Browse entries in the PDBbind-CN Database
HEADER PLANT PROTEIN/RNA 05-FEB-18 5Z9X TITLE ARABIDOPSIS SMALL RNA DEGRADING NUCLEASE 1 IN COMPLEX WITH AN RNA TITLE 2 SUBSTRATE COMPND MOL_ID: 1; COMPND 2 MOLECULE: SMALL RNA DEGRADING NUCLEASE 1; COMPND 3 CHAIN: A; COMPND 4 EC: 3.1.-.-; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: RNA (5'-R(P*GP*CP*CP*CP*AP*UP*UP*AP*G)-3'); COMPND 8 CHAIN: R; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA; SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS; SOURCE 4 ORGANISM_TAXID: 3702; SOURCE 5 GENE: SDN1, AT3G50100, F3A4.180; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 MOL_ID: 2; SOURCE 10 SYNTHETIC: YES; SOURCE 11 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA; SOURCE 12 ORGANISM_TAXID: 3702 KEYWDS EXONUCLEASE, MICRORNA TURNOVER, PROTEIN-RNA COMPLEX, PLANT PROTEIN, KEYWDS 2 PLANT PROTEIN-RNA COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR J.CHEN,L.LIU,C.YOU,J.GU,W.RUAN,L.ZHANG,J.GAN,C.CAO,Y.HUANG,X.CHEN, AUTHOR 2 J.MA REVDAT 2 03-OCT-18 5Z9X 1 JRNL REVDAT 1 27-JUN-18 5Z9X 0 JRNL AUTH J.CHEN,L.LIU,C.YOU,J.GU,W.RUAN,L.ZHANG,J.GAN,C.CAO,Y.HUANG, JRNL AUTH 2 X.CHEN,J.MA JRNL TITL STRUCTURAL AND BIOCHEMICAL INSIGHTS INTO SMALL RNA 3' END JRNL TITL 2 TRIMMING BY ARABIDOPSIS SDN1. JRNL REF NAT COMMUN V. 9 3585 2018 JRNL REFN ESSN 2041-1723 JRNL PMID 30181559 JRNL DOI 10.1038/S41467-018-05942-7 REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.8.4_1496 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.99 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.430 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2 REMARK 3 NUMBER OF REFLECTIONS : 20211 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.253 REMARK 3 R VALUE (WORKING SET) : 0.252 REMARK 3 FREE R VALUE : 0.261 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.850 REMARK 3 FREE R VALUE TEST SET COUNT : 1991 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 28.9877 - 6.7223 0.98 1382 158 0.2066 0.2103 REMARK 3 2 6.7223 - 5.3466 1.00 1366 141 0.2768 0.2462 REMARK 3 3 5.3466 - 4.6740 0.99 1317 146 0.2178 0.2316 REMARK 3 4 4.6740 - 4.2481 0.99 1294 140 0.2018 0.2284 REMARK 3 5 4.2481 - 3.9444 0.99 1321 150 0.2130 0.2324 REMARK 3 6 3.9444 - 3.7123 0.99 1286 137 0.2305 0.2563 REMARK 3 7 3.7123 - 3.5267 0.99 1271 138 0.2428 0.2736 REMARK 3 8 3.5267 - 3.3735 0.99 1289 139 0.2657 0.2846 REMARK 3 9 3.3735 - 3.2438 1.00 1293 142 0.3142 0.3235 REMARK 3 10 3.2438 - 3.1320 0.99 1280 139 0.3176 0.3365 REMARK 3 11 3.1320 - 3.0341 1.00 1291 137 0.3621 0.4193 REMARK 3 12 3.0341 - 2.9475 0.99 1275 143 0.3716 0.3510 REMARK 3 13 2.9475 - 2.8700 0.99 1294 142 0.3893 0.4278 REMARK 3 14 2.8700 - 2.8000 0.99 1261 139 0.4021 0.4695 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) : 0.540 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.370 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 : 0.015 2524 REMARK 3 ANGLE : 1.843 3453 REMARK 3 CHIRALITY : 0.082 413 REMARK 3 PLANARITY : 0.008 410 REMARK 3 DIHEDRAL : 17.381 970 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): 27.4711 39.4699 74.1192 REMARK 3 T TENSOR REMARK 3 T11: -0.3478 T22: 1.4473 REMARK 3 T33: 0.3587 T12: 0.4217 REMARK 3 T13: 0.0417 T23: -0.0929 REMARK 3 L TENSOR REMARK 3 L11: 2.0859 L22: 1.0794 REMARK 3 L33: 2.2153 L12: 0.1644 REMARK 3 L13: -0.1775 L23: 0.1069 REMARK 3 S TENSOR REMARK 3 S11: -0.2119 S12: 1.0518 S13: -0.0148 REMARK 3 S21: -0.6498 S22: 0.3314 S23: -0.0360 REMARK 3 S31: 0.2255 S32: -0.2707 S33: -0.0826 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 5Z9X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-FEB-18. REMARK 100 THE DEPOSITION ID IS D_1300006733. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-APR-13 REMARK 200 TEMPERATURE (KELVIN) : 80 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL17B1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.987 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 0.98.699A REMARK 200 DATA SCALING SOFTWARE : HKL-2000 0.98.699A REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20440 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 200 DATA REDUNDANCY : 6.800 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200
FOR THE DATA SET : 26.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200
FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX 1.7.1_743 REMARK 200 STARTING MODEL: SDN1 DELTAC-SSRNA REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 69.45 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.03 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: LITHUM SULFATE, MAGNESIUM CHLORIDE, 2 REMARK 280 -(N-MORPHOLINO) ETHANESULFONIC ACID, VAPOR DIFFUSION, HANGING REMARK 280 DROP, TEMPERATURE 290K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+2/3 REMARK 290 6555 -X,-X+Y,-Z+1/3 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.54633 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 119.09267 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 119.09267 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 59.54633 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1730 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 16310 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, R 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH A 609 LIES ON A SPECIAL POSITION. REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 1 REMARK 465 LYS A 247 REMARK 465 TYR A 248 REMARK 465 PRO A 249 REMARK 465 ASN A 250 REMARK 465 THR A 251 REMARK 465 ARG A 252 REMARK 465 GLU A 270 REMARK 465 VAL A 271 REMARK 465 ARG A 272 REMARK 465 LYS A 273 REMARK 465 THR A 274 REMARK 465 THR A 301 REMARK 465 THR A 302 REMARK 465 ILE A 303 REMARK 465 LYS A 304 REMARK 465 PRO A 305 REMARK 465 SER A 306 REMARK 465 LYS A 307 REMARK 465 GLU A 308 REMARK 465 MET A 309 REMARK 465 LEU A 310 REMARK 465 GLU A 311 REMARK 465 VAL A 312 REMARK 465 GLU A 313 REMARK 465 LYS A 314 REMARK 465 ALA A 315 REMARK 465 LYS A 316 REMARK 465 LEU A 317 REMARK 465 PHE A 318 REMARK 465 LEU A 319 REMARK 465 HIS A 320 REMARK 465 LYS A 321 REMARK 465 ILE A 322 REMARK 465 PRO A 323 REMARK 465 ASN A 324 REMARK 465 ASN A 325 REMARK 465 VAL A 326 REMARK 465 PRO A 327 REMARK 465 SER A 328 REMARK 465 GLU A 329 REMARK 465 GLU A 330 REMARK 465 LEU A 331 REMARK 465 GLU A 332 REMARK 465 GLN A 333 REMARK 465 VAL A 334 REMARK 465 LEU A 335 REMARK 465 SER A 336 REMARK 465 GLY A 337 REMARK 465 LYS A 338 REMARK 465 PHE A 339 REMARK 465 THR A 340 REMARK 465 LEU A 341 REMARK 465 ASP A 342 REMARK 465 VAL A 343 REMARK 465 LYS A 344 REMARK 465 GLN A 345 REMARK 465 ALA A 346 REMARK 465 LYS A 347 REMARK 465 THR A 348 REMARK 465 GLN A 349 REMARK 465 GLY A 350 REMARK 465 ARG A 351 REMARK 465 TYR A 352 REMARK 465 TYR A 353 REMARK 465 CYS A 354 REMARK 465 ALA A 355 REMARK 465 PHE A 356 REMARK 465 ALA A 357 REMARK 465 LEU A 358 REMARK 465 PHE A 359 REMARK 465 HIS A 360 REMARK 465 SER A 361 REMARK 465 SER A 362 REMARK 465 GLU A 363 REMARK 465 ASP A 364 REMARK 465 ALA A 365 REMARK 465 ASP A 366 REMARK 465 GLN A 367 REMARK 465 ALA A 368 REMARK 465 PHE A 369 REMARK 465 GLU A 370 REMARK 465 HIS A 371 REMARK 465 ILE A 372 REMARK 465 ASP A 373 REMARK 465 GLY A 374 REMARK 465 ILE A 375 REMARK 465 GLU A 376 REMARK 465 MET A 377 REMARK 465 THR A 378 REMARK 465 ASP A 379 REMARK 465 SER A 380 REMARK 465 LEU A 381 REMARK 465 GLY A 382 REMARK 465 LEU A 383 REMARK 465 PRO A 384 REMARK 465 GLN A 385 REMARK 465 LYS A 386 REMARK 465 VAL A 387 REMARK 465 VAL A 388 REMARK 465 ILE A 389 REMARK 465 ILE A 390 REMARK 465 LYS A 391 REMARK 465 LEU A 392 REMARK 465 SER A 393 REMARK 465 SER A 394 REMARK 465 GLY A 395 REMARK 465 SER A 396 REMARK 465 ARG A 397 REMARK 465 ALA A 398 REMARK 465 SER A 399 REMARK 465 ILE A 400 REMARK 465 TYR A 401 REMARK 465 VAL A 402 REMARK 465 ARG A 403 REMARK 465 LYS A 404 REMARK 465 MET A 405 REMARK 465 VAL A 406 REMARK 465 GLN A 407 REMARK 465 ASP A 408 REMARK 465 GLU A 409 REMARK 465 A R 1 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 41 CG CD CE NZ REMARK 470 ASN A 42 CG OD1 ND2 REMARK 470 ASP A 44 CG OD1 OD2 REMARK 470 ASP A 91 CG OD1 OD2 REMARK 470 LYS A 253 CG CD CE NZ REMARK 470 LEU A 254 CG CD1 CD2 REMARK 470 ILE A 266 CG1 CG2 CD1 REMARK 470 LEU A 267 CG CD1 CD2 REMARK 470 ASP A 300 CG OD1 OD2 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 HOH A 613 O HOH A 622 2.06 REMARK 500 O PHE A 60 OG1 THR A 63 2.14 REMARK 500 OG SER A 119 O HOH A 601 2.14 REMARK 500 O CYS A 263 N LEU A 267 2.15 REMARK 500 NH1 ARG A 23 O3 SO4 A 501 2.15 REMARK 500 O ASP A 48 N SER A 50 2.16 REMARK 500 NH2 ARG A 23 O HOH A 602 2.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 ARG A 255 CB ARG A 255 CG 0.248 REMARK 500 ARG A 255 CG ARG A 255 CD 0.221 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 LEU A 171 N - CA - C ANGL. DEV. = -22.5 DEGREES REMARK 500 ARG A 255 NE - CZ - NH1 ANGL. DEV. = -4.7 DEGREES 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 GLN A 87 7.61 -65.20 REMARK 500 HIS A 106 129.96 -38.80 REMARK 500 PRO A 180 -173.29 -64.63 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 ARG A 51 ARG A 52 -134.38 REMARK 500 GLN A 90 ASP A 91 -148.14 REMARK 500 GLU A 120 ASP A 121 143.67 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG A 503 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 144 OD1 REMARK 620 2 GLU A 146 OE2 137.6 REMARK 620 3 ASP A 283 OD2 97.9 114.6 REMARK 620 4 G R 10 OP1 84.0 118.0 94.1 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG A 502 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 144 OD2 REMARK 620 2 HIS A 223 O 136.8 REMARK 620 N 1 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 501 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 502 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 503 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 R 101 DBREF 5Z9X A 1 409 UNP A3KPE8 SDN1_ARATH 1 409 DBREF 5Z9X R 1 10 PDB 5Z9X 5Z9X 1 10 SEQRES 1 A 409 MET GLU LEU LYS LEU ALA THR ALA GLU LYS GLN VAL LEU SEQRES 2 A 409 ASP GLU LEU VAL LYS LEU LEU GLN SER ARG ASP LEU ARG SEQRES 3 A 409 GLY GLU ASN GLY ASN TRP LYS GLU PHE LEU HIS VAL TYR SEQRES 4 A 409 ASP LYS ASN ALA ASP SER PRO SER ASP PRO SER ARG ARG SEQRES 5 A 409 SER HIS GLU ASP LEU VAL GLN PHE LEU THR THR PHE LYS SEQRES 6 A 409 LYS LYS GLU ASP LEU GLN LEU LEU LYS CYS HIS ALA ASN SEQRES 7 A 409 HIS LEU LEU ILE GLU ASN LEU LYS GLN GLU SER GLN ASP SEQRES 8 A 409 GLU ASP THR PRO GLU GLN MET LEU VAL ARG LEU THR VAL SEQRES 9 A 409 GLU HIS PRO SER TYR SER LEU ASP TYR SER PHE LYS PRO SEQRES 10 A 409 TYR SER GLU ASP TRP PHE VAL SER ASP VAL GLY MET LYS SEQRES 11 A 409 MET LYS LYS VAL MET GLU SER THR ASN MET VAL ALA VAL SEQRES 12 A 409 ASP CYS GLU MET VAL LEU CYS GLU ASP GLY THR GLU GLY SEQRES 13 A 409 LEU VAL ARG VAL GLY VAL VAL ASP ARG ASP LEU LYS VAL SEQRES 14 A 409 ILE LEU ASP GLU PHE VAL LYS PRO ASN LYS PRO VAL VAL SEQRES 15 A 409 ASP TYR ARG THR ASP ILE THR GLY ILE THR ALA GLU ASP SEQRES 16 A 409 ILE GLU ASN ALA SER LEU SER VAL VAL ASP ILE GLN GLU SEQRES 17 A 409 THR LEU GLN PRO PHE LEU SER THR GLY THR ILE LEU VAL SEQRES 18 A 409 GLY HIS SER LEU ASN ARG ASP LEU GLU VAL LEU LYS ILE SEQRES 19 A 409 ASP HIS PRO LYS VAL ILE ASP THR ALA LEU VAL PHE LYS SEQRES 20 A 409 TYR PRO ASN THR ARG LYS LEU ARG ARG PRO SER LEU ASN SEQRES 21 A 409 ASN LEU CYS LYS SER ILE LEU GLY TYR GLU VAL ARG LYS SEQRES 22 A 409 THR GLY VAL PRO HIS ASP CYS VAL HIS ASP ALA SER ALA SEQRES 23 A 409 ALA MET LYS LEU ALA LEU ALA VAL VAL GLU LYS ARG VAL SEQRES 24 A 409 ASP THR THR ILE LYS PRO SER LYS GLU MET LEU GLU VAL SEQRES 25 A 409 GLU LYS ALA LYS LEU PHE LEU HIS LYS ILE PRO ASN ASN SEQRES 26 A 409 VAL PRO SER GLU GLU LEU GLU GLN VAL LEU SER GLY LYS SEQRES 27 A 409 PHE THR LEU ASP VAL LYS GLN ALA LYS THR GLN GLY ARG SEQRES 28 A 409 TYR TYR CYS ALA PHE ALA LEU PHE HIS SER SER GLU ASP SEQRES 29 A 409 ALA ASP GLN ALA PHE GLU HIS ILE ASP GLY ILE GLU MET SEQRES 30 A 409 THR ASP SER LEU GLY LEU PRO GLN LYS VAL VAL ILE ILE SEQRES 31 A 409 LYS LEU SER SER GLY SER ARG ALA SER ILE TYR VAL ARG SEQRES 32 A 409 LYS MET VAL GLN ASP GLU SEQRES 1 R 10 A G C C C A U U A G HET SO4 A 501 5 HET MG A 502 1 HET MG A 503 1 HET SO4 R 101 5 HETNAM SO4 SULFATE ION HETNAM MG MAGNESIUM ION FORMUL 3 SO4 2(O4 S 2-) FORMUL 4 MG 2(MG 2+) FORMUL 7 HOH *27(H2 O) HELIX 1 AA1 GLU A 9 ASP A 24 1 16 HELIX 2 AA2 ASN A 31 TYR A 39 1 9 HELIX 3 AA3 SER A 53 THR A 62 1 10 HELIX 4 AA4 LYS A 66 GLN A 87 1 22 HELIX 5 AA5 SER A 89 ASP A 93 5 5 HELIX 6 AA6 THR A 94 HIS A 106 1 13 HELIX 7 AA7 SER A 108 TYR A 113 1 6 HELIX 8 AA8 ASP A 126 LYS A 130 5 5 HELIX 9 AA9 MET A 131 GLU A 136 1 6 HELIX 10 AB1 ILE A 191 ASN A 198 1 8 HELIX 11 AB2 SER A 202 THR A 216 1 15 HELIX 12 AB3 SER A 224 LYS A 233 1 10 HELIX 13 AB4 THR A 242 PHE A 246 1 5 HELIX 14 AB5 SER A 258 LEU A 267 1 10 HELIX 15 AB6 ASP A 279 LYS A 297 1 19 SHEET 1 AA1 2 PHE A 123 VAL A 124 0 SHEET 2 AA1 2 ILE A 234 ASP A 235 1 O ASP A 235 N PHE A 123 SHEET 1 AA2 5 VAL A 169 PHE A 174 0 SHEET 2 AA2 5 GLU A 155 ASP A 164 -1 N VAL A 162 O LEU A 171 SHEET 3 AA2 5 MET A 140 LEU A 149 -1 N ASP A 144 O GLY A 161 SHEET 4 AA2 5 ILE A 219 GLY A 222 1 O ILE A 219 N VAL A 141 SHEET 5 AA2 5 VAL A 239 ASP A 241 1 O ILE A 240 N GLY A 222 LINK OD1 ASP A 144 MG MG A 503 1555 1555 2.15 LINK OD2 ASP A 144 MG MG A 502 1555 1555 2.17 LINK OE2BGLU A 146 MG MG A 503 1555 1555 2.17 LINK O HIS A 223 MG MG A 502 1555 1555 2.88 LINK OD2 ASP A 283 MG MG A 503 1555 1555 2.16 LINK OP1 G R 10 MG MG A 503 1555 1555 2.18 CISPEP 1 LYS A 116 PRO A 117 0 5.02 CISPEP 2 THR A 186 ASP A 187 0 28.24 SITE 1 AC1 4 ARG A 23 LEU A 72 LYS A 116 HOH A 618 SITE 1 AC2 4 ASP A 144 HIS A 223 ASP A 228 G R 10 SITE 1 AC3 6 ASP A 144 CYS A 145 GLU A 146 CYS A 280 SITE 2 AC3 6 ASP A 283 G R 10 SITE 1 AC4 2 A R 9 G R 10 CRYST1 87.993 87.993 178.639 90.00 90.00 120.00 P 31 2 1 6 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 0.011365 0.006561 0.000000 0.00000 SCALE2 0.000000 0.013123 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005598 0.00000 ATOM 1 N GLU A 2 14.307 30.407 85.342 1.00 96.45 N ANISOU 1 N GLU A 2 9181 17013 10453 1548 -196 -795 N ATOM 2 CA GLU A 2 13.127 31.260 85.353 1.00107.72 C ANISOU 2 CA GLU A 2 10553 18580 11794 1545 -193 -687 C ATOM 3 C GLU A 2 13.447 32.654 84.835 1.00109.47 C ANISOU 3 C GLU A 2 10827 18869 11898 1608 -182 -606 C ATOM 4 O GLU A 2 14.603 33.005 84.628 1.00121.76 O ANISOU 4 O GLU A 2 12469 20350 13444 1650 -176 -626 O ATOM 5 CB GLU A 2 12.549 31.356 86.764 1.00104.55 C ANISOU 5 CB GLU A 2 10161 18095 11468 1553 -183 -606 C ATOM 6 CG GLU A 2 11.054 31.618 86.812 1.00116.69 C ANISOU 6 CG GLU A 2 11589 19789 12959 1520 -188 -532 C ATOM 7 CD GLU A 2 10.235 30.352 86.633 1.00134.42 C ANISOU 7 CD GLU A 2 13710 22098 15266 1425 -206 -599 C ATOM 8 OE1 GLU A 2 10.799 29.329 86.188 1.00144.88 O ANISOU 8 OE1 GLU A 2 15025 23370 16655 1384 -215 -713 O ATOM 9 OE2 GLU A 2 9.027 30.377 86.950 1.00134.62 O ANISOU 9 OE2 GLU A 2 13639 22227 15282 1387 -212 -541 O ATOM 10 N LEU A 3 12.415 33.459 84.646 1.00 82.69 N ANISOU 10 N LEU A 3 7372 15619 8426 1614 -179 -509 N ATOM 11 CA LEU A 3 12.554 34.714 83.920 1.00 86.39 C ANISOU 11 CA LEU A 3 7855 16181 8786 1666 -167 -427 C ATOM 12 C LEU A 3 12.114 35.876 84.787 1.00 91.23 C ANISOU 12 C LEU A 3 8495 16762 9407 1722 -149 -297 C ATOM 13 O LEU A 3 11.031 35.829 85.373 1.00102.42 O ANISOU 13 O LEU A 3 9847 18226 10842 1708 -152 -252 O ATOM 14 CB LEU A 3 11.725 34.662 82.635 1.00 94.72 C ANISOU 14 CB LEU A 3 8789 17470 9731 1627 -180 -428 C ATOM 15 CG LEU A 3 12.284 35.047 81.264 1.00 80.04 C ANISOU 15 CG LEU A 3 6922 15732 7758 1640 -177 -441 C ATOM 16 CD1 LEU A 3 13.615 34.341 80.915 1.00 82.39 C ANISOU 16 CD1 LEU A 3 7290 15932 8082 1633 -181 -570 C ATOM 17 CD2 LEU A 3 11.217 34.742 80.219 1.00 64.07 C ANISOU 17 CD2 LEU A 3 4754 13953 5638 1582 -194 -451 C ATOM 18 N LYS A 4 12.916 36.933 84.860 1.00 77.01 N ANISOU 18 N LYS A 4 6778 14888 7594 1784 -131 -240 N ATOM 19 CA LYS A 4 12.638 37.992 85.837 1.00 78.60 C ANISOU 19 CA LYS A 4 7011 15024 7827 1838 -113 -137 C ATOM 20 C LYS A 4 12.136 39.285 85.194 1.00 71.36 C ANISOU 20 C LYS A 4 6045 14227 6840 1888 -101 -21 C ATOM 21 O LYS A 4 12.937 40.124 84.784 1.00 74.36 O ANISOU 21 O LYS A 4 6476 14574 7204 1928 -87 17 O ATOM 22 CB LYS A 4 13.907 38.247 86.674 1.00 88.05 C ANISOU 22 CB LYS A 4 8334 16024 9095 1868 -102 -159 C ATOM 23 CG LYS A 4 14.521 36.957 87.284 1.00 66.82 C ANISOU 23 CG LYS A 4 5691 13211 6485 1828 -115 -267 C ATOM 24 CD LYS A 4 15.896 37.187 87.920 1.00 73.47 C ANISOU 24 CD LYS A 4 6646 13884 7384 1857 -108 -292 C ATOM 25 CE LYS A 4 16.453 35.885 88.498 1.00 89.32 C ANISOU 25 CE LYS A 4 8684 15778 9476 1826 -120 -388 C ATOM 26 NZ LYS A 4 17.869 35.967 88.977 1.00 96.68 N ANISOU 26 NZ LYS A 4 9712 16565 10459 1851 -118 -422 N ATOM 27 N LEU A 5 10.814 39.458 85.142 1.00 84.18 N ANISOU 27 N LEU A 5 7562 15989 8433 1886 -107 42 N ATOM 28 CA LEU A 5 10.207 40.512 84.310 1.00 89.19 C ANISOU 28 CA LEU A 5 8118 16773 8996 1931 -101 152 C ATOM 29 C LEU A 5 9.772 41.760 85.069 1.00 80.91 C ANISOU 29 C LEU A 5 7068 15681 7993 2005 -85 263 C ATOM 30 O LEU A 5 9.194 42.684 84.491 1.00 85.97 O ANISOU 30 O LEU A 5 7634 16435 8596 2054 -82 366 O ATOM 31 CB LEU A 5 9.007 39.916 83.562 1.00 83.90 C ANISOU 31 CB LEU A 5 7306 16317 8253 1883 -125 150 C ATOM 32 CG LEU A 5 9.522 38.737 82.721 1.00 80.98 C ANISOU 32 CG LEU A 5 6935 15991 7844 1810 -140 27 C ATOM 33 CD1 LEU A 5 8.412 37.806 82.316 1.00 91.29 C ANISOU 33 CD1 LEU A 5 8108 17466 9112 1735 -168 -16 C ATOM 34 CD2 LEU A 5 10.277 39.238 81.503 1.00 75.90 C ANISOU 34 CD2 LEU A 5 6306 15416 7118 1833 -131 43 C ATOM 35 N ALA A 6 10.128 41.789 86.349 1.00 89.86 N ANISOU 35 N ALA A 6 8283 16649 9212 2017 -76 239 N ATOM 36 CA ALA A 6 9.708 42.812 87.305 1.00 95.30 C ANISOU 36 CA ALA A 6 8971 17282 9957 2081 -63 316 C ATOM 37 C ALA A 6 9.736 44.255 86.771 1.00 82.63 C ANISOU 37 C ALA A 6 7342 15701 8351 2157 -49 425 C ATOM 38 O ALA A 6 8.698 44.919 86.721 1.00 82.94 O ANISOU 38 O ALA A 6 7285 15842 8385 2204 -51 511 O ATOM 39 CB ALA A 6 10.571 42.707 88.564 1.00108.30 C ANISOU 39 CB ALA A 6 10733 18731 11684 2080 -53 260 C ATOM 40 N THR A 7 10.916 44.733 86.377 1.00 75.04 N ANISOU 40 N THR A 7 6460 14647 7404 2171 -35 425 N ATOM 41 CA THR A 7 11.076 46.128 85.955 1.00 82.01 C ANISOU 41 CA THR A 7 7324 15524 8313 2242 -19 532 C ATOM 42 C THR A 7 11.249 46.298 84.455 1.00 83.58 C ANISOU 42 C THR A 7 7475 15852 8430 2242 -18 582 C ATOM 43 O THR A 7 11.590 47.395 83.975 1.00 69.45 O ANISOU 43 O THR A 7 5676 14049 6664 2296 -2 674 O ATOM 44 CB THR A 7 12.248 46.829 86.669 1.00 85.18 C ANISOU 44 CB THR A 7 7831 15726 8808 2266 -2 519 C ATOM 45 OG1 THR A 7 13.460 46.061 86.544 1.00 90.27 O ANISOU 45 OG1 THR A 7 8568 16291 9440 2211 -3 424 O ATOM 46 CG2 THR A 7 11.900 47.062 88.115 1.00 74.00 C ANISOU 46 CG2 THR A 7 6435 14209 7471 2288 0 502 C ATOM 47 N ALA A 8 11.018 45.206 83.732 1.00 95.69 N ANISOU 47 N ALA A 8 8973 17514 9872 2181 -34 521 N ATOM 48 CA ALA A 8 11.034 45.211 82.271 1.00 89.21 C ANISOU 48 CA ALA A 8 8088 16858 8950 2173 -36 559 C ATOM 49 C ALA A 8 10.152 46.338 81.744 1.00 77.72 C ANISOU 49 C ALA A 8 6521 15526 7481 2244 -34 709 C ATOM 50 O ALA A 8 9.174 46.721 82.409 1.00 79.69 O ANISOU 50 O ALA A 8 6714 15789 7777 2282 -41 758 O ATOM 51 CB ALA A 8 10.566 43.866 81.738 1.00 83.46 C ANISOU 51 CB ALA A 8 7306 16269 8136 2097 -61 466 C ATOM 52 N GLU A 9 10.485 46.862 80.578 1.00 71.62 N ANISOU 52 N GLU A 9 5713 14849 6650 2264 -25 783 N ATOM 53 CA GLU A 9 9.646 47.829 79.924 1.00 69.97 C ANISOU 53 CA GLU A 9 5385 14780 6421 2331 -28 932 C ATOM 54 C GLU A 9 8.490 47.177 79.199 1.00 79.01 C ANISOU 54 C GLU A 9 6397 16167 7455 2298 -57 937 C ATOM 55 O GLU A 9 8.579 46.056 78.691 1.00 86.16 O ANISOU 55 O GLU A 9 7297 17168 8273 2218 -70 836 O ATOM 56 CB GLU A 9 10.469 48.660 78.943 1.00 69.78 C ANISOU 56 CB GLU A 9 5366 14771 6378 2365 -6 1024 C ATOM 57 CG GLU A 9 11.608 49.439 79.554 1.00 76.65 C ANISOU 57 CG GLU A 9 6345 15415 7365 2397 21 1033 C ATOM 58 CD GLU A 9 11.129 50.587 80.421 1.00 94.38 C ANISOU 58 CD GLU A 9 8570 17546 9744 2480 25 1120 C ATOM 59 OE1 GLU A 9 10.058 51.165 80.118 1.00 96.68 O ANISOU 59 OE1 GLU A 9 8745 17956 10032 2540 12 1229 O ATOM 60 OE2 GLU A 9 11.826 50.906 81.414 1.00107.53 O ANISOU 60 OE2 GLU A 9 10329 19006 11521 2487 39 1075 O ATOM 61 N LYS A 10 7.387 47.893 79.142 1.00 84.30 N ANISOU 61 N LYS A 10 6950 16944 8137 2361 -72 1053 N ATOM 62 CA LYS A 10 6.222 47.364 78.486 1.00 85.56 C ANISOU 62 CA LYS A 10 6965 17348 8197 2332 -107 1068 C ATOM 63 C LYS A 10 6.437 47.134 77.023 1.00 97.07 C ANISOU 63 C LYS A 10 8360 18997 9524 2297 -113 1090 C ATOM 64 O LYS A 10 5.869 46.227 76.482 1.00 92.61 O ANISOU 64 O LYS A 10 7714 18611 8863 2227 -140 1031 O ATOM 65 CB LYS A 10 5.015 48.255 78.721 1.00 79.81 C ANISOU 65 CB LYS A 10 6114 16699 7512 2420 -127 1195 C ATOM 66 CG LYS A 10 3.768 47.441 78.965 1.00 88.60 C ANISOU 66 CG LYS A 10 7117 17966 8581 2374 -164 1150 C ATOM 67 CD LYS A 10 2.538 48.296 78.734 1.00102.00 C ANISOU 67 CD LYS A 10 8653 19822 10281 2462 -195 1291 C ATOM 68 CE LYS A 10 1.454 47.517 78.007 1.00108.71 C ANISOU 68 CE LYS A 10 9343 20950 11013 2399 -242 1282 C ATOM 69 NZ LYS A 10 1.446 46.093 78.430 1.00105.89 N ANISOU 69 NZ LYS A 10 9023 20585 10626 2276 -247 1120 N ATOM 70 N GLN A 11 7.197 47.993 76.367 1.00 91.26 N ANISOU 70 N GLN A 11 7648 18239 8786 2345 -90 1182 N ATOM 71 CA GLN A 11 7.350 47.876 74.942 1.00 91.88 C ANISOU 71 CA GLN A 11 7653 18524 8732 2319 -94 1221 C ATOM 72 C GLN A 11 7.970 46.531 74.653 1.00 94.16 C ANISOU 72 C GLN A 11 8000 18838 8937 2211 -93 1048 C ATOM 73 O GLN A 11 7.514 45.770 73.809 1.00113.72 O ANISOU 73 O GLN A 11 10384 21529 11295 2146 -117 1001 O ATOM 74 CB GLN A 11 8.238 48.997 74.415 1.00 98.26 C ANISOU 74 CB GLN A 11 8495 19271 9566 2384 -63 1344 C ATOM 75 CG GLN A 11 8.911 48.678 73.074 1.00109.18 C ANISOU 75 CG GLN A 11 9856 20817 10811 2337 -52 1340 C ATOM 76 CD GLN A 11 10.084 49.591 72.770 1.00119.62 C ANISOU 76 CD GLN A 11 11247 22027 12174 2382 -12 1426 C ATOM 77 OE1 GLN A 11 10.437 50.466 73.574 1.00125.39 O ANISOU 77 OE1 GLN A 11 12047 22548 13049 2445 6 1482 O ATOM 78 NE2 GLN A 11 10.700 49.390 71.604 1.00111.87 N ANISOU 78 NE2 GLN A 11 10241 21195 11068 2346 1 1433 N ATOM 79 N VAL A 12 8.987 46.217 75.419 1.00 86.24 N ANISOU 79 N VAL A 12 7147 17612 8007 2192 -70 945 N ATOM 80 CA VAL A 12 9.710 44.993 75.254 1.00 89.55 C ANISOU 80 CA VAL A 12 7634 18016 8375 2106 -71 776 C ATOM 81 C VAL A 12 8.809 43.835 75.529 1.00 79.56 C ANISOU 81 C VAL A 12 6310 16832 7086 2033 -104 666 C ATOM 82 O VAL A 12 8.789 42.840 74.822 1.00 82.83 O ANISOU 82 O VAL A 12 6681 17382 7409 1956 -121 561 O ATOM 83 CB VAL A 12 10.883 44.960 76.279 1.00 68.32 C ANISOU 83 CB VAL A 12 5113 15046 5798 2112 -49 698 C ATOM 84 CG1 VAL A 12 11.659 43.648 76.196 1.00 71.16 C ANISOU 84 CG1 VAL A 12 5543 15371 6124 2033 -56 516 C ATOM 85 CG2 VAL A 12 11.782 46.205 76.112 1.00 61.52 C ANISOU 85 CG2 VAL A 12 4304 14086 4983 2181 -16 813 C ATOM 86 N LEU A 13 8.036 43.994 76.571 1.00 80.98 N ANISOU 86 N LEU A 13 6480 16933 7355 2058 -115 691 N ATOM 87 CA LEU A 13 7.157 42.939 76.969 1.00 85.01 C ANISOU 87 CA LEU A 13 6932 17507 7862 1988 -146 597 C ATOM 88 C LEU A 13 6.172 42.655 75.870 1.00 90.48 C ANISOU 88 C LEU A 13 7456 18490 8434 1946 -179 625 C ATOM 89 O LEU A 13 5.895 41.515 75.561 1.00 95.51 O ANISOU 89 O LEU A 13 8043 19227 9019 1852 -203 506 O ATOM 90 CB LEU A 13 6.412 43.313 78.245 1.00 94.28 C ANISOU 90 CB LEU A 13 8105 18575 9142 2031 -149 642 C ATOM 91 CG LEU A 13 7.281 43.224 79.491 1.00 87.05 C ANISOU 91 CG LEU A 13 7348 17385 8342 2041 -126 574 C ATOM 92 CD1 LEU A 13 6.493 43.629 80.727 1.00 97.48 C ANISOU 92 CD1 LEU A 13 8655 18627 9755 2084 -128 619 C ATOM 93 CD2 LEU A 13 7.803 41.806 79.613 1.00 75.36 C ANISOU 93 CD2 LEU A 13 5925 15849 6857 1948 -135 407 C ATOM 94 N ASP A 14 5.655 43.698 75.255 1.00 95.43 N ANISOU 94 N ASP A 14 7986 19253 9019 2014 -183 782 N ATOM 95 CA ASP A 14 4.652 43.524 74.247 1.00110.63 C ANISOU 95 CA ASP A 14 9736 21469 10830 1979 -223 825 C ATOM 96 C ASP A 14 5.273 42.736 73.160 1.00107.44 C ANISOU 96 C ASP A 14 9326 21187 10311 1897 -222 724 C ATOM 97 O ASP A 14 4.770 41.697 72.770 1.00102.88 O ANISOU 97 O ASP A 14 8665 20758 9668 1798 -254 618 O ATOM 98 CB ASP A 14 4.159 44.867 73.681 1.00121.72 C ANISOU 98 CB ASP A 14 11042 22993 12214 2080 -229 1026 C ATOM 99 CG ASP A 14 3.600 45.796 74.741 1.00132.30 C ANISOU 99 CG ASP A 14 12386 24203 13678 2179 -227 1127 C ATOM 100 OD1 ASP A 14 3.204 45.311 75.820 1.00149.40 O ANISOU 100 OD1 ASP A 14 14581 26267 15917 2157 -233 1052 O ATOM 101 OD2 ASP A 14 3.543 47.020 74.491 1.00132.06 O ANISOU 101 OD2 ASP A 14 12322 24178 13678 2282 -222 1284 O ATOM 102 N GLU A 15 6.445 43.175 72.750 1.00 94.01 N ANISOU 102 N GLU A 15 7719 19405 8595 1931 -184 741 N ATOM 103 CA GLU A 15 7.019 42.597 71.570 1.00 88.93 C ANISOU 103 CA GLU A 15 7050 18914 7825 1866 -181 665 C ATOM 104 C GLU A 15 7.230 41.134 71.803 1.00 91.80 C ANISOU 104 C GLU A 15 7452 19237 8190 1761 -193 453 C ATOM 105 O GLU A 15 6.998 40.344 70.925 1.00 98.68 O ANISOU 105 O GLU A 15 8231 20305 8957 1676 -215 364 O ATOM 106 CB GLU A 15 8.350 43.268 71.232 1.00 87.44 C ANISOU 106 CB GLU A 15 6969 18621 7632 1919 -135 709 C ATOM 107 CG GLU A 15 8.243 44.745 70.857 1.00101.10 C ANISOU 107 CG GLU A 15 8653 20394 9368 2020 -121 927 C ATOM 108 CD GLU A 15 7.484 44.994 69.545 1.00128.77 C ANISOU 108 CD GLU A 15 11977 24218 12732 2010 -148 1032 C ATOM 109 OE1 GLU A 15 7.676 44.233 68.568 1.00133.54 O ANISOU 109 OE1 GLU A 15 12527 25010 13204 1929 -154 941 O ATOM 110 OE2 GLU A 15 6.691 45.962 69.489 1.00135.79 O ANISOU 110 OE2 GLU A 15 12774 25175 13646 2086 -167 1205 O ATOM 111 N LEU A 16 7.664 40.767 72.994 1.00 90.14 N ANISOU 111 N LEU A 16 7371 18773 8106 1766 -182 371 N ATOM 112 CA LEU A 16 7.967 39.378 73.257 1.00 79.61 C ANISOU 112 CA LEU A 16 6079 17373 6797 1675 -194 173 C ATOM 113 C LEU A 16 6.767 38.479 73.145 1.00 81.19 C ANISOU 113 C LEU A 16 6141 17737 6971 1581 -238 107 C ATOM 114 O LEU A 16 6.841 37.366 72.679 1.00 77.39 O ANISOU 114 O LEU A 16 5622 17331 6452 1485 -255 -44 O ATOM 115 CB LEU A 16 8.527 39.240 74.669 1.00 75.95 C ANISOU 115 CB LEU A 16 5764 16608 6485 1704 -180 126 C ATOM 116 CG LEU A 16 9.854 39.951 74.906 1.00 74.03 C ANISOU 116 CG LEU A 16 5666 16175 6284 1777 -144 158 C ATOM 117 CD1 LEU A 16 9.883 40.596 76.267 1.00 73.65 C ANISOU 117 CD1 LEU A 16 5709 15902 6372 1840 -131 226 C ATOM 118 CD2 LEU A 16 11.039 39.000 74.755 1.00 73.36 C ANISOU 118 CD2 LEU A 16 5674 15996 6204 1733 -140 -10 C ATOM 119 N VAL A 17 5.663 38.975 73.639 1.00 84.75 N ANISOU 119 N VAL A 17 6513 18234 7453 1609 -258 218 N ATOM 120 CA VAL A 17 4.441 38.230 73.582 1.00 93.10 C ANISOU 120 CA VAL A 17 7425 19459 8489 1520 -305 176 C ATOM 121 C VAL A 17 4.081 38.043 72.147 1.00103.11 C ANISOU 121 C VAL A 17 8550 21023 9605 1456 -332 169 C ATOM 122 O VAL A 17 3.655 36.986 71.741 1.00107.53 O ANISOU 122 O VAL A 17 9020 21712 10125 1337 -367 44 O ATOM 123 CB VAL A 17 3.304 38.937 74.341 1.00 94.37 C ANISOU 123 CB VAL A 17 7516 19637 8702 1576 -322 312 C ATOM 124 CG1 VAL A 17 2.048 38.116 74.265 1.00106.90 C ANISOU 124 CG1 VAL A 17 8943 21412 10263 1472 -376 263 C ATOM 125 CG2 VAL A 17 3.688 39.129 75.785 1.00 93.22 C ANISOU 125 CG2 VAL A 17 7511 19207 8701 1634 -293 312 C ATOM 126 N LYS A 18 4.275 39.084 71.366 1.00107.22 N ANISOU 126 N LYS A 18 9044 21651 10043 1530 -318 305 N ATOM 127 CA LYS A 18 3.871 39.042 69.988 1.00 98.30 C ANISOU 127 CA LYS A 18 7764 20827 8760 1477 -348 325 C ATOM 128 C LYS A 18 4.614 37.961 69.283 1.00 94.51 C ANISOU 128 C LYS A 18 7302 20392 8214 1375 -341 137 C ATOM 129 O LYS A 18 4.049 37.270 68.496 1.00101.35 O ANISOU 129 O LYS A 18 8036 21484 8988 1267 -381 61 O ATOM 130 CB LYS A 18 4.125 40.378 69.297 1.00 93.51 C ANISOU 130 CB LYS A 18 7139 20302 8089 1583 -328 513 C ATOM 131 CG LYS A 18 2.966 41.341 69.375 1.00 92.64 C ANISOU 131 CG LYS A 18 6905 20311 7984 1654 -363 702 C ATOM 132 CD LYS A 18 3.459 42.737 69.056 1.00 92.93 C ANISOU 132 CD LYS A 18 6974 20314 8022 1782 -331 888 C ATOM 133 CE LYS A 18 2.341 43.751 69.168 1.00 95.54 C ANISOU 133 CE LYS A 18 7183 20743 8376 1871 -369 1079 C ATOM 134 NZ LYS A 18 2.834 45.090 68.750 1.00101.26 N ANISOU 134 NZ LYS A 18 7925 21441 9110 1990 -342 1262 N ATOM 135 N LEU A 19 5.891 37.823 69.571 1.00 82.72 N ANISOU 135 N LEU A 19 5971 18689 6772 1407 -293 58 N ATOM 136 CA LEU A 19 6.712 36.811 68.959 1.00 77.04 C ANISOU 136 CA LEU A 19 5278 17990 6002 1325 -283 -132 C ATOM 137 C LEU A 19 6.238 35.452 69.307 1.00 83.70 C ANISOU 137 C LEU A 19 6081 18820 6903 1205 -318 -311 C ATOM 138 O LEU A 19 6.335 34.547 68.532 1.00 86.76 O ANISOU 138 O LEU A 19 6403 19339 7222 1101 -331 -462 O ATOM 139 CB LEU A 19 8.150 36.894 69.446 1.00 73.25 C ANISOU 139 CB LEU A 19 4986 17251 5593 1392 -235 -185 C ATOM 140 CG LEU A 19 9.071 38.059 69.183 1.00 91.33 C ANISOU 140 CG LEU A 19 7360 19489 7851 1498 -192 -54 C ATOM 141 CD1 LEU A 19 10.438 37.408 69.140 1.00 90.64 C ANISOU 141 CD1 LEU A 19 7395 19266 7777 1486 -168 -216 C ATOM 142 CD2 LEU A 19 8.716 38.777 67.873 1.00103.25 C ANISOU 142 CD2 LEU A 19 8734 21292 9203 1504 -191 74 C ATOM 143 N LEU A 20 5.829 35.292 70.539 1.00 90.64 N ANISOU 143 N LEU A 20 7008 19513 7919 1218 -328 -302 N ATOM 144 CA LEU A 20 5.374 34.019 71.008 1.00 98.52 C ANISOU 144 CA LEU A 20 7969 20469 8997 1104 -359 -456 C ATOM 145 C LEU A 20 4.142 33.641 70.266 1.00 99.51 C ANISOU 145 C LEU A 20 7897 20884 9029 990 -415 -463 C ATOM 146 O LEU A 20 3.958 32.515 69.830 1.00105.41 O ANISOU 146 O LEU A 20 8568 21720 9762 854 -444 -626 O ATOM 147 CB LEU A 20 5.120 34.065 72.514 1.00106.59 C ANISOU 147 CB LEU A 20 9070 21250 10179 1149 -356 -412 C ATOM 148 CG LEU A 20 6.378 34.237 73.368 1.00100.52 C ANISOU 148 CG LEU A 20 8498 20178 9518 1239 -312 -433 C ATOM 149 CD1 LEU A 20 6.021 34.438 74.828 1.00111.00 C ANISOU 149 CD1 LEU A 20 9887 21304 10984 1284 -309 -366 C ATOM 150 CD2 LEU A 20 7.284 33.035 73.210 1.00 92.52 C ANISOU 150 CD2 LEU A 20 7541 19066 8548 1172 -308 -637 C ATOM 151 N GLN A 21 3.305 34.638 70.093 1.00 99.42 N ANISOU 151 N GLN A 21 7796 21024 8956 1045 -433 -282 N ATOM 152 CA GLN A 21 2.048 34.475 69.440 1.00104.61 C ANISOU 152 CA GLN A 21 8256 21971 9519 952 -497 -254 C ATOM 153 C GLN A 21 2.369 34.017 68.064 1.00111.44 C ANISOU 153 C GLN A 21 9046 23054 10244 861 -509 -355 C ATOM 154 O GLN A 21 1.800 33.072 67.572 1.00116.33 O ANISOU 154 O GLN A 21 9545 23835 10819 710 -560 -480 O ATOM 155 CB GLN A 21 1.291 35.806 69.414 1.00100.24 C ANISOU 155 CB GLN A 21 7631 21535 8921 1061 -510 -25 C ATOM 156 CG GLN A 21 -0.152 35.731 68.991 1.00105.54 C ANISOU 156 CG GLN A 21 8093 22490 9516 983 -586 28 C ATOM 157 CD GLN A 21 -0.799 37.099 69.010 1.00113.68 C ANISOU 157 CD GLN A 21 9060 23613 10521 1115 -597 258 C ATOM 158 OE1 GLN A 21 -2.021 37.228 68.865 1.00126.82 O ANISOU 158 OE1 GLN A 21 10558 25486 12140 1085 -660 331 O ATOM 159 NE2 GLN A 21 0.022 38.139 69.182 1.00115.32 N ANISOU 159 NE2 GLN A 21 9393 23663 10760 1261 -539 371 N ATOM 160 N SER A 22 3.343 34.683 67.475 1.00106.93 N ANISOU 160 N SER A 22 8548 22476 9604 948 -461 -307 N ATOM 161 CA SER A 22 3.744 34.475 66.103 1.00102.04 C ANISOU 161 CA SER A 22 7858 22080 8832 884 -462 -375 C ATOM 162 C SER A 22 4.294 33.111 65.857 1.00107.47 C ANISOU 162 C SER A 22 8565 22735 9535 758 -460 -628 C ATOM 163 O SER A 22 4.034 32.552 64.819 1.00128.23 O ANISOU 163 O SER A 22 11069 25603 12048 635 -494 -726 O ATOM 164 CB SER A 22 4.735 35.580 65.670 1.00 93.44 C ANISOU 164 CB SER A 22 6855 20964 7684 1018 -403 -248 C ATOM 165 OG SER A 22 5.763 35.097 64.823 1.00 92.35 O ANISOU 165 OG SER A 22 6746 20877 7464 975 -368 -387 O ATOM 166 N ARG A 23 5.085 32.587 66.777 1.00105.07 N ANISOU 166 N ARG A 23 8413 22136 9373 786 -423 -736 N ATOM 167 CA ARG A 23 5.692 31.293 66.538 1.00102.65 C ANISOU 167 CA ARG A 23 8125 21780 9097 677 -418 -982 C ATOM 168 C ARG A 23 4.822 30.196 67.081 1.00118.91 C ANISOU 168 C ARG A 23 10113 23809 11260 540 -472 -1097 C ATOM 169 O ARG A 23 5.142 29.033 66.955 1.00127.01 O ANISOU 169 O ARG A 23 11134 24786 12336 430 -479 -1304 O ATOM 170 CB ARG A 23 7.095 31.229 67.118 1.00 94.01 C ANISOU 170 CB ARG A 23 7220 20400 8098 775 -358 -1051 C ATOM 171 CG ARG A 23 7.955 32.331 66.581 1.00 92.35 C ANISOU 171 CG ARG A 23 7078 20226 7787 897 -309 -932 C ATOM 172 CD ARG A 23 9.339 31.865 66.192 1.00 89.35 C ANISOU 172 CD ARG A 23 6791 19767 7390 910 -266 -1093 C ATOM 173 NE ARG A 23 10.144 33.006 65.751 1.00 82.39 N ANISOU 173 NE ARG A 23 5974 18916 6415 1025 -222 -955 N ATOM 174 CZ ARG A 23 11.473 33.042 65.769 1.00 93.66 C ANISOU 174 CZ ARG A 23 7529 20207 7852 1089 -185 -1020 C ATOM 175 NH1 ARG A 23 12.176 31.996 66.204 1.00 86.77 N ANISOU 175 NH1 ARG A 23 6735 19153 7081 1061 -187 -1224 N ATOM 176 NH2 ARG A 23 12.101 34.133 65.355 1.00 99.29 N ANISOU 176 NH2 ARG A 23 8284 20962 8478 1180 -151 -875 N ATOM 177 N ASP A 24 3.698 30.576 67.665 1.00128.63 N ANISOU 177 N ASP A 24 11276 25074 12522 542 -511 -961 N ATOM 178 CA ASP A 24 2.750 29.612 68.178 1.00135.26 C ANISOU 178 CA ASP A 24 12029 25912 13451 403 -567 -1046 C ATOM 179 C ASP A 24 3.360 28.639 69.170 1.00126.13 C ANISOU 179 C ASP A 24 10986 24453 12483 380 -544 -1190 C ATOM 180 O ASP A 24 3.316 27.429 68.971 1.00119.39 O ANISOU 180 O ASP A 24 10083 23601 11679 229 -572 -1378 O ATOM 181 CB ASP A 24 2.061 28.829 67.039 1.00140.28 C ANISOU 181 CB ASP A 24 12489 26840 13969 208 -634 -1171 C ATOM 182 CG ASP A 24 0.771 28.120 67.498 1.00142.36 C ANISOU 182 CG ASP A 24 12628 27167 14295 57 -708 -1200 C ATOM 183 OD1 ASP A 24 0.525 28.055 68.726 1.00137.53 O ANISOU 183 OD1 ASP A 24 12071 26351 13834 97 -698 -1152 O ATOM 184 OD2 ASP A 24 0.010 27.627 66.629 1.00148.25 O ANISOU 184 OD2 ASP A 24 13219 28174 14936 -110 -779 -1272 O ATOM 185 N LEU A 25 3.982 29.167 70.217 1.00115.12 N ANISOU 185 N LEU A 25 9746 22796 11199 527 -496 -1105 N ATOM 186 CA LEU A 25 4.710 28.290 71.128 1.00110.27 C ANISOU 186 CA LEU A 25 9246 21890 10763 522 -474 -1232 C ATOM 187 C LEU A 25 3.892 27.866 72.354 1.00114.92 C ANISOU 187 C LEU A 25 9812 22349 11504 478 -500 -1198 C ATOM 188 O LEU A 25 2.967 28.563 72.782 1.00104.87 O ANISOU 188 O LEU A 25 8487 21148 10211 512 -517 -1042 O ATOM 189 CB LEU A 25 5.964 29.012 71.595 1.00100.95 C ANISOU 189 CB LEU A 25 8250 20489 9618 693 -415 -1175 C ATOM 190 CG LEU A 25 7.063 29.120 70.554 1.00 96.02 C ANISOU 190 CG LEU A 25 7671 19928 8885 726 -382 -1256 C ATOM 191 CD1 LEU A 25 8.052 30.208 70.934 1.00 95.28 C ANISOU 191 CD1 LEU A 25 7736 19677 8789 895 -336 -1134 C ATOM 192 CD2 LEU A 25 7.756 27.765 70.465 1.00 97.96 C ANISOU 192 CD2 LEU A 25 7935 20063 9222 640 -380 -1494 C ATOM 193 N ARG A 26 4.250 26.713 72.891 1.00123.54 N ANISOU 193 N ARG A 26 10935 23254 12750 403 -500 -1346 N ATOM 194 CA ARG A 26 3.487 26.082 73.939 1.00137.05 C ANISOU 194 CA ARG A 26 12602 24859 14610 327 -526 -1339 C ATOM 195 C ARG A 26 4.216 26.178 75.263 1.00139.50 C ANISOU 195 C ARG A 26 13068 24854 15082 448 -483 -1292 C ATOM 196 O ARG A 26 5.394 25.867 75.362 1.00137.84 O ANISOU 196 O ARG A 26 12973 24460 14940 504 -449 -1381 O ATOM 197 CB ARG A 26 3.208 24.615 73.592 1.00146.96 C ANISOU 197 CB ARG A 26 13753 26144 15939 122 -567 -1534 C ATOM 198 CG ARG A 26 2.622 23.786 74.739 1.00151.67 C ANISOU 198 CG ARG A 26 14316 26586 16726 30 -587 -1542 C ATOM 199 CD ARG A 26 2.663 22.293 74.422 1.00157.76 C ANISOU 199 CD ARG A 26 15017 27321 17604 -169 -619 -1751 C ATOM 200 NE ARG A 26 3.477 22.011 73.239 1.00165.08 N ANISOU 200 NE ARG A 26 15960 28322 18443 -193 -611 -1910 N ATOM 201 CZ ARG A 26 3.884 20.799 72.873 1.00160.25 C ANISOU 201 CZ ARG A 26 15311 27680 17895 -333 -620 -2131 C ATOM 202 NH1 ARG A 26 3.566 19.736 73.602 1.00162.72 N ANISOU 202 NH1 ARG A 26 15557 27922 18348 -468 -633 -2230 N ATOM 203 NH2 ARG A 26 4.617 20.650 71.779 1.00149.26 N ANISOU 203 NH2 ARG A 26 13891 26493 16328 -343 -593 -2318 N ATOM 204 N GLY A 27 3.495 26.639 76.274 1.00136.75 N ANISOU 204 N GLY A 27 12715 24459 14786 488 -485 -1151 N ATOM 205 CA GLY A 27 4.013 26.755 77.620 1.00131.83 C ANISOU 205 CA GLY A 27 12222 23560 14308 588 -450 -1094 C ATOM 206 C GLY A 27 3.286 25.826 78.564 1.00135.35 C ANISOU 206 C GLY A 27 12594 23923 14908 480 -471 -1113 C ATOM 207 O GLY A 27 2.809 24.770 78.167 1.00136.84 O ANISOU 207 O GLY A 27 12664 24189 15137 316 -507 -1229 O ATOM 208 N GLU A 28 3.174 26.241 79.818 1.00137.61 N ANISOU 208 N GLU A 28 12946 24062 15278 563 -449 -998 N ATOM 209 CA GLU A 28 2.462 25.466 80.813 1.00137.26 C ANISOU 209 CA GLU A 28 12830 23946 15376 471 -462 -991 C ATOM 210 C GLU A 28 1.050 25.371 80.296 1.00139.73 C ANISOU 210 C GLU A 28 12958 24531 15604 339 -513 -971 C ATOM 211 O GLU A 28 0.392 24.354 80.418 1.00140.87 O ANISOU 211 O GLU A 28 12984 24708 15833 177 -545 -1038 O ATOM 212 CB GLU A 28 2.498 26.109 82.211 1.00137.30 C ANISOU 212 CB GLU A 28 12929 23790 15450 591 -428 -856 C ATOM 213 CG GLU A 28 3.793 25.914 83.014 1.00141.45 C ANISOU 213 CG GLU A 28 13619 24023 16103 685 -386 -881 C ATOM 214 CD GLU A 28 3.676 26.382 84.476 1.00142.84 C ANISOU 214 CD GLU A 28 13863 24058 16350 769 -359 -758 C ATOM 215 OE1 