HEADER MEMBRANE PROTEIN 03-FEB-17 5X33 TITLE LEUKOTRIENE B4 RECEPTOR BLT1 IN COMPLEX WITH BIIL260 COMPND MOL_ID: 1; COMPND 2 MOLECULE: LTB4 RECEPTOR,LYSOZYME,LTB4 RECEPTOR; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: LEUKOTRIENE B4 RECEPTOR; COMPND 5 EC: 3.2.1.17; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 OTHER_DETAILS: CHIMERA PROTEIN OF UNP RESIDUES 15-213 FROM Q9WTK1, COMPND 9 UNP RESIDUES 2-161 FROM A0A097J792, UNP RESIDUES 214-348 FROM Q9WTK1. SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CAVIA PORCELLUS, ENTEROBACTERIA PHAGE RB55; SOURCE 3 ORGANISM_COMMON: GUINEA PIG; SOURCE 4 ORGANISM_TAXID: 10141, 697289; SOURCE 5 GENE: LTB4R, E, RB55_P125; SOURCE 6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS CBS 7435; SOURCE 7 EXPRESSION_SYSTEM_COMMON: PICHIA PASTORIS; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 4922 KEYWDS HELIX, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR T.HORI,K.HIRATA,K.YAMASHITA,Y.KAWANO,M.YAMAMOTO,S.YOKOYAMA REVDAT 3 04-APR-18 5X33 1 JRNL REVDAT 2 07-FEB-18 5X33 1 JRNL REVDAT 1 03-JAN-18 5X33 0 JRNL AUTH T.HORI,T.OKUNO,K.HIRATA,K.YAMASHITA,Y.KAWANO,M.YAMAMOTO, JRNL AUTH 2 M.HATO,M.NAKAMURA,T.SHIMIZU,T.YOKOMIZO,M.MIYANO,S.YOKOYAMA JRNL TITL NA+-MIMICKING LIGANDS STABILIZE THE INACTIVE STATE OF JRNL TITL 2 LEUKOTRIENE B4RECEPTOR BLT1. JRNL REF NAT. CHEM. BIOL. V. 14 262 2018 JRNL REFN ESSN 1552-4469 JRNL PMID 29309055 JRNL DOI 10.1038/NCHEMBIO.2547 REMARK 2 REMARK 2 RESOLUTION. 3.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???) 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) : 3.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.54 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 8262 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.251 REMARK 3 R VALUE (WORKING SET) : 0.248 REMARK 3 FREE R VALUE : 0.296 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010 REMARK 3 FREE R VALUE TEST SET COUNT : 414 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 48.5434 - 5.3350 1.00 2712 143 0.2404 0.2816 REMARK 3 2 5.3350 - 4.2353 1.00 2594 137 0.2375 0.2664 REMARK 3 3 4.2353 - 3.7002 1.00 2542 134 0.2745 0.3533 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) : 0.480 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.650 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 : 0.005 3448 REMARK 3 ANGLE : 0.801 4693 REMARK 3 CHIRALITY : 0.042 556 REMARK 3 PLANARITY : 0.007 580 REMARK 3 DIHEDRAL : 15.004 2015 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 6 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 15 THROUGH 148 ) REMARK 3 ORIGIN FOR THE GROUP (A): 101.9104 183.8565 283.8529 REMARK 3 T TENSOR REMARK 3 T11: 0.0138 T22: 0.8497 REMARK 3 T33: 1.0676 T12: -0.1505 REMARK 3 T13: 0.0214 T23: 0.0277 REMARK 3 L TENSOR REMARK 3 L11: 2.4200 L22: 1.4328 REMARK 3 L33: 1.4670 L12: 0.6852 REMARK 3 L13: -1.0673 L23: -0.0161 REMARK 3 S TENSOR REMARK 3 S11: 0.0295 S12: 0.2746 S13: -0.5560 REMARK 3 S21: -0.4465 S22: 0.0836 S23: 0.2806 REMARK 3 S31: 0.0671 S32: -0.1825 S33: -0.0291 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 149 THROUGH 213 OR RESID 900 REMARK 3 THROUGH 1021 ) REMARK 3 ORIGIN FOR THE GROUP (A): 101.2925 183.0013 299.1973 REMARK 3 T TENSOR REMARK 3 T11: -0.0142 T22: 1.0935 REMARK 3 T33: 0.9258 T12: -0.0537 REMARK 3 T13: -0.0270 T23: 0.0508 REMARK 3 L TENSOR REMARK 3 L11: 1.6149 L22: 0.3542 REMARK 3 L33: 0.5280 L12: -0.1861 REMARK 3 L13: -0.5769 L23: -0.2662 REMARK 3 S TENSOR REMARK 3 S11: -0.0057 S12: -0.2322 S13: -0.3922 REMARK 3 S21: 0.1086 S22: -0.0609 S23: 0.1440 REMARK 3 S31: -0.1278 S32: 0.4489 S33: 0.0804 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1022 THROUGH 1136 ) REMARK 3 ORIGIN FOR THE GROUP (A): 74.7894 178.9009 319.7136 REMARK 3 T TENSOR REMARK 3 T11: 0.0163 T22: 0.7631 REMARK 3 T33: 1.1421 T12: 0.1067 REMARK 3 T13: 0.0407 T23: 0.1078 REMARK 3 L TENSOR REMARK 3 L11: 0.6544 L22: 0.5786 REMARK 3 L33: 0.6353 L12: -0.1516 REMARK 3 L13: 0.0209 L23: -0.4206 REMARK 3 S TENSOR REMARK 3 S11: 0.0104 S12: -0.0477 S13: 0.4890 REMARK 3 S21: 0.1199 S22: -0.0243 S23: -0.1988 REMARK 3 S31: -0.0985 S32: -0.3008 S33: 0.0113 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1137 THROUGH 1203 OR RESID 214 REMARK 3 THROUGH 229 ) REMARK 3 ORIGIN FOR THE GROUP (A): 73.0932 168.6446 312.5627 REMARK 3 T TENSOR REMARK 3 T11: 0.2732 T22: 0.7165 REMARK 3 T33: 0.8870 T12: -0.0334 REMARK 3 T13: -0.0067 T23: -0.0518 REMARK 3 L TENSOR REMARK 3 L11: 2.5785 L22: 1.0270 REMARK 3 L33: 0.3012 L12: 0.9608 REMARK 3 L13: -0.3155 L23: -0.5250 REMARK 3 S TENSOR REMARK 3 S11: -0.0086 S12: 0.3957 S13: 0.0206 REMARK 3 S21: -0.1560 S22: 0.3848 S23: -0.0535 REMARK 3 S31: 0.0685 S32: -0.5876 S33: -0.2568 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 230 THROUGH 287 ) REMARK 3 ORIGIN FOR THE GROUP (A): 112.2995 174.5409 291.0606 REMARK 3 T TENSOR REMARK 3 T11: 0.1132 T22: 0.8846 REMARK 3 T33: 1.3744 T12: 0.0211 REMARK 3 T13: 0.1005 T23: 0.3121 REMARK 3 L TENSOR REMARK 3 L11: 0.2302 L22: 1.5231 REMARK 3 L33: 4.3493 L12: -0.5823 REMARK 3 L13: -0.4163 L23: 0.4453 REMARK 3 S TENSOR REMARK 3 S11: 0.2272 S12: 0.3327 S13: -0.3091 REMARK 3 S21: 0.1911 S22: 0.0160 S23: -0.5314 REMARK 3 S31: 0.1246 S32: 0.5083 S33: -0.0980 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2001 THROUGH 2001 ) REMARK 3 ORIGIN FOR THE GROUP (A): 114.0156 178.7942 283.4466 REMARK 3 T TENSOR REMARK 3 T11: 0.4818 T22: 1.2104 REMARK 3 T33: 1.0363 T12: 0.2284 REMARK 3 T13: 0.2370 T23: -0.1439 REMARK 3 L TENSOR REMARK 3 L11: 8.2343 L22: 0.0158 REMARK 3 L33: 0.4652 L12: 0.3754 REMARK 3 L13: 1.9573 L23: 0.0901 REMARK 3 S TENSOR REMARK 3 S11: 0.0274 S12: -0.7150 S13: 0.8858 REMARK 3 S21: -0.2159 S22: 0.1442 S23: -1.0226 REMARK 3 S31: 0.1856 S32: 0.5857 S33: -0.1578 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 5X33 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-FEB-17. REMARK 100 THE DEPOSITION ID IS D_1300002841. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-OCT-16 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 : NULL REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8291 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.700 REMARK 200 RESOLUTION RANGE LOW (A) : 48.500 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 34.60 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.92 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 31.80 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: 4MBS AND 4K5Y REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 62.82 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.31 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 300, BICINE, LIPIDIC CUBIC PHASE, REMARK 280 TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 X,-Y,-Z REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 -X,-Y+1/2,Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.81000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 67.76500 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.81000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 67.76500 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: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 GLU A 2 REMARK 465 LEU A 3 REMARK 465 MET A 4 REMARK 465 ASP A 5 REMARK 465 TYR A 6 REMARK 465 LYS A 7 REMARK 465 ASP A 8 REMARK 465 ASP A 9 REMARK 465 ASP A 10 REMARK 465 ASP A 11 REMARK 465 LYS A 12 REMARK 465 GLU A 13 REMARK 465 PHE A 14 REMARK 465 THR A 254 REMARK 465 LEU A 255 REMARK 465 GLY A 288 REMARK 465 GLY A 289 REMARK 465 GLY A 290 REMARK 465 LEU A 291 REMARK 465 LEU A 292 REMARK 465 ARG A 293 REMARK 465 SER A 294 REMARK 465 ALA A 295 REMARK 465 GLY A 296 REMARK 465 VAL A 297 REMARK 465 GLY A 298 REMARK 465 PHE A 299 REMARK 465 VAL A 300 REMARK 465 ALA A 301 REMARK 465 LYS A 302 REMARK 465 LEU A 303 REMARK 465 LEU A 304 REMARK 465 GLU A 305 REMARK 465 ALA A 306 REMARK 465 THR A 307 REMARK 465 GLY A 308 REMARK 465 ALA A 309 REMARK 465 GLU A 310 REMARK 465 ALA A 311 REMARK 465 PHE A 312 REMARK 465 SER A 313 REMARK 465 THR A 314 REMARK 465 ARG A 315 REMARK 465 ARG A 316 REMARK 465 GLY A 317 REMARK 465 GLY A 318 REMARK 465 THR A 319 REMARK 465 LEU A 320 REMARK 465 ALA A 321 REMARK 465 GLN A 322 REMARK 465 THR A 323 REMARK 465 VAL A 324 REMARK 465 LYS A 325 REMARK 465 GLY A 326 REMARK 465 ILE A 327 REMARK 465 PRO A 328 REMARK 465 MET A 329 REMARK 465 ALA A 330 REMARK 465 PRO A 331 REMARK 465 GLU A 332 REMARK 465 PRO A 333 REMARK 465 GLY A 334 REMARK 465 ALA A 335 REMARK 465 SER A 336 REMARK 465 GLY A 337 REMARK 465 SER A 338 REMARK 465 LEU A 339 REMARK 465 ASP A 340 REMARK 465 GLY A 341 REMARK 465 LEU A 342 REMARK 465 LYS A 343 REMARK 465 GLN A 344 REMARK 465 SER A 345 REMARK 465 GLU A 346 REMARK 465 SER A 347 REMARK 465 ASP A 348 REMARK 465 GLU A 349 REMARK 465 PHE A 350 REMARK 465 LEU A 351 REMARK 465 GLU A 352 REMARK 465 VAL A 353 REMARK 465 LEU A 354 REMARK 465 PHE A 355 REMARK 465 GLN A 356 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 LYS A 47 CG CD CE NZ REMARK 470 ARG A 48 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 50 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 51 CG CD CE NZ REMARK 470 LYS A 133 CG CD CE NZ REMARK 470 ARG A 211 CG CD NE CZ NH1 NH2 REMARK 470 ARG A1014 CG CD NE CZ NH1 NH2 REMARK 470 LYS A1016 CG CD CE NZ REMARK 470 ASP A1020 CG OD1 OD2 REMARK 470 THR A1021 OG1 CG2 REMARK 470 GLU A1022 CG CD OE1 OE2 REMARK 470 TYR A1024 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS A1043 CG CD CE NZ REMARK 470 LYS A1048 CG CD CE NZ REMARK 470 ARG A1080 CG CD NE CZ NH1 NH2 REMARK 470 LYS A1147 CG CD CE NZ REMARK 470 ARG A 217 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 218 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 256 CG OD1 OD2 REMARK 470 GLN A 257 CG CD OE1 NE2 REMARK 470 LYS A 259 CG CD CE NZ REMARK 470 GLN A 260 CG CD OE1 NE2 REMARK 470 ASN A 264 CG OD1 ND2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O LEU A 35 OG1 THR A 39 2.03 REMARK 500 OG SER A 903 OE1 GLU A 1064 2.12 REMARK 500 OG SER A 1038 OD1 ASN A 1040 2.19 REMARK 500 O LEU A 149 OG1 THR A 152 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ARG A 117 -7.03 -59.11 REMARK 500 ASP A1010 -60.12 -98.92 REMARK 500 ASP A1020 -179.97 -69.13 REMARK 500 ALA A1112 -8.82 -55.21 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 7Y9 A 2001 DBREF 5X33 A 15 213 UNP Q9WTK1 Q9WTK1_CAVPO 15 213 DBREF1 5X33 A 1002 1161 UNP A0A097J792_BPT4 DBREF2 5X33 A A0A097J792 2 161 DBREF 5X33 A 214 348 UNP Q9WTK1 Q9WTK1_CAVPO 214 348 SEQADV 5X33 GLU A 2 UNP Q9WTK1 EXPRESSION TAG SEQADV 5X33 LEU A 3 UNP Q9WTK1 EXPRESSION TAG SEQADV 5X33 MET A 4 UNP Q9WTK1 EXPRESSION TAG SEQADV 5X33 ASP A 5 UNP Q9WTK1 EXPRESSION TAG SEQADV 5X33 TYR A 6 UNP Q9WTK1 EXPRESSION TAG SEQADV 5X33 LYS A 7 UNP Q9WTK1 EXPRESSION TAG SEQADV 5X33 ASP A 8 UNP Q9WTK1 EXPRESSION TAG SEQADV 5X33 ASP A 9 UNP Q9WTK1 EXPRESSION TAG SEQADV 5X33 ASP A 10 UNP Q9WTK1 EXPRESSION TAG SEQADV 5X33 ASP A 11 UNP Q9WTK1 EXPRESSION TAG SEQADV 5X33 LYS A 12 UNP Q9WTK1 EXPRESSION TAG SEQADV 5X33 GLU A 13 UNP Q9WTK1 EXPRESSION TAG SEQADV 5X33 PHE A 14 UNP Q9WTK1 EXPRESSION TAG SEQADV 5X33 GLY A 83 UNP Q9WTK1 HIS 83 ENGINEERED MUTATION SEQADV 5X33 GLY A 88 UNP Q9WTK1 LYS 88 ENGINEERED MUTATION SEQADV 5X33 ALA A 212 UNP Q9WTK1 VAL 212 ENGINEERED MUTATION SEQADV 5X33 GLY A 900 UNP Q9WTK1 LINKER SEQADV 5X33 SER A 901 UNP Q9WTK1 LINKER SEQADV 5X33 GLY A 902 UNP Q9WTK1 LINKER SEQADV 5X33 SER A 903 UNP Q9WTK1 LINKER SEQADV 5X33 THR A 1054 UNP A0A097J79 CYS 54 ENGINEERED MUTATION SEQADV 5X33 ALA A 1097 UNP A0A097J79 CYS 97 ENGINEERED MUTATION SEQADV 5X33 GLY A 1200 UNP A0A097J79 LINKER SEQADV 5X33 SER A 1201 UNP A0A097J79 LINKER SEQADV 5X33 GLY A 1202 UNP A0A097J79 LINKER SEQADV 5X33 SER A 1203 UNP A0A097J79 LINKER SEQADV 5X33 ALA A 309 UNP Q9WTK1 SER 309 ENGINEERED MUTATION SEQADV 5X33 GLU A 349 UNP Q9WTK1 EXPRESSION TAG SEQADV 5X33 PHE A 350 UNP Q9WTK1 EXPRESSION TAG SEQADV 5X33 LEU A 351 UNP Q9WTK1 EXPRESSION TAG SEQADV 5X33 GLU A 352 UNP Q9WTK1 EXPRESSION TAG SEQADV 5X33 VAL A 353 UNP Q9WTK1 EXPRESSION TAG SEQADV 5X33 LEU A 354 UNP Q9WTK1 EXPRESSION TAG SEQADV 5X33 PHE A 355 UNP Q9WTK1 EXPRESSION TAG SEQADV 5X33 GLN A 356 UNP Q9WTK1 EXPRESSION TAG SEQRES 1 A 523 GLU LEU MET ASP TYR LYS ASP ASP ASP ASP LYS GLU PHE SEQRES 2 A 523 SER ASN THR PHE ILE PRO LEU LEU ALA MET ILE LEU LEU SEQRES 3 A 523 SER VAL SER MET VAL VAL GLY LEU PRO GLY ASN THR PHE SEQRES 4 A 523 VAL VAL TRP SER ILE LEU LYS ARG MET ARG LYS ARG SER SEQRES 5 A 523 VAL THR ALA LEU MET VAL LEU ASN LEU ALA LEU ALA ASP SEQRES 6 A 523 LEU ALA VAL LEU LEU THR ALA PRO PHE PHE LEU HIS PHE SEQRES 7 A 523 LEU THR TRP GLY THR TRP SER PHE GLY LEU ALA GLY CYS SEQRES 8 A 523 ARG LEU CYS HIS TYR ILE CYS GLY VAL SER MET TYR ALA SEQRES 9 A 523 SER VAL LEU LEU ILE THR ALA MET SER LEU ASP ARG SER SEQRES 10 A 523 LEU ALA VAL ALA SER PRO PHE LEU SER GLN LYS VAL ARG SEQRES 11 A 523 THR LYS THR ALA ALA ARG TRP LEU LEU VAL GLY ILE TRP SEQRES 12 A 523 GLY ALA SER PHE LEU LEU ALA THR PRO VAL LEU ALA PHE SEQRES 13 A 523 ARG LYS VAL VAL LYS LEU THR ASN GLU THR ASP LEU CYS SEQRES 14 A 523 LEU ALA VAL TYR PRO SER ASP ARG HIS LYS ALA PHE HIS SEQRES 15 A 523 LEU LEU PHE GLU ALA PHE THR GLY PHE VAL VAL PRO PHE SEQRES 16 A 523 LEU ILE VAL VAL ALA SER TYR ALA ASP ILE SER ARG ARG SEQRES 17 A 523 LEU ARG ALA ARG GLY SER GLY SER ASN ILE PHE GLU MET SEQRES 18 A 523 LEU ARG ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS SEQRES 19 A 523 ASP THR GLU GLY TYR TYR THR ILE GLY ILE GLY HIS LEU SEQRES 20 A 523 LEU THR LYS SER PRO SER LEU ASN ALA ALA LYS SER GLU SEQRES 21 A 523 LEU ASP LYS ALA ILE GLY ARG ASN THR ASN GLY VAL ILE SEQRES 22 A 523 THR LYS ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL SEQRES 23 A 523 ASP ALA ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU SEQRES 24 A 523 LYS PRO VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA SEQRES 25 A 523 ALA LEU ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY SEQRES 26 A 523 VAL ALA GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN SEQRES 27 A 523 LYS ARG TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER SEQRES 28 A 523 ARG TRP TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL SEQRES 29 A 523 ILE THR THR PHE ARG THR GLY THR TRP ASP ALA TYR GLY SEQRES 30 A 523 SER GLY SER ARG PHE HIS ARG ARG ARG ARG THR GLY ARG SEQRES 31 A 523 LEU VAL VAL ILE ILE ILE LEU ALA PHE ALA ALA PHE TRP SEQRES 32 A 523 LEU PRO TYR HIS VAL VAL ASP LEU VAL GLU GLY SER ARG SEQRES 33 A 523 VAL LEU ALA GLY THR LEU ASP GLN SER LYS GLN GLN LEU SEQRES 34 A 523 ARG ASN ALA ARG LYS VAL CYS ILE ALA LEU ALA PHE LEU SEQRES 35 A 523 SER SER SER VAL ASN PRO LEU LEU TYR ALA CYS ALA GLY SEQRES 36 A 523 GLY GLY LEU LEU ARG SER ALA GLY VAL GLY PHE VAL ALA SEQRES 37 A 523 LYS LEU LEU GLU ALA THR GLY ALA GLU ALA PHE SER THR SEQRES 38 A 523 ARG ARG GLY GLY THR LEU ALA GLN THR VAL LYS GLY ILE SEQRES 39 A 523 PRO MET ALA PRO GLU PRO GLY ALA SER GLY SER LEU ASP SEQRES 40 A 523 GLY LEU LYS GLN SER GLU SER ASP GLU PHE LEU GLU VAL SEQRES 41 A 523 LEU PHE GLN HET 7Y9 A2001 35 HETNAM 7Y9 4-[[3-[[4-[2-(4-HYDROXYPHENYL)PROPAN-2- HETNAM 2 7Y9 YL]PHENOXY]METHYL]PHENYL]METHOXY]BENZENECARBOXIMIDAMID HETNAM 3 7Y9 E FORMUL 2 7Y9 C30 H30 N2 O3 HELIX 1 AA1 THR A 17 ARG A 48 1 32 HELIX 2 AA2 VAL A 54 GLY A 83 1 30 HELIX 3 AA3 PHE A 87 ARG A 117 1 31 HELIX 4 AA4 SER A 118 SER A 123 1 6 HELIX 5 AA5 SER A 123 ARG A 131 1 9 HELIX 6 AA6 THR A 132 LEU A 149 1 18 HELIX 7 AA7 THR A 152 PHE A 157 1 6 HELIX 8 AA8 SER A 176 THR A 190 1 15 HELIX 9 AA9 PHE A 192 GLY A 900 1 23 HELIX 10 AB1 SER A 903 GLY A 1012 1 12 HELIX 11 AB2 SER A 1038 ALA A 1049 1 12 HELIX 12 AB3 THR A 1059 ARG A 1080 1 22 HELIX 13 AB4 LYS A 1083 LEU A 1091 1 9 HELIX 14 AB5 ASP A 1092 GLY A 1107 1 16 HELIX 15 AB6 GLY A 1107 ALA A 1112 1 6 HELIX 16 AB7 PHE A 1114 GLN A 1123 1 10 HELIX 17 AB8 TRP A 1126 VAL A 1131 1 6 HELIX 18 AB9 ASN A 1132 LYS A 1135 5 4 HELIX 19 AC1 SER A 1136 THR A 1142 1 7 HELIX 20 AC2 THR A 1142 GLY A 1156 1 15 HELIX 21 AC3 THR A 221 VAL A 226 1 6 HELIX 22 AC4 ILE A 229 ARG A 249 1 21 HELIX 23 AC5 GLN A 260 ALA A 273 1 14 HELIX 24 AC6 PHE A 274 SER A 278 5 5 HELIX 25 AC7 VAL A 279 ALA A 285 1 7 SHEET 1 AA1 2 ARG A 158 THR A 164 0 SHEET 2 AA1 2 THR A 167 ALA A 172 -1 O THR A 167 N THR A 164 SHEET 1 AA2 3 TYR A1018 LYS A1019 0 SHEET 2 AA2 3 TYR A1025 ILE A1027 -1 O THR A1026 N TYR A1018 SHEET 3 AA2 3 HIS A1031 LEU A1032 -1 O HIS A1031 N ILE A1027 SSBOND 1 CYS A 92 CYS A 170 1555 1555 2.02 SITE 1 AC1 15 ASP A 66 VAL A 69 PHE A 76 LEU A 80 SITE 2 AC1 15 HIS A 96 CYS A 99 SER A 102 MET A 103 SITE 3 AC1 15 SER A 106 TRP A 236 LYS A 267 ILE A 270 SITE 4 AC1 15 ALA A 273 SER A 276 SER A 277 CRYST1 69.560 77.620 135.530 90.00 90.00 90.00 P 2 21 21 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 0.014376 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012883 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007378 0.00000 ATOM 1 N SER A 15 126.586 161.341 282.733 1.00 89.58 N ANISOU 1 N SER A 15 5360 9594 19084 300 2537 -121 N ATOM 2 CA SER A 15 125.426 162.085 283.211 1.00100.26 C ANISOU 2 CA SER A 15 6826 11157 20112 208 2343 -56 C ATOM 3 C SER A 15 125.503 163.553 282.795 1.00101.33 C ANISOU 3 C SER A 15 7087 11654 19759 121 2227 -179 C ATOM 4 O SER A 15 124.624 164.350 283.136 1.00 98.95 O ANISOU 4 O SER A 15 6891 11562 19142 43 2067 -136 O ATOM 5 CB SER A 15 125.306 161.972 284.733 1.00 96.81 C ANISOU 5 CB SER A 15 6346 10821 19616 291 2200 311 C ATOM 6 OG SER A 15 124.248 162.776 285.228 1.00 92.16 O ANISOU 6 OG SER A 15 5874 10457 18684 201 2019 364 O ATOM 7 N ASN A 16 126.564 163.905 282.061 1.00105.16 N ANISOU 7 N ASN A 16 7561 12202 20194 135 2318 -328 N ATOM 8 CA ASN A 16 126.709 165.265 281.551 1.00104.00 C ANISOU 8 CA ASN A 16 7528 12363 19623 50 2239 -453 C ATOM 9 C ASN A 16 125.727 165.568 280.423 1.00101.76 C ANISOU 9 C ASN A 16 7350 12034 19282 -98 2270 -733 C ATOM 10 O ASN A 16 125.412 166.740 280.187 1.00 98.21 O ANISOU 10 O ASN A 16 7013 11841 18461 -181 2162 -780 O ATOM 11 CB ASN A 16 128.144 165.502 281.060 1.00106.18 C ANISOU 11 CB ASN A 16 7754 12704 19887 104 2343 -533 C ATOM 12 CG ASN A 16 129.020 166.195 282.096 1.00104.15 C ANISOU 12 CG ASN A 16 7461 12752 19358 182 2214 -294 C ATOM 13 OD1 ASN A 16 128.796 166.078 283.302 1.00104.92 O ANISOU 13 OD1 ASN A 16 7524 12932 19408 234 2091 -45 O ATOM 14 ND2 ASN A 16 130.027 166.925 281.623 1.00101.62 N ANISOU 14 ND2 ASN A 16 7146 12606 18858 178 2249 -386 N ATOM 15 N THR A 17 125.234 164.538 279.730 1.00101.59 N ANISOU 15 N THR A 17 7287 11691 19623 -137 2419 -923 N ATOM 16 CA THR A 17 124.395 164.713 278.552 1.00 97.75 C ANISOU 16 CA THR A 17 6875 11158 19107 -289 2473 -1235 C ATOM 17 C THR A 17 122.899 164.589 278.830 1.00 92.90 C ANISOU 17 C THR A 17 6303 10517 18476 -371 2360 -1205 C ATOM 18 O THR A 17 122.097 165.093 278.034 1.00 89.43 O ANISOU 18 O THR A 17 5943 10160 17876 -505 2330 -1408 O ATOM 19 CB THR A 17 124.788 163.694 277.470 1.00100.34 C ANISOU 19 CB THR A 17 7131 11166 19829 -317 2734 -1540 C ATOM 20 OG1 THR A 17 125.238 162.477 278.085 1.00102.15 O ANISOU 20 OG1 THR A 17 7233 11113 20466 -191 2841 -1393 O ATOM 21 CG2 THR A 17 125.894 164.244 276.585 1.00 85.87 C ANISOU 21 CG2 THR A 17 5320 9432 17876 -330 2846 -1729 C ATOM 22 N PHE A 18 122.499 163.952 279.932 1.00 92.93 N ANISOU 22 N PHE A 18 6255 10422 18633 -296 2296 -953 N ATOM 23 CA PHE A 18 121.091 163.626 280.144 1.00 93.25 C ANISOU 23 CA PHE A 18 6319 10384 18729 -374 2223 -945 C ATOM 24 C PHE A 18 120.323 164.725 280.870 1.00 91.57 C ANISOU 24 C PHE A 18 6214 10486 18091 -407 1989 -762 C ATOM 25 O PHE A 18 119.104 164.838 280.687 1.00 91.83 O ANISOU 25 O PHE A 18 6300 10535 18057 -508 1915 -829 O ATOM 26 CB PHE A 18 120.976 162.294 280.896 1.00 83.79 C ANISOU 26 CB PHE A 18 5007 8877 17953 -288 2301 -783 C ATOM 27 CG PHE A 18 120.412 162.411 282.284 1.00 82.51 C ANISOU 27 CG PHE A 18 4858 8826 17665 -236 2127 -449 C ATOM 28 CD1 PHE A 18 119.120 161.990 282.555 1.00 82.48 C ANISOU 28 CD1 PHE A 18 4866 8717 17755 -302 2078 -426 C ATOM 29 CD2 PHE A 18 121.180 162.913 283.325 1.00 89.13 C ANISOU 29 CD2 PHE A 18 5694 9878 18295 -129 2022 -173 C ATOM 30 CE1 PHE A 18 118.599 162.084 283.830 1.00 81.43 C ANISOU 30 CE1 PHE A 18 4749 8684 17508 -261 1933 -131 C ATOM 31 CE2 PHE A 18 120.661 163.016 284.599 1.00 80.54 C ANISOU 31 CE2 PHE A 18 4619 8899 17083 -96 1878 106 C ATOM 32 CZ PHE A 18 119.370 162.598 284.853 1.00 80.48 C ANISOU 32 CZ PHE A 18 4630 8776 17172 -160 1837 131 C ATOM 33 N ILE A 19 120.999 165.533 281.693 1.00 76.85 N ANISOU 33 N ILE A 19 4382 8875 15942 -331 1879 -544 N ATOM 34 CA ILE A 19 120.348 166.719 282.249 1.00 73.96 C ANISOU 34 CA ILE A 19 4131 8820 15150 -378 1687 -423 C ATOM 35 C ILE A 19 120.002 167.722 281.162 1.00 91.98 C ANISOU 35 C ILE A 19 6514 11260 17175 -492 1663 -637 C ATOM 36 O ILE A 19 118.862 168.225 281.156 1.00 91.61 O ANISOU 36 O ILE A 19 6544 11315 16948 -575 1551 -639 O ATOM 37 CB ILE A 19 121.223 167.321 283.376 1.00 72.94 C ANISOU 37 CB ILE A 19 4002 8924 14788 -285 1599 -181 C ATOM 38 CG1 ILE A 19 121.031 166.545 284.680 1.00 73.81 C ANISOU 38 CG1 ILE A 19 4043 8946 15057 -206 1558 73 C ATOM 39 CG2 ILE A 19 120.904 168.797 283.570 1.00 70.06 C ANISOU 39 CG2 ILE A 19 3766 8898 13956 -350 1455 -152 C ATOM 40 CD1 ILE A 19 119.973 167.129 285.603 1.00 81.08 C ANISOU 40 CD1 ILE A 19 5050 10044 15713 -253 1398 214 C ATOM 41 N PRO A 20 120.887 168.057 280.212 1.00 90.23 N ANISOU 41 N PRO A 20 6293 11063 16926 -506 1765 -816 N ATOM 42 CA PRO A 20 120.427 168.841 279.054 1.00 88.17 C ANISOU 42 CA PRO A 20 6115 10905 16479 -630 1762 -1042 C ATOM 43 C PRO A 20 119.349 168.135 278.251 1.00 73.22 C ANISOU 43 C PRO A 20 4203 8828 14790 -740 1812 -1261 C ATOM 44 O PRO A 20 118.482 168.800 277.672 1.00 72.13 O ANISOU 44 O PRO A 20 4135 8817 14453 -850 1735 -1364 O ATOM 45 CB PRO A 20 121.708 169.046 278.232 1.00 87.97 C ANISOU 45 CB PRO A 20 6072 10884 16467 -616 1904 -1202 C ATOM 46 CG PRO A 20 122.810 168.940 279.227 1.00 88.21 C ANISOU 46 CG PRO A 20 6046 10958 16512 -480 1898 -978 C ATOM 47 CD PRO A 20 122.356 167.895 280.204 1.00 90.01 C ANISOU 47 CD PRO A 20 6199 11015 16987 -412 1872 -803 C ATOM 48 N LEU A 21 119.374 166.800 278.210 1.00 75.65 N ANISOU 48 N LEU A 21 4408 8838 15496 -718 1942 -1336 N ATOM 49 CA LEU A 21 118.323 166.048 277.531 1.00 77.07 C ANISOU 49 CA LEU A 21 4559 8837 15886 -836 1995 -1556 C ATOM 50 C LEU A 21 116.987 166.186 278.255 1.00 92.66 C ANISOU 50 C LEU A 21 6574 10886 17748 -869 1819 -1388 C ATOM 51 O LEU A 21 115.937 166.317 277.615 1.00 93.74 O ANISOU 51 O LEU A 21 6741 11060 17815 -1000 1770 -1546 O ATOM 52 CB LEU A 21 118.749 164.580 277.411 1.00 80.16 C ANISOU 52 CB LEU A 21 4829 8869 16758 -796 2199 -1661 C ATOM 53 CG LEU A 21 117.808 163.457 276.956 1.00 82.34 C ANISOU 53 CG LEU A 21 5043 8878 17366 -900 2299 -1867 C ATOM 54 CD1 LEU A 21 116.981 162.910 278.118 1.00 82.19 C ANISOU 54 CD1 LEU A 21 4996 8763 17469 -848 2198 -1604 C ATOM 55 CD2 LEU A 21 116.914 163.901 275.804 1.00 82.10 C ANISOU 55 CD2 LEU A 21 5070 8972 17154 -1094 2270 -2168 C ATOM 56 N LEU A 22 117.002 166.154 279.589 1.00 90.38 N ANISOU 56 N LEU A 22 6284 10631 17427 -760 1724 -1076 N ATOM 57 CA LEU A 22 115.755 166.279 280.337 1.00 88.56 C ANISOU 57 CA LEU A 22 6094 10470 17085 -791 1572 -919 C ATOM 58 C LEU A 22 115.195 167.694 280.246 1.00 71.01 C ANISOU 58 C LEU A 22 3991 8565 14425 -851 1412 -882 C ATOM 59 O LEU A 22 113.981 167.881 280.110 1.00 70.45 O ANISOU 59 O LEU A 22 3956 8548 14263 -939 1318 -911 O ATOM 60 CB LEU A 22 115.976 165.866 281.797 1.00 87.99 C ANISOU 60 CB LEU A 22 5987 10358 17087 -668 1532 -611 C ATOM 61 CG LEU A 22 114.791 165.836 282.772 1.00 85.96 C ANISOU 61 CG LEU A 22 5761 10143 16755 -684 1402 -428 C ATOM 62 CD1 LEU A 22 114.980 164.731 283.799 1.00 74.35 C ANISOU 62 CD1 LEU A 22 4199 8456 15595 -588 1456 -228 C ATOM 63 CD2 LEU A 22 114.622 167.175 283.477 1.00 82.16 C ANISOU 63 CD2 LEU A 22 5393 9998 15825 -677 1241 -266 C ATOM 64 N ALA A 23 116.059 168.706 280.323 1.00 69.52 N ANISOU 64 N ALA A 23 3859 8585 13972 -805 1384 -815 N ATOM 65 CA ALA A 23 115.571 170.079 280.306 1.00 67.14 C ANISOU 65 CA ALA A 23 3667 8564 13280 -852 1250 -760 C ATOM 66 C ALA A 23 115.060 170.498 278.935 1.00 67.30 C ANISOU 66 C ALA A 23 3715 8624 13233 -976 1259 -1003 C ATOM 67 O ALA A 23 114.313 171.477 278.843 1.00 65.72 O ANISOU 67 O ALA A 23 3589 8613 12768 -1029 1142 -959 O ATOM 68 CB ALA A 23 116.669 171.036 280.770 1.00 65.72 C ANISOU 68 CB ALA A 23 3534 8584 12852 -779 1233 -632 C ATOM 69 N MET A 24 115.439 169.790 277.871 1.00 74.60 N ANISOU 69 N MET A 24 4575 9380 14390 -1030 1402 -1266 N ATOM 70 CA MET A 24 115.030 170.174 276.527 1.00 75.01 C ANISOU 70 CA MET A 24 4647 9495 14358 -1167 1420 -1529 C ATOM 71 C MET A 24 113.726 169.527 276.091 1.00 70.97 C ANISOU 71 C MET A 24 4100 8896 13968 -1288 1383 -1671 C ATOM 72 O MET A 24 113.129 169.979 275.107 1.00 71.14 O ANISOU 72 O MET A 24 4145 9032 13854 -1417 1344 -1851 O ATOM 73 CB MET A 24 116.125 169.827 275.513 1.00 71.51 C ANISOU 73 CB MET A 24 4161 8952 14057 -1192 1611 -1793 C ATOM 74 CG MET A 24 116.309 168.336 275.300 1.00 74.22 C ANISOU 74 CG MET A 24 4399 8992 14808 -1200 1775 -1963 C ATOM 75 SD MET A 24 117.790 167.905 274.365 1.00116.52 S ANISOU 75 SD MET A 24 9706 14216 20350 -1194 2028 -2231 S ATOM 76 CE MET A 24 117.221 168.103 272.680 1.00118.05 C ANISOU 76 CE MET A 24 9922 14491 20440 -1424 2096 -2655 C ATOM 77 N ILE A 25 113.273 168.481 276.784 1.00 71.96 N ANISOU 77 N ILE A 25 4168 8831 14343 -1258 1393 -1595 N ATOM 78 CA ILE A 25 111.956 167.929 276.488 1.00 85.77 C ANISOU 78 CA ILE A 25 5890 10516 16183 -1377 1340 -1704 C ATOM 79 C ILE A 25 110.876 168.674 277.264 1.00 84.31 C ANISOU 79 C ILE A 25 5769 10516 15749 -1367 1142 -1463 C ATOM 80 O ILE A 25 109.877 169.115 276.685 1.00 83.62 O ANISOU 80 O ILE A 25 5703 10557 15510 -1478 1039 -1542 O ATOM 81 CB ILE A 25 111.915 166.411 276.760 1.00 75.35 C ANISOU 81 CB ILE A 25 4474 8879 15278 -1368 1467 -1767 C ATOM 82 CG1 ILE A 25 112.625 166.051 278.063 1.00 74.94 C ANISOU 82 CG1 ILE A 25 4398 8721 15355 -1195 1494 -1483 C ATOM 83 CG2 ILE A 25 112.527 165.650 275.600 1.00 80.35 C ANISOU 83 CG2 ILE A 25 5043 9332 16156 -1453 1671 -2117 C ATOM 84 CD1 ILE A 25 112.596 164.567 278.378 1.00 77.41 C ANISOU 84 CD1 ILE A 25 4607 8699 16107 -1172 1628 -1511 C ATOM 85 N LEU A 26 111.069 168.850 278.575 1.00 84.04 N ANISOU 85 N LEU A 26 5763 10511 15656 -1240 1090 -1174 N ATOM 86 CA LEU A 26 110.095 169.578 279.385 1.00 67.68 C ANISOU 86 CA LEU A 26 3758 8616 13341 -1230 930 -961 C ATOM 87 C LEU A 26 109.805 170.948 278.790 1.00 66.10 C ANISOU 87 C LEU A 26 3632 8671 12811 -1280 832 -973 C ATOM 88 O LEU A 26 108.642 171.341 278.638 1.00 65.70 O ANISOU 88 O LEU A 26 3601 8726 12635 -1351 719 -959 O ATOM 89 CB LEU A 26 110.603 169.727 280.820 1.00 70.27 C ANISOU 89 CB LEU A 26 4117 8981 13601 -1098 910 -690 C ATOM 90 CG LEU A 26 111.057 168.480 281.576 1.00 67.91 C ANISOU 90 CG LEU A 26 3740 8444 13620 -1021 1003 -614 C ATOM 91 CD1 LEU A 26 111.341 168.828 283.028 1.00 66.52 C ANISOU 91 CD1 LEU A 26 3603 8374 13296 -918 946 -344 C ATOM 92 CD2 LEU A 26 110.020 167.377 281.471 1.00 69.70 C ANISOU 92 CD2 LEU A 26 3899 8464 14120 -1092 1022 -693 C ATOM 93 N LEU A 27 110.861 171.686 278.437 1.00 65.34 N ANISOU 93 N LEU A 27 3572 8670 12584 -1243 879 -994 N ATOM 94 CA LEU A 27 110.678 172.991 277.814 1.00 64.06 C ANISOU 94 CA LEU A 27 3474 8725 12142 -1288 807 -1005 C ATOM 95 C LEU A 27 109.959 172.880 276.480 1.00 65.48 C ANISOU 95 C LEU A 27 3616 8913 12352 -1432 790 -1250 C ATOM 96 O LEU A 27 109.285 173.826 276.066 1.00 64.71 O ANISOU 96 O LEU A 27 3551 8989 12047 -1485 687 -1228 O ATOM 97 CB LEU A 27 112.028 173.686 277.624 1.00 83.88 C ANISOU 97 CB LEU A 27 6021 11307 14543 -1231 886 -1007 C ATOM 98 CG LEU A 27 112.462 174.712 278.676 1.00 82.32 C ANISOU 98 CG LEU A 27 5903 11273 14103 -1135 834 -758 C ATOM 99 CD1 LEU A 27 112.535 174.071 280.054 1.00 82.92 C ANISOU 99 CD1 LEU A 27 5967 11288 14252 -1050 823 -584 C ATOM 100 CD2 LEU A 27 113.797 175.351 278.305 1.00 60.79 C ANISOU 100 CD2 LEU A 27 3202 8609 11288 -1100 920 -796 C ATOM 101 N SER A 28 110.088 171.745 275.795 1.00 67.73 N ANISOU 101 N SER A 28 3826 9018 12892 -1505 894 -1492 N ATOM 102 CA SER A 28 109.376 171.537 274.541 1.00 69.42 C ANISOU 102 CA SER A 28 4002 9258 13117 -1672 877 -1762 C ATOM 103 C SER A 28 107.970 170.989 274.747 1.00 82.77 C ANISOU 103 C SER A 28 5657 10917 14873 -1744 768 -1742 C ATOM 104 O SER A 28 107.065 171.336 273.978 1.00 85.10 O ANISOU 104 O SER A 28 5946 11348 15041 -1867 664 -1845 O ATOM 105 CB SER A 28 110.168 170.601 273.627 1.00 87.46 C ANISOU 105 CB SER A 28 6229 11377 15623 -1746 1060 -2082 C ATOM 106 OG SER A 28 110.251 169.300 274.174 1.00 83.73 O ANISOU 106 OG SER A 28 5695 10647 15473 -1709 1156 -2094 O ATOM 107 N VAL A 29 107.748 170.148 275.762 1.00 80.22 N ANISOU 107 N VAL A 29 5310 10430 14741 -1677 786 -1610 N ATOM 108 CA VAL A 29 106.372 169.739 276.028 1.00 78.71 C ANISOU 108 CA VAL A 29 5093 10229 14585 -1744 680 -1570 C ATOM 109 C VAL A 29 105.589 170.913 276.594 1.00 68.73 C ANISOU 109 C VAL A 29 3890 9191 13034 -1702 517 -1324 C ATOM 110 O VAL A 29 104.381 171.031 276.360 1.00 81.24 O ANISOU 110 O VAL A 29 5456 10865 14547 -1789 399 -1330 O ATOM 111 CB VAL A 29 106.299 168.508 276.956 1.00 78.46 C ANISOU 111 CB VAL A 29 5014 9953 14845 -1691 755 -1500 C ATOM 112 CG1 VAL A 29 107.345 167.464 276.573 1.00 73.75 C ANISOU 112 CG1 VAL A 29 4357 9109 14555 -1687 950 -1694 C ATOM 113 CG2 VAL A 29 106.415 168.899 278.424 1.00 75.92 C ANISOU 113 CG2 VAL A 29 4743 9673 14429 -1540 710 -1173 C ATOM 114 N SER A 30 106.254 171.810 277.326 1.00 66.58 N ANISOU 114 N SER A 30 3688 9020 12591 -1577 513 -1117 N ATOM 115 CA SER A 30 105.576 173.013 277.784 1.00 64.68 C ANISOU 115 CA SER A 30 3508 8992 12075 -1546 386 -916 C ATOM 116 C SER A 30 105.231 173.926 276.619 1.00 64.80 C ANISOU 116 C SER A 30 3521 9177 11924 -1632 310 -1014 C ATOM 117 O SER A 30 104.262 174.686 276.697 1.00 66.58 O ANISOU 117 O SER A 30 3757 9553 11988 -1648 190 -899 O ATOM 118 CB SER A 30 106.433 173.749 278.806 1.00 62.60 C ANISOU 118 CB SER A 30 3323 8799 11663 -1413 416 -711 C ATOM 119 OG SER A 30 106.242 173.205 280.098 1.00 62.21 O ANISOU 119 OG SER A 30 3284 8677 11677 -1345 423 -563 O ATOM 120 N MET A 31 106.000 173.861 275.530 1.00 65.85 N ANISOU 120 N MET A 31 3634 9291 12095 -1691 384 -1233 N ATOM 121 CA MET A 31 105.648 174.626 274.337 1.00 66.39 C ANISOU 121 CA MET A 31 3690 9527 12009 -1794 312 -1361 C ATOM 122 C MET A 31 104.438 174.021 273.640 1.00 68.39 C ANISOU 122 C MET A 31 3873 9797 12315 -1942 216 -1517 C ATOM 123 O MET A 31 103.505 174.734 273.256 1.00 77.86 O ANISOU 123 O MET A 31 5056 11167 13359 -1993 73 -1467 O ATOM 124 CB MET A 31 106.832 174.690 273.371 1.00 93.31 C ANISOU 124 CB MET A 31 7104 12932 15418 -1833 438 -1587 C ATOM 125 CG MET A 31 108.057 175.383 273.923 1.00 94.36 C ANISOU 125 CG MET A 31 7303 13073 15477 -1701 527 -1448 C ATOM 126 SD MET A 31 108.812 176.549 272.786 1.00 98.47 S ANISOU 126 SD MET A 31 7855 13766 15792 -1749 573 -1580 S ATOM 127 CE MET A 31 107.738 177.951 273.043 1.00100.63 C ANISOU 127 CE MET A 31 8156 14238 15841 -1723 398 -1333 C ATOM 128 N VAL A 32 104.437 172.698 273.468 1.00 70.27 N ANISOU 128 N VAL A 32 4063 9856 12780 -2014 294 -1707 N ATOM 129 CA VAL A 32 103.356 172.039 272.746 1.00 82.98 C ANISOU 129 CA VAL A 32 5609 11479 14439 -2178 214 -1894 C ATOM 130 C VAL A 32 102.057 172.025 273.551 1.00 82.38 C ANISOU 130 C VAL A 32 5514 11433 14353 -2158 81 -1681 C ATOM 131 O VAL A 32 100.972 171.961 272.964 1.00 73.42 O ANISOU 131 O VAL A 32 4332 10401 13165 -2281 -43 -1760 O ATOM 132 CB VAL A 32 103.827 170.627 272.332 1.00 74.80 C ANISOU 132 CB VAL A 32 4533 10220 13666 -2266 371 -2180 C ATOM 133 CG1 VAL A 32 102.657 169.708 271.993 1.00 77.06 C ANISOU 133 CG1 VAL A 32 4762 10462 14057 -2419 308 -2330 C ATOM 134 CG2 VAL A 32 104.781 170.722 271.146 1.00 75.93 C ANISOU 134 CG2 VAL A 32 4686 10406 13757 -2356 479 -2469 C ATOM 135 N VAL A 33 102.123 172.126 274.877 1.00 70.20 N ANISOU 135 N VAL A 33 4010 9828 12834 -2013 102 -1419 N ATOM 136 CA VAL A 33 100.935 172.111 275.719 1.00 69.75 C ANISOU 136 CA VAL A 33 3942 9806 12754 -1995 4 -1231 C ATOM 137 C VAL A 33 100.585 173.503 276.234 1.00 81.52 C ANISOU 137 C VAL A 33 5483 11500 13991 -1905 -90 -980 C ATOM 138 O VAL A 33 99.410 173.871 276.277 1.00 81.64 O ANISOU 138 O VAL A 33 5467 11638 13913 -1942 -211 -895 O ATOM 139 CB VAL A 33 101.099 171.116 276.892 1.00 69.65 C ANISOU 139 CB VAL A 33 3934 9585 12945 -1920 102 -1146 C ATOM 140 CG1 VAL A 33 99.831 171.067 277.733 1.00 69.38 C ANISOU 140 CG1 VAL A 33 3889 9595 12879 -1919 16 -986 C ATOM 141 CG2 VAL A 33 101.448 169.729 276.375 1.00 72.03 C ANISOU 141 CG2 VAL A 33 4176 9656 13535 -2006 218 -1396 C ATOM 142 N GLY A 34 101.583 174.289 276.630 1.00 79.99 N ANISOU 142 N GLY A 34 5362 11342 13689 -1791 -28 -868 N ATOM 143 CA GLY A 34 101.330 175.582 277.235 1.00 78.35 C ANISOU 143 CA GLY A 34 5210 11304 13254 -1705 -84 -648 C ATOM 144 C GLY A 34 101.023 176.697 276.258 1.00 78.90 C ANISOU 144 C GLY A 34 5258 11553 13169 -1747 -180 -651 C ATOM 145 O GLY A 34 100.191 177.564 276.546 1.00 78.28 O ANISOU 145 O GLY A 34 5176 11617 12948 -1721 -264 -499 O ATOM 146 N LEU A 35 101.700 176.705 275.108 1.00 64.79 N ANISOU 146 N LEU A 35 3449 9763 11405 -1812 -157 -839 N ATOM 147 CA LEU A 35 101.364 177.679 274.071 1.00 65.30 C ANISOU 147 CA LEU A 35 3478 9998 11334 -1867 -257 -873 C ATOM 148 C LEU A 35 99.917 177.556 273.617 1.00 66.86 C ANISOU 148 C LEU A 35 3587 10294 11521 -1964 -420 -884 C ATOM 149 O LEU A 35 99.159 178.528 273.767 1.00 66.26 O ANISOU 149 O LEU A 35 3490 10353 11332 -1923 -522 -700 O ATOM 150 CB LEU A 35 102.334 177.547 272.897 1.00 78.62 C ANISOU 150 CB LEU A 35 5161 11686 13024 -1945 -186 -1138 C ATOM 151 CG LEU A 35 103.785 177.963 273.085 1.00 65.07 C ANISOU 151 CG LEU A 35 3520 9923 11282 -1857 -36 -1132 C ATOM 152 CD1 LEU A 35 104.514 177.686 271.791 1.00 66.73 C ANISOU 152 CD1 LEU A 35 3712 10164 11480 -1974 36 -1446 C ATOM 153 CD2 LEU A 35 103.863 179.431 273.451 1.00 63.22 C ANISOU 153 CD2 LEU A 35 3330 9807 10883 -1758 -62 -907 C ATOM 154 N PRO A 36 99.452 176.402 273.086 1.00 69.00 N ANISOU 154 N PRO A 36 3801 10504 11911 -2093 -448 -1090 N ATOM 155 CA PRO A 36 98.093 176.359 272.525 1.00 70.75 C ANISOU 155 CA PRO A 36 3933 10850 12097 -2201 -620 -1112 C ATOM 156 C PRO A 36 97.012 176.563 273.575 1.00 83.70 C ANISOU 156 C PRO A 36 5555 12519 13728 -2134 -685 -856 C ATOM 157 O PRO A 36 96.053 177.311 273.356 1.00 84.35 O ANISOU 157 O PRO A 36 5576 12759 13714 -2140 -826 -734 O ATOM 158 CB PRO A 36 98.012 174.954 271.920 1.00 73.15 C ANISOU 158 CB PRO A 36 4201 11050 12542 -2354 -591 -1404 C ATOM 159 CG PRO A 36 98.915 174.150 272.756 1.00 72.23 C ANISOU 159 CG PRO A 36 4141 10706 12598 -2280 -410 -1412 C ATOM 160 CD PRO A 36 100.058 175.057 273.119 1.00 70.00 C ANISOU 160 CD PRO A 36 3935 10433 12228 -2141 -320 -1288 C ATOM 161 N GLY A 37 97.167 175.886 274.714 1.00 82.76 N ANISOU 161 N GLY A 37 5484 12256 13705 -2071 -575 -788 N ATOM 162 CA GLY A 37 96.175 175.984 275.768 1.00 82.43 C ANISOU 162 CA GLY A 37 5436 12258 13626 -2020 -603 -605 C ATOM 163 C GLY A 37 95.992 177.405 276.258 1.00 81.50 C ANISOU 163 C GLY A 37 5351 12309 13307 -1908 -624 -399 C ATOM 164 O GLY A 37 94.885 177.947 276.225 1.00 83.70 O ANISOU 164 O GLY A 37 5565 12743 13495 -1920 -725 -313 O ATOM 165 N ASN A 38 97.085 178.040 276.687 1.00 78.54 N ANISOU 165 N ASN A 38 5069 11913 12859 -1802 -520 -338 N ATOM 166 CA ASN A 38 96.990 179.405 277.191 1.00 62.76 C ANISOU 166 CA ASN A 38 3111 10066 10669 -1700 -509 -191 C ATOM 167 C ASN A 38 96.522 180.364 276.108 1.00 80.99 C ANISOU 167 C ASN A 38 5333 12539 12899 -1736 -635 -152 C ATOM 168 O ASN A 38 95.744 181.282 276.388 1.00 63.30 O ANISOU 168 O ASN A 38 3114 10418 10518 -1661 -658 -91 O ATOM 169 CB ASN A 38 98.334 179.843 277.769 1.00 60.84 C ANISOU 169 CB ASN A 38 2982 9762 10371 -1601 -377 -157 C ATOM 170 CG ASN A 38 98.467 179.504 279.241 1.00 76.55 C ANISOU 170 CG ASN A 38 5060 11673 12353 -1521 -277 -119 C ATOM 171 OD1 ASN A 38 98.001 180.247 280.103 1.00 77.48 O ANISOU 171 OD1 ASN A 38 5221 11866 12350 -1451 -254 -68 O ATOM 172 ND2 ASN A 38 99.101 178.374 279.537 1.00 74.76 N ANISOU 172 ND2 ASN A 38 4855 11277 12275 -1529 -215 -170 N ATOM 173 N THR A 39 96.963 180.160 274.860 1.00 82.48 N ANISOU 173 N THR A 39 5477 12679 13181 -1818 -700 -259 N ATOM 174 CA THR A 39 96.509 181.027 273.776 1.00 66.26 C ANISOU 174 CA THR A 39 3333 10736 11105 -1847 -847 -233 C ATOM 175 C THR A 39 95.007 180.888 273.561 1.00 67.93 C ANISOU 175 C THR A 39 3452 11036 11323 -1898 -1007 -187 C ATOM 176 O THR A 39 94.334 181.856 273.194 1.00 68.45 O ANISOU 176 O THR A 39 3489 11150 11367 -1833 -1116 -78 O ATOM 177 CB THR A 39 97.266 180.719 272.483 1.00 67.68 C ANISOU 177 CB THR A 39 3506 10892 11319 -1938 -859 -502 C ATOM 178 OG1 THR A 39 98.565 180.204 272.791 1.00 66.63 O ANISOU 178 OG1 THR A 39 3469 10632 11216 -1918 -684 -606 O ATOM 179 CG2 THR A 39 97.446 181.984 271.665 1.00 67.88 C ANISOU 179 CG2 THR A 39 3503 11039 11248 -1901 -917 -504 C ATOM 180 N PHE A 40 94.464 179.692 273.792 1.00 68.95 N ANISOU 180 N PHE A 40 3538 11135 11524 -1996 -1018 -275 N ATOM 181 CA PHE A 40 93.018 179.506 273.728 1.00 84.98 C ANISOU 181 CA PHE A 40 5484 13258 13547 -2046 -1149 -231 C ATOM 182 C PHE A 40 92.340 180.066 274.975 1.00 85.28 C ANISOU 182 C PHE A 40 5589 13400 13413 -1915 -1048 -132 C ATOM 183 O PHE A 40 91.345 180.795 274.876 1.00 86.12 O ANISOU 183 O PHE A 40 5652 13678 13390 -1866 -1109 -115 O ATOM 184 CB PHE A 40 92.694 178.021 273.551 1.00 72.27 C ANISOU 184 CB PHE A 40 3825 11557 12079 -2195 -1167 -412 C ATOM 185 CG PHE A 40 91.220 177.705 273.530 1.00 74.04 C ANISOU 185 CG PHE A 40 3935 11883 12315 -2275 -1300 -369 C ATOM 186 CD1 PHE A 40 90.285 178.644 273.117 1.00 74.90 C ANISOU 186 CD1 PHE A 40 3996 12123 12340 -2225 -1446 -238 C ATOM 187 CD2 PHE A 40 90.773 176.456 273.924 1.00 84.66 C ANISOU 187 CD2 PHE A 40 5269 13127 13770 -2362 -1257 -479 C ATOM 188 CE1 PHE A 40 88.937 178.344 273.109 1.00 76.66 C ANISOU 188 CE1 PHE A 40 4130 12430 12566 -2284 -1554 -205 C ATOM 189 CE2 PHE A 40 89.427 176.149 273.911 1.00 76.75 C ANISOU 189 CE2 PHE A 40 4158 12222 12781 -2444 -1369 -448 C ATOM 190 CZ PHE A 40 88.509 177.095 273.503 1.00 77.56 C ANISOU 190 CZ PHE A 40 4198 12498 12773 -2406 -1517 -314 C ATOM 191 N VAL A 41 92.860 179.730 276.160 1.00 84.35 N ANISOU 191 N VAL A 41 5557 13184 13308 -1850 -884 -154 N ATOM 192 CA VAL A 41 92.242 180.191 277.402 1.00 65.87 C ANISOU 192 CA VAL A 41 3266 10868 10894 -1729 -791 -153 C ATOM 193 C VAL A 41 92.182 181.713 277.436 1.00 79.52 C ANISOU 193 C VAL A 41 5032 12683 12498 -1585 -763 -179 C ATOM 194 O VAL A 41 91.157 182.299 277.806 1.00 65.12 O ANISOU 194 O VAL A 41 3164 10894 10686 -1507 -779 -222 O ATOM 195 CB VAL A 41 92.990 179.624 278.624 1.00 64.15 C ANISOU 195 CB VAL A 41 3138 10492 10743 -1687 -648 -138 C ATOM 196 CG1 VAL A 41 92.480 180.263 279.900 1.00 62.74 C ANISOU 196 CG1 VAL A 41 3021 10302 10514 -1565 -567 -120 C ATOM 197 CG2 VAL A 41 92.826 178.115 278.700 1.00 65.39 C ANISOU 197 CG2 VAL A 41 3259 10511 11076 -1794 -657 -177 C ATOM 198 N VAL A 42 93.270 182.379 277.036 1.00 78.72 N ANISOU 198 N VAL A 42 4995 12577 12337 -1546 -722 -168 N ATOM 199 CA VAL A 42 93.262 183.837 276.976 1.00 77.64 C ANISOU 199 CA VAL A 42 4869 12454 12176 -1408 -694 -247 C ATOM 200 C VAL A 42 92.356 184.337 275.862 1.00 78.69 C ANISOU 200 C VAL A 42 4856 12650 12394 -1394 -845 -367 C ATOM 201 O VAL A 42 91.876 185.476 275.916 1.00 77.62 O ANISOU 201 O VAL A 42 4668 12447 12378 -1270 -880 -329 O ATOM 202 CB VAL A 42 94.693 184.383 276.798 1.00 61.93 C ANISOU 202 CB VAL A 42 2976 10426 10130 -1379 -605 -229 C ATOM 203 CG1 VAL A 42 95.164 184.204 275.362 1.00 68.98 C ANISOU 203 CG1 VAL A 42 3810 11431 10969 -1490 -705 -197 C ATOM 204 CG2 VAL A 42 94.768 185.844 277.205 1.00 60.77 C ANISOU 204 CG2 VAL A 42 2859 10182 10048 -1231 -540 -250 C ATOM 205 N TRP A 43 92.099 183.505 274.851 1.00 67.38 N ANISOU 205 N TRP A 43 3344 11345 10913 -1535 -961 -423 N ATOM 206 CA TRP A 43 91.268 183.924 273.729 1.00 72.58 C ANISOU 206 CA TRP A 43 3838 11797 11941 -1471 -1179 -575 C ATOM 207 C TRP A 43 89.806 184.028 274.143 1.00 73.96 C ANISOU 207 C TRP A 43 3918 12104 12081 -1442 -1244 -530 C ATOM 208 O TRP A 43 89.181 185.086 274.000 1.00 74.86 O ANISOU 208 O TRP A 43 3940 12245 12260 -1343 -1342 -388 O ATOM 209 CB TRP A 43 91.443 182.941 272.568 1.00 71.70 C ANISOU 209 CB TRP A 43 3679 11384 12181 -1644 -1448 -247 C ATOM 210 CG TRP A 43 90.547 183.182 271.395 1.00 74.45 C ANISOU 210 CG TRP A 43 3842 12035 12410 -1723 -1666 -348 C ATOM 211 CD1 TRP A 43 90.000 184.370 271.001 1.00 75.21 C ANISOU 211 CD1 TRP A 43 3828 12379 12368 -1635 -1754 -332 C ATOM 212 CD2 TRP A 43 90.091 182.201 270.459 1.00 77.05 C ANISOU 212 CD2 TRP A 43 4071 12514 12690 -1940 -1849 -383 C ATOM 213 NE1 TRP A 43 89.231 184.188 269.877 1.00 78.14 N ANISOU 213 NE1 TRP A 43 4099 12995 12595 -1749 -1979 -323 N ATOM 214 CE2 TRP A 43 89.270 182.864 269.524 1.00 98.38 C ANISOU 214 CE2 TRP A 43 6653 15503 15223 -1939 -2036 -429 C ATOM 215 CE3 TRP A 43 90.297 180.824 270.321 1.00 77.86 C ANISOU 215 CE3 TRP A 43 4185 12613 12784 -2147 -1845 -425 C ATOM 216 CZ2 TRP A 43 88.656 182.198 268.464 1.00100.86 C ANISOU 216 CZ2 TRP A 43 6900 16033 15389 -2119 -2219 -535 C ATOM 217 CZ3 TRP A 43 89.687 180.164 269.268 1.00 97.29 C ANISOU 217 CZ3 TRP A 43 6570 15258 15139 -2318 -2002 -623 C ATOM 218 CH2 TRP A 43 88.875 180.852 268.353 1.00100.51 C ANISOU 218 CH2 TRP A 43 6883 15910 15395 -2307 -2195 -667 C ATOM 219 N SER A 44 89.246 182.935 274.669 1.00 71.05 N ANISOU 219 N SER A 44 3558 11895 11543 -1559 -1192 -541 N ATOM 220 CA SER A 44 87.821 182.896 274.980 1.00 72.31 C ANISOU 220 CA SER A 44 3609 12092 11775 -1534 -1266 -534 C ATOM 221 C SER A 44 87.418 184.035 275.905 1.00 75.79 C ANISOU 221 C SER A 44 4057 12458 12283 -1368 -1211 -398 C ATOM 222 O SER A 44 86.410 184.711 275.670 1.00 77.44 O ANISOU 222 O SER A 44 4135 12702 12586 -1294 -1329 -345 O ATOM 223 CB SER A 44 87.464 181.546 275.600 1.00 72.56 C ANISOU 223 CB SER A 44 3665 12217 11688 -1700 -1214 -434 C ATOM 224 OG SER A 44 86.306 181.645 276.409 1.00 72.80 O ANISOU 224 OG SER A 44 3633 12226 11801 -1637 -1206 -421 O ATOM 225 N ILE A 45 88.216 184.284 276.944 1.00 73.29 N ANISOU 225 N ILE A 45 3884 12053 11909 -1317 -1040 -317 N ATOM 226 CA ILE A 45 87.906 185.307 277.933 1.00 71.69 C ANISOU 226 CA ILE A 45 3707 11780 11753 -1185 -962 -203 C ATOM 227 C ILE A 45 87.880 186.712 277.341 1.00 71.64 C ANISOU 227 C ILE A 45 3637 11773 11809 -1071 -1030 -104 C ATOM 228 O ILE A 45 87.311 187.628 277.945 1.00 71.38 O ANISOU 228 O ILE A 45 3619 11694 11810 -965 -995 33 O ATOM 229 CB ILE A 45 88.912 185.185 279.097 1.00 64.67 C ANISOU 229 CB ILE A 45 2996 10782 10795 -1173 -780 -164 C ATOM 230 CG1 ILE A 45 88.945 183.733 279.585 1.00 64.64 C ANISOU 230 CG1 ILE A 45 3034 10774 10752 -1290 -743 -185 C ATOM 231 CG2 ILE A 45 88.553 186.123 280.238 1.00 70.04 C ANISOU 231 CG2 ILE A 45 3724 11377 11510 -1063 -689 -64 C ATOM 232 CD1 ILE A 45 89.465 183.550 280.996 1.00 71.86 C ANISOU 232 CD1 ILE A 45 4080 11571 11652 -1262 -599 -126 C ATOM 233 N LEU A 46 88.453 186.902 276.156 1.00 71.66 N ANISOU 233 N LEU A 46 3597 11812 11817 -1095 -1130 -119 N ATOM 234 CA LEU A 46 88.428 188.201 275.493 1.00 69.15 C ANISOU 234 CA LEU A 46 3253 11518 11502 -999 -1208 77 C ATOM 235 C LEU A 46 87.449 188.283 274.332 1.00 94.08 C ANISOU 235 C LEU A 46 6247 14828 14672 -1015 -1444 146 C ATOM 236 O LEU A 46 86.714 189.266 274.226 1.00 95.71 O ANISOU 236 O LEU A 46 6396 15099 14870 -912 -1505 344 O ATOM 237 CB LEU A 46 89.831 188.570 275.008 1.00 68.07 C ANISOU 237 CB LEU A 46 3203 11350 11310 -1012 -1152 101 C ATOM 238 CG LEU A 46 90.607 189.441 275.989 1.00 65.70 C ANISOU 238 CG LEU A 46 3051 10933 10979 -925 -952 186 C ATOM 239 CD1 LEU A 46 92.093 189.267 275.772 1.00 64.36 C ANISOU 239 CD1 LEU A 46 2974 10715 10764 -978 -858 109 C ATOM 240 CD2 LEU A 46 90.202 190.907 275.838 1.00 66.30 C ANISOU 240 CD2 LEU A 46 3101 11041 11048 -805 -967 435 C ATOM 241 N LYS A 47 87.408 187.277 273.462 1.00 73.62 N ANISOU 241 N LYS A 47 3577 12301 12096 -1146 -1582 -1 N ATOM 242 CA LYS A 47 86.593 187.345 272.252 1.00 76.64 C ANISOU 242 CA LYS A 47 3819 12866 12434 -1188 -1832 78 C ATOM 243 C LYS A 47 85.141 186.948 272.476 1.00 87.49 C ANISOU 243 C LYS A 47 5062 14289 13892 -1185 -1925 29 C ATOM 244 O LYS A 47 84.249 187.540 271.862 1.00 88.29 O ANISOU 244 O LYS A 47 5055 14548 13942 -1139 -2091 185 O ATOM 245 CB LYS A 47 87.184 186.448 271.171 1.00 82.79 C ANISOU 245 CB LYS A 47 4584 13699 13174 -1360 -1953 -43 C ATOM 246 N ARG A 48 84.872 185.980 273.354 1.00 90.20 N ANISOU 246 N ARG A 48 5405 14537 14329 -1235 -1813 -171 N ATOM 247 CA ARG A 48 83.549 185.376 273.450 1.00 94.82 C ANISOU 247 CA ARG A 48 5850 15193 14984 -1275 -1903 -257 C ATOM 248 C ARG A 48 82.869 185.645 274.791 1.00 96.72 C ANISOU 248 C ARG A 48 6114 15403 15234 -1186 -1745 -203 C ATOM 249 O ARG A 48 82.077 184.818 275.258 1.00 97.11 O ANISOU 249 O ARG A 48 6126 15475 15297 -1253 -1719 -299 O ATOM 250 CB ARG A 48 83.629 183.866 273.213 1.00 97.07 C ANISOU 250 CB ARG A 48 6172 15416 15294 -1442 -1901 -482 C ATOM 251 N MET A 49 83.137 186.790 275.418 1.00 94.69 N ANISOU 251 N MET A 49 5956 15070 14953 -1047 -1634 -13 N ATOM 252 CA MET A 49 82.501 187.122 276.686 1.00 93.14 C ANISOU 252 CA MET A 49 5793 14808 14789 -970 -1498 60 C ATOM 253 C MET A 49 82.145 188.597 276.731 1.00 90.51 C ANISOU 253 C MET A 49 5448 14458 14485 -812 -1507 300 C ATOM 254 O MET A 49 82.881 189.444 276.218 1.00 88.95 O ANISOU 254 O MET A 49 5303 14251 14244 -752 -1515 429 O ATOM 255 CB MET A 49 83.398 186.786 277.884 1.00 87.69 C ANISOU 255 CB MET A 49 5286 13986 14047 -992 -1276 14 C ATOM 256 CG MET A 49 83.696 185.310 278.032 1.00 86.55 C ANISOU 256 CG MET A 49 5159 13875 13850 -1147 -1237 -161 C ATOM 257 SD MET A 49 83.791 184.787 279.749 1.00 82.85 S ANISOU 257 SD MET A 49 4837 13293 13349 -1165 -1033 -126 S ATOM 258 CE MET A 49 84.614 186.187 280.491 1.00 80.73 C ANISOU 258 CE MET A 49 4735 12869 13071 -1017 -898 10 C ATOM 259 N ARG A 50 81.007 188.894 277.348 1.00 93.82 N ANISOU 259 N ARG A 50 5790 14882 14976 -750 -1495 370 N ATOM 260 CA ARG A 50 80.565 190.270 277.511 1.00 96.00 C ANISOU 260 CA ARG A 50 6042 15134 15300 -600 -1479 601 C ATOM 261 C ARG A 50 80.881 190.788 278.910 1.00 99.78 C ANISOU 261 C ARG A 50 6666 15443 15804 -544 -1251 646 C ATOM 262 O ARG A 50 81.573 191.801 279.066 1.00102.81 O ANISOU 262 O ARG A 50 7143 15742 16178 -464 -1157 776 O ATOM 263 CB ARG A 50 79.061 190.378 277.208 1.00 97.21 C ANISOU 263 CB ARG A 50 5995 15409 15532 -559 -1623 666 C ATOM 264 N LYS A 51 80.381 190.104 279.936 1.00 97.01 N ANISOU 264 N LYS A 51 6331 15048 15480 -596 -1162 544 N ATOM 265 CA LYS A 51 80.661 190.431 281.332 1.00 91.07 C ANISOU 265 CA LYS A 51 5721 14147 14733 -570 -961 569 C ATOM 266 C LYS A 51 81.775 189.505 281.810 1.00 84.73 C ANISOU 266 C LYS A 51 5078 13284 13831 -672 -864 427 C ATOM 267 O LYS A 51 81.536 188.335 282.120 1.00 82.45 O ANISOU 267 O LYS A 51 4780 13027 13521 -773 -865 308 O ATOM 268 CB LYS A 51 79.404 190.289 282.185 1.00 73.20 C ANISOU 268 CB LYS A 51 3375 11884 12554 -563 -930 578 C ATOM 269 N ARG A 52 82.999 190.028 281.858 1.00 81.60 N ANISOU 269 N ARG A 52 4822 12808 13375 -648 -778 454 N ATOM 270 CA ARG A 52 84.155 189.241 282.275 1.00 80.23 C ANISOU 270 CA ARG A 52 4798 12582 13105 -731 -688 341 C ATOM 271 C ARG A 52 84.172 189.156 283.796 1.00 76.43 C ANISOU 271 C ARG A 52 4431 11995 12613 -739 -536 348 C ATOM 272 O ARG A 52 84.492 190.137 284.476 1.00 74.34 O ANISOU 272 O ARG A 52 4248 11636 12363 -675 -428 439 O ATOM 273 CB ARG A 52 85.443 189.860 281.740 1.00 81.75 C ANISOU 273 CB ARG A 52 5081 12739 13240 -704 -657 367 C ATOM 274 CG ARG A 52 85.589 189.774 280.230 1.00 85.21 C ANISOU 274 CG ARG A 52 5416 13285 13676 -720 -813 355 C ATOM 275 CD ARG A 52 86.886 190.411 279.772 1.00 65.39 C ANISOU 275 CD ARG A 52 2998 10736 11112 -698 -766 394 C ATOM 276 NE ARG A 52 87.028 190.352 278.323 1.00 66.97 N ANISOU 276 NE ARG A 52 3097 11046 11303 -721 -924 402 N ATOM 277 CZ ARG A 52 86.496 191.237 277.486 1.00 85.53 C ANISOU 277 CZ ARG A 52 5341 13478 13680 -648 -1040 571 C ATOM 278 NH1 ARG A 52 85.782 192.253 277.954 1.00 85.24 N ANISOU 278 NH1 ARG A 52 5276 13410 13703 -538 -1001 738 N ATOM 279 NH2 ARG A 52 86.678 191.107 276.180 1.00 87.36 N ANISOU 279 NH2 ARG A 52 5491 13833 13867 -688 -1199 589 N ATOM 280 N SER A 53 83.825 187.986 284.331 1.00 75.54 N ANISOU 280 N SER A 53 4300 11873 12530 -826 -537 309 N ATOM 281 CA SER A 53 83.753 187.808 285.772 1.00 72.86 C ANISOU 281 CA SER A 53 4031 11405 12249 -841 -421 378 C ATOM 282 C SER A 53 85.117 188.058 286.410 1.00 62.32 C ANISOU 282 C SER A 53 2866 9965 10846 -836 -305 394 C ATOM 283 O SER A 53 86.162 187.991 285.758 1.00 61.39 O ANISOU 283 O SER A 53 2813 9873 10639 -848 -314 335 O ATOM 284 CB SER A 53 83.256 186.401 286.111 1.00 74.70 C ANISOU 284 CB SER A 53 4214 11643 12526 -942 -450 333 C ATOM 285 OG SER A 53 82.946 186.272 287.489 1.00 73.35 O ANISOU 285 OG SER A 53 4081 11356 12432 -949 -353 406 O ATOM 286 N VAL A 54 85.094 188.377 287.707 1.00 83.02 N ANISOU 286 N VAL A 54 5552 12480 13513 -822 -195 468 N ATOM 287 CA VAL A 54 86.341 188.558 288.446 1.00 81.38 C ANISOU 287 CA VAL A 54 5493 12186 13241 -827 -88 477 C ATOM 288 C VAL A 54 87.151 187.269 288.431 1.00 81.33 C ANISOU 288 C VAL A 54 5541 12167 13192 -902 -105 415 C ATOM 289 O VAL A 54 88.382 187.290 288.307 1.00 80.76 O ANISOU 289 O VAL A 54 5566 12080 13039 -906 -70 385 O ATOM 290 CB VAL A 54 86.055 189.034 289.884 1.00 59.79 C ANISOU 290 CB VAL A 54 2797 9362 10558 -815 25 552 C ATOM 291 CG1 VAL A 54 87.356 189.273 290.629 1.00 58.19 C ANISOU 291 CG1 VAL A 54 2735 9099 10277 -825 125 551 C ATOM 292 CG2 VAL A 54 85.206 190.299 289.876 1.00 60.55 C ANISOU 292 CG2 VAL A 54 2827 9467 10714 -740 51 618 C ATOM 293 N THR A 55 86.473 186.125 288.543 1.00 60.46 N ANISOU 293 N THR A 55 2829 9530 10613 -963 -153 398 N ATOM 294 CA THR A 55 87.150 184.844 288.398 1.00 70.36 C ANISOU 294 CA THR A 55 4115 10769 11849 -1034 -173 346 C ATOM 295 C THR A 55 87.621 184.596 286.969 1.00 72.15 C ANISOU 295 C THR A 55 4314 11101 11999 -1059 -255 255 C ATOM 296 O THR A 55 88.454 183.710 286.754 1.00 74.01 O ANISOU 296 O THR A 55 4593 11325 12204 -1111 -254 213 O ATOM 297 CB THR A 55 86.226 183.715 288.864 1.00 61.51 C ANISOU 297 CB THR A 55 2918 9621 10832 -1099 -196 355 C ATOM 298 OG1 THR A 55 85.467 184.163 289.994 1.00 67.80 O ANISOU 298 OG1 THR A 55 3702 10359 