HEADER STRUCTURAL PROTEIN 21-JUN-09 3HXR TITLE NUCLEOPORIN NUP120 FROM S.CEREVISIAE (AA 1-757) COMPND MOL_ID: 1; COMPND 2 MOLECULE: NUCLEOPORIN NUP120; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: UNP RESIDUES 1-757; COMPND 5 SYNONYM: NUCLEAR PORE PROTEIN NUP120; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; SOURCE 3 ORGANISM_COMMON: BREWER'S YEAST,LAGER BEER YEAST,YEAST; SOURCE 4 ORGANISM_TAXID: 4932; SOURCE 5 GENE: NUP120, RAT2, YKL057C, YKL314, YKL313; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-RIL; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET-DUET KEYWDS STRUCTURAL PROTEIN, COILED COIL, MEMBRANE, MRNA TRANSPORT, KEYWDS 2 NUCLEAR PORE COMPLEX, NUCLEUS, PHOSPHOPROTEIN, PROTEIN KEYWDS 3 TRANSPORT, TRANSLOCATION, TRANSPORT EXPDTA X-RAY DIFFRACTION AUTHOR N.C.LEKSA,S.G.BROHAWN,T.U.SCHWARTZ REVDAT 2 08-SEP-09 3HXR 1 JRNL REVDAT 1 28-JUL-09 3HXR 0 JRNL AUTH N.C.LEKSA,S.G.BROHAWN,T.U.SCHWARTZ JRNL TITL THE STRUCTURE OF THE SCAFFOLD NUCLEOPORIN NUP120 JRNL TITL 2 REVEALS A NEW AND UNEXPECTED DOMAIN ARCHITECTURE. JRNL REF STRUCTURE V. 17 1082 2009 JRNL REFN ISSN 0969-2126 JRNL PMID 19576787 JRNL DOI 10.1016/J.STR.2009.06.003 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 3.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.09 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.900 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 3 NUMBER OF REFLECTIONS : 19288 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.247 REMARK 3 R VALUE (WORKING SET) : 0.244 REMARK 3 FREE R VALUE : 0.299 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120 REMARK 3 FREE R VALUE TEST SET COUNT : 1834 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 48.0958 - 7.0598 0.99 2612 135 0.2373 0.2827 REMARK 3 2 7.0598 - 5.6063 1.00 2611 158 0.2688 0.3254 REMARK 3 3 5.6063 - 4.8984 1.00 2585 173 0.2072 0.2673 REMARK 3 4 4.8984 - 4.4509 1.00 2655 103 0.1927 0.2288 REMARK 3 5 4.4509 - 4.1321 1.00 2671 114 0.2076 0.2940 REMARK 3 6 4.1321 - 3.8886 1.00 2622 153 0.2215 0.2938 REMARK 3 7 3.8886 - 3.6939 1.00 2593 157 0.2390 0.3283 REMARK 3 8 3.6939 - 3.5332 1.00 2626 141 0.2475 0.3188 REMARK 3 9 3.5332 - 3.3972 1.00 2615 157 0.2521 0.2762 REMARK 3 10 3.3972 - 3.2800 1.00 2606 171 0.2745 0.2875 REMARK 3 11 3.2800 - 3.1774 1.00 2649 128 0.2811 0.2789 REMARK 3 12 3.1774 - 3.0866 1.00 2628 127 0.3030 0.3372 REMARK 3 13 3.0866 - 3.0000 0.97 2534 117 0.3025 0.3435 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 : 0.31 REMARK 3 B_SOL : 73.24 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.990 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 82.20 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 : 0.017 NULL REMARK 3 ANGLE : 1.915 NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 4 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN A AND RESID 0:163) REMARK 3 ORIGIN FOR THE GROUP (A): 119.0667 38.7468 27.5949 REMARK 3 T TENSOR REMARK 3 T11: 0.1154 T22: 0.2773 REMARK 3 T33: 0.6297 T12: -0.1200 REMARK 3 T13: 0.1054 T23: -0.2461 REMARK 3 L TENSOR REMARK 3 L11: 4.4663 L22: 4.6921 REMARK 3 L33: 3.9761 L12: -0.0022 REMARK 3 L13: 2.2504 L23: 0.7876 REMARK 3 S TENSOR REMARK 3 S11: -0.1666 S12: -0.6003 S13: 1.2980 REMARK 3 S21: 0.3150 S22: 0.1346 S23: -0.8494 REMARK 3 S31: -0.2521 S32: 0.4713 S33: 0.0020 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN A AND RESID 164:181) REMARK 3 ORIGIN FOR THE GROUP (A): 112.0552 56.3715 29.1313 REMARK 3 T TENSOR REMARK 3 T11: 0.7591 T22: 0.4676 REMARK 3 T33: 1.8565 T12: 0.0144 REMARK 3 T13: 0.0549 T23: -0.3242 REMARK 3 L TENSOR REMARK 3 L11: 0.1677 L22: 0.4620 REMARK 3 L33: 0.6708 L12: -0.0914 REMARK 3 L13: 0.3305 L23: -0.0889 REMARK 3 S TENSOR REMARK 3 S11: -1.0640 S12: -0.0929 S13: 0.9258 REMARK 3 S21: 0.8064 S22: -1.0157 S23: -0.1579 REMARK 3 S31: -1.6631 S32: 0.2055 S33: -0.0158 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN A AND RESID 182:503) REMARK 3 ORIGIN FOR THE GROUP (A): 98.9678 37.1062 24.2158 REMARK 3 T TENSOR REMARK 3 T11: -0.1288 T22: 0.1459 REMARK 3 T33: 0.2489 T12: 0.0091 REMARK 3 T13: 0.1715 T23: -0.1741 REMARK 3 L TENSOR REMARK 3 L11: 3.5929 L22: 3.3406 REMARK 3 L33: 2.8649 L12: 0.5339 REMARK 3 L13: 0.7081 L23: 0.5515 REMARK 3 S TENSOR REMARK 3 S11: 0.0114 S12: -0.3486 S13: 1.4379 REMARK 3 S21: -0.0764 S22: -0.0981 S23: 0.4900 REMARK 3 S31: -0.3270 S32: -0.4186 S33: 0.0040 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN A AND RESID 504:730) REMARK 3 ORIGIN FOR THE GROUP (A): 96.7892 7.5526 6.3297 REMARK 3 T TENSOR REMARK 3 T11: 0.3074 T22: 0.2522 REMARK 3 T33: -0.1910 T12: 0.0463 REMARK 3 T13: -0.1192 T23: 0.1103 REMARK 3 L TENSOR REMARK 3 L11: 5.1495 L22: 5.2153 REMARK 3 L33: 2.1341 L12: 1.0011 REMARK 3 L13: 0.8435 L23: 0.6073 REMARK 3 S TENSOR REMARK 3 S11: 0.1588 S12: 0.5858 S13: -0.1971 REMARK 3 S21: -0.5664 S22: 0.0077 S23: 0.2425 REMARK 3 S31: 0.4769 S32: -0.0011 S33: -0.0137 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 3HXR COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUN-09. REMARK 100 THE RCSB ID CODE IS RCSB053712. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-FEB-09 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 24-ID-C REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19288 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.800 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 3.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.05100 REMARK 200 FOR THE DATA SET : 20.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.10 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6 REMARK 200 DATA REDUNDANCY IN SHELL : 3.00 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.59000 REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD REMARK 200 SOFTWARE USED: SHELXC/D/E REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53.57 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG3350, 0.2M KSCN, 0.1M TRIS- REMARK 280 HCL PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X+1/2,Y+1/2,-Z REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 57.30000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 76.84500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 57.30000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 76.84500 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A -3 REMARK 465 PRO A -2 REMARK 465 GLY A -1 REMARK 465 ASN A 30 REMARK 465 ASN A 31 REMARK 465 SER A 32 REMARK 465 ASN A 33 REMARK 465 ASN A 34 REMARK 465 ASN A 35 REMARK 465 GLY A 36 REMARK 465 LEU A 37 REMARK 465 LYS A 38 REMARK 465 GLU A 39 REMARK 465 GLY A 40 REMARK 465 ASP A 41 REMARK 465 LYS A 42 REMARK 465 SER A 43 REMARK 465 ILE A 44 REMARK 465 SER A 45 REMARK 465 THR A 46 REMARK 465 PRO A 47 REMARK 465 VAL A 48 REMARK 465 PRO A 49 REMARK 465 GLN A 50 REMARK 465 PRO A 51 REMARK 465 TYR A 52 REMARK 465 VAL A 189 REMARK 465 ASP A 190 REMARK 465 GLY A 191 REMARK 465 VAL A 192 REMARK 465 HIS A 193 REMARK 465 TYR A 194 REMARK 465 GLU A 195 REMARK 465 PRO A 196 REMARK 465 LEU A 197 REMARK 465 LEU A 198 REMARK 465 PHE A 199 REMARK 465 ASN A 200 REMARK 465 ASP A 201 REMARK 465 ASN A 202 REMARK 465 SER A 203 REMARK 465 LYS A 217 REMARK 465 SER A 218 REMARK 465 SER A 268 REMARK 465 HIS A 269 REMARK 465 PHE A 270 REMARK 465 ARG A 271 REMARK 465 LYS A 272 REMARK 465 VAL A 273 REMARK 465 GLU A 274 REMARK 465 ALA A 275 REMARK 465 LEU A 303 REMARK 465 LEU A 304 REMARK 465 VAL A 305 REMARK 465 ASP A 306 REMARK 465 SER A 307 REMARK 465 SER A 308 REMARK 465 GLY A 309 REMARK 465 ILE A 310 REMARK 465 LEU A 311 REMARK 465 THR A 312 REMARK 465 TYR A 313 REMARK 465 THR A 401 REMARK 465 GLY A 402 REMARK 465 THR A 501 REMARK 465 ASP A 502 REMARK 465 GLY A 503 REMARK 465 SER A 504 REMARK 465 GLY A 594 REMARK 465 ILE A 595 REMARK 465 PHE A 596 REMARK 465 TRP A 597 REMARK 465 LYS A 598 REMARK 465 LYS A 599 REMARK 465 ASN A 731 REMARK 465 THR A 732 REMARK 465 SER A 733 REMARK 465 HIS A 734 REMARK 465 LYS A 735 REMARK 465 ASN A 736 REMARK 465 ILE A 737 REMARK 465 ARG A 738 REMARK 465 PHE A 739 REMARK 465 PHE A 740 REMARK 465 LEU A 741 REMARK 465 GLU A 742 REMARK 465 ASN A 743 REMARK 465 VAL A 744 REMARK 465 GLU A 745 REMARK 465 CYS A 746 REMARK 465 PRO A 747 REMARK 465 PHE A 748 REMARK 465 TYR A 749 REMARK 465 LEU A 750 REMARK 465 ARG A 751 REMARK 465 HIS A 752 REMARK 465 ASN A 753 REMARK 465 GLU A 754 REMARK 465 VAL A 755 REMARK 465 GLN A 756 REMARK 465 GLU A 757 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 17 CG CD CE NZ REMARK 470 ARG A 75 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 124 CG CD CE NZ REMARK 470 LYS A 188 CG CD CE NZ REMARK 470 LYS A 206 CG CD CE NZ REMARK 470 ARG A 210 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 214 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 232 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 338 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 374 CG CD CE NZ REMARK 470 LYS A 531 CG CD CE NZ REMARK 470 LYS A 555 CG CD CE NZ REMARK 470 LYS A 606 CG CD CE NZ REMARK 470 ARG A 669 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 691 CG CD CE NZ 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 CG MSE A 102 CG PRO A 163 1.51 REMARK 500 O THR A 302 O PHE A 315 1.85 REMARK 500 O ASP A 523 OG SER A 527 1.90 REMARK 500 CB SER A 347 OD1 ASN A 367 1.92 REMARK 500 CB ALA A 604 O GLY A 689 1.93 REMARK 500 OD2 ASP A 643 OE2 GLU A 645 1.97 REMARK 500 O LYS A 555 CG GLU A 559 1.97 REMARK 500 N ALA A 435 OD1 ASP A 439 1.98 REMARK 500 CE2 PHE A 173 O LEU A 186 1.98 REMARK 500 OD2 ASP A 403 ND2 ASN A 437 1.99 REMARK 500 O ILE A 605 CD1 PHE A 688 2.00 REMARK 500 O SER A 413 NZ LYS A 672 2.01 REMARK 500 CB VAL A 169 O PHE A 173 2.01 REMARK 500 ND2 ASN A 369 O ASN A 375 2.08 REMARK 500 N VAL A 169 O PHE A 173 2.08 REMARK 500 O LEU A 667 O GLN A 670 2.09 REMARK 500 CB LEU A 208 CG PHE A 251 2.13 REMARK 500 OD2 ASP A 247 OG1 THR A 249 2.13 REMARK 500 O LEU A 443 N LEU A 446 2.14 REMARK 500 O LEU A 293 CD1 LEU A 297 2.14 REMARK 500 OE2 GLU A 716 NH2 ARG A 725 2.17 REMARK 500 CD2 PHE A 173 O LEU A 186 2.18 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 CYS A 226 CB CYS A 226 SG -0.098 REMARK 500 CYS A 241 CB CYS A 241 SG -0.099 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 SER A 74 N - CA - C ANGL. DEV. = 18.1 DEGREES REMARK 500 ASP A 180 N - CA - C ANGL. DEV. = -20.6 DEGREES REMARK 500 GLY A 181 N - CA - C ANGL. DEV. = -18.9 DEGREES REMARK 500 ASN A 240 N - CA - C ANGL. DEV. = 18.0 DEGREES REMARK 500 CYS A 241 CA - CB - SG ANGL. DEV. = -12.8 DEGREES REMARK 500 TYR A 257 CB - CA - C ANGL. DEV. = -14.8 DEGREES REMARK 500 TYR A 257 N - CA - C ANGL. DEV. = -33.2 DEGREES REMARK 500 ASP A 258 N - CA - CB ANGL. DEV. = -14.7 DEGREES REMARK 500 ASP A 258 N - CA - C ANGL. DEV. = -32.1 DEGREES REMARK 500 ASP A 370 N - CA - C ANGL. DEV. = -16.4 DEGREES REMARK 500 TYR A 466 N - CA - C ANGL. DEV. = -17.1 DEGREES REMARK 500 PHE A 562 N - CA - C ANGL. DEV. = -21.6 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 THR A 77 -4.69 84.24 REMARK 500 GLN A 104 127.79 -33.73 REMARK 500 ARG A 105 -1.54 66.18 REMARK 500 THR A 107 41.92 -98.70 REMARK 500 TYR A 156 3.41 80.65 REMARK 500 HIS A 164 -65.11 -143.54 REMARK 500 THR A 209 71.10 -164.29 REMARK 500 SER A 215 -18.24 -146.15 REMARK 500 ASP A 221 -134.58 59.86 REMARK 500 SER A 222 168.46 126.50 REMARK 500 HIS A 230 -128.51 50.34 REMARK 500 GLN A 255 -178.34 151.17 REMARK 500 ASP A 264 -130.00 63.05 REMARK 500 GLU A 278 78.58 -103.57 REMARK 500 ASN A 284 -132.00 52.10 REMARK 500 ASN A 318 -171.69 167.26 REMARK 500 SER A 326 -65.73 -139.99 REMARK 500 GLU A 371 -1.87 85.91 REMARK 500 PHE A 373 44.34 131.70 REMARK 500 HIS A 436 -134.26 62.85 REMARK 500 ALA A 444 -34.07 -37.94 REMARK 500 SER A 461 -21.97 -143.58 REMARK 500 PRO A 541 134.38 -37.91 REMARK 500 ILE A 605 -120.56 61.78 REMARK 500 ASP A 608 113.48 -167.77 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 GLY A 689 15.11 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 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: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 PRO A 18 46.6 L L OUTSIDE RANGE REMARK 500 ASP A 180 45.6 L L OUTSIDE RANGE REMARK 500 ASN A 240 22.6 L L OUTSIDE RANGE REMARK 500 TYR A 257 48.8 L L OUTSIDE RANGE REMARK 500 ASP A 258 62.9 L L OUTSIDE RANGE REMARK 500 PHE A 562 45.9 L L OUTSIDE RANGE REMARK 500 ASP A 671 24.9 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL DBREF 3HXR A 1 757 UNP P35729 NU120_YEAST 1 757 SEQADV 3HXR GLY A -3 UNP P35729 EXPRESSION TAG SEQADV 3HXR PRO A -2 UNP P35729 EXPRESSION TAG SEQADV 3HXR GLY A -1 UNP P35729 EXPRESSION TAG SEQADV 3HXR SER A 0 UNP P35729 EXPRESSION TAG SEQRES 1 A 761 GLY PRO GLY SER MSE ALA CYS LEU SER ARG ILE ASP ALA SEQRES 2 A 761 ASN LEU LEU GLN TYR TYR GLU LYS PRO GLU PRO ASN ASN SEQRES 3 A 761 THR VAL ASP LEU TYR VAL SER ASN ASN SER ASN ASN ASN SEQRES 4 A 761 GLY LEU LYS GLU GLY ASP LYS SER ILE SER THR PRO VAL SEQRES 5 A 761 PRO GLN PRO TYR GLY SER GLU TYR SER ASN CYS LEU LEU SEQRES 6 A 761 LEU SER ASN SER GLU TYR ILE CYS TYR HIS PHE SER SER SEQRES 7 A 761 ARG SER THR LEU LEU THR PHE TYR PRO LEU SER ASP ALA SEQRES 8 A 761 TYR HIS GLY LYS THR ILE ASN ILE HIS LEU PRO ASN ALA SEQRES 9 A 761 SER MSE ASN GLN ARG TYR THR LEU THR ILE GLN GLU VAL SEQRES 10 A 761 GLU GLN GLN LEU LEU VAL ASN VAL ILE LEU LYS ASP GLY SEQRES 11 A 761 SER PHE LEU THR LEU GLN LEU PRO LEU SER PHE LEU PHE SEQRES 12 A 761 SER SER ALA ASN THR LEU ASN GLY GLU TRP PHE HIS LEU SEQRES 13 A 761 GLN ASN PRO TYR ASP PHE THR VAL ARG VAL PRO HIS PHE SEQRES 14 A 761 LEU PHE TYR VAL SER PRO GLN PHE SER VAL VAL PHE LEU SEQRES 15 A 761 GLU ASP GLY GLY LEU LEU GLY LEU LYS LYS VAL ASP GLY SEQRES 16 A 761 VAL HIS TYR GLU PRO LEU LEU PHE ASN ASP ASN SER TYR SEQRES 17 A 761 LEU LYS SER LEU THR ARG PHE PHE SER ARG SER SER LYS SEQRES 18 A 761 SER ASP TYR ASP SER VAL ILE SER CYS LYS LEU PHE HIS SEQRES 19 A 761 GLU ARG TYR LEU ILE VAL LEU THR GLN ASN CYS HIS LEU SEQRES 20 A 761 LYS ILE TRP ASP LEU THR SER PHE THR LEU ILE GLN ASP SEQRES 21 A 761 TYR ASP MSE VAL SER GLN SER ASP SER ASP PRO SER HIS SEQRES 22 A 761 PHE ARG LYS VAL GLU ALA VAL GLY GLU TYR LEU SER LEU SEQRES 23 A 761 TYR ASN ASN THR LEU VAL THR LEU LEU PRO LEU GLU ASN SEQRES 24 A 761 GLY LEU PHE GLN MSE GLY THR LEU LEU VAL ASP SER SER SEQRES 25 A 761 GLY ILE LEU THR TYR THR PHE GLN ASN ASN ILE PRO THR SEQRES 26 A 761 ASN LEU SER ALA SER ALA ILE TRP SER ILE VAL ASP LEU SEQRES 27 A 761 VAL LEU THR ARG PRO LEU GLU LEU ASN VAL GLU ALA SER SEQRES 28 A 761 TYR LEU ASN LEU ILE VAL LEU TRP LYS SER GLY THR ALA SEQRES 29 A 761 SER LYS LEU GLN ILE LEU ASN VAL ASN ASP GLU SER PHE SEQRES 30 A 761 LYS ASN TYR GLU TRP ILE GLU SER VAL ASN LYS SER LEU SEQRES 31 A 761 VAL ASP LEU GLN SER GLU HIS ASP LEU ASP ILE VAL THR SEQRES 32 A 761 LYS THR GLY ASP VAL GLU ARG GLY PHE CYS ASN LEU LYS SEQRES 33 A 761 SER ARG TYR GLY THR GLN ILE PHE GLU ARG ALA GLN GLN SEQRES 34 A 761 ILE LEU SER GLU ASN LYS ILE ILE MSE ALA HIS ASN GLU SEQRES 35 A 761 ASP GLU GLU TYR LEU ALA ASN LEU GLU THR ILE LEU ARG SEQRES 36 A 761 ASP VAL LYS THR ALA PHE ASN GLU ALA SER SER ILE THR SEQRES 37 A 761 LEU TYR GLY ASP GLU ILE ILE LEU VAL ASN CYS PHE GLN SEQRES 38 A 761 PRO TYR ASN HIS SER LEU TYR LYS LEU ASN THR THR VAL SEQRES 39 A 761 GLU ASN TRP PHE TYR ASN MSE HIS SER GLU THR ASP GLY SEQRES 40 A 761 SER GLU LEU PHE LYS TYR LEU ARG THR LEU ASN GLY PHE SEQRES 41 A 761 ALA SER THR LEU SER ASN ASP VAL LEU ARG SER ILE SER SEQRES 42 A 761 LYS LYS PHE LEU ASP ILE ILE THR GLY GLU LEU PRO ASP SEQRES 43 A 761 SER MSE THR THR VAL GLU LYS PHE THR ASP ILE PHE LYS SEQRES 44 A 761 ASN CYS LEU GLU ASN GLN PHE GLU ILE THR ASN LEU LYS SEQRES 45 A 761 ILE LEU PHE ASP GLU LEU ASN SER PHE ASP ILE PRO VAL SEQRES 46 A 761 VAL LEU ASN ASP LEU ILE ASN ASN GLN MSE LYS PRO GLY SEQRES 47 A 761 ILE PHE TRP LYS LYS ASP PHE ILE SER ALA ILE LYS PHE SEQRES 48 A 761 ASP GLY PHE THR SER ILE ILE SER LEU GLU SER LEU HIS SEQRES 49 A 761 GLN LEU LEU SER ILE HIS TYR ARG ILE THR LEU GLN VAL SEQRES 50 A 761 LEU LEU THR PHE VAL LEU PHE ASP LEU ASP THR GLU ILE SEQRES 51 A 761 PHE GLY GLN HIS ILE SER THR LEU LEU ASP LEU HIS TYR SEQRES 52 A 761 LYS GLN PHE LEU LEU LEU ASN LEU TYR ARG GLN ASP LYS SEQRES 53 A 761 CYS LEU LEU ALA GLU VAL LEU LEU LYS ASP SER SER GLU SEQRES 54 A 761 PHE SER PHE GLY VAL LYS PHE PHE ASN TYR GLY GLN LEU SEQRES 55 A 761 ILE ALA TYR ILE ASP SER LEU ASN SER ASN VAL TYR ASN SEQRES 56 A 761 ALA SER ILE THR GLU ASN SER PHE PHE MSE THR PHE PHE SEQRES 57 A 761 ARG SER TYR ILE ILE GLU ASN THR SER HIS LYS ASN ILE SEQRES 58 A 761 ARG PHE PHE LEU GLU ASN VAL GLU CYS PRO PHE TYR LEU SEQRES 59 A 761 ARG HIS ASN GLU VAL GLN GLU MODRES 3HXR MSE A 1 MET SELENOMETHIONINE MODRES 3HXR MSE A 102 MET SELENOMETHIONINE MODRES 3HXR MSE A 259 MET SELENOMETHIONINE MODRES 3HXR MSE A 300 MET SELENOMETHIONINE MODRES 3HXR MSE A 434 MET SELENOMETHIONINE MODRES 3HXR MSE A 497 MET SELENOMETHIONINE MODRES 3HXR MSE A 544 MET SELENOMETHIONINE MODRES 3HXR MSE A 591 MET SELENOMETHIONINE MODRES 3HXR MSE A 721 MET SELENOMETHIONINE HET MSE A 1 8 HET MSE A 102 8 HET MSE A 259 8 HET MSE A 300 8 HET MSE A 434 8 HET MSE A 497 8 HET MSE A 544 8 HET MSE A 591 8 HET MSE A 721 8 HETNAM MSE SELENOMETHIONINE FORMUL 1 MSE 9(C5 H11 N O2 SE) HELIX 1 1 LEU A 135 SER A 140 1 6 HELIX 2 2 ASN A 369 LYS A 374 1 6 HELIX 3 3 SER A 385 HIS A 393 1 9 HELIX 4 4 ASP A 403 ASN A 430 1 28 HELIX 5 5 ASP A 439 ASN A 458 1 20 HELIX 6 6 THR A 488 ASN A 496 1 9 HELIX 7 7 GLU A 505 SER A 518 1 14 HELIX 8 8 SER A 521 GLY A 538 1 18 HELIX 9 9 THR A 545 LEU A 558 1 14 HELIX 10 10 GLU A 563 ASN A 575 1 13 HELIX 11 11 ASP A 578 ASN A 589 1 12 HELIX 12 12 GLY A 609 PHE A 640 1 32 HELIX 13 13 PHE A 647 SER A 683 1 37 HELIX 14 14 ASN A 694 ASN A 711 1 18 HELIX 15 15 SER A 718 GLU A 730 1 13 SHEET 1 1 1 LEU A 4 ASN A 10 0 SHEET 2 2 1 THR A 23 LEU A 26 0 SHEET 3 3 1 TYR A 56 LEU A 61 0 SHEET 4 4 1 TYR A 67 PHE A 72 0 SHEET 5 5 1 LEU A 78 PRO A 83 0 SHEET 6 6 1 THR A 92 HIS A 96 0 SHEET 7 7 1 LEU A 108 GLU A 112 0 SHEET 8 8 1 GLN A 116 ILE A 122 0 SHEET 9 9 1 PHE A 128 PRO A 134 0 SHEET 10 10 1 PHE A 165 VAL A 169 0 SHEET 11 11 1 PHE A 173 PHE A 177 0 SHEET 12 12 1 LEU A 183 LEU A 186 0 SHEET 13 13 1 VAL A 223 PHE A 229 0 SHEET 14 14 1 TYR A 233 THR A 238 0 SHEET 15 15 1 LEU A 243 LYS A 244 0 SHEET 16 16 1 LEU A 280 TYR A 283 0 SHEET 17 17 1 THR A 286 LEU A 291 0 SHEET 18 18 1 LEU A 297 GLY A 301 0 SHEET 19 19 1 SER A 330 THR A 337 0 SHEET 20 20 1 LEU A 349 SER A 357 0 SHEET 21 21 1 ALA A 360 VAL A 368 0 SHEET 22 22 1 TYR A 376 ILE A 379 0 SHEET 23 23 1 ALA A 460 TYR A 466 0 SHEET 24 24 1 ILE A 470 CYS A 475 0 SHEET 25 25 1 ASN A 480 LEU A 486 0 LINK C SER A 0 N MSE A 1 1555 1555 1.32 LINK C MSE A 1 N ALA A 2 1555 1555 1.32 LINK C SER A 101 N MSE A 102 1555 1555 1.33 LINK C MSE A 102 N ASN A 103 1555 1555 1.32 LINK C ASP A 258 N MSE A 259 1555 1555 1.33 LINK C MSE A 259 N VAL A 260 1555 1555 1.33 LINK C GLN A 299 N MSE A 300 1555 1555 1.33 LINK C MSE A 300 N GLY A 301 1555 1555 1.32 LINK C ILE A 433 N MSE A 434 1555 1555 1.33 LINK C MSE A 434 N ALA A 435 1555 1555 1.33 LINK C ASN A 496 N MSE A 497 1555 1555 1.31 LINK C MSE A 497 N HIS A 498 1555 1555 1.32 LINK C SER A 543 N MSE A 544 1555 1555 1.32 LINK C MSE A 544 N THR A 545 1555 1555 1.33 LINK C GLN A 590 N MSE A 591 1555 1555 1.31 LINK C MSE A 591 N LYS A 592 1555 1555 1.32 LINK C PHE A 720 N MSE A 721 1555 1555 1.32 LINK C MSE A 721 N THR A 722 1555 1555 1.32 CISPEP 1 PRO A 18 GLU A 19 0 0.68 CISPEP 2 SER A 74 ARG A 75 0 -15.20 CISPEP 3 ASN A 240 CYS A 241 0 5.04 CISPEP 4 LEU A 248 THR A 249 0 -7.34 CISPEP 5 MSE A 259 VAL A 260 0 -0.08 CISPEP 6 LEU A 293 GLU A 294 0 -3.22 CISPEP 7 GLY A 467 ASP A 468 0 4.96 CISPEP 8 ILE A 602 SER A 603 0 -3.19 CISPEP 9 SER A 603 ALA A 604 0 -1.04 CISPEP 10 ASP A 608 GLY A 609 0 11.35 CRYST1 114.600 153.690 52.980 90.00 90.00 90.00 P 21 21 2 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.008726 0.000000 0.000000 0.00000 SCALE2 0.000000 0.006507 0.000000 0.00000 SCALE3 0.000000 0.000000 0.018875 0.00000 ATOM 1 N SER A 0 -8.978 228.957 796.404 1.00125.46 N ANISOU 1 N SER A 0 10447 15927 21297 -1338 -699 -962 N ATOM 2 CA SER A 0 -9.308 230.228 797.026 1.00126.89 C ANISOU 2 CA SER A 0 11155 15974 21085 -1245 -507 -899 C ATOM 3 C SER A 0 -8.201 230.629 797.957 1.00118.33 C ANISOU 3 C SER A 0 10649 14732 19580 -1500 -574 -543 C ATOM 4 O SER A 0 -8.214 230.258 799.113 1.00121.04 O ANISOU 4 O SER A 0 11014 15329 19648 -1793 -283 -435 O ATOM 5 CB SER A 0 -10.578 230.080 797.837 1.00132.74 C ANISOU 5 CB SER A 0 11627 17141 21667 -1293 35 -1112 C ATOM 6 OG SER A 0 -10.322 229.349 799.012 1.00135.60 O ANISOU 6 OG SER A 0 11950 17824 21747 -1695 303 -937 O ATOM 7 N MSE A 1 -7.238 231.390 797.466 1.00107.85 N ANISOU 7 N MSE A 1 9804 12985 18188 -1382 -964 -362 N ATOM 8 CA MSE A 1 -6.142 231.796 798.322 1.00108.12 C ANISOU 8 CA MSE A 1 10389 12863 17829 -1579 -1043 -70 C ATOM 9 C MSE A 1 -6.419 233.034 799.152 1.00100.18 C ANISOU 9 C MSE A 1 9837 11805 16421 -1521 -785 -5 C ATOM 10 O MSE A 1 -7.184 233.887 798.767 1.00100.44 O ANISOU 10 O MSE A 1 9913 11766 16484 -1280 -687 -131 O ATOM 11 CB MSE A 1 -4.859 231.931 797.529 1.00119.70 C ANISOU 11 CB MSE A 1 12168 13960 19352 -1512 -1569 87 C ATOM 12 CG MSE A 1 -3.734 231.190 798.174 1.00127.71 C ANISOU 12 CG MSE A 1 13305 14965 20253 -1828 -1734 278 C ATOM 13 SE MSE A 1 -2.073 231.594 797.370 1.00143.46 Se ANISOU 13 SE MSE A 1 15845 16489 22175 -1721 -2382 454 Se ATOM 14 CE MSE A 1 -2.467 233.376 796.751 1.00 98.63 C ANISOU 14 CE MSE A 1 10630 10567 16276 -1320 -2337 450 C ATOM 15 N ALA A 2 -5.765 233.101 800.299 1.00 92.92 N ANISOU 15 N ALA A 2 9245 10904 15157 -1748 -705 192 N ATOM 16 CA ALA A 2 -5.899 234.178 801.285 1.00 84.53 C ANISOU 16 CA ALA A 2 8595 9818 13706 -1729 -474 266 C ATOM 17 C ALA A 2 -4.783 235.217 801.161 1.00 82.64 C ANISOU 17 C ALA A 2 8933 9227 13241 -1612 -734 437 C ATOM 18 O ALA A 2 -3.632 234.948 801.501 1.00 89.49 O ANISOU 18 O ALA A 2 10062 9966 13974 -1745 -957 597 O ATOM 19 CB ALA A 2 -5.925 233.605 802.692 1.00 78.11 C ANISOU 19 CB ALA A 2 7777 9250 12650 -2034 -229 365 C ATOM 20 N CYS A 3 -5.139 236.412 800.701 1.00 75.72 N ANISOU 20 N CYS A 3 8254 8202 12316 -1371 -696 397 N ATOM 21 CA CYS A 3 -4.150 237.438 800.385 1.00 72.65 C ANISOU 21 CA CYS A 3 8373 7517 11715 -1242 -915 549 C ATOM 22 C CYS A 3 -4.170 238.648 801.317 1.00 70.27 C ANISOU 22 C CYS A 3 8423 7211 11064 -1209 -669 608 C ATOM 23 O CYS A 3 -3.405 239.587 801.117 1.00 71.92 O ANISOU 23 O CYS A 3 9034 7225 11066 -1102 -782 722 O ATOM 24 CB CYS A 3 -4.326 237.914 798.940 1.00 67.09 C ANISOU 24 CB CYS A 3 7665 6593 11232 -1006 -1135 519 C ATOM 25 SG CYS A 3 -4.246 236.604 797.706 1.00103.32 S ANISOU 25 SG CYS A 3 11835 11146 16276 -980 -1502 431 S ATOM 26 N LEU A 4 -5.039 238.634 802.321 1.00 63.09 N ANISOU 26 N LEU A 4 7355 6535 10083 -1298 -338 526 N ATOM 27 CA LEU A 4 -5.139 239.760 803.241 1.00 53.87 C ANISOU 27 CA LEU A 4 6463 5378 8626 -1261 -121 558 C ATOM 28 C LEU A 4 -5.120 239.299 804.702 1.00 57.21 C ANISOU 28 C LEU A 4 6902 6008 8827 -1430 33 585 C ATOM 29 O LEU A 4 -5.823 238.354 805.063 1.00 62.35 O ANISOU 29 O LEU A 4 7236 6882 9573 -1584 169 517 O ATOM 30 CB LEU A 4 -6.414 240.556 802.969 1.00 52.91 C ANISOU 30 CB LEU A 4 6181 5303 8620 -1129 103 411 C ATOM 31 CG LEU A 4 -6.761 240.908 801.521 1.00 61.78 C ANISOU 31 CG LEU A 4 7221 6231 10020 -949 -47 362 C ATOM 32 CD1 LEU A 4 -7.874 241.943 801.482 1.00 63.92 C ANISOU 32 CD1 LEU A 4 7445 6487 10356 -841 162 247 C ATOM 33 CD2 LEU A 4 -5.550 241.429 800.782 1.00 67.03 C ANISOU 33 CD2 LEU A 4 8260 6627 10580 -871 -328 555 C ATOM 34 N SER A 5 -4.314 239.956 805.537 1.00 50.04 N ANISOU 34 N SER A 5 6354 5074 7587 -1354 -2 667 N ATOM 35 CA SER A 5 -4.318 239.666 806.975 1.00 54.85 C ANISOU 35 CA SER A 5 7026 5855 7960 -1446 94 685 C ATOM 36 C SER A 5 -5.288 240.593 807.682 1.00 58.62 C ANISOU 36 C SER A 5 7486 6487 8302 -1326 356 567 C ATOM 37 O SER A 5 -5.580 241.688 807.201 1.00 51.12 O ANISOU 37 O SER A 5 6573 5478 7374 -1157 433 502 O ATOM 38 CB SER A 5 -2.943 239.872 807.608 1.00 51.74 C ANISOU 38 CB SER A 5 7006 5329 7323 -1430 -119 787 C ATOM 39 OG SER A 5 -1.917 239.787 806.654 1.00 64.01 O ANISOU 39 OG SER A 5 8717 6657 8948 -1405 -388 853 O ATOM 40 N ARG A 6 -5.721 240.213 808.873 1.00 50.59 N ANISOU 40 N ARG A 6 6447 5645 7132 -1428 463 555 N ATOM 41 CA ARG A 6 -6.601 241.059 809.649 1.00 52.69 C ANISOU 41 CA ARG A 6 6720 6031 7267 -1330 658 437 C ATOM 42 C ARG A 6 -5.695 241.607 810.720 1.00 41.08 C ANISOU 42 C ARG A 6 5556 4499 5555 -1284 550 504 C ATOM 43 O ARG A 6 -4.954 240.879 811.313 1.00 41.14 O ANISOU 43 O ARG A 6 5691 4469 5471 -1417 397 624 O ATOM 44 CB ARG A 6 -7.770 240.306 810.259 1.00 60.68 C ANISOU 44 CB ARG A 6 7516 7285 8254 -1477 835 362 C ATOM 45 CG ARG A 6 -8.561 241.137 811.229 1.00 69.04 C ANISOU 45 CG ARG A 6 8639 8444 9151 -1403 966 253 C ATOM 46 CD ARG A 6 -10.002 240.757 811.296 1.00 78.66 C ANISOU 46 CD ARG A 6 9601 9889 10398 -1473 1174 91 C ATOM 47 NE ARG A 6 -10.333 240.044 812.512 1.00 86.47 N ANISOU 47 NE ARG A 6 10615 11092 11147 -1666 1224 152 N ATOM 48 CZ ARG A 6 -11.472 240.181 813.177 1.00 87.03 C ANISOU 48 CZ ARG A 6 10610 11370 11088 -1700 1377 23 C ATOM 49 NH1 ARG A 6 -12.398 241.022 812.762 1.00 75.53 N ANISOU 49 NH1 ARG A 6 9041 9913 9744 -1548 1482 -200 N ATOM 50 NH2 ARG A 6 -11.677 239.482 814.269 1.00 86.05 N ANISOU 50 NH2 ARG A 6 10534 11446 10715 -1906 1411 131 N ATOM 51 N ILE A 7 -5.754 242.901 810.944 1.00 32.66 N ANISOU 51 N ILE A 7 4589 3403 4416 -1109 624 423 N ATOM 52 CA ILE A 7 -4.929 243.593 811.924 1.00 33.75 C ANISOU 52 CA ILE A 7 4978 3479 4367 -1037 551 445 C ATOM 53 C ILE A 7 -5.831 244.368 812.865 1.00 40.27 C ANISOU 53 C ILE A 7 5757 4408 5136 -985 703 344 C ATOM 54 O ILE A 7 -6.465 245.333 812.451 1.00 49.38 O ANISOU 54 O ILE A 7 6810 5576 6378 -872 845 239 O ATOM 55 CB ILE A 7 -3.947 244.548 811.229 1.00 33.83 C ANISOU 55 CB ILE A 7 5153 3351 4351 -883 505 448 C ATOM 56 CG2 ILE A 7 -3.016 245.177 812.237 1.00 38.87 C ANISOU 56 CG2 ILE A 7 6047 3912 4810 -805 442 451 C ATOM 57 CG1 ILE A 7 -3.129 243.798 810.179 1.00 36.00 C ANISOU 57 CG1 ILE A 7 5485 3504 4690 -938 319 543 C ATOM 58 CD1 ILE A 7 -2.012 242.956 810.749 1.00 36.33 C ANISOU 58 CD1 ILE A 7 5738 3432 4632 -1041 73 638 C ATOM 59 N ASP A 8 -5.895 243.954 814.127 1.00 41.25 N ANISOU 59 N ASP A 8 5965 4581 5127 -1087 649 393 N ATOM 60 CA ASP A 8 -6.857 244.544 815.062 1.00 43.04 C ANISOU 60 CA ASP A 8 6139 4913 5301 -1073 762 313 C ATOM 61 C ASP A 8 -6.365 245.796 815.794 1.00 49.69 C ANISOU 61 C ASP A 8 7122 5665 6093 -924 755 289 C ATOM 62 O ASP A 8 -5.362 245.761 816.513 1.00 43.34 O ANISOU 62 O ASP A 8 6542 4738 5186 -907 604 381 O ATOM 63 CB ASP A 8 -7.317 243.505 816.079 1.00 43.72 C ANISOU 63 CB ASP A 8 6244 5117 5250 -1284 720 408 C ATOM 64 CG ASP A 8 -8.132 242.401 815.452 1.00 57.54 C ANISOU 64 CG ASP A 8 7780 7033 7050 -1444 821 397 C ATOM 65 OD1 ASP A 8 -8.927 242.697 814.534 1.00 49.23 O ANISOU 65 OD1 ASP A 8 6526 6036 6143 -1364 967 244 O ATOM 66 OD2 ASP A 8 -7.975 241.237 815.885 1.00 57.87 O ANISOU 66 OD2 ASP A 8 7852 7139 6998 -1663 758 546 O ATOM 67 N ALA A 9 -7.089 246.899 815.621 1.00 41.18 N ANISOU 67 N ALA A 9 5909 4630 5109 -823 911 166 N ATOM 68 CA ALA A 9 -6.757 248.140 816.314 1.00 34.98 C ANISOU 68 CA ALA A 9 5189 3789 4312 -706 952 148 C ATOM 69 C ALA A 9 -7.745 248.464 817.426 1.00 38.56 C ANISOU 69 C ALA A 9 5561 4356 4735 -757 994 108 C ATOM 70 O ALA A 9 -8.833 248.961 817.165 1.00 43.39 O ANISOU 70 O ALA A 9 5968 5066 5453 -760 1114 -25 O ATOM 71 CB ALA A 9 -6.685 249.295 815.339 1.00 33.77 C ANISOU 71 CB ALA A 9 4943 3591 4295 -587 1096 75 C ATOM 72 N ASN A 10 -7.364 248.186 818.666 1.00 37.08 N ANISOU 72 N ASN A 10 5555 4134 4401 -783 853 216 N ATOM 73 CA ASN A 10 -8.078 248.734 819.808 1.00 37.80 C ANISOU 73 CA ASN A 10 5590 4335 4438 -721 803 123 C ATOM 74 C ASN A 10 -7.425 250.067 820.153 1.00 42.33 C ANISOU 74 C ASN A 10 6151 4839 5092 -482 789 20 C ATOM 75 O ASN A 10 -6.277 250.111 820.585 1.00 42.83 O ANISOU 75 O ASN A 10 6413 4760 5101 -352 642 65 O ATOM 76 CB ASN A 10 -8.003 247.783 820.993 1.00 48.13 C ANISOU 76 CB ASN A 10 7110 5637 5542 -811 580 258 C ATOM 77 CG ASN A 10 -8.962 248.156 822.094 1.00 50.66 C ANISOU 77 CG ASN A 10 7377 6100 5771 -782 507 175 C ATOM 78 OD1 ASN A 10 -8.560 248.380 823.233 1.00 62.54 O ANISOU 78 OD1 ASN A 10 9041 7524 7198 -669 278 206 O ATOM 79 ND2 ASN A 10 -10.239 248.224 821.762 1.00 49.68 N ANISOU 79 ND2 ASN A 10 7038 6177 5662 -867 669 52 N ATOM 80 N LEU A 11 -8.155 251.149 819.935 1.00 28.01 N ANISOU 80 N LEU A 11 4090 3128 3425 -427 943 -131 N ATOM 81 CA LEU A 11 -7.589 252.486 820.008 1.00 38.22 C ANISOU 81 CA LEU A 11 5290 4402 4829 -236 1011 -230 C ATOM 82 C LEU A 11 -7.064 252.876 821.397 1.00 47.89 C ANISOU 82 C LEU A 11 6594 5606 5997 -40 804 -289 C ATOM 83 O LEU A 11 -6.151 253.692 821.510 1.00 52.83 O ANISOU 83 O LEU A 11 7213 6194 6667 155 830 -356 O ATOM 84 CB LEU A 11 -8.612 253.498 819.517 1.00 30.95 C ANISOU 84 CB LEU A 11 4062 3589 4110 -275 1203 -360 C ATOM 85 CG LEU A 11 -8.986 253.334 818.056 1.00 32.04 C ANISOU 85 CG LEU A 11 4126 3692 4357 -417 1386 -314 C ATOM 86 CD1 LEU A 11 -9.872 254.472 817.600 1.00 44.18 C ANISOU 86 CD1 LEU A 11 5388 5270 6128 -452 1535 -433 C ATOM 87 CD2 LEU A 11 -7.724 253.255 817.227 1.00 40.58 C ANISOU 87 CD2 LEU A 11 5380 4652 5387 -372 1438 -186 C ATOM 88 N LEU A 12 -7.643 252.289 822.438 1.00 41.06 N ANISOU 88 N LEU A 12 5806 4771 5024 -82 594 -268 N ATOM 89 CA LEU A 12 -7.232 252.548 823.807 1.00 42.17 C ANISOU 89 CA LEU A 12 6046 4857 5118 108 328 -309 C ATOM 90 C LEU A 12 -6.219 251.512 824.272 1.00 54.14 C ANISOU 90 C LEU A 12 7921 6171 6476 117 84 -144 C ATOM 91 O LEU A 12 -5.814 251.500 825.436 1.00 46.42 O ANISOU 91 O LEU A 12 7099 5087 5453 266 -204 -142 O ATOM 92 CB LEU A 12 -8.448 252.504 824.725 1.00 37.01 C ANISOU 92 CB LEU A 12 5318 4332 4413 51 186 -357 C ATOM 93 CG LEU A 12 -9.604 253.413 824.320 1.00 45.45 C ANISOU 93 CG LEU A 12 6044 5577 5649 9 372 -535 C ATOM 94 CD1 LEU A 12 -10.820 253.168 825.203 1.00 49.84 C ANISOU 94 CD1 LEU A 12 6585 6262 6090 -61 196 -587 C ATOM 95 CD2 LEU A 12 -9.171 254.864 824.378 1.00 49.31 C ANISOU 95 CD2 LEU A 12 6284 6081 6371 214 452 -699 C ATOM 96 N GLN A 13 -5.834 250.641 823.373 1.00 63.88 N ANISOU 96 N GLN A 13 9284 7335 7653 -44 165 -7 N ATOM 97 CA GLN A 13 -4.941 249.569 823.721 1.00 78.28 C ANISOU 97 CA GLN A 13 11436 8951 9355 -95 -76 164 C ATOM 98 C GLN A 13 -3.627 249.951 824.338 1.00 80.55 C ANISOU 98 C GLN A 13 11919 9025 9662 176 -296 102 C ATOM 99 O GLN A 13 -3.228 249.373 825.329 1.00 71.62 O ANISOU 99 O GLN A 13 11041 7714 8459 201 -617 197 O ATOM 100 CB GLN A 13 -4.673 248.781 822.452 1.00 80.81 C ANISOU 100 CB GLN A 13 11790 9243 9673 -286 71 275 C ATOM 101 CG GLN A 13 -3.478 247.898 822.509 1.00 91.59 C ANISOU 101 CG GLN A 13 13463 10361 10976 -313 -156 411 C ATOM 102 CD GLN A 13 -3.842 246.445 822.530 1.00103.89 C ANISOU 102 CD GLN A 13 15123 11910 12441 -634 -240 636 C ATOM 103 NE2 GLN A 13 -3.130 245.665 823.324 1.00106.39 N ANISOU 103 NE2 GLN A 13 15735 12003 12686 -690 -550 792 N ATOM 104 OE1 GLN A 13 -4.745 246.023 821.828 1.00104.46 O ANISOU 104 OE1 GLN A 13 15002 12171 12518 -832 -28 666 O ATOM 105 N TYR A 14 -2.955 250.929 823.786 1.00 80.60 N ANISOU 105 N TYR A 14 11819 9047 9759 383 -134 -61 N ATOM 106 CA TYR A 14 -1.690 251.327 824.341 1.00 78.22 C ANISOU 106 CA TYR A 14 11685 8571 9464 680 -319 -176 C ATOM 107 C TYR A 14 -1.812 251.881 825.752 1.00 75.44 C ANISOU 107 C TYR A 14 11301 8193 9169 910 -558 -294 C ATOM 108 O TYR A 14 -0.894 251.782 826.540 1.00 64.96 O ANISOU 108 O TYR A 14 10196 6647 7841 1126 -854 -345 O ATOM 109 CB TYR A 14 -0.963 252.219 823.357 1.00 81.20 C ANISOU 109 CB TYR A 14 11956 9025 9871 831 -46 -320 C ATOM 110 CG TYR A 14 -0.609 251.399 822.168 1.00 87.57 C ANISOU 110 CG TYR A 14 12914 9760 10600 630 30 -174 C ATOM 111 CD2 TYR A 14 -0.996 250.084 822.120 1.00 94.18 C ANISOU 111 CD2 TYR A 14 13888 10503 11392 354 -116 33 C ATOM 112 CE2 TYR A 14 -0.689 249.292 821.062 1.00 99.24 C ANISOU 112 CE2 TYR A 14 14627 11079 12000 173 -78 155 C ATOM 113 CZ TYR A 14 0.014 249.803 820.020 1.00 99.30 C ANISOU 113 CZ TYR A 14 14642 11097 11988 270 79 84 C ATOM 114 OH TYR A 14 0.290 248.968 818.983 1.00 98.21 O ANISOU 114 OH TYR A 14 14602 10884 11830 94 65 208 O ATOM 115 CE1 TYR A 14 0.419 251.110 820.026 1.00 95.72 C ANISOU 115 CE1 TYR A 14 14090 10747 11532 531 246 -100 C ATOM 116 CD1 TYR A 14 0.110 251.906 821.110 1.00 92.03 C ANISOU 116 CD1 TYR A 14 13479 10361 11126 708 234 -236 C ATOM 117 N TYR A 15 -2.948 252.480 826.055 1.00 70.67 N ANISOU 117 N TYR A 15 10418 7798 8634 877 -459 -354 N ATOM 118 CA TYR A 15 -3.199 253.055 827.360 1.00 61.90 C ANISOU 118 CA TYR A 15 9235 6688 7598 1092 -703 -474 C ATOM 119 C TYR A 15 -3.640 252.075 828.424 1.00 62.41 C ANISOU 119 C TYR A 15 9563 6615 7535 975 -1079 -285 C ATOM 120 O TYR A 15 -4.205 251.060 828.118 1.00 71.80 O ANISOU 120 O TYR A 15 10880 7825 8578 663 -1052 -71 O ATOM 121 CB TYR A 15 -4.091 254.237 827.153 1.00 59.66 C ANISOU 121 CB TYR A 15 8525 6678 7466 1121 -445 -645 C ATOM 122 CG TYR A 15 -3.465 255.006 826.051 1.00 64.61 C ANISOU 122 CG TYR A 15 8984 7398 8168 1186 -88 -751 C ATOM 123 CD1 TYR A 15 -2.442 255.868 826.305 1.00 73.64 C ANISOU 123 CD1 TYR A 15 10056 8536 9389 1505 -68 -948 C ATOM 124 CE1 TYR A 15 -1.830 256.535 825.314 1.00 80.20 C ANISOU 124 CE1 TYR A 15 10771 9476 10224 1550 269 -1023 C ATOM 125 CZ TYR A 15 -2.211 256.328 824.042 1.00 80.48 C ANISOU 125 CZ TYR A 15 10786 9583 10211 1279 547 -880 C ATOM 126 OH TYR A 15 -1.579 257.011 823.054 1.00 79.56 O ANISOU 126 OH TYR A 15 10592 9570 10069 1316 864 -922 O ATOM 127 CE2 TYR A 15 -3.198 255.454 823.755 1.00 69.99 C ANISOU 127 CE2 TYR A 15 9516 8228 8847 985 506 -703 C ATOM 128 CD2 TYR A 15 -3.806 254.783 824.755 1.00 64.95 C ANISOU 128 CD2 TYR A 15 8979 7521 8179 938 210 -646 C ATOM 129 N GLU A 16 -3.359 252.385 829.674 1.00 63.41 N ANISOU 129 N GLU A 16 9771 6608 7716 1231 -1432 -363 N ATOM 130 CA GLU A 16 -3.696 251.506 830.778 1.00 77.44 C ANISOU 130 CA GLU A 16 11848 8222 9354 1133 -1840 -154 C ATOM 131 C GLU A 16 -4.994 251.955 831.425 1.00 76.82 C ANISOU 131 C GLU A 16 11569 8359 9260 1107 -1897 -198 C ATOM 132 O GLU A 16 -5.293 251.583 832.557 1.00 73.66 O ANISOU 132 O GLU A 16 11379 7849 8759 1121 -2282 -80 O ATOM 133 CB GLU A 16 -2.562 251.522 831.803 1.00 91.03 C ANISOU 133 CB GLU A 16 13832 9602 11153 1452 -2279 -204 C ATOM 134 CG GLU A 16 -2.141 250.155 832.316 1.00104.59 C ANISOU 134 CG GLU A 16 16034 10989 12716 1261 -2645 111 C ATOM 135 CD GLU A 16 -0.830 250.213 833.084 1.00122.94 C ANISOU 135 CD GLU A 16 18627 12916 15169 1603 -3064 17 C ATOM 136 OE1 GLU A 16 -0.487 251.304 833.592 1.00130.11 O ANISOU 136 OE1 GLU A 16 19340 13831 16264 2019 -3152 -289 O ATOM 137 OE2 GLU A 16 -0.140 249.173 833.177 1.00124.20 O ANISOU 137 OE2 GLU A 16 19175 12753 15262 1459 -3312 231 O ATOM 138 N LYS A 17 -5.767 252.760 830.703 1.00 82.16 N ANISOU 138 N LYS A 17 11858 9325 10034 1062 -1539 -364 N ATOM 139 CA LYS A 17 -7.011 253.291 831.246 1.00 84.36 C ANISOU 139 CA LYS A 17 11917 9810 10328 1047 -1598 -457 C ATOM 140 C LYS A 17 -8.048 253.629 830.177 1.00 98.44 C ANISOU 140 C LYS A 17 13385 11870 12146 830 -1189 -537 C ATOM 141 O LYS A 17 -7.903 254.614 829.457 1.00106.05 O ANISOU 141 O LYS A 17 14028 12935 13329 917 -904 -721 O ATOM 142 CB LYS A 17 -6.728 254.535 832.094 1.00 70.30 C ANISOU 142 CB LYS A 17 9893 8022 8796 1427 -1793 -720 C ATOM 143 N PRO A 18 -9.059 252.797 830.054 1.00101.85 N ANISOU 143 N PRO A 18 13921 12418 12361 546 -1158 -398 N ATOM 144 CA PRO A 18 -10.109 253.023 829.085 1.00108.26 C ANISOU 144 CA PRO A 18 14465 13458 13210 356 -823 -496 C ATOM 145 C PRO A 18 -11.083 253.688 829.980 1.00131.43 C ANISOU 145 C PRO A 18 17245 16521 16172 441 -1032 -653 C ATOM 146 O PRO A 18 -11.118 253.235 831.111 1.00147.55 O ANISOU 146 O PRO A 18 19538 18494 18032 488 -1393 -546 O ATOM 147 CB PRO A 18 -10.636 251.635 828.885 1.00 95.01 C ANISOU 147 CB PRO A 18 13037 11832 11231 58 -792 -277 C ATOM 148 CG PRO A 18 -10.630 251.124 830.246 1.00 91.63 C ANISOU 148 CG PRO A 18 12907 11319 10588 91 -1197 -130 C ATOM 149 CD PRO A 18 -9.333 251.580 830.820 1.00 94.54 C ANISOU 149 CD PRO A 18 13368 11428 11124 375 -1432 -143 C ATOM 150 N GLU A 19 -11.836 254.695 829.574 1.00127.30 N ANISOU 150 N GLU A 19 16352 16154 15864 454 -866 -882 N ATOM 151 CA GLU A 19 -11.824 255.252 828.251 1.00121.29 C ANISOU 151 CA GLU A 19 15321 15444 15320 377 -468 -974 C ATOM 152 C GLU A 19 -10.919 256.432 828.202 1.00108.47 C ANISOU 152 C GLU A 19 13453 13773 13986 604 -389 -1103 C ATOM 153 O GLU A 19 -10.062 256.619 829.039 1.00107.69 O ANISOU 153 O GLU A 19 13434 13572 13910 839 -608 -1114 O ATOM 154 CB GLU A 19 -13.213 255.744 827.942 1.00134.20 C ANISOU 154 CB GLU A 19 16691 17250 17048 251 -380 -1153 C ATOM 155 CG GLU A 19 -14.177 255.343 829.014 1.00149.73 C ANISOU 155 CG GLU A 19 18791 19313 18785 229 -701 -1180 C ATOM 156 CD GLU A 19 -15.607 255.587 828.627 1.00160.70 C ANISOU 156 CD GLU A 19 19988 20868 20203 85 -622 -1371 C ATOM 157 OE1 GLU A 19 -15.835 256.213 827.572 1.00163.22 O ANISOU 157 OE1 GLU A 19 20036 21190 20789 16 -343 -1490 O ATOM 158 OE2 GLU A 19 -16.505 255.152 829.383 1.00163.93 O ANISOU 158 OE2 GLU A 19 20538 21393 20355 41 -855 -1404 O ATOM 159 N PRO A 20 -11.137 257.242 827.195 1.00 95.42 N ANISOU 159 N PRO A 20 11497 12200 12559 531 -67 -1206 N ATOM 160 CA PRO A 20 -10.347 258.437 827.018 1.00 89.35 C ANISOU 160 CA PRO A 20 10452 11447 12051 703 91 -1323 C ATOM 161 C PRO A 20 -10.619 259.258 828.229 1.00 82.95 C ANISOU 161 C PRO A 20 9415 10703 11400 902 -183 -1510 C ATOM 162 O PRO A 20 -11.696 259.215 828.774 1.00 78.83 O ANISOU 162 O PRO A 20 8847 10244 10861 836 -392 -1580 O ATOM 163 CB PRO A 20 -10.963 259.081 825.788 1.00 91.45 C ANISOU 163 CB PRO A 20 10440 11794 12511 500 438 -1366 C ATOM 164 CG PRO A 20 -12.248 258.463 825.634 1.00 90.48 C ANISOU 164 CG PRO A 20 10375 11705 12299 296 371 -1369 C ATOM 165 CD PRO A 20 -12.157 257.105 826.158 1.00 86.84 C ANISOU 165 CD PRO A 20 10305 11190 11502 280 163 -1220 C ATOM 166 N ASN A 21 -9.626 259.992 828.666 1.00 83.26 N ANISOU 166 N ASN A 21 9314 10735 11588 1166 -199 -1611 N ATOM 167 CA ASN A 21 -9.773 260.826 829.854 1.00 93.89 C ANISOU 167 CA ASN A 21 10397 12142 13134 1403 -485 -1815 C ATOM 168 C ASN A 21 -10.876 261.876 829.712 1.00 93.49 C ANISOU 168 C ASN A 21 9887 12263 13371 1280 -403 -1991 C ATOM 169 O ASN A 21 -11.516 262.247 830.695 1.00 97.62 O ANISOU 169 O ASN A 21 10253 12833 14003 1378 -732 -2136 O ATOM 170 CB ASN A 21 -8.434 261.461 830.276 1.00106.00 C ANISOU 170 CB ASN A 21 11817 13657 14801 1744 -478 -1936 C ATOM 171 CG ASN A 21 -7.765 262.248 829.153 1.00115.43 C ANISOU 171 CG ASN A 21 12765 14971 16122 1706 18 -1970 C ATOM 172 OD1 ASN A 21 -6.591 262.609 829.254 1.00111.64 O ANISOU 172 OD1 ASN A 21 12255 14496 15666 1957 107 -2056 O ATOM 173 ND2 ASN A 21 -8.509 262.518 828.085 1.00121.48 N ANISOU 173 ND2 ASN A 21 13372 15827 16956 1397 331 -1905 N ATOM 174 N ASN A 22 -11.111 262.332 828.486 1.00 91.77 N ANISOU 174 N ASN A 22 9474 12115 13281 1054 0 -1968 N ATOM 175 CA ASN A 22 -12.081 263.393 828.241 1.00 91.79 C ANISOU 175 CA ASN A 22 9029 12241 13605 904 93 -2122 C ATOM 176 C ASN A 22 -13.291 262.912 827.457 1.00 87.30 C ANISOU 176 C ASN A 22 8556 11638 12974 594 153 -2069 C ATOM 177 O ASN A 22 -13.210 262.737 826.245 1.00 94.41 O ANISOU 177 O ASN A 22 9525 12492 13855 406 473 -1941 O ATOM 178 CB ASN A 22 -11.417 264.550 827.487 1.00 96.46 C ANISOU 178 CB ASN A 22 9248 12938 14463 884 504 -2153 C ATOM 179 CG ASN A 22 -12.212 265.847 827.576 1.00102.07 C ANISOU 179 CG ASN A 22 9414 13784 15584 778 537 -2335 C ATOM 180 OD1 ASN A 22 -13.054 266.015 828.460 1.00107.69 O ANISOU 180 OD1 ASN A 22 9986 14519 16413 820 186 -2496 O ATOM 181 ND2 ASN A 22 -11.938 266.773 826.663 1.00 97.41 N ANISOU 181 ND2 ASN A 22 8519 13281 15210 624 946 -2298 N ATOM 182 N THR A 23 -14.409 262.690 828.143 1.00 82.10 N ANISOU 182 N THR A 23 7917 11002 12276 558 -171 -2181 N ATOM 183 CA THR A 23 -15.664 262.393 827.454 1.00 84.69 C ANISOU 183 CA THR A 23 8274 11319 12587 298 -127 -2214 C ATOM 184 C THR A 23 -16.735 263.403 827.845 1.00 87.55 C ANISOU 184 C THR A 23 8249 11751 13265 243 -310 -2464 C ATOM 185 O THR A 23 -16.920 263.703 829.024 1.00 90.31 O ANISOU 185 O THR A 23 8500 12164 13650 411 -662 -2602 O ATOM 186 CB THR A 23 -16.194 260.964 827.735 1.00 84.30 C ANISOU 186 CB THR A 23 8670 11250 12108 254 -320 -2129 C ATOM 187 CG2 THR A 23 -15.053 259.971 827.937 1.00 83.50 C ANISOU 187 CG2 THR A 23 8948 11077 11702 366 -316 -1899 C ATOM 188 OG1 THR A 23 -17.035 260.983 828.894 1.00 95.29 O ANISOU 188 OG1 THR A 23 10066 12717 13422 330 -727 -2283 O ATOM 189 N VAL A 24 -17.438 263.924 826.850 1.00 79.40 N ANISOU 189 N VAL A 24 7005 10683 12482 7 -105 -2522 N ATOM 190 CA VAL A 24 -18.472 264.914 827.084 1.00 79.89 C ANISOU 190 CA VAL A 24 6686 10775 12894 -89 -276 -2762 C ATOM 191 C VAL A 24 -19.853 264.293 826.926 1.00 83.66 C ANISOU 191 C VAL A 24 7344 11214 13229 -226 -464 -2898 C ATOM 192 O VAL A 24 -20.094 263.542 825.984 1.00 74.58 O ANISOU 192 O VAL A 24 6432 9984 11920 -355 -271 -2810 O ATOM 193 CB VAL A 24 -18.337 266.090 826.104 1.00 79.96 C ANISOU 193 CB VAL A 24 6293 10744 13344 -285 59 -2742 C ATOM 194 CG2 VAL A 24 -16.998 266.789 826.297 1.00 73.26 C ANISOU 194 CG2 VAL A 24 5225 9996 12614 -139 275 -2648 C ATOM 195 CG1 VAL A 24 -19.489 267.059 826.282 1.00 83.10 C ANISOU 195 CG1 VAL A 24 6300 11135 14138 -435 -143 -2987 C ATOM 196 N ASP A 25 -20.756 264.608 827.850 1.00 88.04 N ANISOU 196 N ASP A 25 7779 11833 13838 -180 -853 -3136 N ATOM 197 CA ASP A 25 -22.135 264.128 827.778 1.00 81.94 C ANISOU 197 CA ASP A 25 7158 11053 12921 -288 -1056 -3329 C ATOM 198 C ASP A 25 -23.125 265.270 827.559 1.00 86.02 C ANISOU 198 C ASP A 25 7268 11506 13910 -446 -1181 -3595 C ATOM 199 O ASP A 25 -23.506 265.954 828.504 1.00 90.70 O ANISOU 199 O ASP A 25 7622 12167 14673 -372 -1526 -3788 O ATOM 200 CB ASP A 25 -22.514 263.359 829.051 1.00 82.75 C ANISOU 200 CB ASP A 25 7564 11287 12592 -118 -1465 -3395 C ATOM 201 CG ASP A 25 -22.178 261.877 828.971 1.00 86.40 C ANISOU 201 CG ASP A 25 8526 11788 12513 -90 -1353 -3175 C ATOM 202 OD1 ASP A 25 -21.088 261.536 828.475 1.00 88.44 O ANISOU 202 OD1 ASP A 25 8885 11989 12732 -74 -1060 -2926 O ATOM 203 OD2 ASP A 25 -23.003 261.050 829.416 1.00 83.07 O ANISOU 203 OD2 ASP A 25 8395 11470 11697 -93 -1561 -3253 O ATOM 204 N LEU A 26 -23.536 265.469 826.311 1.00 87.89 N ANISOU 204 N LEU A 26 7428 11588 14378 -666 -932 -3601 N ATOM 205 CA LEU A 26 -24.571 266.444 825.983 1.00 89.23 C ANISOU 205 CA LEU A 26 7262 11637 15004 -856 -1069 -3847 C ATOM 206 C LEU A 26 -25.922 265.748 826.003 1.00 93.44 C ANISOU 206 C LEU A 26 8045 12151 15306 -871 -1333 -4122 C ATOM 207 O LEU A 26 -26.071 264.666 825.437 1.00 95.16 O ANISOU 207 O LEU A 26 8613 12360 15181 -859 -1183 -4069 O ATOM 208 CB LEU A 26 -24.341 267.039 824.593 1.00 84.84 C ANISOU 208 CB LEU A 26 6524 10877 14832 -1098 -695 -3698 C ATOM 209 CG LEU A 26 -22.952 267.571 824.237 1.00 78.12 C ANISOU 209 CG LEU A 26 5507 10056 14118 -1112 -316 -3388 C ATOM 210 CD1 LEU A 26 -22.891 267.973 822.768 1.00 76.57 C ANISOU 210 CD1 LEU A 26 5241 9642 14209 -1374 21 -3218 C ATOM 211 CD2 LEU A 26 -22.559 268.732 825.132 1.00 73.08 C ANISOU 211 CD2 LEU A 26 4412 9557 13797 -1065 -417 -3453 C ATOM 212 N TYR A 27 -26.916 266.370 826.612 1.00 93.65 N ANISOU 212 N TYR A 27 7874 12180 15527 -895 -1723 -4437 N ATOM 213 CA TYR A 27 -28.242 265.789 826.673 1.00 95.39 C ANISOU 213 CA TYR A 27 8327 12404 15515 -891 -1996 -4752 C ATOM 214 C TYR A 27 -29.227 266.541 825.826 1.00 92.45 C ANISOU 214 C TYR A 27 7717 11780 15630 -1108 -2061 -5001 C ATOM 215 O TYR A 27 -28.997 267.672 825.459 1.00 81.86 O ANISOU 215 O TYR A 27 5980 10283 14838 -1282 -1990 -4945 O ATOM 216 CB TYR A 27 -28.747 265.726 828.089 1.00104.64 C ANISOU 216 CB TYR A 27 9565 13771 16423 -725 -2475 -4960 C ATOM 217 CG TYR A 27 -27.967 264.794 828.957 1.00103.74 C ANISOU 217 CG TYR A 27 9787 13869 15761 -514 -2484 -4727 C ATOM 218 CD1 TYR A 27 -28.458 263.559 829.283 1.00105.08 C ANISOU 218 CD1 TYR A 27 10416 14197 15313 -428 -2572 -4764 C ATOM 219 CE1 TYR A 27 -27.754 262.720 830.073 1.00108.43 C ANISOU 219 CE1 TYR A 27 11155 14782 15260 -277 -2600 -4517 C ATOM 220 CZ TYR A 27 -26.545 263.116 830.555 1.00112.22 C ANISOU 220 CZ TYR A 27 11501 15244 15894 -172 -2568 -4269 C ATOM 221 OH TYR A 27 -25.816 262.281 831.351 1.00114.14 O ANISOU 221 OH TYR A 27 12079 15593 15694 -21 -2636 -4018 O ATOM 222 CE2 TYR A 27 -26.042 264.334 830.247 1.00104.61 C ANISOU 222 CE2 TYR A 27 10070 14155 15523 -220 -2464 -4269 C ATOM 223 CD2 TYR A 27 -26.748 265.163 829.457 1.00 99.77 C ANISOU 223 CD2 TYR A 27 9137 13406 15367 -408 -2410 -4478 C ATOM 224 N VAL A 28 -30.354 265.943 825.491 1.00102.29 N ANISOU 224 N VAL A 28 9194 12977 16695 -1109 -2199 -5288 N ATOM 225 CA VAL A 28 -31.315 266.659 824.666 1.00109.04 C ANISOU 225 CA VAL A 28 9845 13535 18050 -1306 -2308 -5550 C ATOM 226 C VAL A 28 -32.745 266.626 825.162 1.00118.71 C ANISOU 226 C VAL A 28 11144 14772 19189 -1259 -2776 -6040 C ATOM 227 O VAL A 28 -33.502 265.745 824.808 1.00123.48 O ANISOU 227 O VAL A 28 12057 15396 19464 -1177 -2789 -6264 O ATOM 228 CB VAL A 28 -31.298 266.142 823.243 1.00102.95 C ANISOU 228 CB VAL A 28 9232 12549 17335 -1388 -1961 -5447 C ATOM 229 CG1 VAL A 28 -29.973 266.406 822.610 1.00117.89 C ANISOU 229 CG1 VAL A 28 10814 14170 19810 -1626 -1712 -5178 C ATOM 230 CG2 VAL A 28 -31.621 264.687 823.225 1.00 90.30 C ANISOU 230 CG2 VAL A 28 7992 11158 15161 -1222 -1662 -5207 C ATOM 231 N SER A 29 -33.113 267.603 825.979 1.00124.19 N ANISOU 231 N SER A 29 11538 15467 20182 -1303 -3167 -6228 N ATOM 232 CA SER A 29 -34.459 267.673 826.512 1.00131.54 C ANISOU 232 CA SER A 29 12529 16405 21044 -1259 -3671 -6716 C ATOM 233 C SER A 29 -34.384 267.922 828.002 1.00131.62 C ANISOU 233 C SER A 29 12474 16677 20861 -1114 -4066 -6775 C ATOM 234 O SER A 29 -33.355 268.366 828.495 1.00127.37 O ANISOU 234 O SER A 29 11710 16229 20458 -1092 -3969 -6480 O ATOM 235 CB SER A 29 -35.216 266.383 826.228 1.00127.75 C ANISOU 235 CB SER A 29 12527 16033 19979 -1109 -3638 -6941 C ATOM 236 OG SER A 29 -36.555 266.473 826.675 1.00133.98 O ANISOU 236 OG SER A 29 13394 16831 20683 -1059 -4121 -7454 O ATOM 237 N GLY A 53 -22.063 247.080 824.520 1.00 99.99 N ANISOU 237 N GLY A 53 12815 14756 10421 -1266 888 -1595 N ATOM 238 CA GLY A 53 -22.695 246.711 823.268 1.00109.06 C ANISOU 238 CA GLY A 53 13724 15994 11720 -1274 1174 -1840 C ATOM 239 C GLY A 53 -22.759 247.868 822.298 1.00112.93 C ANISOU 239 C GLY A 53 13958 16199 12750 -1129 1176 -2070 C ATOM 240 O GLY A 53 -22.313 248.953 822.601 1.00111.60 O ANISOU 240 O GLY A 53 13775 15804 12823 -1042 995 -2036 O ATOM 241 N SER A 54 -23.305 247.634 821.117 1.00114.19 N ANISOU 241 N SER A 54 13907 16368 13110 -1107 1380 -2298 N ATOM 242 CA SER A 54 -23.422 248.683 820.114 1.00106.44 C ANISOU 242 CA SER A 54 12707 15090 12648 -997 1373 -2489 C ATOM 243 C SER A 54 -24.389 248.236 819.018 1.00101.65 C ANISOU 243 C SER A 54 11904 14554 12165 -952 1546 -2817 C ATOM 244 O SER A 54 -24.834 247.102 819.036 1.00 97.07 O ANISOU 244 O SER A 54 11334 14280 11269 -1001 1706 -2883 O ATOM 245 CB SER A 54 -22.063 249.105 819.589 1.00100.24 C ANISOU 245 CB SER A 54 11914 13996 12175 -1000 1389 -2190 C ATOM 246 OG SER A 54 -21.962 250.515 819.577 1.00 89.41 O ANISOU 246 OG SER A 54 10449 12379 11141 -924 1254 -2252 O ATOM 247 N GLU A 55 -24.732 249.109 818.079 1.00 93.07 N ANISOU 247 N GLU A 55 10635 13192 11537 -861 1513 -3027 N ATOM 248 CA GLU A 55 -25.660 248.727 817.029 1.00 85.90 C ANISOU 248 CA GLU A 55 9545 12299 10793 -781 1628 -3369 C ATOM 249 C GLU A 55 -25.208 249.078 815.636 1.00 80.68 C ANISOU 249 C GLU A 55 8738 11277 10638 -738 1672 -3318 C ATOM 250 O GLU A 55 -25.566 248.416 814.686 1.00 78.06 O ANISOU 250 O GLU A 55 8273 10958 10428 -675 1790 -3481 O ATOM 251 CB GLU A 55 -27.006 249.326 817.339 1.00 91.02 C ANISOU 251 CB GLU A 55 10145 12998 11442 -693 1481 -3802 C ATOM 252 CG GLU A 55 -27.579 248.694 818.569 1.00100.54 C ANISOU 252 CG GLU A 55 11539 14481 12183 -739 1351 -3776 C ATOM 253 CD GLU A 55 -28.873 249.295 818.963 1.00116.35 C ANISOU 253 CD GLU A 55 13515 16579 14114 -650 1186 -4228 C ATOM 254 OE1 GLU A 55 -29.217 250.332 818.373 1.00116.08 O ANISOU 254 OE1 GLU A 55 13316 16420 14369 -549 1204 -4588 O ATOM 255 OE2 GLU A 55 -29.542 248.739 819.859 1.00128.52 O ANISOU 255 OE2 GLU A 55 15211 18299 15321 -670 1006 -4234 O ATOM 256 N TYR A 56 -24.416 250.123 815.512 1.00 80.38 N ANISOU 256 N TYR A 56 8725 10929 10888 -767 1572 -3093 N ATOM 257 CA TYR A 56 -23.896 250.536 814.215 1.00 75.67 C ANISOU 257 CA TYR A 56 8040 9981 10732 -749 1597 -2983 C ATOM 258 C TYR A 56 -22.684 251.433 814.383 1.00 67.35 C ANISOU 258 C TYR A 56 7072 8719 9800 -816 1555 -2627 C ATOM 259 O TYR A 56 -22.632 252.253 815.291 1.00 62.62 O ANISOU 259 O TYR A 56 6505 8134 9155 -840 1451 -2602 O ATOM 260 CB TYR A 56 -24.963 251.255 813.393 1.00 85.19 C ANISOU 260 CB TYR A 56 9090 10938 12339 -671 1497 -3324 C ATOM 261 CG TYR A 56 -24.455 251.713 812.048 1.00 89.10 C ANISOU 261 CG TYR A 56 9532 11042 13282 -667 1489 -3174 C ATOM 262 CD1 TYR A 56 -24.166 253.050 811.811 1.00 90.76 C ANISOU 262 CD1 TYR A 56 9734 10932 13820 -739 1390 -3037 C ATOM 263 CE1 TYR A 56 -23.692 253.472 810.584 1.00 95.11 C ANISOU 263 CE1 TYR A 56 10275 11129 14733 -759 1381 -2857 C ATOM 264 CZ TYR A 56 -23.492 252.551 809.576 1.00 90.04 C ANISOU 264 CZ TYR A 56 9626 10431 14154 -679 1431 -2830 C ATOM 265 OH TYR A 56 -23.019 252.973 808.356 1.00 80.02 O ANISOU 265 OH TYR A 56 8380 8797 13226 -693 1379 -2633 O ATOM 266 CE2 TYR A 56 -23.767 251.215 809.788 1.00 89.51 C ANISOU 266 CE2 TYR A 56 9520 10682 13807 -595 1528 -2991 C ATOM 267 CD2 TYR A 56 -24.241 250.803 811.019 1.00 89.46 C ANISOU 267 CD2 TYR A 56 9528 11048 13413 -604 1577 -3150 C ATOM 268 N SER A 57 -21.707 251.262 813.503 1.00 62.55 N ANISOU 268 N SER A 57 6493 7935 9339 -832 1629 -2369 N ATOM 269 CA SER A 57 -20.474 252.030 813.564 1.00 60.04 C ANISOU 269 CA SER A 57 6269 7451 9094 -879 1623 -2042 C ATOM 270 C SER A 57 -19.990 252.313 812.162 1.00 61.35 C ANISOU 270 C SER A 57 6411 7314 9584 -879 1653 -1904 C ATOM 271 O SER A 57 -19.891 251.406 811.340 1.00 70.67 O ANISOU 271 O SER A 57 7584 8476 10791 -847 1694 -1891 O ATOM 272 CB SER A 57 -19.380 251.251 814.300 1.00 63.85 C ANISOU 272 CB SER A 57 6926 8109 9226 -910 1662 -1775 C ATOM 273 OG SER A 57 -19.783 250.888 815.604 1.00 70.98 O ANISOU 273 OG SER A 57 7893 9279 9796 -921 1610 -1853 O ATOM 274 N ASN A 58 -19.683 253.571 811.891 1.00 58.68 N ANISOU 274 N ASN A 58 6057 6749 9491 -923 1629 -1792 N ATOM 275 CA ASN A 58 -19.003 253.918 810.658 1.00 63.28 C ANISOU 275 CA ASN A 58 6683 7053 10308 -948 1655 -1572 C ATOM 276 C ASN A 58 -17.945 254.997 810.897 1.00 70.12 C ANISOU 276 C ASN A 58 7668 7844 11130 -955 1693 -1310 C ATOM 277 O ASN A 58 -17.749 255.460 812.022 1.00 54.82 O ANISOU 277 O ASN A 58 5732 6056 9043 -958 1692 -1318 O ATOM 278 CB ASN A 58 -20.006 254.336 809.585 1.00 61.32 C ANISOU 278 CB ASN A 58 6315 6525 10457 -946 1571 -1750 C ATOM 279 CG ASN A 58 -19.542 253.981 808.191 1.00 66.19 C ANISOU 279 CG ASN A 58 6997 6901 11250 -919 1551 -1586 C ATOM 280 OD1 ASN A 58 -18.370 254.146 807.849 1.00 63.60 O ANISOU 280 OD1 ASN A 58 6815 6513 10839 -944 1599 -1267 O ATOM 281 ND2 ASN A 58 -20.462 253.484 807.373 1.00 73.66 N ANISOU 281 ND2 ASN A 58 7846 7716 12427 -832 1460 -1824 N ATOM 282 N CYS A 59 -17.259 255.393 809.834 1.00 73.75 N ANISOU 282 N CYS A 59 8220 8096 11706 -942 1719 -1087 N ATOM 283 CA CYS A 59 -16.151 256.316 809.965 1.00 58.47 C ANISOU 283 CA CYS A 59 6399 6146 9672 -932 1788 -847 C ATOM 284 C CYS A 59 -16.201 257.372 808.865 1.00 72.04 C ANISOU 284 C CYS A 59 8072 7616 11684 -1024 1819 -698 C ATOM 285 O CYS A 59 -15.997 257.063 807.692 1.00 81.46 O ANISOU 285 O CYS A 59 9347 8642 12964 -1016 1784 -565 O ATOM 286 CB CYS A 59 -14.854 255.537 809.882 1.00 47.88 C ANISOU 286 CB CYS A 59 5289 4877 8027 -828 1790 -660 C ATOM 287 SG CYS A 59 -13.795 255.803 811.265 1.00 70.26 S ANISOU 287 SG CYS A 59 8246 7894 10557 -775 1804 -597 S ATOM 288 N LEU A 60 -16.464 258.617 809.253 1.00 66.53 N ANISOU 288 N LEU A 60 7238 6891 11147 -1132 1869 -705 N ATOM 289 CA LEU A 60 -16.689 259.704 808.304 1.00 64.48 C ANISOU 289 CA LEU A 60 6915 6382 11203 -1285 1893 -559 C ATOM 290 C LEU A 60 -15.434 260.543 808.083 1.00 74.16 C ANISOU 290 C LEU A 60 8251 7644 12283 -1330 2053 -250 C ATOM 291 O LEU A 60 -14.778 260.952 809.042 1.00 79.88 O ANISOU 291 O LEU A 60 8951 8580 12820 -1299 2159 -245 O ATOM 292 CB LEU A 60 -17.832 260.593 808.801 1.00 64.76 C ANISOU 292 CB LEU A 60 6694 6351 11559 -1427 1843 -761 C ATOM 293 CG LEU A 60 -18.542 261.514 807.810 1.00 75.79 C ANISOU 293 CG LEU A 60 7999 7406 13392 -1620 1780 -693 C ATOM 294 CD1 LEU A 60 -17.722 262.755 807.524 1.00 74.64 C ANISOU 294 CD1 LEU A 60 7854 7232 13273 -1781 1951 -366 C ATOM 295 CD2 LEU A 60 -18.857 260.769 806.517 1.00 88.47 C ANISOU 295 CD2 LEU A 60 9738 8738 15140 -1573 1644 -665 C ATOM 296 N LEU A 61 -15.104 260.804 806.821 1.00 77.44 N ANISOU 296 N LEU A 61 8787 7853 12784 -1409 2061 0 N ATOM 297 CA LEU A 61 -13.972 261.674 806.501 1.00 82.49 C ANISOU 297 CA LEU A 61 9536 8535 13272 -1494 2236 303 C ATOM 298 C LEU A 61 -14.406 263.145 806.408 1.00 82.75 C ANISOU 298 C LEU A 61 9379 8467 13597 -1748 2349 410 C ATOM 299 O LEU A 61 -15.419 263.461 805.784 1.00 92.44 O ANISOU 299 O LEU A 61 10514 9415 15192 -1894 2230 397 O ATOM 300 CB LEU A 61 -13.299 261.229 805.200 1.00 82.61 C ANISOU 300 CB LEU A 61 9812 8399 13178 -1478 2181 558 C ATOM 301 CG LEU A 61 -12.062 262.055 804.832 1.00 81.81 C ANISOU 301 CG LEU A 61 9870 8369 12844 -1572 2375 876 C ATOM 302 CD1 LEU A 61 -10.974 261.857 805.871 1.00 79.57 C ANISOU 302 CD1 LEU A 61 9641 8402 12191 -1419 2503 804 C ATOM 303 CD2 LEU A 61 -11.548 261.728 803.438 1.00 76.94 C ANISOU 303 CD2 LEU A 61 9527 7555 12151 -1595 2275 1149 C ATOM 304 N LEU A 62 -13.634 264.005 807.055 1.00 77.45 N ANISOU 304 N LEU A 62 8632 8017 12779 -1802 2568 500 N ATOM 305 CA LEU A 62 -13.932 265.412 807.205 1.00 88.25 C ANISOU 305 CA LEU A 62 9749 9379 14401 -2053 2720 586 C ATOM 306 C LEU A 62 -13.119 266.357 806.330 1.00 95.09 C ANISOU 306 C LEU A 62 10709 10222 15197 -2264 2946 976 C ATOM 307 O LEU A 62 -12.156 265.971 805.681 1.00 95.18 O ANISOU 307 O LEU A 62 11008 10257 14899 -2191 2996 1179 O ATOM 308 CB LEU A 62 -13.780 265.814 808.656 1.00 81.97 C ANISOU 308 CB LEU A 62 8708 8887 13548 -1986 2821 377 C ATOM 309 CG LEU A 62 -14.569 264.979 809.632 1.00 75.59 C ANISOU 309 CG LEU A 62 7819 8133 12770 -1814 2607 21 C ATOM 310 CD2 LEU A 62 -16.016 265.019 809.317 1.00 76.64 C ANISOU 310 CD2 LEU A 62 7811 8015 13296 -1940 2415 -134 C ATOM 311 CD1 LEU A 62 -14.329 265.504 810.981 1.00 76.38 C ANISOU 311 CD1 LEU A 62 7685 8509 12827 -1765 2684 -133 C ATOM 312 N SER A 63 -13.521 267.625 806.362 1.00100.58 N ANISOU 312 N SER A 63 11148 10889 16179 -2547 3084 1079 N ATOM 313 CA SER A 63 -12.971 268.659 805.507 1.00106.50 C ANISOU 313 CA SER A 63 11948 11603 16915 -2832 3317 1481 C ATOM 314 C SER A 63 -11.510 268.813 805.736 1.00113.44 C ANISOU 314 C SER A 63 12943 12835 17323 -2734 3609 1616 C ATOM 315 O SER A 63 -10.736 268.911 804.804 1.00116.93 O ANISOU 315 O SER A 63 13659 13250 17517 -2812 3720 1936 O ATOM 316 CB SER A 63 -13.583 269.982 805.886 1.00109.90 C ANISOU 316 CB SER A 63 11987 12049 17722 -3144 3454 1505 C ATOM 317 OG SER A 63 -12.534 270.908 806.085 1.00120.05 O ANISOU 317 OG SER A 63 13172 13668 18775 -3263 3843 1716 O ATOM 318 N ASN A 64 -11.125 268.829 806.993 1.00114.13 N ANISOU 318 N ASN A 64 12834 13248 17281 -2552 3715 1361 N ATOM 319 CA ASN A 64 -9.730 268.775 807.333 1.00111.38 C ANISOU 319 CA ASN A 64 12612 13227 16481 -2379 3940 1400 C ATOM 320 C ASN A 64 -9.462 267.300 807.152 1.00109.35 C ANISOU 320 C ASN A 64 12708 12855 15986 -2094 3671 1295 C ATOM 321 O ASN A 64 -10.404 266.533 807.058 1.00117.90 O ANISOU 321 O ASN A 64 13812 13707 17278 -2037 3384 1145 O ATOM 322 CB ASN A 64 -9.561 269.142 808.770 1.00101.46 C ANISOU 322 CB ASN A 64 11023 12288 15238 -2244 4051 1118 C ATOM 323 CG ASN A 64 -10.081 268.103 809.640 1.00 93.80 C ANISOU 323 CG ASN A 64 10061 11267 14313 -1989 3742 783 C ATOM 324 ND2 ASN A 64 -10.796 268.486 810.663 1.00 80.97 N ANISOU 324 ND2 ASN A 64 8086 9725 12954 -1993 3683 540 N ATOM 325 OD1 ASN A 64 -9.865 266.939 809.384 1.00100.24 O ANISOU 325 OD1 ASN A 64 11191 11970 14923 -1802 3547 750 O ATOM 326 N SER A 65 -8.215 266.869 807.077 1.00103.17 N ANISOU 326 N SER A 65 12188 12234 14779 -1922 3756 1360 N ATOM 327 CA SER A 65 -7.982 265.447 806.852 1.00108.30 C ANISOU 327 CA SER A 65 13146 12757 15248 -1692 3481 1274 C ATOM 328 C SER A 65 -8.014 264.625 808.126 1.00 98.66 C ANISOU 328 C SER A 65 11850 11653 13983 -1436 3328 938 C ATOM 329 O SER A 65 -6.987 264.265 808.665 1.00106.63 O ANISOU 329 O SER A 65 12985 12840 14691 -1250 3369 875 O ATOM 330 CB SER A 65 -6.660 265.239 806.135 1.00107.50 C ANISOU 330 CB SER A 65 13395 12727 14723 -1634 3577 1494 C ATOM 331 OG SER A 65 -6.766 265.674 804.805 1.00106.75 O ANISOU 331 OG SER A 65 13460 12441 14657 -1863 3608 1831 O ATOM 332 N GLU A 66 -9.210 264.314 808.588 1.00 73.98 N ANISOU 332 N GLU A 66 8543 8415 11151 -1436 3138 732 N ATOM 333 CA GLU A 66 -9.391 263.602 809.849 1.00 74.94 C ANISOU 333 CA GLU A 66 8593 8644 11238 -1240 2985 443 C ATOM 334 C GLU A 66 -10.580 262.653 809.825 1.00 72.71 C ANISOU 334 C GLU A 66 8307 8185 11137 -1210 2719 275 C ATOM 335 O GLU A 66 -11.633 262.967 809.272 1.00 83.01 O ANISOU 335 O GLU A 66 9485 9315 12739 -1358 2672 275 O ATOM 336 CB GLU A 66 -9.554 264.587 811.001 1.00 89.31 C ANISOU 336 CB GLU A 66 10073 10672 13190 -1266 3117 299 C ATOM 337 CG GLU A 66 -9.078 264.057 812.343 1.00101.46 C ANISOU 337 CG GLU A 66 11602 12395 14554 -1034 3026 86 C ATOM 338 CD GLU A 66 -7.645 264.451 812.647 1.00105.88 C ANISOU 338 CD GLU A 66 12215 13183 14833 -906 3235 141 C ATOM 339 OE1 GLU A 66 -6.935 264.878 811.712 1.00108.57 O ANISOU 339 OE1 GLU A 66 12684 13540 15026 -983 3438 357 O ATOM 340 OE2 GLU A 66 -7.232 264.340 813.822 1.00104.25 O ANISOU 340 OE2 GLU A 66 11924 13145 14542 -718 3193 -38 O ATOM 341 N TYR A 67 -10.408 261.489 810.438 1.00 65.33 N ANISOU 341 N TYR A 67 7502 7299 10021 -1029 2552 130 N ATOM 342 CA TYR A 67 -11.486 260.517 810.507 1.00 69.49 C ANISOU 342 CA TYR A 67 8014 7730 10659 -995 2345 -43 C ATOM 343 C TYR A 67 -12.201 260.575 811.851 1.00 65.79 C ANISOU 343 C TYR A 67 7348 7390 10260 -972 2273 -283 C ATOM 344 O TYR A 67 -11.592 260.394 812.910 1.00 57.04 O ANISOU 344 O TYR A 67 6263 6445 8965 -866 2253 -341 O ATOM 345 CB TYR A 67 -10.980 259.098 810.196 1.00 74.16 C ANISOU 345 CB TYR A 67 8858 8298 11023 -861 2206 -24 C ATOM 346 CG TYR A 67 -10.786 258.850 808.711 1.00 79.96 C ANISOU 346 CG TYR A 67 9729 8866 11785 -897 2192 159 C ATOM 347 CD1 TYR A 67 -11.855 258.484 807.905 1.00 79.25 C ANISOU 347 CD1 TYR A 67 9562 8610 11939 -949 2092 114 C ATOM 348 CE1 TYR A 67 -11.692 258.275 806.549 1.00 78.73 C ANISOU 348 CE1 TYR A 67 9613 8368 11932 -983 2037 291 C ATOM 349 CZ TYR A 67 -10.446 258.429 805.979 1.00 77.32 C ANISOU 349 CZ TYR A 67 9654 8197 11528 -977 2087 524 C ATOM 350 OH TYR A 67 -10.289 258.217 804.627 1.00 79.53 O ANISOU 350 OH TYR A 67 10074 8286 11856 -1019 1990 715 O ATOM 351 CE2 TYR A 67 -9.366 258.793 806.755 1.00 69.10 C ANISOU 351 CE2 TYR A 67 8700 7338 10215 -928 2214 556 C ATOM 352 CD2 TYR A 67 -9.541 259.006 808.113 1.00 76.49 C ANISOU 352 CD2 TYR A 67 9494 8433 11134 -883 2265 371 C ATOM 353 N ILE A 68 -13.507 260.756 811.794 1.00 62.50 N ANISOU 353 N ILE A 68 6744 6890 10112 -1070 2206 -427 N ATOM 354 CA ILE A 68 -14.333 260.810 812.973 1.00 58.01 C ANISOU 354 CA ILE A 68 5978 6443 9619 -1068 2110 -667 C ATOM 355 C ILE A 68 -15.237 259.611 812.946 1.00 54.45 C ANISOU 355 C ILE A 68 5589 5965 9135 -1030 1953 -832 C ATOM 356 O ILE A 68 -15.742 259.276 811.917 1.00 52.91 O ANISOU 356 O ILE A 68 5425 5605 9073 -1069 1933 -822 O ATOM 357 CB ILE A 68 -15.195 262.050 812.954 1.00 63.24 C ANISOU 357 CB ILE A 68 6334 7049 10646 -1240 2149 -738 C ATOM 358 CG1 ILE A 68 -15.309 262.653 814.344 1.00 70.70 C ANISOU 358 CG1 ILE A 68 7029 8206 11628 -1221 2121 -901 C ATOM 359 CD1 ILE A 68 -16.321 262.034 815.178 1.00 70.84 C ANISOU 359 CD1 ILE A 68 6963 8305 11649 -1185 1918 -1161 C ATOM 360 CG2 ILE A 68 -16.539 261.724 812.427 1.00 54.32 C ANISOU 360 CG2 ILE A 68 5132 5746 9760 -1323 2014 -896 C ATOM 361 N CYS A 69 -15.430 258.962 814.081 1.00 48.95 N ANISOU 361 N CYS A 69 4892 5447 8259 -960 1850 -978 N ATOM 362 CA CYS A 69 -16.221 257.758 814.155 1.00 54.82 C ANISOU 362 CA CYS A 69 5684 6237 8907 -943 1743 -1127 C ATOM 363 C CYS A 69 -17.498 257.931 814.899 1.00 67.18 C ANISOU 363 C CYS A 69 7012 7915 10599 -1006 1648 -1394 C ATOM 364 O CYS A 69 -17.553 258.656 815.865 1.00 71.36 O ANISOU 364 O CYS A 69 7378 8566 11169 -1013 1607 -1463 O ATOM 365 CB CYS A 69 -15.458 256.695 814.898 1.00 45.20 C ANISOU 365 CB CYS A 69 4671 5169 7333 -848 1688 -1057 C ATOM 366 SG CYS A 69 -13.887 256.377 814.250 1.00 94.09 S ANISOU 366 SG CYS A 69 11134 11261 13355 -768 1737 -790 S ATOM 367 N TYR A 70 -18.535 257.234 814.466 1.00 69.52 N ANISOU 367 N TYR A 70 7267 8189 10957 -1039 1593 -1573 N ATOM 368 CA TYR A 70 -19.777 257.267 815.201 1.00 74.84 C ANISOU 368 CA TYR A 70 7830 8965 11641 -1027 1442 -1880 C ATOM 369 C TYR A 70 -20.295 255.908 815.574 1.00 68.04 C ANISOU 369 C TYR A 70 7089 8299 10463 -957 1394 -2022 C ATOM 370 O TYR A 70 -20.008 254.941 814.923 1.00 69.19 O ANISOU 370 O TYR A 70 7339 8442 10508 -940 1478 -1937 O ATOM 371 CB TYR A 70 -20.856 258.077 814.492 1.00 82.98 C ANISOU 371 CB TYR A 70 8680 9774 13075 -1115 1375 -2072 C ATOM 372 CG TYR A 70 -21.043 257.866 813.015 1.00 86.02 C ANISOU 372 CG TYR A 70 9092 9894 13697 -1153 1423 -2031 C ATOM 373 CD2 TYR A 70 -20.157 258.388 812.116 1.00 92.12 C ANISOU 373 CD2 TYR A 70 9904 10470 14625 -1230 1540 -1732 C ATOM 374 CE2 TYR A 70 -20.337 258.229 810.771 1.00 94.86 C ANISOU 374 CE2 TYR A 70 10296 10545 15200 -1258 1534 -1677 C ATOM 375 CZ TYR A 70 -21.424 257.555 810.301 1.00 93.23 C ANISOU 375 CZ TYR A 70 10061 10255 15107 -1186 1416 -1959 C ATOM 376 OH TYR A 70 -21.581 257.403 808.950 1.00 90.13 O ANISOU 376 OH TYR A 70 9707 9560 14976 -1184 1372 -1912 O ATOM 377 CE1 TYR A 70 -22.336 257.041 811.171 1.00 88.73 C ANISOU 377 CE1 TYR A 70 9431 9905 14377 -1103 1334 -2291 C ATOM 378 CD1 TYR A 70 -22.151 257.206 812.519 1.00 86.38 C ANISOU 378 CD1 TYR A 70 9120 9881 13820 -1100 1333 -2311 C ATOM 379 N HIS A 71 -21.045 255.872 816.663 1.00 67.64 N ANISOU 379 N HIS A 71 7015 8436 10249 -924 1254 -2231 N ATOM 380 CA HIS A 71 -21.706 254.677 817.162 1.00 66.44 C ANISOU 380 CA HIS A 71 6972 8524 9749 -881 1215 -2386 C ATOM 381 C HIS A 71 -23.123 255.057 817.578 1.00 77.84 C ANISOU 381 C HIS A 71 8306 10028 11243 -867 1051 -2756 C ATOM 382 O HIS A 71 -23.364 256.174 818.027 1.00 90.15 O ANISOU 382 O HIS A 71 9736 11511 13005 -885 915 -2841 O ATOM 383 CB HIS A 71 -20.955 254.112 818.366 1.00 69.55 C ANISOU 383 CB HIS A 71 7548 9130 9747 -853 1171 -2199 C ATOM 384 CG HIS A 71 -19.656 253.454 818.022 1.00 77.00 C ANISOU 384 CG HIS A 71 8640 10035 10581 -862 1298 -1882 C ATOM 385 ND1 HIS A 71 -19.422 252.113 818.248 1.00 81.24 N ANISOU 385 ND1 HIS A 71 9343 10738 10785 -887 1340 -1776 N ATOM 386 CE1 HIS A 71 -18.197 251.811 817.848 1.00 75.81 C ANISOU 386 CE1 HIS A 71 8759 9945 10100 -898 1414 -1508 C ATOM 387 NE2 HIS A 71 -17.632 252.904 817.372 1.00 78.03 N ANISOU 387 NE2 HIS A 71 8962 10023 10661 -867 1441 -1440 N ATOM 388 CD2 HIS A 71 -18.523 253.946 817.470 1.00 77.97 C ANISOU 388 CD2 HIS A 71 8773 9978 10873 -860 1383 -1655 C ATOM 389 N PHE A 72 -24.060 254.130 817.427 1.00 85.04 N ANISOU 389 N PHE A 72 9252 11090 11968 -831 1064 -2996 N ATOM 390 CA PHE A 72 -25.443 254.360 817.821 1.00 88.24 C ANISOU 390 CA PHE A 72 9591 11581 12356 -795 898 -3393 C ATOM 391 C PHE A 72 -25.822 253.245 818.788 1.00 93.63 C ANISOU 391 C PHE A 72 10446 12649 12479 -762 891 -3464 C ATOM 392 O PHE A 72 -25.600 252.073 818.491 1.00 95.88 O ANISOU 392 O PHE A 72 10816 13094 12521 -768 1072 -3373 O ATOM 393 CB PHE A 72 -26.334 254.309 816.582 1.00 97.59 C ANISOU 393 CB PHE A 72 10653 12580 13848 -762 930 -3676 C ATOM 394 CG PHE A 72 -27.528 255.212 816.650 1.00107.77 C ANISOU 394 CG PHE A 72 11816 13737 15396 -751 708 -4053 C ATOM 395 CD1 PHE A 72 -28.321 255.247 817.782 1.00116.91 C ANISOU 395 CD1 PHE A 72 13019 15134 16269 -715 524 -4304 C ATOM 396 CE1 PHE A 72 -29.422 256.081 817.843 1.00123.38 C ANISOU 396 CE1 PHE A 72 13723 15816 17339 -707 282 -4674 C ATOM 397 CZ PHE A 72 -29.750 256.878 816.766 1.00122.16 C ANISOU 397 CZ PHE A 72 13407 15262 17746 -753 227 -4782 C ATOM 398 CE2 PHE A 72 -28.973 256.847 815.629 1.00118.09 C ANISOU 398 CE2 PHE A 72 12862 14500 17507 -797 415 -4504 C ATOM 399 CD2 PHE A 72 -27.868 256.015 815.573 1.00113.22 C ANISOU 399 CD2 PHE A 72 12360 14043 16615 -786 652 -4151 C ATOM 400 N SER A 73 -26.364 253.549 819.941 1.00 94.37 N ANISOU 400 N SER A 73 10596 12907 12353 -743 684 -3602 N ATOM 401 CA SER A 73 -26.674 252.439 820.801 1.00 97.96 C ANISOU 401 CA SER A 73 11254 13731 12234 -738 693 -3613 C ATOM 402 C SER A 73 -28.080 252.378 821.367 1.00110.65 C ANISOU 402 C SER A 73 12896 15560 13585 -684 529 -4021 C ATOM 403 O SER A 73 -28.565 253.332 821.937 1.00114.13 O ANISOU 403 O SER A 73 13285 15929 14149 -655 263 -4197 O ATOM 404 CB SER A 73 -25.672 252.376 821.931 1.00 85.28 C ANISOU 404 CB SER A 73 9826 12207 10371 -769 600 -3256 C ATOM 405 OG SER A 73 -26.234 252.927 823.083 1.00 82.39 O ANISOU 405 OG SER A 73 9513 11943 9848 -728 309 -3396 O ATOM 406 N SER A 74 -28.751 251.266 821.075 1.00120.35 N ANISOU 406 N SER A 74 14181 17054 14493 -665 702 -4203 N ATOM 407 CA SER A 74 -30.113 250.966 821.523 1.00117.16 C ANISOU 407 CA SER A 74 13841 16936 13739 -599 607 -4623 C ATOM 408 C SER A 74 -31.410 251.729 821.248 1.00110.01 C ANISOU 408 C SER A 74 12811 15919 13068 -494 403 -5152 C ATOM 409 O SER A 74 -32.099 251.960 822.216 1.00105.57 O ANISOU 409 O SER A 74 12367 15535 12212 -467 163 -5342 O ATOM 410 CB SER A 74 -30.053 250.935 823.036 1.00124.41 C ANISOU 410 CB SER A 74 14999 18092 14179 -637 392 -4472 C ATOM 411 OG SER A 74 -29.536 252.164 823.510 1.00121.56 O ANISOU 411 OG SER A 74 14574 17453 14158 -633 124 -4344 O ATOM 412 N ARG A 75 -31.880 252.080 820.057 1.00120.47 N ANISOU 412 N ARG A 75 13936 16971 14868 -428 441 -5428 N ATOM 413 CA ARG A 75 -31.260 252.136 818.767 1.00123.75 C ANISOU 413 CA ARG A 75 14188 17069 15762 -438 621 -5280 C ATOM 414 CB ARG A 75 -32.149 251.593 817.645 1.00133.81 C ANISOU 414 CB ARG A 75 15341 18318 17181 -307 741 -5687 C ATOM 415 C ARG A 75 -31.007 253.577 818.648 1.00113.07 C ANISOU 415 C ARG A 75 12712 15308 14942 -494 401 -5211 C ATOM 416 O ARG A 75 -30.710 254.088 817.591 1.00110.64 O ANISOU 416 O ARG A 75 12262 14640 15138 -517 444 -5145 O ATOM 417 N SER A 76 -31.243 254.262 819.733 1.00110.47 N ANISOU 417 N SER A 76 12427 15042 14504 -519 144 -5261 N ATOM 418 CA SER A 76 -31.163 255.673 819.720 1.00111.10 C ANISOU 418 CA SER A 76 12340 14783 15089 -585 -78 -5253 C ATOM 419 CB SER A 76 -32.492 256.258 819.385 1.00129.48 C ANISOU 419 CB SER A 76 14562 16941 17693 -538 -315 -5759 C ATOM 420 OG SER A 76 -33.262 256.266 820.569 1.00141.84 O ANISOU 420 OG SER A 76 16239 18782 18872 -487 -572 -6018 O ATOM 421 C SER A 76 -30.988 255.921 821.138 1.00107.29 C ANISOU 421 C SER A 76 11956 14517 14291 -597 -278 -5153 C ATOM 422 O SER A 76 -30.841 255.005 821.908 1.00111.63 O ANISOU 422 O SER A 76 12719 15406 14291 -567 -225 -5043 O ATOM 423 N THR A 77 -30.983 257.180 821.480 1.00110.92 N ANISOU 423 N THR A 77 12251 14770 15124 -650 -521 -5175 N ATOM 424 CA THR A 77 -30.868 257.545 822.843 1.00118.94 C ANISOU 424 CA THR A 77 13321 15959 15912 -635 -778 -5119 C ATOM 425 CB THR A 77 -31.525 256.509 823.747 1.00118.99 C ANISOU 425 CB THR A 77 13614 16368 15229 -548 -866 -5273 C ATOM 426 OG1 THR A 77 -30.573 255.519 824.129 1.00121.07 O ANISOU 426 OG1 THR A 77 14089 16847 15067 -557 -654 -4876 O ATOM 427 CG2 THR A 77 -32.655 255.851 823.031 1.00115.93 C ANISOU 427 CG2 THR A 77 13273 16063 14711 -488 -778 -5679 C ATOM 428 C THR A 77 -29.407 257.511 823.037 1.00121.65 C ANISOU 428 C THR A 77 13681 16289 16251 -669 -603 -4632 C ATOM 429 O THR A 77 -28.914 257.781 824.112 1.00131.83 O ANISOU 429 O THR A 77 15010 17682 17396 -642 -771 -4473 O ATOM 430 N LEU A 78 -28.682 257.089 822.017 1.00109.07 N ANISOU 430 N LEU A 78 12082 14575 14783 -707 -281 -4400 N ATOM 431 CA LEU A 78 -27.242 257.204 822.099 1.00 96.93 C ANISOU 431 CA LEU A 78 10548 12980 13302 -735 -129 -3965 C ATOM 432 CB LEU A 78 -26.653 256.076 822.902 1.00 96.57 C ANISOU 432 CB LEU A 78 10782 13210 12701 -691 -76 -3727 C ATOM 433 CG LEU A 78 -25.479 256.685 823.639 1.00 90.33 C ANISOU 433 CG LEU A 78 9965 12362 11992 -668 -152 -3427 C ATOM 434 CD1 LEU A 78 -25.114 257.930 822.901 1.00 94.12 C ANISOU 434 CD1 LEU A 78 10149 12563 13051 -721 -84 -3406 C ATOM 435 CD2 LEU A 78 -25.901 257.044 825.012 1.00 90.71 C ANISOU 435 CD2 LEU A 78 10056 12556 11854 -598 -506 -3545 C ATOM 436 C LEU A 78 -26.504 257.337 820.789 1.00 94.17 C ANISOU 436 C LEU A 78 10099 12376 13306 -801 148 -3756 C ATOM 437 O LEU A 78 -26.650 256.524 819.898 1.00108.62 O ANISOU 437 O LEU A 78 11998 14192 15081 -797 333 -3778 O ATOM 438 N LEU A 79 -25.668 258.356 820.711 1.00 81.93 N ANISOU 438 N LEU A 79 8384 10647 12097 -855 174 -3547 N ATOM 439 CA LEU A 79 -24.775 258.579 819.600 1.00 75.81 C ANISOU 439 CA LEU A 79 7550 9654 11601 -923 426 -3285 C ATOM 440 CB LEU A 79 -25.248 259.750 818.791 1.00 73.27 C ANISOU 440 CB LEU A 79 6980 9037 11821 -1042 393 -3395 C ATOM 441 CG LEU A 79 -25.807 259.381 817.449 1.00 75.78 C ANISOU 441 CG LEU A 79 7321 9139 12332 -1075 483 -3497 C ATOM 442 CD1 LEU A 79 -25.676 260.567 816.575 1.00 73.24 C ANISOU 442 CD1 LEU A 79 6805 8483 12541 -1231 515 -3393 C ATOM 443 CD2 LEU A 79 -24.948 258.289 816.929 1.00 89.29 C ANISOU 443 CD2 LEU A 79 9224 10921 13783 -1020 717 -3245 C ATOM 444 C LEU A 79 -23.485 258.979 820.215 1.00 80.20 C ANISOU 444 C LEU A 79 8099 10257 12116 -900 479 -2980 C ATOM 445 O LEU A 79 -23.483 259.739 821.144 1.00 94.39 O ANISOU 445 O LEU A 79 9769 12115 13979 -874 304 -3035 O ATOM 446 N THR A 80 -22.367 258.538 819.676 1.00 72.63 N ANISOU 446 N THR A 80 7256 9259 11082 -896 703 -2681 N ATOM 447 CA THR A 80 -21.115 259.030 820.183 1.00 72.84 C ANISOU 447 CA THR A 80 7262 9309 11104 -853 756 -2434 C ATOM 448 CB THR A 80 -20.566 258.151 821.246 1.00 64.28 C ANISOU 448 CB THR A 80 6412 8420 9591 -737 667 -2326 C ATOM 449 OG1 THR A 80 -19.664 257.248 820.648 1.00 56.77 O ANISOU 449 OG1 THR A 80 5663 7442 8465 -736 857 -2083 O ATOM 450 CG2 THR A 80 -21.663 257.395 821.889 1.00 65.59 C ANISOU 450 CG2 THR A 80 6701 8757 9463 -717 483 -2537 C ATOM 451 C THR A 80 -20.108 259.187 819.082 1.00 72.77 C ANISOU 451 C THR A 80 7263 9138 11246 -906 1016 -2173 C ATOM 452 O THR A 80 -20.209 258.550 818.061 1.00 56.34 O ANISOU 452 O THR A 80 5282 6958 9166 -950 1134 -2128 O ATOM 453 N PHE A 81 -19.140 260.061 819.304 1.00 75.41 N ANISOU 453 N PHE A 81 7485 9463 11704 -891 1096 -2015 N ATOM 454 CA PHE A 81 -18.108 260.332 818.329 1.00 73.99 C ANISOU 454 CA PHE A 81 7329 9161 11621 -938 1343 -1761 C ATOM 455 CB PHE A 81 -18.321 261.703 817.744 1.00 71.84 C ANISOU 455 CB PHE A 81 6775 8755 11767 -1089 1436 -1759 C ATOM 456 CG PHE A 81 -19.665 261.908 817.185 1.00 77.82 C ANISOU 456 CG PHE A 81 7420 9352 12797 -1219 1327 -1959 C ATOM 457 CD1 PHE A 81 -19.829 262.232 815.863 1.00 76.01 C ANISOU 457 CD1 PHE A 81 7171 8873 12836 -1371 1442 -1857 C ATOM 458 CE1 PHE A 81 -21.056 262.411 815.347 1.00 80.60 C ANISOU 458 CE1 PHE A 81 7666 9263 13697 -1472 1306 -2062 C ATOM 459 CZ PHE A 81 -22.145 262.267 816.141 1.00 88.93 C ANISOU 459 CZ PHE A 81 8651 10403 14736 -1420 1068 -2393 C ATOM 460 CE2 PHE A 81 -21.999 261.943 817.452 1.00 94.21 C ANISOU 460 CE2 PHE A 81 9349 11346 15102 -1279 960 -2481 C ATOM 461 CD2 PHE A 81 -20.764 261.758 817.969 1.00 87.45 C ANISOU 461 CD2 PHE A 81 8581 10651 13995 -1181 1081 -2254 C ATOM 462 C PHE A 81 -16.764 260.372 818.969 1.00 77.09 C ANISOU 462 C PHE A 81 7803 9664 11824 -808 1403 -1588 C ATOM 463 O PHE A 81 -16.657 260.728 820.118 1.00 85.57 O ANISOU 463 O PHE A 81 8789 10865 12859 -702 1263 -1675 O ATOM 464 N TYR A 82 -15.735 260.011 818.221 1.00 74.41 N ANISOU 464 N TYR A 82 7635 9260 11375 -799 1584 -1362 N ATOM 465 CA TYR A 82 -14.377 260.232 818.643 1.00 70.51 C ANISOU 465 CA TYR A 82 7206 8839 10745 -671 1665 -1220 C ATOM 466 CB TYR A 82 -13.896 259.133 819.560 1.00 58.70 C ANISOU 466 CB TYR A 82 5970 7424 8910 -520 1499 -1198 C ATOM 467 CG TYR A 82 -14.077 257.764 819.019 1.00 55.33 C ANISOU 467 CG TYR A 82 5796 6947 8279 -575 1481 -1122 C ATOM 468 CD1 TYR A 82 -13.130 257.186 818.231 1.00 64.37 C ANISOU 468 CD1 TYR A 82 7140 8008 9311 -576 1597 -930 C ATOM 469 CE1 TYR A 82 -13.297 255.949 817.749 1.00 59.58 C ANISOU 469 CE1 TYR A 82 6727 7358 8554 -630 1558 -874 C ATOM 470 CZ TYR A 82 -14.411 255.269 818.059 1.00 57.33 C ANISOU 470 CZ TYR A 82 6409 7166 8206 -686 1475 -1008 C ATOM 471 OH TYR A 82 -14.584 254.021 817.581 1.00 48.05 O ANISOU 471 OH TYR A 82 5368 5999 6889 -746 1481 -963 O ATOM 472 CE2 TYR A 82 -15.354 255.812 818.837 1.00 56.65 C ANISOU 472 CE2 TYR A 82 6170 7172 8184 -678 1364 -1202 C ATOM 473 CD2 TYR A 82 -15.186 257.044 819.312 1.00 51.40 C ANISOU 473 CD2 TYR A 82 5326 6509 7694 -624 1347 -1257 C ATOM 474 C TYR A 82 -13.519 260.302 817.421 1.00 67.22 C ANISOU 474 C TYR A 82 6959 8274 10307 -716 1855 -1006 C ATOM 475 O TYR A 82 -13.856 259.732 816.419 1.00 70.55 O ANISOU 475 O TYR A 82 7538 8541 10727 -790 1859 -951 O ATOM 476 N PRO A 83 -12.407 261.005 817.504 1.00 67.48 N ANISOU 476 N PRO A 83 6971 8357 10310 -644 1990 -905 N ATOM 477 CD PRO A 83 -11.929 261.734 818.689 1.00 59.08 C ANISOU 477 CD PRO A 83 5676 7495 9278 -500 1996 -1006 C ATOM 478 CG PRO A 83 -10.537 262.117 818.312 1.00 55.53 C ANISOU 478 CG PRO A 83 5336 7064 8699 -417 2188 -861 C ATOM 479 CB PRO A 83 -10.440 262.092 816.841 1.00 61.81 C ANISOU 479 CB PRO A 83 6313 7680 9491 -575 2319 -672 C ATOM 480 CA PRO A 83 -11.438 261.019 816.408 1.00 67.90 C ANISOU 480 CA PRO A 83 7241 8296 10262 -659 2143 -695 C ATOM 481 C PRO A 83 -10.757 259.668 816.325 1.00 56.91 C ANISOU 481 C PRO A 83 6188 6858 8578 -563 2039 -605 C ATOM 482 O PRO A 83 -10.445 259.081 817.360 1.00 63.99 O ANISOU 482 O PRO A 83 7136 7865 9313 -441 1927 -660 O ATOM 483 N LEU A 84 -10.540 259.181 815.111 1.00 47.26 N ANISOU 483 N LEU A 84 5173 5475 7310 -614 2065 -467 N ATOM 484 CA LEU A 84 -9.852 257.918 814.915 1.00 39.81 C ANISOU 484 CA LEU A 84 4513 4482 6131 -544 1963 -378 C ATOM 485 CB LEU A 84 -9.985 257.473 813.459 1.00 41.26 C ANISOU 485 CB LEU A 84 4826 4494 6357 -600 1968 -278 C ATOM 486 CG LEU A 84 -9.309 256.162 813.057 1.00 37.76 C ANISOU 486 CG LEU A 84 4628 4000 5720 -541 1857 -196 C ATOM 487 CD1 LEU A 84 -9.911 255.008 813.819 1.00 33.42 C ANISOU 487 CD1 LEU A 84 4090 3515 5094 -546 1705 -298 C ATOM 488 CD2 LEU A 84 -9.451 255.966 811.567 1.00 32.37 C ANISOU 488 CD2 LEU A 84 3995 3181 5122 -573 1874 -109 C ATOM 489 C LEU A 84 -8.383 258.033 815.297 1.00 47.10 C ANISOU 489 C LEU A 84 5565 5481 6851 -415 2024 -292 C ATOM 490 O LEU A 84 -7.788 257.081 815.801 1.00 52.03 O ANISOU 490 O LEU A 84 6366 6122 7282 -331 1912 -272 O ATOM 491 N SER A 85 -7.826 259.184 815.000 1.00 53.25 N ANISOU 491 N SER A 85 6253 6311 7668 -405 2219 -244 N ATOM 492 CA SER A 85 -6.447 259.500 815.257 1.00 65.76 C ANISOU 492 CA SER A 85 7931 8003 9051 -255 2333 -205 C ATOM 493 CB SER A 85 -6.165 260.824 814.624 1.00 90.64 C ANISOU 493 CB SER A 85 10944 11227 12270 -318 2600 -134 C ATOM 494 OG SER A 85 -7.228 261.106 813.747 1.00111.99 O ANISOU 494 OG SER A 85 13554 13795 15201 -518 2616 -69 O ATOM 495 C SER A 85 -6.079 259.570 816.711 1.00 77.57 C ANISOU 495 C SER A 85 9336 9655 10484 -58 2273 -369 C ATOM 496 O SER A 85 -5.009 259.153 817.093 1.00 86.39 O ANISOU 496 O SER A 85 10643 10795 11386 127 2237 -388 O ATOM 497 N ASP A 86 -6.939 260.138 817.533 1.00 75.34 N ANISOU 497 N ASP A 86 8764 9467 10396 -65 2243 -514 N ATOM 498 CA ASP A 86 -6.585 260.290 818.920 1.00 82.68 C ANISOU 498 CA ASP A 86 9598 10521 11296 169 2139 -688 C ATOM 499 CB ASP A 86 -6.292 261.752 819.173 1.00 87.87 C ANISOU 499 CB ASP A 86 9921 11365 12101 245 2360 -791 C ATOM 500 CG ASP A 86 -5.537 261.975 820.430 1.00 95.30 C ANISOU 500 CG ASP A 86 10818 12398 12993 548 2231 -973 C ATOM 501 OD1 ASP A 86 -4.883 261.036 820.898 1.00102.30 O ANISOU 501 OD1 ASP A 86 12019 13172 13679 709 2007 -976 O ATOM 502 OD2 ASP A 86 -5.584 263.098 820.946 1.00 93.78 O ANISOU 502 OD2 ASP A 86 10266 12380 12986 626 2342 -1117 O ATOM 503 C ASP A 86 -7.682 259.873 819.844 1.00 78.05 C ANISOU 503 C ASP A 86 8926 9926 10803 146 1886 -797 C ATOM 504 O ASP A 86 -8.157 260.668 820.601 1.00 74.18 O ANISOU 504 O ASP A 86 8156 9542 10488 196 1848 -945 O ATOM 505 N ALA A 87 -8.023 258.606 819.856 1.00 69.11 N ANISOU 505 N ALA A 87 8038 8687 9533 81 1699 -731 N ATOM 506 CA ALA A 87 -9.120 258.148 820.664 1.00 51.55 C ANISOU 506 CA ALA A 87 5769 6485 7333 36 1479 -819 C ATOM 507 CB ALA A 87 -9.360 256.733 820.421 1.00 42.85 C ANISOU 507 CB ALA A 87 4934 5301 6047 -70 1366 -710 C ATOM 508 C ALA A 87 -8.918 258.399 822.140 1.00 53.24 C ANISOU 508 C ALA A 87 5944 6759 7528 243 1248 -946 C ATOM 509 O ALA A 87 -9.874 258.636 822.845 1.00 57.16 O ANISOU 509 O ALA A 87 6279 7323 8117 228 1102 -1066 O ATOM 510 N TYR A 88 -7.689 258.291 822.621 1.00 56.20 N ANISOU 510 N TYR A 88 6486 7088 7779 451 1172 -932 N ATOM 511 CA TYR A 88 -7.392 258.477 824.045 1.00 56.28 C ANISOU 511 CA TYR A 88 6488 7108 7788 691 900 -1055 C ATOM 512 CB TYR A 88 -6.127 257.749 824.434 1.00 63.35 C ANISOU 512 CB TYR A 88 7729 7854 8488 869 733 -990 C ATOM 513 CG TYR A 88 -5.944 257.682 825.921 1.00 74.29 C ANISOU 513 CG TYR A 88 9181 9181 9866 1100 365 -1084 C ATOM 514 CD1 TYR A 88 -6.661 256.794 826.679 1.00 74.43 C ANISOU 514 CD1 TYR A 88 9383 9131 9765 1009 63 -995 C ATOM 515 CE1 TYR A 88 -6.498 256.724 828.026 1.00 77.15 C ANISOU 515 CE1 TYR A 88 9826 9391 10095 1214 -313 -1047 C ATOM 516 CZ TYR A 88 -5.609 257.543 828.632 1.00 84.93 C ANISOU 516 CZ TYR A 88 10694 10353 11221 1544 -396 -1227 C ATOM 517 OH TYR A 88 -5.451 257.475 829.983 1.00 87.69 O ANISOU 517 OH TYR A 88 11145 10585 11588 1775 -819 -1286 O ATOM 518 CE2 TYR A 88 -4.882 258.423 827.906 1.00 85.99 C ANISOU 518 CE2 TYR A 88 10614 10587 11471 1651 -67 -1349 C ATOM 519 CD2 TYR A 88 -5.051 258.494 826.562 1.00 81.53 C ANISOU 519 CD2 TYR A 88 9982 10113 10884 1415 314 -1260 C ATOM 520 C TYR A 88 -7.320 259.855 824.661 1.00 65.26 C ANISOU 520 C TYR A 88 7251 8386 9157 873 940 -1259 C ATOM 521 O TYR A 88 -7.838 260.068 825.728 1.00 72.74 O ANISOU 521 O TYR A 88 8079 9369 10189 972 689 -1379 O ATOM 522 N HIS A 89 -6.623 260.768 824.014 1.00 70.81 N ANISOU 522 N HIS A 89 7775 9183 9948 922 1249 -1294 N ATOM 523 CA HIS A 89 -6.516 262.121 824.507 1.00 64.41 C ANISOU 523 CA HIS A 89 6547 8551 9376 1071 1351 -1489 C ATOM 524 CB HIS A 89 -5.152 262.679 824.184 1.00 63.94 C ANISOU 524 CB HIS A 89 6476 8574 9246 1261 1600 -1532 C ATOM 525 CG HIS A 89 -4.028 261.927 824.810 1.00 73.57 C ANISOU 525 CG HIS A 89 8048 9651 10255 1544 1362 -1569 C ATOM 526 ND1 HIS A 89 -3.777 261.964 826.158 1.00 79.51 N ANISOU 526 ND1 HIS A 89 8773 10363 11076 1842 1030 -1746 N ATOM 527 CE1 HIS A 89 -2.729 261.214 826.428 1.00 79.77 C ANISOU 527 CE1 HIS A 89 9181 10216 10912 2040 844 -1739 C ATOM 528 NE2 HIS A 89 -2.289 260.694 825.300 1.00 79.71 N ANISOU 528 NE2 HIS A 89 9429 10152 10706 1876 1048 -1571 N ATOM 529 CD2 HIS A 89 -3.085 261.127 824.275 1.00 75.01 C ANISOU 529 CD2 HIS A 89 8625 9693 10182 1575 1370 -1458 C ATOM 530 C HIS A 89 -7.555 262.980 823.864 1.00 62.69 C ANISOU 530 C HIS A 89 5968 8446 9405 814 1572 -1493 C ATOM 531 O HIS A 89 -7.886 264.026 824.356 1.00 59.15 O ANISOU 531 O HIS A 89 5119 8143 9214 857 1597 -1651 O ATOM 532 N GLY A 90 -8.083 262.517 822.756 1.00 68.73 N ANISOU 532 N GLY A 90 6871 9124 10119 544 1708 -1325 N ATOM 533 CA GLY A 90 -9.127 263.225 822.062 1.00 67.16 C ANISOU 533 CA GLY A 90 6385 8962 10170 280 1873 -1317 C ATOM 534 C GLY A 90 -10.364 263.041 822.882 1.00 73.43 C ANISOU 534 C