GLU A 28 2.804 27.224 84.784 1.00140.87 O ANISOU 215 OE1 GLU A 28 13571 23932 16022 802 -362 -642 O ATOM 216 OE2 GLU A 28 4.460 25.901 85.323 1.00141.20 O ANISOU 216 OE2 GLU A 28 13745 23625 16279 802 -334 -779 O ATOM 217 N ASN A 29 0.584 26.475 79.738 1.00137.60 N ANISOU 217 N ASN A 29 12658 24457 15169 409 -520 -870 N ATOM 218 CA ASN A 29 -0.756 26.573 79.204 1.00138.13 C ANISOU 218 CA ASN A 29 12543 24806 15132 307 -571 -831 C ATOM 219 C ASN A 29 -0.862 26.737 77.690 1.00135.77 C ANISOU 219 C ASN A 29 12166 24752 14667 257 -604 -880 C ATOM 220 O ASN A 29 -1.924 27.066 77.177 1.00128.96 O ANISOU 220 O ASN A 29 11160 24147 13693 203 -647 -821 O ATOM 221 CB ASN A 29 -1.483 27.744 79.881 1.00143.17 C ANISOU 221 CB ASN A 29 13170 25508 15720 424 -560 -650 C ATOM 222 CG ASN A 29 -1.607 27.565 81.394 1.00146.05 C ANISOU 222 CG ASN A 29 13581 25682 16231 452 -533 -598 C ATOM 223 OD1 ASN A 29 -1.006 26.663 81.973 1.00143.69 O ANISOU 223 OD1 ASN A 29 13343 25177 16074 408 -517 -680 O ATOM 224 ND2 ASN A 29 -2.387 28.429 82.037 1.00146.63 N ANISOU 224 ND2 ASN A 29 13617 25827 16268 528 -527 -461 N ATOM 225 N GLY A 30 0.232 26.481 76.982 1.00132.39 N ANISOU 225 N GLY A 30 11824 24256 14223 273 -585 -989 N ATOM 226 CA GLY A 30 0.306 26.681 75.546 1.00131.97 C ANISOU 226 CA GLY A 30 11712 24425 14004 240 -606 -1038 C ATOM 227 C GLY A 30 0.187 28.099 75.028 1.00132.40 C ANISOU 227 C GLY A 30 11772 24634 13899 378 -594 -882 C ATOM 228 O GLY A 30 0.918 28.974 75.450 1.00130.83 O ANISOU 228 O GLY A 30 11711 24288 13709 541 -544 -792 O ATOM 229 N ASN A 31 -0.725 28.315 74.093 1.00133.87 N ANISOU 229 N ASN A 31 11802 25119 13943 304 -644 -851 N ATOM 230 CA ASN A 31 -0.801 29.543 73.310 1.00134.05 C ANISOU 230 CA ASN A 31 11803 25324 13806 414 -639 -718 C ATOM 231 C ASN A 31 -1.218 30.792 74.051 1.00124.67 C ANISOU 231 C ASN A 31 10641 24107 12621 570 -618 -517 C ATOM 232 O ASN A 31 -1.926 30.722 75.027 1.00124.19 O ANISOU 232 O ASN A 31 10548 23994 12645 562 -627 -468 O ATOM 233 CB ASN A 31 -1.771 29.300 72.146 1.00146.59 C ANISOU 233 CB ASN A 31 13194 27255 15249 272 -710 -744 C ATOM 234 CG ASN A 31 -1.682 30.353 71.063 1.00157.94 C ANISOU 234 CG ASN A 31 14597 28900 16514 361 -710 -636 C ATOM 235 OD1 ASN A 31 -0.613 30.902 70.801 1.00177.32 O ANISOU 235 OD1 ASN A 31 17178 31253 18944 478 -655 -616 O ATOM 236 ND2 ASN A 31 -2.811 30.638 70.423 1.00148.11 N ANISOU 236 ND2 ASN A 31 13172 27952 15149 302 -774 -562 N ATOM 237 N TRP A 32 -0.852 31.927 73.488 1.00113.98 N ANISOU 237 N TRP A 32 9324 22815 11167 699 -594 -402 N ATOM 238 CA TRP A 32 -1.222 33.216 74.020 1.00105.08 C ANISOU 238 CA TRP A 32 8213 21676 10037 849 -576 -211 C ATOM 239 C TRP A 32 -2.710 33.368 74.044 1.00113.72 C ANISOU 239 C TRP A 32 9119 23000 11089 801 -634 -127 C ATOM 240 O TRP A 32 -3.230 34.011 74.929 1.00115.73 O ANISOU 240 O TRP A 32 9372 23201 11399 888 -624 -13 O ATOM 241 CB TRP A 32 -0.588 34.357 73.215 1.00 97.80 C ANISOU 241 CB TRP A 32 7341 20807 9013 973 -547 -105 C ATOM 242 CG TRP A 32 -1.206 35.747 73.438 1.00 97.57 C ANISOU 242 CG TRP A 32 7271 20841 8960 1111 -546 103 C ATOM 243 CD1 TRP A 32 -1.935 36.471 72.537 1.00 99.14 C ANISOU 243 CD1 TRP A 32 7324 21307 9039 1136 -584 224 C ATOM 244 CD2 TRP A 32 -1.111 36.573 74.617 1.00105.05 C ANISOU 244 CD2 TRP A 32 8321 21580 10013 1242 -507 207 C ATOM 245 NE1 TRP A 32 -2.304 37.683 73.072 1.00 99.54 N ANISOU 245 NE1 TRP A 32 7378 21321 9124 1280 -571 396 N ATOM 246 CE2 TRP A 32 -1.818 37.770 74.349 1.00105.34 C ANISOU 246 CE2 TRP A 32 8263 21766 9994 1343 -522 384 C ATOM 247 CE3 TRP A 32 -0.501 36.418 75.872 1.00112.73 C ANISOU 247 CE3 TRP A 32 9450 22261 11123 1282 -464 168 C ATOM 248 CZ2 TRP A 32 -1.936 38.805 75.291 1.00113.06 C ANISOU 248 CZ2 TRP A 32 9298 22605 11055 1479 -494 510 C ATOM 249 CZ3 TRP A 32 -0.616 37.453 76.808 1.00108.16 C ANISOU 249 CZ3 TRP A 32 8929 21554 10613 1411 -436 295 C ATOM 250 CH2 TRP A 32 -1.332 38.628 76.511 1.00106.47 C ANISOU 250 CH2 TRP A 32 8619 21489 10346 1506 -450 458 C ATOM 251 N LYS A 33 -3.417 32.847 73.057 1.00123.58 N ANISOU 251 N LYS A 33 10201 24521 12232 667 -696 -179 N ATOM 252 CA LYS A 33 -4.869 33.000 73.151 1.00138.42 C ANISOU 252 CA LYS A 33 11893 26626 14075 622 -757 -96 C ATOM 253 C LYS A 33 -5.487 31.795 73.877 1.00144.35 C ANISOU 253 C LYS A 33 12582 27342 14924 463 -787 -210 C ATOM 254 O LYS A 33 -6.531 31.933 74.529 1.00148.94 O ANISOU 254 O LYS A 33 13058 28000 15533 455 -812 -137 O ATOM 255 CB LYS A 33 -5.485 33.161 71.746 1.00137.63 C ANISOU 255 CB LYS A 33 11619 26874 13801 556 -823 -70 C ATOM 256 CG LYS A 33 -4.930 34.324 70.896 1.00131.84 C ANISOU 256 CG LYS A 33 10921 26208 12963 699 -800 55 C ATOM 257 CD LYS A 33 -5.570 34.351 69.503 1.00137.93 C ANISOU 257 CD LYS A 33 11507 27340 13559 615 -875 73 C ATOM 258 CE LYS A 33 -5.007 35.462 68.602 1.00138.31 C ANISOU 258 CE LYS A 33 11580 27467 13504 747 -854 204 C ATOM 259 NZ LYS A 33 -5.565 35.390 67.202 1.00133.32 N ANISOU 259 NZ LYS A 33 10767 27196 12694 652 -932 212 N ATOM 260 N GLU A 34 -4.843 30.631 73.783 1.00140.69 N ANISOU 260 N GLU A 34 12177 26760 14519 337 -782 -387 N ATOM 261 CA GLU A 34 -5.170 29.518 74.675 1.00144.13 C ANISOU 261 CA GLU A 34 12595 27077 15092 207 -793 -488 C ATOM 262 C GLU A 34 -5.161 30.028 76.105 1.00138.93 C ANISOU 262 C GLU A 34 12030 26202 14554 337 -743 -384 C ATOM 263 O GLU A 34 -6.157 29.983 76.848 1.00128.31 O ANISOU 263 O GLU A 34 10586 24915 13250 305 -764 -327 O ATOM 264 CB GLU A 34 -4.181 28.368 74.517 1.00137.44 C ANISOU 264 CB GLU A 34 11843 26053 14326 105 -777 -677 C ATOM 265 CG GLU A 34 -4.454 27.458 73.360 1.00129.45 C ANISOU 265 CG GLU A 34 10707 25245 13231 -95 -840 -825 C ATOM 266 CD GLU A 34 -3.496 26.287 73.343 1.00136.92 C ANISOU 266 CD GLU A 34 11747 25990 14287 -193 -822 -1019 C ATOM 267 OE1 GLU A 34 -3.273 25.684 74.418 1.00139.92 O ANISOU 267 OE1 GLU A 34 12195 26129 14840 -208 -797 -1056 O ATOM 268 OE2 GLU A 34 -2.948 25.979 72.264 1.00146.34 O ANISOU 268 OE2 GLU A 34 12942 27266 15396 -250 -832 -1134 O ATOM 269 N PHE A 35 -3.981 30.512 76.458 1.00136.03 N ANISOU 269 N PHE A 35 11854 25594 14236 481 -678 -366 N ATOM 270 CA PHE A 35 -3.711 31.102 77.744 1.00129.08 C ANISOU 270 CA PHE A 35 11097 24488 13459 618 -626 -276 C ATOM 271 C PHE A 35 -4.668 32.256 78.054 1.00128.07 C ANISOU 271 C PHE A 35 10885 24497 13278 724 -634 -104 C ATOM 272 O PHE A 35 -5.304 32.250 79.102 1.00136.99 O ANISOU 272 O PHE A 35 11982 25586 14482 731 -630 -58 O ATOM 273 CB PHE A 35 -2.265 31.597 77.827 1.00131.85 C ANISOU 273 CB PHE A 35 11656 24602 13837 753 -564 -278 C ATOM 274 CG PHE A 35 -1.936 32.292 79.108 1.00124.10 C ANISOU 274 CG PHE A 35 10805 23396 12950 890 -515 -187 C ATOM 275 CD1 PHE A 35 -1.358 31.591 80.147 1.00124.81 C ANISOU 275 CD1 PHE A 35 11004 23237 13181 873 -488 -258 C ATOM 276 CD2 PHE A 35 -2.197 33.649 79.270 1.00116.29 C ANISOU 276 CD2 PHE A 35 9825 22447 11912 1033 -499 -32 C ATOM 277 CE1 PHE A 35 -1.053 32.221 81.326 1.00129.68 C ANISOU 277 CE1 PHE A 35 11736 23661 13873 989 -446 -179 C ATOM 278 CE2 PHE A 35 -1.899 34.283 80.445 1.00123.16 C ANISOU 278 CE2 PHE A 35 10812 23116 12867 1146 -456 38 C ATOM 279 CZ PHE A 35 -1.325 33.572 81.478 1.00127.94 C ANISOU 279 CZ PHE A 35 11526 23486 13597 1122 -430 -36 C ATOM 280 N LEU A 36 -4.786 33.238 77.160 1.00130.98 N ANISOU 280 N LEU A 36 11210 25034 13524 808 -644 -7 N ATOM 281 CA LEU A 36 -5.609 34.408 77.484 1.00130.61 C ANISOU 281 CA LEU A 36 11088 25091 13446 931 -649 161 C ATOM 282 C LEU A 36 -7.097 34.048 77.624 1.00133.50 C ANISOU 282 C LEU A 36 11241 25695 13789 831 -709 181 C ATOM 283 O LEU A 36 -7.877 34.819 78.190 1.00129.19 O ANISOU 283 O LEU A 36 10624 25213 13249 922 -711 301 O ATOM 284 CB LEU A 36 -5.414 35.493 76.415 1.00127.82 C ANISOU 284 CB LEU A 36 10719 24872 12975 1036 -652 266 C ATOM 285 CG LEU A 36 -5.941 36.910 76.652 1.00125.23 C ANISOU 285 CG LEU A 36 10350 24599 12632 1202 -647 448 C ATOM 286 CD1 LEU A 36 -5.530 37.454 78.000 1.00109.42 C ANISOU 286 CD1 LEU A 36 8494 22326 10754 1320 -587 492 C ATOM 287 CD2 LEU A 36 -5.422 37.801 75.544 1.00130.66 C ANISOU 287 CD2 LEU A 36 11054 25365 13225 1290 -642 532 C ATOM 288 N HIS A 37 -7.491 32.877 77.125 1.00139.34 N ANISOU 288 N HIS A 37 11871 26565 14506 640 -759 60 N ATOM 289 CA HIS A 37 -8.879 32.432 77.273 1.00149.46 C ANISOU 289 CA HIS A 37 12945 28074 15770 520 -820 66 C ATOM 290 C HIS A 37 -9.111 31.625 78.545 1.00156.03 C ANISOU 290 C HIS A 37 13793 28750 16741 443 -801 11 C ATOM 291 O HIS A 37 -10.151 31.775 79.190 1.00160.02 O ANISOU 291 O HIS A 37 14174 29365 17259 437 -818 78 O ATOM 292 CB HIS A 37 -9.318 31.591 76.074 1.00154.95 C ANISOU 292 CB HIS A 37 13491 29018 16365 328 -894 -36 C ATOM 293 CG HIS A 37 -10.637 30.907 76.270 1.00158.04 C ANISOU 293 CG HIS A 37 13678 29618 16753 163 -958 -62 C ATOM 294 ND1 HIS A 37 -11.827 31.597 76.399 1.00159.79 N ANISOU 294 ND1 HIS A 37 13730 30067 16915 212 -995 66 N ATOM 295 CD2 HIS A 37 -10.954 29.595 76.371 1.00158.49 C ANISOU 295 CD2 HIS A 37 13666 29690 16865 -56 -993 -200 C ATOM 296 CE1 HIS A 37 -12.815 30.739 76.563 1.00161.49 C ANISOU 296 CE1 HIS A 37 13780 30440 17139 29 -1049 6 C ATOM 297 NE2 HIS A 37 -12.313 29.516 76.552 1.00163.18 N ANISOU 297 NE2 HIS A 37 14053 30524 17425 -143 -1049 -154 N ATOM 298 N VAL A 38 -8.159 30.758 78.896 1.00155.05 N ANISOU 298 N VAL A 38 13809 28381 16721 383 -767 -109 N ATOM 299 CA VAL A 38 -8.244 29.987 80.148 1.00141.85 C ANISOU 299 CA VAL A 38 12166 26533 15196 318 -744 -152 C ATOM 300 C VAL A 38 -8.099 30.904 81.363 1.00125.10 C ANISOU 300 C VAL A 38 10150 24247 13137 499 -686 -35 C ATOM 301 O VAL A 38 -8.663 30.657 82.422 1.00128.88 O ANISOU 301 O VAL A 38 10585 24691 13693 474 -676 -11 O ATOM 302 CB VAL A 38 -7.159 28.875 80.197 1.00138.17 C ANISOU 302 CB VAL A 38 11829 25830 14838 228 -723 -303 C ATOM 303 CG1 VAL A 38 -7.166 28.143 81.527 1.00128.65 C ANISOU 303 CG1 VAL A 38 10660 24427 13796 178 -695 -328 C ATOM 304 CG2 VAL A 38 -7.353 27.896 79.039 1.00147.51 C ANISOU 304 CG2 VAL A 38 12902 27176 15969 29 -784 -438 C ATOM 305 N TYR A 39 -7.363 31.989 81.167 1.00125.05 N ANISOU 305 N TYR A 39 10271 24153 13089 673 -649 38 N ATOM 306 CA TYR A 39 -6.981 32.910 82.228 1.00120.58 C ANISOU 306 CA TYR A 39 9835 23398 12582 844 -591 131 C ATOM 307 C TYR A 39 -7.860 34.166 82.261 1.00123.85 C ANISOU 307 C TYR A 39 10149 23982 12925 970 -600 278 C ATOM 308 O TYR A 39 -7.822 34.937 83.220 1.00137.35 O ANISOU 308 O TYR A 39 11927 25576 14685 1098 -561 356 O ATOM 309 CB TYR A 39 -5.510 33.301 82.029 1.00122.78 C ANISOU 309 CB TYR A 39 10327 23448 12877 946 -544 108 C ATOM 310 CG TYR A 39 -4.952 34.395 82.922 1.00119.88 C ANISOU 310 CG TYR A 39 10107 22887 12554 1121 -489 200 C ATOM 311 CD1 TYR A 39 -4.272 34.070 84.089 1.00121.40 C ANISOU 311 CD1 TYR A 39 10441 22823 12862 1141 -447 163 C ATOM 312 CD2 TYR A 39 -5.063 35.747 82.573 1.00109.27 C ANISOU 312 CD2 TYR A 39 8760 21615 11142 1262 -482 320 C ATOM 313 CE1 TYR A 39 -3.744 35.052 84.899 1.00124.30 C ANISOU 313 CE1 TYR A 39 10942 23022 13266 1285 -401 235 C ATOM 314 CE2 TYR A 39 -4.543 36.738 83.379 1.00109.40 C ANISOU 314 CE2 TYR A 39 8907 21450 11209 1408 -434 392 C ATOM 315 CZ TYR A 39 -3.881 36.384 84.541 1.00123.01 C ANISOU 315 CZ TYR A 39 10771 22929 13038 1414 -395 344 C ATOM 316 OH TYR A 39 -3.348 37.357 85.359 1.00131.44 O ANISOU 316 OH TYR A 39 11966 23823 14153 1545 -352 406 O ATOM 317 N ASP A 40 -8.600 34.392 81.189 1.00130.10 N ANISOU 317 N ASP A 40 10781 25049 13603 938 -654 314 N ATOM 318 CA ASP A 40 -9.581 35.454 81.198 1.00144.22 C ANISOU 318 CA ASP A 40 12437 27025 15334 1046 -674 450 C ATOM 319 C ASP A 40 -10.942 34.916 80.819 1.00153.06 C ANISOU 319 C ASP A 40 13312 28454 16390 913 -745 445 C ATOM 320 O ASP A 40 -11.129 34.381 79.734 1.00154.38 O ANISOU 320 O ASP A 40 13384 28799 16475 792 -797 390 O ATOM 321 CB ASP A 40 -9.176 36.600 80.262 1.00144.81 C ANISOU 321 CB ASP A 40 12545 27148 15328 1182 -673 542 C ATOM 322 CG ASP A 40 -9.836 37.934 80.630 1.00136.49 C ANISOU 322 CG ASP A 40 11424 26165 14270 1353 -669 695 C ATOM 323 OD1 ASP A 40 -10.989 37.934 81.118 1.00136.82 O ANISOU 323 OD1 ASP A 40 11306 26365 14314 1341 -697 735 O ATOM 324 OD2 ASP A 40 -9.192 38.991 80.431 1.00125.30 O ANISOU 324 OD2 ASP A 40 10109 24644 12854 1500 -638 775 O ATOM 325 N LYS A 41 -11.890 35.063 81.730 1.00153.26 N ANISOU 325 N LYS A 41 13230 28550 16451 930 -747 499 N ATOM 326 CA LYS A 41 -13.257 34.645 81.498 1.00158.11 C ANISOU 326 CA LYS A 41 13597 29468 17008 812 -813 505 C ATOM 327 C LYS A 41 -13.943 35.458 80.415 1.00168.72 C ANISOU 327 C LYS A 41 14783 31097 18226 874 -871 601 C ATOM 328 O LYS A 41 -14.702 34.926 79.619 1.00177.95 O ANISOU 328 O LYS A 41 15772 32530 19310 736 -942 570 O ATOM 329 CB LYS A 41 -14.058 34.722 82.799 1.00156.74 C ANISOU 329 CB LYS A 41 13350 29300 16903 838 -792 549 C ATOM 330 N ASN A 42 -13.690 36.759 80.408 1.00173.05 N ANISOU 330 N ASN A 42 15391 31593 18767 1080 -844 719 N ATOM 331 CA ASN A 42 -14.401 37.663 79.515 1.00178.76 C ANISOU 331 CA ASN A 42 15954 32578 19389 1169 -899 836 C ATOM 332 C ASN A 42 -14.161 37.438 78.030 1.00183.25 C ANISOU 332 C ASN A 42 16481 33305 19840 1091 -951 811 C ATOM 333 O ASN A 42 -13.036 37.276 77.583 1.00183.57 O ANISOU 333 O ASN A 42 16686 33180 19881 1082 -919 755 O ATOM 334 CB ASN A 42 -14.048 39.115 79.864 1.00177.35 C ANISOU 334 CB ASN A 42 15869 32264 19252 1409 -854 965 C ATOM 335 N ALA A 43 -15.236 37.466 77.261 1.00185.18 N ANISOU 335 N ALA A 43 16494 33886 19980 1040 -1034 856 N ATOM 336 CA ALA A 43 -15.142 37.523 75.814 1.00188.75 C ANISOU 336 CA ALA A 43 16879 34534 20304 1000 -1092 867 C ATOM 337 C ALA A 43 -14.549 38.864 75.431 1.00188.34 C ANISOU 337 C ALA A 43 16917 34403 20242 1215 -1063 1003 C ATOM 338 O ALA A 43 -13.963 39.025 74.369 1.00183.67 O ANISOU 338 O ALA A 43 16362 33854 19571 1216 -1077 1013 O ATOM 339 CB ALA A 43 -16.509 37.331 75.174 1.00191.31 C ANISOU 339 CB ALA A 43 16921 35251 20517 906 -1194 896 C ATOM 340 N ASP A 44 -14.729 39.834 76.314 1.00190.30 N ANISOU 340 N ASP A 44 17192 34539 20575 1394 -1025 1109 N ATOM 341 CA ASP A 44 -14.427 41.215 76.027 1.00191.39 C ANISOU 341 CA ASP A 44 17371 34630 20719 1604 -1010 1258 C ATOM 342 C ASP A 44 -12.965 41.398 75.676 1.00189.83 C ANISOU 342 C ASP A 44 17404 34184 20540 1638 -949 1233 C ATOM 343 O ASP A 44 -12.624 42.219 74.829 1.00195.78 O ANISOU 343 O ASP A 44 18163 34980 21244 1738 -960 1333 O ATOM 344 CB ASP A 44 -14.787 42.096 77.228 1.00196.97 C ANISOU 344 CB ASP A 44 18089 35212 21540 1773 -970 1341 C ATOM 345 N SER A 45 -12.100 40.639 76.328 1.00177.67 N ANISOU 345 N SER A 45 16047 32390 19072 1558 -887 1104 N ATOM 346 CA SER A 45 -10.680 40.920 76.312 1.00162.28 C ANISOU 346 CA SER A 45 14330 30161 17168 1617 -818 1083 C ATOM 347 C SER A 45 -10.051 40.998 74.929 1.00149.31 C ANISOU 347 C SER A 45 12701 28610 15418 1595 -836 1092 C ATOM 348 O SER A 45 -10.140 40.071 74.140 1.00146.51 O ANISOU 348 O SER A 45 12277 28415 14974 1439 -878 999 O ATOM 349 CB SER A 45 -9.935 39.875 77.163 1.00159.25 C ANISOU 349 CB SER A 45 14112 29528 16868 1510 -764 927 C ATOM 350 OG SER A 45 -10.148 38.557 76.694 1.00155.63 O ANISOU 350 OG SER A 45 13582 29196 16355 1311 -805 795 O ATOM 351 N PRO A 46 -9.306 42.163 74.693 1.00143.69 N ANISOU 351 N PRO A 46 12095 27771 14729 1755 -798 1205 N ATOM 352 CA PRO A 46 -8.630 42.182 73.388 1.00139.07 C ANISOU 352 CA PRO A 46 11528 27273 14041 1725 -809 1211 C ATOM 353 C PRO A 46 -7.379 41.337 73.382 1.00128.85 C ANISOU 353 C PRO A 46 10421 25775 12761 1628 -754 1058 C ATOM 354 O PRO A 46 -6.938 40.976 74.446 1.00127.01 O ANISOU 354 O PRO A 46 10323 25299 12635 1620 -703 978 O ATOM 355 CB PRO A 46 -8.279 43.669 73.208 1.00144.42 C ANISOU 355 CB PRO A 46 12248 27876 14751 1920 -786 1384 C ATOM 356 CG PRO A 46 -8.107 44.165 74.558 1.00141.48 C ANISOU 356 CG PRO A 46 11992 27240 14525 2022 -729 1397 C ATOM 357 CD PRO A 46 -9.098 43.372 75.475 1.00147.61 C ANISOU 357 CD PRO A 46 12676 28075 15333 1940 -751 1317 C ATOM 358 N SER A 47 -6.830 41.017 72.215 1.00128.57 N ANISOU 358 N SER A 47 10384 25846 12620 1558 -767 1018 N ATOM 359 CA SER A 47 -5.613 40.217 72.152 1.00122.11 C ANISOU 359 CA SER A 47 9735 24845 11816 1474 -716 867 C ATOM 360 C SER A 47 -4.316 40.999 71.979 1.00112.19 C ANISOU 360 C SER A 47 8653 23391 10584 1586 -648 918 C ATOM 361 O SER A 47 -3.239 40.426 72.024 1.00103.44 O ANISOU 361 O SER A 47 7693 22112 9498 1538 -602 799 O ATOM 362 CB SER A 47 -5.711 39.196 71.007 1.00127.09 C ANISOU 362 CB SER A 47 10264 25706 12317 1305 -766 751 C ATOM 363 OG SER A 47 -6.403 38.020 71.391 1.00128.50 O ANISOU 363 OG SER A 47 10364 25948 12514 1150 -805 618 O ATOM 364 N ASP A 48 -4.410 42.305 71.806 1.00112.75 N ANISOU 364 N ASP A 48 8701 23479 10661 1735 -645 1095 N ATOM 365 CA ASP A 48 -3.235 43.068 71.466 1.00116.76 C ANISOU 365 CA ASP A 48 9345 23838 11179 1824 -590 1155 C ATOM 366 C ASP A 48 -2.498 43.393 72.718 1.00126.51 C ANISOU 366 C ASP A 48 10770 24736 12563 1899 -522 1135 C ATOM 367 O ASP A 48 -2.940 44.217 73.515 1.00134.42 O ANISOU 367 O ASP A 48 11767 25649 13656 2009 -516 1233 O ATOM 368 CB ASP A 48 -3.610 44.351 70.714 1.00122.48 C ANISOU 368 CB ASP A 48 9962 24717 11859 1950 -619 1361 C ATOM 369 CG ASP A 48 -2.405 45.262 70.447 1.00126.39 C ANISOU 369 CG ASP A 48 10595 25042 12385 2048 -559 1443 C ATOM 370 OD1 ASP A 48 -1.261 44.752 70.380 1.00136.86 O ANISOU 370 OD1 ASP A 48 12067 26227 13708 1991 -507 1331 O ATOM 371 OD2 ASP A 48 -2.605 46.493 70.295 1.00119.64 O ANISOU 371 OD2 ASP A 48 9696 24199 11564 2184 -567 1622 O ATOM 372 N PRO A 49 -1.256 42.761 72.826 1.00126.83 N ANISOU 372 N PRO A 49 10981 24586 12623 1842 -470 1003 N ATOM 373 CA PRO A 49 -0.657 42.941 74.139 1.00113.04 C ANISOU 373 CA PRO A 49 9404 22528 11018 1897 -418 971 C ATOM 374 C PRO A 49 -0.152 44.332 74.186 1.00111.02 C ANISOU 374 C PRO A 49 9213 22154 10814 2040 -384 1117 C ATOM 375 O PRO A 49 0.977 44.615 74.484 1.00118.41 O ANISOU 375 O PRO A 49 10308 22874 11808 2074 -333 1098 O ATOM 376 CB PRO A 49 0.484 41.914 74.157 1.00115.75 C ANISOU 376 CB PRO A 49 9890 22725 11363 1805 -384 799 C ATOM 377 CG PRO A 49 0.186 40.965 73.022 1.00125.24 C ANISOU 377 CG PRO A 49 10973 24176 12436 1679 -426 711 C ATOM 378 CD PRO A 49 -0.500 41.815 71.991 1.00135.38 C ANISOU 378 CD PRO A 49 12099 25721 13618 1729 -464 867 C ATOM 379 N SER A 50 -1.067 45.224 73.898 1.00105.79 N ANISOU 379 N SER A 50 8411 21645 10139 2125 -420 1270 N ATOM 380 CA SER A 50 -1.027 46.569 74.366 1.00105.75 C ANISOU 380 CA SER A 50 8436 21511 10232 2273 -400 1413 C ATOM 381 C SER A 50 -2.250 46.761 75.243 1.00111.49 C ANISOU 381 C SER A 50 9062 22276 11023 2320 -431 1449 C ATOM 382 O SER A 50 -2.822 47.825 75.303 1.00113.04 O ANISOU 382 O SER A 50 9178 22507 11265 2442 -449 1589 O ATOM 383 CB SER A 50 -0.960 47.552 73.210 1.00112.94 C ANISOU 383 CB SER A 50 9268 22561 11085 2352 -415 1574 C ATOM 384 OG SER A 50 0.185 47.297 72.405 1.00110.39 O ANISOU 384 OG SER A 50 9031 22218 10693 2299 -383 1532 O ATOM 385 N ARG A 51 -2.667 45.681 75.885 1.00123.75 N ANISOU 385 N ARG A 51 10608 23834 12578 2220 -440 1319 N ATOM 386 CA ARG A 51 -3.600 45.724 76.978 1.00126.90 C ANISOU 386 CA ARG A 51 10951 24214 13052 2252 -453 1322 C ATOM 387 C ARG A 51 -2.765 45.667 78.251 1.00129.50 C ANISOU 387 C ARG A 51 11471 24231 13501 2264 -394 1242 C ATOM 388 O ARG A 51 -2.071 44.702 78.510 1.00116.46 O ANISOU 388 O ARG A 51 9932 22467 11851 2165 -371 1109 O ATOM 389 CB ARG A 51 -4.563 44.531 76.909 1.00116.04 C ANISOU 389 CB ARG A 51 9442 23043 11607 2121 -501 1233 C ATOM 390 CG ARG A 51 -3.851 43.229 76.485 1.00114.39 C ANISOU 390 CG ARG A 51 9306 22818 11340 1967 -493 1075 C ATOM 391 CD ARG A 51 -3.863 42.124 77.547 1.00105.91 C ANISOU 391 CD ARG A 51 8295 21613 10332 1869 -480 931 C ATOM 392 NE ARG A 51 -5.062 41.292 77.436 1.00106.29 N ANISOU 392 NE ARG A 51 8165 21891 10330 1762 -537 891 N ATOM 393 CZ ARG A 51 -5.833 40.937 78.460 1.00116.55 C ANISOU 393 CZ ARG A 51 9413 23180 11691 1738 -545 866 C ATOM 394 NH1 ARG A 51 -5.540 41.331 79.695 1.00121.44 N ANISOU 394 NH1 ARG A 51 10148 23572 12421 1816 -498 876 N ATOM 395 NH2 ARG A 51 -6.901 40.186 78.247 1.00120.82 N ANISOU 395 NH2 ARG A 51 9779 23948 12180 1629 -600 832 N ATOM 396 N ARG A 52 -2.945 46.691 79.076 1.00147.12 N ANISOU 396 N ARG A 52 13721 26341 15836 2387 -377 1323 N ATOM 397 CA ARG A 52 -1.956 47.500 79.784 1.00155.70 C ANISOU 397 CA ARG A 52 14973 27151 17035 2469 -324 1337 C ATOM 398 C ARG A 52 -0.981 46.979 80.862 1.00152.21 C ANISOU 398 C ARG A 52 14721 26444 16668 2419 -277 1211 C ATOM 399 O ARG A 52 0.144 47.456 80.917 1.00162.37 O ANISOU 399 O ARG A 52 16147 27543 18004 2449 -240 1211 O ATOM 400 CB ARG A 52 -2.733 48.672 80.421 1.00171.79 C ANISOU 400 CB ARG A 52 16932 29176 19165 2612 -333 1449 C ATOM 401 CG ARG A 52 -1.934 49.583 81.358 1.00173.56 C ANISOU 401 CG ARG A 52 17300 29120 19525 2701 -286 1459 C ATOM 402 CD ARG A 52 -2.747 50.801 81.793 1.00172.14 C ANISOU 402 CD ARG A 52 17019 28951 19437 2853 -301 1573 C ATOM 403 NE ARG A 52 -3.089 51.661 80.660 1.00177.23 N ANISOU 403 NE ARG A 52 17544 29740 20055 2942 -335 1721 N ATOM 404 CZ ARG A 52 -3.764 52.802 80.758 1.00176.93 C ANISOU 404 CZ ARG A 52 17401 29728 20095 3090 -358 1841 C ATOM 405 NH1 ARG A 52 -4.177 53.233 81.943 1.00171.69 N ANISOU 405 NH1 ARG A 52 16735 28959 19540 3165 -347 1820 N ATOM 406 NH2 ARG A 52 -4.026 53.514 79.669 1.00177.91 N ANISOU 406 NH2 ARG A 52 17418 29987 20193 3169 -394 1982 N ATOM 407 N SER A 53 -1.377 46.099 81.765 1.00135.44 N ANISOU 407 N SER A 53 12602 24297 14564 2351 -280 1115 N ATOM 408 CA SER A 53 -0.460 45.849 82.880 1.00125.11 C ANISOU 408 CA SER A 53 11469 22728 13340 2333 -238 1024 C ATOM 409 C SER A 53 0.549 44.747 82.656 1.00103.32 C ANISOU 409 C SER A 53 8828 19879 10549 2221 -225 899 C ATOM 410 O SER A 53 0.207 43.635 82.273 1.00 98.89 O ANISOU 410 O SER A 53 8208 19440 9925 2118 -249 824 O ATOM 411 CB SER A 53 -1.233 45.559 84.173 1.00130.28 C ANISOU 411 CB SER A 53 12091 23359 14052 2331 -240 989 C ATOM 412 OG SER A 53 -0.369 45.616 85.311 1.00108.16 O ANISOU 412 OG SER A 53 9450 20308 11339 2341 -202 928 O ATOM 413 N HIS A 54 1.809 45.056 82.909 1.00 91.99 N ANISOU 413 N HIS A 54 7554 18231 9166 2242 -189 872 N ATOM 414 CA HIS A 54 2.790 44.013 82.625 1.00 95.74 C ANISOU 414 CA HIS A 54 8133 18632 9611 2146 -181 752 C ATOM 415 C HIS A 54 2.187 42.739 83.062 1.00109.68 C ANISOU 415 C HIS A 54 9851 20452 11368 2049 -202 656 C ATOM 416 O HIS A 54 2.343 41.717 82.444 1.00112.34 O ANISOU 416 O HIS A 54 10174 20857 11652 1957 -218 571 O ATOM 417 CB HIS A 54 4.116 44.181 83.405 1.00 93.52 C ANISOU 417 CB HIS A 54 8037 18084 9413 2162 -145 699 C ATOM 418 CG HIS A 54 4.750 45.534 83.291 1.00107.31 C ANISOU 418 CG HIS A 54 9838 19731 11205 2258 -120 792 C ATOM 419 ND1 HIS A 54 4.042 46.671 82.937 1.00108.23 N ANISOU 419 ND1 HIS A 54 9852 19944 11328 2349 -127 925 N ATOM 420 CD2 HIS A 54 6.024 45.934 83.495 1.00114.31 C ANISOU 420 CD2 HIS A 54 10861 20427 12143 2275 -93 773 C ATOM 421 CE1 HIS A 54 4.860 47.704 82.924 1.00116.99 C ANISOU 421 CE1 HIS A 54 11034 20918 12499 2417 -102 983 C ATOM 422 NE2 HIS A 54 6.071 47.289 83.257 1.00125.64 N ANISOU 422 NE2 HIS A 54 12274 21843 13620 2369 -81 892 N ATOM 423 N GLU A 55 1.463 42.814 84.161 1.00115.06 N ANISOU 423 N GLU A 55 10502 21109 12109 2071 -203 670 N ATOM 424 CA GLU A 55 0.958 41.665 84.834 1.00116.31 C ANISOU 424 CA GLU A 55 10626 21281 12284 1983 -216 586 C ATOM 425 C GLU A 55 0.106 40.969 83.836 1.00119.76 C ANISOU 425 C GLU A 55 10909 21960 12634 1904 -257 574 C ATOM 426 O GLU A 55 0.174 39.757 83.719 1.00123.87 O ANISOU 426 O GLU A 55 11423 22494 13147 1795 -271 471 O ATOM 427 CB GLU A 55 0.167 42.061 86.077 1.00122.83 C ANISOU 427 CB GLU A 55 11413 22086 13172 2034 -210 628 C ATOM 428 CG GLU A 55 -0.374 40.896 86.873 1.00134.03 C ANISOU 428 CG GLU A 55 12791 23518 14615 1943 -220 554 C ATOM 429 CD GLU A 55 -1.588 41.289 87.687 1.00145.71 C ANISOU 429 CD GLU A 55 14152 25098 16113 1987 -227 616 C ATOM 430 OE1 GLU A 55 -1.690 40.849 88.851 1.00147.69 O ANISOU 430 OE1 GLU A 55 14432 25265 16419 1965 -213 579 O ATOM 431 OE2 GLU A 55 -2.441 42.040 87.164 1.00149.10 O ANISOU 431 OE2 GLU A 55 14452 25698 16501 2048 -246 705 O ATOM 432 N ASP A 56 -0.642 41.703 83.026 1.00116.97 N ANISOU 432 N ASP A 56 10427 21801 12216 1953 -279 674 N ATOM 433 CA ASP A 56 -1.283 40.819 82.092 1.00101.14 C ANISOU 433 CA ASP A 56 8287 20016 10124 1849 -321 633 C ATOM 434 C ASP A 56 -0.226 40.086 81.291 1.00 98.49 C ANISOU 434 C ASP A 56 8040 19630 9752 1775 -315 533 C ATOM 435 O ASP A 56 -0.289 38.868 81.175 1.00 88.16 O ANISOU 435 O ASP A 56 6705 18355 8437 1659 -334 422 O ATOM 436 CB ASP A 56 -2.214 41.589 81.194 1.00110.15 C ANISOU 436 CB ASP A 56 9263 21401 11186 1901 -355 751 C ATOM 437 CG ASP A 56 -3.277 42.267 81.963 1.00122.66 C ANISOU 437 CG ASP A 56 10748 23045 12811 1979 -364 840 C ATOM 438 OD1 ASP A 56 -3.021 43.392 82.445 1.00121.64 O ANISOU 438 OD1 ASP A 56 10680 22793 12743 2103 -336 919 O ATOM 439 OD2 ASP A 56 -4.350 41.653 82.115 1.00134.68 O ANISOU 439 OD2 ASP A 56 12127 24733 14310 1913 -399 822 O ATOM 440 N LEU A 57 0.806 40.796 80.846 1.00100.99 N ANISOU 440 N LEU A 57 8465 19846 10059 1842 -286 565 N ATOM 441 CA LEU A 57 1.863 40.084 80.089 1.00107.53 C ANISOU 441 CA LEU A 57 9376 20633 10849 1777 -278 462 C ATOM 442 C LEU A 57 2.759 39.012 80.768 1.00104.15 C ANISOU 442 C LEU A 57 9080 19998 10496 1711 -263 318 C ATOM 443 O LEU A 57 3.052 37.971 80.206 1.00 89.71 O ANISOU 443 O LEU A 57 7241 18207 8639 1619 -277 204 O ATOM 444 CB LEU A 57 2.780 41.128 79.444 1.00102.28 C ANISOU 444 CB LEU A 57 8789 19917 10155 1863 -250 537 C ATOM 445 CG LEU A 57 1.913 42.082 78.629 1.00 90.16 C ANISOU 445 CG LEU A 57 7108 18600 8548 1924 -271 681 C ATOM 446 CD1 LEU A 57 2.708 43.267 78.107 1.00 88.29 C ANISOU 446 CD1 LEU A 57 6935 18306 8305 2020 -242 785 C ATOM 447 CD2 LEU A 57 1.270 41.271 77.523 1.00 85.51 C ANISOU 447 CD2 LEU A 57 6373 18272 7843 1826 -314 638 C ATOM 448 N VAL A 58 3.210 39.317 81.967 1.00118.08 N ANISOU 448 N VAL A 58 10960 21547 12357 1763 -235 325 N ATOM 449 CA VAL A 58 4.280 38.626 82.652 1.00123.79 C ANISOU 449 CA VAL A 58 11829 22047 13159 1735 -216 220 C ATOM 450 C VAL A 58 3.835 37.271 83.013 1.00109.94 C ANISOU 450 C VAL A 58 10023 20306 11443 1631 -238 118 C ATOM 451 O VAL A 58 4.570 36.309 83.021 1.00110.06 O ANISOU 451 O VAL A 58 10101 20217 11498 1573 -238 4 O ATOM 452 CB VAL A 58 4.777 39.351 83.963 1.00 78.85 C ANISOU 452 CB VAL A 58 6260 16137 7561 1814 -185 262 C ATOM 453 CG1 VAL A 58 5.409 40.690 83.643 1.00 86.30 C ANISOU 453 CG1 VAL A 58 7267 17030 8492 1910 -161 352 C ATOM 454 CG2 VAL A 58 3.661 39.547 84.932 1.00 82.95 C ANISOU 454 CG2 VAL A 58 6704 16694 8120 1832 -190 317 C ATOM 455 N GLN A 59 2.594 37.227 83.390 1.00 87.83 N ANISOU 455 N GLN A 59 7099 17629 8644 1610 -257 164 N ATOM 456 CA GLN A 59 2.019 35.979 83.772 1.00 90.46 C ANISOU 456 CA GLN A 59 7359 17990 9022 1502 -280 82 C ATOM 457 C GLN A 59 2.131 35.001 82.642 1.00104.97 C ANISOU 457 C GLN A 59 9135 19937 10812 1399 -307 -22 C ATOM 458 O GLN A 59 2.573 33.885 82.850 1.00102.23 O ANISOU 458 O GLN A 59 8821 19488 10534 1322 -311 -135 O ATOM 459 CB GLN A 59 0.539 36.173 84.113 1.00 95.78 C ANISOU 459 CB GLN A 59 7875 18839 9679 1491 -302 158 C ATOM 460 CG GLN A 59 0.238 36.458 85.568 1.00113.18 C ANISOU 460 CG GLN A 59 10111 20928 11963 1539 -281 205 C ATOM 461 CD GLN A 59 0.264 35.201 86.417 1.00128.17 C ANISOU 461 CD GLN A 59 12021 22724 13955 1446 -282 118 C ATOM 462 OE1 GLN A 59 0.395 34.081 85.904 1.00130.32 O ANISOU 462 OE1 GLN A 59 12259 23014 14242 1340 -303 21 O ATOM 463 NE2 GLN A 59 0.142 35.379 87.724 1.00131.48 N ANISOU 463 NE2 GLN A 59 12480 23034 14441 1486 -260 153 N ATOM 464 N PHE A 60 1.787 35.424 81.432 1.00112.18 N ANISOU 464 N PHE A 60 9958 21056 11611 1399 -326 15 N ATOM 465 CA PHE A 60 1.851 34.490 80.320 1.00103.78 C ANISOU 465 CA PHE A 60 8823 20119 10489 1291 -354 -94 C ATOM 466 C PHE A 60 3.283 34.105 80.150 1.00 91.45 C ANISOU 466 C PHE A 60 7410 18377 8961 1301 -328 -194 C ATOM 467 O PHE A 60 3.629 32.946 80.015 1.00 98.20 O ANISOU 467 O PHE A 60 8265 19184 9861 1211 -339 -328 O ATOM 468 CB PHE A 60 1.305 35.121 79.030 1.00113.79 C ANISOU 468 CB PHE A 60 9971 21651 11614 1298 -377 -25 C ATOM 469 CG PHE A 60 1.599 34.323 77.771 1.00111.74 C ANISOU 469 CG PHE A 60 9658 21524 11275 1199 -399 -140 C ATOM 470 CD1 PHE A 60 1.100 33.034 77.616 1.00108.01 C ANISOU 470 CD1 PHE A 60 9086 21129 10825 1051 -436 -265 C ATOM 471 CD2 PHE A 60 2.349 34.877 76.733 1.00 94.36 C ANISOU 471 CD2 PHE A 60 7496 19380 8977 1248 -383 -124 C ATOM 472 CE1 PHE A 60 1.360 32.308 76.475 1.00 97.58 C ANISOU 472 CE1 PHE A 60 7710 19932 9433 954 -457 -384 C ATOM 473 CE2 PHE A 60 2.605 34.151 75.605 1.00 91.51 C ANISOU 473 CE2 PHE A 60 7081 19153 8536 1157 -401 -237 C ATOM 474 CZ PHE A 60 2.100 32.870 75.474 1.00 92.25 C ANISOU 474 CZ PHE A 60 7078 19321 8653 1009 -439 -372 C ATOM 475 N LEU A 61 4.117 35.115 80.243 1.00 83.91 N ANISOU 475 N LEU A 61 6577 17309 7995 1413 -294 -124 N ATOM 476 CA LEU A 61 5.496 35.015 79.876 1.00 87.31 C ANISOU 476 CA LEU A 61 7137 17610 8428 1437 -272 -196 C ATOM 477 C LEU A 61 6.132 33.989 80.756 1.00104.99 C ANISOU 477 C LEU A 61 9462 19635 10793 1398 -267 -310 C ATOM 478 O LEU A 61 7.069 33.328 80.365 1.00112.05 O ANISOU 478 O LEU A 61 10415 20455 11703 1373 -264 -423 O ATOM 479 CB LEU A 61 6.189 36.363 80.009 1.00 81.95 C ANISOU 479 CB LEU A 61 6565 16839 7734 1557 -238 -85 C ATOM 480 CG LEU A 61 6.039 37.293 78.814 1.00 79.15 C ANISOU 480 CG LEU A 61 6145 16673 7254 1599 -237 9 C ATOM 481 CD1 LEU A 61 6.483 38.692 79.170 1.00 78.48 C ANISOU 481 CD1 LEU A 61 6145 16485 7190 1715 -205 139 C ATOM 482 CD2 LEU A 61 6.853 36.746 77.645 1.00 74.39 C ANISOU 482 CD2 LEU A 61 5552 16140 6574 1554 -238 -93 C ATOM 483 N THR A 62 5.647 33.883 81.975 1.00106.16 N ANISOU 483 N THR A 62 9617 19684 11035 1401 -265 -275 N ATOM 484 CA THR A 62 6.216 32.941 82.914 1.00 94.27 C ANISOU 484 CA THR A 62 8187 17973 9660 1371 -259 -362 C ATOM 485 C THR A 62 5.642 31.533 82.767 1.00 91.49 C ANISOU 485 C THR A 62 7722 17677 9362 1244 -288 -469 C ATOM 486 O THR A 62 5.935 30.655 83.548 1.00 98.58 O ANISOU 486 O THR A 62 8652 18419 10384 1209 -285 -531 O ATOM 487 CB THR A 62 6.036 33.512 84.353 1.00 83.24 C ANISOU 487 CB THR A 62 6851 16439 8336 1434 -239 -270 C ATOM 488 OG1 THR A 62 6.962 32.889 85.244 1.00104.16 O ANISOU 488 OG1 THR A 62 9612 18863 11102 1438 -225 -333 O ATOM 489 CG2 THR A 62 4.637 33.320 84.868 1.00 80.17 C ANISOU 489 CG2 THR A 62 6331 16169 7962 1388 -255 -220 C ATOM 490 N THR A 63 4.828 31.347 81.748 1.00 90.39 N ANISOU 490 N THR A 63 7443 17768 9132 1172 -317 -486 N ATOM 491 CA THR A 63 4.287 30.058 81.344 1.00 92.18 C ANISOU 491 CA THR A 63 7546 18084 9394 1030 -350 -600 C ATOM 492 C THR A 63 5.412 29.200 80.782 1.00 89.33 C ANISOU 492 C THR A 63 7245 17623 9073 999 -345 -751 C ATOM 493 O THR A 63 5.396 27.965 80.850 1.00 86.34 O ANISOU 493 O THR A 63 6815 17194 8796 896 -360 -868 O ATOM 494 CB THR A 63 3.100 30.217 80.401 1.00111.21 C ANISOU 494 CB THR A 63 9785 20789 11682 959 -386 -569 C ATOM 495 OG1 THR A 63 2.382 31.392 80.789 1.00120.63 O ANISOU 495 OG1 THR A 63 10956 22060 12819 1044 -380 -411 O ATOM 496 CG2 THR A 63 2.152 29.076 80.541 1.00118.55 C ANISOU 496 CG2 THR A 63 10571 21798 12676 806 -424 -638 C ATOM 497 N PHE A 64 6.410 29.874 80.228 1.00 93.37 N ANISOU 497 N PHE A 64 7860 18104 9512 1087 -323 -748 N ATOM 498 CA PHE A 64 7.393 29.185 79.413 1.00102.09 C ANISOU 498 CA PHE A 64 8996 19179 10613 1059 -322 -894 C ATOM 499 C PHE A 64 8.611 28.895 80.219 1.00105.74 C ANISOU 499 C PHE A 64 9604 19372 11200 1122 -298 -939 C ATOM 500 O PHE A 64 9.280 29.789 80.728 1.00100.48 O ANISOU 500 O PHE A 64 9062 18588 10529 1228 -275 -855 O ATOM 501 CB PHE A 64 7.763 29.992 78.174 1.00 96.84 C ANISOU 501 CB PHE A 64 8336 18677 9781 1104 -315 -874 C ATOM 502 CG PHE A 64 6.614 30.205 77.264 1.00107.10 C ANISOU 502 CG PHE A 64 9480 20262 10952 1037 -341 -835 C ATOM 503 CD1 PHE A 64 6.237 29.221 76.370 1.00111.17 C ANISOU 503 CD1 PHE A 64 9871 20936 11432 907 -371 -967 C ATOM 504 CD2 PHE A 64 5.865 31.368 77.338 1.00111.55 C ANISOU 504 CD2 PHE A 64 10008 20938 11437 1099 -341 -666 C ATOM 505 CE1 PHE A 64 5.150 29.410 75.548 1.00109.70 C ANISOU 505 CE1 PHE A 64 9531 21027 11123 835 -403 -928 C ATOM 506 CE2 PHE A 64 4.783 31.557 76.519 1.00105.05 C ANISOU 506 CE2 PHE A 64 9029 20387 10500 1041 -371 -621 C ATOM 507 CZ PHE A 64 4.423 30.579 75.624 1.00100.60 C ANISOU 507 CZ PHE A 64 8343 19989 9890 906 -404 -750 C ATOM 508 N LYS A 65 8.877 27.608 80.333 1.00104.88 N ANISOU 508 N LYS A 65 9469 19168 11214 1048 -306 -1074 N ATOM 509 CA LYS A 65 9.865 27.146 81.261 1.00101.16 C ANISOU 509 CA LYS A 65 9108 18436 10892 1097 -288 -1110 C ATOM 510 C LYS A 65 11.159 26.728 80.584 1.00 98.10 C ANISOU 510 C LYS A 65 8785 17978 10512 1124 -280 -1241 C ATOM 511 O LYS A 65 12.222 26.950 81.139 1.00 96.60 O ANISOU 511 O LYS A 65 8719 17607 10378 1210 -263 -1230 O ATOM 512 CB LYS A 65 9.285 25.987 82.064 1.00108.39 C ANISOU 512 CB LYS A 65 9946 19261 11975 1009 -296 -1148 C ATOM 513 CG LYS A 65 8.040 26.378 82.846 1.00113.37 C ANISOU 513 CG LYS A 65 10513 19958 12605 985 -304 -1018 C ATOM 514 CD LYS A 65 8.365 27.488 83.842 1.00102.49 C ANISOU 514 CD LYS A 65 9262 18467 11214 1108 -279 -881 C ATOM 515 CE LYS A 65 7.167 27.862 84.687 1.00 91.75 C ANISOU 515 CE LYS A 65 7836 17168 9856 1093 -282 -762 C ATOM 516 NZ LYS A 65 7.398 29.166 85.361 1.00 89.57 N ANISOU 516 NZ LYS A 65 7670 16838 9525 1211 -259 -637 N ATOM 517 N LYS A 66 11.096 26.132 79.395 1.00102.66 N ANISOU 517 N LYS A 66 9273 18704 11028 1048 -293 -1371 N ATOM 518 CA LYS A 66 12.301 25.489 78.856 1.00113.78 C ANISOU 518 CA LYS A 66 10725 20031 12475 1063 -284 -1523 C ATOM 519 C LYS A 66 13.335 26.491 78.334 1.00107.05 C ANISOU 519 C LYS A 66 9981 19195 11497 1168 -272 -1491 C ATOM 520 O LYS A 66 13.010 27.628 77.992 1.00 95.74 O ANISOU 520 O LYS A 66 8560 17897 9920 1205 -269 -1372 O ATOM 521 CB LYS A 66 11.924 24.500 77.742 1.00115.20 C ANISOU 521 CB LYS A 66 10769 20372 12629 938 -298 -1692 C ATOM 522 CG LYS A 66 12.973 23.403 77.518 1.00117.06 C ANISOU 522 CG LYS A 66 11020 20474 12984 931 -284 -1876 C ATOM 523 CD LYS A 66 13.470 22.838 78.860 1.00119.03 C ANISOU 523 CD LYS A 66 11336 20434 13456 980 -268 -1852 C ATOM 524 CE LYS A 66 14.703 21.956 78.704 1.00117.71 C ANISOU 524 CE LYS A 66 11203 20111 13410 1015 -246 -2007 C ATOM 525 NZ LYS A 66 14.433 20.746 77.878 1.00118.39 N ANISOU 525 NZ LYS A 66 11157 20276 13548 891 -242 -2201 N ATOM 526 N LYS A 67 14.586 26.041 78.292 1.00100.28 N ANISOU 526 N LYS A 67 9195 18198 10709 1212 -263 -1594 N ATOM 527 CA LYS A 67 15.725 26.887 77.984 1.00105.22 C ANISOU 527 CA LYS A 67 9928 18800 11252 1306 -255 -1564 C ATOM 528 C LYS A 67 15.619 27.559 76.622 1.00106.32 C ANISOU 528 C LYS A 67 10022 19190 11184 1297 -257 -1565 C ATOM 529 O LYS A 67 15.827 28.771 76.502 1.00103.39 O ANISOU 529 O LYS A 67 9710 18868 10706 1363 -248 -1435 O ATOM 530 CB LYS A 67 17.020 26.073 78.070 1.00110.53 C ANISOU 530 CB LYS A 67 10652 19301 12045 1339 -251 -1698 C ATOM 531 CG LYS A 67 18.279 26.922 77.965 1.00103.39 C ANISOU 531 CG LYS A 67 9858 18342 11084 1433 -248 -1655 C ATOM 532 CD LYS A 67 19.397 26.433 78.874 1.00 85.65 C ANISOU 532 CD LYS A 67 7693 15843 9008 1492 -242 -1686 C ATOM 533 CE LYS A 67 20.604 27.349 78.753 1.00 98.99 C ANISOU 533 CE LYS A 67 9477 17500 10634 1570 -242 -1636 C ATOM 534 NZ LYS A 67 21.739 26.941 79.626 1.00114.52 N ANISOU 534 NZ LYS A 67 11516 19239 12756 1627 -235 -1656 N ATOM 535 N GLU A 68 15.288 26.770 75.604 1.00108.51 N ANISOU 535 N GLU A 68 10188 19632 11409 1210 -264 -1710 N ATOM 536 CA GLU A 68 15.200 27.278 74.239 1.00101.63 C ANISOU 536 CA GLU A 68 9258 19023 10332 1190 -262 -1725 C ATOM 537 C GLU A 68 14.336 28.540 74.130 1.00 95.33 C ANISOU 537 C GLU A 68 8442 18378 9400 1214 -257 -1527 C ATOM 538 O GLU A 68 14.794 29.567 73.602 1.00101.14 O ANISOU 538 O GLU A 68 9221 19199 10010 1279 -244 -1437 O ATOM 539 CB GLU A 68 14.658 26.194 73.307 1.00109.78 C ANISOU 539 CB GLU A 68 10151 20228 11334 1065 -269 -1904 C ATOM 540 CG GLU A 68 15.498 24.927 73.271 1.00129.63 C ANISOU 540 CG GLU A 68 12664 22606 13985 1039 -266 -2117 C ATOM 541 CD GLU A 68 16.923 25.172 72.792 1.00139.35 C ANISOU 541 CD GLU A 68 13975 23799 15171 1123 -259 -2179 C ATOM 542 OE1 GLU A 68 17.133 25.304 71.565 1.00139.77 O ANISOU 542 OE1 GLU A 68 13977 24070 15060 1097 -256 -2259 O ATOM 543 OE2 GLU A 68 17.835 25.225 73.646 1.00138.82 O ANISOU 543 OE2 GLU A 68 14014 23496 15234 1210 -258 -2146 O ATOM 544 N ASP A 69 13.110 28.472 74.656 1.00 84.24 N ANISOU 544 N ASP A 69 6970 17003 8035 1164 -268 -1454 N ATOM 545 CA ASP A 69 12.181 29.599 74.584 1.00 84.75 C ANISOU 545 CA ASP A 69 6997 17215 7992 1187 -266 -1270 C ATOM 546 C ASP A 69 12.715 30.790 75.365 1.00 80.35 C ANISOU 546 C ASP A 69 6569 16505 7454 1306 -246 -1109 C ATOM 547 O ASP A 69 12.467 31.946 75.002 1.00 82.39 O ANISOU 547 O ASP A 69 6822 16879 7601 1355 -234 -965 O ATOM 548 CB ASP A 69 10.799 29.215 75.133 