11701 -1072 -135 433 O ATOM 299 CG2 THR A 55 87.036 182.487 289.277 1.00 61.09 C ANISOU 299 CG2 THR A 55 2927 9488 10796 -1157 -167 347 C ATOM 300 N ALA A 56 87.127 185.360 285.996 1.00 73.25 N ANISOU 300 N ALA A 56 4376 11346 12110 -1022 -323 226 N ATOM 301 CA ALA A 56 87.620 185.285 284.626 1.00 73.84 C ANISOU 301 CA ALA A 56 4422 11538 12096 -1044 -399 131 C ATOM 302 C ALA A 56 88.750 186.267 284.350 1.00 72.38 C ANISOU 302 C ALA A 56 4334 11341 11828 -985 -346 129 C ATOM 303 O ALA A 56 89.330 186.234 283.261 1.00 72.74 O ANISOU 303 O ALA A 56 4367 11475 11794 -1004 -392 45 O ATOM 304 CB ALA A 56 86.480 185.527 283.631 1.00 75.74 C ANISOU 304 CB ALA A 56 4509 11916 12354 -1037 -519 87 C ATOM 305 N LEU A 57 89.064 187.151 285.295 1.00 58.63 N ANISOU 305 N LEU A 57 2680 9498 10099 -924 -246 212 N ATOM 306 CA LEU A 57 90.214 188.034 285.167 1.00 57.26 C ANISOU 306 CA LEU A 57 2606 9303 9848 -884 -178 211 C ATOM 307 C LEU A 57 91.451 187.447 285.825 1.00 56.01 C ANISOU 307 C LEU A 57 2561 9077 9643 -922 -102 200 C ATOM 308 O LEU A 57 92.546 187.519 285.263 1.00 90.12 O ANISOU 308 O LEU A 57 6934 13426 13882 -931 -85 147 O ATOM 309 CB LEU A 57 89.907 189.407 285.770 1.00 56.99 C ANISOU 309 CB LEU A 57 2595 9212 9846 -807 -106 303 C ATOM 310 CG LEU A 57 88.734 190.151 285.142 1.00 58.32 C ANISOU 310 CG LEU A 57 2647 9437 10074 -746 -175 342 C ATOM 311 CD1 LEU A 57 88.660 191.563 285.689 1.00 63.48 C ANISOU 311 CD1 LEU A 57 3336 10029 10756 -671 -79 440 C ATOM 312 CD2 LEU A 57 88.883 190.161 283.636 1.00 68.16 C ANISOU 312 CD2 LEU A 57 3820 10783 11295 -742 -283 289 C ATOM 313 N MET A 58 91.293 186.878 287.022 1.00 55.94 N ANISOU 313 N MET A 58 2583 8982 9690 -942 -55 253 N ATOM 314 CA MET A 58 92.386 186.132 287.628 1.00 79.90 C ANISOU 314 CA MET A 58 5702 11956 12700 -975 -3 250 C ATOM 315 C MET A 58 92.911 185.095 286.648 1.00 75.99 C ANISOU 315 C MET A 58 5183 11516 12174 -1029 -62 176 C ATOM 316 O MET A 58 94.103 185.078 286.327 1.00 71.42 O ANISOU 316 O MET A 58 4664 10949 11522 -1034 -32 141 O ATOM 317 CB MET A 58 91.925 185.470 288.929 1.00 83.99 C ANISOU 317 CB MET A 58 6224 12385 13303 -994 32 314 C ATOM 318 CG MET A 58 91.344 186.432 289.965 1.00 82.50 C ANISOU 318 CG MET A 58 6049 12157 13142 -957 97 384 C ATOM 319 SD MET A 58 92.517 187.679 290.534 1.00 78.63 S ANISOU 319 SD MET A 58 5669 11650 12555 -923 204 396 S ATOM 320 CE MET A 58 91.610 188.407 291.896 1.00 76.94 C ANISOU 320 CE MET A 58 5445 11393 12396 -910 281 471 C ATOM 321 N VAL A 59 92.016 184.255 286.120 1.00 56.62 N ANISOU 321 N VAL A 59 2633 9108 9772 -1078 -143 147 N ATOM 322 CA VAL A 59 92.422 183.272 285.118 1.00 73.10 C ANISOU 322 CA VAL A 59 4684 11263 11827 -1149 -199 76 C ATOM 323 C VAL A 59 93.070 183.967 283.932 1.00 73.94 C ANISOU 323 C VAL A 59 4792 11487 11815 -1141 -221 8 C ATOM 324 O VAL A 59 94.118 183.539 283.439 1.00 72.22 O ANISOU 324 O VAL A 59 4610 11295 11534 -1178 -208 -24 O ATOM 325 CB VAL A 59 91.224 182.415 284.675 1.00 58.78 C ANISOU 325 CB VAL A 59 2751 9504 10078 -1218 -286 50 C ATOM 326 CG1 VAL A 59 91.583 181.618 283.432 1.00 59.46 C ANISOU 326 CG1 VAL A 59 2788 9698 10105 -1309 -352 -25 C ATOM 327 CG2 VAL A 59 90.812 181.482 285.788 1.00 59.20 C ANISOU 327 CG2 VAL A 59 2807 9428 10257 -1242 -253 108 C ATOM 328 N LEU A 60 92.464 185.061 283.468 1.00 78.41 N ANISOU 328 N LEU A 60 5314 12117 12361 -1090 -252 -9 N ATOM 329 CA LEU A 60 92.986 185.792 282.322 1.00 83.28 C ANISOU 329 CA LEU A 60 5914 12801 12927 -1073 -282 -54 C ATOM 330 C LEU A 60 94.440 186.181 282.545 1.00 86.44 C ANISOU 330 C LEU A 60 6444 13152 13248 -1052 -185 -53 C ATOM 331 O LEU A 60 95.326 185.653 281.870 1.00 89.57 O ANISOU 331 O LEU A 60 6857 13569 13605 -1099 -192 -77 O ATOM 332 CB LEU A 60 92.150 187.038 282.034 1.00 57.64 C ANISOU 332 CB LEU A 60 2595 9563 9742 -994 -319 -16 C ATOM 333 CG LEU A 60 92.659 187.819 280.825 1.00 58.14 C ANISOU 333 CG LEU A 60 2612 9661 9817 -971 -363 -21 C ATOM 334 CD1 LEU A 60 92.445 187.013 279.566 1.00 59.86 C ANISOU 334 CD1 LEU A 60 2716 9976 10053 -1049 -492 -95 C ATOM 335 CD2 LEU A 60 91.980 189.164 280.726 1.00 58.66 C ANISOU 335 CD2 LEU A 60 2637 9699 9953 -874 -380 92 C ATOM 336 N ASN A 61 94.698 187.076 283.502 1.00 54.23 N ANISOU 336 N ASN A 61 2439 9007 9160 -993 -93 -11 N ATOM 337 CA ASN A 61 96.060 187.560 283.709 1.00 52.94 C ANISOU 337 CA ASN A 61 2385 8806 8924 -979 -4 -13 C ATOM 338 C ASN A 61 96.995 186.428 284.096 1.00 58.42 C ANISOU 338 C ASN A 61 3126 9472 9598 -1027 22 -9 C ATOM 339 O ASN A 61 98.138 186.373 283.629 1.00 57.73 O ANISOU 339 O ASN A 61 3104 9400 9429 -1038 51 -37 O ATOM 340 CB ASN A 61 96.080 188.646 284.775 1.00 52.23 C ANISOU 340 CB ASN A 61 2355 8632 8858 -926 85 60 C ATOM 341 CG ASN A 61 95.046 189.710 284.528 1.00 52.79 C ANISOU 341 CG ASN A 61 2373 8708 8977 -870 65 99 C ATOM 342 OD1 ASN A 61 94.164 189.925 285.349 1.00 58.88 O ANISOU 342 OD1 ASN A 61 3128 9428 9817 -846 77 174 O ATOM 343 ND2 ASN A 61 95.138 190.378 283.388 1.00 53.99 N ANISOU 343 ND2 ASN A 61 2477 8904 9133 -847 33 85 N ATOM 344 N LEU A 62 96.535 185.519 284.956 1.00 52.99 N ANISOU 344 N LEU A 62 2421 8717 8997 -1045 14 39 N ATOM 345 CA LEU A 62 97.363 184.376 285.319 1.00 68.61 C ANISOU 345 CA LEU A 62 4429 10642 10997 -1078 35 54 C ATOM 346 C LEU A 62 97.669 183.514 284.099 1.00 75.76 C ANISOU 346 C LEU A 62 5284 11629 11872 -1143 -21 5 C ATOM 347 O LEU A 62 98.819 183.111 283.891 1.00 79.08 O ANISOU 347 O LEU A 62 5740 12044 12262 -1158 11 4 O ATOM 348 CB LEU A 62 96.678 183.571 286.424 1.00 63.79 C ANISOU 348 CB LEU A 62 3805 9924 10507 -1082 36 116 C ATOM 349 CG LEU A 62 96.883 182.074 286.629 1.00 61.27 C ANISOU 349 CG LEU A 62 3465 9532 10281 -1124 25 130 C ATOM 350 CD1 LEU A 62 98.341 181.726 286.908 1.00 59.63 C ANISOU 350 CD1 LEU A 62 3319 9280 10059 -1111 84 139 C ATOM 351 CD2 LEU A 62 95.988 181.623 287.775 1.00 54.60 C ANISOU 351 CD2 LEU A 62 2602 8592 9550 -1121 33 196 C ATOM 352 N ALA A 63 96.667 183.248 283.260 1.00 78.08 N ANISOU 352 N ALA A 63 5496 12000 12172 -1185 -107 -26 N ATOM 353 CA ALA A 63 96.931 182.564 282.000 1.00 55.73 C ANISOU 353 CA ALA A 63 2598 9214 9363 -1261 -173 -41 C ATOM 354 C ALA A 63 97.444 183.501 280.914 1.00 55.81 C ANISOU 354 C ALA A 63 2611 9291 9305 -1249 -189 -60 C ATOM 355 O ALA A 63 97.804 183.025 279.835 1.00 56.86 O ANISOU 355 O ALA A 63 2683 9454 9469 -1321 -244 -55 O ATOM 356 CB ALA A 63 95.676 181.838 281.509 1.00 57.50 C ANISOU 356 CB ALA A 63 2697 9476 9674 -1335 -274 -56 C ATOM 357 N LEU A 64 97.479 184.810 281.163 1.00 54.90 N ANISOU 357 N LEU A 64 2551 9180 9130 -1169 -143 -77 N ATOM 358 CA LEU A 64 98.118 185.759 280.256 1.00 54.89 C ANISOU 358 CA LEU A 64 2554 9217 9085 -1152 -133 -101 C ATOM 359 C LEU A 64 99.607 185.875 280.537 1.00 53.62 C ANISOU 359 C LEU A 64 2502 9022 8848 -1141 -36 -76 C ATOM 360 O LEU A 64 100.416 185.896 279.604 1.00 64.80 O ANISOU 360 O LEU A 64 3904 10478 10240 -1177 -39 -57 O ATOM 361 CB LEU A 64 97.458 187.137 280.375 1.00 54.74 C ANISOU 361 CB LEU A 64 2515 9175 9108 -1071 -122 -117 C ATOM 362 CG LEU A 64 97.874 188.272 279.442 1.00 55.02 C ANISOU 362 CG LEU A 64 2516 9211 9178 -1041 -115 -132 C ATOM 363 CD1 LEU A 64 97.647 187.877 278.000 1.00 56.81 C ANISOU 363 CD1 LEU A 64 2619 9507 9459 -1099 -232 -186 C ATOM 364 CD2 LEU A 64 97.113 189.547 279.767 1.00 55.00 C ANISOU 364 CD2 LEU A 64 2470 9173 9256 -961 -104 -58 C ATOM 365 N ALA A 65 99.972 185.941 281.819 1.00 82.29 N ANISOU 365 N ALA A 65 6234 12589 12444 -1099 44 -63 N ATOM 366 CA ALA A 65 101.378 185.980 282.207 1.00 81.20 C ANISOU 366 CA ALA A 65 6194 12427 12232 -1088 125 -44 C ATOM 367 C ALA A 65 102.073 184.666 281.881 1.00 51.73 C ANISOU 367 C ALA A 65 2422 8677 8556 -1138 107 -3 C ATOM 368 O ALA A 65 103.197 184.657 281.359 1.00 51.65 O ANISOU 368 O ALA A 65 2425 8666 8535 -1148 139 26 O ATOM 369 CB ALA A 65 101.500 186.288 283.699 1.00 50.21 C ANISOU 369 CB ALA A 65 2335 8430 8312 -1046 195 -35 C ATOM 370 N ASP A 66 101.421 183.543 282.198 1.00 67.81 N ANISOU 370 N ASP A 66 4395 10676 10692 -1170 64 1 N ATOM 371 CA ASP A 66 101.996 182.235 281.907 1.00 53.20 C ANISOU 371 CA ASP A 66 2478 8768 8969 -1221 59 11 C ATOM 372 C ASP A 66 102.334 182.099 280.435 1.00 58.94 C ANISOU 372 C ASP A 66 3126 9500 9770 -1282 17 1 C ATOM 373 O ASP A 66 103.216 181.317 280.066 1.00 60.48 O ANISOU 373 O ASP A 66 3313 9586 10079 -1298 50 -33 O ATOM 374 CB ASP A 66 101.030 181.124 282.331 1.00 85.04 C ANISOU 374 CB ASP A 66 6462 12724 13125 -1250 17 2 C ATOM 375 CG ASP A 66 100.882 181.018 283.839 1.00 88.16 C ANISOU 375 CG ASP A 66 6918 13056 13524 -1196 66 27 C ATOM 376 OD1 ASP A 66 101.541 181.796 284.560 1.00 92.01 O ANISOU 376 OD1 ASP A 66 7468 13537 13953 -1142 127 44 O ATOM 377 OD2 ASP A 66 100.107 180.154 284.304 1.00 87.94 O ANISOU 377 OD2 ASP A 66 6852 12941 13619 -1213 43 38 O ATOM 378 N LEU A 67 101.654 182.860 279.580 1.00 54.95 N ANISOU 378 N LEU A 67 2584 9075 9219 -1302 -50 4 N ATOM 379 CA LEU A 67 101.934 182.801 278.152 1.00 89.16 C ANISOU 379 CA LEU A 67 6826 13408 13644 -1373 -102 -10 C ATOM 380 C LEU A 67 103.253 183.497 277.815 1.00 80.00 C ANISOU 380 C LEU A 67 5716 12226 12455 -1340 -20 10 C ATOM 381 O LEU A 67 104.006 183.026 276.953 1.00 72.29 O ANISOU 381 O LEU A 67 4708 11160 11599 -1382 2 -89 O ATOM 382 CB LEU A 67 100.759 183.410 277.386 1.00 57.30 C ANISOU 382 CB LEU A 67 2726 9471 9576 -1400 -216 6 C ATOM 383 CG LEU A 67 100.638 183.177 275.883 1.00 59.21 C ANISOU 383 CG LEU A 67 2835 9704 9960 -1501 -324 -41 C ATOM 384 CD1 LEU A 67 101.208 184.371 275.127 1.00 71.50 C ANISOU 384 CD1 LEU A 67 4392 11265 11508 -1468 -311 -9 C ATOM 385 CD2 LEU A 67 101.324 181.877 275.473 1.00 68.83 C ANISOU 385 CD2 LEU A 67 4044 10784 11325 -1571 -285 -223 C ATOM 386 N ALA A 68 103.565 184.601 278.502 1.00 73.06 N ANISOU 386 N ALA A 68 4955 11392 11413 -1258 45 68 N ATOM 387 CA ALA A 68 104.786 185.347 278.202 1.00 85.94 C ANISOU 387 CA ALA A 68 6635 12996 13021 -1230 127 104 C ATOM 388 C ALA A 68 106.031 184.533 278.524 1.00 53.09 C ANISOU 388 C ALA A 68 2489 8759 8925 -1227 207 65 C ATOM 389 O ALA A 68 107.015 184.571 277.776 1.00 53.46 O ANISOU 389 O ALA A 68 2518 8749 9046 -1241 266 7 O ATOM 390 CB ALA A 68 104.800 186.667 278.969 1.00 52.06 C ANISOU 390 CB ALA A 68 2465 8779 8538 -1161 186 135 C ATOM 391 N VAL A 69 106.011 183.791 279.636 1.00 52.56 N ANISOU 391 N VAL A 69 2459 8677 8834 -1203 221 58 N ATOM 392 CA VAL A 69 107.152 182.948 279.990 1.00 56.59 C ANISOU 392 CA VAL A 69 2981 9104 9417 -1185 290 23 C ATOM 393 C VAL A 69 107.451 181.956 278.877 1.00 59.05 C ANISOU 393 C VAL A 69 3223 9286 9929 -1234 297 -112 C ATOM 394 O VAL A 69 108.614 181.717 278.530 1.00 60.13 O ANISOU 394 O VAL A 69 3367 9354 10124 -1223 380 -187 O ATOM 395 CB VAL A 69 106.898 182.217 281.319 1.00 52.05 C ANISOU 395 CB VAL A 69 2436 8513 8829 -1154 291 32 C ATOM 396 CG1 VAL A 69 107.702 180.916 281.366 1.00 52.87 C ANISOU 396 CG1 VAL A 69 2511 8475 9103 -1144 336 -23 C ATOM 397 CG2 VAL A 69 107.269 183.099 282.464 1.00 97.09 C ANISOU 397 CG2 VAL A 69 8253 14291 14344 -1100 332 71 C ATOM 398 N LEU A 70 106.408 181.369 278.295 1.00 55.33 N ANISOU 398 N LEU A 70 2680 8787 9557 -1298 219 -179 N ATOM 399 CA LEU A 70 106.622 180.370 277.263 1.00 57.08 C ANISOU 399 CA LEU A 70 2833 8896 9957 -1368 235 -374 C ATOM 400 C LEU A 70 107.111 180.994 275.970 1.00 68.15 C ANISOU 400 C LEU A 70 4216 10337 11340 -1419 262 -507 C ATOM 401 O LEU A 70 107.759 180.309 275.172 1.00 67.91 O ANISOU 401 O LEU A 70 4157 10239 11408 -1473 331 -719 O ATOM 402 CB LEU A 70 105.334 179.582 277.038 1.00 58.38 C ANISOU 402 CB LEU A 70 2925 9037 10218 -1441 138 -427 C ATOM 403 CG LEU A 70 104.875 178.847 278.300 1.00 67.87 C ANISOU 403 CG LEU A 70 4146 10185 11458 -1398 135 -335 C ATOM 404 CD1 LEU A 70 103.529 178.178 278.100 1.00 68.49 C ANISOU 404 CD1 LEU A 70 4153 10247 11623 -1474 42 -376 C ATOM 405 CD2 LEU A 70 105.922 177.828 278.734 1.00 69.02 C ANISOU 405 CD2 LEU A 70 4301 10176 11747 -1360 239 -393 C ATOM 406 N LEU A 71 106.837 182.280 275.754 1.00 57.07 N ANISOU 406 N LEU A 71 2827 9047 9810 -1406 227 -409 N ATOM 407 CA LEU A 71 107.357 182.944 274.566 1.00 69.42 C ANISOU 407 CA LEU A 71 4377 10668 11330 -1455 271 -554 C ATOM 408 C LEU A 71 108.881 183.042 274.584 1.00 69.93 C ANISOU 408 C LEU A 71 4506 10687 11376 -1420 422 -620 C ATOM 409 O LEU A 71 109.495 183.166 273.518 1.00 69.82 O ANISOU 409 O LEU A 71 4483 10718 11329 -1487 496 -822 O ATOM 410 CB LEU A 71 106.721 184.330 274.416 1.00 57.25 C ANISOU 410 CB LEU A 71 2828 9239 9686 -1435 212 -420 C ATOM 411 CG LEU A 71 105.316 184.371 273.810 1.00 58.53 C ANISOU 411 CG LEU A 71 2892 9486 9859 -1498 59 -431 C ATOM 412 CD1 LEU A 71 104.849 185.802 273.628 1.00 58.20 C ANISOU 412 CD1 LEU A 71 2830 9537 9747 -1459 25 -308 C ATOM 413 CD2 LEU A 71 105.305 183.647 272.485 1.00 60.64 C ANISOU 413 CD2 LEU A 71 3096 9823 10122 -1634 32 -720 C ATOM 414 N THR A 72 109.504 182.974 275.765 1.00 69.13 N ANISOU 414 N THR A 72 4469 10531 11267 -1328 468 -468 N ATOM 415 CA THR A 72 110.959 182.962 275.870 1.00 55.53 C ANISOU 415 CA THR A 72 2795 8766 9537 -1289 596 -516 C ATOM 416 C THR A 72 111.551 181.567 275.714 1.00 85.59 C ANISOU 416 C THR A 72 6563 12458 13501 -1305 658 -677 C ATOM 417 O THR A 72 112.743 181.446 275.405 1.00 86.11 O ANISOU 417 O THR A 72 6641 12488 13587 -1295 774 -785 O ATOM 418 CB THR A 72 111.409 183.549 277.214 1.00 53.77 C ANISOU 418 CB THR A 72 2647 8573 9211 -1195 607 -292 C ATOM 419 OG1 THR A 72 111.039 182.664 278.280 1.00 53.51 O ANISOU 419 OG1 THR A 72 2606 8517 9207 -1163 556 -211 O ATOM 420 CG2 THR A 72 110.776 184.904 277.444 1.00 52.75 C ANISOU 420 CG2 THR A 72 2553 8534 8957 -1179 564 -138 C ATOM 421 N ALA A 73 110.743 180.525 275.902 1.00 57.48 N ANISOU 421 N ALA A 73 2949 8828 10063 -1329 594 -703 N ATOM 422 CA ALA A 73 111.227 179.151 275.784 1.00 58.83 C ANISOU 422 CA ALA A 73 3070 8854 10427 -1342 666 -857 C ATOM 423 C ALA A 73 111.989 178.846 274.497 1.00 73.06 C ANISOU 423 C ALA A 73 4840 10626 12295 -1420 781 -1141 C ATOM 424 O ALA A 73 112.996 178.122 274.577 1.00 71.80 O ANISOU 424 O ALA A 73 4665 10355 12260 -1386 896 -1224 O ATOM 425 CB ALA A 73 110.050 178.177 275.938 1.00 59.76 C ANISOU 425 CB ALA A 73 3130 8901 10674 -1387 582 -876 C ATOM 426 N PRO A 74 111.595 179.327 273.309 1.00 76.77 N ANISOU 426 N PRO A 74 5292 11201 12676 -1529 766 -1308 N ATOM 427 CA PRO A 74 112.388 178.999 272.111 1.00 81.58 C ANISOU 427 CA PRO A 74 5879 11812 13307 -1625 901 -1612 C ATOM 428 C PRO A 74 113.812 179.514 272.177 1.00 78.78 C ANISOU 428 C PRO A 74 5579 11460 12894 -1560 1040 -1605 C ATOM 429 O PRO A 74 114.660 179.055 271.401 1.00 78.39 O ANISOU 429 O PRO A 74 5513 11376 12897 -1617 1183 -1842 O ATOM 430 CB PRO A 74 111.608 179.667 270.967 1.00 86.19 C ANISOU 430 CB PRO A 74 6443 12585 13720 -1762 831 -1746 C ATOM 431 CG PRO A 74 110.245 179.884 271.502 1.00 63.17 C ANISOU 431 CG PRO A 74 3507 9705 10789 -1741 650 -1552 C ATOM 432 CD PRO A 74 110.425 180.154 272.960 1.00 61.09 C ANISOU 432 CD PRO A 74 3297 9358 10555 -1583 633 -1247 C ATOM 433 N PHE A 75 114.102 180.446 273.080 1.00 60.35 N ANISOU 433 N PHE A 75 3311 9168 10451 -1453 1009 -1350 N ATOM 434 CA PHE A 75 115.443 180.993 273.203 1.00 66.61 C ANISOU 434 CA PHE A 75 4159 9972 11176 -1396 1127 -1330 C ATOM 435 C PHE A 75 116.324 180.143 274.103 1.00 67.23 C ANISOU 435 C PHE A 75 4222 9922 11399 -1296 1178 -1254 C ATOM 436 O PHE A 75 117.492 179.899 273.779 1.00 68.51 O ANISOU 436 O PHE A 75 4379 10042 11608 -1285 1310 -1373 O ATOM 437 CB PHE A 75 115.378 182.422 273.737 1.00 57.94 C ANISOU 437 CB PHE A 75 3138 8983 9895 -1344 1079 -1110 C ATOM 438 CG PHE A 75 114.684 183.377 272.815 1.00 58.20 C ANISOU 438 CG PHE A 75 3178 9151 9783 -1433 1052 -1177 C ATOM 439 CD1 PHE A 75 114.436 183.038 271.494 1.00 60.00 C ANISOU 439 CD1 PHE A 75 3357 9451 9991 -1567 1087 -1445 C ATOM 440 CD2 PHE A 75 114.286 184.620 273.268 1.00 83.84 C ANISOU 440 CD2 PHE A 75 6476 12473 12907 -1391 998 -980 C ATOM 441 CE1 PHE A 75 113.800 183.919 270.646 1.00 60.46 C ANISOU 441 CE1 PHE A 75 3409 9685 9878 -1661 1051 -1497 C ATOM 442 CE2 PHE A 75 113.651 185.509 272.425 1.00 84.04 C ANISOU 442 CE2 PHE A 75 6492 12634 12805 -1467 979 -1030 C ATOM 443 CZ PHE A 75 113.409 185.157 271.111 1.00 85.80 C ANISOU 443 CZ PHE A 75 6659 12962 12978 -1603 997 -1281 C ATOM 444 N PHE A 76 115.780 179.682 275.226 1.00 58.94 N ANISOU 444 N PHE A 76 3159 8825 10411 -1228 1079 -1060 N ATOM 445 CA PHE A 76 116.571 178.849 276.120 1.00 59.08 C ANISOU 445 CA PHE A 76 3147 8748 10551 -1139 1119 -980 C ATOM 446 C PHE A 76 116.855 177.496 275.482 1.00 80.02 C ANISOU 446 C PHE A 76 5715 11232 13456 -1171 1221 -1208 C ATOM 447 O PHE A 76 117.939 176.933 275.666 1.00 80.88 O ANISOU 447 O PHE A 76 5790 11257 13683 -1112 1322 -1238 O ATOM 448 CB PHE A 76 115.854 178.678 277.460 1.00 61.92 C ANISOU 448 CB PHE A 76 3515 9127 10886 -1080 998 -743 C ATOM 449 CG PHE A 76 115.791 179.933 278.291 1.00 56.05 C ANISOU 449 CG PHE A 76 2850 8544 9902 -1043 927 -526 C ATOM 450 CD1 PHE A 76 115.972 181.186 277.727 1.00 58.84 C ANISOU 450 CD1 PHE A 76 3262 8989 10106 -1070 947 -532 C ATOM 451 CD2 PHE A 76 115.557 179.851 279.648 1.00 55.10 C ANISOU 451 CD2 PHE A 76 2744 8482 9708 -990 856 -340 C ATOM 452 CE1 PHE A 76 115.909 182.327 278.499 1.00 53.76 C ANISOU 452 CE1 PHE A 76 2686 8464 9276 -1040 898 -342 C ATOM 453 CE2 PHE A 76 115.495 180.989 280.419 1.00 68.95 C ANISOU 453 CE2 PHE A 76 4568 10392 11238 -974 806 -180 C ATOM 454 CZ PHE A 76 115.673 182.229 279.847 1.00 52.84 C ANISOU 454 CZ PHE A 76 2582 8415 9080 -995 828 -170 C ATOM 455 N LEU A 77 115.894 176.969 274.716 1.00 62.36 N ANISOU 455 N LEU A 77 3438 8947 11310 -1269 1201 -1378 N ATOM 456 CA LEU A 77 116.118 175.729 273.978 1.00 64.62 C ANISOU 456 CA LEU A 77 3646 9069 11839 -1326 1320 -1641 C ATOM 457 C LEU A 77 117.241 175.889 272.969 1.00 73.70 C ANISOU 457 C LEU A 77 4798 10230 12974 -1370 1487 -1872 C ATOM 458 O LEU A 77 118.088 175.001 272.813 1.00 67.16 O ANISOU 458 O LEU A 77 3917 9253 12348 -1345 1628 -2003 O ATOM 459 CB LEU A 77 114.838 175.311 273.268 1.00 65.75 C ANISOU 459 CB LEU A 77 3750 9204 12027 -1456 1257 -1802 C ATOM 460 CG LEU A 77 113.814 174.643 274.166 1.00 69.63 C ANISOU 460 CG LEU A 77 4212 9609 12634 -1424 1142 -1645 C ATOM 461 CD1 LEU A 77 112.651 174.141 273.331 1.00 71.17 C ANISOU 461 CD1 LEU A 77 4361 9794 12888 -1571 1092 -1844 C ATOM 462 CD2 LEU A 77 114.486 173.511 274.923 1.00 70.51 C ANISOU 462 CD2 LEU A 77 4272 9518 13001 -1330 1232 -1599 C ATOM 463 N HIS A 78 117.244 177.011 272.251 1.00 75.16 N ANISOU 463 N HIS A 78 5043 10589 12927 -1438 1484 -1931 N ATOM 464 CA HIS A 78 118.343 177.310 271.343 1.00 78.40 C ANISOU 464 CA HIS A 78 5473 11038 13276 -1484 1650 -2135 C ATOM 465 C HIS A 78 119.657 177.442 272.106 1.00 80.34 C ANISOU 465 C HIS A 78 5738 11241 13548 -1348 1716 -1984 C ATOM 466 O HIS A 78 120.673 176.846 271.727 1.00 82.72 O ANISOU 466 O HIS A 78 6004 11446 13979 -1338 1873 -2141 O ATOM 467 CB HIS A 78 118.023 178.586 270.562 1.00 79.09 C ANISOU 467 CB HIS A 78 5627 11339 13086 -1580 1623 -2182 C ATOM 468 CG HIS A 78 119.215 179.449 270.300 1.00 78.92 C ANISOU 468 CG HIS A 78 5671 11397 12919 -1559 1742 -2195 C ATOM 469 ND1 HIS A 78 119.975 179.346 269.154 1.00 80.94 N ANISOU 469 ND1 HIS A 78 5932 11683 13140 -1660 1923 -2481 N ATOM 470 CD2 HIS A 78 119.780 180.430 271.041 1.00 78.64 C ANISOU 470 CD2 HIS A 78 5703 11418 12759 -1461 1713 -1964 C ATOM 471 CE1 HIS A 78 120.955 180.230 269.201 1.00 80.79 C ANISOU 471 CE1 HIS A 78 5983 11730 12984 -1616 1996 -2414 C ATOM 472 NE2 HIS A 78 120.861 180.899 270.336 1.00 79.34 N ANISOU 472 NE2 HIS A 78 5835 11560 12750 -1497 1868 -2106 N ATOM 473 N PHE A 79 119.648 178.216 273.197 1.00 63.26 N ANISOU 473 N PHE A 79 3624 9156 11256 -1251 1598 -1683 N ATOM 474 CA PHE A 79 120.827 178.335 274.050 1.00 62.66 C ANISOU 474 CA PHE A 79 3554 9074 11179 -1135 1630 -1521 C ATOM 475 C PHE A 79 121.229 176.985 274.630 1.00 63.85 C ANISOU 475 C PHE A 79 3612 9058 11591 -1058 1669 -1503 C ATOM 476 O PHE A 79 122.416 176.742 274.874 1.00 64.43 O ANISOU 476 O PHE A 79 3653 9098 11731 -987 1754 -1486 O ATOM 477 CB PHE A 79 120.549 179.359 275.160 1.00 87.54 C ANISOU 477 CB PHE A 79 6769 12357 14134 -1074 1490 -1220 C ATOM 478 CG PHE A 79 121.655 179.494 276.193 1.00 85.30 C ANISOU 478 CG PHE A 79 6481 12114 13816 -973 1493 -1036 C ATOM 479 CD1 PHE A 79 122.991 179.572 275.818 1.00 83.12 C ANISOU 479 CD1 PHE A 79 6194 11836 13553 -955 1619 -1127 C ATOM 480 CD2 PHE A 79 121.342 179.592 277.548 1.00 83.52 C ANISOU 480 CD2 PHE A 79 6259 11957 13519 -909 1368 -780 C ATOM 481 CE1 PHE A 79 123.992 179.708 276.777 1.00 80.26 C ANISOU 481 CE1 PHE A 79 5809 11538 13147 -871 1607 -955 C ATOM 482 CE2 PHE A 79 122.339 179.733 278.505 1.00 82.81 C ANISOU 482 CE2 PHE A 79 6149 11949 13365 -837 1363 -627 C ATOM 483 CZ PHE A 79 123.662 179.791 278.118 1.00 59.07 C ANISOU 483 CZ PHE A 79 3118 8941 10385 -816 1476 -707 C ATOM 484 N LEU A 80 120.262 176.084 274.823 1.00 76.94 N ANISOU 484 N LEU A 80 5220 10605 13410 -1072 1614 -1512 N ATOM 485 CA LEU A 80 120.563 174.774 275.389 1.00 77.63 C ANISOU 485 CA LEU A 80 5214 10508 13772 -998 1660 -1488 C ATOM 486 C LEU A 80 121.325 173.889 274.409 1.00 77.14 C ANISOU 486 C LEU A 80 5086 10280 13944 -1028 1857 -1773 C ATOM 487 O LEU A 80 122.110 173.033 274.831 1.00 76.42 O ANISOU 487 O LEU A 80 4919 10047 14069 -939 1939 -1741 O ATOM 488 CB LEU A 80 119.268 174.083 275.820 1.00 79.46 C ANISOU 488 CB LEU A 80 5417 10654 14119 -1017 1559 -1431 C ATOM 489 CG LEU A 80 119.369 173.055 276.945 1.00 66.38 C ANISOU 489 CG LEU A 80 3691 8861 12670 -916 1545 -1266 C ATOM 490 CD1 LEU A 80 119.879 173.737 278.181 1.00 64.69 C ANISOU 490 CD1 LEU A 80 3513 8811 12256 -820 1453 -984 C ATOM 491 CD2 LEU A 80 118.022 172.404 277.213 1.00 69.21 C ANISOU 491 CD2 LEU A 80 4028 9127 13142 -957 1462 -1244 C ATOM 492 N THR A 81 121.112 174.072 273.110 1.00 69.05 N ANISOU 492 N THR A 81 4083 9277 12877 -1158 1943 -2056 N ATOM 493 CA THR A 81 121.702 173.204 272.098 1.00 77.73 C ANISOU 493 CA THR A 81 5125 10224 14186 -1218 2151 -2374 C ATOM 494 C THR A 81 122.825 173.861 271.314 1.00 79.61 C ANISOU 494 C THR A 81 5407 10554 14288 -1246 2289 -2521 C ATOM 495 O THR A 81 123.808 173.192 270.978 1.00 82.64 O ANISOU 495 O THR A 81 5740 10805 14855 -1218 2464 -2666 O ATOM 496 CB THR A 81 120.621 172.733 271.120 1.00 78.35 C ANISOU 496 CB THR A 81 5184 10266 14319 -1383 2176 -2649 C ATOM 497 OG1 THR A 81 120.207 173.835 270.306 1.00 72.14 O ANISOU 497 OG1 THR A 81 4474 9706 13229 -1506 2131 -2745 O ATOM 498 CG2 THR A 81 119.418 172.196 271.882 1.00 72.46 C ANISOU 498 CG2 THR A 81 4405 9447 13681 -1367 2024 -2495 C ATOM 499 N TRP A 82 122.696 175.155 271.007 1.00 70.42 N ANISOU 499 N TRP A 82 4336 9606 12815 -1300 2226 -2485 N ATOM 500 CA TRP A 82 123.750 175.863 270.285 1.00 87.11 C ANISOU 500 CA TRP A 82 6504 11815 14778 -1333 2359 -2611 C ATOM 501 C TRP A 82 125.071 175.811 271.044 1.00 89.22 C ANISOU 501 C TRP A 82 6747 12037 15117 -1188 2399 -2447 C ATOM 502 O TRP A 82 126.128 175.564 270.451 1.00 92.47 O ANISOU 502 O TRP A 82 7142 12394 15598 -1193 2573 -2617 O ATOM 503 CB TRP A 82 123.322 177.313 270.027 1.00 83.49 C ANISOU 503 CB TRP A 82 6149 11585 13988 -1399 2268 -2542 C ATOM 504 CG TRP A 82 122.916 177.585 268.600 1.00 83.62 C ANISOU 504 CG TRP A 82 6200 11710 13860 -1585 2363 -2847 C ATOM 505 CD1 TRP A 82 123.396 178.570 267.782 1.00 83.21 C ANISOU 505 CD1 TRP A 82 6231 11820 13564 -1669 2455 -2954 C ATOM 506 CD2 TRP A 82 121.966 176.847 267.820 1.00 85.82 C ANISOU 506 CD2 TRP A 82 6431 11967 14211 -1727 2382 -3089 C ATOM 507 NE1 TRP A 82 122.798 178.494 266.547 1.00 85.35 N ANISOU 507 NE1 TRP A 82 6508 12194 13728 -1858 2528 -3239 N ATOM 508 CE2 TRP A 82 121.918 177.444 266.544 1.00 88.07 C ANISOU 508 CE2 TRP A 82 6768 12434 14261 -1903 2478 -3334 C ATOM 509 CE3 TRP A 82 121.151 175.740 268.078 1.00 72.64 C ANISOU 509 CE3 TRP A 82 4678 10149 12771 -1736 2327 -3125 C ATOM 510 CZ2 TRP A 82 121.086 176.972 265.530 1.00 93.76 C ANISOU 510 CZ2 TRP A 82 7455 13221 14949 -2100 2508 -3615 C ATOM 511 CZ3 TRP A 82 120.327 175.273 267.072 1.00 98.09 C ANISOU 511 CZ3 TRP A 82 7872 13410 15988 -1924 2360 -3411 C ATOM 512 CH2 TRP A 82 120.300 175.889 265.813 1.00 97.51 C ANISOU 512 CH2 TRP A 82 7846 13545 15657 -2111 2442 -3655 C ATOM 513 N GLY A 83 125.028 176.016 272.359 1.00 68.98 N ANISOU 513 N GLY A 83 4173 9508 12528 -1069 2243 -2122 N ATOM 514 CA GLY A 83 126.204 176.008 273.195 1.00 68.88 C ANISOU 514 CA GLY A 83 4121 9503 12547 -944 2251 -1940 C ATOM 515 C GLY A 83 126.570 177.361 273.759 1.00 66.86 C ANISOU 515 C GLY A 83 3943 9453 12007 -919 2154 -1733 C ATOM 516 O GLY A 83 127.283 177.420 274.767 1.00 66.41 O ANISOU 516 O GLY A 83 3845 9450 11936 -820 2101 -1520 O ATOM 517 N THR A 84 126.106 178.448 273.147 1.00 65.80 N ANISOU 517 N THR A 84 3913 9441 11648 -1013 2137 -1793 N ATOM 518 CA THR A 84 126.402 179.782 273.647 1.00 64.01 C ANISOU 518 CA THR A 84 3766 9381 11174 -998 2064 -1608 C ATOM 519 C THR A 84 125.182 180.679 273.491 1.00 74.06 C ANISOU 519 C THR A 84 5126 10744 12268 -1069 1962 -1565 C ATOM 520 O THR A 84 124.301 180.416 272.669 1.00 75.80 O ANISOU 520 O THR A 84 5350 10936 12514 -1156 1977 -1735 O ATOM 521 CB THR A 84 127.601 180.396 272.922 1.00 64.71 C ANISOU 521 CB THR A 84 3895 9520 11170 -1030 2209 -1742 C ATOM 522 OG1 THR A 84 127.951 181.633 273.554 1.00 90.67 O ANISOU 522 OG1 THR A 84 7251 12946 14252 -1009 2140 -1548 O ATOM 523 CG2 THR A 84 127.266 180.648 271.465 1.00 65.62 C ANISOU 523 CG2 THR A 84 4076 9645 11211 -1166 2330 -2030 C ATOM 524 N TRP A 85 125.131 181.735 274.304 1.00 71.28 N ANISOU 524 N TRP A 85 4835 10507 11742 -1036 1861 -1338 N ATOM 525 CA TRP A 85 124.075 182.731 274.176 1.00 59.41 C ANISOU 525 CA TRP A 85 3414 9084 10075 -1093 1780 -1282 C ATOM 526 C TRP A 85 124.235 183.480 272.861 1.00 95.05 C ANISOU 526 C TRP A 85 7998 13656 14461 -1199 1903 -1497 C ATOM 527 O TRP A 85 125.343 183.641 272.351 1.00 96.49 O ANISOU 527 O TRP A 85 8198 13846 14616 -1216 2035 -1616 O ATOM 528 CB TRP A 85 124.103 183.706 275.359 1.00 77.41 C ANISOU 528 CB TRP A 85 5743 11454 12215 -1035 1675 -1008 C ATOM 529 CG TRP A 85 122.862 184.564 275.458 1.00 76.48 C ANISOU 529 CG TRP A 85 5690 11387 11983 -1069 1579 -912 C ATOM 530 CD1 TRP A 85 122.776 185.918 275.272 1.00 76.22 C ANISOU 530 CD1 TRP A 85 5748 11424 11789 -1104 1597 -877 C ATOM 531 CD2 TRP A 85 121.530 184.116 275.751 1.00 55.90 C ANISOU 531 CD2 TRP A 85 3055 8756 9428 -1071 1461 -844 C ATOM 532 NE1 TRP A 85 121.476 186.335 275.438 1.00 54.58 N ANISOU 532 NE1 TRP A 85 3027 8703 9008 -1119 1498 -784 N ATOM 533 CE2 TRP A 85 120.695 185.247 275.730 1.00 54.82 C ANISOU 533 CE2 TRP A 85 2986 8683 9160 -1101 1407 -761 C ATOM 534 CE3 TRP A 85 120.965 182.866 276.025 1.00 56.49 C ANISOU 534 CE3 TRP A 85 3052 8754 9658 -1050 1402 -848 C ATOM 535 CZ2 TRP A 85 119.334 185.165 275.975 1.00 54.31 C ANISOU 535 CZ2 TRP A 85 2907 8619 9109 -1109 1290 -677 C ATOM 536 CZ3 TRP A 85 119.618 182.789 276.265 1.00 55.94 C ANISOU 536 CZ3 TRP A 85 2979 8686 9590 -1067 1286 -772 C ATOM 537 CH2 TRP A 85 118.816 183.927 276.239 1.00 54.85 C ANISOU 537 CH2 TRP A 85 2903 8625 9314 -1095 1227 -684 C ATOM 538 N SER A 86 123.115 183.934 272.296 1.00 59.78 N ANISOU 538 N SER A 86 3566 9245 9904 -1278 1860 -1545 N ATOM 539 CA SER A 86 123.155 184.504 270.955 1.00 60.76 C ANISOU 539 CA SER A 86 3742 9457 9888 -1402 1981 -1766 C ATOM 540 C SER A 86 122.382 185.806 270.807 1.00 59.74 C ANISOU 540 C SER A 86 3687 9449 9564 -1449 1930 -1672 C ATOM 541 O SER A 86 122.226 186.288 269.682 1.00 61.92 O ANISOU 541 O SER A 86 4000 9833 9694 -1566 2018 -1836 O ATOM 542 CB SER A 86 122.633 183.490 269.942 1.00 91.56 C ANISOU 542 CB SER A 86 7579 13334 13877 -1501 2033 -2025 C ATOM 543 OG SER A 86 123.148 182.206 270.223 1.00 92.83 O ANISOU 543 OG SER A 86 7659 13346 14267 -1443 2071 -2087 O ATOM 544 N PHE A 87 121.928 186.409 271.899 1.00 72.95 N ANISOU 544 N PHE A 87 5382 11117 11218 -1369 1804 -1416 N ATOM 545 CA PHE A 87 121.000 187.527 271.804 1.00 72.68 C ANISOU 545 CA PHE A 87 5397 11172 11047 -1404 1752 -1322 C ATOM 546 C PHE A 87 121.520 188.806 272.448 1.00 56.02 C ANISOU 546 C PHE A 87 3377 9080 8828 -1358 1775 -1156 C ATOM 547 O PHE A 87 120.775 189.793 272.529 1.00 66.78 O ANISOU 547 O PHE A 87 4779 10492 10101 -1370 1740 -1052 O ATOM 548 CB PHE A 87 119.656 187.124 272.413 1.00 72.81 C ANISOU 548 CB PHE A 87 5354 11159 11150 -1370 1583 -1188 C ATOM 549 CG PHE A 87 119.159 185.796 271.922 1.00 57.81 C ANISOU 549 CG PHE A 87 3364 9219 9384 -1413 1552 -1345 C ATOM 550 CD1 PHE A 87 118.433 185.704 270.752 1.00 59.13 C ANISOU 550 CD1 PHE A 87 3495 9481 9489 -1538 1562 -1534 C ATOM 551 CD2 PHE A 87 119.431 184.640 272.628 1.00 70.02 C ANISOU 551 CD2 PHE A 87 4856 10644 11106 -1341 1518 -1309 C ATOM 552 CE1 PHE A 87 117.983 184.488 270.301 1.00 60.45 C ANISOU 552 CE1 PHE A 87 3580 9607 9783 -1595 1538 -1700 C ATOM 553 CE2 PHE A 87 118.981 183.422 272.179 1.00 71.30 C ANISOU 553 CE2 PHE A 87 4937 10742 11412 -1385 1508 -1466 C ATOM 554 CZ PHE A 87 118.256 183.345 271.014 1.00 60.48 C ANISOU 554 CZ PHE A 87 3538 9450 9993 -1515 1519 -1671 C ATOM 555 N GLY A 88 122.768 188.827 272.892 1.00 55.90 N ANISOU 555 N GLY A 88 3386 9027 8825 -1310 1836 -1135 N ATOM 556 CA GLY A 88 123.348 190.036 273.429 1.00 70.79 C ANISOU 556 CA GLY A 88 5356 10932 10609 -1286 1869 -1014 C ATOM 557 C GLY A 88 122.841 190.343 274.823 1.00 70.84 C ANISOU 557 C GLY A 88 5360 10906 10650 -1204 1738 -767 C ATOM 558 O GLY A 88 121.976 189.663 275.377 1.00 53.01 O ANISOU 558 O GLY A 88 3041 8618 8481 -1164 1617 -673 O ATOM 559 N LEU A 89 123.407 191.413 275.396 1.00 72.56 N ANISOU 559 N LEU A 89 5649 11133 10789 -1188 1772 -671 N ATOM 560 CA LEU A 89 123.102 191.778 276.777 1.00 74.14 C ANISOU 560 CA LEU A 89 5853 11309 11009 -1122 1671 -455 C ATOM 561 C LEU A 89 121.602 191.915 276.983 1.00 76.82 C ANISOU 561 C LEU A 89 6181 11637 11369 -1114 1577 -357 C ATOM 562 O LEU A 89 121.054 191.426 277.975 1.00 77.93 O ANISOU 562 O LEU A 89 6277 11755 11576 -1060 1460 -207 O ATOM 563 CB LEU A 89 123.809 193.083 277.153 1.00 51.11 C ANISOU 563 CB LEU A 89 3022 8401 7995 -1133 1745 -413 C ATOM 564 CG LEU A 89 123.919 193.343 278.662 1.00 67.94 C ANISOU 564 CG LEU A 89 5148 10514 10153 -1075 1664 -224 C ATOM 565 CD1 LEU A 89 125.168 192.672 279.207 1.00 67.81 C ANISOU 565 CD1 LEU A 89 5070 10515 10178 -1044 1660 -207 C ATOM 566 CD2 LEU A 89 123.897 194.831 279.015 1.00 67.96 C ANISOU 566 CD2 LEU A 89 5245 10508 10070 -1098 1721 -180 C ATOM 567 N ALA A 90 120.921 192.565 276.035 1.00 51.21 N ANISOU 567 N ALA A 90 2969 8424 8063 -1172 1629 -434 N ATOM 568 CA ALA A 90 119.475 192.715 276.125 1.00 50.81 C ANISOU 568 CA ALA A 90 2890 8374 8043 -1167 1542 -347 C ATOM 569 C ALA A 90 118.794 191.360 276.224 1.00 73.11 C ANISOU 569 C ALA A 90 5619 11179 10979 -1147 1422 -345 C ATOM 570 O ALA A 90 117.876 191.172 277.029 1.00 74.43 O ANISOU 570 O ALA A 90 5756 11321 11203 -1104 1308 -197 O ATOM 571 CB ALA A 90 118.952 193.490 274.917 1.00 51.66 C ANISOU 571 CB ALA A 90 3018 8552 8057 -1244 1625 -444 C ATOM 572 N GLY A 91 119.248 190.395 275.422 1.00 70.86 N ANISOU 572 N GLY A 91 5291 10904 10728 -1184 1456 -517 N ATOM 573 CA GLY A 91 118.603 189.090 275.407 1.00 68.15 C ANISOU 573 CA GLY A 91 4861 10533 10501 -1178 1360 -546 C ATOM 574 C GLY A 91 118.575 188.428 276.769 1.00 65.75 C ANISOU 574 C GLY A 91 4528 10184 10271 -1097 1257 -364 C ATOM 575 O GLY A 91 117.515 188.039 277.266 1.00 51.22 O ANISOU 575 O GLY A 91 2651 8336 8474 -1079 1144 -260 O ATOM 576 N CYS A 92 119.739 188.305 277.401 1.00 51.41 N ANISOU 576 N CYS A 92 2723 8363 8449 -1055 1294 -319 N ATOM 577 CA CYS A 92 119.803 187.654 278.699 1.00 50.84 C ANISOU 577 CA CYS A 92 2611 8298 8407 -993 1203 -147 C ATOM 578 C CYS A 92 119.434 188.573 279.847 1.00100.78 C ANISOU 578 C CYS A 92 8983 14657 14653 -963 1144 63 C ATOM 579 O CYS A 92 119.057 188.082 280.917 1.00106.11 O ANISOU 579 O CYS A 92 9642 15369 15306 -931 1047 201 O ATOM 580 CB CYS A 92 121.192 187.076 278.945 1.00 51.44 C ANISOU 580 CB CYS A 92 2650 8382 8511 -963 1258 -175 C ATOM 581 SG CYS A 92 121.062 185.402 279.576 1.00158.61 S ANISOU 581 SG CYS A 92 16117 21956 22191 -923 1182 -141 S ATOM 582 N ARG A 93 119.545 189.887 279.656 1.00 91.41 N ANISOU 582 N ARG A 93 7872 13456 13405 -979 1211 63 N ATOM 583 CA ARG A 93 118.999 190.819 280.636 1.00 81.79 C ANISOU 583 CA ARG A 93 6710 12227 12141 -954 1169 225 C ATOM 584 C ARG A 93 117.474 190.773 280.638 1.00 83.16 C ANISOU 584 C ARG A 93 6890 12386 12320 -953 1078 272 C ATOM 585 O ARG A 93 116.852 190.923 281.698 1.00 83.76 O ANISOU 585 O ARG A 93 7023 12450 12353 -921 998 385 O ATOM 586 CB ARG A 93 119.514 192.232 280.348 1.00 74.35 C ANISOU 586 CB ARG A 93 5841 11267 11142 -978 1287 182 C ATOM 587 CG ARG A 93 119.805 193.096 281.561 1.00 71.45 C ANISOU 587 CG ARG A 93 5522 10879 10745 -966 1301 261 C ATOM 588 CD ARG A 93 120.697 194.287 281.201 1.00 74.07 C ANISOU 588 CD ARG A 93 5924 11214 11004 -1001 1433 184 C ATOM 589 NE ARG A 93 120.593 195.370 282.179 1.00 78.61 N ANISOU 589 NE ARG A 93 6542 11776 11551 -1016 1468 220 N ATOM 590 CZ ARG A 93 119.948 196.515 281.965 1.00 82.69 C ANISOU 590 CZ ARG A 93 7124 12273 12022 -1028 1520 243 C ATOM 591 NH1 ARG A 93 119.355 196.737 280.797 1.00 86.77 N ANISOU 591 NH1 ARG A 93 7660 12788 12519 -1030 1544 234 N ATOM 592 NH2 ARG A 93 119.903 197.443 282.917 1.00 81.06 N ANISOU 592 NH2 ARG A 93 6952 12058 11790 -1048 1558 260 N ATOM 593 N LEU A 94 116.865 190.519 279.475 1.00 48.50 N ANISOU 593 N LEU A 94 2432 8013 7984 -998 1091 164 N ATOM 594 CA LEU A 94 115.414 190.519 279.298 1.00 48.50 C ANISOU 594 CA LEU A 94 2406 8014 8008 -1007 1009 200 C ATOM 595 C LEU A 94 114.770 189.181 279.646 1.00 78.25 C ANISOU 595 C LEU A 94 6125 11803 11805 -1001 891 215 C ATOM 596 O LEU A 94 113.806 189.148 280.413 1.00 81.16 O ANISOU 596 O LEU A 94 6539 12190 12110 -979 795 308 O ATOM 597 CB LEU A 94 115.054 190.895 277.859 1.00 49.47 C ANISOU 597 CB LEU A 94 2501 8148 8147 -1066 1067 46 C ATOM 598 CG LEU A 94 113.663 191.447 277.557 1.00 49.62 C ANISOU 598 CG LEU A 94 2481 8182 8191 -1078 1015 96 C ATOM 599 CD1 LEU A 94 113.698 192.191 276.244 1.00 54.32 C ANISOU 599 CD1 LEU A 94 3075 8836 8729 -1143 1110 -51 C ATOM 600 CD2 LEU A 94 112.606 190.357 277.499 1.00 50.05 C ANISOU 600 CD2 LEU A 94 2449 8249 8318 -1089 880 104 C ATOM 601 N CYS A 95 115.256 188.081 279.063 1.00 74.31 N ANISOU 601 N CYS A 95 5553 11301 11381 -1026 909 89 N ATOM 602 CA CYS A 95 114.585 186.794 279.238 1.00 71.66 C ANISOU 602 CA CYS A 95 5153 10970 11104 -1034 821 69 C ATOM 603 C CYS A 95 114.410 186.452 280.707 1.00 49.22 C ANISOU 603 C CYS A 95 2359 8186 8158 -993 747 194 C ATOM 604 O CYS A 95 113.380 185.901 281.109 1.00 49.22 O ANISOU 604 O CYS A 95 2349 8211 8140 -1002 667 197 O ATOM 605 CB CYS A 95 115.366 185.689 278.533 1.00 72.21 C ANISOU 605 CB CYS A 95 5177 10976 11284 -1050 879 -111 C ATOM 606 SG CYS A 95 115.151 185.693 276.749 1.00 52.71 S ANISOU 606 SG CYS A 95 2674 8473 8879 -1134 939 -363 S ATOM 607 N HIS A 96 115.406 186.776 281.526 1.00 48.65 N ANISOU 607 N HIS A 96 2353 8136 7995 -955 777 257 N ATOM 608 CA HIS A 96 115.263 186.530 282.951 1.00 67.16 C ANISOU 608 CA HIS A 96 4720 10550 10246 -943 732 283 C ATOM 609 C HIS A 96 114.319 187.532 283.603 1.00 66.77 C ANISOU 609 C HIS A 96 4748 10536 10085 -951 698 325 C ATOM 610 O HIS A 96 113.631 187.192 284.572 1.00 67.06 O ANISOU 610 O HIS A 96 4780 10629 10069 -968 662 254 O ATOM 611 CB HIS A 96 116.636 186.547 283.613 1.00 67.17 C ANISOU 611 CB HIS A 96 4708 10574 10238 -922 785 298 C ATOM 612 CG HIS A 96 117.497 185.390 283.219 1.00 49.59 C ANISOU 612 CG HIS A 96 2385 8341 8116 -911 819 234 C ATOM 613 ND1 HIS A 96 118.824 185.528 282.878 1.00 75.53 N ANISOU 613 ND1 HIS A 96 5645 11615 11437 -894 897 229 N ATOM 614 CD2 HIS A 96 117.215 184.072 283.104 1.00 71.92 C ANISOU 614 CD2 HIS A 96 5125 11157 11046 -912 799 168 C ATOM 615 CE1 HIS A 96 119.326 184.344 282.579 1.00 75.97 C ANISOU 615 CE1 HIS A 96 5600 11670 11595 -882 921 161 C ATOM 616 NE2 HIS A 96 118.369 183.442 282.707 1.00 74.29 N ANISOU 616 NE2 HIS A 96 5345 11444 11436 -892 865 130 N ATOM 617 N TYR A 97 114.254 188.760 283.087 1.00 47.26 N ANISOU 617 N TYR A 97 2338 8010 7610 -941 731 402 N ATOM 618 CA TYR A 97 113.312 189.722 283.646 1.00 46.77 C ANISOU 618 CA TYR A 97 2334 7985 7451 -947 709 436 C ATOM 619 C TYR A 97 111.876 189.315 283.335 1.00 46.84 C ANISOU 619 C TYR A 97 2323 8056 7418 -975 638 355 C ATOM 620 O TYR A 97 111.007 189.354 284.213 1.00 85.56 O ANISOU 620 O TYR A 97 7236 13020 12253 -1000 622 228 O ATOM 621 CB TYR A 97 113.612 191.127 283.122 1.00 46.41 C ANISOU 621 CB TYR A 97 2342 7820 7472 -919 787 526 C ATOM 622 CG TYR A 97 112.748 192.192 283.756 1.00 46.04 C ANISOU 622 CG TYR A 97 2347 7808 7340 -921 783 572 C ATOM 623 CD1 TYR A 97 112.561 192.227 285.132 1.00 45.99 C ANISOU 623 CD1 TYR A 97 2357 7918 7200 -952 764 526 C ATOM 624 CD2 TYR A 97 112.121 193.159 282.982 1.00 45.89 C ANISOU 624 CD2 TYR A 97 2353 7742 7343 -907 809 615 C ATOM 625 CE1 TYR A 97 111.773 193.190 285.720 1.00 45.79 C ANISOU 625 CE1 TYR A 97 2373 7978 7046 -988 781 453 C ATOM 626 CE2 TYR A 97 111.331 194.131 283.562 1.00 45.72 C ANISOU 626 CE2 TYR A 97 2368 7828 7174 -929 812 605 C ATOM 627 CZ TYR A 97 111.160 194.141 284.933 1.00 78.25 C ANISOU 627 CZ TYR A 97 6507 12083 11143 -983 806 471 C ATOM 628 OH TYR A 97 110.372 195.101 285.527 1.00 78.00 O ANISOU 628 OH TYR A 97 6511 12126 10999 -1045 863 246 O ATOM 629 N ILE A 98 111.616 188.908 282.088 1.00 59.67 N ANISOU 629 N ILE A 98 3899 9627 9144 -976 615 374 N ATOM 630 CA ILE A 98 110.296 188.397 281.717 1.00 60.60 C ANISOU 630 CA ILE A 98 3954 9778 9293 -1007 547 304 C ATOM 631 C ILE A 98 109.956 187.163 282.546 1.00 61.55 C ANISOU 631 C ILE A 98 4055 9924 9409 -1016 505 213 C ATOM 632 O ILE A 98 108.834 187.021 283.054 1.00 47.92 O ANISOU 632 O ILE A 98 2312 8208 7687 -1026 470 135 O ATOM 633 CB ILE A 98 110.245 188.102 280.201 1.00 61.02 C ANISOU 633 CB ILE A 98 3887 9746 9553 -1034 551 287 C ATOM 634 CG1 ILE A 98 109.699 189.300 279.414 1.00 60.96 C ANISOU 634 CG1 ILE A 98 3864 9715 9584 -1035 567 328 C ATOM 635 CG2 ILE A 98 109.376 186.887 279.914 1.00 62.90 C ANISOU 635 CG2 ILE A 98 4028 9992 9878 -1074 472 214 C ATOM 636 CD1 ILE A 98 110.121 190.665 279.925 1.00 48.35 C ANISOU 636 CD1 ILE A 98 2367 8099 7906 -994 642 414 C ATOM 637 N CYS A 99 110.922 186.257 282.706 1.00 62.34 N ANISOU 637 N CYS A 99 4112 9986 9588 -1008 531 206 N ATOM 638 CA CYS A 99 110.713 185.096 283.560 1.00 61.54 C ANISOU 638 CA CYS A 99 3947 9861 9575 -1010 516 139 C ATOM 639 C CYS A 99 110.535 185.513 285.012 1.00 58.88 C ANISOU 639 C CYS A 99 3643 9534 9193 -1001 536 95 C ATOM 640 O CYS A 99 109.701 184.957 285.734 1.00 54.99 O ANISOU 640 O CYS A 99 3110 9000 8784 -1002 511 65 O ATOM 641 CB CYS A 99 111.893 184.139 283.428 1.00 49.25 C ANISOU 641 CB CYS A 99 2327 8271 8115 -998 555 135 C ATOM 642 SG CYS A 99 111.974 183.262 281.845 1.00 58.63 S ANISOU 642 SG CYS A 99 3393 9384 9501 -1033 562 96 S ATOM 643 N GLY A 100 111.305 186.497 285.462 1.00 62.31 N ANISOU 643 N GLY A 100 4145 10011 9520 -996 585 103 N ATOM 644 CA GLY A 100 111.216 186.886 286.854 1.00 65.84 C ANISOU 644 CA GLY A 100 4615 10450 9950 -1002 615 40 C ATOM 645 C GLY A 100 109.943 187.637 287.191 1.00 69.62 C ANISOU 645 C GLY A 100 5126 10898 10430 -1011 610 -2 C ATOM 646 O GLY A 100 109.518 187.663 288.353 1.00 74.24 O ANISOU 646 O GLY A 100 5701 11434 11074 -1013 624 -27 O ATOM 647 N VAL A 101 109.281 188.207 286.188 1.00 67.03 N ANISOU 647 N VAL A 101 4819 10590 10060 -1013 589 8 N ATOM 648 CA VAL A 101 108.094 188.977 286.501 1.00 63.10 C ANISOU 648 CA VAL A 101 4335 10054 9588 -1014 594 -34 C ATOM 649 C VAL A 101 106.865 188.072 286.535 1.00 47.42 C ANISOU 649 C VAL A 101 2273 8024 7721 -1007 526 -19 C ATOM 650 O VAL A 101 105.959 188.287 287.344 1.00 86.73 O ANISOU 650 O VAL A 101 7234 12956 12764 -1002 527 -14 O ATOM 651 CB VAL A 101 107.956 190.129 285.505 1.00 60.95 C ANISOU 651 CB VAL A 101 4109 9822 9227 -1017 615 -46 C ATOM 652 CG1 VAL A 101 106.564 190.132 284.875 1.00 46.92 C ANISOU 652 CG1 VAL A 101 2285 8024 7519 -1007 563 -69 C ATOM 653 CG2 VAL A 101 108.267 191.431 286.206 1.00 46.24 C ANISOU 653 CG2 VAL A 101 2313 7944 7313 -1029 699 -78 C ATOM 654 N SER A 102 106.854 186.994 285.727 1.00 47.90 N ANISOU 654 N SER A 102 2280 8101 7818 -1012 470 5 N ATOM 655 CA SER A 102 105.725 186.066 285.729 1.00 48.52 C ANISOU 655 CA SER A 102 2281 8145 8009 -1019 406 17 C ATOM 656 C SER A 102 105.691 185.276 287.027 1.00100.47 C ANISOU 656 C SER A 102 8818 14663 14693 -1015 416 45 C ATOM 657 O SER A 102 104.612 185.081 287.596 1.00101.24 O ANISOU 657 O SER A 102 8874 14725 14868 -1017 391 65 O ATOM 658 CB SER A 102 105.757 185.172 284.519 1.00 49.10 C ANISOU 658 CB SER A 102 2305 8246 8103 -1043 352 31 C ATOM 659 OG SER A 102 105.458 185.894 283.337 1.00 50.15 O ANISOU 659 OG SER A 102 2461 8447 8145 -1055 326 25 O ATOM 660 N MET A 103 106.856 184.853 287.541 1.00 48.81 N ANISOU 660 N MET A 103 2276 8116 8155 -1008 454 55 N ATOM 661 CA MET A 103 106.867 184.185 288.839 1.00 49.18 C ANISOU 661 CA MET A 103 2287 8103 8296 -1000 464 95 C ATOM 662 C MET A 103 106.216 185.061 289.894 1.00 48.87 C ANISOU 662 C MET A 103 2281 8049 8240 -1002 489 105 C ATOM 663 O MET A 103 105.395 184.599 290.697 1.00 49.28 O ANISOU 663 O MET A 103 2317 8033 8376 -996 468 163 O ATOM 664 CB MET A 103 108.281 183.844 289.259 1.00 49.31 C ANISOU 664 CB MET A 103 2294 8134 8306 -989 506 98 C ATOM 665 CG MET A 103 108.292 183.305 290.740 1.00 84.78 C ANISOU 665 CG MET A 103 6768 12558 12885 -974 514 161 C ATOM 666 SD MET A 103 109.878 183.022 291.577 1.00 50.16 S ANISOU 666 SD MET A 103 2353 8200 8504 -960 560 174 S ATOM 667 CE MET A 103 110.501 184.695 291.706 1.00 49.32 C ANISOU 667 CE MET A 103 2318 8187 8234 -994 621 77 C ATOM 668 N TYR A 104 106.614 186.331 289.917 1.00 48.25 N ANISOU 668 N TYR A 104 2269 8010 8054 -1008 538 60 N ATOM 669 CA TYR A 104 106.101 187.273 290.890 1.00 48.04 C ANISOU 669 CA TYR A 104 2272 7967 8013 -1017 579 64 C ATOM 670 C TYR A 104 104.630 187.573 290.634 1.00 69.58 C ANISOU 670 C TYR A 104 4976 10677 10783 -1013 547 85 C ATOM 671 O TYR A 104 103.826 187.577 291.568 1.00 69.96 O ANISOU 671 O TYR A 104 5013 10686 10882 -1014 549 133 O ATOM 672 CB TYR A 104 106.933 188.540 290.857 1.00 47.49 C ANISOU 672 CB TYR A 104 2289 7924 7832 -1028 647 7 C ATOM 673 CG TYR A 104 108.068 188.501 291.865 1.00 65.54 C ANISOU 673 CG TYR A 104 4587 10213 10104 -1044 696 -13 C ATOM 674 CD1 TYR A 104 107.893 188.952 293.166 1.00 67.67 C ANISOU 674 CD1 TYR A 104 4859 10459 10392 -1069 742 -7 C ATOM 675 CD2 TYR A 104 109.273 187.938 291.547 1.00 63.21 C ANISOU 675 CD2 TYR A 104 4282 9946 9789 -1038 695 -34 C ATOM 676 CE1 TYR A 104 108.886 188.878 294.094 1.00 67.91 C ANISOU 676 CE1 TYR A 104 4883 10484 10436 -1087 783 -24 C ATOM 677 CE2 TYR A 104 110.283 187.858 292.456 1.00 63.55 C ANISOU 677 CE2 TYR A 104 4315 9987 9845 -1050 735 -54 C ATOM 678 CZ TYR A 104 110.098 188.330 293.741 1.00 66.57 C ANISOU 678 CZ TYR A 104 4698 10334 10263 -1075 778 -49 C ATOM 679 OH TYR A 104 111.067 188.286 294.705 1.00 68.38 O ANISOU 679 OH TYR A 104 4902 10548 10533 -1089 818 -54 O ATOM 680 N ALA A 105 104.261 187.864 289.382 1.00 69.31 N ANISOU 680 N ALA A 105 4949 10663 10723 -1002 515 59 N ATOM 681 CA ALA A 105 102.863 188.118 289.055 1.00 48.31 C ANISOU 681 CA ALA A 105 2246 7995 8113 -994 476 75 C ATOM 682 C ALA A 105 102.015 186.867 289.297 1.00 49.03 C ANISOU 682 C ALA A 105 2285 8034 8311 -992 409 126 C ATOM 683 O ALA A 105 100.922 186.952 289.870 1.00 55.96 O ANISOU 683 O ALA A 105 3145 8870 9248 -985 396 171 O ATOM 684 CB ALA A 105 102.755 188.617 287.624 1.00 48.21 C ANISOU 684 CB ALA A 105 2246 8021 8051 -983 449 34 C ATOM 685 N SER A 106 102.494 185.692 288.874 1.00 49.36 N ANISOU 685 N SER A 106 2300 8070 8385 -1001 373 123 N ATOM 686 CA SER A 106 101.689 184.482 289.034 1.00 50.18 C ANISOU 686 CA SER A 106 2353 8110 8605 -1008 318 167 C ATOM 687 C SER A 106 101.447 184.168 290.501 1.00 72.66 C ANISOU 687 C SER A 106 5205 10885 11517 -1001 343 239 C ATOM 688 O SER A 106 100.328 183.814 290.886 1.00 73.06 O ANISOU 688 O SER A 106 5223 10890 11645 -1006 315 283 O ATOM 689 CB SER A 106 102.351 183.286 288.355 1.00 50.61 C ANISOU 689 CB SER A 106 2376 8155 8700 -1022 292 153 C ATOM 690 OG SER A 106 102.212 183.338 286.947 1.00 86.62 O ANISOU 690 OG SER A 106 6907 12788 13215 -1046 250 99 O ATOM 691 N VAL A 107 102.481 184.284 291.335 1.00 71.76 N ANISOU 691 N VAL A 107 5123 10773 11368 -997 396 255 N ATOM 692 CA VAL A 107 102.327 183.862 292.722 1.00 50.50 C ANISOU 692 CA VAL A 107 2423 8031 8733 -999 416 332 C ATOM 693 C VAL A 107 101.470 184.851 293.503 1.00 50.37 C ANISOU 693 C VAL A 107 2424 8026 8689 -1008 447 351 C ATOM 694 O VAL A 107 100.751 184.457 294.429 1.00 68.02 O ANISOU 694 O VAL A 107 4636 10221 10987 -1016 446 419 O ATOM 695 CB VAL A 107 103.703 183.659 293.379 1.00 50.41 C ANISOU 695 CB VAL A 107 2422 8037 8696 -996 457 345 C ATOM 696 CG1 VAL A 107 104.364 184.997 293.668 1.00 49.72 C ANISOU 696 CG1 VAL A 107 2381 8022 8487 -1010 518 286 C ATOM 697 CG2 VAL A 107 103.556 182.843 294.637 1.00 51.14 C ANISOU 697 CG2 VAL A 107 2483 8077 8871 -998 459 446 C ATOM 698 N LEU A 108 101.508 186.138 293.144 1.00 49.76 N ANISOU 698 N LEU A 108 2383 8000 8524 -1008 481 294 N ATOM 699 CA LEU A 108 100.686 187.111 293.855 1.00 61.62 C ANISOU 699 CA LEU A 108 3894 9507 10012 -1016 521 311 C ATOM 700 C LEU A 108 99.210 186.944 293.506 1.00 50.31 C ANISOU 700 C LEU A 108 2419 8041 8657 -1003 471 344 C ATOM 701 O LEU A 108 98.346 187.055 294.383 1.00 50.77 O ANISOU 701 O LEU A 108 2457 8078 8754 -1012 490 393 O ATOM 702 CB LEU A 108 101.161 188.538 293.558 1.00 60.87 C ANISOU 702 CB LEU A 108 3843 9464 9820 -1021 583 247 C ATOM 703 CG LEU A 108 102.556 188.964 294.043 1.00 48.71 C ANISOU 703 CG LEU A 108 2341 7967 8199 -1049 650 196 C ATOM 704 CD1 LEU A 108 102.684 190.486 294.105 1.00 48.34 C ANISOU 704 CD1 LEU A 108 2332 7960 8075 -1071 732 142 C ATOM 705 CD2 LEU A 108 102.914 188.331 295.376 1.00 49.15 C ANISOU 705 CD2 LEU A 108 2382 8013 8279 -1073 669 238 C ATOM 706 N LEU A 109 98.899 186.669 292.236 1.00 50.41 N ANISOU 706 N LEU A 109 2404 8059 8690 -988 409 313 N ATOM 707 CA LEU A 109 97.520 186.352 291.879 1.00 51.15 C ANISOU 707 CA LEU A 109 2439 8131 8865 -983 351 337 C ATOM 708 C LEU A 109 97.023 185.139 292.654 1.00 75.85 C ANISOU 708 C LEU A 109 5530 11198 12091 -1002 329 396 C ATOM 709 O LEU A 109 95.879 185.119 293.125 1.00 81.43 O ANISOU 709 O LEU A 109 6196 11881 12861 -1007 322 438 O ATOM 710 CB LEU A 109 97.398 186.106 290.377 1.00 58.67 C ANISOU 710 CB LEU A 109 3355 9122 9814 -980 282 281 C ATOM 711 CG LEU A 109 97.823 187.238 289.446 1.00 50.72 C ANISOU 711 CG LEU A 109 2372 8181 8719 -961 297 226 C ATOM 712 CD1 LEU A 109 97.552 186.842 288.016 1.00 51.16 C ANISOU 712 CD1 LEU A 109 2371 8295 8773 -971 219 172 C ATOM 713 CD2 LEU A 109 97.104 188.526 289.786 1.00 64.92 C ANISOU 713 CD2 LEU A 109 4174 9977 10517 -934 338 254 C ATOM 714 N ILE A 110 97.876 184.123 292.810 1.00 70.68 N ANISOU 714 N ILE A 110 4881 10515 11460 -1013 325 407 N ATOM 715 CA ILE A 110 97.483 182.935 293.561 1.00 68.05 C ANISOU 715 CA ILE A 110 4510 10112 11234 -1030 313 475 C ATOM 716 C ILE A 110 97.333 183.260 295.040 1.00 67.67 C ANISOU 716 C ILE A 110 4475 10058 11179 -1039 370 543 C ATOM 717 O ILE A 110 96.506 182.658 295.737 1.00 68.42 O ANISOU 717 O ILE A 110 4529 10109 11358 -1056 366 605 O ATOM 718 CB ILE A 110 98.491 181.797 293.320 1.00 52.92 C ANISOU 718 CB ILE A 110 2588 8158 9361 -1032 301 479 C ATOM 719 CG1 ILE A 110 98.505 181.428 291.835 1.00 54.00 C ANISOU 719 CG1 ILE A 110 2700 8312 9507 -1040 248 403 C ATOM 720 CG2 ILE A 110 98.163 180.592 294.189 1.00 53.85 C ANISOU 720 CG2 ILE A 110 2664 8191 9604 -1046 300 566 C ATOM 721 CD1 ILE A 110 98.911 179.999 291.545 1.00 53.95 C ANISOU 721 CD1 ILE A 110 2655 8235 9607 -1054 230 412 C ATOM 722 N THR A 111 98.111 184.214 295.546 1.00 52.17 N ANISOU 722 N THR A 111 2562 8146 9115 -1037 428 525 N ATOM 723 CA THR A 111 97.881 184.691 296.903 1.00 52.37 C ANISOU 723 CA THR A 111 2591 8190 9116 -1060 488 568 C ATOM 724 C THR A 111 96.516 185.362 297.007 1.00 52.71 C ANISOU 724 C THR A 111 2609 8234 9183 -1063 498 571 C ATOM 725 O THR A 111 95.719 185.035 297.893 1.00 53.43 O ANISOU 725 O THR A 111 2664 8307 9330 -1085 513 628 O ATOM 726 CB THR A 111 98.998 185.647 297.318 1.00 51.69 C ANISOU 726 CB THR A 111 2555 8169 8916 -1071 553 523 C ATOM 727 OG1 THR A 111 100.205 185.283 296.639 1.00 80.38 O ANISOU 727 OG1 THR A 111 6208 11809 12523 -1054 533 489 O ATOM 728 CG2 THR A 111 99.240 185.554 298.809 1.00 52.15 C ANISOU 728 CG2 THR A 111 2604 8250 8959 -1108 605 574 C ATOM 729 N ALA A 112 96.211 186.274 296.078 1.00 56.22 N ANISOU 729 N ALA A 112 3063 8702 9596 -1039 489 518 N ATOM 730 CA ALA A 112 94.941 186.994 296.125 1.00 52.76 C ANISOU 730 CA ALA A 112 2590 8265 9191 -1032 500 528 C ATOM 731 C ALA A 112 93.756 186.044 295.998 1.00 53.73 C ANISOU 731 C ALA A 112 2641 8343 9430 -1036 440 569 C ATOM 732 O ALA A 112 92.817 186.101 296.801 1.00 54.43 O ANISOU 732 O ALA A 112 2691 8421 9568 -1052 467 611 O ATOM 733 CB ALA A 112 94.897 188.058 295.028 1.00 52.31 C ANISOU 733 CB ALA A 112 2544 8237 9093 -997 493 479 C ATOM 734 N MET A 113 93.779 185.164 294.989 1.00 62.35 N ANISOU 734 N MET A 113 3709 9415 10565 -1031 363 549 N ATOM 735 CA MET A 113 92.706 184.184 294.838 1.00 54.96 C ANISOU 735 CA MET A 113 2699 8441 9743 -1050 308 574 C ATOM 736 C MET A 113 92.498 183.389 296.117 1.00 78.88 C ANISOU 736 C MET A 113 5712 11423 12835 -1082 343 646 C ATOM 737 O MET A 113 91.360 183.174 296.549 1.00 78.40 O ANISOU 737 O MET A 113 5593 11344 12852 -1101 342 680 O ATOM 738 CB MET A 113 93.011 183.224 293.693 1.00 55.13 C ANISOU 738 CB MET A 113 2698 8453 9795 -1059 235 529 C ATOM 739 CG MET A 113 93.087 183.844 292.323 1.00 94.81 C ANISOU 739 CG MET A 113 7718 13543 14761 -1038 189 457 C ATOM 740 SD MET A 113 93.046 182.525 291.092 1.00 93.26 S ANISOU 740 SD MET A 113 7462 13352 14619 -1078 102 399 S ATOM 741 CE MET A 113 93.952 181.243 291.952 1.00 97.28 C ANISOU 741 CE MET A 113 8003 13766 15194 -1098 140 447 C ATOM 742 N SER A 114 93.590 182.943 296.735 1.00 75.72 N ANISOU 742 N SER A 114 5356 11009 12406 -1090 373 674 N ATOM 743 CA SER A 114 93.488 182.158 297.957 1.00 76.40 C ANISOU 743 CA SER A 114 5421 11060 12549 -1120 405 756 C ATOM 744 C SER A 114 93.180 183.029 299.168 1.00 55.94 C ANISOU 744 C SER A 114 2837 8515 9903 -1139 480 782 C ATOM 745 