GLY A 90 7075 9745 11078 243 1568 -1453 C ATOM 535 O GLY A 90 -10.370 262.247 823.787 1.00 80.69 O ANISOU 535 O GLY A 90 8205 10625 11828 385 1272 -1491 O ATOM 536 N LYS A 91 -11.404 263.799 822.623 1.00 67.11 N ANISOU 536 N LYS A 91 5962 8975 10560 53 1615 -1529 N ATOM 537 CA LYS A 91 -12.570 263.635 823.440 1.00 66.07 C ANISOU 537 CA LYS A 91 5752 8845 10506 39 1296 -1691 C ATOM 538 CB LYS A 91 -13.006 264.964 824.028 1.00 67.34 C ANISOU 538 CB LYS A 91 5426 9132 11028 43 1256 -1882 C ATOM 539 CG LYS A 91 -13.876 265.766 823.118 1.00 72.81 C ANISOU 539 CG LYS A 91 5840 9787 12038 -255 1431 -1884 C ATOM 540 CD LYS A 91 -14.195 267.114 823.679 1.00 71.54 C ANISOU 540 CD LYS A 91 5159 9757 12267 -278 1407 -2058 C ATOM 541 CE LYS A 91 -14.617 268.017 822.579 1.00 55.35 C ANISOU 541 CE LYS A 91 2845 7654 10530 -599 1683 -1973 C ATOM 542 NZ LYS A 91 -14.259 269.400 822.884 1.00 93.19 N ANISOU 542 NZ LYS A 91 7125 12634 15651 -622 1853 -2038 N ATOM 543 C LYS A 91 -13.682 263.051 822.644 1.00 64.86 C ANISOU 543 C LYS A 91 5720 8578 10347 -197 1285 -1659 C ATOM 544 O LYS A 91 -13.975 263.505 821.569 1.00 76.56 O ANISOU 544 O LYS A 91 7089 9991 12011 -398 1504 -1594 O ATOM 545 N THR A 92 -14.279 262.006 823.180 1.00 60.29 N ANISOU 545 N THR A 92 5387 7978 9544 -165 1025 -1702 N ATOM 546 CA THR A 92 -15.433 261.391 822.589 1.00 60.79 C ANISOU 546 CA THR A 92 5546 7974 9579 -343 987 -1740 C ATOM 547 CB THR A 92 -15.585 260.001 823.095 1.00 52.26 C ANISOU 547 CB THR A 92 4818 6913 8124 -286 801 -1702 C ATOM 548 OG1 THR A 92 -16.230 260.065 824.351 1.00 72.71 O ANISOU 548 OG1 THR A 92 7370 9602 10654 -196 483 -1864 O ATOM 549 CG2 THR A 92 -14.255 259.384 823.300 1.00 50.66 C ANISOU 549 CG2 THR A 92 4873 6687 7689 -152 832 -1513 C ATOM 550 C THR A 92 -16.639 262.189 823.031 1.00 72.18 C ANISOU 550 C THR A 92 6688 9456 11282 -412 810 -1978 C ATOM 551 O THR A 92 -16.677 262.684 824.133 1.00 76.51 O ANISOU 551 O THR A 92 7081 10102 11887 -284 596 -2106 O ATOM 552 N ILE A 93 -17.632 262.303 822.169 1.00 71.22 N ANISOU 552 N ILE A 93 6488 9238 11335 -604 865 -2054 N ATOM 553 CA ILE A 93 -18.837 263.072 822.434 1.00 64.20 C ANISOU 553 CA ILE A 93 5321 8344 10730 -698 683 -2300 C ATOM 554 CB ILE A 93 -19.060 264.117 821.340 1.00 65.06 C ANISOU 554 CB ILE A 93 5154 8304 11262 -917 891 -2271 C ATOM 555 CG1 ILE A 93 -17.815 264.987 821.178 1.00 73.21 C ANISOU 555 CG1 ILE A 93 6005 9387 12424 -908 1159 -2079 C ATOM 556 CD1 ILE A 93 -18.025 266.160 820.257 1.00 86.63 C ANISOU 556 CD1 ILE A 93 7401 10972 14541 -1161 1361 -2017 C ATOM 557 CG2 ILE A 93 -20.298 264.952 821.643 1.00 64.59 C ANISOU 557 CG2 ILE A 93 4791 8207 11542 -1034 665 -2538 C ATOM 558 C ILE A 93 -20.070 262.186 822.482 1.00 68.18 C ANISOU 558 C ILE A 93 6012 8843 11051 -731 484 -2478 C ATOM 559 O ILE A 93 -20.459 261.607 821.474 1.00 81.93 O ANISOU 559 O ILE A 93 7886 10477 12768 -830 611 -2458 O ATOM 560 N ASN A 94 -20.685 262.086 823.653 1.00 72.38 N ANISOU 560 N ASN A 94 6552 9503 11447 -633 166 -2665 N ATOM 561 CA ASN A 94 -21.922 261.329 823.801 1.00 78.10 C ANISOU 561 CA ASN A 94 7444 10276 11955 -656 -26 -2873 C ATOM 562 CB ASN A 94 -21.950 260.610 825.151 1.00 84.02 C ANISOU 562 CB ASN A 94 8429 11214 12281 -501 -305 -2889 C ATOM 563 CG ASN A 94 -20.909 259.522 825.247 1.00 82.12 C ANISOU 563 CG ASN A 94 8513 11017 11672 -427 -176 -2604 C ATOM 564 OD1 ASN A 94 -20.384 259.066 824.233 1.00 86.01 O ANISOU 564 OD1 ASN A 94 9092 11424 12163 -495 109 -2439 O ATOM 565 ND2 ASN A 94 -20.605 259.096 826.468 1.00 74.02 N ANISOU 565 ND2 ASN A 94 7679 10100 10346 -293 -422 -2537 N ATOM 566 C ASN A 94 -23.135 262.237 823.681 1.00 77.58 C ANISOU 566 C ASN A 94 7100 10133 12243 -767 -197 -3171 C ATOM 567 O ASN A 94 -23.245 263.222 824.402 1.00 94.20 O ANISOU 567 O ASN A 94 8935 12268 14590 -748 -391 -3285 O ATOM 568 N ILE A 95 -24.049 261.907 822.777 1.00 72.12 N ANISOU 568 N ILE A 95 6463 9332 11609 -873 -150 -3317 N ATOM 569 CA ILE A 95 -25.254 262.707 822.608 1.00 84.49 C ANISOU 569 CA ILE A 95 7799 10777 13525 -981 -348 -3627 C ATOM 570 CB ILE A 95 -25.359 263.266 821.177 1.00 87.80 C ANISOU 570 CB ILE A 95 8068 10907 14385 -1168 -138 -3577 C ATOM 571 CG1 ILE A 95 -24.189 264.209 820.894 1.00 87.22 C ANISOU 571 CG1 ILE A 95 7774 10767 14599 -1255 97 -3274 C ATOM 572 CD1 ILE A 95 -24.299 264.948 819.585 1.00 79.85 C ANISOU 572 CD1 ILE A 95 6681 9543 14115 -1479 269 -3182 C ATOM 573 CG2 ILE A 95 -26.693 263.970 820.976 1.00 59.28 C ANISOU 573 CG2 ILE A 95 4263 7123 11138 -1287 -387 -3920 C ATOM 574 C ILE A 95 -26.501 261.899 822.936 1.00 88.88 C ANISOU 574 C ILE A 95 8559 11441 13770 -920 -578 -3943 C ATOM 575 O ILE A 95 -26.997 261.148 822.102 1.00102.12 O ANISOU 575 O ILE A 95 10391 13065 15346 -938 -456 -4026 O ATOM 576 N HIS A 96 -27.006 262.054 824.155 1.00 88.73 N ANISOU 576 N HIS A 96 8536 11588 13588 -833 -916 -4131 N ATOM 577 CA HIS A 96 -28.194 261.321 824.590 1.00 90.64 C ANISOU 577 CA HIS A 96 8996 11984 13458 -767 -1149 -4441 C ATOM 578 CB HIS A 96 -28.354 261.425 826.103 1.00 92.19 C ANISOU 578 CB HIS A 96 9250 12393 13385 -648 -1522 -4519 C ATOM 579 CG HIS A 96 -27.194 260.874 826.861 1.00 98.08 C ANISOU 579 CG HIS A 96 10185 13286 13796 -537 -1463 -4173 C ATOM 580 ND1 HIS A 96 -27.266 259.705 827.599 1.00102.06 N ANISOU 580 ND1 HIS A 96 11072 14022 13686 -449 -1546 -4098 N ATOM 581 CE1 HIS A 96 -26.101 259.460 828.149 1.00103.31 C ANISOU 581 CE1 HIS A 96 11338 14210 13706 -372 -1506 -3771 C ATOM 582 NE2 HIS A 96 -25.256 260.422 827.794 1.00101.06 N ANISOU 582 NE2 HIS A 96 10747 13751 13898 -381 -1378 -3657 N ATOM 583 CD2 HIS A 96 -25.920 261.308 826.988 1.00 98.02 C ANISOU 583 CD2 HIS A 96 10053 13217 13975 -502 -1333 -3882 C ATOM 584 C HIS A 96 -29.453 261.810 823.885 1.00 93.44 C ANISOU 584 C HIS A 96 9204 12151 14147 -861 -1275 -4817 C ATOM 585 O HIS A 96 -29.509 262.949 823.432 1.00 97.18 O ANISOU 585 O HIS A 96 9366 12381 15177 -994 -1309 -4853 O ATOM 586 N LEU A 97 -30.438 260.937 823.757 1.00100.74 N ANISOU 586 N LEU A 97 10354 13186 14737 -800 -1332 -5094 N ATOM 587 CA LEU A 97 -31.640 261.267 823.018 1.00106.72 C ANISOU 587 CA LEU A 97 11016 13742 15792 -852 -1457 -5491 C ATOM 588 C LEU A 97 -32.899 260.999 823.808 1.00102.39 C ANISOU 588 C LEU A 97 10609 13390 14904 -753 -1809 -5927 C ATOM 589 O LEU A 97 -32.986 260.044 824.566 1.00 92.05 O ANISOU 589 O LEU A 97 9582 12417 12978 -637 -1828 -5924 O ATOM 590 CB LEU A 97 -31.663 260.497 821.706 1.00107.15 C ANISOU 590 CB LEU A 97 11172 13677 15862 -854 -1136 -5470 C ATOM 591 CG LEU A 97 -30.828 261.123 820.603 1.00 97.76 C ANISOU 591 CG LEU A 97 9795 12159 15190 -993 -891 -5165 C ATOM 592 CD2 LEU A 97 -31.539 262.331 820.095 1.00 97.29 C ANISOU 592 CD2 LEU A 97 9474 11746 15745 -1138 -1099 -5384 C ATOM 593 CD1 LEU A 97 -30.597 260.152 819.494 1.00 88.91 C ANISOU 593 CD1 LEU A 97 8823 10985 13972 -952 -585 -5064 C ATOM 594 N PRO A 98 -33.871 261.874 823.650 1.00110.22 N ANISOU 594 N PRO A 98 11413 14167 16297 -813 -2107 -6297 N ATOM 595 CA PRO A 98 -35.126 261.711 824.361 1.00120.78 C ANISOU 595 CA PRO A 98 12888 15673 17330 -713 -2485 -6764 C ATOM 596 C PRO A 98 -35.842 260.447 823.933 1.00130.89 C ANISOU 596 C PRO A 98 14466 17147 18119 -582 -2326 -7016 C ATOM 597 O PRO A 98 -36.275 259.669 824.764 1.00137.09 O ANISOU 597 O PRO A 98 15521 18300 18268 -463 -2424 -7148 O ATOM 598 CB PRO A 98 -35.933 262.922 823.898 1.00109.63 C ANISOU 598 CB PRO A 98 11183 13884 16588 -840 -2780 -7094 C ATOM 599 CG PRO A 98 -35.059 263.674 822.958 1.00102.62 C ANISOU 599 CG PRO A 98 10017 12656 16319 -1025 -2518 -6745 C ATOM 600 CD PRO A 98 -34.016 262.767 822.501 1.00102.39 C ANISOU 600 CD PRO A 98 10153 12747 16002 -975 -2063 -6342 C ATOM 601 N ASN A 99 -35.915 260.221 822.633 1.00130.64 N ANISOU 601 N ASN A 99 14384 16883 18371 -604 -2068 -7059 N ATOM 602 CA ASN A 99 -36.625 259.072 822.109 1.00135.75 C ANISOU 602 CA ASN A 99 15241 17701 18635 -461 -1902 -7350 C ATOM 603 C ASN A 99 -35.882 258.415 820.982 1.00131.66 C ANISOU 603 C ASN A 99 14715 17087 18223 -469 -1465 -7066 C ATOM 604 O ASN A 99 -35.184 259.061 820.223 1.00132.59 O ANISOU 604 O ASN A 99 14647 16859 18873 -591 -1355 -6791 O ATOM 605 CB ASN A 99 -38.018 259.463 821.637 1.00145.25 C ANISOU 605 CB ASN A 99 16394 18688 20106 -405 -2193 -7957 C ATOM 606 CG ASN A 99 -38.980 259.642 822.775 1.00158.70 C ANISOU 606 CG ASN A 99 18216 20623 21460 -330 -2613 -8350 C ATOM 607 ND2 ASN A 99 -39.347 260.887 823.044 1.00163.93 N ANISOU 607 ND2 ASN A 99 18671 20999 22614 -436 -3019 -8511 N ATOM 608 OD1 ASN A 99 -39.399 258.674 823.404 1.00162.21 O ANISOU 608 OD1 ASN A 99 18933 21505 21192 -191 -2581 -8504 O ATOM 609 N ALA A 100 -36.095 257.122 820.846 1.00120.14 N ANISOU 609 N ALA A 100 13451 15947 16250 -341 -1224 -7156 N ATOM 610 CA ALA A 100 -35.361 256.320 819.915 1.00 99.73 C ANISOU 610 CA ALA A 100 10866 13347 13679 -333 -822 -6883 C ATOM 611 C ALA A 100 -35.675 256.789 818.534 1.00102.77 C ANISOU 611 C ALA A 100 11073 13271 14703 -332 -820 -7058 C ATOM 612 O ALA A 100 -36.665 257.442 818.310 1.00111.20 O ANISOU 612 O ALA A 100 12065 14100 16086 -306 -1105 -7476 O ATOM 613 CB ALA A 100 -35.737 254.893 820.069 1.00 95.57 C ANISOU 613 CB ALA A 100 10532 13274 12504 -205 -596 -7030 C ATOM 614 N SER A 101 -34.827 256.461 817.564 1.00106.85 N ANISOU 614 N SER A 101 11535 13628 15434 -363 -530 -6734 N ATOM 615 CA SER A 101 -35.069 256.795 816.155 1.00121.86 C ANISOU 615 CA SER A 101 13303 15069 17930 -351 -533 -6853 C ATOM 616 C SER A 101 -36.193 255.936 815.609 1.00130.49 C ANISOU 616 C SER A 101 14436 16256 18887 -129 -522 -7392 C ATOM 617 O SER A 101 -36.395 254.840 816.089 1.00133.22 O ANISOU 617 O SER A 101 14899 17073 18644 -11 -347 -7511 O ATOM 618 CB SER A 101 -33.821 256.567 815.321 1.00121.39 C ANISOU 618 CB SER A 101 13210 14861 18053 -423 -242 -6351 C ATOM 619 OG SER A 101 -34.160 256.426 813.956 1.00124.92 O ANISOU 619 OG SER A 101 13589 14967 18907 -343 -221 -6510 O ATOM 620 N MSE A 102 -36.928 256.406 814.606 1.00130.59 N ANISOU 620 N MSE A 102 14351 15829 19437 -69 -704 -7722 N ATOM 621 CA MSE A 102 -38.094 255.649 814.158 1.00132.22 C ANISOU 621 CA MSE A 102 14583 16129 19525 188 -732 -8327 C ATOM 622 C MSE A 102 -37.692 254.279 813.661 1.00128.55 C ANISOU 622 C MSE A 102 14127 15977 18741 331 -343 -8241 C ATOM 623 O MSE A 102 -38.284 253.276 814.039 1.00123.32 O ANISOU 623 O MSE A 102 13525 15783 17546 498 -200 -8568 O ATOM 624 CB MSE A 102 -38.797 256.376 813.006 1.00137.87 C ANISOU 624 CB MSE A 102 15196 16223 20967 236 -1009 -8643 C ATOM 625 CG MSE A 102 -40.334 256.581 813.129 1.00142.30 C ANISOU 625 CG MSE A 102 15785 16707 21577 410 -1355 -9391 C ATOM 626 SE MSE A 102 -41.388 255.274 814.103 1.00164.88 Se ANISOU 626 SE MSE A 102 18803 20349 23496 702 -1239 -10004 Se ATOM 627 CE MSE A 102 -40.191 254.949 815.582 1.00190.60 C ANISOU 627 CE MSE A 102 22181 24197 26040 479 -976 -9337 C ATOM 628 N ASN A 103 -36.646 254.233 812.857 1.00123.34 N ANISOU 628 N ASN A 103 13400 15089 18376 248 -166 -7780 N ATOM 629 CA ASN A 103 -36.196 252.991 812.268 1.00118.47 C ANISOU 629 CA ASN A 103 12748 14708 17557 366 168 -7677 C ATOM 630 CB ASN A 103 -36.317 253.079 810.769 1.00125.09 C ANISOU 630 CB ASN A 103 13466 15055 19008 484 100 -7786 C ATOM 631 CG ASN A 103 -35.975 251.801 810.105 1.00125.31 C ANISOU 631 CG ASN A 103 13410 15316 18886 637 399 -7758 C ATOM 632 OD1 ASN A 103 -35.933 250.761 810.746 1.00118.21 O ANISOU 632 OD1 ASN A 103 12525 14983 17407 678 666 -7788 O ATOM 633 ND2 ASN A 103 -35.731 251.857 808.815 1.00128.48 N ANISOU 633 ND2 ASN A 103 13719 15283 19814 712 345 -7690 N ATOM 634 C ASN A 103 -34.761 252.941 812.607 1.00115.35 C ANISOU 634 C ASN A 103 12401 14413 17013 164 370 -7011 C ATOM 635 O ASN A 103 -33.914 253.307 811.801 1.00110.38 O ANISOU 635 O ASN A 103 11724 13429 16785 76 398 -6641 O ATOM 636 N GLN A 104 -34.462 252.539 813.823 1.00125.39 N ANISOU 636 N GLN A 104 13790 16146 17706 86 482 -6847 N ATOM 637 CA GLN A 104 -33.104 252.833 814.277 1.00132.54 C ANISOU 637 CA GLN A 104 14755 17045 18558 -114 573 -6234 C ATOM 638 C GLN A 104 -32.017 252.798 813.203 1.00132.15 C ANISOU 638 C GLN A 104 14643 16700 18868 -168 719 -5827 C ATOM 639 O GLN A 104 -31.906 251.833 812.449 1.00137.25 O ANISOU 639 O GLN A 104 15236 17425 19490 -65 904 -5854 O ATOM 640 CB GLN A 104 -32.725 251.881 815.418 1.00134.61 C ANISOU 640 CB GLN A 104 15163 17858 18123 -154 759 -6050 C ATOM 641 CG GLN A 104 -32.522 250.434 814.991 1.00132.97 C ANISOU 641 CG GLN A 104 14938 18034 17552 -44 1048 -6191 C ATOM 642 CD GLN A 104 -33.830 249.712 814.708 1.00126.16 C ANISOU 642 CD GLN A 104 14243 17712 15981 -129 1209 -6003 C ATOM 643 OE1 GLN A 104 -34.915 250.288 814.830 1.00130.89 O ANISOU 643 OE1 GLN A 104 14997 18397 16337 -229 1056 -5832 O ATOM 644 NE2 GLN A 104 -33.729 248.444 814.332 1.00111.28 N ANISOU 644 NE2 GLN A 104 12319 16185 13777 -95 1507 -6026 N ATOM 645 N ARG A 105 -31.260 253.875 813.143 1.00124.40 N ANISOU 645 N ARG A 105 13655 15395 18216 -327 624 -5474 N ATOM 646 CA ARG A 105 -30.119 254.046 812.267 1.00107.39 C ANISOU 646 CA ARG A 105 11486 12965 16353 -410 736 -5034 C ATOM 647 C ARG A 105 -30.349 254.103 810.800 1.00 98.39 C ANISOU 647 C ARG A 105 10265 11417 15702 -333 685 -5126 C ATOM 648 O ARG A 105 -29.410 254.280 810.051 1.00 89.72 O ANISOU 648 O ARG A 105 9182 10082 14826 -405 749 -4749 O ATOM 649 CB ARG A 105 -29.080 252.979 812.570 1.00 93.04 C ANISOU 649 CB ARG A 105 9756 11483 14112 -425 994 -4694 C ATOM 650 CG ARG A 105 -28.940 251.942 811.515 1.00 96.32 C ANISOU 650 CG ARG A 105 10115 11898 14586 -316 1147 -4712 C ATOM 651 CD ARG A 105 -28.092 252.427 810.374 1.00106.02 C ANISOU 651 CD ARG A 105 11331 12702 16252 -367 1128 -4387 C ATOM 652 NE ARG A 105 -27.788 251.355 809.435 1.00114.53 N ANISOU 652 NE ARG A 105 12353 13803 17359 -260 1254 -4356 N ATOM 653 CZ ARG A 105 -27.177 251.539 808.277 1.00111.56 C ANISOU 653 CZ ARG A 105 11971 13071 17344 -258 1212 -4129 C ATOM 654 NH1 ARG A 105 -26.797 252.742 807.927 1.00118.68 N ANISOU 654 NH1 ARG A 105 12937 13587 18570 -378 1086 -3892 N ATOM 655 NH2 ARG A 105 -26.945 250.521 807.477 1.00100.30 N ANISOU 655 NH2 ARG A 105 10472 11688 15949 -146 1293 -4132 N ATOM 656 N TYR A 106 -31.581 253.963 810.366 1.00103.52 N ANISOU 656 N TYR A 106 10845 11967 16522 -174 545 -5630 N ATOM 657 CA TYR A 106 -31.790 254.018 808.944 1.00108.15 C ANISOU 657 CA TYR A 106 11364 12114 17614 -78 450 -5716 C ATOM 658 C TYR A 106 -32.321 255.381 808.711 1.00117.10 C ANISOU 658 C TYR A 106 12481 12771 19242 -189 157 -5801 C ATOM 659 O TYR A 106 -32.237 255.933 807.625 1.00116.17 O ANISOU 659 O TYR A 106 12353 12157 19631 -227 21 -5683 O ATOM 660 CB TYR A 106 -32.726 252.914 808.486 1.00114.54 C ANISOU 660 CB TYR A 106 12085 13092 18344 199 487 -6224 C ATOM 661 CG TYR A 106 -32.054 251.562 808.498 1.00109.41 C ANISOU 661 CG TYR A 106 11406 12867 17296 263 797 -6060 C ATOM 662 CD1 TYR A 106 -31.103 251.232 807.554 1.00 99.44 C ANISOU 662 CD1 TYR A 106 10121 11422 16241 256 876 -5707 C ATOM 663 CE1 TYR A 106 -30.481 250.013 807.578 1.00 98.36 C ANISOU 663 CE1 TYR A 106 9935 11659 15778 289 1132 -5558 C ATOM 664 CZ TYR A 106 -30.806 249.107 808.553 1.00 96.76 C ANISOU 664 CZ TYR A 106 9714 12026 15026 308 1339 -5731 C ATOM 665 OH TYR A 106 -30.207 247.885 808.598 1.00 86.90 O ANISOU 665 OH TYR A 106 8400 11149 13468 299 1597 -5567 O ATOM 666 CE2 TYR A 106 -31.735 249.409 809.496 1.00104.29 C ANISOU 666 CE2 TYR A 106 10720 13182 15724 318 1278 -6058 C ATOM 667 CD2 TYR A 106 -32.351 250.629 809.470 1.00109.37 C ANISOU 667 CD2 TYR A 106 11406 13446 16704 307 996 -6234 C ATOM 668 N THR A 107 -32.862 255.934 809.780 1.00121.25 N ANISOU 668 N THR A 107 13008 13449 19612 -261 41 -5987 N ATOM 669 CA THR A 107 -33.417 257.281 809.725 1.00116.12 C ANISOU 669 CA THR A 107 12310 12378 19432 -405 -257 -6085 C ATOM 670 C THR A 107 -32.408 258.291 810.277 1.00111.81 C ANISOU 670 C THR A 107 11749 11801 18932 -684 -206 -5576 C ATOM 671 O THR A 107 -32.764 259.212 811.014 1.00117.80 O ANISOU 671 O THR A 107 12441 12528 19788 -818 -380 -5658 O ATOM 672 CB THR A 107 -34.740 257.373 810.512 1.00112.45 C ANISOU 672 CB THR A 107 11829 12059 18837 -306 -481 -6667 C ATOM 673 OG1 THR A 107 -34.593 256.704 811.770 1.00118.30 O ANISOU 673 OG1 THR A 107 12636 13396 18918 -266 -321 -6678 O ATOM 674 CG2 THR A 107 -35.866 256.719 809.734 1.00100.67 C ANISOU 674 CG2 THR A 107 10324 10447 17480 -33 -596 -7235 C ATOM 675 N LEU A 108 -31.147 258.105 809.905 1.00 99.92 N ANISOU 675 N LEU A 108 10291 10314 17359 -757 27 -5075 N ATOM 676 CA LEU A 108 -30.063 258.969 810.352 1.00 91.26 C ANISOU 676 CA LEU A 108 9178 9228 16269 -985 128 -4594 C ATOM 677 C LEU A 108 -29.259 259.446 809.153 1.00 89.40 C ANISOU 677 C LEU A 108 8971 8601 16396 -1115 192 -4176 C ATOM 678 O LEU A 108 -29.221 258.777 808.125 1.00 90.59 O ANISOU 678 O LEU A 108 9191 8588 16643 -994 211 -4171 O ATOM 679 CB LEU A 108 -29.150 258.201 811.300 1.00 81.66 C ANISOU 679 CB LEU A 108 8042 8507 14477 -937 366 -4373 C ATOM 680 CG LEU A 108 -27.985 258.965 811.917 1.00 74.35 C ANISOU 680 CG LEU A 108 7098 7663 13488 -1108 480 -3935 C ATOM 681 CD1 LEU A 108 -28.478 259.741 813.109 1.00 83.79 C ANISOU 681 CD1 LEU A 108 8185 8993 14660 -1175 314 -4112 C ATOM 682 CD2 LEU A 108 -26.871 258.014 812.317 1.00 74.44 C ANISOU 682 CD2 LEU A 108 7242 8014 13029 -1038 716 -3649 C ATOM 683 N THR A 109 -28.655 260.599 809.260 1.00 89.66 N ANISOU 683 N THR A 109 8943 8490 16631 -1355 215 -3838 N ATOM 684 CA THR A 109 -27.776 261.009 808.217 1.00 94.83 C ANISOU 684 CA THR A 109 9663 8851 17516 -1491 314 -3392 C ATOM 685 C THR A 109 -26.730 261.826 808.879 1.00 99.97 C ANISOU 685 C THR A 109 10256 9679 18047 -1682 497 -3008 C ATOM 686 O THR A 109 -27.040 262.666 809.689 1.00102.47 O ANISOU 686 O THR A 109 10414 10061 18461 -1806 425 -3098 O ATOM 687 CB THR A 109 -28.473 261.920 807.305 1.00103.26 C ANISOU 687 CB THR A 109 10687 9382 19164 -1644 84 -3431 C ATOM 688 OG1 THR A 109 -28.459 263.215 807.897 1.00105.75 O ANISOU 688 OG1 THR A 109 10843 9653 19684 -1911 54 -3313 O ATOM 689 CG2 THR A 109 -29.879 261.472 807.163 1.00103.09 C ANISOU 689 CG2 THR A 109 10643 9219 19308 -1459 -182 -3995 C ATOM 690 N ILE A 110 -25.489 261.616 808.508 1.00101.17 N ANISOU 690 N ILE A 110 10527 9904 18009 -1700 720 -2596 N ATOM 691 CA ILE A 110 -24.429 262.422 809.034 1.00 96.00 C ANISOU 691 CA ILE A 110 9816 9413 17246 -1859 914 -2243 C ATOM 692 C ILE A 110 -23.722 262.958 807.844 1.00 96.92 C ANISOU 692 C ILE A 110 10030 9233 17563 -2011 1008 -1827 C ATOM 693 O ILE A 110 -23.244 262.208 807.026 1.00 86.81 O ANISOU 693 O ILE A 110 8937 7888 16159 -1893 1051 -1676 O ATOM 694 CB ILE A 110 -23.459 261.578 809.818 1.00 86.18 C ANISOU 694 CB ILE A 110 8671 8592 15480 -1700 1101 -2140 C ATOM 695 CG1 ILE A 110 -24.082 261.217 811.147 1.00 91.23 C ANISOU 695 CG1 ILE A 110 9229 9550 15884 -1581 1006 -2483 C ATOM 696 CD1 ILE A 110 -25.516 260.843 810.987 1.00103.95 C ANISOU 696 CD1 ILE A 110 10807 11041 17648 -1498 779 -2922 C ATOM 697 CG2 ILE A 110 -22.201 262.322 810.043 1.00 81.87 C ANISOU 697 CG2 ILE A 110 8113 8165 14830 -1812 1318 -1756 C ATOM 698 N GLN A 111 -23.634 264.264 807.746 1.00104.42 N ANISOU 698 N GLN A 111 10851 10038 18787 -2251 1041 -1622 N ATOM 699 CA GLN A 111 -22.926 264.840 806.639 1.00106.31 C ANISOU 699 CA GLN A 111 11209 10045 19139 -2392 1148 -1180 C ATOM 700 C GLN A 111 -22.305 266.098 807.128 1.00100.22 C ANISOU 700 C GLN A 111 10269 9419 18392 -2616 1349 -923 C ATOM 701 O GLN A 111 -22.631 266.577 808.193 1.00107.49 O ANISOU 701 O GLN A 111 10948 10529 19365 -2668 1338 -1125 O ATOM 702 CB GLN A 111 -23.825 265.094 805.449 1.00112.44 C ANISOU 702 CB GLN A 111 12039 10284 20398 -2508 895 -1203 C ATOM 703 CG GLN A 111 -23.225 264.562 804.174 1.00116.83 C ANISOU 703 CG GLN A 111 12864 10637 20890 -2428 898 -906 C ATOM 704 CD GLN A 111 -23.711 263.175 803.863 1.00117.48 C ANISOU 704 CD GLN A 111 13049 10681 20906 -2135 737 -1226 C ATOM 705 OE1 GLN A 111 -23.761 262.769 802.711 1.00114.18 O ANISOU 705 OE1 GLN A 111 12790 9947 20644 -2064 592 -1136 O ATOM 706 NE2 GLN A 111 -24.073 262.436 804.894 1.00119.21 N ANISOU 706 NE2 GLN A 111 13172 11227 20896 -1968 755 -1604 N ATOM 707 N GLU A 112 -21.272 266.551 806.440 1.00 93.30 N ANISOU 707 N GLU A 112 9518 8525 17405 -2720 1555 -484 N ATOM 708 CA GLU A 112 -20.531 267.692 806.932 1.00 91.33 C ANISOU 708 CA GLU A 112 9096 8493 17113 -2914 1812 -244 C ATOM 709 C GLU A 112 -20.657 268.871 806.032 1.00 95.29 C ANISOU 709 C GLU A 112 9546 8673 17986 -3279 1840 81 C ATOM 710 O GLU A 112 -20.189 268.859 804.906 1.00 90.95 O ANISOU 710 O GLU A 112 9243 7917 17395 -3350 1877 421 O ATOM 711 CB GLU A 112 -19.064 267.357 807.038 1.00 86.39 C ANISOU 711 CB GLU A 112 8650 8199 15977 -2758 2087 0 C ATOM 712 CG GLU A 112 -18.207 268.557 807.214 1.00 99.29 C ANISOU 712 CG GLU A 112 10142 10017 17566 -2967 2384 291 C ATOM 713 CD GLU A 112 -16.895 268.394 806.524 1.00117.77 C ANISOU 713 CD GLU A 112 12769 12459 19519 -2917 2600 646 C ATOM 714 OE1 GLU A 112 -15.913 269.053 806.912 1.00118.43 O ANISOU 714 OE1 GLU A 112 12775 12838 19384 -2968 2890 811 O ATOM 715 OE2 GLU A 112 -16.844 267.596 805.579 1.00128.78 O ANISOU 715 OE2 GLU A 112 14458 13642 20830 -2819 2466 742 O ATOM 716 N VAL A 113 -21.249 269.918 806.578 1.00103.18 N ANISOU 716 N VAL A 113 10216 9646 19341 -3529 1819 -6 N ATOM 717 CA VAL A 113 -21.506 271.125 805.845 1.00117.92 C ANISOU 717 CA VAL A 113 11979 11197 21628 -3942 1831 294 C ATOM 718 C VAL A 113 -20.911 272.302 806.566 1.00126.27 C ANISOU 718 C VAL A 113 12702 12585 22691 -4174 2139 454 C ATOM 719 O VAL A 113 -21.097 272.463 807.757 1.00130.98 O ANISOU 719 O VAL A 113 13000 13466 23301 -4096 2140 157 O ATOM 720 CB VAL A 113 -22.989 271.370 805.780 1.00120.58 C ANISOU 720 CB VAL A 113 12168 11123 22524 -4083 1455 -8 C ATOM 721 CG1 VAL A 113 -23.380 271.766 804.393 1.00120.11 C ANISOU 721 CG1 VAL A 113 12293 10503 22841 -4345 1290 285 C ATOM 722 CG2 VAL A 113 -23.723 270.134 806.196 1.00117.11 C ANISOU 722 CG2 VAL A 113 11821 10697 21980 -3720 1191 -502 C ATOM 723 N GLU A 114 -20.201 273.152 805.861 1.00128.96 N ANISOU 723 N GLU A 114 13071 12902 23025 -4467 2401 923 N ATOM 724 CA GLU A 114 -19.760 274.329 806.535 1.00132.37 C ANISOU 724 CA GLU A 114 13113 13653 23527 -4715 2704 1041 C ATOM 725 C GLU A 114 -19.044 273.978 807.814 1.00127.85 C ANISOU 725 C GLU A 114 12392 13621 22563 -4384 2881 785 C ATOM 726 O GLU A 114 -19.401 274.451 808.878 1.00115.78 O ANISOU 726 O GLU A 114 10469 12292 21230 -4402 2854 518 O ATOM 727 CB GLU A 114 -20.967 275.182 806.876 1.00136.90 C ANISOU 727 CB GLU A 114 13300 13990 24726 -5022 2478 854 C ATOM 728 CG GLU A 114 -21.731 275.669 805.670 1.00151.14 C ANISOU 728 CG GLU A 114 15224 15202 27001 -5396 2264 1106 C ATOM 729 CD GLU A 114 -23.052 276.276 806.047 1.00157.26 C ANISOU 729 CD GLU A 114 15665 15680 28405 -5633 1931 814 C ATOM 730 OE1 GLU A 114 -23.206 276.679 807.218 1.00162.51 O ANISOU 730 OE1 GLU A 114 15920 16665 29160 -5621 1963 532 O ATOM 731 OE2 GLU A 114 -23.939 276.341 805.178 1.00151.73 O ANISOU 731 OE2 GLU A 114 15117 14411 28122 -5817 1604 848 O ATOM 732 N GLN A 115 -18.070 273.103 807.756 1.00124.21 N ANISOU 732 N GLN A 115 12248 13374 21573 -4065 3010 839 N ATOM 733 CA GLN A 115 -17.324 272.931 808.960 1.00120.78 C ANISOU 733 CA GLN A 115 11663 13414 20812 -3794 3177 637 C ATOM 734 C GLN A 115 -18.341 272.715 810.034 1.00112.83 C ANISOU 734 C GLN A 115 10398 12420 20053 -3678 2883 183 C ATOM 735 O GLN A 115 -18.369 273.425 811.009 1.00118.18 O ANISOU 735 O GLN A 115 10677 13348 20880 -3730 2947 32 O ATOM 736 CB GLN A 115 -16.545 274.191 809.284 1.00135.86 C ANISOU 736 CB GLN A 115 13234 15657 22730 -4018 3571 842 C ATOM 737 CG GLN A 115 -15.186 274.268 808.658 1.00144.29 C ANISOU 737 CG GLN A 115 14553 16926 23345 -4006 3933 1203 C ATOM 738 CD GLN A 115 -15.254 274.277 807.167 1.00154.57 C ANISOU 738 CD GLN A 115 16201 17856 24671 -4246 3910 1602 C ATOM 739 OE1 GLN A 115 -16.226 273.817 806.585 1.00157.23 O ANISOU 739 OE1 GLN A 115 16697 17763 25280 -4284 3568 1550 O ATOM 740 NE2 GLN A 115 -14.220 274.798 806.528 1.00158.90 N ANISOU 740 NE2 GLN A 115 16878 18569 24926 -4402 4262 1996 N ATOM 741 N GLN A 116 -19.231 271.770 809.826 1.00107.95 N ANISOU 741 N GLN A 116 9988 11532 19498 -3536 2548 -44 N ATOM 742 CA GLN A 116 -20.214 271.463 810.850 1.00 98.96 C ANISOU 742 CA GLN A 116 8651 10427 18522 -3413 2252 -494 C ATOM 743 C GLN A 116 -20.779 270.070 810.573 1.00 95.48 C ANISOU 743 C GLN A 116 8549 9815 17915 -3154 1991 -711 C ATOM 744 O GLN A 116 -21.187 269.780 809.451 1.00106.16 O ANISOU 744 O GLN A 116 10122 10810 19404 -3223 1882 -608 O ATOM 745 CB GLN A 116 -21.328 272.512 810.801 1.00102.98 C ANISOU 745 CB GLN A 116 8817 10677 19634 -3765 2072 -583 C ATOM 746 CG GLN A 116 -22.135 272.680 812.074 1.00100.83 C ANISOU 746 CG GLN A 116 8199 10548 19561 -3714 1821 -1014 C ATOM 747 CD GLN A 116 -23.189 273.775 811.948 1.00103.19 C ANISOU 747 CD GLN A 116 8156 10561 20492 -4094 1619 -1092 C ATOM 748 OE1 GLN A 116 -22.950 274.926 812.317 1.00 98.18 O ANISOU 748 OE1 GLN A 116 7118 10076 20111 -4343 1776 -981 O ATOM 749 NE2 GLN A 116 -24.354 273.423 811.412 1.00101.90 N ANISOU 749 NE2 GLN A 116 8139 9977 20601 -4144 1267 -1297 N ATOM 750 N LEU A 117 -20.784 269.196 811.577 1.00 84.14 N ANISOU 750 N LEU A 117 7147 8637 16184 -2860 1892 -1000 N ATOM 751 CA LEU A 117 -21.390 267.876 811.403 1.00 81.10 C ANISOU 751 CA LEU A 117 7026 8145 15644 -2645 1672 -1231 C ATOM 752 C LEU A 117 -22.906 267.970 811.476 1.00 92.40 C ANISOU 752 C LEU A 117 8312 9328 17466 -2747 1335 -1589 C ATOM 753 O LEU A 117 -23.463 268.434 812.470 1.00104.56 O ANISOU 753 O LEU A 117 9576 10995 19156 -2794 1186 -1849 O ATOM 754 CB LEU A 117 -20.875 266.862 812.428 1.00 72.40 C ANISOU 754 CB LEU A 117 6035 7401 14071 -2339 1684 -1380 C ATOM 755 CG LEU A 117 -19.729 265.939 811.991 1.00 73.69 C ANISOU 755 CG LEU A 117 6543 7663 13791 -2137 1862 -1147 C ATOM 756 CD1 LEU A 117 -19.572 264.782 812.962 1.00 72.93 C ANISOU 756 CD1 LEU A 117 6569 7832 13310 -1878 1782 -1342 C ATOM 757 CD2 LEU A 117 -19.944 265.409 810.582 1.00 79.52 C ANISOU 757 CD2 LEU A 117 7527 8084 14601 -2160 1822 -1018 C ATOM 758 N LEU A 118 -23.568 267.533 810.412 1.00 84.78 N ANISOU 758 N LEU A 118 7536 7999 16678 -2767 1183 -1625 N ATOM 759 CA LEU A 118 -25.018 267.609 810.338 1.00 86.60 C ANISOU 759 CA LEU A 118 7675 7936 17294 -2845 839 -2000 C ATOM 760 C LEU A 118 -25.657 266.266 810.624 1.00 88.45 C ANISOU 760 C LEU A 118 8094 8274 17240 -2520 667 -2384 C ATOM 761 O LEU A 118 -25.362 265.276 809.961 1.00 99.41 O ANISOU 761 O LEU A 118 9729 9630 18412 -2356 732 -2316 O ATOM 762 CB LEU A 118 -25.460 268.114 808.967 1.00 89.25 C ANISOU 762 CB LEU A 118 8086 7753 18071 -3058 739 -1829 C ATOM 763 CG LEU A 118 -25.150 269.587 808.724 1.00102.17 C ANISOU 763 CG LEU A 118 9505 9263 20052 -3426 864 -1486 C ATOM 764 CD1 LEU A 118 -25.751 270.047 807.406 1.00106.13 C ANISOU 764 CD1 LEU A 118 10107 9190 21027 -3662 687 -1333 C ATOM 765 CD2 LEU A 118 -25.674 270.419 809.887 1.00103.37 C ANISOU 765 CD2 LEU A 118 9270 9577 20430 -3566 755 -1740 C ATOM 766 N VAL A 119 -26.539 266.244 811.615 1.00 86.68 N ANISOU 766 N VAL A 119 7736 8191 17008 -2437 447 -2788 N ATOM 767 CA VAL A 119 -27.194 265.016 812.033 1.00 92.50 C ANISOU 767 CA VAL A 119 8631 9101 17414 -2147 308 -3167 C ATOM 768 C VAL A 119 -28.708 265.174 811.975 1.00103.73 C ANISOU 768 C VAL A 119 9988 10277 19147 -2150 -43 -3633 C ATOM 769 O VAL A 119 -29.251 266.162 812.474 1.00115.60 O ANISOU 769 O VAL A 119 11266 11702 20957 -2317 -229 -3771 O ATOM 770 CB VAL A 119 -26.799 264.660 813.472 1.00 91.20 C ANISOU 770 CB VAL A 119 8436 9414 16800 -1991 352 -3243 C ATOM 771 CG1 VAL A 119 -27.033 263.183 813.739 1.00 90.24 C ANISOU 771 CG1 VAL A 119 8551 9530 16207 -1716 342 -3453 C ATOM 772 CG2 VAL A 119 -25.345 265.025 813.715 1.00 90.88 C ANISOU 772 CG2 VAL A 119 8359 9569 16602 -2044 643 -2819 C ATOM 773 N ASN A 120 -29.410 264.185 811.448 1.00 91.65 N ANISOU 773 N ASN A 120 8636 8656 17530 -1950 -147 -3916 N ATOM 774 CA ASN A 120 -30.858 264.241 811.449 1.00100.78 C ANISOU 774 CA ASN A 120 9755 9613 18925 -1900 -486 -4427 C ATOM 775 C ASN A 120 -31.407 262.940 811.927 1.00 89.18 C ANISOU 775 C ASN A 120 8434 8471 16980 -1589 -512 -4811 C ATOM 776 O ASN A 120 -30.746 261.941 811.836 1.00 82.92 O ANISOU 776 O ASN A 120 7784 7922 15801 -1438 -279 -4656 O ATOM 777 CB ASN A 120 -31.377 264.529 810.062 1.00116.85 C ANISOU 777 CB ASN A 120 11835 11085 21476 -1988 -634 -4442 C ATOM 778 CG ASN A 120 -30.504 265.476 809.328 1.00124.27 C ANISOU 778 CG ASN A 120 12724 11747 22745 -2284 -490 -3908 C ATOM 779 OD1 ASN A 120 -29.333 265.607 809.642 1.00136.15 O ANISOU 779 OD1 ASN A 120 14210 13520 24000 -2351 -200 -3511 O ATOM 780 ND2 ASN A 120 -31.055 266.145 808.341 1.00116.86 N ANISOU 780 ND2 ASN A 120 11778 10266 22358 -2465 -695 -3890 N ATOM 781 N VAL A 121 -32.610 262.956 812.466 1.00 91.60 N ANISOU 781 N VAL A 121 8704 8802 17296 -1507 -796 -5312 N ATOM 782 CA VAL A 121 -33.228 261.728 812.906 1.00102.89 C ANISOU 782 CA VAL A 121 10281 10575 18238 -1222 -805 -5701 C ATOM 783 C VAL A 121 -34.719 261.838 812.929 1.00109.49 C ANISOU 783 C VAL A 121 11103 11253 19245 -1131 -1153 -6303 C ATOM 784 O VAL A 121 -35.256 262.918 812.954 1.00107.45 O ANISOU 784 O VAL A 121 10709 10683 19435 -1303 -1429 -6424 O ATOM 785 CB VAL A 121 -32.828 261.383 814.298 1.00104.75 C ANISOU 785 CB VAL A 121 10548 11330 17923 -1164 -724 -5646 C ATOM 786 CG1 VAL A 121 -33.803 260.396 814.863 1.00112.43 C ANISOU 786 CG1 VAL A 121 11654 12623 18441 -930 -822 -6125 C ATOM 787 CG2 VAL A 121 -31.461 260.832 814.295 1.00 91.25 C ANISOU 787 CG2 VAL A 121 8921 9838 15911 -1158 -381 -5163 C ATOM 788 N ILE A 122 -35.392 260.707 812.934 1.00112.78 N ANISOU 788 N ILE A 122 11653 11901 19297 -862 -1138 -6696 N ATOM 789 CA ILE A 122 -36.816 260.719 813.055 1.00113.02 C ANISOU 789 CA ILE A 122 11697 11851 19394 -730 -1461 -7327 C ATOM 790 C ILE A 122 -37.116 259.888 814.236 1.00110.92 C ANISOU 790 C ILE A 122 11544 12175 18426 -561 -1412 -7564 C ATOM 791 O ILE A 122 -36.889 258.700 814.227 1.00111.97 O ANISOU 791 O ILE A 122 11791 12663 18089 -390 -1142 -7553 O ATOM 792 CB ILE A 122 -37.419 260.057 811.883 1.00110.01 C ANISOU 792 CB ILE A 122 11376 11227 19198 -525 -1471 -7634 C ATOM 793 CG1 ILE A 122 -37.015 260.833 810.640 1.00116.01 C ANISOU 793 CG1 ILE A 122 12068 11370 20639 -704 -1526 -7315 C ATOM 794 CD1 ILE A 122 -35.729 261.586 810.839 1.00123.09 C ANISOU 794 CD1 ILE A 122 12891 12259 21619 -997 -1341 -6652 C ATOM 795 CG2 ILE A 122 -38.897 260.024 812.049 1.00100.31 C ANISOU 795 CG2 ILE A 122 10176 9944 17995 -351 -1802 -8344 C ATOM 796 N LEU A 123 -37.656 260.502 815.265 1.00116.65 N ANISOU 796 N LEU A 123 12238 13010 19073 -619 -1690 -7779 N ATOM 797 CA LEU A 123 -37.979 259.799 816.503 1.00127.58 C ANISOU 797 CA LEU A 123 13768 14955 19754 -477 -1700 -7984 C ATOM 798 C LEU A 123 -39.245 258.947 816.483 1.00126.89 C ANISOU 798 C LEU A 123 13824 15069 19321 -214 -1795 -8623 C ATOM 799 O LEU A 123 -40.093 259.107 815.634 1.00127.96 O ANISOU 799 O LEU A 123 13923 14855 19840 -125 -1969 -9030 O ATOM 800 CB LEU A 123 -38.000 260.782 817.674 1.00140.68 C ANISOU 800 CB LEU A 123 15340 16676 21438 -626 -1990 -7946 C ATOM 801 CG LEU A 123 -36.775 261.548 818.189 1.00147.20 C ANISOU 801 CG LEU A 123 16017 17503 22409 -837 -1900 -7380 C ATOM 802 CD1 LEU A 123 -37.048 262.595 819.288 1.00155.25 C ANISOU 802 CD1 LEU A 123 16888 18545 23553 -951 -2269 -7475 C ATOM 803 CD2 LEU A 123 -35.679 260.572 818.555 1.00142.17 C ANISOU 803 CD2 LEU A 123 15527 17263 21229 -767 -1526 -6962 C ATOM 804 N LYS A 124 -39.358 258.047 817.444 1.00121.72 N ANISOU 804 N LYS A 124 13341 14983 17925 -90 -1684 -8705 N ATOM 805 CA LYS A 124 -40.520 257.189 817.584 1.00111.18 C ANISOU 805 CA LYS A 124 12155 13958 16129 156 -1725 -9300 C ATOM 806 C LYS A 124 -41.717 258.082 817.867 1.00114.01 C ANISOU 806 C LYS A 124 12500 14082 16737 175 -2226 -9848 C ATOM 807 O LYS A 124 -42.860 257.704 817.665 1.00108.87 O ANISOU 807 O LYS A 124 11934 13486 15948 387 -2361 -10462 O ATOM 808 CB LYS A 124 -40.315 256.177 818.701 1.00 97.24 C ANISOU 808 CB LYS A 124 10596 12861 13491 213 -1521 -9183 C ATOM 809 N ASP A 125 -41.437 259.270 818.373 1.00115.77 N ANISOU 809 N ASP A 125 12602 14062 17325 -43 -2508 -9636 N ATOM 810 CA ASP A 125 -42.448 260.280 818.554 1.00133.89 C ANISOU 810 CA ASP A 125 14827 16041 20004 -85 -3017 -10090 C ATOM 811 C ASP A 125 -42.945 260.558 817.186 1.00127.68 C ANISOU 811 C ASP A 125 13943 14698 19871 -55 -3096 -10349 C ATOM 812 O ASP A 125 -44.126 260.734 816.972 1.00114.01 O ANISOU 812 O ASP A 125 12252 12768 18297 69 -3433 -10962 O ATOM 813 CB ASP A 125 -41.818 261.585 818.983 1.00151.44 C ANISOU 813 CB ASP A 125 16830 18000 22712 -376 -3219 -9704 C ATOM 814 CG ASP A 125 -41.598 261.660 820.434 1.00169.61 C ANISOU 814 CG ASP A 125 19190 20724 24529 -398 -3351 -9582 C ATOM 815 OD1 ASP A 125 -42.514 261.247 821.164 1.00178.85 O ANISOU 815 OD1 ASP A 125 20556 22205 25195 -233 -3582 -10033 O ATOM 816 OD2 ASP A 125 -40.527 262.150 820.847 1.00171.41 O ANISOU 816 OD2 ASP A 125 19278 20970 24881 -568 -3245 -9055 O ATOM 817 N GLY A 126 -42.010 260.582 816.251 1.00132.15 N ANISOU 817 N GLY A 126 14402 14999 20809 -162 -2802 -9875 N ATOM 818 CA GLY A 126 -42.268 261.020 814.902 1.00134.84 C ANISOU 818 CA GLY A 126 14645 14717 21871 -192 -2904 -9970 C ATOM 819 C GLY A 126 -41.697 262.400 814.678 1.00135.54 C ANISOU 819 C GLY A 126 14526 14318 22655 -548 -3056 -9543 C ATOM 820 O GLY A 126 -41.814 262.972 813.607 1.00137.45 O ANISOU 820 O GLY A 126 14686 13982 23555 -656 -3176 -9511 O ATOM 821 N SER A 127 -41.052 262.935 815.696 1.00132.04 N ANISOU 821 N SER A 127 13990 14116 22064 -735 -3045 -9197 N ATOM 822 CA SER A 127 -40.365 264.215 815.558 1.00126.86 C ANISOU 822 CA SER A 127 13092 13101 22010 -1085 -3102 -8742 C ATOM 823 CB SER A 127 -39.905 264.711 816.934 1.00119.50 C ANISOU 823 CB SER A 127 12046 12532 20829 -1202 -3164 -8542 C ATOM 824 OG SER A 127 -39.778 263.630 817.846 1.00114.86 O ANISOU 824 OG SER A 127 11666 12543 19432 -966 -3005 -8596 O ATOM 825 C SER A 127 -39.187 264.141 814.585 1.00126.73 C ANISOU 825 C SER A 127 13040 12906 22205 -1199 -2705 -8145 C ATOM 826 O SER A 127 -38.783 263.054 814.175 1.00132.95 O ANISOU 826 O SER A 127 13980 13905 22628 -1005 -2385 -8045 O ATOM 827 N PHE A 128 -38.650 265.301 814.213 1.00124.49 N ANISOU 827 N PHE A 128 12549 12249 22504 -1524 -2731 -7754 N ATOM 828 CA PHE A 128 -37.501 265.380 813.309 1.00121.36 C ANISOU 828 CA PHE A 128 12130 11676 22303 -1665 -2379 -7160 C ATOM 829 C PHE A 128 -36.383 266.226 813.922 1.00116.60 C ANISOU 829 C PHE A 128 11320 11233 21750 -1929 -2198 -6630 C ATOM 830 O PHE A 128 -36.564 267.419 814.161 1.00132.01 O ANISOU 830 O PHE A 128 13031 12969 24159 -2199 -2410 -6597 O ATOM 831 CB PHE A 128 -37.925 265.959 811.957 1.00120.18 C ANISOU 831 CB PHE A 128 11962 10846 22854 -1814 -2555 -7169 C ATOM 832 CG PHE A 128 -36.823 265.987 810.929 1.00116.93 C ANISOU 832 CG PHE A 128 11581 10233 22613 -1943 -2231 -6575 C ATOM 833 CD1 PHE A 128 -36.451 264.830 810.260 1.00116.14 C ANISOU 833 CD1 PHE A 128 11678 10240 22212 -1690 -1983 -6510 C ATOM 834 CE1 PHE A 128 -35.443 264.853 809.310 1.00114.84 C ANISOU 834 CE1 PHE A 128 11562 9883 22188 -1800 -1730 -5974 C ATOM 835 CZ PHE A 128 -34.800 266.042 809.014 1.00113.18 C ANISOU 835 CZ PHE A 128 11223 9395 22386 -2173 -1688 -5487 C ATOM 836 CE2 PHE A 128 -35.163 267.201 809.672 1.00113.33 C ANISOU 836 CE2 PHE A 128 11018 9329 22715 -2444 -1891 -5539 C ATOM 837 CD2 PHE A 128 -36.170 267.170 810.621 1.00118.05 C ANISOU 837 CD2 PHE A 128 11550 10095 23211 -2325 -2179 -6087 C ATOM 838 N LEU A 129 -35.228 265.611 814.104 1.00107.67 N ANISOU 838 N LEU A 129 10267 10456 20185 -1851 -1807 -6226 N ATOM 839 CA LEU A 129 -34.124 266.227 814.809 1.00113.84 C ANISOU 839 CA LEU A 129 10876 11476 20901 -2014 -1613 -5786 C ATOM 840 C LEU A 129 -32.911 266.587 813.970 1.00112.01 C ANISOU 840 C LEU A 129 10604 11089 20866 -2198 -1268 -5201 C ATOM 841 O LEU A 129 -32.486 265.825 813.121 1.00 98.84 O ANISOU 841 O LEU A 129 9133 9363 19060 -2093 -1054 -5031 O ATOM 842 CB LEU A 129 -33.704 265.313 815.943 1.00109.65 C ANISOU 842 CB LEU A 129 10475 11513 19672 -1776 -1484 -5797 C ATOM 843 CG LEU A 129 -32.453 265.807 816.614 1.00105.31 C ANISOU 843 CG LEU A 129 9778 11205 19032 -1880 -1268 -5350 C ATOM 844 CD2 LEU A 129 -32.470 265.396 818.052 1.00 97.45 C ANISOU 844 CD2 LEU A 129 8829 10663 17535 -1704 -1380 -5497 C ATOM 845 CD1 LEU A 129 -32.417 267.294 816.461 1.00116.27 C ANISOU 845 CD1 LEU A 129 10832 12303 21043 -2195 -1370 -5216 C ATOM 846 N THR A 130 -32.374 267.773 814.214 1.00116.90 N ANISOU 846 N THR A 130 10952 11656 21809 -2475 -1225 -4910 N ATOM 847 CA THR A 130 -31.200 268.264 813.526 1.00113.18 C ANISOU 847 CA THR A 130 10424 11089 21489 -2677 -886 -4352 C ATOM 848 CB THR A 130 -31.518 269.542 812.788 1.00103.34 C ANISOU 848 CB THR A 130 8967 9370 20927 -3054 -1005 -4217 C ATOM 849 OG1 THR A 130 -32.873 269.496 812.350 1.00105.15 O ANISOU 849 OG1 THR A 130 9263 9209 21480 -3040 -1397 -4654 O ATOM 850 CG2 THR A 130 -30.616 269.705 811.596 1.00100.29 C ANISOU 850 CG2 THR A 130 8683 8757 20665 -3219 -703 -3698 C ATOM 851 C THR A 130 -30.112 268.572 814.536 1.00116.49 C ANISOU 851 C THR A 130 10679 11940 21641 -2682 -656 -4083 C ATOM 852 O THR A 130 -30.385 269.162 815.562 1.00118.34 O ANISOU 852 O THR A 130 10676 12344 21944 -2719 -834 -4258 O ATOM 853 N LEU A 131 -28.882 268.161 814.254 1.00114.37 N ANISOU 853 N LEU A 131 10539 11841 21074 -2623 -289 -3684 N ATOM 854 CA LEU A 131 -27.764 268.417 815.147 1.00106.88 C ANISOU 854 CA LEU A 131 9457 11280 19874 -2591 -63 -3440 C ATOM 855 CB LEU A 131 -27.208 267.114 815.663 1.00 95.94 C ANISOU 855 CB LEU A 131 8350 10239 17863 -2272 55 -3442 C ATOM 856 CG LEU A 131 -28.173 266.486 816.631 1.00 90.02 C ANISOU 856 CG LEU A 131 7672 9674 16857 -2069 -250 -3883 C ATOM 857 CD1 LEU A 131 -27.403 265.747 817.666 1.00 68.89 C ANISOU 857 CD1 LEU A 131 5124 7411 13641 -1845 -154 -3801 C ATOM 858 CD2 LEU A 131 -28.924 267.603 817.241 1.00 70.01 C ANISOU 858 CD2 LEU A 131 4818 7066 14715 -2223 -542 -4116 C ATOM 859 C LEU A 131 -26.651 269.187 814.479 1.00104.21 C ANISOU 859 C LEU A 131 9009 10875 19710 -2816 278 -2954 C ATOM 860 O LEU A 131 -26.210 268.841 813.402 1.00 99.09 O ANISOU 860 O LEU A 131 8577 10045 19026 -2847 461 -2693 O ATOM 861 N GLN A 132 -26.177 270.232 815.129 1.00107.65 N ANISOU 861 N GLN A 132 9102 11482 20318 -2965 366 -2835 N ATOM 862 CA GLN A 132 -25.098 271.030 814.557 1.00103.92 C ANISOU 862 CA GLN A 132 8501 11014 19969 -3188 733 -2382 C ATOM 863 CB GLN A 132 -25.575 272.461 814.297 1.00102.93 C ANISOU 863 CB GLN A 132 7992 10660 20459 -3591 675 -2320 C ATOM 864 CG GLN A 132 -26.632 272.577 813.213 1.00121.29 C ANISOU 864 CG GLN A 132 10434 12453 23196 -3804 437 -2381 C ATOM 865 CD GLN A 132 -27.132 273.996 813.033 1.00147.24 C ANISOU 865 CD GLN A 132 13333 15492 27120 -4241 343 -2314 C ATOM 866 OE1 GLN A 132 -27.067 274.805 813.958 1.00160.36 O ANISOU 866 OE1 GLN A 132 14584 17398 28948 -4338 335 -2393 O ATOM 867 NE2 GLN A 132 -27.631 274.301 811.839 1.00155.30 N ANISOU 867 NE2 GLN A 132 14470 16012 28525 -4511 253 -2164 N ATOM 868 C GLN A 132 -23.866 271.043 815.469 1.00 99.14 C ANISOU 868 C GLN A 132 7798 10862 19010 -3015 990 -2241 C ATOM 869 O GLN A 132 -23.827 271.767 816.462 1.00 87.32 O ANISOU 869 O GLN A 132 5947 9586 17646 -3030 934 -2359 O ATOM 870 N LEU A 133 -22.868 270.231 815.132 1.00102.18 N ANISOU 870 N LEU A 133 8492 11368 18964 -2836 1241 -2011 N ATOM 871 CA LEU A 133 -21.640 270.155 815.921 1.00 94.40 C ANISOU 871 CA LEU A 133 7470 10768 17631 -2642 1466 -1891 C ATOM 872 CB LEU A 133 -21.372 268.717 816.361 1.00 83.21 C ANISOU 872 CB LEU A 133 6422 9502 15691 -2296 1392 -1992 C ATOM 873 CG LEU A 133 -22.570 267.877 816.802 1.00 81.56 C ANISOU 873 CG LEU A 133 6353 9240 15396 -2156 1032 -2358 C ATOM 874 CD1 LEU A 133 -22.116 266.488 817.219 1.00 66.56 C ANISOU 874 CD1 LEU A 133 4803 7532 12956 -1863 1034 -2373 C ATOM 875 CD2 LEU A 133 -23.319 268.555 817.931 1.00 89.95 C ANISOU 875 CD2 LEU A 133 7097 10410 16669 -2164 748 -2662 C ATOM 876 C LEU A 133 -20.449 270.661 815.122 1.00 91.45 C ANISOU 876 C LEU A 133 7144 10417 17185 -2748 1872 -1474 C ATOM 877 O LEU A 133 -19.970 269.977 814.227 1.00 98.79 O ANISOU 877 O LEU A 133 8449 11228 17858 -2677 1999 -1265 O ATOM 878 N PRO A 134 -19.959 271.861 815.456 1.00 85.68 N ANISOU 878 N PRO A 134 6035 9860 16659 -2901 2071 -1366 N ATOM 879 CA PRO A 134 -18.856 272.464 814.702 1.00 83.65 C ANISOU 879 CA PRO A 134 5813 9663 16307 -3025 2479 -977 C ATOM 880 C PRO A 134 -17.675 271.522 814.671 1.00 84.75 C ANISOU 880 C PRO A 134 6340 9975 15887 -2713 2648 -856 C ATOM 881 O PRO A 134 -17.491 270.764 815.618 1.00 87.18 O ANISOU 881 O PRO A 134 6721 10468 15937 -2418 2511 -1068 O ATOM 882 CB PRO A 134 -18.492 273.698 815.534 1.00 87.77 C ANISOU 882 CB PRO A 134 5799 10490 17060 -3131 2645 -1009 C ATOM 883 CG PRO A 134 -19.697 273.977 816.370 1.00 92.09 C ANISOU 883 CG PRO A 134 6001 10989 18000 -3192 2269 -1366 C ATOM 884 CD PRO A 134 -20.307 272.643 816.654 1.00 92.10 C ANISOU 884 CD PRO A 134 6357 10889 17749 -2928 1930 -1618 C ATOM 885 N LEU A 135 -16.858 271.600 813.645 1.00 94.30 N ANISOU 885 N LEU A 135 7787 11128 16915 -2789 2920 -516 N ATOM 886 CA LEU A 135 -15.722 270.735 813.599 1.00 95.90 C ANISOU 886 CA LEU A 135 8352 11476 16608 -2506 3043 -419 C ATOM 887 C LEU A 135 -14.951 271.102 814.804 1.00 91.68 C ANISOU 887 C LEU A 135 7561 11323 15952 -2324 3163 -554 C ATOM 888 O LEU A 135 -14.384 270.274 815.481 1.00 83.74 O ANISOU 888 O LEU A 135 6737 10463 14618 -2017 3087 -675 O ATOM 889 CB LEU A 135 -14.866 271.047 812.395 1.00103.19 C ANISOU 889 CB LEU A 135 9490 12342 17373 -2648 3337 -31 C ATOM 890 CG LEU A 135 -15.354 270.510 811.064 1.00100.67 C ANISOU 890 CG LEU A 135 9514 11639 17098 -2760 3210 150 C ATOM 891 CD1 LEU A 135 -14.178 270.231 810.176 1.00 99.67 C ANISOU 891 CD1 LEU A 135 9742 11542 16586 -2708 3420 465 C ATOM 892 CD2 LEU A 135 -16.148 269.260 811.295 1.00 89.31 C ANISOU 892 CD2 LEU A 135 8264 10048 15623 -2543 2869 -126 C ATOM 893 N SER A 136 -14.946 272.379 815.081 1.00 99.47 N ANISOU 893 N SER A 136 8091 12466 17238 -2524 3341 -535 N ATOM 894 CA SER A 136 -14.124 272.896 816.128 1.00105.98 C ANISOU 894 CA SER A 136 8602 13676 17988 -2349 3502 -657 C ATOM 895 C SER A 136 -14.506 272.245 817.413 1.00104.54 C ANISOU 895 C SER A 136 8354 13582 17784 -2058 3161 -1006 C ATOM 896 O SER A 136 -13.659 271.965 818.234 1.00114.90 O ANISOU 896 O SER A 136 9674 15135 18848 -1755 3186 -1113 O ATOM 897 CB SER A 136 -14.372 274.380 816.242 1.00114.89 C ANISOU 897 CB SER A 136 9159 14941 19552 -2653 3696 -627 C ATOM 898 OG SER A 136 -14.808 274.874 814.997 1.00123.77 O ANISOU 898 OG SER A 136 10346 15802 20880 -3046 3811 -331 O ATOM 899 N PHE A 137 -15.783 272.025 817.629 1.00 93.24 N ANISOU 899 N PHE A 137 6851 11962 16615 -2144 2823 -1193 N ATOM 900 CA PHE A 137 -16.118 271.488 818.915 1.00 87.23 C ANISOU 900 CA PHE A 137 6003 11332 15810 -1882 2499 -1506 C ATOM 901 CB PHE A 137 -17.592 271.398 819.125 1.00 86.62 C ANISOU 901 CB PHE A 137 5830 11062 16019 -2004 2122 -1734 C ATOM 902 CG PHE A 137 -17.930 270.810 820.423 1.00 91.62 C ANISOU 902 CG PHE A 137 6493 11810 16507 -1710 1757 -2031 C ATOM 903 CD1 PHE A 137 -17.312 271.250 821.544 1.00 93.53 C ANISOU 903 CD1 PHE A 137 6467 12322 16748 -1494 1731 -2151 C ATOM 904 CE1 PHE A 137 -17.605 270.722 822.746 1.00 97.56 C ANISOU 904 CE1 PHE A 137 7035 12914 17120 -1226 1358 -2392 C ATOM 905 CZ PHE A 137 -18.513 269.739 822.848 1.00 94.08 C ANISOU 905 CZ PHE A 137 6925 12326 16494 -1187 1046 -2510 C ATOM 906 CE2 PHE A 137 -19.128 269.280 821.745 1.00 89.22 C ANISOU 906 CE2 PHE A 137 6553 11479 15869 -1387 1104 -2424 C ATOM 907 CD2 PHE A 137 -18.834 269.809 820.535 1.00 91.34 C ANISOU 907 CD2 PHE A 137 6764 11625 16317 -1636 1438 -2188 C ATOM 908 C PHE A 137 -15.559 270.131 819.190 1.00 85.02 C ANISOU 908 C PHE A 137 6177 11074 15052 -1565 2400 -1517 C ATOM 909 O PHE A 137 -15.097 269.874 820.279 1.00 94.37 O ANISOU 909 O PHE A 137 7336 12448 16074 -1279 2276 -1669 O ATOM 910 N LEU A 138 -15.640 269.231 818.235 1.00 78.38 N ANISOU 910 N LEU A 138 5785 10006 13990 -1600 2404 -1368 N ATOM 911 CA LEU A 138 -15.156 267.897 818.511 1.00 91.06 C ANISOU 911 CA LEU A 138 7797 11633 15170 -1335 2297 -1375 C ATOM 912 CB LEU A 138 -15.711 266.874 817.538 1.00 85.58 C ANISOU 912 CB LEU A 138 7490 10675 14350 -1404 2209 -1299 C ATOM 913 CG LEU A 138 -16.314 267.393 816.261 1.00 81.23 C ANISOU 913 CG LEU A 138 6929 9862 14072 -1680 2298 -1166 C ATOM 914 CD1 LEU A 138 -15.264 267.299 815.213 1.00 96.26 C ANISOU 914 CD1 LEU A 138 9118 11700 15755 -1687 2551 -858 C ATOM 915 CD2 LEU A 138 -17.480 266.541 815.908 1.00 59.09 C ANISOU 915 CD2 LEU A 138 4280 6851 11321 -1712 2053 -1310 C ATOM 916 C LEU A 138 -13.666 267.788 818.692 1.00 97.71 C ANISOU 916 C LEU A 138 8785 12644 15695 -1124 2503 -1252 C ATOM 917 O LEU A 138 -13.185 267.000 819.480 1.00 92.42 O ANISOU 917 O LEU A 138 8274 12074 14768 -866 2370 -1332 O ATOM 918 N PHE A 139 -12.932 268.515 817.885 1.00102.64 N ANISOU 918 N PHE A 139 9392 13285 16320 -1241 2822 -1042 N ATOM 919 CA PHE A 139 -11.490 268.552 818.020 1.00100.53 C ANISOU 919 CA PHE A 139 9231 13207 15757 -1044 3039 -957 C ATOM 920 CB PHE A 139 -10.884 268.906 816.689 1.00 98.87 C ANISOU 920 CB PHE A 139 9200 12927 15439 -1221 3345 -662 C ATOM 921 CG PHE A 139 -11.243 267.924 815.649 1.00 93.64 C ANISOU 921 CG PHE A 139 8964 11966 14649 -1297 3218 -511 C ATOM 922 CD1 PHE A 139 -10.581 266.726 815.574 1.00 90.43 C ANISOU 922 CD1 PHE A 139 8967 11508 13884 -1093 3111 -478 C ATOM 923 CE1 PHE A 139 -10.927 265.796 814.654 1.00 86.12 C ANISOU 923 CE1 PHE A 139 8756 10713 13253 -1144 2983 -370 C ATOM 924 CZ PHE A 139 -11.955 266.037 813.808 1.00 89.73 C ANISOU 924 CZ PHE A 139 9160 10956 13978 -1366 2948 -311 C ATOM 925 CE2 PHE A 139 -12.640 267.211 813.885 1.00 92.67 C ANISOU 925 CE2 PHE A 139 9159 11342 14709 -1577 3032 -338 C ATOM 926 CD2 PHE A 139 -12.298 268.144 814.816 1.00 88.85 C ANISOU 926 CD2 PHE A 139 8321 11121 14317 -1556 3165 -435 C ATOM 927 C PHE A 139 -10.893 269.290 819.212 1.00 94.42 C ANISOU 927 C PHE A 139 8071 12746 15059 -839 3103 -1147 C ATOM 928 O PHE A 139 -9.937 268.841 819.816 1.00 92.68 O ANISOU 928 O PHE A 139 7988 12650 14577 -542 3087 -1215 O ATOM 929 N SER A 140 -11.471 270.425 819.548 1.00 90.00 N ANISOU 929 N SER A 140 7006 12300 14889 -990 3154 -1249 N ATOM 930 CA SER A 140 -10.999 271.198 820.691 1.00 89.11 C ANISOU 930 CA SER A 140 6440 12497 14921 -783 3195 -1465 C ATOM 931 CB SER A 140 -11.751 272.520 820.797 1.00 89.61 C ANISOU 931 CB SER A 140 5913 12658 15478 -1048 3273 -1533 C ATOM 932 OG SER A 140 -12.993 272.340 821.458 1.00 89.15 O ANISOU 932 OG SER A 140 5716 12475 15682 -1077 2856 -1741 O ATOM 933 C SER A 140 -11.201 270.392 821.969 1.00 91.10 C ANISOU 933 C SER A 140 6783 12738 15091 -455 2766 -1715 C ATOM 934 O SER A 140 -11.819 269.328 821.948 1.00 80.82 O ANISOU 934 O SER A 140 5841 11225 13641 -451 2482 -1709 O ATOM 935 N SER A 141 -10.673 270.894 823.066 1.00 99.06 N ANISOU 935 N SER A 141 7493 13966 16180 -180 2708 -1928 N ATOM 936 CA SER A 141 -10.719 270.184 824.317 1.00 98.87 C ANISOU 936 CA SER A 141 7608 13907 16053 152 2272 -2134 C ATOM 937 CB SER A 141 -9.466 270.485 825.106 1.00 94.71 C ANISOU 937 CB SER A 141 6955 13585 15443 530 2338 -2279 C ATOM 938 OG SER A 141 -9.511 271.809 825.579 1.00 94.32 O ANISOU 938 OG SER A 141 6269 13789 15781 537 2459 -2457 O ATOM 939 C SER A 141 -11.888 270.625 825.136 1.00112.09 C ANISOU 939 C SER A 141 8935 15580 18073 101 1928 -2344 C ATOM 940 O SER A 141 -12.056 270.186 826.254 1.00116.34 O ANISOU 940 O SER A 141 9542 16101 18563 357 1526 -2518 O ATOM 941 N ALA A 142 -12.707 271.504 824.596 1.00115.45 N ANISOU 941 N ALA A 142 9001 16010 18855 -235 2053 -2326 N ATOM 942 CA ALA A 142 -13.722 272.101 825.419 1.00118.28 C ANISOU 942 CA ALA A 142 8956 16395 19589 -274 1723 -2563 C ATOM 943 CB ALA A 142 -14.536 273.024 824.608 1.00128.00 C ANISOU 943 CB ALA A 142 9842 17582 21211 -698 1897 -2498 C ATOM 944 C ALA A 142 -14.609 271.067 826.028 1.00109.42 C ANISOU 944 C ALA A 142 8185 15094 18295 -177 1228 -2672 C ATOM 945 O ALA A 142 -15.114 270.211 825.349 1.00 92.39 O ANISOU 945 O ALA A 142 6431 12743 15928 -320 1199 -2550 O ATOM 946 N ASN A 143 -14.814 271.202 827.329 1.00117.01 N ANISOU 946 N ASN A 143 8963 16140 19357 70 836 -2912 N ATOM 947 CA ASN A 143 -15.632 270.309 828.140 1.00118.56 C ANISOU 947 CA ASN A 143 9469 16217 19361 193 323 -3030 C ATOM 948 CB ASN A 143 -15.456 270.580 829.625 1.00121.79 C ANISOU 948 CB ASN A 143 9663 16743 19867 534 -79 -3260 C ATOM 949 CG ASN A 143 -14.725 269.470 830.320 1.00123.70 C ANISOU 949 CG ASN A 143 10399 16923 19679 866 -294 -3196 C ATOM 950 OD1 ASN A 143 -14.374 268.473 829.704 1.00122.62 O ANISOU 950 OD1 ASN A 143 10749 16670 19172 822 -138 -2987 O ATOM 951 ND2 ASN A 143 -14.500 269.626 831.611 1.00120.10 N ANISOU 951 ND2 ASN A 143 9820 16524 19290 1193 -684 -3373 N ATOM 952 C ASN A 143 -17.093 270.280 827.791 1.00115.26 C ANISOU 952 C ASN A 143 9050 15664 19078 -94 130 -3105 C ATOM 953 O ASN A 143 -17.750 269.275 827.954 1.00116.97 O ANISOU 953 O ASN A 143 9675 15768 18999 -74 -137 -3121 O ATOM 954 N THR A 144 -17.631 271.413 827.406 1.00119.38 N ANISOU 954 N THR A 144 9090 16209 20061 -354 236 -3179 N ATOM 955 CA THR A 144 -18.997 271.425 826.967 1.00129.68 C ANISOU 955 CA THR A 144 10403 17344 21525 -633 54 -3268 C ATOM 956 CB THR A 144 -19.867 271.542 828.152 1.00144.92 C ANISOU 956 CB THR A 144 12191 19312 23560 -507 -486 -3562 C ATOM 957 OG1 THR A 144 -19.741 272.870 828.663 1.00150.15 O ANISOU 957 OG1 THR A 144 12203 20127 24720 -523 -510 -3707 O ATOM 958 CG2 THR A 144 -19.389 270.558 829.196 1.00144.75 C ANISOU 958 CG2 THR A 144 12551 19355 23091 -132 -766 -3575 C ATOM 959 C THR A 144 -19.216 272.624 826.094 1.00130.44 C ANISOU 959 C THR A 144 10045 17411 22106 -990 347 -3212 C ATOM 960 O THR A 144 -18.586 273.645 826.294 1.00140.63 O ANISOU 960 O THR A 144 10861 18885 23687 -997 551 -3210 O ATOM 961 N LEU A 145 -20.118 272.533 825.138 1.00116.41 N ANISOU 961 N LEU A 145 8390 15404 20435 -1293 366 -3171 N ATOM 962 CA LEU A 145 -20.350 273.706 824.332 1.00127.72 C ANISOU 962 CA LEU A 145 9399 16769 22358 -1667 608 -3088 C ATOM 963 CB LEU A 145 -19.660 273.650 822.975 1.00131.85 C ANISOU 963 CB LEU A 145 10120 17200 22779 -1862 1105 -2734 C ATOM 964 CG LEU A 145 -18.362 274.468 822.865 1.00129.87 C ANISOU 964 CG LEU A 145 9559 17205 22581 -1862 1568 -2540 C ATOM 965 CD2 LEU A 145 -17.254 273.876 823.684 1.00131.40 C ANISOU 965 CD2 LEU A 145 9926 17626 22375 -1432 1591 -2574 C ATOM 966 CD1 LEU A 145 -18.587 275.900 823.266 1.00115.80 C ANISOU 966 CD1 LEU A 145 7078 15573 21347 -2059 1593 -2650 C ATOM 967 C LEU A 145 -21.786 274.144 824.234 1.00127.30 C ANISOU 967 C LEU A 145 9162 16510 22695 -1928 273 -3298 C ATOM 968 O LEU A 145 -22.681 273.374 823.947 1.00120.47 O ANISOU 968 O LEU A 145 8660 15437 21676 -1949 38 -3398 O ATOM 969 N ASN A 146 -21.981 275.410 824.560 1.00127.58 N ANISOU 969 N ASN A 146 8594 16630 23250 -2109 238 -3397 N ATOM 970 CA ASN A 146 -23.268 276.059 824.664 1.00131.96 C ANISOU 970 CA ASN A 146 8851 17016 24273 -2359 -128 -3638 C ATOM 971 CB ASN A 146 -23.186 277.127 825.734 1.00137.40 C ANISOU 971 CB ASN A 146 8891 17947 25367 -2318 -300 -3836 C ATOM 972 CG ASN A 146 -22.398 276.674 826.911 1.00122.98 C ANISOU 972 CG ASN A 146 7122 16404 23203 -1852 -417 -3934 C ATOM 973 OD1 ASN A 146 -22.918 276.030 827.795 1.00 92.58 O ANISOU 973 OD1 ASN A 146 3500 12550 19127 -1595 -887 -4165 O ATOM 974 ND2 ASN A 146 -21.129 277.001 826.928 1.00113.07 N ANISOU 974 ND2 ASN A 146 5679 15387 21893 -1735 0 -3758 N ATOM 975 C ASN A 146 -23.765 276.625 823.358 1.00135.03 C ANISOU 975 C ASN A 146 9164 17110 25030 -2819 71 -3463 C ATOM 976 O ASN A 146 -23.054 276.636 822.370 1.00126.87 O ANISOU 976 O ASN A 146 8264 16034 23907 -2961 523 -3126 O ATOM 977 N GLY A 147 -24.999 277.098 823.368 1.00138.92 N ANISOU 977 N GLY A 147 9462 17380 25940 -3050 -303 -3697 N ATOM 978 CA GLY A 147 -25.624 277.606 822.174 1.00135.44 C ANISOU 978 CA GLY A 147 8983 16582 25895 -3490 -218 -3563 C ATOM 979 C GLY A 147 -26.688 276.590 821.928 1.00136.38 C ANISOU 979 C GLY A 147 9611 16416 25791 -3385 -587 -3795 C ATOM 980 O GLY A 147 -26.883 275.731 822.765 1.00137.42 O ANISOU 980 O GLY A 147 10006 16691 25518 -3031 -863 -4032 O ATOM 981 N GLU A 148 -27.387 276.672 820.812 1.00135.35 N ANISOU 981 N GLU A 148 9625 15887 25914 -3679 -604 -3736 N ATOM 982 CA GLU A 148 -28.429 275.703 820.566 1.00128.29 C ANISOU 982 CA GLU A 148 9189 14739 24815 -3547 -948 -4010 C ATOM 983 CB GLU A 148 -29.762 276.407 820.429 1.00125.53 C ANISOU 983 CB GLU A 148 8619 14049 25029 -3829 -1379 -4306 C ATOM 984 CG GLU A 148 -29.633 277.826 819.978 1.00133.60 C ANISOU 984 CG GLU A 148 9118 14929 26715 -4299 -1228 -4080 C ATOM 985 CD GLU A 148 -30.961 278.527 819.978 1.00151.56 C ANISOU 985 CD GLU A 148 11153 16856 29576 -4578 -1721 -4403 C ATOM 986 OE1 GLU A 148 -31.961 277.910 819.571 1.00152.05 O ANISOU 986 OE1 GLU A 148 11584 16595 29592 -4515 -2046 -4675 O ATOM 987 OE2 GLU A 148 -31.012 279.694 820.391 1.00163.58 O ANISOU 987 OE2 GLU A 148 12101 18433 31617 -4856 -1795 -4411 O ATOM 988 C GLU A 148 -28.155 274.864 819.350 1.00124.46 C ANISOU 988 C GLU A 148 9189 14046 24055 -3534 -665 -3761 C ATOM 989 O GLU A 148 -27.867 275.385 818.288 1.00128.66 O ANISOU 989 O GLU A 148 9670 14351 24862 -3835 -394 -3443 O ATOM 990 N TRP A 149 -28.229 273.552 819.552 1.00121.37 N ANISOU 990 N TRP A 149 9258 13751 23108 -3183 -741 -3899 N ATOM 991 CA TRP A 149 -28.100 272.540 818.510 1.00116.26 C ANISOU 991 CA TRP A 149 9084 12930 22159 -3101 -551 -3750 C ATOM 992 CB TRP A 149 -26.829 271.728 818.725 1.00108.43 C ANISOU 992 CB TRP A 149 8331 12257 20610 -2834 -210 -3490 C ATOM 993 CG TRP A 149 -26.536 271.560 820.140 1.00104.68 C ANISOU 993 CG TRP A 149 7764 12155 19854 -2573 -348 -3646 C ATOM 994 CD1 TRP A 149 -25.970 272.458 820.953 1.00100.86 C ANISOU 994 CD1 TRP A 149 6872 11899 19550 -2593 -312 -3603 C ATOM 995 NE1 TRP A 149 -25.875 271.958 822.212 1.00 96.44 N ANISOU 995 NE1 TRP A 149 6375 11621 18649 -2280 -536 -3791 N ATOM 996 CE2 TRP A 149 -26.399 270.701 822.220 1.00100.64 C ANISOU 996 CE2 TRP A 149 7374 12127 18739 -2084 -696 -3937 C ATOM 997 CZ2 TRP A 149 -26.535 269.804 823.244 1.00103.96 C ANISOU 997 CZ2 TRP A 149 8048 12764 18687 -1786 -938 -4107 C ATOM 998 CH2 TRP A 149 -27.106 268.604 822.955 1.00101.11 C ANISOU 998 CH2 TRP A 149 8128 12360 17930 -1673 -1006 -4216 C ATOM 999 CZ3 TRP A 149 -27.537 268.303 821.686 1.00104.63 C ANISOU 999 CZ3 TRP A 149 8736 12539 18478 -1813 -862 -4193 C ATOM 1000 CE3 TRP A 149 -27.406 269.190 820.672 1.00109.18 C ANISOU 1000 CE3 TRP A 149 9086 12856 19540 -2088 -670 -4023 C ATOM 1001 CD2 TRP A 149 -26.825 270.422 820.932 1.00104.72 C ANISOU 1001 CD2 TRP A 149 8091 12342 19354 -2249 -571 -3872 C ATOM 1002 C TRP A 149 -29.320 271.617 818.366 1.00112.90 C ANISOU 1002 C TRP A 149 8995 12321 21579 -2946 -898 -4138 C ATOM 1003 O TRP A 149 -29.232 270.603 817.715 1.00106.49 O ANISOU 1003 O TRP A 149 8563 11449 20450 -2799 -770 -4082 O ATOM 1004 N PHE A 150 -30.448 271.963 818.970 1.00120.90 N ANISOU 1004 N PHE A 150 9859 13265 22813 -2970 -1338 -4549 N ATOM 1005 CA PHE A 150 -31.675 271.183 818.833 1.00122.81 C ANISOU 1005 CA PHE A 150 10399 13347 22917 -2824 -1672 -4971 C ATOM 1006 CB PHE A 150 -32.472 271.176 820.124 1.00120.18 C ANISOU 1006 CB PHE A 150 9992 13227 22445 -2667 -2112 -5406 C ATOM 1007 CG PHE A 150 -31.805 270.521 821.275 1.00116.81 C ANISOU 1007 CG PHE A 150 9769 13248 21365 -2336 -2073 -5403 C ATOM 1008 CD1 PHE A 150 -31.851 269.167 821.445 1.00123.53 C ANISOU 1008 CD1 PHE A 150 11046 14234 21655 -2104 -1872 -5340 C ATOM 1009 CE1 PHE A 150 -31.256 268.579 822.533 1.00127.69 C ANISOU 1009 CE1 PHE A 150 11775 15145 21594 -1838 -1863 -5313 C ATOM 1010 CZ PHE A 150 -30.634 269.356 823.466 1.00126.79 C ANISOU 1010 CZ PHE A 150 11457 15265 21453 -1769 -2092 -5368 C ATOM 1011 CE2 PHE A 150 -30.610 270.712 823.312 1.00119.16 C ANISOU 1011 CE2 PHE A 150 10044 14179 21054 -1968 -2308 -5468 C ATOM 1012 CD2 PHE A 150 -31.198 271.283 822.236 1.00117.05 C ANISOU 1012 CD2 PHE A 150 9560 13548 21364 -2263 -2289 -5484 C ATOM 1013 C PHE A 150 -32.585 271.876 817.837 1.00139.07 C ANISOU 1013 C PHE A 150 12360 14894 25587 -3119 -1864 -5087 C ATOM 1014 O PHE A 150 -32.824 273.059 817.959 1.00151.22 O ANISOU 1014 O PHE A 150 13516 16279 27660 -3411 -2015 -5089 O ATOM 1015 N HIS A 151 -33.097 271.146 816.861 1.00148.13 N ANISOU 1015 N HIS A 151 13837 15763 26682 -3045 -1878 -5190 N ATOM 1016 CA HIS A 151 -34.028 271.699 815.878 1.00168.45 C ANISOU 1016 CA HIS A 151 16378 17787 29840 -3285 -2120 -5335 C ATOM 1017 CB HIS A 151 -33.389 271.769 814.494 1.00180.45 C ANISOU 1017 CB HIS A 151 18011 18985 31565 -3462 -1799 -4884 C ATOM 1018 CG HIS A 151 -33.264 273.160 813.953 1.00195.75 C ANISOU 1018 CG HIS A 151 19628 20580 34168 -3929 -1784 -4578 C ATOM 1019 ND1 HIS A 151 -33.876 273.563 812.784 1.00204.23 N ANISOU 1019 ND1 HIS A 151 20770 21062 35765 -4175 -1951 -4544 N ATOM 1020 CE1 HIS A 151 -33.595 274.833 812.552 1.00206.14 C ANISOU 1020 CE1 HIS A 151 20682 21120 36521 -4620 -1880 -4208 C ATOM 1021 NE2 HIS A 151 -32.826 275.272 813.532 1.00204.86 N ANISOU 1021 NE2 HIS A 151 20210 21437 36191 -4647 -1658 -4057 N ATOM 1022 CD2 HIS A 151 -32.605 274.246 814.421 1.00199.55 C ANISOU 1022 CD2 HIS A 151 19707 21229 34883 -4207 -1618 -4287 C ATOM 1023 C HIS A 151 -35.329 270.903 815.830 1.00171.80 C ANISOU 1023 C HIS A 151 17074 18077 30124 -3042 -2491 -5908 C ATOM 1024 O HIS A 151 -35.967 270.761 814.788 1.00180.35 O ANISOU 1024 O HIS A 151 18316 18726 31485 -3076 -2610 -6040 O ATOM 1025 N LEU A 152 -35.753 270.378 816.976 1.00159.97 N ANISOU 1025 N LEU A 152 15642 16956 28184 -2783 -2692 -6271 N ATOM 1026 CA LEU A 152 -36.851 269.424 816.961 1.00146.53 C ANISOU 1026 CA LEU A 152 14247 15249 26181 -2500 -2947 -6799 C ATOM 1027 CB LEU A 152 -37.248 269.036 818.382 1.00133.39 C ANISOU 1027 CB LEU A 152 12629 14042 24012 -2271 -3183 -7137 C ATOM 1028 CG LEU A 152 -36.833 267.673 818.926 1.00120.38 C ANISOU 1028 CG LEU A 152 11301 12890 21548 -1936 -2945 -7109 C ATOM 1029 CD1 LEU A 152 -37.154 267.552 820.392 1.00107.17 C ANISOU 1029 CD1 LEU A 152 9645 11623 19452 -1784 -3224 -7355 C ATOM 1030 CD2 LEU A 152 -37.554 266.595 818.178 1.00125.70 C ANISOU 1030 CD2 LEU A 152 12295 13490 21975 -1718 -2919 -7425 C ATOM 1031 C LEU A 152 -38.054 269.994 816.244 1.00152.45 C ANISOU 1031 C LEU A 152 14956 15449 27520 -2649 -3344 -7171 C ATOM 1032 O LEU A 152 -38.511 271.085 816.538 1.00149.79 O ANISOU 1032 O LEU A 152 14334 14900 27680 -2903 -3662 -7285 O ATOM 1033 N GLN A 153 -38.569 269.205 815.312 1.00160.59 N ANISOU 1033 N GLN A 153 16269 16250 28498 -2473 -3342 -7382 N ATOM 1034 CA GLN A 153 -39.683 269.585 814.469 1.00170.55 C ANISOU 1034 CA GLN A 153 17558 16931 30313 -2558 -3717 -7749 C ATOM 1035 CB GLN A 153 -39.194 269.960 813.081 1.00166.28 C ANISOU 1035 CB GLN A 153 17016 15886 30276 -2788 -3534 -7318 C ATOM 1036 CG GLN A 153 -37.939 270.759 813.069 1.00158.80 C ANISOU 1036 CG GLN A 153 15832 15007 29498 -3113 -3192 -6642 C ATOM 1037 CD GLN A 153 -37.621 271.239 811.697 1.00155.64 C ANISOU 1037 CD GLN A 153 15457 14066 29615 -3381 -3089 -6241 C ATOM 1038 NE2 GLN A 153 -36.431 271.770 811.516 1.00151.07 N ANISOU 1038 NE2 GLN A 153 14737 13580 29083 -3631 -2710 -5620 N ATOM 1039 OE1 GLN A 153 -38.437 271.130 810.797 1.00159.59 O ANISOU 1039 OE1 GLN A 153 16115 14062 30458 -3352 -3358 -6492 O ATOM 1040 C GLN A 153 -40.600 268.403 814.336 1.00178.45 C ANISOU 1040 C GLN A 153 18878 18020 30907 -2157 -3844 -8313 C ATOM 1041 O GLN A 153 -40.182 267.268 814.500 1.00174.12 O ANISOU 1041 O GLN A 153 18529 17897 29731 -1876 -3531 -8267 O ATOM 1042 N ASN A 154 -41.869 268.668 814.114 1.00189.24 N ANISOU 1042 N ASN A 154 20276 19015 32610 -2131 -4309 -8873 N ATOM 1043 CA ASN A 154 -42.824 267.600 813.961 1.00195.14 C ANISOU 1043 CA ASN A 154 21306 19849 32989 -1734 -4436 -9480 C ATOM 1044 CB ASN A 154 -43.879 267.710 815.049 1.00197.12 C ANISOU 1044 CB ASN A 154 21571 20312 33015 -1620 -4872 -10087 C ATOM 1045 CG ASN A 154 -44.068 266.427 815.800 1.00195.25 C ANISOU 1045 CG ASN A 154 21585 20727 31874 -1229 -4709 -10381 C ATOM 1046 OD1 ASN A 154 -44.513 265.434 815.236 1.00197.13 O ANISOU 1046 OD1 ASN A 154 22042 21018 31842 -928 -4599 -10701 O ATOM 1047 ND2 ASN A 154 -43.737 266.438 817.086 1.00191.63 N ANISOU 1047 ND2 ASN A 154 21089 20775 30946 -1234 -4699 -10271 N ATOM 1048 C ASN A 154 -43.447 267.728 812.594 1.00201.60 C ANISOU 1048 C ASN A 154 22203 19990 34406 -1740 -4635 -9675 C ATOM 1049 O ASN A 154 -44.510 267.187 812.338 1.00209.79 O ANISOU 1049 O ASN A 154 23414 20911 35385 -1455 -4890 -10302 O ATOM 1050 N PRO A 155 -42.788 268.485 811.729 1.00197.55 N ANISOU 1050 N PRO A 155 21566 19021 34474 -2068 -4534 -9141 N ATOM 1051 CD PRO A 155 -41.398 268.930 811.880 1.00194.64 C ANISOU 1051 CD PRO A 155 21026 18853 34075 -2345 -4123 -8384 C ATOM 1052 CG PRO A 155 -41.083 269.491 810.528 1.00193.95 C ANISOU 1052 CG PRO A 155 20932 18135 34626 -2606 -4095 -7986 C ATOM 1053 CB PRO A 155 -42.361 269.925 809.963 1.00196.60 C ANISOU 1053 CB PRO A 155 21308 17839 35550 -2641 -4631 -8485 C ATOM 1054 CA PRO A 155 -43.337 268.854 810.425 1.00195.54 C ANISOU 1054 CA PRO A 155 21374 18009 34914 -2159 -4799 -9235 C ATOM 1055 C PRO A 155 -43.396 267.795 809.344 1.00185.31 C ANISOU 1055 C PRO A 155 20325 16571 33514 -1821 -4651 -9348 C ATOM 1056 O PRO A 155 -42.386 267.205 809.005 1.00171.33 O ANISOU 1056 O PRO A 155 18610 15041 31448 -1759 -4207 -8888 O ATOM 1057 N TYR A 156 -44.586 267.614 808.782 1.00186.24 N ANISOU 1057 N TYR A 156 20574 16263 33926 -1607 -5058 -9975 N ATOM 1058 CA TYR A 156 -44.808 266.737 807.640 1.00187.70 C ANISOU 1058 CA TYR A 156 20952 16193 34172 -1275 -5019 -10168 C ATOM 1059 CB TYR A 156 -43.678 266.946 806.632 1.00 20.00 C ATOM 1060 CG TYR A 156 -42.479 266.053 806.861 1.00 20.00 C ATOM 1061 CD2 TYR A 156 -41.418 266.472 807.651 1.00 20.00 C ATOM 1062 CE2 TYR A 156 -40.320 265.658 807.863 1.00 20.00 C ATOM 1063 CZ TYR A 156 -40.274 264.410 807.279 1.00 20.00 C ATOM 1064 OH TYR A 156 -39.185 263.595 807.487 1.00 20.00 O ATOM 1065 CE1 TYR A 156 -41.316 263.971 806.488 1.00 20.00 C ATOM 1066 CD1 TYR A 156 -42.409 264.790 806.282 1.00 20.00 C ATOM 1067 C TYR A 156 -44.939 265.245 807.912 1.00180.96 C ANISOU 1067 C TYR A 156 20234 15966 32556 -771 -4730 -10555 C ATOM 1068 O TYR A 156 -45.081 264.460 806.983 1.00171.90 O ANISOU 1068 O TYR A 156 19199 14665 31451 -472 -4667 -10725 O ATOM 1069 N ASP A 157 -44.911 264.846 809.170 1.00178.96 N ANISOU 1069 N ASP A 157 19962 16413 31621 -678 -4566 -10695 N ATOM 1070 CA ASP A 157 -45.005 263.426 809.478 1.00172.41 C ANISOU 1070 CA ASP A 157 19256 16220 30030 -253 -4255 -11008 C ATOM 1071 CB ASP A 157 -43.668 262.873 810.012 1.00150.56 C ANISOU 1071 CB ASP A 157 16460 14065 26679 -320 -3702 -10372 C ATOM 1072 CG ASP A 157 -43.526 261.375 809.834 1.00130.05 C ANISOU 1072 CG ASP A 157 13968 11958 23487 56 -3321 -10517 C ATOM 1073 OD1 ASP A 157 -43.567 260.884 808.708 1.00111.16 O ANISOU 1073 OD1 ASP A 157 11603 9284 21351 239 -3270 -10585 O ATOM 1074 OD2 ASP A 157 -43.342 260.681 810.829 1.00113.90 O ANISOU 1074 OD2 ASP A 157 11967 10585 20723 156 -3073 -10536 O ATOM 1075 C ASP A 157 -46.120 263.173 810.468 1.00187.41 C ANISOU 1075 C ASP A 157 21231 18480 31498 -36 -4504 -11727 C ATOM 1076 O ASP A 157 -46.336 263.940 811.397 1.00194.30 O ANISOU 1076 O ASP A 157 22038 19421 32367 -244 -4748 -11764 O ATOM 1077 N PHE A 158 -46.827 262.079 810.258 1.00189.87 N ANISOU 1077 N PHE A 158 21671 19039 31432 394 -4442 -12309 N ATOM 1078 CA PHE A 158 -47.881 261.701 811.153 1.00189.60 C ANISOU 1078 CA PHE A 158 21747 19415 30877 638 -4631 -13012 C ATOM 1079 CB PHE A 158 -49.244 262.110 810.605 1.00187.09 C ANISOU 1079 CB PHE A 158 21490 18523 31073 805 -5190 -13782 C ATOM 1080 CG PHE A 158 -49.435 263.595 810.525 1.00191.82 C ANISOU 1080 CG PHE A 158 21989 18427 32466 412 -5691 -13655 C ATOM 1081 CD1 PHE A 158 -50.051 264.173 809.434 1.00197.28 C ANISOU 1081 CD1 PHE A 158 22687 18281 33990 396 -6111 -13909 C ATOM 1082 CE1 PHE A 158 -50.221 265.541 809.362 1.00194.79 C ANISOU 1082 CE1 PHE A 158 22266 17323 34421 -16 -6565 -13757 C ATOM 1083 CZ PHE A 158 -49.766 266.346 810.377 1.00192.13 C ANISOU 1083 CZ PHE A 158 21778 17211 34014 -395 -6584 -13371 C ATOM 1084 CE2 PHE A 158 -49.144 265.783 811.471 1.00187.48 C ANISOU 1084 CE2 PHE A 158 21178 17448 32606 -342 -6183 -13139 C ATOM 1085 CD2 PHE A 158 -48.980 264.416 811.539 1.00187.13 C ANISOU 1085 CD2 PHE A 158 21278 18010 31812 48 -5748 -13265 C ATOM 1086 C PHE A 158 -47.808 260.214 811.426 1.00192.37 C ANISOU 1086 C PHE A 158 22196 20513 30382 992 -4168 -13183 C ATOM 1087 O PHE A 158 -47.156 259.472 810.710 1.00179.48 O ANISOU 1087 O PHE A 158 20528 18959 28708 1099 -3786 -12900 O ATOM 1088 N THR A 159 -48.489 259.796 812.476 1.00204.17 N ANISOU 1088 N THR A 159 23813 22564 31198 1154 -4219 -13639 N ATOM 1089 CA THR A 159 -48.527 258.411 812.873 1.00204.25 C ANISOU 1089 CA THR A 159 23925 23342 30338 1450 -3788 -13824 C ATOM 1090 CB THR A 159 -49.326 258.226 814.165 1.00213.28 C ANISOU 1090 CB THR A 159 25243 25042 30753 1550 -3946 -14285 C ATOM 1091 OG1 THR A 159 -48.783 259.072 815.188 1.00210.68 O ANISOU 1091 OG1 THR A 159 24898 24766 30386 1204 -4103 -13817 O ATOM 1092 CG2 THR A 159 -49.268 256.779 814.628 1.00214.75 C ANISOU 1092 CG2 THR A 159 25541 26071 29981 1792 -3443 -14370 C ATOM 1093 C THR A 159 -49.230 257.733 811.729 1.00198.51 C ANISOU 1093 C THR A 159 23189 22409 29828 1831 -3770 -14393 C ATOM 1094 O THR A 159 -49.260 256.517 811.622 1.00198.79 O ANISOU 1094 O THR A 159 23235 22966 29328 2112 -3369 -14573 O ATOM 1095 N VAL A 160 -49.841 258.541 810.883 1.00191.63 N ANISOU 1095 N VAL A 160 22283 20759 29767 1840 -4232 -14703 N ATOM 1096 CA VAL A 160 -50.551 258.012 809.741 1.00186.63 C ANISOU 1096 CA VAL A 160 21637 19818 29455 2227 -4306 -15282 C ATOM 1097 CB VAL A 160 -51.046 259.141 808.850 1.00180.59 C ANISOU 1097 CB VAL A 160 20855 18058 29702 2127 -4888 -15449 C ATOM 1098 CG1 VAL A 160 -49.940 259.548 807.889 1.00172.10 C ANISOU 1098 CG1 VAL A 160 19664 16463 29263 1860 -4767 -14664 C ATOM 1099 CG2 VAL A 160 -52.264 258.693 808.076 1.00183.30 C ANISOU 1099 CG2 VAL A 160 21253 18134 30260 2605 -5154 -16369 C ATOM 1100 C VAL A 160 -49.589 257.267 808.863 1.00182.99 C ANISOU 1100 C VAL A 160 21053 19400 29074 2287 -3848 -14802 C ATOM 1101 O VAL A 160 -49.857 256.144 808.471 1.00188.21 O ANISOU 1101 O VAL A 160 21676 20413 29421 2660 -3566 -15172 O ATOM 1102 N ARG A 161 -48.449 257.869 808.570 1.00176.33 N ANISOU 1102 N ARG A 161 20133 18238 28626 1922 -3761 -13982 N ATOM 1103 CA ARG A 161 -47.468 257.185 807.739 1.00172.40 C ANISOU 1103 CA ARG A 161 19534 17772 28197 1964 -3359 -13495 C ATOM 1104 CB ARG A 161 -47.370 257.845 806.371 1.00172.77 C ANISOU 1104 CB ARG A 161 19541 16915 29187 1914 -3665 -13342 C ATOM 1105 CG ARG A 161 -48.737 257.981 805.731 1.00179.23 C ANISOU 1105 CG ARG A 161 20406 17230 30461 2242 -4145 -14195 C ATOM 1106 CD ARG A 161 -48.653 258.353 804.286 1.00181.97 C ANISOU 1106 CD ARG A 161 20734 16722 31685 2274 -4421 -14073 C ATOM 1107 NE ARG A 161 -48.223 257.232 803.469 1.00185.35 N ANISOU 1107 NE ARG A 161 21064 17342 32021 2590 -4081 -14032 N ATOM 1108 CZ ARG A 161 -47.804 257.351 802.216 1.00183.94 C ANISOU 1108 CZ ARG A 161 20862 16544 32483 2611 -4209 -13735 C ATOM 1109 NH1 ARG A 161 -47.762 258.543 801.643 1.00178.58 N ANISOU 1109 NH1 ARG A 161 20275 15021 32557 2311 -4647 -13428 N ATOM 1110 NH2 ARG A 161 -47.419 256.282 801.541 1.00184.90 N ANISOU 1110 NH2 ARG A 161 20866 16895 32494 2914 -3910 -13726 N ATOM 1111 C ARG A 161 -46.157 257.113 808.516 1.00162.40 C ANISOU 1111 C ARG A 161 18247 16978 26480 1639 -2948 -12682 C ATOM 1112 O ARG A 161 -45.603 258.122 808.919 1.00161.00 O ANISOU 1112 O ARG A 161 18068 16580 26526 1262 -3074 -12190 O ATOM 1113 N VAL A 162 -45.700 255.884 808.721 1.00152.77 N ANISOU 1113 N VAL A 162 16997 16417 24631 1799 -2459 -12583 N ATOM 1114 CA VAL A 162 -44.514 255.555 809.494 1.00145.83 C ANISOU 1114 CA VAL A 162 16121 16059 23230 1559 -2048 -11899 C ATOM 1115 CB VAL A 162 -44.611 254.089 809.974 1.00140.74 C ANISOU 1115 CB VAL A 162 15479 16235 21761 1803 -1606 -12118 C ATOM 1116 CG2 VAL A 162 -45.980 253.842 810.546 1.00145.00 C ANISOU 1116 CG2 VAL A 162 16112 17076 21905 2060 -1775 -12929 C ATOM 1117 CG1 VAL A 162 -43.570 253.785 811.024 1.00133.97 C ANISOU 1117 CG1 VAL A 162 14678 15929 20296 1548 -1264 -11492 C ATOM 1118 C VAL A 162 -43.137 255.841 808.913 1.00145.60 C ANISOU 1118 C VAL A 162 16023 15752 23546 1299 -1869 -11087 C ATOM 1119 O VAL A 162 -42.950 255.828 807.703 1.00136.75 O ANISOU 1119 O VAL A 162 14836 14167 22955 1378 -1916 -11009 O ATOM 1120 N PRO A 163 -42.189 256.114 809.799 1.00146.98 N ANISOU 1120 N PRO A 163 16229 16219 23397 1005 -1688 -10503 N ATOM 1121 CD PRO A 163 -42.226 255.705 811.213 1.00147.35 C ANISOU 1121 CD PRO A 163 16370 16819 22798 932 -1660 -10573 C ATOM 1122 CG PRO A 163 -41.022 256.372 811.800 1.00138.87 C ANISOU 1122 CG PRO A 163 15296 15966 21503 659 -1385 -9809 C ATOM 1123 CB PRO A 163 -40.186 256.901 810.678 1.00134.26 C ANISOU 1123 CB PRO A 163 14624 14806 21582 485 -1415 -9345 C ATOM 1124 CA PRO A 163 -40.833 256.407 809.384 1.00137.38 C ANISOU 1124 CA PRO A 163 14971 14839 22387 747 -1490 -9725 C ATOM 1125 C PRO A 163 -40.175 255.130 808.907 1.00133.11 C ANISOU 1125 C PRO A 163 14387 14621 21568 907 -1080 -9531 C ATOM 1126 O PRO A 163 -40.481 254.045 809.384 1.00127.31 O ANISOU 1126 O PRO A 163 13658 14477 20237 1089 -828 -9782 O ATOM 1127 N HIS A 164 -39.273 255.261 807.955 1.00140.11 N ANISOU 1127 N HIS A 164 15831 12358 25045 803 2126 -5427 N ATOM 1128 CA HIS A 164 -38.604 254.097 807.404 1.00136.91 C ANISOU 1128 CA HIS A 164 15238 12121 24660 1175 2614 -6025 C ATOM 1129 CB HIS A 164 -39.390 253.626 806.189 1.00146.00 C ANISOU 1129 CB HIS A 164 16739 12921 25814 1446 2155 -6605 C ATOM 1130 CG HIS A 164 -39.024 252.259 805.723 1.00154.31 C ANISOU 1130 CG HIS A 164 17680 14102 26848 1859 2622 -7331 C ATOM 1131 ND1 HIS A 164 -38.983 251.173 806.566 1.00157.55 N ANISOU 1131 ND1 HIS A 164 17926 14836 27100 1954 3183 -7616 N ATOM 1132 CE1 HIS A 164 -38.646 250.098 805.880 1.00161.31 C ANISOU 1132 CE1 HIS A 164 18174 15638 27479 2043 3328 -7931 C ATOM 1133 NE2 HIS A 164 -38.472 250.448 804.619 1.00162.17 N ANISOU 1133 NE2 HIS A 164 18350 15547 27721 2153 2963 -8009 N ATOM 1134 CD2 HIS A 164 -38.709 251.794 804.492 1.00159.16 C ANISOU 1134 CD2 HIS A 164 18268 14672 27535 2106 2547 -7721 C ATOM 1135 C HIS A 164 -37.132 254.249 807.024 1.00125.57 C ANISOU 1135 C HIS A 164 13369 10974 23368 1189 3008 -5813 C ATOM 1136 O HIS A 164 -36.256 253.609 807.597 1.00116.43 O ANISOU 1136 O HIS A 164 11873 10172 22195 1289 3693 -5903 O ATOM 1137 N PHE A 165 -36.884 255.094 806.033 1.00124.60 N ANISOU 1137 N PHE A 165 13273 10688 23383 1093 2557 -5541 N ATOM 1138 CA PHE A 165 -35.543 255.304 805.501 1.00118.13 C ANISOU 1138 CA PHE A 165 12083 10096 22707 1112 2843 -5347 C ATOM 1139 CB PHE A 165 -35.387 254.510 804.206 1.00126.17 C ANISOU 1139 CB PHE A 165 13153 11000 23785 1475 2812 -5973 C ATOM 1140 CG PHE A 165 -33.999 254.524 803.638 1.00133.21 C ANISOU 1140 CG PHE A 165 13664 12135 24814 1550 3165 -5879 C ATOM 1141 CD1 PHE A 165 -33.521 255.639 802.974 1.00141.58 C ANISOU 1141 CD1 PHE A 165 14662 13121 26013 1348 2801 -5376 C ATOM 1142 CE1 PHE A 165 -32.252 255.650 802.432 1.00143.69 C ANISOU 1142 CE1 PHE A 165 14587 13605 26402 1423 3118 -5296 C ATOM 1143 CZ PHE A 165 -31.447 254.536 802.541 1.00137.91 C ANISOU 1143 CZ PHE A 165 13574 13166 25659 1703 3800 -5726 C ATOM 1144 CE2 PHE A 165 -31.915 253.412 803.193 1.00137.62 C ANISOU 1144 CE2 PHE A 165 13589 13316 25385 1665 4033 -6065 C ATOM 1145 CD2 PHE A 165 -33.186 253.407 803.731 1.00135.29 C ANISOU 1145 CD2 PHE A 165 13631 12738 25036 1758 3811 -6255 C ATOM 1146 C PHE A 165 -35.276 256.787 805.257 1.00113.21 C ANISOU 1146 C PHE A 165 11425 9390 22201 759 2393 -4606 C ATOM 1147 O PHE A 165 -36.111 257.493 804.698 1.00109.75 O ANISOU 1147 O PHE A 165 11315 8602 21784 633 1701 -4470 O ATOM 1148 N LEU A 166 -34.110 257.258 805.684 1.00113.93 N ANISOU 1148 N LEU A 166 11117 9806 22366 600 2788 -4125 N ATOM 1149 CA LEU A 166 -33.732 258.647 805.474 1.00115.33 C ANISOU 1149 CA LEU A 166 11214 9948 22657 269 2423 -3406 C ATOM 1150 CB LEU A 166 -33.525 259.353 806.816 1.00120.25 C ANISOU 1150 CB LEU A 166 11653 10800 23239 -66 2631 -2767 C ATOM 1151 CG LEU A 166 -33.859 260.847 806.897 1.00130.32 C ANISOU 1151 CG LEU A 166 13035 11911 24569 -471 2046 -2035 C ATOM 1152 CD1 LEU A 166 -33.378 261.426 808.221 1.00134.06 C ANISOU 1152 CD1 LEU A 166 13233 12690 25013 -762 2391 -1427 C ATOM 1153 CD2 LEU A 166 -33.265 261.623 805.731 1.00132.04 C ANISOU 1153 CD2 LEU A 166 13186 12036 24945 -533 1711 -1773 C ATOM 1154 C LEU A 166 -32.463 258.720 804.629 1.00109.72 C ANISOU 1154 C LEU A 166 10192 9407 22091 368 2647 -3353 C ATOM 1155 O LEU A 166 -31.412 258.218 805.027 1.00111.26 O ANISOU 1155 O LEU A 166 10018 9959 22298 469 3304 -3390 O ATOM 1156 N PHE A 167 -32.573 259.332 803.455 1.00102.89 N ANISOU 1156 N PHE A 167 9483 8279 21332 341 2094 -3276 N ATOM 1157 CA PHE A 167 -31.431 259.494 802.568 1.00101.16 C ANISOU 1157 CA PHE A 167 9000 8182 21252 421 2229 -3203 C ATOM 1158 CB PHE A 167 -31.719 258.867 801.209 1.00101.02 C ANISOU 1158 CB PHE A 167 9198 7905 21279 738 1954 -3818 C ATOM 1159 CG PHE A 167 -30.539 258.873 800.285 1.00109.19 C ANISOU 1159 CG PHE A 167 9963 9073 22451 863 2138 -3827 C ATOM 1160 CD1 PHE A 167 -30.423 259.832 799.296 1.00116.15 C ANISOU 1160 CD1 PHE A 167 10927 9752 23453 728 1607 -3506 C ATOM 1161 CE1 PHE A 167 -29.336 259.844 798.441 1.00122.58 C ANISOU 1161 CE1 PHE A 167 11498 10686 24390 844 1773 -3512 C ATOM 1162 CZ PHE A 167 -28.344 258.890 798.572 1.00124.85 C ANISOU 1162 CZ PHE A 167 11454 11299 24683 1096 2477 -3839 C ATOM 1163 CE2 PHE A 167 -28.445 257.928 799.560 1.00122.72 C ANISOU 1163 CE2 PHE A 167 11097 11235 24296 1229 3012 -4157 C ATOM 1164 CD2 PHE A 167 -29.538 257.924 800.411 1.00117.24 C ANISOU 1164 CD2 PHE A 167 10648 10420 23477 1112 2844 -4149 C ATOM 1165 C PHE A 167 -31.085 260.962 802.391 1.00103.09 C ANISOU 1165 C PHE A 167 9174 8392 21605 62 1844 -2437 C ATOM 1166 O PHE A 167 -31.973 261.802 802.292 1.00115.31 O ANISOU 1166 O PHE A 167 11015 9650 23147 -166 1216 -2145 O ATOM 1167 N TYR A 168 -29.790 261.260 802.330 1.00 99.21 N ANISOU 1167 N TYR A 168 8294 8194 21209 18 2218 -2119 N ATOM 1168 CA TYR A 168 -29.305 262.638 802.289 1.00103.69 C ANISOU 1168 CA TYR A 168 8727 8796 21873 -328 1955 -1354 C ATOM 1169 CB TYR A 168 -28.031 262.765 803.123 1.00 84.77 C ANISOU 1169 CB TYR A 168 5858 6852 19498 -420 2617 -962 C ATOM 1170 CG TYR A 168 -27.313 264.088 802.989 1.00 98.59 C ANISOU 1170 CG TYR A 168 7410 8691 21360 -731 2439 -210 C ATOM 1171 CD1 TYR A 168 -27.518 265.109 803.909 1.00 88.24 C ANISOU 1171 CD1 TYR A 168 6065 7437 20027 -1104 2292 459 C ATOM 1172 CE1 TYR A 168 -26.856 266.318 803.793 1.00 91.13 C ANISOU 1172 CE1 TYR A 168 6240 7894 20493 -1388 2137 1151 C ATOM 1173 CZ TYR A 168 -25.975 266.518 802.754 1.00 91.20 C ANISOU 1173 CZ TYR A 168 6094 7935 20622 -1302 2130 1180 C ATOM 1174 OH TYR A 168 -25.311 267.719 802.634 1.00 93.08 O ANISOU 1174 OH TYR A 168 6141 8269 20957 -1582 1981 1869 O ATOM 1175 CE2 TYR A 168 -25.750 265.519 801.829 1.00 94.91 C ANISOU 1175 CE2 TYR A 168 6599 8346 21118 -934 2273 523 C ATOM 1176 CD2 TYR A 168 -26.414 264.312 801.950 1.00 99.62 C ANISOU 1176 CD2 TYR A 168 7380 8855 21617 -651 2428 -166 C ATOM 1177 C TYR A 168 -29.072 263.172 800.873 1.00114.57 C ANISOU 1177 C TYR A 168 10187 9959 23384 -306 1492 -1310 C ATOM 1178 O TYR A 168 -28.335 262.583 800.080 1.00106.50 O ANISOU 1178 O TYR A 168 9020 9016 22428 -44 1737 -1661 O ATOM 1179 N VAL A 169 -29.710 264.302 800.579 1.00136.54 N ANISOU 1179 N VAL A 169 13205 12468 26205 -590 816 -867 N ATOM 1180 CA VAL A 169 -29.579 264.979 799.292 1.00148.83 C ANISOU 1180 CA VAL A 169 14868 13797 27885 -627 302 -736 C ATOM 1181 CB VAL A 169 -30.905 265.631 798.871 1.00154.06 C ANISOU 1181 CB VAL A 169 15992 14011 28531 -790 -525 -655 C ATOM 1182 CG1 VAL A 169 -30.720 266.456 797.611 1.00157.42 C ANISOU 1182 CG1 VAL A 169 16510 14215 29086 -872 -1062 -434 C ATOM 1183 CG2 VAL A 169 -31.981 264.575 798.678 1.00152.86 C ANISOU 1183 CG2 VAL A 169 16190 13612 28278 -505 -656 -1387 C ATOM 1184 C VAL A 169 -28.504 266.063 799.358 1.00155.28 C ANISOU 1184 C VAL A 169 15352 14840 28807 -898 390 -16 C ATOM 1185 O VAL A 169 -28.446 266.842 800.313 1.00157.29 O ANISOU 1185 O VAL A 169 15484 15239 29039 -1210 431 573 O ATOM 1186 N SER A 170 -27.678 266.125 798.317 1.00155.71 N ANISOU 1186 N SER A 170 15272 14916 28974 -778 400 -65 N ATOM 1187 CA SER A 170 -26.452 266.931 798.327 1.00154.16 C ANISOU 1187 CA SER A 170 14705 14992 28876 -959 620 521 C ATOM 1188 CB SER A 170 -25.835 266.995 796.922 1.00147.98 C ANISOU 1188 CB SER A 170 13899 14111 28216 -806 448 377 C ATOM 1189 OG SER A 170 -25.433 265.700 796.487 1.00139.28 O ANISOU 1189 OG SER A 170 12718 13095 27106 -399 878 -323 O ATOM 1190 C SER A 170 -26.532 268.334 798.970 1.00157.37 C ANISOU 1190 C SER A 170 15064 15428 29300 -1409 334 1360 C ATOM 1191 O SER A 170 -25.883 268.583 799.985 1.00157.43 O ANISOU 1191 O SER A 170 14758 15771 29287 -1560 783 1762 O ATOM 1192 N PRO A 171 -27.277 269.250 798.392 1.00158.47 N ANISOU 1192 N PRO A 171 15497 15234 29481 -1623 -392 1635 N ATOM 1193 CD PRO A 171 -27.060 269.314 796.940 1.00156.33 C ANISOU 1193 CD PRO A 171 15332 14753 29313 -1480 -728 1432 C ATOM 1194 CG PRO A 171 -27.313 270.770 796.617 1.00159.92 C ANISOU 1194 CG PRO A 171 15903 15019 29839 -1856 -1364 2105 C ATOM 1195 CB PRO A 171 -27.783 271.453 797.861 1.00163.20 C ANISOU 1195 CB PRO A 171 16310 15510 30187 -2192 -1413 2631 C ATOM 1196 CA PRO A 171 -27.254 270.573 798.984 1.00162.54 C ANISOU 1196 CA PRO A 171 15932 15804 30021 -2046 -628 2442 C ATOM 1197 C PRO A 171 -28.186 270.569 800.158 1.00162.61 C ANISOU 1197 C PRO A 171 16088 15783 29913 -2200 -667 2530 C ATOM 1198 O PRO A 171 -29.206 271.242 800.180 1.00165.47 O ANISOU 1198 O PRO A 171 16760 15855 30254 -2424 -1266 2753 O ATOM 1199 N GLN A 172 -27.828 269.763 801.136 1.00154.30 N ANISOU 1199 N GLN A 172 14816 15032 28779 -2068 -14 2332 N ATOM 1200 CA GLN A 172 -28.564 269.754 802.360 1.00155.36 C ANISOU 1200 CA GLN A 172 15036 15194 28800 -2218 36 2453 C ATOM 1201 CB GLN A 172 -28.508 271.156 802.937 1.00157.01 C ANISOU 1201 CB GLN A 172 15150 15462 29045 -2658 -220 3301 C ATOM 1202 CG GLN A 172 -29.509 272.094 802.290 1.00168.33 C ANISOU 1202 CG GLN A 172 16960 16482 30515 -2888 -1076 3546 C ATOM 1203 CD GLN A 172 -28.869 273.337 801.694 1.00170.87 C ANISOU 1203 CD GLN A 172 17140 16818 30966 -3148 -1372 4179 C ATOM 1204 OE1 GLN A 172 -28.243 274.127 802.397 1.00168.02 O ANISOU 1204 OE1 GLN A 172 16489 16720 30630 -3412 -1180 4806 O ATOM 1205 NE2 GLN A 172 -29.039 273.523 800.392 1.00169.69 N ANISOU 1205 NE2 GLN A 172 17199 16381 30894 -3076 -1850 4020 N ATOM 1206 C GLN A 172 -30.017 269.379 802.163 1.00163.71 C ANISOU 1206 C GLN A 172 16568 15856 29777 -2145 -462 2028 C ATOM 1207 O GLN A 172 -30.854 269.803 802.956 1.00166.46 O ANISOU 1207 O GLN A 172 17086 16109 30054 -2372 -705 2284 O ATOM 1208 N PHE A 173 -30.344 268.589 801.144 1.00163.68 N ANISOU 1208 N PHE A 173 16786 15624 29781 -1831 -618 1384 N ATOM 1209 CA PHE A 173 -31.743 268.173 800.980 1.00157.29 C ANISOU 1209 CA PHE A 173 16435 14444 28885 -1740 -1073 948 C ATOM 1210 CB PHE A 173 -32.379 268.495 799.635 1.00153.42 C ANISOU 1210 CB PHE A 173 16300 13533 28459 -1701 -1790 783 C ATOM 1211 CG PHE A 173 -33.811 268.040 799.548 1.00149.42 C ANISOU 1211 CG PHE A 173 16258 12661 27854 -1601 -2227 334 C ATOM 1212 CD1 PHE A 173 -34.241 267.216 798.525 1.00137.58 C ANISOU 1212 CD1 PHE A 173 15011 10914 26351 -1267 -2413 -347 C ATOM 1213 CE1 PHE A 173 -35.547 266.786 798.468 1.00130.54 C ANISOU 1213 CE1 PHE A 173 14543 9695 25362 -1166 -2800 -763 C ATOM 1214 CZ PHE A 173 -36.436 267.163 799.433 1.00140.12 C ANISOU 