1.00110.50 C ANISOU 548 CB ASP A 69 10155 20517 11312 1109 -287 -1231 C ATOM 549 CG ASP A 69 10.351 27.816 74.715 1.00133.58 C ANISOU 549 CG ASP A 69 12959 23513 14284 970 -310 -1408 C ATOM 550 OD1 ASP A 69 10.839 27.297 73.687 1.00129.54 O ANISOU 550 OD1 ASP A 69 12410 23105 13704 924 -308 -1553 O ATOM 551 OD2 ASP A 69 9.490 27.236 75.420 1.00152.73 O ANISOU 551 OD2 ASP A 69 15321 25893 16815 900 -330 -1403 O ATOM 552 N LEU A 70 13.479 30.514 76.416 1.00 76.81 N ANISOU 552 N LEU A 70 6232 15801 7152 1349 -243 -1133 N ATOM 553 CA LEU A 70 13.960 31.583 77.273 1.00 80.75 C ANISOU 553 CA LEU A 70 6849 16147 7683 1444 -226 -992 C ATOM 554 C LEU A 70 15.128 32.325 76.634 1.00 71.22 C ANISOU 554 C LEU A 70 5717 14949 6394 1509 -212 -975 C ATOM 555 O LEU A 70 15.237 33.557 76.736 1.00 58.12 O ANISOU 555 O LEU A 70 4105 13292 4687 1572 -194 -829 O ATOM 556 CB LEU A 70 14.367 31.035 78.651 1.00 80.51 C ANISOU 556 CB LEU A 70 6903 15855 7833 1460 -227 -1017 C ATOM 557 CG LEU A 70 13.307 30.375 79.550 1.00 83.89 C ANISOU 557 CG LEU A 70 7270 16236 8367 1406 -237 -1009 C ATOM 558 CD1 LEU A 70 13.973 29.860 80.814 1.00 94.92 C ANISOU 558 CD1 LEU A 70 8757 17376 9931 1432 -232 -1031 C ATOM 559 CD2 LEU A 70 12.118 31.276 79.917 1.00 71.47 C ANISOU 559 CD2 LEU A 70 5652 14761 6743 1415 -234 -852 C ATOM 560 N GLN A 71 15.996 31.565 75.976 1.00 67.51 N ANISOU 560 N GLN A 71 5249 14485 5918 1489 -220 -1126 N ATOM 561 CA GLN A 71 17.087 32.150 75.213 1.00 74.26 C ANISOU 561 CA GLN A 71 6150 15383 6682 1537 -211 -1126 C ATOM 562 C GLN A 71 16.501 32.955 74.086 1.00 84.83 C ANISOU 562 C GLN A 71 7408 16983 7839 1530 -199 -1036 C ATOM 563 O GLN A 71 16.996 34.034 73.761 1.00 91.47 O ANISOU 563 O GLN A 71 8288 17859 8607 1588 -181 -922 O ATOM 564 CB GLN A 71 18.031 31.098 74.655 1.00 65.06 C ANISOU 564 CB GLN A 71 4979 14201 5540 1512 -225 -1320 C ATOM 565 CG GLN A 71 18.643 30.251 75.674 1.00 68.24 C ANISOU 565 CG GLN A 71 5443 14355 6128 1522 -235 -1405 C ATOM 566 CD GLN A 71 19.392 29.129 75.046 1.00 85.14 C ANISOU 566 CD GLN A 71 7549 16496 8303 1494 -247 -1605 C ATOM 567 OE1 GLN A 71 18.800 28.129 74.645 1.00101.28 O ANISOU 567 OE1 GLN A 71 9501 18618 10364 1419 -253 -1734 O ATOM 568 NE2 GLN A 71 20.705 29.290 74.921 1.00 97.31 N ANISOU 568 NE2 GLN A 71 9153 17960 9862 1548 -250 -1638 N ATOM 569 N LEU A 72 15.464 32.391 73.472 1.00 84.32 N ANISOU 569 N LEU A 72 7221 17107 7710 1454 -207 -1089 N ATOM 570 CA LEU A 72 14.733 33.079 72.433 1.00 75.32 C ANISOU 570 CA LEU A 72 5980 16237 6401 1439 -196 -995 C ATOM 571 C LEU A 72 14.353 34.470 72.931 1.00 73.27 C ANISOU 571 C LEU A 72 5755 15946 6138 1514 -178 -771 C ATOM 572 O LEU A 72 14.797 35.484 72.361 1.00 72.95 O ANISOU 572 O LEU A 72 5730 15979 6007 1569 -157 -661 O ATOM 573 CB LEU A 72 13.498 32.279 72.015 1.00 84.50 C ANISOU 573 CB LEU A 72 6999 17578 7530 1336 -213 -1065 C ATOM 574 CG LEU A 72 12.716 32.692 70.755 1.00 80.64 C ANISOU 574 CG LEU A 72 6370 17412 6857 1294 -209 -1007 C ATOM 575 CD1 LEU A 72 13.559 32.534 69.482 1.00 92.66 C ANISOU 575 CD1 LEU A 72 7869 19097 8240 1278 -193 -1109 C ATOM 576 CD2 LEU A 72 11.400 31.904 70.640 1.00 69.39 C ANISOU 576 CD2 LEU A 72 4802 16127 5437 1182 -238 -1063 C ATOM 577 N LEU A 73 13.585 34.510 74.020 1.00 67.00 N ANISOU 577 N LEU A 73 4970 15035 5452 1518 -186 -708 N ATOM 578 CA LEU A 73 13.019 35.763 74.507 1.00 65.71 C ANISOU 578 CA LEU A 73 4816 14859 5293 1582 -171 -510 C ATOM 579 C LEU A 73 14.069 36.765 74.989 1.00 68.29 C ANISOU 579 C LEU A 73 5271 15013 5665 1670 -147 -419 C ATOM 580 O LEU A 73 13.947 37.992 74.780 1.00 69.42 O ANISOU 580 O LEU A 73 5407 15207 5763 1727 -126 -260 O ATOM 581 CB LEU A 73 12.066 35.465 75.650 1.00 67.69 C ANISOU 581 CB LEU A 73 5051 15013 5655 1563 -185 -489 C ATOM 582 CG LEU A 73 10.729 34.845 75.255 1.00 81.24 C ANISOU 582 CG LEU A 73 6615 16926 7327 1479 -211 -516 C ATOM 583 CD1 LEU A 73 10.214 33.905 76.330 1.00 84.05 C ANISOU 583 CD1 LEU A 73 6967 17150 7818 1427 -231 -586 C ATOM 584 CD2 LEU A 73 9.693 35.927 74.989 1.00 88.10 C ANISOU 584 CD2 LEU A 73 7393 17961 8120 1513 -210 -339 C ATOM 585 N LYS A 74 15.103 36.242 75.639 1.00 69.78 N ANISOU 585 N LYS A 74 5565 14995 5952 1677 -151 -519 N ATOM 586 CA LYS A 74 16.193 37.091 76.105 1.00 76.13 C ANISOU 586 CA LYS A 74 6483 15635 6807 1745 -133 -452 C ATOM 587 C LYS A 74 16.855 37.733 74.891 1.00 68.14 C ANISOU 587 C LYS A 74 5453 14767 5671 1768 -118 -411 C ATOM 588 O LYS A 74 17.079 38.956 74.830 1.00 67.67 O ANISOU 588 O LYS A 74 5414 14701 5595 1823 -94 -264 O ATOM 589 CB LYS A 74 17.176 36.299 76.991 1.00 75.77 C ANISOU 589 CB LYS A 74 6537 15361 6891 1742 -146 -574 C ATOM 590 CG LYS A 74 16.727 36.196 78.470 1.00 79.08 C ANISOU 590 CG LYS A 74 7004 15597 7445 1748 -148 -544 C ATOM 591 CD LYS A 74 17.631 35.295 79.342 1.00 90.36 C ANISOU 591 CD LYS A 74 8514 16816 9004 1742 -161 -660 C ATOM 592 CE LYS A 74 17.622 33.836 78.853 1.00101.77 C ANISOU 592 CE LYS A 74 9902 18302 10464 1682 -184 -829 C ATOM 593 NZ LYS A 74 18.632 32.921 79.491 1.00 88.86 N ANISOU 593 NZ LYS A 74 8330 16474 8958 1684 -196 -944 N ATOM 594 N CYS A 75 17.129 36.885 73.909 1.00 72.60 N ANISOU 594 N CYS A 75 5966 15469 6149 1721 -131 -543 N ATOM 595 CA CYS A 75 17.723 37.309 72.649 1.00 96.45 C ANISOU 595 CA CYS A 75 8952 18664 9032 1730 -118 -525 C ATOM 596 C CYS A 75 16.939 38.449 72.009 1.00 83.98 C ANISOU 596 C CYS A 75 7293 17269 7347 1756 -93 -337 C ATOM 597 O CYS A 75 17.479 39.536 71.732 1.00 78.71 O ANISOU 597 O CYS A 75 6648 16605 6652 1809 -69 -205 O ATOM 598 CB CYS A 75 17.812 36.129 71.679 1.00 99.06 C ANISOU 598 CB CYS A 75 9210 19155 9273 1661 -137 -709 C ATOM 599 SG CYS A 75 18.917 36.443 70.323 1.00127.62 S ANISOU 599 SG CYS A 75 12807 22942 12739 1672 -127 -731 S ATOM 600 N HIS A 76 15.656 38.212 71.791 1.00 65.50 N ANISOU 600 N HIS A 76 4848 15078 4961 1717 -101 -318 N ATOM 601 CA HIS A 76 14.861 39.261 71.204 1.00 73.82 C ANISOU 601 CA HIS A 76 5811 16309 5929 1746 -83 -135 C ATOM 602 C HIS A 76 14.902 40.549 71.999 1.00 72.26 C ANISOU 602 C HIS A 76 5675 15953 5827 1828 -62 44 C ATOM 603 O HIS A 76 14.948 41.630 71.419 1.00 84.41 O ANISOU 603 O HIS A 76 7178 17581 7312 1875 -38 200 O ATOM 604 CB HIS A 76 13.414 38.827 71.031 1.00 87.91 C ANISOU 604 CB HIS A 76 7467 18261 7676 1693 -103 -135 C ATOM 605 CG HIS A 76 12.747 39.509 69.881 1.00104.51 C ANISOU 605 CG HIS A 76 9433 20641 9636 1695 -94 -4 C ATOM 606 ND1 HIS A 76 13.081 39.245 68.566 1.00104.47 N ANISOU 606 ND1 HIS A 76 9353 20864 9475 1653 -85 -55 N ATOM 607 CD2 HIS A 76 11.805 40.483 69.840 1.00108.92 C ANISOU 607 CD2 HIS A 76 9909 21289 10185 1738 -94 183 C ATOM 608 CE1 HIS A 76 12.355 40.007 67.771 1.00121.96 C ANISOU 608 CE1 HIS A 76 11444 23302 11592 1666 -80 101 C ATOM 609 NE2 HIS A 76 11.570 40.768 68.520 1.00121.17 N ANISOU 609 NE2 HIS A 76 11337 23118 11583 1721 -89 249 N ATOM 610 N ALA A 77 14.909 40.436 73.322 1.00 75.14 N ANISOU 610 N ALA A 77 6128 16084 6339 1844 -70 21 N ATOM 611 CA ALA A 77 14.881 41.622 74.157 1.00 71.61 C ANISOU 611 CA ALA A 77 5733 15485 5992 1914 -51 171 C ATOM 612 C ALA A 77 16.185 42.418 74.076 1.00 66.42 C ANISOU 612 C ALA A 77 5158 14717 5359 1960 -26 223 C ATOM 613 O ALA A 77 16.216 43.656 74.208 1.00 61.83 O ANISOU 613 O ALA A 77 4581 14090 4820 2019 -3 379 O ATOM 614 CB ALA A 77 14.577 41.237 75.563 1.00 74.91 C ANISOU 614 CB ALA A 77 6214 15704 6544 1910 -64 120 C ATOM 615 N ASN A 78 17.265 41.690 73.848 1.00 66.61 N ANISOU 615 N ASN A 78 5239 14700 5368 1931 -35 88 N ATOM 616 CA ASN A 78 18.566 42.313 73.715 1.00 69.56 C ANISOU 616 CA ASN A 78 5680 14986 5763 1964 -17 120 C ATOM 617 C ASN A 78 18.675 43.063 72.413 1.00 87.73 C ANISOU 617 C ASN A 78 7903 17495 7936 1981 6 236 C ATOM 618 O ASN A 78 19.131 44.220 72.394 1.00 95.27 O ANISOU 618 O ASN A 78 8872 18396 8929 2030 33 378 O ATOM 619 CB ASN A 78 19.687 41.279 73.807 1.00 67.68 C ANISOU 619 CB ASN A 78 5509 14660 5547 1932 -39 -62 C ATOM 620 CG ASN A 78 19.609 40.454 75.058 1.00 71.42 C ANISOU 620 CG ASN A 78 6051 14938 6149 1913 -62 -172 C ATOM 621 OD1 ASN A 78 19.281 40.963 76.139 1.00 71.21 O ANISOU 621 OD1 ASN A 78 6068 14760 6227 1938 -54 -102 O ATOM 622 ND2 ASN A 78 19.891 39.159 74.923 1.00 84.44 N ANISOU 622 ND2 ASN A 78 7701 16590 7793 1868 -89 -348 N ATOM 623 N HIS A 79 18.286 42.375 71.328 1.00 97.32 N ANISOU 623 N HIS A 79 9029 18947 9003 1936 -4 171 N ATOM 624 CA HIS A 79 18.168 42.991 70.013 1.00 92.12 C ANISOU 624 CA HIS A 79 8269 18534 8196 1944 18 287 C ATOM 625 C HIS A 79 17.336 44.265 70.153 1.00 84.20 C ANISOU 625 C HIS A 79 7214 17544 7233 2001 40 507 C ATOM 626 O HIS A 79 17.802 45.359 69.883 1.00 77.45 O ANISOU 626 O HIS A 79 6358 16677 6393 2049 68 657 O ATOM 627 CB HIS A 79 17.528 42.032 68.992 1.00100.99 C ANISOU 627 CB HIS A 79 9285 19924 9164 1877 3 182 C ATOM 628 CG HIS A 79 18.501 41.097 68.325 1.00121.59 C ANISOU 628 CG HIS A 79 11909 22604 11687 1831 -10 2 C ATOM 629 ND1 HIS A 79 18.245 40.512 67.100 1.00136.14 N ANISOU 629 ND1 HIS A 79 13643 24718 13365 1772 -11 -74 N ATOM 630 CD2 HIS A 79 19.715 40.639 68.712 1.00118.26 C ANISOU 630 CD2 HIS A 79 11584 22015 11333 1833 -26 -124 C ATOM 631 CE1 HIS A 79 19.263 39.740 66.762 1.00130.42 C ANISOU 631 CE1 HIS A 79 12954 23927 12673 1733 -35 -241 C ATOM 632 NE2 HIS A 79 20.169 39.799 67.721 1.00123.77 N ANISOU 632 NE2 HIS A 79 12233 22851 11941 1777 -44 -273 N ATOM 633 N LEU A 80 16.113 44.116 70.643 1.00 83.83 N ANISOU 633 N LEU A 80 7122 17508 7223 1997 24 523 N ATOM 634 CA LEU A 80 15.231 45.245 70.913 1.00 71.17 C ANISOU 634 CA LEU A 80 5463 15899 5679 2058 34 713 C ATOM 635 C LEU A 80 15.910 46.371 71.654 1.00 67.39 C ANISOU 635 C LEU A 80 5070 15195 5341 2124 59 821 C ATOM 636 O LEU A 80 15.647 47.547 71.406 1.00 69.12 O ANISOU 636 O LEU A 80 5235 15441 5587 2183 77 1003 O ATOM 637 CB LEU A 80 14.058 44.765 71.725 1.00 71.11 C ANISOU 637 CB LEU A 80 5431 15859 5730 2043 6 671 C ATOM 638 CG LEU A 80 12.707 45.232 71.241 1.00 82.25 C ANISOU 638 CG LEU A 80 6694 17468 7088 2062 -6 803 C ATOM 639 CD1 LEU A 80 11.765 44.053 71.365 1.00 96.64 C ANISOU 639 CD1 LEU A 80 8457 19390 8873 1991 -43 674 C ATOM 640 CD2 LEU A 80 12.211 46.410 72.059 1.00 83.91 C ANISOU 640 CD2 LEU A 80 6909 17544 7431 2146 -1 958 C ATOM 641 N LEU A 81 16.795 46.011 72.575 1.00 73.80 N ANISOU 641 N LEU A 81 6006 15781 6252 2113 56 708 N ATOM 642 CA LEU A 81 17.539 47.036 73.283 1.00 72.89 C ANISOU 642 CA LEU A 81 5966 15453 6274 2164 78 791 C ATOM 643 C LEU A 81 18.438 47.766 72.314 1.00 75.19 C ANISOU 643 C LEU A 81 6236 15820 6515 2182 105 890 C ATOM 644 O LEU A 81 18.360 48.992 72.260 1.00 88.21 O ANISOU 644 O LEU A 81 7852 17438 8228 2238 129 1060 O ATOM 645 CB LEU A 81 18.369 46.459 74.438 1.00 68.36 C ANISOU 645 CB LEU A 81 5520 14642 5813 2141 66 646 C ATOM 646 CG LEU A 81 19.530 47.384 74.853 1.00 64.07 C ANISOU 646 CG LEU A 81 5044 13917 5382 2174 89 702 C ATOM 647 CD1 LEU A 81 19.033 48.708 75.438 1.00 70.94 C ANISOU 647 CD1 LEU A 81 5896 14684 6374 2235 109 859 C ATOM 648 CD2 LEU A 81 20.515 46.697 75.790 1.00 67.65 C ANISOU 648 CD2 LEU A 81 5607 14174 5922 2144 74 548 C ATOM 649 N ILE A 82 19.279 47.039 71.560 1.00 76.49 N ANISOU 649 N ILE A 82 6410 16081 6571 2139 101 786 N ATOM 650 CA ILE A 82 20.252 47.722 70.688 1.00 81.50 C ANISOU 650 CA ILE A 82 7025 16785 7158 2153 127 877 C ATOM 651 C ILE A 82 19.486 48.568 69.675 1.00 84.44 C ANISOU 651 C ILE A 82 7271 17370 7441 2184 149 1072 C ATOM 652 O ILE A 82 19.956 49.630 69.244 1.00 84.88 O ANISOU 652 O ILE A 82 7298 17433 7521 2222 179 1230 O ATOM 653 CB ILE A 82 21.254 46.735 69.945 1.00 95.69 C ANISOU 653 CB ILE A 82 8836 18685 8835 2101 112 721 C ATOM 654 CG1 ILE A 82 20.571 45.482 69.401 1.00110.33 C ANISOU 654 CG1 ILE A 82 10640 20728 10551 2047 85 578 C ATOM 655 CG2 ILE A 82 22.350 46.263 70.863 1.00 73.06 C ANISOU 655 CG2 ILE A 82 6083 15588 6087 2089 95 579 C ATOM 656 CD1 ILE A 82 20.252 45.491 67.893 1.00103.55 C ANISOU 656 CD1 ILE A 82 9659 20194 9492 2025 97 636 C ATOM 657 N GLU A 83 18.278 48.121 69.346 1.00 86.53 N ANISOU 657 N GLU A 83 7454 17804 7621 2169 133 1067 N ATOM 658 CA GLU A 83 17.409 48.906 68.494 1.00 87.00 C ANISOU 658 CA GLU A 83 7380 18064 7613 2203 145 1255 C ATOM 659 C GLU A 83 17.022 50.225 69.172 1.00 85.03 C ANISOU 659 C GLU A 83 7126 17651 7529 2284 157 1433 C ATOM 660 O GLU A 83 17.298 51.278 68.604 1.00 88.98 O ANISOU 660 O GLU A 83 7575 18189 8043 2329 182 1609 O ATOM 661 CB GLU A 83 16.174 48.104 68.105 1.00 98.54 C ANISOU 661 CB GLU A 83 8745 19732 8965 2165 117 1198 C ATOM 662 CG GLU A 83 16.478 47.079 67.019 1.00119.18 C ANISOU 662 CG GLU A 83 11312 22582 11390 2090 113 1069 C ATOM 663 CD GLU A 83 15.324 46.136 66.750 1.00130.91 C ANISOU 663 CD GLU A 83 12704 24249 12786 2035 81 974 C ATOM 664 OE1 GLU A 83 14.169 46.479 67.106 1.00125.65 O ANISOU 664 OE1 GLU A 83 11973 23594 12174 2063 62 1063 O ATOM 665 OE2 GLU A 83 15.585 45.049 66.179 1.00136.98 O ANISOU 665 OE2 GLU A 83 13460 25151 13437 1963 73 804 O ATOM 666 N ASN A 84 16.436 50.212 70.371 1.00 89.54 N ANISOU 666 N ASN A 84 7747 18042 8232 2305 139 1392 N ATOM 667 CA ASN A 84 16.152 51.505 71.010 1.00 93.05 C ANISOU 667 CA ASN A 84 8185 18328 8841 2385 149 1547 C ATOM 668 C ASN A 84 17.407 52.358 71.147 1.00 85.23 C ANISOU 668 C ASN A 84 7259 17171 7955 2409 182 1608 C ATOM 669 O ASN A 84 17.337 53.593 71.161 1.00 80.68 O ANISOU 669 O ASN A 84 6642 16526 7485 2476 198 1777 O ATOM 670 CB ASN A 84 15.532 51.326 72.385 1.00 86.86 C ANISOU 670 CB ASN A 84 7458 17360 8184 2397 128 1468 C ATOM 671 CG ASN A 84 14.156 51.916 72.461 1.00112.21 C ANISOU 671 CG ASN A 84 10563 20643 11428 2458 109 1590 C ATOM 672 OD1 ASN A 84 13.223 51.422 71.816 1.00132.57 O ANISOU 672 OD1 ASN A 84 13041 23443 13888 2440 84 1597 O ATOM 673 ND2 ASN A 84 14.011 52.988 73.234 1.00121.61 N ANISOU 673 ND2 ASN A 84 11765 21657 12785 2531 114 1683 N ATOM 674 N LEU A 85 18.550 51.684 71.235 1.00 97.91 N ANISOU 674 N LEU A 85 8955 18711 9534 2354 188 1470 N ATOM 675 CA LEU A 85 19.831 52.353 71.378 1.00 92.27 C ANISOU 675 CA LEU A 85 8297 17846 8915 2364 214 1504 C ATOM 676 C LEU A 85 20.071 53.182 70.135 1.00 95.56 C ANISOU 676 C LEU A 85 8618 18429 9262 2389 242 1688 C ATOM 677 O LEU A 85 20.446 54.354 70.232 1.00 94.96 O ANISOU 677 O LEU A 85 8528 18241 9314 2437 267 1831 O ATOM 678 CB LEU A 85 20.981 51.359 71.610 1.00 75.62 C ANISOU 678 CB LEU A 85 6285 15669 6778 2302 204 1312 C ATOM 679 CG LEU A 85 22.409 51.916 71.503 1.00 81.77 C ANISOU 679 CG LEU A 85 7098 16349 7623 2300 228 1339 C ATOM 680 CD1 LEU A 85 22.585 53.221 72.282 1.00 84.96 C ANISOU 680 CD1 LEU A 85 7512 16535 8232 2351 251 1457 C ATOM 681 CD2 LEU A 85 23.445 50.876 71.961 1.00 82.12 C ANISOU 681 CD2 LEU A 85 7234 16299 7669 2248 207 1131 C ATOM 682 N LYS A 86 19.830 52.582 68.970 1.00104.19 N ANISOU 682 N LYS A 86 9636 19794 10157 2356 239 1686 N ATOM 683 CA LYS A 86 20.035 53.301 67.708 1.00 98.18 C ANISOU 683 CA LYS A 86 8772 19227 9304 2373 266 1867 C ATOM 684 C LYS A 86 19.038 54.478 67.573 1.00103.26 C ANISOU 684 C LYS A 86 9314 19892 10028 2452 269 2090 C ATOM 685 O LYS A 86 19.452 55.603 67.292 1.00 94.81 O ANISOU 685 O LYS A 86 8207 18776 9040 2498 294 2266 O ATOM 686 CB LYS A 86 19.943 52.332 66.506 1.00 80.55 C ANISOU 686 CB LYS A 86 6472 17303 6829 2313 259 1797 C ATOM 687 CG LYS A 86 21.238 51.498 66.315 1.00 74.21 C ANISOU 687 CG LYS A 86 5744 16502 5948 2252 258 1626 C ATOM 688 CD LYS A 86 21.129 50.306 65.340 1.00 87.95 C ANISOU 688 CD LYS A 86 7436 18518 7462 2185 241 1489 C ATOM 689 CE LYS A 86 19.928 49.388 65.634 1.00 96.42 C ANISOU 689 CE LYS A 86 8491 19649 8497 2160 210 1368 C ATOM 690 NZ LYS A 86 20.017 48.048 64.956 1.00 95.81 N ANISOU 690 NZ LYS A 86 8393 19770 8240 2085 189 1169 N ATOM 691 N GLN A 87 17.755 54.233 67.854 1.00108.38 N ANISOU 691 N GLN A 87 9919 20590 10672 2472 237 2079 N ATOM 692 CA GLN A 87 16.675 55.225 67.692 1.00 96.28 C ANISOU 692 CA GLN A 87 8275 19102 9205 2554 222 2275 C ATOM 693 C GLN A 87 16.707 56.469 68.579 1.00104.57 C ANISOU 693 C GLN A 87 9354 19889 10489 2638 228 2386 C ATOM 694 O GLN A 87 15.740 57.226 68.589 1.00104.47 O ANISOU 694 O GLN A 87 9257 19891 10547 2717 204 2525 O ATOM 695 CB GLN A 87 15.315 54.543 67.875 1.00 97.64 C ANISOU 695 CB GLN A 87 8393 19389 9318 2549 179 2208 C ATOM 696 CG GLN A 87 14.846 53.742 66.655 1.00113.76 C ANISOU 696 CG GLN A 87 10325 21763 11134 2493 163 2189 C ATOM 697 CD GLN A 87 13.518 53.042 66.889 1.00122.76 C ANISOU 697 CD GLN A 87 11405 23009 12229 2479 116 2114 C ATOM 698 OE1 GLN A 87 12.960 53.097 67.996 1.00137.31 O ANISOU 698 OE1 GLN A 87 13293 24678 14201 2511 97 2071 O ATOM 699 NE2 GLN A 87 13.005 52.373 65.852 1.00109.20 N ANISOU 699 NE2 GLN A 87 9575 21588 10329 2427 95 2095 N ATOM 700 N GLU A 88 17.777 56.675 69.339 1.00118.10 N ANISOU 700 N GLU A 88 11179 21365 12329 2624 253 2317 N ATOM 701 CA GLU A 88 17.900 57.885 70.157 1.00125.85 C ANISOU 701 CA GLU A 88 12181 22095 13542 2697 261 2410 C ATOM 702 C GLU A 88 18.999 58.755 69.547 1.00130.52 C ANISOU 702 C GLU A 88 12754 22654 14182 2707 299 2545 C ATOM 703 O GLU A 88 20.050 58.240 69.170 1.00136.71 O ANISOU 703 O GLU A 88 13583 23482 14880 2639 322 2472 O ATOM 704 CB GLU A 88 18.181 57.531 71.617 1.00121.01 C ANISOU 704 CB GLU A 88 11692 21228 13059 2674 256 2228 C ATOM 705 CG GLU A 88 17.033 56.758 72.265 1.00135.51 C ANISOU 705 CG GLU A 88 13536 23093 14860 2669 219 2117 C ATOM 706 CD GLU A 88 17.232 56.518 73.751 1.00151.91 C ANISOU 706 CD GLU A 88 15723 24923 17072 2653 213 1961 C ATOM 707 OE1 GLU A 88 18.289 56.916 74.290 1.00159.79 O ANISOU 707 OE1 GLU A 88 16793 25728 18191 2643 234 1927 O ATOM 708 OE2 GLU A 88 16.328 55.929 74.382 1.00152.14 O ANISOU 708 OE2 GLU A 88 15759 24961 17086 2649 185 1875 O ATOM 709 N SER A 89 18.763 60.050 69.442 1.00128.46 N ANISOU 709 N SER A 89 12425 22321 14063 2793 301 2739 N ATOM 710 CA SER A 89 19.713 60.925 68.771 1.00138.68 C ANISOU 710 CA SER A 89 13684 23603 15406 2805 336 2895 C ATOM 711 C SER A 89 20.997 61.215 69.535 1.00134.18 C ANISOU 711 C SER A 89 13207 22785 14992 2774 367 2813 C ATOM 712 O SER A 89 21.051 61.133 70.744 1.00128.79 O ANISOU 712 O SER A 89 12606 21885 14443 2772 358 2674 O ATOM 713 CB SER A 89 19.039 62.262 68.432 1.00148.21 C ANISOU 713 CB SER A 89 14786 24792 16736 2918 319 3137 C ATOM 714 OG SER A 89 18.596 62.288 67.084 1.00156.80 O ANISOU 714 OG SER A 89 15756 26165 17655 2930 308 3300 O ATOM 715 N GLN A 90 22.016 61.602 68.787 1.00135.35 N ANISOU 715 N GLN A 90 13325 22980 15120 2750 403 2909 N ATOM 716 CA GLN A 90 23.373 61.766 69.266 1.00126.42 C ANISOU 716 CA GLN A 90 12260 21670 14104 2705 433 2832 C ATOM 717 C GLN A 90 23.502 62.819 70.312 1.00124.13 C ANISOU 717 C GLN A 90 11992 21083 14091 2761 437 2853 C ATOM 718 O GLN A 90 24.468 62.844 71.051 1.00111.02 O ANISOU 718 O GLN A 90 10394 19238 12551 2721 453 2736 O ATOM 719 CB GLN A 90 24.289 62.129 68.096 1.00133.74 C ANISOU 719 CB GLN A 90 13118 22743 14953 2680 470 2978 C ATOM 720 CG GLN A 90 24.063 61.306 66.845 1.00136.49 C ANISOU 720 CG GLN A 90 13413 23429 15020 2637 467 3002 C ATOM 721 CD GLN A 90 25.094 60.214 66.697 1.00135.63 C ANISOU 721 CD GLN A 90 13366 23395 14772 2545 474 2814 C ATOM 722 OE1 GLN A 90 25.923 60.008 67.586 1.00146.43 O ANISOU 722 OE1 GLN A 90 14821 24560 16257 2513 476 2660 O ATOM 723 NE2 GLN A 90 25.057 59.507 65.572 1.00124.34 N ANISOU 723 NE2 GLN A 90 11886 22263 13095 2502 472 2818 N ATOM 724 N ASP A 91 22.554 63.733 70.340 1.00138.65 N ANISOU 724 N ASP A 91 13767 22878 16036 2856 418 3003 N ATOM 725 CA ASP A 91 22.813 65.087 70.748 1.00140.47 C ANISOU 725 CA ASP A 91 13970 22884 16519 2928 427 3119 C ATOM 726 C ASP A 91 23.379 65.200 72.147 1.00150.79 C ANISOU 726 C ASP A 91 15362 23908 18023 2907 431 2938 C ATOM 727 O ASP A 91 24.336 65.935 72.358 1.00158.34 O ANISOU 727 O ASP A 91 16312 24705 19144 2902 460 2963 O ATOM 728 CB ASP A 91 21.528 65.914 70.630 1.00127.88 C ANISOU 728 CB ASP A 91 12301 21291 14999 3049 387 3282 C ATOM 729 N GLU A 92 22.816 64.481 73.101 1.00145.95 N ANISOU 729 N GLU A 92 14820 23239 17397 2892 403 2758 N ATOM 730 CA GLU A 92 23.351 64.533 74.451 1.00146.29 C ANISOU 730 CA GLU A 92 14938 23032 17613 2867 403 2581 C ATOM 731 C GLU A 92 23.741 63.165 74.972 1.00137.14 C ANISOU 731 C GLU A 92 13877 21903 16328 2769 395 2357 C ATOM 732 O GLU A 92 23.906 62.965 76.162 1.00132.98 O ANISOU 732 O GLU A 92 13417 21207 15904 2748 382 2196 O ATOM 733 CB GLU A 92 22.335 65.192 75.385 1.00152.10 C ANISOU 733 CB GLU A 92 15665 23613 18511 2956 369 2577 C ATOM 734 CG GLU A 92 22.210 66.697 75.173 1.00154.89 C ANISOU 734 CG GLU A 92 15937 23848 19064 3063 371 2764 C ATOM 735 CD GLU A 92 20.823 67.228 75.484 1.00153.76 C ANISOU 735 CD GLU A 92 15751 23679 18991 3179 326 2829 C ATOM 736 OE1 GLU A 92 19.860 66.432 75.459 1.00152.88 O ANISOU 736 OE1 GLU A 92 15644 23718 18727 3176 299 2786 O ATOM 737 OE2 GLU A 92 20.697 68.443 75.747 1.00151.77 O ANISOU 737 OE2 GLU A 92 15457 23258 18951 3278 314 2920 O ATOM 738 N ASP A 93 23.902 62.232 74.054 1.00128.27 N ANISOU 738 N ASP A 93 12756 20999 14980 2714 400 2350 N ATOM 739 CA ASP A 93 24.276 60.874 74.378 1.00122.15 C ANISOU 739 CA ASP A 93 12069 20271 14073 2631 387 2148 C ATOM 740 C ASP A 93 25.677 60.866 74.992 1.00116.22 C ANISOU 740 C ASP A 93 11369 19353 13435 2575 405 2026 C ATOM 741 O ASP A 93 26.486 61.731 74.713 1.00117.92 O ANISOU 741 O ASP A 93 11537 19502 13765 2581 437 2115 O ATOM 742 CB ASP A 93 24.179 60.043 73.086 1.00124.60 C ANISOU 742 CB ASP A 93 12349 20864 14128 2597 388 2185 C ATOM 743 CG ASP A 93 25.010 58.788 73.115 1.00131.67 C ANISOU 743 CG ASP A 93 13319 21810 14900 2512 381 1997 C ATOM 744 OD1 ASP A 93 25.045 58.137 74.170 1.00138.17 O ANISOU 744 OD1 ASP A 93 14226 22506 15765 2484 358 1822 O ATOM 745 OD2 ASP A 93 25.619 58.448 72.074 1.00134.19 O ANISOU 745 OD2 ASP A 93 13607 22301 15077 2478 394 2025 O ATOM 746 N THR A 94 25.932 59.895 75.862 1.00107.99 N ANISOU 746 N THR A 94 10417 18244 12370 2522 382 1824 N ATOM 747 CA THR A 94 27.115 59.857 76.708 1.00 99.29 C ANISOU 747 CA THR A 94 9364 16967 11397 2475 389 1687 C ATOM 748 C THR A 94 28.242 58.996 76.215 1.00 96.26 C ANISOU 748 C THR A 94 9003 16672 10900 2406 396 1592 C ATOM 749 O THR A 94 28.047 57.881 75.766 1.00 98.01 O ANISOU 749 O THR A 94 9258 17049 10933 2377 375 1523 O ATOM 750 CB THR A 94 26.769 59.368 78.147 1.00102.21 C ANISOU 750 CB THR A 94 9814 17186 11833 2462 357 1519 C ATOM 751 OG1 THR A 94 26.132 58.082 78.096 1.00103.91 O ANISOU 751 OG1 THR A 94 10086 17534 11863 2436 326 1429 O ATOM 752 CG2 THR A 94 25.858 60.368 78.846 1.00106.65 C ANISOU 752 CG2 THR A 94 10347 17620 12554 2532 350 1586 C ATOM 753 N PRO A 95 29.442 59.519 76.347 1.00 91.93 N ANISOU 753 N PRO A 95 8430 16018 10481 2382 425 1577 N ATOM 754 CA PRO A 95 30.609 58.946 75.655 1.00 94.52 C ANISOU 754 CA PRO A 95 8746 16449 10718 2327 440 1523 C ATOM 755 C PRO A 95 30.674 57.413 75.637 1.00101.54 C ANISOU 755 C PRO A 95 9708 17446 11426 2284 403 1357 C ATOM 756 O PRO A 95 31.092 56.836 74.626 1.00118.35 O ANISOU 756 O PRO A 95 11812 19754 13402 2260 407 1354 O ATOM 757 CB PRO A 95 31.811 59.520 76.444 1.00 84.47 C ANISOU 757 CB PRO A 95 7459 14979 9656 2298 465 1447 C ATOM 758 CG PRO A 95 31.222 60.227 77.630 1.00 89.55 C ANISOU 758 CG PRO A 95 8124 15419 10483 2334 453 1434 C ATOM 759 CD PRO A 95 29.831 60.616 77.242 1.00 88.59 C ANISOU 759 CD PRO A 95 7984 15367 10308 2399 442 1580 C ATOM 760 N GLU A 96 30.260 56.757 76.712 1.00 94.51 N ANISOU 760 N GLU A 96 8900 16455 10554 2276 368 1221 N ATOM 761 CA GLU A 96 30.289 55.300 76.751 1.00101.64 C ANISOU 761 CA GLU A 96 9870 17442 11305 2240 331 1064 C ATOM 762 C GLU A 96 29.213 54.731 75.819 1.00 99.48 C ANISOU 762 C GLU A 96 9584 17381 10833 2255 314 1120 C ATOM 763 O GLU A 96 29.389 53.678 75.165 1.00107.72 O ANISOU 763 O GLU A 96 10637 18575 11716 2227 295 1036 O ATOM 764 CB GLU A 96 30.086 54.787 78.188 1.00117.74 C ANISOU 764 CB GLU A 96 11995 19320 13421 2228 300 921 C ATOM 765 CG GLU A 96 31.010 55.411 79.255 1.00113.75 C ANISOU 765 CG GLU A 96 11495 18606 13119 2214 313 863 C ATOM 766 CD GLU A 96 30.450 56.696 79.848 1.00119.22 C ANISOU 766 CD GLU A 96 12156 19161 13980 2256 329 962 C ATOM 767 OE1 GLU A 96 29.349 57.137 79.428 1.00121.53 O ANISOU 767 OE1 GLU A 96 12421 19517 14238 2301 330 1086 O ATOM 768 OE2 GLU A 96 31.120 57.264 80.737 1.00116.37 O ANISOU 768 OE2 GLU A 96 11791 18633 13792 2245 338 910 O ATOM 769 N GLN A 97 28.095 55.441 75.759 1.00 88.41 N ANISOU 769 N GLN A 97 8150 15992 9450 2301 320 1254 N ATOM 770 CA GLN A 97 26.996 55.021 74.913 1.00 93.00 C ANISOU 770 CA GLN A 97 8701 16778 9857 2318 307 1317 C ATOM 771 C GLN A 97 27.249 55.481 73.477 1.00109.17 C ANISOU 771 C GLN A 97 10660 19018 11803 2327 335 1467 C ATOM 772 O GLN A 97 26.755 54.866 72.524 1.00109.49 O ANISOU 772 O GLN A 97 10668 19279 11653 2319 323 1482 O ATOM 773 CB GLN A 97 25.686 55.572 75.476 1.00 95.88 C ANISOU 773 CB GLN A 97 9055 17085 10289 2368 301 1395 C ATOM 774 CG GLN A 97 24.396 54.984 74.916 1.00110.11 C ANISOU 774 CG GLN A 97 10830 19078 11929 2381 281 1422 C ATOM 775 CD GLN A 97 23.168 55.481 75.680 1.00130.01 C ANISOU 775 CD GLN A 97 13339 21518 14540 2431 271 1472 C ATOM 776 OE1 GLN A 97 23.291 56.199 76.684 1.00128.96 O ANISOU 776 OE1 GLN A 97 13229 21182 14586 2455 275 1469 O ATOM 777 NE2 GLN A 97 21.978 55.098 75.209 1.00132.08 N ANISOU 777 NE2 GLN A 97 13556 21948 14680 2447 255 1510 N ATOM 778 N MET A 98 28.015 56.565 73.332 1.00111.90 N ANISOU 778 N MET A 98 10957 19284 12276 2340 371 1576 N ATOM 779 CA MET A 98 28.582 56.922 72.041 1.00103.81 C ANISOU 779 CA MET A 98 9850 18432 11163 2335 400 1701 C ATOM 780 C MET A 98 29.294 55.702 71.526 1.00 92.64 C ANISOU 780 C MET A 98 8457 17155 9586 2280 381 1549 C ATOM 781 O MET A 98 29.003 55.209 70.439 1.00110.69 O ANISOU 781 O MET A 98 10701 19681 11676 2271 372 1580 O ATOM 782 CB MET A 98 29.566 58.101 72.145 1.00 98.47 C ANISOU 782 CB MET A 98 9125 17616 10674 2341 443 1794 C ATOM 783 CG MET A 98 30.512 58.228 70.939 1.00102.82 C ANISOU 783 CG MET A 98 9597 18336 11134 2313 474 1871 C ATOM 784 SD MET A 98 32.020 59.193 71.186 1.00147.66 S ANISOU 784 SD MET A 98 15223 23850 17031 2288 527 1893 S ATOM 785 CE MET A 98 32.713 59.214 69.529 1.00113.66 C ANISOU 785 CE MET A 98 10809 19825 12551 2258 560 2014 C ATOM 786 N LEU A 99 30.215 55.200 72.331 1.00 64.00 N ANISOU 786 N LEU A 99 4890 13381 6046 2245 371 1378 N ATOM 787 CA LEU A 99 31.007 54.071 71.907 1.00 82.27 C ANISOU 787 CA LEU A 99 7217 15802 8238 2200 352 1223 C ATOM 788 C LEU A 99 30.162 52.873 71.529 1.00 82.34 C ANISOU 788 C LEU A 99 7255 15973 8056 2191 308 1131 C ATOM 789 O LEU A 99 30.367 52.295 70.457 1.00 75.09 O ANISOU 789 O LEU A 99 6292 15269 6970 2171 299 1107 O ATOM 790 CB LEU A 99 31.994 53.680 73.002 1.00 91.88 C ANISOU 790 CB LEU A 99 8496 16820 9595 2172 345 1050 C ATOM 791 CG LEU A 99 33.447 54.068 72.774 1.00 97.62 C ANISOU 791 CG LEU A 99 9167 17518 10406 2145 383 1037 C ATOM 792 CD1 LEU A 99 33.533 55.555 72.484 1.00100.43 C ANISOU 792 CD1 LEU A 99 9445 17836 10878 2167 434 1237 C ATOM 793 CD2 LEU A 99 34.273 53.694 74.002 1.00101.76 C ANISOU 793 CD2 LEU A 99 9751 17840 11075 2122 374 868 C ATOM 794 N VAL A 100 29.210 52.492 72.371 1.00 85.30 N ANISOU 794 N VAL A 100 7695 16260 8456 2202 282 1074 N ATOM 795 CA VAL A 100 28.470 51.280 72.029 1.00 95.83 C ANISOU 795 CA VAL A 100 9046 17743 9622 2185 244 968 C ATOM 796 C VAL A 100 27.668 51.512 70.749 1.00 99.41 C ANISOU 796 C VAL A 100 9414 18452 9905 2199 253 1107 C ATOM 797 O VAL A 100 27.577 50.615 69.872 1.00102.94 O ANISOU 797 O VAL A 100 9832 19107 10173 2171 230 1031 O ATOM 798 CB VAL A 100 27.616 50.796 73.238 1.00 98.24 C ANISOU 798 CB VAL A 100 9429 17902 9995 2188 217 878 C ATOM 799 CG1 VAL A 100 26.574 51.814 73.626 1.00107.38 C ANISOU 799 CG1 VAL A 100 10567 18999 11234 2233 235 1031 C ATOM 800 CG2 VAL A 100 26.992 49.429 72.955 1.00 95.39 C ANISOU 800 CG2 VAL A 100 9084 17675 9484 2161 178 742 C ATOM 801 N ARG A 101 27.146 52.731 70.625 1.00 93.49 N ANISOU 801 N ARG A 101 8613 17691 9218 2241 285 1308 N ATOM 802 CA ARG A 101 26.503 53.176 69.396 1.00 94.67 C ANISOU 802 CA ARG A 101 8664 18080 9225 2260 302 1479 C ATOM 803 C ARG A 101 27.369 52.841 68.199 1.00 81.98 C ANISOU 803 C ARG A 101 7002 16683 7464 2225 305 1469 C ATOM 804 O ARG A 101 26.976 52.022 67.375 1.00 78.44 O ANISOU 804 O ARG A 101 6519 16463 6820 2200 283 1411 O ATOM 805 CB ARG A 101 26.230 54.669 69.459 1.00 97.94 C ANISOU 805 CB ARG A 101 9026 18412 9777 2315 340 1703 C ATOM 806 CG ARG A 101 25.904 55.307 68.163 1.00 90.70 C ANISOU 806 CG ARG A 101 7996 17726 8740 2335 364 1908 C ATOM 807 CD ARG A 101 25.035 56.492 68.450 1.00 96.61 C ANISOU 807 CD ARG A 101 8698 18384 9624 2404 382 2097 C ATOM 808 NE ARG A 101 23.624 56.133 68.365 1.00106.69 N ANISOU 808 NE ARG A 101 9946 19778 10815 2425 359 2107 N ATOM 809 CZ ARG A 101 22.627 56.989 68.549 1.00117.11 C ANISOU 809 CZ ARG A 101 11211 21058 12228 2492 359 2255 C ATOM 810 NH1 ARG A 101 21.373 56.571 68.436 1.00121.12 N ANISOU 810 NH1 ARG A 101 11678 21691 12650 2506 333 2250 N ATOM 811 NH2 ARG A 101 22.883 58.261 68.843 1.00116.96 N ANISOU 811 NH2 ARG A 101 11169 20872 12397 2545 381 2403 N ATOM 812 N LEU A 102 28.559 53.436 68.140 1.00 80.43 N ANISOU 812 N LEU A 102 6790 16411 7359 2220 330 1508 N ATOM 813 CA LEU A 102 29.513 53.122 67.079 1.00 87.62 C ANISOU 813 CA LEU A 102 7642 17510 8140 2184 331 1483 C ATOM 814 C LEU A 102 29.661 51.618 66.868 1.00 90.23 C ANISOU 814 C LEU A 102 8003 17951 8328 2142 283 1251 C ATOM 815 O LEU A 102 29.424 51.127 65.779 1.00 88.55 O ANISOU 815 O LEU A 102 7729 18001 7914 2120 266 1244 O ATOM 816 CB LEU A 102 30.886 53.725 67.369 1.00 85.53 C ANISOU 816 CB LEU A 102 7368 17096 8035 2173 363 1488 C ATOM 817 CG LEU A 102 31.123 55.151 66.879 1.00 85.04 C ANISOU 817 CG LEU A 102 7220 17045 8048 2196 416 1732 C ATOM 818 CD1 LEU A 102 30.193 56.134 67.562 1.00 95.19 C ANISOU 818 CD1 LEU A 102 8520 18168 9479 2250 433 1880 C ATOM 819 CD2 LEU A 102 32.561 55.538 67.118 1.00 94.18 C ANISOU 819 CD2 LEU A 102 8355 18076 9353 2168 451 1693 C ATOM 820 N THR A 103 30.019 50.861 67.892 1.00 97.43 N ANISOU 820 N THR A 103 9004 18671 9344 2128 258 1057 N ATOM 821 CA THR A 103 30.328 49.473 67.591 1.00 96.11 C ANISOU 821 CA THR A 103 8849 18605 9063 2091 214 841 C ATOM 822 C THR A 103 29.124 48.560 67.413 1.00 86.13 C ANISOU 822 C THR A 103 7597 17466 7661 2081 177 763 C ATOM 823 O THR A 103 29.296 47.349 67.340 1.00 83.44 O ANISOU 823 O THR A 103 7273 17170 7259 2051 137 565 O ATOM 824 CB THR A 103 31.272 48.827 68.661 1.00 84.19 C ANISOU 824 CB THR A 103 7416 16864 7707 2078 200 649 C ATOM 825 OG1 THR A 103 30.673 47.634 69.178 1.00 89.19 O ANISOU 825 OG1 THR A 103 8114 17462 8313 2066 155 479 O ATOM 826 CG2 THR A 103 31.583 49.764 69.786 1.00 72.45 C ANISOU 826 CG2 THR A 103 5976 15118 6433 2099 233 722 C ATOM 827 N VAL A 104 27.909 49.098 67.366 1.00 90.00 N ANISOU 827 N VAL A 104 8070 18008 8118 2106 193 907 N ATOM 828 CA VAL A 104 26.796 48.265 66.880 1.00 86.33 C ANISOU 828 CA VAL A 104 7578 17733 7492 2086 167 844 C ATOM 829 C VAL A 104 26.232 48.837 65.589 1.00 91.98 C ANISOU 829 C VAL A 104 8180 18734 8033 2089 191 1020 C ATOM 830 O VAL A 104 25.515 48.162 64.838 1.00101.85 O ANISOU 830 O VAL A 104 9375 20217 9108 2060 177 968 O ATOM 831 CB VAL A 104 25.659 48.118 67.936 1.00 74.70 C ANISOU 831 CB VAL A 104 6161 16109 6113 2103 161 827 C ATOM 832 CG1 VAL A 104 26.141 47.330 69.128 1.00 70.18 C ANISOU 832 CG1 VAL A 104 5692 15297 5676 2089 132 639 C ATOM 833 CG2 VAL A 104 25.099 49.478 68.347 1.00 72.81 C ANISOU 833 CG2 VAL A 104 5906 15767 5990 2154 199 1044 C ATOM 834 N GLU A 105 26.564 50.094 65.341 1.00 95.72 N ANISOU 834 N GLU A 105 8612 19194 8562 2121 232 1229 N ATOM 835 CA GLU A 105 26.183 50.744 64.107 1.00 97.56 C ANISOU 835 CA GLU A 105 8731 19696 8642 2126 261 1423 C ATOM 836 C GLU A 105 27.071 50.277 62.959 1.00 97.01 C ANISOU 836 C GLU A 105 8601 19865 8394 2079 243 1362 C ATOM 837 O GLU A 105 26.558 49.900 61.899 1.00107.00 O ANISOU 837 O GLU A 105 9780 21319 9557 2031 231 1346 O ATOM 838 CB GLU A 105 26.219 52.259 64.260 1.00100.25 C ANISOU 838 CB GLU A 105 9040 19926 9124 2178 308 1676 C ATOM 839 CG GLU A 105 24.927 52.783 64.863 1.00109.93 C ANISOU 839 CG GLU A 105 10263 21058 10448 2226 320 1782 C ATOM 840 CD GLU A 105 24.708 54.253 64.592 1.00122.92 C ANISOU 840 CD GLU A 105 11831 22690 12182 2281 362 2057 C ATOM 841 OE1 GLU A 105 25.701 54.939 64.262 1.00134.44 O ANISOU 841 OE1 GLU A 105 13268 24129 13683 2282 387 2157 O ATOM 842 OE2 GLU A 105 23.547 54.719 64.703 1.00118.84 O ANISOU 842 OE2 GLU A 105 11267 22182 11704 2326 365 2172 O ATOM 843 N HIS A 106 28.387 50.307 63.179 1.00 94.29 N ANISOU 843 N HIS A 106 8283 19397 8144 2071 236 1293 N ATOM 844 CA HIS A 106 29.349 49.757 62.230 1.00104.57 C ANISOU 844 CA HIS A 106 9523 20894 9313 2026 208 1193 C ATOM 845 C HIS A 106 28.834 48.460 61.602 1.00 98.41 C ANISOU 845 C HIS A 106 8716 20231 8445 1962 161 985 C ATOM 846 O HIS A 106 28.417 47.536 62.301 1.00 81.96 O ANISOU 846 O HIS A 106 6705 18033 6405 1955 134 808 O ATOM 847 CB HIS A 106 30.684 49.529 62.926 1.00106.28 C ANISOU 847 CB HIS A 106 9788 20886 9707 2019 205 1048 C ATOM 848 CG HIS A 106 31.739 48.956 62.033 1.00106.54 C ANISOU 848 CG HIS A 106 9740 21093 9647 1975 184 925 C ATOM 849 ND1 HIS A 106 32.886 49.653 61.700 1.00113.63 N ANISOU 849 ND1 HIS A 106 10571 21988 10615 1967 225 1002 N ATOM 850 CD2 HIS A 106 31.826 47.765 61.405 1.00 93.91 C ANISOU 850 CD2 HIS A 106 8102 19673 7909 1934 132 723 C ATOM 851 CE1 HIS A 106 33.631 48.905 60.912 1.00101.40 C ANISOU 851 CE1 HIS A 106 8943 20611 8975 1922 206 850 C ATOM 852 NE2 HIS A 106 33.017 47.751 60.718 1.00 88.88 N ANISOU 852 NE2 HIS A 106 7372 19135 7265 1904 145 676 N ATOM 853 N PRO A 107 28.894 48.394 60.267 1.00107.31 N ANISOU 853 N PRO A 107 9731 21581 9459 1910 154 1008 N ATOM 854 CA PRO A 107 28.198 47.424 59.406 1.00113.81 C ANISOU 854 CA PRO A 107 10494 22557 10191 1840 123 869 C ATOM 855 C PRO A 107 28.650 45.965 59.507 1.00107.12 C ANISOU 855 C PRO A 107 9670 21687 9344 1796 72 564 C ATOM 856 O PRO A 107 27.904 45.086 59.064 1.00110.61 O ANISOU 856 O PRO A 107 10075 22223 9728 1745 49 436 O ATOM 857 CB PRO A 107 28.485 47.953 57.998 1.00109.16 C ANISOU 857 CB PRO A 107 9713 22360 9402 1830 131 1016 C ATOM 858 CG PRO A 107 29.789 48.625 58.135 1.00108.47 C ANISOU 858 CG PRO A 107 9625 22234 9354 1859 143 1094 C ATOM 859 CD PRO A 107 29.733 49.309 59.474 1.00101.62 C ANISOU 859 CD PRO A 107 8922 21000 8689 1910 176 1178 C ATOM 860 N SER A 108 29.849 45.792 60.041 1.00 91.61 N ANISOU 860 N SER A 108 7743 19635 7430 1822 60 468 N ATOM 861 CA SER A 108 30.503 44.541 60.369 1.00 96.90 C ANISOU 861 CA SER A 108 8437 20255 8126 1805 20 193 C ATOM 862 C SER A 108 29.785 43.820 61.487 1.00105.30 C ANISOU 862 C SER A 108 9613 21108 9288 1819 4 73 C ATOM 863 O SER A 108 29.842 42.597 61.630 1.00 98.69 O ANISOU 863 O SER A 108 8787 20240 8471 1791 -33 -157 O ATOM 864 CB SER A 108 31.959 44.776 60.765 1.00101.72 C ANISOU 864 CB SER A 108 9049 20836 8762 1845 23 164 C ATOM 865 OG SER A 108 32.719 43.588 60.667 1.00114.21 O ANISOU 865 OG SER A 108 10600 22437 10357 1820 -6 -99 O ATOM 866 N TYR A 109 29.170 44.610 62.345 1.00111.10 N ANISOU 866 N TYR A 109 10424 21697 10091 1867 33 232 N ATOM 867 CA TYR A 109 28.650 44.091 63.580 1.00 94.76 C ANISOU 867 CA TYR A 109 8461 19423 8120 1889 21 140 C ATOM 868 C TYR A 109 27.604 43.057 63.339 1.00 84.99 C ANISOU 868 C TYR A 109 7206 18228 6859 1837 -4 5 C ATOM 869 O TYR A 109 27.626 42.014 63.942 1.00 83.20 O ANISOU 869 O TYR A 109 7027 17894 6689 1825 -35 -186 O ATOM 870 CB TYR A 109 28.055 45.242 64.421 1.00 99.13 C ANISOU 870 CB TYR A 109 9073 19859 8732 1948 61 355 C ATOM 871 CG TYR A 109 27.304 44.808 65.674 1.00 95.63 C ANISOU 871 CG TYR A 109 8725 19234 8376 1968 52 286 C ATOM 872 CD1 TYR A 109 27.978 44.570 66.865 1.00 98.97 C ANISOU 872 CD1 TYR A 109 9241 19370 8994 1982 44 189 C ATOM 873 CD2 TYR A 109 25.925 44.653 65.668 1.00 94.47 C ANISOU 873 CD2 TYR A 109 8559 19126 8207 1954 57 317 C ATOM 874 CE1 TYR A 109 27.314 44.159 67.998 1.00 88.22 C ANISOU 874 CE1 TYR A 109 7958 17819 7744 1988 33 128 C ATOM 875 CE2 TYR A 109 25.251 44.250 66.804 1.00 94.72 C ANISOU 875 CE2 TYR A 109 8665 19007 8316 1969 47 255 C ATOM 876 CZ TYR A 109 25.953 44.007 67.967 1.00 86.05 C ANISOU 876 CZ TYR A 109 7665 17631 7401 1981 34 163 C ATOM 877 OH TYR A 109 25.281 43.613 69.100 1.00 83.65 O ANISOU 877 OH TYR A 109 7427 17146 7211 1984 23 108 O ATOM 878 N SER A 110 26.711 43.324 62.414 1.00 90.66 N ANISOU 878 N SER A 110 7841 19118 7486 1803 12 104 N ATOM 879 CA SER A 110 25.535 42.514 62.308 1.00 92.37 C ANISOU 879 CA SER A 110 8034 19384 7678 1757 -1 10 C ATOM 880 C SER A 110 25.936 41.097 62.021 1.00 97.20 C ANISOU 880 C SER A 110 8629 20016 8288 1699 -44 -258 C ATOM 881 O SER A 110 25.378 40.186 62.565 1.00103.13 O ANISOU 881 O SER A 110 9412 20688 9085 1679 -64 -400 O ATOM 882 CB SER A 110 24.572 43.035 61.260 1.00107.94 C ANISOU 882 CB SER A 110 9897 21582 9536 1728 25 158 C ATOM 883 OG SER A 110 23.290 42.491 61.508 1.00109.15 O