HEADER STRUCTURAL PROTEIN 02-JUL-21 7F8X TITLE CRYSTAL STRUCTURE OF THE CHOLECYSTOKININ RECEPTOR CCKAR IN COMPLEX TITLE 2 WITH NN9056 COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHOLECYSTOKININ RECEPTOR TYPE A,ENDOLYSIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: CCK-A RECEPTOR,CCK-AR,CHOLECYSTOKININ-1 RECEPTOR,CCK1-R, COMPND 5 LYSIS PROTEIN,LYSOZYME,MURAMIDASE; COMPND 6 EC: 3.2.1.17; COMPND 7 ENGINEERED: YES; COMPND 8 MUTATION: YES; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: ASP-SMF-NLE-GLY-TRP-NLE-OEM-MEA-NH2 (NN9056); COMPND 11 CHAIN: C; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA VIRUS T4; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 10665; SOURCE 5 GENE: CCKAR, CCKRA; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 MOL_ID: 2; SOURCE 9 SYNTHETIC: YES; SOURCE 10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 11 ORGANISM_TAXID: 32630 KEYWDS G PROTEIN-COULPED RECEPTOR, STRUCTURAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR X.ZHANG,C.HE,M.WANG,Q.ZHOU,D.YANG,Y.ZHU,B.WU,Q.ZHAO REVDAT 1 29-DEC-21 7F8X 0 JRNL AUTH X.ZHANG,C.HE,M.WANG,Q.ZHOU,D.YANG,Y.ZHU,W.FENG,H.ZHANG, JRNL AUTH 2 A.DAI,X.CHU,J.WANG,Z.YANG,Y.JIANG,U.SENSFUSS,Q.TAN,S.HAN, JRNL AUTH 3 S.REEDTZ-RUNGE,H.E.XU,S.ZHAO,M.W.WANG,B.WU,Q.ZHAO JRNL TITL STRUCTURES OF THE HUMAN CHOLECYSTOKININ RECEPTORS BOUND TO JRNL TITL 2 AGONISTS AND ANTAGONISTS. JRNL REF NAT.CHEM.BIOL. V. 17 1230 2021 JRNL REFN ESSN 1552-4469 JRNL PMID 34556863 JRNL DOI 10.1038/S41589-021-00866-8 REMARK 2 REMARK 2 RESOLUTION. 3.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19.2_4158 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.54 REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0 REMARK 3 NUMBER OF REFLECTIONS : 26392 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.240 REMARK 3 R VALUE (WORKING SET) : 0.238 REMARK 3 FREE R VALUE : 0.261 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900 REMARK 3 FREE R VALUE TEST SET COUNT : 2636 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 3.1070 - 3.0000 0.00 0 1374 0.3820 0.3140 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : NULL REMARK 3 SHRINKAGE RADIUS : NULL REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 92.57 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 117.8 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.002 3674 REMARK 3 ANGLE : 0.606 4986 REMARK 3 CHIRALITY : 0.042 583 REMARK 3 PLANARITY : 0.005 610 REMARK 3 DIHEDRAL : 13.399 1321 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): 7.5318 -18.3596 15.4762 REMARK 3 T TENSOR REMARK 3 T11: 1.1086 T22: 0.6206 REMARK 3 T33: 0.5105 T12: -0.1355 REMARK 3 T13: -0.0370 T23: -0.0390 REMARK 3 L TENSOR REMARK 3 L11: 0.9460 L22: 1.6508 REMARK 3 L33: 6.0810 L12: -0.1517 REMARK 3 L13: -0.7664 L23: -1.0218 REMARK 3 S TENSOR REMARK 3 S11: -0.0988 S12: -0.1112 S13: -0.0230 REMARK 3 S21: 0.0441 S22: -0.0391 S23: -0.0463 REMARK 3 S31: -0.1332 S32: 0.1285 S33: 0.1602 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 7F8X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-JUL-21. REMARK 100 THE DEPOSITION ID IS D_1300022811. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 28-JUL-18 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SPRING-8 REMARK 200 BEAMLINE : BL41XU REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS VERSION JAN 26, 2018 REMARK 200 DATA SCALING SOFTWARE : XSCALE VERSION JAN 26, 2018 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26470 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1 REMARK 200 DATA REDUNDANCY : 4.400 REMARK 200 R MERGE (I) : 0.20600 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.4500 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) : 3.08 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.57300 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER 1.19.2 REMARK 200 STARTING MODEL: 5ZBQ REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 58.70 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES,7.5, 10 (V/V) PPG400 AND REMARK 280 100 MM AMMONIUM ACETATE, LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 36.25000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2020 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 23360 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C 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 ASP A -8 REMARK 465 TYR A -7 REMARK 465 LYS A -6 REMARK 465 ASP A -5 REMARK 465 ASP A -4 REMARK 465 ASP A -3 REMARK 465 ASP A -2 REMARK 465 GLY A -1 REMARK 465 ALA A 0 REMARK 465 PRO A 1 REMARK 465 ASP A 2 REMARK 465 VAL A 3 REMARK 465 VAL A 4 REMARK 465 ASP A 5 REMARK 465 SER A 6 REMARK 465 LEU A 7 REMARK 465 LEU A 8 REMARK 465 VAL A 9 REMARK 465 ASN A 10 REMARK 465 GLY A 11 REMARK 465 SER A 12 REMARK 465 ASN A 13 REMARK 465 ILE A 14 REMARK 465 THR A 15 REMARK 465 PRO A 16 REMARK 465 PRO A 17 REMARK 465 CYS A 18 REMARK 465 GLU A 19 REMARK 465 LEU A 20 REMARK 465 GLY A 21 REMARK 465 LEU A 22 REMARK 465 GLU A 23 REMARK 465 ASN A 24 REMARK 465 GLU A 25 REMARK 465 THR A 26 REMARK 465 LEU A 27 REMARK 465 PHE A 28 REMARK 465 CYS A 29 REMARK 465 LEU A 30 REMARK 465 ASP A 31 REMARK 465 GLN A 32 REMARK 465 PRO A 33 REMARK 465 ARG A 34 REMARK 465 PRO A 35 REMARK 465 SER A 36 REMARK 465 PHE A 615 REMARK 465 MET A 616 REMARK 465 ALA A 617 REMARK 465 THR A 618 REMARK 465 PHE A 619 REMARK 465 PRO A 620 REMARK 465 CYS A 621 REMARK 465 CYS A 622 REMARK 465 PRO A 623 REMARK 465 ASN A 624 REMARK 465 PRO A 625 REMARK 465 GLY A 626 REMARK 465 PRO A 627 REMARK 465 PRO A 628 REMARK 465 GLY A 629 REMARK 465 ALA A 630 REMARK 465 ARG A 631 REMARK 465 GLY A 632 REMARK 465 GLU A 633 REMARK 465 VAL A 634 REMARK 465 GLY A 635 REMARK 465 GLU A 636 REMARK 465 GLU A 637 REMARK 465 GLU A 638 REMARK 465 GLU A 639 REMARK 465 GLY A 640 REMARK 465 GLU A 641 REMARK 465 PHE A 642 REMARK 465 LEU A 643 REMARK 465 GLU A 644 REMARK 465 VAL A 645 REMARK 465 LEU A 646 REMARK 465 PHE A 647 REMARK 465 GLN A 648 REMARK 465 GLY A 649 REMARK 465 PRO A 650 REMARK 465 HIS A 651 REMARK 465 HIS A 652 REMARK 465 HIS A 653 REMARK 465 HIS A 654 REMARK 465 HIS A 655 REMARK 465 HIS A 656 REMARK 465 HIS A 657 REMARK 465 HIS A 658 REMARK 465 HIS A 659 REMARK 465 HIS A 660 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLU A 250 CD OE1 OE2 REMARK 470 LYS A 255 CD CE NZ REMARK 470 LYS A 274 CD CE NZ REMARK 470 ASN A 279 CG OD1 ND2 REMARK 470 LYS A 355 CG CD CE NZ REMARK 470 LYS A 439 CG CD CE NZ 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 CYS A 94 -37.99 -136.30 REMARK 500 PHE A 97 11.24 -65.21 REMARK 500 LYS A 187 -79.08 -98.96 REMARK 500 PHE A 218 -48.81 -141.55 REMARK 500 ILE A 268 70.21 -109.64 REMARK 500 VAL A 431 74.77 -113.58 REMARK 500 LYS A 498 5.40 57.96 REMARK 500 SER A 582 -21.28 -155.41 REMARK 500 NLE C 3 117.19 25.63 REMARK 500 OEM C 7 109.65 -58.49 REMARK 500 REMARK 500 REMARK: NULL DBREF 7F8X A 2 240 UNP P32238 CCKAR_HUMAN 2 240 DBREF 7F8X A 241 535 UNP P00720 ENLYS_BPT4 2 161 DBREF 7F8X A 536 640 UNP P32238 CCKAR_HUMAN 302 406 DBREF 7F8X C 1 9 PDB 7F8X 7F8X 1 9 SEQADV 7F8X ASP A -8 UNP P32238 EXPRESSION TAG SEQADV 7F8X TYR A -7 UNP P32238 EXPRESSION TAG SEQADV 7F8X LYS A -6 UNP P32238 EXPRESSION TAG SEQADV 7F8X ASP A -5 UNP P32238 EXPRESSION TAG SEQADV 7F8X ASP A -4 UNP P32238 EXPRESSION TAG SEQADV 7F8X ASP A -3 UNP P32238 EXPRESSION TAG SEQADV 7F8X ASP A -2 UNP P32238 EXPRESSION TAG SEQADV 7F8X GLY A -1 UNP P32238 EXPRESSION TAG SEQADV 7F8X ALA A 0 UNP P32238 EXPRESSION TAG SEQADV 7F8X PRO A 1 UNP P32238 EXPRESSION TAG SEQADV 7F8X TRP A 130 UNP P32238 PHE 130 ENGINEERED MUTATION SEQADV 7F8X GLY A 251 UNP P00720 ARG 12 ENGINEERED MUTATION SEQADV 7F8X THR A 428 UNP P00720 CYS 54 ENGINEERED MUTATION SEQADV 7F8X ALA A 471 UNP P00720 CYS 97 ENGINEERED MUTATION SEQADV 7F8X ARG A 511 UNP P00720 ILE 137 ENGINEERED MUTATION SEQADV 7F8X GLU A 641 UNP P32238 EXPRESSION TAG SEQADV 7F8X PHE A 642 UNP P32238 EXPRESSION TAG SEQADV 7F8X LEU A 643 UNP P32238 EXPRESSION TAG SEQADV 7F8X GLU A 644 UNP P32238 EXPRESSION TAG SEQADV 7F8X VAL A 645 UNP P32238 EXPRESSION TAG SEQADV 7F8X LEU A 646 UNP P32238 EXPRESSION TAG SEQADV 7F8X PHE A 647 UNP P32238 EXPRESSION TAG SEQADV 7F8X GLN A 648 UNP P32238 EXPRESSION TAG SEQADV 7F8X GLY A 649 UNP P32238 EXPRESSION TAG SEQADV 7F8X PRO A 650 UNP P32238 EXPRESSION TAG SEQADV 7F8X HIS A 651 UNP P32238 EXPRESSION TAG SEQADV 7F8X HIS A 652 UNP P32238 EXPRESSION TAG SEQADV 7F8X HIS A 653 UNP P32238 EXPRESSION TAG SEQADV 7F8X HIS A 654 UNP P32238 EXPRESSION TAG SEQADV 7F8X HIS A 655 UNP P32238 EXPRESSION TAG SEQADV 7F8X HIS A 656 UNP P32238 EXPRESSION TAG SEQADV 7F8X HIS A 657 UNP P32238 EXPRESSION TAG SEQADV 7F8X HIS A 658 UNP P32238 EXPRESSION TAG SEQADV 7F8X HIS A 659 UNP P32238 EXPRESSION TAG SEQADV 7F8X HIS A 660 UNP P32238 EXPRESSION TAG SEQRES 1 A 534 ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO ASP VAL VAL SEQRES 2 A 534 ASP SER LEU LEU VAL ASN GLY SER ASN ILE THR PRO PRO SEQRES 3 A 534 CYS GLU LEU GLY LEU GLU ASN GLU THR LEU PHE CYS LEU SEQRES 4 A 534 ASP GLN PRO ARG PRO SER LYS GLU TRP GLN PRO ALA VAL SEQRES 5 A 534 GLN ILE LEU LEU TYR SER LEU ILE PHE LEU LEU SER VAL SEQRES 6 A 534 LEU GLY ASN THR LEU VAL ILE THR VAL LEU ILE ARG ASN SEQRES 7 A 534 LYS ARG MET ARG THR VAL THR ASN ILE PHE LEU LEU SER SEQRES 8 A 534 LEU ALA VAL SER ASP LEU MET LEU CYS LEU PHE CYS MET SEQRES 9 A 534 PRO PHE ASN LEU ILE PRO ASN LEU LEU LYS ASP PHE ILE SEQRES 10 A 534 PHE GLY SER ALA VAL CYS LYS THR THR THR TYR PHE MET SEQRES 11 A 534 GLY THR SER VAL SER VAL SER THR TRP ASN LEU VAL ALA SEQRES 12 A 534 ILE SER LEU GLU ARG TYR GLY ALA ILE CYS LYS PRO LEU SEQRES 13 A 534 GLN SER ARG VAL TRP GLN THR LYS SER HIS ALA LEU LYS SEQRES 14 A 534 VAL ILE ALA ALA THR TRP CYS LEU SER PHE THR ILE MET SEQRES 15 A 534 THR PRO TYR PRO ILE TYR SER ASN LEU VAL PRO PHE THR SEQRES 16 A 534 LYS ASN ASN ASN GLN THR ALA ASN MET CYS ARG PHE LEU SEQRES 17 A 534 LEU PRO ASN ASP VAL MET GLN GLN SER TRP HIS THR PHE SEQRES 18 A 534 LEU LEU LEU ILE LEU PHE LEU ILE PRO GLY ILE VAL MET SEQRES 19 A 534 MET VAL ALA TYR GLY LEU ILE SER LEU GLU LEU TYR GLN SEQRES 20 A 534 GLY ILE ASN ILE PHE GLU MET LEU ARG ILE ASP GLU GLY SEQRES 21 A 534 LEU ARG LEU LYS ILE TYR LYS ASP THR GLU GLY TYR TYR SEQRES 22 A 534 THR ILE GLY ILE GLY HIS LEU LEU THR LYS SER PRO SER SEQRES 23 A 534 LEU ASN ALA ALA LYS SER GLU LEU ASP LYS ALA ILE GLY SEQRES 24 A 534 ARG ASN THR ASN GLY VAL ILE THR LYS ASP GLU ALA GLU SEQRES 25 A 534 LYS LEU PHE ASN GLN ASP VAL ASP ALA ALA VAL ARG GLY SEQRES 26 A 534 ILE LEU ARG ASN ALA LYS LEU LYS PRO VAL TYR ASP SER SEQRES 27 A 534 LEU ASP ALA VAL ARG ARG ALA ALA LEU ILE ASN MET VAL SEQRES 28 A 534 PHE GLN MET GLY GLU THR GLY VAL ALA GLY PHE THR ASN SEQRES 29 A 534 SER LEU ARG MET LEU GLN GLN LYS ARG TRP ASP GLU ALA SEQRES 30 A 534 ALA VAL ASN LEU ALA LYS SER ARG TRP TYR ASN GLN THR SEQRES 31 A 534 PRO ASN ARG ALA LYS ARG VAL ILE THR THR PHE ARG THR SEQRES 32 A 534 GLY THR TRP ASP ALA TYR ALA ALA ASN LEU MET ALA LYS SEQRES 33 A 534 LYS ARG VAL ILE ARG MET LEU ILE VAL ILE VAL VAL LEU SEQRES 34 A 534 PHE PHE LEU CYS TRP MET PRO ILE PHE SER ALA ASN ALA SEQRES 35 A 534 TRP ARG ALA TYR ASP THR ALA SER ALA GLU ARG ARG LEU SEQRES 36 A 534 SER GLY THR PRO ILE SER PHE ILE LEU LEU LEU SER TYR SEQRES 37 A 534 THR SER SER CYS VAL ASN PRO ILE ILE TYR CYS PHE MET SEQRES 38 A 534 ASN LYS ARG PHE ARG LEU GLY PHE MET ALA THR PHE PRO SEQRES 39 A 534 CYS CYS PRO ASN PRO GLY PRO PRO GLY ALA ARG GLY GLU SEQRES 40 A 534 VAL GLY GLU GLU GLU GLU GLY GLU PHE LEU GLU VAL LEU SEQRES 41 A 534 PHE GLN GLY PRO HIS HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 42 A 534 HIS SEQRES 1 C 9 ASP SMF NLE GLY TRP NLE OEM MEA NH2 HET SMF C 2 16 HET NLE C 3 8 HET NLE C 6 8 HET OEM C 7 9 HET MEA C 8 12 HET NH2 C 9 1 HETNAM SMF 4-SULFOMETHYL-L-PHENYLALANINE HETNAM NLE NORLEUCINE HETNAM OEM N-METHYL-D-ASPARTIC ACID HETNAM MEA N-METHYLPHENYLALANINE HETNAM NH2 AMINO GROUP FORMUL 2 SMF C10 H13 N O5 S FORMUL 2 NLE 2(C6 H13 N O2) FORMUL 2 OEM C5 H9 N O4 FORMUL 2 MEA C10 H13 N O2 FORMUL 2 NH2 H2 N HELIX 1 AA1 GLU A 38 ASN A 69 1 32 HELIX 2 AA2 THR A 74 PHE A 93 1 20 HELIX 3 AA3 MET A 95 LYS A 105 1 11 HELIX 4 AA4 GLY A 110 CYS A 144 1 35 HELIX 5 AA5 THR A 154 MET A 173 1 20 HELIX 6 AA6 THR A 174 TYR A 179 1 6 HELIX 7 AA7 ASN A 202 PHE A 218 1 17 HELIX 8 AA8 PHE A 218 GLN A 238 1 21 HELIX 9 AA9 ASN A 241 GLY A 251 1 11 HELIX 10 AB1 SER A 277 ILE A 424 1 13 HELIX 11 AB2 THR A 433 ASN A 455 1 23 HELIX 12 AB3 LYS A 457 ASP A 463 1 7 HELIX 13 AB4 ASP A 466 GLY A 481 1 16 HELIX 14 AB5 GLY A 481 GLY A 487 1 7 HELIX 15 AB6 PHE A 488 GLN A 497 1 10 HELIX 16 AB7 ARG A 499 ALA A 508 1 10 HELIX 17 AB8 SER A 510 THR A 516 1 7 HELIX 18 AB9 THR A 516 GLY A 530 1 15 HELIX 19 AC1 ALA A 537 ASP A 573 1 37 HELIX 20 AC2 ASP A 573 LEU A 581 1 9 HELIX 21 AC3 THR A 584 PHE A 606 1 23 HELIX 22 AC4 MET A 607 ASN A 608 5 2 HELIX 23 AC5 LYS A 609 LEU A 613 5 5 SHEET 1 AA1 2 SER A 180 THR A 186 0 SHEET 2 AA1 2 THR A 192 PHE A 198 -1 O MET A 195 N VAL A 183 SHEET 1 AA2 3 ARG A 253 LYS A 258 0 SHEET 2 AA2 3 TYR A 264 GLY A 267 -1 O THR A 265 N TYR A 257 SHEET 3 AA2 3 HIS A 270 THR A 273 -1 O LEU A 272 N TYR A 264 SSBOND 1 CYS A 114 CYS A 196 1555 1555 2.03 LINK C ASP C 1 N SMF C 2 1555 1555 1.33 LINK C SMF C 2 N NLE C 3 1555 1555 1.34 LINK C NLE C 3 N GLY C 4 1555 1555 1.33 LINK C TRP C 5 N NLE C 6 1555 1555 1.33 LINK C NLE C 6 N OEM C 7 1555 1555 1.33 LINK C OEM C 7 N MEA C 8 1555 1555 1.34 LINK C MEA C 8 N NH2 C 9 1555 1555 1.33 CRYST1 56.600 72.500 87.000 90.00 100.00 90.00 P 1 21 1 2 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.017668 0.000000 0.003115 0.00000 SCALE2 0.000000 0.013793 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011672 0.00000 ATOM 1 N LYS A 37 -13.064 -5.273 -21.841 1.00164.84 N ANISOU 1 N LYS A 37 24268 25306 13058 2826 -2851 1571 N ATOM 2 CA LYS A 37 -13.924 -4.117 -21.621 1.00169.01 C ANISOU 2 CA LYS A 37 24691 26139 13387 3491 -2827 1822 C ATOM 3 C LYS A 37 -13.285 -3.249 -20.530 1.00174.63 C ANISOU 3 C LYS A 37 25738 26279 14336 3778 -2549 1833 C ATOM 4 O LYS A 37 -12.159 -3.518 -20.117 1.00170.40 O ANISOU 4 O LYS A 37 25499 25155 14090 3450 -2400 1658 O ATOM 5 CB LYS A 37 -15.340 -4.571 -21.243 1.00169.89 C ANISOU 5 CB LYS A 37 24137 27077 13337 3518 -3031 1923 C ATOM 6 CG LYS A 37 -16.421 -3.513 -21.415 1.00168.06 C ANISOU 6 CG LYS A 37 23713 27363 12778 4229 -3070 2219 C ATOM 7 CD LYS A 37 -16.588 -3.127 -22.876 1.00157.40 C ANISOU 7 CD LYS A 37 22469 26107 11227 4351 -3156 2306 C ATOM 8 CE LYS A 37 -17.733 -2.146 -23.060 1.00155.53 C ANISOU 8 CE LYS A 37 21955 26297 10844 4954 -3139 2558 C ATOM 9 NZ LYS A 37 -17.438 -0.830 -22.430 1.00162.57 N ANISOU 9 NZ LYS A 37 23240 26706 11823 5561 -2846 2669 N ATOM 10 N GLU A 38 -13.988 -2.213 -20.065 1.00226.08 N ANISOU 10 N GLU A 38 32220 32972 20708 4393 -2475 2041 N ATOM 11 CA GLU A 38 -13.379 -1.250 -19.154 1.00225.52 C ANISOU 11 CA GLU A 38 32570 32318 20799 4698 -2207 2061 C ATOM 12 C GLU A 38 -13.255 -1.767 -17.726 1.00220.15 C ANISOU 12 C GLU A 38 31699 31527 20422 4447 -2127 1931 C ATOM 13 O GLU A 38 -12.486 -1.196 -16.943 1.00214.89 O ANISOU 13 O GLU A 38 31418 30286 19945 4517 -1912 1881 O ATOM 14 CB GLU A 38 -14.177 0.059 -19.142 1.00230.33 C ANISOU 14 CB GLU A 38 33284 33114 21118 5486 -2132 2333 C ATOM 15 CG GLU A 38 -15.250 0.140 -18.058 1.00234.49 C ANISOU 15 CG GLU A 38 33371 34113 21612 5804 -2131 2444 C ATOM 16 CD GLU A 38 -16.594 -0.401 -18.503 1.00237.95 C ANISOU 16 CD GLU A 38 33100 35437 21873 5820 -2363 2553 C ATOM 17 OE1 GLU A 38 -16.655 -1.042 -19.570 1.00237.16 O ANISOU 17 OE1 GLU A 38 32842 35597 21671 5490 -2562 2510 O ATOM 18 OE2 GLU A 38 -17.590 -0.187 -17.781 1.00236.74 O ANISOU 18 OE2 GLU A 38 32548 35725 21678 6146 -2340 2679 O ATOM 19 N TRP A 39 -13.981 -2.827 -17.364 1.00216.13 N ANISOU 19 N TRP A 39 30622 31548 19949 4135 -2294 1876 N ATOM 20 CA TRP A 39 -14.010 -3.247 -15.967 1.00215.26 C ANISOU 20 CA TRP A 39 30311 31389 20089 3968 -2214 1785 C ATOM 21 C TRP A 39 -12.735 -3.970 -15.548 1.00213.09 C ANISOU 21 C TRP A 39 30282 30520 20163 3403 -2122 1535 C ATOM 22 O TRP A 39 -12.345 -3.891 -14.378 1.00212.50 O ANISOU 22 O TRP A 39 30291 30135 20313 3373 -1974 1466 O ATOM 23 CB TRP A 39 -15.228 -4.135 -15.704 1.00220.71 C ANISOU 23 CB TRP A 39 30316 32858 20685 3804 -2414 1823 C ATOM 24 CG TRP A 39 -15.167 -5.478 -16.363 1.00226.48 C ANISOU 24 CG TRP A 39 30818 33797 21438 3145 -2617 1665 C ATOM 25 CD1 TRP A 39 -15.412 -5.760 -17.675 1.00227.22 C ANISOU 25 CD1 TRP A 39 30853 34185 21296 3021 -2808 1689 C ATOM 26 CD2 TRP A 39 -14.847 -6.726 -15.737 1.00226.17 C ANISOU 26 CD2 TRP A 39 30621 33666 21647 2526 -2645 1457 C ATOM 27 NE1 TRP A 39 -15.262 -7.106 -17.906 1.00226.60 N ANISOU 27 NE1 TRP A 39 30616 34186 21297 2350 -2948 1500 N ATOM 28 CE2 TRP A 39 -14.916 -7.722 -16.731 1.00230.55 C ANISOU 28 CE2 TRP A 39 31061 34445 22093 2045 -2846 1359 C ATOM 29 CE3 TRP A 39 -14.509 -7.098 -14.432 1.00219.76 C ANISOU 29 CE3 TRP A 39 29783 32595 21121 2339 -2514 1347 C ATOM 30 CZ2 TRP A 39 -14.656 -9.064 -16.463 1.00234.41 C ANISOU 30 CZ2 TRP A 39 31446 34877 22744 1399 -2908 1157 C ATOM 31 CZ3 TRP A 39 -14.252 -8.431 -14.167 1.00222.39 C ANISOU 31 CZ3 