 13198 14753 -1133 -2602 5332 N ATOM 896 N ALA B 176 47.733 58.018 196.433 1.00 73.56 N ANISOU 896 N ALA B 176 7893 8378 11679 -435 -2176 3833 N ATOM 897 CA ALA B 176 46.548 58.062 197.284 1.00 54.17 C ANISOU 897 CA ALA B 176 5274 5738 9569 -285 -2189 3635 C ATOM 898 C ALA B 176 46.629 57.030 198.402 1.00 52.28 C ANISOU 898 C ALA B 176 4941 5507 9415 -226 -2012 3336 C ATOM 899 O ALA B 176 46.246 57.313 199.544 1.00 49.30 O ANISOU 899 O ALA B 176 4457 4946 9327 -138 -1886 3142 O ATOM 900 CB ALA B 176 45.290 57.847 196.444 1.00 56.64 C ANISOU 900 CB ALA B 176 5551 6129 9841 -250 -2435 3712 C ATOM 901 N VAL B 177 47.120 55.828 198.095 1.00 51.22 N ANISOU 901 N VAL B 177 4844 5596 9021 -279 -2002 3294 N ATOM 902 CA VAL B 177 47.239 54.793 199.118 1.00 51.18 C ANISOU 902 CA VAL B 177 4751 5603 9093 -227 -1843 3020 C ATOM 903 C VAL B 177 48.323 55.157 200.126 1.00 52.55 C ANISOU 903 C VAL B 177 4939 5653 9375 -232 -1608 2939 C ATOM 904 O VAL B 177 48.154 54.963 201.336 1.00 49.04 O ANISOU 904 O VAL B 177 4405 5098 9130 -164 -1453 2706 O ATOM 905 CB VAL B 177 47.507 53.426 198.463 1.00 50.17 C ANISOU 905 CB VAL B 177 4638 5752 8670 -279 -1920 2985 C ATOM 906 CG1 VAL B 177 47.644 52.345 199.525 1.00 42.26 C ANISOU 906 CG1 VAL B 177 3548 4754 7752 -237 -1737 2670 C ATOM 907 CG2 VAL B 177 46.395 53.082 197.482 1.00 50.17 C ANISOU 907 CG2 VAL B 177 4624 5880 8558 -284 -2161 3031 C ATOM 908 N LEU B 178 49.452 55.689 199.649 1.00 53.41 N ANISOU 908 N LEU B 178 5172 5793 9329 -333 -1567 3122 N ATOM 909 CA LEU B 178 50.515 56.099 200.561 1.00 58.85 C ANISOU 909 CA LEU B 178 5881 6363 10117 -357 -1343 3033 C ATOM 910 C LEU B 178 50.068 57.255 201.448 1.00 56.56 C ANISOU 910 C LEU B 178 5515 5831 10144 -280 -1289 2933 C ATOM 911 O LEU B 178 50.418 57.308 202.633 1.00 53.86 O ANISOU 911 O LEU B 178 5118 5392 9954 -240 -1117 2727 O ATOM 912 CB LEU B 178 51.767 56.482 199.771 1.00 73.46 C ANISOU 912 CB LEU B 178 7884 8320 11708 -521 -1282 3221 C ATOM 913 CG LEU B 178 52.497 55.358 199.034 1.00 76.92 C ANISOU 913 CG LEU B 178 8401 9097 11727 -636 -1203 3109 C ATOM 914 CD1 LEU B 178 53.644 55.921 198.206 1.00 78.81 C ANISOU 914 CD1 LEU B 178 8774 9459 11713 -811 -1126 3294 C ATOM 915 CD2 LEU B 178 53.003 54.311 200.015 1.00 72.34 C ANISOU 915 CD2 LEU B 178 7757 8570 11158 -600 -1006 2767 C ATOM 916 N LEU B 179 49.293 58.189 200.894 1.00 60.36 N ANISOU 916 N LEU B 179 5991 6222 10721 -259 -1442 3075 N ATOM 917 CA LEU B 179 48.815 59.317 201.687 1.00 59.32 C ANISOU 917 CA LEU B 179 5779 5857 10904 -180 -1407 2986 C ATOM 918 C LEU B 179 47.716 58.898 202.655 1.00 52.89 C ANISOU 918 C LEU B 179 4821 4979 10296 -70 -1364 2743 C ATOM 919 O LEU B 179 47.626 59.444 203.761 1.00 52.37 O ANISOU 919 O LEU B 179 4682 4766 10452 -16 -1239 2568 O ATOM 920 CB LEU B 179 48.320 60.433 200.766 1.00 62.99 C ANISOU 920 CB LEU B 179 6279 6229 11425 -190 -1593 3227 C ATOM 921 CG LEU B 179 48.000 61.776 201.424 1.00 62.96 C ANISOU 921 CG LEU B 179 6207 5964 11750 -121 -1574 3179 C ATOM 922 CD1 LEU B 179 49.270 62.421 201.961 1.00 51.62 C ANISOU 922 CD1 LEU B 179 4831 4447 10337 -177 -1414 3139 C ATOM 923 CD2 LEU B 179 47.300 62.700 200.439 1.00 64.75 C ANISOU 923 CD2 LEU B 179 6454 6100 12048 -114 -1793 3429 C ATOM 924 N GLY B 180 46.875 57.939 202.262 1.00 48.27 N ANISOU 924 N GLY B 180 4201 4514 9625 -47 -1461 2724 N ATOM 925 CA GLY B 180 45.810 57.495 203.146 1.00 44.75 C ANISOU 925 CA GLY B 180 3635 4021 9346 34 -1402 2499 C ATOM 926 C GLY B 180 46.329 56.776 204.376 1.00 45.36 C ANISOU 926 C GLY B 180 3691 4122 9422 34 -1179 2259 C ATOM 927 O GLY B 180 45.823 56.980 205.484 1.00 41.33 O ANISOU 927 O GLY B 180 3106 3508 9090 85 -1059 2072 O ATOM 928 N VAL B 181 47.340 55.922 204.201 1.00 41.80 N ANISOU 928 N VAL B 181 3308 3812 8761 -25 -1124 2267 N ATOM 929 CA VAL B 181 47.908 55.191 205.331 1.00 40.79 C ANISOU 929 CA VAL B 181 3171 3712 8618 -27 -926 2057 C ATOM 930 C VAL B 181 48.571 56.151 206.313 1.00 46.19 C ANISOU 930 C VAL B 181 3842 4258 9448 -23 -781 1976 C ATOM 931 O VAL B 181 48.458 55.988 207.534 1.00 45.68 O ANISOU 931 O VAL B 181 3739 4149 9467 0 -632 1773 O ATOM 932 CB VAL B 181 48.896 54.121 204.830 1.00 40.08 C ANISOU 932 CB VAL B 181 3140 3796 8293 -80 -921 2095 C ATOM 933 CG1 VAL B 181 49.597 53.447 206.001 1.00 33.44 C ANISOU 933 CG1 VAL B 181 2297 2972 7437 -83 -723 1890 C ATOM 934 CG2 VAL B 181 48.171 53.092 203.978 1.00 46.41 C ANISOU 934 CG2 VAL B 181 3933 4750 8953 -81 -1065 2114 C ATOM 935 N TRP B 182 49.270 57.166 205.796 1.00 39.65 N ANISOU 935 N TRP B 182 3064 3368 8633 -54 -824 2130 N ATOM 936 CA TRP B 182 49.941 58.129 206.666 1.00 38.27 C ANISOU 936 CA TRP B 182 2883 3066 8594 -50 -702 2038 C ATOM 937 C TRP B 182 48.938 58.893 207.524 1.00 46.13 C ANISOU 937 C TRP B 182 3777 3901 9850 25 -674 1898 C ATOM 938 O TRP B 182 49.105 59.003 208.745 1.00 39.15 O ANISOU 938 O TRP B 182 2848 2964 9063 45 -525 1696 O ATOM 939 CB TRP B 182 50.786 59.094 205.830 1.00 39.96 C ANISOU 939 CB TRP B 182 3195 3235 8752 -112 -762 2240 C ATOM 940 CG TRP B 182 52.022 58.475 205.233 1.00 62.38 C ANISOU 940 CG TRP B 182 6149 6224 11326 -214 -720 2334 C ATOM 941 CD1 TRP B 182 52.663 57.346 205.656 1.00 53.09 C ANISOU 941 CD1 TRP B 182 4983 5173 10015 -239 -605 2211 C ATOM 942 CD2 TRP B 182 52.767 58.959 204.106 1.00 57.44 C ANISOU 942 CD2 TRP B 182 5647 5644 10533 -325 -777 2566 C ATOM 943 NE1 TRP B 182 53.757 57.096 204.862 1.00 36.47 N ANISOU 943 NE1 TRP B 182 2991 3194 7674 -363 -575 2329 N ATOM 944 CE2 TRP B 182 53.842 58.071 203.903 1.00 38.94 C ANISOU 944 CE2 TRP B 182 3375 3470 7950 -424 -672 2552 C ATOM 945 CE3 TRP B 182 52.627 60.055 203.249 1.00 53.88 C ANISOU 945 CE3 TRP B 182 5253 5114 10107 -363 -899 2785 C ATOM 946 CZ2 TRP B 182 54.772 58.245 202.879 1.00 41.57 C ANISOU 946 CZ2 TRP B 182 3824 3918 8051 -570 -663 2736 C ATOM 947 CZ3 TRP B 182 53.552 60.226 202.233 1.00 53.28 C ANISOU 947 CZ3 TRP B 182 5306 5143 9795 -505 -904 2991 C ATOM 948 CH2 TRP B 182 54.610 59.326 202.057 1.00 48.83 C ANISOU 948 CH2 TRP B 182 4804 4770 8978 -612 -777 2960 C ATOM 949 N LEU B 183 47.884 59.428 206.902 1.00 50.00 N ANISOU 949 N LEU B 183 4230 4314 10452 66 -820 2003 N ATOM 950 CA LEU B 183 46.916 60.233 207.643 1.00 43.36 C ANISOU 950 CA LEU B 183 3287 3307 9881 144 -800 1876 C ATOM 951 C LEU B 183 46.083 59.380 208.594 1.00 42.74 C ANISOU 951 C LEU B 183 3141 3275 9823 180 -690 1660 C ATOM 952 O LEU B 183 45.721 59.837 209.685 1.00 42.52 O ANISOU 952 O LEU B 183 3044 3144 9966 225 -575 1474 O ATOM 953 CB LEU B 183 46.008 60.991 206.674 1.00 46.44 C ANISOU 953 CB LEU B 183 3651 3601 10393 184 -999 2058 C ATOM 954 CG LEU B 183 46.460 62.381 206.213 1.00 52.07 C ANISOU 954 CG LEU B 183 4401 4152 11231 178 -1082 2215 C ATOM 955 CD1 LEU B 183 46.668 63.297 207.411 1.00 52.73 C ANISOU 955 CD1 LEU B 183 4423 4058 11552 220 -945 2017 C ATOM 956 CD2 LEU B 183 47.719 62.308 205.364 1.00 56.29 C ANISOU 956 CD2 LEU B 183 5077 4783 11527 77 -1111 2410 C ATOM 957 N ALA B 184 45.766 58.144 208.202 1.00 40.74 N ANISOU 957 N ALA B 184 2915 3176 9389 159 -722 1679 N ATOM 958 CA ALA B 184 44.986 57.275 209.080 1.00 39.71 C ANISOU 958 CA ALA B 184 2747 3094 9247 185 -617 1491 C ATOM 959 C ALA B 184 45.777 56.887 210.323 1.00 51.18 C ANISOU 959 C ALA B 184 4241 4575 10631 157 -416 1312 C ATOM 960 O ALA B 184 45.226 56.854 211.430 1.00 39.33 O ANISOU 960 O ALA B 184 2699 3041 9204 194 -294 1132 O ATOM 961 CB ALA B 184 44.531 56.029 208.322 1.00 38.98 C ANISOU 961 CB ALA B 184 2684 3154 8973 166 -709 1551 C ATOM 962 N SER B 185 47.070 56.590 210.161 1.00 41.79 N ANISOU 962 N SER B 185 3129 3453 9294 96 -382 1363 N ATOM 963 CA SER B 185 47.888 56.198 211.304 1.00 36.53 C ANISOU 963 CA SER B 185 2513 2814 8554 72 -213 1207 C ATOM 964 C SER B 185 48.146 57.378 212.233 1.00 39.76 C ANISOU 964 C SER B 185 2868 3082 9158 92 -118 1087 C ATOM 965 O SER B 185 48.193 57.212 213.457 1.00 39.41 O ANISOU 965 O SER B 185 2833 3033 9107 106 22 900 O ATOM 966 CB SER B 185 49.203 55.590 210.820 1.00 42.66 C ANISOU 966 CB SER B 185 3371 3692 9146 11 -213 1294 C ATOM 967 OG SER B 185 48.968 54.438 210.027 1.00 35.05 O ANISOU 967 OG SER B 185 2455 2863 8000 1 -293 1365 O ATOM 968 N LEU B 186 48.321 58.577 211.671 1.00 42.58 N ANISOU 968 N LEU B 186 3179 3328 9672 104 -201 1187 N ATOM 969 CA LEU B 186 48.481 59.762 212.506 1.00 44.77 C ANISOU 969 CA LEU B 186 3403 3451 10157 134 -126 1054 C ATOM 970 C LEU B 186 47.204 60.078 213.273 1.00 49.90 C ANISOU 970 C LEU B 186 3969 4012 10979 205 -78 890 C ATOM 971 O LEU B 186 47.268 60.538 214.419 1.00 46.07 O ANISOU 971 O LEU B 186 3448 3457 10601 227 52 682 O ATOM 972 CB LEU B 186 48.901 60.958 211.649 1.00 43.04 C ANISOU 972 CB LEU B 186 3191 3116 10045 138 -245 1216 C ATOM 973 CG LEU B 186 49.051 62.306 212.360 1.00 44.32 C ANISOU 973 CG LEU B 186 3308 3084 10446 173 -195 1090 C ATOM 974 CD1 LEU B 186 50.159 62.251 213.401 1.00 40.99 C ANISOU 974 CD1 LEU B 186 2915 2684 9976 136 -41 911 C ATOM 975 CD2 LEU B 186 49.307 63.419 211.355 1.00 44.60 C ANISOU 975 CD2 LEU B 186 3383 2989 10575 170 -338 1294 C ATOM 976 N ALA B 187 46.041 59.830 212.666 1.00 52.04 N ANISOU 976 N ALA B 187 4199 4294 11278 247 -180 968 N ATOM 977 CA ALA B 187 44.777 60.093 213.347 1.00 52.61 C ANISOU 977 CA ALA B 187 4172 4297 11520 324 -133 814 C ATOM 978 C ALA B 187 44.589 59.165 214.541 1.00 45.22 C ANISOU 978 C ALA B 187 3251 3477 10452 322 40 615 C ATOM 979 O ALA B 187 44.072 59.584 215.584 1.00 42.51 O ANISOU 979 O ALA B 187 2834 3085 10234 371 158 412 O ATOM 980 CB ALA B 187 43.613 59.954 212.367 1.00 44.04 C ANISOU 980 CB ALA B 187 3032 3212 10487 367 -293 953 C ATOM 981 N PHE B 188 45.000 57.902 214.409 1.00 38.80 N ANISOU 981 N PHE B 188 2534 2829 9379 269 54 668 N ATOM 982 CA PHE B 188 44.892 56.973 215.530 1.00 37.62 C ANISOU 982 CA PHE B 188 2414 2809 9069 267 203 508 C ATOM 983 C PHE B 188 45.839 57.357 216.661 1.00 45.94 C ANISOU 983 C PHE B 188 3497 3852 10106 250 347 345 C ATOM 984 O PHE B 188 45.482 57.252 217.840 1.00 50.78 O ANISOU 984 O PHE B 188 4071 4525 10699 272 489 153 O ATOM 985 CB PHE B 188 45.168 55.544 215.064 1.00 35.42 C ANISOU 985 CB PHE B 188 2237 2696 8524 219 162 612 C ATOM 986 CG PHE B 188 45.064 54.519 216.160 1.00 34.41 C ANISOU 986 CG PHE B 188 2140 2721 8215 211 293 484 C ATOM 987 CD1 PHE B 188 43.827 54.059 216.579 1.00 39.08 C ANISOU 987 CD1 PHE B 188 2647 3373 8828 241 335 417 C ATOM 988 CD2 PHE B 188 46.201 54.020 216.774 1.00 32.75 C ANISOU 988 CD2 PHE B 188 2025 2604 7814 170 367 442 C ATOM 989 CE1 PHE B 188 43.724 53.121 217.588 1.00 41.51 C ANISOU 989 CE1 PHE B 188 2967 3839 8968 218 454 327 C ATOM 990 CE2 PHE B 188 46.106 53.081 217.785 1.00 32.16 C ANISOU 990 CE2 PHE B 188 1966 2689 7563 151 471 352 C ATOM 991 CZ PHE B 188 44.866 52.631 218.191 1.00 47.04 C ANISOU 991 CZ PHE B 188 3766 4637 9470 169 518 303 C ATOM 992 N ALA B 189 47.053 57.800 216.323 1.00 36.50 N ANISOU 992 N ALA B 189 2356 2598 8915 204 317 412 N ATOM 993 CA ALA B 189 48.027 58.159 217.347 1.00 39.18 C ANISOU 993 CA ALA B 189 2716 2925 9244 182 440 250 C ATOM 994 C ALA B 189 47.680 59.460 218.060 1.00 42.67 C ANISOU 994 C ALA B 189 3053 3213 9948 225 510 62 C ATOM 995 O ALA B 189 48.249 59.736 219.121 1.00 38.96 O ANISOU 995 O ALA B 189 2580 2751 9472 213 636 -139 O ATOM 996 CB ALA B 189 49.423 58.260 216.732 1.00 35.01 C ANISOU 996 CB ALA B 189 2257 2374 8671 119 385 377 C ATOM 997 N LEU B 190 46.770 60.262 217.507 1.00 49.32 N ANISOU 997 N LEU B 190 3806 3922 11013 278 426 109 N ATOM 998 CA LEU B 190 46.331 61.485 218.166 1.00 49.79 C ANISOU 998 CA LEU B 190 3761 3825 11331 334 485 -85 C ATOM 999 C LEU B 190 45.344 61.233 219.298 1.00 44.79 C ANISOU 999 C LEU B 190 3055 3270 10691 387 633 -321 C ATOM 1000 O LEU B 190 45.027 62.170 220.038 1.00 47.08 O ANISOU 1000 O LEU B 190 3257 3456 11173 432 716 -538 O ATOM 1001 CB LEU B 190 45.701 62.440 217.148 1.00 56.01 C ANISOU 1001 CB LEU B 190 4478 4444 12361 385 325 64 C ATOM 1002 CG LEU B 190 46.650 63.198 216.220 1.00 45.93 C ANISOU 1002 CG LEU B 190 3243 3060 11149 349 197 253 C ATOM 1003 CD1 LEU B 190 45.867 63.914 215.134 1.00 48.19 C ANISOU 1003 CD1 LEU B 190 3475 3219 11617 404 19 439 C ATOM 1004 CD2 LEU B 190 47.486 64.185 217.014 1.00 47.06 C ANISOU 1004 CD2 LEU B 190 3379 3080 11423 338 283 71 C ATOM 1005 N LEU B 191 44.860 60.001 219.452 1.00 51.20 N ANISOU 1005 N LEU B 191 3897 4273 11285 379 671 -288 N ATOM 1006 CA LEU B 191 43.865 59.719 220.483 1.00 59.58 C ANISOU 1006 CA LEU B 191 4871 5445 12323 420 817 -487 C ATOM 1007 C LEU B 191 44.348 60.012 221.901 1.00 61.16 C ANISOU 1007 C LEU B 191 5057 5714 12466 403 1010 -768 C ATOM 1008 O LEU B 191 43.569 60.599 222.672 1.00 60.89 O ANISOU 1008 O LEU B 191 4910 5661 12566 455 1123 -989 O ATOM 1009 CB LEU B 191 43.389 58.264 220.358 1.00 57.45 C ANISOU 1009 CB LEU B 191 4639 5382 11808 395 815 -372 C ATOM 1010 CG LEU B 191 42.136 57.987 219.521 1.00 59.29 C ANISOU 1010 CG LEU B 191 4798 5594 12136 440 705 -245 C ATOM 1011 CD1 LEU B 191 42.288 58.501 218.097 1.00 67.22 C ANISOU 1011 CD1 LEU B 191 5826 6439 13277 447 500 -31 C ATOM 1012 CD2 LEU B 191 41.820 56.500 219.518 1.00 50.98 C ANISOU 1012 CD2 LEU B 191 3787 4748 10834 398 715 -158 C ATOM 1013 N PRO B 192 45.564 59.635 222.322 1.00 60.56 N ANISOU 1013 N PRO B 192 5080 5734 12195 333 1057 -790 N ATOM 1014 CA PRO B 192 45.988 59.984 223.691 1.00 56.77 C ANISOU 1014 CA PRO B 192 4574 5337 11657 309 1237 -1083 C ATOM 1015 C PRO B 192 46.039 61.479 223.950 1.00 56.89 C ANISOU 1015 C PRO B 192 4517 5130 11967 347 1261 -1291 C ATOM 1016 O PRO B 192 45.813 61.908 225.089 1.00 54.51 O ANISOU 1016 O PRO B 192 4153 4888 11671 354 1422 -1588 O ATOM 1017 CB PRO B 192 47.380 59.347 223.800 1.00 55.51 C ANISOU 1017 CB PRO B 192 4530 5297 11265 224 1229 -1015 C ATOM 1018 CG PRO B 192 47.360 58.241 222.820 1.00 56.98 C ANISOU 1018 CG PRO B 192 4797 5555 11299 207 1098 -719 C ATOM 1019 CD PRO B 192 46.545 58.747 221.671 1.00 59.42 C ANISOU 1019 CD PRO B 192 5064 5670 11842 269 962 -572 C ATOM 1020 N VAL B 193 46.336 62.288 222.930 1.00 58.71 N ANISOU 1020 N VAL B 193 4755 5123 12430 363 1104 -1143 N ATOM 1021 CA VAL B 193 46.288 63.735 223.105 1.00 61.17 C ANISOU 1021 CA VAL B 193 4989 5208 13044 402 1102 -1313 C ATOM 1022 C VAL B 193 44.850 64.209 223.269 1.00 64.53 C ANISOU 1022 C VAL B 193 5280 5573 13665 496 1131 -1421 C ATOM 1023 O VAL B 193 44.586 65.187 223.980 1.00 65.10 O ANISOU 1023 O VAL B 193 5266 5544 13924 535 1215 -1686 O ATOM 1024 N LEU B 194 43.904 63.531 222.624 1.00 68.38 N ANISOU 1024 N LEU B 194 5739 6120 14121 533 1063 -1233 N ATOM 1025 CA LEU B 194 42.493 63.891 222.687 1.00 64.80 C ANISOU 1025 CA LEU B 194 5142 5615 13865 627 1079 -1314 C ATOM 1026 C LEU B 194 41.778 63.303 223.897 1.00 67.07 C ANISOU 1026 C LEU B 194 5362 6124 13998 636 1291 -1552 C ATOM 1027 O LEU B 194 40.575 63.537 224.055 1.00 79.30 O ANISOU 1027 O LEU B 194 6773 7656 15701 712 1331 -1645 O ATOM 1028 CB LEU B 194 41.785 63.452 221.401 1.00 59.96 C ANISOU 1028 CB LEU B 194 4517 4970 13294 657 897 -1010 C ATOM 1029 CG LEU B 194 41.783 64.414 220.206 1.00 65.31 C ANISOU 1029 CG LEU B 194 5173 5406 14236 694 687 -812 C ATOM 1030 CD1 LEU B 194 43.175 64.937 219.876 1.00 55.78 C ANISOU 1030 CD1 LEU B 194 4071 4100 13023 627 623 -727 C ATOM 1031 CD2 LEU B 194 41.175 63.733 218.989 1.00 74.78 C ANISOU 1031 CD2 LEU B 194 6382 6646 15385 701 518 -521 C ATOM 1032 N GLY B 195 42.475 62.550 224.748 1.00 63.37 N ANISOU 1032 N GLY B 195 4977 5877 13226 557 1427 -1646 N ATOM 1033 CA GLY B 195 41.911 62.004 225.964 1.00 68.98 C ANISOU 1033 CA GLY B 195 5628 6838 13744 542 1642 -1860 C ATOM 1034 C GLY B 195 41.744 60.498 225.969 1.00 72.56 C ANISOU 1034 C GLY B 195 6133 7554 13885 485 1666 -1679 C ATOM 1035 O GLY B 195 41.640 59.906 227.052 1.00 74.63 O ANISOU 1035 O GLY B 195 6379 8070 13906 432 1849 -1817 O ATOM 1036 N VAL B 196 41.712 59.860 224.801 1.00 71.72 N ANISOU 1036 N VAL B 196 6085 7401 13766 485 1487 -1373 N ATOM 1037 CA VAL B 196 41.499 58.419 224.705 1.00 69.79 C ANISOU 1037 CA VAL B 196 5884 7377 13254 431 1485 -1194 C ATOM 1038 C VAL B 196 42.871 57.755 224.626 1.00 69.90 C ANISOU 1038 C VAL B 196 6058 7476 13023 344 1440 -1069 C ATOM 1039 O VAL B 196 43.480 57.681 223.559 1.00 68.39 O ANISOU 1039 O VAL B 196 5960 7165 12860 338 1269 -865 O ATOM 1040 CB VAL B 196 40.625 58.055 223.504 1.00 63.08 C ANISOU 1040 CB VAL B 196 5002 6444 12522 475 1317 -968 C ATOM 1041 CG1 VAL B 196 40.346 56.558 223.485 1.00 53.08 C ANISOU 1041 CG1 VAL B 196 3770 5400 11000 412 1323 -816 C ATOM 1042 CG2 VAL B 196 39.328 58.848 223.536 1.00 65.90 C ANISOU 1042 CG2 VAL B 196 5182 6692 13164 570 1343 -1094 C ATOM 1043 N GLY B 197 43.352 57.260 225.759 1.00 68.28 N ANISOU 1043 N GLY B 197 5879 7497 12569 270 1597 -1190 N ATOM 1044 CA GLY B 197 44.649 56.617 225.841 1.00 61.42 C ANISOU 1044 CA GLY B 197 5138 6734 11465 185 1566 -1092 C ATOM 1045 C GLY B 197 45.652 57.477 226.592 1.00 63.52 C ANISOU 1045 C GLY B 197 5422 6977 11737 156 1652 -1319 C ATOM 1046 O GLY B 197 45.348 58.569 227.074 1.00 73.03 O ANISOU 1046 O GLY B 197 6548 8077 13122 200 1739 -1568 O ATOM 1047 N GLN B 198 46.875 56.955 226.678 1.00 62.18 N ANISOU 1047 N GLN B 198 5350 6904 11371 76 1618 -1241 N ATOM 1048 CA GLN B 198 47.938 57.648 227.389 1.00 62.45 C ANISOU 1048 CA GLN B 198 5397 6945 11385 28 1690 -1457 C ATOM 1049 C GLN B 198 49.288 57.073 226.985 1.00 49.92 C ANISOU 1049 C GLN B 198 3911 5400 9655 -44 1576 -1281 C ATOM 1050 O GLN B 198 49.424 55.862 226.793 1.00 39.96 O ANISOU 1050 O GLN B 198 2711 4292 8180 -93 1518 -1063 O ATOM 1051 CB GLN B 198 47.755 57.540 228.908 1.00 72.88 C ANISOU 1051 CB GLN B 198 6670 8533 12489 -40 1912 -1718 C ATOM 1052 CG GLN B 198 48.724 58.390 229.712 1.00 78.71 C ANISOU 1052 CG GLN B 198 7413 9284 13210 -90 1997 -2016 C ATOM 1053 CD GLN B 198 48.556 58.210 231.207 1.00 89.80 C ANISOU 1053 CD GLN B 198 8791 11004 14326 -179 2216 -2276 C ATOM 1054 OE1 GLN B 198 47.986 57.220 231.665 1.00 91.86 O ANISOU 1054 OE1 GLN B 198 9046 11511 14346 -234 2299 -2166 O ATOM 1055 NE2 GLN B 198 49.051 59.172 231.977 1.00 95.98 N ANISOU 1055 NE2 GLN B 198 9566 11784 15116 -205 2309 -2624 N ATOM 1056 N TYR B 199 50.277 57.953 226.856 1.00 53.92 N ANISOU 1056 N TYR B 199 4428 5760 10299 -55 1538 -1383 N ATOM 1057 CA TYR B 199 51.665 57.569 226.645 1.00 48.03 C ANISOU 1057 CA TYR B 199 3751 5070 9428 -141 1448 -1273 C ATOM 1058 C TYR B 199 52.430 57.770 227.947 1.00 53.97 C ANISOU 1058 C TYR B 199 4527 6007 9973 -245 1547 -1523 C ATOM 1059 O TYR B 199 52.401 58.861 228.525 1.00 64.98 O ANISOU 1059 O TYR B 199 5892 7312 11485 -232 1627 -1813 O ATOM 1060 CB TYR B 199 52.300 58.398 225.528 1.00 44.27 C ANISOU 1060 CB TYR B 199 3295 4312 9214 -108 1309 -1178 C ATOM 1061 CG TYR B 199 51.718 58.154 224.154 1.00 40.26 C ANISOU 1061 CG TYR B 199 2835 3656 8807 -35 1164 -895 C ATOM 1062 CD1 TYR B 199 51.477 56.865 223.696 1.00 47.74 C ANISOU 1062 CD1 TYR B 199 3860 4752 9529 -44 1092 -666 C ATOM 1063 CD2 TYR B 199 51.404 59.216 223.316 1.00 38.98 C ANISOU 1063 CD2 TYR B 199 2637 3206 8968 34 1094 -864 C ATOM 1064 CE1 TYR B 199 50.945 56.641 222.438 1.00 49.02 C ANISOU 1064 CE1 TYR B 199 4061 4801 9765 12 964 -445 C ATOM 1065 CE2 TYR B 199 50.870 59.003 222.060 1.00 38.11 C ANISOU 1065 CE2 TYR B 199 2560 2994 8927 78 959 -607 C ATOM 1066 CZ TYR B 199 50.643 57.715 221.625 1.00 41.50 C ANISOU 1066 CZ TYR B 199 3065 3594 9111 67 900 -414 C ATOM 1067 OH TYR B 199 50.111 57.500 220.373 1.00 40.52 O ANISOU 1067 OH TYR B 199 2968 3386 9042 101 769 -192 O ATOM 1068 N THR B 200 53.109 56.722 228.406 1.00 48.05 N ANISOU 1068 N THR B 200 3869 5504 8883 -349 1506 -1405 N ATOM 1069 CA THR B 200 53.845 56.765 229.660 1.00 55.34 C ANISOU 1069 CA THR B 200 4868 6644 9515 -462 1545 -1593 C ATOM 1070 C THR B 200 55.278 56.302 229.429 1.00 47.00 C ANISOU 1070 C THR B 200 3922 5638 8300 -544 1366 -1433 C ATOM 1071 O THR B 200 55.611 55.725 228.391 1.00 45.36 O ANISOU 1071 O THR B 200 3730 5345 8160 -519 1243 -1172 O ATOM 1072 CB THR B 200 53.173 55.902 230.739 1.00 59.09 C ANISOU 1072 CB THR B 200 5334 7427 9691 -520 1686 -1619 C ATOM 1073 OG1 THR B 200 53.833 56.103 231.994 1.00 70.11 O ANISOU 1073 OG1 THR B 200 6805 9044 10790 -632 1723 -1828 O ATOM 1074 CG2 THR B 200 53.244 54.431 230.367 1.00 48.10 C ANISOU 1074 CG2 THR B 200 3984 6156 8137 -553 1597 -1278 C ATOM 1075 N VAL B 201 56.129 56.565 230.417 1.00 41.26 N ANISOU 1075 N VAL B 201 3258 5059 7359 -644 1352 -1609 N ATOM 1076 CA VAL B 201 57.533 56.174 230.342 1.00 46.21 C ANISOU 1076 CA VAL B 201 3963 5753 7841 -725 1180 -1490 C ATOM 1077 C VAL B 201 57.647 54.680 230.610 1.00 45.02 C ANISOU 1077 C VAL B 201 3858 5837 7410 -764 1124 -1245 C ATOM 1078 O VAL B 201 57.061 54.160 231.567 1.00 49.50 O ANISOU 1078 O VAL B 201 4440 6627 7742 -807 1220 -1276 O ATOM 1079 CB VAL B 201 58.379 56.985 231.337 1.00 47.04 C ANISOU 1079 CB VAL B 201 4108 5941 7823 -824 1163 -1773 C ATOM 1080 CG1 VAL B 201 59.834 56.538 231.288 1.00 40.49 C ANISOU 1080 CG1 VAL B 201 3332 5197 6856 -906 974 -1648 C ATOM 1081 CG2 VAL B 201 58.267 58.472 231.043 1.00 42.72 C ANISOU 1081 CG2 VAL B 201 3514 5116 7603 -787 1211 -2018 C ATOM 1082 N GLN B 202 58.401 53.987 229.765 1.00 35.99 N ANISOU 1082 N GLN B 202 2735 4642 6300 -754 974 -1002 N ATOM 1083 CA GLN B 202 58.589 52.550 229.875 1.00 35.00 C ANISOU 1083 CA GLN B 202 2646 4679 5975 -776 894 -756 C ATOM 1084 C GLN B 202 59.962 52.230 230.458 1.00 45.43 C ANISOU 1084 C GLN B 202 4020 6149 7094 -858 741 -737 C ATOM 1085 O GLN B 202 60.900 53.027 230.386 1.00 43.09 O ANISOU 1085 O GLN B 202 3718 5790 6865 -891 671 -866 O ATOM 1086 CB GLN B 202 58.428 51.877 228.509 1.00 32.60 C ANISOU 1086 CB GLN B 202 2312 4216 5858 -695 830 -514 C ATOM 1087 CG GLN B 202 57.104 52.177 227.822 1.00 39.14 C ANISOU 1087 CG GLN B 202 3076 4892 6903 -610 943 -510 C ATOM 1088 CD GLN B 202 55.915 51.584 228.554 1.00 43.36 C ANISOU 1088 CD GLN B 202 3586 5569 7321 -619 1072 -501 C ATOM 1089 OE1 GLN B 202 56.022 50.539 229.198 1.00 48.60 O ANISOU 1089 OE1 GLN B 202 4292 6415 7758 -681 1048 -378 O ATOM 1090 NE2 GLN B 202 54.772 52.251 228.458 1.00 35.07 N ANISOU 1090 NE2 GLN B 202 2456 4431 6439 -561 1208 -622 N ATOM 1091 N TRP B 203 60.063 51.040 231.040 1.00 54.66 N ANISOU 1091 N TRP B 203 5231 7508 8029 -896 679 -564 N ATOM 1092 CA TRP B 203 61.326 50.576 231.592 1.00 36.27 C ANISOU 1092 CA TRP B 203 2940 5326 5517 -961 504 -504 C ATOM 1093 C TRP B 203 62.336 50.355 230.465 1.00 43.83 C ANISOU 1093 C TRP B 203 3853 6126 6676 -908 361 -383 C ATOM 1094 O TRP B 203 61.975 49.846 229.399 1.00 33.91 O ANISOU 1094 O TRP B 203 2567 4724 5592 -829 371 -229 O ATOM 1095 CB TRP B 203 61.105 49.280 232.375 1.00 37.10 C ANISOU 1095 CB TRP B 203 3099 5635 5361 -1003 459 -296 C ATOM 1096 CG TRP B 203 62.334 48.695 232.995 1.00 41.58 C ANISOU 1096 CG TRP B 203 3700 6357 5741 -1059 251 -197 C ATOM 1097 CD1 TRP B 203 62.807 48.928 234.254 1.00 40.58 C ANISOU 1097 CD1 TRP B 203 3628 6470 5322 -1164 193 -301 C ATOM 1098 CD2 TRP B 203 63.245 47.769 232.389 1.00 46.77 C ANISOU 1098 CD2 TRP B 203 4329 6945 6496 -1008 64 19 C ATOM 1099 NE1 TRP B 203 63.958 48.207 234.468 1.00 42.45 N ANISOU 1099 NE1 TRP B 203 3867 6786 5476 -1179 -38 -141 N ATOM 1100 CE2 TRP B 203 64.248 47.488 233.338 1.00 38.74 C ANISOU 1100 CE2 TRP B 203 3339 6120 5259 -1077 -115 50 C ATOM 1101 CE3 TRP B 203 63.311 47.153 231.135 1.00 34.61 C ANISOU 1101 CE3 TRP B 203 2737 5206 5209 -908 28 173 C ATOM 1102 CZ2 TRP B 203 65.303 46.618 233.074 1.00 38.44 C ANISOU 1102 CZ2 TRP B 203 3262 6062 5282 -1036 -328 234 C ATOM 1103 CZ3 TRP B 203 64.359 46.289 230.875 1.00 34.34 C ANISOU 1103 CZ3 TRP B 203 2669 5158 5220 -872 -163 330 C ATOM 1104 CH2 TRP B 203 65.341 46.030 231.839 1.00 41.08 C ANISOU 1104 CH2 TRP B 203 3535 6187 5888 -929 -340 362 C ATOM 1105 N PRO B 204 63.613 50.723 230.667 1.00 56.34 N ANISOU 1105 N PRO B 204 5421 7749 8237 -957 231 -460 N ATOM 1106 CA PRO B 204 64.196 51.278 231.890 1.00 37.39 C ANISOU 1106 CA PRO B 204 3050 5531 5624 -1060 179 -647 C ATOM 1107 C PRO B 204 64.305 52.800 231.893 1.00 38.30 C ANISOU 1107 C PRO B 204 3142 5538 5871 -1100 255 -942 C ATOM 1108 O PRO B 204 65.346 53.334 232.271 1.00 46.75 O ANISOU 1108 O PRO B 204 4193 6656 6913 -1174 148 -1076 O ATOM 1109 CB PRO B 204 65.586 50.641 231.913 1.00 37.46 C ANISOU 1109 CB PRO B 204 3025 5616 5593 -1077 -41 -525 C ATOM 1110 CG PRO B 204 65.911 50.366 230.440 1.00 42.11 C ANISOU 1110 CG PRO B 204 3540 5990 6469 -987 -59 -390 C ATOM 1111 CD PRO B 204 64.643 50.544 229.632 1.00 43.60 C ANISOU 1111 CD PRO B 204 3742 6012 6810 -918 115 -366 C ATOM 1112 N GLY B 205 63.247 53.485 231.474 1.00 46.89 N ANISOU 1112 N GLY B 205 4223 6466 7125 -1050 427 -1040 N ATOM 1113 CA GLY B 205 63.232 54.933 231.498 1.00 43.31 C ANISOU 1113 CA GLY B 205 3748 5871 6835 -1078 503 -1318 C ATOM 1114 C GLY B 205 63.828 55.606 230.286 1.00 37.87 C ANISOU 1114 C GLY B 205 3003 4922 6465 -1056 463 -1290 C ATOM 1115 O GLY B 205 64.111 56.808 230.343 1.00 39.17 O ANISOU 1115 O GLY B 205 3149 4956 6780 -1104 483 -1506 O ATOM 1116 N THR B 206 64.024 54.877 229.188 1.00 41.17 N ANISOU 1116 N THR B 206 3394 5260 6989 -994 411 -1035 N ATOM 1117 CA THR B 206 64.665 55.417 227.998 1.00 42.46 C ANISOU 1117 CA THR B 206 3507 5218 7409 -991 378 -979 C ATOM 1118 C THR B 206 63.727 55.530 226.804 1.00 37.10 C ANISOU 1118 C THR B 206 2821 4336 6940 -898 468 -848 C ATOM 1119 O THR B 206 64.165 55.957 225.731 1.00 32.54 O ANISOU 1119 O THR B 206 2212 3598 6554 -902 450 -769 O ATOM 1120 CB THR B 206 65.878 54.559 227.619 1.00 47.58 C ANISOU 1120 CB THR B 206 4111 5958 8009 -1008 237 -817 C ATOM 1121 OG1 THR B 206 65.470 53.194 227.455 1.00 44.44 O ANISOU 1121 OG1 THR B 206 3732 5656 7497 -931 214 -608 O ATOM 1122 CG2 THR B 206 66.949 54.641 228.701 1.00 38.34 C ANISOU 1122 CG2 THR B 206 2924 4964 6678 -1107 115 -951 C ATOM 1123 N TRP B 207 62.456 55.166 226.954 1.00 34.17 N ANISOU 1123 N TRP B 207 2472 3980 6531 -825 560 -817 N ATOM 1124 CA TRP B 207 61.521 55.231 225.840 1.00 36.88 C ANISOU 1124 CA TRP B 207 2798 4145 7068 -735 620 -689 C ATOM 1125 C TRP B 207 60.101 55.308 226.381 1.00 40.34 C ANISOU 1125 C TRP B 207 3234 4593 7501 -678 744 -773 C ATOM 1126 O TRP B 207 59.820 54.877 227.502 1.00 37.35 O ANISOU 1126 O TRP B 207 2875 4405 6910 -706 787 -857 O ATOM 1127 CB TRP B 207 61.681 54.027 224.904 1.00 39.72 C ANISOU 1127 CB TRP B 207 3154 4543 7395 -690 552 -436 C ATOM 1128 CG TRP B 207 61.439 52.697 225.560 1.00 42.04 C ANISOU 1128 CG TRP B 207 3470 5032 7473 -677 529 -346 C ATOM 1129 CD1 TRP B 207 62.176 52.127 226.559 1.00 30.05 C ANISOU 1129 CD1 TRP B 207 1972 3702 5744 -734 456 -366 C ATOM 1130 CD2 TRP B 207 60.399 51.762 225.246 1.00 38.58 C ANISOU 1130 CD2 TRP B 207 3032 4606 7020 -611 563 -202 C ATOM 1131 NE1 TRP B 207 61.651 50.902 226.893 1.00 29.68 N ANISOU 1131 NE1 TRP B 207 1947 3773 5557 -708 446 -225 N ATOM 1132 CE2 TRP B 207 60.562 50.653 226.101 1.00 33.07 C ANISOU 1132 CE2 TRP B 207 2361 4093 6110 -638 517 -131 C ATOM 1133 CE3 TRP B 207 59.344 51.757 224.327 1.00 27.55 C ANISOU 1133 CE3 TRP B 207 1684 3088 5698 -514 592 -116 C ATOM 1134 CZ2 TRP B 207 59.709 49.551 226.064 1.00 38.15 C ANISOU 1134 CZ2 TRP B 207 3009 4779 6706 -603 535 17 C ATOM 1135 CZ3 TRP B 207 58.499 50.661 224.293 1.00 26.96 C ANISOU 1135 CZ3 TRP B 207 1629 3072 5543 -473 596 6 C ATOM 1136 CH2 TRP B 207 58.685 49.574 225.157 1.00 27.23 C ANISOU 1136 CH2 TRP B 207 1624 3269 5453 -530 584 71 C ATOM 1137 N CYS B 208 59.212 55.875 225.567 1.00 47.18 N ANISOU 1137 N CYS B 208 4066 5259 8602 -601 799 -744 N ATOM 1138 CA CYS B 208 57.799 56.006 225.892 1.00 43.47 C ANISOU 1138 CA CYS B 208 3555 4767 8193 -529 919 -820 C ATOM 1139 C CYS B 208 56.958 55.246 224.873 1.00 36.52 C ANISOU 1139 C CYS B 208 2645 3839 7391 -447 904 -592 C ATOM 1140 O CYS B 208 57.295 55.185 223.687 1.00 40.53 O ANISOU 1140 O CYS B 208 3229 4238 7931 -406 794 -416 O ATOM 1141 CB CYS B 208 57.371 57.481 225.937 1.00 43.11 C ANISOU 1141 CB CYS B 208 3470 4504 8407 -496 988 -1027 C ATOM 1142 SG CYS B 208 57.876 58.337 227.447 1.00 58.13 S ANISOU 1142 SG CYS B 208 5392 6492 10201 -585 1052 -1390 S ATOM 1143 N PHE B 209 55.857 54.665 225.345 1.00 38.57 N ANISOU 1143 N PHE B 209 2871 4199 7586 -409 990 -595 N ATOM 1144 CA PHE B 209 54.977 53.884 224.488 1.00 40.15 C ANISOU 1144 CA PHE B 209 3127 4369 7758 -323 933 -391 C ATOM 1145 C PHE B 209 53.575 53.881 225.090 1.00 41.27 C ANISOU 1145 C PHE B 209 3195 4552 7935 -282 1063 -481 C ATOM 1146 O PHE B 209 53.310 54.531 226.105 1.00 40.67 O ANISOU 1146 O PHE B 209 3030 4524 7897 -307 1208 -711 O ATOM 1147 CB PHE B 209 55.528 52.465 224.301 1.00 37.26 C ANISOU 1147 CB PHE B 209 2840 4149 7168 -353 835 -201 C ATOM 1148 CG PHE B 209 54.928 51.724 223.138 1.00 34.02 C ANISOU 1148 CG PHE B 209 2503 3677 6745 -278 743 -17 C ATOM 1149 CD1 PHE B 209 54.931 52.279 221.869 1.00 27.83 C ANISOU 1149 CD1 PHE B 209 1762 2725 6087 -219 667 51 C ATOM 1150 CD2 PHE B 209 54.375 50.465 223.313 1.00 27.22 C ANISOU 1150 CD2 PHE B 209 1657 2929 5756 -282 734 86 C ATOM 1151 CE1 PHE B 209 54.381 51.598 220.798 1.00 26.14 C ANISOU 1151 CE1 PHE B 209 1602 2475 5854 -166 587 194 C ATOM 1152 CE2 PHE B 209 53.827 49.779 222.246 1.00 26.21 C ANISOU 1152 CE2 PHE B 209 1587 2739 5630 -225 648 216 C ATOM 1153 CZ PHE B 209 53.830 50.347 220.986 1.00 25.66 C ANISOU 1153 CZ PHE B 209 1559 2522 5670 -168 576 259 C ATOM 1154 N ILE B 210 52.671 53.141 224.442 1.00 44.94 N ANISOU 1154 N ILE B 210 3693 5006 8378 -224 1013 -322 N ATOM 1155 CA ILE B 210 51.284 53.071 224.888 1.00 44.42 C ANISOU 1155 CA ILE B 210 3552 4978 8347 -188 1120 -383 C ATOM 1156 C ILE B 210 51.211 52.411 226.256 1.00 45.38 C ANISOU 1156 C ILE B 210 3628 5351 8264 -278 1258 -455 C ATOM 1157 O ILE B 210 51.795 51.344 226.485 1.00 45.76 O ANISOU 1157 O ILE B 210 3722 5541 8124 -352 1213 -320 O ATOM 1158 CB ILE B 210 50.433 52.314 223.856 1.00 33.99 C ANISOU 1158 CB ILE B 210 2272 3604 7039 -132 1016 -193 C ATOM 1159 CG1 ILE B 210 50.468 53.033 222.506 1.00 32.40 C ANISOU 1159 CG1 ILE B 210 2105 3176 7029 -62 894 -118 C ATOM 1160 CG2 ILE B 210 49.002 52.154 224.349 1.00 34.90 C ANISOU 1160 CG2 ILE B 210 2296 3777 7186 -110 1122 -250 C ATOM 1161 CD1 ILE B 210 49.709 52.314 221.411 1.00 30.49 C ANISOU 1161 CD1 ILE B 210 1900 2895 6791 -22 785 51 C ATOM 1162 N SER B 211 50.486 53.045 227.174 1.00 35.70 N ANISOU 1162 N SER B 211 2307 4182 7076 -278 1433 -671 N ATOM 1163 CA SER B 211 50.313 52.488 228.507 1.00 43.76 C ANISOU 1163 CA SER B 211 3281 5472 7871 -380 1599 -751 C ATOM 1164 C SER B 211 49.335 51.319 228.470 1.00 51.07 C ANISOU 1164 C SER B 211 4200 6502 8702 -394 1606 -562 C ATOM 1165 O SER B 211 48.291 51.379 227.814 1.00 37.13 O ANISOU 1165 O SER B 211 2406 4622 7081 -309 1573 -520 O ATOM 1166 CB SER B 211 49.815 53.563 229.471 1.00 46.34 C ANISOU 1166 CB SER B 211 3520 5845 8242 -374 1798 -1079 C ATOM 1167 OG SER B 211 49.740 53.065 230.795 1.00 59.29 O ANISOU 1167 OG SER B 211 5137 7792 9600 -498 1976 -1173 O ATOM 1168 N THR B 212 49.680 50.247 229.187 1.00 58.62 N ANISOU 1168 N THR B 212 5174 7672 9427 -517 1645 -445 N ATOM 1169 CA THR B 212 48.905 49.012 229.174 1.00 61.18 C ANISOU 1169 CA THR B 212 5494 8086 9667 -558 1639 -239 C ATOM 1170 C THR B 212 48.362 48.658 230.554 1.00 58.91 C ANISOU 1170 C THR B 212 5143 8070 9170 -684 1862 -293 C ATOM 1171 O THR B 212 47.995 47.503 230.796 1.00 61.42 O ANISOU 1171 O THR B 212 5463 8501 9372 -772 1871 -91 O ATOM 1172 CB THR B 212 49.747 47.858 228.624 1.00 61.92 C ANISOU 1172 CB THR B 212 5678 8153 9696 -597 1459 13 C ATOM 1173 OG1 THR B 212 49.008 46.634 228.716 1.00 72.62 O ANISOU 1173 OG1 THR B 212 7028 9584 10980 -657 1459 193 O ATOM 1174 CG2 THR B 212 51.042 47.720 229.410 1.00 59.62 C ANISOU 1174 CG2 THR B 212 5418 7990 9244 -704 1470 17 C ATOM 1175 N GLY B 213 48.302 49.625 231.464 1.00 59.25 N ANISOU 1175 N GLY B 213 5141 8224 9147 -704 2042 -569 N ATOM 1176 CA GLY B 213 47.780 49.385 232.797 1.00 71.63 C ANISOU 1176 CA GLY B 213 6675 10088 10454 -831 2269 -654 C ATOM 1177 C GLY B 213 48.832 49.483 233.884 1.00 81.90 C ANISOU 1177 C GLY B 213 8094 11616 11407 -957 2292 -746 C ATOM 1178 O GLY B 213 48.722 50.306 234.793 1.00 89.66 O ANISOU 1178 O GLY B 213 9065 12752 12251 -987 2453 -1034 O ATOM 1179 N GLY B 226 40.284 55.630 228.772 1.00 55.92 N ANISOU 1179 N GLY B 226 3975 6665 10608 175 2180 -1502 N ATOM 1180 CA GLY B 226 40.283 54.330 228.128 1.00 52.97 C ANISOU 1180 CA GLY B 226 3661 6364 10100 119 2057 -1203 C ATOM 1181 C GLY B 226 41.658 53.895 227.658 1.00 66.69 C ANISOU 1181 C GLY B 226 5570 8069 11699 68 1916 -1038 C ATOM 1182 O GLY B 226 41.903 53.767 226.458 1.00 73.89 O ANISOU 1182 O GLY B 226 6554 8808 12712 107 1715 -858 O ATOM 1183 N ASN B 227 42.561 53.669 228.614 1.00 61.17 N ANISOU 1183 N ASN B 227 4681 9007 9553 -363 1333 -634 N ATOM 1184 CA ASN B 227 43.919 53.261 228.270 1.00 58.28 C ANISOU 1184 CA ASN B 227 4493 8547 9105 -428 1175 -533 C ATOM 1185 C ASN B 227 43.956 51.829 227.751 1.00 56.01 C ANISOU 1185 C ASN B 227 4295 8371 8615 -540 1006 -202 C ATOM 1186 O ASN B 227 44.707 51.520 226.818 1.00 58.39 O ANISOU 1186 O ASN B 227 4733 8575 8875 -532 825 -66 O ATOM 1187 CB ASN B 227 44.835 53.418 229.482 1.00 65.78 C ANISOU 1187 CB ASN B 227 5485 9567 9940 -552 1278 -791 C ATOM 1188 CG ASN B 227 44.980 54.862 229.919 1.00 68.12 C ANISOU 1188 CG ASN B 227 5712 9727 10444 -455 1427 -1150 C ATOM 1189 OD1 ASN B 227 44.105 55.690 229.666 1.00 76.19 O ANISOU 1189 OD1 ASN B 227 6618 10641 11691 -307 1509 -1236 O ATOM 1190 ND2 ASN B 227 46.088 55.172 230.582 1.00 59.38 N ANISOU 1190 ND2 ASN B 227 4670 8619 9272 -544 1456 -1367 N ATOM 1191 N LEU B 228 43.155 50.939 228.343 1.00 60.21 N ANISOU 1191 N LEU B 228 4766 9079 9032 -651 1072 -101 N ATOM 1192 CA LEU B 228 43.154 49.546 227.909 1.00 51.78 C ANISOU 1192 CA LEU B 228 3803 7967 7905 -746 930 196 C ATOM 1193 C LEU B 228 42.469 49.372 226.559 1.00 46.39 C ANISOU 1193 C LEU B 228 3189 7421 7018 -707 754 248 C ATOM 1194 O LEU B 228 42.830 48.468 225.798 1.00 33.39 O ANISOU 1194 O LEU B 228 1732 5551 5404 -802 700 -39 O ATOM 1195 CB LEU B 228 42.487 48.666 228.966 1.00 44.38 C ANISOU 1195 CB LEU B 228 2846 7155 6861 -916 1070 110 C ATOM 1196 CG LEU B 228 43.223 48.598 230.305 1.00 39.67 C ANISOU 1196 CG LEU B 228 2327 6790 5957 -1083 1142 -87 C ATOM 1197 CD1 LEU B 228 42.509 47.667 231.268 1.00 41.70 C ANISOU 1197 CD1 LEU B 228 2598 7317 5928 -1281 1217 -80 C ATOM 1198 CD2 LEU B 228 44.664 48.159 230.095 1.00 37.30 C ANISOU 1198 CD2 LEU B 228 2207 6387 5577 -1134 969 -20 C ATOM 1199 N PHE B 229 41.485 50.217 226.245 1.00 37.21 N ANISOU 1199 N PHE B 229 1837 6289 6010 -591 844 156 N ATOM 1200 CA PHE B 229 40.859 50.154 224.928 1.00 42.35 C ANISOU 1200 CA PHE B 229 2498 6872 6722 -545 753 84 C ATOM 1201 C PHE B 229 41.830 50.599 223.842 1.00 37.97 C ANISOU 1201 C PHE B 229 2105 6014 6306 -431 624 124 C ATOM 1202 O PHE B 229 41.957 49.944 222.801 1.00 33.71 O ANISOU 1202 O PHE B 229 1720 5333 5755 -439 496 207 O ATOM 1203 CB PHE B 229 39.594 51.013 224.897 1.00 39.10 C ANISOU 1203 CB PHE B 229 1847 6527 6481 -411 855 75 C ATOM 1204 CG PHE B 229 39.105 51.310 223.506 1.00 38.58 C ANISOU 1204 CG PHE B 229 1811 6261 6585 -295 744 108 C ATOM 1205 CD1 PHE B 229 38.442 50.343 222.770 1.00 37.91 C ANISOU 1205 CD1 PHE B 229 1767 6197 6439 -381 661 154 C ATOM 1206 CD2 PHE B 229 39.323 52.551 222.928 1.00 38.97 C ANISOU 1206 CD2 PHE B 229 1859 6052 6897 -109 728 114 C ATOM 1207 CE1 PHE B 229 37.998 50.608 221.488 1.00 40.66 C ANISOU 1207 CE1 PHE B 229 2140 6375 6936 -274 554 268 C ATOM 1208 CE2 PHE B 229 38.882 52.822 221.646 1.00 38.76 C ANISOU 1208 CE2 PHE B 229 1855 5857 7014 -19 618 221 C ATOM 1209 CZ PHE B 229 38.218 51.850 220.925 1.00 38.10 C ANISOU 1209 CZ PHE B 229 1800 5849 6826 -100 529 314 C ATOM 1210 N PHE B 230 42.520 51.719 224.068 1.00 34.50 N ANISOU 1210 N PHE B 230 1658 5421 6028 -316 665 78 N ATOM 1211 CA PHE B 230 43.456 52.229 223.072 1.00 34.49 C ANISOU 1211 CA PHE B 230 1816 5133 6156 -222 550 127 C ATOM 1212 C PHE B 230 44.626 51.273 222.875 1.00 31.54 C ANISOU 1212 C PHE B 230 1646 4737 5600 -323 436 187 C ATOM 1213 O PHE B 230 45.117 51.107 221.751 1.00 28.21 O ANISOU 1213 O PHE B 230 1381 4141 5197 -281 316 291 O ATOM 1214 CB PHE B 230 43.950 53.614 223.483 1.00 33.98 C ANISOU 1214 CB PHE B 230 1695 4883 6332 -111 640 -3 C ATOM 1215 CG PHE B 230 44.917 54.221 222.513 1.00 32.46 C ANISOU 1215 CG PHE B 230 1647 4406 6280 -39 532 58 C ATOM 1216 CD1 PHE B 230 44.478 54.713 221.295 1.00 32.52 C ANISOU 1216 CD1 PHE B 230 1670 4240 6447 54 457 179 C ATOM 1217 CD2 PHE B 230 46.266 54.306 222.819 1.00 45.35 C ANISOU 1217 CD2 PHE B 230 3388 5959 7884 -80 507 8 C ATOM 1218 CE1 PHE B 230 45.366 55.274 220.399 1.00 48.58 C ANISOU 1218 CE1 PHE B 230 3828 6032 8599 93 369 263 C ATOM 1219 CE2 PHE B 230 47.160 54.867 221.925 1.00 33.86 C ANISOU 1219 CE2 PHE B 230 2053 4262 6552 -28 417 73 C ATOM 1220 CZ PHE B 230 46.709 55.352 220.714 1.00 43.06 C ANISOU 1220 CZ PHE B 230 3235 5261 7866 53 352 207 C ATOM 1221 N ALA B 231 45.088 50.638 223.954 1.00 30.03 N ANISOU 1221 N ALA B 231 1452 4721 5237 -459 478 134 N ATOM 1222 CA ALA B 231 46.148 49.645 223.822 1.00 34.37 C ANISOU 1222 CA ALA B 231 2187 5227 5646 -550 374 171 C ATOM 1223 C ALA B 231 45.656 48.400 223.097 1.00 38.19 C ANISOU 1223 C ALA B 231 2782 5660 6068 -591 296 262 C ATOM 1224 O ALA B 231 46.454 47.687 222.478 1.00 44.25 O ANISOU 1224 O ALA B 231 3730 6296 6788 -582 182 360 O ATOM 1225 CB ALA B 231 46.703 49.280 225.199 1.00 28.58 C ANISOU 1225 CB ALA B 231 1409 4678 4772 -704 440 92 C ATOM 1226 N SER B 232 44.352 48.120 223.162 1.00 33.36 N ANISOU 1226 N SER B 232 2058 5149 5467 -626 356 251 N ATOM 1227 CA SER B 232 43.793 46.973 222.456 1.00 29.84 C ANISOU 1227 CA SER B 232 1708 4643 4987 -657 277 378 C ATOM 1228 C SER B 232 43.511 47.287 220.993 1.00 32.07 C ANISOU 1228 C SER B 232 2032 4794 5358 -537 178 514 C ATOM 1229 O SER B 232 43.625 46.398 220.141 1.00 33.78 O ANISOU 1229 O SER B 232 2375 4922 5537 -544 68 675 O ATOM 1230 CB SER B 232 42.511 46.504 223.144 1.00 39.58 C ANISOU 1230 CB SER B 232 2797 6017 6224 -757 385 336 C ATOM 1231 OG SER B 232 42.762 46.115 224.483 1.00 46.85 O ANISOU 1231 OG SER B 232 3688 7002 7109 -876 485 287 O ATOM 1232 N ALA B 233 43.140 48.532 220.685 1.00 36.15 N ANISOU 1232 N ALA B 233 2436 5289 6010 -430 214 481 N ATOM 1233 CA ALA B 233 42.909 48.917 219.297 1.00 27.67 C ANISOU 1233 CA ALA B 233 1395 4052 5065 -329 125 639 C ATOM 1234 C ALA B 233 44.189 48.863 218.473 1.00 37.40 C ANISOU 1234 C ALA B 233 2817 5103 6291 -294 24 743 C ATOM 1235 O ALA B 233 44.144 48.533 217.282 1.00 25.11 O ANISOU 1235 O ALA B 233 1341 3452 4748 -277 -68 900 O ATOM 1236 CB ALA B 233 42.298 50.316 219.236 1.00 29.44 C ANISOU 1236 CB ALA B 233 1460 4249 5476 -217 188 591 C ATOM 1237 N PHE B 234 45.333 49.183 219.083 1.00 32.05 N ANISOU 1237 N PHE B 234 2199 4395 5583 -292 43 652 N ATOM 1238 CA PHE B 234 46.601 49.110 218.363 1.00 33.24 C ANISOU 1238 CA PHE B 234 2513 4391 5724 -265 -42 733 C ATOM 1239 C PHE B 234 46.978 47.667 218.051 1.00 39.50 C ANISOU 1239 C PHE B 234 3441 5196 6370 -328 -125 826 C ATOM 1240 O PHE B 234 47.466 47.372 216.953 1.00 37.38 O ANISOU 1240 O PHE B 234 3281 4824 6097 -305 -206 946 O ATOM 1241 CB PHE B 234 47.703 49.793 219.177 1.00 26.00 C ANISOU 1241 CB PHE B 234 1608 3459 4813 -257 -1 604 C ATOM 1242 CG PHE B 234 49.085 49.615 218.606 1.00 23.89 C ANISOU 1242 CG PHE B 234 1494 3064 4519 -243 -80 664 C ATOM 1243 CD1 PHE B 234 49.568 50.486 217.642 1.00 27.32 C ANISOU 1243 CD1 PHE B 234 1968 3330 5081 -178 -110 733 C ATOM 1244 CD2 PHE B 234 49.907 48.583 219.042 1.00 27.61 C ANISOU 1244 CD2 PHE B 234 2059 3586 4844 -302 -121 655 C ATOM 1245 CE1 PHE B 234 50.842 50.326 217.115 1.00 33.54 C ANISOU 1245 CE1 PHE B 234 2880 4029 5837 -175 -169 777 C ATOM 1246 CE2 PHE B 234 51.179 48.417 218.518 1.00 18.83 C ANISOU 1246 CE2 PHE B 234 1069 2373 3715 -280 -186 701 C ATOM 1247 CZ PHE B 234 51.647 49.290 217.555 1.00 19.26 C ANISOU 1247 CZ PHE B 234 1153 2283 3881 -219 -204 753 C ATOM 1248 N ALA B 235 46.759 46.756 219.002 1.00 39.31 N ANISOU 1248 N ALA B 235 3405 5301 6232 -416 -101 774 N ATOM 1249 CA ALA B 235 47.175 45.370 218.813 1.00 25.27 C ANISOU 1249 CA ALA B 235 1753 3512 4335 -471 -186 869 C ATOM 1250 C ALA B 235 46.366 44.686 217.717 1.00 28.54 C ANISOU 1250 C ALA B 235 2189 3908 4744 -477 -253 1007 C ATOM 1251 O ALA B 235 46.927 43.966 216.883 1.00 20.27 O ANISOU 1251 O ALA B 235 1259 2791 3654 -474 -339 1099 O ATOM 1252 CB ALA B 235 47.056 44.602 220.129 1.00 21.57 C ANISOU 1252 CB ALA B 235 1263 3168 3765 -579 -147 807 C ATOM 1253 N PHE B 236 45.047 44.900 217.699 1.00 27.81 N ANISOU 1253 N PHE B 236 1974 3895 4698 -493 -209 1009 N ATOM 1254 CA PHE B 236 44.220 44.274 216.671 1.00 26.26 C ANISOU 1254 CA PHE B 236 1782 3704 4493 -514 -276 1136 C ATOM 1255 C PHE B 236 44.479 44.871 215.293 1.00 27.74 C ANISOU 1255 C PHE B 236 2011 3782 4749 -443 -331 1229 C ATOM 1256 O PHE B 236 44.354 44.166 214.284 1.00 22.38 O ANISOU 1256 O PHE B 236 1391 3091 4022 -472 -408 1332 O ATOM 1257 CB PHE B 236 42.739 44.391 217.033 1.00 34.95 C ANISOU 1257 CB PHE B 236 2719 4928 5633 -553 -213 1113 C ATOM 1258 CG PHE B 236 42.279 43.373 218.040 1.00 47.46 C ANISOU 1258 CG PHE B 236 4283 6629 7121 -669 -181 1082 C ATOM 1259 CD1 PHE B 236 42.121 42.045 217.675 1.00 48.04 C ANISOU 1259 CD1 PHE B 236 4443 6710 7101 -749 -268 1189 C ATOM 1260 CD2 PHE B 236 41.996 43.743 219.345 1.00 47.15 C ANISOU 1260 CD2 PHE B 236 4134 6694 7086 -712 -60 944 C ATOM 1261 CE1 PHE B 236 41.698 41.102 218.595 1.00 40.72 C ANISOU 1261 CE1 PHE B 236 3505 5874 6091 -869 -247 1190 C ATOM 1262 CE2 PHE B 236 41.570 42.804 220.270 1.00 37.24 C ANISOU 1262 CE2 PHE B 236 2867 5542 5742 -840 -23 940 C ATOM 1263 CZ PHE B 236 41.422 41.482 219.893 1.00 37.66 C ANISOU 1263 CZ PHE B 236 3020 5587 5704 -917 -124 1079 C ATOM 1264 N LEU B 237 44.831 46.159 215.224 1.00 29.55 N ANISOU 1264 N LEU B 237 2203 3936 5090 -365 -291 1193 N ATOM 1265 CA LEU B 237 45.208 46.748 213.942 1.00 26.47 C ANISOU 1265 CA LEU B 237 1860 3435 4762 -321 -341 1298 C ATOM 1266 C LEU B 237 46.457 46.084 213.379 1.00 26.43 C ANISOU 1266 C LEU B 237 2011 3369 4663 -337 -402 1329 C ATOM 1267 O LEU B 237 46.545 45.833 212.172 1.00 33.40 O ANISOU 1267 O LEU B 237 2942 4231 5517 -354 -461 1429 O ATOM 1268 CB LEU B 237 45.425 48.254 214.088 1.00 25.56 C ANISOU 1268 CB LEU B 237 1678 3231 4802 -246 -287 1255 C ATOM 1269 CG LEU B 237 44.184 49.149 214.043 1.00 34.09 C ANISOU 1269 CG LEU B 237 2592 4330 6032 -205 -248 1271 C ATOM 1270 CD1 LEU B 237 44.566 50.600 214.292 1.00 34.45 C ANISOU 1270 CD1 LEU B 237 2581 4260 6250 -130 -195 1214 C ATOM 1271 CD2 LEU B 237 43.468 49.003 212.709 1.00 25.54 C ANISOU 1271 CD2 LEU B 237 1492 3248 4963 -225 -322 1446 C ATOM 1272 N GLY B 238 47.436 45.797 214.239 1.00 26.03 N ANISOU 1272 N GLY B 238 2023 3305 4561 -336 -386 1237 N ATOM 1273 CA GLY B 238 48.623 45.092 213.783 1.00 19.49 C ANISOU 1273 CA GLY B 238 1322 2426 3657 -346 -439 1252 C ATOM 1274 C GLY B 238 48.316 43.679 213.326 1.00 24.09 C ANISOU 1274 C GLY B 238 1953 3058 4141 -407 -503 1305 C ATOM 1275 O GLY B 238 48.790 43.236 212.276 1.00 28.77 O ANISOU 1275 O GLY B 238 2610 3623 4699 -420 -551 1347 O ATOM 1276 N LEU B 239 47.516 42.950 214.112 1.00 19.11 N ANISOU 1276 N LEU B 239 1284 2509 3468 -458 -500 1294 N ATOM 1277 CA LEU B 239 47.100 41.610 213.707 1.00 28.04 C ANISOU 1277 CA LEU B 239 2450 3679 4525 -529 -566 1345 C ATOM 1278 C LEU B 239 46.295 41.643 212.415 1.00 25.86 C ANISOU 1278 C LEU B 239 2140 3429 4254 -550 -600 1425 C ATOM 1279 O LEU B 239 46.344 40.692 211.628 1.00 22.65 O ANISOU 1279 O LEU B 239 1783 3030 3792 -602 -663 1451 O ATOM 1280 CB LEU B 239 46.288 40.947 214.821 1.00 29.26 C ANISOU 1280 CB LEU B 239 2555 3924 4641 -599 -551 1332 C ATOM 1281 CG LEU B 239 46.976 40.783 216.179 1.00 30.70 C ANISOU 1281 CG LEU B 239 2760 4114 4791 -612 -523 1267 C ATOM 1282 CD1 LEU B 239 46.018 40.179 217.192 1.00 25.97 C ANISOU 1282 CD1 LEU B 239 2098 3626 4144 -709 -498 1270 C ATOM 1283 CD2 LEU B 239 48.232 39.935 216.054 1.00 18.84 C ANISOU 1283 CD2 LEU B 239 1375 2529 3254 -608 -594 1277 C ATOM 1284 N LEU B 240 45.545 42.723 212.184 1.00 22.56 N ANISOU 1284 N LEU B 240 1630 3031 3912 -518 -564 1459 N ATOM 1285 CA LEU B 240 44.825 42.866 210.924 1.00 28.79 C ANISOU 1285 CA LEU B 240 2378 3854 4708 -542 -605 1556 C ATOM 1286 C LEU B 240 45.789 43.036 209.756 1.00 32.71 C ANISOU 1286 C LEU B 240 2952 4297 5181 -533 -640 1588 C ATOM 1287 O LEU B 240 45.581 42.459 208.682 1.00 29.61 O ANISOU 1287 O LEU B 240 2571 3956 4723 -594 -696 1635 O ATOM 1288 CB LEU B 240 43.863 44.051 211.001 1.00 26.51 C ANISOU 1288 CB LEU B 240 1956 3583 4532 -501 -562 1594 C ATOM 1289 CG LEU B 240 43.047 44.346 209.740 1.00 25.06 C ANISOU 1289 CG LEU B 240 1707 3443 4371 -528 -611 1719 C ATOM 1290 CD1 LEU B 240 42.060 43.222 209.459 1.00 25.08 C ANISOU 1290 CD1 LEU B 240 1677 3559 4292 -620 -662 1752 C ATOM 1291 CD2 LEU B 240 42.330 45.682 209.856 1.00 30.71 C ANISOU 1291 CD2 LEU B 240 2289 4140 5241 -465 -568 1758 C ATOM 1292 N ALA B 241 46.850 43.826 209.948 1.00 34.57 N ANISOU 1292 N ALA B 241 3228 4445 5461 -471 -605 1551 N ATOM 1293 CA ALA B 241 47.802 44.065 208.867 1.00 29.99 C ANISOU 1293 CA ALA B 241 2704 3833 4858 -472 -627 1577 C ATOM 1294 C ALA B 241 48.564 42.797 208.506 1.00 25.92 C ANISOU 1294 C ALA B 241 2269 3336 4242 -515 -666 1514 C ATOM 1295 O ALA B 241 48.833 42.543 207.326 1.00 19.21 O ANISOU 1295 O ALA B 241 1431 2531 3335 -557 -700 1531 O ATOM 1296 CB ALA B 241 48.769 45.182 209.259 1.00 27.12 C ANISOU 1296 CB ALA B 241 2357 3373 4575 -405 -579 1545 C ATOM 1297 N LEU B 242 48.916 41.984 209.505 1.00 22.29 N ANISOU 1297 N LEU B 242 1852 2850 3767 -510 -662 1435 N ATOM 1298 CA LEU B 242 49.565 40.711 209.217 1.00 25.29 C ANISOU 1298 CA LEU B 242 2293 3227 4089 -551 -704 1371 C ATOM 1299 C LEU B 242 48.604 39.725 208.566 1.00 30.26 C ANISOU 1299 C LEU B 242 2901 3933 4666 -638 -759 1393 C ATOM 1300 O LEU B 242 49.029 38.887 207.763 1.00 42.86 O ANISOU 1300 O LEU B 242 4522 5543 6220 -687 -796 1335 O ATOM 1301 CB LEU B 242 50.154 40.115 210.495 1.00 32.18 C ANISOU 1301 CB LEU B 242 3209 4043 4975 -530 -699 1311 C ATOM 1302 CG LEU B 242 51.281 40.913 211.154 1.00 29.87 C ANISOU 1302 CG LEU B 242 2942 3683 4724 -461 -654 1265 C ATOM 1303 CD1 LEU B 242 51.907 40.117 212.292 1.00 22.43 C ANISOU 1303 CD1 LEU B 242 2040 2703 3779 -461 -671 1220 C ATOM 1304 CD2 LEU B 242 52.329 41.314 210.125 1.00 20.10 C ANISOU 1304 CD2 LEU B 242 1726 2422 3491 -442 -647 1236 C ATOM 1305 N THR B 243 47.313 39.803 208.899 1.00 29.41 N ANISOU 1305 N THR B 243 2732 3880 4564 -666 -761 1458 N ATOM 1306 CA THR B 243 46.342 38.890 208.305 1.00 26.96 C ANISOU 1306 CA THR B 243 2393 3648 4204 -763 -816 1480 C ATOM 1307 C THR B 243 46.132 39.192 206.826 1.00 31.89 C ANISOU 1307 C THR B 243 2986 4344 4786 -805 -844 1521 C ATOM 1308 O THR B 243 46.094 38.273 205.998 1.00 32.97 O ANISOU 1308 O THR B 243 3135 4529 4864 -890 -892 1474 O ATOM 1309 CB THR B 243 45.014 38.965 209.060 1.00 31.28 C ANISOU 1309 CB THR B 243 2863 4252 4771 -787 -805 1537 C ATOM 1310 OG1 THR B 243 45.239 38.721 210.453 1.00 36.92 O ANISOU 1310 OG1 THR B 243 3596 4927 5504 -764 -775 1498 O ATOM 1311 CG2 THR B 243 44.036 37.930 208.524 1.00 30.67 C ANISOU 1311 CG2 THR B 243 2757 4253 4644 -903 -865 1556 C ATOM 1312 N VAL B 244 45.988 40.472 206.475 1.00 30.24 N ANISOU 1312 N VAL B 244 2732 4147 4612 -757 -819 1605 N ATOM 1313 CA VAL B 244 45.845 40.849 205.071 1.00 30.95 C ANISOU 1313 CA VAL B 244 2787 4320 4652 -806 -853 1673 C ATOM 1314 C VAL B 244 47.102 40.487 204.290 1.00 40.46 C ANISOU 1314 C VAL B 244 