ANISOU 883 OG SER A 110 10030 21764 9676 1705 22 110 O ATOM 884 N LEU A 111 26.871 40.906 61.117 1.00107.51 N ANISOU 884 N LEU A 111 9867 21447 9534 1670 -58 -328 N ATOM 885 CA LEU A 111 27.423 39.586 60.881 1.00107.78 C ANISOU 885 CA LEU A 111 9872 21503 9575 1626 -98 -592 C ATOM 886 C LEU A 111 28.340 38.995 61.925 1.00 98.94 C ANISOU 886 C LEU A 111 8831 20191 8568 1671 -121 -743 C ATOM 887 O LEU A 111 28.265 37.822 62.198 1.00112.25 O ANISOU 887 O LEU A 111 10524 21823 10302 1646 -149 -949 O ATOM 888 CB LEU A 111 28.177 39.601 59.552 1.00115.49 C ANISOU 888 CB LEU A 111 10725 22714 10442 1584 -105 -623 C ATOM 889 CG LEU A 111 27.298 39.807 58.323 1.00125.64 C ANISOU 889 CG LEU A 111 11846 24373 11519 1541 -99 -549 C ATOM 890 CD1 LEU A 111 28.160 39.889 57.079 1.00135.38 C ANISOU 890 CD1 LEU A 111 12902 25953 12584 1519 -116 -578 C ATOM 891 CD2 LEU A 111 26.278 38.679 58.214 1.00126.61 C ANISOU 891 CD2 LEU A 111 11926 24578 11603 1480 -116 -724 C ATOM 892 N ASP A 112 29.269 39.779 62.428 1.00 93.29 N ANISOU 892 N ASP A 112 8161 19396 7889 1733 -107 -646 N ATOM 893 CA ASP A 112 30.234 39.265 63.389 1.00109.87 C ANISOU 893 CA ASP A 112 10324 21338 10082 1777 -127 -785 C ATOM 894 C ASP A 112 29.683 38.847 64.736 1.00101.11 C ANISOU 894 C ASP A 112 9330 19997 9089 1803 -138 -830 C ATOM 895 O ASP A 112 30.081 37.853 65.293 1.00 91.93 O ANISOU 895 O ASP A 112 8195 18712 8023 1805 -161 -1013 O ATOM 896 CB ASP A 112 31.350 40.293 63.581 1.00116.55 C ANISOU 896 CB ASP A 112 11178 22149 10955 1828 -98 -657 C ATOM 897 CG ASP A 112 32.238 40.419 62.348 1.00118.89 C ANISOU 897 CG ASP A 112 11345 22671 11155 1803 -89 -675 C ATOM 898 OD1 ASP A 112 32.425 39.406 61.638 1.00106.07 O ANISOU 898 OD1 ASP A 112 9636 21191 9476 1762 -117 -871 O ATOM 899 OD2 ASP A 112 32.742 41.530 62.085 1.00131.09 O1+ ANISOU 899 OD2 ASP A 112 12863 24251 12693 1821 -49 -496 O1+ ATOM 900 N TYR A 113 28.744 39.614 65.242 1.00 91.00 N ANISOU 900 N TYR A 113 8107 18644 7827 1819 -112 -655 N ATOM 901 CA TYR A 113 28.235 39.407 66.566 1.00 72.45 C ANISOU 901 CA TYR A 113 5858 16092 5576 1847 -117 -669 C ATOM 902 C TYR A 113 26.934 38.661 66.529 1.00 92.40 C ANISOU 902 C TYR A 113 8369 18640 8097 1800 -127 -734 C ATOM 903 O TYR A 113 26.087 38.868 67.365 1.00107.94 O ANISOU 903 O TYR A 113 10392 20511 10107 1816 -116 -664 O ATOM 904 CB TYR A 113 28.062 40.730 67.290 1.00 70.92 C ANISOU 904 CB TYR A 113 5727 15764 5456 1893 -75 -445 C ATOM 905 CG TYR A 113 29.375 41.254 67.811 1.00 85.60 C ANISOU 905 CG TYR A 113 7625 17443 7457 1924 -56 -417 C ATOM 906 CD1 TYR A 113 30.064 42.243 67.136 1.00 91.79 C ANISOU 906 CD1 TYR A 113 8355 18321 8197 1937 -26 -284 C ATOM 907 CD2 TYR A 113 29.945 40.734 68.962 1.00 82.75 C ANISOU 907 CD2 TYR A 113 7340 16826 7273 1936 -63 -524 C ATOM 908 CE1 TYR A 113 31.254 42.731 67.610 1.00 74.46 C ANISOU 908 CE1 TYR A 113 6182 15968 6140 1958 1 -263 C ATOM 909 CE2 TYR A 113 31.139 41.213 69.438 1.00 70.35 C ANISOU 909 CE2 TYR A 113 5794 15107 5828 1959 -39 -502 C ATOM 910 CZ TYR A 113 31.790 42.206 68.756 1.00 63.48 C ANISOU 910 CZ TYR A 113 4868 14333 4919 1968 -5 -378 C ATOM 911 OH TYR A 113 32.994 42.681 69.217 1.00 71.77 O ANISOU 911 OH TYR A 113 5928 15241 6100 1983 27 -364 O ATOM 912 N SER A 114 26.741 37.839 65.517 1.00 89.59 N ANISOU 912 N SER A 114 7926 18435 7680 1737 -143 -864 N ATOM 913 CA SER A 114 25.559 37.019 65.467 1.00 84.05 C ANISOU 913 CA SER A 114 7195 17770 6969 1683 -152 -951 C ATOM 914 C SER A 114 25.934 35.620 65.872 1.00 89.11 C ANISOU 914 C SER A 114 7848 18322 7688 1664 -190 -1199 C ATOM 915 O SER A 114 26.755 34.999 65.237 1.00 94.61 O ANISOU 915 O SER A 114 8489 19089 8372 1644 -210 -1348 O ATOM 916 CB SER A 114 24.945 37.048 64.068 1.00 80.43 C ANISOU 916 CB SER A 114 6619 17555 6385 1617 -140 -928 C ATOM 917 OG SER A 114 23.666 36.451 64.077 1.00 95.91 O ANISOU 917 OG SER A 114 8544 19574 8326 1566 -140 -977 O ATOM 918 N PHE A 115 25.337 35.123 66.945 1.00 91.82 N ANISOU 918 N PHE A 115 8253 18521 8113 1672 -200 -1244 N ATOM 919 CA PHE A 115 25.824 33.897 67.544 1.00 84.75 C ANISOU 919 CA PHE A 115 7380 17508 7311 1672 -235 -1459 C ATOM 920 C PHE A 115 24.935 32.678 67.440 1.00 78.85 C ANISOU 920 C PHE A 115 6580 16799 6579 1604 -250 -1626 C ATOM 921 O PHE A 115 25.381 31.596 67.731 1.00 75.92 O ANISOU 921 O PHE A 115 6204 16332 6311 1595 -273 -1812 O ATOM 922 CB PHE A 115 26.170 34.161 69.025 1.00 76.46 C ANISOU 922 CB PHE A 115 6447 16159 6445 1729 -226 -1387 C ATOM 923 CG PHE A 115 27.267 35.169 69.228 1.00 68.72 C ANISOU 923 CG PHE A 115 5514 15093 5505 1784 -206 -1265 C ATOM 924 CD1 PHE A 115 28.575 34.857 68.928 1.00 67.35 C ANISOU 924 CD1 PHE A 115 5316 14892 5384 1799 -210 -1364 C ATOM 925 CD2 PHE A 115 26.985 36.425 69.724 1.00 70.40 C ANISOU 925 CD2 PHE A 115 5783 15249 5718 1819 -177 -1054 C ATOM 926 CE1 PHE A 115 29.597 35.794 69.123 1.00 69.20 C ANISOU 926 CE1 PHE A 115 5581 15051 5662 1843 -185 -1253 C ATOM 927 CE2 PHE A 115 27.985 37.356 69.918 1.00 67.18 C ANISOU 927 CE2 PHE A 115 5408 14759 5359 1861 -154 -948 C ATOM 928 CZ PHE A 115 29.296 37.043 69.622 1.00 65.06 C ANISOU 928 CZ PHE A 115 5114 14469 5136 1870 -158 -1047 C ATOM 929 N LYS A 116 23.694 32.839 67.019 1.00 79.18 N ANISOU 929 N LYS A 116 6572 16966 6549 1552 -229 -1556 N ATOM 930 CA LYS A 116 22.796 31.698 66.945 1.00 81.94 C ANISOU 930 CA LYS A 116 6860 17369 6906 1478 -238 -1715 C ATOM 931 C LYS A 116 23.296 30.797 65.856 1.00 98.01 C ANISOU 931 C LYS A 116 8801 19523 8916 1415 -253 -1915 C ATOM 932 O LYS A 116 23.962 31.250 64.959 1.00111.05 O ANISOU 932 O LYS A 116 10414 21280 10501 1416 -248 -1883 O ATOM 933 CB LYS A 116 21.364 32.158 66.646 1.00 76.21 C ANISOU 933 CB LYS A 116 6076 16797 6084 1436 -210 -1587 C ATOM 934 CG LYS A 116 20.780 33.150 67.641 1.00 83.99 C ANISOU 934 CG LYS A 116 7132 17699 7082 1500 -192 -1380 C ATOM 935 CD LYS A 116 20.202 34.379 66.943 1.00 90.39 C ANISOU 935 CD LYS A 116 7891 18677 7776 1510 -159 -1163 C ATOM 936 CE LYS A 116 18.823 34.716 67.466 1.00100.53 C ANISOU 936 CE LYS A 116 9145 20029 9025 1511 -142 -1048 C ATOM 937 NZ LYS A 116 18.324 36.002 66.886 1.00115.22 N1+ ANISOU 937 NZ LYS A 116 10952 22045 10783 1540 -110 -821 N1+ ATOM 938 N PRO A 117 23.017 29.511 65.933 1.00 98.91 N ANISOU 938 N PRO A 117 8869 19626 9086 1357 -268 -2129 N ATOM 939 CA PRO A 117 22.168 28.908 66.946 1.00105.41 C ANISOU 939 CA PRO A 117 9719 20349 9981 1344 -272 -2175 C ATOM 940 C PRO A 117 22.840 28.726 68.278 1.00 99.98 C ANISOU 940 C PRO A 117 9137 19350 9502 1419 -282 -2163 C ATOM 941 O PRO A 117 24.036 28.531 68.361 1.00109.11 O ANISOU 941 O PRO A 117 10319 20385 10752 1464 -291 -2225 O ATOM 942 CB PRO A 117 21.804 27.547 66.329 1.00111.87 C ANISOU 942 CB PRO A 117 10425 21272 10808 1241 -276 -2427 C ATOM 943 CG PRO A 117 22.129 27.675 64.872 1.00104.98 C ANISOU 943 CG PRO A 117 9411 20703 9772 1204 -271 -2499 C ATOM 944 CD PRO A 117 23.331 28.558 64.864 1.00 96.65 C ANISOU 944 CD PRO A 117 8456 19508 8758 1286 -278 -2357 C ATOM 945 N TYR A 118 22.027 28.747 69.317 1.00 89.97 N ANISOU 945 N TYR A 118 7916 17936 8334 1422 -272 -2073 N ATOM 946 CA TYR A 118 22.508 28.695 70.665 1.00 96.65 C ANISOU 946 CA TYR A 118 8863 18475 9384 1484 -272 -2018 C ATOM 947 C TYR A 118 22.607 27.251 71.075 1.00125.93 C ANISOU 947 C TYR A 118 12542 22032 13274 1451 -276 -2206 C ATOM 948 O TYR A 118 21.630 26.539 71.091 1.00139.48 O ANISOU 948 O TYR A 118 14195 23789 15013 1379 -272 -2278 O ATOM 949 CB TYR A 118 21.581 29.440 71.612 1.00 71.29 C ANISOU 949 CB TYR A 118 5706 15188 6194 1503 -259 -1826 C ATOM 950 CG TYR A 118 21.669 30.930 71.495 1.00 61.49 C ANISOU 950 CG TYR A 118 4511 14014 4837 1557 -244 -1620 C ATOM 951 CD1 TYR A 118 22.880 31.556 71.248 1.00 63.50 C ANISOU 951 CD1 TYR A 118 4812 14245 5069 1613 -244 -1582 C ATOM 952 CD2 TYR A 118 20.539 31.713 71.635 1.00 61.39 C ANISOU 952 CD2 TYR A 118 4485 14088 4753 1552 -226 -1459 C ATOM 953 CE1 TYR A 118 22.956 32.926 71.139 1.00 62.03 C ANISOU 953 CE1 TYR A 118 4660 14113 4794 1657 -224 -1390 C ATOM 954 CE2 TYR A 118 20.601 33.082 71.533 1.00 58.49 C ANISOU 954 CE2 TYR A 118 4151 13771 4302 1604 -205 -1267 C ATOM 955 CZ TYR A 118 21.809 33.683 71.286 1.00 58.80 C ANISOU 955 CZ TYR A 118 4240 13779 4324 1655 -203 -1233 C ATOM 956 OH TYR A 118 21.861 35.052 71.190 1.00 73.96 O ANISOU 956 OH TYR A 118 6185 15740 6178 1702 -177 -1038 O ATOM 957 N SER A 119 23.804 26.839 71.445 1.00123.09 N ANISOU 957 N SER A 119 12222 21488 13058 1505 -275 -2273 N ATOM 958 CA SER A 119 24.109 25.452 71.710 1.00116.83 C ANISOU 958 CA SER A 119 11392 20545 12452 1489 -264 -2455 C ATOM 959 C SER A 119 23.288 24.980 72.887 1.00109.02 C ANISOU 959 C SER A 119 10431 19381 11612 1474 -256 -2409 C ATOM 960 O SER A 119 23.096 23.792 73.080 1.00114.34 O ANISOU 960 O SER A 119 11054 19962 12430 1438 -239 -2545 O ATOM 961 CB SER A 119 25.606 25.257 71.996 1.00115.25 C ANISOU 961 CB SER A 119 11235 20169 12386 1572 -249 -2493 C ATOM 962 OG SER A 119 26.407 25.567 70.866 1.00110.75 O ANISOU 962 OG SER A 119 10617 19766 11699 1580 -250 -2552 O ATOM 963 N GLU A 120 22.857 25.922 73.706 1.00103.62 N ANISOU 963 N GLU A 120 9826 18640 10906 1505 -261 -2213 N ATOM 964 CA GLU A 120 22.155 25.608 74.939 1.00110.38 C ANISOU 964 CA GLU A 120 10712 19324 11904 1498 -254 -2143 C ATOM 965 C GLU A 120 23.179 24.969 75.849 1.00111.16 C ANISOU 965 C GLU A 120 10867 19160 12209 1560 -241 -2178 C ATOM 966 O GLU A 120 22.867 24.101 76.628 1.00 95.81 O ANISOU 966 O GLU A 120 8912 17064 10429 1548 -227 -2209 O ATOM 967 CB GLU A 120 20.930 24.705 74.679 1.00120.69 C ANISOU 967 CB GLU A 120 11910 20721 13226 1398 -250 -2240 C ATOM 968 CG GLU A 120 19.971 24.515 75.854 1.00136.89 C ANISOU 968 CG GLU A 120 13969 22646 15395 1375 -246 -2142 C ATOM 969 CD GLU A 120 20.164 23.186 76.582 1.00142.30 C ANISOU 969 CD GLU A 120 14633 23119 16317 1366 -227 -2244 C ATOM 970 OE1 GLU A 120 20.701 22.235 75.973 1.00140.49 O ANISOU 970 OE1 GLU A 120 14348 22881 16153 1349 -210 -2425 O ATOM 971 OE2 GLU A 120 19.790 23.095 77.772 1.00143.26 O1+ ANISOU 971 OE2 GLU A 120 14787 23081 16563 1378 -221 -2141 O1+ ATOM 972 N ASP A 121 24.422 25.374 75.665 1.00118.77 N ANISOU 972 N ASP A 121 11878 20087 13161 1626 -240 -2175 N ATOM 973 CA ASP A 121 25.483 25.597 76.603 1.00 94.56 C ANISOU 973 CA ASP A 121 8901 16819 10210 1705 -231 -2105 C ATOM 974 C ASP A 121 25.726 27.090 76.658 1.00 88.63 C ANISOU 974 C ASP A 121 8222 16129 9325 1736 -242 -1941 C ATOM 975 O ASP A 121 26.604 27.536 77.337 1.00 77.24 O ANISOU 975 O ASP A 121 6851 14559 7940 1792 -235 -1870 O ATOM 976 CB ASP A 121 26.745 24.879 76.133 1.00 96.24 C ANISOU 976 CB ASP A 121 9083 16977 10505 1747 -211 -2247 C ATOM 977 CG ASP A 121 27.366 24.039 77.203 1.00118.11 C ANISOU 977 CG ASP A 121 11887 19496 13492 1802 -182 -2265 C ATOM 978 OD1 ASP A 121 26.667 23.729 78.190 1.00117.48 O ANISOU 978 OD1 ASP A 121 11832 19297 13509 1790 -179 -2203 O ATOM 979 OD2 ASP A 121 28.553 23.680 77.046 1.00132.39 O1+ ANISOU 979 OD2 ASP A 121 13692 21234 15374 1861 -156 -2336 O1+ ATOM 980 N TRP A 122 24.982 27.846 75.875 1.00103.16 N ANISOU 980 N TRP A 122 10033 18176 10988 1700 -252 -1886 N ATOM 981 CA TRP A 122 25.170 29.265 75.732 1.00 86.80 C ANISOU 981 CA TRP A 122 8012 16181 8788 1730 -250 -1733 C ATOM 982 C TRP A 122 24.535 30.004 76.860 1.00 61.97 C ANISOU 982 C TRP A 122 4939 12934 5672 1743 -242 -1570 C ATOM 983 O TRP A 122 23.619 29.519 77.454 1.00 70.22 O ANISOU 983 O TRP A 122 5972 13930 6779 1713 -242 -1567 O ATOM 984 CB TRP A 122 24.578 29.718 74.374 1.00 91.80 C ANISOU 984 CB TRP A 122 8571 17090 9218 1690 -256 -1734 C ATOM 985 CG TRP A 122 25.626 29.743 73.355 1.00 76.40 C ANISOU 985 CG TRP A 122 6583 15243 7202 1705 -259 -1815 C ATOM 986 CD1 TRP A 122 26.192 28.673 72.726 1.00 70.33 C ANISOU 986 CD1 TRP A 122 5746 14499 6479 1689 -264 -2005 C ATOM 987 CD2 TRP A 122 26.323 30.891 72.903 1.00 69.91 C ANISOU 987 CD2 TRP A 122 5784 14502 6278 1742 -252 -1707 C ATOM 988 NE1 TRP A 122 27.198 29.095 71.888 1.00 64.38 N ANISOU 988 NE1 TRP A 122 4966 13847 5649 1714 -261 -2023 N ATOM 989 CE2 TRP A 122 27.295 30.458 71.982 1.00 63.39 C ANISOU 989 CE2 TRP A 122 4896 13759 5430 1745 -256 -1837 C ATOM 990 CE3 TRP A 122 26.221 32.251 73.186 1.00 64.72 C ANISOU 990 CE3 TRP A 122 5183 13849 5558 1773 -236 -1513 C ATOM 991 CZ2 TRP A 122 28.162 31.334 71.354 1.00 63.39 C ANISOU 991 CZ2 TRP A 122 4889 13854 5345 1774 -247 -1771 C ATOM 992 CZ3 TRP A 122 27.069 33.118 72.548 1.00 65.86 C ANISOU 992 CZ3 TRP A 122 5322 14080 5622 1801 -226 -1448 C ATOM 993 CH2 TRP A 122 28.034 32.658 71.646 1.00 63.21 C ANISOU 993 CH2 TRP A 122 4924 13833 5262 1800 -233 -1574 C ATOM 994 N PHE A 123 25.019 31.186 77.165 1.00 55.21 N ANISOU 994 N PHE A 123 4149 12049 4779 1785 -232 -1436 N ATOM 995 CA PHE A 123 24.344 31.966 78.142 1.00 58.80 C ANISOU 995 CA PHE A 123 4661 12431 5251 1794 -220 -1288 C ATOM 996 C PHE A 123 23.920 33.170 77.414 1.00 58.26 C ANISOU 996 C PHE A 123 4576 12529 5030 1797 -207 -1169 C ATOM 997 O PHE A 123 24.730 33.819 76.836 1.00 61.43 O ANISOU 997 O PHE A 123 4984 12983 5371 1823 -201 -1140 O ATOM 998 CB PHE A 123 25.229 32.317 79.352 1.00 67.03 C ANISOU 998 CB PHE A 123 5792 13267 6409 1837 -211 -1230 C ATOM 999 CG PHE A 123 24.685 33.469 80.179 1.00 68.09 C ANISOU 999 CG PHE A 123 5982 13359 6531 1851 -195 -1069 C ATOM 1000 CD1 PHE A 123 23.481 33.343 80.861 1.00 71.21 C ANISOU 1000 CD1 PHE A 123 6371 13734 6952 1828 -192 -1020 C ATOM 1001 CD2 PHE A 123 25.368 34.681 80.246 1.00 54.10 C ANISOU 1001 CD2 PHE A 123 4255 11572 4730 1884 -179 -969 C ATOM 1002 CE1 PHE A 123 22.982 34.395 81.595 1.00 67.85 C ANISOU 1002 CE1 PHE A 123 5985 13275 6519 1844 -176 -882 C ATOM 1003 CE2 PHE A 123 24.874 35.731 80.973 1.00 57.23 C ANISOU 1003 CE2 PHE A 123 4691 11927 5128 1897 -160 -834 C ATOM 1004 CZ PHE A 123 23.684 35.591 81.654 1.00 66.20 C ANISOU 1004 CZ PHE A 123 5824 13044 6287 1879 -159 -793 C ATOM 1005 N VAL A 124 22.650 33.489 77.466 1.00 56.94 N ANISOU 1005 N VAL A 124 4381 12445 4810 1775 -200 -1089 N ATOM 1006 CA VAL A 124 22.178 34.745 76.892 1.00 52.26 C ANISOU 1006 CA VAL A 124 3771 11998 4090 1790 -181 -944 C ATOM 1007 C VAL A 124 21.862 35.753 77.990 1.00 48.56 C ANISOU 1007 C VAL A 124 3364 11406 3679 1823 -161 -792 C ATOM 1008 O VAL A 124 21.035 35.478 78.855 1.00 49.31 O ANISOU 1008 O VAL A 124 3464 11431 3841 1808 -163 -774 O ATOM 1009 CB VAL A 124 20.889 34.498 76.065 1.00 70.35 C ANISOU 1009 CB VAL A 124 5962 14502 6267 1744 -183 -950 C ATOM 1010 CG1 VAL A 124 20.574 35.685 75.173 1.00 93.03 C ANISOU 1010 CG1 VAL A 124 8794 17560 8993 1763 -161 -812 C ATOM 1011 CG2 VAL A 124 20.977 33.179 75.267 1.00 65.62 C ANISOU 1011 CG2 VAL A 124 5292 13994 5646 1692 -205 -1141 C ATOM 1012 N SER A 125 22.498 36.917 77.948 1.00 53.96 N ANISOU 1012 N SER A 125 4087 12072 4345 1863 -141 -685 N ATOM 1013 CA SER A 125 22.249 37.975 78.914 1.00 47.71 C ANISOU 1013 CA SER A 125 3345 11171 3612 1894 -120 -548 C ATOM 1014 C SER A 125 20.777 38.361 78.981 1.00 48.32 C ANISOU 1014 C SER A 125 3373 11340 3648 1888 -110 -452 C ATOM 1015 O SER A 125 20.040 38.163 78.046 1.00 58.39 O ANISOU 1015 O SER A 125 4567 12797 4821 1866 -113 -455 O ATOM 1016 CB SER A 125 23.089 39.196 78.574 1.00 47.69 C ANISOU 1016 CB SER A 125 3364 11170 3587 1931 -97 -449 C ATOM 1017 OG SER A 125 22.545 40.337 79.178 1.00 47.57 O ANISOU 1017 OG SER A 125 3364 11107 3605 1958 -73 -305 O ATOM 1018 N ASP A 126 20.332 38.882 80.109 1.00 49.78 N ANISOU 1018 N ASP A 126 3594 11407 3912 1906 -100 -374 N ATOM 1019 CA ASP A 126 18.928 39.257 80.256 1.00 58.20 C ANISOU 1019 CA ASP A 126 4605 12557 4953 1905 -92 -284 C ATOM 1020 C ASP A 126 18.768 40.757 80.479 1.00 60.03 C ANISOU 1020 C ASP A 126 4843 12769 5195 1956 -65 -127 C ATOM 1021 O ASP A 126 17.703 41.218 80.895 1.00 59.66 O ANISOU 1021 O ASP A 126 4759 12748 5160 1970 -58 -44 O ATOM 1022 CB ASP A 126 18.259 38.474 81.405 1.00 77.62 C ANISOU 1022 CB ASP A 126 7076 14918 7500 1880 -106 -332 C ATOM 1023 CG ASP A 126 19.002 38.613 82.748 1.00 99.59 C ANISOU 1023 CG ASP A 126 9954 17485 10401 1900 -102 -337 C ATOM 1024 OD1 ASP A 126 19.608 39.677 82.996 1.00117.78 O1+ ANISOU 1024 OD1 ASP A 126 12303 19722 12727 1938 -85 -263 O1+ ATOM 1025 OD2 ASP A 126 18.979 37.657 83.566 1.00 85.94 O ANISOU 1025 OD2 ASP A 126 8247 15659 8748 1876 -116 -414 O ATOM 1026 N VAL A 127 19.794 41.524 80.127 1.00 49.65 N ANISOU 1026 N VAL A 127 3562 11422 3881 1984 -49 -85 N ATOM 1027 CA VAL A 127 19.750 42.932 80.428 1.00 52.59 C ANISOU 1027 CA VAL A 127 3940 11745 4295 2030 -23 55 C ATOM 1028 C VAL A 127 18.676 43.559 79.580 1.00 62.54 C ANISOU 1028 C VAL A 127 5105 13184 5472 2050 -11 173 C ATOM 1029 O VAL A 127 18.217 44.675 79.819 1.00 65.19 O ANISOU 1029 O VAL A 127 5418 13502 5847 2094 8 300 O ATOM 1030 CB VAL A 127 21.142 43.571 80.164 1.00 48.13 C ANISOU 1030 CB VAL A 127 3418 11111 3759 2048 -8 72 C ATOM 1031 CG1 VAL A 127 21.682 43.102 78.865 1.00 48.64 C ANISOU 1031 CG1 VAL A 127 3446 11319 3716 2031 -14 23 C ATOM 1032 CG2 VAL A 127 21.109 45.091 80.231 1.00 51.05 C ANISOU 1032 CG2 VAL A 127 3773 11448 4177 2095 22 224 C ATOM 1033 N GLY A 128 18.241 42.788 78.595 1.00 70.17 N ANISOU 1033 N GLY A 128 6007 14329 6327 2018 -24 123 N ATOM 1034 CA GLY A 128 17.094 43.138 77.802 1.00 70.70 C ANISOU 1034 CA GLY A 128 5966 14592 6303 2026 -19 217 C ATOM 1035 C GLY A 128 15.821 43.243 78.613 1.00 70.50 C ANISOU 1035 C GLY A 128 5904 14555 6327 2035 -26 264 C ATOM 1036 O GLY A 128 14.820 43.730 78.097 1.00 87.27 O ANISOU 1036 O GLY A 128 7932 16831 8397 2054 -23 364 O ATOM 1037 N MET A 129 15.828 42.831 79.877 1.00 80.91 N ANISOU 1037 N MET A 129 7289 15708 7747 2025 -35 200 N ATOM 1038 CA MET A 129 14.592 42.959 80.640 1.00 79.38 C ANISOU 1038 CA MET A 129 7049 15519 7592 2035 -40 247 C ATOM 1039 C MET A 129 14.674 43.787 81.915 1.00 73.70 C ANISOU 1039 C MET A 129 6389 14622 6990 2079 -27 302 C ATOM 1040 O MET A 129 13.754 43.781 82.731 1.00 68.61 O ANISOU 1040 O MET A 129 5718 13964 6388 2086 -33 320 O ATOM 1041 CB MET A 129 14.052 41.573 80.978 1.00 61.45 C ANISOU 1041 CB MET A 129 4760 13270 5320 1972 -66 127 C ATOM 1042 CG MET A 129 13.263 40.983 79.858 1.00 60.66 C ANISOU 1042 CG MET A 129 4546 13393 5108 1932 -82 108 C ATOM 1043 SD MET A 129 13.858 39.345 79.507 1.00 77.97 S ANISOU 1043 SD MET A 129 6758 15583 7283 1855 -105 -84 S ATOM 1044 CE MET A 129 15.542 39.700 78.974 1.00119.87 C ANISOU 1044 CE MET A 129 12158 20812 12575 1882 -91 -112 C ATOM 1045 N LYS A 130 15.758 44.533 82.066 1.00 60.46 N ANISOU 1045 N LYS A 130 4783 12821 5368 2107 -9 327 N ATOM 1046 CA LYS A 130 15.862 45.441 83.184 1.00 56.27 C ANISOU 1046 CA LYS A 130 4296 12135 4950 2149 4 377 C ATOM 1047 C LYS A 130 15.038 46.651 82.827 1.00 70.21 C ANISOU 1047 C LYS A 130 5978 13979 6719 2210 17 523 C ATOM 1048 O LYS A 130 14.415 46.666 81.801 1.00 72.01 O ANISOU 1048 O LYS A 130 6120 14380 6860 2215 15 579 O ATOM 1049 CB LYS A 130 17.322 45.785 83.466 1.00 52.84 C ANISOU 1049 CB LYS A 130 3952 11546 4580 2150 14 346 C ATOM 1050 CG LYS A 130 18.190 44.651 84.044 1.00 47.84 C ANISOU 1050 CG LYS A 130 3400 10809 3967 2102 -3 205 C ATOM 1051 CD LYS A 130 17.480 43.317 84.421 1.00 50.88 C ANISOU 1051 CD LYS A 130 3775 11229 4328 2058 -26 114 C ATOM 1052 CE LYS A 130 18.547 42.382 85.091 1.00 46.80 C ANISOU 1052 CE LYS A 130 3344 10576 3864 2026 -40 -8 C ATOM 1053 NZ LYS A 130 18.219 40.940 85.377 1.00 50.86 N ANISOU 1053 NZ LYS A 130 3855 11094 4377 1980 -63 -112 N ATOM 1054 N MET A 131 15.009 47.651 83.695 1.00 84.56 N ANISOU 1054 N MET A 131 7812 15674 8643 2258 29 580 N ATOM 1055 CA MET A 131 14.338 48.917 83.400 1.00 89.16 C ANISOU 1055 CA MET A 131 8314 16303 9261 2330 42 721 C ATOM 1056 C MET A 131 15.248 49.762 82.520 1.00 79.31 C ANISOU 1056 C MET A 131 7067 15044 8024 2354 62 797 C ATOM 1057 O MET A 131 16.407 49.409 82.326 1.00 70.09 O ANISOU 1057 O MET A 131 5968 13818 6846 2315 67 732 O ATOM 1058 CB MET A 131 14.045 49.669 84.691 1.00105.77 C ANISOU 1058 CB MET A 131 10431 18267 11488 2375 45 737 C ATOM 1059 CG MET A 131 15.301 50.355 85.252 1.00 98.28 C ANISOU 1059 CG MET A 131 9564 17128 10650 2382 61 718 C ATOM 1060 SD MET A 131 15.259 50.567 87.033 1.00 91.43 S ANISOU 1060 SD MET A 131 8750 16090 9900 2394 56 653 S ATOM 1061 CE MET A 131 14.998 48.879 87.531 1.00 82.07 C ANISOU 1061 CE MET A 131 7608 14948 8626 2320 36 529 C ATOM 1062 N LYS A 132 14.773 50.883 82.041 1.00 79.91 N ANISOU 1062 N LYS A 132 7064 15168 8131 2420 73 934 N ATOM 1063 CA LYS A 132 15.625 51.678 81.213 1.00 79.21 C ANISOU 1063 CA LYS A 132 6969 15069 8059 2441 95 1017 C ATOM 1064 C LYS A 132 16.842 52.152 81.960 1.00 81.92 C ANISOU 1064 C LYS A 132 7398 15203 8525 2435 109 974 C ATOM 1065 O LYS A 132 17.943 52.015 81.483 1.00 87.86 O ANISOU 1065 O LYS A 132 8192 15935 9258 2403 119 948 O ATOM 1066 CB LYS A 132 14.866 52.887 80.632 1.00 80.95 C ANISOU 1066 CB LYS A 132 7081 15363 8315 2524 102 1187 C ATOM 1067 CG LYS A 132 13.781 52.519 79.621 1.00 94.46 C ANISOU 1067 CG LYS A 132 8685 17316 9891 2531 86 1251 C ATOM 1068 CD LYS A 132 13.511 53.647 78.626 1.00115.46 C ANISOU 1068 CD LYS A 132 11242 20070 12558 2604 95 1432 C ATOM 1069 CE LYS A 132 12.775 53.157 77.360 1.00120.07 C ANISOU 1069 CE LYS A 132 11722 20924 12975 2591 81 1488 C ATOM 1070 NZ LYS A 132 13.615 52.278 76.487 1.00107.70 N1+ ANISOU 1070 NZ LYS A 132 10191 19456 11272 2513 90 1416 N1+ ATOM 1071 N LYS A 133 16.705 52.616 83.182 1.00 84.19 N ANISOU 1071 N LYS A 133 7712 15339 8936 2460 106 949 N ATOM 1072 CA LYS A 133 17.864 53.203 83.819 1.00 85.58 C ANISOU 1072 CA LYS A 133 7950 15329 9236 2456 119 917 C ATOM 1073 C LYS A 133 19.000 52.215 83.915 1.00 74.49 C ANISOU 1073 C LYS A 133 6635 13884 7785 2383 115 792 C ATOM 1074 O LYS A 133 20.139 52.602 83.910 1.00 74.64 O ANISOU 1074 O LYS A 133 6685 13806 7868 2371 127 780 O ATOM 1075 CB LYS A 133 17.487 53.724 85.202 1.00 75.53 C ANISOU 1075 CB LYS A 133 6689 13917 8092 2489 113 887 C ATOM 1076 CG LYS A 133 16.211 54.549 85.169 1.00101.09 C ANISOU 1076 CG LYS A 133 9831 17208 11371 2569 110 994 C ATOM 1077 CD LYS A 133 16.473 56.004 85.532 1.00118.55 C ANISOU 1077 CD LYS A 133 12011 19274 13761 2637 122 1061 C ATOM 1078 CE LYS A 133 15.187 56.816 85.457 1.00131.63 C ANISOU 1078 CE LYS A 133 13563 20987 15465 2731 114 1168 C ATOM 1079 NZ LYS A 133 15.349 58.154 86.099 1.00141.96 N1+ ANISOU 1079 NZ LYS A 133 14842 22126 16969 2804 119 1201 N1+ ATOM 1080 N VAL A 134 18.693 50.944 84.059 1.00 64.90 N ANISOU 1080 N VAL A 134 5452 12735 6472 2336 95 696 N ATOM 1081 CA VAL A 134 19.723 49.916 84.063 1.00 75.42 C ANISOU 1081 CA VAL A 134 6858 14038 7758 2275 85 577 C ATOM 1082 C VAL A 134 20.292 49.708 82.661 1.00 81.39 C ANISOU 1082 C VAL A 134 7591 14916 8418 2259 92 600 C ATOM 1083 O VAL A 134 21.512 49.569 82.481 1.00 69.23 O ANISOU 1083 O VAL A 134 6091 13323 6890 2235 96 550 O ATOM 1084 CB VAL A 134 19.147 48.566 84.546 1.00 68.26 C ANISOU 1084 CB VAL A 134 5981 13173 6784 2234 59 471 C ATOM 1085 CG1 VAL A 134 20.234 47.488 84.611 1.00 54.30 C ANISOU 1085 CG1 VAL A 134 4283 11359 4988 2180 45 344 C ATOM 1086 CG2 VAL A 134 18.449 48.728 85.881 1.00 77.80 C ANISOU 1086 CG2 VAL A 134 7199 14294 8067 2251 53 458 C ATOM 1087 N MET A 135 19.391 49.657 81.676 1.00 77.28 N ANISOU 1087 N MET A 135 6994 14570 7797 2274 93 673 N ATOM 1088 CA MET A 135 19.763 49.465 80.276 1.00 66.70 C ANISOU 1088 CA MET A 135 5617 13384 6344 2262 100 703 C ATOM 1089 C MET A 135 20.766 50.494 79.824 1.00 76.66 C ANISOU 1089 C MET A 135 6871 14593 7665 2285 126 786 C ATOM 1090 O MET A 135 21.730 50.162 79.157 1.00 78.74 O ANISOU 1090 O MET A 135 7149 14896 7875 2257 130 749 O ATOM 1091 CB MET A 135 18.507 49.496 79.401 1.00 54.50 C ANISOU 1091 CB MET A 135 3973 12040 4696 2283 97 792 C ATOM 1092 CG MET A 135 18.040 48.107 78.920 1.00 52.62 C ANISOU 1092 CG MET A 135 3719 11951 4323 2231 73 687 C ATOM 1093 SD MET A 135 16.282 48.129 78.496 1.00 95.66 S ANISOU 1093 SD MET A 135 9050 17597 9699 2252 62 772 S ATOM 1094 CE MET A 135 15.971 46.392 78.520 1.00 53.82 C ANISOU 1094 CE MET A 135 3763 12375 4310 2175 31 598 C ATOM 1095 N GLU A 136 20.561 51.740 80.218 1.00 71.14 N ANISOU 1095 N GLU A 136 6143 13801 7087 2336 144 894 N ATOM 1096 CA GLU A 136 21.446 52.801 79.789 1.00 74.85 C ANISOU 1096 CA GLU A 136 6591 14215 7634 2359 171 986 C ATOM 1097 C GLU A 136 22.664 52.953 80.699 1.00 83.69 C ANISOU 1097 C GLU A 136 7780 15139 8879 2335 175 899 C ATOM 1098 O GLU A 136 23.379 53.950 80.593 1.00 92.80 O ANISOU 1098 O GLU A 136 8911 16210 10138 2354 198 969 O ATOM 1099 CB GLU A 136 20.676 54.120 79.727 1.00 76.94 C ANISOU 1099 CB GLU A 136 6778 14465 7990 2432 186 1145 C ATOM 1100 CG GLU A 136 19.504 54.101 78.766 1.00 89.24 C ANISOU 1100 CG GLU A 136 8248 16229 9431 2464 182 1250 C ATOM 1101 CD GLU A 136 18.537 55.253 78.986 1.00115.44 C ANISOU 1101 CD GLU A 136 11491 19517 12855 2546 184 1384 C ATOM 1102 OE1 GLU A 136 18.477 55.791 80.120 1.00126.09 O ANISOU 1102 OE1 GLU A 136 12866 20690 14353 2572 181 1355 O ATOM 1103 OE2 GLU A 136 17.833 55.616 78.018 1.00122.14 O1+ ANISOU 1103 OE2 GLU A 136 12247 20526 13636 2587 186 1515 O1+ ATOM 1104 N SER A 137 22.897 51.963 81.576 1.00 73.22 N ANISOU 1104 N SER A 137 6530 13744 7546 2292 151 751 N ATOM 1105 CA SER A 137 24.025 51.965 82.532 1.00 66.11 C ANISOU 1105 CA SER A 137 5692 12672 6754 2266 149 656 C ATOM 1106 C SER A 137 25.374 52.130 81.856 1.00 77.96 C ANISOU 1106 C SER A 137 7187 14172 8264 2247 165 653 C ATOM 1107 O SER A 137 25.655 51.458 80.871 1.00 94.48 O ANISOU 1107 O SER A 137 9268 16396 10232 2226 162 635 O ATOM 1108 CB SER A 137 24.099 50.699 83.372 1.00 72.36 C ANISOU 1108 CB SER A 137 6558 13428 7508 2224 119 506 C ATOM 1109 OG SER A 137 25.398 50.599 83.970 1.00 84.54 O ANISOU 1109 OG SER A 137 8147 14846 9126 2197 117 419 O ATOM 1110 N THR A 138 26.232 52.970 82.419 1.00 72.56 N ANISOU 1110 N THR A 138 6502 13341 7726 2250 181 658 N ATOM 1111 CA THR A 138 27.477 53.307 81.752 1.00 72.27 C ANISOU 1111 CA THR A 138 6438 13305 7716 2235 203 673 C ATOM 1112 C THR A 138 28.742 52.648 82.304 1.00 74.72 C ANISOU 1112 C THR A 138 6796 13537 8056 2191 192 533 C ATOM 1113 O THR A 138 29.828 53.203 82.165 1.00 79.47 O ANISOU 1113 O THR A 138 7367 14085 8742 2182 214 539 O ATOM 1114 CB THR A 138 27.670 54.833 81.762 1.00 81.26 C ANISOU 1114 CB THR A 138 7514 14348 9013 2271 236 792 C ATOM 1115 OG1 THR A 138 27.848 55.288 83.107 1.00 97.79 O ANISOU 1115 OG1 THR A 138 9633 16260 11264 2272 230 731 O ATOM 1116 CG2 THR A 138 26.453 55.512 81.183 1.00 85.25 C ANISOU 1116 CG2 THR A 138 7962 14934 9496 2325 245 941 C ATOM 1117 N ASN A 139 28.661 51.484 82.922 1.00 67.02 N ANISOU 1117 N ASN A 139 5887 12555 7021 2166 159 409 N ATOM 1118 CA ASN A 139 29.896 51.021 83.539 1.00 82.97 C ANISOU 1118 CA ASN A 139 7941 14489 9094 2134 150 290 C ATOM 1119 C ASN A 139 30.531 49.859 82.774 1.00 83.86 C ANISOU 1119 C ASN A 139 8063 14709 9090 2110 135 205 C ATOM 1120 O ASN A 139 29.855 48.911 82.339 1.00 94.99 O ANISOU 1120 O ASN A 139 9491 16224 10378 2106 113 171 O ATOM 1121 CB ASN A 139 29.684 50.719 85.045 1.00118.50 C ANISOU 1121 CB ASN A 139 12502 18865 13658 2127 126 206 C ATOM 1122 CG ASN A 139 29.283 49.298 85.329 1.00110.99 C ANISOU 1122 CG ASN A 139 11608 17960 12603 2108 92 108 C ATOM 1123 OD1 ASN A 139 30.138 48.442 85.585 1.00 83.64 O ANISOU 1123 OD1 ASN A 139 8174 14476 9128 2086 74 3 O ATOM 1124 ND2 ASN A 139 27.969 49.038 85.337 1.00109.84 N ANISOU 1124 ND2 ASN A 139 11469 17871 12394 2120 82 142 N ATOM 1125 N MET A 140 31.844 49.987 82.588 1.00 73.87 N ANISOU 1125 N MET A 140 6774 13419 7874 2095 149 167 N ATOM 1126 CA MET A 140 32.604 49.116 81.699 1.00 69.70 C ANISOU 1126 CA MET A 140 6229 13000 7254 2080 142 97 C ATOM 1127 C MET A 140 33.463 48.089 82.401 1.00 75.65 C ANISOU 1127 C MET A 140 7024 13695 8026 2061 117 -53 C ATOM 1128 O MET A 140 33.950 48.313 83.500 1.00 98.33 O ANISOU 1128 O MET A 140 9918 16438 11003 2056 114 -93 O ATOM 1129 CB MET A 140 33.523 49.960 80.811 1.00 83.99 C ANISOU 1129 CB MET A 140 7960 14854 9097 2080 182 165 C ATOM 1130 CG MET A 140 32.840 51.089 80.043 1.00 85.49 C ANISOU 1130 CG MET A 140 8095 15103 9283 2104 213 333 C ATOM 1131 SD MET A 140 34.083 52.227 79.422 1.00124.44 S ANISOU 1131 SD MET A 140 12934 20029 14319 2098 267 411 S ATOM 1132 CE MET A 140 33.171 52.935 78.059 1.00137.33 C ANISOU 1132 CE MET A 140 14502 21823 15853 2128 290 599 C ATOM 1133 N VAL A 141 33.696 46.975 81.731 1.00 75.52 N ANISOU 1133 N VAL A 141 7006 13778 7911 2055 97 -136 N ATOM 1134 CA VAL A 141 34.657 46.004 82.217 1.00 82.97 C ANISOU 1134 CA VAL A 141 7969 14677 8879 2045 77 -272 C ATOM 1135 C VAL A 141 35.215 45.202 81.022 1.00 92.82 C ANISOU 1135 C VAL A 141 9170 16061 10036 2044 73 -338 C ATOM 1136 O VAL A 141 34.490 44.476 80.347 1.00 94.74 O ANISOU 1136 O VAL A 141 9415 16408 10175 2044 53 -361 O ATOM 1137 CB VAL A 141 34.101 45.001 83.254 1.00 54.86 C ANISOU 1137 CB VAL A 141 4480 11045 5319 2043 38 -353 C ATOM 1138 CG1 VAL A 141 34.469 45.460 84.644 1.00 85.03 C ANISOU 1138 CG1 VAL A 141 8333 14720 9254 2041 39 -362 C ATOM 1139 CG2 VAL A 141 32.604 44.791 83.093 1.00 52.13 C ANISOU 1139 CG2 VAL A 141 4159 10751 4898 2044 25 -306 C ATOM 1140 N ALA A 142 36.506 45.370 80.751 1.00 86.08 N ANISOU 1140 N ALA A 142 8265 15215 9227 2042 95 -374 N ATOM 1141 CA ALA A 142 37.143 44.784 79.579 1.00 76.74 C ANISOU 1141 CA ALA A 142 7021 14170 7969 2043 101 -433 C ATOM 1142 C ALA A 142 37.541 43.315 79.734 1.00 71.01 C ANISOU 1142 C ALA A 142 6309 13444 7227 2049 68 -589 C ATOM 1143 O ALA A 142 38.394 42.978 80.540 1.00 89.71 O ANISOU 1143 O ALA A 142 8687 15719 9679 2055 65 -663 O ATOM 1144 CB ALA A 142 38.367 45.611 79.201 1.00 86.51 C ANISOU 1144 CB ALA A 142 8180 15422 9267 2038 148 -404 C ATOM 1145 N VAL A 143 36.924 42.455 78.937 1.00 60.86 N ANISOU 1145 N VAL A 143 5017 12269 5839 2050 45 -636 N ATOM 1146 CA VAL A 143 37.265 41.036 78.850 1.00 69.73 C ANISOU 1146 CA VAL A 143 6134 13405 6953 2059 18 -787 C ATOM 1147 C VAL A 143 38.389 40.786 77.836 1.00 65.53 C ANISOU 1147 C VAL A 143 5513 12986 6399 2066 41 -857 C ATOM 1148 O VAL A 143 38.618 41.616 76.954 1.00 74.01 O ANISOU 1148 O VAL A 143 6529 14168 7425 2058 74 -783 O ATOM 1149 CB VAL A 143 36.009 40.224 78.417 1.00 64.79 C ANISOU 1149 CB VAL A 143 5529 12852 6238 2051 -16 -816 C ATOM 1150 CG1 VAL A 143 36.221 38.716 78.501 1.00 61.43 C ANISOU 1150 CG1 VAL A 143 5100 12406 5836 2060 -44 -972 C ATOM 1151 CG2 VAL A 143 34.795 40.660 79.223 1.00 59.19 C ANISOU 1151 CG2 VAL A 143 4889 12067 5535 2042 -27 -725 C ATOM 1152 N ASP A 144 39.086 39.659 77.959 1.00 61.05 N ANISOU 1152 N ASP A 144 4928 12396 5873 2084 31 -996 N ATOM 1153 CA ASP A 144 39.889 39.149 76.860 1.00 66.42 C ANISOU 1153 CA ASP A 144 5517 13205 6514 2094 51 -1088 C ATOM 1154 C ASP A 144 40.189 37.675 77.054 1.00 69.74 C ANISOU 1154 C ASP A 144 5931 13584 6981 2121 31 -1244 C ATOM 1155 O ASP A 144 40.305 37.217 78.181 1.00 86.70 O ANISOU 1155 O ASP A 144 8134 15589 9221 2138 14 -1274 O ATOM 1156 CB ASP A 144 41.178 39.920 76.660 1.00 73.00 C ANISOU 1156 CB ASP A 144 6281 14063 7391 2097 103 -1065 C ATOM 1157 CG ASP A 144 41.748 39.687 75.267 1.00103.03 C ANISOU 1157 CG ASP A 144 9979 18047 11120 2097 136 -1124 C ATOM 1158 OD1 ASP A 144 42.583 38.761 75.115 1.00102.82 O ANISOU 1158 OD1 ASP A 144 9903 18034 11130 2123 148 -1258 O ATOM 1159 OD2 ASP A 144 41.308 40.384 74.308 1.00129.68 O ANISOU 1159 OD2 ASP A 144 13318 21558 14397 2075 150 -1036 O ATOM 1160 N CYS A 145 40.343 36.923 75.970 1.00 64.77 N ANISOU 1160 N CYS A 145 5231 13081 6297 2127 38 -1345 N ATOM 1161 CA CYS A 145 40.736 35.524 76.125 1.00 65.62 C ANISOU 1161 CA CYS A 145 5319 13138 6475 2160 31 -1499 C ATOM 1162 C CYS A 145 41.976 35.116 75.376 1.00 73.20 C ANISOU 1162 C CYS A 145 6178 14183 7453 2189 78 -1606 C ATOM 1163 O CYS A 145 42.432 35.801 74.474 1.00 69.30 O ANISOU 1163 O CYS A 145 5614 13824 6891 2174 115 -1577 O ATOM 1164 CB CYS A 145 39.602 34.585 75.732 1.00 64.07 C ANISOU 1164 CB CYS A 145 5135 12977 6232 2147 -5 -1565 C ATOM 1165 SG CYS A 145 38.111 34.861 76.660 1.00 73.50 S ANISOU 1165 SG CYS A 145 6438 14073 7414 2117 -51 -1459 S ATOM 1166 N GLU A 146 42.508 33.976 75.797 1.00 84.05 N ANISOU 1166 N GLU A 146 7541 15470 8926 2235 83 -1727 N ATOM 1167 CA AGLU A 146 43.475 33.209 75.034 0.63 86.64 C ANISOU 1167 CA AGLU A 146 7769 15873 9277 2274 132 -1864 C ATOM 1168 CA BGLU A 146 43.575 33.209 75.034 0.37 89.59 C ANISOU 1168 CA BGLU A 146 8138 16247 9656 2277 136 -1868 C ATOM 1169 C GLU A 146 42.887 31.843 74.793 1.00 83.47 C ANISOU 1169 C GLU A 146 7364 15448 8904 2293 118 -1990 C ATOM 1170 O GLU A 146 42.494 31.128 75.739 1.00 74.29 O ANISOU 1170 O GLU A 146 6264 14133 7832 2314 89 -2005 O ATOM 1171 CB AGLU A 146 44.811 33.109 75.785 0.63 96.35 C ANISOU 1171 CB AGLU A 146 8975 17014 10620 2328 168 -1894 C ATOM 1172 CB BGLU A 146 44.878 33.072 75.811 0.37 99.02 C ANISOU 1172 CB BGLU A 146 9310 17348 10964 2332 170 -1899 C ATOM 1173 CG AGLU A 146 45.603 34.417 75.823 0.63101.86 C ANISOU 1173 CG AGLU A 146 9643 17760 11300 2308 199 -1799 C ATOM 1174 CG BGLU A 146 45.554 34.411 76.097 0.37101.24 C ANISOU 1174 CG BGLU A 146 9582 17647 11237 2310 191 -1789 C ATOM 1175 CD AGLU A 146 46.590 34.497 76.978 0.63100.57 C ANISOU 1175 CD AGLU A 146 9487 17479 11247 2347 209 -1794 C ATOM 1176 CD BGLU A 146 45.985 35.139 74.821 0.37108.06 C ANISOU 1176 CD BGLU A 146 10352 18695 12009 2281 243 -1775 C ATOM 1177 OE1AGLU A 146 47.654 33.848 76.926 0.63101.43 O ANISOU 1177 OE1AGLU A 146 9523 17597 11419 2405 251 -1895 O ATOM 1178 OE1BGLU A 146 46.508 34.478 73.898 0.37112.98 O ANISOU 1178 OE1BGLU A 146 10886 19426 12614 2305 289 -1891 O ATOM 1179 OE2AGLU A 146 46.299 35.229 77.939 0.63101.95 O ANISOU 1179 OE2AGLU A 146 9734 17560 11443 2323 179 -1691 O ATOM 1180 OE2BGLU A 146 45.803 36.374 74.743 0.37103.62 O ANISOU 1180 OE2BGLU A 146 9801 18171 11399 2236 247 -1646 O ATOM 1181 N MET A 147 42.849 31.468 73.526 1.00 91.47 N ANISOU 1181 N MET A 147 8295 16614 9845 2283 146 -2083 N ATOM 1182 CA MET A 147 42.256 30.228 73.081 1.00 85.67 C ANISOU 1182 CA MET A 147 7539 15883 9128 2290 143 -2217 C ATOM 1183 C MET A 147 43.275 29.410 72.346 1.00 80.88 C ANISOU 1183 C MET A 147 6833 15332 8565 2342 220 -2376 C ATOM 1184 O MET A 147 44.227 29.924 71.811 1.00 76.81 O ANISOU 1184 O MET A 147 6250 14919 8014 2353 272 -2378 O ATOM 1185 CB MET A 147 41.074 30.553 72.144 1.00 81.48 C ANISOU 1185 CB MET A 147 6997 15512 8449 2220 108 -2192 C ATOM 1186 CG MET A 147 39.976 31.379 72.802 1.00 89.43 C ANISOU 1186 CG MET A 147 8100 16476 9403 2176 44 -2034 C ATOM 1187 SD MET A 147 39.425 32.852 71.915 1.00116.56 S ANISOU 1187 SD MET A 147 11521 20115 12653 2118 31 -1883 S ATOM 1188 CE MET A 147 40.748 34.002 72.191 1.00 69.90 C ANISOU 1188 CE MET A 147 5599 14185 6775 2139 79 -1783 C ATOM 1189 N VAL A 148 43.062 28.116 72.349 1.00 78.43 N ANISOU 1189 N VAL A 148 6515 14946 8341 2378 237 -2508 N ATOM 1190 CA VAL A 148 43.878 27.234 71.579 1.00 92.29 C ANISOU 1190 CA VAL A 148 8180 16749 10136 2433 324 -2675 C ATOM 1191 C VAL A 148 42.981 26.367 70.736 1.00102.61 C ANISOU 1191 C VAL A 148 9457 18120 11409 2402 333 -2803 C ATOM 1192 O VAL A 148 41.952 25.923 71.192 1.00 94.62 O ANISOU 1192 O VAL A 148 8502 17019 10431 2377 283 -2795 O ATOM 1193 CB VAL A 148 44.788 26.394 72.499 1.00 90.89 C ANISOU 1193 CB VAL A 148 8014 16386 10132 2534 366 -2730 C ATOM 1194 CG1 VAL A 148 45.650 27.318 73.359 1.00 83.14 C ANISOU 1194 CG1 VAL A 148 7055 15361 9173 2553 352 -2606 C ATOM 1195 CG2 VAL A 148 43.973 25.467 73.365 1.00 85.50 C ANISOU 1195 CG2 VAL A 148 7405 15518 9561 2552 331 -2742 C ATOM 1196 N LEU A 149 43.382 26.110 69.506 1.00115.98 N ANISOU 1196 N LEU A 149 11058 19975 13034 2401 406 -2929 N ATOM 1197 CA LEU A 149 42.580 25.281 68.642 1.00126.75 C ANISOU 1197 CA LEU A 149 12387 21416 14359 2365 427 -3070 C ATOM 1198 C LEU A 149 42.481 23.875 69.202 1.00120.69 C ANISOU 1198 C LEU A 149 11652 20444 13762 2431 468 -3194 C ATOM 1199 O LEU A 149 43.476 23.238 69.493 1.00109.19 O ANISOU 1199 O LEU A 149 10187 18874 12425 2528 545 -3269 O ATOM 1200 CB LEU A 149 43.185 25.265 67.233 1.00127.91 C ANISOU 1200 CB LEU A 149 12428 21776 14398 2357 520 -3192 C ATOM 1201 CG LEU A 149 42.392 24.617 66.101 1.00124.98 C ANISOU 1201 CG LEU A 149 12005 21548 13935 2298 551 -3342 C ATOM 1202 CD1 LEU A 149 42.729 25.296 64.781 1.00135.23 C ANISOU 1202 CD1 LEU A 149 13209 23122 15051 2247 598 -3359 C ATOM 1203 CD2 LEU A 149 42.704 23.141 66.029 1.00115.71 C ANISOU 1203 CD2 LEU A 149 10828 20243 12892 2371 657 -3552 C ATOM 1204 N CYS A 150 41.260 23.380 69.280 1.00114.10 N ANISOU 1204 N CYS A 150 10848 19572 12933 2380 424 -3220 N ATOM 1205 CA CYS A 150 40.969 22.086 69.862 1.00115.36 C ANISOU 1205 CA CYS A 150 11047 19526 13257 2431 461 -3319 C ATOM 1206 C CYS A 150 40.880 20.975 68.849 1.00142.34 C ANISOU 1206 C CYS A 150 14415 22986 16683 2438 566 -3542 C ATOM 1207 O CYS A 150 40.850 21.215 67.657 1.00153.34 O ANISOU 1207 O CYS A 150 15740 24591 17933 2385 597 -3622 O ATOM 1208 CB CYS A 150 39.651 22.096 70.647 1.00107.49 C ANISOU 1208 CB CYS A 150 10117 18442 12283 2369 366 -3225 C ATOM 1209 SG CYS