TRP A 39 29982 32894 21622 1710 -2581 1156 C ATOM 32 CH2 TRP A 39 -14.327 -9.398 -15.178 1.00232.13 C ANISOU 32 CH2 TRP A 39 31136 34326 22736 1252 -2770 1064 C ATOM 33 N GLN A 40 -12.072 -4.673 -16.473 1.00159.05 N ANISOU 33 N GLN A 40 23559 23520 13351 2975 -2201 1403 N ATOM 34 CA GLN A 40 -10.855 -5.393 -16.098 1.00150.88 C ANISOU 34 CA GLN A 40 22740 21961 12627 2479 -2105 1183 C ATOM 35 C GLN A 40 -9.698 -4.452 -15.787 1.00136.94 C ANISOU 35 C GLN A 40 21507 19515 11008 2637 -1870 1169 C ATOM 36 O GLN A 40 -9.016 -4.665 -14.769 1.00131.07 O ANISOU 36 O GLN A 40 20845 18428 10528 2437 -1746 1055 O ATOM 37 CB GLN A 40 -10.489 -6.409 -17.186 1.00154.51 C ANISOU 37 CB GLN A 40 23204 22454 13049 2018 -2237 1056 C ATOM 38 CG GLN A 40 -11.654 -7.257 -17.664 1.00161.97 C ANISOU 38 CG GLN A 40 23676 24080 13784 1830 -2490 1078 C ATOM 39 CD GLN A 40 -11.283 -8.160 -18.824 1.00160.40 C ANISOU 39 CD GLN A 40 23576 23870 13500 1403 -2613 952 C ATOM 40 OE1 GLN A 40 -10.350 -7.875 -19.575 1.00157.72 O ANISOU 40 OE1 GLN A 40 23643 23116 13166 1409 -2524 915 O ATOM 41 NE2 GLN A 40 -12.014 -9.258 -18.975 1.00163.66 N ANISOU 41 NE2 GLN A 40 23632 24736 13814 1017 -2811 888 N ATOM 42 N PRO A 41 -9.402 -3.423 -16.594 1.00141.08 N ANISOU 42 N PRO A 41 22415 19819 11369 2958 -1799 1280 N ATOM 43 CA PRO A 41 -8.316 -2.510 -16.200 1.00134.51 C ANISOU 43 CA PRO A 41 22098 18342 10666 3054 -1571 1268 C ATOM 44 C PRO A 41 -8.630 -1.710 -14.950 1.00131.89 C ANISOU 44 C PRO A 41 21831 17905 10377 3395 -1442 1339 C ATOM 45 O PRO A 41 -7.724 -1.439 -14.152 1.00124.66 O ANISOU 45 O PRO A 41 21197 16507 9663 3263 -1282 1254 O ATOM 46 CB PRO A 41 -8.162 -1.604 -17.430 1.00133.06 C ANISOU 46 CB PRO A 41 22286 18034 10236 3343 -1544 1398 C ATOM 47 CG PRO A 41 -8.670 -2.425 -18.558 1.00145.67 C ANISOU 47 CG PRO A 41 23599 20077 11673 3177 -1754 1391 C ATOM 48 CD PRO A 41 -9.838 -3.162 -17.977 1.00150.43 C ANISOU 48 CD PRO A 41 23633 21269 12255 3145 -1920 1396 C ATOM 49 N ALA A 42 -9.894 -1.323 -14.755 1.00128.17 N ANISOU 49 N ALA A 42 21103 17894 9701 3837 -1505 1498 N ATOM 50 CA ALA A 42 -10.244 -0.486 -13.612 1.00117.87 C ANISOU 50 CA ALA A 42 19907 16487 8392 4235 -1362 1581 C ATOM 51 C ALA A 42 -10.017 -1.218 -12.295 1.00116.59 C ANISOU 51 C ALA A 42 19526 16257 8514 3903 -1327 1431 C ATOM 52 O ALA A 42 -9.480 -0.642 -11.341 1.00115.63 O ANISOU 52 O ALA A 42 19713 15709 8512 3969 -1158 1395 O ATOM 53 CB ALA A 42 -11.696 -0.023 -13.725 1.00122.10 C ANISOU 53 CB ALA A 42 20150 17615 8627 4804 -1437 1800 C ATOM 54 N VAL A 43 -10.415 -2.490 -12.223 1.00102.06 N ANISOU 54 N VAL A 43 17184 14824 6770 3527 -1486 1340 N ATOM 55 CA VAL A 43 -10.231 -3.240 -10.986 1.00 99.43 C ANISOU 55 CA VAL A 43 16646 14439 6694 3213 -1453 1206 C ATOM 56 C VAL A 43 -8.765 -3.597 -10.783 1.00 95.49 C ANISOU 56 C VAL A 43 16459 13360 6464 2768 -1357 1022 C ATOM 57 O VAL A 43 -8.315 -3.775 -9.645 1.00 93.31 O ANISOU 57 O VAL A 43 16210 12849 6394 2614 -1264 929 O ATOM 58 CB VAL A 43 -11.126 -4.493 -10.974 1.00 99.98 C ANISOU 58 CB VAL A 43 16120 15111 6758 2929 -1644 1174 C ATOM 59 CG1 VAL A 43 -12.589 -4.099 -11.116 1.00104.30 C ANISOU 59 CG1 VAL A 43 16302 16307 7022 3378 -1737 1380 C ATOM 60 CG2 VAL A 43 -10.715 -5.462 -12.073 1.00101.98 C ANISOU 60 CG2 VAL A 43 16326 15399 7022 2468 -1783 1062 C ATOM 61 N GLN A 44 -7.991 -3.701 -11.866 1.00107.08 N ANISOU 61 N GLN A 44 18154 14612 7921 2567 -1374 976 N ATOM 62 CA GLN A 44 -6.570 -3.993 -11.718 1.00105.85 C ANISOU 62 CA GLN A 44 18271 13950 7996 2181 -1271 826 C ATOM 63 C GLN A 44 -5.812 -2.804 -11.144 1.00104.37 C ANISOU 63 C GLN A 44 18550 13256 7848 2363 -1079 856 C ATOM 64 O GLN A 44 -4.799 -2.989 -10.461 1.00 98.32 O ANISOU 64 O GLN A 44 17922 12138 7296 2074 -983 743 O ATOM 65 CB GLN A 44 -5.969 -4.407 -13.061 1.00111.15 C ANISOU 65 CB GLN A 44 19058 14555 8619 1945 -1324 784 C ATOM 66 CG GLN A 44 -6.110 -5.887 -13.376 1.00115.67 C ANISOU 66 CG GLN A 44 19293 15402 9255 1534 -1467 662 C ATOM 67 CD GLN A 44 -5.502 -6.258 -14.714 1.00124.35 C ANISOU 67 CD GLN A 44 20557 16412 10280 1333 -1503 619 C ATOM 68 OE1 GLN A 44 -4.354 -6.698 -14.785 1.00122.68 O ANISOU 68 OE1 GLN A 44 20521 15865 10225 1040 -1413 509 O ATOM 69 NE2 GLN A 44 -6.269 -6.082 -15.784 1.00124.41 N ANISOU 69 NE2 GLN A 44 20501 16742 10028 1509 -1631 714 N ATOM 70 N ILE A 45 -6.283 -1.585 -11.402 1.00102.28 N ANISOU 70 N ILE A 45 18548 12952 7361 2834 -1020 1012 N ATOM 71 CA ILE A 45 -5.600 -0.401 -10.894 1.00102.43 C ANISOU 71 CA ILE A 45 19086 12457 7375 2991 -833 1041 C ATOM 72 C ILE A 45 -5.881 -0.210 -9.409 1.00 99.00 C ANISOU 72 C ILE A 45 18611 11974 7031 3102 -758 1019 C ATOM 73 O ILE A 45 -4.966 0.044 -8.618 1.00 99.03 O ANISOU 73 O ILE A 45 18882 11561 7183 2899 -642 931 O ATOM 74 CB ILE A 45 -6.000 0.841 -11.711 1.00101.37 C ANISOU 74 CB ILE A 45 19323 12250 6942 3474 -779 1220 C ATOM 75 CG1 ILE A 45 -5.535 0.696 -13.162 1.00 97.86 C ANISOU 75 CG1 ILE A 45 18984 11782 6416 3324 -832 1233 C ATOM 76 CG2 ILE A 45 -5.422 2.103 -11.087 1.00 98.51 C ANISOU 76 CG2 ILE A 45 19549 11342 6537 3645 -578 1254 C ATOM 77 CD1 ILE A 45 -6.231 1.633 -14.122 1.00101.68 C ANISOU 77 CD1 ILE A 45 19685 12375 6572 3824 -836 1426 C ATOM 78 N LEU A 46 -7.148 -0.335 -9.003 1.00 96.87 N ANISOU 78 N LEU A 46 17993 12155 6659 3417 -825 1102 N ATOM 79 CA LEU A 46 -7.483 -0.093 -7.603 1.00 96.91 C ANISOU 79 CA LEU A 46 17976 12127 6718 3576 -738 1095 C ATOM 80 C LEU A 46 -7.017 -1.234 -6.708 1.00 93.47 C ANISOU 80 C LEU A 46 17244 11699 6573 3093 -773 925 C ATOM 81 O LEU A 46 -6.728 -1.009 -5.529 1.00 99.12 O ANISOU 81 O LEU A 46 18089 12182 7390 3074 -672 870 O ATOM 82 CB LEU A 46 -8.988 0.147 -7.450 1.00100.28 C ANISOU 82 CB LEU A 46 18100 13074 6927 4093 -779 1259 C ATOM 83 CG LEU A 46 -9.993 -1.001 -7.555 1.00100.60 C ANISOU 83 CG LEU A 46 17459 13789 6975 3981 -961 1270 C ATOM 84 CD1 LEU A 46 -10.342 -1.535 -6.172 1.00 99.52 C ANISOU 84 CD1 LEU A 46 17028 13800 6986 3891 -933 1211 C ATOM 85 CD2 LEU A 46 -11.246 -0.550 -8.293 1.00105.53 C ANISOU 85 CD2 LEU A 46 17878 14934 7286 4489 -1037 1480 C ATOM 86 N LEU A 47 -6.929 -2.456 -7.238 1.00 90.50 N ANISOU 86 N LEU A 47 16506 11570 6311 2707 -911 840 N ATOM 87 CA LEU A 47 -6.381 -3.558 -6.450 1.00 87.36 C ANISOU 87 CA LEU A 47 15892 11126 6176 2253 -929 682 C ATOM 88 C LEU A 47 -4.878 -3.400 -6.252 1.00 85.66 C ANISOU 88 C LEU A 47 16040 10376 6130 1949 -822 573 C ATOM 89 O LEU A 47 -4.371 -3.548 -5.134 1.00 88.40 O ANISOU 89 O LEU A 47 16420 10529 6638 1786 -755 490 O ATOM 90 CB LEU A 47 -6.695 -4.901 -7.111 1.00 86.70 C ANISOU 90 CB LEU A 47 15395 11415 6133 1931 -1091 623 C ATOM 91 CG LEU A 47 -7.937 -5.668 -6.645 1.00 88.68 C ANISOU 91 CG LEU A 47 15142 12204 6350 1943 -1200 650 C ATOM 92 CD1 LEU A 47 -7.781 -6.090 -5.192 1.00 87.73 C ANISOU 92 CD1 LEU A 47 14920 11993 6422 1795 -1130 568 C ATOM 93 CD2 LEU A 47 -9.209 -4.865 -6.832 1.00 93.53 C ANISOU 93 CD2 LEU A 47 15623 13210 6703 2454 -1229 835 C ATOM 94 N TYR A 48 -4.148 -3.098 -7.327 1.00 93.64 N ANISOU 94 N TYR A 48 17314 11173 7093 1862 -806 581 N ATOM 95 CA TYR A 48 -2.700 -2.958 -7.215 1.00 92.87 C ANISOU 95 CA TYR A 48 17518 10631 7138 1551 -706 497 C ATOM 96 C TYR A 48 -2.307 -1.712 -6.434 1.00 91.33 C ANISOU 96 C TYR A 48 17753 10050 6900 1709 -564 530 C ATOM 97 O TYR A 48 -1.296 -1.725 -5.722 1.00 91.73 O ANISOU 97 O TYR A 48 17939 9816 7099 1425 -493 444 O ATOM 98 CB TYR A 48 -2.063 -2.939 -8.604 1.00 96.51 C ANISOU 98 CB TYR A 48 18139 10994 7536 1428 -713 512 C ATOM 99 CG TYR A 48 -1.694 -4.310 -9.127 1.00 93.88 C ANISOU 99 CG TYR A 48 17517 10826 7329 1069 -798 412 C ATOM 100 CD1 TYR A 48 -0.480 -4.896 -8.792 1.00 94.50 C ANISOU 100 CD1 TYR A 48 17613 10688 7603 705 -736 307 C ATOM 101 CD2 TYR A 48 -2.560 -5.021 -9.947 1.00 90.43 C ANISOU 101 CD2 TYR A 48 16803 10767 6789 1101 -937 427 C ATOM 102 CE1 TYR A 48 -0.137 -6.148 -9.265 1.00 96.67 C ANISOU 102 CE1 TYR A 48 17678 11086 7967 424 -790 221 C ATOM 103 CE2 TYR A 48 -2.225 -6.273 -10.424 1.00100.45 C ANISOU 103 CE2 TYR A 48 17881 12141 8143 770 -1003 327 C ATOM 104 CZ TYR A 48 -1.013 -6.832 -10.080 1.00 99.60 C ANISOU 104 CZ TYR A 48 17836 11780 8229 454 -919 224 C ATOM 105 OH TYR A 48 -0.674 -8.079 -10.552 1.00103.62 O ANISOU 105 OH TYR A 48 18205 12368 8798 170 -962 131 O ATOM 106 N SER A 49 -3.082 -0.631 -6.549 1.00 88.26 N ANISOU 106 N SER A 49 17599 9649 6287 2158 -518 656 N ATOM 107 CA SER A 49 -2.766 0.576 -5.793 1.00 90.80 C ANISOU 107 CA SER A 49 18405 9566 6530 2318 -372 683 C ATOM 108 C SER A 49 -3.017 0.386 -4.302 1.00 89.93 C ANISOU 108 C SER A 49 18170 9477 6523 2324 -345 620 C ATOM 109 O SER A 49 -2.310 0.975 -3.477 1.00 88.34 O ANISOU 109 O SER A 49 18314 8900 6350 2208 -244 570 O ATOM 110 CB SER A 49 -3.575 1.760 -6.324 1.00 93.03 C ANISOU 110 CB SER A 49 19014 9818 6515 2854 -314 846 C ATOM 111 OG SER A 49 -4.963 1.564 -6.121 1.00 98.97 O ANISOU 111 OG SER A 49 19419 11023 7162 3255 -379 932 O ATOM 112 N LEU A 50 -4.008 -0.432 -3.938 1.00 87.30 N ANISOU 112 N LEU A 50 17354 9585 6231 2431 -436 624 N ATOM 113 CA LEU A 50 -4.280 -0.681 -2.525 1.00 86.62 C ANISOU 113 CA LEU A 50 17126 9547 6240 2434 -407 570 C ATOM 114 C LEU A 50 -3.203 -1.564 -1.905 1.00 83.22 C ANISOU 114 C LEU A 50 16575 8975 6071 1917 -424 417 C ATOM 115 O LEU A 50 -2.678 -1.254 -0.829 1.00 85.92 O ANISOU 115 O LEU A 50 17117 9055 6474 1820 -348 356 O ATOM 116 CB LEU A 50 -5.661 -1.315 -2.357 1.00 87.15 C ANISOU 116 CB LEU A 50 16692 10161 6259 2673 -493 633 C ATOM 117 CG LEU A 50 -6.862 -0.376 -2.483 1.00 90.98 C ANISOU 117 CG LEU A 50 17254 10844 6469 3283 -447 804 C ATOM 118 CD1 LEU A 50 -8.164 -1.153 -2.360 1.00 91.95 C ANISOU 118 CD1 LEU A 50 16785 11597 6556 3433 -550 871 C ATOM 119 CD2 LEU A 50 -6.793 0.733 -1.445 1.00 92.64 C ANISOU 119 CD2 LEU A 50 17924 10695 6580 3572 -279 825 C ATOM 120 N ILE A 51 -2.860 -2.671 -2.568 1.00 81.89 N ANISOU 120 N ILE A 51 16096 8979 6038 1594 -522 357 N ATOM 121 CA ILE A 51 -1.835 -3.558 -2.031 1.00 87.32 C ANISOU 121 CA ILE A 51 16666 9556 6955 1153 -530 230 C ATOM 122 C ILE A 51 -0.458 -2.911 -2.067 1.00 88.69 C ANISOU 122 C ILE A 51 17230 9306 7162 927 -443 195 C ATOM 123 O ILE A 51 0.431 -3.313 -1.308 1.00 91.07 O ANISOU 123 O ILE A 51 17506 9480 7618 626 -423 110 O ATOM 124 CB ILE A 51 -1.827 -4.904 -2.781 1.00 83.19 C ANISOU 124 CB ILE A 51 15774 9301 6534 899 -637 181 C ATOM 125 CG1 ILE A 51 -1.324 -4.722 -4.215 1.00 97.63 C ANISOU 125 CG1 ILE A 51 17758 11047 8290 840 -649 211 C ATOM 126 CG2 ILE A 51 -3.213 -5.532 -2.766 1.00 83.07 C ANISOU 126 CG2 ILE A 51 15370 9733 6459 1060 -734 220 C ATOM 127 CD1 ILE A 51 -1.171 -6.021 -4.977 1.00 95.25 C ANISOU 127 CD1 ILE A 51 17179 10943 8067 575 -736 151 C ATOM 128 N PHE A 52 -0.253 -1.914 -2.931 1.00105.58 N ANISOU 128 N PHE A 52 19728 11242 9145 1054 -392 270 N ATOM 129 CA PHE A 52 1.000 -1.167 -2.903 1.00106.69 C ANISOU 129 CA PHE A 52 20269 10984 9284 820 -300 250 C ATOM 130 C PHE A 52 1.070 -0.271 -1.675 1.00107.32 C ANISOU 130 C PHE A 52 20677 10795 9306 891 -215 236 C ATOM 131 O PHE A 52 2.111 -0.196 -1.012 1.00107.67 O ANISOU 131 O PHE A 52 20847 10625 9436 562 -180 166 O ATOM 132 CB PHE A 52 1.151 -0.342 -4.181 1.00106.24 C ANISOU 132 CB PHE A 52 20537 10775 9056 929 -258 342 C ATOM 133 CG PHE A 52 2.511 0.278 -4.348 1.00108.71 C ANISOU 133 CG PHE A 52 21209 10727 9367 605 -169 329 C ATOM 134 CD1 PHE A 52 2.783 1.535 -3.832 1.00109.52 C ANISOU 134 CD1 PHE A 52 21824 10459 9331 642 -65 355 C ATOM 135 CD2 PHE A 52 3.516 -0.396 -5.021 1.00111.72 C ANISOU 135 CD2 PHE A 52 21430 11151 9867 256 -182 296 C ATOM 136 CE1 PHE A 52 4.032 2.107 -3.984 1.00106.29 C ANISOU 136 CE1 PHE A 52 21737 9745 8902 284 11 348 C ATOM 137 CE2 PHE A 52 4.767 0.170 -5.176 1.00107.85 C ANISOU 137 CE2 PHE A 52 21224 10390 9364 -60 -97 301 C ATOM 138 CZ PHE A 52 5.025 1.424 -4.657 1.00109.32 C ANISOU 138 CZ PHE A 52 21898 10226 9413 -71 -7 327 C ATOM 139 N LEU A 53 -0.031 0.414 -1.356 1.00105.09 N ANISOU 139 N LEU A 53 20537 10535 8856 1327 -181 305 N ATOM 140 CA LEU A 53 -0.058 1.277 -0.180 1.00100.98 C ANISOU 140 CA LEU A 53 20377 9744 8246 1440 -88 289 C ATOM 141 C LEU A 53 0.015 0.463 1.106 1.00100.46 C ANISOU 141 C LEU A 53 20007 9807 8357 1260 -124 190 C ATOM 142 O LEU A 53 0.657 0.881 2.076 1.00104.38 O ANISOU 142 O LEU A 53 20766 10037 8858 1082 -72 126 O ATOM 143 CB LEU A 53 -1.320 2.140 -0.198 1.00101.27 C ANISOU 143 CB LEU A 53 20623 9814 8041 2021 -25 405 C ATOM 144 CG LEU A 53 -1.495 3.154 0.934 1.00106.98 C ANISOU 144 CG LEU A 53 21811 10228 8610 2238 98 403 C ATOM 145 CD1 LEU A 53 -0.450 4.256 0.839 1.00105.68 C ANISOU 145 CD1 LEU A 53 22304 9525 8324 2023 197 385 C ATOM 146 CD2 LEU A 53 -2.900 3.737 0.914 1.00102.99 C ANISOU 146 CD2 LEU A 53 21372 9885 7876 2886 157 534 C ATOM 147 N LEU A 54 -0.635 -0.702 1.130 1.00 91.50 N ANISOU 147 N LEU A 54 18338 9077 7351 1282 -216 177 N ATOM 148 CA LEU A 54 -0.653 -1.515 2.342 1.00 86.59 C ANISOU 148 CA LEU A 54 17431 8588 6883 1136 -244 95 C ATOM 149 C LEU A 54 0.719 -2.109 2.633 1.00 89.07 C ANISOU 149 C LEU A 54 17691 8771 7382 647 -268 -4 C ATOM 150 O LEU A 54 1.172 -2.103 3.783 1.00 90.31 O ANISOU 150 O LEU A 54 17912 8808 7592 497 -246 -69 O ATOM 151 CB LEU A 54 -1.700 -2.622 2.214 1.00 89.56 C ANISOU 151 CB LEU A 54 17277 9425 7328 1247 -331 115 C ATOM 152 CG LEU A 54 -3.056 -2.375 2.879 1.00 93.70 C ANISOU 152 CG LEU A 54 17692 10179 7729 1665 -301 184 C ATOM 153 CD1 LEU A 54 -3.714 -1.119 2.326 1.00 96.71 C ANISOU 153 CD1 LEU A 54 18407 10481 7856 2123 -231 306 C ATOM 154 CD2 LEU A 54 -3.966 -3.581 2.705 1.00 89.92 C ANISOU 154 CD2 LEU A 54 16655 10187 7325 1654 -401 200 C ATOM 155 N SER A 55 1.396 -2.627 1.608 1.00101.55 N ANISOU 155 N SER A 55 19148 10392 9043 412 -310 -9 N ATOM 156 CA SER A 55 2.701 -3.242 1.808 1.00 98.10 C ANISOU 156 CA SER A 55 18617 9890 8767 -8 -323 -80 C ATOM 157 C SER A 55 3.810 -2.221 2.023 1.00 99.79 C ANISOU 157 C SER A 55 19244 9761 8912 -223 -256 -87 C ATOM 158 O SER A 55 4.850 -2.571 2.591 1.00100.75 O ANISOU 158 O SER A 55 19295 9847 9138 -553 -264 -140 O ATOM 159 CB SER A 55 3.051 -4.137 0.617 1.00 95.15 C ANISOU 159 CB SER A 55 17993 9681 8477 -156 -370 -75 C ATOM 160 OG SER A 55 3.215 -3.374 -0.566 1.00115.48 O ANISOU 160 OG SER A 55 20822 12129 10925 -95 -338 -9 O ATOM 161 N VAL A 56 3.620 -0.976 1.585 1.00103.51 N ANISOU 161 N VAL A 56 20149 9989 9192 -55 -190 -27 N ATOM 162 CA VAL A 56 4.638 0.049 1.788 1.00107.99 C ANISOU 162 CA VAL A 56 21163 10206 9661 -305 -123 -34 C ATOM 163 C VAL A 56 4.450 0.792 3.105 1.00108.96 C ANISOU 163 C VAL A 56 21605 10113 9682 -243 -80 -75 C ATOM 164 O VAL A 56 5.408 1.398 3.607 1.00108.13 O ANISOU 164 O VAL A 56 21803 9759 9523 -561 -51 -111 O ATOM 165 CB VAL A 56 4.659 1.050 0.617 1.00113.71 C ANISOU 165 CB VAL A 56 22281 10717 10207 -203 -58 52 C ATOM 166 CG1 VAL A 56 3.540 2.072 0.759 1.00116.87 C ANISOU 166 CG1 VAL A 56 23063 10954 10389 256 8 110 C ATOM 167 CG2 VAL A 56 6.015 1.734 0.520 1.00113.25 C ANISOU 167 CG2 VAL A 56 22552 10380 10096 -627 -5 46 C ATOM 168 N LEU A 57 3.251 0.757 3.686 1.00118.87 N ANISOU 168 N LEU A 57 22800 11473 10893 142 -73 -67 N ATOM 169 CA LEU A 57 3.009 1.355 4.993 1.00120.42 C ANISOU 169 CA LEU A 57 23280 11487 10988 236 -23 -109 C ATOM 170 C LEU A 57 3.363 0.410 6.134 1.00118.95 C ANISOU 170 C LEU A 57 22747 11472 10977 1 -87 -197 C ATOM 171 O LEU A 57 3.932 0.847 7.142 1.00120.82 O ANISOU 171 O LEU A 57 23240 11505 11161 -196 -69 -259 O ATOM 172 CB LEU A 57 1.546 1.786 5.119 1.00118.62 C ANISOU 172 CB LEU A 57 23143 11320 10607 802 35 -42 C ATOM 173 CG LEU A 57 1.167 3.135 4.507 1.00121.81 C ANISOU 173 CG LEU A 57 24117 11423 10743 1119 142 44 C ATOM 174 CD1 LEU A 57 -0.334 3.375 4.613 1.00119.41 C ANISOU 174 CD1 LEU A 57 23780 11294 10295 1734 195 134 C ATOM 175 CD2 LEU A 57 1.945 4.273 5.161 1.00124.23 C ANISOU 175 CD2 LEU A 57 25081 11240 10880 917 229 -5 C ATOM 176 N GLY A 58 3.046 -0.880 5.993 1.00102.47 N ANISOU 176 N GLY A 58 20110 9745 9079 7 -161 -203 N ATOM 177 CA GLY A 58 3.328 -1.818 7.067 1.00 96.81 C ANISOU 177 CA GLY A 58 19082 9186 8516 -180 -211 -273 C ATOM 178 C GLY A 58 4.797 -2.196 7.141 1.00 95.36 C ANISOU 178 C GLY A 58 18822 8968 8443 -646 -254 -318 C ATOM 179 O GLY A 58 5.403 -2.163 8.214 1.00102.48 O ANISOU 179 O GLY A 58 19784 9801 9352 -855 -268 -373 O ATOM 180 N ASN A 59 5.394 -2.551 5.999 1.00 96.24 N ANISOU 180 N ASN A 59 18792 9150 8625 -804 -274 -286 N ATOM 181 CA ASN A 59 6.797 -2.961 5.998 1.00 93.99 C ANISOU 181 CA ASN A 59 18381 8897 8435 -1212 -303 -305 C ATOM 182 C ASN A 59 7.719 -1.819 6.400 1.00100.69 C ANISOU 182 C ASN A 59 19641 9471 9146 -1488 -275 -316 C ATOM 183 O ASN A 59 8.747 -2.055 7.040 1.00100.28 O ANISOU 183 O ASN A 59 19492 9470 9138 -1818 -311 -344 O ATOM 184 CB ASN A 59 7.181 -3.509 4.625 1.00 91.79 C ANISOU 184 CB ASN A 59 17900 8746 8229 -1278 -307 -258 C ATOM 185 CG ASN A 59 6.541 -4.847 4.340 1.00 92.56 C ANISOU 185 CG ASN A 59 17578 9123 8466 -1129 -349 -265 C ATOM 186 OD1 ASN A 59 6.955 -5.869 4.884 1.00 96.21 O ANISOU 186 OD1 ASN A 59 17751 9745 9058 -1257 -379 -297 O ATOM 187 ND2 ASN A 59 5.536 -4.852 3.472 1.00 96.58 N ANISOU 187 ND2 ASN A 59 18069 9697 8930 -867 -351 -231 N ATOM 188 N