1214 CZ PHE A 173 15935 10825 26480 -1399 -3002 -508 C ATOM 1215 CE2 PHE A 173 -36.023 267.976 800.467 1.00149.91 C ANISOU 1215 CE2 PHE A 173 16926 12309 27724 -1735 -2819 168 C ATOM 1216 CD2 PHE A 173 -34.714 268.402 800.526 1.00150.97 C ANISOU 1216 CD2 PHE A 173 16632 12775 27955 -1832 -2427 582 C ATOM 1217 C PHE A 173 -31.843 266.703 801.252 1.00146.16 C ANISOU 1217 C PHE A 173 15023 13132 27378 -1369 -573 217 C ATOM 1218 O PHE A 173 -30.972 265.937 800.854 1.00144.98 O ANISOU 1218 O PHE A 173 14643 13176 27265 -1094 -105 -138 O ATOM 1219 N SER A 174 -32.894 266.315 801.958 1.00139.55 N ANISOU 1219 N SER A 174 14439 12169 26417 -1367 -663 3 N ATOM 1220 CA SER A 174 -32.966 264.926 802.406 1.00135.86 C ANISOU 1220 CA SER A 174 13939 11837 25844 -1039 -126 -646 C ATOM 1221 C SER A 174 -34.304 264.301 802.029 1.00145.69 C ANISOU 1221 C SER A 174 15644 12710 27000 -855 -542 -1223 C ATOM 1222 O SER A 174 -35.349 264.946 802.133 1.00152.44 O ANISOU 1222 O SER A 174 16827 13276 27819 -1065 -1123 -1012 O ATOM 1223 CB SER A 174 -32.756 264.820 803.922 1.00127.90 C ANISOU 1223 CB SER A 174 12703 11151 24744 -1173 397 -391 C ATOM 1224 OG SER A 174 -31.407 265.068 804.297 1.00121.94 O ANISOU 1224 OG SER A 174 11486 10791 24056 -1247 934 -12 O ATOM 1225 N VAL A 175 -34.258 263.042 801.595 1.00139.15 N ANISOU 1225 N VAL A 175 14837 11895 26137 -463 -237 -1950 N ATOM 1226 CA VAL A 175 -35.442 262.305 801.164 1.00123.85 C ANISOU 1226 CA VAL A 175 13314 9629 24114 -233 -570 -2575 C ATOM 1227 C VAL A 175 -35.832 261.253 802.190 1.00118.45 C ANISOU 1227 C VAL A 175 12633 9091 23281 -72 -97 -2979 C ATOM 1228 O VAL A 175 -34.975 260.545 802.714 1.00111.31 O ANISOU 1228 O VAL A 175 11393 8540 22359 70 600 -3126 O ATOM 1229 CB VAL A 175 -35.191 261.591 799.833 1.00110.43 C ANISOU 1229 CB VAL A 175 11666 7811 22482 121 -607 -3159 C ATOM 1230 CG1 VAL A 175 -36.457 260.892 799.360 1.00107.49 C ANISOU 1230 CG1 VAL A 175 11738 7083 22021 352 -993 -3786 C ATOM 1231 CG2 VAL A 175 -34.699 262.576 798.795 1.00109.13 C ANISOU 1231 CG2 VAL A 175 11473 7526 22468 -20 -1024 -2777 C ATOM 1232 N VAL A 176 -37.126 261.148 802.474 1.00125.10 N ANISOU 1232 N VAL A 176 13860 9659 24012 -93 -479 -3159 N ATOM 1233 CA VAL A 176 -37.605 260.161 803.436 1.00128.86 C ANISOU 1233 CA VAL A 176 14378 10245 24337 55 -77 -3552 C ATOM 1234 C VAL A 176 -38.584 259.156 802.814 1.00129.28 C ANISOU 1234 C VAL A 176 14794 10017 24308 392 -288 -4323 C ATOM 1235 O VAL A 176 -39.552 259.536 802.154 1.00128.85 O ANISOU 1235 O VAL A 176 15129 9576 24251 362 -962 -4390 O ATOM 1236 CB VAL A 176 -38.222 260.832 804.694 1.00103.37 C ANISOU 1236 CB VAL A 176 11232 7025 21019 -281 -192 -3057 C ATOM 1237 CG1 VAL A 176 -39.161 261.955 804.298 1.00106.88 C ANISOU 1237 CG1 VAL A 176 12035 7084 21490 -551 -1029 -2684 C ATOM 1238 CG2 VAL A 176 -38.943 259.803 805.552 1.00103.24 C ANISOU 1238 CG2 VAL A 176 11350 7040 20835 -112 103 -3524 C ATOM 1239 N PHE A 177 -38.403 257.879 803.109 1.00130.14 N ANISOU 1239 N PHE A 177 14791 10317 24338 702 283 -4895 N ATOM 1240 CA PHE A 177 -39.295 256.840 802.633 1.00131.10 C ANISOU 1240 CA PHE A 177 15227 10216 24371 1035 161 -5642 C ATOM 1241 CB PHE A 177 -38.497 255.661 802.085 1.00122.76 C ANISOU 1241 CB PHE A 177 13937 9361 23345 1420 703 -6234 C ATOM 1242 CG PHE A 177 -37.422 256.039 801.113 1.00113.15 C ANISOU 1242 CG PHE A 177 12479 8219 22294 1443 715 -6076 C ATOM 1243 CD1 PHE A 177 -37.709 256.261 799.797 1.00115.80 C ANISOU 1243 CD1 PHE A 177 13042 8244 22712 1546 172 -6255 C ATOM 1244 CE1 PHE A 177 -36.728 256.590 798.902 1.00101.61 C ANISOU 1244 CE1 PHE A 177 11030 6514 21065 1572 185 -6119 C ATOM 1245 CZ PHE A 177 -35.442 256.683 799.302 1.00 98.47 C ANISOU 1245 CZ PHE A 177 10186 6496 20734 1504 746 -5813 C ATOM 1246 CE2 PHE A 177 -35.131 256.453 800.605 1.00102.98 C ANISOU 1246 CE2 PHE A 177 10523 7381 21223 1408 1296 -5638 C ATOM 1247 CD2 PHE A 177 -36.118 256.123 801.508 1.00104.14 C ANISOU 1247 CD2 PHE A 177 10886 7461 21222 1379 1282 -5773 C ATOM 1248 C PHE A 177 -40.113 256.338 803.810 1.00136.73 C ANISOU 1248 C PHE A 177 16081 10958 24913 1023 340 -5790 C ATOM 1249 O PHE A 177 -39.699 256.458 804.945 1.00136.10 O ANISOU 1249 O PHE A 177 15761 11160 24790 852 762 -5453 O ATOM 1250 N LEU A 178 -41.284 255.787 803.534 1.00142.68 N ANISOU 1250 N LEU A 178 17230 11416 25566 1203 7 -6290 N ATOM 1251 CA LEU A 178 -42.117 255.162 804.555 1.00144.40 C ANISOU 1251 CA LEU A 178 17611 11645 25611 1244 180 -6531 C ATOM 1252 C LEU A 178 -42.583 253.884 803.893 1.00146.43 C ANISOU 1252 C LEU A 178 18049 11786 25803 1672 257 -7373 C ATOM 1253 O LEU A 178 -42.608 253.831 802.673 1.00147.94 O ANISOU 1253 O LEU A 178 18361 11776 26076 1842 -67 -7640 O ATOM 1254 CB LEU A 178 -43.272 256.059 804.954 1.00143.90 C ANISOU 1254 CB LEU A 178 17914 11279 25484 954 -452 -6164 C ATOM 1255 CG LEU A 178 -44.038 256.618 803.775 1.00151.08 C ANISOU 1255 CG LEU A 178 19204 11751 26449 952 -1254 -6215 C ATOM 1256 CD1 LEU A 178 -44.430 258.043 804.074 1.00147.30 C ANISOU 1256 CD1 LEU A 178 18861 11101 26006 523 -1807 -5486 C ATOM 1257 CD2 LEU A 178 -43.213 256.503 802.510 1.00154.78 C ANISOU 1257 CD2 LEU A 178 19518 12229 27063 1140 -1245 -6399 C ATOM 1258 N GLU A 179 -42.947 252.854 804.649 1.00147.59 N ANISOU 1258 N GLU A 179 18217 12056 25805 1852 674 -7801 N ATOM 1259 CA GLU A 179 -43.249 251.583 803.995 1.00155.55 C ANISOU 1259 CA GLU A 179 19344 12999 26759 2276 816 -8612 C ATOM 1260 CB GLU A 179 -43.451 250.414 804.965 1.00157.30 C ANISOU 1260 CB GLU A 179 19395 13608 26765 2374 1358 -8884 C ATOM 1261 CG GLU A 179 -44.059 250.752 806.284 1.00159.32 C ANISOU 1261 CG GLU A 179 19861 13720 26951 2205 1417 -8704 C ATOM 1262 CD GLU A 179 -43.039 251.311 807.209 1.00163.19 C ANISOU 1262 CD GLU A 179 19954 14559 27492 1931 1853 -8096 C ATOM 1263 OE1 GLU A 179 -42.799 250.725 808.283 1.00162.71 O ANISOU 1263 OE1 GLU A 179 19708 14780 27335 1944 2428 -8148 O ATOM 1264 OE2 GLU A 179 -42.452 252.333 806.832 1.00168.47 O ANISOU 1264 OE2 GLU A 179 20491 15222 28299 1708 1624 -7571 O ATOM 1265 C GLU A 179 -44.371 251.618 802.983 1.00164.70 C ANISOU 1265 C GLU A 179 20967 13711 27901 2410 110 -8955 C ATOM 1266 O GLU A 179 -44.266 250.974 801.949 1.00166.98 O ANISOU 1266 O GLU A 179 21159 14116 28168 2642 49 -9298 O ATOM 1267 N ASP A 180 -45.432 252.361 803.198 1.00169.67 N ANISOU 1267 N ASP A 180 21957 14039 28472 2193 -486 -8693 N ATOM 1268 CA ASP A 180 -46.382 252.280 802.137 1.00171.11 C ANISOU 1268 CA ASP A 180 22553 13816 28644 2366 -1106 -9081 C ATOM 1269 C ASP A 180 -45.308 252.583 801.138 1.00170.85 C ANISOU 1269 C ASP A 180 22264 13861 28792 2403 -1080 -8963 C ATOM 1270 O ASP A 180 -44.518 253.488 801.360 1.00176.58 O ANISOU 1270 O ASP A 180 22736 14737 29621 2119 -1031 -8346 O ATOM 1271 CB ASP A 180 -47.351 253.438 802.214 1.00170.41 C ANISOU 1271 CB ASP A 180 22827 13382 28539 2051 -1853 -8620 C ATOM 1272 CG ASP A 180 -47.690 253.806 803.622 1.00168.26 C ANISOU 1272 CG ASP A 180 22550 13221 28162 1769 -1723 -8209 C ATOM 1273 OD1 ASP A 180 -47.174 253.142 804.533 1.00160.79 O ANISOU 1273 OD1 ASP A 180 21322 12618 27152 1825 -1049 -8294 O ATOM 1274 OD2 ASP A 180 -48.463 254.758 803.819 1.00175.17 O ANISOU 1274 OD2 ASP A 180 23701 13839 29017 1489 -2296 -7800 O ATOM 1275 N GLY A 181 -45.222 251.842 800.051 1.00165.24 N ANISOU 1275 N GLY A 181 21534 13162 28088 2720 -1107 -9460 N ATOM 1276 CA GLY A 181 -44.132 252.148 799.167 1.00162.68 C ANISOU 1276 CA GLY A 181 20945 12929 27936 2740 -1047 -9322 C ATOM 1277 C GLY A 181 -44.473 253.596 799.067 1.00170.78 C ANISOU 1277 C GLY A 181 22211 13620 29057 2390 -1686 -8731 C ATOM 1278 O GLY A 181 -45.621 253.947 798.867 1.00173.08 O ANISOU 1278 O GLY A 181 22922 13554 29288 2332 -2298 -8760 O ATOM 1279 N GLY A 182 -43.497 254.455 799.266 1.00160.97 N ANISOU 1279 N GLY A 182 16971 13806 30385 440 1131 -8554 N ATOM 1280 CA GLY A 182 -43.783 255.868 799.232 1.00170.46 C ANISOU 1280 CA GLY A 182 18278 14524 31965 178 983 -8484 C ATOM 1281 C GLY A 182 -42.724 256.644 799.966 1.00171.60 C ANISOU 1281 C GLY A 182 18507 14973 31721 -112 977 -7955 C ATOM 1282 O GLY A 182 -41.917 256.081 800.701 1.00170.44 O ANISOU 1282 O GLY A 182 18345 15451 30963 -116 1084 -7746 O ATOM 1283 N LEU A 183 -42.756 257.954 799.782 1.00169.04 N ANISOU 1283 N LEU A 183 18262 14197 31770 -367 854 -7754 N ATOM 1284 CA LEU A 183 -41.743 258.820 800.311 1.00163.84 C ANISOU 1284 CA LEU A 183 17664 13739 30848 -646 850 -7228 C ATOM 1285 C LEU A 183 -42.284 260.223 800.461 1.00168.89 C ANISOU 1285 C LEU A 183 18323 13987 31861 -978 729 -7291 C ATOM 1286 O LEU A 183 -43.329 260.547 799.921 1.00178.12 O ANISOU 1286 O LEU A 183 19492 14613 33574 -981 629 -7649 O ATOM 1287 CB LEU A 183 -40.588 258.845 799.320 1.00156.73 C ANISOU 1287 CB LEU A 183 16846 12615 30090 -565 845 -6546 C ATOM 1288 CG LEU A 183 -40.965 259.409 797.950 1.00153.32 C ANISOU 1288 CG LEU A 183 16461 11383 30412 -528 709 -6382 C ATOM 1289 CD1 LEU A 183 -40.666 260.890 797.863 1.00150.52 C ANISOU 1289 CD1 LEU A 183 16170 10718 30303 -891 635 -5964 C ATOM 1290 CD2 LEU A 183 -40.237 258.688 796.869 1.00145.47 C ANISOU 1290 CD2 LEU A 183 15491 10261 29518 -244 699 -5970 C ATOM 1291 N LEU A 184 -41.558 261.053 801.196 1.00162.88 N ANISOU 1291 N LEU A 184 17563 13501 30822 -1261 740 -6945 N ATOM 1292 CA LEU A 184 -41.894 262.453 801.371 1.00159.81 C ANISOU 1292 CA LEU A 184 17156 12799 30765 -1617 640 -6916 C ATOM 1293 C LEU A 184 -40.596 263.214 801.143 1.00158.48 C ANISOU 1293 C LEU A 184 17024 12650 30540 -1797 685 -6167 C ATOM 1294 O LEU A 184 -39.532 262.647 801.274 1.00156.57 O ANISOU 1294 O LEU A 184 16812 12821 29858 -1671 788 -5806 O ATOM 1295 CB LEU A 184 -42.407 262.687 802.781 1.00155.11 C ANISOU 1295 CB LEU A 184 16462 12689 29785 -1787 620 -7339 C ATOM 1296 CG LEU A 184 -42.874 264.072 803.217 1.00157.62 C ANISOU 1296 CG LEU A 184 16707 12802 30378 -2165 505 -7424 C ATOM 1297 CD1 LEU A 184 -42.126 265.168 802.495 1.00161.22 C ANISOU 1297 CD1 LEU A 184 17189 12855 31213 -2400 503 -6800 C ATOM 1298 CD2 LEU A 184 -44.357 264.214 803.037 1.00159.26 C ANISOU 1298 CD2 LEU A 184 16899 12588 31025 -2192 375 -8071 C ATOM 1299 N GLY A 185 -40.668 264.482 800.777 1.00161.88 N ANISOU 1299 N GLY A 185 17450 12649 31407 -2094 619 -5927 N ATOM 1300 CA GLY A 185 -39.473 265.289 800.605 1.00161.06 C ANISOU 1300 CA GLY A 185 17367 12605 31225 -2295 689 -5231 C ATOM 1301 C GLY A 185 -39.287 266.234 801.777 1.00160.07 C ANISOU 1301 C GLY A 185 17113 12844 30861 -2625 714 -5243 C ATOM 1302 O GLY A 185 -40.243 266.875 802.215 1.00169.38 O ANISOU 1302 O GLY A 185 18200 13863 32292 -2832 615 -5648 O ATOM 1303 N LEU A 186 -38.032 266.482 802.140 1.00145.14 N ANISOU 1303 N LEU A 186 15209 11366 28573 -2699 836 -4749 N ATOM 1304 CA LEU A 186 -37.749 267.454 803.178 1.00131.21 C ANISOU 1304 CA LEU A 186 13290 9950 26615 -2985 870 -4697 C ATOM 1305 C LEU A 186 -37.079 268.726 802.726 1.00137.51 C ANISOU 1305 C LEU A 186 14057 10531 27661 -3296 942 -4145 C ATOM 1306 O LEU A 186 -35.938 268.716 802.303 1.00134.11 O ANISOU 1306 O LEU A 186 13706 10216 27035 -3260 1064 -3603 O ATOM 1307 CB LEU A 186 -36.936 266.810 804.259 1.00114.64 C ANISOU 1307 CB LEU A 186 11155 8590 23814 -2830 959 -4671 C ATOM 1308 CG LEU A 186 -37.820 265.651 804.654 1.00114.11 C ANISOU 1308 CG LEU A 186 11116 8673 23570 -2577 886 -5254 C ATOM 1309 CD1 LEU A 186 -37.961 265.593 806.145 1.00108.75 C ANISOU 1309 CD1 LEU A 186 10319 8581 22417 -2604 860 -5570 C ATOM 1310 CD2 LEU A 186 -39.179 265.872 804.033 1.00118.38 C ANISOU 1310 CD2 LEU A 186 11661 8622 24694 -2633 754 -5676 C ATOM 1311 N LYS A 187 -37.807 269.829 802.815 1.00149.40 N ANISOU 1311 N LYS A 187 15443 11729 29594 -3614 869 -4293 N ATOM 1312 CA LYS A 187 -37.243 271.134 802.552 1.00160.76 C ANISOU 1312 CA LYS A 187 16808 13021 31251 -3959 959 -3809 C ATOM 1313 CB LYS A 187 -37.944 271.818 801.401 1.00166.15 C ANISOU 1313 CB LYS A 187 17568 12909 32652 -4173 874 -3714 C ATOM 1314 CG LYS A 187 -37.459 271.295 800.095 1.00170.45 C ANISOU 1314 CG LYS A 187 18350 13086 33326 -3985 896 -3279 C ATOM 1315 CD LYS A 187 -36.041 270.779 800.240 1.00166.17 C ANISOU 1315 CD LYS A 187 17868 13091 32179 -3808 1060 -2833 C ATOM 1316 CE LYS A 187 -35.028 271.876 800.017 1.00164.31 C ANISOU 1316 CE LYS A 187 17608 12918 31903 -4102 1225 -2202 C ATOM 1317 NZ LYS A 187 -34.916 272.240 798.583 1.00162.39 N ANISOU 1317 NZ LYS A 187 17559 12048 32094 -4198 1205 -1712 N ATOM 1318 C LYS A 187 -37.325 271.978 803.806 1.00169.28 C ANISOU 1318 C LYS A 187 17635 14505 32178 -4198 966 -4004 C ATOM 1319 O LYS A 187 -36.832 273.102 803.851 1.00176.53 O ANISOU 1319 O LYS A 187 18430 15436 33209 -4495 1066 -3661 O ATOM 1320 N LYS A 188 -37.945 271.414 804.832 1.00164.99 N ANISOU 1320 N LYS A 188 17012 14309 31367 -4060 859 -4556 N ATOM 1321 CA LYS A 188 -38.109 272.110 806.107 1.00160.11 C ANISOU 1321 CA LYS A 188 16152 14093 30589 -4246 815 -4798 C ATOM 1322 C LYS A 188 -36.975 273.079 806.404 1.00160.35 C ANISOU 1322 C LYS A 188 16038 14410 30479 -4441 987 -4297 C ATOM 1323 O LYS A 188 -36.796 273.499 807.549 1.00157.06 O ANISOU 1323 O LYS A 188 15419 14448 29808 -4510 978 -4424 O ATOM 1324 CB LYS A 188 -38.227 271.094 807.245 1.00150.06 C ANISOU 1324 CB LYS A 188 14876 13395 28746 -3965 750 -5200 C ATOM 1325 N TYR A 204 -41.382 270.090 803.699 1.00135.06 N ANISOU 1325 N TYR A 204 13445 9352 28521 -3799 434 -5955 N ATOM 1326 CA TYR A 204 -42.281 268.988 803.398 1.00148.59 C ANISOU 1326 CA TYR A 204 15275 10896 30284 -3496 352 -6461 C ATOM 1327 CB TYR A 204 -43.509 269.046 804.307 1.00157.38 C ANISOU 1327 CB TYR A 204 16284 12128 31387 -3572 200 -7186 C ATOM 1328 CG TYR A 204 -44.382 270.280 804.144 1.00170.37 C ANISOU 1328 CG TYR A 204 17834 13252 33645 -3946 53 -7382 C ATOM 1329 CD2 TYR A 204 -44.169 271.421 804.904 1.00174.91 C ANISOU 1329 CD2 TYR A 204 18212 14033 34214 -4301 27 -7261 C ATOM 1330 CE2 TYR A 204 -44.974 272.556 804.747 1.00183.64 C ANISOU 1330 CE2 TYR A 204 19214 14656 35905 -4673 -110 -7443 C ATOM 1331 CZ TYR A 204 -46.001 272.555 803.821 1.00186.27 C ANISOU 1331 CZ TYR A 204 19667 14267 36841 -4684 -230 -7748 C ATOM 1332 OH TYR A 204 -46.789 273.676 803.666 1.00193.32 O ANISOU 1332 OH TYR A 204 20465 14658 38329 -5071 -374 -7927 O ATOM 1333 CE1 TYR A 204 -46.231 271.432 803.055 1.00184.19 C ANISOU 1333 CE1 TYR A 204 19607 13777 36601 -4306 -207 -7882 C ATOM 1334 CD1 TYR A 204 -45.424 270.304 803.220 1.00179.71 C ANISOU 1334 CD1 TYR A 204 19116 13723 35443 -3943 -63 -7697 C ATOM 1335 C TYR A 204 -42.708 269.062 801.941 1.00155.22 C ANISOU 1335 C TYR A 204 16260 10931 31784 -3466 300 -6355 C ATOM 1336 O TYR A 204 -43.642 269.769 801.620 1.00154.06 O ANISOU 1336 O TYR A 204 16092 10254 32189 -3677 172 -6609 O ATOM 1337 N LEU A 205 -42.015 268.348 801.059 1.00153.51 N ANISOU 1337 N LEU A 205 16191 10615 31522 -3203 383 -5970 N ATOM 1338 CA LEU A 205 -42.322 268.361 799.630 1.00159.94 C ANISOU 1338 CA LEU A 205 17142 10690 32937 -3114 318 -5794 C ATOM 1339 C LEU A 205 -42.650 266.986 799.110 1.00157.90 C ANISOU 1339 C LEU A 205 16976 10381 32638 -2662 305 -6073 C ATOM 1340 O LEU A 205 -41.934 266.040 799.380 1.00159.41 O ANISOU 1340 O LEU A 205 17180 11082 32305 -2409 411 -5961 O ATOM 1341 CB LEU A 205 -41.150 268.904 798.842 1.00163.35 C ANISOU 1341 CB LEU A 205 17656 10981 33429 -3222 408 -4976 C ATOM 1342 CG LEU A 205 -40.624 270.139 799.539 1.00170.68 C ANISOU 1342 CG LEU A 205 18454 12150 34247 -3644 484 -4689 C ATOM 1343 CD1 LEU A 205 -40.444 271.218 798.506 1.00172.51 C ANISOU 1343 CD1 LEU A 205 18758 11769 35019 -3934 476 -4161 C ATOM 1344 CD2 LEU A 205 -41.638 270.562 800.569 1.00174.62 C ANISOU 1344 CD2 LEU A 205 18787 12755 34807 -3845 384 -5319 C ATOM 1345 N LYS A 206 -43.724 266.872 798.349 1.00161.72 N ANISOU 1345 N LYS A 206 17513 10238 33694 -2561 178 -6442 N ATOM 1346 CA LYS A 206 -44.145 265.567 797.881 1.00162.65 C ANISOU 1346 CA LYS A 206 17678 10308 33812 -2122 174 -6787 C ATOM 1347 C LYS A 206 -44.024 265.292 796.383 1.00163.14 C ANISOU 1347 C LYS A 206 17860 9749 34377 -1888 110 -6451 C ATOM 1348 O LYS A 206 -44.195 266.179 795.557 1.00171.89 O ANISOU 1348 O LYS A 206 19045 10200 36067 -2071 3 -6172 O ATOM 1349 CB LYS A 206 -45.580 265.306 798.339 1.00163.52 C ANISOU 1349 CB LYS A 206 17736 10316 34078 -2077 89 -7653 C ATOM 1350 N SER A 207 -43.730 264.036 796.074 1.00140.99 N ANISOU 1350 N SER A 207 15063 7173 31335 -1484 169 -6481 N ATOM 1351 CA SER A 207 -43.645 263.496 794.722 1.00137.75 C ANISOU 1351 CA SER A 207 14732 6266 31340 -1168 94 -6247 C ATOM 1352 CB SER A 207 -42.416 262.601 794.576 1.00131.30 C ANISOU 1352 CB SER A 207 13923 5941 30023 -926 198 -5788 C ATOM 1353 OG SER A 207 -41.225 263.362 794.614 1.00134.84 O ANISOU 1353 OG SER A 207 14441 6564 30230 -1185 245 -5069 O ATOM 1354 C SER A 207 -44.925 262.727 794.396 1.00155.39 C ANISOU 1354 C SER A 207 16921 8172 33946 -860 27 -6985 C ATOM 1355 O SER A 207 -45.617 262.263 795.301 1.00122.90 O ANISOU 1355 O SER A 207 12718 4432 29546 -822 94 -7632 O ATOM 1356 N LEU A 208 -45.183 262.586 793.110 1.00169.57 N ANISOU 1356 N LEU A 208 18783 9293 36353 -636 -103 -6863 N ATOM 1357 CA LEU A 208 -46.402 261.996 792.614 1.00181.25 C ANISOU 1357 CA LEU A 208 20222 10326 38319 -337 -182 -7528 C ATOM 1358 CB LEU A 208 -46.648 262.577 791.225 1.00193.53 C ANISOU 1358 CB LEU A 208 21899 10930 40704 -299 -391 -7213 C ATOM 1359 CG LEU A 208 -47.980 262.239 790.581 1.00201.97 C ANISOU 1359 CG LEU A 208 22934 11423 42382 99 -500 -7770 C ATOM 1360 CD1 LEU A 208 -48.409 263.407 789.738 1.00206.21 C ANISOU 1360 CD1 LEU A 208 23438 11774 43140 -39 -519 -8586 C ATOM 1361 CD2 LEU A 208 -47.859 260.988 789.748 1.00206.83 C ANISOU 1361 CD2 LEU A 208 23685 11160 43742 179 -720 -7272 C ATOM 1362 C LEU A 208 -46.499 260.485 792.507 1.00183.56 C ANISOU 1362 C LEU A 208 20401 10957 38387 136 -85 -7889 C ATOM 1363 O LEU A 208 -45.981 259.880 791.574 1.00181.81 O ANISOU 1363 O LEU A 208 20178 10580 38320 437 -126 -7543 O ATOM 1364 N THR A 209 -47.179 259.894 793.486 1.00189.32 N ANISOU 1364 N THR A 209 21027 12163 38741 184 41 -8590 N ATOM 1365 CA THR A 209 -47.482 258.474 793.498 1.00193.04 C ANISOU 1365 CA THR A 209 21369 12973 39004 597 166 -9062 C ATOM 1366 C THR A 209 -48.579 258.111 794.507 1.00192.29 C ANISOU 1366 C THR A 209 21176 13263 38624 574 270 -9912 C ATOM 1367 O THR A 209 -48.295 257.479 795.518 1.00188.91 O ANISOU 1367 O THR A 209 20668 13633 37475 555 438 -10036 O ATOM 1368 CB THR A 209 -46.231 257.634 793.717 1.00189.49 C ANISOU 1368 CB THR A 209 20867 13200 37929 726 306 -8598 C ATOM 1369 OG1 THR A 209 -46.034 257.422 795.114 1.00181.60 O ANISOU 1369 OG1 THR A 209 19818 13019 36163 540 469 -8774 O ATOM 1370 CG2 THR A 209 -45.032 258.351 793.147 1.00189.14 C ANISOU 1370 CG2 THR A 209 20937 12982 37945 567 211 -7697 C ATOM 1371 N ARG A 210 -49.828 258.477 794.256 1.00194.88 N ANISOU 1371 N ARG A 210 21516 13043 39487 574 168 -10498 N ATOM 1372 CA ARG A 210 -50.861 258.104 795.214 1.00193.53 C ANISOU 1372 CA ARG A 210 21262 13275 38997 553 264 -11311 C ATOM 1373 C ARG A 210 -51.397 256.797 794.725 1.00197.08 C ANISOU 1373 C ARG A 210 21572 13782 39528 1011 378 -11800 C ATOM 1374 O ARG A 210 -52.130 256.747 793.754 1.00199.44 O ANISOU 1374 O ARG A 210 21861 13395 40522 1248 280 -12099 O ATOM 1375 CB ARG A 210 -51.994 259.120 795.233 1.00195.15 C ANISOU 1375 CB ARG A 210 21544 12887 39718 319 98 -11775 C ATOM 1376 N PHE A 211 -51.043 255.727 795.406 1.00193.60 N ANISOU 1376 N PHE A 211 21011 14159 38389 1134 590 -11890 N ATOM 1377 CA PHE A 211 -51.499 254.416 794.969 1.00191.94 C ANISOU 1377 CA PHE A 211 20630 14080 38220 1556 733 -12343 C ATOM 1378 CB PHE A 211 -50.347 253.411 795.010 1.00191.27 C ANISOU 1378 CB PHE A 211 20438 14611 37623 1714 886 -11864 C ATOM 1379 CG PHE A 211 -49.227 253.733 794.061 1.00200.76 C ANISOU 1379 CG PHE A 211 21704 15434 39142 1772 749 -11047 C ATOM 1380 CD1 PHE A 211 -49.300 253.364 792.729 1.00208.02 C ANISOU 1380 CD1 PHE A 211 22554 15767 40716 2137 651 -10978 C ATOM 1381 CE1 PHE A 211 -48.271 253.662 791.855 1.00210.40 C ANISOU 1381 CE1 PHE A 211 22934 15731 41278 2186 503 -10207 C ATOM 1382 CZ PHE A 211 -47.155 254.335 792.307 1.00209.36 C ANISOU 1382 CZ PHE A 211 22950 15855 40745 1864 479 -9522 C ATOM 1383 CE2 PHE A 211 -47.071 254.708 793.635 1.00205.35 C ANISOU 1383 CE2 PHE A 211 22492 15922 39608 1512 591 -9607 C ATOM 1384 CD2 PHE A 211 -48.103 254.409 794.504 1.00202.81 C ANISOU 1384 CD2 PHE A 211 22093 15928 39039 1470 711 -10353 C ATOM 1385 C PHE A 211 -52.655 253.916 795.820 1.00182.88 C ANISOU 1385 C PHE A 211 19409 13332 36744 1559 875 -13218 C ATOM 1386 O PHE A 211 -52.503 253.680 797.016 1.00190.23 O ANISOU 1386 O PHE A 211 20338 15019 36922 1362 1003 -13293 O ATOM 1387 N PHE A 212 -53.796 253.740 795.187 1.00165.01 N ANISOU 1387 N PHE A 212 17095 10557 35044 1794 846 -13870 N ATOM 1388 CA PHE A 212 -54.934 253.279 795.900 1.00169.32 C ANISOU 1388 CA PHE A 212 17586 11440 35309 1810 981 -14732 C ATOM 1389 CB PHE A 212 -56.013 254.290 795.758 1.00189.81 C ANISOU 1389 CB PHE A 212 20303 13355 38463 1662 787 -15210 C ATOM 1390 CG PHE A 212 -56.591 254.663 797.032 1.00197.22 C ANISOU 1390 CG PHE A 212 21315 14755 38864 1332 803 -15635 C ATOM 1391 CD2 PHE A 212 -57.857 255.201 797.110 1.00205.62 C ANISOU 1391 CD2 PHE A 212 22447 15406 40274 1245 691 -16360 C ATOM 1392 CE2 PHE A 212 -58.386 255.550 798.314 1.00208.20 C ANISOU 1392 CE2 PHE A 212 22842 16186 40077 933 679 -16751 C ATOM 1393 CZ PHE A 212 -57.642 255.364 799.463 1.00206.19 C ANISOU 1393 CZ PHE A 212 22589 16795 38959 718 777 -16396 C ATOM 1394 CE1 PHE A 212 -56.371 254.825 799.385 1.00190.48 C ANISOU 1394 CE1 PHE A 212 20537 15195 36644 808 897 -15672 C ATOM 1395 CD1 PHE A 212 -55.858 254.482 798.175 1.00186.52 C ANISOU 1395 CD1 PHE A 212 19967 14248 36655 1105 910 -15307 C ATOM 1396 C PHE A 212 -55.408 251.966 795.385 1.00165.89 C ANISOU 1396 C PHE A 212 16946 11129 34956 2245 1176 -15221 C ATOM 1397 O PHE A 212 -55.702 251.804 794.222 1.00161.41 O ANISOU 1397 O PHE A 212 16306 9915 35107 2569 1104 -15329 O ATOM 1398 N SER A 213 -55.508 251.024 796.295 1.00158.16 N ANISOU 1398 N SER A 213 15870 10997 33227 2242 1426 -15531 N ATOM 1399 CA SER A 213 -55.932 249.684 795.942 1.00159.46 C ANISOU 1399 CA SER A 213 15809 11416 33364 2621 1665 -16012 C ATOM 1400 C SER A 213 -57.441 249.567 795.993 1.00178.71 C ANISOU 1400 C SER A 213 18224 13661 36017 2733 1728 -17014 C ATOM 1401 O SER A 213 -58.067 249.877 797.005 1.00166.52 O ANISOU 1401 O SER A 213 16794 12447 34029 2465 1752 -17432 O ATOM 1402 CB SER A 213 -55.309 248.661 796.890 1.00154.20 C ANISOU 1402 CB SER A 213 15049 11769 31771 2543 1925 -15853 C ATOM 1403 OG SER A 213 -55.981 248.656 798.137 1.00160.58 O ANISOU 1403 OG SER A 213 15942 13134 31936 2291 2031 -16342 O ATOM 1404 N ARG A 214 -58.013 249.124 794.881 1.00195.71 N ANISOU 1404 N ARG A 214 20229 15267 38867 3143 1742 -17402 N ATOM 1405 CA ARG A 214 -59.429 248.805 794.802 1.00199.42 C ANISOU 1405 CA ARG A 214 20635 15565 39571 3334 1846 -18413 C ATOM 1406 C ARG A 214 -59.546 247.299 794.672 1.00200.82 C ANISOU 1406 C ARG A 214 20528 16287 39488 3680 2180 -18774 C ATOM 1407 O ARG A 214 -60.621 246.763 794.398 1.00212.76 O ANISOU 1407 O ARG A 214 21914 17685 41239 3949 2326 -19609 O ATOM 1408 CB ARG A 214 -60.098 249.514 793.623 1.00185.71 C ANISOU 1408 CB ARG A 214 18944 12711 38906 3547 1596 -18653 C ATOM 1409 N SER A 215 -58.416 246.626 794.869 1.00190.23 N ANISOU 1409 N SER A 215 19080 15536 37661 3661 2303 -18142 N ATOM 1410 CA SER A 215 -58.353 245.176 794.824 1.00194.78 C ANISOU 1410 CA SER A 215 19374 16713 37922 3925 2627 -18369 C ATOM 1411 C SER A 215 -57.335 244.606 795.803 1.00192.01 C ANISOU 1411 C SER A 215 19022 17293 36641 3659 2791 -17826 C ATOM 1412 O SER A 215 -57.377 243.414 796.115 1.00195.57 O ANISOU 1412 O SER A 215 19276 18402 36629 3757 3097 -18073 O ATOM 1413 CB SER A 215 -57.980 244.715 793.424 1.00207.18 C ANISOU 1413 CB SER A 215 20710 17763 40246 4370 2567 -18145 C ATOM 1414 OG SER A 215 -57.778 243.306 793.401 1.00217.13 O ANISOU 1414 OG SER A 215 21666 19651 41182 4594 2878 -18284 O ATOM 1415 N SER A 216 -56.415 245.455 796.258 1.00179.74 N ANISOU 1415 N SER A 216 17681 15771 34842 3326 2589 -17086 N ATOM 1416 CA SER A 216 -55.328 245.046 797.144 1.00169.60 C ANISOU 1416 CA SER A 216 16425 15273 32744 3069 2691 -16482 C ATOM 1417 C SER A 216 -54.107 245.933 796.948 1.00156.68 C ANISOU 1417 C SER A 216 14940 13363 31230 2893 2429 -15559 C ATOM 1418 O SER A 216 -52.971 245.460 796.983 1.00143.13 O ANISOU 1418 O SER A 216 13166 12011 29205 2868 2470 -14937 O ATOM 1419 CB SER A 216 -54.936 243.587 796.900 1.00174.30 C ANISOU 1419 CB SER A 216 16738 16377 33112 3307 2964 -16470 C ATOM 1420 OG SER A 216 -54.726 243.343 795.520 1.00179.64 O ANISOU 1420 OG SER A 216 17218 16475 34564 3697 2880 -16343 O ATOM 1421 N ASP A 219 -50.113 246.231 803.445 1.00185.94 N ANISOU 1421 N ASP A 219 19339 20546 30764 1126 2527 -13275 N ATOM 1422 CA ASP A 219 -48.873 246.561 802.780 1.00173.61 C ANISOU 1422 CA ASP A 219 17778 18709 29479 1161 2404 -12542 C ATOM 1423 C ASP A 219 -48.190 245.339 802.196 1.00168.48 C ANISOU 1423 C ASP A 219 16953 18275 28786 1363 2559 -12305 C ATOM 1424 O ASP A 219 -48.367 244.206 802.621 1.00163.68 O ANISOU 1424 O ASP A 219 16246 18204 27743 1385 2776 -12537 O ATOM 1425 CB ASP A 219 -47.948 247.294 803.720 1.00164.87 C ANISOU 1425 CB ASP A 219 16841 17865 27936 859 2275 -11967 C ATOM 1426 CG ASP A 219 -47.130 246.371 804.537 1.00166.01 C ANISOU 1426 CG ASP A 219 16983 18719 27375 754 2407 -11632 C ATOM 1427 OD1 ASP A 219 -46.655 246.786 805.601 1.00160.63 O ANISOU 1427 OD1 ASP A 219 16438 18385 26211 506 2336 -11342 O ATOM 1428 OD2 ASP A 219 -46.952 245.222 804.120 1.00170.34 O ANISOU 1428 OD2 ASP A 219 17387 19467 27868 917 2573 -11656 O ATOM 1429 N TYR A 220 -47.368 245.650 801.216 1.00165.02 N ANISOU 1429 N TYR A 220 16489 17400 28811 1488 2430 -11808 N ATOM 1430 CA TYR A 220 -46.648 244.753 800.322 1.00154.45 C ANISOU 1430 CA TYR A 220 14980 16049 27653 1718 2490 -11517 C ATOM 1431 C TYR A 220 -45.380 245.521 799.928 1.00171.51 C ANISOU 1431 C TYR A 220 17259 17938 29967 1646 2288 -10738 C ATOM 1432 O TYR A 220 -45.366 246.749 799.942 1.00181.23 O ANISOU 1432 O TYR A 220 18651 18786 31423 1517 2115 -10572 O ATOM 1433 CB TYR A 220 -47.483 244.507 799.075 1.00122.94 C ANISOU 1433 CB TYR A 220 10809 11503 24399 2078 2500 -11971 C ATOM 1434 CG TYR A 220 -47.753 243.065 798.759 1.00130.23 C ANISOU 1434 CG TYR A 220 11471 12749 25263 2314 2734 -12316 C ATOM 1435 CD1 TYR A 220 -48.516 242.286 799.600 1.00137.79 C ANISOU 1435 CD1 TYR A 220 12369 14261 25725 2243 2980 -12862 C ATOM 1436 CE1 TYR A 220 -48.777 240.961 799.309 1.00139.37 C ANISOU 1436 CE1 TYR A 220 12310 14770 25872 2446 3224 -13195 C ATOM 1437 CZ TYR A 220 -48.288 240.409 798.162 1.00129.50 C ANISOU 1437 CZ TYR A 220 10841 13266 25098 2738 3203 -12997 C ATOM 1438 OH TYR A 220 -48.548 239.100 797.877 1.00126.91 O ANISOU 1438 OH TYR A 220 10224 13257 24740 2939 3453 -13342 O ATOM 1439 CE2 TYR A 220 -47.542 241.165 797.309 1.00126.25 C ANISOU 1439 CE2 TYR A 220 10493 12295 25183 2827 2934 -12454 C ATOM 1440 CD2 TYR A 220 -47.277 242.484 797.608 1.00134.33 C ANISOU 1440 CD2 TYR A 220 11792 13018 26228 2609 2711 -12113 C ATOM 1441 N ASP A 221 -44.346 244.800 799.516 1.00165.34 N ANISOU 1441 N ASP A 221 16394 17334 29094 1732 2311 -10286 N ATOM 1442 CA ASP A 221 -43.099 245.398 799.038 1.00144.94 C ANISOU 1442 CA ASP A 221 13915 14515 26641 1696 2135 -9560 C ATOM 1443 C ASP A 221 -42.372 246.280 800.044 1.00155.06 C ANISOU 1443 C ASP A 221 15421 16026 27469 1363 2057 -9135 C ATOM 1444 O ASP A 221 -42.228 245.922 801.214 1.00165.62 O ANISOU 1444 O ASP A 221 16809 17952 28169 1155 2156 -9153 O ATOM 1445 CB ASP A 221 -43.333 246.187 797.754 1.00126.25 C ANISOU 1445 CB ASP A 221 11551 11332 25084 1906 1951 -9502 C ATOM 1446 CG ASP A 221 -43.593 247.626 798.006 1.00110.44 C ANISOU 1446 CG ASP A 221 9754 8945 23264 1706 1804 -9445 C ATOM 1447 OD1 ASP A 221 -42.735 248.441 797.683 1.00100.74 O ANISOU 1447 OD1 ASP A 221 8660 7446 22169 1620 1655 -8880 O ATOM 1448 OD2 ASP A 221 -44.673 247.967 798.489 1.00111.36 O ANISOU 1448 OD2 ASP A 221 9894 9007 23409 1631 1833 -9976 O ATOM 1449 N SER A 222 -41.925 247.444 799.582 1.00152.05 N ANISOU 1449 N SER A 222 15174 15165 27434 1316 1879 -8751 N ATOM 1450 CA SER A 222 -41.119 248.344 800.404 1.00134.13 C ANISOU 1450 CA SER A 222 13092 13069 24803 1028 1807 -8308 C ATOM 1451 C SER A 222 -39.810 248.722 799.697 1.00130.50 C ANISOU 1451 C SER A 222 12710 12390 24482 1051 1693 -7614 C ATOM 1452 O SER A 222 -39.439 248.124 798.693 1.00139.46 O ANISOU 1452 O SER A 222 13753 13348 25888 1278 1669 -7446 O ATOM 1453 CB SER A 222 -40.786 247.642 801.706 1.00116.60 C ANISOU 1453 CB SER A 222 10886 11603 21813 843 1932 -8301 C ATOM 1454 OG SER A 222 -40.359 248.571 802.649 1.00122.82 O ANISOU 1454 OG SER A 222 11832 12547 22289 583 1865 -8051 O ATOM 1455 N VAL A 223 -39.105 249.710 800.230 1.00120.08 N ANISOU 1455 N VAL A 223 11556 11099 22969 822 1624 -7220 N ATOM 1456 CA VAL A 223 -37.826 250.116 799.669 1.00114.68 C ANISOU 1456 CA VAL A 223 10971 10262 22341 817 1536 -6569 C ATOM 1457 C VAL A 223 -36.756 249.779 800.678 1.00115.21 C ANISOU 1457 C VAL A 223 11100 10954 21719 643 1604 -6241 C ATOM 1458 O VAL A 223 -36.864 250.159 801.830 1.00114.69 O ANISOU 1458 O VAL A 223 11095 11206 21275 432 1638 -6333 O ATOM 1459 CB VAL A 223 -37.758 251.598 799.450 1.00101.02 C ANISOU 1459 CB VAL A 223 9391 8044 20947 670 1413 -6337 C ATOM 1460 CG1 VAL A 223 -36.646 251.913 798.503 1.00 96.48 C ANISOU 1460 CG1 VAL A 223 8908 7176 20573 734 1318 -5723 C ATOM 1461 CG2 VAL A 223 -39.061 252.094 798.943 1.00 95.97 C ANISOU 1461 CG2 VAL A 223 8720 6855 20888 728 1346 -6786 C ATOM 1462 N ILE A 224 -35.730 249.044 800.267 1.00114.16 N ANISOU 1462 N ILE A 224 10953 10997 21425 732 1607 -5867 N ATOM 1463 CA ILE A 224 -34.681 248.692 801.212 1.00115.18 C ANISOU 1463 CA ILE A 224 11162 11684 20917 557 1653 -5556 C ATOM 1464 C ILE A 224 -33.253 249.187 800.944 1.00118.76 C ANISOU 1464 C ILE A 224 11755 12101 21269 506 1584 -4936 C ATOM 1465 O ILE A 224 -32.334 248.819 801.662 1.00117.31 O ANISOU 1465 O ILE A 224 11645 12350 20577 375 1610 -4685 O ATOM 1466 CB ILE A 224 -34.696 247.217 801.568 1.00103.85 C ANISOU 1466 CB ILE A 224 9623 10723 19112 588 1749 -5733 C ATOM 1467 CG1 ILE A 224 -35.980 246.882 802.291 1.00 92.28 C ANISOU 1467 CG1 ILE A 224 8074 9450 17540 549 1847 -6317 C ATOM 1468 CD1 ILE A 224 -35.782 245.841 803.338 1.00 82.02 C ANISOU 1468 CD1 ILE A 224 6779 8759 15625 411 1939 -6373 C ATOM 1469 CG2 ILE A 224 -33.593 246.924 802.528 1.00103.47 C ANISOU 1469 CG2 ILE A 224 9703 11163 18449 384 1756 -5384 C ATOM 1470 N SER A 225 -33.033 249.955 799.879 1.00112.03 N ANISOU 1470 N SER A 225 10954 10721 20893 609 1487 -4676 N ATOM 1471 CA SER A 225 -31.715 250.555 799.641 1.00 96.63 C ANISOU 1471 CA SER A 225 9156 8723 18836 549 1433 -4097 C ATOM 1472 C SER A 225 -31.707 251.653 798.597 1.00103.77 C ANISOU 1472 C SER A 225 10163 8979 20287 592 1316 -3838 C ATOM 1473 O SER A 225 -32.572 251.691 797.754 1.00 95.22 O ANISOU 1473 O SER A 225 9015 7439 19727 737 1244 -4039 O ATOM 1474 CB SER A 225 -30.695 249.538 799.242 1.00 77.23 C ANISOU 1474 CB SER A 225 6680 6521 16145 657 1416 -3800 C ATOM 1475 OG SER A 225 -29.822 250.160 798.343 1.00 65.40 O ANISOU 1475 OG SER A 225 5297 4694 14858 723 1315 -3314 O ATOM 1476 N CYS A 226 -30.709 252.527 798.624 1.00108.03 N ANISOU 1476 N CYS A 226 10852 9507 20688 426 1283 -3350 N ATOM 1477 CA CYS A 226 -30.614 253.602 797.633 1.00117.33 C ANISOU 1477 CA CYS A 226 12117 10164 22299 357 1157 -2980 C ATOM 1478 C CYS A 226 -29.249 254.221 797.464 1.00118.13 C ANISOU 1478 C CYS A 226 12367 10364 22154 216 1134 -2362 C ATOM 1479 O CYS A 226 -28.382 254.029 798.288 1.00121.85 O ANISOU 1479 O CYS A 226 12883 11303 22113 134 1223 -2244 O ATOM 1480 CB CYS A 226 -31.505 254.748 797.977 1.00117.98 C ANISOU 1480 CB CYS A 226 12214 9961 22650 154 1157 -3187 C ATOM 1481 SG CYS A 226 -30.768 256.155 797.335 1.00 80.00 S ANISOU 1481 SG CYS A 226 7555 4816 18025 -66 1083 -2569 S ATOM 1482 N LYS A 227 -29.066 254.955 796.372 1.00117.12 N ANISOU 1482 N LYS A 227 12327 9781 22394 191 1013 -1970 N ATOM 1483 CA LYS A 227 -27.843 255.713 796.101 1.00105.91 C ANISOU 1483 CA LYS A 227 11067 8404 20769 29 999 -1370 C ATOM 1484 C LYS A 227 -28.058 256.805 795.041 1.00123.71 C ANISOU 1484 C LYS A 227 13421 10071 23512 -74 884 -1029 C ATOM 1485 O LYS A 227 -29.048 256.788 794.330 1.00136.39 O ANISOU 1485 O LYS A 227 14976 11201 25647 40 776 -1217 O ATOM 1486 CB LYS A 227 -26.663 254.808 795.837 1.00 85.10 C ANISOU 1486 CB LYS A 227 8473 6100 17761 170 969 -1075 C ATOM 1487 CG LYS A 227 -26.172 254.189 797.116 1.00 87.69 C ANISOU 1487 CG LYS A 227 8767 7029 17523 136 1113 -1273 C ATOM 1488 CD LYS A 227 -24.684 253.965 797.107 1.00 81.04 C ANISOU 1488 CD LYS A 227 8043 6523 16227 115 1114 -845 C ATOM 1489 CE LYS A 227 -24.171 253.733 798.481 1.00 71.30 C ANISOU 1489 CE LYS A 227 6814 5813 14462 16 1260 -993 C ATOM 1490 NZ LYS A 227 -24.987 252.757 799.197 1.00 75.44 N ANISOU 1490 NZ LYS A 227 7197 6537 14929 124 1318 -1504 N ATOM 1491 N LEU A 228 -27.163 257.773 794.945 1.00118.01 N ANISOU 1491 N LEU A 228 12844 9370 22625 -297 915 -539 N ATOM 1492 CA LEU A 228 -27.416 258.902 794.033 1.00114.00 C ANISOU 1492 CA LEU A 228 12439 8308 22566 -451 830 -206 C ATOM 1493 C LEU A 228 -26.400 259.056 792.887 1.00121.90 C ANISOU 1493 C LEU A 228 13618 9163 23534 -430 712 441 C ATOM 1494 O LEU A 228 -25.230 259.365 793.119 1.00120.42 O ANISOU 1494 O LEU A 228 13541 9321 22891 -565 798 811 O ATOM 1495 CB LEU A 228 -27.537 260.215 794.822 1.00 88.74 C ANISOU 1495 CB LEU A 228 9247 5139 19332 -801 974 -203 C ATOM 1496 CG LEU A 228 -27.718 261.498 794.008 1.00 95.69 C ANISOU 1496 CG LEU A 228 10235 5491 20632 -1036 925 175 C ATOM 1497 CD1 LEU A 228 -28.675 262.462 794.692 1.00 76.80 C ANISOU 1497 CD1 LEU A 228 7743 2930 18510 -1291 1001 -147 C ATOM 1498 CD2 LEU A 228 -26.381 262.167 793.735 1.00 98.20 C ANISOU 1498 CD2 LEU A 228 10717 5989 20607 -1220 996 804 C ATOM 1499 N PHE A 229 -26.882 258.848 791.661 1.00126.86 N ANISOU 1499 N PHE A 229 14275 9272 24653 -254 508 558 N ATOM 1500 CA PHE A 229 -26.013 258.960 790.502 1.00128.79 C ANISOU 1500 CA PHE A 229 14698 9341 24894 -216 351 1175 C ATOM 1501 C PHE A 229 -25.774 260.343 789.994 1.00142.78 C ANISOU 1501 C PHE A 229 16657 10783 26809 -518 355 1676 C ATOM 1502 O PHE A 229 -26.689 261.147 789.844 1.00149.27 O ANISOU 1502 O PHE A 229 17473 11145 28097 -663 347 1586 O ATOM 1503 CB PHE A 229 -26.453 258.161 789.286 1.00113.07 C ANISOU 1503 CB PHE A 229 12677 6932 23353 115 89 1195 C ATOM 1504 CG PHE A 229 -25.590 258.433 788.094 1.00105.15 C ANISOU 1504 CG PHE A 229 11883 5717 22352 120 -101 1873 C ATOM 1505 CD1 PHE A 229 -25.027 257.426 787.371 1.00 99.13 C ANISOU 1505 CD1 PHE A 229 11114 5045 21507 401 -295 2044 C ATOM 1506 CE1 PHE A 229 -24.225 257.704 786.305 1.00102.18 C ANISOU 1506 CE1 PHE A 229 11707 5257 21858 394 -491 2675 C ATOM 1507 CZ PHE A 229 -23.957 258.982 785.962 1.00104.14 C ANISOU 1507 CZ PHE A 229 12183 5256 22128 94 -467 3154 C ATOM 1508 CE2 PHE A 229 -24.484 259.993 786.680 1.00110.64 C ANISOU 1508 CE2 PHE A 229 13002 5999 23039 -201 -249 2995 C ATOM 1509 CD2 PHE A 229 -25.288 259.727 787.747 1.00114.83 C ANISOU 1509 CD2 PHE A 229 13314 6696 23620 -186 -78 2355 C ATOM 1510 N HIS A 230 -24.510 260.609 789.725 1.00141.41 N ANISOU 1510 N HIS A 230 16656 10858 26214 -623 372 2209 N ATOM 1511 CA HIS A 230 -24.140 261.881 789.198 1.00136.83 C ANISOU 1511 CA HIS A 230 16272 10026 25693 -923 397 2744 C ATOM 1512 CB HIS A 230 -24.602 262.016 787.763 1.00129.87 C ANISOU 1512 CB HIS A 230 15515 8469 25363 -824 127 3072 C ATOM 1513 CG HIS A 230 -23.735 262.905 786.930 1.00123.90 C ANISOU 1513 CG HIS A 230 15028 7574 24473 -1048 88 3804 C ATOM 1514 ND1 HIS A 230 -23.430 264.192 787.296 1.00121.65 N ANISOU 1514 ND1 HIS A 230 14833 7349 24040 -1451 309 4064 N ATOM 1515 CE1 HIS A 230 -22.684 264.747 786.366 1.00116.52 C ANISOU 1515 CE1 HIS A 230 14437 6556 23279 -1587 233 4725 C ATOM 1516 NE2 HIS A 230 -22.495 263.865 785.408 1.00113.42 N ANISOU 1516 NE2 HIS A 230 14126 6004 22963 -1275 -58 4909 N ATOM 1517 CD2 HIS A 230 -23.145 262.706 785.733 1.00118.05 C ANISOU 1517 CD2 HIS A 230 14484 6636 23732 -932 -149 4335 C ATOM 1518 C HIS A 230 -24.802 262.860 790.136 1.00142.80 C ANISOU 1518 C HIS A 230 16924 10761 26571 -1216 609 2460 C ATOM 1519 O HIS A 230 -24.643 262.759 791.347 1.00149.60 O ANISOU 1519 O HIS A 230 17658 12106 27077 -1275 799 2128 O ATOM 1520 N GLU A 231 -25.545 263.807 789.592 1.00138.71 N ANISOU 1520 N GLU A 231 16458 9677 26568 -1403 560 2590 N ATOM 1521 CA GLU A 231 -26.188 264.792 790.432 1.00127.62 C ANISOU 1521 CA GLU A 231 14942 8231 25316 -1707 740 2332 C ATOM 1522 CB GLU A 231 -25.851 266.167 789.854 1.00113.33 C ANISOU 1522 CB GLU A 231 13301 6133 23626 -2079 800 2908 C ATOM 1523 CG GLU A 231 -24.892 266.977 790.670 1.00 98.29 C ANISOU 1523 CG GLU A 231 11391 4750 21203 -2385 1081 3110 C ATOM 1524 CD GLU A 231 -23.873 266.136 791.338 1.00 90.88 C ANISOU 1524 CD GLU A 231 10428 4487 19615 -2202 1169 3029 C ATOM 1525 OE1 GLU A 231 -23.692 265.005 790.892 1.00 86.91 O ANISOU 1525 OE1 GLU A 231 9967 4022 19032 -1875 996 2996 O ATOM 1526 OE2 GLU A 231 -23.262 266.594 792.310 1.00 82.71 O ANISOU 1526 OE2 GLU A 231 9321 3934 18171 -2380 1403 2986 O ATOM 1527 C GLU A 231 -27.696 264.768 790.682 1.00135.95 C ANISOU 1527 C GLU A 231 15834 8892 26930 -1664 677 1755 C ATOM 1528 O GLU A 231 -28.148 265.201 791.735 1.00141.92 O ANISOU 1528 O GLU A 231 16439 9837 27647 -1839 829 1376 O ATOM 1529 N ARG A 232 -28.462 264.269 789.720 1.00136.08 N ANISOU 1529 N ARG A 232 15876 8367 27461 -1424 445 1679 N ATOM 1530 CA ARG A 232 -29.930 264.298 789.719 1.00129.95 C ANISOU 1530 CA ARG A 232 14981 7103 27291 -1372 357 1164 C ATOM 1531 CB ARG A 232 -30.444 264.818 788.372 1.00121.12 C ANISOU 1531 CB ARG A 232 14018 5178 26825 -1391 139 1501 C ATOM 1532 C ARG A 232 -30.653 262.990 790.056 1.00132.12 C ANISOU 1532 C ARG A 232 15077 7505 27619 -997 298 517 C ATOM 1533 O ARG A 232 -31.780 263.015 790.553 1.00132.31 O ANISOU 1533 O ARG A 232 14967 7368 27938 -1001 314 -45 O ATOM 1534 N TYR A 233 -30.020 261.855 789.780 1.00131.84 N ANISOU 1534 N TYR A 233 15036 7761 27297 -685 234 586 N ATOM 1535 CA TYR A 233 -30.724 260.575 789.816 1.00125.31 C ANISOU 1535 CA TYR A 233 14040 6966 26604 -311 161 39 C ATOM 1536 C TYR A 233 -30.531 259.775 791.101 1.00134.41 C ANISOU 1536 C TYR A 233 15037 8825 27206 -247 345 -399 C ATOM 1537 O TYR A 233 -29.410 259.407 791.454 1.00131.50 O ANISOU 1537 O TYR A 233 14704 8979 26281 -246 424 -154 O ATOM 1538 CB TYR A 233 -30.323 259.718 788.613 1.00112.26 C ANISOU 1538 CB TYR A 233 12436 5127 25091 24 -59 335 C ATOM 1539 CG TYR A 233 -30.281 260.478 787.303 1.00 99.82 C ANISOU 1539 CG TYR A 233 11059 2896 23974 -35 -268 895 C ATOM 1540 CD1 TYR A 233 -29.118 261.102 786.882 1.00 99.83 C ANISOU 1540 CD1 TYR A 233 11273 2991 23668 -233 -280 1598 C ATOM 1541 CE1 TYR A 233 -29.073 261.795 785.691 1.00105.24 C ANISOU 1541 CE1 TYR A 233 12161 3085 24738 -306 -474 2143 C ATOM 1542 CZ TYR A 233 -30.199 261.870 784.903 1.00110.70 C ANISOU 1542 CZ TYR A 233 12844 3046 26173 -166 -675 1987 C ATOM 1543 OH TYR A 233 -30.145 262.560 783.718 1.00116.38 O ANISOU 1543 OH TYR A 233 13787 3150 27283 -243 -886 2563 O ATOM 1544 CE2 TYR A 233 -31.367 261.256 785.297 1.00110.80 C ANISOU 1544 CE2 TYR A 233 12635 2940 26525 48 -665 1259 C ATOM 1545 CD2 TYR A 233 -31.405 260.567 786.488 1.00105.40 C ANISOU 1545 CD2 TYR A 233 11752 2884 25413 106 -456 720 C ATOM 1546 N LEU A 234 -31.637 259.505 791.787 1.00141.63 N ANISOU 1546 N LEU A 234 15795 9741 28276 -199 404 -1048 N ATOM 1547 CA LEU A 234 -31.622 258.626 792.950 1.00143.35 C ANISOU 1547 CA LEU A 234 15871 10579 28015 -110 555 -1500 C ATOM 1548 CB LEU A 234 -32.510 259.183 794.064 1.00145.06 C ANISOU 1548 CB LEU A 234 16001 10880 28236 -321 673 -1996 C ATOM 1549 CG LEU A 234 -32.059 260.504 794.695 1.00156.11 C ANISOU 1549 CG LEU A 234 17468 12389 29459 -713 774 -1723 C ATOM 1550 CD1 LEU A 234 -33.102 261.014 795.677 1.00159.73 C ANISOU 1550 CD1 LEU A 234 17815 12856 30019 -894 834 -2259 C ATOM 1551 CD2 LEU A 234 -30.709 260.341 795.376 1.00156.62 C ANISOU 1551 CD2 LEU A 234 17571 13088 28850 -777 905 -1412 C ATOM 1552 C LEU A 234 -32.084 257.222 792.550 1.00152.34 C ANISOU 1552 C LEU A 234 16875 11725 29282 282 484 -1860 C ATOM 1553 O LEU A 234 -33.244 257.019 792.187 1.00163.68 O ANISOU 1553 O LEU A 234 18223 12760 31206 433 413 -2277 O ATOM 1554 N ILE A 235 -31.167 256.257 792.600 1.00143.87 N ANISOU 1554 N ILE A 235 15778 11104 27782 444 506 -1706 N ATOM 1555 CA ILE A 235 -31.481 254.877 792.239 1.00128.53 C ANISOU 1555 CA ILE A 235 13676 9235 25925 802 458 -2015 C ATOM 1556 C ILE A 235 -31.906 254.081 793.471 1.00126.07 C ANISOU 1556 C ILE A 235 13216 9445 25242 830 648 -2594 C ATOM 1557 O ILE A 235 -31.162 253.982 794.446 1.00109.26 O ANISOU 1557 O ILE A 235 11118 7857 22539 686 781 -2523 O ATOM 1558 CB ILE A 235 -30.286 254.185 791.569 1.00100.03 C ANISOU 1558 CB ILE A 235 10101 5824 22083 960 359 -1548 C ATOM 1559 CG1 ILE A 235 -29.737 255.060 790.443 1.00 90.49 C ANISOU 1559 CG1 ILE A 235 9084 4164 21134 886 173 -907 C ATOM 1560 CD1 ILE A 235 -28.285 254.829 790.141 1.00 78.85 C ANISOU 1560 CD1 ILE A 235 7725 3011 19222 879 117 -352 C ATOM 1561 CG2 ILE A 235 -30.701 252.819 791.050 1.00 93.40 C ANISOU 1561 CG2 ILE A 235 9057 4988 21444 1334 290 -1865 C ATOM 1562 N VAL A 236 -33.102 253.503 793.412 1.00130.18 N ANISOU 1562 N VAL A 236 13582 9794 26086 1021 659 -3167 N ATOM 1563 CA VAL A 236 -33.713 252.891 794.588 1.00121.43 C ANISOU 1563 CA VAL A 236 12355 9126 24656 1012 841 -3753 C ATOM 1564 C VAL A 236 -33.940 251.382 794.421 1.00132.67 C ANISOU 1564 C VAL A 236 13585 10792 26033 1327 893 -4093 C ATOM 1565 O VAL A 236 -34.031 250.878 793.305 1.00133.41 O ANISOU 1565 O VAL A 236 13590 10573 26527 1593 767 -4027 O ATOM 1566 CB VAL A 236 -35.030 253.610 794.936 1.00 97.31 C ANISOU 1566 CB VAL A 236 9289 5751 21933 896 859 -4231 C ATOM 1567 CG2 VAL A 236 -34.803 255.107 794.951 1.00 99.19 C ANISOU 1567 CG2 VAL A 236 9689 5703 22297 581 798 -3864 C ATOM 1568 CG1 VAL A 236 -35.556 253.157 796.275 1.00 85.27 C ANISOU 1568 CG1 VAL A 236 7689 4728 19980 825 1036 -4770 C ATOM 1569 N LEU A 237 -34.064 250.673 795.540 1.00131.66 N ANISOU 1569 N LEU A 237 13374 11232 25418 1280 1073 -4451 N ATOM 1570 CA LEU A 237 -34.282 249.232 795.548 1.00112.90 C ANISOU 1570 CA LEU A 237 10779 9227 22891 1472 1153 -4757 C ATOM 1571 CB LEU A 237 -33.096 248.547 796.157 1.00 78.39 C ANISOU 1571 CB LEU A 237 6426 5470 17890 1375 1224 -4462 C ATOM 1572 CG LEU A 237 -32.969 247.111 795.754 1.00 81.42 C ANISOU 1572 CG LEU A 237 6608 6111 18217 1575 1244 -4570 C ATOM 1573 CD1 LEU A 237 -32.427 246.366 796.904 1.00 80.94 C ANISOU 1573 CD1 LEU A 237 6557 6729 17467 1374 1380 -4587 C ATOM 1574 CD2 LEU A 237 -34.296 246.598 795.380 1.00 75.68 C ANISOU 1574 CD2 LEU A 237 5679 5181 17896 1772 1284 -5135 C ATOM 1575 C LEU A 237 -35.510 248.905 796.375 1.00121.94 C ANISOU 1575 C LEU A 237 11808 10582 23941 1420 1294 -5412 C ATOM 1576 O LEU A 237 -35.879 249.661 797.262 1.00139.40 O ANISOU 1576 O LEU A 237 14115 12869 25981 1193 1343 -5561 O ATOM 1577 N THR A 238 -36.130 247.772 796.085 1.00112.45 N ANISOU 1577 N THR A 238 10393 9490 22842 1629 1357 -5804 N ATOM 1578 CA THR A 238 -37.370 247.357 796.708 1.00123.38 C ANISOU 1578 CA THR A 238 11659 11047 24175 1621 1495 -6461 C ATOM 1579 C THR A 238 -37.271 246.114 797.531 1.00122.35 C ANISOU 1579 C THR A 238 11413 11600 23474 1563 1666 -6660 C ATOM 1580 O THR A 238 -36.371 245.314 797.381 1.00117.33 O ANISOU 1580 O THR A 238 10730 11249 22600 1597 1673 -6368 O ATOM 1581 CB THR A 238 -38.356 246.987 795.666 1.00123.64 C ANISOU 1581 CB THR A 238 11516 10622 24839 1932 1457 -6852 C ATOM 1582 OG1 THR A 238 -37.650 246.784 794.457 1.00116.97 O ANISOU 1582 OG1 THR A 238 10628 9463 24353 2161 1305 -6440 O ATOM 1583 CG2 THR A 238 -39.339 248.083 795.444 1.00124.64 C ANISOU 1583 CG2 THR A 238 11731 10167 25457 1912 1372 -7110 C ATOM 1584 N GLN A 239 -38.247 245.904 798.393 1.00125.77 N ANISOU 1584 N GLN A 239 11805 12290 23693 1468 1799 -7178 N ATOM 1585 CA GLN A 239 -38.193 244.749 799.264 1.00128.92 C ANISOU 1585 CA GLN A 239 12128 13340 23517 1372 1964 -7351 C ATOM 1586 C GLN A 239 -38.236 243.501 798.428 1.00131.65 C ANISOU 1586 C GLN A 239 12240 13719 24060 1630 2025 -7489 C ATOM 1587 O GLN A 239 -37.842 242.430 798.862 1.00134.29 O ANISOU 1587 O GLN A 239 12506 14545 23973 1569 2137 -7473 O ATOM 1588 CB GLN A 239 -39.294 244.780 800.311 1.00132.96 C ANISOU 1588 CB GLN A 239 12647 14107 23763 1232 2086 -7885 C ATOM 1589 CG GLN A 239 -39.357 243.555 801.208 1.00143.56 C ANISOU 1589 CG GLN A 239 13925 16103 24521 1130 2263 -8083 C ATOM 1590 CD GLN A 239 -38.007 243.097 801.756 1.00151.05 C ANISOU 1590 CD GLN A 239 14976 17472 24944 951 2245 -7546 C ATOM 1591 OE1 GLN A 239 -37.089 242.802 801.001 1.00159.41 O ANISOU 1591 OE1 GLN A 239 16006 18425 26135 1050 2175 -7167 O ATOM 1592 NE2 GLN A 239 -37.903 242.990 803.082 1.00143.27 N ANISOU 1592 NE2 GLN A 239 14114 16961 23361 695 2295 -7530 N ATOM 1593 N ASN A 240 -38.737 243.641 797.216 1.00130.56 N ANISOU 1593 N ASN A 240 11977 13035 24597 1922 1943 -7632 N ATOM 1594 CA ASN A 240 -38.892 242.488 796.311 1.00136.56 C ANISOU 1594 CA ASN A 240 12464 13771 25651 2222 1988 -7817 C ATOM 1595 C ASN A 240 -37.818 241.543 795.761 1.00133.52 C ANISOU 1595 C ASN A 240 11958 13588 25187 2325 1952 -7437 C ATOM 1596 O ASN A 240 -38.044 240.333 795.814 1.00132.04 O ANISOU 1596 O ASN A 240 11553 13747 24870 2406 2107 -7727 O ATOM 1597 CB ASN A 240 -39.708 242.914 795.111 1.00 95.14 C ANISOU 1597 CB ASN A 240 7112 7828 21209 2539 1872 -8058 C ATOM 1598 CG ASN A 240 -41.139 242.758 795.354 1.00 99.69 C ANISOU 1598 CG ASN A 240 7580 8358 21941 2615 2018 -8785 C ATOM 1599 ND2 ASN A 240 -41.913 242.711 794.303 1.00105.03 N ANISOU 1599 ND2 ASN A 240 8094 8510 23301 2943 1958 -9107 N ATOM 1600 OD1 ASN A 240 -41.554 242.659 796.487 1.00104.03 O ANISOU 1600 OD1 ASN A 240 8194 9341 21992 2387 2176 -9066 O ATOM 1601 N CYS A 241 -36.678 241.984 795.228 1.00135.73 N ANISOU 1601 N CYS A 241 12355 13686 25531 2327 1762 -6828 N ATOM 1602 CA CYS A 241 -36.148 243.320 795.127 1.00130.70 C ANISOU 1602 CA CYS A 241 11971 12701 24986 2216 1593 -6384 C ATOM 1603 C CYS A 241 -35.963 243.669 793.663 1.00133.01 C ANISOU 1603 C CYS A 241 12216 12375 25948 2513 1371 -6116 C ATOM 1604 O CYS A 241 -35.583 242.820 792.878 1.00118.67 O ANISOU 1604 O CYS A 241 10214 10570 24306 2736 1308 -6015 O ATOM 1605 CB CYS A 241 -34.747 243.180 795.587 1.00114.86 C ANISOU 1605 CB CYS A 241 10109 11085 22447 2014 1564 -5847 C ATOM 1606 SG CYS A 241 -34.210 241.869 794.621 1.00 94.47 S ANISOU 1606 SG CYS A 241 7277 8595 20025 2273 1517 -5745 S ATOM 1607 N HIS A 242 -36.166 244.944 793.337 1.00145.37 N ANISOU 1607 N HIS A 242 13963 13407 27863 2490 1236 -5961 N ATOM 1608 CA HIS A 242 -36.092 245.526 792.003 1.00144.77 C ANISOU 1608 CA HIS A 242 13917 12642 28446 2727 993 -5670 C ATOM 1609 C HIS A 242 -35.733 246.994 792.266 1.00153.13 C ANISOU 1609 C HIS A 242 15289 13424 29468 2474 907 -5288 C ATOM 1610 O HIS A 242 -35.717 247.445 793.403 1.00155.82 O ANISOU 1610 O HIS A 242 15757 14090 29358 2180 1038 -5357 O ATOM 1611 CB HIS A 242 -37.473 245.453 791.501 1.00129.52 C ANISOU 1611 CB HIS A 242 11831 10283 27098 2958 998 -6238 C ATOM 1612 CG HIS A 242 -38.425 245.619 792.614 1.00130.73 C ANISOU 1612 CG HIS A 242 12008 10678 26986 2756 1201 -6781 C ATOM 1613 ND1 HIS A 242 -38.429 244.772 793.694 1.00126.91 N ANISOU 1613 ND1 HIS A 242 11441 10900 25878 2599 1428 -7042 N ATOM 1614 CE1 HIS A 242 -39.307 245.205 794.570 1.00127.77 C ANISOU 1614 CE1 HIS A 242 11622 11094 25833 2422 1543 -7462 C ATOM 1615 NE2 HIS A 242 -39.867 246.299 794.095 1.00131.22 N ANISOU 1615 NE2 HIS A 242 12175 10901 26780 2450 1406 -7502 N ATOM 1616 CD2 HIS A 242 -39.306 246.597 792.888 1.00138.64 C ANISOU 1616 CD2 HIS A 242 13140 11331 28206 2642 1193 -7053 C ATOM 1617 N LEU A 243 -35.409 247.729 791.224 1.00148.55 N ANISOU 1617 N LEU A 243 14834 12257 29351 2578 680 -4861 N ATOM 1618 CA LEU A 243 -34.903 249.094 791.314 1.00135.61 C ANISOU 1618 CA LEU A 243 13487 10361 27677 2311 587 -4394 C ATOM 1619 C LEU A 243 -35.795 250.116 790.614 1.00146.88 C ANISOU 1619 C LEU A 243 15004 11044 29761 2313 436 -4447 C ATOM 1620 O LEU A 243 -36.424 249.818 789.597 1.00149.97 O ANISOU 1620 O LEU A 243 15276 10958 30746 2609 299 -4601 O ATOM 1621 CB LEU A 243 -33.459 249.192 790.814 1.00118.35 C ANISOU 1621 CB LEU A 243 11420 8278 25269 2265 442 -3664 C ATOM 1622 CG LEU A 243 -33.129 249.009 789.336 1.00 89.03 C ANISOU 1622 CG LEU A 243 7671 4128 22026 2529 169 -3280 C ATOM 1623 CD1 LEU A 243 -33.581 250.196 788.522 1.00113.18 C ANISOU 1623 CD1 LEU A 243 10899 6457 25646 2483 -23 -3050 C ATOM 1624 CD2 LEU A 243 -31.641 248.823 789.188 1.00 90.32 C ANISOU 1624 CD2 LEU A 243 7932 4632 21755 2460 86 -2674 C ATOM 1625 N LYS A 244 -35.840 251.321 791.179 1.00148.42 N ANISOU 1625 N LYS A 244 15398 11136 29859 1980 459 -4324 N ATOM 1626 CA LYS A 244 -36.629 252.423 790.635 1.00144.83 C ANISOU 1626 CA LYS A 244 15054 9985 29991 1900 324 -4339 C ATOM 1627 C LYS A 244 -35.753 253.670 790.482 1.00147.78 C ANISOU 1627 C LYS A 244 15672 10194 30283 1590 228 -3653 C ATOM 1628 O LYS A 244 -35.210 254.179 791.468 1.00147.95 O ANISOU 1628 O LYS A 244 15787 10627 29798 1288 361 -3517 O ATOM 1629 CB LYS A 244 -37.831 252.722 791.531 1.00136.08 C ANISOU 1629 CB LYS A 244 13911 8878 28915 1771 465 -5001 C ATOM 1630 CG LYS A 244 -38.878 251.619 791.555 1.00150.94 C ANISOU 1630 CG LYS A 244 15566 10823 30963 2077 563 -5726 C ATOM 1631 CD LYS A 244 -40.031 251.971 792.481 1.00164.22 C ANISOU 1631 CD LYS A 244 17245 12539 32612 1919 691 -6370 C ATOM 1632 CE LYS A 244 -41.088 250.879 792.487 1.00176.14 C ANISOU 1632 CE LYS A 244 18509 14185 34233 2187 802 -7082 C ATOM 1633 NZ LYS A 244 -42.212 251.200 793.409 1.00181.83 N ANISOU 1633 NZ LYS A 244 19228 15002 34856 2013 912 -7709 N ATOM 1634 N ILE A 245 -35.612 254.155 789.246 1.00143.42 N ANISOU 1634 N ILE A 245 15221 9047 30225 1666 -1 -3217 N ATOM 1635 CA ILE A 245 -34.729 255.293 788.961 1.00134.00 C ANISOU 1635 CA ILE A 245 14267 7696 28952 1377 -86 -2515 C ATOM 1636 C ILE A 245 -35.460 256.634 788.977 1.00135.57 C ANISOU 1636 C ILE A 245 14594 7372 29544 1096 -115 -2537 C ATOM 1637 O ILE A 245 -36.661 256.696 788.702 1.00120.91 O ANISOU 1637 O ILE A 245 12673 5038 28230 1203 -174 -2989 O ATOM 1638 CB ILE A 245 -33.994 255.130 787.622 1.00120.77 C ANISOU 1638 CB ILE A 245 12670 5712 27505 1568 -330 -1915 C ATOM 1639 CG1 ILE A 245 -33.054 253.934 787.690 1.00104.06 C ANISOU 1639 CG1 ILE A 245 10441 4177 24919 1769 -306 -1807 C ATOM 1640 CD1 ILE A 245 -31.847 254.078 786.812 1.00 98.69 C ANISOU 1640 CD1 ILE A 245 9918 3453 24127 1776 -496 -1062 C ATOM 1641 CG2 ILE A 245 -33.194 256.374 787.294 1.00101.29 C ANISOU 1641 CG2 ILE A 245 10468 3047 24968 1248 -403 -1208 C ATOM 1642 N TRP A 246 -34.725 257.701 789.290 1.00154.09 N ANISOU 1642 N TRP A 246 17113 9811 31623 731 -67 -2059 N ATOM 1643 CA TRP A 246 -35.332 259.019 789.463 1.00170.79 C ANISOU 1643 CA TRP A 246 19326 11521 34045 399 -61 -2070 C ATOM 1644 C TRP A 246 -34.590 260.226 788.882 1.00175.37 C ANISOU 1644 C TRP A 246 20127 11808 34698 102 -134 -1331 C ATOM 1645 O TRP A 246 -33.384 260.195 788.649 1.00176.04 O ANISOU 1645 O TRP A 246 20314 12174 34398 70 -134 -774 O ATOM 1646 CB TRP A 246 -35.637 259.272 790.936 1.00 99.28 C ANISOU 1646 CB TRP A 246 10186 2945 24591 158 155 -2513 C ATOM 1647 CG TRP A 246 -37.084 259.226 791.203 1.00102.47 C ANISOU 1647 CG TRP A 246 10480 3061 25392 211 151 -3220 C ATOM 1648 CD1 TRP A 246 -38.007 260.157 790.836 1.00107.57 C ANISOU 1648 CD1 TRP A 246 11182 3062 26629 55 49 -3346 C ATOM 1649 NE1 TRP A 246 -39.257 259.767 791.241 1.00116.50 N ANISOU 1649 NE1 TRP A 246 12186 4106 27975 172 72 -4104 N ATOM 1650 CE2 TRP A 246 -39.158 258.563 791.884 1.00108.96 C ANISOU 1650 CE2 TRP A 246 11091 3762 26548 401 205 -4465 C ATOM 1651 CZ2 TRP A 246 -40.145 257.773 792.469 1.00111.00 C ANISOU 1651 CZ2 TRP A 246 11199 4213 26762 573 293 -5224 C ATOM 1652 CH2 TRP A 246 -39.750 256.596 793.046 1.00105.22 C ANISOU 1652 CH2 TRP A 246 10353 4139 25487 761 438 -5399 C ATOM 1653 CZ3 TRP A 246 -38.408 256.200 793.052 1.00 97.45 C ANISOU 1653 CZ3 TRP A 246 9398 3594 24035 783 479 -4855 C ATOM 1654 CE3 TRP A 246 -37.429 256.982 792.471 1.00 96.99 C ANISOU 1654 CE3 TRP A 246 9491 3347 24014 627 383 -4131 C ATOM 1655 CD2 TRP A 246 -37.801 258.189 791.874 1.00106.17 C ANISOU 1655 CD2 TRP A 246 10775 3866 25700 428 252 -3917 C ATOM 1656 N ASP A 247 -35.354 261.285 788.624 1.00173.10 N ANISOU 1656 N ASP A 247 19914 10937 34919 -123 -196 -1347 N ATOM 1657 CA ASP A 247 -34.868 262.619 788.290 1.00174.50 C ANISOU 1657 CA ASP A 247 20282 10838 35183 -503 -211 -738 C ATOM 1658 C ASP A 247 -36.064 263.461 788.686 1.00185.76 C ANISOU 1658 C ASP A 247 21663 11866 37051 -743 -192 -1170 C ATOM 1659 O ASP A 247 -37.166 262.963 788.576 1.00194.02 O ANISOU 1659 O ASP A 247 22609 12607 38504 -521 -274 -1740 O ATOM 1660 CB ASP A 247 -34.575 262.753 786.800 1.00173.17 C ANISOU 1660 CB ASP A 247 20295 10078 35425 -384 -452 -148 C ATOM 1661 CG ASP A 247 -34.153 264.150 786.415 1.00171.75 C ANISOU 1661 CG ASP A 247 20325 9580 35351 -801 -456 485 C ATOM 1662 OD1 ASP A 247 -32.971 264.369 786.085 1.00163.04 O ANISOU 1662 OD1 ASP A 247 19371 8707 33870 -901 -441 1130 O ATOM 1663 OD2 ASP A 247 -35.025 265.035 786.432 1.00181.72 O ANISOU 1663 OD2 ASP A 247 21604 10356 37083 -1042 -470 328 O ATOM 1664 N LEU A 248 -35.906 264.694 789.169 1.00188.06 N ANISOU 1664 N LEU A 248 22006 12169 37278 -1187 -84 -957 N ATOM 1665 CA LEU A 248 -37.121 265.463 789.499 1.00191.46 C ANISOU 1665 CA LEU A 248 22378 12182 38185 -1414 -99 -1406 C ATOM 1666 C LEU A 248 -37.305 266.834 788.823 1.00190.63 C ANISOU 1666 C LEU A 248 22425 11414 38592 -1788 -180 -969 C ATOM 1667 O LEU A 248 -36.595 267.792 789.102 1.00183.51 O ANISOU 1667 O LEU A 248 21576 10702 37448 -2165 -52 -520 O ATOM 1668 CB LEU A 248 -37.299 265.600 791.018 1.00183.62 C ANISOU 1668 CB LEU A 248 21215 11800 36754 -1606 98 -1886 C ATOM 1669 CG LEU A 248 -36.861 266.905 791.679 1.00172.39 C ANISOU 1669 CG LEU A 248 19789 10561 35150 -2096 239 -1599 C ATOM 1670 CD1 LEU A 248 -37.516 267.081 793.026 1.00162.97 C ANISOU 1670 CD1 LEU A 248 18410 9732 33781 -2251 339 -2222 C ATOM 1671 CD2 LEU A 248 -35.362 266.958 791.803 1.00159.98 C ANISOU 1671 CD2 LEU A 248 18284 9528 32973 -2165 379 -990 C ATOM 1672 N THR A 249 -38.328 266.912 787.986 1.00198.22 N ANISOU 1672 N THR A 249 23441 11595 40279 -1684 -383 -1155 N ATOM 1673 CA THR A 249 -39.052 265.705 787.666 1.00206.45 C ANISOU 1673 CA THR A 249 24398 12489 41555 -1203 -506 -1685 C ATOM 1674 C THR A 249 -39.451 265.051 788.962 1.00211.77 C ANISOU 1674 C THR A 249 24859 13801 41803 -1120 -339 -2407 C ATOM 1675 O THR A 249 -39.080 263.922 789.211 1.00215.90 O ANISOU 1675 O THR A 249 25291 14825 41915 -803 -279 -2567 O ATOM 1676 CB THR A 249 -38.115 264.733 786.927 1.00203.57 C ANISOU 1676 CB THR A 249 24088 12318 40941 -835 -580 -1268 C ATOM 1677 OG1 THR A 249 -37.102 265.472 786.229 1.00204.41 O ANISOU 1677 OG1 THR A 249 24404 12290 40974 -1053 -623 -410 O ATOM 1678 CG2 THR A 249 -38.889 263.862 785.952 1.00205.13 C ANISOU 1678 CG2 THR A 249 24261 11971 41710 -375 -803 -1554 C ATOM 1679 N SER A 250 -40.197 265.746 789.804 1.00211.78 N ANISOU 1679 N SER A 250 24780 13800 41888 -1415 -271 -2833 N ATOM 1680 CA SER A 250 -40.452 265.254 791.151 1.00207.58 C ANISOU 1680 CA SER A 250 24068 13946 40856 -1398 -113 -3436 C ATOM 1681 C SER A 250 -41.063 263.876 791.270 1.00206.75 C ANISOU 1681 C SER A 250 23848 14022 40686 -953 -119 -4066 C ATOM 1682 O SER A 250 -40.714 263.154 792.184 1.00200.89 O ANISOU 1682 O SER A 250 23001 13992 39338 -858 29 -4288 O ATOM 1683 CB SER A 250 -41.302 266.237 791.938 1.00208.81 C ANISOU 1683 CB SER A 250 24155 13986 41198 -1775 -93 -3835 C ATOM 1684 OG SER A 250 -40.551 266.782 793.002 1.00203.03 O ANISOU 1684 OG SER A 250 23355 13887 39902 -2081 77 -3645 O ATOM 1685 N PHE A 251 -41.968 263.493 790.386 1.00211.58 N ANISOU 1685 N PHE A 251 24472 14011 41909 -683 -277 -4367 N ATOM 1686 CA PHE A 251 -42.539 262.154 790.477 1.00211.34 C ANISOU 1686 CA PHE A 251 24305 14183 41813 -253 -252 -4980 C ATOM 1687 C PHE A 251 -42.382 261.475 789.102 1.00215.01 C ANISOU 1687 C PHE A 251 24810 14195 42690 147 -413 -4714 C ATOM 1688 O PHE A 251 -43.350 261.308 788.368 1.00212.30 O ANISOU 1688 O PHE A 251 24456 13221 42986 366 -557 -5063 O ATOM 1689 CB PHE A 251 -44.008 262.216 790.954 1.00213.16 C ANISOU 1689 CB PHE A 251 24453 14182 42357 -269 -266 -5831 C ATOM 1690 CG PHE A 251 -44.939 263.038 790.047 1.00221.26 C ANISOU 1690 CG PHE A 251 25580 14243 44245 -367 -470 -5897 C ATOM 1691 CD1 PHE A 251 -45.582 262.445 788.967 1.00220.97 C ANISOU 1691 CD1 PHE A 251 25635 13907 44417 -838 -515 -5646 C ATOM 1692 CE1 PHE A 251 -46.421 263.188 788.147 1.00226.35 C ANISOU 1692 CE1 PHE A 251 26419 13688 45896 -951 -705 -5696 C ATOM 1693 CZ PHE A 251 -46.634 264.525 788.391 1.00232.11 C ANISOU 1693 CZ PHE A 251 27168 13792 47233 -569 -863 -6002 C ATOM 1694 CE2 PHE A 251 -46.023 265.128 789.450 1.00232.76 C ANISOU 1694 CE2 PHE A 251 27142 14167 47130 -80 -819 -6262 C ATOM 1695 CD2 PHE A 251 -45.178 264.392 790.279 1.00228.50 C ANISOU 1695 CD2 PHE A 251 26493 14544 45782 10 -619 -6205 C ATOM 1696 N THR A 252 -41.138 261.095 788.774 1.00219.26 N ANISOU 1696 N THR A 252 25389 15063 42855 241 -398 -4100 N ATOM 1697 CA THR A 252 -40.748 260.504 787.471 1.00224.42 C ANISOU 1697 CA THR A 252 26086 15363 43822 593 -578 -3712 C ATOM 1698 C THR A 252 -39.708 259.329 787.534 1.00176.14 C ANISOU 1698 C THR A 252 19879 9914 37131 866 -502 -3505 C ATOM 1699 O THR A 252 -38.839 259.365 788.392 1.00172.38 O ANISOU 1699 O THR A 252 19407 10101 35987 668 -335 -3301 O ATOM 1700 CB THR A 252 -40.159 261.630 786.608 1.00225.39 C ANISOU 1700 CB THR A 252 26441 14968 44230 336 -732 -2913 C ATOM 1701 OG1 THR A 252 -38.732 261.615 786.710 1.00223.11 O ANISOU 1701 OG1 THR A 252 26226 15212 43335 234 -658 -2260 O ATOM 1702 CG2 THR A 252 -40.667 262.977 787.110 1.00222.71 C ANISOU 1702 CG2 THR A 252 26181 14363 44077 -138 -689 -2966 C ATOM 1703 N LEU A 253 -39.790 258.309 786.655 1.00167.20 N ANISOU 1703 N LEU A 253 18653 8607 36266 1310 -630 -3567 N ATOM 1704 CA LEU A 253 -38.823 257.183 786.675 1.00159.75 C ANISOU 1704 CA LEU A 253 17605 8275 34818 1554 -575 -3381 C ATOM 1705 C LEU A 253 -38.689 256.195 785.468 1.00194.67 C ANISOU 1705 C LEU A 253 21931 12444 39591 2025 -776 -3255 C ATOM 1706 O LEU A 253 -39.654 255.986 784.749 1.00200.20 O ANISOU 1706 O LEU A 253 22556 12560 40949 2297 -916 -3596 O ATOM 1707 CB LEU A 253 -39.098 256.351 787.932 1.00158.49 C ANISOU 1707 CB LEU A 253 17253 8835 34131 1591 -316 -4019 C ATOM 1708 CG LEU A 253 -40.380 256.584 788.753 1.00156.00 C ANISOU 1708 CG LEU A 253 16867 8464 33942 1483 -195 -4779 C ATOM 1709 CD1 LEU A 253 -41.339 257.568 788.178 1.00154.73 C ANISOU 1709 CD1 LEU A 253 16811 7482 34499 1378 -354 -4889 C ATOM 1710 CD2 LEU A 253 -41.086 255.311 789.151 1.00154.49 C ANISOU 1710 CD2 LEU A 253 16444 8612 33643 1799 -58 -5511 C ATOM 1711 N ILE A 254 -37.577 255.491 785.263 1.00197.42 N ANISOU 1711 N ILE A 254 22246 13234 39532 2159 -797 -2849 N ATOM 1712 CA ILE A 254 -37.662 254.565 784.124 1.00210.18 C ANISOU 1712 CA ILE A 254 23725 14555 41578 2624 -1010 -2833 C ATOM 1713 C ILE A 254 -38.782 253.593 784.471 1.00216.25 C ANISOU 1713 C ILE A 254 24211 15417 42538 2921 -876 -3710 C ATOM 1714 O ILE A 254 -39.640 253.303 783.635 1.00225.24 O ANISOU 1714 O ILE A 254 25244 15987 44351 3248 -1030 -4005 O ATOM 1715 CB ILE A 254 -36.379 253.779 783.729 1.00151.78 C ANISOU 1715 CB ILE A 254 16290 7597 33785 2784 -1093 -2330 C ATOM 1716 CG1 ILE A 254 -35.303 254.732 783.215 1.00157.70 C ANISOU 1716 CG1 ILE A 254 16765 9082 34070 2959 -872 -2816 C ATOM 1717 CD1 ILE A 254 -33.935 254.082 783.058 1.00168.85 C ANISOU 1717 CD1 ILE A 254 18050 10778 35326 3239 -1006 -2495 C ATOM 1718 CG2 ILE A 254 -36.686 252.605 782.820 1.00146.73 C ANISOU 1718 CG2 ILE A 254 15923 7135 32693 2428 -1120 -1554 C ATOM 1719 N GLN A 255 -38.810 253.121 785.711 1.00205.20 N ANISOU 1719 N GLN A 255 22696 14716 40554 2806 -587 -4138 N ATOM 1720 CA GLN A 255 -39.914 252.249 786.127 1.00199.12 C ANISOU 1720 CA GLN A 255 21677 14076 39902 3044 -424 -4991 C ATOM 1721 C GLN A 255 -39.584 251.245 787.212 1.00175.12 C ANISOU 1721 C GLN A 255 18469 11919 36148 3037 -146 -5302 C ATOM 1722 O GLN A 255 -38.477 251.184 787.685 1.00164.99 O ANISOU 1722 O GLN A 255 17255 11156 34277 2858 -82 -4875 O ATOM 1723 CB GLN A 255 -40.591 251.557 784.918 1.00210.49 C ANISOU 1723 CB GLN A 255 22931 14972 42073 3530 -610 -5237 C ATOM 1724 CG GLN A 255 -42.144 251.615 784.950 1.00190.01 C ANISOU 1724 CG GLN A 255 20246 11932 40019 3664 -560 -6036 C ATOM 1725 CD GLN A 255 -42.834 250.510 784.147 1.00199.78 C ANISOU 1725 CD GLN A 255 21188 12939 41781 4194 -613 -6514 C ATOM 1726 OE1 GLN A 255 -42.271 249.965 783.199 1.00203.91 O ANISOU 1726 OE1 GLN A 255 21607 13341 42527 4489 -803 -6148 O ATOM 1727 NE2 GLN A 255 -44.068 250.189 784.524 1.00203.25 N ANISOU 1727 NE2 GLN A 255 21482 13322 42420 4320 -450 -7350 N ATOM 1728 N ASP A 256 -40.566 250.436 787.564 1.00175.58 N ANISOU 1728 N ASP A 256 18308 12123 36281 3242 18 -6056 N ATOM 1729 CA ASP A 256 -40.430 249.443 788.592 1.00177.81 C ANISOU 1729 CA ASP A 256 18428 13205 35925 3236 295 -6414 C ATOM 1730 C ASP A 256 -39.702 248.402 787.840 1.00184.88 C ANISOU 1730 C ASP A 256 19137 14266 36842 3544 217 -6149 C ATOM 1731 O ASP A 256 -40.242 247.349 787.542 1.00196.71 O ANISOU 1731 O ASP A 256 20347 15867 38525 3849 280 -6595 O ATOM 1732 CB ASP A 256 -41.800 248.855 788.857 1.00191.50 C ANISOU 1732 CB ASP A 256 19950 14960 37853 3398 449 -7272 C ATOM 1733 CG ASP A 256 -42.386 248.178 787.607 1.00206.37 C ANISOU 1733 CG ASP A 256 21608 16351 40453 3871 315 -7514 C ATOM 1734 OD1 ASP A 256 -42.720 248.889 786.638 1.00211.22 O ANISOU 1734 OD1 ASP A 256 22335 16160 41760 3996 70 -7361 O ATOM 1735 OD2 ASP A 256 -42.503 246.934 787.578 1.00208.76 O ANISOU 1735 OD2 ASP A 256 21615 17057 40646 4117 447 -7845 O ATOM 1736 N TYR A 257 -38.461 248.690 787.513 1.00182.60 N ANISOU 1736 N TYR A 257 18988 14048 36343 3434 70 -5412 N ATOM 1737 CA TYR A 257 -37.724 247.757 786.689 1.00187.26 C ANISOU 1737 CA TYR A 257 19408 14749 36994 3726 -61 -5115 C ATOM 1738 C TYR A 257 -37.909 246.975 787.969 1.00192.28 C ANISOU 1738 C TYR A 257 19900 16138 37020 3607 274 -5616 C ATOM 1739 O TYR A 257 -37.860 247.528 789.056 1.00192.03 O ANISOU 1739 O TYR A 257 20031 16412 36519 3264 431 -5658 O ATOM 1740 CB TYR A 257 -36.230 247.966 786.860 1.00178.15 C ANISOU 1740 CB TYR A 257 18428 13974 35289 3496 -120 -4395 C ATOM 1741 CG TYR A 257 -35.486 248.605 785.719 1.00172.96 C ANISOU 1741 CG TYR A 257 17947 12847 34924 3523 -446 -3667 C ATOM 1742 CD1 TYR A 257 -35.575 249.957 785.480 1.00174.02 C ANISOU 1742 CD1 TYR A 257 18364 12473 35282 3289 -568 -3331 C ATOM 1743 CE1 TYR A 257 -34.873 250.544 784.457 1.00171.26 C ANISOU 1743 CE1 TYR A 257 18201 11721 35149 3287 -855 -2635 C ATOM 1744 CZ TYR A 257 -34.051 249.782 783.673 1.00165.90 C ANISOU 1744 CZ TYR A 257 17429 11158 34448 3529 -1046 -2271 C ATOM 1745 OH TYR A 257 -33.340 250.366 782.654 1.00162.80 O ANISOU 1745 OH TYR A 257 17245 10384 34229 3520 -1348 -1560 O ATOM 1746 CE2 TYR A 257 -33.935 248.438 783.902 1.00162.29 C ANISOU 1746 CE2 TYR A 257 16671 11205 33786 3764 -941 -2608 C ATOM 1747 CD2 TYR A 257 -34.642 247.861 784.926 1.00164.69 C ANISOU 1747 CD2 TYR A 257 16790 11905 33879 3751 -630 -3294 C ATOM 1748 N ASP A 258 -38.163 245.684 787.858 1.00195.79 N ANISOU 1748 N ASP A 258 20023 16912 37456 3855 376 -5992 N ATOM 1749 CA ASP A 258 -38.347 244.913 789.069 1.00193.37 C ANISOU 1749 CA ASP A 258 19591 17353 36527 3682 686 -6422 C ATOM 1750 C ASP A 258 -37.296 244.099 788.364 1.00199.94 C ANISOU 1750 C ASP A 258 20281 18361 37325 3867 558 -5992 C ATOM 1751 O ASP A 258 -37.488 242.936 788.000 1.00199.97 O ANISOU 1751 O ASP A 258 19968 18560 37450 4121 608 -6271 O ATOM 1752 CB ASP A 258 -39.755 244.442 788.741 1.00187.97 C ANISOU 1752 CB ASP A 258 18669 16409 36343 3956 765 -7153 C ATOM 1753 CG ASP A 258 -40.747 244.796 789.830 1.00174.74 C ANISOU 1753 CG ASP A 258 17068 14902 34421 3724 985 -7715 C ATOM 1754 OD1 ASP A 258 -40.692 245.925 790.350 1.00156.80 O ANISOU 1754 OD1 ASP A 258 15074 12488 32013 3434 948 -7532 O ATOM 1755 OD2 ASP A 258 -41.579 243.939 790.173 1.00177.30 O ANISOU 1755 OD2 ASP A 258 17168 15520 34677 3825 1195 -8343 O ATOM 1756 N MSE A 259 -36.166 244.768 788.176 1.00201.62 N ANISOU 1756 N MSE A 259 20736 18501 37369 3725 387 -5304 N ATOM 1757 CA MSE A 259 -35.001 244.195 787.533 1.00195.56 C ANISOU 1757 CA MSE A 259 19902 17890 36512 3850 220 -4796 C ATOM 1758 C MSE A 259 -35.382 243.646 786.152 1.00189.79 C ANISOU 1758 C MSE A 259 18918 16689 36505 4303 -7 -4858 C ATOM 1759 O MSE A 259 -36.048 244.360 785.412 1.00187.44 O ANISOU 1759 O MSE A 259 18701 15695 36824 4460 -179 -4876 O ATOM 1760 CB MSE A 259 -34.311 243.236 788.501 1.00190.41 C ANISOU 1760 CB MSE A 259 19152 18067 35128 3658 437 -4840 C ATOM 1761 CG MSE A 259 -33.522 243.963 789.613 1.00181.94 C ANISOU 1761 CG MSE A 259 18390 17352 33387 3241 542 -4521 C ATOM 1762 SE MSE A 259 -32.240 245.244 788.902 1.00138.16 Se ANISOU 1762 SE MSE A 259 13202 11394 27897 3163 242 -3621 Se ATOM 1763 CE MSE A 259 -31.390 244.180 787.546 1.00199.63 C ANISOU 1763 CE MSE A 259 20763 19155 35934 3523 -40 -3255 C ATOM 1764 N VAL A 260 -35.010 242.431 785.761 1.00183.25 N ANISOU 1764 N VAL A 260 17785 16178 35662 4519 -29 -4894 N ATOM 1765 CA VAL A 260 -34.226 241.452 786.504 1.00170.63 C ANISOU 1765 CA VAL A 260 16067 15357 33406 4351 149 -4875 C ATOM 1766 C VAL A 260 -35.052 240.617 787.469 1.00167.43 C ANISOU 1766 C VAL A 260 15457 15442 32715 4262 505 -5560 C ATOM 1767 O VAL A 260 -34.531 239.740 788.155 1.00144.99 O ANISOU 1767 O VAL A 260 12520 13236 29333 4098 677 -5597 O ATOM 1768 CB VAL A 260 -32.968 242.001 787.120 1.00156.57 C ANISOU 1768 CB VAL A 260 14600 13889 31001 4006 131 -4304 C ATOM 1769 CG1 VAL A 260 -32.275 240.909 787.880 1.00148.17 C ANISOU 1769 CG1 VAL A 260 13406 13577 29316 3843 310 -4351 C ATOM 1770 CG2 VAL A 260 -32.097 242.585 786.049 1.00159.03 C ANISOU 1770 CG2 VAL A 260 15068 13782 31574 4131 -225 -3631 C ATOM 1771 N SER A 261 -36.346 240.909 787.504 1.00183.86 N ANISOU 1771 N SER A 261 17492 17204 35164 4360 606 -6094 N ATOM 1772 CA SER A 261 -37.284 240.165 788.315 1.00186.25 C ANISOU 1772 CA SER A 261 17603 17909 35253 4310 932 -6786 C ATOM 1773 C SER A 261 -37.389 238.776 787.642 1.00178.31 C ANISOU 1773 C SER A 261 16160 17080 34509 4639 961 -7046 C ATOM 1774 O SER A 261 -37.486 237.752 788.302 1.00178.79 O ANISOU 1774 O SER A 261 16030 17729 34175 4545 1223 -7373 O ATOM 1775 CB SER A 261 -38.623 240.886 788.404 1.00190.31 C ANISOU 1775 CB SER A 261 18183 17983 36141 4356 995 -7288 C ATOM 1776 OG SER A 261 -38.661 241.715 789.548 1.00181.99 O ANISOU 1776 OG SER A 261 17435 17121 34593 3964 1118 -7270 O ATOM 1777 N GLN A 262 -37.366 238.792 786.308 1.00166.62 N ANISOU 1777 N GLN A 262 14531 15060 33717 5022 674 -6875 N ATOM 1778 CA GLN A 262 -37.438 237.644 785.409 1.00168.38 C ANISOU 1778 CA GLN A 262 14316 15302 34359 5408 612 -7053 C ATOM 1779 C GLN A 262 -36.040 237.146 785.073 1.00173.21 C ANISOU 1779 C GLN A 262 14882 16205 34724 5380 425 -6455 C ATOM 1780 O GLN A 262 -35.816 235.945 784.904 1.00172.93 O ANISOU 1780 O GLN A 262 14493 16555 34656 5505 494 -6600 O ATOM 1781 CB GLN A 262 -38.163 237.989 784.107 1.00159.55 C ANISOU 1781 CB GLN A 262 13072 13383 34166 5862 345 -7163 C ATOM 1782 CG GLN A 262 -37.685 237.137 782.936 1.00157.43 C ANISOU 1782 CG GLN A 262 12447 13024 34346 6253 95 -6969 C ATOM 1783 CD GLN A 262 -38.454 237.377 781.648 1.00169.91 C ANISOU 1783 CD GLN A 262 13873 13806 36879 6740 -182 -7111 C ATOM 1784 OE1 GLN A 262 -39.658 237.630 781.663 1.00181.81 O ANISOU 1784 OE1 GLN A 262 15347 14968 38764 6873 -60 -7669 O ATOM 1785 NE2 GLN A 262 -37.758 237.279 780.519 1.00162.70 N ANISOU 1785 NE2 GLN A 262 12867 12587 36363 7016 -574 -6609 N ATOM 1786 N SER A 263 -35.104 238.074 785.002 1.00179.52 N ANISOU 1786 N SER A 263 16038 16835 35337 5202 200 -5800 N ATOM 1787 CA SER A 263 -33.750 237.709 784.664 1.00184.77 C ANISOU 1787 CA SER A 263 16701 17747 35758 5169 -4 -5220 C ATOM 1788 C SER A 263 -33.235 236.653 785.620 1.00183.78 C ANISOU 1788 C SER A 263 16450 18416 34964 4910 269 -5356 C ATOM 1789 O SER A 263 -33.395 236.733 786.822 1.00178.95 O ANISOU 1789 O SER A 263 16004 18185 33803 4573 557 -5557 O ATOM 1790 CB SER A 263 -32.863 238.944 784.662 1.00178.80 C ANISOU 1790 CB SER A 263 16393 16757 34785 4952 -216 -4546 C ATOM 1791 OG SER A 263 -33.465 239.953 783.872 1.00185.24 O ANISOU 1791 OG SER A 263 17357 16815 36212 5144 -434 -4453 O ATOM 1792 N ASP A 264 -32.604 235.661 785.018 1.00183.99 N ANISOU 1792 N ASP A 264 16179 18655 35076 5081 141 -5220 N ATOM 1793 CA ASP A 264 -32.034 234.494 785.672 1.00172.01 C ANISOU 1793 CA ASP A 264 14482 17833 33039 4887 342 -5310 C ATOM 1794 C ASP A 264 -32.957 233.523 786.415 1.00185.60 C ANISOU 1794 C ASP A 264 15936 19975 34610 4833 748 -6000 C ATOM 1795 O ASP A 264 -33.972 233.068 785.891 1.00184.46 O ANISOU 1795 O ASP A 264 15449 19648 34990 5151 821 -6496 O ATOM 1796 CB ASP A 264 -30.839 234.826 786.537 1.00131.71 C ANISOU 1796 CB ASP A 264 9748 13105 27192 4465 357 -4837 C ATOM 1797 CG ASP A 264 -29.936 233.673 786.652 1.00113.34 C ANISOU 1797 CG ASP A 264 7225 11298 24539 4377 371 -4721 C ATOM 1798 OD1 ASP A 264 -30.324 232.635 786.122 1.00114.69 O ANISOU 1798 OD1 ASP A 264 6958 11561 25056 4626 402 -5040 O ATOM 1799 OD2 ASP A 264 -28.861 233.776 787.236 1.00 93.66 O ANISOU 1799 OD2 ASP A 264 4992 9110 21484 4074 352 -4338 O ATOM 1800 N SER A 265 -32.595 233.205 787.647 1.00191.28 N ANISOU 1800 N SER A 265 16820 21255 34602 4429 1008 -6028 N ATOM 1801 CA SER A 265 -33.355 232.246 788.410 1.00194.06 C ANISOU 1801 CA SER A 265 16953 22060 34722 4334 1388 -6613 C ATOM 1802 C SER A 265 -34.785 232.631 788.480 1.00187.47 C ANISOU 1802 C SER A 265 16072 20951 34207 4477 1556 -7175 C ATOM 1803 O SER A 265 -35.139 233.764 788.745 1.00176.58 O ANISOU 1803 O SER A 265 15012 19253 32829 4388 1512 -7128 O ATOM 1804 CB SER A 265 -32.781 232.103 789.820 1.00196.62 C ANISOU 1804 CB SER A 265 17577 22938 34193 3847 1602 -6493 C ATOM 1805 OG SER A 265 -32.897 233.317 790.544 1.00198.38 O ANISOU 1805 OG SER A 265 18236 23005 34136 3611 1606 -6361 O ATOM 1806 N ASP A 266 -35.600 231.605 788.352 1.00192.18 N ANISOU 1806 N ASP A 266 16258 21745 35016 4665 1787 -7745 N ATOM 1807 CA ASP A 266 -37.015 231.700 788.493 1.00194.38 C ANISOU 1807 CA ASP A 266 16431 21876 35549 4803 2010 -8397 C ATOM 1808 C ASP A 266 -37.182 231.153 789.901 1.00191.38 C ANISOU 1808 C ASP A 266 16152 22154 34411 4403 2386 -8657 C ATOM 1809 O ASP A 266 -36.808 230.023 790.159 1.00195.40 O ANISOU 1809 O ASP A 266 16436 23166 34640 4311 2553 -8710 O ATOM 1810 CB ASP A 266 -37.657 230.745 787.499 1.00197.02 C ANISOU 1810 CB ASP A 266 16213 22113 36532 5254 2050 -8845 C ATOM 1811 CG ASP A 266 -36.626 230.012 786.647 1.00193.95 C ANISOU 1811 CG ASP A 266 15540 21803 36350 5422 1817 -8450 C ATOM 1812 OD1 ASP A 266 -36.871 229.808 785.442 1.00197.48 O ANISOU 1812 OD1 ASP A 266 15646 21861 37526 5871 1611 -8531 O ATOM 1813 OD2 ASP A 266 -35.567 229.627 787.182 1.00187.16 O ANISOU 1813 OD2 ASP A 266 14793 21386 34933 5112 1824 -8065 O ATOM 1814 N PRO A 267 -37.717 231.922 790.830 1.00181.33 N ANISOU 1814 N PRO A 267 15213 20890 32794 4154 2508 -8801 N ATOM 1815 CA PRO A 267 -37.868 231.375 792.169 1.00172.56 C ANISOU 1815 CA PRO A 267 14205 20403 30956 3784 2833 -9017 C ATOM 1816 C PRO A 267 -38.084 229.879 792.075 1.00171.78 C ANISOU 1816 C PRO A 267 13665 20758 30848 3881 3098 -9391 C ATOM 1817 O PRO A 267 -37.164 229.097 792.231 1.00165.34 O ANISOU 1817 O PRO A 267 12775 20316 29729 3733 3110 -9102 O ATOM 1818 CB PRO A 267 -39.147 232.039 792.663 1.00175.79 C ANISOU 1818 CB PRO A 267 14743 20658 31390 3769 2984 -9521 C ATOM 1819 CG PRO A 267 -39.262 233.264 791.891 1.00176.88 C ANISOU 1819 CG PRO A 267 15034 20104 32070 3967 2687 -9333 C ATOM 1820 CD PRO A 267 -38.738 232.937 790.545 1.00182.78 C ANISOU 1820 CD PRO A 267 15504 20528 33414 4326 2448 -9087 C ATOM 1821 N VAL A 276 -34.044 245.914 805.579 1.00 74.46 N ANISOU 1821 N VAL A 276 6128 8589 13573 -37 1873 -5738 N ATOM 1822 CA VAL A 276 -33.321 247.103 805.128 1.00 82.88 C ANISOU 1822 CA VAL A 276 7283 9330 14877 -40 1781 -5370 C ATOM 1823 C VAL A 276 -31.818 246.973 805.377 1.00 91.83 C ANISOU 1823 C VAL A 276 8576 10652 15665 -145 1715 -4846 C ATOM 1824 O VAL A 276 -31.380 246.723 806.501 1.00 87.95 O ANISOU 1824 O VAL A 276 8195 10527 14695 -314 1690 -4741 O ATOM 1825 CB VAL A 276 -33.861 248.393 805.784 1.00 88.63 C ANISOU 1825 CB VAL A 276 8046 9958 15671 -149 1752 -5500 C ATOM 1826 CG1 VAL A 276 -33.162 249.616 805.207 1.00 98.27 C ANISOU 1826 CG1 VAL A 276 9342 10808 17186 -147 1688 -5139 C ATOM 1827 CG2 VAL A 276 -35.369 248.504 805.590 1.00 77.56 C ANISOU 1827 CG2 VAL A 276 6526 8355 14587 -64 1795 -6062 C ATOM 1828 N GLY A 277 -31.033 247.136 804.317 1.00101.76 N ANISOU 1828 N GLY A 277 9858 11634 17171 -32 1672 -4521 N ATOM 1829 CA GLY A 277 -29.594 246.953 804.396 1.00100.64 C ANISOU 1829 CA GLY A 277 9885 11634 16719 -105 1608 -4056 C ATOM 1830 C GLY A 277 -28.842 247.592 803.242 1.00102.73 C ANISOU 1830 C GLY A 277 10178 11543 17312 20 1563 -3696 C ATOM 1831 O GLY A 277 -29.397 248.396 802.489 1.00104.38 O ANISOU 1831 O GLY A 277 10303 11359 18000 137 1564 -3759 O ATOM 1832 N GLU A 278 -27.571 247.222 803.104 1.00 95.55 N ANISOU 1832 N GLU A 278 9409 10752 16145 -1 1509 -3318 N ATOM 1833 CA GLU A 278 -26.687 247.823 802.112 1.00 93.09 C ANISOU 1833 CA GLU A 278 9145 10174 16052 104 1463 -2920 C ATOM 1834 C GLU A 278 -26.491 246.882 800.923 1.00 95.01 C ANISOU 1834 C GLU A 278 9276 10306 16519 316 1414 -2849 C ATOM 1835 O GLU A 278 -25.466 246.208 800.816 1.00 98.19 O ANISOU 1835 O GLU A 278 9768 10890 16650 312 1365 -2600 O ATOM 1836 CB GLU A 278 -25.333 248.147 802.756 1.00 92.10 C ANISOU 1836 CB GLU A 278 9265 10252 15476 -47 1429 -2548 C ATOM 1837 CG GLU A 278 -24.800 249.535 802.444 1.00 96.16 C ANISOU 1837 CG GLU A 278 9836 10543 16159 -50 1448 -2248 C ATOM 1838 CD GLU A 278 -25.473 250.603 803.284 1.00102.17 C ANISOU 1838 CD GLU A 278 10578 11273 16971 -181 1508 -2437 C ATOM 1839 OE1 GLU A 278 -25.287 251.808 802.994 1.00101.80 O ANISOU 1839 OE1 GLU A 278 10524 10999 17156 -173 1552 -2262 O ATOM 1840 OE2 GLU A 278 -26.191 250.233 804.239 1.00103.54 O ANISOU 1840 OE2 GLU A 278 10729 11657 16955 -286 1510 -2760 O ATOM 1841 N TYR A 279 -27.475 246.836 800.031 1.00 96.72 N ANISOU 1841 N TYR A 279 9297 10205 17248 514 1411 -3083 N ATOM 1842 CA TYR A 279 -27.426 245.946 798.873 1.00 87.36 C ANISOU 1842 CA TYR A 279 7961 8885 16347 750 1345 -3059 C ATOM 1843 CB TYR A 279 -28.755 245.206 798.700 1.00 84.19 C ANISOU 1843 CB TYR A 279 7337 8433 16218 877 1407 -3572 C ATOM 1844 CG TYR A 279 -29.334 244.657 799.985 1.00 93.35 C ANISOU 1844 CG TYR A 279 8505 9997 16965 685 1530 -3932 C ATOM 1845 CD2 TYR A 279 -30.309 245.358 800.682 1.00100.28 C ANISOU 1845 CD2 TYR A 279 9387 10838 17877 587 1594 -4239 C ATOM 1846 CE2 TYR A 279 -30.843 244.864 801.857 1.00105.63 C ANISOU 1846 CE2 TYR A 279 10073 11897 18167 423 1684 -4544 C ATOM 1847 CZ TYR A 279 -30.410 243.654 802.349 1.00111.64 C ANISOU 1847 CZ TYR A 279 10853 13053 18513 346 1717 -4536 C ATOM 1848 CE1 TYR A 279 -29.444 242.933 801.675 1.00104.53 C ANISOU 1848 CE1 TYR A 279 9955 12176 17587 430 1663 -4253 C ATOM 1849 CD1 TYR A 279 -28.912 243.438 800.497 1.00 99.03 C ANISOU 1849 CD1 TYR A 279 9235 11124 17268 602 1567 -3959 C ATOM 1850 OH TYR A 279 -30.949 243.172 803.520 1.00118.85 O ANISOU 1850 OH TYR A 279 11783 14332 19044 186 1796 -4807 O ATOM 1851 C TYR A 279 -27.110 246.714 797.597 1.00 87.11 C ANISOU 1851 C TYR A 279 7928 8384 16787 945 1221 -2730 C ATOM 1852 O TYR A 279 -27.430 246.265 796.501 1.00 87.21 O ANISOU 1852 O TYR A 279 7789 8125 17221 1188 1130 -2764 O ATOM 1853 N LEU A 280 -26.489 247.877 797.743 1.00 90.03 N ANISOU 1853 N LEU A 280 8474 8640 17094 843 1208 -2403 N ATOM 1854 CA LEU A 280 -26.163 248.716 796.597 1.00 97.45 C ANISOU 1854 CA LEU A 280 9485 9098 18443 983 1075 -2035 C ATOM 1855 C LEU A 280 -24.808 249.381 796.771 1.00112.38 C ANISOU 1855 C LEU A 280 11585 11150 19963 805 1047 -1528 C ATOM 1856 O LEU A 280 -24.380 249.675 797.891 1.00119.82 O ANISOU 1856 O LEU A 280 12619 12420 20488 624 1171 -1541 O ATOM 1857 CB LEU A 280 -27.225 249.800 796.397 1.00102.27 C ANISOU 1857 CB LEU A 280 10119 9251 19489 924 1059 -2182 C ATOM 1858 CG LEU A 280 -28.671 249.400 796.091 1.00105.04 C ANISOU 1858 CG LEU A 280 10289 9327 20294 1100 1070 -2696 C ATOM 1859 CD1 LEU A 280 -29.544 250.636 795.957 1.00116.56 C ANISOU 1859 CD1 LEU A 280 11815 10324 22148 985 1037 -2783 C ATOM 1860 CD2 LEU A 280 -28.746 248.589 794.837 1.00107.58 C ANISOU 1860 CD2 LEU A 280 10469 9413 20995 1389 929 -2650 C ATOM 1861 N SER A 281 -24.114 249.566 795.672 1.00114.37 N ANISOU 1861 N SER A 281 11912 11190 20353 868 880 -1093 N ATOM 1862 CA SER A 281 -22.863 250.260 795.723 1.00111.29 C ANISOU 1862 CA SER A 281 11729 10929 19626 701 859 -619 C ATOM 1863 C SER A 281 -22.719 250.772 794.345 1.00103.64 C ANISOU 1863 C SER A 281 10836 9527 19016 769 663 -225 C ATOM 1864 O SER A 281 -23.051 250.081 793.418 1.00102.75 O ANISOU 1864 O SER A 281 10604 9207 19230 992 514 -254 O ATOM 1865 CB SER A 281 -21.741 249.308 796.043 1.00116.54 C ANISOU 1865 CB SER A 281 12410 12044 19826 726 859 -507 C ATOM 1866 OG SER A 281 -20.629 250.019 796.531 1.00118.72 O ANISOU 1866 OG SER A 281 12888 12532 19688 533 910 -186 O ATOM 1867 N LEU A 282 -22.314 252.003 794.167 1.00110.77 N ANISOU 1867 N LEU A 282 11924 10262 19900 582 660 136 N ATOM 1868 CA LEU A 282 -22.205 252.450 792.810 1.00115.91 C ANISOU 1868 CA LEU A 282 12665 10484 20891 643 459 539 C ATOM 1869 C LEU A 282 -20.911 253.168 792.568 1.00108.99 C ANISOU 1869 C LEU A 282 12025 9726 19662 473 435 1086 C ATOM 1870 O LEU A 282 -20.590 254.128 793.234 1.00103.28 O ANISOU 1870 O LEU A 282 11413 9120 18706 235 593 1185 O ATOM 1871 CB LEU A 282 -23.413 253.304 792.444 1.00116.76 C ANISOU 1871 CB LEU A 282 12751 10064 21548 608 444 419 C ATOM 1872 CG LEU A 282 -23.291 254.812 792.528 1.00118.15 C ANISOU 1872 CG LEU A 282 13101 10048 21742 322 516 712 C ATOM 1873 CD1 LEU A 282 -22.748 255.352 791.224 1.00118.97 C ANISOU 1873 CD1 LEU A 282 13383 9808 22014 313 327 1292 C ATOM 1874 CD2 LEU A 282 -24.638 255.397 792.824 1.00125.67 C ANISOU 1874 CD2 LEU A 282 13961 10667 23122 255 582 339 C ATOM 1875 N TYR A 283 -20.163 252.713 791.592 1.00108.03 N ANISOU 1875 N TYR A 283 11969 9580 19497 597 233 1438 N ATOM 1876 CA TYR A 283 -18.937 253.385 791.305 1.00118.32 C ANISOU 1876 CA TYR A 283 13514 11004 20438 436 207 1952 C ATOM 1877 C TYR A 283 -19.056 253.896 789.901 1.00129.59 C ANISOU 1877 C TYR A 283 15056 11944 22238 484 -20 2375 C ATOM 1878 O TYR A 283 -19.388 253.147 788.988 1.00138.66 O ANISOU 1878 O TYR A 283 16106 12861 23718 731 -252 2380 O ATOM 1879 CB TYR A 283 -17.767 252.435 791.423 1.00123.96 C ANISOU 1879 CB TYR A 283 14255 12166 20679 507 148 2043 C ATOM 1880 CG TYR A 283 -16.438 253.082 791.154 1.00129.13 C ANISOU 1880 CG TYR A 283 15172 12988 20902 344 127 2541 C ATOM 1881 CD1 TYR A 283 -16.020 253.316 789.868 1.00139.97 C ANISOU 1881 CD1 TYR A 283 16693 14114 22374 387 -109 3014 C ATOM 1882 CE1 TYR A 283 -14.809 253.900 789.612 1.00138.06 C ANISOU 1882 CE1 TYR A 283 16706 14051 21697 230 -119 3461 C ATOM 1883 CZ TYR A 283 -14.001 254.257 790.648 1.00126.75 C ANISOU 1883 CZ TYR A 283 15366 13038 19755 44 118 3412 C ATOM 1884 OH TYR A 283 -12.794 254.843 790.383 1.00124.81 O ANISOU 1884 OH TYR A 283 15373 12983 19064 -108 127 3827 O ATOM 1885 CE2 TYR A 283 -14.393 254.034 791.933 1.00118.66 C ANISOU 1885 CE2 TYR A 283 14187 12239 18661 15 339 2951 C ATOM 1886 CD2 TYR A 283 -15.604 253.454 792.182 1.00119.10 C ANISOU 1886 CD2 