A 150 39.700 22.017 72.446 1.00150.31 S ANISOU 1209 SG CYS A 150 15644 23595 17872 2428 320 -3077 S ATOM 1210 N GLU A 151 40.786 19.750 69.331 1.00150.90 N ANISOU 1210 N GLU A 151 15541 23864 17929 2503 629 -3643 N ATOM 1211 CA GLU A 151 40.843 18.595 68.457 1.00161.32 C ANISOU 1211 CA GLU A 151 16842 25178 19275 2531 759 -3874 C ATOM 1212 C GLU A 151 39.716 18.743 67.465 1.00156.28 C ANISOU 1212 C GLU A 151 16159 24743 18477 2398 729 -3943 C ATOM 1213 O GLU A 151 39.829 18.381 66.310 1.00159.56 O ANISOU 1213 O GLU A 151 16530 25294 18800 2374 819 -4113 O ATOM 1214 CB GLU A 151 40.729 17.302 69.271 1.00166.46 C ANISOU 1214 CB GLU A 151 17569 25547 20130 2619 826 -3946 C ATOM 1215 CG GLU A 151 40.640 16.033 68.451 1.00170.92 C ANISOU 1215 CG GLU A 151 18152 26063 20725 2648 973 -4195 C ATOM 1216 CD GLU A 151 39.215 15.691 68.055 1.00173.13 C ANISOU 1216 CD GLU A 151 18439 26395 20946 2524 951 -4273 C ATOM 1217 OE1 GLU A 151 38.280 16.342 68.567 1.00165.69 O ANISOU 1217 OE1 GLU A 151 17486 25499 19971 2434 819 -4121 O ATOM 1218 OE2 GLU A 151 39.029 14.775 67.227 1.00183.05 O ANISOU 1218 OE2 GLU A 151 19720 27650 22181 2516 1070 -4493 O ATOM 1219 N ASP A 152 38.603 19.236 67.972 1.00148.75 N ANISOU 1219 N ASP A 152 15223 23805 17491 2312 607 -3812 N ATOM 1220 CA ASP A 152 37.355 19.342 67.246 1.00131.07 C ANISOU 1220 CA ASP A 152 12940 21745 15115 2184 560 -3856 C ATOM 1221 C ASP A 152 37.471 20.296 66.090 1.00116.65 C ANISOU 1221 C ASP A 152 11033 20219 13072 2114 536 -3839 C ATOM 1222 O ASP A 152 36.634 20.316 65.212 1.00106.62 O ANISOU 1222 O ASP A 152 9707 19142 11662 2013 522 -3909 O ATOM 1223 CB ASP A 152 36.261 19.797 68.204 1.00135.23 C ANISOU 1223 CB ASP A 152 13508 22216 15658 2126 431 -3687 C ATOM 1224 CG ASP A 152 34.899 19.333 67.785 1.00135.42 C ANISOU 1224 CG ASP A 152 13500 22325 15626 2018 412 -3777 C ATOM 1225 OD1 ASP A 152 34.791 18.781 66.667 1.00140.31 O ANISOU 1225 OD1 ASP A 152 14067 23075 16169 1973 491 -3966 O ATOM 1226 OD2 ASP A 152 33.941 19.526 68.570 1.00118.18 O ANISOU 1226 OD2 ASP A 152 11348 20085 13468 1973 324 -3664 O ATOM 1227 N GLY A 153 38.489 21.131 66.133 1.00120.79 N ANISOU 1227 N GLY A 153 11547 20785 13563 2165 530 -3734 N ATOM 1228 CA GLY A 153 38.664 22.149 65.130 1.00126.17 C ANISOU 1228 CA GLY A 153 12155 21740 14044 2107 510 -3684 C ATOM 1229 C GLY A 153 37.872 23.305 65.634 1.00124.93 C ANISOU 1229 C GLY A 153 12025 21642 13800 2047 368 -3463 C ATOM 1230 O GLY A 153 37.834 24.362 65.038 1.00116.38 O ANISOU 1230 O GLY A 153 10902 20766 12553 1999 325 -3358 O ATOM 1231 N THR A 154 37.256 23.077 66.784 1.00127.16 N ANISOU 1231 N THR A 154 12387 21729 14201 2057 306 -3389 N ATOM 1232 CA THR A 154 36.568 24.101 67.508 1.00118.12 C ANISOU 1232 CA THR A 154 11301 20582 12999 2021 190 -3179 C ATOM 1233 C THR A 154 37.608 24.659 68.410 1.00117.69 C ANISOU 1233 C THR A 154 11308 20379 13029 2101 193 -3055 C ATOM 1234 O THR A 154 38.329 23.927 69.064 1.00116.03 O ANISOU 1234 O THR A 154 11127 19974 12985 2181 247 -3111 O ATOM 1235 CB THR A 154 35.396 23.586 68.369 1.00103.11 C ANISOU 1235 CB THR A 154 9457 18541 11180 1990 135 -3159 C ATOM 1236 OG1 THR A 154 35.896 22.630 69.311 1.00117.34 O ANISOU 1236 OG1 THR A 154 11311 20076 13197 2072 189 -3213 O ATOM 1237 CG2 THR A 154 34.322 22.941 67.540 1.00100.10 C ANISOU 1237 CG2 THR A 154 9007 18302 10726 1902 136 -3298 C ATOM 1238 N GLU A 155 37.691 25.969 68.425 1.00109.35 N ANISOU 1238 N GLU A 155 10271 19421 11855 2080 141 -2885 N ATOM 1239 CA GLU A 155 38.576 26.662 69.325 1.00107.72 C ANISOU 1239 CA GLU A 155 10127 19088 11715 2137 139 -2754 C ATOM 1240 C GLU A 155 38.081 26.547 70.740 1.00 99.68 C ANISOU 1240 C GLU A 155 9213 17849 10811 2154 89 -2661 C ATOM 1241 O GLU A 155 36.892 26.439 70.970 1.00 88.82 O ANISOU 1241 O GLU A 155 7871 16466 9410 2104 36 -2633 O ATOM 1242 CB GLU A 155 38.704 28.140 68.935 1.00103.08 C ANISOU 1242 CB GLU A 155 9534 18660 10971 2104 110 -2594 C ATOM 1243 CG GLU A 155 39.901 28.459 68.067 1.00114.15 C ANISOU 1243 CG GLU A 155 10851 20196 12326 2126 184 -2636 C ATOM 1244 CD GLU A 155 40.105 29.953 67.891 1.00116.46 C ANISOU 1244 CD GLU A 155 11148 20602 12499 2101 165 -2455 C ATOM 1245 OE1 GLU A 155 39.344 30.738 68.508 1.00101.14 O ANISOU 1245 OE1 GLU A 155 9288 18618 10522 2076 99 -2297 O ATOM 1246 OE2 GLU A 155 41.028 30.340 67.133 1.00120.39 O ANISOU 1246 OE2 GLU A 155 11568 21229 12945 2108 229 -2471 O ATOM 1247 N GLY A 156 39.050 26.655 71.648 1.00 92.25 N ANISOU 1247 N GLY A 156 8316 16752 9983 2220 110 -2610 N ATOM 1248 CA GLY A 156 38.818 26.533 73.064 1.00101.12 C ANISOU 1248 CA GLY A 156 9534 17664 11224 2245 77 -2524 C ATOM 1249 C GLY A 156 39.543 27.477 74.031 1.00115.14 C ANISOU 1249 C GLY A 156 11371 19353 13023 2273 64 -2378 C ATOM 1250 O GLY A 156 40.592 28.126 73.750 1.00114.88 O ANISOU 1250 O GLY A 156 11303 19386 12960 2296 96 -2355 O ATOM 1251 N LEU A 157 38.918 27.527 75.198 1.00106.47 N ANISOU 1251 N LEU A 157 10361 18109 11982 2265 21 -2285 N ATOM 1252 CA LEU A 157 39.278 28.426 76.250 1.00 86.08 C ANISOU 1252 CA LEU A 157 7850 15439 9416 2275 2 -2144 C ATOM 1253 C LEU A 157 40.182 27.747 77.222 1.00 86.97 C ANISOU 1253 C LEU A 157 7977 15385 9684 2349 30 -2174 C ATOM 1254 O LEU A 157 39.815 26.717 77.883 1.00 96.56 O ANISOU 1254 O LEU A 157 9216 16460 11014 2376 31 -2214 O ATOM 1255 CB LEU A 157 38.031 28.937 76.950 1.00 85.08 C ANISOU 1255 CB LEU A 157 7809 15268 9248 2222 -51 -2024 C ATOM 1256 CG LEU A 157 38.237 30.083 77.936 1.00 79.01 C ANISOU 1256 CG LEU A 157 7116 14434 8470 2217 -65 -1872 C ATOM 1257 CD1 LEU A 157 38.983 31.283 77.276 1.00 64.73 C ANISOU 1257 CD1 LEU A 157 5274 12753 6569 2209 -46 -1813 C ATOM 1258 CD2 LEU A 157 36.862 30.466 78.511 1.00 66.18 C ANISOU 1258 CD2 LEU A 157 5567 12777 6803 2168 -104 -1771 C ATOM 1259 N VAL A 158 41.365 28.365 77.247 1.00 91.37 N ANISOU 1259 N VAL A 158 8509 15972 10238 2380 57 -2150 N ATOM 1260 CA VAL A 158 42.431 28.204 78.204 1.00 92.25 C ANISOU 1260 CA VAL A 158 8627 15965 10458 2447 79 -2139 C ATOM 1261 C VAL A 158 42.770 29.366 79.149 1.00 89.17 C ANISOU 1261 C VAL A 158 8292 15538 10049 2430 55 -2004 C ATOM 1262 O VAL A 158 43.123 29.090 80.229 1.00 80.12 O ANISOU 1262 O VAL A 158 7180 14270 8993 2469 51 -1981 O ATOM 1263 CB VAL A 158 43.758 27.747 77.513 1.00 73.04 C ANISOU 1263 CB VAL A 158 6096 13591 8066 2516 148 -2256 C ATOM 1264 CG1 VAL A 158 43.527 26.404 76.798 1.00 71.00 C ANISOU 1264 CG1 VAL A 158 5789 13325 7864 2552 189 -2408 C ATOM 1265 CG2 VAL A 158 44.327 28.829 76.600 1.00 73.45 C ANISOU 1265 CG2 VAL A 158 6090 13815 8002 2482 169 -2232 C ATOM 1266 N ARG A 159 42.780 30.630 78.746 1.00 94.24 N ANISOU 1266 N ARG A 159 8935 16286 10587 2380 49 -1922 N ATOM 1267 CA ARG A 159 43.034 31.727 79.710 1.00 76.27 C ANISOU 1267 CA ARG A 159 6712 13957 8310 2362 34 -1800 C ATOM 1268 C ARG A 159 42.151 32.932 79.546 1.00 76.16 C ANISOU 1268 C ARG A 159 6747 13998 8193 2293 11 -1679 C ATOM 1269 O ARG A 159 42.139 33.528 78.516 1.00100.81 O ANISOU 1269 O ARG A 159 9825 17253 11227 2265 26 -1664 O ATOM 1270 CB ARG A 159 44.478 32.182 79.672 1.00 79.89 C ANISOU 1270 CB ARG A 159 7104 14455 8796 2396 76 -1815 C ATOM 1271 CG ARG A 159 44.913 32.805 80.981 1.00 84.21 C ANISOU 1271 CG ARG A 159 7698 14903 9395 2401 63 -1735 C ATOM 1272 CD ARG A 159 45.936 33.887 80.759 1.00 93.38 C ANISOU 1272 CD ARG A 159 8801 16141 10537 2391 98 -1702 C ATOM 1273 NE ARG A 159 46.401 34.495 81.998 1.00114.32 N ANISOU 1273 NE ARG A 159 11486 18709 13242 2394 88 -1640 N ATOM 1274 CZ ARG A 159 47.024 35.669 82.061 1.00111.22 C ANISOU 1274 CZ ARG A 159 11063 18355 12841 2367 110 -1583 C ATOM 1275 NH1 ARG A 159 47.419 36.157 83.234 1.00107.62 N ANISOU 1275 NH1 ARG A 159 10632 17821 12437 2369 98 -1542 N ATOM 1276 NH2 ARG A 159 47.243 36.364 80.953 1.00102.39 N ANISOU 1276 NH2 ARG A 159 9882 17357 11666 2336 147 -1567 N ATOM 1277 N VAL A 160 41.463 33.318 80.599 1.00 66.51 N ANISOU 1277 N VAL A 160 5611 12675 6984 2270 -20 -1589 N ATOM 1278 CA VAL A 160 40.499 34.422 80.536 1.00 66.78 C ANISOU 1278 CA VAL A 160 5696 12746 6932 2215 -37 -1470 C ATOM 1279 C VAL A 160 40.912 35.563 81.488 1.00 67.18 C ANISOU 1279 C VAL A 160 5785 12729 7011 2205 -30 -1370 C ATOM 1280 O VAL A 160 41.191 35.338 82.625 1.00 68.02 O ANISOU 1280 O VAL A 160 5927 12724 7192 2225 -39 -1370 O ATOM 1281 CB VAL A 160 39.045 34.057 80.876 1.00 62.10 C ANISOU 1281 CB VAL A 160 5170 12109 6317 2187 -72 -1440 C ATOM 1282 CG1 VAL A 160 38.969 33.142 82.072 1.00 68.15 C ANISOU 1282 CG1 VAL A 160 5979 12727 7187 2214 -87 -1471 C ATOM 1283 CG2 VAL A 160 38.235 35.350 81.097 1.00 50.72 C ANISOU 1283 CG2 VAL A 160 3782 10681 4808 2145 -78 -1302 C ATOM 1284 N GLY A 161 40.850 36.813 81.067 1.00 60.84 N ANISOU 1284 N GLY A 161 4973 11991 6151 2174 -13 -1278 N ATOM 1285 CA GLY A 161 41.058 37.906 82.010 1.00 53.56 C ANISOU 1285 CA GLY A 161 4088 10992 5270 2160 -5 -1186 C ATOM 1286 C GLY A 161 40.014 38.991 81.920 1.00 61.81 C ANISOU 1286 C GLY A 161 5175 12050 6259 2122 -6 -1062 C ATOM 1287 O GLY A 161 39.704 39.306 80.841 1.00 78.11 O ANISOU 1287 O GLY A 161 7204 14225 8248 2109 6 -1033 O ATOM 1288 N VAL A 162 39.513 39.517 83.012 1.00 65.42 N ANISOU 1288 N VAL A 162 5698 12406 6753 2111 -17 -995 N ATOM 1289 CA VAL A 162 38.535 40.554 82.961 1.00 58.99 C ANISOU 1289 CA VAL A 162 4915 11598 5901 2084 -11 -878 C ATOM 1290 C VAL A 162 39.154 41.662 83.734 1.00 66.40 C ANISOU 1290 C VAL A 162 5852 12461 6917 2078 11 -821 C ATOM 1291 O VAL A 162 39.880 41.395 84.634 1.00 76.57 O ANISOU 1291 O VAL A 162 7146 13675 8272 2091 4 -873 O ATOM 1292 CB VAL A 162 37.227 40.098 83.617 1.00 45.38 C ANISOU 1292 CB VAL A 162 3263 9819 4159 2076 -41 -860 C ATOM 1293 CG1 VAL A 162 36.098 41.098 83.293 1.00 58.00 C ANISOU 1293 CG1 VAL A 162 4877 11456 5703 2057 -31 -741 C ATOM 1294 CG2 VAL A 162 36.856 38.690 83.149 1.00 50.82 C ANISOU 1294 CG2 VAL A 162 3947 10549 4814 2085 -66 -955 C ATOM 1295 N VAL A 163 38.921 42.898 83.353 1.00 70.03 N ANISOU 1295 N VAL A 163 6291 12943 7372 2062 38 -718 N ATOM 1296 CA VAL A 163 39.544 44.008 84.034 1.00 62.74 C ANISOU 1296 CA VAL A 163 5351 11944 6542 2054 63 -671 C ATOM 1297 C VAL A 163 38.593 45.161 84.195 1.00 76.57 C ANISOU 1297 C VAL A 163 7125 13658 8308 2041 76 -549 C ATOM 1298 O VAL A 163 37.880 45.491 83.293 1.00 91.21 O ANISOU 1298 O VAL A 163 8967 15590 10100 2039 87 -476 O ATOM 1299 CB VAL A 163 40.799 44.449 83.258 1.00 56.77 C ANISOU 1299 CB VAL A 163 4502 11254 5814 2052 104 -682 C ATOM 1300 CG1 VAL A 163 41.129 45.908 83.502 1.00 52.83 C ANISOU 1300 CG1 VAL A 163 3965 10702 5405 2034 142 -595 C ATOM 1301 CG2 VAL A 163 41.990 43.524 83.584 1.00 49.44 C ANISOU 1301 CG2 VAL A 163 3545 10322 4918 2072 97 -807 C ATOM 1302 N ASP A 164 38.630 45.810 85.339 1.00 81.74 N ANISOU 1302 N ASP A 164 7804 14201 9050 2036 76 -529 N ATOM 1303 CA ASP A 164 37.715 46.894 85.614 1.00 85.58 C ANISOU 1303 CA ASP A 164 8307 14639 9572 2031 88 -423 C ATOM 1304 C ASP A 164 38.139 48.225 85.080 1.00 77.49 C ANISOU 1304 C ASP A 164 7210 13613 8620 2024 134 -337 C ATOM 1305 O ASP A 164 39.200 48.383 84.542 1.00 64.69 O ANISOU 1305 O ASP A 164 5523 12031 7026 2017 160 -357 O ATOM 1306 CB ASP A 164 37.463 47.034 87.120 1.00 94.49 C ANISOU 1306 CB ASP A 164 9486 15648 10766 2030 68 -444 C ATOM 1307 CG ASP A 164 38.562 47.802 87.841 1.00114.24 C ANISOU 1307 CG ASP A 164 11945 18073 13385 2023 85 -468 C ATOM 1308 OD1 ASP A 164 39.694 47.880 87.314 1.00110.31 O1+ ANISOU 1308 OD1 ASP A 164 11384 17613 12916 2018 107 -498 O1+ ATOM 1309 OD2 ASP A 164 38.289 48.321 88.950 1.00123.93 O ANISOU 1309 OD2 ASP A 164 13197 19212 14679 2022 76 -462 O ATOM 1310 N ARG A 165 37.276 49.188 85.286 1.00 73.05 N ANISOU 1310 N ARG A 165 6654 13001 8100 2027 145 -240 N ATOM 1311 CA ARG A 165 37.389 50.500 84.725 1.00 70.05 C ANISOU 1311 CA ARG A 165 6203 12613 7798 2026 190 -134 C ATOM 1312 C ARG A 165 38.636 51.167 85.211 1.00 86.67 C ANISOU 1312 C ARG A 165 8249 14641 10041 2010 217 -169 C ATOM 1313 O ARG A 165 39.096 52.119 84.631 1.00100.51 O ANISOU 1313 O ARG A 165 9922 16395 11870 2003 261 -102 O ATOM 1314 CB ARG A 165 36.133 51.312 85.101 1.00 69.72 C ANISOU 1314 CB ARG A 165 6185 12513 7794 2042 190 -37 C ATOM 1315 CG ARG A 165 36.170 52.816 84.830 1.00 80.03 C ANISOU 1315 CG ARG A 165 7416 13765 9227 2048 234 75 C ATOM 1316 CD ARG A 165 34.752 53.394 84.698 1.00 97.16 C ANISOU 1316 CD ARG A 165 9598 15935 11385 2078 233 187 C ATOM 1317 NE ARG A 165 34.742 54.695 84.018 1.00110.73 N ANISOU 1317 NE ARG A 165 11233 17641 13197 2093 276 315 N ATOM 1318 CZ ARG A 165 33.645 55.346 83.623 1.00113.28 C ANISOU 1318 CZ ARG A 165 11541 17984 13516 2128 284 438 C ATOM 1319 NH1 ARG A 165 33.753 56.522 83.013 1.00 94.79 N1+ ANISOU 1319 NH1 ARG A 165 9117 15626 11273 2146 324 556 N1+ ATOM 1320 NH2 ARG A 165 32.439 54.830 83.836 1.00123.18 N ANISOU 1320 NH2 ARG A 165 12852 19276 14673 2147 254 445 N ATOM 1321 N ASP A 166 39.144 50.707 86.331 1.00 92.73 N ANISOU 1321 N ASP A 166 9048 15341 10844 2004 191 -269 N ATOM 1322 CA ASP A 166 40.332 51.307 86.938 1.00 91.35 C ANISOU 1322 CA ASP A 166 8812 15097 10799 1989 213 -315 C ATOM 1323 C ASP A 166 41.538 50.383 86.775 1.00 86.26 C ANISOU 1323 C ASP A 166 8143 14519 10114 1985 209 -419 C ATOM 1324 O ASP A 166 42.539 50.520 87.476 1.00 79.34 O ANISOU 1324 O ASP A 166 7228 13601 9317 1977 214 -487 O ATOM 1325 CB ASP A 166 40.090 51.598 88.422 1.00110.65 C ANISOU 1325 CB ASP A 166 11296 17425 13320 1990 187 -351 C ATOM 1326 CG ASP A 166 38.658 52.072 88.712 1.00134.57 C ANISOU 1326 CG ASP A 166 14374 20405 16350 2004 176 -273 C ATOM 1327 OD1 ASP A 166 38.066 52.772 87.855 1.00142.21 O ANISOU 1327 OD1 ASP A 166 15310 21391 17330 2012 204 -168 O ATOM 1328 OD2 ASP A 166 38.124 51.741 89.803 1.00130.74 O1+ ANISOU 1328 OD2 ASP A 166 13953 19873 15850 2011 141 -314 O1+ ATOM 1329 N LEU A 167 41.411 49.436 85.849 1.00 90.04 N ANISOU 1329 N LEU A 167 8636 15106 10469 1995 199 -436 N ATOM 1330 CA LEU A 167 42.463 48.474 85.510 1.00 80.16 C ANISOU 1330 CA LEU A 167 7353 13931 9174 2001 197 -536 C ATOM 1331 C LEU A 167 42.791 47.493 86.642 1.00 79.79 C ANISOU 1331 C LEU A 167 7357 13840 9118 2016 152 -644 C ATOM 1332 O LEU A 167 43.746 46.725 86.548 1.00 84.35 O ANISOU 1332 O LEU A 167 7901 14466 9681 2030 150 -732 O ATOM 1333 CB LEU A 167 43.734 49.204 85.068 1.00 85.65 C ANISOU 1333 CB LEU A 167 7934 14653 9956 1983 252 -537 C ATOM 1334 CG LEU A 167 43.746 49.724 83.629 1.00 87.96 C ANISOU 1334 CG LEU A 167 8156 15044 10222 1972 301 -455 C ATOM 1335 CD1 LEU A 167 42.811 50.920 83.479 1.00 74.84 C ANISOU 1335 CD1 LEU A 167 6495 13328 8611 1965 321 -319 C ATOM 1336 CD2 LEU A 167 45.170 50.071 83.198 1.00 84.66 C ANISOU 1336 CD2 LEU A 167 7619 14676 9872 1954 358 -489 C ATOM 1337 N LYS A 168 41.984 47.574 87.674 1.00 84.43 N ANISOU 1337 N LYS A 168 8017 14343 9718 2018 121 -631 N ATOM 1338 CA LYS A 168 42.049 46.605 88.707 1.00 86.25 C ANISOU 1338 CA LYS A 168 8304 14542 9924 2035 78 -713 C ATOM 1339 C LYS A 168 41.543 45.328 88.128 1.00 72.59 C ANISOU 1339 C LYS A 168 6617 12874 8090 2052 54 -745 C ATOM 1340 O LYS A 168 40.523 45.253 87.418 1.00 74.49 O ANISOU 1340 O LYS A 168 6886 13152 8266 2047 53 -690 O ATOM 1341 CB LYS A 168 41.246 47.038 89.948 1.00 96.72 C ANISOU 1341 CB LYS A 168 9691 15775 11284 2031 56 -687 C ATOM 1342 CG LYS A 168 41.940 48.094 90.820 1.00101.99 C ANISOU 1342 CG LYS A 168 10311 16373 12066 2020 70 -696 C ATOM 1343 CD LYS A 168 41.167 48.363 92.121 1.00115.91 C ANISOU 1343 CD LYS A 168 12135 18058 13850 2022 42 -691 C ATOM 1344 CE LYS A 168 41.815 47.678 93.337 1.00112.89 C ANISOU 1344 CE LYS A 168 11770 17666 13458 2038 7 -784 C ATOM 1345 NZ LYS A 168 41.003 47.830 94.590 1.00104.65 N1+ ANISOU 1345 NZ LYS A 168 10785 16565 12412 2042 -20 -782 N1+ ATOM 1346 N VAL A 169 42.274 44.302 88.467 1.00 68.90 N ANISOU 1346 N VAL A 169 6145 12419 7613 2075 34 -837 N ATOM 1347 CA VAL A 169 42.072 43.057 87.830 1.00 67.16 C ANISOU 1347 CA VAL A 169 5940 12256 7323 2094 17 -886 C ATOM 1348 C VAL A 169 41.191 42.161 88.621 1.00 81.78 C ANISOU 1348 C VAL A 169 7871 14057 9144 2105 -21 -903 C ATOM 1349 O VAL A 169 41.445 41.804 89.833 1.00111.57 O ANISOU 1349 O VAL A 169 11672 17769 12951 2121 -43 -940 O ATOM 1350 CB VAL A 169 43.398 42.307 87.558 1.00 64.39 C ANISOU 1350 CB VAL A 169 5522 11954 6988 2123 25 -982 C ATOM 1351 CG1 VAL A 169 44.372 42.480 88.714 1.00 80.98 C ANISOU 1351 CG1 VAL A 169 7601 14006 9160 2138 20 -1025 C ATOM 1352 CG2 VAL A 169 43.116 40.814 87.276 1.00 60.97 C ANISOU 1352 CG2 VAL A 169 5113 11544 6507 2154 -1 -1049 C ATOM 1353 N ILE A 170 40.218 41.778 87.816 1.00 66.81 N ANISOU 1353 N ILE A 170 5999 12204 7182 2098 -26 -878 N ATOM 1354 CA ILE A 170 39.050 41.087 88.193 1.00 67.65 C ANISOU 1354 CA ILE A 170 6172 12283 7250 2097 -52 -870 C ATOM 1355 C ILE A 170 38.843 39.628 88.019 1.00 78.46 C ANISOU 1355 C ILE A 170 7552 13664 8596 2117 -74 -941 C ATOM 1356 O ILE A 170 38.071 39.164 88.761 1.00 80.67 O ANISOU 1356 O ILE A 170 7882 13893 8875 2116 -93 -933 O ATOM 1357 CB ILE A 170 37.760 41.754 87.527 1.00 88.72 C ANISOU 1357 CB ILE A 170 8859 14988 9861 2073 -43 -778 C ATOM 1358 CG1 ILE A 170 37.787 43.278 87.595 1.00 94.59 C ANISOU 1358 CG1 ILE A 170 9584 15711 10644 2057 -16 -691 C ATOM 1359 CG2 ILE A 170 36.436 41.317 88.215 1.00 42.97 C ANISOU 1359 CG2 ILE A 170 3131 9155 4042 2067 -65 -755 C ATOM 1360 CD1 ILE A 170 36.379 43.902 87.415 1.00 78.82 C ANISOU 1360 CD1 ILE A 170 7616 13722 8611 2046 -11 -594 C ATOM 1361 N LEU A 171 39.273 38.945 86.979 1.00 89.94 N ANISOU 1361 N LEU A 171 8959 15187 10027 2131 -70 -1000 N ATOM 1362 CA LEU A 171 39.013 37.507 86.878 1.00 76.19 C ANISOU 1362 CA LEU A 171 7223 13440 8286 2153 -90 -1074 C ATOM 1363 C LEU A 171 40.279 37.370 86.118 1.00 62.81 C ANISOU 1363 C LEU A 171 5454 11806 6607 2177 -71 -1139 C ATOM 1364 O LEU A 171 40.366 37.949 85.100 1.00 76.66 O ANISOU 1364 O LEU A 171 7169 13644 8315 2161 -52 -1119 O ATOM 1365 CB LEU A 171 37.727 37.137 86.148 1.00 77.46 C ANISOU 1365 CB LEU A 171 7401 13647 8382 2131 -100 -1059 C ATOM 1366 CG LEU A 171 37.485 35.634 86.137 1.00 77.11 C ANISOU 1366 CG LEU A 171 7353 13579 8366 2152 -117 -1143 C ATOM 1367 CD1 LEU A 171 38.199 34.985 87.316 1.00 64.44 C ANISOU 1367 CD1 LEU A 171 5761 11875 6850 2189 -123 -1179 C ATOM 1368 CD2 LEU A 171 36.005 35.353 86.167 1.00 70.40 C ANISOU 1368 CD2 LEU A 171 6541 12729 7480 2124 -132 -1110 C ATOM 1369 N ASP A 172 41.263 36.628 86.594 1.00 61.19 N ANISOU 1369 N ASP A 172 5220 11565 6463 2219 -71 -1212 N ATOM 1370 CA ASP A 172 42.355 36.120 85.787 1.00 65.75 C ANISOU 1370 CA ASP A 172 5717 12207 7059 2254 -51 -1296 C ATOM 1371 C ASP A 172 42.423 34.598 85.951 1.00 75.30 C ANISOU 1371 C ASP A 172 6919 13373 8319 2303 -62 -1381 C ATOM 1372 O ASP A 172 42.752 34.139 87.008 1.00 92.80 O ANISOU 1372 O ASP A 172 9153 15510 10596 2337 -72 -1391 O ATOM 1373 CB ASP A 172 43.672 36.789 86.194 1.00 75.09 C ANISOU 1373 CB ASP A 172 6850 13394 8286 2270 -30 -1301 C ATOM 1374 CG ASP A 172 44.881 36.293 85.396 1.00102.73 C ANISOU 1374 CG ASP A 172 10254 16969 11808 2312 0 -1390 C ATOM 1375 OD1 ASP A 172 44.865 35.164 84.851 1.00101.50 O ANISOU 1375 OD1 ASP A 172 10074 16831 11660 2347 1 -1466 O ATOM 1376 OD2 ASP A 172 45.880 37.046 85.332 1.00125.15 O ANISOU 1376 OD2 ASP A 172 13034 19852 14667 2311 28 -1388 O ATOM 1377 N GLU A 173 42.192 33.794 84.921 1.00 94.44 N ANISOU 1377 N GLU A 173 9307 15848 10727 2314 -57 -1447 N ATOM 1378 CA GLU A 173 42.235 32.361 85.177 1.00 92.02 C ANISOU 1378 CA GLU A 173 8991 15476 10495 2365 -60 -1525 C ATOM 1379 C GLU A 173 42.596 31.415 84.092 1.00 89.16 C ANISOU 1379 C GLU A 173 8557 15169 10152 2402 -38 -1633 C ATOM 1380 O GLU A 173 42.554 31.704 82.953 1.00109.84 O ANISOU 1380 O GLU A 173 11135 17894 12706 2378 -25 -1657 O ATOM 1381 CB GLU A 173 40.873 31.907 85.720 1.00 91.41 C ANISOU 1381 CB GLU A 173 8985 15326 10421 2338 -87 -1486 C ATOM 1382 CG GLU A 173 40.562 32.213 87.198 1.00113.41 C ANISOU 1382 CG GLU A 173 11840 18017 13235 2331 -105 -1408 C ATOM 1383 CD GLU A 173 41.472 31.477 88.195 1.00125.08 C ANISOU 1383 CD GLU A 173 13303 19415 14806 2399 -100 -1438 C ATOM 1384 OE1 GLU A 173 41.567 31.913 89.369 1.00103.44 O ANISOU 1384 OE1 GLU A 173 10602 16626 12076 2399 -111 -1382 O ATOM 1385 OE2 GLU A 173 42.079 30.454 87.814 1.00135.24 O ANISOU 1385 OE2 GLU A 173 14536 20692 16159 2458 -82 -1519 O ATOM 1386 N PHE A 174 43.004 30.253 84.498 1.00 79.18 N ANISOU 1386 N PHE A 174 7272 13828 8985 2467 -27 -1698 N ATOM 1387 CA PHE A 174 43.299 29.186 83.558 1.00 78.19 C ANISOU 1387 CA PHE A 174 7077 13730 8900 2513 3 -1814 C ATOM 1388 C PHE A 174 42.092 28.248 83.463 1.00 80.09 C ANISOU 1388 C PHE A 174 7348 13913 9171 2499 -10 -1839 C ATOM 1389 O PHE A 174 41.601 27.760 84.481 1.00109.85 O ANISOU 1389 O PHE A 174 11167 17567 13006 2510 -25 -1799 O ATOM 1390 CB PHE A 174 44.553 28.398 83.980 1.00 84.14 C ANISOU 1390 CB PHE A 174 7776 14431 9762 2612 38 -1879 C ATOM 1391 CG PHE A 174 45.866 29.096 83.675 1.00104.68 C ANISOU 1391 CG PHE A 174 10310 17124 12341 2634 66 -1897 C ATOM 1392 CD1 PHE A 174 45.943 30.479 83.555 1.00116.64 C ANISOU 1392 CD1 PHE A 174 11835 18717 13767 2568 54 -1825 C ATOM 1393 CD2 PHE A 174 47.030 28.356 83.498 1.00112.65 C ANISOU 1393 CD2 PHE A 174 11237 18138 13427 2727 112 -1988 C ATOM 1394 CE1 PHE A 174 47.160 31.109 83.272 1.00117.83 C ANISOU 1394 CE1 PHE A 174 11911 18952 13909 2586 87 -1842 C ATOM 1395 CE2 PHE A 174 48.244 28.980 83.213 1.00108.59 C ANISOU 1395 CE2 PHE A 174 10648 17718 12894 2748 143 -2009 C ATOM 1396 CZ PHE A 174 48.306 30.357 83.102 1.00107.41 C ANISOU 1396 CZ PHE A 174 10504 17647 12658 2673 130 -1936 C ATOM 1397 N VAL A 175 41.605 28.019 82.244 1.00 80.01 N ANISOU 1397 N VAL A 175 7300 13992 9109 2471 -2 -1905 N ATOM 1398 CA VAL A 175 40.552 27.041 82.004 1.00 77.66 C ANISOU 1398 CA VAL A 175 7007 13653 8848 2459 -7 -1955 C ATOM 1399 C VAL A 175 41.113 25.859 81.228 1.00 83.21 C ANISOU 1399 C VAL A 175 7631 14353 9631 2524 44 -2099 C ATOM 1400 O VAL A 175 41.922 26.045 80.328 1.00 98.83 O ANISOU 1400 O VAL A 175 9544 16436 11570 2543 75 -2165 O ATOM 1401 CB VAL A 175 39.363 27.644 81.266 1.00 73.79 C ANISOU 1401 CB VAL A 175 6534 13270 8234 2373 -39 -1924 C ATOM 1402 CG1 VAL A 175 38.196 26.672 81.287 1.00 78.57 C ANISOU 1402 CG1 VAL A 175 7146 13818 8886 2353 -48 -1964 C ATOM 1403 CG2 VAL A 175 38.960 28.955 81.913 1.00 85.36 C ANISOU 1403 CG2 VAL A 175 8070 14745 9617 2322 -71 -1783 C ATOM 1404 N LYS A 176 40.696 24.648 81.584 1.00 88.04 N ANISOU 1404 N LYS A 176 8247 14844 10362 2562 63 -2147 N ATOM 1405 CA LYS A 176 41.077 23.459 80.823 1.00 96.77 C ANISOU 1405 CA LYS A 176 9283 15930 11555 2627 126 -2293 C ATOM 1406 C LYS A 176 39.813 22.881 80.208 1.00102.43 C ANISOU 1406 C LYS A 176 9994 16662 12264 2571 121 -2354 C ATOM 1407 O LYS A 176 38.856 22.592 80.929 1.00 90.43 O ANISOU 1407 O LYS A 176 8521 15050 10790 2541 97 -2297 O ATOM 1408 CB LYS A 176 41.770 22.429 81.726 1.00105.56 C ANISOU 1408 CB LYS A 176 10397 16873 12837 2738 173 -2309 C ATOM 1409 CG LYS A 176 42.246 21.158 81.037 1.00110.63 C ANISOU 1409 CG LYS A 176 10979 17467 13590 2829 259 -2459 C ATOM 1410 CD LYS A 176 43.431 21.430 80.121 1.00124.56 C ANISOU 1410 CD LYS A 176 12671 19353 15305 2872 303 -2545 C ATOM 1411 CE LYS A 176 43.787 20.203 79.286 1.00135.18 C ANISOU 1411 CE LYS A 176 13960 20662 16741 2958 403 -2713 C ATOM 1412 NZ LYS A 176 42.688 19.777 78.361 1.00132.00 N1+ ANISOU 1412 NZ LYS A 176 13549 20303 16303 2889 413 -2806 N1+ ATOM 1413 N PRO A 177 39.801 22.740 78.867 1.00108.06 N ANISOU 1413 N PRO A 177 10641 17504 12911 2551 148 -2471 N ATOM 1414 CA PRO A 177 38.581 22.430 78.115 1.00100.31 C ANISOU 1414 CA PRO A 177 9641 16593 11880 2477 134 -2534 C ATOM 1415 C PRO A 177 38.124 20.986 78.238 1.00101.83 C ANISOU 1415 C PRO A 177 9821 16645 12223 2515 189 -2636 C ATOM 1416 O PRO A 177 38.947 20.071 78.263 1.00107.91 O ANISOU 1416 O PRO A 177 10571 17311 13120 2614 267 -2723 O ATOM 1417 CB PRO A 177 38.975 22.748 76.667 1.00 94.11 C ANISOU 1417 CB PRO A 177 8780 16001 10976 2457 157 -2633 C ATOM 1418 CG PRO A 177 40.206 23.632 76.770 1.00 90.37 C ANISOU 1418 CG PRO A 177 8301 15576 10459 2494 161 -2571 C ATOM 1419 CD PRO A 177 40.911 23.108 77.966 1.00100.27 C ANISOU 1419 CD PRO A 177 9591 16644 11865 2582 185 -2537 C ATOM 1420 N ASN A 178 36.805 20.826 78.328 1.00102.07 N ANISOU 1420 N ASN A 178 9867 16674 12241 2440 155 -2619 N ATOM 1421 CA ASN A 178 36.119 19.537 78.362 1.00118.09 C ANISOU 1421 CA ASN A 178 11880 18587 14402 2451 207 -2715 C ATOM 1422 C ASN A 178 36.653 18.551 77.318 1.00129.00 C ANISOU 1422 C ASN A 178 13203 19974 15838 2505 305 -2912 C ATOM 1423 O ASN A 178 36.948 17.392 77.629 1.00130.48 O ANISOU 1423 O ASN A 178 13401 19984 16191 2594 393 -2986 O ATOM 1424 CB ASN A 178 34.612 19.747 78.169 1.00128.74 C ANISOU 1424 CB ASN A 178 13223 20023 15671 2335 152 -2696 C ATOM 1425 CG ASN A 178 34.290 20.638 76.968 1.00131.54 C ANISOU 1425 CG ASN A 178 13534 20625 15821 2251 105 -2726 C ATOM 1426 OD1 ASN A 178 35.032 21.576 76.659 1.00134.04 O ANISOU 1426 OD1 ASN A 178 13853 21044 16030 2261 82 -2676 O ATOM 1427 ND2 ASN A 178 33.183 20.341 76.284 1.00119.40 N ANISOU 1427 ND2 ASN A 178 11948 19191 14228 2169 96 -2805 N ATOM 1428 N LYS A 179 36.770 19.023 76.078 1.00132.85 N ANISOU 1428 N LYS A 179 13634 20663 16181 2457 300 -2996 N ATOM 1429 CA LYS A 179 37.363 18.241 74.997 1.00128.79 C ANISOU 1429 CA LYS A 179 13065 20184 15686 2505 402 -3190 C ATOM 1430 C LYS A 179 38.841 18.588 74.870 1.00137.17 C ANISOU 1430 C LYS A 179 14112 21266 16741 2593 438 -3187 C ATOM 1431 O LYS A 179 39.223 19.748 75.047 1.00143.31 O ANISOU 1431 O LYS A 179 14893 22141 17417 2568 368 -3062 O ATOM 1432 CB LYS A 179 36.651 18.511 73.670 1.00123.58 C ANISOU 1432 CB LYS A 179 12339 19753 14863 2398 387 -3292 C ATOM 1433 CG LYS A 179 35.225 18.038 73.649 1.00129.85 C ANISOU 1433 CG LYS A 179 13127 20548 15662 2309 367 -3332 C ATOM 1434 CD LYS A 179 34.510 18.427 72.376 1.00134.56 C ANISOU 1434 CD LYS A 179 13650 21404 16073 2195 337 -3417 C ATOM 1435 CE LYS A 179 33.051 18.013 72.462 1.00141.08 C ANISOU 1435 CE LYS A 179 14462 22242 16901 2099 310 -3445 C ATOM 1436 NZ LYS A 179 32.237 18.480 71.312 1.00145.49 N1+ ANISOU 1436 NZ LYS A 179 14942 23078 17260 1977 264 -3505 N1+ ATOM 1437 N PRO A 180 39.680 17.581 74.564 1.00138.72 N ANISOU 1437 N PRO A 180 14296 21367 17046 2702 557 -3329 N ATOM 1438 CA PRO A 180 41.134 17.771 74.492 1.00138.17 C ANISOU 1438 CA PRO A 180 14202 21307 16988 2800 606 -3338 C ATOM 1439 C PRO A 180 41.538 18.720 73.373 1.00129.91 C ANISOU 1439 C PRO A 180 13087 20511 15762 2742 590 -3365 C ATOM 1440 O PRO A 180 40.688 19.326 72.736 1.00135.58 O ANISOU 1440 O PRO A 180 13780 21393 16339 2627 528 -3353 O ATOM 1441 CB PRO A 180 41.655 16.360 74.205 1.00133.18 C ANISOU 1441 CB PRO A 180 13577 20527 16496 2923 753 -3514 C ATOM 1442 CG PRO A 180 40.517 15.679 73.523 1.00127.88 C ANISOU 1442 CG PRO A 180 12914 19866 15810 2851 789 -3647 C ATOM 1443 CD PRO A 180 39.287 16.210 74.195 1.00131.62 C ANISOU 1443 CD PRO A 180 13408 20348 16253 2739 667 -3502 C ATOM 1444 N VAL A 181 42.835 18.851 73.137 1.00120.96 N ANISOU 1444 N VAL A 181 11915 19412 14632 2824 648 -3398 N ATOM 1445 CA VAL A 181 43.315 19.856 72.199 1.00123.14 C ANISOU 1445 CA VAL A 181 12123 19921 14743 2772 636 -3396 C ATOM 1446 C VAL A 181 44.556 19.379 71.447 1.00137.34 C ANISOU 1446 C VAL A 181 13860 21762 16560 2869 763 -3544 C ATOM 1447 O VAL A 181 45.429 18.726 72.024 1.00146.11 O ANISOU 1447 O VAL A 181 14984 22723 17809 2995 830 -3572 O ATOM 1448 CB VAL A 181 43.791 21.133 72.951 1.00129.86 C ANISOU 1448 CB VAL A 181 12990 20807 15544 2753 548 -3204 C ATOM 1449 CG1 VAL A 181 43.032 22.347 72.547 1.00139.24 C ANISOU 1449 CG1 VAL A 181 14177 22169 16558 2627 456 -3100 C ATOM 1450 CG2 VAL A 181 43.746 20.930 74.456 1.00126.50 C ANISOU 1450 CG2 VAL A 181 12642 20171 15251 2800 505 -3087 C ATOM 1451 N VAL A 182 44.610 19.693 70.152 1.00136.87 N ANISOU 1451 N VAL A 182 13733 21915 16358 2814 802 -3638 N ATOM 1452 CA VAL A 182 45.717 19.293 69.285 1.00132.49 C ANISOU 1452 CA VAL A 182 13115 21434 15793 2893 934 -3792 C ATOM 1453 C VAL A 182 46.843 20.337 69.258 1.00130.30 C ANISOU 1453 C VAL A 182 12775 21283 15450 2908 925 -3701 C ATOM 1454 O VAL A 182 48.020 19.988 69.357 1.00135.81 O ANISOU 1454 O VAL A 182 13441 21938 16223 3021 1012 -3760 O ATOM 1455 CB VAL A 182 45.231 19.029 67.840 1.00129.42 C ANISOU 1455 CB VAL A 182 12681 21223 15270 2823 1001 -3960 C ATOM 1456 CG1 VAL A 182 44.270 20.116 67.385 1.00121.08 C ANISOU 1456 CG1 VAL A 182 11598 20368 14038 2671 887 -3852 C ATOM 1457 CG2 VAL A 182 46.413 18.911 66.886 1.00133.69 C ANISOU 1457 CG2 VAL A 182 13150 21887 15757 2887 1133 -4096 C ATOM 1458 N ASP A 183 46.480 21.613 69.155 1.00124.87 N ANISOU 1458 N ASP A 183 12074 20744 14627 2799 826 -3557 N ATOM 1459 CA ASP A 183 47.461 22.679 68.975 1.00125.49 C ANISOU 1459 CA ASP A 183 12093 20961 14627 2795 830 -3477 C ATOM 1460 C ASP A 183 47.311 23.808 70.000 1.00118.67 C ANISOU 1460 C ASP A 183 11281 20056 13753 2748 711 -3262 C ATOM 1461 O ASP A 183 46.272 24.464 70.059 1.00115.04 O ANISOU 1461 O ASP A 183 10864 19637 13207 2651 617 -3156 O ATOM 1462 CB ASP A 183 47.355 23.254 67.556 1.00131.94 C ANISOU 1462 CB ASP A 183 12832 22040 15259 2710 865 -3527 C ATOM 1463 CG ASP A 183 48.359 24.374 67.293 1.00134.03 C ANISOU 1463 CG ASP A 183 13029 22454 15442 2700 884 -3443 C ATOM 1464 OD1 ASP A 183 49.413 24.411 67.964 1.00133.01 O1+ ANISOU 1464 OD1 ASP A 183 12887 22242 15408 2781 913 -3418 O1+ ATOM 1465 OD2 ASP A 183 48.093 25.213 66.405 1.00135.88 O ANISOU 1465 OD2 ASP A 183 13217 22895 15515 2609 875 -3401 O ATOM 1466 N TYR A 184 48.366 24.052 70.772 1.00118.75 N ANISOU 1466 N TYR A 184 11283 19994 13840 2818 723 -3205 N ATOM 1467 CA TYR A 184 48.365 25.070 71.813 1.00112.57 C ANISOU 1467 CA TYR A 184 10556 19160 13057 2783 630 -3020 C ATOM 1468 C TYR A 184 48.845 26.433 71.399 1.00109.49 C ANISOU 1468 C TYR A 184 10119 18938 12545 2720 623 -2925 C ATOM 1469 O TYR A 184 48.859 27.338 72.196 1.00126.20 O ANISOU 1469 O TYR A 184 12282 21014 14656 2688 560 -2781 O ATOM 1470 CB TYR A 184 49.182 24.581 73.010 1.00118.66 C ANISOU 1470 CB TYR A 184 11349 19755 13983 2889 641 -3005 C ATOM 1471 CG TYR A 184 48.519 23.402 73.676 1.00128.21 C ANISOU 1471 CG TYR A 184 12627 20768 15319 2940 631 -3044 C ATOM 1472 CD1 TYR A 184 47.519 23.583 74.625 1.00116.96 C ANISOU 1472 CD1 TYR A 184 11299 19228 13915 2887 535 -2924 C ATOM 1473 CD2 TYR A 184 48.857 22.104 73.323 1.00144.63 C ANISOU 1473 CD2 TYR A 184 14677 22777 17498 3042 730 -3204 C ATOM 1474 CE1 TYR A 184 46.891 22.497 75.223 1.00116.14 C ANISOU 1474 CE1 TYR A 184 11251 18946 13931 2930 535 -2955 C ATOM 1475 CE2 TYR A 184 48.237 21.013 73.916 1.00145.83 C ANISOU 1475 CE2 TYR A 184 14895 22738 17777 3092 734 -3236 C ATOM 1476 CZ TYR A 184 47.250 21.215 74.860 1.00131.07 C ANISOU 1476 CZ TYR A 184 13112 20762 15928 3031 635 -3108 C ATOM 1477 OH TYR A 184 46.639 20.128 75.448 1.00129.63 O ANISOU 1477 OH TYR A 184 12987 20390 15875 3078 648 -3135 O ATOM 1478 N ARG A 185 49.309 26.570 70.184 1.00101.29 N ANISOU 1478 N ARG A 185 8987 18083 11416 2708 701 -3009 N ATOM 1479 CA ARG A 185 49.508 27.875 69.631 1.00 97.76 C ANISOU 1479 CA ARG A 185 8496 17808 10838 2631 697 -2910 C ATOM 1480 C ARG A 185 50.468 28.676 70.470 1.00 99.36 C ANISOU 1480 C ARG A 185 8693 17968 11091 2652 692 -2806 C ATOM 1481 O ARG A 185 50.458 29.896 70.437 1.00 97.74 O ANISOU 1481 O ARG A 185 8488 17839 10808 2584 666 -2676 O ATOM 1482 CB ARG A 185 48.162 28.619 69.477 1.00 89.46 C ANISOU 1482 CB ARG A 185 7509 16807 9674 2524 602 -2788 C ATOM 1483 CG ARG A 185 47.042 27.832 68.800 1.00 89.70 C ANISOU 1483 CG ARG A 185 7551 16874 9657 2492 587 -2883 C ATOM 1484 CD ARG A 185 45.785 28.701 68.633 1.00 94.77 C ANISOU 1484 CD ARG A 185 8241 17593 10173 2392 494 -2749 C ATOM 1485 NE ARG A 185 44.955 28.295 67.492 1.00110.52 N ANISOU 1485 NE ARG A 185 10193 19742 12057 2340 501 -2841 N ATOM 1486 CZ ARG A 185 43.744 28.784 67.221 1.00111.61 C ANISOU 1486 CZ ARG A 185 10360 19965 12082 2261 424 -2757 C ATOM 1487 NH1 ARG A 185 43.073 28.355 66.165 1.00114.14 N ANISOU 1487 NH1 ARG A 185 10625 20442 12300 2213 436 -2856 N ATOM 1488 NH2 ARG A 185 43.194 29.698 68.008 1.00111.60 N ANISOU 1488 NH2 ARG A 185 10441 19898 12066 2232 340 -2577 N ATOM 1489 N THR A 186 51.333 28.004 71.202 1.00 98.42 N ANISOU 1489 N THR A 186 8562 17731 11103 2751 726 -2864 N ATOM 1490 CA THR A 186 52.448 28.681 71.807 1.00107.14 C ANISOU 1490 CA THR A 186 9626 18836 12247 2778 743 -2802 C ATOM 1491 C THR A 186 53.300 28.963 70.612 1.00136.11 C ANISOU 1491 C THR A 186 13170 22708 15839 2773 849 -2877 C ATOM 1492 O THR A 186 53.390 28.116 69.748 1.00148.91 O ANISOU 1492 O THR A 186 14739 24394 17446 2812 925 -3022 O ATOM 1493 CB THR A 186 53.208 27.798 72.814 1.00109.31 C ANISOU 1493 CB THR A 186 9901 18957 12675 2897 759 -2856 C ATOM 1494 OG1 THR A 186 53.497 26.546 72.191 1.00130.48 O ANISOU 1494 OG1 THR A 186 12533 21638 15405 2987 846 -3026 O ATOM 1495 CG2 THR A 186 52.388 27.489 74.009 1.00100.82 C ANISOU 1495 CG2 THR A 186 8946 17687 11674 2901 665 -2779 C ATOM 1496 N ASP A 187 53.857 30.150 70.472 1.00139.11 N ANISOU 1496 N ASP A 187 13498 23197 16160 2719 866 -2785 N ATOM 1497 CA ASP A 187 54.240 31.055 71.521 1.00140.14 C ANISOU 1497 CA ASP A 187 13656 23254 16337 2701 819 -2655 C ATOM 1498 C ASP A 187 53.190 31.622 72.452 1.00150.89 C ANISOU 1498 C ASP A 187 15149 24482 17701 2642 703 -2509 C ATOM 1499 O ASP A 187 53.422 31.717 73.649 1.00166.35 O ANISOU 1499 O ASP A 187 17155 26307 19744 2670 658 -2455 O ATOM 1500 CB ASP A 187 54.987 32.237 70.890 1.00144.15 C ANISOU 1500 CB ASP A 187 14067 23933 16771 2641 885 -2598 C ATOM 1501 CG ASP A 187 54.087 33.104 70.033 1.00144.67 C ANISOU 1501 CG ASP A 187 14153 24113 16703 2534 868 -2503 C ATOM 1502 OD1 ASP A 187 53.024 32.603 69.602 1.00137.65 O ANISOU 1502 OD1 ASP A 187 13320 23223 15759 2515 827 -2529 O ATOM 1503 OD2 ASP A 187 54.432 34.284 69.802 1.00147.80 O ANISOU 1503 OD2 ASP A 187 14504 24601 17052 2470 897 -2401 O ATOM 1504 N ILE A 188 52.055 32.043 71.922 1.00142.42 N ANISOU 1504 N ILE A 188 14130 23455 16530 2563 659 -2443 N ATOM 1505 CA ILE A 188 51.171 32.888 72.713 1.00133.60 C ANISOU 1505 CA ILE A 188 13121 22242 15398 2501 568 -2286 C ATOM 1506 C ILE A 188 50.314 32.062 73.639 1.00118.69 C ANISOU 1506 C ILE A 188 11343 20176 13576 2529 490 -2293 C ATOM 1507 O ILE A 188 49.099 32.080 73.580 1.00101.30 O ANISOU 1507 O ILE A 188 9217 17949 11322 2482 430 -2245 O ATOM 1508 CB ILE A 188 50.329 33.704 71.680 1.00139.64 C ANISOU 1508 CB ILE A 188 13885 23150 16021 2412 561 -2207 C ATOM 1509 CG1 ILE A 188 51.228 34.664 70.888 1.00138.00 C ANISOU 1509 CG1 ILE A 188 13568 23109 15757 2378 645 -2173 C ATOM 1510 CG2 ILE A 188 49.205 34.443 72.283 1.00134.77 C ANISOU 1510 CG2 ILE A 188 13381 22449 15376 2357 475 -2060 C ATOM 1511 CD1 ILE A 188 50.555 35.316 69.694 1.00129.51 C ANISOU 1511 CD1 ILE A 188 12465 22206 14536 2304 659 -2110 C ATOM 1512 N THR A 189 50.964 31.305 74.501 1.00119.33 N ANISOU 1512 N THR A 189 11426 20139 13776 2610 496 -2352 N ATOM 1513 CA THR A 189 50.236 30.441 75.398 1.00115.78 C ANISOU 1513 CA THR A 189 11070 19520 13401 2642 436 -2358 C ATOM 1514 C THR A 189 51.080 29.866 76.504 1.00111.62 C ANISOU 1514 C THR A 189 10540 18868 13000 2731 443 -2385 C ATOM 1515 O THR A 189 52.292 29.910 76.474 1.00104.19 O ANISOU 1515 O THR A 189 9512 17980 12096 2784 500 -2430 O ATOM 1516 CB THR A 189 49.551 29.238 74.655 1.00133.16 C ANISOU 1516 CB THR A 189 13268 21723 15603 2665 451 -2478 C ATOM 1517 OG1 THR A 189 49.298 29.558 73.282 1.00132.51 O ANISOU 1517 OG1 THR A 189 13127 21820 15400 2611 485 -2513 O ATOM 1518 CG2 THR A 189 48.240 28.853 75.317 1.00139.34 C ANISOU 1518 CG2 THR A 189 14163 22374 16407 2637 372 -2430 C ATOM 1519 N GLY A 190 50.401 29.321 77.487 1.00115.11 N ANISOU 1519 N GLY A 190 11076 19154 13507 2748 385 -2352 N ATOM 1520 CA GLY A 190 51.004 28.451 78.450 1.00124.59 C ANISOU 1520 CA GLY A 190 12277 20230 14831 2847 393 -2390 C ATOM 1521 C GLY A 190 50.977 27.094 77.808 1.00125.16 C ANISOU 1521 C GLY A 190 12312 20281 14963 2923 447 -2527 C ATOM 1522 O GLY A 190 50.599 26.948 76.669 1.00115.10 O ANISOU 1522 O GLY A 190 11007 19101 13626 2891 478 -2594 O ATOM 1523 N ILE A 191 51.406 26.097 78.546 1.00126.48 N ANISOU 1523 N ILE A 191 12480 20324 15254 3029 466 -2569 N ATOM 1524 CA ILE A 191 51.436 24.735 78.053 1.00121.93 C ANISOU 1524 CA ILE A 191 11873 19694 14760 3120 533 -2701 C ATOM 1525 C ILE A 191 50.496 23.810 78.793 1.00130.81 C ANISOU 1525 C ILE A 191 13087 20639 15976 3143 500 -2682 C ATOM 1526 O ILE A 191 50.193 24.017 79.952 1.00137.78 O ANISOU 1526 O ILE A 191 14039 21422 16889 3130 438 -2575 O ATOM 1527 CB ILE A 191 52.884 24.188 78.177 1.00140.84 C ANISOU 1527 CB ILE A 191 14175 22093 17244 3257 613 -2782 C ATOM 1528 CG1 ILE A 191 53.872 25.180 77.566 1.00147.45 C ANISOU 1528 CG1 ILE A 191 14914 23112 17997 3229 648 -2790 C ATOM 1529 CG2 ILE A 191 53.052 22.823 77.516 1.00147.25 C ANISOU 1529 CG2 ILE A 191 14948 22857 18142 3366 708 -2936 C