THR A 60 7.374 -0.581 6.039 1.00111.66 N ANISOU 188 N THR A 60 21504 10576 10347 -1368 -210 -289 N ATOM 189 CA THR A 60 8.144 0.559 6.526 1.00112.03 C ANISOU 189 CA THR A 60 22024 10316 10225 -1652 -179 -310 C ATOM 190 C THR A 60 7.928 0.767 8.019 1.00114.08 C ANISOU 190 C THR A 60 22433 10488 10424 -1644 -192 -384 C ATOM 191 O THR A 60 8.830 1.243 8.719 1.00116.33 O ANISOU 191 O THR A 60 22933 10641 10625 -2009 -212 -426 O ATOM 192 CB THR A 60 7.767 1.819 5.747 1.00103.42 C ANISOU 192 CB THR A 60 21469 8901 8924 -1493 -89 -258 C ATOM 193 OG1 THR A 60 7.943 1.582 4.345 1.00109.45 O ANISOU 193 OG1 THR A 60 22082 9764 9739 -1490 -79 -186 O ATOM 194 CG2 THR A 60 8.641 2.995 6.159 1.00104.98 C ANISOU 194 CG2 THR A 60 22212 8750 8925 -1859 -51 -281 C ATOM 195 N LEU A 61 6.750 0.400 8.525 1.00113.38 N ANISOU 195 N LEU A 61 22220 10496 10365 -1249 -183 -397 N ATOM 196 CA LEU A 61 6.478 0.542 9.951 1.00109.99 C ANISOU 196 CA LEU A 61 21920 9999 9872 -1203 -183 -464 C ATOM 197 C LEU A 61 7.253 -0.487 10.765 1.00109.26 C ANISOU 197 C LEU A 61 21418 10153 9944 -1503 -275 -511 C ATOM 198 O LEU A 61 7.826 -0.155 11.809 1.00113.62 O ANISOU 198 O LEU A 61 22156 10602 10413 -1742 -302 -569 O ATOM 199 CB LEU A 61 4.974 0.422 10.204 1.00112.27 C ANISOU 199 CB LEU A 61 22153 10369 10136 -680 -133 -444 C ATOM 200 CG LEU A 61 4.421 0.701 11.603 1.00120.98 C ANISOU 200 CG LEU A 61 23448 11385 11133 -510 -96 -496 C ATOM 201 CD1 LEU A 61 3.037 1.320 11.496 1.00119.59 C ANISOU 201 CD1 LEU A 61 23495 11143 10800 39 9 -440 C ATOM 202 CD2 LEU A 61 4.360 -0.572 12.438 1.00124.81 C ANISOU 202 CD2 LEU A 61 23424 12191 11808 -566 -165 -532 C ATOM 203 N VAL A 62 7.290 -1.739 10.300 1.00 84.26 N ANISOU 203 N VAL A 62 17722 7306 6988 -1493 -322 -484 N ATOM 204 CA VAL A 62 7.917 -2.795 11.089 1.00 82.37 C ANISOU 204 CA VAL A 62 17101 7304 6891 -1696 -394 -514 C ATOM 205 C VAL A 62 9.436 -2.660 11.089 1.00 88.37 C ANISOU 205 C VAL A 62 17857 8080 7641 -2155 -442 -510 C ATOM 206 O VAL A 62 10.094 -3.030 12.068 1.00 91.71 O ANISOU 206 O VAL A 62 18146 8617 8084 -2367 -501 -539 O ATOM 207 CB VAL A 62 7.466 -4.181 10.587 1.00 73.11 C ANISOU 207 CB VAL A 62 15430 6432 5917 -1533 -413 -486 C ATOM 208 CG1 VAL A 62 5.950 -4.283 10.613 1.00 80.27 C ANISOU 208 CG1 VAL A 62 16310 7379 6811 -1126 -375 -479 C ATOM 209 CG2 VAL A 62 7.986 -4.441 9.190 1.00 84.05 C ANISOU 209 CG2 VAL A 62 16680 7888 7367 -1629 -410 -432 C ATOM 210 N ILE A 63 10.024 -2.129 10.013 1.00129.98 N ANISOU 210 N ILE A 63 23256 13265 12865 -2320 -417 -464 N ATOM 211 CA ILE A 63 11.464 -1.903 10.019 1.00130.91 C ANISOU 211 CA ILE A 63 23363 13432 12944 -2781 -456 -444 C ATOM 212 C ILE A 63 11.827 -0.708 10.886 1.00132.62 C ANISOU 212 C ILE A 63 24061 13383 12945 -3043 -467 -496 C ATOM 213 O ILE A 63 12.979 -0.583 11.315 1.00132.72 O ANISOU 213 O ILE A 63 24034 13488 12905 -3466 -528 -494 O ATOM 214 CB ILE A 63 12.012 -1.716 8.590 1.00128.68 C ANISOU 214 CB ILE A 63 23065 13159 12667 -2900 -414 -370 C ATOM 215 CG1 ILE A 63 11.405 -0.474 7.937 1.00136.86 C ANISOU 215 CG1 ILE A 63 24622 13842 13535 -2776 -338 -361 C ATOM 216 CG2 ILE A 63 11.754 -2.958 7.749 1.00126.99 C ANISOU 216 CG2 ILE A 63 22398 13207 12645 -2677 -406 -328 C ATOM 217 CD1 ILE A 63 12.090 -0.064 6.652 1.00146.46 C ANISOU 217 CD1 ILE A 63 25918 15020 14709 -2970 -291 -286 C ATOM 218 N THR A 64 10.867 0.177 11.159 1.00107.31 N ANISOU 218 N THR A 64 21321 9860 9593 -2798 -407 -537 N ATOM 219 CA THR A 64 11.122 1.308 12.043 1.00100.95 C ANISOU 219 CA THR A 64 21053 8751 8551 -3022 -406 -600 C ATOM 220 C THR A 64 11.032 0.893 13.507 1.00103.60 C ANISOU 220 C THR A 64 21291 9184 8890 -3025 -469 -671 C ATOM 221 O THR A 64 11.949 1.160 14.291 1.00110.24 O ANISOU 221 O THR A 64 22228 10032 9628 -3434 -543 -709 O ATOM 222 CB THR A 64 10.141 2.444 11.745 1.00107.83 C ANISOU 222 CB THR A 64 22519 9220 9232 -2709 -293 -606 C ATOM 223 OG1 THR A 64 10.340 2.913 10.406 1.00 98.89 O ANISOU 223 OG1 THR A 64 21526 7979 8068 -2749 -238 -534 O ATOM 224 CG2 THR A 64 10.347 3.597 12.717 1.00113.17 C ANISOU 224 CG2 THR A 64 23831 9534 9636 -2918 -276 -682 C ATOM 225 N VAL A 65 9.941 0.223 13.888 1.00 95.71 N ANISOU 225 N VAL A 65 20086 8284 7995 -2592 -444 -683 N ATOM 226 CA VAL A 65 9.746 -0.169 15.281 1.00 92.21 C ANISOU 226 CA VAL A 65 19570 7921 7545 -2553 -486 -744 C ATOM 227 C VAL A 65 10.808 -1.153 15.750 1.00100.36 C ANISOU 227 C VAL A 65 20132 9295 8707 -2872 -599 -734 C ATOM 228 O VAL A 65 11.053 -1.268 16.955 1.00105.80 O ANISOU 228 O VAL A 65 20833 10032 9335 -2994 -658 -785 O ATOM 229 CB VAL A 65 8.330 -0.751 15.483 1.00 82.42 C ANISOU 229 CB VAL A 65 18158 6763 6395 -2029 -424 -739 C ATOM 230 CG1 VAL A 65 7.277 0.236 15.007 1.00 85.47 C ANISOU 230 CG1 VAL A 65 18981 6865 6630 -1663 -307 -725 C ATOM 231 CG2 VAL A 65 8.188 -2.083 14.762 1.00 93.40 C ANISOU 231 CG2 VAL A 65 18950 8496 8041 -1912 -449 -679 C ATOM 232 N LEU A 66 11.450 -1.869 14.827 1.00118.27 N ANISOU 232 N LEU A 66 21993 11809 11135 -2986 -625 -663 N ATOM 233 CA LEU A 66 12.542 -2.763 15.190 1.00117.60 C ANISOU 233 CA LEU A 66 21471 12065 11146 -3257 -717 -630 C ATOM 234 C LEU A 66 13.878 -2.034 15.259 1.00124.48 C ANISOU 234 C LEU A 66 22482 12947 11868 -3778 -783 -618 C ATOM 235 O LEU A 66 14.701 -2.332 16.131 1.00126.30 O ANISOU 235 O LEU A 66 22533 13394 12063 -4042 -879 -618 O ATOM 236 CB LEU A 66 12.630 -3.924 14.196 1.00109.94 C ANISOU 236 CB LEU A 66 20014 11365 10395 -3110 -697 -553 C ATOM 237 CG LEU A 66 11.494 -4.945 14.264 1.00106.32 C ANISOU 237 CG LEU A 66 19313 10992 10091 -2692 -659 -559 C ATOM 238 CD1 LEU A 66 11.622 -5.969 13.146 1.00108.92 C ANISOU 238 CD1 LEU A 66 19265 11528 10592 -2592 -633 -493 C ATOM 239 CD2 LEU A 66 11.470 -5.629 15.620 1.00107.23 C ANISOU 239 CD2 LEU A 66 19264 11249 10228 -2665 -709 -590 C ATOM 240 N ILE A 67 14.109 -1.077 14.356 1.00140.69 N ANISOU 240 N ILE A 67 24851 14788 13816 -3944 -736 -599 N ATOM 241 CA ILE A 67 15.344 -0.296 14.387 1.00144.82 C ANISOU 241 CA ILE A 67 25542 15314 14170 -4494 -793 -583 C ATOM 242 C ILE A 67 15.325 0.787 15.452 1.00148.99 C ANISOU 242 C ILE A 67 26627 15542 14441 -4728 -828 -679 C ATOM 243 O ILE A 67 16.383 1.343 15.775 1.00151.47 O ANISOU 243 O ILE A 67 27057 15905 14590 -5251 -907 -679 O ATOM 244 CB ILE A 67 15.622 0.326 13.004 1.00141.97 C ANISOU 244 CB ILE A 67 25342 14825 13776 -4615 -718 -520 C ATOM 245 CG1 ILE A 67 17.129 0.442 12.760 1.00145.54 C ANISOU 245 CG1 ILE A 67 25591 15543 14164 -5167 -780 -445 C ATOM 246 CG2 ILE A 67 14.942 1.682 12.870 1.00148.35 C ANISOU 246 CG2 ILE A 67 26867 15124 14375 -4570 -637 -577 C ATOM 247 CD1 ILE A 67 17.816 -0.887 12.535 1.00143.80 C ANISOU 247 CD1 ILE A 67 24665 15829 14142 -5127 -818 -352 C ATOM 248 N ARG A 68 14.157 1.099 16.016 1.00158.96 N ANISOU 248 N ARG A 68 28238 16513 15645 -4364 -769 -758 N ATOM 249 CA ARG A 68 14.050 2.098 17.073 1.00160.81 C ANISOU 249 CA ARG A 68 28912 16513 15677 -4443 -751 -781 C ATOM 250 C ARG A 68 14.177 1.475 18.459 1.00160.19 C ANISOU 250 C ARG A 68 28621 16638 15606 -4478 -849 -832 C ATOM 251 O ARG A 68 14.898 1.997 19.315 1.00162.61 O ANISOU 251 O ARG A 68 29041 16976 15768 -4819 -908 -819 O ATOM 252 CB ARG A 68 12.719 2.850 16.961 1.00157.35 C ANISOU 252 CB ARG A 68 28942 15685 15159 -3966 -605 -793 C ATOM 253 CG ARG A 68 12.633 3.831 15.803 1.00159.15 C ANISOU 253 CG ARG A 68 29537 15646 15288 -3953 -498 -728 C ATOM 254 CD ARG A 68 13.774 4.833 15.821 1.00167.26 C ANISOU 254 CD ARG A 68 30815 16617 16121 -4481 -512 -668 C ATOM 255 NE ARG A 68 14.044 5.361 14.489 1.00174.99 N ANISOU 255 NE ARG A 68 31941 17488 17058 -4583 -444 -602 N ATOM 256 CZ ARG A 68 15.130 6.047 14.160 1.00177.50 C ANISOU 256 CZ ARG A 68 32378 17833 17230 -5076 -456 -543 C ATOM 257 NH1 ARG A 68 16.073 6.315 15.047 1.00173.20 N ANISOU 257 NH1 ARG A 68 31820 17430 16559 -5533 -540 -538 N ATOM 258 NH2 ARG A 68 15.272 6.475 12.908 1.00176.68 N ANISOU 258 NH2 ARG A 68 32409 17629 17091 -5119 -382 -485 N ATOM 259 N ASN A 69 13.484 0.362 18.693 1.00147.73 N ANISOU 259 N ASN A 69 26750 15206 14175 -4137 -867 -886 N ATOM 260 CA ASN A 69 13.442 -0.284 20.000 1.00149.79 C ANISOU 260 CA ASN A 69 26828 15646 14440 -4095 -941 -929 C ATOM 261 C ASN A 69 14.367 -1.496 19.985 1.00148.31 C ANISOU 261 C ASN A 69 25973 15946 14431 -4245 -1041 -846 C ATOM 262 O ASN A 69 14.074 -2.501 19.329 1.00146.23 O ANISOU 262 O ASN A 69 25277 15883 14400 -3959 -998 -777 O ATOM 263 CB ASN A 69 12.015 -0.693 20.355 1.00148.11 C ANISOU 263 CB ASN A 69 26622 15341 14311 -3530 -842 -956 C ATOM 264 CG ASN A 69 11.006 0.403 20.074 1.00150.87 C ANISOU 264 CG ASN A 69 27529 15272 14521 -3248 -706 -986 C ATOM 265 OD1 ASN A 69 11.352 1.583 20.019 1.00155.50 O ANISOU 265 OD1 ASN A 69 28504 15622 14956 -3436 -666 -948 O ATOM 266 ND2 ASN A 69 9.748 0.017 19.894 1.00144.96 N ANISOU 266 ND2 ASN A 69 26705 14508 13866 -2738 -607 -979 N ATOM 267 N LYS A 70 15.484 -1.400 20.711 1.00144.28 N ANISOU 267 N LYS A 70 25396 15633 13791 -4688 -1173 -846 N ATOM 268 CA LYS A 70 16.364 -2.551 20.870 1.00143.50 C ANISOU 268 CA LYS A 70 24673 16026 13826 -4779 -1265 -754 C ATOM 269 C LYS A 70 15.743 -3.626 21.752 1.00142.69 C ANISOU 269 C LYS A 70 24307 16067 13841 -4410 -1264 -760 C ATOM 270 O LYS A 70 16.193 -4.777 21.716 1.00143.11 O ANISOU 270 O LYS A 70 23846 16483 14046 -4323 -1295 -672 O ATOM 271 CB LYS A 70 17.709 -2.112 21.451 1.00142.15 C ANISOU 271 CB LYS A 70 24483 16076 13450 -5356 -1417 -739 C ATOM 272 CG LYS A 70 18.331 -0.919 20.744 1.00150.57 C ANISOU 272 CG LYS A 70 25894 16971 14346 -5810 -1421 -742 C ATOM 273 CD LYS A 70 19.744 -0.656 21.242 1.00153.63 C ANISOU 273 CD LYS A 70 26091 17707 14574 -6376 -1562 -673 C ATOM 274 CE LYS A 70 20.331 0.597 20.611 1.00153.92 C ANISOU 274 CE LYS A 70 26420 17584 14477 -6767 -1506 -612 C ATOM 275 NZ LYS A 70 20.410 0.490 19.127 1.00154.39 N ANISOU 275 NZ LYS A 70 26380 17638 14642 -6756 -1436 -570 N ATOM 276 N ARG A 71 14.723 -3.275 22.539 1.00154.07 N ANISOU 276 N ARG A 71 26111 17228 15202 -4180 -1217 -856 N ATOM 277 CA ARG A 71 14.045 -4.261 23.373 1.00153.48 C ANISOU 277 CA ARG A 71 25813 17272 15230 -3833 -1198 -858 C ATOM 278 C ARG A 71 13.266 -5.266 22.534 1.00155.96 C ANISOU 278 C ARG A 71 25788 17663 15805 -3418 -1092 -797 C ATOM 279 O ARG A 71 13.063 -6.407 22.966 1.00155.55 O ANISOU 279 O ARG A 71 25399 17823 15881 -3211 -1089 -758 O ATOM 280 CB ARG A 71 13.108 -3.554 24.354 1.00155.94 C ANISOU 280 CB ARG A 71 26615 17265 15370 -3678 -1151 -967 C ATOM 281 CG ARG A 71 12.682 -4.397 25.544 1.00156.68 C ANISOU 281 CG ARG A 71 26537 17505 15489 -3458 -1162 -976 C ATOM 282 CD ARG A 71 13.876 -4.828 26.378 1.00160.53 C ANISOU 282 CD ARG A 71 26780 18315 15898 -3787 -1322 -946 C ATOM 283 NE ARG A 71 13.463 -5.547 27.577 1.00170.86 N ANISOU 283 NE ARG A 71 27990 19730 17198 -3580 -1329 -955 N ATOM 284 CZ ARG A 71 13.661 -5.114 28.815 1.00170.37 C ANISOU 284 CZ ARG A 71 28193 19631 16909 -3744 -1408 -1024 C ATOM 285 NH1 ARG A 71 14.267 -3.963 29.057 1.00171.05 N ANISOU 285 NH1 ARG A 71 28674 19567 16750 -4142 -1493 -1095 N ATOM 286 NH2 ARG A 71 13.239 -5.854 29.837 1.00166.61 N ANISOU 286 NH2 ARG A 71 27602 19262 16439 -3520 -1399 -1020 N ATOM 287 N MET A 72 12.826 -4.866 21.339 1.00135.14 N ANISOU 287 N MET A 72 23260 14854 13233 -3309 -1006 -787 N ATOM 288 CA MET A 72 12.035 -5.742 20.484 1.00130.92 C ANISOU 288 CA MET A 72 22445 14383 12916 -2949 -914 -738 C ATOM 289 C MET A 72 12.889 -6.669 19.630 1.00124.38 C ANISOU 289 C MET A 72 21166 13846 12246 -3034 -938 -642 C ATOM 290 O MET A 72 12.374 -7.672 19.126 1.00116.27 O ANISOU 290 O MET A 72 19865 12920 11393 -2768 -880 -602 O ATOM 291 CB MET A 72 11.130 -4.908 19.574 1.00122.56 C ANISOU 291 CB MET A 72 21702 13032 11835 -2761 -815 -762 C ATOM 292 CG MET A 72 9.958 -4.252 20.283 1.00124.14 C ANISOU 292 CG MET A 72 22284 12975 11909 -2496 -742 -832 C ATOM 293 SD MET A 72 8.497 -5.306 20.327 1.00132.88 S ANISOU 293 SD MET A 72 23098 14206 13185 -2005 -650 -806 S ATOM 294 CE MET A 72 7.253 -4.133 20.861 1.00140.25 C ANISOU 294 CE MET A 72 24548 14827 13913 -1699 -542 -864 C ATOM 295 N ARG A 73 14.177 -6.363 19.460 1.00123.86 N ANISOU 295 N ARG A 73 21028 13927 12107 -3401 -1016 -601 N ATOM 296 CA ARG A 73 15.045 -7.116 18.553 1.00118.73 C ANISOU 296 CA ARG A 73 19976 13559 11578 -3463 -1017 -496 C ATOM 297 C ARG A 73 15.444 -8.447 19.192 1.00120.96 C ANISOU 297 C ARG A 73 19846 14165 11947 -3347 -1050 -431 C ATOM 298 O ARG A 73 16.573 -8.657 19.641 1.00123.74 O ANISOU 298 O ARG A 73 19978 14808 12231 -3568 -1136 -367 O ATOM 299 CB ARG A 73 16.269 -6.290 18.180 1.00121.06 C ANISOU 299 CB ARG A 73 20318 13939 11741 -3900 -1080 -457 C ATOM 300 CG ARG A 73 15.951 -5.036 17.387 1.00127.50 C ANISOU 300 CG ARG A 73 21561 14418 12467 -4015 -1028 -503 C ATOM 301 CD ARG A 73 17.067 -4.702 16.411 1.00127.46 C ANISOU 301 CD ARG A 73 21438 14563 12429 -4343 -1036 -419 C ATOM 302 NE ARG A 73 18.303 -4.352 17.099 1.00132.06 N ANISOU 302 NE ARG A 73 21944 15383 12848 -4804 -1155 -388 N ATOM 303 CZ ARG A 73 18.616 -3.128 17.501 1.00137.11 C ANISOU 303 CZ ARG A 73 22996 15835 13265 -5201 -1212 -447 C ATOM 304 NH1 ARG A 73 17.800 -2.105 17.302 1.00134.54 N ANISOU 304 NH1 ARG A 73 23225 15048 12846 -5157 -1146 -537 N ATOM 305 NH2 ARG A 73 19.775 -2.924 18.120 1.00138.44 N ANISOU 305 NH2 ARG A 73 23032 16291 13279 -5652 -1337 -408 N ATOM 306 N THR A 74 14.480 -9.363 19.224 1.00104.55 N ANISOU 306 N THR A 74 17670 12048 10007 -2991 -978 -440 N ATOM 307 CA THR A 74 14.760 -10.730 19.630 1.00100.88 C ANISOU 307 CA THR A 74 16858 11840 9633 -2832 -976 -370 C ATOM 308 C THR A 74 15.303 -11.512 18.436 1.00104.20 C ANISOU 308 C THR A 74 16995 12428 10170 -2759 -918 -277 C ATOM 309 O THR A 74 15.385 -11.006 17.313 1.00105.63 O ANISOU 309 O THR A 74 17237 12528 10371 -2828 -882 -272 O ATOM 310 CB THR A 74 13.507 -11.387 20.206 1.00 99.48 C ANISOU 310 CB THR A 74 16726 11541 9529 -2528 -916 -416 C ATOM 311 OG1 THR A 74 13.837 -12.682 20.723 1.00104.56 O ANISOU 311 OG1 THR A 74 17094 12405 10230 -2397 -912 -346 O ATOM 312 CG2 THR A 74 12.439 -11.534 19.134 1.00 89.62 C ANISOU 312 CG2 THR A 74 15529 10121 8400 -2313 -817 -440 C ATOM 313 N VAL A 75 15.687 -12.766 18.680 1.00129.05 N ANISOU 313 N VAL A 75 19857 15799 13378 -2600 -899 -197 N ATOM 314 CA VAL A 75 16.241 -13.589 17.608 1.00127.92 C ANISOU 314 CA VAL A 75 19475 15811 13319 -2492 -826 -104 C ATOM 315 C VAL A 75 15.187 -13.851 16.538 1.00122.89 C ANISOU 315 C VAL A 75 18948 14942 12802 -2298 -727 -153 C ATOM 316 O VAL A 75 15.492 -13.883 15.340 1.00123.71 O ANISOU 316 O VAL A 75 18996 15064 12944 -2297 -674 -116 O ATOM 317 CB VAL A 75 16.810 -14.898 18.183 1.00136.90 C ANISOU 317 CB VAL A 75 20347 17202 14466 -2312 -809 -6 C ATOM 318 CG1 VAL A 75 17.343 -15.788 17.070 1.00138.79 C ANISOU 318 CG1 VAL A 75 20391 17572 14770 -2149 -709 91 C ATOM 319 CG2 VAL A 75 17.900 -14.596 19.200 1.00146.81 C ANISOU 319 CG2 VAL A 75 21456 18746 15578 -2511 -925 57 C ATOM 320 N THR A 76 13.930 -14.029 16.949 1.00104.23 N ANISOU 320 N THR A 76 16733 12385 10485 -2142 -703 -231 N ATOM 321 CA THR A 76 12.861 -14.261 15.982 1.00100.41 C ANISOU 321 CA THR A 76 16332 11727 10092 -1983 -628 -273 C ATOM 322 C THR A 76 12.567 -13.005 15.170 1.00 96.15 C ANISOU 322 C THR A 76 15991 11023 9518 -2086 -636 -319 C ATOM 323 O THR A 76 12.310 -13.086 13.963 1.00 97.04 O ANISOU 323 O THR A 76 16108 11081 9682 -2025 -586 -313 O ATOM 324 CB THR A 76 11.600 -14.742 16.700 1.00101.09 C ANISOU 324 CB THR A 76 16488 11708 10214 -1816 -603 -328 C ATOM 325 OG1 THR A 76 11.919 -15.863 17.534 1.00103.24 O ANISOU 325 OG1 THR A 76 16618 12110 10497 -1733 -591 -280 O ATOM 326 CG2 THR A 76 10.534 -15.154 15.693 1.00 94.14 C ANISOU 326 CG2 THR A 76 15634 10721 9413 -1677 -537 -356 C ATOM 327 N ASN A 77 12.607 -11.835 15.811 1.00108.44 N ANISOU 327 N ASN A 77 17749 12484 10970 -2240 -695 -363 N ATOM 328 CA ASN A 77 12.295 -10.592 15.115 1.00103.83 C ANISOU 328 CA ASN A 77 17424 11701 10324 -2317 -689 -402 C ATOM 329 C ASN A 77 13.393 -10.170 14.149 1.00105.73 C ANISOU 329 C ASN A 77 17622 12015 10537 -2528 -692 -344 C ATOM 330 O ASN A 77 13.126 -9.382 13.236 1.00108.89 O ANISOU 330 O ASN A 77 18211 12255 10909 -2552 -662 -357 O ATOM 331 CB ASN A 77 12.034 -9.474 16.126 1.00107.03 C ANISOU 331 CB ASN A 77 18130 11944 10593 -2416 -735 -469 C ATOM 332 CG ASN A 77 10.669 -9.583 16.776 1.00108.14 C ANISOU 332 CG ASN A 77 18380 11964 10743 -2160 -699 -527 C ATOM 333 OD1 ASN A 77 9.808 -10.335 16.318 1.00108.79 O ANISOU 333 OD1 ASN A 77 18334 12072 10930 -1939 -645 -519 O ATOM 334 ND2 ASN A 77 10.465 -8.833 17.853 1.00114.81 N ANISOU 334 ND2 ASN A 77 19469 12692 11460 -2202 -726 -582 N ATOM 335 N ILE A 78 14.619 -10.667 14.330 1.00 91.34 N ANISOU 335 N ILE A 78 15549 10451 8706 -2668 -720 -267 N ATOM 336 CA ILE A 78 15.687 -10.353 13.385 1.00 95.34 C ANISOU 336 CA ILE A 78 15960 11084 9181 -2861 -707 -192 C ATOM 337 C ILE A 78 15.384 -10.960 12.021 1.00 94.40 C ANISOU 337 C ILE A 78 15760 10943 9163 -2666 -613 -163 C ATOM 338 O ILE A 78 15.571 -10.314 10.982 1.00 91.63 O ANISOU 338 O ILE A 78 15509 10521 8784 -2761 -580 -145 O ATOM 339 CB ILE A 78 17.045 -10.827 13.935 1.00 95.84 C ANISOU 339 CB ILE A 78 15717 