O SER A 114 92.466 182.587 300.077 1.00 56.81 O ANISOU 745 O SER A 114 2904 8610 10073 -1171 505 843 O ATOM 746 CB SER A 114 94.782 181.371 298.172 1.00 75.27 C ANISOU 746 CB SER A 114 5305 10892 12401 -1116 407 789 C ATOM 747 OG SER A 114 94.859 180.857 299.486 1.00 74.71 O ANISOU 747 OG SER A 114 5217 10811 12358 -1142 448 883 O ATOM 748 N LEU A 115 93.697 184.260 299.197 1.00 55.14 N ANISOU 748 N LEU A 115 2784 8475 9691 -1128 525 732 N ATOM 749 CA LEU A 115 93.386 185.184 300.283 1.00 71.03 C ANISOU 749 CA LEU A 115 4798 10541 11651 -1158 608 733 C ATOM 750 C LEU A 115 91.925 185.614 300.260 1.00 73.66 C ANISOU 750 C LEU A 115 5075 10866 12046 -1157 616 735 C ATOM 751 O LEU A 115 91.411 186.087 301.283 1.00 56.55 O ANISOU 751 O LEU A 115 2886 8732 9868 -1192 689 746 O ATOM 752 CB LEU A 115 94.307 186.407 300.200 1.00 68.99 C ANISOU 752 CB LEU A 115 4599 10343 11271 -1153 660 663 C ATOM 753 CG LEU A 115 94.592 187.274 301.427 1.00 54.50 C ANISOU 753 CG LEU A 115 2779 8578 9352 -1205 762 638 C ATOM 754 CD1 LEU A 115 96.007 187.821 301.342 1.00 53.68 C ANISOU 754 CD1 LEU A 115 2733 8519 9145 -1212 792 577 C ATOM 755 CD2 LEU A 115 93.592 188.415 301.534 1.00 56.01 C ANISOU 755 CD2 LEU A 115 2948 8791 9541 -1210 821 606 C ATOM 756 N ASP A 116 91.247 185.438 299.121 1.00 75.45 N ANISOU 756 N ASP A 116 5268 11058 12341 -1123 545 720 N ATOM 757 CA ASP A 116 89.856 185.837 298.939 1.00 77.72 C ANISOU 757 CA ASP A 116 5488 11342 12700 -1114 540 724 C ATOM 758 C ASP A 116 88.864 184.744 299.320 1.00 79.92 C ANISOU 758 C ASP A 116 5691 11580 13094 -1147 515 773 C ATOM 759 O ASP A 116 87.882 185.025 300.016 1.00 81.69 O ANISOU 759 O ASP A 116 5863 11814 13362 -1166 561 795 O ATOM 760 CB ASP A 116 89.611 186.258 297.492 1.00 56.76 C ANISOU 760 CB ASP A 116 2818 8692 10055 -1065 472 682 C ATOM 761 CG ASP A 116 88.147 186.242 297.136 1.00 79.56 C ANISOU 761 CG ASP A 116 5609 11574 13046 -1057 435 695 C ATOM 762 OD1 ASP A 116 87.461 187.244 297.418 1.00 81.36 O ANISOU 762 OD1 ASP A 116 5806 11821 13286 -1037 484 704 O ATOM 763 OD2 ASP A 116 87.675 185.216 296.602 1.00 78.50 O ANISOU 763 OD2 ASP A 116 5421 11419 12987 -1073 360 694 O ATOM 764 N ARG A 117 89.080 183.500 298.881 1.00 58.38 N ANISOU 764 N ARG A 117 2952 8804 10424 -1158 451 786 N ATOM 765 CA ARG A 117 88.179 182.434 299.302 1.00 59.61 C ANISOU 765 CA ARG A 117 3036 8916 10697 -1199 438 832 C ATOM 766 C ARG A 117 88.146 182.274 300.817 1.00101.41 C ANISOU 766 C ARG A 117 8328 14215 15987 -1241 519 897 C ATOM 767 O ARG A 117 87.309 181.520 301.319 1.00103.00 O ANISOU 767 O ARG A 117 8465 14385 16285 -1280 526 942 O ATOM 768 CB ARG A 117 88.566 181.112 298.636 1.00 59.81 C ANISOU 768 CB ARG A 117 3053 8882 10791 -1211 372 833 C ATOM 769 CG ARG A 117 87.457 180.074 298.650 1.00 61.24 C ANISOU 769 CG ARG A 117 3143 9015 11110 -1256 344 854 C ATOM 770 CD ARG A 117 87.911 178.788 298.015 1.00 91.62 C ANISOU 770 CD ARG A 117 6981 12797 15032 -1277 294 846 C ATOM 771 NE ARG A 117 86.880 177.757 298.073 1.00 92.26 N ANISOU 771 NE ARG A 117 6973 12827 15255 -1332 277 861 N ATOM 772 CZ ARG A 117 87.005 176.603 298.721 1.00 92.14 C ANISOU 772 CZ ARG A 117 6941 12730 15338 -1370 304 928 C ATOM 773 NH1 ARG A 117 88.125 176.315 299.374 1.00 90.73 N ANISOU 773 NH1 ARG A 117 6822 12520 15132 -1351 343 996 N ATOM 774 NH2 ARG A 117 86.007 175.729 298.706 1.00 94.06 N ANISOU 774 NH2 ARG A 117 7098 12927 15714 -1427 294 931 N ATOM 775 N SER A 118 89.006 182.981 301.558 1.00 59.35 N ANISOU 775 N SER A 118 3063 8939 10550 -1242 584 898 N ATOM 776 CA SER A 118 88.876 183.052 303.006 1.00 59.94 C ANISOU 776 CA SER A 118 3124 9052 10600 -1294 669 943 C ATOM 777 C SER A 118 88.038 184.229 303.458 1.00 60.29 C ANISOU 777 C SER A 118 3141 9151 10617 -1306 741 905 C ATOM 778 O SER A 118 87.612 184.245 304.614 1.00 64.16 O ANISOU 778 O SER A 118 3598 9677 11104 -1361 816 931 O ATOM 779 CB SER A 118 90.243 183.134 303.694 1.00 63.32 C ANISOU 779 CB SER A 118 3615 9523 10921 -1308 707 957 C ATOM 780 OG SER A 118 90.103 183.043 305.103 1.00 63.94 O ANISOU 780 OG SER A 118 3669 9649 10977 -1370 784 1005 O ATOM 781 N LEU A 119 87.806 185.213 302.593 1.00 59.81 N ANISOU 781 N LEU A 119 3087 9099 10539 -1259 726 849 N ATOM 782 CA LEU A 119 86.857 186.270 302.900 1.00 78.03 C ANISOU 782 CA LEU A 119 5349 11441 12857 -1260 792 826 C ATOM 783 C LEU A 119 85.448 185.943 302.425 1.00 61.49 C ANISOU 783 C LEU A 119 3160 9309 10896 -1245 748 846 C ATOM 784 O LEU A 119 84.489 186.569 302.891 1.00 98.59 O ANISOU 784 O LEU A 119 7796 14029 15633 -1254 809 846 O ATOM 785 CB LEU A 119 87.316 187.594 302.284 1.00 59.50 C ANISOU 785 CB LEU A 119 3049 9122 10436 -1214 812 771 C ATOM 786 CG LEU A 119 86.675 188.842 302.882 1.00 60.06 C ANISOU 786 CG LEU A 119 3089 9235 10496 -1223 916 748 C ATOM 787 CD1 LEU A 119 87.107 188.998 304.324 1.00 60.32 C ANISOU 787 CD1 LEU A 119 3141 9337 10440 -1308 1024 730 C ATOM 788 CD2 LEU A 119 87.028 190.072 302.080 1.00 59.34 C ANISOU 788 CD2 LEU A 119 3034 9150 10363 -1167 928 710 C ATOM 789 N ALA A 120 85.299 184.979 301.516 1.00 66.72 N ANISOU 789 N ALA A 120 3798 9921 11630 -1229 648 856 N ATOM 790 CA ALA A 120 83.976 184.526 301.116 1.00 62.88 C ANISOU 790 CA ALA A 120 3208 9413 11271 -1234 602 866 C ATOM 791 C ALA A 120 83.344 183.594 302.138 1.00 64.06 C ANISOU 791 C ALA A 120 3302 9544 11494 -1301 641 914 C ATOM 792 O ALA A 120 82.147 183.306 302.041 1.00 72.97 O ANISOU 792 O ALA A 120 4332 10663 12729 -1317 626 920 O ATOM 793 CB ALA A 120 84.036 183.825 299.759 1.00 62.79 C ANISOU 793 CB ALA A 120 3181 9374 11301 -1212 486 839 C ATOM 794 N VAL A 121 84.111 183.108 303.107 1.00 63.81 N ANISOU 794 N VAL A 121 3321 9511 11411 -1342 690 951 N ATOM 795 CA VAL A 121 83.546 182.332 304.200 1.00 65.01 C ANISOU 795 CA VAL A 121 3420 9656 11623 -1411 743 1007 C ATOM 796 C VAL A 121 83.660 183.048 305.532 1.00 65.18 C ANISOU 796 C VAL A 121 3456 9750 11558 -1454 861 1012 C ATOM 797 O VAL A 121 82.860 182.766 306.435 1.00 66.42 O ANISOU 797 O VAL A 121 3549 9925 11763 -1513 924 1042 O ATOM 798 CB VAL A 121 84.183 180.929 304.290 1.00 65.07 C ANISOU 798 CB VAL A 121 3448 9604 11671 -1437 704 1065 C ATOM 799 CG1 VAL A 121 84.748 180.505 302.941 1.00 64.31 C ANISOU 799 CG1 VAL A 121 3383 9457 11593 -1390 603 1032 C ATOM 800 CG2 VAL A 121 85.244 180.860 305.361 1.00 64.64 C ANISOU 800 CG2 VAL A 121 3456 9584 11522 -1463 765 1114 C ATOM 801 N ALA A 122 84.600 183.976 305.685 1.00 64.11 N ANISOU 801 N ALA A 122 3396 9667 11296 -1438 898 974 N ATOM 802 CA ALA A 122 84.670 184.729 306.931 1.00 66.96 C ANISOU 802 CA ALA A 122 3761 10114 11568 -1497 1019 954 C ATOM 803 C ALA A 122 83.456 185.634 307.080 1.00 65.37 C ANISOU 803 C ALA A 122 3487 9940 11410 -1500 1084 919 C ATOM 804 O ALA A 122 82.830 185.681 308.143 1.00 84.00 O ANISOU 804 O ALA A 122 5794 12349 13773 -1570 1177 924 O ATOM 805 CB ALA A 122 85.966 185.542 306.996 1.00 65.38 C ANISOU 805 CB ALA A 122 3649 9966 11225 -1490 1048 903 C ATOM 806 N SER A 123 83.097 186.347 306.019 1.00 65.01 N ANISOU 806 N SER A 123 3430 9865 11404 -1425 1039 889 N ATOM 807 CA SER A 123 81.861 187.116 306.021 1.00 73.30 C ANISOU 807 CA SER A 123 4394 10925 12532 -1409 1087 876 C ATOM 808 C SER A 123 81.396 187.318 304.585 1.00 73.81 C ANISOU 808 C SER A 123 4426 10935 12685 -1318 986 874 C ATOM 809 O SER A 123 81.947 188.175 303.886 1.00 73.36 O ANISOU 809 O SER A 123 4419 10877 12577 -1259 970 847 O ATOM 810 CB SER A 123 82.055 188.466 306.714 1.00 66.06 C ANISOU 810 CB SER A 123 3497 10077 11524 -1428 1212 828 C ATOM 811 OG SER A 123 82.773 189.360 305.878 1.00 69.38 O ANISOU 811 OG SER A 123 3983 10488 11891 -1361 1187 795 O ATOM 812 N PRO A 124 80.400 186.569 304.101 1.00 66.90 N ANISOU 812 N PRO A 124 3461 10022 11936 -1313 917 899 N ATOM 813 CA PRO A 124 80.041 186.670 302.680 1.00 66.85 C ANISOU 813 CA PRO A 124 3416 9989 11996 -1241 808 889 C ATOM 814 C PRO A 124 79.267 187.917 302.322 1.00 75.42 C ANISOU 814 C PRO A 124 4433 11088 13134 -1177 839 883 C ATOM 815 O PRO A 124 78.939 188.100 301.141 1.00 75.67 O ANISOU 815 O PRO A 124 4421 11115 13216 -1115 749 879 O ATOM 816 CB PRO A 124 79.183 185.415 302.440 1.00 68.04 C ANISOU 816 CB PRO A 124 3476 10114 12261 -1279 738 908 C ATOM 817 CG PRO A 124 79.511 184.514 303.577 1.00 68.19 C ANISOU 817 CG PRO A 124 3526 10124 12258 -1359 793 938 C ATOM 818 CD PRO A 124 79.736 185.426 304.738 1.00 68.08 C ANISOU 818 CD PRO A 124 3546 10160 12163 -1382 923 934 C ATOM 819 N PHE A 125 78.932 188.757 303.291 1.00 68.04 N ANISOU 819 N PHE A 125 3480 10176 12196 -1192 966 882 N ATOM 820 CA PHE A 125 78.247 190.001 302.985 1.00 83.37 C ANISOU 820 CA PHE A 125 5355 12115 14205 -1122 1011 885 C ATOM 821 C PHE A 125 79.203 191.139 302.682 1.00 77.84 C ANISOU 821 C PHE A 125 4748 11414 13413 -1072 1049 864 C ATOM 822 O PHE A 125 78.811 192.087 301.994 1.00 76.99 O ANISOU 822 O PHE A 125 4597 11287 13370 -991 1050 877 O ATOM 823 CB PHE A 125 77.331 190.395 304.145 1.00 87.82 C ANISOU 823 CB PHE A 125 5839 12698 14829 -1163 1144 889 C ATOM 824 CG PHE A 125 76.225 189.421 304.393 1.00 71.70 C ANISOU 824 CG PHE A 125 3686 10658 12899 -1207 1117 911 C ATOM 825 CD1 PHE A 125 75.453 188.950 303.348 1.00 72.45 C ANISOU 825 CD1 PHE A 125 3685 10738 13104 -1166 998 927 C ATOM 826 CD2 PHE A 125 75.972 188.964 305.670 1.00 77.94 C ANISOU 826 CD2 PHE A 125 4460 11478 13675 -1301 1212 912 C ATOM 827 CE1 PHE A 125 74.441 188.048 303.576 1.00 73.93 C ANISOU 827 CE1 PHE A 125 3763 10933 13395 -1217 978 940 C ATOM 828 CE2 PHE A 125 74.962 188.063 305.903 1.00 79.38 C ANISOU 828 CE2 PHE A 125 4537 11660 13964 -1347 1195 932 C ATOM 829 CZ PHE A 125 74.195 187.602 304.857 1.00 74.63 C ANISOU 829 CZ PHE A 125 3841 11035 13480 -1306 1079 945 C ATOM 830 N LEU A 126 80.441 191.065 303.171 1.00 74.40 N ANISOU 830 N LEU A 126 4432 11002 12836 -1120 1082 835 N ATOM 831 CA LEU A 126 81.436 192.076 302.837 1.00 72.57 C ANISOU 831 CA LEU A 126 4290 10774 12510 -1084 1115 807 C ATOM 832 C LEU A 126 82.004 191.857 301.441 1.00 70.81 C ANISOU 832 C LEU A 126 4107 10524 12272 -1021 986 810 C ATOM 833 O LEU A 126 82.394 192.825 300.775 1.00 63.45 O ANISOU 833 O LEU A 126 3207 9581 11320 -961 995 804 O ATOM 834 CB LEU A 126 82.554 192.071 303.883 1.00 73.00 C ANISOU 834 CB LEU A 126 4442 10885 12411 -1168 1195 766 C ATOM 835 CG LEU A 126 83.587 193.195 303.838 1.00 73.13 C ANISOU 835 CG LEU A 126 4545 10925 12317 -1160 1262 724 C ATOM 836 CD1 LEU A 126 82.940 194.521 303.442 1.00 74.71 C ANISOU 836 CD1 LEU A 126 4697 11085 12605 -1086 1329 736 C ATOM 837 CD2 LEU A 126 84.278 193.321 305.191 1.00 63.25 C ANISOU 837 CD2 LEU A 126 3341 9764 10926 -1270 1372 676 C ATOM 838 N SER A 127 82.032 190.602 300.984 1.00 63.82 N ANISOU 838 N SER A 127 3217 9631 11402 -1038 873 818 N ATOM 839 CA SER A 127 82.558 190.289 299.661 1.00 68.01 C ANISOU 839 CA SER A 127 3779 10151 11911 -994 752 810 C ATOM 840 C SER A 127 81.796 191.031 298.572 1.00 70.48 C ANISOU 840 C SER A 127 4010 10463 12306 -911 703 828 C ATOM 841 O SER A 127 82.400 191.590 297.652 1.00 67.84 O ANISOU 841 O SER A 127 3717 10133 11925 -860 667 818 O ATOM 842 CB SER A 127 82.508 188.779 299.434 1.00 63.14 C ANISOU 842 CB SER A 127 3146 9523 11320 -1037 655 812 C ATOM 843 OG SER A 127 83.472 188.134 300.246 1.00 62.35 O ANISOU 843 OG SER A 127 3132 9421 11137 -1095 689 806 O ATOM 844 N GLN A 128 80.467 191.066 298.668 1.00 74.18 N ANISOU 844 N GLN A 128 4353 10932 12900 -897 704 857 N ATOM 845 CA GLN A 128 79.683 191.791 297.672 1.00 80.00 C ANISOU 845 CA GLN A 128 4991 11681 13725 -813 655 886 C ATOM 846 C GLN A 128 80.073 193.262 297.635 1.00 82.49 C ANISOU 846 C GLN A 128 5347 11974 14022 -748 747 901 C ATOM 847 O GLN A 128 80.078 193.887 296.566 1.00 79.74 O ANISOU 847 O GLN A 128 4973 11634 13691 -672 695 924 O ATOM 848 CB GLN A 128 78.185 191.651 297.963 1.00 83.27 C ANISOU 848 CB GLN A 128 5253 12104 14283 -810 659 916 C ATOM 849 CG GLN A 128 77.486 190.541 297.190 1.00 85.18 C ANISOU 849 CG GLN A 128 5396 12388 14581 -832 519 908 C ATOM 850 CD GLN A 128 77.125 189.356 298.064 1.00 86.70 C ANISOU 850 CD GLN A 128 5570 12571 14802 -926 534 895 C ATOM 851 OE1 GLN A 128 77.415 189.343 299.261 1.00 87.29 O ANISOU 851 OE1 GLN A 128 5705 12615 14845 -973 643 897 O ATOM 852 NE2 GLN A 128 76.483 188.355 297.471 1.00 88.05 N ANISOU 852 NE2 GLN A 128 5649 12777 15029 -959 426 879 N ATOM 853 N LYS A 129 80.405 193.832 298.794 1.00 93.53 N ANISOU 853 N LYS A 129 6803 13351 15384 -782 890 888 N ATOM 854 CA LYS A 129 80.816 195.225 298.886 1.00103.95 C ANISOU 854 CA LYS A 129 8164 14643 16688 -736 1001 892 C ATOM 855 C LYS A 129 82.321 195.414 298.731 1.00114.87 C ANISOU 855 C LYS A 129 9690 16036 17919 -760 1011 849 C ATOM 856 O LYS A 129 82.790 196.558 298.769 1.00120.70 O ANISOU 856 O LYS A 129 10473 16753 18634 -732 1107 845 O ATOM 857 CB LYS A 129 80.355 195.835 300.217 1.00 66.19 C ANISOU 857 CB LYS A 129 3358 9846 11945 -772 1164 885 C ATOM 858 CG LYS A 129 78.989 196.510 300.150 1.00 68.08 C ANISOU 858 CG LYS A 129 3457 10049 12361 -700 1210 937 C ATOM 859 CD LYS A 129 78.784 197.495 301.299 1.00 82.99 C ANISOU 859 CD LYS A 129 5343 11909 14282 -720 1402 920 C ATOM 860 CE LYS A 129 78.786 196.790 302.650 1.00 81.38 C ANISOU 860 CE LYS A 129 5158 11755 14009 -838 1466 874 C ATOM 861 NZ LYS A 129 78.597 197.712 303.810 1.00 80.68 N ANISOU 861 NZ LYS A 129 5063 11659 13932 -876 1657 845 N ATOM 862 N VAL A 130 83.086 194.335 298.550 1.00115.68 N ANISOU 862 N VAL A 130 9860 16166 17928 -809 922 818 N ATOM 863 CA VAL A 130 84.532 194.459 298.401 1.00 60.85 C ANISOU 863 CA VAL A 130 3040 9236 10843 -832 929 775 C ATOM 864 C VAL A 130 84.990 193.818 297.096 1.00 60.11 C ANISOU 864 C VAL A 130 2966 9152 10722 -802 790 769 C ATOM 865 O VAL A 130 85.914 194.322 296.450 1.00 59.34 O ANISOU 865 O VAL A 130 2937 9060 10551 -779 787 749 O ATOM 866 CB VAL A 130 85.258 193.866 299.627 1.00 60.28 C ANISOU 866 CB VAL A 130 3039 9197 10668 -929 985 734 C ATOM 867 CG1 VAL A 130 86.142 192.693 299.261 1.00 59.25 C ANISOU 867 CG1 VAL A 130 2971 9078 10465 -959 885 714 C ATOM 868 CG2 VAL A 130 86.057 194.949 300.324 1.00 59.84 C ANISOU 868 CG2 VAL A 130 3054 9168 10516 -961 1117 695 C ATOM 869 N ARG A 131 84.341 192.730 296.676 1.00 60.70 N ANISOU 869 N ARG A 131 2973 9234 10855 -809 680 780 N ATOM 870 CA ARG A 131 84.703 192.053 295.426 1.00 60.25 C ANISOU 870 CA ARG A 131 2922 9201 10771 -794 550 760 C ATOM 871 C ARG A 131 83.962 192.711 294.259 1.00 70.93 C ANISOU 871 C ARG A 131 4181 10577 12192 -715 486 790 C ATOM 872 O ARG A 131 82.982 192.195 293.718 1.00 71.67 O ANISOU 872 O ARG A 131 4164 10701 12365 -704 394 803 O ATOM 873 CB ARG A 131 84.417 190.559 295.531 1.00 60.62 C ANISOU 873 CB ARG A 131 2938 9251 10844 -852 471 747 C ATOM 874 CG ARG A 131 84.685 189.766 294.273 1.00 60.45 C ANISOU 874 CG ARG A 131 2905 9261 10802 -851 343 711 C ATOM 875 CD ARG A 131 84.606 188.275 294.516 1.00 60.74 C ANISOU 875 CD ARG A 131 2930 9286 10864 -919 292 694 C ATOM 876 NE ARG A 131 84.349 187.581 293.261 1.00 65.24 N ANISOU 876 NE ARG A 131 3437 9903 11450 -924 169 655 N ATOM 877 CZ ARG A 131 84.850 186.394 292.937 1.00 65.29 C ANISOU 877 CZ ARG A 131 3464 9906 11438 -975 114 614 C ATOM 878 NH1 ARG A 131 85.653 185.754 293.777 1.00 60.33 N ANISOU 878 NH1 ARG A 131 2919 9220 10784 -1013 167 623 N ATOM 879 NH2 ARG A 131 84.556 185.856 291.761 1.00 61.77 N ANISOU 879 NH2 ARG A 131 2948 9522 11001 -990 7 563 N ATOM 880 N THR A 132 84.457 193.892 293.890 1.00 70.62 N ANISOU 880 N THR A 132 4181 10530 12123 -661 539 803 N ATOM 881 CA THR A 132 83.955 194.670 292.764 1.00 61.40 C ANISOU 881 CA THR A 132 2934 9386 11011 -575 489 846 C ATOM 882 C THR A 132 84.925 194.522 291.600 1.00 60.42 C ANISOU 882 C THR A 132 2865 9304 10789 -567 408 808 C ATOM 883 O THR A 132 86.141 194.623 291.791 1.00 64.11 O ANISOU 883 O THR A 132 3450 9755 11153 -599 461 767 O ATOM 884 CB THR A 132 83.817 196.153 293.138 1.00 61.74 C ANISOU 884 CB THR A 132 2976 9380 11104 -515 621 898 C ATOM 885 OG1 THR A 132 83.243 196.270 294.444 1.00 84.06 O ANISOU 885 OG1 THR A 132 5783 12165 13990 -547 728 906 O ATOM 886 CG2 THR A 132 82.936 196.893 292.141 1.00 72.47 C ANISOU 886 CG2 THR A 132 4213 10756 12566 -412 569 974 C ATOM 887 N LYS A 133 84.388 194.285 290.399 1.00 61.29 N ANISOU 887 N LYS A 133 2880 9480 10927 -529 279 814 N ATOM 888 CA LYS A 133 85.228 194.225 289.206 1.00 71.56 C ANISOU 888 CA LYS A 133 4216 10835 12139 -520 203 773 C ATOM 889 C LYS A 133 86.076 195.483 289.069 1.00 70.48 C ANISOU 889 C LYS A 133 4157 10664 11958 -474 300 801 C ATOM 890 O LYS A 133 87.222 195.423 288.605 1.00 68.73 O ANISOU 890 O LYS A 133 4022 10457 11634 -497 299 748 O ATOM 891 CB LYS A 133 84.374 194.013 287.960 1.00 62.04 C ANISOU 891 CB LYS A 133 2873 9724 10974 -478 54 782 C ATOM 892 N THR A 134 85.535 196.634 289.486 1.00 73.25 N ANISOU 892 N THR A 134 4474 10967 12392 -411 396 879 N ATOM 893 CA THR A 134 86.319 197.863 289.453 1.00 75.40 C ANISOU 893 CA THR A 134 4820 11195 12634 -375 512 905 C ATOM 894 C THR A 134 87.397 197.861 290.530 1.00 76.51 C ANISOU 894 C THR A 134 5097 11289 12683 -455 633 841 C ATOM 895 O THR A 134 88.470 198.439 290.327 1.00 79.75 O ANISOU 895 O THR A 134 5597 11692 13014 -463 698 816 O ATOM 896 CB THR A 134 85.405 199.094 289.588 1.00 61.13 C ANISOU 896 CB THR A 134 2929 9339 10959 -282 594 1009 C ATOM 897 OG1 THR A 134 86.019 200.225 288.954 1.00 66.22 O ANISOU 897 OG1 THR A 134 3585 9931 11643 -217 663 1106 O ATOM 898 CG2 THR A 134 85.134 199.443 291.050 1.00 61.28 C ANISOU 898 CG2 THR A 134 2975 9280 11029 -315 742 1008 C ATOM 899 N ALA A 135 87.154 197.196 291.659 1.00 73.87 N ANISOU 899 N ALA A 135 4777 10936 12356 -517 661 813 N ATOM 900 CA ALA A 135 88.158 197.069 292.705 1.00 69.83 C ANISOU 900 CA ALA A 135 4380 10407 11746 -596 754 753 C ATOM 901 C ALA A 135 88.962 195.783 292.579 1.00 56.18 C ANISOU 901 C ALA A 135 2709 8715 9923 -660 668 687 C ATOM 902 O ALA A 135 89.795 195.500 293.445 1.00 64.19 O ANISOU 902 O ALA A 135 3804 9728 10856 -724 725 642 O ATOM 903 CB ALA A 135 87.503 197.148 294.090 1.00 68.76 C ANISOU 903 CB ALA A 135 4223 10239 11663 -629 847 763 C ATOM 904 N ALA A 136 88.715 194.995 291.535 1.00 56.41 N ANISOU 904 N ALA A 136 2687 8781 9964 -644 535 679 N ATOM 905 CA ALA A 136 89.557 193.861 291.180 1.00 70.65 C ANISOU 905 CA ALA A 136 4541 10615 11688 -695 461 613 C ATOM 906 C ALA A 136 90.522 194.213 290.058 1.00 69.50 C ANISOU 906 C ALA A 136 4438 10504 11464 -677 437 576 C ATOM 907 O ALA A 136 91.708 193.874 290.125 1.00 67.98 O ANISOU 907 O ALA A 136 4332 10318 11181 -720 458 519 O ATOM 908 CB ALA A 136 88.693 192.662 290.773 1.00 56.46 C ANISOU 908 CB ALA A 136 2657 8845 9951 -709 338 607 C ATOM 909 N ARG A 137 90.028 194.891 289.019 1.00 55.48 N ANISOU 909 N ARG A 137 2594 8757 9727 -613 395 610 N ATOM 910 CA ARG A 137 90.911 195.406 287.981 1.00 54.87 C ANISOU 910 CA ARG A 137 2553 8714 9582 -593 390 583 C ATOM 911 C ARG A 137 91.925 196.378 288.569 1.00 77.97 C ANISOU 911 C ARG A 137 5582 11598 12445 -607 534 578 C ATOM 912 O ARG A 137 93.126 196.290 288.287 1.00 77.50 O ANISOU 912 O ARG A 137 5600 11558 12290 -643 554 516 O ATOM 913 CB ARG A 137 90.087 196.074 286.880 1.00 56.03 C ANISOU 913 CB ARG A 137 2594 8900 9793 -512 324 645 C ATOM 914 CG ARG A 137 89.907 195.190 285.659 1.00 56.83 C ANISOU 914 CG ARG A 137 2609 9075 9908 -517 167 628 C ATOM 915 CD ARG A 137 88.484 195.211 285.124 1.00 79.63 C ANISOU 915 CD ARG A 137 5337 12001 12918 -460 56 721 C ATOM 916 NE ARG A 137 88.444 195.641 283.729 1.00 80.60 N ANISOU 916 NE ARG A 137 5357 12178 13088 -405 -43 826 N ATOM 917 CZ ARG A 137 88.796 194.881 282.695 1.00 80.06 C ANISOU 917 CZ ARG A 137 5251 12192 12976 -446 -164 770 C ATOM 918 NH1 ARG A 137 89.219 193.639 282.891 1.00 78.31 N ANISOU 918 NH1 ARG A 137 5086 11991 12677 -536 -188 607 N ATOM 919 NH2 ARG A 137 88.727 195.366 281.461 1.00 82.02 N ANISOU 919 NH2 ARG A 137 5399 12508 13255 -398 -260 890 N ATOM 920 N TRP A 138 91.465 197.297 289.416 1.00 54.32 N ANISOU 920 N TRP A 138 2585 8552 9504 -586 640 634 N ATOM 921 CA TRP A 138 92.382 198.250 290.025 1.00 72.81 C ANISOU 921 CA TRP A 138 5018 10864 11783 -613 784 617 C ATOM 922 C TRP A 138 93.312 197.601 291.047 1.00 68.66 C ANISOU 922 C TRP A 138 4578 10348 11160 -701 821 543 C ATOM 923 O TRP A 138 94.159 198.296 291.622 1.00 68.26 O ANISOU 923 O TRP A 138 4600 10297 11037 -742 932 512 O ATOM 924 CB TRP A 138 91.592 199.397 290.658 1.00 78.11 C ANISOU 924 CB TRP A 138 5654 11478 12546 -571 897 687 C ATOM 925 CG TRP A 138 92.063 200.745 290.196 1.00 81.00 C ANISOU 925 CG TRP A 138 6050 11817 12908 -534 1004 717 C ATOM 926 CD1 TRP A 138 92.147 201.190 288.904 1.00 85.75 C ANISOU 926 CD1 TRP A 138 6606 12410 13565 -465 971 796 C ATOM 927 CD2 TRP A 138 92.519 201.822 291.022 1.00 81.67 C ANISOU 927 CD2 TRP A 138 6199 11856 12974 -563 1173 708 C ATOM 928 NE1 TRP A 138 92.632 202.477 288.877 1.00 86.91 N ANISOU 928 NE1 TRP A 138 6784 12488 13750 -441 1122 856 N ATOM 929 CE2 TRP A 138 92.868 202.888 290.164 1.00 83.30 C ANISOU 929 CE2 TRP A 138 6410 12023 13219 -509 1244 769 C ATOM 930 CE3 TRP A 138 92.668 201.989 292.403 1.00 77.98 C ANISOU 930 CE3 TRP A 138 5776 11377 12476 -632 1277 666 C ATOM 931 CZ2 TRP A 138 93.357 204.102 290.644 1.00 82.18 C ANISOU 931 CZ2 TRP A 138 6327 11821 13076 -525 1421 773 C ATOM 932 CZ3 TRP A 138 93.152 203.194 292.877 1.00 77.38 C ANISOU 932 CZ3 TRP A 138 5756 11265 12380 -655 1440 657 C ATOM 933 CH2 TRP A 138 93.491 204.235 292.001 1.00 78.74 C ANISOU 933 CH2 TRP A 138 5947 11395 12576 -604 1510 697 C ATOM 934 N LEU A 139 93.182 196.295 291.279 1.00 65.14 N ANISOU 934 N LEU A 139 4120 9918 10713 -733 731 518 N ATOM 935 CA LEU A 139 94.157 195.545 292.058 1.00 61.83 C ANISOU 935 CA LEU A 139 3771 9514 10207 -805 747 460 C ATOM 936 C LEU A 139 95.184 194.859 291.164 1.00 60.44 C ANISOU 936 C LEU A 139 3631 9371 9961 -819 681 402 C ATOM 937 O LEU A 139 96.373 194.824 291.505 1.00 59.01 O ANISOU 937 O LEU A 139 3521 9211 9690 -864 728 351 O ATOM 938 CB LEU A 139 93.444 194.509 292.937 1.00 52.32 C ANISOU 938 CB LEU A 139 2530 8295 9055 -830 707 479 C ATOM 939 CG LEU A 139 94.274 193.376 293.550 1.00 51.78 C ANISOU 939 CG LEU A 139 2506 8239 8929 -888 686 441 C ATOM 940 CD1 LEU A 139 93.860 193.143 294.989 1.00 52.24 C ANISOU 940 CD1 LEU A 139 2554 8289 9005 -930 739 462 C ATOM 941 CD2 LEU A 139 94.125 192.092 292.749 1.00 51.89 C ANISOU 941 CD2 LEU A 139 2486 8250 8979 -880 565 435 C ATOM 942 N LEU A 140 94.737 194.306 290.030 1.00 60.48 N ANISOU 942 N LEU A 140 3580 9393 10006 -786 574 402 N ATOM 943 CA LEU A 140 95.637 193.604 289.120 1.00 50.84 C ANISOU 943 CA LEU A 140 2380 8211 8724 -805 514 337 C ATOM 944 C LEU A 140 96.813 194.484 288.737 1.00 93.84 C ANISOU 944 C LEU A 140 7893 13677 14084 -814 591 297 C ATOM 945 O LEU A 140 97.970 194.053 288.787 1.00 94.01 O ANISOU 945 O LEU A 140 7970 13720 14031 -854 607 238 O ATOM 946 CB LEU A 140 94.878 193.166 287.871 1.00 51.55 C ANISOU 946 CB LEU A 140 2384 8339 8864 -774 398 332 C ATOM 947 CG LEU A 140 94.055 191.875 287.865 1.00 78.19 C ANISOU 947 CG LEU A 140 5691 11721 12298 -792 297 330 C ATOM 948 CD1 LEU A 140 93.691 191.397 289.256 1.00 52.42 C ANISOU 948 CD1 LEU A 140 2441 8401 9075 -817 334 372 C ATOM 949 CD2 LEU A 140 92.792 192.098 287.042 1.00 80.12 C ANISOU 949 CD2 LEU A 140 5825 12003 12614 -748 212 359 C ATOM 950 N VAL A 141 96.530 195.735 288.368 1.00 50.31 N ANISOU 950 N VAL A 141 2370 8157 8587 -775 646 334 N ATOM 951 CA VAL A 141 97.593 196.698 288.089 1.00 62.06 C ANISOU 951 CA VAL A 141 3923 9659 9999 -790 742 304 C ATOM 952 C VAL A 141 98.546 196.795 289.275 1.00 60.32 C ANISOU 952 C VAL A 141 3781 9440 9697 -855 834 266 C ATOM 953 O VAL A 141 99.774 196.790 289.117 1.00 48.48 O ANISOU 953 O VAL A 141 2337 7977 8106 -898 868 203 O ATOM 954 CB VAL A 141 96.990 198.067 287.733 1.00 50.31 C ANISOU 954 CB VAL A 141 2407 8145 8563 -735 807 376 C ATOM 955 CG1 VAL A 141 98.056 199.148 287.807 1.00 53.51 C ANISOU 955 CG1 VAL A 141 2891 8552 8888 -768 941 354 C ATOM 956 CG2 VAL A 141 96.371 198.015 286.348 1.00 51.21 C ANISOU 956 CG2 VAL A 141 2423 8268 8766 -670 711 442 C ATOM 957 N GLY A 142 97.990 196.871 290.484 1.00 59.84 N ANISOU 957 N GLY A 142 3716 9356 9666 -869 872 298 N ATOM 958 CA GLY A 142 98.829 196.856 291.669 1.00 49.11 C ANISOU 958 CA GLY A 142 2412 8024 8224 -939 944 256 C ATOM 959 C GLY A 142 99.712 195.626 291.727 1.00 48.72 C ANISOU 959 C GLY A 142 2382 8000 8128 -972 882 202 C ATOM 960 O GLY A 142 100.924 195.728 291.918 1.00 48.11 O ANISOU 960 O GLY A 142 2363 7958 7959 -1016 926 147 O ATOM 961 N ILE A 143 99.118 194.446 291.541 1.00 48.81 N ANISOU 961 N ILE A 143 2350 7987 8209 -948 780 224 N ATOM 962 CA ILE A 143 99.909 193.218 291.543 1.00 48.50 C ANISOU 962 CA ILE A 143 2321 7959 8146 -970 725 188 C ATOM 963 C ILE A 143 100.950 193.263 290.432 1.00 85.45 C ANISOU 963 C ILE A 143 7027 12677 12765 -972 718 128 C ATOM 964 O ILE A 143 102.127 192.963 290.654 1.00 86.07 O ANISOU 964 O ILE A 143 7162 12765 12776 -998 738 89 O ATOM 965 CB ILE A 143 99.003 191.980 291.425 1.00 49.01 C ANISOU 965 CB ILE A 143 2330 7991 8301 -949 624 228 C ATOM 966 CG1 ILE A 143 98.277 191.726 292.745 1.00 49.51 C ANISOU 966 CG1 ILE A 143 2375 8024 8413 -965 644 279 C ATOM 967 CG2 ILE A 143 99.821 190.763 291.049 1.00 48.81 C ANISOU 967 CG2 ILE A 143 2307 7975 8262 -962 568 196 C ATOM 968 CD1 ILE A 143 97.566 190.395 292.806 1.00 50.07 C ANISOU 968 CD1 ILE A 143 2396 8061 8568 -960 560 318 C ATOM 969 N TRP A 144 100.537 193.666 289.225 1.00 84.57 N ANISOU 969 N TRP A 144 6889 12572 12671 -938 688 128 N ATOM 970 CA TRP A 144 101.474 193.772 288.108 1.00 47.67 C ANISOU 970 CA TRP A 144 2255 7925 7932 -938 685 73 C ATOM 971 C TRP A 144 102.551 194.810 288.384 1.00 47.20 C ANISOU 971 C TRP A 144 2287 7869 7777 -965 791 49 C ATOM 972 O TRP A 144 103.745 194.545 288.207 1.00 55.67 O ANISOU 972 O TRP A 144 3421 8958 8772 -987 802 2 O ATOM 973 CB TRP A 144 100.734 194.131 286.827 1.00 48.05 C ANISOU 973 CB TRP A 144 2242 7991 8025 -902 640 76 C ATOM 974 CG TRP A 144 100.020 193.000 286.218 1.00 48.58 C ANISOU 974 CG TRP A 144 2232 8077 8148 -891 522 68 C ATOM 975 CD1 TRP A 144 98.678 192.779 286.232 1.00 49.33 C ANISOU 975 CD1 TRP A 144 2255 8159 8331 -861 454 117 C ATOM 976 CD2 TRP A 144 100.599 191.919 285.486 1.00 56.18 C ANISOU 976 CD2 TRP A 144 3205 9067 9075 -910 458 13 C ATOM 977 NE1 TRP A 144 98.382 191.624 285.554 1.00 56.77 N ANISOU 977 NE1 TRP A 144 3138 9139 9292 -875 352 80 N ATOM 978 CE2 TRP A 144 99.547 191.078 285.085 1.00 56.44 C ANISOU 978 CE2 TRP A 144 3148 9123 9175 -906 356 17 C ATOM 979 CE3 TRP A 144 101.906 191.580 285.125 1.00 56.29 C ANISOU 979 CE3 TRP A 144 3290 9098 9001 -935 480 -37 C ATOM 980 CZ2 TRP A 144 99.759 189.919 284.345 1.00 49.66 C ANISOU 980 CZ2 TRP A 144 2272 8303 8293 -934 282 -28 C ATOM 981 CZ3 TRP A 144 102.112 190.427 284.390 1.00 48.36 C ANISOU 981 CZ3 TRP A 144 2262 8135 7977 -954 407 -69 C ATOM 982 CH2 TRP A 144 101.044 189.614 284.009 1.00 49.15 C ANISOU 982 CH2 TRP A 144 2277 8257 8142 -958 312 -65 C ATOM 983 N GLY A 145 102.140 196.015 288.781 1.00 47.38 N ANISOU 983 N GLY A 145 2313 7885 7803 -965 872 84 N ATOM 984 CA GLY A 145 103.112 197.040 289.119 1.00 47.12 C ANISOU 984 CA GLY A 145 2367 7869 7668 -1003 976 65 C ATOM 985 C GLY A 145 104.040 196.604 290.236 1.00 47.65 C ANISOU 985 C GLY A 145 2493 7953 7660 -1051 993 30 C ATOM 986 O GLY A 145 105.260 196.763 290.146 1.00 46.61 O ANISOU 986 O GLY A 145 2429 7855 7427 -1082 1023 -10 O ATOM 987 N ALA A 146 103.474 196.037 291.301 1.00 47.18 N ANISOU 987 N ALA A 146 2397 7878 7651 -1060 974 47 N ATOM 988 CA ALA A 146 104.278 195.514 292.399 1.00 47.16 C ANISOU 988 CA ALA A 146 2429 7886 7603 -1103 987 8 C ATOM 989 C ALA A 146 104.954 194.200 292.048 1.00 52.26 C ANISOU 989 C ALA A 146 3062 8520 8273 -1088 913 -19 C ATOM 990 O ALA A 146 105.702 193.664 292.870 1.00 50.91 O ANISOU 990 O ALA A 146 2902 8344 8097 -1113 923 -52 O ATOM 991 CB ALA A 146 103.424 195.330 293.655 1.00 51.60 C ANISOU 991 CB ALA A 146 2950 8439 8218 -1121 999 37 C ATOM 992 N SER A 147 104.687 193.661 290.866 1.00 46.82 N ANISOU 992 N SER A 147 2340 7828 7622 -1049 844 -7 N ATOM 993 CA SER A 147 105.444 192.532 290.354 1.00 46.71 C ANISOU 993 CA SER A 147 2318 7822 7607 -1040 785 -30 C ATOM 994 C SER A 147 106.538 192.960 289.391 1.00 55.90 C ANISOU 994 C SER A 147 3540 9023 8676 -1047 811 -77 C ATOM 995 O SER A 147 107.609 192.348 289.376 1.00 46.30 O ANISOU 995 O SER A 147 2339 7832 7422 -1056 803 -105 O ATOM 996 CB SER A 147 104.510 191.539 289.657 1.00 46.99 C ANISOU 996 CB SER A 147 2278 7849 7727 -1010 692 4 C ATOM 997 OG SER A 147 105.230 190.450 289.127 1.00 79.83 O ANISOU 997 OG SER A 147 6425 12027 11879 -1008 643 -12 O ATOM 998 N PHE A 148 106.298 194.012 288.603 1.00 56.13 N ANISOU 998 N PHE A 148 3593 9062 8670 -1042 845 -77 N ATOM 999 CA PHE A 148 107.326 194.545 287.717 1.00 45.96 C ANISOU 999 CA PHE A 148 2363 7825 7276 -1056 880 -104 C ATOM 1000 C PHE A 148 108.518 195.091 288.479 1.00 58.80 C ANISOU 1000 C PHE A 148 4055 9504 8783 -1099 943 -109 C ATOM 1001 O PHE A 148 109.618 195.168 287.921 1.00 45.74 O ANISOU 1001 O PHE A 148 2435 7949 6997 -1109 935 -48 O ATOM 1002 CB PHE A 148 106.750 195.651 286.837 1.00 62.03 C ANISOU 1002 CB PHE A 148 4400 9852 9315 -1044 919 -92 C ATOM 1003 CG PHE A 148 106.123 195.152 285.572 1.00 63.20 C ANISOU 1003 CG PHE A 148 4493 9993 9529 -1011 851 -110 C ATOM 1004 CD1 PHE A 148 106.434 193.899 285.082 1.00 46.21 C ANISOU 1004 CD1 PHE A 148 2317 7873 7368 -1009 772 -130 C ATOM 1005 CD2 PHE A 148 105.225 195.937 284.872 1.00 64.66 C ANISOU 1005 CD2 PHE A 148 4638 10152 9779 -986 866 -96 C ATOM 1006 CE1 PHE A 148 105.862 193.430 283.921 1.00 46.53 C ANISOU 1006 CE1 PHE A 148 2305 7927 7448 -994 705 -156 C ATOM 1007 CE2 PHE A 148 104.646 195.476 283.706 1.00 65.86 C ANISOU 1007 CE2 PHE A 148 4688 10300 10035 -961 799 -88 C ATOM 1008 CZ PHE A 148 104.966 194.220 283.229 1.00 47.20 C ANISOU 1008 CZ PHE A 148 2309 7970 7655 -972 717 -132 C ATOM 1009 N LEU A 149 108.323 195.481 289.734 1.00 65.01 N ANISOU 1009 N LEU A 149 4076 10897 9727 -846 -323 -15 N ATOM 1010 CA LEU A 149 109.400 196.071 290.511 1.00 65.73 C ANISOU 1010 CA LEU A 149 4160 11094 9721 -925 -317 -7 C ATOM 1011 C LEU A 149 110.229 195.032 291.244 1.00 53.17 C ANISOU 1011 C LEU A 149 2555 9558 8088 -909 -342 5 C ATOM 1012 O LEU A 149 111.438 195.223 291.412 1.00 60.37 O ANISOU 1012 O LEU A 149 3454 10569 8913 -949 -351 17 O ATOM 1013 CB LEU A 149 108.834 197.066 291.525 1.00 65.55 C ANISOU 1013 CB LEU A 149 4142 11076 9688 -1004 -282 -16 C ATOM 1014 CG LEU A 149 108.749 198.530 291.078 1.00 65.54 C ANISOU 1014 CG LEU A 149 4140 11083 9681 -1071 -247 -22 C ATOM 1015 CD1 LEU A 149 107.869 198.708 289.834 1.00 64.93 C ANISOU 1015 CD1 LEU A 149 4066 10923 9681 -1014 -237 -20 C ATOM 1016 CD2 LEU A 149 108.267 199.406 292.227 1.00 53.69 C ANISOU 1016 CD2 LEU A 149 2640 9591 8170 -1156 -209 -36 C ATOM 1017 N LEU A 150 109.602 193.941 291.685 1.00 52.92 N ANISOU 1017 N LEU A 150 2519 9475 8115 -852 -349 7 N ATOM 1018 CA LEU A 150 110.273 192.967 292.532 1.00 53.31 C ANISOU 1018 CA LEU A 150 2544 9589 8124 -839 -363 27 C ATOM 1019 C LEU A 150 111.182 192.045 291.727 1.00 53.60 C ANISOU 1019 C LEU A 150 2552 9676 8137 -786 -387 41 C ATOM 1020 O LEU A 150 112.041 191.385 292.317 1.00 54.07 O ANISOU 1020 O LEU A 150 2586 9812 8145 -782 -396 65 O ATOM 1021 CB LEU A 150 109.230 192.182 293.356 1.00 53.06 C ANISOU 1021 CB LEU A 150 2506 9484 8171 -800 -354 27 C ATOM 1022 CG LEU A 150 108.685 192.805 294.664 1.00 53.12 C ANISOU 1022 CG LEU A 150 2524 9499 8160 -857 -330 26 C ATOM 1023 CD1 LEU A 150 108.477 194.356 294.531 1.00 58.46 C ANISOU 1023 CD1 LEU A 150 3222 10196 8796 -939 -308 8 C ATOM 1024 CD2 LEU A 150 107.414 192.073 295.183 1.00 52.74 C ANISOU 1024 CD2 LEU A 150 2471 9351 8217 -806 -317 25 C ATOM 1025 N ALA A 151 111.088 192.078 290.393 1.00 53.41 N ANISOU 1025 N ALA A 151 2531 9623 8139 -750 -394 28 N ATOM 1026 CA ALA A 151 112.003 191.369 289.503 1.00 53.72 C ANISOU 1026 CA ALA A 151 2545 9716 8152 -706 -413 38 C ATOM 1027 C ALA A 151 113.098 192.265 288.938 1.00 54.05 C ANISOU 1027 C ALA A 151 2589 9848 8101 -752 -416 47 C ATOM 1028 O ALA A 151 113.885 191.811 288.101 1.00 54.33 O ANISOU 1028 O ALA A 151 2603 9933 8106 -718 -429 56 O ATOM 1029 CB ALA A 151 111.232 190.725 288.348 1.00 53.43 C ANISOU 1029 CB ALA A 151 2501 9601 8198 -632 -422 17 C ATOM 1030 N THR A 152 113.162 193.522 289.372 1.00 69.60 N ANISOU 1030 N THR A 152 4578 11834 10031 -830 -400 45 N ATOM 1031 CA THR A 152 114.165 194.440 288.838 1.00 54.45 C ANISOU 1031 CA THR A 152 2656 9991 8041 -878 -398 54 C ATOM 1032 C THR A 152 115.604 194.044 289.152 1.00 77.04 C ANISOU 1032 C THR A 152 5490 12969 10812 -894 -414 82 C ATOM 1033 O THR A 152 116.466 194.257 288.281 1.00 78.77 O ANISOU 1033 O THR A 152 5696 13246 10987 -893 -420 94 O ATOM 1034 CB THR A 152 113.889 195.864 289.332 1.00 54.44 C ANISOU 1034 CB THR A 152 2674 9971 8039 -964 -373 42 C ATOM 1035 OG1 THR A 152 113.413 195.819 290.679 1.00 54.43 O ANISOU 1035 OG1 THR A 152 2681 9958 8043 -998 -365 35 O ATOM 1036 CG2 THR A 152 112.858 196.538 288.450 1.00 53.97 C ANISOU 1036 CG2 THR A 152 2631 9823 8053 -947 -353 26 C ATOM 1037 N PRO A 153 115.950 193.506 290.330 1.00 75.54 N ANISOU 1037 N PRO A 153 5288 12827 10588 -910 -420 98 N ATOM 1038 CA PRO A 153 117.350 193.091 290.530 1.00 75.18 C ANISOU 1038 CA PRO A 153 5210 12901 10454 -919 -435 133 C ATOM 1039 C PRO A 153 117.837 192.096 289.491 1.00 74.31 C ANISOU 1039 C PRO A 153 5075 12804 10354 -840 -447 148 C ATOM 1040 O PRO A 153 119.038 192.058 289.197 1.00 56.69 O ANISOU 1040 O PRO A 153 2820 10668 8052 -849 -456 175 O ATOM 1041 CB PRO A 153 117.338 192.482 291.940 1.00 56.34 C ANISOU 1041 CB PRO A 153 2810 10549 8047 -928 -437 151 C ATOM 1042 CG PRO A 153 116.234 193.176 292.628 1.00 55.94 C ANISOU 1042 CG PRO A 153 2790 10426 8039 -967 -421 121 C ATOM 1043 CD PRO A 153 115.175 193.380 291.579 1.00 55.25 C ANISOU 1043 CD PRO A 153 2727 10219 8045 -927 -411 91 C ATOM 1044 N VAL A 154 116.936 191.308 288.899 1.00 73.21 N ANISOU 1044 N VAL A 154 4938 12573 10305 -765 -448 128 N ATOM 1045 CA VAL A 154 117.361 190.268 287.969 1.00 55.88 C ANISOU 1045 CA VAL A 154 2713 10388 8130 -690 -457 134 C ATOM 1046 C VAL A 154 117.921 190.867 286.683 1.00 85.59 C ANISOU 1046 C VAL A 154 6477 14191 11853 -690 -460 132 C ATOM 1047 O VAL A 154 118.744 190.236 286.010 1.00 86.37 O ANISOU 1047 O VAL A 154 6546 14342 11928 -649 -467 147 O ATOM 1048 CB VAL A 154 116.194 189.302 287.690 1.00 80.25 C ANISOU 1048 CB VAL A 154 5796 13362 11334 -617 -456 106 C ATOM 1049 CG1 VAL A 154 116.673 188.082 286.914 1.00 55.77 C ANISOU 1049 CG1 VAL A 154 2654 10270 8266 -542 -463 109 C ATOM 1050 CG2 VAL A 154 115.536 188.883 289.001 1.00 80.34 C ANISOU 1050 CG2 VAL A 154 5807 13329 11390 -622 -449 111 C ATOM 1051 N LEU A 155 117.507 192.078 286.311 1.00 55.70 N ANISOU 1051 N LEU A 155 2720 10382 8063 -733 -451 116 N ATOM 1052 CA LEU A 155 118.110 192.701 285.140 1.00 55.89 C ANISOU 1052 CA LEU A 155 2738 10454 8045 -735 -450 122 C ATOM 1053 C LEU A 155 119.367 193.490 285.475 1.00 56.46 C ANISOU 1053 C LEU A 155 2798 10627 8026 -807 -447 153 C ATOM 1054 O LEU A 155 120.068 193.935 284.560 1.00 72.63 O ANISOU 1054 O LEU A 155 4833 12729 10035 -809 -446 167 O ATOM 1055 CB LEU A 155 117.104 193.606 284.415 1.00 55.45 C ANISOU 1055 CB LEU A 155 2706 10328 8033 -739 -437 98 C ATOM 1056 CG LEU A 155 116.339 194.750 285.085 1.00 55.15 C ANISOU 1056 CG LEU A 155 2697 10233 8024 -805 -417 86 C ATOM 1057 CD1 LEU A 155 117.248 195.866 285.576 1.00 93.63 C ANISOU 1057 CD1 LEU A 155 7566 15171 12837 -895 -404 103 C ATOM 1058 CD2 LEU A 155 115.336 195.303 284.093 1.00 55.10 C ANISOU 1058 CD2 LEU A 155 2703 10161 8072 -779 -404 69 C ATOM 1059 N ALA A 156 119.661 193.694 286.753 1.00 82.69 N ANISOU 1059 N ALA A 156 6121 13981 11315 -867 -447 164 N ATOM 1060 CA ALA A 156 120.909 194.346 287.113 1.00 79.45 C ANISOU 1060 CA ALA A 156 5693 13675 10819 -938 -449 192 C ATOM 1061 C ALA A 156 122.040 193.346 287.308 1.00 79.63 C ANISOU 1061 C ALA A 156 5680 13795 10782 -909 -464 231 C ATOM 1062 O ALA A 156 123.211 193.696 287.112 1.00 72.58 O ANISOU 1062 O ALA A 156 4764 12996 9818 -942 -468 261 O ATOM 1063 CB ALA A 156 120.721 195.184 288.381 1.00 72.31 C ANISOU 1063 CB ALA A 156 4802 12772 9899 -1028 -441 179 C ATOM 1064 N PHE A 157 121.708 192.101 287.646 1.00 84.82 N ANISOU 1064 N PHE A 157 6327 14425 11474 -845 -471 235 N ATOM 1065 CA PHE A 157 122.686 191.112 288.068 1.00 58.38 C ANISOU 1065 CA PHE A 157 2938 11162 8080 -819 -480 279 C ATOM 1066 C PHE A 157 122.916 190.006 287.050 1.00 58.41 C ANISOU 1066 C PHE A 157 2916 11157 8122 -727 -481 285 C ATOM 1067 O PHE A 157 123.782 189.160 287.277 1.00 58.97 O ANISOU 1067 O PHE A 157 2948 11296 8163 -699 -484 326 O ATOM 1068 CB PHE A 157 122.263 190.487 289.405 1.00 64.81 C ANISOU 1068 CB PHE A 157 3748 11967 8909 -819 -480 289 C ATOM 1069 CG PHE A 157 122.345 191.429 290.578 1.00 58.64 C ANISOU 1069 CG PHE A 157 2980 11234 8067 -913 -480 290 C ATOM 1070 CD1 PHE A 157 121.593 192.589 290.612 1.00 70.01 C ANISOU 1070 CD1 PHE A 157 4458 12613 9530 -970 -471 247 C ATOM 1071 CD2 PHE A 157 123.162 191.145 291.652 1.00 59.34 C ANISOU 1071 CD2 PHE A 157 3039 11433 8076 -944 -487 333 C ATOM 1072 CE1 PHE A 157 121.664 193.449 291.684 1.00 70.66 C ANISOU 1072 CE1 PHE A 157 4548 12737 9564 -1059 -468 239 C ATOM 1073 CE2 PHE A 157 123.236 191.995 292.734 1.00 72.42 C ANISOU 1073 CE2 PHE A 157 4702 13143 9672 -1032 -489 326 C ATOM 1074 CZ PHE A 157 122.488 193.151 292.751 1.00 71.46 C ANISOU 1074 CZ PHE A 157 4618 12953 9579 -1092 -479 275 C ATOM 1075 N ARG A 158 122.171 189.976 285.945 1.00 57.94 N ANISOU 1075 N ARG A 158 2871 11017 8125 -680 -478 247 N ATOM 1076 CA ARG A 158 122.335 188.942 284.924 1.00 58.04 C ANISOU 1076 CA ARG A 158 2855 11019 8178 -595 -480 242 C ATOM 1077 C ARG A 158 122.824 189.599 283.641 1.00 87.15 C ANISOU 1077 C ARG A 158 6542 14750 11822 -594 -479 240 C ATOM 1078 O ARG A 158 122.090 190.369 283.011 1.00 86.44 O ANISOU 1078 O ARG A 158 6480 14611 11751 -603 -476 211 O ATOM 1079 CB ARG A 158 121.034 188.171 284.686 1.00 66.61 C ANISOU 1079 CB ARG A 158 3946 11983 9378 -533 -478 196 C ATOM 1080 CG ARG A 158 121.016 186.772 285.315 1.00 57.76 C ANISOU 1080 CG ARG A 158 2788 10835 8323 -481 -474 207 C ATOM 1081 CD ARG A 158 119.611 186.361 285.750 1.00 76.94 C ANISOU 1081 CD ARG A 158 5231 13141 10861 -458 -470 171 C ATOM 1082 NE ARG A 158 119.614 185.289 286.746 1.00 78.14 N ANISOU 1082 NE ARG A 158 5348 13276 11066 -430 -462 193 N ATOM 1083 CZ ARG A 158 119.551 185.487 288.061 1.00 79.45 C ANISOU 1083 CZ ARG A 158 5521 13463 11202 -472 -458 221 C ATOM 1084 NH1 ARG A 158 119.481 186.720 288.550 1.00 57.34 N ANISOU 1084 NH1 ARG A 158 2764 10698 8326 -548 -463 223 N ATOM 1085 NH2 ARG A 158 119.558 184.452 288.893 1.00 57.88 N ANISOU 1085 NH2 ARG A 158 2751 10722 8520 -437 -447 246 N ATOM 1086 N LYS A 159 124.062 189.293 283.259 1.00 88.25 N ANISOU 1086 N LYS A 159 6646 14984 11902 -580 -480 277 N ATOM 1087 CA LYS A 159 124.674 189.843 282.059 1.00 87.64 C ANISOU 1087 CA LYS A 159 6561 14963 11777 -574 -478 285 C ATOM 1088 C LYS A 159 125.504 188.749 281.397 1.00 89.49 C ANISOU 1088 C LYS A 159 6749 15249 12005 -504 -477 303 C ATOM 1089 O LYS A 159 125.931 187.793 282.048 1.00 89.09 O ANISOU 1089 O LYS A 159 6669 15215 11968 -481 -477 326 O ATOM 1090 CB LYS A 159 125.538 191.077 282.386 1.00 84.86 C ANISOU 1090 CB LYS A 159 6212 14692 11339 -661 -477 323 C ATOM 1091 CG LYS A 159 124.767 192.249 283.008 1.00 79.54 C ANISOU 1091 CG LYS A 159 5577 13966 10680 -735 -472 301 C ATOM 1092 CD LYS A 159 125.683 193.398 283.419 1.00 78.23 C ANISOU 1092 CD LYS A 159 5404 13877 10444 -827 -469 332 C ATOM 1093 CE LYS A 159 126.552 193.047 284.628 1.00 78.03 C ANISOU 1093 CE LYS A 159 5356 13931 10360 -868 -479 367 C ATOM 1094 NZ LYS A 159 127.814 192.334 284.271 1.00 81.29 N ANISOU 1094 NZ LYS A 159 5726 14445 10717 -833 -485 417 N ATOM 1095 N VAL A 160 125.712 188.884 280.083 1.00 90.15 N ANISOU 1095 N VAL A 160 6822 15358 12071 -467 -474 293 N ATOM 1096 CA VAL A 160 126.510 187.908 279.345 1.00 60.11 C ANISOU 1096 CA VAL A 160 2971 11606 8261 -400 -470 305 C ATOM 1097 C VAL A 160 127.986 188.183 279.579 1.00 60.77 C ANISOU 1097 C VAL A 160 3028 11809 8254 -435 -469 372 C ATOM 1098 O VAL A 160 128.437 189.336 279.575 1.00 60.88 O ANISOU 1098 O VAL A 160 3054 11876 8200 -498 -469 400 O ATOM 1099 CB VAL A 160 126.174 187.927 277.843 1.00 60.06 C ANISOU 1099 CB VAL A 160 2962 11597 8262 -344 -468 268 C ATOM 1100 CG1 VAL A 160 126.522 189.272 277.222 1.00 77.50 C ANISOU 1100 CG1 VAL A 160 5186 13868 10394 -388 -464 293 C ATOM 1101 CG2 VAL A 160 126.923 186.814 277.127 1.00 60.65 C ANISOU 1101 CG2 VAL A 160 2984 11717 8342 -271 -461 271 C ATOM 1102 N VAL A 161 128.747 187.117 279.797 1.00 61.29 N ANISOU 1102 N VAL A 161 3050 11914 8324 -394 -464 401 N ATOM 1103 CA VAL A 161 130.191 187.198 279.963 1.00 74.56 C ANISOU 1103 CA VAL A 161 4696 13713 9920 -416 -462 470 C ATOM 1104 C VAL A 161 130.830 186.293 278.922 1.00 75.05 C ANISOU 1104 C VAL A 161 4711 13813 9991 -335 -451 474 C ATOM 1105 O VAL A 161 130.418 185.139 278.755 1.00 75.20 O ANISOU 1105 O VAL A 161 4707 13772 10095 -266 -443 441 O ATOM 1106 CB VAL A 161 130.627 186.808 281.389 1.00 74.16 C ANISOU 1106 CB VAL A 161 4630 13695 9854 -449 -465 517 C ATOM 1107 CG1 VAL A 161 130.213 187.892 282.389 1.00 62.02 C ANISOU 1107 CG1 VAL A 161 3134 12148 8284 -541 -476 515 C ATOM 1108 CG2 VAL A 161 130.031 185.471 281.785 1.00 73.81 C ANISOU 1108 CG2 VAL A 161 4564 13572 9907 -384 -458 494 C ATOM 1109 N LYS A 162 131.815 186.825 278.207 1.00 75.84 N ANISOU 1109 N LYS A 162 4794 14009 10013 -344 -447 513 N ATOM 1110 CA LYS A 162 132.493 186.061 277.168 1.00 75.94 C ANISOU 1110 CA LYS A 162 4761 14069 10024 -269 -435 519 C ATOM 1111 C LYS A 162 133.441 185.065 277.824 1.00 75.34 C ANISOU 1111 C LYS A 162 4635 14042 9950 -245 -426 573 C ATOM 1112 O LYS A 162 134.422 185.458 278.463 1.00 64.60 O ANISOU 1112 O LYS A 162 3261 12771 8513 -296 -429 644 O ATOM 1113 CB LYS A 162 133.232 187.005 276.224 1.00 76.70 C ANISOU 1113 CB LYS A 162 4853 14255 10033 -286 -431 551 C ATOM 1114 CG LYS A 162 132.517 188.340 276.026 1.00 75.41 C ANISOU 1114 CG LYS A 162 4737 14063 9851 -343 -438 530 C ATOM 1115 CD LYS A 162 132.466 188.760 274.564 1.00 74.47 C ANISOU 1115 CD LYS A 162 4614 13976 9705 -303 -429 515 C ATOM 1116 CE LYS A 162 131.634 190.027 274.394 1.00 62.82 C ANISOU 1116 CE LYS A 162 3181 12461 8228 -353 -432 496 C ATOM 1117 NZ LYS A 162 131.471 190.404 272.963 1.00 62.93 N ANISOU 1117 NZ LYS A 162 3187 12509 8215 -307 -422 485 N ATOM 1118 N LEU A 163 133.141 183.775 277.682 1.00 75.09 N ANISOU 1118 N LEU A 163 4569 13950 10010 -169 -413 540 N ATOM 1119 CA LEU A 163 133.915 182.711 278.311 1.00 76.64 C ANISOU 1119 CA LEU A 163 4711 14178 10232 -136 -399 590 C ATOM 1120 C LEU A 163 135.045 182.223 277.408 1.00 79.19 C ANISOU 1120 C LEU A 163 4979 14583 10526 -81 -381 623 C ATOM 1121 O LEU A 163 136.204 182.172 277.830 1.00 79.61 O ANISOU 1121 O LEU A 163 5000 14734 10515 -96 -376 705 O ATOM 1122 CB LEU A 163 132.990 181.544 278.678 1.00 64.72 C ANISOU 1122 CB LEU A 163 3183 12548 8858 -82 -388 539 C ATOM 1123 CG LEU A 163 133.536 180.476 279.624 1.00 65.33 C ANISOU 1123 CG LEU A 163 3206 12636 8980 -54 -370 594 C ATOM 1124 CD1 LEU A 163 133.227 180.853 281.062 1.00 71.76 C ANISOU 1124 CD1 LEU A 163 4050 13448 9766 -118 -383 630 C ATOM 1125 CD2 LEU A 163 132.983 179.097 279.287 1.00 65.49 C ANISOU 1125 CD2 LEU A 163 3178 12550 9156 34 -344 537 C ATOM 1126 N THR A 164 134.710 181.863 276.167 1.00 80.91 N ANISOU 1126 N THR A 164 5185 14769 10789 -17 -371 560 N ATOM 1127 CA THR A 164 135.652 181.404 275.156 1.00 66.38 C ANISOU 1127 CA THR A 164 3293 13001 8927 43 -352 577 C ATOM 1128 C THR A 164 135.409 182.199 273.878 1.00 83.92 C ANISOU 1128 C THR A 164 5541 15252 11094 49 -358 537 C ATOM 1129 O THR A 164 134.331 182.768 273.681 1.00 83.60 O ANISOU 1129 O THR A 164 5548 15150 11067 27 -373 481 O ATOM 1130 CB THR A 164 135.494 179.889 274.895 1.00 66.79 C ANISOU 1130 CB THR A 164 3285 12984 9108 133 -325 532 C ATOM 1131 OG1 THR A 164 135.557 179.177 276.136 1.00 66.97 O ANISOU 1131 OG1 THR A 164 3283 12969 9192 130 -316 570 O ATOM 1132 CG2 THR A 164 136.580 179.356 273.972 1.00 67.65 C ANISOU 1132 CG2 THR A 164 3333 13174 9197 196 -299 555 C ATOM 1133 N ASN A 165 136.431 182.250 273.016 1.00 66.80 N ANISOU 1133 N ASN A 165 3338 13184 8860 78 -345 573 N ATOM 1134 CA ASN A 165 136.307 182.931 271.728 1.00 66.76 C ANISOU 1134 CA ASN A 165 3346 13224 8795 95 -346 544 C ATOM 1135 C ASN A 165 135.031 182.533 271.000 1.00 66.36 C ANISOU 1135 C ASN A 165 3308 13086 8819 143 -348 439 C ATOM 1136 O ASN A 165 134.357 183.378 270.402 1.00 74.80 O ANISOU 1136 O ASN A 165 4417 14156 9849 127 -360 408 O ATOM 1137 CB ASN A 165 137.522 182.623 270.851 1.00 82.42 C ANISOU 1137 CB ASN A 165 5275 15315 10725 146 -325 586 C ATOM 1138 CG ASN A 165 138.497 183.785 270.761 1.00 82.84 C ANISOU 1138 CG ASN A 165 5336 15483 10656 90 -330 675 C ATOM 1139 OD1 ASN A 165 138.753 184.486 271.741 1.00 84.52 O ANISOU 1139 OD1 ASN A 165 5573 15708 10832 10 -344 731 O ATOM 1140 ND2 ASN A 165 139.044 183.993 269.572 1.00 81.20 N ANISOU 1140 ND2 ASN A 165 5104 15360 10388 131 -317 686 N ATOM 1141 N GLU A 166 134.678 181.251 271.047 1.00 66.54 N ANISOU 1141 N GLU A 166 3293 13035 8956 204 -335 386 N ATOM 1142 CA GLU A 166 133.504 180.745 270.352 1.00 80.93 C ANISOU 1142 CA GLU A 166 5116 14775 10858 252 -335 285 C ATOM 1143 C GLU A 166 132.354 180.415 271.293 1.00 81.06 C ANISOU 1143 C GLU A 166 5158 14659 10982 229 -346 244 C ATOM 1144 O GLU A 166 131.358 179.830 270.856 1.00 83.07 O ANISOU 1144 O GLU A 166 5405 14833 11323 268 -345 163 O ATOM 1145 CB GLU A 166 133.876 179.513 269.525 1.00 67.11 C ANISOU 1145 CB GLU A 166 3293 13032 9173 342 -306 242 C ATOM 1146 CG GLU A 166 134.998 179.768 268.541 1.00 87.78 C ANISOU 1146 CG GLU A 166 5881 15784 11686 373 -293 279 C ATOM 1147 CD GLU A 166 134.669 180.863 267.538 1.00 88.72 C ANISOU 1147 CD GLU A 166 6040 15975 11694 362 -308 263 C ATOM 1148 OE1 GLU A 166 133.472 181.106 267.274 1.00 67.05 O ANISOU 1148 OE1 GLU A 166 3331 13174 8972 357 -325 195 O ATOM 1149 OE2 GLU A 166 135.616 181.485 267.010 1.00 89.89 O ANISOU 1149 OE2 GLU A 166 6181 16239 11735 359 -303 323 O ATOM 1150 N THR A 167 132.457 180.782 272.568 1.00 79.09 N ANISOU 1150 N THR A 167 4936 14390 10725 166 -356 300 N ATOM 1151 CA THR A 167 131.406 180.464 273.532 1.00 64.78 C ANISOU 1151 CA THR A 167 3145 12456 9011 145 -364 270 C ATOM 1152 C THR A 167 131.342 181.576 274.565 1.00 64.23 C ANISOU 1152 C THR A 167 3134 12400 8869 56 -385 322 C ATOM 1153 O THR A 167 132.283 181.759 275.340 1.00 64.52 O ANISOU 1153 O THR A 167 3162 12503 8851 20 -383 398 O ATOM 1154 CB THR A 167 131.660 179.118 274.203 1.00 65.25 C ANISOU 1154 CB THR A 167 3145 12459 9189 189 -340 277 C ATOM 1155 OG1 THR A 167 131.381 178.059 273.280 1.00 66.58 O ANISOU 1155 OG1 THR A 167 3259 12578 9461 268 -319 208 O ATOM 1156 CG2 THR A 167 130.773 178.963 275.423 1.00 64.72 C ANISOU 1156 CG2 THR A 167 3101 12288 9201 155 -348 272 C ATOM 1157 N ASP A 168 130.241 182.315 274.575 1.00 63.50 N ANISOU 1157 N ASP A 168 3097 12252 8778 21 -403 282 N ATOM 1158 CA ASP A 168 129.943 183.255 275.646 1.00 62.96 C ANISOU 1158 CA ASP A 168 3081 12169 8672 -61 -419 314 C ATOM 1159 C ASP A 168 128.700 182.761 276.371 1.00 62.43 C ANISOU 1159 C ASP A 168 3031 11974 8715 -59 -423 267 C ATOM 1160 O ASP A 168 127.644 182.580 275.754 1.00 62.09 O ANISOU 1160 O ASP A 168 2999 11858 8735 -29 -427 200 O ATOM 1161 CB ASP A 168 129.747 184.678 275.115 1.00 62.60 C ANISOU 1161 CB ASP A 168 3083 12165 8537 -110 -430 318 C ATOM 1162 CG ASP A 168 129.401 184.714 273.643 1.00 77.94 C ANISOU 1162 CG ASP A 168 5020 14124 10470 -57 -427 268 C ATOM 1163 OD1 ASP A 168 128.880 183.707 273.124 1.00 79.88 O ANISOU 1163 OD1 ASP A 168 5238 14319 10794 9 -422 209 O ATOM 1164 OD2 ASP A 168 129.652 185.756 272.999 1.00 75.94 O ANISOU 1164 OD2 ASP A 168 4783 13939 10130 -81 -429 290 O ATOM 1165 N LEU A 169 128.837 182.516 277.666 1.00 68.46 N ANISOU 1165 N LEU A 169 3793 12719 9501 -90 -422 306 N ATOM 1166 CA LEU A 169 127.730 182.054 278.484 1.00 61.98 C ANISOU 1166 CA LEU A 169 2984 11782 8782 -90 -424 273 C ATOM 1167 C LEU A 169 127.068 183.235 279.176 1.00 72.66 C ANISOU 1167 C LEU A 169 4402 13117 10087 -167 -441 277 C ATOM 1168 O LEU A 169 127.635 184.326 279.281 1.00 69.56 O ANISOU 1168 O LEU A 169 4037 12805 9588 -227 -449 316 O ATOM 1169 CB LEU A 169 128.200 181.031 279.523 1.00 62.44 C ANISOU 1169 CB LEU A 169 2995 11832 8898 -70 -408 314 C ATOM 1170 CG LEU A 169 128.717 179.694 278.983 1.00 63.16 C ANISOU 1170 CG LEU A 169 3010 11913 9075 12 -382 306 C ATOM 1171 CD1 LEU A 169 128.638 178.608 280.044 1.00 63.48 C ANISOU 1171 CD1 LEU A 169 3005 11894 9220 39 -361 327 C ATOM 1172 CD2 LEU A 169 127.949 179.286 277.737 1.00 68.28 C ANISOU 1172 CD2 LEU A 169 3649 12491 9805 67 -379 222 C ATOM 1173 N CYS A 170 125.847 183.005 279.641 1.00 77.13 N ANISOU 1173 N CYS A 170 4989 13574 10743 -165 -445 235 N ATOM 1174 CA CYS A 170 125.114 184.004 280.396 1.00 83.61 C ANISOU 1174 CA CYS A 170 5868 14363 11538 -233 -457 234 C ATOM 1175 C CYS A 170 124.558 183.391 281.671 1.00 83.77 C ANISOU 1175 C CYS A 170 5883 14313 11633 -237 -453 240 C ATOM 1176 O CYS A 170 123.897 182.348 281.626 1.00 84.00 O ANISOU 1176 O CYS A 170 5884 14251 11783 -181 -444 205 O ATOM 1177 CB CYS A 170 123.966 184.595 279.592 1.00 90.12 C ANISOU 1177 CB CYS A 170 6732 15124 12386 -231 -466 177 C ATOM 1178 SG CYS A 170 122.709 185.191 280.722 1.00 91.89 S ANISOU 1178 SG CYS A 170 7009 15256 12650 -285 -473 163 S ATOM 1179 N LEU A 171 124.823 184.046 282.796 1.00 59.98 N ANISOU 1179 N LEU A 171 2893 11344 8551 -303 -458 284 N ATOM 1180 CA LEU A 171 124.172 183.755 284.067 1.00 79.27 C ANISOU 1180 CA LEU A 171 5343 13732 11045 -319 -455 290 C ATOM 1181 C LEU A 171 124.455 184.938 284.983 1.00 79.03 C ANISOU 1181 C LEU A 171 5351 13771 10907 -408 -465 326 C ATOM 1182 O LEU A 171 125.149 185.888 284.606 1.00 59.82 O ANISOU 1182 O LEU A 171 2933 11417 8379 -454 -472 344 O ATOM 1183 CB LEU A 171 124.647 182.424 284.679 1.00 78.62 C ANISOU 1183 CB LEU A 171 5198 13653 11020 -268 -438 325 C ATOM 1184 CG LEU A 171 123.836 181.788 285.829 1.00 75.96 C ANISOU 1184 CG LEU A 171 4852 13240 10769 -258 -428 326 C ATOM 1185 CD1 LEU A 171 122.340 181.760 285.520 1.00 59.56 C ANISOU 1185 CD1 LEU A 171 2802 11024 8803 -241 -430 255 C ATOM 1186 CD2 LEU A 171 124.337 180.389 286.196 1.00 74.70 C ANISOU 1186 CD2 LEU A 171 4619 13080 