ATOM 1530 CD1 ILE A 191 53.949 25.103 76.044 1.00150.78 C ANISOU 1530 CD1 ILE A 191 15262 23684 18343 3209 726 -2904 C ATOM 1531 N THR A 192 50.099 22.738 78.132 1.00138.62 N ANISOU 1531 N THR A 192 14068 21585 17015 3185 555 -2796 N ATOM 1532 CA THR A 192 49.005 21.907 78.598 1.00148.32 C ANISOU 1532 CA THR A 192 15377 22659 18320 3183 532 -2785 C ATOM 1533 C THR A 192 49.363 21.420 79.982 1.00145.97 C ANISOU 1533 C THR A 192 15117 22198 18148 3273 521 -2716 C ATOM 1534 O THR A 192 48.494 21.177 80.802 1.00139.75 O ANISOU 1534 O THR A 192 14406 21288 17404 3247 473 -2638 O ATOM 1535 CB THR A 192 48.712 20.724 77.652 1.00157.52 C ANISOU 1535 CB THR A 192 16519 23793 19540 3233 619 -2943 C ATOM 1536 OG1 THR A 192 47.390 20.223 77.902 1.00157.98 O ANISOU 1536 OG1 THR A 192 16651 23743 19631 3182 583 -2923 O ATOM 1537 CG2 THR A 192 49.736 19.600 77.798 1.00159.86 C ANISOU 1537 CG2 THR A 192 16774 23985 19979 3403 723 -3042 C ATOM 1538 N ALA A 193 50.647 21.275 80.243 1.00150.80 N ANISOU 1538 N ALA A 193 15664 22817 18815 3382 568 -2743 N ATOM 1539 CA ALA A 193 51.068 20.822 81.546 1.00149.59 C ANISOU 1539 CA ALA A 193 15535 22528 18775 3477 559 -2677 C ATOM 1540 C ALA A 193 50.554 21.828 82.546 1.00152.25 C ANISOU 1540 C ALA A 193 15941 22863 19043 3374 456 -2525 C ATOM 1541 O ALA A 193 50.126 21.453 83.625 1.00153.98 O ANISOU 1541 O ALA A 193 16223 22951 19331 3395 424 -2447 O ATOM 1542 CB ALA A 193 52.586 20.691 81.619 1.00145.29 C ANISOU 1542 CB ALA A 193 14896 22030 18279 3604 619 -2728 C ATOM 1543 N GLU A 194 50.595 23.108 82.196 1.00151.75 N ANISOU 1543 N GLU A 194 15869 22943 18846 3267 412 -2482 N ATOM 1544 CA GLU A 194 50.181 24.133 83.137 1.00142.61 C ANISOU 1544 CA GLU A 194 14780 21782 17622 3177 329 -2346 C ATOM 1545 C GLU A 194 48.724 24.030 83.544 1.00129.71 C ANISOU 1545 C GLU A 194 13249 20057 15980 3099 275 -2276 C ATOM 1546 O GLU A 194 48.387 24.167 84.707 1.00125.94 O ANISOU 1546 O GLU A 194 12835 19496 15523 3087 230 -2180 O ATOM 1547 CB GLU A 194 50.434 25.527 82.562 1.00132.47 C ANISOU 1547 CB GLU A 194 13470 20657 16206 3080 309 -2317 C ATOM 1548 CG GLU A 194 51.849 25.730 82.077 1.00131.46 C ANISOU 1548 CG GLU A 194 13229 20642 16079 3143 368 -2386 C ATOM 1549 CD GLU A 194 52.084 27.133 81.589 1.00127.23 C ANISOU 1549 CD GLU A 194 12666 20249 15425 3046 355 -2343 C ATOM 1550 OE1 GLU A 194 51.266 28.015 81.927 1.00121.96 O ANISOU 1550 OE1 GLU A 194 12078 19574 14688 2944 294 -2241 O ATOM 1551 OE2 GLU A 194 53.079 27.352 80.866 1.00127.43 O ANISOU 1551 OE2 GLU A 194 12589 20395 15433 3075 413 -2409 O ATOM 1552 N ASP A 195 47.854 23.831 82.574 1.00119.58 N ANISOU 1552 N ASP A 195 11974 18804 14657 3041 281 -2326 N ATOM 1553 CA ASP A 195 46.423 23.785 82.832 1.00125.67 C ANISOU 1553 CA ASP A 195 12828 19511 15410 2960 232 -2267 C ATOM 1554 C ASP A 195 45.749 22.646 83.548 1.00138.62 C ANISOU 1554 C ASP A 195 14512 20983 17173 3006 241 -2259 C ATOM 1555 O ASP A 195 44.885 22.873 84.376 1.00146.00 O ANISOU 1555 O ASP A 195 15519 21856 18099 2950 191 -2162 O ATOM 1556 CB ASP A 195 45.703 23.921 81.501 1.00123.58 C ANISOU 1556 CB ASP A 195 12545 19353 15058 2885 237 -2333 C ATOM 1557 CG ASP A 195 46.096 25.172 80.780 1.00135.95 C ANISOU 1557 CG ASP A 195 14078 21088 16489 2820 223 -2313 C ATOM 1558 OD1 ASP A 195 46.819 25.986 81.404 1.00135.02 O ANISOU 1558 OD1 ASP A 195 13962 20990 16350 2822 208 -2242 O ATOM 1559 OD2 ASP A 195 45.687 25.341 79.607 1.00139.61 O ANISOU 1559 OD2 ASP A 195 14510 21666 16869 2768 233 -2368 O ATOM 1560 N ILE A 196 46.128 21.424 83.238 1.00140.55 N ANISOU 1560 N ILE A 196 14715 21151 17537 3111 314 -2359 N ATOM 1561 CA ILE A 196 45.327 20.303 83.660 1.00145.73 C ANISOU 1561 CA ILE A 196 15409 21647 18314 3146 338 -2363 C ATOM 1562 C ILE A 196 45.296 20.319 85.153 1.00150.88 C ANISOU 1562 C ILE A 196 16114 22191 19023 3171 302 -2237 C ATOM 1563 O ILE A 196 44.272 20.048 85.757 1.00146.23 O ANISOU 1563 O ILE A 196 15581 21512 18470 3130 279 -2172 O ATOM 1564 CB ILE A 196 45.852 18.948 83.099 1.00151.02 C ANISOU 1564 CB ILE A 196 16032 22230 19120 3277 444 -2498 C ATOM 1565 CG1 ILE A 196 44.973 17.786 83.580 1.00147.69 C ANISOU 1565 CG1 ILE A 196 15657 21621 18837 3314 479 -2494 C ATOM 1566 CG2 ILE A 196 47.326 18.730 83.437 1.00147.73 C ANISOU 1566 CG2 ILE A 196 15562 21799 18768 3413 491 -2518 C ATOM 1567 CD1 ILE A 196 45.243 16.477 82.861 1.00145.84 C ANISOU 1567 CD1 ILE A 196 15396 21290 18727 3430 597 -2642 C ATOM 1568 N GLU A 197 46.428 20.647 85.749 1.00157.60 N ANISOU 1568 N GLU A 197 16938 23063 19879 3237 301 -2205 N ATOM 1569 CA GLU A 197 46.486 20.736 87.192 1.00155.05 C ANISOU 1569 CA GLU A 197 16658 22660 19593 3261 266 -2089 C ATOM 1570 C GLU A 197 45.535 21.827 87.633 1.00151.80 C ANISOU 1570 C GLU A 197 16317 22299 19061 3121 187 -1987 C ATOM 1571 O GLU A 197 44.773 21.647 88.574 1.00153.76 O ANISOU 1571 O GLU A 197 16622 22458 19342 3100 164 -1902 O ATOM 1572 CB GLU A 197 47.918 21.029 87.674 1.00148.80 C ANISOU 1572 CB GLU A 197 15814 21917 18807 3349 273 -2084 C ATOM 1573 CG GLU A 197 48.051 21.312 89.174 1.00141.82 C ANISOU 1573 CG GLU A 197 14969 20988 17931 3364 229 -1968 C ATOM 1574 CD GLU A 197 49.459 21.736 89.580 1.00143.91 C ANISOU 1574 CD GLU A 197 15170 21329 18180 3438 229 -1973 C ATOM 1575 OE1 GLU A 197 49.693 22.951 89.765 1.00141.55 O ANISOU 1575 OE1 GLU A 197 14878 21140 17765 3358 182 -1935 O ATOM 1576 OE2 GLU A 197 50.332 20.852 89.720 1.00143.67 O ANISOU 1576 OE2 GLU A 197 15082 21248 18259 3582 281 -2016 O ATOM 1577 N ASN A 198 45.561 22.953 86.933 1.00146.80 N ANISOU 1577 N ASN A 198 15679 21807 18292 3031 156 -1994 N ATOM 1578 CA ASN A 198 44.707 24.064 87.300 1.00143.00 C ANISOU 1578 CA ASN A 198 15266 21371 17695 2911 93 -1899 C ATOM 1579 C ASN A 198 43.374 23.884 86.636 1.00126.10 C ANISOU 1579 C ASN A 198 13156 19230 15527 2832 82 -1913 C ATOM 1580 O ASN A 198 42.862 24.755 85.963 1.00112.15 O ANISOU 1580 O ASN A 198 11403 17566 13643 2742 53 -1903 O ATOM 1581 CB ASN A 198 45.360 25.395 86.915 1.00148.50 C ANISOU 1581 CB ASN A 198 15945 22207 18272 2860 73 -1889 C ATOM 1582 CG ASN A 198 46.734 25.577 87.557 1.00149.42 C ANISOU 1582 CG ASN A 198 16016 22338 18418 2938 85 -1887 C ATOM 1583 OD1 ASN A 198 46.852 26.088 88.675 1.00150.08 O ANISOU 1583 OD1 ASN A 198 16137 22399 18487 2930 54 -1808 O ATOM 1584 ND2 ASN A 198 47.779 25.152 86.850 1.00137.80 N ANISOU 1584 ND2 ASN A 198 14458 20912 16987 3017 134 -1980 N ATOM 1585 N ALA A 199 42.802 22.730 86.898 1.00122.63 N ANISOU 1585 N ALA A 199 12723 18669 15202 2872 108 -1928 N ATOM 1586 CA ALA A 199 41.638 22.261 86.206 1.00113.95 C ANISOU 1586 CA ALA A 199 11630 17560 14108 2817 112 -1969 C ATOM 1587 C ALA A 199 40.403 23.014 86.616 1.00118.79 C ANISOU 1587 C ALA A 199 12307 18196 14631 2707 55 -1874 C ATOM 1588 O ALA A 199 39.366 22.887 85.987 1.00118.92 O ANISOU 1588 O ALA A 199 12324 18241 14618 2643 46 -1901 O ATOM 1589 CB ALA A 199 41.433 20.763 86.443 1.00107.79 C ANISOU 1589 CB ALA A 199 10833 16623 13498 2901 170 -2013 C ATOM 1590 N SER A 200 40.498 23.783 87.687 1.00123.59 N ANISOU 1590 N SER A 200 12966 18796 15198 2688 21 -1768 N ATOM 1591 CA SER A 200 39.330 24.152 88.457 1.00127.36 C ANISOU 1591 CA SER A 200 13507 19244 15641 2617 -13 -1671 C ATOM 1592 C SER A 200 38.269 24.914 87.692 1.00125.36 C ANISOU 1592 C SER A 200 13274 19091 15265 2514 -44 -1662 C ATOM 1593 O SER A 200 37.098 24.573 87.747 1.00124.91 O ANISOU 1593 O SER A 200 13231 19006 15222 2469 -51 -1644 O ATOM 1594 CB SER A 200 39.763 24.997 89.657 1.00134.06 C ANISOU 1594 CB SER A 200 14401 20088 16447 2617 -38 -1574 C ATOM 1595 OG SER A 200 40.408 26.180 89.217 1.00136.42 O ANISOU 1595 OG SER A 200 14698 20500 16634 2587 -55 -1576 O ATOM 1596 N LEU A 201 38.684 25.911 86.937 1.00120.36 N ANISOU 1596 N LEU A 201 12634 18580 14519 2481 -59 -1674 N ATOM 1597 CA LEU A 201 37.754 26.772 86.235 1.00111.49 C ANISOU 1597 CA LEU A 201 11530 17562 13269 2395 -86 -1649 C ATOM 1598 C LEU A 201 37.168 26.156 84.962 1.00101.36 C ANISOU 1598 C LEU A 201 10196 16342 11975 2373 -78 -1744 C ATOM 1599 O LEU A 201 37.830 25.398 84.252 1.00 99.54 O ANISOU 1599 O LEU A 201 9904 16117 11801 2422 -46 -1850 O ATOM 1600 CB LEU A 201 38.412 28.117 85.929 1.00103.93 C ANISOU 1600 CB LEU A 201 10580 16706 12201 2372 -96 -1612 C ATOM 1601 CG LEU A 201 37.352 29.214 86.053 1.00 95.96 C ANISOU 1601 CG LEU A 201 9630 15748 11085 2296 -123 -1516 C ATOM 1602 CD1 LEU A 201 36.775 29.271 87.442 1.00 79.46 C ANISOU 1602 CD1 LEU A 201 7602 13561 9030 2287 -133 -1430 C ATOM 1603 CD2 LEU A 201 37.888 30.555 85.669 1.00105.78 C ANISOU 1603 CD2 LEU A 201 10875 17082 12233 2274 -124 -1473 C ATOM 1604 N SER A 202 35.914 26.492 84.685 1.00 83.40 N ANISOU 1604 N SER A 202 7942 14123 9624 2301 -102 -1711 N ATOM 1605 CA SER A 202 35.256 26.061 83.472 1.00 79.39 C ANISOU 1605 CA SER A 202 7381 13703 9078 2268 -101 -1798 C ATOM 1606 C SER A 202 34.592 27.269 82.839 1.00 83.90 C ANISOU 1606 C SER A 202 7971 14422 9486 2200 -130 -1740 C ATOM 1607 O SER A 202 34.810 28.394 83.278 1.00 89.55 O ANISOU 1607 O SER A 202 8736 15155 10135 2189 -141 -1641 O ATOM 1608 CB SER A 202 34.249 24.950 83.761 1.00 77.82 C ANISOU 1608 CB SER A 202 7169 13419 8978 2256 -92 -1829 C ATOM 1609 OG SER A 202 33.071 25.462 84.352 1.00 56.97 O ANISOU 1609 OG SER A 202 4575 10784 6287 2197 -119 -1730 O ATOM 1610 N VAL A 203 33.788 27.043 81.805 1.00 81.26 N ANISOU 1610 N VAL A 203 7593 14196 9087 2157 -138 -1800 N ATOM 1611 CA VAL A 203 33.136 28.142 81.109 1.00 73.92 C ANISOU 1611 CA VAL A 203 6671 13419 7996 2103 -161 -1740 C ATOM 1612 C VAL A 203 31.819 28.504 81.794 1.00 65.59 C ANISOU 1612 C VAL A 203 5664 12345 6910 2058 -178 -1640 C ATOM 1613 O VAL A 203 31.515 29.688 81.999 1.00 78.46 O ANISOU 1613 O VAL A 203 7342 14022 8449 2038 -186 -1527 O ATOM 1614 CB VAL A 203 33.008 27.772 79.592 1.00 62.86 C ANISOU 1614 CB VAL A 203 5187 12176 6521 2083 -159 -1857 C ATOM 1615 CG1 VAL A 203 32.223 28.812 78.809 1.00 63.23 C ANISOU 1615 CG1 VAL A 203 5232 12399 6394 2031 -180 -1789 C ATOM 1616 CG2 VAL A 203 34.419 27.645 79.010 1.00 55.89 C ANISOU 1616 CG2 VAL A 203 4258 11318 5661 2133 -132 -1935 C ATOM 1617 N VAL A 204 31.045 27.498 82.182 1.00 60.04 N ANISOU 1617 N VAL A 204 4946 11570 6296 2045 -177 -1679 N ATOM 1618 CA VAL A 204 29.819 27.801 82.904 1.00 65.62 C ANISOU 1618 CA VAL A 204 5690 12259 6985 2004 -188 -1583 C ATOM 1619 C VAL A 204 30.173 28.596 84.170 1.00 85.31 C ANISOU 1619 C VAL A 204 8263 14655 9497 2026 -185 -1462 C ATOM 1620 O VAL A 204 29.366 29.389 84.668 1.00104.22 O ANISOU 1620 O VAL A 204 10698 17069 11834 1998 -190 -1360 O ATOM 1621 CB VAL A 204 29.068 26.520 83.213 1.00 65.67 C ANISOU 1621 CB VAL A 204 5655 12188 7110 1990 -179 -1643 C ATOM 1622 CG1 VAL A 204 28.337 26.054 81.968 1.00 85.60 C ANISOU 1622 CG1 VAL A 204 8099 14849 9575 1943 -185 -1745 C ATOM 1623 CG2 VAL A 204 30.048 25.458 83.630 1.00 72.67 C ANISOU 1623 CG2 VAL A 204 6527 12928 8157 2050 -154 -1714 C ATOM 1624 N ASP A 205 31.395 28.411 84.671 1.00 83.41 N ANISOU 1624 N ASP A 205 8038 14321 9334 2077 -174 -1479 N ATOM 1625 CA ASP A 205 31.803 29.062 85.913 1.00 96.10 C ANISOU 1625 CA ASP A 205 9709 15841 10962 2096 -172 -1382 C ATOM 1626 C ASP A 205 31.997 30.544 85.671 1.00 88.27 C ANISOU 1626 C ASP A 205 8751 14935 9852 2081 -176 -1306 C ATOM 1627 O ASP A 205 31.738 31.376 86.552 1.00 99.94 O ANISOU 1627 O ASP A 205 10283 16380 11310 2071 -175 -1210 O ATOM 1628 CB ASP A 205 33.087 28.444 86.476 1.00 99.16 C ANISOU 1628 CB ASP A 205 10093 16124 11460 2159 -157 -1423 C ATOM 1629 CG ASP A 205 32.870 27.038 87.039 1.00 98.25 C ANISOU 1629 CG ASP A 205 9953 15889 11489 2187 -142 -1464 C ATOM 1630 OD1 ASP A 205 31.693 26.644 87.261 1.00 74.70 O ANISOU 1630 OD1 ASP A 205 6966 12890 8528 2150 -145 -1443 O ATOM 1631 OD2 ASP A 205 33.888 26.331 87.256 1.00107.46 O1+ ANISOU 1631 OD2 ASP A 205 11098 16979 12754 2250 -123 -1513 O1+ ATOM 1632 N ILE A 206 32.459 30.885 84.482 1.00 67.69 N ANISOU 1632 N ILE A 206 6108 12438 7174 2080 -175 -1348 N ATOM 1633 CA ILE A 206 32.794 32.265 84.262 1.00 73.88 C ANISOU 1633 CA ILE A 206 6914 13288 7869 2073 -170 -1270 C ATOM 1634 C ILE A 206 31.554 32.964 83.694 1.00 74.86 C ANISOU 1634 C ILE A 206 7039 13519 7883 2032 -175 -1202 C ATOM 1635 O ILE A 206 31.430 34.199 83.700 1.00 67.65 O ANISOU 1635 O ILE A 206 6152 12646 6906 2023 -165 -1105 O ATOM 1636 CB ILE A 206 34.054 32.354 83.371 1.00 62.64 C ANISOU 1636 CB ILE A 206 5441 11926 6431 2099 -160 -1333 C ATOM 1637 CG1 ILE A 206 34.317 33.781 82.932 1.00 68.50 C ANISOU 1637 CG1 ILE A 206 6189 12753 7084 2087 -149 -1248 C ATOM 1638 CG2 ILE A 206 33.911 31.495 82.149 1.00 66.15 C ANISOU 1638 CG2 ILE A 206 5817 12463 6852 2096 -163 -1442 C ATOM 1639 CD1 ILE A 206 35.398 33.853 81.902 1.00 86.76 C ANISOU 1639 CD1 ILE A 206 8439 15154 9372 2105 -135 -1308 C ATOM 1640 N GLN A 207 30.588 32.159 83.274 1.00 69.61 N ANISOU 1640 N GLN A 207 6343 12897 7209 2008 -185 -1251 N ATOM 1641 CA GLN A 207 29.271 32.712 82.975 1.00 57.69 C ANISOU 1641 CA GLN A 207 4831 11481 5606 1972 -187 -1180 C ATOM 1642 C GLN A 207 28.571 33.068 84.267 1.00 64.97 C ANISOU 1642 C GLN A 207 5807 12310 6569 1965 -182 -1087 C ATOM 1643 O GLN A 207 27.973 34.154 84.397 1.00 57.77 O ANISOU 1643 O GLN A 207 4918 11439 5592 1957 -173 -982 O ATOM 1644 CB GLN A 207 28.433 31.725 82.171 1.00 61.19 C ANISOU 1644 CB GLN A 207 5211 12010 6030 1943 -199 -1268 C ATOM 1645 CG GLN A 207 28.965 31.460 80.792 1.00 66.62 C ANISOU 1645 CG GLN A 207 5835 12823 6653 1943 -204 -1363 C ATOM 1646 CD GLN A 207 28.334 30.239 80.176 1.00 78.67 C ANISOU 1646 CD GLN A 207 7292 14402 8197 1915 -214 -1486 C ATOM 1647 OE1 GLN A 207 27.817 29.376 80.880 1.00 79.76 O ANISOU 1647 OE1 GLN A 207 7428 14439 8438 1904 -215 -1515 O ATOM 1648 NE2 GLN A 207 28.377 30.153 78.852 1.00 89.85 N ANISOU 1648 NE2 GLN A 207 8641 15981 9515 1899 -220 -1560 N ATOM 1649 N GLU A 208 28.653 32.136 85.221 1.00 81.62 N ANISOU 1649 N GLU A 208 7929 14294 8789 1974 -185 -1123 N ATOM 1650 CA GLU A 208 28.132 32.347 86.565 1.00 66.47 C ANISOU 1650 CA GLU A 208 6057 12282 6917 1971 -179 -1044 C ATOM 1651 C GLU A 208 28.733 33.609 87.111 1.00 52.19 C ANISOU 1651 C GLU A 208 4299 10448 5081 1988 -170 -964 C ATOM 1652 O GLU A 208 28.043 34.483 87.630 1.00 48.92 O ANISOU 1652 O GLU A 208 3913 10040 4633 1978 -161 -874 O ATOM 1653 CB GLU A 208 28.458 31.162 87.469 1.00 65.64 C ANISOU 1653 CB GLU A 208 5953 12047 6941 1990 -180 -1093 C ATOM 1654 CG GLU A 208 27.277 30.237 87.732 1.00 89.19 C ANISOU 1654 CG GLU A 208 8901 15012 9975 1962 -180 -1102 C ATOM 1655 CD GLU A 208 27.461 29.377 88.979 1.00122.55 C ANISOU 1655 CD GLU A 208 13137 19095 14330 1983 -171 -1097 C ATOM 1656 OE1 GLU A 208 28.402 29.634 89.775 1.00122.48 O ANISOU 1656 OE1 GLU A 208 13171 19011 14352 2019 -167 -1072 O ATOM 1657 OE2 GLU A 208 26.650 28.441 89.161 1.00136.41 O1+ ANISOU 1657 OE2 GLU A 208 14850 20821 16158 1964 -166 -1114 O1+ ATOM 1658 N THR A 209 30.038 33.713 86.960 1.00 45.65 N ANISOU 1658 N THR A 209 3474 9595 4275 2015 -169 -1002 N ATOM 1659 CA THR A 209 30.743 34.853 87.496 1.00 42.48 C ANISOU 1659 CA THR A 209 3110 9164 3868 2028 -158 -940 C ATOM 1660 C THR A 209 30.361 36.171 86.826 1.00 47.87 C ANISOU 1660 C THR A 209 3790 9937 4462 2014 -146 -859 C ATOM 1661 O THR A 209 30.285 37.200 87.483 1.00 42.05 O ANISOU 1661 O THR A 209 3083 9167 3726 2015 -134 -781 O ATOM 1662 CB THR A 209 32.240 34.617 87.407 1.00 43.51 C ANISOU 1662 CB THR A 209 3226 9261 4044 2059 -158 -1003 C ATOM 1663 OG1 THR A 209 32.555 33.529 88.281 1.00 51.63 O ANISOU 1663 OG1 THR A 209 4260 10191 5165 2082 -164 -1051 O ATOM 1664 CG2 THR A 209 33.016 35.844 87.818 1.00 42.67 C ANISOU 1664 CG2 THR A 209 3141 9139 3933 2066 -146 -947 C ATOM 1665 N LEU A 210 30.102 36.167 85.521 1.00 67.20 N ANISOU 1665 N LEU A 210 6194 12502 6836 2004 -147 -876 N ATOM 1666 CA LEU A 210 29.866 37.451 84.845 1.00 58.72 C ANISOU 1666 CA LEU A 210 5109 11516 5684 2001 -130 -786 C ATOM 1667 C LEU A 210 28.391 37.918 84.884 1.00 49.31 C ANISOU 1667 C LEU A 210 3918 10376 4441 1985 -123 -701 C ATOM 1668 O LEU A 210 28.085 39.134 84.843 1.00 43.20 O ANISOU 1668 O LEU A 210 3147 9628 3640 1991 -104 -598 O ATOM 1669 CB LEU A 210 30.378 37.388 83.409 1.00 52.70 C ANISOU 1669 CB LEU A 210 4293 10875 4855 2003 -129 -827 C ATOM 1670 CG LEU A 210 31.780 37.985 83.198 1.00 64.37 C ANISOU 1670 CG LEU A 210 5760 12342 6357 2021 -114 -829 C ATOM 1671 CD1 LEU A 210 31.844 39.419 83.678 1.00 64.99 C ANISOU 1671 CD1 LEU A 210 5861 12381 6451 2024 -91 -714 C ATOM 1672 CD2 LEU A 210 32.878 37.175 83.852 1.00 57.65 C ANISOU 1672 CD2 LEU A 210 4916 11390 5597 2040 -123 -922 C ATOM 1673 N GLN A 211 27.494 36.942 85.010 1.00 43.04 N ANISOU 1673 N GLN A 211 3113 9592 3649 1968 -137 -743 N ATOM 1674 CA GLN A 211 26.060 37.179 85.015 1.00 43.15 C ANISOU 1674 CA GLN A 211 3109 9669 3616 1952 -133 -677 C ATOM 1675 C GLN A 211 25.576 38.372 85.887 1.00 66.45 C ANISOU 1675 C GLN A 211 6091 12575 6581 1964 -114 -562 C ATOM 1676 O GLN A 211 24.834 39.227 85.415 1.00 50.98 O ANISOU 1676 O GLN A 211 4106 10700 4564 1968 -99 -476 O ATOM 1677 CB GLN A 211 25.365 35.879 85.413 1.00 49.15 C ANISOU 1677 CB GLN A 211 3853 10402 4419 1930 -148 -745 C ATOM 1678 CG GLN A 211 23.845 35.934 85.520 1.00 55.86 C ANISOU 1678 CG GLN A 211 4672 11319 5234 1909 -145 -689 C ATOM 1679 CD GLN A 211 23.355 36.561 86.801 1.00 60.91 C ANISOU 1679 CD GLN A 211 5349 11880 5915 1919 -132 -605 C ATOM 1680 OE1 GLN A 211 23.684 36.112 87.897 1.00 81.96 O ANISOU 1680 OE1 GLN A 211 8052 14429 8662 1922 -135 -627 O ATOM 1681 NE2 GLN A 211 22.578 37.619 86.669 1.00 60.31 N ANISOU 1681 NE2 GLN A 211 5258 11873 5786 1927 -117 -507 N ATOM 1682 N PRO A 212 25.992 38.440 87.162 1.00 72.16 N ANISOU 1682 N PRO A 212 6864 13171 7384 1972 -113 -561 N ATOM 1683 CA PRO A 212 25.561 39.617 87.930 1.00 62.50 C ANISOU 1683 CA PRO A 212 5660 11912 6175 1985 -95 -465 C ATOM 1684 C PRO A 212 26.085 40.943 87.365 1.00 59.25 C ANISOU 1684 C PRO A 212 5240 11524 5749 2002 -76 -397 C ATOM 1685 O PRO A 212 25.393 41.936 87.551 1.00 63.43 O ANISOU 1685 O PRO A 212 5759 12065 6277 2015 -59 -308 O ATOM 1686 CB PRO A 212 26.144 39.364 89.301 1.00 53.14 C ANISOU 1686 CB PRO A 212 4522 10600 5068 1989 -101 -496 C ATOM 1687 CG PRO A 212 26.656 37.969 89.262 1.00 57.91 C ANISOU 1687 CG PRO A 212 5126 11174 5701 1981 -120 -594 C ATOM 1688 CD PRO A 212 26.988 37.650 87.902 1.00 58.81 C ANISOU 1688 CD PRO A 212 5204 11372 5770 1977 -125 -638 C ATOM 1689 N PHE A 213 27.261 40.985 86.730 1.00 48.32 N ANISOU 1689 N PHE A 213 3851 10143 4365 2006 -76 -433 N ATOM 1690 CA PHE A 213 27.688 42.239 86.109 1.00 42.62 C ANISOU 1690 CA PHE A 213 3106 9451 3636 2021 -53 -357 C ATOM 1691 C PHE A 213 26.772 42.538 84.950 1.00 63.20 C ANISOU 1691 C PHE A 213 5664 12197 6153 2024 -43 -291 C ATOM 1692 O PHE A 213 26.349 43.683 84.747 1.00 60.51 O ANISOU 1692 O PHE A 213 5299 11880 5811 2042 -21 -184 O ATOM 1693 CB PHE A 213 29.101 42.166 85.613 1.00 43.35 C ANISOU 1693 CB PHE A 213 3190 9537 3744 2023 -53 -410 C ATOM 1694 CG PHE A 213 30.125 42.152 86.686 1.00 62.90 C ANISOU 1694 CG PHE A 213 5700 11891 6309 2026 -57 -457 C ATOM 1695 CD1 PHE A 213 30.622 40.952 87.179 1.00 73.88 C ANISOU 1695 CD1 PHE A 213 7111 13234 7724 2023 -80 -557 C ATOM 1696 CD2 PHE A 213 30.653 43.335 87.159 1.00 70.29 C ANISOU 1696 CD2 PHE A 213 6635 12762 7308 2034 -38 -403 C ATOM 1697 CE1 PHE A 213 31.615 40.941 88.143 1.00 76.48 C ANISOU 1697 CE1 PHE A 213 7463 13469 8128 2030 -83 -596 C ATOM 1698 CE2 PHE A 213 31.642 43.329 88.119 1.00 72.26 C ANISOU 1698 CE2 PHE A 213 6905 12917 7633 2035 -44 -454 C ATOM 1699 CZ PHE A 213 32.121 42.130 88.610 1.00 74.07 C ANISOU 1699 CZ PHE A 213 7157 13114 7871 2035 -67 -548 C ATOM 1700 N LEU A 214 26.464 41.496 84.181 1.00 51.84 N ANISOU 1700 N LEU A 214 4200 10853 4644 2008 -60 -356 N ATOM 1701 CA LEU A 214 25.754 41.688 82.914 1.00 50.08 C ANISOU 1701 CA LEU A 214 3919 10793 4318 2008 -54 -306 C ATOM 1702 C LEU A 214 24.339 42.175 83.183 1.00 52.14 C ANISOU 1702 C LEU A 214 4159 11092 4560 2015 -44 -215 C ATOM 1703 O LEU A 214 23.910 43.134 82.566 1.00 59.92 O ANISOU 1703 O LEU A 214 5103 12157 5505 2035 -23 -109 O ATOM 1704 CB LEU A 214 25.796 40.414 82.054 1.00 51.45 C ANISOU 1704 CB LEU A 214 4061 11062 4424 1987 -77 -418 C ATOM 1705 CG LEU A 214 27.219 39.955 81.666 1.00 51.38 C ANISOU 1705 CG LEU A 214 4056 11032 4433 1988 -86 -510 C ATOM 1706 CD1 LEU A 214 27.219 38.626 80.935 1.00 45.19 C ANISOU 1706 CD1 LEU A 214 3237 10328 3606 1969 -111 -638 C ATOM 1707 CD2 LEU A 214 28.031 41.004 80.928 1.00 45.18 C ANISOU 1707 CD2 LEU A 214 3247 10297 3622 2005 -63 -441 C ATOM 1708 N SER A 215 23.648 41.550 84.145 1.00 57.51 N ANISOU 1708 N SER A 215 4861 11712 5279 2003 -57 -250 N ATOM 1709 CA SER A 215 22.275 41.915 84.504 1.00 55.66 C ANISOU 1709 CA SER A 215 4597 11516 5034 2010 -49 -174 C ATOM 1710 C SER A 215 22.200 43.234 85.210 1.00 48.26 C ANISOU 1710 C SER A 215 3674 10502 4160 2042 -28 -75 C ATOM 1711 O SER A 215 21.123 43.813 85.298 1.00 45.24 O ANISOU 1711 O SER A 215 3252 10168 3768 2061 -17 8 O ATOM 1712 CB SER A 215 21.643 40.848 85.407 1.00 47.36 C ANISOU 1712 CB SER A 215 3559 10419 4016 1985 -67 -241 C ATOM 1713 OG SER A 215 21.376 39.653 84.700 1.00 48.96 O ANISOU 1713 OG SER A 215 3725 10708 4171 1953 -86 -325 O ATOM 1714 N THR A 216 23.322 43.726 85.713 1.00 47.03 N ANISOU 1714 N THR A 216 3563 10230 4076 2050 -22 -86 N ATOM 1715 CA THR A 216 23.301 45.099 86.179 1.00 62.11 C ANISOU 1715 CA THR A 216 5470 12076 6054 2082 0 7 C ATOM 1716 C THR A 216 23.636 46.012 85.030 1.00 69.37 C ANISOU 1716 C THR A 216 6345 13064 6949 2102 22 91 C ATOM 1717 O THR A 216 23.725 47.229 85.222 1.00 62.93 O ANISOU 1717 O THR A 216 5512 12193 6204 2131 42 175 O ATOM 1718 CB THR A 216 24.346 45.393 87.274 1.00 73.77 C ANISOU 1718 CB THR A 216 7000 13399 7629 2081 0 -35 C ATOM 1719 OG1 THR A 216 25.630 44.901 86.854 1.00 84.42 O ANISOU 1719 OG1 THR A 216 8368 14732 8975 2064 -8 -107 O ATOM 1720 CG2 THR A 216 23.951 44.794 88.615 1.00 71.31 C ANISOU 1720 CG2 THR A 216 6729 13015 7353 2071 -16 -88 C ATOM 1721 N GLY A 217 23.880 45.413 83.860 1.00 73.89 N ANISOU 1721 N GLY A 217 6892 13752 7429 2087 16 63 N ATOM 1722 CA GLY A 217 24.029 46.141 82.614 1.00 55.26 C ANISOU 1722 CA GLY A 217 4477 11501 5017 2105 36 152 C ATOM 1723 C GLY A 217 25.418 46.687 82.378 1.00 56.76 C ANISOU 1723 C GLY A 217 4677 11632 5258 2107 51 154 C ATOM 1724 O GLY A 217 25.588 47.857 82.036 1.00 63.49 O ANISOU 1724 O GLY A 217 5493 12480 6151 2133 77 262 O ATOM 1725 N THR A 218 26.426 45.848 82.535 1.00 52.91 N ANISOU 1725 N THR A 218 4225 11100 4777 2082 33 37 N ATOM 1726 CA THR A 218 27.782 46.320 82.320 1.00 56.09 C ANISOU 1726 CA THR A 218 4624 11456 5231 2083 47 32 C ATOM 1727 C THR A 218 28.091 46.332 80.827 1.00 69.03 C ANISOU 1727 C THR A 218 6205 13252 6770 2084 57 62 C ATOM 1728 O THR A 218 27.689 45.426 80.071 1.00 68.83 O ANISOU 1728 O THR A 218 6162 13356 6634 2071 39 10 O ATOM 1729 CB THR A 218 28.837 45.485 83.099 1.00 95.76 C ANISOU 1729 CB THR A 218 9697 16376 10311 2062 27 -101 C ATOM 1730 OG1 THR A 218 28.619 44.093 82.866 1.00110.22 O ANISOU 1730 OG1 THR A 218 11541 18266 12071 2045 -3 -205 O ATOM 1731 CG2 THR A 218 28.728 45.733 84.605 1.00 81.59 C ANISOU 1731 CG2 THR A 218 7951 14431 8619 2063 22 -112 C ATOM 1732 N ILE A 219 28.794 47.364 80.384 1.00 76.62 N ANISOU 1732 N ILE A 219 7129 14210 7773 2097 87 145 N ATOM 1733 CA ILE A 219 29.280 47.373 79.007 1.00 71.38 C ANISOU 1733 CA ILE A 219 6407 13699 7017 2096 98 171 C ATOM 1734 C ILE A 219 30.554 46.549 78.922 1.00 66.49 C ANISOU 1734 C ILE A 219 5796 13066 6401 2075 85 37 C ATOM 1735 O ILE A 219 31.549 46.900 79.548 1.00 84.61 O ANISOU 1735 O ILE A 219 8103 15241 8806 2072 96 12 O ATOM 1736 CB ILE A 219 29.557 48.775 78.490 1.00 61.56 C ANISOU 1736 CB ILE A 219 5106 12467 5819 2118 139 321 C ATOM 1737 CG1 ILE A 219 28.283 49.614 78.525 1.00 61.81 C ANISOU 1737 CG1 ILE A 219 5115 12514 5857 2149 153 460 C ATOM 1738 CG2 ILE A 219 30.021 48.685 77.092 1.00 69.61 C ANISOU 1738 CG2 ILE A 219 6062 13662 6726 2114 150 347 C ATOM 1739 CD1 ILE A 219 28.507 51.083 78.219 1.00 56.63 C ANISOU 1739 CD1 ILE A 219 4401 11828 5288 2177 193 616 C ATOM 1740 N LEU A 220 30.538 45.444 78.194 1.00 51.55 N ANISOU 1740 N LEU A 220 3891 11296 4400 2062 60 -58 N ATOM 1741 CA LEU A 220 31.795 44.772 77.924 1.00 68.04 C ANISOU 1741 CA LEU A 220 5965 13391 6494 2051 52 -175 C ATOM 1742 C LEU A 220 32.644 45.581 76.958 1.00 74.95 C ANISOU 1742 C LEU A 220 6770 14355 7353 2055 86 -103 C ATOM 1743 O LEU A 220 32.135 46.325 76.133 1.00 78.02 O ANISOU 1743 O LEU A 220 7112 14860 7673 2065 107 23 O ATOM 1744 CB LEU A 220 31.550 43.379 77.360 1.00 67.72 C ANISOU 1744 CB LEU A 220 5918 13457 6357 2037 17 -305 C ATOM 1745 CG LEU A 220 30.860 42.487 78.375 1.00 57.45 C ANISOU 1745 CG LEU A 220 4679 12052 5096 2029 -14 -384 C ATOM 1746 CD1 LEU A 220 30.690 41.078 77.894 1.00 48.94 C ANISOU 1746 CD1 LEU A 220 3585 11053 3957 2014 -47 -524 C ATOM 1747 CD2 LEU A 220 31.727 42.518 79.599 1.00 64.11 C ANISOU 1747 CD2 LEU A 220 5571 12712 6074 2032 -12 -426 C ATOM 1748 N VAL A 221 33.950 45.432 77.056 1.00 63.81 N ANISOU 1748 N VAL A 221 5341 12898 6005 2050 96 -178 N ATOM 1749 CA VAL A 221 34.857 46.164 76.198 1.00 69.87 C ANISOU 1749 CA VAL A 221 6031 13746 6771 2049 134 -118 C ATOM 1750 C VAL A 221 35.928 45.185 75.735 1.00 72.10 C ANISOU 1750 C VAL A 221 6276 14091 7028 2041 126 -266 C ATOM 1751 O VAL A 221 36.304 44.275 76.455 1.00 65.86 O ANISOU 1751 O VAL A 221 5526 13209 6290 2040 102 -396 O ATOM 1752 CB VAL A 221 35.504 47.356 76.968 1.00 75.59 C ANISOU 1752 CB VAL A 221 6751 14319 7651 2051 172 -40 C ATOM 1753 CG1 VAL A 221 36.688 47.958 76.212 1.00 83.77 C ANISOU 1753 CG1 VAL A 221 7698 15419 8713 2042 218 -9 C ATOM 1754 CG2 VAL A 221 34.448 48.417 77.303 1.00 59.32 C ANISOU 1754 CG2 VAL A 221 4708 12202 5626 2065 185 110 C ATOM 1755 N GLY A 222 36.402 45.345 74.511 1.00 88.50 N ANISOU 1755 N GLY A 222 8268 16333 9024 2036 149 -245 N ATOM 1756 CA GLY A 222 37.403 44.434 73.989 1.00 88.57 C ANISOU 1756 CA GLY A 222 8225 16417 9009 2030 148 -391 C ATOM 1757 C GLY A 222 37.732 44.670 72.536 1.00 93.94 C ANISOU 1757 C GLY A 222 8803 17313 9577 2021 175 -355 C ATOM 1758 O GLY A 222 37.157 45.532 71.883 1.00 94.70 O ANISOU 1758 O GLY A 222 8868 17512 9603 2019 191 -206 O ATOM 1759 N HIS A 223 38.680 43.888 72.041 1.00 99.44 N ANISOU 1759 N HIS A 223 9440 18082 10261 2017 183 -492 N ATOM 1760 CA HIS A 223 39.178 44.021 70.686 1.00 79.43 C ANISOU 1760 CA HIS A 223 6795 15759 7626 2003 217 -484 C ATOM 1761 C HIS A 223 38.811 42.763 69.943 1.00 72.11 C ANISOU 1761 C HIS A 223 5843 14976 6581 1999 177 -628 C ATOM 1762 O HIS A 223 39.330 41.698 70.255 1.00 79.28 O ANISOU 1762 O HIS A 223 6756 15824 7544 2008 165 -796 O ATOM 1763 CB HIS A 223 40.685 44.248 70.692 1.00 80.56 C ANISOU 1763 CB HIS A 223 6868 15877 7865 1997 278 -531 C ATOM 1764 CG HIS A 223 41.235 44.664 69.364 1.00109.56 C ANISOU 1764 CG HIS A 223 10417 19761 11448 1975 332 -488 C ATOM 1765 ND1 HIS A 223 41.278 45.972 68.956 1.00115.06 N ANISOU 1765 ND1 HIS A 223 11065 20508 12144 1959 380 -307 N ATOM 1766 CD2 HIS A 223 41.761 43.925 68.347 1.00122.20 C ANISOU 1766 CD2 HIS A 223 11929 21540 12962 1964 351 -607 C ATOM 1767 CE1 HIS A 223 41.815 46.035 67.741 1.00124.03 C ANISOU 1767 CE1 HIS A 223 12087 21852 13188 1935 427 -306 C ATOM 1768 NE2 HIS A 223 42.116 44.808 67.361 1.00120.13 N ANISOU 1768 NE2 HIS A 223 11566 21440 12636 1937 412 -492 N ATOM 1769 N SER A 224 37.916 42.889 68.969 1.00 72.77 N ANISOU 1769 N SER A 224 5891 15249 6509 1986 157 -561 N ATOM 1770 CA SER A 224 37.359 41.737 68.253 1.00 88.27 C ANISOU 1770 CA SER A 224 7825 17360 8352 1974 113 -696 C ATOM 1771 C SER A 224 36.705 40.852 69.299 1.00 85.14 C ANISOU 1771 C SER A 224 7529 16794 8027 1985 64 -793 C ATOM 1772 O SER A 224 36.840 39.618 69.325 1.00 66.83 O ANISOU 1772 O SER A 224 5203 14459 5729 1984 40 -972 O ATOM 1773 CB SER A 224 38.436 40.995 67.461 1.00106.98 C ANISOU 1773 CB SER A 224 10094 19844 10707 1964 141 -856 C ATOM 1774 OG SER A 224 39.028 41.859 66.504 1.00121.48 O ANISOU 1774 OG SER A 224 11832 21846 12478 1947 196 -757 O ATOM 1775 N LEU A 225 35.967 41.537 70.156 1.00 91.00 N ANISOU 1775 N LEU A 225 8356 17407 8813 1994 57 -665 N ATOM 1776 CA LEU A 225 35.418 40.959 71.368 1.00 85.67 C ANISOU 1776 CA LEU A 225 7780 16541 8231 2003 25 -720 C ATOM 1777 C LEU A 225 34.577 39.712 71.091 1.00 89.42 C ANISOU 1777 C LEU A 225 8255 17085 8635 1988 -23 -853 C ATOM 1778 O LEU A 225 34.381 38.885 71.991 1.00 87.79 O ANISOU 1778 O LEU A 225 8108 16728 8519 1993 -47 -948 O ATOM 1779 CB LEU A 225 34.586 42.011 72.103 1.00 80.27 C ANISOU 1779 CB LEU A 225 7165 15757 7577 2011 33 -547 C ATOM 1780 CG LEU A 225 33.973 41.602 73.439 1.00 72.39 C ANISOU 1780 CG LEU A 225 6265 14564 6676 2016 8 -579 C ATOM 1781 CD1 LEU A 225 35.072 41.623 74.490 1.00 68.26 C ANISOU 1781 CD1 LEU A 225 5779 13848 6311 2027 23 -626 C ATOM 1782 CD2 LEU A 225 32.777 42.486 73.812 1.00 66.88 C ANISOU 1782 CD2 LEU A 225 5609 13840 5961 2020 15 -421 C ATOM 1783 N ASN A 226 34.121 39.561 69.845 1.00 86.36 N ANISOU 1783 N ASN A 226 7790 16931 8090 1967 -34 -863 N ATOM 1784 CA ASN A 226 33.240 38.452 69.499 1.00 83.22 C ANISOU 1784 CA ASN A 226 7378 16622 7621 1943 -77 -990 C ATOM 1785 C ASN A 226 33.926 37.100 69.512 1.00 71.81 C ANISOU 1785 C ASN A 226 5903 15126 6254 1942 -90 -1209 C ATOM 1786 O ASN A 226 33.275 36.072 69.673 1.00 71.10 O ANISOU 1786 O ASN A 226 5823 15015 6178 1926 -122 -1328 O ATOM 1787 CB ASN A 226 32.576 38.668 68.133 1.00 98.51 C ANISOU 1787 CB ASN A 226 9228 18846 9356 1915 -88 -947 C ATOM 1788 CG ASN A 226 33.572 38.892 67.012 1.00 99.18 C ANISOU 1788 CG ASN A 226 9208 19105 9372 1907 -65 -964 C ATOM 1789 OD1 ASN A 226 34.138 39.980 66.877 1.00 93.85 O ANISOU 1789 OD1 ASN A 226 8518 18441 8701 1922 -26 -819 O ATOM 1790 ND2 ASN A 226 33.766 37.872 66.180 1.00 90.01 N ANISOU 1790 ND2 ASN A 226 7962 18087 8152 1880 -82 -1142 N ATOM 1791 N ARG A 227 35.233 37.086 69.324 1.00 67.06 N ANISOU 1791 N ARG A 227 5257 14509 5715 1959 -56 -1263 N ATOM 1792 CA ARG A 227 35.906 35.807 69.251 1.00 82.34 C ANISOU 1792 CA ARG A 227 7151 16406 7730 1966 -53 -1468 C ATOM 1793 C ARG A 227 35.916 35.284 70.661 1.00 84.00 C ANISOU 1793 C ARG A 227 7456 16358 8103 1991 -66 -1502 C ATOM 1794 O ARG A 227 35.697 34.080 70.926 1.00 89.32 O ANISOU 1794 O ARG A 227 8133 16960 8845 1993 -84 -1645 O ATOM 1795 CB ARG A 227 37.320 35.951 68.680 1.00104.54 C ANISOU 1795 CB ARG A 227 9880 19276 10565 1982 2 -1515 C ATOM 1796 CG ARG A 227 37.361 36.316 67.178 1.00109.66 C ANISOU 1796 CG ARG A 227 10413 20203 11048 1951 21 -1501 C ATOM 1797 CD ARG A 227 36.794 35.201 66.299 1.00104.48 C ANISOU 1797 CD ARG A 227 9685 19704 10310 1918 -5 -1668 C ATOM 1798 NE ARG A 227 37.658 34.023 66.279 1.00115.38 N ANISOU 1798 NE ARG A 227 11020 21015 11803 1939 32 -1876 N ATOM 1799 CZ ARG A 227 37.215 32.774 66.165 1.00112.61 C ANISOU 1799 CZ ARG A 227 10649 20654 11485 1927 15 -2049 C ATOM 1800 NH1 ARG A 227 35.913 32.535 66.061 1.00 98.14 N1+ ANISOU 1800 NH1 ARG A 227 8831 18884 9572 1886 -44 -2047 N1+ ATOM 1801 NH2 ARG A 227 38.074 31.764 66.162 1.00114.46 N ANISOU 1801 NH2 ARG A 227 10843 20811 11837 1958 68 -2226 N ATOM 1802 N ASP A 228 36.137 36.249 71.558 1.00 88.60 N ANISOU 1802 N ASP A 228 8110 16808 8746 2008 -52 -1362 N ATOM 1803 CA ASP A 228 36.046 36.081 72.999 1.00 70.58 C ANISOU 1803 CA ASP A 228 5924 14295 6598 2026 -64 -1346 C ATOM 1804 C ASP A 228 34.670 35.576 73.389 1.00 64.28 C ANISOU 1804 C ASP A 228 5178 13465 5781 2006 -103 -1351 C ATOM 1805 O ASP A 228 34.554 34.458 73.854 1.00 64.78 O ANISOU 1805 O ASP A 228 5254 13432 5927 2010 -120 -1468 O ATOM 1806 CB ASP A 228 36.375 37.393 73.697 1.00 62.95 C ANISOU 1806 CB ASP A 228 5008 13238 5672 2035 -39 -1186 C ATOM 1807 CG ASP A 228 37.816 37.853 73.446 1.00 84.06 C ANISOU 1807 CG ASP A 228 7625 15925 8390 2052 7 -1191 C ATOM 1808 OD1 ASP A 228 38.723 36.990 73.337 1.00 92.46 O1+ ANISOU 1808 OD1 ASP A 228 8643 16976 9513 2071 20 -1329 O1+ ATOM 1809 OD2 ASP A 228 38.050 39.084 73.360 1.00 94.38 O ANISOU 1809 OD2 ASP A 228 8924 17254 9681 2046 37 -1055 O ATOM 1810 N LEU A 229 33.628 36.377 73.171 1.00 62.11 N ANISOU 1810 N LEU A 229 4922 13275 5401 1985 -110 -1221 N ATOM 1811 CA LEU A 229 32.272 35.984 73.575 1.00 60.23 C ANISOU 1811 CA LEU A 229 4725 13015 5145 1965 -138 -1215 C ATOM 1812 C LEU A 229 31.977 34.599 73.059 1.00 59.76 C ANISOU 1812 C LEU A 229 4612 13018 5077 1943 -163 -1392 C ATOM 1813 O LEU A 229 31.402 33.771 73.740 1.00 76.40 O ANISOU 1813 O LEU A 229 6751 15017 7261 1934 -181 -1456 O ATOM 1814 CB LEU A 229 31.217 36.972 73.041 1.00 52.92 C ANISOU 1814 CB LEU A 229 3791 12235 4080 1949 -133 -1065 C ATOM 1815 CG LEU A 229 31.376 38.466 73.394 1.00 57.04 C ANISOU 1815 CG LEU A 229 4350 12711 4611 1970 -99 -874 C ATOM 1816 CD1 LEU A 229 30.054 39.226 73.315 1.00 54.50 C ANISOU 1816 CD1 LEU A 229 4039 12464 4205 1963 -92 -728 C ATOM 1817 CD2 LEU A 229 32.005 38.656 74.759 1.00 56.58 C ANISOU 1817 CD2 LEU A 229 4367 12416 4714 1990 -89 -860 C ATOM 1818 N GLU A 230 32.427 34.354 71.845 1.00 77.68 N ANISOU 1818 N GLU A 230 6790 15462 7262 1933 -161 -1475 N ATOM 1819 CA GLU A 230 32.162 33.115 71.153 1.00 87.57 C ANISOU 1819 CA GLU A 230 7970 16806 8496 1906 -179 -1654 C ATOM 1820 C GLU A 230 32.781 31.924 71.865 1.00 66.98 C ANISOU 1820 C GLU A 230 5375 14008 6068 1930 -173 -1800 C ATOM 1821 O GLU A 230 32.141 30.880 71.992 1.00 67.17 O ANISOU 1821 O GLU A 230 5385 13995 6142 1909 -189 -1910 O ATOM 1822 CB GLU A 230 32.674 33.181 69.708 1.00 96.74 C ANISOU 1822 CB GLU A 230 9022 18202 9534 1890 -169 -1713 C ATOM 1823 CG GLU A 230 32.033 32.194 68.755 1.00101.09 C ANISOU 1823 CG GLU A 230 9483 18923 10005 1841 -191 -1872 C ATOM 1824 CD GLU A 230 32.438 32.449 67.315 1.00137.70 C ANISOU 1824 CD GLU A 230 14007 23822 14493 1818 -181 -1904 C ATOM 1825 OE1 GLU A 230 32.642 31.467 66.566 1.00155.21 O ANISOU 1825 OE1 GLU A 230 16131 26133 16710 1792 -175 -2091 O ATOM 1826 OE2 GLU A 230 32.560 33.635 66.935 1.00148.73 O1+ ANISOU 1826 OE2 GLU A 230 15401 25329 15780 1825 -172 -1742 O1+ ATOM 1827 N VAL A 231 34.022 32.054 72.320 1.00 62.18 N ANISOU 1827 N VAL A 231 4783 13281 5563 1975 -145 -1799 N ATOM 1828 CA VAL A 231 34.563 30.961 73.124 1.00 66.10 C ANISOU 1828 CA VAL A 231 5296 13585 6235 2009 -134 -1911 C ATOM 1829 C VAL A 231 33.861 30.915 74.513 1.00 86.86 C ANISOU 1829 C VAL A 231 8025 16025 8954 2010 -155 -1833 C ATOM 1830 O VAL A 231 33.575 29.824 75.019 1.00 84.97 O ANISOU 1830 O VAL A 231 7790 15672 8824 2014 -159 -1922 O ATOM 1831 CB VAL A 231 36.109 31.104 73.290 1.00 62.34 C ANISOU 1831 CB VAL A 231 4804 13041 5841 2061 -92 -1929 C ATOM 1832 CG1 VAL A 231 36.457 32.161 74.336 1.00 64.66 C ANISOU 1832 CG1 VAL A 231 5181 13216 6172 2078 -91 -1774 C ATOM 1833 CG2 VAL A 231 36.714 29.776 73.675 1.00 63.14 C ANISOU 1833 CG2 VAL A 231 4884 13006 6099 2104 -69 -2078 C ATOM 1834 N LEU A 232 33.540 32.084 75.088 1.00 87.16 N ANISOU 1834 N LEU A 232 8133 16037 8948 2005 -160 -1667 N ATOM 1835 CA LEU A 232 32.859 32.199 76.399 1.00 79.85 C ANISOU 1835 CA LEU A 232 7295 14951 8094 2003 -172 -1581 C ATOM 1836 C LEU A 232 31.390 31.788 76.359 1.00 57.10 C ANISOU 1836 C LEU A 232 4414 12113 5169 1961 -194 -1586 C ATOM 1837 O LEU A 232 30.789 31.559 77.402 1.00 59.60 O ANISOU 1837 O LEU A 232 4784 12299 5562 1957 -200 -1549 O ATOM 1838 CB LEU A 232 32.924 33.635 76.945 1.00 82.41 C ANISOU 1838 CB LEU A 232 7681 15245 8385 2008 -160 -1410 C ATOM 1839 CG LEU A 232 34.248 34.260 77.369 1.00 63.86 C ANISOU 1839 CG LEU A 232 5346 12819 6098 2041 -135 -1373 C ATOM 1840 CD1 LEU A 232 34.038 35.690 77.809 1.00 51.98 C ANISOU 1840 CD1 LEU A 232 3892 11298 4561 2035 -122 -1208 C ATOM 1841 CD2 LEU A 232 34.811 33.434 78.466 1.00 61.37 C ANISOU 1841 CD2 LEU A 232 5063 12325 5928 2069 -137 -1437 C ATOM 1842 N LYS A 233 30.814 31.734 75.165 1.00 57.26 N ANISOU 1842 N LYS A 233 4366 12329 5061 1928 -203 -1627 N ATOM 1843 CA LYS A 233 29.427 31.329 74.997 1.00 60.68 C ANISOU 1843 CA LYS A 233 4779 12835 5440 1883 -221 -1643 C ATOM 1844 C LYS A 233 28.463 32.274 75.714 1.00 55.11 C ANISOU 1844 C LYS A 233 4138 12102 4698 1875 -218 -1475 C ATOM 1845 O LYS A 233 27.413 31.863 76.220 1.00 55.05 O ANISOU 1845 O LYS A 233 4139 12058 4719 1849 -225 -1471 O ATOM 1846 CB LYS A 233 29.231 29.881 75.429 1.00 65.15 C ANISOU 1846 CB LYS A 233 5325 13285 6144 1872 -227 -1785 C ATOM 1847 CG LYS A 233 30.071 28.949 74.568 1.00 70.12 C ANISOU 1847 CG LYS A 233 5875 13961 6808 1881 -218 -1961 C ATOM 1848 CD LYS A 233 29.426 27.603 74.362 1.00 70.48 C ANISOU 1848 CD LYS A 233 5857 14000 6921 1844 -220 -2116 C ATOM 1849 CE LYS A 233 30.516 26.565 74.145 1.00 70.53 C ANISOU 1849 CE LYS A 233 5816 13923 7058 1883 -188 -2274 C ATOM 1850 NZ LYS A 233 30.016 25.179 74.371 1.00 78.79 N1+ ANISOU 1850 NZ LYS A 233 6822 14870 8243 1865 -171 -2408 N1+ ATOM 1851 N ILE A 234 28.828 33.550 75.694 1.00 53.75 N ANISOU 1851 N ILE A 234 3999 11956 4468 1898 -201 -1338 N ATOM 1852 CA ILE A 234 28.028 34.636 76.247 1.00 58.16 C