11501 9197 -3015 -754 -94 C ATOM 340 CG1 ILE A 78 17.474 -9.953 15.114 1.00 96.90 C ANISOU 340 CG1 ILE A 78 15970 11661 9185 -3309 -867 -125 C ATOM 341 CG2 ILE A 78 18.106 -10.804 12.845 1.00102.29 C ANISOU 341 CG2 ILE A 78 16347 12522 9998 -3141 -709 11 C ATOM 342 CD1 ILE A 78 18.718 -10.446 15.818 1.00109.72 C ANISOU 342 CD1 ILE A 78 17264 13685 10741 -3447 -936 -24 C ATOM 343 N PHE A 79 14.905 -12.206 11.999 1.00105.55 N ANISOU 343 N PHE A 79 17025 12402 10677 -2406 -567 -159 N ATOM 344 CA PHE A 79 14.491 -12.815 10.740 1.00104.49 C ANISOU 344 CA PHE A 79 16865 12218 10617 -2231 -485 -150 C ATOM 345 C PHE A 79 13.284 -12.096 10.154 1.00100.36 C ANISOU 345 C PHE A 79 16592 11444 10096 -2166 -481 -227 C ATOM 346 O PHE A 79 13.209 -11.886 8.938 1.00105.22 O ANISOU 346 O PHE A 79 17263 12003 10711 -2147 -439 -213 O ATOM 347 CB PHE A 79 14.171 -14.293 10.949 1.00107.22 C ANISOU 347 CB PHE A 79 17067 12631 11042 -2002 -439 -141 C ATOM 348 CG PHE A 79 15.355 -15.124 11.347 1.00111.52 C ANISOU 348 CG PHE A 79 17372 13432 11570 -1982 -417 -43 C ATOM 349 CD1 PHE A 79 16.436 -15.267 10.497 1.00108.58 C ANISOU 349 CD1 PHE A 79 16850 13237 11167 -2008 -360 52 C ATOM 350 CD2 PHE A 79 15.382 -15.769 12.573 1.00110.63 C ANISOU 350 CD2 PHE A 79 17177 13401 11455 -1910 -444 -33 C ATOM 351 CE1 PHE A 79 17.525 -16.033 10.862 1.00111.55 C ANISOU 351 CE1 PHE A 79 16984 13892 11507 -1940 -329 163 C ATOM 352 CE2 PHE A 79 16.468 -16.537 12.944 1.00116.16 C ANISOU 352 CE2 PHE A 79 17656 14360 12121 -1848 -421 74 C ATOM 353 CZ PHE A 79 17.542 -16.669 12.087 1.00117.74 C ANISOU 353 CZ PHE A 79 17692 14759 12286 -1850 -363 177 C ATOM 354 N LEU A 80 12.326 -11.717 11.004 1.00 82.15 N ANISOU 354 N LEU A 80 14433 9005 7776 -2107 -520 -296 N ATOM 355 CA LEU A 80 11.145 -11.004 10.531 1.00 78.40 C ANISOU 355 CA LEU A 80 14177 8332 7278 -1996 -512 -350 C ATOM 356 C LEU A 80 11.495 -9.641 9.951 1.00 77.58 C ANISOU 356 C LEU A 80 14312 8090 7073 -2146 -514 -342 C ATOM 357 O LEU A 80 10.725 -9.106 9.146 1.00 77.75 O ANISOU 357 O LEU A 80 14500 7973 7067 -2032 -489 -356 O ATOM 358 CB LEU A 80 10.134 -10.851 11.668 1.00 82.84 C ANISOU 358 CB LEU A 80 14837 8817 7822 -1881 -536 -409 C ATOM 359 CG LEU A 80 9.006 -11.885 11.727 1.00 79.26 C ANISOU 359 CG LEU A 80 14255 8412 7448 -1670 -512 -429 C ATOM 360 CD1 LEU A 80 9.557 -13.303 11.775 1.00 78.50 C ANISOU 360 CD1 LEU A 80 13924 8468 7435 -1671 -491 -395 C ATOM 361 CD2 LEU A 80 8.099 -11.619 12.919 1.00 75.04 C ANISOU 361 CD2 LEU A 80 13806 7830 6876 -1569 -523 -472 C ATOM 362 N LEU A 81 12.633 -9.066 10.347 1.00 79.10 N ANISOU 362 N LEU A 81 14532 8329 7194 -2409 -544 -314 N ATOM 363 CA LEU A 81 13.108 -7.849 9.698 1.00 79.11 C ANISOU 363 CA LEU A 81 14770 8202 7088 -2609 -535 -296 C ATOM 364 C LEU A 81 13.613 -8.144 8.292 1.00 89.16 C ANISOU 364 C LEU A 81 15918 9561 8397 -2620 -477 -228 C ATOM 365 O LEU A 81 13.346 -7.380 7.356 1.00 92.73 O ANISOU 365 O LEU A 81 16586 9853 8793 -2618 -442 -222 O ATOM 366 CB LEU A 81 14.205 -7.199 10.539 1.00 79.50 C ANISOU 366 CB LEU A 81 14869 8309 7029 -2949 -593 -282 C ATOM 367 CG LEU A 81 14.820 -5.916 9.976 1.00 82.15 C ANISOU 367 CG LEU A 81 15479 8508 7225 -3242 -583 -260 C ATOM 368 CD1 LEU A 81 13.916 -4.726 10.248 1.00 85.84 C ANISOU 368 CD1 LEU A 81 16426 8618 7570 -3193 -576 -334 C ATOM 369 CD2 LEU A 81 16.208 -5.682 10.553 1.00 83.82 C ANISOU 369 CD2 LEU A 81 15570 8929 7347 -3640 -644 -211 C ATOM 370 N SER A 82 14.347 -9.247 8.125 1.00 94.78 N ANISOU 370 N SER A 82 16303 10523 9186 -2607 -456 -170 N ATOM 371 CA SER A 82 14.780 -9.654 6.792 1.00 92.97 C ANISOU 371 CA SER A 82 15959 10381 8983 -2571 -383 -107 C ATOM 372 C SER A 82 13.589 -10.017 5.916 1.00 87.75 C ANISOU 372 C SER A 82 15384 9584 8373 -2310 -351 -151 C ATOM 373 O SER A 82 13.549 -9.667 4.731 1.00 94.14 O ANISOU 373 O SER A 82 16291 10329 9149 -2298 -307 -127 O ATOM 374 CB SER A 82 15.753 -10.829 6.895 1.00 93.98 C ANISOU 374 CB SER A 82 15746 10800 9162 -2547 -351 -32 C ATOM 375 OG SER A 82 16.141 -11.287 5.612 1.00 94.99 O ANISOU 375 OG SER A 82 15784 11006 9300 -2472 -262 28 O ATOM 376 N LEU A 83 12.606 -10.721 6.485 1.00 75.63 N ANISOU 376 N LEU A 83 13806 8026 6903 -2116 -375 -209 N ATOM 377 CA LEU A 83 11.394 -11.044 5.741 1.00 73.19 C ANISOU 377 CA LEU A 83 13557 7632 6620 -1907 -365 -249 C ATOM 378 C LEU A 83 10.650 -9.786 5.313 1.00 76.75 C ANISOU 378 C LEU A 83 14281 7896 6986 -1871 -378 -268 C ATOM 379 O LEU A 83 10.027 -9.766 4.245 1.00 77.76 O ANISOU 379 O LEU A 83 14467 7983 7094 -1749 -362 -265 O ATOM 380 CB LEU A 83 10.488 -11.940 6.589 1.00 73.78 C ANISOU 380 CB LEU A 83 13532 7740 6761 -1760 -391 -300 C ATOM 381 CG LEU A 83 9.106 -12.288 6.031 1.00 76.67 C ANISOU 381 CG LEU A 83 13925 8071 7137 -1582 -399 -340 C ATOM 382 CD1 LEU A 83 9.207 -13.404 5.004 1.00 79.32 C ANISOU 382 CD1 LEU A 83 14156 8479 7503 -1542 -360 -330 C ATOM 383 CD2 LEU A 83 8.152 -12.669 7.152 1.00 69.73 C ANISOU 383 CD2 LEU A 83 12994 7212 6287 -1490 -430 -383 C ATOM 384 N ALA A 84 10.713 -8.727 6.121 1.00 84.86 N ANISOU 384 N ALA A 84 15502 8801 7940 -1967 -404 -283 N ATOM 385 CA ALA A 84 10.030 -7.485 5.778 1.00 85.23 C ANISOU 385 CA ALA A 84 15870 8637 7877 -1896 -398 -292 C ATOM 386 C ALA A 84 10.807 -6.663 4.760 1.00 86.71 C ANISOU 386 C ALA A 84 16229 8736 7981 -2060 -357 -238 C ATOM 387 O ALA A 84 10.208 -5.876 4.019 1.00 86.39 O ANISOU 387 O ALA A 84 16435 8538 7853 -1945 -334 -225 O ATOM 388 CB ALA A 84 9.782 -6.657 7.038 1.00 89.72 C ANISOU 388 CB ALA A 84 16656 9066 8368 -1923 -424 -334 C ATOM 389 N VAL A 85 12.131 -6.821 4.712 1.00 87.11 N ANISOU 389 N VAL A 85 16149 8906 8042 -2318 -343 -193 N ATOM 390 CA VAL A 85 12.925 -6.105 3.718 1.00 89.39 C ANISOU 390 CA VAL A 85 16569 9147 8249 -2504 -293 -128 C ATOM 391 C VAL A 85 12.701 -6.698 2.332 1.00 86.73 C ANISOU 391 C VAL A 85 16130 8874 7948 -2341 -243 -94 C ATOM 392 O VAL A 85 12.624 -5.970 1.334 1.00 89.61 O ANISOU 392 O VAL A 85 16709 9113 8226 -2342 -202 -59 O ATOM 393 CB VAL A 85 14.413 -6.119 4.119 1.00 90.06 C ANISOU 393 CB VAL A 85 16491 9410 8318 -2841 -292 -74 C ATOM 394 CG1 VAL A 85 15.295 -5.716 2.947 1.00 83.12 C ANISOU 394 CG1 VAL A 85 15635 8572 7373 -3023 -221 14 C ATOM 395 CG2 VAL A 85 14.647 -5.193 5.303 1.00 78.64 C ANISOU 395 CG2 VAL A 85 15258 7848 6775 -3071 -348 -109 C ATOM 396 N SER A 86 12.572 -8.024 2.246 1.00 87.55 N ANISOU 396 N SER A 86 15945 9157 8162 -2199 -243 -106 N ATOM 397 CA SER A 86 12.329 -8.658 0.954 1.00 90.95 C ANISOU 397 CA SER A 86 16311 9638 8606 -2054 -200 -88 C ATOM 398 C SER A 86 10.933 -8.338 0.434 1.00 89.87 C ANISOU 398 C SER A 86 16348 9370 8427 -1831 -234 -126 C ATOM 399 O SER A 86 10.743 -8.153 -0.774 1.00 97.55 O ANISOU 399 O SER A 86 17417 10310 9339 -1763 -205 -97 O ATOM 400 CB SER A 86 12.526 -10.170 1.063 1.00 89.12 C ANISOU 400 CB SER A 86 15794 9592 8474 -1967 -185 -97 C ATOM 401 OG SER A 86 11.511 -10.766 1.850 1.00 90.23 O ANISOU 401 OG SER A 86 15881 9725 8676 -1823 -243 -168 O ATOM 402 N ASP A 87 9.941 -8.272 1.327 1.00 85.95 N ANISOU 402 N ASP A 87 15879 8830 7947 -1703 -292 -180 N ATOM 403 CA ASP A 87 8.587 -7.935 0.899 1.00 89.22 C ANISOU 403 CA ASP A 87 16416 9183 8301 -1468 -324 -196 C ATOM 404 C ASP A 87 8.510 -6.514 0.359 1.00 92.25 C ANISOU 404 C ASP A 87 17136 9369 8544 -1446 -296 -152 C ATOM 405 O ASP A 87 7.723 -6.238 -0.554 1.00 94.35 O ANISOU 405 O ASP A 87 17502 9615 8732 -1259 -302 -128 O ATOM 406 CB ASP A 87 7.607 -8.117 2.058 1.00 94.13 C ANISOU 406 CB ASP A 87 16978 9832 8957 -1333 -374 -246 C ATOM 407 CG ASP A 87 7.454 -9.569 2.469 1.00100.99 C ANISOU 407 CG ASP A 87 17552 10878 9943 -1331 -397 -285 C ATOM 408 OD1 ASP A 87 8.067 -10.441 1.818 1.00101.52 O ANISOU 408 OD1 ASP A 87 17489 11028 10055 -1404 -371 -276 O ATOM 409 OD2 ASP A 87 6.721 -9.837 3.445 1.00100.05 O ANISOU 409 OD2 ASP A 87 17357 10803 9855 -1249 -429 -320 O ATOM 410 N LEU A 88 9.311 -5.600 0.907 1.00 87.48 N ANISOU 410 N LEU A 88 16731 8620 7888 -1642 -268 -137 N ATOM 411 CA LEU A 88 9.367 -4.245 0.374 1.00 87.58 C ANISOU 411 CA LEU A 88 17129 8401 7745 -1662 -223 -91 C ATOM 412 C LEU A 88 10.216 -4.178 -0.887 1.00 94.79 C ANISOU 412 C LEU A 88 18059 9330 8625 -1809 -165 -26 C ATOM 413 O LEU A 88 9.928 -3.378 -1.785 1.00100.83 O ANISOU 413 O LEU A 88 19096 9949 9266 -1721 -128 22 O ATOM 414 CB LEU A 88 9.910 -3.287 1.435 1.00 94.90 C ANISOU 414 CB LEU A 88 18313 9145 8599 -1870 -213 -107 C ATOM 415 CG LEU A 88 9.834 -1.788 1.139 1.00 96.33 C ANISOU 415 CG LEU A 88 19001 9014 8587 -1884 -158 -71 C ATOM 416 CD1 LEU A 88 8.384 -1.342 1.016 1.00 96.67 C ANISOU 416 CD1 LEU A 88 19244 8947 8540 -1466 -156 -69 C ATOM 417 CD2 LEU A 88 10.554 -0.995 2.218 1.00 88.56 C ANISOU 417 CD2 LEU A 88 18269 7859 7521 -2182 -155 -99 C ATOM 418 N MET A 89 11.262 -5.005 -0.968 1.00 95.01 N ANISOU 418 N MET A 89 17809 9545 8747 -2007 -146 -12 N ATOM 419 CA MET A 89 12.037 -5.111 -2.199 1.00 93.46 C ANISOU 419 CA MET A 89 17580 9412 8520 -2108 -77 56 C ATOM 420 C MET A 89 11.171 -5.608 -3.349 1.00 92.31 C ANISOU 420 C MET A 89 17408 9305 8359 -1844 -82 55 C ATOM 421 O MET A 89 11.313 -5.153 -4.489 1.00 99.98 O ANISOU 421 O MET A 89 18539 10215 9234 -1837 -30 113 O ATOM 422 CB MET A 89 13.225 -6.048 -1.982 1.00 93.55 C ANISOU 422 CB MET A 89 17256 9663 8627 -2292 -47 79 C ATOM 423 CG MET A 89 14.255 -6.044 -3.093 1.00 97.03 C ANISOU 423 CG MET A 89 17654 10196 9017 -2433 49 168 C ATOM 424 SD MET A 89 15.574 -7.229 -2.762 1.00103.19 S ANISOU 424 SD MET A 89 18006 11311 9891 -2555 97 214 S ATOM 425 CE MET A 89 16.762 -6.786 -4.025 1.00113.45 C ANISOU 425 CE MET A 89 19320 12704 11082 -2748 228 341 C ATOM 426 N LEU A 90 10.261 -6.539 -3.063 1.00 96.29 N ANISOU 426 N LEU A 90 17721 9920 8943 -1646 -148 -7 N ATOM 427 CA LEU A 90 9.395 -7.093 -4.096 1.00 97.85 C ANISOU 427 CA LEU A 90 17877 10192 9111 -1438 -175 -16 C ATOM 428 C LEU A 90 8.231 -6.166 -4.428 1.00 97.58 C ANISOU 428 C LEU A 90 18078 10046 8953 -1217 -216 2 C ATOM 429 O LEU A 90 7.718 -6.202 -5.552 1.00104.64 O ANISOU 429 O LEU A 90 19019 10977 9761 -1079 -228 28 O ATOM 430 CB LEU A 90 8.889 -8.469 -3.656 1.00 90.62 C ANISOU 430 CB LEU A 90 16680 9446 8305 -1365 -230 -86 C ATOM 431 CG LEU A 90 7.956 -9.265 -4.567 1.00 92.89 C ANISOU 431 CG LEU A 90 16893 9844 8558 -1211 -279 -113 C ATOM 432 CD1 LEU A 90 8.296 -10.738 -4.488 1.00 99.51 C ANISOU 432 CD1 LEU A 90 17518 10806 9485 -1273 -265 -161 C ATOM 433 CD2 LEU A 90 6.515 -9.046 -4.148 1.00 93.19 C ANISOU 433 CD2 LEU A 90 16924 9922 8562 -1027 -372 -139 C ATOM 434 N CYS A 91 7.804 -5.333 -3.479 1.00103.71 N ANISOU 434 N CYS A 91 19012 10695 9697 -1158 -232 -5 N ATOM 435 CA CYS A 91 6.699 -4.421 -3.745 1.00105.74 C ANISOU 435 CA CYS A 91 19508 10856 9813 -887 -251 30 C ATOM 436 C CYS A 91 7.172 -3.158 -4.455 1.00116.26 C ANISOU 436 C CYS A 91 21231 11950 10992 -925 -174 106 C ATOM 437 O CYS A 91 6.535 -2.705 -5.412 1.00118.17 O ANISOU 437 O CYS A 91 21632 12166 11102 -711 -173 163 O ATOM 438 CB CYS A 91 5.987 -4.063 -2.440 1.00111.19 C ANISOU 438 CB CYS A 91 20241 11500 10506 -757 -279 -3 C ATOM 439 SG CYS A 91 4.843 -2.669 -2.574 1.00120.64 S ANISOU 439 SG CYS A 91 21818 12530 11488 -390 -259 64 S ATOM 440 N LEU A 92 8.286 -2.579 -4.005 1.00118.99 N ANISOU 440 N LEU A 92 21741 12134 11337 -1211 -110 115 N ATOM 441 CA LEU A 92 8.768 -1.335 -4.595 1.00118.69 C ANISOU 441 CA LEU A 92 22121 11841 11136 -1303 -27 188 C ATOM 442 C LEU A 92 9.433 -1.574 -5.945 1.00116.64 C ANISOU 442 C LEU A 92 21816 11651 10852 -1412 24 248 C ATOM 443 O LEU A 92 9.111 -0.903 -6.931 1.00124.05 O ANISOU 443 O LEU A 92 23022 12470 11642 -1272 62 317 O ATOM 444 CB LEU A 92 9.743 -0.645 -3.638 1.00115.77 C ANISOU 444 CB LEU A 92 21943 11295 10750 -1637 15 176 C ATOM 445 CG LEU A 92 9.143 0.122 -2.460 1.00112.84 C ANISOU 445 CG LEU A 92 21848 10721 10306 -1533 2 136 C ATOM 446 CD1 LEU A 92 10.246 0.754 -1.627 1.00115.30 C ANISOU 446 CD1 LEU A 92 22359 10871 10578 -1943 34 119 C ATOM 447 CD2 LEU A 92 8.168 1.179 -2.949 1.00112.91 C ANISOU 447 CD2 LEU A 92 22291 10494 10115 -1196 45 191 C ATOM 448 N PHE A 93 10.355 -2.530 -6.009 1.00108.66 N ANISOU 448 N PHE A 93 20479 10836 9970 -1631 36 232 N ATOM 449 CA PHE A 93 11.210 -2.711 -7.174 1.00112.13 C ANISOU 449 CA PHE A 93 20885 11343 10377 -1770 113 296 C ATOM 450 C PHE A 93 10.642 -3.677 -8.206 1.00114.32 C ANISOU 450 C PHE A 93 20971 11796 10668 -1549 83 285 C ATOM 451 O PHE A 93 11.260 -3.859 -9.260 1.00116.62 O ANISOU 451 O PHE A 93 21256 12141 10912 -1619 154 337 O ATOM 452 CB PHE A 93 12.596 -3.203 -6.737 1.00109.55 C ANISOU 452 CB PHE A 93 20310 11164 10149 -2101 163 305 C ATOM 453 CG PHE A 93 13.380 -2.200 -5.936 1.00113.10 C ANISOU 453 CG PHE A 93 20958 11469 10544 -2417 195 331 C ATOM 454 CD1 PHE A 93 12.997 -0.869 -5.888 1.00117.58 C ANISOU 454 CD1 PHE A 93 21989 11729 10957 -2421 214 354 C ATOM 455 CD2 PHE A 93 14.504 -2.594 -5.228 1.00113.94 C ANISOU 455 CD2 PHE A 93 20806 11754 10731 -2713 207 338 C ATOM 456 CE1 PHE A 93 13.721 0.049 -5.150 1.00123.33 C ANISOU 456 CE1 PHE A 93 22953 12299 11608 -2757 242 367 C ATOM 457 CE2 PHE A 93 15.231 -1.681 -4.488 1.00118.16 C ANISOU 457 CE2 PHE A 93 21518 12185 11194 -3055 220 359 C ATOM 458 CZ PHE A 93 14.840 -0.358 -4.449 1.00127.00 C ANISOU 458 CZ PHE A 93 23134 12966 12155 -3099 236 366 C ATOM 459 N CYS A 94 9.495 -4.303 -7.943 1.00107.65 N ANISOU 459 N CYS A 94 19979 11054 9870 -1306 -18 221 N ATOM 460 CA CYS A 94 9.030 -5.363 -8.831 1.00100.83 C ANISOU 460 CA CYS A 94 18921 10376 9013 -1171 -59 195 C ATOM 461 C CYS A 94 7.541 -5.274 -9.145 1.00104.83 C ANISOU 461 C CYS A 94 19467 10934 9431 -874 -162 185 C ATOM 462 O CYS A 94 7.128 -5.558 -10.274 1.00111.41 O ANISOU 462 O CYS A 94 20307 11855 10169 -761 -189 203 O ATOM 463 CB CYS A 94 9.353 -6.729 -8.224 1.00104.22 C ANISOU 463 CB CYS A 94 19012 10982 9603 -1260 -79 120 C ATOM 464 SG CYS A 94 11.112 -7.008 -7.909 1.00112.84 S ANISOU 464 SG CYS A 94 19974 12118 10782 -1556 40 155 S ATOM 465 N MET A 95 6.726 -4.897 -8.161 1.00115.96 N ANISOU 465 N MET A 95 20888 12318 10854 -742 -221 164 N ATOM 466 CA MET A 95 5.284 -4.846 -8.388 1.00116.72 C ANISOU 466 CA MET A 95 20957 12535 10855 -442 -318 173 C ATOM 467 C MET A 95 4.872 -3.858 -9.476 1.00120.12 C ANISOU 467 C MET A 95 21678 12882 11080 -238 -303 270 C ATOM 468 O MET A 95 3.966 -4.196 -10.258 1.00121.23 O ANISOU 468 O MET A 95 21721 13215 11124 -51 -387 287 O ATOM 469 CB MET A 95 4.556 -4.538 -7.073 1.00120.81 C ANISOU 469 CB MET A 95 21444 13048 11411 -315 -355 150 C ATOM 470 CG MET A 95 3.082 -4.919 -7.084 1.00122.80 C ANISOU 470 CG MET A 95 21499 13550 11608 -49 -466 149 C ATOM 471 SD MET A 95 2.213 -4.427 -5.584 1.00127.53 S ANISOU 471 SD MET A 95 22085 14152 12217 151 -478 145 S ATOM 472 CE MET A 95 3.001 -5.484 -4.371 1.00123.69 C ANISOU 472 CE MET A 95 21351 13679 11966 -166 -472 35 C ATOM 473 N PRO A 96 5.450 -2.654 -9.586 1.00110.42 N ANISOU 473 N PRO A 96 20816 11383 9757 -267 -203 340 N ATOM 474 CA PRO A 96 5.087 -1.798 -10.732 1.00105.52 C ANISOU 474 CA PRO A 96 20493 10676 8924 -61 -179 442 C ATOM 475 C PRO A 96 5.430 -2.423 -12.073 1.00105.42 C ANISOU 475 C PRO A 96 20396 10787 8872 -134 -181 455 C ATOM 476 O PRO A 96 4.569 -2.498 -12.957 1.00105.61 O ANISOU 476 O PRO A 96 20408 10960 8760 97 -254 494 O ATOM 477 CB PRO A 96 5.882 -0.508 -10.469 1.00104.18 C ANISOU 477 CB PRO A 96 20757 10151 8676 -182 -51 500 C ATOM 478 CG PRO A 96 6.953 -0.901 -9.502 1.00106.45 C ANISOU 478 CG PRO A 96 20900 10401 9145 -545 -13 427 C ATOM 479 CD PRO A 96 6.309 -1.929 -8.635 1.00109.68 C ANISOU 479 CD PRO A 96 20923 11042 9707 -472 -117 336 C ATOM 480 N PHE A 97 6.663 -2.908 -12.241 1.00101.82 N ANISOU 480 N PHE A 97 19868 10302 8517 -441 -102 428 N ATOM 481 CA PHE A 97 7.112 -3.514 -13.497 1.00 97.09 C ANISOU 481 CA PHE A 97 19217 9803 7871 -510 -75 441 C ATOM 482 C PHE A 97 6.376 -4.810 -13.847 1.00 98.11 C ANISOU 482 C PHE A 97 19044 10205 8027 -428 -193 363 C ATOM 483 O PHE A 97 6.816 -5.520 -14.759 1.00 96.35 O ANISOU 483 O PHE A 97 18769 10063 7778 -509 -167 349 O ATOM 484 CB PHE A 97 8.617 -3.770 -13.435 1.00 97.59 C ANISOU 484 CB PHE A 97 19234 9811 8034 -833 53 441 C ATOM 485 CG PHE A 97 9.440 -2.517 -13.392 1.00 94.87 C ANISOU 485 CG PHE A 97 19209 9221 7617 -991 174 529 C ATOM 486 CD1 PHE A 97 9.581 -1.729 -14.522 1.00104.25 C ANISOU 486 CD1 PHE A 97 20706 10283 8620 -947 249 629 C ATOM 487 CD2 PHE A 97 10.069 -2.125 -12.223 1.00 99.13 C ANISOU 487 CD2 PHE A 97 19761 9652 8251 -1206 212 514 C ATOM 488 CE1 PHE A 97 10.334 -0.574 -14.486 1.00108.22 C ANISOU 488 CE1 PHE A 97 21540 10541 9037 -1134 368 713 C ATOM 489 CE2 PHE A 97 10.824 -0.971 -12.182 1.00104.41 C ANISOU 489 CE2 PHE A 97 20753 10090 8828 -1410 318 591 C ATOM 490 CZ PHE A 97 10.956 -0.195 -13.314 1.00108.76 C ANISOU 490 CZ PHE A 97 21626 10502 9196 -1383 400 691 C ATOM 491 N ASN A 98 5.292 -5.130 -13.147 1.00110.01 N ANISOU 491 N ASN A 98 20372 11855 9572 -286 -315 315 N ATOM 492 CA ASN A 98 4.439 -6.266 -13.459 1.00115.32 C ANISOU 492 CA ASN A 98 20787 12795 10236 -237 -443 247 C ATOM 493 C ASN A 98 3.029 -5.863 -13.860 1.00112.61 C ANISOU 493 C ASN A 98 20441 12626 9720 49 -570 300 C ATOM 494 O ASN A 98 2.386 -6.593 -14.619 1.00111.70 O ANISOU 