4050 5528 5794 -824 -859 1582 C ATOM 1315 O VAL B 244 47.028 39.994 203.157 1.00 43.17 O ANISOU 1315 O VAL B 244 4378 5973 6052 -912 -902 1562 O ATOM 1316 CB VAL B 244 45.516 42.349 204.949 1.00 23.13 C ANISOU 1316 CB VAL B 244 1732 3315 3740 -750 -827 1800 C ATOM 1317 CG1 VAL B 244 45.413 42.755 203.487 1.00 24.20 C ANISOU 1317 CG1 VAL B 244 1830 3549 3817 -813 -871 1900 C ATOM 1318 CG2 VAL B 244 44.226 42.667 205.680 1.00 24.03 C ANISOU 1318 CG2 VAL B 244 1757 3440 3933 -733 -815 1859 C ATOM 1319 N THR B 245 48.276 40.718 204.885 1.00 32.01 N ANISOU 1319 N THR B 245 3036 4363 4765 -748 -815 1512 N ATOM 1320 CA THR B 245 49.528 40.443 204.186 1.00 33.32 C ANISOU 1320 CA THR B 245 3234 4542 4886 -758 -812 1411 C ATOM 1321 C THR B 245 49.731 38.948 203.973 1.00 26.99 C ANISOU 1321 C THR B 245 2452 3757 4046 -825 -846 1268 C ATOM 1322 O THR B 245 50.157 38.524 202.892 1.00 29.93 O ANISOU 1322 O THR B 245 2805 4210 4355 -889 -864 1181 O ATOM 1323 CB THR B 245 50.704 41.041 204.959 1.00 37.41 C ANISOU 1323 CB THR B 245 3792 4953 5468 -664 -759 1370 C ATOM 1324 OG1 THR B 245 50.532 42.460 205.072 1.00 42.99 O ANISOU 1324 OG1 THR B 245 4474 5630 6229 -615 -731 1487 O ATOM 1325 CG2 THR B 245 52.016 40.755 204.246 1.00 36.42 C ANISOU 1325 CG2 THR B 245 3677 4857 5304 -673 -752 1255 C ATOM 1326 N PHE B 246 49.424 38.132 204.983 1.00 20.40 N ANISOU 1326 N PHE B 246 1647 2848 3255 -821 -856 1236 N ATOM 1327 CA PHE B 246 49.632 36.693 204.847 1.00 20.83 C ANISOU 1327 CA PHE B 246 1722 2884 3307 -889 -893 1104 C ATOM 1328 C PHE B 246 48.600 36.072 203.913 1.00 34.10 C ANISOU 1328 C PHE B 246 3363 4667 4925 -1011 -945 1098 C ATOM 1329 O PHE B 246 48.913 35.135 203.169 1.00 24.74 O ANISOU 1329 O PHE B 246 2173 3504 3721 -1091 -973 955 O ATOM 1330 CB PHE B 246 49.585 36.010 206.215 1.00 20.39 C ANISOU 1330 CB PHE B 246 1712 2719 3318 -863 -902 1103 C ATOM 1331 CG PHE B 246 50.740 36.356 207.122 1.00 35.55 C ANISOU 1331 CG PHE B 246 3672 4541 5295 -762 -867 1082 C ATOM 1332 CD1 PHE B 246 51.711 37.269 206.735 1.00 34.25 C ANISOU 1332 CD1 PHE B 246 3502 4381 5130 -700 -823 1059 C ATOM 1333 CD2 PHE B 246 50.863 35.746 208.359 1.00 35.89 C ANISOU 1333 CD2 PHE B 246 3753 4495 5386 -743 -885 1091 C ATOM 1334 CE1 PHE B 246 52.766 37.579 207.573 1.00 27.51 C ANISOU 1334 CE1 PHE B 246 2682 3442 4330 -619 -793 1035 C ATOM 1335 CE2 PHE B 246 51.918 36.047 209.198 1.00 35.75 C ANISOU 1335 CE2 PHE B 246 3769 4400 5416 -662 -862 1076 C ATOM 1336 CZ PHE B 246 52.871 36.965 208.805 1.00 36.46 C ANISOU 1336 CZ PHE B 246 3852 4490 5510 -600 -814 1042 C ATOM 1337 N SER B 247 47.366 36.583 203.935 1.00 32.76 N ANISOU 1337 N SER B 247 3152 4562 4732 -1034 -958 1238 N ATOM 1338 CA SER B 247 46.314 36.012 203.100 1.00 31.14 C ANISOU 1338 CA SER B 247 2903 4464 4466 -1158 -1014 1246 C ATOM 1339 C SER B 247 46.559 36.292 201.623 1.00 26.03 C ANISOU 1339 C SER B 247 2220 3943 3728 -1219 -1034 1220 C ATOM 1340 O SER B 247 46.336 35.419 200.776 1.00 30.82 O ANISOU 1340 O SER B 247 2810 4621 4280 -1336 -1080 1118 O ATOM 1341 CB SER B 247 44.951 36.553 203.531 1.00 30.27 C ANISOU 1341 CB SER B 247 2736 4400 4363 -1160 -1022 1406 C ATOM 1342 OG SER B 247 44.689 36.242 204.888 1.00 34.95 O ANISOU 1342 OG SER B 247 3350 4907 5022 -1122 -1003 1418 O ATOM 1343 N CYS B 248 47.015 37.503 201.293 1.00 25.27 N ANISOU 1343 N CYS B 248 2109 3880 3614 -1154 -1003 1310 N ATOM 1344 CA CYS B 248 47.239 37.844 199.892 1.00 41.19 C ANISOU 1344 CA CYS B 248 4086 6040 5525 -1224 -1026 1316 C ATOM 1345 C CYS B 248 48.482 37.154 199.343 1.00 42.63 C ANISOU 1345 C CYS B 248 4286 6230 5681 -1249 -1013 1104 C ATOM 1346 O CYS B 248 48.508 36.750 198.174 1.00 33.87 O ANISOU 1346 O CYS B 248 3143 5250 4474 -1358 -1048 1022 O ATOM 1347 CB CYS B 248 47.356 39.360 199.731 1.00 47.06 C ANISOU 1347 CB CYS B 248 4804 6805 6270 -1158 -1000 1495 C ATOM 1348 SG CYS B 248 45.853 40.285 200.118 1.00 51.92 S ANISOU 1348 SG CYS B 248 5358 7425 6945 -1137 -1019 1729 S ATOM 1349 N ASN B 249 49.519 37.006 200.170 1.00 38.89 N ANISOU 1349 N ASN B 249 3855 5625 5298 -1156 -965 1005 N ATOM 1350 CA ASN B 249 50.751 36.378 199.702 1.00 40.21 C ANISOU 1350 CA ASN B 249 4014 5791 5472 -1168 -948 789 C ATOM 1351 C ASN B 249 50.541 34.901 199.398 1.00 38.24 C ANISOU 1351 C ASN B 249 3759 5528 5241 -1273 -997 601 C ATOM 1352 O ASN B 249 51.013 34.401 198.370 1.00 41.65 O ANISOU 1352 O ASN B 249 4153 6051 5620 -1375 -1033 466 O ATOM 1353 CB ASN B 249 51.861 36.561 200.738 1.00 49.35 C ANISOU 1353 CB ASN B 249 5208 6812 6732 -1045 -894 743 C ATOM 1354 CG ASN B 249 52.382 37.984 200.788 1.00 47.99 C ANISOU 1354 CG ASN B 249 5034 6655 6545 -965 -849 876 C ATOM 1355 OD1 ASN B 249 51.807 38.890 200.183 1.00 56.50 O ANISOU 1355 OD1 ASN B 249 6089 7826 7553 -992 -860 1033 O ATOM 1356 ND2 ASN B 249 53.477 38.189 201.511 1.00 39.49 N ANISOU 1356 ND2 ASN B 249 3980 5484 5541 -873 -804 820 N ATOM 1357 N LEU B 250 49.835 34.186 200.277 1.00 31.61 N ANISOU 1357 N LEU B 250 2957 4582 4470 -1278 -1014 612 N ATOM 1358 CA LEU B 250 49.568 32.773 200.033 1.00 29.88 C ANISOU 1358 CA LEU B 250 2743 4327 4283 -1405 -1076 464 C ATOM 1359 C LEU B 250 48.688 32.584 198.803 1.00 36.39 C ANISOU 1359 C LEU B 250 3525 5309 4991 -1551 -1138 461 C ATOM 1360 O LEU B 250 48.859 31.619 198.049 1.00 34.81 O ANISOU 1360 O LEU B 250 3317 5129 4780 -1678 -1193 281 O ATOM 1361 CB LEU B 250 48.923 32.141 201.267 1.00 26.70 C ANISOU 1361 CB LEU B 250 2394 3785 3965 -1391 -1082 522 C ATOM 1362 CG LEU B 250 49.817 32.070 202.507 1.00 28.26 C ANISOU 1362 CG LEU B 250 2647 3826 4264 -1279 -1048 528 C ATOM 1363 CD1 LEU B 250 49.025 31.624 203.724 1.00 33.27 C ANISOU 1363 CD1 LEU B 250 3332 4361 4949 -1274 -1063 639 C ATOM 1364 CD2 LEU B 250 50.991 31.138 202.263 1.00 31.23 C ANISOU 1364 CD2 LEU B 250 3033 4112 4722 -1317 -1077 338 C ATOM 1365 N ALA B 251 47.736 33.496 198.587 1.00 38.52 N ANISOU 1365 N ALA B 251 3771 5691 5176 -1542 -1137 654 N ATOM 1366 CA ALA B 251 46.907 33.429 197.389 1.00 43.76 C ANISOU 1366 CA ALA B 251 4390 6535 5703 -1687 -1203 687 C ATOM 1367 C ALA B 251 47.726 33.708 196.134 1.00 56.40 C ANISOU 1367 C ALA B 251 5962 8293 7173 -1757 -1215 622 C ATOM 1368 O ALA B 251 47.512 33.073 195.094 1.00 57.85 O ANISOU 1368 O ALA B 251 6129 8608 7241 -1918 -1275 521 O ATOM 1369 CB ALA B 251 45.743 34.413 197.502 1.00 32.88 C ANISOU 1369 CB ALA B 251 2978 5239 4277 -1664 -1210 939 C ATOM 1370 N THR B 252 48.665 34.654 196.210 1.00 54.54 N ANISOU 1370 N THR B 252 5723 8061 6939 -1652 -1155 676 N ATOM 1371 CA THR B 252 49.490 34.975 195.049 1.00 46.64 C ANISOU 1371 CA THR B 252 4690 7237 5793 -1730 -1156 632 C ATOM 1372 C THR B 252 50.431 33.826 194.705 1.00 48.57 C ANISOU 1372 C THR B 252 4939 7459 6057 -1806 -1170 344 C ATOM 1373 O THR B 252 50.682 33.556 193.525 1.00 55.99 O ANISOU 1373 O THR B 252 5858 8592 6824 -1957 -1194 241 O ATOM 1374 CB THR B 252 50.281 36.259 195.304 1.00 37.56 C ANISOU 1374 CB THR B 252 3534 6078 4659 -1604 -1087 763 C ATOM 1375 OG1 THR B 252 49.381 37.310 195.677 1.00 38.39 O ANISOU 1375 OG1 THR B 252 3641 6169 4778 -1534 -1081 1010 O ATOM 1376 CG2 THR B 252 51.044 36.678 194.055 1.00 31.77 C ANISOU 1376 CG2 THR B 252 2758 5573 3741 -1711 -1082 761 C ATOM 1377 N ILE B 253 50.957 33.138 195.722 1.00 42.06 N ANISOU 1377 N ILE B 253 4142 6408 5431 -1716 -1155 207 N ATOM 1378 CA ILE B 253 51.853 32.011 195.476 1.00 40.82 C ANISOU 1378 CA ILE B 253 3987 6181 5341 -1782 -1183 -77 C ATOM 1379 C ILE B 253 51.115 30.899 194.740 1.00 59.99 C ANISOU 1379 C ILE B 253 6441 8650 7703 -1960 -1264 -224 C ATOM 1380 O ILE B 253 51.618 30.336 193.761 1.00 67.68 O ANISOU 1380 O ILE B 253 7420 9726 8569 -2089 -1286 -433 O ATOM 1381 CB ILE B 253 52.458 31.506 196.798 1.00 38.46 C ANISOU 1381 CB ILE B 253 3712 5623 5280 -1656 -1162 -159 C ATOM 1382 CG1 ILE B 253 53.416 32.545 197.381 1.00 37.78 C ANISOU 1382 CG1 ILE B 253 3600 5520 5235 -1499 -1082 -66 C ATOM 1383 CG2 ILE B 253 53.174 30.181 196.588 1.00 33.26 C ANISOU 1383 CG2 ILE B 253 3065 4837 4736 -1737 -1220 -459 C ATOM 1384 CD1 ILE B 253 53.830 32.260 198.809 1.00 30.36 C ANISOU 1384 CD1 ILE B 253 2699 4378 4460 -1380 -1047 -70 C ATOM 1385 N LYS B 254 49.903 30.575 195.197 1.00 57.23 N ANISOU 1385 N LYS B 254 6113 8234 7397 -1980 -1297 -129 N ATOM 1386 CA LYS B 254 49.126 29.527 194.542 1.00 55.95 C ANISOU 1386 CA LYS B 254 5974 8100 7184 -2154 -1376 -263 C ATOM 1387 C LYS B 254 48.712 29.943 193.136 1.00 47.78 C ANISOU 1387 C LYS B 254 4911 7370 5872 -2303 -1399 -222 C ATOM 1388 O LYS B 254 48.728 29.123 192.211 1.00 54.69 O ANISOU 1388 O LYS B 254 5811 8329 6639 -2467 -1442 -433 O ATOM 1389 CB LYS B 254 47.902 29.172 195.386 1.00 67.14 C ANISOU 1389 CB LYS B 254 7408 9406 8699 -2150 -1397 -143 C ATOM 1390 CG LYS B 254 47.048 28.057 194.802 1.00 80.84 C ANISOU 1390 CG LYS B 254 9163 11147 10406 -2334 -1481 -276 C ATOM 1391 CD LYS B 254 47.868 26.793 194.578 1.00 88.30 C ANISOU 1391 CD LYS B 254 10164 11918 11468 -2407 -1523 -603 C ATOM 1392 CE LYS B 254 48.417 26.242 195.885 1.00 88.52 C ANISOU 1392 CE LYS B 254 10228 11653 11753 -2299 -1489 -657 C ATOM 1393 NZ LYS B 254 49.183 24.982 195.675 1.00 89.34 N ANISOU 1393 NZ LYS B 254 10391 11539 12014 -2364 -1540 -983 N ATOM 1394 N ALA B 255 48.342 31.213 192.955 1.00 44.26 N ANISOU 1394 N ALA B 255 4421 7092 5304 -2256 -1367 44 N ATOM 1395 CA ALA B 255 47.969 31.692 191.629 1.00 41.32 C ANISOU 1395 CA ALA B 255 4014 7030 4657 -2407 -1388 123 C ATOM 1396 C ALA B 255 49.156 31.683 190.674 1.00 55.10 C ANISOU 1396 C ALA B 255 5754 8948 6232 -2492 -1344 -54 C ATOM 1397 O ALA B 255 48.970 31.577 189.457 1.00 57.28 O ANISOU 1397 O ALA B 255 6017 9493 6254 -2676 -1358 -109 O ATOM 1398 CB ALA B 255 47.375 33.097 191.724 1.00 40.15 C ANISOU 1398 CB ALA B 255 3819 6980 4454 -2330 -1370 463 C ATOM 1399 N LEU B 256 50.375 31.790 191.203 1.00 51.79 N ANISOU 1399 N LEU B 256 5339 8404 5934 -2371 -1283 -151 N ATOM 1400 CA LEU B 256 51.560 31.822 190.355 1.00 60.03 C ANISOU 1400 CA LEU B 256 6364 9635 6812 -2448 -1217 -332 C ATOM 1401 C LEU B 256 52.010 30.419 189.964 1.00 63.13 C ANISOU 1401 C LEU B 256 6806 9974 7208 -2557 -1224 -722 C ATOM 1402 O LEU B 256 52.437 30.195 188.826 1.00 66.48 O ANISOU 1402 O LEU B 256 7221 10651 7385 -2711 -1171 -919 O ATOM 1403 CB LEU B 256 52.687 32.569 191.068 1.00 59.57 C ANISOU 1403 CB LEU B 256 6274 9477 6882 -2277 -1144 -273 C ATOM 1404 CG LEU B 256 53.988 32.774 190.293 1.00 60.81 C ANISOU 1404 CG LEU B 256 6385 9850 6869 -2340 -1051 -438 C ATOM 1405 CD1 LEU B 256 53.729 33.547 189.010 1.00 62.70 C ANISOU 1405 CD1 LEU B 256 6582 10475 6767 -2507 -1023 -297 C ATOM 1406 CD2 LEU B 256 55.003 33.496 191.160 1.00 55.80 C ANISOU 1406 CD2 LEU B 256 5714 9081 6408 -2158 -992 -360 C ATOM 1407 N VAL B 257 51.921 29.464 190.894 1.00 63.43 N ANISOU 1407 N VAL B 257 6899 9681 7519 -2485 -1279 -845 N ATOM 1408 CA VAL B 257 52.332 28.095 190.600 1.00 63.53 C ANISOU 1408 CA VAL B 257 6983 9573 7581 -2574 -1293 -1220 C ATOM 1409 C VAL B 257 51.363 27.435 189.626 1.00 64.94 C ANISOU 1409 C VAL B 257 7199 9896 7579 -2774 -1343 -1324 C ATOM 1410 O VAL B 257 51.770 26.608 188.799 1.00 75.07 O ANISOU 1410 O VAL B 257 8529 11245 8751 -2897 -1307 -1657 O ATOM 1411 CB VAL B 257 52.465 27.292 191.908 1.00 55.43 C ANISOU 1411 CB VAL B 257 6015 8128 6916 -2451 -1358 -1272 C ATOM 1412 CG1 VAL B 257 52.857 25.854 191.620 1.00 53.76 C ANISOU 1412 CG1 VAL B 257 5907 7736 6785 -2537 -1378 -1648 C ATOM 1413 CG2 VAL B 257 53.490 27.942 192.824 1.00 42.33 C ANISOU 1413 CG2 VAL B 257 4313 6354 5416 -2269 -1308 -1180 C ATOM 1414 N ASP B 258 50.077 27.791 189.690 1.00 59.69 N ANISOU 1414 N ASP B 258 6509 9291 6879 -2807 -1413 -1062 N ATOM 1415 CA ASP B 258 49.101 27.201 188.778 1.00 68.20 C ANISOU 1415 CA ASP B 258 7608 10521 7784 -3006 -1472 -1141 C ATOM 1416 C ASP B 258 49.388 27.591 187.334 1.00 75.00 C ANISOU 1416 C ASP B 258 8437 11783 8276 -3171 -1406 -1218 C ATOM 1417 O ASP B 258 49.226 26.775 186.419 1.00 77.66 O ANISOU 1417 O ASP B 258 8813 12236 8457 -3348 -1411 -1474 O ATOM 1418 CB ASP B 258 47.687 27.624 189.176 1.00 68.61 C ANISOU 1418 CB ASP B 258 7618 10582 7870 -2998 -1545 -827 C ATOM 1419 CG ASP B 258 47.266 27.059 190.518 1.00 70.47 C ANISOU 1419 CG ASP B 258 7880 10465 8431 -2880 -1591 -790 C ATOM 1420 OD1 ASP B 258 48.102 26.407 191.179 1.00 70.61 O ANISOU 1420 OD1 ASP B 258 7950 10215 8664 -2797 -1583 -970 O ATOM 1421 OD2 ASP B 258 46.099 27.268 190.911 1.00 69.17 O ANISOU 1421 OD2 ASP B 258 7680 10302 8298 -2878 -1629 -577 O ATOM 1422 N ARG B 259 49.810 28.837 187.106 1.00 76.11 N ANISOU 1422 N ARG B 259 8504 12144 8269 -3126 -1340 -999 N ATOM 1423 CA ARG B 259 50.205 29.243 185.762 1.00 76.00 C ANISOU 1423 CA ARG B 259 8448 12531 7897 -3294 -1263 -1059 C ATOM 1424 C ARG B 259 51.469 28.525 185.307 1.00 72.54 C ANISOU 1424 C ARG B 259 8037 12124 7401 -3332 -1147 -1482 C ATOM 1425 O ARG B 259 51.612 28.217 184.118 1.00 73.66 O ANISOU 1425 O ARG B 259 8172 12555 7262 -3519 -1085 -1692 O ATOM 1426 N CYS B 260 52.394 28.252 186.233 1.00 68.73 N ANISOU 1426 N CYS B 260 7576 11356 7181 -3158 -1108 -1619 N ATOM 1427 CA CYS B 260 53.606 27.522 185.878 1.00 70.97 C ANISOU 1427 CA CYS B 260 7876 11634 7455 -3164 -983 -2051 C ATOM 1428 C CYS B 260 53.315 26.064 185.546 1.00 76.87 C ANISOU 1428 C CYS B 260 8723 12224 8260 -3257 -1008 -2418 C ATOM 1429 O CYS B 260 53.964 25.489 184.666 1.00 71.74 O ANISOU 1429 O CYS B 260 8078 11717 7462 -3346 -887 -2792 O ATOM 1430 CB CYS B 260 54.624 27.612 187.016 1.00 66.72 C ANISOU 1430 CB CYS B 260 7326 10810 7212 -2944 -945 -2083 C ATOM 1431 SG CYS B 260 56.142 26.668 186.741 1.00 75.94 S ANISOU 1431 SG CYS B 260 8496 11908 8450 -2894 -777 -2639 S ATOM 1432 N ARG B 261 52.347 25.450 186.229 1.00 79.42 N ANISOU 1432 N ARG B 261 9121 12253 8802 -3240 -1154 -2325 N ATOM 1433 CA ARG B 261 52.016 24.058 185.954 1.00 86.12 C ANISOU 1433 CA ARG B 261 10075 12918 9730 -3336 -1195 -2649 C ATOM 1434 C ARG B 261 51.165 23.897 184.702 1.00 83.53 C ANISOU 1434 C ARG B 261 9741 12911 9086 -3573 -1214 -2700 C ATOM 1435 O ARG B 261 51.101 22.793 184.151 1.00 84.81 O ANISOU 1435 O ARG B 261 9981 13006 9236 -3682 -1207 -3043 O ATOM 1436 CB ARG B 261 51.301 23.439 187.157 1.00 86.56 C ANISOU 1436 CB ARG B 261 10205 12546 10137 -3252 -1348 -2518 C ATOM 1437 CG ARG B 261 52.178 23.328 188.395 1.00 85.95 C ANISOU 1437 CG ARG B 261 10155 12112 10389 -3042 -1339 -2517 C ATOM 1438 CD ARG B 261 51.391 22.854 189.605 1.00 90.16 C ANISOU 1438 CD ARG B 261 10745 12274 11237 -2982 -1492 -2319 C ATOM 1439 NE ARG B 261 52.233 22.767 190.794 1.00 90.99 N ANISOU 1439 NE ARG B 261 10882 12057 11633 -2801 -1490 -2287 N ATOM 1440 CZ ARG B 261 51.784 22.486 192.013 1.00 92.97 C ANISOU 1440 CZ ARG B 261 11171 11990 12162 -2728 -1605 -2084 C ATOM 1441 NH1 ARG B 261 50.491 22.262 192.211 1.00 95.50 N ANISOU 1441 NH1 ARG B 261 11473 12276 12537 -2799 -1710 -1931 N ATOM 1442 NH2 ARG B 261 52.626 22.430 193.035 1.00 84.84 N ANISOU 1442 NH2 ARG B 261 10185 10706 11346 -2590 -1594 -2042 N ATOM 1443 N ALA B 262 50.516 24.967 184.241 1.00 80.59 N ANISOU 1443 N ALA B 262 9281 12874 8466 -3654 -1238 -2365 N ATOM 1444 CA ALA B 262 49.728 24.886 183.017 1.00 87.47 C ANISOU 1444 CA ALA B 262 10134 14083 9016 -3892 -1259 -2387 C ATOM 1445 C ALA B 262 50.615 24.918 181.778 1.00 94.39 C ANISOU 1445 C ALA B 262 10976 15317 9570 -4025 -1097 -2667 C ATOM 1446 O ALA B 262 50.331 24.229 180.791 1.00103.77 O ANISOU 1446 O ALA B 262 12192 16674 10562 -4217 -1080 -2921 O ATOM 1447 CB ALA B 262 48.707 26.023 182.974 1.00 85.37 C ANISOU 1447 CB ALA B 262 9783 14034 8621 -3926 -1345 -1911 C ATOM 1448 N LYS B 263 51.689 25.711 181.807 1.00 89.34 N ANISOU 1448 N LYS B 263 10267 14809 8869 -3933 -971 -2632 N ATOM 1449 CA LYS B 263 52.572 25.814 180.650 1.00 93.38 C ANISOU 1449 CA LYS B 263 10719 15693 9069 -4062 -796 -2886 C ATOM 1450 C LYS B 263 53.499 24.612 180.521 1.00 95.48 C ANISOU 1450 C LYS B 263 11041 15780 9456 -4019 -668 -3433 C ATOM 1451 O LYS B 263 53.901 24.265 179.404 1.00 97.72 O ANISOU 1451 O LYS B 263 11296 16347 9486 -4171 -536 -3742 O ATOM 1452 CB LYS B 263 53.383 27.113 180.721 1.00 92.36 C ANISOU 1452 CB LYS B 263 10480 15778 8834 -3992 -705 -2642 C ATOM 1453 CG LYS B 263 54.221 27.294 181.985 1.00 92.39 C ANISOU 1453 CG LYS B 263 10486 15443 9173 -3729 -683 -2625 C ATOM 1454 CD LYS B 263 55.654 26.804 181.803 1.00 97.25 C ANISOU 1454 CD LYS B 263 11072 16059 9821 -3663 -491 -3067 C ATOM 1455 CE LYS B 263 56.408 26.795 183.124 1.00 95.11 C ANISOU 1455 CE LYS B 263 10807 15404 9926 -3400 -491 -3077 C ATOM 1456 NZ LYS B 263 57.764 26.194 182.998 1.00 97.14 N ANISOU 1456 NZ LYS B 263 11024 15615 10270 -3307 -307 -3538 N ATOM 1457 N ALA B 264 53.851 23.974 181.634 1.00 94.35 N ANISOU 1457 N ALA B 264 10972 15171 9706 -3813 -700 -3555 N ATOM 1458 CA ALA B 264 54.800 22.865 181.627 1.00 95.69 C ANISOU 1458 CA ALA B 264 11191 15109 10059 -3725 -577 -4055 C ATOM 1459 C ALA B 264 54.284 21.670 180.830 1.00 98.80 C ANISOU 1459 C ALA B 264 11672 15478 10388 -3886 -587 -4396 C ATOM 1460 O ALA B 264 54.874 21.282 179.822 1.00102.91 O ANISOU 1460 O ALA B 264 12159 16222 10719 -3979 -426 -4763 O ATOM 1461 N ALA B 271 63.573 26.708 181.071 1.00106.11 N ANISOU 1461 N ALA B 271 11560 17653 11105 -3129 643 -4824 N ATOM 1462 CA ALA B 271 63.532 26.818 182.525 1.00100.33 C ANISOU 1462 CA ALA B 271 10886 16483 10754 -2896 498 -4632 C ATOM 1463 C ALA B 271 63.110 28.218 182.957 1.00 96.89 C ANISOU 1463 C ALA B 271 10430 16202 10183 -2955 372 -4086 C ATOM 1464 O ALA B 271 62.943 28.481 184.145 1.00 91.84 O ANISOU 1464 O ALA B 271 9830 15239 9825 -2794 234 -3848 O ATOM 1465 CB ALA B 271 64.886 26.464 183.121 1.00102.15 C ANISOU 1465 CB ALA B 271 11010 16493 11310 -2633 631 -4956 C ATOM 1466 N GLN B 272 62.928 29.107 181.977 1.00 99.80 N ANISOU 1466 N GLN B 272 10731 17051 10137 -3189 417 -3869 N ATOM 1467 CA GLN B 272 62.694 30.517 182.277 1.00 97.05 C ANISOU 1467 CA GLN B 272 10343 16864 9668 -3236 323 -3347 C ATOM 1468 C GLN B 272 61.385 30.722 183.030 1.00 93.02 C ANISOU 1468 C GLN B 272 9967 16070 9305 -3195 84 -2932 C ATOM 1469 O GLN B 272 61.338 31.453 184.028 1.00 86.83 O ANISOU 1469 O GLN B 272 9182 15089 8720 -3055 -19 -2603 O ATOM 1470 CB GLN B 272 62.701 31.333 180.983 1.00 98.22 C ANISOU 1470 CB GLN B 272 10398 17566 9354 -3510 411 -3186 C ATOM 1471 CG GLN B 272 64.031 31.337 180.239 1.00101.29 C ANISOU 1471 CG GLN B 272 10620 18284 9580 -3568 656 -3527 C ATOM 1472 CD GLN B 272 65.032 32.326 180.813 1.00 94.55 C ANISOU 1472 CD GLN B 272 9641 17500 8782 -3475 711 -3376 C ATOM 1473 OE1 GLN B 272 65.159 32.471 182.030 1.00 86.03 O ANISOU 1473 OE1 GLN B 272 8592 16071 8022 -3258 614 -3276 O ATOM 1474 NE2 GLN B 272 65.749 33.015 179.933 1.00 96.03 N ANISOU 1474 NE2 GLN B 272 9677 18138 8674 -3653 855 -3347 N ATOM 1475 N TRP B 273 60.305 30.091 182.563 1.00 92.62 N ANISOU 1475 N TRP B 273 10023 15997 9172 -3312 -2 -2943 N ATOM 1476 CA TRP B 273 58.994 30.336 183.157 1.00 90.68 C ANISOU 1476 CA TRP B 273 9881 15538 9037 -3292 -216 -2541 C ATOM 1477 C TRP B 273 58.915 29.813 184.587 1.00 90.14 C ANISOU 1477 C TRP B 273 9889 14947 9413 -3053 -323 -2549 C ATOM 1478 O TRP B 273 58.371 30.486 185.470 1.00 90.81 O ANISOU 1478 O TRP B 273 9996 14849 9658 -2950 -454 -2156 O ATOM 1479 N GLY B 274 59.450 28.616 184.838 1.00 90.70 N ANISOU 1479 N GLY B 274 9997 14761 9702 -2956 -265 -2983 N ATOM 1480 CA GLY B 274 59.434 28.076 186.186 1.00 86.14 C ANISOU 1480 CA GLY B 274 9488 13688 9552 -2744 -367 -2981 C ATOM 1481 C GLY B 274 60.437 28.729 187.117 1.00 88.99 C ANISOU 1481 C GLY B 274 9754 13936 10122 -2551 -330 -2897 C ATOM 1482 O GLY B 274 60.241 28.738 188.336 1.00 83.61 O ANISOU 1482 O GLY B 274 9113 12906 9749 -2395 -446 -2706 O ATOM 1483 N ARG B 275 61.520 29.280 186.564 1.00 93.91 N ANISOU 1483 N ARG B 275 10241 14862 10578 -2569 -167 -3035 N ATOM 1484 CA ARG B 275 62.539 29.911 187.398 1.00 96.09 C ANISOU 1484 CA ARG B 275 10404 15053 11054 -2395 -129 -2972 C ATOM 1485 C ARG B 275 62.015 31.187 188.047 1.00 89.37 C ANISOU 1485 C ARG B 275 9550 14195 10210 -2368 -248 -2413 C ATOM 1486 O ARG B 275 62.338 31.479 189.204 1.00 88.19 O ANISOU 1486 O ARG B 275 9379 13774 10356 -2181 -300 -2259 O ATOM 1487 CB ARG B 275 63.787 30.199 186.566 1.00103.36 C ANISOU 1487 CB ARG B 275 11165 16337 11770 -2445 81 -3258 C ATOM 1488 CG ARG B 275 64.977 30.715 187.352 1.00103.38 C ANISOU 1488 CG ARG B 275 11019 16263 11998 -2266 137 -3272 C ATOM 1489 CD ARG B 275 65.999 31.344 186.419 1.00114.02 C ANISOU 1489 CD ARG B 275 12211 18051 13059 -2356 343 -3385 C ATOM 1490 NE ARG B 275 67.340 31.349 186.996 1.00120.61 N ANISOU 1490 NE ARG B 275 12927 18730 14170 -2099 477 -3523 N ATOM 1491 CZ ARG B 275 68.262 30.425 186.744 1.00124.08 C ANISOU 1491 CZ ARG B 275 13299 19113 14732 -1972 641 -4014 C ATOM 1492 NH1 ARG B 275 67.988 29.422 185.921 1.00125.54 N ANISOU 1492 NH1 ARG B 275 13540 19373 14787 -2084 701 -4436 N ATOM 1493 NH2 ARG B 275 69.458 30.504 187.310 1.00124.69 N ANISOU 1493 NH2 ARG B 275 13246 19058 15074 -1733 743 -4095 N ATOM 1494 N ILE B 276 61.207 31.959 187.318 1.00 84.08 N ANISOU 1494 N ILE B 276 8904 13805 9238 -2537 -287 -2101 N ATOM 1495 CA ILE B 276 60.686 33.212 187.857 1.00 67.67 C ANISOU 1495 CA ILE B 276 6836 11688 7190 -2483 -384 -1581 C ATOM 1496 C ILE B 276 59.700 32.938 188.986 1.00 64.41 C ANISOU 1496 C ILE B 276 6534 10866 7072 -2347 -546 -1375 C ATOM 1497 O ILE B 276 59.649 33.676 189.978 1.00 59.84 O ANISOU 1497 O ILE B 276 5958 10081 6696 -2189 -600 -1079 O ATOM 1498 CB ILE B 276 60.046 34.049 186.733 1.00 62.54 C ANISOU 1498 CB ILE B 276 6181 11418 6163 -2691 -388 -1317 C ATOM 1499 CG1 ILE B 276 61.090 34.407 185.674 1.00 64.63 C ANISOU 1499 CG1 ILE B 276 6323 12118 6117 -2844 -220 -1486 C ATOM 1500 CG2 ILE B 276 59.407 35.311 187.295 1.00 53.75 C ANISOU 1500 CG2 ILE B 276 5096 10200 5127 -2605 -491 -800 C ATOM 1501 CD1 ILE B 276 60.562 35.303 184.574 1.00 66.14 C ANISOU 1501 CD1 ILE B 276 6497 12704 5929 -3068 -226 -1185 C ATOM 1502 N THR B 277 58.911 31.869 188.861 1.00 66.19 N ANISOU 1502 N THR B 277 6853 10971 7326 -2408 -615 -1537 N ATOM 1503 CA THR B 277 57.880 31.582 189.855 1.00 65.60 C ANISOU 1503 CA THR B 277 6874 10553 7498 -2315 -765 -1336 C ATOM 1504 C THR B 277 58.496 31.226 191.204 1.00 55.65 C ANISOU 1504 C THR B 277 5617 8925 6602 -2114 -789 -1389 C ATOM 1505 O THR B 277 58.050 31.716 192.248 1.00 52.02 O ANISOU 1505 O THR B 277 5182 8250 6334 -1987 -870 -1091 O ATOM 1506 CB THR B 277 56.977 30.451 189.362 1.00 69.38 C ANISOU 1506 CB THR B 277 7446 10992 7924 -2446 -830 -1519 C ATOM 1507 OG1 THR B 277 57.763 29.274 189.135 1.00 77.10 O ANISOU 1507 OG1 THR B 277 8442 11884 8969 -2454 -753 -1984 O ATOM 1508 CG2 THR B 277 56.284 30.848 188.067 1.00 67.57 C ANISOU 1508 CG2 THR B 277 7204 11138 7330 -2650 -819 -1426 C ATOM 1509 N THR B 278 59.522 30.371 191.203 1.00 55.88 N ANISOU 1509 N THR B 278 5618 8874 6739 -2072 -708 -1783 N ATOM 1510 CA THR B 278 60.153 29.987 192.462 1.00 56.05 C ANISOU 1510 CA THR B 278 5634 8546 7117 -1877 -735 -1839 C ATOM 1511 C THR B 278 60.870 31.170 193.101 1.00 54.05 C ANISOU 1511 C THR B 278 5280 8327 6929 -1743 -697 -1595 C ATOM 1512 O THR B 278 60.854 31.322 194.327 1.00 50.27 O ANISOU 1512 O THR B 278 4823 7582 6696 -1597 -769 -1403 O ATOM 1513 CB THR B 278 61.124 28.828 192.238 1.00 56.79 C ANISOU 1513 CB THR B 278 5708 8519 7351 -1820 -645 -2342 C ATOM 1514 OG1 THR B 278 62.031 29.160 191.181 1.00 72.64 O ANISOU 1514 OG1 THR B 278 7594 10876 9131 -1882 -480 -2586 O ATOM 1515 CG2 THR B 278 60.366 27.559 191.876 1.00 54.71 C ANISOU 1515 CG2 THR B 278 5584 8097 7108 -1914 -699 -2554 C ATOM 1516 N GLU B 279 61.499 32.020 192.285 1.00 57.35 N ANISOU 1516 N GLU B 279 5596 9076 7120 -1802 -582 -1588 N ATOM 1517 CA GLU B 279 62.153 33.210 192.821 1.00 55.47 C ANISOU 1517 CA GLU B 279 5279 8860 6937 -1684 -543 -1332 C ATOM 1518 C GLU B 279 61.136 34.165 193.431 1.00 50.13 C ANISOU 1518 C GLU B 279 4689 8066 6293 -1638 -646 -873 C ATOM 1519 O GLU B 279 61.396 34.782 194.472 1.00 42.92 O ANISOU 1519 O GLU B 279 3776 6955 5577 -1478 -666 -676 O ATOM 1520 CB GLU B 279 62.956 33.907 191.723 1.00 61.75 C ANISOU 1520 CB GLU B 279 5958 10044 7460 -1789 -398 -1402 C ATOM 1521 CG GLU B 279 64.174 33.129 191.252 1.00 73.22 C ANISOU 1521 CG GLU B 279 7281 11612 8928 -1787 -257 -1888 C ATOM 1522 CD GLU B 279 64.833 33.757 190.041 1.00 81.58 C ANISOU 1522 CD GLU B 279 8219 13120 9656 -1944 -104 -1965 C ATOM 1523 OE1 GLU B 279 64.331 34.796 189.562 1.00 82.14 O ANISOU 1523 OE1 GLU B 279 8325 13394 9489 -2058 -125 -1613 O ATOM 1524 OE2 GLU B 279 65.854 33.214 189.568 1.00 84.55 O ANISOU 1524 OE2 GLU B 279 8490 13615 10021 -1924 46 -2360 O ATOM 1525 N THR B 280 59.970 34.302 192.796 1.00 46.31 N ANISOU 1525 N THR B 280 4274 7695 5627 -1762 -701 -731 N ATOM 1526 CA THR B 280 58.923 35.151 193.351 1.00 41.47 C ANISOU 1526 CA THR B 280 3730 6957 5072 -1688 -774 -370 C ATOM 1527 C THR B 280 58.289 34.522 194.586 1.00 42.07 C ANISOU 1527 C THR B 280 3874 6689 5420 -1569 -865 -344 C ATOM 1528 O THR B 280 57.884 35.240 195.507 1.00 43.68 O ANISOU 1528 O THR B 280 4113 6733 5752 -1430 -869 -134 O ATOM 1529 CB THR B 280 57.860 35.431 192.289 1.00 46.08 C ANISOU 1529 CB THR B 280 4344 7778 5386 -1851 -802 -242 C ATOM 1530 OG1 THR B 280 58.497 35.855 191.077 1.00 54.83 O ANISOU 1530 OG1 THR B 280 5382 9244 6205 -2000 -717 -295 O ATOM 1531 CG2 THR B 280 56.906 36.521 192.758 1.00 44.09 C ANISOU 1531 CG2 THR B 280 4139 7437 5176 -1761 -841 110 C ATOM 1532 N ALA B 281 58.198 33.190 194.626 1.00 47.09 N ANISOU 1532 N ALA B 281 4541 7219 6133 -1630 -921 -580 N ATOM 1533 CA ALA B 281 57.634 32.520 195.794 1.00 31.67 C ANISOU 1533 CA ALA B 281 2649 4951 4433 -1544 -1014 -549 C ATOM 1534 C ALA B 281 58.522 32.704 197.019 1.00 39.52 C ANISOU 1534 C ALA B 281 3611 5735 5669 -1375 -1009 -515 C ATOM 1535 O ALA B 281 58.019 32.877 198.136 1.00 39.38 O ANISOU 1535 O ALA B 281 3621 5586 5755 -1261 -982 -431 O ATOM 1536 CB ALA B 281 57.424 31.036 195.499 1.00 33.85 C ANISOU 1536 CB ALA B 281 2989 5134 4737 -1668 -1082 -809 C ATOM 1537 N ILE B 282 59.844 32.662 196.832 1.00 31.53 N ANISOU 1537 N ILE B 282 2533 4796 4650 -1361 -947 -660 N ATOM 1538 CA ILE B 282 60.763 32.926 197.936 1.00 28.82 C ANISOU 1538 CA ILE B 282 2161 4319 4470 -1212 -926 -590 C ATOM 1539 C ILE B 282 60.598 34.357 198.429 1.00 39.05 C ANISOU 1539 C ILE B 282 3439 5584 5812 -1066 -877 -368 C ATOM 1540 O ILE B 282 60.691 34.633 199.633 1.00 34.08 O ANISOU 1540 O ILE B 282 2856 4980 5113 -987 -788 -315 O ATOM 1541 CB ILE B 282 62.214 32.640 197.506 1.00 40.38 C ANISOU 1541 CB ILE B 282 3510 5850 5983 -1137 -815 -921 C ATOM 1542 CG1 ILE B 282 62.372 31.183 197.065 1.00 35.80 C ANISOU 1542 CG1 ILE B 282 2939 5161 5502 -1163 -821 -1326 C ATOM 1543 CG2 ILE B 282 63.186 32.963 198.634 1.00 39.45 C ANISOU 1543 CG2 ILE B 282 3357 5570 6060 -937 -796 -851 C ATOM 1544 CD1 ILE B 282 62.097 30.180 198.157 1.00 32.55 C ANISOU 1544 CD1 ILE B 282 2633 4367 5368 -1063 -932 -1330 C ATOM 1545 N GLN B 283 60.344 35.288 197.507 1.00 38.92 N ANISOU 1545 N GLN B 283 3410 5784 5594 -1132 -815 -271 N ATOM 1546 CA GLN B 283 60.153 36.685 197.883 1.00 37.82 C ANISOU 1546 CA GLN B 283 3313 5657 5399 -1036 -738 -69 C ATOM 1547 C GLN B 283 58.954 36.848 198.810 1.00 38.28 C ANISOU 1547 C GLN B 283 3490 5595 5459 -970 -744 65 C ATOM 1548 O GLN B 283 59.033 37.540 199.831 1.00 44.50 O ANISOU 1548 O GLN B 283 4344 6287 6279 -853 -697 165 O ATOM 1549 CB GLN B 283 59.979 37.540 196.626 1.00 46.78 C ANISOU 1549 CB GLN B 283 4436 7039 6301 -1152 -705 58 C ATOM 1550 CG GLN B 283 59.628 38.990 196.904 1.00 53.24 C ANISOU 1550 CG GLN B 283 5315 7841 7071 -1082 -664 299 C ATOM 1551 CD GLN B 283 60.804 39.777 197.442 1.00 56.73 C ANISOU 1551 CD GLN B 283 5733 8220 7604 -979 -595 298 C ATOM 1552 OE1 GLN B 283 61.957 39.477 197.134 1.00 60.67 O ANISOU 1552 OE1 GLN B 283 6134 8785 8133 -997 -561 163 O ATOM 1553 NE2 GLN B 283 60.519 40.790 198.253 1.00 58.12 N ANISOU 1553 NE2 GLN B 283 5994 8276 7814 -879 -573 444 N ATOM 1554 N LEU B 284 57.832 36.207 198.472 1.00 43.21 N ANISOU 1554 N LEU B 284 4151 6235 6033 -1059 -804 76 N ATOM 1555 CA LEU B 284 56.618 36.366 199.266 1.00 39.53 C ANISOU 1555 CA LEU B 284 3782 5678 5561 -1014 -809 229 C ATOM 1556 C LEU B 284 56.724 35.654 200.610 1.00 42.52 C ANISOU 1556 C LEU B 284 4217 5883 6056 -939 -811 190 C ATOM 1557 O LEU B 284 56.254 36.172 201.631 1.00 46.22 O ANISOU 1557 O LEU B 284 4766 6258 6536 -852 -784 336 O ATOM 1558 CB LEU B 284 55.412 35.859 198.476 1.00 35.94 C ANISOU 1558 CB LEU B 284 3336 5307 5014 -1143 -874 255 C ATOM 1559 CG LEU B 284 55.093 36.676 197.223 1.00 41.44 C ANISOU 1559 CG LEU B 284 4002 6213 5529 -1236 -879 380 C ATOM 1560 CD1 LEU B 284 54.020 36.002 196.388 1.00 43.02 C ANISOU 1560 CD1 LEU B 284 4204 6528 5614 -1387 -951 372 C ATOM 1561 CD2 LEU B 284 54.668 38.082 197.611 1.00 24.61 C ANISOU 1561 CD2 LEU B 284 1910 4066 3374 -1146 -840 619 C ATOM 1562 N MET B 285 57.337 34.468 200.636 1.00 28.95 N ANISOU 1562 N MET B 285 2465 4116 4417 -988 -853 13 N ATOM 1563 CA MET B 285 57.472 33.743 201.895 1.00 25.58 C ANISOU 1563 CA MET B 285 2118 3498 4105 -929 -886 49 C ATOM 1564 C MET B 285 58.434 34.442 202.847 1.00 29.27 C ANISOU 1564 C MET B 285 2602 3892 4626 -783 -843 124 C ATOM 1565 O MET B 285 58.246 34.385 204.068 1.00 20.98 O ANISOU 1565 O MET B 285 1637 2692 3645 -703 -858 237 O ATOM 1566 CB MET B 285 57.933 32.310 201.634 1.00 34.08 C ANISOU 1566 CB MET B 285 3183 4471 5293 -1013 -972 -130 C ATOM 1567 CG MET B 285 56.895 31.442 200.947 1.00 48.31 C ANISOU 1567 CG MET B 285 5009 6295 7052 -1172 -1023 -218 C ATOM 1568 SD MET B 285 57.424 29.725 200.810 1.00 66.10 S ANISOU 1568 SD MET B 285 7318 8305 9493 -1244 -1134 -450 S ATOM 1569 CE MET B 285 58.807 29.887 199.686 1.00 63.53 C ANISOU 1569 CE MET B 285 6874 8095 9168 -1250 -1115 -696 C ATOM 1570 N GLY B 286 59.466 35.100 202.312 1.00 31.61 N ANISOU 1570 N GLY B 286 2816 4304 4891 -759 -791 57 N ATOM 1571 CA GLY B 286 60.383 35.837 203.162 1.00 20.03 C ANISOU 1571 CA GLY B 286 1368 2781 3462 -633 -745 118 C ATOM 1572 C GLY B 286 59.740 37.030 203.839 1.00 24.35 C ANISOU 1572 C GLY B 286 2008 3301 3944 -570 -689 277 C ATOM 1573 O GLY B 286 60.086 37.361 204.977 1.00 23.65 O ANISOU 1573 O GLY B 286 1980 3095 3911 -486 -682 353 O ATOM 1574 N ILE B 287 58.801 37.691 203.154 1.00 25.35 N ANISOU 1574 N ILE B 287 2138 3507 3987 -620 -674 355 N ATOM 1575 CA ILE B 287 58.081 38.808 203.757 1.00 17.79 C ANISOU 1575 CA ILE B 287 1250 2486 3023 -582 -666 566 C ATOM 1576 C ILE B 287 57.285 38.337 204.967 1.00 31.21 C ANISOU 1576 C ILE B 287 3027 4051 4778 -556 -699 651 C ATOM 1577 O ILE B 287 57.265 38.997 206.014 1.00 21.81 O ANISOU 1577 O ILE B 287 1887 2768 3630 -496 -682 751 O ATOM 1578 CB ILE B 287 57.171 39.482 202.713 1.00 18.47 C ANISOU 1578 CB ILE B 287 1315 2684 3019 -651 -672 671 C ATOM 1579 CG1 ILE B 287 57.996 39.999 201.535 1.00 25.37 C ANISOU 1579 CG1 ILE B 287 2111 3695 3833 -689 -643 611 C ATOM 1580 CG2 ILE B 287 56.377 40.616 203.343 1.00 23.92 C ANISOU 1580 CG2 ILE B 287 2058 3308 3721 -611 -667 881 C ATOM 1581 CD1 ILE B 287 57.164 40.613 200.431 1.00 20.14 C ANISOU 1581 CD1 ILE B 287 1429 3158 3064 -772 -666 745 C ATOM 1582 N MET B 288 56.619 37.187 204.843 1.00 31.38 N ANISOU 1582 N MET B 288 3053 4068 4803 -613 -745 600 N ATOM 1583 CA MET B 288 55.823 36.665 205.948 1.00 28.50 C ANISOU 1583 CA MET B 288 2752 3593 4486 -605 -781 687 C ATOM 1584 C MET B 288 56.703 36.258 207.123 1.00 30.84 C ANISOU 1584 C MET B 288 3085 3759 4873 -536 -795 668 C ATOM 1585 O MET B 288 56.307 36.411 208.284 1.00 27.70 O ANISOU 1585 O MET B 288 2737 3283 4503 -507 -804 773 O ATOM 1586 CB MET B 288 54.980 35.483 205.466 1.00 43.82 C ANISOU 1586 CB MET B 288 4684 5553 6412 -701 -833 631 C ATOM 1587 CG MET B 288 54.069 35.822 204.290 1.00 52.11 C ANISOU 1587 CG MET B 288 5691 6740 7367 -783 -833 653 C ATOM 1588 SD MET B 288 53.241 34.389 203.565 1.00 43.69 S ANISOU 1588 SD MET B 288 4608 5707 6285 -922 -892 535 S ATOM 1589 CE MET B 288 52.359 33.747 204.985 1.00 39.04 C ANISOU 1589 CE MET B 288 4091 4982 5761 -917 -933 658 C ATOM 1590 N LEU B 289 57.903 35.743 206.843 1.00 34.68 N ANISOU 1590 N LEU B 289 3537 4235 5405 -514 -801 533 N ATOM 1591 CA LEU B 289 58.782 35.302 207.922 1.00 30.86 C ANISOU 1591 CA LEU B 289 3079 3611 5035 -447 -842 538 C ATOM 1592 C LEU B 289 59.299 36.479 208.739 1.00 34.76 C ANISOU 1592 C LEU B 289 3600 4092 5515 -382 -785 604 C ATOM 1593 O LEU B 289 59.336 36.416 209.973 1.00 32.24 O ANISOU 1593 O LEU B 289 3329 3679 5241 -358 -807 675 O ATOM 1594 CB LEU B 289 59.951 34.498 207.357 1.00 34.47 C ANISOU 1594 CB LEU B 289 3463 4020 5612 -433 -900 404 C ATOM 1595 CG LEU B 289 60.927 33.979 208.414 1.00 39.53 C ANISOU 1595 CG LEU B 289 4116 4482 6420 -351 -972 413 C ATOM 1596 CD1 LEU B 289 60.257 32.926 209.284 1.00 44.45 C ANISOU 1596 CD1 LEU B 289 4801 4934 7155 -374 -1089 510 C ATOM 1597 CD2 LEU B 289 62.205 33.443 207.780 1.00 40.95 C ANISOU 1597 CD2 LEU B 289 4197 4621 6742 -300 -1014 250 C ATOM 1598 N VAL B 290 59.698 37.563 208.072 1.00 15.91 N ANISOU 1598 N VAL B 290 1176 1797 3073 -372 -722 589 N ATOM 1599 CA VAL B 290 60.219 38.723 208.790 1.00 15.28 C ANISOU 1599 CA VAL B 290 1116 1688 3001 -329 -678 644 C ATOM 1600 C VAL B 290 59.127 39.353 209.647 1.00 40.56 C ANISOU 1600 C VAL B 290 4372 4851 6188 -338 -667 775 C ATOM 1601 O VAL B 290 59.341 39.659 210.827 1.00 32.22 O ANISOU 1601 O VAL B 290 3346 3734 5161 -316 -662 807 O ATOM 1602 CB VAL B 290 60.820 39.741 207.805 1.00 20.92 C ANISOU 1602 CB VAL B 290 1775 2506 3666 -329 -625 612 C ATOM 1603 CG1 VAL B 290 61.245 41.005 208.539 1.00 14.88 C ANISOU 1603 CG1 VAL B 290 1034 1700 2921 -296 -586 673 C ATOM 1604 CG2 VAL B 290 61.997 39.127 207.063 1.00 15.99 C ANISOU 1604 CG2 VAL B 290 1070 1956 3049 -320 -626 461 C ATOM 1605 N LEU B 291 57.941 39.553 209.066 1.00 32.13 N ANISOU 1605 N LEU B 291 3301 3837 5070 -375 -665 841 N ATOM 1606 CA LEU B 291 56.846 40.186 209.795 1.00 25.66 C ANISOU 1606 CA LEU B 291 2504 3003 4243 -378 -652 950 C ATOM 1607 C LEU B 291 56.422 39.361 211.005 1.00 32.04 C ANISOU 1607 C LEU B 291 3344 3759 5071 -386 -688 977 C ATOM 1608 O LEU B 291 56.203 39.908 212.093 1.00 14.63 O ANISOU 1608 O LEU B 291 1147 1540 2872 -371 -668 1016 O ATOM 1609 CB LEU B 291 55.658 40.403 208.859 1.00 22.93 C ANISOU 1609 CB LEU B 291 2133 2734 3848 -419 -656 1017 C ATOM 1610 CG LEU B 291 55.691 41.629 207.947 1.00 29.22 C ANISOU 1610 CG LEU B 291 2895 3582 4624 -416 -625 1065 C ATOM 1611 CD1 LEU B 291 54.648 41.497 206.850 1.00 16.31 C ANISOU 1611 CD1 LEU B 291 1226 2040 2929 -476 -653 1125 C ATOM 1612 CD2 LEU B 291 55.459 42.897 208.756 1.00 15.27 C ANISOU 1612 CD2 LEU B 291 1131 1761 2911 -374 -589 1134 C ATOM 1613 N SER B 292 56.304 38.041 210.838 1.00 27.77 N ANISOU 1613 N SER B 292 2812 3200 4541 -417 -746 949 N ATOM 1614 CA SER B 292 55.834 37.198 211.933 1.00 33.56 C ANISOU 1614 CA SER B 292 3573 3890 5289 -440 -798 1002 C ATOM 1615 C SER B 292 56.873 37.066 213.041 1.00 38.13 C ANISOU 1615 C SER B 292 4175 4397 5915 -411 -814 991 C ATOM 1616 O SER B 292 56.510 36.839 214.200 1.00 36.86 O ANISOU 1616 O SER B 292 4030 4232 5741 -433 -840 1058 O ATOM 1617 CB SER B 292 55.437 35.819 211.405 1.00 20.93 C ANISOU 1617 CB SER B 292 1975 2273 3706 -491 -870 978 C ATOM 1618 OG SER B 292 56.508 35.214 210.706 1.00 27.95 O ANISOU 1618 OG SER B 292 2851 3118 4650 -474 -893 862 O ATOM 1619 N VAL B 293 58.159 37.185 212.714 1.00 43.63 N ANISOU 1619 N VAL B 293 4863 5058 6658 -374 -803 906 N ATOM 1620 CA VAL B 293 59.185 37.099 213.748 1.00 34.30 C ANISOU 1620 CA VAL B 293 3693 3818 5522 -357 -824 895 C ATOM 1621 C VAL B 293 59.334 38.431 214.475 1.00 33.70 C ANISOU 1621 C VAL B 293 3610 3791 5404 -343 -760 908 C ATOM 1622 O VAL B 293 59.543 38.467 215.694 1.00 28.25 O ANISOU 1622 O VAL B 293 2927 3102 4706 -359 -778 937 O ATOM 1623 CB VAL B 293 60.518 36.630 213.135 1.00 28.28 C ANISOU 1623 CB VAL B 293 2902 3012 4832 -318 -847 784 C ATOM 1624 CG1 VAL B 293 61.653 36.775 214.138 1.00 15.62 C ANISOU 1624 CG1 VAL B 293 1293 1374 3268 -299 -866 767 C ATOM 1625 CG2 VAL B 293 60.405 35.184 212.674 1.00 25.03 C ANISOU 1625 CG2 VAL B 293 2482 2507 4519 -331 -950 775 C ATOM 1626 N CYS B 294 59.205 39.544 213.751 1.00 29.22 N ANISOU 1626 N CYS B 294 3021 3271 4809 -321 -694 889 N ATOM 1627 CA CYS B 294 59.470 40.856 214.333 1.00 20.06 C ANISOU 1627 CA CYS B 294 1846 2139 3638 -301 -644 879 C ATOM 1628 C CYS B 294 58.279 41.402 215.115 1.00 26.43 C ANISOU 1628 C CYS B 294 2641 2992 4408 -315 -621 933 C ATOM 1629 O CYS B 294 58.461 41.998 216.183 1.00 14.53 O ANISOU 1629 O CYS B 294 1114 1516 2890 -314 -607 910 O ATOM 1630 CB CYS B 294 59.872 41.838 213.232 1.00 27.89 C ANISOU 1630 CB CYS B 294 2814 3148 4636 -276 -597 848 C ATOM 1631 SG CYS B 294 61.459 41.472 212.451 1.00 33.13 S ANISOU 1631 SG CYS B 294 3450 3810 5328 -254 -607 752 S ATOM 1632 N TRP B 295 57.058 41.221 214.605 1.00 31.80 N ANISOU 1632 N TRP B 295 3317 3698 5067 -332 -620 989 N ATOM 1633 CA TRP B 295 55.896 41.897 215.169 1.00 14.48 C ANISOU 1633 CA TRP B 295 1084 1562 2854 -338 -588 1020 C ATOM 1634 C TRP B 295 55.049 41.033 216.094 1.00 15.74 C ANISOU 1634 C TRP B 295 1236 1776 2969 -386 -619 1062 C ATOM 1635 O TRP B 295 54.319 41.587 216.924 1.00 15.33 O ANISOU 1635 O TRP B 295 1130 1796 2897 -401 -583 1051 O ATOM 1636 CB TRP B 295 55.009 42.447 214.048 1.00 14.64 C ANISOU 1636 CB TRP B 295 1081 1595 2888 -330 -565 1063 C ATOM 1637 CG TRP B 295 55.428 43.804 213.582 1.00 18.27 C ANISOU 1637 CG TRP B 295 1518 2026 3396 -293 -522 1046 C ATOM 1638 CD1 TRP B 295 56.121 44.106 212.447 1.00 16.57 C ANISOU 1638 CD1 TRP B 295 1316 1787 3194 -284 -522 1050 C ATOM 1639 CD2 TRP B 295 55.189 45.050 214.250 1.00 26.08 C ANISOU 1639 CD2 TRP B 295 2457 3014 4438 -267 -476 1018 C ATOM 1640 NE1 TRP B 295 56.325 45.463 212.363 1.00 14.55 N ANISOU 1640 NE1 TRP B 295 1030 1502 2997 -256 -487 1053 N ATOM 1641 CE2 TRP B 295 55.762 46.065 213.458 1.00 19.89 C ANISOU 1641 CE2 TRP B 295 1667 2178 3712 -242 -459 1026 C ATOM 1642 CE3 TRP B 295 54.543 45.404 215.439 1.00 18.23 C ANISOU 1642 CE3 TRP B 295 1407 2068 3452 -271 -444 974 C ATOM 1643 CZ2 TRP B 295 55.709 47.410 213.817 1.00 20.40 C ANISOU 1643 CZ2 TRP B 295 1680 2206 3864 -214 -419 1000 C ATOM 1644 CZ3 TRP B 295 54.492 46.739 215.793 1.00 15.63 C ANISOU 1644 CZ3 TRP B 295 1015 1721 3203 -243 -393 921 C ATOM 1645 CH2 TRP B 295 55.071 47.726 214.985 1.00 22.12 C ANISOU 1645 CH2 TRP B 295 1842 2459 4104 -211 -385 938 C ATOM 1646 N SER B 296 55.115 39.707 215.977 1.00 18.72 N ANISOU 1646 N SER B 296 1653 2122 3336 -419 -686 1101 N ATOM 1647 CA SER B 296 54.263 38.853 216.805 1.00 20.90 C ANISOU 1647 CA SER B 296 1922 2452 3568 -481 -729 1162 C ATOM 1648 C SER B 296 54.531 38.996 218.299 1.00 30.40 C ANISOU 1648 C SER B 296 3108 3714 4729 -515 -727 1157 C ATOM 1649 O SER B 296 53.556 39.104 219.065 1.00 31.59 O ANISOU 1649 O SER B 296 3209 3967 4825 -569 -702 1172 O ATOM 1650 CB SER B 296 54.399 37.393 216.359 1.00 20.53 C ANISOU 1650 CB SER B 296 1921 2337 3542 -510 -818 1202 C ATOM 1651 OG SER B 296 53.990 37.230 215.012 1.00 40.47 O ANISOU 1651 OG SER B 296 4445 4849 6085 -503 -817 1187 O ATOM 1652 N PRO B 297 55.780 38.991 218.792 1.00 33.69 N ANISOU 1652 N PRO B 297 3549 4088 5162 -502 -750 1130 N ATOM 1653 CA PRO B 297 55.969 39.066 220.253 1.00 31.19 C ANISOU 1653 CA PRO B 297 3204 3853 4793 -563 -772 1152 C ATOM 1654 C PRO B 297 55.404 40.328 220.881 1.00 25.44 C ANISOU 1654 C PRO B 297 2396 3247 4022 -570 -674 1057 C ATOM 1655 O PRO B 297 54.878 40.272 221.999 1.00 21.42 O ANISOU 1655 O PRO B 297 1835 2852 3453 -662 -678 1095 O ATOM 1656 CB PRO B 297 57.495 38.990 220.414 1.00 19.81 C ANISOU 1656 CB PRO B 297 1792 2337 3399 -539 -816 1130 C ATOM 1657 CG PRO B 297 57.973 38.310 219.188 1.00 24.41 C ANISOU 1657 CG PRO B 297 2425 2788 4062 -492 -838 1120 C ATOM 1658 CD PRO B 297 57.067 38.793 218.096 1.00 28.74 C ANISOU 1658 CD PRO B 297 2963 3351 4607 -456 -773 1093 C ATOM 1659 N LEU B 298 55.500 41.469 220.197 1.00 22.97 N ANISOU 1659 N LEU B 298 2058 2910 3760 -496 -601 965 N ATOM 1660 CA LEU B 298 55.019 42.718 220.779 1.00 30.77 C ANISOU 1660 CA LEU B 298 2955 3986 4751 -501 -511 859 C ATOM 1661 C LEU B 298 53.495 42.748 220.842 1.00 32.48 C ANISOU 1661 C LEU B 298 3108 4275 4957 -540 -457 871 C ATOM 1662 O LEU B 298 52.913 43.093 221.876 1.00 38.30 O ANISOU 1662 O LEU B 298 3760 5127 5665 -608 -395 804 O ATOM 1663 CB LEU B 298 55.549 43.909 219.981 1.00 30.25 C ANISOU 1663 CB LEU B 298 2880 3846 4768 -420 -471 797 C ATOM 1664 CG LEU B 298 54.988 45.269 220.401 1.00 20.07 C ANISOU 1664 CG LEU B 298 1488 2613 3523 -417 -379 686 C ATOM 1665 CD1 LEU B 298 55.515 45.660 221.770 1.00 17.09 C ANISOU 1665 CD1 LEU B 298 1049 2344 3100 -479 -351 560 C ATOM 1666 CD2 LEU B 298 55.310 46.335 219.367 1.00 16.16 C ANISOU 1666 CD2 LEU B 298 1000 2008 3130 -339 -359 681 C ATOM 1667 N LEU B 299 52.832 42.387 219.742 1.00 24.73 N ANISOU 1667 N LEU B 299 2154 3236 4006 -509 -478 951 N ATOM 1668 CA LEU B 299 51.373 42.418 219.714 1.00 17.75 C ANISOU 1668 CA LEU B 299 1200 2423 3121 -544 -433 966 C ATOM 1669 C LEU B 299 50.782 41.413 220.695 1.00 20.15 C ANISOU 1669 C LEU B 299 1493 2825 3338 -653 -447 1008 C ATOM 1670 O LEU B 299 49.791 41.706 221.374 1.00 24.21 O ANISOU 1670 O LEU B 299 1914 3448 3838 -713 -367 961 O ATOM 1671 CB LEU B 299 50.869 42.146 218.297 1.00 17.48 C ANISOU 1671 CB LEU B 299 1199 2320 3124 -504 -471 1052 C ATOM 1672 CG LEU B 299 51.360 43.105 217.208 1.00 16.87 C ANISOU 1672 CG LEU B 299 1138 2148 3125 -420 -459 1044 C ATOM 1673 CD1 LEU B 299 50.941 42.618 215.829 1.00 16.79 C ANISOU 1673 CD1 LEU B 299 1163 2095 3120 -414 -505 1133 C ATOM 1674 CD2 LEU B 299 50.868 44.522 217.458 1.00 17.44 C ANISOU 1674 CD2 LEU B 299 1112 2241 3274 -386 -377 973 C ATOM 1675 N ILE B 300 51.373 40.220 220.777 1.00 18.43 N ANISOU 1675 N ILE B 300 1365 2566 3073 -687 -545 1098 N ATOM 1676 CA ILE B 300 50.871 39.198 221.691 1.00 19.78 C ANISOU 1676 CA ILE B 300 1530 2819 3167 -815 -599 1214 C ATOM 1677 C ILE B 300 51.089 39.616 223.140 1.00 45.36 C ANISOU 1677 C ILE B 300 4710 6186 6340 -906 -566 1200 C ATOM 1678 O ILE B 300 50.204 39.450 223.989 1.00 50.57 O ANISOU 1678 O ILE B 300 5309 6983 6923 -1024 -524 1234 O ATOM 1679 CB ILE B 300 51.537 37.842 221.388 1.00 19.74 C ANISOU 1679 CB ILE B 300 1625 2714 3162 -831 -747 1345 C ATOM 1680 CG1 ILE B 300 51.036 37.279 220.056 1.00 34.67 C ANISOU 1680 CG1 ILE B 300 3549 4524 5099 -786 -771 1351 C ATOM 1681 CG2 ILE B 300 51.302 36.857 222.523 1.00 21.42 C ANISOU 1681 CG2 ILE B 300 1844 3008 3287 -980 -838 1492 C ATOM 1682 CD1 ILE B 300 51.738 36.006 219.631 1.00 19.39 C ANISOU 1682 CD1 ILE B 300 1691 2470 3206 -791 -910 1439 C ATOM 1683 N MET B 301 52.262 40.174 223.446 1.00 44.43 N ANISOU 1683 N MET B 301 4603 6041 6237 -868 -578 1146 N ATOM 1684 CA MET B 301 52.570 40.536 224.826 1.00 47.19 C ANISOU 1684 CA MET B 301 4894 6533 6502 -976 -562 1134 C ATOM 1685 C MET B 301 51.682 41.674 225.317 1.00 39.69 C ANISOU 1685 C MET B 301 3807 5705 5569 -1002 -399 982 C ATOM 1686 O MET B 301 51.315 41.714 226.498 1.00 26.04 O ANISOU 1686 O MET B 301 2010 4155 3728 -1142 -353 991 O ATOM 1687 CB MET B 301 54.049 40.903 224.952 1.00 40.37 C ANISOU 1687 CB MET B 301 4063 5613 5663 -926 -619 1093 C ATOM 1688 CG MET B 301 54.579 40.871 226.372 1.00 49.77 C ANISOU 1688 CG MET B 301 5227 6961 6724 -1069 -669 1139 C ATOM 1689 SD MET B 301 56.348 41.204 226.443 1.00 75.48 S ANISOU 1689 SD MET B 301 8519 10142 10018 -1002 -758 1091 S ATOM 1690 CE MET B 301 56.986 39.862 225.442 1.00 69.68 C ANISOU 1690 CE MET B 301 7916 9192 9367 -920 -889 1249 C ATOM 1691 N MET B 302 51.329 42.611 224.430 1.00 33.89 N ANISOU 1691 N MET B 302 3026 4887 4964 -881 -311 847 N ATOM 1692 CA MET B 302 50.400 43.669 224.814 1.00 32.28 C ANISOU 1692 CA MET B 302 2671 4770 4824 -894 -158 702 C ATOM 1693 C MET B 302 49.036 43.097 225.176 1.00 33.55 C ANISOU 1693 C MET B 302 2774 5043 4930 -987 -103 764 C ATOM 1694 O MET B 302 48.408 43.534 226.148 1.00 35.63 O ANISOU 1694 O MET B 302 2910 5455 5172 -1074 18 695 O ATOM 1695 CB MET B 302 50.267 44.696 223.690 1.00 28.78 C ANISOU 1695 CB MET B 302 2205 4216 4514 -754 -112 592 C ATOM 1696 CG MET B 302 51.523 45.510 223.432 1.00 36.45 C ANISOU 1696 CG MET B 302 3212 5107 5532 -679 -137 515 C ATOM 1697 SD MET B 302 51.256 46.823 222.223 1.00 38.41 S ANISOU 1697 SD MET B 302 3438 5259 5898 -545 -95 455 S ATOM 1698 CE MET B 302 50.181 47.916 223.149 1.00 33.20 C ANISOU 1698 CE MET B 302 2560 4746 5307 -588 53 315 C ATOM 1699 N LEU B 303 48.562 42.113 224.408 1.00 28.35 N ANISOU 1699 N LEU B 303 2199 4325 4248 -977 -182 889 N ATOM 1700 CA LEU B 303 47.284 41.483 224.719 1.00 25.01 C ANISOU 1700 CA LEU B 303 1726 4010 3768 -1076 -143 957 C ATOM 1701 C LEU B 303 47.328 40.779 226.071 1.00 26.71 C ANISOU 1701 C LEU B 303 1949 4394 3805 -1254 -160 1063 C ATOM 1702 O LEU B 303 46.333 40.765 226.804 1.00 28.59 O ANISOU 1702 O LEU B 303 2094 4794 3975 -1361 -59 1057 O ATOM 1703 CB LEU B 303 46.899 40.505 223.610 1.00 24.22 C ANISOU 1703 CB LEU B 303 1719 3811 3675 -1044 -245 1069 C ATOM 1704 CG LEU B 303 46.578 41.139 222.253 1.00 31.14 C ANISOU 1704 CG LEU B 303 2583 4579 4669 -908 -228 996 C ATOM 1705 CD1 LEU B 303 46.396 40.073 221.185 1.00 22.53 C ANISOU 1705 CD1 LEU B 303 1587 3411 3563 -899 -344 1124 C ATOM 1706 CD2 LEU B 303 45.340 42.019 222.352 1.00 24.32 C ANISOU 1706 CD2 LEU B 303 1559 3800 3882 -904 -97 892 C ATOM 1707 N LYS B 304 48.474 40.186 226.420 1.00 37.16 N ANISOU 1707 N LYS B 304 3383 5700 5037 -1296 -290 1168 N ATOM 1708 CA LYS B 304 48.588 39.506 227.707 1.00 33.40 C ANISOU 1708 CA LYS B 304 2933 5406 4352 -1488 -337 1297 C ATOM 1709 C LYS B 304 48.537 40.483 228.875 1.00 37.02 C ANISOU 1709 C LYS B 304 3277 6080 4711 -1579 -195 1169 C ATOM 1710 O LYS B 304 48.012 40.143 229.941 1.00 42.35 O ANISOU 1710 O LYS B 304 3927 6982 5183 -1758 -152 1224 O ATOM 1711 CB LYS B 304 49.882 38.692 227.768 1.00 31.21 C ANISOU 1711 CB LYS B 304 2789 5046 4025 -1507 -532 1449 C ATOM 1712 CG LYS B 304 49.886 37.437 226.912 1.00 35.40 C ANISOU 1712 CG LYS B 304 3427 5409 4615 -1470 -683 1597 C ATOM 1713 CD LYS B 304 51.112 36.588 227.215 1.00 48.73 C ANISOU 1713 CD LYS B 304 5219 7029 6267 -1510 -881 1760 C ATOM 1714 CE LYS B 304 51.084 35.270 226.459 1.00 54.86 C ANISOU 1714 CE LYS B 304 6077 7641 7126 -1486 -1038 1888 C ATOM 1715 NZ LYS B 304 52.278 34.432 226.766 1.00 56.95 N ANISOU 1715 NZ LYS B 304 6414 7818 7407 -1515 -1251 2041 N ATOM 1716 N MET B 305 49.070 41.692 228.699 1.00 45.60 N ANISOU 1716 N MET B 305 4291 7111 5924 -1469 -118 987 N ATOM 1717 CA MET B 305 49.096 42.651 229.798 1.00 52.54 C ANISOU 1717 CA MET B 305 5053 8198 6711 -1556 20 833 C ATOM 1718 C MET B 305 47.780 43.403 229.931 1.00 44.02 C ANISOU 1718 C MET B 305 3810 7202 5714 -1536 229 684 C ATOM 1719 O MET B 305 47.410 43.801 231.042 1.00 41.09 O ANISOU 1719 O MET B 305 3350 7082 5180 -1660 365 582 O ATOM 1720 CB MET B 305 50.253 43.633 229.612 1.00 52.11 C ANISOU 1720 CB MET B 305 4981 8044 6775 -1457 6 693 C ATOM 1721 CG MET B 305 51.625 42.996 229.747 1.00 56.33 C ANISOU 1721 CG MET B 305 5649 8545 7210 -1495 -187 821 C ATOM 1722 SD MET B 305 52.961 44.187 229.552 1.00 80.50 S ANISOU 1722 SD MET B 305 8677 11498 10412 -1386 -202 638 S ATOM 1723 CE MET B 305 52.729 44.661 227.843 1.00 74.96 C ANISOU 1723 CE MET B 305 7978 10479 10026 -1137 -171 571 C ATOM 1724 N ILE B 306 47.068 43.615 228.822 1.00 44.68 N ANISOU 1724 N ILE B 306 3849 7095 6033 -1385 259 656 N ATOM 1725 CA ILE B 306 45.760 44.258 228.891 1.00 40.98 C ANISOU 1725 CA ILE B 306 3208 6683 5679 -1354 439 543 C ATOM 1726 C ILE B 306 44.783 43.386 