10684 -194 -403 359 C ATOM 1187 N ALA A 172 123.891 184.875 286.187 1.00 77.37 N ANISOU 1187 N ALA A 172 5151 13528 10718 -433 -463 334 N ATOM 1188 CA ALA A 172 124.035 185.946 287.162 1.00 74.99 C ANISOU 1188 CA ALA A 172 4881 13285 10325 -519 -471 358 C ATOM 1189 C ALA A 172 125.499 186.192 287.507 1.00 72.91 C ANISOU 1189 C ALA A 172 4591 13167 9944 -559 -476 424 C ATOM 1190 O ALA A 172 126.243 185.259 287.826 1.00 72.71 O ANISOU 1190 O ALA A 172 4517 13198 9913 -522 -469 473 O ATOM 1191 CB ALA A 172 123.247 185.593 288.423 1.00 59.34 C ANISOU 1191 CB ALA A 172 2903 11256 8389 -525 -466 361 C ATOM 1192 N VAL A 173 125.909 187.456 287.435 1.00 71.16 N ANISOU 1192 N VAL A 173 4396 13005 9637 -634 -485 426 N ATOM 1193 CA VAL A 173 127.234 187.885 287.866 1.00 61.04 C ANISOU 1193 CA VAL A 173 3090 11862 8240 -689 -491 484 C ATOM 1194 C VAL A 173 127.038 188.668 289.160 1.00 76.18 C ANISOU 1194 C VAL A 173 5028 13812 10105 -774 -498 488 C ATOM 1195 O VAL A 173 126.669 189.847 289.145 1.00 76.12 O ANISOU 1195 O VAL A 173 5058 13783 10083 -841 -501 452 O ATOM 1196 CB VAL A 173 127.949 188.712 286.790 1.00 61.18 C ANISOU 1196 CB VAL A 173 3111 11927 8207 -713 -494 484 C ATOM 1197 CG1 VAL A 173 128.519 187.802 285.717 1.00 61.43 C ANISOU 1197 CG1 VAL A 173 3107 11973 8261 -631 -488 500 C ATOM 1198 CG2 VAL A 173 127.004 189.729 286.163 1.00 60.48 C ANISOU 1198 CG2 VAL A 173 3071 11752 8156 -739 -492 425 C ATOM 1199 N TYR A 174 127.254 188.012 290.290 1.00 61.55 N ANISOU 1199 N TYR A 174 3147 12013 8228 -772 -498 531 N ATOM 1200 CA TYR A 174 127.091 188.683 291.565 1.00 61.73 C ANISOU 1200 CA TYR A 174 3182 12082 8191 -850 -505 534 C ATOM 1201 C TYR A 174 128.449 189.170 292.036 1.00 74.38 C ANISOU 1201 C TYR A 174 4752 13842 9667 -918 -517 585 C ATOM 1202 O TYR A 174 129.364 188.346 292.188 1.00 74.77 O ANISOU 1202 O TYR A 174 4753 13982 9675 -882 -518 652 O ATOM 1203 CB TYR A 174 126.474 187.743 292.593 1.00 73.10 C ANISOU 1203 CB TYR A 174 4606 13498 9669 -811 -498 554 C ATOM 1204 CG TYR A 174 125.044 187.308 292.306 1.00 73.89 C ANISOU 1204 CG TYR A 174 4735 13440 9900 -754 -486 500 C ATOM 1205 CD1 TYR A 174 124.001 188.221 292.307 1.00 60.17 C ANISOU 1205 CD1 TYR A 174 3049 11615 8197 -796 -486 438 C ATOM 1206 CD2 TYR A 174 124.739 185.975 292.074 1.00 76.75 C ANISOU 1206 CD2 TYR A 174 5066 13738 10356 -661 -473 512 C ATOM 1207 CE1 TYR A 174 122.693 187.826 292.060 1.00 59.43 C ANISOU 1207 CE1 TYR A 174 2978 11382 8219 -745 -476 393 C ATOM 1208 CE2 TYR A 174 123.441 185.567 291.838 1.00 79.93 C ANISOU 1208 CE2 TYR A 174 5489 13997 10882 -613 -463 460 C ATOM 1209 CZ TYR A 174 122.419 186.494 291.826 1.00 81.97 C ANISOU 1209 CZ TYR A 174 5802 14178 11165 -655 -466 403 C ATOM 1210 OH TYR A 174 121.127 186.077 291.582 1.00 58.75 O ANISOU 1210 OH TYR A 174 2877 11099 8347 -608 -457 356 O ATOM 1211 N PRO A 175 128.641 190.479 292.251 1.00 62.81 N ANISOU 1211 N PRO A 175 3307 12414 8144 -1015 -526 557 N ATOM 1212 CA PRO A 175 129.982 190.975 292.627 1.00 65.33 C ANISOU 1212 CA PRO A 175 3590 12885 8347 -1085 -539 601 C ATOM 1213 C PRO A 175 130.617 190.262 293.811 1.00 64.66 C ANISOU 1213 C PRO A 175 3458 12929 8182 -1087 -546 669 C ATOM 1214 O PRO A 175 131.797 189.896 293.744 1.00 65.46 O ANISOU 1214 O PRO A 175 3511 13145 8214 -1080 -552 735 O ATOM 1215 CB PRO A 175 129.730 192.465 292.920 1.00 63.78 C ANISOU 1215 CB PRO A 175 3424 12678 8131 -1194 -542 541 C ATOM 1216 CG PRO A 175 128.231 192.652 292.903 1.00 62.79 C ANISOU 1216 CG PRO A 175 3350 12406 8103 -1177 -530 478 C ATOM 1217 CD PRO A 175 127.699 191.582 292.009 1.00 62.14 C ANISOU 1217 CD PRO A 175 3273 12229 8107 -1064 -521 484 C ATOM 1218 N SER A 176 129.875 190.063 294.897 1.00 64.58 N ANISOU 1218 N SER A 176 3454 12908 8174 -1095 -545 661 N ATOM 1219 CA SER A 176 130.347 189.308 296.048 1.00 65.40 C ANISOU 1219 CA SER A 176 3510 13133 8205 -1085 -549 733 C ATOM 1220 C SER A 176 129.334 188.217 296.366 1.00 64.89 C ANISOU 1220 C SER A 176 3447 12977 8230 -998 -533 743 C ATOM 1221 O SER A 176 128.236 188.181 295.808 1.00 67.45 O ANISOU 1221 O SER A 176 3814 13149 8666 -960 -522 684 O ATOM 1222 CB SER A 176 130.570 190.215 297.268 1.00 74.89 C ANISOU 1222 CB SER A 176 4705 14450 9300 -1194 -564 719 C ATOM 1223 OG SER A 176 131.200 189.511 298.326 1.00 76.08 O ANISOU 1223 OG SER A 176 4800 14749 9359 -1186 -570 800 O ATOM 1224 N ASP A 177 129.714 187.316 297.275 1.00 85.16 N ANISOU 1224 N ASP A 177 5964 15641 10752 -965 -530 822 N ATOM 1225 CA ASP A 177 128.827 186.220 297.651 1.00 84.10 C ANISOU 1225 CA ASP A 177 5820 15425 10708 -880 -510 843 C ATOM 1226 C ASP A 177 127.733 186.661 298.609 1.00 64.94 C ANISOU 1226 C ASP A 177 3424 12960 8289 -918 -509 799 C ATOM 1227 O ASP A 177 126.646 186.071 298.612 1.00 64.29 O ANISOU 1227 O ASP A 177 3357 12752 8317 -858 -492 779 O ATOM 1228 CB ASP A 177 129.629 185.082 298.270 1.00 83.26 C ANISOU 1228 CB ASP A 177 5642 15437 10557 -825 -501 955 C ATOM 1229 CG ASP A 177 130.459 184.353 297.249 1.00 82.02 C ANISOU 1229 CG ASP A 177 5452 15278 10434 -759 -492 997 C ATOM 1230 OD1 ASP A 177 130.035 184.323 296.072 1.00 79.41 O ANISOU 1230 OD1 ASP A 177 5153 14814 10205 -723 -486 935 O ATOM 1231 OD2 ASP A 177 131.530 183.822 297.616 1.00 82.86 O ANISOU 1231 OD2 ASP A 177 5499 15520 10464 -744 -491 1092 O ATOM 1232 N ARG A 178 128.005 187.669 299.439 1.00 65.41 N ANISOU 1232 N ARG A 178 3489 13127 8237 -1018 -526 783 N ATOM 1233 CA ARG A 178 126.935 188.276 300.222 1.00 65.01 C ANISOU 1233 CA ARG A 178 3474 13030 8198 -1064 -524 724 C ATOM 1234 C ARG A 178 125.864 188.858 299.308 1.00 91.33 C ANISOU 1234 C ARG A 178 6872 16179 11649 -1062 -516 632 C ATOM 1235 O ARG A 178 124.664 188.736 299.586 1.00 92.23 O ANISOU 1235 O ARG A 178 7014 16186 11843 -1038 -503 599 O ATOM 1236 CB ARG A 178 127.505 189.351 301.146 1.00 65.83 C ANISOU 1236 CB ARG A 178 3569 13282 8163 -1181 -543 707 C ATOM 1237 CG ARG A 178 128.278 188.801 302.326 1.00 67.11 C ANISOU 1237 CG ARG A 178 3662 13644 8192 -1188 -550 798 C ATOM 1238 CD ARG A 178 127.426 187.826 303.116 1.00 75.40 C ANISOU 1238 CD ARG A 178 4694 14672 9284 -1114 -532 845 C ATOM 1239 NE ARG A 178 127.712 187.861 304.547 1.00 76.62 N ANISOU 1239 NE ARG A 178 4795 15034 9284 -1163 -539 899 N ATOM 1240 CZ ARG A 178 127.157 188.723 305.395 1.00 76.74 C ANISOU 1240 CZ ARG A 178 4820 15115 9224 -1248 -544 844 C ATOM 1241 NH1 ARG A 178 126.290 189.628 304.956 1.00 75.53 N ANISOU 1241 NH1 ARG A 178 4729 14827 9142 -1293 -541 737 N ATOM 1242 NH2 ARG A 178 127.467 188.682 306.681 1.00 69.79 N ANISOU 1242 NH2 ARG A 178 3882 14441 8193 -1287 -551 895 N ATOM 1243 N HIS A 179 126.285 189.492 298.208 1.00 88.43 N ANISOU 1243 N HIS A 179 6527 15778 11293 -1086 -522 597 N ATOM 1244 CA HIS A 179 125.339 189.936 297.189 1.00 85.47 C ANISOU 1244 CA HIS A 179 6207 15236 11030 -1070 -513 524 C ATOM 1245 C HIS A 179 124.524 188.760 296.658 1.00 61.84 C ANISOU 1245 C HIS A 179 3216 12117 8163 -959 -498 531 C ATOM 1246 O HIS A 179 123.290 188.817 296.600 1.00 61.06 O ANISOU 1246 O HIS A 179 3153 11891 8157 -940 -487 482 O ATOM 1247 CB HIS A 179 126.086 190.636 296.049 1.00 62.51 C ANISOU 1247 CB HIS A 179 3309 12335 8108 -1100 -520 505 C ATOM 1248 CG HIS A 179 126.529 192.032 296.372 1.00 62.94 C ANISOU 1248 CG HIS A 179 3374 12455 8086 -1216 -529 468 C ATOM 1249 ND1 HIS A 179 127.538 192.306 297.271 1.00 64.01 N ANISOU 1249 ND1 HIS A 179 3470 12753 8098 -1286 -544 500 N ATOM 1250 CD2 HIS A 179 126.109 193.231 295.903 1.00 62.54 C ANISOU 1250 CD2 HIS A 179 3361 12329 8071 -1277 -524 401 C ATOM 1251 CE1 HIS A 179 127.713 193.613 297.349 1.00 74.95 C ANISOU 1251 CE1 HIS A 179 4870 14155 9453 -1389 -547 445 C ATOM 1252 NE2 HIS A 179 126.858 194.198 296.529 1.00 73.85 N ANISOU 1252 NE2 HIS A 179 4777 13869 9413 -1384 -533 387 N ATOM 1253 N LYS A 180 125.205 187.676 296.279 1.00 62.21 N ANISOU 1253 N LYS A 180 3220 12198 8220 -887 -495 589 N ATOM 1254 CA LYS A 180 124.507 186.487 295.800 1.00 61.76 C ANISOU 1254 CA LYS A 180 3152 12022 8291 -784 -477 590 C ATOM 1255 C LYS A 180 123.591 185.915 296.873 1.00 79.31 C ANISOU 1255 C LYS A 180 5366 14209 10558 -758 -464 603 C ATOM 1256 O LYS A 180 122.443 185.555 296.587 1.00 79.83 O ANISOU 1256 O LYS A 180 5453 14134 10746 -710 -451 560 O ATOM 1257 CB LYS A 180 125.517 185.434 295.343 1.00 62.37 C ANISOU 1257 CB LYS A 180 3174 12156 8367 -718 -472 654 C ATOM 1258 CG LYS A 180 124.908 184.077 295.027 1.00 62.15 C ANISOU 1258 CG LYS A 180 3120 12019 8477 -614 -450 659 C ATOM 1259 CD LYS A 180 125.790 183.269 294.084 1.00 70.50 C ANISOU 1259 CD LYS A 180 4134 13092 9560 -551 -442 688 C ATOM 1260 CE LYS A 180 125.082 181.995 293.634 1.00 70.58 C ANISOU 1260 CE LYS A 180 4117 12971 9731 -452 -417 667 C ATOM 1261 NZ LYS A 180 125.568 181.473 292.319 1.00 71.17 N ANISOU 1261 NZ LYS A 180 4169 13009 9862 -397 -411 648 N ATOM 1262 N ALA A 181 124.079 185.830 298.114 1.00 79.27 N ANISOU 1262 N ALA A 181 5327 14337 10455 -788 -467 664 N ATOM 1263 CA ALA A 181 123.314 185.196 299.185 1.00 78.58 C ANISOU 1263 CA ALA A 181 5222 14235 10401 -755 -451 693 C ATOM 1264 C ALA A 181 121.943 185.835 299.337 1.00 77.56 C ANISOU 1264 C ALA A 181 5147 13985 10339 -780 -446 617 C ATOM 1265 O ALA A 181 120.910 185.179 299.154 1.00 76.70 O ANISOU 1265 O ALA A 181 5042 13742 10357 -716 -428 596 O ATOM 1266 CB ALA A 181 124.082 185.281 300.504 1.00 63.62 C ANISOU 1266 CB ALA A 181 3285 12526 8360 -801 -459 766 C ATOM 1267 N PHE A 182 121.918 187.127 299.667 1.00 61.63 N ANISOU 1267 N PHE A 182 3165 12009 8242 -876 -460 572 N ATOM 1268 CA PHE A 182 120.657 187.764 300.017 1.00 73.16 C ANISOU 1268 CA PHE A 182 4671 13372 9755 -905 -451 510 C ATOM 1269 C PHE A 182 119.676 187.720 298.854 1.00 59.91 C ANISOU 1269 C PHE A 182 3032 11511 8219 -858 -442 449 C ATOM 1270 O PHE A 182 118.503 187.381 299.041 1.00 69.72 O ANISOU 1270 O PHE A 182 4288 12642 9559 -819 -427 428 O ATOM 1271 CB PHE A 182 120.904 189.198 300.491 1.00 72.93 C ANISOU 1271 CB PHE A 182 4666 13424 9620 -1021 -464 468 C ATOM 1272 CG PHE A 182 121.235 189.300 301.961 1.00 73.27 C ANISOU 1272 CG PHE A 182 4667 13649 9522 -1075 -468 511 C ATOM 1273 CD1 PHE A 182 120.252 189.095 302.920 1.00 73.26 C ANISOU 1273 CD1 PHE A 182 4660 13642 9532 -1065 -453 516 C ATOM 1274 CD2 PHE A 182 122.523 189.593 302.384 1.00 73.40 C ANISOU 1274 CD2 PHE A 182 4646 13851 9393 -1135 -487 548 C ATOM 1275 CE1 PHE A 182 120.546 189.183 304.270 1.00 74.63 C ANISOU 1275 CE1 PHE A 182 4790 14000 9566 -1114 -456 558 C ATOM 1276 CE2 PHE A 182 122.823 189.682 303.739 1.00 64.43 C ANISOU 1276 CE2 PHE A 182 3466 12900 8116 -1187 -492 586 C ATOM 1277 CZ PHE A 182 121.833 189.478 304.680 1.00 76.19 C ANISOU 1277 CZ PHE A 182 4948 14389 9610 -1176 -477 591 C ATOM 1278 N HIS A 183 120.142 188.010 297.640 1.00 59.68 N ANISOU 1278 N HIS A 183 3019 11456 8202 -857 -452 425 N ATOM 1279 CA HIS A 183 119.238 187.973 296.497 1.00 67.13 C ANISOU 1279 CA HIS A 183 3996 12243 9269 -812 -445 370 C ATOM 1280 C HIS A 183 118.698 186.565 296.258 1.00 67.38 C ANISOU 1280 C HIS A 183 3997 12185 9419 -711 -431 385 C ATOM 1281 O HIS A 183 117.530 186.396 295.887 1.00 57.95 O ANISOU 1281 O HIS A 183 2825 10855 8340 -675 -421 340 O ATOM 1282 CB HIS A 183 119.937 188.499 295.250 1.00 67.10 C ANISOU 1282 CB HIS A 183 4005 12247 9242 -827 -457 351 C ATOM 1283 CG HIS A 183 119.054 188.526 294.046 1.00 67.51 C ANISOU 1283 CG HIS A 183 4087 12159 9404 -784 -452 299 C ATOM 1284 ND1 HIS A 183 119.047 187.519 293.106 1.00 57.81 N ANISOU 1284 ND1 HIS A 183 2837 10874 8254 -701 -450 298 N ATOM 1285 CD2 HIS A 183 118.123 189.424 293.645 1.00 69.16 C ANISOU 1285 CD2 HIS A 183 4343 12277 9658 -811 -448 246 C ATOM 1286 CE1 HIS A 183 118.162 187.805 292.167 1.00 72.32 C ANISOU 1286 CE1 HIS A 183 4707 12601 10172 -681 -449 247 C ATOM 1287 NE2 HIS A 183 117.586 188.955 292.471 1.00 70.70 N ANISOU 1287 NE2 HIS A 183 4543 12373 9947 -745 -447 219 N ATOM 1288 N LEU A 184 119.529 185.539 296.464 1.00 68.80 N ANISOU 1288 N LEU A 184 4123 12437 9581 -664 -428 446 N ATOM 1289 CA LEU A 184 119.033 184.170 296.357 1.00 69.57 C ANISOU 1289 CA LEU A 184 4181 12448 9804 -570 -408 458 C ATOM 1290 C LEU A 184 118.034 183.854 297.456 1.00 70.50 C ANISOU 1290 C LEU A 184 4294 12523 9970 -558 -390 466 C ATOM 1291 O LEU A 184 117.093 183.082 297.241 1.00 70.83 O ANISOU 1291 O LEU A 184 4325 12438 10149 -495 -373 439 O ATOM 1292 CB LEU A 184 120.186 183.175 296.408 1.00 60.18 C ANISOU 1292 CB LEU A 184 2929 11350 8585 -525 -402 529 C ATOM 1293 CG LEU A 184 120.965 183.013 295.110 1.00 61.57 C ANISOU 1293 CG LEU A 184 3096 11526 8771 -500 -410 516 C ATOM 1294 CD1 LEU A 184 121.633 181.662 295.116 1.00 62.30 C ANISOU 1294 CD1 LEU A 184 3118 11646 8906 -425 -391 573 C ATOM 1295 CD2 LEU A 184 120.059 183.177 293.895 1.00 59.39 C ANISOU 1295 CD2 LEU A 184 2856 11103 8605 -476 -412 431 C ATOM 1296 N LEU A 185 118.236 184.419 298.643 1.00 59.60 N ANISOU 1296 N LEU A 185 2916 11251 8480 -617 -394 501 N ATOM 1297 CA LEU A 185 117.222 184.318 299.681 1.00 59.48 C ANISOU 1297 CA LEU A 185 2901 11199 8498 -613 -377 504 C ATOM 1298 C LEU A 185 116.062 185.261 299.404 1.00 92.50 C ANISOU 1298 C LEU A 185 7145 15267 12734 -650 -378 426 C ATOM 1299 O LEU A 185 114.908 184.923 299.684 1.00 79.40 O ANISOU 1299 O LEU A 185 5491 13504 11175 -616 -360 406 O ATOM 1300 CB LEU A 185 117.834 184.624 301.045 1.00 60.28 C ANISOU 1300 CB LEU A 185 2980 11469 8455 -665 -381 567 C ATOM 1301 CG LEU A 185 118.262 183.445 301.909 1.00 61.17 C ANISOU 1301 CG LEU A 185 3023 11666 8551 -606 -364 662 C ATOM 1302 CD1 LEU A 185 118.828 182.325 301.068 1.00 61.41 C ANISOU 1302 CD1 LEU A 185 3013 11662 8658 -528 -355 691 C ATOM 1303 CD2 LEU A 185 119.289 183.936 302.889 1.00 62.09 C ANISOU 1303 CD2 LEU A 185 3117 11985 8489 -671 -380 722 C ATOM 1304 N PHE A 186 116.352 186.440 298.845 1.00 58.29 N ANISOU 1304 N PHE A 186 2856 10952 8340 -718 -396 384 N ATOM 1305 CA PHE A 186 115.315 187.449 298.656 1.00 57.54 C ANISOU 1305 CA PHE A 186 2816 10760 8286 -760 -393 319 C ATOM 1306 C PHE A 186 114.238 186.973 297.693 1.00 63.86 C ANISOU 1306 C PHE A 186 3632 11394 9239 -694 -384 276 C ATOM 1307 O PHE A 186 113.055 187.281 297.877 1.00 62.79 O ANISOU 1307 O PHE A 186 3523 11161 9174 -697 -371 242 O ATOM 1308 CB PHE A 186 115.925 188.753 298.154 1.00 57.51 C ANISOU 1308 CB PHE A 186 2848 10806 8198 -841 -409 288 C ATOM 1309 CG PHE A 186 114.912 189.821 297.872 1.00 68.96 C ANISOU 1309 CG PHE A 186 4349 12156 9696 -883 -400 227 C ATOM 1310 CD1 PHE A 186 114.435 190.624 298.893 1.00 69.54 C ANISOU 1310 CD1 PHE A 186 4433 12271 9717 -951 -390 215 C ATOM 1311 CD2 PHE A 186 114.440 190.029 296.585 1.00 68.84 C ANISOU 1311 CD2 PHE A 186 4362 12033 9762 -856 -401 190 C ATOM 1312 CE1 PHE A 186 113.504 191.614 298.637 1.00 68.77 C ANISOU 1312 CE1 PHE A 186 4375 12096 9659 -991 -376 166 C ATOM 1313 CE2 PHE A 186 113.507 191.016 296.324 1.00 68.39 C ANISOU 1313 CE2 PHE A 186 4347 11888 9750 -891 -390 144 C ATOM 1314 CZ PHE A 186 113.039 191.809 297.351 1.00 55.75 C ANISOU 1314 CZ PHE A 186 2756 10320 8105 -958 -376 134 C ATOM 1315 N GLU A 187 114.621 186.236 296.652 1.00 56.79 N ANISOU 1315 N GLU A 187 2716 10465 8396 -637 -390 275 N ATOM 1316 CA GLU A 187 113.631 185.711 295.723 1.00 66.81 C ANISOU 1316 CA GLU A 187 3990 11585 9810 -575 -384 229 C ATOM 1317 C GLU A 187 112.996 184.419 296.215 1.00 70.53 C ANISOU 1317 C GLU A 187 4416 11987 10394 -503 -363 241 C ATOM 1318 O GLU A 187 112.218 183.810 295.473 1.00 72.54 O ANISOU 1318 O GLU A 187 4662 12118 10781 -448 -357 200 O ATOM 1319 CB GLU A 187 114.252 185.479 294.344 1.00 64.01 C ANISOU 1319 CB GLU A 187 3628 11223 9470 -545 -398 213 C ATOM 1320 CG GLU A 187 115.205 184.293 294.257 1.00 63.54 C ANISOU 1320 CG GLU A 187 3509 11216 9417 -490 -394 253 C ATOM 1321 CD GLU A 187 115.671 184.041 292.834 1.00 63.09 C ANISOU 1321 CD GLU A 187 3444 11139 9389 -456 -405 228 C ATOM 1322 OE1 GLU A 187 115.057 184.603 291.906 1.00 62.41 O ANISOU 1322 OE1 GLU A 187 3394 10982 9338 -461 -414 181 O ATOM 1323 OE2 GLU A 187 116.651 183.290 292.640 1.00 57.46 O ANISOU 1323 OE2 GLU A 187 2686 10486 8660 -422 -403 261 O ATOM 1324 N ALA A 188 113.314 183.982 297.434 1.00 56.92 N ANISOU 1324 N ALA A 188 2659 10344 8623 -502 -350 295 N ATOM 1325 CA ALA A 188 112.689 182.808 298.024 1.00 57.14 C ANISOU 1325 CA ALA A 188 2641 10313 8756 -435 -323 311 C ATOM 1326 C ALA A 188 111.592 183.207 299.000 1.00 56.83 C ANISOU 1326 C ALA A 188 2623 10237 8733 -456 -307 304 C ATOM 1327 O ALA A 188 110.466 182.707 298.927 1.00 65.11 O ANISOU 1327 O ALA A 188 3665 11161 9912 -412 -289 267 O ATOM 1328 CB ALA A 188 113.742 181.935 298.721 1.00 58.09 C ANISOU 1328 CB ALA A 188 2701 10552 8818 -406 -313 390 C ATOM 1329 N PHE A 189 111.913 184.089 299.942 1.00 57.03 N ANISOU 1329 N PHE A 189 2669 10373 8628 -524 -313 335 N ATOM 1330 CA PHE A 189 110.879 184.580 300.837 1.00 56.74 C ANISOU 1330 CA PHE A 189 2654 10304 8602 -550 -297 324 C ATOM 1331 C PHE A 189 109.781 185.246 300.039 1.00 55.84 C ANISOU 1331 C PHE A 189 2590 10049 8577 -561 -298 252 C ATOM 1332 O PHE A 189 108.602 184.913 300.175 1.00 68.19 O ANISOU 1332 O PHE A 189 4153 11503 10253 -525 -278 227 O ATOM 1333 CB PHE A 189 111.441 185.577 301.844 1.00 57.14 C ANISOU 1333 CB PHE A 189 2718 10498 8493 -633 -305 353 C ATOM 1334 CG PHE A 189 112.385 184.985 302.836 1.00 80.69 C ANISOU 1334 CG PHE A 189 5646 13641 11370 -626 -304 436 C ATOM 1335 CD1 PHE A 189 112.577 183.614 302.939 1.00 80.91 C ANISOU 1335 CD1 PHE A 189 5619 13660 11463 -543 -287 487 C ATOM 1336 CD2 PHE A 189 113.080 185.821 303.686 1.00 81.64 C ANISOU 1336 CD2 PHE A 189 5760 13946 11312 -708 -317 469 C ATOM 1337 CE1 PHE A 189 113.462 183.101 303.870 1.00 59.57 C ANISOU 1337 CE1 PHE A 189 2865 11109 8660 -535 -284 577 C ATOM 1338 CE2 PHE A 189 113.957 185.316 304.614 1.00 83.94 C ANISOU 1338 CE2 PHE A 189 5996 14405 11491 -705 -318 553 C ATOM 1339 CZ PHE A 189 114.151 183.955 304.709 1.00 85.46 C ANISOU 1339 CZ PHE A 189 6140 14576 11755 -615 -301 615 C ATOM 1340 N THR A 190 110.162 186.188 299.179 1.00 55.53 N ANISOU 1340 N THR A 190 2591 10017 8491 -608 -319 221 N ATOM 1341 CA THR A 190 109.159 187.003 298.507 1.00 61.84 C ANISOU 1341 CA THR A 190 3439 10704 9355 -627 -318 166 C ATOM 1342 C THR A 190 108.455 186.225 297.407 1.00 61.15 C ANISOU 1342 C THR A 190 3341 10482 9411 -556 -319 132 C ATOM 1343 O THR A 190 107.237 186.326 297.250 1.00 53.83 O ANISOU 1343 O THR A 190 2431 9441 8582 -540 -307 99 O ATOM 1344 CB THR A 190 109.791 188.274 297.955 1.00 54.65 C ANISOU 1344 CB THR A 190 2568 9848 8350 -700 -335 149 C ATOM 1345 OG1 THR A 190 110.641 188.839 298.971 1.00 55.24 O ANISOU 1345 OG1 THR A 190 2638 10064 8288 -767 -338 178 O ATOM 1346 CG2 THR A 190 108.665 189.278 297.473 1.00 60.32 C ANISOU 1346 CG2 THR A 190 3333 10457 9127 -726 -326 103 C ATOM 1347 N GLY A 191 109.198 185.437 296.639 1.00 60.96 N ANISOU 1347 N GLY A 191 3286 10472 9404 -513 -331 137 N ATOM 1348 CA GLY A 191 108.570 184.652 295.595 1.00 54.39 C ANISOU 1348 CA GLY A 191 2436 9518 8710 -448 -333 98 C ATOM 1349 C GLY A 191 107.647 183.593 296.155 1.00 54.46 C ANISOU 1349 C GLY A 191 2405 9438 8849 -390 -307 86 C ATOM 1350 O GLY A 191 106.487 183.487 295.756 1.00 54.02 O ANISOU 1350 O GLY A 191 2355 9261 8909 -366 -302 44 O ATOM 1351 N PHE A 192 108.136 182.826 297.119 1.00 55.07 N ANISOU 1351 N PHE A 192 2438 9582 8904 -369 -290 125 N ATOM 1352 CA PHE A 192 107.425 181.651 297.595 1.00 55.31 C ANISOU 1352 CA PHE A 192 2418 9541 9057 -305 -260 108 C ATOM 1353 C PHE A 192 107.052 181.704 299.064 1.00 55.52 C ANISOU 1353 C PHE A 192 2440 9617 9039 -317 -235 148 C ATOM 1354 O PHE A 192 105.918 181.363 299.422 1.00 70.06 O ANISOU 1354 O PHE A 192 4272 11374 10975 -289 -211 113 O ATOM 1355 CB PHE A 192 108.287 180.412 297.345 1.00 56.02 C ANISOU 1355 CB PHE A 192 2443 9660 9182 -248 -252 121 C ATOM 1356 CG PHE A 192 107.576 179.118 297.561 1.00 56.34 C ANISOU 1356 CG PHE A 192 2423 9620 9365 -177 -219 78 C ATOM 1357 CD1 PHE A 192 106.899 178.498 296.514 1.00 75.68 C ANISOU 1357 CD1 PHE A 192 4855 11940 11960 -134 -217 -12 C ATOM 1358 CD2 PHE A 192 107.592 178.504 298.801 1.00 63.55 C ANISOU 1358 CD2 PHE A 192 3299 10595 10252 -154 -186 128 C ATOM 1359 CE1 PHE A 192 106.252 177.282 296.716 1.00 75.61 C ANISOU 1359 CE1 PHE A 192 4828 11874 12026 -71 -181 -70 C ATOM 1360 CE2 PHE A 192 106.953 177.296 299.003 1.00 57.31 C ANISOU 1360 CE2 PHE A 192 2451 9750 9573 -88 -150 83 C ATOM 1361 CZ PHE A 192 106.281 176.683 297.963 1.00 75.96 C ANISOU 1361 CZ PHE A 192 4809 11998 12053 -48 -147 -32 C ATOM 1362 N VAL A 193 107.982 182.073 299.938 1.00 55.99 N ANISOU 1362 N VAL A 193 2499 9819 8954 -356 -239 220 N ATOM 1363 CA VAL A 193 107.753 181.789 301.349 1.00 56.43 C ANISOU 1363 CA VAL A 193 2530 9936 8975 -350 -212 274 C ATOM 1364 C VAL A 193 106.720 182.726 301.933 1.00 55.90 C ANISOU 1364 C VAL A 193 2507 9834 8900 -393 -203 253 C ATOM 1365 O VAL A 193 105.859 182.308 302.706 1.00 55.97 O ANISOU 1365 O VAL A 193 2497 9808 8962 -364 -173 257 O ATOM 1366 CB VAL A 193 109.069 181.820 302.134 1.00 57.23 C ANISOU 1366 CB VAL A 193 2608 10213 8923 -375 -219 363 C ATOM 1367 CG1 VAL A 193 108.771 182.138 303.566 1.00 87.42 C ANISOU 1367 CG1 VAL A 193 6429 14119 12669 -401 -203 414 C ATOM 1368 CG2 VAL A 193 109.719 180.468 302.030 1.00 57.95 C ANISOU 1368 CG2 VAL A 193 2632 10326 9059 -304 -205 403 C ATOM 1369 N VAL A 194 106.783 183.997 301.579 1.00 55.43 N ANISOU 1369 N VAL A 194 2503 9783 8774 -462 -225 229 N ATOM 1370 CA VAL A 194 105.731 184.931 301.997 1.00 66.91 C ANISOU 1370 CA VAL A 194 3997 11187 10237 -503 -212 202 C ATOM 1371 C VAL A 194 104.363 184.488 301.479 1.00 63.11 C ANISOU 1371 C VAL A 194 3518 10540 9921 -451 -194 142 C ATOM 1372 O VAL A 194 103.409 184.453 302.273 1.00 61.06 O ANISOU 1372 O VAL A 194 3253 10248 9698 -442 -165 139 O ATOM 1373 CB VAL A 194 106.097 186.367 301.584 1.00 68.94 C ANISOU 1373 CB VAL A 194 4304 11497 10392 -587 -234 188 C ATOM 1374 CG1 VAL A 194 104.855 187.177 301.260 1.00 70.29 C ANISOU 1374 CG1 VAL A 194 4516 11561 10631 -608 -222 142 C ATOM 1375 CG2 VAL A 194 106.911 187.028 302.662 1.00 55.45 C ANISOU 1375 CG2 VAL A 194 2586 9979 8504 -659 -237 238 C ATOM 1376 N PRO A 195 104.186 184.142 300.181 1.00 64.21 N ANISOU 1376 N PRO A 195 3658 10583 10157 -417 -209 93 N ATOM 1377 CA PRO A 195 102.896 183.585 299.734 1.00 66.18 C ANISOU 1377 CA PRO A 195 3896 10690 10561 -367 -194 27 C ATOM 1378 C PRO A 195 102.548 182.240 300.347 1.00 70.93 C ANISOU 1378 C PRO A 195 4437 11280 11233 -300 -163 12 C ATOM 1379 O PRO A 195 101.415 182.043 300.793 1.00 72.59 O ANISOU 1379 O PRO A 195 4658 11432 11491 -279 -136 -25 O ATOM 1380 CB PRO A 195 103.089 183.456 298.219 1.00 53.41 C ANISOU 1380 CB PRO A 195 2282 9006 9006 -349 -223 -9 C ATOM 1381 CG PRO A 195 104.072 184.493 297.884 1.00 53.34 C ANISOU 1381 CG PRO A 195 2314 9086 8867 -409 -250 30 C ATOM 1382 CD PRO A 195 105.033 184.485 299.023 1.00 53.92 C ANISOU 1382 CD PRO A 195 2372 9298 8816 -435 -243 87 C ATOM 1383 N PHE A 196 103.494 181.298 300.345 1.00 54.78 N ANISOU 1383 N PHE A 196 2344 9296 9174 -264 -164 41 N ATOM 1384 CA PHE A 196 103.199 179.991 300.928 1.00 55.36 C ANISOU 1384 CA PHE A 196 2357 9375 9304 -199 -129 31 C ATOM 1385 C PHE A 196 102.755 180.120 302.381 1.00 85.12 C ANISOU 1385 C PHE A 196 6125 13203 13015 -206 -99 92 C ATOM 1386 O PHE A 196 101.908 179.347 302.835 1.00 85.47 O ANISOU 1386 O PHE A 196 6138 13223 13113 -159 -66 68 O ATOM 1387 CB PHE A 196 104.408 179.058 300.817 1.00 86.11 C ANISOU 1387 CB PHE A 196 6198 13341 13177 -163 -130 77 C ATOM 1388 CG PHE A 196 104.100 177.612 301.142 1.00 83.47 C ANISOU 1388 CG PHE A 196 5796 13006 12912 -88 -91 58 C ATOM 1389 CD1 PHE A 196 103.244 176.872 300.335 1.00 81.59 C ANISOU 1389 CD1 PHE A 196 5565 12684 12753 -42 -80 -56 C ATOM 1390 CD2 PHE A 196 104.670 176.991 302.247 1.00 80.64 C ANISOU 1390 CD2 PHE A 196 5396 12748 12494 -62 -65 170 C ATOM 1391 CE1 PHE A 196 102.959 175.542 300.630 1.00 78.77 C ANISOU 1391 CE1 PHE A 196 5149 12361 12418 25 -43 -66 C ATOM 1392 CE2 PHE A 196 104.389 175.663 302.542 1.00 77.79 C ANISOU 1392 CE2 PHE A 196 4975 12392 12191 11 -26 176 C ATOM 1393 CZ PHE A 196 103.534 174.940 301.732 1.00 76.98 C ANISOU 1393 CZ PHE A 196 4850 12221 12177 54 -14 52 C ATOM 1394 N LEU A 197 103.287 181.105 303.116 1.00 84.39 N ANISOU 1394 N LEU A 197 6064 13201 12799 -267 -109 168 N ATOM 1395 CA LEU A 197 102.814 181.327 304.481 1.00 82.57 C ANISOU 1395 CA LEU A 197 5831 13026 12514 -278 -81 223 C ATOM 1396 C LEU A 197 101.441 181.981 304.492 1.00 79.79 C ANISOU 1396 C LEU A 197 5516 12581 12220 -295 -66 161 C ATOM 1397 O LEU A 197 100.602 181.656 305.339 1.00 80.39 O ANISOU 1397 O LEU A 197 5572 12662 12311 -270 -32 179 O ATOM 1398 CB LEU A 197 103.805 182.181 305.269 1.00 56.33 C ANISOU 1398 CB LEU A 197 2515 9872 9015 -344 -98 316 C ATOM 1399 CG LEU A 197 105.152 181.548 305.614 1.00 57.18 C ANISOU 1399 CG LEU A 197 2580 10110 9036 -328 -106 398 C ATOM 1400 CD1 LEU A 197 105.766 182.224 306.835 1.00 57.96 C ANISOU 1400 CD1 LEU A 197 2666 10410 8946 -385 -111 494 C ATOM 1401 CD2 LEU A 197 105.021 180.042 305.810 1.00 57.68 C ANISOU 1401 CD2 LEU A 197 2584 10135 9195 -238 -75 420 C ATOM 1402 N ILE A 198 101.196 182.911 303.569 1.00 77.19 N ANISOU 1402 N ILE A 198 5236 12176 11915 -337 -90 102 N ATOM 1403 CA ILE A 198 99.902 183.583 303.525 1.00 53.86 C ANISOU 1403 CA ILE A 198 2313 9139 9013 -354 -74 53 C ATOM 1404 C ILE A 198 98.808 182.606 303.123 1.00 53.64 C ANISOU 1404 C ILE A 198 2288 9005 9088 -286 -53 -38 C ATOM 1405 O ILE A 198 97.743 182.551 303.748 1.00 53.58 O ANISOU 1405 O ILE A 198 2289 8983 9085 -272 -21 -56 O ATOM 1406 CB ILE A 198 99.948 184.793 302.576 1.00 53.24 C ANISOU 1406 CB ILE A 198 2289 9015 8926 -410 -102 29 C ATOM 1407 CG1 ILE A 198 100.767 185.927 303.201 1.00 53.60 C ANISOU 1407 CG1 ILE A 198 2354 9205 8805 -492 -112 103 C ATOM 1408 CG2 ILE A 198 98.543 185.258 302.253 1.00 52.63 C ANISOU 1408 CG2 ILE A 198 2258 8822 8918 -408 -84 -29 C ATOM 1409 CD1 ILE A 198 100.635 187.272 302.492 1.00 53.10 C ANISOU 1409 CD1 ILE A 198 2343 9119 8714 -556 -126 82 C ATOM 1410 N VAL A 199 99.056 181.810 302.086 1.00 53.72 N ANISOU 1410 N VAL A 199 2302 8976 9132 -245 -71 -85 N ATOM 1411 CA VAL A 199 98.014 180.937 301.553 1.00 81.11 C ANISOU 1411 CA VAL A 199 5796 12395 12628 -189 -56 -182 C ATOM 1412 C VAL A 199 97.859 179.724 302.464 1.00 80.82 C ANISOU 1412 C VAL A 199 5686 12443 12580 -134 -22 -153 C ATOM 1413 O VAL A 199 96.993 178.870 302.244 1.00 79.90 O ANISOU 1413 O VAL A 199 5566 12350 12442 -86 -5 -203 O ATOM 1414 CB VAL A 199 98.302 180.512 300.091 1.00 53.57 C ANISOU 1414 CB VAL A 199 2333 8854 9167 -167 -85 -254 C ATOM 1415 CG1 VAL A 199 98.685 181.713 299.241 1.00 53.01 C ANISOU 1415 CG1 VAL A 199 2314 8706 9122 -218 -121 -222 C ATOM 1416 CG2 VAL A 199 99.340 179.392 300.018 1.00 54.30 C ANISOU 1416 CG2 VAL A 199 2355 9006 9271 -127 -86 -231 C ATOM 1417 N VAL A 200 98.684 179.642 303.501 1.00 54.91 N ANISOU 1417 N VAL A 200 2334 9235 9294 -140 -11 -52 N ATOM 1418 CA VAL A 200 98.557 178.554 304.458 1.00 55.68 C ANISOU 1418 CA VAL A 200 2354 9404 9398 -84 25 8 C ATOM 1419 C VAL A 200 97.762 179.048 305.658 1.00 67.87 C ANISOU 1419 C VAL A 200 3916 10962 10909 -98 55 66 C ATOM 1420 O VAL A 200 96.998 178.289 306.262 1.00 67.53 O ANISOU 1420 O VAL A 200 3850 10934 10874 -48 89 101 O ATOM 1421 CB VAL A 200 99.939 178.003 304.852 1.00 56.48 C ANISOU 1421 CB VAL A 200 2414 9579 9466 -69 23 116 C ATOM 1422 CG1 VAL A 200 99.954 177.546 306.294 1.00 58.17 C ANISOU 1422 CG1 VAL A 200 2596 9870 9636 -40 60 248 C ATOM 1423 CG2 VAL A 200 100.304 176.856 303.925 1.00 56.85 C ANISOU 1423 CG2 VAL A 200 2416 9618 9567 -15 21 66 C ATOM 1424 N ALA A 201 97.893 180.336 305.983 1.00 69.72 N ANISOU 1424 N ALA A 201 4192 11199 11100 -166 44 90 N ATOM 1425 CA ALA A 201 97.089 180.900 307.062 1.00 73.24 C ANISOU 1425 CA ALA A 201 4643 11679 11505 -184 74 154 C ATOM 1426 C ALA A 201 95.628 181.021 306.648 1.00 76.04 C ANISOU 1426 C ALA A 201 5025 11954 11913 -172 89 52 C ATOM 1427 O ALA A 201 94.728 180.563 307.362 1.00 78.14 O ANISOU 1427 O ALA A 201 5278 12235 12178 -134 123 90 O ATOM 1428 CB ALA A 201 97.646 182.261 307.484 1.00 55.41 C ANISOU 1428 CB ALA A 201 2411 9491 9153 -265 58 217 C ATOM 1429 N SER A 202 95.376 181.623 305.483 1.00 75.32 N ANISOU 1429 N SER A 202 5003 11782 11835 -200 63 -52 N ATOM 1430 CA SER A 202 94.003 181.832 305.037 1.00 72.90 C ANISOU 1430 CA SER A 202 4763 11427 11510 -193 73 -129 C ATOM 1431 C SER A 202 93.323 180.511 304.694 1.00 73.91 C ANISOU 1431 C SER A 202 4875 11593 11613 -122 80 -153 C ATOM 1432 O SER A 202 92.190 180.258 305.121 1.00 74.14 O ANISOU 1432 O SER A 202 4897 11645 11626 -95 106 -124 O ATOM 1433 CB SER A 202 93.982 182.775 303.834 1.00 70.12 C ANISOU 1433 CB SER A 202 4495 10992 11154 -234 42 -210 C ATOM 1434 OG SER A 202 94.420 182.110 302.663 1.00 52.61 O ANISOU 1434 OG SER A 202 2291 8763 8934 -206 12 -272 O ATOM 1435 N TYR A 203 93.995 179.652 303.927 1.00 53.89 N ANISOU 1435 N TYR A 203 2314 9077 9083 -90 60 -169 N ATOM 1436 CA TYR A 203 93.351 178.432 303.455 1.00 54.22 C ANISOU 1436 CA TYR A 203 2324 9172 9107 -27 66 -151 C ATOM 1437 C TYR A 203 93.279 177.341 304.511 1.00 55.06 C ANISOU 1437 C TYR A 203 2336 9303 9280 32 105 -45 C ATOM 1438 O TYR A 203 92.603 176.332 304.283 1.00 55.42 O ANISOU 1438 O TYR A 203 2344 9356 9358 88 120 3 O ATOM 1439 CB TYR A 203 94.065 177.883 302.223 1.00 61.83 C ANISOU 1439 CB TYR A 203 3289 10157 10047 -13 36 -201 C ATOM 1440 CG TYR A 203 93.154 177.661 301.038 1.00 54.05 C ANISOU 1440 CG TYR A 203 2336 9219 8983 2 21 -212 C ATOM 1441 CD1 TYR A 203 92.142 176.715 301.081 1.00 73.02 C ANISOU 1441 CD1 TYR A 203 4689 11626 11431 55 43 -120 C ATOM 1442 CD2 TYR A 203 93.319 178.390 299.870 1.00 53.51 C ANISOU 1442 CD2 TYR A 203 2334 9171 8826 -35 -14 -289 C ATOM 1443 CE1 TYR A 203 91.314 176.512 299.996 1.00 75.75 C ANISOU 1443 CE1 TYR A 203 5046 11977 11757 66 28 -91 C ATOM 1444 CE2 TYR A 203 92.506 178.194 298.783 1.00 53.34 C ANISOU 1444 CE2 TYR A 203 2327 9213 8725 -21 -29 -236 C ATOM 1445 CZ TYR A 203 91.501 177.256 298.849 1.00 78.72 C ANISOU 1445 CZ TYR A 203 5487 12401 12021 27 -9 -134 C ATOM 1446 OH TYR A 203 90.679 177.054 297.763 1.00 81.01 O ANISOU 1446 OH TYR A 203 5777 12682 12321 38 -24 -79 O ATOM 1447 N ALA A 204 93.966 177.499 305.642 1.00 55.45 N ANISOU 1447 N ALA A 204 2347 9361 9362 23 123 15 N ATOM 1448 CA ALA A 204 93.760 176.601 306.769 1.00 83.86 C ANISOU 1448 CA ALA A 204 5909 12961 12992 80 165 153 C ATOM 1449 C ALA A 204 92.846 177.193 307.830 1.00 56.12 C ANISOU 1449 C ALA A 204 2421 9435 9466 69 194 204 C ATOM 1450 O ALA A 204 92.265 176.436 308.613 1.00 59.11 O ANISOU 1450 O ALA A 204 2779 9798 9882 124 232 314 O ATOM 1451 CB ALA A 204 95.099 176.206 307.408 1.00 84.86 C ANISOU 1451 CB ALA A 204 5991 13130 13123 90 170 239 C ATOM 1452 N ASP A 205 92.711 178.521 307.876 1.00 55.49 N ANISOU 1452 N ASP A 205 2380 9353 9350 2 182 146 N ATOM 1453 CA ASP A 205 91.668 179.124 308.700 1.00 55.44 C ANISOU 1453 CA ASP A 205 2392 9338 9335 -8 213 200 C ATOM 1454 C ASP A 205 90.292 178.652 308.256 1.00 55.11 C ANISOU 1454 C ASP A 205 2376 9250 9314 32 223 186 C ATOM 1455 O ASP A 205 89.420 178.378 309.088 1.00 89.64 O ANISOU 1455 O ASP A 205 6746 13596 13717 68 260 283 O ATOM 1456 CB ASP A 205 91.763 180.652 308.637 1.00 54.91 C ANISOU 1456 CB ASP A 205 2358 9271 9236 -91 201 147 C ATOM 1457 CG ASP A 205 90.418 181.339 308.856 1.00 60.52 C ANISOU 1457 CG ASP A 205 3101 9955 9939 -104 225 139 C ATOM 1458 OD1 ASP A 205 90.148 181.782 309.993 1.00 54.94 O ANISOU 1458 OD1 ASP A 205 2382 9274 9219 -115 260 229 O ATOM 1459 OD2 ASP A 205 89.633 181.447 307.886 1.00 59.94 O ANISOU 1459 OD2 ASP A 205 3064 9853 9857 -104 211 54 O ATOM 1460 N ILE A 206 90.084 178.544 306.943 1.00 54.56 N ANISOU 1460 N ILE A 206 2330 9174 9225 29 191 91 N ATOM 1461 CA ILE A 206 88.802 178.086 306.414 1.00 54.42 C ANISOU 1461 CA ILE A 206 2336 9110 9233 66 196 127 C ATOM 1462 C ILE A 206 88.506 176.670 306.895 1.00 55.30 C ANISOU 1462 C ILE A 206 2410 9158 9445 144 228 252 C ATOM 1463 O ILE A 206 87.491 176.417 307.553 1.00 58.72 O ANISOU 1463 O ILE A 206 2853 9521 9936 177 262 337 O ATOM 1464 CB ILE A 206 88.794 178.159 304.878 1.00 62.39 C ANISOU 1464 CB ILE A 206 3363 10141 10203 50 154 49 C ATOM 1465 CG1 ILE A 206 89.085 179.575 304.383 1.00 53.17 C ANISOU 1465 CG1 ILE A 206 2261 9003 8938 -24 127 -55 C ATOM 1466 CG2 ILE A 206 87.463 177.671 304.336 1.00 62.43 C ANISOU 1466 CG2 ILE A 206 3392 10066 10264 86 159 110 C ATOM 1467 CD1 ILE A 206 89.405 179.612 302.905 1.00 52.87 C ANISOU 1467 CD1 ILE A 206 2263 8989 8836 -37 85 -109 C ATOM 1468 N SER A 207 89.392 175.722 306.567 1.00 55.89 N ANISOU 1468 N SER A 207 2440 9244 9552 175 222 267 N ATOM 1469 CA SER A 207 89.182 174.327 306.952 1.00 77.14 C ANISOU 1469 CA SER A 207 5092 11860 12359 249 259 386 C ATOM 1470 C SER A 207 89.075 174.154 308.461 1.00 57.44 C ANISOU 1470 C SER A 207 2576 9357 9892 278 305 503 C ATOM 1471 O SER A 207 88.571 173.125 308.925 1.00 58.21 O ANISOU 1471 O SER A 207 2650 9371 10097 340 345 617 O ATOM 1472 CB SER A 207 90.314 173.444 306.412 1.00 77.78 C ANISOU 1472 CB SER A 207 5123 11966 12462 273 250 380 C ATOM 1473 OG SER A 207 90.368 173.457 304.994 1.00 77.53 O ANISOU 1473 OG SER A 207 5104 11947 12408 255 212 289 O ATOM 1474 N ARG A 208 89.549 175.130 309.230 1.00 57.18 N ANISOU 1474 N ARG A 208 2550 9403 9774 234 302 481 N ATOM 1475 CA ARG A 208 89.350 175.188 310.669 1.00 74.27 C ANISOU 1475 CA ARG A 208 4700 11581 11939 254 344 590 C ATOM 1476 C ARG A 208 88.113 175.997 311.044 1.00 75.53 C ANISOU 1476 C ARG A 208 4898 11705 12094 236 360 599 C ATOM 1477 O ARG A 208 87.690 175.960 312.204 1.00 79.74 O ANISOU 1477 O ARG A 208 5415 12238 12645 264 403 717 O ATOM 1478 CB ARG A 208 90.598 175.789 311.331 1.00 72.79 C ANISOU 1478 CB ARG A 208 4481 11497 11677 216 337 612 C ATOM 1479 CG ARG A 208 90.910 175.305 312.741 1.00 72.09 C ANISOU 1479 CG ARG A 208 4341 11461 11589 261 381 785 C ATOM 1480 CD ARG A 208 90.915 176.464 313.736 1.00 70.15 C ANISOU 1480 CD ARG A 208 4095 11300 11257 215 392 831 C ATOM 1481 NE ARG A 208 91.273 177.743 313.120 1.00 66.43 N ANISOU 1481 NE ARG A 208 3659 10857 10725 127 352 703 N ATOM 1482 CZ ARG A 208 90.397 178.692 312.793 1.00 63.69 C ANISOU 1482 CZ ARG A 208 3358 10468 10375 83 348 620 C ATOM 1483 NH1 ARG A 208 89.100 178.509 313.016 1.00 63.24 N ANISOU 1483 NH1 ARG A 208 3320 10345 10365 119 378 650 N ATOM 1484 NH2 ARG A 208 90.816 179.820 312.238 1.00 62.27 N ANISOU 1484 NH2 ARG A 208 3205 10304 10149 6 317 519 N ATOM 1485 N ARG A 209 87.532 176.726 310.088 1.00 71.88 N ANISOU 1485 N ARG A 209 4487 11221 11604 194 331 488 N ATOM 1486 CA ARG A 209 86.295 177.462 310.328 1.00 69.50 C ANISOU 1486 CA ARG A 209 4225 10875 11307 180 348 500 C ATOM 1487 C ARG A 209 85.085 176.560 310.137 1.00 56.05 C ANISOU 1487 C ARG A 209 2539 9052 9706 239 368 563 C ATOM 1488 O ARG A 209 84.123 176.625 310.912 1.00 56.28 O ANISOU 1488 O ARG A 209 2577 9024 9782 263 405 648 O ATOM 1489 CB ARG A 209 86.227 178.667 309.385 1.00 54.95 C ANISOU 1489 CB ARG A 209 2426 9061 9390 109 310 370 C ATOM 1490 CG ARG A 209 85.407 179.839 309.870 1.00 54.62 C ANISOU 1490 CG ARG A 209 2414 9013 9327 71 332 376 C ATOM 1491 CD ARG A 209 86.093 181.153 309.512 1.00 54.11 C ANISOU 1491 CD ARG A 209 2362 9015 9184 -12 309 271 C ATOM 1492 NE ARG A 209 86.908 181.662 310.613 1.00 67.85 N ANISOU 1492 NE ARG A 209 4064 10814 10901 -43 331 313 N ATOM 1493 CZ ARG A 209 86.588 182.720 311.353 1.00 68.48 C ANISOU 1493 CZ ARG A 209 4146 10915 10957 -85 362 337 C ATOM 1494 NH1 ARG A 209 85.474 183.394 311.098 1.00 67.21 N ANISOU 1494 NH1 ARG A 209 4024 10712 10799 -100 377 313 N ATOM 1495 NH2 ARG A 209 87.387 183.110 312.342 1.00 68.72 N ANISOU 1495 NH2 ARG A 209 4138 11019 10952 -113 381 397 N ATOM 1496 N LEU A 210 85.139 175.692 309.125 1.00 56.17 N ANISOU 1496 N LEU A 210 2548 9012 9781 263 347 547 N ATOM 1497 CA LEU A 210 84.008 174.833 308.794 1.00 66.82 C ANISOU 1497 CA LEU A 210 3906 10214 11267 310 366 613 C ATOM 1498 C LEU A 210 83.762 173.778 309.865 1.00 68.54 C ANISOU 1498 C LEU A 210 4086 10359 11596 377 421 755 C ATOM 1499 O LEU A 210 82.621 173.335 310.041 1.00 69.24 O ANISOU 1499 O LEU A 210 4188 10320 11799 410 451 824 O ATOM 1500 CB LEU A 210 84.243 174.171 307.436 1.00 66.31 C ANISOU 1500 CB LEU A 210 3834 10109 11252 313 334 559 C ATOM 1501 CG LEU A 210 83.898 174.920 306.144 1.00 55.67 C ANISOU 1501 CG LEU A 210 2529 8773 9850 265 287 454 C ATOM 1502 CD1 LEU A 210 84.430 176.341 306.124 1.00 54.82 C ANISOU 1502 CD1 LEU A 210 2450 8802 9579 201 259 366 C ATOM 1503 CD2 LEU A 210 84.445 174.149 304.959 1.00 55.93 C ANISOU 1503 CD2 LEU A 210 2537 8795 9919 274 260 411 C ATOM 1504 N ARG A 211 84.811 173.364 310.584 1.00 58.17 N ANISOU 1504 N ARG A 211 2724 9121 10256 397 437 808 N ATOM 1505 CA ARG A 211 84.641 172.393 311.664 1.00 82.33 C ANISOU 1505 CA ARG A 211 5745 12127 13411 464 494 962 C ATOM 1506 C ARG A 211 83.624 172.877 312.692 1.00 83.29 C ANISOU 1506 C ARG A 211 5889 12226 13531 475 531 1032 C ATOM 1507 O ARG A 211 82.845 172.082 313.232 1.00 87.09 O ANISOU 1507 O ARG A 211 6359 12599 14133 531 578 1152 O ATOM 1508 CB ARG A 211 85.985 172.109 312.335 1.00 59.91 C ANISOU 1508 CB ARG A 211 2850 9400 10512 478 503 1011 C ATOM 1509 N ALA A 212 83.617 174.181 312.976 1.00 78.90 N ANISOU 1509 N ALA A 212 5360 11763 12855 423 515 969 N ATOM 1510 CA ALA A 212 82.574 174.745 313.825 1.00 76.94 C ANISOU 1510 CA ALA A 212 5130 11485 12619 430 551 1039 C ATOM 1511 C ALA A 212 81.238 174.768 313.095 1.00 75.69 C ANISOU 1511 C ALA A 212 5026 11191 12542 430 546 1005 C ATOM 1512 O ALA A 212 80.211 174.348 313.641 1.00 74.24 O ANISOU 1512 O ALA A 212 4848 10904 12455 474 588 1103 O ATOM 1513 CB ALA A 212 82.965 176.151 314.272 1.00 58.17 C ANISOU 1513 CB ALA A 212 2756 9233 10112 369 543 992 C ATOM 1514 N ARG A 213 81.242 175.248 311.846 1.00 75.71 N ANISOU 1514 N ARG A 213 5066 11193 12508 383 496 874 N ATOM 1515 CA ARG A 213 80.019 175.367 311.060 1.00 74.76 C ANISOU 1515 CA ARG A 213 4994 10954 12459 377 486 844 C ATOM 1516 C ARG A 213 79.422 174.020 310.681 1.00 73.04 C ANISOU 1516 C ARG A 213 4759 10572 12422 428 504 914 C ATOM 1517 O ARG A 213 78.271 173.975 310.235 1.00 70.85 O ANISOU 1517 O ARG A 213 4512 10170 12238 431 506 916 O ATOM 1518 CB ARG A 213 80.285 176.170 309.788 1.00 55.69 C ANISOU 1518 CB ARG A 213 2612 8589 9960 317 429 708 C ATOM 1519 CG ARG A 213 80.476 177.642 310.026 1.00 55.04 C ANISOU 1519 CG ARG A 213 2552 8612 9749 258 421 649 C ATOM 1520 CD ARG A 213 80.791 178.368 308.741 1.00 54.21 C ANISOU 1520 CD ARG A 213 2476 8559 9561 203 368 524 C ATOM 1521 NE ARG A 213 81.068 179.774 308.999 1.00 83.23 N ANISOU 1521 NE ARG A 213 6164 12324 13135 142 368 477 N ATOM 1522 CZ ARG A 213 81.437 180.644 308.069 1.00 84.14 C ANISOU 1522 CZ ARG A 213 6302 12501 13165 86 330 377 C ATOM 1523 NH1 ARG A 213 81.575 180.250 306.810 1.00 81.60 N ANISOU 1523 NH1 ARG A 213 5994 12176 12833 86 288 318 N ATOM 1524 NH2 ARG A 213 81.671 181.908 308.401 1.00 87.31 N ANISOU 1524 NH2 ARG A 213 6709 12969 13494 29 340 342 N ATOM 1525 N GLY A 900 80.171 172.932 310.825 1.00 58.19 N ANISOU 1525 N GLY A 900 2827 8681 10601 465 519 968 N ATOM 1526 CA GLY A 900 79.663 171.628 310.452 1.00 59.00 C ANISOU 1526 CA GLY A 900 2906 8619 10892 508 542 1027 C ATOM 1527 C GLY A 900 79.553 171.459 308.950 1.00 79.44 C ANISOU 1527 C GLY A 900 5508 11147 13527 479 497 918 C ATOM 1528 O GLY A 900 79.244 172.415 308.232 1.00 77.28 O ANISOU 1528 O GLY A 900 5279 10911 13173 433 456 822 O ATOM 1529 N SER A 901 79.802 170.250 308.460 1.00 82.04 N ANISOU 1529 N SER A 901 5797 11385 13989 507 508 932 N ATOM 1530 CA SER A 901 79.780 170.015 307.024 1.00 81.81 C ANISOU 1530 CA SER A 901 5771 11308 14004 481 467 824 C ATOM 1531 C SER A 901 78.353 170.092 306.490 1.00 82.27 C ANISOU 1531 C SER A 901 5864 11225 14171 468 462 799 C ATOM 1532 O SER A 901 77.383 169.789 307.192 1.00 79.67 O ANISOU 1532 O SER A 901 5538 10781 13953 495 504 884 O ATOM 1533 CB SER A 901 80.401 168.656 306.694 1.00 84.82 C ANISOU 1533 CB SER A 901 6094 11618 14514 514 488 845 C ATOM 1534 OG SER A 901 80.599 168.498 305.299 1.00 84.17 O ANISOU 1534 OG SER A 901 6009 11524 14447 487 444 729 O ATOM 1535 N GLY A 902 78.235 170.506 305.228 1.00 81.87 N ANISOU 1535 N GLY A 902 5834 11189 14084 428 410 683 N ATOM 1536 CA GLY A 902 76.947 170.705 304.601 1.00 84.48 C ANISOU 1536 CA GLY A 902 6195 11409 14496 410 397 643 C ATOM 1537 C GLY A 902 76.166 171.799 305.315 1.00 85.40 C ANISOU 1537 C GLY A 902 6360 11552 14536 399 405 680 C ATOM 1538 O GLY A 902 76.702 172.599 306.086 1.00 90.32 O ANISOU 1538 O GLY A 902 7000 12302 15016 393 410 706 O ATOM 1539 N SER A 903 74.867 171.823 305.036 1.00 80.62 N ANISOU 1539 N SER A 903 5775 10822 14034 396 408 678 N ATOM 1540 CA SER A 903 73.945 172.689 305.754 1.00 72.38 C ANISOU 1540 CA SER A 903 4774 9769 12957 394 428 728 C ATOM 1541 C SER A 903 73.340 172.002 306.976 1.00 73.02 C ANISOU 1541 C SER A 903 4840 9740 13164 440 492 858 C ATOM 1542 O SER A 903 72.401 172.541 307.573 1.00 71.18 O ANISOU 1542 O SER A 903 4638 9470 12939 446 515 910 O ATOM 1543 CB SER A 903 72.832 173.165 304.816 1.00 68.46 C ANISOU 1543 CB SER A 903 4307 9206 12497 366 398 662 C ATOM 1544 OG SER A 903 72.644 174.566 304.908 1.00 64.64 O ANISOU 1544 OG SER A 903 3873 8821 11866 338 383 642 O ATOM 1545 N ASN A1002 73.875 170.838 307.366 1.00 72.42 N ANISOU 1545 N ASN A1002 4714 9615 13186 476 525 920 N ATOM 1546 CA ASN A1002 73.226 169.997 308.370 1.00 75.67 C ANISOU 1546 CA ASN A1002 5104 9897 13751 523 590 1051 C ATOM 1547 C ASN A1002 72.981 170.736 309.680 1.00 77.53 C ANISOU 1547 C ASN A1002 5363 10200 13893 542 625 1148 C ATOM 1548 O ASN A1002 71.977 170.480 310.355 1.00 83.16 O ANISOU 1548 O ASN A1002 6080 10803 14714 569 671 1242 O ATOM 1549 CB ASN A1002 74.063 168.743 308.631 1.00 75.87 C ANISOU 1549 CB ASN A1002 5070 9888 13871 559 623 1109 C ATOM 1550 CG ASN A1002 74.153 167.833 307.418 1.00 79.10 C ANISOU 1550 CG ASN A1002 5445 10196 14412 546 601 1022 C ATOM 1551 OD1 ASN A1002 74.122 168.293 306.273 1.00 81.57 O ANISOU 1551 OD1 ASN A1002 5777 10540 14674 505 545 895 O ATOM 1552 ND2 ASN A1002 74.263 166.532 307.664 1.00 79.35 N ANISOU 1552 ND2 ASN A1002 5424 10105 14619 581 650 1090 N ATOM 1553 N ILE A1003 73.877 171.647 310.064 1.00 74.83 N ANISOU 1553 N ILE A1003 5035 10039 13357 527 607 1123 N ATOM 1554 CA ILE A1003 73.703 172.324 311.344 1.00 72.49 C ANISOU 1554 CA ILE A1003 4754 9816 12973 544 644 1206 C ATOM 1555 C ILE A1003 72.574 173.342 311.260 1.00 70.00 C ANISOU 1555 C ILE A1003 4491 9472 12632 520 639 1180 C ATOM 1556 O ILE A1003 71.921 173.637 312.269 1.00 58.22 O ANISOU 1556 O ILE A1003 3013 7967 11142 544 683 1267 O ATOM 1557 CB ILE A1003 75.029 172.969 311.790 1.00 74.15 C ANISOU 1557 CB ILE A1003 4953 10228 12994 529 628 1175 C ATOM 1558 CG1 ILE A1003 75.051 173.175 313.307 1.00 58.81 C ANISOU 1558 CG1 ILE A1003 2997 8353 10995 563 680 1287 C ATOM 1559 CG2 ILE A1003 75.271 174.282 311.055 1.00 74.73 C ANISOU 1559 CG2 ILE A1003 5068 10412 12913 467 574 1043 C ATOM 1560 CD1 ILE A1003 74.521 174.514 313.770 1.00 58.10 C ANISOU 1560 CD1 ILE A1003 2947 8330 10797 537 684 1265 C ATOM 1561 N PHE A1004 72.305 173.871 310.063 1.00 57.39 N ANISOU 1561 N PHE A1004 2925 7865 11015 476 589 1067 N ATOM 1562 CA PHE A1004 71.310 174.929 309.912 1.00 56.69 C ANISOU 1562 CA PHE A1004 2887 7762 10892 453 583 1040 C ATOM 1563 C PHE A1004 69.899 174.387 310.096 1.00 57.25 C ANISOU 1563 C PHE A1004 2962 7653 11136 480 618 1115 C ATOM 1564 O PHE A1004 69.148 174.857 310.959 1.00 83.19 O ANISOU 1564 O PHE A1004 6269 10920 14419 498 658 1189 O ATOM 1565 CB PHE A1004 71.458 175.593 308.542 1.00 55.92 C ANISOU 1565 CB PHE A1004 2814 7709 10725 402 521 908 C ATOM 1566 CG PHE A1004 70.454 176.686 308.278 1.00 75.00 C ANISOU 1566 CG PHE A1004 5278 10108 13110 378 515 882 C ATOM 1567 CD1 PHE A1004 70.016 177.515 309.297 1.00 72.78 C ANISOU 1567 CD1 PHE A1004 5024 9859 12770 385 555 939 C ATOM 1568 CD2 PHE A1004 69.945 176.881 307.003 1.00 76.57 C ANISOU 1568 CD2 PHE A1004 5491 10263 13338 350 472 802 C ATOM 1569 CE1 PHE A1004 69.095 178.519 309.046 1.00 54.44 C ANISOU 1569 CE1 PHE A1004 2744 7516 10426 366 555 919 C ATOM 1570 CE2 PHE A1004 69.021 177.883 306.750 1.00 75.64 C ANISOU 1570 CE2 PHE A1004 5414 10131 13194 331 470 786 C ATOM 1571 CZ PHE A1004 68.596 178.701 307.775 1.00 74.21 C ANISOU 1571 CZ PHE A1004 5262 9972 12962 340 513 847 C ATOM 1572 N GLU A1005 69.515 173.401 309.281 1.00 57.81 N ANISOU 1572 N GLU A1005 3009 7591 11364 482 606 1094 N ATOM 1573 CA GLU A1005 68.160 172.864 309.364 1.00 58.40 C ANISOU 1573 CA GLU A1005 3082 7489 11617 500 636 1154 C ATOM 1574 C GLU A1005 67.857 172.334 310.758 1.00 68.68 C ANISOU 1574 C GLU A1005 4367 8737 12991 551 707 1306 C ATOM 1575 O GLU A1005 66.723 172.451 311.237 1.00 69.42 O ANISOU 1575 O GLU A1005 4477 8738 13160 566 743 1377 O ATOM 1576 CB GLU A1005 67.973 171.767 308.323 1.00 83.47 C ANISOU 1576 CB GLU A1005 6219 10538 14956 492 615 1097 C ATOM 1577 CG GLU A1005 68.521 172.145 306.972 1.00 83.88 C ANISOU 1577 CG GLU A1005 6277 10670 14925 448 546 951 C ATOM 1578 CD GLU A1005 67.461 172.110 305.902 1.00 87.41 C ANISOU 1578 CD GLU A1005 6726 11017 15470 423 515 878 C ATOM 1579 OE1 GLU A1005 66.716 171.108 305.842 1.00 89.72 O ANISOU 1579 OE1 GLU A1005 6984 11149 15955 436 538 904 O ATOM 1580 OE2 GLU A1005 67.366 173.088 305.131 1.00 87.47 O ANISOU 1580 OE2 GLU A1005 6763 11107 15365 390 470 795 O ATOM 1581 N MET A1006 68.859 171.752 311.424 1.00 59.65 N ANISOU 1581 N MET A1006 3189 7654 11823 579 731 1364 N ATOM 1582 CA MET A1006 68.694 171.338 312.815 1.00 60.41 C ANISOU 1582 CA MET A1006 3265 7730 11957 631 800 1518 C ATOM 1583 C MET A1006 68.275 172.512 313.679 1.00 59.82 C ANISOU 1583 C MET A1006 3230 7744 11753 635 820 1555 C ATOM 1584 O MET A1006 67.359 172.402 314.500 1.00 60.28 O ANISOU 1584 O MET A1006 3293 7726 11884 668 873 1665 O ATOM 1585 CB MET A1006 69.991 170.734 313.355 1.00 90.67 C ANISOU 1585 CB MET A1006 7052 11655 15742 658 815 1565 C ATOM 1586 CG MET A1006 70.236 170.997 314.853 1.00 90.80 C ANISOU 1586 CG MET A1006 7060 11775 15666 701 867 1688 C ATOM 1587 SD MET A1006 71.774 170.276 315.480 1.00 90.41 S ANISOU 1587 SD MET A1006 6949 11844 15558 735 884 1750 S ATOM 1588 CE MET A1006 71.912 171.016 317.094 1.00 62.09 C ANISOU 1588 CE MET A1006 3361 8414 11816 769 928 1854 C ATOM 1589 N LEU A1007 68.940 173.651 313.506 1.00 58.84 N ANISOU 1589 N LEU A1007 3134 7782 11442 601 782 1462 N ATOM 1590 CA LEU A1007 68.612 174.813 314.317 1.00 70.87 C ANISOU 1590 CA LEU A1007 4689 9393 12847 600 805 1485 C ATOM 1591 C LEU A1007 67.294 175.444 313.886 1.00 71.39 C ANISOU 1591 C LEU A1007 4799 9359 12966 583 804 1466 C ATOM 1592 O LEU A1007 66.596 176.039 314.716 1.00 72.96 O ANISOU 1592 O LEU A1007 5012 9547 13161 602 851 1545 O ATOM 1593 CB LEU A1007 69.752 175.829 314.258 1.00 69.07 C ANISOU 1593 CB LEU A1007 4460 9345 12437 562 774 1403 C ATOM 1594 CG LEU A1007 70.612 175.897 315.519 1.00 68.38 C ANISOU 1594 CG LEU A1007 4333 9387 12263 588 812 1485 C ATOM 1595 CD1 LEU A1007 69.818 176.523 316.648 1.00 58.57 C ANISOU 1595 CD1 LEU A1007 3096 8144 11014 615 874 1588 C ATOM 1596 CD2 LEU A1007 71.095 174.511 315.916 1.00 59.20 C ANISOU 1596 CD2 LEU A1007 3123 8193 11177 635 833 1569 C ATOM 1597 N ARG A1008 66.928 175.319 312.607 1.00 69.22 N ANISOU 1597 N ARG A1008 4538 9006 12756 551 757 1376 N ATOM 1598 CA ARG A1008 65.667 175.896 312.148 1.00 67.20 C ANISOU 1598 CA ARG A1008 4320 8660 12552 535 754 1359 C ATOM 1599 C ARG A1008 64.484 175.272 312.873 1.00 67.38 C ANISOU 1599 C ARG A1008 4336 8534 12732 577 812 1486 C ATOM 1600 O ARG A1008 63.621 175.980 313.403 1.00 66.75 O ANISOU 1600 O ARG A1008 4287 8439 12637 587 845 1534 O ATOM 1601 CB ARG A1008 65.515 175.721 310.638 1.00 57.03 C ANISOU 1601 CB ARG A1008 3032 7317 11320 497 694 1247 C ATOM 1602 CG ARG A1008 64.065 175.791 310.194 1.00 57.14 C ANISOU 1602 CG ARG A1008 3063 7194 11455 494 698 1257 C ATOM 1603 CD ARG A1008 63.833 175.015 308.922 1.00 79.11 C ANISOU 1603 CD ARG A1008 5818 9884 14357 472 653 1178 C ATOM 1604 NE ARG A1008 64.218 175.782 307.744 1.00 77.51 N ANISOU 1604 NE ARG A1008 5632 9776 14043 428 590 1050 N ATOM 1605 CZ ARG A1008 64.069 175.355 306.494 1.00 77.96 C ANISOU 1605 CZ ARG A1008 5666 9791 14165 404 542 958 C ATOM 1606 NH1 ARG A1008 63.544 174.160 306.259 1.00 80.70 N ANISOU 1606 NH1 ARG A1008 5971 9996 14696 414 549 970 N ATOM 1607 NH2 ARG A1008 64.445 176.123 305.479 1.00 75.37 N ANISOU 1607 NH2 ARG A1008 5353 9566 13720 368 489 854 N ATOM 1608 N ILE A1009 64.437 173.936 312.907 1.00 67.68 N ANISOU 1608 N ILE A1009 4330 8457 12927 601 830 1544 N ATOM 1609 CA ILE A1009 63.409 173.194 313.637 1.00 59.96 C ANISOU 1609 CA ILE A1009 3337 7332 12113 640 891 1678 C ATOM 1610 C ILE A1009 63.275 173.697 315.069 1.00 78.16 C ANISOU 1610 C ILE A1009 5655 9707 14334 681 952 1795 C ATOM 1611 O ILE A1009 62.180 173.691 315.645 1.00 78.89 O ANISOU 1611 O ILE A1009 5757 9707 14509 706 999 1890 O ATOM 1612 CB ILE A1009 63.735 171.683 313.604 1.00 61.07 C ANISOU 1612 CB ILE A1009 3420 7368 12415 660 909 1727 C ATOM 1613 CG1 ILE A1009 63.611 171.112 312.192 1.00 61.16 C ANISOU 1613 CG1 ILE A1009 3413 7283 12541 621 857 1610 C ATOM 1614 CG2 ILE A1009 62.843 170.899 314.549 1.00 62.15 C ANISOU 1614 CG2 ILE A1009 3535 7368 12711 705 984 1887 C ATOM 1615 CD1 ILE A1009 63.811 169.600 312.130 1.00 62.36 C ANISOU 1615 CD1 ILE A1009 3506 7308 12881 639 883 1654 C ATOM 1616 N ASP A1010 64.373 174.169 315.654 1.00 77.96 N ANISOU 1616 N ASP A1010 5626 9853 14142 688 950 1784 N ATOM 1617 CA ASP A1010 64.470 174.380 317.092 1.00 79.15 C ANISOU 1617 CA ASP A1010 5762 10074 14238 734 1015 1914 C ATOM 1618 C ASP A1010 64.242 175.833 317.502 1.00 79.62 C ANISOU 1618 C ASP A1010 5851 10224 14176 722 1029 1904 C ATOM 1619 O ASP A1010 63.325 176.126 318.276 1.00 60.05 O ANISOU 1619 O ASP A1010 3384 7700 11733 753 1086 2004 O ATOM 1620 CB ASP A1010 65.843 173.872 317.545 1.00 60.67 C ANISOU 1620 CB ASP A1010 3376 7853 11823 751 1014 1933 C ATOM 1621 CG ASP A1010 65.967 172.376 317.398 1.00 61.56 C ANISOU 1621 CG ASP A1010 3449 7855 12086 776 1026 1988 C ATOM 1622 OD1 ASP A1010 65.334 171.841 316.467 1.00 76.40 O ANISOU 1622 OD1 ASP A1010 5330 9580 14117 755 1007 1951 O ATOM 1623 OD2 ASP A1010 66.673 171.738 318.205 1.00 62.34 O ANISOU 1623 OD2 ASP A1010 3505 8009 12173 817 1061 2082 O ATOM 1624 N GLU A1011 65.072 176.748 317.009 1.00 78.56 N ANISOU 1624 N GLU A1011 5728 10217 13903 678 985 1788 N ATOM 1625 CA GLU A1011 64.954 178.156 317.360 1.00 76.98 C ANISOU 1625 CA GLU A1011 5550 