494 O ASN A 98 20191 12738 9511 72 -677 274 O ATOM 495 CB ASN A 98 4.368 -7.224 -12.256 1.00115.13 C ANISOU 495 CB ASN A 98 20481 12862 10403 -364 -481 147 C ATOM 496 CG ASN A 98 3.574 -8.483 -12.551 1.00120.19 C ANISOU 496 CG ASN A 98 20888 13753 11026 -388 -602 70 C ATOM 497 OD1 ASN A 98 2.352 -8.510 -12.403 1.00125.48 O ANISOU 497 OD1 ASN A 98 21428 14620 11627 -250 -726 74 O ATOM 498 ND2 ASN A 98 4.269 -9.536 -12.968 1.00121.98 N ANISOU 498 ND2 ASN A 98 21069 13981 11296 -569 -559 4 N ATOM 499 N LEU A 99 2.538 -4.718 -13.384 1.00102.49 N ANISOU 499 N LEU A 99 19318 11254 8371 272 -558 379 N ATOM 500 CA LEU A 99 1.184 -4.268 -13.692 1.00104.90 C ANISOU 500 CA LEU A 99 19601 11763 8493 606 -667 456 C ATOM 501 C LEU A 99 1.145 -3.384 -14.937 1.00107.01 C ANISOU 501 C LEU A 99 20172 11955 8533 799 -639 572 C ATOM 502 O LEU A 99 0.413 -3.674 -15.888 1.00109.79 O ANISOU 502 O LEU A 99 20433 12558 8725 926 -750 605 O ATOM 503 CB LEU A 99 0.592 -3.520 -12.492 1.00105.82 C ANISOU 503 CB LEU A 99 19745 11833 8627 816 -653 491 C ATOM 504 CG LEU A 99 -0.602 -2.621 -12.829 1.00108.14 C ANISOU 504 CG LEU A 99 20138 12264 8688 1251 -704 621 C ATOM 505 CD1 LEU A 99 -1.860 -3.451 -13.040 1.00114.29 C ANISOU 505 CD1 LEU A 99 20510 13516 9399 1360 -879 618 C ATOM 506 CD2 LEU A 99 -0.816 -1.567 -11.755 1.00104.42 C ANISOU 506 CD2 LEU A 99 19883 11594 8199 1478 -617 673 C ATOM 507 N ILE A 100 1.922 -2.304 -14.942 1.00 98.84 N ANISOU 507 N ILE A 100 19511 10579 7463 804 -495 639 N ATOM 508 CA ILE A 100 1.873 -1.338 -16.038 1.00 94.94 C ANISOU 508 CA ILE A 100 19366 9969 6736 1007 -448 766 C ATOM 509 C ILE A 100 2.416 -1.938 -17.337 1.00 99.64 C ANISOU 509 C ILE A 100 19954 10629 7277 843 -448 754 C ATOM 510 O ILE A 100 1.945 -1.543 -18.414 1.00105.87 O ANISOU 510 O ILE A 100 20891 11490 7844 1057 -484 846 O ATOM 511 CB ILE A 100 2.574 -0.017 -15.651 1.00100.59 C ANISOU 511 CB ILE A 100 20537 10270 7414 1010 -282 838 C ATOM 512 CG1 ILE A 100 2.660 0.947 -16.840 1.00114.19 C ANISOU 512 CG1 ILE A 100 22669 11828 8889 1180 -209 973 C ATOM 513 CG2 ILE A 100 3.939 -0.237 -15.016 1.00102.15 C ANISOU 513 CG2 ILE A 100 20742 10255 7816 590 -171 758 C ATOM 514 CD1 ILE A 100 3.129 2.337 -16.461 1.00116.80 C ANISOU 514 CD1 ILE A 100 23517 11736 9127 1216 -51 1056 C ATOM 515 N PRO A 101 3.357 -2.898 -17.329 1.00 85.33 N ANISOU 515 N PRO A 101 17982 8809 5630 505 -407 652 N ATOM 516 CA PRO A 101 3.629 -3.602 -18.594 1.00 85.59 C ANISOU 516 CA PRO A 101 17989 8956 5574 414 -423 635 C ATOM 517 C PRO A 101 2.448 -4.425 -19.074 1.00 86.10 C ANISOU 517 C PRO A 101 17804 9375 5535 532 -614 595 C ATOM 518 O PRO A 101 2.207 -4.513 -20.285 1.00 87.62 O ANISOU 518 O PRO A 101 18079 9678 5535 606 -664 632 O ATOM 519 CB PRO A 101 4.838 -4.480 -18.247 1.00 83.44 C ANISOU 519 CB PRO A 101 17585 8612 5507 73 -325 538 C ATOM 520 CG PRO A 101 5.522 -3.722 -17.185 1.00 82.87 C ANISOU 520 CG PRO A 101 17620 8303 5565 -27 -213 561 C ATOM 521 CD PRO A 101 4.376 -3.267 -16.329 1.00 83.19 C ANISOU 521 CD PRO A 101 17615 8398 5595 207 -315 571 C ATOM 522 N ASN A 102 1.699 -5.033 -18.152 1.00100.90 N ANISOU 522 N ASN A 102 19375 11445 7516 530 -727 524 N ATOM 523 CA ASN A 102 0.528 -5.808 -18.547 1.00103.77 C ANISOU 523 CA ASN A 102 19481 12183 7765 591 -919 491 C ATOM 524 C ASN A 102 -0.595 -4.902 -19.032 1.00103.51 C ANISOU 524 C ASN A 102 19503 12337 7489 961 -1017 628 C ATOM 525 O ASN A 102 -1.280 -5.222 -20.011 1.00101.93 O ANISOU 525 O ASN A 102 19228 12411 7088 1027 -1152 651 O ATOM 526 CB ASN A 102 0.050 -6.674 -17.382 1.00106.63 C ANISOU 526 CB ASN A 102 19508 12707 8300 465 -998 391 C ATOM 527 CG ASN A 102 0.786 -7.994 -17.297 1.00113.00 C ANISOU 527 CG ASN A 102 20209 13470 9256 125 -968 250 C ATOM 528 OD1 ASN A 102 0.262 -9.036 -17.691 1.00114.46 O ANISOU 528 OD1 ASN A 102 20235 13877 9376 -5 -1087 173 O ATOM 529 ND2 ASN A 102 2.007 -7.959 -16.775 1.00111.51 N ANISOU 529 ND2 ASN A 102 20120 13002 9246 -22 -806 221 N ATOM 530 N LEU A 103 -0.801 -3.767 -18.359 1.00 97.02 N ANISOU 530 N LEU A 103 18828 11377 6660 1216 -949 726 N ATOM 531 CA LEU A 103 -1.851 -2.842 -18.771 1.00 94.88 C ANISOU 531 CA LEU A 103 18637 11274 6138 1638 -1017 878 C ATOM 532 C LEU A 103 -1.556 -2.227 -20.132 1.00 94.58 C ANISOU 532 C LEU A 103 18928 11130 5878 1759 -977 978 C ATOM 533 O LEU A 103 -2.486 -1.914 -20.883 1.00 97.23 O ANISOU 533 O LEU A 103 19246 11734 5963 2056 -1090 1087 O ATOM 534 CB LEU A 103 -2.027 -1.743 -17.724 1.00 98.68 C ANISOU 534 CB LEU A 103 19290 11559 6646 1901 -917 957 C ATOM 535 CG LEU A 103 -2.877 -2.086 -16.500 1.00 93.92 C ANISOU 535 CG LEU A 103 18346 11194 6146 1978 -992 922 C ATOM 536 CD1 LEU A 103 -2.902 -0.916 -15.533 1.00102.69 C ANISOU 536 CD1 LEU A 103 19726 12035 7255 2245 -860 997 C ATOM 537 CD2 LEU A 103 -4.287 -2.474 -16.916 1.00103.37 C ANISOU 537 CD2 LEU A 103 19187 12931 7156 2199 -1187 985 C ATOM 538 N LEU A 104 -0.278 -2.047 -20.463 1.00 99.05 N ANISOU 538 N LEU A 104 19779 11337 6518 1539 -816 954 N ATOM 539 CA LEU A 104 0.125 -1.510 -21.755 1.00 97.46 C ANISOU 539 CA LEU A 104 19905 11011 6114 1610 -754 1047 C ATOM 540 C LEU A 104 0.260 -2.579 -22.830 1.00 95.30 C ANISOU 540 C LEU A 104 19495 10938 5775 1409 -839 971 C ATOM 541 O LEU A 104 0.345 -2.233 -24.013 1.00105.87 O ANISOU 541 O LEU A 104 21061 12265 6900 1510 -827 1051 O ATOM 542 CB LEU A 104 1.458 -0.763 -21.625 1.00 94.66 C ANISOU 542 CB LEU A 104 19926 10195 5845 1444 -526 1073 C ATOM 543 CG LEU A 104 1.442 0.568 -20.872 1.00 95.85 C ANISOU 543 CG LEU A 104 20403 10049 5967 1647 -411 1173 C ATOM 544 CD1 LEU A 104 2.811 1.227 -20.930 1.00 97.60 C ANISOU 544 CD1 LEU A 104 21001 9848 6236 1392 -200 1198 C ATOM 545 CD2 LEU A 104 0.377 1.488 -21.444 1.00 99.17 C ANISOU 545 CD2 LEU A 104 21029 10561 6091 2131 -465 1335 C ATOM 546 N LYS A 105 0.282 -3.858 -22.447 1.00114.41 N ANISOU 546 N LYS A 105 21592 13522 8357 1134 -917 819 N ATOM 547 CA LYS A 105 0.526 -4.965 -23.374 1.00113.88 C ANISOU 547 CA LYS A 105 21455 13583 8232 906 -973 723 C ATOM 548 C LYS A 105 1.849 -4.791 -24.114 1.00113.12 C ANISOU 548 C LYS A 105 21662 13186 8132 767 -780 736 C ATOM 549 O LYS A 105 1.997 -5.225 -25.259 1.00118.55 O ANISOU 549 O LYS A 105 22443 13943 8659 716 -798 723 O ATOM 550 CB LYS A 105 -0.630 -5.133 -24.365 1.00116.50 C ANISOU 550 CB LYS A 105 21699 14289 8276 1075 -1179 768 C ATOM 551 CG LYS A 105 -1.972 -5.404 -23.705 1.00118.38 C ANISOU 551 CG LYS A 105 21574 14914 8492 1184 -1378 766 C ATOM 552 CD LYS A 105 -2.331 -6.879 -23.764 1.00120.62 C ANISOU 552 CD LYS A 105 21572 15463 8795 865 -1529 611 C ATOM 553 CE LYS A 105 -3.120 -7.304 -22.535 1.00125.57 C ANISOU 553 CE LYS A 105 21834 16314 9564 819 -1628 565 C ATOM 554 NZ LYS A 105 -4.550 -6.899 -22.619 1.00132.75 N ANISOU 554 NZ LYS A 105 22502 17677 10259 1095 -1818 684 N ATOM 555 N ASP A 106 2.818 -4.155 -23.458 1.00105.55 N ANISOU 555 N ASP A 106 20856 11912 7338 691 -594 766 N ATOM 556 CA ASP A 106 4.115 -3.872 -24.054 1.00107.20 C ANISOU 556 CA ASP A 106 21325 11861 7545 544 -393 804 C ATOM 557 C ASP A 106 5.084 -3.510 -22.938 1.00104.21 C ANISOU 557 C ASP A 106 20962 11231 7402 363 -236 795 C ATOM 558 O ASP A 106 4.718 -2.797 -22.001 1.00104.27 O ANISOU 558 O ASP A 106 20992 11153 7474 465 -247 829 O ATOM 559 CB ASP A 106 4.019 -2.732 -25.078 1.00110.75 C ANISOU 559 CB ASP A 106 22136 12207 7737 767 -343 962 C ATOM 560 CG ASP A 106 5.370 -2.342 -25.654 1.00114.14 C ANISOU 560 CG ASP A 106 22839 12372 8156 593 -119 1020 C ATOM 561 OD1 ASP A 106 6.291 -3.185 -25.661 1.00114.83 O ANISOU 561 OD1 ASP A 106 22804 12453 8374 335 -27 936 O ATOM 562 OD2 ASP A 106 5.509 -1.185 -26.104 1.00118.49 O ANISOU 562 OD2 ASP A 106 23737 12732 8553 722 -24 1160 O ATOM 563 N PHE A 107 6.315 -4.012 -23.044 1.00 92.48 N ANISOU 563 N PHE A 107 19465 9649 6026 104 -88 755 N ATOM 564 CA PHE A 107 7.358 -3.722 -22.060 1.00 89.90 C ANISOU 564 CA PHE A 107 19123 9133 5901 -109 59 756 C ATOM 565 C PHE A 107 8.169 -2.531 -22.564 1.00 98.64 C ANISOU 565 C PHE A 107 20582 9999 6898 -158 232 893 C ATOM 566 O PHE A 107 9.225 -2.667 -23.187 1.00 97.70 O ANISOU 566 O PHE A 107 20524 9839 6758 -330 383 928 O ATOM 567 CB PHE A 107 8.228 -4.950 -21.823 1.00 88.62 C ANISOU 567 CB PHE A 107 18714 9052 5904 -342 124 654 C ATOM 568 CG PHE A 107 8.905 -4.965 -20.482 1.00 96.50 C ANISOU 568 CG PHE A 107 19555 9975 7136 -527 189 621 C ATOM 569 CD1 PHE A 107 8.180 -5.220 -19.330 1.00 95.07 C ANISOU 569 CD1 PHE A 107 19179 9852 7092 -487 65 545 C ATOM 570 CD2 PHE A 107 10.266 -4.728 -20.373 1.00 99.63 C ANISOU 570 CD2 PHE A 107 19981 10273 7599 -748 372 675 C ATOM 571 CE1 PHE A 107 8.797 -5.234 -18.094 1.00 95.04 C ANISOU 571 CE1 PHE A 107 19041 9785 7286 -654 117 515 C ATOM 572 CE2 PHE A 107 10.889 -4.743 -19.139 1.00 94.84 C ANISOU 572 CE2 PHE A 107 19214 9634 7185 -930 414 650 C ATOM 573 CZ PHE A 107 10.154 -4.996 -17.999 1.00 95.85 C ANISOU 573 CZ PHE A 107 19175 9796 7447 -878 284 566 C ATOM 574 N ILE A 108 7.651 -1.332 -22.280 1.00103.27 N ANISOU 574 N ILE A 108 21421 10421 7396 4 221 981 N ATOM 575 CA ILE A 108 8.282 -0.108 -22.766 1.00102.69 C ANISOU 575 CA ILE A 108 21758 10079 7179 -39 381 1119 C ATOM 576 C ILE A 108 9.635 0.112 -22.100 1.00103.08 C ANISOU 576 C ILE A 108 21813 9971 7380 -410 548 1125 C ATOM 577 O ILE A 108 10.517 0.767 -22.670 1.00109.36 O ANISOU 577 O ILE A 108 22864 10610 8076 -578 711 1227 O ATOM 578 CB ILE A 108 7.339 1.094 -22.552 1.00100.94 C ANISOU 578 CB ILE A 108 21854 9695 6805 259 335 1211 C ATOM 579 CG1 ILE A 108 7.926 2.366 -23.172 1.00115.02 C ANISOU 579 CG1 ILE A 108 24142 11165 8397 225 507 1361 C ATOM 580 CG2 ILE A 108 7.054 1.299 -21.070 1.00104.63 C ANISOU 580 CG2 ILE A 108 22229 10090 7435 249 292 1151 C ATOM 581 CD1 ILE A 108 8.113 2.292 -24.673 1.00115.41 C ANISOU 581 CD1 ILE A 108 24330 11274 8248 281 556 1439 C ATOM 582 N PHE A 109 9.831 -0.434 -20.904 1.00 99.05 N ANISOU 582 N PHE A 109 21014 9525 7096 -558 510 1025 N ATOM 583 CA PHE A 109 11.099 -0.278 -20.213 1.00100.30 C ANISOU 583 CA PHE A 109 21125 9596 7387 -918 645 1033 C ATOM 584 C PHE A 109 12.194 -1.078 -20.920 1.00105.32 C ANISOU 584 C PHE A 109 21572 10395 8051 -1114 765 1043 C ATOM 585 O PHE A 109 11.931 -1.945 -21.759 1.00109.22 O ANISOU 585 O PHE A 109 21945 11058 8496 -973 729 1006 O ATOM 586 CB PHE A 109 10.961 -0.704 -18.753 1.00101.79 C ANISOU 586 CB PHE A 109 21044 9838 7793 -991 560 926 C ATOM 587 CG PHE A 109 9.770 -0.106 -18.059 1.00100.18 C ANISOU 587 CG PHE A 109 20976 9529 7559 -740 441 909 C ATOM 588 CD1 PHE A 109 9.838 1.162 -17.508 1.00100.77 C ANISOU 588 CD1 PHE A 109 21414 9314 7559 -781 502 972 C ATOM 589 CD2 PHE A 109 8.582 -0.811 -17.961 1.00101.88 C ANISOU 589 CD2 PHE A 109 20969 9942 7799 -466 276 835 C ATOM 590 CE1 PHE A 109 8.745 1.717 -16.871 1.00105.57 C ANISOU 590 CE1 PHE A 109 22169 9826 8117 -500 415 965 C ATOM 591 CE2 PHE A 109 7.484 -0.261 -17.326 1.00100.40 C ANISOU 591 CE2 PHE A 109 20873 9706 7570 -207 182 837 C ATOM 592 CZ PHE A 109 7.566 1.004 -16.780 1.00103.19 C ANISOU 592 CZ PHE A 109 21595 9765 7848 -196 258 904 C ATOM 593 N GLY A 110 13.439 -0.772 -20.569 1.00119.38 N ANISOU 593 N GLY A 110 23333 12135 9890 -1443 912 1097 N ATOM 594 CA GLY A 110 14.582 -1.317 -21.269 1.00123.23 C ANISOU 594 CA GLY A 110 23670 12784 10367 -1617 1065 1148 C ATOM 595 C GLY A 110 14.764 -2.810 -21.055 1.00116.91 C ANISOU 595 C GLY A 110 22455 12248 9716 -1570 1033 1044 C ATOM 596 O GLY A 110 14.020 -3.479 -20.337 1.00121.41 O ANISOU 596 O GLY A 110 22841 12879 10411 -1441 886 926 O ATOM 597 N SER A 111 15.792 -3.342 -21.719 1.00109.09 N ANISOU 597 N SER A 111 21338 11418 8695 -1669 1190 1098 N ATOM 598 CA SER A 111 16.139 -4.749 -21.569 1.00109.24 C ANISOU 598 CA SER A 111 21017 11667 8824 -1612 1205 1020 C ATOM 599 C SER A 111 16.944 -5.018 -20.306 1.00108.90 C ANISOU 599 C SER A 111 20665 11743 8970 -1817 1234 1012 C ATOM 600 O SER A 111 16.951 -6.155 -19.823 1.00114.09 O ANISOU 600 O SER A 111 21058 12545 9746 -1728 1199 925 O ATOM 601 CB SER A 111 16.923 -5.233 -22.790 1.00115.13 C ANISOU 601 CB SER A 111 21764 12546 9434 -1582 1382 1092 C ATOM 602 OG SER A 111 17.321 -6.584 -22.637 1.00118.14 O ANISOU 602 OG SER A 111 21866 13125 9898 -1498 1425 1025 O ATOM 603 N ALA A 112 17.618 -4.001 -19.764 1.00112.38 N ANISOU 603 N ALA A 112 21154 12123 9422 -2099 1296 1102 N ATOM 604 CA ALA A 112 18.389 -4.181 -18.541 1.00109.51 C ANISOU 604 CA ALA A 112 20495 11899 9214 -2321 1306 1101 C ATOM 605 C ALA A 112 17.504 -4.278 -17.306 1.00107.54 C ANISOU 605 C ALA A 112 20197 11551 9113 -2253 1119 976 C ATOM 606 O ALA A 112 17.930 -4.854 -16.300 1.00111.92 O ANISOU 606 O ALA A 112 20457 12257 9812 -2335 1097 939 O ATOM 607 CB ALA A 112 19.391 -3.038 -18.377 1.00110.44 C ANISOU 607 CB ALA A 112 20700 11997 9266 -2702 1420 1237 C ATOM 608 N VAL A 113 16.292 -3.729 -17.354 1.00 94.28 N ANISOU 608 N VAL A 113 18791 9645 7386 -2088 992 921 N ATOM 609 CA VAL A 113 15.385 -3.834 -16.217 1.00 94.64 C ANISOU 609 CA VAL A 113 18783 9619 7555 -1993 827 810 C ATOM 610 C VAL A 113 14.550 -5.111 -16.277 1.00 98.86 C ANISOU 610 C VAL A 113 19125 10275 8161 -1726 721 693 C ATOM 611 O VAL A 113 14.096 -5.598 -15.237 1.00103.02 O ANISOU 611 O VAL A 113 19480 10837 8826 -1687 615 603 O ATOM 612 CB VAL A 113 14.487 -2.590 -16.123 1.00 94.63 C ANISOU 612 CB VAL A 113 19160 9341 7455 -1922 755 824 C ATOM 613 CG1 VAL A 113 15.335 -1.332 -16.008 1.00 94.90 C ANISOU 613 CG1 VAL A 113 19449 9210 7398 -2233 867 932 C ATOM 614 CG2 VAL A 113 13.575 -2.508 -17.324 1.00103.59 C ANISOU 614 CG2 VAL A 113 20508 10417 8434 -1639 719 837 C ATOM 615 N CYS A 114 14.326 -5.661 -17.475 1.00 99.63 N ANISOU 615 N CYS A 114 19272 10431 8150 -1564 746 692 N ATOM 616 CA CYS A 114 13.752 -6.998 -17.577 1.00 93.12 C ANISOU 616 CA CYS A 114 18277 9732 7371 -1386 668 581 C ATOM 617 C CYS A 114 14.653 -8.032 -16.919 1.00 89.45 C ANISOU 617 C CYS A 114 17513 9430 7044 -1468 745 556 C ATOM 618 O CYS A 114 14.164 -9.030 -16.376 1.00 95.28 O ANISOU 618 O CYS A 114 18101 10227 7874 -1376 661 452 O ATOM 619 CB CYS A 114 13.504 -7.352 -19.045 1.00 99.15 C ANISOU 619 CB CYS A 114 19193 10522 7958 -1238 699 590 C ATOM 620 SG CYS A 114 13.084 -9.088 -19.384 1.00 97.36 S ANISOU 620 SG CYS A 114 18832 10431 7731 -1090 649 458 S ATOM 621 N LYS A 115 15.967 -7.806 -16.946 1.00 80.56 N ANISOU 621 N LYS A 115 16296 8396 5918 -1639 907 661 N ATOM 622 CA LYS A 115 16.900 -8.691 -16.262 1.00 87.89 C ANISOU 622 CA LYS A 115 16918 9518 6958 -1690 988 667 C ATOM 623 C LYS A 115 17.002 -8.369 -14.777 1.00 89.97 C ANISOU 623 C LYS A 115 17023 9787 7373 -1846 908 648 C ATOM 624 O LYS A 115 17.307 -9.258 -13.975 1.00 92.65 O ANISOU 624 O LYS A 115 17117 10260 7825 -1818 905 612 O ATOM 625 CB LYS A 115 18.283 -8.596 -16.909 1.00 89.96 C ANISOU 625 CB LYS A 115 17095 9951 7136 -1799 1198 809 C ATOM 626 CG LYS A 115 18.294 -8.851 -18.407 1.00 90.43 C ANISOU 626 CG LYS A 115 17330 10006 7022 -1649 1303 840 C ATOM 627 CD LYS A 115 19.683 -8.641 -18.988 1.00 85.82 C ANISOU 627 CD LYS A 115 16644 9615 6347 -1768 1527 1001 C ATOM 628 CE LYS A 115 19.743 -9.050 -20.450 1.00 92.18 C ANISOU 628 CE LYS A 115 17619 10432 6972 -1585 1651 1027 C ATOM 629 NZ LYS A 115 19.585 -10.519 -20.626 1.00 93.52 N ANISOU 629 NZ LYS A 115 17730 10666 7137 -1320 1673 933 N ATOM 630 N THR A 116 16.747 -7.116 -14.395 1.00123.80 N ANISOU 630 N THR A 116 21480 13913 11645 -1998 848 674 N ATOM 631 CA THR A 116 16.908 -6.707 -13.003 1.00123.66 C ANISOU 631 CA THR A 116 21361 13884 11741 -2174 780 657 C ATOM 632 C THR A 116 15.689 -7.076 -12.165 1.00123.03 C ANISOU 632 C THR A 116 21273 13710 11762 -2008 613 527 C ATOM 633 O THR A 116 15.829 -7.599 -11.053 1.00126.22 O ANISOU 633 O THR A 116 21463 14202 12293 -2042 567 481 O ATOM 634 CB THR A 116 17.170 -5.201 -12.926 1.00128.77 C ANISOU 634 CB THR A 116 22260 14365 12301 -2422 800 735 C ATOM 635 OG1 THR A 116 18.327 -4.876 -13.706 1.00132.03 O ANISOU 635 OG1 THR A 116 22660 14895 12611 -2616 963 867 O ATOM 636 CG2 THR A 116 17.400 -4.774 -11.484 1.00129.02 C ANISOU 636 CG2 THR A 116 22218 14380 12423 -2634 731 711 C ATOM 637 N THR A 117 14.486 -6.805 -12.677 1.00 97.61 N ANISOU 637 N THR A 117 18272 10339 8475 -1822 523 478 N ATOM 638 CA THR A 117 13.275 -7.108 -11.921 1.00 93.14 C ANISOU 638 CA THR A 117 17675 9727 7986 -1667 370 372 C ATOM 639 C THR A 117 13.126 -8.608 -11.700 1.00 97.92 C ANISOU 639 C THR A 117 18033 10486 8685 -1564 343 288 C ATOM 640 O THR A 117 12.865 -9.058 -10.579 1.00102.34 O ANISOU 640 O THR A 117 18437 11081 9367 -1566 273 225 O ATOM 641 CB THR A 117 12.047 -6.546 -12.638 1.00 87.72 C ANISOU 641 CB THR A 117 17233 8919 7176 -1470 286 362 C ATOM 642 OG1 THR A 117 11.963 -7.107 -13.953 1.00 99.81 O ANISOU 642 OG1 THR A 117 18801 10519 8602 -1361 318 369 O ATOM 643 CG2 THR A 117 12.132 -5.031 -12.735 1.00 97.64 C ANISOU 643 CG2 THR A 117 18800 9973 8324 -1541 322 446 C ATOM 644 N THR A 118 13.294 -9.401 -12.762 1.00 88.51 N ANISOU 644 N THR A 118 16838 9370 7421 -1475 405 287 N ATOM 645 CA THR A 118 13.206 -10.850 -12.618 1.00 93.02 C ANISOU 645 CA THR A 118 17250 10044 8048 -1384 401 209 C ATOM 646 C THR A 118 14.277 -11.384 -11.675 1.00 93.11 C ANISOU 646 C THR A 118 17028 10173 