229.669 1.00 44.18 C ANISOU 1726 C ILE B 306 3604 7311 5869 -1522 483 641 C ATOM 1727 O ILE B 306 44.035 43.875 230.525 1.00 45.31 O ANISOU 1727 O ILE B 306 3613 7657 5944 -1587 655 531 O ATOM 1728 CB ILE B 306 45.242 44.564 227.473 1.00 40.52 C ANISOU 1728 CB ILE B 306 3121 6391 5882 -1184 425 507 C ATOM 1729 CG1 ILE B 306 46.131 45.608 226.797 1.00 29.32 C ANISOU 1729 CG1 ILE B 306 1698 4797 4646 -1040 407 373 C ATOM 1730 CG2 ILE B 306 43.796 45.037 227.521 1.00 39.96 C ANISOU 1730 CG2 ILE B 306 2866 6377 5940 -1161 585 428 C ATOM 1731 CD1 ILE B 306 45.893 45.734 225.312 1.00 27.70 C ANISOU 1731 CD1 ILE B 306 1546 4453 4526 -916 330 362 C ATOM 1732 N PHE B 307 44.780 42.086 229.393 1.00 44.20 N ANISOU 1732 N PHE B 307 3750 7285 5760 -1595 330 841 N ATOM 1733 CA PHE B 307 43.901 41.156 230.090 1.00 52.93 C ANISOU 1733 CA PHE B 307 4862 8584 6667 -1770 345 960 C ATOM 1734 C PHE B 307 44.677 40.335 231.116 1.00 58.25 C ANISOU 1734 C PHE B 307 5665 9421 7045 -1963 233 1104 C ATOM 1735 O PHE B 307 45.209 40.877 232.085 1.00 64.90 O ANISOU 1735 O PHE B 307 6482 10447 7728 -2049 295 1017 O ATOM 1736 CB PHE B 307 43.200 40.232 229.093 1.00 54.97 C ANISOU 1736 CB PHE B 307 5173 8699 7014 -1738 249 1088 C ATOM 1737 CG PHE B 307 42.593 40.953 227.925 1.00 55.15 C ANISOU 1737 CG PHE B 307 5098 8551 7305 -1558 308 971 C ATOM 1738 CD1 PHE B 307 41.460 41.732 228.087 1.00 62.07 C ANISOU 1738 CD1 PHE B 307 5781 9509 8295 -1531 488 842 C ATOM 1739 CD2 PHE B 307 43.152 40.847 226.662 1.00 50.74 C ANISOU 1739 CD2 PHE B 307 4640 7767 6872 -1422 181 991 C ATOM 1740 CE1 PHE B 307 40.899 42.398 227.014 1.00 60.10 C ANISOU 1740 CE1 PHE B 307 5437 9109 8288 -1379 520 745 C ATOM 1741 CE2 PHE B 307 42.596 41.509 225.584 1.00 54.23 C ANISOU 1741 CE2 PHE B 307 5007 8092 7507 -1284 217 892 C ATOM 1742 CZ PHE B 307 41.468 42.285 225.761 1.00 58.98 C ANISOU 1742 CZ PHE B 307 5414 8770 8224 -1267 376 772 C ATOM 1743 N LYS B 323 60.475 40.326 235.119 1.00 69.08 N ANISOU 1743 N LYS B 323 7792 10693 7761 -2060 -1425 1526 N ATOM 1744 CA LYS B 323 60.805 40.035 233.728 1.00 70.85 C ANISOU 1744 CA LYS B 323 8033 10554 8331 -1815 -1439 1536 C ATOM 1745 C LYS B 323 59.812 40.690 232.776 1.00 66.03 C ANISOU 1745 C LYS B 323 7349 9867 7873 -1732 -1266 1379 C ATOM 1746 O LYS B 323 60.068 40.796 231.577 1.00 63.11 O ANISOU 1746 O LYS B 323 6983 9234 7762 -1526 -1234 1312 O ATOM 1747 CB LYS B 323 60.839 38.525 233.483 1.00 72.27 C ANISOU 1747 CB LYS B 323 8310 10543 8607 -1809 -1567 1823 C ATOM 1748 CG LYS B 323 61.730 37.754 234.442 1.00 79.57 C ANISOU 1748 CG LYS B 323 9296 11505 9432 -1886 -1729 1992 C ATOM 1749 CD LYS B 323 61.877 36.307 234.002 1.00 75.10 C ANISOU 1749 CD LYS B 323 8796 10669 9069 -1842 -1844 2203 C ATOM 1750 CE LYS B 323 60.522 35.643 233.822 1.00 69.40 C ANISOU 1750 CE LYS B 323 8086 9944 8340 -1981 -1805 2343 C ATOM 1751 NZ LYS B 323 59.697 35.712 235.058 1.00 72.09 N ANISOU 1751 NZ LYS B 323 8414 10622 8354 -2249 -1780 2439 N ATOM 1752 N GLU B 324 58.671 41.122 233.320 1.00 69.60 N ANISOU 1752 N GLU B 324 7727 10557 8159 -1896 -1135 1308 N ATOM 1753 CA GLU B 324 57.643 41.741 232.489 1.00 69.25 C ANISOU 1753 CA GLU B 324 7600 10425 8285 -1804 -945 1155 C ATOM 1754 C GLU B 324 58.155 43.023 231.843 1.00 63.78 C ANISOU 1754 C GLU B 324 6838 9592 7803 -1630 -850 886 C ATOM 1755 O GLU B 324 57.875 43.291 230.669 1.00 68.30 O ANISOU 1755 O GLU B 324 7397 9933 8619 -1450 -775 826 O ATOM 1756 CB GLU B 324 56.392 42.015 233.323 1.00 68.64 C ANISOU 1756 CB GLU B 324 7439 10642 7998 -2008 -784 1094 C ATOM 1757 CG GLU B 324 55.154 42.331 232.504 1.00 66.96 C ANISOU 1757 CG GLU B 324 7160 10315 7967 -1898 -597 1004 C ATOM 1758 CD GLU B 324 53.894 42.360 233.346 1.00 80.43 C ANISOU 1758 CD GLU B 324 8796 12302 9463 -2082 -430 970 C ATOM 1759 OE1 GLU B 324 54.009 42.425 234.588 1.00 82.77 O ANISOU 1759 OE1 GLU B 324 9073 12916 9459 -2309 -414 948 O ATOM 1760 OE2 GLU B 324 52.787 42.310 232.767 1.00 82.81 O ANISOU 1760 OE2 GLU B 324 9061 12516 9886 -2000 -313 958 O ATOM 1761 N CYS B 325 58.906 43.830 232.596 1.00 66.50 N ANISOU 1761 N CYS B 325 7144 10079 8044 -1696 -858 723 N ATOM 1762 CA CYS B 325 59.523 45.016 232.014 1.00 63.65 C ANISOU 1762 CA CYS B 325 6724 9567 7895 -1552 -793 490 C ATOM 1763 C CYS B 325 60.625 44.647 231.030 1.00 63.87 C ANISOU 1763 C CYS B 325 6826 9322 8121 -1352 -911 567 C ATOM 1764 O CYS B 325 60.829 45.351 230.034 1.00 52.79 O ANISOU 1764 O CYS B 325 5390 7723 6947 -1195 -838 441 O ATOM 1765 CB CYS B 325 60.082 45.914 233.118 1.00 60.74 C ANISOU 1765 CB CYS B 325 6307 9424 7349 -1694 -777 282 C ATOM 1766 SG CYS B 325 58.839 46.638 234.212 1.00 64.20 S ANISOU 1766 SG CYS B 325 6631 10206 7557 -1923 -555 52 S ATOM 1767 N ASN B 326 61.338 43.548 231.289 1.00 62.78 N ANISOU 1767 N ASN B 326 6783 9176 7893 -1360 -1077 767 N ATOM 1768 CA ASN B 326 62.472 43.173 230.450 1.00 63.45 C ANISOU 1768 CA ASN B 326 6923 9038 8148 -1180 -1158 804 C ATOM 1769 C ASN B 326 62.015 42.668 229.085 1.00 56.08 C ANISOU 1769 C ASN B 326 6032 7876 7399 -1034 -1101 862 C ATOM 1770 O ASN B 326 62.513 43.121 228.048 1.00 55.85 O ANISOU 1770 O ASN B 326 6001 7691 7530 -884 -1041 751 O ATOM 1771 CB ASN B 326 63.317 42.116 231.159 1.00 66.83 C ANISOU 1771 CB ASN B 326 7425 9508 8460 -1228 -1335 994 C ATOM 1772 CG ASN B 326 64.467 41.622 230.305 1.00 71.76 C ANISOU 1772 CG ASN B 326 8086 9913 9267 -1049 -1396 1016 C ATOM 1773 OD1 ASN B 326 65.067 42.385 229.548 1.00 64.97 O ANISOU 1773 OD1 ASN B 326 7184 8960 8541 -925 -1327 846 O ATOM 1774 ND2 ASN B 326 64.776 40.336 230.417 1.00 81.77 N ANISOU 1774 ND2 ASN B 326 9424 11102 10543 -1050 -1515 1217 N ATOM 1775 N PHE B 327 61.072 41.722 229.067 1.00 52.58 N ANISOU 1775 N PHE B 327 5636 7431 6911 -1096 -1116 1037 N ATOM 1776 CA PHE B 327 60.641 41.128 227.804 1.00 41.15 C ANISOU 1776 CA PHE B 327 4242 5778 5614 -979 -1077 1093 C ATOM 1777 C PHE B 327 59.951 42.143 226.902 1.00 30.65 C ANISOU 1777 C PHE B 327 2861 4394 4392 -884 -914 920 C ATOM 1778 O PHE B 327 60.012 42.016 225.673 1.00 32.54 O ANISOU 1778 O PHE B 327 3147 4469 4748 -758 -874 902 O ATOM 1779 CB PHE B 327 59.715 39.940 228.068 1.00 42.91 C ANISOU 1779 CB PHE B 327 4517 6022 5766 -1095 -1136 1314 C ATOM 1780 CG PHE B 327 60.441 38.662 228.379 1.00 57.57 C ANISOU 1780 CG PHE B 327 6454 7795 7626 -1139 -1300 1513 C ATOM 1781 CD1 PHE B 327 60.868 37.828 227.358 1.00 63.33 C ANISOU 1781 CD1 PHE B 327 7242 8282 8539 -1033 -1333 1549 C ATOM 1782 CD2 PHE B 327 60.696 38.293 229.689 1.00 67.01 C ANISOU 1782 CD2 PHE B 327 7659 9153 8648 -1298 -1411 1644 C ATOM 1783 CE1 PHE B 327 61.536 36.651 227.639 1.00 65.88 C ANISOU 1783 CE1 PHE B 327 7611 8499 8921 -1073 -1474 1688 C ATOM 1784 CE2 PHE B 327 61.363 37.117 229.977 1.00 68.65 C ANISOU 1784 CE2 PHE B 327 7930 9254 8899 -1330 -1558 1815 C ATOM 1785 CZ PHE B 327 61.784 36.295 228.950 1.00 67.55 C ANISOU 1785 CZ PHE B 327 7829 8847 8989 -1210 -1589 1824 C ATOM 1786 N PHE B 328 59.294 43.148 227.482 1.00 24.30 N ANISOU 1786 N PHE B 328 1958 3725 3548 -955 -815 791 N ATOM 1787 CA PHE B 328 58.615 44.148 226.665 1.00 27.99 C ANISOU 1787 CA PHE B 328 2367 4120 4148 -865 -664 636 C ATOM 1788 C PHE B 328 59.607 45.033 225.918 1.00 29.80 C ANISOU 1788 C PHE B 328 2597 4237 4488 -744 -635 497 C ATOM 1789 O PHE B 328 59.296 45.529 224.828 1.00 21.73 O ANISOU 1789 O PHE B 328 1591 3111 3554 -646 -553 447 O ATOM 1790 CB PHE B 328 57.687 44.992 227.539 1.00 34.33 C ANISOU 1790 CB PHE B 328 3043 5082 4920 -979 -551 522 C ATOM 1791 CG PHE B 328 56.642 45.740 226.767 1.00 21.98 C ANISOU 1791 CG PHE B 328 1412 3440 3498 -898 -402 417 C ATOM 1792 CD1 PHE B 328 55.748 45.062 225.957 1.00 21.18 C ANISOU 1792 CD1 PHE B 328 1369 3270 3410 -844 -388 522 C ATOM 1793 CD2 PHE B 328 56.543 47.118 226.861 1.00 22.45 C ANISOU 1793 CD2 PHE B 328 1349 3501 3681 -887 -286 217 C ATOM 1794 CE1 PHE B 328 54.784 45.743 225.245 1.00 34.22 C ANISOU 1794 CE1 PHE B 328 2967 4873 5163 -775 -273 440 C ATOM 1795 CE2 PHE B 328 55.578 47.805 226.153 1.00 37.25 C ANISOU 1795 CE2 PHE B 328 3166 5330 5656 -818 -164 145 C ATOM 1796 CZ PHE B 328 54.697 47.117 225.344 1.00 36.75 C ANISOU 1796 CZ PHE B 328 3172 5212 5580 -759 -167 264 C ATOM 1797 N LEU B 329 60.800 45.241 226.481 1.00 31.58 N ANISOU 1797 N LEU B 329 2812 4504 4684 -766 -710 451 N ATOM 1798 CA LEU B 329 61.832 45.994 225.774 1.00 29.78 C ANISOU 1798 CA LEU B 329 2588 4191 4537 -671 -685 342 C ATOM 1799 C LEU B 329 62.372 45.207 224.586 1.00 18.50 C ANISOU 1799 C LEU B 329 1267 2622 3142 -556 -713 441 C ATOM 1800 O LEU B 329 62.614 45.776 223.515 1.00 30.38 O ANISOU 1800 O LEU B 329 2796 4041 4705 -475 -645 393 O ATOM 1801 CB LEU B 329 62.965 46.356 226.734 1.00 34.48 C ANISOU 1801 CB LEU B 329 3134 4881 5086 -735 -764 263 C ATOM 1802 CG LEU B 329 64.191 47.063 226.148 1.00 23.55 C ANISOU 1802 CG LEU B 329 1745 3445 3760 -665 -749 166 C ATOM 1803 CD1 LEU B 329 63.813 48.400 225.530 1.00 20.12 C ANISOU 1803 CD1 LEU B 329 1269 2971 3406 -654 -618 55 C ATOM 1804 CD2 LEU B 329 65.266 47.235 227.209 1.00 22.89 C ANISOU 1804 CD2 LEU B 329 1610 3470 3617 -737 -852 98 C ATOM 1805 N ILE B 330 62.572 43.899 224.758 1.00 24.91 N ANISOU 1805 N ILE B 330 2140 3410 3915 -566 -814 587 N ATOM 1806 CA ILE B 330 63.025 43.061 223.652 1.00 21.71 C ANISOU 1806 CA ILE B 330 1816 2865 3567 -480 -830 656 C ATOM 1807 C ILE B 330 61.992 43.055 222.532 1.00 25.32 C ANISOU 1807 C ILE B 330 2315 3242 4063 -438 -743 669 C ATOM 1808 O ILE B 330 62.341 43.062 221.345 1.00 20.82 O ANISOU 1808 O ILE B 330 1780 2562 3570 -378 -723 680 O ATOM 1809 CB ILE B 330 63.321 41.635 224.151 1.00 19.54 C ANISOU 1809 CB ILE B 330 1586 2561 3278 -521 -960 810 C ATOM 1810 CG1 ILE B 330 64.396 41.654 225.240 1.00 21.85 C ANISOU 1810 CG1 ILE B 330 1841 2945 3516 -558 -1064 809 C ATOM 1811 CG2 ILE B 330 63.751 40.744 222.999 1.00 18.12 C ANISOU 1811 CG2 ILE B 330 1466 2228 3192 -450 -968 842 C ATOM 1812 CD1 ILE B 330 64.708 40.283 225.806 1.00 21.56 C ANISOU 1812 CD1 ILE B 330 1848 2874 3469 -605 -1207 980 C ATOM 1813 N ALA B 331 60.706 43.063 222.893 1.00 22.95 N ANISOU 1813 N ALA B 331 1993 2995 3733 -491 -715 706 N ATOM 1814 CA ALA B 331 59.647 42.991 221.891 1.00 16.14 C ANISOU 1814 CA ALA B 331 1161 2072 2900 -456 -651 733 C ATOM 1815 C ALA B 331 59.602 44.252 221.036 1.00 15.65 C ANISOU 1815 C ALA B 331 1074 1964 2910 -396 -574 661 C ATOM 1816 O ALA B 331 59.487 44.175 219.807 1.00 25.40 O ANISOU 1816 O ALA B 331 2352 3099 4200 -348 -563 711 O ATOM 1817 CB ALA B 331 58.299 42.752 222.571 1.00 17.51 C ANISOU 1817 CB ALA B 331 1293 2333 3026 -535 -638 786 C ATOM 1818 N VAL B 332 59.688 45.426 221.666 1.00 16.06 N ANISOU 1818 N VAL B 332 1050 2088 2965 -413 -521 542 N ATOM 1819 CA VAL B 332 59.667 46.663 220.896 1.00 19.50 C ANISOU 1819 CA VAL B 332 1463 2457 3489 -363 -460 496 C ATOM 1820 C VAL B 332 60.939 46.822 220.074 1.00 26.12 C ANISOU 1820 C VAL B 332 2346 3203 4377 -315 -490 510 C ATOM 1821 O VAL B 332 60.927 47.514 219.049 1.00 37.03 O ANISOU 1821 O VAL B 332 3738 4495 5835 -273 -459 530 O ATOM 1822 CB VAL B 332 59.445 47.880 221.816 1.00 26.67 C ANISOU 1822 CB VAL B 332 2270 3458 4405 -408 -392 355 C ATOM 1823 CG1 VAL B 332 60.725 48.251 222.555 1.00 17.08 C ANISOU 1823 CG1 VAL B 332 1027 2305 3157 -447 -421 262 C ATOM 1824 CG2 VAL B 332 58.913 49.060 221.019 1.00 24.86 C ANISOU 1824 CG2 VAL B 332 2015 3133 4298 -355 -330 350 C ATOM 1825 N ARG B 333 62.039 46.189 220.489 1.00 23.86 N ANISOU 1825 N ARG B 333 2075 2941 4052 -327 -551 505 N ATOM 1826 CA ARG B 333 63.244 46.190 219.669 1.00 20.79 C ANISOU 1826 CA ARG B 333 1711 2479 3709 -288 -572 510 C ATOM 1827 C ARG B 333 63.136 45.204 218.513 1.00 29.69 C ANISOU 1827 C ARG B 333 2902 3521 4859 -262 -587 595 C ATOM 1828 O ARG B 333 63.708 45.444 217.443 1.00 14.66 O ANISOU 1828 O ARG B 333 1005 1564 2999 -236 -570 593 O ATOM 1829 CB ARG B 333 64.471 45.875 220.528 1.00 16.42 C ANISOU 1829 CB ARG B 333 1130 1990 3117 -307 -635 466 C ATOM 1830 CG ARG B 333 64.943 47.042 221.385 1.00 19.99 C ANISOU 1830 CG ARG B 333 1508 2533 3556 -346 -618 353 C ATOM 1831 CD ARG B 333 66.456 47.022 221.558 1.00 28.26 C ANISOU 1831 CD ARG B 333 2526 3610 4603 -343 -673 316 C ATOM 1832 NE ARG B 333 66.887 46.374 222.794 1.00 34.14 N ANISOU 1832 NE ARG B 333 3242 4466 5263 -384 -756 303 N ATOM 1833 CZ ARG B 333 67.393 47.025 223.837 1.00 39.17 C ANISOU 1833 CZ ARG B 333 3807 5232 5845 -448 -777 200 C ATOM 1834 NH1 ARG B 333 67.540 48.343 223.792 1.00 35.72 N ANISOU 1834 NH1 ARG B 333 3320 4816 5436 -487 -712 100 N ATOM 1835 NH2 ARG B 333 67.762 46.358 224.923 1.00 37.86 N ANISOU 1835 NH2 ARG B 333 3618 5163 5603 -486 -877 209 N ATOM 1836 N LEU B 334 62.403 44.104 218.703 1.00 37.14 N ANISOU 1836 N LEU B 334 3879 4463 5768 -282 -618 661 N ATOM 1837 CA LEU B 334 62.151 43.186 217.597 1.00 14.46 C ANISOU 1837 CA LEU B 334 1054 1518 2922 -272 -628 720 C ATOM 1838 C LEU B 334 61.186 43.795 216.589 1.00 14.09 C ANISOU 1838 C LEU B 334 1013 1450 2891 -259 -574 750 C ATOM 1839 O LEU B 334 61.331 43.588 215.379 1.00 13.91 O ANISOU 1839 O LEU B 334 1005 1392 2889 -247 -567 763 O ATOM 1840 CB LEU B 334 61.610 41.859 218.128 1.00 14.71 C ANISOU 1840 CB LEU B 334 1115 1546 2927 -309 -685 788 C ATOM 1841 CG LEU B 334 62.596 40.991 218.911 1.00 18.15 C ANISOU 1841 CG LEU B 334 1550 1976 3369 -324 -766 790 C ATOM 1842 CD1 LEU B 334 61.907 39.751 219.456 1.00 15.79 C ANISOU 1842 CD1 LEU B 334 1283 1661 3054 -377 -830 884 C ATOM 1843 CD2 LEU B 334 63.782 40.608 218.037 1.00 23.82 C ANISOU 1843 CD2 LEU B 334 2262 2630 4159 -282 -785 739 C ATOM 1844 N ALA B 335 60.194 44.550 217.067 1.00 35.48 N ANISOU 1844 N ALA B 335 3693 4195 5590 -264 -538 754 N ATOM 1845 CA ALA B 335 59.291 45.246 216.155 1.00 22.90 C ANISOU 1845 CA ALA B 335 2092 2577 4032 -247 -498 793 C ATOM 1846 C ALA B 335 60.031 46.312 215.358 1.00 15.74 C ANISOU 1846 C ALA B 335 1171 1625 3183 -221 -473 774 C ATOM 1847 O ALA B 335 59.760 46.506 214.167 1.00 17.53 O ANISOU 1847 O ALA B 335 1407 1827 3428 -215 -465 831 O ATOM 1848 CB ALA B 335 58.130 45.865 216.933 1.00 16.14 C ANISOU 1848 CB ALA B 335 1182 1770 3179 -254 -462 780 C ATOM 1849 N SER B 336 60.968 47.015 216.000 1.00 21.95 N ANISOU 1849 N SER B 336 1929 2418 3992 -215 -466 699 N ATOM 1850 CA SER B 336 61.762 48.015 215.296 1.00 22.70 C ANISOU 1850 CA SER B 336 2004 2473 4146 -200 -448 686 C ATOM 1851 C SER B 336 62.672 47.378 214.254 1.00 33.21 C ANISOU 1851 C SER B 336 3357 3808 5455 -201 -467 702 C ATOM 1852 O SER B 336 63.023 48.026 213.261 1.00 27.94 O ANISOU 1852 O SER B 336 2670 3129 4815 -199 -452 728 O ATOM 1853 CB SER B 336 62.583 48.828 216.297 1.00 14.88 C ANISOU 1853 CB SER B 336 968 1504 3183 -205 -442 591 C ATOM 1854 OG SER B 336 61.743 49.500 217.220 1.00 15.26 O ANISOU 1854 OG SER B 336 971 1571 3256 -213 -412 544 O ATOM 1855 N LEU B 337 63.061 46.116 214.464 1.00 14.15 N ANISOU 1855 N LEU B 337 966 1416 2995 -208 -500 682 N ATOM 1856 CA LEU B 337 63.913 45.419 213.505 1.00 14.23 C ANISOU 1856 CA LEU B 337 969 1442 2995 -206 -513 661 C ATOM 1857 C LEU B 337 63.228 45.258 212.155 1.00 31.43 C ANISOU 1857 C LEU B 337 3153 3635 5154 -215 -499 715 C ATOM 1858 O LEU B 337 63.903 45.198 211.121 1.00 26.26 O ANISOU 1858 O LEU B 337 2464 3029 4486 -218 -491 689 O ATOM 1859 CB LEU B 337 64.309 44.049 214.060 1.00 14.31 C ANISOU 1859 CB LEU B 337 993 1451 2995 -205 -562 630 C ATOM 1860 CG LEU B 337 65.357 43.230 213.304 1.00 14.69 C ANISOU 1860 CG LEU B 337 1006 1519 3057 -188 -582 569 C ATOM 1861 CD1 LEU B 337 66.715 43.926 213.309 1.00 15.15 C ANISOU 1861 CD1 LEU B 337 1005 1620 3133 -173 -571 505 C ATOM 1862 CD2 LEU B 337 65.459 41.835 213.899 1.00 14.97 C ANISOU 1862 CD2 LEU B 337 1056 1517 3114 -183 -646 560 C ATOM 1863 N ASN B 338 61.893 45.185 212.144 1.00 34.10 N ANISOU 1863 N ASN B 338 3519 3958 5480 -225 -498 785 N ATOM 1864 CA ASN B 338 61.165 45.033 210.887 1.00 32.57 C ANISOU 1864 CA ASN B 338 3321 3799 5256 -242 -496 844 C ATOM 1865 C ASN B 338 61.420 46.213 209.958 1.00 22.95 C ANISOU 1865 C ASN B 338 2066 2603 4053 -245 -474 887 C ATOM 1866 O ASN B 338 61.577 46.035 208.744 1.00 19.12 O ANISOU 1866 O ASN B 338 1551 2192 3522 -268 -477 899 O ATOM 1867 CB ASN B 338 59.670 44.874 211.164 1.00 26.81 C ANISOU 1867 CB ASN B 338 2613 3056 4519 -252 -503 917 C ATOM 1868 CG ASN B 338 58.862 44.652 209.899 1.00 22.84 C ANISOU 1868 CG ASN B 338 2098 2605 3976 -279 -515 982 C ATOM 1869 OD1 ASN B 338 58.781 43.535 209.387 1.00 23.46 O ANISOU 1869 OD1 ASN B 338 2180 2724 4010 -302 -541 953 O ATOM 1870 ND2 ASN B 338 58.253 45.718 209.392 1.00 24.80 N ANISOU 1870 ND2 ASN B 338 2321 2854 4247 -280 -503 1070 N ATOM 1871 N GLN B 339 61.459 47.427 210.509 1.00 26.32 N ANISOU 1871 N GLN B 339 2481 2975 4545 -227 -457 909 N ATOM 1872 CA GLN B 339 61.757 48.605 209.704 1.00 28.84 C ANISOU 1872 CA GLN B 339 2758 3295 4903 -232 -447 968 C ATOM 1873 C GLN B 339 63.221 48.662 209.289 1.00 27.30 C ANISOU 1873 C GLN B 339 2527 3157 4689 -244 -439 903 C ATOM 1874 O GLN B 339 63.564 49.418 208.373 1.00 28.82 O ANISOU 1874 O GLN B 339 2675 3387 4887 -265 -434 958 O ATOM 1875 CB GLN B 339 61.375 49.876 210.467 1.00 33.80 C ANISOU 1875 CB GLN B 339 3370 3832 5642 -207 -434 992 C ATOM 1876 CG GLN B 339 59.874 50.138 210.537 1.00 30.09 C ANISOU 1876 CG GLN B 339 2897 3319 5215 -198 -434 1072 C ATOM 1877 CD GLN B 339 59.140 49.144 211.419 1.00 30.69 C ANISOU 1877 CD GLN B 339 3005 3414 5242 -198 -433 1024 C ATOM 1878 OE1 GLN B 339 58.174 48.513 210.990 1.00 35.05 O ANISOU 1878 OE1 GLN B 339 3569 3999 5751 -213 -446 1084 O ATOM 1879 NE2 GLN B 339 59.598 49.000 212.658 1.00 23.32 N ANISOU 1879 NE2 GLN B 339 2076 2476 4307 -188 -423 921 N ATOM 1880 N ILE B 340 64.089 47.886 209.941 1.00 21.62 N ANISOU 1880 N ILE B 340 1812 2453 3950 -235 -441 794 N ATOM 1881 CA ILE B 340 65.480 47.800 209.510 1.00 22.74 C ANISOU 1881 CA ILE B 340 1898 2668 4074 -246 -431 718 C ATOM 1882 C ILE B 340 65.621 46.827 208.346 1.00 15.82 C ANISOU 1882 C ILE B 340 987 1900 3125 -266 -429 682 C ATOM 1883 O ILE B 340 66.383 47.072 207.405 1.00 16.50 O ANISOU 1883 O ILE B 340 1000 2089 3180 -297 -408 653 O ATOM 1884 CB ILE B 340 66.380 47.398 210.695 1.00 28.90 C ANISOU 1884 CB ILE B 340 2677 3429 4875 -224 -445 621 C ATOM 1885 CG1 ILE B 340 66.249 48.405 211.840 1.00 34.54 C ANISOU 1885 CG1 ILE B 340 3404 4070 5648 -218 -444 627 C ATOM 1886 CG2 ILE B 340 67.834 47.274 210.251 1.00 25.84 C ANISOU 1886 CG2 ILE B 340 2210 3131 4477 -232 -436 537 C ATOM 1887 CD1 ILE B 340 66.968 47.988 213.108 1.00 15.49 C ANISOU 1887 CD1 ILE B 340 986 1663 3236 -208 -471 545 C ATOM 1888 N LEU B 341 64.881 45.718 208.386 1.00 24.40 N ANISOU 1888 N LEU B 341 2110 2978 4183 -259 -451 670 N ATOM 1889 CA LEU B 341 64.959 44.694 207.352 1.00 27.38 C ANISOU 1889 CA LEU B 341 2441 3460 4503 -279 -454 602 C ATOM 1890 C LEU B 341 64.111 45.006 206.125 1.00 28.38 C ANISOU 1890 C LEU B 341 2550 3665 4567 -329 -449 679 C ATOM 1891 O LEU B 341 64.224 44.289 205.124 1.00 35.47 O ANISOU 1891 O LEU B 341 3388 4682 5407 -365 -445 601 O ATOM 1892 CB LEU B 341 64.537 43.338 207.926 1.00 15.47 C ANISOU 1892 CB LEU B 341 972 1899 3007 -256 -491 558 C ATOM 1893 CG LEU B 341 65.305 42.836 209.151 1.00 15.34 C ANISOU 1893 CG LEU B 341 972 1805 3052 -214 -517 504 C ATOM 1894 CD1 LEU B 341 64.858 41.431 209.526 1.00 15.30 C ANISOU 1894 CD1 LEU B 341 998 1744 3071 -202 -568 482 C ATOM 1895 CD2 LEU B 341 66.809 42.879 208.915 1.00 16.00 C ANISOU 1895 CD2 LEU B 341 970 1963 3147 -193 -505 405 C ATOM 1896 N ASP B 342 63.273 46.045 206.175 1.00 16.10 N ANISOU 1896 N ASP B 342 1032 2054 3031 -335 -453 822 N ATOM 1897 CA ASP B 342 62.375 46.335 205.057 1.00 20.07 C ANISOU 1897 CA ASP B 342 1519 2630 3478 -383 -467 930 C ATOM 1898 C ASP B 342 63.100 46.599 203.740 1.00 29.46 C ANISOU 1898 C ASP B 342 2624 3972 4598 -445 -449 913 C ATOM 1899 O ASP B 342 62.718 45.992 202.724 1.00 27.90 O ANISOU 1899 O ASP B 342 2391 3894 4317 -502 -458 893 O ATOM 1900 CB ASP B 342 61.453 47.502 205.422 1.00 28.12 C ANISOU 1900 CB ASP B 342 2572 3550 4561 -364 -482 1092 C ATOM 1901 CG ASP B 342 60.184 47.047 206.116 1.00 40.95 C ANISOU 1901 CG ASP B 342 4252 5100 6209 -344 -499 1128 C ATOM 1902 OD1 ASP B 342 59.608 46.025 205.687 1.00 48.67 O ANISOU 1902 OD1 ASP B 342 5233 6140 7119 -373 -518 1104 O ATOM 1903 OD2 ASP B 342 59.761 47.711 207.085 1.00 51.26 O ANISOU 1903 OD2 ASP B 342 5581 6294 7600 -306 -492 1165 O ATOM 1904 N PRO B 343 64.115 47.469 203.664 1.00 28.36 N ANISOU 1904 N PRO B 343 2442 3849 4485 -453 -423 914 N ATOM 1905 CA PRO B 343 64.746 47.716 202.357 1.00 29.66 C ANISOU 1905 CA PRO B 343 2517 4178 4575 -534 -399 908 C ATOM 1906 C PRO B 343 65.434 46.494 201.777 1.00 32.63 C ANISOU 1906 C PRO B 343 2815 4684 4900 -564 -364 701 C ATOM 1907 O PRO B 343 65.612 46.422 200.555 1.00 31.75 O ANISOU 1907 O PRO B 343 2628 4721 4713 -647 -341 684 O ATOM 1908 CB PRO B 343 65.752 48.835 202.658 1.00 19.64 C ANISOU 1908 CB PRO B 343 1217 2875 3369 -534 -376 935 C ATOM 1909 CG PRO B 343 66.056 48.679 204.100 1.00 18.63 C ANISOU 1909 CG PRO B 343 1140 2608 3329 -454 -376 857 C ATOM 1910 CD PRO B 343 64.769 48.250 204.730 1.00 17.72 C ANISOU 1910 CD PRO B 343 1113 2386 3233 -406 -412 912 C ATOM 1911 N TRP B 344 65.822 45.528 202.612 1.00 24.12 N ANISOU 1911 N TRP B 344 1743 3553 3869 -500 -362 547 N ATOM 1912 CA TRP B 344 66.502 44.340 202.109 1.00 19.55 C ANISOU 1912 CA TRP B 344 1063 3085 3280 -510 -337 327 C ATOM 1913 C TRP B 344 65.515 43.311 201.572 1.00 24.80 C ANISOU 1913 C TRP B 344 1733 3779 3910 -537 -368 281 C ATOM 1914 O TRP B 344 65.741 42.729 200.506 1.00 26.21 O ANISOU 1914 O TRP B 344 1811 4063 4086 -594 -347 150 O ATOM 1915 CB TRP B 344 67.368 43.726 203.210 1.00 24.84 C ANISOU 1915 CB TRP B 344 1726 3711 4002 -429 -344 214 C ATOM 1916 CG TRP B 344 68.347 44.692 203.806 1.00 23.32 C ANISOU 1916 CG TRP B 344 1524 3486 3849 -409 -323 249 C ATOM 1917 CD1 TRP B 344 68.171 45.452 204.925 1.00 29.85 C ANISOU 1917 CD1 TRP B 344 2448 4159 4733 -369 -348 371 C ATOM 1918 CD2 TRP B 344 69.650 45.010 203.306 1.00 20.25 C ANISOU 1918 CD2 TRP B 344 1008 3228 3460 -442 -269 140 C ATOM 1919 NE1 TRP B 344 69.287 46.219 205.157 1.00 25.52 N ANISOU 1919 NE1 TRP B 344 1846 3636 4214 -377 -323 350 N ATOM 1920 CE2 TRP B 344 70.210 45.967 204.176 1.00 26.29 C ANISOU 1920 CE2 TRP B 344 1808 3910 4272 -422 -274 220 C ATOM 1921 CE3 TRP B 344 70.401 44.575 202.209 1.00 21.58 C ANISOU 1921 CE3 TRP B 344 1021 3553 3627 -489 -210 -41 C ATOM 1922 CZ2 TRP B 344 71.484 46.497 203.982 1.00 30.78 C ANISOU 1922 CZ2 TRP B 344 2268 4576 4852 -455 -230 149 C ATOM 1923 CZ3 TRP B 344 71.664 45.105 202.017 1.00 22.62 C ANISOU 1923 CZ3 TRP B 344 1074 3729 3792 -504 -155 -102 C ATOM 1924 CH2 TRP B 344 72.193 46.055 202.899 1.00 24.80 C ANISOU 1924 CH2 TRP B 344 1360 3985 4078 -502 -168 -15 C ATOM 1925 N VAL B 345 64.408 43.085 202.287 1.00 23.68 N ANISOU 1925 N VAL B 345 1700 3526 3770 -504 -417 387 N ATOM 1926 CA VAL B 345 63.458 42.060 201.874 1.00 18.87 C ANISOU 1926 CA VAL B 345 1097 2941 3132 -537 -452 341 C ATOM 1927 C VAL B 345 62.710 42.442 200.604 1.00 45.50 C ANISOU 1927 C VAL B 345 4448 6421 6417 -632 -460 433 C ATOM 1928 O VAL B 345 62.154 41.565 199.933 1.00 50.04 O ANISOU 1928 O VAL B 345 4995 7057 6962 -689 -486 357 O ATOM 1929 CB VAL B 345 62.462 41.753 203.009 1.00 17.84 C ANISOU 1929 CB VAL B 345 1084 2659 3038 -487 -497 446 C ATOM 1930 CG1 VAL B 345 63.181 41.150 204.199 1.00 38.47 C ANISOU 1930 CG1 VAL B 345 3721 5168 5727 -410 -507 377 C ATOM 1931 CG2 VAL B 345 61.720 43.007 203.420 1.00 24.89 C ANISOU 1931 CG2 VAL B 345 2055 3468 3935 -474 -503 661 C ATOM 1932 N TYR B 346 62.678 43.725 200.245 1.00 35.73 N ANISOU 1932 N TYR B 346 3225 5217 5132 -661 -451 613 N ATOM 1933 CA TYR B 346 61.946 44.165 199.063 1.00 32.79 C ANISOU 1933 CA TYR B 346 2841 4976 4644 -758 -475 755 C ATOM 1934 C TYR B 346 62.842 44.496 197.876 1.00 42.91 C ANISOU 1934 C TYR B 346 4023 6441 5838 -857 -438 745 C ATOM 1935 O TYR B 346 62.531 44.098 196.749 1.00 57.32 O ANISOU 1935 O TYR B 346 5796 8461 7520 -981 -460 776 O ATOM 1936 CB TYR B 346 61.076 45.383 199.399 1.00 33.66 C ANISOU 1936 CB TYR B 346 3022 5011 4758 -736 -516 1017 C ATOM 1937 CG TYR B 346 59.829 45.041 200.191 1.00 43.30 C ANISOU 1937 CG TYR B 346 4318 6109 6023 -687 -558 1081 C ATOM 1938 CD1 TYR B 346 58.700 44.535 199.559 1.00 33.46 C ANISOU 1938 CD1 TYR B 346 3073 4940 4700 -750 -602 1132 C ATOM 1939 CD2 TYR B 346 59.780 45.228 201.567 1.00 35.87 C ANISOU 1939 CD2 TYR B 346 3442 4989 5198 -591 -550 1088 C ATOM 1940 CE1 TYR B 346 57.562 44.221 200.275 1.00 22.76 C ANISOU 1940 CE1 TYR B 346 1773 3483 3391 -716 -632 1188 C ATOM 1941 CE2 TYR B 346 58.644 44.915 202.292 1.00 20.98 C ANISOU 1941 CE2 TYR B 346 1613 3006 3351 -560 -576 1143 C ATOM 1942 CZ TYR B 346 57.539 44.413 201.640 1.00 21.60 C ANISOU 1942 CZ TYR B 346 1685 3161 3361 -621 -615 1194 C ATOM 1943 OH TYR B 346 56.406 44.101 202.356 1.00 27.94 O ANISOU 1943 OH TYR B 346 2531 3880 4205 -598 -637 1246 O ATOM 1944 N LEU B 347 63.943 45.218 198.085 1.00 38.74 N ANISOU 1944 N LEU B 347 3535 5889 5296 -1364 -678 -570 N ATOM 1945 CA LEU B 347 64.741 45.710 196.968 1.00 32.56 C ANISOU 1945 CA LEU B 347 2838 5167 4368 -1362 -713 -613 C ATOM 1946 C LEU B 347 66.183 45.226 196.983 1.00 31.33 C ANISOU 1946 C LEU B 347 2784 4960 4162 -1362 -650 -653 C ATOM 1947 O LEU B 347 66.679 44.747 195.955 1.00 32.05 O ANISOU 1947 O LEU B 347 2914 5077 4185 -1392 -672 -723 O ATOM 1948 CB LEU B 347 64.710 47.247 196.944 1.00 34.06 C ANISOU 1948 CB LEU B 347 3041 5442 4458 -1316 -736 -551 C ATOM 1949 CG LEU B 347 65.357 47.910 195.727 1.00 35.95 C ANISOU 1949 CG LEU B 347 3353 5760 4549 -1315 -780 -572 C ATOM 1950 CD1 LEU B 347 64.684 47.451 194.444 1.00 29.30 C ANISOU 1950 CD1 LEU B 347 2471 4976 3687 -1354 -863 -633 C ATOM 1951 CD2 LEU B 347 65.299 49.423 195.852 1.00 33.70 C ANISOU 1951 CD2 LEU B 347 3085 5544 4176 -1273 -806 -493 C ATOM 1952 N LEU B 348 66.875 45.331 198.118 1.00 28.38 N ANISOU 1952 N LEU B 348 2446 4521 3814 -1330 -572 -610 N ATOM 1953 CA LEU B 348 68.329 45.206 198.109 1.00 25.23 C ANISOU 1953 CA LEU B 348 2139 4101 3348 -1321 -517 -628 C ATOM 1954 C LEU B 348 68.801 43.766 197.945 1.00 25.58 C ANISOU 1954 C LEU B 348 2196 4090 3432 -1355 -481 -701 C ATOM 1955 O LEU B 348 69.838 43.533 197.317 1.00 25.51 O ANISOU 1955 O LEU B 348 2241 4110 3340 -1365 -460 -748 O ATOM 1956 CB LEU B 348 68.914 45.814 199.384 1.00 27.32 C ANISOU 1956 CB LEU B 348 2439 4315 3626 -1278 -459 -558 C ATOM 1957 CG LEU B 348 68.657 47.310 199.590 1.00 34.59 C ANISOU 1957 CG LEU B 348 3367 5291 4483 -1251 -496 -491 C ATOM 1958 CD1 LEU B 348 69.290 47.802 200.883 1.00 32.86 C ANISOU 1958 CD1 LEU B 348 3195 5016 4275 -1221 -448 -433 C ATOM 1959 CD2 LEU B 348 69.164 48.116 198.401 1.00 23.85 C ANISOU 1959 CD2 LEU B 348 2054 4018 2990 -1258 -546 -492 C ATOM 1960 N LEU B 349 68.074 42.792 198.498 1.00 29.41 N ANISOU 1960 N LEU B 349 2630 4506 4040 -1377 -471 -709 N ATOM 1961 CA LEU B 349 68.468 41.398 198.310 1.00 26.58 C ANISOU 1961 CA LEU B 349 2289 4093 3715 -1418 -444 -784 C ATOM 1962 C LEU B 349 68.291 40.952 196.864 1.00 29.87 C ANISOU 1962 C LEU B 349 2712 4567 4070 -1470 -515 -880 C ATOM 1963 O LEU B 349 69.083 40.145 196.366 1.00 28.23 O ANISOU 1963 O LEU B 349 2551 4356 3819 -1495 -489 -966 O ATOM 1964 CB LEU B 349 67.673 40.487 199.245 1.00 47.88 C ANISOU 1964 CB LEU B 349 4931 6703 6560 -1438 -424 -755 C ATOM 1965 CG LEU B 349 68.060 40.495 200.725 1.00 43.74 C ANISOU 1965 CG LEU B 349 4415 6108 6095 -1392 -336 -680 C ATOM 1966 CD1 LEU B 349 67.169 39.545 201.511 1.00 26.44 C ANISOU 1966 CD1 LEU B 349 2156 3847 4041 -1422 -319 -644 C ATOM 1967 CD2 LEU B 349 69.527 40.131 200.902 1.00 37.62 C ANISOU 1967 CD2 LEU B 349 3723 5307 5265 -1371 -264 -714 C ATOM 1968 N ARG B 350 67.260 41.455 196.180 1.00 35.25 N ANISOU 1968 N ARG B 350 3344 5308 4743 -1487 -605 -875 N ATOM 1969 CA ARG B 350 67.088 41.135 194.766 1.00 42.97 C ANISOU 1969 CA ARG B 350 4334 6348 5646 -1533 -685 -966 C ATOM 1970 C ARG B 350 68.225 41.707 193.928 1.00 38.48 C ANISOU 1970 C ARG B 350 3836 5869 4917 -1511 -666 -1000 C ATOM 1971 O ARG B 350 68.664 41.081 192.957 1.00 39.03 O ANISOU 1971 O ARG B 350 3945 5974 4912 -1544 -685 -1100 O ATOM 1972 CB ARG B 350 65.744 41.662 194.263 1.00 52.75 C ANISOU 1972 CB ARG B 350 5499 7638 6907 -1549 -790 -940 C ATOM 1973 CG ARG B 350 64.543 40.803 194.623 1.00 66.34 C ANISOU 1973 CG ARG B 350 7136 9292 8780 -1604 -839 -932 C ATOM 1974 CD ARG B 350 63.255 41.459 194.145 1.00 76.42 C ANISOU 1974 CD ARG B 350 8322 10638 10077 -1614 -940 -896 C ATOM 1975 NE ARG B 350 62.087 40.601 194.327 1.00 84.30 N ANISOU 1975 NE ARG B 350 9224 11581 11224 -1681 -1004 -886 N ATOM 1976 CZ ARG B 350 61.614 39.780 193.394 1.00 91.29 C ANISOU 1976 CZ ARG B 350 10105 12459 12124 -1759 -1110 -963 C ATOM 1977 NH1 ARG B 350 62.209 39.706 192.211 1.00 93.12 N ANISOU 1977 NH1 ARG B 350 10426 12738 12218 -1769 -1156 -1063 N ATOM 1978 NH2 ARG B 350 60.545 39.036 193.641 1.00 94.50 N ANISOU 1978 NH2 ARG B 350 10416 12810 12681 -1828 -1175 -937 N ATOM 1979 N LYS B 351 68.714 42.895 194.291 1.00 39.48 N ANISOU 1979 N LYS B 351 3979 6035 4987 -1459 -632 -918 N ATOM 1980 CA LYS B 351 69.776 43.527 193.514 1.00 34.00 C ANISOU 1980 CA LYS B 351 3339 5434 4145 -1447 -617 -926 C ATOM 1981 C LYS B 351 71.095 42.778 193.664 1.00 38.17 C ANISOU 1981 C LYS B 351 3913 5946 4645 -1455 -531 -974 C ATOM 1982 O LYS B 351 71.841 42.626 192.690 1.00 46.64 O ANISOU 1982 O LYS B 351 5015 7105 5602 -1474 -527 -1038 O ATOM 1983 CB LYS B 351 69.932 44.987 193.936 1.00 27.33 C ANISOU 1983 CB LYS B 351 2503 4622 3260 -1401 -612 -816 C ATOM 1984 CG LYS B 351 70.952 45.765 193.124 1.00 31.93 C ANISOU 1984 CG LYS B 351 3131 5308 3694 -1397 -607 -798 C ATOM 1985 CD LYS B 351 70.521 45.891 191.673 1.00 36.70 C ANISOU 1985 CD LYS B 351 3727 6019 4197 -1418 -684 -849 C ATOM 1986 CE LYS B 351 71.643 46.451 190.814 1.00 46.81 C ANISOU 1986 CE LYS B 351 5048 7414 5325 -1422 -667 -835 C ATOM 1987 NZ LYS B 351 72.129 47.764 191.323 1.00 43.66 N ANISOU 1987 NZ LYS B 351 4669 7024 4896 -1396 -651 -711 N ATOM 1988 N ILE B 352 71.402 42.308 194.876 1.00 33.51 N ANISOU 1988 N ILE B 352 3324 5256 4152 -1440 -461 -945 N ATOM 1989 CA ILE B 352 72.639 41.563 195.090 1.00 35.82 C ANISOU 1989 CA ILE B 352 3650 5534 4426 -1447 -376 -990 C ATOM 1990 C ILE B 352 72.618 40.259 194.302 1.00 48.78 C ANISOU 1990 C ILE B 352 5300 7176 6060 -1497 -384 -1129 C ATOM 1991 O ILE B 352 73.609 39.886 193.662 1.00 51.06 O ANISOU 1991 O ILE B 352 5617 7531 6253 -1514 -346 -1206 O ATOM 1992 CB ILE B 352 72.862 41.312 196.594 1.00 31.12 C ANISOU 1992 CB ILE B 352 3055 4827 3943 -1416 -307 -927 C ATOM 1993 CG1 ILE B 352 73.101 42.631 197.330 1.00 26.36 C ANISOU 1993 CG1 ILE B 352 2465 4225 3326 -1368 -303 -806 C ATOM 1994 CG2 ILE B 352 74.025 40.356 196.812 1.00 25.46 C ANISOU 1994 CG2 ILE B 352 2363 4088 3222 -1427 -221 -985 C ATOM 1995 CD1 ILE B 352 73.262 42.473 198.828 1.00 23.39 C ANISOU 1995 CD1 ILE B 352 2094 3743 3049 -1331 -247 -743 C ATOM 1996 N LEU B 353 71.490 39.554 194.327 1.00 51.43 N ANISOU 1996 N LEU B 353 5610 7440 6490 -1525 -439 -1165 N ATOM 1997 CA LEU B 353 71.341 38.291 193.617 1.00 41.19 C ANISOU 1997 CA LEU B 353 4334 6119 5198 -1579 -467 -1299 C ATOM 1998 C LEU B 353 70.931 38.468 192.161 1.00 43.32 C ANISOU 1998 C LEU B 353 4619 6482 5359 -1606 -567 -1373 C ATOM 1999 O LEU B 353 70.704 37.467 191.474 1.00 41.39 O ANISOU 1999 O LEU B 353 4407 6213 5109 -1651 -615 -1493 O ATOM 2000 CB LEU B 353 70.318 37.405 194.335 1.00 33.43 C ANISOU 2000 CB LEU B 353 3317 5008 4375 -1611 -492 -1293 C ATOM 2001 CG LEU B 353 70.682 36.965 195.754 1.00 29.82 C ANISOU 2001 CG LEU B 353 2852 4450 4027 -1587 -394 -1234 C ATOM 2002 CD1 LEU B 353 69.530 36.217 196.398 1.00 30.48 C ANISOU 2002 CD1 LEU B 353 2890 4430 4262 -1625 -429 -1205 C ATOM 2003 CD2 LEU B 353 71.932 36.102 195.732 1.00 44.60 C ANISOU 2003 CD2 LEU B 353 4777 6304 5865 -1591 -305 -1329 C ATOM 2004 N LEU B 354 70.830 39.704 191.677 1.00 50.51 N ANISOU 2004 N LEU B 354 5516 7494 6180 -1577 -604 -1307 N ATOM 2005 CA LEU B 354 70.359 39.939 190.318 1.00 58.02 C ANISOU 2005 CA LEU B 354 6480 8538 7026 -1595 -705 -1364 C ATOM 2006 C LEU B 354 71.360 39.405 189.300 1.00 58.96 C ANISOU 2006 C LEU B 354 6664 8737 7001 -1604 -685 -1487 C ATOM 2007 O LEU B 354 72.574 39.565 189.455 1.00 64.91 O ANISOU 2007 O LEU B 354 7435 9543 7684 -1583 -592 -1480 O ATOM 2008 CB LEU B 354 70.123 41.431 190.087 1.00 65.47 C ANISOU 2008 CB LEU B 354 7398 9575 7904 -1557 -736 -1257 C ATOM 2009 CG LEU B 354 69.428 41.815 188.778 1.00 66.39 C ANISOU 2009 CG LEU B 354 7516 9784 7924 -1567 -850 -1292 C ATOM 2010 CD1 LEU B 354 68.046 41.183 188.697 1.00 66.01 C ANISOU 2010 CD1 LEU B 354 7430 9667 7985 -1610 -952 -1327 C ATOM 2011 CD2 LEU B 354 69.342 43.326 188.639 1.00 64.45 C ANISOU 2011 CD2 LEU B 354 7251 9626 7612 -1525 -864 -1178 C ATOM 2012 N ARG B 355 70.835 38.769 188.255 1.00 66.46 N ANISOU 2012 N ARG B 355 7652 9698 7902 -1636 -779 -1599 N ATOM 2013 CA ARG B 355 71.637 38.217 187.164 1.00 61.56 C ANISOU 2013 CA ARG B 355 7111 9153 7125 -1633 -778 -1734 C ATOM 2014 C ARG B 355 72.704 37.252 187.673 1.00 61.12 C ANISOU 2014 C ARG B 355 7094 9045 7084 -1632 -668 -1814 C ATOM 2015 O ARG B 355 72.607 36.042 187.469 1.00 64.85 O ANISOU 2015 O ARG B 355 7628 9430 7583 -1658 -689 -1942 O ATOM 2016 CB ARG B 355 72.288 39.339 186.350 1.00 52.39 C ANISOU 2016 CB ARG B 355 5954 8164 5786 -1590 -769 -1687 C ATOM 2017 CG ARG B 355 72.946 38.856 185.068 1.00 57.81 C ANISOU 2017 CG ARG B 355 6728 8952 6285 -1570 -784 -1821 C ATOM 2018 CD ARG B 355 73.013 39.957 184.022 1.00 63.24 C ANISOU 2018 CD ARG B 355 7419 9803 6807 -1534 -829 -1767 C ATOM 2019 NE ARG B 355 73.158 39.411 182.676 1.00 61.66 N ANISOU 2019 NE ARG B 355 7318 9675 6437 -1507 -887 -1902 N ATOM 2020 CZ ARG B 355 72.140 39.013 181.919 1.00 67.56 C ANISOU 2020 CZ ARG B 355 8113 10382 7177 -1525 -1020 -1979 C ATOM 2021 NH1 ARG B 355 70.898 39.100 182.377 1.00 71.01 N ANISOU 2021 NH1 ARG B 355 8489 10719 7771 -1575 -1105 -1929 N ATOM 2022 NH2 ARG B 355 72.361 38.527 180.705 1.00 68.56 N ANISOU 2022 NH2 ARG B 355 8351 10568 7131 -1488 -1071 -2102 N ATOM 2023 N ALA B1001 51.172 21.854 180.607 1.00101.55 N ANISOU 2023 N ALA B1001 11341 13320 13924 -3793 -2960 -3667 N ATOM 2024 CA ALA B1001 51.130 20.761 179.643 1.00105.10 C ANISOU 2024 CA ALA B1001 12012 13785 14138 -4068 -3033 -3818 C ATOM 2025 C ALA B1001 51.265 21.285 178.218 1.00104.78 C ANISOU 2025 C ALA B1001 12030 13847 13936 -3936 -3199 -3969 C ATOM 2026 O ALA B1001 51.237 20.515 177.258 1.00107.70 O ANISOU 2026 O ALA B1001 12584 14211 14126 -4105 -3306 -4115 O ATOM 2027 N LYS B1104 64.565 25.261 176.408 1.00 95.03 N ANISOU 2027 N LYS B1104 13145 12113 10849 -2356 -2807 -3516 N ATOM 2028 CA LYS B1104 65.002 26.208 177.427 1.00 89.61 C ANISOU 2028 CA LYS B1104 12217 11553 10277 -2280 -2601 -3365 C ATOM 2029 C LYS B1104 63.855 27.122 177.845 1.00 92.89 C ANISOU 2029 C LYS B1104 12379 12050 10863 -2358 -2679 -3189 C ATOM 2030 O LYS B1104 63.921 27.782 178.881 1.00 94.09 O ANISOU 2030 O LYS B1104 12329 12262 11157 -2337 -2537 -3045 O ATOM 2031 N TYR B1105 62.804 27.161 177.022 1.00 97.59 N ANISOU 2031 N TYR B1105 12997 12646 11436 -2443 -2908 -3203 N ATOM 2032 CA TYR B1105 61.665 28.023 177.322 1.00 97.84 C ANISOU 2032 CA TYR B1105 12792 12759 11625 -2502 -2993 -3044 C ATOM 2033 C TYR B1105 60.848 27.499 178.496 1.00 99.09 C ANISOU 2033 C TYR B1105 12790 12786 12073 -2621 -3005 -2935 C ATOM 2034 O TYR B1105 60.208 28.286 179.202 1.00 97.68 O ANISOU 2034 O TYR B1105 12385 12678 12053 -2635 -2978 -2776 O ATOM 2035 N GLY B1106 60.852 26.188 178.717 1.00101.17 N ANISOU 2035 N GLY B1106 13173 12863 12403 -2702 -3034 -3010 N ATOM 2036 CA GLY B1106 60.085 25.587 179.794 1.00 99.06 C ANISOU 2036 CA GLY B1106 12769 12470 12400 -2821 -3043 -2899 C ATOM 2037 C GLY B1106 60.546 25.980 181.183 1.00 93.53 C ANISOU 2037 C GLY B1106 11914 11786 11838 -2783 -2841 -2777 C ATOM 2038 O GLY B1106 59.817 26.626 181.935 1.00 92.86 O ANISOU 2038 O GLY B1106 11607 11759 11918 -2806 -2818 -2610 O TER 2039 GLY B1106 ATOM 2040 N CYS A 47 76.430 45.325 234.093 1.00 72.63 N ANISOU 2040 N CYS A 47 9012 10681 7903 -2037 773 -2512 N ATOM 2041 CA CYS A 47 76.438 44.163 233.214 1.00 71.61 C ANISOU 2041 CA CYS A 47 8764 10476 7968 -1984 623 -2201 C ATOM 2042 C CYS A 47 75.695 44.457 231.914 1.00 76.25 C ANISOU 2042 C CYS A 47 9230 10844 8898 -1754 707 -2225 C ATOM 2043 O CYS A 47 74.951 43.615 231.410 1.00 75.52 O ANISOU 2043 O CYS A 47 9013 10767 8913 -1708 717 -2051 O ATOM 2044 N GLY A 48 75.901 45.662 231.378 1.00 75.34 N ANISOU 2044 N GLY A 48 9156 10522 8947 -1625 757 -2432 N ATOM 2045 CA GLY A 48 75.252 46.030 230.131 1.00 74.81 C ANISOU 2045 CA GLY A 48 8985 10246 9193 -1408 813 -2438 C ATOM 2046 C GLY A 48 75.784 45.274 228.931 1.00 80.67 C ANISOU 2046 C GLY A 48 9669 10842 10140 -1368 618 -2205 C ATOM 2047 O GLY A 48 75.035 44.992 227.990 1.00 81.14 O ANISOU 2047 O GLY A 48 9610 10827 10391 -1244 637 -2114 O ATOM 2048 N SER A 49 77.074 44.938 228.940 1.00 80.65 N ANISOU 2048 N SER A 49 9737 10808 10097 -1473 430 -2114 N ATOM 2049 CA SER A 49 77.678 44.219 227.826 1.00 75.57 C ANISOU 2049 CA SER A 49 9042 10029 9642 -1425 265 -1913 C ATOM 2050 C SER A 49 77.438 42.717 227.895 1.00 65.29 C ANISOU 2050 C SER A 49 7670 8833 8303 -1495 182 -1681 C ATOM 2051 O SER A 49 77.600 42.030 226.881 1.00 64.33 O ANISOU 2051 O SER A 49 7497 8591 8356 -1429 89 -1533 O ATOM 2052 CB SER A 49 79.181 44.499 227.773 1.00 77.81 C ANISOU 2052 CB SER A 49 9417 10224 9922 -1406 119 -1811 C ATOM 2053 OG SER A 49 79.822 44.060 228.959 1.00 80.42 O ANISOU 2053 OG SER A 49 9797 10732 10028 -1574 31 -1777 O ATOM 2054 N VAL A 50 77.060 42.195 229.060 1.00 55.42 N ANISOU 2054 N VAL A 50 6437 7798 6823 -1624 219 -1633 N ATOM 2055 CA VAL A 50 76.818 40.764 229.236 1.00 51.20 C ANISOU 2055 CA VAL A 50 5860 7348 6244 -1710 139 -1387 C ATOM 2056 C VAL A 50 75.420 40.468 228.701 1.00 53.12 C ANISOU 2056 C VAL A 50 5988 7600 6594 -1644 271 -1362 C ATOM 2057 O VAL A 50 74.423 40.649 229.402 1.00 32.22 O ANISOU 2057 O VAL A 50 3302 5127 3814 -1684 437 -1428 O ATOM 2058 CB VAL A 50 76.966 40.336 230.698 1.00 39.24 C ANISOU 2058 CB VAL A 50 4418 6072 4421 -1899 119 -1317 C ATOM 2059 CG1 VAL A 50 77.056 38.819 230.800 1.00 35.53 C ANISOU 2059 CG1 VAL A 50 3935 5624 3942 -1990 -22 -1018 C ATOM 2060 CG2 VAL A 50 78.180 41.001 231.322 1.00 36.93 C ANISOU 2060 CG2 VAL A 50 4228 5813 3992 -1970 19 -1414 C ATOM 2061 N SER A 51 75.343 40.003 227.455 1.00 40.42 N ANISOU 2061 N SER A 51 4317 5823 5220 -1552 199 -1271 N ATOM 2062 CA SER A 51 74.064 39.712 226.822 1.00 28.45 C ANISOU 2062 CA SER A 51 2677 4316 3818 -1502 289 -1238 C ATOM 2063 C SER A 51 74.306 38.818 225.617 1.00 26.68 C ANISOU 2063 C SER A 51 2430 3919 3787 -1473 150 -1096 C ATOM 2064 O SER A 51 75.214 39.081 224.823 1.00 40.07 O ANISOU 2064 O SER A 51 4185 5443 5596 -1370 56 -1105 O ATOM 2065 CB SER A 51 73.354 41.002 226.395 1.00 36.39 C ANISOU 2065 CB SER A 51 3615 5290 4922 -1345 436 -1436 C ATOM 2066 OG SER A 51 72.163 40.719 225.680 1.00 34.60 O ANISOU 2066 OG SER A 51 3240 5080 4826 -1288 490 -1386 O ATOM 2067 N VAL A 52 73.494 37.764 225.483 1.00 28.60 N ANISOU 2067 N VAL A 52 2607 4206 4052 -1554 146 -954 N ATOM 2068 CA VAL A 52 73.620 36.854 224.346 1.00 27.82 C ANISOU 2068 CA VAL A 52 2537 3924 4111 -1490 21 -810 C ATOM 2069 C VAL A 52 73.075 37.460 223.064 1.00 24.74 C ANISOU 2069 C VAL A 52 2101 3442 3855 -1325 43 -866 C ATOM 2070 O VAL A 52 73.206 36.850 221.995 1.00 24.65 O ANISOU 2070 O VAL A 52 2143 3294 3928 -1261 -54 -761 O ATOM 2071 CB VAL A 52 72.912 35.515 224.646 1.00 26.98 C ANISOU 2071 CB VAL A 52 2405 3867 3978 -1641 -1 -634 C ATOM 2072 CG1 VAL A 52 71.420 35.619 224.364 1.00 27.77 C ANISOU 2072 CG1 VAL A 52 2366 4081 4104 -1647 112 -651 C ATOM 2073 CG2 VAL A 52 73.545 34.375 223.857 1.00 40.20 C ANISOU 2073 CG2 VAL A 52 4171 5316 5789 -1604 -159 -491 C ATOM 2074 N ALA A 53 72.478 38.652 223.135 1.00 32.09 N ANISOU 2074 N ALA A 53 2933 4456 4805 -1269 169 -1036 N ATOM 2075 CA ALA A 53 71.943 39.288 221.936 1.00 35.16 C ANISOU 2075 CA ALA A 53 3263 4766 5330 -1124 174 -1076 C ATOM 2076 C ALA A 53 73.043 39.677 220.959 1.00 29.88 C ANISOU 2076 C ALA A 53 2733 3908 4712 -1002 79 -1063 C ATOM 2077 O ALA A 53 72.797 39.739 219.750 1.00 22.19 O ANISOU 2077 O ALA A 53 1761 2858 3811 -920 33 -1017 O ATOM 2078 CB ALA A 53 71.119 40.519 222.314 1.00 32.81 C ANISOU 2078 CB ALA A 53 2810 4577 5081 -1069 332 -1264 C ATOM 2079 N PHE A 54 74.252 39.941 221.454 1.00 30.31 N ANISOU 2079 N PHE A 54 2898 3913 4708 -1003 51 -1091 N ATOM 2080 CA PHE A 54 75.347 40.351 220.582 1.00 33.60 C ANISOU 2080 CA PHE A 54 3426 4189 5152 -896 -14 -1063 C ATOM 2081 C PHE A 54 75.927 39.177 219.793 1.00 34.83 C ANISOU 2081 C PHE A 54 3662 4274 5299 -888 -117 -900 C ATOM 2082 O PHE A 54 76.031 39.275 218.564 1.00 28.86 O ANISOU 2082 O PHE A 54 2938 3451 4576 -812 -135 -871 O ATOM 2083 CB PHE A 54 76.444 41.062 221.382 1.00 36.85 C ANISOU 2083 CB PHE A 54 3908 4593 5500 -909 -10 -1140 C ATOM 2084 CG PHE A 54 76.018 42.385 221.949 1.00 40.52 C ANISOU 2084 CG PHE A 54 4332 5085 5979 -905 103 -1345 C ATOM 2085 CD1 PHE A 54 75.893 43.494 221.128 1.00 41.40 C ANISOU 2085 CD1 PHE A 54 4444 5085 6203 -797 139 -1421 C ATOM 2086 CD2 PHE A 54 75.741 42.522 223.299 1.00 45.17 C ANISOU 2086 CD2 PHE A 54 4892 5808 6464 -1025 178 -1475 C ATOM 2087 CE1 PHE A 54 75.498 44.716 221.641 1.00 48.42 C ANISOU 2087 CE1 PHE A 54 5312 5948 7138 -781 245 -1631 C ATOM 2088 CE2 PHE A 54 75.346 43.743 223.820 1.00 51.20 C ANISOU 2088 CE2 PHE A 54 5645 6581 7227 -1009 304 -1698 C ATOM 2089 CZ PHE A 54 75.225 44.840 222.989 1.00 50.53 C ANISOU 2089 CZ PHE A 54 5569 6336 7294 -875 337 -1784 C ATOM 2090 N PRO A 55 76.316 38.058 220.428 1.00 20.59 N ANISOU 2090 N PRO A 55 1885 2482 3457 -977 -181 -808 N ATOM 2091 CA PRO A 55 76.854 36.946 219.623 1.00 20.07 C ANISOU 2091 CA PRO A 55 1886 2330 3409 -968 -258 -699 C ATOM 2092 C PRO A 55 75.851 36.381 218.632 1.00 37.57 C ANISOU 2092 C PRO A 55 4091 4535 5651 -971 -257 -659 C ATOM 2093 O PRO A 55 76.230 36.032 217.506 1.00 30.03 O ANISOU 2093 O PRO A 55 3195 3512 4703 -922 -276 -644 O ATOM 2094 CB PRO A 55 77.259 35.907 220.680 1.00 22.26 C ANISOU 2094 CB PRO A 55 2168 2616 3675 -1088 -328 -622 C ATOM 2095 CG PRO A 55 76.470 36.255 221.887 1.00 22.11 C ANISOU 2095 CG PRO A 55 2069 2719 3612 -1186 -280 -661 C ATOM 2096 CD PRO A 55 76.355 37.742 221.868 1.00 21.77 C ANISOU 2096 CD PRO A 55 2004 2723 3545 -1104 -186 -810 C ATOM 2097 N ILE A 56 74.576 36.287 219.018 1.00 29.05 N ANISOU 2097 N ILE A 56 2921 3537 4579 -1042 -229 -653 N ATOM 2098 CA ILE A 56 73.558 35.779 218.101 1.00 28.51 C ANISOU 2098 CA ILE A 56 2824 3479 4531 -1068 -247 -609 C ATOM 2099 C ILE A 56 73.393 36.724 216.917 1.00 31.25 C ANISOU 2099 C ILE A 56 3160 3811 4902 -962 -228 -671 C ATOM 2100 O ILE A 56 73.336 36.295 215.759 1.00 31.56 O ANISOU 2100 O ILE A 56 3248 3811 4931 -960 -270 -641 O ATOM 2101 CB ILE A 56 72.225 35.565 218.840 1.00 24.89 C ANISOU 2101 CB ILE A 56 2231 3142 4085 -1173 -210 -584 C ATOM 2102 CG1 ILE A 56 72.378 34.491 219.918 1.00 23.54 C ANISOU 2102 CG1 ILE A 56 2075 2971 3899 -1310 -242 -492 C ATOM 2103 CG2 ILE A 56 71.125 35.187 217.857 1.00 24.42 C ANISOU 2103 CG2 ILE A 56 2116 3113 4050 -1205 -242 -537 C ATOM 2104 CD1 ILE A 56 71.122 34.257 220.726 1.00 25.14 C ANISOU 2104 CD1 ILE A 56 2137 3317 4099 -1429 -171 -464 C ATOM 2105 N THR A 57 73.320 38.029 217.192 1.00 31.07 N ANISOU 2105 N THR A 57 3074 3815 4916 -889 -165 -769 N ATOM 2106 CA THR A 57 73.193 39.004 216.113 1.00 20.07 C ANISOU 2106 CA THR A 57 1663 2388 3577 -802 -162 -818 C ATOM 2107 C THR A 57 74.418 38.985 215.208 1.00 26.29 C ANISOU 2107 C THR A 57 2583 3083 4323 -753 -194 -794 C ATOM 2108 O THR A 57 74.294 39.062 213.980 1.00 23.19 O ANISOU 2108 O THR A 57 2208 2670 3932 -741 -226 -778 O ATOM 2109 CB THR A 57 72.976 40.405 216.688 1.00 24.32 C ANISOU 2109 CB THR A 57 2109 2935 4197 -741 -87 -949 C ATOM 2110 OG1 THR A 57 71.848 40.392 217.573 1.00 21.85 O ANISOU 2110 OG1 THR A 57 1640 2744 3919 -788 -24 -995 O ATOM 2111 CG2 THR A 57 72.731 41.414 215.575 1.00 25.06 C ANISOU 2111 CG2 THR A 57 2163 2969 4391 -663 -107 -986 C ATOM 2112 N MET A 58 75.611 38.870 215.797 1.00 26.90 N ANISOU 2112 N MET A 58 2734 3124 4361 -739 -187 -791 N ATOM 2113 CA MET A 58 76.834 38.898 215.002 1.00 26.08 C ANISOU 2113 CA MET A 58 2715 2961 4232 -695 -197 -778 C ATOM 2114 C MET A 58 77.005 37.628 214.175 1.00 21.68 C ANISOU 2114 C MET A 58 2210 2377 3650 -727 -233 -729 C ATOM 2115 O MET A 58 77.589 37.675 213.086 1.00 18.03 O ANISOU 2115 O MET A 58 1789 1884 3177 -703 -231 -740 O ATOM 2116 CB MET A 58 78.041 39.126 215.913 1.00 21.34 C ANISOU 2116 CB MET A 58 2144 2349 3615 -682 -188 -791 C ATOM 2117 CG MET A 58 78.081 40.526 216.517 1.00 30.31 C ANISOU 2117 CG MET A 58 3257 3492 4768 -657 -146 -868 C ATOM 2118 SD MET A 58 79.541 40.869 217.523 1.00 31.64 S ANISOU 2118 SD MET A 58 3463 3663 4897 -676 -156 -886 S ATOM 2119 CE MET A 58 79.286 39.740 218.889 1.00 39.20 C ANISOU 2119 CE MET A 58 4395 4677 5822 -767 -201 -853 C ATOM 2120 N LEU A 59 76.505 36.492 214.664 1.00 19.53 N ANISOU 2120 N LEU A 59 1935 2111 3374 -799 -264 -686 N ATOM 2121 CA LEU A 59 76.616 35.255 213.897 1.00 31.86 C ANISOU 2121 CA LEU A 59 3553 3620 4930 -841 -294 -666 C ATOM 2122 C LEU A 59 75.715 35.282 212.667 1.00 33.46 C ANISOU 2122 C LEU A 59 3757 3846 5109 -876 -315 -670 C ATOM 2123 O LEU A 59 76.100 34.793 211.598 1.00 31.29 O ANISOU 2123 O LEU A 59 3543 3527 4818 -886 -325 -695 O ATOM 2124 CB LEU A 59 76.282 34.054 214.782 1.00 30.46 C ANISOU 2124 CB LEU A 59 3382 3425 4767 -935 -327 -617 C ATOM 2125 CG LEU A 59 76.247 32.679 214.106 1.00 28.21 C ANISOU 2125 CG LEU A 59 3164 3056 4497 -1000 -356 -613 C ATOM 2126 CD1 LEU A 59 77.563 32.382 213.400 1.00 23.51 C ANISOU 2126 CD1 LEU A 59 2617 2366 3951 -919 -337 -674 C ATOM 2127 CD2 LEU A 59 75.925 31.590 215.117 1.00 27.08 C ANISOU 2127 CD2 LEU A 59 3030 2879 4382 -1112 -384 -558 C ATOM 2128 N LEU A 60 74.513 35.848 212.799 1.00 34.93 N ANISOU 2128 N LEU A 60 3861 4108 5303 -904 -326 -657 N ATOM 2129 CA LEU A 60 73.569 35.843 211.686 1.00 35.33 C ANISOU 2129 CA LEU A 60 3885 4199 5339 -961 -372 -650 C ATOM 2130 C LEU A 60 73.965 36.848 210.610 1.00 26.08 C ANISOU 2130 C LEU A 60 2729 3019 4162 -909 -371 -688 C ATOM 2131 O LEU A 60 73.902 36.540 209.414 1.00 20.96 O ANISOU 2131 O LEU A 60 2127 2368 3470 -966 -415 -693 O ATOM 2132 CB LEU A 60 72.157 36.125 212.197 1.00 38.51 C ANISOU 2132 CB LEU A 60 4148 4703 5780 -1007 -388 -623 C ATOM 2133 CG LEU A 60 71.613 35.105 213.201 1.00 36.01 C ANISOU 2133 CG LEU A 60 3804 4414 5462 -1103 -395 -567 C ATOM 2134 CD1 LEU A 60 70.209 35.479 213.650 1.00 28.67 C ANISOU 2134 CD1 LEU A 60 2696 3615 4581 -1146 -393 -542 C ATOM 2135 CD2 LEU A 60 71.644 33.700 212.613 1.00 35.64 C ANISOU 2135 CD2 LEU A 60 3861 4310 5371 -1214 -452 -531 C ATOM 2136 N THR A 61 74.376 38.055 211.011 1.00 20.41 N ANISOU 2136 N THR A 61 1978 2290 3487 -822 -328 -719 N ATOM 2137 CA THR A 61 74.779 39.054 210.026 1.00 19.03 C ANISOU 2137 CA THR A 61 1821 2092 3318 -795 -334 -745 C ATOM 2138 C THR A 61 76.075 38.653 209.333 1.00 24.56 C ANISOU 2138 C THR A 61 2631 2744 3957 -796 -312 -758 C ATOM 2139 O THR A 61 76.256 38.922 208.139 1.00 35.03 O ANISOU 2139 O THR A 61 3993 4066 5250 -838 -336 -771 O ATOM 2140 CB THR A 61 74.930 40.424 210.687 1.00 22.24 C ANISOU 2140 CB THR A 61 2174 2468 3807 -716 -295 -784 C ATOM 2141 OG1 THR A 61 75.951 40.366 211.690 1.00 37.55 O ANISOU 2141 OG1 THR A 61 4161 4380 5727 -672 -237 -797 O ATOM 2142 CG2 THR A 61 73.621 40.854 211.329 1.00 21.60 C ANISOU 