10104 13593 660 1004 1770 C ATOM 1626 C GLU A1011 63.969 178.902 316.474 1.00 57.76 C ANISOU 1626 C GLU A1011 3166 7583 11198 627 984 1705 C ATOM 1627 O GLU A1011 63.717 180.087 316.714 1.00 57.44 O ANISOU 1627 O GLU A1011 3146 7589 11088 613 1008 1697 O ATOM 1628 CB GLU A1011 66.325 178.842 317.290 1.00 78.20 C ANISOU 1628 CB GLU A1011 5688 10437 13587 622 973 1681 C ATOM 1629 CG GLU A1011 67.313 178.438 318.384 1.00 80.58 C ANISOU 1629 CG GLU A1011 5936 10863 13817 654 1003 1755 C ATOM 1630 CD GLU A1011 67.320 179.391 319.578 1.00 84.47 C ANISOU 1630 CD GLU A1011 6412 11471 14212 668 1064 1817 C ATOM 1631 OE1 GLU A1011 67.160 180.615 319.374 1.00 85.96 O ANISOU 1631 OE1 GLU A1011 6625 11699 14335 627 1066 1749 O ATOM 1632 OE2 GLU A1011 67.495 178.914 320.723 1.00 86.94 O ANISOU 1632 OE2 GLU A1011 6683 11836 14513 720 1113 1936 O ATOM 1633 N GLY A1012 63.411 178.246 315.462 1.00 57.63 N ANISOU 1633 N GLY A1012 3163 7444 11290 614 944 1661 N ATOM 1634 CA GLY A1012 62.450 178.895 314.598 1.00 57.09 C ANISOU 1634 CA GLY A1012 3134 7299 11258 586 923 1606 C ATOM 1635 C GLY A1012 63.094 179.791 313.565 1.00 56.20 C ANISOU 1635 C GLY A1012 3040 7278 11034 530 865 1469 C ATOM 1636 O GLY A1012 63.918 180.653 313.887 1.00 55.89 O ANISOU 1636 O GLY A1012 2999 7368 10868 512 871 1439 O ATOM 1637 N LEU A1013 62.713 179.590 312.313 1.00 55.86 N ANISOU 1637 N LEU A1013 3010 7173 11041 503 812 1386 N ATOM 1638 CA LEU A1013 63.235 180.351 311.188 1.00 69.43 C ANISOU 1638 CA LEU A1013 4746 8972 12664 453 754 1260 C ATOM 1639 C LEU A1013 62.215 181.416 310.795 1.00 71.97 C ANISOU 1639 C LEU A1013 5103 9250 12994 439 764 1255 C ATOM 1640 O LEU A1013 61.156 181.095 310.244 1.00 74.07 O ANISOU 1640 O LEU A1013 5375 9406 13361 444 754 1261 O ATOM 1641 CB LEU A1013 63.531 179.417 310.018 1.00 67.53 C ANISOU 1641 CB LEU A1013 4488 8709 12461 436 690 1171 C ATOM 1642 CG LEU A1013 63.820 180.072 308.669 1.00 65.48 C ANISOU 1642 CG LEU A1013 4243 8514 12121 389 628 1047 C ATOM 1643 CD1 LEU A1013 65.214 180.690 308.646 1.00 53.90 C ANISOU 1643 CD1 LEU A1013 2774 7202 10502 360 608 987 C ATOM 1644 CD2 LEU A1013 63.641 179.063 307.544 1.00 65.58 C ANISOU 1644 CD2 LEU A1013 4226 8453 12237 381 579 990 C ATOM 1645 N ARG A1014 62.531 182.678 311.076 1.00 71.09 N ANISOU 1645 N ARG A1014 5009 9222 12780 420 787 1245 N ATOM 1646 CA ARG A1014 61.718 183.810 310.649 1.00 53.98 C ANISOU 1646 CA ARG A1014 2874 7025 10612 405 800 1237 C ATOM 1647 C ARG A1014 62.571 184.755 309.815 1.00 82.33 C ANISOU 1647 C ARG A1014 6473 10726 14084 354 761 1133 C ATOM 1648 O ARG A1014 63.726 185.022 310.158 1.00 82.40 O ANISOU 1648 O ARG A1014 6468 10847 13992 334 761 1101 O ATOM 1649 CB ARG A1014 61.127 184.554 311.849 1.00 54.28 C ANISOU 1649 CB ARG A1014 2924 7039 10660 432 885 1339 C ATOM 1650 N LEU A1015 62.005 185.265 308.718 1.00 53.00 N ANISOU 1650 N LEU A1015 2776 6983 10378 334 731 1084 N ATOM 1651 CA LEU A1015 62.750 186.100 307.780 1.00 52.44 C ANISOU 1651 CA LEU A1015 2711 7011 10202 287 692 989 C ATOM 1652 C LEU A1015 62.397 187.581 307.892 1.00 52.25 C ANISOU 1652 C LEU A1015 2711 6992 10149 272 741 1010 C ATOM 1653 O LEU A1015 62.685 188.353 306.971 1.00 51.86 O ANISOU 1653 O LEU A1015 2669 6996 10039 237 715 946 O ATOM 1654 CB LEU A1015 62.526 185.623 306.346 1.00 52.28 C ANISOU 1654 CB LEU A1015 2684 6982 10197 274 620 911 C ATOM 1655 CG LEU A1015 62.667 184.123 306.101 1.00 52.60 C ANISOU 1655 CG LEU A1015 2698 6993 10295 290 578 889 C ATOM 1656 CD1 LEU A1015 62.588 183.809 304.612 1.00 62.13 C ANISOU 1656 CD1 LEU A1015 3890 8222 11493 270 508 796 C ATOM 1657 CD2 LEU A1015 63.957 183.605 306.689 1.00 52.63 C ANISOU 1657 CD2 LEU A1015 2683 7075 10238 287 574 877 C ATOM 1658 N LYS A1016 61.778 187.994 308.996 1.00 52.58 N ANISOU 1658 N LYS A1016 2764 6980 10235 298 819 1102 N ATOM 1659 CA LYS A1016 61.440 189.391 309.219 1.00 52.53 C ANISOU 1659 CA LYS A1016 2778 6969 10212 287 882 1129 C ATOM 1660 C LYS A1016 61.753 189.752 310.660 1.00 68.48 C ANISOU 1660 C LYS A1016 4789 9022 12207 297 961 1189 C ATOM 1661 O LYS A1016 61.781 188.887 311.539 1.00 69.99 O ANISOU 1661 O LYS A1016 4964 9205 12423 331 974 1241 O ATOM 1662 CB LYS A1016 59.965 189.684 308.921 1.00 52.69 C ANISOU 1662 CB LYS A1016 2820 6869 10331 315 908 1190 C ATOM 1663 N ILE A1017 61.988 191.044 310.892 1.00 66.95 N ANISOU 1663 N ILE A1017 4604 8869 11965 268 1019 1180 N ATOM 1664 CA ILE A1017 62.315 191.513 312.232 1.00 65.54 C ANISOU 1664 CA ILE A1017 4412 8741 11751 271 1102 1223 C ATOM 1665 C ILE A1017 61.139 191.237 313.159 1.00 53.86 C ANISOU 1665 C ILE A1017 2941 7161 10362 333 1168 1337 C ATOM 1666 O ILE A1017 59.983 191.505 312.814 1.00 70.76 O ANISOU 1666 O ILE A1017 5110 9190 12585 358 1189 1384 O ATOM 1667 CB ILE A1017 62.666 193.008 312.201 1.00 63.22 C ANISOU 1667 CB ILE A1017 4125 8492 11404 222 1163 1186 C ATOM 1668 CG1 ILE A1017 64.005 193.256 311.489 1.00 61.07 C ANISOU 1668 CG1 ILE A1017 3836 8337 11030 156 1105 1079 C ATOM 1669 CG2 ILE A1017 62.711 193.563 313.605 1.00 53.92 C ANISOU 1669 CG2 ILE A1017 2932 7350 10205 228 1269 1235 C ATOM 1670 CD1 ILE A1017 63.926 193.338 309.971 1.00 52.31 C ANISOU 1670 CD1 ILE A1017 2746 7203 9925 137 1031 1023 C ATOM 1671 N TYR A1018 61.418 190.686 314.338 1.00 54.35 N ANISOU 1671 N TYR A1018 2976 7267 10408 362 1202 1389 N ATOM 1672 CA TYR A1018 60.366 190.439 315.325 1.00 81.28 C ANISOU 1672 CA TYR A1018 6392 10596 13895 424 1272 1505 C ATOM 1673 C TYR A1018 60.906 190.789 316.711 1.00 81.71 C ANISOU 1673 C TYR A1018 6414 10754 13877 432 1354 1539 C ATOM 1674 O TYR A1018 61.968 191.408 316.849 1.00 81.60 O ANISOU 1674 O TYR A1018 6376 10865 13762 381 1364 1468 O ATOM 1675 CB TYR A1018 59.842 188.998 315.228 1.00 81.07 C ANISOU 1675 CB TYR A1018 6362 10488 13954 468 1221 1557 C ATOM 1676 CG TYR A1018 60.852 187.901 315.526 1.00 80.42 C ANISOU 1676 CG TYR A1018 6242 10487 13828 470 1173 1540 C ATOM 1677 CD1 TYR A1018 61.565 187.284 314.501 1.00 79.34 C ANISOU 1677 CD1 TYR A1018 6099 10378 13670 437 1081 1450 C ATOM 1678 CD2 TYR A1018 61.064 187.461 316.827 1.00 55.87 C ANISOU 1678 CD2 TYR A1018 3101 7427 10701 510 1224 1620 C ATOM 1679 CE1 TYR A1018 62.474 186.278 314.769 1.00 54.89 C ANISOU 1679 CE1 TYR A1018 2968 7347 10541 444 1045 1440 C ATOM 1680 CE2 TYR A1018 61.967 186.459 317.102 1.00 56.07 C ANISOU 1680 CE2 TYR A1018 3089 7524 10691 517 1185 1616 C ATOM 1681 CZ TYR A1018 62.669 185.871 316.073 1.00 55.57 C ANISOU 1681 CZ TYR A1018 3023 7477 10615 483 1097 1526 C ATOM 1682 OH TYR A1018 63.569 184.871 316.358 1.00 55.83 O ANISOU 1682 OH TYR A1018 3019 7575 10620 494 1066 1527 O ATOM 1683 N LYS A1019 60.160 190.429 317.754 1.00 56.22 N ANISOU 1683 N LYS A1019 3181 7483 10697 494 1417 1649 N ATOM 1684 CA LYS A1019 60.594 190.658 319.124 1.00 56.96 C ANISOU 1684 CA LYS A1019 3237 7688 10717 511 1498 1690 C ATOM 1685 C LYS A1019 60.918 189.322 319.782 1.00 76.46 C ANISOU 1685 C LYS A1019 5670 10197 13186 556 1467 1753 C ATOM 1686 O LYS A1019 60.144 188.365 319.677 1.00 57.46 O ANISOU 1686 O LYS A1019 3277 7677 10878 602 1442 1825 O ATOM 1687 CB LYS A1019 59.538 191.422 319.922 1.00 72.87 C ANISOU 1687 CB LYS A1019 5273 9643 12772 552 1613 1772 C ATOM 1688 CG LYS A1019 59.487 192.915 319.601 1.00 71.93 C ANISOU 1688 CG LYS A1019 5179 9522 12629 504 1677 1709 C ATOM 1689 CD LYS A1019 58.863 193.701 320.754 1.00 71.97 C ANISOU 1689 CD LYS A1019 5188 9528 12629 540 1816 1774 C ATOM 1690 CE LYS A1019 58.957 195.205 320.544 1.00 70.53 C ANISOU 1690 CE LYS A1019 5029 9350 12419 485 1900 1703 C ATOM 1691 NZ LYS A1019 60.365 195.684 320.555 1.00 69.22 N ANISOU 1691 NZ LYS A1019 4825 9342 12135 403 1895 1590 N ATOM 1692 N ASP A1020 62.066 189.262 320.451 1.00 77.08 N ANISOU 1692 N ASP A1020 5698 10436 13154 539 1473 1727 N ATOM 1693 CA ASP A1020 62.561 188.019 321.024 1.00 78.15 C ANISOU 1693 CA ASP A1020 5792 10625 13278 578 1443 1783 C ATOM 1694 C ASP A1020 61.685 187.581 322.196 1.00 79.06 C ANISOU 1694 C ASP A1020 5898 10702 13441 659 1518 1928 C ATOM 1695 O ASP A1020 60.703 188.236 322.561 1.00 77.98 O ANISOU 1695 O ASP A1020 5787 10499 13342 685 1593 1979 O ATOM 1696 CB ASP A1020 64.016 188.183 321.463 1.00 58.40 C ANISOU 1696 CB ASP A1020 3233 8318 10637 537 1435 1722 C ATOM 1697 N THR A1021 62.057 186.445 322.795 1.00 80.24 N ANISOU 1697 N THR A1021 6009 10892 13587 703 1502 2000 N ATOM 1698 CA THR A1021 61.321 185.938 323.948 1.00 80.59 C ANISOU 1698 CA THR A1021 6038 10913 13669 783 1572 2149 C ATOM 1699 C THR A1021 61.327 186.947 325.091 1.00 79.86 C ANISOU 1699 C THR A1021 5920 10948 13476 799 1676 2177 C ATOM 1700 O THR A1021 60.311 187.128 325.774 1.00 61.82 O ANISOU 1700 O THR A1021 3650 8605 11234 854 1754 2274 O ATOM 1701 CB THR A1021 61.914 184.604 324.402 1.00 61.09 C ANISOU 1701 CB THR A1021 3524 8486 11200 823 1541 2220 C ATOM 1702 N GLU A1022 62.457 187.627 325.296 1.00 76.93 N ANISOU 1702 N GLU A1022 5135 11518 12577 1523 402 117 N ATOM 1703 CA GLU A1022 62.605 188.655 326.317 1.00 77.29 C ANISOU 1703 CA GLU A1022 5145 11500 12721 1617 410 94 C ATOM 1704 C GLU A1022 62.209 190.044 325.819 1.00 62.04 C ANISOU 1704 C GLU A1022 3189 9491 10893 1701 437 117 C ATOM 1705 O GLU A1022 62.558 191.045 326.457 1.00 64.78 O ANISOU 1705 O GLU A1022 3517 9731 11364 1774 441 101 O ATOM 1706 CB GLU A1022 64.046 188.676 326.835 1.00 60.80 C ANISOU 1706 CB GLU A1022 3091 9277 10735 1584 377 95 C ATOM 1707 N GLY A1023 61.499 190.127 324.696 1.00 61.95 N ANISOU 1707 N GLY A1023 3176 9518 10845 1691 454 152 N ATOM 1708 CA GLY A1023 61.078 191.405 324.156 1.00 73.33 C ANISOU 1708 CA GLY A1023 4593 10891 12378 1768 481 182 C ATOM 1709 C GLY A1023 62.222 192.245 323.626 1.00 74.38 C ANISOU 1709 C GLY A1023 4760 10840 12662 1762 469 231 C ATOM 1710 O GLY A1023 62.496 193.332 324.144 1.00 75.37 O ANISOU 1710 O GLY A1023 4865 10854 12918 1836 476 218 O ATOM 1711 N TYR A1024 62.895 191.749 322.590 1.00 77.01 N ANISOU 1711 N TYR A1024 5142 11132 12987 1673 453 285 N ATOM 1712 CA TYR A1024 64.022 192.449 321.991 1.00 80.67 C ANISOU 1712 CA TYR A1024 5637 11423 13591 1655 442 336 C ATOM 1713 C TYR A1024 64.079 192.104 320.509 1.00 89.83 C ANISOU 1713 C TYR A1024 6832 12586 14712 1591 446 408 C ATOM 1714 O TYR A1024 63.567 191.070 320.075 1.00 93.51 O ANISOU 1714 O TYR A1024 7313 13171 15047 1538 446 409 O ATOM 1715 CB TYR A1024 65.342 192.095 322.685 1.00 77.62 C ANISOU 1715 CB TYR A1024 5281 10942 13268 1605 405 312 C ATOM 1716 N TYR A1025 64.719 192.980 319.735 1.00 90.89 N ANISOU 1716 N TYR A1025 6980 12583 14971 1596 451 468 N ATOM 1717 CA TYR A1025 64.729 192.862 318.280 1.00 89.70 C ANISOU 1717 CA TYR A1025 6857 12426 14800 1553 462 546 C ATOM 1718 C TYR A1025 65.674 191.755 317.825 1.00 85.17 C ANISOU 1718 C TYR A1025 6342 11843 14176 1455 439 567 C ATOM 1719 O TYR A1025 66.870 191.780 318.138 1.00 84.26 O ANISOU 1719 O TYR A1025 6252 11619 14143 1425 417 568 O ATOM 1720 CB TYR A1025 65.129 194.194 317.646 1.00 62.20 C ANISOU 1720 CB TYR A1025 3366 8796 11473 1593 476 607 C ATOM 1721 CG TYR A1025 63.989 195.176 317.567 1.00 77.40 C ANISOU 1721 CG TYR A1025 5238 10748 13421 1683 508 612 C ATOM 1722 CD1 TYR A1025 63.232 195.290 316.413 1.00 77.11 C ANISOU 1722 CD1 TYR A1025 5195 10764 13339 1686 532 672 C ATOM 1723 CD2 TYR A1025 63.656 195.976 318.649 1.00 79.66 C ANISOU 1723 CD2 TYR A1025 5482 11008 13776 1769 516 556 C ATOM 1724 CE1 TYR A1025 62.179 196.182 316.329 1.00 78.70 C ANISOU 1724 CE1 TYR A1025 5348 10991 13564 1769 562 681 C ATOM 1725 CE2 TYR A1025 62.602 196.869 318.577 1.00 80.96 C ANISOU 1725 CE2 TYR A1025 5601 11198 13961 1858 548 561 C ATOM 1726 CZ TYR A1025 61.868 196.970 317.412 1.00 80.33 C ANISOU 1726 CZ TYR A1025 5514 11172 13836 1856 571 625 C ATOM 1727 OH TYR A1025 60.819 197.855 317.324 1.00 81.25 O ANISOU 1727 OH TYR A1025 5584 11313 13976 1944 603 634 O ATOM 1728 N THR A1026 65.139 190.787 317.079 1.00 83.76 N ANISOU 1728 N THR A1026 6183 11772 13871 1406 444 583 N ATOM 1729 CA THR A1026 65.948 189.760 316.434 1.00 82.09 C ANISOU 1729 CA THR A1026 6029 11551 13612 1320 429 612 C ATOM 1730 C THR A1026 65.397 189.511 315.033 1.00 82.23 C ANISOU 1730 C THR A1026 6059 11611 13575 1297 448 674 C ATOM 1731 O THR A1026 64.321 189.996 314.667 1.00 58.70 O ANISOU 1731 O THR A1026 3040 8681 10582 1339 469 688 O ATOM 1732 CB THR A1026 65.978 188.443 317.232 1.00 81.40 C ANISOU 1732 CB THR A1026 5959 11557 13412 1269 407 548 C ATOM 1733 OG1 THR A1026 64.689 187.818 317.190 1.00 81.24 O ANISOU 1733 OG1 THR A1026 5916 11680 13273 1266 417 517 O ATOM 1734 CG2 THR A1026 66.384 188.677 318.683 1.00 57.90 C ANISOU 1734 CG2 THR A1026 2962 8553 10483 1298 389 487 C ATOM 1735 N ILE A1027 66.156 188.749 314.246 1.00 80.53 N ANISOU 1735 N ILE A1027 5889 11358 13352 1230 445 728 N ATOM 1736 CA ILE A1027 65.717 188.317 312.924 1.00 79.46 C ANISOU 1736 CA ILE A1027 5761 11250 13182 1200 466 806 C ATOM 1737 C ILE A1027 66.444 187.021 312.601 1.00 56.34 C ANISOU 1737 C ILE A1027 2883 8324 10199 1123 454 820 C ATOM 1738 O ILE A1027 67.561 186.788 313.068 1.00 55.93 O ANISOU 1738 O ILE A1027 2864 8206 10179 1098 437 803 O ATOM 1739 CB ILE A1027 65.980 189.407 311.855 1.00 57.91 C ANISOU 1739 CB ILE A1027 3025 8422 10558 1231 489 899 C ATOM 1740 CG1 ILE A1027 65.416 188.966 310.501 1.00 57.84 C ANISOU 1740 CG1 ILE A1027 3019 8456 10502 1206 511 982 C ATOM 1741 CG2 ILE A1027 67.461 189.727 311.780 1.00 57.76 C ANISOU 1741 CG2 ILE A1027 3041 8265 10641 1213 481 930 C ATOM 1742 CD1 ILE A1027 66.098 189.576 309.327 1.00 62.99 C ANISOU 1742 CD1 ILE A1027 3686 9007 11242 1209 531 1086 C ATOM 1743 N GLY A1028 65.801 186.166 311.806 1.00 56.03 N ANISOU 1743 N GLY A1028 2850 8359 10079 1086 464 853 N ATOM 1744 CA GLY A1028 66.415 184.893 311.505 1.00 55.17 C ANISOU 1744 CA GLY A1028 2789 8258 9914 1018 455 863 C ATOM 1745 C GLY A1028 66.372 183.953 312.697 1.00 65.52 C ANISOU 1745 C GLY A1028 4108 9638 11150 987 430 770 C ATOM 1746 O GLY A1028 65.480 184.018 313.548 1.00 64.21 O ANISOU 1746 O GLY A1028 3904 9551 10940 1009 425 703 O ATOM 1747 N ILE A1029 67.361 183.062 312.759 1.00 68.56 N ANISOU 1747 N ILE A1029 4539 9990 11519 936 417 770 N ATOM 1748 CA ILE A1029 67.473 182.104 313.855 1.00 53.34 C ANISOU 1748 CA ILE A1029 2624 8120 9524 901 394 690 C ATOM 1749 C ILE A1029 68.170 182.766 315.041 1.00 80.60 C ANISOU 1749 C ILE A1029 6070 11522 13034 932 375 638 C ATOM 1750 O ILE A1029 69.349 182.507 315.315 1.00 80.74 O ANISOU 1750 O ILE A1029 6122 11469 13086 906 360 640 O ATOM 1751 CB ILE A1029 68.202 180.827 313.393 1.00 52.53 C ANISOU 1751 CB ILE A1029 2574 8006 9379 835 389 714 C ATOM 1752 CG1 ILE A1029 67.519 180.270 312.146 1.00 52.45 C ANISOU 1752 CG1 ILE A1029 2569 8039 9319 810 408 772 C ATOM 1753 CG2 ILE A1029 68.212 179.765 314.489 1.00 51.98 C ANISOU 1753 CG2 ILE A1029 2515 8002 9233 796 367 635 C ATOM 1754 CD1 ILE A1029 67.580 178.770 312.033 1.00 51.71 C ANISOU 1754 CD1 ILE A1029 2510 7994 9142 746 400 759 C ATOM 1755 N GLY A1030 67.445 183.642 315.739 1.00 54.16 N ANISOU 1755 N GLY A1030 2674 8207 9697 989 376 592 N ATOM 1756 CA GLY A1030 67.904 184.239 316.976 1.00 60.20 C ANISOU 1756 CA GLY A1030 3426 8945 10502 1024 356 533 C ATOM 1757 C GLY A1030 69.000 185.279 316.861 1.00 54.73 C ANISOU 1757 C GLY A1030 2745 8111 9940 1048 352 571 C ATOM 1758 O GLY A1030 69.553 185.675 317.896 1.00 57.16 O ANISOU 1758 O GLY A1030 3039 8365 10314 1066 334 537 O ATOM 1759 N HIS A1031 69.336 185.736 315.654 1.00 54.91 N ANISOU 1759 N HIS A1031 2781 8051 10033 1047 371 655 N ATOM 1760 CA HIS A1031 70.357 186.769 315.503 1.00 71.75 C ANISOU 1760 CA HIS A1031 4919 10040 12302 1066 368 693 C ATOM 1761 C HIS A1031 69.860 188.062 316.136 1.00 72.75 C ANISOU 1761 C HIS A1031 4994 10138 12511 1139 372 668 C ATOM 1762 O HIS A1031 68.912 188.682 315.646 1.00 56.85 O ANISOU 1762 O HIS A1031 2949 8160 10492 1183 394 687 O ATOM 1763 CB HIS A1031 70.715 186.995 314.037 1.00 71.62 C ANISOU 1763 CB HIS A1031 4921 9950 12343 1053 393 797 C ATOM 1764 CG HIS A1031 71.803 188.011 313.829 1.00 72.54 C ANISOU 1764 CG HIS A1031 5041 9914 12605 1066 392 842 C ATOM 1765 ND1 HIS A1031 73.094 187.825 314.278 1.00 72.66 N ANISOU 1765 ND1 HIS A1031 5085 9840 12681 1032 368 835 N ATOM 1766 CD2 HIS A1031 71.789 189.223 313.224 1.00 56.60 C ANISOU 1766 CD2 HIS A1031 3000 7814 10690 1106 410 897 C ATOM 1767 CE1 HIS A1031 73.827 188.877 313.960 1.00 56.11 C ANISOU 1767 CE1 HIS A1031 2982 7614 10725 1048 371 883 C ATOM 1768 NE2 HIS A1031 73.059 189.740 313.320 1.00 56.75 N ANISOU 1768 NE2 HIS A1031 3033 7696 10832 1093 397 920 N ATOM 1769 N LEU A1032 70.507 188.468 317.226 1.00 73.19 N ANISOU 1769 N LEU A1032 5035 10119 12653 1152 349 629 N ATOM 1770 CA LEU A1032 70.177 189.708 317.918 1.00 74.34 C ANISOU 1770 CA LEU A1032 5130 10212 12905 1222 351 603 C ATOM 1771 C LEU A1032 70.734 190.888 317.133 1.00 58.41 C ANISOU 1771 C LEU A1032 3107 8048 11037 1243 363 672 C ATOM 1772 O LEU A1032 71.949 191.002 316.952 1.00 59.17 O ANISOU 1772 O LEU A1032 3228 8023 11231 1206 348 705 O ATOM 1773 CB LEU A1032 70.738 189.674 319.335 1.00 57.94 C ANISOU 1773 CB LEU A1032 3040 8095 10879 1224 320 536 C ATOM 1774 CG LEU A1032 70.880 190.995 320.090 1.00 59.10 C ANISOU 1774 CG LEU A1032 3142 8127 11187 1287 312 508 C ATOM 1775 CD1 LEU A1032 69.536 191.697 320.198 1.00 59.89 C ANISOU 1775 CD1 LEU A1032 3194 8299 11262 1368 341 490 C ATOM 1776 CD2 LEU A1032 71.480 190.751 321.468 1.00 59.19 C ANISOU 1776 CD2 LEU A1032 3144 8105 11239 1277 275 436 C ATOM 1777 N LEU A1033 69.846 191.760 316.655 1.00 65.04 N ANISOU 1777 N LEU A1033 3913 8900 11898 1301 390 697 N ATOM 1778 CA LEU A1033 70.286 192.906 315.867 1.00 59.81 C ANISOU 1778 CA LEU A1033 3243 8105 11378 1322 405 768 C ATOM 1779 C LEU A1033 70.933 193.971 316.744 1.00 74.08 C ANISOU 1779 C LEU A1033 5020 9764 13362 1355 387 739 C ATOM 1780 O LEU A1033 72.034 194.447 316.444 1.00 70.51 O ANISOU 1780 O LEU A1033 4578 9167 13045 1328 376 782 O ATOM 1781 CB LEU A1033 69.114 193.500 315.088 1.00 88.47 C ANISOU 1781 CB LEU A1033 6844 11794 14977 1374 440 805 C ATOM 1782 CG LEU A1033 68.545 192.608 313.996 1.00 59.57 C ANISOU 1782 CG LEU A1033 3211 8249 11175 1338 456 846 C ATOM 1783 CD1 LEU A1033 67.884 193.440 312.916 1.00 60.20 C ANISOU 1783 CD1 LEU A1033 3268 8321 11285 1378 488 917 C ATOM 1784 CD2 LEU A1033 69.658 191.767 313.409 1.00 77.19 C ANISOU 1784 CD2 LEU A1033 5497 10440 13391 1263 445 884 C ATOM 1785 N THR A1034 70.261 194.367 317.822 1.00 78.82 N ANISOU 1785 N THR A1034 5580 10395 13974 1414 383 667 N ATOM 1786 CA THR A1034 70.778 195.436 318.666 1.00 86.64 C ANISOU 1786 CA THR A1034 6538 11238 15145 1452 365 630 C ATOM 1787 C THR A1034 70.104 195.395 320.028 1.00 92.05 C ANISOU 1787 C THR A1034 7189 11989 15797 1505 356 533 C ATOM 1788 O THR A1034 68.961 194.943 320.162 1.00 91.97 O ANISOU 1788 O THR A1034 7167 12136 15643 1537 377 510 O ATOM 1789 CB THR A1034 70.543 196.810 318.037 1.00 89.11 C ANISOU 1789 CB THR A1034 6819 11448 15589 1508 390 682 C ATOM 1790 OG1 THR A1034 71.093 197.820 318.892 1.00 91.74 O ANISOU 1790 OG1 THR A1034 7120 11624 16112 1541 367 637 O ATOM 1791 CG2 THR A1034 69.053 197.053 317.881 1.00 87.83 C ANISOU 1791 CG2 THR A1034 6627 11413 15331 1580 427 677 C ATOM 1792 N LYS A1035 70.827 195.882 321.037 1.00 93.13 N ANISOU 1792 N LYS A1035 7308 12003 16075 1514 322 475 N ATOM 1793 CA LYS A1035 70.244 196.129 322.354 1.00 90.41 C ANISOU 1793 CA LYS A1035 6924 11686 15740 1581 315 380 C ATOM 1794 C LYS A1035 69.691 197.555 322.370 1.00 92.86 C ANISOU 1794 C LYS A1035 7191 11910 16180 1674 338 374 C ATOM 1795 O LYS A1035 70.247 198.470 322.978 1.00 96.87 O ANISOU 1795 O LYS A1035 7677 12259 16871 1703 314 330 O ATOM 1796 CB LYS A1035 71.278 195.903 323.453 1.00 82.54 C ANISOU 1796 CB LYS A1035 5929 10599 14834 1545 262 309 C ATOM 1797 CG LYS A1035 71.510 194.439 323.820 1.00 76.17 C ANISOU 1797 CG LYS A1035 5155 9912 13875 1477 243 290 C ATOM 1798 CD LYS A1035 72.177 194.325 325.192 1.00 72.75 C ANISOU 1798 CD LYS A1035 4706 9414 13521 1469 193 198 C ATOM 1799 CE LYS A1035 72.088 192.911 325.751 1.00 62.26 C ANISOU 1799 CE LYS A1035 3400 8234 12023 1424 183 171 C ATOM 1800 NZ LYS A1035 70.685 192.421 325.681 1.00 64.80 N ANISOU 1800 NZ LYS A1035 3711 8748 12162 1466 228 174 N ATOM 1801 N SER A1036 68.573 197.733 321.661 1.00 90.00 N ANISOU 1801 N SER A1036 6819 11653 15724 1721 384 418 N ATOM 1802 CA SER A1036 68.013 199.062 321.456 1.00 86.36 C ANISOU 1802 CA SER A1036 6322 11117 15375 1809 413 432 C ATOM 1803 C SER A1036 66.526 198.948 321.170 1.00 67.03 C ANISOU 1803 C SER A1036 3853 8840 12776 1871 458 444 C ATOM 1804 O SER A1036 66.063 197.910 320.681 1.00 66.01 O ANISOU 1804 O SER A1036 3743 8864 12474 1826 466 470 O ATOM 1805 CB SER A1036 68.713 199.798 320.310 1.00 83.13 C ANISOU 1805 CB SER A1036 5923 10568 15095 1777 417 522 C ATOM 1806 OG SER A1036 68.354 201.167 320.305 1.00 68.56 O ANISOU 1806 OG SER A1036 4041 8617 13392 1861 438 524 O ATOM 1807 N PRO A1037 65.759 199.991 321.463 1.00 79.60 N ANISOU 1807 N PRO A1037 5405 10406 14435 1974 487 423 N ATOM 1808 CA PRO A1037 64.305 199.952 321.244 1.00 79.64 C ANISOU 1808 CA PRO A1037 5383 10572 14306 2040 529 432 C ATOM 1809 C PRO A1037 63.855 200.284 319.827 1.00 78.50 C ANISOU 1809 C PRO A1037 5239 10447 14140 2034 557 529 C ATOM 1810 O PRO A1037 62.902 199.681 319.334 1.00 77.66 O ANISOU 1810 O PRO A1037 5127 10500 13882 2030 576 550 O ATOM 1811 CB PRO A1037 63.784 200.997 322.245 1.00 82.34 C ANISOU 1811 CB PRO A1037 5684 10857 14746 2162 548 363 C ATOM 1812 CG PRO A1037 64.935 201.234 323.213 1.00 81.98 C ANISOU 1812 CG PRO A1037 5647 10651 14851 2146 506 293 C ATOM 1813 CD PRO A1037 66.150 201.081 322.370 1.00 80.87 C ANISOU 1813 CD PRO A1037 5541 10401 14785 2040 474 358 C ATOM 1814 N SER A1038 64.510 201.227 319.154 1.00 76.95 N ANISOU 1814 N SER A1038 5046 10090 14100 2032 559 587 N ATOM 1815 CA SER A1038 63.951 201.795 317.927 1.00 76.41 C ANISOU 1815 CA SER A1038 4968 10031 14035 2052 593 676 C ATOM 1816 C SER A1038 64.038 200.844 316.742 1.00 68.13 C ANISOU 1816 C SER A1038 3954 9070 12863 1961 590 749 C ATOM 1817 O SER A1038 65.075 200.229 316.495 1.00 67.25 O ANISOU 1817 O SER A1038 3881 8913 12757 1875 563 767 O ATOM 1818 CB SER A1038 64.654 203.101 317.569 1.00 70.40 C ANISOU 1818 CB SER A1038 4198 9067 13485 2075 597 722 C ATOM 1819 OG SER A1038 64.044 203.678 316.430 1.00 70.82 O ANISOU 1819 OG SER A1038 4237 9133 13538 2102 632 810 O ATOM 1820 N LEU A1039 62.945 200.772 315.978 1.00 83.55 N ANISOU 1820 N LEU A1039 5889 11140 14715 1983 618 791 N ATOM 1821 CA LEU A1039 62.924 199.925 314.788 1.00 81.45 C ANISOU 1821 CA LEU A1039 5655 10953 14341 1904 617 857 C ATOM 1822 C LEU A1039 63.916 200.422 313.743 1.00 82.45 C ANISOU 1822 C LEU A1039 5805 10941 14581 1863 619 949 C ATOM 1823 O LEU A1039 64.759 199.656 313.263 1.00 81.80 O ANISOU 1823 O LEU A1039 5767 10846 14468 1779 600 977 O ATOM 1824 CB LEU A1039 61.508 199.852 314.201 1.00 82.59 C ANISOU 1824 CB LEU A1039 5768 11236 14377 1939 645 881 C ATOM 1825 CG LEU A1039 61.309 199.781 312.674 1.00 82.38 C ANISOU 1825 CG LEU A1039 5752 11229 14319 1900 660 982 C ATOM 1826 CD1 LEU A1039 61.794 198.471 312.024 1.00 81.86 C ANISOU 1826 CD1 LEU A1039 5737 11221 14146 1796 638 1002 C ATOM 1827 CD2 LEU A1039 59.856 200.051 312.296 1.00 67.72 C ANISOU 1827 CD2 LEU A1039 3851 9480 12401 1956 689 1002 C ATOM 1828 N ASN A1040 63.823 201.704 313.370 1.00 81.71 N ANISOU 1828 N ASN A1040 5682 10742 14621 1922 643 1000 N ATOM 1829 CA ASN A1040 64.729 202.245 312.361 1.00 82.82 C ANISOU 1829 CA ASN A1040 5840 10751 14878 1886 649 1095 C ATOM 1830 C ASN A1040 66.180 202.063 312.780 1.00 84.79 C ANISOU 1830 C ASN A1040 6120 10873 15222 1824 615 1077 C ATOM 1831 O ASN A1040 67.047 201.795 311.941 1.00 87.58 O ANISOU 1831 O ASN A1040 6505 11174 15597 1756 611 1146 O ATOM 1832 CB ASN A1040 64.428 203.722 312.100 1.00 69.83 C ANISOU 1832 CB ASN A1040 4154 9000 13380 1965 679 1142 C ATOM 1833 CG ASN A1040 64.366 204.543 313.375 1.00 88.24 C ANISOU 1833 CG ASN A1040 6455 11247 15826 2042 675 1060 C ATOM 1834 OD1 ASN A1040 63.683 204.174 314.331 1.00 89.78 O ANISOU 1834 OD1 ASN A1040 6637 11540 15937 2083 671 973 O ATOM 1835 ND2 ASN A1040 65.076 205.668 313.393 1.00 87.64 N ANISOU 1835 ND2 ASN A1040 6365 10987 15948 2063 677 1086 N ATOM 1836 N ALA A1041 66.462 202.199 314.078 1.00 83.12 N ANISOU 1836 N ALA A1041 5898 10611 15072 1847 592 986 N ATOM 1837 CA ALA A1041 67.775 201.834 314.596 1.00 81.51 C ANISOU 1837 CA ALA A1041 5722 10307 14941 1781 554 957 C ATOM 1838 C ALA A1041 68.035 200.344 314.409 1.00 66.31 C ANISOU 1838 C ALA A1041 3843 8500 12852 1699 536 950 C ATOM 1839 O ALA A1041 69.109 199.941 313.948 1.00 71.22 O ANISOU 1839 O ALA A1041 4500 9058 13503 1626 519 991 O ATOM 1840 CB ALA A1041 67.884 202.222 316.070 1.00 82.38 C ANISOU 1840 CB ALA A1041 5808 10352 15139 1827 531 853 C ATOM 1841 N ALA A1042 67.053 199.509 314.755 1.00 65.78 N ANISOU 1841 N ALA A1042 3776 8605 12614 1711 539 899 N ATOM 1842 CA ALA A1042 67.205 198.068 314.576 1.00 64.43 C ANISOU 1842 CA ALA A1042 3646 8548 12286 1635 523 889 C ATOM 1843 C ALA A1042 67.249 197.698 313.097 1.00 73.54 C ANISOU 1843 C ALA A1042 4829 9733 13381 1589 540 982 C ATOM 1844 O ALA A1042 68.096 196.903 312.671 1.00 62.95 O ANISOU 1844 O ALA A1042 3531 8379 12007 1516 526 1008 O ATOM 1845 CB ALA A1042 66.071 197.330 315.288 1.00 70.05 C ANISOU 1845 CB ALA A1042 4343 9432 12842 1660 524 814 C ATOM 1846 N LYS A1043 66.340 198.269 312.298 1.00 73.50 N ANISOU 1846 N LYS A1043 4797 9765 13363 1633 571 1035 N ATOM 1847 CA LYS A1043 66.301 197.977 310.866 1.00 71.43 C ANISOU 1847 CA LYS A1043 4557 9533 13050 1596 589 1127 C ATOM 1848 C LYS A1043 67.578 198.433 310.175 1.00 69.43 C ANISOU 1848 C LYS A1043 4327 9129 12926 1560 590 1206 C ATOM 1849 O LYS A1043 68.174 197.687 309.388 1.00 63.24 O ANISOU 1849 O LYS A1043 3584 8354 12091 1498 588 1253 O ATOM 1850 CB LYS A1043 65.083 198.645 310.227 1.00 64.76 C ANISOU 1850 CB LYS A1043 3672 8745 12188 1657 621 1170 C ATOM 1851 N SER A1044 68.004 199.669 310.444 1.00 68.59 N ANISOU 1851 N SER A1044 4192 8878 12992 1600 595 1223 N ATOM 1852 CA SER A1044 69.244 200.162 309.857 1.00 68.09 C ANISOU 1852 CA SER A1044 4143 8661 13068 1563 596 1298 C ATOM 1853 C SER A1044 70.434 199.331 310.312 1.00 64.41 C ANISOU 1853 C SER A1044 3716 8153 12603 1492 562 1266 C ATOM 1854 O SER A1044 71.325 199.025 309.512 1.00 63.96 O ANISOU 1854 O SER A1044 3690 8047 12563 1438 564 1335 O ATOM 1855 CB SER A1044 69.449 201.634 310.210 1.00 66.62 C ANISOU 1855 CB SER A1044 3913 8321 13080 1617 602 1310 C ATOM 1856 OG SER A1044 70.786 202.034 309.982 1.00 87.76 O ANISOU 1856 OG SER A1044 6599 10837 15909 1572 592 1360 O ATOM 1857 N GLU A1045 70.462 198.951 311.592 1.00 64.22 N ANISOU 1857 N GLU A1045 3691 8150 12560 1493 532 1165 N ATOM 1858 CA GLU A1045 71.558 198.128 312.095 1.00 85.72 C ANISOU 1858 CA GLU A1045 6450 10839 15282 1426 498 1131 C ATOM 1859 C GLU A1045 71.717 196.865 311.262 1.00 85.64 C ANISOU 1859 C GLU A1045 6490 10929 15122 1366 503 1167 C ATOM 1860 O GLU A1045 72.841 196.445 310.959 1.00 86.44 O ANISOU 1860 O GLU A1045 6624 10964 15254 1309 492 1202 O ATOM 1861 CB GLU A1045 71.325 197.770 313.562 1.00 63.36 C ANISOU 1861 CB GLU A1045 3607 8050 12417 1441 469 1016 C ATOM 1862 CG GLU A1045 72.505 198.083 314.466 1.00 63.67 C ANISOU 1862 CG GLU A1045 3642 7942 12609 1416 431 977 C ATOM 1863 CD GLU A1045 73.764 197.323 314.083 1.00 79.84 C ANISOU 1863 CD GLU A1045 5734 9943 14660 1333 413 1016 C ATOM 1864 OE1 GLU A1045 73.658 196.203 313.539 1.00 77.68 O ANISOU 1864 OE1 GLU A1045 5501 9783 14230 1295 421 1034 O ATOM 1865 OE2 GLU A1045 74.868 197.849 314.332 1.00 81.18 O ANISOU 1865 OE2 GLU A1045 5895 9956 14992 1308 389 1028 O ATOM 1866 N LEU A1046 70.598 196.260 310.863 1.00 61.81 N ANISOU 1866 N LEU A1046 3475 8063 11946 1379 519 1160 N ATOM 1867 CA LEU A1046 70.654 195.073 310.020 1.00 60.76 C ANISOU 1867 CA LEU A1046 3387 8022 11678 1325 524 1191 C ATOM 1868 C LEU A1046 71.296 195.388 308.670 1.00 70.88 C ANISOU 1868 C LEU A1046 4679 9217 13034 1304 551 1314 C ATOM 1869 O LEU A1046 72.241 194.713 308.247 1.00 70.55 O ANISOU 1869 O LEU A1046 4673 9138 12993 1250 548 1355 O ATOM 1870 CB LEU A1046 69.246 194.502 309.853 1.00 60.62 C ANISOU 1870 CB LEU A1046 3353 8161 11518 1343 538 1172 C ATOM 1871 CG LEU A1046 68.993 193.499 308.735 1.00 60.05 C ANISOU 1871 CG LEU A1046 3303 8164 11350 1300 555 1239 C ATOM 1872 CD1 LEU A1046 67.986 192.474 309.162 1.00 59.54 C ANISOU 1872 CD1 LEU A1046 3236 8250 11137 1288 546 1173 C ATOM 1873 CD2 LEU A1046 68.476 194.227 307.535 1.00 65.43 C ANISOU 1873 CD2 LEU A1046 3960 8833 12068 1331 590 1338 C ATOM 1874 N ASP A1047 70.805 196.434 307.990 1.00 61.83 N ANISOU 1874 N ASP A1047 3500 8038 11956 1351 579 1379 N ATOM 1875 CA ASP A1047 71.298 196.778 306.654 1.00 77.84 C ANISOU 1875 CA ASP A1047 5532 9995 14049 1337 609 1505 C ATOM 1876 C ASP A1047 72.811 196.936 306.621 1.00 78.45 C ANISOU 1876 C ASP A1047 5632 9933 14243 1296 599 1540 C ATOM 1877 O ASP A1047 73.445 196.636 305.603 1.00 76.60 O ANISOU 1877 O ASP A1047 5418 9666 14021 1263 619 1635 O ATOM 1878 CB ASP A1047 70.646 198.070 306.154 1.00 80.46 C ANISOU 1878 CB ASP A1047 5820 10291 14462 1398 637 1560 C ATOM 1879 CG ASP A1047 69.166 197.904 305.822 1.00 84.45 C ANISOU 1879 CG ASP A1047 6300 10933 14855 1436 656 1561 C ATOM 1880 OD1 ASP A1047 68.767 196.843 305.287 1.00 86.17 O ANISOU 1880 OD1 ASP A1047 6536 11255 14949 1404 661 1579 O ATOM 1881 OD2 ASP A1047 68.398 198.856 306.081 1.00 85.61 O ANISOU 1881 OD2 ASP A1047 6406 11078 15042 1498 665 1546 O ATOM 1882 N LYS A1048 73.405 197.410 307.719 1.00 82.34 N ANISOU 1882 N LYS A1048 6117 10341 14829 1298 568 1471 N ATOM 1883 CA LYS A1048 74.858 197.500 307.796 1.00 86.13 C ANISOU 1883 CA LYS A1048 6611 10683 15430 1252 553 1503 C ATOM 1884 C LYS A1048 75.501 196.123 307.679 1.00 88.69 C ANISOU 1884 C LYS A1048 6987 11062 15648 1192 542 1495 C ATOM 1885 O LYS A1048 76.530 195.965 307.012 1.00 90.92 O ANISOU 1885 O LYS A1048 7288 11269 15987 1155 552 1574 O ATOM 1886 CB LYS A1048 75.279 198.181 309.099 1.00 62.90 C ANISOU 1886 CB LYS A1048 3638 7632 12630 1262 520 1433 C ATOM 1887 N ALA A1049 74.905 195.110 308.302 1.00 60.40 N ANISOU 1887 N ALA A1049 3422 7602 11926 1184 525 1413 N ATOM 1888 CA ALA A1049 75.496 193.781 308.292 1.00 59.45 C ANISOU 1888 CA ALA A1049 3345 7522 11720 1129 515 1406 C ATOM 1889 C ALA A1049 75.095 192.951 307.077 1.00 59.03 C ANISOU 1889 C ALA A1049 3313 7554 11562 1114 548 1480 C ATOM 1890 O ALA A1049 75.447 191.770 307.021 1.00 58.24 O ANISOU 1890 O ALA A1049 3249 7501 11377 1073 542 1471 O ATOM 1891 CB ALA A1049 75.116 193.024 309.562 1.00 58.86 C ANISOU 1891 CB ALA A1049 3279 7537 11548 1122 481 1285 C ATOM 1892 N ILE A1050 74.369 193.514 306.116 1.00 59.57 N ANISOU 1892 N ILE A1050 3358 7643 11631 1148 581 1551 N ATOM 1893 CA ILE A1050 73.936 192.754 304.950 1.00 59.23 C ANISOU 1893 CA ILE A1050 3332 7685 11488 1137 609 1620 C ATOM 1894 C ILE A1050 74.387 193.519 303.714 1.00 59.87 C ANISOU 1894 C ILE A1050 3403 7683 11661 1149 645 1749 C ATOM 1895 O ILE A1050 74.671 192.937 302.660 1.00 59.61 O ANISOU 1895 O ILE A1050 3393 7670 11586 1130 669 1829 O ATOM 1896 CB ILE A1050 72.408 192.519 304.961 1.00 64.51 C ANISOU 1896 CB ILE A1050 3980 8493 12039 1165 613 1581 C ATOM 1897 CG1 ILE A1050 72.040 191.383 305.925 1.00 58.43 C ANISOU 1897 CG1 ILE A1050 3227 7824 11149 1139 583 1474 C ATOM 1898 CG2 ILE A1050 71.893 192.148 303.580 1.00 64.72 C ANISOU 1898 CG2 ILE A1050 4010 8586 11996 1165 645 1673 C ATOM 1899 CD1 ILE A1050 71.829 191.818 307.350 1.00 58.59 C ANISOU 1899 CD1 ILE A1050 3227 7840 11195 1161 554 1367 C ATOM 1900 N GLY A1051 74.452 194.838 303.846 1.00 61.49 N ANISOU 1900 N GLY A1051 3573 7796 11996 1182 650 1769 N ATOM 1901 CA GLY A1051 74.949 195.703 302.808 1.00 61.45 C ANISOU 1901 CA GLY A1051 3553 7697 12100 1194 683 1889 C ATOM 1902 C GLY A1051 73.922 196.134 301.788 1.00 61.99 C ANISOU 1902 C GLY A1051 3594 7827 12132 1234 718 1964 C ATOM 1903 O GLY A1051 74.259 196.914 300.888 1.00 74.82 O ANISOU 1903 O GLY A1051 5202 9379 13847 1247 749 2071 O ATOM 1904 N ARG A1052 72.683 195.658 301.892 1.00 61.76 N ANISOU 1904 N ARG A1052 3558 7929 11978 1252 715 1915 N ATOM 1905 CA ARG A1052 71.631 196.023 300.954 1.00 62.28 C ANISOU 1905 CA ARG A1052 3596 8064 12004 1289 744 1984 C ATOM 1906 C ARG A1052 70.412 196.536 301.707 1.00 79.28 C ANISOU 1906 C ARG A1052 5711 10277 14135 1335 734 1908 C ATOM 1907 O ARG A1052 70.202 196.215 302.878 1.00 73.06 O ANISOU 1907 O ARG A1052 4927 9522 13312 1332 703 1795 O ATOM 1908 CB ARG A1052 71.236 194.840 300.062 1.00 79.96 C ANISOU 1908 CB ARG A1052 5860 10420 14101 1266 755 2021 C ATOM 1909 CG ARG A1052 70.392 193.776 300.736 1.00 60.94 C ANISOU 1909 CG ARG A1052 3462 8140 11552 1250 728 1919 C ATOM 1910 CD ARG A1052 70.029 192.710 299.724 1.00 69.35 C ANISOU 1910 CD ARG A1052 4549 9308 12493 1227 740 1967 C ATOM 1911 NE ARG A1052 69.239 191.620 300.284 1.00 59.78 N ANISOU 1911 NE ARG A1052 3346 8219 11149 1204 715 1877 N ATOM 1912 CZ ARG A1052 67.915 191.643 300.391 1.00 85.78 C ANISOU 1912 CZ ARG A1052 6607 11613 14374 1226 711 1849 C ATOM 1913 NH1 ARG A1052 67.271 190.603 300.900 1.00 85.18 N ANISOU 1913 NH1 ARG A1052 6539 11642 14183 1198 688 1771 N ATOM 1914 NH2 ARG A1052 67.234 192.709 299.997 1.00 86.37 N ANISOU 1914 NH2 ARG A1052 6638 11681 14498 1274 731 1901 N ATOM 1915 N ASN A1053 69.597 197.336 301.017 1.00 63.49 N ANISOU 1915 N ASN A1053 3674 8295 12156 1380 761 1974 N ATOM 1916 CA ASN A1053 68.409 197.940 301.626 1.00 70.74 C ANISOU 1916 CA ASN A1053 4550 9266 13062 1433 757 1917 C ATOM 1917 C ASN A1053 67.305 196.898 301.692 1.00 73.56 C ANISOU 1917 C ASN A1053 4909 9782 13258 1425 747 1869 C ATOM 1918 O ASN A1053 66.487 196.756 300.781 1.00 63.71 O ANISOU 1918 O ASN A1053 3646 8616 11946 1436 767 1935 O ATOM 1919 CB ASN A1053 67.960 199.173 300.857 1.00 69.85 C ANISOU 1919 CB ASN A1053 4395 9111 13033 1485 791 2011 C ATOM 1920 CG ASN A1053 68.948 200.308 300.962 1.00 69.98 C ANISOU 1920 CG ASN A1053 4401 8965 13222 1496 798 2046 C ATOM 1921 OD1 ASN A1053 68.922 201.088 301.915 1.00 66.28 O ANISOU 1921 OD1 ASN A1053 3912 8436 12835 1529 784 1977 O ATOM 1922 ND2 ASN A1053 69.837 200.403 299.984 1.00 70.17 N ANISOU 1922 ND2 ASN A1053 4440 8918 13305 1470 821 2154 N ATOM 1923 N THR A1054 67.282 196.169 302.807 1.00 76.76 N ANISOU 1923 N THR A1054 5331 10232 13602 1403 715 1754 N ATOM 1924 CA THR A1054 66.324 195.085 302.981 1.00 78.88 C ANISOU 1924 CA THR A1054 5602 10646 13722 1385 702 1701 C ATOM 1925 C THR A1054 64.917 195.614 303.198 1.00 81.58 C ANISOU 1925 C THR A1054 5894 11069 14034 1439 710 1680 C ATOM 1926 O THR A1054 63.939 194.994 302.761 1.00 81.85 O ANISOU 1926 O THR A1054 5917 11220 13964 1432 713 1694 O ATOM 1927 CB THR A1054 66.734 194.238 304.175 1.00 61.44 C ANISOU 1927 CB THR A1054 3423 8457 11466 1350 668 1587 C ATOM 1928 OG1 THR A1054 66.570 195.019 305.362 1.00 61.89 O ANISOU 1928 OG1 THR A1054 3453 8480 11582 1392 654 1504 O ATOM 1929 CG2 THR A1054 68.182 193.811 304.036 1.00 60.92 C ANISOU 1929 CG2 THR A1054 3404 8300 11444 1301 660 1609 C ATOM 1930 N ASN A1055 64.799 196.750 303.885 1.00 82.61 N ANISOU 1930 N ASN A1055 5993 11137 14259 1494 712 1646 N ATOM 1931 CA ASN A1055 63.517 197.266 304.360 1.00 64.36 C ANISOU 1931 CA ASN A1055 3633 8897 11924 1553 718 1606 C ATOM 1932 C ASN A1055 62.817 196.269 305.275 1.00 63.76 C ANISOU 1932 C ASN A1055 3557 8943 11726 1536 694 1501 C ATOM 1933 O ASN A1055 61.591 196.275 305.395 1.00 82.09 O ANISOU 1933 O ASN A1055 5842 11363 13987 1566 700 1484 O ATOM 1934 CB ASN A1055 62.604 197.666 303.198 1.00 65.04 C ANISOU 1934 CB ASN A1055 3686 9032 11996 1582 749 1710 C ATOM 1935 CG ASN A1055 62.789 199.108 302.789 1.00 98.15 C ANISOU 1935 CG ASN A1055 7851 13118 16325 1637 776 1781 C ATOM 1936 OD1 ASN A1055 63.103 199.964 303.617 1.00 66.56 O ANISOU 1936 OD1 ASN A1055 3838 9032 12419 1676 771 1729 O ATOM 1937 ND2 ASN A1055 62.592 199.392 301.505 1.00 99.09 N ANISOU 1937 ND2 ASN A1055 7958 13238 16455 1642 805 1903 N ATOM 1938 N GLY A1056 63.585 195.401 305.924 1.00 62.87 N ANISOU 1938 N GLY A1056 3484 8824 11578 1485 667 1434 N ATOM 1939 CA GLY A1056 63.040 194.499 306.912 1.00 62.32 C ANISOU 1939 CA GLY A1056 3416 8859 11404 1468 643 1331 C ATOM 1940 C GLY A1056 62.911 193.047 306.508 1.00 61.41 C ANISOU 1940 C GLY A1056 3330 8835 11168 1398 632 1334 C ATOM 1941 O GLY A1056 62.336 192.263 307.272 1.00 61.01 O ANISOU 1941 O GLY A1056 3275 8878 11028 1381 615 1255 O ATOM 1942 N VAL A1057 63.434 192.655 305.348 1.00 77.29 N ANISOU 1942 N VAL A1057 5370 10821 13175 1359 642 1424 N ATOM 1943 CA VAL A1057 63.273 191.296 304.845 1.00 74.63 C ANISOU 1943 CA VAL A1057 5062 10569 12725 1298 634 1434 C ATOM 1944 C VAL A1057 64.618 190.773 304.354 1.00 72.22 C ANISOU 1944 C VAL A1057 4810 10188 12441 1251 631 1472 C ATOM 1945 O VAL A1057 65.392 191.500 303.723 1.00 71.30 O ANISOU 1945 O VAL A1057 4701 9971 12418 1265 648 1546 O ATOM 1946 CB VAL A1057 62.213 191.229 303.724 1.00 75.31 C ANISOU 1946 CB VAL A1057 5121 10737 12757 1304 652 1516 C ATOM 1947 CG1 VAL A1057 62.643 192.053 302.510 1.00 75.90 C ANISOU 1947 CG1 VAL A1057 5193 10735 12909 1328 680 1636 C ATOM 1948 CG2 VAL A1057 61.953 189.790 303.331 1.00 74.67 C ANISOU 1948 CG2 VAL A1057 5066 10748 12557 1241 639 1514 C ATOM 1949 N ILE A1058 64.898 189.504 304.650 1.00 58.77 N ANISOU 1949 N ILE A1058 3144 8532 10655 1195 611 1424 N ATOM 1950 CA ILE A1058 66.113 188.851 304.190 1.00 58.12 C ANISOU 1950 CA ILE A1058 3113 8391 10580 1150 609 1457 C ATOM 1951 C ILE A1058 65.745 187.533 303.523 1.00 57.51 C ANISOU 1951 C ILE A1058 3058 8407 10386 1101 606 1473 C ATOM 1952 O ILE A1058 64.677 186.965 303.757 1.00 76.53 O ANISOU 1952 O ILE A1058 5448 10923 12708 1089 595 1433 O ATOM 1953 CB ILE A1058 67.109 188.609 305.337 1.00 57.62 C ANISOU 1953 CB ILE A1058 3077 8267 10548 1129 585 1377 C ATOM 1954 CG1 ILE A1058 66.519 187.615 306.331 1.00 57.06 C ANISOU 1954 CG1 ILE A1058 3008 8297 10374 1101 560 1275 C ATOM 1955 CG2 ILE A1058 67.439 189.914 306.032 1.00 58.27 C ANISOU 1955 CG2 ILE A1058 3135 8257 10749 1177 585 1356 C ATOM 1956 CD1 ILE A1058 67.516 187.092 307.315 1.00 56.44 C ANISOU 1956 CD1 ILE A1058 2963 8176 10304 1070 536 1207 C ATOM 1957 N THR A1059 66.657 187.048 302.685 1.00 57.12 N ANISOU 1957 N THR A1059 3049 8316 10339 1073 615 1535 N ATOM 1958 CA THR A1059 66.446 185.816 301.943 1.00 56.57 C ANISOU 1958 CA THR A1059 3004 8324 10166 1029 613 1557 C ATOM 1959 C THR A1059 66.681 184.602 302.838 1.00 55.71 C ANISOU 1959 C THR A1059 2927 8253 9989 980 586 1464 C ATOM 1960 O THR A1059 67.213 184.704 303.945 1.00 55.50 O ANISOU 1960 O THR A1059 2908 8183 9998 978 571 1394 O ATOM 1961 CB THR A1059 67.377 185.752 300.730 1.00 73.63 C ANISOU 1961 CB THR A1059 5194 10426 12355 1024 636 1655 C ATOM 1962 OG1 THR A1059 67.605 187.073 300.221 1.00 72.88 O ANISOU 1962 OG1 THR A1059 5076 10252 12363 1071 661 1732 O ATOM 1963 CG2 THR A1059 66.767 184.896 299.628 1.00 75.15 C ANISOU 1963 CG2 THR A1059 5392 10713 12448 1003 642 1705 C ATOM 1964 N LYS A1060 66.268 183.432 302.341 1.00 55.25 N ANISOU 1964 N LYS A1060 2884 8278 9830 938 581 1467 N ATOM 1965 CA LYS A1060 66.622 182.181 303.005 1.00 77.95 C ANISOU 1965 CA LYS A1060 5795 11181 12643 887 559 1395 C ATOM 1966 C LYS A1060 68.134 182.021 303.089 1.00 76.49 C ANISOU 1966 C LYS A1060 5655 10897 12512 876 562 1404 C ATOM 1967 O LYS A1060 68.662 181.522 304.090 1.00 53.49 O ANISOU 1967 O LYS A1060 2763 7967 9595 852 543 1332 O ATOM 1968 CB LYS A1060 65.997 180.996 302.264 1.00 78.00 C ANISOU 1968 CB LYS A1060 5811 11281 12544 845 555 1411 C ATOM 1969 CG LYS A1060 66.267 179.629 302.900 1.00 76.54 C ANISOU 1969 CG LYS A1060 5661 11130 12291 788 534 1339 C ATOM 1970 CD LYS A1060 65.499 178.515 302.180 1.00 74.63 C ANISOU 1970 CD LYS A1060 5423 10983 11950 746 529 1353 C ATOM 1971 CE LYS A1060 65.884 178.424 300.700 1.00 72.27 C ANISOU 1971 CE LYS A1060 5140 10672 11646 752 550 1449 C ATOM 1972 NZ LYS A1060 65.192 177.303 299.991 1.00 70.41 N ANISOU 1972 NZ LYS A1060 4909 10530 11314 709 541 1462 N ATOM 1973 N ASP A1061 68.847 182.442 302.043 1.00 76.09 N ANISOU 1973 N ASP A1061 5617 10780 12514 893 587 1496 N ATOM 1974 CA ASP A1061 70.303 182.420 302.085 1.00 75.91 C ANISOU 1974 CA ASP A1061 5632 10654 12557 887 593 1517 C ATOM 1975 C ASP A1061 70.822 183.397 303.128 1.00 54.24 C ANISOU 1975 C ASP A1061 2874 7821 9912 909 583 1478 C ATOM 1976 O ASP A1061 71.555 183.014 304.045 1.00 58.44 O ANISOU 1976 O ASP A1061 3430 8317 10459 887 565 1420 O ATOM 1977 CB ASP A1061 70.875 182.746 300.705 1.00 77.91 C ANISOU 1977 CB ASP A1061 5895 10859 12848 905 626 1631 C ATOM 1978 CG ASP A1061 70.486 181.722 299.653 1.00 81.24 C ANISOU 1978 CG ASP A1061 6333 11366 13170 884 635 1668 C ATOM 1979 OD1 ASP A1061 69.643 180.844 299.944 1.00 81.97 O ANISOU 1979 OD1 ASP A1061 6422 11554 13168 854 615 1609 O ATOM 1980 OD2 ASP A1061 71.020 181.806 298.526 1.00 83.45 O ANISOU 1980 OD2 ASP A1061 6624 11616 13466 897 662 1758 O ATOM 1981 N GLU A1062 70.429 184.670 303.014 1.00 55.01 N ANISOU 1981 N GLU A1062 2933 7886 10081 954 594 1510 N ATOM 1982 CA GLU A1062 70.920 185.677 303.948 1.00 55.37 C ANISOU 1982 CA GLU A1062 2963 7843 10231 978 585 1476 C ATOM 1983 C GLU A1062 70.646 185.285 305.395 1.00 61.14 C ANISOU 1983 C GLU A1062 3691 8616 10924 964 553 1359 C ATOM 1984 O GLU A1062 71.431 185.625 306.286 1.00 62.28 O ANISOU 1984 O GLU A1062 3841 8686 11136 964 537 1318 O ATOM 1985 CB GLU A1062 70.300 187.036 303.624 1.00 56.29 C ANISOU 1985 CB GLU A1062 3034 7936 10418 1030 602 1520 C ATOM 1986 CG GLU A1062 70.447 187.438 302.168 1.00 72.91 C ANISOU 1986 CG GLU A1062 5137 10011 12553 1046 635 1641 C ATOM 1987 CD GLU A1062 70.026 188.872 301.914 1.00 74.99 C ANISOU 1987 CD GLU A1062 5357 10231 12906 1098 653 1689 C ATOM 1988 OE1 GLU A1062 69.928 189.641 302.893 1.00 76.66 O ANISOU 1988 OE1 GLU A1062 5544 10403 13180 1122 640 1631 O ATOM 1989 OE2 GLU A1062 69.794 189.229 300.736 1.00 58.11 O ANISOU 1989 OE2 GLU A1062 3208 8098 10775 1117 681 1785 O ATOM 1990 N ALA A1063 69.561 184.549 305.648 1.00 59.62 N ANISOU 1990 N ALA A1063 3487 8542 10624 949 542 1306 N ATOM 1991 CA ALA A1063 69.306 184.070 307.004 1.00 54.39 C ANISOU 1991 CA ALA A1063 2822 7929 9916 934 513 1198 C ATOM 1992 C ALA A1063 70.302 182.997 307.414 1.00 87.44 C ANISOU 1992 C ALA A1063 7055 12095 14075 886 498 1168 C ATOM 1993 O ALA A1063 70.606 182.855 308.605 1.00 87.09 O ANISOU 1993 O ALA A1063 7013 12044 14033 877 475 1092 O ATOM 1994 CB ALA A1063 67.877 183.539 307.122 1.00 54.37 C ANISOU 1994 CB ALA A1063 2793 8057 9810 927 508 1158 C ATOM 1995 N GLU A1064 70.821 182.241 306.450 1.00 53.21 N ANISOU 1995 N GLU A1064 2755 7750 9713 857 511 1227 N ATOM 1996 CA GLU A1064 71.744 181.151 306.734 1.00 52.48 C ANISOU 1996 CA GLU A1064 2707 7641 9591 813 500 1205 C ATOM 1997 C GLU A1064 73.173 181.648 306.923 1.00 65.28 C ANISOU 1997 C GLU A1064 4350 9135 11320 819 501 1233 C ATOM 1998 O GLU A1064 73.821 181.308 307.917 1.00 52.19 O ANISOU 1998 O GLU A1064 2707 7450 9672 799 479 1177 O ATOM 1999 CB GLU A1064 71.675 180.117 305.612 1.00 52.09 C ANISOU 1999 CB GLU A1064 2686 7639 9468 785 516 1255 C ATOM 2000 CG GLU A1064 72.631 178.963 305.770 1.00 85.24 C ANISOU 2000 CG GLU A1064 6932 11819 13638 744 510 1241 C ATOM 2001 CD GLU A1064 72.333 177.845 304.798 1.00 76.65 C ANISOU 2001 CD GLU A1064 5866 10798 12461 716 521 1271 C ATOM 2002 OE1 GLU A1064 72.537 176.670 305.166 1.00 67.68 O ANISOU 2002 OE1 GLU A1064 4757 9695 11263 677 510 1228 O ATOM 2003 OE2 GLU A1064 71.881 178.141 303.672 1.00 72.50 O ANISOU 2003 OE2 GLU A1064 5327 10293 11928 735 542 1339 O ATOM 2004 N LYS A1065 73.676 182.447 305.978 1.00 63.35 N ANISOU 2004 N LYS A1065 4102 8811 11157 843 526 1323 N ATOM 2005 CA LYS A1065 74.997 183.048 306.139 1.00 63.00 C ANISOU 2005 CA LYS A1065 4069 8637 11230 847 527 1357 C ATOM 2006 C LYS A1065 75.081 183.808 307.455 1.00 62.61 C ANISOU 2006 C LYS A1065 3996 8547 11245 861 499 1284 C ATOM 2007 O LYS A1065 76.027 183.634 308.233 1.00 60.84 O ANISOU 2007 O LYS A1065 3789 8263 11063 841 479 1252 O ATOM 2008 CB LYS A1065 75.307 183.985 304.965 1.00 64.94 C ANISOU 2008 CB LYS A1065 4305 8810 11560 877 559 1465 C ATOM 2009 CG LYS A1065 75.302 183.331 303.588 1.00 53.65 C ANISOU 2009 CG LYS A1065 2896 7417 10073 870 589 1546 C ATOM 2010 CD LYS A1065 75.395 184.380 302.485 1.00 54.39 C ANISOU 2010 CD LYS A1065 2969 7453 10243 906 622 1651 C ATOM 2011 CE LYS A1065 75.265 183.760 301.096 1.00 54.28 C ANISOU 2011 CE LYS A1065 2972 7491 10162 905 652 1731 C ATOM 2012 NZ LYS A1065 75.274 184.789 300.015 1.00 55.05 N ANISOU 2012 NZ LYS A1065 3046 7543 10327 942 685 1837 N ATOM 2013 N LEU A1066 74.080 184.652 307.720 1.00 63.01 N ANISOU 2013 N LEU A1066 4006 8633 11303 897 497 1257 N ATOM 2014 CA LEU A1066 74.037 185.393 308.975 1.00 54.29 C ANISOU 2014 CA LEU A1066 2874 7501 10251 917 472 1183 C ATOM 2015 C LEU A1066 74.060 184.448 310.169 1.00 64.14 C ANISOU 2015 C LEU A1066 4137 8809 11424 887 441 1087 C ATOM 2016 O LEU A1066 74.661 184.758 311.206 1.00 64.71 O ANISOU 2016 O LEU A1066 4206 8829 11551 887 416 1037 O ATOM 2017 CB LEU A1066 72.789 186.275 309.006 1.00 54.93 C ANISOU 2017 CB LEU A1066 2908 7633 10328 965 480 1168 C ATOM 2018 CG LEU A1066 72.982 187.725 309.439 1.00 55.72 C ANISOU 2018 CG LEU A1066 2976 7641 10554 1009 477 1165 C ATOM 2019 CD1 LEU A1066 71.658 188.460 309.474 1.00 56.33 C ANISOU 2019 CD1 LEU A1066 3007 7784 10612 1059 487 1148 C ATOM 2020 CD2 LEU A1066 73.652 187.756 310.793 1.00 90.61 C ANISOU 2020 CD2 LEU A1066 7398 12019 15011 1000 442 1085 C ATOM 2021 N PHE A1067 73.418 183.285 310.036 1.00 62.58 N ANISOU 2021 N PHE A1067 3954 8720 11103 859 442 1064 N ATOM 2022 CA PHE A1067 73.435 182.296 311.107 1.00 61.18 C ANISOU 2022 CA PHE A1067 3791 8603 10850 827 416 980 C ATOM 2023 C PHE A1067 74.828 181.726 311.328 1.00 60.63 C ANISOU 2023 C PHE A1067 3762 8458 10818 792 404 991 C ATOM 2024 O PHE A1067 75.180 181.358 312.455 1.00 60.75 O ANISOU 2024 O PHE A1067 3783 8479 10820 775 377 924 O ATOM 2025 CB PHE A1067 72.451 181.170 310.794 1.00 60.04 C ANISOU 2025 CB PHE A1067 3652 8583 10576 800 421 962 C ATOM 2026 CG PHE A1067 72.677 179.931 311.604 1.00 51.36 C ANISOU 2026 CG PHE A1067 2579 7535 9401 756 399 899 C ATOM 2027 CD1 PHE A1067 72.461 179.939 312.973 1.00 73.25 C ANISOU 2027 CD1 PHE A1067 5333 10346 12152 759 374 812 C ATOM 2028 CD2 PHE A1067 73.100 178.757 311.001 1.00 50.76 C ANISOU 2028 CD2 PHE A1067 2544 7470 9274 714 406 928 C ATOM 2029 CE1 PHE A1067 72.666 178.799 313.727 1.00 72.42 C ANISOU 2029 CE1 PHE A1067 5250 10290 11978 717 355 759 C ATOM 2030 CE2 PHE A1067 73.304 177.615 311.747 1.00 50.16 C ANISOU 2030 CE2 PHE A1067 2490 7436 9131 673 388 872 C ATOM 2031 CZ PHE A1067 73.087 177.636 313.113 1.00 71.91 C ANISOU 2031 CZ PHE A1067 5226 10229 11866 673 362 789 C ATOM 2032 N ASN A1068 75.635 181.638 310.271 1.00 52.01 N ANISOU 2032 N ASN A1068 2696 7295 9770 782 426 1076 N ATOM 2033 CA ASN A1068 76.994 181.144 310.443 1.00 51.66 C ANISOU 2033 CA ASN A1068 2687 7172 9769 753 418 1093 C ATOM 2034 C ASN A1068 77.813 182.087 311.311 1.00 52.06 C ANISOU 2034 C ASN A1068 2723 7122 9937 764 395 1073 C ATOM 2035 O ASN A1068 78.561 181.642 312.188 1.00 51.76 O ANISOU 2035 O ASN A1068 2700 7059 9909 740 370 1032 O ATOM 2036 CB ASN A1068 77.649 180.924 309.084 1.00 51.63 C ANISOU 2036 CB ASN A1068 2710 7117 9790 748 451 1194 C ATOM 2037 CG ASN A1068 77.100 179.703 308.387 1.00 62.04 C ANISOU 2037 CG ASN A1068 4052 8532 10988 726 466 1203 C ATOM 2038 OD1 ASN A1068 76.577 178.794 309.036 1.00 61.35 O ANISOU 2038 OD1 ASN A1068 3971 8530 10808 701 448 1133 O ATOM 2039 ND2 ASN A1068 77.205 179.673 307.064 1.00 62.28 N ANISOU 2039 ND2 ASN A1068 4093 8549 11021 735 498 1289 N ATOM 2040 N GLN A1069 77.664 183.394 311.108 1.00 52.78 N ANISOU 2040 N GLN A1069 2782 7153 10120 801 402 1100 N ATOM 2041 CA GLN A1069 78.295 184.343 312.016 1.00 53.24 C ANISOU 2041 CA GLN A1069 2818 7119 10290 813 376 1068 C ATOM 2042 C GLN A1069 77.785 184.191 313.441 1.00 53.10 C ANISOU 2042 C GLN A1069 2785 7171 10220 816 341 959 C ATOM 2043 O GLN A1069 78.494 184.556 314.384 1.00 63.25 O ANISOU 2043 O GLN A1069 4064 8394 11576 812 311 920 O ATOM 2044 CB GLN A1069 78.076 185.770 311.515 1.00 60.92 C ANISOU 2044 CB GLN A1069 3757 8023 11367 854 391 1114 C ATOM 2045 CG GLN A1069 79.054 186.209 310.427 1.00 60.64 C ANISOU 2045 CG GLN A1069 3731 7873 11435 849 416 1223 C ATOM 2046 CD GLN A1069 78.841 185.505 309.095 1.00 59.57 C ANISOU 2046 CD GLN A1069 3620 7785 11227 841 454 1300 C ATOM 2047 OE1 GLN A1069 78.733 184.279 309.025 1.00 58.28 O ANISOU 2047 OE1 GLN A1069 3486 7699 10957 815 455 1283 O ATOM 2048 NE2 GLN A1069 78.786 186.289 308.027 1.00 54.65 N ANISOU 2048 NE2 GLN A1069 2982 7116 10665 866 485 1388 N ATOM 2049 N ASP A1070 76.585 183.645 313.620 1.00 72.37 N ANISOU 2049 N ASP A1070 5217 9740 12539 823 345 912 N ATOM 2050 CA ASP A1070 76.070 183.406 314.960 1.00 73.59 C ANISOU 2050 CA ASP A1070 5355 9975 12632 826 317 813 C ATOM 2051 C ASP A1070 76.626 182.135 315.588 1.00 75.39 C ANISOU 2051 C ASP A1070 5615 10236 12792 779 297 776 C ATOM 2052 O ASP A1070 76.545 181.993 316.811 1.00 78.74 O ANISOU 2052 O ASP A1070 6028 10702 13188 779 269 701 O ATOM 2053 CB ASP A1070 74.539 183.350 314.940 1.00 73.72 C ANISOU 2053 CB ASP A1070 5344 10118 12550 852 330 779 C ATOM 2054 CG ASP A1070 73.900 184.706 315.202 1.00 75.50 C ANISOU 2054 CG ASP A1070 5522 10328 12835 911 332 762 C ATOM 2055 OD1 ASP A1070 73.440 184.939 316.344 1.00 77.14 O ANISOU 2055 OD1 ASP A1070 5704 10587 13019 936 313 684 O ATOM 2056 OD2 ASP A1070 73.862 185.541 314.270 1.00 74.35 O ANISOU 2056 OD2 ASP A1070 5366 10121 12761 936 355 828 O ATOM 2057 N VAL A1071 77.174 181.214 314.797 1.00 73.14 N ANISOU 2057 N VAL A1071 5370 9940 12481 743 312 829 N ATOM 2058 CA VAL A1071 77.856 180.037 315.329 1.00 50.85 C ANISOU 2058 CA VAL A1071 2579 7132 9609 699 295 804 C ATOM 2059 C VAL A1071 79.372 180.195 315.275 1.00 67.83 C ANISOU 2059 C VAL A1071 4750 9153 11868 682 286 849 C ATOM 2060 O VAL A1071 80.078 179.724 316.168 1.00 66.98 O ANISOU 2060 O VAL A1071 4654 9031 11763 658 258 812 O ATOM 2061 CB VAL A1071 77.398 178.751 314.599 1.00 50.25 C ANISOU 2061 CB VAL A1071 2532 7139 9420 670 316 823 C ATOM 2062 CG1 VAL A1071 77.342 178.951 313.110 1.00 50.39 C ANISOU 2062 CG1 VAL A1071 2560 7126 9461 680 351 911 C ATOM 2063 CG2 VAL A1071 78.320 177.586 314.919 1.00 49.64 C ANISOU 2063 CG2 VAL A1071 2494 7051 9317 627 305 818 C ATOM 2064 N ASP A1072 79.883 180.867 314.241 1.00 68.96 N ANISOU 2064 N ASP A1072 4896 9204 12102 695 309 932 N ATOM 2065 CA ASP A1072 81.303 181.204 314.192 1.00 68.83 C ANISOU 2065 CA ASP A1072 4890 9058 12205 682 301 979 