8177 -1470 485 236 C ATOM 647 O THR A 118 14.064 -12.400 -11.004 1.00 90.25 O ANISOU 647 O THR A 118 16538 9856 7897 -1406 452 166 O ATOM 648 CB THR A 118 13.319 -11.528 -13.984 1.00 86.99 C ANISOU 648 CB THR A 118 16591 9313 7149 -1280 477 208 C ATOM 649 OG1 THR A 118 14.484 -11.047 -14.664 1.00 95.04 O ANISOU 649 OG1 THR A 118 17640 10374 8095 -1350 640 325 O ATOM 650 CG2 THR A 118 12.087 -11.232 -14.827 1.00 87.62 C ANISOU 650 CG2 THR A 118 16866 9322 7104 -1179 357 165 C ATOM 651 N TYR A 119 15.430 -10.714 -11.608 1.00 82.84 N ANISOU 651 N TYR A 119 15666 8939 6869 -1622 592 345 N ATOM 652 CA TYR A 119 16.455 -11.098 -10.645 1.00 78.78 C ANISOU 652 CA TYR A 119 14893 8590 6448 -1714 653 390 C ATOM 653 C TYR A 119 15.990 -10.841 -9.217 1.00 88.56 C ANISOU 653 C TYR A 119 16059 9781 7810 -1790 524 332 C ATOM 654 O TYR A 119 16.193 -11.679 -8.331 1.00 90.78 O ANISOU 654 O TYR A 119 16148 10162 8183 -1751 514 304 O ATOM 655 CB TYR A 119 17.749 -10.339 -10.934 1.00 80.56 C ANISOU 655 CB TYR A 119 15054 8944 6613 -1909 783 532 C ATOM 656 CG TYR A 119 18.968 -10.874 -10.218 1.00 79.44 C ANISOU 656 CG TYR A 119 14593 9069 6523 -1973 871 612 C ATOM 657 CD1 TYR A 119 19.035 -12.198 -9.804 1.00 76.54 C ANISOU 657 CD1 TYR A 119 14061 8807 6213 -1773 893 574 C ATOM 658 CD2 TYR A 119 20.056 -10.052 -9.960 1.00 84.23 C ANISOU 658 CD2 TYR A 119 15070 9836 7098 -2241 933 735 C ATOM 659 CE1 TYR A 119 20.153 -12.686 -9.152 1.00 81.58 C ANISOU 659 CE1 TYR A 119 14401 9718 6878 -1785 977 666 C ATOM 660 CE2 TYR A 119 21.176 -10.529 -9.309 1.00 80.78 C ANISOU 660 CE2 TYR A 119 14297 9708 6687 -2295 1002 825 C ATOM 661 CZ TYR A 119 21.220 -11.845 -8.907 1.00 80.60 C ANISOU 661 CZ TYR A 119 14102 9801 6723 -2040 1026 795 C ATOM 662 OH TYR A 119 22.338 -12.318 -8.259 1.00 82.57 O ANISOU 662 OH TYR A 119 14009 10384 6978 -2050 1098 904 O ATOM 663 N PHE A 120 15.358 -9.690 -8.977 1.00120.17 N ANISOU 663 N PHE A 120 20240 13620 11798 -1876 434 317 N ATOM 664 CA PHE A 120 14.893 -9.361 -7.636 1.00121.08 C ANISOU 664 CA PHE A 120 20326 13673 12005 -1934 323 262 C ATOM 665 C PHE A 120 13.601 -10.087 -7.285 1.00117.55 C ANISOU 665 C PHE A 120 19872 13176 11617 -1740 210 149 C ATOM 666 O PHE A 120 13.356 -10.368 -6.106 1.00120.41 O ANISOU 666 O PHE A 120 20120 13556 12076 -1747 145 100 O ATOM 667 CB PHE A 120 14.701 -7.848 -7.499 1.00122.09 C ANISOU 667 CB PHE A 120 20701 13622 12066 -2072 289 291 C ATOM 668 CG PHE A 120 15.990 -7.070 -7.477 1.00124.96 C ANISOU 668 CG PHE A 120 21064 14041 12376 -2360 380 396 C ATOM 669 CD1 PHE A 120 17.213 -7.720 -7.422 1.00126.50 C ANISOU 669 CD1 PHE A 120 20973 14492 12598 -2464 472 466 C ATOM 670 CD2 PHE A 120 15.976 -5.685 -7.512 1.00128.52 C ANISOU 670 CD2 PHE A 120 21807 14297 12727 -2529 380 434 C ATOM 671 CE1 PHE A 120 18.397 -7.004 -7.403 1.00128.09 C ANISOU 671 CE1 PHE A 120 21130 14805 12734 -2764 549 576 C ATOM 672 CE2 PHE A 120 17.156 -4.964 -7.492 1.00135.05 C ANISOU 672 CE2 PHE A 120 22647 15181 13486 -2856 459 531 C ATOM 673 CZ PHE A 120 18.367 -5.625 -7.438 1.00134.73 C ANISOU 673 CZ PHE A 120 22268 15446 13478 -2990 538 604 C ATOM 674 N MET A 121 12.765 -10.395 -8.281 1.00 99.78 N ANISOU 674 N MET A 121 17735 10882 9295 -1585 183 112 N ATOM 675 CA MET A 121 11.559 -11.174 -8.017 1.00 97.13 C ANISOU 675 CA MET A 121 17363 10548 8994 -1447 76 13 C ATOM 676 C MET A 121 11.897 -12.579 -7.541 1.00 91.50 C ANISOU 676 C MET A 121 16470 9934 8360 -1425 110 -30 C ATOM 677 O MET A 121 11.179 -13.142 -6.707 1.00 89.11 O ANISOU 677 O MET A 121 16089 9639 8129 -1391 30 -100 O ATOM 678 CB MET A 121 10.683 -11.241 -9.269 1.00 99.97 C ANISOU 678 CB MET A 121 17870 10884 9229 -1324 33 -8 C ATOM 679 CG MET A 121 10.004 -9.933 -9.640 1.00 96.56 C ANISOU 679 CG MET A 121 17631 10354 8703 -1270 -23 31 C ATOM 680 SD MET A 121 9.068 -10.053 -11.176 1.00102.50 S ANISOU 680 SD MET A 121 18529 11135 9281 -1118 -80 23 S ATOM 681 CE MET A 121 8.469 -8.375 -11.353 1.00 99.21 C ANISOU 681 CE MET A 121 18349 10593 8754 -1017 -119 102 C ATOM 682 N GLY A 122 12.978 -13.160 -8.055 1.00 90.35 N ANISOU 682 N GLY A 122 16273 9867 8189 -1427 239 21 N ATOM 683 CA GLY A 122 13.375 -14.496 -7.664 1.00 89.74 C ANISOU 683 CA GLY A 122 16075 9867 8157 -1360 298 -4 C ATOM 684 C GLY A 122 14.124 -14.527 -6.349 1.00 95.20 C ANISOU 684 C GLY A 122 16566 10651 8956 -1426 315 35 C ATOM 685 O GLY A 122 13.960 -15.458 -5.555 1.00 97.03 O ANISOU 685 O GLY A 122 16713 10903 9251 -1366 300 -9 O ATOM 686 N THR A 123 14.954 -13.509 -6.109 1.00 87.57 N ANISOU 686 N THR A 123 15534 9745 7993 -1570 344 121 N ATOM 687 CA THR A 123 15.691 -13.440 -4.852 1.00 86.65 C ANISOU 687 CA THR A 123 15221 9748 7955 -1670 340 163 C ATOM 688 C THR A 123 14.754 -13.197 -3.675 1.00 85.49 C ANISOU 688 C THR A 123 15091 9501 7892 -1698 203 80 C ATOM 689 O THR A 123 14.970 -13.733 -2.582 1.00 86.00 O ANISOU 689 O THR A 123 15006 9644 8027 -1693 184 72 O ATOM 690 CB THR A 123 16.755 -12.343 -4.926 1.00 84.35 C ANISOU 690 CB THR A 123 14879 9553 7617 -1880 390 272 C ATOM 691 OG1 THR A 123 17.565 -12.538 -6.092 1.00 85.35 O ANISOU 691 OG1 THR A 123 14986 9790 7655 -1844 530 359 O ATOM 692 CG2 THR A 123 17.645 -12.374 -3.691 1.00 89.92 C ANISOU 692 CG2 THR A 123 15347 10445 8375 -2004 383 326 C ATOM 693 N SER A 124 13.700 -12.404 -3.885 1.00 83.22 N ANISOU 693 N SER A 124 14984 9054 7580 -1700 115 27 N ATOM 694 CA SER A 124 12.790 -12.066 -2.794 1.00 78.42 C ANISOU 694 CA SER A 124 14400 8365 7030 -1700 3 -39 C ATOM 695 C SER A 124 12.061 -13.297 -2.268 1.00 76.61 C ANISOU 695 C SER A 124 14078 8164 6867 -1578 -37 -114 C ATOM 696 O SER A 124 11.887 -13.450 -1.053 1.00 84.59 O ANISOU 696 O SER A 124 15003 9190 7949 -1595 -84 -141 O ATOM 697 CB SER A 124 11.786 -11.012 -3.258 1.00 74.45 C ANISOU 697 CB SER A 124 14116 7713 6459 -1661 -62 -60 C ATOM 698 OG SER A 124 10.820 -10.758 -2.254 1.00 84.88 O ANISOU 698 OG SER A 124 15456 8977 7819 -1608 -154 -117 O ATOM 699 N VAL A 125 11.621 -14.181 -3.165 1.00 78.35 N ANISOU 699 N VAL A 125 14339 8381 7048 -1475 -17 -148 N ATOM 700 CA VAL A 125 10.892 -15.368 -2.728 1.00 78.49 C ANISOU 700 CA VAL A 125 14314 8405 7104 -1405 -50 -221 C ATOM 701 C VAL A 125 11.827 -16.361 -2.052 1.00 75.91 C ANISOU 701 C VAL A 125 13866 8150 6827 -1383 33 -194 C ATOM 702 O VAL A 125 11.424 -17.069 -1.120 1.00 75.32 O ANISOU 702 O VAL A 125 13738 8074 6808 -1362 4 -235 O ATOM 703 CB VAL A 125 10.155 -16.009 -3.920 1.00 75.50 C ANISOU 703 CB VAL A 125 14057 7995 6635 -1346 -60 -271 C ATOM 704 CG1 VAL A 125 9.263 -17.147 -3.447 1.00 73.68 C ANISOU 704 CG1 VAL A 125 13813 7761 6422 -1337 -108 -351 C ATOM 705 CG2 VAL A 125 9.342 -14.962 -4.662 1.00 70.58 C ANISOU 705 CG2 VAL A 125 13537 7341 5939 -1336 -139 -271 C ATOM 706 N SER A 126 13.084 -16.429 -2.495 1.00 95.60 N ANISOU 706 N SER A 126 16309 10727 9288 -1372 146 -111 N ATOM 707 CA SER A 126 14.018 -17.395 -1.926 1.00 95.47 C ANISOU 707 CA SER A 126 16167 10815 9291 -1294 239 -62 C ATOM 708 C SER A 126 14.387 -17.038 -0.491 1.00 98.33 C ANISOU 708 C SER A 126 16362 11265 9733 -1370 187 -32 C ATOM 709 O SER A 126 14.419 -17.914 0.381 1.00104.17 O ANISOU 709 O SER A 126 17037 12034 10510 -1295 197 -39 O ATOM 710 CB SER A 126 15.268 -17.486 -2.798 1.00 97.81 C ANISOU 710 CB SER A 126 16418 11233 9511 -1238 381 40 C ATOM 711 OG SER A 126 15.782 -16.196 -3.071 1.00105.20 O ANISOU 711 OG SER A 126 17306 12232 10432 -1390 370 105 O ATOM 712 N VAL A 127 14.672 -15.760 -0.222 1.00 95.38 N ANISOU 712 N VAL A 127 15950 10923 9367 -1529 135 1 N ATOM 713 CA VAL A 127 15.000 -15.368 1.145 1.00 95.04 C ANISOU 713 CA VAL A 127 15781 10955 9373 -1631 74 19 C ATOM 714 C VAL A 127 13.770 -15.452 2.038 1.00 92.16 C ANISOU 714 C VAL A 127 15485 10464 9069 -1606 -27 -78 C ATOM 715 O VAL A 127 13.880 -15.788 3.223 1.00 97.99 O ANISOU 715 O VAL A 127 16124 11257 9850 -1605 -56 -79 O ATOM 716 CB VAL A 127 15.621 -13.958 1.184 1.00 97.82 C ANISOU 716 CB VAL A 127 16134 11344 9688 -1849 46 72 C ATOM 717 CG1 VAL A 127 17.016 -13.969 0.583 1.00 99.81 C ANISOU 717 CG1 VAL A 127 16235 11809 9879 -1906 152 194 C ATOM 718 CG2 VAL A 127 14.733 -12.955 0.468 1.00 99.90 C ANISOU 718 CG2 VAL A 127 16632 11409 9917 -1891 0 21 C ATOM 719 N SER A 128 12.585 -15.163 1.496 1.00 75.60 N ANISOU 719 N SER A 128 13540 8223 6960 -1575 -79 -149 N ATOM 720 CA SER A 128 11.377 -15.186 2.313 1.00 73.38 C ANISOU 720 CA SER A 128 13292 7869 6720 -1544 -165 -225 C ATOM 721 C SER A 128 11.026 -16.605 2.744 1.00 75.34 C ANISOU 721 C SER A 128 13486 8135 7005 -1456 -145 -259 C ATOM 722 O SER A 128 10.619 -16.826 3.890 1.00 84.54 O ANISOU 722 O SER A 128 14600 9305 8215 -1455 -185 -285 O ATOM 723 CB SER A 128 10.216 -14.550 1.550 1.00 70.01 C ANISOU 723 CB SER A 128 13005 7347 6248 -1508 -221 -269 C ATOM 724 OG SER A 128 10.472 -13.181 1.289 1.00 74.85 O ANISOU 724 OG SER A 128 13727 7900 6814 -1575 -233 -235 O ATOM 725 N THR A 129 11.176 -17.579 1.843 1.00 83.61 N ANISOU 725 N THR A 129 14577 9176 8014 -1387 -73 -259 N ATOM 726 CA THR A 129 10.912 -18.965 2.216 1.00 87.44 C ANISOU 726 CA THR A 129 15080 9638 8507 -1318 -35 -289 C ATOM 727 C THR A 129 11.945 -19.474 3.212 1.00 85.71 C ANISOU 727 C THR A 129 14744 9504 8317 -1263 25 -224 C ATOM 728 O THR A 129 11.596 -20.159 4.181 1.00 86.40 O ANISOU 728 O THR A 129 14820 9573 8435 -1237 16 -244 O ATOM 729 CB THR A 129 10.893 -19.859 0.976 1.00 85.11 C ANISOU 729 CB THR A 129 14927 9282 8130 -1259 39 -309 C ATOM 730 OG1 THR A 129 12.079 -19.634 0.203 1.00 88.53 O ANISOU 730 OG1 THR A 129 15342 9775 8519 -1205 133 -233 O ATOM 731 CG2 THR A 129 9.672 -19.571 0.122 1.00 80.68 C ANISOU 731 CG2 THR A 129 14468 8664 7521 -1322 -44 -380 C ATOM 732 N TRP A 130 13.218 -19.149 2.994 1.00101.98 N ANISOU 732 N TRP A 130 16705 11685 10356 -1246 87 -134 N ATOM 733 CA TRP A 130 14.281 -19.682 3.835 1.00105.37 C ANISOU 733 CA TRP A 130 16990 12260 10786 -1167 146 -48 C ATOM 734 C TRP A 130 14.501 -18.871 5.105 1.00105.90 C ANISOU 734 C TRP A 130 16916 12423 10898 -1285 54 -29 C ATOM 735 O TRP A 130 15.217 -19.336 5.999 1.00107.35 O ANISOU 735 O TRP A 130 16969 12743 11077 -1225 75 36 O ATOM 736 CB TRP A 130 15.580 -19.784 3.033 1.00106.27 C ANISOU 736 CB TRP A 130 17019 12527 10832 -1086 263 60 C ATOM 737 CG TRP A 130 15.569 -20.953 2.095 1.00110.41 C ANISOU 737 CG TRP A 130 17705 12962 11285 -901 388 54 C ATOM 738 CD1 TRP A 130 15.218 -20.943 0.777 1.00108.65 C ANISOU 738 CD1 TRP A 130 17645 12629 11007 -898 424 11 C ATOM 739 CD2 TRP A 130 15.885 -22.314 2.415 1.00111.61 C ANISOU 739 CD2 TRP A 130 17920 13098 11387 -687 498 88 C ATOM 740 NE1 TRP A 130 15.315 -22.209 0.251 1.00112.02 N ANISOU 740 NE1 TRP A 130 18245 12969 11349 -714 549 8 N ATOM 741 CE2 TRP A 130 15.722 -23.069 1.238 1.00113.85 C ANISOU 741 CE2 TRP A 130 18435 13243 11581 -574 603 56 C ATOM 742 CE3 TRP A 130 16.299 -22.964 3.582 1.00107.93 C ANISOU 742 CE3 TRP A 130 17367 12715 10927 -570 523 146 C ATOM 743 CZ2 TRP A 130 15.958 -24.441 1.193 1.00118.96 C ANISOU 743 CZ2 TRP A 130 19264 13800 12135 -348 742 77 C ATOM 744 CZ3 TRP A 130 16.532 -24.326 3.536 1.00107.22 C ANISOU 744 CZ3 TRP A 130 17437 12549 10752 -326 661 178 C ATOM 745 CH2 TRP A 130 16.362 -25.050 2.349 1.00120.66 C ANISOU 745 CH2 TRP A 130 19405 14082 12358 -217 775 141 C ATOM 746 N ASN A 131 13.916 -17.677 5.209 1.00 97.57 N ANISOU 746 N ASN A 131 15907 11299 9866 -1437 -44 -80 N ATOM 747 CA ASN A 131 13.836 -17.023 6.509 1.00 88.02 C ANISOU 747 CA ASN A 131 14645 10117 8681 -1540 -134 -93 C ATOM 748 C ASN A 131 12.667 -17.557 7.322 1.00 86.10 C ANISOU 748 C ASN A 131 14466 9767 8482 -1477 -175 -169 C ATOM 749 O ASN A 131 12.713 -17.537 8.557 1.00 98.85 O ANISOU 749 O ASN A 131 16023 11425 10110 -1498 -217 -167 O ATOM 750 CB ASN A 131 13.714 -15.508 6.345 1.00 90.02 C ANISOU 750 CB ASN A 131 14983 10311 8911 -1709 -202 -112 C ATOM 751 CG ASN A 131 15.024 -14.857 5.949 1.00 95.67 C ANISOU 751 CG ASN A 131 15608 11171 9570 -1851 -174 -23 C ATOM 752 OD1 ASN A 131 15.044 -13.873 5.209 1.00 93.20 O ANISOU 752 OD1 ASN A 131 15407 10788 9218 -1965 -179 -21 O ATOM 753 ND2 ASN A 131 16.129 -15.409 6.438 1.00 96.78 N ANISOU 753 ND2 ASN A 131 15543 11536 9693 -1843 -141 65 N ATOM 754 N LEU A 132 11.619 -18.040 6.650 1.00 62.67 N ANISOU 754 N LEU A 132 11609 6681 5522 -1419 -165 -232 N ATOM 755 CA LEU A 132 10.487 -18.632 7.350 1.00 66.43 C ANISOU 755 CA LEU A 132 12123 7092 6027 -1387 -194 -293 C ATOM 756 C LEU A 132 10.817 -20.002 7.925 1.00 75.17 C ANISOU 756 C LEU A 132 13213 8215 7135 -1299 -125 -265 C ATOM 757 O LEU A 132 10.140 -20.447 8.857 1.00 74.84 O ANISOU 757 O LEU A 132 13180 8144 7112 -1295 -143 -294 O ATOM 758 CB LEU A 132 9.284 -18.734 6.413 1.00 65.44 C ANISOU 758 CB LEU A 132 12097 6884 5883 -1390 -214 -357 C ATOM 759 CG LEU A 132 8.453 -17.460 6.254 1.00 59.98 C ANISOU 759 CG LEU A 132 11438 6172 5181 -1423 -294 -388 C ATOM 760 CD1 LEU A 132 7.224 -17.722 5.397 1.00 67.32 C ANISOU 760 CD1 LEU A 132 12416 7088 6074 -1411 -324 -435 C ATOM 761 CD2 LEU A 132 8.058 -16.903 7.610 1.00 66.84 C ANISOU 761 CD2 LEU A 132 12274 7051 6072 -1428 -342 -400 C ATOM 762 N VAL A 133 11.829 -20.686 7.388 1.00 83.36 N ANISOU 762 N VAL A 133 14242 9296 8135 -1207 -32 -202 N ATOM 763 CA VAL A 133 12.306 -21.914 8.012 1.00 85.02 C ANISOU 763 CA VAL A 133 14460 9522 8321 -1075 49 -153 C ATOM 764 C VAL A 133 13.351 -21.631 9.082 1.00 89.79 C ANISOU 764 C VAL A 133 14885 10306 8925 -1045 33 -66 C ATOM 765 O VAL A 133 13.576 -22.481 9.956 1.00 96.73 O ANISOU 765 O VAL A 133 15758 11211 9785 -934 72 -24 O ATOM 766 CB VAL A 133 12.883 -22.895 6.974 1.00 84.35 C ANISOU 766 CB VAL A 133 14484 9399 8165 -932 179 -115 C ATOM 767 CG1 VAL A 133 11.857 -23.198 5.894 1.00 84.35 C ANISOU 767 CG1 VAL A 133 14680 9229 8139 -996 180 -209 C ATOM 768 CG2 VAL A 133 14.166 -22.348 6.371 1.00 96.25 C ANISOU 768 CG2 VAL A 133 15853 11077 9642 -883 223 -22 C ATOM 769 N ALA A 134 13.995 -20.462 9.042 1.00 74.89 N ANISOU 769 N ALA A 134 12867 8549 7040 -1157 -26 -34 N ATOM 770 CA ALA A 134 14.942 -20.106 10.091 1.00 83.19 C ANISOU 770 CA ALA A 134 13739 9800 8068 -1189 -68 43 C ATOM 771 C ALA A 134 14.226 -19.837 11.408 1.00 85.66 C ANISOU 771 C ALA A 134 14077 10061 8410 -1258 -158 -13 C ATOM 772 O ALA A 134 14.733 -20.190 12.479 1.00 92.59 O ANISOU 772 O ALA A 134 14860 11062 9258 -1210 -171 42 O ATOM 773 CB ALA A 134 15.765 -18.891 9.666 1.00 87.94 C ANISOU 773 CB ALA A 134 14229 10543 8643 -1357 -111 85 C ATOM 774 N ILE A 135 13.046 -19.216 11.351 1.00 92.87 N ANISOU 774 N ILE A 135 15115 10810 9363 -1349 -215 -114 N ATOM 775 CA ILE A 135 12.275 -18.999 12.571 1.00 94.64 C ANISOU 775 CA ILE A 135 15375 10985 9600 -1383 -278 -165 C ATOM 776 C ILE A 135 11.699 -20.312 13.082 1.00 93.81 C ANISOU 776 C ILE A 135 15316 10821 9508 -1260 -220 -169 C ATOM 777 O ILE A 135 11.563 -20.505 14.296 1.00 98.34 O ANISOU 777 O ILE A 135 15873 11421 10072 -1243 -243 -163 O ATOM 778 CB ILE A 135 11.173 -17.948 12.339 1.00 87.80 C ANISOU 778 CB ILE A 135 14622 9989 8750 -1466 -336 -252 C ATOM 779 CG1 ILE A 135 10.190 -18.416 11.265 1.00 90.44 C ANISOU 779 CG1 ILE A 135 15035 10218 9110 -1414 -298 -297 C ATOM 780 CG2 ILE A 135 11.779 -16.618 11.955 1.00 85.41 C ANISOU 780 CG2 ILE A 135 14337 9705 8411 -1600 -384 -244 C ATOM 781 CD1 ILE A 135 8.969 -17.540 11.135 1.00 92.52 C ANISOU 781 CD1 ILE A 135 15379 10402 9372 -1438 -349 -363 C ATOM 782 N SER A 136 11.355 -21.235 12.180 1.00 75.44 N ANISOU 782 N SER A 136 13076 8401 7185 -1188 -142 -180 N ATOM 783 CA SER A 136 10.875 -22.542 12.614 1.00 75.74 C ANISOU 783 CA SER A 136 13212 8356 7211 -1104 -73 -180 C ATOM 784 C SER A 136 11.978 -23.324 13.313 1.00 81.49 C ANISOU 784 C SER A 136 13892 9180 7890 -954 -12 -79 C ATOM 785 O SER A 136 11.736 -23.970 14.339 1.00 76.34 O ANISOU 785 O SER A 136 13281 8504 7220 -902 6 -62 O ATOM 786 CB SER A 136 10.336 -23.326 11.419 1.00 72.21 C ANISOU 786 CB SER A 136 12916 7773 6747 -1097 -5 -219 C ATOM 787 OG SER A 136 11.394 -23.907 10.677 1.00 73.30 O ANISOU 787 OG SER A 136 13085 7929 6836 -968 87 -154 O ATOM 788 N LEU A 137 13.198 -23.276 12.772 1.00 91.03 N ANISOU 788 N LEU A 137 15004 10521 9063 -869 25 3 N ATOM 789 CA LEU A 137 14.327 -23.909 13.443 1.00 95.20 C ANISOU 789 CA LEU A 137 15436 11213 9523 -693 77 125 C ATOM 790 C LEU A 137 14.681 -23.189 14.737 1.00 95.65 C ANISOU 790 C LEU A 137 15328 11443 9573 -773 -33 153 C ATOM 791 O LEU A 137 15.140 -23.824 15.693 1.00 94.51 O ANISOU 791 O LEU A 137 15141 11397 9371 -639 -14 232 O ATOM 792 CB LEU A 137 15.538 -23.949 12.511 1.00 91.61 C ANISOU 792 CB LEU A 137 14872 10918 9016 -579 147 221 C ATOM 793 CG LEU A 137 15.531 -25.018 11.418 1.00 80.16 C ANISOU 793 CG LEU A 137 13617 9320 7519 -402 296 230 C ATOM 794 CD1 LEU A 137 16.862 -25.030 10.685 1.00 90.58 C ANISOU 794 CD1 LEU A 137 14790 10858 8767 -244 380 353 C ATOM 795 CD2 LEU A 137 15.222 -26.389 12.001 1.00 90.53 C ANISOU 795 CD2 LEU A 137 15143 10478 8776 -223 394 249 C ATOM 796 N GLU A 138 14.476 -21.871 14.786 1.00 98.20 N ANISOU 796 N GLU A 138 15588 11793 9931 -984 -145 92 N ATOM 797 CA GLU A 138 14.745 -21.121 16.008 1.00101.95 C ANISOU 797 CA GLU A 138 15964 12398 10374 -1095 -255 99 C ATOM 798 C GLU A 138 13.757 -21.494 17.105 1.00100.08 