2142 CG2 THR A 61 1948 2432 3829 -702 -307 -805 C ATOM 2143 N GLY A 62 76.988 38.010 210.063 1.00 18.15 N ANISOU 2143 N GLY A 62 1853 1899 3143 -759 -271 -761 N ATOM 2144 CA GLY A 62 78.217 37.542 209.445 1.00 18.13 C ANISOU 2144 CA GLY A 62 1908 1856 3125 -749 -243 -794 C ATOM 2145 C GLY A 62 77.976 36.432 208.441 1.00 28.99 C ANISOU 2145 C GLY A 62 3334 3212 4470 -818 -272 -820 C ATOM 2146 O GLY A 62 78.625 36.380 207.392 1.00 37.02 O ANISOU 2146 O GLY A 62 4389 4211 5466 -836 -253 -875 O ATOM 2147 N PHE A 63 77.044 35.528 208.749 1.00 26.87 N ANISOU 2147 N PHE A 63 3067 2944 4198 -873 -316 -791 N ATOM 2148 CA PHE A 63 76.730 34.438 207.831 1.00 25.72 C ANISOU 2148 CA PHE A 63 2984 2764 4023 -958 -356 -823 C ATOM 2149 C PHE A 63 76.141 34.964 206.528 1.00 33.06 C ANISOU 2149 C PHE A 63 3927 3742 4894 -1031 -412 -837 C ATOM 2150 O PHE A 63 76.569 34.569 205.437 1.00 22.38 O ANISOU 2150 O PHE A 63 2638 2359 3509 -1069 -415 -910 O ATOM 2151 CB PHE A 63 75.766 33.454 208.497 1.00 21.09 C ANISOU 2151 CB PHE A 63 2396 2171 3447 -1032 -402 -777 C ATOM 2152 CG PHE A 63 75.331 32.330 207.597 1.00 30.74 C ANISOU 2152 CG PHE A 63 3694 3342 4644 -1140 -460 -811 C ATOM 2153 CD1 PHE A 63 76.087 31.173 207.499 1.00 38.54 C ANISOU 2153 CD1 PHE A 63 4762 4210 5673 -1139 -433 -879 C ATOM 2154 CD2 PHE A 63 74.167 32.429 206.850 1.00 28.70 C ANISOU 2154 CD2 PHE A 63 3419 3146 4340 -1245 -552 -784 C ATOM 2155 CE1 PHE A 63 75.691 30.137 206.672 1.00 35.12 C ANISOU 2155 CE1 PHE A 63 4415 3704 5225 -1240 -488 -932 C ATOM 2156 CE2 PHE A 63 73.768 31.397 206.019 1.00 29.07 C ANISOU 2156 CE2 PHE A 63 3537 3132 4374 -1349 -629 -825 C ATOM 2157 CZ PHE A 63 74.531 30.250 205.931 1.00 25.76 C ANISOU 2157 CZ PHE A 63 3222 2580 3985 -1348 -592 -906 C ATOM 2158 N VAL A 64 75.152 35.856 206.622 1.00 31.86 N ANISOU 2158 N VAL A 64 3700 3668 4736 -1054 -459 -781 N ATOM 2159 CA VAL A 64 74.453 36.329 205.428 1.00 28.67 C ANISOU 2159 CA VAL A 64 3283 3321 4288 -1145 -548 -778 C ATOM 2160 C VAL A 64 75.404 37.101 204.521 1.00 25.87 C ANISOU 2160 C VAL A 64 2975 2948 3906 -1132 -524 -829 C ATOM 2161 O VAL A 64 75.445 36.881 203.304 1.00 26.20 O ANISOU 2161 O VAL A 64 3066 2997 3893 -1209 -574 -882 O ATOM 2162 CB VAL A 64 73.234 37.183 205.822 1.00 25.84 C ANISOU 2162 CB VAL A 64 2788 3062 3967 -1159 -598 -717 C ATOM 2163 CG1 VAL A 64 72.598 37.802 204.588 1.00 25.18 C ANISOU 2163 CG1 VAL A 64 2662 3058 3847 -1255 -715 -703 C ATOM 2164 CG2 VAL A 64 72.217 36.342 206.574 1.00 25.73 C ANISOU 2164 CG2 VAL A 64 2712 3092 3973 -1204 -623 -672 C ATOM 2165 N GLY A 65 76.184 38.015 205.100 1.00 23.95 N ANISOU 2165 N GLY A 65 2714 2684 3703 -1043 -446 -825 N ATOM 2166 CA GLY A 65 77.100 38.807 204.292 1.00 28.12 C ANISOU 2166 CA GLY A 65 3279 3196 4209 -1056 -417 -864 C ATOM 2167 C GLY A 65 78.139 37.959 203.584 1.00 33.83 C ANISOU 2167 C GLY A 65 4070 3893 4891 -1069 -350 -960 C ATOM 2168 O GLY A 65 78.400 38.138 202.391 1.00 33.80 O ANISOU 2168 O GLY A 65 4105 3919 4819 -1152 -349 -1026 O ATOM 2169 N ASN A 66 78.743 37.014 204.308 1.00 28.49 N ANISOU 2169 N ASN A 66 3396 3170 4258 -997 -284 -989 N ATOM 2170 CA ASN A 66 79.800 36.198 203.724 1.00 22.15 C ANISOU 2170 CA ASN A 66 2625 2336 3454 -996 -196 -1109 C ATOM 2171 C ASN A 66 79.256 35.143 202.769 1.00 38.84 C ANISOU 2171 C ASN A 66 4807 4441 5509 -1084 -232 -1189 C ATOM 2172 O ASN A 66 79.964 34.736 201.841 1.00 41.43 O ANISOU 2172 O ASN A 66 5175 4771 5797 -1124 -150 -1324 O ATOM 2173 CB ASN A 66 80.623 35.540 204.831 1.00 21.70 C ANISOU 2173 CB ASN A 66 2526 2223 3498 -895 -133 -1119 C ATOM 2174 CG ASN A 66 81.535 36.525 205.540 1.00 32.29 C ANISOU 2174 CG ASN A 66 3800 3580 4888 -825 -81 -1089 C ATOM 2175 OD1 ASN A 66 82.121 37.407 204.912 1.00 31.83 O ANISOU 2175 OD1 ASN A 66 3736 3554 4804 -856 -37 -1119 O ATOM 2176 ND2 ASN A 66 81.655 36.383 206.856 1.00 34.79 N ANISOU 2176 ND2 ASN A 66 4073 3878 5269 -752 -91 -1032 N ATOM 2177 N ALA A 67 78.014 34.692 202.969 1.00 57.94 N ANISOU 2177 N ALA A 67 7237 6858 7918 -1129 -342 -1122 N ATOM 2178 CA ALA A 67 77.443 33.699 202.064 1.00 25.51 C ANISOU 2178 CA ALA A 67 3197 2740 3757 -1226 -394 -1201 C ATOM 2179 C ALA A 67 77.064 34.324 200.728 1.00 26.75 C ANISOU 2179 C ALA A 67 3372 2996 3797 -1334 -442 -1249 C ATOM 2180 O ALA A 67 77.257 33.709 199.672 1.00 28.47 O ANISOU 2180 O ALA A 67 3663 3233 3920 -1417 -408 -1383 O ATOM 2181 CB ALA A 67 76.229 33.032 202.708 1.00 25.60 C ANISOU 2181 CB ALA A 67 3196 2727 3804 -1264 -504 -1113 C ATOM 2182 N LEU A 68 76.518 35.543 200.752 1.00 26.22 N ANISOU 2182 N LEU A 68 3238 3001 3721 -1348 -516 -1151 N ATOM 2183 CA LEU A 68 76.204 36.232 199.504 1.00 31.66 C ANISOU 2183 CA LEU A 68 3940 3810 4278 -1470 -566 -1183 C ATOM 2184 C LEU A 68 77.470 36.545 198.717 1.00 35.48 C ANISOU 2184 C LEU A 68 4499 4330 4653 -1515 -424 -1287 C ATOM 2185 O LEU A 68 77.468 36.503 197.480 1.00 31.65 O ANISOU 2185 O LEU A 68 4091 3954 3978 -1660 -414 -1365 O ATOM 2186 CB LEU A 68 75.419 37.513 199.789 1.00 31.16 C ANISOU 2186 CB LEU A 68 3775 3804 4260 -1471 -676 -1054 C ATOM 2187 CG LEU A 68 74.028 37.364 200.411 1.00 32.44 C ANISOU 2187 CG LEU A 68 3822 3983 4523 -1454 -810 -965 C ATOM 2188 CD1 LEU A 68 73.396 38.728 200.634 1.00 27.06 C ANISOU 2188 CD1 LEU A 68 3012 3369 3902 -1447 -893 -869 C ATOM 2189 CD2 LEU A 68 73.138 36.498 199.534 1.00 31.61 C ANISOU 2189 CD2 LEU A 68 3721 3966 4322 -1565 -895 -1020 C ATOM 2190 N ALA A 69 78.561 36.865 199.418 1.00 34.48 N ANISOU 2190 N ALA A 69 4348 4134 4620 -1412 -308 -1288 N ATOM 2191 CA ALA A 69 79.830 37.123 198.745 1.00 27.63 C ANISOU 2191 CA ALA A 69 3520 3307 3672 -1461 -151 -1398 C ATOM 2192 C ALA A 69 80.346 35.867 198.055 1.00 29.20 C ANISOU 2192 C ALA A 69 3785 3504 3806 -1497 -40 -1577 C ATOM 2193 O ALA A 69 80.730 35.900 196.880 1.00 31.04 O ANISOU 2193 O ALA A 69 4092 3840 3860 -1635 47 -1692 O ATOM 2194 CB ALA A 69 80.857 37.654 199.746 1.00 28.92 C ANISOU 2194 CB ALA A 69 3610 3401 3976 -1339 -61 -1363 C ATOM 2195 N MET A 70 80.359 34.742 198.776 1.00 33.45 N ANISOU 2195 N MET A 70 4307 3926 4475 -1391 -37 -1602 N ATOM 2196 CA MET A 70 80.813 33.488 198.184 1.00 36.07 C ANISOU 2196 CA MET A 70 4705 4218 4784 -1414 63 -1782 C ATOM 2197 C MET A 70 79.901 33.042 197.049 1.00 46.50 C ANISOU 2197 C MET A 70 6131 5611 5928 -1565 -10 -1846 C ATOM 2198 O MET A 70 80.344 32.333 196.138 1.00 52.16 O ANISOU 2198 O MET A 70 6928 6343 6546 -1636 98 -2025 O ATOM 2199 CB MET A 70 80.899 32.402 199.256 1.00 31.04 C ANISOU 2199 CB MET A 70 4041 3424 4328 -1287 50 -1768 C ATOM 2200 CG MET A 70 81.924 32.682 200.341 1.00 32.82 C ANISOU 2200 CG MET A 70 4159 3599 4714 -1149 127 -1727 C ATOM 2201 SD MET A 70 82.045 31.348 201.549 1.00 44.23 S ANISOU 2201 SD MET A 70 5586 4874 6344 -1033 106 -1710 S ATOM 2202 CE MET A 70 80.340 31.218 202.081 1.00 49.52 C ANISOU 2202 CE MET A 70 6311 5539 6965 -1090 -88 -1534 C ATOM 2203 N LEU A 71 78.629 33.446 197.085 1.00 46.17 N ANISOU 2203 N LEU A 71 6076 5621 5846 -1619 -188 -1712 N ATOM 2204 CA LEU A 71 77.701 33.078 196.021 1.00 42.44 C ANISOU 2204 CA LEU A 71 5680 5245 5199 -1777 -280 -1759 C ATOM 2205 C LEU A 71 78.001 33.841 194.736 1.00 36.06 C ANISOU 2205 C LEU A 71 4946 4623 4133 -1940 -227 -1810 C ATOM 2206 O LEU A 71 77.902 33.281 193.638 1.00 38.56 O ANISOU 2206 O LEU A 71 5370 5023 4257 -2079 -201 -1934 O ATOM 2207 CB LEU A 71 76.262 33.328 196.481 1.00 51.75 C ANISOU 2207 CB LEU A 71 6781 6448 6432 -1786 -483 -1600 C ATOM 2208 CG LEU A 71 75.094 32.753 195.670 1.00 35.98 C ANISOU 2208 CG LEU A 71 4821 4540 4311 -1933 -613 -1626 C ATOM 2209 CD1 LEU A 71 74.665 33.700 194.555 1.00 42.90 C ANISOU 2209 CD1 LEU A 71 5721 5636 4941 -2094 -690 -1575 C ATOM 2210 CD2 LEU A 71 75.452 31.387 195.106 1.00 38.00 C ANISOU 2210 CD2 LEU A 71 5200 4718 4521 -1986 -532 -1818 C ATOM 2211 N LEU A 72 78.372 35.118 194.850 1.00 34.99 N ANISOU 2211 N LEU A 72 4769 4554 3972 -1945 -214 -1709 N ATOM 2212 CA LEU A 72 78.604 35.928 193.658 1.00 39.60 C ANISOU 2212 CA LEU A 72 5442 5326 4277 -2137 -186 -1712 C ATOM 2213 C LEU A 72 79.924 35.574 192.982 1.00 44.38 C ANISOU 2213 C LEU A 72 6122 5965 4777 -2190 53 -1910 C ATOM 2214 O LEU A 72 80.013 35.577 191.748 1.00 44.87 O ANISOU 2214 O LEU A 72 6300 6190 4557 -2377 101 -1986 O ATOM 2215 CB LEU A 72 78.569 37.415 194.017 1.00 43.70 C ANISOU 2215 CB LEU A 72 5909 5884 4812 -2147 -261 -1529 C ATOM 2216 CG LEU A 72 77.239 37.971 194.532 1.00 34.64 C ANISOU 2216 CG LEU A 72 4674 4740 3749 -2115 -493 -1333 C ATOM 2217 CD1 LEU A 72 77.314 39.480 194.694 1.00 34.08 C ANISOU 2217 CD1 LEU A 72 4579 4698 3671 -2156 -562 -1160 C ATOM 2218 CD2 LEU A 72 76.096 37.584 193.605 1.00 51.41 C ANISOU 2218 CD2 LEU A 72 6843 7013 5676 -2258 -655 -1299 C ATOM 2219 N VAL A 73 80.961 35.269 193.767 1.00 48.52 N ANISOU 2219 N VAL A 73 6568 6354 5513 -2033 207 -1993 N ATOM 2220 CA VAL A 73 82.264 34.967 193.177 1.00 48.77 C ANISOU 2220 CA VAL A 73 6626 6427 5480 -2072 453 -2193 C ATOM 2221 C VAL A 73 82.240 33.611 192.481 1.00 40.91 C ANISOU 2221 C VAL A 73 5715 5408 4423 -2096 524 -2390 C ATOM 2222 O VAL A 73 82.892 33.419 191.448 1.00 43.46 O ANISOU 2222 O VAL A 73 6110 5841 4560 -2214 693 -2558 O ATOM 2223 CB VAL A 73 83.372 35.045 194.244 1.00 47.23 C ANISOU 2223 CB VAL A 73 6291 6107 5548 -1896 578 -2217 C ATOM 2224 CG1 VAL A 73 83.508 36.469 194.761 1.00 34.98 C ANISOU 2224 CG1 VAL A 73 4678 4586 4026 -1909 529 -2048 C ATOM 2225 CG2 VAL A 73 83.090 34.086 195.389 1.00 54.58 C ANISOU 2225 CG2 VAL A 73 7152 6841 6745 -1693 498 -2185 C ATOM 2226 N SER A 74 81.492 32.651 193.030 1.00 46.06 N ANISOU 2226 N SER A 74 6364 5912 5225 -1998 401 -2375 N ATOM 2227 CA SER A 74 81.346 31.361 192.365 1.00 48.62 C ANISOU 2227 CA SER A 74 6790 6189 5494 -2040 441 -2557 C ATOM 2228 C SER A 74 80.612 31.506 191.040 1.00 55.42 C ANISOU 2228 C SER A 74 7783 7243 6031 -2269 377 -2583 C ATOM 2229 O SER A 74 80.865 30.743 190.101 1.00 57.30 O ANISOU 2229 O SER A 74 8128 7515 6129 -2359 485 -2780 O ATOM 2230 CB SER A 74 80.611 30.378 193.276 1.00 52.70 C ANISOU 2230 CB SER A 74 7290 6507 6227 -1922 300 -2506 C ATOM 2231 OG SER A 74 81.299 30.202 194.502 1.00 50.85 O ANISOU 2231 OG SER A 74 6948 6111 6260 -1726 348 -2464 O ATOM 2232 N ARG A 75 79.707 32.481 190.945 1.00 61.21 N ANISOU 2232 N ARG A 75 8507 8108 6640 -2365 196 -2383 N ATOM 2233 CA ARG A 75 78.947 32.691 189.719 1.00 70.50 C ANISOU 2233 CA ARG A 75 9798 9492 7495 -2592 96 -2363 C ATOM 2234 C ARG A 75 79.797 33.356 188.641 1.00 73.68 C ANISOU 2234 C ARG A 75 10288 10096 7609 -2757 255 -2425 C ATOM 2235 O ARG A 75 79.673 33.023 187.457 1.00 72.40 O ANISOU 2235 O ARG A 75 10253 10082 7174 -2936 285 -2526 O ATOM 2236 CB ARG A 75 77.698 33.521 190.028 1.00 66.09 C ANISOU 2236 CB ARG A 75 9177 9008 6924 -2625 -166 -2107 C ATOM 2237 CG ARG A 75 76.982 34.095 188.819 1.00 76.38 C ANISOU 2237 CG ARG A 75 10573 10566 7883 -2861 -303 -2008 C ATOM 2238 CD ARG A 75 77.230 35.589 188.692 1.00 77.83 C ANISOU 2238 CD ARG A 75 10751 10887 7935 -2930 -344 -1811 C ATOM 2239 NE ARG A 75 76.530 36.159 187.545 1.00 79.44 N ANISOU 2239 NE ARG A 75 11047 11339 7798 -3155 -509 -1665 N ATOM 2240 CZ ARG A 75 76.606 37.435 187.183 1.00 75.93 C ANISOU 2240 CZ ARG A 75 10637 11043 7170 -3265 -594 -1452 C ATOM 2241 NH1 ARG A 75 77.352 38.281 187.880 1.00 73.99 N ANISOU 2241 NH1 ARG A 75 10347 10713 7052 -3186 -519 -1387 N ATOM 2242 NH2 ARG A 75 75.935 37.866 186.125 1.00 75.81 N ANISOU 2242 NH2 ARG A 75 10705 11253 6846 -3461 -769 -1287 N ATOM 2243 N SER A 76 80.665 34.287 189.026 1.00 74.73 N ANISOU 2243 N SER A 76 10360 10246 7790 -2716 362 -2366 N ATOM 2244 CA SER A 76 81.452 35.043 188.058 1.00 63.41 C ANISOU 2244 CA SER A 76 9006 9018 6070 -2899 508 -2391 C ATOM 2245 C SER A 76 82.669 34.242 187.607 1.00 60.48 C ANISOU 2245 C SER A 76 8647 8632 5701 -2878 804 -2670 C ATOM 2246 O SER A 76 82.840 33.969 186.419 1.00 70.25 O ANISOU 2246 O SER A 76 10001 10027 6665 -3046 902 -2791 O ATOM 2247 CB SER A 76 81.893 36.384 188.647 1.00 57.88 C ANISOU 2247 CB SER A 76 8239 8336 5417 -2890 502 -2218 C ATOM 2248 OG SER A 76 80.779 37.220 188.903 1.00 65.93 O ANISOU 2248 OG SER A 76 9257 9387 6408 -2927 225 -1954 O ATOM 2249 N ARG A 78 85.834 31.283 188.539 1.00 88.46 N ANISOU 2249 N ARG A 78 11954 11710 9948 -2360 1458 -3367 N ATOM 2250 CA ARG A 78 86.612 30.371 189.368 1.00 89.01 C ANISOU 2250 CA ARG A 78 11903 11553 10363 -2117 1560 -3491 C ATOM 2251 C ARG A 78 85.815 29.930 190.592 1.00 89.81 C ANISOU 2251 C ARG A 78 11969 11432 10722 -1959 1337 -3341 C ATOM 2252 O ARG A 78 85.797 28.749 190.939 1.00 95.22 O ANISOU 2252 O ARG A 78 12673 11917 11591 -1829 1327 -3437 O ATOM 2253 CB ARG A 78 87.924 31.029 189.801 1.00 90.23 C ANISOU 2253 CB ARG A 78 11876 11749 10657 -2036 1745 -3508 C ATOM 2254 CG ARG A 78 89.140 30.114 189.738 1.00 97.95 C ANISOU 2254 CG ARG A 78 12759 12636 11823 -1882 1974 -3746 C ATOM 2255 CD ARG A 78 89.139 29.112 190.882 1.00101.47 C ANISOU 2255 CD ARG A 78 13130 12794 12628 -1632 1885 -3739 C ATOM 2256 NE ARG A 78 90.456 28.518 191.096 1.00102.04 N ANISOU 2256 NE ARG A 78 13053 12780 12939 -1449 2083 -3907 N ATOM 2257 CZ ARG A 78 90.792 27.816 192.173 1.00100.88 C ANISOU 2257 CZ ARG A 78 12796 12405 13127 -1220 2032 -3884 C ATOM 2258 NH1 ARG A 78 92.013 27.314 192.285 1.00103.00 N ANISOU 2258 NH1 ARG A 78 12919 12612 13605 -1050 2208 -4030 N ATOM 2259 NH2 ARG A 78 89.907 27.620 193.142 1.00 97.00 N ANISOU 2259 NH2 ARG A 78 12339 11759 12758 -1161 1802 -3703 N ATOM 2260 N LYS A 86 89.019 36.841 187.402 1.00 72.32 N ANISOU 2260 N LYS A 86 9750 10513 7213 -2977 1975 -3009 N ATOM 2261 CA LYS A 86 90.205 37.564 187.844 1.00 75.49 C ANISOU 2261 CA LYS A 86 9996 10961 7727 -2963 2159 -3007 C ATOM 2262 C LYS A 86 90.627 37.132 189.243 1.00 79.04 C ANISOU 2262 C LYS A 86 10237 11172 8622 -2685 2155 -3073 C ATOM 2263 O LYS A 86 89.852 36.517 189.976 1.00 75.45 O ANISOU 2263 O LYS A 86 9784 10514 8369 -2525 1969 -3049 O ATOM 2264 CB LYS A 86 89.957 39.074 187.812 1.00 75.19 C ANISOU 2264 CB LYS A 86 10052 11056 7461 -3170 2071 -2741 C ATOM 2265 CG LYS A 86 89.749 39.638 186.417 1.00 79.45 C ANISOU 2265 CG LYS A 86 10780 11853 7552 -3457 2080 -2616 C ATOM 2266 CD LYS A 86 90.882 39.235 185.487 1.00 84.86 C ANISOU 2266 CD LYS A 86 11399 12693 8150 -3515 2366 -2800 C ATOM 2267 CE LYS A 86 90.532 39.521 184.035 1.00 88.02 C ANISOU 2267 CE LYS A 86 12003 13331 8109 -3785 2346 -2710 C ATOM 2268 NZ LYS A 86 91.176 38.550 183.106 1.00 91.42 N ANISOU 2268 NZ LYS A 86 12413 13854 8468 -3786 2566 -2989 N ATOM 2269 N SER A 87 91.867 37.463 189.608 1.00 87.39 N ANISOU 2269 N SER A 87 11102 12267 9835 -2633 2350 -3126 N ATOM 2270 CA SER A 87 92.383 37.094 190.920 1.00 91.14 C ANISOU 2270 CA SER A 87 11360 12543 10727 -2379 2340 -3173 C ATOM 2271 C SER A 87 91.756 37.914 192.038 1.00 89.96 C ANISOU 2271 C SER A 87 11216 12276 10689 -2358 2136 -2994 C ATOM 2272 O SER A 87 91.725 37.452 193.184 1.00 82.31 O ANISOU 2272 O SER A 87 10124 11100 10051 -2144 2028 -2995 O ATOM 2273 CB SER A 87 93.903 37.249 190.950 1.00 96.73 C ANISOU 2273 CB SER A 87 11836 13348 11570 -2334 2577 -3256 C ATOM 2274 OG SER A 87 94.518 36.423 189.976 1.00103.05 O ANISOU 2274 OG SER A 87 12626 14228 12299 -2321 2755 -3446 O ATOM 2275 N PHE A 88 91.262 39.118 191.736 1.00 93.42 N ANISOU 2275 N PHE A 88 11769 12800 10926 -2539 2003 -2717 N ATOM 2276 CA PHE A 88 90.589 39.914 192.757 1.00 94.20 C ANISOU 2276 CA PHE A 88 11857 12733 11201 -2473 1733 -2439 C ATOM 2277 C PHE A 88 89.296 39.249 193.212 1.00 93.37 C ANISOU 2277 C PHE A 88 11844 12462 11168 -2367 1499 -2438 C ATOM 2278 O PHE A 88 88.958 39.287 194.400 1.00102.69 O ANISOU 2278 O PHE A 88 12942 13462 12615 -2212 1341 -2345 O ATOM 2279 CB PHE A 88 90.319 41.325 192.234 1.00 99.26 C ANISOU 2279 CB PHE A 88 12617 13475 11621 -2679 1648 -2145 C ATOM 2280 CG PHE A 88 91.499 42.248 192.350 1.00106.49 C ANISOU 2280 CG PHE A 88 13405 14465 12592 -2762 1798 -2055 C ATOM 2281 CD1 PHE A 88 92.370 42.144 193.421 1.00104.05 C ANISOU 2281 CD1 PHE A 88 12864 14061 12608 -2609 1857 -2121 C ATOM 2282 CD2 PHE A 88 91.737 43.219 191.391 1.00110.79 C ANISOU 2282 CD2 PHE A 88 14057 15181 12856 -3011 1870 -1889 C ATOM 2283 CE1 PHE A 88 93.457 42.990 193.535 1.00102.89 C ANISOU 2283 CE1 PHE A 88 12583 13996 12514 -2711 1984 -2041 C ATOM 2284 CE2 PHE A 88 92.824 44.069 191.499 1.00105.91 C ANISOU 2284 CE2 PHE A 88 13320 14629 12294 -3117 2010 -1801 C ATOM 2285 CZ PHE A 88 93.685 43.953 192.573 1.00103.22 C ANISOU 2285 CZ PHE A 88 12734 14198 12285 -2971 2068 -1885 C ATOM 2286 N LEU A 89 88.557 38.639 192.282 1.00 80.98 N ANISOU 2286 N LEU A 89 10448 10971 9352 -2471 1476 -2542 N ATOM 2287 CA LEU A 89 87.376 37.876 192.671 1.00 66.36 C ANISOU 2287 CA LEU A 89 8636 8976 7603 -2332 1261 -2476 C ATOM 2288 C LEU A 89 87.758 36.648 193.486 1.00 64.55 C ANISOU 2288 C LEU A 89 8266 8569 7692 -2073 1310 -2598 C ATOM 2289 O LEU A 89 87.039 36.262 194.414 1.00 64.43 O ANISOU 2289 O LEU A 89 8217 8392 7870 -1907 1128 -2480 O ATOM 2290 CB LEU A 89 86.578 37.468 191.432 1.00 59.61 C ANISOU 2290 CB LEU A 89 7962 8254 6434 -2482 1214 -2498 C ATOM 2291 CG LEU A 89 85.793 38.568 190.715 1.00 53.63 C ANISOU 2291 CG LEU A 89 7365 7655 5356 -2721 1055 -2299 C ATOM 2292 CD1 LEU A 89 85.155 38.025 189.446 1.00 46.58 C ANISOU 2292 CD1 LEU A 89 6629 6919 4149 -2869 1025 -2339 C ATOM 2293 CD2 LEU A 89 84.741 39.165 191.638 1.00 43.13 C ANISOU 2293 CD2 LEU A 89 6005 6187 4194 -2634 773 -2054 C ATOM 2294 N LEU A 90 88.889 36.020 193.151 1.00 60.51 N ANISOU 2294 N LEU A 90 7668 8091 7232 -2036 1550 -2818 N ATOM 2295 CA LEU A 90 89.317 34.827 193.874 1.00 59.96 C ANISOU 2295 CA LEU A 90 7471 7842 7468 -1798 1581 -2921 C ATOM 2296 C LEU A 90 89.713 35.155 195.308 1.00 53.70 C ANISOU 2296 C LEU A 90 6503 6922 6978 -1638 1509 -2819 C ATOM 2297 O LEU A 90 89.384 34.407 196.235 1.00 62.80 O ANISOU 2297 O LEU A 90 7611 7903 8349 -1456 1380 -2756 O ATOM 2298 CB LEU A 90 90.480 34.158 193.143 1.00 69.18 C ANISOU 2298 CB LEU A 90 8570 9076 8640 -1782 1844 -3165 C ATOM 2299 CG LEU A 90 90.115 32.984 192.239 1.00 76.67 C ANISOU 2299 CG LEU A 90 9653 9999 9479 -1786 1878 -3310 C ATOM 2300 CD1 LEU A 90 91.360 32.411 191.582 1.00 84.73 C ANISOU 2300 CD1 LEU A 90 10588 11078 10529 -1745 2144 -3544 C ATOM 2301 CD2 LEU A 90 89.391 31.924 193.050 1.00 73.05 C ANISOU 2301 CD2 LEU A 90 9218 9301 9237 -1607 1699 -3262 C ATOM 2302 N CYS A 91 90.420 36.267 195.510 1.00 41.88 N ANISOU 2302 N CYS A 91 4917 5514 5481 -1723 1586 -2797 N ATOM 2303 CA CYS A 91 90.871 36.609 196.853 1.00 38.12 C ANISOU 2303 CA CYS A 91 4270 4929 5286 -1591 1515 -2712 C ATOM 2304 C CYS A 91 89.712 37.041 197.740 1.00 33.66 C ANISOU 2304 C CYS A 91 3772 4259 4758 -1527 1239 -2438 C ATOM 2305 O CYS A 91 89.732 36.786 198.949 1.00 40.62 O ANISOU 2305 O CYS A 91 4552 5021 5861 -1354 1131 -2345 O ATOM 2306 CB CYS A 91 91.934 37.706 196.784 1.00 51.59 C ANISOU 2306 CB CYS A 91 5856 6771 6975 -1707 1653 -2706 C ATOM 2307 SG CYS A 91 92.879 37.910 198.307 1.00 54.19 S ANISOU 2307 SG CYS A 91 5914 7012 7663 -1538 1603 -2626 S ATOM 2308 N ILE A 92 88.700 37.694 197.164 1.00 41.40 N ANISOU 2308 N ILE A 92 4917 5297 5514 -1658 1125 -2301 N ATOM 2309 CA ILE A 92 87.537 38.103 197.945 1.00 39.69 C ANISOU 2309 CA ILE A 92 4752 4992 5335 -1570 880 -2053 C ATOM 2310 C ILE A 92 86.693 36.890 198.318 1.00 30.48 C ANISOU 2310 C ILE A 92 3620 3723 4240 -1428 767 -2041 C ATOM 2311 O ILE A 92 86.117 36.828 199.412 1.00 29.58 O ANISOU 2311 O ILE A 92 3477 3511 4252 -1291 615 -1887 O ATOM 2312 CB ILE A 92 86.722 39.155 197.169 1.00 31.33 C ANISOU 2312 CB ILE A 92 3838 4020 4048 -1754 786 -1922 C ATOM 2313 CG1 ILE A 92 87.530 40.445 197.018 1.00 31.80 C ANISOU 2313 CG1 ILE A 92 3870 4143 4069 -1904 868 -1868 C ATOM 2314 CG2 ILE A 92 85.398 39.440 197.862 1.00 29.48 C ANISOU 2314 CG2 ILE A 92 3640 3695 3865 -1652 547 -1710 C ATOM 2315 CD1 ILE A 92 86.869 41.481 196.138 1.00 32.72 C ANISOU 2315 CD1 ILE A 92 4138 4342 3952 -2128 786 -1727 C ATOM 2316 N GLY A 93 86.615 35.903 197.423 1.00 32.36 N ANISOU 2316 N GLY A 93 3930 3984 4383 -1474 845 -2201 N ATOM 2317 CA GLY A 93 85.826 34.716 197.711 1.00 39.56 C ANISOU 2317 CA GLY A 93 4890 4782 5359 -1373 737 -2189 C ATOM 2318 C GLY A 93 86.361 33.929 198.891 1.00 41.32 C ANISOU 2318 C GLY A 93 4995 4861 5845 -1185 736 -2191 C ATOM 2319 O GLY A 93 85.603 33.509 199.770 1.00 48.69 O ANISOU 2319 O GLY A 93 5943 5697 6861 -1095 584 -2057 O ATOM 2320 N TRP A 94 87.679 33.720 198.930 1.00 36.98 N ANISOU 2320 N TRP A 94 4318 4305 5427 -1138 908 -2345 N ATOM 2321 CA TRP A 94 88.286 32.987 200.033 1.00 32.23 C ANISOU 2321 CA TRP A 94 3586 3569 5090 -966 896 -2350 C ATOM 2322 C TRP A 94 88.441 33.837 201.285 1.00 30.01 C ANISOU 2322 C TRP A 94 3195 3285 4921 -903 798 -2182 C ATOM 2323 O TRP A 94 88.613 33.284 202.377 1.00 29.42 O ANISOU 2323 O TRP A 94 3041 3106 5031 -776 724 -2128 O ATOM 2324 CB TRP A 94 89.643 32.422 199.612 1.00 45.93 C ANISOU 2324 CB TRP A 94 5201 5295 6957 -920 1105 -2583 C ATOM 2325 CG TRP A 94 89.537 31.365 198.555 1.00 47.92 C ANISOU 2325 CG TRP A 94 5570 5515 7124 -940 1199 -2751 C ATOM 2326 CD1 TRP A 94 89.702 31.528 197.211 1.00 44.13 C ANISOU 2326 CD1 TRP A 94 5169 5168 6430 -1078 1352 -2902 C ATOM 2327 CD2 TRP A 94 89.221 29.982 198.756 1.00 57.22 C ANISOU 2327 CD2 TRP A 94 6819 6512 8409 -832 1144 -2785 C ATOM 2328 NE1 TRP A 94 89.517 30.330 196.563 1.00 56.48 N ANISOU 2328 NE1 TRP A 94 6846 6648 7967 -1053 1394 -3039 N ATOM 2329 CE2 TRP A 94 89.220 29.365 197.489 1.00 58.72 C ANISOU 2329 CE2 TRP A 94 7130 6726 8454 -902 1268 -2973 C ATOM 2330 CE3 TRP A 94 88.942 29.204 199.885 1.00 55.75 C ANISOU 2330 CE3 TRP A 94 6619 6146 8416 -699 1004 -2677 C ATOM 2331 CZ2 TRP A 94 88.951 28.008 197.320 1.00 55.57 C ANISOU 2331 CZ2 TRP A 94 6844 6156 8115 -835 1254 -3065 C ATOM 2332 CZ3 TRP A 94 88.676 27.857 199.715 1.00 52.04 C ANISOU 2332 CZ3 TRP A 94 6264 5508 8002 -643 992 -2755 C ATOM 2333 CH2 TRP A 94 88.683 27.273 198.442 1.00 47.15 C ANISOU 2333 CH2 TRP A 94 5768 4895 7252 -706 1115 -2952 C ATOM 2334 N LEU A 95 88.392 35.163 201.153 1.00 29.05 N ANISOU 2334 N LEU A 95 3082 3272 4684 -997 788 -2097 N ATOM 2335 CA LEU A 95 88.345 36.012 202.337 1.00 33.18 C ANISOU 2335 CA LEU A 95 3549 3785 5274 -937 671 -1915 C ATOM 2336 C LEU A 95 87.004 35.877 203.046 1.00 39.56 C ANISOU 2336 C LEU A 95 4461 4539 6032 -878 482 -1721 C ATOM 2337 O LEU A 95 86.951 35.790 204.279 1.00 32.39 O ANISOU 2337 O LEU A 95 3504 3581 5222 -781 395 -1617 O ATOM 2338 CB LEU A 95 88.607 37.469 201.954 1.00 26.89 C ANISOU 2338 CB LEU A 95 2764 3090 4365 -1058 705 -1863 C ATOM 2339 CG LEU A 95 88.459 38.495 203.079 1.00 25.15 C ANISOU 2339 CG LEU A 95 2531 2852 4173 -1004 577 -1665 C ATOM 2340 CD1 LEU A 95 89.461 38.232 204.194 1.00 25.04 C ANISOU 2340 CD1 LEU A 95 2359 2805 4349 -903 586 -1693 C ATOM 2341 CD2 LEU A 95 88.601 39.911 202.545 1.00 25.39 C ANISOU 2341 CD2 LEU A 95 2610 2946 4089 -1139 598 -1600 C ATOM 2342 N ALA A 96 85.909 35.855 202.280 1.00 38.50 N ANISOU 2342 N ALA A 96 4461 4427 5740 -954 423 -1685 N ATOM 2343 CA ALA A 96 84.591 35.646 202.870 1.00 27.95 C ANISOU 2343 CA ALA A 96 3200 3050 4371 -919 261 -1532 C ATOM 2344 C ALA A 96 84.478 34.259 203.488 1.00 24.62 C ANISOU 2344 C ALA A 96 2772 2526 4056 -841 236 -1557 C ATOM 2345 O ALA A 96 83.843 34.088 204.535 1.00 27.08 O ANISOU 2345 O ALA A 96 3087 2799 4401 -789 135 -1429 O ATOM 2346 CB ALA A 96 83.505 35.857 201.815 1.00 24.91 C ANISOU 2346 CB ALA A 96 2930 2715 3821 -1035 198 -1517 C ATOM 2347 N LEU A 97 85.092 33.254 202.855 1.00 26.38 N ANISOU 2347 N LEU A 97 2993 2697 4334 -842 336 -1728 N ATOM 2348 CA LEU A 97 85.077 31.910 203.424 1.00 27.07 C ANISOU 2348 CA LEU A 97 3085 2649 4552 -768 311 -1755 C ATOM 2349 C LEU A 97 85.883 31.849 204.714 1.00 30.60 C ANISOU 2349 C LEU A 97 3396 3040 5191 -655 300 -1712 C ATOM 2350 O LEU A 97 85.520 31.110 205.637 1.00 26.25 O ANISOU 2350 O LEU A 97 2859 2394 4723 -606 214 -1635 O ATOM 2351 CB LEU A 97 85.609 30.900 202.404 1.00 29.54 C ANISOU 2351 CB LEU A 97 3435 2898 4892 -782 431 -1966 C ATOM 2352 CG LEU A 97 85.250 29.420 202.587 1.00 41.85 C ANISOU 2352 CG LEU A 97 5079 4287 6533 -746 389 -2004 C ATOM 2353 CD1 LEU A 97 85.264 28.707 201.243 1.00 42.71 C ANISOU 2353 CD1 LEU A 97 5300 4371 6556 -811 482 -2197 C ATOM 2354 CD2 LEU A 97 86.195 28.722 203.556 1.00 49.52 C ANISOU 2354 CD2 LEU A 97 5938 5119 7758 -605 411 -2027 C ATOM 2355 N THR A 98 86.971 32.615 204.799 1.00 35.89 N ANISOU 2355 N THR A 98 3934 3769 5934 -631 380 -1764 N ATOM 2356 CA THR A 98 87.754 32.660 206.029 1.00 39.21 C ANISOU 2356 CA THR A 98 4211 4147 6540 -539 346 -1727 C ATOM 2357 C THR A 98 86.942 33.263 207.169 1.00 33.07 C ANISOU 2357 C THR A 98 3477 3406 5681 -534 209 -1524 C ATOM 2358 O THR A 98 86.897 32.713 208.275 1.00 25.66 O ANISOU 2358 O THR A 98 2509 2394 4848 -479 126 -1457 O ATOM 2359 CB THR A 98 89.038 33.460 205.805 1.00 35.06 C ANISOU 2359 CB THR A 98 3530 3693 6098 -547 458 -1837 C ATOM 2360 OG1 THR A 98 89.760 32.908 204.698 1.00 39.96 O ANISOU 2360 OG1 THR A 98 4108 4298 6777 -561 619 -2051 O ATOM 2361 CG2 THR A 98 89.915 33.418 207.046 1.00 28.42 C ANISOU 2361 CG2 THR A 98 2521 2799 5480 -459 402 -1821 C ATOM 2362 N ASP A 99 86.290 34.400 206.912 1.00 32.28 N ANISOU 2362 N ASP A 99 3453 3411 5401 -597 187 -1430 N ATOM 2363 CA ASP A 99 85.532 35.079 207.957 1.00 34.13 C ANISOU 2363 CA ASP A 99 3728 3682 5559 -588 86 -1265 C ATOM 2364 C ASP A 99 84.365 34.236 208.453 1.00 36.74 C ANISOU 2364 C ASP A 99 4136 3964 5858 -593 3 -1187 C ATOM 2365 O ASP A 99 84.031 34.281 209.642 1.00 41.13 O ANISOU 2365 O ASP A 99 4686 4520 6423 -573 -61 -1094 O ATOM 2366 CB ASP A 99 85.022 36.426 207.444 1.00 35.11 C ANISOU 2366 CB ASP A 99 3915 3890 5535 -646 81 -1200 C ATOM 2367 CG ASP A 99 86.144 37.358 207.038 1.00 37.98 C ANISOU 2367 CG ASP A 99 4215 4298 5916 -672 160 -1260 C ATOM 2368 OD1 ASP A 99 87.321 37.014 207.272 1.00 46.62 O ANISOU 2368 OD1 ASP A 99 5195 5377 7143 -641 220 -1353 O ATOM 2369 OD2 ASP A 99 85.849 38.436 206.481 1.00 39.22 O ANISOU 2369 OD2 ASP A 99 4430 4498 5975 -735 159 -1217 O ATOM 2370 N LEU A 100 83.738 33.458 207.567 1.00 32.35 N ANISOU 2370 N LEU A 100 3660 3371 5260 -640 5 -1233 N ATOM 2371 CA LEU A 100 82.588 32.661 207.981 1.00 24.63 C ANISOU 2371 CA LEU A 100 2759 2348 4249 -675 -74 -1161 C ATOM 2372 C LEU A 100 83.010 31.496 208.868 1.00 26.73 C ANISOU 2372 C LEU A 100 2996 2492 4669 -631 -94 -1172 C ATOM 2373 O LEU A 100 82.367 31.223 209.888 1.00 22.63 O ANISOU 2373 O LEU A 100 2493 1956 4149 -650 -162 -1074 O ATOM 2374 CB LEU A 100 81.827 32.158 206.756 1.00 28.26 C ANISOU 2374 CB LEU A 100 3320 2797 4620 -760 -81 -1215 C ATOM 2375 CG LEU A 100 80.583 31.321 207.061 1.00 43.88 C ANISOU 2375 CG LEU A 100 5376 4732 6564 -831 -167 -1149 C ATOM 2376 CD1 LEU A 100 79.630 32.097 207.959 1.00 41.72 C ANISOU 2376 CD1 LEU A 100 5074 4547 6230 -847 -227 -1010 C ATOM 2377 CD2 LEU A 100 79.887 30.902 205.776 1.00 38.63 C ANISOU 2377 CD2 LEU A 100 4806 4062 5808 -931 -193 -1213 C ATOM 2378 N VAL A 101 84.091 30.802 208.502 1.00 36.92 N ANISOU 2378 N VAL A 101 4234 3684 6109 -575 -35 -1297 N ATOM 2379 CA VAL A 101 84.566 29.681 209.311 1.00 32.51 C ANISOU 2379 CA VAL A 101 3638 2966 5747 -517 -71 -1305 C ATOM 2380 C VAL A 101 84.976 30.160 210.699 1.00 34.55 C ANISOU 2380 C VAL A 101 3796 3246 6086 -474 -140 -1208 C ATOM 2381 O VAL A 101 84.691 29.502 211.708 1.00 33.11 O ANISOU 2381 O VAL A 101 3627 2973 5981 -480 -225 -1122 O ATOM 2382 CB VAL A 101 85.720 28.955 208.594 1.00 33.82 C ANISOU 2382 CB VAL A 101 3744 3013 6091 -441 17 -1477 C ATOM 2383 CG1 VAL A 101 86.321 27.885 209.492 1.00 32.54 C ANISOU 2383 CG1 VAL A 101 3526 2652 6186 -349 -40 -1467 C ATOM 2384 CG2 VAL A 101 85.231 28.343 207.289 1.00 28.99 C ANISOU 2384 CG2 VAL A 101 3268 2369 5378 -502 78 -1584 C ATOM 2385 N GLY A 102 85.646 31.313 210.773 1.00 37.05 N ANISOU 2385 N GLY A 102 4021 3676 6380 -450 -109 -1218 N ATOM 2386 CA GLY A 102 86.018 31.862 212.067 1.00 22.90 C ANISOU 2386 CA GLY A 102 2154 1918 4629 -433 -182 -1134 C ATOM 2387 C GLY A 102 84.824 32.205 212.935 1.00 28.26 C ANISOU 2387 C GLY A 102 2925 2670 5142 -501 -244 -997 C ATOM 2388 O GLY A 102 84.888 32.086 214.161 1.00 21.94 O ANISOU 2388 O GLY A 102 2096 1853 4389 -513 -325 -922 O ATOM 2389 N GLN A 103 83.720 32.630 212.317 1.00 27.92 N ANISOU 2389 N GLN A 103 2981 2708 4921 -554 -212 -969 N ATOM 2390 CA GLN A 103 82.508 32.929 213.070 1.00 26.06 C ANISOU 2390 CA GLN A 103 2804 2538 4561 -617 -254 -867 C ATOM 2391 C GLN A 103 81.753 31.664 213.460 1.00 29.18 C ANISOU 2391 C GLN A 103 3249 2844 4995 -679 -304 -825 C ATOM 2392 O GLN A 103 81.117 31.629 214.520 1.00 21.03 O ANISOU 2392 O GLN A 103 2221 1840 3928 -739 -347 -745 O ATOM 2393 CB GLN A 103 81.603 33.856 212.258 1.00 23.59 C ANISOU 2393 CB GLN A 103 2541 2321 4100 -645 -222 -854 C ATOM 2394 CG GLN A 103 82.195 35.235 212.011 1.00 22.07 C ANISOU 2394 CG GLN A 103 2319 2199 3866 -608 -182 -870 C ATOM 2395 CD GLN A 103 81.563 35.937 210.825 1.00 25.89 C ANISOU 2395 CD GLN A 103 2848 2726 4263 -633 -160 -877 C ATOM 2396 OE1 GLN A 103 80.691 35.385 210.154 1.00 18.61 O ANISOU 2396 OE1 GLN A 103 1971 1794 3304 -680 -181 -876 O ATOM 2397 NE2 GLN A 103 82.004 37.161 210.558 1.00 31.41 N ANISOU 2397 NE2 GLN A 103 3536 3465 4935 -619 -131 -884 N ATOM 2398 N LEU A 104 81.813 30.622 212.625 1.00 22.16 N ANISOU 2398 N LEU A 104 2402 1841 4175 -680 -292 -885 N ATOM 2399 CA LEU A 104 81.123 29.374 212.932 1.00 31.48 C ANISOU 2399 CA LEU A 104 3653 2908 5400 -755 -339 -846 C ATOM 2400 C LEU A 104 81.859 28.552 213.984 1.00 44.15 C ANISOU 2400 C LEU A 104 5214 4360 7201 -722 -405 -804 C ATOM 2401 O LEU A 104 81.226 27.778 214.711 1.00 25.49 O ANISOU 2401 O LEU A 104 2899 1921 4864 -805 -461 -717 O ATOM 2402 CB LEU A 104 80.941 28.543 211.659 1.00 24.49 C ANISOU 2402 CB LEU A 104 2855 1933 4518 -779 -307 -937 C ATOM 2403 CG LEU A 104 80.061 29.131 210.554 1.00 34.32 C ANISOU 2403 CG LEU A 104 4154 3298 5586 -844 -287 -958 C ATOM 2404 CD1 LEU A 104 80.049 28.217 209.337 1.00 25.42 C ANISOU 2404 CD1 LEU A 104 3122 2068 4467 -881 -268 -1066 C ATOM 2405 CD2 LEU A 104 78.645 29.382 211.055 1.00 32.33 C ANISOU 2405 CD2 LEU A 104 3920 3144 5218 -952 -336 -853 C ATOM 2406 N LEU A 105 83.182 28.696 214.074 1.00 43.80 N ANISOU 2406 N LEU A 105 5068 4261 7314 -612 -412 -853 N ATOM 2407 CA LEU A 105 83.972 27.963 215.056 1.00 38.73 C ANISOU 2407 CA LEU A 105 4359 3449 6906 -567 -516 -790 C ATOM 2408 C LEU A 105 83.990 28.624 216.426 1.00 35.47 C ANISOU 2408 C LEU A 105 3888 3134 6456 -618 -606 -670 C ATOM 2409 O LEU A 105 84.436 27.994 217.391 1.00 39.22 O ANISOU 2409 O LEU A 105 4322 3475 7106 -621 -739 -560 O ATOM 2410 CB LEU A 105 85.412 27.802 214.564 1.00 30.85 C ANISOU 2410 CB LEU A 105 3243 2343 6137 -427 -501 -901 C ATOM 2411 CG LEU A 105 85.677 26.805 213.436 1.00 33.86 C ANISOU 2411 CG LEU A 105 3674 2566 6626 -361 -422 -1027 C ATOM 2412 CD1 LEU A 105 87.106 26.940 212.944 1.00 30.78 C ANISOU 2412 CD1 LEU A 105 3128 2128 6437 -224 -369 -1162 C ATOM 2413 CD2 LEU A 105 85.404 25.386 213.905 1.00 37.90 C ANISOU 2413 CD2 LEU A 105 4279 2834 7287 -360 -502 -941 C ATOM 2414 N THR A 106 83.515 29.860 216.539 1.00 40.60 N ANISOU 2414 N THR A 106 4543 4001 6883 -663 -549 -676 N ATOM 2415 CA THR A 106 83.704 30.661 217.741 1.00 39.09 C ANISOU 2415 CA THR A 106 4298 3931 6625 -709 -608 -607 C ATOM 2416 C THR A 106 82.400 30.999 218.445 1.00 37.47 C ANISOU 2416 C THR A 106 4156 3852 6227 -835 -589 -540 C ATOM 2417 O THR A 106 82.291 30.813 219.663 1.00 27.50 O ANISOU 2417 O THR A 106 2872 2609 4966 -925 -677 -441 O ATOM 2418 CB THR A 106 84.450 31.955 217.378 1.00 30.46 C ANISOU 2418 CB THR A 106 3149 2969 5455 -650 -544 -690 C ATOM 2419 OG1 THR A 106 85.722 31.632 216.803 1.00 46.68 O ANISOU 2419 OG1 THR A 106 5101 4920 7715 -551 -555 -764 O ATOM 2420 CG2 THR A 106 84.664 32.804 218.601 1.00 33.42 C ANISOU 2420 CG2 THR A 106 3488 3476 5732 -713 -598 -639 C ATOM 2421 N THR A 107 81.407 31.486 217.710 1.00 35.07 N ANISOU 2421 N THR A 107 3914 3639 5772 -851 -493 -583 N ATOM 2422 CA THR A 107 80.160 31.990 218.276 1.00 37.47 C ANISOU 2422 CA THR A 107 4238 4074 5925 -953 -465 -545 C ATOM 2423 C THR A 107 79.312 30.916 218.962 1.00 37.04 C ANISOU 2423 C THR A 107 4202 3975 5895 -1086 -505 -459 C ATOM 2424 O THR A 107 78.760 31.187 220.036 1.00 33.25 O ANISOU 2424 O THR A 107 3688 3599 5345 -1194 -513 -411 O ATOM 2425 CB THR A 107 79.338 32.685 217.187 1.00 36.71 C ANISOU 2425 CB THR A 107 4173 4047 5726 -921 -393 -590 C ATOM 2426 OG1 THR A 107 80.209 33.463 216.356 1.00 29.07 O ANISOU 2426 OG1 THR A 107 3199 3083 4764 -809 -356 -655 O ATOM 2427 CG2 THR A 107 78.298 33.601 217.817 1.00 23.45 C ANISOU 2427 CG2 THR A 107 2464 2499 3946 -976 -373 -571 C ATOM 2428 N PRO A 108 79.153 29.710 218.393 1.00 23.95 N ANISOU 2428 N PRO A 108 2599 2166 4333 -1098 -523 -441 N ATOM 2429 CA PRO A 108 78.318 28.704 219.076 1.00 25.46 C ANISOU 2429 CA PRO A 108 2819 2302 4551 -1243 -557 -340 C ATOM 2430 C PRO A 108 78.792 28.347 220.475 1.00 26.76 C ANISOU 2430 C PRO A 108 2953 2421 4794 -1307 -669 -194 C ATOM 2431 O PRO A 108 77.966 27.986 221.322 1.00 27.85 O ANISOU 2431 O PRO A 108 3094 2604 4883 -1456 -684 -81 O ATOM 2432 CB PRO A 108 78.392 27.495 218.133 1.00 26.49 C ANISOU 2432 CB PRO A 108 3036 2234 4794 -1220 -567 -360 C ATOM 2433 CG PRO A 108 78.625 28.088 216.801 1.00 30.82 C ANISOU 2433 CG PRO A 108 3596 2831 5283 -1115 -501 -490 C ATOM 2434 CD PRO A 108 79.551 29.241 217.052 1.00 34.88 C ANISOU 2434 CD PRO A 108 4031 3437 5784 -1007 -497 -521 C ATOM 2435 N VAL A 109 80.095 28.435 220.748 1.00 33.21 N ANISOU 2435 N VAL A 109 3731 3161 5724 -1213 -764 -168 N ATOM 2436 CA VAL A 109 80.583 28.168 222.098 1.00 36.78 C ANISOU 2436 CA VAL A 109 4157 3597 6220 -1299 -922 19 C ATOM 2437 C VAL A 109 80.124 29.260 223.057 1.00 34.80 C ANISOU 2437 C VAL A 109 3857 3610 5754 -1408 -890 15 C ATOM 2438 O VAL A 109 79.731 28.981 224.196 1.00 32.21 O ANISOU 2438 O VAL A 109 3546 3360 5333 -1577 -965 189 O ATOM 2439 CB VAL A 109 82.116 28.024 222.094 1.00 32.34 C ANISOU 2439 CB VAL A 109 3531 2900 5856 -1175 -1057 44 C ATOM 2440 CG1 VAL A 109 82.631 27.793 223.505 1.00 37.92 C ANISOU 2440 CG1 VAL A 109 4227 3669 6510 -1238 -1222 275 C ATOM 2441 CG2 VAL A 109 82.542 26.891 221.175 1.00 30.02 C ANISOU 2441 CG2 VAL A 109 3282 2321 5805 -1058 -1071 26 C ATOM 2442 N VAL A 110 80.162 30.517 222.610 1.00 28.30 N ANISOU 2442 N VAL A 110 2990 2932 4832 -1328 -772 -172 N ATOM 2443 CA VAL A 110 79.777 31.633 223.469 1.00 28.27 C ANISOU 2443 CA VAL A 110 2941 3147 4652 -1413 -729 -220 C ATOM 2444 C VAL A 110 78.301 31.542 223.836 1.00 43.85 C ANISOU 2444 C VAL A 110 4911 5222 6529 -1548 -644 -193 C ATOM 2445 O VAL A 110 77.907 31.839 224.971 1.00 49.53 O ANISOU 2445 O VAL A 110 5618 6114 7087 -1694 -651 -124 O ATOM 2446 CB VAL A 110 80.106 32.971 222.779 1.00 30.36 C ANISOU 2446 CB VAL A 110 3192 3494 4852 -1296 -622 -404 C ATOM 2447 CG1 VAL A 110 79.714 34.142 223.668 1.00 28.38 C ANISOU 2447 CG1 VAL A 110 2907 3427 4448 -1388 -584 -475 C ATOM 2448 CG2 VAL A 110 81.584 33.032 222.414 1.00 28.92 C ANISOU 2448 CG2 VAL A 110 2992 3233 4766 -1174 -690 -419 C ATOM 2449 N ILE A 111 77.464 31.123 222.884 1.00 42.99 N ANISOU 2449 N ILE A 111 4816 5048 6469 -1520 -554 -243 N ATOM 2450 CA ILE A 111 76.026 31.054 223.125 1.00 33.34 C ANISOU 2450 CA ILE A 111 3545 3924 5200 -1626 -473 -227 C ATOM 2451 C ILE A 111 75.703 29.998 224.176 1.00 39.58 C ANISOU 2451 C ILE A 111 4385 4725 5928 -1812 -546 2 C ATOM 2452 O ILE A 111 74.832 30.202 225.031 1.00 42.06 O ANISOU 2452 O ILE A 111 4660 5231 6089 -1955 -484 61 O ATOM 2453 CB ILE A 111 75.283 30.794 221.802 1.00 33.76 C ANISOU 2453 CB ILE A 111 3609 3931 5287 -1581 -386 -326 C ATOM 2454 CG1 ILE A 111 75.547 31.936 220.817 1.00 32.56 C ANISOU 2454 CG1 ILE A 111 3507 3834 5029 -1459 -408 -363 C ATOM 2455 CG2 ILE A 111 73.790 30.625 222.044 1.00 31.95 C ANISOU 2455 CG2 ILE A 111 3276 3762 5102 -1655 -345 -278 C ATOM 2456 CD1 ILE A 111 74.921 31.735 219.456 1.00 26.38 C ANISOU 2456 CD1 ILE A 111 2759 3011 4255 -1405 -399 -381 C ATOM 2457 N VAL A 112 76.398 28.858 224.136 1.00 29.63 N ANISOU 2457 N VAL A 112 3216 3267 4775 -1819 -669 143 N ATOM 2458 CA VAL A 112 76.150 27.800 225.115 1.00 39.03 C ANISOU 2458 CA VAL A 112 4478 4434 5919 -2006 -756 400 C ATOM 2459 C VAL A 112 76.488 28.280 226.522 1.00 43.71 C ANISOU 2459 C VAL A 112 5064 5238 6306 -2142 -813 528 C ATOM 2460 O VAL A 112 75.752 28.010 227.479 1.00 40.90 O ANISOU 2460 O VAL A 112 4730 5044 5767 -2325 -775 672 O ATOM 2461 CB VAL A 112 76.937 26.530 224.742 1.00 33.09 C ANISOU 2461 CB VAL A 112 3828 3373 5373 -1952 -895 526 C ATOM 2462 CG1 VAL A 112 76.855 25.502 225.859 1.00 35.88 C ANISOU 2462 CG1 VAL A 112 4273 3676 5684 -2142 -1016 836 C ATOM 2463 CG2 VAL A 112 76.410 25.943 223.444 1.00 32.64 C ANISOU 2463 CG2 VAL A 112 3804 3160 5438 -1871 -807 387 C ATOM 2464 N VAL A 113 77.606 28.997 226.671 1.00 41.17 N ANISOU 2464 N VAL A 113 4727 4951 5965 -2004 -869 453 N ATOM 2465 CA VAL A 113 78.012 29.485 227.988 1.00 44.61 C ANISOU 2465 CA VAL A 113 5181 5615 6155 -2070 -904 529 C ATOM 2466 C VAL A 113 76.977 30.459 228.541 1.00 44.79 C ANISOU 2466 C VAL A 113 5156 5922 5941 -2173 -722 399 C ATOM 2467 O VAL A 113 76.693 30.470 229.746 1.00 45.28 O ANISOU 2467 O VAL A 113 5255 6199 5749 -2325 -701 505 O ATOM 2468 CB VAL A 113 79.412 30.123 227.912 1.00 44.18 C ANISOU 2468 CB VAL A 113 5097 5542 6146 -1915 -1003 445 C ATOM 2469 CG1 VAL A 113 79.835 30.661 229.271 1.00 34.23 C ANISOU 2469 CG1 VAL A 113 3863 4536 4608 -2010 -1055 507 C ATOM 2470 CG2 VAL A 113 80.429 29.113 227.401 1.00 38.91 C ANISOU 2470 CG2 VAL A 113 4448 4604 5732 -1793 -1167 573 C ATOM 2471 N TYR A 114 76.391 31.285 227.672 1.00 41.26 N ANISOU 2471 N TYR A 114 4624 5483 5570 -2087 -584 170 N ATOM 2472 CA TYR A 114 75.350 32.209 228.113 1.00 42.39 C ANISOU 2472 CA TYR A 114 4699 5869 5537 -2145 -397 33 C ATOM 2473 C TYR A 114 74.105 31.458 228.569 1.00 43.18 C ANISOU 2473 C TYR A 114 4777 6082 5547 -2333 -314 171 C ATOM 2474 O TYR A 114 73.589 31.698 229.667 1.00 52.44 O ANISOU 2474 O TYR A 114 5947 7505 6474 -2465 -213 198 O ATOM 2475 CB TYR A 114 75.004 33.189 226.992 1.00 44.08 C ANISOU 2475 CB TYR A 114 4822 6033 5894 -1991 -295 -206 C ATOM 2476 CG TYR A 114 75.822 34.463 226.992 1.00 40.24 C ANISOU 2476 CG TYR A 114 4341 5569 5379 -1865 -281 -393 C ATOM 2477 CD1 TYR A 114 75.441 35.553 227.765 1.00 35.89 C ANISOU 2477 CD1 TYR A 114 3774 5218 4646 -1881 -146 -540 C ATOM 2478 CD2 TYR A 114 76.965 34.582 226.213 1.00 42.46 C ANISOU 2478 CD2 TYR A 114 4644 5669 5819 -1740 -391 -434 C ATOM 2479 CE1 TYR A 114 76.180 36.723 227.767 1.00 37.05 C ANISOU 2479 CE1 TYR A 114 3946 5356 4775 -1788 -136 -719 C ATOM 2480 CE2 TYR A 114 77.710 35.748 226.207 1.00 39.94 C ANISOU 2480 CE2 TYR A 114 4329 5368 5477 -1657 -380 -596 C ATOM 2481 CZ TYR A 114 77.313 36.815 226.986 1.00 38.50 C ANISOU 2481 CZ TYR A 114 4150 5360 5119 -1688 -260 -736 C ATOM 2482 OH TYR A 114 78.051 37.978 226.984 1.00 34.53 O ANISOU 2482 OH TYR A 114 3672 4847 4602 -1626 -251 -904 O ATOM 2483 N LEU A 115 73.606 30.543 227.734 1.00 40.72 N ANISOU 2483 N LEU A 115 4450 5598 5422 -2365 -347 251 N ATOM 2484 CA LEU A 115 72.356 29.852 228.033 1.00 44.05 C ANISOU 2484 CA LEU A 115 4840 6113 5782 -2523 -259 367 C ATOM 2485 C LEU A 115 72.484 28.882 229.200 1.00 44.08 C ANISOU 2485 C LEU A 115 4948 6174 5626 -2759 -334 649 C ATOM 2486 O LEU A 115 71.464 28.507 229.789 1.00 50.07 O ANISOU 2486 O LEU A 115 5681 7095 6250 -2921 -230 745 O ATOM 2487 CB LEU A 115 71.862 29.107 226.791 1.00 34.59 C ANISOU 2487 CB LEU A 115 3638 4683 4821 -2420 -281 350 C ATOM 2488 CG LEU A 115 71.638 29.964 225.543 1.00 32.35 C ANISOU 2488 CG LEU A 115 3260 4343 4688 -2205 -226 119 C ATOM 2489 CD1 LEU A 115 71.130 29.117 224.388 1.00 32.19 C ANISOU 2489 CD1 LEU A 115 3247 4130 4855 -2153 -255 111 C ATOM 2490 CD2 LEU A 115 70.680 31.108 225.837 1.00 32.49 C ANISOU 2490 CD2 LEU A 115 3130 4624 4593 -2202 -64 -7 C ATOM 2491 N SER A 116 73.701 28.465 229.546 1.00 44.71 N ANISOU 2491 N SER A 116 5152 6119 5717 -2719 -512 785 N ATOM 2492 CA SER A 116 73.905 27.531 230.646 1.00 41.00 C ANISOU 2492 CA SER A 116 4803 5678 5099 -2900 -615 1087 C ATOM 2493 C SER A 116 74.051 28.219 231.995 1.00 55.69 C ANISOU 2493 C SER A 116 6685 7864 6610 -2992 -566 1103 C ATOM 2494 O SER A 116 73.775 27.591 233.024 1.00 52.90 O ANISOU 2494 O SER A 116 6410 7645 6046 -3208 -584 1344 O ATOM 2495 CB SER A 116 75.144 26.667 230.389 1.00 43.60 C ANISOU 2495 CB SER A 116 5245 5696 5627 -2793 -851 1253 C ATOM 2496 OG SER A 116 76.309 27.465 230.276 1.00 39.66 O ANISOU 2496 OG SER A 116 4723 5195 5151 -2593 -925 1117 O ATOM 2497 N LYS A 117 74.481 29.479 232.012 1.00 67.19 N ANISOU 2497 N LYS A 117 6047 9380 10103 -1691 188 3053 N ATOM 2498 CA LYS A 117 74.743 30.218 233.248 1.00 76.27 C ANISOU 2498 CA LYS A 117 7197 10853 10931 -1797 397 3044 C ATOM 2499 C LYS A 117 75.747 29.482 234.133 1.00 82.21 C ANISOU 2499 C LYS A 117 8010 11718 11507 -1936 222 3307 C ATOM 2500 O LYS A 117 76.722 28.913 233.642 1.00 80.59 O ANISOU 2500 O LYS A 117 7839 11334 11447 -1900 -37 3378 O ATOM 2501 CB LYS A 117 73.446 30.468 234.024 1.00 74.98 C ANISOU 2501 CB LYS A 117 6979 10878 10632 -1878 663 3060 C ATOM 2502 CG LYS A 117 72.435 31.344 233.303 1.00 71.26 C ANISOU 2502 CG LYS A 117 6432 10326 10316 -1753 854 2802 C ATOM 2503 CD LYS A 117 71.239 31.636 234.196 1.00 70.13 C ANISOU 2503 CD LYS A 117 6222 10383 10042 -1843 1138 2807 C ATOM 2504 CE LYS A 117 70.160 32.407 233.455 1.00 69.42 C ANISOU 2504 CE LYS A 117 6039 10192 10146 -1725 1292 2583 C ATOM 2505 NZ LYS A 117 68.950 32.612 234.301 1.00 77.43 N ANISOU 2505 NZ LYS A 117 6967 11379 11074 -1815 1567 2588 N ATOM 2506 N ARG A 119 79.394 28.357 234.587 1.00 69.84 N ANISOU 2506 N ARG A 119 6652 10049 9836 -1936 -449 3535 N ATOM 2507 CA ARG A 119 80.796 28.761 234.587 1.00 72.01 C ANISOU 2507 CA ARG A 119 7007 10329 10023 -1832 -585 3355 C ATOM 2508 C ARG A 119 81.572 28.033 233.497 1.00 72.97 C ANISOU 2508 C ARG A 119 7127 10093 10505 -1687 -858 3339 C ATOM 2509 O ARG A 119 81.302 26.868 233.208 1.00 73.00 O ANISOU 2509 O ARG A 119 7106 9882 10750 -1717 -1029 3583 O ATOM 2510 CB ARG A 119 81.442 28.492 235.949 1.00 72.79 C ANISOU 2510 CB ARG A 119 7189 10689 9779 -1968 -687 3560 C ATOM 2511 CG ARG A 119 80.631 28.958 237.147 1.00 78.02 C ANISOU 2511 CG ARG A 119 7866 11724 10055 -2150 -428 3631 C ATOM 2512 CD ARG A 119 79.882 27.802 237.792 1.00 85.68 C ANISOU 2512 CD ARG A 119 8817 12735 11002 -2333 -486 4068 C ATOM 2513 NE ARG A 119 79.261 28.192 239.054 1.00 96.69 N ANISOU 2513 NE ARG A 119 10238 14528 11973 -2525 -246 4152 N ATOM 2514 CZ ARG A 119 79.895 28.211 240.222 1.00102.48 C ANISOU 2514 CZ ARG A 119 11074 15555 12308 -2655 -310 4267 C ATOM 2515 NH1 ARG A 119 81.173 27.863 240.290 1.00 97.91 N ANISOU 2515 NH1 ARG A 119 10565 14906 11729 -2603 -622 4327 N ATOM 2516 NH2 ARG A 119 79.253 28.580 241.322 1.00107.45 N ANISOU 2516 NH2 ARG A 119 11731 16559 12537 -2838 -62 4320 N ATOM 2517 N TRP A 120 82.540 28.729 232.894 1.00 69.35 N ANISOU 2517 N TRP A 120 6692 9568 10088 -1534 -887 3043 N ATOM 2518 CA TRP A 120 83.382 28.099 231.882 1.00 61.62 C ANISOU 2518 CA TRP A 120 5709 8274 9429 -1392 -1120 2993 C ATOM 2519 C TRP A 120 84.180 26.943 232.468 1.00 65.92 C ANISOU 2519 C TRP A 120 6280 8749 10017 -1430 -1410 3282 C ATOM 2520 O TRP A 120 84.456 25.960 231.770 1.00 62.22 O ANISOU 2520 O TRP A 120 5790 7977 9873 -1359 -1611 3366 O ATOM 2521 CB TRP A 120 84.325 29.135 231.264 1.00 49.54 C ANISOU 2521 CB TRP A 120 4194 6732 7896 -1241 -1073 2633 C ATOM 2522 CG TRP A 120 85.073 28.642 230.057 1.00 49.20 C ANISOU 2522 CG TRP A 120 4136 6377 8182 -1086 -1246 2523 C ATOM 2523 CD1 TRP A 120 86.103 27.744 230.038 1.00 43.44 C ANISOU 2523 CD1 TRP A 120 3407 5492 7607 -1031 -1503 2629 C ATOM 2524 CD2 TRP A 120 84.863 29.037 228.695 1.00 47.90 C ANISOU 2524 CD2 TRP A 120 3948 6026 8226 -966 -1165 2278 C ATOM 2525 NE1 TRP A 120 86.535 27.545 228.749 1.00 41.69 N ANISOU 2525 NE1 TRP A 120 3164 4999 7677 -884 -1565 2442 N ATOM 2526 CE2 TRP A 120 85.793 28.329 227.906 1.00 43.80 C ANISOU 2526 CE2 TRP A 120 3426 5255 7963 -850 -1364 2229 C ATOM 2527 CE3 TRP A 120 83.977 29.916 228.065 1.00 43.06 C ANISOU 2527 CE3 TRP A 120 3312 5438 7612 -946 -947 2103 C ATOM 2528 CZ2 TRP A 120 85.861 28.473 226.522 1.00 37.60 C ANISOU 2528 CZ2 TRP A 120 2631 4266 7390 -731 -1340 2003 C ATOM 2529 CZ3 TRP A 120 84.046 30.058 226.691 1.00 36.64 C ANISOU 2529 CZ3 TRP A 120 2487 4417 7016 -828 -950 1908 C ATOM 2530 CH2 TRP A 120 84.981 29.340 225.935 1.00 36.03 C ANISOU 2530 CH2 TRP A 120 2423 4114 7152 -729 -1140 1854 C ATOM 2531 N GLU A 121 84.547 27.037 233.747 1.00 66.10 N ANISOU 2531 N GLU A 121 6347 9046 9722 -1546 -1440 3436 N ATOM 2532 CA GLU A 121 85.382 26.013 234.366 1.00 65.10 C ANISOU 2532 CA GLU A 121 6238 8872 9624 -1581 -1738 3732 C ATOM 2533 C GLU A 121 84.635 24.690 234.487 1.00 69.26 C ANISOU 2533 C GLU A 121 6746 9230 10339 -1681 -1860 4110 C ATOM 2534 O GLU A 121 85.163 23.632 234.122 1.00 64.09 O ANISOU 2534 O GLU A 121 6071 8287 9994 -1616 -2116 4266 O ATOM 2535 CB GLU A 121 85.866 26.492 235.737 1.00 67.48 C ANISOU 2535 CB GLU A 121 6599 9548 9494 -1707 -1740 3815 C ATOM 2536 CG GLU A 121 86.767 27.723 235.694 1.00 74.33 C ANISOU 2536 CG GLU A 121 7485 10564 10194 -1622 -1665 3454 C ATOM 2537 CD GLU A 121 86.003 29.009 235.431 1.00 75.13 C ANISOU 2537 CD GLU A 121 7592 10802 10154 -1617 -1319 3128 C ATOM 2538 OE1 GLU A 121 84.914 29.187 236.017 1.00 76.35 O ANISOU 2538 OE1 GLU A 121 7759 11144 10107 -1751 -1117 3215 O ATOM 2539 OE2 GLU A 121 86.489 29.838 234.633 1.00 71.50 O ANISOU 2539 OE2 GLU A 121 7114 10254 9799 -1478 -1246 2794 O ATOM 2540 N HIS A 122 83.403 24.726 235.001 1.00 73.58 N ANISOU 2540 N HIS A 122 7290 9944 10724 -1840 -1673 4259 N ATOM 2541 CA HIS A 122 82.625 23.500 235.141 1.00 75.07 C ANISOU 2541 CA HIS A 122 7452 9979 11093 -1960 -1774 4629 C ATOM 2542 C HIS A 122 82.156 22.959 233.797 1.00 61.81 C ANISOU 2542 C HIS A 122 5713 7914 9857 -1858 -1814 4535 C ATOM 2543 O HIS A 122 81.829 21.771 233.701 1.00 60.86 O ANISOU 2543 O HIS A 122 5569 7589 9966 -1880 -1970 4723 O ATOM 2544 CB HIS A 122 81.432 23.737 236.066 1.00 81.24 C ANISOU 2544 CB HIS A 122 8229 11067 11571 -2168 -1537 4804 C ATOM 2545 CG HIS A 122 81.805 23.839 237.513 1.00 80.96 C ANISOU 2545 CG HIS A 122 8267 11390 11105 -2323 -1555 5018 C ATOM 2546 ND1 HIS A 122 81.071 24.568 238.424 1.00 80.43 N ANISOU 2546 ND1 HIS A 122 8220 11710 10632 -2478 -1275 5010 N ATOM 2547 CD2 HIS A 122 82.836 23.301 238.206 1.00 78.85 C ANISOU 2547 CD2 HIS A 122 8055 11163 10743 -2351 -1825 5244 C ATOM 2548 CE1 HIS A 122 81.635 24.476 239.615 1.00 78.79 C ANISOU 2548 CE1 HIS A 122 8092 11779 10066 -2607 -1371 5215 C ATOM 2549 NE2 HIS A 122 82.707 23.712 239.510 1.00 79.48 N ANISOU 2549 NE2 HIS A 122 8198 11664 10335 -2534 -1716 5375 N ATOM 2550 N ILE A 123 82.112 23.799 232.763 1.00 58.46 N ANISOU 2550 N ILE A 123 5267 7421 9523 -1717 -1674 4153 N ATOM 2551 CA ILE A 123 81.815 23.311 231.421 1.00 60.29 C ANISOU 2551 CA ILE A 123 5457 7300 10149 -1617 -1737 4032 C ATOM 2552 C ILE A 123 83.068 22.730 230.777 1.00 68.72 C ANISOU 2552 C ILE A 123 6544 8085 11482 -1457 -1985 3946 C ATOM 2553 O ILE A 123 83.005 21.724 230.061 1.00 64.70 O ANISOU 2553 O ILE A 123 6013 7272 11298 -1405 -2136 3959 O ATOM 2554 CB ILE A 123 81.211 24.444 230.568 1.00 55.09 C ANISOU 2554 CB ILE A 123 4767 6698 9468 -1542 -1493 3688 C ATOM 2555 CG1 ILE A 123 79.860 24.885 231.133 1.00 55.01 C ANISOU 2555 CG1 ILE A 123 4720 6925 9255 -1666 -1248 3759 C ATOM 2556 CG2 ILE A 123 81.065 24.012 229.115 1.00 47.60 C ANISOU 