TYR A 283 14007 12125 19123 156 338 2532 C ATOM 1887 N ASN A 284 -18.821 255.188 789.737 1.00127.38 N ANISOU 1887 N ASN A 284 14973 11499 21926 244 47 2730 N ATOM 1888 CA ASN A 284 -18.898 255.792 788.430 1.00130.47 C ANISOU 1888 CA ASN A 284 15516 11411 22644 245 -163 3192 C ATOM 1889 C ASN A 284 -20.214 255.460 787.780 1.00137.83 C ANISOU 1889 C ASN A 284 16285 11822 24262 464 -325 2956 C ATOM 1890 O ASN A 284 -21.266 255.544 788.399 1.00138.11 O ANISOU 1890 O ASN A 284 16163 11735 24578 457 -189 2505 O ATOM 1891 CB ASN A 284 -17.750 255.342 787.560 1.00127.26 C ANISOU 1891 CB ASN A 284 15263 11147 21944 336 -389 3642 C ATOM 1892 CG ASN A 284 -16.653 256.344 787.528 1.00127.19 C ANISOU 1892 CG ASN A 284 15534 11317 21474 60 -294 4125 C ATOM 1893 OD1 ASN A 284 -16.896 257.526 787.326 1.00133.30 O ANISOU 1893 OD1 ASN A 284 16438 11816 22394 -156 -208 4373 O ATOM 1894 ND2 ASN A 284 -15.431 255.895 787.733 1.00119.55 N ANISOU 1894 ND2 ASN A 284 14660 10819 19944 52 -297 4252 N ATOM 1895 N ASN A 285 -20.138 255.031 786.533 1.00141.55 N ANISOU 1895 N ASN A 285 16789 12002 24994 675 -630 3242 N ATOM 1896 CA ASN A 285 -21.311 254.643 785.782 1.00137.56 C ANISOU 1896 CA ASN A 285 16123 10975 25168 932 -820 3037 C ATOM 1897 C ASN A 285 -21.640 253.195 786.052 1.00132.71 C ANISOU 1897 C ASN A 285 15215 10600 24610 1228 -848 2542 C ATOM 1898 O ASN A 285 -22.606 252.677 785.531 1.00139.64 O ANISOU 1898 O ASN A 285 15906 11127 26025 1483 -978 2275 O ATOM 1899 CB ASN A 285 -21.021 254.831 784.314 1.00138.12 C ANISOU 1899 CB ASN A 285 16358 10630 25491 1038 -1159 3597 C ATOM 1900 CG ASN A 285 -20.053 255.940 784.080 1.00140.68 C ANISOU 1900 CG ASN A 285 17011 11002 25438 733 -1130 4206 C ATOM 1901 OD1 ASN A 285 -19.966 256.863 784.875 1.00137.94 O ANISOU 1901 OD1 ASN A 285 16753 10795 24864 428 -852 4195 O ATOM 1902 ND2 ASN A 285 -19.301 255.856 783.001 1.00144.05 N ANISOU 1902 ND2 ASN A 285 17614 11340 25778 808 -1415 4737 N ATOM 1903 N THR A 286 -20.819 252.544 786.864 1.00122.29 N ANISOU 1903 N THR A 286 13852 9876 22736 1190 -720 2422 N ATOM 1904 CA THR A 286 -20.993 251.142 787.170 1.00116.60 C ANISOU 1904 CA THR A 286 12860 9446 21998 1426 -724 1993 C ATOM 1905 C THR A 286 -21.716 250.935 788.461 1.00114.93 C ANISOU 1905 C THR A 286 12488 9469 21711 1359 -429 1413 C ATOM 1906 O THR A 286 -21.340 251.488 789.471 1.00113.16 O ANISOU 1906 O THR A 286 12373 9540 21084 1112 -207 1388 O ATOM 1907 CB THR A 286 -19.666 250.501 787.356 1.00112.27 C ANISOU 1907 CB THR A 286 12366 9411 20880 1402 -761 2190 C ATOM 1908 OG1 THR A 286 -18.761 251.009 786.371 1.00116.62 O ANISOU 1908 OG1 THR A 286 13160 9834 21315 1357 -990 2802 O ATOM 1909 CG2 THR A 286 -19.808 249.015 787.217 1.00104.57 C ANISOU 1909 CG2 THR A 286 11104 8621 20008 1677 -862 1876 C ATOM 1910 N LEU A 287 -22.760 250.129 788.424 1.00119.10 N ANISOU 1910 N LEU A 287 12753 9872 22626 1588 -430 941 N ATOM 1911 CA LEU A 287 -23.555 249.868 789.601 1.00119.46 C ANISOU 1911 CA LEU A 287 12648 10134 22608 1538 -165 368 C ATOM 1912 C LEU A 287 -23.632 248.396 789.898 1.00119.24 C ANISOU 1912 C LEU A 287 12360 10465 22481 1736 -125 -11 C ATOM 1913 O LEU A 287 -23.849 247.585 789.023 1.00117.57 O ANISOU 1913 O LEU A 287 11968 10106 22597 2005 -301 -54 O ATOM 1914 CB LEU A 287 -24.959 250.409 789.435 1.00121.67 C ANISOU 1914 CB LEU A 287 12859 9919 23450 1582 -140 60 C ATOM 1915 CG LEU A 287 -25.919 249.868 790.483 1.00117.95 C ANISOU 1915 CG LEU A 287 12190 9664 22961 1604 90 -599 C ATOM 1916 CD1 LEU A 287 -25.794 250.614 791.788 1.00106.22 C ANISOU 1916 CD1 LEU A 287 10828 8469 21060 1294 324 -689 C ATOM 1917 CD2 LEU A 287 -27.319 249.963 789.979 1.00118.43 C ANISOU 1917 CD2 LEU A 287 12120 9216 23661 1769 44 -958 C ATOM 1918 N VAL A 288 -23.452 248.057 791.157 1.00119.46 N ANISOU 1918 N VAL A 288 12361 10969 22058 1596 108 -282 N ATOM 1919 CA VAL A 288 -23.477 246.662 791.562 1.00116.10 C ANISOU 1919 CA VAL A 288 11704 10931 21479 1730 182 -628 C ATOM 1920 C VAL A 288 -24.614 246.424 792.540 1.00110.63 C ANISOU 1920 C VAL A 288 10870 10343 20823 1710 424 -1216 C ATOM 1921 O VAL A 288 -24.741 247.109 793.556 1.00110.83 O ANISOU 1921 O VAL A 288 11022 10495 20593 1490 596 -1319 O ATOM 1922 CB VAL A 288 -22.147 246.223 792.186 1.00118.61 C ANISOU 1922 CB VAL A 288 12117 11768 21180 1589 223 -419 C ATOM 1923 CG1 VAL A 288 -22.345 244.967 793.018 1.00120.64 C ANISOU 1923 CG1 VAL A 288 12163 12453 21220 1629 389 -847 C ATOM 1924 CG2 VAL A 288 -21.110 246.000 791.095 1.00122.41 C ANISOU 1924 CG2 VAL A 288 12658 12205 21647 1682 -47 57 C ATOM 1925 N THR A 289 -25.444 245.446 792.215 1.00109.62 N ANISOU 1925 N THR A 289 10468 10170 21012 1946 432 -1608 N ATOM 1926 CA THR A 289 -26.643 245.167 792.983 1.00111.01 C ANISOU 1926 CA THR A 289 10512 10436 21230 1904 639 -2184 C ATOM 1927 C THR A 289 -26.621 243.738 793.519 1.00122.65 C ANISOU 1927 C THR A 289 11807 12416 22377 1867 754 -2484 C ATOM 1928 O THR A 289 -26.278 242.800 792.799 1.00129.98 O ANISOU 1928 O THR A 289 12563 13404 23421 2043 645 -2421 O ATOM 1929 CB THR A 289 -27.883 245.377 792.106 1.00106.46 C ANISOU 1929 CB THR A 289 9798 9311 21343 2146 560 -2445 C ATOM 1930 OG1 THR A 289 -27.491 245.336 790.730 1.00112.88 O ANISOU 1930 OG1 THR A 289 10579 9760 22550 2378 287 -2079 O ATOM 1931 CG2 THR A 289 -28.503 246.727 792.370 1.00 93.05 C ANISOU 1931 CG2 THR A 289 8284 7248 19821 2003 596 -2473 C ATOM 1932 N LEU A 290 -26.997 243.545 794.767 1.00118.54 N ANISOU 1932 N LEU A 290 11333 12248 21461 1633 958 -2798 N ATOM 1933 CA LEU A 290 -26.979 242.219 795.350 1.00120.38 C ANISOU 1933 CA LEU A 290 11454 12932 21351 1557 1068 -3052 C ATOM 1934 C LEU A 290 -28.356 241.615 795.354 1.00134.62 C ANISOU 1934 C LEU A 290 13021 14700 23428 1671 1188 -3612 C ATOM 1935 O LEU A 290 -29.305 242.270 795.739 1.00145.41 O ANISOU 1935 O LEU A 290 14415 15914 24921 1628 1270 -3888 O ATOM 1936 CB LEU A 290 -26.506 242.305 796.785 1.00100.63 C ANISOU 1936 CB LEU A 290 9191 10841 18203 1223 1190 -3026 C ATOM 1937 CG LEU A 290 -26.752 241.090 797.669 1.00100.16 C ANISOU 1937 CG LEU A 290 9083 11212 17762 1091 1324 -3342 C ATOM 1938 CD1 LEU A 290 -27.958 240.327 797.212 1.00115.98 C ANISOU 1938 CD1 LEU A 290 10782 13150 20136 1283 1407 -3810 C ATOM 1939 CD2 LEU A 290 -25.561 240.202 797.671 1.00 93.30 C ANISOU 1939 CD2 LEU A 290 8269 10621 16562 1042 1267 -3082 C ATOM 1940 N LEU A 291 -28.476 240.354 794.950 1.00130.20 N ANISOU 1940 N LEU A 291 12217 14299 22953 1815 1208 -3804 N ATOM 1941 CA LEU A 291 -29.781 239.694 794.930 1.00131.04 C ANISOU 1941 CA LEU A 291 12068 14407 23314 1944 1351 -4372 C ATOM 1942 C LEU A 291 -29.884 238.560 795.932 1.00124.49 C ANISOU 1942 C LEU A 291 11193 14112 21997 1756 1548 -4652 C ATOM 1943 O LEU A 291 -28.888 238.045 796.397 1.00127.14 O ANISOU 1943 O LEU A 291 11645 14774 21889 1587 1539 -4398 O ATOM 1944 CB LEU A 291 -30.163 239.289 793.527 1.00138.05 C ANISOU 1944 CB LEU A 291 12656 14944 24854 2323 1228 -4460 C ATOM 1945 CG LEU A 291 -29.871 240.511 792.666 1.00142.47 C ANISOU 1945 CG LEU A 291 13355 14973 25804 2452 1000 -4066 C ATOM 1946 CD1 LEU A 291 -30.943 240.731 791.641 1.00151.54 C ANISOU 1946 CD1 LEU A 291 14313 15584 27681 2781 913 -4327 C ATOM 1947 CD2 LEU A 291 -29.796 241.701 793.567 1.00131.38 C ANISOU 1947 CD2 LEU A 291 12263 13558 24096 2177 1059 -3938 C ATOM 1948 N PRO A 292 -31.107 238.214 796.277 1.00115.31 N ANISOU 1948 N PRO A 292 9879 13018 20915 1785 1724 -5178 N ATOM 1949 CA PRO A 292 -31.439 237.267 797.360 1.00115.17 C ANISOU 1949 CA PRO A 292 9839 13499 20422 1586 1937 -5490 C ATOM 1950 C PRO A 292 -31.054 235.768 797.265 1.00133.66 C ANISOU 1950 C PRO A 292 11973 16203 22607 1608 2024 -5555 C ATOM 1951 O PRO A 292 -30.510 235.267 798.250 1.00126.08 O ANISOU 1951 O PRO A 292 11173 15640 21093 1345 2094 -5451 O ATOM 1952 CB PRO A 292 -32.955 237.415 797.488 1.00120.48 C ANISOU 1952 CB PRO A 292 10369 14068 21341 1677 2088 -6060 C ATOM 1953 CG PRO A 292 -33.219 238.814 797.052 1.00113.04 C ANISOU 1953 CG PRO A 292 9548 12628 20775 1759 1946 -5949 C ATOM 1954 CD PRO A 292 -32.275 239.027 795.901 1.00112.97 C ANISOU 1954 CD PRO A 292 9520 12307 21097 1943 1728 -5486 C ATOM 1955 N LEU A 293 -31.248 235.104 796.132 1.00142.54 N ANISOU 1955 N LEU A 293 12761 17185 24211 1909 2000 -5686 N ATOM 1956 CA LEU A 293 -30.881 233.689 796.001 1.00145.61 C ANISOU 1956 CA LEU A 293 12908 17924 24493 1932 2089 -5755 C ATOM 1957 C LEU A 293 -30.392 233.305 794.619 1.00146.43 C ANISOU 1957 C LEU A 293 12735 17805 25097 2241 1907 -5577 C ATOM 1958 O LEU A 293 -30.195 234.153 793.755 1.00150.23 O ANISOU 1958 O LEU A 293 13254 17854 25973 2428 1683 -5324 O ATOM 1959 CB LEU A 293 -32.049 232.802 796.382 1.00154.99 C ANISOU 1959 CB LEU A 293 13841 19381 25667 1955 2375 -6351 C ATOM 1960 CG LEU A 293 -33.191 233.094 795.437 1.00171.83 C ANISOU 1960 CG LEU A 293 15706 21118 28462 2303 2384 -6743 C ATOM 1961 CD1 LEU A 293 -34.328 232.120 795.691 1.00177.36 C ANISOU 1961 CD1 LEU A 293 16107 22102 29178 2365 2691 -7373 C ATOM 1962 CD2 LEU A 293 -33.609 234.558 795.646 1.00172.61 C ANISOU 1962 CD2 LEU A 293 16087 20846 28650 2260 2283 -6690 C ATOM 1963 N GLU A 294 -30.227 232.003 794.424 1.00147.59 N ANISOU 1963 N GLU A 294 12585 18257 25234 2293 2001 -5715 N ATOM 1964 CA GLU A 294 -30.440 231.054 795.506 1.00146.18 C ANISOU 1964 CA GLU A 294 12395 18588 24559 2041 2275 -5979 C ATOM 1965 C GLU A 294 -29.324 231.284 796.467 1.00128.41 C ANISOU 1965 C GLU A 294 10548 16550 21691 1698 2205 -5549 C ATOM 1966 O GLU A 294 -29.492 231.294 797.669 1.00124.22 O ANISOU 1966 O GLU A 294 10249 16282 20669 1421 2343 -5628 O ATOM 1967 CB GLU A 294 -30.419 229.603 795.015 1.00155.87 C ANISOU 1967 CB GLU A 294 13185 20094 25943 2168 2394 -6188 C ATOM 1968 CG GLU A 294 -31.784 229.049 794.630 1.00167.63 C ANISOU 1968 CG GLU A 294 14269 21588 27833 2411 2622 -6806 C ATOM 1969 CD GLU A 294 -32.007 229.051 793.135 1.00182.71 C ANISOU 1969 CD GLU A 294 15812 23100 30508 2852 2446 -6868 C ATOM 1970 OE1 GLU A 294 -31.001 228.958 792.402 1.00185.77 O ANISOU 1970 OE1 GLU A 294 16143 23384 31058 2947 2191 -6457 O ATOM 1971 OE2 GLU A 294 -33.175 229.133 792.695 1.00189.27 O ANISOU 1971 OE2 GLU A 294 16413 23720 31782 3111 2548 -7329 O ATOM 1972 N ASN A 295 -28.157 231.465 795.883 1.00125.68 N ANISOU 1972 N ASN A 295 10279 16078 21395 1739 1967 -5088 N ATOM 1973 CA ASN A 295 -26.963 231.731 796.637 1.00120.26 C ANISOU 1973 CA ASN A 295 9974 15540 20180 1461 1869 -4659 C ATOM 1974 C ASN A 295 -26.773 233.162 796.309 1.00118.47 C ANISOU 1974 C ASN A 295 9986 14916 20111 1519 1679 -4375 C ATOM 1975 O ASN A 295 -27.409 233.690 795.412 1.00133.62 O ANISOU 1975 O ASN A 295 11740 16478 22551 1776 1607 -4472 O ATOM 1976 CB ASN A 295 -25.786 230.886 796.213 1.00102.40 C ANISOU 1976 CB ASN A 295 7611 13447 17848 1462 1754 -4376 C ATOM 1977 CG ASN A 295 -25.175 230.171 797.367 1.00 89.55 C ANISOU 1977 CG ASN A 295 6175 12227 15621 1146 1867 -4314 C ATOM 1978 OD1 ASN A 295 -25.688 230.217 798.466 1.00 83.38 O ANISOU 1978 OD1 ASN A 295 5574 11619 14490 940 2030 -4494 O ATOM 1979 ND2 ASN A 295 -24.090 229.486 797.125 1.00 94.36 N ANISOU 1979 ND2 ASN A 295 6737 12990 16125 1108 1767 -4062 N ATOM 1980 N GLY A 296 -25.953 233.839 797.057 1.00101.31 N ANISOU 1980 N GLY A 296 8200 12786 17508 1287 1605 -4040 N ATOM 1981 CA GLY A 296 -25.888 235.262 796.809 1.00104.32 C ANISOU 1981 CA GLY A 296 8786 12810 18042 1326 1470 -3806 C ATOM 1982 C GLY A 296 -25.686 235.554 795.338 1.00101.56 C ANISOU 1982 C GLY A 296 8238 12101 18248 1634 1269 -3609 C ATOM 1983 O GLY A 296 -24.704 235.123 794.735 1.00112.87 O ANISOU 1983 O GLY A 296 9610 13582 19692 1701 1116 -3315 O ATOM 1984 N LEU A 297 -26.626 236.255 794.746 1.00 91.41 N ANISOU 1984 N LEU A 297 6844 10448 17439 1830 1248 -3773 N ATOM 1985 CA LEU A 297 -26.484 236.578 793.359 1.00103.61 C ANISOU 1985 CA LEU A 297 8226 11604 19538 2138 1022 -3564 C ATOM 1986 C LEU A 297 -26.091 238.028 793.352 1.00111.78 C ANISOU 1986 C LEU A 297 9566 12350 20554 2071 901 -3197 C ATOM 1987 O LEU A 297 -26.808 238.869 793.861 1.00121.73 O ANISOU 1987 O LEU A 297 10959 13467 21826 1985 999 -3355 O ATOM 1988 CB LEU A 297 -27.812 236.404 792.630 1.00110.10 C ANISOU 1988 CB LEU A 297 8727 12139 20969 2436 1061 -3993 C ATOM 1989 CG LEU A 297 -28.456 235.028 792.496 1.00116.06 C ANISOU 1989 CG LEU A 297 9148 13164 21784 2506 1271 -4514 C ATOM 1990 CD1 LEU A 297 -29.828 235.103 791.869 1.00122.79 C ANISOU 1990 CD1 LEU A 297 10145 14537 21972 2161 1498 -4641 C ATOM 1991 CD2 LEU A 297 -27.561 234.134 791.674 1.00119.10 C ANISOU 1991 CD2 LEU A 297 9374 13260 22620 2698 1376 -4993 C ATOM 1992 N PHE A 298 -24.950 238.335 792.775 1.00105.40 N ANISOU 1992 N PHE A 298 8861 11471 19715 2107 689 -2709 N ATOM 1993 CA PHE A 298 -24.542 239.710 792.732 1.00104.73 C ANISOU 1993 CA PHE A 298 9052 11131 19611 2047 593 -2347 C ATOM 1994 C PHE A 298 -24.826 240.147 791.363 1.00119.67 C ANISOU 1994 C PHE A 298 10811 12528 22129 2368 365 -2191 C ATOM 1995 O PHE A 298 -24.198 239.694 790.430 1.00125.93 O ANISOU 1995 O PHE A 298 11478 13272 23097 2551 143 -1935 O ATOM 1996 CB PHE A 298 -23.060 239.840 792.968 1.00106.74 C ANISOU 1996 CB PHE A 298 9533 11618 19406 1883 499 -1891 C ATOM 1997 CG PHE A 298 -22.725 240.270 794.337 1.00108.91 C ANISOU 1997 CG PHE A 298 10105 12163 19112 1555 674 -1889 C ATOM 1998 CD1 PHE A 298 -21.833 241.276 794.553 1.00103.68 C ANISOU 1998 CD1 PHE A 298 9711 11476 18206 1434 621 -1505 C ATOM 1999 CE1 PHE A 298 -21.550 241.666 795.803 1.00 97.33 C ANISOU 1999 CE1 PHE A 298 9163 10900 16919 1160 765 -1521 C ATOM 2000 CZ PHE A 298 -22.158 241.067 796.856 1.00 95.11 C ANISOU 2000 CZ PHE A 298 8903 10855 16379 1000 929 -1890 C ATOM 2001 CE2 PHE A 298 -23.048 240.081 796.659 1.00 96.04 C ANISOU 2001 CE2 PHE A 298 8768 11014 16709 1105 988 -2257 C ATOM 2002 CD2 PHE A 298 -23.335 239.688 795.412 1.00107.93 C ANISOU 2002 CD2 PHE A 298 9991 12307 18709 1381 879 -2274 C ATOM 2003 N GLN A 299 -25.759 241.061 791.239 1.00124.08 N ANISOU 2003 N GLN A 299 11418 12695 23033 2433 391 -2327 N ATOM 2004 CA GLN A 299 -26.135 241.516 789.940 1.00127.40 C ANISOU 2004 CA GLN A 299 11755 12558 24094 2742 157 -2183 C ATOM 2005 C GLN A 299 -25.415 242.782 789.630 1.00122.81 C ANISOU 2005 C GLN A 299 11483 11691 23489 2682 -5 -1647 C ATOM 2006 O GLN A 299 -25.408 243.713 790.432 1.00117.90 O ANISOU 2006 O GLN A 299 11103 11088 22607 2442 133 -1606 O ATOM 2007 CB GLN A 299 -27.640 241.723 789.892 1.00133.31 C ANISOU 2007 CB GLN A 299 12376 12978 25296 2864 267 -2673 C ATOM 2008 CG GLN A 299 -28.083 242.934 789.115 1.00141.46 C ANISOU 2008 CG GLN A 299 13553 13354 26843 2999 97 -2483 C ATOM 2009 CD GLN A 299 -28.483 242.621 787.707 1.00146.10 C ANISOU 2009 CD GLN A 299 13930 13470 28110 3386 -159 -2458 C ATOM 2010 OE1 GLN A 299 -28.130 241.586 787.170 1.00149.97 O ANISOU 2010 OE1 GLN A 299 14176 14137 28669 3568 -266 -2445 O ATOM 2011 NE2 GLN A 299 -29.224 243.523 787.097 1.00148.69 N ANISOU 2011 NE2 GLN A 299 14359 13192 28945 3477 -278 -2442 N ATOM 2012 N MSE A 300 -24.788 242.797 788.463 1.00119.38 N ANISOU 2012 N MSE A 300 11059 11025 23273 2836 -313 -1219 N ATOM 2013 CA MSE A 300 -24.098 243.974 788.023 1.00122.81 C ANISOU 2013 CA MSE A 300 11828 11199 23636 2695 -492 -663 C ATOM 2014 C MSE A 300 -24.801 244.545 786.806 1.00133.65 C ANISOU 2014 C MSE A 300 13199 11915 25667 2907 -728 -535 C ATOM 2015 O MSE A 300 -24.840 243.928 785.760 1.00141.83 O ANISOU 2015 O MSE A 300 14047 12760 27083 3189 -972 -464 O ATOM 2016 CB MSE A 300 -22.644 243.657 787.649 1.00120.37 C ANISOU 2016 CB MSE A 300 11615 11160 22959 2649 -692 -178 C ATOM 2017 CG MSE A 300 -21.655 243.358 788.807 1.00167.21 C ANISOU 2017 CG MSE A 300 17655 17686 28190 2388 -505 -158 C ATOM 2018 SE MSE A 300 -19.761 243.806 788.389 1.00164.07 Se ANISOU 2018 SE MSE A 300 17594 17473 27272 2214 -750 574 Se ATOM 2019 CE MSE A 300 -19.668 245.423 789.423 1.00112.65 C ANISOU 2019 CE MSE A 300 11460 10936 20407 1861 -496 699 C ATOM 2020 N GLY A 301 -25.340 245.741 786.970 1.00131.59 N ANISOU 2020 N GLY A 301 13150 11305 25543 2758 -664 -499 N ATOM 2021 CA GLY A 301 -25.943 246.569 785.946 1.00128.62 C ANISOU 2021 CA GLY A 301 12865 10259 25744 2869 -872 -307 C ATOM 2022 C GLY A 301 -25.134 247.831 785.762 1.00128.44 C ANISOU 2022 C GLY A 301 13216 10089 25495 2603 -965 300 C ATOM 2023 O GLY A 301 -24.649 248.417 786.728 1.00127.09 O ANISOU 2023 O GLY A 301 13228 10228 24832 2298 -758 369 O ATOM 2024 N THR A 302 -24.980 248.251 784.514 1.00132.02 N ANISOU 2024 N THR A 302 13781 10074 26306 2722 -1276 749 N ATOM 2025 CA THR A 302 -24.181 249.432 784.215 1.00132.10 C ANISOU 2025 CA THR A 302 14153 9942 26096 2467 -1369 1372 C ATOM 2026 C THR A 302 -25.021 250.491 783.499 1.00133.96 C ANISOU 2026 C THR A 302 14527 9465 26905 2459 -1486 1523 C ATOM 2027 O THR A 302 -26.254 250.465 783.572 1.00139.85 O ANISOU 2027 O THR A 302 15118 9886 28135 2579 -1416 1062 O ATOM 2028 CB THR A 302 -22.955 249.072 783.354 1.00130.68 C ANISOU 2028 CB THR A 302 14066 9898 25688 2545 -1664 1919 C ATOM 2029 OG1 THR A 302 -23.386 248.454 782.134 1.00137.35 O ANISOU 2029 OG1 THR A 302 14729 10348 27108 2914 -1991 1953 O ATOM 2030 CG2 THR A 302 -22.041 248.111 784.113 1.00112.09 C ANISOU 2030 CG2 THR A 302 11607 8241 22742 2502 -1547 1791 C ATOM 2031 N THR A 314 -27.054 256.061 780.493 1.00141.54 N ANISOU 2031 N THR A 314 16553 7451 29777 1811 -2002 3082 N ATOM 2032 CA THR A 314 -28.275 255.789 781.236 1.00154.00 C ANISOU 2032 CA THR A 314 17882 8961 31670 1891 -1806 2321 C ATOM 2033 C THR A 314 -28.658 254.318 781.162 1.00172.65 C ANISOU 2033 C THR A 314 19907 11497 34196 2326 -1873 1810 C ATOM 2034 O THR A 314 -29.792 253.941 781.437 1.00185.96 O ANISOU 2034 O THR A 314 21374 13006 36277 2494 -1787 1185 O ATOM 2035 CB THR A 314 -29.434 256.692 780.758 1.00155.74 C ANISOU 2035 CB THR A 314 18187 8380 32606 1831 -1886 2260 C ATOM 2036 OG1 THR A 314 -30.664 255.956 780.762 1.00153.63 O ANISOU 2036 OG1 THR A 314 17642 7855 32875 2158 -1902 1570 O ATOM 2037 CG2 THR A 314 -29.165 257.205 779.360 1.00156.12 C ANISOU 2037 CG2 THR A 314 18480 7823 33017 1878 -2242 2954 C ATOM 2038 N PHE A 315 -27.696 253.482 780.799 1.00175.54 N ANISOU 2038 N PHE A 315 20224 12231 34242 2498 -2019 2067 N ATOM 2039 CA PHE A 315 -27.941 252.052 780.682 1.00175.28 C ANISOU 2039 CA PHE A 315 19847 12406 34344 2896 -2084 1632 C ATOM 2040 C PHE A 315 -28.169 251.304 781.972 1.00170.57 C ANISOU 2040 C PHE A 315 19010 12417 33384 2870 -1741 988 C ATOM 2041 O PHE A 315 -27.594 251.615 783.002 1.00167.95 O ANISOU 2041 O PHE A 315 18781 12578 32455 2563 -1489 1003 O ATOM 2042 CB PHE A 315 -26.862 251.364 779.871 1.00172.42 C ANISOU 2042 CB PHE A 315 19485 12243 33783 3081 -2372 2095 C ATOM 2043 CG PHE A 315 -27.274 251.079 778.471 1.00181.14 C ANISOU 2043 CG PHE A 315 20521 12737 35567 3454 -2776 2277 C ATOM 2044 CD1 PHE A 315 -27.386 249.776 778.019 1.00182.44 C ANISOU 2044 CD1 PHE A 315 20343 13010 35964 3866 -2939 2007 C ATOM 2045 CE1 PHE A 315 -27.778 249.512 776.715 1.00180.36 C ANISOU 2045 CE1 PHE A 315 19993 12167 36369 4241 -3334 2166 C ATOM 2046 CZ PHE A 315 -28.068 250.551 775.859 1.00180.09 C ANISOU 2046 CZ PHE A 315 20245 11413 36768 4196 -3573 2613 C ATOM 2047 CE2 PHE A 315 -27.968 251.853 776.301 1.00183.33 C ANISOU 2047 CE2 PHE A 315 21007 11706 36941 3758 -3397 2894 C ATOM 2048 CD2 PHE A 315 -27.579 252.112 777.602 1.00183.56 C ANISOU 2048 CD2 PHE A 315 21091 12339 36314 3395 -2996 2712 C ATOM 2049 N GLN A 316 -29.037 250.312 781.882 1.00173.55 N ANISOU 2049 N GLN A 316 19062 12736 34144 3206 -1738 421 N ATOM 2050 CA GLN A 316 -29.404 249.488 783.003 1.00173.11 C ANISOU 2050 CA GLN A 316 18757 13211 33807 3219 -1426 -223 C ATOM 2051 C GLN A 316 -29.324 248.062 782.535 1.00177.66 C ANISOU 2051 C GLN A 316 19003 13997 34505 3596 -1539 -429 C ATOM 2052 O GLN A 316 -30.354 247.447 782.316 1.00183.00 O ANISOU 2052 O GLN A 316 19407 14461 35664 3885 -1523 -949 O ATOM 2053 CB GLN A 316 -30.850 249.798 783.357 1.00179.52 C ANISOU 2053 CB GLN A 316 19480 13665 35065 3242 -1271 -819 C ATOM 2054 CG GLN A 316 -31.048 251.199 783.868 1.00183.31 C ANISOU 2054 CG GLN A 316 20251 13836 35561 2884 -1197 -637 C ATOM 2055 CD GLN A 316 -30.258 251.501 785.121 1.00192.38 C ANISOU 2055 CD GLN A 316 21630 14284 37181 2884 -1503 -73 C ATOM 2056 NE2 GLN A 316 -29.661 252.687 785.184 1.00189.27 N ANISOU 2056 NE2 GLN A 316 21503 13998 36413 2651 -1592 617 N ATOM 2057 OE1 GLN A 316 -30.154 250.664 786.007 1.00196.98 O ANISOU 2057 OE1 GLN A 316 22165 14228 38449 3079 -1651 -259 O ATOM 2058 N ASN A 317 -28.132 247.522 782.319 1.00176.30 N ANISOU 2058 N ASN A 317 18834 14217 33935 3608 -1664 -42 N ATOM 2059 CA ASN A 317 -28.111 246.183 781.761 1.00179.04 C ANISOU 2059 CA ASN A 317 18832 14710 34484 3977 -1805 -232 C ATOM 2060 C ASN A 317 -26.889 245.280 781.930 1.00173.07 C ANISOU 2060 C ASN A 317 17988 14585 33187 3958 -1840 -29 C ATOM 2061 O ASN A 317 -25.775 245.693 781.628 1.00174.72 O ANISOU 2061 O ASN A 317 18445 14885 33054 3806 -2014 563 O ATOM 2062 CB ASN A 317 -28.296 246.460 780.290 1.00187.68 C ANISOU 2062 CB ASN A 317 19963 15129 36218 4248 -2215 133 C ATOM 2063 CG ASN A 317 -28.639 247.929 780.042 1.00190.35 C ANISOU 2063 CG ASN A 317 20660 14882 36784 4037 -2273 448 C ATOM 2064 OD1 ASN A 317 -27.907 248.840 780.453 1.00187.23 O ANISOU 2064 OD1 ASN A 317 20589 14631 35919 3669 -2198 866 O ATOM 2065 ND2 ASN A 317 -29.766 248.161 779.394 1.00194.15 N ANISOU 2065 ND2 ASN A 317 21071 14702 37996 4262 -2393 226 N ATOM 2066 N ASN A 318 -27.075 244.029 782.340 1.00167.21 N ANISOU 2066 N ASN A 318 16889 14264 32378 4115 -1690 -505 N ATOM 2067 CA ASN A 318 -25.902 243.159 782.440 1.00165.31 C ANISOU 2067 CA ASN A 318 16561 14586 31665 4087 -1750 -300 C ATOM 2068 C ASN A 318 -26.009 241.817 783.177 1.00163.03 C ANISOU 2068 C ASN A 318 15909 14869 31166 4149 -1503 -822 C ATOM 2069 O ASN A 318 -27.097 241.382 783.561 1.00154.79 O ANISOU 2069 O ASN A 318 14623 13816 30376 4269 -1273 -1414 O ATOM 2070 CB ASN A 318 -24.688 243.953 782.908 1.00160.89 C ANISOU 2070 CB ASN A 318 16394 14287 30450 3714 -1737 224 C ATOM 2071 CG ASN A 318 -23.419 243.468 782.285 1.00158.69 C ANISOU 2071 CG ASN A 318 16136 14247 29910 3753 -2025 694 C ATOM 2072 OD1 ASN A 318 -23.004 242.340 782.521 1.00161.73 O ANISOU 2072 OD1 ASN A 318 16271 15087 30094 3821 -1995 512 O ATOM 2073 ND2 ASN A 318 -22.791 244.312 781.478 1.00154.84 N ANISOU 2073 ND2 ASN A 318 15952 13463 29417 3697 -2310 1307 N ATOM 2074 N ILE A 319 -24.853 241.178 783.365 1.00166.85 N ANISOU 2074 N ILE A 319 16372 15852 31171 4048 -1553 -591 N ATOM 2075 CA ILE A 319 -24.762 239.845 783.964 1.00163.25 C ANISOU 2075 CA ILE A 319 15578 15955 30497 4080 -1359 -988 C ATOM 2076 C ILE A 319 -24.286 239.696 785.396 1.00147.66 C ANISOU 2076 C ILE A 319 13722 14557 27826 3733 -1020 -1128 C ATOM 2077 O ILE A 319 -23.210 240.130 785.731 1.00139.22 O ANISOU 2077 O ILE A 319 12941 13699 26259 3483 -1063 -728 O ATOM 2078 CB ILE A 319 -23.766 239.029 783.192 1.00165.18 C ANISOU 2078 CB ILE A 319 15662 16394 30706 4211 -1668 -670 C ATOM 2079 CG1 ILE A 319 -22.839 238.327 784.174 1.00152.05 C ANISOU 2079 CG1 ILE A 319 13988 15402 28381 3950 -1480 -703 C ATOM 2080 CD1 ILE A 319 -21.594 239.098 784.462 1.00140.40 C ANISOU 2080 CD1 ILE A 319 12941 14075 26332 3646 -1566 -176 C ATOM 2081 CG2 ILE A 319 -22.934 239.944 782.342 1.00170.65 C ANISOU 2081 CG2 ILE A 319 16697 16778 31365 4171 -2033 8 C ATOM 2082 N PRO A 320 -25.090 239.020 786.207 1.00147.17 N ANISOU 2082 N PRO A 320 13450 14760 27707 3686 -696 -1703 N ATOM 2083 CA PRO A 320 -24.812 238.772 787.625 1.00142.89 C ANISOU 2083 CA PRO A 320 13031 14757 26504 3319 -370 -1892 C ATOM 2084 C PRO A 320 -23.685 237.753 787.844 1.00136.92 C ANISOU 2084 C PRO A 320 12195 14512 25314 3200 -402 -1747 C ATOM 2085 O PRO A 320 -23.391 236.960 786.949 1.00128.72 O ANISOU 2085 O PRO A 320 10887 13479 24543 3424 -622 -1667 O ATOM 2086 CB PRO A 320 -26.135 238.178 788.125 1.00146.60 C ANISOU 2086 CB PRO A 320 13265 15298 27138 3351 -84 -2551 C ATOM 2087 CG PRO A 320 -26.706 237.519 786.910 1.00150.70 C ANISOU 2087 CG PRO A 320 13405 15532 28320 3755 -265 -2713 C ATOM 2088 CD PRO A 320 -26.428 238.525 785.835 1.00153.89 C ANISOU 2088 CD PRO A 320 13976 15377 29117 3949 -616 -2230 C ATOM 2089 N THR A 321 -23.067 237.787 789.027 1.00133.56 N ANISOU 2089 N THR A 321 12006 14494 24248 2851 -201 -1715 N ATOM 2090 CA THR A 321 -22.050 236.805 789.407 1.00116.76 C ANISOU 2090 CA THR A 321 9840 12844 21678 2693 -195 -1630 C ATOM 2091 C THR A 321 -22.395 236.142 790.743 1.00115.47 C ANISOU 2091 C THR A 321 9705 13087 21080 2420 152 -2032 C ATOM 2092 O THR A 321 -23.027 236.752 791.609 1.00109.48 O ANISOU 2092 O THR A 321 9135 12307 20156 2259 362 -2228 O ATOM 2093 CB THR A 321 -20.655 237.437 789.562 1.00 96.11 C ANISOU 2093 CB THR A 321 7552 10343 18625 2517 -340 -1111 C ATOM 2094 OG1 THR A 321 -20.528 237.973 790.878 1.00 87.32 O ANISOU 2094 OG1 THR A 321 6747 9430 16999 2197 -84 -1170 O ATOM 2095 CG2 THR A 321 -20.429 238.543 788.546 1.00 87.47 C ANISOU 2095 CG2 THR A 321 6591 8804 17840 2703 -629 -674 C ATOM 2096 N ASN A 322 -21.951 234.901 790.915 1.00118.29 N ANISOU 2096 N ASN A 322 9889 13813 21245 2360 189 -2132 N ATOM 2097 CA ASN A 322 -22.294 234.116 792.099 1.00118.09 C ANISOU 2097 CA ASN A 322 9877 14161 20829 2121 493 -2496 C ATOM 2098 C ASN A 322 -21.497 234.456 793.356 1.00108.83 C ANISOU 2098 C ASN A 322 9121 13244 18987 1767 600 -2323 C ATOM 2099 O ASN A 322 -20.608 235.304 793.339 1.00 87.77 O ANISOU 2099 O ASN A 322 6722 10496 16131 1697 464 -1933 O ATOM 2100 CB ASN A 322 -22.161 232.625 791.800 1.00125.35 C ANISOU 2100 CB ASN A 322 10432 15367 21829 2189 505 -2674 C ATOM 2101 CG ASN A 322 -23.183 232.147 790.788 1.00151.80 C ANISOU 2101 CG ASN A 322 13331 18514 25832 2535 474 -2983 C ATOM 2102 OD1 ASN A 322 -24.179 232.825 790.540 1.00161.52 O ANISOU 2102 OD1 ASN A 322 14543 19419 27407 2690 510 -3166 O ATOM 2103 ND2 ASN A 322 -22.943 230.976 790.200 1.00158.45 N ANISOU 2103 ND2 ASN A 322 13793 19541 26869 2664 403 -3057 N ATOM 2104 N LEU A 323 -21.836 233.774 794.445 1.00118.18 N ANISOU 2104 N LEU A 323 10352 14732 19820 1559 839 -2622 N ATOM 2105 CA LEU A 323 -21.123 233.898 795.708 1.00109.33 C ANISOU 2105 CA LEU A 323 9610 13857 18074 1244 925 -2496 C ATOM 2106 C LEU A 323 -20.661 232.531 796.175 1.00108.16 C ANISOU 2106 C LEU A 323 9369 14088 17640 1112 1005 -2593 C ATOM 2107 O LEU A 323 -21.214 231.510 795.771 1.00120.02 O ANISOU 2107 O LEU A 323 10506 15704 19394 1222 1081 -2866 O ATOM 2108 CB LEU A 323 -22.039 234.478 796.779 1.00114.40 C ANISOU 2108 CB LEU A 323 10452 14492 18523 1087 1116 -2748 C ATOM 2109 CG LEU A 323 -22.540 235.903 796.570 1.00141.20 C ANISOU 2109 CG LEU A 323 13969 17537 22144 1153 1074 -2680 C ATOM 2110 CD1 LEU A 323 -23.190 236.414 797.843 1.00151.26 C ANISOU 2110 CD1 LEU A 323 15474 18889 23109 934 1233 -2884 C ATOM 2111 CD2 LEU A 323 -21.406 236.812 796.155 1.00150.17 C ANISOU 2111 CD2 LEU A 323 15313 18524 23221 1159 886 -2199 C ATOM 2112 N SER A 324 -19.708 232.514 797.092 1.00 94.73 N ANISOU 2112 N SER A 324 7991 12582 15422 875 1005 -2397 N ATOM 2113 CA SER A 324 -19.221 231.286 797.684 1.00 99.58 C ANISOU 2113 CA SER A 324 8567 13541 15728 715 1082 -2466 C ATOM 2114 CB SER A 324 -17.727 231.392 797.885 1.00 90.30 C ANISOU 2114 CB SER A 324 7651 12449 14212 596 929 -2091 C ATOM 2115 OG SER A 324 -17.152 232.062 796.799 1.00 80.59 O ANISOU 2115 OG SER A 324 6375 11007 13238 768 710 -1795 O ATOM 2116 C SER A 324 -19.912 231.138 799.032 1.00105.84 C ANISOU 2116 C SER A 324 9540 14502 16173 503 1294 -2725 C ATOM 2117 O SER A 324 -19.991 232.092 799.761 1.00108.48 O ANISOU 2117 O SER A 324 10194 14736 16286 401 1293 -2659 O ATOM 2118 N ALA A 325 -20.456 229.983 799.378 1.00109.45 N ANISOU 2118 N ALA A 325 9775 15222 16588 435 1469 -3021 N ATOM 2119 CA ALA A 325 -21.113 229.893 800.678 1.00116.30 C ANISOU 2119 CA ALA A 325 10820 16260 17107 227 1644 -3236 C ATOM 2120 C ALA A 325 -21.313 228.499 801.256 1.00126.99 C ANISOU 2120 C ALA A 325 11996 17986 18267 74 1832 -3456 C ATOM 2121 O ALA A 325 -21.288 227.531 800.533 1.00138.97 O ANISOU 2121 O ALA A 325 13151 19630 20022 163 1884 -3556 O ATOM 2122 CB ALA A 325 -22.413 230.587 800.612 1.00122.20 C ANISOU 2122 CB ALA A 325 11500 16839 18093 322 1734 -3505 C ATOM 2123 N SER A 326 -21.517 228.401 802.562 1.00132.43 N ANISOU 2123 N SER A 326 12919 18857 18541 -159 1929 -3522 N ATOM 2124 CA SER A 326 -21.759 227.103 803.198 1.00147.31 C ANISOU 2124 CA SER A 326 14647 21111 20214 -336 2133 -3717 C ATOM 2125 C SER A 326 -22.832 227.139 804.291 1.00155.55 C ANISOU 2125 C SER A 326 15773 22311 21019 -491 2309 -3978 C ATOM 2126 O SER A 326 -23.879 226.512 804.180 1.00157.58 O ANISOU 2126 O SER A 326 15731 22743 21399 -467 2539 -4334 O ATOM 2127 CB SER A 326 -20.483 226.526 803.770 1.00146.74 C ANISOU 2127 CB SER A 326 14761 21198 19797 -528 2049 -3439 C ATOM 2128 OG SER A 326 -20.813 225.597 804.789 1.00148.20 O ANISOU 2128 OG SER A 326 14927 21709 19674 -766 2241 -3588 O ATOM 2129 N ALA A 327 -22.513 227.862 805.360 1.00157.44 N ANISOU 2129 N ALA A 327 16407 22502 20912 -647 2192 -3791 N ATOM 2130 CA ALA A 327 -23.376 228.110 806.505 1.00155.41 C ANISOU 2130 CA ALA A 327 16280 22368 20400 -804 2285 -3954 C ATOM 2131 C ALA A 327 -24.154 229.360 806.143 1.00148.70 C ANISOU 2131 C ALA A 327 15456 21239 19805 -648 2229 -4058 C ATOM 2132 O ALA A 327 -24.192 229.739 804.976 1.00154.36 O ANISOU 2132 O ALA A 327 16021 21719 20910 -427 2180 -4067 O ATOM 2133 CB ALA A 327 -22.559 228.344 807.736 1.00152.03 C ANISOU 2133 CB ALA A 327 16220 21984 19560 -1013 2138 -3672 C ATOM 2134 N ILE A 328 -24.797 230.011 807.098 1.00131.15 N ANISOU 2134 N ILE A 328 13397 19037 17396 -758 2231 -4134 N ATOM 2135 CA ILE A 328 -25.543 231.190 806.692 1.00124.82 C ANISOU 2135 CA ILE A 328 12587 17970 16870 -617 2189 -4246 C ATOM 2136 CB ILE A 328 -26.974 231.181 807.238 1.00126.41 C ANISOU 2136 CB ILE A 328 12662 18334 17036 -665 2379 -4637 C ATOM 2137 CG1 ILE A 328 -27.928 230.600 806.200 1.00130.18 C ANISOU 2137 CG1 ILE A 328 12751 18823 17887 -472 2588 -5033 C ATOM 2138 CD1 ILE A 328 -28.327 231.589 805.141 1.00126.95 C ANISOU 2138 CD1 ILE A 328 12247 18031 17959 -229 2508 -5101 C ATOM 2139 CG2 ILE A 328 -27.423 232.576 807.506 1.00127.47 C ANISOU 2139 CG2 ILE A 328 12943 18244 17247 -644 2266 -4627 C ATOM 2140 C ILE A 328 -24.870 232.528 806.984 1.00117.52 C ANISOU 2140 C ILE A 328 11980 16783 15890 -631 1949 -3924 C ATOM 2141 O ILE A 328 -24.585 232.871 808.122 1.00112.10 O ANISOU 2141 O ILE A 328 11529 16175 14887 -797 1859 -3778 O ATOM 2142 N TRP A 329 -24.635 233.279 805.915 1.00102.35 N ANISOU 2142 N TRP A 329 10032 14551 14305 -445 1856 -3817 N ATOM 2143 CA TRP A 329 -24.028 234.599 806.013 1.00 74.01 C ANISOU 2143 CA TRP A 329 6706 10708 10706 -443 1669 -3527 C ATOM 2144 C TRP A 329 -24.985 235.684 805.551 1.00 80.88 C ANISOU 2144 C TRP A 329 7486 11333 11912 -333 1693 -3687 C ATOM 2145 O TRP A 329 -25.733 235.498 804.594 1.00 98.55 O ANISOU 2145 O TRP A 329 9454 13464 14527 -162 1792 -3921 O ATOM 2146 CB TRP A 329 -22.757 234.657 805.169 1.00 64.85 C ANISOU 2146 CB TRP A 329 5625 9393 9620 -338 1537 -3198 C ATOM 2147 CG TRP A 329 -21.763 233.601 805.523 1.00 62.98 C ANISOU 2147 CG TRP A 329 5459 9378 9094 -433 1509 -3051 C ATOM 2148 CD1 TRP A 329 -21.746 232.317 805.079 1.00 69.44 C ANISOU 2148 CD1 TRP A 329 6038 10381 9965 -407 1617 -3171 C ATOM 2149 NE1 TRP A 329 -20.681 231.644 805.627 1.00 70.86 N ANISOU 2149 NE1 TRP A 329 6363 10729 9830 -535 1554 -2975 N ATOM 2150 CE2 TRP A 329 -19.986 232.494 806.445 1.00 50.46 C ANISOU 2150 CE2 TRP A 329 4120 8059 6995 -625 1393 -2734 C ATOM 2151 CZ2 TRP A 329 -18.844 232.273 807.214 1.00 47.89 C ANISOU 2151 CZ2 TRP A 329 4027 7818 6350 -748 1271 -2503 C ATOM 2152 CH2 TRP A 329 -18.361 233.322 807.944 1.00 48.09 C ANISOU 2152 CH2 TRP A 329 4333 7716 6225 -792 1113 -2315 C ATOM 2153 CZ3 TRP A 329 -18.991 234.576 807.928 1.00 60.29 C ANISOU 2153 CZ3 TRP A 329 5929 9070 7910 -738 1088 -2341 C ATOM 2154 CE3 TRP A 329 -20.128 234.794 807.164 1.00 57.82 C ANISOU 2154 CE3 TRP A 329 5399 8671 7900 -636 1215 -2564 C ATOM 2155 CD2 TRP A 329 -20.644 233.743 806.404 1.00 54.58 C ANISOU 2155 CD2 TRP A 329 4699 8369 7670 -567 1364 -2772 C ATOM 2156 N SER A 330 -24.947 236.820 806.236 1.00 75.20 N ANISOU 2156 N SER A 330 6974 10518 11082 -423 1597 -3566 N ATOM 2157 CA SER A 330 -25.739 237.978 805.858 1.00 83.04 C ANISOU 2157 CA SER A 330 7901 11263 12387 -342 1609 -3681 C ATOM 2158 C SER A 330 -24.808 239.170 805.650 1.00 86.50 C ANISOU 2158 C SER A 330 8555 11456 12854 -331 1461 -3318 C ATOM 2159 O SER A 330 -23.990 239.475 806.512 1.00 92.51 O ANISOU 2159 O SER A 330 9562 12299 13290 -460 1353 -3085 O ATOM 2160 CB SER A 330 -26.782 238.272 806.937 1.00 82.57 C ANISOU 2160 CB SER A 330 7827 11362 12185 -470 1676 -3943 C ATOM 2161 OG SER A 330 -26.322 237.856 808.212 1.00 76.25 O ANISOU 2161 OG SER A 330 7196 10837 10938 -659 1624 -3824 O ATOM 2162 N ILE A 331 -24.919 239.830 804.499 1.00 86.68 N ANISOU 2162 N ILE A 331 8473 11178 13283 -165 1459 -3270 N ATOM 2163 CA ILE A 331 -24.000 240.911 804.150 1.00 81.14 C ANISOU 2163 CA ILE A 331 7950 10257 12623 -143 1354 -2912 C ATOM 2164 C ILE A 331 -24.085 242.078 805.115 1.00 86.39 C ANISOU 2164 C ILE A 331 8788 10902 13136 -285 1320 -2864 C ATOM 2165 O ILE A 331 -25.175 242.527 805.465 1.00 89.20 O ANISOU 2165 O ILE A 331 9030 11240 13623 -320 1384 -3129 O ATOM 2166 CB ILE A 331 -24.247 241.459 802.741 1.00 85.19 C ANISOU 2166 CB ILE A 331 8280 10440 13650 65 1362 -2866 C ATOM 2167 CG2 ILE A 331 -25.681 241.927 802.599 1.00 81.25 C ANISOU 2167 CG2 ILE A 331 7576 9785 13508 124 1452 -3218 C ATOM 2168 CG1 ILE A 331 -23.290 242.620 802.474 1.00 85.46 C ANISOU 2168 CG1 ILE A 331 8497 10289 13685 63 1281 -2478 C ATOM 2169 CD1 ILE A 331 -23.442 243.247 801.122 1.00 86.43 C ANISOU 2169 CD1 ILE A 331 8448 10076 14315 262 1264 -2361 C ATOM 2170 N VAL A 332 -22.920 242.575 805.519 1.00 83.00 N ANISOU 2170 N VAL A 332 8612 10479 12444 -352 1219 -2543 N ATOM 2171 CA VAL A 332 -22.817 243.666 806.474 1.00 70.59 C ANISOU 2171 CA VAL A 332 7202 8904 10715 -475 1172 -2473 C ATOM 2172 CB VAL A 332 -21.609 243.463 807.401 1.00 72.40 C ANISOU 2172 CB VAL A 332 7693 9302 10514 -565 1046 -2240 C ATOM 2173 CG2 VAL A 332 -21.742 242.148 808.139 1.00 74.02 C ANISOU 2173 CG2 VAL A 332 7870 9782 10470 -644 1025 -2372 C ATOM 2174 CG1 VAL A 332 -21.484 244.608 808.381 1.00 65.51 C ANISOU 2174 CG1 VAL A 332 6952 8422 9516 -661 988 -2179 C ATOM 2175 C VAL A 332 -22.670 244.990 805.745 1.00 77.33 C ANISOU 2175 C VAL A 332 8059 9470 11854 -404 1197 -2311 C ATOM 2176 O VAL A 332 -23.354 245.964 806.065 1.00 81.65 O ANISOU 2176 O VAL A 332 8553 9924 12546 -454 1237 -2429 O ATOM 2177 N ASP A 333 -21.779 245.020 804.760 1.00 79.36 N ANISOU 2177 N ASP A 333 8353 9599 12199 -288 1179 -2035 N ATOM 2178 CA ASP A 333 -21.570 246.220 803.955 1.00 87.87 C ANISOU 2178 CA ASP A 333 9404 10414 13567 -211 1214 -1829 C ATOM 2179 CB ASP A 333 -20.726 247.249 804.715 1.00 99.16 C ANISOU 2179 CB ASP A 333 11078 11870 14730 -301 1188 -1620 C ATOM 2180 CG ASP A 333 -20.940 248.673 804.220 1.00111.16 C ANISOU 2180 CG ASP A 333 12520 13141 16574 -273 1271 -1515 C ATOM 2181 OD1 ASP A 333 -21.039 249.586 805.069 1.00118.97 O ANISOU 2181 OD1 ASP A 333 13596 14139 17467 -367 1291 -1564 O ATOM 2182 OD2 ASP A 333 -21.006 248.889 802.992 1.00114.24 O ANISOU 2182 OD2 ASP A 333 12741 13328 17336 -149 1307 -1377 O ATOM 2183 C ASP A 333 -20.911 245.838 802.638 1.00 76.87 C ANISOU 2183 C ASP A 333 7928 8920 12359 -48 1189 -1586 C ATOM 2184 O ASP A 333 -20.418 244.721 802.489 1.00 66.76 O ANISOU 2184 O ASP A 333 6659 7793 10913 -12 1138 -1559 O ATOM 2185 N LEU A 334 -20.889 246.777 801.697 1.00 76.92 N ANISOU 2185 N LEU A 334 7829 8676 12723 52 1213 -1397 N ATOM 2186 CA LEU A 334 -20.548 246.486 800.315 1.00 75.47 C ANISOU 2186 CA LEU A 334 7484 8351 12840 244 1155 -1187 C ATOM 2187 C LEU A 334 -19.973 247.738 799.670 1.00 77.11 C ANISOU 2187 C LEU A 334 7697 8372 13230 297 1155 -828 C ATOM 2188 O LEU A 334 -20.592 248.794 799.724 1.00 95.11 O ANISOU 2188 O LEU A 334 9924 10452 15761 279 1225 -872 O ATOM 2189 CB LEU A 334 -21.826 246.084 799.582 1.00 79.42 C ANISOU 2189 CB LEU A 334 7707 8642 13826 398 1158 -1472 C ATOM 2190 CG LEU A 334 -21.776 245.085 798.426 1.00 86.41 C ANISOU 2190 CG LEU A 334 8399 9460 14974 613 1059 -1443 C ATOM 2191 CD1 LEU A 334 -23.164 244.917 797.831 1.00 84.95 C ANISOU 2191 CD1 LEU A 334 7964 9011 15300 778 1073 -1778 C ATOM 2192 CD2 LEU A 334 -20.804 245.528 797.365 1.00 90.50 C ANISOU 2192 CD2 LEU A 334 8921 9828 15637 756 930 -997 C ATOM 2193 N VAL A 335 -18.802 247.629 799.054 1.00 72.06 N ANISOU 2193 N VAL A 335 7101 7804 12473 365 1076 -474 N ATOM 2194 CA VAL A 335 -18.157 248.803 798.466 1.00 77.39 C ANISOU 2194 CA VAL A 335 7829 8336 13239 371 1058 -88 C ATOM 2195 C VAL A 335 -17.432 248.503 797.152 1.00 84.50 C ANISOU 2195 C VAL A 335 8770 9116 14219 476 854 272 C ATOM 2196 O VAL A 335 -16.648 247.563 797.068 1.00 94.21 O ANISOU 2196 O VAL A 335 9994 10586 15217 528 778 334 O ATOM 2197 CB VAL A 335 -17.190 249.475 799.467 1.00 79.15 C ANISOU 2197 CB VAL A 335 8233 8831 13011 189 1172 46 C ATOM 2198 CG1 VAL A 335 -16.260 250.437 798.756 1.00 76.72 C ANISOU 2198 CG1 VAL A 335 8106 8415 12629 111 1114 497 C ATOM 2199 CG2 VAL A 335 -17.975 250.195 800.562 1.00 84.97 C ANISOU 2199 CG2 VAL A 335 9058 9518 13708 51 1282 -220 C ATOM 2200 N LEU A 336 -17.692 249.323 796.136 1.00 86.82 N ANISOU 2200 N LEU A 336 9115 9033 14842 495 751 519 N ATOM 2201 CA LEU A 336 -17.204 249.089 794.775 1.00 90.02 C ANISOU 2201 CA LEU A 336 9553 9257 15394 616 517 867 C ATOM 2202 CB LEU A 336 -18.401 249.021 793.826 1.00 94.02 C ANISOU 2202 CB LEU A 336 9902 9322 16500 790 400 760 C ATOM 2203 CG LEU A 336 -18.162 248.814 792.335 1.00102.21 C ANISOU 2203 CG LEU A 336 10943 10079 17812 956 120 1098 C ATOM 2204 CD2 LEU A 336 -19.302 249.433 791.538 1.00112.38 C ANISOU 2204 CD2 LEU A 336 12182 10827 19691 1043 42 1087 C ATOM 2205 CD1 LEU A 336 -18.017 247.340 792.013 1.00101.53 C ANISOU 2205 CD1 LEU A 336 10650 10177 17747 1160 -7 948 C ATOM 2206 C LEU A 336 -16.246 250.190 794.319 1.00 91.91 C ANISOU 2206 C LEU A 336 10048 9434 15440 473 472 1353 C ATOM 2207 O LEU A 336 -16.649 251.345 794.188 1.00 97.20 O ANISOU 2207 O LEU A 336 10798 9843 16291 361 533 1475 O ATOM 2208 N THR A 337 -14.984 249.841 794.068 1.00 87.82 N ANISOU 2208 N THR A 337 9659 9159 14551 461 372 1625 N ATOM 2209 CA THR A 337 -13.964 250.855 793.789 1.00 84.48 C ANISOU 2209 CA THR A 337 9496 8765 13836 303 372 2056 C ATOM 2210 CB THR A 337 -13.232 251.262 795.076 1.00 81.11 C ANISOU 2210 CB THR A 337 9177 8706 12934 126 602 1968 C ATOM 2211 CG2 THR A 337 -14.031 250.844 796.294 1.00 82.96 C ANISOU 2211 CG2 THR A 337 9237 9068 13215 134 770 1490 C ATOM 2212 OG1 THR A 337 -11.945 250.634 795.115 1.00 82.06 O ANISOU 2212 OG1 THR A 337 9413 9154 12613 128 525 2098 O ATOM 2213 C THR A 337 -12.889 250.441 792.780 1.00 86.56 C ANISOU 2213 C THR A 337 9887 9096 13906 366 129 2433 C ATOM 2214 O THR A 337 -12.945 249.362 792.193 1.00 83.61 O ANISOU 2214 O THR A 337 9378 8715 13674 545 -71 2382 O ATOM 2215 N ARG A 338 -11.906 251.320 792.597 1.00 88.80 N ANISOU 2215 N ARG A 338 10423 9464 13852 211 153 2801 N ATOM 2216 CA ARG A 338 -10.764 251.066 791.721 1.00 91.06 C ANISOU 2216 CA ARG A 338 10882 9861 13858 233 -69 3176 C ATOM 2217 C ARG A 338 -9.984 249.842 792.186 1.00 95.17 C ANISOU 2217 C ARG A 338 11349 10761 14051 295 -132 2987 C ATOM 2218 O ARG A 338 -10.156 249.392 793.316 1.00 90.39 O ANISOU 2218 O ARG A 338 10631 10365 13349 275 43 2619 O ATOM 2219 CB ARG A 338 -9.841 252.290 791.681 1.00 84.83 C ANISOU 2219 CB ARG A 338 10380 9164 12687 21 44 3541 C ATOM 2220 N PRO A 339 -9.118 249.303 791.313 1.00105.01 N ANISOU 2220 N PRO A 339 12683 12092 15125 360 -397 3250 N ATOM 2221 CD PRO A 339 -8.884 249.774 789.938 1.00115.80 C ANISOU 2221 CD PRO A 339 14199 13218 16581 391 -646 3717 C ATOM 2222 CG PRO A 339 -8.383 248.544 789.251 1.00113.57 C ANISOU 2222 CG PRO A 339 13830 13051 16270 550 -965 3757 C ATOM 2223 CB PRO A 339 -7.629 247.784 790.294 1.00 97.27 C ANISOU 2223 CB PRO A 339 11743 11410 13803 487 -853 3471 C ATOM 2224 CA PRO A 339 -8.334 248.100 791.620 1.00 96.22 C ANISOU 2224 CA PRO A 339 11515 11315 13728 405 -498 3096 C ATOM 2225 C PRO A 339 -7.284 248.355 792.685 1.00100.73 C ANISOU 2225 C PRO A 339 12272 12249 13752 234 -301 3028 C ATOM 2226 O PRO A 339 -6.776 249.473 792.788 1.00 98.27 O ANISOU 2226 O PRO A 339 12184 11966 13187 91 -168 3240 O ATOM 2227 N LEU A 340 -6.974 247.325 793.468 1.00 99.63 N ANISOU 2227 N LEU A 340 12032 12374 13449 248 -276 2730 N ATOM 2228 CA LEU A 340 -5.852 247.373 794.398 1.00 90.05 C ANISOU 2228 CA LEU A 340 10999 11491 11725 114 -149 2663 C ATOM 2229 C LEU A 340 -4.783 246.458 793.834 1.00 97.61 C ANISOU 2229 C LEU A 340 12021 12641 12425 140 -417 2777 C ATOM 2230 O LEU A 340 -5.093 245.527 793.087 1.00103.73 O ANISOU 2230 O LEU A 340 12613 13343 13458 268 -654 2777 O ATOM 2231 CB LEU A 340 -6.256 246.874 795.787 1.00 74.04 C ANISOU 2231 CB LEU A 340 8836 9606 9690 90 65 2248 C ATOM 2232 CG LEU A 340 -7.691 247.074 796.281 1.00 72.40 C ANISOU 2232 CG LEU A 340 8423 9207 9878 130 236 1997 C ATOM 2233 CD1 LEU A 340 -7.918 246.267 797.547 1.00 66.41 C ANISOU 2233 CD1 LEU A 340 7546 8645 9041 112 375 1616 C ATOM 2234 CD2 LEU A 340 -8.020 248.542 796.512 1.00 71.04 C ANISOU 2234 CD2 LEU A 340 8357 8894 9743 36 431 2099 C ATOM 2235 N GLU A 341 -3.526 246.711 794.173 1.00 97.24 N ANISOU 2235 N GLU A 341 12198 12848 11902 19 -381 2822 N ATOM 2236 CA GLU A 341 -2.465 245.821 793.728 1.00 95.61 C ANISOU 2236 CA GLU A 341 12043 12839 11446 14 -629 2860 C ATOM 2237 CB GLU A 341 -1.101 246.300 794.217 1.00 89.77 C ANISOU 2237 CB GLU A 341 11498 12346 10264 -140 -520 2759 C ATOM 2238 CG GLU A 341 -0.446 247.328 793.320 1.00 86.51 C ANISOU 2238 CG GLU A 341 11311 11925 9635 -200 -581 3091 C ATOM 2239 CD GLU A 341 1.020 247.509 793.637 1.00 76.21 C ANISOU 2239 CD GLU A 341 10196 10871 7889 -316 -550 2992 C ATOM 2240 OE2 GLU A 341 1.809 247.729 792.692 1.00 48.89 O ANISOU 2240 OE2 GLU A 341 6927 7475 4172 -358 -730 3270 O ATOM 2241 OE1 GLU A 341 1.378 247.430 794.835 1.00 56.26 O ANISOU 2241 OE1 GLU A 341 7631 8456 5289 -356 -364 2640 O ATOM 2242 C GLU A 341 -2.743 244.409 794.227 1.00105.36 C ANISOU 2242 C GLU A 341 13069 14165 12798 81 -705 2600 C ATOM 2243 O GLU A 341 -2.873 244.181 795.427 1.00110.05 O ANISOU 2243 O GLU A 341 13611 14865 13339 20 -486 2294 O ATOM 2244 N LEU A 342 -2.862 243.479 793.300 1.00112.52 N ANISOU 2244 N LEU A 342 13802 15030 13920 187 -994 2660 N ATOM 2245 CA LEU A 342 -3.122 242.098 793.628 1.00125.61 C ANISOU 2245 CA LEU A 342 15191 16790 15746 225 -1056 2376 C ATOM 2246 CB LEU A 342 -4.575 241.787 793.361 1.00140.21 C ANISOU 2246 CB LEU A 342 16719 18416 18140 372 -1018 2238 C ATOM 2247 CG LEU A 342 -5.114 242.194 791.980 1.00165.41 C ANISOU 2247 CG LEU A 342 19848 21324 21676 527 -1233 2517 C ATOM 2248 CD1 LEU A 342 -4.173 241.679 790.937 1.00176.04 C ANISOU 2248 CD1 LEU A 342 21239 22761 22887 564 -1605 2768 C ATOM 2249 CD2 LEU A 342 -6.557 241.770 791.606 1.00172.69 C ANISOU 2249 CD2 LEU A 342 20426 22002 23188 708 -1228 2345 C ATOM 2250 C LEU A 342 -2.331 241.266 792.679 1.00133.84 C ANISOU 2250 C LEU A 342 16205 17939 16710 258 -1417 2525 C ATOM 2251 O LEU A 342 -2.051 241.711 791.581 1.00142.72 O ANISOU 2251 O LEU A 342 17437 18969 17822 315 -1643 2847 O ATOM 2252 N ASN A 343 -1.968 240.047 793.048 1.00130.94 N ANISOU 2252 N ASN A 343 15691 17764 16296 215 -1497 2311 N ATOM 2253 CA ASN A 343 -1.208 239.257 792.099 1.00129.88 C ANISOU 2253 CA ASN A 343 15508 17736 16105 239 -1872 2451 C ATOM 2254 CB ASN A 343 -0.430 238.136 792.753 1.00131.28 C ANISOU 2254 CB ASN A 343 15639 18169 16071 106 -1919 2226 C ATOM 2255 CG ASN A 343 0.061 237.136 791.742 1.00138.27 C ANISOU 2255 CG ASN A 343 16353 19148 17036 147 -2319 2315 C ATOM 2256 OD1 ASN A 343 -0.533 236.978 790.677 1.00140.67 O ANISOU 2256 OD1 ASN A 343 16441 19311 17697 317 -2528 2455 O ATOM 2257 ND2 ASN A 343 1.154 236.463 792.054 1.00139.92 N ANISOU 2257 ND2 ASN A 343 16656 19569 16938 -12 -2422 2222 N ATOM 2258 C ASN A 343 -2.234 238.656 791.203 1.00122.00 C ANISOU 2258 C ASN A 343 14146 16567 15643 429 -2034 2452 C ATOM 2259 O ASN A 343 -2.803 237.617 791.491 1.00111.69 O ANISOU 2259 O ASN A 343 12518 15312 14607 460 -1994 2186 O ATOM 2260 N VAL A 344 -2.476 239.341 790.106 1.00124.06 N ANISOU 2260 N VAL A 344 14461 16616 16061 557 -2212 2759 N ATOM 2261 CA VAL A 344 -3.487 238.911 789.201 1.00127.14 C ANISOU 2261 CA VAL A 344 14522 16790 16997 770 -2374 2773 C ATOM 2262 C VAL A 344 -3.245 239.529 787.851 1.00132.95 C ANISOU 2262 C VAL A 344 15397 17344 17773 881 -2701 3200 C ATOM 2263 O VAL A 344 -2.447 240.444 787.712 1.00136.36 O ANISOU 2263 O VAL A 344 16197 17810 17804 774 -2726 3477 O ATOM 2264 CB VAL A 344 -4.813 239.419 789.725 1.00122.05 C ANISOU 2264 CB VAL A 344 13764 15920 16688 833 -2048 2588 C ATOM 2265 CG1 VAL A 344 -5.907 239.105 788.753 1.00119.50 C ANISOU 2265 CG1 VAL A 344 13018 15616 16771 932 -1974 2230 C ATOM 2266 CG2 VAL A 344 -5.113 238.736 791.023 1.00120.26 C ANISOU 2266 CG2 VAL A 344 13789 15802 16103 645 -1692 2462 C ATOM 2267 N GLU A 345 -3.949 239.014 786.857 1.00131.96 N ANISOU 2267 N GLU A 345 14972 17028 18138 1100 -2948 3250 N ATOM 2268 CA GLU A 345 -3.899 239.539 785.512 1.00137.53 C ANISOU 2268 CA GLU A 345 15777 17504 18975 1240 -3289 3666 C ATOM 2269 C GLU A 345 -4.761 240.780 785.588 1.00143.49 C ANISOU 2269 C GLU A 345 16681 17934 19904 1260 -3045 3771 C ATOM 2270 O GLU A 345 -5.351 241.048 786.617 1.00146.52 O ANISOU 2270 O GLU A 345 17040 18310 20321 1183 -2665 3493 O ATOM 2271 CB GLU A 345 -4.443 238.532 784.520 1.00144.03 C ANISOU 2271 CB GLU A 345 16190 18213 20324 1491 -3623 3638 C ATOM 2272 CG GLU A 345 -3.829 237.156 784.699 1.00149.35 C ANISOU 2272 CG GLU A 345 16607 19222 20916 1448 -3774 3412 C ATOM 2273 CD GLU A 345 -3.275 236.589 783.409 1.00156.39 C ANISOU 2273 CD GLU A 345 17386 20136 21900 1586 -4308 3674 C ATOM 2274 OE1 GLU A 345 -3.802 236.937 782.335 1.00159.95 O ANISOU 2274 OE1 GLU A 345 17783 20283 22709 1806 -4555 3933 O ATOM 2275 OE2 GLU A 345 -2.309 235.803 783.471 1.00154.92 O ANISOU 2275 OE2 GLU A 345 17168 20261 21435 1472 -4498 3624 O ATOM 2276 N ALA A 346 -4.830 241.568 784.536 1.00146.93 N ANISOU 2276 N ALA A 346 17285 18101 20442 1345 -3263 4178 N ATOM 2277 CA ALA A 346 -5.586 242.804 784.631 1.00146.25 C ANISOU 2277 CA ALA A 346 17361 17702 20505 1321 -3024 4293 C ATOM 2278 C ALA A 346 -7.040 242.632 785.062 1.00146.66 C ANISOU 2278 C ALA A 346 17099 17514 21110 1446 -2781 3929 C ATOM 2279 O ALA A 346 -7.734 241.724 784.629 1.00145.42 O ANISOU 2279 O ALA A 346 16583 17250 21420 1659 -2926 3744 O ATOM 2280 CB ALA A 346 -5.529 243.536 783.311 1.00143.93 C ANISOU 2280 CB ALA A 346 17262 17112 20314 1407 -3340 4806 C ATOM 2281 N SER A 347 -7.479 243.524 785.944 1.00143.10 N ANISOU 2281 N SER A 347 16785 16998 20590 1308 -2404 3811 N ATOM 2282 CA SER A 347 -8.856 243.557 786.418 1.00140.36 C ANISOU 2282 CA SER A 347 16201 16421 20707 1393 -2153 3471 C ATOM 2283 C SER A 347 -9.273 245.015 786.312 1.00132.83 C ANISOU 2283 C SER A 347 15497 15157 19815 1307 -2013 3708 C ATOM 2284 O SER A 347 -8.447 245.896 786.504 1.00124.65 O ANISOU 2284 O SER A 347 14790 14238 18334 1110 -1932 3970 O ATOM 2285 CB SER A 347 -8.976 243.041 787.846 1.00137.90 C ANISOU 2285 CB SER A 347 15771 16408 20216 1277 -1813 3012 C ATOM 2286 OG SER A 347 -8.302 243.884 788.751 1.00135.08 O ANISOU 2286 OG SER A 347 15720 16235 19370 1039 -1569 3065 O ATOM 2287 N TYR A 348 -10.530 245.273 785.959 1.00132.71 N ANISOU 2287 N TYR A 348 15324 14742 20357 1449 -1989 3620 N ATOM 2288 CA TYR A 348 -11.006 246.648 785.782 1.00127.54 C ANISOU 2288 CA TYR A 348 14886 13743 19830 1356 -1876 3851 C ATOM 2289 C TYR A 348 -11.729 247.262 786.979 1.00117.11 C ANISOU 2289 C TYR A 348 13552 12416 18530 1213 -1465 3519 C ATOM 2290 O TYR A 348 -12.000 248.448 787.010 1.00118.76 O ANISOU 2290 O TYR A 348 13943 12405 18775 1081 -1332 3691 O ATOM 2291 CB TYR A 348 -11.767 246.766 784.451 1.00132.18 C ANISOU 2291 CB TYR A 348 15394 13831 20996 1580 -2175 4081 C ATOM 2292 CG TYR A 348 -12.988 247.643 784.409 1.00129.38 C ANISOU 2292 CG TYR A 348 15031 13016 21110 1589 -2028 4021 C ATOM 2293 CD2 TYR A 348 -12.946 248.897 783.837 1.00130.14 C ANISOU 2293 CD2 TYR A 348 15420 12801 21226 1466 -2069 4463 C ATOM 2294 CE2 TYR A 348 -14.071 249.684 783.771 1.00134.07 C ANISOU 2294 CE2 TYR A 348 15904 12850 22186 1460 -1953 4405 C ATOM 2295 CZ TYR A 348 -15.258 249.205 784.259 1.00136.35 C ANISOU 2295 CZ TYR A 348 15889 13007 22909 1598 -1807 3883 C ATOM 2296 OH TYR A 348 -16.397 249.967 784.209 1.00136.40 O ANISOU 2296 OH TYR A 348 15883 12561 23384 1588 -1703 3786 O ATOM 2297 CE1 TYR A 348 -15.322 247.953 784.802 1.00134.00 C ANISOU 2297 CE1 TYR A 348 15304 13034 22575 1731 -1759 3446 C ATOM 2298 CD1 TYR A 348 -14.200 247.182 784.867 1.00129.81 C ANISOU 2298 CD1 TYR A 348 14782 12937 21604 1722 -1869 3528 C ATOM 2299 N LEU A 349 -12.016 246.451 787.981 1.00109.21 N ANISOU 2299 N LEU A 349 12335 11671 17490 1223 -1271 3054 N ATOM 2300 CA LEU A 349 -12.623 246.957 789.209 1.00101.28 C ANISOU 2300 CA LEU A 349 11322 10716 16444 1083 -906 2729 C ATOM 2301 C LEU A 349 -12.275 246.101 790.421 1.00 94.00 C ANISOU 2301 C LEU A 349 10299 10230 15187 1015 -721 2364 C ATOM 2302 O LEU A 349 -11.622 245.066 790.303 1.00102.30 O ANISOU 2302 O LEU A 349 11264 11530 16073 1070 -864 2337 O ATOM 2303 CB LEU A 349 -14.144 247.036 789.076 1.00 97.17 C ANISOU 2303 CB LEU A 349 10585 9818 16518 1220 -843 2456 C ATOM 2304 CG LEU A 349 -14.736 248.105 788.163 1.00 94.54 C ANISOU 2304 CG LEU A 349 10367 8982 16572 1242 -945 2748 C ATOM 2305 CD1 LEU A 349 -16.222 248.251 788.442 1.00 86.51 C ANISOU 2305 CD1 LEU A 349 9156 7659 16056 1319 -795 2361 C ATOM 2306 CD2 LEU A 349 -14.028 249.431 788.358 1.00 99.60 C ANISOU 2306 CD2 LEU A 349 11344 9651 16851 979 -828 3111 C ATOM 2307 N ASN A 350 -12.724 246.555 791.587 1.00 83.91 N ANISOU 2307 N ASN A 350 9034 9030 13819 885 -416 2094 N ATOM 2308 CA ASN A 350 -12.601 245.807 792.829 1.00 86.28 C ANISOU 2308 CA ASN A 350 9242 9690 13852 819 -225 1731 C ATOM 2309 C ASN A 350 -13.870 245.976 793.651 1.00 83.39 C ANISOU 2309 C ASN A 350 8729 9225 13729 815 14 1339 C ATOM 2310 O ASN A 350 -14.253 247.093 793.992 1.00 75.73 O ANISOU 2310 O ASN A 350 7871 8104 12799 708 158 1365 O ATOM 2311 CB ASN A 350 -11.387 246.282 793.638 1.00 93.52 C ANISOU 2311 CB ASN A 350 10420 10915 14197 615 -108 1863 C ATOM 2312 CG ASN A 350 -10.106 245.544 793.278 1.00 96.72 C ANISOU 2312 CG ASN A 350 10908 11577 14265 613 -307 2044 C ATOM 2313 OD1 ASN A 350 -9.654 245.571 792.135 1.00106.10 O ANISOU 2313 OD1 ASN A 350 12161 12657 15495 681 -561 2367 O ATOM 2314 ND2 ASN A 350 -9.508 244.889 794.264 1.00 88.39 N ANISOU 2314 ND2 ASN A 350 9860 10854 12869 528 -206 1843 N ATOM 2315 N LEU A 351 -14.529 244.868 793.962 1.00 87.59 N ANISOU 2315 N LEU A 351 9004 9858 14419 920 58 969 N ATOM 2316 CA LEU A 351 -15.720 244.912 794.797 1.00 78.93 C ANISOU 2316 CA LEU A 351 7774 8721 13496 912 282 563 C ATOM 2317 C LEU A 351 -15.481 244.275 796.161 1.00 79.68 C ANISOU 2317 C LEU A 351 7856 9212 13208 793 474 288 C ATOM 2318 O LEU A 351 -15.379 243.057 796.275 1.00 87.93 O ANISOU 2318 O LEU A 351 8839 10435 14136 780 444 126 O ATOM 2319 CB LEU A 351 -16.882 244.209 794.108 1.00 74.97 C ANISOU 2319 CB LEU A 351 6981 7998 13507 1130 217 310 C ATOM 2320 CG LEU A 351 -18.124 244.174 794.994 1.00 77.89 C ANISOU 2320 CG LEU A 351 7226 8360 14007 1109 453 -150 C ATOM 2321 CD2 LEU A 351 -19.294 243.524 794.273 1.00 80.79 C ANISOU 2321 CD2 LEU A 351 7329 8495 14873 1309 402 -431 C ATOM 2322 CD1 LEU A 351 -18.461 245.588 795.417 1.00 76.27 C ANISOU 2322 CD1 LEU A 351 7201 7963 13816 977 564 -93 C ATOM 2323 N ILE A 352 -15.450 245.087 797.203 1.00 77.91 N ANISOU 2323 N ILE A 352 7826 9055 12720 608 649 236 N ATOM 2324 CA ILE A 352 -15.241 244.600 798.557 1.00 77.70 C ANISOU 2324 CA ILE A 352 8025 9270 12226 412 756 18 C ATOM 2325 CB ILE A 352 -14.598 245.686 799.383 1.00 66.66 C ANISOU 2325 CB ILE A 352 6881 7939 10508 277 842 153 C ATOM 2326 CG1 ILE A 352 -13.424 246.260 798.630 1.00 61.15 C ANISOU 2326 CG1 ILE A 352 6165 7311 9757 310 782 556 C ATOM 2327 CD1 ILE A 352 -12.621 247.158 799.441 1.00 56.54 C ANISOU 2327 CD1 ILE A 352 5842 6843 8798 174 870 669 C ATOM 2328 CG2 ILE A 352 -14.146 245.153 800.699 1.00 63.56 C ANISOU 2328 CG2 ILE A 352 6760 7754 9636 157 843 -9 C ATOM 2329 C ILE A 352 -16.534 244.210 799.248 1.00 76.95 C ANISOU 2329 C ILE A 352 7899 9120 12218 360 850 -389 C ATOM 2330 O ILE A 352 -17.463 244.983 799.305 1.00 83.20 O ANISOU 2330 O ILE A 352 8631 9720 13263 357 925 -508 O ATOM 2331 N VAL A 353 -16.594 243.013 799.795 1.00 63.22 N ANISOU 2331 N VAL A 353 6187 7567 10267 310 843 -605 N ATOM 2332 CA VAL A 353 -17.803 242.575 800.444 1.00 69.72 C ANISOU 2332 CA VAL A 353 6952 8392 11146 254 924 -986 C ATOM 2333 C VAL A 353 -17.567 242.115 801.842 1.00 62.60 C ANISOU 2333 C VAL A 353 6284 7718 9783 85 933 -1120 C ATOM 2334 O VAL A 353 -16.650 241.388 802.090 1.00 67.41 O ANISOU 2334 O VAL A 353 6998 8510 10104 57 870 -1026 O ATOM 2335 CB VAL A 353 -18.385 241.411 799.710 1.00 78.23 C ANISOU 2335 CB VAL A 353 7748 9481 12496 379 908 -1173 C ATOM 2336 CG1 VAL A 353 -19.845 241.293 800.008 1.00 77.83 C ANISOU 2336 CG1 VAL A 353 7551 9361 12661 372 1010 -1559 C ATOM 2337 CG2 VAL A 353 -18.149 241.574 798.254 1.00 78.40 C ANISOU 2337 CG2 VAL A 353 7555 9318 12916 585 799 -946 C ATOM 2338 N LEU A 354 -18.417 242.523 802.758 1.00 56.13 N ANISOU 2338 N LEU A 354 5521 6887 8919 -22 988 -1341 N ATOM 2339 CA LEU A 354 -18.248 242.132 804.133 1.00 63.23 C ANISOU 2339 CA LEU A 354 6612 7993 9420 -173 950 -1446 C ATOM 2340 C LEU A 354 -19.418 241.308 804.560 1.00 67.05 C ANISOU 2340 C LEU A 354 6936 8584 9957 -228 1013 -1792 C ATOM 2341 O LEU A 354 -20.543 241.735 804.439 1.00 79.50 O ANISOU 2341 O LEU A 354 8362 10053 11793 -218 1091 -1998 O ATOM 2342 CB LEU A 354 -18.206 243.375 804.991 1.00 71.07 C ANISOU 2342 CB LEU A 354 7785 8926 10292 -264 935 -1396 C ATOM 2343 CG LEU A 354 -17.310 243.350 806.199 1.00 64.76 C ANISOU 2343 CG LEU A 354 7227 8288 9090 -363 820 -1306 C ATOM 2344 CD2 LEU A 354 -16.899 241.958 806.372 1.00 72.37 C ANISOU 2344 CD2 LEU A 354 8183 9442 9870 -381 764 -1339 C ATOM 2345 CD1 LEU A 354 -18.123 243.789 807.356 1.00 59.74 C ANISOU 2345 CD1 LEU A 354 6603 7694 8400 -487 812 -1497 C ATOM 2346 N TRP A 355 -19.150 240.127 805.080 1.00 55.77 N ANISOU 2346 N TRP A 355 5525 7381 8284 -288 987 -1861 N ATOM 2347 CA TRP A 355 -20.219 239.244 805.514 1.00 64.18 C ANISOU 2347 CA TRP A 355 6420 8603 9363 -349 1072 -2185 C ATOM 2348 C TRP A 355 -20.120 239.037 807.007 1.00 64.16 C ANISOU 2348 C TRP A 355 6575 8806 8999 -526 1014 -2218 C ATOM 2349 O TRP A 355 -19.068 239.256 807.599 1.00 67.94 O ANISOU 2349 O TRP A 355 7270 9315 9231 -577 890 -1994 O ATOM 2350 CB TRP A 355 -20.134 237.888 804.799 1.00 72.31 C ANISOU 2350 CB TRP A 355 7254 9751 10471 -270 1124 -2263 C ATOM 2351 CG TRP A 355 -20.930 237.808 803.530 1.00 70.83 C ANISOU 2351 CG TRP A 355 6762 9407 10743 -93 1208 -2412 C ATOM 2352 CD2 TRP A 355 -20.421 237.887 802.194 1.00 63.66 C ANISOU 2352 CD2 TRP A 355 5727 8331 10130 89 1158 -2223 C ATOM 2353 CE3 TRP A 355 -19.152 238.054 801.651 1.00 58.23 C ANISOU 2353 CE3 TRP A 355 5142 7605 9376 143 1046 -1876 C ATOM 2354 CZ3 TRP A 355 -19.018 238.090 800.280 1.00 78.37 C ANISOU 2354 CZ3 TRP A 355 7473 9996 12310 337 990 -1749 C ATOM 2355 CH2 TRP A 355 -20.131 237.962 799.438 1.00 94.15 C ANISOU 2355 CH2 TRP A 355 9154 11833 14787 502 1034 -1973 C ATOM 2356 CZ2 TRP A 355 -21.391 237.804 799.941 1.00 89.72 C ANISOU 2356 CZ2 TRP A 355 8493 11292 14305 465 1166 -2348 C ATOM 2357 CE2 TRP A 355 -21.531 237.764 801.327 1.00 84.64 C ANISOU 2357 CE2 TRP A 355 8067 10849 13245 246 1232 -2467 C ATOM 2358 NE1 TRP A 355 -22.645 237.616 802.096 1.00 86.28 N ANISOU 2358 NE1 TRP A 355 8222 11154 13406 156 1348 -2807 N ATOM 2359 CD1 TRP A 355 -22.279 237.639 803.419 1.00 87.98 C ANISOU 2359 CD1 TRP A 355 8700 11566 13161 -56 1329 -2757 C ATOM 2360 N LYS A 356 -21.213 238.595 807.614 1.00 72.32 N ANISOU 2360 N LYS A 356 7471 9986 10019 -610 1099 -2497 N ATOM 2361 CA LYS A 356 -21.209 238.311 809.042 1.00 73.12 C ANISOU 2361 CA LYS A 356 7667 10305 9811 -777 1046 -2515 C ATOM 2362 CB LYS A 356 -21.546 239.572 809.839 1.00 65.28 C ANISOU 2362 CB LYS A 356 6755 9244 8803 -842 985 -2496 C ATOM 2363 CG LYS A 356 -22.032 239.303 811.244 1.00 69.00 C ANISOU 2363 CG LYS A 356 7206 9952 9057 -991 974 -2592 C ATOM 2364 CD LYS A 356 -22.256 240.595 812.007 1.00 67.36 C ANISOU 2364 CD LYS A 356 7050 9689 8856 -1036 904 -2551 C ATOM 2365 CE LYS A 356 -23.347 241.448 811.378 1.00 71.38 C ANISOU 2365 CE LYS A 356 7420 10056 9646 -981 1009 -2766 C ATOM 2366 NZ LYS A 356 -23.613 242.677 812.188 1.00 68.77 N ANISOU 2366 NZ LYS A 356 7110 9707 9311 -1031 960 -2751 N ATOM 2367 C LYS A 356 -22.167 237.186 809.418 1.00 75.47 C ANISOU 2367 C LYS A 356 7772 10850 10051 -850 1185 -2802 C ATOM 2368 O LYS A 356 -23.355 237.231 809.102 1.00 79.46 O ANISOU 2368 O LYS A 356 8084 11359 10750 -813 1320 -3083 O ATOM 2369 N SER A 357 -21.633 236.171 810.083 1.00 73.32 N ANISOU 2369 N SER A 357 7549 10791 9520 -953 1167 -2740 N ATOM 2370 CA SER A 357 -22.455 235.147 810.701 1.00 73.22 C ANISOU 2370 CA SER A 357 7389 11057 9375 -1065 1313 -2976 C ATOM 2371 C SER A 357 -22.290 235.261 812.201 1.00 79.18 C ANISOU 2371 C SER A 357 8275 11958 9854 -1226 1229 -2864 C ATOM 2372 O SER A 357 -21.333 234.736 812.769 1.00 79.98 O ANISOU 2372 O SER A 357 8494 12128 9765 -1304 1142 -2666 O ATOM 2373 CB SER A 357 -22.041 233.757 810.241 1.00 74.64 C ANISOU 2373 CB SER A 357 7471 11389 9500 -1068 1403 -3003 C ATOM 2374 OG SER A 357 -22.813 232.770 810.904 1.00 83.78 O ANISOU 2374 OG SER A 357 8496 12845 10493 -1200 1574 -3224 O ATOM 2375 N GLY A 358 -23.222 235.955 812.840 1.00 82.27 N ANISOU 2375 N GLY A 358 8622 12388 10247 -1267 1259 -2994 N ATOM 2376 CA GLY A 358 -23.075 236.276 814.244 1.00 85.23 C ANISOU 2376 CA GLY A 358 9098 12871 10413 -1384 1172 -2860 C ATOM 2377 C GLY A 358 -21.830 237.120 814.431 1.00 84.06 C ANISOU 2377 C GLY A 358 9134 12520 10283 -1343 958 -2536 C ATOM 2378 O GLY A 358 -21.571 238.038 813.657 1.00 71.70 O ANISOU 2378 O GLY A 358 7617 10727 8899 -1236 893 -2474 O ATOM 2379 N THR A 359 -21.049 236.799 815.454 1.00 90.91 N ANISOU 2379 N THR A 359 10101 13468 10971 -1426 870 -2336 N ATOM 2380 CA THR A 359 -19.831 237.544 815.753 1.00 86.65 C ANISOU 2380 CA THR A 359 9752 12745 10426 -1299 750 -2008 C ATOM 2381 C THR A 359 -18.841 237.501 814.588 1.00 79.28 C ANISOU 2381 C THR A 359 8907 11634 9582 -1178 698 -1876 C ATOM 2382 O THR A 359 -18.287 238.530 814.187 1.00 71.52 O ANISOU 2382 O THR A 359 8028 10456 8690 -1044 637 -1718 O ATOM 2383 CB THR A 359 -19.150 236.991 817.020 1.00 91.02 C ANISOU 2383 CB THR A 359 10386 13401 10798 -1381 714 -1836 C ATOM 2384 OG1 THR A 359 -18.691 235.650 816.786 1.00 85.04 O ANISOU 2384 OG1 THR A 359 9617 12746 9948 -1484 739 -1853 O ATOM 2385 CG2 THR A 359 -20.131 236.987 818.183 1.00 88.60 C ANISOU 2385 CG2 THR A 359 9987 13298 10378 -1522 765 -1961 C ATOM 2386 N ALA A 360 -18.631 236.297 814.058 1.00 78.67 N ANISOU 2386 N ALA A 360 8777 11654 9462 -1243 728 -1958 N ATOM 2387 CA ALA A 360 -17.657 236.045 812.996 1.00 66.26 C ANISOU 2387 CA ALA A 360 7266 9971 7939 -1148 679 -1849 C ATOM 2388 C ALA A 360 -17.993 236.769 811.699 1.00 59.91 C ANISOU 2388 C ALA A 360 6431 8992 7342 -1038 685 -1935 C ATOM 2389 O ALA A 360 -19.120 236.718 811.222 1.00 69.43 O ANISOU 2389 O ALA A 360 7485 10214 8679 -1024 816 -2162 O ATOM 2390 CB ALA A 360 -17.549 234.560 812.742 1.00 58.29 C ANISOU 2390 CB ALA A 360 6166 9144 6836 -1256 735 -1971 C ATOM 2391 N SER A 361 -16.999 237.432 811.125 1.00 55.59 N ANISOU 2391 N SER A 361 6016 8273 6832 -912 606 -1714 N ATOM 2392 CA SER A 361 -17.192 238.151 809.874 1.00 65.73 C ANISOU 2392 CA SER A 361 7286 9371 8317 -802 632 -1742 C ATOM 2393 C SER A 361 -16.220 237.657 808.805 1.00 63.12 C ANISOU 2393 C SER A 361 6976 9010 7997 -694 624 -1603 C ATOM 2394 O SER A 361 -15.120 237.190 809.114 1.00 62.83 O ANISOU 2394 O SER A 361 7034 9048 7789 -722 525 -1461 O ATOM 2395 CB SER A 361 -17.057 239.670 810.085 1.00 63.39 C ANISOU 2395 CB SER A 361 7106 8905 8074 -752 582 -1603 C ATOM 2396 OG SER A 361 -15.967 239.999 810.932 1.00 50.34 O ANISOU 2396 OG SER A 361 5597 7266 6263 -715 496 -1342 O ATOM 2397 N LYS A 362 -16.636 237.752 807.550 1.00 54.25 N ANISOU 2397 N LYS A 362 5723 7780 7108 -569 729 -1645 N ATOM 2398 CA LYS A 362 -15.781 237.345 806.442 1.00 54.67 C ANISOU 2398 CA LYS A 362 5738 7815 7217 -453 725 -1494 C ATOM 2399 C LYS A 362 -15.648 238.456 805.411 1.00 56.67 C ANISOU 2399 C LYS A 362 5993 7851 7690 -317 735 -1336 C ATOM 2400 O LYS A 362 -16.648 239.001 804.937 1.00 52.12 O ANISOU 2400 O LYS A 362 5286 7131 7388 -266 821 -1448 O ATOM 2401 CB LYS A 362 -16.331 236.086 805.774 1.00 62.35 C ANISOU 2401 CB LYS A 362 6447 8907 8338 -420 841 -1673 C ATOM 2402 CG LYS A 362 -15.438 235.549 804.671 1.00 71.90 C ANISOU 2402 CG LYS A 362 7555 10134 9628 -310 818 -1512 C ATOM 2403 CD LYS A 362 -16.149 234.473 803.886 1.00 74.00 C ANISOU 2403 CD LYS A 362 7482 10484 10149 -246 931 -1710 C ATOM 2404 CE LYS A 362 -16.685 233.407 804.809 1.00 72.80 C ANISOU 2404 CE LYS A 362 7270 10565 9827 -395 1025 -1944 C ATOM 2405 NZ LYS A 362 -17.937 232.833 804.260 1.00 74.09 N ANISOU 2405 NZ LYS A 362 7102 10766 10283 -331 1182 -2240 N ATOM 2406 N LEU A 363 -14.409 238.787 805.064 1.00 52.99 N ANISOU 2406 N LEU A 363 5651 7368 7114 -266 651 -1075 N ATOM 2407 CA LEU A 363 -14.145 239.839 804.096 1.00 56.35 C ANISOU 2407 CA LEU A 363 6068 7621 7722 -152 665 -875 C ATOM 2408 C LEU A 363 -13.680 239.233 802.792 1.00 66.31 C ANISOU 2408 C LEU A 363 7136 8906 9153 -37 659 -743 C ATOM 2409 O LEU A 363 -12.862 238.315 802.784 1.00 84.16 O ANISOU 2409 O LEU A 363 9394 11337 11247 -57 602 -691 O ATOM 2410 CB LEU A 363 -13.069 240.787 804.608 1.00 62.34 C ANISOU 2410 CB LEU A 363 7067 8371 8248 -174 575 -665 C ATOM 2411 CG LEU A 363 -12.923 242.053 803.766 1.00 69.71 C ANISOU 2411 CG LEU A 363 7990 9141 9356 -85 623 -460 C ATOM 2412 CD1 LEU A 363 -13.820 243.156 804.307 1.00 41.20 C ANISOU 2412 CD1 LEU A 363 4422 5377 5854 -127 686 -564 C ATOM 2413 CD2 LEU A 363 -11.475 242.498 803.742 1.00 85.11 C ANISOU 2413 CD2 LEU A 363 10085 11174 11079 -64 537 -211 C ATOM 2414 N GLN A 364 -14.223 239.710 801.695 1.00 62.49 N ANISOU 2414 N GLN A 364 6454 8250 9039 80 697 -693 N ATOM 2415 CA GLN A 364 -13.846 239.179 800.421 1.00 62.31 C ANISOU 2415 CA GLN A 364 6190 8234 9249 204 631 -554 C ATOM 2416 C GLN A 364 -13.720 240.285 799.450 1.00 64.18 C ANISOU 2416 C GLN A 364 6355 8285 9747 310 589 -303 C ATOM 2417 O GLN A 364 -14.327 241.315 799.598 1.00 64.12 O ANISOU 2417 O GLN A 364 6398 8106 9861 305 660 -319 O ATOM 2418 CB GLN A 364 -14.909 238.242 799.912 1.00 56.45 C ANISOU 2418 CB GLN A 364 5142 7472 8834 283 672 -811 C ATOM 2419 CG GLN A 364 -14.890 236.915 800.550 1.00 59.40 C ANISOU 2419 CG GLN A 364 5491 8079 9001 193 707 -1010 C ATOM 2420 CD GLN A 364 -16.141 236.171 800.301 1.00 71.43 C ANISOU 2420 CD GLN A 364 6728 9597 10814 249 801 -1326 C ATOM 2421 OE1 GLN A 364 -17.037 236.653 799.638 1.00 68.73 O ANISOU 2421 OE1 GLN A 364 6211 9056 10849 371 827 -1414 O ATOM 2422 NE2 GLN A 364 -16.224 234.989 800.839 1.00 79.49 N ANISOU 2422 NE2 GLN A 364 7686 10842 11674 160 861 -1511 N ATOM 2423 N ILE A 365 -12.929 240.057 798.431 1.00 63.18 N ANISOU 2423 N ILE A 365 6085 8199 9721 403 451 -61 N ATOM 2424 CA ILE A 365 -12.775 241.038 797.410 1.00 70.19 C ANISOU 2424 CA ILE A 365 6874 8919 10875 522 357 220 C ATOM 2425 C ILE A 365 -13.033 240.363 796.104 1.00 86.20 C ANISOU 2425 C ILE A 365 8583 10856 13314 719 172 267 C ATOM 2426 O ILE A 365 -12.628 239.238 795.901 1.00 84.32 O ANISOU 2426 O ILE A 365 8231 10784 13024 727 79 223 O ATOM 2427 CB ILE A 365 -11.399 241.534 797.354 1.00 55.92 C ANISOU 2427 CB ILE A 365 5213 7259 8776 471 270 536 C ATOM 2428 CG1 ILE A 365 -11.121 242.348 798.578 1.00 56.59 C ANISOU 2428 CG1 ILE A 365 5607 7398 8496 315 436 502 C ATOM 2429 CD1 ILE A 365 -9.819 242.983 798.513 1.00 58.30 C ANISOU 2429 CD1 ILE A 365 5945 7763 8445 263 390 790 C ATOM 2430 CG2 ILE A 365 -11.253 242.421 796.201 1.00 52.25 C ANISOU 2430 CG2 ILE A 365 4705 6597 8551 592 113 857 C ATOM 2431 N LEU A 366 -13.715 241.047 795.211 1.00 89.05 N ANISOU 2431 N LEU A 366 8801 10929 14105 892 96 359 N ATOM 2432 CA LEU A 366 -13.987 240.478 793.924 1.00 96.25 C ANISOU 2432 CA LEU A 366 9438 11692 15443 1126 -130 423 C ATOM 2433 C LEU A 366 -13.225 241.259 792.888 1.00 97.87 C ANISOU 2433 C LEU A 366 9819 11712 15654 1173 -386 878 C ATOM 2434 O LEU A 366 -13.386 242.446 792.751 1.00101.33 O ANISOU 2434 O LEU A 366 10452 11919 16131 1137 -357 1056 O ATOM 2435 CB LEU A 366 -15.468 240.569 793.624 1.00 97.90 C ANISOU 2435 CB LEU A 366 9460 11608 16128 1263 -49 157 C ATOM 2436 CG LEU A 366 -16.409 239.407 793.916 1.00 97.50 C ANISOU 2436 CG LEU A 366 9198 11639 16209 1269 82 -284 C ATOM 2437 CD1 LEU A 366 -16.611 238.584 792.692 1.00 82.06 C ANISOU 2437 CD1 LEU A 366 6911 9584 14685 1520 -129 -283 C ATOM 2438 CD2 LEU A 366 -16.022 238.559 795.116 1.00 98.89 C ANISOU 2438 CD2 LEU A 366 9508 12170 15896 1035 246 -480 C ATOM 2439 N ASN A 367 -12.388 240.562 792.162 1.00 87.33 N ANISOU 2439 N ASN A 367 8435 10489 14256 1226 -639 1066 N ATOM 2440 CA ASN A 367 -11.614 241.111 791.075 1.00 88.61 C ANISOU 2440 CA ASN A 367 8778 10506 14385 1265 -927 1509 C ATOM 2441 C ASN A 367 -12.412 240.944 789.803 1.00107.98 C ANISOU 2441 C ASN A 367 11009 12618 17401 1521 -1151 1568 C ATOM 2442 O ASN A 367 -12.941 239.867 789.530 1.00120.58 O ANISOU 2442 O ASN A 367 12262 14248 19305 1680 -1204 1320 O ATOM 2443 CB ASN A 367 -10.265 240.419 790.947 1.00 95.10 C ANISOU 2443 CB ASN A 367 9668 11635 14832 1188 -1120 1672 C ATOM 2444 CG ASN A 367 -9.407 241.038 789.868 1.00104.34 C ANISOU 2444 CG ASN A 367 11068 12690 15888 1208 -1421 2141 C ATOM 2445 OD1 ASN A 367 -9.788 242.041 789.265 1.00107.88 O ANISOU 2445 OD1 ASN A 367 11646 12827 16516 1259 -1464 2374 O ATOM 2446 ND2 ASN A 367 -8.245 240.447 789.616 1.00107.07 N ANISOU 2446 ND2 ASN A 367 11473 13284 15924 1154 -1636 2287 N ATOM 2447 N VAL A 368 -12.356 241.962 788.936 1.00112.16 N ANISOU 2447 N VAL A 368 11737 12832 18047 1563 -1314 1936 N ATOM 2448 CA VAL A 368 -13.042 241.943 787.636 1.00117.14 C ANISOU 2448 CA VAL A 368 12209 13073 19228 1816 -1574 2064 C ATOM 2449 C VAL A 368 -12.298 242.466 786.374 1.00129.37 C ANISOU 2449 C VAL A 368 13966 14432 20757 1869 -1942 2606 C ATOM 2450 O VAL A 368 -11.391 243.271 786.488 1.00129.04 O ANISOU 2450 O VAL A 368 14267 14483 20280 1679 -1940 2925 O ATOM 2451 CB VAL A 368 -14.294 242.772 787.766 1.00119.29 C ANISOU 2451 CB VAL A 368 12475 12976 19873 1855 -1388 1914 C ATOM 2452 CG1 VAL A 368 -14.991 242.878 786.453 1.00131.47 C ANISOU 2452 CG1 VAL A 368 13896 14060 21995 2111 -1656 2062 C ATOM 2453 CG2 VAL A 368 -15.192 242.196 788.818 1.00109.47 C ANISOU 2453 CG2 VAL A 368 10999 11881 18714 1848 -1075 1374 C ATOM 2454 N ASN A 369 -12.636 241.917 785.228 1.00136.57 N ANISOU 2454 N ASN A 369 14657 15122 22112 2127 -2255 2689 N ATOM 2455 CA ASN A 369 -11.981 242.300 783.999 1.00144.82 C ANISOU 2455 CA ASN A 369 15883 15987 23153 2197 -2644 3205 C ATOM 2456 C ASN A 369 -12.772 243.288 783.215 1.00139.68 C ANISOU 2456 C ASN A 369 15342 14803 22926 2302 -2732 3442 C ATOM 2457 O ASN A 369 -13.982 243.373 783.334 1.00139.93 O ANISOU 2457 O ASN A 369 15194 14549 23423 2418 -2581 3151 O ATOM 2458 CB ASN A 369 -11.687 241.067 783.146 1.00161.98 C ANISOU 2458 CB ASN A 369 17758 18259 25526 2418 -3009 3214 C ATOM 2459 CG ASN A 369 -11.143 239.908 783.960 1.00169.71 C ANISOU 2459 CG ASN A 369 18539 19733 26209 2324 -2896 2889 C ATOM 2460 OD1 ASN A 369 -10.343 239.113 783.472 1.00179.65 O ANISOU 2460 OD1 ASN A 369 19697 21210 27351 2364 -3185 3000 O ATOM 2461 ND2 ASN A 369 -11.577 239.809 785.211 1.00161.38 N ANISOU 2461 ND2 ASN A 369 17431 18853 25034 2186 -2488 2492 N ATOM 2462 N ASP A 370 -12.107 244.030 782.366 1.00138.08 N ANISOU 2462 N ASP A 370 15443 14448 22574 2259 -2990 3975 N ATOM 2463 CA ASP A 370 -12.901 244.947 781.626 1.00143.32 C ANISOU 2463 CA ASP A 370 16212 14572 23672 2345 -3074 4208 C ATOM 2464 C ASP A 370 -13.742 243.885 780.981 1.00142.90 C ANISOU 2464 C ASP A 370 15732 14322 24243 2696 -3283 3942 C ATOM 2465 O ASP A 370 -13.412 242.699 781.030 1.00135.85 O ANISOU 2465 O ASP A 370 14564 13747 23305 2802 -3380 3730 O ATOM 2466 CB ASP A 370 -12.115 245.751 780.602 1.00152.19 C ANISOU 2466 CB ASP A 370 17696 15529 24601 2285 -3386 4863 C ATOM 2467 CG ASP A 370 -12.857 247.004 780.169 1.00156.11 C ANISOU 2467 CG ASP A 370 18400 15495 25420 2245 -3348 5124 C ATOM 2468 OD1 ASP A 370 -14.100 246.991 780.194 1.00157.39 O ANISOU 2468 OD1 ASP A 370 18345 15299 26156 2394 -3252 4821 O ATOM 2469 OD2 ASP A 370 -12.207 248.004 779.812 1.00156.82 O ANISOU 2469 OD2 ASP A 370 18869 15526 25189 2051 -3403 5620 O ATOM 2470 N GLU A 371 -14.755 244.343 780.262 1.00142.30 N ANISOU 2470 N GLU A 371 15611 13700 24758 2879 -3387 3999 N ATOM 2471 CA GLU A 371 -15.772 243.469 779.747 1.00130.75 C ANISOU 2471 CA GLU A 371 13726 11990 23963 3229 -3514 3664 C ATOM 2472 C GLU A 371 -16.702 243.415 780.927 1.00124.97 C ANISOU 2472 C GLU A 371 12834 11337 23310 3152 -3054 3086 C ATOM 2473 O GLU A 371 -17.755 242.779 780.882 1.00128.84 O ANISOU 2473 O GLU A 371 12972 11670 24311 3388 -2995 2651 O ATOM 2474 CB GLU A 371 -15.201 242.085 779.450 1.00121.94 C ANISOU 2474 CB GLU A 371 12292 11232 22808 3399 -3747 3556 C ATOM 2475 CG GLU A 371 -14.164 242.068 778.339 1.00145.73 C ANISOU 2475 CG GLU A 371 15429 14179 25762 3505 -4261 4110 C ATOM 2476 CD GLU A 371 -14.704 242.613 777.030 1.00162.38 C ANISOU 2476 CD GLU A 371 17217 16695 27783 3627 -4484 3985 C ATOM 2477 OE1 GLU A 371 -15.869 242.314 776.696 1.00170.98 O ANISOU 2477 OE1 GLU A 371 18037 18160 28768 3572 -4202 3506 O ATOM 2478 OE2 GLU A 371 -13.961 243.339 776.337 1.00161.68 O ANISOU 2478 OE2 GLU A 371 17147 16553 27730 3766 -4951 4376 O ATOM 2479 N SER A 372 -16.305 244.100 782.000 1.00110.35 N ANISOU 2479 N SER A 372 11246 9741 20940 2821 -2727 3074 N ATOM 2480 CA SER A 372 -17.157 244.119 783.163 1.00108.25 C ANISOU 2480 CA SER A 372 10862 9563 20707 2729 -2311 2554 C ATOM 2481 C SER A 372 -17.467 242.667 783.361 1.00112.82 C ANISOU 2481 C SER A 372 11013 10410 21444 2923 -2283 2094 C ATOM 2482 O SER A 372 -18.590 242.277 783.615 1.00120.69 O ANISOU 2482 O SER A 372 11738 11287 22830 3065 -2114 1630 O ATOM 2483 CB SER A 372 -18.421 244.927 782.912 1.00 99.39 C ANISOU 2483 CB SER A 372 9751 7886 20126 2806 -2243 2451 C ATOM 2484 OG SER A 372 -19.072 245.257 784.119 1.00 82.39 O ANISOU 2484 OG SER A 372 7592 5839 17872 2634 -1842 2038 O ATOM 2485 N PHE A 373 -16.446 241.855 783.226 1.00108.41 N ANISOU 2485 N PHE A 373 10392 10226 20573 2918 -2451 2221 N ATOM 2486 CA PHE A 373 -16.626 240.424 783.360 1.00112.91 C ANISOU 2486 CA PHE A 373 10538 11084 21280 3076 -2439 1824 C ATOM 2487 C PHE A 373 -16.018 239.530 782.275 1.00136.32 C ANISOU 2487 C PHE A 373 13291 14106 24398 3291 -2860 2034 C ATOM 2488 O PHE A 373 -16.645 238.612 781.793 1.00139.73 O ANISOU 2488 O PHE A 373 13313 14475 25303 3564 -2955 1763 O ATOM 2489 CB PHE A 373 -18.087 240.068 783.604 1.00105.02 C ANISOU 2489 CB PHE A 373 9216 9894 20792 3257 -2212 1285 C ATOM 2490 CG PHE A 373 -18.365 238.625 783.481 1.00104.30 C ANISOU 2490 CG PHE A 373 8651 10035 20944 3464 -2230 910 C ATOM 2491 CD1 PHE A 373 -17.392 237.703 783.759 1.00109.73 C ANISOU 2491 CD1 PHE A 373 9234 11208 21252 3362 -2274 929 C ATOM 2492 CE1 PHE A 373 -17.626 236.399 783.631 1.00106.22 C ANISOU 2492 CE1 PHE A 373 8340 10984 21036 3525 -2282 603 C ATOM 2493 CZ PHE A 373 -18.851 235.985 783.260 1.00106.27 C ANISOU 2493 CZ PHE A 373 7986 10753 21638 3808 -2221 225 C ATOM 2494 CE2 PHE A 373 -19.836 236.886 782.996 1.00109.26 C ANISOU 2494 CE2 PHE A 373 8478 10640 22396 3929 -2178 177 C ATOM 2495 CD2 PHE A 373 -19.598 238.190 783.116 1.00103.65 C ANISOU 2495 CD2 PHE A 373 8221 9694 21467 3748 -2185 521 C ATOM 2496 N LYS A 374 -14.787 239.819 781.885 1.00147.55 N ANISOU 2496 N LYS A 374 14991 15660 25413 3167 -3115 2512 N ATOM 2497 CA LYS A 374 -14.097 239.020 780.895 1.00151.43 C ANISOU 2497 CA LYS A 374 15314 16242 25980 3337 -3547 2739 C ATOM 2498 C LYS A 374 -14.012 237.721 781.675 1.00144.18 C ANISOU 2498 C LYS A 374 14040 15797 24945 3298 -3354 2279 C ATOM 2499 O LYS A 374 -14.153 236.626 781.158 1.00143.97 O ANISOU 2499 O LYS A 374 13602 15855 25243 3513 -3535 2111 O ATOM 2500 CB LYS A 374 -12.731 239.579 780.494 1.00150.90 C ANISOU 2500 CB LYS A 374 15649 16297 25388 3162 -3818 3300 C ATOM 2501 N ASN A 375 -13.771 237.900 782.963 1.00139.80 N ANISOU 2501 N ASN A 375 13657 15548 23914 3006 -2974 2090 N ATOM 2502 CA ASN A 375 -13.678 236.838 783.938 1.00136.54 C ANISOU 2502 CA ASN A 375 12999 15584 23298 2890 -2719 1676 C ATOM 2503 C ASN A 375 -13.608 237.524 785.297 1.00120.54 C ANISOU 2503 C ASN A 375 11279 13717 20804 2587 -2312 1557 C ATOM 2504 O ASN A 375 -13.342 238.725 785.378 1.00117.11 O ANISOU 2504 O ASN A 375 11234 13119 20145 2457 -2285 1846 O ATOM 2505 CB ASN A 375 -12.469 235.933 783.695 1.00148.46 C ANISOU 2505 CB ASN A 375 14424 17467 24519 2826 -2983 1821 C ATOM 2506 CG ASN A 375 -12.660 235.014 782.503 1.00166.65 C ANISOU 2506 CG ASN A 375 16308 19681 27332 3137 -3355 1827 C ATOM 2507 OD1 ASN A 375 -13.786 234.722 782.104 1.00176.62 O ANISOU 2507 OD1 ASN A 375 17239 20698 29173 3402 -3321 1571 O ATOM 2508 ND2 ASN A 375 -11.554 234.552 781.929 1.00170.44 N ANISOU 2508 ND2 ASN A 375 16791 20362 27605 3114 -3720 2102 N ATOM 2509 N TYR A 376 -13.860 236.769 786.356 1.00114.63 N ANISOU 2509 N TYR A 376 10348 13289 19919 2475 -1998 1139 N ATOM 2510 CA TYR A 376 -13.781 237.312 787.704 1.00109.50 C ANISOU 2510 CA TYR A 376 9963 12814 18829 2202 -1634 1010 C ATOM 2511 C TYR A 376 -13.102 236.324 788.645 1.00106.79 C ANISOU 2511 C TYR A 376 9541 12949 18085 2005 -1493 815 C ATOM 2512 O TYR A 376 -13.291 235.116 788.526 1.00108.04 O ANISOU 2512 O TYR A 376 9343 13286 18424 2077 -1509 573 O ATOM 2513 CB TYR A 376 -15.176 237.668 788.226 1.00109.20 C ANISOU 2513 CB TYR A 376 9833 12572 19085 2259 -1323 649 C ATOM 2514 CG TYR A 376 -16.099 236.482 788.405 1.00111.45 C ANISOU 2514 CG TYR A 376 9696 12976 19673 2375 -1161 163 C ATOM 2515 CD1 TYR A 376 -17.140 236.248 787.516 1.00119.67 C ANISOU 2515 CD1 TYR A 376 10434 13707 21329 2674 -1253 -6 C ATOM 2516 CE1 TYR A 376 -17.986 235.166 787.676 1.00122.95 C ANISOU 2516 CE1 TYR A 376 10501 14243 21974 2738 -1073 -477 C ATOM 2517 CZ TYR A 376 -17.800 234.304 788.738 1.00115.55 C ANISOU 2517 CZ TYR A 376 9547 13728 20628 2481 -804 -750 C ATOM 2518 OH TYR A 376 -18.639 233.225 788.906 1.00111.94 O ANISOU 2518 OH TYR A 376 8757 13409 20368 2532 -612 -1205 O ATOM 2519 CE2 TYR A 376 -16.775 234.513 789.634 1.00107.41 C ANISOU 2519 CE2 TYR A 376 8844 12971 18997 2180 -729 -567 C ATOM 2520 CD2 TYR A 376 -15.935 235.597 789.467 1.00107.22 C ANISOU 2520 CD2 TYR A 376 9134 12836 18768 2136 -902 -132 C ATOM 2521 N GLU A 377 -12.300 236.839 789.570 1.00101.75 N ANISOU 2521 N GLU A 377 9246 12505 16909 1742 -1353 920 N ATOM 2522 CA GLU A 377 -11.680 235.997 790.585 1.00 97.32 C ANISOU 2522 CA GLU A 377 8668 12351 15958 1530 -1199 736 C ATOM 2523 C GLU A 377 -12.142 236.430 791.968 1.00 98.66 C ANISOU 2523 C GLU A 377 9058 12575 15854 1322 -799 489 C ATOM 2524 O GLU A 377 -12.339 237.619 792.215 1.00103.07 O ANISOU 2524 O GLU A 377 9833 12964 16364 1305 -710 600 O ATOM 2525 CB GLU A 377 -10.152 236.058 790.494 1.00 98.94 C ANISOU 2525 CB GLU A 377 9132 12749 15712 1378 -1419 1060 C ATOM 2526 CG GLU A 377 -9.444 235.195 791.533 1.00102.47 C ANISOU 2526 CG GLU A 377 9590 13575 15768 1146 -1282 882 C ATOM 2527 CD GLU A 377 -7.979 234.942 791.211 1.00101.07 C ANISOU 2527 CD GLU A 377 9565 13589 15249 1039 -1568 1144 C ATOM 2528 OE1 GLU A 377 -7.591 235.071 790.028 1.00 88.43 O ANISOU 2528 OE1 GLU A 377 7961 11871 13768 1169 -1910 1423 O ATOM 2529 OE2 GLU A 377 -7.221 234.600 792.148 1.00101.02 O ANISOU 2529 OE2 GLU A 377 9696 13839 14847 819 -1461 1065 O ATOM 2530 N TRP A 378 -12.336 235.464 792.860 1.00 95.67 N ANISOU 2530 N TRP A 378 8632 12421 15298 1168 -574 166 N ATOM 2531 CA TRP A 378 -12.640 235.767 794.253 1.00 80.62 C ANISOU 2531 CA TRP A 378 6994 10588 13050 958 -251 -38 C ATOM 2532 C TRP A 378 -11.362 235.724 795.078 1.00 72.10 C ANISOU 2532 C TRP A 378 6198 9758 11438 739 -241 98 C ATOM 2533 O TRP A 378 -10.587 234.774 794.988 1.00 74.31 O ANISOU 2533 O TRP A 378 6393 10250 11592 678 -354 123 O ATOM 2534 CB TRP A 378 -13.654 234.775 794.825 1.00 80.43 C ANISOU 2534 CB TRP A 378 6812 10645 13104 922 -30 -457 C ATOM 2535 CG TRP A 378 -15.072 235.082 794.483 1.00 83.43 C ANISOU 2535 CG TRP A 378 7017 10775 13906 1080 64 -684 C ATOM 2536 CD1 TRP A 378 -15.734 234.709 793.357 1.00 98.10 C ANISOU 2536 CD1 TRP A 378 8511 12473 16289 1330 -59 -761 C ATOM 2537 NE1 TRP A 378 -17.028 235.166 793.395 1.00101.82 N ANISOU 2537 NE1 TRP A 378 8921 12718 17050 1421 86 -1010 N ATOM 2538 CE2 TRP A 378 -17.223 235.851 794.563 1.00 90.45 C ANISOU 2538 CE2 TRP A 378 7803 11305 15259 1212 293 -1087 C ATOM 2539 CZ2 TRP A 378 -18.359 236.493 795.046 1.00 85.00 C ANISOU 2539 CZ2 TRP A 378 7176 10451 14670 1192 467 -1329 C ATOM 2540 CH2 TRP A 378 -18.266 237.106 796.265 1.00 87.51 C ANISOU 2540 CH2 TRP A 378 7832 10851 14566 962 611 -1345 C ATOM 2541 CZ3 TRP A 378 -17.079 237.092 797.004 1.00 93.07 C ANISOU 2541 CZ3 TRP A 378 8821 11773 14770 776 595 -1136 C ATOM 2542 CE3 TRP A 378 -15.944 236.452 796.522 1.00 94.58 C ANISOU 2542 CE3 TRP A 378 8957 12119 14861 797 444 -913 C ATOM 2543 CD2 TRP A 378 -16.009 235.817 795.278 1.00 87.42 C ANISOU 2543 CD2 TRP A 378 7696 11155 14363 1007 282 -882 C ATOM 2544 N ILE A 379 -11.139 236.763 795.874 1.00 76.06 N ANISOU 2544 N ILE A 379 7020 10228 11650 625 -112 176 N ATOM 2545 CA ILE A 379 -9.999 236.789 796.778 1.00 73.68 C ANISOU 2545 CA ILE A 379 7002 10138 10856 435 -77 261 C ATOM 2546 C ILE A 379 -10.466 236.728 798.223 1.00 77.65 C ANISOU 2546 C ILE A 379 7745 10683 11077 291 171 3 C ATOM 2547 O ILE A 379 -11.373 237.451 798.626 1.00 79.10 O ANISOU 2547 O ILE A 379 8016 10704 11333 302 303 -112 O ATOM 2548 CB ILE A 379 -9.137 238.037 796.582 1.00 65.50 C ANISOU 2548 CB ILE A 379 6154 9073 9660 427 -170 581 C ATOM 2549 CG1 ILE A 379 -8.746 238.193 795.112 1.00 68.29 C ANISOU 2549 CG1 ILE A 379 6329 9351 10267 600 -499 881 C ATOM 2550 CD1 ILE A 379 -7.991 237.006 794.548 1.00 70.59 C ANISOU 2550 CD1 ILE A 379 6464 9823 10533 600 -744 923 C ATOM 2551 CG2 ILE A 379 -7.907 237.954 797.458 1.00 63.13 C ANISOU 2551 CG2 ILE A 379 6107 9002 8878 248 -148 634 C ATOM 2552 N GLU A 380 -9.839 235.852 798.996 1.00 82.93 N ANISOU 2552 N GLU A 380 8515 11561 11432 157 193 -79 N ATOM 2553 CA GLU A 380 -10.189 235.662 800.395 1.00 81.06 C ANISOU 2553 CA GLU A 380 8511 11377 10912 32 342 -298 C ATOM 2554 C GLU A 380 -9.212 236.392 801.309 1.00 75.47 C ANISOU 2554 C GLU A 380 8150 10714 9810 -64 322 -171 C ATOM 2555 O GLU A 380 -8.271 237.035 800.839 1.00 79.24 O ANISOU 2555 O GLU A 380 8681 11209 10218 -47 239 71 O ATOM 2556 CB GLU A 380 -10.194 234.169 800.724 1.00 78.07 C ANISOU 2556 CB GLU A 380 7998 11194 10470 -53 368 -479 C ATOM 2557 CG GLU A 380 -11.348 233.397 800.097 1.00 65.41 C ANISOU 2557 CG GLU A 380 6045 9570 9238 34 429 -694 C ATOM 2558 CD GLU A 380 -12.623 233.535 800.900 1.00 71.73 C ANISOU 2558 CD GLU A 380 6907 10305 10043 0 594 -967 C ATOM 2559 OE1 GLU A 380 -12.638 234.333 801.860 1.00 86.82 O ANISOU 2559 OE1 GLU A 380 9123 12157 11709 -77 620 -960 O ATOM 2560 OE2 GLU A 380 -13.609 232.846 800.585 1.00 70.76 O ANISOU 2560 OE2 GLU A 380 6507 10202 10175 49 680 -1199 O ATOM 2561 N SER A 381 -9.439 236.287 802.613 1.00 67.37 N ANISOU 2561 N SER A 381 7332 9716 8549 -162 367 -342 N ATOM 2562 CA SER A 381 -8.569 236.924 803.593 1.00 60.78 C ANISOU 2562 CA SER A 381 6782 8904 7406 -233 285 -272 C ATOM 2563 C SER A 381 -8.649 236.177 804.911 1.00 62.87 C ANISOU 2563 C SER A 381 7141 9256 7491 -365 251 -460 C ATOM 2564 