ANISOU 1852 CA ILE A 234 4607 12498 4992 1900 -188 -1170 C ATOM 1853 C ILE A 234 27.547 35.546 75.117 1.00 57.99 C ANISOU 1853 C ILE A 234 4536 12693 4805 1892 -177 -1075 C ATOM 1854 O ILE A 234 28.330 35.994 74.268 1.00 50.83 O ANISOU 1854 O ILE A 234 3594 11889 3831 1903 -168 -1066 O ATOM 1855 CB ILE A 234 28.888 35.451 77.286 1.00 64.74 C ANISOU 1855 CB ILE A 234 5516 13160 5923 1936 -169 -1078 C ATOM 1856 CG1 ILE A 234 29.223 34.588 78.502 1.00 55.35 C ANISOU 1856 CG1 ILE A 234 4373 11771 4886 1945 -178 -1149 C ATOM 1857 CG2 ILE A 234 28.220 36.764 77.703 1.00 53.08 C ANISOU 1857 CG2 ILE A 234 4076 11678 4413 1942 -147 -904 C ATOM 1858 CD1 ILE A 234 30.493 34.987 79.152 1.00 56.12 C ANISOU 1858 CD1 ILE A 234 4511 11744 5069 1977 -165 -1131 C ATOM 1859 N ASP A 235 26.255 35.826 75.113 1.00 57.58 N ANISOU 1859 N ASP A 235 4473 12716 4689 1873 -173 -998 N ATOM 1860 CA ASP A 235 25.707 36.721 74.114 1.00 60.77 C ANISOU 1860 CA ASP A 235 4826 13326 4939 1871 -156 -886 C ATOM 1861 C ASP A 235 25.054 37.857 74.832 1.00 58.42 C ANISOU 1861 C ASP A 235 4569 12962 4665 1894 -130 -707 C ATOM 1862 O ASP A 235 24.025 37.676 75.460 1.00 60.74 O ANISOU 1862 O ASP A 235 4871 13216 4991 1882 -131 -685 O ATOM 1863 CB ASP A 235 24.712 36.048 73.175 1.00 79.60 C ANISOU 1863 CB ASP A 235 7125 15920 7201 1825 -170 -957 C ATOM 1864 CG ASP A 235 24.129 37.034 72.148 1.00 96.31 C ANISOU 1864 CG ASP A 235 9179 18265 9147 1826 -148 -819 C ATOM 1865 OD1 ASP A 235 24.858 37.960 71.705 1.00 96.65 O1+ ANISOU 1865 OD1 ASP A 235 9223 18350 9148 1857 -130 -721 O1+ ATOM 1866 OD2 ASP A 235 22.934 36.898 71.798 1.00109.54 O ANISOU 1866 OD2 ASP A 235 10798 20083 10741 1796 -145 -799 O ATOM 1867 N HIS A 236 25.720 38.986 74.853 1.00 56.05 N ANISOU 1867 N HIS A 236 4293 12628 4376 1927 -105 -589 N ATOM 1868 CA HIS A 236 25.254 40.114 75.594 1.00 56.66 C ANISOU 1868 CA HIS A 236 4407 12616 4505 1954 -78 -429 C ATOM 1869 C HIS A 236 25.335 41.351 74.752 1.00 61.24 C ANISOU 1869 C HIS A 236 4943 13320 5004 1977 -48 -277 C ATOM 1870 O HIS A 236 26.379 41.671 74.248 1.00 69.45 O ANISOU 1870 O HIS A 236 5972 14382 6032 1987 -39 -273 O ATOM 1871 CB HIS A 236 26.125 40.203 76.860 1.00 56.57 C ANISOU 1871 CB HIS A 236 4478 12367 4649 1969 -77 -450 C ATOM 1872 CG HIS A 236 26.013 41.498 77.596 1.00 65.78 C ANISOU 1872 CG HIS A 236 5679 13429 5884 1997 -48 -301 C ATOM 1873 ND1 HIS A 236 24.920 41.811 78.380 1.00 47.50 N ANISOU 1873 ND1 HIS A 236 3380 11061 3606 2002 -42 -231 N ATOM 1874 CD2 HIS A 236 26.857 42.549 77.673 1.00 61.15 C ANISOU 1874 CD2 HIS A 236 5104 12782 5348 2020 -23 -217 C ATOM 1875 CE1 HIS A 236 25.090 43.019 78.882 1.00 47.29 C ANISOU 1875 CE1 HIS A 236 3374 10946 3647 2030 -16 -114 C ATOM 1876 NE2 HIS A 236 26.254 43.493 78.476 1.00 57.05 N ANISOU 1876 NE2 HIS A 236 4608 12171 4897 2039 -3 -101 N ATOM 1877 N PRO A 237 24.155 42.101 74.660 1.00 56.96 N ANISOU 1877 N PRO A 237 4367 12855 4419 1990 -28 -136 N ATOM 1878 CA PRO A 237 24.253 43.245 73.749 1.00 64.86 C ANISOU 1878 CA PRO A 237 5314 13987 5344 2015 4 20 C ATOM 1879 C PRO A 237 25.240 44.360 74.002 1.00 63.36 C ANISOU 1879 C PRO A 237 5151 13680 5244 2047 31 121 C ATOM 1880 O PRO A 237 25.833 44.741 73.032 1.00 69.91 O ANISOU 1880 O PRO A 237 5932 14631 5999 2051 45 168 O ATOM 1881 CB PRO A 237 22.843 43.843 73.823 1.00 52.24 C ANISOU 1881 CB PRO A 237 3673 12453 3723 2031 20 152 C ATOM 1882 CG PRO A 237 22.275 43.332 75.122 1.00 55.68 C ANISOU 1882 CG PRO A 237 4166 12720 4268 2023 3 86 C ATOM 1883 CD PRO A 237 22.817 41.952 75.240 1.00 57.50 C ANISOU 1883 CD PRO A 237 4429 12915 4504 1984 -31 -109 C ATOM 1884 N LYS A 238 25.450 44.870 75.200 1.00 64.47 N ANISOU 1884 N LYS A 238 5356 13607 5535 2064 41 151 N ATOM 1885 CA LYS A 238 26.198 46.116 75.318 1.00 71.57 C ANISOU 1885 CA LYS A 238 6255 14419 6518 2092 74 270 C ATOM 1886 C LYS A 238 27.685 45.897 75.236 1.00 83.67 C ANISOU 1886 C LYS A 238 7804 15897 8090 2080 72 185 C ATOM 1887 O LYS A 238 28.300 45.496 76.176 1.00 88.40 O ANISOU 1887 O LYS A 238 8462 16335 8792 2071 60 88 O ATOM 1888 CB LYS A 238 25.856 46.819 76.643 1.00 58.04 C ANISOU 1888 CB LYS A 238 4591 12505 4955 2112 85 327 C ATOM 1889 CG LYS A 238 24.361 46.871 76.895 1.00 66.20 C ANISOU 1889 CG LYS A 238 5607 13581 5966 2125 82 384 C ATOM 1890 CD LYS A 238 24.001 47.440 78.254 1.00 73.71 C ANISOU 1890 CD LYS A 238 6603 14343 7060 2144 87 415 C ATOM 1891 CE LYS A 238 24.461 48.874 78.395 1.00 79.90 C ANISOU 1891 CE LYS A 238 7371 15034 7952 2179 120 544 C ATOM 1892 NZ LYS A 238 23.957 49.412 79.687 1.00 90.19 N ANISOU 1892 NZ LYS A 238 8707 16175 9386 2199 121 564 N ATOM 1893 N VAL A 239 28.257 46.214 74.089 1.00 69.89 N ANISOU 1893 N VAL A 239 5995 14298 6261 2080 87 233 N ATOM 1894 CA VAL A 239 29.632 45.909 73.819 1.00 67.79 C ANISOU 1894 CA VAL A 239 5720 14022 6014 2067 86 143 C ATOM 1895 C VAL A 239 30.352 47.071 73.212 1.00 61.92 C ANISOU 1895 C VAL A 239 4919 13318 5288 2081 126 279 C ATOM 1896 O VAL A 239 29.753 47.928 72.637 1.00 55.51 O ANISOU 1896 O VAL A 239 4061 12603 4428 2099 150 437 O ATOM 1897 CB VAL A 239 29.688 44.701 72.873 1.00 54.81 C ANISOU 1897 CB VAL A 239 4038 12556 4229 2043 53 7 C ATOM 1898 CG1 VAL A 239 29.224 43.440 73.591 1.00 54.39 C ANISOU 1898 CG1 VAL A 239 4040 12425 4201 2025 14 -151 C ATOM 1899 CG2 VAL A 239 28.777 44.956 71.713 1.00 56.68 C ANISOU 1899 CG2 VAL A 239 4203 13030 4301 2042 58 105 C ATOM 1900 N ILE A 240 31.657 47.088 73.390 1.00 59.73 N ANISOU 1900 N ILE A 240 4640 12962 5094 2073 137 217 N ATOM 1901 CA ILE A 240 32.543 48.069 72.780 1.00 62.69 C ANISOU 1901 CA ILE A 240 4947 13377 5497 2077 179 322 C ATOM 1902 C ILE A 240 33.657 47.325 72.091 1.00 85.26 C ANISOU 1902 C ILE A 240 7757 16334 8302 2055 175 194 C ATOM 1903 O ILE A 240 34.518 46.752 72.762 1.00 89.08 O ANISOU 1903 O ILE A 240 8271 16696 8878 2046 168 59 O ATOM 1904 CB ILE A 240 33.165 49.027 73.841 1.00 61.50 C ANISOU 1904 CB ILE A 240 4820 13001 5544 2084 212 372 C ATOM 1905 CG1 ILE A 240 32.098 49.696 74.677 1.00 69.46 C ANISOU 1905 CG1 ILE A 240 5874 13889 6628 2107 213 469 C ATOM 1906 CG2 ILE A 240 34.017 50.078 73.223 1.00 63.00 C ANISOU 1906 CG2 ILE A 240 4930 13227 5781 2084 261 486 C ATOM 1907 CD1 ILE A 240 31.153 50.473 73.901 1.00 81.06 C ANISOU 1907 CD1 ILE A 240 7292 15483 8024 2131 231 643 C ATOM 1908 N ASP A 241 33.667 47.315 70.761 1.00 98.59 N ANISOU 1908 N ASP A 241 9364 18253 9843 2048 179 235 N ATOM 1909 CA ASP A 241 34.785 46.675 70.102 1.00 93.22 C ANISOU 1909 CA ASP A 241 8624 17670 9126 2027 181 109 C ATOM 1910 C ASP A 241 35.779 47.709 69.644 1.00 93.81 C ANISOU 1910 C ASP A 241 8620 17771 9253 2022 239 218 C ATOM 1911 O ASP A 241 35.435 48.692 68.996 1.00102.83 O ANISOU 1911 O ASP A 241 9709 19014 10347 2028 266 399 O ATOM 1912 CB ASP A 241 34.306 45.824 68.924 1.00 82.21 C ANISOU 1912 CB ASP A 241 7175 16526 7535 2012 147 41 C ATOM 1913 CG ASP A 241 35.226 44.664 68.645 1.00 83.29 C ANISOU 1913 CG ASP A 241 7279 16703 7665 1994 131 -169 C ATOM 1914 OD1 ASP A 241 36.424 44.769 68.983 1.00 69.64 O ANISOU 1914 OD1 ASP A 241 5535 14873 6053 1994 165 -219 O ATOM 1915 OD2 ASP A 241 34.751 43.651 68.090 1.00100.39 O ANISOU 1915 OD2 ASP A 241 9425 19002 9715 1979 90 -289 O ATOM 1916 N THR A 242 37.025 47.453 70.016 1.00 95.08 N ANISOU 1916 N THR A 242 8768 17839 9521 2011 262 104 N ATOM 1917 CA THR A 242 38.131 48.373 69.834 1.00111.14 C ANISOU 1917 CA THR A 242 10727 19854 11647 1998 328 176 C ATOM 1918 C THR A 242 38.530 48.456 68.368 1.00118.63 C ANISOU 1918 C THR A 242 11556 21056 12460 1977 357 213 C ATOM 1919 O THR A 242 38.913 49.520 67.863 1.00111.76 O ANISOU 1919 O THR A 242 10609 20240 11614 1965 415 362 O ATOM 1920 CB THR A 242 39.343 47.909 70.649 1.00108.00 C ANISOU 1920 CB THR A 242 10341 19307 11389 1990 345 20 C ATOM 1921 OG1 THR A 242 38.905 47.496 71.946 1.00 94.06 O ANISOU 1921 OG1 THR A 242 8684 17343 9710 2006 302 -47 O ATOM 1922 CG2 THR A 242 40.375 49.010 70.769 1.00114.77 C ANISOU 1922 CG2 THR A 242 11129 20097 12380 1972 419 101 C ATOM 1923 N ALA A 243 38.451 47.327 67.695 1.00116.93 N ANISOU 1923 N ALA A 243 11319 20998 12112 1968 322 74 N ATOM 1924 CA ALA A 243 38.730 47.300 66.294 1.00109.36 C ANISOU 1924 CA ALA A 243 10244 20300 11006 1943 344 91 C ATOM 1925 C ALA A 243 37.728 48.200 65.634 1.00104.24 C ANISOU 1925 C ALA A 243 9570 19789 10246 1949 337 310 C ATOM 1926 O ALA A 243 38.076 49.116 64.932 1.00123.45 O ANISOU 1926 O ALA A 243 11916 22329 12659 1934 389 459 O ATOM 1927 CB ALA A 243 38.645 45.884 65.742 1.00102.49 C ANISOU 1927 CB ALA A 243 9355 19568 10018 1933 299 -110 C ATOM 1928 N LEU A 244 36.465 47.938 65.874 1.00 82.79 N ANISOU 1928 N LEU A 244 6925 17071 7459 1970 280 335 N ATOM 1929 CA LEU A 244 35.425 48.618 65.155 1.00 74.81 C ANISOU 1929 CA LEU A 244 5882 16227 6315 1979 271 530 C ATOM 1930 C LEU A 244 35.344 50.099 65.360 1.00 84.19 C ANISOU 1930 C LEU A 244 7058 17327 7602 2000 321 769 C ATOM 1931 O LEU A 244 34.972 50.799 64.456 1.00110.15 O ANISOU 1931 O LEU A 244 10272 20795 10784 2001 336 950 O ATOM 1932 CB LEU A 244 34.079 47.990 65.497 1.00 62.87 C ANISOU 1932 CB LEU A 244 4448 14713 4725 1995 213 491 C ATOM 1933 CG LEU A 244 33.660 46.753 64.696 1.00 73.55 C ANISOU 1933 CG LEU A 244 5767 16284 5895 1968 158 333 C ATOM 1934 CD1 LEU A 244 34.814 45.784 64.424 1.00 73.29 C ANISOU 1934 CD1 LEU A 244 5689 16278 5880 1940 154 114 C ATOM 1935 CD2 LEU A 244 32.520 46.020 65.377 1.00 82.00 C ANISOU 1935 CD2 LEU A 244 6927 17277 6954 1977 114 251 C ATOM 1936 N VAL A 245 35.578 50.576 66.563 1.00 88.50 N ANISOU 1936 N VAL A 245 7675 17602 8349 2017 344 777 N ATOM 1937 CA VAL A 245 35.381 51.991 66.842 1.00 96.65 C ANISOU 1937 CA VAL A 245 8695 18528 9501 2040 389 995 C ATOM 1938 C VAL A 245 36.303 53.010 66.207 1.00103.16 C ANISOU 1938 C VAL A 245 9411 19407 10380 2020 458 1131 C ATOM 1939 O VAL A 245 35.840 53.969 65.623 1.00110.85 O ANISOU 1939 O VAL A 245 10327 20469 11322 2035 481 1349 O ATOM 1940 CB VAL A 245 35.430 52.274 68.392 1.00 94.97 C ANISOU 1940 CB VAL A 245 8577 17997 9510 2057 395 949 C ATOM 1941 CG1 VAL A 245 34.134 51.851 69.066 1.00 81.05 C ANISOU 1941 CG1 VAL A 245 6910 16165 7720 2085 346 925 C ATOM 1942 CG2 VAL A 245 36.633 51.595 69.066 1.00 92.88 C ANISOU 1942 CG2 VAL A 245 8337 17602 9353 2031 400 743 C ATOM 1943 N PHE A 246 37.597 52.745 66.280 1.00112.51 N ANISOU 1943 N PHE A 246 10557 20550 11640 1984 495 1001 N ATOM 1944 CA PHE A 246 38.685 53.714 66.080 1.00117.40 C ANISOU 1944 CA PHE A 246 11084 21140 12385 1953 581 1088 C ATOM 1945 C PHE A 246 39.727 53.542 67.187 1.00116.69 C ANISOU 1945 C PHE A 246 11028 20819 12491 1936 610 926 C ATOM 1946 O PHE A 246 39.667 54.185 68.231 1.00111.94 O ANISOU 1946 O PHE A 246 10475 19989 12067 1951 619 961 O ATOM 1947 CB PHE A 246 38.268 55.190 65.953 1.00120.91 C ANISOU 1947 CB PHE A 246 11484 21546 12911 1970 623 1352 C ATOM 1948 CG PHE A 246 38.580 55.761 64.577 1.00141.51 C ANISOU 1948 CG PHE A 246 13958 24400 15409 1938 675 1512 C ATOM 1949 CD1 PHE A 246 37.767 55.461 63.482 1.00138.78 C ANISOU 1949 CD1 PHE A 246 13578 24326 14828 1948 630 1600 C ATOM 1950 CD2 PHE A 246 39.720 56.530 64.357 1.00148.64 C ANISOU 1950 CD2 PHE A 246 14763 25281 16434 1887 774 1563 C ATOM 1951 CE1 PHE A 246 38.061 55.949 62.209 1.00122.43 C ANISOU 1951 CE1 PHE A 246 11377 22500 12641 1911 676 1749 C ATOM 1952 CE2 PHE A 246 40.018 57.020 63.076 1.00130.63 C ANISOU 1952 CE2 PHE A 246 12354 23237 14043 1844 833 1711 C ATOM 1953 CZ PHE A 246 39.184 56.730 62.010 1.00118.16 C ANISOU 1953 CZ PHE A 246 10744 21928 12226 1858 781 1808 C ATOM 1954 N LYS A 253 38.885 52.921 54.792 1.00146.90 N ANISOU 1954 N LYS A 253 13698 27899 14219 1686 617 1630 N ATOM 1955 CA LYS A 253 39.656 51.725 55.087 1.00141.08 C ANISOU 1955 CA LYS A 253 13050 26943 13611 1634 660 1261 C ATOM 1956 C LYS A 253 38.805 50.672 55.777 1.00143.41 C ANISOU 1956 C LYS A 253 13486 27058 13946 1680 541 1066 C ATOM 1957 O LYS A 253 38.494 50.787 56.950 1.00130.32 O ANISOU 1957 O LYS A 253 11995 25010 12510 1720 521 1050 O ATOM 1958 CB LYS A 253 40.901 52.077 56.019 1.00 93.81 C ANISOU 1958 CB LYS A 253 7170 20508 7964 1597 798 1166 C ATOM 1959 N LEU A 254 38.426 49.647 55.030 1.00158.89 N ANISOU 1959 N LEU A 254 15371 29305 15696 1661 471 912 N ATOM 1960 CA LEU A 254 37.649 48.536 55.563 1.00147.01 C ANISOU 1960 CA LEU A 254 13979 27670 14208 1687 369 709 C ATOM 1961 C LEU A 254 38.382 47.728 56.628 1.00134.38 C ANISOU 1961 C LEU A 254 12554 25585 12920 1672 426 441 C ATOM 1962 O LEU A 254 37.769 47.246 57.569 1.00131.10 O ANISOU 1962 O LEU A 254 12257 24986 12568 1720 352 365 O ATOM 1963 CB LEU A 254 37.172 47.568 54.402 1.00117.36 C ANISOU 1963 CB LEU A 254 10063 24373 10155 1653 288 577 C ATOM 1964 N ARG A 255 39.684 47.547 56.453 1.00126.77 N ANISOU 1964 N ARG A 255 11539 24600 12026 1633 536 318 N ATOM 1965 CA ARG A 255 40.457 46.645 57.301 1.00128.85 C ANISOU 1965 CA ARG A 255 11871 24647 12441 1653 557 72 C ATOM 1966 C ARG A 255 40.476 47.072 58.768 1.00125.61 C ANISOU 1966 C ARG A 255 11591 23898 12238 1712 538 123 C ATOM 1967 O ARG A 255 40.570 48.252 59.076 1.00128.68 O ANISOU 1967 O ARG A 255 11989 24193 12710 1719 577 328 O ATOM 1968 CB ARG A 255 41.905 46.457 56.665 1.00 91.69 C ANISOU 1968 CB ARG A 255 7064 20029 7744 1596 701 -52 C ATOM 1969 CG ARG A 255 41.919 45.744 55.046 1.00124.21 C ANISOU 1969 CG ARG A 255 11047 24522 11624 1521 743 -169 C ATOM 1970 CD ARG A 255 43.228 46.113 53.967 1.00 97.86 C ANISOU 1970 CD ARG A 255 7589 21379 8215 1435 933 -172 C ATOM 1971 NE ARG A 255 44.247 46.829 54.811 1.00105.34 N ANISOU 1971 NE ARG A 255 8569 22093 9361 1449 1017 -112 N ATOM 1972 CZ ARG A 255 45.063 46.177 55.669 1.00119.00 C ANISOU 1972 CZ ARG A 255 10346 23614 11254 1487 1040 -306 C ATOM 1973 NH1 ARG A 255 44.943 44.809 55.677 1.00123.75 N ANISOU 1973 NH1 ARG A 255 10966 24224 11830 1514 993 -557 N ATOM 1974 NH2 ARG A 255 45.950 46.854 56.515 1.00120.44 N ANISOU 1974 NH2 ARG A 255 10552 23585 11625 1497 1107 -252 N ATOM 1975 N ARG A 256 40.389 46.097 59.667 1.00110.51 N ANISOU 1975 N ARG A 256 9775 21801 10414 1748 484 -68 N ATOM 1976 CA ARG A 256 40.347 46.368 61.096 1.00109.37 C ANISOU 1976 CA ARG A 256 9757 21342 10455 1796 463 -42 C ATOM 1977 C ARG A 256 41.735 46.381 61.696 1.00111.89 C ANISOU 1977 C ARG A 256 10070 21493 10949 1792 549 -139 C ATOM 1978 O ARG A 256 42.538 45.511 61.394 1.00128.61 O ANISOU 1978 O ARG A 256 12138 23665 13065 1778 588 -332 O ATOM 1979 CB ARG A 256 39.484 45.327 61.817 1.00118.64 C ANISOU 1979 CB ARG A 256 11040 22403 11634 1830 366 -182 C ATOM 1980 CG ARG A 256 38.014 45.690 61.863 1.00130.81 C ANISOU 1980 CG ARG A 256 12640 23985 13077 1849 289 -32 C ATOM 1981 CD ARG A 256 37.149 44.493 61.535 1.00132.50 C ANISOU 1981 CD ARG A 256 12863 24319 13163 1840 210 -188 C ATOM 1982 NE ARG A 256 37.401 43.380 62.447 1.00132.20 N ANISOU 1982 NE ARG A 256 12903 24078 13249 1856 188 -408 N ATOM 1983 CZ ARG A 256 37.036 42.123 62.215 1.00134.78 C ANISOU 1983 CZ ARG A 256 13220 24471 13519 1842 140 -606 C ATOM 1984 NH1 ARG A 256 37.308 41.175 63.104 1.00129.41 N ANISOU 1984 NH1 ARG A 256 12610 23587 12974 1861 128 -783 N ATOM 1985 NH2 ARG A 256 36.407 41.811 61.090 1.00141.82 N ANISOU 1985 NH2 ARG A 256 14024 25638 14224 1804 104 -626 N ATOM 1986 N PRO A 257 41.998 47.276 62.635 1.00 94.81 N ANISOU 1986 N PRO A 257 7961 19114 8948 1810 575 -25 N ATOM 1987 CA PRO A 257 43.340 47.473 63.179 1.00 85.23 C ANISOU 1987 CA PRO A 257 6723 17761 7900 1798 661 -91 C ATOM 1988 C PRO A 257 43.767 46.343 64.085 1.00 94.02 C ANISOU 1988 C PRO A 257 7904 18708 9112 1830 630 -314 C ATOM 1989 O PRO A 257 43.018 45.414 64.271 1.00108.88 O ANISOU 1989 O PRO A 257 9852 20577 10941 1856 547 -415 O ATOM 1990 CB PRO A 257 43.212 48.779 63.989 1.00 76.38 C ANISOU 1990 CB PRO A 257 5647 16452 6923 1807 679 103 C ATOM 1991 CG PRO A 257 42.076 49.509 63.327 1.00 82.60 C ANISOU 1991 CG PRO A 257 6425 17373 7587 1809 645 316 C ATOM 1992 CD PRO A 257 41.110 48.412 62.942 1.00 86.30 C ANISOU 1992 CD PRO A 257 6931 17971 7890 1829 550 213 C ATOM 1993 N SER A 258 45.002 46.362 64.551 1.00100.80 N ANISOU 1993 N SER A 258 8731 19464 10103 1823 701 -395 N ATOM 1994 CA SER A 258 45.450 45.385 65.526 1.00109.21 C ANISOU 1994 CA SER A 258 9859 20358 11277 1860 670 -580 C ATOM 1995 C SER A 258 45.795 46.146 66.778 1.00116.91 C ANISOU 1995 C SER A 258 10892 21097 12433 1870 678 -509 C ATOM 1996 O SER A 258 46.135 47.318 66.721 1.00117.18 O ANISOU 1996 O SER A 258 10878 21120 12526 1840 742 -366 O ATOM 1997 CB SER A 258 46.673 44.613 64.995 1.00111.28 C ANISOU 1997 CB SER A 258 10023 20725 11536 1852 748 -760 C ATOM 1998 OG SER A 258 47.272 43.835 66.019 1.00114.52 O ANISOU 1998 OG SER A 258 10480 20957 12075 1893 730 -911 O ATOM 1999 N LEU A 259 45.702 45.484 67.917 1.00119.91 N ANISOU 1999 N LEU A 259 11368 21287 12904 1908 618 -610 N ATOM 2000 CA LEU A 259 45.771 46.186 69.182 1.00112.36 C ANISOU 2000 CA LEU A 259 10481 20107 12105 1916 608 -539 C ATOM 2001 C LEU A 259 47.077 46.926 69.409 1.00110.47 C ANISOU 2001 C LEU A 259 10156 19826 11992 1888 701 -527 C ATOM 2002 O LEU A 259 47.073 48.091 69.769 1.00111.37 O ANISOU 2002 O LEU A 259 10265 19855 12197 1866 732 -389 O ATOM 2003 CB LEU A 259 45.525 45.186 70.331 1.00 97.34 C ANISOU 2003 CB LEU A 259 8687 18032 10263 1957 532 -667 C ATOM 2004 CG LEU A 259 45.176 45.623 71.765 1.00 82.20 C ANISOU 2004 CG LEU A 259 6875 15882 8473 1969 491 -614 C ATOM 2005 CD1 LEU A 259 44.200 46.796 71.836 1.00 75.32 C ANISOU 2005 CD1 LEU A 259 6043 14971 7602 1957 483 -422 C ATOM 2006 CD2 LEU A 259 44.581 44.432 72.512 1.00 82.45 C ANISOU 2006 CD2 LEU A 259 7011 15817 8500 2003 410 -730 C ATOM 2007 N ASN A 260 48.186 46.258 69.139 1.00101.33 N ANISOU 2007 N ASN A 260 8920 18740 10842 1889 752 -672 N ATOM 2008 CA ASN A 260 49.526 46.801 69.332 1.00104.83 C ANISOU 2008 CA ASN A 260 9267 19165 11398 1861 847 -688 C ATOM 2009 C ASN A 260 49.733 48.129 68.604 1.00114.08 C ANISOU 2009 C ASN A 260 10345 20429 12573 1800 939 -524 C ATOM 2010 O ASN A 260 50.538 48.966 69.022 1.00129.26 O ANISOU 2010 O ASN A 260 12208 22279 14625 1766 1008 -482 O ATOM 2011 CB ASN A 260 50.551 45.758 68.848 1.00113.40 C ANISOU 2011 CB ASN A 260 10269 20369 12449 1876 895 -871 C ATOM 2012 CG ASN A 260 51.916 45.893 69.518 1.00121.64 C ANISOU 2012 CG ASN A 260 11244 21345 13630 1874 959 -944 C ATOM 2013 OD1 ASN A 260 52.330 46.983 69.911 1.00130.41 O ANISOU 2013 OD1 ASN A 260 12318 22388 14844 1834 1008 -846 O ATOM 2014 ND2 ASN A 260 52.627 44.772 69.635 1.00122.59 N ANISOU 2014 ND2 ASN A 260 11337 21486 13755 1919 962 -1119 N ATOM 2015 N ASN A 261 48.997 48.321 67.516 1.00108.98 N ANISOU 2015 N ASN A 261 9678 19946 11783 1782 940 -429 N ATOM 2016 CA ASN A 261 49.167 49.512 66.707 1.00110.98 C ANISOU 2016 CA ASN A 261 9836 20309 12023 1722 1033 -263 C ATOM 2017 C ASN A 261 48.255 50.650 67.162 1.00109.50 C ANISOU 2017 C ASN A 261 9707 19994 11903 1721 1000 -64 C ATOM 2018 O ASN A 261 48.528 51.820 66.898 1.00113.62 O ANISOU 2018 O ASN A 261 10155 20524 12490 1673 1082 81 O ATOM 2019 CB ASN A 261 48.972 49.135 65.245 1.00120.42 C ANISOU 2019 CB ASN A 261 10960 21773 13021 1699 1063 -263 C ATOM 2020 CG ASN A 261 49.884 47.968 64.837 1.00124.74 C ANISOU 2020 CG ASN A 261 11447 22433 13516 1705 1104 -479 C ATOM 2021 OD1 ASN A 261 49.477 46.802 64.855 1.00128.38 O ANISOU 2021 OD1 ASN A 261 11962 22907 13908 1752 1028 -617 O ATOM 2022 ND2 ASN A 261 51.137 48.283 64.514 1.00120.75 N ANISOU 2022 ND2 ASN A 261 10824 22001 13054 1658 1230 -511 N ATOM 2023 N LEU A 262 47.202 50.270 67.853 1.00110.03 N ANISOU 2023 N LEU A 262 9902 19943 11961 1774 888 -66 N ATOM 2024 CA LEU A 262 46.295 51.238 68.382 1.00113.27 C ANISOU 2024 CA LEU A 262 10376 20222 12441 1786 854 102 C ATOM 2025 C LEU A 262 46.947 51.852 69.580 1.00127.16 C ANISOU 2025 C LEU A 262 12143 21759 14412 1776 883 88 C ATOM 2026 O LEU A 262 46.997 53.071 69.703 1.00138.48 O ANISOU 2026 O LEU A 262 13534 23122 15959 1747 936 228 O ATOM 2027 CB LEU A 262 44.934 50.611 68.723 1.00108.13 C ANISOU 2027 CB LEU A 262 9855 19529 11702 1839 737 98 C ATOM 2028 CG LEU A 262 43.851 50.819 67.653 1.00111.06 C ANISOU 2028 CG LEU A 262 10215 20083 11901 1844 710 238 C ATOM 2029 CD1 LEU A 262 42.527 50.149 68.041 1.00118.77 C ANISOU 2029 CD1 LEU A 262 11312 21020 12794 1890 603 218 C ATOM 2030 CD2 LEU A 262 43.630 52.299 67.397 1.00100.91 C ANISOU 2030 CD2 LEU A 262 8878 18789 10676 1826 764 468 C ATOM 2031 N CYS A 263 47.495 51.022 70.460 1.00127.52 N ANISOU 2031 N CYS A 263 12233 21701 14518 1797 851 -82 N ATOM 2032 CA CYS A 263 48.162 51.570 71.625 1.00127.17 C ANISOU 2032 CA CYS A 263 12188 21465 14668 1785 874 -105 C ATOM 2033 C CYS A 263 49.292 52.392 71.100 1.00133.17 C ANISOU 2033 C CYS A 263 12800 22294 15504 1722 997 -68 C ATOM 2034 O CYS A 263 49.388 53.576 71.364 1.00133.42 O ANISOU 2034 O CYS A 263 12790 22234 15670 1687 1049 45 O ATOM 2035 CB CYS A 263 48.690 50.454 72.531 1.00123.11 C ANISOU 2035 CB CYS A 263 11725 20869 14181 1818 824 -294 C ATOM 2036 SG CYS A 263 47.444 49.268 72.997 1.00129.21 S ANISOU 2036 SG CYS A 263 12655 21590 14847 1878 696 -360 S ATOM 2037 N LYS A 264 50.027 51.794 70.178 1.00136.29 N ANISOU 2037 N LYS A 264 13110 22876 15798 1704 1052 -149 N ATOM 2038 CA LYS A 264 51.227 52.396 69.655 1.00133.54 C ANISOU 2038 CA LYS A 264 12615 22618 15508 1636 1183 -141 C ATOM 2039 C LYS A 264 50.774 53.681 69.039 1.00128.70 C ANISOU 2039 C LYS A 264 11953 22036 14913 1587 1243 66 C ATOM 2040 O LYS A 264 51.380 54.722 69.215 1.00130.77 O ANISOU 2040 O LYS A 264 12131 22235 15321 1528 1334 135 O ATOM 2041 CB LYS A 264 51.906 51.524 68.591 1.00134.19 C ANISOU 2041 CB LYS A 264 12616 22925 15446 1625 1237 -251 C ATOM 2042 CG LYS A 264 52.715 52.320 67.581 1.00140.25 C ANISOU 2042 CG LYS A 264 13232 23852 16204 1539 1386 -174 C ATOM 2043 CD LYS A 264 52.727 51.651 66.199 1.00144.95 C ANISOU 2043 CD LYS A 264 13773 24708 16594 1528 1425 -210 C ATOM 2044 CE LYS A 264 52.986 52.667 65.082 1.00146.52 C ANISOU 2044 CE LYS A 264 13855 25070 16746 1434 1559 -56 C ATOM 2045 NZ LYS A 264 53.280 52.001 63.776 1.00141.97 N ANISOU 2045 NZ LYS A 264 13206 24763 15975 1409 1622 -120 N ATOM 2046 N SER A 265 49.661 53.606 68.346 1.00129.59 N ANISOU 2046 N SER A 265 12115 22241 14881 1613 1190 167 N ATOM 2047 CA SER A 265 49.051 54.801 67.842 1.00135.72 C ANISOU 2047 CA SER A 265 12859 23036 15670 1583 1228 383 C ATOM 2048 C SER A 265 48.579 55.720 68.968 1.00140.45 C ANISOU 2048 C SER A 265 13515 23389 16460 1601 1196 469 C ATOM 2049 O SER A 265 48.848 56.912 68.942 1.00134.68 O ANISOU 2049 O SER A 265 12708 22604 15863 1549 1280 591 O ATOM 2050 CB SER A 265 47.875 54.552 66.951 1.00142.33 C ANISOU 2050 CB SER A 265 13739 24027 16312 1617 1164 485 C ATOM 2051 OG SER A 265 47.371 55.802 66.512 1.00144.53 O ANISOU 2051 OG SER A 265 13975 24320 16620 1592 1208 713 O ATOM 2052 N ILE A 266 47.873 55.171 69.955 1.00145.56 N ANISOU 2052 N ILE A 266 14294 23889 17125 1667 1083 402 N ATOM 2053 CA ILE A 266 47.473 55.948 71.130 1.00134.78 C ANISOU 2053 CA ILE A 266 12983 22284 15941 1683 1053 451 C ATOM 2054 C ILE A 266 48.547 56.321 72.161 1.00142.08 C ANISOU 2054 C ILE A 266 13861 23046 17075 1647 1102 353 C ATOM 2055 O ILE A 266 48.602 57.450 72.615 1.00147.00 O ANISOU 2055 O ILE A 266 14443 23536 17876 1619 1146 434 O ATOM 2056 CB ILE A 266 46.334 55.251 71.889 1.00123.36 C ANISOU 2056 CB ILE A 266 11693 20740 14439 1755 927 412 C ATOM 2057 N LEU A 267 49.378 55.363 72.555 1.00143.49 N ANISOU 2057 N LEU A 267 14043 23237 17239 1651 1090 175 N ATOM 2058 CA LEU A 267 50.495 55.643 73.457 1.00136.42 C ANISOU 2058 CA LEU A 267 13087 22226 16520 1617 1136 77 C ATOM 2059 C LEU A 267 51.476 54.483 73.468 1.00127.46 C ANISOU 2059 C LEU A 267 11929 21185 15315 1626 1136 -100 C ATOM 2060 O LEU A 267 51.089 53.343 73.239 1.00124.40 O ANISOU 2060 O LEU A 267 11616 20874 14775 1677 1066 -175 O ATOM 2061 CB LEU A 267 49.993 55.923 74.878 1.00131.24 C ANISOU 2061 CB LEU A 267 12524 21340 16002 1649 1063 61 C ATOM 2062 N GLY A 268 52.723 54.735 73.830 1.00120.22 N ANISOU 2062 N GLY A 268 10907 20251 14518 1582 1211 -175 N ATOM 2063 CA GLY A 268 53.736 53.731 73.605 1.00123.00 C ANISOU 2063 CA GLY A 268 11207 20731 14797 1591 1231 -326 C ATOM 2064 C GLY A 268 53.401 52.427 74.290 1.00126.87 C ANISOU 2064 C GLY A 268 11821 21178 15207 1672 1112 -454 C ATOM 2065 O GLY A 268 53.042 52.403 75.453 1.00128.05 O ANISOU 2065 O GLY A 268 12059 21163 15431 1701 1037 -477 O ATOM 2066 N TYR A 269 53.528 51.340 73.542 1.00124.16 N ANISOU 2066 N TYR A 269 11475 20987 14712 1702 1102 -541 N ATOM 2067 CA TYR A 269 53.340 49.998 74.063 1.00121.25 C ANISOU 2067 CA TYR A 269 11203 20595 14273 1774 1005 -675 C ATOM 2068 C TYR A 269 54.552 49.157 73.703 1.00113.53 C ANISOU 2068 C TYR A 269 10126 19749 13261 1787 1055 -823 C ATOM 2069 O TYR A 269 54.744 48.798 72.547 1.00106.70 O ANISOU 2069 O TYR A 269 9196 19059 12287 1779 1108 -845 O ATOM 2070 CB TYR A 269 52.066 49.327 73.506 1.00120.98 C ANISOU 2070 CB TYR A 269 11276 20605 14087 1812 928 -649 C ATOM 2071 CG TYR A 269 51.961 47.808 73.757 1.00123.54 C ANISOU 2071 CG TYR A 269 11672 20938 14330 1877 850 -801 C ATOM 2072 CD1 TYR A 269 51.202 47.307 74.806 1.00108.36 C ANISOU 2072 CD1 TYR A 269 9884 18864 12425 1918 749 -826 C ATOM 2073 CD2 TYR A 269 52.608 46.882 72.929 1.00132.11 C ANISOU 2073 CD2 TYR A 269 12684 22183 15330 1895 886 -920 C ATOM 2074 CE1 TYR A 269 51.107 45.945 75.033 1.00109.27 C ANISOU 2074 CE1 TYR A 269 10055 18979 12482 1972 687 -956 C ATOM 2075 CE2 TYR A 269 52.521 45.524 73.158 1.00131.08 C ANISOU 2075 CE2 TYR A 269 12608 22045 15150 1956 823 -1057 C ATOM 2076 CZ TYR A 269 51.765 45.063 74.208 1.00127.26 C ANISOU 2076 CZ TYR A 269 12256 21403 14693 1993 723 -1071 C ATOM 2077 OH TYR A 269 51.669 43.712 74.435 1.00136.77 O ANISOU 2077 OH TYR A 269 13509 22593 15863 2050 668 -1201 O ATOM 2078 N GLY A 275 57.053 41.418 68.627 1.00111.26 N ANISOU 2078 N GLY A 275 9515 20405 12354 2074 1221 -1766 N ATOM 2079 CA GLY A 275 56.394 40.143 68.450 1.00117.23 C ANISOU 2079 CA GLY A 275 10339 21144 13057 2137 1158 -1878 C ATOM 2080 C GLY A 275 56.642 39.271 69.649 1.00123.61 C ANISOU 2080 C GLY A 275 11204 21783 13978 2223 1089 -1970 C ATOM 2081 O GLY A 275 57.681 38.652 69.761 1.00124.17 O ANISOU 2081 O GLY A 275 11192 21885 14101 2282 1143 -2092 O ATOM 2082 N VAL A 276 55.689 39.240 70.563 1.00133.51 N ANISOU 2082 N VAL A 276 12597 22861 15268 2231 975 -1906 N ATOM 2083 CA VAL A 276 55.861 38.515 71.808 1.00144.75 C ANISOU 2083 CA VAL A 276 14083 24117 16797 2303 908 -1968 C ATOM 2084 C VAL A 276 54.569 37.858 72.258 1.00149.89 C ANISOU 2084 C VAL A 276 14879 24637 17435 2324 798 -1959 C ATOM 2085 O VAL A 276 53.485 38.333 71.923 1.00151.77 O ANISOU 2085 O VAL A 276 15186 24880 17600 2271 757 -1862 O ATOM 2086 CB VAL A 276 56.388 39.457 72.936 1.00122.35 C ANISOU 2086 CB VAL A 276 11249 21176 14061 2281 895 -1882 C ATOM 2087 CG1 VAL A 276 57.868 39.250 73.157 1.00117.79 C ANISOU 2087 CG1 VAL A 276 10544 20656 13555 2326 968 -1978 C ATOM 2088 CG2 VAL A 276 56.084 40.920 72.619 1.00120.91 C ANISOU 2088 CG2 VAL A 276 11059 21027 13855 2186 923 -1725 C ATOM 2089 N PRO A 277 54.706 36.749 73.110 1.00137.81 N ANISOU 2089 N PRO A 277 13393 22983 15985 2405 753 -2056 N ATOM 2090 CA PRO A 277 53.438 36.030 73.328 1.00122.54 C ANISOU 2090 CA PRO A 277 11582 20949 14030 2416 666 -2058 C ATOM 2091 C PRO A 277 52.382 36.896 73.972 1.00109.88 C ANISOU 2091 C PRO A 277 10095 19242 12411 2356 588 -1907 C ATOM 2092 O PRO A 277 52.721 37.833 74.668 1.00115.36 O ANISOU 2092 O PRO A 277 10797 19882 13154 2329 587 -1819 O ATOM 2093 CB PRO A 277 53.840 34.880 74.267 1.00116.98 C ANISOU 2093 CB PRO A 277 10900 20117 13431 2509 640 -2158 C ATOM 2094 CG PRO A 277 55.136 35.321 74.883 1.00120.49 C ANISOU 2094 CG PRO A 277 11265 20565 13951 2534 682 -2160 C ATOM 2095 CD PRO A 277 55.832 36.131 73.827 1.00129.38 C ANISOU 2095 CD PRO A 277 12269 21871 15018 2486 776 -2151 C ATOM 2096 N HIS A 278 51.120 36.626 73.655 1.00113.91 N ANISOU 2096 N HIS A 278 10687 19742 12854 2333 533 -1882 N ATOM 2097 CA HIS A 278 49.981 37.423 74.125 1.00120.43 C ANISOU 2097 CA HIS A 278 11621 20487 13650 2280 466 -1740 C ATOM 2098 C HIS A 278 49.457 37.183 75.545 1.00114.25 C ANISOU 2098 C HIS A 278 10956 19511 12943 2299 390 -1708 C ATOM 2099 O HIS A 278 49.456 36.069 76.034 1.00121.46 O ANISOU 2099 O HIS A 278 11898 20344 13908 2352 363 -1800 O ATOM 2100 CB HIS A 278 48.782 37.367 73.178 1.00136.05 C ANISOU 2100 CB HIS A 278 13628 22556 15510 2244 439 -1710 C ATOM 2101 CG HIS A 278 49.005 38.065 71.874 1.00131.22 C ANISOU 2101 CG HIS A 278 12920 22139 14800 2201 504 -1673 C ATOM 2102 ND1 HIS A 278 47.999 38.288 70.969 1.00129.90 N ANISOU 2102 ND1 HIS A 278 12761 22085 14509 2161 485 -1618 N ATOM 2103 CD2 HIS A 278 50.134 38.587 71.329 1.00124.33 C ANISOU 2103 CD2 HIS A 278 11932 21378 13931 2190 593 -1679 C ATOM 2104 CE1 HIS A 278 48.491 38.920 69.913 1.00134.76 C ANISOU 2104 CE1 HIS A 278 13275 22876 15054 2128 558 -1586 C ATOM 2105 NE2 HIS A 278 49.780 39.110 70.111 1.00130.22 N ANISOU 2105 NE2 HIS A 278 12624 22298 14556 2142 629 -1624 N ATOM 2106 N ASP A 279 48.965 38.242 76.175 1.00104.42 N ANISOU 2106 N ASP A 279 9779 18193 11705 2255 362 -1576 N ATOM 2107 CA ASP A 279 48.548 38.203 77.568 1.00100.04 C ANISOU 2107 CA ASP A 279 9327 17467 11216 2264 302 -1538 C ATOM 2108 C ASP A 279 47.165 38.824 77.752 1.00 96.93 C ANISOU 2108 C ASP A 279 9035 17024 10772 2217 255 -1419 C ATOM 2109 O ASP A 279 47.021 40.030 77.726 1.00 97.23 O ANISOU 2109 O ASP A 279 9075 17068 10802 2176 272 -1306 O ATOM 2110 CB ASP A 279 49.573 38.927 78.443 1.00111.85 C ANISOU 2110 CB ASP A 279 10790 18907 12801 2265 327 -1512 C ATOM 2111 CG ASP A 279 49.119 39.063 79.886 1.00128.64 C ANISOU 2111 CG ASP A 279 13020 20874 14986 2265 270 -1463 C ATOM 2112 OD1 ASP A 279 48.722 38.038 80.483 1.00136.15 O ANISOU 2112 OD1 ASP A 279 14032 21744 15953 2302 225 -1516 O ATOM 2113 OD2 ASP A 279 49.150 40.195 80.420 1.00133.16 O1+ ANISOU 2113 OD2 ASP A 279 13605 21399 15590 2227 276 -1373 O1+ ATOM 2114 N CYS A 280 46.147 37.999 77.942 1.00100.76 N ANISOU 2114 N CYS A 280 9598 17457 11230 2227 202 -1444 N ATOM 2115 CA CYS A 280 44.761 38.469 77.928 1.00 96.13 C ANISOU 2115 CA CYS A 280 9093 16853 10578 2188 163 -1343 C ATOM 2116 C CYS A 280 44.442 39.517 78.999 1.00 97.62 C ANISOU 2116 C CYS A 280 9352 16926 10814 2163 149 -1225 C ATOM 2117 O CYS A 280 43.473 40.261 78.877 1.00103.06 O ANISOU 2117 O CYS A 280 10086 17619 11454 2131 138 -1119 O ATOM 2118 CB CYS A 280 43.805 37.281 78.091 1.00 86.03 C ANISOU 2118 CB CYS A 280 7876 15530 9283 2203 112 -1407 C ATOM 2119 SG CYS A 280 43.877 36.483 79.717 1.00 99.06 S ANISOU 2119 SG CYS A 280 9601 16990 11046 2239 76 -1447 S ATOM 2120 N VAL A 281 45.249 39.592 80.046 1.00 97.92 N ANISOU 2120 N VAL A 281 9392 16867 10945 2180 153 -1246 N ATOM 2121 CA VAL A 281 44.998 40.602 81.068 1.00 99.92 C ANISOU 2121 CA VAL A 281 9702 17016 11249 2155 144 -1149 C ATOM 2122 C VAL A 281 45.646 41.936 80.689 1.00101.96 C ANISOU 2122 C VAL A 281 9888 17319 11533 2126 198 -1074 C ATOM 2123 O VAL A 281 45.087 43.016 80.945 1.00103.38 O ANISOU 2123 O VAL A 281 10099 17451 11728 2095 203 -963 O ATOM 2124 CB VAL A 281 45.506 40.131 82.444 1.00 88.98 C ANISOU 2124 CB VAL A 281 8348 15513 9946 2184 120 -1202 C ATOM 2125 CG1 VAL A 281 45.019 41.061 83.553 1.00 88.05 C ANISOU 2125 CG1 VAL A 281 8297 15287 9869 2157 104 -1113 C ATOM 2126 CG2 VAL A 281 45.039 38.705 82.715 1.00 82.44 C ANISOU 2126 CG2 VAL A 281 7568 14646 9110 2219 80 -1280 C ATOM 2127 N HIS A 282 46.822 41.862 80.076 1.00 89.47 N ANISOU 2127 N HIS A 282 8203 15826 9967 2136 245 -1134 N ATOM 2128 CA HIS A 282 47.402 43.050 79.488 1.00 89.20 C ANISOU 2128 CA HIS A 282 8082 15856 9952 2103 307 -1063 C ATOM 2129 C HIS A 282 46.499 43.460 78.360 1.00101.71 C ANISOU 2129 C HIS A 282 9667 17535 11441 2078 316 -976 C ATOM 2130 O HIS A 282 46.271 44.646 78.164 1.00104.84 O ANISOU 2130 O HIS A 282 10048 17932 11856 2045 346 -857 O ATOM 2131 CB HIS A 282 48.821 42.808 78.998 1.00 89.39 C ANISOU 2131 CB HIS A 282 7985 15975 10003 2118 364 -1151 C ATOM 2132 CG HIS A 282 49.862 43.048 80.039 1.00108.41 C ANISOU 2132 CG HIS A 282 10359 18312 12519 2127 376 -1188 C ATOM 2133 ND1 HIS A 282 50.451 42.030 80.754 1.00113.41 N ANISOU 2133 ND1 HIS A 282 10995 18909 13185 2179 349 -1298 N ATOM 2134 CD2 HIS A 282 50.414 44.198 80.501 1.00118.66 C ANISOU 2134 CD2 HIS A 282 11611 19571 13903 2094 411 -1131 C ATOM 2135 CE1 HIS A 282 51.326 42.536 81.604 1.00116.97 C ANISOU 2135 CE1 HIS A 282 11404 19317 13723 2177 364 -1307 C ATOM 2136 NE2 HIS A 282 51.320 43.852 81.467 1.00120.28 N ANISOU 2136 NE2 HIS A 282 11792 19732 14178 2123 402 -1212 N ATOM 2137 N ASP A 283 45.982 42.468 77.630 1.00106.40 N ANISOU 2137 N ASP A 283 10274 18212 11941 2095 291 -1037 N ATOM 2138 CA ASP A 283 45.106 42.715 76.484 1.00103.57 C ANISOU 2138 CA ASP A 283 9908 17975 11469 2076 293 -967 C ATOM 2139 C ASP A 283 43.896 43.505 76.940 1.00 99.58 C ANISOU 2139 C ASP A 283 9489 17392 10957 2057 263 -834 C ATOM 2140 O ASP A 283 43.548 44.541 76.340 1.00104.64 O ANISOU 2140 O ASP A 283 10101 18090 11568 2034 293 -709 O ATOM 2141 CB ASP A 283 44.677 41.407 75.817 1.00104.17 C ANISOU 2141 CB ASP A 283 9987 18136 11455 2097 261 -1075 C ATOM 2142 CG ASP A 283 45.757 40.825 74.891 1.00115.01 C ANISOU 2142 CG ASP A 283 11246 19642 12809 2112 311 -1189 C ATOM 2143 OD1 ASP A 283 46.937 41.245 74.991 1.00108.70 O ANISOU 2143 OD1 ASP A 283 10373 18849 12077 2113 366 -1202 O ATOM 2144 OD2 ASP A 283 45.423 39.934 74.068 1.00126.11 O1+ ANISOU 2144 OD2 ASP A 283 12630 21151 14135 2123 299 -1272 O1+ ATOM 2145 N ALA A 284 43.284 43.005 78.023 1.00 77.58 N ANISOU 2145 N ALA A 284 6800 14475 8203 2070 211 -860 N ATOM 2146 CA ALA A 284 42.032 43.534 78.546 1.00 68.81 C ANISOU 2146 CA ALA A 284 5776 13288 7081 2058 181 -757 C ATOM 2147 C ALA A 284 42.266 44.922 79.069 1.00 84.11 C ANISOU 2147 C ALA A 284 7703 15145 9112 2040 215 -647 C ATOM 2148 O ALA A 284 41.480 45.836 78.820 1.00 66.67 O ANISOU 2148 O ALA A 284 5503 12941 6886 2028 226 -522 O ATOM 2149 CB ALA A 284 41.459 42.648 79.596 1.00 65.43 C ANISOU 2149 CB ALA A 284 5438 12748 6673 2072 128 -819 C ATOM 2150 N SER A 285 43.375 45.085 79.774 1.00105.09 N ANISOU 2150 N SER A 285 10327 17729 11872 2040 236 -698 N ATOM 2151 CA SER A 285 43.697 46.381 80.340 1.00109.30 C ANISOU 2151 CA SER A 285 10836 18176 12515 2020 270 -614 C ATOM 2152 C SER A 285 43.992 47.399 79.236 1.00 98.47 C ANISOU 2152 C SER A 285 9370 16900 11143 1998 333 -517 C ATOM 2153 O SER A 285 43.695 48.574 79.374 1.00 80.50 O ANISOU 2153 O SER A 285 7083 14567 8937 1981 359 -404 O ATOM 2154 CB SER A 285 44.882 46.265 81.307 1.00114.65 C ANISOU 2154 CB SER A 285 11487 18778 13297 2023 277 -702 C ATOM 2155 OG SER A 285 46.041 45.816 80.629 1.00133.50 O ANISOU 2155 OG SER A 285 13781 21268 15675 2031 312 -783 O ATOM 2156 N ALA A 286 44.564 46.933 78.134 1.00102.26 N ANISOU 2156 N ALA A 286 9776 17528 11550 1999 360 -562 N ATOM 2157 CA ALA A 286 44.949 47.809 77.027 1.00100.84 C ANISOU 2157 CA ALA A 286 9493 17462 11360 1974 427 -475 C ATOM 2158 C ALA A 286 43.709 48.302 76.305 1.00101.06 C ANISOU 2158 C ALA A 286 9547 17552 11299 1973 416 -340 C ATOM 2159 O ALA A 286 43.565 49.497 75.988 1.00111.65 O ANISOU 2159 O ALA A 286 10843 18893 12685 1956 459 -203 O ATOM 2160 CB ALA A 286 45.878 47.082 76.077 1.00 83.36 C ANISOU 2160 CB ALA A 286 7190 15403 9082 1976 461 -573 C ATOM 2161 N ALA A 287 42.815 47.350 76.057 1.00 79.53 N ANISOU 2161 N ALA A 287 6887 14881 8452 1993 360 -381 N ATOM 2162 CA ALA A 287 41.512 47.641 75.490 1.00 88.26 C ANISOU 2162 CA ALA A 287 8025 16052 9457 1998 338 -267 C ATOM 2163 C ALA A 287 40.771 48.654 76.370 1.00101.13 C ANISOU 2163 C ALA A 287 9711 17533 11180 2000 334 -149 C ATOM 2164 O ALA A 287 40.293 49.711 75.886 1.00 99.85 O ANISOU 2164 O ALA A 287 9517 17402 11022 1998 363 3 O ATOM 2165 CB ALA A 287 40.703 46.361 75.319 1.00 82.58 C ANISOU 2165 CB ALA A 287 7369 15392 8617 2015 276 -358 C ATOM 2166 N MET A 288 40.694 48.333 77.663 1.00 91.76 N ANISOU 2166 N MET A 288 8602 16189 10073 2006 301 -218 N ATOM 2167 CA MET A 288 40.045 49.207 78.620 1.00 96.28 C ANISOU 2167 CA MET A 288 9224 16614 10744 2008 297 -133 C ATOM 2168 C MET A 288 40.676 50.597 78.567 1.00106.69 C ANISOU 2168 C MET A 288 10461 17883 12193 1992 358 -36 C ATOM 2169 O MET A 288 39.977 51.616 78.579 1.00105.15 O ANISOU 2169 O MET A 288 10262 17643 12048 1998 373 94 O ATOM 2170 CB MET A 288 40.119 48.628 80.040 1.00 86.59 C ANISOU 2170 CB MET A 288 8074 15241 9584 2011 257 -237 C ATOM 2171 CG MET A 288 39.664 49.593 81.107 1.00 78.53 C ANISOU 2171 CG MET A 288 7087 14068 8682 2009 260 -170 C ATOM 2172 SD MET A 288 37.989 50.202 80.824 1.00 71.36 S ANISOU 2172 SD MET A 288 6218 13174 7722 2027 251 -25 S ATOM 2173 CE MET A 288 37.018 48.727 81.210 1.00 79.26 C ANISOU 2173 CE MET A 288 7318 14198 8597 2036 188 -118 C ATOM 2174 N LYS A 289 41.996 50.632 78.462 1.00102.65 N ANISOU 2174 N LYS A 289 9874 17386 11744 1973 397 -99 N ATOM 2175 CA LYS A 289 42.725 51.885 78.545 1.00 97.57 C ANISOU 2175 CA LYS A 289 9142 