2556 CG2 ILE A 123 3811 5420 8856 -1406 -1577 3500 C ATOM 2557 CD1 ILE A 123 79.248 26.052 230.392 1.00 47.70 C ANISOU 2557 CD1 ILE A 123 3768 6060 8295 -1568 -1011 3429 C ATOM 2558 N ASP A 124 84.226 23.344 231.034 1.00 71.71 N ANISOU 2558 N ASP A 124 6951 8587 11709 -1362 -2016 3795 N ATOM 2559 CA ASP A 124 85.498 22.977 230.414 1.00 73.19 C ANISOU 2559 CA ASP A 124 7132 8540 12137 -1193 -2213 3666 C ATOM 2560 C ASP A 124 86.494 22.608 231.509 1.00 81.56 C ANISOU 2560 C ASP A 124 8201 9706 13080 -1220 -2412 3901 C ATOM 2561 O ASP A 124 87.289 23.452 231.948 1.00 89.96 O ANISOU 2561 O ASP A 124 9278 10996 13907 -1186 -2380 3764 O ATOM 2562 CB ASP A 124 86.026 24.123 229.553 1.00 64.90 C ANISOU 2562 CB ASP A 124 6081 7527 11050 -1044 -2068 3244 C ATOM 2563 CG ASP A 124 87.274 23.750 228.781 1.00 54.85 C ANISOU 2563 CG ASP A 124 4786 6008 10048 -867 -2234 3083 C ATOM 2564 OD1 ASP A 124 87.604 22.548 228.712 1.00 57.24 O ANISOU 2564 OD1 ASP A 124 5125 6060 10565 -869 -2369 3180 O ATOM 2565 OD2 ASP A 124 87.926 24.668 228.241 1.00 52.34 O ANISOU 2565 OD2 ASP A 124 4475 5746 9668 -757 -2126 2766 O ATOM 2566 N PRO A 125 86.485 21.348 231.977 1.00 75.07 N ANISOU 2566 N PRO A 125 7382 8742 12398 -1303 -2575 4173 N ATOM 2567 CA PRO A 125 87.482 20.894 232.953 1.00 71.42 C ANISOU 2567 CA PRO A 125 6935 8360 11844 -1335 -2744 4340 C ATOM 2568 C PRO A 125 88.867 20.702 232.339 1.00 64.30 C ANISOU 2568 C PRO A 125 6027 7242 11162 -1158 -2836 4084 C ATOM 2569 O PRO A 125 88.965 20.290 231.183 1.00 60.11 O ANISOU 2569 O PRO A 125 5487 6414 10939 -1048 -2809 3844 O ATOM 2570 CB PRO A 125 86.914 19.558 233.437 1.00 67.52 C ANISOU 2570 CB PRO A 125 6423 7754 11477 -1469 -2842 4620 C ATOM 2571 CG PRO A 125 86.087 19.071 232.301 1.00 60.27 C ANISOU 2571 CG PRO A 125 5468 6571 10859 -1431 -2776 4461 C ATOM 2572 CD PRO A 125 85.501 20.298 231.659 1.00 60.72 C ANISOU 2572 CD PRO A 125 5537 6731 10802 -1385 -2579 4267 C ATOM 2573 N GLY A 127 90.726 22.873 230.782 1.00 52.13 N ANISOU 2573 N GLY A 127 4478 5745 9587 -799 -2647 3286 N ATOM 2574 CA GLY A 127 90.867 24.018 229.900 1.00 48.98 C ANISOU 2574 CA GLY A 127 4069 5395 9145 -688 -2473 2924 C ATOM 2575 C GLY A 127 91.122 23.627 228.457 1.00 47.51 C ANISOU 2575 C GLY A 127 3913 4881 9259 -550 -2405 2636 C ATOM 2576 O GLY A 127 91.758 24.366 227.707 1.00 45.59 O ANISOU 2576 O GLY A 127 3674 4635 9012 -433 -2294 2323 O ATOM 2577 N ARG A 128 90.611 22.456 228.069 1.00 51.52 N ANISOU 2577 N ARG A 128 4434 5128 10014 -585 -2469 2737 N ATOM 2578 CA ARG A 128 90.820 21.968 226.710 1.00 58.41 C ANISOU 2578 CA ARG A 128 5325 5708 11158 -484 -2426 2464 C ATOM 2579 C ARG A 128 90.133 22.862 225.684 1.00 53.94 C ANISOU 2579 C ARG A 128 4790 5168 10537 -446 -2238 2216 C ATOM 2580 O ARG A 128 90.722 23.199 224.650 1.00 47.20 O ANISOU 2580 O ARG A 128 3961 4227 9746 -332 -2149 1908 O ATOM 2581 CB ARG A 128 90.318 20.528 226.596 1.00 73.01 C ANISOU 2581 CB ARG A 128 7155 7315 13270 -561 -2549 2618 C ATOM 2582 CG ARG A 128 90.138 20.027 225.171 1.00 72.27 C ANISOU 2582 CG ARG A 128 7064 6971 13425 -502 -2506 2345 C ATOM 2583 CD ARG A 128 88.665 19.822 224.840 1.00 57.16 C ANISOU 2583 CD ARG A 128 5141 5036 11543 -612 -2476 2417 C ATOM 2584 NE ARG A 128 88.475 19.259 223.506 1.00 56.79 N ANISOU 2584 NE ARG A 128 5079 4785 11712 -565 -2472 2161 N ATOM 2585 CZ ARG A 128 88.230 19.980 222.417 1.00 58.69 C ANISOU 2585 CZ ARG A 128 5352 5033 11915 -510 -2344 1894 C ATOM 2586 NH1 ARG A 128 88.141 21.301 222.498 1.00 60.46 N ANISOU 2586 NH1 ARG A 128 5631 5429 11912 -487 -2195 1845 N ATOM 2587 NH2 ARG A 128 88.071 19.381 221.244 1.00 55.26 N ANISOU 2587 NH2 ARG A 128 4894 4451 11652 -467 -2368 1677 N ATOM 2588 N LEU A 129 88.888 23.260 225.952 1.00 53.83 N ANISOU 2588 N LEU A 129 4767 5286 10400 -545 -2173 2355 N ATOM 2589 CA LEU A 129 88.153 24.088 225.001 1.00 44.65 C ANISOU 2589 CA LEU A 129 3626 4150 9190 -515 -1998 2139 C ATOM 2590 C LEU A 129 88.650 25.529 225.003 1.00 52.57 C ANISOU 2590 C LEU A 129 4628 5393 9954 -447 -1842 1922 C ATOM 2591 O LEU A 129 88.598 26.202 223.967 1.00 37.66 O ANISOU 2591 O LEU A 129 2780 3478 8050 -375 -1698 1653 O ATOM 2592 CB LEU A 129 86.657 24.034 225.318 1.00 41.89 C ANISOU 2592 CB LEU A 129 3238 3874 8805 -648 -1970 2359 C ATOM 2593 CG LEU A 129 85.685 24.788 224.410 1.00 43.63 C ANISOU 2593 CG LEU A 129 3480 4127 8972 -637 -1790 2175 C ATOM 2594 CD1 LEU A 129 85.762 24.272 222.981 1.00 39.15 C ANISOU 2594 CD1 LEU A 129 2978 3273 8623 -555 -1809 1955 C ATOM 2595 CD2 LEU A 129 84.268 24.675 224.950 1.00 40.60 C ANISOU 2595 CD2 LEU A 129 3047 3848 8532 -783 -1750 2416 C ATOM 2596 N CYS A 130 89.142 26.014 226.146 1.00 51.96 N ANISOU 2596 N CYS A 130 4503 5554 9685 -485 -1878 2036 N ATOM 2597 CA CYS A 130 89.594 27.400 226.237 1.00 55.67 C ANISOU 2597 CA CYS A 130 4954 6255 9942 -452 -1736 1825 C ATOM 2598 C CYS A 130 90.834 27.637 225.383 1.00 59.33 C ANISOU 2598 C CYS A 130 5458 6602 10483 -306 -1703 1536 C ATOM 2599 O CYS A 130 90.957 28.685 224.738 1.00 63.51 O ANISOU 2599 O CYS A 130 6005 7200 10925 -255 -1536 1285 O ATOM 2600 CB CYS A 130 89.861 27.762 227.697 1.00 63.75 C ANISOU 2600 CB CYS A 130 5907 7570 10745 -556 -1815 2019 C ATOM 2601 SG CYS A 130 90.433 29.452 228.009 1.00 76.02 S ANISOU 2601 SG CYS A 130 7461 9412 12012 -556 -1633 1748 S ATOM 2602 N THR A 131 91.767 26.682 225.371 1.00 62.84 N ANISOU 2602 N THR A 131 5908 6874 11095 -248 -1850 1575 N ATOM 2603 CA THR A 131 92.955 26.821 224.533 1.00 58.48 C ANISOU 2603 CA THR A 131 5369 6215 10635 -121 -1808 1308 C ATOM 2604 C THR A 131 92.590 26.813 223.052 1.00 56.52 C ANISOU 2604 C THR A 131 5179 5792 10503 -65 -1684 1079 C ATOM 2605 O THR A 131 93.161 27.573 222.261 1.00 47.90 O ANISOU 2605 O THR A 131 4106 4726 9366 7 -1555 826 O ATOM 2606 CB THR A 131 93.954 25.706 224.844 1.00 57.18 C ANISOU 2606 CB THR A 131 5176 5895 10656 -80 -1986 1407 C ATOM 2607 OG1 THR A 131 94.269 25.719 226.242 1.00 64.55 O ANISOU 2607 OG1 THR A 131 6062 7011 11454 -146 -2122 1646 O ATOM 2608 CG2 THR A 131 95.233 25.893 224.042 1.00 51.87 C ANISOU 2608 CG2 THR A 131 4489 5145 10077 43 -1930 1137 C ATOM 2609 N PHE A 132 91.637 25.962 222.661 1.00 54.01 N ANISOU 2609 N PHE A 132 4888 5304 10329 -113 -1730 1173 N ATOM 2610 CA PHE A 132 91.181 25.943 221.275 1.00 47.03 C ANISOU 2610 CA PHE A 132 4054 4278 9539 -84 -1638 968 C ATOM 2611 C PHE A 132 90.445 27.226 220.908 1.00 42.27 C ANISOU 2611 C PHE A 132 3485 3848 8729 -95 -1458 863 C ATOM 2612 O PHE A 132 90.525 27.679 219.759 1.00 33.85 O ANISOU 2612 O PHE A 132 2461 2742 7660 -45 -1351 638 O ATOM 2613 CB PHE A 132 90.290 24.722 221.036 1.00 49.26 C ANISOU 2613 CB PHE A 132 4337 4349 10031 -156 -1755 1103 C ATOM 2614 CG PHE A 132 89.552 24.751 219.726 1.00 47.16 C ANISOU 2614 CG PHE A 132 4111 3976 9834 -158 -1687 929 C ATOM 2615 CD1 PHE A 132 90.186 24.383 218.551 1.00 48.48 C ANISOU 2615 CD1 PHE A 132 4277 3998 10145 -96 -1684 673 C ATOM 2616 CD2 PHE A 132 88.221 25.133 219.672 1.00 45.20 C ANISOU 2616 CD2 PHE A 132 3884 3790 9500 -224 -1632 1024 C ATOM 2617 CE1 PHE A 132 89.511 24.407 217.345 1.00 43.85 C ANISOU 2617 CE1 PHE A 132 3709 3343 9609 -111 -1648 515 C ATOM 2618 CE2 PHE A 132 87.540 25.159 218.469 1.00 40.05 C ANISOU 2618 CE2 PHE A 132 3270 3042 8904 -218 -1593 882 C ATOM 2619 CZ PHE A 132 88.186 24.795 217.304 1.00 38.47 C ANISOU 2619 CZ PHE A 132 3071 2713 8833 -165 -1608 627 C ATOM 2620 N PHE A 133 89.727 27.823 221.861 1.00 37.17 N ANISOU 2620 N PHE A 133 2811 3402 7911 -171 -1421 1023 N ATOM 2621 CA PHE A 133 88.993 29.052 221.581 1.00 35.17 C ANISOU 2621 CA PHE A 133 2576 3310 7476 -190 -1239 922 C ATOM 2622 C PHE A 133 89.948 30.214 221.334 1.00 42.65 C ANISOU 2622 C PHE A 133 3533 4377 8294 -122 -1115 697 C ATOM 2623 O PHE A 133 89.785 30.969 220.368 1.00 43.02 O ANISOU 2623 O PHE A 133 3632 4425 8290 -88 -980 519 O ATOM 2624 CB PHE A 133 88.047 29.367 222.741 1.00 40.51 C ANISOU 2624 CB PHE A 133 3194 4178 8019 -302 -1217 1134 C ATOM 2625 CG PHE A 133 87.065 30.470 222.452 1.00 40.92 C ANISOU 2625 CG PHE A 133 3260 4358 7931 -329 -1024 1050 C ATOM 2626 CD1 PHE A 133 87.416 31.797 222.639 1.00 43.54 C ANISOU 2626 CD1 PHE A 133 3579 4863 8100 -312 -876 897 C ATOM 2627 CD2 PHE A 133 85.783 30.177 222.018 1.00 43.55 C ANISOU 2627 CD2 PHE A 133 3612 4626 8308 -373 -997 1129 C ATOM 2628 CE1 PHE A 133 86.514 32.814 222.381 1.00 36.66 C ANISOU 2628 CE1 PHE A 133 2721 4081 7127 -328 -698 824 C ATOM 2629 CE2 PHE A 133 84.875 31.190 221.761 1.00 40.58 C ANISOU 2629 CE2 PHE A 133 3247 4359 7813 -385 -824 1060 C ATOM 2630 CZ PHE A 133 85.242 32.509 221.946 1.00 32.74 C ANISOU 2630 CZ PHE A 133 2245 3522 6672 -358 -673 909 C ATOM 2631 N GLY A 134 90.951 30.373 222.202 1.00 31.64 N ANISOU 2631 N GLY A 134 2087 3086 6848 -112 -1171 717 N ATOM 2632 CA GLY A 134 91.901 31.461 222.032 1.00 30.70 C ANISOU 2632 CA GLY A 134 1964 3077 6623 -62 -1064 513 C ATOM 2633 C GLY A 134 92.713 31.340 220.757 1.00 30.14 C ANISOU 2633 C GLY A 134 1943 2853 6657 31 -1023 307 C ATOM 2634 O GLY A 134 93.036 32.344 220.117 1.00 28.89 O ANISOU 2634 O GLY A 134 1813 2751 6412 58 -881 126 O ATOM 2635 N LEU A 135 93.063 30.109 220.375 1.00 31.31 N ANISOU 2635 N LEU A 135 2092 2804 7000 69 -1144 332 N ATOM 2636 CA LEU A 135 93.818 29.899 219.144 1.00 31.16 C ANISOU 2636 CA LEU A 135 2098 2645 7098 141 -1101 123 C ATOM 2637 C LEU A 135 92.994 30.285 217.922 1.00 29.88 C ANISOU 2637 C LEU A 135 2000 2442 6909 131 -987 1 C ATOM 2638 O LEU A 135 93.491 30.964 217.016 1.00 28.95 O ANISOU 2638 O LEU A 135 1906 2347 6746 163 -870 -188 O ATOM 2639 CB LEU A 135 94.275 28.440 219.057 1.00 38.37 C ANISOU 2639 CB LEU A 135 2980 3348 8252 170 -1256 168 C ATOM 2640 CG LEU A 135 95.007 27.971 217.797 1.00 46.10 C ANISOU 2640 CG LEU A 135 3954 4173 9390 231 -1228 -56 C ATOM 2641 CD1 LEU A 135 96.124 27.008 218.167 1.00 51.49 C ANISOU 2641 CD1 LEU A 135 4563 4744 10257 281 -1350 -34 C ATOM 2642 CD2 LEU A 135 94.044 27.307 216.820 1.00 33.53 C ANISOU 2642 CD2 LEU A 135 2394 2429 7916 199 -1247 -104 C ATOM 2643 N THR A 136 91.728 29.860 217.882 1.00 29.74 N ANISOU 2643 N THR A 136 2006 2371 6924 78 -1028 123 N ATOM 2644 CA THR A 136 90.870 30.190 216.748 1.00 31.50 C ANISOU 2644 CA THR A 136 2280 2563 7127 64 -948 33 C ATOM 2645 C THR A 136 90.662 31.696 216.638 1.00 30.80 C ANISOU 2645 C THR A 136 2223 2656 6826 56 -779 -32 C ATOM 2646 O THR A 136 90.604 32.245 215.530 1.00 26.42 O ANISOU 2646 O THR A 136 1704 2096 6239 71 -691 -169 O ATOM 2647 CB THR A 136 89.530 29.465 216.880 1.00 39.94 C ANISOU 2647 CB THR A 136 3354 3552 8269 0 -1036 204 C ATOM 2648 OG1 THR A 136 89.758 28.054 216.980 1.00 35.34 O ANISOU 2648 OG1 THR A 136 2741 2772 7913 -4 -1202 266 O ATOM 2649 CG2 THR A 136 88.641 29.744 215.675 1.00 37.23 C ANISOU 2649 CG2 THR A 136 3053 3179 7914 -11 -983 119 C ATOM 2650 N MET A 137 90.553 32.382 217.778 1.00 30.72 N ANISOU 2650 N MET A 137 2188 2805 6681 26 -739 65 N ATOM 2651 CA MET A 137 90.457 33.838 217.761 1.00 25.63 C ANISOU 2651 CA MET A 137 1563 2310 5864 17 -581 -11 C ATOM 2652 C MET A 137 91.696 34.460 217.134 1.00 38.86 C ANISOU 2652 C MET A 137 3255 3995 7517 67 -506 -197 C ATOM 2653 O MET A 137 91.597 35.421 216.361 1.00 40.00 O ANISOU 2653 O MET A 137 3443 4171 7585 67 -386 -294 O ATOM 2654 CB MET A 137 90.255 34.363 219.182 1.00 25.89 C ANISOU 2654 CB MET A 137 1539 2509 5787 -31 -562 94 C ATOM 2655 CG MET A 137 88.922 33.980 219.804 1.00 34.96 C ANISOU 2655 CG MET A 137 2662 3687 6933 -100 -592 279 C ATOM 2656 SD MET A 137 87.533 34.894 219.111 1.00 25.26 S ANISOU 2656 SD MET A 137 1480 2487 5631 -119 -445 264 S ATOM 2657 CE MET A 137 87.752 36.480 219.904 1.00 24.82 C ANISOU 2657 CE MET A 137 1394 2618 5419 -135 -280 177 C ATOM 2658 N THR A 138 92.875 33.921 217.451 1.00 40.49 N ANISOU 2658 N THR A 138 3418 4169 7798 103 -580 -234 N ATOM 2659 CA THR A 138 94.124 34.496 216.962 1.00 35.87 C ANISOU 2659 CA THR A 138 2830 3604 7196 141 -507 -399 C ATOM 2660 C THR A 138 94.356 34.176 215.489 1.00 33.25 C ANISOU 2660 C THR A 138 2528 3155 6950 168 -471 -541 C ATOM 2661 O THR A 138 94.838 35.030 214.736 1.00 36.47 O ANISOU 2661 O THR A 138 2958 3606 7294 168 -354 -668 O ATOM 2662 CB THR A 138 95.294 33.991 217.808 1.00 45.13 C ANISOU 2662 CB THR A 138 3928 4786 8432 171 -608 -380 C ATOM 2663 OG1 THR A 138 95.036 34.260 219.192 1.00 38.43 O ANISOU 2663 OG1 THR A 138 3033 4074 7496 127 -658 -246 O ATOM 2664 CG2 THR A 138 96.591 34.677 217.400 1.00 60.40 C ANISOU 2664 CG2 THR A 138 5843 6758 10347 198 -525 -540 C ATOM 2665 N VAL A 139 94.023 32.955 215.062 1.00 35.12 N ANISOU 2665 N VAL A 139 2756 3248 7340 181 -574 -526 N ATOM 2666 CA VAL A 139 94.253 32.557 213.673 1.00 38.78 C ANISOU 2666 CA VAL A 139 3220 3615 7900 199 -550 -691 C ATOM 2667 C VAL A 139 93.425 33.419 212.729 1.00 31.49 C ANISOU 2667 C VAL A 139 2346 2747 6874 167 -446 -733 C ATOM 2668 O VAL A 139 93.956 34.087 211.834 1.00 37.47 O ANISOU 2668 O VAL A 139 3107 3553 7579 169 -336 -869 O ATOM 2669 CB VAL A 139 93.939 31.063 213.478 1.00 28.52 C ANISOU 2669 CB VAL A 139 1890 2141 6805 208 -696 -673 C ATOM 2670 CG1 VAL A 139 93.952 30.711 211.999 1.00 29.04 C ANISOU 2670 CG1 VAL A 139 1941 2139 6955 216 -668 -864 C ATOM 2671 CG2 VAL A 139 94.935 30.206 214.233 1.00 46.72 C ANISOU 2671 CG2 VAL A 139 4136 4377 9238 247 -796 -641 C ATOM 2672 N PHE A 140 92.105 33.417 212.921 1.00 28.29 N ANISOU 2672 N PHE A 140 1968 2339 6441 133 -482 -599 N ATOM 2673 CA PHE A 140 91.212 34.107 211.999 1.00 33.82 C ANISOU 2673 CA PHE A 140 2700 3079 7073 106 -415 -612 C ATOM 2674 C PHE A 140 91.254 35.619 212.166 1.00 37.47 C ANISOU 2674 C PHE A 140 3195 3678 7363 88 -274 -597 C ATOM 2675 O PHE A 140 90.889 36.341 211.232 1.00 44.52 O ANISOU 2675 O PHE A 140 4102 4604 8207 73 -200 -633 O ATOM 2676 CB PHE A 140 89.788 33.580 212.173 1.00 24.93 C ANISOU 2676 CB PHE A 140 1582 1908 5983 70 -509 -459 C ATOM 2677 CG PHE A 140 89.625 32.147 211.751 1.00 26.19 C ANISOU 2677 CG PHE A 140 1712 1903 6337 78 -656 -489 C ATOM 2678 CD1 PHE A 140 89.910 31.114 212.628 1.00 27.11 C ANISOU 2678 CD1 PHE A 140 1805 1921 6575 86 -767 -413 C ATOM 2679 CD2 PHE A 140 89.194 31.833 210.472 1.00 26.72 C ANISOU 2679 CD2 PHE A 140 1765 1912 6477 73 -696 -595 C ATOM 2680 CE1 PHE A 140 89.768 29.795 212.240 1.00 28.51 C ANISOU 2680 CE1 PHE A 140 1953 1913 6966 89 -911 -444 C ATOM 2681 CE2 PHE A 140 89.045 30.516 210.079 1.00 35.93 C ANISOU 2681 CE2 PHE A 140 2901 2917 7833 83 -839 -648 C ATOM 2682 CZ PHE A 140 89.333 29.496 210.964 1.00 38.94 C ANISOU 2682 CZ PHE A 140 3264 3164 8370 102 -946 -574 C ATOM 2683 N GLY A 141 91.678 36.112 213.329 1.00 35.54 N ANISOU 2683 N GLY A 141 2953 3510 7042 87 -244 -546 N ATOM 2684 CA GLY A 141 91.880 37.544 213.475 1.00 37.48 C ANISOU 2684 CA GLY A 141 3226 3859 7157 71 -116 -566 C ATOM 2685 C GLY A 141 93.028 38.048 212.620 1.00 32.16 C ANISOU 2685 C GLY A 141 2553 3192 6475 80 -34 -715 C ATOM 2686 O GLY A 141 92.898 39.048 211.907 1.00 31.05 O ANISOU 2686 O GLY A 141 2439 3086 6273 60 65 -742 O ATOM 2687 N LEU A 142 94.169 37.356 212.678 1.00 23.61 N ANISOU 2687 N LEU A 142 1431 2076 5465 109 -75 -802 N ATOM 2688 CA LEU A 142 95.327 37.757 211.886 1.00 28.33 C ANISOU 2688 CA LEU A 142 2014 2691 6060 112 11 -944 C ATOM 2689 C LEU A 142 95.123 37.489 210.400 1.00 35.49 C ANISOU 2689 C LEU A 142 2914 3563 7008 110 51 -1040 C ATOM 2690 O LEU A 142 95.631 38.244 209.563 1.00 24.54 O ANISOU 2690 O LEU A 142 1528 2226 5569 91 166 -1120 O ATOM 2691 CB LEU A 142 96.578 37.035 212.384 1.00 29.46 C ANISOU 2691 CB LEU A 142 2097 2809 6288 148 -48 -1003 C ATOM 2692 CG LEU A 142 97.025 37.365 213.809 1.00 36.85 C ANISOU 2692 CG LEU A 142 3008 3807 7186 151 -87 -932 C ATOM 2693 CD1 LEU A 142 98.128 36.422 214.256 1.00 40.98 C ANISOU 2693 CD1 LEU A 142 3453 4288 7830 197 -181 -962 C ATOM 2694 CD2 LEU A 142 97.486 38.811 213.898 1.00 39.26 C ANISOU 2694 CD2 LEU A 142 3333 4202 7382 114 28 -971 C ATOM 2695 N SER A 143 94.398 36.422 210.054 1.00 33.94 N ANISOU 2695 N SER A 143 2700 3284 6911 127 -43 -1037 N ATOM 2696 CA SER A 143 94.185 36.090 208.648 1.00 26.31 C ANISOU 2696 CA SER A 143 1708 2294 5995 131 -15 -1160 C ATOM 2697 C SER A 143 93.472 37.224 207.922 1.00 26.57 C ANISOU 2697 C SER A 143 1762 2404 5931 96 81 -1122 C ATOM 2698 O SER A 143 93.906 37.660 206.850 1.00 36.42 O ANISOU 2698 O SER A 143 2989 3703 7145 89 195 -1236 O ATOM 2699 CB SER A 143 93.395 34.787 208.527 1.00 28.74 C ANISOU 2699 CB SER A 143 1990 2484 6447 151 -160 -1158 C ATOM 2700 OG SER A 143 94.156 33.687 208.995 1.00 42.39 O ANISOU 2700 OG SER A 143 3684 4128 8293 185 -243 -1204 O ATOM 2701 N SER A 144 92.372 37.715 208.495 1.00 28.57 N ANISOU 2701 N SER A 144 2049 2671 6136 71 45 -951 N ATOM 2702 CA SER A 144 91.663 38.840 207.894 1.00 34.68 C ANISOU 2702 CA SER A 144 2831 3509 6836 35 121 -879 C ATOM 2703 C SER A 144 92.554 40.073 207.812 1.00 39.22 C ANISOU 2703 C SER A 144 3431 4149 7323 20 267 -912 C ATOM 2704 O SER A 144 92.466 40.849 206.853 1.00 50.49 O ANISOU 2704 O SER A 144 4840 5623 8722 -8 361 -918 O ATOM 2705 CB SER A 144 90.396 39.147 208.693 1.00 36.94 C ANISOU 2705 CB SER A 144 3152 3794 7090 17 64 -689 C ATOM 2706 OG SER A 144 89.731 40.286 208.177 1.00 42.88 O ANISOU 2706 OG SER A 144 3906 4592 7795 -12 131 -602 O ATOM 2707 N LEU A 145 93.422 40.269 208.807 1.00 31.59 N ANISOU 2707 N LEU A 145 2493 3189 6321 28 279 -924 N ATOM 2708 CA LEU A 145 94.268 41.458 208.827 1.00 23.04 C ANISOU 2708 CA LEU A 145 1429 2154 5170 2 394 -950 C ATOM 2709 C LEU A 145 95.294 41.436 207.701 1.00 24.02 C ANISOU 2709 C LEU A 145 1518 2307 5302 -6 488 -1087 C ATOM 2710 O LEU A 145 95.611 42.483 207.125 1.00 30.23 O ANISOU 2710 O LEU A 145 2310 3133 6042 -40 606 -1088 O ATOM 2711 CB LEU A 145 94.966 41.585 210.181 1.00 39.89 C ANISOU 2711 CB LEU A 145 3576 4297 7284 7 362 -946 C ATOM 2712 CG LEU A 145 94.134 42.119 211.347 1.00 22.05 C ANISOU 2712 CG LEU A 145 1349 2049 4982 0 337 -834 C ATOM 2713 CD1 LEU A 145 94.936 42.082 212.639 1.00 22.19 C ANISOU 2713 CD1 LEU A 145 1347 2097 4989 5 302 -861 C ATOM 2714 CD2 LEU A 145 93.660 43.531 211.049 1.00 21.80 C ANISOU 2714 CD2 LEU A 145 1350 2025 4910 -29 436 -787 C ATOM 2715 N PHE A 146 95.828 40.259 207.374 1.00 24.82 N ANISOU 2715 N PHE A 146 1579 2384 5469 25 448 -1205 N ATOM 2716 CA PHE A 146 96.900 40.169 206.392 1.00 31.72 C ANISOU 2716 CA PHE A 146 2415 3296 6339 21 556 -1356 C ATOM 2717 C PHE A 146 96.433 39.749 205.004 1.00 27.02 C ANISOU 2717 C PHE A 146 1794 2722 5749 26 621 -1463 C ATOM 2718 O PHE A 146 97.139 40.021 204.028 1.00 28.16 O ANISOU 2718 O PHE A 146 1927 2934 5840 5 767 -1578 O ATOM 2719 CB PHE A 146 97.993 39.217 206.891 1.00 32.00 C ANISOU 2719 CB PHE A 146 2411 3297 6451 57 496 -1444 C ATOM 2720 CG PHE A 146 98.911 39.846 207.900 1.00 32.87 C ANISOU 2720 CG PHE A 146 2518 3427 6545 45 493 -1402 C ATOM 2721 CD1 PHE A 146 100.016 40.577 207.492 1.00 31.51 C ANISOU 2721 CD1 PHE A 146 2321 3307 6345 17 609 -1465 C ATOM 2722 CD2 PHE A 146 98.653 39.734 209.257 1.00 25.77 C ANISOU 2722 CD2 PHE A 146 1632 2499 5659 59 380 -1304 C ATOM 2723 CE1 PHE A 146 100.855 41.169 208.419 1.00 27.25 C ANISOU 2723 CE1 PHE A 146 1764 2780 5810 5 597 -1442 C ATOM 2724 CE2 PHE A 146 99.488 40.324 210.187 1.00 25.78 C ANISOU 2724 CE2 PHE A 146 1618 2529 5648 50 379 -1291 C ATOM 2725 CZ PHE A 146 100.590 41.042 209.767 1.00 26.50 C ANISOU 2725 CZ PHE A 146 1679 2662 5729 23 480 -1364 C ATOM 2726 N ILE A 147 95.275 39.096 204.883 1.00 28.57 N ANISOU 2726 N ILE A 147 1979 2871 6005 48 522 -1440 N ATOM 2727 CA ILE A 147 94.674 38.932 203.562 1.00 30.06 C ANISOU 2727 CA ILE A 147 2235 3100 6086 6 546 -1489 C ATOM 2728 C ILE A 147 94.299 40.294 202.991 1.00 34.10 C ANISOU 2728 C ILE A 147 2800 3707 6449 -76 638 -1350 C ATOM 2729 O ILE A 147 94.470 40.554 201.793 1.00 31.58 O ANISOU 2729 O ILE A 147 2561 3474 5963 -139 726 -1393 O ATOM 2730 CB ILE A 147 93.461 37.985 203.629 1.00 27.71 C ANISOU 2730 CB ILE A 147 2001 2727 5802 -3 350 -1420 C ATOM 2731 CG1 ILE A 147 93.917 36.549 203.893 1.00 30.72 C ANISOU 2731 CG1 ILE A 147 2348 2993 6331 69 269 -1577 C ATOM 2732 CG2 ILE A 147 92.656 38.049 202.340 1.00 28.73 C ANISOU 2732 CG2 ILE A 147 2262 2920 5732 -94 322 -1394 C ATOM 2733 CD1 ILE A 147 92.780 35.550 203.957 1.00 33.09 C ANISOU 2733 CD1 ILE A 147 2705 3197 6669 47 76 -1516 C ATOM 2734 N ALA A 148 93.794 41.189 203.844 1.00 33.42 N ANISOU 2734 N ALA A 148 2669 3604 6424 -78 622 -1181 N ATOM 2735 CA ALA A 148 93.506 42.551 203.408 1.00 33.03 C ANISOU 2735 CA ALA A 148 2650 3608 6290 -142 713 -1040 C ATOM 2736 C ALA A 148 94.789 43.305 203.080 1.00 46.91 C ANISOU 2736 C ALA A 148 4369 5423 8033 -165 905 -1130 C ATOM 2737 O ALA A 148 94.830 44.081 202.118 1.00 58.41 O ANISOU 2737 O ALA A 148 5886 6946 9361 -239 1001 -1067 O ATOM 2738 CB ALA A 148 92.709 43.290 204.482 1.00 25.10 C ANISOU 2738 CB ALA A 148 1594 2549 5393 -126 668 -874 C ATOM 2739 N SER A 149 95.843 43.094 203.872 1.00 55.96 N ANISOU 2739 N SER A 149 5485 6537 9239 -119 915 -1228 N ATOM 2740 CA SER A 149 97.121 43.739 203.589 1.00 27.59 C ANISOU 2740 CA SER A 149 1900 2990 5595 -152 1048 -1289 C ATOM 2741 C SER A 149 97.699 43.249 202.270 1.00 29.33 C ANISOU 2741 C SER A 149 2088 3300 5757 -175 1194 -1456 C ATOM 2742 O SER A 149 98.324 44.020 201.533 1.00 41.29 O ANISOU 2742 O SER A 149 3602 4892 7194 -241 1359 -1463 O ATOM 2743 CB SER A 149 98.103 43.487 204.733 1.00 27.17 C ANISOU 2743 CB SER A 149 1858 2887 5577 -119 963 -1325 C ATOM 2744 OG SER A 149 97.689 44.146 205.916 1.00 25.92 O ANISOU 2744 OG SER A 149 1741 2678 5430 -117 880 -1201 O ATOM 2745 N ALA A 150 97.502 41.968 201.956 1.00 29.84 N ANISOU 2745 N ALA A 150 2137 3353 5846 -125 1143 -1602 N ATOM 2746 CA ALA A 150 97.968 41.442 200.679 1.00 31.79 C ANISOU 2746 CA ALA A 150 2441 3683 5954 -155 1254 -1767 C ATOM 2747 C ALA A 150 97.241 42.102 199.514 1.00 44.38 C ANISOU 2747 C ALA A 150 4185 5381 7296 -272 1282 -1635 C ATOM 2748 O ALA A 150 97.870 42.490 198.523 1.00 38.11 O ANISOU 2748 O ALA A 150 3428 4705 6349 -345 1452 -1691 O ATOM 2749 CB ALA A 150 97.787 39.925 200.638 1.00 32.30 C ANISOU 2749 CB ALA A 150 2528 3675 6069 -85 1135 -1925 C ATOM 2750 N MET A 151 95.916 42.244 199.620 1.00 40.87 N ANISOU 2750 N MET A 151 3819 4902 6806 -297 1115 -1447 N ATOM 2751 CA MET A 151 95.149 42.879 198.552 1.00 37.31 C ANISOU 2751 CA MET A 151 3500 4547 6130 -408 1103 -1285 C ATOM 2752 C MET A 151 95.548 44.335 198.356 1.00 36.52 C ANISOU 2752 C MET A 151 3379 4497 6001 -473 1253 -1135 C ATOM 2753 O MET A 151 95.488 44.846 197.232 1.00 34.75 O ANISOU 2753 O MET A 151 3254 4388 5563 -578 1320 -1051 O ATOM 2754 CB MET A 151 93.652 42.776 198.845 1.00 38.71 C ANISOU 2754 CB MET A 151 3724 4663 6322 -408 884 -1098 C ATOM 2755 CG MET A 151 93.072 41.394 198.607 1.00 52.54 C ANISOU 2755 CG MET A 151 5539 6389 8036 -396 726 -1214 C ATOM 2756 SD MET A 151 91.283 41.325 198.830 1.00 51.07 S ANISOU 2756 SD MET A 151 5389 6150 7866 -421 474 -977 S ATOM 2757 CE MET A 151 91.149 41.677 200.580 1.00 45.57 C ANISOU 2757 CE MET A 151 4538 5317 7460 -315 455 -880 C ATOM 2758 N ALA A 152 95.949 45.019 199.430 1.00 36.06 N ANISOU 2758 N ALA A 152 3199 4352 6150 -425 1301 -1095 N ATOM 2759 CA ALA A 152 96.410 46.397 199.295 1.00 38.32 C ANISOU 2759 CA ALA A 152 3455 4655 6448 -492 1449 -972 C ATOM 2760 C ALA A 152 97.662 46.474 198.430 1.00 47.57 C ANISOU 2760 C ALA A 152 4620 5946 7510 -556 1660 -1106 C ATOM 2761 O ALA A 152 97.816 47.402 197.628 1.00 62.80 O ANISOU 2761 O ALA A 152 6599 7947 9315 -661 1775 -976 O ATOM 2762 CB ALA A 152 96.667 47.003 200.674 1.00 35.45 C ANISOU 2762 CB ALA A 152 2962 4174 6334 -433 1458 -957 C ATOM 2763 N VAL A 153 98.568 45.506 198.581 1.00 39.20 N ANISOU 2763 N VAL A 153 3486 4903 6504 -493 1718 -1357 N ATOM 2764 CA VAL A 153 99.760 45.469 197.740 1.00 40.44 C ANISOU 2764 CA VAL A 153 3617 5182 6566 -545 1937 -1512 C ATOM 2765 C VAL A 153 99.393 45.088 196.312 1.00 59.37 C ANISOU 2765 C VAL A 153 6180 7723 8654 -633 1967 -1529 C ATOM 2766 O VAL A 153 100.041 45.534 195.356 1.00 63.03 O ANISOU 2766 O VAL A 153 6675 8326 8948 -735 2160 -1541 O ATOM 2767 CB VAL A 153 100.799 44.503 198.340 1.00 36.31 C ANISOU 2767 CB VAL A 153 2983 4611 6203 -435 1941 -1751 C ATOM 2768 CG1 VAL A 153 102.094 44.539 197.541 1.00 38.59 C ANISOU 2768 CG1 VAL A 153 3266 5002 6395 -479 2117 -1866 C ATOM 2769 CG2 VAL A 153 101.054 44.841 199.803 1.00 34.43 C ANISOU 2769 CG2 VAL A 153 2714 4224 6145 -364 1758 -1644 C ATOM 2770 N GLU A 154 98.353 44.267 196.138 1.00 60.55 N ANISOU 2770 N GLU A 154 6439 7852 8714 -610 1777 -1528 N ATOM 2771 CA GLU A 154 97.907 43.901 194.796 1.00 53.14 C ANISOU 2771 CA GLU A 154 5672 7060 7459 -710 1773 -1546 C ATOM 2772 C GLU A 154 97.425 45.126 194.028 1.00 51.26 C ANISOU 2772 C GLU A 154 5535 6922 7020 -849 1794 -1260 C ATOM 2773 O GLU A 154 97.796 45.332 192.867 1.00 46.88 O ANISOU 2773 O GLU A 154 5074 6543 6197 -968 1934 -1270 O ATOM 2774 CB GLU A 154 96.795 42.853 194.877 1.00 59.99 C ANISOU 2774 CB GLU A 154 6623 7863 8306 -669 1532 -1578 C ATOM 2775 CG GLU A 154 97.161 41.583 195.627 1.00 57.85 C ANISOU 2775 CG GLU A 154 6263 7467 8249 -536 1482 -1829 C ATOM 2776 CD GLU A 154 98.051 40.660 194.824 1.00 69.85 C ANISOU 2776 CD GLU A 154 7803 9064 9672 -533 1636 -2145 C ATOM 2777 OE1 GLU A 154 98.193 40.879 193.603 1.00 78.90 O ANISOU 2777 OE1 GLU A 154 9066 10385 10526 -652 1759 -2180 O ATOM 2778 OE2 GLU A 154 98.608 39.711 195.416 1.00 76.87 O ANISOU 2778 OE2 GLU A 154 8590 9839 10779 -413 1635 -2356 O ATOM 2779 N ARG A 155 96.591 45.953 194.666 1.00 62.21 N ANISOU 2779 N ARG A 155 6901 8199 8538 -835 1660 -997 N ATOM 2780 CA ARG A 155 96.075 47.144 194.001 1.00 61.35 C ANISOU 2780 CA ARG A 155 6872 8148 8291 -952 1657 -693 C ATOM 2781 C ARG A 155 97.179 48.158 193.730 1.00 52.98 C ANISOU 2781 C ARG A 155 5759 7140 7232 -1029 1902 -649 C ATOM 2782 O ARG A 155 97.120 48.883 192.731 1.00 53.23 O ANISOU 2782 O ARG A 155 5887 7290 7048 -1163 1966 -461 O ATOM 2783 CB ARG A 155 94.967 47.775 194.845 1.00 61.67 C ANISOU 2783 CB ARG A 155 6871 8026 8533 -895 1474 -449 C ATOM 2784 CG ARG A 155 93.807 46.836 195.136 1.00 68.26 C ANISOU 2784 CG ARG A 155 7741 8810 9384 -833 1232 -461 C ATOM 2785 CD ARG A 155 92.769 47.491 196.035 1.00 77.20 C ANISOU 2785 CD ARG A 155 8806 9788 10739 -770 1088 -235 C ATOM 2786 NE ARG A 155 91.677 46.578 196.360 1.00 83.38 N ANISOU 2786 NE ARG A 155 9600 10525 11555 -718 870 -242 N ATOM 2787 CZ ARG A 155 90.477 46.966 196.783 1.00 91.09 C ANISOU 2787 CZ ARG A 155 10542 11414 12653 -688 713 -28 C ATOM 2788 NH1 ARG A 155 89.545 46.064 197.055 1.00 93.54 N ANISOU 2788 NH1 ARG A 155 10852 11694 12995 -653 526 -45 N ATOM 2789 NH2 ARG A 155 90.208 48.255 196.930 1.00 94.99 N ANISOU 2789 NH2 ARG A 155 10993 11840 13258 -694 748 204 N ATOM 2790 N ALA A 156 98.186 48.224 194.603 1.00 54.32 N ANISOU 2790 N ALA A 156 5771 7225 7641 -957 2032 -804 N ATOM 2791 CA ALA A 156 99.289 49.157 194.396 1.00 59.05 C ANISOU 2791 CA ALA A 156 6297 7866 8271 -1038 2267 -776 C ATOM 2792 C ALA A 156 100.116 48.765 193.177 1.00 68.27 C ANISOU 2792 C ALA A 156 7524 9250 9167 -1137 2469 -919 C ATOM 2793 O ALA A 156 100.444 49.612 192.338 1.00 69.26 O ANISOU 2793 O ALA A 156 7699 9487 9130 -1279 2617 -764 O ATOM 2794 CB ALA A 156 100.164 49.221 195.647 1.00 40.46 C ANISOU 2794 CB ALA A 156 3750 5384 6240 -943 2331 -928 C ATOM 2795 N LEU A 157 100.458 47.480 193.059 1.00 66.31 N ANISOU 2795 N LEU A 157 7270 9058 8868 -1068 2487 -1217 N ATOM 2796 CA LEU A 157 101.249 47.011 191.929 1.00 64.52 C ANISOU 2796 CA LEU A 157 7091 9035 8387 -1150 2701 -1405 C ATOM 2797 C LEU A 157 100.432 46.880 190.651 1.00 67.19 C ANISOU 2797 C LEU A 157 7654 9549 8327 -1278 2639 -1304 C ATOM 2798 O LEU A 157 101.017 46.772 189.567 1.00 72.31 O ANISOU 2798 O LEU A 157 8374 10405 8696 -1391 2838 -1402 O ATOM 2799 CB LEU A 157 101.896 45.664 192.261 1.00 62.01 C ANISOU 2799 CB LEU A 157 6680 8690 8191 -1018 2743 -1776 C ATOM 2800 CG LEU A 157 102.905 45.660 193.410 1.00 62.68 C ANISOU 2800 CG LEU A 157 6528 8643 8646 -899 2817 -1907 C ATOM 2801 CD1 LEU A 157 103.455 44.260 193.634 1.00 56.44 C ANISOU 2801 CD1 LEU A 157 5695 7789 7961 -754 2752 -2195 C ATOM 2802 CD2 LEU A 157 104.032 46.647 193.140 1.00 66.58 C ANISOU 2802 CD2 LEU A 157 6973 9185 9141 -970 2965 -1805 C ATOM 2803 N ALA A 158 99.102 46.887 190.748 1.00 57.64 N ANISOU 2803 N ALA A 158 6551 8273 7077 -1271 2370 -1111 N ATOM 2804 CA ALA A 158 98.269 46.796 189.554 1.00 65.15 C ANISOU 2804 CA ALA A 158 7709 9398 7648 -1404 2272 -990 C ATOM 2805 C ALA A 158 98.216 48.126 188.812 1.00 70.56 C ANISOU 2805 C ALA A 158 8466 10192 8153 -1567 2343 -648 C ATOM 2806 O ALA A 158 98.414 48.173 187.593 1.00 69.84 O ANISOU 2806 O ALA A 158 8510 10335 7693 -1722 2453 -629 O ATOM 2807 CB ALA A 158 96.859 46.334 189.928 1.00 65.71 C ANISOU 2807 CB ALA A 158 7841 9358 7767 -1343 1947 -891 C ATOM 2808 N ILE A 159 97.951 49.216 189.532 1.00 71.83 N ANISOU 2808 N ILE A 159 8540 10183 8568 -1539 2284 -375 N ATOM 2809 CA ILE A 159 97.879 50.523 188.887 1.00 74.62 C ANISOU 2809 CA ILE A 159 8951 10596 8806 -1687 2338 -22 C ATOM 2810 C ILE A 159 99.275 51.063 188.581 1.00 71.25 C ANISOU 2810 C ILE A 159 8451 10260 8362 -1776 2662 -83 C ATOM 2811 O ILE A 159 99.442 51.869 187.658 1.00 67.74 O ANISOU 2811 O ILE A 159 8090 9954 7693 -1945 2768 151 O ATOM 2812 CB ILE A 159 97.066 51.497 189.760 1.00 71.31 C ANISOU 2812 CB ILE A 159 8460 9935 8700 -1619 2165 275 C ATOM 2813 CG1 ILE A 159 96.806 52.809 189.013 1.00 79.26 C ANISOU 2813 CG1 ILE A 159 9539 10977 9599 -1768 2175 680 C ATOM 2814 CG2 ILE A 159 97.774 51.755 191.083 1.00 66.01 C ANISOU 2814 CG2 ILE A 159 7593 9056 8432 -1495 2262 137 C ATOM 2815 CD1 ILE A 159 96.089 52.628 187.691 1.00 81.86 C ANISOU 2815 CD1 ILE A 159 10066 11533 9503 -1909 2053 857 C ATOM 2816 N ARG A 160 100.294 50.628 189.327 1.00 70.03 N ANISOU 2816 N ARG A 160 8132 10037 8441 -1675 2819 -380 N ATOM 2817 CA ARG A 160 101.655 51.074 189.043 1.00 71.27 C ANISOU 2817 CA ARG A 160 8192 10287 8602 -1761 3133 -457 C ATOM 2818 C ARG A 160 102.139 50.542 187.700 1.00 78.61 C ANISOU 2818 C ARG A 160 9239 11513 9114 -1893 3326 -594 C ATOM 2819 O ARG A 160 102.872 51.231 186.981 1.00 84.37 O ANISOU 2819 O ARG A 160 9973 12391 9693 -2049 3562 -490 O ATOM 2820 CB ARG A 160 102.600 50.635 190.162 1.00 70.23 C ANISOU 2820 CB ARG A 160 7839 10020 8824 -1614 3226 -750 C ATOM 2821 CG ARG A 160 103.151 51.776 191.005 1.00 76.47 C ANISOU 2821 CG ARG A 160 8467 10642 9946 -1620 3296 -613 C ATOM 2822 CD ARG A 160 102.088 52.369 191.914 1.00 81.08 C ANISOU 2822 CD ARG A 160 9058 10993 10755 -1544 3044 -394 C ATOM 2823 NE ARG A 160 102.621 53.439 192.753 1.00 83.06 N ANISOU 2823 NE ARG A 160 9170 11069 11320 -1540 3086 -300 N ATOM 2824 CZ ARG A 160 101.929 54.056 193.705 1.00 88.26 C ANISOU 2824 CZ ARG A 160 9796 11508 12230 -1473 2923 -163 C ATOM 2825 NH1 ARG A 160 100.672 53.707 193.945 1.00 86.69 N ANISOU 2825 NH1 ARG A 160 9679 11240 12019 -1396 2709 -86 N ATOM 2826 NH2 ARG A 160 102.494 55.020 194.420 1.00 89.38 N ANISOU 2826 NH2 ARG A 160 9867 11502 12593 -1437 2877 -107 N ATOM 2827 N ALA A 161 101.742 49.323 187.347 1.00 81.49 N ANISOU 2827 N ALA A 161 9704 11969 9288 -1844 3238 -833 N ATOM 2828 CA ALA A 161 102.116 48.717 186.068 1.00 85.84 C ANISOU 2828 CA ALA A 161 10388 12808 9418 -1968 3415 -1012 C ATOM 2829 C ALA A 161 100.964 47.862 185.568 1.00 84.17 C ANISOU 2829 C ALA A 161 10373 12665 8944 -1972 3167 -1056 C ATOM 2830 O ALA A 161 100.981 46.629 185.684 1.00 83.51 O ANISOU 2830 O ALA A 161 10290 12566 8874 -1870 3138 -1401 O ATOM 2831 CB ALA A 161 103.395 47.890 186.199 1.00 85.02 C ANISOU 2831 CB ALA A 161 10133 12746 9424 -1887 3686 -1434 C ATOM 2832 N PRO A 162 99.926 48.486 185.003 1.00 80.25 N ANISOU 2832 N PRO A 162 10038 12234 8220 -2093 2969 -704 N ATOM 2833 CA PRO A 162 98.817 47.700 184.436 1.00 77.22 C ANISOU 2833 CA PRO A 162 9839 11941 7559 -2125 2719 -734 C ATOM 2834 C PRO A 162 99.230 46.850 183.250 1.00 82.46 C ANISOU 2834 C PRO A 162 10654 12895 7783 -2246 2884 -1028 C ATOM 2835 O PRO A 162 98.554 45.859 182.948 1.00 83.17 O ANISOU 2835 O PRO A 162 10863 13028 7709 -2239 2713 -1212 O ATOM 2836 CB PRO A 162 97.797 48.773 184.028 1.00 76.55 C ANISOU 2836 CB PRO A 162 9865 11883 7339 -2247 2505 -243 C ATOM 2837 CG PRO A 162 98.187 50.001 184.798 1.00 74.38 C ANISOU 2837 CG PRO A 162 9430 11415 7418 -2205 2586 12 C ATOM 2838 CD PRO A 162 99.677 49.934 184.916 1.00 77.23 C ANISOU 2838 CD PRO A 162 9661 11817 7863 -2197 2940 -251 C ATOM 2839 N HIS A 163 100.317 47.211 182.566 1.00 89.53 N ANISOU 2839 N HIS A 163 11544 13990 8483 -2366 3220 -1088 N ATOM 2840 CA HIS A 163 100.789 46.428 181.429 1.00 93.55 C ANISOU 2840 CA HIS A 163 12191 14792 8561 -2486 3425 -1400 C ATOM 2841 C HIS A 163 101.335 45.076 181.875 1.00 93.14 C ANISOU 2841 C HIS A 163 12038 14640 8710 -2312 3523 -1920 C ATOM 2842 O HIS A 163 100.942 44.030 181.344 1.00 86.25 O ANISOU 2842 O HIS A 163 11305 13857 7608 -2328 3451 -2195 O ATOM 2843 CB HIS A 163 101.852 47.223 180.674 1.00 96.58 C ANISOU 2843 CB HIS A 163 12565 15409 8723 -2656 3786 -1315 C ATOM 2844 CG HIS A 163 102.675 48.107 181.558 1.00 95.57 C ANISOU 2844 CG HIS A 163 12198 15092 9022 -2579 3941 -1179 C ATOM 2845 ND1 HIS A 163 102.326 49.411 181.838 1.00 93.56 N ANISOU 2845 ND1 HIS A 163 11920 14730 8899 -2637 3832 -715 N ATOM 2846 CD2 HIS A 163 103.823 47.872 182.236 1.00 95.33 C ANISOU 2846 CD2 HIS A 163 11938 14903 9380 -2408 4111 -1426 C ATOM 2847 CE1 HIS A 163 103.226 49.943 182.645 1.00 93.79 C ANISOU 2847 CE1 HIS A 163 11723 14594 9317 -2559 4004 -723 C ATOM 2848 NE2 HIS A 163 104.145 49.030 182.902 1.00 94.54 N ANISOU 2848 NE2 HIS A 163 11690 14644 9587 -2398 4130 -1133 N ATOM 2849 N TRP A 164 102.245 45.076 182.852 1.00 97.86 N ANISOU 2849 N TRP A 164 12391 15043 9749 -2147 3676 -2059 N ATOM 2850 CA TRP A 164 102.834 43.828 183.324 1.00102.51 C ANISOU 2850 CA TRP A 164 12857 15513 10578 -1968 3767 -2524 C ATOM 2851 C TRP A 164 101.886 43.050 184.228 1.00 99.27 C ANISOU 2851 C TRP A 164 12438 14839 10442 -1800 3421 -2575 C ATOM 2852 O TRP A 164 101.941 41.816 184.261 1.00101.87 O ANISOU 2852 O TRP A 164 12770 15108 10828 -1701 3409 -2941 O ATOM 2853 CB TRP A 164 104.146 44.112 184.059 1.00104.14 C ANISOU 2853 CB TRP A 164 12799 15548 11223 -1815 3919 -2563 C ATOM 2854 CG TRP A 164 104.886 42.878 184.488 1.00107.59 C ANISOU 2854 CG TRP A 164 13100 15805 11973 -1599 3912 -2929 C ATOM 2855 CD1 TRP A 164 105.782 42.161 183.749 1.00110.89 C ANISOU 2855 CD1 TRP A 164 13515 16294 12325 -1568 4060 -3186 C ATOM 2856 CD2 TRP A 164 104.802 42.225 185.762 1.00106.35 C ANISOU 2856 CD2 TRP A 164 12789 15362 12259 -1388 3739 -3042 C ATOM 2857 NE1 TRP A 164 106.256 41.099 184.481 1.00109.74 N ANISOU 2857 NE1 TRP A 164 13221 15915 12562 -1354 3984 -3436 N ATOM 2858 CE2 TRP A 164 105.671 41.116 185.720 1.00107.87 C ANISOU 2858 CE2 TRP A 164 12895 15459 12634 -1244 3776 -3342 C ATOM 2859 CE3 TRP A 164 104.076 42.469 186.931 1.00101.23 C ANISOU 2859 CE3 TRP A 164 12065 14529 11870 -1311 3555 -2903 C ATOM 2860 CZ2 TRP A 164 105.832 40.253 186.802 1.00106.08 C ANISOU 2860 CZ2 TRP A 164 12519 14960 12826 -1037 3612 -3470 C ATOM 2861 CZ3 TRP A 164 104.237 41.610 188.005 1.00 97.43 C ANISOU 2861 CZ3 TRP A 164 11438 13786 11793 -1100 3397 -3053 C ATOM 2862 CH2 TRP A 164 105.108 40.516 187.932 1.00 99.91 C ANISOU 2862 CH2 TRP A 164 11680 14012 12268 -971 3416 -3316 C ATOM 2863 N TYR A 165 101.015 43.746 184.963 1.00 90.68 N ANISOU 2863 N TYR A 165 11333 13585 9535 -1767 3149 -2216 N ATOM 2864 CA TYR A 165 100.101 43.060 185.870 1.00 84.18 C ANISOU 2864 CA TYR A 165 10487 12521 8978 -1617 2835 -2239 C ATOM 2865 C TYR A 165 99.007 42.324 185.107 1.00 86.62 C ANISOU 2865 C TYR A 165 11017 12926 8969 -1703 2613 -2291 C ATOM 2866 O TYR A 165 98.612 41.218 185.491 1.00 91.10 O ANISOU 2866 O TYR A 165 11583 13351 9679 -1596 2461 -2521 O ATOM 2867 N ALA A 166 98.507 42.918 184.022 1.00 86.74 N ANISOU 2867 N ALA A 166 11221 13181 8555 -1907 2579 -2069 N ATOM 2868 CA ALA A 166 97.431 42.305 183.253 1.00 84.14 C ANISOU 2868 CA ALA A 166 11103 12968 7897 -2016 2341 -2092 C ATOM 2869 C ALA A 166 97.898 41.136 182.395 1.00 89.61 C ANISOU 2869 C ALA A 166 11911 13819 8318 -2068 2501 -2556 C ATOM 2870 O ALA A 166 97.057 40.469 181.784 1.00 89.64 O ANISOU 2870 O ALA A 166 12091 13907 8062 -2159 2303 -2647 O ATOM 2871 N SER A 167 99.204 40.871 182.333 1.00 93.08 N ANISOU 2871 N SER A 167 12247 14295 8822 -2014 2853 -2864 N ATOM 2872 CA SER A 167 99.738 39.801 181.505 1.00100.47 C ANISOU 2872 CA SER A 167 13278 15376 9522 -2053 3054 -3336 C ATOM 2873 C SER A 167 100.528 38.747 182.266 1.00102.84 C ANISOU 2873 C SER A 167 13390 15438 10246 -1829 3184 -3751 C ATOM 2874 O SER A 167 100.688 37.636 181.749 1.00104.21 O ANISOU 2874 O SER A 167 13624 15583 10387 -1791 3183 -4070 O ATOM 2875 N HIS A 168 101.026 39.054 183.465 1.00100.37 N ANISOU 2875 N HIS A 168 12835 14888 10412 -1649 3203 -3653 N ATOM 2876 CA HIS A 168 101.843 38.118 184.223 1.00 91.89 C ANISOU 2876 CA HIS A 168 11557 13547 9811 -1412 3240 -3915 C ATOM 2877 C HIS A 168 101.201 37.655 185.523 1.00 84.97 C ANISOU 2877 C HIS A 168 10578 12381 9325 -1252 3002 -3918 C ATOM 2878 O HIS A 168 101.743 36.753 186.171 1.00 84.28 O ANISOU 2878 O HIS A 168 10339 12047 9636 -1058 2950 -4071 O ATOM 2879 CB HIS A 168 103.215 38.739 184.531 1.00 85.60 C ANISOU 2879 CB HIS A 168 10542 12716 9265 -1330 3454 -3822 C ATOM 2880 CG HIS A 168 104.036 39.022 183.312 1.00 87.07 C ANISOU 2880 CG HIS A 168 10793 13146 9144 -1451 3701 -3861 C ATOM 2881 ND1 HIS A 168 103.704 40.001 182.400 1.00 88.78 N ANISOU 2881 ND1 HIS A 168 11176 13651 8904 -1680 3789 -3645 N ATOM 2882 CD2 HIS A 168 105.177 38.453 182.853 1.00 92.54 C ANISOU 2882 CD2 HIS A 168 11404 13837 9918 -1379 3876 -4075 C ATOM 2883 CE1 HIS A 168 104.604 40.023 181.433 1.00 96.33 C ANISOU 2883 CE1 HIS A 168 12153 14774 9673 -1741 4011 -3733 C ATOM 2884 NE2 HIS A 168 105.508 39.094 181.684 1.00 95.53 N ANISOU 2884 NE2 HIS A 168 11900 14505 9893 -1560 4079 -4008 N ATOM 2885 N MET A 169 100.075 38.240 185.924 1.00 82.46 N ANISOU 2885 N MET A 169 10324 12007 8999 -1294 2704 -3547 N ATOM 2886 CA MET A 169 99.390 37.792 187.129 1.00 87.60 C ANISOU 2886 CA MET A 169 10884 12368 10033 -1142 2417 -3462 C ATOM 2887 C MET A 169 98.727 36.443 186.884 1.00 91.52 C ANISOU 2887 C MET A 169 11496 12772 10504 -1126 2243 -3731 C ATOM 2888 O MET A 169 97.999 36.265 185.902 1.00 93.78 O ANISOU 2888 O MET A 169 11993 13221 10419 -1286 2148 -3753 O ATOM 2889 CB MET A 169 98.350 38.822 187.568 1.00 86.79 C ANISOU 2889 CB MET A 169 10810 12241 9925 -1195 2172 -3002 C ATOM 2890 CG MET A 169 97.604 38.454 188.842 1.00 86.36 C ANISOU 2890 CG MET A 169 10657 11911 10244 -1052 1894 -2890 C ATOM 2891 SD MET A 169 98.670 38.397 190.296 1.00 91.38 S ANISOU 2891 SD MET A 169 11014 12317 11389 -834 2004 -2962 S ATOM 2892 CE MET A 169 97.479 38.004 191.575 1.00 83.97 C ANISOU 2892 CE MET A 169 10030 11122 10754 -728 1647 -2778 C ATOM 2893 N LYS A 170 98.981 35.492 187.778 1.00 89.81 N ANISOU 2893 N LYS A 170 11140 12293 10689 -943 2189 -3928 N ATOM 2894 CA LYS A 170 98.451 34.144 187.656 1.00 86.30 C ANISOU 2894 CA LYS A 170 10780 11707 10301 -912 2033 -4200 C ATOM 2895 C LYS A 170 97.692 33.780 188.923 1.00 83.55 C ANISOU 2895 C LYS A 170 10337 11078 10330 -790 1734 -4022 C ATOM 2896 O LYS A 170 97.976 34.297 190.007 1.00 81.05 O ANISOU 2896 O LYS A 170 9846 10644 10305 -675 1720 -3818 O ATOM 2897 N THR A 171 96.714 32.884 188.772 1.00 81.38 N ANISOU 2897 N THR A 171 10181 10705 10036 -829 1496 -4103 N ATOM 2898 CA THR A 171 95.925 32.444 189.916 1.00 76.18 C ANISOU 2898 CA THR A 171 9441 9787 9715 -733 1214 -3938 C ATOM 2899 C THR A 171 96.738 31.599 190.887 1.00 79.17 C ANISOU 2899 C THR A 171 9633 9900 10547 -527 1269 -4124 C ATOM 2900 O THR A 171 96.360 31.486 192.058 1.00 69.25 O ANISOU 2900 O THR A 171 8263 8449 9598 -429 1088 -3929 O ATOM 2901 CB THR A 171 94.698 31.660 189.444 1.00 73.88 C ANISOU 2901 CB THR A 171 9315 9459 9295 -846 951 -3988 C ATOM 2902 OG1 THR A 171 95.110 30.612 188.558 1.00 81.52 O ANISOU 2902 OG1 THR A 171 10389 10429 10158 -877 1062 -4427 O ATOM 2903 CG2 THR A 171 93.726 32.579 188.720 1.00 69.67 C ANISOU 2903 CG2 THR A 171 8932 9167 8373 -1038 821 -3705 C ATOM 2904 N ARG A 172 97.844 31.005 190.429 1.00 86.80 N ANISOU 2904 N ARG A 172 10553 10872 11554 -455 1464 -4336 N ATOM 2905 CA ARG A 172 98.696 30.225 191.319 1.00 85.25 C ANISOU 2905 CA ARG A 172 10162 10457 11772 -260 1452 -4311 C ATOM 2906 C ARG A 172 99.415 31.095 192.340 1.00 80.38 C ANISOU 2906 C ARG A 172 9345 9832 11364 -168 1517 -4090 C ATOM 2907 O ARG A 172 99.806 30.591 193.399 1.00 80.18 O ANISOU 2907 O ARG A 172 9161 9623 11679 -33 1414 -3984 O ATOM 2908 N ILE A 173 99.600 32.384 192.048 1.00 75.89 N ANISOU 2908 N ILE A 173 8786 9466 10583 -252 1678 -4009 N ATOM 2909 CA ILE A 173 100.157 33.296 193.042 1.00 72.39 C ANISOU 2909 CA ILE A 173 8166 9009 10329 -184 1715 -3782 C ATOM 2910 C ILE A 173 99.113 33.624 194.103 1.00 68.55 C ANISOU 2910 C ILE A 173 7660 8399 9988 -161 1500 -3581 C ATOM 2911 O ILE A 173 99.427 33.713 195.296 1.00 70.23 O ANISOU 2911 O ILE A 173 7716 8491 10476 -58 1410 -3401 O ATOM 2912 CB ILE A 173 100.701 34.566 192.357 1.00 74.64 C ANISOU 2912 CB ILE A 173 8465 9540 10355 -290 1967 -3744 C ATOM 2913 CG1 ILE A 173 102.187 34.406 192.016 1.00 79.94 C ANISOU 2913 CG1 ILE A 173 9027 10259 11087 -246 2157 -3828 C ATOM 2914 CG2 ILE A 173 100.488 35.799 193.230 1.00 74.84 C ANISOU 2914 CG2 ILE A 173 8400 9574 10461 -291 1951 -3484 C ATOM 2915 CD1 ILE A 173 102.483 33.330 190.992 1.00 85.23 C ANISOU 2915 CD1 ILE A 173 9784 10951 11647 -254 2234 -4102 C ATOM 2916 N THR A 174 97.854 33.795 193.688 1.00 63.89 N ANISOU 2916 N THR A 174 7239 7862 9176 -281 1346 -3479 N ATOM 2917 CA THR A 174 96.788 34.090 194.641 1.00 53.04 C ANISOU 2917 CA THR A 174 5849 6388 7914 -277 1092 -3162 C ATOM 2918 C THR A 174 96.611 32.954 195.642 1.00 55.95 C ANISOU 2918 C THR A 174 6129 6497 8630 -151 917 -3218 C ATOM 2919 O THR A 174 96.435 33.196 196.842 1.00 41.70 O ANISOU 2919 O THR A 174 4211 4589 7043 -79 807 -3007 O ATOM 2920 CB THR A 174 95.480 34.361 193.896 1.00 50.40 C ANISOU 2920 CB THR A 174 5700 6167 7282 -436 930 -3006 C ATOM 2921 OG1 THR A 174 95.629 35.526 193.075 1.00 51.50 O ANISOU 2921 OG1 THR A 174 5911 6542 7115 -554 1072 -2887 O ATOM 2922 CG2 THR A 174 94.336 34.582 194.876 1.00 46.80 C ANISOU 2922 CG2 THR A 174 5208 5602 6971 -424 679 -2699 C ATOM 2923 N ARG A 175 96.667 31.706 195.170 1.00 55.54 N ANISOU 2923 N ARG A 175 6132 6335 8636 -128 895 -3502 N ATOM 2924 CA ARG A 175 96.576 30.573 196.084 1.00 51.34 C ANISOU 2924 CA ARG A 175 5514 5577 8415 -18 711 -3439 C ATOM 2925 C ARG A 175 97.785 30.501 197.008 1.00 54.55 C ANISOU 2925 C ARG A 175 5722 5942 9064 117 774 -3335 C ATOM 2926 O ARG A 175 97.658 30.058 198.155 1.00 57.37 O ANISOU 2926 O ARG A 175 5979 6158 9662 192 612 -3166 O ATOM 2927 CB ARG A 175 96.429 29.270 195.298 1.00 55.91 C ANISOU 2927 CB ARG A 175 6199 6081 8964 -36 663 -3653 C ATOM 2928 CG ARG A 175 95.126 29.159 194.521 1.00 68.76 C ANISOU 2928 CG ARG A 175 8024 7735 10367 -195 520 -3728 C ATOM 2929 CD ARG A 175 94.950 27.773 193.924 1.00 81.11 C ANISOU 2929 CD ARG A 175 9681 9187 11949 -204 445 -3915 C ATOM 2930 NE ARG A 175 95.975 27.466 192.930 1.00 92.11 N ANISOU 2930 NE ARG A 175 11109 10681 13207 -190 675 -4171 N ATOM 2931 CZ ARG A 175 95.847 27.705 191.629 1.00 95.48 C ANISOU 2931 CZ ARG A 175 11708 11302 13270 -330 779 -4368 C ATOM 2932 NH1 ARG A 175 94.736 28.256 191.160 1.00 92.25 N ANISOU 2932 NH1 ARG A 175 11449 11013 12587 -505 652 -4335 N ATOM 2933 NH2 ARG A 175 96.831 27.392 190.796 1.00 96.84 N ANISOU 2933 NH2 ARG A 175 11896 11560 13339 -308 999 -4588 N ATOM 2934 N ALA A 176 98.956 30.935 196.534 1.00 55.27 N ANISOU 2934 N ALA A 176 5756 6164 9080 126 993 -3423 N ATOM 2935 CA ALA A 176 100.152 30.900 197.370 1.00 46.30 C ANISOU 2935 CA ALA A 176 4437 4994 8160 219 1024 -3328 C ATOM 2936 C ALA A 176 100.080 31.937 198.484 1.00 43.29 C ANISOU 2936 C ALA A 176 3967 4637 7845 222 965 -3070 C ATOM 2937 O ALA A 176 100.475 31.661 199.623 1.00 42.33 O ANISOU 2937 O ALA A 176 3727 4424 7932 285 847 -2929 O ATOM 2938 CB ALA A 176 101.398 31.116 196.514 1.00 48.68 C ANISOU 2938 CB ALA A 176 4706 5424 8365 209 1265 -3487 C ATOM 2939 N VAL A 177 99.583 33.137 198.177 1.00 44.02 N ANISOU 2939 N VAL A 177 4121 4854 7752 144 1048 -3012 N ATOM 2940 CA VAL A 177 99.466 34.173 199.198 1.00 43.50 C ANISOU 2940 CA VAL A 177 3978 4805 7745 142 1003 -2773 C ATOM 2941 C VAL A 177 98.388 33.805 200.211 1.00 49.03 C ANISOU 2941 C VAL A 177 4677 5367 8586 175 771 -2618 C ATOM 2942 O VAL A 177 98.562 33.997 201.421 1.00 38.95 O ANISOU 2942 O VAL A 177 3310 4050 7440 205 672 -2431 O ATOM 2943 CB VAL A 177 99.190 35.539 198.544 1.00 38.94 C ANISOU 2943 CB VAL A 177 3457 4386 6952 54 1170 -2751 C ATOM 2944 CG1 VAL A 177 99.056 36.621 199.605 1.00 36.48 C ANISOU 2944 CG1 VAL A 177 3067 4079 6716 53 1124 -2500 C ATOM 2945 CG2 VAL A 177 100.293 35.888 197.555 1.00 41.09 C ANISOU 2945 CG2 VAL A 177 3730 4809 7075 6 1406 -2881 C ATOM 2946 N LEU A 178 97.260 33.270 199.736 1.00 46.49 N ANISOU 2946 N LEU A 178 4473 4973 8220 147 673 -2692 N ATOM 2947 CA LEU A 178 96.201 32.851 200.648 1.00 50.96 C ANISOU 2947 CA LEU A 178 5039 5395 8927 163 446 -2532 C ATOM 2948 C LEU A 178 96.652 31.689 201.526 1.00 48.37 C ANISOU 2948 C LEU A 178 4617 4949 8813 242 316 -2476 C ATOM 2949 O LEU A 178 96.299 31.625 202.710 1.00 43.72 O ANISOU 2949 O LEU A 178 3964 4295 8355 265 175 -2277 O ATOM 2950 CB LEU A 178 94.947 32.475 199.858 1.00 65.57 C ANISOU 2950 CB LEU A 178 7054 7238 10621 59 322 -2539 C ATOM 2951 CG LEU A 178 94.221 33.614 199.138 1.00 67.37 C ANISOU 2951 CG LEU A 178 7392 7659 10546 -72 349 -2382 C ATOM 2952 CD1 LEU A 178 93.069 33.073 198.305 1.00 68.81 C ANISOU 2952 CD1 LEU A 178 7726 7847 10570 -183 197 -2393 C ATOM 2953 CD2 LEU A 178 93.726 34.653 200.133 1.00 65.65 C ANISOU 2953 CD2 LEU A 178 7103 7471 10370 -72 299 -2080 C ATOM 2954 N LEU A 179 97.433 30.761 200.967 1.00 52.66 N ANISOU 2954 N LEU A 179 5152 5461 9394 278 368 -2651 N ATOM 2955 CA LEU A 179 97.909 29.629 201.755 1.00 52.64 C ANISOU 2955 CA LEU A 179 5055 5327 9619 353 249 -2610 C ATOM 2956 C LEU A 179 98.994 30.043 202.741 1.00 49.84 C ANISOU 2956 C LEU A 179 4565 5012 9360 387 269 -2489 C ATOM 2957 O LEU A 179 99.067 29.492 203.846 1.00 52.73 O ANISOU 2957 O LEU A 179 4858 5281 9895 421 120 -2355 O ATOM 2958 CB LEU A 179 98.430 28.526 200.834 1.00 56.04 C ANISOU 2958 CB LEU A 179 5514 5695 10084 385 309 -2846 C ATOM 2959 CG LEU A 179 98.754 27.187 201.501 1.00 58.49 C ANISOU 2959 CG LEU A 179 5739 5827 10655 462 174 -2826 C ATOM 2960 CD1 LEU A 179 97.482 26.524 202.011 1.00 48.94 C ANISOU 2960 CD1 LEU A 179 4584 4481 9532 445 -39 -2699 C ATOM 2961 CD2 LEU A 179 99.505 26.270 200.546 1.00 62.48 C ANISOU 2961 CD2 LEU A 179 6253 6281 11204 504 283 -3081 C ATOM 2962 N GLY A 180 99.840 31.003 202.365 1.00 49.21 N ANISOU 2962 N GLY A 180 4462 5070 9165 362 442 -2533 N ATOM 2963 CA GLY A 180 100.895 31.439 203.265 1.00 38.57 C ANISOU 2963 CA GLY A 180 3010 3753 7893 375 447 -2430 C ATOM 2964 C GLY A 180 100.365 32.157 204.492 1.00 39.55 C ANISOU 2964 C GLY A 180 3132 3886 8010 343 332 -2201 C ATOM 2965 O GLY A 180 100.846 31.935 205.607 1.00 36.93 O ANISOU 2965 O GLY A 180 2738 3502 7792 365 228 -2093 O ATOM 2966 N VAL A 181 99.368 33.026 204.306 1.00 38.69 N ANISOU 2966 N VAL A 181 3096 3840 7766 291 353 -2130 N ATOM 2967 CA VAL A 181 98.799 33.764 205.431 1.00 35.35 C ANISOU 2967 CA VAL A 181 2682 3428 7323 258 265 -1921 C ATOM 2968 C VAL A 181 98.115 32.813 206.405 1.00 45.45 C ANISOU 2968 C VAL