O SER A 381 -9.652 235.527 805.201 1.00 73.54 O ANISOU 2564 O SER A 381 8396 10623 8923 -403 336 -652 O ATOM 2565 CB SER A 381 -8.991 238.364 803.823 1.00 56.23 C ANISOU 2565 CB SER A 381 6333 8143 6887 -184 299 -233 C ATOM 2566 OG SER A 381 -10.235 238.398 804.491 1.00 67.96 O ANISOU 2566 OG SER A 381 7819 9537 8466 -218 365 -448 O ATOM 2567 N VAL A 382 -7.596 236.274 805.712 1.00 51.62 N ANISOU 2567 N VAL A 382 5855 7886 5873 -447 113 -410 N ATOM 2568 CA VAL A 382 -7.588 235.625 807.012 1.00 43.74 C ANISOU 2568 CA VAL A 382 4877 6895 4847 -562 130 -500 C ATOM 2569 C VAL A 382 -8.508 236.406 807.919 1.00 46.85 C ANISOU 2569 C VAL A 382 5327 7140 5334 -555 160 -568 C ATOM 2570 O VAL A 382 -8.285 237.583 808.163 1.00 62.32 O ANISOU 2570 O VAL A 382 7366 8957 7356 -493 135 -474 O ATOM 2571 CB VAL A 382 -6.192 235.591 807.614 1.00 47.03 C ANISOU 2571 CB VAL A 382 5348 7283 5237 -610 107 -369 C ATOM 2572 CG1 VAL A 382 -6.154 234.617 808.771 1.00 58.08 C ANISOU 2572 CG1 VAL A 382 6750 8730 6590 -741 147 -441 C ATOM 2573 CG2 VAL A 382 -5.185 235.195 806.564 1.00 45.96 C ANISOU 2573 CG2 VAL A 382 5160 7280 5023 -618 71 -261 C ATOM 2574 N ASN A 383 -9.551 235.752 808.407 1.00 58.93 N ANISOU 2574 N ASN A 383 6795 8731 6865 -632 221 -742 N ATOM 2575 CA ASN A 383 -10.607 236.459 809.113 1.00 73.22 C ANISOU 2575 CA ASN A 383 8623 10443 8754 -637 258 -820 C ATOM 2576 C ASN A 383 -10.386 236.535 810.615 1.00 70.35 C ANISOU 2576 C ASN A 383 8315 10051 8364 -689 264 -757 C ATOM 2577 O ASN A 383 -11.275 236.934 811.365 1.00 65.96 O ANISOU 2577 O ASN A 383 7753 9471 7838 -715 298 -824 O ATOM 2578 CB ASN A 383 -11.963 235.850 808.775 1.00 95.32 C ANISOU 2578 CB ASN A 383 11296 13324 11598 -698 336 -1080 C ATOM 2579 CG ASN A 383 -12.369 236.124 807.343 1.00105.15 C ANISOU 2579 CG ASN A 383 12447 14490 13013 -561 428 -1087 C ATOM 2580 OD1 ASN A 383 -12.391 237.275 806.906 1.00 99.84 O ANISOU 2580 OD1 ASN A 383 11836 13659 12441 -470 420 -987 O ATOM 2581 ND2 ASN A 383 -12.685 235.067 806.601 1.00111.64 N ANISOU 2581 ND2 ASN A 383 13075 15417 13925 -537 537 -1180 N ATOM 2582 N LYS A 384 -9.167 236.222 811.022 1.00 74.09 N ANISOU 2582 N LYS A 384 8837 10523 8789 -706 231 -637 N ATOM 2583 CA LYS A 384 -8.727 236.319 812.401 1.00 60.47 C ANISOU 2583 CA LYS A 384 7174 8748 7055 -746 231 -579 C ATOM 2584 C LYS A 384 -7.311 236.906 812.447 1.00 51.79 C ANISOU 2584 C LYS A 384 6150 7540 5987 -685 182 -444 C ATOM 2585 O LYS A 384 -6.522 236.678 811.569 1.00 53.09 O ANISOU 2585 O LYS A 384 6306 7735 6132 -674 159 -400 O ATOM 2586 CB LYS A 384 -8.761 234.946 813.054 1.00 46.11 C ANISOU 2586 CB LYS A 384 5315 7075 5129 -905 273 -647 C ATOM 2587 CG LYS A 384 -9.973 234.684 813.883 1.00 46.47 C ANISOU 2587 CG LYS A 384 5316 7201 5140 -997 329 -765 C ATOM 2588 CD LYS A 384 -10.261 233.207 814.020 1.00 66.70 C ANISOU 2588 CD LYS A 384 7802 9969 7572 -1183 389 -883 C ATOM 2589 CE LYS A 384 -11.524 232.976 814.834 1.00 72.65 C ANISOU 2589 CE LYS A 384 8497 10833 8274 -1301 456 -1022 C ATOM 2590 NZ LYS A 384 -12.405 231.889 814.336 1.00 69.69 N ANISOU 2590 NZ LYS A 384 7981 10679 7818 -1441 537 -1239 N ATOM 2591 N SER A 385 -6.988 237.665 813.471 1.00 35.64 N ANISOU 2591 N SER A 385 4166 5389 3986 -655 172 -397 N ATOM 2592 CA SER A 385 -5.652 238.224 813.618 1.00 26.34 C ANISOU 2592 CA SER A 385 3045 4125 2839 -616 143 -316 C ATOM 2593 C SER A 385 -4.634 237.114 813.864 1.00 42.25 C ANISOU 2593 C SER A 385 5077 6195 4781 -729 151 -306 C ATOM 2594 O SER A 385 -4.989 236.009 814.279 1.00 40.92 O ANISOU 2594 O SER A 385 4893 6118 4537 -845 179 -352 O ATOM 2595 CB SER A 385 -5.620 239.198 814.784 1.00 40.44 C ANISOU 2595 CB SER A 385 4875 5813 4678 -570 139 -295 C ATOM 2596 OG SER A 385 -5.316 238.522 815.987 1.00 44.58 O ANISOU 2596 OG SER A 385 5430 6347 5161 -656 157 -302 O ATOM 2597 N LEU A 386 -3.365 237.396 813.593 1.00 56.66 N ANISOU 2597 N LEU A 386 6937 7978 6611 -725 132 -257 N ATOM 2598 CA LEU A 386 -2.314 236.451 813.942 1.00 49.05 C ANISOU 2598 CA LEU A 386 6021 7046 5572 -861 141 -248 C ATOM 2599 C LEU A 386 -2.285 236.288 815.453 1.00 46.33 C ANISOU 2599 C LEU A 386 5754 6633 5216 -923 162 -257 C ATOM 2600 O LEU A 386 -2.089 235.187 815.958 1.00 42.90 O ANISOU 2600 O LEU A 386 5366 6245 4688 -1076 180 -268 O ATOM 2601 CB LEU A 386 -0.949 236.930 813.450 1.00 44.51 C ANISOU 2601 CB LEU A 386 5482 6433 4997 -868 122 -206 C ATOM 2602 CG LEU A 386 0.219 236.070 813.936 1.00 36.33 C ANISOU 2602 CG LEU A 386 4543 5389 3871 -1037 132 -196 C ATOM 2603 CD1 LEU A 386 0.424 234.903 813.004 1.00 37.44 C ANISOU 2603 CD1 LEU A 386 4637 5682 3907 -1159 120 -186 C ATOM 2604 CD2 LEU A 386 1.499 236.875 814.098 1.00 39.31 C ANISOU 2604 CD2 LEU A 386 5016 5660 4261 -1051 129 -175 C ATOM 2605 N VAL A 387 -2.472 237.392 816.170 1.00 39.10 N ANISOU 2605 N VAL A 387 4859 5616 4381 -821 158 -247 N ATOM 2606 CA VAL A 387 -2.539 237.342 817.624 1.00 39.90 C ANISOU 2606 CA VAL A 387 5031 5658 4472 -868 174 -248 C ATOM 2607 C VAL A 387 -3.628 236.368 818.059 1.00 46.97 C ANISOU 2607 C VAL A 387 5901 6651 5293 -972 197 -287 C ATOM 2608 O VAL A 387 -3.380 235.467 818.858 1.00 56.46 O ANISOU 2608 O VAL A 387 7187 7862 6402 -1128 214 -287 O ATOM 2609 CB VAL A 387 -2.830 238.719 818.226 1.00 34.39 C ANISOU 2609 CB VAL A 387 4318 4882 3865 -735 162 -236 C ATOM 2610 CG1 VAL A 387 -3.040 238.620 819.733 1.00 33.86 C ANISOU 2610 CG1 VAL A 387 4316 4772 3777 -787 177 -235 C ATOM 2611 CG2 VAL A 387 -1.704 239.671 817.921 1.00 35.79 C ANISOU 2611 CG2 VAL A 387 4522 4987 4090 -672 151 -212 C ATOM 2612 N ASP A 388 -4.833 236.554 817.531 1.00 43.11 N ANISOU 2612 N ASP A 388 5317 6235 4827 -912 200 -325 N ATOM 2613 CA ASP A 388 -5.942 235.648 817.816 1.00 47.00 C ANISOU 2613 CA ASP A 388 5768 6857 5235 -1031 235 -389 C ATOM 2614 C ASP A 388 -5.557 234.194 817.555 1.00 56.07 C ANISOU 2614 C ASP A 388 6926 8120 6260 -1211 257 -413 C ATOM 2615 O ASP A 388 -5.690 233.342 818.433 1.00 54.79 O ANISOU 2615 O ASP A 388 6814 8015 5988 -1390 282 -430 O ATOM 2616 CB ASP A 388 -7.178 236.023 816.993 1.00 38.52 C ANISOU 2616 CB ASP A 388 4596 5845 4196 -952 242 -448 C ATOM 2617 CG ASP A 388 -7.764 237.357 817.395 1.00 51.72 C ANISOU 2617 CG ASP A 388 6265 7432 5953 -830 226 -436 C ATOM 2618 OD1 ASP A 388 -7.556 237.763 818.558 1.00 48.43 O ANISOU 2618 OD1 ASP A 388 5892 6963 5546 -832 220 -404 O ATOM 2619 OD2 ASP A 388 -8.433 237.994 816.552 1.00 61.33 O ANISOU 2619 OD2 ASP A 388 7441 8643 7219 -746 220 -460 O ATOM 2620 N LEU A 389 -5.077 233.916 816.347 1.00 51.81 N ANISOU 2620 N LEU A 389 6342 7625 5718 -1187 244 -409 N ATOM 2621 CA LEU A 389 -4.667 232.565 815.971 1.00 59.49 C ANISOU 2621 CA LEU A 389 7305 8735 6562 -1363 260 -430 C ATOM 2622 C LEU A 389 -3.700 231.951 816.978 1.00 65.20 C ANISOU 2622 C LEU A 389 8170 9408 7196 -1538 259 -384 C ATOM 2623 O LEU A 389 -3.857 230.801 817.383 1.00 69.45 O ANISOU 2623 O LEU A 389 8734 10063 7591 -1753 285 -413 O ATOM 2624 CB LEU A 389 -4.036 232.555 814.576 1.00 58.12 C ANISOU 2624 CB LEU A 389 7076 8603 6405 -1299 232 -406 C ATOM 2625 CG LEU A 389 -4.970 232.312 813.391 1.00 49.62 C ANISOU 2625 CG LEU A 389 5866 7665 5322 -1246 243 -476 C ATOM 2626 CD1 LEU A 389 -6.397 232.687 813.737 1.00 52.14 C ANISOU 2626 CD1 LEU A 389 6141 7987 5682 -1196 274 -559 C ATOM 2627 CD2 LEU A 389 -4.479 233.066 812.164 1.00 42.94 C ANISOU 2627 CD2 LEU A 389 4996 6774 4547 -1097 198 -416 C ATOM 2628 N GLN A 390 -2.707 232.726 817.388 1.00 65.42 N ANISOU 2628 N GLN A 390 8304 9262 7292 -1465 232 -320 N ATOM 2629 CA GLN A 390 -1.668 232.211 818.267 1.00 64.06 C ANISOU 2629 CA GLN A 390 8313 8997 7028 -1630 224 -276 C ATOM 2630 C GLN A 390 -2.213 231.678 819.585 1.00 65.83 C ANISOU 2630 C GLN A 390 8641 9215 7156 -1786 239 -281 C ATOM 2631 O GLN A 390 -1.746 230.656 820.077 1.00 70.64 O ANISOU 2631 O GLN A 390 9391 9835 7613 -2018 232 -259 O ATOM 2632 CB GLN A 390 -0.601 233.273 818.511 1.00 69.98 C ANISOU 2632 CB GLN A 390 9167 9553 7868 -1511 202 -230 C ATOM 2633 CG GLN A 390 0.260 233.522 817.285 1.00 81.68 C ANISOU 2633 CG GLN A 390 10604 11053 9378 -1460 184 -214 C ATOM 2634 CD GLN A 390 1.341 234.547 817.525 1.00 90.81 C ANISOU 2634 CD GLN A 390 11873 12036 10594 -1382 176 -186 C ATOM 2635 OE1 GLN A 390 1.227 235.387 818.420 1.00 89.40 O ANISOU 2635 OE1 GLN A 390 11749 11736 10484 -1285 185 -184 O ATOM 2636 NE2 GLN A 390 2.400 234.488 816.723 1.00100.78 N ANISOU 2636 NE2 GLN A 390 13178 13297 11818 -1438 160 -166 N ATOM 2637 N SER A 391 -3.203 232.355 820.149 1.00 66.66 N ANISOU 2637 N SER A 391 8691 9306 7329 -1687 252 -302 N ATOM 2638 CA SER A 391 -3.790 231.895 821.404 1.00 70.01 C ANISOU 2638 CA SER A 391 9217 9738 7646 -1856 263 -302 C ATOM 2639 C SER A 391 -4.618 230.614 821.215 1.00 73.51 C ANISOU 2639 C SER A 391 9592 10410 7930 -2083 299 -364 C ATOM 2640 O SER A 391 -4.605 229.731 822.073 1.00 81.40 O ANISOU 2640 O SER A 391 10732 11436 8760 -2341 298 -346 O ATOM 2641 CB SER A 391 -4.620 233.006 822.063 1.00 69.56 C ANISOU 2641 CB SER A 391 9110 9627 7692 -1705 264 -307 C ATOM 2642 OG SER A 391 -5.707 233.406 821.243 1.00 73.62 O ANISOU 2642 OG SER A 391 9425 10269 8280 -1578 285 -371 O ATOM 2643 N GLU A 392 -5.320 230.517 820.087 1.00 70.35 N ANISOU 2643 N GLU A 392 8995 10170 7567 -2004 330 -440 N ATOM 2644 CA GLU A 392 -6.174 229.364 819.797 1.00 76.41 C ANISOU 2644 CA GLU A 392 9664 11184 8183 -2206 382 -536 C ATOM 2645 C GLU A 392 -5.358 228.110 819.535 1.00 87.39 C ANISOU 2645 C GLU A 392 11113 12674 9416 -2437 381 -522 C ATOM 2646 O GLU A 392 -5.567 227.065 820.160 1.00 88.63 O ANISOU 2646 O GLU A 392 11338 12958 9381 -2729 405 -542 O ATOM 2647 CB GLU A 392 -7.048 229.623 818.566 1.00 74.56 C ANISOU 2647 CB GLU A 392 9225 11070 8032 -2045 411 -636 C ATOM 2648 CG GLU A 392 -8.290 230.460 818.811 1.00 84.04 C ANISOU 2648 CG GLU A 392 10350 12270 9312 -1927 431 -696 C ATOM 2649 CD GLU A 392 -9.211 230.485 817.603 1.00 86.36 C ANISOU 2649 CD GLU A 392 10476 12688 9650 -1832 464 -822 C ATOM 2650 OE1 GLU A 392 -9.637 229.397 817.151 1.00 76.30 O ANISOU 2650 OE1 GLU A 392 9107 11627 8256 -1994 521 -945 O ATOM 2651 OE2 GLU A 392 -9.509 231.594 817.111 1.00 91.13 O ANISOU 2651 OE2 GLU A 392 11049 13177 10401 -1612 436 -810 O ATOM 2652 N HIS A 393 -4.431 228.219 818.591 1.00 91.21 N ANISOU 2652 N HIS A 393 11575 13117 9965 -2330 350 -485 N ATOM 2653 CA HIS A 393 -3.688 227.062 818.119 1.00 97.49 C ANISOU 2653 CA HIS A 393 12389 14042 10610 -2540 346 -476 C ATOM 2654 C HIS A 393 -2.334 226.931 818.811 1.00 98.84 C ANISOU 2654 C HIS A 393 12803 14031 10722 -2664 288 -362 C ATOM 2655 O HIS A 393 -1.422 226.298 818.282 1.00 98.65 O ANISOU 2655 O HIS A 393 12816 14054 10614 -2784 261 -325 O ATOM 2656 CB HIS A 393 -3.533 227.120 816.596 1.00100.59 C ANISOU 2656 CB HIS A 393 12611 14540 11069 -2392 342 -506 C ATOM 2657 CG HIS A 393 -4.828 227.298 815.867 1.00105.98 C ANISOU 2657 CG HIS A 393 13096 15362 11809 -2260 388 -628 C ATOM 2658 ND1 HIS A 393 -5.428 226.286 815.143 1.00110.73 N ANISOU 2658 ND1 HIS A 393 13543 16237 12293 -2382 440 -754 N ATOM 2659 CE1 HIS A 393 -6.552 226.727 814.616 1.00109.42 C ANISOU 2659 CE1 HIS A 393 13243 16119 12214 -2228 474 -869 C ATOM 2660 NE2 HIS A 393 -6.715 227.993 814.974 1.00105.24 N ANISOU 2660 NE2 HIS A 393 12778 15362 11844 -2022 439 -801 N ATOM 2661 CD2 HIS A 393 -5.652 228.369 815.757 1.00104.91 C ANISOU 2661 CD2 HIS A 393 12904 15132 11826 -2032 389 -658 C ATOM 2662 N ASP A 394 -2.213 227.534 819.993 1.00101.29 N ANISOU 2662 N ASP A 394 13288 14130 11066 -2640 264 -309 N ATOM 2663 CA ASP A 394 -1.061 227.301 820.859 1.00110.23 C ANISOU 2663 CA ASP A 394 14710 15067 12105 -2794 203 -216 C ATOM 2664 C ASP A 394 0.256 227.402 820.081 1.00116.16 C ANISOU 2664 C ASP A 394 15509 15739 12885 -2747 164 -171 C ATOM 2665 O ASP A 394 1.192 226.634 820.315 1.00121.59 O ANISOU 2665 O ASP A 394 16398 16379 13421 -2971 112 -112 O ATOM 2666 CB ASP A 394 -1.205 225.923 821.518 1.00118.65 C ANISOU 2666 CB ASP A 394 15912 16252 12916 -3174 191 -202 C ATOM 2667 CG ASP A 394 -0.112 225.628 822.523 1.00120.16 C ANISOU 2667 CG ASP A 394 16467 16209 12980 -3359 99 -95 C ATOM 2668 OD2 ASP A 394 0.103 224.433 822.822 1.00114.11 O ANISOU 2668 OD2 ASP A 394 15840 15531 11985 -3699 61 -59 O ATOM 2669 OD1 ASP A 394 0.525 226.584 823.013 1.00125.92 O ANISOU 2669 OD1 ASP A 394 17357 16666 13821 -3173 57 -51 O ATOM 2670 N LEU A 395 0.248 228.261 819.068 1.00115.36 N ANISOU 2670 N LEU A 395 15223 15653 12954 -2489 182 -198 N ATOM 2671 CA LEU A 395 1.400 228.565 818.210 1.00109.77 C ANISOU 2671 CA LEU A 395 14533 14886 12287 -2427 149 -160 C ATOM 2672 C LEU A 395 2.531 229.358 818.860 1.00109.73 C ANISOU 2672 C LEU A 395 14768 14600 12323 -2365 112 -108 C ATOM 2673 O LEU A 395 3.687 229.119 818.581 1.00112.15 O ANISOU 2673 O LEU A 395 15220 14835 12556 -2466 70 -65 O ATOM 2674 CB LEU A 395 0.954 229.257 816.923 1.00 95.98 C ANISOU 2674 CB LEU A 395 12536 13248 10685 -2194 169 -198 C ATOM 2675 CG LEU A 395 0.854 228.453 815.637 1.00 76.23 C ANISOU 2675 CG LEU A 395 9865 10989 8110 -2264 168 -215 C ATOM 2676 CD1 LEU A 395 0.468 227.040 815.898 1.00 44.09 C ANISOU 2676 CD1 LEU A 395 5788 7111 3851 -2531 187 -242 C ATOM 2677 CD2 LEU A 395 -0.144 229.108 814.743 1.00 73.27 C ANISOU 2677 CD2 LEU A 395 9277 10699 7863 -2029 190 -267 C ATOM 2678 N ASP A 396 2.178 230.311 819.715 1.00105.41 N ANISOU 2678 N ASP A 396 14270 13899 11882 -2201 127 -117 N ATOM 2679 CA ASP A 396 3.133 231.226 820.336 1.00101.69 C ANISOU 2679 CA ASP A 396 14014 13166 11458 -2094 105 -86 C ATOM 2680 C ASP A 396 4.202 230.541 821.129 1.00101.16 C ANISOU 2680 C ASP A 396 14304 12915 11216 -2291 39 -29 C ATOM 2681 O ASP A 396 3.907 229.704 821.958 1.00105.12 O ANISOU 2681 O ASP A 396 14949 13407 11585 -2476 5 -3 O ATOM 2682 CB ASP A 396 2.380 232.143 821.296 1.00102.74 C ANISOU 2682 CB ASP A 396 14140 13201 11695 -1926 127 -100 C ATOM 2683 CG ASP A 396 3.250 233.233 821.875 1.00107.38 C ANISOU 2683 CG ASP A 396 14920 13541 12340 -1766 116 -79 C ATOM 2684 OD1 ASP A 396 3.122 234.386 821.444 1.00106.00 O ANISOU 2684 OD1 ASP A 396 14588 13382 12305 -1547 149 -103 O ATOM 2685 OD2 ASP A 396 4.049 232.951 822.780 1.00114.52 O ANISOU 2685 OD2 ASP A 396 16148 14265 13097 -1808 61 -43 O ATOM 2686 N ILE A 397 5.449 230.928 820.882 1.00 96.88 N ANISOU 2686 N ILE A 397 13939 12213 10659 -2257 7 -5 N ATOM 2687 CA ILE A 397 6.598 230.357 821.565 1.00 96.87 C ANISOU 2687 CA ILE A 397 14328 12030 10446 -2372 -94 37 C ATOM 2688 C ILE A 397 7.342 231.382 822.392 1.00 94.41 C ANISOU 2688 C ILE A 397 14272 11493 10106 -2100 -139 11 C ATOM 2689 O ILE A 397 8.051 231.058 823.322 1.00 83.86 O ANISOU 2689 O ILE A 397 13294 9964 8606 -2140 -249 29 O ATOM 2690 CB ILE A 397 7.597 229.799 820.548 1.00 97.07 C ANISOU 2690 CB ILE A 397 14392 12138 10354 -2488 -150 40 C ATOM 2691 CG1 ILE A 397 7.145 228.442 820.023 1.00 97.06 C ANISOU 2691 CG1 ILE A 397 14253 12344 10280 -2819 -145 88 C ATOM 2692 CD1 ILE A 397 6.181 228.508 818.871 1.00 93.41 C ANISOU 2692 CD1 ILE A 397 13370 12170 9952 -2755 -58 47 C ATOM 2693 CG2 ILE A 397 8.964 229.685 821.159 1.00 97.02 C ANISOU 2693 CG2 ILE A 397 14797 11916 10150 -2483 -293 24 C ATOM 2694 N VAL A 398 7.191 232.633 822.015 1.00 88.47 N ANISOU 2694 N VAL A 398 13336 10778 9501 -1823 -68 -38 N ATOM 2695 CA VAL A 398 7.859 233.728 822.688 1.00 86.54 C ANISOU 2695 CA VAL A 398 13272 10383 9227 -1540 -94 -82 C ATOM 2696 C VAL A 398 7.436 234.021 824.123 1.00 94.29 C ANISOU 2696 C VAL A 398 14416 11214 10194 -1432 -126 -63 C ATOM 2697 O VAL A 398 8.256 234.372 824.958 1.00 93.44 O ANISOU 2697 O VAL A 398 14603 10937 9965 -1281 -214 -94 O ATOM 2698 CB VAL A 398 7.762 234.983 821.868 1.00 74.04 C ANISOU 2698 CB VAL A 398 11432 8917 7783 -1308 -10 -130 C ATOM 2699 CG1 VAL A 398 7.777 236.157 822.764 1.00 82.37 C ANISOU 2699 CG1 VAL A 398 12547 9885 8863 -1030 1 -160 C ATOM 2700 CG2 VAL A 398 8.876 235.033 820.882 1.00 58.17 C ANISOU 2700 CG2 VAL A 398 9476 6958 5669 -1307 -41 -179 C ATOM 2701 N THR A 399 6.144 233.891 824.390 1.00 91.55 N ANISOU 2701 N THR A 399 13880 10948 9959 -1497 -72 -32 N ATOM 2702 CA THR A 399 5.565 234.190 825.692 1.00 92.21 C ANISOU 2702 CA THR A 399 14085 10930 10020 -1399 -110 -14 C ATOM 2703 C THR A 399 6.041 233.266 826.794 1.00106.49 C ANISOU 2703 C THR A 399 16306 12543 11612 -1557 -255 35 C ATOM 2704 O THR A 399 6.450 232.144 826.540 1.00123.92 O ANISOU 2704 O THR A 399 18645 14736 13704 -1833 -308 71 O ATOM 2705 CB THR A 399 4.078 234.137 825.601 1.00 85.41 C ANISOU 2705 CB THR A 399 12928 10235 9289 -1468 -35 -11 C ATOM 2706 OG1 THR A 399 3.695 234.621 824.316 1.00 83.18 O ANISOU 2706 OG1 THR A 399 12286 10130 9186 -1416 58 -50 O ATOM 2707 CG2 THR A 399 3.474 235.003 826.649 1.00 81.43 C ANISOU 2707 CG2 THR A 399 12448 9686 8806 -1254 -50 -13 C ATOM 2708 N LYS A 400 6.018 233.747 828.026 1.00100.45 N ANISOU 2708 N LYS A 400 15760 11630 10776 -1384 -345 41 N ATOM 2709 CA LYS A 400 6.541 232.947 829.127 1.00 99.14 C ANISOU 2709 CA LYS A 400 16039 11242 10387 -1514 -538 94 C ATOM 2710 C LYS A 400 5.458 232.621 830.155 1.00 84.92 C ANISOU 2710 C LYS A 400 14299 9448 8520 -1609 -594 162 C ATOM 2711 O LYS A 400 5.638 231.743 831.002 1.00 69.39 O ANISOU 2711 O LYS A 400 12672 7342 6351 -1807 -762 248 O ATOM 2712 CB LYS A 400 7.703 233.679 829.801 1.00105.55 C ANISOU 2712 CB LYS A 400 17160 11841 11102 -1219 -681 27 C ATOM 2713 CG LYS A 400 8.716 234.264 828.822 1.00110.86 C ANISOU 2713 CG LYS A 400 17734 12569 11820 -1065 -612 -75 C ATOM 2714 CD LYS A 400 9.790 235.063 829.548 1.00110.45 C ANISOU 2714 CD LYS A 400 17946 12348 11671 -749 -749 -209 C ATOM 2715 CE LYS A 400 10.872 235.552 828.595 1.00100.59 C ANISOU 2715 CE LYS A 400 16624 11171 10424 -636 -689 -344 C ATOM 2716 NZ LYS A 400 11.974 236.220 829.338 1.00 96.95 N ANISOU 2716 NZ LYS A 400 16425 10539 9873 -351 -826 -544 N ATOM 2717 N ASP A 403 4.164 230.809 836.308 1.00 85.86 N ANISOU 2717 N ASP A 403 15893 8958 7774 -1885 -1510 916 N ATOM 2718 CA ASP A 403 3.384 231.255 837.458 1.00 98.85 C ANISOU 2718 CA ASP A 403 17620 10589 9351 -1733 -1643 1050 C ATOM 2719 C ASP A 403 2.171 232.087 837.040 1.00107.14 C ANISOU 2719 C ASP A 403 18229 11966 10514 -1596 -1434 890 C ATOM 2720 O ASP A 403 2.226 232.829 836.060 1.00109.46 O ANISOU 2720 O ASP A 403 18193 12385 11010 -1435 -1241 668 O ATOM 2721 CB ASP A 403 4.262 232.049 838.432 1.00 99.36 C ANISOU 2721 CB ASP A 403 17995 10313 9443 -1357 -1929 1096 C ATOM 2722 CG ASP A 403 3.447 232.817 839.461 1.00100.06 C ANISOU 2722 CG ASP A 403 18072 10435 9512 -1110 -2067 1173 C ATOM 2723 OD1 ASP A 403 2.852 233.849 839.096 1.00103.65 O ANISOU 2723 OD1 ASP A 403 18180 11132 10071 -882 -1923 970 O ATOM 2724 OD2 ASP A 403 3.408 232.399 840.637 1.00 94.70 O ANISOU 2724 OD2 ASP A 403 17731 9520 8729 -1146 -2331 1456 O ATOM 2725 N VAL A 404 1.092 231.966 837.798 1.00110.13 N ANISOU 2725 N VAL A 404 18617 12460 10766 -1663 -1481 1035 N ATOM 2726 CA VAL A 404 -0.157 232.639 837.494 1.00110.51 C ANISOU 2726 CA VAL A 404 18284 12806 10898 -1572 -1306 920 C ATOM 2727 C VAL A 404 -0.009 234.130 837.473 1.00112.04 C ANISOU 2727 C VAL A 404 18303 12988 11277 -1146 -1309 745 C ATOM 2728 O VAL A 404 -0.626 234.812 836.672 1.00105.55 O ANISOU 2728 O VAL A 404 17090 12378 10637 -1051 -1096 586 O ATOM 2729 CB VAL A 404 -1.236 232.299 838.516 1.00108.72 C ANISOU 2729 CB VAL A 404 18186 12679 10444 -1695 -1416 1126 C ATOM 2730 CG1 VAL A 404 -1.834 230.965 838.216 1.00109.02 C ANISOU 2730 CG1 VAL A 404 18217 12892 10313 -2132 -1287 1242 C ATOM 2731 CG2 VAL A 404 -0.676 232.330 839.912 1.00110.04 C ANISOU 2731 CG2 VAL A 404 18803 12544 10463 -1570 -1766 1356 C ATOM 2732 N GLU A 405 0.810 234.652 838.361 1.00119.92 N ANISOU 2732 N GLU A 405 19586 13740 12239 -881 -1564 789 N ATOM 2733 CA GLU A 405 0.948 236.074 838.402 1.00124.90 C ANISOU 2733 CA GLU A 405 20041 14397 13019 -473 -1576 619 C ATOM 2734 C GLU A 405 1.434 236.479 837.041 1.00120.15 C ANISOU 2734 C GLU A 405 19147 13879 12627 -426 -1309 404 C ATOM 2735 O GLU A 405 0.919 237.418 836.457 1.00127.41 O ANISOU 2735 O GLU A 405 19706 14989 13716 -266 -1131 271 O ATOM 2736 CB GLU A 405 2.001 236.444 839.428 1.00138.31 C ANISOU 2736 CB GLU A 405 22096 15788 14667 -187 -1909 686 C ATOM 2737 CG GLU A 405 1.637 237.622 840.282 1.00149.26 C ANISOU 2737 CG GLU A 405 23412 17211 16091 185 -2091 662 C ATOM 2738 CD GLU A 405 1.118 238.774 839.476 1.00155.27 C ANISOU 2738 CD GLU A 405 23718 18263 17016 360 -1836 413 C ATOM 2739 OE1 GLU A 405 1.347 238.790 838.253 1.00156.80 O ANISOU 2739 OE1 GLU A 405 23687 18555 17337 271 -1547 266 O ATOM 2740 OE2 GLU A 405 0.478 239.666 840.067 1.00156.65 O ANISOU 2740 OE2 GLU A 405 23755 18556 17208 584 -1942 390 O ATOM 2741 N ARG A 406 2.411 235.761 836.514 1.00108.76 N ANISOU 2741 N ARG A 406 17860 12292 11172 -578 -1290 398 N ATOM 2742 CA ARG A 406 2.935 236.097 835.201 1.00101.76 C ANISOU 2742 CA ARG A 406 16715 11476 10475 -541 -1062 236 C ATOM 2743 C ARG A 406 1.935 235.917 834.070 1.00 96.27 C ANISOU 2743 C ARG A 406 15593 11045 9939 -735 -789 209 C ATOM 2744 O ARG A 406 1.781 236.783 833.221 1.00 87.06 O ANISOU 2744 O ARG A 406 14088 10014 8975 -579 -618 110 O ATOM 2745 CB ARG A 406 4.212 235.306 834.919 1.00 95.92 C ANISOU 2745 CB ARG A 406 16262 10528 9655 -679 -1138 242 C ATOM 2746 CG ARG A 406 4.957 235.760 833.685 1.00 86.12 C ANISOU 2746 CG ARG A 406 14810 9337 8577 -590 -955 101 C ATOM 2747 CD ARG A 406 6.437 235.487 833.778 1.00 95.77 C ANISOU 2747 CD ARG A 406 16386 10321 9683 -550 -1112 52 C ATOM 2748 NE ARG A 406 7.179 236.623 834.312 1.00109.61 N ANISOU 2748 NE ARG A 406 18238 11982 11427 -143 -1227 -97 N ATOM 2749 CZ ARG A 406 8.504 236.670 834.408 1.00116.03 C ANISOU 2749 CZ ARG A 406 19314 12600 12174 -25 -1360 -251 C ATOM 2750 NH2 ARG A 406 9.105 237.741 834.905 1.00118.72 N ANISOU 2750 NH2 ARG A 406 19685 12862 12562 350 -1438 -474 N ATOM 2751 NH1 ARG A 406 9.235 235.644 834.007 1.00110.52 N ANISOU 2751 NH1 ARG A 406 18822 11768 11404 -290 -1409 -241 N ATOM 2752 N GLY A 407 1.221 234.809 834.086 1.00 94.70 N ANISOU 2752 N GLY A 407 15409 10932 9638 -1067 -770 311 N ATOM 2753 CA GLY A 407 0.275 234.522 833.033 1.00 87.31 C ANISOU 2753 CA GLY A 407 14090 10249 8836 -1248 -553 272 C ATOM 2754 C GLY A 407 -0.748 235.607 833.027 1.00 89.71 C ANISOU 2754 C GLY A 407 14093 10725 9268 -1038 -471 216 C ATOM 2755 O GLY A 407 -1.258 236.030 832.015 1.00 91.15 O ANISOU 2755 O GLY A 407 13912 11071 9649 -1011 -307 140 O ATOM 2756 N PHE A 408 -1.055 236.045 834.217 1.00 92.02 N ANISOU 2756 N PHE A 408 14560 10976 9428 -893 -621 268 N ATOM 2757 CA PHE A 408 -2.080 237.055 834.432 1.00 89.74 C ANISOU 2757 CA PHE A 408 14031 10858 9207 -705 -586 224 C ATOM 2758 C PHE A 408 -1.683 238.353 833.737 1.00 77.56 C ANISOU 2758 C PHE A 408 12225 9344 7900 -415 -483 96 C ATOM 2759 O PHE A 408 -2.461 238.914 832.964 1.00 70.13 O ANISOU 2759 O PHE A 408 10927 8591 7129 -390 -336 40 O ATOM 2760 CB PHE A 408 -2.274 237.291 835.930 1.00101.41 C ANISOU 2760 CB PHE A 408 15795 12264 10473 -581 -829 315 C ATOM 2761 CG PHE A 408 -3.537 238.027 836.274 1.00107.70 C ANISOU 2761 CG PHE A 408 16384 13272 11264 -480 -822 295 C ATOM 2762 CD2 PHE A 408 -4.759 237.376 836.258 1.00108.20 C ANISOU 2762 CD2 PHE A 408 16363 13530 11216 -726 -757 357 C ATOM 2763 CE2 PHE A 408 -5.922 238.048 836.579 1.00114.34 C ANISOU 2763 CE2 PHE A 408 16973 14509 11964 -640 -764 328 C ATOM 2764 CZ PHE A 408 -5.875 239.387 836.927 1.00118.43 C ANISOU 2764 CZ PHE A 408 17388 15038 12573 -313 -844 240 C ATOM 2765 CE1 PHE A 408 -4.661 240.047 836.952 1.00118.09 C ANISOU 2765 CE1 PHE A 408 17407 14817 12643 -64 -904 177 C ATOM 2766 CD1 PHE A 408 -3.502 239.367 836.627 1.00113.80 C ANISOU 2766 CD1 PHE A 408 17051 14071 12119 -143 -890 203 C ATOM 2767 N CYS A 409 -0.465 238.815 834.016 1.00 74.86 N ANISOU 2767 N CYS A 409 12071 8823 7547 -204 -576 56 N ATOM 2768 CA CYS A 409 0.065 240.033 833.414 1.00 74.05 C ANISOU 2768 CA CYS A 409 11751 8766 7618 66 -487 -51 C ATOM 2769 C CYS A 409 0.112 239.889 831.898 1.00 76.06 C ANISOU 2769 C CYS A 409 11716 9118 8067 -74 -285 -64 C ATOM 2770 O CYS A 409 -0.196 240.833 831.162 1.00 73.02 O ANISOU 2770 O CYS A 409 11009 8883 7852 39 -177 -108 O ATOM 2771 CB CYS A 409 1.465 240.340 833.955 1.00 80.06 C ANISOU 2771 CB CYS A 409 12806 9327 8286 288 -633 -102 C ATOM 2772 SG CYS A 409 1.541 240.643 835.750 1.00120.14 S ANISOU 2772 SG CYS A 409 18233 14270 13146 519 -964 -98 S ATOM 2773 N ASN A 410 0.413 238.687 831.438 1.00 75.70 N ANISOU 2773 N ASN A 410 11779 9000 7982 -342 -263 -19 N ATOM 2774 CA ASN A 410 0.493 238.437 830.016 1.00 72.81 C ANISOU 2774 CA ASN A 410 11165 8723 7778 -481 -122 -35 C ATOM 2775 C ASN A 410 -0.800 238.725 829.324 1.00 64.40 C ANISOU 2775 C ASN A 410 9727 7874 6867 -536 -19 -50 C ATOM 2776 O ASN A 410 -0.833 239.361 828.300 1.00 50.66 O ANISOU 2776 O ASN A 410 7723 6227 5299 -476 58 -81 O ATOM 2777 CB ASN A 410 0.756 236.954 829.786 1.00 83.58 C ANISOU 2777 CB ASN A 410 12693 10022 9040 -798 -139 9 C ATOM 2778 CG ASN A 410 2.198 236.570 829.996 1.00 91.59 C ANISOU 2778 CG ASN A 410 14043 10824 9934 -795 -232 17 C ATOM 2779 OD1 ASN A 410 3.004 237.367 830.450 1.00 97.55 O ANISOU 2779 OD1 ASN A 410 14942 11467 10655 -538 -298 -18 O ATOM 2780 ND2 ASN A 410 2.528 235.338 829.659 1.00 85.05 N ANISOU 2780 ND2 ASN A 410 13338 9957 9022 -1084 -248 53 N ATOM 2781 N LEU A 411 -1.877 238.253 829.909 1.00 68.76 N ANISOU 2781 N LEU A 411 10286 8509 7333 -659 -40 -24 N ATOM 2782 CA LEU A 411 -3.203 238.437 829.364 1.00 62.81 C ANISOU 2782 CA LEU A 411 9218 7964 6685 -721 36 -51 C ATOM 2783 C LEU A 411 -3.613 239.878 829.339 1.00 62.74 C ANISOU 2783 C LEU A 411 8995 8042 6800 -477 51 -91 C ATOM 2784 O LEU A 411 -4.282 240.324 828.435 1.00 56.34 O ANISOU 2784 O LEU A 411 7896 7366 6145 -487 110 -125 O ATOM 2785 CB LEU A 411 -4.203 237.617 830.143 1.00 58.19 C ANISOU 2785 CB LEU A 411 8733 7462 5914 -903 2 -13 C ATOM 2786 CG LEU A 411 -4.310 236.183 829.682 1.00 61.87 C ANISOU 2786 CG LEU A 411 9234 7975 6298 -1215 33 6 C ATOM 2787 CD1 LEU A 411 -4.552 235.315 830.835 1.00 65.12 C ANISOU 2787 CD1 LEU A 411 9940 8370 6431 -1381 -53 92 C ATOM 2788 CD2 LEU A 411 -5.406 236.045 828.714 1.00 68.46 C ANISOU 2788 CD2 LEU A 411 9745 9023 7242 -1315 124 -59 C ATOM 2789 N LYS A 412 -3.234 240.608 830.363 1.00 65.57 N ANISOU 2789 N LYS A 412 9509 8334 7070 -261 -27 -93 N ATOM 2790 CA LYS A 412 -3.612 241.986 830.430 1.00 75.02 C ANISOU 2790 CA LYS A 412 10502 9647 8357 -39 -24 -142 C ATOM 2791 CB LYS A 412 -3.063 242.600 831.691 1.00 90.81 C ANISOU 2791 CB LYS A 412 12720 11568 10216 202 -147 -164 C ATOM 2792 CG LYS A 412 -3.734 243.879 832.104 1.00103.45 C ANISOU 2792 CG LYS A 412 14131 13332 11843 403 -178 -231 C ATOM 2793 CD LYS A 412 -3.436 244.133 833.564 1.00111.03 C ANISOU 2793 CD LYS A 412 15358 14218 12610 603 -362 -262 C ATOM 2794 CE LYS A 412 -3.939 245.470 834.036 1.00108.07 C ANISOU 2794 CE LYS A 412 14796 14015 12249 830 -423 -366 C ATOM 2795 NZ LYS A 412 -3.711 245.595 835.495 1.00105.33 N ANISOU 2795 NZ LYS A 412 14725 13591 11705 1016 -670 -400 N ATOM 2796 C LYS A 412 -2.999 242.641 829.241 1.00 82.55 C ANISOU 2796 C LYS A 412 11255 10621 9490 17 44 -160 C ATOM 2797 O LYS A 412 -3.600 243.497 828.621 1.00 83.24 O ANISOU 2797 O LYS A 412 11074 10849 9706 54 74 -186 O ATOM 2798 N SER A 413 -1.770 242.247 828.946 1.00 87.00 N ANISOU 2798 N SER A 413 11979 11046 10032 11 47 -145 N ATOM 2799 CA SER A 413 -1.026 242.756 827.802 1.00 83.83 C ANISOU 2799 CA SER A 413 11444 10661 9748 42 96 -153 C ATOM 2800 C SER A 413 -1.549 242.360 826.427 1.00 69.93 C ANISOU 2800 C SER A 413 9464 8976 8130 -151 147 -146 C ATOM 2801 O SER A 413 -1.507 243.142 825.504 1.00 76.51 O ANISOU 2801 O SER A 413 10117 9885 9069 -113 160 -157 O ATOM 2802 CB SER A 413 0.444 242.388 827.926 1.00 86.85 C ANISOU 2802 CB SER A 413 12092 10884 10024 85 75 -152 C ATOM 2803 OG SER A 413 1.260 243.365 827.311 1.00 81.32 O ANISOU 2803 OG SER A 413 11306 10234 9359 222 101 -179 O ATOM 2804 N ARG A 414 -2.010 241.134 826.288 1.00 40.90 N ANISOU 2804 N ARG A 414 5823 5287 4430 -361 158 -136 N ATOM 2805 CA ARG A 414 -2.476 240.633 824.994 1.00 45.77 C ANISOU 2805 CA ARG A 414 6249 5985 5158 -528 182 -152 C ATOM 2806 C ARG A 414 -3.825 241.221 824.621 1.00 50.57 C ANISOU 2806 C ARG A 414 6605 6741 5867 -527 174 -182 C ATOM 2807 O ARG A 414 -4.244 241.170 823.465 1.00 63.76 O ANISOU 2807 O ARG A 414 8112 8480 7635 -602 163 -209 O ATOM 2808 CB ARG A 414 -2.531 239.095 824.970 1.00 54.65 C ANISOU 2808 CB ARG A 414 7480 7090 6194 -764 190 -149 C ATOM 2809 CG ARG A 414 -3.057 238.494 823.654 1.00 55.27 C ANISOU 2809 CG ARG A 414 7354 7283 6361 -920 199 -187 C ATOM 2810 CD ARG A 414 -2.471 237.108 823.377 1.00 63.09 C ANISOU 2810 CD ARG A 414 8463 8251 7256 -1130 203 -185 C ATOM 2811 NE ARG A 414 -2.795 236.154 824.433 1.00 74.76 N ANISOU 2811 NE ARG A 414 10118 9723 8566 -1284 199 -166 N ATOM 2812 CZ ARG A 414 -1.981 235.179 824.832 1.00 74.15 C ANISOU 2812 CZ ARG A 414 10281 9553 8338 -1437 179 -133 C ATOM 2813 NH1 ARG A 414 -0.791 235.037 824.261 1.00 77.70 N ANISOU 2813 NH1 ARG A 414 10813 9914 8795 -1445 171 -123 N ATOM 2814 NH2 ARG A 414 -2.350 234.355 825.808 1.00 55.05 N ANISOU 2814 NH2 ARG A 414 8041 7139 5735 -1595 155 -102 N ATOM 2815 N TYR A 415 -4.512 241.774 825.608 1.00 48.60 N ANISOU 2815 N TYR A 415 6352 6544 5571 -438 164 -186 N ATOM 2816 CA TYR A 415 -5.806 242.392 825.376 1.00 51.13 C ANISOU 2816 CA TYR A 415 6460 7010 5958 -440 150 -225 C ATOM 2817 C TYR A 415 -5.744 243.821 825.893 1.00 60.24 C ANISOU 2817 C TYR A 415 7560 8204 7123 -243 123 -232 C ATOM 2818 O TYR A 415 -5.024 244.108 826.852 1.00 66.76 O ANISOU 2818 O TYR A 415 8535 8970 7859 -99 115 -217 O ATOM 2819 CB TYR A 415 -6.894 241.610 826.113 1.00 49.51 C ANISOU 2819 CB TYR A 415 6287 6888 5638 -557 167 -242 C ATOM 2820 CG TYR A 415 -7.084 240.177 825.644 1.00 43.26 C ANISOU 2820 CG TYR A 415 5529 6110 4798 -778 193 -252 C ATOM 2821 CD2 TYR A 415 -8.126 239.839 824.795 1.00 50.49 C ANISOU 2821 CD2 TYR A 415 6269 7158 5759 -898 199 -317 C ATOM 2822 CE2 TYR A 415 -8.313 238.542 824.368 1.00 55.26 C ANISOU 2822 CE2 TYR A 415 6906 7813 6276 -1063 226 -343 C ATOM 2823 CZ TYR A 415 -7.461 237.554 824.796 1.00 47.99 C ANISOU 2823 CZ TYR A 415 6159 6814 5261 -1195 234 -299 C ATOM 2824 OH TYR A 415 -7.655 236.257 824.364 1.00 45.53 O ANISOU 2824 OH TYR A 415 5858 6593 4849 -1390 257 -334 O ATOM 2825 CE1 TYR A 415 -6.420 237.861 825.645 1.00 39.08 C ANISOU 2825 CE1 TYR A 415 5236 5526 4087 -1094 219 -228 C ATOM 2826 CD1 TYR A 415 -6.239 239.165 826.065 1.00 35.76 C ANISOU 2826 CD1 TYR A 415 4799 5055 3733 -872 200 -210 C ATOM 2827 N GLY A 416 -6.478 244.727 825.261 1.00 66.78 N ANISOU 2827 N GLY A 416 8195 9138 8040 -240 93 -270 N ATOM 2828 CA GLY A 416 -6.532 246.090 825.756 1.00 75.48 C ANISOU 2828 CA GLY A 416 9229 10320 9132 -90 60 -297 C ATOM 2829 C GLY A 416 -7.075 246.062 827.169 1.00 71.98 C ANISOU 2829 C GLY A 416 8839 9938 8571 -5 62 -321 C ATOM 2830 O GLY A 416 -7.800 245.139 827.523 1.00 78.06 O ANISOU 2830 O GLY A 416 9660 10726 9275 -111 86 -322 O ATOM 2831 N THR A 417 -6.726 247.047 827.990 1.00 69.05 N ANISOU 2831 N THR A 417 8478 9617 8143 182 26 -353 N ATOM 2832 CA THR A 417 -7.314 247.113 829.322 1.00 73.04 C ANISOU 2832 CA THR A 417 9048 10191 8514 286 -3 -401 C ATOM 2833 C THR A 417 -8.833 247.226 829.214 1.00 66.30 C ANISOU 2833 C THR A 417 8027 9495 7669 176 6 -463 C ATOM 2834 O THR A 417 -9.552 246.794 830.107 1.00 64.38 O ANISOU 2834 O THR A 417 7875 9303 7282 171 -7 -488 O ATOM 2835 CB THR A 417 -6.777 248.287 830.153 1.00 82.41 C ANISOU 2835 CB THR A 417 10232 11441 9641 528 -70 -472 C ATOM 2836 OG1 THR A 417 -7.229 249.520 829.585 1.00 91.04 O ANISOU 2836 OG1 THR A 417 11076 12693 10822 515 -88 -546 O ATOM 2837 CG2 THR A 417 -5.260 248.265 830.193 1.00 89.81 C ANISOU 2837 CG2 THR A 417 11331 12242 10550 646 -78 -437 C ATOM 2838 N GLN A 418 -9.317 247.805 828.119 1.00 58.34 N ANISOU 2838 N GLN A 418 6817 8556 6796 75 7 -498 N ATOM 2839 CA GLN A 418 -10.756 247.868 827.888 1.00 57.07 C ANISOU 2839 CA GLN A 418 6511 8529 6643 -43 18 -581 C ATOM 2840 C GLN A 418 -11.366 246.475 827.964 1.00 59.81 C ANISOU 2840 C GLN A 418 6951 8865 6911 -184 73 -554 C ATOM 2841 O GLN A 418 -12.259 246.232 828.773 1.00 60.73 O ANISOU 2841 O GLN A 418 7101 9091 6882 -196 83 -606 O ATOM 2842 CB GLN A 418 -11.080 248.498 826.533 1.00 56.12 C ANISOU 2842 CB GLN A 418 6399 8337 6586 -134 42 -618 C ATOM 2843 CG GLN A 418 -12.577 248.662 826.275 1.00 46.10 C ANISOU 2843 CG GLN A 418 5059 7165 5292 -220 76 -737 C ATOM 2844 CD GLN A 418 -12.887 249.034 824.842 1.00 48.06 C ANISOU 2844 CD GLN A 418 5351 7307 5601 -295 113 -766 C ATOM 2845 OE1 GLN A 418 -12.310 248.481 823.910 1.00 43.40 O ANISOU 2845 OE1 GLN A 418 4853 6583 5054 -324 123 -681 O ATOM 2846 NE2 GLN A 418 -13.810 249.971 824.657 1.00 49.57 N ANISOU 2846 NE2 GLN A 418 5468 7565 5801 -318 134 -903 N ATOM 2847 N ILE A 419 -10.882 245.566 827.115 1.00 52.30 N ANISOU 2847 N ILE A 419 6051 7797 6024 -302 96 -490 N ATOM 2848 CA ILE A 419 -11.330 244.173 827.132 1.00 40.39 C ANISOU 2848 CA ILE A 419 4630 6293 4425 -461 143 -478 C ATOM 2849 C ILE A 419 -11.078 243.515 828.484 1.00 51.95 C ANISOU 2849 C ILE A 419 6330 7729 5681 -434 142 -427 C ATOM 2850 O ILE A 419 -11.950 242.854 829.036 1.00 59.78 O ANISOU 2850 O ILE A 419 7389 8823 6501 -540 156 -450 O ATOM 2851 CB ILE A 419 -10.631 243.338 826.041 1.00 30.79 C ANISOU 2851 CB ILE A 419 3437 4957 3304 -570 151 -434 C ATOM 2852 CG1 ILE A 419 -11.163 243.700 824.655 1.00 41.87 C ANISOU 2852 CG1 ILE A 419 4809 6336 4765 -556 158 -485 C ATOM 2853 CD1 ILE A 419 -10.313 243.169 823.519 1.00 39.84 C ANISOU 2853 CD1 ILE A 419 4635 5944 4557 -555 160 -436 C ATOM 2854 CG2 ILE A 419 -10.844 241.863 826.280 1.00 40.70 C ANISOU 2854 CG2 ILE A 419 4810 6225 4428 -732 196 -424 C ATOM 2855 N PHE A 420 -9.884 243.702 829.029 1.00 57.03 N ANISOU 2855 N PHE A 420 7129 8233 6307 -299 108 -363 N ATOM 2856 CA PHE A 420 -9.543 243.053 830.281 1.00 58.67 C ANISOU 2856 CA PHE A 420 7624 8369 6298 -283 60 -311 C ATOM 2857 C PHE A 420 -10.431 243.506 831.427 1.00 63.93 C ANISOU 2857 C PHE A 420 8344 9166 6781 -207 -14 -354 C ATOM 2858 O PHE A 420 -10.822 242.698 832.260 1.00 68.84 O ANISOU 2858 O PHE A 420 9176 9808 7174 -309 -69 -313 O ATOM 2859 CB PHE A 420 -8.077 243.269 830.635 1.00 58.79 C ANISOU 2859 CB PHE A 420 7814 8201 6323 -128 16 -264 C ATOM 2860 CG PHE A 420 -7.551 242.273 831.624 1.00 51.21 C ANISOU 2860 CG PHE A 420 7200 7105 5152 -182 -57 -194 C ATOM 2861 CD1 PHE A 420 -7.766 242.444 832.978 1.00 52.37 C ANISOU 2861 CD1 PHE A 420 7554 7257 5088 -83 -193 -183 C ATOM 2862 CE1 PHE A 420 -7.288 241.527 833.890 1.00 51.77 C ANISOU 2862 CE1 PHE A 420 7831 7040 4799 -157 -310 -94 C ATOM 2863 CZ PHE A 420 -6.597 240.422 833.454 1.00 54.20 C ANISOU 2863 CZ PHE A 420 8274 7216 5104 -342 -263 -33 C ATOM 2864 CE2 PHE A 420 -6.386 240.235 832.105 1.00 49.66 C ANISOU 2864 CE2 PHE A 420 7475 6655 4740 -435 -113 -67 C ATOM 2865 CD2 PHE A 420 -6.862 241.158 831.198 1.00 40.68 C ANISOU 2865 CD2 PHE A 420 5999 5645 3814 -350 -24 -139 C ATOM 2866 N GLU A 421 -10.745 244.799 831.475 1.00 74.45 N ANISOU 2866 N GLU A 421 9497 10601 8189 -43 -37 -438 N ATOM 2867 CA GLU A 421 -11.629 245.329 832.511 1.00 73.25 C ANISOU 2867 CA GLU A 421 9374 10594 7863 38 -133 -512 C ATOM 2868 C GLU A 421 -13.033 244.779 832.334 1.00 75.83 C ANISOU 2868 C GLU A 421 9635 11090 8088 -158 -88 -560 C ATOM 2869 O GLU A 421 -13.720 244.475 833.309 1.00 90.98 O ANISOU 2869 O GLU A 421 11712 13102 9753 -193 -185 -567 O ATOM 2870 CB GLU A 421 -11.668 246.856 832.480 1.00 72.24 C ANISOU 2870 CB GLU A 421 9031 10564 7854 232 -161 -630 C ATOM 2871 CG GLU A 421 -10.571 247.535 833.292 1.00 81.40 C ANISOU 2871 CG GLU A 421 10308 11637 8983 479 -274 -642 C ATOM 2872 CD GLU A 421 -10.894 248.990 833.596 1.00 92.52 C ANISOU 2872 CD GLU A 421 11515 13207 10432 655 -341 -805 C ATOM 2873 OE1 GLU A 421 -12.028 249.267 834.049 1.00 89.48 O ANISOU 2873 OE1 GLU A 421 11075 12975 9949 629 -410 -903 O ATOM 2874 OE2 GLU A 421 -10.016 249.854 833.388 1.00 98.00 O ANISOU 2874 OE2 GLU A 421 12103 13889 11242 805 -336 -852 O ATOM 2875 N ARG A 422 -13.450 244.652 831.079 1.00 61.91 N ANISOU 2875 N ARG A 422 7652 9370 6502 -286 30 -598 N ATOM 2876 CA ARG A 422 -14.766 244.110 830.760 1.00 55.62 C ANISOU 2876 CA ARG A 422 6777 8739 5619 -467 87 -680 C ATOM 2877 C ARG A 422 -14.880 242.636 831.163 1.00 60.27 C ANISOU 2877 C ARG A 422 7587 9330 5984 -655 98 -605 C ATOM 2878 O ARG A 422 -15.914 242.197 831.662 1.00 65.53 O ANISOU 2878 O ARG A 422 8318 10166 6416 -767 90 -659 O ATOM 2879 CB ARG A 422 -15.073 244.309 829.274 1.00 45.99 C ANISOU 2879 CB ARG A 422 5299 7531 4643 -548 171 -746 C ATOM 2880 CG ARG A 422 -16.261 243.529 828.759 1.00 55.80 C ANISOU 2880 CG ARG A 422 6475 8915 5811 -739 241 -846 C ATOM 2881 CD ARG A 422 -17.517 243.858 829.524 1.00 57.64 C ANISOU 2881 CD ARG A 422 6706 9356 5839 -740 228 -982 C ATOM 2882 NE ARG A 422 -17.837 245.273 829.419 1.00 76.09 N ANISOU 2882 NE ARG A 422 8866 11739 8306 -607 197 -1093 N ATOM 2883 CZ ARG A 422 -18.504 245.807 828.402 1.00 88.11 C ANISOU 2883 CZ ARG A 422 10172 13305 10000 -655 246 -1228 C ATOM 2884 NH1 ARG A 422 -18.920 245.034 827.403 1.00 91.77 N ANISOU 2884 NH1 ARG A 422 10578 13767 10523 -807 315 -1272 N ATOM 2885 NH2 ARG A 422 -18.756 247.113 828.385 1.00 75.41 N ANISOU 2885 NH2 ARG A 422 8418 11738 8497 -556 217 -1338 N ATOM 2886 N ALA A 423 -13.814 241.874 830.962 1.00 55.64 N ANISOU 2886 N ALA A 423 7125 8571 5445 -704 112 -492 N ATOM 2887 CA ALA A 423 -13.829 240.475 831.357 1.00 62.26 C ANISOU 2887 CA ALA A 423 8180 9415 6061 -908 119 -419 C ATOM 2888 C ALA A 423 -13.811 240.356 832.876 1.00 69.85 C ANISOU 2888 C ALA A 423 9446 10375 6719 -878 -20 -336 C ATOM 2889 O ALA A 423 -14.448 239.468 833.444 1.00 80.52 O ANISOU 2889 O ALA A 423 10963 11846 7785 -1061 -40 -301 O ATOM 2890 CB ALA A 423 -12.659 239.726 830.741 1.00 58.71 C ANISOU 2890 CB ALA A 423 7789 8782 5737 -978 154 -340 C ATOM 2891 N GLN A 424 -13.081 241.256 833.531 1.00 59.66 N ANISOU 2891 N GLN A 424 8238 8960 5469 -648 -137 -304 N ATOM 2892 CA GLN A 424 -13.021 241.288 834.987 1.00 69.74 C ANISOU 2892 CA GLN A 424 9811 10217 6470 -579 -339 -226 C ATOM 2893 C GLN A 424 -14.418 241.462 835.576 1.00 77.02 C ANISOU 2893 C GLN A 424 10724 11385 7155 -630 -410 -292 C ATOM 2894 O GLN A 424 -14.828 240.721 836.476 1.00 73.92 O ANISOU 2894 O GLN A 424 10591 11061 6435 -765 -526 -198 O ATOM 2895 CB GLN A 424 -12.132 242.441 835.463 1.00 81.46 C ANISOU 2895 CB GLN A 424 11313 11568 8070 -280 -464 -242 C ATOM 2896 CG GLN A 424 -10.653 242.310 835.126 1.00 83.24 C ANISOU 2896 CG GLN A 424 11618 11551 8459 -204 -432 -185 C ATOM 2897 CD GLN A 424 -9.861 241.600 836.202 1.00 85.61 C ANISOU 2897 CD GLN A 424 12314 11669 8544 -214 -615 -49 C ATOM 2898 OE1 GLN A 424 -10.124 240.441 836.524 1.00 85.80 O ANISOU 2898 OE1 GLN A 424 12544 11695 8360 -449 -640 61 O ATOM 2899 NE2 GLN A 424 -8.873 242.290 836.758 1.00 87.10 N ANISOU 2899 NE2 GLN A 424 12617 11706 8771 35 -757 -57 N ATOM 2900 N GLN A 425 -15.143 242.456 835.066 1.00 72.91 N ANISOU 2900 N GLN A 425 9919 11004 6781 -534 -353 -451 N ATOM 2901 CA GLN A 425 -16.475 242.772 835.562 1.00 71.04 C ANISOU 2901 CA GLN A 425 9653 11008 6333 -565 -430 -560 C ATOM 2902 C GLN A 425 -17.427 241.587 835.416 1.00 81.10 C ANISOU 2902 C GLN A 425 10992 12454 7367 -844 -335 -566 C ATOM 2903 O GLN A 425 -18.058 241.165 836.387 1.00 83.95 O ANISOU 2903 O GLN A 425 11575 12951 7369 -938 -468 -524 O ATOM 2904 CB GLN A 425 -17.029 244.008 834.844 1.00 75.91 C ANISOU 2904 CB GLN A 425 9933 11724 7184 -443 -360 -753 C ATOM 2905 CG GLN A 425 -18.453 244.399 835.247 1.00 87.99 C ANISOU 2905 CG GLN A 425 11410 13507 8514 -481 -438 -918 C ATOM 2906 CD GLN A 425 -18.580 244.757 836.724 1.00 91.56 C ANISOU 2906 CD GLN A 425 12085 14013 8689 -374 -736 -886 C ATOM 2907 OE1 GLN A 425 -19.631 244.554 837.337 1.00 83.73 O ANISOU 2907 OE1 GLN A 425 11192 13222 7401 -472 -852 -946 O ATOM 2908 NE2 GLN A 425 -17.506 245.290 837.297 1.00 91.65 N ANISOU 2908 NE2 GLN A 425 12182 13854 8787 -171 -886 -798 N ATOM 2909 N ILE A 426 -17.517 241.049 834.201 1.00 80.43 N ANISOU 2909 N ILE A 426 10720 12378 7464 -977 -124 -619 N ATOM 2910 CA ILE A 426 -18.380 239.904 833.910 1.00 67.61 C ANISOU 2910 CA ILE A 426 9116 10936 5635 -1238 -7 -663 C ATOM 2911 C ILE A 426 -18.101 238.704 834.818 1.00 68.08 C ANISOU 2911 C ILE A 426 9521 10996 5352 -1420 -75 -486 C ATOM 2912 O ILE A 426 -19.032 238.050 835.290 1.00 65.76 O ANISOU 2912 O ILE A 426 9353 10927 4706 -1601 -73 -506 O ATOM 2913 CB ILE A 426 -18.253 239.487 832.436 1.00 57.08 C ANISOU 2913 CB ILE A 426 7536 9565 4587 -1323 183 -734 C ATOM 2914 CG1 ILE A 426 -19.192 240.331 831.572 1.00 49.69 C ANISOU 2914 CG1 ILE A 426 6298 8748 3834 -1260 257 -946 C ATOM 2915 CD1 ILE A 426 -18.765 240.440 830.125 1.00 39.12 C ANISOU 2915 CD1 ILE A 426 4715 7287 2864 -1244 355 -981 C ATOM 2916 CG2 ILE A 426 -18.559 238.011 832.268 1.00 51.26 C ANISOU 2916 CG2 ILE A 426 6895 8946 3636 -1594 287 -720 C ATOM 2917 N LEU A 427 -16.824 238.418 835.058 1.00 67.33 N ANISOU 2917 N LEU A 427 9591 10656 5336 -1384 -135 -316 N ATOM 2918 CA LEU A 427 -16.446 237.350 835.978 1.00 72.62 C ANISOU 2918 CA LEU A 427 10620 11287 5684 -1557 -231 -122 C ATOM 2919 C LEU A 427 -16.926 237.635 837.395 1.00 76.35 C ANISOU 2919 C LEU A 427 11362 11847 5800 -1514 -470 -33 C ATOM 2920 O LEU A 427 -17.191 236.712 838.162 1.00 79.92 O ANISOU 2920 O LEU A 427 12102 12391 5873 -1721 -543 110 O ATOM 2921 CB LEU A 427 -14.931 237.140 835.990 1.00 73.71 C ANISOU 2921 CB LEU A 427 10896 11118 5994 -1497 -280 18 C ATOM 2922 CG LEU A 427 -14.290 236.345 834.854 1.00 59.21 C ANISOU 2922 CG LEU A 427 8933 9193 4370 -1634 -104 0 C ATOM 2923 CD1 LEU A 427 -12.793 236.221 835.094 1.00 48.26 C ANISOU 2923 CD1 LEU A 427 7744 7506 3087 -1563 -195 128 C ATOM 2924 CD2 LEU A 427 -14.934 234.976 834.728 1.00 62.64 C ANISOU 2924 CD2 LEU A 427 9434 9829 4536 -1963 7 17 C ATOM 2925 N SER A 428 -17.020 238.915 837.744 1.00 79.65 N ANISOU 2925 N SER A 428 11692 12246 6327 -1253 -612 -109 N ATOM 2926 CA SER A 428 -17.466 239.305 839.078 1.00 81.32 C ANISOU 2926 CA SER A 428 12136 12542 6221 -1179 -900 -38 C ATOM 2927 C SER A 428 -18.983 239.455 839.121 1.00 84.02 C ANISOU 2927 C SER A 428 12381 13215 6329 -1272 -881 -201 C ATOM 2928 O SER A 428 -19.586 239.392 840.192 1.00 95.51 O ANISOU 2928 O SER A 428 14068 14814 7407 -1313 -1105 -130 O ATOM 2929 CB SER A 428 -16.806 240.605 839.524 1.00 73.61 C ANISOU 2929 CB SER A 428 11112 11403 5453 -846 -1103 -61 C ATOM 2930 OG SER A 428 -17.600 241.711 839.148 1.00 79.73 O ANISOU 2930 OG SER A 428 11589 12340 6364 -714 -1077 -285 O ATOM 2931 N GLU A 429 -19.593 239.661 837.957 1.00 73.96 N ANISOU 2931 N GLU A 429 10775 12057 5269 -1302 -637 -419 N ATOM 2932 CA GLU A 429 -21.048 239.645 837.847 1.00 75.69 C ANISOU 2932 CA GLU A 429 10902 12592 5265 -1421 -579 -613 C ATOM 2933 C GLU A 429 -21.554 238.226 838.011 1.00 70.09 C ANISOU 2933 C GLU A 429 10393 12067 4171 -1733 -476 -542 C ATOM 2934 O GLU A 429 -22.719 238.014 838.330 1.00 67.32 O ANISOU 2934 O GLU A 429 10100 12007 3473 -1862 -484 -653 O ATOM 2935 CB GLU A 429 -21.500 240.155 836.482 1.00 91.44 C ANISOU 2935 CB GLU A 429 12504 14630 7611 -1378 -348 -860 C ATOM 2936 CG GLU A 429 -21.519 241.651 836.310 1.00100.98 C ANISOU 2936 CG GLU A 429 13486 15783 9100 -1125 -431 -1000 C ATOM 2937 CD GLU A 429 -22.202 242.047 835.016 1.00109.75 C ANISOU 2937 CD GLU A 429 14253 16970 10477 -1137 -222 -1240 C ATOM 2938 OE1 GLU A 429 -23.117 241.310 834.591 1.00110.67 O ANISOU 2938 OE1 GLU A 429 14337 17275 10438 -1325 -82 -1368 O ATOM 2939 OE2 GLU A 429 -21.825 243.081 834.425 1.00112.39 O ANISOU 2939 OE2 GLU A 429 14361 17181 11161 -964 -200 -1304 O ATOM 2940 N ASN A 430 -20.680 237.252 837.766 1.00 74.93 N ANISOU 2940 N ASN A 430 11108 12529 4832 -1864 -374 -374 N ATOM 2941 CA ASN A 430 -21.061 235.849 837.861 1.00 81.91 C ANISOU 2941 CA ASN A 430 12168 13595 5359 -2184 -250 -301 C ATOM 2942 C ASN A 430 -20.473 235.167 839.089 1.00 86.85 C ANISOU 2942 C ASN A 430 13224 14138 5638 -2299 -451 13 C ATOM 2943 O ASN A 430 -20.503 233.943 839.202 1.00 95.14 O ANISOU 2943 O ASN A 430 14453 15289 6405 -2581 -350 134 O ATOM 2944 CB ASN A 430 -20.695 235.091 836.581 1.00 87.08 C ANISOU 2944 CB ASN A 430 12603 14202 6282 -2308 24 -372 C ATOM 2945 CG ASN A 430 -21.659 235.377 835.435 1.00 88.18 C ANISOU 2945 CG ASN A 430 12381 14520 6601 -2294 225 -676 C ATOM 2946 OD1 ASN A 430 -21.668 236.477 834.870 1.00 81.12 O ANISOU 2946 OD1 ASN A 430 11240 13528 6056 -2071 212 -810 O ATOM 2947 ND2 ASN A 430 -22.475 234.383 835.084 1.00 88.29 N ANISOU 2947 ND2 ASN A 430 12373 14804 6369 -2536 415 -791 N ATOM 2948 N LYS A 431 -19.948 235.976 840.003 1.00 91.46 N ANISOU 2948 N LYS A 431 13971 14542 6239 -2080 -744 143 N ATOM 2949 CA LYS A 431 -19.446 235.498 841.292 1.00 98.90 C ANISOU 2949 CA LYS A 431 15348 15382 6846 -2146 -1012 455 C ATOM 2950 C LYS A 431 -18.311 234.481 841.145 1.00 99.83 C ANISOU 2950 C LYS A 431 15632 15271 7029 -2301 -936 659 C ATOM 2951 O LYS A 431 -18.294 233.450 841.818 1.00103.69 O ANISOU 2951 O LYS A 431 16452 15809 7136 -2555 -991 893 O ATOM 2952 CB LYS A 431 -20.586 234.883 842.103 1.00110.19 C ANISOU 2952 CB LYS A 431 17032 17146 7691 -2383 -1089 529 C ATOM 2953 CG LYS A 431 -21.650 235.880 842.534 1.00126.78 C ANISOU 2953 CG LYS A 431 19058 19466 9647 -2233 -1262 357 C ATOM 2954 CD LYS A 431 -22.763 235.199 843.314 1.00149.22 C ANISOU 2954 CD LYS A 431 22177 22662 11859 -2488 -1333 427 C ATOM 2955 CE LYS A 431 -23.814 236.199 843.764 1.00162.62 C ANISOU 2955 CE LYS A 431 23809 24583 13395 -2343 -1542 236 C ATOM 2956 NZ LYS A 431 -24.924 235.541 844.509 1.00170.68 N ANISOU 2956 NZ LYS A 431 25114 25978 13759 -2599 -1614 287 N ATOM 2957 N ILE A 432 -17.361 234.780 840.267 1.00 96.31 N ANISOU 2957 N ILE A 432 14964 14580 7048 -2160 -817 575 N ATOM 2958 CA ILE A 432 -16.196 233.923 840.094 1.00 94.29 C ANISOU 2958 CA ILE A 432 14854 14088 6885 -2282 -772 735 C ATOM 2959 C ILE A 432 -14.957 234.612 840.662 1.00101.87 C ANISOU 2959 C ILE A 432 15968 14690 8048 -2015 -1016 854 C ATOM 2960 O ILE A 432 -14.340 235.453 840.008 1.00 99.72 O ANISOU 2960 O ILE A 432 15453 14257 8178 -1772 -963 706 O ATOM 2961 CB ILE A 432 -15.993 233.540 838.617 1.00 85.06 C ANISOU 2961 CB ILE A 432 13348 12927 6045 -2363 -461 552 C ATOM 2962 CG1 ILE A 432 -17.288 232.945 838.051 1.00 86.14 C ANISOU 2962 CG1 ILE A 432 13310 13431 5989 -2587 -234 396 C ATOM 2963 CD1 ILE A 432 -17.191 232.480 836.614 1.00 77.36 C ANISOU 2963 CD1 ILE A 432 11871 12352 5171 -2671 33 220 C ATOM 2964 CG2 ILE A 432 -14.848 232.554 838.480 1.00 80.86 C ANISOU 2964 CG2 ILE A 432 12984 12187 5551 -2528 -434 708 C ATOM 2965 N ILE A 433 -14.612 234.243 841.892 1.00109.64 N ANISOU 2965 N ILE A 433 17366 15559 8732 -2063 -1292 1129 N ATOM 2966 CA ILE A 433 -13.546 234.889 842.655 1.00113.38 C ANISOU 2966 CA ILE A 433 18037 15708 9334 -1791 -1590 1254 C ATOM 2967 C ILE A 433 -12.171 234.263 842.408 1.00119.04 C ANISOU 2967 C ILE A 433 18899 16111 10218 -1847 -1564 1360 C ATOM 2968 O ILE A 433 -12.072 233.119 841.970 1.00122.38 O ANISOU 2968 O ILE A 433 19379 16573 10546 -2156 -1385 1426 O ATOM 2969 CB ILE A 433 -13.872 234.846 844.169 1.00114.39 C ANISOU 2969 CB ILE A 433 18561 15843 9060 -1787 -1970 1524 C ATOM 2970 CG1 ILE A 433 -14.645 236.098 844.586 1.00110.13 C ANISOU 2970 CG1 ILE A 433 17867 15455 8523 -1515 -2154 1385 C ATOM 2971 CD1 ILE A 433 -14.996 236.134 846.063 1.00108.02 C ANISOU 2971 CD1 ILE A 433 17967 15207 7871 -1483 -2580 1647 C ATOM 2972 CG2 ILE A 433 -12.610 234.695 845.006 1.00116.54 C ANISOU 2972 CG2 ILE A 433 19190 15734 9355 -1683 -2268 1782 C ATOM 2973 N MSE A 434 -11.113 235.023 842.685 1.00120.34 N ANISOU 2973 N MSE A 434 19118 15982 10622 -1547 -1747 1360 N ATOM 2974 CA MSE A 434 -9.751 234.499 842.607 1.00127.41 C ANISOU 2974 CA MSE A 434 20209 16559 11642 -1573 -1780 1462 C ATOM 2975 C MSE A 434 -9.159 234.234 843.992 1.00127.71 C ANISOU 2975 C MSE A 434 20724 16339 11460 -1534 -2171 1780 C ATOM 2976 O MSE A 434 -9.473 234.932 844.957 1.00124.38 O ANISOU 2976 O MSE A 434 20411 15910 10936 -1319 -2468 1863 O ATOM 2977 CB MSE A 434 -8.840 235.451 841.821 1.00133.45 C ANISOU 2977 CB MSE A 434 20713 17160 12832 -1273 -1687 1228 C ATOM 2978 CG MSE A 434 -7.392 234.963 841.692 1.00136.04 C ANISOU 2978 CG MSE A 434 21244 17167 13279 -1285 -1726 1296 C ATOM 2979 SE MSE A 434 -6.279 235.972 840.432 1.00144.67 Se ANISOU 2979 SE MSE A 434 21994 18126 14849 -985 -1526 984 Se ATOM 2980 CE MSE A 434 -6.211 237.683 841.374 1.00110.57 C ANISOU 2980 CE MSE A 434 17641 13754 10616 -483 -1815 913 C ATOM 2981 N ALA A 435 -8.300 233.220 844.077 1.00131.04 N ANISOU 2981 N ALA A 435 21426 16541 11822 -1742 -2194 1969 N ATOM 2982 CA ALA A 435 -7.556 232.928 845.300 1.00126.05 C ANISOU 2982 CA ALA A 435 21263 15583 11047 -1699 -2574 2296 C ATOM 2983 C ALA A 435 -6.060 233.165 845.073 1.00131.05 C ANISOU 2983 C ALA A 435 21962 15845 11986 -1496 -2642 2238 C ATOM 2984 O ALA A 435 -5.209 232.477 845.640 1.00123.40 O ANISOU 2984 O ALA A 435 21369 14563 10954 -1588 -2836 2492 O ATOM 2985 CB ALA A 435 -7.813 231.499 845.743 1.00118.79 C ANISOU 2985 CB ALA A 435 20686 14691 9760 -2139 -2580 2623 C ATOM 2986 N HIS A 436 -5.758 234.137 844.234 1.00144.06 N ANISOU 2986 N HIS A 436 23252 17529 13955 -1228 -2481 1911 N ATOM 2987 CA HIS A 436 -4.399 234.470 843.821 1.00155.56 C ANISOU 2987 CA HIS A 436 24711 18706 15690 -1025 -2487 1789 C ATOM 2988 C HIS A 436 -3.672 233.368 843.060 1.00160.65 C ANISOU 2988 C HIS A 436 25437 19248 16356 -1331 -2297 1807 C ATOM 2989 O HIS A 436 -4.236 232.754 842.166 1.00159.79 O ANISOU 2989 O HIS A 436 25111 19382 16220 -1615 -1997 1716 O ATOM 2990 CB HIS A 436 -3.532 234.932 844.979 1.00163.79 C ANISOU 2990 CB HIS A 436 26073 19389 16770 -711 -2908 1957 C ATOM 2991 CG HIS A 436 -2.409 235.810 844.537 1.00167.64 C ANISOU 2991 CG HIS A 436 26432 19698 17566 -364 -2902 1725 C ATOM 2992 ND1 HIS A 436 -2.255 237.103 844.981 1.00168.94 N ANISOU 2992 ND1 HIS A 436 26465 19830 17892 76 -3094 1606 N ATOM 2993 CE1 HIS A 436 -1.202 237.643 844.396 1.00167.31 C ANISOU 2993 CE1 HIS A 436 26156 19496 17918 299 -3015 1400 C ATOM 2994 NE2 HIS A 436 -0.681 236.752 843.572 1.00165.92 N ANISOU 2994 NE2 HIS A 436 26045 19265 17732 16 -2789 1380 N ATOM 2995 CD2 HIS A 436 -1.427 235.603 843.630 1.00167.02 C ANISOU 2995 CD2 HIS A 436 26309 19506 17646 -400 -2714 1575 C ATOM 2996 N ASN A 437 -2.425 233.103 843.415 1.00167.68 N ANISOU 2996 N ASN A 437 26635 19773 17305 -1270 -2489 1924 N ATOM 2997 CA ASN A 437 -1.670 232.100 842.677 1.00173.40 C ANISOU 2997 CA ASN A 437 27434 20397 18055 -1556 -2330 1929 C ATOM 2998 C ASN A 437 -2.235 230.690 842.769 1.00179.79 C ANISOU 2998 C ASN A 437 28400 21319 18592 -2041 -2249 2168 C ATOM 2999 O ASN A 437 -2.891 230.328 843.739 1.00183.90 O ANISOU 2999 O ASN A 437 29154 21860 18860 -2162 -2414 2439 O ATOM 3000 CB ASN A 437 -0.188 232.101 843.049 1.00173.13 C ANISOU 3000 CB ASN A 437 27720 19918 18143 -1392 -2566 2008 C ATOM 3001 CG ASN A 437 0.653 231.296 842.075 1.00169.84 C ANISOU 3001 CG ASN A 437 27306 19432 17794 -1639 -2381 1930 C ATOM 3002 OD1 ASN A 437 0.368 230.128 841.810 1.00169.12 O ANISOU 3002 OD1 ASN A 437 27268 19437 17551 -2055 -2256 2062 O ATOM 3003 ND2 ASN A 437 1.692 231.921 841.527 1.00166.99 N ANISOU 3003 ND2 ASN A 437 26881 18922 17645 -1386 -2365 1715 N ATOM 3004 N GLU A 438 -1.970 229.889 841.751 1.00177.23 N ANISOU 3004 N GLU A 438 27947 21084 18309 -2322 -1999 2074 N ATOM 3005 CA GLU A 438 -2.411 228.525 841.788 1.00174.26 C ANISOU 3005 CA GLU A 438 27700 20830 17681 -2789 -1906 2292 C ATOM 3006 C GLU A 438 -3.894 228.659 842.020 1.00167.55 C ANISOU 3006 C GLU A 438 26685 20337 16638 -2847 -1815 2299 C ATOM 3007 O GLU A 438 -4.524 227.826 842.663 1.00165.53 O ANISOU 3007 O GLU A 438 26645 20180 16069 -3143 -1850 2567 O ATOM 3008 CB GLU A 438 -1.736 227.813 842.960 1.00178.64 C ANISOU 3008 CB GLU A 438 28794 21005 18074 -2929 -2212 2691 C ATOM 3009 CG GLU A 438 -0.252 228.186 843.156 1.00176.34 C ANISOU 3009 CG GLU A 438 28736 20247 18019 -2677 -2437 2690 C ATOM 3010 CD GLU A 438 0.392 227.525 844.383 1.00176.95 C ANISOU 3010 CD GLU A 438 29364 19865 18006 -2788 -2776 3113 C ATOM 3011 OE1 GLU A 438 0.135 227.974 845.518 1.00177.37 O ANISOU 3011 OE1 GLU A 438 29641 19759 17992 -2586 -3066 3316 O ATOM 3012 OE2 GLU A 438 1.175 226.568 844.213 1.00175.03 O ANISOU 3012 OE2 GLU A 438 29328 19390 17785 -3076 -2769 3251 O ATOM 3013 N ASP A 439 -4.474 229.720 841.461 1.00161.15 N ANISOU 3013 N ASP A 439 25490 19731 16009 -2575 -1684 2007 N ATOM 3014 CA ASP A 439 -5.923 229.889 841.478 1.00158.91 C ANISOU 3014 CA ASP A 439 24994 19808 15576 -2628 -1562 1959 C ATOM 3015 C ASP A 439 -6.216 229.928 840.019 1.00148.91 C ANISOU 3015 C ASP A 439 23264 18774 14540 -2669 -1226 1651 C ATOM 3016 O ASP A 439 -7.122 230.586 839.538 1.00151.83 O ANISOU 3016 O ASP A 439 23298 19382 15007 -2547 -1081 1458 O ATOM 3017 CB ASP A 439 -6.489 231.122 842.145 1.00163.09 C ANISOU 3017 CB ASP A 439 25472 20372 16121 -2282 -1729 1912 C ATOM 3018 CG ASP A 439 -8.003 231.159 841.999 1.00166.71 C ANISOU 3018 CG ASP A 439 25703 21228 16412 -2392 -1570 1840 C ATOM 3019 OD1 ASP A 439 -8.657 232.105 842.484 1.00170.58 O ANISOU 3019 OD1 ASP A 439 26121 21811 16881 -2155 -1689 1790 O ATOM 3020 OD2 ASP A 439 -8.537 230.216 841.380 1.00165.15 O ANISOU 3020 OD2 ASP A 439 25394 21261 16096 -2720 -1329 1822 O ATOM 3021 N GLU A 440 -5.402 229.208 839.300 1.00137.29 N ANISOU 3021 N GLU A 440 21783 17215 13166 -2841 -1124 1621 N ATOM 3022 CA GLU A 440 -5.562 229.203 837.900 1.00132.89 C ANISOU 3022 CA GLU A 440 20806 16845 12843 -2869 -853 1356 C ATOM 3023 C GLU A 440 -6.938 228.695 837.595 1.00133.32 C ANISOU 3023 C GLU A 440 20645 17277 12735 -3089 -659 1323 C ATOM 3024 O GLU A 440 -7.529 229.087 836.598 1.00138.17 O ANISOU 3024 O GLU A 440 20861 18088 13551 -3007 -468 1090 O ATOM 3025 CB GLU A 440 -4.527 228.280 837.258 1.00135.33 C ANISOU 3025 CB GLU A 440 21179 17036 13205 -3085 -804 1368 C ATOM 3026 CG GLU A 440 -3.110 228.762 837.389 1.00149.58 C ANISOU 3026 CG GLU A 440 23407 18458 14969 -3045 -1053 1548 C ATOM 3027 CD GLU A 440 -2.102 227.786 836.803 1.00166.75 C ANISOU 3027 CD GLU A 440 26019 20530 16807 -3262 -1247 1909 C ATOM 3028 OE1 GLU A 440 -2.519 226.670 836.479 1.00171.80 O ANISOU 3028 OE1 GLU A 440 26720 21323 17233 -3654 -1141 2058 O ATOM 3029 OE2 GLU A 440 -0.903 228.120 836.674 1.00173.68 O ANISOU 3029 OE2 GLU A 440 27177 21182 17632 -3046 -1509 2058 O ATOM 3030 N GLU A 441 -7.480 227.809 838.415 1.00128.93 N ANISOU 3030 N GLU A 441 20352 16830 11805 -3375 -701 1562 N ATOM 3031 CA GLU A 441 -8.731 227.318 837.945 1.00130.61 C ANISOU 3031 CA GLU A 441 20324 17430 11871 -3578 -474 1477 C ATOM 3032 C GLU A 441 -9.382 228.580 837.480 1.00123.00 C ANISOU 3032 C GLU A 441 19018 16562 11156 -3248 -420 1225 C ATOM 3033 O GLU A 441 -10.047 228.608 836.462 1.00120.09 O ANISOU 3033 O GLU A 441 18281 16421 10926 -3259 -211 1011 O ATOM 3034 CB GLU A 441 -9.526 226.743 839.097 1.00146.21 C ANISOU 3034 CB GLU A 441 22612 19551 13391 -3805 -550 1743 C ATOM 3035 CG GLU A 441 -9.502 225.240 839.166 1.00158.51 C ANISOU 3035 CG GLU A 441 24348 21227 14651 -4260 -439 1947 C ATOM 3036 CD GLU A 441 -10.595 224.625 838.333 1.00162.56 C ANISOU 3036 CD GLU A 441 24537 22173 15058 -4475 -127 1773 C ATOM 3037 OE1 GLU A 441 -11.509 225.369 837.929 1.00161.50 O ANISOU 3037 OE1 GLU A 441 24110 22234 15019 -4280 -38 1539 O ATOM 3038 OE2 GLU A 441 -10.546 223.402 838.085 1.00162.81 O ANISOU 3038 OE2 GLU A 441 24603 22347 14909 -4838 30 1870 O ATOM 3039 N TYR A 442 -9.181 229.646 838.229 1.00118.45 N ANISOU 3039 N TYR A 442 18563 15803 10640 -2946 -622 1259 N ATOM 3040 CA TYR A 442 -9.817 230.896 837.881 1.00104.50 C ANISOU 3040 CA TYR A 442 16485 14130 9089 -2643 -577 1048 C ATOM 3041 C TYR A 442 -9.457 231.504 836.561 1.00100.39 C ANISOU 3041 C TYR A 442 15577 13575 8991 -2466 -416 800 C ATOM 3042 O TYR A 442 -10.328 231.847 835.792 1.00100.10 O ANISOU 3042 O TYR A 442 15204 13749 9080 -2427 -257 627 O ATOM 3043 CB TYR A 442 -9.412 231.920 838.920 1.00 97.21 C ANISOU 3043 CB TYR A 442 15773 12990 8174 -2337 -845 1133 C ATOM 3044 CG TYR A 442 -9.730 233.334 838.544 1.00 90.70 C ANISOU 3044 CG TYR A 442 14635 12203 7626 -1993 -815 920 C ATOM 3045 CD1 TYR A 442 -8.745 234.219 838.203 1.00 86.60 C ANISOU 3045 CD1 TYR A 442 14023 11462 7421 -1708 -845 815 C ATOM 3046 CE1 TYR A 442 -9.045 235.512 837.881 1.00 83.42 C ANISOU 3046 CE1 TYR A 442 13338 11114 7246 -1417 -807 644 C ATOM 3047 CZ TYR A 442 -10.338 235.931 837.897 1.00 83.12 C ANISOU 3047 CZ TYR A 442 13111 11336 7136 -1408 -758 570 C ATOM 3048 OH TYR A 442 -10.664 237.222 837.574 1.00 69.74 O ANISOU 3048 OH TYR A 442 11135 9704 5660 -1141 -726 409 O ATOM 3049 CE2 TYR A 442 -11.321 235.071 838.235 1.00 87.25 C ANISOU 3049 CE2 TYR A 442 13732 12073 7345 -1676 -738 653 C ATOM 3050 CD2 TYR A 442 -11.018 233.787 838.559 1.00 90.43 C ANISOU 3050 CD2 TYR A 442 14413 12439 7509 -1965 -758 830 C ATOM 3051 N LEU A 443 -8.177 231.630 836.272 1.00101.51 N ANISOU 3051 N LEU A 443 15778 13453 9340 -2364 -466 789 N ATOM 3052 CA LEU A 443 -7.819 232.261 835.017 1.00101.62 C ANISOU 3052 CA LEU A 443 15439 13439 9731 -2193 -326 581 C ATOM 3053 C LEU A 443 -8.208 231.443 833.821 1.00 99.33 C ANISOU 3053 C LEU A 443 14881 13348 9511 -2416 -129 475 C ATOM 3054 O LEU A 443 -8.856 231.924 832.918 1.00 97.40 O ANISOU 3054 O LEU A 443 14291 13250 9468 -2326 -3 317 O ATOM 3055 CB LEU A 443 -6.336 232.576 834.992 1.00 99.50 C ANISOU 3055 CB LEU A 443 15319 12862 9623 -2037 -424 587 C ATOM 3056 CG LEU A 443 -5.437 231.369 835.075 1.00 97.54 C ANISOU 3056 CG LEU A 443 15343 12485 9233 -2298 -476 706 C ATOM 3057 CD1 LEU A 443 -5.709 230.529 833.862 1.00102.66 C ANISOU 3057 CD1 LEU A 443 15724 13330 9952 -2535 -283 607 C ATOM 3058 CD2 LEU A 443 -4.007 231.827 835.122 1.00 87.26 C ANISOU 3058 CD2 LEU A 443 14209 10876 8070 -2105 -591 691 C ATOM 3059 N ALA A 444 -7.879 230.175 833.837 1.00100.58 N ANISOU 3059 N ALA A 444 15204 13527 9482 -2717 -115 570 N ATOM 3060 CA ALA A 444 -8.301 229.360 832.706 1.00 95.16 C ANISOU 3060 CA ALA A 444 14250 13069 8838 -2921 63 455 C ATOM 3061 C ALA A 444 -9.689 229.814 832.285 1.00 84.59 C ANISOU 3061 C ALA A 444 12606 11993 7542 -2853 185 314 C ATOM 3062 O ALA A 444 -10.039 229.808 831.105 1.00 74.23 O ANISOU 3062 O ALA A 444 10968 10811 6424 -2837 304 149 O ATOM 3063 CB ALA A 444 -8.320 227.891 833.088 1.00100.80 C ANISOU 3063 CB ALA A 444 15185 13899 9217 -3303 89 604 C ATOM 3064 N ASN A 445 -10.468 230.219 833.281 1.00 84.31 N ANISOU 3064 N ASN A 445 12700 12029 7306 -2806 128 384 N ATOM 3065 CA ASN A 445 -11.831 230.680 833.076 1.00 85.24 C ANISOU 3065 CA ASN A 445 12585 12398 7405 -2750 223 256 C ATOM 3066 C ASN A 445 -11.871 232.110 832.539 1.00 81.80 C ANISOU 3066 C ASN A 445 11887 11870 7323 -2414 210 119 C ATOM 3067 O ASN A 445 -12.869 232.538 831.964 1.00 82.67 O ANISOU 3067 O ASN A 445 11731 12161 7517 -2357 301 -27 O ATOM 3068 CB ASN A 445 -12.605 230.594 834.395 1.00 96.90 C ANISOU 3068 CB ASN A 445 14329 13996 8492 -2833 142 392 C ATOM 3069 CG ASN A 445 -14.055 230.215 834.199 1.00 97.56 C ANISOU 3069 CG ASN A 445 14264 14443 8362 -2988 295 283 C ATOM 3070 OD1 ASN A 445 -14.361 229.131 833.706 1.00 92.25 O ANISOU 3070 OD1 ASN A 445 13531 13968 7554 -3246 450 246 O ATOM 3071 ND2 ASN A 445 -14.960 231.107 834.594 1.00 98.51 N ANISOU 3071 ND2 ASN A 445 14327 14670 8431 -2830 255 215 N ATOM 3072 N LEU A 446 -10.778 232.844 832.732 1.00 85.89 N ANISOU 3072 N LEU A 446 12493 12113 8029 -2202 100 168 N ATOM 3073 CA LEU A 446 -10.670 234.226 832.265 1.00 77.51 C ANISOU 3073 CA LEU A 446 11204 10964 7282 -1892 96 67 C ATOM 3074 C LEU A 446 -10.139 234.316 830.837 1.00 82.79 C ANISOU 3074 C LEU A 446 11604 11578 8274 -1849 185 -38 C ATOM 3075 O LEU A 446 -10.602 235.141 830.051 1.00 85.44 O ANISOU 3075 O LEU A 446 11657 11973 8832 -1706 236 -144 O ATOM 3076 CB LEU A 446 -9.776 235.040 833.205 1.00 68.70 C ANISOU 3076 CB LEU A 446 10314 9612 6175 -1664 -60 156 C ATOM 3077 CG LEU A 446 -9.173 236.340 832.666 1.00 61.89 C ANISOU 3077 CG LEU A 446 9261 8619 5635 -1362 -52 72 C ATOM 3078 CD1 LEU A 446 -10.251 237.335 832.298 1.00 60.87 C ANISOU 3078 CD1 LEU A 446 8835 8667 5626 -1229 6 -37 C ATOM 3079 CD2 LEU A 446 -8.228 236.949 833.685 1.00 62.23 C ANISOU 3079 CD2 LEU A 446 9569 8448 5627 -1153 -213 146 C ATOM 3080 N GLU A 447 -9.159 233.476 830.510 1.00 87.21 N ANISOU 3080 N GLU A 447 12271 12027 8839 -1982 181 2 N ATOM 3081 CA GLU A 447 -8.633 233.407 829.151 1.00 86.30 C ANISOU 3081 CA GLU A 447 11932 11882 8976 -1969 238 -86 C ATOM 3082 C GLU A 447 -9.796 233.323 828.183 1.00 85.39 C ANISOU 3082 C GLU A 447 11509 12001 8936 -2018 331 -216 C ATOM 3083 O GLU A 447 -9.837 234.025 827.175 1.00 90.40 O ANISOU 3083 O GLU A 447 11902 12623 9822 -1874 343 -297 O ATOM 3084 CB GLU A 447 -7.757 232.170 828.964 1.00 83.41 C ANISOU 3084 CB GLU A 447 11724 11464 8506 -2196 229 -40 C ATOM 3085 CG GLU A 447 -6.486 232.153 829.785 1.00 95.20 C ANISOU 3085 CG GLU A 447 13549 12699 9924 -2166 120 74 C ATOM 3086 CD GLU A 447 -5.845 230.773 829.825 1.00105.08 C ANISOU 3086 CD GLU A 447 15004 13938 10985 -2460 99 142 C ATOM 3087 OE1 GLU A 447 -6.406 229.832 829.218 1.00 98.06 O ANISOU 3087 OE1 GLU A 447 13975 13268 10015 -2682 184 96 O ATOM 3088 OE2 GLU A 447 -4.783 230.633 830.469 1.00110.18 O ANISOU 3088 OE2 GLU A 447 15955 14362 11546 -2468 -8 237 O ATOM 3089 N THR A 448 -10.745 232.455 828.502 1.00 76.11 N ANISOU 3089 N THR A 448 10365 11042 7512 -2227 390 -232 N ATOM 3090 CA THR A 448 -11.867 232.216 827.613 1.00 74.50 C ANISOU 3090 CA THR A 448 9902 11075 7331 -2289 487 -382 C ATOM 3091 C THR A 448 -12.851 233.384 827.585 1.00 58.08 C ANISOU 3091 C THR A 448 7653 9058 5358 -2104 493 -462 C ATOM 3092 O THR A 448 -13.401 233.705 826.535 1.00 62.19 O ANISOU 3092 O THR A 448 7929 9653 6049 -2043 526 -592 O ATOM 3093 CB THR A 448 -12.575 230.881 827.936 1.00 80.52 C ANISOU 3093 CB THR A 448 10749 12087 7760 -2582 584 -394 C ATOM 3094 OG1 THR A 448 -13.988 231.023 827.736 1.00 76.98 O ANISOU 3094 OG1 THR A 448 10131 11879 7238 -2590 678 -533 O ATOM 3095 CG2 THR A 448 -12.311 230.475 829.373 1.00 86.28 C ANISOU 3095 CG2 THR A 448 11824 12772 8185 -2709 532 -215 C ATOM 3096 N ILE A 449 -13.067 234.032 828.723 1.00 49.72 N ANISOU 3096 N ILE A 449 6739 7970 4183 -2015 444 -388 N ATOM 3097 CA ILE A 449 -13.936 235.207 828.738 1.00 59.94 C ANISOU 3097 CA ILE A 449 7875 9330 5568 -1839 440 -468 C ATOM 3098 C ILE A 449 -13.320 236.355 827.933 1.00 58.91 C ANISOU 3098 C ILE A 449 7567 9029 5787 -1611 396 -485 C ATOM 3099 O ILE A 449 -14.029 237.111 827.272 1.00 64.02 O ANISOU 3099 O ILE A 449 7999 9747 6580 -1523 412 -588 O ATOM 3100 CB ILE A 449 -14.271 235.687 830.159 1.00 64.51 C ANISOU 3100 CB ILE A 449 8658 9933 5922 -1777 370 -391 C ATOM 3101 CG1 ILE A 449 -14.835 234.540 830.986 1.00 71.45 C ANISOU 3101 CG1 ILE A 449 9757 10986 6403 -2026 394 -340 C ATOM 3102 CD1 ILE A 449 -16.167 234.037 830.473 1.00 69.18 C ANISOU 3102 CD1 ILE A 449 9304 10994 5986 -2178 527 -502 C ATOM 3103 CG2 ILE A 449 -15.295 236.809 830.103 1.00 58.02 C ANISOU 3103 CG2 ILE A 449 7651 9231 5163 -1629 374 -507 C ATOM 3104 N LEU A 450 -11.999 236.483 827.989 1.00 47.91 N ANISOU 3104 N LEU A 450 6282 7418 4501 -1530 341 -386 N ATOM 3105 CA LEU A 450 -11.314 237.439 827.136 1.00 53.66 C ANISOU 3105 CA LEU A 450 6861 8008 5519 -1348 311 -395 C ATOM 3106 C LEU A 450 -11.638 237.200 825.656 1.00 59.27 C ANISOU 3106 C LEU A 450 7351 8785 6386 -1407 333 -493 C ATOM 3107 O LEU A 450 -12.126 238.104 824.971 1.00 61.03 O ANISOU 3107 O LEU A 450 7394 9031 6763 -1303 314 -556 O ATOM 3108 CB LEU A 450 -9.810 237.403 827.386 1.00 51.31 C ANISOU 3108 CB LEU A 450 6741 7491 5264 -1283 267 -297 C ATOM 3109 CG LEU A 450 -9.455 237.924 828.777 1.00 58.51 C ANISOU 3109 CG LEU A 450 7876 8310 6044 -1154 209 -219 C ATOM 3110 CD1 LEU A 450 -8.035 237.546 829.182 1.00 60.35 C ANISOU 3110 CD1 LEU A 450 8364 8331 6237 -1141 161 -137 C ATOM 3111 CD2 LEU A 450 -9.669 239.434 828.852 1.00 63.92 C ANISOU 3111 CD2 LEU A 450 8417 9006 6864 -912 188 -251 C ATOM 3112 N ARG A 451 -11.383 235.990 825.165 1.00 49.45 N ANISOU 3112 N ARG A 451 6137 7576 5077 -1578 358 -512 N ATOM 3113 CA ARG A 451 -11.697 235.662 823.777 1.00 53.03 C ANISOU 3113 CA ARG A 451 6434 8101 5614 -1590 371 -613 C ATOM 3114 C ARG A 451 -13.107 236.110 823.439 1.00 59.82 C ANISOU 3114 C ARG A 451 7144 9111 6475 -1561 407 -737 C ATOM 3115 O ARG A 451 -13.315 236.932 822.546 1.00 65.80 O ANISOU 3115 O ARG A 451 7839 9808 7353 -1375 395 -769 O ATOM 3116 CB ARG A 451 -11.562 234.162 823.516 1.00 47.70 C ANISOU 3116 CB ARG A 451 5797 7532 4796 -1818 410 -650 C ATOM 3117 CG ARG A 451 -10.164 233.646 823.717 1.00 64.26 C ANISOU 3117 CG ARG A 451 8054 9483 6878 -1869 376 -546 C ATOM 3118 CD ARG A 451 -9.992 232.210 823.271 1.00 58.47 C ANISOU 3118 CD ARG A 451 7340 8875 6000 -2087 411 -590 C ATOM 3119 NE ARG A 451 -8.624 231.782 823.539 1.00 67.75 N ANISOU 3119 NE ARG A 451 8692 9900 7148 -2149 371 -489 N ATOM 3120 CZ ARG A 451 -8.166 230.552 823.345 1.00100.36 C ANISOU 3120 CZ ARG A 451 12889 14108 11136 -2365 383 -495 C ATOM 3121 NH1 ARG A 451 -8.969 229.604 822.874 1.00109.14 N ANISOU 3121 NH1 ARG A 451 13891 15466 12110 -2522 453 -597 N ATOM 3122 NH2 ARG A 451 -6.902 230.272 823.626 1.00110.98 N ANISOU 3122 NH2 ARG A 451 14417 15295 12454 -2420 338 -404 N ATOM 3123 N ASP A 452 -14.074 235.570 824.167 1.00 48.97 N ANISOU 3123 N ASP A 452 5770 7923 4913 -1723 472 -802 N ATOM 3124 CA ASP A 452 -15.466 235.887 823.915 1.00 48.27 C ANISOU 3124 CA ASP A 452 5543 8004 4795 -1725 527 -956 C ATOM 3125 C ASP A 452 -15.724 237.390 823.901 1.00 59.57 C ANISOU 3125 C ASP A 452 6883 9357 6393 -1543 468 -958 C ATOM 3126 O ASP A 452 -16.459 237.878 823.042 1.00 62.84 O ANISOU 3126 O ASP A 452 7192 9797 6886 -1470 485 -1078 O ATOM 3127 CB ASP A 452 -16.359 235.189 824.931 1.00 51.49 C ANISOU 3127 CB ASP A 452 6042 8625 4897 -1878 626 -997 C ATOM 3128 CG ASP A 452 -16.388 233.698 824.731 1.00 66.72 C ANISOU 3128 CG ASP A 452 8017 10697 6638 -2091 715 -1041 C ATOM 3129 OD1 ASP A 452 -15.800 233.218 823.734 1.00 66.81 O ANISOU 3129 OD1 ASP A 452 7963 10651 6770 -2104 697 -1065 O ATOM 3130 OD2 ASP A 452 -17.003 233.007 825.569 1.00 76.46 O ANISOU 3130 OD2 ASP A 452 9359 12119 7574 -2251 803 -1053 O ATOM 3131 N VAL A 453 -15.118 238.119 824.841 1.00 59.04 N ANISOU 3131 N VAL A 453 6911 9185 6335 -1432 421 -829 N ATOM 3132 CA VAL A 453 -15.283 239.573 824.899 1.00 49.22 C ANISOU 3132 CA VAL A 453 5577 7894 5229 -1264 372 -832 C ATOM 3133 C VAL A 453 -14.739 240.257 823.656 1.00 49.04 C ANISOU 3133 C VAL A 453 5570 7691 5370 -1082 340 -809 C ATOM 3134 O VAL A 453 -15.366 241.172 823.126 1.00 44.21 O ANISOU 3134 O VAL A 453 4902 7075 4821 -991 342 -882 O ATOM 3135 CB VAL A 453 -14.634 240.197 826.147 1.00 50.02 C ANISOU 3135 CB VAL A 453 5812 7919 5275 -1138 336 -709 C ATOM 3136 CG2 VAL A 453 -15.491 239.941 827.375 1.00 55.45 C ANISOU 3136 CG2 VAL A 453 6611 8769 5691 -1188 367 -736 C ATOM 3137 CG1 VAL A 453 -14.423 241.695 825.948 1.00 41.74 C ANISOU 3137 CG1 VAL A 453 4650 6802 4406 -959 278 -707 C ATOM 3138 N LYS A 454 -13.580 239.811 823.182 1.00 52.33 N ANISOU 3138 N LYS A 454 6084 7965 5834 -1046 317 -712 N ATOM 3139 CA LYS A 454 -12.991 240.422 821.998 1.00 56.53 C ANISOU 3139 CA LYS A 454 6651 8343 6486 -892 289 -673 C ATOM 3140 C LYS A 454 -13.755 240.100 820.712 1.00 61.63 C ANISOU 3140 C LYS A 454 7246 9029 7141 -913 328 -778 C ATOM 3141 O LYS A 454 -14.018 240.995 819.908 1.00 63.02 O ANISOU 3141 O LYS A 454 7412 9135 7397 -819 319 -800 O ATOM 3142 CB LYS A 454 -11.511 240.062 821.849 1.00 53.19 C ANISOU 3142 CB LYS A 454 6325 7783 6101 -852 257 -559 C ATOM 3143 CG LYS A 454 -10.857 240.738 820.650 1.00 47.13 C ANISOU 3143 CG LYS A 454 5588 6885 5434 -715 228 -514 C ATOM 3144 CD LYS A 454 -9.403 240.341 820.466 1.00 49.47 C ANISOU 3144 CD LYS A 454 5959 7081 5755 -693 205 -429 C ATOM 3145 CE LYS A 454 -8.989 240.535 819.013 1.00 54.24 C ANISOU 3145 CE LYS A 454 6573 7623 6412 -620 190 -411 C ATOM 3146 NZ LYS A 454 -7.515 240.647 818.839 1.00 57.70 N ANISOU 3146 NZ LYS A 454 7069 7967 6887 -573 164 -337 N ATOM 3147 N THR A 455 -14.109 238.833 820.504 1.00 54.01 N ANISOU 3147 N THR A 455 6248 8183 6090 -1053 375 -855 N ATOM 3148 CA THR A 455 -14.852 238.470 819.297 1.00 60.72 C ANISOU 3148 CA THR A 455 7028 9089 6955 -1075 421 -987 C ATOM 3149 C THR A 455 -16.131 239.293 819.220 1.00 62.07 C ANISOU 3149 C THR A 455 7108 9317 7159 -1066 455 -1127 C ATOM 3150 O THR A 455 -16.589 239.660 818.142 1.00 72.98 O ANISOU 3150 O THR A 455 8455 10649 8624 -1015 475 -1213 O ATOM 3151 CB THR A 455 -15.216 236.971 819.253 1.00 61.77 C ANISOU 3151 CB THR A 455 7102 9400 6966 -1262 485 -1098 C ATOM 3152 OG1 THR A 455 -16.383 236.730 820.051 1.00 65.65 O ANISOU 3152 OG1 THR A 455 7501 10089 7355 -1415 545 -1238 O ATOM 3153 CG2 THR A 455 -14.062 236.121 819.762 1.00 59.13 C ANISOU 3153 CG2 THR A 455 6858 9045 6563 -1334 461 -974 C ATOM 3154 N ALA A 456 -16.696 239.579 820.387 1.00 51.74 N ANISOU 3154 N ALA A 456 5756 8118 5785 -1125 464 -1160 N ATOM 3155 CA ALA A 456 -17.931 240.338 820.486 1.00 49.12 C ANISOU 3155 CA ALA A 456 5318 7875 5469 -1135 501 -1319 C ATOM 3156 C ALA A 456 -17.658 241.790 820.155 1.00 58.51 C ANISOU 3156 C ALA A 456 6553 8897 6782 -977 454 -1253 C ATOM 3157 O ALA A 456 -18.400 242.421 819.401 1.00 61.47 O ANISOU 3157 O ALA A 456 6874 9243 7240 -956 487 -1380 O ATOM 3158 CB ALA A 456 -18.497 240.220 821.876 1.00 47.34 C ANISOU 3158 CB ALA A 456 5028 7843 5117 -1248 516 -1359 C ATOM 3159 N PHE A 457 -16.590 242.311 820.751 1.00 62.86 N ANISOU 3159 N PHE A 457 7195 9343 7345 -886 386 -1075 N ATOM 3160 CA PHE A 457 -16.127 243.670 820.511 1.00 55.37 C ANISOU 3160 CA PHE A 457 6295 8253 6490 -760 344 -1005 C ATOM 3161 C PHE A 457 -15.841 243.874 819.031 1.00 58.15 C ANISOU 3161 C PHE A 457 6700 8463 6932 -710 348 -986 C ATOM 3162 O PHE A 457 -16.083 244.948 818.487 1.00 54.48 O ANISOU 3162 O PHE A 457 6235 7924 6542 -670 355 -1020 O ATOM 3163 CB PHE A 457 -14.851 243.928 821.313 1.00 54.66 C ANISOU 3163 CB PHE A 457 6283 8086 6398 -684 282 -838 C ATOM 3164 CG PHE A 457 -15.095 244.423 822.711 1.00 57.76 C ANISOU 3164 CG PHE A 457 6618 8589 6740 -680 266 -853 C ATOM 3165 CD1 PHE A 457 -16.197 244.003 823.433 1.00 65.36 C ANISOU 3165 CD1 PHE A 457 7478 9748 7610 -782 302 -970 C ATOM 3166 CE1 PHE A 457 -16.415 244.464 824.720 1.00 63.72 C ANISOU 3166 CE1 PHE A 457 7201 9668 7341 -768 281 -983 C ATOM 3167 CZ PHE A 457 -15.525 245.337 825.293 1.00 62.06 C ANISOU 3167 CZ PHE A 457 7021 9385 7173 -639 225 -890 C ATOM 3168 CE2 PHE A 457 -14.417 245.753 824.587 1.00 59.18 C ANISOU 3168 CE2 PHE A 457 6758 8825 6902 -550 197 -788 C ATOM 3169 CD2 PHE A 457 -14.205 245.298 823.309 1.00 52.54 C ANISOU 3169 CD2 PHE A 457 5989 7862 6112 -577 216 -764 C ATOM 3170 N ASN A 458 -15.337 242.825 818.385 1.00 56.64 N ANISOU 3170 N ASN A 458 6545 8246 6728 -727 348 -943 N ATOM 3171 CA ASN A 458 -14.903 242.908 816.993 1.00 51.06 C ANISOU 3171 CA ASN A 458 5888 7420 6092 -674 341 -905 C ATOM 3172 C ASN A 458 -15.977 242.621 815.938 1.00 51.46 C ANISOU 3172 C ASN A 458 5860 7500 6194 -724 408 -1078 C ATOM 3173 O ASN A 458 -15.685 242.639 814.742 1.00 57.13 O ANISOU 3173 O ASN A 458 6608 8125 6975 -684 407 -1058 O ATOM 3174 CB ASN A 458 -13.678 242.017 816.766 1.00 53.73 C ANISOU 3174 CB ASN A 458 6293 7720 6402 -653 303 -781 C ATOM 3175 CG ASN A 458 -12.373 242.724 817.084 1.00 55.82 C ANISOU 3175 CG ASN A 458 6643 7873 6695 -563 243 -626 C ATOM 3176 OD1 ASN A 458 -12.282 243.493 818.039 1.00 69.94 O ANISOU 3176 OD1 ASN A 458 8434 9655 8484 -538 227 -601 O ATOM 3177 ND2 ASN A 458 -11.352 242.468 816.274 1.00 51.96 N ANISOU 3177 ND2 ASN A 458 6206 7313 6225 -520 215 -543 N ATOM 3178 N GLU A 459 -17.209 242.372 816.376 1.00 36.95 N ANISOU 3178 N GLU A 459 3908 5796 4337 -813 470 -1265 N ATOM 3179 CA GLU A 459 -18.311 242.147 815.445 1.00 41.02 C ANISOU 3179 CA GLU A 459 4313 6334 4940 -865 550 -1488 C ATOM 3180 C GLU A 459 -18.436 243.334 814.501 1.00 52.21 C ANISOU 3180 C GLU A 459 5752 7574 6512 -798 564 -1500 C ATOM 3181 O GLU A 459 -18.519 244.474 814.942 1.00 51.35 O ANISOU 3181 O GLU A 459 5661 7420 6431 -772 555 -1475 O ATOM 3182 CB GLU A 459 -19.633 241.893 816.178 1.00 46.18 C ANISOU 3182 CB GLU A 459 4817 7175 5556 -977 620 -1720 C ATOM 3183 CG GLU A 459 -20.837 241.772 815.245 1.00 64.12 C ANISOU 3183 CG GLU A 459 6938 9456 7970 -1027 715 -2008 C ATOM 3184 CD GLU A 459 -22.054 241.123 815.895 1.00 69.15 C ANISOU 3184 CD GLU A 459 7399 10334 8540 -1166 793 -2274 C ATOM 3185 OE1 GLU A 459 -23.159 241.248 815.325 1.00 59.32 O ANISOU 3185 OE1 GLU A 459 5997 9101 7443 -1205 876 -2557 O ATOM 3186 OE2 GLU A 459 -21.910 240.485 816.960 1.00 72.47 O ANISOU 3186 OE2 GLU A 459 7827 10934 8775 -1246 779 -2217 O ATOM 3187 N ALA A 460 -18.442 243.059 813.199 1.00 51.13 N ANISOU 3187 N ALA A 460 5604 7337 6487 -779 594 -1550 N ATOM 3188 CA ALA A 460 -18.417 244.116 812.194 1.00 42.81 C ANISOU 3188 CA ALA A 460 4581 6084 5602 -725 620 -1536 C ATOM 3189 C ALA A 460 -19.789 244.730 811.971 1.00 53.36 C ANISOU 3189 C ALA A 460 5769 7369 7135 -770 721 -1789 C ATOM 3190 O ALA A 460 -20.814 244.111 812.255 1.00 66.71 O ANISOU 3190 O ALA A 460 7312 9186 8847 -842 774 -2020 O ATOM 3191 CB ALA A 460 -17.852 243.602 810.896 1.00 44.84 C ANISOU 3191 CB ALA A 460 4871 6234 5931 -682 616 -1486 C ATOM 3192 N SER A 461 -19.800 245.951 811.447 1.00 55.94 N ANISOU 3192 N SER A 461 6120 7511 7624 -735 759 -1763 N ATOM 3193 CA SER A 461 -21.041 246.665 811.218 1.00 64.15 C ANISOU 3193 CA SER A 461 7002 8463 8908 -771 861 -2002 C ATOM 3194 C SER A 461 -20.933 247.471 809.942 1.00 62.12 C ANISOU 3194 C SER A 461 6746 7915 8941 -721 934 -1959 C ATOM 3195 O SER A 461 -21.943 247.827 809.331 1.00 70.23 O ANISOU 3195 O SER A 461 7603 8792 10291 -734 1031 -2161 O ATOM 3196 CB SER A 461 -21.330 247.613 812.377 1.00 74.68 C ANISOU 3196 CB SER A 461 8324 9889 10161 -796 851 -2030 C ATOM 3197 OG SER A 461 -20.615 248.827 812.218 1.00 80.03 O ANISOU 3197 OG SER A 461 9109 10421 10878 -752 850 -1869 O ATOM 3198 N SER A 462 -19.705 247.760 809.536 1.00 47.74 N ANISOU 3198 N SER A 462 5095 6005 7038 -660 891 -1696 N ATOM 3199 CA SER A 462 -19.513 248.629 808.390 1.00 56.38 C ANISOU 3199 CA SER A 462 6187 6833 8402 -594 986 -1589 C ATOM 3200 C SER A 462 -18.076 248.681 807.933 1.00 57.92 C ANISOU 3200 C SER A 462 6547 7022 8440 -501 945 -1275 C ATOM 3201 O SER A 462 -17.159 248.409 808.702 1.00 66.25 O ANISOU 3201 O SER A 462 7751 8225 9197 -522 821 -1181 O ATOM 3202 CB SER A 462 -19.972 250.044 808.718 1.00 76.17 C ANISOU 3202 CB SER A 462 8653 9227 11061 -625 1060 -1655 C ATOM 3203 OG SER A 462 -19.246 250.983 807.947 1.00 88.62 O ANISOU 3203 OG SER A 462 10275 10644 12751 -532 1141 -1407 O ATOM 3204 N ILE A 463 -17.887 249.054 806.677 1.00 54.95 N ANISOU 3204 N ILE A 463 6101 6480 8296 -397 1043 -1106 N ATOM 3205 CA ILE A 463 -16.550 249.157 806.126 1.00 56.81 C ANISOU 3205 CA ILE A 463 6449 6743 8393 -306 1016 -799 C ATOM 3206 C ILE A 463 -16.243 250.592 805.707 1.00 59.86 C ANISOU 3206 C ILE A 463 6817 7009 8918 -265 1122 -614 C ATOM 3207 O ILE A 463 -17.066 251.262 805.091 1.00 67.37 O ANISOU 3207 O ILE A 463 7595 7776 10225 -259 1242 -635 O ATOM 3208 CB ILE A 463 -16.325 248.135 804.976 1.00 70.26 C ANISOU 3208 CB ILE A 463 8059 8445 10193 -219 1011 -692 C ATOM 3209 CG1 ILE A 463 -15.049 248.444 804.191 1.00 69.31 C ANISOU 3209 CG1 ILE A 463 7991 8351 9993 -127 1003 -354 C ATOM 3210 CD1 ILE A 463 -15.258 249.381 803.032 1.00 75.47 C ANISOU 3210 CD1 ILE A 463 8596 8950 11128 -70 1119 -153 C ATOM 3211 CG2 ILE A 463 -17.519 248.097 804.046 1.00 77.00 C ANISOU 3211 CG2 ILE A 463 8654 9112 11491 -182 1107 -808 C ATOM 3212 N THR A 464 -15.062 251.059 806.090 1.00 61.59 N ANISOU 3212 N THR A 464 7184 7343 8873 -245 1073 -445 N ATOM 3213 CA THR A 464 -14.581 252.381 805.739 1.00 66.15 C ANISOU 3213 CA THR A 464 7736 7880 9517 -222 1177 -251 C ATOM 3214 C THR A 464 -13.371 252.215 804.843 1.00 71.62 C ANISOU 3214 C THR A 464 8460 8663 10091 -146 1157 45 C ATOM 3215 O THR A 464 -12.559 251.312 805.037 1.00 70.90 O ANISOU 3215 O THR A 464 8475 8714 9749 -114 1027 62 O ATOM 3216 CB THR A 464 -14.128 253.161 806.986 1.00 69.96 C ANISOU 3216 CB THR A 464 8325 8470 9788 -276 1140 -324 C ATOM 3217 OG1 THR A 464 -15.244 253.383 807.856 1.00 80.04 O ANISOU 3217 OG1 THR A 464 9552 9698 11162 -360 1150 -590 O ATOM 3218 CG2 THR A 464 -13.514 254.496 806.587 1.00 65.21 C ANISOU 3218 CG2 THR A 464 7679 7870 9227 -272 1265 -118 C ATOM 3219 N LEU A 465 -13.222 253.103 803.898 1.00 72.75 N ANISOU 3219 N LEU A 465 8495 8738 10407 -148 1276 283 N ATOM 3220 CA LEU A 465 -12.086 252.991 803.070 1.00 69.73 C ANISOU 3220 CA LEU A 465 8141 8472 9881 -117 1249 568 C ATOM 3221 C LEU A 465 -11.214 254.071 803.617 1.00 77.03 C ANISOU 3221 C LEU A 465 9162 9517 10589 -159 1288 627 C ATOM 3222 O LEU A 465 -11.511 255.224 803.443 1.00 86.01 O ANISOU 3222 O LEU A 465 10232 10572 11875 -239 1421 717 O ATOM 3223 CB LEU A 465 -12.473 253.333 801.654 1.00 67.05 C ANISOU 3223 CB LEU A 465 7635 7966 9874 -165 1334 845 C ATOM 3224 CG LEU A 465 -11.863 252.444 800.598 1.00 72.68 C ANISOU 3224 CG LEU A 465 8330 8728 10558 -138 1244 1083 C ATOM 3225 CD1 LEU A 465 -12.570 251.147 800.580 1.00 62.76 C ANISOU 3225 CD1 LEU A 465 6951 7434 9462 -61 1179 876 C ATOM 3226 CD2 LEU A 465 -12.001 253.108 799.284 1.00 81.16 C ANISOU 3226 CD2 LEU A 465 9364 9569 11904 -251 1270 1459 C ATOM 3227 N TYR A 466 -10.112 253.713 804.252 1.00 75.52 N ANISOU 3227 N TYR A 466 9105 9510 10080 -125 1173 580 N ATOM 3228 CA TYR A 466 -9.174 254.684 804.784 1.00 71.95 C ANISOU 3228 CA TYR A 466 8715 9177 9444 -165 1213 613 C ATOM 3229 C TYR A 466 -8.471 254.879 803.468 1.00 85.19 C ANISOU 3229 C TYR A 466 10381 10910 11076 -189 1272 924 C ATOM 3230 O TYR A 466 -7.389 254.404 803.245 1.00 81.87 O ANISOU 3230 O TYR A 466 10034 10639 10433 -166 1190 993 O ATOM 3231 CB TYR A 466 -8.276 253.990 805.783 1.00 60.03 C ANISOU 3231 CB TYR A 466 7314 7803 7693 -130 1045 461 C ATOM 3232 CG TYR A 466 -7.290 254.813 806.557 1.00 52.10 C ANISOU 3232 CG TYR A 466 6353 6912 6530 -162 1071 439 C ATOM 3233 CD1 TYR A 466 -7.650 255.451 807.710 1.00 59.60 C ANISOU 3233 CD1 TYR A 466 7293 7838 7515 -202 1088 284 C ATOM 3234 CE1 TYR A 466 -6.754 256.161 808.423 1.00 63.07 C ANISOU 3234 CE1 TYR A 466 7745 8387 7833 -224 1125 267 C ATOM 3235 CZ TYR A 466 -5.467 256.214 808.016 1.00 65.92 C ANISOU 3235 CZ TYR A 466 8148 8875 8022 -211 1152 381 C ATOM 3236 OH TYR A 466 -4.550 256.928 808.723 1.00 69.43 O ANISOU 3236 OH TYR A 466 8600 9433 8348 -229 1221 352 O ATOM 3237 CE2 TYR A 466 -5.077 255.565 806.897 1.00 62.55 C ANISOU 3237 CE2 TYR A 466 7751 8478 7535 -185 1124 522 C ATOM 3238 CD2 TYR A 466 -5.980 254.868 806.185 1.00 52.54 C ANISOU 3238 CD2 TYR A 466 6454 7111 6400 -159 1076 558 C ATOM 3239 N GLY A 467 -9.118 255.640 802.608 1.00104.56 N ANISOU 3239 N GLY A 467 12746 13221 13759 -269 1408 1123 N ATOM 3240 CA GLY A 467 -8.675 255.908 801.263 1.00103.69 C ANISOU 3240 CA GLY A 467 12655 13092 13649 -345 1443 1489 C ATOM 3241 C GLY A 467 -7.288 256.382 801.349 1.00 95.24 C ANISOU 3241 C GLY A 467 11716 12236 12233 -380 1461 1582 C ATOM 3242 O GLY A 467 -6.869 256.779 802.415 1.00 88.73 O ANISOU 3242 O GLY A 467 10919 11521 11273 -364 1491 1381 O ATOM 3243 N ASP A 468 -6.566 256.244 800.244 1.00 94.60 N ANISOU 3243 N ASP A 468 11727 12204 12013 -427 1420 1881 N ATOM 3244 CA ASP A 468 -7.152 255.753 798.988 1.00 90.13 C ANISOU 3244 CA ASP A 468 11137 11446 11661 -446 1339 2150 C ATOM 3245 C ASP A 468 -7.773 254.364 798.832 1.00 85.69 C ANISOU 3245 C ASP A 468 10479 10804 11273 -338 1198 2039 C ATOM 3246 O ASP A 468 -8.890 254.231 798.380 1.00 93.52 O ANISOU 3246 O ASP A 468 11362 11538 12634 -346 1200 2090 O ATOM 3247 CB ASP A 468 -6.023 255.714 797.947 1.00 85.89 C ANISOU 3247 CB ASP A 468 10774 11012 10847 -500 1251 2483 C ATOM 3248 CG ASP A 468 -5.429 257.051 797.664 1.00 90.80 C ANISOU 3248 CG ASP A 468 11516 11685 11299 -644 1396 2717 C ATOM 3249 OD1 ASP A 468 -5.978 258.057 798.121 1.00 92.17 O ANISOU 3249 OD1 ASP A 468 11615 11779 11627 -719 1570 2670 O ATOM 3250 OD2 ASP A 468 -4.410 257.089 796.959 1.00 94.55 O ANISOU 3250 OD2 ASP A 468 12161 12286 11478 -694 1337 