16680 11251 1949 461 -31 C ATOM 2176 C LYS A 289 42.389 52.769 77.345 1.00104.08 C ANISOU 2176 C LYS A 289 9894 17609 12042 1944 507 124 C ATOM 2177 O LYS A 289 42.276 53.992 77.473 1.00105.42 O ANISOU 2177 O LYS A 289 10020 17698 12335 1936 546 236 O ATOM 2178 CB LYS A 289 44.229 51.619 78.621 1.00 84.60 C ANISOU 2178 CB LYS A 289 7422 15056 9667 1927 498 -142 C ATOM 2179 CG LYS A 289 44.984 52.627 79.454 1.00 85.62 C ANISOU 2179 CG LYS A 289 7493 15051 9988 1901 540 -137 C ATOM 2180 CD LYS A 289 46.478 52.370 79.408 1.00101.63 C ANISOU 2180 CD LYS A 289 9427 17126 12061 1878 585 -241 C ATOM 2181 CE LYS A 289 46.807 50.933 79.753 1.00107.77 C ANISOU 2181 CE LYS A 289 10259 17942 12746 1905 532 -389 C ATOM 2182 NZ LYS A 289 48.242 50.644 79.449 1.00116.66 N1+ ANISOU 2182 NZ LYS A 289 11278 19153 13895 1891 583 -482 N1+ ATOM 2183 N LEU A 290 42.213 52.143 76.185 1.00104.02 N ANISOU 2183 N LEU A 290 9868 17784 11870 1949 503 130 N ATOM 2184 CA LEU A 290 41.802 52.885 74.999 1.00 96.37 C ANISOU 2184 CA LEU A 290 8834 16946 10838 1948 540 288 C ATOM 2185 C LEU A 290 40.382 53.431 75.147 1.00 91.23 C ANISOU 2185 C LEU A 290 8244 16250 10171 1979 508 422 C ATOM 2186 O LEU A 290 40.092 54.596 74.814 1.00 85.13 O ANISOU 2186 O LEU A 290 7417 15466 9461 1983 547 581 O ATOM 2187 CB LEU A 290 41.877 51.991 73.761 1.00 91.94 C ANISOU 2187 CB LEU A 290 8239 16607 10087 1947 534 248 C ATOM 2188 CG LEU A 290 43.283 51.588 73.327 1.00101.89 C ANISOU 2188 CG LEU A 290 9408 17951 11354 1917 584 137 C ATOM 2189 CD1 LEU A 290 43.227 50.534 72.244 1.00107.64 C ANISOU 2189 CD1 LEU A 290 10116 18887 11895 1922 565 64 C ATOM 2190 CD2 LEU A 290 44.030 52.805 72.840 1.00103.10 C ANISOU 2190 CD2 LEU A 290 9441 18127 11604 1880 676 247 C ATOM 2191 N ALA A 291 39.494 52.575 75.643 1.00 88.59 N ANISOU 2191 N ALA A 291 8013 15892 9755 2002 442 358 N ATOM 2192 CA ALA A 291 38.110 52.976 75.861 1.00 95.06 C ANISOU 2192 CA ALA A 291 8889 16674 10554 2032 415 467 C ATOM 2193 C ALA A 291 38.039 54.204 76.775 1.00100.18 C ANISOU 2193 C ALA A 291 9531 17132 11401 2037 440 543 C ATOM 2194 O ALA A 291 37.332 55.180 76.498 1.00 84.26 O ANISOU 2194 O ALA A 291 7487 15108 9419 2060 458 698 O ATOM 2195 CB ALA A 291 37.322 51.818 76.440 1.00 97.22 C ANISOU 2195 CB ALA A 291 9268 16932 10739 2044 350 359 C ATOM 2196 N LEU A 292 38.799 54.159 77.861 1.00108.60 N ANISOU 2196 N LEU A 292 10614 18049 12602 2018 440 431 N ATOM 2197 CA LEU A 292 38.810 55.263 78.809 1.00107.85 C ANISOU 2197 CA LEU A 292 10505 17769 12704 2019 460 471 C ATOM 2198 C LEU A 292 39.379 56.488 78.131 1.00102.60 C ANISOU 2198 C LEU A 292 9723 17113 12149 2007 529 590 C ATOM 2199 O LEU A 292 38.827 57.592 78.232 1.00 98.77 O ANISOU 2199 O LEU A 292 9209 16547 11773 2027 548 711 O ATOM 2200 CB LEU A 292 39.636 54.917 80.039 1.00100.64 C ANISOU 2200 CB LEU A 292 9619 16724 11897 1997 446 320 C ATOM 2201 CG LEU A 292 39.194 53.661 80.771 1.00 86.09 C ANISOU 2201 CG LEU A 292 7885 14870 9953 2006 382 201 C ATOM 2202 CD1 LEU A 292 40.202 53.343 81.854 1.00 80.63 C ANISOU 2202 CD1 LEU A 292 7201 14078 9356 1985 374 65 C ATOM 2203 CD2 LEU A 292 37.795 53.862 81.329 1.00 86.27 C ANISOU 2203 CD2 LEU A 292 7981 14829 9969 2033 348 259 C ATOM 2204 N ALA A 293 40.487 56.259 77.435 1.00 94.30 N ANISOU 2204 N ALA A 293 8597 16163 11070 1974 569 551 N ATOM 2205 CA ALA A 293 41.132 57.272 76.617 1.00103.81 C ANISOU 2205 CA ALA A 293 9677 17414 12353 1950 646 659 C ATOM 2206 C ALA A 293 40.114 58.090 75.842 1.00109.02 C ANISOU 2206 C ALA A 293 10313 18132 12976 1984 655 859 C ATOM 2207 O ALA A 293 40.092 59.309 75.967 1.00110.33 O ANISOU 2207 O ALA A 293 10417 18199 13305 1987 696 965 O ATOM 2208 CB ALA A 293 42.142 56.638 75.678 1.00 88.59 C ANISOU 2208 CB ALA A 293 7682 15657 10319 1915 681 600 C ATOM 2209 N VAL A 294 39.247 57.438 75.072 1.00 96.80 N ANISOU 2209 N VAL A 294 8811 16744 11223 2012 616 911 N ATOM 2210 CA VAL A 294 38.253 58.231 74.357 1.00100.73 C ANISOU 2210 CA VAL A 294 9282 17309 11682 2050 623 1115 C ATOM 2211 C VAL A 294 37.269 58.867 75.329 1.00104.71 C ANISOU 2211 C VAL A 294 9841 17635 12310 2093 597 1162 C ATOM 2212 O VAL A 294 36.937 60.043 75.175 1.00107.95 O ANISOU 2212 O VAL A 294 10193 17990 12832 2119 627 1316 O ATOM 2213 CB VAL A 294 37.461 57.421 73.289 1.00 95.58 C ANISOU 2213 CB VAL A 294 8655 16888 10774 2070 587 1163 C ATOM 2214 CG1 VAL A 294 36.958 56.123 73.831 1.00 97.02 C ANISOU 2214 CG1 VAL A 294 8947 17072 10843 2077 519 1006 C ATOM 2215 CG2 VAL A 294 36.287 58.233 72.755 1.00 89.74 C ANISOU 2215 CG2 VAL A 294 7895 16203 9999 2119 586 1376 C ATOM 2216 N VAL A 295 36.828 58.124 76.344 1.00 99.02 N ANISOU 2216 N VAL A 295 9222 16822 11578 2100 542 1030 N ATOM 2217 CA VAL A 295 35.738 58.637 77.170 1.00114.14 C ANISOU 2217 CA VAL A 295 11187 18604 13579 2142 516 1075 C ATOM 2218 C VAL A 295 36.081 59.945 77.883 1.00126.14 C ANISOU 2218 C VAL A 295 12648 19927 15353 2147 551 1111 C ATOM 2219 O VAL A 295 35.320 60.909 77.795 1.00137.34 O ANISOU 2219 O VAL A 295 14035 21297 16849 2193 559 1249 O ATOM 2220 CB VAL A 295 35.270 57.599 78.185 1.00116.94 C ANISOU 2220 CB VAL A 295 11653 18899 13879 2139 458 923 C ATOM 2221 CG1 VAL A 295 34.268 58.224 79.137 1.00119.13 C ANISOU 2221 CG1 VAL A 295 11964 19030 14269 2177 439 957 C ATOM 2222 CG2 VAL A 295 34.618 56.444 77.457 1.00121.21 C ANISOU 2222 CG2 VAL A 295 12243 19626 14184 2145 422 907 C ATOM 2223 N GLU A 296 37.220 60.019 78.541 1.00119.73 N ANISOU 2223 N GLU A 296 11809 19007 14677 2103 572 988 N ATOM 2224 CA GLU A 296 37.563 61.256 79.217 1.00121.07 C ANISOU 2224 CA GLU A 296 11912 18993 15097 2103 605 1002 C ATOM 2225 C GLU A 296 38.127 62.309 78.268 1.00128.80 C ANISOU 2225 C GLU A 296 12765 20010 16164 2094 676 1140 C ATOM 2226 O GLU A 296 37.717 63.458 78.293 1.00131.70 O ANISOU 2226 O GLU A 296 13079 20287 16675 2130 695 1254 O ATOM 2227 CB GLU A 296 38.542 60.980 80.361 1.00115.93 C ANISOU 2227 CB GLU A 296 11269 18214 14567 2057 602 814 C ATOM 2228 CG GLU A 296 39.667 60.010 80.034 1.00127.15 C ANISOU 2228 CG GLU A 296 12682 19741 15887 2006 614 705 C ATOM 2229 CD GLU A 296 40.267 59.382 81.285 1.00127.30 C ANISOU 2229 CD GLU A 296 12750 19660 15960 1980 584 523 C ATOM 2230 OE1 GLU A 296 39.552 59.280 82.303 1.00111.84 O ANISOU 2230 OE1 GLU A 296 10867 17597 14028 2003 536 479 O ATOM 2231 OE2 GLU A 296 41.452 58.993 81.254 1.00134.22 O1+ ANISOU 2231 OE2 GLU A 296 13583 20570 16845 1939 610 429 O1+ ATOM 2232 N LYS A 297 39.065 61.897 77.423 1.00124.41 N ANISOU 2232 N LYS A 297 12156 19595 15520 2047 715 1128 N ATOM 2233 CA LYS A 297 39.711 62.794 76.476 1.00130.83 C ANISOU 2233 CA LYS A 297 12841 20470 16399 2022 794 1254 C ATOM 2234 C LYS A 297 39.246 62.463 75.085 1.00138.75 C ANISOU 2234 C LYS A 297 13835 21704 17180 2040 796 1404 C ATOM 2235 O LYS A 297 39.385 61.334 74.643 1.00145.19 O ANISOU 2235 O LYS A 297 14693 22670 17802 2023 771 1329 O ATOM 2236 CB LYS A 297 41.235 62.690 76.583 1.00128.72 C ANISOU 2236 CB LYS A 297 12494 20196 16218 1942 854 1122 C ATOM 2237 CG LYS A 297 41.976 63.620 75.636 1.00131.92 C ANISOU 2237 CG LYS A 297 12754 20671 16698 1897 953 1242 C ATOM 2238 CD LYS A 297 43.465 63.664 75.932 1.00134.41 C ANISOU 2238 CD LYS A 297 12977 20951 17141 1810 1026 1096 C ATOM 2239 CE LYS A 297 44.161 64.677 75.031 1.00137.07 C ANISOU 2239 CE LYS A 297 13160 21354 17566 1748 1142 1218 C ATOM 2240 NZ LYS A 297 45.622 64.783 75.300 1.00132.97 N ANISOU 2240 NZ LYS A 297 12535 20809 17179 1650 1231 1073 N ATOM 2241 N ARG A 298 38.716 63.455 74.384 1.00135.54 N ANISOU 2241 N ARG A 298 13365 21330 16802 2075 824 1616 N ATOM 2242 CA ARG A 298 38.174 63.227 73.049 1.00144.06 C ANISOU 2242 CA ARG A 298 14427 22644 17665 2097 822 1782 C ATOM 2243 C ARG A 298 39.232 62.965 71.983 1.00150.57 C ANISOU 2243 C ARG A 298 15162 23659 18389 2030 884 1790 C ATOM 2244 O ARG A 298 40.291 63.575 71.988 1.00155.21 O ANISOU 2244 O ARG A 298 15654 24194 19124 1971 962 1773 O ATOM 2245 CB ARG A 298 37.320 64.424 72.621 1.00147.10 C ANISOU 2245 CB ARG A 298 14762 23011 18119 2161 836 2028 C ATOM 2246 CG ARG A 298 36.052 64.620 73.432 1.00148.82 C ANISOU 2246 CG ARG A 298 15061 23093 18389 2239 773 2044 C ATOM 2247 CD ARG A 298 35.206 65.735 72.835 1.00153.74 C ANISOU 2247 CD ARG A 298 15626 23729 19061 2314 785 2303 C ATOM 2248 NE ARG A 298 33.911 65.868 73.498 1.00155.98 N ANISOU 2248 NE ARG A 298 15980 23912 19375 2393 728 2319 N ATOM 2249 CZ ARG A 298 32.971 66.732 73.128 1.00156.14 C ANISOU 2249 CZ ARG A 298 15964 23928 19435 2476 721 2526 C ATOM 2250 NH1 ARG A 298 33.184 67.541 72.100 1.00154.51 N ANISOU 2250 NH1 ARG A 298 15656 23809 19240 2493 766 2750 N ATOM 2251 NH2 ARG A 298 31.820 66.788 73.783 1.00153.86 N ANISOU 2251 NH2 ARG A 298 15733 23552 19175 2544 672 2512 N ATOM 2252 N VAL A 299 38.925 62.055 71.064 1.00144.37 N ANISOU 2252 N VAL A 299 14401 23103 17351 2033 853 1806 N ATOM 2253 CA VAL A 299 39.903 61.573 70.097 1.00134.03 C ANISOU 2253 CA VAL A 299 13016 21990 15918 1969 902 1770 C ATOM 2254 C VAL A 299 39.301 61.185 68.750 1.00123.63 C ANISOU 2254 C VAL A 299 11678 20954 14343 1986 881 1902 C ATOM 2255 O VAL A 299 38.093 61.073 68.612 1.00115.71 O ANISOU 2255 O VAL A 299 10732 20001 13233 2048 819 1995 O ATOM 2256 CB VAL A 299 40.730 60.336 70.613 1.00124.13 C ANISOU 2256 CB VAL A 299 11815 20727 14623 1929 881 1504 C ATOM 2257 CG1 VAL A 299 42.184 60.436 70.156 1.00121.95 C ANISOU 2257 CG1 VAL A 299 11424 20518 14394 1846 976 1443 C ATOM 2258 CG2 VAL A 299 40.693 60.190 72.126 1.00118.94 C ANISOU 2258 CG2 VAL A 299 11245 19822 14124 1944 840 1351 C ATOM 2259 N ASP A 300 40.171 60.935 67.779 1.00127.41 N ANISOU 2259 N ASP A 300 12068 21624 14718 1924 937 1893 N ATOM 2260 CA ASP A 300 39.763 60.532 66.432 1.00136.97 C ANISOU 2260 CA ASP A 300 13239 23131 15674 1925 922 1998 C ATOM 2261 C ASP A 300 40.958 60.097 65.577 1.00142.38 C ANISOU 2261 C ASP A 300 13831 24000 16268 1840 993 1912 C ATOM 2262 O ASP A 300 40.802 59.480 64.520 1.00142.15 O ANISOU 2262 O ASP A 300 13770 24228 16012 1829 975 1924 O ATOM 2263 CB ASP A 300 39.013 61.665 65.737 1.00136.48 C ANISOU 2263 CB ASP A 300 13111 23140 15605 1960 941 2297 C TER 2264 ASP A 300 ATOM 2265 P G R 2 31.700 41.193 53.252 1.00199.31 P ANISOU 2265 P G R 2 20330 35259 20139 1471 -115 -497 P ATOM 2266 OP1 G R 2 33.018 40.520 53.394 1.00190.21 O ANISOU 2266 OP1 G R 2 19158 34092 19020 1478 -107 -726 O ATOM 2267 OP2 G R 2 31.223 41.618 51.910 1.00179.24 O ANISOU 2267 OP2 G R 2 17554 33168 17381 1415 -121 -371 O ATOM 2268 O5' G R 2 30.596 40.237 53.891 1.00169.90 O ANISOU 2268 O5' G R 2 16725 31314 16516 1451 -142 -645 O ATOM 2269 C5' G R 2 30.955 38.963 54.401 1.00159.99 C ANISOU 2269 C5' G R 2 15519 29908 15363 1440 -159 -942 C ATOM 2270 C4' G R 2 29.785 38.014 54.402 1.00156.77 C ANISOU 2270 C4' G R 2 15102 29510 14952 1384 -187 -1085 C ATOM 2271 O4' G R 2 28.853 38.364 53.344 1.00157.66 O ANISOU 2271 O4' G R 2 15051 29970 14882 1324 -199 -971 O ATOM 2272 C3' G R 2 30.127 36.558 54.133 1.00159.51 C ANISOU 2272 C3' G R 2 15340 29973 15294 1332 -207 -1434 C ATOM 2273 O3' G R 2 30.614 35.888 55.284 1.00153.03 O ANISOU 2273 O3' G R 2 14685 28791 14669 1380 -209 -1579 O ATOM 2274 C2' G R 2 28.815 36.001 53.597 1.00159.76 C ANISOU 2274 C2' G R 2 15266 30202 15234 1248 -231 -1498 C ATOM 2275 O2' G R 2 27.910 35.735 54.657 1.00157.13 O ANISOU 2275 O2' G R 2 15127 29540 15035 1265 -235 -1481 O ATOM 2276 C1' G R 2 28.288 37.192 52.792 1.00160.07 C ANISOU 2276 C1' G R 2 15211 30490 15119 1236 -228 -1213 C ATOM 2277 N9 G R 2 28.677 37.119 51.369 1.00170.85 N ANISOU 2277 N9 G R 2 16278 32350 16287 1165 -221 -1282 N ATOM 2278 C8 G R 2 29.290 38.117 50.647 1.00175.75 C ANISOU 2278 C8 G R 2 16785 33208 16784 1180 -197 -1094 C ATOM 2279 N7 G R 2 29.528 37.792 49.407 1.00177.80 N ANISOU 2279 N7 G R 2 16775 33936 16844 1095 -174 -1212 N ATOM 2280 C5 G R 2 29.041 36.497 49.301 1.00177.87 C ANISOU 2280 C5 G R 2 16712 34018 16854 1019 -181 -1508 C ATOM 2281 C6 G R 2 29.022 35.621 48.188 1.00175.08 C ANISOU 2281 C6 G R 2 16099 34118 16305 899 -151 -1766 C ATOM 2282 O6 G R 2 29.445 35.828 47.047 1.00185.00 O ANISOU 2282 O6 G R 2 17142 35817 17331 833 -117 -1778 O ATOM 2283 N1 G R 2 28.439 34.396 48.498 1.00169.54 N ANISOU 2283 N1 G R 2 15402 33338 15679 845 -159 -2036 N ATOM 2284 C2 G R 2 27.935 34.051 49.727 1.00171.94 C ANISOU 2284 C2 G R 2 15926 33191 16214 901 -197 -2042 C ATOM 2285 N2 G R 2 27.412 32.820 49.832 1.00167.85 N ANISOU 2285 N2 G R 2 15356 32687 15732 828 -194 -2321 N ATOM 2286 N3 G R 2 27.946 34.860 50.776 1.00178.44 N ANISOU 2286 N3 G R 2 17004 33596 17197 1009 -228 -1800 N ATOM 2287 C4 G R 2 28.508 36.061 50.498 1.00178.75 C ANISOU 2287 C4 G R 2 17048 33695 17172 1063 -215 -1549 C ATOM 2288 P C R 3 32.058 35.180 55.265 1.00161.10 P ANISOU 2288 P C R 3 15649 29840 15723 1403 -202 -1821 P ATOM 2289 OP1 C R 3 32.385 34.789 56.656 1.00164.67 O ANISOU 2289 OP1 C R 3 16308 29861 16399 1466 -209 -1874 O ATOM 2290 OP2 C R 3 33.020 36.026 54.513 1.00150.53 O ANISOU 2290 OP2 C R 3 14197 28743 14254 1415 -176 -1716 O ATOM 2291 O5' C R 3 31.794 33.818 54.489 1.00153.15 O ANISOU 2291 O5' C R 3 14447 29116 14628 1320 -216 -2146 O ATOM 2292 C5' C R 3 30.891 32.856 55.015 1.00151.27 C ANISOU 2292 C5' C R 3 14260 28730 14486 1289 -238 -2290 C ATOM 2293 C4' C R 3 31.043 31.536 54.311 1.00151.03 C ANISOU 2293 C4' C R 3 14027 28970 14390 1217 -236 -2648 C ATOM 2294 O4' C R 3 30.524 31.653 52.964 1.00150.47 O ANISOU 2294 O4' C R 3 13723 29352 14097 1117 -223 -2661 O ATOM 2295 C3' C R 3 32.481 31.073 54.139 1.00151.17 C ANISOU 2295 C3' C R 3 14037 28920 14480 1250 -144 -2828 C ATOM 2296 O3' C R 3 32.953 30.373 55.281 1.00151.57 O ANISOU 2296 O3' C R 3 14289 28487 14813 1316 -87 -2917 O ATOM 2297 C2' C R 3 32.435 30.239 52.860 1.00152.50 C ANISOU 2297 C2' C R 3 13997 29447 14499 1145 -68 -3090 C ATOM 2298 O2' C R 3 31.995 28.915 53.125 1.00151.37 O ANISOU 2298 O2' C R 3 13847 29214 14452 1104 -53 -3368 O ATOM 2299 C1' C R 3 31.350 30.959 52.057 1.00157.54 C ANISOU 2299 C1' C R 3 14408 30580 14871 1068 -193 -2943 C ATOM 2300 N1 C R 3 31.882 31.949 51.088 1.00164.26 N ANISOU 2300 N1 C R 3 15170 31690 15550 1056 -140 -2770 N ATOM 2301 C2 C R 3 32.413 31.516 49.864 1.00165.96 C ANISOU 2301 C2 C R 3 15289 32138 15630 971 10 -2945 C ATOM 2302 O2 C R 3 32.463 30.297 49.621 1.00168.77 O ANISOU 2302 O2 C R 3 15653 32458 16014 913 100 -3253 O ATOM 2303 N3 C R 3 32.867 32.445 48.984 1.00161.97 N ANISOU 2303 N3 C R 3 14714 31875 14953 951 64 -2773 N ATOM 2304 C4 C R 3 32.795 33.748 49.283 1.00160.44 C ANISOU 2304 C4 C R 3 14521 31699 14738 1017 -25 -2440 C ATOM 2305 N4 C R 3 33.254 34.622 48.390 1.00160.09 N ANISOU 2305 N4 C R 3 14403 31896 14529 990 42 -2275 N ATOM 2306 C5 C R 3 32.251 34.220 50.512 1.00159.80 C ANISOU 2306 C5 C R 3 14575 31337 14806 1108 -154 -2254 C ATOM 2307 C6 C R 3 31.804 33.293 51.369 1.00158.81 C ANISOU 2307 C6 C R 3 14569 30920 14852 1119 -177 -2418 C ATOM 2308 P C R 4 34.445 30.606 55.827 1.00137.38 P ANISOU 2308 P C R 4 12671 26277 13249 1404 54 -2849 P ATOM 2309 OP1 C R 4 34.584 29.948 57.151 1.00137.51 O ANISOU 2309 OP1 C R 4 12873 25823 13552 1464 71 -2887 O ATOM 2310 OP2 C R 4 34.761 32.056 55.697 1.00141.52 O ANISOU 2310 OP2 C R 4 13219 26858 13695 1429 41 -2562 O ATOM 2311 O5' C R 4 35.325 29.755 54.808 1.00160.96 O ANISOU 2311 O5' C R 4 15562 29396 16199 1372 208 -3109 O ATOM 2312 C5' C R 4 36.686 30.070 54.570 1.00154.62 C ANISOU 2312 C5' C R 4 14814 28472 15462 1414 350 -3077 C ATOM 2313 C4' C R 4 37.131 29.619 53.201 1.00155.79 C ANISOU 2313 C4' C R 4 14832 28938 15424 1351 471 -3276 C ATOM 2314 O4' C R 4 36.162 30.034 52.196 1.00159.09 O ANISOU 2314 O4' C R 4 15064 29832 15549 1252 386 -3243 O ATOM 2315 C3' C R 4 38.437 30.220 52.720 1.00149.73 C ANISOU 2315 C3' C R 4 14086 28162 14644 1376 610 -3204 C ATOM 2316 O3' C R 4 39.568 29.569 53.259 1.00148.76 O ANISOU 2316 O3' C R 4 14090 27681 14752 1452 743 -3313 O ATOM 2317 C2' C R 4 38.313 30.126 51.204 1.00147.38 C ANISOU 2317 C2' C R 4 13627 28324 14048 1276 672 -3328 C ATOM 2318 O2' C R 4 38.557 28.797 50.757 1.00145.91 O ANISOU 2318 O2' C R 4 13448 28132 13861 1255 788 -3652 O ATOM 2319 C1' C R 4 36.829 30.436 51.016 1.00145.71 C ANISOU 2319 C1' C R 4 13287 28412 13666 1205 497 -3244 C ATOM 2320 N1 C R 4 36.576 31.885 50.811 1.00126.73 N ANISOU 2320 N1 C R 4 10817 26210 11126 1199 412 -2927 N ATOM 2321 C2 C R 4 36.621 32.412 49.525 1.00134.81 C ANISOU 2321 C2 C R 4 11696 27646 11881 1118 459 -2877 C ATOM 2322 O2 C R 4 36.883 31.641 48.586 1.00149.85 O ANISOU 2322 O2 C R 4 13550 29729 13656 1047 576 -3112 O ATOM 2323 N3 C R 4 36.382 33.736 49.352 1.00125.49 N ANISOU 2323 N3 C R 4 10451 26644 10584 1120 386 -2571 N ATOM 2324 C4 C R 4 36.104 34.522 50.396 1.00117.90 C ANISOU 2324 C4 C R 4 9579 25459 9758 1200 273 -2335 C ATOM 2325 N4 C R 4 35.871 35.821 50.189 1.00116.92 N ANISOU 2325 N4 C R 4 9397 25513 9515 1208 213 -2035 N ATOM 2326 C5 C R 4 36.045 34.012 51.714 1.00108.61 C ANISOU 2326 C5 C R 4 8572 23852 8841 1275 228 -2391 C ATOM 2327 C6 C R 4 36.286 32.708 51.862 1.00110.37 C ANISOU 2327 C6 C R 4 8838 23916 9181 1270 297 -2679 C ATOM 2328 P C R 5 40.596 30.398 54.170 1.00115.81 P ANISOU 2328 P C R 5 10013 23225 10765 1539 766 -3114 P ATOM 2329 OP1 C R 5 41.792 29.509 54.324 1.00124.81 O ANISOU 2329 OP1 C R 5 11178 24209 12034 1610 904 -3321 O ATOM 2330 OP2 C R 5 39.883 30.955 55.346 1.00108.37 O ANISOU 2330 OP2 C R 5 9143 22104 9930 1573 609 -2923 O ATOM 2331 O5' C R 5 40.955 31.685 53.288 1.00160.97 O ANISOU 2331 O5' C R 5 15655 29208 16298 1489 803 -2922 O ATOM 2332 C5' C R 5 41.600 31.591 52.019 1.00138.00 C ANISOU 2332 C5' C R 5 12666 26554 13215 1437 948 -3029 C ATOM 2333 C4' C R 5 41.983 32.959 51.504 1.00118.87 C ANISOU 2333 C4' C R 5 10184 24322 10658 1404 971 -2795 C ATOM 2334 O4' C R 5 40.806 33.687 51.084 1.00115.84 O ANISOU 2334 O4' C R 5 9697 24256 10062 1344 829 -2637 O ATOM 2335 C3' C R 5 42.660 33.883 52.508 1.00105.33 C ANISOU 2335 C3' C R 5 8524 22388 9107 1475 948 -2597 C ATOM 2336 O3' C R 5 44.046 33.611 52.605 1.00103.77 O ANISOU 2336 O3' C R 5 8326 22101 9002 1524 1086 -2712 O ATOM 2337 C2' C R 5 42.342 35.286 51.977 1.00113.10 C ANISOU 2337 C2' C R 5 9458 23578 9936 1418 918 -2320 C ATOM 2338 O2' C R 5 43.315 35.737 51.048 1.00136.02 O ANISOU 2338 O2' C R 5 12294 26670 12718 1376 1070 -2305 O ATOM 2339 C1' C R 5 41.026 35.073 51.222 1.00113.85 C ANISOU 2339 C1' C R 5 9447 24012 9797 1352 810 -2347 C ATOM 2340 N1 C R 5 39.869 35.719 51.874 1.00116.05 N ANISOU 2340 N1 C R 5 9741 24275 10079 1370 629 -2143 N ATOM 2341 C2 C R 5 39.093 35.081 52.878 1.00124.51 C ANISOU 2341 C2 C R 5 10904 25103 11302 1411 515 -2203 C ATOM 2342 O2 C R 5 39.345 33.925 53.278 1.00125.15 O ANISOU 2342 O2 C R 5 11051 24967 11534 1435 559 -2426 O ATOM 2343 N3 C R 5 38.043 35.758 53.415 1.00123.90 N ANISOU 2343 N3 C R 5 10848 25033 11197 1428 361 -2004 N ATOM 2344 C4 C R 5 37.744 36.997 53.012 1.00124.74 C ANISOU 2344 C4 C R 5 10885 25368 11145 1416 315 -1749 C ATOM 2345 N4 C R 5 36.695 37.606 53.585 1.00117.29 N ANISOU 2345 N4 C R 5 9979 24413 10172 1446 173 -1558 N ATOM 2346 C5 C R 5 38.519 37.652 51.999 1.00128.09 C ANISOU 2346 C5 C R 5 11204 26040 11426 1375 426 -1675 C ATOM 2347 C6 C R 5 39.556 36.990 51.461 1.00117.02 C ANISOU 2347 C6 C R 5 9786 24633 10041 1347 581 -1878 C ATOM 2348 P A R 6 44.853 33.877 53.966 1.00124.92 P ANISOU 2348 P A R 6 11073 24472 11919 1621 1067 -2646 P ATOM 2349 OP1 A R 6 46.281 33.511 53.721 1.00112.62 O ANISOU 2349 OP1 A R 6 9476 22910 10404 1657 1230 -2790 O ATOM 2350 OP2 A R 6 44.109 33.249 55.098 1.00129.95 O ANISOU 2350 OP2 A R 6 11804 24855 12718 1675 938 -2683 O ATOM 2351 O5' A R 6 44.754 35.448 54.140 1.00 99.98 O ANISOU 2351 O5' A R 6 7911 21355 8721 1596 1016 -2339 O ATOM 2352 C5' A R 6 45.575 36.288 53.368 1.00 97.74 C ANISOU 2352 C5' A R 6 7552 21253 8330 1551 1136 -2244 C ATOM 2353 C4' A R 6 45.091 37.703 53.440 1.00102.90 C ANISOU 2353 C4' A R 6 8209 21959 8931 1519 1069 -1944 C ATOM 2354 O4' A R 6 43.696 37.762 53.064 1.00101.01 O ANISOU 2354 O4' A R 6 7966 21850 8562 1479 951 -1867 O ATOM 2355 C3' A R 6 45.105 38.334 54.810 1.00107.50 C ANISOU 2355 C3' A R 6 8882 22261 9703 1583 984 -1795 C ATOM 2356 O3' A R 6 46.389 38.744 55.240 1.00137.54 O ANISOU 2356 O3' A R 6 12678 25954 13627 1609 1084 -1780 O ATOM 2357 C2' A R 6 44.101 39.468 54.660 1.00103.32 C ANISOU 2357 C2' A R 6 8358 21824 9074 1548 894 -1528 C ATOM 2358 O2' A R 6 44.670 40.587 53.997 1.00105.23 O ANISOU 2358 O2' A R 6 8531 22220 9231 1496 992 -1353 O ATOM 2359 C1' A R 6 43.071 38.837 53.729 1.00103.66 C ANISOU 2359 C1' A R 6 8353 22095 8939 1497 843 -1609 C ATOM 2360 N9 A R 6 41.919 38.317 54.470 1.00113.69 N ANISOU 2360 N9 A R 6 9700 23231 10266 1532 691 -1635 N ATOM 2361 C8 A R 6 41.618 37.013 54.781 1.00120.59 C ANISOU 2361 C8 A R 6 10607 24005 11207 1554 655 -1866 C ATOM 2362 N7 A R 6 40.498 36.898 55.461 1.00127.74 N ANISOU 2362 N7 A R 6 11581 24807 12146 1573 517 -1816 N ATOM 2363 C5 A R 6 40.048 38.206 55.602 1.00123.32 C ANISOU 2363 C5 A R 6 11041 24281 11535 1573 460 -1538 C ATOM 2364 C6 A R 6 38.916 38.749 56.228 1.00120.21 C ANISOU 2364 C6 A R 6 10721 23819 11133 1595 333 -1364 C ATOM 2365 N6 A R 6 38.007 37.996 56.845 1.00125.21 N ANISOU 2365 N6 A R 6 11424 24343 11806 1611 236 -1454 N ATOM 2366 N1 A R 6 38.759 40.091 56.193 1.00119.74 N ANISOU 2366 N1 A R 6 10665 23806 11024 1599 324 -1094 N ATOM 2367 C2 A R 6 39.689 40.823 55.563 1.00126.65 C ANISOU 2367 C2 A R 6 11466 24790 11866 1573 433 -1007 C ATOM 2368 N3 A R 6 40.796 40.431 54.930 1.00124.08 N ANISOU 2368 N3 A R 6 11066 24547 11533 1542 560 -1152 N ATOM 2369 C4 A R 6 40.917 39.092 54.992 1.00117.95 C ANISOU 2369 C4 A R 6 10295 23721 10801 1548 567 -1421 C ATOM 2370 P U R 7 46.710 38.694 56.814 1.00107.33 P ANISOU 2370 P U R 7 8954 21787 10041 1692 1021 -1775 P ATOM 2371 OP1 U R 7 48.121 39.084 57.100 1.00105.57 O ANISOU 2371 OP1 U R 7 8693 21498 9922 1706 1138 -1777 O ATOM 2372 OP2 U R 7 46.191 37.361 57.243 1.00107.50 O ANISOU 2372 OP2 U R 7 9032 21689 10126 1739 948 -1973 O ATOM 2373 O5' U R 7 45.822 39.884 57.401 1.00 94.13 O ANISOU 2373 O5' U R 7 7350 20034 8380 1686 912 -1506 O ATOM 2374 C5' U R 7 46.161 41.237 57.123 1.00 97.14 C ANISOU 2374 C5' U R 7 7690 20491 8727 1644 972 -1287 C ATOM 2375 C4' U R 7 45.196 42.206 57.756 1.00104.26 C ANISOU 2375 C4' U R 7 8671 21288 9655 1656 865 -1054 C ATOM 2376 O4' U R 7 43.860 42.042 57.197 1.00110.95 O ANISOU 2376 O4' U R 7 9520 22287 10348 1639 766 -1007 O ATOM 2377 C3' U R 7 44.945 42.056 59.243 1.00108.22 C ANISOU 2377 C3' U R 7 9302 21480 10336 1724 774 -1059 C ATOM 2378 O3' U R 7 46.000 42.478 60.080 1.00119.27 O ANISOU 2378 O3' U R 7 10719 22695 11904 1745 836 -1045 O ATOM 2379 C2' U R 7 43.654 42.832 59.396 1.00 94.62 C ANISOU 2379 C2' U R 7 7639 19759 8554 1724 673 -848 C ATOM 2380 O2' U R 7 43.888 44.212 59.137 1.00 93.10 O ANISOU 2380 O2' U R 7 7405 19617 8350 1693 732 -620 O ATOM 2381 C1' U R 7 42.895 42.286 58.204 1.00 99.98 C ANISOU 2381 C1' U R 7 8246 20709 9031 1685 642 -902 C ATOM 2382 N1 U R 7 42.230 41.009 58.549 1.00100.64 N ANISOU 2382 N1 U R 7 8385 20726 9125 1712 554 -1093 N ATOM 2383 C2 U R 7 40.988 41.122 59.152 1.00101.45 C ANISOU 2383 C2 U R 7 8582 20744 9221 1735 434 -1000 C ATOM 2384 O2 U R 7 40.462 42.209 59.387 1.00 91.40 O ANISOU 2384 O2 U R 7 7347 19450 7932 1742 404 -774 O ATOM 2385 N3 U R 7 40.391 39.914 59.463 1.00110.22 N ANISOU 2385 N3 U R 7 9737 21793 10348 1749 365 -1182 N ATOM 2386 C4 U R 7 40.896 38.639 59.241 1.00108.70 C ANISOU 2386 C4 U R 7 9506 21603 10191 1748 401 -1438 C ATOM 2387 O4 U R 7 40.240 37.648 59.576 1.00112.61 O ANISOU 2387 O4 U R 7 10045 22027 10713 1758 336 -1575 O ATOM 2388 C5 U R 7 42.187 38.612 58.622 1.00104.14 C ANISOU 2388 C5 U R 7 8838 21111 9620 1735 529 -1518 C ATOM 2389 C6 U R 7 42.788 39.765 58.307 1.00102.04 C ANISOU 2389 C6 U R 7 8527 20918 9326 1714 599 -1349 C ATOM 2390 P U R 8 46.432 41.529 61.297 1.00 98.53 P ANISOU 2390 P U R 8 8173 19813 9452 1810 801 -1219 P ATOM 2391 OP1 U R 8 47.622 42.161 61.950 1.00104.29 O ANISOU 2391 OP1 U R 8 8885 20414 10327 1816 880 -1182 O ATOM 2392 OP2 U R 8 46.500 40.108 60.842 1.00 96.68 O ANISOU 2392 OP2 U R 8 7909 19650 9177 1827 805 -1456 O ATOM 2393 O5' U R 8 45.179 41.644 62.276 1.00126.16 O ANISOU 2393 O5' U R 8 11809 23134 12994 1842 665 -1124 O ATOM 2394 C5' U R 8 44.598 42.906 62.572 1.00109.42 C ANISOU 2394 C5' U R 8 9733 20968 10876 1830 638 -890 C ATOM 2395 C4' U R 8 43.256 42.754 63.235 1.00106.46 C ANISOU 2395 C4' U R 8 9476 20483 10492 1858 519 -839 C ATOM 2396 O4' U R 8 42.329 42.011 62.405 1.00111.55 O ANISOU 2396 O4' U R 8 10096 21309 10978 1843 461 -908 O ATOM 2397 C3' U R 8 43.260 41.990 64.541 1.00112.45 C ANISOU 2397 C3' U R 8 10344 20987 11396 1903 467 -957 C ATOM 2398 O3' U R 8 43.760 42.754 65.619 1.00118.14 O ANISOU 2398 O3' U R 8 11119 21501 12269 1919 488 -868 O ATOM 2399 C2' U R 8 41.804 41.566 64.675 1.00109.22 C ANISOU 2399 C2' U R 8 10014 20576 10908 1911 365 -944 C ATOM 2400 O2' U R 8 40.983 42.642 65.101 1.00117.44 O ANISOU 2400 O2' U R 8 11123 21555 11944 1913 333 -735 O ATOM 2401 C1' U R 8 41.463 41.248 63.223 1.00103.43 C ANISOU 2401 C1' U R 8 9175 20133 9990 1874 369 -982 C ATOM 2402 N1 U R 8 41.713 39.822 62.953 1.00105.74 N ANISOU 2402 N1 U R 8 9435 20458 10284 1878 368 -1227 N ATOM 2403 C2 U R 8 40.676 38.969 63.275 1.00110.95 C ANISOU 2403 C2 U R 8 10159 21069 10928 1886 282 -1309 C ATOM 2404 O2 U R 8 39.611 39.372 63.721 1.00103.87 O ANISOU 2404 O2 U R 8 9342 20122 10001 1888 214 -1188 O ATOM 2405 N3 U R 8 40.943 37.643 63.034 1.00111.39 N ANISOU 2405 N3 U R 8 10177 21137 11008 1891 292 -1538 N ATOM 2406 C4 U R 8 42.121 37.119 62.529 1.00 98.80 C ANISOU 2406 C4 U R 8 8495 19597 9448 1896 384 -1687 C ATOM 2407 O4 U R 8 42.206 35.903 62.372 1.00104.75 O ANISOU 2407 O4 U R 8 9225 20342 10232 1907 394 -1889 O ATOM 2408 C5 U R 8 43.150 38.072 62.229 1.00 93.96 C ANISOU 2408 C5 U R 8 7821 19042 8836 1888 472 -1589 C ATOM 2409 C6 U R 8 42.918 39.367 62.450 1.00 91.36 C ANISOU 2409 C6 U R 8 7522 18702 8490 1875 459 -1367 C ATOM 2410 P A R 9 44.582 42.014 66.772 1.00107.05 P ANISOU 2410 P A R 9 9763 19881 11030 1956 489 -1018 P ATOM 2411 OP1 A R 9 45.226 43.046 67.631 1.00116.57 O ANISOU 2411 OP1 A R 9 10987 20934 12371 1954 528 -910 O ATOM 2412 OP2 A R 9 45.440 40.952 66.158 1.00 91.88 O ANISOU 2412 OP2 A R 9 7756 18060 9094 1966 538 -1215 O ATOM 2413 O5' A R 9 43.415 41.303 67.579 1.00114.19 O ANISOU 2413 O5' A R 9 10794 20649 11945 1983 386 -1054 O ATOM 2414 C5' A R 9 43.677 40.139 68.326 1.00107.38 C ANISOU 2414 C5' A R 9 9976 19650 11175 2018 359 -1220 C ATOM 2415 C4' A R 9 42.602 39.108 68.148 1.00 95.84 C ANISOU 2415 C4' A R 9 8555 18216 9644 2022 289 -1310 C ATOM 2416 O4' A R 9 42.391 38.851 66.737 1.00106.99 O ANISOU 2416 O4' A R 9 9870 19874 10908 1994 305 -1356 O ATOM 2417 C3' A R 9 42.946 37.751 68.722 1.00 88.95 C ANISOU 2417 C3' A R 9 7704 17221 8871 2059 275 -1497 C ATOM 2418 O3' A R 9 42.762 37.695 70.121 1.00 99.48 O ANISOU 2418 O3' A R 9 9146 18327 10324 2082 234 -1469 O ATOM 2419 C2' A R 9 42.078 36.804 67.903 1.00 85.82 C ANISOU 2419 C2' A R 9 7281 16953 8372 2044 239 -1605 C ATOM 2420 O2' A R 9 40.728 36.808 68.339 1.00 80.67 O ANISOU 2420 O2' A R 9 6720 16248 7684 2030 162 -1538 O ATOM 2421 C1' A R 9 42.136 37.474 66.532 1.00 99.25 C ANISOU 2421 C1' A R 9 8879 18909 9922 2005 279 -1545 C ATOM 2422 N9 A R 9 43.214 36.915 65.695 1.00 95.75 N ANISOU 2422 N9 A R 9 8321 18587 9474 2009 360 -1691 N ATOM 2423 C8 A R 9 44.331 37.539 65.192 1.00 97.64 C ANISOU 2423 C8 A R 9 8473 18918 9708 2001 451 -1663 C ATOM 2424 N7 A R 9 45.090 36.740 64.479 1.00101.99 N ANISOU 2424 N7 A R 9 8932 19572 10249 2010 522 -1831 N ATOM 2425 C5 A R 9 44.428 35.512 64.521 1.00101.32 C ANISOU 2425 C5 A R 9 8875 19447 10173 2027 474 -1980 C ATOM 2426 C6 A R 9 44.702 34.243 63.968 1.00111.72 C ANISOU 2426 C6 A R 9 10134 20816 11499 2046 519 -2196 C ATOM 2427 N6 A R 9 45.777 33.967 63.212 1.00122.18 N ANISOU 2427 N6 A R 9 11356 22256 12810 2056 631 -2310 N ATOM 2428 N1 A R 9 43.815 33.246 64.222 1.00107.47 N ANISOU 2428 N1 A R 9 9644 20200 10988 2053 456 -2296 N ATOM 2429 C2 A R 9 42.736 33.493 64.970 1.00102.54 C ANISOU 2429 C2 A R 9 9120 19470 10371 2041 356 -2188 C ATOM 2430 N3 A R 9 42.376 34.638 65.536 1.00105.14 N ANISOU 2430 N3 A R 9 9516 19748 10684 2027 309 -1988 N ATOM 2431 C4 A R 9 43.272 35.611 65.270 1.00100.17 C ANISOU 2431 C4 A R 9 8838 19185 10038 2022 372 -1893 C ATOM 2432 P G R 10 44.030 37.840 71.098 1.00 97.12 P ANISOU 2432 P G R 10 8851 17875 10175 2114 274 -1488 P ATOM 2433 OP1 G R 10 43.432 38.084 72.434 1.00115.60 O ANISOU 2433 OP1 G R 10 11312 20020 12592 2119 221 -1409 O ATOM 2434 OP2 G R 10 45.079 38.788 70.645 1.00 78.74 O ANISOU 2434 OP2 G R 10 6437 15633 7849 2100 349 -1428 O ATOM 2435 O5' G R 10 44.615 36.370 71.082 1.00 80.09 O ANISOU 2435 O5' G R 10 6657 15691 8082 2159 286 -1688 O ATOM 2436 C5' G R 10 43.854 35.351 71.696 1.00 89.88 C ANISOU 2436 C5' G R 10 7971 16812 9366 2178 228 -1759 C ATOM 2437 C4' G R 10 43.865 34.084 70.911 1.00 93.39 C ANISOU 2437 C4' G R 10 8353 17335 9797 2197 245 -1932 C ATOM 2438 O4' G R 10 43.686 34.402 69.516 1.00102.50 O ANISOU 2438 O4' G R 10 9422 18716 10809 2158 272 -1935 O ATOM 2439 C3' G R 10 45.165 33.304 70.963 1.00 97.75 C ANISOU 2439 C3' G R 10 8838 17853 10451 2257 310 -2070 C ATOM 2440 O3' G R 10 45.263 32.488 72.119 1.00 93.05 O ANISOU 2440 O3' G R 10 8305 17059 9991 2308 285 -2119 O ATOM 2441 C2' G R 10 45.138 32.525 69.658 1.00100.23 C ANISOU 2441 C2' G R 10 9059 18331 10693 2255 353 -2214 C ATOM 2442 O2' G R 10 44.305 31.381 69.778 1.00 96.45 O ANISOU 2442 O2' G R 10 8616 17781 10248 2265 316 -2316 O ATOM 2443 C1' G R 10 44.466 33.535 68.722 1.00109.90 C ANISOU 2443 C1' G R 10 10259 19744 11753 2184 340 -2103 C ATOM 2444 N9 G R 10 45.455 34.346 67.988 1.00112.13 N ANISOU 2444 N9 G R 10 10447 20173 11982 2172 418 -2066 N ATOM 2445 C8 G R 10 45.706 35.695 68.097 1.00117.86 C ANISOU 2445 C8 G R 10 11175 20926 12681 2142 430 -1900 C ATOM 2446 N7 G R 10 46.659 36.106 67.305 1.00111.40 N ANISOU 2446 N7 G R 10 10250 20251 11824 2131 517 -1911 N ATOM 2447 C5 G R 10 47.058 34.955 66.639 1.00106.31 C ANISOU 2447 C5 G R 10 9535 19683 11175 2160 568 -2101 C ATOM 2448 C6 G R 10 48.055 34.744 65.657 1.00106.61 C ANISOU 2448 C6 G R 10 9451 19884 11174 2165 677 -2207 C ATOM 2449 O6 G R 10 48.822 35.573 65.148 1.00105.25 O ANISOU 2449 O6 G R 10 9199 19832 10957 2138 753 -2147 O ATOM 2450 N1 G R 10 48.096 33.400 65.279 1.00112.22 N ANISOU 2450 N1 G R 10 10132 20604 11903 2204 706 -2405 N ATOM 2451 C2 G R 10 47.294 32.386 65.767 1.00114.26 C ANISOU 2451 C2 G R 10 10463 20730 12220 2231 640 -2487 C ATOM 2452 N2 G R 10 47.468 31.144 65.289 1.00121.89 N ANISOU 2452 N2 G R 10 11386 21714 13212 2270 695 -2683 N ATOM 2453 N3 G R 10 46.364 32.572 66.677 1.00107.16 N ANISOU 2453 N3 G R 10 9672 19686 11357 2220 536 -2385 N ATOM 2454 C4 G R 10 46.316 33.865 67.052 1.00105.97 C ANISOU 2454 C4 G R 10 9556 19529 11178 2186 507 -2198 C TER 2455 G R 10 HETATM 2456 S SO4 A 501 15.613 32.349 65.927 1.00139.55 S ANISOU 2456 S SO4 A 501 13699 25587 13737 1226 -140 -1353 S HETATM 2457 O1 SO4 A 501 15.490 33.761 65.562 1.00139.85 O ANISOU 2457 O1 SO4 A 501 13727 25724 13686 1293 -117 -1108 O HETATM 2458 O2 SO4 A 501 16.081 31.581 64.775 1.00136.56 O ANISOU 2458 O2 SO4 A 501 13247 25328 13312 1144 -140 -1532 O HETATM 2459 O3 SO4 A 501 14.318 31.830 66.354 1.00134.50 O1+ ANISOU 2459 O3 SO4 A 501 12976 24960 13169 1154 -160 -1362 O1+ HETATM 2460 O4 SO4 A 501 16.575 32.203 67.018 1.00147.78 O ANISOU 2460 O4 SO4 A 501 14896 26305 14949 1296 -160 -1390 O HETATM 2461 MG MG A 502 40.921 40.269 72.177 0.97 81.59 MG ANISOU 2461 MG MG A 502 7111 15782 8106 2052 165 -1044 MG HETATM 2462 MG MG A 503 44.452 38.029 74.355 0.57108.21 MG ANISOU 2462 MG MG A 503 10441 18818 11857 2160 221 -1426 MG HETATM 2463 S SO4 R 101 49.937 32.641 62.084 1.00157.81 S ANISOU 2463 S SO4 R 101 15598 26912 17451 2186 1027 -2731 S HETATM 2464 O1 SO4 R 101 50.398 32.363 60.730 1.00171.30 O ANISOU 2464 O1 SO4 R 101 17198 28855 19032 2162 1154 -2856 O HETATM 2465 O2 SO4 R 101 48.480 32.784 62.057 1.00154.41 O ANISOU 2465 O2 SO4 R 101 15236 26485 16946 2133 911 -2648 O HETATM 2466 O3 SO4 R 101 50.317 31.528 62.952 1.00150.65 O ANISOU 2466 O3 SO4 R 101 14732 25797 16710 2281 1024 -2864 O HETATM 2467 O4 SO4 R 101 50.563 33.878 62.548 1.00152.91 O ANISOU 2467 O4 SO4 R 101 14968 26275 16858 2167 1033 -2560 O HETATM 2468 O HOH A 601 28.454 25.929 70.357 1.00 71.87 O ANISOU 2468 O HOH A 601 5695 14814 6799 1672 -224 -2578 O HETATM 2469 O HOH A 602 13.124 35.986 64.862 1.00 99.13 O ANISOU 2469 O HOH A 602 8341 20970 8355 1329 -98 -614 O HETATM 2470 O HOH A 603 23.052 34.869 66.417 1.00 91.75 O ANISOU 2470 O HOH A 603 8148 18705 8006 1583 -178 -1199 O HETATM 2471 O HOH A 604 33.753 24.109 87.288 1.00101.86 O ANISOU 2471 O HOH A 604 10316 16116 12271 2312 -76 -1618 O HETATM 2472 O HOH A 605 13.917 48.952 71.802 1.00 66.31 O ANISOU 2472 O HOH A 605 4755 15107 5332 2281 69 1244 O HETATM 2473 O HOH A 606 21.508 31.608 78.064 1.00 85.88 O ANISOU 2473 O HOH A 606 7982 16046 8603 1705 -220 -1239 O HETATM 2474 O HOH A 607 32.124 52.801 82.488 1.00 87.54 O ANISOU 2474 O HOH A 607 8392 15023 9846 2129 221 386 O HETATM 2475 O HOH A 608 25.719 28.197 80.469 1.00 59.71 O ANISOU 2475 O HOH A 608 4792 11999 5898 1819 -224 -1591 O HETATM 2476 O HOH A 609 20.080 34.780 89.320 0.50 39.61 O ANISOU 2476 O HOH A 609 3934 7303 3813 2918 48 -28 O HETATM 2477 O HOH A 610 22.111 52.666 75.928 1.00 86.31 O ANISOU 2477 O HOH A 610 7887 16171 8735 2345 205 1178 O HETATM 2478 O HOH A 611 17.905 43.933 66.178 1.00 79.35 O ANISOU 2478 O HOH A 611 6340 17700 6111 1915 74 522 O HETATM 2479 O HOH A 612 24.777 41.066 67.078 1.00111.51 O ANISOU 2479 O HOH A 612 10810 21083 10474 1859 -45 -252 O HETATM 2480 O HOH A 613 12.485 42.618 85.465 1.00 83.22 O ANISOU 2480 O HOH A 613 7595 15653 8373 2049 -53 226 O HETATM 2481 O HOH A 614 25.688 47.401 61.721 1.00 76.35 O ANISOU 2481 O HOH A 614 5915 17488 5608 1926 149 910 O HETATM 2482 O HOH A 615 15.707 40.912 84.425 1.00 53.05 O ANISOU 2482 O HOH A 615 3954 11665 4538 1969 -67 -19 O HETATM 2483 O HOH A 616 15.968 38.946 67.479 1.00 80.50 O ANISOU 2483 O HOH A 616 6463 17796 6328 1665 -51 -232 O HETATM 2484 O HOH A 617 31.995 24.981 81.189 1.00 73.69 O ANISOU 2484 O HOH A 617 6543 13219 8235 2107 -127 -1963 O HETATM 2485 O HOH A 618 15.338 29.191 66.589 1.00107.19 O ANISOU 2485 O HOH A 618 9545 21286 9897 1038 -187 -1857 O HETATM 2486 O HOH A 619 48.218 48.945 81.758 1.00 73.95 O ANISOU 2486 O HOH A 619 6035 13580 8483 1951 448 -684 O HETATM 2487 O HOH A 620 43.854 58.899 82.818 1.00 67.44 O ANISOU 2487 O HOH A 620 5030 11975 8619 1859 649 169 O HETATM 2488 O HOH A 621 27.477 29.631 67.747 1.00 62.90 O ANISOU 2488 O HOH A 621 4503 14451 4946 1613 -284 -2180 O HETATM 2489 O HOH A 622 13.407 41.913 87.161 1.00118.96 O ANISOU 2489 O HOH A 622 12251 19939 13010 2024 -55 121 O HETATM 2490 O HOH A 623 23.357 41.302 68.795 1.00 90.28 O ANISOU 2490 O HOH A 623 8204 18194 7903 1896 -32 -169 O HETATM 2491 O HOH A 624 26.404 41.419 70.912 1.00 61.01 O ANISOU 2491 O HOH A 624 4705 13892 4584 1952 -45 -287 O HETATM 2492 O HOH A 625 12.941 37.190 79.163 1.00 69.77 O ANISOU 2492 O HOH A 625 5610 14674 6227 1733 -147 -279 O HETATM 2493 O HOH R 201 43.341 42.332 54.248 1.00 93.52 O ANISOU 2493 O HOH R 201 7086 20753 7696 1489 860 -932 O HETATM 2494 O HOH R 202 46.743 44.613 60.941 1.00 81.11 O ANISOU 2494 O HOH R 202 5894 17681 7241 1723 911 -739 O CONECT 1158 2462 CONECT 1159 2461 CONECT 1180 2462 CONECT 1762 2461 CONECT 2144 2462 CONECT 2433 2462 CONECT 2456 2457 2458 2459 2460 CONECT 2457 2456 CONECT 2458 2456 CONECT 2459 2456 CONECT 2460 2456 CONECT 2461 1159 1762 CONECT 2462 1158 1180 2144 2433 CONECT 2463 2464 2465 2466 2467 CONECT 2464 2463 CONECT 2465 2463 CONECT 2466 2463 CONECT 2467 2463 MASTER 508 0 4 15 7 0 5 6 2486 2 18 33 END
Display Options:
Goto PDB code:
3D presentation of molecule is powered by
3Dmol
, which supports all modern browsers and mobile devices via WebGL.
Hold mouse button:
left to rotate,middle to shift,right to zoom
Related entries of code: 5z9x
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
Check Database
Protein Sequence Similarity
No similar entries are found!
Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
No complexes with the same small molecule ligand are found!
Entry Information
PDB ID
5z9x
Complex Type
Protein-Nucleic Acid
PDBbind Subset
general set
Protein Name
Small RNA degrading nuclease 1, SDN1 Delta C
Ligand Name
miR173 RNA
EC.Number
E.C.3.1.-.-
Resolution
2.8(Å)
Affinity (Kd/Ki/IC50)
Kd=124.5uM
Release Year
2018
Protein/NA Sequence
Check fasta file
Primary Reference
(2018) Nat Commun Vol. 9: pp. 3585-3585
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
A3KPE8
Entrez Gene ID
NCBI Entrez Gene ID:
824172
ASD
Information of known allosteric effects of PDB entries
This site has been visited
times since Nov 2007.
Copyright ©2007-2024 涓婃捣鐩堣禌鎬濅俊鎭鎶鏈夐檺鍏徃 缃戠珯澶囨鍙凤細
娌狪CP澶2021015625鍙-3
娌叕缃戝畨澶囷細
姝e湪鐢宠涓
Technical Support锛堟妧鏈敮鎸侊級:
yingsaisi@foxmail.com