A 181 3949 4582 8738 284 68 -1808 C ATOM 2969 O VAL A 181 98.211 32.978 207.628 1.00 45.98 O ANISOU 2969 O VAL A 181 4002 4634 8833 277 -17 -1660 O ATOM 2970 CB VAL A 181 97.832 34.849 204.921 1.00 36.59 C ANISOU 2970 CB VAL A 181 2904 3662 7336 207 340 -1875 C ATOM 2971 CG1 VAL A 181 97.132 35.535 206.084 1.00 36.81 C ANISOU 2971 CG1 VAL A 181 2949 3690 7346 178 253 -1663 C ATOM 2972 CG2 VAL A 181 98.579 35.866 204.072 1.00 36.69 C ANISOU 2972 CG2 VAL A 181 2925 3799 7216 169 540 -1955 C ATOM 2973 N TRP A 182 97.417 31.803 205.882 1.00 44.37 N ANISOU 2973 N TRP A 182 3832 4350 8678 309 -7 -1876 N ATOM 2974 CA TRP A 182 96.733 30.844 206.744 1.00 44.99 C ANISOU 2974 CA TRP A 182 3896 4298 8901 324 -198 -1754 C ATOM 2975 C TRP A 182 97.725 30.074 207.610 1.00 48.45 C ANISOU 2975 C TRP A 182 4258 4663 9489 365 -274 -1723 C ATOM 2976 O TRP A 182 97.552 29.970 208.830 1.00 45.57 O ANISOU 2976 O TRP A 182 3881 4255 9178 355 -391 -1551 O ATOM 2977 CB TRP A 182 95.897 29.883 205.895 1.00 49.86 C ANISOU 2977 CB TRP A 182 4567 4813 9566 336 -262 -1850 C ATOM 2978 CG TRP A 182 94.680 30.513 205.279 1.00 54.45 C ANISOU 2978 CG TRP A 182 5241 5420 10026 285 -253 -1838 C ATOM 2979 CD1 TRP A 182 94.039 31.643 205.698 1.00 46.62 C ANISOU 2979 CD1 TRP A 182 4255 4499 8960 247 -236 -1695 C ATOM 2980 CD2 TRP A 182 93.966 30.052 204.123 1.00 54.20 C ANISOU 2980 CD2 TRP A 182 5327 5335 9933 248 -270 -1978 C ATOM 2981 NE1 TRP A 182 92.967 31.910 204.880 1.00 41.23 N ANISOU 2981 NE1 TRP A 182 3676 3798 8191 185 -254 -1720 N ATOM 2982 CE2 TRP A 182 92.901 30.950 203.905 1.00 46.06 C ANISOU 2982 CE2 TRP A 182 4370 4336 8795 168 -286 -1900 C ATOM 2983 CE3 TRP A 182 94.123 28.968 203.254 1.00 52.82 C ANISOU 2983 CE3 TRP A 182 5212 5084 9774 255 -280 -2166 C ATOM 2984 CZ2 TRP A 182 91.998 30.796 202.854 1.00 44.50 C ANISOU 2984 CZ2 TRP A 182 4305 4155 8449 64 -339 -1955 C ATOM 2985 CZ3 TRP A 182 93.225 28.817 202.211 1.00 52.58 C ANISOU 2985 CZ3 TRP A 182 5325 5035 9618 168 -315 -2274 C ATOM 2986 CH2 TRP A 182 92.176 29.726 202.021 1.00 46.48 C ANISOU 2986 CH2 TRP A 182 4624 4314 8721 62 -359 -2181 C ATOM 2987 N LEU A 183 98.778 29.530 206.993 1.00 48.76 N ANISOU 2987 N LEU A 183 4250 4681 9596 414 -203 -1887 N ATOM 2988 CA LEU A 183 99.742 28.728 207.740 1.00 49.34 C ANISOU 2988 CA LEU A 183 4236 4662 9850 466 -282 -1864 C ATOM 2989 C LEU A 183 100.586 29.577 208.683 1.00 48.16 C ANISOU 2989 C LEU A 183 4052 4590 9655 454 -264 -1765 C ATOM 2990 O LEU A 183 100.958 29.111 209.766 1.00 56.07 O ANISOU 2990 O LEU A 183 5009 5519 10778 481 -386 -1651 O ATOM 2991 CB LEU A 183 100.644 27.951 206.779 1.00 53.66 C ANISOU 2991 CB LEU A 183 4734 5160 10496 527 -195 -2076 C ATOM 2992 CG LEU A 183 100.174 26.560 206.339 1.00 50.03 C ANISOU 2992 CG LEU A 183 4282 4540 10188 570 -280 -2158 C ATOM 2993 CD1 LEU A 183 99.958 25.664 207.550 1.00 47.37 C ANISOU 2993 CD1 LEU A 183 3895 4052 10052 589 -487 -1980 C ATOM 2994 CD2 LEU A 183 98.915 26.634 205.489 1.00 48.45 C ANISOU 2994 CD2 LEU A 183 4199 4355 9855 528 -268 -2211 C ATOM 2995 N ALA A 184 100.907 30.812 208.292 1.00 44.23 N ANISOU 2995 N ALA A 184 3582 4236 8987 415 -116 -1803 N ATOM 2996 CA ALA A 184 101.692 31.678 209.167 1.00 40.92 C ANISOU 2996 CA ALA A 184 3141 3889 8516 402 -100 -1719 C ATOM 2997 C ALA A 184 100.906 32.061 210.415 1.00 46.35 C ANISOU 2997 C ALA A 184 3883 4582 9145 372 -210 -1522 C ATOM 2998 O ALA A 184 101.463 32.096 211.519 1.00 36.06 O ANISOU 2998 O ALA A 184 2545 3279 7879 393 -284 -1427 O ATOM 2999 CB ALA A 184 102.140 32.927 208.409 1.00 34.18 C ANISOU 2999 CB ALA A 184 2309 3176 7501 357 82 -1797 C ATOM 3000 N SER A 185 99.611 32.350 210.261 1.00 41.29 N ANISOU 3000 N SER A 185 3321 3955 8411 329 -218 -1458 N ATOM 3001 CA SER A 185 98.796 32.731 211.410 1.00 39.52 C ANISOU 3001 CA SER A 185 3149 3746 8118 303 -298 -1273 C ATOM 3002 C SER A 185 98.565 31.547 212.340 1.00 35.52 C ANISOU 3002 C SER A 185 2613 3120 7763 335 -472 -1155 C ATOM 3003 O SER A 185 98.512 31.713 213.565 1.00 37.32 O ANISOU 3003 O SER A 185 2844 3378 7958 334 -543 -1003 O ATOM 3004 CB SER A 185 97.465 33.314 210.935 1.00 46.93 C ANISOU 3004 CB SER A 185 4165 4721 8944 255 -256 -1233 C ATOM 3005 OG SER A 185 97.669 34.467 210.135 1.00 44.99 O ANISOU 3005 OG SER A 185 3947 4584 8565 223 -102 -1310 O ATOM 3006 N LEU A 186 98.420 30.345 211.779 1.00 32.52 N ANISOU 3006 N LEU A 186 2200 2611 7547 360 -543 -1218 N ATOM 3007 CA LEU A 186 98.276 29.155 212.611 1.00 42.78 C ANISOU 3007 CA LEU A 186 3464 3773 9017 383 -715 -1094 C ATOM 3008 C LEU A 186 99.554 28.870 213.391 1.00 49.38 C ANISOU 3008 C LEU A 186 4222 4592 9949 437 -765 -1065 C ATOM 3009 O LEU A 186 99.499 28.415 214.539 1.00 44.49 O ANISOU 3009 O LEU A 186 3585 3929 9391 445 -900 -887 O ATOM 3010 CB LEU A 186 97.898 27.953 211.745 1.00 44.66 C ANISOU 3010 CB LEU A 186 3677 3873 9420 399 -774 -1188 C ATOM 3011 CG LEU A 186 97.768 26.602 212.454 1.00 45.29 C ANISOU 3011 CG LEU A 186 3715 3783 9713 418 -955 -1066 C ATOM 3012 CD1 LEU A 186 96.636 26.630 213.472 1.00 35.71 C ANISOU 3012 CD1 LEU A 186 2555 2557 8457 357 -1064 -825 C ATOM 3013 CD2 LEU A 186 97.571 25.477 211.448 1.00 41.79 C ANISOU 3013 CD2 LEU A 186 3241 3212 9425 447 -986 -1205 C ATOM 3014 N ALA A 187 100.714 29.141 212.786 1.00 50.74 N ANISOU 3014 N ALA A 187 4337 4805 10136 472 -660 -1224 N ATOM 3015 CA ALA A 187 101.982 28.896 213.467 1.00 49.30 C ANISOU 3015 CA ALA A 187 4060 4606 10065 528 -711 -1201 C ATOM 3016 C ALA A 187 102.162 29.823 214.662 1.00 44.03 C ANISOU 3016 C ALA A 187 3402 4068 9261 509 -736 -1058 C ATOM 3017 O ALA A 187 102.683 29.407 215.704 1.00 37.60 O ANISOU 3017 O ALA A 187 2521 3232 8532 543 -864 -932 O ATOM 3018 CB ALA A 187 103.143 29.052 212.486 1.00 38.53 C ANISOU 3018 CB ALA A 187 2626 3270 8745 563 -574 -1406 C ATOM 3019 N PHE A 188 101.740 31.084 214.534 1.00 36.47 N ANISOU 3019 N PHE A 188 2517 3251 8090 454 -621 -1074 N ATOM 3020 CA PHE A 188 101.848 32.010 215.657 1.00 36.61 C ANISOU 3020 CA PHE A 188 2536 3406 7968 431 -637 -960 C ATOM 3021 C PHE A 188 100.910 31.617 216.791 1.00 33.38 C ANISOU 3021 C PHE A 188 2152 2997 7535 413 -775 -753 C ATOM 3022 O PHE A 188 101.277 31.710 217.968 1.00 34.05 O ANISOU 3022 O PHE A 188 2181 3162 7594 414 -872 -630 O ATOM 3023 CB PHE A 188 101.559 33.439 215.196 1.00 31.78 C ANISOU 3023 CB PHE A 188 1996 2924 7156 372 -475 -1031 C ATOM 3024 CG PHE A 188 101.664 34.462 216.294 1.00 31.16 C ANISOU 3024 CG PHE A 188 1910 2992 6939 339 -478 -949 C ATOM 3025 CD1 PHE A 188 102.900 34.934 216.702 1.00 33.66 C ANISOU 3025 CD1 PHE A 188 2140 3381 7270 349 -475 -991 C ATOM 3026 CD2 PHE A 188 100.528 34.945 216.923 1.00 29.89 C ANISOU 3026 CD2 PHE A 188 1810 2902 6644 293 -485 -840 C ATOM 3027 CE1 PHE A 188 103.003 35.870 217.712 1.00 38.41 C ANISOU 3027 CE1 PHE A 188 2720 4126 7751 306 -487 -938 C ATOM 3028 CE2 PHE A 188 100.624 35.882 217.935 1.00 29.61 C ANISOU 3028 CE2 PHE A 188 1752 3014 6486 252 -483 -792 C ATOM 3029 CZ PHE A 188 101.863 36.345 218.330 1.00 37.73 C ANISOU 3029 CZ PHE A 188 2696 4115 7526 254 -489 -847 C ATOM 3030 N ALA A 189 99.695 31.176 216.457 1.00 32.67 N ANISOU 3030 N ALA A 189 2133 2832 7448 386 -793 -707 N ATOM 3031 CA ALA A 189 98.724 30.810 217.482 1.00 35.54 C ANISOU 3031 CA ALA A 189 2517 3202 7785 354 -911 -497 C ATOM 3032 C ALA A 189 99.071 29.504 218.184 1.00 34.69 C ANISOU 3032 C ALA A 189 2343 2972 7864 386 -1097 -361 C ATOM 3033 O ALA A 189 98.499 29.218 219.241 1.00 35.07 O ANISOU 3033 O ALA A 189 2389 3053 7883 351 -1213 -154 O ATOM 3034 CB ALA A 189 97.326 30.719 216.871 1.00 38.56 C ANISOU 3034 CB ALA A 189 2981 3533 8136 311 -877 -481 C ATOM 3035 N LEU A 190 99.981 28.706 217.624 1.00 48.02 N ANISOU 3035 N LEU A 190 3972 4525 9748 445 -1125 -464 N ATOM 3036 CA LEU A 190 100.422 27.481 218.279 1.00 46.36 C ANISOU 3036 CA LEU A 190 3690 4184 9742 481 -1302 -332 C ATOM 3037 C LEU A 190 101.407 27.736 219.412 1.00 39.82 C ANISOU 3037 C LEU A 190 2776 3466 8887 505 -1390 -222 C ATOM 3038 O LEU A 190 101.724 26.800 220.154 1.00 44.26 O ANISOU 3038 O LEU A 190 3279 3945 9595 525 -1560 -61 O ATOM 3039 CB LEU A 190 101.058 26.534 217.257 1.00 45.36 C ANISOU 3039 CB LEU A 190 3508 3876 9850 539 -1293 -499 C ATOM 3040 CG LEU A 190 100.116 25.781 216.316 1.00 42.23 C ANISOU 3040 CG LEU A 190 3160 3337 9550 514 -1288 -572 C ATOM 3041 CD1 LEU A 190 100.908 25.077 215.229 1.00 41.96 C ANISOU 3041 CD1 LEU A 190 3053 3186 9705 576 -1241 -789 C ATOM 3042 CD2 LEU A 190 99.269 24.786 217.091 1.00 41.21 C ANISOU 3042 CD2 LEU A 190 3042 3085 9529 474 -1464 -344 C ATOM 3043 N LEU A 191 101.888 28.970 219.563 1.00 47.49 N ANISOU 3043 N LEU A 191 3736 4625 9683 494 -1291 -298 N ATOM 3044 CA LEU A 191 102.875 29.264 220.598 1.00 55.21 C ANISOU 3044 CA LEU A 191 4615 5730 10634 506 -1385 -214 C ATOM 3045 C LEU A 191 102.385 28.989 222.020 1.00 59.05 C ANISOU 3045 C LEU A 191 5089 6304 11044 454 -1565 49 C ATOM 3046 O LEU A 191 103.160 28.410 222.799 1.00 51.53 O ANISOU 3046 O LEU A 191 4044 5346 10188 479 -1729 178 O ATOM 3047 CB LEU A 191 103.349 30.718 220.459 1.00 52.85 C ANISOU 3047 CB LEU A 191 4309 5617 10156 479 -1239 -356 C ATOM 3048 CG LEU A 191 104.606 30.991 219.628 1.00 59.43 C ANISOU 3048 CG LEU A 191 5074 6423 11084 531 -1135 -550 C ATOM 3049 CD1 LEU A 191 104.468 30.459 218.212 1.00 67.27 C ANISOU 3049 CD1 LEU A 191 6112 7250 12200 565 -1023 -711 C ATOM 3050 CD2 LEU A 191 104.907 32.481 219.606 1.00 51.85 C ANISOU 3050 CD2 LEU A 191 4120 5643 9938 479 -1001 -654 C ATOM 3051 N PRO A 192 101.165 29.371 222.428 1.00 58.53 N ANISOU 3051 N PRO A 192 5099 6333 10808 376 -1551 147 N ATOM 3052 CA PRO A 192 100.736 29.042 223.801 1.00 55.87 C ANISOU 3052 CA PRO A 192 4740 6097 10392 310 -1729 410 C ATOM 3053 C PRO A 192 100.692 27.552 224.082 1.00 57.38 C ANISOU 3053 C PRO A 192 4918 6091 10793 330 -1907 605 C ATOM 3054 O PRO A 192 100.908 27.141 225.229 1.00 51.72 O ANISOU 3054 O PRO A 192 4153 5444 10056 294 -2090 831 O ATOM 3055 CB PRO A 192 99.339 29.673 223.890 1.00 58.57 C ANISOU 3055 CB PRO A 192 5162 6543 10549 225 -1638 443 C ATOM 3056 CG PRO A 192 99.359 30.764 222.891 1.00 56.18 C ANISOU 3056 CG PRO A 192 4900 6278 10167 243 -1420 191 C ATOM 3057 CD PRO A 192 100.185 30.242 221.756 1.00 53.22 C ANISOU 3057 CD PRO A 192 4521 5713 9988 335 -1372 32 C ATOM 3058 N VAL A 193 100.411 26.729 223.070 1.00 63.84 N ANISOU 3058 N VAL A 193 5776 6669 11811 374 -1865 526 N ATOM 3059 CA VAL A 193 100.470 25.284 223.259 1.00 65.06 C ANISOU 3059 CA VAL A 193 5904 6608 12208 389 -2029 683 C ATOM 3060 C VAL A 193 101.912 24.834 223.448 1.00 57.28 C ANISOU 3060 C VAL A 193 4804 5566 11395 471 -2123 670 C ATOM 3061 O VAL A 193 102.183 23.879 224.186 1.00 54.54 O ANISOU 3061 O VAL A 193 4406 5130 11188 470 -2309 882 O ATOM 3062 CB VAL A 193 99.801 24.565 222.072 1.00 64.20 C ANISOU 3062 CB VAL A 193 5850 6270 12273 399 -1960 561 C ATOM 3063 CG1 VAL A 193 99.791 23.057 222.290 1.00 69.56 C ANISOU 3063 CG1 VAL A 193 6492 6719 13219 399 -2131 718 C ATOM 3064 CG2 VAL A 193 98.390 25.088 221.865 1.00 52.32 C ANISOU 3064 CG2 VAL A 193 4445 4834 10602 320 -1869 576 C ATOM 3065 N LEU A 194 102.856 25.518 222.805 1.00 64.56 N ANISOU 3065 N LEU A 194 5677 6539 12314 536 -1999 438 N ATOM 3066 CA LEU A 194 104.271 25.178 222.891 1.00 67.81 C ANISOU 3066 CA LEU A 194 5961 6905 12901 617 -2067 404 C ATOM 3067 C LEU A 194 104.961 25.788 224.105 1.00 69.36 C ANISOU 3067 C LEU A 194 6078 7326 12950 594 -2184 541 C ATOM 3068 O LEU A 194 106.163 25.565 224.286 1.00 78.10 O ANISOU 3068 O LEU A 194 7063 8417 14196 657 -2260 535 O ATOM 3069 CB LEU A 194 104.991 25.618 221.611 1.00 63.09 C ANISOU 3069 CB LEU A 194 5333 6267 12371 684 -1875 96 C ATOM 3070 CG LEU A 194 105.023 24.652 220.420 1.00 66.16 C ANISOU 3070 CG LEU A 194 5715 6410 13011 739 -1815 -63 C ATOM 3071 CD1 LEU A 194 103.642 24.110 220.072 1.00 58.19 C ANISOU 3071 CD1 LEU A 194 4820 5288 12003 681 -1816 -23 C ATOM 3072 CD2 LEU A 194 105.642 25.333 219.209 1.00 75.66 C ANISOU 3072 CD2 LEU A 194 6901 7648 14197 776 -1605 -358 C ATOM 3073 N GLY A 195 104.244 26.546 224.935 1.00 65.30 N ANISOU 3073 N GLY A 195 5619 7029 12162 498 -2206 655 N ATOM 3074 CA GLY A 195 104.785 27.111 226.153 1.00 66.43 C ANISOU 3074 CA GLY A 195 5690 7415 12135 446 -2338 783 C ATOM 3075 C GLY A 195 104.946 28.617 226.138 1.00 74.76 C ANISOU 3075 C GLY A 195 6738 8715 12954 399 -2202 604 C ATOM 3076 O GLY A 195 105.032 29.226 227.213 1.00 75.29 O ANISOU 3076 O GLY A 195 6769 9023 12816 313 -2304 698 O ATOM 3077 N VAL A 196 104.991 29.235 224.960 1.00 77.68 N ANISOU 3077 N VAL A 196 7141 9032 13341 439 -1981 350 N ATOM 3078 CA VAL A 196 105.209 30.674 224.839 1.00 73.47 C ANISOU 3078 CA VAL A 196 6600 8695 12618 391 -1837 174 C ATOM 3079 C VAL A 196 103.839 31.341 224.741 1.00 67.68 C ANISOU 3079 C VAL A 196 5987 8038 11691 312 -1716 151 C ATOM 3080 O VAL A 196 103.230 31.385 223.671 1.00 68.35 O ANISOU 3080 O VAL A 196 6161 7996 11811 340 -1555 32 O ATOM 3081 CB VAL A 196 106.092 31.013 223.638 1.00 66.56 C ANISOU 3081 CB VAL A 196 5694 7727 11868 464 -1666 -65 C ATOM 3082 CG1 VAL A 196 106.380 32.508 223.597 1.00 61.32 C ANISOU 3082 CG1 VAL A 196 5020 7255 11022 398 -1530 -219 C ATOM 3083 CG2 VAL A 196 107.384 30.212 223.689 1.00 65.34 C ANISOU 3083 CG2 VAL A 196 5404 7473 11947 550 -1782 -39 C ATOM 3084 N GLY A 197 103.359 31.868 225.859 1.00 61.21 N ANISOU 3084 N GLY A 197 5160 7434 10664 206 -1799 263 N ATOM 3085 CA GLY A 197 102.064 32.514 225.925 1.00 52.14 C ANISOU 3085 CA GLY A 197 4096 6374 9341 122 -1694 254 C ATOM 3086 C GLY A 197 101.065 31.677 226.706 1.00 51.31 C ANISOU 3086 C GLY A 197 4027 6267 9201 66 -1839 510 C ATOM 3087 O GLY A 197 101.373 30.602 227.222 1.00 61.45 O ANISOU 3087 O GLY A 197 5284 7475 10589 88 -2026 708 O ATOM 3088 N GLN A 198 99.842 32.198 226.779 1.00 54.16 N ANISOU 3088 N GLN A 198 4447 6708 9424 -13 -1743 517 N ATOM 3089 CA GLN A 198 98.790 31.518 227.521 1.00 52.10 C ANISOU 3089 CA GLN A 198 4217 6469 9110 -91 -1858 773 C ATOM 3090 C GLN A 198 97.430 32.063 227.106 1.00 45.48 C ANISOU 3090 C GLN A 198 3440 5647 8195 -142 -1683 723 C ATOM 3091 O GLN A 198 97.275 33.267 226.885 1.00 36.84 O ANISOU 3091 O GLN A 198 2341 4665 6992 -176 -1519 532 O ATOM 3092 CB GLN A 198 98.990 31.684 229.033 1.00 58.56 C ANISOU 3092 CB GLN A 198 4975 7547 9729 -219 -2045 954 C ATOM 3093 CG GLN A 198 98.044 30.857 229.885 1.00 66.43 C ANISOU 3093 CG GLN A 198 6007 8583 10652 -317 -2185 1279 C ATOM 3094 CD GLN A 198 98.242 31.096 231.369 1.00 74.07 C ANISOU 3094 CD GLN A 198 6938 9853 11351 -474 -2364 1462 C ATOM 3095 OE1 GLN A 198 98.814 32.107 231.776 1.00 67.42 O ANISOU 3095 OE1 GLN A 198 6047 9222 10347 -539 -2356 1308 O ATOM 3096 NE2 GLN A 198 97.771 30.162 232.186 1.00 82.33 N ANISOU 3096 NE2 GLN A 198 8019 10930 12333 -554 -2529 1796 N ATOM 3097 N TYR A 199 96.456 31.164 227.002 1.00 48.52 N ANISOU 3097 N TYR A 199 3876 5905 8654 -152 -1719 899 N ATOM 3098 CA TYR A 199 95.061 31.520 226.785 1.00 44.71 C ANISOU 3098 CA TYR A 199 3433 5450 8105 -216 -1585 913 C ATOM 3099 C TYR A 199 94.301 31.335 228.091 1.00 51.98 C ANISOU 3099 C TYR A 199 4313 6566 8870 -369 -1698 1191 C ATOM 3100 O TYR A 199 94.350 30.256 228.692 1.00 64.19 O ANISOU 3100 O TYR A 199 5863 8068 10460 -394 -1887 1450 O ATOM 3101 CB TYR A 199 94.436 30.657 225.687 1.00 39.11 C ANISOU 3101 CB TYR A 199 2802 4473 7585 -144 -1542 915 C ATOM 3102 CG TYR A 199 95.010 30.873 224.303 1.00 37.25 C ANISOU 3102 CG TYR A 199 2617 4078 7461 -28 -1412 650 C ATOM 3103 CD1 TYR A 199 95.240 32.152 223.813 1.00 39.15 C ANISOU 3103 CD1 TYR A 199 2867 4418 7592 -15 -1235 423 C ATOM 3104 CD2 TYR A 199 95.317 29.793 223.485 1.00 35.30 C ANISOU 3104 CD2 TYR A 199 2404 3580 7428 50 -1467 633 C ATOM 3105 CE1 TYR A 199 95.762 32.348 222.545 1.00 35.74 C ANISOU 3105 CE1 TYR A 199 2485 3857 7236 70 -1121 216 C ATOM 3106 CE2 TYR A 199 95.838 29.979 222.219 1.00 38.37 C ANISOU 3106 CE2 TYR A 199 2829 3850 7899 132 -1350 396 C ATOM 3107 CZ TYR A 199 96.059 31.257 221.754 1.00 35.17 C ANISOU 3107 CZ TYR A 199 2440 3565 7358 139 -1180 201 C ATOM 3108 OH TYR A 199 96.579 31.442 220.492 1.00 31.99 O ANISOU 3108 OH TYR A 199 2073 3059 7021 201 -1068 -8 O ATOM 3109 N THR A 200 93.605 32.380 228.528 1.00 48.60 N ANISOU 3109 N THR A 200 3910 6348 8209 -474 -1533 1122 N ATOM 3110 CA THR A 200 92.869 32.351 229.784 1.00 48.22 C ANISOU 3110 CA THR A 200 3923 6520 7878 -627 -1528 1319 C ATOM 3111 C THR A 200 91.432 32.793 229.544 1.00 39.97 C ANISOU 3111 C THR A 200 2938 5496 6752 -676 -1291 1287 C ATOM 3112 O THR A 200 91.090 33.342 228.494 1.00 40.46 O ANISOU 3112 O THR A 200 2999 5438 6938 -598 -1133 1093 O ATOM 3113 CB THR A 200 93.529 33.242 230.846 1.00 52.59 C ANISOU 3113 CB THR A 200 4488 7356 8138 -724 -1526 1236 C ATOM 3114 OG1 THR A 200 92.873 33.052 232.106 1.00 63.72 O ANISOU 3114 OG1 THR A 200 5963 8994 9253 -883 -1540 1449 O ATOM 3115 CG2 THR A 200 93.429 34.705 230.453 1.00 38.98 C ANISOU 3115 CG2 THR A 200 2787 5700 6324 -718 -1270 910 C ATOM 3116 N VAL A 201 90.586 32.545 230.540 1.00 39.93 N ANISOU 3116 N VAL A 201 2978 5655 6538 -809 -1269 1492 N ATOM 3117 CA VAL A 201 89.180 32.928 230.462 1.00 50.46 C ANISOU 3117 CA VAL A 201 4344 7032 7797 -865 -1042 1486 C ATOM 3118 C VAL A 201 89.065 34.428 230.696 1.00 43.03 C ANISOU 3118 C VAL A 201 3429 6272 6651 -893 -799 1217 C ATOM 3119 O VAL A 201 89.660 34.973 231.633 1.00 42.95 O ANISOU 3119 O VAL A 201 3445 6477 6398 -969 -804 1155 O ATOM 3120 CB VAL A 201 88.341 32.139 231.480 1.00 41.56 C ANISOU 3120 CB VAL A 201 3244 6030 6517 -1008 -1083 1802 C ATOM 3121 CG1 VAL A 201 86.888 32.589 231.432 1.00 41.10 C ANISOU 3121 CG1 VAL A 201 3191 6032 6395 -1065 -829 1784 C ATOM 3122 CG2 VAL A 201 88.443 30.649 231.206 1.00 42.41 C ANISOU 3122 CG2 VAL A 201 3325 5916 6874 -980 -1329 2072 C ATOM 3123 N GLN A 202 88.302 35.098 229.840 1.00 39.13 N ANISOU 3123 N GLN A 202 2924 5681 6261 -834 -596 1058 N ATOM 3124 CA GLN A 202 88.118 36.538 229.911 1.00 36.06 C ANISOU 3124 CA GLN A 202 2549 5404 5748 -840 -355 798 C ATOM 3125 C GLN A 202 86.756 36.879 230.503 1.00 40.29 C ANISOU 3125 C GLN A 202 3092 6078 6137 -928 -139 846 C ATOM 3126 O GLN A 202 85.816 36.081 230.469 1.00 41.83 O ANISOU 3126 O GLN A 202 3266 6231 6395 -960 -152 1058 O ATOM 3127 CB GLN A 202 88.256 37.166 228.523 1.00 35.99 C ANISOU 3127 CB GLN A 202 2513 5191 5972 -707 -272 590 C ATOM 3128 CG GLN A 202 89.563 36.834 227.826 1.00 38.16 C ANISOU 3128 CG GLN A 202 2765 5325 6409 -615 -449 524 C ATOM 3129 CD GLN A 202 90.765 37.443 228.520 1.00 33.68 C ANISOU 3129 CD GLN A 202 2199 4902 5698 -649 -493 391 C ATOM 3130 OE1 GLN A 202 90.674 38.511 229.126 1.00 34.16 O ANISOU 3130 OE1 GLN A 202 2287 5118 5576 -715 -338 238 O ATOM 3131 NE2 GLN A 202 91.900 36.761 228.437 1.00 39.30 N ANISOU 3131 NE2 GLN A 202 2871 5554 6506 -607 -709 440 N ATOM 3132 N TRP A 203 86.664 38.086 231.050 1.00 33.22 N ANISOU 3132 N TRP A 203 2521 5996 4104 -1416 -453 725 N ATOM 3133 CA TRP A 203 85.404 38.566 231.593 1.00 36.09 C ANISOU 3133 CA TRP A 203 2874 6513 4326 -1489 -363 658 C ATOM 3134 C TRP A 203 84.392 38.757 230.463 1.00 34.80 C ANISOU 3134 C TRP A 203 2754 6112 4357 -1384 -279 499 C ATOM 3135 O TRP A 203 84.750 39.240 229.384 1.00 31.64 O ANISOU 3135 O TRP A 203 2405 5494 4124 -1258 -273 358 O ATOM 3136 CB TRP A 203 85.629 39.881 232.343 1.00 36.57 C ANISOU 3136 CB TRP A 203 2930 6784 4180 -1532 -330 509 C ATOM 3137 CG TRP A 203 84.398 40.484 232.947 1.00 41.67 C ANISOU 3137 CG TRP A 203 3551 7610 4670 -1608 -226 397 C ATOM 3138 CD1 TRP A 203 83.921 40.280 234.210 1.00 40.40 C ANISOU 3138 CD1 TRP A 203 3327 7780 4244 -1774 -204 485 C ATOM 3139 CD2 TRP A 203 83.494 41.403 232.320 1.00 37.66 C ANISOU 3139 CD2 TRP A 203 3072 6972 4264 -1524 -131 177 C ATOM 3140 NE1 TRP A 203 82.772 41.009 234.405 1.00 41.56 N ANISOU 3140 NE1 TRP A 203 3458 8007 4327 -1793 -85 300 N ATOM 3141 CE2 TRP A 203 82.489 41.706 233.260 1.00 41.68 C ANISOU 3141 CE2 TRP A 203 3527 7732 4577 -1637 -45 117 C ATOM 3142 CE3 TRP A 203 83.434 41.994 231.053 1.00 28.48 C ANISOU 3142 CE3 TRP A 203 1971 5514 3336 -1373 -117 42 C ATOM 3143 CZ2 TRP A 203 81.437 42.575 232.974 1.00 41.02 C ANISOU 3143 CZ2 TRP A 203 3442 7591 4551 -1590 52 -85 C ATOM 3144 CZ3 TRP A 203 82.388 42.856 230.771 1.00 33.73 C ANISOU 3144 CZ3 TRP A 203 2640 6130 4046 -1335 -37 -118 C ATOM 3145 CH2 TRP A 203 81.404 43.138 231.728 1.00 42.09 C ANISOU 3145 CH2 TRP A 203 3638 7423 4933 -1437 47 -187 C ATOM 3146 N PRO A 204 83.118 38.390 230.676 1.00 36.82 N ANISOU 3146 N PRO A 204 2984 6410 4595 -1438 -218 527 N ATOM 3147 CA PRO A 204 82.546 37.866 231.917 1.00 31.82 C ANISOU 3147 CA PRO A 204 2287 6043 3759 -1596 -207 691 C ATOM 3148 C PRO A 204 82.447 36.345 231.956 1.00 32.86 C ANISOU 3148 C PRO A 204 2390 6120 3975 -1647 -268 946 C ATOM 3149 O PRO A 204 81.414 35.815 232.360 1.00 51.05 O ANISOU 3149 O PRO A 204 4658 8492 6246 -1725 -222 1032 O ATOM 3150 CB PRO A 204 81.151 38.490 231.928 1.00 34.44 C ANISOU 3150 CB PRO A 204 2608 6399 4077 -1599 -88 532 C ATOM 3151 CG PRO A 204 80.817 38.712 230.447 1.00 29.51 C ANISOU 3151 CG PRO A 204 2038 5442 3733 -1440 -68 385 C ATOM 3152 CD PRO A 204 82.082 38.520 229.640 1.00 33.95 C ANISOU 3152 CD PRO A 204 2649 5830 4423 -1347 -150 394 C ATOM 3153 N GLY A 205 83.505 35.654 231.543 1.00 36.28 N ANISOU 3153 N GLY A 205 2832 6421 4531 -1601 -370 1066 N ATOM 3154 CA GLY A 205 83.521 34.208 231.595 1.00 33.77 C ANISOU 3154 CA GLY A 205 2479 6030 4322 -1646 -447 1325 C ATOM 3155 C GLY A 205 82.920 33.516 230.396 1.00 32.61 C ANISOU 3155 C GLY A 205 2359 5596 4434 -1554 -415 1256 C ATOM 3156 O GLY A 205 82.630 32.318 230.475 1.00 35.38 O ANISOU 3156 O GLY A 205 2676 5879 4886 -1600 -462 1457 O ATOM 3157 N THR A 206 82.725 34.227 229.287 1.00 31.20 N ANISOU 3157 N THR A 206 2237 5254 4364 -1433 -344 985 N ATOM 3158 CA THR A 206 82.079 33.671 228.107 1.00 41.11 C ANISOU 3158 CA THR A 206 3518 6281 5821 -1361 -308 885 C ATOM 3159 C THR A 206 83.014 33.535 226.913 1.00 34.39 C ANISOU 3159 C THR A 206 2709 5243 5115 -1250 -342 777 C ATOM 3160 O THR A 206 82.571 33.095 225.847 1.00 28.27 O ANISOU 3160 O THR A 206 1959 4313 4468 -1200 -315 676 O ATOM 3161 CB THR A 206 80.869 34.527 227.717 1.00 47.11 C ANISOU 3161 CB THR A 206 4296 7018 6585 -1328 -199 671 C ATOM 3162 OG1 THR A 206 81.282 35.887 227.528 1.00 39.95 O ANISOU 3162 OG1 THR A 206 3424 6125 5629 -1257 -174 492 O ATOM 3163 CG2 THR A 206 79.805 34.469 228.808 1.00 39.24 C ANISOU 3163 CG2 THR A 206 3246 6199 5466 -1444 -148 771 C ATOM 3164 N TRP A 207 84.287 33.895 227.056 1.00 33.63 N ANISOU 3164 N TRP A 207 2616 5179 4983 -1220 -396 789 N ATOM 3165 CA TRP A 207 85.225 33.812 225.945 1.00 35.20 C ANISOU 3165 CA TRP A 207 2847 5228 5301 -1121 -414 677 C ATOM 3166 C TRP A 207 86.641 33.731 226.494 1.00 35.19 C ANISOU 3166 C TRP A 207 2812 5277 5281 -1124 -505 804 C ATOM 3167 O TRP A 207 86.919 34.171 227.613 1.00 32.89 O ANISOU 3167 O TRP A 207 2494 5159 4845 -1189 -540 906 O ATOM 3168 CB TRP A 207 85.076 35.004 224.990 1.00 37.73 C ANISOU 3168 CB TRP A 207 3228 5497 5611 -1035 -329 394 C ATOM 3169 CG TRP A 207 85.312 36.347 225.626 1.00 38.73 C ANISOU 3169 CG TRP A 207 3363 5723 5629 -1028 -312 322 C ATOM 3170 CD1 TRP A 207 84.562 36.937 226.604 1.00 32.93 C ANISOU 3170 CD1 TRP A 207 2611 5125 4774 -1091 -287 355 C ATOM 3171 CD2 TRP A 207 86.359 37.276 225.310 1.00 37.51 C ANISOU 3171 CD2 TRP A 207 3234 5547 5472 -962 -321 209 C ATOM 3172 NE1 TRP A 207 85.083 38.168 226.923 1.00 32.15 N ANISOU 3172 NE1 TRP A 207 2530 5092 4595 -1069 -286 271 N ATOM 3173 CE2 TRP A 207 86.184 38.402 226.141 1.00 39.42 C ANISOU 3173 CE2 TRP A 207 3478 5896 5604 -986 -311 189 C ATOM 3174 CE3 TRP A 207 87.427 37.264 224.407 1.00 26.81 C ANISOU 3174 CE3 TRP A 207 1892 4117 4179 -903 -337 143 C ATOM 3175 CZ2 TRP A 207 87.040 39.503 226.098 1.00 37.40 C ANISOU 3175 CZ2 TRP A 207 3242 5651 5318 -949 -327 115 C ATOM 3176 CZ3 TRP A 207 88.273 38.360 224.365 1.00 22.18 C ANISOU 3176 CZ3 TRP A 207 1316 3540 3570 -865 -347 68 C ATOM 3177 CH2 TRP A 207 88.075 39.462 225.206 1.00 22.33 C ANISOU 3177 CH2 TRP A 207 1343 3642 3499 -887 -348 65 C ATOM 3178 N CYS A 208 87.530 33.151 225.690 1.00 35.09 N ANISOU 3178 N CYS A 208 2795 5126 5412 -1058 -544 797 N ATOM 3179 CA CYS A 208 88.939 33.014 226.028 1.00 39.61 C ANISOU 3179 CA CYS A 208 3326 5708 6017 -1042 -632 899 C ATOM 3180 C CYS A 208 89.787 33.767 225.013 1.00 40.96 C ANISOU 3180 C CYS A 208 3535 5823 6203 -948 -582 668 C ATOM 3181 O CYS A 208 89.455 33.815 223.825 1.00 45.88 O ANISOU 3181 O CYS A 208 4205 6358 6870 -898 -511 501 O ATOM 3182 CB CYS A 208 89.362 31.537 226.073 1.00 47.78 C ANISOU 3182 CB CYS A 208 4293 6609 7252 -1049 -737 1135 C ATOM 3183 SG CYS A 208 88.849 30.653 227.568 1.00 60.48 S ANISOU 3183 SG CYS A 208 5828 8322 8829 -1184 -842 1505 S ATOM 3184 N PHE A 209 90.881 34.358 225.485 1.00 46.26 N ANISOU 3184 N PHE A 209 4185 6569 6822 -937 -621 669 N ATOM 3185 CA PHE A 209 91.770 35.125 224.623 1.00 41.95 C ANISOU 3185 CA PHE A 209 3665 5991 6282 -861 -575 467 C ATOM 3186 C PHE A 209 93.159 35.146 225.254 1.00 41.63 C ANISOU 3186 C PHE A 209 3564 5995 6257 -856 -662 562 C ATOM 3187 O PHE A 209 93.403 34.525 226.293 1.00 41.44 O ANISOU 3187 O PHE A 209 3482 6023 6239 -912 -765 791 O ATOM 3188 CB PHE A 209 91.220 36.536 224.388 1.00 32.55 C ANISOU 3188 CB PHE A 209 2539 4844 4983 -842 -482 249 C ATOM 3189 CG PHE A 209 91.846 37.250 223.220 1.00 28.11 C ANISOU 3189 CG PHE A 209 2002 4241 4436 -786 -432 83 C ATOM 3190 CD1 PHE A 209 91.876 36.663 221.965 1.00 23.01 C ANISOU 3190 CD1 PHE A 209 1374 3534 3834 -765 -400 50 C ATOM 3191 CD2 PHE A 209 92.395 38.513 223.376 1.00 26.69 C ANISOU 3191 CD2 PHE A 209 1828 4091 4222 -768 -425 -9 C ATOM 3192 CE1 PHE A 209 92.451 37.317 220.891 1.00 22.17 C ANISOU 3192 CE1 PHE A 209 1294 3441 3690 -743 -357 -52 C ATOM 3193 CE2 PHE A 209 92.968 39.173 222.304 1.00 22.93 C ANISOU 3193 CE2 PHE A 209 1377 3587 3748 -730 -378 -134 C ATOM 3194 CZ PHE A 209 92.996 38.573 221.059 1.00 21.05 C ANISOU 3194 CZ PHE A 209 1169 3344 3486 -727 -339 -139 C ATOM 3195 N ILE A 210 94.074 35.869 224.604 1.00 45.91 N ANISOU 3195 N ILE A 210 4117 6528 6799 -798 -623 395 N ATOM 3196 CA ILE A 210 95.450 35.962 225.074 1.00 44.20 C ANISOU 3196 CA ILE A 210 3839 6347 6609 -785 -699 452 C ATOM 3197 C ILE A 210 95.488 36.673 226.418 1.00 38.92 C ANISOU 3197 C ILE A 210 3160 5826 5802 -846 -756 519 C ATOM 3198 O ILE A 210 94.892 37.744 226.593 1.00 43.26 O ANISOU 3198 O ILE A 210 3762 6431 6243 -859 -698 393 O ATOM 3199 CB ILE A 210 96.312 36.690 224.031 1.00 25.22 C ANISOU 3199 CB ILE A 210 1449 3924 4210 -724 -626 248 C ATOM 3200 CG1 ILE A 210 96.292 35.929 222.703 1.00 24.79 C ANISOU 3200 CG1 ILE A 210 1403 3763 4251 -686 -577 219 C ATOM 3201 CG2 ILE A 210 97.733 36.863 224.536 1.00 26.29 C ANISOU 3201 CG2 ILE A 210 1513 4101 4377 -710 -700 290 C ATOM 3202 CD1 ILE A 210 97.055 36.618 221.591 1.00 24.07 C ANISOU 3202 CD1 ILE A 210 1324 3683 4138 -659 -514 94 C ATOM 3203 N SER A 211 96.192 36.079 227.379 1.00 32.45 N ANISOU 3203 N SER A 211 2269 5067 4992 -887 -879 732 N ATOM 3204 CA SER A 211 96.335 36.690 228.692 1.00 36.92 C ANISOU 3204 CA SER A 211 2821 5820 5386 -966 -945 815 C ATOM 3205 C SER A 211 97.315 37.854 228.625 1.00 50.98 C ANISOU 3205 C SER A 211 4603 7629 7139 -924 -933 634 C ATOM 3206 O SER A 211 98.385 37.752 228.018 1.00 45.68 O ANISOU 3206 O SER A 211 3892 6873 6591 -857 -943 573 O ATOM 3207 CB SER A 211 96.813 35.658 229.712 1.00 37.85 C ANISOU 3207 CB SER A 211 2861 6007 5516 -1033 -1095 1121 C ATOM 3208 OG SER A 211 96.859 36.213 231.015 1.00 55.92 O ANISOU 3208 OG SER A 211 5139 8526 7584 -1135 -1157 1209 O ATOM 3209 N THR A 212 96.946 38.965 229.266 1.00 57.44 N ANISOU 3209 N THR A 212 5458 8568 7798 -971 -912 551 N ATOM 3210 CA THR A 212 97.730 40.194 229.213 1.00 55.67 C ANISOU 3210 CA THR A 212 5240 8344 7568 -938 -901 378 C ATOM 3211 C THR A 212 98.191 40.647 230.595 1.00 60.22 C ANISOU 3211 C THR A 212 5784 9126 7973 -1026 -996 460 C ATOM 3212 O THR A 212 98.567 41.810 230.767 1.00 64.67 O ANISOU 3212 O THR A 212 6361 9714 8497 -1024 -987 321 O ATOM 3213 CB THR A 212 96.930 41.305 228.531 1.00 51.83 C ANISOU 3213 CB THR A 212 4833 7766 7092 -901 -788 181 C ATOM 3214 OG1 THR A 212 97.667 42.533 228.584 1.00 60.15 O ANISOU 3214 OG1 THR A 212 5890 8808 8156 -885 -797 63 O ATOM 3215 CG2 THR A 212 95.589 41.493 229.222 1.00 54.48 C ANISOU 3215 CG2 THR A 212 5210 8226 7266 -979 -756 226 C ATOM 3216 N GLY A 213 98.172 39.756 231.580 1.00 65.46 N ANISOU 3216 N GLY A 213 6401 9937 8532 -1112 -1094 695 N ATOM 3217 CA GLY A 213 98.610 40.101 232.920 1.00 72.18 C ANISOU 3217 CA GLY A 213 7219 11020 9187 -1213 -1190 783 C ATOM 3218 C GLY A 213 97.481 40.118 233.932 1.00 80.70 C ANISOU 3218 C GLY A 213 8317 12337 10007 -1349 -1173 879 C ATOM 3219 O GLY A 213 97.526 39.411 234.939 1.00 90.42 O ANISOU 3219 O GLY A 213 9503 13750 11101 -1456 -1271 1114 O ATOM 3220 N GLY A 226 106.571 33.447 228.836 1.00 63.31 N ANISOU 3220 N GLY A 226 5448 8722 9887 -606 -1612 1317 N ATOM 3221 CA GLY A 226 106.558 34.734 228.165 1.00 57.83 C ANISOU 3221 CA GLY A 226 4816 8120 9037 -595 -1465 1030 C ATOM 3222 C GLY A 226 105.175 35.164 227.719 1.00 64.48 C ANISOU 3222 C GLY A 226 5782 8987 9730 -625 -1338 915 C ATOM 3223 O GLY A 226 104.901 35.269 226.524 1.00 69.60 O ANISOU 3223 O GLY A 226 6472 9558 10416 -582 -1203 755 O ATOM 3224 N ASN A 227 104.296 35.413 228.693 1.00 58.34 N ANISOU 3224 N ASN A 227 5063 8330 8775 -708 -1382 1005 N ATOM 3225 CA ASN A 227 102.933 35.822 228.371 1.00 51.39 C ANISOU 3225 CA ASN A 227 4291 7472 7764 -738 -1269 904 C ATOM 3226 C ASN A 227 102.898 37.244 227.825 1.00 47.74 C ANISOU 3226 C ASN A 227 3890 7067 7180 -724 -1143 620 C ATOM 3227 O ASN A 227 102.134 37.541 226.899 1.00 40.74 O ANISOU 3227 O ASN A 227 3077 6130 6274 -703 -1015 470 O ATOM 3228 CB ASN A 227 102.044 35.701 229.608 1.00 55.85 C ANISOU 3228 CB ASN A 227 4886 8167 8166 -842 -1347 1092 C ATOM 3229 CG ASN A 227 101.905 34.270 230.087 1.00 55.06 C ANISOU 3229 CG ASN A 227 4731 7998 8191 -872 -1466 1400 C ATOM 3230 OD1 ASN A 227 102.775 33.434 229.839 1.00 61.43 O ANISOU 3230 OD1 ASN A 227 5454 8666 9219 -815 -1537 1498 O ATOM 3231 ND2 ASN A 227 100.809 33.980 230.777 1.00 47.92 N ANISOU 3231 ND2 ASN A 227 3864 7183 7160 -966 -1489 1561 N ATOM 3232 N LEU A 228 103.718 38.136 228.386 1.00 57.32 N ANISOU 3232 N LEU A 228 5072 8380 8327 -737 -1187 548 N ATOM 3233 CA LEU A 228 103.732 39.521 227.927 1.00 45.58 C ANISOU 3233 CA LEU A 228 3633 6915 6771 -725 -1084 294 C ATOM 3234 C LEU A 228 104.399 39.661 226.565 1.00 36.62 C ANISOU 3234 C LEU A 228 2475 5711 5726 -667 -976 148 C ATOM 3235 O LEU A 228 104.042 40.559 225.794 1.00 29.50 O ANISOU 3235 O LEU A 228 1628 4797 4786 -671 -870 -3 O ATOM 3236 CB LEU A 228 104.432 40.406 228.958 1.00 41.12 C ANISOU 3236 CB LEU A 228 3033 6459 6132 -764 -1177 272 C ATOM 3237 CG LEU A 228 103.746 40.524 230.318 1.00 39.52 C ANISOU 3237 CG LEU A 228 2864 6394 5758 -856 -1268 409 C ATOM 3238 CD1 LEU A 228 104.520 41.460 231.232 1.00 45.33 C ANISOU 3238 CD1 LEU A 228 3566 7245 6412 -898 -1357 362 C ATOM 3239 CD2 LEU A 228 102.313 41.001 230.149 1.00 32.51 C ANISOU 3239 CD2 LEU A 228 2082 5497 4775 -883 -1166 338 C ATOM 3240 N PHE A 229 105.367 38.797 226.250 1.00 31.99 N ANISOU 3240 N PHE A 229 1804 5083 5269 -627 -1015 238 N ATOM 3241 CA PHE A 229 105.978 38.832 224.926 1.00 38.67 C ANISOU 3241 CA PHE A 229 2628 5878 6187 -590 -915 155 C ATOM 3242 C PHE A 229 104.992 38.381 223.856 1.00 34.52 C ANISOU 3242 C PHE A 229 2181 5266 5669 -577 -812 135 C ATOM 3243 O PHE A 229 104.859 39.025 222.808 1.00 28.87 O ANISOU 3243 O PHE A 229 1513 4555 4901 -588 -705 37 O ATOM 3244 CB PHE A 229 107.236 37.961 224.893 1.00 33.21 C ANISOU 3244 CB PHE A 229 1816 5125 5676 -540 -987 259 C ATOM 3245 CG PHE A 229 107.698 37.627 223.503 1.00 32.87 C ANISOU 3245 CG PHE A 229 1752 4987 5750 -493 -888 210 C ATOM 3246 CD1 PHE A 229 108.346 38.575 222.728 1.00 32.44 C ANISOU 3246 CD1 PHE A 229 1689 4978 5660 -508 -805 107 C ATOM 3247 CD2 PHE A 229 107.475 36.369 222.966 1.00 33.39 C ANISOU 3247 CD2 PHE A 229 1796 4883 6009 -441 -890 291 C ATOM 3248 CE1 PHE A 229 108.765 38.275 221.444 1.00 32.36 C ANISOU 3248 CE1 PHE A 229 1659 4871 5766 -470 -716 73 C ATOM 3249 CE2 PHE A 229 107.893 36.062 221.683 1.00 35.39 C ANISOU 3249 CE2 PHE A 229 2023 5032 6390 -395 -798 221 C ATOM 3250 CZ PHE A 229 108.540 37.016 220.922 1.00 32.71 C ANISOU 3250 CZ PHE A 229 1687 4769 5974 -409 -706 109 C ATOM 3251 N PHE A 230 104.296 37.268 224.101 1.00 30.37 N ANISOU 3251 N PHE A 230 1665 4655 5218 -564 -856 257 N ATOM 3252 CA PHE A 230 103.349 36.757 223.117 1.00 29.23 C ANISOU 3252 CA PHE A 230 1589 4420 5099 -552 -771 234 C ATOM 3253 C PHE A 230 102.182 37.717 222.921 1.00 36.16 C ANISOU 3253 C PHE A 230 2576 5368 5795 -598 -686 120 C ATOM 3254 O PHE A 230 101.688 37.880 221.798 1.00 38.29 O ANISOU 3254 O PHE A 230 2906 5605 6039 -598 -594 54 O ATOM 3255 CB PHE A 230 102.848 35.379 223.545 1.00 30.41 C ANISOU 3255 CB PHE A 230 1706 4440 5407 -540 -859 418 C ATOM 3256 CG PHE A 230 101.867 34.770 222.589 1.00 35.78 C ANISOU 3256 CG PHE A 230 2444 5009 6142 -526 -785 390 C ATOM 3257 CD1 PHE A 230 102.292 34.261 221.374 1.00 31.47 C ANISOU 3257 CD1 PHE A 230 1871 4337 5750 -472 -726 326 C ATOM 3258 CD2 PHE A 230 100.520 34.705 222.905 1.00 44.93 C ANISOU 3258 CD2 PHE A 230 3677 6186 7207 -570 -774 420 C ATOM 3259 CE1 PHE A 230 101.391 33.698 220.491 1.00 41.57 C ANISOU 3259 CE1 PHE A 230 3198 5508 7087 -461 -667 287 C ATOM 3260 CE2 PHE A 230 99.614 34.144 222.025 1.00 28.03 C ANISOU 3260 CE2 PHE A 230 1585 3945 5121 -560 -714 388 C ATOM 3261 CZ PHE A 230 100.050 33.641 220.816 1.00 30.22 C ANISOU 3261 CZ PHE A 230 1837 4095 5549 -506 -664 320 C ATOM 3262 N ALA A 231 101.728 38.362 223.998 1.00 27.48 N ANISOU 3262 N ALA A 231 1500 4347 4595 -636 -727 109 N ATOM 3263 CA ALA A 231 100.665 39.352 223.870 1.00 26.13 C ANISOU 3263 CA ALA A 231 1415 4201 4312 -666 -656 -8 C ATOM 3264 C ALA A 231 101.144 40.598 223.137 1.00 34.58 C ANISOU 3264 C ALA A 231 2507 5305 5327 -670 -580 -150 C ATOM 3265 O ALA A 231 100.338 41.294 222.508 1.00 39.42 O ANISOU 3265 O ALA A 231 3230 5884 5863 -671 -495 -222 O ATOM 3266 CB ALA A 231 100.121 39.721 225.250 1.00 26.59 C ANISOU 3266 CB ALA A 231 1488 4302 4312 -701 -728 39 C ATOM 3267 N SER A 232 102.443 40.895 223.199 1.00 26.25 N ANISOU 3267 N SER A 232 1382 4296 4295 -666 -608 -155 N ATOM 3268 CA SER A 232 102.979 42.047 222.484 1.00 29.56 C ANISOU 3268 CA SER A 232 1855 4746 4631 -680 -533 -221 C ATOM 3269 C SER A 232 103.257 41.729 221.022 1.00 34.28 C ANISOU 3269 C SER A 232 2459 5322 5245 -685 -475 -141 C ATOM 3270 O SER A 232 103.127 42.610 220.165 1.00 27.17 O ANISOU 3270 O SER A 232 1636 4408 4279 -711 -424 -110 O ATOM 3271 CB SER A 232 104.254 42.546 223.165 1.00 35.47 C ANISOU 3271 CB SER A 232 2517 5547 5415 -683 -595 -243 C ATOM 3272 OG SER A 232 103.998 42.941 224.501 1.00 39.85 O ANISOU 3272 OG SER A 232 3059 6066 6017 -679 -687 -281 O ATOM 3273 N ALA A 233 103.643 40.486 220.720 1.00 39.22 N ANISOU 3273 N ALA A 233 2999 5884 6018 -645 -500 -91 N ATOM 3274 CA ALA A 233 103.866 40.098 219.332 1.00 29.94 C ANISOU 3274 CA ALA A 233 1835 4604 4935 -613 -437 -77 C ATOM 3275 C ALA A 233 102.575 40.143 218.525 1.00 24.43 C ANISOU 3275 C ALA A 233 1247 3860 4175 -626 -380 -88 C ATOM 3276 O ALA A 233 102.600 40.467 217.331 1.00 23.95 O ANISOU 3276 O ALA A 233 1225 3740 4136 -620 -320 -110 O ATOM 3277 CB ALA A 233 104.486 38.703 219.270 1.00 26.98 C ANISOU 3277 CB ALA A 233 1373 4121 4759 -545 -470 -42 C ATOM 3278 N PHE A 234 101.442 39.819 219.152 1.00 28.40 N ANISOU 3278 N PHE A 234 1794 4381 4615 -641 -400 -82 N ATOM 3279 CA PHE A 234 100.165 39.891 218.450 1.00 33.10 C ANISOU 3279 CA PHE A 234 2488 4939 5151 -656 -356 -88 C ATOM 3280 C PHE A 234 99.781 41.333 218.144 1.00 36.39 C ANISOU 3280 C PHE A 234 2998 5384 5443 -692 -330 -79 C ATOM 3281 O PHE A 234 99.272 41.628 217.056 1.00 38.50 O ANISOU 3281 O PHE A 234 3319 5582 5727 -691 -295 -79 O ATOM 3282 CB PHE A 234 99.072 39.208 219.275 1.00 29.89 C ANISOU 3282 CB PHE A 234 2096 4535 4728 -661 -382 -85 C ATOM 3283 CG PHE A 234 97.685 39.390 218.718 1.00 28.13 C ANISOU 3283 CG PHE A 234 1966 4293 4427 -684 -342 -94 C ATOM 3284 CD1 PHE A 234 97.194 38.527 217.752 1.00 33.23 C ANISOU 3284 CD1 PHE A 234 2637 4826 5162 -657 -322 -85 C ATOM 3285 CD2 PHE A 234 96.870 40.420 219.167 1.00 20.99 C ANISOU 3285 CD2 PHE A 234 1158 3438 3380 -705 -323 -116 C ATOM 3286 CE1 PHE A 234 95.918 38.693 217.237 1.00 32.64 C ANISOU 3286 CE1 PHE A 234 2643 4732 5028 -676 -297 -92 C ATOM 3287 CE2 PHE A 234 95.597 40.591 218.655 1.00 20.16 C ANISOU 3287 CE2 PHE A 234 1138 3301 3222 -717 -301 -93 C ATOM 3288 CZ PHE A 234 95.120 39.726 217.690 1.00 19.98 C ANISOU 3288 CZ PHE A 234 1109 3196 3286 -708 -292 -85 C ATOM 3289 N ALA A 235 100.011 42.244 219.093 1.00 36.80 N ANISOU 3289 N ALA A 235 3072 5511 5401 -715 -354 -72 N ATOM 3290 CA ALA A 235 99.596 43.630 218.906 1.00 21.37 C ANISOU 3290 CA ALA A 235 1203 3500 3416 -735 -366 0 C ATOM 3291 C ALA A 235 100.403 44.312 217.807 1.00 28.69 C ANISOU 3291 C ALA A 235 2107 4366 4428 -729 -335 -31 C ATOM 3292 O ALA A 235 99.839 45.035 216.976 1.00 20.67 O ANISOU 3292 O ALA A 235 1144 3281 3429 -728 -306 -57 O ATOM 3293 CB ALA A 235 99.723 44.397 220.222 1.00 21.80 C ANISOU 3293 CB ALA A 235 1267 3552 3466 -756 -443 91 C ATOM 3294 N PHE A 236 101.721 44.095 217.784 1.00 26.69 N ANISOU 3294 N PHE A 236 1762 4157 4222 -728 -333 -49 N ATOM 3295 CA PHE A 236 102.550 44.724 216.759 1.00 27.78 C ANISOU 3295 CA PHE A 236 1863 4260 4431 -733 -292 -80 C ATOM 3296 C PHE A 236 102.290 44.135 215.378 1.00 29.30 C ANISOU 3296 C PHE A 236 2080 4379 4672 -700 -221 -135 C ATOM 3297 O PHE A 236 102.415 44.844 214.373 1.00 21.99 O ANISOU 3297 O PHE A 236 1180 3419 3756 -708 -171 -170 O ATOM 3298 CB PHE A 236 104.029 44.600 217.124 1.00 31.85 C ANISOU 3298 CB PHE A 236 2267 4833 5000 -735 -307 -84 C ATOM 3299 CG PHE A 236 104.485 45.599 218.151 1.00 41.77 C ANISOU 3299 CG PHE A 236 3523 6135 6212 -768 -362 -56 C ATOM 3300 CD1 PHE A 236 104.648 46.934 217.814 1.00 49.26 C ANISOU 3300 CD1 PHE A 236 4497 7041 7178 -796 -353 -65 C ATOM 3301 CD2 PHE A 236 104.753 45.204 219.451 1.00 37.99 C ANISOU 3301 CD2 PHE A 236 3008 5750 5677 -775 -422 -39 C ATOM 3302 CE1 PHE A 236 105.065 47.858 218.758 1.00 42.41 C ANISOU 3302 CE1 PHE A 236 3618 6194 6303 -828 -410 -49 C ATOM 3303 CE2 PHE A 236 105.171 46.123 220.399 1.00 37.67 C ANISOU 3303 CE2 PHE A 236 2964 5751 5600 -813 -480 -6 C ATOM 3304 CZ PHE A 236 105.327 47.451 220.051 1.00 37.88 C ANISOU 3304 CZ PHE A 236 3013 5690 5688 -836 -482 -3 C ATOM 3305 N LEU A 237 101.935 42.848 215.305 1.00 27.59 N ANISOU 3305 N LEU A 237 1850 4144 4489 -669 -216 -148 N ATOM 3306 CA LEU A 237 101.558 42.261 214.022 1.00 22.00 C ANISOU 3306 CA LEU A 237 1167 3365 3828 -644 -153 -210 C ATOM 3307 C LEU A 237 100.315 42.932 213.455 1.00 30.90 C ANISOU 3307 C LEU A 237 2398 4465 4877 -664 -140 -215 C ATOM 3308 O LEU A 237 100.232 43.181 212.247 1.00 40.87 O ANISOU 3308 O LEU A 237 3684 5702 6141 -669 -86 -266 O ATOM 3309 CB LEU A 237 101.332 40.756 214.172 1.00 22.39 C ANISOU 3309 CB LEU A 237 1180 3375 3954 -606 -163 -223 C ATOM 3310 CG LEU A 237 102.566 39.854 214.124 1.00 23.70 C ANISOU 3310 CG LEU A 237 1230 3511 4264 -563 -153 -254 C ATOM 3311 CD1 LEU A 237 102.179 38.409 214.390 1.00 33.42 C ANISOU 3311 CD1 LEU A 237 2429 4671 5599 -523 -179 -253 C ATOM 3312 CD2 LEU A 237 103.261 39.979 212.778 1.00 24.18 C ANISOU 3312 CD2 LEU A 237 1261 3542 4384 -554 -65 -341 C ATOM 3313 N GLY A 238 99.337 43.230 214.311 1.00 24.90 N ANISOU 3313 N GLY A 238 1692 3721 4048 -678 -189 -165 N ATOM 3314 CA GLY A 238 98.156 43.940 213.850 1.00 22.94 C ANISOU 3314 CA GLY A 238 1532 3438 3746 -689 -184 -172 C ATOM 3315 C GLY A 238 98.476 45.347 213.381 1.00 28.19 C ANISOU 3315 C GLY A 238 2216 4097 4397 -709 -168 -185 C ATOM 3316 O GLY A 238 97.996 45.788 212.332 1.00 19.13 O ANISOU 3316 O GLY A 238 1111 2926 3233 -720 -138 -212 O ATOM 3317 N LEU A 239 99.292 46.072 214.153 1.00 19.82 N ANISOU 3317 N LEU A 239 1120 3066 3344 -724 -193 -161 N ATOM 3318 CA LEU A 239 99.711 47.407 213.736 1.00 27.03 C ANISOU 3318 CA LEU A 239 2038 3972 4260 -751 -179 -172 C ATOM 3319 C LEU A 239 100.494 47.364 212.432 1.00 27.89 C ANISOU 3319 C LEU A 239 2113 4083 4400 -764 -118 -199 C ATOM 3320 O LEU A 239 100.431 48.309 211.637 1.00 23.94 O ANISOU 3320 O LEU A 239 1631 3573 3893 -797 -97 -198 O ATOM 3321 CB LEU A 239 100.549 48.068 214.831 1.00 28.20 C ANISOU 3321 CB LEU A 239 2140 4151 4423 -769 -221 -152 C ATOM 3322 CG LEU A 239 99.904 48.238 216.210 1.00 36.15 C ANISOU 3322 CG LEU A 239 3165 5166 5403 -768 -281 -131 C ATOM 3323 CD1 LEU A 239 100.895 48.846 217.193 1.00 29.18 C ANISOU 3323 CD1 LEU A 239 2224 4320 4545 -794 -326 -121 C ATOM 3324 CD2 LEU A 239 98.635 49.076 216.130 1.00 25.16 C ANISOU 3324 CD2 LEU A 239 1848 3734 3979 -767 -279 -161 C ATOM 3325 N LEU A 240 101.243 46.283 212.198 1.00 35.43 N ANISOU 3325 N LEU A 240 3007 5054 5400 -744 -87 -222 N ATOM 3326 CA LEU A 240 101.944 46.129 210.928 1.00 30.10 C ANISOU 3326 CA LEU A 240 2290 4389 4759 -756 -13 -266 C ATOM 3327 C LEU A 240 100.967 45.933 209.775 1.00 31.54 C ANISOU 3327 C LEU A 240 2530 4553 4902 -767 23 -298 C ATOM 3328 O LEU A 240 101.154 46.502 208.693 1.00 26.39 O ANISOU 3328 O LEU A 240 1873 3919 4235 -808 72 -309 O ATOM 3329 CB LEU A 240 102.920 44.956 211.009 1.00 26.60 C ANISOU 3329 CB LEU A 240 1756 3956 4392 -723 14 -302 C ATOM 3330 CG LEU A 240 103.718 44.649 209.739 1.00 31.88 C ANISOU 3330 CG LEU A 240 2364 4641 5108 -731 108 -370 C ATOM 3331 CD1 LEU A 240 104.684 45.780 209.417 1.00 24.13 C ANISOU 3331 CD1 LEU A 240 1338 3699 4132 -777 140 -348 C ATOM 3332 CD2 LEU A 240 104.456 43.326 209.872 1.00 27.52 C ANISOU 3332 CD2 LEU A 240 1722 4076 4660 -681 131 -423 C ATOM 3333 N ALA A 241 99.918 45.133 209.987 1.00 37.74 N ANISOU 3333 N ALA A 241 3362 5311 5668 -739 -3 -308 N ATOM 3334 CA ALA A 241 98.957 44.872 208.918 1.00 30.57 C ANISOU 3334 CA ALA A 241 2502 4391 4722 -754 21 -345 C ATOM 3335 C ALA A 241 98.178 46.129 208.552 1.00 26.57 C ANISOU 3335 C ALA A 241 2056 3880 4161 -791 -4 -302 C ATOM 3336 O ALA A 241 97.885 46.363 207.373 1.00 20.02 O ANISOU 3336 O ALA A 241 1238 3065 3302 -831 26 -319 O ATOM 3337 CB ALA A 241 98.006 43.749 209.328 1.00 19.82 C ANISOU 3337 CB ALA A 241 1169 2995 3366 -720 -9 -359 C ATOM 3338 N LEU A 242 97.833 46.951 209.547 1.00 21.42 N ANISOU 3338 N LEU A 242 1432 3209 3499 -785 -60 -250 N ATOM 3339 CA LEU A 242 97.176 48.219 209.255 1.00 19.15 C ANISOU 3339 CA LEU A 242 1182 2902 3191 -818 -90 -210 C ATOM 3340 C LEU A 242 98.129 49.205 208.593 1.00 24.53 C ANISOU 3340 C LEU A 242 1821 3600 3899 -868 -63 -184 C ATOM 3341 O LEU A 242 97.699 50.025 207.775 1.00 32.31 O ANISOU 3341 O LEU A 242 2820 4569 4887 -911 -72 -148 O ATOM 3342 CB LEU A 242 96.601 48.826 210.534 1.00 21.99 C ANISOU 3342 CB LEU A 242 1572 3242 3542 -800 -145 -185 C ATOM 3343 CG LEU A 242 95.486 48.048 211.235 1.00 27.16 C ANISOU 3343 CG LEU A 242 2266 3884 4172 -763 -170 -195 C ATOM 3344 CD1 LEU A 242 94.891 48.875 212.367 1.00 17.88 C ANISOU 3344 CD1 LEU A 242 1110 2699 2984 -757 -209 -185 C ATOM 3345 CD2 LEU A 242 94.413 47.628 210.245 1.00 29.22 C ANISOU 3345 CD2 LEU A 242 2564 4127 4412 -768 -169 -203 C ATOM 3346 N THR A 243 99.420 49.144 208.930 1.00 22.23 N ANISOU 3346 N THR A 243 1469 3337 3641 -868 -35 -192 N ATOM 3347 CA THR A 243 100.384 50.062 208.332 1.00 29.63 C ANISOU 3347 CA THR A 243 2354 4292 4612 -921 -3 -160 C ATOM 3348 C THR A 243 100.603 49.747 206.857 1.00 34.12 C ANISOU 3348 C THR A 243 2899 4896 5168 -960 74 -182 C ATOM 3349 O THR A 243 100.641 50.657 206.021 1.00 32.35 O ANISOU 3349 O THR A 243 2664 4672 4955 -1021 92 -137 O ATOM 3350 CB THR A 243 101.709 50.008 209.095 1.00 30.83 C ANISOU 3350 CB THR A 243 2437 4471 4805 -912 6 -167 C ATOM 3351 OG1 THR A 243 101.471 50.259 210.486 1.00 27.52 O ANISOU 3351 OG1 THR A 243 2040 4036 4381 -885 -62 -160 O ATOM 3352 CG2 THR A 243 102.675 51.056 208.564 1.00 22.94 C ANISOU 3352 CG2 THR A 243 1379 3490 3849 -975 34 -125 C ATOM 3353 N VAL A 244 100.755 48.463 206.521 1.00 32.90 N ANISOU 3353 N VAL A 244 2730 4774 4996 -933 126 -256 N ATOM 3354 CA VAL A 244 100.908 48.070 205.122 1.00 26.94 C ANISOU 3354 CA VAL A 244 1954 4076 4206 -977 213 -305 C ATOM 3355 C VAL A 244 99.654 48.416 204.328 1.00 25.37 C ANISOU 3355 C VAL A 244 1820 3877 3942 -1021 190 -294 C ATOM 3356 O VAL A 244 99.735 48.896 203.191 1.00 24.46 O ANISOU 3356 O VAL A 244 1689 3839 3765 -1115 257 -318 O ATOM 3357 CB VAL A 244 101.243 46.569 205.024 1.00 23.17 C ANISOU 3357 CB VAL A 244 1439 3624 3740 -936 269 -417 C ATOM 3358 CG1 VAL A 244 101.355 46.141 203.571 1.00 24.57 C ANISOU 3358 CG1 VAL A 244 1581 3901 3853 -1011 393 -557 C ATOM 3359 CG2 VAL A 244 102.530 46.266 205.768 1.00 23.71 C ANISOU 3359 CG2 VAL A 244 1429 3691 3891 -896 284 -421 C ATOM 3360 N THR A 245 98.477 48.184 204.916 1.00 21.42 N ANISOU 3360 N THR A 245 1386 3318 3436 -976 109 -279 N ATOM 3361 CA THR A 245 97.229 48.445 204.205 1.00 22.30 C ANISOU 3361 CA THR A 245 1551 3423 3500 -1011 73 -268 C ATOM 3362 C THR A 245 97.016 49.937 203.982 1.00 21.41 C ANISOU 3362 C THR A 245 1441 3271 3422 -1057 34 -179 C ATOM 3363 O THR A 245 96.597 50.355 202.896 1.00 22.27 O ANISOU 3363 O THR A 245 1555 3443 3461 -1148 57 -191 O ATOM 3364 CB THR A 245 96.050 47.848 204.975 1.00 25.36 C ANISOU 3364 CB THR A 245 1994 3754 3889 -950 1 -272 C ATOM 3365 OG1 THR A 245 96.233 46.434 205.109 1.00 31.34 O ANISOU 3365 OG1 THR A 245 2738 4528 4640 -913 37 -352 O ATOM 3366 CG2 THR A 245 94.743 48.112 204.243 1.00 23.10 C ANISOU 3366 CG2 THR A 245 1754 3454 3571 -982 -48 -257 C ATOM 3367 N PHE A 246 97.308 50.758 204.993 1.00 23.03 N ANISOU 3367 N PHE A 246 1633 3414 3702 -1029 -13 -125 N ATOM 3368 CA PHE A 246 97.091 52.194 204.856 1.00 27.78 C ANISOU 3368 CA PHE A 246 2222 3950 4383 -1066 -53 -59 C ATOM 3369 C PHE A 246 98.119 52.829 203.928 1.00 32.22 C ANISOU 3369 C PHE A 246 2730 4549 4962 -1143 26 -35 C ATOM 3370 O PHE A 246 97.795 53.774 203.201 1.00 29.95 O ANISOU 3370 O PHE A 246 2439 4258 4683 -1220 35 -15 O ATOM 3371 CB PHE A 246 97.126 52.875 206.227 1.00 23.89 C ANISOU 3371 CB PHE A 246 1744 3400 3934 -1020 -121 -22 C ATOM 3372 CG PHE A 246 95.971 52.510 207.129 1.00 33.05 C ANISOU 3372 CG PHE A 246 2969 4544 5045 -965 -184 -32 C ATOM 3373 CD1 PHE A 246 95.008 51.594 206.730 1.00 30.02 C ANISOU 3373 CD1 PHE A 246 2614 4166 4627 -949 -188 -66 C ATOM 3374 CD2 PHE A 246 95.848 53.095 208.378 1.00 43.73 C ANISOU 3374 CD2 PHE A 246 4346 5900 6368 -950 -227 -18 C ATOM 3375 CE1 PHE A 246 93.955 51.264 207.562 1.00 30.68 C ANISOU 3375 CE1 PHE A 246 2747 4238 4670 -906 -232 -72 C ATOM 3376 CE2 PHE A 246 94.794 52.771 209.214 1.00 44.53 C ANISOU 3376 CE2 PHE A 246 4491 6009 6418 -916 -255 -47 C ATOM 3377 CZ PHE A 246 93.847 51.854 208.805 1.00 38.00 C ANISOU 3377 CZ PHE A 246 3692 5171 5574 -890 -258 -64 C ATOM 3378 N SER A 247 99.357 52.327 203.939 1.00 32.61 N ANISOU 3378 N SER A 247 2733 4667 4990 -1148 96 -52 N ATOM 3379 CA SER A 247 100.401 52.911 203.103 1.00 33.25 C ANISOU 3379 CA SER A 247 2751 4818 5063 -1243 191 -38 C ATOM 3380 C SER A 247 100.149 52.643 201.624 1.00 35.41 C ANISOU 3380 C SER A 247 3042 5250 5164 -1367 281 -80 C ATOM 3381 O SER A 247 100.361 53.525 200.783 1.00 33.86 O ANISOU 3381 O SER A 247 2834 5114 4919 -1485 324 -17 O ATOM 3382 CB SER A 247 101.769 52.370 203.518 1.00 26.34 C ANISOU 3382 CB SER A 247 1811 3983 4215 -1211 244 -57 C ATOM 3383 OG SER A 247 102.039 52.661 204.878 1.00 30.21 O ANISOU 3383 