2955 O ATOM 3251 N GLU A 469 -7.045 253.343 799.222 1.00 65.84 N ANISOU 3251 N GLU A 469 7998 8495 8523 -253 1081 1879 N ATOM 3252 CA GLU A 469 -7.479 251.972 799.122 1.00 70.89 C ANISOU 3252 CA GLU A 469 8545 9111 9278 -170 966 1776 C ATOM 3253 C GLU A 469 -7.521 251.101 800.343 1.00 81.81 C ANISOU 3253 C GLU A 469 9892 10619 10572 -78 916 1395 C ATOM 3254 O GLU A 469 -7.912 249.971 800.233 1.00 85.76 O ANISOU 3254 O GLU A 469 10310 11111 11163 -31 845 1322 O ATOM 3255 CB GLU A 469 -6.529 251.281 798.191 1.00 82.26 C ANISOU 3255 CB GLU A 469 10080 10651 10523 -175 806 2014 C ATOM 3256 CG GLU A 469 -5.201 251.146 798.817 1.00 92.75 C ANISOU 3256 CG GLU A 469 11516 12250 11474 -176 764 1867 C ATOM 3257 CD GLU A 469 -4.128 251.138 797.808 1.00103.77 C ANISOU 3257 CD GLU A 469 13065 13737 12627 -231 652 2155 C ATOM 3258 OE1 GLU A 469 -2.960 250.980 798.190 1.00107.30 O ANISOU 3258 OE1 GLU A 469 13606 14383 12780 -251 617 2045 O ATOM 3259 OE2 GLU A 469 -4.455 251.298 796.626 1.00108.44 O ANISOU 3259 OE2 GLU A 469 13698 14164 13341 -253 575 2500 O ATOM 3260 N ILE A 470 -7.120 251.576 801.502 1.00 80.87 N ANISOU 3260 N ILE A 470 9851 10586 10292 -68 930 1176 N ATOM 3261 CA ILE A 470 -7.134 250.721 802.676 1.00 57.20 C ANISOU 3261 CA ILE A 470 6882 7635 7218 -13 815 873 C ATOM 3262 C ILE A 470 -8.491 250.267 803.092 1.00 47.81 C ANISOU 3262 C ILE A 470 5642 6290 6235 12 822 696 C ATOM 3263 O ILE A 470 -9.426 251.003 802.991 1.00 51.26 O ANISOU 3263 O ILE A 470 6020 6574 6883 -9 942 697 O ATOM 3264 CB ILE A 470 -6.544 251.431 803.839 1.00 48.30 C ANISOU 3264 CB ILE A 470 5843 6556 5953 -36 811 723 C ATOM 3265 CG1 ILE A 470 -5.286 252.163 803.413 1.00 55.36 C ANISOU 3265 CG1 ILE A 470 6796 7581 6657 -83 869 887 C ATOM 3266 CD1 ILE A 470 -4.142 251.312 803.278 1.00 54.45 C ANISOU 3266 CD1 ILE A 470 6725 7607 6357 -86 756 886 C ATOM 3267 CG2 ILE A 470 -6.253 250.469 804.910 1.00 36.79 C ANISOU 3267 CG2 ILE A 470 4427 5141 4413 -26 650 506 C ATOM 3268 N ILE A 471 -8.598 249.040 803.567 1.00 45.17 N ANISOU 3268 N ILE A 471 5331 5994 5840 28 699 536 N ATOM 3269 CA ILE A 471 -9.897 248.541 803.996 1.00 49.69 C ANISOU 3269 CA ILE A 471 5882 6433 6565 8 715 340 C ATOM 3270 C ILE A 471 -10.026 248.613 805.503 1.00 58.47 C ANISOU 3270 C ILE A 471 7106 7553 7558 -59 631 113 C ATOM 3271 O ILE A 471 -9.336 247.900 806.224 1.00 71.80 O ANISOU 3271 O ILE A 471 8851 9354 9078 -86 486 45 O ATOM 3272 CB ILE A 471 -10.097 247.079 803.577 1.00 50.80 C ANISOU 3272 CB ILE A 471 5961 6621 6721 18 654 301 C ATOM 3273 CG1 ILE A 471 -10.060 246.949 802.056 1.00 49.44 C ANISOU 3273 CG1 ILE A 471 5611 6430 6744 69 717 547 C ATOM 3274 CD1 ILE A 471 -10.445 245.584 801.569 1.00 54.91 C ANISOU 3274 CD1 ILE A 471 6167 7148 7547 86 676 477 C ATOM 3275 CG2 ILE A 471 -11.402 246.532 804.135 1.00 48.61 C ANISOU 3275 CG2 ILE A 471 5656 6245 6569 -35 677 43 C ATOM 3276 N LEU A 472 -10.922 249.466 805.984 1.00 58.85 N ANISOU 3276 N LEU A 472 7147 7482 7731 -102 718 9 N ATOM 3277 CA LEU A 472 -11.126 249.604 807.419 1.00 54.45 C ANISOU 3277 CA LEU A 472 6657 6947 7083 -184 636 -177 C ATOM 3278 C LEU A 472 -12.498 249.076 807.810 1.00 54.51 C ANISOU 3278 C LEU A 472 6619 6890 7201 -261 650 -389 C ATOM 3279 O LEU A 472 -13.508 249.511 807.278 1.00 68.89 O ANISOU 3279 O LEU A 472 8348 8578 9248 -263 785 -441 O ATOM 3280 CB LEU A 472 -10.974 251.068 807.832 1.00 54.13 C ANISOU 3280 CB LEU A 472 6621 6879 7066 -197 719 -153 C ATOM 3281 CG LEU A 472 -10.578 251.385 809.274 1.00 60.80 C ANISOU 3281 CG LEU A 472 7512 7802 7788 -257 619 -258 C ATOM 3282 CD1 LEU A 472 -11.762 251.279 810.215 1.00 66.85 C ANISOU 3282 CD1 LEU A 472 8252 8537 8610 -351 594 -463 C ATOM 3283 CD2 LEU A 472 -9.448 250.485 809.724 1.00 70.23 C ANISOU 3283 CD2 LEU A 472 8742 9114 8827 -247 454 -227 C ATOM 3284 N VAL A 473 -12.535 248.130 808.738 1.00 43.58 N ANISOU 3284 N VAL A 473 5260 5608 5688 -334 514 -515 N ATOM 3285 CA VAL A 473 -13.805 247.583 809.204 1.00 50.62 C ANISOU 3285 CA VAL A 473 6082 6499 6652 -425 526 -731 C ATOM 3286 CB VAL A 473 -13.800 246.037 809.162 1.00 55.84 C ANISOU 3286 CB VAL A 473 6712 7273 7233 -450 451 -785 C ATOM 3287 CG1 VAL A 473 -14.962 245.462 809.959 1.00 57.38 C ANISOU 3287 CG1 VAL A 473 6798 7566 7437 -514 481 -959 C ATOM 3288 CG2 VAL A 473 -13.849 245.554 807.727 1.00 56.10 C ANISOU 3288 CG2 VAL A 473 6680 7249 7385 -357 547 -714 C ATOM 3289 C VAL A 473 -14.111 248.067 810.618 1.00 49.32 C ANISOU 3289 C VAL A 473 5902 6422 6415 -485 483 -806 C ATOM 3290 O VAL A 473 -13.309 247.873 811.529 1.00 57.14 O ANISOU 3290 O VAL A 473 6923 7526 7263 -464 386 -712 O ATOM 3291 N ASN A 474 -15.265 248.703 810.797 1.00 45.43 N ANISOU 3291 N ASN A 474 5328 5878 6056 -528 580 -956 N ATOM 3292 CA ASN A 474 -15.639 249.244 812.102 1.00 52.80 C ANISOU 3292 CA ASN A 474 6215 6919 6927 -561 563 -1018 C ATOM 3293 C ASN A 474 -16.484 248.265 812.908 1.00 59.14 C ANISOU 3293 C ASN A 474 6924 7878 7671 -598 546 -1134 C ATOM 3294 O ASN A 474 -17.456 247.703 812.404 1.00 56.93 O ANISOU 3294 O ASN A 474 6550 7589 7494 -634 612 -1291 O ATOM 3295 CB ASN A 474 -16.399 250.558 811.948 1.00 44.30 C ANISOU 3295 CB ASN A 474 5079 5720 6031 -595 682 -1142 C ATOM 3296 CG ASN A 474 -15.835 251.427 810.858 1.00 54.53 C ANISOU 3296 CG ASN A 474 6448 6803 7467 -563 769 -1049 C ATOM 3297 OD1 ASN A 474 -14.679 251.844 810.912 1.00 51.70 O ANISOU 3297 OD1 ASN A 474 6171 6484 6989 -509 737 -874 O ATOM 3298 ND2 ASN A 474 -16.654 251.712 809.855 1.00 67.96 N ANISOU 3298 ND2 ASN A 474 8045 8341 9434 -537 919 -1091 N ATOM 3299 N CYS A 475 -16.113 248.077 814.166 1.00 57.23 N ANISOU 3299 N CYS A 475 6690 7768 7287 -591 473 -1072 N ATOM 3300 CA CYS A 475 -16.755 247.081 815.003 1.00 49.50 C ANISOU 3300 CA CYS A 475 5633 6940 6235 -630 467 -1156 C ATOM 3301 C CYS A 475 -17.763 247.712 815.945 1.00 46.53 C ANISOU 3301 C CYS A 475 5151 6658 5870 -676 503 -1313 C ATOM 3302 O CYS A 475 -17.894 248.931 816.009 1.00 46.55 O ANISOU 3302 O CYS A 475 5140 6605 5942 -673 528 -1355 O ATOM 3303 CB CYS A 475 -15.700 246.323 815.792 1.00 54.23 C ANISOU 3303 CB CYS A 475 6297 7603 6706 -595 384 -991 C ATOM 3304 SG CYS A 475 -14.311 245.840 814.766 1.00 81.34 S ANISOU 3304 SG CYS A 475 9839 10934 10132 -531 330 -816 S ATOM 3305 N PHE A 476 -18.472 246.862 816.673 1.00 55.73 N ANISOU 3305 N PHE A 476 6229 7981 6964 -727 512 -1418 N ATOM 3306 CA PHE A 476 -19.574 247.287 817.527 1.00 53.07 C ANISOU 3306 CA PHE A 476 5761 7778 6626 -779 548 -1607 C ATOM 3307 C PHE A 476 -19.086 248.099 818.714 1.00 56.49 C ANISOU 3307 C PHE A 476 6213 8266 6986 -737 489 -1521 C ATOM 3308 O PHE A 476 -19.532 249.222 818.930 1.00 82.61 O ANISOU 3308 O PHE A 476 9457 11574 10358 -738 512 -1631 O ATOM 3309 CB PHE A 476 -20.363 246.062 818.000 1.00 68.23 C ANISOU 3309 CB PHE A 476 7580 9887 8459 -860 577 -1738 C ATOM 3310 CG PHE A 476 -21.423 245.608 817.028 1.00 68.83 C ANISOU 3310 CG PHE A 476 7539 9962 8653 -924 667 -1975 C ATOM 3311 CD1 PHE A 476 -22.244 244.539 817.332 1.00 60.84 C ANISOU 3311 CD1 PHE A 476 6404 9143 7569 -1023 715 -2153 C ATOM 3312 CE1 PHE A 476 -23.222 244.133 816.449 1.00 65.81 C ANISOU 3312 CE1 PHE A 476 6894 9775 8334 -1080 805 -2415 C ATOM 3313 CZ PHE A 476 -23.399 244.800 815.248 1.00 62.87 C ANISOU 3313 CZ PHE A 476 6507 9181 8201 -1029 846 -2486 C ATOM 3314 CE2 PHE A 476 -22.598 245.870 814.936 1.00 58.98 C ANISOU 3314 CE2 PHE A 476 6147 8489 7773 -942 806 -2288 C ATOM 3315 CD2 PHE A 476 -21.616 246.273 815.825 1.00 67.58 C ANISOU 3315 CD2 PHE A 476 7373 9608 8696 -895 717 -2043 C ATOM 3316 N GLN A 477 -18.159 247.530 819.476 1.00 56.39 N ANISOU 3316 N GLN A 477 6272 8293 6860 -701 421 -1346 N ATOM 3317 CA GLN A 477 -17.559 248.230 820.607 1.00 57.47 C ANISOU 3317 CA GLN A 477 6418 8472 6946 -645 364 -1265 C ATOM 3318 C GLN A 477 -16.741 249.417 820.158 1.00 56.74 C ANISOU 3318 C GLN A 477 6394 8241 6922 -590 347 -1190 C ATOM 3319 O GLN A 477 -15.878 249.283 819.286 1.00 62.50 O ANISOU 3319 O GLN A 477 7226 8839 7681 -563 334 -1064 O ATOM 3320 CB GLN A 477 -16.664 247.295 821.412 1.00 60.97 C ANISOU 3320 CB GLN A 477 6919 8948 7300 -620 311 -1106 C ATOM 3321 CG GLN A 477 -17.354 246.734 822.603 1.00 66.62 C ANISOU 3321 CG GLN A 477 7537 9861 7914 -671 316 -1180 C ATOM 3322 CD GLN A 477 -17.833 247.819 823.518 1.00 76.68 C ANISOU 3322 CD GLN A 477 8712 11251 9171 -634 302 -1280 C ATOM 3323 OE1 GLN A 477 -17.076 248.722 823.877 1.00 67.82 O ANISOU 3323 OE1 GLN A 477 7618 10075 8074 -546 258 -1213 O ATOM 3324 NE2 GLN A 477 -19.104 247.748 823.903 1.00 87.51 N ANISOU 3324 NE2 GLN A 477 9946 12807 10496 -702 341 -1469 N ATOM 3325 N PRO A 478 -17.001 250.582 820.766 1.00 43.44 N ANISOU 3325 N PRO A 478 4638 6612 5257 -580 350 -1287 N ATOM 3326 CA PRO A 478 -16.270 251.805 820.445 1.00 38.44 C ANISOU 3326 CA PRO A 478 4044 5881 4681 -556 351 -1256 C ATOM 3327 C PRO A 478 -14.772 251.585 820.603 1.00 49.06 C ANISOU 3327 C PRO A 478 5493 7174 5972 -491 285 -1053 C ATOM 3328 O PRO A 478 -14.362 250.831 821.488 1.00 58.16 O ANISOU 3328 O PRO A 478 6653 8392 7054 -448 236 -971 O ATOM 3329 CB PRO A 478 -16.770 252.795 821.495 1.00 44.40 C ANISOU 3329 CB PRO A 478 4671 6766 5431 -549 348 -1413 C ATOM 3330 CG PRO A 478 -18.102 252.277 821.908 1.00 47.29 C ANISOU 3330 CG PRO A 478 4921 7267 5780 -587 372 -1574 C ATOM 3331 CD PRO A 478 -17.981 250.787 821.847 1.00 48.22 C ANISOU 3331 CD PRO A 478 5102 7401 5819 -595 354 -1451 C ATOM 3332 N TYR A 479 -13.982 252.231 819.749 1.00 52.36 N ANISOU 3332 N TYR A 479 5982 7478 6437 -491 297 -994 N ATOM 3333 CA TYR A 479 -12.523 252.153 819.800 1.00 49.65 C ANISOU 3333 CA TYR A 479 5713 7097 6056 -436 243 -842 C ATOM 3334 C TYR A 479 -11.997 250.830 819.268 1.00 50.42 C ANISOU 3334 C TYR A 479 5893 7125 6138 -410 214 -708 C ATOM 3335 O TYR A 479 -10.806 250.544 819.368 1.00 67.32 O ANISOU 3335 O TYR A 479 8082 9237 8262 -365 174 -600 O ATOM 3336 CB TYR A 479 -12.017 252.395 821.223 1.00 51.10 C ANISOU 3336 CB TYR A 479 5839 7395 6180 -378 193 -838 C ATOM 3337 CG TYR A 479 -12.694 253.553 821.907 1.00 47.44 C ANISOU 3337 CG TYR A 479 5260 7041 5724 -393 213 -1009 C ATOM 3338 CD1 TYR A 479 -13.415 253.369 823.081 1.00 50.34 C ANISOU 3338 CD1 TYR A 479 5533 7548 6044 -358 188 -1091 C ATOM 3339 CE1 TYR A 479 -14.045 254.429 823.704 1.00 57.99 C ANISOU 3339 CE1 TYR A 479 6374 8632 7027 -358 198 -1280 C ATOM 3340 CZ TYR A 479 -13.964 255.695 823.150 1.00 56.50 C ANISOU 3340 CZ TYR A 479 6152 8399 6919 -415 250 -1397 C ATOM 3341 OH TYR A 479 -14.583 256.756 823.776 1.00 56.55 O ANISOU 3341 OH TYR A 479 6010 8510 6967 -420 265 -1624 O ATOM 3342 CE2 TYR A 479 -13.262 255.898 821.975 1.00 55.61 C ANISOU 3342 CE2 TYR A 479 6142 8136 6853 -469 292 -1309 C ATOM 3343 CD2 TYR A 479 -12.635 254.830 821.364 1.00 46.72 C ANISOU 3343 CD2 TYR A 479 5142 6917 5693 -447 264 -1112 C ATOM 3344 N ASN A 480 -12.885 250.024 818.701 1.00 40.58 N ANISOU 3344 N ASN A 480 4645 5865 4907 -445 243 -745 N ATOM 3345 CA ASN A 480 -12.464 248.773 818.088 1.00 39.30 C ANISOU 3345 CA ASN A 480 4542 5655 4736 -432 225 -656 C ATOM 3346 C ASN A 480 -12.683 248.741 816.600 1.00 40.99 C ANISOU 3346 C ASN A 480 4790 5783 4999 -449 257 -667 C ATOM 3347 O ASN A 480 -13.807 248.752 816.124 1.00 60.83 O ANISOU 3347 O ASN A 480 7258 8297 7556 -495 314 -784 O ATOM 3348 CB ASN A 480 -13.140 247.589 818.754 1.00 46.68 C ANISOU 3348 CB ASN A 480 5434 6678 5626 -462 230 -695 C ATOM 3349 CG ASN A 480 -12.609 247.342 820.128 1.00 53.62 C ANISOU 3349 CG ASN A 480 6300 7616 6456 -436 194 -645 C ATOM 3350 OD1 ASN A 480 -11.714 246.517 820.320 1.00 50.02 O ANISOU 3350 OD1 ASN A 480 5891 7125 5989 -418 171 -556 O ATOM 3351 ND2 ASN A 480 -13.120 248.090 821.097 1.00 58.01 N ANISOU 3351 ND2 ASN A 480 6785 8265 6990 -433 194 -717 N ATOM 3352 N HIS A 481 -11.580 248.720 815.874 1.00 20.68 N ANISOU 3352 N HIS A 481 2286 3143 2430 -411 226 -563 N ATOM 3353 CA HIS A 481 -11.606 248.681 814.433 1.00 32.88 C ANISOU 3353 CA HIS A 481 3867 4611 4014 -416 249 -557 C ATOM 3354 C HIS A 481 -10.667 247.590 813.967 1.00 44.89 C ANISOU 3354 C HIS A 481 5423 6131 5502 -377 199 -460 C ATOM 3355 O HIS A 481 -9.798 247.140 814.716 1.00 44.50 O ANISOU 3355 O HIS A 481 5380 6108 5421 -350 160 -397 O ATOM 3356 CB HIS A 481 -11.183 250.025 813.856 1.00 29.01 C ANISOU 3356 CB HIS A 481 3411 4052 3561 -427 278 -557 C ATOM 3357 CG HIS A 481 -12.000 251.169 814.363 1.00 45.57 C ANISOU 3357 CG HIS A 481 5461 6144 5708 -476 347 -675 C ATOM 3358 ND1 HIS A 481 -13.191 251.547 813.785 1.00 61.34 N ANISOU 3358 ND1 HIS A 481 7424 8063 7818 -523 448 -800 N ATOM 3359 CE1 HIS A 481 -13.696 252.572 814.447 1.00 63.04 C ANISOU 3359 CE1 HIS A 481 7579 8294 8079 -563 501 -911 C ATOM 3360 NE2 HIS A 481 -12.875 252.867 815.441 1.00 63.42 N ANISOU 3360 NE2 HIS A 481 7625 8442 8031 -544 429 -859 N ATOM 3361 CD2 HIS A 481 -11.808 252.006 815.412 1.00 47.78 C ANISOU 3361 CD2 HIS A 481 5702 6489 5964 -487 339 -710 C ATOM 3362 N SER A 482 -10.863 247.155 812.729 1.00 46.93 N ANISOU 3362 N SER A 482 5694 6355 5783 -380 212 -466 N ATOM 3363 CA SER A 482 -10.042 246.109 812.156 1.00 40.71 C ANISOU 3363 CA SER A 482 4919 5588 4961 -351 170 -397 C ATOM 3364 C SER A 482 -9.601 246.517 810.766 1.00 47.91 C ANISOU 3364 C SER A 482 5861 6459 5885 -334 161 -361 C ATOM 3365 O SER A 482 -10.430 246.796 809.905 1.00 68.44 O ANISOU 3365 O SER A 482 8467 8992 8545 -354 219 -423 O ATOM 3366 CB SER A 482 -10.827 244.812 812.113 1.00 41.87 C ANISOU 3366 CB SER A 482 5021 5792 5096 -385 193 -467 C ATOM 3367 OG SER A 482 -11.384 244.530 813.382 1.00 50.02 O ANISOU 3367 OG SER A 482 6017 6882 6106 -420 210 -518 O ATOM 3368 N LEU A 483 -8.291 246.583 810.562 1.00 35.20 N ANISOU 3368 N LEU A 483 4256 4882 4234 -302 111 -274 N ATOM 3369 CA LEU A 483 -7.734 246.880 809.250 1.00 35.88 C ANISOU 3369 CA LEU A 483 4350 4980 4302 -237 147 -173 C ATOM 3370 C LEU A 483 -7.287 245.592 808.589 1.00 46.71 C ANISOU 3370 C LEU A 483 5679 6438 5629 -231 91 -142 C ATOM 3371 O LEU A 483 -6.594 244.779 809.195 1.00 56.26 O ANISOU 3371 O LEU A 483 6867 7692 6817 -263 46 -157 O ATOM 3372 CB LEU A 483 -6.574 247.877 809.345 1.00 35.24 C ANISOU 3372 CB LEU A 483 4281 4923 4185 -197 183 -90 C ATOM 3373 CG LEU A 483 -5.480 247.952 808.273 1.00 45.20 C ANISOU 3373 CG LEU A 483 5532 6261 5381 -140 230 40 C ATOM 3374 CD1 LEU A 483 -5.990 247.645 806.894 1.00 62.67 C ANISOU 3374 CD1 LEU A 483 7719 8482 7612 -90 282 141 C ATOM 3375 CD2 LEU A 483 -4.885 249.343 808.271 1.00 44.88 C ANISOU 3375 CD2 LEU A 483 5525 6230 5299 -117 342 105 C ATOM 3376 N TYR A 484 -7.709 245.413 807.344 1.00 44.29 N ANISOU 3376 N TYR A 484 5362 6129 5336 -170 164 -69 N ATOM 3377 CA TYR A 484 -7.305 244.274 806.548 1.00 40.09 C ANISOU 3377 CA TYR A 484 4775 5706 4754 -156 130 -17 C ATOM 3378 C TYR A 484 -6.168 244.674 805.623 1.00 44.52 C ANISOU 3378 C TYR A 484 5299 6347 5269 -100 150 157 C ATOM 3379 O TYR A 484 -6.336 245.519 804.741 1.00 47.90 O ANISOU 3379 O TYR A 484 5720 6739 5741 -38 255 298 O ATOM 3380 CB TYR A 484 -8.501 243.746 805.769 1.00 41.05 C ANISOU 3380 CB TYR A 484 4860 5784 4955 -132 229 -39 C ATOM 3381 CG TYR A 484 -9.473 243.008 806.651 1.00 40.66 C ANISOU 3381 CG TYR A 484 4810 5722 4918 -222 214 -251 C ATOM 3382 CD1 TYR A 484 -9.438 241.623 806.747 1.00 33.75 C ANISOU 3382 CD1 TYR A 484 3883 4967 3974 -273 171 -335 C ATOM 3383 CE1 TYR A 484 -10.310 240.945 807.560 1.00 38.33 C ANISOU 3383 CE1 TYR A 484 4435 5571 4559 -368 174 -523 C ATOM 3384 CZ TYR A 484 -11.235 241.646 808.299 1.00 50.74 C ANISOU 3384 CZ TYR A 484 6022 7052 6206 -407 214 -617 C ATOM 3385 OH TYR A 484 -12.115 240.972 809.113 1.00 57.12 O ANISOU 3385 OH TYR A 484 6764 7920 7019 -472 267 -749 O ATOM 3386 CE2 TYR A 484 -11.286 243.022 808.231 1.00 45.02 C ANISOU 3386 CE2 TYR A 484 5355 6203 5546 -370 237 -557 C ATOM 3387 CD2 TYR A 484 -10.404 243.693 807.409 1.00 34.61 C ANISOU 3387 CD2 TYR A 484 4071 4854 4226 -271 251 -369 C ATOM 3388 N LYS A 485 -5.006 244.071 805.846 1.00 39.36 N ANISOU 3388 N LYS A 485 4608 5803 4546 -151 75 148 N ATOM 3389 CA LYS A 485 -3.804 244.434 805.112 1.00 51.22 C ANISOU 3389 CA LYS A 485 6097 7395 5970 -148 114 279 C ATOM 3390 C LYS A 485 -3.464 243.447 803.996 1.00 61.88 C ANISOU 3390 C LYS A 485 7366 8884 7262 -166 90 393 C ATOM 3391 O LYS A 485 -3.695 242.236 804.114 1.00 60.51 O ANISOU 3391 O LYS A 485 7126 8773 7090 -205 22 325 O ATOM 3392 CB LYS A 485 -2.609 244.547 806.056 1.00 46.71 C ANISOU 3392 CB LYS A 485 5571 6827 5350 -217 103 203 C ATOM 3393 CG LYS A 485 -1.346 245.029 805.374 1.00 43.49 C ANISOU 3393 CG LYS A 485 5231 6500 4793 -234 163 316 C ATOM 3394 CD LYS A 485 -0.117 244.689 806.177 1.00 52.77 C ANISOU 3394 CD LYS A 485 6473 7683 5894 -308 155 239 C ATOM 3395 CE LYS A 485 0.336 243.269 805.901 1.00 59.60 C ANISOU 3395 CE LYS A 485 7297 8628 6720 -397 95 234 C ATOM 3396 NZ LYS A 485 1.704 243.037 806.440 1.00 70.11 N ANISOU 3396 NZ LYS A 485 8751 9959 7929 -472 108 197 N ATOM 3397 N LEU A 486 -2.903 243.983 802.918 1.00 58.11 N ANISOU 3397 N LEU A 486 6909 8465 6706 -158 141 587 N ATOM 3398 CA LEU A 486 -2.422 243.164 801.824 1.00 55.22 C ANISOU 3398 CA LEU A 486 6502 8228 6251 -202 95 751 C ATOM 3399 C LEU A 486 -1.191 242.416 802.308 1.00 64.66 C ANISOU 3399 C LEU A 486 7743 9506 7321 -313 35 654 C ATOM 3400 O LEU A 486 -0.304 243.008 802.924 1.00 73.43 O ANISOU 3400 O LEU A 486 8970 10580 8349 -346 61 588 O ATOM 3401 CB LEU A 486 -2.051 244.048 800.641 1.00 64.86 C ANISOU 3401 CB LEU A 486 7820 9449 7375 -195 111 1026 C ATOM 3402 CG LEU A 486 -2.281 243.452 799.258 1.00 69.18 C ANISOU 3402 CG LEU A 486 8335 10021 7927 -181 0 1308 C ATOM 3403 CD1 LEU A 486 -3.738 243.641 798.872 1.00 69.97 C ANISOU 3403 CD1 LEU A 486 8323 9973 8289 -92 71 1420 C ATOM 3404 CD2 LEU A 486 -1.363 244.116 798.249 1.00 73.91 C ANISOU 3404 CD2 LEU A 486 9110 10633 8338 -209 -105 1574 C ATOM 3405 N ASN A 487 -1.149 241.115 802.039 1.00 63.20 N ANISOU 3405 N ASN A 487 7469 9425 7121 -372 -29 656 N ATOM 3406 CA ASN A 487 -0.010 240.292 802.419 1.00 53.56 C ANISOU 3406 CA ASN A 487 6304 8266 5782 -498 -76 590 C ATOM 3407 C ASN A 487 1.176 240.477 801.492 1.00 60.56 C ANISOU 3407 C ASN A 487 7356 9217 6436 -539 -166 757 C ATOM 3408 O ASN A 487 1.020 240.526 800.274 1.00 65.70 O ANISOU 3408 O ASN A 487 8018 9920 7026 -497 -268 972 O ATOM 3409 CB ASN A 487 -0.397 238.819 802.416 1.00 57.15 C ANISOU 3409 CB ASN A 487 6609 8829 6275 -567 -111 547 C ATOM 3410 CG ASN A 487 -1.350 238.470 803.522 1.00 58.14 C ANISOU 3410 CG ASN A 487 6634 8901 6556 -558 -82 350 C ATOM 3411 OD1 ASN A 487 -1.761 239.331 804.294 1.00 48.82 O ANISOU 3411 OD1 ASN A 487 5530 7569 5450 -488 -59 261 O ATOM 3412 ND2 ASN A 487 -1.718 237.200 803.604 1.00 61.99 N ANISOU 3412 ND2 ASN A 487 7101 9459 6994 -596 -71 297 N ATOM 3413 N THR A 488 2.364 240.578 802.078 1.00 53.78 N ANISOU 3413 N THR A 488 6647 8344 5444 -614 -167 674 N ATOM 3414 CA THR A 488 3.588 240.494 801.310 1.00 48.32 C ANISOU 3414 CA THR A 488 6134 7739 4488 -673 -295 792 C ATOM 3415 C THR A 488 3.748 239.028 800.934 1.00 54.90 C ANISOU 3415 C THR A 488 6901 8672 5287 -760 -444 813 C ATOM 3416 O THR A 488 3.017 238.179 801.439 1.00 50.40 O ANISOU 3416 O THR A 488 6164 8106 4880 -786 -392 718 O ATOM 3417 CB THR A 488 4.796 240.936 802.134 1.00 55.47 C ANISOU 3417 CB THR A 488 7228 8600 5250 -721 -245 674 C ATOM 3418 OG1 THR A 488 5.252 239.845 802.942 1.00 62.52 O ANISOU 3418 OG1 THR A 488 8119 9473 6163 -824 -266 539 O ATOM 3419 CG2 THR A 488 4.426 242.105 803.024 1.00 43.64 C ANISOU 3419 CG2 THR A 488 5722 6985 3875 -637 -85 579 C ATOM 3420 N THR A 489 4.701 238.727 800.060 1.00 64.01 N ANISOU 3420 N THR A 489 8186 9923 6214 -809 -645 934 N ATOM 3421 CA THR A 489 4.893 237.354 799.598 1.00 67.18 C ANISOU 3421 CA THR A 489 8509 10433 6583 -886 -851 960 C ATOM 3422 CB THR A 489 6.056 237.248 798.587 1.00 77.56 C ANISOU 3422 CB THR A 489 9992 11851 7626 -929 -1132 1097 C ATOM 3423 OG1 THR A 489 5.583 237.560 797.271 1.00 77.16 O ANISOU 3423 OG1 THR A 489 9887 11839 7591 -819 -1323 1344 O ATOM 3424 CG2 THR A 489 6.621 235.849 798.580 1.00 72.72 C ANISOU 3424 CG2 THR A 489 9332 11333 6964 -1054 -1331 1027 C ATOM 3425 C THR A 489 5.102 236.361 800.751 1.00 67.19 C ANISOU 3425 C THR A 489 8471 10418 6640 -1012 -764 761 C ATOM 3426 O THR A 489 4.504 235.284 800.760 1.00 63.18 O ANISOU 3426 O THR A 489 7784 9980 6243 -1053 -801 733 O ATOM 3427 N VAL A 490 5.935 236.727 801.723 1.00 75.48 N ANISOU 3427 N VAL A 490 9688 11375 7615 -1070 -657 634 N ATOM 3428 CA VAL A 490 6.243 235.826 802.833 1.00 72.37 C ANISOU 3428 CA VAL A 490 9302 10933 7262 -1198 -600 487 C ATOM 3429 CB VAL A 490 7.329 236.391 803.742 1.00 73.13 C ANISOU 3429 CB VAL A 490 9631 10907 7249 -1225 -538 382 C ATOM 3430 CG1 VAL A 490 8.041 235.255 804.448 1.00 67.20 C ANISOU 3430 CG1 VAL A 490 8967 10134 6432 -1387 -595 293 C ATOM 3431 CG2 VAL A 490 8.308 237.210 802.931 1.00 88.30 C ANISOU 3431 CG2 VAL A 490 11757 12885 8910 -1181 -644 453 C ATOM 3432 C VAL A 490 5.022 235.536 803.690 1.00 63.78 C ANISOU 3432 C VAL A 490 8012 9790 6430 -1188 -420 406 C ATOM 3433 O VAL A 490 4.938 234.493 804.336 1.00 60.70 O ANISOU 3433 O VAL A 490 7568 9417 6080 -1310 -395 340 O ATOM 3434 N GLU A 491 4.077 236.465 803.688 1.00 61.82 N ANISOU 3434 N GLU A 491 7664 9487 6336 -1053 -310 414 N ATOM 3435 CA GLU A 491 2.868 236.320 804.480 1.00 57.52 C ANISOU 3435 CA GLU A 491 6936 8896 6023 -1031 -180 321 C ATOM 3436 CB GLU A 491 2.260 237.695 804.751 1.00 52.41 C ANISOU 3436 CB GLU A 491 6279 8130 5506 -883 -109 292 C ATOM 3437 CG GLU A 491 3.145 238.561 805.627 1.00 54.96 C ANISOU 3437 CG GLU A 491 6784 8313 5786 -870 -71 227 C ATOM 3438 CD GLU A 491 2.614 239.960 805.797 1.00 58.92 C ANISOU 3438 CD GLU A 491 7283 8725 6377 -728 -15 217 C ATOM 3439 OE1 GLU A 491 2.444 240.389 806.958 1.00 66.77 O ANISOU 3439 OE1 GLU A 491 8293 9595 7481 -702 29 121 O ATOM 3440 OE2 GLU A 491 2.354 240.629 804.776 1.00 66.02 O ANISOU 3440 OE2 GLU A 491 8178 9681 7226 -650 -23 325 O ATOM 3441 C GLU A 491 1.851 235.391 803.832 1.00 58.15 C ANISOU 3441 C GLU A 491 6808 9132 6155 -1033 -189 364 C ATOM 3442 O GLU A 491 1.119 234.688 804.524 1.00 44.38 O ANISOU 3442 O GLU A 491 4926 7419 4519 -1093 -105 270 O ATOM 3443 N ASN A 492 1.805 235.392 802.504 1.00 63.82 N ANISOU 3443 N ASN A 492 7511 9951 6786 -960 -317 512 N ATOM 3444 CA ASN A 492 0.953 234.460 801.780 1.00 60.55 C ANISOU 3444 CA ASN A 492 6912 9682 6414 -926 -393 553 C ATOM 3445 CB ASN A 492 0.946 234.772 800.289 1.00 62.96 C ANISOU 3445 CB ASN A 492 7177 10015 6729 -798 -647 739 C ATOM 3446 CG ASN A 492 0.252 236.067 799.973 1.00 67.33 C ANISOU 3446 CG ASN A 492 7760 10461 7361 -645 -566 838 C ATOM 3447 OD1 ASN A 492 -0.664 236.479 800.682 1.00 76.16 O ANISOU 3447 OD1 ASN A 492 8828 11524 8586 -604 -349 739 O ATOM 3448 ND2 ASN A 492 0.676 236.717 798.898 1.00 67.53 N ANISOU 3448 ND2 ASN A 492 7872 10459 7328 -569 -752 1043 N ATOM 3449 C ASN A 492 1.438 233.038 801.989 1.00 59.60 C ANISOU 3449 C ASN A 492 6746 9676 6225 -1083 -481 486 C ATOM 3450 O ASN A 492 0.648 232.120 802.200 1.00 63.44 O ANISOU 3450 O ASN A 492 7062 10250 6791 -1106 -427 392 O ATOM 3451 N TRP A 493 2.751 232.861 801.919 1.00 56.99 N ANISOU 3451 N TRP A 493 6572 9339 5743 -1192 -626 514 N ATOM 3452 CA TRP A 493 3.335 231.555 802.152 1.00 58.79 C ANISOU 3452 CA TRP A 493 6772 9662 5905 -1369 -736 449 C ATOM 3453 CB TRP A 493 4.853 231.610 802.009 1.00 58.92 C ANISOU 3453 CB TRP A 493 7015 9645 5725 -1468 -915 478 C ATOM 3454 CG TRP A 493 5.276 231.892 800.608 1.00 72.54 C ANISOU 3454 CG TRP A 493 8737 11442 7384 -1383 -1204 615 C ATOM 3455 CD1 TRP A 493 4.509 231.783 799.482 1.00 80.55 C ANISOU 3455 CD1 TRP A 493 9515 12539 8552 -1254 -1374 718 C ATOM 3456 NE1 TRP A 493 5.248 232.118 798.375 1.00 78.31 N ANISOU 3456 NE1 TRP A 493 9315 12293 8148 -1208 -1660 866 N ATOM 3457 CE2 TRP A 493 6.516 232.438 798.768 1.00 79.81 C ANISOU 3457 CE2 TRP A 493 9807 12446 8071 -1314 -1663 834 C ATOM 3458 CZ2 TRP A 493 7.621 232.831 798.016 1.00 79.49 C ANISOU 3458 CZ2 TRP A 493 9971 12446 7787 -1325 -1897 931 C ATOM 3459 CH2 TRP A 493 8.782 233.092 798.687 1.00 82.06 C ANISOU 3459 CH2 TRP A 493 10581 12720 7877 -1432 -1836 829 C ATOM 3460 CZ3 TRP A 493 8.866 232.966 800.079 1.00 81.52 C ANISOU 3460 CZ3 TRP A 493 10587 12535 7853 -1517 -1571 655 C ATOM 3461 CE3 TRP A 493 7.777 232.575 800.829 1.00 77.03 C ANISOU 3461 CE3 TRP A 493 9823 11921 7525 -1514 -1353 591 C ATOM 3462 CD2 TRP A 493 6.577 232.303 800.176 1.00 77.01 C ANISOU 3462 CD2 TRP A 493 9541 11998 7720 -1418 -1384 669 C ATOM 3463 C TRP A 493 2.926 231.044 803.521 1.00 60.18 C ANISOU 3463 C TRP A 493 6947 9811 6108 -1484 -487 326 C ATOM 3464 O TRP A 493 2.517 229.898 803.668 1.00 66.91 O ANISOU 3464 O TRP A 493 7654 10786 6984 -1581 -491 258 O ATOM 3465 N PHE A 494 3.024 231.884 804.521 1.00 52.19 N ANISOU 3465 N PHE A 494 6061 8630 5140 -1478 -305 288 N ATOM 3466 CA PHE A 494 2.643 231.462 805.841 1.00 56.76 C ANISOU 3466 CA PHE A 494 6617 9155 5792 -1593 -130 195 C ATOM 3467 CB PHE A 494 2.957 232.596 806.775 1.00 58.20 C ANISOU 3467 CB PHE A 494 6927 9098 6089 -1541 -85 142 C ATOM 3468 CG PHE A 494 2.607 232.328 808.161 1.00 53.94 C ANISOU 3468 CG PHE A 494 6460 8434 5598 -1565 -23 41 C ATOM 3469 CD1 PHE A 494 3.464 231.671 808.979 1.00 61.48 C ANISOU 3469 CD1 PHE A 494 7557 9333 6471 -1763 -23 38 C ATOM 3470 CE1 PHE A 494 3.133 231.439 810.251 1.00 61.22 C ANISOU 3470 CE1 PHE A 494 7615 9187 6458 -1777 20 -30 C ATOM 3471 CZ PHE A 494 1.950 231.849 810.717 1.00 53.93 C ANISOU 3471 CZ PHE A 494 6633 8219 5638 -1607 60 -96 C ATOM 3472 CE2 PHE A 494 1.102 232.499 809.921 1.00 53.98 C ANISOU 3472 CE2 PHE A 494 6515 8268 5727 -1420 58 -103 C ATOM 3473 CD2 PHE A 494 1.426 232.742 808.658 1.00 48.34 C ANISOU 3473 CD2 PHE A 494 5721 7654 4993 -1392 19 -36 C ATOM 3474 C PHE A 494 1.166 231.147 805.967 1.00 60.00 C ANISOU 3474 C PHE A 494 6900 9634 6262 -1472 -47 108 C ATOM 3475 O PHE A 494 0.776 230.130 806.483 1.00 62.15 O ANISOU 3475 O PHE A 494 7156 9993 6465 -1562 -12 27 O ATOM 3476 N TYR A 495 0.341 232.039 805.470 1.00 57.32 N ANISOU 3476 N TYR A 495 6511 9246 6020 -1264 -42 108 N ATOM 3477 CA TYR A 495 -1.094 231.882 805.524 1.00 56.91 C ANISOU 3477 CA TYR A 495 6403 9217 6005 -1131 1 -3 C ATOM 3478 CB TYR A 495 -1.795 233.194 805.291 1.00 46.95 C ANISOU 3478 CB TYR A 495 5165 7804 4869 -932 -2 5 C ATOM 3479 CG TYR A 495 -1.783 234.080 806.487 1.00 48.83 C ANISOU 3479 CG TYR A 495 5526 7809 5217 -898 19 -55 C ATOM 3480 CD1 TYR A 495 -2.439 233.731 807.624 1.00 46.63 C ANISOU 3480 CD1 TYR A 495 5292 7461 4964 -924 62 -168 C ATOM 3481 CE1 TYR A 495 -2.428 234.530 808.700 1.00 32.69 C ANISOU 3481 CE1 TYR A 495 3624 5509 3288 -888 75 -189 C ATOM 3482 CZ TYR A 495 -1.759 235.688 808.659 1.00 43.76 C ANISOU 3482 CZ TYR A 495 5077 6795 4754 -825 53 -131 C ATOM 3483 OH TYR A 495 -1.745 236.508 809.734 1.00 53.43 O ANISOU 3483 OH TYR A 495 6383 7859 6058 -783 67 -155 O ATOM 3484 CE2 TYR A 495 -1.101 236.056 807.558 1.00 43.13 C ANISOU 3484 CE2 TYR A 495 4956 6786 4646 -816 18 -46 C ATOM 3485 CD2 TYR A 495 -1.116 235.264 806.476 1.00 47.27 C ANISOU 3485 CD2 TYR A 495 5386 7491 5084 -852 -3 7 C ATOM 3486 C TYR A 495 -1.699 230.778 804.697 1.00 71.52 C ANISOU 3486 C TYR A 495 8107 11329 7740 -1148 10 -31 C ATOM 3487 O TYR A 495 -2.669 230.177 805.108 1.00 74.32 O ANISOU 3487 O TYR A 495 8398 11715 8125 -1146 65 -196 O ATOM 3488 N ASN A 496 -1.138 230.501 803.535 1.00 70.39 N ANISOU 3488 N ASN A 496 7772 11243 7730 -1167 -137 86 N ATOM 3489 CA ASN A 496 -1.712 229.456 802.744 1.00 74.74 C ANISOU 3489 CA ASN A 496 7982 11878 8539 -1162 -220 17 C ATOM 3490 CB ASN A 496 -2.241 229.999 801.449 1.00 63.39 C ANISOU 3490 CB ASN A 496 6334 10373 7377 -963 -335 96 C ATOM 3491 CG ASN A 496 -2.702 231.382 801.572 1.00 62.88 C ANISOU 3491 CG ASN A 496 6454 10162 7275 -810 -238 149 C ATOM 3492 OD1 ASN A 496 -3.881 231.657 801.466 1.00 65.49 O ANISOU 3492 OD1 ASN A 496 6702 10397 7783 -674 -130 63 O ATOM 3493 ND2 ASN A 496 -1.778 232.283 801.792 1.00 58.70 N ANISOU 3493 ND2 ASN A 496 6170 9605 6528 -843 -273 279 N ATOM 3494 C ASN A 496 -0.653 228.473 802.432 1.00 93.07 C ANISOU 3494 C ASN A 496 10204 14312 10846 -1347 -410 56 C ATOM 3495 O ASN A 496 -0.237 228.310 801.312 1.00 98.92 O ANISOU 3495 O ASN A 496 10769 15089 11729 -1316 -654 140 O ATOM 3496 N MSE A 497 -0.230 227.803 803.476 1.00102.21 N ANISOU 3496 N MSE A 497 11493 15518 11824 -1546 -321 -8 N ATOM 3497 CA MSE A 497 0.784 226.794 803.387 1.00110.82 C ANISOU 3497 CA MSE A 497 12526 16697 12885 -1769 -494 4 C ATOM 3498 CB MSE A 497 1.309 226.459 804.774 1.00113.38 C ANISOU 3498 CB MSE A 497 13112 16994 12972 -1976 -365 -30 C ATOM 3499 CG MSE A 497 2.324 227.437 805.288 1.00110.51 C ANISOU 3499 CG MSE A 497 13091 16471 12426 -1978 -360 67 C ATOM 3500 SE MSE A 497 4.085 226.870 804.947 1.00 96.32 Se ANISOU 3500 SE MSE A 497 11414 14653 10532 -2187 -674 106 Se ATOM 3501 CE MSE A 497 3.998 225.292 805.935 1.00 93.60 C ANISOU 3501 CE MSE A 497 11000 14398 10167 -2498 -611 7 C ATOM 3502 C MSE A 497 0.205 225.567 802.763 1.00113.27 C ANISOU 3502 C MSE A 497 12428 17151 13457 -1822 -540 -87 C ATOM 3503 O MSE A 497 0.912 224.725 802.244 1.00122.99 O ANISOU 3503 O MSE A 497 13492 18477 14763 -1968 -750 -75 O ATOM 3504 N HIS A 498 -1.105 225.451 802.775 1.00109.03 N ANISOU 3504 N HIS A 498 11713 16635 13080 -1702 -349 -198 N ATOM 3505 CA HIS A 498 -1.730 224.276 802.206 1.00107.64 C ANISOU 3505 CA HIS A 498 11111 16604 13184 -1745 -342 -312 C ATOM 3506 CB HIS A 498 -2.975 223.984 802.992 1.00105.05 C ANISOU 3506 CB HIS A 498 10757 16307 12851 -1737 -44 -483 C ATOM 3507 CG HIS A 498 -2.757 224.083 804.461 1.00110.30 C ANISOU 3507 CG HIS A 498 11791 16942 13175 -1891 96 -495 C ATOM 3508 ND1 HIS A 498 -1.836 223.302 805.122 1.00110.26 N ANISOU 3508 ND1 HIS A 498 11876 17006 13013 -2172 54 -458 N ATOM 3509 CE1 HIS A 498 -1.840 223.608 806.403 1.00111.87 C ANISOU 3509 CE1 HIS A 498 12418 17142 12945 -2241 171 -468 C ATOM 3510 NE2 HIS A 498 -2.722 224.572 806.598 1.00117.42 N ANISOU 3510 NE2 HIS A 498 13250 17748 13618 -2015 262 -523 N ATOM 3511 CD2 HIS A 498 -3.301 224.894 805.396 1.00117.99 C ANISOU 3511 CD2 HIS A 498 13070 17809 13953 -1803 231 -537 C ATOM 3512 C HIS A 498 -2.010 224.337 800.721 1.00104.82 C ANISOU 3512 C HIS A 498 10408 16253 13166 -1550 -534 -277 C ATOM 3513 O HIS A 498 -1.950 223.334 800.041 1.00 94.30 O ANISOU 3513 O HIS A 498 8710 15056 12065 -1615 -658 -323 O ATOM 3514 N SER A 499 -2.308 225.516 800.214 1.00112.72 N ANISOU 3514 N SER A 499 11513 17105 14212 -1314 -573 -188 N ATOM 3515 CA SER A 499 -2.599 225.656 798.804 1.00118.41 C ANISOU 3515 CA SER A 499 11926 17798 15266 -1111 -783 -126 C ATOM 3516 CB SER A 499 -2.922 227.092 798.473 1.00121.82 C ANISOU 3516 CB SER A 499 12551 18039 15696 -889 -789 -6 C ATOM 3517 OG SER A 499 -1.831 227.629 797.747 1.00123.88 O ANISOU 3517 OG SER A 499 12923 18282 15863 -873 -1108 206 O ATOM 3518 C SER A 499 -1.409 225.334 797.955 1.00119.80 C ANISOU 3518 C SER A 499 12014 18051 15453 -1181 -1159 13 C ATOM 3519 O SER A 499 -0.299 225.687 798.290 1.00111.60 O ANISOU 3519 O SER A 499 11286 17000 14116 -1304 -1280 117 O ATOM 3520 N GLU A 500 -1.651 224.689 796.826 1.00132.02 N ANISOU 3520 N GLU A 500 13141 19672 17349 -1085 -1362 3 N ATOM 3521 CA GLU A 500 -0.577 224.391 795.913 1.00134.99 C ANISOU 3521 CA GLU A 500 13421 20125 17743 -1127 -1777 137 C ATOM 3522 CB GLU A 500 -1.006 223.462 794.776 1.00136.55 C ANISOU 3522 CB GLU A 500 13071 20429 18384 -1021 -1975 83 C ATOM 3523 CG GLU A 500 -1.267 222.029 795.211 1.00150.42 C ANISOU 3523 CG GLU A 500 14492 22379 20283 -1225 -1812 -131 C ATOM 3524 CD GLU A 500 -1.758 221.156 794.071 1.00169.48 C ANISOU 3524 CD GLU A 500 16314 24904 23175 -1092 -1987 -207 C ATOM 3525 OE1 GLU A 500 -2.077 221.705 792.996 1.00174.31 O ANISOU 3525 OE1 GLU A 500 16786 25409 24035 -805 -2207 -103 O ATOM 3526 OE2 GLU A 500 -1.829 219.922 794.251 1.00175.08 O ANISOU 3526 OE2 GLU A 500 16688 25808 24026 -1274 -1908 -368 O ATOM 3527 C GLU A 500 -0.187 225.762 795.422 1.00137.18 C ANISOU 3527 C GLU A 500 14004 20252 17866 -960 -1953 354 C ATOM 3528 O GLU A 500 -0.555 226.756 796.047 1.00130.93 O ANISOU 3528 O GLU A 500 13503 19328 16918 -897 -1720 373 O ATOM 3529 N GLU A 505 8.995 227.486 794.421 1.00 71.65 N ANISOU 3529 N GLU A 505 7392 9019 10813 390 -4279 2692 N ATOM 3530 CA GLU A 505 9.925 226.521 794.985 1.00 84.38 C ANISOU 3530 CA GLU A 505 9027 10768 12265 279 -4359 2525 C ATOM 3531 CB GLU A 505 11.301 226.647 794.354 1.00 93.44 C ANISOU 3531 CB GLU A 505 10449 11980 13074 195 -4800 2693 C ATOM 3532 CG GLU A 505 11.575 225.667 793.230 1.00109.66 C ANISOU 3532 CG GLU A 505 12141 13911 15615 232 -5350 2783 C ATOM 3533 CD GLU A 505 12.504 224.537 793.618 1.00114.44 C ANISOU 3533 CD GLU A 505 12673 14610 16198 116 -5536 2593 C ATOM 3534 OE1 GLU A 505 13.628 224.823 794.062 1.00116.81 O ANISOU 3534 OE1 GLU A 505 13393 15066 15924 -1 -5580 2562 O ATOM 3535 OE2 GLU A 505 12.123 223.365 793.447 1.00106.85 O ANISOU 3535 OE2 GLU A 505 11204 13560 15834 135 -5638 2457 O ATOM 3536 C GLU A 505 10.071 226.779 796.440 1.00 86.08 C ANISOU 3536 C GLU A 505 9540 11156 12011 186 -3914 2330 C ATOM 3537 O GLU A 505 9.526 226.083 797.268 1.00 89.11 O ANISOU 3537 O GLU A 505 9726 11577 12555 175 -3651 2120 O ATOM 3538 N LEU A 506 10.826 227.803 796.762 1.00 89.45 N ANISOU 3538 N LEU A 506 10424 11695 11869 115 -3826 2394 N ATOM 3539 CA LEU A 506 11.010 228.135 798.143 1.00 84.09 C ANISOU 3539 CA LEU A 506 10012 11146 10791 41 -3418 2206 C ATOM 3540 CB LEU A 506 11.218 229.626 798.284 1.00 75.00 C ANISOU 3540 CB LEU A 506 9202 10066 9230 28 -3221 2284 C ATOM 3541 CG LEU A 506 12.108 230.018 799.443 1.00 76.15 C ANISOU 3541 CG LEU A 506 9669 10346 8917 -54 -2977 2106 C ATOM 3542 CD1 LEU A 506 12.272 231.500 799.502 1.00 71.65 C ANISOU 3542 CD1 LEU A 506 9334 9853 8035 -49 -2788 2166 C ATOM 3543 CD2 LEU A 506 11.505 229.503 800.689 1.00 71.87 C ANISOU 3543 CD2 LEU A 506 9049 9806 8451 -66 -2652 1901 C ATOM 3544 C LEU A 506 9.750 227.731 798.854 1.00 85.08 C ANISOU 3544 C LEU A 506 9888 11243 11196 93 -3091 2060 C ATOM 3545 O LEU A 506 9.748 226.916 799.750 1.00 89.47 O ANISOU 3545 O LEU A 506 10373 11864 11758 36 -2953 1888 O ATOM 3546 N PHE A 507 8.644 228.285 798.433 1.00 80.05 N ANISOU 3546 N PHE A 507 9102 10511 10803 197 -2985 2130 N ATOM 3547 CA PHE A 507 7.406 227.951 799.115 1.00 74.99 C ANISOU 3547 CA PHE A 507 8225 9866 10402 255 -2671 1960 C ATOM 3548 C PHE A 507 7.380 226.476 799.519 1.00 71.52 C ANISOU 3548 C PHE A 507 7495 9453 10228 182 -2628 1757 C ATOM 3549 O PHE A 507 7.022 226.142 800.645 1.00 64.94 O ANISOU 3549 O PHE A 507 6711 8696 9265 92 -2271 1571 O ATOM 3550 CB PHE A 507 6.199 228.302 798.242 1.00 72.59 C ANISOU 3550 CB PHE A 507 7628 9387 10567 405 -2683 2024 C ATOM 3551 CG PHE A 507 4.888 227.906 798.846 1.00 68.52 C ANISOU 3551 CG PHE A 507 6871 8833 10329 416 -2277 1754 C ATOM 3552 CD1 PHE A 507 4.460 228.476 800.028 1.00 61.43 C ANISOU 3552 CD1 PHE A 507 6211 8057 9071 373 -1921 1638 C ATOM 3553 CE1 PHE A 507 3.257 228.114 800.588 1.00 63.59 C ANISOU 3553 CE1 PHE A 507 6313 8315 9535 352 -1542 1373 C ATOM 3554 CZ PHE A 507 2.465 227.170 799.964 1.00 67.15 C ANISOU 3554 CZ PHE A 507 6334 8627 10553 378 -1467 1192 C ATOM 3555 CE2 PHE A 507 2.883 226.595 798.783 1.00 64.51 C ANISOU 3555 CE2 PHE A 507 5719 8149 10641 437 -1807 1297 C ATOM 3556 CD2 PHE A 507 4.086 226.962 798.232 1.00 62.55 C ANISOU 3556 CD2 PHE A 507 5661 7917 10189 453 -2232 1590 C ATOM 3557 N LYS A 508 7.773 225.597 798.601 1.00 70.24 N ANISOU 3557 N LYS A 508 7052 9198 10440 176 -2948 1785 N ATOM 3558 CA LYS A 508 7.803 224.165 798.884 1.00 71.23 C ANISOU 3558 CA LYS A 508 6882 9306 10876 51 -2858 1577 C ATOM 3559 C LYS A 508 8.804 223.847 799.998 1.00 74.91 C ANISOU 3559 C LYS A 508 7647 9918 10898 -109 -2805 1512 C ATOM 3560 O LYS A 508 8.502 223.096 800.926 1.00 76.40 O ANISOU 3560 O LYS A 508 7770 10141 11118 -238 -2479 1335 O ATOM 3561 CB LYS A 508 8.148 223.372 797.618 1.00 76.47 C ANISOU 3561 CB LYS A 508 7176 9833 12048 82 -3284 1638 C ATOM 3562 CG LYS A 508 7.228 223.646 796.435 1.00 74.52 C ANISOU 3562 CG LYS A 508 6605 9388 12321 258 -3404 1721 C ATOM 3563 CD LYS A 508 7.836 223.114 795.135 1.00 84.29 C ANISOU 3563 CD LYS A 508 7570 10493 13961 307 -3967 1869 C ATOM 3564 CE LYS A 508 7.173 223.730 793.902 1.00 88.23 C ANISOU 3564 CE LYS A 508 7882 10777 14863 502 -4210 2067 C ATOM 3565 NZ LYS A 508 7.936 223.477 792.642 1.00 83.72 N ANISOU 3565 NZ LYS A 508 7171 10098 14539 554 -4861 2307 N ATOM 3566 N TYR A 509 9.993 224.429 799.895 1.00 76.86 N ANISOU 3566 N TYR A 509 8230 10242 10732 -106 -3123 1656 N ATOM 3567 CA TYR A 509 11.017 224.305 800.929 1.00 69.26 C ANISOU 3567 CA TYR A 509 7586 9387 9342 -230 -3102 1584 C ATOM 3568 C TYR A 509 10.462 224.677 802.304 1.00 61.89 C ANISOU 3568 C TYR A 509 6856 8523 8136 -264 -2645 1487 C ATOM 3569 O TYR A 509 10.575 223.907 803.257 1.00 63.67 O ANISOU 3569 O TYR A 509 7088 8754 8349 -404 -2457 1358 O ATOM 3570 CB TYR A 509 12.212 225.195 800.574 1.00 68.37 C ANISOU 3570 CB TYR A 509 7878 9302 8797 -219 -3340 1698 C ATOM 3571 CG TYR A 509 13.289 225.298 801.636 1.00 53.48 C ANISOU 3571 CG TYR A 509 6356 7475 6487 -322 -3250 1579 C ATOM 3572 CD1 TYR A 509 13.242 226.286 802.604 1.00 55.99 C ANISOU 3572 CD1 TYR A 509 6984 7827 6461 -310 -2882 1525 C ATOM 3573 CE1 TYR A 509 14.230 226.393 803.563 1.00 72.92 C ANISOU 3573 CE1 TYR A 509 9412 9985 8309 -376 -2811 1399 C ATOM 3574 CZ TYR A 509 15.288 225.507 803.560 1.00 72.79 C ANISOU 3574 CZ TYR A 509 9414 9954 8288 -467 -3119 1327 C ATOM 3575 OH TYR A 509 16.276 225.611 804.516 1.00 72.91 O ANISOU 3575 OH TYR A 509 9706 9955 8042 -516 -3073 1188 O ATOM 3576 CE2 TYR A 509 15.360 224.521 802.600 1.00 65.55 C ANISOU 3576 CE2 TYR A 509 8202 9021 7683 -504 -3497 1374 C ATOM 3577 CD2 TYR A 509 14.366 224.425 801.646 1.00 62.80 C ANISOU 3577 CD2 TYR A 509 7534 8654 7672 -427 -3557 1500 C ATOM 3578 N LEU A 510 9.860 225.861 802.400 1.00 53.14 N ANISOU 3578 N LEU A 510 5914 7452 6826 -148 -2481 1563 N ATOM 3579 CA LEU A 510 9.254 226.305 803.648 1.00 63.01 C ANISOU 3579 CA LEU A 510 7341 8768 7833 -165 -2098 1481 C ATOM 3580 C LEU A 510 8.134 225.371 804.082 1.00 69.96 C ANISOU 3580 C LEU A 510 7944 9613 9023 -249 -1768 1322 C ATOM 3581 O LEU A 510 7.864 225.212 805.274 1.00 64.39 O ANISOU 3581 O LEU A 510 7375 8966 8126 -340 -1490 1237 O ATOM 3582 CB LEU A 510 8.705 227.724 803.506 1.00 66.03 C ANISOU 3582 CB LEU A 510 7887 9121 8081 -76 -1902 1531 C ATOM 3583 CG LEU A 510 9.745 228.828 803.341 1.00 65.30 C ANISOU 3583 CG LEU A 510 8098 9019 7693 -92 -1931 1568 C ATOM 3584 CD1 LEU A 510 9.052 230.166 803.182 1.00 56.83 C ANISOU 3584 CD1 LEU A 510 7076 7938 6577 -24 -1744 1608 C ATOM 3585 CD2 LEU A 510 10.692 228.837 804.526 1.00 56.84 C ANISOU 3585 CD2 LEU A 510 7275 7982 6340 -174 -1811 1432 C ATOM 3586 N ARG A 511 7.479 224.758 803.103 1.00 75.27 N ANISOU 3586 N ARG A 511 8229 10189 10180 -220 -1799 1280 N ATOM 3587 CA ARG A 511 6.353 223.882 803.381 1.00 79.99 C ANISOU 3587 CA ARG A 511 8530 10768 11094 -297 -1444 1093 C ATOM 3588 C ARG A 511 6.832 222.591 804.039 1.00 78.00 C ANISOU 3588 C ARG A 511 8203 10541 10891 -503 -1355 1002 C ATOM 3589 O ARG A 511 6.217 222.104 804.992 1.00 77.74 O ANISOU 3589 O ARG A 511 8181 10574 10783 -631 -989 891 O ATOM 3590 CB ARG A 511 5.565 223.598 802.097 1.00 85.54 C ANISOU 3590 CB ARG A 511 8800 11337 12365 -189 -1505 1046 C ATOM 3591 CG ARG A 511 4.200 222.960 802.327 1.00 89.73 C ANISOU 3591 CG ARG A 511 9033 11861 13201 -231 -1074 804 C ATOM 3592 CD ARG A 511 3.273 223.186 801.139 1.00 88.59 C ANISOU 3592 CD ARG A 511 8541 11554 13565 -58 -1116 749 C ATOM 3593 NE ARG A 511 3.936 222.908 799.873 1.00 93.57 N ANISOU 3593 NE ARG A 511 8930 12040 14584 25 -1562 887 N ATOM 3594 CZ ARG A 511 3.927 221.724 799.274 1.00 95.58 C ANISOU 3594 CZ ARG A 511 8745 12208 15364 -14 -1616 776 C ATOM 3595 NH1 ARG A 511 3.279 220.707 799.826 1.00 97.72 N ANISOU 3595 NH1 ARG A 511 8770 12536 15824 -147 -1200 519 N ATOM 3596 NH2 ARG A 511 4.564 221.556 798.121 1.00 90.22 N ANISOU 3596 NH2 ARG A 511 7866 11393 15020 70 -2089 927 N ATOM 3597 N THR A 512 7.939 222.049 803.541 1.00 71.13 N ANISOU 3597 N THR A 512 7274 9619 10134 -550 -1700 1060 N ATOM 3598 CA THR A 512 8.477 220.813 804.087 1.00 73.55 C ANISOU 3598 CA THR A 512 7486 9914 10547 -761 -1655 985 C ATOM 3599 C THR A 512 9.038 221.048 805.485 1.00 75.80 C ANISOU 3599 C THR A 512 8190 10263 10349 -867 -1539 1015 C ATOM 3600 O THR A 512 8.897 220.199 806.363 1.00 85.78 O ANISOU 3600 O THR A 512 9431 11533 11628 -1056 -1289 958 O ATOM 3601 CB THR A 512 9.564 220.205 803.178 1.00 79.84 C ANISOU 3601 CB THR A 512 8110 10624 11603 -788 -2108 1022 C ATOM 3602 OG1 THR A 512 10.813 220.866 803.408 1.00 88.86 O ANISOU 3602 OG1 THR A 512 9652 11796 12314 -766 -2418 1118 O ATOM 3603 CG2 THR A 512 9.175 220.334 801.710 1.00 75.36 C ANISOU 3603 CG2 THR A 512 7212 9974 11448 -625 -2354 1063 C ATOM 3604 N LEU A 513 9.663 222.205 805.691 1.00 51.68 N ANISOU 3604 N LEU A 513 5506 7247 6884 -747 -1713 1111 N ATOM 3605 CA LEU A 513 10.185 222.556 807.006 1.00 48.41 C ANISOU 3605 CA LEU A 513 5474 6866 6053 -806 -1623 1129 C ATOM 3606 C LEU A 513 9.071 222.621 808.044 1.00 54.27 C ANISOU 3606 C LEU A 513 6282 7670 6668 -858 -1209 1099 C ATOM 3607 O LEU A 513 9.186 222.045 809.120 1.00 51.75 O ANISOU 3607 O LEU A 513 6080 7341 6243 -1018 -1055 1096 O ATOM 3608 CB LEU A 513 10.922 223.892 806.971 1.00 56.29 C ANISOU 3608 CB LEU A 513 6811 7910 6667 -645 -1833 1207 C ATOM 3609 CG LEU A 513 12.152 223.994 806.077 1.00 56.09 C ANISOU 3609 CG LEU A 513 6832 7866 6613 -603 -2255 1240 C ATOM 3610 CD1 LEU A 513 12.982 225.191 806.489 1.00 52.68 C ANISOU 3610 CD1 LEU A 513 6795 7430 5792 -528 -2234 1233 C ATOM 3611 CD2 LEU A 513 12.971 222.729 806.176 1.00 70.64 C ANISOU 3611 CD2 LEU A 513 8562 9616 8661 -780 -2418 1159 C ATOM 3612 N ASN A 514 7.997 223.335 807.721 1.00 68.64 N ANISOU 3612 N ASN A 514 8039 9547 8493 -731 -1050 1084 N ATOM 3613 CA ASN A 514 6.869 223.462 808.636 1.00 65.54 C ANISOU 3613 CA ASN A 514 7717 9234 7951 -777 -684 1031 C ATOM 3614 C ASN A 514 6.193 222.116 808.860 1.00 72.10 C ANISOU 3614 C ASN A 514 8293 10082 9021 -975 -394 928 C ATOM 3615 O ASN A 514 5.519 221.910 809.871 1.00 71.05 O ANISOU 3615 O ASN A 514 8278 10030 8688 -1094 -99 904 O ATOM 3616 CB ASN A 514 5.851 224.473 808.116 1.00 61.05 C ANISOU 3616 CB ASN A 514 7098 8699 7398 -606 -599 999 C ATOM 3617 CG ASN A 514 4.830 224.862 809.166 1.00 66.78 C ANISOU 3617 CG ASN A 514 7982 9521 7870 -638 -292 941 C ATOM 3618 OD1 ASN A 514 3.715 224.341 809.189 1.00 66.11 O ANISOU 3618 OD1 ASN A 514 7715 9484 7920 -707 -9 804 O ATOM 3619 ND2 ASN A 514 5.212 225.777 810.050 1.00 75.94 N ANISOU 3619 ND2 ASN A 514 9476 10715 8661 -591 -352 1028 N ATOM 3620 N GLY A 515 6.375 221.209 807.905 1.00 61.08 N ANISOU 3620 N GLY A 515 6542 8617 8049 -1019 -483 873 N ATOM 3621 CA GLY A 515 5.885 219.850 808.039 1.00 71.44 C ANISOU 3621 CA GLY A 515 7562 9943 9639 -1227 -202 769 C ATOM 3622 C GLY A 515 6.575 219.127 809.179 1.00 77.84 C ANISOU 3622 C GLY A 515 8571 10744 10262 -1459 -148 855 C ATOM 3623 O GLY A 515 5.923 218.563 810.057 1.00 84.08 O ANISOU 3623 O GLY A 515 9401 11616 10931 -1641 203 840 O ATOM 3624 N PHE A 516 7.904 219.153 809.169 1.00 78.42 N ANISOU 3624 N PHE A 516 8784 10711 10301 -1460 -503 945 N ATOM 3625 CA PHE A 516 8.694 218.535 810.229 1.00 69.06 C ANISOU 3625 CA PHE A 516 7799 9456 8983 -1666 -513 1029 C ATOM 3626 C PHE A 516 8.589 219.306 811.543 1.00 62.70 C ANISOU 3626 C PHE A 516 7429 8691 7704 -1650 -412 1130 C ATOM 3627 O PHE A 516 8.331 218.727 812.596 1.00 70.50 O ANISOU 3627 O PHE A 516 8533 9686 8567 -1849 -186 1203 O ATOM 3628 CB PHE A 516 10.160 218.420 809.809 1.00 58.12 C ANISOU 3628 CB PHE A 516 6447 7932 7705 -1653 -948 1047 C ATOM 3629 CG PHE A 516 11.056 217.909 810.897 1.00 69.31 C ANISOU 3629 CG PHE A 516 8094 9227 9015 -1841 -1003 1119 C ATOM 3630 CD1 PHE A 516 11.127 216.554 811.173 1.00 80.11 C ANISOU 3630 CD1 PHE A 516 9253 10514 10669 -2120 -869 1128 C ATOM 3631 CE1 PHE A 516 11.946 216.084 812.176 1.00 77.25 C ANISOU 3631 CE1 PHE A 516 9104 9998 10249 -2302 -934 1214 C ATOM 3632 CZ PHE A 516 12.703 216.965 812.915 1.00 63.08 C ANISOU 3632 CZ PHE A 516 7720 8124 8125 -2184 -1136 1262 C ATOM 3633 CE2 PHE A 516 12.639 218.315 812.649 1.00 58.55 C ANISOU 3633 CE2 PHE A 516 7335 7652 7260 -1900 -1246 1229 C ATOM 3634 CD2 PHE A 516 11.819 218.780 811.648 1.00 64.64 C ANISOU 3634 CD2 PHE A 516 7906 8582 8073 -1742 -1177 1172 C ATOM 3635 N ALA A 517 8.794 220.616 811.469 1.00 44.83 N ANISOU 3635 N ALA A 517 5395 6452 5189 -1420 -589 1149 N ATOM 3636 CA ALA A 517 8.756 221.461 812.653 1.00 50.16 C ANISOU 3636 CA ALA A 517 6445 7149 5463 -1370 -544 1232 C ATOM 3637 C ALA A 517 7.423 221.336 813.376 1.00 67.12 C ANISOU 3637 C ALA A 517 8620 9423 7458 -1464 -179 1240 C ATOM 3638 O ALA A 517 7.357 221.431 814.603 1.00 71.85 O ANISOU 3638 O ALA A 517 9492 10022 7785 -1545 -106 1345 O ATOM 3639 CB ALA A 517 9.021 222.897 812.280 1.00 35.62 C ANISOU 3639 CB ALA A 517 4760 5338 3437 -1111 -737 1226 C ATOM 3640 N SER A 518 6.358 221.121 812.610 1.00 73.52 N ANISOU 3640 N SER A 518 9149 10336 8448 -1452 36 1120 N ATOM 3641 CA SER A 518 5.019 221.021 813.174 1.00 67.88 C ANISOU 3641 CA SER A 518 8451 9771 7570 -1538 397 1069 C ATOM 3642 C SER A 518 4.935 219.883 814.185 1.00 70.32 C ANISOU 3642 C SER A 518 8832 10102 7782 -1835 623 1160 C ATOM 3643 O SER A 518 4.097 219.905 815.088 1.00 74.83 O ANISOU 3643 O SER A 518 9585 10800 8049 -1938 858 1194 O ATOM 3644 CB SER A 518 3.982 220.816 812.068 1.00 20.00 C ATOM 3645 OG SER A 518 4.187 219.585 811.397 1.00 20.00 O ATOM 3646 N THR A 519 5.817 218.899 814.040 1.00 61.74 N ANISOU 3646 N THR A 519 7617 8893 6948 -1987 535 1214 N ATOM 3647 CA THR A 519 5.749 217.689 814.851 1.00 76.34 C ANISOU 3647 CA THR A 519 9477 10745 8785 -2305 772 1318 C ATOM 3648 C THR A 519 6.402 217.839 816.226 1.00 78.43 C ANISOU 3648 C THR A 519 10155 10903 8742 -2398 636 1549 C ATOM 3649 O THR A 519 6.386 216.912 817.033 1.00 82.52 O ANISOU 3649 O THR A 519 10745 11398 9209 -2677 805 1697 O ATOM 3650 CB THR A 519 6.407 216.503 814.121 1.00 89.69 C ANISOU 3650 CB THR A 519 10811 12321 10944 -2457 734 1276 C ATOM 3651 OG1 THR A 519 6.118 216.586 812.720 1.00 95.36 O ANISOU 3651 OG1 THR A 519 11151 13069 12013 -2291 694 1079 O ATOM 3652 CG2 THR A 519 5.891 215.175 814.671 1.00 92.71 C ANISOU 3652 CG2 THR A 519 11073 12772 11382 -2808 1130 1331 C ATOM 3653 N LEU A 520 6.971 219.006 816.495 1.00 79.18 N ANISOU 3653 N LEU A 520 10510 10922 8653 -2169 337 1587 N ATOM 3654 CA LEU A 520 7.705 219.215 817.739 1.00 79.72 C ANISOU 3654 CA LEU A 520 10936 10839 8514 -2212 157 1781 C ATOM 3655 C LEU A 520 6.866 219.936 818.793 1.00 81.26 C ANISOU 3655 C LEU A 520 11428 11149 8299 -2179 252 1884 C ATOM 3656 O LEU A 520 6.198 220.925 818.493 1.00 87.87 O ANISOU 3656 O LEU A 520 12234 12106 9045 -1961 238 1716 O ATOM 3657 CB LEU A 520 9.004 219.986 817.470 1.00 74.86 C ANISOU 3657 CB LEU A 520 10413 10049 7981 -1992 -235 1737 C ATOM 3658 CG LEU A 520 10.231 219.185 817.008 1.00 76.39 C ANISOU 3658 CG LEU A 520 10472 10048 8506 -2085 -443 1704 C ATOM 3659 CD2 LEU A 520 11.354 220.106 816.536 1.00 65.41 C ANISOU 3659 CD2 LEU A 520 9169 8561 7124 -1838 -797 1595 C ATOM 3660 CD1 LEU A 520 9.868 218.189 815.913 1.00 87.71 C ANISOU 3660 CD1 LEU A 520 11500 11554 10270 -2215 -292 1599 C ATOM 3661 N SER A 521 6.902 219.436 820.024 1.00 75.66 N ANISOU 3661 N SER A 521 10949 10368 7428 -2377 277 2089 N ATOM 3662 CA SER A 521 6.247 220.121 821.134 1.00 82.97 C ANISOU 3662 CA SER A 521 12092 11344 8091 -2305 205 2077 C ATOM 3663 C SER A 521 6.776 221.544 821.224 1.00 85.29 C ANISOU 3663 C SER A 521 12433 11520 8453 -1979 -117 1921 C ATOM 3664 O SER A 521 7.914 221.813 820.847 1.00 81.84 O ANISOU 3664 O SER A 521 11980 10923 8193 -1858 -324 1893 O ATOM 3665 CB SER A 521 6.532 219.396 822.446 1.00 90.36 C ANISOU 3665 CB SER A 521 13284 12149 8900 -2553 176 2367 C ATOM 3666 OG SER A 521 7.870 219.623 822.864 1.00 88.19 O ANISOU 3666 OG SER A 521 13143 11579 8786 -2471 -149 2468 O ATOM 3667 N ASN A 522 5.957 222.461 821.726 1.00 89.75 N ANISOU 3667 N ASN A 522 13047 12157 8897 -1858 -136 1815 N ATOM 3668 CA ASN A 522 6.402 223.841 821.872 1.00 89.07 C ANISOU 3668 CA ASN A 522 12963 11945 8935 -1587 -361 1671 C ATOM 3669 C ASN A 522 7.590 223.948 822.821 1.00 86.88 C ANISOU 3669 C ASN A 522 12885 11422 8706 -1569 -605 1797 C ATOM 3670 O ASN A 522 8.450 224.807 822.652 1.00 88.94 O ANISOU 3670 O ASN A 522 13121 11547 9124 -1367 -761 1675 O ATOM 3671 CB ASN A 522 5.262 224.749 822.339 1.00 90.64 C ANISOU 3671 CB ASN A 522 13176 12241 9022 -1504 -322 1579 C ATOM 3672 CG ASN A 522 4.093 224.756 821.378 1.00 94.38 C ANISOU 3672 CG ASN A 522 13463 12928 9468 -1495 -100 1430 C ATOM 3673 OD1 ASN A 522 3.271 223.838 821.377 1.00105.79 O ANISOU 3673 OD1 ASN A 522 14929 14544 10723 -1696 122 1479 O ATOM 3674 ND2 ASN A 522 4.007 225.797 820.557 1.00 81.84 N ANISOU 3674 ND2 ASN A 522 11700 11329 8068 -1272 -134 1251 N ATOM 3675 N ASP A 523 7.636 223.067 823.816 1.00 87.45 N ANISOU 3675 N ASP A 523 13162 11427 8637 -1790 -621 2054 N ATOM 3676 CA ASP A 523 8.746 223.040 824.762 1.00 84.86 C ANISOU 3676 CA ASP A 523 13042 10825 8377 -1789 -871 2218 C ATOM 3677 C ASP A 523 10.066 222.920 824.020 1.00 81.21 C ANISOU 3677 C ASP A 523 12521 10202 8134 -1708 -992 2150 C ATOM 3678 O ASP A 523 10.970 223.726 824.210 1.00 85.24 O ANISOU 3678 O ASP A 523 13086 10543 8759 -1508 -1193 2048 O ATOM 3679 CB ASP A 523 8.598 221.867 825.726 1.00 94.78 C ANISOU 3679 CB ASP A 523 14511 12016 9486 -2095 -840 2565 C ATOM 3680 CG ASP A 523 7.375 221.991 826.604 1.00108.79 C ANISOU 3680 CG ASP A 523 16416 13947 10973 -2193 -768 2668 C ATOM 3681 OD1 ASP A 523 6.926 223.139 826.824 1.00113.74 O ANISOU 3681 OD1 ASP A 523 17022 14622 11571 -1991 -854 2509 O ATOM 3682 OD2 ASP A 523 6.864 220.948 827.072 1.00113.92 O ANISOU 3682 OD2 ASP A 523 17195 14670 11420 -2491 -616 2919 O ATOM 3683 N VAL A 524 10.165 221.901 823.178 1.00 83.04 N ANISOU 3683 N VAL A 524 12646 10490 8415 -1873 -861 2212 N ATOM 3684 CA VAL A 524 11.366 221.658 822.391 1.00 78.01 C ANISOU 3684 CA VAL A 524 11964 9708 7968 -1834 -995 2179 C ATOM 3685 C VAL A 524 11.715 222.848 821.494 1.00 72.78 C ANISOU 3685 C VAL A 524 11169 9118 7364 -1536 -1088 1875 C ATOM 3686 O VAL A 524 12.882 223.206 821.346 1.00 71.81 O ANISOU 3686 O VAL A 524 11118 8838 7329 -1408 -1298 1798 O ATOM 3687 CB VAL A 524 11.213 220.383 821.544 1.00 72.50 C ANISOU 3687 CB VAL A 524 11095 9069 7381 -2086 -800 2270 C ATOM 3688 CG1 VAL A 524 12.279 220.322 820.467 1.00 63.03 C ANISOU 3688 CG1 VAL A 524 9713 7782 6454 -1993 -982 2052 C ATOM 3689 CG2 VAL A 524 11.269 219.152 822.438 1.00 80.70 C ANISOU 3689 CG2 VAL A 524 12222 9944 8497 -2417 -726 2519 C ATOM 3690 N LEU A 525 10.697 223.462 820.903 1.00 75.15 N ANISOU 3690 N LEU A 525 11287 9641 7625 -1438 -921 1710 N ATOM 3691 CA LEU A 525 10.900 224.631 820.057 1.00 69.68 C ANISOU 3691 CA LEU A 525 10459 8992 7026 -1191 -953 1466 C ATOM 3692 C LEU A 525 11.463 225.804 820.851 1.00 68.76 C ANISOU 3692 C LEU A 525 10466 8725 6934 -1003 -1070 1368 C ATOM 3693 O LEU A 525 12.361 226.500 820.387 1.00 73.71 O ANISOU 3693 O LEU A 525 11091 9284 7629 -843 -1158 1230 O ATOM 3694 CB LEU A 525 9.595 225.021 819.363 1.00 63.31 C ANISOU 3694 CB LEU A 525 9444 8398 6213 -1143 -749 1364 C ATOM 3695 CG LEU A 525 9.224 224.066 818.226 1.00 62.43 C ANISOU 3695 CG LEU A 525 9168 8437 6116 -1257 -639 1414 C ATOM 3696 CD1 LEU A 525 7.761 224.193 817.820 1.00 66.82 C ANISOU 3696 CD1 LEU A 525 9569 9191 6628 -1253 -414 1350 C ATOM 3697 CD2 LEU A 525 10.140 224.299 817.046 1.00 35.08 C ANISOU 3697 CD2 LEU A 525 5609 4946 2773 -1141 -789 1337 C ATOM 3698 N ARG A 526 10.886 226.018 822.013 1.00 74.20 N ANISOU 3698 N ARG A 526 11263 9382 7546 -1027 -1062 1449 N ATOM 3699 CA ARG A 526 11.310 227.053 822.914 1.00 78.92 C ANISOU 3699 CA ARG A 526 11980 9839 8167 -859 -1179 1401 C ATOM 3700 C ARG A 526 12.689 226.688 823.403 1.00 77.24 C ANISOU 3700 C ARG A 526 11962 9391 7993 -853 -1403 1476 C ATOM 3701 O ARG A 526 13.542 227.530 823.578 1.00 68.39 O ANISOU 3701 O ARG A 526 10906 8154 6926 -660 -1513 1359 O ATOM 3702 CB ARG A 526 10.346 227.126 824.093 1.00 89.13 C ANISOU 3702 CB ARG A 526 13369 11150 9345 -928 -1174 1534 C ATOM 3703 CG ARG A 526 8.931 227.595 823.763 1.00109.42 C ANISOU 3703 CG ARG A 526 15884 13755 11937 -737 -1152 1412 C ATOM 3704 CD ARG A 526 8.060 227.679 825.023 1.00125.32 C ANISOU 3704 CD ARG A 526 18079 15703 13834 -787 -1283 1591 C ATOM 3705 NE ARG A 526 6.657 228.057 824.801 1.00130.85 N ANISOU 3705 NE ARG A 526 18712 16501 14504 -682 -1243 1520 N ATOM 3706 CZ ARG A 526 5.717 228.076 825.742 1.00130.89 C ANISOU 3706 CZ ARG A 526 18724 16418 14589 -482 -1349 1456 C ATOM 3707 NH1 ARG A 526 6.017 227.777 826.995 1.00122.37 N ANISOU 3707 NH1 ARG A 526 17719 15160 13618 -344 -1488 1430 N ATOM 3708 NH2 ARG A 526 4.472 228.406 825.429 1.00135.46 N ANISOU 3708 NH2 ARG A 526 19238 17095 15134 -416 -1322 1417 N ATOM 3709 N SER A 527 12.885 225.404 823.646 1.00 85.12 N ANISOU 3709 N SER A 527 13062 10310 8970 -1069 -1465 1691 N ATOM 3710 CA SER A 527 14.135 224.901 824.169 1.00 87.85 C ANISOU 3710 CA SER A 527 13607 10371 9400 -1091 -1703 1817 C ATOM 3711 C SER A 527 15.220 225.188 823.191 1.00 84.22 C ANISOU 3711 C SER A 527 13111 9888 9000 -949 -1803 1619 C ATOM 3712 O SER A 527 16.299 225.600 823.550 1.00 85.80 O ANISOU 3712 O SER A 527 13455 9893 9255 -795 -2008 1557 O ATOM 3713 CB SER A 527 14.025 223.397 824.302 1.00 92.96 C ANISOU 3713 CB SER A 527 14317 10941 10064 -1395 -1677 2107 C ATOM 3714 OG SER A 527 12.706 222.978 824.002 1.00106.57 O ANISOU 3714 OG SER A 527 15902 12936 11654 -1553 -1417 2151 O ATOM 3715 N ILE A 528 14.937 224.913 821.940 1.00 71.16 N ANISOU 3715 N ILE A 528 11273 8438 7326 -1001 -1683 1530 N ATOM 3716 CA ILE A 528 15.878 225.170 820.881 1.00 69.19 C ANISOU 3716 CA ILE A 528 10980 8220 7088 -885 -1796 1343 C ATOM 3717 C ILE A 528 16.150 226.622 820.625 1.00 64.51 C ANISOU 3717 C ILE A 528 10357 7681 6474 -631 -1743 1094 C ATOM 3718 O ILE A 528 17.268 227.030 820.458 1.00 65.43 O ANISOU 3718 O ILE A 528 10575 7729 6557 -496 -1900 952 O ATOM 3719 CB ILE A 528 15.325 224.650 819.603 1.00 72.83 C ANISOU 3719 CB ILE A 528 11224 8893 7553 -984 -1683 1332 C ATOM 3720 CG1 ILE A 528 15.500 223.151 819.546 1.00 91.77 C ANISOU 3720 CG1 ILE A 528 13584 11193 10092 -1244 -1734 1478 C ATOM 3721 CD1 ILE A 528 15.145 222.589 818.239 1.00103.92 C ANISOU 3721 CD1 ILE A 528 14861 12903 11723 -1328 -1664 1420 C ATOM 3722 CG2 ILE A 528 16.022 225.279 818.462 1.00 57.77 C ANISOU 3722 CG2 ILE A 528 9241 7065 5643 -834 -1759 1112 C ATOM 3723 N SER A 529 15.104 227.412 820.606 1.00 56.47 N ANISOU 3723 N SER A 529 9199 6793 5465 -567 -1519 1047 N ATOM 3724 CA SER A 529 15.246 228.803 820.303 1.00 54.12 C ANISOU 3724 CA SER A 529 8847 6550 5166 -345 -1428 869 C ATOM 3725 C SER A 529 16.111 229.445 821.313 1.00 53.80 C ANISOU 3725 C SER A 529 8997 6350 5095 -185 -1570 820 C ATOM 3726 O SER A 529 16.899 230.282 821.002 1.00 52.36 O ANISOU 3726 O SER A 529 8850 6183 4863 -7 -1590 666 O ATOM 3727 CB SER A 529 13.901 229.476 820.284 1.00 51.43 C ANISOU 3727 CB SER A 529 8331 6344 4866 -318 -1210 863 C ATOM 3728 OG SER A 529 14.018 230.800 819.852 1.00 42.45 O ANISOU 3728 OG SER A 529 7119 5269 3742 -122 -1116 728 O ATOM 3729 N LYS A 530 15.970 229.072 822.553 1.00 49.09 N ANISOU 3729 N LYS A 530 8529 5603 4520 -238 -1681 965 N ATOM 3730 CA LYS A 530 16.804 229.707 823.525 1.00 59.66 C ANISOU 3730 CA LYS A 530 10035 6765 5868 -51 -1859 932 C ATOM 3731 C LYS A 530 18.240 229.394 823.268 1.00 78.53 C ANISOU 3731 C LYS A 530 12573 9038 8227 19 -2090 841 C ATOM 3732 O LYS A 530 19.103 230.243 823.381 1.00 88.77 O ANISOU 3732 O LYS A 530 13940 10318 9469 242 -2181 666 O ATOM 3733 CB LYS A 530 16.443 229.277 824.923 1.00 67.92 C ANISOU 3733 CB LYS A 530 11204 7619 6982 -124 -1995 1162 C ATOM 3734 CG LYS A 530 17.296 229.955 825.953 1.00 88.21 C ANISOU 3734 CG LYS A 530 13920 9955 9640 111 -2221 1153 C ATOM 3735 CD LYS A 530 16.431 230.581 827.011 1.00108.65 C ANISOU 3735 CD LYS A 530 16485 12526 12270 159 -2218 1256 C ATOM 3736 CE LYS A 530 15.335 231.441 826.374 1.00115.14 C ANISOU 3736 CE LYS A 530 17097 13655 12997 170 -1932 1123 C ATOM 3737 NZ LYS A 530 14.342 232.018 827.335 1.00112.79 N ANISOU 3737 NZ LYS A 530 16769 13378 12710 190 -1948 1224 N ATOM 3738 N LYS A 531 18.509 228.163 822.899 1.00 76.16 N ANISOU 3738 N LYS A 531 12311 8684 7941 -173 -2207 941 N ATOM 3739 CA LYS A 531 19.874 227.767 822.707 1.00 76.51 C ANISOU 3739 CA LYS A 531 12415 8536 8118 -174 -2381 715 C ATOM 3740 C LYS A 531 20.509 228.623 821.654 1.00 74.11 C ANISOU 3740 C LYS A 531 12083 8457 7618 -16 -2351 432 C ATOM 3741 O LYS A 531 21.639 229.019 821.792 1.00 76.86 O ANISOU 3741 O LYS A 531 12511 8684 8008 109 -2443 158 O ATOM 3742 CB LYS A 531 19.932 226.309 822.325 1.00 79.71 C ANISOU 3742 CB LYS A 531 12772 8846 8667 -456 -2442 809 C ATOM 3743 N PHE A 532 19.769 228.938 820.612 1.00 67.37 N ANISOU 3743 N PHE A 532 11097 7891 6609 -31 -2173 477 N ATOM 3744 CA PHE A 532 20.292 229.773 819.566 1.00 68.97 C ANISOU 3744 CA PHE A 532 11256 8269 6682 92 -2086 262 C ATOM 3745 C PHE A 532 20.635 231.086 820.182 1.00 69.07 C ANISOU 3745 C PHE A 532 11335 8297 6611 333 -2020 123 C ATOM 3746 O PHE A 532 21.529 231.755 819.736 1.00 67.09 O ANISOU 3746 O PHE A 532 11148 8152 6192 456 -2032 -107 O ATOM 3747 CB PHE A 532 19.284 229.980 818.467 1.00 69.00 C ANISOU 3747 CB PHE A 532 11033 8450 6734 35 -1831 353 C ATOM 3748 CG PHE A 532 18.993 228.752 817.686 1.00 79.96 C ANISOU 3748 CG PHE A 532 12324 9869 8187 -176 -1906 457 C ATOM 3749 CD1 PHE A 532 19.974 227.855 817.416 1.00 80.13 C ANISOU 3749 CD1 PHE A 532 12441 9839 8165 -271 -2192 383 C ATOM 3750 CE1 PHE A 532 19.702 226.740 816.694 1.00 75.96 C ANISOU 3750 CE1 PHE A 532 11789 9359 7715 -461 -2289 479 C ATOM 3751 CZ PHE A 532 18.456 226.513 816.240 1.00 63.92 C ANISOU 3751 CZ PHE A 532 10061 7939 6288 -541 -2083 645 C ATOM 3752 CE2 PHE A 532 17.478 227.391 816.494 1.00 68.12 C ANISOU 3752 CE2 PHE A 532 10511 8521 6850 -452 -1797 686 C ATOM 3753 CD2 PHE A 532 17.736 228.505 817.205 1.00 79.60 C ANISOU 3753 CD2 PHE A 532 12072 9922 8250 -278 -1718 594 C ATOM 3754 N LEU A 533 19.888 231.505 821.180 1.00 62.92 N ANISOU 3754 N LEU A 533 10529 7441 5935 396 -1940 253 N ATOM 3755 CA LEU A 533 20.227 232.761 821.800 1.00 65.98 C ANISOU 3755 CA LEU A 533 10956 7858 6255 639 -1914 122 C ATOM 3756 C LEU A 533 21.582 232.688 822.470 1.00 73.06 C ANISOU 3756 C LEU A 533 11989 8524 7248 740 -2100 -135 C ATOM 3757 O LEU A 533 22.419 233.556 822.306 1.00 73.15 O ANISOU 3757 O LEU A 533 12018 8600 7175 904 -2031 -424 O ATOM 3758 CB LEU A 533 19.203 233.092 822.855 1.00 60.74 C ANISOU 3758 CB LEU A 533 10227 7104 5747 671 -1854 308 C ATOM 3759 CG LEU A 533 17.885 233.625 822.354 1.00 54.38 C ANISOU 3759 CG LEU A 533 9199 6459 5004 614 -1558 379 C ATOM 3760 CD1 LEU A 533 17.091 233.972 823.548 1.00 59.75 C ANISOU 3760 CD1 LEU A 533 9858 7056 5787 649 -1578 493 C ATOM 3761 CD2 LEU A 533 18.139 234.846 821.571 1.00 45.71 C ANISOU 3761 CD2 LEU A 533 8007 5560 3801 771 -1388 236 C ATOM 3762 N ASP A 534 21.813 231.602 823.173 1.00 73.31 N ANISOU 3762 N ASP A 534 12086 8236 7534 617 -2279 -59 N ATOM 3763 CA ASP A 534 23.016 231.455 823.951 1.00 77.14 C ANISOU 3763 CA ASP A 534 12657 8370 8281 700 -2431 -309 C ATOM 3764 C ASP A 534 24.231 231.618 823.108 1.00 71.70 C ANISOU 3764 C ASP A 534 12025 7766 7452 742 -2440 -693 C ATOM 3765 O ASP A 534 25.225 232.143 823.560 1.00 74.80 O ANISOU 3765 O ASP A 534 12463 8005 7953 911 -2457 -1021 O ATOM 3766 CB ASP A 534 23.031 230.094 824.602 1.00 79.12 C ANISOU 3766 CB ASP A 534 12971 8276 8816 496 -2627 -121 C ATOM 3767 CG ASP A 534 21.995 229.967 825.656 1.00 84.75 C ANISOU 3767 CG ASP A 534 13680 8864 9656 462 -2648 243 C ATOM 3768 OD1 ASP A 534 21.603 230.987 826.224 1.00 88.55 O ANISOU 3768 OD1 ASP A 534 14120 9394 10132 655 -2589 264 O ATOM 3769 OD2 ASP A 534 21.574 228.844 825.928 1.00 84.06 O ANISOU 3769 OD2 ASP A 534 13631 8638 9671 230 -2726 511 O ATOM 3770 N ILE A 535 24.167 231.160 821.881 1.00 64.92 N ANISOU 3770 N ILE A 535 11161 7149 6356 590 -2439 -669 N ATOM 3771 CA ILE A 535 25.305 231.287 821.015 1.00 77.87 C ANISOU 3771 CA ILE A 535 12883 8903 7803 607 -2484 -1017 C ATOM 3772 C ILE A 535 25.680 232.732 820.802 1.00 80.87 C ANISOU 3772 C ILE A 535 13277 9525 7926 829 -2281 -1255 C ATOM 3773 O ILE A 535 26.845 233.069 820.836 1.00 79.79 O ANISOU 3773 O ILE A 535 13234 9338 7746 928 -2294 -1641 O ATOM 3774 CB ILE A 535 24.975 230.754 819.655 1.00 78.56 C ANISOU 3774 CB ILE A 535 12935 9263 7652 430 -2522 -890 C ATOM 3775 CG1 ILE A 535 24.654 229.278 819.736 1.00 76.78 C ANISOU 3775 CG1 ILE A 535 12657 8828 7687 188 -2691 -685 C ATOM 3776 CD1 ILE A 535 24.379 228.690 818.435 1.00 63.38 C ANISOU 3776 CD1 ILE A 535 10881 7358 5841 26 -2753 -587 C ATOM 3777 CG2 ILE A 535 26.122 230.967 818.752 1.00 81.70 C ANISOU 3777 CG2 ILE A 535 13442 9812 7789 446 -2598 -1227 C ATOM 3778 N ILE A 536 24.705 233.594 820.566 1.00 74.15 N ANISOU 3778 N ILE A 536 12328 8940 6905 896 -2078 -1046 N ATOM 3779 CA ILE A 536 25.012 234.993 820.386 1.00 70.04 C ANISOU 3779 CA ILE A 536 11797 8653 6165 1084 -1851 -1244 C ATOM 3780 C ILE A 536 25.505 235.621 821.656 1.00 73.93 C ANISOU 3780 C ILE A 536 12257 8896 6938 1295 -1798 -1469 C ATOM 3781 O ILE A 536 26.462 236.358 821.683 1.00 62.54 O ANISOU 3781 O ILE A 536 10850 7498 5413 1438 -1682 -1834 O ATOM 3782 CB ILE A 536 23.817 235.737 819.998 1.00 60.78 C ANISOU 3782 CB ILE A 536 10502 7750 4842 1098 -1665 -957 C ATOM 3783 CG1 ILE A 536 23.457 235.359 818.587 1.00 66.12 C ANISOU 3783 CG1 ILE A 536 11111 8601 5410 943 -1627 -748 C ATOM 3784 CD1 ILE A 536 24.291 236.031 817.616 1.00 69.31 C ANISOU 3784 CD1 ILE A 536 11577 9244 5513 977 -1531 -930 C ATOM 3785 CG2 ILE A 536 24.145 237.170 820.006 1.00 58.26 C ANISOU 3785 CG2 ILE A 536 10144 7622 4370 1281 -1415 -1151 C ATOM 3786 N THR A 537 24.842 235.285 822.737 1.00 70.03 N ANISOU 3786 N THR A 537 11693 8127 6788 1309 -1894 -1248 N ATOM 3787 CA THR A 537 25.191 235.812 824.017 1.00 74.63 C ANISOU 3787 CA THR A 537 12218 8423 7715 1514 -1902 -1402 C ATOM 3788 C THR A 537 26.583 235.329 824.222 1.00 91.44 C ANISOU 3788 C THR A 537 14464 10286 9992 1542 -2034 -1789 C ATOM 3789 O THR A 537 27.370 235.942 824.914 1.00 97.91 O ANISOU 3789 O THR A 537 15253 10928 11022 1747 -1988 -2121 O ATOM 3790 CB THR A 537 24.368 235.178 825.078 1.00 71.48 C ANISOU 3790 CB THR A 537 11788 7729 7644 1464 -2083 -1063 C ATOM 3791 OG1 THR A 537 24.625 233.776 825.065 1.00 80.00 O ANISOU 3791 OG1 THR A 537 12985 8577 8835 1257 -2303 -974 O ATOM 3792 CG2 THR A 537 22.943 235.395 824.787 1.00 69.67 C ANISOU 3792 CG2 THR A 537 11472 7760 7239 1384 -1988 -689 C ATOM 3793 N GLY A 538 26.891 234.198 823.626 1.00 96.74 N ANISOU 3793 N GLY A 538 15253 10910 10593 1333 -2207 -1768 N ATOM 3794 CA GLY A 538 28.204 233.640 823.791 1.00100.47 C ANISOU 3794 CA GLY A 538 15844 11107 11225 1329 -2370 -2147 C ATOM 3795 C GLY A 538 28.150 232.763 825.000 1.00103.01 C ANISOU 3795 C GLY A 538 16165 10919 12054 1290 -2607 -1994 C ATOM 3796 O GLY A 538 29.160 232.270 825.461 1.00110.48 O ANISOU 3796 O GLY A 538 17186 11507 13284 1303 -2776 -2277 O ATOM 3797 N GLU A 539 26.952 232.539 825.510 1.00100.57 N ANISOU 3797 N GLU A 539 15785 10572 11854 1225 -2630 -1537 N ATOM 3798 CA GLU A 539 26.846 231.685 826.671 1.00108.68 C ANISOU 3798 CA GLU A 539 16841 11127 13326 1159 -2863 -1324 C ATOM 3799 C GLU A 539 27.428 230.376 826.212 1.00116.83 C ANISOU 3799 C GLU A 539 17973 11997 14420 912 -3045 -1368 C ATOM 3800 O GLU A 539 28.152 229.733 826.946 1.00121.95 O ANISOU 3800 O GLU A 539 18683 12193 15460 884 -3253 -1472 O ATOM 3801 CB GLU A 539 25.409 231.500 827.113 1.00113.80 C ANISOU 3801 CB GLU A 539 17438 11834 13967 1063 -2859 -801 C ATOM 3802 CG GLU A 539 25.279 231.125 828.572 1.00135.29 C ANISOU 3802 CG GLU A 539 20187 14086 17129 1086 -3074 -580 C ATOM 3803 CD GLU A 539 25.511 232.300 829.513 1.00152.82 C ANISOU 3803 CD GLU A 539 22315 16155 19596 1408 -3070 -748 C ATOM 3804 OE1 GLU A 539 25.600 233.445 829.030 1.00158.44 O ANISOU 3804 OE1 GLU A 539 22922 17176 20102 1594 -2847 -999 O ATOM 3805 OE2 GLU A 539 25.598 232.085 830.741 1.00155.06 O ANISOU 3805 OE2 GLU A 539 22616 16001 20300 1472 -3292 -615 O ATOM 3806 N LEU A 540 27.149 229.988 824.978 1.00115.96 N ANISOU 3806 N LEU A 540 17863 12233 13963 732 -2986 -1302 N ATOM 3807 CA LEU A 540 27.743 228.773 824.481 1.00110.67 C ANISOU 3807 CA LEU A 540 17251 11420 13376 497 -3176 -1373 C ATOM 3808 C LEU A 540 29.116 229.255 824.132 1.00120.15 C ANISOU 3808 C LEU A 540 18535 12614 14504 636 -3205 -1926 C ATOM 3809 O LEU A 540 29.292 230.052 823.222 1.00114.67 O ANISOU 3809 O LEU A 540 17852 12315 13401 724 -3051 -2121 O ATOM 3810 CB LEU A 540 27.055 228.302 823.223 1.00 92.97 C ANISOU 3810 CB LEU A 540 14952 9561 10813 295 -3118 -1166 C ATOM 3811 CG LEU A 540 25.900 227.367 823.473 1.00 79.56 C ANISOU 3811 CG LEU A 540 13180 7810 9239 72 -3122 -688 C ATOM 3812 CD1 LEU A 540 25.681 226.536 822.272 1.00 71.32 C ANISOU 3812 CD1 LEU A 540 12062 6985 8051 -155 -3150 -611 C ATOM 3813 CD2 LEU A 540 26.278 226.507 824.602 1.00 78.98 C ANISOU 3813 CD2 LEU A 540 13164 7234 9610 -30 -3309 -610 C ATOM 3814 N PRO A 541 30.096 228.765 824.869 1.00135.81 N ANISOU 3814 N PRO A 541 20586 14136 16881 645 -3402 -2179 N ATOM 3815 CA PRO A 541 31.485 229.198 824.681 1.00146.03 C ANISOU 3815 CA PRO A 541 21971 15371 18143 786 -3433 -2778 C ATOM 3816 C PRO A 541 31.806 229.416 823.206 1.00147.88 C ANISOU 3816 C PRO A 541 22264 16092 17833 718 -3368 -2986 C ATOM 3817 O PRO A 541 31.394 228.616 822.362 1.00152.29 O ANISOU 3817 O PRO A 541 22803 16816 18245 483 -3468 -2751 O ATOM 3818 CB PRO A 541 32.289 228.018 825.234 1.00151.26 C ANISOU 3818 CB PRO A 541 22694 15491 19285 634 -3739 -2906 C ATOM 3819 CG PRO A 541 31.413 227.451 826.312 1.00147.96 C ANISOU 3819 CG PRO A 541 22216 14734 19268 553 -3815 -2398 C ATOM 3820 CD PRO A 541 29.987 227.669 825.850 1.00142.37 C ANISOU 3820 CD PRO A 541 21423 14463 18207 487 -3619 -1920 C ATOM 3821 N ASP A 542 32.463 230.529 822.916 1.00143.17 N ANISOU 3821 N ASP A 542 21725 15735 16939 923 -3189 -3390 N ATOM 3822 CA ASP A 542 32.824 230.905 821.561 1.00137.79 C ANISOU 3822 CA ASP A 542 21136 15536 15683 876 -3119 -3583 C ATOM 3823 C ASP A 542 33.823 229.996 820.893 1.00133.63 C ANISOU 3823 C ASP A 542 20738 14939 15098 691 -3404 -3888 C ATOM 3824 O ASP A 542 33.764 229.772 819.697 1.00134.35 O ANISOU 3824 O ASP A 542 20873 15375 14798 542 -3479 -3820 O ATOM 3825 CB ASP A 542 33.310 232.335 821.504 1.00140.63 C ANISOU 3825 CB ASP A 542 21535 16167 15730 1123 -2822 -3941 C ATOM 3826 CG ASP A 542 33.445 232.811 820.104 1.00139.75 C ANISOU 3826 CG ASP A 542 21529 16601 14969 1054 -2723 -4002 C ATOM 3827 OD1 ASP A 542 33.281 231.966 819.209 1.00138.42 O ANISOU 3827 OD1 ASP A 542 21400 16547 14646 831 -2942 -3817 O ATOM 3828 OD2 ASP A 542 33.711 234.004 819.892 1.00139.28 O ANISOU 3828 OD2 ASP A 542 21504 16848 14569 1212 -2435 -4219 O ATOM 3829 N SER A 543 34.745 229.475 821.679 1.00125.39 N ANISOU 3829 N SER A 543 19745 13423 14475 704 -3589 -4226 N ATOM 3830 CA SER A 543 35.798 228.635 821.165 1.00126.68 C ANISOU 3830 CA SER A 543 20028 13463 14641 535 -3885 -4588 C ATOM 3831 C SER A 543 35.212 227.467 820.441 1.00133.38 C ANISOU 3831 C SER A 543 20803 14361 15513 235 -4112 -4196 C ATOM 3832 O SER A 543 35.797 226.956 819.503 1.00132.46 O ANISOU 3832 O SER A 543 20760 14384 15183 74 -4334 -4389 O ATOM 3833 CB SER A 543 36.584 228.064 822.309 1.00124.21 C ANISOU 3833 CB SER A 543 19729 12517 14948 562 -4073 -4871 C ATOM 3834 OG SER A 543 36.835 226.705 822.034 1.00124.89 O ANISOU 3834 OG SER A 543 19814 12356 15282 275 -4414 -4815 O ATOM 3835 N MSE A 544 34.054 227.038 820.900 1.00135.52 N ANISOU 3835 N MSE A 544 20920 14518 16055 159 -4060 -3656 N ATOM 3836 CA MSE A 544 33.352 225.897 820.353 1.00133.02 C ANISOU 3836 CA MSE A 544 20482 14221 15838 -122 -4216 -3253 C ATOM 3837 C MSE A 544 33.084 226.089 818.866 1.00120.17 C ANISOU 3837 C MSE A 544 18848 13128 13684 -193 -4213 -3182 C ATOM 3838 O MSE A 544 32.743 227.170 818.434 1.00113.92 O ANISOU 3838 O MSE A 544 18091 12723 12468 -32 -3984 -3148 O ATOM 3839 CB MSE A 544 32.012 225.827 821.091 1.00132.59 C ANISOU 3839 CB MSE A 544 20289 14090 15999 -126 -4037 -2705 C ATOM 3840 CG MSE A 544 31.590 224.474 821.635 1.00134.02 C ANISOU 3840 CG MSE A 544 20366 13894 16662 -384 -4189 -2369 C ATOM 3841 SE MSE A 544 30.251 224.684 823.005 1.00136.36 Se ANISOU 3841 SE MSE A 544 20595 14012 17205 -314 -3971 -1823 Se ATOM 3842 CE MSE A 544 29.503 222.928 822.991 1.00 69.42 C ANISOU 3842 CE MSE A 544 11975 5343 9059 -733 -4082 -1344 C ATOM 3843 N THR A 545 33.255 225.034 818.079 1.00111.89 N ANISOU 3843 N THR A 545 17741 12079 12693 -439 -4487 -3152 N ATOM 3844 CA THR A 545 32.987 225.090 816.649 1.00102.87 C ANISOU 3844 CA THR A 545 16568 11393 11123 -517 -4555 -3046 C ATOM 3845 C THR A 545 31.485 225.131 816.384 1.00107.25 C ANISOU 3845 C THR A 545 16934 12166 11651 -539 -4346 -2499 C ATOM 3846 O THR A 545 30.700 224.564 817.143 1.00105.39 O ANISOU 3846 O THR A 545 16559 11691 11792 -615 -4256 -2187 O ATOM 3847 CB THR A 545 33.591 223.874 815.924 1.00 89.93 C ANISOU 3847 CB THR A 545 14876 9653 9641 -777 -4951 -3173 C ATOM 3848 OG1 THR A 545 34.987 224.103 815.706 1.00 91.29 O ANISOU 3848 OG1 THR A 545 15266 9814 9605 -741 -5157 -3732 O ATOM 3849 CG2 THR A 545 32.911 223.653 814.579 1.00 86.06 C ANISOU 3849 CG2 THR A 545 14250 9549 8901 -887 -5037 -2879 C ATOM 3850 N THR A 546 31.107 225.688 815.254 1.00109.74 N ANISOU 3850 N THR A 546 17244 12918 11532 -503 -4300 -2384 N ATOM 3851 CA THR A 546 29.709 225.785 814.959 1.00109.56 C ANISOU 3851 CA THR A 546 17042 13089 11496 -509 -4103 -1918 C ATOM 3852 C THR A 546 29.156 224.381 815.002 1.00103.06 C ANISOU 3852 C THR A 546 15993 12042 11122 -750 -4233 -1667 C ATOM 3853 O THR A 546 28.119 224.132 815.586 1.00 92.79 O ANISOU 3853 O THR A 546 14556 10652 10047 -782 -4037 -1342 O ATOM 3854 CB THR A 546 29.528 226.364 813.580 1.00105.80 C ANISOU 3854 CB THR A 546 16583 13056 10561 -479 -4131 -1843 C ATOM 3855 OG1 THR A 546 29.990 227.711 813.579 1.00102.82 O ANISOU 3855 OG1 THR A 546 16413 12907 9747 -276 -3951 -2048 O ATOM 3856 CG2 THR A 546 28.102 226.380 813.235 1.00107.70 C ANISOU 3856 CG2 THR A 546 16619 13450 10854 -491 -3955 -1398 C ATOM 3857 N VAL A 547 29.877 223.452 814.414 1.00101.95 N ANISOU 3857 N VAL A 547 15811 11811 11113 -932 -4562 -1834 N ATOM 3858 CA VAL A 547 29.474 222.050 814.448 1.00101.63 C ANISOU 3858 CA VAL A 547 15527 11541 11548 -1188 -4684 -1632 C ATOM 3859 C VAL A 547 29.305 221.569 815.882 1.00103.06 C ANISOU 3859 C VAL A 547 15700 11310 12147 -1249 -4552 -1534 C ATOM 3860 O VAL A 547 28.295 220.952 816.227 1.00107.20 O ANISOU 3860 O VAL A 547 16044 11761 12925 -1375 -4391 -1180 O ATOM 3861 CB VAL A 547 30.497 221.141 813.744 1.00105.51 C ANISOU 3861 CB VAL A 547 15981 11934 12173 -1378 -5103 -1902 C ATOM 3862 CG1 VAL A 547 30.212 219.675 814.056 1.00 98.92 C ANISOU 3862 CG1 VAL A 547 14886 10779 11922 -1659 -5193 -1732 C ATOM 3863 CG2 VAL A 547 30.476 221.391 812.247 1.00108.11 C ANISOU 3863 CG2 VAL A 547 16270 12660 12147 -1364 -5288 -1890 C ATOM 3864 N GLU A 548 30.298 221.851 816.720 1.00 91.12 N ANISOU 3864 N GLU A 548 14389 9527 10705 -1162 -4622 -1851 N ATOM 3865 CA GLU A 548 30.241 221.452 818.116 1.00 85.08 C ANISOU 3865 CA GLU A 548 13644 8327 10357 -1205 -4547 -1752 C ATOM 3866 C GLU A 548 28.968 221.970 818.779 1.00 89.35 C ANISOU 3866 C GLU A 548 14146 8958 10843 -1100 -4210 -1356 C ATOM 3867 O GLU A 548 28.239 221.210 819.414 1.00 91.14 O ANISOU 3867 O GLU A 548 14266 8994 11369 -1264 -4124 -1023 O ATOM 3868 CB GLU A 548 31.474 221.951 818.868 1.00 85.00 C ANISOU 3868 CB GLU A 548 13856 8035 10403 -1052 -4651 -2189 C ATOM 3869 CG GLU A 548 32.787 221.481 818.272 1.00 89.52 C ANISOU 3869 CG GLU A 548 14498 8511 11005 -1154 -4997 -2644 C ATOM 3870 CD GLU A 548 33.970 221.803 819.158 1.00 91.02 C ANISOU 3870 CD GLU A 548 14885 8337 11362 -1026 -5091 -3097 C ATOM 3871 OE2 GLU A 548 35.034 221.172 818.973 1.00 86.29 O ANISOU 3871 OE2 GLU A 548 14332 7511 10942 -1156 -5397 -3465 O ATOM 3872 OE1 GLU A 548 33.834 222.685 820.033 1.00 87.92 O ANISOU 3872 OE1 GLU A 548 14584 7872 10949 -793 -4869 -3104 O ATOM 3873 N LYS A 549 28.708 223.266 818.622 1.00 96.07 N ANISOU 3873 N LYS A 549 15091 10114 11298 -843 -4021 -1395 N ATOM 3874 CA LYS A 549 27.552 223.901 819.244 1.00 98.86 C ANISOU 3874 CA LYS A 549 15418 10565 11578 -723 -3729 -1070 C ATOM 3875 C LYS A 549 26.256 223.235 818.802 1.00 93.31 C ANISOU 3875 C LYS A 549 14511 10031 10911 -900 -3606 -662 C ATOM 3876 O LYS A 549 25.351 223.018 819.603 1.00 88.73 O ANISOU 3876 O LYS A 549 13889 9354 10469 -952 -3444 -353 O ATOM 3877 CB LYS A 549 27.505 225.393 818.902 1.00106.14 C ANISOU 3877 CB LYS A 549 16432 11828 12068 -447 -3556 -1197 C ATOM 3878 CG LYS A 549 28.668 226.212 819.444 1.00110.37 C ANISOU 3878 CG LYS A 549 17151 12231 12554 -241 -3586 -1615 C ATOM 3879 CD LYS A 549 28.654 227.625 818.872 1.00107.96 C ANISOU 3879 CD LYS A 549 16910 12326 11782 -17 -3390 -1742 C ATOM 3880 CE LYS A 549 29.873 228.417 819.322 1.00109.62 C ANISOU 3880 CE LYS A 549 17283 12441 11927 179 -3381 -2217 C ATOM 3881 NZ LYS A 549 29.945 229.752 818.668 1.00106.31 N ANISOU 3881 NZ LYS A 549 16928 12443 11021 357 -3165 -2350 N ATOM 3882 N PHE A 550 26.178 222.907 817.516 1.00 95.66 N ANISOU 3882 N PHE A 550 14682 10582 11084 -992 -3692 -675 N ATOM 3883 CA PHE A 550 24.981 222.294 816.945 1.00 97.38 C ANISOU 3883 CA PHE A 550 14667 10974 11361 -1140 -3568 -348 C ATOM 3884 C PHE A 550 24.763 220.852 817.411 1.00101.57 C ANISOU 3884 C PHE A 550 15046 11222 12324 -1432 -3600 -173 C ATOM 3885 O PHE A 550 23.631 220.443 817.677 1.00102.66 O ANISOU 3885 O PHE A 550 15056 11406 12546 -1540 -3378 137 O ATOM 3886 CB PHE A 550 25.024 222.375 815.417 1.00 92.02 C ANISOU 3886 CB PHE A 550 13875 10610 10479 -1135 -3693 -417 C ATOM 3887 CG PHE A 550 24.517 223.677 814.874 1.00 93.78 C ANISOU 3887 CG PHE A 550 14159 11179 10294 -909 -3531 -371 C ATOM 3888 CD1 PHE A 550 24.049 223.772 813.577 1.00 93.42 C ANISOU 3888 CD1 PHE A 550 13972 11420 10102 -907 -3570 -276 C ATOM 3889 CE1 PHE A 550 23.576 224.970 813.086 1.00 91.34 C ANISOU 3889 CE1 PHE A 550 13767 11443 9494 -718 -3422 -205 C ATOM 3890 CZ PHE A 550 23.555 226.082 813.893 1.00 82.98 C ANISOU 3890 CZ PHE A 550 12875 10385 8267 -530 -3190 -239 C ATOM 3891 CE2 PHE A 550 24.010 225.997 815.189 1.00 83.66 C ANISOU 3891 CE2 PHE A 550 13090 10219 8480 -518 -3183 -356 C ATOM 3892 CD2 PHE A 550 24.483 224.803 815.675 1.00 92.38 C ANISOU 3892 CD2 PHE A 550 14159 11018 9925 -702 -3346 -409 C ATOM 3893 N THR A 551 25.840 220.081 817.508 1.00 98.01 N ANISOU 3893 N THR A 551 14611 10485 12141 -1577 -3863 -379 N ATOM 3894 CA THR A 551 25.737 218.740 818.062 1.00100.60 C ANISOU 3894 CA THR A 551 14808 10502 12915 -1875 -3886 -209 C ATOM 3895 C THR A 551 25.345 218.832 819.539 1.00106.53 C ANISOU 3895 C THR A 551 15705 10998 13776 -1869 -3714 17 C ATOM 3896 O THR A 551 24.686 217.942 820.076 1.00107.67 O ANISOU 3896 O THR A 551 15751 11006 14153 -2101 -3583 322 O ATOM 3897 CB THR A 551 27.051 217.939 817.892 1.00104.25 C ANISOU 3897 CB THR A 551 15261 10669 13679 -2035 -4237 -504 C ATOM 3898 OG1 THR A 551 28.097 218.549 818.658 1.00107.75 O ANISOU 3898 OG1 THR A 551 15972 10860 14109 -1876 -4370 -791 O ATOM 3899 CG2 THR A 551 27.463 217.890 816.425 1.00 96.53 C ANISOU 3899 CG2 THR A 551 14160 9958 12560 -2035 -4465 -721 C ATOM 3900 N ASP A 552 25.737 219.926 820.189 1.00112.10 N ANISOU 3900 N ASP A 552 16638 11649 14307 -1607 -3712 -124 N ATOM 3901 CA ASP A 552 25.352 220.165 821.577 1.00117.00 C ANISOU 3901 CA ASP A 552 17396 12036 15021 -1557 -3595 97 C ATOM 3902 CB ASP A 552 26.105 221.363 822.153 1.00125.85 C ANISOU 3902 CB ASP A 552 18723 13059 16034 -1245 -3660 -179 C ATOM 3903 CG ASP A 552 25.649 221.712 823.557 1.00133.62 C ANISOU 3903 CG ASP A 552 19826 13814 17129 -1159 -3576 64 C ATOM 3904 OD1 ASP A 552 25.193 220.794 824.273 1.00137.69 O ANISOU 3904 OD1 ASP A 552 20330 14094 17893 -1390 -3566 396 O ATOM 3905 OD2 ASP A 552 25.742 222.898 823.944 1.00133.15 O ANISOU 3905 OD2 ASP A 552 19865 13813 16911 -872 -3524 -63 O ATOM 3906 C ASP A 552 23.852 220.404 821.691 1.00112.61 C ANISOU 3906 C ASP A 552 16776 11762 14250 -1554 -3297 466 C ATOM 3907 O ASP A 552 23.159 219.728 822.453 1.00116.38 O ANISOU 3907 O ASP A 552 17242 12102 14873 -1743 -3186 797 O ATOM 3908 N ILE A 553 23.363 221.381 820.933 1.00105.00 N ANISOU 3908 N ILE A 553 15781 11188 12925 -1351 -3171 403 N ATOM 3909 CA ILE A 553 21.937 221.696 820.889 1.00101.24 C ANISOU 3909 CA ILE A 553 15232 11001 12232 -1331 -2900 688 C ATOM 3910 CB ILE A 553 21.637 222.789 819.845 1.00 90.27 C ANISOU 3910 CB ILE A 553 13797 10005 10496 -1109 -2816 559 C ATOM 3911 CG2 ILE A 553 20.141 222.944 819.650 1.00 81.61 C ANISOU 3911 CG2 ILE A 553 12587 9185 9238 -1126 -2552 821 C ATOM 3912 CG1 ILE A 553 22.257 224.116 820.275 1.00 86.50 C ANISOU 3912 CG1 ILE A 553 13502 9519 9846 -817 -2851 351 C ATOM 3913 CD1 ILE A 553 22.238 225.163 819.199 1.00 85.33 C ANISOU 3913 CD1 ILE A 553 13331 9725 9366 -629 -2794 201 C ATOM 3914 C ILE A 553 21.114 220.462 820.550 1.00105.20 C ANISOU 3914 C ILE A 553 15530 11560 12879 -1631 -2773 931 C ATOM 3915 O ILE A 553 20.021 220.264 821.083 1.00114.42 O ANISOU 3915 O ILE A 553 16687 12797 13991 -1723 -2556 1218 O ATOM 3916 N PHE A 554 21.645 219.632 819.661 1.00103.16 N ANISOU 3916 N PHE A 554 15105 11284 12807 -1787 -2907 799 N ATOM 3917 CA PHE A 554 20.957 218.417 819.250 1.00 99.16 C ANISOU 3917 CA PHE A 554 14347 10827 12501 -2074 -2779 984 C ATOM 3918 CB PHE A 554 21.755 217.682 818.182 1.00 97.42 C ANISOU 3918 CB PHE A 554 13929 10577 12511 -2195 -3010 771 C ATOM 3919 CG PHE A 554 21.120 216.400 817.734 1.00102.08 C ANISOU 3919 CG PHE A 554 14203 11200 13383 -2492 -2879 929 C ATOM 3920 CD2 PHE A 554 21.210 215.257 818.509 1.00108.07 C ANISOU 3920 CD2 PHE A 554 14916 11671 14473 -2798 -2834 1094 C ATOM 3921 CE2 PHE A 554 20.627 214.074 818.100 1.00110.94 C ANISOU 3921 CE2 PHE A 554 14961 12081 15111 -3087 -2667 1227 C ATOM 3922 CZ PHE A 554 19.942 214.023 816.905 1.00110.19 C ANISOU 3922 CZ PHE A 554 14572 12303 14993 -3045 -2564 1176 C ATOM 3923 CE1 PHE A 554 19.842 215.156 816.123 1.00112.15 C ANISOU 3923 CE1 PHE A 554 14874 12809 14928 -2730 -2644 1028 C ATOM 3924 CD1 PHE A 554 20.428 216.338 816.539 1.00106.46 C ANISOU 3924 CD1 PHE A 554 14488 12060 13901 -2469 -2791 916 C ATOM 3925 C PHE A 554 20.719 217.486 820.426 1.00 99.09 C ANISOU 3925 C PHE A 554 14388 10535 12725 -2335 -2685 1256 C ATOM 3926 O PHE A 554 19.579 217.179 820.762 1.00101.54 O ANISOU 3926 O PHE A 554 14651 10974 12956 -2459 -2410 1530 O ATOM 3927 N LYS A 555 21.805 217.034 821.045 1.00103.02 N ANISOU 3927 N LYS A 555 14993 10643 13507 -2430 -2917 1177 N ATOM 3928 CA LYS A 555 21.725 216.037 822.110 1.00107.76 C ANISOU 3928 CA LYS A 555 15639 10917 14386 -2719 -2870 1460 C ATOM 3929 CB LYS A 555 23.124 215.687 822.633 1.00101.07 C ANISOU 3929 CB LYS A 555 14905 9598 13897 -2774 -3193 1286 C ATOM 3930 C LYS A 555 20.823 216.476 823.262 1.00110.35 C ANISOU 3930 C LYS A 555 16171 11257 14500 -2676 -2680 1785 C ATOM 3931 O LYS A 555 20.163 215.650 823.893 1.00120.73 O ANISOU 3931 O LYS A 555 17484 12502 15887 -2950 -2506 2122 O ATOM 3932 N ASN A 556 20.789 217.780 823.523 1.00 99.42 N ANISOU 3932 N ASN A 556 14958 9973 12842 -2345 -2716 1687 N ATOM 3933 CA ASN A 556 20.046 218.315 824.660 1.00105.20 C ANISOU 3933 CA ASN A 556 15892 10690 13390 -2271 -2617 1965 C ATOM 3934 CB ASN A 556 20.707 219.599 825.174 1.00105.55 C ANISOU 3934 CB ASN A 556 16121 10613 13371 -1916 -2804 1764 C ATOM 3935 CG ASN A 556 21.908 219.322 826.052 1.00111.77 C ANISOU 3935 CG ASN A 556 17049 10884 14535 -1930 -3082 1695 C ATOM 3936 OD1 ASN A 556 22.347 218.179 826.178 1.00111.47 O ANISOU 3936 OD1 ASN A 556 16970 10568 14815 -2210 -3163 1775 O ATOM 3937 ND2 ASN A 556 22.446 220.370 826.670 1.00111.68 N ANISOU 3937 ND2 ASN A 556 17183 10722 14529 -1629 -3224 1532 N ATOM 3938 C ASN A 556 18.561 218.578 824.410 1.00109.70 C ANISOU 3938 C ASN A 556 16398 11678 13604 -2274 -2309 2154 C ATOM 