C ATOM 2066 C ASP A1072 81.730 181.962 315.441 1.00 51.85 C ANISOU 2066 C ASP A1072 2712 6853 10135 687 259 919 C ATOM 2067 O ASP A1072 82.735 181.625 316.077 1.00 63.84 O ANISOU 2067 O ASP A1072 4242 8322 11691 660 233 907 O ATOM 2068 CB ASP A1072 81.604 182.038 312.946 1.00 69.31 C ANISOU 2068 CB ASP A1072 4945 9032 12357 701 333 1076 C ATOM 2069 CG ASP A1072 81.950 181.190 311.750 1.00 51.60 C ANISOU 2069 CG ASP A1072 2738 6795 10073 686 369 1155 C ATOM 2070 OD1 ASP A1072 81.651 179.978 311.776 1.00 54.05 O ANISOU 2070 OD1 ASP A1072 3074 7191 10270 666 372 1130 O ATOM 2071 OD2 ASP A1072 82.523 181.737 310.786 1.00 51.99 O ANISOU 2071 OD2 ASP A1072 2786 6762 10204 697 395 1244 O ATOM 2072 N ALA A1073 80.977 183.001 315.802 1.00 52.38 N ANISOU 2072 N ALA A1073 2742 6928 10231 723 252 882 N ATOM 2073 CA ALA A1073 81.282 183.763 317.002 1.00 52.90 C ANISOU 2073 CA ALA A1073 2774 6938 10386 733 212 825 C ATOM 2074 C ALA A1073 80.797 183.077 318.275 1.00 73.22 C ANISOU 2074 C ALA A1073 5339 9606 12874 726 184 736 C ATOM 2075 O ALA A1073 81.248 183.440 319.366 1.00 75.37 O ANISOU 2075 O ALA A1073 5585 9824 13229 724 147 691 O ATOM 2076 CB ALA A1073 80.679 185.165 316.908 1.00 61.87 C ANISOU 2076 CB ALA A1073 3865 8027 11614 780 218 829 C ATOM 2077 N ALA A1074 79.893 182.102 318.168 1.00 70.97 N ANISOU 2077 N ALA A1074 5073 9460 12433 720 200 709 N ATOM 2078 CA ALA A1074 79.492 181.335 319.340 1.00 51.69 C ANISOU 2078 CA ALA A1074 2624 7111 9905 708 177 633 C ATOM 2079 C ALA A1074 80.417 180.163 319.616 1.00 51.05 C ANISOU 2079 C ALA A1074 2581 7029 9788 659 162 634 C ATOM 2080 O ALA A1074 80.303 179.549 320.681 1.00 50.87 O ANISOU 2080 O ALA A1074 2551 7067 9712 645 138 576 O ATOM 2081 CB ALA A1074 78.060 180.818 319.189 1.00 55.34 C ANISOU 2081 CB ALA A1074 3082 7724 10222 721 198 601 C ATOM 2082 N VAL A1075 81.319 179.844 318.690 1.00 50.76 N ANISOU 2082 N VAL A1075 2581 6926 9778 637 178 701 N ATOM 2083 CA VAL A1075 82.274 178.763 318.897 1.00 66.60 C ANISOU 2083 CA VAL A1075 4622 8921 11763 596 167 710 C ATOM 2084 C VAL A1075 83.577 179.274 319.507 1.00 50.68 C ANISOU 2084 C VAL A1075 2593 6778 9885 583 134 721 C ATOM 2085 O VAL A1075 84.224 178.550 320.270 1.00 50.45 O ANISOU 2085 O VAL A1075 2573 6749 9845 554 108 698 O ATOM 2086 CB VAL A1075 82.526 178.017 317.572 1.00 66.72 C ANISOU 2086 CB VAL A1075 4674 8922 11753 580 207 790 C ATOM 2087 CG1 VAL A1075 83.884 178.382 316.972 1.00 67.99 C ANISOU 2087 CG1 VAL A1075 4847 8947 12038 572 213 869 C ATOM 2088 CG2 VAL A1075 82.411 176.523 317.780 1.00 49.15 C ANISOU 2088 CG2 VAL A1075 2479 6783 9412 547 209 768 C ATOM 2089 N ARG A1076 83.973 180.512 319.194 1.00 51.38 N ANISOU 2089 N ARG A1076 2657 6756 10110 603 131 757 N ATOM 2090 CA ARG A1076 85.115 181.112 319.871 1.00 51.97 C ANISOU 2090 CA ARG A1076 2708 6706 10332 589 92 759 C ATOM 2091 C ARG A1076 84.828 181.294 321.354 1.00 66.90 C ANISOU 2091 C ARG A1076 4561 8620 12239 593 46 671 C ATOM 2092 O ARG A1076 85.697 181.044 322.197 1.00 67.56 O ANISOU 2092 O ARG A1076 4637 8658 12375 566 6 649 O ATOM 2093 CB ARG A1076 85.464 182.455 319.232 1.00 63.12 C ANISOU 2093 CB ARG A1076 4094 7994 11893 609 98 813 C ATOM 2094 CG ARG A1076 85.864 182.397 317.768 1.00 65.44 C ANISOU 2094 CG ARG A1076 4420 8253 12192 608 143 910 C ATOM 2095 CD ARG A1076 85.992 183.810 317.232 1.00 69.90 C ANISOU 2095 CD ARG A1076 4951 8707 12899 631 150 958 C ATOM 2096 NE ARG A1076 86.736 184.654 318.164 1.00 73.80 N ANISOU 2096 NE ARG A1076 5403 9083 13555 622 101 934 N ATOM 2097 CZ ARG A1076 86.598 185.973 318.255 1.00 75.50 C ANISOU 2097 CZ ARG A1076 5572 9208 13906 645 89 935 C ATOM 2098 NH1 ARG A1076 85.733 186.604 317.471 1.00 55.29 N ANISOU 2098 NH1 ARG A1076 3005 6669 11332 680 126 961 N ATOM 2099 NH2 ARG A1076 87.318 186.658 319.135 1.00 75.72 N ANISOU 2099 NH2 ARG A1076 5559 9123 14087 631 38 907 N ATOM 2100 N GLY A1077 83.612 181.731 321.690 1.00 66.40 N ANISOU 2100 N GLY A1077 4469 8628 12132 628 51 620 N ATOM 2101 CA GLY A1077 83.219 181.786 323.087 1.00 66.80 C ANISOU 2101 CA GLY A1077 4483 8719 12178 637 13 534 C ATOM 2102 C GLY A1077 83.337 180.439 323.777 1.00 65.66 C ANISOU 2102 C GLY A1077 4362 8668 11919 603 -1 501 C ATOM 2103 O GLY A1077 83.720 180.363 324.946 1.00 65.35 O ANISOU 2103 O GLY A1077 4298 8615 11916 591 -45 450 O ATOM 2104 N ILE A1078 83.020 179.359 323.059 1.00 51.35 N ANISOU 2104 N ILE A1078 2593 6945 9971 586 35 529 N ATOM 2105 CA ILE A1078 83.194 178.019 323.611 1.00 50.70 C ANISOU 2105 CA ILE A1078 2537 6942 9786 550 25 505 C ATOM 2106 C ILE A1078 84.673 177.693 323.748 1.00 50.67 C ANISOU 2106 C ILE A1078 2550 6841 9860 516 0 538 C ATOM 2107 O ILE A1078 85.152 177.314 324.824 1.00 63.52 O ANISOU 2107 O ILE A1078 4165 8470 11498 495 -39 499 O ATOM 2108 CB ILE A1078 82.483 176.975 322.737 1.00 49.90 C ANISOU 2108 CB ILE A1078 2475 6947 9537 540 67 526 C ATOM 2109 CG1 ILE A1078 80.993 177.266 322.658 1.00 70.37 C ANISOU 2109 CG1 ILE A1078 5044 9643 12050 572 88 493 C ATOM 2110 CG2 ILE A1078 82.690 175.591 323.311 1.00 49.30 C ANISOU 2110 CG2 ILE A1078 2423 6941 9366 502 58 503 C ATOM 2111 CD1 ILE A1078 80.242 176.237 321.859 1.00 69.98 C ANISOU 2111 CD1 ILE A1078 5028 9697 11865 556 122 505 C ATOM 2112 N LEU A1079 85.417 177.823 322.650 1.00 72.84 N ANISOU 2112 N LEU A1079 5385 9566 12723 509 24 613 N ATOM 2113 CA LEU A1079 86.839 177.512 322.683 1.00 76.88 C ANISOU 2113 CA LEU A1079 5913 9987 13312 479 6 654 C ATOM 2114 C LEU A1079 87.612 178.450 323.603 1.00 82.71 C ANISOU 2114 C LEU A1079 6606 10618 14203 476 -48 631 C ATOM 2115 O LEU A1079 88.700 178.087 324.063 1.00 86.99 O ANISOU 2115 O LEU A1079 7150 11107 14797 447 -79 642 O ATOM 2116 CB LEU A1079 87.421 177.546 321.265 1.00 75.40 C ANISOU 2116 CB LEU A1079 5758 9734 13157 479 46 745 C ATOM 2117 CG LEU A1079 87.502 176.236 320.460 1.00 49.61 C ANISOU 2117 CG LEU A1079 2544 6527 9779 463 85 784 C ATOM 2118 CD1 LEU A1079 86.830 175.060 321.164 1.00 49.02 C ANISOU 2118 CD1 LEU A1079 2483 6577 9567 447 79 723 C ATOM 2119 CD2 LEU A1079 86.926 176.422 319.058 1.00 49.52 C ANISOU 2119 CD2 LEU A1079 2548 6522 9744 484 136 840 C ATOM 2120 N ARG A1080 87.084 179.639 323.892 1.00 52.14 N ANISOU 2120 N ARG A1080 2691 6710 10409 504 -63 598 N ATOM 2121 CA ARG A1080 87.700 180.529 324.865 1.00 53.03 C ANISOU 2121 CA ARG A1080 2755 6721 10674 501 -122 561 C ATOM 2122 C ARG A1080 87.028 180.446 326.229 1.00 53.25 C ANISOU 2122 C ARG A1080 2749 6823 10662 510 -160 465 C ATOM 2123 O ARG A1080 87.226 181.337 327.062 1.00 69.23 O ANISOU 2123 O ARG A1080 4723 8770 12810 519 -209 416 O ATOM 2124 CB ARG A1080 87.694 181.972 324.358 1.00 53.84 C ANISOU 2124 CB ARG A1080 2825 6711 10921 527 -121 586 C ATOM 2125 N ASN A1081 86.241 179.399 326.477 1.00 52.55 N ANISOU 2125 N ASN A1081 2681 6876 10409 509 -139 436 N ATOM 2126 CA ASN A1081 85.589 179.202 327.764 1.00 66.46 C ANISOU 2126 CA ASN A1081 4410 8721 12120 518 -170 353 C ATOM 2127 C ASN A1081 86.371 178.194 328.590 1.00 65.23 C ANISOU 2127 C ASN A1081 4264 8588 11932 477 -206 337 C ATOM 2128 O ASN A1081 86.893 177.207 328.061 1.00 63.53 O ANISOU 2128 O ASN A1081 4095 8393 11652 448 -184 386 O ATOM 2129 CB ASN A1081 84.143 178.723 327.604 1.00 66.54 C ANISOU 2129 CB ASN A1081 4428 8882 11972 542 -127 331 C ATOM 2130 CG ASN A1081 83.274 179.082 328.798 1.00 52.78 C ANISOU 2130 CG ASN A1081 2635 7202 10217 573 -151 250 C ATOM 2131 OD1 ASN A1081 83.098 178.285 329.723 1.00 52.59 O ANISOU 2131 OD1 ASN A1081 2603 7265 10112 558 -170 209 O ATOM 2132 ND2 ASN A1081 82.729 180.295 328.784 1.00 53.51 N ANISOU 2132 ND2 ASN A1081 2689 7250 10393 618 -150 228 N ATOM 2133 N ALA A1082 86.437 178.450 329.896 1.00 66.23 N ANISOU 2133 N ALA A1082 4347 8711 12108 478 -262 267 N ATOM 2134 CA ALA A1082 87.230 177.615 330.787 1.00 67.06 C ANISOU 2134 CA ALA A1082 4452 8829 12197 440 -305 249 C ATOM 2135 C ALA A1082 86.682 176.196 330.880 1.00 66.76 C ANISOU 2135 C ALA A1082 4448 8939 11980 424 -273 251 C ATOM 2136 O ALA A1082 87.459 175.238 330.981 1.00 51.66 O ANISOU 2136 O ALA A1082 2562 7033 10033 388 -281 277 O ATOM 2137 CB ALA A1082 87.289 178.254 332.171 1.00 53.90 C ANISOU 2137 CB ALA A1082 2726 7133 10622 448 -375 164 C ATOM 2138 N LYS A1083 85.363 176.032 330.828 1.00 65.56 N ANISOU 2138 N LYS A1083 4293 8902 11715 450 -236 226 N ATOM 2139 CA LYS A1083 84.759 174.761 331.200 1.00 62.57 C ANISOU 2139 CA LYS A1083 3931 8665 11179 433 -219 213 C ATOM 2140 C LYS A1083 84.347 173.906 330.009 1.00 60.30 C ANISOU 2140 C LYS A1083 3698 8438 10777 422 -159 265 C ATOM 2141 O LYS A1083 84.571 172.692 330.030 1.00 58.78 O ANISOU 2141 O LYS A1083 3536 8299 10499 390 -150 279 O ATOM 2142 CB LYS A1083 83.545 175.006 332.103 1.00 62.19 C ANISOU 2142 CB LYS A1083 3836 8718 11075 466 -224 147 C ATOM 2143 CG LYS A1083 83.282 173.894 333.113 1.00 51.28 C ANISOU 2143 CG LYS A1083 2447 7454 9583 443 -238 116 C ATOM 2144 CD LYS A1083 82.151 174.260 334.072 1.00 51.81 C ANISOU 2144 CD LYS A1083 2459 7612 9614 482 -245 55 C ATOM 2145 CE LYS A1083 82.637 175.108 335.244 1.00 72.56 C ANISOU 2145 CE LYS A1083 5033 10165 12370 498 -312 -10 C ATOM 2146 NZ LYS A1083 82.994 176.505 334.865 1.00 73.48 N ANISOU 2146 NZ LYS A1083 5132 10141 12645 527 -328 -20 N ATOM 2147 N LEU A1084 83.746 174.491 328.972 1.00 59.90 N ANISOU 2147 N LEU A1084 3656 8377 10726 449 -119 291 N ATOM 2148 CA LEU A1084 83.197 173.701 327.876 1.00 49.45 C ANISOU 2148 CA LEU A1084 2377 7119 9292 440 -67 328 C ATOM 2149 C LEU A1084 84.147 173.560 326.697 1.00 57.34 C ANISOU 2149 C LEU A1084 3422 8023 10341 424 -46 399 C ATOM 2150 O LEU A1084 83.793 172.900 325.715 1.00 57.51 O ANISOU 2150 O LEU A1084 3482 8086 10284 416 -6 432 O ATOM 2151 CB LEU A1084 81.857 174.282 327.398 1.00 49.55 C ANISOU 2151 CB LEU A1084 2373 7198 9257 477 -35 316 C ATOM 2152 CG LEU A1084 81.574 175.783 327.393 1.00 58.91 C ANISOU 2152 CG LEU A1084 3518 8318 10546 523 -41 305 C ATOM 2153 CD1 LEU A1084 80.614 176.111 326.268 1.00 58.43 C ANISOU 2153 CD1 LEU A1084 3466 8296 10438 548 5 331 C ATOM 2154 CD2 LEU A1084 80.968 176.211 328.716 1.00 60.03 C ANISOU 2154 CD2 LEU A1084 3604 8511 10693 549 -70 237 C ATOM 2155 N LYS A1085 85.340 174.158 326.761 1.00 56.88 N ANISOU 2155 N LYS A1085 3358 7839 10414 419 -73 425 N ATOM 2156 CA LYS A1085 86.324 173.905 325.709 1.00 57.86 C ANISOU 2156 CA LYS A1085 3523 7879 10581 404 -52 499 C ATOM 2157 C LYS A1085 86.787 172.453 325.686 1.00 48.60 C ANISOU 2157 C LYS A1085 2389 6748 9328 371 -42 518 C ATOM 2158 O LYS A1085 86.750 171.835 324.606 1.00 48.08 O ANISOU 2158 O LYS A1085 2364 6691 9212 367 0 564 O ATOM 2159 CB LYS A1085 87.509 174.865 325.848 1.00 61.55 C ANISOU 2159 CB LYS A1085 3969 8205 11214 404 -85 524 C ATOM 2160 CG LYS A1085 88.672 174.488 324.935 1.00 65.16 C ANISOU 2160 CG LYS A1085 4463 8579 11716 386 -66 605 C ATOM 2161 CD LYS A1085 89.930 175.295 325.217 1.00 68.20 C ANISOU 2161 CD LYS A1085 4821 8828 12263 377 -105 631 C ATOM 2162 CE LYS A1085 91.112 174.764 324.413 1.00 50.20 C ANISOU 2162 CE LYS A1085 2575 6480 10019 360 -84 715 C ATOM 2163 NZ LYS A1085 90.852 174.758 322.944 1.00 49.85 N ANISOU 2163 NZ LYS A1085 2566 6430 9945 378 -24 779 N ATOM 2164 N PRO A1086 87.226 171.847 326.798 1.00 48.63 N ANISOU 2164 N PRO A1086 2382 6775 9320 348 -78 486 N ATOM 2165 CA PRO A1086 87.779 170.482 326.699 1.00 48.05 C ANISOU 2165 CA PRO A1086 2347 6725 9186 318 -66 513 C ATOM 2166 C PRO A1086 86.789 169.465 326.162 1.00 55.84 C ANISOU 2166 C PRO A1086 3364 7817 10037 311 -25 508 C ATOM 2167 O PRO A1086 87.123 168.687 325.260 1.00 56.59 O ANISOU 2167 O PRO A1086 3500 7895 10106 300 9 558 O ATOM 2168 CB PRO A1086 88.190 170.172 328.147 1.00 57.86 C ANISOU 2168 CB PRO A1086 3560 7989 10436 298 -118 468 C ATOM 2169 CG PRO A1086 87.330 171.055 328.986 1.00 57.92 C ANISOU 2169 CG PRO A1086 3518 8039 10450 319 -145 403 C ATOM 2170 CD PRO A1086 87.216 172.323 328.195 1.00 49.22 C ANISOU 2170 CD PRO A1086 2407 6858 9435 349 -132 424 C ATOM 2171 N VAL A1087 85.567 169.464 326.693 1.00 54.95 N ANISOU 2171 N VAL A1087 3228 7809 9842 317 -27 451 N ATOM 2172 CA VAL A1087 84.558 168.499 326.269 1.00 46.80 C ANISOU 2172 CA VAL A1087 2217 6880 8684 305 7 442 C ATOM 2173 C VAL A1087 84.268 168.651 324.782 1.00 72.47 C ANISOU 2173 C VAL A1087 5498 10105 11931 318 51 488 C ATOM 2174 O VAL A1087 84.234 167.665 324.036 1.00 72.45 O ANISOU 2174 O VAL A1087 5533 10120 11875 300 80 517 O ATOM 2175 CB VAL A1087 83.288 168.667 327.118 1.00 51.34 C ANISOU 2175 CB VAL A1087 2752 7569 9185 314 -3 376 C ATOM 2176 CG1 VAL A1087 83.098 170.134 327.446 1.00 51.89 C ANISOU 2176 CG1 VAL A1087 2779 7603 9334 352 -23 355 C ATOM 2177 CG2 VAL A1087 82.075 168.113 326.392 1.00 46.56 C ANISOU 2177 CG2 VAL A1087 2161 7055 8475 309 34 369 C ATOM 2178 N TYR A1088 84.062 169.893 324.331 1.00 46.94 N ANISOU 2178 N TYR A1088 2247 6828 8760 350 55 497 N ATOM 2179 CA TYR A1088 83.802 170.156 322.918 1.00 71.79 C ANISOU 2179 CA TYR A1088 5418 9950 11910 365 95 545 C ATOM 2180 C TYR A1088 84.871 169.518 322.033 1.00 72.90 C ANISOU 2180 C TYR A1088 5601 10014 12082 352 116 613 C ATOM 2181 O TYR A1088 84.554 168.841 321.047 1.00 74.26 O ANISOU 2181 O TYR A1088 5803 10209 12202 346 152 645 O ATOM 2182 CB TYR A1088 83.716 171.670 322.692 1.00 47.38 C ANISOU 2182 CB TYR A1088 2298 6798 8908 401 91 552 C ATOM 2183 CG TYR A1088 83.571 172.148 321.254 1.00 63.88 C ANISOU 2183 CG TYR A1088 4405 8845 11020 421 128 608 C ATOM 2184 CD1 TYR A1088 83.238 171.285 320.220 1.00 62.64 C ANISOU 2184 CD1 TYR A1088 4279 8719 10804 410 165 647 C ATOM 2185 CD2 TYR A1088 83.768 173.479 320.939 1.00 67.00 C ANISOU 2185 CD2 TYR A1088 4778 9160 11518 451 127 632 C ATOM 2186 CE1 TYR A1088 83.124 171.732 318.925 1.00 61.31 C ANISOU 2186 CE1 TYR A1088 4119 8506 10671 428 199 709 C ATOM 2187 CE2 TYR A1088 83.647 173.935 319.641 1.00 68.19 C ANISOU 2187 CE2 TYR A1088 4937 9264 11707 468 162 696 C ATOM 2188 CZ TYR A1088 83.323 173.054 318.637 1.00 65.18 C ANISOU 2188 CZ TYR A1088 4586 8920 11259 458 198 735 C ATOM 2189 OH TYR A1088 83.198 173.486 317.337 1.00 67.11 O ANISOU 2189 OH TYR A1088 4837 9125 11537 477 233 800 O ATOM 2190 N ASP A1089 86.145 169.709 322.377 1.00 70.21 N ANISOU 2190 N ASP A1089 5261 9581 11835 347 96 641 N ATOM 2191 CA ASP A1089 87.209 169.134 321.561 1.00 67.49 C ANISOU 2191 CA ASP A1089 4953 9164 11528 340 119 712 C ATOM 2192 C ASP A1089 87.068 167.622 321.420 1.00 62.69 C ANISOU 2192 C ASP A1089 4377 8615 10826 315 138 715 C ATOM 2193 O ASP A1089 87.429 167.062 320.379 1.00 53.96 O ANISOU 2193 O ASP A1089 3303 7478 9720 316 174 774 O ATOM 2194 CB ASP A1089 88.573 169.501 322.145 1.00 66.26 C ANISOU 2194 CB ASP A1089 4784 8908 11482 334 87 735 C ATOM 2195 CG ASP A1089 88.930 170.961 321.917 1.00 63.08 C ANISOU 2195 CG ASP A1089 4355 8415 11197 357 76 757 C ATOM 2196 OD1 ASP A1089 88.792 171.438 320.767 1.00 47.62 O ANISOU 2196 OD1 ASP A1089 2407 6420 9268 376 111 808 O ATOM 2197 OD2 ASP A1089 89.336 171.635 322.889 1.00 62.15 O ANISOU 2197 OD2 ASP A1089 4202 8257 11154 354 32 727 O ATOM 2198 N SER A1090 86.519 166.947 322.434 1.00 45.76 N ANISOU 2198 N SER A1090 2222 6557 8608 293 117 656 N ATOM 2199 CA SER A1090 86.363 165.497 322.357 1.00 52.74 C ANISOU 2199 CA SER A1090 3133 7493 9412 266 134 658 C ATOM 2200 C SER A1090 85.161 165.081 321.518 1.00 50.85 C ANISOU 2200 C SER A1090 2907 7328 9087 263 167 652 C ATOM 2201 O SER A1090 85.186 164.013 320.896 1.00 49.54 O ANISOU 2201 O SER A1090 2770 7170 8883 247 194 683 O ATOM 2202 CB SER A1090 86.240 164.904 323.762 1.00 54.36 C ANISOU 2202 CB SER A1090 3320 7761 9573 241 100 602 C ATOM 2203 OG SER A1090 85.227 165.555 324.511 1.00 55.60 O ANISOU 2203 OG SER A1090 3439 7993 9693 248 78 537 O ATOM 2204 N LEU A1091 84.113 165.899 321.483 1.00 45.12 N ANISOU 2204 N LEU A1091 2156 6653 8336 278 165 615 N ATOM 2205 CA LEU A1091 82.876 165.510 320.821 1.00 52.56 C ANISOU 2205 CA LEU A1091 3102 7675 9194 271 190 602 C ATOM 2206 C LEU A1091 83.039 165.475 319.307 1.00 52.23 C ANISOU 2206 C LEU A1091 3088 7586 9171 283 228 668 C ATOM 2207 O LEU A1091 83.627 166.379 318.705 1.00 45.09 O ANISOU 2207 O LEU A1091 2183 6600 8348 312 237 715 O ATOM 2208 CB LEU A1091 81.754 166.472 321.199 1.00 45.19 C ANISOU 2208 CB LEU A1091 2130 6806 8236 289 177 550 C ATOM 2209 CG LEU A1091 81.431 166.485 322.687 1.00 45.36 C ANISOU 2209 CG LEU A1091 2117 6890 8228 280 143 483 C ATOM 2210 CD1 LEU A1091 80.438 167.581 323.000 1.00 45.77 C ANISOU 2210 CD1 LEU A1091 2126 6992 8272 310 135 442 C ATOM 2211 CD2 LEU A1091 80.894 165.129 323.094 1.00 45.00 C ANISOU 2211 CD2 LEU A1091 2078 6927 8092 240 145 455 C ATOM 2212 N ASP A1092 82.492 164.426 318.695 1.00 44.47 N ANISOU 2212 N ASP A1092 2124 6650 8122 261 252 679 N ATOM 2213 CA ASP A1092 82.542 164.245 317.253 1.00 70.61 C ANISOU 2213 CA ASP A1092 5458 9930 11441 271 289 741 C ATOM 2214 C ASP A1092 81.697 165.309 316.547 1.00 71.53 C ANISOU 2214 C ASP A1092 5556 10066 11558 297 299 741 C ATOM 2215 O ASP A1092 80.962 166.074 317.175 1.00 72.07 O ANISOU 2215 O ASP A1092 5590 10175 11618 305 279 694 O ATOM 2216 CB ASP A1092 82.071 162.838 316.882 1.00 70.75 C ANISOU 2216 CB ASP A1092 5493 9998 11390 237 308 749 C ATOM 2217 CG ASP A1092 80.776 162.442 317.585 1.00 71.17 C ANISOU 2217 CG ASP A1092 5523 10157 11360 205 291 680 C ATOM 2218 OD1 ASP A1092 79.928 163.323 317.834 1.00 44.20 O ANISOU 2218 OD1 ASP A1092 2079 6788 7928 217 278 637 O ATOM 2219 OD2 ASP A1092 80.604 161.242 317.885 1.00 71.37 O ANISOU 2219 OD2 ASP A1092 5558 10218 11341 167 292 671 O ATOM 2220 N ALA A1093 81.798 165.338 315.214 1.00 44.67 N ANISOU 2220 N ALA A1093 2170 6632 8172 312 332 803 N ATOM 2221 CA ALA A1093 81.140 166.387 314.439 1.00 45.04 C ANISOU 2221 CA ALA A1093 2196 6679 8239 341 344 825 C ATOM 2222 C ALA A1093 79.637 166.415 314.687 1.00 45.06 C ANISOU 2222 C ALA A1093 2170 6785 8164 327 334 765 C ATOM 2223 O ALA A1093 79.026 167.490 314.716 1.00 45.45 O ANISOU 2223 O ALA A1093 2188 6845 8235 352 328 755 O ATOM 2224 CB ALA A1093 81.431 166.202 312.949 1.00 55.34 C ANISOU 2224 CB ALA A1093 3523 7949 9556 356 383 900 C ATOM 2225 N VAL A1094 79.024 165.246 314.874 1.00 44.71 N ANISOU 2225 N VAL A1094 2134 6815 8038 288 332 731 N ATOM 2226 CA VAL A1094 77.578 165.187 315.076 1.00 44.77 C ANISOU 2226 CA VAL A1094 2113 6921 7976 270 325 680 C ATOM 2227 C VAL A1094 77.200 165.821 316.410 1.00 44.95 C ANISOU 2227 C VAL A1094 2104 6981 7995 277 294 611 C ATOM 2228 O VAL A1094 76.450 166.802 316.462 1.00 45.34 O ANISOU 2228 O VAL A1094 2118 7055 8054 302 291 594 O ATOM 2229 CB VAL A1094 77.078 163.735 314.988 1.00 44.50 C ANISOU 2229 CB VAL A1094 2090 6941 7877 221 331 675 C ATOM 2230 CG1 VAL A1094 75.570 163.708 315.137 1.00 44.64 C ANISOU 2230 CG1 VAL A1094 2075 7052 7833 200 324 629 C ATOM 2231 CG2 VAL A1094 77.509 163.091 313.676 1.00 45.93 C ANISOU 2231 CG2 VAL A1094 2299 7085 8069 219 363 752 C ATOM 2232 N ARG A1095 77.723 165.267 317.508 1.00 72.49 N ANISOU 2232 N ARG A1095 5597 10471 11475 257 274 577 N ATOM 2233 CA ARG A1095 77.397 165.718 318.859 1.00 69.47 C ANISOU 2233 CA ARG A1095 5182 10133 11081 261 245 511 C ATOM 2234 C ARG A1095 77.889 167.129 319.159 1.00 66.12 C ANISOU 2234 C ARG A1095 4736 9651 10735 307 233 518 C ATOM 2235 O ARG A1095 77.534 167.677 320.208 1.00 45.63 O ANISOU 2235 O ARG A1095 2108 7097 8134 320 211 464 O ATOM 2236 CB ARG A1095 77.980 164.746 319.895 1.00 44.71 C ANISOU 2236 CB ARG A1095 2056 7003 7927 229 228 488 C ATOM 2237 CG ARG A1095 77.413 163.323 319.825 1.00 44.40 C ANISOU 2237 CG ARG A1095 2030 7020 7821 179 237 480 C ATOM 2238 CD ARG A1095 78.117 162.374 320.793 1.00 44.20 C ANISOU 2238 CD ARG A1095 2016 6989 7788 151 221 469 C ATOM 2239 NE ARG A1095 77.549 161.024 320.773 1.00 67.37 N ANISOU 2239 NE ARG A1095 4960 9971 10665 100 230 464 N ATOM 2240 CZ ARG A1095 77.967 160.036 319.986 1.00 68.76 C ANISOU 2240 CZ ARG A1095 5170 10112 10844 78 251 518 C ATOM 2241 NH1 ARG A1095 78.961 160.237 319.132 1.00 70.97 N ANISOU 2241 NH1 ARG A1095 5476 10310 11178 105 268 580 N ATOM 2242 NH2 ARG A1095 77.389 158.841 320.047 1.00 67.91 N ANISOU 2242 NH2 ARG A1095 5066 10048 10689 30 256 515 N ATOM 2243 N ARG A1096 78.698 167.724 318.284 1.00 64.05 N ANISOU 2243 N ARG A1096 4490 9294 10553 332 248 584 N ATOM 2244 CA ARG A1096 79.187 169.074 318.538 1.00 46.01 C ANISOU 2244 CA ARG A1096 2183 6940 8358 371 237 595 C ATOM 2245 C ARG A1096 78.081 170.098 318.373 1.00 46.44 C ANISOU 2245 C ARG A1096 2199 7036 8409 402 241 576 C ATOM 2246 O ARG A1096 77.979 171.046 319.159 1.00 47.20 O ANISOU 2246 O ARG A1096 2264 7131 8540 428 221 542 O ATOM 2247 CB ARG A1096 80.333 169.405 317.596 1.00 46.10 C ANISOU 2247 CB ARG A1096 2220 6836 8460 387 254 675 C ATOM 2248 CG ARG A1096 81.647 168.850 318.023 1.00 45.90 C ANISOU 2248 CG ARG A1096 2220 6746 8475 371 244 692 C ATOM 2249 CD ARG A1096 82.666 169.142 316.970 1.00 46.04 C ANISOU 2249 CD ARG A1096 2259 6656 8577 387 268 777 C ATOM 2250 NE ARG A1096 83.986 168.695 317.374 1.00 71.91 N ANISOU 2250 NE ARG A1096 5556 9864 11904 375 258 799 N ATOM 2251 CZ ARG A1096 85.108 169.171 316.857 1.00 66.27 C ANISOU 2251 CZ ARG A1096 4850 9042 11289 390 268 866 C ATOM 2252 NH1 ARG A1096 85.054 170.120 315.932 1.00 62.01 N ANISOU 2252 NH1 ARG A1096 4301 8453 10808 418 289 916 N ATOM 2253 NH2 ARG A1096 86.281 168.707 317.267 1.00 64.77 N ANISOU 2253 NH2 ARG A1096 4673 8794 11141 378 258 886 N ATOM 2254 N ALA A1097 77.256 169.933 317.339 1.00 46.41 N ANISOU 2254 N ALA A1097 2197 7069 8367 400 265 600 N ATOM 2255 CA ALA A1097 76.248 170.938 317.033 1.00 61.53 C ANISOU 2255 CA ALA A1097 4075 9016 10287 433 273 594 C ATOM 2256 C ALA A1097 75.278 171.127 318.188 1.00 47.05 C ANISOU 2256 C ALA A1097 2201 7274 8400 437 253 515 C ATOM 2257 O ALA A1097 74.731 172.220 318.368 1.00 68.62 O ANISOU 2257 O ALA A1097 4895 10016 11160 476 251 500 O ATOM 2258 CB ALA A1097 75.496 170.556 315.759 1.00 61.90 C ANISOU 2258 CB ALA A1097 4131 9097 10293 424 300 632 C ATOM 2259 N ALA A1098 75.067 170.089 318.993 1.00 46.69 N ANISOU 2259 N ALA A1098 2160 7297 8282 400 239 464 N ATOM 2260 CA ALA A1098 74.162 170.221 320.124 1.00 46.89 C ANISOU 2260 CA ALA A1098 2144 7416 8255 405 223 389 C ATOM 2261 C ALA A1098 74.773 171.035 321.256 1.00 47.18 C ANISOU 2261 C ALA A1098 2160 7428 8337 436 197 359 C ATOM 2262 O ALA A1098 74.052 171.765 321.944 1.00 47.62 O ANISOU 2262 O ALA A1098 2172 7537 8385 468 190 317 O ATOM 2263 CB ALA A1098 73.743 168.845 320.623 1.00 46.46 C ANISOU 2263 CB ALA A1098 2099 7438 8115 354 218 346 C ATOM 2264 N LEU A1099 76.084 170.916 321.477 1.00 67.21 N ANISOU 2264 N LEU A1099 4725 9882 10928 428 184 384 N ATOM 2265 CA LEU A1099 76.759 171.883 322.335 1.00 65.27 C ANISOU 2265 CA LEU A1099 4456 9579 10763 459 160 376 C ATOM 2266 C LEU A1099 76.573 173.288 321.785 1.00 61.81 C ANISOU 2266 C LEU A1099 3997 9089 10400 507 169 399 C ATOM 2267 O LEU A1099 76.311 174.234 322.538 1.00 61.17 O ANISOU 2267 O LEU A1099 3873 9009 10360 543 156 371 O ATOM 2268 CB LEU A1099 78.247 171.545 322.450 1.00 47.25 C ANISOU 2268 CB LEU A1099 2208 7199 8546 438 146 409 C ATOM 2269 CG LEU A1099 78.961 171.756 323.789 1.00 47.54 C ANISOU 2269 CG LEU A1099 2223 7208 8632 439 109 381 C ATOM 2270 CD1 LEU A1099 78.579 173.070 324.456 1.00 48.27 C ANISOU 2270 CD1 LEU A1099 2264 7293 8783 484 93 352 C ATOM 2271 CD2 LEU A1099 78.695 170.588 324.715 1.00 55.99 C ANISOU 2271 CD2 LEU A1099 3291 8370 9613 405 96 338 C ATOM 2272 N ILE A1100 76.692 173.435 320.463 1.00 59.88 N ANISOU 2272 N ILE A1100 3775 8789 10188 509 195 460 N ATOM 2273 CA ILE A1100 76.387 174.704 319.816 1.00 59.68 C ANISOU 2273 CA ILE A1100 3728 8718 10231 553 209 490 C ATOM 2274 C ILE A1100 74.908 175.030 319.961 1.00 48.76 C ANISOU 2274 C ILE A1100 2303 7440 8782 577 218 448 C ATOM 2275 O ILE A1100 74.513 176.202 319.930 1.00 50.74 O ANISOU 2275 O ILE A1100 2522 7675 9082 623 221 448 O ATOM 2276 CB ILE A1100 76.827 174.649 318.337 1.00 48.37 C ANISOU 2276 CB ILE A1100 2327 7210 8843 547 238 573 C ATOM 2277 CG1 ILE A1100 78.346 174.463 318.248 1.00 48.21 C ANISOU 2277 CG1 ILE A1100 2340 7079 8899 530 231 617 C ATOM 2278 CG2 ILE A1100 76.401 175.902 317.593 1.00 54.00 C ANISOU 2278 CG2 ILE A1100 3015 7885 9618 590 255 609 C ATOM 2279 CD1 ILE A1100 78.887 174.446 316.831 1.00 59.50 C ANISOU 2279 CD1 ILE A1100 3798 8433 10376 530 262 704 C ATOM 2280 N ASN A1101 74.070 174.012 320.152 1.00 48.42 N ANISOU 2280 N ASN A1101 2259 7503 8635 547 221 411 N ATOM 2281 CA ASN A1101 72.643 174.258 320.310 1.00 58.48 C ANISOU 2281 CA ASN A1101 3491 8879 9850 567 229 370 C ATOM 2282 C ASN A1101 72.319 174.763 321.710 1.00 57.80 C ANISOU 2282 C ASN A1101 3361 8848 9754 598 209 306 C ATOM 2283 O ASN A1101 71.626 175.773 321.871 1.00 59.47 O ANISOU 2283 O ASN A1101 3529 9077 9989 649 215 293 O ATOM 2284 CB ASN A1101 71.860 172.985 320.004 1.00 59.87 C ANISOU 2284 CB ASN A1101 3678 9137 9934 518 239 354 C ATOM 2285 CG ASN A1101 70.489 173.273 319.456 1.00 62.19 C ANISOU 2285 CG ASN A1101 3938 9494 10198 533 257 349 C ATOM 2286 OD1 ASN A1101 70.106 174.431 319.298 1.00 65.49 O ANISOU 2286 OD1 ASN A1101 4324 9900 10659 583 264 358 O ATOM 2287 ND2 ASN A1101 69.743 172.225 319.143 1.00 61.07 N ANISOU 2287 ND2 ASN A1101 3802 9411 9991 487 265 338 N ATOM 2288 N MET A1102 72.813 174.074 322.736 1.00 55.89 N ANISOU 2288 N MET A1102 3122 8623 9489 573 188 276 N ATOM 2289 CA MET A1102 72.570 174.530 324.098 1.00 49.43 C ANISOU 2289 CA MET A1102 2256 7849 8676 605 170 229 C ATOM 2290 C MET A1102 73.190 175.899 324.337 1.00 83.41 C ANISOU 2290 C MET A1102 6539 12052 13100 656 159 248 C ATOM 2291 O MET A1102 72.589 176.751 325.002 1.00 84.50 O ANISOU 2291 O MET A1102 6627 12218 13260 707 158 221 O ATOM 2292 CB MET A1102 73.116 173.512 325.088 1.00 49.09 C ANISOU 2292 CB MET A1102 2223 7834 8595 564 147 203 C ATOM 2293 CG MET A1102 72.666 172.110 324.806 1.00 48.47 C ANISOU 2293 CG MET A1102 2170 7828 8420 507 157 187 C ATOM 2294 SD MET A1102 72.946 171.131 326.267 1.00 48.34 S ANISOU 2294 SD MET A1102 2142 7872 8353 475 131 143 S ATOM 2295 CE MET A1102 72.808 169.483 325.615 1.00 61.60 C ANISOU 2295 CE MET A1102 3869 9575 9960 400 144 144 C ATOM 2296 N VAL A1103 74.392 176.130 323.799 1.00 49.92 N ANISOU 2296 N VAL A1103 2334 7686 8946 643 153 295 N ATOM 2297 CA VAL A1103 75.022 177.442 323.926 1.00 50.57 C ANISOU 2297 CA VAL A1103 2398 7652 9164 683 141 312 C ATOM 2298 C VAL A1103 74.173 178.503 323.242 1.00 51.08 C ANISOU 2298 C VAL A1103 2436 7716 9255 734 166 326 C ATOM 2299 O VAL A1103 74.057 179.635 323.726 1.00 68.48 O ANISOU 2299 O VAL A1103 4599 9875 11544 784 160 313 O ATOM 2300 CB VAL A1103 76.452 177.408 323.360 1.00 50.31 C ANISOU 2300 CB VAL A1103 2409 7487 9219 654 133 362 C ATOM 2301 CG1 VAL A1103 76.978 178.816 323.151 1.00 59.08 C ANISOU 2301 CG1 VAL A1103 3502 8469 10477 691 127 388 C ATOM 2302 CG2 VAL A1103 77.361 176.648 324.295 1.00 56.19 C ANISOU 2302 CG2 VAL A1103 3167 8216 9967 617 101 342 C ATOM 2303 N PHE A1104 73.565 178.153 322.106 1.00 50.72 N ANISOU 2303 N PHE A1104 2411 7715 9145 722 193 353 N ATOM 2304 CA PHE A1104 72.588 179.042 321.487 1.00 51.21 C ANISOU 2304 CA PHE A1104 2443 7799 9215 768 217 364 C ATOM 2305 C PHE A1104 71.374 179.231 322.386 1.00 51.67 C ANISOU 2305 C PHE A1104 2447 7970 9216 805 219 306 C ATOM 2306 O PHE A1104 70.761 180.304 322.400 1.00 52.39 O ANISOU 2306 O PHE A1104 2497 8056 9351 863 230 303 O ATOM 2307 CB PHE A1104 72.148 178.486 320.132 1.00 65.42 C ANISOU 2307 CB PHE A1104 4274 9630 10952 741 242 401 C ATOM 2308 CG PHE A1104 72.822 179.127 318.945 1.00 64.43 C ANISOU 2308 CG PHE A1104 4171 9387 10923 748 257 479 C ATOM 2309 CD1 PHE A1104 73.535 178.355 318.042 1.00 50.38 C ANISOU 2309 CD1 PHE A1104 2437 7558 9149 705 267 536 C ATOM 2310 CD2 PHE A1104 72.725 180.492 318.719 1.00 64.18 C ANISOU 2310 CD2 PHE A1104 4112 9295 10980 801 264 499 C ATOM 2311 CE1 PHE A1104 74.147 178.928 316.945 1.00 50.57 C ANISOU 2311 CE1 PHE A1104 2477 7478 9259 714 284 613 C ATOM 2312 CE2 PHE A1104 73.338 181.071 317.619 1.00 51.75 C ANISOU 2312 CE2 PHE A1104 2554 7611 9497 806 281 576 C ATOM 2313 CZ PHE A1104 74.046 180.285 316.732 1.00 51.25 C ANISOU 2313 CZ PHE A1104 2535 7505 9434 762 291 634 C ATOM 2314 N GLN A1105 71.005 178.193 323.134 1.00 74.69 N ANISOU 2314 N GLN A1105 5357 10986 12034 774 210 260 N ATOM 2315 CA GLN A1105 69.795 178.254 323.941 1.00 75.55 C ANISOU 2315 CA GLN A1105 5412 11214 12079 807 215 206 C ATOM 2316 C GLN A1105 69.987 179.154 325.153 1.00 80.46 C ANISOU 2316 C GLN A1105 5989 11810 12772 864 201 182 C ATOM 2317 O GLN A1105 69.282 180.155 325.319 1.00 82.65 O ANISOU 2317 O GLN A1105 6221 12099 13084 929 215 172 O ATOM 2318 CB GLN A1105 69.400 176.855 324.391 1.00 71.43 C ANISOU 2318 CB GLN A1105 4898 10798 11445 753 210 165 C ATOM 2319 CG GLN A1105 68.249 176.875 325.359 1.00 71.27 C ANISOU 2319 CG GLN A1105 4818 10897 11366 784 215 105 C ATOM 2320 CD GLN A1105 67.562 175.546 325.478 1.00 70.85 C ANISOU 2320 CD GLN A1105 4768 10938 11213 725 217 60 C ATOM 2321 OE1 GLN A1105 68.146 174.501 325.187 1.00 67.63 O ANISOU 2321 OE1 GLN A1105 4409 10509 10780 661 209 71 O ATOM 2322 NE2 GLN A1105 66.308 175.571 325.902 1.00 75.44 N ANISOU 2322 NE2 GLN A1105 5298 11611 11756 746 230 6 N ATOM 2323 N MET A1106 70.960 178.822 326.003 1.00 52.40 N ANISOU 2323 N MET A1106 2447 8212 9250 841 173 173 N ATOM 2324 CA MET A1106 71.103 179.443 327.311 1.00 53.12 C ANISOU 2324 CA MET A1106 2493 8286 9403 886 155 139 C ATOM 2325 C MET A1106 72.387 180.246 327.496 1.00 53.46 C ANISOU 2325 C MET A1106 2547 8162 9605 892 128 152 C ATOM 2326 O MET A1106 72.594 180.803 328.580 1.00 82.03 O ANISOU 2326 O MET A1106 6127 11741 13299 927 106 114 O ATOM 2327 CB MET A1106 71.011 178.352 328.386 1.00 52.83 C ANISOU 2327 CB MET A1106 2447 8352 9275 855 140 103 C ATOM 2328 CG MET A1106 71.147 176.940 327.805 1.00 51.84 C ANISOU 2328 CG MET A1106 2371 8278 9047 777 141 113 C ATOM 2329 SD MET A1106 70.615 175.609 328.902 1.00 75.44 S ANISOU 2329 SD MET A1106 5341 11416 11907 741 134 66 S ATOM 2330 CE MET A1106 71.115 174.157 327.989 1.00 50.46 C ANISOU 2330 CE MET A1106 2249 8242 8682 649 134 82 C ATOM 2331 N GLY A1107 73.248 180.333 326.484 1.00 53.09 N ANISOU 2331 N GLY A1107 2546 8010 9617 860 126 199 N ATOM 2332 CA GLY A1107 74.514 181.024 326.643 1.00 53.43 C ANISOU 2332 CA GLY A1107 2596 7891 9814 856 97 208 C ATOM 2333 C GLY A1107 75.526 180.176 327.384 1.00 69.08 C ANISOU 2333 C GLY A1107 4599 9851 11798 804 61 193 C ATOM 2334 O GLY A1107 75.150 179.397 328.265 1.00 68.12 O ANISOU 2334 O GLY A1107 4464 9833 11587 793 53 157 O ATOM 2335 N GLU A1108 76.809 180.326 327.040 1.00 69.58 N ANISOU 2335 N GLU A1108 4692 9781 11965 772 40 223 N ATOM 2336 CA GLU A1108 77.851 179.475 327.614 1.00 68.60 C ANISOU 2336 CA GLU A1108 4592 9631 11843 720 6 216 C ATOM 2337 C GLU A1108 77.828 179.518 329.135 1.00 68.10 C ANISOU 2337 C GLU A1108 4484 9590 11802 733 -31 149 C ATOM 2338 O GLU A1108 77.896 178.475 329.798 1.00 52.66 O ANISOU 2338 O GLU A1108 2536 7714 9760 700 -44 130 O ATOM 2339 CB GLU A1108 79.219 179.899 327.092 1.00 52.62 C ANISOU 2339 CB GLU A1108 2593 7448 9953 695 -12 257 C ATOM 2340 CG GLU A1108 79.229 180.189 325.619 1.00 81.20 C ANISOU 2340 CG GLU A1108 6244 11026 13583 696 25 324 C ATOM 2341 CD GLU A1108 80.092 181.383 325.286 1.00 82.27 C ANISOU 2341 CD GLU A1108 6368 10997 13895 708 10 353 C ATOM 2342 OE1 GLU A1108 81.215 181.473 325.831 1.00 80.03 O ANISOU 2342 OE1 GLU A1108 6080 10615 13711 683 -30 346 O ATOM 2343 OE2 GLU A1108 79.639 182.240 324.494 1.00 83.81 O ANISOU 2343 OE2 GLU A1108 6554 11161 14130 742 37 383 O ATOM 2344 N THR A1109 77.728 180.720 329.705 1.00 54.05 N ANISOU 2344 N THR A1109 2655 7737 10143 782 -50 108 N ATOM 2345 CA THR A1109 77.686 180.850 331.155 1.00 64.09 C ANISOU 2345 CA THR A1109 3880 9020 11451 802 -89 34 C ATOM 2346 C THR A1109 76.599 179.971 331.773 1.00 66.86 C ANISOU 2346 C THR A1109 4215 9549 11641 811 -67 13 C ATOM 2347 O THR A1109 76.764 179.476 332.894 1.00 54.53 O ANISOU 2347 O THR A1109 2633 8025 10061 800 -99 -30 O ATOM 2348 CB THR A1109 77.489 182.323 331.525 1.00 61.90 C ANISOU 2348 CB THR A1109 3552 8644 11324 866 -104 -13 C ATOM 2349 OG1 THR A1109 76.193 182.762 331.096 1.00 59.13 O ANISOU 2349 OG1 THR A1109 3182 8374 10912 924 -53 -3 O ATOM 2350 CG2 THR A1109 78.547 183.178 330.836 1.00 62.65 C ANISOU 2350 CG2 THR A1109 3660 8562 11581 851 -124 17 C ATOM 2351 N GLY A1110 75.510 179.729 331.046 1.00 54.04 N ANISOU 2351 N GLY A1110 2598 8036 9899 827 -17 45 N ATOM 2352 CA GLY A1110 74.434 178.896 331.547 1.00 53.81 C ANISOU 2352 CA GLY A1110 2550 8178 9717 832 5 31 C ATOM 2353 C GLY A1110 74.651 177.409 331.343 1.00 67.40 C ANISOU 2353 C GLY A1110 4315 9981 11312 762 7 56 C ATOM 2354 O GLY A1110 74.452 176.619 332.271 1.00 52.73 O ANISOU 2354 O GLY A1110 2440 8215 9380 746 -4 33 O ATOM 2355 N VAL A1111 75.048 177.014 330.128 1.00 67.19 N ANISOU 2355 N VAL A1111 4344 9920 11267 722 23 101 N ATOM 2356 CA VAL A1111 75.297 175.604 329.847 1.00 66.62 C ANISOU 2356 CA VAL A1111 4317 9907 11090 657 26 119 C ATOM 2357 C VAL A1111 76.528 175.098 330.592 1.00 66.29 C ANISOU 2357 C VAL A1111 4290 9802 11095 618 -15 113 C ATOM 2358 O VAL A1111 76.582 173.919 330.962 1.00 66.11 O ANISOU 2358 O VAL A1111 4283 9854 10983 575 -19 108 O ATOM 2359 CB VAL A1111 75.391 175.361 328.324 1.00 50.59 C ANISOU 2359 CB VAL A1111 2338 7843 9039 632 54 166 C ATOM 2360 CG1 VAL A1111 75.997 176.541 327.626 1.00 50.96 C ANISOU 2360 CG1 VAL A1111 2392 7752 9218 659 54 198 C ATOM 2361 CG2 VAL A1111 76.192 174.111 327.994 1.00 49.77 C ANISOU 2361 CG2 VAL A1111 2290 7728 8894 567 49 188 C ATOM 2362 N ALA A1112 77.491 175.970 330.895 1.00 66.28 N ANISOU 2362 N ALA A1112 4278 9666 11238 630 -48 107 N ATOM 2363 CA ALA A1112 78.590 175.587 331.776 1.00 66.73 C ANISOU 2363 CA ALA A1112 4338 9670 11348 597 -95 89 C ATOM 2364 C ALA A1112 78.127 175.050 333.129 1.00 51.89 C ANISOU 2364 C ALA A1112 2418 7896 9403 599 -115 43 C ATOM 2365 O ALA A1112 78.959 174.528 333.875 1.00 51.87 O ANISOU 2365 O ALA A1112 2417 7871 9420 566 -154 29 O ATOM 2366 CB ALA A1112 79.521 176.780 332.005 1.00 68.51 C ANISOU 2366 CB ALA A1112 4543 9736 11753 615 -135 74 C ATOM 2367 N GLY A1113 76.839 175.137 333.464 1.00 52.15 N ANISOU 2367 N GLY A1113 2412 8045 9356 638 -89 23 N ATOM 2368 CA GLY A1113 76.405 174.671 334.771 1.00 52.45 C ANISOU 2368 CA GLY A1113 2408 8183 9339 644 -105 -13 C ATOM 2369 C GLY A1113 76.341 173.157 334.875 1.00 58.59 C ANISOU 2369 C GLY A1113 3211 9070 9981 586 -97 7 C ATOM 2370 O GLY A1113 76.602 172.588 335.941 1.00 58.46 O ANISOU 2370 O GLY A1113 3175 9092 9946 568 -126 -11 O ATOM 2371 N PHE A1114 75.981 172.481 333.778 1.00 58.02 N ANISOU 2371 N PHE A1114 3183 9044 9819 557 -60 39 N ATOM 2372 CA PHE A1114 75.772 171.029 333.796 1.00 50.24 C ANISOU 2372 CA PHE A1114 2221 8159 8709 502 -50 43 C ATOM 2373 C PHE A1114 77.120 170.319 333.706 1.00 60.27 C ANISOU 2373 C PHE A1114 3540 9344 10016 450 -75 62 C ATOM 2374 O PHE A1114 77.413 169.600 332.752 1.00 59.52 O ANISOU 2374 O PHE A1114 3498 9225 9890 412 -56 87 O ATOM 2375 CB PHE A1114 74.892 170.532 332.652 1.00 49.68 C ANISOU 2375 CB PHE A1114 2178 8151 8548 486 -7 49 C ATOM 2376 CG PHE A1114 73.744 171.430 332.269 1.00 79.21 C ANISOU 2376 CG PHE A1114 5883 11936 12278 539 22 39 C ATOM 2377 CD1 PHE A1114 73.201 172.370 333.135 1.00 79.59 C ANISOU 2377 CD1 PHE A1114 5868 12016 12355 601 19 24 C ATOM 2378 CD2 PHE A1114 73.178 171.284 331.017 1.00 49.70 C ANISOU 2378 CD2 PHE A1114 2174 8205 8503 526 53 45 C ATOM 2379 CE1 PHE A1114 72.141 173.160 332.735 1.00 80.57 C ANISOU 2379 CE1 PHE A1114 5962 12183 12469 653 49 17 C ATOM 2380 CE2 PHE A1114 72.125 172.059 330.619 1.00 50.09 C ANISOU 2380 CE2 PHE A1114 2192 8296 8543 572 78 34 C ATOM 2381 CZ PHE A1114 71.602 172.998 331.473 1.00 50.91 C ANISOU 2381 CZ PHE A1114 2235 8438 8671 637 77 20 C ATOM 2382 N THR A1115 77.942 170.522 334.735 1.00 60.66 N ANISOU 2382 N THR A1115 3567 9344 10138 451 -120 47 N ATOM 2383 CA THR A1115 79.278 169.935 334.740 1.00 49.86 C ANISOU 2383 CA THR A1115 2238 7892 8814 406 -148 64 C ATOM 2384 C THR A1115 79.219 168.408 334.692 1.00 50.20 C ANISOU 2384 C THR A1115 2313 8017 8745 354 -134 75 C ATOM 2385 O THR A1115 79.844 167.778 333.831 1.00 49.91 O ANISOU 2385 O THR A1115 2331 7925 8708 320 -120 106 O ATOM 2386 CB THR A1115 80.038 170.417 335.969 1.00 50.56 C ANISOU 2386 CB THR A1115 2288 7926 8997 415 -206 33 C ATOM 2387 OG1 THR A1115 79.392 169.919 337.145 1.00 50.84 O ANISOU 2387 OG1 THR A1115 2278 8081 8957 417 -218 5 O ATOM 2388 CG2 THR A1115 80.027 171.934 336.016 1.00 51.34 C ANISOU 2388 CG2 THR A1115 2353 7934 9221 466 -222 6 C ATOM 2389 N ASN A1116 78.458 167.793 335.602 1.00 49.27 N ANISOU 2389 N ASN A1116 2159 8026 8536 348 -135 50 N ATOM 2390 CA ASN A1116 78.398 166.333 335.637 1.00 48.69 C ANISOU 2390 CA ASN A1116 2111 8020 8368 296 -124 49 C ATOM 2391 C ASN A1116 77.827 165.756 334.353 1.00 48.03 C ANISOU 2391 C ASN A1116 2074 7947 8229 273 -79 55 C ATOM 2392 O ASN A1116 78.243 164.677 333.923 1.00 54.65 O ANISOU 2392 O ASN A1116 2957 8762 9045 227 -70 68 O ATOM 2393 CB ASN A1116 77.584 165.863 336.834 1.00 49.03 C ANISOU 2393 CB ASN A1116 2100 8201 8328 296 -132 19 C ATOM 2394 CG ASN A1116 78.397 165.842 338.098 1.00 49.49 C ANISOU 2394 CG ASN A1116 2128 8246 8430 293 -182 19 C ATOM 2395 OD1 ASN A1116 78.618 166.877 338.723 1.00 50.18 O ANISOU 2395 OD1 ASN A1116 2177 8288 8602 332 -213 12 O ATOM 2396 ND2 ASN A1116 78.869 164.660 338.477 1.00 65.66 N ANISOU 2396 ND2 ASN A1116 4194 10320 10435 245 -194 18 N ATOM 2397 N SER A1117 76.876 166.446 333.731 1.00 76.46 N ANISOU 2397 N SER A1117 5661 11575 11815 304 -51 48 N ATOM 2398 CA SER A1117 76.453 166.057 332.395 1.00 75.46 C ANISOU 2398 CA SER A1117 5579 11431 11662 284 -14 57 C ATOM 2399 C SER A1117 77.413 166.543 331.323 1.00 47.36 C ANISOU 2399 C SER A1117 2068 7741 8187 290 -10 109 C ATOM 2400 O SER A1117 77.345 166.057 330.189 1.00 46.87 O ANISOU 2400 O SER A1117 2050 7649 8111 268 17 132 O ATOM 2401 CB SER A1117 75.049 166.584 332.105 1.00 75.55 C ANISOU 2401 CB SER A1117 5556 11521 11630 313 12 26 C ATOM 2402 OG SER A1117 74.119 166.076 333.044 1.00 76.63 O ANISOU 2402 OG SER A1117 5669 11753 11693 303 12 -25 O ATOM 2403 N LEU A1118 78.291 167.492 331.648 1.00 47.77 N ANISOU 2403 N LEU A1118 2108 7707 8334 319 -36 125 N ATOM 2404 CA LEU A1118 79.292 167.931 330.684 1.00 47.60 C ANISOU 2404 CA LEU A1118 2129 7554 8403 322 -33 171 C ATOM 2405 C LEU A1118 80.416 166.915 330.573 1.00 47.14 C ANISOU 2405 C LEU A1118 2115 7439 8358 280 -41 201 C ATOM 2406 O LEU A1118 80.751 166.467 329.472 1.00 60.33 O ANISOU 2406 O LEU A1118 3832 9057 10032 263 -15 241 O ATOM 2407 CB LEU A1118 79.858 169.299 331.077 1.00 48.27 C ANISOU 2407 CB LEU A1118 2183 7552 8605 362 -61 171 C ATOM 2408 CG LEU A1118 79.781 170.447 330.068 1.00 48.47 C ANISOU 2408 CG LEU A1118 2214 7499 8702 397 -43 195 C ATOM 2409 CD1 LEU A1118 79.891 169.911 328.663 1.00 47.83 C ANISOU 2409 CD1 LEU A1118 2188 7389 8597 376 -6 240 C ATOM 2410 CD2 LEU A1118 78.510 171.265 330.232 1.00 48.93 C ANISOU 2410 CD2 LEU A1118 2226 7630 8735 442 -29 165 C ATOM 2411 N ARG A1119 81.011 166.541 331.706 1.00 47.33 N ANISOU 2411 N ARG A1119 2121 7472 8391 264 -76 185 N ATOM 2412 CA ARG A1119 82.169 165.660 331.648 1.00 46.99 C ANISOU 2412 CA ARG A1119 2116 7366 8372 230 -85 216 C ATOM 2413 C ARG A1119 81.786 164.259 331.201 1.00 69.02 C ANISOU 2413 C ARG A1119 4941 10209 11074 191 -55 224 C ATOM 2414 O ARG A1119 82.607 163.566 330.592 1.00 60.74 O ANISOU 2414 O ARG A1119 3937 9093 10049 170 -44 267 O ATOM 2415 CB ARG A1119 82.888 165.615 333.002 1.00 60.69 C ANISOU 2415 CB ARG A1119 3818 9099 10141 223 -135 196 C ATOM 2416 CG ARG A1119 82.117 164.927 334.127 1.00 61.44 C ANISOU 2416 CG ARG A1119 3877 9323 10143 208 -146 153 C ATOM 2417 CD ARG A1119 82.960 164.747 335.398 1.00 47.91 C ANISOU 2417 CD ARG A1119 2136 7604 8465 196 -198 140 C ATOM 2418 NE ARG A1119 82.203 164.104 336.475 1.00 65.86 N ANISOU 2418 NE ARG A1119 4371 10005 10648 185 -208 104 N ATOM 2419 CZ ARG A1119 82.166 162.790 336.692 1.00 67.39 C ANISOU 2419 CZ ARG A1119 4581 10252 10772 145 -199 103 C ATOM 2420 NH1 ARG A1119 81.445 162.299 337.694 1.00 47.91 N ANISOU 2420 NH1 ARG A1119 2073 7901 8230 137 -208 68 N ATOM 2421 NH2 ARG A1119 82.850 161.962 335.912 1.00 68.76 N ANISOU 2421 NH2 ARG A1119 4810 10358 10957 116 -180 140 N ATOM 2422 N MET A1120 80.553 163.823 331.474 1.00 46.31 N ANISOU 2422 N MET A1120 2045 7446 8106 181 -42 185 N ATOM 2423 CA MET A1120 80.159 162.489 331.040 1.00 45.80 C ANISOU 2423 CA MET A1120 2012 7416 7974 139 -15 189 C ATOM 2424 C MET A1120 80.263 162.351 329.530 1.00 57.04 C ANISOU 2424 C MET A1120 3485 8773 9416 135 20 236 C ATOM 2425 O MET A1120 80.637 161.288 329.026 1.00 55.72 O ANISOU 2425 O MET A1120 3357 8574 9240 104 36 268 O ATOM 2426 CB MET A1120 78.749 162.173 331.525 1.00 45.91 C ANISOU 2426 CB MET A1120 1990 7550 7903 128 -6 133 C ATOM 2427 CG MET A1120 78.728 161.739 332.977 1.00 92.52 C ANISOU 2427 CG MET A1120 7853 13524 13775 116 -35 93 C ATOM 2428 SD MET A1120 77.097 161.688 333.748 1.00 90.86 S ANISOU 2428 SD MET A1120 7585 13450 13488 117 -28 16 S ATOM 2429 CE MET A1120 77.485 160.757 335.238 1.00 93.41 C ANISOU 2429 CE MET A1120 7889 13813 13789 88 -59 -10 C ATOM 2430 N LEU A1121 79.977 163.424 328.796 1.00 58.02 N ANISOU 2430 N LEU A1121 3605 8870 9571 170 32 245 N ATOM 2431 CA LEU A1121 80.208 163.423 327.356 1.00 45.21 C ANISOU 2431 CA LEU A1121 2025 7177 7976 173 63 296 C ATOM 2432 C LEU A1121 81.693 163.357 327.046 1.00 49.69 C ANISOU 2432 C LEU A1121 2625 7631 8623 175 58 351 C ATOM 2433 O LEU A1121 82.129 162.571 326.196 1.00 48.87 O ANISOU 2433 O LEU A1121 2563 7483 8524 158 82 397 O ATOM 2434 CB LEU A1121 79.594 164.672 326.743 1.00 45.48 C ANISOU 2434 CB LEU A1121 2041 7208 8031 212 74 294 C ATOM 2435 CG LEU A1121 78.182 164.831 327.269 1.00 45.71 C ANISOU 2435 CG LEU A1121 2027 7351 7988 216 75 236 C ATOM 2436 CD1 LEU A1121 77.677 166.231 327.012 1.00 46.13 C ANISOU 2436 CD1 LEU A1121 2051 7403 8075 265 78 229 C ATOM 2437 CD2 LEU A1121 77.335 163.779 326.594 1.00 45.33 C ANISOU 2437 CD2 LEU A1121 1999 7350 7873 178 102 232 C ATOM 2438 N GLN A1122 82.481 164.191 327.723 1.00 45.50 N ANISOU 2438 N GLN A1122 2074 7050 8164 196 27 349 N ATOM 2439 CA GLN A1122 83.921 164.209 327.507 1.00 45.51 C ANISOU 2439 CA GLN A1122 2099 6940 8252 198 19 398 C ATOM 2440 C GLN A1122 84.527 162.828 327.714 1.00 45.17 C ANISOU 2440 C GLN A1122 2083 6894 8186 163 21 419 C ATOM 2441 O GLN A1122 85.461 162.441 327.006 1.00 93.23 O ANISOU 2441 O GLN A1122 8204 12899 14319 161 37 476 O ATOM 2442 CB GLN A1122 84.548 165.243 328.440 1.00 46.08 C ANISOU 2442 CB GLN A1122 2135 6970 8405 218 -24 380 C ATOM 2443 CG GLN A1122 86.054 165.277 328.478 1.00 68.81 C ANISOU 2443 CG GLN A1122 5027 9738 11379 214 -43 423 C ATOM 2444 CD GLN A1122 86.559 166.388 329.380 1.00 72.61 C ANISOU 2444 CD GLN A1122 5465 10174 11948 230 -90 399 C ATOM 2445 OE1 GLN A1122 86.363 167.571 329.093 1.00 71.78 O ANISOU 2445 OE1 GLN A1122 5342 10029 11902 258 -92 395 O ATOM 2446 NE2 GLN A1122 87.191 166.013 330.489 1.00 76.17 N ANISOU 2446 NE2 GLN A1122 5897 10630 12414 212 -130 382 N ATOM 2447 N GLN A1123 83.983 162.055 328.651 1.00 45.12 N ANISOU 2447 N GLN A1123 2060 6976 8109 137 8 377 N ATOM 2448 CA GLN A1123 84.462 160.703 328.919 1.00 62.53 C ANISOU 2448 CA GLN A1123 4287 9182 10290 103 10 396 C ATOM 2449 C GLN A1123 83.794 159.657 328.037 1.00 44.40 C ANISOU 2449 C GLN A1123 2022 6913 7934 78 49 415 C ATOM 2450 O GLN A1123 83.942 158.451 328.296 1.00 44.20 O ANISOU 2450 O GLN A1123 2011 6902 7881 46 54 426 O ATOM 2451 CB GLN A1123 84.246 160.357 330.391 1.00 61.49 C ANISOU 2451 CB GLN A1123 4117 9127 10118 86 -25 346 C ATOM 2452 CG GLN A1123 84.798 161.400 331.341 1.00 61.54 C ANISOU 2452 CG GLN A1123 4084 9116 10184 109 -70 324 C ATOM 2453 CD GLN A1123 84.550 161.043 332.783 1.00 45.90 C ANISOU 2453 CD GLN A1123 2063 7219 8159 94 -105 277 C ATOM 2454 OE1 GLN A1123 84.035 159.967 333.085 1.00 45.68 O ANISOU 2454 OE1 GLN A1123 2037 7258 8060 64 -94 263 O ATOM 2455 NE2 GLN A1123 84.913 161.941 333.687 1.00 49.07 N ANISOU 2455 NE2 GLN A1123 2422 7614 8609 113 -147 253 N ATOM 2456 N LYS A1124 83.051 160.121 327.031 1.00 44.31 N ANISOU 2456 N LYS A1124 2018 6909 7907 91 76 419 N ATOM 2457 CA LYS A1124 82.405 159.309 326.003 1.00 58.43 C ANISOU 2457 CA LYS A1124 3834 8713 9652 70 113 442 C ATOM 2458 C LYS A1124 81.357 158.350 326.556 1.00 58.67 C ANISOU 2458 C LYS A1124 3852 8837 9604 29 113 402 C ATOM 2459 O LYS A1124 81.056 157.342 325.921 1.00 59.31 O ANISOU 2459 O LYS A1124 3957 8920 9657 -1 138 429 O ATOM 2460 CB LYS A1124 83.433 158.526 325.179 1.00 58.49 C ANISOU 2460 CB LYS A1124 3885 8636 9703 66 136 515 C ATOM 2461 CG LYS A1124 84.627 159.365 324.708 1.00 58.15 C ANISOU 2461 CG LYS A1124 3853 8490 9750 103 136 561 C ATOM 2462 CD LYS A1124 84.538 159.713 323.233 1.00 57.23 C ANISOU 2462 CD LYS A1124 3759 8330 9654 124 172 607 C ATOM 2463 CE LYS A1124 85.630 160.702 322.861 1.00 44.01 C ANISOU 2463 CE LYS A1124 2089 6558 8074 160 170 648 C ATOM 2464 NZ LYS A1124 86.907 160.410 323.582 1.00 48.44 N ANISOU 2464 NZ LYS A1124 2653 7061 8692 158 150 669 N ATOM 2465 N ARG A1125 80.783 158.635 327.720 1.00 44.13 N ANISOU 2465 N ARG A1125 1970 7070 7728 27 87 340 N ATOM 2466 CA ARG A1125 79.697 157.829 328.269 1.00 51.55 C ANISOU 2466 CA ARG A1125 2891 8096 8599 -11 89 298 C ATOM 2467 C ARG A1125 78.410 158.612 328.044 1.00 44.31 C ANISOU 2467 C ARG A1125 1945 7242 7648 3 97 254 C ATOM 2468 O ARG A1125 78.123 159.572 328.764 1.00 50.35 O ANISOU 2468 O ARG A1125 2670 8049 8413 33 78 210 O ATOM 2469 CB ARG A1125 79.916 157.539 329.751 1.00 51.71 C ANISOU 2469 CB ARG A1125 2882 8160 8606 -22 57 261 C ATOM 2470 CG ARG A1125 80.316 158.769 330.543 1.00 52.89 C ANISOU 2470 CG ARG A1125 2995 8316 8786 19 25 232 C ATOM 2471 CD ARG A1125 80.052 158.605 332.014 1.00 53.77 C ANISOU 2471 CD ARG A1125 3061 8504 8866 11 -4 180 C ATOM 2472 NE ARG A1125 81.250 158.212 332.736 1.00 45.14 N ANISOU 2472 NE ARG A1125 1972 7372 7808 4 -32 202 N ATOM 2473 CZ ARG A1125 81.223 157.729 333.967 1.00 63.65 C ANISOU 2473 CZ ARG A1125 4284 9772 10127 -13 -57 170 C ATOM 2474 NH1 ARG A1125 80.060 157.585 334.580 1.00 62.59 N ANISOU 2474 NH1 ARG A1125 4114 9730 9939 -23 -56 113 N ATOM 2475 NH2 ARG A1125 82.344 157.389 334.580 1.00 64.78 N ANISOU 2475 NH2 ARG A1125 4431 9877 10307 -19 -84 194 N ATOM 2476 N TRP A1126 77.629 158.200 327.047 1.00 44.13 N ANISOU 2476 N TRP A1126 1939 7226 7603 -17 125 270 N ATOM 2477 CA TRP A1126 76.448 158.969 326.681 1.00 59.01 C ANISOU 2477 CA TRP A1126 3797 9157 9466 -2 134 236 C ATOM 2478 C TRP A1126 75.233 158.590 327.521 1.00 60.47 C ANISOU 2478 C TRP A1126 3945 9422 9609 -28 130 177 C ATOM 2479 O TRP A1126 74.519 159.468 328.019 1.00 62.26 O ANISOU 2479 O TRP A1126 4128 9698 9830 0 123 125 O ATOM 2480 CB TRP A1126 76.149 158.786 325.190 1.00 58.56 C ANISOU 2480 CB TRP A1126 3771 9068 9412 -10 164 284 C ATOM 2481 CG TRP A1126 77.335 159.027 324.313 1.00 59.78 C ANISOU 2481 CG TRP A1126 3962 9135 9617 15 173 347 C ATOM 2482 CD1 TRP A1126 77.773 160.225 323.823 1.00 59.15 C ANISOU 2482 CD1 TRP A1126 3882 9011 9583 63 174 363 C ATOM 2483 CD2 TRP A1126 78.244 158.040 323.828 1.00 63.01 C ANISOU 2483 CD2 TRP A1126 4411 9483 10046 -5 186 406 C ATOM 2484 NE1 TRP A1126 78.901 160.043 323.063 1.00 43.86 N ANISOU 2484 NE1 TRP A1126 1983 6986 7695 72 187 428 N ATOM 2485 CE2 TRP A1126 79.209 158.708 323.046 1.00 65.65 C ANISOU 2485 CE2 TRP A1126 4768 9737 10440 34 195 454 C ATOM 2486 CE3 TRP A1126 78.336 156.654 323.977 1.00 65.90 C ANISOU 2486 CE3 TRP A1126 4795 9852 10391 -51 192 427 C ATOM 2487 CZ2 TRP A1126 80.252 158.036 322.417 1.00 68.40 C ANISOU 2487 CZ2 TRP A1126 5153 10010 10827 32 213 519 C ATOM 2488 CZ3 TRP A1126 79.370 155.989 323.355 1.00 68.57 C ANISOU 2488 CZ3 TRP A1126 5171 10118 10766 -52 208 493 C ATOM 2489 CH2 TRP A1126 80.317 156.679 322.583 1.00 69.68 C ANISOU 2489 CH2 TRP A1126 5330 10181 10965 -9 219 538 C ATOM 2490 N ASP A1127 75.001 157.289 327.702 1.00 61.14 N ANISOU 2490 N ASP A1127 4044 9511 9674 -81 136 189 N ATOM 2491 CA ASP A1127 73.808 156.836 328.408 1.00 61.92 C ANISOU 2491 CA ASP A1127 4111 9663 9751 -111 136 149 C ATOM 2492 C ASP A1127 73.717 157.415 329.809 1.00 60.34 C ANISOU 2492 C ASP A1127 3863 9507 9556 -84 113 82 C ATOM 2493 O ASP A1127 72.612 157.622 330.318 1.00 61.38 O ANISOU 2493 O ASP A1127 3956 9675 9689 -83 115 41 O ATOM 2494 CB ASP A1127 73.782 155.313 328.465 1.00 68.76 C ANISOU 2494 CB ASP A1127 5005 10517 10602 -172 143 191 C ATOM 2495 CG ASP A1127 73.633 154.699 327.098 1.00 75.10 C ANISOU 2495 CG ASP A1127 5847 11291 11397 -201 166 255 C ATOM 2496 OD1 ASP A1127 72.724 155.133 326.357 1.00 74.63 O ANISOU 2496 OD1 ASP A1127 5778 11247 11332 -197 178 256 O ATOM 2497 OD2 ASP A1127 74.435 153.804 326.756 1.00 80.57 O ANISOU 2497 OD2 ASP A1127 6575 11946 12092 -224 171 307 O ATOM 2498 N GLU A1128 74.850 157.689 330.444 1.00 57.16 N ANISOU 2498 N GLU A1128 3459 9097 9162 -62 90 79 N ATOM 2499 CA GLU A1128 74.829 158.317 331.755 1.00 57.56 C ANISOU 2499 CA GLU A1128 3458 9198 9214 -32 64 20 C ATOM 2500 C GLU A1128 74.728 159.833 331.682 1.00 55.49 C ANISOU 2500 C GLU A1128 3164 8961 8957 28 57 -3 C ATOM 2501 O GLU A1128 74.529 160.473 332.718 1.00 55.26 O ANISOU 2501 O GLU A1128 3107 8970 8920 59 37 -42 O ATOM 2502 CB GLU A1128 76.068 157.911 332.552 1.00 60.79 C ANISOU 2502 CB GLU A1128 3874 9592 9631 -37 37 36 C ATOM 2503 CG GLU A1128 76.093 156.437 332.897 1.00 65.75 C ANISOU 2503 CG GLU A1128 4523 10206 10252 -93 41 56 C ATOM 2504 CD GLU A1128 77.390 156.022 333.550 1.00 71.36 C ANISOU 2504 CD GLU A1128 5245 10894 10976 -96 16 81 C ATOM 2505 OE1 GLU A1128 77.982 155.014 333.109 1.00 74.40 O ANISOU 2505 OE1 GLU A1128 5672 11230 11366 -129 26 138 O ATOM 2506 OE2 GLU A1128 77.823 156.711 334.499 1.00 72.49 O ANISOU 2506 OE2 GLU A1128 5350 11068 11126 -66 -15 49 O ATOM 2507 N ALA A1129 74.862 160.418 330.495 1.00 45.58 N ANISOU 2507 N ALA A1129 1936 7668 7716 48 72 37 N ATOM 2508 CA ALA A1129 74.579 161.833 330.296 1.00 46.74 C ANISOU 2508 CA ALA A1129 2053 7832 7874 103 71 26 C ATOM 2509 C ALA A1129 73.207 162.072 329.695 1.00 46.05 C ANISOU 2509 C ALA A1129 1948 7774 7775 105 96 -2 C ATOM 2510 O ALA A1129 72.597 163.114 329.958 1.00 60.57 O ANISOU 2510 O ALA A1129 3758 9644 9612 149 95 -29 O ATOM 2511 CB ALA A1129 75.636 162.468 329.391 1.00 46.72 C ANISOU 2511 CB ALA A1129 2087 7745 7918 129 72 91 C ATOM 2512 N ALA A1130 72.717 161.129 328.892 1.00 66.79 N ANISOU 2512 N ALA A1130 4607 10376 10395 58 118 21 N ATOM 2513 CA ALA A1130 71.359 161.225 328.373 1.00 67.33 C ANISOU 2513 CA ALA A1130 4658 10461 10464 52 140 7 C ATOM 2514 C ALA A1130 70.341 161.133 329.501 1.00 65.28 C ANISOU 2514 C ALA A1130 4367 10228 10208 48 137 -41 C ATOM 2515 O ALA A1130 69.415 161.950 329.586 1.00 62.32 O ANISOU 2515 O ALA A1130 3963 9870 9846 81 145 -66 O ATOM 2516 CB ALA A1130 71.120 160.127 327.336 1.00 62.59 C ANISOU 2516 CB ALA A1130 4103 9824 9854 -3 160 64 C ATOM 2517 N VAL A1131 70.507 160.149 330.390 1.00 65.76 N ANISOU 2517 N VAL A1131 4432 10285 10269 12 128 -44 N ATOM 2518 CA VAL A1131 69.565 159.983 331.493 1.00 65.91 C ANISOU 2518 CA VAL A1131 4417 10313 10313 8 127 -67 C ATOM 2519 C VAL A1131 69.785 161.049 332.562 1.00 70.74 C ANISOU 2519 C VAL A1131 5001 10943 10935 67 108 -125 C ATOM 2520 O VAL A1131 68.852 161.403 333.295 1.00 71.43 O ANISOU 2520 O VAL A1131 5047 11031 11062 88 114 -143 O ATOM 2521 CB VAL A1131 69.658 158.560 332.085 1.00 61.95 C ANISOU 2521 CB VAL A1131 3922 9805 9811 -50 124 -34 C ATOM 2522 CG1 VAL A1131 69.551 157.508 330.982 1.00 56.86 C ANISOU 2522 CG1 VAL A1131 3314 9149 9141 -107 141 30 C ATOM 2523 CG2 VAL A1131 70.933 158.379 332.908 1.00 46.49 C ANISOU 2523 CG2 VAL A1131 1978 7842 7845 -44 97 -57 C ATOM 2524 N ASN A1132 71.005 161.587 332.668 1.00 47.14 N ANISOU 2524 N ASN A1132 2023 7975 7912 96 84 -135 N ATOM 2525 CA ASN A1132 71.279 162.601 333.683 1.00 61.36 C ANISOU 2525 CA ASN A1132 3791 9819 9703 152 61 -174 C ATOM 2526 C ASN A1132 70.686 163.948 333.293 1.00 61.24 C ANISOU 2526 C ASN A1132 3749 9834 9684 211 71 -184 C ATOM 2527 O ASN A1132 70.222 164.704 334.156 1.00 61.12 O ANISOU 2527 O ASN A1132 3694 9856 9674 257 65 -225 O ATOM 2528 CB ASN A1132 72.786 162.732 333.907 1.00 62.37 C ANISOU 2528 CB ASN A1132 3928 9965 9803 161 32 -134 C ATOM 2529 CG ASN A1132 73.126 163.645 335.069 1.00 63.39 C ANISOU 2529 CG ASN A1132 4015 10155 9917 214 3 -140 C ATOM 2530 OD1 ASN A1132 73.224 164.863 334.917 1.00 48.45 O ANISOU 2530 OD1 ASN A1132 2094 8281 8034 268 0 -106 O ATOM 2531 ND2 ASN A1132 73.310 163.053 336.243 1.00 63.83 N ANISOU 2531 ND2 ASN A1132 4060 10230 9964 198 -18 -171 N ATOM 2532 N LEU A1133 70.704 164.275 332.002 1.00 47.77 N ANISOU 2532 N LEU A1133 2061 8113 7977 214 88 -143 N ATOM 2533 CA LEU A1133 70.100 165.518 331.547 1.00 48.16 C ANISOU 2533 CA LEU A1133 2083 8184 8033 269 100 -145 C ATOM 2534 C LEU A1133 68.580 165.492 331.626 1.00 85.29 C ANISOU 2534 C LEU A1133 6761 12876 12769 266 124 -189 C ATOM 2535 O LEU A1133 67.957 166.551 331.509 1.00 89.94 O ANISOU 2535 O LEU A1133 7318 13487 13367 318 134 -203 O ATOM 2536 CB LEU A1133 70.547 165.815 330.117 1.00 47.76 C ANISOU 2536 CB LEU A1133 2053 8097 7996 270 112 -88 C ATOM 2537 CG LEU A1133 71.990 166.275 329.909 1.00 47.57 C ANISOU 2537 CG LEU A1133 2033 8041 8000 291 94 -33 C ATOM 2538 CD1 LEU A1133 72.354 166.195 328.444 1.00 47.10 C ANISOU 2538 CD1 LEU A1133 2010 7918 7969 277 111 17 C ATOM 2539 CD2 LEU A1133 72.157 167.690 330.408 1.00 48.18 C ANISOU 2539 CD2 LEU A1133 2063 8135 8110 362 82 -23 C ATOM 2540 N ALA A1134 67.972 164.320 331.843 1.00 78.51 N ANISOU 2540 N ALA A1134 5908 11976 11946 209 135 -185 N ATOM 2541 CA ALA A1134 66.517 164.190 331.865 1.00 71.95 C ANISOU 2541 CA ALA A1134 5042 11128 11168 201 163 -167 C ATOM 2542 C ALA A1134 65.862 164.889 333.051 1.00 67.31 C ANISOU 2542 C ALA A1134 4400 10539 10637 250 166 -196 C ATOM 2543 O ALA A1134 64.644 165.098 333.026 1.00 64.10 O ANISOU 2543 O ALA A1134 3951 10140 10264 262 193 -161 O ATOM 2544 CB ALA A1134 66.119 162.712 331.871 1.00 48.47 C ANISOU 2544 CB ALA A1134 2078 8144 8196 129 173 -107 C ATOM 2545 N LYS A1135 66.622 165.253 334.081 1.00 49.79 N ANISOU 2545 N LYS A1135 2172 8321 8424 282 141 -245 N ATOM 2546 CA LYS A1135 66.045 165.829 335.286 1.00 73.48 C ANISOU 2546 CA LYS A1135 5115 11296 11509 328 146 -253 C ATOM 2547 C LYS A1135 66.244 167.335 335.379 1.00 80.03 C ANISOU 2547 C LYS A1135 5922 12166 12320 408 135 -329 C ATOM 2548 O LYS A1135 65.931 167.926 336.417 1.00 84.58 O ANISOU 2548 O LYS A1135 6448 12691 12998 455 139 -334 O ATOM 2549 CB LYS A1135 66.632 165.151 336.523 1.00 67.40 C ANISOU 2549 CB LYS A1135 4336 10495 10777 310 125 -234 C ATOM 2550 CG LYS A1135 66.850 163.658 336.370 1.00 63.27 C ANISOU 2550 CG LYS A1135 3846 9983 10210 234 123 -182 C ATOM 2551 CD LYS A1135 67.376 163.059 337.661 1.00 50.21 C ANISOU 2551 CD LYS A1135 2173 8321 8582 223 100 -155 C ATOM 2552 CE LYS A1135 67.826 161.625 337.470 1.00 49.57 C ANISOU 2552 CE LYS A1135 2132 8257 8447 150 93 -124 C ATOM 2553 NZ LYS A1135 68.442 161.086 338.713 1.00 49.75 N ANISOU 2553 NZ LYS A1135 2136 8284 8484 142 66 -104 N ATOM 2554 N SER A1136 66.747 167.971 334.329 1.00 50.83 N ANISOU 2554 N SER A1136 2251 8569 8493 431 127 -329 N ATOM 2555 CA SER A1136 67.019 169.397 334.390 1.00 59.37 C ANISOU 2555 CA SER A1136 3302 9770 9484 519 120 -306 C ATOM 2556 C SER A1136 65.746 170.203 334.162 1.00 58.26 C ANISOU 2556 C SER A1136 3122 9598 9417 562 150 -347 C ATOM 2557 O SER A1136 64.808 169.747 333.501 1.00 61.20 O ANISOU 2557 O SER A1136 3495 9878 9879 521 179 -336 O ATOM 2558 CB SER A1136 68.073 169.783 333.353 1.00 61.23 C ANISOU 2558 CB SER A1136 3565 10017 9684 524 112 -200 C ATOM 2559 OG SER A1136 67.639 169.452 332.045 1.00 50.37 O ANISOU 2559 OG SER A1136 2220 8582 8338 484 132 -204 O ATOM 2560 N ARG A1137 65.712 171.409 334.738 1.00 58.34 N ANISOU 2560 N ARG A1137 3417 9430 9319 166 434 -280 N ATOM 2561 CA ARG A1137 64.635 172.344 334.422 1.00 57.48 C ANISOU 2561 CA ARG A1137 3227 9351 9260 293 614 -250 C ATOM 2562 C ARG A1137 64.609 172.638 332.933 1.00 56.51 C ANISOU 2562 C ARG A1137 3100 9084 9289 387 616 -186 C ATOM 2563 O ARG A1137 63.539 172.795 332.335 1.00 56.89 O ANISOU 2563 O ARG A1137 3058 9184 9374 450 666 -47 O ATOM 2564 CB ARG A1137 64.803 173.643 335.212 1.00 62.45 C ANISOU 2564 CB ARG A1137 3865 9964 9901 363 826 -442 C ATOM 2565 CG ARG A1137 64.540 173.510 336.695 1.00 72.94 C ANISOU 2565 CG ARG A1137 5174 11483 11056 270 866 -502 C ATOM 2566 CD ARG A1137 65.139 174.677 337.456 1.00 80.66 C ANISOU 2566 CD ARG A1137 6195 12413 12040 301 1042 -746 C ATOM 2567 NE ARG A1137 65.197 174.412 338.892 1.00 85.40 N ANISOU 2567 NE ARG A1137 6800 13205 12442 170 1042 -823 N ATOM 2568 CZ ARG A1137 66.190 173.766 339.499 1.00 84.27 C ANISOU 2568 CZ ARG A1137 6730 13097 12192 32 889 -862 C ATOM 2569 NH1 ARG A1137 67.224 173.310 338.798 1.00 80.47 N ANISOU 2569 NH1 ARG A1137 6323 12453 11800 15 732 -841 N ATOM 2570 NH2 ARG A1137 66.148 173.575 340.813 1.00 85.77 N ANISOU 2570 NH2 ARG A1137 6910 13492 12187 -96 896 -915 N ATOM 2571 N TRP A1138 65.791 172.718 332.321 1.00 57.11 N ANISOU 2571 N TRP A1138 3267 8985 9449 391 561 -279 N ATOM 2572 CA TRP A1138 65.884 172.844 330.872 1.00 59.20 C ANISOU 2572 CA TRP A1138 3533 9128 9831 451 539 -215 C ATOM 2573 C TRP A1138 65.060 171.767 330.166 1.00 61.99 C ANISOU 2573 C TRP A1138 3830 9578 10144 388 403 -17 C ATOM 2574 O TRP A1138 64.334 172.059 329.208 1.00 64.83 O ANISOU 2574 O TRP A1138 4125 9950 10559 449 440 99 O ATOM 2575 CB TRP A1138 67.356 172.797 330.457 1.00 55.29 C ANISOU 2575 CB TRP A1138 3149 8453 9406 429 469 -342 C ATOM 2576 CG TRP A1138 67.563 172.540 329.011 1.00 52.51 C ANISOU 2576 CG TRP A1138 2809 8005 9136 440 400 -274 C ATOM 2577 CD1 TRP A1138 67.211 173.351 327.982 1.00 52.59 C ANISOU 2577 CD1 TRP A1138 2776 7966 9238 542 492 -221 C ATOM 2578 CD2 TRP A1138 68.171 171.386 328.427 1.00 51.53 C ANISOU 2578 CD2 TRP A1138 2736 7832 9011 336 227 -251 C ATOM 2579 NE1 TRP A1138 67.553 172.773 326.788 1.00 51.74 N ANISOU 2579 NE1 TRP A1138 2695 7802 9160 498 386 -169 N ATOM 2580 CE2 TRP A1138 68.148 171.565 327.035 1.00 51.08 C ANISOU 2580 CE2 TRP A1138 2672 7710 9027 374 229 -200 C ATOM 2581 CE3 TRP A1138 68.729 170.216 328.948 1.00 52.21 C ANISOU 2581 CE3 TRP A1138 2862 7921 9054 210 74 -263 C ATOM 2582 CZ2 TRP A1138 68.663 170.618 326.152 1.00 50.28 C ANISOU 2582 CZ2 TRP A1138 2612 7549 8944 286 97 -189 C ATOM 2583 CZ3 TRP A1138 69.244 169.275 328.068 1.00 52.21 C ANISOU 2583 CZ3 TRP A1138 2895 7838 9105 134 -57 -245 C ATOM 2584 CH2 TRP A1138 69.205 169.482 326.686 1.00 50.22 C ANISOU 2584 CH2 TRP A1138 2643 7524 8913 171 -39 -221 C ATOM 2585 N TYR A1139 65.138 170.519 330.643 1.00 61.15 N ANISOU 2585 N TYR A1139 3738 9549 9949 259 244 31 N ATOM 2586 CA TYR A1139 64.294 169.455 330.100 1.00 60.49 C ANISOU 2586 CA TYR A1139 3593 9564 9828 187 118 211 C ATOM 2587 C TYR A1139 62.824 169.702 330.403 1.00 60.29 C ANISOU 2587 C TYR A1139 3451 9709 9746 230 201 349 C ATOM 2588 O TYR A1139 61.954 169.330 329.609 1.00 58.90 O ANISOU 2588 O TYR A1139 3206 9597 9575 222 155 506 O ATOM 2589 CB TYR A1139 64.717 168.100 330.668 1.00 59.12 C ANISOU 2589 CB TYR A1139 3445 9421 9596 41 -61 233 C ATOM 2590 CG TYR A1139 63.974 166.904 330.102 1.00 60.39 C ANISOU 2590 CG TYR A1139 3548 9659 9740 -47 -202 399 C ATOM 2591 CD1 TYR A1139 62.698 166.565 330.547 1.00 62.49 C ANISOU 2591 CD1 TYR A1139 3714 10108 9922 -68 -206 553 C ATOM 2592 CD2 TYR A1139 64.564 166.095 329.145 1.00 59.47 C ANISOU 2592 CD2 TYR A1139 3472 9429 9694 -117 -328 393 C ATOM 2593 CE1 TYR A1139 62.025 165.469 330.028 1.00 62.52 C ANISOU 2593 CE1 TYR A1139 3662 10178 9916 -156 -339 702 C ATOM 2594 CE2 TYR A1139 63.901 164.997 328.626 1.00 59.16 C ANISOU 2594 CE2 TYR A1139 3379 9453 9647 -209 -452 524 C ATOM 2595 CZ TYR A1139 62.635 164.690 329.069 1.00 58.64 C ANISOU 2595 CZ TYR A1139 3214 9567 9498 -228 -462 681 C ATOM 2596 OH TYR A1139 61.989 163.598 328.545 1.00 56.68 O ANISOU 2596 OH TYR A1139 2911 9377 9248 -325 -589 808 O ATOM 2597 N ASN A1140 62.525 170.304 331.554 1.00 66.66 N ANISOU 2597 N ASN A1140 4230 10599 10498 265 325 292 N ATOM 2598 CA ASN A1140 61.136 170.529 331.935 1.00 71.14 C ANISOU 2598 CA ASN A1140 4680 11328 11021 304 418 416 C ATOM 2599 C ASN A1140 60.543 171.736 331.224 1.00 69.66 C ANISOU 2599 C ASN A1140 4425 11091 10953 450 588 446 C ATOM 2600 O ASN A1140 59.417 171.665 330.718 1.00 69.30 O ANISOU 2600 O ASN A1140 4274 11133 10923 476 597 623 O ATOM 2601 CB ASN A1140 61.025 170.701 333.450 1.00 81.41 C ANISOU 2601 CB ASN A1140 5970 12749 12212 274 499 333 C ATOM 2602 CG ASN A1140 61.309 169.409 334.202 1.00 88.73 C ANISOU 2602 CG ASN A1140 6922 13775 13015 119 320 377 C ATOM 2603 OD1 ASN A1140 61.366 168.331 333.601 1.00 91.94 O ANISOU 2603 OD1 ASN A1140 7332 14167 13433 40 144 488 O ATOM 2604 ND2 ASN A1140 61.479 169.508 335.519 1.00 90.95 N ANISOU 2604 ND2 ASN A1140 7211 14164 13183 66 367 291 N ATOM 2605 N GLN A1141 61.270 172.855 331.172 1.00 65.78 N ANISOU 2605 N GLN A1141 3980 10456 10559 543 722 288 N ATOM 2606 CA GLN A1141 60.664 174.059 330.607 1.00 66.35 C ANISOU 2606 CA GLN A1141 3964 10476 10770 685 897 330 C ATOM 2607 C GLN A1141 60.474 173.951 329.098 1.00 65.02 C ANISOU 2607 C GLN A1141 3765 10259 10682 705 819 484 C ATOM 2608 O GLN A1141 59.563 174.576 328.543 1.00 72.78 O ANISOU 2608 O GLN A1141 4631 11267 11755 790 912 624 O ATOM 2609 CB GLN A1141 61.494 175.295 330.955 1.00 62.58 C ANISOU 2609 CB GLN A1141 3535 9847 10395 776 1063 120 C ATOM 2610 CG GLN A1141 61.867 175.437 332.438 1.00 64.84 C ANISOU 2610 CG GLN A1141 3870 10183 10584 734 1137 -68 C ATOM 2611 CD GLN A1141 60.687 175.284 333.394 1.00 68.73 C ANISOU 2611 CD GLN A1141 4264 10869 10980 715 1214 -4 C ATOM 2612 OE1 GLN A1141 60.178 174.183 333.600 1.00 71.87 O ANISOU 2612 OE1 GLN A1141 4641 11416 11252 617 1075 129 O ATOM 2613 NE2 GLN A1141 60.252 176.394 333.984 1.00 69.68 N ANISOU 2613 NE2 GLN A1141 4319 10984 11173 806 1444 -104 N ATOM 2614 N THR A1142 61.319 173.182 328.417 1.00 60.55 N ANISOU 2614 N THR A1142 3291 9628 10087 622 655 464 N ATOM 2615 CA THR A1142 61.205 172.966 326.978 1.00 56.66 C ANISOU 2615 CA THR A1142 2779 9113 9637 610 571 592 C ATOM 2616 C THR A1142 61.620 171.547 326.647 1.00 55.90 C ANISOU 2616 C THR A1142 2753 9039 9448 462 362 604 C ATOM 2617 O THR A1142 62.805 171.254 326.469 1.00 54.15 O ANISOU 2617 O THR A1142 2640 8695 9238 418 294 470 O ATOM 2618 CB THR A1142 62.076 173.897 326.189 1.00 59.09 C ANISOU 2618 CB THR A1142 3130 9254 10067 689 641 507 C ATOM 2619 OG1 THR A1142 62.358 173.254 324.949 1.00 58.31 O ANISOU 2619 OG1 THR A1142 3062 9143 9952 615 503 576 O ATOM 2620 CG2 THR A1142 63.406 174.073 326.917 1.00 55.03 C ANISOU 2620 CG2 THR A1142 2741 8606 9561 685 659 273 C ATOM 2621 N PRO A1143 60.654 170.643 326.510 1.00 55.44 N ANISOU 2621 N PRO A1143 2626 9126 9313 384 260 767 N ATOM 2622 CA PRO A1143 60.952 169.203 326.373 1.00 57.58 C ANISOU 2622 CA PRO A1143 2949 9419 9511 235 68 774 C ATOM 2623 C PRO A1143 60.890 168.655 324.957 1.00 59.82 C ANISOU 2623 C PRO A1143 3229 9699 9800 164 -41 853 C ATOM 2624 O PRO A1143 61.303 167.508 324.734 1.00 58.83 O ANISOU 2624 O PRO A1143 3154 9553 9645 41 -186 824 O ATOM 2625 CB PRO A1143 59.847 168.550 327.221 1.00 57.36 C ANISOU 2625 CB PRO A1143 2835 9563 9395 186 31 904 C ATOM 2626 CG PRO A1143 59.158 169.645 327.953 1.00 58.84 C ANISOU 2626 CG PRO A1143 2948 9810 9600 306 213 922 C ATOM 2627 CD PRO A1143 59.389 170.913 327.219 1.00 59.57 C ANISOU 2627 CD PRO A1143 3032 9794 9809 430 349 887 C ATOM 2628 N ASN A1144 60.331 169.411 324.017 1.00 63.39 N ANISOU 2628 N ASN A1144 3619 10178 10287 228 27 958 N ATOM 2629 CA ASN A1144 60.343 168.965 322.634 1.00 65.99 C ANISOU 2629 CA ASN A1144 3973 10510 10589 146 -70 1008 C ATOM 2630 C ASN A1144 61.730 169.106 322.041 1.00 64.28 C ANISOU 2630 C ASN A1144 3841 10144 10438 138 -77 851 C ATOM 2631 O ASN A1144 62.188 168.221 321.306 1.00 64.81 O ANISOU 2631 O ASN A1144 3961 10187 10477 20 -193 805 O ATOM 2632 CB ASN A1144 59.303 169.762 321.841 1.00 65.89 C ANISOU 2632 CB ASN A1144 3914 10561 10561 204 -2 1165 C ATOM 2633 CG ASN A1144 57.898 169.335 322.179 1.00 64.41 C ANISOU 2633 CG ASN A1144 3681 10504 10287 175 -32 1321 C ATOM 2634 OD1 ASN A1144 57.661 168.163 322.472 1.00 60.54 O ANISOU 2634 OD1 ASN A1144 3208 10073 9722 65 -152 1333 O ATOM 2635 ND2 ASN A1144 56.960 170.275 322.163 1.00 65.73 N ANISOU 2635 ND2 ASN A1144 3792 10702 10479 271 77 1441 N ATOM 2636 N ARG A1145 62.420 170.187 322.391 1.00 62.86 N ANISOU 2636 N ARG A1145 3700 9845 10340 257 51 742 N ATOM 2637 CA ARG A1145 63.775 170.411 321.923 1.00 58.28 C ANISOU 2637 CA ARG A1145 3226 9099 9817 260 56 577 C ATOM 2638 C ARG A1145 64.805 169.765 322.824 1.00 52.86 C ANISOU 2638 C ARG A1145 2646 8305 9134 211 -1 403 C ATOM 2639 O ARG A1145 65.945 169.566 322.397 1.00 51.06 O ANISOU 2639 O ARG A1145 2507 7944 8948 177 -37 271 O ATOM 2640 CB ARG A1145 64.056 171.910 321.817 1.00 61.79 C ANISOU 2640 CB ARG A1145 3655 9457 10367 409 217 551 C ATOM 2641 CG ARG A1145 64.962 172.304 320.665 1.00 64.12 C ANISOU 2641 CG ARG A1145 4000 9647 10715 412 224 494 C ATOM 2642 CD ARG A1145 65.110 173.812 320.609 1.00 64.31 C ANISOU 2642 CD ARG A1145 3985 9588 10863 564 386 497 C ATOM 2643 NE ARG A1145 65.941 174.372 321.664 1.00 61.96 N ANISOU 2643 NE ARG A1145 3757 9148 10636 642 474 316 N ATOM 2644 CZ ARG A1145 66.790 175.380 321.494 1.00 57.38 C ANISOU 2644 CZ ARG A1145 3210 8420 10171 732 574 219 C ATOM 2645 NH1 ARG A1145 66.973 175.928 320.303 1.00 57.03 N ANISOU 2645 NH1 ARG A1145 3156 8347 10164 755 593 287 N ATOM 2646 NH2 ARG A1145 67.469 175.822 322.525 1.00 56.12 N ANISOU 2646 NH2 ARG A1145 3111 8149 10062 786 646 53 N ATOM 2647 N ALA A1146 64.445 169.451 324.060 1.00 52.09 N ANISOU 2647 N ALA A1146 2531 8266 8994 204 -8 407 N ATOM 2648 CA ALA A1146 65.395 168.761 324.915 1.00 53.31 C ANISOU 2648 CA ALA A1146 2769 8337 9148 139 -81 274 C ATOM 2649 C ALA A1146 65.384 167.258 324.692 1.00 53.97 C ANISOU 2649 C ALA A1146 2859 8447 9201 -10 -251 310 C ATOM 2650 O ALA A1146 66.416 166.605 324.877 1.00 53.22 O ANISOU 2650 O ALA A1146 2836 8234 9150 -78 -329 198 O ATOM 2651 CB ALA A1146 65.113 169.076 326.385 1.00 56.92 C ANISOU 2651 CB ALA A1146 3205 8858 9563 178 -18 257 C ATOM 2652 N LYS A1147 64.249 166.691 324.290 1.00 55.89 N ANISOU 2652 N LYS A1147 3020 8831 9384 -66 -309 464 N ATOM 2653 CA LYS A1147 64.178 165.252 324.076 1.00 59.12 C ANISOU 2653 CA LYS A1147 3425 9258 9780 -212 -466 495 C ATOM 2654 C LYS A1147 64.894 164.811 322.809 1.00 59.69 C ANISOU 2654 C LYS A1147 3552 9225 9901 -286 -520 409 C ATOM 2655 O LYS A1147 65.167 163.615 322.656 1.00 61.60 O ANISOU 2655 O LYS A1147 3808 9426 10173 -410 -638 378 O ATOM 2656 CB LYS A1147 62.716 164.796 324.040 1.00 59.37 C ANISOU 2656 CB LYS A1147 3349 9477 9733 -254 -510 685 C ATOM 2657 N ARG A1148 65.213 165.741 321.912 1.00 60.77 N ANISOU 2657 N ARG A1148 3715 9319 10057 -217 -433 369 N ATOM 2658 CA ARG A1148 65.910 165.447 320.665 1.00 60.68 C ANISOU 2658 CA ARG A1148 3755 9225 10075 -287 -464 280 C ATOM 2659 C ARG A1148 67.371 165.853 320.681 1.00 58.57 C ANISOU 2659 C ARG A1148 3587 8765 9903 -243 -417 99 C ATOM 2660 O ARG A1148 68.214 165.124 320.154 1.00 58.43 O ANISOU 2660 O ARG A1148 3624 8635 9940 -332 -475 -18 O ATOM 2661 CB ARG A1148 65.208 166.142 319.499 1.00 63.79 C ANISOU 2661 CB ARG A1148 4094 9733 10412 -264 -412 388 C ATOM 2662 CG ARG A1148 63.762 165.733 319.357 1.00 63.70 C ANISOU 2662 CG ARG A1148 3976 9916 10310 -317 -466 579 C ATOM 2663 CD ARG A1148 63.241 166.129 318.001 1.00 60.65 C ANISOU 2663 CD ARG A1148 3539 9641 9864 -347 -454 679 C ATOM 2664 NE ARG A1148 63.544 167.523 317.696 1.00 55.87 N ANISOU 2664 NE ARG A1148 2931 8996 9302 -214 -326 692 N ATOM 2665 CZ ARG A1148 62.825 168.553 318.126 1.00 53.32 C ANISOU 2665 CZ ARG A1148 2527 8732 9002 -84 -229 824 C ATOM 2666 NH1 ARG A1148 61.762 168.352 318.893 1.00 53.85 N ANISOU 2666 NH1 ARG A1148 2514 8909 9039 -69 -240 951 N ATOM 2667 NH2 ARG A1148 63.170 169.787 317.790 1.00 53.39 N ANISOU 2667 NH2 ARG A1148 2526 8683 9077 31 -114 830 N ATOM 2668 N VAL A1149 67.688 167.011 321.264 1.00 57.07 N ANISOU 2668 N VAL A1149 3415 8526 9742 -110 -306 68 N ATOM 2669 CA VAL A1149 69.086 167.366 321.493 1.00 55.85 C ANISOU 2669 CA VAL A1149 3353 8187 9681 -70 -270 -101 C ATOM 2670 C VAL A1149 69.779 166.270 322.295 1.00 62.31 C ANISOU 2670 C VAL A1149 4211 8917 10548 -160 -374 -180 C ATOM 2671 O VAL A1149 70.852 165.783 321.920 1.00 72.13 O ANISOU 2671 O VAL A1149 5516 10013 11879 -215 -414 -301 O ATOM 2672 CB VAL A1149 69.186 168.733 322.191 1.00 50.54 C ANISOU 2672 CB VAL A1149 2682 7489 9031 78 -137 -120 C ATOM 2673 CG1 VAL A1149 70.496 168.851 322.942 1.00 48.47 C ANISOU 2673 CG1 VAL A1149 2506 7064 8847 95 -130 -281 C ATOM 2674 CG2 VAL A1149 69.063 169.840 321.171 1.00 49.28 C ANISOU 2674 CG2 VAL A1149 2501 7332 8893 164 -33 -83 C ATOM 2675 N ILE A1150 69.156 165.844 323.395 1.00 54.12 N ANISOU 2675 N ILE A1150 3128 7971 9463 -181 -421 -100 N ATOM 2676 CA ILE A1150 69.706 164.749 324.186 1.00 48.93 C ANISOU 2676 CA ILE A1150 2484 7250 8857 -277 -534 -133 C ATOM 2677 C ILE A1150 69.766 163.464 323.370 1.00 48.97 C ANISOU 2677 C ILE A1150 2478 7213 8915 -410 -644 -137 C ATOM 2678 O ILE A1150 70.687 162.654 323.534 1.00 48.74 O ANISOU 2678 O ILE A1150 2477 7043 8998 -484 -718 -217 O ATOM 2679 CB ILE A1150 68.878 164.585 325.474 1.00 49.50 C ANISOU 2679 CB ILE A1150 2495 7467 8847 -281 -558 -21 C ATOM 2680 CG1 ILE A1150 69.078 165.810 326.370 1.00 49.66 C ANISOU 2680 CG1 ILE A1150 2538 7498 8833 -167 -439 -70 C ATOM 2681 CG2 ILE A1150 69.226 163.287 326.202 1.00 49.61 C ANISOU 2681 CG2 ILE A1150 2492 7447 8910 -402 -698 0 C ATOM 2682 CD1 ILE A1150 68.099 165.896 327.514 1.00 50.52 C ANISOU 2682 CD1 ILE A1150 2579 7780 8835 -157 -420 32 C ATOM 2683 N THR A1151 68.811 163.265 322.461 1.00 52.41 N ANISOU 2683 N THR A1151 2867 7763 9283 -446 -654 -55 N ATOM 2684 CA THR A1151 68.827 162.063 321.634 1.00 59.69 C ANISOU 2684 CA THR A1151 3778 8651 10252 -585 -747 -81 C ATOM 2685 C THR A1151 70.002 162.072 320.661 1.00 68.83 C ANISOU 2685 C THR A1151 5009 9642 11502 -609 -717 -250 C ATOM 2686 O THR A1151 70.589 161.020 320.381 1.00 75.26 O ANISOU 2686 O THR A1151 5834 10337 12424 -717 -785 -338 O ATOM 2687 CB THR A1151 67.499 161.924 320.888 1.00 59.20 C ANISOU 2687 CB THR A1151 3645 8772 10076 -628 -763 48 C ATOM 2688 OG1 THR A1151 66.462 161.641 321.835 1.00 61.34 O ANISOU 2688 OG1 THR A1151 3840 9180 10286 -629 -808 201 O ATOM 2689 CG2 THR A1151 67.564 160.793 319.868 1.00 56.24 C ANISOU 2689 CG2 THR A1151 3266 8363 9740 -780 -841 -13 C ATOM 2690 N THR A1152 70.374 163.246 320.148 1.00 66.99 N ANISOU 2690 N THR A1152 4821 9390 11243 -509 -609 -298 N ATOM 2691 CA THR A1152 71.549 163.322 319.287 1.00 61.28 C ANISOU 2691 CA THR A1152 4167 8510 10605 -526 -572 -458 C ATOM 2692 C THR A1152 72.841 162.991 320.037 1.00 65.49 C ANISOU 2692 C THR A1152 4751 8841 11290 -525 -596 -577 C ATOM 2693 O THR A1152 73.834 162.613 319.400 1.00 69.72 O ANISOU 2693 O THR A1152 5331 9225 11933 -576 -592 -714 O ATOM 2694 CB THR A1152 71.641 164.707 318.640 1.00 52.12 C ANISOU 2694 CB THR A1152 3031 7381 9392 -414 -453 -459 C ATOM 2695 OG1 THR A1152 71.625 165.717 319.655 1.00 48.76 O ANISOU 2695 OG1 THR A1152 2607 6955 8963 -280 -388 -419 O ATOM 2696 CG2 THR A1152 70.476 164.932 317.688 1.00 49.01 C ANISOU 2696 CG2 THR A1152 2576 7180 8867 -440 -441 -334 C ATOM 2697 N PHE A1153 72.850 163.098 321.370 1.00 58.45 N ANISOU 2697 N PHE A1153 3848 7952 10408 -479 -621 -525 N ATOM 2698 CA PHE A1153 74.042 162.733 322.134 1.00 52.96 C ANISOU 2698 CA PHE A1153 3187 7083 9853 -495 -661 -609 C ATOM 2699 C PHE A1153 74.201 161.218 322.209 1.00 52.89 C ANISOU 2699 C PHE A1153 3203 6997 9896 -623 -766 -596 C ATOM 2700 O PHE A1153 75.243 160.671 321.830 1.00 57.57 O ANISOU 2700 O PHE A1153 3869 7407 10598 -665 -771 -700 O ATOM 2701 CB PHE A1153 73.983 163.329 323.543 1.00 48.50 C ANISOU 2701 CB PHE A1153 2617 6571 9240 -423 -653 -550 C ATOM 2702 CG PHE A1153 74.364 164.788 323.621 1.00 47.01 C ANISOU 2702 CG PHE A1153 2482 6365 9016 -290 -530 -610 C ATOM 2703 CD1 PHE A1153 75.600 165.178 324.105 1.00 46.60 C ANISOU 2703 CD1 PHE A1153 2486 6164 9057 -257 -511 -715 C ATOM 2704 CD2 PHE A1153 73.474 165.770 323.238 1.00 47.19 C ANISOU 2704 CD2 PHE A1153 2486 6515 8928 -201 -434 -552 C ATOM 2705 CE1 PHE A1153 75.941 166.519 324.189 1.00 46.35 C ANISOU 2705 CE1 PHE A1153 2498 6107 9004 -139 -396 -775 C ATOM 2706 CE2 PHE A1153 73.811 167.103 323.327 1.00 46.98 C ANISOU 2706 CE2 PHE A1153 2494 6456 8899 -79 -316 -604 C ATOM 2707 CZ PHE A1153 75.048 167.479 323.795 1.00 46.55 C ANISOU 2707 CZ PHE A1153 2502 6249 8934 -49 -296 -723 C ATOM 2708 N ARG A1154 73.175 160.519 322.701 1.00 50.01 N ANISOU 2708 N ARG A1154 2787 6763 9451 -678 -838 -462 N ATOM 2709 CA ARG A1154 73.289 159.081 322.923 1.00 50.67 C ANISOU 2709 CA ARG A1154 2901 6772 9580 -788 -929 -430 C ATOM 2710 C ARG A1154 73.370 158.288 321.624 1.00 49.85 C ANISOU 2710 C ARG A1154 2825 6590 9524 -877 -927 -519 C ATOM 2711 O ARG A1154 73.876 157.159 321.638 1.00 49.64 O ANISOU 2711 O ARG A1154 2845 6426 9591 -953 -971 -548 O ATOM 2712 CB ARG A1154 72.114 158.589 323.770 1.00 56.31 C ANISOU 2712 CB ARG A1154 3549 7659 10189 -822 -999 -261 C ATOM 2713 CG ARG A1154 70.858 159.441 323.633 1.00 63.43 C ANISOU 2713 CG ARG A1154 4363 8777 10962 -765 -960 -174 C ATOM 2714 CD ARG A1154 69.620 158.749 324.199 1.00 69.82 C ANISOU 2714 CD ARG A1154 5110 9751 11669 -817 -1029 -15 C ATOM 2715 NE ARG A1154 69.318 157.499 323.503 1.00 73.32 N ANISOU 2715 NE ARG A1154 5568 10163 12129 -933 -1090 -15 N ATOM 2716 CZ ARG A1154 69.453 156.287 324.038 1.00 74.85 C ANISOU 2716 CZ ARG A1154 5787 10288 12366 -1012 -1165 22 C ATOM 2717 NH1 ARG A1154 69.875 156.148 325.291 1.00 73.50 N ANISOU 2717 NH1 ARG A1154 5625 10090 12210 -995 -1200 79 N ATOM 2718 NH2 ARG A1154 69.154 155.211 323.320 1.00 76.82 N ANISOU 2718 NH2 ARG A1154 6043 10501 12645 -1112 -1204 3 N ATOM 2719 N THR A1155 72.895 158.849 320.506 1.00 53.77 N ANISOU 2719 N THR A1155 3290 7179 9963 -874 -872 -564 N ATOM 2720 CA THR A1155 72.936 158.167 319.218 1.00 58.21 C ANISOU 2720 CA THR A1155 3868 7699 10549 -978 -863 -664 C ATOM 2721 C THR A1155 73.995 158.702 318.259 1.00 56.05 C ANISOU 2721 C THR A1155 3648 7301 10349 -958 -776 -838 C ATOM 2722 O THR A1155 74.376 157.982 317.328 1.00 55.85 O ANISOU 2722 O THR A1155 3659 7189 10374 -1052 -760 -957 O ATOM 2723 CB THR A1155 71.565 158.231 318.517 1.00 65.77 C ANISOU 2723 CB THR A1155 4740 8878 11371 -1029 -878 -582 C ATOM 2724 OG1 THR A1155 70.980 159.529 318.692 1.00 67.48 O ANISOU 2724 OG1 THR A1155 4889 9247 11502 -919 -832 -492 O ATOM 2725 CG2 THR A1155 70.614 157.157 319.062 1.00 68.80 C ANISOU 2725 CG2 THR A1155 5089 9343 11708 -1108 -971 -455 C ATOM 2726 N GLY A1156 74.481 159.928 318.457 1.00 52.62 N ANISOU 2726 N GLY A1156 3216 6855 9921 -842 -710 -860 N ATOM 2727 CA GLY A1156 75.520 160.473 317.600 1.00 51.46 C ANISOU 2727 CA GLY A1156 3118 6591 9845 -818 -624 -1016 C ATOM 2728 C GLY A1156 75.142 160.559 316.140 1.00 53.56 C ANISOU 2728 C GLY A1156 3348 6958 10044 -894 -579 -1084 C ATOM 2729 O GLY A1156 76.023 160.519 315.273 1.00 56.46 O ANISOU 2729 O GLY A1156 3765 7216 10473 -930 -518 -1236 O ATOM 2730 N THR A1157 73.849 160.667 315.840 1.00 51.65 N ANISOU 2730 N THR A1157 3040 6934 9651 -923 -603 -962 N ATOM 2731 CA THR A1157 73.370 160.774 314.471 1.00 52.36 C ANISOU 2731 CA THR A1157 3125 7162 9607 -1002 -565 -984 C ATOM 2732 C THR A1157 72.273 161.824 314.407 1.00 50.14 C ANISOU 2732 C THR A1157 2808 7103 9140 -917 -541 -797 C ATOM 2733 O THR A1157 71.727 162.254 315.426 1.00 49.78 O ANISOU 2733 O THR A1157 2734 7108 9074 -818 -557 -662 O ATOM 2734 CB THR A1157 72.838 159.436 313.935 1.00 56.98 C ANISOU 2734 CB THR A1157 3666 7786 10196 -1182 -636 -1029 C ATOM 2735 OG1 THR A1157 71.761 158.980 314.764 1.00 58.82 O ANISOU 2735 OG1 THR A1157 3831 8123 10395 -1191 -728 -868 O ATOM 2736 CG2 THR A1157 73.939 158.379 313.904 1.00 61.23 C ANISOU 2736 CG2 THR A1157 4287 8083 10893 -1251 -633 -1198 C ATOM 2737 N TRP A1158 71.938 162.227 313.183 1.00 52.35 N ANISOU 2737 N TRP A1158 3080 7521 9288 -967 -498 -786 N ATOM 2738 CA TRP A1158 70.835 163.146 312.954 1.00 60.84 C ANISOU 2738 CA TRP A1158 4099 8813 10204 -907 -479 -589 C ATOM 2739 C TRP A1158 69.487 162.434 312.862 1.00 78.27 C ANISOU 2739 C TRP A1158 6228 11207 12304 -1011 -567 -459 C ATOM 2740 O TRP A1158 68.539 162.999 312.301 1.00 87.96 O ANISOU 2740 O TRP A1158 7395 12636 13388 -1013 -561 -302 O ATOM 2741 CB TRP A1158 71.071 163.953 311.677 1.00 55.51 C ANISOU 2741 CB TRP A1158 3435 8221 9435 -918 -402 -601 C ATOM 2742 CG TRP A1158 72.430 164.534 311.568 1.00 51.65 C ANISOU 2742 CG TRP A1158 3021 7552 9051 -842 -318 -743 C ATOM 2743 CD1 TRP A1158 73.487 164.019 310.875 1.00 52.91 C ANISOU 2743 CD1 TRP A1158 3240 7590 9275 -933 -289 -945 C ATOM 2744 CD2 TRP A1158 72.892 165.750 312.163 1.00 50.02 C ANISOU 2744 CD2 TRP A1158 2835 7263 8908 -663 -244 -700 C ATOM 2745 NE1 TRP A1158 74.581 164.841 311.002 1.00 53.19 N ANISOU 2745 NE1 TRP A1158 3330 7474 9406 -818 -209 -1018 N ATOM 2746 CE2 TRP A1158 74.241 165.910 311.791 1.00 49.61 C ANISOU 2746 CE2 TRP A1158 2855 7040 8953 -653 -183 -871 C ATOM 2747 CE3 TRP A1158 72.298 166.717 312.974 1.00 49.72 C ANISOU 2747 CE3 TRP A1158 2757 7272 8863 -514 -216 -543 C ATOM 2748 CZ2 TRP A1158 75.004 166.998 312.206 1.00 48.86 C ANISOU 2748 CZ2 TRP A1158 2796 6825 8945 -502 -106 -882 C ATOM 2749 CZ3 TRP A1158 73.055 167.795 313.380 1.00 49.06 C ANISOU 2749 CZ3 TRP A1158 2708 7065 8869 -367 -132 -570 C ATOM 2750 CH2 TRP A1158 74.394 167.927 312.997 1.00 48.62 C ANISOU 2750 CH2 TRP A1158 2726 6842 8904 -363 -83 -735 C ATOM 2751 N ASP A1159 69.385 161.207 313.390 1.00 81.48 N ANISOU 2751 N ASP A1159 6623 11548 12788 -1101 -652 -508 N ATOM 2752 CA ASP A1159 68.165 160.420 313.218 1.00 80.21 C ANISOU 2752 CA ASP A1159 6387 11552 12537 -1220 -741 -401 C ATOM 2753 C ASP A1159 66.948 161.150 313.777 1.00 73.24 C ANISOU 2753 C ASP A1159 5430 10847 11549 -1119 -750 -158 C ATOM 2754 O ASP A1159 65.883 161.168 313.148 1.00 73.15 O ANISOU 2754 O ASP A1159 5352 11040 11403 -1187 -781 -26 O ATOM 2755 CB ASP A1159 68.324 159.045 313.881 1.00 79.53 C ANISOU 2755 CB ASP A1159 6291 11335 12591 -1310 -827 -479 C ATOM 2756 CG ASP A1159 69.049 158.031 312.991 1.00 80.10 C ANISOU 2756 CG ASP A1159 6397 11292 12747 -1474 -831 -700 C ATOM 2757 OD1 ASP A1159 68.922 158.125 311.754 1.00 80.74 O ANISOU 2757 OD1 ASP A1159 6485 11485 12709 -1574 -798 -759 O ATOM 2758 OD2 ASP A1159 69.741 157.135 313.528 1.00 79.34 O ANISOU 2758 OD2 ASP A1159 6333 10995 12817 -1504 -858 -804 O ATOM 2759 N ALA A1160 67.097 161.784 314.944 1.00 68.50 N ANISOU 2759 N ALA A1160 4837 10177 11011 -962 -717 -100 N ATOM 2760 CA ALA A1160 65.956 162.375 315.634 1.00 65.95 C ANISOU 2760 CA ALA A1160 4438 10002 10617 -867 -714 111 C ATOM 2761 C ALA A1160 65.434 163.632 314.952 1.00 62.94 C ANISOU 2761 C ALA A1160 4016 9761 10139 -787 -635 242 C ATOM 2762 O ALA A1160 64.307 164.053 315.238 1.00 59.74 O ANISOU 2762 O ALA A1160 3525 9505 9670 -735 -633 434 O ATOM 2763 CB ALA A1160 66.334 162.693 317.080 1.00 67.01 C ANISOU 2763 CB ALA A1160 4593 10025 10841 -737 -689 108 C ATOM 2764 N TYR A1161 66.211 164.228 314.052 1.00 64.67 N ANISOU 2764 N TYR A1161 4283 9934 10355 -779 -569 154 N ATOM 2765 CA TYR A1161 65.867 165.523 313.472 1.00 63.17 C ANISOU 2765 CA TYR A1161 4046 9849 10106 -688 -487 287 C ATOM 2766 C TYR A1161 65.247 165.444 312.079 1.00 65.44 C ANISOU 2766 C TYR A1161 4277 10333 10253 -821 -519 378 C ATOM 2767 O TYR A1161 64.275 166.152 311.809 1.00 67.21 O ANISOU 2767 O TYR A1161 4405 10724 10409 -781 -505 591 O ATOM 2768 CB TYR A1161 67.111 166.420 313.443 1.00 60.47 C ANISOU 2768 CB TYR A1161 3780 9340 9857 -578 -387 164 C ATOM 2769 CG TYR A1161 67.254 167.280 314.677 1.00 53.05 C ANISOU 2769 CG TYR A1161 2844 8300 9013 -397 -314 189 C ATOM 2770 CD1 TYR A1161 67.444 166.709 315.931 1.00 50.98 C ANISOU 2770 CD1 TYR A1161 2613 7940 8816 -376 -350 122 C ATOM 2771 CD2 TYR A1161 67.191 168.663 314.590 1.00 52.11 C ANISOU 2771 CD2 TYR A1161 2687 8189 8922 -257 -208 280 C ATOM 2772 CE1 TYR A1161 67.569 167.496 317.064 1.00 50.55 C ANISOU 2772 CE1 TYR A1161 2563 7815 8827 -229 -279 130 C ATOM 2773 CE2 TYR A1161 67.317 169.457 315.712 1.00 51.25 C ANISOU 2773 CE2 TYR A1161 2581 7988 8905 -102 -129 278 C ATOM 2774 CZ TYR A1161 67.507 168.871 316.947 1.00 50.69 C ANISOU 2774 CZ TYR A1161 2551 7837 8873 -94 -164 195 C ATOM 2775 OH TYR A1161 67.631 169.664 318.066 1.00 50.43 O ANISOU 2775 OH TYR A1161 2522 7732 8909 42 -81 179 O ATOM 2776 N GLY A1200 65.768 164.613 311.187 1.00 60.91 N ANISOU 2776 N GLY A1200 3753 9752 9638 -984 -559 224 N ATOM 2777 CA GLY A1200 65.254 164.587 309.830 1.00 60.45 C ANISOU 2777 CA GLY A1200 3645 9900 9423 -1128 -585 296 C ATOM 2778 C GLY A1200 65.733 163.363 309.084 1.00 60.45 C ANISOU 2778 C GLY A1200 3701 9880 9387 -1332 -636 87 C ATOM 2779 O GLY A1200 66.405 162.496 309.645 1.00 62.55 O ANISOU 2779 O GLY A1200 4032 9960 9773 -1356 -655 -96 O ATOM 2780 N SER A1201 65.380 163.300 307.800 1.00 60.18 N ANISOU 2780 N SER A1201 3632 10042 9191 -1489 -655 117 N ATOM 2781 CA SER A1201 65.800 162.164 306.979 1.00 62.52 C ANISOU 2781 CA SER A1201 3976 10337 9440 -1704 -686 -103 C ATOM 2782 C SER A1201 65.848 162.603 305.514 1.00 66.21 C ANISOU 2782 C SER A1201 4427 11002 9727 -1833 -656 -91 C ATOM 2783 O SER A1201 64.820 162.634 304.835 1.00 69.16 O ANISOU 2783 O SER A1201 4715 11634 9929 -1947 -715 77 O ATOM 2784 CB SER A1201 64.865 160.977 307.166 1.00 62.85 C ANISOU 2784 CB SER A1201 3972 10459 9451 -1843 -795 -83 C ATOM 2785 OG SER A1201 64.972 160.439 308.471 1.00 62.36 O ANISOU 2785 OG SER A1201 3928 10206 9559 -1749 -824 -117 O ATOM 2786 N GLY A1202 67.046 162.958 305.049 1.00 67.77 N ANISOU 2786 N GLY A1202 4700 11086 9963 -1816 -568 -258 N ATOM 2787 CA GLY A1202 67.314 163.173 303.631 1.00 68.74 C ANISOU 2787 CA GLY A1202 4822 11379 9916 -1970 -533 -306 C ATOM 2788 C GLY A1202 67.091 164.563 303.055 1.00 69.18 C ANISOU 2788 C GLY A1202 4811 11603 9870 -1893 -492 -73 C ATOM 2789 O GLY A1202 67.076 164.700 301.828 1.00 68.72 O ANISOU 2789 O GLY A1202 4727 11750 9632 -2051 -485 -61 O ATOM 2790 N SER A1203 66.921 165.595 303.879 1.00 69.48 N ANISOU 2790 N SER A1203 4813 11566 10021 -1666 -461 114 N ATOM 2791 CA SER A1203 66.699 166.937 303.358 1.00 74.47 C ANISOU 2791 CA SER A1203 5364 12335 10597 -1585 -418 350 C ATOM 2792 C SER A1203 67.861 167.876 303.633 1.00 72.69 C ANISOU 2792 C SER A1203 5196 11900 10521 -1407 -308 278 C ATOM 2793 O SER A1203 67.729 169.083 303.415 1.00 72.53 O ANISOU 2793 O SER A1203 5104 11941 10513 -1299 -261 481 O ATOM 2794 CB SER A1203 65.413 167.526 303.936 1.00 75.97 C ANISOU 2794 CB SER A1203 5431 12635 10800 -1474 -459 660 C ATOM 2795 OG SER A1203 65.497 167.650 305.347 1.00 76.62 O ANISOU 2795 OG SER A1203 5544 12495 11073 -1277 -432 637 O ATOM 2796 N ARG A 214 68.998 167.356 304.084 1.00 77.27 N ANISOU 2796 N ARG A 214 5897 12233 11230 -1379 -266 5 N ATOM 2797 CA ARG A 214 70.111 168.196 304.483 1.00 80.16 C ANISOU 2797 CA ARG A 214 6322 12382 11755 -1205 -168 -69 C ATOM 2798 C ARG A 214 71.317 168.086 303.566 1.00 89.70 C ANISOU 2798 C ARG A 214 7604 13540 12938 -1299 -104 -277 C ATOM 2799 O ARG A 214 72.247 168.893 303.696 1.00 95.10 O ANISOU 2799 O ARG A 214 8325 14073 13737 -1167 -21 -316 O ATOM 2800 CB ARG A 214 70.541 167.849 305.913 1.00 77.83 C ANISOU 2800 CB ARG A 214 6095 11819 11656 -1066 -166 -194 C ATOM 2801 CG ARG A 214 70.640 166.354 306.165 1.00 76.63 C ANISOU 2801 CG ARG A 214 6001 11595 11521 -1202 -231 -393 C ATOM 2802 CD ARG A 214 69.445 165.838 306.952 1.00 76.27 C ANISOU 2802 CD ARG A 214 5896 11622 11461 -1200 -321 -260 C ATOM 2803 NE ARG A 214 69.669 165.914 308.394 1.00 74.91 N ANISOU 2803 NE ARG A 214 5755 11250 11459 -1035 -316 -275 N ATOM 2804 CZ ARG A 214 69.419 166.984 309.144 1.00 73.74 C ANISOU 2804 CZ ARG A 214 5571 11074 11373 -849 -272 -125 C ATOM 2805 NH1 ARG A 214 68.930 168.090 308.599 1.00 75.45 N ANISOU 2805 NH1 ARG A 214 5712 11431 11525 -790 -228 67 N ATOM 2806 NH2 ARG A 214 69.661 166.946 310.447 1.00 71.20 N ANISOU 2806 NH2 ARG A 214 5282 10586 11185 -728 -269 -166 N ATOM 2807 N PHE A 215 71.330 167.126 302.649 1.00 86.91 N ANISOU 2807 N PHE A 215 7271 13309 12443 -1524 -133 -418 N ATOM 2808 CA PHE A 215 72.536 166.831 301.887 1.00 84.63 C ANISOU 2808 CA PHE A 215 7061 12943 12150 -1623 -59 -667 C ATOM 2809 C PHE A 215 72.807 167.924 300.860 1.00 87.81 C ANISOU 2809 C PHE A 215 7421 13501 12441 -1630 2 -545 C ATOM 2810 O PHE A 215 72.008 168.142 299.942 1.00 91.47 O ANISOU 2810 O PHE A 215 7799 14257 12697 -1760 -36 -372 O ATOM 2811 CB PHE A 215 72.405 165.472 301.212 1.00 79.44 C ANISOU 2811 CB PHE A 215 6429 12377 11378 -1873 -96 -867 C ATOM 2812 CG PHE A 215 72.530 164.327 302.160 1.00 76.69 C ANISOU 2812 CG PHE A 215 6134 11811 11194 -1870 -135 -1042 C ATOM 2813 CD1 PHE A 215 71.625 164.167 303.194 1.00 76.47 C ANISOU 2813 CD1 PHE A 215 6065 11766 11224 -1780 -219 -891 C ATOM 2814 CD2 PHE A 215 73.556 163.415 302.024 1.00 77.54 C ANISOU 2814 CD2 PHE A 215 6321 11729 11411 -1957 -85 -1348 C ATOM 2815 CE1 PHE A 215 71.741 163.118 304.075 1.00 78.75 C ANISOU 2815 CE1 PHE A 215 6390 11864 11666 -1781 -261 -1029 C ATOM 2816 CE2 PHE A 215 73.677 162.360 302.898 1.00 79.75 C ANISOU 2816 CE2 PHE A 215 6631 11803 11868 -1955 -125 -1485 C ATOM 2817 CZ PHE A 215 72.770 162.212 303.928 1.00 80.02 C ANISOU 2817 CZ PHE A 215 6623 11833 11948 -1869 -218 -1319 C ATOM 2818 N HIS A 216 73.936 168.612 301.024 1.00 84.94 N ANISOU 2818 N HIS A 216 7110 12945 12219 -1494 93 -621 N ATOM 2819 CA HIS A 216 74.371 169.648 300.103 1.00 81.36 C ANISOU 2819 CA HIS A 216 6620 12600 11693 -1490 160 -521 C ATOM 2820 C HIS A 216 75.849 169.451 299.795 1.00 78.56 C ANISOU 2820 C HIS A 216 6365 12062 11422 -1508 256 -795 C ATOM 2821 O HIS A 216 76.565 168.727 300.495 1.00 72.64 O ANISOU 2821 O HIS A 216 5704 11058 10836 -1472 273 -1026 O ATOM 2822 CB HIS A 216 74.141 171.060 300.671 1.00 75.72 C ANISOU 2822 CB HIS A 216 5835 11838 11099 -1259 184 -260 C ATOM 2823 CG HIS A 216 72.699 171.425 300.863 1.00 75.91 C ANISOU 2823 CG HIS A 216 5738 12050 11054 -1233 109 38 C ATOM 2824 ND1 HIS A 216 71.845 170.709 301.676 1.00 75.69 N ANISOU 2824 ND1 HIS A 216 5705 12010 11042 -1230 33 50 N ATOM 2825 CD2 HIS A 216 71.967 172.450 300.364 1.00 76.75 C ANISOU 2825 CD2 HIS A 216 5712 12353 11095 -1204 102 349 C ATOM 2826 CE1 HIS A 216 70.649 171.268 301.659 1.00 76.86 C ANISOU 2826 CE1 HIS A 216 5729 12341 11132 -1200 -14 345 C ATOM 2827 NE2 HIS A 216 70.696 172.328 300.872 1.00 77.64 N ANISOU 2827 NE2 HIS A 216 5745 12566 11190 -1183 26 534 N ATOM 2828 N ARG A 217 76.289 170.114 298.726 1.00 85.40 N ANISOU 2828 N ARG A 217 7204 13067 12179 -1570 317 -750 N ATOM 2829 CA ARG A 217 77.695 170.201 298.326 1.00 88.85 C ANISOU 2829 CA ARG A 217 7716 13353 12690 -1571 422 -962 C ATOM 2830 C ARG A 217 78.180 171.614 298.658 1.00 93.55 C ANISOU 2830 C ARG A 217 8283 13832 13431 -1351 476 -795 C ATOM 2831 O ARG A 217 78.166 172.507 297.808 1.00 96.03 O ANISOU 2831 O ARG A 217 8524 14320 13643 -1371 507 -622 O ATOM 2832 CB ARG A 217 77.868 169.878 296.842 1.00 90.46 C ANISOU 2832 CB ARG A 217 7907 13810 12652 -1820 459 -1048 C ATOM 2833 N ARG A 218 78.615 171.805 299.908 1.00 91.33 N ANISOU 2833 N ARG A 218 8053 13256 13392 -1148 487 -847 N ATOM 2834 CA ARG A 218 79.045 173.125 300.366 1.00 89.70 C ANISOU 2834 CA ARG A 218 7821 12913 13348 -932 540 -708 C ATOM 2835 C ARG A 218 80.275 173.623 299.613 1.00 90.80 C ANISOU 2835 C ARG A 218 7989 12995 13515 -940 638 -800 C ATOM 2836 O ARG A 218 80.481 174.839 299.498 1.00 90.75 O ANISOU 2836 O ARG A 218 7925 12978 13576 -817 682 -629 O ATOM 2837 CB ARG A 218 79.324 173.088 301.868 1.00 84.45 C ANISOU 2837 CB ARG A 218 7216 11954 12916 -746 532 -787 C ATOM 2838 N ARG A 219 81.104 172.709 299.105 1.00 92.70 N ANISOU 2838 N ARG A 219 8309 13189 13723 -1081 678 -1068 N ATOM 2839 CA ARG A 219 82.302 173.101 298.371 1.00 92.34 C ANISOU 2839 CA ARG A 219 8291 13092 13702 -1099 779 -1173 C ATOM 2840 C ARG A 219 81.929 173.841 297.091 1.00 93.03 C ANISOU 2840 C ARG A 219 8281 13492 13573 -1205 796 -966 C ATOM 2841 O ARG A 219 81.049 173.408 296.341 1.00 93.94 O ANISOU 2841 O ARG A 219 8344 13896 13452 -1389 745 -894 O ATOM 2842 CB ARG A 219 83.156 171.868 298.054 1.00 93.21 C ANISOU 2842 CB ARG A 219 8494 13101 13820 -1247 827 -1509 C ATOM 2843 CG ARG A 219 82.382 170.673 297.497 1.00 95.82 C ANISOU 2843 CG ARG A 219 8821 13635 13951 -1478 779 -1608 C ATOM 2844 CD ARG A 219 82.907 169.354 298.073 1.00 96.29 C ANISOU 2844 CD ARG A 219 8968 13457 14162 -1523 785 -1909 C ATOM 2845 NE ARG A 219 82.436 168.184 297.328 1.00 97.99 N ANISOU 2845 NE ARG A 219 9183 13844 14203 -1770 773 -2064 N ATOM 2846 CZ ARG A 219 82.769 166.926 297.612 1.00 96.72 C ANISOU 2846 CZ ARG A 219 9077 13514 14157 -1854 783 -2328 C ATOM 2847 NH1 ARG A 219 83.577 166.663 298.631 1.00 96.15 N ANISOU 2847 NH1 ARG A 219 9059 13105 14369 -1711 796 -2447 N ATOM 2848 NH2 ARG A 219 82.294 165.930 296.875 1.00 95.97 N ANISOU 2848 NH2 ARG A 219 8974 13588 13901 -2087 779 -2469 N ATOM 2849 N ARG A 220 82.599 174.966 296.850 1.00 93.14 N ANISOU 2849 N ARG A 220 8263 13455 13672 -1095 863 -858 N ATOM 2850 CA ARG A 220 82.331 175.824 295.706 1.00 95.36 C ANISOU 2850 CA ARG A 220 8434 14016 13784 -1172 879 -622 C ATOM 2851 C ARG A 220 83.431 175.659 294.655 1.00105.52 C ANISOU 2851 C ARG A 220 9759 15352 14982 -1309 974 -797 C ATOM 2852 O ARG A 220 84.329 174.819 294.797 1.00111.09 O ANISOU 2852 O ARG A 220 10573 15875 15762 -1349 1030 -1108 O ATOM 2853 CB ARG A 220 82.191 177.279 296.164 1.00 89.46 C ANISOU 2853 CB ARG A 220 7596 13186 13207 -950 886 -339 C ATOM 2854 CG ARG A 220 80.777 177.670 296.580 1.00 84.31 C ANISOU 2854 CG ARG A 220 6838 12660 12536 -890 800 -57 C ATOM 2855 CD ARG A 220 80.702 179.153 296.881 1.00 81.54 C ANISOU 2855 CD ARG A 220 6381 12229 12371 -686 830 214 C ATOM 2856 NE ARG A 220 81.916 179.597 297.557 1.00 79.67 N ANISOU 2856 NE ARG A 220 6226 11663 12383 -514 910 55 N ATOM 2857 CZ ARG A 220 82.162 179.408 298.849 1.00 79.01 C ANISOU 2857 CZ ARG A 220 6228 11297 12496 -363 911 -97 C ATOM 2858 NH1 ARG A 220 81.272 178.782 299.609 1.00 78.86 N ANISOU 2858 NH1 ARG A 220 6224 11282 12456 -358 840 -109 N ATOM 2859 NH2 ARG A 220 83.301 179.840 299.379 1.00 78.02 N ANISOU 2859 NH2 ARG A 220 6169 10894 12582 -226 979 -232 N ATOM 2860 N THR A 221 83.355 176.475 293.592 1.00101.60 N ANISOU 2860 N THR A 221 9162 15107 14336 -1384 996 -584 N ATOM 2861 CA THR A 221 84.335 176.436 292.508 1.00 97.49 C ANISOU 2861 CA THR A 221 8660 14679 13703 -1525 1092 -716 C ATOM 2862 C THR A 221 85.755 176.700 293.002 1.00 98.64 C ANISOU 2862 C THR A 221 8890 14479 14111 -1366 1190 -903 C ATOM 2863 O THR A 221 86.712 176.474 292.250 1.00105.53 O ANISOU 2863 O THR A 221 9800 15367 14929 -1473 1284 -1080 O ATOM 2864 CB THR A 221 83.963 177.453 291.418 1.00 82.27 C ANISOU 2864 CB THR A 221 6588 13076 11596 -1603 1087 -391 C ATOM 2865 OG1 THR A 221 84.671 177.154 290.209 1.00 79.95 O ANISOU 2865 OG1 THR A 221 6308 12969 11100 -1814 1168 -532 O ATOM 2866 CG2 THR A 221 84.313 178.869 291.856 1.00 77.02 C ANISOU 2866 CG2 THR A 221 5853 12238 11174 -1359 1112 -154 C ATOM 2867 N GLY A 222 85.907 177.179 294.243 1.00 93.95 N ANISOU 2867 N GLY A 222 8321 13581 13794 -1121 1172 -867 N ATOM 2868 CA GLY A 222 87.212 177.309 294.871 1.00 84.55 C ANISOU 2868 CA GLY A 222 7217 12045 12864 -973 1248 -1058 C ATOM 2869 C GLY A 222 87.905 175.988 295.133 1.00 77.26 C ANISOU 2869 C GLY A 222 6416 10946 11992 -1054 1281 -1420 C ATOM 2870 O GLY A 222 89.115 175.970 295.380 1.00 73.99 O ANISOU 2870 O GLY A 222 6067 10281 11763 -982 1356 -1598 O ATOM 2871 N ARG A 223 87.159 174.880 295.102 1.00 73.66 N ANISOU 2871 N ARG A 223 5985 10606 11398 -1201 1226 -1525 N ATOM 2872 CA ARG A 223 87.777 173.559 295.083 1.00 75.05 C ANISOU 2872 CA ARG A 223 6254 10656 11605 -1322 1271 -1868 C ATOM 2873 C ARG A 223 88.639 173.365 293.834 1.00 75.46 C ANISOU 2873 C ARG A 223 6315 10821 11536 -1494 1390 -2032 C ATOM 2874 O ARG A 223 89.652 172.657 293.882 1.00 78.48 O ANISOU 2874 O ARG A 223 6769 10996 12052 -1523 1473 -2316 O ATOM 2875 CB ARG A 223 86.692 172.485 295.171 1.00 78.63 C ANISOU 2875 CB ARG A 223 6711 11246 11917 -1463 1187 -1919 C ATOM 2876 CG ARG A 223 87.079 171.222 295.921 1.00 82.06 C ANISOU 2876 CG ARG A 223 7233 11423 12523 -1476 1186 -2205 C ATOM 2877 CD ARG A 223 85.940 170.209 295.882 1.00 86.68 C ANISOU 2877 CD ARG A 223 7807 12173 12953 -1631 1103 -2235 C ATOM 2878 NE ARG A 223 85.615 169.792 294.518 1.00 91.70 N ANISOU 2878 NE ARG A 223 8413 13128 13301 -1891 1140 -2300 N ATOM 2879 CZ ARG A 223 86.087 168.690 293.942 1.00 94.35 C ANISOU 2879 CZ ARG A 223 8794 13452 13604 -2080 1217 -2607 C ATOM 2880 NH1 ARG A 223 86.904 167.889 294.615 1.00 94.74 N ANISOU 2880 NH1 ARG A 223 8910 13171 13916 -2029 1260 -2858 N ATOM 2881 NH2 ARG A 223 85.739 168.384 292.696 1.00 95.85 N ANISOU 2881 NH2 ARG A 223 8953 13961 13506 -2329 1252 -2662 N ATOM 2882 N LEU A 224 88.258 173.975 292.704 1.00 74.66 N ANISOU 2882 N LEU A 224 6131 11051 11184 -1615 1403 -1853 N ATOM 2883 CA LEU A 224 89.170 174.024 291.561 1.00 73.63 C ANISOU 2883 CA LEU A 224 6001 11029 10947 -1754 1527 -1978 C ATOM 2884 C LEU A 224 90.299 175.008 291.815 1.00 71.87 C ANISOU 2884 C LEU A 224 5780 10577 10949 -1563 1597 -1929 C ATOM 2885 O LEU A 224 91.444 174.771 291.419 1.00 74.47 O ANISOU 2885 O LEU A 224 6155 10796 11346 -1605 1714 -2145 O ATOM 2886 CB LEU A 224 88.426 174.407 290.279 1.00 74.15 C ANISOU 2886 CB LEU A 224 5967 11544 10663 -1955 1512 -1777 C ATOM 2887 CG LEU A 224 89.249 175.103 289.178 1.00 74.18 C ANISOU 2887 CG LEU A 224 5926 11698 10560 -2031 1618 -1737 C ATOM 2888 CD1 LEU A 224 88.891 174.560 287.807 1.00 76.75 C ANISOU 2888 CD1 LEU A 224 6216 12432 10512 -2352 1653 -1804 C ATOM 2889 CD2 LEU A 224 89.074 176.626 289.204 1.00 74.62 C ANISOU 2889 CD2 LEU A 224 5874 11808 10670 -1866 1577 -1348 C ATOM 2890 N VAL A 225 89.990 176.129 292.466 1.00 68.53 N ANISOU 2890 N VAL A 225 5304 10080 10655 -1355 1534 -1651 N ATOM 2891 CA VAL A 225 91.001 177.133 292.758 1.00 65.21 C ANISOU 2891 CA VAL A 225 4880 9437 10461 -1168 1594 -1591 C ATOM 2892 C VAL A 225 92.078 176.592 293.697 1.00 65.37 C ANISOU 2892 C VAL A 225 5007 9061 10768 -1051 1637 -1863 C ATOM 2893 O VAL A 225 93.166 177.168 293.782 1.00 66.57 O ANISOU 2893 O VAL A 225 5173 9022 11099 -942 1709 -1895 O ATOM 2894 CB VAL A 225 90.302 178.394 293.321 1.00 64.45 C ANISOU 2894 CB VAL A 225 4694 9339 10454 -978 1516 -1245 C ATOM 2895 CG1 VAL A 225 91.292 179.514 293.592 1.00 63.53 C ANISOU 2895 CG1 VAL A 225 4562 9002 10576 -789 1577 -1168 C ATOM 2896 CG2 VAL A 225 89.215 178.866 292.354 1.00 64.59 C ANISOU 2896 CG2 VAL A 225 4587 9755 10199 -1108 1468 -955 C ATOM 2897 N VAL A 226 91.820 175.470 294.380 1.00 61.69 N ANISOU 2897 N VAL A 226 4612 8472 10356 -1080 1593 -2053 N ATOM 2898 CA VAL A 226 92.768 174.921 295.349 1.00 57.82 C ANISOU 2898 CA VAL A 226 4208 7610 10151 -972 1616 -2279 C ATOM 2899 C VAL A 226 93.671 173.849 294.754 1.00 58.11 C ANISOU 2899 C VAL A 226 4298 7579 10202 -1129 1723 -2599 C ATOM 2900 O VAL A 226 94.519 173.303 295.472 1.00 57.11 O ANISOU 2900 O VAL A 226 4231 7143 10326 -1058 1748 -2790 O ATOM 2901 CB VAL A 226 92.050 174.361 296.596 1.00 55.91 C ANISOU 2901 CB VAL A 226 4001 7232 10011 -892 1503 -2283 C ATOM 2902 CG1 VAL A 226 91.578 172.933 296.358 1.00 56.68 C ANISOU 2902 CG1 VAL A 226 4128 7412 9995 -1082 1487 -2480 C ATOM 2903 CG2 VAL A 226 92.963 174.428 297.814 1.00 54.15 C ANISOU 2903 CG2 VAL A 226 3835 6634 10107 -708 1498 -2372 C ATOM 2904 N ILE A 227 93.528 173.526 293.474 1.00 60.28 N ANISOU 2904 N ILE A 227 4547 8134 10224 -1345 1792 -2665 N ATOM 2905 CA ILE A 227 94.481 172.642 292.822 1.00 64.43 C ANISOU 2905 CA ILE A 227 5113 8594 10774 -1492 1924 -2979 C ATOM 2906 C ILE A 227 95.495 173.425 291.998 1.00 65.78 C ANISOU 2906 C ILE A 227 5259 8799 10936 -1493 2046 -2967 C ATOM 2907 O ILE A 227 96.671 173.063 291.962 1.00 66.77 O ANISOU 2907 O ILE A 227 5422 8704 11244 -1487 2156 -3189 O ATOM 2908 CB ILE A 227 93.769 171.567 291.971 1.00 72.22 C ANISOU 2908 CB ILE A 227 6097 9844 11499 -1759 1943 -3137 C ATOM 2909 CG1 ILE A 227 92.834 172.197 290.939 1.00 79.35 C ANISOU 2909 CG1 ILE A 227 6924 11183 12042 -1895 1911 -2908 C ATOM 2910 CG2 ILE A 227 93.026 170.590 292.877 1.00 71.62 C ANISOU 2910 CG2 ILE A 227 6055 9653 11505 -1754 1841 -3211 C ATOM 2911 CD1 ILE A 227 92.216 171.208 289.969 1.00 85.20 C ANISOU 2911 CD1 ILE A 227 7660 12219 12495 -2187 1939 -3072 C ATOM 2912 N ILE A 228 95.081 174.525 291.363 1.00 66.03 N ANISOU 2912 N ILE A 228 5216 9093 10781 -1493 2027 -2693 N ATOM 2913 CA ILE A 228 96.030 175.291 290.559 1.00 65.04 C ANISOU 2913 CA ILE A 228 5056 9013 10643 -1499 2139 -2661 C ATOM 2914 C ILE A 228 97.095 175.963 291.411 1.00 62.24 C ANISOU 2914 C ILE A 228 4726 8294 10628 -1259 2159 -2643 C ATOM 2915 O ILE A 228 98.109 176.425 290.871 1.00 62.27 O ANISOU 2915 O ILE A 228 4715 8257 10686 -1252 2266 -2675 O ATOM 2916 CB ILE A 228 95.297 176.321 289.675 1.00 66.21 C ANISOU 2916 CB ILE A 228 5100 9537 10521 -1561 2103 -2338 C ATOM 2917 CG1 ILE A 228 95.166 177.662 290.389 1.00 67.40 C ANISOU 2917 CG1 ILE A 228 5197 9568 10844 -1315 2025 -2022 C ATOM 2918 CG2 ILE A 228 93.921 175.811 289.288 1.00 65.96 C ANISOU 2918 CG2 ILE A 228 5036 9829 10197 -1735 2016 -2265 C ATOM 2919 CD1 ILE A 228 94.596 178.737 289.504 1.00 70.50 C ANISOU 2919 CD1 ILE A 228 5466 10294 11027 -1364 2002 -1687 C ATOM 2920 N ILE A 229 96.892 176.014 292.729 1.00 62.20 N ANISOU 2920 N ILE A 229 4755 8032 10845 -1073 2059 -2596 N ATOM 2921 CA ILE A 229 97.949 176.428 293.645 1.00 65.08 C ANISOU 2921 CA ILE A 229 5156 8030 11542 -869 2074 -2632 C ATOM 2922 C ILE A 229 98.856 175.256 294.023 1.00 73.04 C ANISOU 2922 C ILE A 229 6238 8763 12752 -902 2137 -2955 C ATOM 2923 O ILE A 229 100.048 175.458 294.274 1.00 69.47 O ANISOU 2923 O ILE A 229 5804 8058 12533 -808 2203 -3041 O ATOM 2924 CB ILE A 229 97.370 177.098 294.911 1.00 67.14 C ANISOU 2924 CB ILE A 229 5414 8148 11947 -661 1945 -2433 C ATOM 2925 CG1 ILE A 229 97.201 176.081 296.049 1.00 67.48 C ANISOU 2925 CG1 ILE A 229 5527 7973 12138 -625 1873 -2591 C ATOM 2926 CG2 ILE A 229 96.046 177.791 294.610 1.00 64.10 C ANISOU 2926 CG2 ILE A 229 4952 8061 11341 -674 1865 -2147 C ATOM 2927 CD1 ILE A 229 97.200 176.689 297.439 1.00 69.46 C ANISOU 2927 CD1 ILE A 229 5794 7983 12614 -407 1783 -2479 C ATOM 2928 N LEU A 230 98.324 174.031 294.061 1.00 77.26 N ANISOU 2928 N LEU A 230 5734 10435 13187 -138 915 2771 N ATOM 2929 CA LEU A 230 99.148 172.887 294.438 1.00 58.44 C ANISOU 2929 CA LEU A 230 3327 7874 11005 -197 851 2776 C ATOM 2930 C LEU A 230 100.035 172.435 293.282 1.00 80.55 C ANISOU 2930 C LEU A 230 6067 10683 13855 -167 832 2651 C ATOM 2931 O LEU A 230 101.220 172.148 293.486 1.00 81.98 O ANISOU 2931 O LEU A 230 6252 10722 14175 -141 784 2673 O ATOM 2932 CB LEU A 230 98.270 171.737 294.934 1.00 59.50 C ANISOU 2932 CB LEU A 230 3402 7998 11206 -323 848 2781 C ATOM 2933 CG LEU A 230 97.474 172.037 296.208 1.00 59.48 C ANISOU 2933 CG LEU A 230 3455 7971 11175 -361 871 2914 C ATOM 2934 CD1 LEU A 230 96.807 170.789 296.765 1.00 60.77 C ANISOU 2934 CD1 LEU A 230 3567 8089 11434 -518 875 2923 C ATOM 2935 CD2 LEU A 230 98.364 172.680 297.252 1.00 58.62 C ANISOU 2935 CD2 LEU A 230 3446 7676 11150 -288 834 3067 C ATOM 2936 N ALA A 231 99.487 172.367 292.065 1.00 78.74 N ANISOU 2936 N ALA A 231 5770 10633 13516 -164 868 2519 N ATOM 2937 CA ALA A 231 100.335 172.146 290.898 1.00 77.02 C ANISOU 2937 CA ALA A 231 5502 10440 13321 -113 863 2408 C ATOM 2938 C ALA A 231 101.404 173.221 290.805 1.00 58.39 C ANISOU 2938 C ALA A 231 3214 8039 10933 -25 873 2438 C ATOM 2939 O ALA A 231 102.552 172.942 290.443 1.00 81.95 O ANISOU 2939 O ALA A 231 6170 10960 14006 6 849 2398 O ATOM 2940 CB ALA A 231 99.494 172.118 289.625 1.00 59.71 C ANISOU 2940 CB ALA A 231 3230 8461 10996 -110 905 2272 C ATOM 2941 N PHE A 232 101.044 174.458 291.146 1.00 57.67 N ANISOU 2941 N PHE A 232 3202 7987 10724 11 915 2516 N ATOM 2942 CA PHE A 232 102.033 175.525 291.197 1.00 57.11 C ANISOU 2942 CA PHE A 232 3194 7863 10643 63 934 2569 C ATOM 2943 C PHE A 232 103.070 175.252 292.280 1.00 57.09 C ANISOU 2943 C PHE A 232 3212 7679 10799 35 869 2652 C ATOM 2944 O PHE A 232 104.278 175.283 292.019 1.00 97.89 O ANISOU 2944 O PHE A 232 8352 12808 16033 51 851 2614 O ATOM 2945 CB PHE A 232 101.337 176.866 291.431 1.00 56.58 C ANISOU 2945 CB PHE A 232 3202 7859 10435 108 999 2669 C ATOM 2946 CG PHE A 232 102.210 178.056 291.166 1.00 56.29 C ANISOU 2946 CG PHE A 232 3214 7802 10371 153 1048 2717 C ATOM 2947 CD1 PHE A 232 103.147 178.465 292.099 1.00 71.02 C ANISOU 2947 CD1 PHE A 232 5123 9529 12332 126 1021 2818 C ATOM 2948 CD2 PHE A 232 102.093 178.769 289.984 1.00 69.64 C ANISOU 2948 CD2 PHE A 232 4895 9618 11946 216 1127 2666 C ATOM 2949 CE1 PHE A 232 103.954 179.556 291.859 1.00 70.71 C ANISOU 2949 CE1 PHE A 232 5110 9482 12276 141 1075 2860 C ATOM 2950 CE2 PHE A 232 102.896 179.864 289.739 1.00 69.76 C ANISOU 2950 CE2 PHE A 232 4948 9610 11946 242 1190 2724 C ATOM 2951 CZ PHE A 232 103.828 180.258 290.679 1.00 70.25 C ANISOU 2951 CZ PHE A 232 5046 9540 