OG SER A 247 2291 4406 4782 -1152 160 -24 O ATOM 3384 N CYS A 248 99.699 51.432 201.284 1.00 35.43 N ANISOU 3384 N CYS A 248 3072 5335 5054 -1358 308 -178 N ATOM 3385 CA CYS A 248 99.477 51.098 199.881 1.00 46.07 C ANISOU 3385 CA CYS A 248 4435 6867 6203 -1494 391 -230 C ATOM 3386 C CYS A 248 98.233 51.786 199.333 1.00 50.98 C ANISOU 3386 C CYS A 248 5124 7507 6740 -1577 306 -145 C ATOM 3387 O CYS A 248 98.205 52.189 198.164 1.00 54.73 O ANISOU 3387 O CYS A 248 5613 8139 7043 -1735 346 -91 O ATOM 3388 CB CYS A 248 99.370 49.583 199.712 1.00 49.22 C ANISOU 3388 CB CYS A 248 4831 7335 6534 -1461 446 -391 C ATOM 3389 SG CYS A 248 100.886 48.676 200.095 1.00 51.26 S ANISOU 3389 SG CYS A 248 4996 7598 6882 -1387 556 -504 S ATOM 3390 N ASN A 249 97.193 51.928 200.158 1.00 48.06 N ANISOU 3390 N ASN A 249 4794 6988 6479 -1477 184 -119 N ATOM 3391 CA ASN A 249 95.968 52.571 199.693 1.00 45.74 C ANISOU 3391 CA ASN A 249 4553 6696 6131 -1542 90 -40 C ATOM 3392 C ASN A 249 96.194 54.051 199.414 1.00 40.70 C ANISOU 3392 C ASN A 249 3904 6032 5528 -1626 67 98 C ATOM 3393 O ASN A 249 95.724 54.575 198.397 1.00 30.92 O ANISOU 3393 O ASN A 249 2700 4901 4147 -1771 30 211 O ATOM 3394 CB ASN A 249 94.850 52.377 200.718 1.00 47.76 C ANISOU 3394 CB ASN A 249 4839 6785 6523 -1399 -16 -67 C ATOM 3395 CG ASN A 249 94.310 50.959 200.730 1.00 42.97 C ANISOU 3395 CG ASN A 249 4259 6215 5853 -1352 -14 -166 C ATOM 3396 OD1 ASN A 249 94.874 50.063 200.103 1.00 41.01 O ANISOU 3396 OD1 ASN A 249 3995 6101 5484 -1408 76 -253 O ATOM 3397 ND2 ASN A 249 93.214 50.749 201.450 1.00 37.48 N ANISOU 3397 ND2 ASN A 249 3595 5396 5249 -1250 -104 -170 N ATOM 3398 N LEU A 250 96.910 54.741 200.305 1.00 35.59 N ANISOU 3398 N LEU A 250 3211 5244 5067 -1549 77 102 N ATOM 3399 CA LEU A 250 97.197 56.155 200.086 1.00 30.09 C ANISOU 3399 CA LEU A 250 2498 4508 4428 -1630 64 213 C ATOM 3400 C LEU A 250 98.077 56.353 198.859 1.00 42.89 C ANISOU 3400 C LEU A 250 4106 6305 5885 -1798 154 310 C ATOM 3401 O LEU A 250 97.915 57.331 198.120 1.00 49.98 O ANISOU 3401 O LEU A 250 5024 7241 6723 -1928 117 468 O ATOM 3402 CB LEU A 250 97.855 56.754 201.328 1.00 27.01 C ANISOU 3402 CB LEU A 250 2052 3943 4267 -1520 74 148 C ATOM 3403 CG LEU A 250 96.967 56.819 202.572 1.00 27.39 C ANISOU 3403 CG LEU A 250 2112 3836 4459 -1378 2 40 C ATOM 3404 CD1 LEU A 250 97.773 57.233 203.792 1.00 32.65 C ANISOU 3404 CD1 LEU A 250 2758 4386 5262 -1266 20 -42 C ATOM 3405 CD2 LEU A 250 95.807 57.774 202.346 1.00 25.71 C ANISOU 3405 CD2 LEU A 250 1944 3606 4220 -1433 -73 80 C ATOM 3406 N ALA A 251 99.019 55.436 198.628 1.00 46.65 N ANISOU 3406 N ALA A 251 4546 6892 6287 -1799 272 224 N ATOM 3407 CA ALA A 251 99.840 55.509 197.424 1.00 48.09 C ANISOU 3407 CA ALA A 251 4713 7270 6290 -1957 387 280 C ATOM 3408 C ALA A 251 99.008 55.248 196.174 1.00 54.14 C ANISOU 3408 C ALA A 251 5548 8237 6785 -2112 369 340 C ATOM 3409 O ALA A 251 99.217 55.887 195.136 1.00 50.72 O ANISOU 3409 O ALA A 251 5134 7941 6194 -2277 395 484 O ATOM 3410 CB ALA A 251 100.999 54.518 197.517 1.00 37.64 C ANISOU 3410 CB ALA A 251 3323 6013 4964 -1906 525 138 C ATOM 3411 N THR A 252 98.062 54.307 196.254 1.00 58.08 N ANISOU 3411 N THR A 252 6086 8761 7222 -2067 319 239 N ATOM 3412 CA THR A 252 97.218 54.001 195.103 1.00 47.56 C ANISOU 3412 CA THR A 252 4815 7628 5629 -2222 287 281 C ATOM 3413 C THR A 252 96.280 55.158 194.781 1.00 40.56 C ANISOU 3413 C THR A 252 3980 6697 4733 -2309 125 512 C ATOM 3414 O THR A 252 96.014 55.440 193.607 1.00 37.79 O ANISOU 3414 O THR A 252 3673 6533 4152 -2497 100 655 O ATOM 3415 CB THR A 252 96.423 52.719 195.361 1.00 43.74 C ANISOU 3415 CB THR A 252 4347 7150 5121 -2144 265 105 C ATOM 3416 OG1 THR A 252 97.321 51.658 195.711 1.00 46.10 O ANISOU 3416 OG1 THR A 252 4591 7459 5466 -2052 401 -96 O ATOM 3417 CG2 THR A 252 95.635 52.316 194.123 1.00 34.00 C ANISOU 3417 CG2 THR A 252 3165 6147 3605 -2324 241 118 C ATOM 3418 N ILE A 253 95.773 55.841 195.811 1.00 40.74 N ANISOU 3418 N ILE A 253 3997 6478 5003 -2176 11 551 N ATOM 3419 CA ILE A 253 94.883 56.979 195.588 1.00 43.06 C ANISOU 3419 CA ILE A 253 4326 6694 5340 -2235 -151 761 C ATOM 3420 C ILE A 253 95.622 58.092 194.856 1.00 51.80 C ANISOU 3420 C ILE A 253 5428 7854 6399 -2381 -133 968 C ATOM 3421 O ILE A 253 95.110 58.672 193.891 1.00 53.91 O ANISOU 3421 O ILE A 253 5741 8214 6530 -2536 -234 1187 O ATOM 3422 CB ILE A 253 94.297 57.474 196.923 1.00 43.33 C ANISOU 3422 CB ILE A 253 4342 6458 5661 -2047 -237 703 C ATOM 3423 CG1 ILE A 253 93.329 56.441 197.501 1.00 41.26 C ANISOU 3423 CG1 ILE A 253 4100 6153 5426 -1918 -275 543 C ATOM 3424 CG2 ILE A 253 93.604 58.815 196.740 1.00 43.33 C ANISOU 3424 CG2 ILE A 253 4358 6352 5755 -2098 -389 912 C ATOM 3425 CD1 ILE A 253 92.929 56.713 198.935 1.00 34.17 C ANISOU 3425 CD1 ILE A 253 3178 5028 4779 -1725 -302 427 C ATOM 3426 N LYS A 254 96.844 58.399 195.298 1.00 55.57 N ANISOU 3426 N LYS A 254 5849 8272 6994 -2336 -13 913 N ATOM 3427 CA LYS A 254 97.623 59.446 194.646 1.00 57.07 C ANISOU 3427 CA LYS A 254 6027 8497 7159 -2466 18 1100 C ATOM 3428 C LYS A 254 98.010 59.045 193.227 1.00 51.20 C ANISOU 3428 C LYS A 254 5318 8045 6090 -2656 108 1179 C ATOM 3429 O LYS A 254 97.975 59.875 192.312 1.00 55.73 O ANISOU 3429 O LYS A 254 5927 8698 6548 -2810 57 1415 O ATOM 3430 CB LYS A 254 98.867 59.766 195.475 1.00 63.81 C ANISOU 3430 CB LYS A 254 6803 9224 8219 -2374 132 997 C ATOM 3431 CG LYS A 254 99.740 60.869 194.894 1.00 81.93 C ANISOU 3431 CG LYS A 254 9075 11531 10524 -2499 174 1175 C ATOM 3432 CD LYS A 254 98.961 62.162 194.699 1.00 91.27 C ANISOU 3432 CD LYS A 254 10293 12593 11792 -2561 2 1410 C ATOM 3433 CE LYS A 254 98.455 62.714 196.023 1.00 93.50 C ANISOU 3433 CE LYS A 254 10549 12610 12365 -2402 -95 1314 C ATOM 3434 NZ LYS A 254 97.734 64.004 195.843 1.00 97.39 N ANISOU 3434 NZ LYS A 254 11062 12966 12976 -2451 -264 1534 N ATOM 3435 N ALA A 255 98.378 57.778 193.025 1.00 50.79 N ANISOU 3435 N ALA A 255 5256 8156 5885 -2644 244 977 N ATOM 3436 CA ALA A 255 98.727 57.315 191.686 1.00 42.54 C ANISOU 3436 CA ALA A 255 4244 7409 4509 -2819 355 994 C ATOM 3437 C ALA A 255 97.522 57.323 190.755 1.00 54.93 C ANISOU 3437 C ALA A 255 5903 9131 5838 -2967 219 1143 C ATOM 3438 O ALA A 255 97.683 57.445 189.535 1.00 51.67 O ANISOU 3438 O ALA A 255 5539 8952 5142 -3145 258 1259 O ATOM 3439 CB ALA A 255 99.334 55.914 191.755 1.00 41.92 C ANISOU 3439 CB ALA A 255 4124 7445 4357 -2754 529 704 C ATOM 3440 N LEU A 256 96.314 57.197 191.306 1.00 56.01 N ANISOU 3440 N LEU A 256 6061 9140 6081 -2896 55 1144 N ATOM 3441 CA LEU A 256 95.116 57.157 190.475 1.00 58.11 C ANISOU 3441 CA LEU A 256 6401 9538 6141 -3036 -96 1288 C ATOM 3442 C LEU A 256 94.641 58.556 190.101 1.00 56.66 C ANISOU 3442 C LEU A 256 6252 9266 6012 -3123 -282 1628 C ATOM 3443 O LEU A 256 94.204 58.783 188.968 1.00 59.68 O ANISOU 3443 O LEU A 256 6702 9833 6139 -3303 -364 1828 O ATOM 3444 CB LEU A 256 94.011 56.390 191.199 1.00 54.60 C ANISOU 3444 CB LEU A 256 5952 8983 5809 -2917 -198 1137 C ATOM 3445 CG LEU A 256 92.696 56.174 190.452 1.00 56.89 C ANISOU 3445 CG LEU A 256 6300 9395 5918 -3050 -367 1246 C ATOM 3446 CD1 LEU A 256 92.930 55.421 189.153 1.00 57.36 C ANISOU 3446 CD1 LEU A 256 6411 9816 5569 -3256 -249 1201 C ATOM 3447 CD2 LEU A 256 91.722 55.426 191.340 1.00 55.04 C ANISOU 3447 CD2 LEU A 256 6048 9002 5862 -2879 -457 1058 C ATOM 3448 N VAL A 257 94.716 59.505 191.038 1.00 59.13 N ANISOU 3448 N VAL A 257 6518 9292 6656 -2992 -354 1691 N ATOM 3449 CA VAL A 257 94.286 60.867 190.742 1.00 65.67 C ANISOU 3449 CA VAL A 257 7363 9999 7588 -3055 -534 1999 C ATOM 3450 C VAL A 257 95.263 61.546 189.790 1.00 71.67 C ANISOU 3450 C VAL A 257 8137 10898 8195 -3209 -454 2182 C ATOM 3451 O VAL A 257 94.855 62.344 188.936 1.00 76.92 O ANISOU 3451 O VAL A 257 8846 11608 8772 -3342 -597 2469 O ATOM 3452 CB VAL A 257 94.115 61.663 192.050 1.00 62.97 C ANISOU 3452 CB VAL A 257 6962 9315 7650 -2864 -610 1962 C ATOM 3453 CG1 VAL A 257 93.702 63.096 191.759 1.00 69.75 C ANISOU 3453 CG1 VAL A 257 7822 10025 8656 -2919 -795 2265 C ATOM 3454 CG2 VAL A 257 93.089 60.989 192.949 1.00 55.34 C ANISOU 3454 CG2 VAL A 257 5988 8223 6816 -2702 -682 1776 C ATOM 3455 N ASP A 258 96.557 61.238 189.905 1.00 69.83 N ANISOU 3455 N ASP A 258 7863 10732 7937 -3188 -233 2023 N ATOM 3456 CA ASP A 258 97.544 61.838 189.013 1.00 70.95 C ANISOU 3456 CA ASP A 258 8008 11008 7940 -3326 -135 2173 C ATOM 3457 C ASP A 258 97.352 61.369 187.575 1.00 80.21 C ANISOU 3457 C ASP A 258 9263 12516 8697 -3516 -115 2258 C ATOM 3458 O ASP A 258 97.511 62.155 186.634 1.00 82.21 O ANISOU 3458 O ASP A 258 9553 12866 8818 -3660 -160 2507 O ATOM 3459 CB ASP A 258 98.956 61.522 189.503 1.00 69.46 C ANISOU 3459 CB ASP A 258 7743 10809 7840 -3249 98 1961 C ATOM 3460 CG ASP A 258 99.272 62.184 190.830 1.00 73.85 C ANISOU 3460 CG ASP A 258 8223 11049 8787 -3086 74 1902 C ATOM 3461 OD1 ASP A 258 98.366 62.820 191.409 1.00 72.32 O ANISOU 3461 OD1 ASP A 258 8037 10646 8796 -3018 -109 1989 O ATOM 3462 OD2 ASP A 258 100.426 62.068 191.294 1.00 77.47 O ANISOU 3462 OD2 ASP A 258 8611 11470 9354 -3025 236 1757 O ATOM 3463 N ARG A 259 97.015 60.090 187.385 1.00 84.02 N ANISOU 3463 N ARG A 259 9775 13180 8969 -3518 -46 2042 N ATOM 3464 CA ARG A 259 96.716 59.599 186.044 1.00 88.60 C ANISOU 3464 CA ARG A 259 10440 14082 9141 -3691 -37 2083 C ATOM 3465 C ARG A 259 95.442 60.227 185.490 1.00 81.98 C ANISOU 3465 C ARG A 259 9676 13240 8231 -3789 -307 2376 C ATOM 3466 O ARG A 259 95.349 60.478 184.283 1.00 83.30 O ANISOU 3466 O ARG A 259 9911 13621 8117 -3949 -351 2544 O ATOM 3467 CB ARG A 259 96.608 58.072 186.055 1.00 95.94 C ANISOU 3467 CB ARG A 259 11375 15179 9899 -3656 96 1750 C ATOM 3468 CG ARG A 259 96.134 57.468 184.741 1.00111.41 C ANISOU 3468 CG ARG A 259 13429 17461 11441 -3816 91 1739 C ATOM 3469 CD ARG A 259 96.414 55.974 184.667 1.00120.23 C ANISOU 3469 CD ARG A 259 14533 18748 12402 -3776 287 1356 C ATOM 3470 NE ARG A 259 97.833 55.692 184.472 1.00127.98 N ANISOU 3470 NE ARG A 259 15452 19816 13358 -3757 539 1178 N ATOM 3471 CZ ARG A 259 98.323 54.495 184.163 1.00132.32 C ANISOU 3471 CZ ARG A 259 15979 20529 13767 -3735 732 851 C ATOM 3472 NH1 ARG A 259 97.507 53.461 184.010 1.00134.77 N ANISOU 3472 NH1 ARG A 259 16330 20936 13940 -3732 707 654 N ATOM 3473 NH2 ARG A 259 99.629 54.332 184.003 1.00133.61 N ANISOU 3473 NH2 ARG A 259 16074 20745 13945 -3713 947 715 N ATOM 3474 N CYS A 260 94.460 60.499 186.354 1.00 74.36 N ANISOU 3474 N CYS A 260 8692 12027 7535 -3688 -496 2436 N ATOM 3475 CA CYS A 260 93.235 61.150 185.904 1.00 68.41 C ANISOU 3475 CA CYS A 260 7989 11226 6776 -3761 -774 2724 C ATOM 3476 C CYS A 260 93.481 62.598 185.499 1.00 70.50 C ANISOU 3476 C CYS A 260 8245 11385 7157 -3822 -890 3048 C ATOM 3477 O CYS A 260 92.837 63.100 184.572 1.00 70.82 O ANISOU 3477 O CYS A 260 8338 11510 7059 -3945 -1071 3306 O ATOM 3478 CB CYS A 260 92.171 61.080 186.999 1.00 59.33 C ANISOU 3478 CB CYS A 260 6799 9810 5933 -3618 -933 2679 C ATOM 3479 SG CYS A 260 90.625 61.929 186.602 1.00 65.49 S ANISOU 3479 SG CYS A 260 7613 10467 6803 -3673 -1297 3028 S ATOM 3480 N ARG A 261 94.401 63.284 186.177 1.00 65.66 N ANISOU 3480 N ARG A 261 7560 10581 6806 -3737 -794 3034 N ATOM 3481 CA ARG A 261 94.698 64.671 185.843 1.00 65.94 C ANISOU 3481 CA ARG A 261 7576 10499 6978 -3795 -890 3328 C ATOM 3482 C ARG A 261 95.585 64.800 184.613 1.00 71.67 C ANISOU 3482 C ARG A 261 8341 11502 7389 -3971 -762 3435 C ATOM 3483 O ARG A 261 95.638 65.881 184.015 1.00 76.52 O ANISOU 3483 O ARG A 261 8958 12083 8034 -4067 -872 3727 O ATOM 3484 CB ARG A 261 95.358 65.367 187.035 1.00 63.57 C ANISOU 3484 CB ARG A 261 7185 9893 7077 -3643 -831 3254 C ATOM 3485 CG ARG A 261 94.449 65.496 188.246 1.00 63.99 C ANISOU 3485 CG ARG A 261 7193 9644 7476 -3462 -975 3169 C ATOM 3486 CD ARG A 261 95.199 66.042 189.448 1.00 75.42 C ANISOU 3486 CD ARG A 261 8557 10827 9273 -3307 -882 3025 C ATOM 3487 NE ARG A 261 94.340 66.141 190.625 1.00 77.71 N ANISOU 3487 NE ARG A 261 8806 10847 9873 -3123 -998 2903 N ATOM 3488 CZ ARG A 261 94.767 66.483 191.836 1.00 78.98 C ANISOU 3488 CZ ARG A 261 8901 10778 10329 -2963 -931 2720 C ATOM 3489 NH1 ARG A 261 96.049 66.759 192.036 1.00 84.35 N ANISOU 3489 NH1 ARG A 261 9544 11454 11052 -2972 -763 2651 N ATOM 3490 NH2 ARG A 261 93.914 66.545 192.849 1.00 70.65 N ANISOU 3490 NH2 ARG A 261 7817 9508 9520 -2798 -1029 2594 N ATOM 3491 N ALA A 262 96.275 63.728 184.220 1.00 71.27 N ANISOU 3491 N ALA A 262 8313 11717 7050 -4012 -530 3196 N ATOM 3492 CA ALA A 262 97.116 63.777 183.030 1.00 71.55 C ANISOU 3492 CA ALA A 262 8382 12030 6775 -4174 -389 3262 C ATOM 3493 C ALA A 262 96.290 63.699 181.752 1.00 79.60 C ANISOU 3493 C ALA A 262 9494 13294 7455 -4337 -533 3435 C ATOM 3494 O ALA A 262 96.624 64.349 180.755 1.00 87.07 O ANISOU 3494 O ALA A 262 10467 14378 8236 -4485 -544 3657 O ATOM 3495 CB ALA A 262 98.146 62.647 183.069 1.00 67.24 C ANISOU 3495 CB ALA A 262 7811 11666 6072 -4144 -88 2918 C ATOM 3496 N LYS A 263 95.214 62.909 181.758 1.00 77.83 N ANISOU 3496 N LYS A 263 9318 13127 7125 -4315 -645 3336 N ATOM 3497 CA LYS A 263 94.389 62.769 180.564 1.00 85.49 C ANISOU 3497 CA LYS A 263 10376 14327 7780 -4459 -789 3470 C ATOM 3498 C LYS A 263 93.486 63.976 180.343 1.00 88.02 C ANISOU 3498 C LYS A 263 10698 14476 8269 -4501 -1097 3854 C ATOM 3499 O LYS A 263 93.142 64.284 179.196 1.00 91.42 O ANISOU 3499 O LYS A 263 11184 15084 8466 -4650 -1206 4056 O ATOM 3500 CB LYS A 263 93.548 61.490 180.652 1.00 86.48 C ANISOU 3500 CB LYS A 263 10546 14560 7752 -4416 -803 3216 C ATOM 3501 CG LYS A 263 92.642 61.406 181.878 1.00 83.29 C ANISOU 3501 CG LYS A 263 10106 13869 7671 -4261 -953 3181 C ATOM 3502 CD LYS A 263 91.236 61.925 181.591 1.00 86.80 C ANISOU 3502 CD LYS A 263 10584 14219 8178 -4290 -1276 3439 C ATOM 3503 CE LYS A 263 90.417 62.054 182.866 1.00 85.77 C ANISOU 3503 CE LYS A 263 10397 13763 8428 -4131 -1427 3437 C ATOM 3504 NZ LYS A 263 89.089 62.682 182.621 1.00 84.35 N ANISOU 3504 NZ LYS A 263 10224 13449 8375 -4141 -1749 3698 N ATOM 3505 N ALA A 264 93.094 64.660 181.415 1.00 82.60 N ANISOU 3505 N ALA A 264 11039 12060 8287 -2531 447 3929 N ATOM 3506 CA ALA A 264 92.152 65.771 181.330 1.00 85.02 C ANISOU 3506 CA ALA A 264 11258 12236 8809 -2492 199 4276 C ATOM 3507 C ALA A 264 92.706 66.926 180.501 1.00 83.50 C ANISOU 3507 C ALA A 264 11105 12033 8588 -2578 252 4539 C ATOM 3508 O ALA A 264 92.199 67.226 179.421 1.00 86.82 O ANISOU 3508 O ALA A 264 11586 12617 8786 -2701 86 4791 O ATOM 3509 CB ALA A 264 91.783 66.254 182.725 1.00 84.50 C ANISOU 3509 CB ALA A 264 11020 11851 9235 -2296 157 4249 C ATOM 3510 N ALA A 271 83.124 61.975 181.015 1.00 94.69 N ANISOU 3510 N ALA A 271 12162 13897 9920 -2484 -1620 4561 N ATOM 3511 CA ALA A 271 83.129 61.864 182.469 1.00 93.72 C ANISOU 3511 CA ALA A 271 11917 13518 10174 -2284 -1515 4402 C ATOM 3512 C ALA A 271 83.539 60.462 182.911 1.00 89.45 C ANISOU 3512 C ALA A 271 11471 13095 9419 -2292 -1370 4046 C ATOM 3513 O ALA A 271 83.665 60.192 184.104 1.00 85.00 O ANISOU 3513 O ALA A 271 10833 12355 9107 -2148 -1261 3884 O ATOM 3514 CB ALA A 271 81.761 62.220 183.032 1.00 99.06 C ANISOU 3514 CB ALA A 271 12394 13987 11256 -2160 -1746 4553 C ATOM 3515 N GLN A 272 83.742 59.575 181.933 1.00 90.24 N ANISOU 3515 N GLN A 272 11733 13495 9061 -2467 -1365 3915 N ATOM 3516 CA GLN A 272 83.979 58.165 182.236 1.00 87.45 C ANISOU 3516 CA GLN A 272 11458 13269 8501 -2491 -1255 3564 C ATOM 3517 C GLN A 272 85.285 57.967 182.999 1.00 83.31 C ANISOU 3517 C GLN A 272 10962 12669 8022 -2428 -933 3327 C ATOM 3518 O GLN A 272 85.327 57.241 183.999 1.00 78.25 O ANISOU 3518 O GLN A 272 10277 11944 7510 -2333 -849 3113 O ATOM 3519 CB GLN A 272 83.980 57.347 180.944 1.00 92.17 C ANISOU 3519 CB GLN A 272 12216 14192 8613 -2701 -1292 3449 C ATOM 3520 CG GLN A 272 82.649 57.339 180.202 1.00 95.15 C ANISOU 3520 CG GLN A 272 12566 14660 8927 -2777 -1615 3642 C ATOM 3521 CD GLN A 272 81.649 56.350 180.781 1.00 88.57 C ANISOU 3521 CD GLN A 272 11664 13796 8194 -2710 -1759 3490 C ATOM 3522 OE1 GLN A 272 81.525 56.208 181.998 1.00 74.31 O ANISOU 3522 OE1 GLN A 272 9749 11786 6700 -2542 -1715 3411 O ATOM 3523 NE2 GLN A 272 80.930 55.659 179.904 1.00 93.49 N ANISOU 3523 NE2 GLN A 272 12348 14618 8555 -2844 -1929 3445 N ATOM 3524 N TRP A 273 86.366 58.602 182.536 1.00 86.06 N ANISOU 3524 N TRP A 273 11378 13044 8276 -2485 -748 3362 N ATOM 3525 CA TRP A 273 87.671 58.372 183.150 1.00 84.88 C ANISOU 3525 CA TRP A 273 11252 12833 8164 -2442 -432 3117 C ATOM 3526 C TRP A 273 87.712 58.906 184.577 1.00 84.19 C ANISOU 3526 C TRP A 273 11015 12434 8539 -2245 -378 3138 C ATOM 3527 O TRP A 273 88.270 58.259 185.471 1.00 83.07 O ANISOU 3527 O TRP A 273 10849 12226 8489 -2179 -200 2884 O ATOM 3528 CB TRP A 273 88.772 59.009 182.303 1.00 83.92 C ANISOU 3528 CB TRP A 273 11224 12792 7871 -2541 -255 3171 C ATOM 3529 CG TRP A 273 90.150 58.493 182.610 1.00 83.36 C ANISOU 3529 CG TRP A 273 11194 12728 7751 -2541 75 2863 C ATOM 3530 CD1 TRP A 273 90.840 58.635 183.781 1.00 83.97 C ANISOU 3530 CD1 TRP A 273 11177 12585 8141 -2403 255 2739 C ATOM 3531 CD2 TRP A 273 91.009 57.761 181.727 1.00 83.04 C ANISOU 3531 CD2 TRP A 273 11281 12912 7358 -2686 267 2629 C ATOM 3532 NE1 TRP A 273 92.070 58.031 183.683 1.00 82.69 N ANISOU 3532 NE1 TRP A 273 11067 12494 7858 -2447 534 2453 N ATOM 3533 CE2 TRP A 273 92.199 57.488 182.431 1.00 83.94 C ANISOU 3533 CE2 TRP A 273 11358 12917 7619 -2614 555 2376 C ATOM 3534 CE3 TRP A 273 90.887 57.308 180.410 1.00 83.67 C ANISOU 3534 CE3 TRP A 273 11494 13265 7031 -2869 225 2597 C ATOM 3535 CZ2 TRP A 273 93.259 56.783 181.863 1.00 84.88 C ANISOU 3535 CZ2 TRP A 273 11552 13175 7521 -2707 802 2095 C ATOM 3536 CZ3 TRP A 273 91.939 56.609 179.847 1.00 87.41 C ANISOU 3536 CZ3 TRP A 273 12057 13885 7271 -2969 483 2307 C ATOM 3537 CH2 TRP A 273 93.110 56.353 180.573 1.00 89.56 C ANISOU 3537 CH2 TRP A 273 12275 14028 7726 -2882 770 2061 C ATOM 3538 N GLY A 274 87.128 60.082 184.811 1.00 84.91 N ANISOU 3538 N GLY A 274 10995 12326 8943 -2153 -522 3423 N ATOM 3539 CA GLY A 274 87.075 60.622 186.158 1.00 81.37 C ANISOU 3539 CA GLY A 274 10396 11569 8951 -1967 -473 3418 C ATOM 3540 C GLY A 274 86.098 59.898 187.059 1.00 81.29 C ANISOU 3540 C GLY A 274 10296 11475 9115 -1867 -592 3328 C ATOM 3541 O GLY A 274 86.256 59.931 188.284 1.00 78.20 O ANISOU 3541 O GLY A 274 9808 10871 9033 -1730 -487 3208 O ATOM 3542 N ARG A 275 85.088 59.248 186.475 1.00 80.05 N ANISOU 3542 N ARG A 275 10165 11477 8771 -1935 -810 3377 N ATOM 3543 CA ARG A 275 84.113 58.508 187.268 1.00 79.36 C ANISOU 3543 CA ARG A 275 9994 11316 8843 -1844 -933 3298 C ATOM 3544 C ARG A 275 84.748 57.293 187.933 1.00 68.46 C ANISOU 3544 C ARG A 275 8669 10002 7343 -1847 -745 2980 C ATOM 3545 O ARG A 275 84.432 56.973 189.085 1.00 57.34 O ANISOU 3545 O ARG A 275 7148 8397 6240 -1682 -715 2802 O ATOM 3546 CB ARG A 275 82.948 58.080 186.376 1.00 88.61 C ANISOU 3546 CB ARG A 275 11184 12657 9826 -1932 -1211 3406 C ATOM 3547 CG ARG A 275 81.793 57.407 187.094 1.00 91.17 C ANISOU 3547 CG ARG A 275 11404 12892 10346 -1833 -1372 3356 C ATOM 3548 CD ARG A 275 80.926 56.651 186.098 1.00 99.66 C ANISOU 3548 CD ARG A 275 12537 14198 11132 -1959 -1598 3359 C ATOM 3549 NE ARG A 275 79.564 56.443 186.579 1.00108.75 N ANISOU 3549 NE ARG A 275 13540 15216 12565 -1856 -1812 3411 N ATOM 3550 CZ ARG A 275 78.535 57.223 186.264 1.00115.00 C ANISOU 3550 CZ ARG A 275 14208 15900 13586 -1831 -2015 3655 C ATOM 3551 NH1 ARG A 275 78.712 58.264 185.461 1.00114.98 N ANISOU 3551 NH1 ARG A 275 14218 15920 13551 -1905 -2053 3889 N ATOM 3552 NH2 ARG A 275 77.329 56.960 186.746 1.00117.22 N ANISOU 3552 NH2 ARG A 275 14346 16049 14143 -1736 -2171 3661 N ATOM 3553 N ILE A 276 85.649 56.609 187.225 1.00 65.90 N ANISOU 3553 N ILE A 276 8488 9914 6635 -1989 -593 2790 N ATOM 3554 CA ILE A 276 86.275 55.409 187.772 1.00 52.81 C ANISOU 3554 CA ILE A 276 6846 8281 4940 -1944 -399 2365 C ATOM 3555 C ILE A 276 87.211 55.766 188.920 1.00 48.43 C ANISOU 3555 C ILE A 276 6205 7494 4704 -1805 -172 2225 C ATOM 3556 O ILE A 276 87.296 55.042 189.919 1.00 41.21 O ANISOU 3556 O ILE A 276 5219 6461 3977 -1677 -94 1949 O ATOM 3557 CB ILE A 276 87.014 54.645 186.657 1.00 52.50 C ANISOU 3557 CB ILE A 276 6969 8544 4434 -2142 -276 2196 C ATOM 3558 CG1 ILE A 276 86.032 54.195 185.573 1.00 51.96 C ANISOU 3558 CG1 ILE A 276 6991 8723 4030 -2293 -518 2298 C ATOM 3559 CG2 ILE A 276 87.767 53.449 187.227 1.00 47.18 C ANISOU 3559 CG2 ILE A 276 6284 7858 3786 -2085 -57 1754 C ATOM 3560 CD1 ILE A 276 86.669 53.364 184.479 1.00 51.04 C ANISOU 3560 CD1 ILE A 276 7018 8870 3504 -2463 -389 2040 C ATOM 3561 N THR A 277 87.920 56.892 188.802 1.00 50.26 N ANISOU 3561 N THR A 277 6437 7656 5002 -1836 -74 2422 N ATOM 3562 CA THR A 277 88.910 57.259 189.809 1.00 54.09 C ANISOU 3562 CA THR A 277 6847 7940 5763 -1730 141 2282 C ATOM 3563 C THR A 277 88.253 57.599 191.143 1.00 48.47 C ANISOU 3563 C THR A 277 5987 6949 5479 -1538 73 2272 C ATOM 3564 O THR A 277 88.709 57.151 192.202 1.00 43.33 O ANISOU 3564 O THR A 277 5276 6179 5007 -1430 198 2010 O ATOM 3565 CB THR A 277 89.754 58.431 189.309 1.00 58.56 C ANISOU 3565 CB THR A 277 7441 8473 6334 -1786 245 2465 C ATOM 3566 OG1 THR A 277 88.904 59.554 189.041 1.00 70.20 O ANISOU 3566 OG1 THR A 277 8870 9837 7965 -1744 49 2775 O ATOM 3567 CG2 THR A 277 90.492 58.045 188.037 1.00 57.53 C ANISOU 3567 CG2 THR A 277 7456 8601 5800 -1948 347 2396 C ATOM 3568 N THR A 278 87.183 58.396 191.114 1.00 46.08 N ANISOU 3568 N THR A 278 5619 6539 5350 -1500 -123 2557 N ATOM 3569 CA THR A 278 86.517 58.774 192.357 1.00 46.49 C ANISOU 3569 CA THR A 278 5525 6322 5817 -1328 -164 2538 C ATOM 3570 C THR A 278 85.845 57.576 193.016 1.00 48.26 C ANISOU 3570 C THR A 278 5717 6554 6067 -1239 -216 2282 C ATOM 3571 O THR A 278 85.853 57.455 194.247 1.00 54.51 O ANISOU 3571 O THR A 278 6424 7173 7116 -1112 -136 2102 O ATOM 3572 CB THR A 278 85.499 59.884 192.096 1.00 54.06 C ANISOU 3572 CB THR A 278 6401 7152 6987 -1300 -356 2878 C ATOM 3573 OG1 THR A 278 84.622 59.490 191.034 1.00 68.65 O ANISOU 3573 OG1 THR A 278 8303 9193 8589 -1396 -577 3046 O ATOM 3574 CG2 THR A 278 86.205 61.178 191.716 1.00 55.62 C ANISOU 3574 CG2 THR A 278 6601 7274 7260 -1305 -283 3000 C ATOM 3575 N GLU A 279 85.259 56.680 192.217 1.00 48.05 N ANISOU 3575 N GLU A 279 5757 6729 5770 -1316 -349 2262 N ATOM 3576 CA GLU A 279 84.635 55.486 192.780 1.00 51.34 C ANISOU 3576 CA GLU A 279 6140 7153 6214 -1242 -395 2022 C ATOM 3577 C GLU A 279 85.668 54.577 193.435 1.00 44.97 C ANISOU 3577 C GLU A 279 5357 6357 5374 -1209 -186 1677 C ATOM 3578 O GLU A 279 85.407 53.993 194.494 1.00 36.46 O ANISOU 3578 O GLU A 279 4205 5163 4484 -1095 -160 1492 O ATOM 3579 CB GLU A 279 83.868 54.732 191.695 1.00 58.37 C ANISOU 3579 CB GLU A 279 7100 8265 6812 -1352 -580 2064 C ATOM 3580 CG GLU A 279 82.633 55.457 191.188 1.00 72.11 C ANISOU 3580 CG GLU A 279 8784 9980 8633 -1368 -839 2403 C ATOM 3581 CD GLU A 279 82.011 54.772 189.987 1.00 78.73 C ANISOU 3581 CD GLU A 279 9711 11076 9129 -1513 -1034 2457 C ATOM 3582 OE1 GLU A 279 82.552 53.735 189.548 1.00 79.92 O ANISOU 3582 OE1 GLU A 279 9969 11419 8977 -1603 -946 2207 O ATOM 3583 OE2 GLU A 279 80.983 55.270 189.482 1.00 78.39 O ANISOU 3583 OE2 GLU A 279 9620 11037 9128 -1543 -1279 2745 O ATOM 3584 N THR A 280 86.846 54.445 192.821 1.00 45.16 N ANISOU 3584 N THR A 280 5473 6515 5169 -1312 -33 1596 N ATOM 3585 CA THR A 280 87.898 53.631 193.419 1.00 38.47 C ANISOU 3585 CA THR A 280 4625 5659 4332 -1281 163 1287 C ATOM 3586 C THR A 280 88.497 54.305 194.647 1.00 36.39 C ANISOU 3586 C THR A 280 4275 5177 4374 -1170 281 1253 C ATOM 3587 O THR A 280 88.898 53.620 195.595 1.00 33.12 O ANISOU 3587 O THR A 280 3812 4690 4080 -1092 366 1025 O ATOM 3588 CB THR A 280 88.985 53.337 192.386 1.00 40.32 C ANISOU 3588 CB THR A 280 4967 6089 4264 -1428 309 1206 C ATOM 3589 OG1 THR A 280 88.380 52.866 191.175 1.00 51.34 O ANISOU 3589 OG1 THR A 280 6459 7706 5343 -1558 190 1257 O ATOM 3590 CG2 THR A 280 89.947 52.278 192.905 1.00 31.00 C ANISOU 3590 CG2 THR A 280 3765 4903 3112 -1397 488 872 C ATOM 3591 N ALA A 281 88.562 55.639 194.651 1.00 37.57 N ANISOU 3591 N ALA A 281 4399 5219 4658 -1169 280 1481 N ATOM 3592 CA ALA A 281 89.096 56.349 195.809 1.00 39.78 C ANISOU 3592 CA ALA A 281 4596 5290 5230 -1078 387 1438 C ATOM 3593 C ALA A 281 88.192 56.183 197.025 1.00 41.62 C ANISOU 3593 C ALA A 281 4735 5362 5715 -945 316 1362 C ATOM 3594 O ALA A 281 88.681 56.043 198.152 1.00 37.10 O ANISOU 3594 O ALA A 281 4114 4682 5300 -875 414 1185 O ATOM 3595 CB ALA A 281 89.286 57.829 195.476 1.00 30.19 C ANISOU 3595 CB ALA A 281 3366 3980 4125 -1114 398 1702 C ATOM 3596 N ILE A 282 86.873 56.202 196.818 1.00 44.73 N ANISOU 3596 N ILE A 282 5101 5744 6151 -917 147 1497 N ATOM 3597 CA ILE A 282 85.945 55.946 197.917 1.00 49.77 C ANISOU 3597 CA ILE A 282 5649 6245 7017 -801 96 1414 C ATOM 3598 C ILE A 282 86.114 54.522 198.430 1.00 43.27 C ANISOU 3598 C ILE A 282 4841 5496 6103 -773 134 1146 C ATOM 3599 O ILE A 282 86.021 54.262 199.636 1.00 41.10 O ANISOU 3599 O ILE A 282 4508 5110 5997 -689 183 1004 O ATOM 3600 CB ILE A 282 84.497 56.219 197.468 1.00 60.19 C ANISOU 3600 CB ILE A 282 6918 7539 8411 -786 -98 1624 C ATOM 3601 CG1 ILE A 282 84.336 57.670 197.009 1.00 57.53 C ANISOU 3601 CG1 ILE A 282 6545 7098 8218 -807 -143 1916 C ATOM 3602 CG2 ILE A 282 83.516 55.910 198.592 1.00 59.20 C ANISOU 3602 CG2 ILE A 282 6692 7273 8528 -671 -127 1525 C ATOM 3603 CD1 ILE A 282 84.590 58.688 198.093 1.00 53.80 C ANISOU 3603 CD1 ILE A 282 5982 6385 8075 -728 -22 1897 C ATOM 3604 N GLN A 283 86.369 53.578 197.520 1.00 39.78 N ANISOU 3604 N GLN A 283 4476 5243 5395 -853 116 1072 N ATOM 3605 CA GLN A 283 86.574 52.188 197.915 1.00 41.14 C ANISOU 3605 CA GLN A 283 4651 5472 5507 -832 155 822 C ATOM 3606 C GLN A 283 87.793 52.044 198.819 1.00 40.68 C ANISOU 3606 C GLN A 283 4573 5346 5536 -799 319 649 C ATOM 3607 O GLN A 283 87.742 51.360 199.847 1.00 46.46 O ANISOU 3607 O GLN A 283 5256 6011 6386 -728 337 501 O ATOM 3608 CB GLN A 283 86.718 51.310 196.672 1.00 48.93 C ANISOU 3608 CB GLN A 283 5722 6665 6202 -940 129 761 C ATOM 3609 CG GLN A 283 87.084 49.866 196.968 1.00 55.24 C ANISOU 3609 CG GLN A 283 6516 7510 6965 -927 191 492 C ATOM 3610 CD GLN A 283 85.933 49.084 197.563 1.00 58.70 C ANISOU 3610 CD GLN A 283 6891 7892 7518 -854 74 439 C ATOM 3611 OE1 GLN A 283 84.768 49.374 197.293 1.00 72.80 O ANISOU 3611 OE1 GLN A 283 8661 9676 9324 -848 -75 585 O ATOM 3612 NE2 GLN A 283 86.253 48.085 198.376 1.00 58.02 N ANISOU 3612 NE2 GLN A 283 6762 7756 7528 -799 139 241 N ATOM 3613 N LEU A 284 88.902 52.690 198.451 1.00 37.07 N ANISOU 3613 N LEU A 284 4149 4907 5029 -856 432 678 N ATOM 3614 CA LEU A 284 90.132 52.550 199.225 1.00 36.45 C ANISOU 3614 CA LEU A 284 4040 4772 5037 -837 573 519 C ATOM 3615 C LEU A 284 90.028 53.256 200.572 1.00 39.65 C ANISOU 3615 C LEU A 284 4376 5000 5688 -754 584 525 C ATOM 3616 O LEU A 284 90.526 52.748 201.585 1.00 38.63 O ANISOU 3616 O LEU A 284 4207 4820 5649 -712 632 370 O ATOM 3617 CB LEU A 284 91.316 53.086 198.419 1.00 29.40 C ANISOU 3617 CB LEU A 284 3190 3943 4038 -929 697 554 C ATOM 3618 CG LEU A 284 91.645 52.294 197.151 1.00 28.58 C ANISOU 3618 CG LEU A 284 3160 4030 3670 -1031 736 489 C ATOM 3619 CD1 LEU A 284 92.691 53.011 196.317 1.00 31.21 C ANISOU 3619 CD1 LEU A 284 3538 4426 3895 -1135 868 561 C ATOM 3620 CD2 LEU A 284 92.111 50.894 197.509 1.00 23.11 C ANISOU 3620 CD2 LEU A 284 2434 3363 2983 -1008 794 232 C ATOM 3621 N MET A 285 89.388 54.428 200.607 1.00 28.70 N ANISOU 3621 N MET A 285 2970 3516 4418 -737 540 700 N ATOM 3622 CA MET A 285 89.231 55.143 201.868 1.00 21.72 C ANISOU 3622 CA MET A 285 2020 2460 3770 -670 569 679 C ATOM 3623 C MET A 285 88.274 54.425 202.811 1.00 26.90 C ANISOU 3623 C MET A 285 2638 3077 4507 -596 509 585 C ATOM 3624 O MET A 285 88.452 54.482 204.033 1.00 20.09 O ANISOU 3624 O MET A 285 1765 2140 3727 -539 542 457 O ATOM 3625 CB MET A 285 88.749 56.569 201.608 1.00 31.79 C ANISOU 3625 CB MET A 285 3268 3619 5191 -671 548 884 C ATOM 3626 CG MET A 285 89.783 57.457 200.940 1.00 49.16 C ANISOU 3626 CG MET A 285 5502 5825 7351 -737 623 972 C ATOM 3627 SD MET A 285 89.223 59.163 200.793 1.00 61.18 S ANISOU 3627 SD MET A 285 6997 7189 9059 -697 575 1168 S ATOM 3628 CE MET A 285 87.870 58.972 199.638 1.00 57.55 C ANISOU 3628 CE MET A 285 6523 6793 8548 -739 419 1445 C ATOM 3629 N GLY A 286 87.257 53.749 202.269 1.00 26.13 N ANISOU 3629 N GLY A 286 2548 3048 4333 -585 401 628 N ATOM 3630 CA GLY A 286 86.344 52.999 203.114 1.00 18.17 C ANISOU 3630 CA GLY A 286 1496 2003 3404 -521 353 544 C ATOM 3631 C GLY A 286 87.002 51.822 203.804 1.00 17.24 C ANISOU 3631 C GLY A 286 1384 1933 3233 -513 400 352 C ATOM 3632 O GLY A 286 86.650 51.490 204.941 1.00 16.17 O ANISOU 3632 O GLY A 286 1219 1738 3187 -463 406 270 O ATOM 3633 N ILE A 287 87.955 51.173 203.131 1.00 16.97 N ANISOU 3633 N ILE A 287 1390 2006 3051 -563 433 281 N ATOM 3634 CA ILE A 287 88.696 50.079 203.752 1.00 15.97 C ANISOU 3634 CA ILE A 287 1247 1903 2919 -555 475 114 C ATOM 3635 C ILE A 287 89.487 50.585 204.952 1.00 32.69 C ANISOU 3635 C ILE A 287 3377 3946 5097 -514 516 59 C ATOM 3636 O ILE A 287 89.527 49.940 206.008 1.00 23.52 O ANISOU 3636 O ILE A 287 2231 2768 3936 -457 482 -24 O ATOM 3637 CB ILE A 287 89.612 49.402 202.716 1.00 16.61 C ANISOU 3637 CB ILE A 287 1359 2096 2855 -616 520 41 C ATOM 3638 CG1 ILE A 287 88.787 48.862 201.548 1.00 18.57 C ANISOU 3638 CG1 ILE A 287 1647 2450 2959 -651 442 72 C ATOM 3639 CG2 ILE A 287 90.414 48.283 203.360 1.00 15.81 C ANISOU 3639 CG2 ILE A 287 1214 1989 2804 -601 561 -120 C ATOM 3640 CD1 ILE A 287 89.618 48.244 200.448 1.00 18.57 C ANISOU 3640 CD1 ILE A 287 1687 2572 2796 -730 509 -23 C ATOM 3641 N MET A 288 90.127 51.749 204.810 1.00 19.55 N ANISOU 3641 N MET A 288 1732 2247 3451 -535 567 112 N ATOM 3642 CA MET A 288 90.921 52.300 205.904 1.00 27.73 C ANISOU 3642 CA MET A 288 2796 3225 4514 -496 581 48 C ATOM 3643 C MET A 288 90.044 52.700 207.084 1.00 33.52 C ANISOU 3643 C MET A 288 3536 3881 5320 -437 551 36 C ATOM 3644 O MET A 288 90.454 52.564 208.242 1.00 29.11 O ANISOU 3644 O MET A 288 2998 3307 4755 -412 545 -48 O ATOM 3645 CB MET A 288 91.731 53.500 205.410 1.00 38.30 C ANISOU 3645 CB MET A 288 4143 4536 5875 -536 642 106 C ATOM 3646 CG MET A 288 92.651 53.190 204.237 1.00 45.47 C ANISOU 3646 CG MET A 288 5048 5527 6701 -607 703 116 C ATOM 3647 SD MET A 288 93.417 54.665 203.530 1.00 36.79 S ANISOU 3647 SD MET A 288 3961 4395 5624 -664 777 225 S ATOM 3648 CE MET A 288 94.262 55.331 204.962 1.00 35.63 C ANISOU 3648 CE MET A 288 3817 4154 5569 -605 766 123 C ATOM 3649 N LEU A 289 88.833 53.193 206.814 1.00 41.72 N ANISOU 3649 N LEU A 289 4550 4868 6434 -422 536 123 N ATOM 3650 CA LEU A 289 87.963 53.631 207.901 1.00 33.88 C ANISOU 3650 CA LEU A 289 3554 3792 5529 -366 535 95 C ATOM 3651 C LEU A 289 87.469 52.452 208.731 1.00 32.15 C ANISOU 3651 C LEU A 289 3345 3610 5261 -337 500 19 C ATOM 3652 O LEU A 289 87.439 52.526 209.964 1.00 25.57 O ANISOU 3652 O LEU A 289 2533 2750 4433 -320 521 -56 O ATOM 3653 CB LEU A 289 86.784 54.429 207.348 1.00 37.61 C ANISOU 3653 CB LEU A 289 3976 4182 6131 -347 523 219 C ATOM 3654 CG LEU A 289 85.822 54.945 208.420 1.00 45.46 C ANISOU 3654 CG LEU A 289 4949 5075 7250 -287 549 176 C ATOM 3655 CD1 LEU A 289 86.509 55.989 209.286 1.00 50.04 C ANISOU 3655 CD1 LEU A 289 5547 5587 7879 -285 626 94 C ATOM 3656 CD2 LEU A 289 84.550 55.501 207.796 1.00 46.17 C ANISOU 3656 CD2 LEU A 289 4964 5079 7497 -254 515 311 C ATOM 3657 N VAL A 290 87.080 51.356 208.077 1.00 14.14 N ANISOU 3657 N VAL A 290 1046 1393 2933 -343 450 38 N ATOM 3658 CA VAL A 290 86.582 50.197 208.812 1.00 13.45 C ANISOU 3658 CA VAL A 290 967 1332 2812 -314 413 -19 C ATOM 3659 C VAL A 290 87.688 49.587 209.665 1.00 34.17 C ANISOU 3659 C VAL A 290 3627 3994 5360 -322 414 -99 C ATOM 3660 O VAL A 290 87.490 49.298 210.852 1.00 32.02 O ANISOU 3660 O VAL A 290 3372 3713 5080 -310 412 -136 O ATOM 3661 CB VAL A 290 85.983 49.161 207.845 1.00 23.32 C ANISOU 3661 CB VAL A 290 2180 2636 4045 -324 356 8 C ATOM 3662 CG1 VAL A 290 85.582 47.898 208.599 1.00 12.87 C ANISOU 3662 CG1 VAL A 290 867 1329 2695 -293 319 -47 C ATOM 3663 CG2 VAL A 290 84.792 49.751 207.105 1.00 14.44 C ANISOU 3663 CG2 VAL A 290 1000 1472 3015 -323 325 114 C ATOM 3664 N LEU A 291 88.870 49.386 209.075 1.00 20.50 N ANISOU 3664 N LEU A 291 1899 2306 3585 -349 419 -117 N ATOM 3665 CA LEU A 291 89.970 48.760 209.806 1.00 21.76 C ANISOU 3665 CA LEU A 291 2073 2489 3706 -352 404 -173 C ATOM 3666 C LEU A 291 90.388 49.591 211.014 1.00 27.23 C ANISOU 3666 C LEU A 291 2786 3152 4409 -364 425 -199 C ATOM 3667 O LEU A 291 90.629 49.046 212.097 1.00 18.95 O ANISOU 3667 O LEU A 291 1741 2123 3338 -373 396 -224 O ATOM 3668 CB LEU A 291 91.161 48.536 208.874 1.00 17.49 C ANISOU 3668 CB LEU A 291 1518 1981 3146 -377 423 -193 C ATOM 3669 CG LEU A 291 91.120 47.290 207.987 1.00 21.13 C ANISOU 3669 CG LEU A 291 1952 2483 3592 -378 408 -220 C ATOM 3670 CD1 LEU A 291 92.162 47.384 206.882 1.00 15.90 C ANISOU 3670 CD1 LEU A 291 1272 1852 2917 -419 467 -249 C ATOM 3671 CD2 LEU A 291 91.338 46.038 208.825 1.00 12.59 C ANISOU 3671 CD2 LEU A 291 866 1396 2522 -346 357 -254 C ATOM 3672 N SER A 292 90.484 50.912 210.849 1.00 25.69 N ANISOU 3672 N SER A 292 2595 2911 4254 -376 475 -190 N ATOM 3673 CA SER A 292 90.932 51.754 211.953 1.00 30.43 C ANISOU 3673 CA SER A 292 3208 3481 4874 -400 504 -238 C ATOM 3674 C SER A 292 89.877 51.864 213.048 1.00 28.47 C ANISOU 3674 C SER A 292 2967 3208 4642 -397 523 -269 C ATOM 3675 O SER A 292 90.223 52.062 214.217 1.00 26.17 O ANISOU 3675 O SER A 292 2684 2927 4330 -440 537 -330 O ATOM 3676 CB SER A 292 91.310 53.144 211.438 1.00 28.87 C ANISOU 3676 CB SER A 292 3006 3223 4740 -411 559 -225 C ATOM 3677 OG SER A 292 90.229 53.739 210.744 1.00 38.74 O ANISOU 3677 OG SER A 292 4243 4419 6058 -385 584 -162 O ATOM 3678 N VAL A 293 88.596 51.744 212.701 1.00 30.34 N ANISOU 3678 N VAL A 293 3195 3417 4917 -360 529 -233 N ATOM 3679 CA VAL A 293 87.552 51.820 213.719 1.00 29.64 C ANISOU 3679 CA VAL A 293 3106 3299 4857 -358 567 -270 C ATOM 3680 C VAL A 293 87.400 50.484 214.440 1.00 26.40 C ANISOU 3680 C VAL A 293 2702 2959 4369 -374 521 -273 C ATOM 3681 O VAL A 293 87.171 50.443 215.655 1.00 17.29 O ANISOU 3681 O VAL A 293 1557 1821 3191 -417 555 -322 O ATOM 3682 CB VAL A 293 86.227 52.285 213.088 1.00 22.12 C ANISOU 3682 CB VAL A 293 2123 2269 4012 -309 592 -220 C ATOM 3683 CG1 VAL A 293 85.075 52.128 214.067 1.00 15.06 C ANISOU 3683 CG1 VAL A 293 1221 1345 3156 -301 637 -261 C ATOM 3684 CG2 VAL A 293 86.336 53.736 212.647 1.00 23.58 C ANISOU 3684 CG2 VAL A 293 2288 2365 4308 -300 645 -207 C ATOM 3685 N CYS A 294 87.552 49.375 213.715 1.00 15.88 N ANISOU 3685 N CYS A 294 1362 1671 3002 -351 452 -226 N ATOM 3686 CA CYS A 294 87.291 48.063 214.297 1.00 12.47 C ANISOU 3686 CA CYS A 294 923 1286 2528 -356 406 -212 C ATOM 3687 C CYS A 294 88.477 47.537 215.101 1.00 22.31 C ANISOU 3687 C CYS A 294 2168 2588 3720 -408 366 -220 C ATOM 3688 O CYS A 294 88.287 46.944 216.169 1.00 25.78 O ANISOU 3688 O CYS A 294 2601 3064 4131 -452 351 -210 O ATOM 3689 CB CYS A 294 86.914 47.073 213.195 1.00 22.42 C ANISOU 3689 CB CYS A 294 2167 2554 3798 -312 354 -172 C ATOM 3690 SG CYS A 294 85.327 47.418 212.393 1.00 24.19 S ANISOU 3690 SG CYS A 294 2370 2725 4098 -270 368 -138 S ATOM 3691 N TRP A 295 89.703 47.736 214.612 1.00 23.90 N ANISOU 3691 N TRP A 295 2367 2798 3917 -413 345 -228 N ATOM 3692 CA TRP A 295 90.865 47.075 215.195 1.00 12.73 C ANISOU 3692 CA TRP A 295 932 1426 2481 -452 286 -218 C ATOM 3693 C TRP A 295 91.693 47.950 216.131 1.00 18.04 C ANISOU 3693 C TRP A 295 1606 2113 3136 -526 293 -253 C ATOM 3694 O TRP A 295 92.408 47.404 216.979 1.00 13.84 O ANISOU 3694 O TRP A 295 1049 1626 2584 -587 228 -231 O ATOM 3695 CB TRP A 295 91.774 46.536 214.085 1.00 12.54 C ANISOU 3695 CB TRP A 295 888 1395 2482 -413 260 -213 C ATOM 3696 CG TRP A 295 91.374 45.178 213.606 1.00 12.28 C ANISOU 3696 CG TRP A 295 837 1362 2468 -372 224 -191 C ATOM 3697 CD1 TRP A 295 90.699 44.878 212.460 1.00 12.01 C ANISOU 3697 CD1 TRP A 295 806 1310 2447 -330 242 -200 C ATOM 3698 CD2 TRP A 295 91.619 43.929 214.267 1.00 29.47 C ANISOU 3698 CD2 TRP A 295 2982 3552 4664 -379 162 -158 C ATOM 3699 NE1 TRP A 295 90.510 43.520 212.363 1.00 12.01 N ANISOU 3699 NE1 TRP A 295 783 1304 2476 -306 201 -192 N ATOM 3700 CE2 TRP A 295 91.065 42.915 213.460 1.00 20.71 C ANISOU 3700 CE2 TRP A 295 1863 2416 3590 -328 155 -161 C ATOM 3701 CE3 TRP A 295 92.254 43.571 215.461 1.00 21.94 C ANISOU 3701 CE3 TRP A 295 1999 2629 3708 -434 106 -121 C ATOM 3702 CZ2 TRP A 295 91.127 41.567 213.807 1.00 16.83 C ANISOU 3702 CZ2 TRP A 295 1337 1907 3151 -315 104 -132 C ATOM 3703 CZ3 TRP A 295 92.314 42.232 215.804 1.00 19.33 C ANISOU 3703 CZ3 TRP A 295 1630 2291 3425 -425 46 -76 C ATOM 3704 CH2 TRP A 295 91.754 41.246 214.980 1.00 20.78 C ANISOU 3704 CH2 TRP A 295 1807 2427 3662 -358 51 -82 C ATOM 3705 N SER A 296 91.621 49.277 216.010 1.00 22.66 N ANISOU 3705 N SER A 296 2214 2657 3738 -530 363 -304 N ATOM 3706 CA SER A 296 92.471 50.138 216.835 1.00 17.54 C ANISOU 3706 CA SER A 296 1568 2016 3082 -605 373 -358 C ATOM 3707 C SER A 296 92.210 50.002 218.331 1.00 22.22 C ANISOU 3707 C SER A 296 2167 2658 3616 -704 365 -392 C ATOM 3708 O SER A 296 93.188 49.901 219.093 1.00 20.50 O ANISOU 3708 O SER A 296 1933 2487 3368 -788 298 -397 O ATOM 3709 CB SER A 296 92.330 51.595 216.384 1.00 15.98 C ANISOU 3709 CB SER A 296 1390 1747 2937 -586 462 -412 C ATOM 3710 OG SER A 296 92.741 51.756 215.038 1.00 29.49 O ANISOU 3710 OG SER A 296 3091 3427 4688 -527 464 -371 O ATOM 3711 N PRO A 297 90.964 50.008 218.829 1.00 27.12 N ANISOU 3711 N PRO A 297 2810 3277 4218 -715 431 -419 N ATOM 3712 CA PRO A 297 90.785 49.933 220.292 1.00 25.59 C ANISOU 3712 CA PRO A 297 2633 3150 3941 -842 448 -472 C ATOM 3713 C PRO A 297 91.349 48.666 220.913 1.00 25.27 C ANISOU 3713 C PRO A 297 2559 3193 3849 -912 323 -383 C ATOM 3714 O PRO A 297 91.890 48.720 222.023 1.00 25.23 O ANISOU 3714 O PRO A 297 2565 3266 3754 -1047 282 -415 O ATOM 3715 CB PRO A 297 89.261 50.021 220.464 1.00 20.23 C ANISOU 3715 CB PRO A 297 1975 2443 3269 -818 558 -504 C ATOM 3716 CG PRO A 297 88.783 50.712 219.244 1.00 25.47 C ANISOU 3716 CG PRO A 297 2633 3005 4040 -695 604 -500 C ATOM 3717 CD PRO A 297 89.676 50.225 218.143 1.00 26.94 C ANISOU 3717 CD PRO A 297 2797 3192 4247 -630 503 -415 C ATOM 3718 N LEU A 298 91.243 47.525 220.229 1.00 15.76 N ANISOU 3718 N LEU A 298 1315 1978 2695 -832 253 -273 N ATOM 3719 CA LEU A 298 91.719 46.273 220.810 1.00 33.07 C ANISOU 3719 CA LEU A 298 3456 4227 4881 -893 130 -171 C ATOM 3720 C LEU A 298 93.242 46.231 220.874 1.00 29.62 C ANISOU 3720 C LEU A 298 2977 3807 4469 -930 15 -140 C ATOM 3721 O LEU A 298 93.820 45.880 221.910 1.00 22.33 O ANISOU 3721 O LEU A 298 2017 2932 3535 -1036 -84 -108 O ATOM 3722 CB LEU A 298 91.184 45.086 220.010 1.00 27.39 C ANISOU 3722 CB LEU A 298 2710 3485 4210 -795 105 -90 C ATOM 3723 CG LEU A 298 91.753 43.727 220.423 1.00 15.86 C ANISOU 3723 CG LEU A 298 1193 2067 2765 -831 -2 -8 C ATOM 3724 CD1 LEU A 298 91.239 43.321 221.794 1.00 16.97 C ANISOU 3724 CD1 LEU A 298 1317 2258 2874 -953 -15 31 C ATOM 3725 CD2 LEU A 298 91.443 42.662 219.383 1.00 15.06 C ANISOU 3725 CD2 LEU A 298 1079 1903 2741 -692 -8 20 C ATOM 3726 N LEU A 299 93.911 46.584 219.774 1.00 17.97 N ANISOU 3726 N LEU A 299 1502 2285 3040 -839 32 -162 N ATOM 3727 CA LEU A 299 95.369 46.536 219.751 1.00 16.55 C ANISOU 3727 CA LEU A 299 1281 2121 2887 -865 -50 -146 C ATOM 3728 C LEU A 299 95.970 47.531 220.734 1.00 22.19 C ANISOU 3728 C LEU A 299 2001 2857 3574 -981 -88 -193 C ATOM 3729 O LEU A 299 96.943 47.218 221.430 1.00 31.51 O ANISOU 3729 O LEU A 299 3133 4085 4755 -1072 -217 -144 O ATOM 3730 CB LEU A 299 95.882 46.805 218.336 1.00 15.77 C ANISOU 3730 CB LEU A 299 1183 1955 2853 -746 10 -176 C ATOM 3731 CG LEU A 299 95.412 45.854 217.235 1.00 14.90 C ANISOU 3731 CG LEU A 299 1069 1807 2785 -632 39 -156 C ATOM 3732 CD1 LEU A 299 95.838 46.366 215.869 1.00 14.43 C ANISOU 3732 CD1 LEU A 299 1020 1693 2771 -554 108 -199 C ATOM 3733 CD2 LEU A 299 95.953 44.454 217.476 1.00 15.37 C ANISOU 3733 CD2 LEU A 299 1069 1873 2897 -622 -44 -99 C ATOM 3734 N ILE A 300 95.403 48.736 220.807 1.00 17.67 N ANISOU 3734 N ILE A 300 1490 2256 2968 -984 29 -307 N ATOM 3735 CA ILE A 300 95.921 49.747 221.723 1.00 18.93 C ANISOU 3735 CA ILE A 300 1676 2445 3070 -1096 28 -408 C ATOM 3736 C ILE A 300 95.673 49.339 223.171 1.00 43.61 C ANISOU 3736 C ILE A 300 4828 5688 6054 -1248 -32 -423 C ATOM 3737 O ILE A 300 96.545 49.503 224.034 1.00 36.10 O ANISOU 3737 O ILE A 300 3876 4808 5034 -1362 -137 -440 O ATOM 3738 CB ILE A 300 95.303 51.121 221.402 1.00 29.05 C ANISOU 3738 CB ILE A 300 3018 3670 4351 -1064 191 -536 C ATOM 3739 CG1 ILE A 300 95.838 51.648 220.068 1.00 23.33 C ANISOU 3739 CG1 ILE A 300 2271 2858 3734 -949 227 -514 C ATOM 3740 CG2 ILE A 300 95.581 52.114 222.519 1.00 20.31 C ANISOU 3740 CG2 ILE A 300 1954 2606 3158 -1199 216 -671 C ATOM 3741 CD1 ILE A 300 95.188 52.940 219.617 1.00 22.41 C ANISOU 3741 CD1 ILE A 300 2192 2665 3658 -904 370 -603 C ATOM 3742 N MET A 301 94.488 48.793 223.461 1.00 44.46 N ANISOU 3742 N MET A 301 4969 5836 6087 -1265 28 -407 N ATOM 3743 CA MET A 301 94.157 48.439 224.838 1.00 42.62 C ANISOU 3743 CA MET A 301 4792 5752 5651 -1440 -11 -405 C ATOM 3744 C MET A 301 95.035 47.307 225.358 1.00 38.92 C ANISOU 3744 C MET A 301 4268 5359 5160 -1493 -225 -239 C ATOM 3745 O MET A 301 95.377 47.289 226.546 1.00 27.24 O ANISOU 3745 O MET A 301 2839 4020 3490 -1659 -326 -218 O ATOM 3746 CB MET A 301 92.680 48.060 224.942 1.00 40.45 C ANISOU 3746 CB MET A 301 4554 5491 5324 -1439 115 -404 C ATOM 3747 CG MET A 301 92.122 48.098 226.352 1.00 51.07 C ANISOU 3747 CG MET A 301 5998 6986 6420 -1620 151 -444 C ATOM 3748 SD MET A 301 90.356 47.738 226.396 1.00 63.51 S ANISOU 3748 SD MET A 301 7612 8540 7978 -1568 332 -443 S ATOM 3749 CE MET A 301 89.715 49.056 225.365 1.00 58.81 C ANISOU 3749 CE MET A 301 6993 7775 7577 -1453 538 -624 C ATOM 3750 N MET A 302 95.403 46.357 224.494 1.00 40.07 N ANISOU 3750 N MET A 302 4314 5411 5500 -1352 -295 -122 N ATOM 3751 CA MET A 302 96.337 45.313 224.904 1.00 31.99 C ANISOU 3751 CA MET A 302 3223 4419 4513 -1361 -484 29 C ATOM 3752 C MET A 302 97.698 45.903 225.248 1.00 36.02 C ANISOU 3752 C MET A 302 3709 4947 5032 -1410 -586 -8 C ATOM 3753 O MET A 302 98.326 45.504 226.235 1.00 41.96 O ANISOU 3753 O MET A 302 4461 5796 5686 -1512 -753 99 O ATOM 3754 CB MET A 302 96.476 44.262 223.801 1.00 34.59 C ANISOU 3754 CB MET A 302 3462 4630 5052 -1185 -475 90 C ATOM 3755 CG MET A 302 95.220 43.444 223.549 1.00 44.22 C ANISOU 3755 CG MET A 302 4695 5829 6279 -1132 -413 151 C ATOM 3756 SD MET A 302 95.491 42.108 222.366 1.00 37.67 S ANISOU 3756 SD MET A 302 3794 4885 5635 -947 -416 208 S ATOM 3757 CE MET A 302 96.555 41.023 223.314 1.00 28.49 C ANISOU 3757 CE MET A 302 2564 3736 4525 -986 -630 402 C ATOM 3758 N LEU A 303 98.164 46.864 224.447 1.00 46.54 N ANISOU 3758 N LEU A 303 5015 6183 6486 -1342 -494 -142 N ATOM 3759 CA LEU A 303 99.446 47.507 224.720 1.00 23.88 C ANISOU 3759 CA LEU A 303 2109 3315 3650 -1385 -575 -192 C ATOM 3760 C LEU A 303 99.423 48.255 226.047 1.00 25.69 C ANISOU 3760 C LEU A 303 2441 3681 3638 -1571 -632 -242 C ATOM 3761 O LEU A 303 100.428 48.286 226.767 1.00 39.44 O ANISOU 3761 O LEU A 303 4161 5487 5339 -1651 -781 -212 O ATOM 3762 CB LEU A 303 99.805 48.456 223.576 1.00 22.75 C ANISOU 3762 CB LEU A 303 1925 3025 3693 -1284 -462 -295 C ATOM 3763 CG LEU A 303 100.097 47.808 222.220 1.00 21.40 C ANISOU 3763 CG LEU A 303 1742 2895 3495 -1199 -354 -255 C ATOM 3764 CD1 LEU A 303 100.243 48.868 221.140 1.00 20.48 C ANISOU 3764 CD1 LEU A 303 1668 2676 3439 -1137 -293 -226 C ATOM 3765 CD2 LEU A 303 101.345 46.944 222.298 1.00 22.37 C ANISOU 3765 CD2 LEU A 303 1755 3003 3741 -1163 -475 -188 C ATOM 3766 N LYS A 304 98.287 48.869 226.388 1.00 39.38 N ANISOU 3766 N LYS A 304 4290 5471 5201 -1645 -495 -343 N ATOM 3767 CA LYS A 304 98.194 49.595 227.652 1.00 43.67 C ANISOU 3767 CA LYS A 304 4946 6160 5487 -1835 -499 -447 C ATOM 3768 C LYS A 304 98.252 48.656 228.850 1.00 42.68 C ANISOU 3768 C LYS A 304 4859 6212 5144 -1984 -673 -297 C ATOM 3769 O LYS A 304 98.782 49.028 229.903 1.00 46.87 O ANISOU 3769 O LYS A 304 5453 6872 5485 -2137 -770 -326 O ATOM 3770 CB LYS A 304 96.912 50.428 227.694 1.00 39.13 C ANISOU 3770 CB LYS A 304 4471 5584 4812 -1867 -266 -622 C ATOM 3771 CG LYS A 304 96.931 51.645 226.781 1.00 45.15 C ANISOU 3771 CG LYS A 304 5217 6188 5751 -1751 -108 -765 C ATOM 3772 CD LYS A 304 95.731 52.547 227.035 1.00 57.89 C ANISOU 3772 CD LYS A 304 6919 7792 7284 -1788 118 -946 C ATOM 3773 CE LYS A 304 95.810 53.820 226.205 1.00 63.30 C ANISOU 3773 CE LYS A 304 7581 8317 8152 -1675 255 -1058 C ATOM 3774 NZ LYS A 304 94.651 54.725 226.448 1.00 64.62 N ANISOU 3774 NZ LYS A 304 7808 8446 8297 -1693 479 -1231 N ATOM 3775 N MET A 305 97.717 47.443 228.713 1.00 42.78 N ANISOU 3775 N MET A 305 4839 6234 5181 -1942 -719 -124 N ATOM 3776 CA MET A 305 97.695 46.508 229.831 1.00 50.63 C ANISOU 3776 CA MET A 305 5872 7391 5975 -2084 -889 62 C ATOM 3777 C MET A 305 99.009 45.750 229.975 1.00 49.63 C ANISOU 3777 C MET A 305 5642 7240 5974 -2041 -1125 254 C ATOM 3778 O MET A 305 99.381 45.375 231.093 1.00 44.07 O ANISOU 3778 O MET A 305 4981 6681 5081 -2188 -1296 390 O ATOM 3779 CB MET A 305 96.530 45.531 229.669 1.00 54.87 C ANISOU 3779 CB MET A 305 6407 7933 6508 -2062 -835 180 C ATOM 3780 CG MET A 305 95.165 46.186 229.804 1.00 57.14 C ANISOU 3780 CG MET A 305 6807 8260 6645 -2120 -593 3 C ATOM 3781 SD MET A 305 93.805 45.019 229.623 1.00 80.56 S ANISOU 3781 SD MET A 305 9775 11192 9642 -2024 -500 151 S ATOM 3782 CE MET A 305 94.005 44.535 227.910 1.00 69.93 C ANISOU 3782 CE MET A 305 8266 9615 8691 -1774 -492 190 C ATOM 3783 N ILE A 306 99.716 45.509 228.868 1.00 50.80 N ANISOU 3783 N ILE A 306 5658 7209 6436 -1848 -1123 264 N ATOM 3784 CA ILE A 306 101.017 44.851 228.944 1.00 42.41 C ANISOU 3784 CA ILE A 306 4485 6100 5528 -1798 -1307 410 C ATOM 3785 C ILE A 306 102.012 45.720 229.702 1.00 36.99 C ANISOU 3785 C ILE A 306 3822 5495 4739 -1918 -1411 340 C ATOM 3786 O ILE A 306 102.755 45.234 230.564 1.00 37.86 O ANISOU 3786 O ILE A 306 3915 5683 4788 -2003 -1613 500 O ATOM 3787 CB ILE A 306 101.527 44.509 227.531 1.00 39.58 C ANISOU 3787 CB ILE A 306 3995 5545 5498 -1580 -1222 376 C ATOM 3788 CG1 ILE A 306 100.628 43.459 226.878 1.00 30.88 C ANISOU 3788 CG1 ILE A 306 2873 4367 4494 -1464 -1148 462 C ATOM 3789 CG2 ILE A 306 102.969 44.028 227.583 1.00 39.97 C ANISOU 3789 CG2 ILE A 306 3931 5541 5713 -1540 -1373 479 C ATOM 3790 CD1 ILE A 306 100.862 43.299 225.394 1.00 26.29 C ANISOU 3790 CD1 ILE A 306 2213 3627 4151 -1274 -1004 369 C ATOM 3791 N PHE A 307 102.036 47.015 229.405 1.00 37.46 N ANISOU 3791 N PHE A 307 3915 5528 4788 -1928 -1279 111 N ATOM 3792 CA PHE A 307 102.944 47.939 230.073 1.00 48.08 C ANISOU 3792 CA PHE A 307 5279 6933 6055 -2038 -1360 13 C ATOM 3793 C PHE A 307 102.205 48.786 231.105 1.00 57.18 C ANISOU 3793 C PHE A 307 6604 8249 6871 -2230 -1298 -120 C ATOM 3794 O PHE A 307 101.623 48.260 232.053 1.00 65.77 O ANISOU 3794 O PHE A 307 7791 9500 7698 -2368 -1358 -18 O ATOM 3795 CB PHE A 307 103.636 48.841 229.049 1.00 50.88 C ANISOU 3795 CB PHE A 307 5540 7128 6663 -1920 -1253 -156 C ATOM 3796 CG PHE A 307 104.211 48.095 227.878 1.00 52.64 C ANISOU 3796 CG PHE A 307 5612 7205 7184 -1735 -1228 -85 C ATOM 3797 CD1 PHE A 307 105.347 47.315 228.026 1.00 55.86 C ANISOU 3797 CD1 PHE A 307 5911 7603 7709 -1710 -1387 58 C ATOM 3798 CD2 PHE A 307 103.613 48.169 