3939 O ASN A 556 17.744 218.459 825.325 1.00117.67 O ANISOU 3939 O ASN A 556 17538 12687 14486 -2377 -2188 2472 O ATOM 3940 N CYS A 557 18.209 218.939 823.181 1.00101.33 N ANISOU 3940 N CYS A 557 15151 10966 12383 -2164 -2199 1959 N ATOM 3941 CA CYS A 557 16.850 219.392 822.910 1.00 92.05 C ANISOU 3941 CA CYS A 557 13920 10166 10887 -2110 -1931 2068 C ATOM 3942 CB CYS A 557 16.872 220.802 822.315 1.00 88.49 C ANISOU 3942 CB CYS A 557 13480 9934 10208 -1760 -1974 1836 C ATOM 3943 SG CYS A 557 17.613 222.052 823.395 1.00103.14 S ANISOU 3943 SG CYS A 557 15601 11571 12014 -1464 -2189 1762 S ATOM 3944 C CYS A 557 16.054 218.456 822.005 1.00 91.96 C ANISOU 3944 C CYS A 557 13638 10389 10916 -2335 -1684 2110 C ATOM 3945 O CYS A 557 14.859 218.248 822.220 1.00 92.13 O ANISOU 3945 O CYS A 557 13639 10611 10756 -2449 -1413 2295 O ATOM 3946 N LEU A 558 16.718 217.890 821.003 1.00 83.99 N ANISOU 3946 N LEU A 558 12410 9351 10150 -2399 -1785 1918 N ATOM 3947 CA LEU A 558 16.029 217.124 819.968 1.00 75.05 C ANISOU 3947 CA LEU A 558 10956 8442 9117 -2556 -1581 1899 C ATOM 3948 CB LEU A 558 16.435 217.639 818.588 1.00 71.97 C ANISOU 3948 CB LEU A 558 10392 8207 8748 -2350 -1739 1620 C ATOM 3949 CG LEU A 558 16.491 219.165 818.466 1.00 78.11 C ANISOU 3949 CG LEU A 558 11348 9121 9210 -2002 -1827 1501 C ATOM 3950 CD2 LEU A 558 15.197 219.777 818.954 1.00 82.63 C ANISOU 3950 CD2 LEU A 558 11999 9895 9501 -1929 -1560 1658 C ATOM 3951 CD1 LEU A 558 16.779 219.599 817.041 1.00 76.67 C ANISOU 3951 CD1 LEU A 558 10999 9115 9020 -1841 -1961 1289 C ATOM 3952 C LEU A 558 16.264 215.617 820.055 1.00 90.81 C ANISOU 3952 C LEU A 558 12779 10256 11469 -2922 -1529 2004 C ATOM 3953 O LEU A 558 15.522 214.838 819.461 1.00 91.00 O ANISOU 3953 O LEU A 558 12523 10451 11599 -3101 -1283 2038 O ATOM 3954 N GLU A 559 17.264 215.294 820.850 1.00106.93 N ANISOU 3954 N GLU A 559 14987 11940 13700 -3016 -1748 2050 N ATOM 3955 CA GLU A 559 17.804 213.984 821.063 1.00112.18 C ANISOU 3955 CA GLU A 559 15534 12332 14756 -3354 -1786 2137 C ATOM 3956 CB GLU A 559 18.855 214.102 822.188 1.00117.07 C ANISOU 3956 CB GLU A 559 16451 12525 15507 -3348 -2065 2187 C ATOM 3957 CG GLU A 559 18.403 214.861 823.492 1.00190.25 C ANISOU 3957 CG GLU A 559 26066 21734 24486 -3228 -2021 2431 C ATOM 3958 CD GLU A 559 17.652 214.033 824.565 1.00191.73 C ANISOU 3958 CD GLU A 559 26363 21834 24653 -3553 -1799 2866 C ATOM 3959 OE2 GLU A 559 17.391 214.577 825.668 1.00190.53 O ANISOU 3959 OE2 GLU A 559 26502 21589 24304 -3472 -1839 3087 O ATOM 3960 OE1 GLU A 559 17.383 212.833 824.343 1.00193.35 O ANISOU 3960 OE1 GLU A 559 26366 22045 25053 -3899 -1603 2998 O ATOM 3961 C GLU A 559 16.625 213.139 821.487 1.00109.14 C ANISOU 3961 C GLU A 559 15068 12081 14320 -3652 -1388 2442 C ATOM 3962 O GLU A 559 16.484 211.987 821.102 1.00 93.87 O ANISOU 3962 O GLU A 559 12855 10145 12668 -3947 -1231 2487 O ATOM 3963 N ASN A 560 15.734 213.754 822.234 1.00121.72 N ANISOU 3963 N ASN A 560 16891 13823 15532 -3571 -1213 2632 N ATOM 3964 CA ASN A 560 14.558 213.077 822.709 1.00128.11 C ANISOU 3964 CA ASN A 560 17688 14806 16181 -3843 -824 2913 C ATOM 3965 C ASN A 560 13.804 212.712 821.486 1.00132.56 C ANISOU 3965 C ASN A 560 17873 15697 16795 -3876 -553 2738 C ATOM 3966 O ASN A 560 14.065 213.226 820.417 1.00139.97 O ANISOU 3966 O ASN A 560 18633 16738 17810 -3638 -697 2455 O ATOM 3967 CB ASN A 560 13.695 214.007 823.547 1.00122.67 C ANISOU 3967 CB ASN A 560 17309 14278 15022 -3689 -737 3077 C ATOM 3968 CG ASN A 560 12.816 214.892 822.713 1.00112.61 C ANISOU 3968 CG ASN A 560 15924 13385 13476 -3428 -595 2867 C ATOM 3969 OD1 ASN A 560 12.716 214.737 821.501 1.00109.63 O ANISOU 3969 OD1 ASN A 560 15232 13170 13253 -3379 -521 2634 O ATOM 3970 ND2 ASN A 560 12.163 215.827 823.363 1.00103.84 N ANISOU 3970 ND2 ASN A 560 15064 12401 11988 -3261 -578 2957 N ATOM 3971 N GLN A 561 12.895 211.776 821.634 1.00130.20 N ANISOU 3971 N GLN A 561 17442 15552 16477 -4184 -160 2908 N ATOM 3972 CA GLN A 561 12.154 211.308 820.501 1.00128.44 C ANISOU 3972 CA GLN A 561 16811 15612 16378 -4232 130 2725 C ATOM 3973 C GLN A 561 11.375 212.378 819.755 1.00131.75 C ANISOU 3973 C GLN A 561 17184 16340 16536 -3893 185 2508 C ATOM 3974 O GLN A 561 10.747 213.257 820.318 1.00134.56 O ANISOU 3974 O GLN A 561 17816 16830 16481 -3739 234 2577 O ATOM 3975 CB GLN A 561 11.194 210.190 820.934 1.00122.09 C ANISOU 3975 CB GLN A 561 15908 14956 15527 -4628 618 2941 C ATOM 3976 CG GLN A 561 10.061 210.633 821.843 1.00117.11 C ANISOU 3976 CG GLN A 561 15602 14555 14339 -4647 882 3142 C ATOM 3977 CD GLN A 561 8.873 211.155 821.079 1.00112.82 C ANISOU 3977 CD GLN A 561 14897 14400 13570 -4461 1154 2908 C ATOM 3978 OE1 GLN A 561 8.371 212.235 821.356 1.00 96.17 O ANISOU 3978 OE1 GLN A 561 13037 12426 11077 -4215 1089 2885 O ATOM 3979 NE2 GLN A 561 8.417 210.387 820.107 1.00114.19 N ANISOU 3979 NE2 GLN A 561 14627 14734 14024 -4576 1450 2719 N ATOM 3980 N PHE A 562 11.480 212.279 818.449 1.00123.50 N ANISOU 3980 N PHE A 562 15769 15376 15779 -3784 136 2248 N ATOM 3981 CA PHE A 562 10.735 213.025 817.488 1.00106.95 C ANISOU 3981 CA PHE A 562 13515 13541 13581 -3515 208 2036 C ATOM 3982 CB PHE A 562 11.569 214.113 816.895 1.00 92.85 C ANISOU 3982 CB PHE A 562 11816 11680 11783 -3172 -214 1873 C ATOM 3983 CG PHE A 562 12.692 213.618 816.088 1.00 96.19 C ANISOU 3983 CG PHE A 562 12011 11923 12612 -3194 -526 1738 C ATOM 3984 CD1 PHE A 562 13.975 214.011 816.356 1.00 92.30 C ANISOU 3984 CD1 PHE A 562 11743 11197 12128 -3102 -922 1706 C ATOM 3985 CE1 PHE A 562 15.010 213.555 815.611 1.00 90.65 C ANISOU 3985 CE1 PHE A 562 11345 10838 12262 -3133 -1234 1556 C ATOM 3986 CZ PHE A 562 14.773 212.705 814.585 1.00 97.26 C ANISOU 3986 CZ PHE A 562 11740 11745 13469 -3250 -1177 1461 C ATOM 3987 CE2 PHE A 562 13.502 212.309 814.307 1.00105.82 C ANISOU 3987 CE2 PHE A 562 12566 13045 14595 -3327 -771 1492 C ATOM 3988 CD2 PHE A 562 12.468 212.765 815.054 1.00103.77 C ANISOU 3988 CD2 PHE A 562 12520 12947 13960 -3302 -436 1618 C ATOM 3989 C PHE A 562 10.680 211.810 816.610 1.00110.04 C ANISOU 3989 C PHE A 562 13425 13946 14440 -3728 365 1932 C ATOM 3990 O PHE A 562 11.675 211.136 816.465 1.00110.17 O ANISOU 3990 O PHE A 562 13315 13735 14808 -3865 146 1929 O ATOM 3991 N GLU A 563 9.552 211.482 816.024 1.00107.28 N ANISOU 3991 N GLU A 563 12777 13841 14142 -3764 736 1824 N ATOM 3992 CA GLU A 563 9.524 210.231 815.309 1.00108.77 C ANISOU 3992 CA GLU A 563 12476 14021 14830 -3995 910 1733 C ATOM 3993 C GLU A 563 10.532 210.128 814.204 1.00104.06 C ANISOU 3993 C GLU A 563 11587 13260 14689 -3873 488 1561 C ATOM 3994 O GLU A 563 10.691 211.024 813.406 1.00106.89 O ANISOU 3994 O GLU A 563 11940 13655 15017 -3554 208 1416 O ATOM 3995 CB GLU A 563 8.123 209.940 814.836 1.00117.16 C ANISOU 3995 CB GLU A 563 13242 15372 15901 -4025 1397 1596 C ATOM 3996 CG GLU A 563 7.193 209.800 815.986 1.00125.05 C ANISOU 3996 CG GLU A 563 14529 16543 16441 -4231 1826 1774 C ATOM 3997 CD GLU A 563 5.985 209.008 815.632 1.00138.70 C ANISOU 3997 CD GLU A 563 15903 18529 18270 -4409 2390 1634 C ATOM 3998 OE1 GLU A 563 5.779 208.773 814.431 1.00143.49 O ANISOU 3998 OE1 GLU A 563 16031 19172 19315 -4294 2423 1371 O ATOM 3999 OE2 GLU A 563 5.242 208.617 816.550 1.00143.11 O ANISOU 3999 OE2 GLU A 563 16655 19251 18468 -4665 2798 1783 O ATOM 4000 N ILE A 564 11.222 208.999 814.161 1.00104.26 N ANISOU 4000 N ILE A 564 11369 13104 15142 -4150 434 1591 N ATOM 4001 CA ILE A 564 12.262 208.821 813.150 1.00104.67 C ANISOU 4001 CA ILE A 564 11151 12988 15630 -4066 -23 1426 C ATOM 4002 CB ILE A 564 13.035 207.504 813.349 1.00 94.48 C ANISOU 4002 CB ILE A 564 9627 11464 14809 -4434 -69 1483 C ATOM 4003 CG2 ILE A 564 14.329 207.533 812.559 1.00 79.53 C ANISOU 4003 CG2 ILE A 564 7615 9364 13239 -4331 -658 1323 C ATOM 4004 CG1 ILE A 564 13.307 207.264 814.833 1.00 99.73 C ANISOU 4004 CG1 ILE A 564 10697 11967 15230 -4685 51 1756 C ATOM 4005 CD1 ILE A 564 14.040 208.392 815.510 1.00 96.21 C ANISOU 4005 CD1 ILE A 564 10792 11381 14381 -4453 -313 1814 C ATOM 4006 C ILE A 564 11.685 208.823 811.745 1.00113.46 C ANISOU 4006 C ILE A 564 11797 14260 17052 -3887 -10 1203 C ATOM 4007 O ILE A 564 12.285 209.364 810.814 1.00113.62 O ANISOU 4007 O ILE A 564 11750 14233 17185 -3642 -446 1073 O ATOM 4008 N THR A 565 10.518 208.208 811.596 1.00121.38 N ANISOU 4008 N THR A 565 12480 15447 18193 -4014 492 1159 N ATOM 4009 CA THR A 565 9.845 208.149 810.305 1.00127.38 C ANISOU 4009 CA THR A 565 12755 16332 19312 -3843 552 935 C ATOM 4010 C THR A 565 9.642 209.545 809.706 1.00122.28 C ANISOU 4010 C THR A 565 12310 15767 18384 -3427 291 858 C ATOM 4011 O THR A 565 9.752 209.730 808.493 1.00119.09 O ANISOU 4011 O THR A 565 11601 15341 18307 -3221 9 718 O ATOM 4012 CB THR A 565 8.496 207.412 810.415 1.00132.78 C ANISOU 4012 CB THR A 565 13133 17225 20094 -4026 1215 868 C ATOM 4013 CG2 THR A 565 7.793 207.785 811.711 1.00133.18 C ANISOU 4013 CG2 THR A 565 13668 17427 19506 -4125 1598 1036 C ATOM 4014 OG1 THR A 565 7.662 207.761 809.302 1.00132.31 O ANISOU 4014 OG1 THR A 565 12729 17290 20252 -3761 1281 637 O ATOM 4015 N ASN A 566 9.357 210.524 810.561 1.00119.09 N ANISOU 4015 N ASN A 566 12410 15445 17392 -3314 369 968 N ATOM 4016 CA ASN A 566 9.154 211.903 810.115 1.00114.21 C ANISOU 4016 CA ASN A 566 12009 14901 16484 -2949 156 918 C ATOM 4017 CB ASN A 566 8.558 212.752 811.240 1.00104.13 C ANISOU 4017 CB ASN A 566 11215 13743 14607 -2901 381 1033 C ATOM 4018 CG ASN A 566 7.048 212.656 811.300 1.00103.82 C ANISOU 4018 CG ASN A 566 11042 13923 14480 -2928 894 942 C ATOM 4019 ND2 ASN A 566 6.483 212.918 812.473 1.00100.76 N ANISOU 4019 ND2 ASN A 566 11022 13647 13615 -3024 1163 1062 N ATOM 4020 OD1 ASN A 566 6.393 212.356 810.302 1.00105.12 O ANISOU 4020 OD1 ASN A 566 10778 14152 15012 -2859 1030 754 O ATOM 4021 C ASN A 566 10.429 212.560 809.594 1.00114.67 C ANISOU 4021 C ASN A 566 12221 14812 16538 -2757 -439 923 C ATOM 4022 O ASN A 566 10.429 213.186 808.533 1.00113.02 O ANISOU 4022 O ASN A 566 11890 14628 16425 -2505 -695 838 O ATOM 4023 N LEU A 567 11.513 212.417 810.347 1.00112.58 N ANISOU 4023 N LEU A 567 12234 14390 16153 -2884 -658 1023 N ATOM 4024 CA LEU A 567 12.800 212.968 809.941 1.00 99.25 C ANISOU 4024 CA LEU A 567 10716 12571 14423 -2735 -1199 989 C ATOM 4025 CB LEU A 567 13.883 212.635 810.968 1.00 95.60 C ANISOU 4025 CB LEU A 567 10541 11904 13878 -2922 -1351 1067 C ATOM 4026 CG LEU A 567 15.325 212.919 810.544 1.00 91.54 C ANISOU 4026 CG LEU A 567 10151 11237 13391 -2832 -1901 969 C ATOM 4027 CD1 LEU A 567 16.196 213.228 811.742 1.00 87.51 C ANISOU 4027 CD1 LEU A 567 10089 10554 12608 -2878 -2010 1027 C ATOM 4028 CD2 LEU A 567 15.900 211.753 809.758 1.00 92.57 C ANISOU 4028 CD2 LEU A 567 9854 11244 14073 -3021 -2129 869 C ATOM 4029 C LEU A 567 13.208 212.473 808.560 1.00 92.99 C ANISOU 4029 C LEU A 567 9489 11732 14111 -2699 -1523 859 C ATOM 4030 O LEU A 567 13.746 213.234 807.759 1.00 91.67 O ANISOU 4030 O LEU A 567 9398 11573 13859 -2471 -1920 813 O ATOM 4031 N LYS A 568 12.968 211.194 808.278 1.00 93.02 N ANISOU 4031 N LYS A 568 9031 11690 14621 -2933 -1363 811 N ATOM 4032 CA LYS A 568 13.321 210.668 806.968 1.00 90.92 C ANISOU 4032 CA LYS A 568 8303 11367 14877 -2901 -1698 689 C ATOM 4033 C LYS A 568 12.620 211.457 805.878 1.00 91.82 C ANISOU 4033 C LYS A 568 8274 11606 15007 -2590 -1775 637 C ATOM 4034 O LYS A 568 13.272 212.005 804.990 1.00 90.50 O ANISOU 4034 O LYS A 568 8136 11409 14839 -2400 -2262 620 O ATOM 4035 CB LYS A 568 13.046 209.171 806.825 1.00 84.22 C ANISOU 4035 CB LYS A 568 6910 10458 14632 -3199 -1459 631 C ATOM 4036 CG LYS A 568 13.163 208.708 805.379 1.00 78.19 C ANISOU 4036 CG LYS A 568 5596 9652 14460 -3117 -1786 496 C ATOM 4037 CD LYS A 568 14.012 207.470 805.241 1.00 82.65 C ANISOU 4037 CD LYS A 568 5813 10038 15554 -3401 -2000 442 C ATOM 4038 CE LYS A 568 14.435 207.260 803.794 1.00 97.90 C ANISOU 4038 CE LYS A 568 7309 11906 17985 -3270 -2529 326 C ATOM 4039 NZ LYS A 568 14.937 205.872 803.540 1.00 98.76 N ANISOU 4039 NZ LYS A 568 6898 11856 18769 -3566 -2645 240 N ATOM 4040 N ILE A 569 11.294 211.516 805.956 1.00 92.77 N ANISOU 4040 N ILE A 569 8257 11862 15130 -2549 -1298 613 N ATOM 4041 CA ILE A 569 10.514 212.339 805.045 1.00 91.22 C ANISOU 4041 CA ILE A 569 7959 11754 14948 -2253 -1326 567 C ATOM 4042 CB ILE A 569 9.080 212.580 805.564 1.00 85.98 C ANISOU 4042 CB ILE A 569 7320 11244 14103 -2231 -746 527 C ATOM 4043 CG2 ILE A 569 8.351 213.567 804.672 1.00 75.11 C ANISOU 4043 CG2 ILE A 569 5893 9915 12730 -1916 -819 482 C ATOM 4044 CG1 ILE A 569 8.293 211.269 805.617 1.00 96.06 C ANISOU 4044 CG1 ILE A 569 8117 12556 15827 -2469 -276 403 C ATOM 4045 CD1 ILE A 569 7.791 210.808 804.265 1.00108.08 C ANISOU 4045 CD1 ILE A 569 9021 14035 18010 -2351 -330 232 C ATOM 4046 C ILE A 569 11.216 213.678 804.875 1.00 83.86 C ANISOU 4046 C ILE A 569 7480 10826 13557 -2009 -1744 661 C ATOM 4047 O ILE A 569 11.413 214.145 803.756 1.00 78.41 O ANISOU 4047 O ILE A 569 6676 10115 13002 -1807 -2116 663 O ATOM 4048 N LEU A 570 11.621 214.275 805.991 1.00 85.34 N ANISOU 4048 N LEU A 570 8174 11036 13216 -2037 -1685 748 N ATOM 4049 CA LEU A 570 12.268 215.582 805.955 1.00 90.04 C ANISOU 4049 CA LEU A 570 9207 11656 13349 -1819 -2001 817 C ATOM 4050 CB LEU A 570 12.568 216.081 807.367 1.00 91.61 C ANISOU 4050 CB LEU A 570 9896 11862 13051 -1874 -1846 887 C ATOM 4051 CG LEU A 570 12.947 217.561 807.447 1.00 94.81 C ANISOU 4051 CG LEU A 570 10727 12330 12965 -1632 -2031 939 C ATOM 4052 CD1 LEU A 570 14.369 217.793 806.986 1.00 96.94 C ANISOU 4052 CD1 LEU A 570 11150 12531 13150 -1586 -2526 906 C ATOM 4053 CD2 LEU A 570 11.985 218.408 806.628 1.00 95.66 C ANISOU 4053 CD2 LEU A 570 10738 12553 13055 -1407 -1961 958 C ATOM 4054 C LEU A 570 13.541 215.587 805.115 1.00101.37 C ANISOU 4054 C LEU A 570 10634 13007 14875 -1774 -2578 800 C ATOM 4055 O LEU A 570 13.707 216.435 804.241 1.00110.91 O ANISOU 4055 O LEU A 570 11913 14263 15964 -1560 -2874 838 O ATOM 4056 N PHE A 571 14.442 214.650 805.380 1.00103.99 N ANISOU 4056 N PHE A 571 10895 13213 15404 -1990 -2748 748 N ATOM 4057 CA PHE A 571 15.710 214.606 804.660 1.00106.61 C ANISOU 4057 CA PHE A 571 11248 13470 15789 -1974 -3319 698 C ATOM 4058 C PHE A 571 15.517 214.300 803.178 1.00108.98 C ANISOU 4058 C PHE A 571 11106 13772 16530 -1882 -3623 681 C ATOM 4059 O PHE A 571 16.092 214.970 802.322 1.00105.83 O ANISOU 4059 O PHE A 571 10829 13410 15970 -1718 -4065 715 O ATOM 4060 CB PHE A 571 16.657 213.592 805.300 1.00106.11 C ANISOU 4060 CB PHE A 571 11171 13240 15907 -2248 -3428 621 C ATOM 4061 CG PHE A 571 17.871 213.284 804.477 1.00 99.42 C ANISOU 4061 CG PHE A 571 10246 12307 15222 -2277 -4022 523 C ATOM 4062 CD2 PHE A 571 18.831 214.253 804.247 1.00102.13 C ANISOU 4062 CD2 PHE A 571 10995 12700 15108 -2121 -4412 492 C ATOM 4063 CE2 PHE A 571 19.954 213.970 803.489 1.00108.20 C ANISOU 4063 CE2 PHE A 571 11723 13415 15971 -2160 -4979 384 C ATOM 4064 CZ PHE A 571 20.127 212.707 802.951 1.00102.94 C ANISOU 4064 CZ PHE A 571 10579 12622 15911 -2352 -5189 312 C ATOM 4065 CE1 PHE A 571 19.178 211.736 803.176 1.00 98.81 C ANISOU 4065 CE1 PHE A 571 9613 12036 15895 -2506 -4784 345 C ATOM 4066 CD1 PHE A 571 18.055 212.027 803.936 1.00 94.18 C ANISOU 4066 CD1 PHE A 571 9097 11525 15161 -2471 -4189 447 C ATOM 4067 N ASP A 572 14.705 213.290 802.882 1.00115.87 N ANISOU 4067 N ASP A 572 11461 14604 17960 -1991 -3385 634 N ATOM 4068 CA ASP A 572 14.423 212.919 801.497 1.00117.99 C ANISOU 4068 CA ASP A 572 11235 14840 18755 -1894 -3657 609 C ATOM 4069 CB ASP A 572 13.445 211.740 801.427 1.00121.09 C ANISOU 4069 CB ASP A 572 11041 15192 19777 -2040 -3252 512 C ATOM 4070 CG ASP A 572 14.152 210.390 801.439 1.00131.54 C ANISOU 4070 CG ASP A 572 12010 16382 21586 -2321 -3403 420 C ATOM 4071 OD1 ASP A 572 15.400 210.368 801.377 1.00136.11 O ANISOU 4071 OD1 ASP A 572 12780 16885 22050 -2383 -3888 417 O ATOM 4072 OD2 ASP A 572 13.462 209.348 801.503 1.00133.77 O ANISOU 4072 OD2 ASP A 572 11814 16638 22374 -2489 -3029 334 O ATOM 4073 C ASP A 572 13.891 214.106 800.700 1.00111.28 C ANISOU 4073 C ASP A 572 10501 14075 17704 -1588 -3773 712 C ATOM 4074 O ASP A 572 14.254 214.301 799.538 1.00116.37 O ANISOU 4074 O ASP A 572 11014 14690 18512 -1456 -4262 766 O ATOM 4075 N GLU A 573 13.039 214.908 801.325 1.00 97.34 N ANISOU 4075 N GLU A 573 8991 12408 15586 -1487 -3347 756 N ATOM 4076 CA GLU A 573 12.470 216.058 800.637 1.00 91.17 C ANISOU 4076 CA GLU A 573 8317 11684 14638 -1219 -3417 860 C ATOM 4077 CB GLU A 573 11.264 216.613 801.398 1.00 87.49 C ANISOU 4077 CB GLU A 573 7984 11305 13953 -1161 -2851 847 C ATOM 4078 CG GLU A 573 10.023 215.731 801.283 1.00 98.18 C ANISOU 4078 CG GLU A 573 8837 12633 15832 -1220 -2427 708 C ATOM 4079 CD GLU A 573 8.810 216.316 801.987 1.00101.60 C ANISOU 4079 CD GLU A 573 9425 13168 16012 -1164 -1902 668 C ATOM 4080 OE1 GLU A 573 8.857 217.503 802.366 1.00 91.04 O ANISOU 4080 OE1 GLU A 573 8527 11898 14166 -1040 -1921 771 O ATOM 4081 OE2 GLU A 573 7.807 215.592 802.158 1.00110.58 O ANISOU 4081 OE2 GLU A 573 10236 14325 17453 -1251 -1466 519 O ATOM 4082 C GLU A 573 13.516 217.138 800.378 1.00 86.92 C ANISOU 4082 C GLU A 573 8245 11202 13580 -1097 -3861 986 C ATOM 4083 O GLU A 573 13.544 217.725 799.296 1.00 86.16 O ANISOU 4083 O GLU A 573 8117 11104 13516 -923 -4204 1104 O ATOM 4084 N LEU A 574 14.386 217.381 801.355 1.00 81.20 N ANISOU 4084 N LEU A 574 7946 10518 12389 -1193 -3853 962 N ATOM 4085 CA LEU A 574 15.426 218.403 801.219 1.00 79.22 C ANISOU 4085 CA LEU A 574 8154 10344 11602 -1094 -4209 1032 C ATOM 4086 CB LEU A 574 16.183 218.599 802.532 1.00 79.89 C ANISOU 4086 CB LEU A 574 8661 10443 11249 -1197 -4067 951 C ATOM 4087 CG LEU A 574 15.736 219.767 803.414 1.00 86.27 C ANISOU 4087 CG LEU A 574 9851 11350 11577 -1080 -3710 1008 C ATOM 4088 CD2 LEU A 574 16.685 219.946 804.594 1.00 82.05 C ANISOU 4088 CD2 LEU A 574 9710 10793 10671 -1160 -3679 917 C ATOM 4089 CD1 LEU A 574 14.307 219.565 803.890 1.00 90.97 C ANISOU 4089 CD1 LEU A 574 10241 11947 12376 -1088 -3211 1024 C ATOM 4090 C LEU A 574 16.416 218.124 800.087 1.00 89.65 C ANISOU 4090 C LEU A 574 9378 11636 13048 -1095 -4832 1048 C ATOM 4091 O LEU A 574 17.096 219.035 799.611 1.00 99.19 O ANISOU 4091 O LEU A 574 10913 12940 13835 -985 -5156 1138 O ATOM 4092 N ASN A 575 16.500 216.872 799.657 1.00 87.30 N ANISOU 4092 N ASN A 575 8632 11220 13318 -1231 -5001 963 N ATOM 4093 CA ASN A 575 17.400 216.524 798.565 1.00103.60 C ANISOU 4093 CA ASN A 575 10563 13249 15550 -1242 -5641 973 C ATOM 4094 CB ASN A 575 17.689 215.020 798.553 1.00112.41 C ANISOU 4094 CB ASN A 575 11226 14217 17265 -1465 -5755 818 C ATOM 4095 CG ASN A 575 18.436 214.560 799.795 1.00109.40 C ANISOU 4095 CG ASN A 575 11078 13788 16700 -1686 -5593 664 C ATOM 4096 OD1 ASN A 575 18.460 215.254 800.815 1.00103.88 O ANISOU 4096 OD1 ASN A 575 10808 13149 15512 -1666 -5273 666 O ATOM 4097 ND2 ASN A 575 19.047 213.384 799.715 1.00103.84 N ANISOU 4097 ND2 ASN A 575 10074 12950 16430 -1899 -5830 533 N ATOM 4098 C ASN A 575 16.868 216.983 797.210 1.00112.42 C ANISOU 4098 C ASN A 575 11478 14373 16863 -1038 -5927 1157 C ATOM 4099 O ASN A 575 17.536 216.840 796.185 1.00116.72 O ANISOU 4099 O ASN A 575 11936 14902 17511 -1018 -6512 1221 O ATOM 4100 N SER A 576 15.672 217.548 797.214 1.00119.61 N ANISOU 4100 N SER A 576 12325 15295 17825 -891 -5540 1247 N ATOM 4101 CA SER A 576 15.046 218.029 795.993 1.00123.55 C ANISOU 4101 CA SER A 576 12628 15753 18563 -690 -5767 1432 C ATOM 4102 C SER A 576 15.202 219.519 795.756 1.00114.66 C ANISOU 4102 C SER A 576 11991 14750 16825 -531 -5869 1648 C ATOM 4103 O SER A 576 14.622 220.043 794.823 1.00103.38 O ANISOU 4103 O SER A 576 10449 13269 15562 -367 -6019 1839 O ATOM 4104 CB SER A 576 13.557 217.701 796.004 1.00125.46 C ANISOU 4104 CB SER A 576 12439 15897 19333 -621 -5293 1373 C ATOM 4105 OG SER A 576 13.306 216.449 796.605 1.00127.00 O ANISOU 4105 OG SER A 576 12273 16033 19948 -805 -4984 1155 O ATOM 4106 N PHE A 577 15.968 220.207 796.590 1.00114.56 N ANISOU 4106 N PHE A 577 12503 14884 16141 -580 -5778 1619 N ATOM 4107 CA PHE A 577 16.141 221.645 796.421 1.00111.33 C ANISOU 4107 CA PHE A 577 12578 14576 15146 -460 -5764 1803 C ATOM 4108 C PHE A 577 17.566 222.117 796.322 1.00107.32 C ANISOU 4108 C PHE A 577 12550 14159 14065 -527 -6060 1804 C ATOM 4109 O PHE A 577 18.438 221.592 796.976 1.00111.38 O ANISOU 4109 O PHE A 577 13176 14709 14434 -656 -6131 1607 O ATOM 4110 CB PHE A 577 15.559 222.391 797.617 1.00110.44 C ANISOU 4110 CB PHE A 577 12731 14525 14706 -435 -5160 1744 C ATOM 4111 CG PHE A 577 14.162 222.026 797.950 1.00110.74 C ANISOU 4111 CG PHE A 577 12391 14503 15184 -391 -4769 1692 C ATOM 4112 CD2 PHE A 577 13.124 222.816 797.561 1.00106.40 C ANISOU 4112 CD2 PHE A 577 11791 13926 14712 -237 -4595 1827 C ATOM 4113 CE2 PHE A 577 11.849 222.483 797.876 1.00100.98 C ANISOU 4113 CE2 PHE A 577 10804 13154 14409 -213 -4170 1721 C ATOM 4114 CZ PHE A 577 11.594 221.360 798.581 1.00 94.98 C ANISOU 4114 CZ PHE A 577 9802 12361 13926 -355 -3894 1506 C ATOM 4115 CE1 PHE A 577 12.605 220.571 798.977 1.00102.62 C ANISOU 4115 CE1 PHE A 577 10810 13345 14835 -520 -4053 1410 C ATOM 4116 CD1 PHE A 577 13.887 220.901 798.672 1.00112.12 C ANISOU 4116 CD1 PHE A 577 12305 14608 15686 -533 -4497 1488 C ATOM 4117 N ASP A 578 17.793 223.135 795.513 1.00 96.27 N ANISOU 4117 N ASP A 578 11435 12803 12341 -450 -6222 2019 N ATOM 4118 CA ASP A 578 19.113 223.681 795.370 1.00 94.72 C ANISOU 4118 CA ASP A 578 11699 12736 11553 -513 -6470 2011 C ATOM 4119 CB ASP A 578 19.190 224.514 794.109 1.00 97.37 C ANISOU 4119 CB ASP A 578 12184 13109 11704 -448 -6787 2319 C ATOM 4120 CG ASP A 578 20.568 225.032 793.844 1.00101.87 C ANISOU 4120 CG ASP A 578 13217 13856 11633 -527 -7086 2314 C ATOM 4121 OD1 ASP A 578 21.309 225.261 794.801 1.00105.39 O ANISOU 4121 OD1 ASP A 578 13969 14405 11667 -587 -6845 2076 O ATOM 4122 OD2 ASP A 578 20.919 225.218 792.676 1.00 94.98 O ANISOU 4122 OD2 ASP A 578 12403 13022 10663 -526 -7575 2548 O ATOM 4123 C ASP A 578 19.016 224.560 796.571 1.00 96.96 C ANISOU 4123 C ASP A 578 12318 13092 11430 -502 -5881 1899 C ATOM 4124 O ASP A 578 18.677 225.712 796.482 1.00103.27 O ANISOU 4124 O ASP A 578 13330 13942 11966 -432 -5628 2038 O ATOM 4125 N ILE A 579 19.322 224.002 797.721 1.00 94.14 N ANISOU 4125 N ILE A 579 11982 12726 11061 -580 -5679 1648 N ATOM 4126 CA ILE A 579 19.224 224.729 798.961 1.00 90.02 C ANISOU 4126 CA ILE A 579 11733 12241 10231 -561 -5148 1531 C ATOM 4127 CB ILE A 579 19.655 223.850 800.096 1.00 95.18 C ANISOU 4127 CB ILE A 579 12360 12847 10957 -667 -5076 1284 C ATOM 4128 CG2 ILE A 579 19.930 224.686 801.293 1.00 92.90 C ANISOU 4128 CG2 ILE A 579 12422 12589 10287 -640 -4656 1159 C ATOM 4129 CG1 ILE A 579 18.569 222.838 800.411 1.00 90.29 C ANISOU 4129 CG1 ILE A 579 11291 12139 10877 -704 -4941 1279 C ATOM 4130 CD1 ILE A 579 18.981 221.854 801.409 1.00 82.05 C ANISOU 4130 CD1 ILE A 579 10169 11046 9959 -856 -4934 1074 C ATOM 4131 C ILE A 579 20.043 225.967 799.080 1.00 88.73 C ANISOU 4131 C ILE A 579 12028 12205 9482 -534 -5041 1517 C ATOM 4132 O ILE A 579 19.590 226.957 799.597 1.00 97.02 O ANISOU 4132 O ILE A 579 13217 13284 10362 -468 -4616 1540 O ATOM 4133 N PRO A 580 21.248 225.933 798.593 1.00 83.33 N ANISOU 4133 N PRO A 580 11558 11610 8492 -589 -5432 1463 N ATOM 4134 CD PRO A 580 21.817 224.928 797.703 1.00 85.53 C ANISOU 4134 CD PRO A 580 11674 11871 8954 -667 -6033 1469 C ATOM 4135 CG PRO A 580 22.841 225.700 796.982 1.00 90.91 C ANISOU 4135 CG PRO A 580 12729 12726 9088 -678 -6321 1527 C ATOM 4136 CB PRO A 580 23.313 226.708 797.898 1.00 85.76 C ANISOU 4136 CB PRO A 580 12448 12181 7956 -649 -5900 1376 C ATOM 4137 CA PRO A 580 22.089 227.107 798.695 1.00 88.18 C ANISOU 4137 CA PRO A 580 12600 12387 8519 -567 -5325 1424 C ATOM 4138 C PRO A 580 21.398 228.265 798.029 1.00 97.71 C ANISOU 4138 C PRO A 580 13853 13661 9612 -491 -5153 1699 C ATOM 4139 O PRO A 580 21.512 229.383 798.487 1.00 97.12 O ANISOU 4139 O PRO A 580 14010 13685 9207 -450 -4804 1674 O ATOM 4140 N VAL A 581 20.692 228.002 796.950 1.00 99.71 N ANISOU 4140 N VAL A 581 13861 13849 10175 -472 -5415 1956 N ATOM 4141 CA VAL A 581 19.981 229.042 796.212 1.00 95.27 C ANISOU 4141 CA VAL A 581 13316 13315 9568 -412 -5316 2250 C ATOM 4142 CB VAL A 581 19.721 228.615 794.747 1.00 96.56 C ANISOU 4142 CB VAL A 581 13277 13412 9999 -405 -5857 2548 C ATOM 4143 CG2 VAL A 581 20.987 228.782 793.921 1.00102.32 C ANISOU 4143 CG2 VAL A 581 14314 14313 10249 -481 -6356 2638 C ATOM 4144 CG1 VAL A 581 18.565 229.407 794.144 1.00 88.16 C ANISOU 4144 CG1 VAL A 581 12086 12270 9142 -326 -5709 2843 C ATOM 4145 C VAL A 581 18.683 229.518 796.877 1.00 86.00 C ANISOU 4145 C VAL A 581 11969 12042 8664 -338 -4784 2256 C ATOM 4146 O VAL A 581 18.435 230.719 796.939 1.00 89.58 O ANISOU 4146 O VAL A 581 12574 12569 8892 -307 -4499 2349 O ATOM 4147 N VAL A 582 17.859 228.594 797.374 1.00 84.88 N ANISOU 4147 N VAL A 582 11508 11752 8991 -318 -4659 2153 N ATOM 4148 CA VAL A 582 16.586 228.986 797.993 1.00 85.76 C ANISOU 4148 CA VAL A 582 11465 11788 9333 -255 -4192 2143 C ATOM 4149 CB VAL A 582 15.612 227.800 798.211 1.00 85.59 C ANISOU 4149 CB VAL A 582 11044 11628 9847 -237 -4165 2079 C ATOM 4150 CG2 VAL A 582 15.878 227.117 799.542 1.00 82.77 C ANISOU 4150 CG2 VAL A 582 10713 11277 9460 -300 -3943 1822 C ATOM 4151 CG1 VAL A 582 15.706 226.812 797.065 1.00 85.38 C ANISOU 4151 CG1 VAL A 582 10732 11525 10184 -235 -4688 2196 C ATOM 4152 C VAL A 582 16.817 229.706 799.317 1.00 82.30 C ANISOU 4152 C VAL A 582 11257 11418 8595 -258 -3729 1939 C ATOM 4153 O VAL A 582 15.989 230.507 799.751 1.00 87.42 O ANISOU 4153 O VAL A 582 11881 12057 9277 -210 -3358 1949 O ATOM 4154 N LEU A 583 17.943 229.422 799.960 1.00 76.67 N ANISOU 4154 N LEU A 583 10747 10759 7624 -307 -3781 1744 N ATOM 4155 CA LEU A 583 18.331 230.193 801.128 1.00 77.52 C ANISOU 4155 CA LEU A 583 11075 10918 7462 -284 -3410 1561 C ATOM 4156 CB LEU A 583 19.512 229.551 801.857 1.00 79.23 C ANISOU 4156 CB LEU A 583 11458 11136 7512 -333 -3534 1327 C ATOM 4157 CG LEU A 583 19.157 228.436 802.844 1.00 70.30 C ANISOU 4157 CG LEU A 583 10159 9865 6688 -377 -3446 1190 C ATOM 4158 CD2 LEU A 583 17.913 228.802 803.616 1.00 62.82 C ANISOU 4158 CD2 LEU A 583 9075 8856 5938 -329 -3011 1210 C ATOM 4159 CD1 LEU A 583 20.311 228.180 803.799 1.00 71.78 C ANISOU 4159 CD1 LEU A 583 10564 10035 6674 -409 -3483 951 C ATOM 4160 C LEU A 583 18.654 231.625 800.703 1.00 78.99 C ANISOU 4160 C LEU A 583 11477 11250 7285 -247 -3317 1666 C ATOM 4161 O LEU A 583 18.047 232.566 801.195 1.00 82.61 O ANISOU 4161 O LEU A 583 11921 11719 7749 -193 -2956 1667 O ATOM 4162 N ASN A 584 19.594 231.789 799.775 1.00 82.35 N ANISOU 4162 N ASN A 584 12096 11804 7389 -286 -3663 1764 N ATOM 4163 CA ASN A 584 19.918 233.119 799.269 1.00 87.58 C ANISOU 4163 CA ASN A 584 12975 12642 7658 -275 -3598 1910 C ATOM 4164 CB ASN A 584 20.885 233.039 798.091 1.00 94.00 C ANISOU 4164 CB ASN A 584 13997 13603 8115 -346 -4077 2061 C ATOM 4165 CG ASN A 584 22.325 233.167 798.524 1.00105.94 C ANISOU 4165 CG ASN A 584 15837 15288 9126 -376 -4136 1820 C ATOM 4166 ND2 ASN A 584 22.728 234.382 798.873 1.00103.70 N ANISOU 4166 ND2 ASN A 584 15774 15180 8446 -351 -3840 1779 N ATOM 4167 OD1 ASN A 584 23.065 232.184 798.561 1.00115.54 O ANISOU 4167 OD1 ASN A 584 17096 16481 10325 -422 -4448 1654 O ATOM 4168 C ASN A 584 18.689 233.934 798.888 1.00 92.84 C ANISOU 4168 C ASN A 584 13476 13266 8531 -237 -3387 2139 C ATOM 4169 O ASN A 584 18.674 235.154 799.033 1.00104.88 O ANISOU 4169 O ASN A 584 15115 14903 9830 -216 -3134 2190 O ATOM 4170 N ASP A 585 17.656 233.258 798.406 1.00 86.02 N ANISOU 4170 N ASP A 585 12330 12241 8114 -226 -3501 2267 N ATOM 4171 CA ASP A 585 16.406 233.931 798.093 1.00 89.10 C ANISOU 4171 CA ASP A 585 12542 12558 8755 -184 -3317 2450 C ATOM 4172 C ASP A 585 15.658 234.269 799.384 1.00 85.93 C ANISOU 4172 C ASP A 585 12037 12105 8508 -135 -2834 2233 C ATOM 4173 O ASP A 585 15.052 235.336 799.504 1.00 87.77 O ANISOU 4173 O ASP A 585 12249 12361 8737 -104 -2583 2299 O ATOM 4174 CB ASP A 585 15.542 233.064 797.179 1.00 93.90 C ANISOU 4174 CB ASP A 585 12863 12997 9818 -164 -3608 2630 C ATOM 4175 CG ASP A 585 14.375 233.825 796.585 1.00 95.78 C ANISOU 4175 CG ASP A 585 12951 13148 10294 -117 -3521 2866 C ATOM 4176 OD1 ASP A 585 14.392 235.072 796.627 1.00 89.39 O ANISOU 4176 OD1 ASP A 585 12293 12437 9234 -127 -3321 2959 O ATOM 4177 OD2 ASP A 585 13.441 233.174 796.072 1.00102.83 O ANISOU 4177 OD2 ASP A 585 13558 13866 11649 -65 -3662 2956 O ATOM 4178 N LEU A 586 15.717 233.359 800.350 1.00 78.79 N ANISOU 4178 N LEU A 586 11069 11131 7737 -135 -2736 1990 N ATOM 4179 CA LEU A 586 15.040 233.557 801.629 1.00 65.28 C ANISOU 4179 CA LEU A 586 9273 9366 6163 -97 -2336 1796 C ATOM 4180 C LEU A 586 15.720 234.645 802.450 1.00 57.78 C ANISOU 4180 C LEU A 586 8521 8519 4914 -60 -2095 1669 C ATOM 4181 O LEU A 586 15.047 235.420 803.121 1.00 57.86 O ANISOU 4181 O LEU A 586 8459 8519 5007 -10 -1799 1615 O ATOM 4182 CB LEU A 586 15.003 232.254 802.436 1.00 62.48 C ANISOU 4182 CB LEU A 586 8828 8916 5996 -127 -2334 1620 C ATOM 4183 CG LEU A 586 13.800 231.999 803.357 1.00 62.04 C ANISOU 4183 CG LEU A 586 8588 8779 6205 -110 -2035 1522 C ATOM 4184 CD2 LEU A 586 13.202 233.284 803.902 1.00 48.78 C ANISOU 4184 CD2 LEU A 586 6917 7129 4489 -50 -1718 1488 C ATOM 4185 CD1 LEU A 586 14.185 231.074 804.505 1.00 55.83 C ANISOU 4185 CD1 LEU A 586 7838 7943 5434 -154 -1980 1343 C ATOM 4186 N ILE A 587 17.035 234.634 802.458 1.00 69.78 N ANISOU 4186 N ILE A 587 10272 10133 6108 -77 -2240 1601 N ATOM 4187 CA ILE A 587 17.792 235.581 803.241 1.00 76.24 C ANISOU 4187 CA ILE A 587 11274 11055 6640 -24 -2036 1462 C ATOM 4188 CB ILE A 587 19.137 234.978 803.569 1.00 73.04 C ANISOU 4188 CB ILE A 587 11082 10686 5984 -42 -2213 1286 C ATOM 4189 CG2 ILE A 587 19.643 235.515 804.848 1.00 49.98 C ANISOU 4189 CG2 ILE A 587 8263 7772 2955 39 -1966 1065 C ATOM 4190 CG1 ILE A 587 19.021 233.473 803.655 1.00 68.49 C ANISOU 4190 CG1 ILE A 587 10394 9960 5669 -100 -2418 1230 C ATOM 4191 CD1 ILE A 587 18.770 232.987 805.004 1.00 47.45 C ANISOU 4191 CD1 ILE A 587 7659 7155 3215 -76 -2219 1047 C ATOM 4192 C ILE A 587 18.135 236.923 802.687 1.00 74.78 C ANISOU 4192 C ILE A 587 11233 11054 6127 -13 -1975 1600 C ATOM 4193 O ILE A 587 17.976 237.923 803.349 1.00 71.95 O ANISOU 4193 O ILE A 587 10869 10742 5728 49 -1695 1543 O ATOM 4194 N ASN A 588 18.629 236.961 801.471 1.00 72.90 N ANISOU 4194 N ASN A 588 11128 10931 5639 -80 -2257 1799 N ATOM 4195 CA ASN A 588 18.990 238.242 800.937 1.00 81.77 C ANISOU 4195 CA ASN A 588 12421 12258 6389 -95 -2192 1966 C ATOM 4196 CB ASN A 588 20.309 238.142 800.196 1.00 89.94 C ANISOU 4196 CB ASN A 588 13763 13489 6919 -168 -2491 2010 C ATOM 4197 CG ASN A 588 21.124 236.962 800.640 1.00 98.01 C ANISOU 4197 CG ASN A 588 14859 14453 7929 -171 -2691 1752 C ATOM 4198 ND2 ASN A 588 20.861 235.815 800.049 1.00108.06 N ANISOU 4198 ND2 ASN A 588 16010 15593 9455 -216 -3017 1829 N ATOM 4199 OD1 ASN A 588 21.972 237.072 801.509 1.00 94.76 O ANISOU 4199 OD1 ASN A 588 14596 14105 7302 -131 -2566 1486 O ATOM 4200 C ASN A 588 17.929 238.895 800.106 1.00 90.12 C ANISOU 4200 C ASN A 588 13339 13290 7612 -118 -2173 2274 C ATOM 4201 O ASN A 588 18.087 240.025 799.676 1.00 90.27 O ANISOU 4201 O ASN A 588 13481 13469 7349 -146 -2092 2458 O ATOM 4202 N ASN A 589 16.848 238.191 799.838 1.00 92.28 N ANISOU 4202 N ASN A 589 13363 13369 8331 -112 -2255 2344 N ATOM 4203 CA ASN A 589 15.805 238.828 799.077 1.00 89.49 C ANISOU 4203 CA ASN A 589 12872 12964 8166 -122 -2247 2626 C ATOM 4204 CB ASN A 589 15.568 238.086 797.769 1.00 86.63 C ANISOU 4204 CB ASN A 589 12452 12509 7955 -165 -2662 2895 C ATOM 4205 CG ASN A 589 16.627 238.375 796.749 1.00 91.38 C ANISOU 4205 CG ASN A 589 13332 13283 8106 -243 -2981 3139 C ATOM 4206 ND2 ASN A 589 16.685 237.572 795.711 1.00 92.55 N ANISOU 4206 ND2 ASN A 589 13450 13354 8359 -273 -3423 3339 N ATOM 4207 OD1 ASN A 589 17.390 239.314 796.900 1.00 94.49 O ANISOU 4207 OD1 ASN A 589 13965 13888 8048 -277 -2843 3152 O ATOM 4208 C ASN A 589 14.525 238.943 799.855 1.00 85.29 C ANISOU 4208 C ASN A 589 12078 12284 8044 -59 -1957 2501 C ATOM 4209 O ASN A 589 14.043 240.027 800.111 1.00 89.49 O ANISOU 4209 O ASN A 589 12572 12852 8579 -37 -1725 2549 O ATOM 4210 N GLN A 590 13.964 237.806 800.206 1.00 79.05 N ANISOU 4210 N GLN A 590 11113 11339 7582 -39 -1987 2351 N ATOM 4211 CA GLN A 590 12.726 237.765 800.941 1.00 76.66 C ANISOU 4211 CA GLN A 590 10587 10916 7624 8 -1740 2222 C ATOM 4212 CB GLN A 590 12.244 236.339 800.933 1.00 84.33 C ANISOU 4212 CB GLN A 590 11403 11754 8885 3 -1865 2144 C ATOM 4213 CG GLN A 590 10.815 236.232 800.678 1.00 83.12 C ANISOU 4213 CG GLN A 590 11018 11475 9089 34 -1813 2211 C ATOM 4214 CD GLN A 590 10.442 236.920 799.442 1.00 79.87 C ANISOU 4214 CD GLN A 590 10575 11024 8748 37 -1984 2523 C ATOM 4215 NE2 GLN A 590 10.969 236.455 798.339 1.00 79.06 N ANISOU 4215 NE2 GLN A 590 10508 10899 8633 14 -2343 2733 N ATOM 4216 OE1 GLN A 590 9.697 237.879 799.462 1.00 82.69 O ANISOU 4216 OE1 GLN A 590 10877 11360 9180 58 -1826 2596 O ATOM 4217 C GLN A 590 12.754 238.270 802.375 1.00 73.90 C ANISOU 4217 C GLN A 590 10247 10599 7232 59 -1415 1962 C ATOM 4218 O GLN A 590 11.888 238.998 802.795 1.00 76.12 O ANISOU 4218 O GLN A 590 10415 10858 7651 95 -1212 1943 O ATOM 4219 N MSE A 591 13.744 237.871 803.141 1.00 77.21 N ANISOU 4219 N MSE A 591 10798 11052 7485 69 -1398 1770 N ATOM 4220 CA MSE A 591 13.766 238.290 804.520 1.00 70.55 C ANISOU 4220 CA MSE A 591 9950 10201 6656 134 -1142 1551 C ATOM 4221 C MSE A 591 14.468 239.589 804.798 1.00 69.21 C ANISOU 4221 C MSE A 591 9913 10171 6211 183 -1011 1553 C ATOM 4222 O MSE A 591 14.094 240.291 805.691 1.00 72.01 O ANISOU 4222 O MSE A 591 10197 10517 6647 249 -805 1459 O ATOM 4223 CB MSE A 591 14.319 237.189 805.424 1.00 72.05 C ANISOU 4223 CB MSE A 591 10189 10311 6877 133 -1172 1344 C ATOM 4224 CG MSE A 591 13.291 236.172 805.900 1.00 69.79 C ANISOU 4224 CG MSE A 591 9726 9890 6903 107 -1128 1271 C ATOM 4225 SE MSE A 591 13.819 235.418 807.491 1.00 60.71 Se ANISOU 4225 SE MSE A 591 8649 8645 5774 119 -1055 1043 Se ATOM 4226 CE MSE A 591 12.891 233.865 807.401 1.00 64.15 C ANISOU 4226 CE MSE A 591 8924 8989 6459 24 -1121 1062 C ATOM 4227 N LYS A 592 15.502 239.925 804.051 1.00 77.73 N ANISOU 4227 N LYS A 592 11194 11398 6940 148 -1137 1665 N ATOM 4228 CA LYS A 592 16.213 241.149 804.367 1.00 85.37 C ANISOU 4228 CA LYS A 592 12302 12536 7597 188 -976 1656 C ATOM 4229 CB LYS A 592 17.670 240.827 804.703 1.00 94.37 C ANISOU 4229 CB LYS A 592 13685 13774 8398 201 -1049 1489 C ATOM 4230 CG LYS A 592 18.201 241.596 805.900 1.00100.03 C ANISOU 4230 CG LYS A 592 14457 14554 8994 304 -814 1292 C ATOM 4231 CD LYS A 592 19.583 241.160 806.352 1.00 98.78 C ANISOU 4231 CD LYS A 592 14531 14461 8539 331 -890 1076 C ATOM 4232 CE LYS A 592 20.166 242.192 807.295 1.00100.69 C ANISOU 4232 CE LYS A 592 14847 14826 8583 433 -646 917 C ATOM 4233 NZ LYS A 592 21.260 241.668 808.132 1.00101.00 N ANISOU 4233 NZ LYS A 592 15052 14850 8474 497 -693 635 N ATOM 4234 C LYS A 592 16.135 242.247 803.317 1.00 93.91 C ANISOU 4234 C LYS A 592 13447 13773 8460 130 -971 1945 C ATOM 4235 O LYS A 592 16.471 242.053 802.163 1.00 87.85 O ANISOU 4235 O LYS A 592 12802 13076 7503 45 -1194 2156 O ATOM 4236 N PRO A 593 15.688 243.416 803.751 1.00106.56 N ANISOU 4236 N PRO A 593 14972 15427 10089 169 -731 1977 N ATOM 4237 CD PRO A 593 15.183 243.707 805.107 1.00 97.82 C ANISOU 4237 CD PRO A 593 13707 14231 9229 273 -513 1760 C ATOM 4238 CG PRO A 593 14.947 245.198 805.090 1.00100.24 C ANISOU 4238 CG PRO A 593 13991 14669 9428 275 -308 1904 C ATOM 4239 CB PRO A 593 15.601 245.749 803.845 1.00108.35 C ANISOU 4239 CB PRO A 593 15221 15892 10056 166 -370 2180 C ATOM 4240 CA PRO A 593 15.554 244.577 802.864 1.00112.83 C ANISOU 4240 CA PRO A 593 15822 16364 10683 98 -679 2281 C ATOM 4241 C PRO A 593 16.697 244.685 801.855 1.00118.11 C ANISOU 4241 C PRO A 593 16784 17243 10850 0 -835 2462 C ATOM 4242 O PRO A 593 17.101 245.798 801.511 1.00119.15 O ANISOU 4242 O PRO A 593 17060 17581 10631 -58 -700 2639 O ATOM 4243 N ASP A 600 10.938 259.432 801.680 1.00138.50 N ANISOU 4243 N ASP A 600 18301 20205 14119 -971 2207 5057 N ATOM 4244 CA ASP A 600 9.860 259.010 800.804 1.00141.00 C ANISOU 4244 CA ASP A 600 18564 20184 14825 -1003 1862 5340 C ATOM 4245 CB ASP A 600 10.165 257.637 800.226 1.00143.68 C ANISOU 4245 CB ASP A 600 19086 20487 15020 -886 1433 5260 C ATOM 4246 CG ASP A 600 9.030 257.094 799.396 1.00143.28 C ANISOU 4246 CG ASP A 600 18941 20073 15426 -886 1080 5486 C ATOM 4247 OD2 ASP A 600 8.162 257.881 798.985 1.00146.92 O ANISOU 4247 OD2 ASP A 600 19273 20319 16231 -1019 1151 5817 O ATOM 4248 OD1 ASP A 600 9.003 255.877 799.144 1.00137.09 O ANISOU 4248 OD1 ASP A 600 18197 19199 14690 -764 742 5331 O ATOM 4249 C ASP A 600 8.575 258.935 801.593 1.00135.64 C ANISOU 4249 C ASP A 600 17571 19204 14761 -900 1801 5129 C ATOM 4250 O ASP A 600 7.597 258.336 801.161 1.00129.92 O ANISOU 4250 O ASP A 600 16767 18177 14418 -860 1497 5195 O ATOM 4251 N PHE A 601 8.572 259.555 802.762 1.00136.24 N ANISOU 4251 N PHE A 601 17463 19366 14934 -865 2096 4868 N ATOM 4252 CA PHE A 601 7.401 259.488 803.615 1.00132.58 C ANISOU 4252 CA PHE A 601 16723 18650 15003 -780 2029 4648 C ATOM 4253 CB PHE A 601 7.676 258.570 804.799 1.00127.51 C ANISOU 4253 CB PHE A 601 16073 18081 14293 -538 1905 4143 C ATOM 4254 CG PHE A 601 7.964 257.166 804.412 1.00121.46 C ANISOU 4254 CG PHE A 601 15493 17290 13364 -400 1543 4006 C ATOM 4255 CD2 PHE A 601 9.066 256.513 804.898 1.00118.25 C ANISOU 4255 CD2 PHE A 601 15239 17086 12604 -272 1517 3718 C ATOM 4256 CE2 PHE A 601 9.324 255.228 804.544 1.00114.12 C ANISOU 4256 CE2 PHE A 601 14846 16522 11994 -179 1207 3591 C ATOM 4257 CZ PHE A 601 8.489 254.583 803.703 1.00114.24 C ANISOU 4257 CZ PHE A 601 14831 16319 12258 -201 937 3738 C ATOM 4258 CE1 PHE A 601 7.390 255.212 803.213 1.00117.64 C ANISOU 4258 CE1 PHE A 601 15124 16545 13030 -305 952 4015 C ATOM 4259 CD1 PHE A 601 7.124 256.494 803.567 1.00118.62 C ANISOU 4259 CD1 PHE A 601 15129 16686 13257 -409 1244 4153 C ATOM 4260 C PHE A 601 6.868 260.804 804.128 1.00129.25 C ANISOU 4260 C PHE A 601 16021 18180 14908 -934 2379 4733 C ATOM 4261 O PHE A 601 7.574 261.790 804.226 1.00135.21 O ANISOU 4261 O PHE A 601 16749 19166 15458 -1062 2765 4829 O ATOM 4262 N ILE A 602 5.583 260.793 804.420 1.00120.67 N ANISOU 4262 N ILE A 602 14707 16784 14359 -938 2247 4683 N ATOM 4263 CA ILE A 602 4.894 261.938 804.937 1.00115.68 C ANISOU 4263 CA ILE A 602 13744 16042 14165 -1097 2514 4719 C ATOM 4264 CB ILE A 602 4.011 262.455 803.840 1.00116.13 C ANISOU 4264 CB ILE A 602 13733 15781 14609 -1307 2449 5134 C ATOM 4265 CG2 ILE A 602 3.756 261.352 802.858 1.00102.50 C ANISOU 4265 CG2 ILE A 602 12249 13876 12821 -1221 2055 5277 C ATOM 4266 CG1 ILE A 602 2.671 262.887 804.392 1.00123.77 C ANISOU 4266 CG1 ILE A 602 14333 16428 16265 -1326 2351 4932 C ATOM 4267 CD1 ILE A 602 1.680 263.158 803.312 1.00128.71 C ANISOU 4267 CD1 ILE A 602 14899 16659 17345 -1490 2198 5272 C ATOM 4268 C ILE A 602 4.023 261.499 806.099 1.00107.95 C ANISOU 4268 C ILE A 602 12542 14909 13565 -925 2305 4268 C ATOM 4269 O ILE A 602 3.228 260.588 805.939 1.00105.84 O ANISOU 4269 O ILE A 602 12328 14418 13470 -833 1970 4180 O ATOM 4270 N SER A 603 4.109 262.152 807.252 1.00100.95 N ANISOU 4270 N SER A 603 11395 14130 12832 -885 2488 3983 N ATOM 4271 CA SER A 603 5.040 263.220 807.481 1.00109.87 C ANISOU 4271 CA SER A 603 12419 15527 13800 -983 2919 4040 C ATOM 4272 CB SER A 603 4.283 264.485 807.814 1.00124.27 C ANISOU 4272 CB SER A 603 13821 17202 16195 -1141 3091 4050 C ATOM 4273 OG SER A 603 3.340 264.767 806.805 1.00132.89 O ANISOU 4273 OG SER A 603 14879 17987 17626 -1331 2979 4385 O ATOM 4274 C SER A 603 5.979 262.879 808.612 1.00110.44 C ANISOU 4274 C SER A 603 12516 15866 13581 -774 3003 3655 C ATOM 4275 O SER A 603 7.188 262.960 808.447 1.00112.73 O ANISOU 4275 O SER A 603 12988 16446 13398 -774 3257 3693 O ATOM 4276 N ALA A 604 5.436 262.475 809.760 1.00109.54 N ANISOU 4276 N ALA A 604 12235 15648 13738 -596 2774 3281 N ATOM 4277 CA ALA A 604 3.999 262.365 809.991 1.00103.61 C ANISOU 4277 CA ALA A 604 11291 14582 13495 -602 2470 3195 C ATOM 4278 CB ALA A 604 3.694 261.042 810.622 1.00107.50 C ANISOU 4278 CB ALA A 604 11943 15016 13887 -389 2100 2912 C ATOM 4279 C ALA A 604 3.325 263.486 810.783 1.00 99.30 C ANISOU 4279 C ALA A 604 10301 13934 13495 -671 2556 3049 C ATOM 4280 O ALA A 604 2.144 263.422 811.018 1.00 91.37 O ANISOU 4280 O ALA A 604 9142 12681 12891 -682 2291 2940 O ATOM 4281 N ILE A 605 4.054 264.505 811.197 1.00104.98 N ANISOU 4281 N ILE A 605 10799 14843 14244 -719 2921 3023 N ATOM 4282 CA ILE A 605 3.441 265.626 811.914 1.00111.93 C ANISOU 4282 CA ILE A 605 11209 15623 15696 -798 3006 2894 C ATOM 4283 CB ILE A 605 2.466 266.366 811.033 1.00100.06 C ANISOU 4283 CB ILE A 605 9546 13868 14604 -1060 3028 3184 C ATOM 4284 CG2 ILE A 605 1.252 265.527 810.799 1.00 94.92 C ANISOU 4284 CG2 ILE A 605 9010 12918 14139 -1023 2576 3132 C ATOM 4285 CG1 ILE A 605 2.066 267.669 811.698 1.00 85.81 C ANISOU 4285 CG1 ILE A 605 7229 12002 13371 -1178 3197 3078 C ATOM 4286 CD1 ILE A 605 0.938 268.334 811.017 1.00 72.85 C ANISOU 4286 CD1 ILE A 605 5393 10049 12239 -1426 3137 3293 C ATOM 4287 C ILE A 605 2.761 265.337 813.252 1.00124.23 C ANISOU 4287 C ILE A 605 12557 17069 17575 -616 2663 2496 C ATOM 4288 O ILE A 605 3.402 264.895 814.184 1.00137.24 O ANISOU 4288 O ILE A 605 14243 18862 19040 -405 2610 2239 O ATOM 4289 N LYS A 606 1.470 265.631 813.359 1.00117.52 N ANISOU 4289 N LYS A 606 11484 15954 17213 -707 2421 2450 N ATOM 4290 CA LYS A 606 0.714 265.437 814.602 1.00102.57 C ANISOU 4290 CA LYS A 606 9395 13957 15620 -570 2059 2093 C ATOM 4291 CB LYS A 606 -0.686 266.019 814.484 1.00 95.60 C ANISOU 4291 CB LYS A 606 8244 12787 15293 -740 1862 2076 C ATOM 4292 C LYS A 606 0.614 263.983 814.998 1.00 95.61 C ANISOU 4292 C LYS A 606 8864 13085 14379 -363 1702 1919 C ATOM 4293 O LYS A 606 0.709 263.108 814.157 1.00 92.37 O ANISOU 4293 O LYS A 606 8802 12668 13626 -360 1660 2069 O ATOM 4294 N PHE A 607 0.444 263.734 816.294 1.00 90.92 N ANISOU 4294 N PHE A 607 8164 12506 13876 -196 1440 1618 N ATOM 4295 CA PHE A 607 0.415 262.368 816.836 1.00 83.82 C ANISOU 4295 CA PHE A 607 7587 11633 12628 -9 1117 1458 C ATOM 4296 CB PHE A 607 0.546 262.368 818.359 1.00 83.84 C ANISOU 4296 CB PHE A 607 7429 11681 12747 171 897 1183 C ATOM 4297 CG PHE A 607 0.227 261.038 818.986 1.00 87.79 C ANISOU 4297 CG PHE A 607 8233 12166 12955 313 517 1041 C ATOM 4298 CD1 PHE A 607 1.095 259.963 818.842 1.00 89.39 C ANISOU 4298 CD1 PHE A 607 8795 12482 12687 432 555 1084 C ATOM 4299 CE1 PHE A 607 0.803 258.735 819.408 1.00 88.64 C ANISOU 4299 CE1 PHE A 607 8972 12371 12335 535 234 978 C ATOM 4300 CZ PHE A 607 -0.365 258.567 820.121 1.00 85.74 C ANISOU 4300 CZ PHE A 607 8551 11903 12125 519 -124 828 C ATOM 4301 CE2 PHE A 607 -1.243 259.630 820.270 1.00 84.30 C ANISOU 4301 CE2 PHE A 607 8027 11616 12385 409 -193 761 C ATOM 4302 CD2 PHE A 607 -0.945 260.856 819.703 1.00 87.41 C ANISOU 4302 CD2 PHE A 607 8122 12000 13091 307 124 868 C ATOM 4303 C PHE A 607 -0.802 261.532 816.440 1.00 83.52 C ANISOU 4303 C PHE A 607 7742 11418 12576 -60 799 1429 C ATOM 4304 O PHE A 607 -1.947 261.982 816.528 1.00 84.08 O ANISOU 4304 O PHE A 607 7610 11313 13024 -167 624 1340 O ATOM 4305 N ASP A 608 -0.525 260.292 816.049 1.00 75.88 N ANISOU 4305 N ASP A 608 7152 10501 11180 22 728 1471 N ATOM 4306 CA ASP A 608 -1.519 259.358 815.535 1.00 74.60 C ANISOU 4306 CA ASP A 608 7195 10197 10953 -13 497 1442 C ATOM 4307 CB ASP A 608 -1.912 259.761 814.112 1.00 76.78 C ANISOU 4307 CB ASP A 608 7448 10315 11409 -188 651 1685 C ATOM 4308 CG ASP A 608 -2.944 258.838 813.502 1.00 84.13 C ANISOU 4308 CG ASP A 608 8549 11070 12347 -212 437 1628 C ATOM 4309 OD1 ASP A 608 -3.423 257.934 814.211 1.00 94.34 O ANISOU 4309 OD1 ASP A 608 9969 12388 13489 -117 195 1386 O ATOM 4310 OD2 ASP A 608 -3.283 259.020 812.312 1.00 79.34 O ANISOU 4310 OD2 ASP A 608 7942 10294 11909 -330 517 1827 O ATOM 4311 C ASP A 608 -0.828 258.003 815.511 1.00 83.90 C ANISOU 4311 C ASP A 608 8739 11501 11640 123 446 1446 C ATOM 4312 O ASP A 608 0.105 257.806 814.735 1.00 92.13 O ANISOU 4312 O ASP A 608 9942 12635 12428 128 653 1642 O ATOM 4313 N GLY A 609 -1.272 257.057 816.335 1.00 78.58 N ANISOU 4313 N GLY A 609 8205 10836 10817 218 169 1242 N ATOM 4314 CA GLY A 609 -2.506 257.127 817.092 1.00 68.03 C ANISOU 4314 CA GLY A 609 6750 9399 9700 188 -114 1018 C ATOM 4315 C GLY A 609 -3.242 255.855 816.715 1.00 64.84 C ANISOU 4315 C GLY A 609 6612 8947 9079 180 -268 941 C ATOM 4316 O GLY A 609 -3.142 254.820 817.375 1.00 63.49 O ANISOU 4316 O GLY A 609 6659 8868 8596 269 -419 842 O ATOM 4317 N PHE A 610 -3.872 255.902 815.568 1.00 57.06 N ANISOU 4317 N PHE A 610 5609 7809 8261 72 -197 1013 N ATOM 4318 CA PHE A 610 -4.486 254.750 815.017 1.00 53.91 C ANISOU 4318 CA PHE A 610 5418 7352 7713 68 -279 943 C ATOM 4319 CB PHE A 610 -5.623 255.182 814.136 1.00 64.54 C ANISOU 4319 CB PHE A 610 6617 8458 9447 -59 -291 904 C ATOM 4320 CG PHE A 610 -6.038 254.155 813.169 1.00 57.57 C ANISOU 4320 CG PHE A 610 5895 7476 8503 -58 -287 898 C ATOM 4321 CD2 PHE A 610 -5.809 254.321 811.847 1.00 63.12 C ANISOU 4321 CD2 PHE A 610 6577 8035 9370 -102 -148 1147 C ATOM 4322 CE2 PHE A 610 -6.185 253.389 810.973 1.00 61.71 C ANISOU 4322 CE2 PHE A 610 6506 7745 9197 -83 -169 1135 C ATOM 4323 CZ PHE A 610 -6.801 252.281 811.396 1.00 61.04 C ANISOU 4323 CZ PHE A 610 6542 7709 8940 -33 -279 855 C ATOM 4324 CE1 PHE A 610 -7.043 252.101 812.702 1.00 60.85 C ANISOU 4324 CE1 PHE A 610 6570 7850 8701 -12 -394 620 C ATOM 4325 CD1 PHE A 610 -6.670 253.033 813.582 1.00 59.05 C ANISOU 4325 CD1 PHE A 610 6241 7712 8481 -19 -422 650 C ATOM 4326 C PHE A 610 -3.429 254.186 814.147 1.00 60.31 C ANISOU 4326 C PHE A 610 6408 8230 8277 115 -102 1181 C ATOM 4327 O PHE A 610 -3.163 253.019 814.119 1.00 74.78 O ANISOU 4327 O PHE A 610 8464 10138 9811 183 -144 1157 O ATOM 4328 N THR A 611 -2.789 255.084 813.448 1.00 64.03 N ANISOU 4328 N THR A 611 6771 8682 8874 64 100 1421 N ATOM 4329 CA THR A 611 -1.755 254.765 812.515 1.00 60.09 C ANISOU 4329 CA THR A 611 6434 8252 8145 82 262 1678 C ATOM 4330 CB THR A 611 -1.175 256.040 811.983 1.00 72.17 C ANISOU 4330 CB THR A 611 7811 9787 9822 -10 496 1923 C ATOM 4331 CG2 THR A 611 0.218 256.218 812.504 1.00 83.05 C ANISOU 4331 CG2 THR A 611 9257 11408 10892 73 657 1969 C ATOM 4332 OG1 THR A 611 -1.151 256.005 810.561 1.00 67.32 O ANISOU 4332 OG1 THR A 611 7268 9058 9253 -95 570 2199 O ATOM 4333 C THR A 611 -0.640 254.094 813.241 1.00 53.49 C ANISOU 4333 C THR A 611 5783 7633 6907 212 268 1637 C ATOM 4334 O THR A 611 -0.000 253.219 812.729 1.00 51.43 O ANISOU 4334 O THR A 611 5733 7436 6372 256 283 1728 O ATOM 4335 N SER A 612 -0.372 254.536 814.443 1.00 52.74 N ANISOU 4335 N SER A 612 5592 7632 6815 274 242 1499 N ATOM 4336 CA SER A 612 0.696 253.976 815.218 1.00 45.20 C ANISOU 4336 CA SER A 612 4790 6839 5544 405 236 1446 C ATOM 4337 CB SER A 612 0.815 254.733 816.510 1.00 34.40 C ANISOU 4337 CB SER A 612 3231 5514 4326 470 189 1300 C ATOM 4338 OG SER A 612 1.845 254.196 817.281 1.00 69.68 O ANISOU 4338 OG SER A 612 7838 10096 8541 608 167 1241 O ATOM 4339 C SER A 612 0.479 252.520 815.512 1.00 54.48 C ANISOU 4339 C SER A 612 6205 8025 6468 463 45 1339 C ATOM 4340 O SER A 612 1.400 251.751 815.474 1.00 57.08 O ANISOU 4340 O SER A 612 6731 8446 6512 530 69 1382 O ATOM 4341 N ILE A 613 -0.742 252.142 815.834 1.00 61.96 N ANISOU 4341 N ILE A 613 7138 8888 7518 423 -136 1186 N ATOM 4342 CA ILE A 613 -1.061 250.759 816.119 1.00 47.73 C ANISOU 4342 CA ILE A 613 5553 7110 5473 447 -281 1081 C ATOM 4343 CB ILE A 613 -2.478 250.632 816.562 1.00 43.10 C ANISOU 4343 CB ILE A 613 4918 6455 5002 383 -451 879 C ATOM 4344 CG2 ILE A 613 -2.854 249.228 816.541 1.00 31.13 C ANISOU 4344 CG2 ILE A 613 3612 4971 3243 373 -516 793 C ATOM 4345 CG1 ILE A 613 -2.638 251.164 817.964 1.00 38.43 C ANISOU 4345 CG1 ILE A 613 4247 5911 4444 419 -625 759 C ATOM 4346 CD1 ILE A 613 -4.019 251.201 818.398 1.00 34.93 C ANISOU 4346 CD1 ILE A 613 3755 5419 4098 340 -813 554 C ATOM 4347 C ILE A 613 -0.944 249.834 814.946 1.00 42.78 C ANISOU 4347 C ILE A 613 5059 6451 4746 417 -199 1167 C ATOM 4348 O ILE A 613 -0.435 248.769 815.064 1.00 45.19 O ANISOU 4348 O ILE A 613 5459 6771 4941 419 -145 1040 O ATOM 4349 N ILE A 614 -1.414 250.251 813.796 1.00 36.26 N ANISOU 4349 N ILE A 614 4134 5504 4138 351 -129 1273 N ATOM 4350 CA ILE A 614 -1.378 249.395 812.651 1.00 54.36 C ANISOU 4350 CA ILE A 614 6523 7740 6391 338 -101 1370 C ATOM 4351 CB ILE A 614 -1.885 250.111 811.444 1.00 52.86 C ANISOU 4351 CB ILE A 614 6185 7371 6528 262 -38 1511 C ATOM 4352 CG2 ILE A 614 -1.347 249.469 810.267 1.00 43.52 C ANISOU 4352 CG2 ILE A 614 5102 6159 5275 273 -15 1705 C ATOM 4353 CG1 ILE A 614 -3.377 249.980 811.321 1.00 48.65 C ANISOU 4353 CG1 ILE A 614 5538 6663 6284 209 -124 1302 C ATOM 4354 CD1 ILE A 614 -4.012 249.534 812.523 1.00 50.58 C ANISOU 4354 CD1 ILE A 614 5825 6991 6403 221 -232 1019 C ATOM 4355 C ILE A 614 0.036 249.057 812.360 1.00 55.35 C ANISOU 4355 C ILE A 614 6680 7961 6389 364 18 1379 C ATOM 4356 O ILE A 614 0.349 247.961 811.991 1.00 47.81 O ANISOU 4356 O ILE A 614 5780 6999 5385 368 14 1284 O ATOM 4357 N SER A 615 0.917 250.010 812.510 1.00 63.08 N ANISOU 4357 N SER A 615 7622 9025 7321 392 110 1501 N ATOM 4358 CA SER A 615 2.304 249.773 812.250 1.00 60.78 C ANISOU 4358 CA SER A 615 7379 8826 6890 442 183 1499 C ATOM 4359 CB SER A 615 3.003 251.093 812.399 1.00 69.83 C ANISOU 4359 CB SER A 615 8484 10071 7976 458 319 1667 C ATOM 4360 OG SER A 615 2.098 252.113 812.067 1.00 75.68 O ANISOU 4360 OG SER A 615 9131 10734 8891 362 380 1873 O ATOM 4361 C SER A 615 2.917 248.767 813.186 1.00 52.21 C ANISOU 4361 C SER A 615 6369 7769 5700 509 136 1267 C ATOM 4362 O SER A 615 3.633 247.894 812.772 1.00 49.40 O ANISOU 4362 O SER A 615 6078 7404 5288 521 129 1214 O ATOM 4363 N LEU A 616 2.643 248.886 814.462 1.00 35.80 N ANISOU 4363 N LEU A 616 4291 5706 3607 543 89 1156 N ATOM 4364 CA LEU A 616 3.188 247.945 815.397 1.00 37.53 C ANISOU 4364 CA LEU A 616 4595 5907 3758 593 44 985 C ATOM 4365 CB LEU A 616 2.893 248.402 816.798 1.00 40.13 C ANISOU 4365 CB LEU A 616 4922 6261 4065 635 -30 928 C ATOM 4366 CG LEU A 616 4.054 248.403 817.754 1.00 46.52 C ANISOU 4366 CG LEU A 616 5788 7101 4785 747 -33 881 C ATOM 4367 CD2 LEU A 616 5.008 247.421 817.306 1.00 28.25 C ANISOU 4367 CD2 LEU A 616 3564 4742 2429 760 7 832 C ATOM 4368 CD1 LEU A 616 3.544 247.980 819.044 1.00 44.50 C ANISOU 4368 CD1 LEU A 616 5595 6789 4525 751 -177 782 C ATOM 4369 C LEU A 616 2.630 246.560 815.206 1.00 45.95 C ANISOU 4369 C LEU A 616 5723 6881 4857 531 -9 873 C ATOM 4370 O LEU A 616 3.336 245.595 815.267 1.00 41.60 O ANISOU 4370 O LEU A 616 5241 6292 4271 545 -14 808 O ATOM 4371 N GLU A 617 1.338 246.447 814.998 1.00 43.79 N ANISOU 4371 N GLU A 617 5430 6570 4638 463 -52 858 N ATOM 4372 CA GLU A 617 0.771 245.142 814.825 1.00 31.00 C ANISOU 4372 CA GLU A 617 3869 4890 3020 413 -82 764 C ATOM 4373 CB GLU A 617 -0.731 245.200 814.891 1.00 43.18 C ANISOU 4373 CB GLU A 617 5416 6421 4569 359 -143 723 C ATOM 4374 CG GLU A 617 -1.258 245.685 816.204 1.00 41.13 C ANISOU 4374 CG GLU A 617 5190 6198 4239 359 -236 655 C ATOM 4375 CD GLU A 617 -0.923 244.796 817.337 1.00 47.00 C ANISOU 4375 CD GLU A 617 6035 6933 4891 362 -274 573 C ATOM 4376 OE1 GLU A 617 -1.381 243.668 817.363 1.00 48.09 O ANISOU 4376 OE1 GLU A 617 6244 7055 4973 309 -279 513 O ATOM 4377 OE2 GLU A 617 -0.218 245.230 818.235 1.00 59.60 O ANISOU 4377 OE2 GLU A 617 7645 8538 6462 416 -307 588 O ATOM 4378 C GLU A 617 1.239 244.494 813.572 1.00 38.64 C ANISOU 4378 C GLU A 617 4825 5831 4024 401 -45 818 C ATOM 4379 O GLU A 617 1.495 243.322 813.545 1.00 46.05 O ANISOU 4379 O GLU A 617 5812 6740 4944 386 -56 755 O ATOM 4380 N SER A 618 1.330 245.270 812.512 1.00 44.79 N ANISOU 4380 N SER A 618 5543 6621 4854 398 -15 966 N ATOM 4381 CA SER A 618 1.790 244.777 811.238 1.00 52.45 C ANISOU 4381 CA SER A 618 6510 7571 5846 383 -13 1061 C ATOM 4382 CB SER A 618 1.643 245.851 810.180 1.00 48.40 C ANISOU 4382 CB SER A 618 5937 7049 5405 364 1 1286 C ATOM 4383 OG SER A 618 0.326 246.297 810.083 1.00 49.54 O ANISOU 4383 OG SER A 618 6035 7109 5680 334 -23 1334 O ATOM 4384 C SER A 618 3.226 244.343 811.323 1.00 55.44 C ANISOU 4384 C SER A 618 6948 7991 6125 417 -5 1035 C ATOM 4385 O SER A 618 3.606 243.354 810.755 1.00 52.52 O ANISOU 4385 O SER A 618 6613 7599 5743 396 -38 1027 O ATOM 4386 N LEU A 619 4.039 245.105 812.020 1.00 60.85 N ANISOU 4386 N LEU A 619 7652 8736 6733 474 31 1033 N ATOM 4387 CA LEU A 619 5.416 244.736 812.173 1.00 54.88 C ANISOU 4387 CA LEU A 619 6981 8008 5864 518 31 1001 C ATOM 4388 CB LEU A 619 6.152 245.804 812.946 1.00 51.25 C ANISOU 4388 CB LEU A 619 6534 7626 5312 601 85 1015 C ATOM 4389 CG LEU A 619 7.630 246.004 812.662 1.00 56.31 C ANISOU 4389 CG LEU A 619 7272 8344 5777 653 115 1057 C ATOM 4390 CD1 LEU A 619 8.333 246.430 813.883 1.00 47.64 C ANISOU 4390 CD1 LEU A 619 6220 7282 4600 756 146 979 C ATOM 4391 CD2 LEU A 619 8.263 244.808 812.089 1.00 50.06 C ANISOU 4391 CD2 LEU A 619 6574 7508 4939 616 47 1019 C ATOM 4392 C LEU A 619 5.481 243.450 812.948 1.00 59.91 C ANISOU 4392 C LEU A 619 7680 8568 6514 509 -16 854 C ATOM 4393 O LEU A 619 6.261 242.579 812.664 1.00 64.62 O ANISOU 4393 O LEU A 619 8347 9142 7064 496 -49 834 O ATOM 4394 N HIS A 620 4.654 243.327 813.956 1.00 49.62 N ANISOU 4394 N HIS A 620 6368 7227 5258 501 -29 771 N ATOM 4395 CA HIS A 620 4.686 242.147 814.772 1.00 39.34 C ANISOU 4395 CA HIS A 620 5144 5857 3947 474 -72 678 C ATOM 4396 CB HIS A 620 3.678 242.294 815.883 1.00 44.51 C ANISOU 4396 CB HIS A 620 5806 6498 4608 459 -100 628 C ATOM 4397 CG HIS A 620 3.470 241.057 816.686 1.00 46.52 C ANISOU 4397 CG HIS A 620 6154 6696 4825 400 -151 577 C ATOM 4398 CD2 HIS A 620 2.418 240.222 816.773 1.00 42.65 C ANISOU 4398 CD2 HIS A 620 5683 6205 4319 317 -169 554 C ATOM 4399 NE2 HIS A 620 2.747 239.249 817.673 1.00 43.27 N ANISOU 4399 NE2 HIS A 620 5874 6242 4323 269 -216 548 N ATOM 4400 CE1 HIS A 620 3.949 239.489 818.140 1.00 52.29 C ANISOU 4400 CE1 HIS A 620 7073 7340 5456 332 -237 556 C ATOM 4401 ND1 HIS A 620 4.404 240.580 817.565 1.00 52.35 N ANISOU 4401 ND1 HIS A 620 7001 7383 5507 419 -192 563 N ATOM 4402 C HIS A 620 4.341 240.953 813.980 1.00 45.80 C ANISOU 4402 C HIS A 620 5959 6646 4799 400 -91 676 C ATOM 4403 O HIS A 620 4.955 239.930 814.087 1.00 54.78 O ANISOU 4403 O HIS A 620 7161 7746 5906 372 -121 652 O ATOM 4404 N GLN A 621 3.343 241.071 813.151 1.00 45.59 N ANISOU 4404 N GLN A 621 5858 6636 4830 369 -78 713 N ATOM 4405 CA GLN A 621 2.987 239.921 812.401 1.00 44.49 C ANISOU 4405 CA GLN A 621 5709 6482 4715 316 -96 719 C ATOM 4406 CB GLN A 621 1.798 240.235 811.543 1.00 35.13 C ANISOU 4406 CB GLN A 621 4452 5302 3593 306 -87 769 C ATOM 4407 CG GLN A 621 1.577 239.233 810.504 1.00 40.17 C ANISOU 4407 CG GLN A 621 5064 5932 4266 279 -111 819 C ATOM 4408 CD GLN A 621 0.311 239.444 809.767 1.00 52.99 C ANISOU 4408 CD GLN A 621 6637 7533 5964 289 -114 874 C ATOM 4409 NE2 GLN A 621 -0.757 238.864 810.255 1.00 61.95 N ANISOU 4409 NE2 GLN A 621 7796 8694 7048 274 -92 773 N ATOM 4410 OE1 GLN A 621 0.291 240.092 808.748 1.00 51.02 O ANISOU 4410 OE1 GLN A 621 6339 7235 5813 306 -148 1022 O ATOM 4411 C GLN A 621 4.124 239.488 811.523 1.00 55.48 C ANISOU 4411 C GLN A 621 7120 7877 6082 311 -127 783 C ATOM 4412 O GLN A 621 4.409 238.329 811.448 1.00 53.96 O ANISOU 4412 O GLN A 621 6959 7670 5875 267 -160 765 O ATOM 4413 N LEU A 622 4.794 240.409 810.858 1.00 58.00 N ANISOU 4413 N LEU A 622 7435 8232 6371 343 -127 874 N ATOM 4414 CA LEU A 622 5.858 240.012 809.977 1.00 49.23 C ANISOU 4414 CA LEU A 622 6375 7140 5192 327 -186 951 C ATOM 4415 CB LEU A 622 6.419 241.233 809.290 1.00 50.03 C ANISOU 4415 CB LEU A 622 6486 7306 5216 357 -181 1084 C ATOM 4416 CG LEU A 622 6.591 241.239 807.780 1.00 50.67 C ANISOU 4416 CG LEU A 622 6569 7409 5276 315 -266 1276 C ATOM 4417 CD1 LEU A 622 7.604 242.239 807.455 1.00 44.80 C ANISOU 4417 CD1 LEU A 622 5907 6759 4359 336 -261 1390 C ATOM 4418 CD2 LEU A 622 7.008 239.929 807.260 1.00 37.05 C ANISOU 4418 CD2 LEU A 622 4882 5655 3540 270 -376 1276 C ATOM 4419 C LEU A 622 6.967 239.362 810.714 1.00 54.69 C ANISOU 4419 C LEU A 622 7172 7811 5798 332 -213 867 C ATOM 4420 O LEU A 622 7.427 238.331 810.322 1.00 67.42 O ANISOU 4420 O LEU A 622 8824 9405 7387 284 -282 876 O ATOM 4421 N LEU A 623 7.382 239.951 811.813 1.00 49.99 N ANISOU 4421 N LEU A 623 6624 7209 5161 392 -174 799 N ATOM 4422 CA LEU A 623 8.471 239.389 812.576 1.00 47.48 C ANISOU 4422 CA LEU A 623 6429 6847 4763 408 -211 732 C ATOM 4423 CB LEU A 623 8.879 240.323 813.690 1.00 45.81 C ANISOU 4423 CB LEU A 623 6262 6640 4505 504 -171 686 C ATOM 4424 CG LEU A 623 9.635 241.485 813.113 1.00 41.39 C ANISOU 4424 CG LEU A 623 5718 6184 3824 574 -134 753 C ATOM 4425 CD2 LEU A 623 10.152 241.023 811.837 1.00 39.13 C ANISOU 4425 CD2 LEU A 623 5475 5936 3459 515 -191 827 C ATOM 4426 CD1 LEU A 623 10.751 241.803 813.989 1.00 50.11 C ANISOU 4426 CD1 LEU A 623 6942 7294 4805 669 -133 695 C ATOM 4427 C LEU A 623 8.146 238.038 813.139 1.00 46.32 C ANISOU 4427 C LEU A 623 6308 6625 4667 333 -249 679 C ATOM 4428 O LEU A 623 8.972 237.158 813.159 1.00 55.53 O ANISOU 4428 O LEU A 623 7566 7753 5779 294 -315 670 O ATOM 4429 N SER A 624 6.939 237.870 813.622 1.00 45.32 N ANISOU 4429 N SER A 624 6116 6487 4618 301 -215 655 N ATOM 4430 CA SER A 624 6.583 236.601 814.153 1.00 46.74 C ANISOU 4430 CA SER A 624 6330 6628 4802 214 -243 634 C ATOM 4431 CB SER A 624 5.196 236.661 814.699 1.00 54.21 C ANISOU 4431 CB SER A 624 7228 7593 5777 189 -205 614 C ATOM 4432 OG SER A 624 5.001 237.933 815.223 1.00 66.39 O ANISOU 4432 OG SER A 624 8758 9140 7328 267 -181 596 O ATOM 4433 C SER A 624 6.653 235.644 813.020 1.00 45.79 C ANISOU 4433 C SER A 624 6169 6535 4694 149 -277 683 C ATOM 4434 O SER A 624 7.128 234.561 813.157 1.00 56.80 O ANISOU 4434 O SER A 624 7620 7906 6055 77 -329 691 O ATOM 4435 N ILE A 625 6.191 236.040 811.865 1.00 31.41 N ANISOU 4435 N ILE A 625 4253 4764 2919 168 -266 735 N ATOM 4436 CA ILE A 625 6.255 235.120 810.774 1.00 41.29 C ANISOU 4436 CA ILE A 625 5464 6039 4184 115 -328 806 C ATOM 4437 CB ILE A 625 5.625 235.668 809.539 1.00 50.81 C ANISOU 4437 CB ILE A 625 6575 7276 5453 147 -337 898 C ATOM 4438 CG2 ILE A 625 5.964 234.816 808.400 1.00 35.03 C ANISOU 4438 CG2 ILE A 625 4550 5284 3474 109 -455 1006 C ATOM 4439 CG1 ILE A 625 4.119 235.689 809.698 1.00 48.30 C ANISOU 4439 CG1 ILE A 625 6176 6972 5205 156 -262 869 C ATOM 4440 CD1 ILE A 625 3.430 236.132 808.507 1.00 48.91 C ANISOU 4440 CD1 ILE A 625 6170 7043 5371 190 -289 979 C ATOM 4441 C ILE A 625 7.694 234.823 810.516 1.00 49.37 C ANISOU 4441 C ILE A 625 6589 7044 5126 99 -425 832 C ATOM 4442 O ILE A 625 8.043 233.719 810.228 1.00 60.10 O ANISOU 4442 O ILE A 625 7963 8399 6474 31 -507 863 O ATOM 4443 N HIS A 626 8.541 235.824 810.609 1.00 53.72 N ANISOU 4443 N HIS A 626 7215 7597 5599 165 -425 823 N ATOM 4444 CA HIS A 626 9.954 235.626 810.395 1.00 56.92 C ANISOU 4444 CA HIS A 626 7753 7997 5876 162 -526 833 C ATOM 4445 CB HIS A 626 10.684 236.935 810.521 1.00 61.76 C ANISOU 4445 CB HIS A 626 8442 8653 6373 256 -488 827 C ATOM 4446 CG HIS A 626 10.668 237.769 809.288 1.00 62.60 C ANISOU 4446 CG HIS A 626 8516 8850 6419 269 -508 952 C ATOM 4447 CD2 HIS A 626 9.798 237.826 808.264 1.00 66.60 C ANISOU 4447 CD2 HIS A 626 8911 9378 7014 234 -530 1068 C ATOM 4448 NE2 HIS A 626 10.261 238.775 807.395 1.00 66.76 N ANISOU 4448 NE2 HIS A 626 8979 9483 6904 251 -565 1203 N ATOM 4449 CE1 HIS A 626 11.377 239.280 807.868 1.00 63.88 C ANISOU 4449 CE1 HIS A 626 8750 9171 6350 297 -546 1153 C ATOM 4450 ND1 HIS A 626 11.646 238.690 809.013 1.00 61.27 N ANISOU 4450 ND1 HIS A 626 8456 8766 6057 319 -516 995 N ATOM 4451 C HIS A 626 10.544 234.722 811.423 1.00 59.73 C ANISOU 4451 C HIS A 626 8214 8276 6204 122 -563 761 C ATOM 4452 O HIS A 626 11.363 233.904 811.111 1.00 77.61 O ANISOU 4452 O HIS A 626 10560 10524 8405 68 -684 779 O ATOM 4453 N TYR A 627 10.150 234.875 812.668 1.00 39.40 N ANISOU 4453 N TYR A 627 5653 5650 3668 143 -488 696 N ATOM 4454 CA TYR A 627 10.733 234.064 813.706 1.00 43.44 C ANISOU 4454 CA TYR A 627 6292 6073 4140 96 -544 660 C ATOM 4455 CB TYR A 627 10.155 234.492 815.039 1.00 36.82 C ANISOU 4455 CB TYR A 627 5471 5189 3332 132 -478 622 C ATOM 4456 CG TYR A 627 10.671 233.763 816.240 1.00 43.68 C ANISOU 4456 CG TYR A 627 6495 5952 4150 83 -551 617 C ATOM 4457 CD2 TYR A 627 11.939 233.941 816.677 1.00 48.30 C ANISOU 4457 CD2 TYR A 627 7240 6462 4649 149 -632 581 C ATOM 4458 CE2 TYR A 627 12.395 233.297 817.756 1.00 52.98 C ANISOU 4458 CE2 TYR A 627 7990 6940 5199 106 -727 593 C ATOM 4459 CZ TYR A 627 11.588 232.469 818.434 1.00 52.39 C ANISOU 4459 CZ TYR A 627 7918 6841 5147 -23 -734 663 C ATOM 4460 OH TYR A 627 12.063 231.811 819.531 1.00 54.92 O ANISOU 4460 OH TYR A 627 8418 7039 5411 -84 -854 715 O ATOM 4461 CE1 TYR A 627 10.325 232.270 818.031 1.00 47.36 C ANISOU 4461 CE1 TYR A 627 7127 6304 4564 -94 -637 693 C ATOM 4462 CD1 TYR A 627 9.868 232.916 816.950 1.00 42.09 C ANISOU 4462 CD1 TYR A 627 6299 5735 3960 -32 -550 660 C ATOM 4463 C TYR A 627 10.466 232.612 813.463 1.00 53.79 C ANISOU 4463 C TYR A 627 7578 7383 5479 -42 -604 710 C ATOM 4464 O TYR A 627 11.350 231.804 813.555 1.00 53.33 O ANISOU 4464 O TYR A 627 7626 7275 5362 -103 -716 722 O ATOM 4465 N ARG A 628 9.243 232.269 813.116 1.00 58.98 N ANISOU 4465 N ARG A 628 8094 8105 6212 -88 -538 744 N ATOM 4466 CA ARG A 628 8.904 230.872 812.853 1.00 50.12 C ANISOU 4466 CA ARG A 628 6927 7020 5097 -215 -577 806 C ATOM 4467 CB ARG A 628 7.426 230.700 812.501 1.00 39.24 C ANISOU 4467 CB ARG A 628 5398 5738 3772 -229 -476 826 C ATOM 4468 CG ARG A 628 7.146 229.451 811.670 1.00 43.10 C ANISOU 4468 CG ARG A 628 5795 6309 4271 -316 -521 913 C ATOM 4469 CD ARG A 628 5.662 229.278 811.387 1.00 52.76 C ANISOU 4469 CD ARG A 628 6899 7640 5509 -312 -398 917 C ATOM 4470 NE ARG A 628 4.888 229.242 812.623 1.00 73.14 N ANISOU 4470 NE ARG A 628 9550 10243 7998 -369 -273 853 N ATOM 4471 CZ ARG A 628 4.300 228.154 813.113 1.00 78.19 C ANISOU 4471 CZ ARG A 628 10218 10974 8517 -511 -170 872 C ATOM 4472 NH2 ARG A 628 3.623 228.224 814.251 1.00 81.15 N ANISOU 4472 NH2 ARG A 628 10688 11364 8780 -572 -81 824 N ATOM 4473 NH1 ARG A 628 4.380 227.001 812.463 1.00 76.33 N ANISOU 4473 NH1 ARG A 628 9922 10822 8256 -607 -136 956 N ATOM 4474 C ARG A 628 9.760 230.325 811.729 1.00 53.45 C ANISOU 4474 C ARG A 628 7346 7455 5508 -243 -724 866 C ATOM 4475 O ARG A 628 10.405 229.295 811.886 1.00 66.96 O ANISOU 4475 O ARG A 628 9122 9138 7181 -340 -837 901 O ATOM 4476 N ILE A 629 9.777 231.021 810.597 1.00 52.89 N ANISOU 4476 N ILE A 629 7210 7424 5461 -168 -754 895 N ATOM 4477 CA ILE A 629 10.559 230.565 809.463 1.00 53.86 C ANISOU 4477 CA ILE A 629 7340 7561 5564 -190 -948 972 C ATOM 4478 CB ILE A 629 10.488 231.531 808.273 1.00 46.76 C ANISOU 4478 CB ILE A 629 6394 6704 4669 -111 -987 1040 C ATOM 4479 CG2 ILE A 629 11.502 231.125 807.213 1.00 34.50 C ANISOU 4479 CG2 ILE A 629 4894 5159 3055 -135 -1247 1126 C ATOM 4480 CG1 ILE A 629 9.072 231.565 807.692 1.00 48.27 C ANISOU 4480 CG1 ILE A 629 6403 6931 5008 -87 -915 1105 C ATOM 4481 CD1 ILE A 629 8.915 232.495 806.505 1.00 43.06 C ANISOU 4481 CD1 ILE A 629 5700 6283 4376 -23 -980 1217 C ATOM 4482 C ILE A 629 12.014 230.412 809.860 1.00 58.28 C ANISOU 4482 C ILE A 629 8088 8061 5997 -207 -1077 925 C ATOM 4483 O ILE A 629 12.607 229.351 809.663 1.00 63.75 O ANISOU 4483 O ILE A 629 8808 8735 6679 -291 -1255 958 O ATOM 4484 N THR A 630 12.584 231.475 810.421 1.00 46.41 N ANISOU 4484 N THR A 630 6706 6529 4397 -118 -1007 846 N ATOM 4485 CA THR A 630 14.000 231.484 810.769 1.00 49.28 C ANISOU 4485 CA THR A 630 7271 6845 4609 -99 -1131 783 C ATOM 4486 CB THR A 630 14.420 232.835 811.363 1.00 52.10 C ANISOU 4486 CB THR A 630 7725 7205 4867 34 -1018 704 C ATOM 4487 CG2 THR A 630 15.779 232.731 812.034 1.00 49.13 C ANISOU 4487 CG2 THR A 630 7567 6766 4333 69 -1130 611 C ATOM 4488 OG1 THR A 630 14.497 233.797 810.308 1.00 60.14 O ANISOU 4488 OG1 THR A 630 8717 8336 5798 93 -1010 757 O ATOM 4489 C THR A 630 14.344 230.360 811.734 1.00 55.86 C ANISOU 4489 C THR A 630 8189 7578 5457 -193 -1206 758 C ATOM 4490 O THR A 630 15.366 229.692 811.579 1.00 59.35 O ANISOU 4490 O THR A 630 8746 7985 5818 -242 -1410 743 O ATOM 4491 N LEU A 631 13.476 230.147 812.716 1.00 47.75 N ANISOU 4491 N LEU A 631 7113 6511 4518 -231 -1070 763 N ATOM 4492 CA LEU A 631 13.676 229.091 813.700 1.00 45.72 C ANISOU 4492 CA LEU A 631 6947 6165 4258 -346 -1137 787 C ATOM 4493 CB LEU A 631 12.508 229.051 814.688 1.00 47.08 C ANISOU 4493 CB LEU A 631 7066 6337 4486 -386 -973 815 C ATOM 4494 CG LEU A 631 12.885 228.972 816.171 1.00 56.51 C ANISOU 4494 CG LEU A 631 8442 7401 5630 -403 -1005 813 C ATOM 4495 CD1 LEU A 631 11.699 228.535 817.033 1.00 48.51 C ANISOU 4495 CD1 LEU A 631 7393 6414 4623 -505 -900 888 C ATOM 4496 CD2 LEU A 631 14.065 228.034 816.350 1.00 58.28 C ANISOU 4496 CD2 LEU A 631 8828 7522 5794 -491 -1217 845 C ATOM 4497 C LEU A 631 13.823 227.741 813.010 1.00 54.21 C ANISOU 4497 C LEU A 631 7963 7275 5359 -488 -1304 873 C ATOM 4498 O LEU A 631 14.727 226.969 813.327 1.00 53.36 O ANISOU 4498 O LEU A 631 7978 7091 5207 -567 -1492 878 O ATOM 4499 N GLN A 632 12.939 227.476 812.053 1.00 54.52 N ANISOU 4499 N GLN A 632 7805 7428 5482 -510 -1266 941 N ATOM 4500 CA GLN A 632 12.900 226.193 811.352 1.00 53.18 C ANISOU 4500 CA GLN A 632 7514 7317 5376 -626 -1439 1037 C ATOM 4501 CB GLN A 632 11.624 226.091 810.514 1.00 58.87 C ANISOU 4501 CB GLN A 632 7999 8163 6205 -604 -1344 1108 C ATOM 4502 CG GLN A 632 10.329 226.062 811.318 1.00 45.71 C ANISOU 4502 CG GLN A 632 6293 6556 4518 -638 -1076 1122 C ATOM 4503 CD GLN A 632 9.090 226.071 810.435 1.00 52.35 C ANISOU 4503 CD GLN A 632 6926 7520 5445 -583 -994 1166 C ATOM 4504 NE2 GLN A 632 7.946 225.763 811.031 1.00 57.47 N ANISOU 4504 NE2 GLN A 632 7554 8256 6027 -642 -770 1179 N ATOM 4505 OE1 GLN A 632 9.162 226.351 809.235 1.00 51.35 O ANISOU 4505 OE1 GLN A 632 6674 7402 5437 -489 -1136 1192 O ATOM 4506 C GLN A 632 14.123 225.952 810.466 1.00 57.41 C ANISOU 4506 C GLN A 632 8084 7830 5898 -620 -1746 1013 C ATOM 4507 O GLN A 632 14.656 224.848 810.425 1.00 53.48 O ANISOU 4507 O GLN A 632 7554 7318 5447 -736 -1984 1031 O ATOM 4508 N VAL A 633 14.553 226.978 809.744 1.00 64.23 N ANISOU 4508 N VAL A 633 9003 8708 6692 -500 -1767 968 N ATOM 4509 CA VAL A 633 15.752 226.860 808.923 1.00 61.48 C ANISOU 4509 CA VAL A 633 8735 8361 6264 -495 -2069 936 C ATOM 4510 CB VAL A 633 16.065 228.160 808.154 1.00 59.80 C ANISOU 4510 CB VAL A 633 8606 8209 5904 -370 -2041 928 C ATOM 4511 CG1 VAL A 633 17.480 228.118 807.601 1.00 58.95 C ANISOU 4511 CG1 VAL A 633 8669 8121 5607 -372 -2346 864 C ATOM 4512 CG2 VAL A 633 15.060 228.379 807.039 1.00 60.77 C ANISOU 4512 CG2 VAL A 633 8526 8403 6159 -340 -2021 1061 C ATOM 4513 C VAL A 633 16.960 226.486 809.777 1.00 59.39 C ANISOU 4513 C VAL A 633 8678 8000 5885 -542 -2218 822 C ATOM 4514 O VAL A 633 17.748 225.635 809.387 1.00 66.96 O ANISOU 4514 O VAL A 633 9631 8946 6863 -627 -2533 785 O ATOM 4515 N LEU A 634 17.106 227.124 810.936 1.00 55.61 N ANISOU 4515 N LEU A 634 8364 7447 5320 -483 -2031 750 N ATOM 4516 CA LEU A 634 18.203 226.815 811.853 1.00 58.52 C ANISOU 4516 CA LEU A 634 8940 7698 5596 -507 -2183 638 C ATOM 4517 CB LEU A 634 18.212 227.791 813.031 1.00 56.98 C ANISOU 4517 CB LEU A 634 8891 7427 5332 -387 -1969 576 C ATOM 4518 CG LEU A 634 18.811 229.174 812.803 1.00 49.34 C ANISOU 4518 CG LEU A 634 8034 6524 4189 -208 -1892 464 C ATOM 4519 CD2 LEU A 634 20.217 229.050 812.275 1.00 54.87 C ANISOU 4519 CD2 LEU A 634 8901 7256 4690 -197 -2165 324 C ATOM 4520 CD1 LEU A 634 18.802 229.953 814.097 1.00 56.77 C ANISOU 4520 CD1 LEU A 634 9076 7379 5115 -92 -1734 404 C ATOM 4521 C LEU A 634 18.067 225.393 812.378 1.00 68.24 C ANISOU 4521 C LEU A 634 10107 8860 6961 -691 -2331 702 C ATOM 4522 O LEU A 634 19.056 224.681 812.576 1.00 71.13 O ANISOU 4522 O LEU A 634 10557 9148 7321 -781 -2622 606 O ATOM 4523 N LEU A 635 16.820 225.001 812.611 1.00 68.98 N ANISOU 4523 N LEU A 635 10043 8999 7168 -762 -2139 847 N ATOM 4524 CA LEU A 635 16.478 223.642 813.001 1.00 65.55 C ANISOU 4524 CA LEU A 635 9495 8538 6872 -962 -2208 946 C ATOM 4525 CB LEU A 635 14.956 223.491 813.025 1.00 58.97 C ANISOU 4525 CB LEU A 635 8487 7811 6107 -999 -1909 1084 C ATOM 4526 CG LEU A 635 14.359 222.142 813.412 1.00 65.20 C ANISOU 4526 CG LEU A 635 9093 8521 7159 -1242 -1740 1158 C ATOM 4527 CD1 LEU A 635 14.738 221.791 814.834 1.00 67.94 C ANISOU 4527 CD1 LEU A 635 9654 8688 7473 -1361 -1704 1218 C ATOM 4528 CD2 LEU A 635 12.855 222.187 813.261 1.00 72.29 C ANISOU 4528 CD2 LEU A 635 9830 9574 8062 -1243 -1436 1232 C ATOM 4529 C LEU A 635 17.099 222.603 812.062 1.00 70.49 C ANISOU 4529 C LEU A 635 9920 9108 7757 -1099 -2448 872 C ATOM 4530 O LEU A 635 17.600 221.571 812.513 1.00 86.57 O ANISOU 4530 O LEU A 635 11916 10961 10015 -1285 -2519 839 O ATOM 4531 N THR A 636 17.068 222.873 810.760 1.00 52.49 N ANISOU 4531 N THR A 636 7504 6967 5472 -1015 -2595 860 N ATOM 4532 CA THR A 636 17.590 221.915 809.792 1.00 56.20 C ANISOU 4532 CA THR A 636 7749 7391 6212 -1133 -2867 800 C ATOM 4533 CB THR A 636 17.249 222.292 808.327 1.00 62.26 C ANISOU 4533 CB THR A 636 8340 8317 6997 -1018 -3015 855 C ATOM 4534 OG1 THR A 636 18.123 223.334 807.866 1.00 59.00 O ANISOU 4534 OG1 THR A 636 8190 7978 6249 -872 -3200 804 O ATOM 4535 CG2 THR A 636 15.803 222.735 808.208 1.00 54.77 C ANISOU 4535 CG2 THR A 636 7257 7472 6081 -929 -2703 986 C ATOM 4536 C THR A 636 19.093 221.745 809.945 1.00 64.28 C ANISOU 4536 C THR A 636 8961 8297 7166 -1179 -3183 627 C ATOM 4537 O THR A 636 19.612 220.634 809.839 1.00 69.58 O ANISOU 4537 O THR A 636 9482 8822 8131 -1361 -3359 556 O ATOM 4538 N PHE A 637 19.790 222.849 810.197 1.00 68.10 N ANISOU 4538 N PHE A 637 9759 8839 7275 -1020 -3244 536 N ATOM 4539 CA PHE A 637 21.240 222.816 810.373 1.00 77.40 C ANISOU 4539 CA PHE A 637 11149 9916 8344 -1041 -3521 312 C ATOM 4540 CB PHE A 637 21.794 224.235 810.506 1.00 79.06 C ANISOU 4540 CB PHE A 637 11667 10210 8162 -828 -3430 219 C ATOM 4541 CG PHE A 637 21.929 224.960 809.203 1.00 75.79 C ANISOU 4541 CG PHE A 637 11260 9956 7581 -720 -3472 254 C ATOM 4542 CD1 PHE A 637 22.993 224.697 808.364 1.00 80.67 C ANISOU 4542 CD1 PHE A 637 11943 10622 8088 -766 -3849 114 C ATOM 4543 CE1 PHE A 637 23.123 225.365 807.169 1.00 89.75 C ANISOU 4543 CE1 PHE A 637 13130 11931 9041 -686 -3925 184 C ATOM 4544 CZ PHE A 637 22.186 226.308 806.800 1.00 87.93 C ANISOU 4544 CZ PHE A 637 12851 11791 8769 -570 -3616 381 C ATOM 4545 CE2 PHE A 637 21.124 226.581 807.631 1.00 73.54 C ANISOU 4545 CE2 PHE A 637 10938 9905 7098 -526 -3232 476 C ATOM 4546 CD2 PHE A 637 21.001 225.911 808.825 1.00 72.97 C ANISOU 4546 CD2 PHE A 637 10851 9696 7178 -596 -3163 419 C ATOM 4547 C PHE A 637 21.642 221.994 811.592 1.00 68.35 C ANISOU 4547 C PHE A 637 10048 8487 7434 -1195 -3482 242 C ATOM 4548 O PHE A 637 22.672 221.319 811.585 1.00 65.19 O ANISOU 4548 O PHE A 637 9669 7924 7176 -1315 -3747 67 O ATOM 4549 N VAL A 638 20.831 222.049 812.627 1.00 55.37 N ANISOU 4549 N VAL A 638 8426 6775 5837 -1201 -3176 387 N ATOM 4550 CA VAL A 638 21.131 221.280 813.795 1.00 58.61 C ANISOU 4550 CA VAL A 638 8891 6903 6475 -1357 -3143 385 C ATOM 4551 CB VAL A 638 20.167 221.598 814.889 1.00 60.96 C ANISOU 4551 CB VAL A 638 9263 7181 6717 -1326 -2826 578 C ATOM 4552 CG2 VAL A 638 20.445 222.944 815.434 1.00 63.51 C ANISOU 4552 CG2 VAL A 638 9849 7550 6731 -1084 -2786 501 C ATOM 4553 CG1 VAL A 638 20.260 220.575 815.944 1.00 57.69 C ANISOU 4553 CG1 VAL A 638 8854 6483 6581 -1544 -2788 666 C ATOM 4554 C VAL A 638 21.027 219.801 813.542 1.00 75.20 C ANISOU 4554 C VAL A 638 10716 8872 8987 -1629 -3202 439 C ATOM 4555 O VAL A 638 21.904 219.059 813.915 1.00 86.55 O ANISOU 4555 O VAL A 638 12176 10065 10645 -1781 -3384 331 O ATOM 4556 N LEU A 639 19.958 219.356 812.905 1.00 74.57 N ANISOU 4556 N LEU A 639 10350 8938 9045 -1696 -3040 591 N ATOM 4557 CA LEU A 639 19.824 217.934 812.655 1.00 64.76 C ANISOU 4557 CA LEU A 639 8794 7581 8229 -1962 -3054 631 C ATOM 4558 CB LEU A 639 18.435 217.657 812.142 1.00 67.31 C ANISOU 4558 CB LEU A 639 8823 8089 8665 -1989 -2767 786 C ATOM 4559 CG LEU A 639 17.324 218.236 812.975 1.00 69.42 C ANISOU 4559 CG LEU A 639 9221 8454 8700 -1919 -2390 946 C ATOM 4560 CD1 LEU A 639 16.051 218.144 812.226 1.00 64.42 C ANISOU 4560 CD1 LEU A 639 8304 8023 8148 -1896 -2155 1017 C ATOM 4561 CD2 LEU A 639 17.234 217.419 814.196 1.00 72.83 C ANISOU 4561 CD2 LEU A 639 9714 8696 9262 -2150 -2215 1067 C ATOM 4562 C LEU A 639 20.793 217.308 811.679 1.00 73.50 C ANISOU 4562 C LEU A 639 9738 8629 9559 -2048 -3444 456 C ATOM 4563 O LEU A 639 21.418 216.315 811.982 1.00 88.44 O ANISOU 4563 O LEU A 639 11547 10293 11764 -2267 -3575 395 O ATOM 4564 N PHE A 640 20.959 217.889 810.506 1.00 74.58 N ANISOU 4564 N PHE A 640 9838 8960 9540 -1888 -3661 383 N ATOM 4565 CA PHE A 640 21.884 217.291 809.584 1.00 88.29 C ANISOU 4565 CA PHE A 640 11431 10648 11466 -1975 -4082 224 C ATOM 4566 CB PHE A 640 21.306 217.175 808.200 1.00 90.29 C ANISOU 4566 CB PHE A 640 11366 11086 11856 -1924 -4197 294 C ATOM 4567 CG PHE A 640 19.843 217.026 808.160 1.00 83.70 C ANISOU 4567 CG PHE A 640 10275 10345 11183 -1915 -3805 486 C ATOM 4568 CD2 PHE A 640 19.043 218.121 808.086 1.00 80.34 C ANISOU 4568 CD2 PHE A 640 9979 10102 10444 -1701 -3589 593 C ATOM 4569 CE2 PHE A 640 17.702 217.979 808.019 1.00 79.89 C ANISOU 4569 CE2 PHE A 640 9688 10126 10541 -1694 -3243 723 C ATOM 4570 CZ PHE A 640 17.145 216.746 808.019 1.00 83.20 C ANISOU 4570 CZ PHE A 640 9737 10467 11407 -1900 -3077 745 C ATOM 4571 CE1 PHE A 640 17.926 215.654 808.085 1.00 84.72 C ANISOU 4571 CE1 PHE A 640 9781 10488 11923 -2122 -3270 663 C ATOM 4572 CD1 PHE A 640 19.266 215.789 808.147 1.00 84.93 C ANISOU 4572 CD1 PHE A 640 10041 10410 11819 -2130 -3650 536 C ATOM 4573 C PHE A 640 22.969 218.259 809.482 1.00100.60 C ANISOU 4573 C PHE A 640 13347 12260 12616 -1812 -4345 37 C ATOM 4574 O PHE A 640 22.784 219.338 808.986 1.00113.87 O ANISOU 4574 O PHE A 640 15171 14162 13932 -1603 -4331 70 O ATOM 4575 N ASP A 641 24.143 217.886 809.927 1.00103.90 N ANISOU 4575 N ASP A 641 13912 12472 13095 -1915 -4583 -177 N ATOM 4576 CA ASP A 641 25.183 218.860 809.811 1.00114.39 C ANISOU 4576 CA ASP A 641 15590 13880 13992 -1751 -4800 -401 C ATOM 4577 CB ASP A 641 26.197 218.738 810.931 1.00117.47 C ANISOU 4577 CB ASP A 641 16225 13989 14420 -1808 -4855 -627 C ATOM 4578 CG ASP A 641 25.668 219.273 812.230 1.00106.80 C ANISOU 4578 CG ASP A 641 15041 12541 12997 -1716 -4475 -506 C ATOM 4579 OD1 ASP A 641 24.875 218.586 812.885 1.00 97.71 O ANISOU 4579 OD1 ASP A 641 13730 11251 12145 -1855 -4240 -289 O ATOM 4580 OD2 ASP A 641 26.044 220.389 812.590 1.00108.19 O ANISOU 4580 OD2 ASP A 641 15503 12791 12812 -1510 -4412 -628 O ATOM 4581 C ASP A 641 25.804 218.798 808.440 1.00117.52 C ANISOU 4581 C ASP A 641 15921 14434 14297 -1750 -5231 -516 C ATOM 4582 O ASP A 641 26.576 217.921 808.099 1.00107.29 O ANISOU 4582 O ASP A 641 14511 13003 13250 -1920 -5581 -679 O ATOM 4583 N LEU A 642 25.444 219.815 807.679 1.00123.52 N ANISOU 4583 N LEU A 642 16773 15482 14679 -1556 -5210 -412 N ATOM 4584 CA LEU A 642 25.904 220.068 806.349 1.00126.93 C ANISOU 4584 CA LEU A 642 17215 16120 14894 -1510 -5597 -445 C ATOM 4585 CB LEU A 642 24.929 220.996 805.670 1.00120.03 C ANISOU 4585 CB LEU A 642 16319 15499 13788 -1328 -5423 -181 C ATOM 4586 CG LEU A 642 23.586 220.720 806.311 1.00112.37 C ANISOU 4586 CG LEU A 642 15111 14442 13141 -1336 -4979 28 C ATOM 4587 CD2 LEU A 642 23.539 219.245 806.524 1.00116.38 C ANISOU 4587 CD2 LEU A 642 15293 14719 14207 -1568 -5040 -6 C ATOM 4588 CD1 LEU A 642 22.449 221.171 805.446 1.00104.84 C ANISOU 4588 CD1 LEU A 642 13974 13665 12198 -1214 -4866 283 C ATOM 4589 C LEU A 642 27.169 220.797 806.658 1.00132.38 C ANISOU 4589 C LEU A 642 18324 16849 15126 -1442 -5742 -738 C ATOM 4590 O LEU A 642 27.614 220.774 807.797 1.00135.27 O ANISOU 4590 O LEU A 642 18849 17018 15528 -1461 -5591 -912 O ATOM 4591 N ASP A 643 27.774 221.432 805.666 1.00129.80 N ANISOU 4591 N ASP A 643 18181 16765 14372 -1365 -6032 -799 N ATOM 4592 CA ASP A 643 29.028 222.104 805.918 1.00126.76 C ANISOU 4592 CA ASP A 643 18199 16427 13539 -1304 -6119 -1116 C ATOM 4593 CB ASP A 643 29.815 222.198 804.641 1.00132.52 C ANISOU 4593 CB ASP A 643 19041 17346 13966 -1323 -6553 -1182 C ATOM 4594 CG ASP A 643 30.084 220.861 804.068 1.00149.10 C ANISOU 4594 CG ASP A 643 20849 19329 16474 -1541 -7064 -1254 C ATOM 4595 OD2 ASP A 643 31.093 220.714 803.359 1.00162.25 O ANISOU 4595 OD2 ASP A 643 22652 21077 17918 -1611 -7521 -1457 O ATOM 4596 OD1 ASP A 643 29.285 219.948 804.354 1.00149.79 O ANISOU 4596 OD1 ASP A 643 20559 19220 17134 -1644 -6961 -1104 O ATOM 4597 C ASP A 643 28.914 223.472 806.492 1.00120.17 C ANISOU 4597 C ASP A 643 17647 15699 12311 -1086 -5666 -1092 C ATOM 4598 O ASP A 643 28.507 224.408 805.840 1.00118.71 O ANISOU 4598 O ASP A 643 17532 15721 11850 -949 -5486 -879 O ATOM 4599 N THR A 644 29.360 223.573 807.722 1.00115.24 N ANISOU 4599 N THR A 644 17177 14911 11698 -1072 -5516 -1340 N ATOM 4600 CA THR A 644 29.358 224.809 808.415 1.00114.76 C ANISOU 4600 CA THR A 644 17348 14920 11335 -871 -5116 -1377 C ATOM 4601 CB THR A 644 30.040 224.665 809.714 1.00120.61 C ANISOU 4601 CB THR A 644 18233 15422 12171 -887 -5095 -1717 C ATOM 4602 CG2 THR A 644 30.024 225.977 810.420 1.00126.16 C ANISOU 4602 CG2 THR A 644 19134 16204 12597 -661 -4693 -1766 C ATOM 4603 OG1 THR A 644 29.291 223.744 810.502 1.00121.57 O ANISOU 4603 OG1 THR A 644 18108 15247 12837 -994 -4985 -1537 O ATOM 4604 C THR A 644 30.270 225.593 807.546 1.00126.25 C ANISOU 4604 C THR A 644 19066 16634 12271 -803 -5251 -1530 C ATOM 4605 O THR A 644 30.242 226.803 807.531 1.00137.46 O ANISOU 4605 O THR A 644 20652 18238 13337 -643 -4949 -1489 O ATOM 4606 N GLU A 645 31.125 224.892 806.831 1.00128.88 N ANISOU 4606 N GLU A 645 19436 16987 12547 -947 -5724 -1723 N ATOM 4607 CA GLU A 645 32.058 225.570 805.968 1.00129.37 C ANISOU 4607 CA GLU A 645 19784 17324 12046 -914 -5906 -1881 C ATOM 4608 CB GLU A 645 33.027 224.575 805.327 1.00147.36 C ANISOU 4608 CB GLU A 645 22082 19570 14338 -1106 -6506 -2142 C ATOM 4609 CG GLU A 645 32.346 223.442 804.576 1.00165.00 C ANISOU 4609 CG GLU A 645 23940 21712 17040 -1253 -6830 -1860 C ATOM 4610 CD GLU A 645 33.338 222.518 803.894 1.00186.76 C ANISOU 4610 CD GLU A 645 26693 24445 19822 -1446 -7462 -2124 C ATOM 4611 OE2 GLU A 645 32.918 221.448 803.403 1.00192.11 O ANISOU 4611 OE2 GLU A 645 27014 25004 20976 -1591 -7769 -1971 O ATOM 4612 OE1 GLU A 645 34.537 222.864 803.844 1.00194.38 O ANISOU 4612 OE1 GLU A 645 27998 25517 20342 -1458 -7653 -2504 O ATOM 4613 C GLU A 645 31.309 226.334 804.912 1.00117.63 C ANISOU 4613 C GLU A 645 18265 16096 10334 -833 -5775 -1470 C ATOM 4614 O GLU A 645 31.619 227.463 804.607 1.00115.68 O ANISOU 4614 O GLU A 645 18263 16096 9596 -734 -5600 -1474 O ATOM 4615 N ILE A 646 30.297 225.699 804.367 1.00110.88 N ANISOU 4615 N ILE A 646 17089 15170 9873 -886 -5854 -1123 N ATOM 4616 CA ILE A 646 29.508 226.276 803.298 1.00106.86 C ANISOU 4616 CA ILE A 646 16503 14839 9261 -829 -5790 -730 C ATOM 4617 CB ILE A 646 28.862 225.211 802.424 1.00103.30 C ANISOU 4617 CB ILE A 646 15703 14302 9242 -936 -6137 -492 C ATOM 4618 CG2 ILE A 646 27.770 225.818 801.609 1.00105.29 C ANISOU 4618 CG2 ILE A 646 15823 14650 9531 -851 -5964 -83 C ATOM 4619 CG1 ILE A 646 29.855 224.645 801.432 1.00 91.96 C ANISOU 4619 CG1 ILE A 646 14347 12963 7632 -1063 -6760 -622 C ATOM 4620 CD1 ILE A 646 29.167 223.991 800.274 1.00 85.77 C ANISOU 4620 CD1 ILE A 646 13235 12166 7187 -1118 -7100 -309 C ATOM 4621 C ILE A 646 28.434 227.271 803.699 1.00101.15 C ANISOU 4621 C ILE A 646 15723 14134 8575 -679 -5231 -474 C ATOM 4622 O ILE A 646 28.154 228.217 802.990 1.00108.36 O ANISOU 4622 O ILE A 646 16718 15235 9219 -614 -5106 -261 O ATOM 4623 N PHE A 647 27.807 227.040 804.832 1.00 90.31 N ANISOU 4623 N PHE A 647 14202 12560 7551 -644 -4921 -488 N ATOM 4624 CA PHE A 647 26.743 227.909 805.280 1.00 89.83 C ANISOU 4624 CA PHE A 647 14062 12496 7575 -516 -4424 -272 C ATOM 4625 CB PHE A 647 25.579 227.059 805.721 1.00 92.23 C ANISOU 4625 CB PHE A 647 