12107 194 1167 2818 C ATOM 2952 N ALA A 233 102.615 174.970 293.503 1.00 57.00 N ANISOU 2952 N ALA A 233 3236 7569 10852 -3 833 2763 N ATOM 2953 CA ALA A 233 103.548 174.773 294.609 1.00 72.09 C ANISOU 2953 CA ALA A 233 5164 9309 12919 -18 766 2856 C ATOM 2954 C ALA A 233 104.447 173.564 294.372 1.00 73.64 C ANISOU 2954 C ALA A 233 5270 9437 13273 -20 704 2781 C ATOM 2955 O ALA A 233 105.647 173.609 294.668 1.00 74.79 O ANISOU 2955 O ALA A 233 5389 9515 13514 1 657 2789 O ATOM 2956 CB ALA A 233 102.784 174.628 295.927 1.00 56.95 C ANISOU 2956 CB ALA A 233 3296 7299 11045 -53 746 2996 C ATOM 2957 N ALA A 234 103.891 172.481 293.825 1.00 58.50 N ANISOU 2957 N ALA A 234 3289 7551 11389 -42 704 2707 N ATOM 2958 CA ALA A 234 104.688 171.287 293.566 1.00 59.50 C ANISOU 2958 CA ALA A 234 3321 7605 11682 -25 652 2654 C ATOM 2959 C ALA A 234 105.731 171.501 292.477 1.00 73.54 C ANISOU 2959 C ALA A 234 5045 9470 13425 43 664 2534 C ATOM 2960 O ALA A 234 106.699 170.737 292.409 1.00 74.12 O ANISOU 2960 O ALA A 234 5038 9489 13636 90 615 2502 O ATOM 2961 CB ALA A 234 103.779 170.119 293.186 1.00 60.28 C ANISOU 2961 CB ALA A 234 3357 7713 11833 -81 661 2614 C ATOM 2962 N PHE A 235 105.562 172.518 291.630 1.00 72.83 N ANISOU 2962 N PHE A 235 4989 9521 13163 57 731 2474 N ATOM 2963 CA PHE A 235 106.518 172.788 290.561 1.00 71.95 C ANISOU 2963 CA PHE A 235 4823 9502 13014 111 759 2365 C ATOM 2964 C PHE A 235 107.570 173.814 290.951 1.00 69.13 C ANISOU 2964 C PHE A 235 4485 9135 12647 114 761 2401 C ATOM 2965 O PHE A 235 108.669 173.814 290.385 1.00 67.40 O ANISOU 2965 O PHE A 235 4189 8971 12450 147 763 2321 O ATOM 2966 CB PHE A 235 105.792 173.274 289.302 1.00 59.19 C ANISOU 2966 CB PHE A 235 3212 8041 11235 125 837 2280 C ATOM 2967 CG PHE A 235 105.138 172.176 288.518 1.00 59.82 C ANISOU 2967 CG PHE A 235 3219 8174 11334 126 835 2194 C ATOM 2968 CD1 PHE A 235 105.138 170.877 288.992 1.00 60.58 C ANISOU 2968 CD1 PHE A 235 3259 8164 11595 104 777 2215 C ATOM 2969 CD2 PHE A 235 104.536 172.438 287.302 1.00 59.84 C ANISOU 2969 CD2 PHE A 235 3199 8329 11207 150 893 2101 C ATOM 2970 CE1 PHE A 235 104.541 169.864 288.274 1.00 61.39 C ANISOU 2970 CE1 PHE A 235 3281 8307 11736 87 780 2148 C ATOM 2971 CE2 PHE A 235 103.936 171.428 286.577 1.00 60.59 C ANISOU 2971 CE2 PHE A 235 3211 8485 11327 140 888 2022 C ATOM 2972 CZ PHE A 235 103.941 170.139 287.062 1.00 61.39 C ANISOU 2972 CZ PHE A 235 3254 8476 11596 100 834 2046 C ATOM 2973 N TRP A 236 107.259 174.684 291.902 1.00 58.63 N ANISOU 2973 N TRP A 236 3241 7747 11287 77 763 2519 N ATOM 2974 CA TRP A 236 108.143 175.773 292.277 1.00 58.61 C ANISOU 2974 CA TRP A 236 3253 7742 11276 58 775 2565 C ATOM 2975 C TRP A 236 108.864 175.529 293.592 1.00 90.59 C ANISOU 2975 C TRP A 236 7282 11671 15466 37 683 2647 C ATOM 2976 O TRP A 236 109.732 176.323 293.968 1.00 95.32 O ANISOU 2976 O TRP A 236 7862 12276 16079 7 677 2675 O ATOM 2977 CB TRP A 236 107.347 177.074 292.350 1.00 57.76 C ANISOU 2977 CB TRP A 236 3248 7659 11039 43 851 2655 C ATOM 2978 CG TRP A 236 107.082 177.656 291.008 1.00 57.70 C ANISOU 2978 CG TRP A 236 3239 7784 10902 74 947 2578 C ATOM 2979 CD1 TRP A 236 106.019 177.399 290.189 1.00 74.97 C ANISOU 2979 CD1 TRP A 236 5435 10059 12993 111 986 2524 C ATOM 2980 CD2 TRP A 236 107.906 178.596 290.316 1.00 82.02 C ANISOU 2980 CD2 TRP A 236 6294 10930 13941 66 1019 2550 C ATOM 2981 NE1 TRP A 236 106.130 178.131 289.029 1.00 77.17 N ANISOU 2981 NE1 TRP A 236 5703 10444 13173 145 1074 2470 N ATOM 2982 CE2 TRP A 236 107.282 178.873 289.085 1.00 80.44 C ANISOU 2982 CE2 TRP A 236 6101 10840 13623 115 1104 2491 C ATOM 2983 CE3 TRP A 236 109.114 179.236 290.621 1.00 82.97 C ANISOU 2983 CE3 TRP A 236 6373 11037 14114 13 1025 2567 C ATOM 2984 CZ2 TRP A 236 107.824 179.760 288.160 1.00 82.22 C ANISOU 2984 CZ2 TRP A 236 6308 11141 13791 120 1203 2466 C ATOM 2985 CZ3 TRP A 236 109.657 180.112 289.693 1.00 83.63 C ANISOU 2985 CZ3 TRP A 236 6429 11209 14138 -4 1127 2531 C ATOM 2986 CH2 TRP A 236 109.007 180.369 288.481 1.00 83.25 C ANISOU 2986 CH2 TRP A 236 6403 11249 13980 53 1220 2489 C ATOM 2987 N LEU A 237 108.538 174.465 294.296 1.00 84.88 N ANISOU 2987 N LEU A 237 6552 10843 14856 47 614 2691 N ATOM 2988 CA LEU A 237 109.284 174.209 295.515 1.00 80.36 C ANISOU 2988 CA LEU A 237 5948 10157 14428 44 520 2770 C ATOM 2989 C LEU A 237 110.673 173.660 295.190 1.00 77.61 C ANISOU 2989 C LEU A 237 5460 9863 14165 95 464 2664 C ATOM 2990 O LEU A 237 111.656 174.140 295.771 1.00 61.70 O ANISOU 2990 O LEU A 237 3391 7861 12191 82 415 2678 O ATOM 2991 CB LEU A 237 108.507 173.268 296.437 1.00 59.72 C ANISOU 2991 CB LEU A 237 3365 7397 11930 41 468 2871 C ATOM 2992 CG LEU A 237 109.099 173.158 297.835 1.00 60.21 C ANISOU 2992 CG LEU A 237 3413 7325 12139 41 369 2986 C ATOM 2993 CD1 LEU A 237 109.143 174.532 298.474 1.00 59.55 C ANISOU 2993 CD1 LEU A 237 3402 7243 11980 -8 387 3080 C ATOM 2994 CD2 LEU A 237 108.283 172.195 298.664 1.00 60.33 C ANISOU 2994 CD2 LEU A 237 3453 7187 12282 34 333 3095 C ATOM 2995 N PRO A 238 110.814 172.667 294.284 1.00 74.94 N ANISOU 2995 N PRO A 238 5045 9574 13856 159 467 2555 N ATOM 2996 CA PRO A 238 112.169 172.201 293.932 1.00 73.28 C ANISOU 2996 CA PRO A 238 4688 9447 13707 236 420 2448 C ATOM 2997 C PRO A 238 113.140 173.321 293.620 1.00 63.60 C ANISOU 2997 C PRO A 238 3406 8364 12394 198 455 2387 C ATOM 2998 O PRO A 238 114.288 173.293 294.081 1.00 64.85 O ANISOU 2998 O PRO A 238 3449 8575 12616 224 385 2356 O ATOM 2999 CB PRO A 238 111.933 171.323 292.697 1.00 71.79 C ANISOU 2999 CB PRO A 238 4453 9317 13507 302 461 2343 C ATOM 3000 CG PRO A 238 110.495 170.978 292.695 1.00 62.65 C ANISOU 3000 CG PRO A 238 3394 8071 12341 255 494 2407 C ATOM 3001 CD PRO A 238 109.789 171.737 293.769 1.00 74.34 C ANISOU 3001 CD PRO A 238 4990 9463 13794 172 492 2540 C ATOM 3002 N TYR A 239 112.707 174.316 292.848 1.00 62.74 N ANISOU 3002 N TYR A 239 3364 8329 12147 137 561 2370 N ATOM 3003 CA TYR A 239 113.616 175.399 292.496 1.00 79.66 C ANISOU 3003 CA TYR A 239 5445 10598 14226 82 613 2321 C ATOM 3004 C TYR A 239 113.994 176.218 293.722 1.00 79.58 C ANISOU 3004 C TYR A 239 5447 10533 14256 1 566 2424 C ATOM 3005 O TYR A 239 115.170 176.541 293.923 1.00 82.73 O ANISOU 3005 O TYR A 239 5717 11028 14687 -32 536 2374 O ATOM 3006 CB TYR A 239 112.996 176.291 291.421 1.00 78.58 C ANISOU 3006 CB TYR A 239 5384 10527 13947 45 742 2302 C ATOM 3007 CG TYR A 239 113.730 177.601 291.257 1.00 63.04 C ANISOU 3007 CG TYR A 239 3381 8644 11926 -45 813 2300 C ATOM 3008 CD1 TYR A 239 115.087 177.624 290.965 1.00 64.68 C ANISOU 3008 CD1 TYR A 239 3422 8987 12165 -65 810 2196 C ATOM 3009 CD2 TYR A 239 113.072 178.814 291.403 1.00 76.64 C ANISOU 3009 CD2 TYR A 239 5226 10323 13572 -112 890 2406 C ATOM 3010 CE1 TYR A 239 115.772 178.818 290.823 1.00 65.46 C ANISOU 3010 CE1 TYR A 239 3474 9173 12224 -181 888 2193 C ATOM 3011 CE2 TYR A 239 113.750 180.017 291.258 1.00 77.72 C ANISOU 3011 CE2 TYR A 239 5332 10525 13674 -212 969 2418 C ATOM 3012 CZ TYR A 239 115.101 180.009 290.966 1.00 64.56 C ANISOU 3012 CZ TYR A 239 3496 8988 12044 -263 970 2308 C ATOM 3013 OH TYR A 239 115.789 181.192 290.825 1.00 65.57 O ANISOU 3013 OH TYR A 239 3583 9190 12140 -398 1061 2313 O ATOM 3014 N HIS A 240 113.018 176.546 294.566 1.00 77.69 N ANISOU 3014 N HIS A 240 5347 10155 14017 -31 557 2565 N ATOM 3015 CA HIS A 240 113.281 177.519 295.620 1.00 76.98 C ANISOU 3015 CA HIS A 240 5285 10014 13950 -115 531 2677 C ATOM 3016 C HIS A 240 114.102 176.949 296.762 1.00 79.78 C ANISOU 3016 C HIS A 240 5543 10323 14445 -100 392 2701 C ATOM 3017 O HIS A 240 114.847 177.695 297.406 1.00 81.93 O ANISOU 3017 O HIS A 240 5759 10625 14744 -178 355 2732 O ATOM 3018 CB HIS A 240 111.972 178.085 296.147 1.00 73.51 C ANISOU 3018 CB HIS A 240 5018 9455 13459 -133 570 2828 C ATOM 3019 CG HIS A 240 111.428 179.181 295.296 1.00 60.08 C ANISOU 3019 CG HIS A 240 3394 7817 11616 -161 702 2837 C ATOM 3020 ND1 HIS A 240 111.506 180.508 295.655 1.00 60.07 N ANISOU 3020 ND1 HIS A 240 3445 7806 11573 -236 756 2935 N ATOM 3021 CD2 HIS A 240 110.841 179.152 294.078 1.00 81.20 C ANISOU 3021 CD2 HIS A 240 6096 10570 14187 -118 791 2762 C ATOM 3022 CE1 HIS A 240 110.963 181.248 294.705 1.00 85.85 C ANISOU 3022 CE1 HIS A 240 6771 11132 14717 -226 880 2931 C ATOM 3023 NE2 HIS A 240 110.553 180.449 293.737 1.00 82.99 N ANISOU 3023 NE2 HIS A 240 6391 10828 14313 -152 898 2824 N ATOM 3024 N VAL A 241 113.977 175.653 297.041 1.00 63.53 N ANISOU 3024 N VAL A 241 3460 8196 12483 -5 311 2691 N ATOM 3025 CA VAL A 241 114.802 175.058 298.086 1.00 64.81 C ANISOU 3025 CA VAL A 241 3519 8323 12781 41 169 2709 C ATOM 3026 C VAL A 241 116.277 175.236 297.756 1.00 66.65 C ANISOU 3026 C VAL A 241 3557 8755 13011 47 134 2571 C ATOM 3027 O VAL A 241 117.101 175.487 298.643 1.00 67.82 O ANISOU 3027 O VAL A 241 3609 8938 13220 25 34 2586 O ATOM 3028 CB VAL A 241 114.423 173.581 298.289 1.00 65.02 C ANISOU 3028 CB VAL A 241 3547 8239 12918 160 101 2719 C ATOM 3029 CG1 VAL A 241 115.600 172.795 298.832 1.00 66.96 C ANISOU 3029 CG1 VAL A 241 3637 8527 13277 275 -42 2661 C ATOM 3030 CG2 VAL A 241 113.239 173.485 299.235 1.00 63.82 C ANISOU 3030 CG2 VAL A 241 3542 7885 12820 127 90 2891 C ATOM 3031 N VAL A 242 116.629 175.150 296.472 1.00 67.09 N ANISOU 3031 N VAL A 242 3539 8963 12989 72 217 2432 N ATOM 3032 CA VAL A 242 118.013 175.391 296.073 1.00 84.79 C ANISOU 3032 CA VAL A 242 5577 11428 15213 65 207 2293 C ATOM 3033 C VAL A 242 118.396 176.842 296.344 1.00 91.21 C ANISOU 3033 C VAL A 242 6375 12303 15977 -113 254 2325 C ATOM 3034 O VAL A 242 119.455 177.122 296.919 1.00 97.29 O ANISOU 3034 O VAL A 242 6985 13193 16787 -160 178 2283 O ATOM 3035 CB VAL A 242 118.227 175.013 294.597 1.00 79.85 C ANISOU 3035 CB VAL A 242 4882 10943 14514 127 300 2150 C ATOM 3036 CG1 VAL A 242 119.622 175.415 294.161 1.00 79.42 C ANISOU 3036 CG1 VAL A 242 4605 11141 14429 96 313 2009 C ATOM 3037 CG2 VAL A 242 118.021 173.522 294.403 1.00 69.71 C ANISOU 3037 CG2 VAL A 242 3585 9604 13296 305 238 2117 C ATOM 3038 N ASP A 243 117.541 177.787 295.937 1.00 67.74 N ANISOU 3038 N ASP A 243 3561 9261 12918 -211 378 2399 N ATOM 3039 CA ASP A 243 117.759 179.184 296.308 1.00 67.96 C ANISOU 3039 CA ASP A 243 3608 9303 12909 -382 427 2464 C ATOM 3040 C ASP A 243 117.857 179.336 297.816 1.00 79.29 C ANISOU 3040 C ASP A 243 5054 10633 14438 -423 298 2584 C ATOM 3041 O ASP A 243 118.653 180.134 298.323 1.00 78.72 O ANISOU 3041 O ASP A 243 4890 10639 14381 -559 271 2585 O ATOM 3042 CB ASP A 243 116.631 180.065 295.778 1.00 66.25 C ANISOU 3042 CB ASP A 243 3589 8994 12589 -430 566 2555 C ATOM 3043 CG ASP A 243 116.737 180.314 294.302 1.00 92.07 C ANISOU 3043 CG ASP A 243 6830 12391 15760 -435 702 2443 C ATOM 3044 OD1 ASP A 243 117.757 179.907 293.704 1.00 93.45 O ANISOU 3044 OD1 ASP A 243 6826 12733 15946 -424 699 2296 O ATOM 3045 OD2 ASP A 243 115.805 180.928 293.744 1.00 90.65 O ANISOU 3045 OD2 ASP A 243 6798 12154 15490 -440 812 2505 O ATOM 3046 N LEU A 244 117.042 178.579 298.548 1.00 79.82 N ANISOU 3046 N LEU A 244 5231 10524 14572 -321 220 2689 N ATOM 3047 CA LEU A 244 117.100 178.619 299.999 1.00 67.26 C ANISOU 3047 CA LEU A 244 3652 8820 13084 -341 89 2813 C ATOM 3048 C LEU A 244 118.360 177.939 300.523 1.00 85.85 C ANISOU 3048 C LEU A 244 5793 11294 15531 -283 -66 2715 C ATOM 3049 O LEU A 244 118.903 178.360 301.550 1.00 87.68 O ANISOU 3049 O LEU A 244 5960 11530 15824 -353 -176 2767 O ATOM 3050 CB LEU A 244 115.854 177.955 300.584 1.00 65.64 C ANISOU 3050 CB LEU A 244 3615 8398 12926 -252 63 2951 C ATOM 3051 CG LEU A 244 115.297 178.536 301.882 1.00 64.98 C ANISOU 3051 CG LEU A 244 3645 8149 12894 -312 10 3147 C ATOM 3052 CD1 LEU A 244 114.644 179.884 301.622 1.00 63.93 C ANISOU 3052 CD1 LEU A 244 3646 7999 12645 -418 144 3235 C ATOM 3053 CD2 LEU A 244 114.318 177.562 302.531 1.00 69.92 C ANISOU 3053 CD2 LEU A 244 4375 8591 13599 -211 -37 3256 C ATOM 3054 N VAL A 245 118.846 176.900 299.836 1.00 85.95 N ANISOU 3054 N VAL A 245 5687 11419 15550 -145 -86 2572 N ATOM 3055 CA VAL A 245 119.997 176.173 300.360 1.00 72.52 C ANISOU 3055 CA VAL A 245 3781 9849 13924 -37 -244 2477 C ATOM 3056 C VAL A 245 121.304 176.819 299.912 1.00 84.50 C ANISOU 3056 C VAL A 245 5066 11653 15386 -130 -228 2322 C ATOM 3057 O VAL A 245 122.320 176.706 300.604 1.00 82.50 O ANISOU 3057 O VAL A 245 4625 11542 15178 -105 -368 2260 O ATOM 3058 CB VAL A 245 119.940 174.687 299.958 1.00 72.83 C ANISOU 3058 CB VAL A 245 3797 9874 14002 185 -288 2406 C ATOM 3059 CG1 VAL A 245 120.795 174.417 298.727 1.00 86.87 C ANISOU 3059 CG1 VAL A 245 5398 11900 15707 247 -226 2215 C ATOM 3060 CG2 VAL A 245 120.391 173.820 301.115 1.00 74.21 C ANISOU 3060 CG2 VAL A 245 3908 10002 14285 344 -487 2430 C ATOM 3061 N GLU A 246 121.309 177.505 298.767 1.00 77.16 N ANISOU 3061 N GLU A 246 4136 10825 14357 -241 -62 2254 N ATOM 3062 CA GLU A 246 122.531 178.160 298.318 1.00 76.63 C ANISOU 3062 CA GLU A 246 3841 11033 14241 -363 -25 2106 C ATOM 3063 C GLU A 246 122.872 179.342 299.217 1.00 77.37 C ANISOU 3063 C GLU A 246 3913 11135 14350 -586 -57 2175 C ATOM 3064 O GLU A 246 123.997 179.449 299.713 1.00 80.66 O ANISOU 3064 O GLU A 246 4100 11752 14794 -639 -160 2081 O ATOM 3065 CB GLU A 246 122.393 178.590 296.857 1.00 92.59 C ANISOU 3065 CB GLU A 246 5886 13136 16157 -427 169 2028 C ATOM 3066 CG GLU A 246 123.371 177.877 295.929 1.00 97.43 C ANISOU 3066 CG GLU A 246 6266 14008 16745 -314 181 1830 C ATOM 3067 CD GLU A 246 122.996 177.974 294.460 1.00100.62 C ANISOU 3067 CD GLU A 246 6734 14437 17061 -314 354 1775 C ATOM 3068 OE1 GLU A 246 122.902 179.102 293.938 1.00101.20 O ANISOU 3068 OE1 GLU A 246 6857 14527 17066 -502 496 1787 O ATOM 3069 OE2 GLU A 246 122.797 176.917 293.823 1.00103.05 O ANISOU 3069 OE2 GLU A 246 7044 14744 17368 -124 346 1722 O ATOM 3070 N GLY A 247 121.900 180.219 299.471 1.00 75.47 N ANISOU 3070 N GLY A 247 3903 10685 14088 -712 20 2340 N ATOM 3071 CA GLY A 247 122.149 181.344 300.358 1.00 90.22 C ANISOU 3071 CA GLY A 247 5778 12531 15969 -931 -12 2425 C ATOM 3072 C GLY A 247 122.516 180.917 301.768 1.00 92.28 C ANISOU 3072 C GLY A 247 5962 12760 16341 -879 -233 2478 C ATOM 3073 O GLY A 247 123.341 181.556 302.427 1.00 95.30 O ANISOU 3073 O GLY A 247 6209 13258 16741 -1046 -315 2453 O ATOM 3074 N SER A 248 121.914 179.827 302.249 1.00 75.96 N ANISOU 3074 N SER A 248 3980 10536 14347 -658 -335 2549 N ATOM 3075 CA SER A 248 122.248 179.325 303.578 1.00 76.95 C ANISOU 3075 CA SER A 248 4040 10619 14580 -575 -556 2602 C ATOM 3076 C SER A 248 123.667 178.770 303.613 1.00 79.95 C ANISOU 3076 C SER A 248 4114 11295 14969 -489 -688 2404 C ATOM 3077 O SER A 248 124.437 179.061 304.537 1.00 81.88 O ANISOU 3077 O SER A 248 4215 11645 15252 -554 -847 2387 O ATOM 3078 CB SER A 248 121.243 178.252 304.000 1.00 98.61 C ANISOU 3078 CB SER A 248 6958 13116 17394 -363 -612 2719 C ATOM 3079 OG SER A 248 121.336 177.106 303.170 1.00 98.92 O ANISOU 3079 OG SER A 248 6944 13223 17417 -167 -586 2595 O ATOM 3080 N ARG A 249 124.032 177.977 302.606 1.00 95.94 N ANISOU 3080 N ARG A 249 6028 13474 16951 -336 -631 2250 N ATOM 3081 CA ARG A 249 125.321 177.301 302.544 1.00 97.96 C ANISOU 3081 CA ARG A 249 5988 14032 17200 -193 -748 2055 C ATOM 3082 C ARG A 249 126.377 178.103 301.781 1.00 99.09 C ANISOU 3082 C ARG A 249 5885 14500 17265 -383 -650 1878 C ATOM 3083 O ARG A 249 127.412 177.542 301.401 1.00 88.16 O ANISOU 3083 O ARG A 249 4234 13409 15854 -258 -698 1689 O ATOM 3084 CB ARG A 249 125.152 175.913 301.919 1.00 83.24 C ANISOU 3084 CB ARG A 249 4138 12156 15335 100 -750 1990 C ATOM 3085 CG ARG A 249 124.056 175.070 302.571 1.00 81.25 C ANISOU 3085 CG ARG A 249 4137 11574 15162 262 -820 2155 C ATOM 3086 CD ARG A 249 124.627 173.881 303.319 1.00 83.15 C ANISOU 3086 CD ARG A 249 4286 11857 15451 553 -1034 2106 C ATOM 3087 NE ARG A 249 124.170 172.615 302.756 1.00 82.59 N ANISOU 3087 NE ARG A 249 4312 11678 15389 790 -1009 2091 N ATOM 3088 CZ ARG A 249 124.663 172.073 301.648 1.00 83.62 C ANISOU 3088 CZ ARG A 249 4315 12000 15457 911 -939 1939 C ATOM 3089 NH1 ARG A 249 125.625 172.690 300.978 1.00 85.26 N ANISOU 3089 NH1 ARG A 249 4285 12523 15588 815 -878 1784 N ATOM 3090 NH2 ARG A 249 124.191 170.918 301.205 1.00 83.17 N ANISOU 3090 NH2 ARG A 249 4366 11815 15419 1119 -928 1943 N ATOM 3091 N VAL A 250 126.132 179.392 301.541 1.00 98.89 N ANISOU 3091 N VAL A 250 5944 14429 17199 -678 -507 1934 N ATOM 3092 CA VAL A 250 127.119 180.305 300.975 1.00102.41 C ANISOU 3092 CA VAL A 250 6175 15154 17581 -920 -408 1781 C ATOM 3093 C VAL A 250 127.688 181.232 302.042 1.00105.83 C ANISOU 3093 C VAL A 250 6516 15651 18042 -1166 -514 1803 C ATOM 3094 O VAL A 250 128.430 182.170 301.724 1.00109.93 O ANISOU 3094 O VAL A 250 6888 16366 18515 -1441 -423 1693 O ATOM 3095 CB VAL A 250 126.535 181.109 299.799 1.00 85.77 C ANISOU 3095 CB VAL A 250 4231 12967 15391 -1086 -154 1805 C ATOM 3096 CG1 VAL A 250 125.662 182.232 300.306 1.00 83.99 C ANISOU 3096 CG1 VAL A 250 4273 12482 15157 -1301 -91 2002 C ATOM 3097 CG2 VAL A 250 127.636 181.626 298.873 1.00 88.44 C ANISOU 3097 CG2 VAL A 250 4314 13624 15665 -1259 -27 1598 C ATOM 3098 N LEU A 251 127.353 180.995 303.308 1.00103.91 N ANISOU 3098 N LEU A 251 6364 15242 17876 -1090 -705 1940 N ATOM 3099 CA LEU A 251 128.010 181.663 304.419 1.00 90.62 C ANISOU 3099 CA LEU A 251 4561 13648 16224 -1282 -863 1943 C ATOM 3100 C LEU A 251 128.971 180.758 305.171 1.00 93.26 C ANISOU 3100 C LEU A 251 4624 14213 16598 -1065 -1116 1816 C ATOM 3101 O LEU A 251 129.954 181.250 305.727 1.00100.71 O ANISOU 3101 O LEU A 251 5334 15396 17535 -1227 -1233 1707 O ATOM 3102 CB LEU A 251 126.964 182.234 305.381 1.00 88.36 C ANISOU 3102 CB LEU A 251 4578 13009 15987 -1382 -909 2200 C ATOM 3103 CG LEU A 251 126.147 183.298 304.648 1.00 86.38 C ANISOU 3103 CG LEU A 251 4575 12581 15665 -1606 -659 2305 C ATOM 3104 CD1 LEU A 251 124.974 183.771 305.478 1.00 83.96 C ANISOU 3104 CD1 LEU A 251 4584 11923 15394 -1652 -680 2565 C ATOM 3105 CD2 LEU A 251 127.047 184.460 304.271 1.00 88.89 C ANISOU 3105 CD2 LEU A 251 4753 13115 15905 -1960 -552 2177 C ATOM 3106 N ALA A 252 128.725 179.452 305.181 1.00 92.53 N ANISOU 3106 N ALA A 252 4559 14063 16534 -702 -1202 1817 N ATOM 3107 CA ALA A 252 129.722 178.459 305.564 1.00 95.36 C ANISOU 3107 CA ALA A 252 4649 14692 16891 -426 -1407 1654 C ATOM 3108 C ALA A 252 129.937 177.527 304.379 1.00109.63 C ANISOU 3108 C ALA A 252 6362 16644 18648 -189 -1299 1510 C ATOM 3109 O ALA A 252 128.996 176.861 303.932 1.00108.12 O ANISOU 3109 O ALA A 252 6407 16202 18470 -27 -1217 1612 O ATOM 3110 CB ALA A 252 129.286 177.675 306.802 1.00 94.72 C ANISOU 3110 CB ALA A 252 4717 14393 16880 -173 -1641 1791 C ATOM 3111 N GLY A 253 131.164 177.496 303.863 1.00111.09 N ANISOU 3111 N GLY A 253 6197 17235 18778 -183 -1300 1268 N ATOM 3112 CA GLY A 253 131.500 176.677 302.709 1.00110.48 C ANISOU 3112 CA GLY A 253 5997 17330 18652 33 -1203 1114 C ATOM 3113 C GLY A 253 130.618 176.886 301.488 1.00106.80 C ANISOU 3113 C GLY A 253 5752 16668 18161 -66 -945 1186 C ATOM 3114 O GLY A 253 131.019 176.606 300.356 1.00 97.54 O ANISOU 3114 O GLY A 253 4445 15676 16938 -5 -823 1039 O ATOM 3115 N ASP A 256 132.358 174.678 294.962 1.00100.73 N ANISOU 3115 N ASP A 256 4387 16712 17175 473 -300 441 N ATOM 3116 CA ASP A 256 133.465 173.759 295.203 1.00112.91 C ANISOU 3116 CA ASP A 256 5614 18531 18754 777 -468 237 C ATOM 3117 C ASP A 256 133.333 172.496 294.354 1.00112.63 C ANISOU 3117 C ASP A 256 5624 18473 18697 1131 -465 192 C ATOM 3118 O ASP A 256 133.054 172.562 293.156 1.00110.11 O ANISOU 3118 O ASP A 256 5366 18121 18348 1077 -286 177 O ATOM 3119 CB ASP A 256 133.539 173.400 296.680 1.00104.79 C ANISOU 3119 CB ASP A 256 4593 17473 17750 921 -713 305 C ATOM 3120 N GLN A 257 133.553 171.342 294.984 1.00117.49 N ANISOU 3120 N GLN A 257 6214 19100 19326 1505 -669 169 N ATOM 3121 CA GLN A 257 133.329 170.048 294.355 1.00118.23 C ANISOU 3121 CA GLN A 257 6405 19115 19402 1868 -692 156 C ATOM 3122 C GLN A 257 132.128 169.309 294.921 1.00115.40 C ANISOU 3122 C GLN A 257 6427 18399 19022 2018 -760 404 C ATOM 3123 O GLN A 257 131.467 168.575 294.183 1.00112.72 O ANISOU 3123 O GLN A 257 6279 17880 18669 2160 -690 467 O ATOM 3124 CB GLN A 257 134.573 169.160 294.494 1.00123.76 C ANISOU 3124 CB GLN A 257 6884 19981 20157 2202 -858 -55 C ATOM 3125 N SER A 258 131.833 169.492 296.213 1.00116.28 N ANISOU 3125 N SER A 258 6645 18381 19157 1976 -893 536 N ATOM 3126 CA SER A 258 130.623 168.919 296.798 1.00114.07 C ANISOU 3126 CA SER A 258 6730 17699 18912 2055 -938 767 C ATOM 3127 C SER A 258 129.382 169.683 296.351 1.00110.13 C ANISOU 3127 C SER A 258 6499 16903 18442 1721 -748 935 C ATOM 3128 O SER A 258 128.325 169.083 296.118 1.00106.08 O ANISOU 3128 O SER A 258 6257 16085 17962 1783 -704 1065 O ATOM 3129 CB SER A 258 130.734 168.912 298.324 1.00 99.46 C ANISOU 3129 CB SER A 258 4903 15794 17094 2117 -1143 843 C ATOM 3130 OG SER A 258 131.104 170.189 298.820 1.00 99.76 O ANISOU 3130 OG SER A 258 4796 15966 17142 1792 -1133 827 O ATOM 3131 N LYS A 259 129.491 171.004 296.225 1.00111.35 N ANISOU 3131 N LYS A 259 6582 17143 18584 1373 -637 926 N ATOM 3132 CA LYS A 259 128.397 171.840 295.753 1.00108.47 C ANISOU 3132 CA LYS A 259 6462 16530 18222 1080 -458 1064 C ATOM 3133 C LYS A 259 128.326 171.931 294.230 1.00110.96 C ANISOU 3133 C LYS A 259 6763 16919 18476 1035 -268 983 C ATOM 3134 O LYS A 259 127.494 172.682 293.709 1.00110.72 O ANISOU 3134 O LYS A 259 6920 16723 18426 811 -116 1074 O ATOM 3135 CB LYS A 259 128.513 173.247 296.355 1.00106.98 C ANISOU 3135 CB LYS A 259 6241 16367 18038 746 -428 1106 C ATOM 3136 N GLN A 260 129.166 171.187 293.501 1.00112.80 N ANISOU 3136 N GLN A 260 6785 17395 18677 1260 -278 813 N ATOM 3137 CA GLN A 260 129.092 171.179 292.044 1.00 93.00 C ANISOU 3137 CA GLN A 260 4270 14945 16120 1244 -107 739 C ATOM 3138 C GLN A 260 127.831 170.508 291.523 1.00 90.25 C ANISOU 3138 C GLN A 260 4226 14284 15780 1328 -53 874 C ATOM 3139 O GLN A 260 127.555 170.595 290.322 1.00 89.55 O ANISOU 3139 O GLN A 260 4180 14198 15648 1286 93 843 O ATOM 3140 CB GLN A 260 130.320 170.484 291.451 1.00103.95 C ANISOU 3140 CB GLN A 260 5346 16659 17490 1492 -144 516 C ATOM 3141 N GLN A 261 127.070 169.838 292.392 1.00 88.88 N ANISOU 3141 N GLN A 261 4254 13846 15669 1440 -166 1015 N ATOM 3142 CA GLN A 261 125.819 169.209 291.985 1.00102.69 C ANISOU 3142 CA GLN A 261 6278 15292 17449 1485 -115 1136 C ATOM 3143 C GLN A 261 124.661 170.199 291.950 1.00100.00 C ANISOU 3143 C GLN A 261 6165 14728 17102 1187 3 1275 C ATOM 3144 O GLN A 261 123.719 170.012 291.169 1.00 99.78 O ANISOU 3144 O GLN A 261 6307 14542 17063 1161 101 1326 O ATOM 3145 CB GLN A 261 125.490 168.040 292.925 1.00101.96 C ANISOU 3145 CB GLN A 261 6299 15000 17440 1726 -277 1222 C ATOM 3146 CG GLN A 261 124.010 167.609 292.983 1.00 98.32 C ANISOU 3146 CG GLN A 261 6137 14169 17050 1679 -241 1388 C ATOM 3147 CD GLN A 261 123.518 166.904 291.724 1.00 83.46 C ANISOU 3147 CD GLN A 261 4325 12229 15158 1773 -141 1360 C ATOM 3148 OE1 GLN A 261 123.944 167.211 290.612 1.00 93.79 O ANISOU 3148 OE1 GLN A 261 5520 13729 16387 1749 -35 1250 O ATOM 3149 NE2 GLN A 261 122.610 165.952 291.901 1.00 82.60 N ANISOU 3149 NE2 GLN A 261 4398 11848 15139 1875 -175 1461 N ATOM 3150 N LEU A 262 124.716 171.256 292.766 1.00 97.62 N ANISOU 3150 N LEU A 262 5866 14422 16805 975 -9 1331 N ATOM 3151 CA LEU A 262 123.583 172.168 292.885 1.00 80.08 C ANISOU 3151 CA LEU A 262 3880 11974 14574 738 84 1474 C ATOM 3152 C LEU A 262 123.162 172.716 291.528 1.00 92.57 C ANISOU 3152 C LEU A 262 5526 13577 16068 626 264 1441 C ATOM 3153 O LEU A 262 122.014 172.545 291.111 1.00 90.76 O ANISOU 3153 O LEU A 262 5505 13150 15829 615 325 1524 O ATOM 3154 CB LEU A 262 123.909 173.308 293.849 1.00 80.27 C ANISOU 3154 CB LEU A 262 3864 12030 14605 536 53 1520 C ATOM 3155 CG LEU A 262 123.295 173.089 295.231 1.00 90.39 C ANISOU 3155 CG LEU A 262 5292 13076 15975 553 -76 1673 C ATOM 3156 CD1 LEU A 262 124.234 172.259 296.098 1.00 93.09 C ANISOU 3156 CD1 LEU A 262 5457 13536 16376 760 -264 1612 C ATOM 3157 CD2 LEU A 262 122.942 174.406 295.893 1.00 78.02 C ANISOU 3157 CD2 LEU A 262 3822 11420 14403 304 -41 1783 C ATOM 3158 N ARG A 263 124.085 173.365 290.814 1.00 80.63 N ANISOU 3158 N ARG A 263 3826 12318 14493 545 350 1314 N ATOM 3159 CA ARG A 263 123.736 173.875 289.493 1.00 79.84 C ANISOU 3159 CA ARG A 263 3785 12239 14311 457 520 1283 C ATOM 3160 C ARG A 263 123.308 172.753 288.554 1.00 79.50 C ANISOU 3160 C ARG A 263 3794 12148 14264 656 537 1250 C ATOM 3161 O ARG A 263 122.448 172.966 287.695 1.00111.56 O ANISOU 3161 O ARG A 263 8008 16105 18273 606 644 1287 O ATOM 3162 CB ARG A 263 124.899 174.659 288.890 1.00101.97 C ANISOU 3162 CB ARG A 263 6352 15329 17063 340 614 1144 C ATOM 3163 CG ARG A 263 124.515 175.448 287.640 1.00101.14 C ANISOU 3163 CG ARG A 263 6330 15224 16875 209 803 1137 C ATOM 3164 CD ARG A 263 123.919 176.814 287.979 1.00 79.77 C ANISOU 3164 CD ARG A 263 3789 12384 14135 -39 886 1255 C ATOM 3165 NE ARG A 263 122.657 177.074 287.288 1.00 77.35 N ANISOU 3165 NE ARG A 263 3735 11881 13772 -50 981 1352 N ATOM 3166 CZ ARG A 263 122.549 177.369 285.994 1.00 84.13 C ANISOU 3166 CZ ARG A 263 4607 12797 14561 -65 1124 1306 C ATOM 3167 NH1 ARG A 263 123.629 177.429 285.228 1.00 86.43 N ANISOU 3167 NH1 ARG A 263 4678 13327 14833 -80 1201 1167 N ATOM 3168 NH2 ARG A 263 121.355 177.594 285.462 1.00 81.81 N ANISOU 3168 NH2 ARG A 263 4535 12332 14216 -58 1191 1394 N ATOM 3169 N ASN A 264 123.877 171.553 288.700 1.00 81.15 N ANISOU 3169 N ASN A 264 3878 12432 14524 895 428 1183 N ATOM 3170 CA ASN A 264 123.376 170.422 287.921 1.00 80.85 C ANISOU 3170 CA ASN A 264 3914 12307 14499 1088 435 1173 C ATOM 3171 C ASN A 264 122.009 169.976 288.423 1.00 82.02 C ANISOU 3171 C ASN A 264 4315 12143 14704 1078 397 1326 C ATOM 3172 O ASN A 264 121.162 169.535 287.636 1.00 77.38 O ANISOU 3172 O ASN A 264 3850 11442 14110 1109 458 1349 O ATOM 3173 CB ASN A 264 124.371 169.261 287.958 1.00 83.53 C ANISOU 3173 CB ASN A 264 4061 12802 14874 1375 329 1064 C ATOM 3174 N ALA A 265 121.773 170.087 289.732 1.00 77.89 N ANISOU 3174 N ALA A 265 3860 11490 14245 1028 299 1427 N ATOM 3175 CA ALA A 265 120.457 169.791 290.283 1.00 86.11 C ANISOU 3175 CA ALA A 265 5128 12244 15346 984 276 1575 C ATOM 3176 C ALA A 265 119.498 170.962 290.114 1.00 73.47 C ANISOU 3176 C ALA A 265 3693 10550 13673 753 386 1655 C ATOM 3177 O ALA A 265 118.294 170.753 289.939 1.00 71.76 O ANISOU 3177 O ALA A 265 3646 10161 13460 719 421 1733 O ATOM 3178 CB ALA A 265 120.576 169.414 291.760 1.00 86.77 C ANISOU 3178 CB ALA A 265 5221 12215 15531 1041 127 1658 C ATOM 3179 N ARG A 266 120.006 172.192 290.163 1.00 73.63 N ANISOU 3179 N ARG A 266 3659 10690 13626 601 439 1634 N ATOM 3180 CA ARG A 266 119.147 173.345 289.925 1.00 71.74 C ANISOU 3180 CA ARG A 266 3581 10369 13308 419 548 1709 C ATOM 3181 C ARG A 266 118.668 173.389 288.481 1.00 85.13 C ANISOU 3181 C ARG A 266 5324 12104 14919 429 672 1653 C ATOM 3182 O ARG A 266 117.564 173.871 288.218 1.00 83.61 O ANISOU 3182 O ARG A 266 5302 11798 14669 354 738 1725 O ATOM 3183 CB ARG A 266 119.889 174.630 290.295 1.00 85.77 C ANISOU 3183 CB ARG A 266 5278 12260 15050 257 582 1702 C ATOM 3184 CG ARG A 266 119.126 175.915 290.062 1.00 70.87 C ANISOU 3184 CG ARG A 266 3550 10295 13081 90 699 1784 C ATOM 3185 CD ARG A 266 119.636 176.986 290.995 1.00 71.40 C ANISOU 3185 CD ARG A 266 3582 10383 13162 -68 685 1837 C ATOM 3186 NE ARG A 266 119.979 178.217 290.298 1.00 93.44 N ANISOU 3186 NE ARG A 266 6346 13283 15875 -224 827 1807 N ATOM 3187 CZ ARG A 266 120.624 179.228 290.868 1.00 94.46 C ANISOU 3187 CZ ARG A 266 6408 13475 16009 -396 845 1824 C ATOM 3188 NH1 ARG A 266 120.992 179.137 292.140 1.00 95.26 N ANISOU 3188 NH1 ARG A 266 6455 13551 16187 -418 715 1866 N ATOM 3189 NH2 ARG A 266 120.901 180.322 290.168 1.00 93.13 N ANISOU 3189 NH2 ARG A 266 6225 13392 15770 -553 994 1801 N ATOM 3190 N LYS A 267 119.468 172.865 287.545 1.00 86.52 N ANISOU 3190 N LYS A 267 5343 12448 15081 537 698 1525 N ATOM 3191 CA LYS A 267 119.105 172.900 286.130 1.00 72.47 C ANISOU 3191 CA LYS A 267 3593 10716 13225 556 814 1468 C ATOM 3192 C LYS A 267 117.749 172.252 285.878 1.00 84.49 C ANISOU 3192 C LYS A 267 5288 12062 14754 601 809 1532 C ATOM 3193 O LYS A 267 116.936 172.779 285.111 1.00 83.02 O ANISOU 3193 O LYS A 267 5209 11850 14484 542 900 1547 O ATOM 3194 CB LYS A 267 120.184 172.209 285.294 1.00 74.67 C ANISOU 3194 CB LYS A 267 3669 11192 13510 703 824 1327 C ATOM 3195 CG LYS A 267 121.334 173.104 284.855 1.00 76.35 C ANISOU 3195 CG LYS A 267 3704 11634 13670 617 908 1230 C ATOM 3196 CD LYS A 267 122.457 172.275 284.238 1.00 89.33 C ANISOU 3196 CD LYS A 267 5122 13490 15331 795 895 1086 C ATOM 3197 CE LYS A 267 123.742 173.083 284.078 1.00 91.43 C ANISOU 3197 CE LYS A 267 5159 14014 15567 696 959 979 C ATOM 3198 NZ LYS A 267 124.829 172.305 283.409 1.00 94.13 N ANISOU 3198 NZ LYS A 267 5261 14587 15917 883 956 824 N ATOM 3199 N VAL A 268 117.485 171.109 286.514 1.00 84.88 N ANISOU 3199 N VAL A 268 5351 11994 14904 707 704 1571 N ATOM 3200 CA VAL A 268 116.218 170.415 286.300 1.00 83.68 C ANISOU 3200 CA VAL A 268 5331 11687 14778 729 703 1626 C ATOM 3201 C VAL A 268 115.091 171.089 287.077 1.00 67.76 C ANISOU 3201 C VAL A 268 3484 9525 12736 587 704 1749 C ATOM 3202 O VAL A 268 114.005 171.326 286.535 1.00 66.53 O ANISOU 3202 O VAL A 268 3437 9331 12511 535 765 1771 O ATOM 3203 CB VAL A 268 116.360 168.920 286.656 1.00 84.72 C ANISOU 3203 CB VAL A 268 5407 11732 15049 894 604 1630 C ATOM 3204 CG1 VAL A 268 117.357 168.720 287.786 1.00 72.09 C ANISOU 3204 CG1 VAL A 268 3712 10149 13529 961 496 1641 C ATOM 3205 CG2 VAL A 268 115.007 168.315 287.012 1.00 69.62 C ANISOU 3205 CG2 VAL A 268 3627 9616 13208 856 582 1730 C ATOM 3206 N CYS A 269 115.336 171.424 288.348 1.00 67.62 N ANISOU 3206 N CYS A 269 3482 9441 12769 533 636 1827 N ATOM 3207 CA CYS A 269 114.347 172.149 289.145 1.00 65.95 C ANISOU 3207 CA CYS A 269 3426 9101 12530 412 641 1949 C ATOM 3208 C CYS A 269 113.964 173.464 288.479 1.00 64.99 C ANISOU 3208 C CYS A 269 3380 9048 12265 314 754 1948 C ATOM 3209 O CYS A 269 112.787 173.841 288.440 1.00 63.62 O ANISOU 3209 O CYS A 269 3339 8807 12027 267 794 2011 O ATOM 3210 CB CYS A 269 114.892 172.409 290.550 1.00107.37 C ANISOU 3210 CB CYS A 269 8655 14288 17853 378 554 2026 C ATOM 3211 SG CYS A 269 115.463 170.944 291.445 1.00108.40 S ANISOU 3211 SG CYS A 269 8689 14338 18161 523 408 2038 S ATOM 3212 N ILE A 270 114.962 174.182 287.962 1.00 65.92 N ANISOU 3212 N ILE A 270 3402 9309 12337 289 810 1876 N ATOM 3213 CA ILE A 270 114.714 175.406 287.205 1.00 72.49 C ANISOU 3213 CA ILE A 270 4290 10201 13050 209 932 1876 C ATOM 3214 C ILE A 270 113.944 175.098 285.921 1.00 71.30 C ANISOU 3214 C ILE A 270 4181 10084 12827 269 1001 1822 C ATOM 3215 O ILE A 270 113.089 175.882 285.489 1.00 63.94 O ANISOU 3215 O ILE A 270 3355 9141 11800 233 1078 1864 O ATOM 3216 CB ILE A 270 116.052 176.120 286.918 1.00 75.37 C ANISOU 3216 CB ILE A 270 4512 10720 13406 154 985 1807 C ATOM 3217 CG1 ILE A 270 116.221 177.377 287.772 1.00 75.38 C ANISOU 3217 CG1 ILE A 270 4555 10688 13397 13 1007 1899 C ATOM 3218 CG2 ILE A 270 116.198 176.442 285.461 1.00 76.64 C ANISOU 3218 CG2 ILE A 270 4633 11001 13485 167 1108 1722 C ATOM 3219 CD1 ILE A 270 117.452 178.201 287.416 1.00 77.39 C ANISOU 3219 CD1 ILE A 270 4663 11106 13635 -86 1084 1829 C ATOM 3220 N ALA A 271 114.230 173.953 285.295 1.00 73.09 N ANISOU 3220 N ALA A 271 4316 10357 13098 376 973 1733 N ATOM 3221 CA ALA A 271 113.559 173.565 284.057 1.00 74.77 C ANISOU 3221 CA ALA A 271 4548 10609 13254 437 1029 1675 C ATOM 3222 C ALA A 271 112.239 172.847 284.298 1.00 64.60 C ANISOU 3222 C ALA A 271 3354 9210 11982 448 982 1724 C ATOM 3223 O ALA A 271 111.328 172.956 283.470 1.00 64.05 O ANISOU 3223 O ALA A 271 3334 9171 11831 454 1035 1704 O ATOM 3224 CB ALA A 271 114.472 172.675 283.215 1.00 78.13 C ANISOU 3224 CB ALA A 271 4824 11139 13723 554 1030 1560 C ATOM 3225 N LEU A 272 112.123 172.109 285.406 1.00 73.11 N ANISOU 3225 N LEU A 272 4442 10169 13169 449 886 1787 N ATOM 3226 CA LEU A 272 110.840 171.531 285.798 1.00 72.62 C ANISOU 3226 CA LEU A 272 4460 10000 13132 424 852 1849 C ATOM 3227 C LEU A 272 109.774 172.611 285.931 1.00 72.08 C ANISOU 3227 C LEU A 272 4516 9933 12938 340 902 1911 C ATOM 3228 O LEU A 272 108.636 172.437 285.479 1.00 61.85 O ANISOU 3228 O LEU A 272 3260 8659 11583 331 924 1902 O ATOM 3229 CB LEU A 272 110.992 170.775 287.124 1.00 72.66 C ANISOU 3229 CB LEU A 272 4459 9862 13287 425 752 1932 C ATOM 3230 CG LEU A 272 110.061 169.652 287.609 1.00 72.87 C ANISOU 3230 CG LEU A 272 4502 9755 13429 418 701 1992 C ATOM 3231 CD1 LEU A 272 110.104 169.571 289.133 1.00 63.82 C ANISOU 3231 CD1 LEU A 272 3396 8462 12389 381 626 2112 C ATOM 3232 CD2 LEU A 272 108.623 169.768 287.121 1.00 63.15 C ANISOU 3232 CD2 LEU A 272 3338 8553 12104 350 751 1994 C ATOM 3233 N ALA A 273 110.130 173.738 286.550 1.00 61.85 N ANISOU 3233 N ALA A 273 3272 8627 11603 285 921 1974 N ATOM 3234 CA ALA A 273 109.175 174.811 286.794 1.00 60.70 C ANISOU 3234 CA ALA A 273 3244 8471 11350 232 969 2055 C ATOM 3235 C ALA A 273 108.606 175.405 285.514 1.00 60.53 C ANISOU 3235 C ALA A 273 3239 8563 11195 260 1065 2001 C ATOM 3236 O ALA A 273 107.638 176.168 285.588 1.00 69.61 O ANISOU 3236 O ALA A 273 4475 9724 12249 248 1106 2064 O ATOM 3237 CB ALA A 273 109.831 175.914 287.626 1.00 60.56 C ANISOU 3237 CB ALA A 273 3259 8415 11335 174 980 2139 C ATOM 3238 N PHE A 274 109.174 175.081 284.350 1.00 71.76 N ANISOU 3238 N PHE A 274 4576 10078 12610 313 1102 1893 N ATOM 3239 CA PHE A 274 108.636 175.571 283.086 1.00 71.20 C ANISOU 3239 CA PHE A 274 4515 10114 12425 354 1192 1843 C ATOM 3240 C PHE A 274 107.342 174.876 282.685 1.00 61.08 C ANISOU 3240 C PHE A 274 3240 8867 11102 382 1168 1807 C ATOM 3241 O PHE A 274 106.803 175.181 281.616 1.00 65.14 O ANISOU 3241 O PHE A 274 3747 9482 11520 429 1230 1757 O ATOM 3242 CB PHE A 274 109.682 175.421 281.976 1.00 71.61 C ANISOU 3242 CB PHE A 274 4465 10254 12488 405 1245 1741 C ATOM 3243 CG PHE A 274 110.620 176.591 281.869 1.00 62.89 C ANISOU 3243 CG PHE A 274 3352 9183 11359 364 1331 1767 C ATOM 3244 CD1 PHE A 274 111.639 176.765 282.792 1.00 69.67 C ANISOU 3244 CD1 PHE A 274 4170 10005 12296 302 1295 1797 C ATOM 3245 CD2 PHE A 274 110.479 177.522 280.851 1.00 63.07 C ANISOU 3245 CD2 PHE A 274 3397 9280 11288 383 1455 1767 C ATOM 3246 CE1 PHE A 274 112.500 177.846 282.703 1.00 69.89 C ANISOU 3246 CE1 PHE A 274 4169 10078 12307 236 1383 1817 C ATOM 3247 CE2 PHE A 274 111.338 178.603 280.754 1.00 63.71 C ANISOU 3247 CE2 PHE A 274 3463 9386 11357 324 1554 1803 C ATOM 3248 CZ PHE A 274 112.348 178.766 281.682 1.00 69.71 C ANISOU 3248 CZ PHE A 274 4173 10118 12196 238 1519 1824 C ATOM 3249 N LEU A 275 106.832 173.963 283.512 1.00 60.92 N ANISOU 3249 N LEU A 275 3220 8771 11156 349 1085 1835 N ATOM 3250 CA LEU A 275 105.567 173.292 283.249 1.00 76.77 C ANISOU 3250 CA LEU A 275 5211 10824 13134 342 1064 1803 C ATOM 3251 C LEU A 275 104.391 173.927 283.984 1.00 75.87 C ANISOU 3251 C LEU A 275 5178 10714 12935 295 1066 1884 C ATOM 3252 O LEU A 275 103.241 173.710 283.581 1.00 60.24 O ANISOU 3252 O LEU A 275 3171 8833 10884 292 1072 1844 O ATOM 3253 CB LEU A 275 105.669 171.804 283.626 1.00 77.90 C ANISOU 3253 CB LEU A 275 5283 10885 13430 325 988 1791 C ATOM 3254 CG LEU A 275 106.268 170.791 282.635 1.00 62.82 C ANISOU 3254 CG LEU A 275 3262 9004 11601 395 986 1697 C ATOM 3255 CD1 LEU A 275 107.642 171.208 282.143 1.00 63.23 C ANISOU 3255 CD1 LEU A 275 3286 9084 11655 467 1021 1657 C ATOM 3256 CD2 LEU A 275 106.330 169.395 283.251 1.00 63.62 C ANISOU 3256 CD2 LEU A 275 3303 8981 11888 381 915 1729 C ATOM 3257 N SER A 276 104.653 174.712 285.037 1.00 75.58 N ANISOU 3257 N SER A 276 5225 10589 12903 265 1064 1995 N ATOM 3258 CA SER A 276 103.574 175.355 285.784 1.00 75.91 C ANISOU 3258 CA SER A 276 5342 10635 12866 241 1073 2088 C ATOM 3259 C SER A 276 102.822 176.358 284.924 1.00 80.05 C ANISOU 3259 C SER A 276 5887 11298 13232 304 1155 2078 C ATOM 3260 O SER A 276 101.617 176.560 285.112 1.00 82.58 O ANISOU 3260 O SER A 276 6218 11694 13463 311 1162 2102 O ATOM 3261 CB SER A 276 104.129 176.045 287.033 1.00 72.66 C ANISOU 3261 CB SER A 276 5012 10094 12501 209 1060 2220 C ATOM 3262 OG SER A 276 104.704 177.304 286.717 1.00 58.01 O ANISOU 3262 OG SER A 276 3198 8257 10588 237 1134 2263 O ATOM 3263 N SER A 277 103.516 177.005 283.988 1.00 58.88 N ANISOU 3263 N SER A 277 3200 8657 10513 358 1223 2047 N ATOM 3264 CA SER A 277 102.834 177.857 283.025 1.00 59.05 C ANISOU 3264 CA SER A 277 3231 8809 10396 442 1308 2040 C ATOM 3265 C SER A 277 101.901 177.058 282.130 1.00 59.64 C ANISOU 3265 C SER A 277 3217 9022 10422 473 1286 1914 C ATOM 3266 O SER A 277 100.964 177.626 281.557 1.00 59.88 O ANISOU 3266 O SER A 277 3242 9182 10329 548 1333 1909 O ATOM 3267 CB SER A 277 103.858 178.604 282.177 1.00 59.42 C ANISOU 3267 CB SER A 277 3282 8860 10434 484 1399 2039 C ATOM 3268 OG SER A 277 103.223 179.256 281.096 1.00 89.44 O ANISOU 3268 OG SER A 277 7085 12788 14112 584 1486 2027 O ATOM 3269 N SER A 278 102.135 175.752 282.006 1.00 68.06 N ANISOU 3269 N SER A 278 4202 10070 11587 426 1218 1820 N ATOM 3270 CA SER A 278 101.356 174.875 281.145 1.00 69.26 C ANISOU 3270 CA SER A 278 4247 10349 11718 436 1196 1698 C ATOM 3271 C SER A 278 100.491 173.906 281.944 1.00 69.81 C ANISOU 3271 C SER A 278 4270 10416 11837 339 1125 1694 C ATOM 3272 O SER A 278 100.178 172.812 281.470 1.00 70.80 O ANISOU 3272 O SER A 278 4289 10595 12016 302 1091 1605 O ATOM 3273 CB SER A 278 102.277 174.099 280.210 1.00 61.57 C ANISOU 3273 CB SER A 278 3200 9369 10826 466 1194 1605 C ATOM 3274 OG SER A 278 101.525 173.230 279.384 1.00 62.49 O ANISOU 3274 OG SER A 278 3204 9605 10935 473 1173 1496 O ATOM 3275 N VAL A 279 100.101 174.290 283.156 1.00 60.45 N ANISOU 3275 N VAL A 279 3157 9169 10644 291 1110 1799 N ATOM 3276 CA VAL A 279 99.293 173.424 284.001 1.00 82.63 C ANISOU 3276 CA VAL A 279 5924 11969 13503 185 1057 1812 C ATOM 3277 C VAL A 279 97.846 173.895 284.123 1.00 84.39 C ANISOU 3277 C VAL A 279 6119 12354 13591 183 1078 1807 C ATOM 3278 O VAL A 279 96.970 173.068 284.424 1.00 91.85 O ANISOU 3278 O VAL A 279 6978 13365 14556 83 1049 1767 O ATOM 3279 CB VAL A 279 99.925 173.257 285.401 1.00 79.94 C ANISOU 3279 CB VAL A 279 5666 11428 13279 126 1018 1935 C ATOM 3280 CG1 VAL A 279 99.520 174.402 286.336 1.00 79.38 C ANISOU 3280 CG1 VAL A 279 5699 11338 13125 144 1044 2059 C ATOM 3281 CG2 VAL A 279 99.560 171.901 285.993 1.00 78.94 C ANISOU 3281 CG2 VAL A 279 5472 11243 13278 12 964 1935 C ATOM 3282 N ASN A 280 97.557 175.180 283.886 1.00 78.63 N ANISOU 3282 N ASN A 280 5448 11699 12730 289 1135 1852 N ATOM 3283 CA ASN A 280 96.168 175.634 283.971 1.00 73.35 C ANISOU 3283 CA ASN A 280 4735 11203 11931 318 1155 1851 C ATOM 3284 C ASN A 280 95.299 175.066 282.857 1.00 74.85 C ANISOU 3284 C ASN A 280 4769 11599 12073 321 1148 1690 C ATOM 3285 O ASN A 280 94.186 174.598 283.155 1.00 63.42 O ANISOU 3285 O ASN A 280 3219 10277 10599 246 1128 1642 O ATOM 3286 CB ASN A 280 96.115 177.162 283.988 1.00 71.41 C ANISOU 3286 CB ASN A 280 4593 10979 11561 457 1225 1971 C ATOM 3287 CG ASN A 280 96.935 177.754 285.097 1.00 69.70 C ANISOU 3287 CG ASN A 280 4514 10567 11400 442 1236 2134 C ATOM 3288 OD1 ASN A 280 97.691 177.050 285.770 1.00 70.78 O ANISOU 3288 OD1 ASN A 280 4673 10546 11674 343 1184 2147 O ATOM 3289 ND2 ASN A 280 96.803 179.059 285.294 1.00 68.13 N ANISOU 3289 ND2 ASN A 280 4405 10383 11099 549 1305 2271 N ATOM 3290 N PRO A 281 95.705 175.091 281.579 1.00 76.07 N ANISOU 3290 N PRO A 281 4884 11805 12214 401 1167 1602 N ATOM 3291 CA PRO A 281 94.805 174.578 280.531 1.00 79.13 C ANISOU 3291 CA PRO A 281 5109 12394 12561 411 1155 1452 C ATOM 3292 C PRO A 281 94.389 173.129 280.731 1.00 65.28 C ANISOU 3292 C PRO A 281 3219 10672 10911 237 1097 1359 C ATOM 3293 O PRO A 281 93.268 172.764 280.355 1.00 66.67 O ANISOU 3293 O PRO A 281 3246 11035 11052 193 1085 1259 O ATOM 3294 CB PRO A 281 95.626 174.765 279.247 1.00 80.19 C ANISOU 3294 CB PRO A 281 5250 12521 12696 522 1187 1399 C ATOM 3295 CG PRO A 281 96.539 175.897 279.556 1.00 63.08 C ANISOU 3295 CG PRO A 281 3250 10219 10499 606 1244 1536 C ATOM 3296 CD PRO A 281 96.910 175.712 280.994 1.00 62.15 C ANISOU 3296 CD PRO A 281 3214 9940 10461 495 1211 1639 C ATOM 3297 N LEU A 282 95.247 172.287 281.313 1.00 64.84 N ANISOU 3297 N LEU A 282 3203 10441 10991 133 1066 1402 N ATOM 3298 CA LEU A 282 94.837 170.911 281.577 1.00 65.99 C ANISOU 3298 CA LEU A 282 3229 10602 11241 -45 1024 1352 C ATOM 3299 C LEU A 282 93.851 170.846 282.734 1.00 76.03 C ANISOU 3299 C LEU A 282 4487 11911 12490 -168 1021 1397 C ATOM 3300 O LEU A 282 92.903 170.053 282.707 1.00 77.97 O ANISOU 3300 O LEU A 282 4587 12288 12750 -317 1010 1315 O ATOM 3301 CB LEU A 282 96.055 170.033 281.862 1.00 65.66 C ANISOU 3301 CB LEU A 282 3236 10342 11369 -93 996 1413 C ATOM 3302 CG LEU A 282 96.967 169.686 280.684 1.00 65.92 C ANISOU 3302 CG LEU A 282 3234 10353 11459 -3 998 1352 C ATOM 3303 CD1 LEU A 282 97.651 168.350 280.925 1.00 66.57 C ANISOU 3303 CD1 LEU A 282 3278 10272 11744 -93 962 1389 C ATOM 3304 CD2 LEU A 282 96.196 169.664 279.374 1.00 83.31 C ANISOU 3304 CD2 LEU A 282 5295 12784 13575 36 1011 1210 C ATOM 3305 N LEU A 283 94.059 171.672 283.761 1.00 75.25 N ANISOU 3305 N LEU A 283 4531 11702 12357 -119 1036 1529 N ATOM 3306 CA LEU A 283 93.111 171.723 284.866 1.00 77.46 C ANISOU 3306 CA LEU A 283 4803 12025 12603 -211 1043 1584 C ATOM 3307 C LEU A 283 91.763 172.264 284.412 1.00 81.49 C ANISOU 3307 C LEU A 283 5195 12795 12972 -167 1071 1499 C ATOM 3308 O LEU A 283 90.726 171.894 284.973 1.00 85.00 O ANISOU 3308 O LEU A 283 5544 13351 13401 -288 1078 1475 O ATOM 3309 CB LEU A 283 93.675 172.572 286.006 1.00 63.82 C ANISOU 3309 CB LEU A 283 3253 10122 10873 -144 1053 1757 C ATOM 3310 CG LEU A 283 94.584 171.893 287.037 1.00 63.19 C ANISOU 3310 CG LEU A 283 3263 9791 10956 -234 1019 1866 C ATOM 3311 CD1 LEU A 283 95.416 170.779 286.422 1.00 63.64 C ANISOU 3311 CD1 LEU A 283 3272 9752 11158 -287 984 1807 C ATOM 3312 CD2 LEU A 283 95.491 172.925 287.680 1.00 61.61 C ANISOU 3312 CD2 LEU A 283 3230 9423 10757 -120 1025 2008 C ATOM 3313 N TYR A 284 91.753 173.129 283.397 1.00 66.39 N ANISOU 3313 N TYR A 284 3282 10980 10962 9 1091 1461 N ATOM 3314 CA TYR A 284 90.484 173.557 282.826 1.00 67.80 C ANISOU 3314 CA TYR A 284 3328 11407 11025 77 1108 1385 C ATOM 3315 C TYR A 284 89.915 172.491 281.905 1.00 69.65 C ANISOU 3315 C TYR A 284 3357 11787 11319 -36 1080 1211 C ATOM 3316 O TYR A 284 88.692 172.368 281.788 1.00 84.59 O ANISOU 3316 O TYR A 284 5092 13877 13170 -80 1080 1144 O ATOM 3317 CB TYR A 284 90.648 174.873 282.068 1.00 67.26 C ANISOU 3317 CB TYR A 284 3341 11386 10828 317 1145 1436 C ATOM 3318 CG TYR A 284 91.266 175.996 282.873 1.00 65.63 C ANISOU 3318 CG TYR A 284 3335 11035 10565 423 1184 1621 C ATOM 3319 CD1 TYR A 284 91.383 175.921 284.257 1.00 64.86 C ANISOU 3319 CD1 TYR A 284 3319 10811 10513 329 1179 1733 C ATOM 3320 CD2 TYR A 284 91.729 177.139 282.242 1.00 65.04 C ANISOU 3320 CD2 TYR A 284 3366 10951 10395 613 1233 1696 C ATOM 3321 CE1 TYR A 284 91.952 176.946 284.981 1.00 63.53 C ANISOU 3321 CE1 TYR A 284 3322 10509 10307 421 1214 1910 C ATOM 3322 CE2 TYR A 284 92.294 178.168 282.957 1.00 63.80 C ANISOU 3322 CE2 TYR A 284 3381 10665 10195 692 1279 1875 C ATOM 3323 CZ TYR A 284 92.402 178.068 284.322 1.00 63.04 C ANISOU 3323 CZ TYR A 284 3354 10444 10156 596 1265 1979 C ATOM 3324 OH TYR A 284 92.968 179.103 285.024 1.00 61.96 O ANISOU 3324 OH TYR A 284 3377 10177 9987 673 1312 2166 O ATOM 3325 N ALA A 285 90.778 171.716 281.253 1.00 69.51 N ANISOU 3325 N ALA A 285 3328 11680 11402 -83 1056 1150 N ATOM 3326 CA ALA A 285 90.355 170.555 280.483 1.00 88.02 C ANISOU 3326 CA ALA A 285 5480 14137 13827 -225 1026 1006 C ATOM 3327 C ALA A 285 90.219 169.302 281.342 1.00 90.91 C ANISOU 3327 C ALA A 285 5794 14443 14305 -495 1011 1008 C ATOM 3328 O ALA A 285 90.013 168.211 280.798 1.00 91.78 O ANISOU 3328 O ALA A 285 5758 14613 14500 -658 988 912 O ATOM 3329 CB ALA A 285 91.333 170.295 279.332 1.00 86.19 C ANISOU 3329 CB ALA A 285 5255 13852 13643 -137 1014 958 C ATOM 3330 N CYS A 286 90.333 169.440 282.666 1.00 91.97 N ANISOU 3330 N CYS A 286 6048 14452 14445 -554 1025 1131 N ATOM 3331 CA CYS A 286 90.169 168.295 283.555 1.00 96.50 C ANISOU 3331 CA CYS A 286 6593 14949 15122 -815 1020 1159 C ATOM 3332 C CYS A 286 88.748 167.744 283.508 1.00 99.39 C ANISOU 3332 C CYS A 286 6758 15528 15478 -1015 1038 1037 C ATOM 3333 O CYS A 286 88.542 166.550 283.757 1.00103.43 O ANISOU 3333 O CYS A 286 7198 16013 16087 -1285 1037 1007 O ATOM 3334 CB CYS A 286 90.553 168.694 284.984 1.00 94.83 C ANISOU 3334 CB CYS A 286 6559 14553 14919 -803 1033 1329 C ATOM 3335 SG CYS A 286 90.344 167.419 286.256 1.00 96.70 S ANISOU 3335 SG CYS A 286 6802 14653 15285 -1111 1041 1404 S ATOM 3336 N ALA A 287 87.763 168.580 283.180 1.00 99.68 N ANISOU 3336 N ALA A 287 6703 15761 15410 -895 1055 982 N ATOM 3337 CA ALA A 287 86.367 168.146 283.120 1.00 99.79 C ANISOU 3337 CA ALA A 287 6508 15976 15431 -1060 1068 890 C ATOM 3338 C ALA A 287 86.122 167.217 281.932 1.00102.62 C ANISOU 3338 C ALA A 287 6682 16432 15878 -1188 1030 758 C ATOM 3339 O ALA A 287 85.378 166.239 282.038 1.00104.97 O ANISOU 3339 O ALA A 287 6836 16794 16254 -1464 1031 701 O ATOM 3340 CB ALA A 287 85.434 169.352 283.053 1.00 97.71 C ANISOU 3340 CB ALA A 287 6198 15902 15025 -850 1082 922 C TER 3341 ALA A 287 HETATM 3342 C10 7Y9 A2001 117.021 175.089 281.698 1.00 74.49 C ANISOU 3342 C10 7Y9 A2001 5287 12340 10674 2710 2557 -1084 C HETATM 3343 C13 7Y9 A2001 119.673 174.528 281.574 1.00 92.94 C ANISOU 3343 C13 7Y9 A2001 7238 14674 13400 2820 2607 -1221 C HETATM 3344 C15 7Y9 A2001 118.258 179.706 282.323 1.00 81.51 C ANISOU 3344 C15 7Y9 A2001 5455 13040 12474 2222 2677 -1415 C HETATM 3345 C17 7Y9 A2001 117.081 179.806 283.042 1.00 76.95 C ANISOU 3345 C17 7Y9 A2001 4986 12517 11733 2195 2521 -1509 C HETATM 3346 C20 7Y9 A2001 121.963 174.839 280.912 1.00 90.83 C ANISOU 3346 C20 7Y9 A2001 6645 14365 13503 2817 2807 -1305 C HETATM 3347 C21 7Y9 A2001 115.457 181.430 283.666 1.00 85.76 C ANISOU 3347 C21 7Y9 A2001 6062 13536 12987 2002 2364 -1727 C HETATM 3348 C22 7Y9 A2001 114.432 180.789 284.605 1.00 85.93 C ANISOU 3348 C22 7Y9 A2001 6239 13795 12616 2057 2167 -1812 C HETATM 3349 C24 7Y9 A2001 112.123 180.678 285.243 1.00 86.96 C ANISOU 3349 C24 7Y9 A2001 6641 14113 12287 2029 1982 -1872 C HETATM 3350 C26 7Y9 A2001 110.686 181.157 285.049 1.00 69.96 C ANISOU 3350 C26 7Y9 A2001 4641 11888 10051 1958 1980 -1890 C HETATM 3351 C28 7Y9 A2001 113.745 179.317 286.368 1.00 88.47 C ANISOU 3351 C28 7Y9 A2001 6641 14684 12290 2185 1799 -1866 C HETATM 3352 O01 7Y9 A2001 116.773 180.967 283.763 1.00 77.73 O ANISOU 3352 O01 7Y9 A2001 4922 12587 12024 2075 2380 -1712 O HETATM 3353 O02 7Y9 A2001 123.293 174.404 280.907 1.00 91.86 O ANISOU 3353 O02 7Y9 A2001 6595 14522 13785 2898 2806 -1365 O HETATM 3354 O03 7Y9 A2001 109.852 180.041 285.029 1.00 69.03 O ANISOU 3354 O03 7Y9 A2001 4808 11946 9475 2054 1956 -1686 O HETATM 3355 N04 7Y9 A2001 103.811 182.349 285.022 1.00 61.90 N ANISOU 3355 N04 7Y9 A2001 4483 10812 8225 1699 1750 -1968 N HETATM 3356 N05 7Y9 A2001 103.566 180.147 285.844 1.00 60.13 N ANISOU 3356 N05 7Y9 A2001 4550 11163 7135 1882 1586 -1627 N HETATM 3357 C06 7Y9 A2001 117.841 176.141 280.948 1.00 75.92 C ANISOU 3357 C06 7Y9 A2001 5313 12408 11126 2584 2783 -1125 C HETATM 3358 C07 7Y9 A2001 117.632 177.468 281.669 1.00 76.10 C ANISOU 3358 C07 7Y9 A2001 5177 12435 11301 2442 2723 -1222 C HETATM 3359 C08 7Y9 A2001 119.312 175.700 280.928 1.00 92.64 C ANISOU 3359 C08 7Y9 A2001 7230 14548 13421 2662 2797 -1189 C HETATM 3360 C09 7Y9 A2001 117.281 176.250 279.538 1.00 89.66 C ANISOU 3360 C09 7Y9 A2001 7239 14039 12788 2521 3014 -994 C HETATM 3361 C11 7Y9 A2001 118.522 178.535 281.634 1.00 80.88 C ANISOU 3361 C11 7Y9 A2001 5525 12987 12218 2345 2789 -1279 C HETATM 3362 C12 7Y9 A2001 116.467 177.582 282.378 1.00 74.46 C ANISOU 3362 C12 7Y9 A2001 5082 12300 10911 2417 2569 -1259 C HETATM 3363 C14 7Y9 A2001 120.294 176.427 280.262 1.00 94.83 C ANISOU 3363 C14 7Y9 A2001 7328 14778 13925 2587 2986 -1179 C HETATM 3364 C16 7Y9 A2001 116.204 178.743 283.056 1.00 86.11 C ANISOU 3364 C16 7Y9 A2001 6405 13775 12537 2292 2478 -1415 C HETATM 3365 C18 7Y9 A2001 120.992 174.101 281.567 1.00 80.79 C ANISOU 3365 C18 7Y9 A2001 5513 13144 12040 2895 2609 -1285 C HETATM 3366 C19 7Y9 A2001 121.614 176.008 280.259 1.00 82.09 C ANISOU 3366 C19 7Y9 A2001 5546 13204 12442 2665 2992 -1231 C HETATM 3367 C23 7Y9 A2001 113.125 181.194 284.448 1.00 86.39 C ANISOU 3367 C23 7Y9 A2001 6435 13793 12596 1993 2162 -1820 C HETATM 3368 C25 7Y9 A2001 114.748 179.847 285.574 1.00 87.49 C ANISOU 3368 C25 7Y9 A2001 6416 14287 12541 2155 1986 -1851 C HETATM 3369 C27 7Y9 A2001 112.433 179.734 286.208 1.00 87.96 C ANISOU 3369 C27 7Y9 A2001 6731 14575 12116 2123 1798 -1880 C HETATM 3370 C29 7Y9 A2001 108.489 180.313 285.119 1.00 66.19 C ANISOU 3370 C29 7Y9 A2001 4599 11611 8939 2003 1902 -1713 C HETATM 3371 C30 7Y9 A2001 107.597 179.288 284.846 1.00 74.52 C ANISOU 3371 C30 7Y9 A2001 6027 12702 9587 2058 1895 -1421 C HETATM 3372 C31 7Y9 A2001 108.042 181.574 285.483 1.00 67.13 C ANISOU 3372 C31 7Y9 A2001 4544 11643 9319 1874 1817 -2003 C HETATM 3373 C32 7Y9 A2001 105.799 180.779 285.299 1.00 70.52 C ANISOU 3373 C32 7Y9 A2001 5490 12186 9120 1889 1776 -1746 C HETATM 3374 C33 7Y9 A2001 106.239 179.520 284.934 1.00 71.47 C ANISOU 3374 C33 7Y9 A2001 5822 12328 9004 1997 1834 -1422 C HETATM 3375 C34 7Y9 A2001 106.684 181.804 285.578 1.00 72.14 C ANISOU 3375 C34 7Y9 A2001 5324 12308 9778 1829 1755 -2046 C HETATM 3376 C35 7Y9 A2001 104.317 181.049 285.409 1.00 61.52 C ANISOU 3376 C35 7Y9 A2001 4529 11067 7780 1827 1703 -1778 C CONECT 581 1178 CONECT 1178 581 CONECT 3342 3357 CONECT 3343 3359 3365 CONECT 3344 3345 3361 CONECT 3345 3344 3352 3364 CONECT 3346 3353 3365 3366 CONECT 3347 3348 3352 CONECT 3348 3347 3367 3368 CONECT 3349 3350 3367 3369 CONECT 3350 3349 3354 CONECT 3351 3368 3369 CONECT 3352 3345 3347 CONECT 3353 3346 CONECT 3354 3350 3370 CONECT 3355 3376 CONECT 3356 3376 CONECT 3357 3342 3358 3359 3360 CONECT 3358 3357 3361 3362 CONECT 3359 3343 3357 3363 CONECT 3360 3357 CONECT 3361 3344 3358 CONECT 3362 3358 3364 CONECT 3363 3359 3366 CONECT 3364 3345 3362 CONECT 3365 3343 3346 CONECT 3366 3346 3363 CONECT 3367 3348 3349 CONECT 3368 3348 3351 CONECT 3369 3349 3351 CONECT 3370 3354 3371 3372 CONECT 3371 3370 3374 CONECT 3372 3370 3375 CONECT 3373 3374 3375 3376 CONECT 3374 3371 3373 CONECT 3375 3372 3373 CONECT 3376 3355 3356 3373 MASTER 442 0 1 25 5 0 4 6 3375 1 37 41 END