226.631 1.00 47.02 C ANISOU 3798 CD2 PHE A 307 4879 6374 6615 -1597 -1032 -164 C ATOM 3799 CE1 PHE A 307 105.876 46.625 226.950 1.00 55.13 C ANISOU 3799 CE1 PHE A 307 5703 7388 7857 -1554 -1330 107 C ATOM 3800 CE2 PHE A 307 104.136 47.481 225.552 1.00 45.67 C ANISOU 3800 CE2 PHE A 307 4601 6109 6641 -1456 -976 -118 C ATOM 3801 CZ PHE A 307 105.270 46.709 225.712 1.00 52.62 C ANISOU 3801 CZ PHE A 307 5387 6980 7625 -1434 -1119 14 C ATOM 3802 N LYS A 323 86.413 48.748 235.115 1.00 72.64 N ANISOU 3802 N LYS A 323 9586 10785 7230 -2833 1153 -1014 N ATOM 3803 CA LYS A 323 86.102 49.107 233.736 1.00 71.87 C ANISOU 3803 CA LYS A 323 9347 10419 7540 -2580 1217 -1058 C ATOM 3804 C LYS A 323 87.074 48.449 232.763 1.00 74.36 C ANISOU 3804 C LYS A 323 9559 10649 8046 -2427 936 -834 C ATOM 3805 O LYS A 323 86.814 48.385 231.561 1.00 69.56 O ANISOU 3805 O LYS A 323 8836 9847 7746 -2219 947 -796 O ATOM 3806 CB LYS A 323 86.136 50.625 233.555 1.00 70.36 C ANISOU 3806 CB LYS A 323 9155 10119 7462 -2580 1396 -1376 C ATOM 3807 CG LYS A 323 85.277 51.392 234.545 1.00 76.18 C ANISOU 3807 CG LYS A 323 9978 10901 8068 -2723 1664 -1635 C ATOM 3808 CD LYS A 323 85.204 52.864 234.174 1.00 74.12 C ANISOU 3808 CD LYS A 323 9661 10440 8063 -2663 1814 -1906 C ATOM 3809 CE LYS A 323 86.594 53.466 234.039 1.00 68.81 C ANISOU 3809 CE LYS A 323 9002 9810 7333 -2725 1675 -1977 C ATOM 3810 NZ LYS A 323 87.399 53.295 235.279 1.00 70.61 N ANISOU 3810 NZ LYS A 323 9344 10285 7201 -2953 1529 -1953 N ATOM 3811 N GLU A 324 88.201 47.967 233.293 1.00 76.20 N ANISOU 3811 N GLU A 324 9828 11030 8094 -2541 685 -689 N ATOM 3812 CA GLU A 324 89.202 47.327 232.445 1.00 70.12 C ANISOU 3812 CA GLU A 324 8946 10176 7519 -2410 427 -489 C ATOM 3813 C GLU A 324 88.649 46.066 231.795 1.00 66.55 C ANISOU 3813 C GLU A 324 8403 9634 7248 -2258 377 -257 C ATOM 3814 O GLU A 324 88.904 45.803 230.614 1.00 62.60 O ANISOU 3814 O GLU A 324 7785 8969 7029 -2073 310 -194 O ATOM 3815 N CYS A 325 87.888 45.273 232.552 1.00 72.70 N ANISOU 3815 N CYS A 325 9235 10521 7865 -2346 417 -133 N ATOM 3816 CA CYS A 325 87.245 44.095 231.980 1.00 65.74 C ANISOU 3816 CA CYS A 325 8264 9542 7170 -2211 392 69 C ATOM 3817 C CYS A 325 86.139 44.475 231.003 1.00 63.75 C ANISOU 3817 C CYS A 325 7947 9106 7170 -2039 607 -67 C ATOM 3818 O CYS A 325 85.915 43.765 230.016 1.00 54.19 O ANISOU 3818 O CYS A 325 6627 7755 6210 -1872 553 45 O ATOM 3819 CB CYS A 325 86.684 43.213 233.095 1.00 57.79 C ANISOU 3819 CB CYS A 325 7332 8698 5926 -2364 394 240 C ATOM 3820 SG CYS A 325 87.931 42.476 234.175 1.00 60.03 S ANISOU 3820 SG CYS A 325 7669 9195 5943 -2561 79 499 S ATOM 3821 N ASN A 326 85.444 45.586 231.257 1.00 64.38 N ANISOU 3821 N ASN A 326 8084 9179 7200 -2081 847 -310 N ATOM 3822 CA ASN A 326 84.307 45.964 230.423 1.00 62.01 C ANISOU 3822 CA ASN A 326 7709 8702 7148 -1931 1046 -420 C ATOM 3823 C ASN A 326 84.759 46.438 229.046 1.00 48.94 C ANISOU 3823 C ASN A 326 5956 6869 5771 -1748 982 -462 C ATOM 3824 O ASN A 326 84.248 45.972 228.021 1.00 44.76 O ANISOU 3824 O ASN A 326 5328 6204 5474 -1587 971 -386 O ATOM 3825 CB ASN A 326 83.486 47.046 231.124 1.00 64.62 C ANISOU 3825 CB ASN A 326 8110 9058 7384 -2033 1326 -672 C ATOM 3826 CG ASN A 326 82.329 47.539 230.279 1.00 71.12 C ANISOU 3826 CG ASN A 326 8855 9655 8514 -1815 1460 -773 C ATOM 3827 OD1 ASN A 326 81.705 46.768 229.549 1.00 66.45 O ANISOU 3827 OD1 ASN A 326 8179 8961 8109 -1661 1409 -631 O ATOM 3828 ND2 ASN A 326 82.038 48.831 230.370 1.00 81.61 N ANISOU 3828 ND2 ASN A 326 10203 10899 9905 -1810 1616 -1011 N ATOM 3829 N PHE A 327 85.714 47.371 229.003 1.00 45.40 N ANISOU 3829 N PHE A 327 5533 6424 5294 -1782 941 -584 N ATOM 3830 CA PHE A 327 86.147 47.928 227.725 1.00 44.50 C ANISOU 3830 CA PHE A 327 5333 6149 5427 -1627 904 -625 C ATOM 3831 C PHE A 327 86.827 46.885 226.848 1.00 34.44 C ANISOU 3831 C PHE A 327 3975 4832 4277 -1514 692 -426 C ATOM 3832 O PHE A 327 86.772 46.984 225.616 1.00 33.87 O ANISOU 3832 O PHE A 327 3822 4622 4423 -1364 687 -421 O ATOM 3833 CB PHE A 327 87.082 49.115 227.954 1.00 49.72 C ANISOU 3833 CB PHE A 327 6035 6825 6031 -1705 905 -791 C ATOM 3834 CG PHE A 327 86.367 50.405 228.235 1.00 55.92 C ANISOU 3834 CG PHE A 327 6851 7549 6848 -1744 1147 -1033 C ATOM 3835 CD1 PHE A 327 85.935 51.212 227.195 1.00 58.41 C ANISOU 3835 CD1 PHE A 327 7091 7670 7432 -1589 1243 -1108 C ATOM 3836 CD2 PHE A 327 86.131 50.814 229.537 1.00 62.12 C ANISOU 3836 CD2 PHE A 327 7740 8465 7397 -1930 1272 -1183 C ATOM 3837 CE1 PHE A 327 85.277 52.400 227.448 1.00 65.97 C ANISOU 3837 CE1 PHE A 327 8066 8536 8462 -1592 1444 -1317 C ATOM 3838 CE2 PHE A 327 85.474 52.003 229.797 1.00 63.91 C ANISOU 3838 CE2 PHE A 327 7979 8615 7687 -1967 1517 -1432 C ATOM 3839 CZ PHE A 327 85.046 52.796 228.751 1.00 66.53 C ANISOU 3839 CZ PHE A 327 8220 8723 8336 -1794 1602 -1497 C ATOM 3840 N PHE A 328 87.474 45.886 227.453 1.00 25.18 N ANISOU 3840 N PHE A 328 2816 3773 2977 -1591 519 -261 N ATOM 3841 CA PHE A 328 88.148 44.865 226.658 1.00 31.71 C ANISOU 3841 CA PHE A 328 3548 4541 3961 -1487 332 -88 C ATOM 3842 C PHE A 328 87.151 43.979 225.922 1.00 30.65 C ANISOU 3842 C PHE A 328 3342 4308 3996 -1360 371 0 C ATOM 3843 O PHE A 328 87.461 43.465 224.841 1.00 35.78 O ANISOU 3843 O PHE A 328 3900 4855 4838 -1235 289 58 O ATOM 3844 CB PHE A 328 89.063 44.028 227.552 1.00 42.52 C ANISOU 3844 CB PHE A 328 4929 6038 5187 -1605 130 82 C ATOM 3845 CG PHE A 328 90.113 43.262 226.798 1.00 30.39 C ANISOU 3845 CG PHE A 328 3279 4428 3841 -1515 -63 215 C ATOM 3846 CD1 PHE A 328 91.019 43.923 225.987 1.00 21.78 C ANISOU 3846 CD1 PHE A 328 2137 3261 2876 -1449 -93 122 C ATOM 3847 CD2 PHE A 328 90.205 41.884 226.913 1.00 30.76 C ANISOU 3847 CD2 PHE A 328 3258 4470 3958 -1501 -203 429 C ATOM 3848 CE1 PHE A 328 91.988 43.225 225.295 1.00 37.56 C ANISOU 3848 CE1 PHE A 328 4022 5187 5063 -1372 -243 224 C ATOM 3849 CE2 PHE A 328 91.174 41.180 226.224 1.00 23.84 C ANISOU 3849 CE2 PHE A 328 2260 3506 3293 -1418 -361 530 C ATOM 3850 CZ PHE A 328 92.066 41.852 225.414 1.00 27.02 C ANISOU 3850 CZ PHE A 328 2623 3834 3810 -1337 -368 413 C ATOM 3851 N LEU A 329 85.954 43.791 226.485 1.00 27.13 N ANISOU 3851 N LEU A 329 2933 3892 3485 -1399 503 0 N ATOM 3852 CA LEU A 329 84.914 43.050 225.780 1.00 25.53 C ANISOU 3852 CA LEU A 329 2654 3586 3459 -1284 549 64 C ATOM 3853 C LEU A 329 84.378 43.847 224.597 1.00 27.79 C ANISOU 3853 C LEU A 329 2901 3729 3930 -1125 636 -59 C ATOM 3854 O LEU A 329 84.119 43.283 223.527 1.00 27.45 O ANISOU 3854 O LEU A 329 2790 3589 4051 -981 568 3 O ATOM 3855 CB LEU A 329 83.784 42.683 226.741 1.00 30.57 C ANISOU 3855 CB LEU A 329 3335 4291 3988 -1371 675 98 C ATOM 3856 CG LEU A 329 82.568 41.986 226.127 1.00 28.72 C ANISOU 3856 CG LEU A 329 3025 3943 3946 -1245 728 153 C ATOM 3857 CD1 LEU A 329 82.973 40.672 225.477 1.00 20.58 C ANISOU 3857 CD1 LEU A 329 1900 2856 3064 -1179 557 322 C ATOM 3858 CD2 LEU A 329 81.501 41.755 227.183 1.00 23.08 C ANISOU 3858 CD2 LEU A 329 2359 3294 3115 -1328 866 173 C ATOM 3859 N ILE A 330 84.199 45.158 224.772 1.00 28.80 N ANISOU 3859 N ILE A 330 3083 3845 4015 -1137 760 -221 N ATOM 3860 CA ILE A 330 83.766 46.003 223.662 1.00 18.65 C ANISOU 3860 CA ILE A 330 1774 2424 2887 -976 798 -300 C ATOM 3861 C ILE A 330 84.803 45.983 222.547 1.00 31.30 C ANISOU 3861 C ILE A 330 3341 3980 4570 -888 659 -258 C ATOM 3862 O ILE A 330 84.461 45.989 221.358 1.00 21.74 O ANISOU 3862 O ILE A 330 2104 2685 3472 -749 623 -236 O ATOM 3863 CB ILE A 330 83.492 47.437 224.156 1.00 23.26 C ANISOU 3863 CB ILE A 330 2413 2988 3438 -1021 956 -480 C ATOM 3864 CG1 ILE A 330 82.389 47.438 225.219 1.00 23.01 C ANISOU 3864 CG1 ILE A 330 2419 2996 3329 -1100 1113 -540 C ATOM 3865 CG2 ILE A 330 83.130 48.348 222.995 1.00 22.18 C ANISOU 3865 CG2 ILE A 330 2247 2705 3476 -868 972 -530 C ATOM 3866 CD1 ILE A 330 82.084 48.813 225.781 1.00 22.53 C ANISOU 3866 CD1 ILE A 330 2407 2900 3254 -1155 1287 -747 C ATOM 3867 N ALA A 331 86.087 45.938 222.914 1.00 26.86 N ANISOU 3867 N ALA A 331 2785 3486 3935 -979 576 -249 N ATOM 3868 CA ALA A 331 87.150 45.971 221.915 1.00 16.58 C ANISOU 3868 CA ALA A 331 1450 2139 2711 -897 461 -220 C ATOM 3869 C ALA A 331 87.167 44.702 221.070 1.00 15.66 C ANISOU 3869 C ALA A 331 1276 1993 2680 -803 349 -97 C ATOM 3870 O ALA A 331 87.288 44.771 219.842 1.00 19.11 O ANISOU 3870 O ALA A 331 1712 2373 3177 -686 321 -104 O ATOM 3871 CB ALA A 331 88.501 46.181 222.596 1.00 37.84 C ANISOU 3871 CB ALA A 331 4151 4906 5319 -1020 386 -238 C ATOM 3872 N VAL A 332 87.048 43.533 221.704 1.00 16.18 N ANISOU 3872 N VAL A 332 1305 2104 2739 -866 294 6 N ATOM 3873 CA VAL A 332 87.051 42.290 220.941 1.00 26.20 C ANISOU 3873 CA VAL A 332 2536 3341 4078 -777 206 78 C ATOM 3874 C VAL A 332 85.788 42.150 220.101 1.00 32.05 C ANISOU 3874 C VAL A 332 3289 4018 4871 -660 260 55 C ATOM 3875 O VAL A 332 85.802 41.452 219.080 1.00 34.56 O ANISOU 3875 O VAL A 332 3595 4285 5251 -557 207 61 O ATOM 3876 CB VAL A 332 87.230 41.075 221.873 1.00 26.12 C ANISOU 3876 CB VAL A 332 2485 3364 4075 -853 136 190 C ATOM 3877 CG1 VAL A 332 85.933 40.743 222.595 1.00 17.19 C ANISOU 3877 CG1 VAL A 332 1361 2252 2916 -907 220 240 C ATOM 3878 CG2 VAL A 332 87.736 39.877 221.087 1.00 31.25 C ANISOU 3878 CG2 VAL A 332 3099 3948 4828 -733 30 242 C ATOM 3879 N ARG A 333 84.694 42.807 220.495 1.00 30.98 N ANISOU 3879 N ARG A 333 3175 3875 4719 -674 368 17 N ATOM 3880 CA ARG A 333 83.501 42.818 219.660 1.00 20.61 C ANISOU 3880 CA ARG A 333 1864 2493 3475 -566 404 -7 C ATOM 3881 C ARG A 333 83.638 43.787 218.492 1.00 32.93 C ANISOU 3881 C ARG A 333 3446 3995 5072 -479 409 -73 C ATOM 3882 O ARG A 333 83.068 43.545 217.422 1.00 13.29 O ANISOU 3882 O ARG A 333 949 1455 2645 -394 381 -69 O ATOM 3883 CB ARG A 333 82.270 43.164 220.499 1.00 21.09 C ANISOU 3883 CB ARG A 333 1930 2553 3530 -604 523 -28 C ATOM 3884 CG ARG A 333 81.774 42.015 221.365 1.00 31.14 C ANISOU 3884 CG ARG A 333 3177 3870 4784 -672 525 62 C ATOM 3885 CD ARG A 333 80.262 42.060 221.527 1.00 29.05 C ANISOU 3885 CD ARG A 333 2904 3564 4569 -640 621 43 C ATOM 3886 NE ARG A 333 79.849 42.737 222.752 1.00 28.94 N ANISOU 3886 NE ARG A 333 2921 3597 4477 -739 769 -5 N ATOM 3887 CZ ARG A 333 79.338 42.116 223.811 1.00 36.51 C ANISOU 3887 CZ ARG A 333 3880 4617 5374 -833 836 56 C ATOM 3888 NH1 ARG A 333 79.170 40.800 223.795 1.00 33.58 N ANISOU 3888 NH1 ARG A 333 3467 4256 5036 -840 756 182 N ATOM 3889 NH2 ARG A 333 78.987 42.812 224.884 1.00 44.67 N ANISOU 3889 NH2 ARG A 333 4966 5700 6305 -926 992 -22 N ATOM 3890 N LEU A 334 84.389 44.878 218.673 1.00 30.72 N ANISOU 3890 N LEU A 334 3191 3723 4758 -514 443 -129 N ATOM 3891 CA LEU A 334 84.661 45.776 217.556 1.00 13.42 C ANISOU 3891 CA LEU A 334 1014 1478 2605 -446 444 -169 C ATOM 3892 C LEU A 334 85.621 45.140 216.559 1.00 21.83 C ANISOU 3892 C LEU A 334 2073 2554 3669 -406 351 -138 C ATOM 3893 O LEU A 334 85.481 45.334 215.346 1.00 12.55 O ANISOU 3893 O LEU A 334 899 1340 2529 -345 339 -142 O ATOM 3894 CB LEU A 334 85.217 47.104 218.067 1.00 13.92 C ANISOU 3894 CB LEU A 334 1105 1537 2649 -496 513 -244 C ATOM 3895 CG LEU A 334 84.228 47.986 218.829 1.00 23.10 C ANISOU 3895 CG LEU A 334 2279 2660 3838 -523 640 -318 C ATOM 3896 CD1 LEU A 334 84.913 49.236 219.355 1.00 19.55 C ANISOU 3896 CD1 LEU A 334 1857 2200 3370 -584 713 -420 C ATOM 3897 CD2 LEU A 334 83.047 48.349 217.942 1.00 29.55 C ANISOU 3897 CD2 LEU A 334 3074 3383 4771 -428 666 -307 C ATOM 3898 N ALA A 335 86.600 44.374 217.047 1.00 22.35 N ANISOU 3898 N ALA A 335 2124 2668 3700 -450 290 -107 N ATOM 3899 CA ALA A 335 87.494 43.660 216.140 1.00 20.22 C ANISOU 3899 CA ALA A 335 1840 2392 3449 -407 222 -95 C ATOM 3900 C ALA A 335 86.735 42.609 215.341 1.00 19.03 C ANISOU 3900 C ALA A 335 1677 2208 3347 -343 196 -78 C ATOM 3901 O ALA A 335 87.005 42.410 214.151 1.00 21.76 O ANISOU 3901 O ALA A 335 2022 2530 3716 -298 181 -102 O ATOM 3902 CB ALA A 335 88.640 43.021 216.923 1.00 16.36 C ANISOU 3902 CB ALA A 335 1324 1944 2948 -464 159 -60 C ATOM 3903 N SER A 336 85.784 41.924 215.982 1.00 18.62 N ANISOU 3903 N SER A 336 1610 2155 3311 -352 196 -41 N ATOM 3904 CA SER A 336 84.964 40.946 215.274 1.00 21.81 C ANISOU 3904 CA SER A 336 1998 2516 3773 -296 170 -31 C ATOM 3905 C SER A 336 84.057 41.611 214.247 1.00 27.60 C ANISOU 3905 C SER A 336 2743 3216 4527 -254 197 -62 C ATOM 3906 O SER A 336 83.695 40.984 213.244 1.00 24.62 O ANISOU 3906 O SER A 336 2353 2812 4189 -219 165 -74 O ATOM 3907 CB SER A 336 84.134 40.138 216.272 1.00 24.20 C ANISOU 3907 CB SER A 336 2277 2820 4099 -321 171 23 C ATOM 3908 OG SER A 336 84.967 39.437 217.179 1.00 13.29 O ANISOU 3908 OG SER A 336 871 1467 2712 -373 129 77 O ATOM 3909 N LEU A 337 83.688 42.876 214.473 1.00 12.07 N ANISOU 3909 N LEU A 337 792 1246 2549 -265 254 -77 N ATOM 3910 CA LEU A 337 82.829 43.583 213.529 1.00 12.07 C ANISOU 3910 CA LEU A 337 786 1205 2597 -229 268 -83 C ATOM 3911 C LEU A 337 83.498 43.733 212.169 1.00 23.57 C ANISOU 3911 C LEU A 337 2241 2671 4043 -219 235 -97 C ATOM 3912 O LEU A 337 82.812 43.803 211.144 1.00 32.93 O ANISOU 3912 O LEU A 337 3401 3842 5267 -203 212 -86 O ATOM 3913 CB LEU A 337 82.453 44.955 214.091 1.00 13.24 C ANISOU 3913 CB LEU A 337 942 1325 2765 -240 345 -99 C ATOM 3914 CG LEU A 337 81.383 45.760 213.348 1.00 15.51 C ANISOU 3914 CG LEU A 337 1203 1545 3145 -202 362 -83 C ATOM 3915 CD1 LEU A 337 80.036 45.048 213.402 1.00 13.06 C ANISOU 3915 CD1 LEU A 337 859 1200 2904 -177 348 -57 C ATOM 3916 CD2 LEU A 337 81.275 47.165 213.918 1.00 13.28 C ANISOU 3916 CD2 LEU A 337 925 1213 2907 -211 449 -113 C ATOM 3917 N ASN A 338 84.833 43.783 212.144 1.00 25.07 N ANISOU 3917 N ASN A 338 2447 2892 4186 -239 233 -119 N ATOM 3918 CA ASN A 338 85.554 43.919 210.882 1.00 23.57 C ANISOU 3918 CA ASN A 338 2250 2720 3984 -243 223 -141 C ATOM 3919 C ASN A 338 85.281 42.741 209.955 1.00 20.23 C ANISOU 3919 C ASN A 338 1799 2305 3583 -233 181 -162 C ATOM 3920 O ASN A 338 85.117 42.920 208.743 1.00 15.26 O ANISOU 3920 O ASN A 338 1144 1699 2957 -250 174 -176 O ATOM 3921 CB ASN A 338 87.052 44.058 211.154 1.00 24.96 C ANISOU 3921 CB ASN A 338 2441 2917 4126 -263 234 -165 C ATOM 3922 CG ASN A 338 87.860 44.259 209.887 1.00 20.56 C ANISOU 3922 CG ASN A 338 1871 2378 3560 -277 248 -195 C ATOM 3923 OD1 ASN A 338 87.958 45.372 209.369 1.00 25.43 O ANISOU 3923 OD1 ASN A 338 2492 2999 4170 -296 284 -183 O ATOM 3924 ND2 ASN A 338 88.448 43.181 209.384 1.00 12.03 N ANISOU 3924 ND2 ASN A 338 770 1305 2494 -274 232 -236 N ATOM 3925 N GLN A 339 85.232 41.526 210.506 1.00 11.84 N ANISOU 3925 N GLN A 339 731 1226 2542 -218 153 -166 N ATOM 3926 CA GLN A 339 84.930 40.354 209.693 1.00 31.44 C ANISOU 3926 CA GLN A 339 3183 3697 5066 -209 119 -202 C ATOM 3927 C GLN A 339 83.468 40.308 209.271 1.00 33.73 C ANISOU 3927 C GLN A 339 3451 3978 5388 -202 93 -185 C ATOM 3928 O GLN A 339 83.123 39.560 208.349 1.00 12.85 O ANISOU 3928 O GLN A 339 772 1338 2772 -210 60 -229 O ATOM 3929 CB GLN A 339 85.299 39.074 210.446 1.00 34.04 C ANISOU 3929 CB GLN A 339 3505 3988 5442 -192 98 -199 C ATOM 3930 CG GLN A 339 86.797 38.803 210.520 1.00 34.55 C ANISOU 3930 CG GLN A 339 3563 4048 5517 -197 105 -225 C ATOM 3931 CD GLN A 339 87.530 39.778 211.421 1.00 26.98 C ANISOU 3931 CD GLN A 339 2629 3120 4504 -216 119 -185 C ATOM 3932 OE1 GLN A 339 88.499 40.415 211.007 1.00 29.90 O ANISOU 3932 OE1 GLN A 339 3003 3508 4852 -229 144 -215 O ATOM 3933 NE2 GLN A 339 87.074 39.897 212.662 1.00 22.65 N ANISOU 3933 NE2 GLN A 339 2088 2579 3939 -229 110 -125 N ATOM 3934 N ILE A 340 82.604 41.083 209.927 1.00 26.91 N ANISOU 3934 N ILE A 340 2596 3095 4532 -192 109 -131 N ATOM 3935 CA ILE A 340 81.215 41.183 209.494 1.00 22.24 C ANISOU 3935 CA ILE A 340 1971 2482 3996 -182 81 -105 C ATOM 3936 C ILE A 340 81.086 42.171 208.343 1.00 14.42 C ANISOU 3936 C ILE A 340 950 1522 3007 -204 62 -90 C ATOM 3937 O ILE A 340 80.318 41.948 207.401 1.00 20.76 O ANISOU 3937 O ILE A 340 1704 2340 3844 -219 0 -83 O ATOM 3938 CB ILE A 340 80.317 41.568 210.683 1.00 29.17 C ANISOU 3938 CB ILE A 340 2857 3312 4914 -162 119 -61 C ATOM 3939 CG1 ILE A 340 80.454 40.540 211.808 1.00 29.22 C ANISOU 3939 CG1 ILE A 340 2876 3308 4917 -161 130 -57 C ATOM 3940 CG2 ILE A 340 78.866 41.682 210.244 1.00 35.74 C ANISOU 3940 CG2 ILE A 340 3645 4103 5833 -145 91 -29 C ATOM 3941 CD1 ILE A 340 79.744 40.928 213.087 1.00 12.73 C ANISOU 3941 CD1 ILE A 340 788 1199 2849 -165 188 -25 C ATOM 3942 N LEU A 341 81.837 43.272 208.396 1.00 12.88 N ANISOU 3942 N LEU A 341 774 1338 2780 -217 106 -76 N ATOM 3943 CA LEU A 341 81.778 44.299 207.363 1.00 28.68 C ANISOU 3943 CA LEU A 341 2738 3361 4798 -247 91 -33 C ATOM 3944 C LEU A 341 82.631 43.973 206.143 1.00 28.10 C ANISOU 3944 C LEU A 341 2641 3367 4668 -309 72 -78 C ATOM 3945 O LEU A 341 82.535 44.688 205.139 1.00 26.28 O ANISOU 3945 O LEU A 341 2365 3172 4449 -361 43 -26 O ATOM 3946 CB LEU A 341 82.215 45.649 207.938 1.00 13.29 C ANISOU 3946 CB LEU A 341 817 1373 2858 -240 159 1 C ATOM 3947 CG LEU A 341 81.445 46.173 209.152 1.00 28.15 C ANISOU 3947 CG LEU A 341 2715 3178 4804 -198 204 17 C ATOM 3948 CD1 LEU A 341 81.919 47.571 209.525 1.00 13.37 C ANISOU 3948 CD1 LEU A 341 861 1265 2956 -200 272 28 C ATOM 3949 CD2 LEU A 341 79.946 46.163 208.890 1.00 13.85 C ANISOU 3949 CD2 LEU A 341 848 1315 3100 -171 162 72 C ATOM 3950 N ASP A 342 83.454 42.923 206.204 1.00 27.42 N ANISOU 3950 N ASP A 342 2576 3304 4539 -312 88 -166 N ATOM 3951 CA ASP A 342 84.359 42.615 205.096 1.00 29.92 C ANISOU 3951 CA ASP A 342 2869 3689 4812 -376 103 -246 C ATOM 3952 C ASP A 342 83.644 42.341 203.777 1.00 31.19 C ANISOU 3952 C ASP A 342 2966 3917 4967 -450 32 -277 C ATOM 3953 O ASP A 342 84.026 42.948 202.761 1.00 32.56 O ANISOU 3953 O ASP A 342 3200 4173 4999 -500 37 -258 O ATOM 3954 CB ASP A 342 85.266 41.442 205.483 1.00 32.96 C ANISOU 3954 CB ASP A 342 3277 4051 5194 -349 133 -336 C ATOM 3955 CG ASP A 342 86.525 41.888 206.197 1.00 52.11 C ANISOU 3955 CG ASP A 342 5745 6455 7599 -329 192 -328 C ATOM 3956 OD1 ASP A 342 87.118 42.904 205.777 1.00 60.29 O ANISOU 3956 OD1 ASP A 342 6785 7523 8599 -366 237 -314 O ATOM 3957 OD2 ASP A 342 86.926 41.219 207.173 1.00 62.40 O ANISOU 3957 OD2 ASP A 342 7071 7709 8928 -285 185 -328 O ATOM 3958 N PRO A 343 82.634 41.466 203.699 1.00 23.29 N ANISOU 3958 N PRO A 343 1939 2904 4004 -435 -46 -296 N ATOM 3959 CA PRO A 343 82.013 41.204 202.390 1.00 25.59 C ANISOU 3959 CA PRO A 343 2229 3284 4209 -502 -140 -325 C ATOM 3960 C PRO A 343 81.317 42.416 201.796 1.00 36.20 C ANISOU 3960 C PRO A 343 3607 4669 5477 -517 -217 -167 C ATOM 3961 O PRO A 343 81.149 42.478 200.571 1.00 41.26 O ANISOU 3961 O PRO A 343 4295 5422 5961 -589 -291 -160 O ATOM 3962 CB PRO A 343 81.018 40.075 202.690 1.00 24.94 C ANISOU 3962 CB PRO A 343 2085 3150 4243 -477 -206 -369 C ATOM 3963 CG PRO A 343 80.706 40.233 204.129 1.00 15.69 C ANISOU 3963 CG PRO A 343 953 1874 3133 -371 -153 -272 C ATOM 3964 CD PRO A 343 81.984 40.680 204.765 1.00 20.71 C ANISOU 3964 CD PRO A 343 1639 2497 3733 -351 -52 -276 C ATOM 3965 N TRP A 344 80.913 43.384 202.620 1.00 24.27 N ANISOU 3965 N TRP A 344 2070 3072 4079 -459 -203 -40 N ATOM 3966 CA TRP A 344 80.229 44.564 202.103 1.00 18.48 C ANISOU 3966 CA TRP A 344 1342 2344 3335 -464 -279 127 C ATOM 3967 C TRP A 344 81.215 45.590 201.559 1.00 29.43 C ANISOU 3967 C TRP A 344 2806 3783 4592 -502 -224 188 C ATOM 3968 O TRP A 344 80.985 46.171 200.492 1.00 23.22 O ANISOU 3968 O TRP A 344 2057 3074 3690 -557 -307 299 O ATOM 3969 CB TRP A 344 79.364 45.188 203.199 1.00 21.64 C ANISOU 3969 CB TRP A 344 1665 2609 3948 -389 -264 219 C ATOM 3970 CG TRP A 344 78.388 44.233 203.813 1.00 24.99 C ANISOU 3970 CG TRP A 344 2031 2978 4486 -347 -291 168 C ATOM 3971 CD1 TRP A 344 78.570 43.488 204.942 1.00 24.23 C ANISOU 3971 CD1 TRP A 344 1992 2832 4383 -289 -193 76 C ATOM 3972 CD2 TRP A 344 77.076 43.917 203.332 1.00 25.26 C ANISOU 3972 CD2 TRP A 344 2012 3007 4578 -345 -417 220 C ATOM 3973 NE1 TRP A 344 77.452 42.729 205.194 1.00 21.93 N ANISOU 3973 NE1 TRP A 344 1683 2498 4150 -256 -233 70 N ATOM 3974 CE2 TRP A 344 76.520 42.975 204.220 1.00 24.45 C ANISOU 3974 CE2 TRP A 344 1935 2840 4516 -285 -362 144 C ATOM 3975 CE3 TRP A 344 76.316 44.342 202.237 1.00 21.90 C ANISOU 3975 CE3 TRP A 344 1528 2629 4164 -395 -584 341 C ATOM 3976 CZ2 TRP A 344 75.241 42.449 204.047 1.00 25.90 C ANISOU 3976 CZ2 TRP A 344 2076 2992 4771 -271 -443 164 C ATOM 3977 CZ3 TRP A 344 75.046 43.817 202.066 1.00 27.45 C ANISOU 3977 CZ3 TRP A 344 2194 3306 4930 -376 -680 357 C ATOM 3978 CH2 TRP A 344 74.522 42.881 202.967 1.00 25.60 C ANISOU 3978 CH2 TRP A 344 1977 2994 4755 -313 -597 260 C ATOM 3979 N VAL A 345 82.320 45.823 202.275 1.00 33.37 N ANISOU 3979 N VAL A 345 3326 4243 5109 -482 -92 129 N ATOM 3980 CA VAL A 345 83.278 46.840 201.859 1.00 17.53 C ANISOU 3980 CA VAL A 345 1380 2266 3014 -517 -26 188 C ATOM 3981 C VAL A 345 84.046 46.436 200.607 1.00 41.96 C ANISOU 3981 C VAL A 345 4547 5504 5892 -606 -15 125 C ATOM 3982 O VAL A 345 84.616 47.300 199.932 1.00 36.28 O ANISOU 3982 O VAL A 345 3884 4837 5066 -657 17 208 O ATOM 3983 CB VAL A 345 84.255 47.165 203.006 1.00 16.30 C ANISOU 3983 CB VAL A 345 1215 2028 2948 -479 102 130 C ATOM 3984 CG1 VAL A 345 83.513 47.783 204.175 1.00 25.22 C ANISOU 3984 CG1 VAL A 345 2291 3033 4260 -415 113 188 C ATOM 3985 CG2 VAL A 345 84.996 45.919 203.445 1.00 18.23 C ANISOU 3985 CG2 VAL A 345 1448 2289 3191 -478 154 -35 C ATOM 3986 N TYR A 346 84.083 45.148 200.271 1.00 33.24 N ANISOU 3986 N TYR A 346 3441 4462 4728 -634 -26 -28 N ATOM 3987 CA TYR A 346 84.825 44.692 199.102 1.00 35.90 C ANISOU 3987 CA TYR A 346 3844 4936 4862 -730 15 -130 C ATOM 3988 C TYR A 346 83.937 44.341 197.915 1.00 43.53 C ANISOU 3988 C TYR A 346 4848 6028 5664 -811 -115 -115 C ATOM 3989 O TYR A 346 84.261 44.712 196.782 1.00 56.97 O ANISOU 3989 O TYR A 346 6633 7867 7146 -912 -116 -81 O ATOM 3990 CB TYR A 346 85.700 43.486 199.462 1.00 39.88 C ANISOU 3990 CB TYR A 346 4314 5416 5424 -722 120 -346 C ATOM 3991 CG TYR A 346 86.937 43.854 200.254 1.00 50.80 C ANISOU 3991 CG TYR A 346 5676 6724 6899 -685 250 -370 C ATOM 3992 CD1 TYR A 346 88.066 44.359 199.620 1.00 51.11 C ANISOU 3992 CD1 TYR A 346 5765 6828 6829 -745 359 -390 C ATOM 3993 CD2 TYR A 346 86.977 43.697 201.634 1.00 46.30 C ANISOU 3993 CD2 TYR A 346 5039 6030 6521 -602 260 -368 C ATOM 3994 CE1 TYR A 346 89.198 44.698 200.339 1.00 41.64 C ANISOU 3994 CE1 TYR A 346 4532 5556 5732 -716 465 -411 C ATOM 3995 CE2 TYR A 346 88.105 44.036 202.361 1.00 38.49 C ANISOU 3995 CE2 TYR A 346 4031 4985 5610 -581 354 -386 C ATOM 3996 CZ TYR A 346 89.212 44.535 201.708 1.00 42.40 C ANISOU 3996 CZ TYR A 346 4561 5532 6018 -635 451 -409 C ATOM 3997 OH TYR A 346 90.337 44.872 202.426 1.00 46.66 O ANISOU 3997 OH TYR A 346 5066 6010 6651 -618 533 -427 O ATOM 3998 N LEU A 347 82.832 43.628 198.130 1.00 29.05 N ANISOU 3998 N LEU A 347 2671 4789 3579 -767 295 788 N ATOM 3999 CA LEU A 347 82.043 43.116 197.016 1.00 31.28 C ANISOU 3999 CA LEU A 347 3051 5134 3700 -791 347 781 C ATOM 4000 C LEU A 347 80.604 43.611 197.002 1.00 34.26 C ANISOU 4000 C LEU A 347 3496 5453 4067 -825 259 812 C ATOM 4001 O LEU A 347 80.126 44.069 195.957 1.00 35.99 O ANISOU 4001 O LEU A 347 3731 5722 4221 -876 237 886 O ATOM 4002 CB LEU A 347 82.059 41.579 197.033 1.00 34.51 C ANISOU 4002 CB LEU A 347 3540 5591 3982 -711 473 636 C ATOM 4003 CG LEU A 347 81.427 40.902 195.816 1.00 35.39 C ANISOU 4003 CG LEU A 347 3743 5754 3951 -722 530 592 C ATOM 4004 CD1 LEU A 347 82.149 41.323 194.546 1.00 33.69 C ANISOU 4004 CD1 LEU A 347 3466 5631 3706 -776 544 683 C ATOM 4005 CD2 LEU A 347 81.430 39.390 195.969 1.00 31.17 C ANISOU 4005 CD2 LEU A 347 3311 5198 3335 -628 644 436 C ATOM 4006 N LEU A 348 79.895 43.536 198.131 1.00 29.78 N ANISOU 4006 N LEU A 348 2962 4793 3562 -795 206 757 N ATOM 4007 CA LEU A 348 78.439 43.656 198.098 1.00 21.34 C ANISOU 4007 CA LEU A 348 1970 3691 2446 -819 149 742 C ATOM 4008 C LEU A 348 77.953 45.089 197.904 1.00 25.26 C ANISOU 4008 C LEU A 348 2441 4130 3029 -870 8 877 C ATOM 4009 O LEU A 348 76.926 45.297 197.250 1.00 31.01 O ANISOU 4009 O LEU A 348 3208 4906 3669 -904 -24 904 O ATOM 4010 CB LEU A 348 77.837 43.067 199.374 1.00 19.56 C ANISOU 4010 CB LEU A 348 1799 3376 2256 -772 146 625 C ATOM 4011 CG LEU A 348 78.109 41.576 199.593 1.00 29.37 C ANISOU 4011 CG LEU A 348 3128 4643 3388 -684 300 464 C ATOM 4012 CD1 LEU A 348 77.456 41.084 200.875 1.00 30.20 C ANISOU 4012 CD1 LEU A 348 3353 4584 3536 -579 280 317 C ATOM 4013 CD2 LEU A 348 77.643 40.754 198.399 1.00 31.08 C ANISOU 4013 CD2 LEU A 348 3418 4956 3436 -703 402 402 C ATOM 4014 N LEU A 349 78.654 46.084 198.453 1.00 35.43 N ANISOU 4014 N LEU A 349 3664 5318 4480 -868 -73 951 N ATOM 4015 CA LEU A 349 78.231 47.467 198.243 1.00 31.33 C ANISOU 4015 CA LEU A 349 3140 4728 4036 -903 -190 1076 C ATOM 4016 C LEU A 349 78.403 47.897 196.792 1.00 29.75 C ANISOU 4016 C LEU A 349 2920 4645 3739 -965 -151 1198 C ATOM 4017 O LEU A 349 77.595 48.680 196.281 1.00 31.29 O ANISOU 4017 O LEU A 349 3132 4844 3911 -995 -222 1297 O ATOM 4018 CB LEU A 349 79.000 48.413 199.165 1.00 42.63 C ANISOU 4018 CB LEU A 349 4521 6014 5660 -878 -266 1097 C ATOM 4019 CG LEU A 349 78.607 48.433 200.642 1.00 42.35 C ANISOU 4019 CG LEU A 349 4521 5828 5744 -798 -352 991 C ATOM 4020 CD1 LEU A 349 79.475 49.423 201.404 1.00 40.75 C ANISOU 4020 CD1 LEU A 349 4266 5506 5709 -771 -410 999 C ATOM 4021 CD2 LEU A 349 77.135 48.774 200.800 1.00 36.88 C ANISOU 4021 CD2 LEU A 349 3914 5069 5028 -786 -443 993 C ATOM 4022 N ARG A 350 79.443 47.405 196.116 1.00 35.40 N ANISOU 4022 N ARG A 350 3595 5458 4396 -977 -41 1193 N ATOM 4023 CA ARG A 350 79.608 47.706 194.698 1.00 44.96 C ANISOU 4023 CA ARG A 350 4794 6783 5506 -1026 5 1293 C ATOM 4024 C ARG A 350 78.478 47.102 193.875 1.00 44.54 C ANISOU 4024 C ARG A 350 4798 6847 5278 -1023 23 1262 C ATOM 4025 O ARG A 350 78.036 47.692 192.883 1.00 50.75 O ANISOU 4025 O ARG A 350 5583 7705 5995 -1056 2 1366 O ATOM 4026 CB ARG A 350 80.963 47.196 194.205 1.00 54.04 C ANISOU 4026 CB ARG A 350 5892 8008 6631 -1032 120 1269 C ATOM 4027 CG ARG A 350 82.137 48.087 194.569 1.00 64.22 C ANISOU 4027 CG ARG A 350 7102 9222 8077 -1065 112 1329 C ATOM 4028 CD ARG A 350 83.448 47.471 194.113 1.00 71.13 C ANISOU 4028 CD ARG A 350 7919 10190 8918 -1071 228 1286 C ATOM 4029 NE ARG A 350 84.579 48.374 194.311 1.00 78.21 N ANISOU 4029 NE ARG A 350 8727 11033 9954 -1121 234 1335 N ATOM 4030 CZ ARG A 350 85.032 49.212 193.384 1.00 81.89 C ANISOU 4030 CZ ARG A 350 9168 11518 10428 -1195 268 1448 C ATOM 4031 NH1 ARG A 350 84.449 49.264 192.194 1.00 83.34 N ANISOU 4031 NH1 ARG A 350 9405 11779 10481 -1216 290 1532 N ATOM 4032 NH2 ARG A 350 86.067 49.999 193.647 1.00 82.93 N ANISOU 4032 NH2 ARG A 350 9220 11594 10697 -1248 287 1467 N ATOM 4033 N LYS A 351 77.999 45.921 194.273 1.00 40.23 N ANISOU 4033 N LYS A 351 4301 6324 4660 -983 69 1110 N ATOM 4034 CA LYS A 351 76.934 45.259 193.526 1.00 27.55 C ANISOU 4034 CA LYS A 351 2746 4829 2893 -981 97 1040 C ATOM 4035 C LYS A 351 75.612 46.005 193.670 1.00 36.66 C ANISOU 4035 C LYS A 351 3916 5972 4041 -1006 -16 1095 C ATOM 4036 O LYS A 351 74.855 46.131 192.700 1.00 41.90 O ANISOU 4036 O LYS A 351 4580 6756 4583 -1024 -26 1125 O ATOM 4037 CB LYS A 351 76.793 43.813 194.000 1.00 23.85 C ANISOU 4037 CB LYS A 351 2338 4355 2370 -931 188 846 C ATOM 4038 CG LYS A 351 75.770 42.990 193.233 1.00 32.83 C ANISOU 4038 CG LYS A 351 3527 5589 3359 -927 231 732 C ATOM 4039 CD LYS A 351 76.179 42.803 191.782 1.00 39.00 C ANISOU 4039 CD LYS A 351 4280 6496 4044 -936 285 765 C ATOM 4040 CE LYS A 351 75.051 42.190 190.969 1.00 40.01 C ANISOU 4040 CE LYS A 351 4436 6724 4043 -936 302 662 C ATOM 4041 NZ LYS A 351 74.591 40.895 191.545 1.00 28.46 N ANISOU 4041 NZ LYS A 351 3051 5189 2575 -895 369 459 N ATOM 4042 N ILE A 352 75.316 46.501 194.874 1.00 37.54 N ANISOU 4042 N ILE A 352 4037 5944 4283 -1000 -105 1102 N ATOM 4043 CA ILE A 352 74.076 47.243 195.094 1.00 36.74 C ANISOU 4043 CA ILE A 352 3951 5817 4190 -1021 -225 1155 C ATOM 4044 C ILE A 352 74.074 48.533 194.283 1.00 43.72 C ANISOU 4044 C ILE A 352 4798 6724 5091 -1051 -297 1350 C ATOM 4045 O ILE A 352 73.071 48.887 193.651 1.00 36.89 O ANISOU 4045 O ILE A 352 3940 5951 4126 -1066 -344 1402 O ATOM 4046 CB ILE A 352 73.880 47.519 196.597 1.00 25.34 C ANISOU 4046 CB ILE A 352 2529 4183 2916 -992 -315 1107 C ATOM 4047 CG1 ILE A 352 73.671 46.209 197.359 1.00 18.44 C ANISOU 4047 CG1 ILE A 352 1705 3293 2010 -960 -235 909 C ATOM 4048 CG2 ILE A 352 72.711 48.466 196.822 1.00 17.98 C ANISOU 4048 CG2 ILE A 352 1610 3198 2023 -1007 -460 1175 C ATOM 4049 CD1 ILE A 352 73.541 46.387 198.857 1.00 15.56 C ANISOU 4049 CD1 ILE A 352 1368 2733 1812 -904 -320 834 C ATOM 4050 N LEU A 353 75.195 49.249 194.283 1.00 45.26 N ANISOU 4050 N LEU A 353 4954 6838 5406 -1056 -295 1448 N ATOM 4051 CA LEU A 353 75.329 50.502 193.552 1.00 41.40 C ANISOU 4051 CA LEU A 353 4439 6340 4950 -1083 -338 1626 C ATOM 4052 C LEU A 353 75.733 50.301 192.097 1.00 47.27 C ANISOU 4052 C LEU A 353 5167 7245 5550 -1101 -236 1680 C ATOM 4053 O LEU A 353 75.956 51.289 191.390 1.00 40.02 O ANISOU 4053 O LEU A 353 4236 6320 4648 -1121 -243 1827 O ATOM 4054 CB LEU A 353 76.353 51.404 194.250 1.00 23.64 C ANISOU 4054 CB LEU A 353 2158 3922 2901 -1088 -369 1684 C ATOM 4055 CG LEU A 353 76.000 51.839 195.674 1.00 25.57 C ANISOU 4055 CG LEU A 353 2418 3987 3310 -1052 -486 1635 C ATOM 4056 CD1 LEU A 353 77.148 52.613 196.302 1.00 22.85 C ANISOU 4056 CD1 LEU A 353 2034 3502 3147 -1050 -493 1656 C ATOM 4057 CD2 LEU A 353 74.720 52.662 195.688 1.00 22.34 C ANISOU 4057 CD2 LEU A 353 2038 3540 2911 -1051 -613 1710 C ATOM 4058 N LEU A 354 75.826 49.056 191.637 1.00 56.17 N ANISOU 4058 N LEU A 354 6300 8499 6542 -1087 -139 1555 N ATOM 4059 CA LEU A 354 76.316 48.779 190.294 1.00 62.51 C ANISOU 4059 CA LEU A 354 7085 9441 7223 -1095 -44 1585 C ATOM 4060 C LEU A 354 75.359 49.311 189.235 1.00 60.11 C ANISOU 4060 C LEU A 354 6791 9254 6796 -1091 -76 1679 C ATOM 4061 O LEU A 354 74.136 49.203 189.365 1.00 53.81 O ANISOU 4061 O LEU A 354 6015 8504 5929 -1073 -135 1632 O ATOM 4062 CB LEU A 354 76.519 47.275 190.104 1.00 63.70 C ANISOU 4062 CB LEU A 354 7250 9680 7272 -1068 56 1406 C ATOM 4063 CG LEU A 354 77.231 46.836 188.824 1.00 60.50 C ANISOU 4063 CG LEU A 354 6825 9396 6765 -1071 157 1412 C ATOM 4064 CD1 LEU A 354 78.631 47.429 188.760 1.00 58.97 C ANISOU 4064 CD1 LEU A 354 6592 9141 6673 -1102 197 1513 C ATOM 4065 CD2 LEU A 354 77.281 45.319 188.733 1.00 61.37 C ANISOU 4065 CD2 LEU A 354 6963 9561 6795 -1035 243 1220 C ATOM 4066 N ARG A 355 75.933 49.891 188.184 1.00 68.96 N ANISOU 4066 N ARG A 355 7897 10422 7883 -1105 -28 1807 N ATOM 4067 CA ARG A 355 75.186 50.423 187.046 1.00 65.51 C ANISOU 4067 CA ARG A 355 7474 10100 7316 -1083 -40 1909 C ATOM 4068 C ARG A 355 74.139 51.448 187.473 1.00 69.08 C ANISOU 4068 C ARG A 355 7958 10478 7811 -1061 -157 1997 C ATOM 4069 O ARG A 355 74.239 52.627 187.131 1.00 67.63 O ANISOU 4069 O ARG A 355 7798 10225 7673 -1058 -179 2160 O ATOM 4070 CB ARG A 355 74.522 49.286 186.265 1.00 57.07 C ANISOU 4070 CB ARG A 355 6400 9222 6061 -1051 7 1771 C ATOM 4071 CG ARG A 355 73.921 49.722 184.944 1.00 63.24 C ANISOU 4071 CG ARG A 355 7189 10149 6691 -1013 13 1862 C ATOM 4072 CD ARG A 355 73.860 48.571 183.958 1.00 70.90 C ANISOU 4072 CD ARG A 355 8134 11299 7505 -994 94 1733 C ATOM 4073 NE ARG A 355 73.783 49.053 182.583 1.00 76.90 N ANISOU 4073 NE ARG A 355 8896 12187 8137 -961 124 1850 N ATOM 4074 CZ ARG A 355 74.842 49.386 181.852 1.00 78.90 C ANISOU 4074 CZ ARG A 355 9147 12436 8394 -982 197 1966 C ATOM 4075 NH1 ARG A 355 76.062 49.289 182.365 1.00 67.54 N ANISOU 4075 NH1 ARG A 355 7698 10881 7084 -1037 245 1970 N ATOM 4076 NH2 ARG A 355 74.684 49.817 180.608 1.00 86.14 N ANISOU 4076 NH2 ARG A 355 10077 13471 9182 -944 227 2073 N ATOM 4077 N ALA A1001 95.804 66.654 180.347 1.00 93.64 N ANISOU 4077 N ALA A1001 11148 11882 12549 -3251 2608 3293 N ATOM 4078 CA ALA A1001 95.884 67.680 179.315 1.00101.50 C ANISOU 4078 CA ALA A1001 12336 12761 13468 -3356 2788 3480 C ATOM 4079 C ALA A1001 95.793 67.061 177.925 1.00104.96 C ANISOU 4079 C ALA A1001 12843 13358 13678 -3278 2861 3603 C ATOM 4080 O ALA A1001 95.921 67.756 176.916 1.00108.67 O ANISOU 4080 O ALA A1001 13474 13765 14049 -3353 3021 3762 O ATOM 4081 CB ALA A1001 97.170 68.477 179.458 1.00108.79 C ANISOU 4081 CB ALA A1001 13214 13576 14544 -3617 2997 3389 C ATOM 4082 N ASP A1002 95.570 65.745 177.882 1.00101.89 N ANISOU 4082 N ASP A1002 12338 13179 13197 -3129 2738 3525 N ATOM 4083 CA ASP A1002 95.523 65.042 176.603 1.00102.37 C ANISOU 4083 CA ASP A1002 12440 13416 13040 -3052 2792 3612 C ATOM 4084 C ASP A1002 94.299 65.444 175.789 1.00 98.71 C ANISOU 4084 C ASP A1002 12188 12937 12382 -2925 2736 3833 C ATOM 4085 O ASP A1002 94.381 65.583 174.563 1.00104.54 O ANISOU 4085 O ASP A1002 13041 13724 12956 -2931 2862 3968 O ATOM 4086 CB ASP A1002 95.540 63.532 176.837 1.00102.88 C ANISOU 4086 CB ASP A1002 12334 13702 13052 -2929 2659 3460 C ATOM 4087 CG ASP A1002 96.752 63.079 177.627 1.00105.03 C ANISOU 4087 CG ASP A1002 12396 14004 13505 -3029 2707 3241 C ATOM 4088 OD1 ASP A1002 97.627 63.924 177.913 1.00105.54 O ANISOU 4088 OD1 ASP A1002 12433 13932 13734 -3205 2857 3197 O ATOM 4089 OD2 ASP A1002 96.829 61.879 177.966 1.00103.64 O ANISOU 4089 OD2 ASP A1002 12085 13990 13303 -2933 2596 3105 O ATOM 4090 N LEU A1003 93.159 65.631 176.448 1.00 89.18 N ANISOU 4090 N LEU A1003 11030 11668 11185 -2804 2550 3867 N ATOM 4091 CA LEU A1003 91.923 65.989 175.761 1.00 79.51 C ANISOU 4091 CA LEU A1003 9991 10439 9780 -2663 2479 4059 C ATOM 4092 C LEU A1003 92.018 67.368 175.116 1.00 83.25 C ANISOU 4092 C LEU A1003 10677 10722 10232 -2759 2641 4249 C ATOM 4093 O LEU A1003 91.739 67.528 173.927 1.00 89.92 O ANISOU 4093 O LEU A1003 11668 11620 10879 -2710 2714 4410 O ATOM 4094 N LYS A1104 82.458 63.107 175.904 1.00 92.28 N ANISOU 4094 N LYS A1104 11772 12776 10513 -1427 1220 4146 N ATOM 4095 CA LYS A1104 81.916 62.281 176.977 1.00 91.31 C ANISOU 4095 CA LYS A1104 11518 12709 10467 -1390 1059 3973 C ATOM 4096 C LYS A1104 82.970 61.326 177.528 1.00 89.96 C ANISOU 4096 C LYS A1104 11183 12588 10409 -1496 1091 3803 C ATOM 4097 O LYS A1104 82.809 60.770 178.614 1.00 93.22 O ANISOU 4097 O LYS A1104 11495 12994 10932 -1498 981 3658 O ATOM 4098 CB LYS A1104 80.704 61.486 176.485 1.00 94.88 C ANISOU 4098 CB LYS A1104 11960 13379 10711 -1241 944 3931 C ATOM 4099 CG LYS A1104 79.528 62.341 176.042 1.00 99.12 C ANISOU 4099 CG LYS A1104 12649 13888 11125 -1108 884 4070 C ATOM 4100 CD LYS A1104 78.354 61.472 175.615 1.00 95.73 C ANISOU 4100 CD LYS A1104 12184 13694 10497 -968 770 3991 C ATOM 4101 CE LYS A1104 77.153 62.315 175.219 1.00 92.66 C ANISOU 4101 CE LYS A1104 11942 13286 9978 -820 697 4110 C ATOM 4102 NZ LYS A1104 75.994 61.467 174.824 1.00 93.03 N ANISOU 4102 NZ LYS A1104 11940 13574 9832 -686 587 4009 N ATOM 4103 N TYR A1105 84.052 61.139 176.768 1.00 91.37 N ANISOU 4103 N TYR A1105 11345 12818 10553 -1579 1243 3819 N ATOM 4104 CA TYR A1105 85.097 60.213 177.191 1.00 86.72 C ANISOU 4104 CA TYR A1105 10607 12290 10053 -1666 1281 3655 C ATOM 4105 C TYR A1105 85.894 60.750 178.373 1.00 81.71 C ANISOU 4105 C TYR A1105 9918 11460 9669 -1782 1299 3595 C ATOM 4106 O TYR A1105 86.422 59.964 179.169 1.00 74.00 O ANISOU 4106 O TYR A1105 8811 10516 8788 -1816 1262 3428 O ATOM 4107 N GLY A1106 85.997 62.069 178.504 1.00 81.82 N ANISOU 4107 N GLY A1106 10032 11271 9784 -1838 1357 3720 N ATOM 4108 CA GLY A1106 86.754 62.676 179.584 1.00 78.01 C ANISOU 4108 CA GLY A1106 9497 10599 9543 -1956 1383 3657 C ATOM 4109 C GLY A1106 86.173 62.425 180.962 1.00 71.78 C ANISOU 4109 C GLY A1106 8631 9759 8881 -1907 1207 3533 C ATOM 4110 O GLY A1106 86.805 61.800 181.813 1.00 74.08 O ANISOU 4110 O GLY A1106 8790 10067 9288 -1953 1179 3370 O TER 4111 GLY A1106 HETATM 4112 C2 P2E B1201 64.680 52.025 223.997 1.00 34.67 C HETATM 4113 C3 P2E B1201 64.003 51.085 222.961 1.00 18.42 C HETATM 4114 C4 P2E B1201 63.166 51.867 221.937 1.00 14.58 C HETATM 4115 C5 P2E B1201 62.876 50.957 220.699 1.00 30.40 C HETATM 4116 C6 P2E B1201 62.913 51.481 219.475 1.00 29.50 C HETATM 4117 C7 P2E B1201 63.229 52.957 219.315 1.00 18.89 C HETATM 4118 C8 P2E B1201 64.121 53.208 218.007 1.00 31.64 C HETATM 4119 C9 P2E B1201 65.427 52.858 218.253 1.00 31.33 C HETATM 4120 O3 P2E B1201 65.942 52.845 219.311 1.00 24.19 O HETATM 4121 C12 P2E B1201 63.723 52.281 216.860 1.00 31.67 C HETATM 4122 C11 P2E B1201 65.153 52.042 216.041 1.00 28.29 C HETATM 4123 O4 P2E B1201 65.338 50.691 215.754 1.00 36.55 O HETATM 4124 C10 P2E B1201 66.134 52.469 216.866 1.00 22.19 C HETATM 4125 C13 P2E B1201 62.732 52.919 216.009 1.00 27.01 C HETATM 4126 C14 P2E B1201 61.880 52.159 215.237 1.00 26.75 C HETATM 4127 C15 P2E B1201 60.833 52.850 214.345 1.00 42.95 C HETATM 4128 O5 P2E B1201 61.230 52.787 213.023 1.00 49.86 O HETATM 4129 C16 P2E B1201 59.457 52.144 214.501 1.00 37.27 C HETATM 4130 C17 P2E B1201 59.088 51.883 215.976 1.00 23.99 C HETATM 4131 C18 P2E B1201 57.774 51.137 216.125 1.00 22.85 C HETATM 4132 C19 P2E B1201 57.798 50.130 217.331 1.00 24.30 C HETATM 4133 C20 P2E B1201 56.457 49.962 217.954 1.00 27.62 C HETATM 4134 O1 P2E B1201 66.102 51.307 225.821 1.00 40.42 O HETATM 4135 C1 P2E B1201 65.967 51.426 224.579 1.00 40.90 C HETATM 4136 O2 P2E B1201 66.881 51.051 223.813 1.00 45.64 O HETATM 4137 P POV B1202 75.794 50.977 228.301 1.00114.67 P HETATM 4138 C1 POV B1202 77.596 49.489 227.059 1.00 94.02 C HETATM 4139 C2 POV B1202 78.127 49.251 225.645 1.00 82.83 C HETATM 4140 C3 POV B1202 77.570 50.357 224.751 1.00 79.82 C HETATM 4141 C210 POV B1202 75.999 43.658 215.961 1.00 19.85 C HETATM 4142 C310 POV B1202 76.807 49.299 214.054 1.00 51.89 C HETATM 4143 O11 POV B1202 76.403 50.219 226.969 1.00109.81 O HETATM 4144 C211 POV B1202 75.998 44.604 214.762 1.00 14.13 C HETATM 4145 C311 POV B1202 77.089 48.186 213.049 1.00 45.94 C HETATM 4146 O12 POV B1202 74.419 51.796 227.911 1.00109.28 O HETATM 4147 C212 POV B1202 75.919 43.793 213.471 1.00 20.48 C HETATM 4148 C312 POV B1202 77.683 48.796 211.782 1.00 49.28 C HETATM 4149 O13 POV B1202 75.558 50.032 229.391 1.00113.95 O HETATM 4150 C213 POV B1202 75.386 44.683 212.350 1.00 24.31 C HETATM 4151 C313 POV B1202 76.641 49.683 211.103 1.00 53.16 C HETATM 4152 O14 POV B1202 76.779 51.870 228.908 1.00123.04 O HETATM 4153 C214 POV B1202 76.248 44.511 211.101 1.00 36.40 C HETATM 4154 C314 POV B1202 77.241 50.314 209.849 1.00 55.60 C HETATM 4155 C215 POV B1202 75.363 44.564 209.859 1.00 38.14 C HETATM 4156 C315 POV B1202 77.877 49.225 208.988 1.00 59.39 C HETATM 4157 C216 POV B1202 76.076 45.341 208.755 1.00 38.80 C HETATM 4158 C316 POV B1202 78.081 49.748 207.568 1.00 64.21 C HETATM 4159 C217 POV B1202 75.412 45.026 207.416 1.00 38.08 C HETATM 4160 C218 POV B1202 75.600 46.202 206.461 1.00 38.96 C HETATM 4161 C21 POV B1202 78.620 47.246 224.444 1.00 65.63 C HETATM 4162 O21 POV B1202 77.692 47.999 225.183 1.00 79.12 O HETATM 4163 C22 POV B1202 79.188 47.763 223.121 1.00 43.91 C HETATM 4164 O22 POV B1202 78.963 46.185 224.846 1.00 74.83 O HETATM 4165 C23 POV B1202 79.434 46.602 222.161 1.00 34.75 C HETATM 4166 C24 POV B1202 79.775 47.156 220.779 1.00 37.85 C HETATM 4167 C25 POV B1202 80.104 46.007 219.828 1.00 42.88 C HETATM 4168 C26 POV B1202 79.347 46.196 218.514 1.00 39.94 C HETATM 4169 C27 POV B1202 79.068 44.837 217.876 1.00 34.59 C HETATM 4170 C28 POV B1202 78.010 44.993 216.784 1.00 36.12 C HETATM 4171 C29 POV B1202 76.751 44.216 217.169 1.00 32.46 C HETATM 4172 C31 POV B1202 78.955 51.851 223.595 1.00 55.94 C HETATM 4173 O31 POV B1202 78.391 51.487 224.822 1.00 74.91 O HETATM 4174 C32 POV B1202 78.089 51.902 222.340 1.00 52.71 C HETATM 4175 O32 POV B1202 80.106 52.120 223.530 1.00 50.35 O HETATM 4176 C33 POV B1202 78.974 51.710 221.110 1.00 51.32 C HETATM 4177 C34 POV B1202 78.101 51.424 219.890 1.00 40.04 C HETATM 4178 C35 POV B1202 78.945 50.747 218.813 1.00 38.61 C HETATM 4179 C36 POV B1202 78.141 49.610 218.189 1.00 42.48 C HETATM 4180 C37 POV B1202 78.613 49.372 216.757 1.00 46.85 C HETATM 4181 C38 POV B1202 78.054 50.473 215.860 1.00 49.29 C HETATM 4182 C39 POV B1202 78.109 50.016 214.405 1.00 53.09 C HETATM 4183 C2 P2E A1201 82.070 36.950 223.940 1.00 20.40 C HETATM 4184 C3 P2E A1201 82.867 37.925 223.030 1.00 12.99 C HETATM 4185 C4 P2E A1201 83.729 37.176 222.002 1.00 14.27 C HETATM 4186 C5 P2E A1201 83.978 38.100 220.767 1.00 20.01 C HETATM 4187 C6 P2E A1201 83.955 37.572 219.546 1.00 23.62 C HETATM 4188 C7 P2E A1201 83.695 36.085 219.394 1.00 18.42 C HETATM 4189 C8 P2E A1201 82.690 35.804 218.177 1.00 26.38 C HETATM 4190 C9 P2E A1201 81.420 36.210 218.510 1.00 24.92 C HETATM 4191 O3 P2E A1201 80.995 36.309 219.604 1.00 18.67 O HETATM 4192 C12 P2E A1201 83.010 36.677 216.964 1.00 23.50 C HETATM 4193 C11 P2E A1201 81.528 36.845 216.227 1.00 20.61 C HETATM 4194 O4 P2E A1201 81.340 38.154 215.786 1.00 26.82 O HETATM 4195 C10 P2E A1201 80.607 36.536 217.166 1.00 16.67 C HETATM 4196 C13 P2E A1201 83.944 36.028 216.062 1.00 16.71 C HETATM 4197 C14 P2E A1201 84.809 36.788 215.303 1.00 26.51 C HETATM 4198 C15 P2E A1201 85.796 36.104 214.338 1.00 42.54 C HETATM 4199 O5 P2E A1201 85.358 36.291 213.042 1.00 49.86 O HETATM 4200 C16 P2E A1201 87.218 36.714 214.473 1.00 33.02 C HETATM 4201 C17 P2E A1201 87.622 37.003 215.932 1.00 19.56 C HETATM 4202 C18 P2E A1201 89.048 37.516 216.036 1.00 9.62 C HETATM 4203 C19 P2E A1201 89.155 38.777 216.966 1.00 3.63 C HETATM 4204 C20 P2E A1201 90.363 38.735 217.833 1.00 1.21 C HETATM 4205 O1 P2E A1201 80.546 37.591 225.705 1.00 32.91 O HETATM 4206 C1 P2E A1201 80.777 37.578 224.473 1.00 28.31 C HETATM 4207 O2 P2E A1201 79.954 38.082 223.676 1.00 36.48 O HETATM 4208 P POV A1202 70.717 38.346 228.420 1.00125.81 P HETATM 4209 C1 POV A1202 69.214 39.920 226.910 1.00 95.07 C HETATM 4210 C2 POV A1202 68.634 39.989 225.495 1.00 83.85 C HETATM 4211 C3 POV A1202 69.133 38.776 224.712 1.00 79.16 C HETATM 4212 C210 POV A1202 70.999 45.181 215.608 1.00 25.35 C HETATM 4213 C310 POV A1202 69.748 39.085 214.430 1.00 50.28 C HETATM 4214 O11 POV A1202 70.164 38.890 226.964 1.00114.40 O HETATM 4215 C211 POV A1202 70.592 44.267 214.452 1.00 26.55 C HETATM 4216 C311 POV A1202 69.381 40.492 213.964 1.00 40.97 C HETATM 4217 O12 POV A1202 69.511 37.594 229.253 1.00132.18 O HETATM 4218 C212 POV A1202 71.231 44.766 213.157 1.00 26.57 C HETATM 4219 C312 POV A1202 69.966 40.721 212.574 1.00 36.88 C HETATM 4220 O13 POV A1202 71.868 37.461 228.246 1.00123.43 O HETATM 4221 C213 POV A1202 70.424 44.262 211.961 1.00 28.72 C HETATM 4222 C313 POV A1202 69.123 39.979 211.540 1.00 35.16 C HETATM 4223 O14 POV A1202 71.312 39.427 229.204 1.00126.03 O HETATM 4224 C214 POV A1202 71.302 44.217 210.712 1.00 25.28 C HETATM 4225 C314 POV A1202 69.966 38.885 210.887 1.00 36.19 C HETATM 4226 C215 POV A1202 70.453 44.573 209.492 1.00 28.44 C HETATM 4227 C315 POV A1202 69.442 38.609 209.481 1.00 36.39 C HETATM 4228 C216 POV A1202 71.276 44.390 208.219 1.00 36.12 C HETATM 4229 C316 POV A1202 69.483 39.901 208.669 1.00 34.37 C HETATM 4230 C217 POV A1202 71.141 42.950 207.730 1.00 40.48 C HETATM 4231 C218 POV A1202 71.560 42.860 206.264 1.00 33.81 C HETATM 4232 C21 POV A1202 68.083 41.842 224.105 1.00 61.09 C HETATM 4233 O21 POV A1202 69.056 41.166 224.859 1.00 77.72 O HETATM 4234 C22 POV A1202 67.547 41.261 222.796 1.00 46.54 C HETATM 4235 O22 POV A1202 67.675 42.888 224.480 1.00 65.30 O HETATM 4236 C23 POV A1202 66.996 42.388 221.924 1.00 41.54 C HETATM 4237 C24 POV A1202 67.098 41.985 220.454 1.00 45.17 C HETATM 4238 C25 POV A1202 66.522 43.076 219.554 1.00 43.47 C HETATM 4239 C26 POV A1202 67.199 43.030 218.184 1.00 41.95 C HETATM 4240 C27 POV A1202 68.574 43.691 218.260 1.00 41.74 C HETATM 4241 C28 POV A1202 69.059 44.054 216.857 1.00 41.48 C HETATM 4242 C29 POV A1202 70.404 44.776 216.957 1.00 30.47 C HETATM 4243 C31 POV A1202 67.588 37.210 223.926 1.00 62.77 C HETATM 4244 O31 POV A1202 68.347 37.659 225.011 1.00 74.78 O HETATM 4245 C32 POV A1202 68.284 36.830 222.622 1.00 48.67 C HETATM 4246 O32 POV A1202 66.409 37.128 224.017 1.00 62.82 O HETATM 4247 C33 POV A1202 67.394 37.228 221.448 1.00 43.31 C HETATM 4248 C34 POV A1202 68.244 37.418 220.195 1.00 43.53 C HETATM 4249 C35 POV A1202 67.564 38.432 219.279 1.00 36.53 C HETATM 4250 C36 POV A1202 68.619 39.378 218.715 1.00 35.50 C HETATM 4251 C37 POV A1202 68.373 39.552 217.223 1.00 36.40 C HETATM 4252 C38 POV A1202 68.708 38.237 216.525 1.00 45.60 C HETATM 4253 C39 POV A1202 68.519 38.400 215.020 1.00 53.37 C CONECT 570 1142 CONECT 1142 570 CONECT 2601 3183 CONECT 3183 2601 CONECT 4112 4113 4135 CONECT 4113 4112 4114 CONECT 4114 4113 4115 CONECT 4115 4114 4116 CONECT 4116 4115 4117 CONECT 4117 4116 4118 CONECT 4118 4117 4119 4121 CONECT 4119 4118 4120 4124 CONECT 4120 4119 CONECT 4121 4118 4122 4125 CONECT 4122 4121 4123 4124 CONECT 4123 4122 CONECT 4124 4119 4122 CONECT 4125 4121 4126 CONECT 4126 4125 4127 CONECT 4127 4126 4128 4129 CONECT 4128 4127 CONECT 4129 4127 4130 CONECT 4130 4129 4131 CONECT 4131 4130 4132 CONECT 4132 4131 4133 CONECT 4133 4132 CONECT 4134 4135 CONECT 4135 4112 4134 4136 CONECT 4136 4135 CONECT 4137 4143 4146 4149 4152 CONECT 4138 4139 4143 CONECT 4139 4138 4140 4162 CONECT 4140 4139 4173 CONECT 4141 4144 4171 CONECT 4142 4145 4182 CONECT 4143 4137 4138 CONECT 4144 4141 4147 CONECT 4145 4142 4148 CONECT 4146 4137 CONECT 4147 4144 4150 CONECT 4148 4145 4151 CONECT 4149 4137 CONECT 4150 4147 4153 CONECT 4151 4148 4154 CONECT 4152 4137 CONECT 4153 4150 4155 CONECT 4154 4151 4156 CONECT 4155 4153 4157 CONECT 4156 4154 4158 CONECT 4157 4155 4159 CONECT 4158 4156 CONECT 4159 4157 4160 CONECT 4160 4159 CONECT 4161 4162 4163 4164 CONECT 4162 4139 4161 CONECT 4163 4161 4165 CONECT 4164 4161 CONECT 4165 4163 4166 CONECT 4166 4165 4167 CONECT 4167 4166 4168 CONECT 4168 4167 4169 CONECT 4169 4168 4170 CONECT 4170 4169 4171 CONECT 4171 4141 4170 CONECT 4172 4173 4174 4175 CONECT 4173 4140 4172 CONECT 4174 4172 4176 CONECT 4175 4172 CONECT 4176 4174 4177 CONECT 4177 4176 4178 CONECT 4178 4177 4179 CONECT 4179 4178 4180 CONECT 4180 4179 4181 CONECT 4181 4180 4182 CONECT 4182 4142 4181 CONECT 4183 4184 4206 CONECT 4184 4183 4185 CONECT 4185 4184 4186 CONECT 4186 4185 4187 CONECT 4187 4186 4188 CONECT 4188 4187 4189 CONECT 4189 4188 4190 4192 CONECT 4190 4189 4191 4195 CONECT 4191 4190 CONECT 4192 4189 4193 4196 CONECT 4193 4192 4194 4195 CONECT 4194 4193 CONECT 4195 4190 4193 CONECT 4196 4192 4197 CONECT 4197 4196 4198 CONECT 4198 4197 4199 4200 CONECT 4199 4198 CONECT 4200 4198 4201 CONECT 4201 4200 4202 CONECT 4202 4201 4203 CONECT 4203 4202 4204 CONECT 4204 4203 CONECT 4205 4206 CONECT 4206 4183 4205 4207 CONECT 4207 4206 CONECT 4208 4214 4217 4220 4223 CONECT 4209 4210 4214 CONECT 4210 4209 4211 4233 CONECT 4211 4210 4244 CONECT 4212 4215 4242 CONECT 4213 4216 4253 CONECT 4214 4208 4209 CONECT 4215 4212 4218 CONECT 4216 4213 4219 CONECT 4217 4208 CONECT 4218 4215 4221 CONECT 4219 4216 4222 CONECT 4220 4208 CONECT 4221 4218 4224 CONECT 4222 4219 4225 CONECT 4223 4208 CONECT 4224 4221 4226 CONECT 4225 4222 4227 CONECT 4226 4224 4228 CONECT 4227 4225 4229 CONECT 4228 4226 4230 CONECT 4229 4227 CONECT 4230 4228 4231 CONECT 4231 4230 CONECT 4232 4233 4234 4235 CONECT 4233 4210 4232 CONECT 4234 4232 4236 CONECT 4235 4232 CONECT 4236 4234 4237 CONECT 4237 4236 4238 CONECT 4238 4237 4239 CONECT 4239 4238 4240 CONECT 4240 4239 4241 CONECT 4241 4240 4242 CONECT 4242 4212 4241 CONECT 4243 4244 4245 4246 CONECT 4244 4211 4243 CONECT 4245 4243 4247 CONECT 4246 4243 CONECT 4247 4245 4248 CONECT 4248 4247 4249 CONECT 4249 4248 4250 CONECT 4250 4249 4251 CONECT 4251 4250 4252 CONECT 4252 4251 4253 CONECT 4253 4213 4252 MASTER 715 0 4 24 4 0 13 6 4251 2 146 66 END