14043 12599 8401 -562 -4308 -102 C ATOM 4626 CG PHE A 647 24.986 226.262 804.620 1.00 93.93 C ANISOU 4626 CG PHE A 647 13994 12818 8878 -653 -4581 111 C ATOM 4627 CD2 PHE A 647 24.990 224.900 804.662 1.00 94.83 C ANISOU 4627 CD2 PHE A 647 13884 12796 9352 -797 -4869 57 C ATOM 4628 CE2 PHE A 647 24.440 224.183 803.657 1.00 95.33 C ANISOU 4628 CE2 PHE A 647 13653 12865 9705 -865 -5125 236 C ATOM 4629 CZ PHE A 647 23.886 224.817 802.594 1.00 96.82 C ANISOU 4629 CZ PHE A 647 13800 13173 9815 -783 -5121 482 C ATOM 4630 CE1 PHE A 647 23.872 226.163 802.540 1.00100.22 C ANISOU 4630 CE1 PHE A 647 14476 13729 9876 -662 -4842 552 C ATOM 4631 CD1 PHE A 647 24.418 226.882 803.542 1.00 98.49 C ANISOU 4631 CD1 PHE A 647 14520 13526 9377 -601 -4564 364 C ATOM 4632 C PHE A 647 27.046 228.944 806.328 1.00 88.64 C ANISOU 4632 C PHE A 647 14105 12366 7207 -383 -4052 -441 C ATOM 4633 O PHE A 647 26.169 229.390 807.013 1.00 87.19 O ANISOU 4633 O PHE A 647 13808 12106 7215 -298 -3686 -316 O ATOM 4634 N GLY A 648 28.283 229.334 806.484 1.00 96.53 N ANISOU 4634 N GLY A 648 15387 13473 7816 -362 -4152 -750 N ATOM 4635 CA GLY A 648 28.551 230.316 807.503 1.00 98.95 C ANISOU 4635 CA GLY A 648 15838 13799 7960 -221 -3799 -931 C ATOM 4636 C GLY A 648 27.926 231.688 807.421 1.00 92.07 C ANISOU 4636 C GLY A 648 14955 13089 6937 -95 -3391 -734 C ATOM 4637 O GLY A 648 27.431 232.150 808.422 1.00 84.39 O ANISOU 4637 O GLY A 648 13905 12013 6147 11 -3076 -734 O ATOM 4638 N GLN A 649 27.970 232.352 806.279 1.00 93.41 N ANISOU 4638 N GLN A 649 15203 13505 6781 -117 -3421 -570 N ATOM 4639 CA GLN A 649 27.348 233.653 806.235 1.00 87.06 C ANISOU 4639 CA GLN A 649 14363 12836 5879 -23 -3039 -383 C ATOM 4640 CB GLN A 649 27.641 234.432 804.959 1.00 76.69 C ANISOU 4640 CB GLN A 649 13210 11825 4102 -76 -3111 -224 C ATOM 4641 CG GLN A 649 28.575 235.611 805.203 1.00 71.62 C ANISOU 4641 CG GLN A 649 12839 11451 2922 -17 -2891 -451 C ATOM 4642 CD GLN A 649 29.084 236.255 803.940 1.00 82.79 C ANISOU 4642 CD GLN A 649 14489 13202 3765 -113 -3014 -317 C ATOM 4643 NE2 GLN A 649 30.369 236.539 803.898 1.00 80.61 N ANISOU 4643 NE2 GLN A 649 14538 13165 2925 -140 -3079 -638 N ATOM 4644 OE1 GLN A 649 28.333 236.503 803.022 1.00 77.72 O ANISOU 4644 OE1 GLN A 649 13752 12607 3172 -167 -3052 60 O ATOM 4645 C GLN A 649 25.877 233.451 806.455 1.00 86.02 C ANISOU 4645 C GLN A 649 13912 12507 6263 -5 -2854 -101 C ATOM 4646 O GLN A 649 25.242 234.222 807.140 1.00 96.73 O ANISOU 4646 O GLN A 649 15169 13829 7755 94 -2510 -53 O ATOM 4647 N HIS A 650 25.318 232.410 805.879 1.00 73.97 N ANISOU 4647 N HIS A 650 12217 10862 5028 -103 -3088 63 N ATOM 4648 CA HIS A 650 23.915 232.209 806.092 1.00 73.06 C ANISOU 4648 CA HIS A 650 11811 10586 5363 -94 -2888 278 C ATOM 4649 C HIS A 650 23.623 231.958 807.539 1.00 71.10 C ANISOU 4649 C HIS A 650 11494 10142 5379 -39 -2678 151 C ATOM 4650 O HIS A 650 22.731 232.534 808.111 1.00 77.35 O ANISOU 4650 O HIS A 650 12155 10879 6355 31 -2371 237 O ATOM 4651 CB HIS A 650 23.461 230.996 805.328 1.00 83.53 C ANISOU 4651 CB HIS A 650 12959 11822 6957 -210 -3185 420 C ATOM 4652 CG HIS A 650 23.417 231.208 803.862 1.00 97.29 C ANISOU 4652 CG HIS A 650 14706 13715 8545 -256 -3413 629 C ATOM 4653 CD2 HIS A 650 23.795 230.420 802.836 1.00102.46 C ANISOU 4653 CD2 HIS A 650 15354 14404 9173 -350 -3853 694 C ATOM 4654 NE2 HIS A 650 23.523 231.107 801.681 1.00107.71 N ANISOU 4654 NE2 HIS A 650 16041 15211 9675 -352 -3931 946 N ATOM 4655 CE1 HIS A 650 22.991 232.274 801.991 1.00107.00 C ANISOU 4655 CE1 HIS A 650 15962 15173 9520 -273 -3535 1022 C ATOM 4656 ND1 HIS A 650 22.913 232.358 803.303 1.00104.78 N ANISOU 4656 ND1 HIS A 650 15660 14790 9362 -209 -3222 824 N ATOM 4657 N ILE A 651 24.392 231.095 808.151 1.00 71.07 N ANISOU 4657 N ILE A 651 11586 10027 5392 -81 -2877 -58 N ATOM 4658 CA ILE A 651 24.138 230.799 809.528 1.00 72.66 C ANISOU 4658 CA ILE A 651 11746 10029 5831 -46 -2731 -144 C ATOM 4659 CB ILE A 651 24.950 229.668 810.007 1.00 78.41 C ANISOU 4659 CB ILE A 651 12560 10616 6617 -140 -3031 -349 C ATOM 4660 CG2 ILE A 651 25.039 229.746 811.473 1.00 81.51 C ANISOU 4660 CG2 ILE A 651 13016 10839 7116 -72 -2898 -485 C ATOM 4661 CG1 ILE A 651 24.256 228.373 809.657 1.00 74.71 C ANISOU 4661 CG1 ILE A 651 11870 10037 6478 -298 -3204 -182 C ATOM 4662 CD1 ILE A 651 24.870 227.213 810.313 1.00 80.04 C ANISOU 4662 CD1 ILE A 651 12574 10535 7304 -424 -3476 -359 C ATOM 4663 C ILE A 651 24.365 231.958 810.444 1.00 74.72 C ANISOU 4663 C ILE A 651 12115 10322 5952 111 -2458 -270 C ATOM 4664 O ILE A 651 23.655 232.134 811.397 1.00 70.69 O ANISOU 4664 O ILE A 651 11508 9686 5666 170 -2249 -214 O ATOM 4665 N SER A 652 44.913 228.626 813.048 1.00 76.32 N ANISOU 4665 N SER A 652 12525 10708 5766 175 -2472 -455 N ATOM 4666 CA SER A 652 45.185 229.735 813.921 1.00 71.91 C ANISOU 4666 CA SER A 652 12049 10201 5073 329 -2213 -607 C ATOM 4667 CB SER A 652 46.399 230.488 813.426 1.00 75.11 C ANISOU 4667 CB SER A 652 12699 10863 4978 362 -2236 -844 C ATOM 4668 OG SER A 652 46.065 231.210 812.268 1.00 79.11 O ANISOU 4668 OG SER A 652 13182 11598 5278 327 -2156 -613 O ATOM 4669 C SER A 652 44.016 230.667 813.911 1.00 72.10 C ANISOU 4669 C SER A 652 11880 10270 5247 396 -1901 -356 C ATOM 4670 O SER A 652 43.616 231.165 814.938 1.00 63.86 O ANISOU 4670 O SER A 652 10769 9141 4353 503 -1702 -379 O ATOM 4671 N THR A 653 50.535 218.306 818.803 1.00 68.70 N ANISOU 4671 N THR A 653 11359 9966 4778 331 -1889 -129 N ATOM 4672 CA THR A 653 49.322 219.087 818.784 1.00 59.66 C ANISOU 4672 CA THR A 653 10017 8850 3802 373 -1626 82 C ATOM 4673 CB THR A 653 49.077 219.691 817.441 1.00 57.88 C ANISOU 4673 CB THR A 653 9764 8793 3435 296 -1673 291 C ATOM 4674 CG2 THR A 653 49.744 221.006 817.373 1.00 62.95 C ANISOU 4674 CG2 THR A 653 10584 9696 3637 340 -1564 242 C ATOM 4675 OG1 THR A 653 49.691 218.864 816.467 1.00 72.34 O ANISOU 4675 OG1 THR A 653 11676 10627 5184 183 -2001 303 O ATOM 4676 C THR A 653 48.127 218.283 819.233 1.00 61.69 C ANISOU 4676 C THR A 653 10047 8883 4510 355 -1546 193 C ATOM 4677 O THR A 653 47.289 218.782 819.944 1.00 63.96 O ANISOU 4677 O THR A 653 10209 9133 4959 431 -1324 234 O ATOM 4678 N LEU A 654 48.040 217.030 818.833 1.00 45.59 N ANISOU 4678 N LEU A 654 7955 6711 2655 242 -1733 232 N ATOM 4679 CA LEU A 654 46.900 216.250 819.234 1.00 57.57 C ANISOU 4679 CA LEU A 654 9279 8061 4536 199 -1633 328 C ATOM 4680 CB LEU A 654 47.026 214.847 818.707 1.00 68.58 C ANISOU 4680 CB LEU A 654 10637 9357 6064 55 -1861 361 C ATOM 4681 CG LEU A 654 46.760 214.847 817.237 1.00 73.23 C ANISOU 4681 CG LEU A 654 11117 10048 6658 -22 -1982 506 C ATOM 4682 CD1 LEU A 654 45.358 214.460 816.985 1.00 72.71 C ANISOU 4682 CD1 LEU A 654 10804 9933 6888 -70 -1839 650 C ATOM 4683 CD2 LEU A 654 46.967 216.262 816.905 1.00 75.45 C ANISOU 4683 CD2 LEU A 654 11477 10498 6692 65 -1894 528 C ATOM 4684 C LEU A 654 46.869 216.157 820.709 1.00 58.10 C ANISOU 4684 C LEU A 654 9395 8002 4680 284 -1525 222 C ATOM 4685 O LEU A 654 45.842 216.286 821.316 1.00 53.65 O ANISOU 4685 O LEU A 654 8697 7376 4312 315 -1344 288 O ATOM 4686 N LEU A 655 48.010 215.911 821.293 1.00 43.17 N ANISOU 4686 N LEU A 655 7706 6070 2625 320 -1671 42 N ATOM 4687 CA LEU A 655 48.068 215.809 822.711 1.00 57.19 C ANISOU 4687 CA LEU A 655 9553 7712 4464 412 -1624 -59 C ATOM 4688 CB LEU A 655 49.418 215.279 823.123 1.00 62.58 C ANISOU 4688 CB LEU A 655 10463 8326 4988 412 -1869 -299 C ATOM 4689 CG LEU A 655 49.617 213.866 822.597 1.00 64.93 C ANISOU 4689 CG LEU A 655 10754 8502 5416 226 -2124 -256 C ATOM 4690 CD2 LEU A 655 48.676 212.918 823.245 1.00 51.73 C ANISOU 4690 CD2 LEU A 655 8977 6649 4028 143 -2086 -86 C ATOM 4691 CD1 LEU A 655 51.008 213.416 822.805 1.00 59.80 C ANISOU 4691 CD1 LEU A 655 10312 7790 4618 200 -2410 -544 C ATOM 4692 C LEU A 655 47.756 217.141 823.330 1.00 69.51 C ANISOU 4692 C LEU A 655 11083 9378 5952 575 -1392 -85 C ATOM 4693 O LEU A 655 47.106 217.226 824.335 1.00 66.95 O ANISOU 4693 O LEU A 655 10698 8958 5782 646 -1287 -57 O ATOM 4694 N ASP A 656 48.269 218.201 822.757 1.00 76.73 N ANISOU 4694 N ASP A 656 12050 10504 6599 627 -1330 -140 N ATOM 4695 CA ASP A 656 47.996 219.503 823.313 1.00 77.34 C ANISOU 4695 CA ASP A 656 12083 10711 6591 765 -1102 -160 C ATOM 4696 CB ASP A 656 48.841 220.561 822.613 1.00 76.58 C ANISOU 4696 CB ASP A 656 12112 10884 6102 780 -1053 -243 C ATOM 4697 CG ASP A 656 48.524 221.953 823.062 1.00 72.22 C ANISOU 4697 CG ASP A 656 11495 10501 5444 890 -792 -240 C ATOM 4698 OD2 ASP A 656 49.290 222.515 823.844 1.00 62.27 O ANISOU 4698 OD2 ASP A 656 10358 9335 3966 1003 -700 -483 O ATOM 4699 OD1 ASP A 656 47.526 222.506 822.604 1.00 68.44 O ANISOU 4699 OD1 ASP A 656 10840 10069 5096 858 -673 -24 O ATOM 4700 C ASP A 656 46.539 219.842 823.194 1.00 72.30 C ANISOU 4700 C ASP A 656 11200 10053 6218 749 -936 55 C ATOM 4701 O ASP A 656 45.933 220.293 824.125 1.00 74.55 O ANISOU 4701 O ASP A 656 11400 10305 6620 845 -808 58 O ATOM 4702 N LEU A 657 45.956 219.599 822.047 1.00 58.79 N ANISOU 4702 N LEU A 657 9372 8362 4603 626 -961 212 N ATOM 4703 CA LEU A 657 44.568 219.921 821.880 1.00 44.91 C ANISOU 4703 CA LEU A 657 7386 6592 3085 605 -816 358 C ATOM 4704 CB LEU A 657 44.150 219.679 820.462 1.00 52.55 C ANISOU 4704 CB LEU A 657 8261 7606 4100 479 -882 495 C ATOM 4705 CG LEU A 657 44.784 220.620 819.466 1.00 60.34 C ANISOU 4705 CG LEU A 657 9341 8795 4792 470 -915 556 C ATOM 4706 CD1 LEU A 657 43.894 220.705 818.276 1.00 54.87 C ANISOU 4706 CD1 LEU A 657 8495 8132 4221 380 -935 740 C ATOM 4707 CD2 LEU A 657 44.951 221.958 820.082 1.00 59.12 C ANISOU 4707 CD2 LEU A 657 9223 8782 4458 581 -739 523 C ATOM 4708 C LEU A 657 43.694 219.120 822.771 1.00 49.01 C ANISOU 4708 C LEU A 657 7807 6930 3884 593 -788 362 C ATOM 4709 O LEU A 657 42.748 219.622 823.296 1.00 58.50 O ANISOU 4709 O LEU A 657 8877 8129 5222 640 -657 396 O ATOM 4710 N HIS A 658 44.001 217.851 822.932 1.00 55.33 N ANISOU 4710 N HIS A 658 8684 7591 4749 510 -926 335 N ATOM 4711 CA HIS A 658 43.191 216.978 823.754 1.00 54.49 C ANISOU 4711 CA HIS A 658 8519 7331 4855 460 -911 364 C ATOM 4712 CB HIS A 658 43.809 215.595 823.720 1.00 52.21 C ANISOU 4712 CB HIS A 658 8348 6920 4568 340 -1095 357 C ATOM 4713 CG HIS A 658 43.164 214.602 824.628 1.00 47.91 C ANISOU 4713 CG HIS A 658 7800 6230 4173 259 -1107 410 C ATOM 4714 CD2 HIS A 658 42.371 213.545 824.363 1.00 47.74 C ANISOU 4714 CD2 HIS A 658 7682 6179 4278 94 -1101 509 C ATOM 4715 NE2 HIS A 658 42.084 212.944 825.558 1.00 43.31 N ANISOU 4715 NE2 HIS A 658 7201 5496 3759 60 -1131 546 N ATOM 4716 CE1 HIS A 658 42.689 213.599 826.523 1.00 46.64 C ANISOU 4716 CE1 HIS A 658 7759 5852 4110 214 -1176 470 C ATOM 4717 ND1 HIS A 658 43.362 214.594 825.984 1.00 51.63 N ANISOU 4717 ND1 HIS A 658 8398 6585 4634 340 -1150 374 N ATOM 4718 C HIS A 658 43.191 217.485 825.154 1.00 53.76 C ANISOU 4718 C HIS A 658 8486 7186 4754 599 -864 302 C ATOM 4719 O HIS A 658 42.193 217.511 825.824 1.00 43.92 O ANISOU 4719 O HIS A 658 7142 5896 3650 605 -786 345 O ATOM 4720 N TYR A 659 44.340 217.909 825.607 1.00 57.22 N ANISOU 4720 N TYR A 659 9096 7647 4999 718 -932 183 N ATOM 4721 CA TYR A 659 44.421 218.401 826.939 1.00 58.10 C ANISOU 4721 CA TYR A 659 9266 7720 5088 874 -919 111 C ATOM 4722 CB TYR A 659 45.850 218.766 827.225 1.00 62.24 C ANISOU 4722 CB TYR A 659 9994 8303 5352 992 -1008 -88 C ATOM 4723 CG TYR A 659 46.105 219.405 828.545 1.00 64.65 C ANISOU 4723 CG TYR A 659 10365 8609 5589 1182 -1005 -227 C ATOM 4724 CD2 TYR A 659 46.409 218.655 829.644 1.00 70.60 C ANISOU 4724 CD2 TYR A 659 11256 9168 6401 1227 -1210 -298 C ATOM 4725 CE2 TYR A 659 46.665 219.241 830.831 1.00 75.23 C ANISOU 4725 CE2 TYR A 659 11882 9735 6967 1413 -1238 -466 C ATOM 4726 CZ TYR A 659 46.637 220.591 830.930 1.00 76.54 C ANISOU 4726 CZ TYR A 659 11940 10095 7048 1547 -1005 -583 C ATOM 4727 OH TYR A 659 46.902 221.202 832.117 1.00 75.24 O ANISOU 4727 OH TYR A 659 11666 9787 7133 1745 -944 -775 O ATOM 4728 CE1 TYR A 659 46.351 221.350 829.856 1.00 76.89 C ANISOU 4728 CE1 TYR A 659 11893 10386 6936 1485 -800 -486 C ATOM 4729 CD1 TYR A 659 46.096 220.760 828.675 1.00 71.20 C ANISOU 4729 CD1 TYR A 659 11126 9643 6284 1309 -817 -301 C ATOM 4730 C TYR A 659 43.551 219.604 827.063 1.00 57.98 C ANISOU 4730 C TYR A 659 9079 7834 5117 958 -731 160 C ATOM 4731 O TYR A 659 42.861 219.757 828.025 1.00 65.08 O ANISOU 4731 O TYR A 659 9923 8679 6127 1018 -708 185 O ATOM 4732 N LYS A 660 43.582 220.483 826.090 1.00 48.05 N ANISOU 4732 N LYS A 660 7744 6754 3759 951 -622 188 N ATOM 4733 CA LYS A 660 42.750 221.658 826.150 1.00 38.41 C ANISOU 4733 CA LYS A 660 6357 5659 2579 1010 -460 252 C ATOM 4734 CB LYS A 660 43.194 222.679 825.122 1.00 46.78 C ANISOU 4734 CB LYS A 660 7416 6930 3430 1000 -370 280 C ATOM 4735 CG LYS A 660 44.383 223.478 825.556 1.00 48.61 C ANISOU 4735 CG LYS A 660 7805 7318 3346 1117 -315 132 C ATOM 4736 CD LYS A 660 45.004 224.212 824.417 1.00 57.91 C ANISOU 4736 CD LYS A 660 9052 8710 4241 1054 -252 160 C ATOM 4737 CE LYS A 660 46.450 224.530 824.705 1.00 62.72 C ANISOU 4737 CE LYS A 660 9888 9463 4481 1122 -228 -75 C ATOM 4738 NZ LYS A 660 47.261 224.616 823.474 1.00 65.80 N ANISOU 4738 NZ LYS A 660 10428 10007 4568 1012 -285 -63 N ATOM 4739 C LYS A 660 41.273 221.376 826.053 1.00 42.20 C ANISOU 4739 C LYS A 660 6644 6069 3320 921 -414 358 C ATOM 4740 O LYS A 660 40.496 221.996 826.725 1.00 50.10 O ANISOU 4740 O LYS A 660 7540 7095 4401 983 -343 378 O ATOM 4741 N GLN A 661 40.884 220.454 825.196 1.00 46.60 N ANISOU 4741 N GLN A 661 7157 6564 3985 772 -460 409 N ATOM 4742 CA GLN A 661 39.487 220.091 825.037 1.00 49.08 C ANISOU 4742 CA GLN A 661 7304 6842 4503 678 -413 470 C ATOM 4743 CB GLN A 661 39.341 219.044 823.965 1.00 38.53 C ANISOU 4743 CB GLN A 661 5941 5474 3225 527 -470 510 C ATOM 4744 CG GLN A 661 39.606 219.530 822.613 1.00 46.27 C ANISOU 4744 CG GLN A 661 6882 6566 4133 499 -472 566 C ATOM 4745 CD GLN A 661 40.020 218.432 821.725 1.00 55.46 C ANISOU 4745 CD GLN A 661 8088 7696 5289 381 -589 591 C ATOM 4746 NE2 GLN A 661 40.339 218.754 820.513 1.00 54.40 N ANISOU 4746 NE2 GLN A 661 7946 7653 5069 350 -641 658 N ATOM 4747 OE1 GLN A 661 40.060 217.295 822.124 1.00 60.56 O ANISOU 4747 OE1 GLN A 661 8778 8240 5993 311 -650 569 O ATOM 4748 C GLN A 661 38.961 219.489 826.288 1.00 49.71 C ANISOU 4748 C GLN A 661 7412 6804 4670 680 -446 449 C ATOM 4749 O GLN A 661 37.864 219.719 826.693 1.00 47.89 O ANISOU 4749 O GLN A 661 7074 6586 4536 673 -395 472 O ATOM 4750 N PHE A 662 39.763 218.668 826.901 1.00 53.56 N ANISOU 4750 N PHE A 662 8070 7178 5103 677 -560 415 N ATOM 4751 CA PHE A 662 39.329 218.031 828.096 1.00 56.24 C ANISOU 4751 CA PHE A 662 8474 7400 5496 659 -630 431 C ATOM 4752 CB PHE A 662 40.401 217.096 828.564 1.00 56.28 C ANISOU 4752 CB PHE A 662 8688 7266 5429 641 -791 414 C ATOM 4753 CG PHE A 662 40.029 216.323 829.752 1.00 56.19 C ANISOU 4753 CG PHE A 662 8774 7118 5457 595 -908 475 C ATOM 4754 CD2 PHE A 662 40.350 216.767 830.990 1.00 63.17 C ANISOU 4754 CD2 PHE A 662 9758 7932 6312 747 -1016 458 C ATOM 4755 CE2 PHE A 662 40.024 216.058 832.064 1.00 62.35 C ANISOU 4755 CE2 PHE A 662 9752 7691 6246 697 -1171 555 C ATOM 4756 CZ PHE A 662 39.366 214.899 831.920 1.00 53.42 C ANISOU 4756 CZ PHE A 662 8633 6522 5141 481 -1186 668 C ATOM 4757 CE1 PHE A 662 39.039 214.451 830.706 1.00 42.13 C ANISOU 4757 CE1 PHE A 662 7096 5187 3724 338 -1054 663 C ATOM 4758 CD1 PHE A 662 39.371 215.149 829.630 1.00 45.54 C ANISOU 4758 CD1 PHE A 662 7419 5726 4157 400 -932 568 C ATOM 4759 C PHE A 662 39.068 219.039 829.155 1.00 64.75 C ANISOU 4759 C PHE A 662 9532 8510 6562 813 -610 411 C ATOM 4760 O PHE A 662 38.150 218.915 829.900 1.00 68.81 O ANISOU 4760 O PHE A 662 10010 8993 7141 788 -632 451 O ATOM 4761 N LEU A 663 39.897 220.041 829.267 1.00 67.25 N ANISOU 4761 N LEU A 663 9880 8908 6766 974 -586 351 N ATOM 4762 CA LEU A 663 39.651 221.018 830.287 1.00 62.48 C ANISOU 4762 CA LEU A 663 9236 8360 6145 1129 -577 336 C ATOM 4763 CB LEU A 663 40.811 221.983 830.387 1.00 59.52 C ANISOU 4763 CB LEU A 663 8929 8107 5580 1306 -549 245 C ATOM 4764 CG LEU A 663 41.977 221.481 831.208 1.00 57.49 C ANISOU 4764 CG LEU A 663 8887 7743 5211 1415 -730 140 C ATOM 4765 CD1 LEU A 663 43.038 222.481 831.209 1.00 36.04 C ANISOU 4765 CD1 LEU A 663 6236 5214 2243 1566 -653 -30 C ATOM 4766 CD2 LEU A 663 41.534 221.223 832.592 1.00 34.90 C ANISOU 4766 CD2 LEU A 663 6045 4741 2474 1497 -914 188 C ATOM 4767 C LEU A 663 38.387 221.784 830.058 1.00 56.07 C ANISOU 4767 C LEU A 663 8220 7656 5428 1098 -456 393 C ATOM 4768 O LEU A 663 37.662 222.035 830.962 1.00 59.96 O ANISOU 4768 O LEU A 663 8668 8140 5975 1135 -499 417 O ATOM 4769 N LEU A 664 38.113 222.190 828.845 1.00 44.03 N ANISOU 4769 N LEU A 664 6576 6233 3922 1028 -337 424 N ATOM 4770 CA LEU A 664 36.917 222.955 828.673 1.00 41.51 C ANISOU 4770 CA LEU A 664 6077 6003 3692 1003 -252 477 C ATOM 4771 CB LEU A 664 36.824 223.472 827.267 1.00 43.50 C ANISOU 4771 CB LEU A 664 6229 6356 3944 940 -158 528 C ATOM 4772 CG LEU A 664 35.940 224.694 827.256 1.00 41.58 C ANISOU 4772 CG LEU A 664 5830 6232 3738 965 -73 590 C ATOM 4773 CD1 LEU A 664 36.752 225.902 827.485 1.00 37.94 C ANISOU 4773 CD1 LEU A 664 5384 5915 3116 1087 6 610 C ATOM 4774 CD2 LEU A 664 35.218 224.805 825.981 1.00 54.63 C ANISOU 4774 CD2 LEU A 664 7374 7915 5468 853 -33 657 C ATOM 4775 C LEU A 664 35.674 222.190 828.966 1.00 48.90 C ANISOU 4775 C LEU A 664 6970 6860 4750 887 -298 497 C ATOM 4776 O LEU A 664 34.803 222.662 829.638 1.00 52.92 O ANISOU 4776 O LEU A 664 7412 7400 5296 907 -310 514 O ATOM 4777 N LEU A 665 35.596 220.983 828.465 1.00 50.37 N ANISOU 4777 N LEU A 665 7204 6961 4972 758 -334 499 N ATOM 4778 CA LEU A 665 34.414 220.158 828.656 1.00 46.14 C ANISOU 4778 CA LEU A 665 6646 6385 4500 632 -367 524 C ATOM 4779 CB LEU A 665 34.523 218.865 827.858 1.00 33.97 C ANISOU 4779 CB LEU A 665 5140 4793 2972 493 -383 537 C ATOM 4780 CG LEU A 665 34.800 218.987 826.364 1.00 44.86 C ANISOU 4780 CG LEU A 665 6430 6232 4384 464 -320 538 C ATOM 4781 CD2 LEU A 665 33.640 219.635 825.642 1.00 28.11 C ANISOU 4781 CD2 LEU A 665 4145 4198 2339 448 -245 556 C ATOM 4782 CD1 LEU A 665 35.093 217.616 825.795 1.00 28.95 C ANISOU 4782 CD1 LEU A 665 4469 4167 2364 337 -368 556 C ATOM 4783 C LEU A 665 34.187 219.842 830.121 1.00 55.94 C ANISOU 4783 C LEU A 665 8000 7554 5701 651 -488 544 C ATOM 4784 O LEU A 665 33.128 219.343 830.491 1.00 68.91 O ANISOU 4784 O LEU A 665 9646 9191 7346 557 -533 582 O ATOM 4785 N ASN A 666 35.191 220.118 830.947 1.00 30.86 N ANISOU 4785 N ASN A 666 4931 4327 2469 777 -566 527 N ATOM 4786 CA ASN A 666 35.085 219.918 832.394 1.00 41.54 C ANISOU 4786 CA ASN A 666 6396 5593 3795 822 -741 568 C ATOM 4787 CB ASN A 666 36.423 219.475 832.991 1.00 46.81 C ANISOU 4787 CB ASN A 666 7241 6131 4414 907 -877 558 C ATOM 4788 CG ASN A 666 36.491 217.980 833.221 1.00 55.97 C ANISOU 4788 CG ASN A 666 8561 7149 5558 748 -1002 637 C ATOM 4789 OD1 ASN A 666 35.881 217.454 834.155 1.00 55.15 O ANISOU 4789 OD1 ASN A 666 8535 6972 5447 685 -1156 742 O ATOM 4790 ND2 ASN A 666 37.237 217.284 832.368 1.00 62.53 N ANISOU 4790 ND2 ASN A 666 9445 7946 6367 671 -957 611 N ATOM 4791 C ASN A 666 34.603 221.166 833.100 1.00 48.04 C ANISOU 4791 C ASN A 666 7115 6499 4638 953 -766 567 C ATOM 4792 O ASN A 666 33.775 221.100 834.005 1.00 56.30 O ANISOU 4792 O ASN A 666 8175 7517 5700 933 -908 625 O ATOM 4793 N LEU A 667 35.140 222.307 832.684 1.00 50.07 N ANISOU 4793 N LEU A 667 7273 6872 4881 1082 -649 520 N ATOM 4794 CA LEU A 667 34.663 223.583 833.175 1.00 48.38 C ANISOU 4794 CA LEU A 667 6918 6773 4690 1193 -650 534 C ATOM 4795 CB LEU A 667 35.478 224.726 832.569 1.00 54.55 C ANISOU 4795 CB LEU A 667 7620 7711 5397 1317 -493 508 C ATOM 4796 CG LEU A 667 36.970 224.758 832.930 1.00 55.78 C ANISOU 4796 CG LEU A 667 7902 7853 5437 1483 -542 446 C ATOM 4797 CD1 LEU A 667 37.591 226.116 832.625 1.00 32.82 C ANISOU 4797 CD1 LEU A 667 4920 5172 2378 1615 -391 430 C ATOM 4798 CD2 LEU A 667 37.188 224.396 834.383 1.00 33.75 C ANISOU 4798 CD2 LEU A 667 5176 4910 2738 1617 -815 448 C ATOM 4799 C LEU A 667 33.185 223.698 832.821 1.00 51.44 C ANISOU 4799 C LEU A 667 7191 7214 5139 1057 -609 569 C ATOM 4800 O LEU A 667 32.376 224.142 833.623 1.00 56.89 O ANISOU 4800 O LEU A 667 7824 7922 5869 1079 -732 601 O ATOM 4801 N TYR A 668 32.835 223.264 831.619 1.00 55.69 N ANISOU 4801 N TYR A 668 7694 7767 5698 925 -477 561 N ATOM 4802 CA TYR A 668 31.441 223.226 831.208 1.00 59.19 C ANISOU 4802 CA TYR A 668 8050 8247 6191 804 -457 579 C ATOM 4803 CB TYR A 668 31.316 222.628 829.811 1.00 56.64 C ANISOU 4803 CB TYR A 668 7690 7921 5909 695 -345 566 C ATOM 4804 CG TYR A 668 29.898 222.578 829.307 1.00 51.12 C ANISOU 4804 CG TYR A 668 6912 7260 5252 592 -331 571 C ATOM 4805 CD2 TYR A 668 29.165 221.410 829.378 1.00 59.48 C ANISOU 4805 CD2 TYR A 668 8048 8279 6273 478 -386 568 C ATOM 4806 CE2 TYR A 668 27.871 221.353 828.920 1.00 71.68 C ANISOU 4806 CE2 TYR A 668 9542 9873 7819 400 -376 557 C ATOM 4807 CZ TYR A 668 27.290 222.474 828.386 1.00 64.55 C ANISOU 4807 CZ TYR A 668 8513 9034 6979 428 -329 554 C ATOM 4808 OH TYR A 668 25.996 222.394 827.937 1.00 66.79 O ANISOU 4808 OH TYR A 668 8771 9357 7250 356 -338 529 O ATOM 4809 CE1 TYR A 668 27.998 223.654 828.300 1.00 58.71 C ANISOU 4809 CE1 TYR A 668 7689 8329 6290 521 -276 584 C ATOM 4810 CD1 TYR A 668 29.294 223.699 828.758 1.00 56.52 C ANISOU 4810 CD1 TYR A 668 7460 8029 5986 606 -269 590 C ATOM 4811 C TYR A 668 30.572 222.444 832.191 1.00 74.81 C ANISOU 4811 C TYR A 668 10131 10160 8135 731 -627 606 C ATOM 4812 O TYR A 668 29.511 222.914 832.589 1.00 95.16 O ANISOU 4812 O TYR A 668 12656 12787 10714 712 -702 622 O ATOM 4813 N ARG A 669 48.922 210.202 832.445 1.00 68.27 N ANISOU 4813 N ARG A 669 9460 9226 7253 679 -713 630 N ATOM 4814 CA ARG A 669 48.851 208.923 833.098 1.00 56.97 C ANISOU 4814 CA ARG A 669 8153 7747 5745 592 -892 699 C ATOM 4815 CB ARG A 669 50.143 208.162 832.930 1.00 38.00 C ANISOU 4815 CB ARG A 669 5930 5232 3275 511 -966 757 C ATOM 4816 C ARG A 669 48.569 209.094 834.558 1.00 63.64 C ANISOU 4816 C ARG A 669 9003 8578 6598 704 -1100 739 C ATOM 4817 O ARG A 669 47.804 208.358 835.120 1.00 78.48 O ANISOU 4817 O ARG A 669 10904 10484 8430 651 -1247 784 O ATOM 4818 N GLN A 670 49.179 210.072 835.185 1.00 62.44 N ANISOU 4818 N GLN A 670 8825 8389 6509 870 -1144 722 N ATOM 4819 CA GLN A 670 48.967 210.297 836.596 1.00 70.22 C ANISOU 4819 CA GLN A 670 9764 9346 7571 1011 -1387 762 C ATOM 4820 CB GLN A 670 50.287 210.672 837.220 1.00 72.52 C ANISOU 4820 CB GLN A 670 10137 9498 7919 1159 -1530 780 C ATOM 4821 CG GLN A 670 51.449 210.319 836.342 1.00 85.53 C ANISOU 4821 CG GLN A 670 11962 11061 9475 1062 -1438 779 C ATOM 4822 CD GLN A 670 52.731 210.201 837.103 1.00 91.88 C ANISOU 4822 CD GLN A 670 12905 11668 10337 1165 -1685 841 C ATOM 4823 OE1 GLN A 670 52.904 210.827 838.134 1.00 96.74 O ANISOU 4823 OE1 GLN A 670 13435 12216 11107 1380 -1863 836 O ATOM 4824 NE2 GLN A 670 53.640 209.383 836.605 1.00 83.68 N ANISOU 4824 NE2 GLN A 670 12055 10519 9221 1022 -1720 910 N ATOM 4825 C GLN A 670 48.026 211.436 836.806 1.00 76.35 C ANISOU 4825 C GLN A 670 10313 10256 8441 1126 -1297 709 C ATOM 4826 O GLN A 670 48.214 212.480 836.253 1.00 93.32 O ANISOU 4826 O GLN A 670 12390 12482 10585 1191 -1092 660 O ATOM 4827 N ASP A 671 46.995 211.240 837.602 1.00 70.16 N ANISOU 4827 N ASP A 671 9413 9508 7738 1143 -1471 734 N ATOM 4828 CA ASP A 671 46.024 212.295 837.876 1.00 64.30 C ANISOU 4828 CA ASP A 671 8410 8888 7131 1241 -1418 705 C ATOM 4829 CB ASP A 671 46.447 213.212 839.010 1.00 60.92 C ANISOU 4829 CB ASP A 671 7788 8422 6936 1492 -1563 696 C ATOM 4830 CG ASP A 671 45.268 213.691 839.825 1.00 67.30 C ANISOU 4830 CG ASP A 671 8262 9293 8018 1580 -1682 681 C ATOM 4831 OD1 ASP A 671 45.320 213.667 841.058 1.00 63.29 O ANISOU 4831 OD1 ASP A 671 7575 8681 7791 1734 -1956 669 O ATOM 4832 OD2 ASP A 671 44.277 214.101 839.230 1.00 68.05 O ANISOU 4832 OD2 ASP A 671 8237 9519 8101 1496 -1511 678 O ATOM 4833 C ASP A 671 45.451 213.077 836.708 1.00 54.97 C ANISOU 4833 C ASP A 671 7149 7847 5890 1175 -1100 680 C ATOM 4834 O ASP A 671 45.626 214.254 836.635 1.00 48.97 O ANISOU 4834 O ASP A 671 6274 7167 5164 1291 -967 683 O ATOM 4835 N LYS A 672 44.753 212.422 835.807 1.00 54.43 N ANISOU 4835 N LYS A 672 7131 7805 5746 1003 -1000 670 N ATOM 4836 CA LYS A 672 44.186 213.113 834.673 1.00 45.45 C ANISOU 4836 CA LYS A 672 5908 6760 4600 943 -749 671 C ATOM 4837 CB LYS A 672 43.302 212.195 833.856 1.00 37.47 C ANISOU 4837 CB LYS A 672 4925 5745 3568 781 -724 647 C ATOM 4838 CG LYS A 672 43.923 210.946 833.363 1.00 61.20 C ANISOU 4838 CG LYS A 672 8100 8665 6487 681 -742 618 C ATOM 4839 CD LYS A 672 42.896 210.110 832.676 1.00 62.98 C ANISOU 4839 CD LYS A 672 8325 8921 6685 556 -735 587 C ATOM 4840 CE LYS A 672 43.487 208.833 832.170 1.00 68.03 C ANISOU 4840 CE LYS A 672 9118 9512 7219 452 -745 577 C ATOM 4841 NZ LYS A 672 43.478 207.744 833.170 1.00 82.37 N ANISOU 4841 NZ LYS A 672 11079 11322 8897 410 -970 607 N ATOM 4842 C LYS A 672 43.292 214.212 835.150 1.00 59.94 C ANISOU 4842 C LYS A 672 7519 8706 6550 1029 -748 724 C ATOM 4843 O LYS A 672 43.193 215.228 834.518 1.00 61.59 O ANISOU 4843 O LYS A 672 7659 9002 6740 1045 -554 780 O ATOM 4844 N CYS A 673 42.609 214.026 836.256 1.00 64.01 N ANISOU 4844 N CYS A 673 7886 9213 7220 1084 -985 719 N ATOM 4845 CA CYS A 673 41.725 215.068 836.728 1.00 57.12 C ANISOU 4845 CA CYS A 673 6683 8423 6596 1178 -991 758 C ATOM 4846 CB CYS A 673 41.005 214.607 837.972 1.00 72.70 C ANISOU 4846 CB CYS A 673 8448 10346 8829 1220 -1299 698 C ATOM 4847 SG CYS A 673 40.128 215.882 838.787 1.00 62.16 S ANISOU 4847 SG CYS A 673 6650 9006 7962 1264 -1144 621 S ATOM 4848 C CYS A 673 42.438 216.349 837.035 1.00 56.81 C ANISOU 4848 C CYS A 673 6513 8412 6661 1319 -777 741 C ATOM 4849 O CYS A 673 41.970 217.390 836.678 1.00 67.05 O ANISOU 4849 O CYS A 673 7660 9774 8041 1277 -496 754 O ATOM 4850 N LEU A 674 43.572 216.284 837.698 1.00 53.52 N ANISOU 4850 N LEU A 674 6162 7930 6242 1465 -880 696 N ATOM 4851 CA LEU A 674 44.321 217.478 838.018 1.00 58.93 C ANISOU 4851 CA LEU A 674 6736 8631 7022 1595 -637 607 C ATOM 4852 CB LEU A 674 45.473 217.151 838.937 1.00 64.72 C ANISOU 4852 CB LEU A 674 7520 9227 7845 1772 -844 530 C ATOM 4853 CG LEU A 674 46.343 218.324 839.337 1.00 67.04 C ANISOU 4853 CG LEU A 674 7699 9517 8255 1928 -597 372 C ATOM 4854 CD2 LEU A 674 47.445 217.840 840.179 1.00 64.49 C ANISOU 4854 CD2 LEU A 674 7440 9002 8062 2099 -854 302 C ATOM 4855 CD1 LEU A 674 45.522 219.282 840.097 1.00 70.21 C ANISOU 4855 CD1 LEU A 674 7698 9970 9007 1974 -404 268 C ATOM 4856 C LEU A 674 44.862 218.116 836.772 1.00 58.52 C ANISOU 4856 C LEU A 674 6887 8686 6661 1531 -356 655 C ATOM 4857 O LEU A 674 44.888 219.310 836.641 1.00 61.25 O ANISOU 4857 O LEU A 674 7125 9127 7020 1544 -52 614 O ATOM 4858 N LEU A 675 45.300 217.297 835.843 1.00 49.07 N ANISOU 4858 N LEU A 675 5987 7483 5176 1450 -464 745 N ATOM 4859 CA LEU A 675 45.852 217.790 834.619 1.00 41.69 C ANISOU 4859 CA LEU A 675 5247 6635 3958 1387 -268 799 C ATOM 4860 CB LEU A 675 46.257 216.641 833.735 1.00 40.52 C ANISOU 4860 CB LEU A 675 5263 6345 3790 1229 -277 724 C ATOM 4861 CG LEU A 675 47.323 217.053 832.756 1.00 42.94 C ANISOU 4861 CG LEU A 675 5692 6632 3992 1220 -151 683 C ATOM 4862 CD1 LEU A 675 47.228 216.268 831.519 1.00 33.74 C ANISOU 4862 CD1 LEU A 675 4551 5368 2900 1059 -128 662 C ATOM 4863 CD2 LEU A 675 47.092 218.465 832.476 1.00 51.67 C ANISOU 4863 CD2 LEU A 675 6742 7908 4981 1261 29 755 C ATOM 4864 C LEU A 675 44.829 218.600 833.906 1.00 55.32 C ANISOU 4864 C LEU A 675 6859 8471 5688 1273 -30 885 C ATOM 4865 O LEU A 675 45.141 219.599 833.334 1.00 65.55 O ANISOU 4865 O LEU A 675 8199 9868 6840 1256 202 910 O ATOM 4866 N ALA A 676 43.591 218.175 833.915 1.00 66.24 N ANISOU 4866 N ALA A 676 8107 9829 7232 1181 -97 936 N ATOM 4867 CA ALA A 676 42.564 218.931 833.238 1.00 63.14 C ANISOU 4867 CA ALA A 676 7596 9495 6900 1061 113 1041 C ATOM 4868 CB ALA A 676 41.294 218.167 833.209 1.00 61.83 C ANISOU 4868 CB ALA A 676 7319 9254 6920 961 -31 1058 C ATOM 4869 C ALA A 676 42.345 220.281 833.873 1.00 55.80 C ANISOU 4869 C ALA A 676 6431 8640 6130 1093 383 1014 C ATOM 4870 O ALA A 676 42.142 221.249 833.197 1.00 55.76 O ANISOU 4870 O ALA A 676 6431 8727 6028 1012 631 1125 O ATOM 4871 N GLU A 677 42.371 220.347 835.183 1.00 46.86 N ANISOU 4871 N GLU A 677 5080 7470 5254 1205 335 873 N ATOM 4872 CA GLU A 677 42.164 221.600 835.851 1.00 55.80 C ANISOU 4872 CA GLU A 677 5943 8680 6579 1236 626 815 C ATOM 4873 CB GLU A 677 42.211 221.385 837.344 1.00 61.84 C ANISOU 4873 CB GLU A 677 6442 9357 7699 1384 481 638 C ATOM 4874 CG GLU A 677 41.026 220.685 837.906 1.00 76.82 C ANISOU 4874 CG GLU A 677 8120 11155 9914 1327 241 644 C ATOM 4875 CD GLU A 677 41.095 220.601 839.386 1.00 93.04 C ANISOU 4875 CD GLU A 677 9882 13125 12345 1481 80 483 C ATOM 4876 OE2 GLU A 677 40.293 219.874 839.987 1.00 93.24 O ANISOU 4876 OE2 GLU A 677 9754 13060 12614 1457 -211 465 O ATOM 4877 OE1 GLU A 677 41.972 221.267 839.947 1.00100.63 O ANISOU 4877 OE1 GLU A 677 10765 14104 13366 1631 232 359 O ATOM 4878 C GLU A 677 43.227 222.593 835.536 1.00 63.76 C ANISOU 4878 C GLU A 677 7090 9817 7319 1289 896 775 C ATOM 4879 O GLU A 677 42.955 223.741 835.292 1.00 66.33 O ANISOU 4879 O GLU A 677 7334 10276 7592 1214 1226 831 O ATOM 4880 N VAL A 678 44.464 222.159 835.544 1.00 61.48 N ANISOU 4880 N VAL A 678 7023 9491 6846 1406 757 675 N ATOM 4881 CA VAL A 678 45.523 223.081 835.259 1.00 60.80 C ANISOU 4881 CA VAL A 678 7083 9523 6496 1458 989 589 C ATOM 4882 CB VAL A 678 46.839 222.401 835.403 1.00 63.74 C ANISOU 4882 CB VAL A 678 7670 9787 6760 1588 765 461 C ATOM 4883 CG2 VAL A 678 46.968 221.858 836.766 1.00 52.70 C ANISOU 4883 CG2 VAL A 678 6070 8224 5728 1749 567 313 C ATOM 4884 CG1 VAL A 678 47.927 223.345 835.127 1.00 71.09 C ANISOU 4884 CG1 VAL A 678 8751 10831 7428 1639 986 326 C ATOM 4885 C VAL A 678 45.407 223.613 833.866 1.00 65.14 C ANISOU 4885 C VAL A 678 7849 10210 6689 1298 1143 780 C ATOM 4886 O VAL A 678 45.533 224.784 833.636 1.00 74.61 O ANISOU 4886 O VAL A 678 9057 11577 7714 1256 1449 786 O ATOM 4887 N LEU A 679 45.152 222.740 832.926 1.00 55.88 N ANISOU 4887 N LEU A 679 6850 8971 5411 1206 925 940 N ATOM 4888 CA LEU A 679 45.017 223.122 831.545 1.00 35.95 C ANISOU 4888 CA LEU A 679 4501 6515 2645 1070 979 1130 C ATOM 4889 CB LEU A 679 44.874 221.880 830.704 1.00 43.22 C ANISOU 4889 CB LEU A 679 5468 7231 3722 1027 651 1156 C ATOM 4890 CG LEU A 679 46.138 221.116 830.454 1.00 39.95 C ANISOU 4890 CG LEU A 679 5192 6693 3296 1095 461 999 C ATOM 4891 CD1 LEU A 679 46.001 220.484 829.154 1.00 34.30 C ANISOU 4891 CD1 LEU A 679 4482 5848 2702 986 348 1016 C ATOM 4892 CD2 LEU A 679 47.196 222.100 830.379 1.00 40.95 C ANISOU 4892 CD2 LEU A 679 5451 6922 3187 1149 579 939 C ATOM 4893 C LEU A 679 43.841 224.022 831.254 1.00 64.18 C ANISOU 4893 C LEU A 679 7933 10180 6275 928 1223 1323 C ATOM 4894 O LEU A 679 43.905 224.900 830.422 1.00 63.50 O ANISOU 4894 O LEU A 679 7934 10158 6037 849 1316 1435 O ATOM 4895 N LEU A 680 42.747 223.769 831.938 1.00 67.80 N ANISOU 4895 N LEU A 680 8123 10558 7082 899 1221 1330 N ATOM 4896 CA LEU A 680 41.504 224.513 831.750 1.00 65.18 C ANISOU 4896 CA LEU A 680 7603 10247 6915 746 1423 1515 C ATOM 4897 CB LEU A 680 40.309 223.655 832.179 1.00 60.81 C ANISOU 4897 CB LEU A 680 6820 9516 6767 707 1234 1504 C ATOM 4898 CG LEU A 680 39.803 222.543 831.254 1.00 56.42 C ANISOU 4898 CG LEU A 680 6394 8816 6229 641 963 1589 C ATOM 4899 CD1 LEU A 680 38.805 223.088 830.259 1.00 72.50 C ANISOU 4899 CD1 LEU A 680 8407 10806 8334 471 1073 1841 C ATOM 4900 CD2 LEU A 680 40.940 221.856 830.540 1.00 48.13 C ANISOU 4900 CD2 LEU A 680 5654 7780 4852 712 794 1558 C ATOM 4901 C LEU A 680 41.489 225.844 832.513 1.00 77.56 C ANISOU 4901 C LEU A 680 8976 11972 8520 739 1800 1467 C ATOM 4902 O LEU A 680 40.684 226.725 832.213 1.00 87.32 O ANISOU 4902 O LEU A 680 10114 13273 9791 583 2043 1664 O ATOM 4903 N LYS A 681 42.370 225.986 833.500 1.00 72.78 N ANISOU 4903 N LYS A 681 8305 11417 7931 903 1860 1207 N ATOM 4904 CA LYS A 681 42.464 227.237 834.251 1.00 75.38 C ANISOU 4904 CA LYS A 681 8431 11910 8299 914 2257 1101 C ATOM 4905 CB LYS A 681 42.972 226.986 835.670 1.00 74.68 C ANISOU 4905 CB LYS A 681 8103 11752 8520 1124 2210 779 C ATOM 4906 CG LYS A 681 42.982 228.227 836.553 1.00 78.66 C ANISOU 4906 CG LYS A 681 8316 12410 9162 1150 2646 620 C ATOM 4907 CD LYS A 681 43.215 227.880 838.017 1.00 82.07 C ANISOU 4907 CD LYS A 681 8414 12710 10057 1363 2543 323 C ATOM 4908 CE LYS A 681 43.119 229.124 838.901 1.00 84.92 C ANISOU 4908 CE LYS A 681 8414 13221 10630 1386 3014 142 C ATOM 4909 NZ LYS A 681 41.801 229.811 838.766 1.00 78.84 N ANISOU 4909 NZ LYS A 681 7399 12540 10018 1154 3294 363 N ATOM 4910 C LYS A 681 43.362 228.244 833.538 1.00 85.68 C ANISOU 4910 C LYS A 681 10018 13441 9097 877 2513 1126 C ATOM 4911 O LYS A 681 43.191 229.457 833.691 1.00 83.01 O ANISOU 4911 O LYS A 681 9587 13295 8658 790 2913 1152 O ATOM 4912 N ASP A 682 44.317 227.751 832.771 1.00 87.88 N ANISOU 4912 N ASP A 682 10637 13706 9047 928 2289 1112 N ATOM 4913 CA ASP A 682 45.234 228.604 832.039 1.00 93.70 C ANISOU 4913 CA ASP A 682 11671 14639 9291 893 2439 1114 C ATOM 4914 CB ASP A 682 46.450 227.809 831.597 1.00 91.80 C ANISOU 4914 CB ASP A 682 11701 14275 8904 1009 2074 976 C ATOM 4915 CG ASP A 682 47.578 227.888 832.567 1.00 95.65 C ANISOU 4915 CG ASP A 682 12182 14811 9350 1198 2190 613 C ATOM 4916 OD1 ASP A 682 47.325 228.167 833.744 1.00102.47 O ANISOU 4916 OD1 ASP A 682 12742 15658 10533 1291 2367 435 O ATOM 4917 OD2 ASP A 682 48.726 227.671 832.165 1.00 87.62 O ANISOU 4917 OD2 ASP A 682 11412 13750 8129 1261 2001 488 O ATOM 4918 C ASP A 682 44.598 229.178 830.799 1.00 98.31 C ANISOU 4918 C ASP A 682 12396 15253 9703 692 2416 1452 C ATOM 4919 O ASP A 682 44.884 230.295 830.403 1.00106.73 O ANISOU 4919 O ASP A 682 13599 16517 10437 604 2638 1510 O ATOM 4920 N SER A 683 43.763 228.374 830.163 1.00 91.15 N ANISOU 4920 N SER A 683 11464 14151 9019 626 2138 1660 N ATOM 4921 CA SER A 683 43.084 228.757 828.941 1.00 88.39 C ANISOU 4921 CA SER A 683 11208 13774 8602 462 2068 1977 C ATOM 4922 CB SER A 683 43.033 227.549 828.038 1.00 80.43 C ANISOU 4922 CB SER A 683 10267 12528 7766 496 1637 2004 C ATOM 4923 OG SER A 683 42.937 226.382 828.824 1.00 84.69 O ANISOU 4923 OG SER A 683 10676 12929 8573 604 1493 1831 O ATOM 4924 C SER A 683 41.685 229.263 829.135 1.00 92.70 C ANISOU 4924 C SER A 683 11537 14326 9360 298 2313 2227 C ATOM 4925 O SER A 683 41.042 229.681 828.194 1.00 85.84 O ANISOU 4925 O SER A 683 10734 13427 8453 150 2290 2524 O ATOM 4926 N SER A 684 41.173 229.171 830.347 1.00101.96 N ANISOU 4926 N SER A 684 12410 15510 10820 316 2532 2111 N ATOM 4927 CA SER A 684 39.806 229.589 830.587 1.00108.09 C ANISOU 4927 CA SER A 684 12908 16249 11911 141 2752 2327 C ATOM 4928 CB SER A 684 39.116 228.518 831.435 1.00120.36 C ANISOU 4928 CB SER A 684 14161 17570 13999 224 2525 2149 C ATOM 4929 OG SER A 684 37.704 228.621 831.382 1.00131.20 O ANISOU 4929 OG SER A 684 15298 18799 15755 53 2562 2350 O ATOM 4930 C SER A 684 39.626 230.942 831.230 1.00100.70 C ANISOU 4930 C SER A 684 11798 15530 10936 39 3234 2347 C ATOM 4931 O SER A 684 40.216 231.238 832.249 1.00103.18 O ANISOU 4931 O SER A 684 11964 15962 11278 163 3430 2048 O ATOM 4932 N GLU A 685 38.783 231.751 830.625 1.00 95.61 N ANISOU 4932 N GLU A 685 11156 14921 10251 -193 3431 2707 N ATOM 4933 CA GLU A 685 38.529 233.058 831.149 1.00118.20 C ANISOU 4933 CA GLU A 685 13856 18003 13052 -337 3930 2774 C ATOM 4934 CB GLU A 685 37.540 233.751 830.236 1.00134.45 C ANISOU 4934 CB GLU A 685 15984 20032 15068 -617 4037 3263 C ATOM 4935 CG GLU A 685 36.505 234.564 830.939 1.00145.13 C ANISOU 4935 CG GLU A 685 16968 21411 16766 -816 4440 3392 C ATOM 4936 CD GLU A 685 35.329 234.871 830.043 1.00150.68 C ANISOU 4936 CD GLU A 685 17698 21944 17611 -1084 4411 3892 C ATOM 4937 OE2 GLU A 685 35.341 234.439 828.875 1.00149.95 O ANISOU 4937 OE2 GLU A 685 17905 21707 17363 -1085 4057 4116 O ATOM 4938 OE1 GLU A 685 34.388 235.535 830.509 1.00151.93 O ANISOU 4938 OE1 GLU A 685 17557 22083 18088 -1286 4722 4053 O ATOM 4939 C GLU A 685 37.958 232.907 832.539 1.00117.94 C ANISOU 4939 C GLU A 685 13339 17884 13590 -279 4059 2524 C ATOM 4940 O GLU A 685 38.340 233.620 833.450 1.00113.38 O ANISOU 4940 O GLU A 685 12573 17498 13010 -236 4421 2303 O ATOM 4941 N PHE A 686 37.053 231.956 832.706 1.00117.75 N ANISOU 4941 N PHE A 686 13104 17570 14068 -272 3750 2533 N ATOM 4942 CA PHE A 686 36.455 231.679 834.002 1.00114.34 C ANISOU 4942 CA PHE A 686 12206 17025 14213 -215 3771 2297 C ATOM 4943 CB PHE A 686 34.967 231.475 833.884 1.00108.63 C ANISOU 4943 CB PHE A 686 11236 16062 13975 -407 3678 2516 C ATOM 4944 CG PHE A 686 34.193 232.728 834.036 1.00111.08 C ANISOU 4944 CG PHE A 686 11315 16471 14420 -660 4140 2754 C ATOM 4945 CD2 PHE A 686 33.999 233.566 832.962 1.00106.89 C ANISOU 4945 CD2 PHE A 686 11046 16027 13539 -881 4340 3165 C ATOM 4946 CE2 PHE A 686 33.292 234.727 833.103 1.00107.17 C ANISOU 4946 CE2 PHE A 686 10886 16159 13675 -1143 4786 3422 C ATOM 4947 CZ PHE A 686 32.773 235.071 834.330 1.00114.19 C ANISOU 4947 CZ PHE A 686 11275 17061 15051 -1183 5058 3239 C ATOM 4948 CE1 PHE A 686 32.965 234.252 835.412 1.00116.31 C ANISOU 4948 CE1 PHE A 686 11253 17236 15703 -946 4840 2809 C ATOM 4949 CD1 PHE A 686 33.677 233.089 835.264 1.00117.51 C ANISOU 4949 CD1 PHE A 686 11640 17292 15716 -687 4375 2582 C ATOM 4950 C PHE A 686 37.089 230.462 834.591 1.00112.94 C ANISOU 4950 C PHE A 686 12023 16725 14162 50 3382 1956 C ATOM 4951 O PHE A 686 36.782 230.066 835.701 1.00 99.65 O ANISOU 4951 O PHE A 686 9993 14943 12929 144 3299 1728 O ATOM 4952 N SER A 687 37.975 229.877 833.804 1.00122.99 N ANISOU 4952 N SER A 687 13691 18002 15036 155 3131 1947 N ATOM 4953 CA SER A 687 38.727 228.689 834.163 1.00118.41 C ANISOU 4953 CA SER A 687 13199 17313 14477 383 2756 1680 C ATOM 4954 CB SER A 687 39.288 228.829 835.564 1.00112.49 C ANISOU 4954 CB SER A 687 12182 16614 13946 566 2861 1341 C ATOM 4955 OG SER A 687 38.293 228.538 836.509 1.00105.19 O ANISOU 4955 OG SER A 687 10840 15546 13580 552 2786 1270 O ATOM 4956 C SER A 687 37.928 227.404 834.043 1.00111.73 C ANISOU 4956 C SER A 687 12300 16210 13943 379 2340 1699 C ATOM 4957 O SER A 687 38.412 226.339 834.382 1.00107.45 O ANISOU 4957 O SER A 687 11822 15573 13433 537 2020 1508 O ATOM 4958 N PHE A 688 36.722 227.461 833.521 1.00105.45 N ANISOU 4958 N PHE A 688 11397 15296 13374 190 2344 1923 N ATOM 4959 CA PHE A 688 35.991 226.227 833.404 1.00 95.41 C ANISOU 4959 CA PHE A 688 10079 13789 12383 184 1968 1888 C ATOM 4960 CB PHE A 688 34.576 226.413 833.888 1.00 91.58 C ANISOU 4960 CB PHE A 688 9228 13167 12401 20 2034 1957 C ATOM 4961 CG PHE A 688 34.480 226.642 835.345 1.00 87.31 C ANISOU 4961 CG PHE A 688 8295 12657 12223 84 2118 1736 C ATOM 4962 CD2 PHE A 688 35.360 226.048 836.197 1.00 75.26 C ANISOU 4962 CD2 PHE A 688 6754 11171 10670 306 1946 1460 C ATOM 4963 CE2 PHE A 688 35.270 226.250 837.527 1.00 75.82 C ANISOU 4963 CE2 PHE A 688 6439 11245 11125 382 1987 1259 C ATOM 4964 CZ PHE A 688 34.304 227.056 838.023 1.00 87.42 C ANISOU 4964 CZ PHE A 688 7514 12696 13007 225 2228 1318 C ATOM 4965 CE1 PHE A 688 33.424 227.654 837.192 1.00 94.82 C ANISOU 4965 CE1 PHE A 688 8470 13597 13962 -17 2424 1601 C ATOM 4966 CD1 PHE A 688 33.516 227.457 835.861 1.00 98.07 C ANISOU 4966 CD1 PHE A 688 9284 13989 13989 -82 2360 1816 C ATOM 4967 C PHE A 688 36.010 225.663 832.004 1.00 93.77 C ANISOU 4967 C PHE A 688 10201 13491 11935 141 1762 2055 C ATOM 4968 O PHE A 688 35.478 224.595 831.748 1.00 87.16 O ANISOU 4968 O PHE A 688 9369 12474 11273 140 1468 1999 O ATOM 4969 N GLY A 689 36.633 226.380 831.090 1.00 99.90 N ANISOU 4969 N GLY A 689 11248 14403 12306 107 1915 2242 N ATOM 4970 CA GLY A 689 36.771 225.876 829.746 1.00 96.52 C ANISOU 4970 CA GLY A 689 11110 13895 11668 75 1721 2412 C ATOM 4971 C GLY A 689 35.807 226.498 828.774 1.00100.21 C ANISOU 4971 C GLY A 689 11568 14239 12268 -122 1782 2750 C ATOM 4972 O GLY A 689 35.465 227.568 829.040 1.00109.03 O ANISOU 4972 O GLY A 689 12442 15300 13686 -265 1964 2871 O ATOM 4973 N VAL A 690 35.894 226.067 827.533 1.00 94.45 N ANISOU 4973 N VAL A 690 11097 13452 11339 -131 1617 2913 N ATOM 4974 CA VAL A 690 35.093 226.635 826.489 1.00 92.76 C ANISOU 4974 CA VAL A 690 10921 13090 11235 -293 1613 3265 C ATOM 4975 CB VAL A 690 35.864 226.640 825.200 1.00 91.40 C ANISOU 4975 CB VAL A 690 11029 12948 10749 -219 1407 3345 C ATOM 4976 CG1 VAL A 690 34.967 226.942 824.064 1.00 99.64 C ANISOU 4976 CG1 VAL A 690 12086 13788 11984 -354 1322 3688 C ATOM 4977 CG2 VAL A 690 36.970 227.634 825.282 1.00 84.99 C ANISOU 4977 CG2 VAL A 690 10380 12420 9492 -185 1563 3341 C ATOM 4978 C VAL A 690 33.840 225.826 826.313 1.00 90.48 C ANISOU 4978 C VAL A 690 10443 12484 11451 -343 1413 3231 C ATOM 4979 O VAL A 690 33.652 224.828 826.970 1.00 95.68 O ANISOU 4979 O VAL A 690 10987 13067 12301 -251 1252 2925 O ATOM 4980 N LYS A 691 32.971 226.276 825.434 1.00 85.84 N ANISOU 4980 N LYS A 691 9828 11706 11080 -498 1422 3548 N ATOM 4981 CA LYS A 691 31.783 225.538 825.093 1.00 81.81 C ANISOU 4981 CA LYS A 691 9153 10858 11072 -549 1228 3510 C ATOM 4982 CB LYS A 691 30.559 226.426 825.240 1.00 60.15 C ANISOU 4982 CB LYS A 691 6187 7949 8719 -764 1400 3774 C ATOM 4983 C LYS A 691 31.959 225.130 823.648 1.00 89.71 C ANISOU 4983 C LYS A 691 10359 11714 12013 -509 1005 3654 C ATOM 4984 O LYS A 691 32.266 225.960 822.825 1.00 94.46 O ANISOU 4984 O LYS A 691 11134 12366 12391 -570 1049 3998 O ATOM 4985 N PHE A 692 31.790 223.851 823.340 1.00 77.35 N ANISOU 4985 N PHE A 692 8773 9983 10636 -407 764 3385 N ATOM 4986 CA PHE A 692 31.942 223.362 821.975 1.00 70.87 C ANISOU 4986 CA PHE A 692 8089 9006 9831 -352 555 3469 C ATOM 4987 CB PHE A 692 32.512 221.947 821.964 1.00 68.14 C ANISOU 4987 CB PHE A 692 7798 8695 9397 -194 383 3081 C ATOM 4988 CG PHE A 692 33.704 221.761 822.848 1.00 70.93 C ANISOU 4988 CG PHE A 692 8270 9363 9317 -93 446 2885 C ATOM 4989 CD2 PHE A 692 33.750 220.716 823.754 1.00 60.55 C ANISOU 4989 CD2 PHE A 692 6889 8092 8026 -20 382 2521 C ATOM 4990 CE2 PHE A 692 34.847 220.534 824.567 1.00 61.64 C ANISOU 4990 CE2 PHE A 692 7133 8473 7813 76 410 2366 C ATOM 4991 CZ PHE A 692 35.920 221.397 824.474 1.00 72.81 C ANISOU 4991 CZ PHE A 692 8691 10095 8879 115 509 2488 C ATOM 4992 CE1 PHE A 692 35.893 222.438 823.570 1.00 76.72 C ANISOU 4992 CE1 PHE A 692 9223 10590 9337 54 560 2750 C ATOM 4993 CD1 PHE A 692 34.789 222.614 822.758 1.00 80.67 C ANISOU 4993 CD1 PHE A 692 9663 10847 10143 -60 532 3011 C ATOM 4994 C PHE A 692 30.604 223.335 821.253 1.00 75.60 C ANISOU 4994 C PHE A 692 8530 9217 10979 -453 457 3613 C ATOM 4995 O PHE A 692 29.693 222.616 821.658 1.00 84.89 O ANISOU 4995 O PHE A 692 9508 10196 12551 -467 396 3352 O ATOM 4996 N PHE A 693 30.481 224.107 820.183 1.00 71.57 N ANISOU 4996 N PHE A 693 8111 8581 10501 -524 417 4024 N ATOM 4997 CA PHE A 693 29.285 224.039 819.356 1.00 71.39 C ANISOU 4997 CA PHE A 693 7948 8134 11044 -598 280 4177 C ATOM 4998 CB PHE A 693 28.490 225.337 819.423 1.00 74.39 C ANISOU 4998 CB PHE A 693 8261 8397 11605 -813 430 4623 C ATOM 4999 CG PHE A 693 27.910 225.615 820.772 1.00 80.44 C ANISOU 4999 CG PHE A 693 8823 9233 12509 -926 654 4488 C ATOM 5000 CD2 PHE A 693 27.558 226.905 821.139 1.00 87.87 C ANISOU 5000 CD2 PHE A 693 9723 10232 13432 -1129 899 4864 C ATOM 5001 CE2 PHE A 693 27.013 227.164 822.381 1.00 92.23 C ANISOU 5001 CE2 PHE A 693 10035 10839 14170 -1236 1110 4728 C ATOM 5002 CZ PHE A 693 26.808 226.127 823.269 1.00 98.37 C ANISOU 5002 CZ PHE A 693 10630 11607 15139 -1136 1028 4225 C ATOM 5003 CE1 PHE A 693 27.150 224.832 822.913 1.00 97.32 C ANISOU 5003 CE1 PHE A 693 10578 11429 14970 -943 776 3865 C ATOM 5004 CD1 PHE A 693 27.689 224.583 821.668 1.00 85.71 C ANISOU 5004 CD1 PHE A 693 9326 9906 13332 -844 614 3993 C ATOM 5005 C PHE A 693 29.641 223.715 817.913 1.00 81.30 C ANISOU 5005 C PHE A 693 9322 9238 12329 -499 41 4303 C ATOM 5006 O PHE A 693 28.776 223.368 817.119 1.00 86.89 O ANISOU 5006 O PHE A 693 9903 9564 13548 -501 -121 4332 O ATOM 5007 N ASN A 694 30.922 223.829 817.582 1.00 81.44 N ANISOU 5007 N ASN A 694 9568 9543 11835 -410 9 4359 N ATOM 5008 CA ASN A 694 31.395 223.519 816.242 1.00 77.90 C ANISOU 5008 CA ASN A 694 9203 8994 11400 -309 -237 4449 C ATOM 5009 CB ASN A 694 31.791 224.798 815.511 1.00 80.16 C ANISOU 5009 CB ASN A 694 9622 9413 11423 -392 -291 4884 C ATOM 5010 CG ASN A 694 30.662 225.791 815.434 1.00101.98 C ANISOU 5010 CG ASN A 694 12343 11918 14486 -578 -232 5349 C ATOM 5011 OD1 ASN A 694 29.576 225.473 814.949 1.00114.63 O ANISOU 5011 OD1 ASN A 694 13809 13057 16688 -606 -351 5460 O ATOM 5012 ND2 ASN A 694 30.907 227.008 815.910 1.00109.73 N ANISOU 5012 ND2 ASN A 694 13439 13179 15074 -715 -33 5615 N ATOM 5013 C ASN A 694 32.590 222.595 816.308 1.00 75.84 C ANISOU 5013 C ASN A 694 9005 9013 10796 -155 -282 4043 C ATOM 5014 O ASN A 694 33.406 222.702 817.215 1.00 77.13 O ANISOU 5014 O ASN A 694 9244 9526 10538 -137 -138 3851 O ATOM 5015 N TYR A 695 32.696 221.682 815.352 1.00 75.79 N ANISOU 5015 N TYR A 695 8953 8829 11013 -46 -475 3907 N ATOM 5016 CA TYR A 695 33.902 220.884 815.252 1.00 67.72 C ANISOU 5016 CA TYR A 695 7991 8065 9673 58 -509 3578 C ATOM 5017 CB TYR A 695 33.832 219.918 814.069 1.00 69.81 C ANISOU 5017 CB TYR A 695 8164 8072 10291 166 -707 3479 C ATOM 5018 CG TYR A 695 33.189 218.590 814.401 1.00 66.96 C ANISOU 5018 CG TYR A 695 7661 7534 10246 240 -661 3080 C ATOM 5019 CD2 TYR A 695 32.124 218.098 813.657 1.00 69.50 C ANISOU 5019 CD2 TYR A 695 7763 7474 11168 268 -750 2981 C ATOM 5020 CE2 TYR A 695 31.543 216.881 813.965 1.00 76.92 C ANISOU 5020 CE2 TYR A 695 8553 8325 12348 302 -675 2508 C ATOM 5021 CZ TYR A 695 32.031 216.139 815.027 1.00 77.50 C ANISOU 5021 CZ TYR A 695 8712 8696 12039 301 -536 2178 C ATOM 5022 OH TYR A 695 31.470 214.929 815.356 1.00 84.93 O ANISOU 5022 OH TYR A 695 9542 9586 13141 315 -470 1719 O ATOM 5023 CE1 TYR A 695 33.086 216.606 815.774 1.00 64.50 C ANISOU 5023 CE1 TYR A 695 7270 7396 9842 282 -472 2304 C ATOM 5024 CD1 TYR A 695 33.658 217.822 815.460 1.00 64.84 C ANISOU 5024 CD1 TYR A 695 7445 7521 9669 257 -522 2726 C ATOM 5025 C TYR A 695 35.073 221.845 815.118 1.00 78.34 C ANISOU 5025 C TYR A 695 9488 9754 10524 18 -500 3703 C ATOM 5026 O TYR A 695 36.056 221.745 815.850 1.00 81.75 O ANISOU 5026 O TYR A 695 9999 10490 10571 45 -389 3449 O ATOM 5027 N GLY A 696 34.948 222.799 814.201 1.00 82.08 N ANISOU 5027 N GLY A 696 10010 10145 11032 -46 -633 4099 N ATOM 5028 CA GLY A 696 35.985 223.792 813.992 1.00 85.34 C ANISOU 5028 CA GLY A 696 10601 10854 10972 -96 -652 4247 C ATOM 5029 C GLY A 696 36.299 224.553 815.264 1.00 88.75 C ANISOU 5029 C GLY A 696 11123 11584 11015 -146 -388 4189 C ATOM 5030 O GLY A 696 37.411 225.049 815.443 1.00 89.87 O ANISOU 5030 O GLY A 696 11411 12010 10725 -143 -347 4106 O ATOM 5031 N GLN A 697 35.310 224.635 816.151 1.00 83.36 N ANISOU 5031 N GLN A 697 10343 10802 10526 -191 -213 4226 N ATOM 5032 CA GLN A 697 35.445 225.357 817.409 1.00 84.83 C ANISOU 5032 CA GLN A 697 10570 11230 10432 -238 54 4194 C ATOM 5033 CB GLN A 697 34.071 225.843 817.880 1.00 86.90 C ANISOU 5033 CB GLN A 697 10720 11285 11015 -369 202 4469 C ATOM 5034 CG GLN A 697 34.109 226.989 818.877 1.00 98.65 C ANISOU 5034 CG GLN A 697 12251 13011 12221 -477 500 4604 C ATOM 5035 CD GLN A 697 32.725 227.522 819.207 1.00107.70 C ANISOU 5035 CD GLN A 697 13259 13920 13743 -660 660 4920 C ATOM 5036 NE2 GLN A 697 32.675 228.678 819.865 1.00109.24 N ANISOU 5036 NE2 GLN A 697 13480 14312 13713 -800 949 5126 N ATOM 5037 OE1 GLN A 697 31.712 226.904 818.877 1.00108.72 O ANISOU 5037 OE1 GLN A 697 13248 13676 14386 -689 542 4965 O ATOM 5038 C GLN A 697 36.110 224.486 818.483 1.00 81.96 C ANISOU 5038 C GLN A 697 10171 11030 9942 -120 147 3720 C ATOM 5039 O GLN A 697 36.779 224.991 819.387 1.00 79.78 O ANISOU 5039 O GLN A 697 9958 11002 9353 -102 311 3603 O ATOM 5040 N LEU A 698 35.916 223.177 818.375 1.00 71.17 N ANISOU 5040 N LEU A 698 8709 9507 8825 -41 39 3462 N ATOM 5041 CA LEU A 698 36.520 222.222 819.290 1.00 57.97 C ANISOU 5041 CA LEU A 698 7021 7961 7042 55 86 3050 C ATOM 5042 CB LEU A 698 35.770 220.891 819.226 1.00 60.36 C ANISOU 5042 CB LEU A 698 7224 8035 7674 87 3 2880 C ATOM 5043 CG LEU A 698 36.467 219.625 819.730 1.00 51.58 C ANISOU 5043 CG LEU A 698 6132 7027 6440 172 -16 2482 C ATOM 5044 CD2 LEU A 698 35.559 218.427 819.552 1.00 61.56 C ANISOU 5044 CD2 LEU A 698 7331 8050 8007 191 -95 2376 C ATOM 5045 CD1 LEU A 698 36.865 219.764 821.176 1.00 39.97 C ANISOU 5045 CD1 LEU A 698 4676 5748 4763 199 105 2322 C ATOM 5046 C LEU A 698 37.971 222.017 818.907 1.00 57.33 C ANISOU 5046 C LEU A 698 7048 8062 6674 121 15 2845 C ATOM 5047 O LEU A 698 38.859 222.049 819.751 1.00 56.62 O ANISOU 5047 O LEU A 698 7010 8153 6351 176 98 2628 O ATOM 5048 N ILE A 699 38.198 221.803 817.616 1.00 70.33 N ANISOU 5048 N ILE A 699 8718 9615 8390 114 -151 2930 N ATOM 5049 CA ILE A 699 39.545 221.684 817.061 1.00 70.11 C ANISOU 5049 CA ILE A 699 8790 9713 8136 143 -237 2793 C ATOM 5050 CB ILE A 699 39.496 221.476 815.535 1.00 59.06 C ANISOU 5050 CB ILE A 699 7380 8155 6906 124 -453 2970 C ATOM 5051 CG2 ILE A 699 40.834 221.794 814.902 1.00 50.48 C ANISOU 5051 CG2 ILE A 699 6424 7205 5552 117 -562 2948 C ATOM 5052 CG1 ILE A 699 39.088 220.038 815.215 1.00 55.72 C ANISOU 5052 CG1 ILE A 699 6832 7546 6792 176 -504 2776 C ATOM 5053 CD1 ILE A 699 38.802 219.803 813.755 1.00 71.13 C ANISOU 5053 CD1 ILE A 699 8719 9274 9033 187 -721 2967 C ATOM 5054 C ILE A 699 40.373 222.921 817.390 1.00 69.53 C ANISOU 5054 C ILE A 699 8865 9859 7694 122 -168 2879 C ATOM 5055 O ILE A 699 41.547 222.819 817.746 1.00 70.95 O ANISOU 5055 O ILE A 699 9126 10170 7660 169 -146 2647 O ATOM 5056 N ALA A 700 39.749 224.088 817.272 1.00 66.63 N ANISOU 5056 N ALA A 700 8546 9514 7259 41 -125 3228 N ATOM 5057 CA ALA A 700 40.384 225.342 817.642 1.00 57.21 C ANISOU 5057 CA ALA A 700 7517 8551 5670 2 -14 3338 C ATOM 5058 CB ALA A 700 39.420 226.487 817.453 1.00 49.93 C ANISOU 5058 CB ALA A 700 6631 7618 4723 -124 59 3779 C ATOM 5059 C ALA A 700 40.855 225.291 819.089 1.00 63.54 C ANISOU 5059 C ALA A 700 8305 9496 6341 79 189 3046 C ATOM 5060 O ALA A 700 41.963 225.715 819.411 1.00 72.83 O ANISOU 5060 O ALA A 700 9614 10842 7216 115 235 2910 O ATOM 5061 N TYR A 701 40.010 224.764 819.964 1.00 57.22 N ANISOU 5061 N TYR A 701 7350 8607 5784 105 290 2961 N ATOM 5062 CA TYR A 701 40.312 224.789 821.385 1.00 51.98 C ANISOU 5062 CA TYR A 701 6660 8060 5032 175 461 2748 C ATOM 5063 CB TYR A 701 39.046 224.559 822.212 1.00 51.92 C ANISOU 5063 CB TYR A 701 6488 7950 5290 144 572 2808 C ATOM 5064 CG TYR A 701 39.297 224.640 823.693 1.00 52.49 C ANISOU 5064 CG TYR A 701 6516 8140 5289 207 740 2633 C ATOM 5065 CD2 TYR A 701 39.233 223.508 824.488 1.00 55.38 C ANISOU 5065 CD2 TYR A 701 6789 8434 5817 287 672 2382 C ATOM 5066 CE2 TYR A 701 39.476 223.573 825.841 1.00 52.39 C ANISOU 5066 CE2 TYR A 701 6367 8154 5386 347 797 2251 C ATOM 5067 CZ TYR A 701 39.793 224.779 826.418 1.00 62.89 C ANISOU 5067 CZ TYR A 701 7722 9661 6513 330 1039 2334 C ATOM 5068 OH TYR A 701 40.036 224.846 827.773 1.00 81.57 O ANISOU 5068 OH TYR A 701 10007 12126 8858 392 1195 2190 O ATOM 5069 CE1 TYR A 701 39.868 225.918 825.649 1.00 54.33 C ANISOU 5069 CE1 TYR A 701 6740 8670 5232 240 1145 2558 C ATOM 5070 CD1 TYR A 701 39.623 225.845 824.296 1.00 53.96 C ANISOU 5070 CD1 TYR A 701 6760 8519 5222 177 974 2724 C ATOM 5071 C TYR A 701 41.398 223.785 821.752 1.00 47.72 C ANISOU 5071 C TYR A 701 6131 7523 4478 292 374 2373 C ATOM 5072 O TYR A 701 42.271 224.071 822.565 1.00 54.50 O ANISOU 5072 O TYR A 701 7056 8503 5149 361 456 2219 O ATOM 5073 N ILE A 702 41.339 222.608 821.150 1.00 59.22 N ANISOU 5073 N ILE A 702 7527 8835 6140 306 225 2242 N ATOM 5074 CA ILE A 702 42.380 221.608 821.355 1.00 62.40 C ANISOU 5074 CA ILE A 702 7949 9218 6541 378 158 1933 C ATOM 5075 CB ILE A 702 42.062 220.296 820.604 1.00 51.89 C ANISOU 5075 CB ILE A 702 6547 7737 5433 356 47 1836 C ATOM 5076 CG2 ILE A 702 43.195 219.311 820.752 1.00 42.30 C ANISOU 5076 CG2 ILE A 702 5371 6502 4198 397 7 1567 C ATOM 5077 CG1 ILE A 702 40.784 219.672 821.156 1.00 48.84 C ANISOU 5077 CG1 ILE A 702 6042 7262 5253 346 78 1831 C ATOM 5078 CD1 ILE A 702 40.792 219.536 822.664 1.00 50.87 C ANISOU 5078 CD1 ILE A 702 6273 7579 5477 401 157 1691 C ATOM 5079 C ILE A 702 43.724 222.163 820.887 1.00 54.96 C ANISOU 5079 C ILE A 702 7163 8367 5354 388 116 1904 C ATOM 5080 O ILE A 702 44.766 221.895 821.481 1.00 52.18 O ANISOU 5080 O ILE A 702 6868 8037 4920 455 124 1697 O ATOM 5081 N ASP A 703 43.691 222.950 819.822 1.00 60.73 N ANISOU 5081 N ASP A 703 7975 9136 5964 314 53 2138 N ATOM 5082 CA ASP A 703 44.909 223.510 819.262 1.00 66.38 C ANISOU 5082 CA ASP A 703 8865 9945 6411 302 -21 2136 C ATOM 5083 CB ASP A 703 44.628 224.133 817.892 1.00 77.79 C ANISOU 5083 CB ASP A 703 10383 11394 7779 202 -162 2442 C ATOM 5084 CG ASP A 703 45.890 224.377 817.093 1.00 98.34 C ANISOU 5084 CG ASP A 703 13157 14058 10148 179 -317 2421 C ATOM 5085 OD1 ASP A 703 45.839 224.264 815.852 1.00109.06 O ANISOU 5085 OD1 ASP A 703 14528 15345 11563 121 -516 2587 O ATOM 5086 OD2 ASP A 703 46.937 224.676 817.705 1.00109.85 O ANISOU 5086 OD2 ASP A 703 14738 15622 11378 223 -258 2245 O ATOM 5087 C ASP A 703 45.533 224.535 820.205 1.00 57.90 C ANISOU 5087 C ASP A 703 7920 9051 5029 339 127 2101 C ATOM 5088 O ASP A 703 46.751 224.597 820.343 1.00 64.38 O ANISOU 5088 O ASP A 703 8866 9923 5674 382 99 1938 O ATOM 5089 N SER A 704 59.923 226.128 821.971 1.00 47.47 N ANISOU 5089 N SER A 704 6572 7822 3642 316 298 2260 N ATOM 5090 CA SER A 704 60.424 227.137 822.894 1.00 58.07 C ANISOU 5090 CA SER A 704 8028 9361 4675 342 495 2229 C ATOM 5091 CB SER A 704 59.313 228.106 823.298 1.00 66.64 C ANISOU 5091 CB SER A 704 9073 10552 5695 258 716 2492 C ATOM 5092 OG SER A 704 58.233 227.417 823.895 1.00 71.00 O ANISOU 5092 OG SER A 704 9411 10963 6601 278 752 2487 O ATOM 5093 C SER A 704 61.050 226.489 824.126 1.00 60.96 C ANISOU 5093 C SER A 704 8338 9694 5131 477 546 1920 C ATOM 5094 O SER A 704 62.125 226.891 824.564 1.00 69.17 O ANISOU 5094 O SER A 704 9512 10837 5933 533 598 1772 O ATOM 5095 N LEU A 705 65.583 220.673 824.708 1.00 56.05 N ANISOU 5095 N LEU A 705 7536 8930 4832 524 521 1834 N ATOM 5096 CA LEU A 705 66.196 219.853 825.745 1.00 53.81 C ANISOU 5096 CA LEU A 705 7212 8581 4653 641 501 1577 C ATOM 5097 CB LEU A 705 65.279 218.690 826.128 1.00 48.92 C ANISOU 5097 CB LEU A 705 6415 7815 4355 651 439 1527 C ATOM 5098 CG LEU A 705 64.427 218.840 827.389 1.00 45.79 C ANISOU 5098 CG LEU A 705 5903 7466 4028 682 568 1559 C ATOM 5099 CD1 LEU A 705 63.611 220.113 827.338 1.00 48.02 C ANISOU 5099 CD1 LEU A 705 6169 7877 4200 595 768 1806 C ATOM 5100 CD2 LEU A 705 63.527 217.629 827.572 1.00 43.49 C ANISOU 5100 CD2 LEU A 705 5477 7037 4009 664 464 1512 C ATOM 5101 C LEU A 705 67.534 219.319 825.243 1.00 55.25 C ANISOU 5101 C LEU A 705 7511 8692 4789 673 355 1408 C ATOM 5102 O LEU A 705 68.535 219.353 825.955 1.00 45.39 O ANISOU 5102 O LEU A 705 6350 7465 3431 759 373 1250 O ATOM 5103 N ASN A 706 53.479 227.372 822.981 1.00 61.58 N ANISOU 5103 N ASN A 706 8314 9404 5680 597 216 1453 N ATOM 5104 CA ASN A 706 54.691 226.716 822.500 1.00 56.17 C ANISOU 5104 CA ASN A 706 7734 8651 4956 592 85 1331 C ATOM 5105 CB ASN A 706 54.403 225.978 821.193 1.00 53.73 C ANISOU 5105 CB ASN A 706 7387 8263 4766 494 -46 1429 C ATOM 5106 CG ASN A 706 55.530 225.054 820.779 1.00 58.02 C ANISOU 5106 CG ASN A 706 7998 8714 5333 475 -175 1302 C ATOM 5107 OD1 ASN A 706 55.476 224.442 819.711 1.00 68.56 O ANISOU 5107 OD1 ASN A 706 9309 9997 6743 401 -289 1374 O ATOM 5108 ND2 ASN A 706 56.557 224.946 821.617 1.00 40.33 N ANISOU 5108 ND2 ASN A 706 5843 6446 3033 541 -167 1132 N ATOM 5109 C ASN A 706 55.824 227.721 822.309 1.00 61.97 C ANISOU 5109 C ASN A 706 8678 9531 5337 605 103 1324 C ATOM 5110 O ASN A 706 56.937 227.519 822.800 1.00 63.96 O ANISOU 5110 O ASN A 706 9029 9751 5521 667 68 1151 O ATOM 5111 N SER A 707 55.527 228.801 821.593 1.00 72.91 N ANISOU 5111 N SER A 707 10148 11080 6473 536 158 1522 N ATOM 5112 CA SER A 707 56.465 229.898 821.393 1.00 72.15 C ANISOU 5112 CA SER A 707 10280 11182 5953 524 210 1521 C ATOM 5113 CB SER A 707 55.812 230.997 820.555 1.00 75.56 C ANISOU 5113 CB SER A 707 10793 11796 6121 408 287 1810 C ATOM 5114 OG SER A 707 56.602 232.172 820.541 1.00 85.10 O ANISOU 5114 OG SER A 707 12234 13250 6851 383 407 1792 O ATOM 5115 C SER A 707 56.935 230.461 822.734 1.00 70.02 C ANISOU 5115 C SER A 707 10046 10997 5562 637 390 1329 C ATOM 5116 O SER A 707 58.129 230.668 822.949 1.00 72.47 O ANISOU 5116 O SER A 707 10521 11361 5655 684 375 1154 O ATOM 5117 N ASN A 708 55.984 230.699 823.630 1.00 67.67 N ANISOU 5117 N ASN A 708 9593 10711 5408 679 553 1358 N ATOM 5118 CA ASN A 708 56.289 231.215 824.957 1.00 72.15 C ANISOU 5118 CA ASN A 708 10156 11361 5896 791 737 1184 C ATOM 5119 CB ASN A 708 55.013 231.331 825.795 1.00 74.15 C ANISOU 5119 CB ASN A 708 10198 11608 6366 809 883 1265 C ATOM 5120 CG ASN A 708 54.163 232.521 825.407 1.00 87.40 C ANISOU 5120 CG ASN A 708 11866 13481 7863 694 1125 1488 C ATOM 5121 ND2 ASN A 708 53.622 233.207 826.405 1.00 99.61 N ANISOU 5121 ND2 ASN A 708 13291 15136 9422 719 1401 1466 N ATOM 5122 OD1 ASN A 708 53.993 232.822 824.224 1.00 91.66 O ANISOU 5122 OD1 ASN A 708 12498 14073 8257 573 1079 1691 O ATOM 5123 C ASN A 708 57.294 230.345 825.694 1.00 70.51 C ANISOU 5123 C ASN A 708 9979 10998 5814 910 598 943 C ATOM 5124 O ASN A 708 58.095 230.839 826.480 1.00 78.28 O ANISOU 5124 O ASN A 708 11057 12066 6620 1004 701 754 O ATOM 5125 N VAL A 709 57.241 229.044 825.444 1.00 61.08 N ANISOU 5125 N VAL A 709 8706 9581 4921 896 391 940 N ATOM 5126 CA VAL A 709 58.089 228.104 826.157 1.00 60.27 C ANISOU 5126 CA VAL A 709 8630 9309 4961 979 267 762 C ATOM 5127 CB VAL A 709 57.476 226.697 826.151 1.00 54.68 C ANISOU 5127 CB VAL A 709 7770 8394 4614 937 145 786 C ATOM 5128 CG2 VAL A 709 56.353 226.619 827.163 1.00 53.47 C ANISOU 5128 CG2 VAL A 709 7450 8235 4630 986 218 812 C ATOM 5129 CG1 VAL A 709 58.537 225.646 826.434 1.00 50.51 C ANISOU 5129 CG1 VAL A 709 7324 7691 4178 955 9 652 C ATOM 5130 C VAL A 709 59.494 228.056 825.572 1.00 70.62 C ANISOU 5130 C VAL A 709 10146 10609 6078 963 155 658 C ATOM 5131 O VAL A 709 60.478 228.052 826.309 1.00 81.90 O ANISOU 5131 O VAL A 709 11688 12007 7424 1055 133 483 O ATOM 5132 N TYR A 710 59.587 228.026 824.247 1.00 74.46 N ANISOU 5132 N TYR A 710 10689 11121 6483 846 67 763 N ATOM 5133 CA TYR A 710 60.881 227.938 823.579 1.00 68.26 C ANISOU 5133 CA TYR A 710 10099 10332 5506 810 -74 678 C ATOM 5134 CB TYR A 710 60.709 227.525 822.111 1.00 58.34 C ANISOU 5134 CB TYR A 710 8836 9055 4277 673 -219 833 C ATOM 5135 CG TYR A 710 60.390 226.062 821.923 1.00 56.40 C ANISOU 5135 CG TYR A 710 8427 8591 4412 628 -318 845 C ATOM 5136 CD2 TYR A 710 59.850 225.595 820.736 1.00 58.22 C ANISOU 5136 CD2 TYR A 710 8578 8798 4745 522 -410 990 C ATOM 5137 CE2 TYR A 710 59.567 224.256 820.562 1.00 54.36 C ANISOU 5137 CE2 TYR A 710 7947 8148 4560 474 -463 973 C ATOM 5138 CZ TYR A 710 59.830 223.370 821.576 1.00 52.86 C ANISOU 5138 CZ TYR A 710 7711 7820 4552 514 -430 833 C ATOM 5139 OH TYR A 710 59.549 222.040 821.405 1.00 61.56 O ANISOU 5139 OH TYR A 710 8696 8801 5894 447 -458 821 O ATOM 5140 CE1 TYR A 710 60.372 223.806 822.766 1.00 53.46 C ANISOU 5140 CE1 TYR A 710 7875 7893 4544 619 -373 719 C ATOM 5141 CD1 TYR A 710 60.656 225.143 822.928 1.00 59.94 C ANISOU 5141 CD1 TYR A 710 8820 8872 5083 685 -318 714 C ATOM 5142 C TYR A 710 61.666 229.240 823.659 1.00 68.14 C ANISOU 5142 C TYR A 710 10300 10545 5043 842 22 571 C ATOM 5143 O TYR A 710 62.853 229.277 823.350 1.00 77.17 O ANISOU 5143 O TYR A 710 11635 11704 5981 833 -93 435 O ATOM 5144 N ASN A 711 60.995 230.311 824.071 1.00 59.47 N ANISOU 5144 N ASN A 711 9177 9641 3776 865 250 612 N ATOM 5145 CA ASN A 711 61.628 231.621 824.126 1.00 60.65 C ANISOU 5145 CA ASN A 711 9530 10060 3452 871 422 483 C ATOM 5146 CB ASN A 711 60.743 232.676 823.461 1.00 69.00 C ANISOU 5146 CB ASN A 711 10605 11357 4256 756 598 709 C ATOM 5147 CG ASN A 711 60.639 232.487 821.960 1.00 74.86 C ANISOU 5147 CG ASN A 711 11428 12102 4913 610 386 946 C ATOM 5148 ND2 ASN A 711 60.131 233.500 821.267 1.00 68.61 N ANISOU 5148 ND2 ASN A 711 10736 11543 3791 491 503 1158 N ATOM 5149 OD1 ASN A 711 61.013 231.442 821.430 1.00 83.55 O ANISOU 5149 OD1 ASN A 711 12504 13004 6237 595 128 947 O ATOM 5150 C ASN A 711 61.957 232.048 825.548 1.00 71.95 C ANISOU 5150 C ASN A 711 10949 11538 4852 1022 624 219 C ATOM 5151 O ASN A 711 62.567 233.097 825.757 1.00 83.12 O ANISOU 5151 O ASN A 711 12517 13177 5889 1046 824 10 O ATOM 5152 N ALA A 712 61.546 231.237 826.520 1.00 69.81 N ANISOU 5152 N ALA A 712 10497 11067 4961 1121 583 204 N ATOM 5153 CA ALA A 712 61.782 231.537 827.931 1.00 66.61 C ANISOU 5153 CA ALA A 712 10053 10680 4577 1281 748 -44 C ATOM 5154 CB ALA A 712 61.112 230.505 828.811 1.00 58.90 C ANISOU 5154 CB ALA A 712 8885 9485 4010 1353 634 36 C ATOM 5155 C ALA A 712 63.275 231.599 828.223 1.00 66.52 C ANISOU 5155 C ALA A 712 10247 10644 4382 1368 688 -380 C ATOM 5156 O ALA A 712 64.069 230.963 827.531 1.00 66.81 O ANISOU 5156 O ALA A 712 10420 10560 4404 1309 437 -374 O ATOM 5157 N SER A 713 63.654 232.364 829.245 1.00 61.50 N ANISOU 5157 N SER A 713 9616 10110 3643 1510 936 -712 N ATOM 5158 CA SER A 713 65.062 232.538 829.572 1.00 78.88 C ANISOU 5158 CA SER A 713 12006 12273 5692 1611 911 -1123 C ATOM 5159 CB SER A 713 65.299 233.910 830.207 1.00 96.34 C ANISOU 5159 CB SER A 713 14203 14711 7691 1723 1335 -1516 C ATOM 5160 OG SER A 713 64.621 234.022 831.446 1.00118.54 O ANISOU 5160 OG SER A 713 16734 17450 10858 1881 1539 -1606 O ATOM 5161 C SER A 713 65.559 231.441 830.507 1.00 94.77 C ANISOU 5161 C SER A 713 14002 13966 8040 1744 676 -1252 C ATOM 5162 O SER A 713 65.304 231.469 831.711 1.00102.92 O ANISOU 5162 O SER A 713 14847 14874 9385 1905 773 -1391 O ATOM 5163 N ILE A 714 66.260 230.471 829.930 1.00 96.73 N ANISOU 5163 N ILE A 714 14389 14028 8336 1663 339 -1160 N ATOM 5164 CA ILE A 714 66.902 229.402 830.681 1.00 89.77 C ANISOU 5164 CA ILE A 714 13556 12840 7712 1744 85 -1266 C ATOM 5165 CB ILE A 714 67.789 228.555 829.758 1.00 88.90 C ANISOU 5165 CB ILE A 714 13607 12583 7587 1605 -228 -1175 C ATOM 5166 CG2 ILE A 714 68.753 227.704 830.568 1.00 95.17 C ANISOU 5166 CG2 ILE A 714 14480 13043 8636 1677 -468 -1356 C ATOM 5167 CG1 ILE A 714 66.932 227.678 828.850 1.00 96.16 C ANISOU 5167 CG1 ILE A 714 14392 13456 8687 1441 -341 -720 C ATOM 5168 CD1 ILE A 714 67.729 226.956 827.781 1.00102.03 C ANISOU 5168 CD1 ILE A 714 15248 14087 9433 1294 -576 -654 C ATOM 5169 C ILE A 714 67.788 229.962 831.786 1.00 95.58 C ANISOU 5169 C ILE A 714 14247 13399 8670 1943 167 -1697 C ATOM 5170 O ILE A 714 67.683 229.560 832.941 1.00100.67 O ANISOU 5170 O ILE A 714 14718 13780 9753 2081 96 -1717 O ATOM 5171 N THR A 715 68.663 230.890 831.411 1.00 95.10 N ANISOU 5171 N THR A 715 14342 13474 8317 1956 297 -2044 N ATOM 5172 CA THR A 715 69.649 231.450 832.326 1.00101.83 C ANISOU 5172 CA THR A 715 15165 14141 9385 2144 375 -2523 C ATOM 5173 CB THR A 715 70.345 232.681 831.719 1.00108.41 C ANISOU 5173 CB THR A 715 16184 15260 9747 2122 613 -2906 C ATOM 5174 OG1 THR A 715 69.359 233.610 831.256 1.00114.42 O ANISOU 5174 OG1 THR A 715 16903 16436 10136 2047 959 -2764 O ATOM 5175 CG2 THR A 715 71.230 232.267 830.550 1.00101.43 C ANISOU 5175 CG2 THR A 715 15609 14402 8526 1949 327 -2906 C ATOM 5176 C THR A 715 69.032 231.809 833.674 1.00109.53 C ANISOU 5176 C THR A 715 15821 15003 10791 2349 568 -2606 C ATOM 5177 O THR A 715 68.029 232.518 833.747 1.00112.98 O ANISOU 5177 O THR A 715 16092 15698 11139 2352 868 -2517 O ATOM 5178 N GLU A 716 69.645 231.308 834.737 1.00112.49 N ANISOU 5178 N GLU A 716 16100 14973 11667 2514 372 -2763 N ATOM 5179 CA GLU A 716 69.094 231.443 836.076 1.00117.59 C ANISOU 5179 CA GLU A 716 16424 15442 12814 2718 445 -2799 C ATOM 5180 CB GLU A 716 69.423 230.193 836.894 1.00124.26 C ANISOU 5180 CB GLU A 716 17242 15826 14145 2782 29 -2633 C ATOM 5181 CG GLU A 716 70.728 229.523 836.483 1.00128.81 C ANISOU 5181 CG GLU A 716 18090 16149 14704 2709 -261 -2729 C ATOM 5182 CD GLU A 716 70.629 228.007 836.465 1.00127.71 C ANISOU 5182 CD GLU A 716 18036 15775 14711 2574 -642 -2295 C ATOM 5183 OE1 GLU A 716 69.514 227.481 836.249 1.00117.86 O ANISOU 5183 OE1 GLU A 716 16730 14692 13358 2465 -653 -1905 O ATOM 5184 OE2 GLU A 716 71.670 227.346 836.660 1.00133.66 O ANISOU 5184 OE2 GLU A 716 18920 16179 15687 2566 -916 -2354 O ATOM 5185 C GLU A 716 69.568 232.719 836.773 1.00121.12 C ANISOU 5185 C GLU A 716 16715 15909 13398 2929 775 -3326 C ATOM 5186 O GLU A 716 70.766 232.935 836.955 1.00114.84 O ANISOU 5186 O GLU A 716 16023 14917 12693 3027 728 -3728 O ATOM 5187 N ASN A 717 68.606 233.555 837.159 1.00128.60 N ANISOU 5187 N ASN A 717 17393 17086 14384 2992 1121 -3336 N ATOM 5188 CA ASN A 717 68.889 234.870 837.730 1.00137.98 C ANISOU 5188 CA ASN A 717 18391 18375 15661 3169 1533 -3834 C ATOM 5189 CB ASN A 717 67.594 235.674 837.861 1.00150.37 C ANISOU 5189 CB ASN A 717 19679 20274 17181 3143 1925 -3703 C ATOM 5190 CG ASN A 717 66.603 235.032 838.813 1.00164.04 C ANISOU 5190 CG ASN A 717 21633 22472 18223 2874 2146 -3459 C ATOM 5191 ND2 ASN A 717 65.576 235.783 839.192 1.00166.47 N ANISOU 5191 ND2 ASN A 717 21739 22997 18517 2785 2343 -3153 N ATOM 5192 OD1 ASN A 717 66.760 233.875 839.203 1.00171.67 O ANISOU 5192 OD1 ASN A 717 22944 23585 18696 2745 2114 -3537 O ATOM 5193 C ASN A 717 69.601 234.819 839.080 1.00133.01 C ANISOU 5193 C ASN A 717 17536 17294 15708 3460 1408 -4188 C ATOM 5194 O ASN A 717 70.718 235.318 839.222 1.00130.97 O ANISOU 5194 O ASN A 717 17354 16917 15492 3579 1489 -4679 O ATOM 5195 N SER A 718 68.942 234.225 840.071 1.00129.85 N ANISOU 5195 N SER A 718 16859 16632 15847 3577 1194 -3947 N ATOM 5196 CA SER A 718 69.496 234.119 841.416 1.00124.81 C ANISOU 5196 CA SER A 718 15973 15528 15920 3865 1014 -4206 C ATOM 5197 CB SER A 718 68.512 234.658 842.456 1.00127.39 C ANISOU 5197 CB SER A 718 15825 15870 16708 4037 1195 -4220 C ATOM 5198 OG SER A 718 67.323 233.889 842.481 1.00123.80 O ANISOU 5198 OG SER A 718 15302 15472 16265 3910 980 -3680 O ATOM 5199 C SER A 718 69.845 232.667 841.721 1.00110.36 C ANISOU 5199 C SER A 718 14294 13267 14369 3843 439 -3866 C ATOM 5200 O SER A 718 69.590 231.781 840.905 1.00 98.64 O ANISOU 5200 O SER A 718 13070 11880 12528 3606 233 -3458 O ATOM 5201 N PHE A 719 70.444 232.392 842.854 1.00105.22 N ANISOU 5201 N PHE A 719 13490 12137 14352 4075 177 -4019 N ATOM 5202 CA PHE A 719 70.711 231.010 843.158 1.00 98.15 C ANISOU 5202 CA PHE A 719 12751 10852 13689 4023 -356 -3637 C ATOM 5203 CB PHE A 719 71.546 230.866 844.397 1.00 96.31 C ANISOU 5203 CB PHE A 719 12364 10052 14179 4296 -636 -3855 C ATOM 5204 CG PHE A 719 70.801 231.139 845.623 1.00 91.82 C ANISOU 5204 CG PHE A 719 11371 9349 14166 4527 -671 -3834 C ATOM 5205 CD2 PHE A 719 71.269 232.028 846.540 1.00 99.85 C ANISOU 5205 CD2 PHE A 719 12066 10132 15742 4840 -530 -4327 C ATOM 5206 CE2 PHE A 719 70.582 232.278 847.668 1.00105.07 C ANISOU 5206 CE2 PHE A 719 12297 10659 16965 5058 -587 -4309 C ATOM 5207 CZ PHE A 719 69.422 231.649 847.898 1.00102.81 C ANISOU 5207 CZ PHE A 719 11923 10482 16658 4957 -801 -3805 C ATOM 5208 CE1 PHE A 719 68.940 230.768 846.993 1.00 91.95 C ANISOU 5208 CE1 PHE A 719 10889 9349 14700 4643 -924 -3335 C ATOM 5209 CD1 PHE A 719 69.624 230.512 845.859 1.00 83.54 C ANISOU 5209 CD1 PHE A 719 10228 8409 13104 4435 -851 -3347 C ATOM 5210 C PHE A 719 69.385 230.313 843.344 1.00 98.47 C ANISOU 5210 C PHE A 719 12687 11015 13712 3918 -513 -3106 C ATOM 5211 O PHE A 719 69.261 229.132 843.103 1.00 97.70 O ANISOU 5211 O PHE A 719 12800 10824 13497 3747 -846 -2683 O ATOM 5212 N PHE A 720 68.346 231.047 843.688 1.00 99.72 N ANISOU 5212 N PHE A 720 12524 11418 13948 3991 -246 -3132 N ATOM 5213 CA PHE A 720 67.071 230.382 843.847 1.00 84.13 C ANISOU 5213 CA PHE A 720 10455 9555 11957 3880 -414 -2660 C ATOM 5214 C PHE A 720 66.703 229.760 842.542 1.00 81.75 C ANISOU 5214 C PHE A 720 10483 9553 11027 3568 -405 -2325 C ATOM 5215 O PHE A 720 66.330 228.618 842.497 1.00 80.30 O ANISOU 5215 O PHE A 720 10434 9288 10787 3434 -725 -1924 O ATOM 5216 CB PHE A 720 65.960 231.374 844.145 1.00 72.34 C ANISOU 5216 CB PHE A 720 8581 8350 10556 3945 -62 -2750 C ATOM 5217 CG PHE A 720 66.036 232.003 845.483 1.00 75.91 C ANISOU 5217 CG PHE A 720 8606 8544 11693 4255 -55 -3049 C ATOM 5218 CD1 PHE A 720 65.298 231.525 846.522 1.00 76.21 C ANISOU 5218 CD1 PHE A 720 8375 8382 12200 4356 -381 -2810 C ATOM 5219 CE1 PHE A 720 65.359 232.117 847.741 1.00 86.26 C ANISOU 5219 CE1 PHE A 720 9218 9406 14152 4652 -399 -3084 C ATOM 5220 CZ PHE A 720 66.140 233.195 847.934 1.00 85.73 C ANISOU 5220 CZ PHE A 720 8976 9293 14302 4851 -46 -3624 C ATOM 5221 CE2 PHE A 720 66.863 233.690 846.911 1.00 85.52 C ANISOU 5221 CE2 PHE A 720 9238 9490 13768 4743 309 -3887 C ATOM 5222 CD2 PHE A 720 66.811 233.102 845.693 1.00 80.64 C ANISOU 5222 CD2 PHE A 720 9055 9117 12468 4445 284 -3587 C ATOM 5223 N MSE A 721 66.773 230.517 841.468 1.00 83.76 N ANISOU 5223 N MSE A 721 10874 10151 10799 3450 -45 -2495 N ATOM 5224 CA MSE A 721 66.363 229.965 840.207 1.00 75.54 C ANISOU 5224 CA MSE A 721 10097 9393 9211 3169 -42 -2167 C ATOM 5225 C MSE A 721 67.149 228.705 839.958 1.00 67.52 C ANISOU 5225 C MSE A 721 9389 8134 8131 3053 -418 -1974 C ATOM 5226 O MSE A 721 66.580 227.702 839.654 1.00 67.70 O ANISOU 5226 O MSE A 721 9535 8222 7967 2870 -588 -1596 O ATOM 5227 CB MSE A 721 66.524 230.982 839.079 1.00 87.14 C ANISOU 5227 CB MSE A 721 11681 11257 10172 3063 368 -2368 C ATOM 5228 CG MSE A 721 66.128 230.496 837.662 1.00163.23 C ANISOU 5228 CG MSE A 721 21584 21175 19259 2781 354 -2033 C ATOM 5229 SE MSE A 721 64.335 229.817 837.349 1.00119.65 Se ANISOU 5229 SE MSE A 721 15960 15788 13715 2613 231 -1477 Se ATOM 5230 CE MSE A 721 64.427 229.667 835.460 1.00123.59 C ANISOU 5230 CE MSE A 721 15970 16209 14780 2852 374 -1621 C ATOM 5231 N THR A 722 68.457 228.734 840.099 1.00 77.93 N ANISOU 5231 N THR A 722 10821 9164 9625 3150 -536 -2248 N ATOM 5232 CA THR A 722 69.251 227.554 839.812 1.00 82.82 C ANISOU 5232 CA THR A 722 11717 9523 10228 3020 -891 -2057 C ATOM 5233 C THR A 722 68.882 226.361 840.668 1.00 82.39 C ANISOU 5233 C THR A 722 11627 9181 10497 3016 -1268 -1672 C ATOM 5234 O THR A 722 68.963 225.226 840.240 1.00 80.03 O ANISOU 5234 O THR A 722 11537 8823 10046 2820 -1495 -1349 O ATOM 5235 CB THR A 722 70.726 227.818 839.863 1.00 79.55 C ANISOU 5235 CB THR A 722 11432 8833 9960 3108 -950 -2441 C ATOM 5236 CG2 THR A 722 71.025 228.945 840.804 1.00 85.49 C ANISOU 5236 CG2 THR A 722 11930 9461 11090 3398 -757 -2901 C ATOM 5237 OG1 THR A 722 71.368 226.635 840.315 1.00 75.81 O ANISOU 5237 OG1 THR A 722 11085 7934 9785 3070 -1362 -2225 O ATOM 5238 N PHE A 723 68.527 226.614 841.910 1.00 76.11 N ANISOU 5238 N PHE A 723 10563 8198 10159 3232 -1344 -1716 N ATOM 5239 CA PHE A 723 68.130 225.538 842.783 1.00 71.59 C ANISOU 5239 CA PHE A 723 9966 7372 9862 3229 -1731 -1339 C ATOM 5240 C PHE A 723 66.900 224.863 842.261 1.00 70.51 C ANISOU 5240 C PHE A 723 9877 7546 9369 3015 -1733 -945 C ATOM 5241 O PHE A 723 66.822 223.660 842.212 1.00 77.43 O ANISOU 5241 O PHE A 723 10936 8333 10149 2852 -2000 -595 O ATOM 5242 CB PHE A 723 67.828 226.099 844.158 1.00 70.31 C ANISOU 5242 CB PHE A 723 9455 7003 10255 3513 -1803 -1476 C ATOM 5243 CG PHE A 723 67.261 225.103 845.114 1.00 74.74 C ANISOU 5243 CG PHE A 723 9974 7349 11075 3517 -2223 -1076 C ATOM 5244 CD1 PHE A 723 65.941 224.783 845.088 1.00 67.52 C ANISOU 5244 CD1 PHE A 723 8978 6706 9971 3406 -2233 -792 C ATOM 5245 CE1 PHE A 723 65.436 223.887 845.971 1.00 69.14 C ANISOU 5245 CE1 PHE A 723 9167 6737 10367 3401 -2634 -448 C ATOM 5246 CZ PHE A 723 66.232 223.308 846.883 1.00 68.92 C ANISOU 5246 CZ PHE A 723 9208 6258 10720 3503 -3033 -338 C ATOM 5247 CE2 PHE A 723 67.528 223.621 846.929 1.00 71.81 C ANISOU 5247 CE2 PHE A 723 9637 6319 11328 3619 -3027 -598 C ATOM 5248 CD2 PHE A 723 68.046 224.514 846.058 1.00 79.20 C ANISOU 5248 CD2 PHE A 723 10584 7431 12077 3630 -2622 -988 C ATOM 5249 N PHE A 724 65.939 225.645 841.825 1.00 71.08 N ANISOU 5249 N PHE A 724 9787 7988 9232 2999 -1413 -1013 N ATOM 5250 CA PHE A 724 64.694 225.081 841.385 1.00 77.30 C ANISOU 5250 CA PHE A 724 10584 9042 9746 2816 -1411 -682 C ATOM 5251 C PHE A 724 64.947 224.169 840.224 1.00 80.75 C ANISOU 5251 C PHE A 724 11334 9579 9767 2560 -1457 -470 C ATOM 5252 O PHE A 724 64.392 223.107 840.145 1.00 82.38 O ANISOU 5252 O PHE A 724 11636 9806 9857 2408 -1635 -151 O ATOM 5253 CB PHE A 724 63.751 226.179 840.930 1.00 93.24 C ANISOU 5253 CB PHE A 724 12397 11426 11606 2818 -1024 -808 C ATOM 5254 CG PHE A 724 63.375 227.167 842.008 1.00112.62 C ANISOU 5254 CG PHE A 724 14478 13830 14482 3053 -911 -1033 C ATOM 5255 CD1 PHE A 724 63.251 226.775 843.321 1.00117.11 C ANISOU 5255 CD1 PHE A 724 14870 14103 15522 3210 -1234 -963 C ATOM 5256 CE1 PHE A 724 62.888 227.683 844.293 1.00120.46 C ANISOU 5256 CE1 PHE A 724 14905 14477 16388 3431 -1139 -1180 C ATOM 5257 CZ PHE A 724 62.629 228.987 843.964 1.00121.58 C ANISOU 5257 CZ PHE A 724 14835 14881 16477 3478 -674 -1468 C ATOM 5258 CE2 PHE A 724 62.723 229.389 842.662 1.00120.93 C ANISOU 5258 CE2 PHE A 724 14961 15114 15875 3304 -338 -1513 C ATOM 5259 CD2 PHE A 724 63.087 228.485 841.688 1.00118.32 C ANISOU 5259 CD2 PHE A 724 15013 14816 15126 3101 -480 -1294 C ATOM 5260 N ARG A 725 65.789 224.588 839.306 1.00 87.26 N ANISOU 5260 N ARG A 725 12310 10478 10367 2509 -1292 -667 N ATOM 5261 CA ARG A 725 66.092 223.764 838.157 1.00 79.43 C ANISOU 5261 CA ARG A 725 11578 9572 9029 2272 -1343 -489 C ATOM 5262 CB ARG A 725 66.932 224.537 837.156 1.00 73.68 C ANISOU 5262 CB ARG A 725 10971 8971 8053 2244 -1147 -765 C ATOM 5263 CG ARG A 725 67.569 223.658 836.120 1.00 74.62 C ANISOU 5263 CG ARG A 725 11336 9079 7938 2028 -1276 -631 C ATOM 5264 CD ARG A 725 68.914 223.184 836.564 1.00 80.05 C ANISOU 5264 CD ARG A 725 12154 9385 8877 2053 -1515 -734 C ATOM 5265 NE ARG A 725 69.850 224.286 836.596 1.00 82.29 N ANISOU 5265 NE ARG A 725 12442 9610 9213 2198 -1397 -1166 N ATOM 5266 CZ ARG A 725 71.145 224.144 836.792 1.00 88.19 C ANISOU 5266 CZ ARG A 725 13307 10038 10162 2225 -1564 -1364 C ATOM 5267 NH2 ARG A 725 71.926 225.199 836.812 1.00 95.94 N ANISOU 5267 NH2 ARG A 725 14290 10993 11169 2362 -1432 -1807 N ATOM 5268 NH1 ARG A 725 71.659 222.946 836.955 1.00 86.05 N ANISOU 5268 NH1 ARG A 725 13157 9476 10062 2102 -1852 -1126 N ATOM 5269 C ARG A 725 66.804 222.495 838.515 1.00 80.84 C ANISOU 5269 C ARG A 725 11933 9433 9349 2189 -1678 -287 C ATOM 5270 O ARG A 725 66.501 221.448 837.993 1.00 88.18 O ANISOU 5270 O ARG A 725 12992 10430 10082 1985 -1770 -3 O ATOM 5271 N SER A 726 67.769 222.588 839.408 1.00 77.58 N ANISOU 5271 N SER A 726 11519 8661 9297 2340 -1850 -438 N ATOM 5272 CA SER A 726 68.523 221.418 839.796 1.00 80.50 C ANISOU 5272 CA SER A 726 12066 8690 9832 2249 -2176 -221 C ATOM 5273 CB SER A 726 69.642 221.795 840.729 1.00 83.93 C ANISOU 5273 CB SER A 726 12471 8700 10720 2452 -2338 -457 C ATOM 5274 OG SER A 726 70.677 222.416 840.016 1.00 88.45 O ANISOU 5274 OG SER A 726 13133 9254 11221 2456 -2202 -804 O ATOM 5275 C SER A 726 67.625 220.425 840.463 1.00 81.12 C ANISOU 5275 C SER A 726 12134 8748 9941 2178 -2384 168 C ATOM 5276 O SER A 726 67.763 219.231 840.291 1.00 80.00 O ANISOU 5276 O SER A 726 12178 8535 9683 1975 -2550 467 O ATOM 5277 N TYR A 727 66.711 220.941 841.258 1.00 83.86 N ANISOU 5277 N TYR A 727 12256 9161 10445 2340 -2371 149 N ATOM 5278 CA TYR A 727 65.798 220.110 842.040 1.00 81.03 C ANISOU 5278 CA TYR A 727 11872 8786 10129 2298 -2608 481 C ATOM 5279 C TYR A 727 64.992 219.181 841.147 1.00 80.51 C ANISOU 5279 C TYR A 727 11947 9019 9623 2027 -2537 748 C ATOM 5280 O TYR A 727 64.563 218.115 841.577 1.00 89.90 O ANISOU 5280 O TYR A 727 13218 10184 10756 1822 -2670 952 O ATOM 5281 CB TYR A 727 64.849 220.991 842.856 1.00 75.08 C ANISOU 5281 CB TYR A 727 10804 8114 9609 2508 -2563 359 C ATOM 5282 CG TYR A 727 64.017 220.246 843.877 1.00 74.16 C ANISOU 5282 CG TYR A 727 10641 7925 9611 2506 -2887 658 C ATOM 5283 CD2 TYR A 727 64.604 219.704 845.013 1.00 72.97 C ANISOU 5283 CD2 TYR A 727 10543 7386 9797 2595 -3285 818 C ATOM 5284 CE2 TYR A 727 63.850 219.028 845.956 1.00 71.82 C ANISOU 5284 CE2 TYR A 727 10378 7194 9717 2564 -3607 1090 C ATOM 5285 CZ TYR A 727 62.491 218.889 845.771 1.00 65.65 C ANISOU 5285 CZ TYR A 727 9514 6758 8672 2401 -3482 1120 C ATOM 5286 OH TYR A 727 61.747 218.212 846.712 1.00 68.00 O ANISOU 5286 OH TYR A 727 9808 7020 9009 2319 -3786 1324 O ATOM 5287 CE1 TYR A 727 61.880 219.423 844.656 1.00 59.39 C ANISOU 5287 CE1 TYR A 727 8651 6320 7595 2327 -3080 956 C ATOM 5288 CD1 TYR A 727 62.645 220.095 843.712 1.00 65.09 C ANISOU 5288 CD1 TYR A 727 9402 7084 8246 2411 -2821 779 C ATOM 5289 N ILE A 728 64.786 219.596 839.903 1.00 74.37 N ANISOU 5289 N ILE A 728 11173 8534 8550 1934 -2234 622 N ATOM 5290 CA ILE A 728 64.040 218.799 838.939 1.00 87.76 C ANISOU 5290 CA ILE A 728 12924 10478 9944 1604 -2011 683 C ATOM 5291 C ILE A 728 64.964 217.882 838.136 1.00106.99 C ANISOU 5291 C ILE A 728 15561 12823 12267 1377 -2009 737 C ATOM 5292 O ILE A 728 64.597 216.758 837.791 1.00110.48 O ANISOU 5292 O ILE A 728 16044 13308 12625 1112 -1940 843 O ATOM 5293 CB ILE A 728 63.264 219.700 837.979 1.00 86.40 C ANISOU 5293 CB ILE A 728 12614 10619 9594 1617 -1690 537 C ATOM 5294 CG2 ILE A 728 62.760 218.905 836.789 1.00 85.52 C ANISOU 5294 CG2 ILE A 728 12516 10643 9336 1323 -1447 551 C ATOM 5295 CG1 ILE A 728 62.110 220.375 838.722 1.00 79.49 C ANISOU 5295 CG1 ILE A 728 11513 9861 8830 1769 -1674 531 C ATOM 5296 CD1 ILE A 728 61.384 221.407 837.898 1.00 75.27 C ANISOU 5296 CD1 ILE A 728 10839 9617 8143 1805 -1388 432 C ATOM 5297 N ILE A 729 66.167 218.370 837.852 1.00117.20 N ANISOU 5297 N ILE A 729 16959 13985 13587 1501 -2101 660 N ATOM 5298 CA ILE A 729 67.179 217.598 837.134 1.00122.67 C ANISOU 5298 CA ILE A 729 17833 14562 14216 1307 -2151 714 C ATOM 5299 C ILE A 729 67.688 216.386 837.930 1.00131.60 C ANISOU 5299 C ILE A 729 19099 15403 15502 1174 -2405 958 C ATOM 5300 O ILE A 729 68.313 215.484 837.369 1.00139.89 O ANISOU 5300 O ILE A 729 20274 16383 16495 946 -2425 1065 O ATOM 5301 CB ILE A 729 68.359 218.505 836.693 1.00 96.60 C ANISOU 5301 CB ILE A 729 14584 11162 10957 1440 -2159 464 C ATOM 5302 CG2 ILE A 729 69.697 217.788 836.835 1.00100.07 C ANISOU 5302 CG2 ILE A 729 15188 11246 11588 1339 -2372 508 C ATOM 5303 CG1 ILE A 729 68.164 218.959 835.245 1.00 92.98 C ANISOU 5303 CG1 ILE A 729 14120 11030 10179 1347 -1930 345 C ATOM 5304 CD1 ILE A 729 66.800 219.546 834.969 1.00 91.31 C ANISOU 5304 CD1 ILE A 729 13739 11131 9823 1381 -1681 324 C ATOM 5305 N GLU A 730 67.402 216.360 839.232 1.00126.35 N ANISOU 5305 N GLU A 730 18397 14571 15040 1307 -2610 1067 N ATOM 5306 CA GLU A 730 67.816 215.251 840.094 1.00117.97 C ANISOU 5306 CA GLU A 730 17477 13234 14110 1179 -2884 1344 C ATOM 5307 CB GLU A 730 67.074 215.296 841.436 1.00111.69 C ANISOU 5307 CB GLU A 730 16593 12365 13480 1309 -3084 1450 C ATOM 5308 CG GLU A 730 65.577 215.009 841.344 1.00104.31 C ANISOU 5308 CG GLU A 730 15545 11776 12311 1169 -2899 1446 C ATOM 5309 CD GLU A 730 64.879 215.096 842.693 1.00101.41 C ANISOU 5309 CD GLU A 730 15090 11324 12118 1307 -3157 1556 C ATOM 5310 OE1 GLU A 730 65.155 216.056 843.445 1.00 98.77 O ANISOU 5310 OE1 GLU A 730 14622 10795 12110 1624 -3325 1469 O ATOM 5311 OE2 GLU A 730 64.047 214.211 842.995 1.00 97.33 O ANISOU 5311 OE2 GLU A 730 14620 10924 11436 1114 -3199 1716 O ATOM 5312 C GLU A 730 67.608 213.893 839.418 1.00115.39 C ANISOU 5312 C GLU A 730 17251 13060 13533 797 -2758 1506 C ATOM 5313 O GLU A 730 66.893 213.028 839.927 1.00113.73 O ANISOU 5313 O GLU A 730 17062 12917 13234 642 -2799 1683 O CONECT 9 8 15 10 CONECT 7 3 8 CONECT 622 621 628 623 CONECT 620 616 621 CONECT 1758 1757 1759 1764 CONECT 1756 1750 1757 CONECT 2014 2015 2020 2013 CONECT 2012 2005 2013 CONECT 2975 2974 2981 2976 CONECT 2973 2967 2974 CONECT 3502 3497 3503 3504 CONECT 3496 3494 3497 CONECT 3837 3836 3838 3843 CONECT 3835 3831 3836 CONECT 4221 4220 4222 4227 CONECT 4219 4217 4220 CONECT 5225 5224 5226 5231 CONECT 5223 5214 5224 END