C ANISOU 798 C GLU A 138 15842 12035 10150 -1070 -267 46 C ATOM 799 O GLU A 138 14.151 -21.756 18.248 1.00 99.94 O ANISOU 799 O GLU A 138 15766 12132 10074 -1019 -294 99 O ATOM 800 CB GLU A 138 14.698 -19.619 15.721 1.00 98.19 C ANISOU 800 CB GLU A 138 15481 11919 9908 -1329 -352 37 C ATOM 801 CG GLU A 138 15.109 -18.735 16.892 1.00111.74 C ANISOU 801 CG GLU A 138 17139 13760 11556 -1487 -469 39 C ATOM 802 CD GLU A 138 13.946 -18.384 17.803 1.00110.44 C ANISOU 802 CD GLU A 138 17137 13421 11405 -1520 -512 -61 C ATOM 803 OE1 GLU A 138 12.799 -18.323 17.310 1.00103.77 O ANISOU 803 OE1 GLU A 138 16427 12377 10624 -1492 -476 -140 O ATOM 804 OE2 GLU A 138 14.177 -18.169 19.012 1.00106.09 O ANISOU 804 OE2 GLU A 138 16567 12956 10785 -1569 -580 -53 O ATOM 805 N ARG A 139 12.463 -21.524 16.776 1.00 90.57 N ANISOU 805 N ARG A 139 14786 10622 9005 -1106 -246 -50 N ATOM 806 CA ARG A 139 11.453 -21.877 17.765 1.00 87.94 C ANISOU 806 CA ARG A 139 14543 10193 8677 -1095 -243 -93 C ATOM 807 C ARG A 139 11.534 -23.341 18.178 1.00 91.52 C ANISOU 807 C ARG A 139 15063 10614 9098 -938 -145 -29 C ATOM 808 O ARG A 139 11.089 -23.685 19.278 1.00 95.76 O ANISOU 808 O ARG A 139 15646 11130 9610 -916 -142 -26 O ATOM 809 CB ARG A 139 10.056 -21.561 17.227 1.00 81.23 C ANISOU 809 CB ARG A 139 13791 9192 7882 -1173 -242 -190 C ATOM 810 CG ARG A 139 9.815 -20.086 16.935 1.00 76.20 C ANISOU 810 CG ARG A 139 13146 8551 7255 -1285 -325 -249 C ATOM 811 CD ARG A 139 9.413 -19.326 18.188 1.00 89.87 C ANISOU 811 CD ARG A 139 14906 10292 8948 -1322 -383 -282 C ATOM 812 NE ARG A 139 10.567 -18.971 19.007 1.00 95.31 N ANISOU 812 NE ARG A 139 15537 11105 9573 -1363 -443 -236 N ATOM 813 CZ ARG A 139 10.532 -18.816 20.323 1.00 90.46 C ANISOU 813 CZ ARG A 139 14944 10528 8898 -1368 -481 -239 C ATOM 814 NH1 ARG A 139 9.413 -18.979 21.009 1.00 85.65 N ANISOU 814 NH1 ARG A 139 14414 9840 8290 -1316 -450 -279 N ATOM 815 NH2 ARG A 139 11.649 -18.490 20.967 1.00 90.46 N ANISOU 815 NH2 ARG A 139 14875 10674 8821 -1436 -553 -193 N ATOM 816 N TYR A 140 12.087 -24.207 17.328 1.00 83.77 N ANISOU 816 N TYR A 140 14120 9611 8098 -817 -53 25 N ATOM 817 CA TYR A 140 12.258 -25.605 17.709 1.00 86.64 C ANISOU 817 CA TYR A 140 14608 9911 8400 -638 58 96 C ATOM 818 C TYR A 140 13.377 -25.758 18.730 1.00 95.57 C ANISOU 818 C TYR A 140 15612 11250 9452 -488 42 215 C ATOM 819 O TYR A 140 13.226 -26.467 19.732 1.00 99.10 O ANISOU 819 O TYR A 140 16142 11667 9846 -393 78 257 O ATOM 820 CB TYR A 140 12.537 -26.460 16.472 1.00 85.48 C ANISOU 820 CB TYR A 140 14593 9658 8227 -525 176 119 C ATOM 821 CG TYR A 140 13.091 -27.831 16.791 1.00 79.11 C ANISOU 821 CG TYR A 140 13940 8800 7318 -276 310 222 C ATOM 822 CD1 TYR A 140 12.258 -28.854 17.227 1.00 83.69 C ANISOU 822 CD1 TYR A 140 14778 9160 7862 -274 391 201 C ATOM 823 CD2 TYR A 140 14.447 -28.102 16.661 1.00 81.16 C ANISOU 823 CD2 TYR A 140 14096 9242 7498 -35 365 353 C ATOM 824 CE1 TYR A 140 12.760 -30.108 17.522 1.00 86.75 C ANISOU 824 CE1 TYR A 140 15369 9459 8132 -29 529 300 C ATOM 825 CE2 TYR A 140 14.958 -29.352 16.955 1.00 87.35 C ANISOU 825 CE2 TYR A 140 15047 9978 8165 251 503 462 C ATOM 826 CZ TYR A 140 14.110 -30.351 17.385 1.00 93.48 C ANISOU 826 CZ TYR A 140 16133 10482 8903 258 588 432 C ATOM 827 OH TYR A 140 14.614 -31.599 17.678 1.00 96.39 O ANISOU 827 OH TYR A 140 16730 10761 9132 559 740 546 O ATOM 828 N GLY A 141 14.513 -25.098 18.492 1.00111.66 N ANISOU 828 N GLY A 141 17439 13523 11464 -478 -14 279 N ATOM 829 CA GLY A 141 15.627 -25.201 19.417 1.00116.75 C ANISOU 829 CA GLY A 141 17912 14437 12011 -352 -48 405 C ATOM 830 C GLY A 141 15.377 -24.506 20.740 1.00119.36 C ANISOU 830 C GLY A 141 18187 14843 12323 -492 -174 371 C ATOM 831 O GLY A 141 15.944 -24.895 21.764 1.00129.08 O ANISOU 831 O GLY A 141 19350 16237 13459 -371 -192 464 O ATOM 832 N ALA A 142 14.528 -23.478 20.743 1.00110.77 N ANISOU 832 N ALA A 142 17143 13641 11305 -724 -256 243 N ATOM 833 CA ALA A 142 14.245 -22.747 21.971 1.00109.88 C ANISOU 833 CA ALA A 142 17025 13571 11155 -849 -363 199 C ATOM 834 C ALA A 142 13.185 -23.424 22.830 1.00110.13 C ANISOU 834 C ALA A 142 17223 13431 11189 -784 -307 167 C ATOM 835 O ALA A 142 13.124 -23.157 24.035 1.00116.00 O ANISOU 835 O ALA A 142 17969 14238 11868 -811 -369 166 O ATOM 836 CB ALA A 142 13.804 -21.318 21.646 1.00107.55 C ANISOU 836 CB ALA A 142 16749 13212 10902 -1087 -454 86 C ATOM 837 N ILE A 143 12.360 -24.290 22.248 1.00 97.06 N ANISOU 837 N ILE A 143 15716 11572 9592 -720 -192 141 N ATOM 838 CA ILE A 143 11.269 -24.950 22.963 1.00 94.07 C ANISOU 838 CA ILE A 143 15494 11036 9211 -706 -127 113 C ATOM 839 C ILE A 143 11.545 -26.439 23.150 1.00101.26 C ANISOU 839 C ILE A 143 16534 11882 10060 -511 -2 212 C ATOM 840 O ILE A 143 11.535 -26.945 24.274 1.00103.17 O ANISOU 840 O ILE A 143 16834 12139 10227 -425 19 267 O ATOM 841 CB ILE A 143 9.917 -24.718 22.252 1.00 85.86 C ANISOU 841 CB ILE A 143 14540 9823 8260 -845 -101 4 C ATOM 842 CG1 ILE A 143 9.563 -23.230 22.239 1.00 84.83 C ANISOU 842 CG1 ILE A 143 14332 9737 8161 -984 -207 -81 C ATOM 843 CG2 ILE A 143 8.823 -25.534 22.918 1.00 79.24 C ANISOU 843 CG2 ILE A 143 13839 8862 7405 -855 -19 -5 C ATOM 844 CD1 ILE A 143 8.368 -22.899 21.373 1.00 80.46 C ANISOU 844 CD1 ILE A 143 13820 9074 7679 -1078 -189 -167 C ATOM 845 N CYS A 144 11.795 -27.160 22.056 1.00118.75 N ANISOU 845 N CYS A 144 18830 14006 12285 -426 90 237 N ATOM 846 CA CYS A 144 11.885 -28.614 22.130 1.00117.83 C ANISOU 846 CA CYS A 144 18932 13748 12089 -241 236 316 C ATOM 847 C CYS A 144 13.200 -29.077 22.748 1.00121.27 C ANISOU 847 C CYS A 144 19297 14372 12408 32 256 469 C ATOM 848 O CYS A 144 13.216 -30.044 23.517 1.00129.15 O ANISOU 848 O CYS A 144 20461 15298 13311 196 343 550 O ATOM 849 CB CYS A 144 11.706 -29.220 20.739 1.00118.34 C ANISOU 849 CB CYS A 144 19158 13631 12173 -236 336 285 C ATOM 850 SG CYS A 144 10.027 -29.077 20.084 1.00125.62 S ANISOU 850 SG CYS A 144 20201 14343 13185 -540 332 132 S ATOM 851 N LYS A 145 14.308 -28.412 22.428 1.00105.15 N ANISOU 851 N LYS A 145 17007 12591 10356 86 180 524 N ATOM 852 CA LYS A 145 15.624 -28.764 22.963 1.00114.01 C ANISOU 852 CA LYS A 145 17986 13984 11350 347 183 688 C ATOM 853 C LYS A 145 16.348 -27.505 23.434 1.00124.16 C ANISOU 853 C LYS A 145 18944 15607 12625 202 2 699 C ATOM 854 O LYS A 145 17.341 -27.074 22.834 1.00131.48 O ANISOU 854 O LYS A 145 19647 16780 13530 222 -35 762 O ATOM 855 CB LYS A 145 16.439 -29.542 21.927 1.00114.01 C ANISOU 855 CB LYS A 145 18027 13999 11291 609 317 789 C ATOM 856 CG LYS A 145 16.602 -28.861 20.571 1.00118.18 C ANISOU 856 CG LYS A 145 18443 14553 11907 480 299 725 C ATOM 857 CD LYS A 145 17.354 -29.752 19.594 1.00123.82 C ANISOU 857 CD LYS A 145 19246 15260 12540 779 461 829 C ATOM 858 CE LYS A 145 18.802 -29.933 20.015 1.00134.42 C ANISOU 858 CE LYS A 145 20334 16998 13743 1079 470 1028 C ATOM 859 NZ LYS A 145 19.571 -30.749 19.036 1.00133.53 N ANISOU 859 NZ LYS A 145 20297 16907 13533 1418 647 1143 N ATOM 860 N PRO A 146 15.887 -26.901 24.535 1.00128.39 N ANISOU 860 N PRO A 146 19461 16166 13154 41 -107 642 N ATOM 861 CA PRO A 146 16.517 -25.664 25.022 1.00128.94 C ANISOU 861 CA PRO A 146 19285 16518 13188 -147 -285 633 C ATOM 862 C PRO A 146 17.919 -25.856 25.579 1.00137.02 C ANISOU 862 C PRO A 146 20066 17938 14056 16 -341 804 C ATOM 863 O PRO A 146 18.556 -24.863 25.952 1.00139.05 O ANISOU 863 O PRO A 146 20109 18468 14255 -178 -499 807 O ATOM 864 CB PRO A 146 15.555 -25.194 26.129 1.00121.36 C ANISOU 864 CB PRO A 146 18448 15432 12231 -306 -352 532 C ATOM 865 CG PRO A 146 14.287 -25.977 25.916 1.00116.62 C ANISOU 865 CG PRO A 146 18108 14491 11713 -263 -214 467 C ATOM 866 CD PRO A 146 14.740 -27.290 25.370 1.00121.55 C ANISOU 866 CD PRO A 146 18818 15067 12300 2 -68 579 C ATOM 867 N LEU A 147 18.425 -27.087 25.647 1.00137.82 N ANISOU 867 N LEU A 147 20205 18093 14069 364 -218 952 N ATOM 868 CA LEU A 147 19.719 -27.351 26.264 1.00143.55 C ANISOU 868 CA LEU A 147 20681 19241 14621 576 -266 1141 C ATOM 869 C LEU A 147 20.875 -27.265 25.272 1.00151.26 C ANISOU 869 C LEU A 147 21386 20525 15561 679 -246 1257 C ATOM 870 O LEU A 147 21.944 -26.751 25.615 1.00151.16 O ANISOU 870 O LEU A 147 21035 20965 15433 635 -371 1365 O ATOM 871 CB LEU A 147 19.716 -28.731 26.930 1.00140.21 C ANISOU 871 CB LEU A 147 20452 18737 14085 958 -131 1268 C ATOM 872 CG LEU A 147 19.195 -28.848 28.367 1.00133.57 C ANISOU 872 CG LEU A 147 19737 17840 13175 934 -187 1254 C ATOM 873 CD1 LEU A 147 20.044 -28.015 29.317 1.00127.63 C ANISOU 873 CD1 LEU A 147 18671 17529 12292 814 -395 1314 C ATOM 874 CD2 LEU A 147 17.723 -28.468 28.476 1.00128.83 C ANISOU 874 CD2 LEU A 147 19386 16844 12718 651 -183 1054 C ATOM 875 N GLN A 148 20.684 -27.758 24.048 1.00193.18 N ANISOU 875 N GLN A 148 26831 25618 20949 800 -91 1240 N ATOM 876 CA GLN A 148 21.760 -27.855 23.069 1.00195.72 C ANISOU 876 CA GLN A 148 26929 26216 21221 967 -28 1367 C ATOM 877 C GLN A 148 21.600 -26.866 21.919 1.00198.38 C ANISOU 877 C GLN A 148 27193 26492 21690 657 -68 1247 C ATOM 878 O GLN A 148 22.222 -27.040 20.866 1.00197.15 O ANISOU 878 O GLN A 148 26939 26448 21520 792 28 1321 O ATOM 879 CB GLN A 148 21.851 -29.282 22.524 1.00195.69 C ANISOU 879 CB GLN A 148 27166 26034 21154 1416 207 1471 C ATOM 880 CG GLN A 148 21.712 -30.369 23.579 1.00197.12 C ANISOU 880 CG GLN A 148 27562 26121 21214 1723 285 1564 C ATOM 881 CD GLN A 148 20.272 -30.794 23.794 1.00196.56 C ANISOU 881 CD GLN A 148 27921 25519 21243 1592 347 1402 C ATOM 882 OE1 GLN A 148 19.343 -30.150 23.306 1.00192.40 O ANISOU 882 OE1 GLN A 148 27480 24746 20877 1252 298 1217 O ATOM 883 NE2 GLN A 148 20.079 -31.885 24.527 1.00204.26 N ANISOU 883 NE2 GLN A 148 29166 26334 22109 1864 459 1483 N ATOM 884 N SER A 149 20.783 -25.829 22.097 1.00199.97 N ANISOU 884 N SER A 149 27458 26517 22003 269 -197 1070 N ATOM 885 CA SER A 149 20.543 -24.842 21.052 1.00201.24 C ANISOU 885 CA SER A 149 27596 26587 22278 -19 -235 954 C ATOM 886 C SER A 149 21.190 -23.496 21.356 1.00202.85 C ANISOU 886 C SER A 149 27534 27100 22439 -360 -421 949 C ATOM 887 O SER A 149 20.946 -22.528 20.628 1.00198.96 O ANISOU 887 O SER A 149 27061 26509 22027 -637 -466 846 O ATOM 888 CB SER A 149 19.040 -24.661 20.831 1.00193.62 C ANISOU 888 CB SER A 149 26949 25159 21459 -182 -218 759 C ATOM 889 OG SER A 149 18.378 -24.362 22.048 1.00192.87 O ANISOU 889 OG SER A 149 26942 24979 21359 -308 -312 686 O ATOM 890 N ARG A 150 22.019 -23.416 22.402 1.00179.32 N ANISOU 890 N ARG A 150 24327 24492 19314 -358 -530 1062 N ATOM 891 CA ARG A 150 22.609 -22.139 22.793 1.00176.08 C ANISOU 891 CA ARG A 150 23705 24367 18831 -743 -721 1047 C ATOM 892 C ARG A 150 23.429 -21.519 21.669 1.00173.08 C ANISOU 892 C ARG A 150 23097 24218 18448 -902 -719 1102 C ATOM 893 O ARG A 150 23.565 -20.291 21.606 1.00170.78 O ANISOU 893 O ARG A 150 22763 23982 18143 -1308 -847 1028 O ATOM 894 CB ARG A 150 23.477 -22.321 24.039 1.00171.16 C ANISOU 894 CB ARG A 150 22841 24172 18019 -690 -836 1187 C ATOM 895 CG ARG A 150 22.728 -22.857 25.246 1.00166.67 C ANISOU 895 CG ARG A 150 22496 23401 17431 -555 -847 1142 C ATOM 896 CD ARG A 150 23.548 -22.696 26.514 1.00166.77 C ANISOU 896 CD ARG A 150 22279 23844 17241 -611 -1011 1250 C ATOM 897 NE ARG A 150 22.854 -23.214 27.687 1.00160.39 N ANISOU 897 NE ARG A 150 21694 22848 16400 -473 -1013 1215 N ATOM 898 CZ ARG A 150 23.342 -23.186 28.919 1.00159.92 C ANISOU 898 CZ ARG A 150 21513 23089 16161 -487 -1148 1291 C ATOM 899 NH1 ARG A 150 24.532 -22.670 29.179 1.00159.90 N ANISOU 899 NH1 ARG A 150 21150 23616 15987 -654 -1307 1407 N ATOM 900 NH2 ARG A 150 22.618 -23.689 29.915 1.00163.63 N ANISOU 900 NH2 ARG A 150 22221 23343 16609 -349 -1126 1254 N ATOM 901 N VAL A 151 23.977 -22.342 20.772 1.00165.28 N ANISOU 901 N VAL A 151 21992 23353 17455 -589 -563 1231 N ATOM 902 CA VAL A 151 24.727 -21.824 19.634 1.00163.15 C ANISOU 902 CA VAL A 151 21510 23301 17179 -711 -533 1293 C ATOM 903 C VAL A 151 23.831 -21.233 18.559 1.00158.60 C ANISOU 903 C VAL A 151 21201 22296 16764 -901 -486 1120 C ATOM 904 O VAL A 151 24.339 -20.654 17.593 1.00157.82 O ANISOU 904 O VAL A 151 20973 22326 16667 -1055 -466 1149 O ATOM 905 CB VAL A 151 25.609 -22.928 19.017 1.00159.51 C ANISOU 905 CB VAL A 151 20852 23118 16636 -262 -358 1498 C ATOM 906 CG1 VAL A 151 26.652 -23.397 20.019 1.00157.13 C ANISOU 906 CG1 VAL A 151 20218 23342 16142 -63 -413 1705 C ATOM 907 CG2 VAL A 151 24.750 -24.091 18.545 1.00161.56 C ANISOU 907 CG2 VAL A 151 21475 22926 16986 114 -165 1445 C ATOM 908 N TRP A 152 22.511 -21.359 18.700 1.00195.28 N ANISOU 908 N TRP A 152 26202 26463 21532 -893 -465 952 N ATOM 909 CA TRP A 152 21.568 -20.854 17.709 1.00192.54 C ANISOU 909 CA TRP A 152 26105 25728 21324 -1036 -425 797 C ATOM 910 C TRP A 152 20.913 -19.542 18.118 1.00192.27 C ANISOU 910 C TRP A 152 26216 25514 21324 -1419 -570 644 C ATOM 911 O TRP A 152 20.787 -18.637 17.287 1.00196.67 O ANISOU 911 O TRP A 152 26836 25968 21923 -1642 -584 578 O ATOM 912 CB TRP A 152 20.480 -21.898 17.431 1.00190.44 C ANISOU 912 CB TRP A 152 26134 25072 21154 -769 -292 723 C ATOM 913 CG TRP A 152 19.583 -21.534 16.286 1.00188.51 C ANISOU 913 CG TRP A 152 26104 24495 21028 -871 -244 591 C ATOM 914 CD1 TRP A 152 18.462 -20.757 16.336 1.00184.20 C ANISOU 914 CD1 TRP A 152 25758 23662 20568 -1085 -314 432 C ATOM 915 CD2 TRP A 152 19.735 -21.930 14.917 1.00189.93 C ANISOU 915 CD2 TRP A 152 26317 24616 21232 -741 -113 616 C ATOM 916 NE1 TRP A 152 17.906 -20.646 15.085 1.00182.64 N ANISOU 916 NE1 TRP A 152 25697 23252 20446 -1099 -247 363 N ATOM 917 CE2 TRP A 152 18.669 -21.357 14.196 1.00185.48 C ANISOU 917 CE2 TRP A 152 25968 23735 20771 -906 -127 466 C ATOM 918 CE3 TRP A 152 20.669 -22.713 14.231 1.00192.20 C ANISOU 918 CE3 TRP A 152 26482 25097 21447 -478 20 758 C ATOM 919 CZ2 TRP A 152 18.510 -21.543 12.824 1.00184.35 C ANISOU 919 CZ2 TRP A 152 25922 23462 20661 -845 -27 446 C ATOM 920 CZ3 TRP A 152 20.510 -22.896 12.869 1.00193.57 C ANISOU 920 CZ3 TRP A 152 26774 25119 21654 -411 134 731 C ATOM 921 CH2 TRP A 152 19.439 -22.314 12.180 1.00187.77 C ANISOU 921 CH2 TRP A 152 26256 24066 21023 -609 102 573 C ATOM 922 N GLN A 153 20.490 -19.410 19.375 1.00183.37 N ANISOU 922 N GLN A 153 25175 24335 20164 -1481 -665 589 N ATOM 923 CA GLN A 153 19.821 -18.196 19.828 1.00183.47 C ANISOU 923 CA GLN A 153 25380 24148 20183 -1796 -782 442 C ATOM 924 C GLN A 153 20.784 -17.054 20.135 1.00180.32 C ANISOU 924 C GLN A 153 24836 24025 19653 -2161 -927 473 C ATOM 925 O GLN A 153 20.369 -16.067 20.751 1.00179.95 O ANISOU 925 O GLN A 153 24981 23831 19560 -2421 -1032 361 O ATOM 926 CB GLN A 153 18.956 -18.485 21.059 1.00187.95 C ANISOU 926 CB GLN A 153 26120 24543 20748 -1716 -814 370 C ATOM 927 CG GLN A 153 17.652 -19.205 20.747 1.00184.86 C ANISOU 927 CG GLN A 153 25956 23795 20488 -1501 -694 287 C ATOM 928 CD GLN A 153 17.791 -20.711 20.765 1.00183.64 C ANISOU 928 CD GLN A 153 25751 23683 20340 -1166 -574 388 C ATOM 929 OE1 GLN A 153 18.699 -21.252 21.392 1.00190.65 O ANISOU 929 OE1 GLN A 153 26462 24852 21125 -1039 -589 517 O ATOM 930 NE2 GLN A 153 16.892 -21.398 20.069 1.00173.39 N ANISOU 930 NE2 GLN A 153 24626 22110 19143 -1021 -454 336 N ATOM 931 N THR A 154 22.047 -17.160 19.734 1.00131.51 N ANISOU 931 N THR A 154 18335 18245 13388 -2194 -930 624 N ATOM 932 CA THR A 154 22.957 -16.028 19.826 1.00128.63 C ANISOU 932 CA THR A 154 17830 18153 12891 -2611 -1062 655 C ATOM 933 C THR A 154 22.746 -15.100 18.636 1.00126.73 C ANISOU 933 C THR A 154 17742 17698 12711 -2837 -1024 582 C ATOM 934 O THR A 154 22.504 -15.551 17.513 1.00126.74 O ANISOU 934 O THR A 154 17760 17573 12823 -2630 -886 595 O ATOM 935 CB THR A 154 24.412 -16.501 19.890 1.00128.44 C ANISOU 935 CB THR A 154 17352 18715 12733 -2567 -1081 868 C ATOM 936 OG1 THR A 154 25.291 -15.373 19.794 1.00124.11 O ANISOU 936 OG1 THR A 154 16655 18449 12053 -3033 -1201 903 O ATOM 937 CG2 THR A 154 24.716 -17.487 18.774 1.00126.09 C ANISOU 937 CG2 THR A 154 16896 18503 12509 -2196 -897 986 C ATOM 938 N LYS A 155 22.824 -13.792 18.894 1.00161.69 N ANISOU 938 N LYS A 155 22323 22065 17047 -3265 -1143 503 N ATOM 939 CA LYS A 155 22.490 -12.815 17.863 1.00156.32 C ANISOU 939 CA LYS A 155 21875 21112 16407 -3478 -1106 422 C ATOM 940 C LYS A 155 23.486 -12.837 16.710 1.00153.15 C ANISOU 940 C LYS A 155 21198 21003 15990 -3546 -1036 558 C ATOM 941 O LYS A 155 23.122 -12.507 15.576 1.00155.44 O ANISOU 941 O LYS A 155 21640 21061 16358 -3544 -945 519 O ATOM 942 CB LYS A 155 22.412 -11.416 18.472 1.00161.14 C ANISOU 942 CB LYS A 155 22769 21571 16884 -3923 -1239 314 C ATOM 943 CG LYS A 155 21.484 -11.319 19.674 1.00163.24 C ANISOU 943 CG LYS A 155 23316 21573 17134 -3857 -1301 185 C ATOM 944 CD LYS A 155 20.025 -11.407 19.254 1.00155.91 C ANISOU 944 CD LYS A 155 22704 20173 16362 -3573 -1191 61 C ATOM 945 CE LYS A 155 19.096 -11.032 20.397 1.00156.05 C ANISOU 945 CE LYS A 155 23036 19922 16332 -3557 -1243 -67 C ATOM 946 NZ LYS A 155 19.167 -9.579 20.717 1.00150.12 N ANISOU 946 NZ LYS A 155 22624 18999 15416 -3945 -1331 -158 N ATOM 947 N SER A 156 24.737 -13.221 16.972 1.00123.87 N ANISOU 947 N SER A 156 17074 17824 12166 -3589 -1074 728 N ATOM 948 CA SER A 156 25.728 -13.274 15.902 1.00122.84 C ANISOU 948 CA SER A 156 16642 18029 12003 -3631 -991 879 C ATOM 949 C SER A 156 25.451 -14.416 14.933 1.00126.09 C ANISOU 949 C SER A 156 17000 18356 12551 -3139 -800 930 C ATOM 950 O SER A 156 25.853 -14.347 13.765 1.00126.11 O ANISOU 950 O SER A 156 16912 18437 12567 -3136 -694 998 O ATOM 951 CB SER A 156 27.133 -13.403 16.490 1.00124.43 C ANISOU 951 CB SER A 156 16371 18885 12022 -3784 -1081 1068 C ATOM 952 OG SER A 156 27.225 -14.525 17.350 1.00129.89 O ANISOU 952 OG SER A 156 16874 19776 12702 -3408 -1085 1144 O ATOM 953 N HIS A 157 24.772 -15.470 15.392 1.00129.72 N ANISOU 953 N HIS A 157 17543 18646 13097 -2739 -750 896 N ATOM 954 CA HIS A 157 24.436 -16.577 14.501 1.00125.63 C ANISOU 954 CA HIS A 157 17054 17993 12686 -2301 -569 925 C ATOM 955 C HIS A 157 23.336 -16.182 13.524 1.00123.84 C ANISOU 955 C HIS A 157 17184 17280 12591 -2321 -505 771 C ATOM 956 O HIS A 157 23.395 -16.533 12.340 1.00128.44 O ANISOU 956 O HIS A 157 17766 17821 13216 -2162 -372 807 O ATOM 957 CB HIS A 157 24.012 -17.798 15.317 1.00126.86 C ANISOU 957 CB HIS A 157 17244 18087 12871 -1916 -534 932 C ATOM 958 CG HIS A 157 23.959 -19.067 14.525 1.00133.31 C ANISOU 958 CG HIS A 157 18069 18847 13736 -1468 -344 999 C ATOM 959 ND1 HIS A 157 25.091 -19.723 14.093 1.00134.91 N ANISOU 959 ND1 HIS A 157 17965 19452 13842 -1232 -238 1194 N ATOM 960 CD2 HIS A 157 22.909 -19.803 14.089 1.00137.36 C ANISOU 960 CD2 HIS A 157 18880 18950 14361 -1221 -238 899 C ATOM 961 CE1 HIS A 157 24.742 -20.807 13.424 1.00137.70 C ANISOU 961 CE1 HIS A 157 18475 19603 14242 -841 -65 1203 C ATOM 962 NE2 HIS A 157 23.423 -20.879 13.407 1.00140.82 N ANISOU 962 NE2 HIS A 157 19238 19505 14763 -856 -70 1021 N ATOM 963 N ALA A 158 22.324 -15.453 14.002 1.00104.85 N ANISOU 963 N ALA A 158 15087 14518 10233 -2497 -595 607 N ATOM 964 CA ALA A 158 21.231 -15.044 13.127 1.00 99.77 C ANISOU 964 CA ALA A 158 14764 13449 9695 -2493 -544 474 C ATOM 965 C ALA A 158 21.696 -14.058 12.064 1.00101.38 C ANISOU 965 C ALA A 158 14985 13675 9860 -2755 -526 497 C ATOM 966 O ALA A 158 21.133 -14.025 10.964 1.00 99.72 O ANISOU 966 O ALA A 158 14937 13231 9720 -2661 -440 451 O ATOM 967 CB ALA A 158 20.095 -14.440 13.952 1.00 95.62 C ANISOU 967 CB ALA A 158 14542 12590 9199 -2589 -635 318 C ATOM 968 N LEU A 159 22.715 -13.252 12.365 1.00112.30 N ANISOU 968 N LEU A 159 16208 15344 11115 -3103 -609 571 N ATOM 969 CA LEU A 159 23.196 -12.283 11.386 1.00113.60 C ANISOU 969 CA LEU A 159 16406 15532 11226 -3396 -585 602 C ATOM 970 C LEU A 159 23.943 -12.967 10.248 1.00117.27 C ANISOU 970 C LEU A 159 16606 16256 11697 -3206 -440 744 C ATOM 971 O LEU A 159 23.867 -12.525 9.096 1.00120.79 O ANISOU 971 O LEU A 159 17168 16570 12156 -3267 -361 739 O ATOM 972 CB LEU A 159 24.089 -11.245 12.065 1.00117.72 C ANISOU 972 CB LEU A 159 16845 16300 11585 -3879 -717 644 C ATOM 973 CG LEU A 159 23.423 -10.365 13.123 1.00115.41 C ANISOU 973 CG LEU A 159 16888 15720 11242 -4119 -853 497 C ATOM 974 CD1 LEU A 159 24.427 -9.385 13.710 1.00113.02 C ANISOU 974 CD1 LEU A 159 16516 15683 10745 -4645 -983 544 C ATOM 975 CD2 LEU A 159 22.228 -9.632 12.536 1.00110.87 C ANISOU 975 CD2 LEU A 159 16778 14612 10734 -4101 -812 349 C ATOM 976 N LYS A 160 24.668 -14.045 10.547 1.00137.87 N ANISOU 976 N LYS A 160 18876 19230 14277 -2947 -393 877 N ATOM 977 CA LYS A 160 25.442 -14.728 9.519 1.00139.95 C ANISOU 977 CA LYS A 160 18891 19765 14517 -2721 -235 1027 C ATOM 978 C LYS A 160 24.611 -15.701 8.694 1.00137.56 C ANISOU 978 C LYS A 160 18795 19144 14329 -2300 -91 966 C ATOM 979 O LYS A 160 25.078 -16.143 7.639 1.00138.59 O ANISOU 979 O LYS A 160 18827 19394 14436 -2118 56 1058 O ATOM 980 CB LYS A 160 26.628 -15.464 10.149 1.00149.16 C ANISOU 980 CB LYS A 160 19612 21490 15571 -2578 -228 1219 C ATOM 981 CG LYS A 160 26.295 -16.823 10.737 1.00154.34 C ANISOU 981 CG LYS A 160 20267 22106 16271 -2105 -174 1231 C ATOM 982 CD LYS A 160 27.484 -17.387 11.501 1.00162.69 C ANISOU 982 CD LYS A 160 20888 23741 17187 -1979 -189 1433 C ATOM 983 CE LYS A 160 27.314 -18.870 11.782 1.00165.87 C ANISOU 983 CE LYS A 160 21306 24113 17604 -1426 -73 1486 C ATOM 984 NZ LYS A 160 28.481 -19.431 12.517 1.00165.04 N ANISOU 984 NZ LYS A 160 20773 24594 17339 -1243 -81 1704 N ATOM 985 N VAL A 161 23.403 -16.044 9.137 1.00104.24 N ANISOU 985 N VAL A 161 14858 14536 10211 -2157 -126 817 N ATOM 986 CA VAL A 161 22.535 -16.886 8.322 1.00104.96 C ANISOU 986 CA VAL A 161 15173 14315 10392 -1839 -8 745 C ATOM 987 C VAL A 161 21.600 -16.052 7.448 1.00106.62 C ANISOU 987 C VAL A 161 15686 14159 10664 -1994 -21 613 C ATOM 988 O VAL A 161 21.209 -16.500 6.366 1.00107.67 O ANISOU 988 O VAL A 161 15951 14131 10828 -1815 85 589 O ATOM 989 CB VAL A 161 21.746 -17.874 9.198 1.00 94.89 C ANISOU 989 CB VAL A 161 14017 12861 9176 -1587 -20 677 C ATOM 990 CG1 VAL A 161 22.698 -18.718 10.031 1.00104.41 C ANISOU 990 CG1 VAL A 161 14942 14429 10299 -1390 3 824 C ATOM 991 CG2 VAL A 161 20.766 -17.139 10.092 1.00104.82 C ANISOU 991 CG2 VAL A 161 15472 13866 10489 -1795 -164 532 C ATOM 992 N ILE A 162 21.232 -14.845 7.886 1.00119.80 N ANISOU 992 N ILE A 162 17494 15693 12332 -2311 -145 531 N ATOM 993 CA ILE A 162 20.521 -13.940 6.988 1.00119.61 C ANISOU 993 CA ILE A 162 17745 15371 12331 -2444 -146 441 C ATOM 994 C ILE A 162 21.483 -13.349 5.970 1.00117.47 C ANISOU 994 C ILE A 162 17369 15283 11980 -2620 -78 546 C ATOM 995 O ILE A 162 21.073 -12.963 4.868 1.00116.14 O ANISOU 995 O ILE A 162 17389 14919 11821 -2622 -22 512 O ATOM 996 CB ILE A 162 19.781 -12.842 7.777 1.00119.15 C ANISOU 996 CB ILE A 162 17928 15074 12270 -2676 -276 325 C ATOM 997 CG1 ILE A 162 20.771 -11.860 8.407 1.00126.97 C ANISOU 997 CG1 ILE A 162 18822 16275 13145 -3055 -361 384 C ATOM 998 CG2 ILE A 162 18.872 -13.454 8.825 1.00118.45 C ANISOU 998 CG2 ILE A 162 17909 14847 12249 -2497 -329 237 C ATOM 999 CD1 ILE A 162 20.111 -10.658 9.042 1.00127.49 C ANISOU 999 CD1 ILE A 162 19211 16061 13170 -3295 -466 269 C ATOM 1000 N ALA A 163 22.771 -13.267 6.310 1.00 79.23 N ANISOU 1000 N ALA A 163 12214 10846 7045 -2774 -81 685 N ATOM 1001 CA ALA A 163 23.768 -12.893 5.316 1.00 78.76 C ANISOU 1001 CA ALA A 163 11993 11033 6900 -2914 10 814 C ATOM 1002 C ALA A 163 23.959 -14.008 4.298 1.00 82.37 C ANISOU 1002 C ALA A 163 12352 11570 7373 -2532 181 886 C ATOM 1003 O ALA A 163 24.096 -13.746 3.098 1.00 84.77 O ANISOU 1003 O ALA A 163 12721 11837 7650 -2546 281 917 O ATOM 1004 CB ALA A 163 25.091 -12.550 5.997 1.00 81.28 C ANISOU 1004 CB ALA A 163 11955 11831 7096 -3194 -45 959 C ATOM 1005 N ALA A 164 23.959 -15.262 4.758 1.00 97.33 N ANISOU 1005 N ALA A 164 14132 13553 9296 -2182 227 912 N ATOM 1006 CA ALA A 164 24.064 -16.388 3.838 1.00 97.36 C ANISOU 1006 CA ALA A 164 14128 13571 9292 -1794 401 965 C ATOM 1007 C ALA A 164 22.781 -16.584 3.043 1.00 92.20 C ANISOU 1007 C ALA A 164 13855 12455 8721 -1667 426 808 C ATOM 1008 O ALA A 164 22.833 -16.993 1.878 1.00 96.30 O ANISOU 1008 O ALA A 164 14453 12927 9208 -1494 560 831 O ATOM 1009 CB ALA A 164 24.416 -17.663 4.603 1.00 94.86 C ANISOU 1009 CB ALA A 164 13645 13443 8956 -1450 450 1041 C ATOM 1010 N THR A 165 21.625 -16.304 3.649 1.00 93.19 N ANISOU 1010 N THR A 165 14210 12264 8935 -1748 301 655 N ATOM 1011 CA THR A 165 20.367 -16.424 2.920 1.00 86.08 C ANISOU 1011 CA THR A 165 13629 10983 8095 -1657 306 518 C ATOM 1012 C THR A 165 20.286 -15.403 1.792 1.00 94.11 C ANISOU 1012 C THR A 165 14778 11899 9079 -1835 319 507 C ATOM 1013 O THR A 165 19.848 -15.730 0.684 1.00 95.56 O ANISOU 1013 O THR A 165 15124 11932 9254 -1695 395 473 O ATOM 1014 CB THR A 165 19.182 -16.260 3.871 1.00 90.53 C ANISOU 1014 CB THR A 165 14360 11297 8742 -1707 172 380 C ATOM 1015 OG1 THR A 165 19.344 -17.135 4.994 1.00 97.15 O ANISOU 1015 OG1 THR A 165 15073 12244 9597 -1568 160 403 O ATOM 1016 CG2 THR A 165 17.879 -16.592 3.161 1.00 87.04 C ANISOU 1016 CG2 THR A 165 14186 10540 8345 -1585 178 258 C ATOM 1017 N TRP A 166 20.712 -14.165 2.051 1.00103.29 N ANISOU 1017 N TRP A 166 15904 13135 10208 -2154 248 537 N ATOM 1018 CA TRP A 166 20.664 -13.141 1.014 1.00100.62 C ANISOU 1018 CA TRP A 166 15729 12681 9821 -2333 270 538 C ATOM 1019 C TRP A 166 21.763 -13.348 -0.022 1.00106.94 C ANISOU 1019 C TRP A 166 16354 13741 10536 -2302 420 679 C ATOM 1020 O TRP A 166 21.547 -13.121 -1.217 1.00108.19 O ANISOU 1020 O TRP A 166 16675 13773 10661 -2271 493 674 O ATOM 1021 CB TRP A 166 20.770 -11.751 1.642 1.00 99.64 C ANISOU 1021 CB TRP A 166 15687 12511 9659 -2704 160 524 C ATOM 1022 CG TRP A 166 19.466 -11.224 2.164 1.00100.60 C ANISOU 1022 CG TRP A 166 16106 12283 9833 -2710 47 378 C ATOM 1023 CD1 TRP A 166 18.951 -11.404 3.414 1.00 98.90 C ANISOU 1023 CD1 TRP A 166 15898 12010 9671 -2682 -51 305 C ATOM 1024 CD2 TRP A 166 18.512 -10.429 1.448 1.00102.60 C ANISOU 1024 CD2 TRP A 166 16687 12222 10074 -2717 33 302 C ATOM 1025 NE1 TRP A 166 17.736 -10.771 3.522 1.00 94.79 N ANISOU 1025 NE1 TRP A 166 15675 11171 9170 -2664 -117 191 N ATOM 1026 CE2 TRP A 166 17.444 -10.165 2.329 1.00100.71 C ANISOU 1026 CE2 TRP A 166 16623 11766 9878 -2674 -70 191 C ATOM 1027 CE3 TRP A 166 18.458 -9.916 0.148 1.00102.20 C ANISOU 1027 CE3 TRP A 166 16799 12067 9965 -2735 102 328 C ATOM 1028 CZ2 TRP A 166 16.335 -9.411 1.952 1.00100.36 C ANISOU 1028 CZ2 TRP A 166 16890 11429 9815 -2623 -102 115 C ATOM 1029 CZ3 TRP A 166 17.355 -9.167 -0.224 1.00 99.60 C ANISOU 1029 CZ3 TRP A 166 16794 11432 9619 -2695 60 248 C ATOM 1030 CH2 TRP A 166 16.309 -8.922 0.675 1.00 99.07 C ANISOU 1030 CH2 TRP A 166 16877 11175 9590 -2628 -40 147 C ATOM 1031 N CYS A 167 22.947 -13.785 0.415 1.00117.65 N ANISOU 1031 N CYS A 167 17371 15489 11843 -2291 472 817 N ATOM 1032 CA CYS A 167 24.056 -13.974 -0.515 1.00121.35 C ANISOU 1032 CA CYS A 167 17628 16267 12212 -2242 631 976 C ATOM 1033 C CYS A 167 23.795 -15.143 -1.458 1.00120.08 C ANISOU 1033 C CYS A 167 17565 16014 12047 -1834 780 967 C ATOM 1034 O CYS A 167 23.944 -15.014 -2.679 1.00120.84 O ANISOU 1034 O CYS A 167 17748 16085 12080 -1796 894 1002 O ATOM 1035 CB CYS A 167 25.359 -14.186 0.255 1.00124.67 C ANISOU 1035 CB CYS A 167 17622 17187 12561 -2300 646 1142 C ATOM 1036 SG CYS A 167 26.819 -14.400 -0.789 1.00145.83 S ANISOU 1036 SG CYS A 167 19962 20351 15094 -2227 855 1374 S ATOM 1037 N LEU A 168 23.405 -16.296 -0.908 1.00108.06 N ANISOU 1037 N LEU A 168 16063 14424 10570 -1535 786 920 N ATOM 1038 CA LEU A 168 23.181 -17.470 -1.746 1.00109.65 C ANISOU 1038 CA LEU A 168 16412 14512 10737 -1164 933 905 C ATOM 1039 C LEU A 168 21.933 -17.325 -2.608 1.00109.54 C ANISOU 1039 C LEU A 168 16773 14088 10759 -1172 897 747 C ATOM 1040 O LEU A 168 21.852 -17.934 -3.680 1.00112.48 O ANISOU 1040 O LEU A 168 17301 14372 11063 -967 1021 741 O ATOM 1041 CB LEU A 168 23.089 -18.729 -0.882 1.00110.91 C ANISOU 1041 CB LEU A 168 16546 14678 10915 -871 953 899 C ATOM 1042 CG LEU A 168 24.405 -19.433 -0.533 1.00118.94 C ANISOU 1042 CG LEU A 168 17236 16122 11834 -635 1083 1091 C ATOM 1043 CD1 LEU A 168 25.232 -18.628 0.460 1.00121.69 C ANISOU 1043 CD1 LEU A 168 17215 16842 12178 -907 976 1199 C ATOM 1044 CD2 LEU A 168 24.137 -20.832 0.002 1.00113.19 C ANISOU 1044 CD2 LEU A 168 16625 15285 11097 -265 1146 1071 C ATOM 1045 N SER A 169 20.956 -16.530 -2.167 1.00100.26 N ANISOU 1045 N SER A 169 15748 12676 9669 -1391 731 624 N ATOM 1046 CA SER A 169 19.763 -16.321 -2.981 1.00 96.81 C ANISOU 1046 CA SER A 169 15625 11910 9247 -1391 685 494 C ATOM 1047 C SER A 169 20.093 -15.549 -4.252 1.00 97.02 C ANISOU 1047 C SER A 169 15726 11946 9190 -1489 757 547 C ATOM 1048 O SER A 169 19.535 -15.831 -5.319 1.00100.61 O ANISOU 1048 O SER A 169 16396 12234 9597 -1370 801 492 O ATOM 1049 CB SER A 169 18.694 -15.591 -2.173 1.00 97.72 C ANISOU 1049 CB SER A 169 15858 11819 9452 -1562 507 377 C ATOM 1050 OG SER A 169 18.140 -16.442 -1.184 1.00 96.18 O ANISOU 1050 OG SER A 169 15653 11564 9326 -1442 452 310 O ATOM 1051 N PHE A 170 20.993 -14.568 -4.157 1.00103.98 N ANISOU 1051 N PHE A 170 16445 13025 10036 -1728 766 655 N ATOM 1052 CA PHE A 170 21.429 -13.855 -5.352 1.00103.52 C ANISOU 1052 CA PHE A 170 16449 12999 9883 -1835 856 727 C ATOM 1053 C PHE A 170 22.271 -14.747 -6.256 1.00102.72 C ANISOU 1053 C PHE A 170 16239 13105 9685 -1593 1054 834 C ATOM 1054 O PHE A 170 22.272 -14.563 -7.478 1.00108.88 O ANISOU 1054 O PHE A 170 17166 13822 10382 -1558 1146 852 O ATOM 1055 CB PHE A 170 22.215 -12.603 -4.962 1.00104.24 C ANISOU 1055 CB PHE A 170 16409 13256 9942 -2202 822 821 C ATOM 1056 CG PHE A 170 21.348 -11.430 -4.599 1.00104.72 C ANISOU 1056 CG PHE A 170 16726 13026 10037 -2440 673 721 C ATOM 1057 CD1 PHE A 170 20.509 -10.854 -5.538 1.00106.70 C ANISOU 1057 CD1 PHE A 170 17294 12992 10255 -2427 662 658 C ATOM 1058 CD2 PHE A 170 21.379 -10.898 -3.320 1.00103.57 C ANISOU 1058 CD2 PHE A 170 16522 12895 9933 -2653 549 697 C ATOM 1059 CE1 PHE A 170 19.712 -9.773 -5.207 1.00106.65 C ANISOU 1059 CE1 PHE A 170 17545 12722 10256 -2587 544 582 C ATOM 1060 CE2 PHE A 170 20.584 -9.819 -2.983 1.00106.84 C ANISOU 1060 CE2 PHE A 170 17217 13023 10353 -2832 433 609 C ATOM 1061 CZ PHE A 170 19.750 -9.256 -3.927 1.00107.60 C ANISOU 1061 CZ PHE A 170 17632 12837 10414 -2781 438 556 C ATOM 1062 N THR A 171 22.984 -15.715 -5.677 1.00 93.33 N ANISOU 1062 N THR A 171 14811 12161 8489 -1396 1131 911 N ATOM 1063 CA THR A 171 23.818 -16.610 -6.471 1.00 88.07 C ANISOU 1063 CA THR A 171 14054 11702 7708 -1105 1343 1026 C ATOM 1064 C THR A 171 22.997 -17.725 -7.108 1.00 87.62 C ANISOU 1064 C THR A 171 14313 11355 7625 -790 1400 909 C ATOM 1065 O THR A 171 23.257 -18.114 -8.252 1.00 95.19 O ANISOU 1065 O THR A 171 15389 12312 8466 -610 1557 945 O ATOM 1066 CB THR A 171 24.930 -17.199 -5.602 1.00 89.86 C ANISOU 1066 CB THR A 171 13907 12328 7907 -975 1414 1175 C ATOM 1067 OG1 THR A 171 25.568 -16.150 -4.864 1.00102.23 O ANISOU 1067 OG1 THR A 171 15192 14157 9492 -1336 1317 1261 O ATOM 1068 CG2 THR A 171 25.966 -17.904 -6.464 1.00 97.27 C ANISOU 1068 CG2 THR A 171 14710 13554 8696 -673 1659 1336 C ATOM 1069 N ILE A 172 22.006 -18.249 -6.386 1.00 89.42 N ANISOU 1069 N ILE A 172 14694 11338 7944 -740 1278 768 N ATOM 1070 CA ILE A 172 21.174 -19.317 -6.933 1.00 89.63 C ANISOU 1070 CA ILE A 172 15041 11084 7929 -509 1315 649 C ATOM 1071 C ILE A 172 20.323 -18.795 -8.085 1.00 89.57 C ANISOU 1071 C ILE A 172 15311 10838 7883 -614 1268 551 C ATOM 1072 O ILE A 172 20.176 -19.462 -9.117 1.00 86.64 O ANISOU 1072 O ILE A 172 15171 10354 7396 -438 1374 519 O ATOM 1073 CB ILE A 172 20.309 -19.940 -5.821 1.00 86.28 C ANISOU 1073 CB ILE A 172 14693 10485 7606 -486 1190 534 C ATOM 1074 CG1 ILE A 172 21.168 -20.814 -4.906 1.00 96.42 C ANISOU 1074 CG1 ILE A 172 15779 11980 8876 -269 1284 638 C ATOM 1075 CG2 ILE A 172 19.167 -20.752 -6.414 1.00 79.49 C ANISOU 1075 CG2 ILE A 172 14199 9298 6704 -392 1172 381 C ATOM 1076 CD1 ILE A 172 20.494 -21.177 -3.599 1.00 95.50 C ANISOU 1076 CD1 ILE A 172 15668 11750 8867 -303 1151 556 C ATOM 1077 N MET A 173 19.764 -17.594 -7.939 1.00 92.41 N ANISOU 1077 N MET A 173 15675 11118 8318 -887 1114 507 N ATOM 1078 CA MET A 173 18.898 -17.008 -8.954 1.00 90.39 C ANISOU 1078 CA MET A 173 15672 10654 8017 -971 1052 426 C ATOM 1079 C MET A 173 19.670 -16.289 -10.057 1.00 92.60 C ANISOU 1079 C MET A 173 15946 11049 8190 -1026 1172 538 C ATOM 1080 O MET A 173 19.109 -15.405 -10.717 1.00 94.18 O ANISOU 1080 O MET A 173 16311 11114 8361 -1155 1105 505 O ATOM 1081 CB MET A 173 17.900 -16.051 -8.302 1.00 89.64 C ANISOU 1081 CB MET A 173 15622 10412 8027 -1182 850 341 C ATOM 1082 CG MET A 173 16.972 -16.729 -7.309 1.00 84.38 C ANISOU 1082 CG MET A 173 14979 9627 7454 -1137 731 226 C ATOM 1083 SD MET A 173 15.463 -17.332 -8.088 1.00 99.05 S ANISOU 1083 SD MET A 173 17136 11244 9256 -1064 645 73 S ATOM 1084 CE MET A 173 14.832 -18.410 -6.806 1.00 87.93 C ANISOU 1084 CE MET A 173 15693 9776 7940 -1016 574 -15 C ATOM 1085 N THR A 174 20.936 -16.648 -10.265 1.00 86.38 N ANISOU 1085 N THR A 174 14969 10523 7330 -915 1355 679 N ATOM 1086 CA THR A 174 21.713 -16.040 -11.340 1.00 85.00 C ANISOU 1086 CA THR A 174 14773 10486 7036 -964 1493 799 C ATOM 1087 C THR A 174 21.180 -16.341 -12.743 1.00 92.85 C ANISOU 1087 C THR A 174 16089 11289 7902 -822 1556 737 C ATOM 1088 O THR A 174 21.303 -15.455 -13.607 1.00 94.96 O ANISOU 1088 O THR A 174 16433 11551 8095 -949 1587 787 O ATOM 1089 CB THR A 174 23.183 -16.475 -11.215 1.00 86.34 C ANISOU 1089 CB THR A 174 14625 11039 7140 -839 1687 981 C ATOM 1090 OG1 THR A 174 23.640 -16.236 -9.878 1.00 98.32 O ANISOU 1090 OG1 THR A 174 15838 12759 8761 -981 1606 1036 O ATOM 1091 CG2 THR A 174 24.062 -15.693 -12.175 1.00 93.68 C ANISOU 1091 CG2 THR A 174 15469 12172 7954 -955 1828 1129 C ATOM 1092 N PRO A 175 20.617 -17.519 -13.050 1.00 89.69 N ANISOU 1092 N PRO A 175 15906 10724 7448 -585 1580 632 N ATOM 1093 CA PRO A 175 20.077 -17.731 -14.407 1.00 89.93 C ANISOU 1093 CA PRO A 175 16264 10575 7331 -495 1619 564 C ATOM 1094 C PRO A 175 19.017 -16.727 -14.835 1.00 92.41 C ANISOU 1094 C PRO A 175 16749 10703 7659 -698 1440 481 C ATOM 1095 O PRO A 175 18.793 -16.577 -16.042 1.00 93.76 O ANISOU 1095 O PRO A 175 17140 10795 7691 -662 1480 470 O ATOM 1096 CB PRO A 175 19.492 -19.148 -14.348 1.00 83.24 C ANISOU 1096 CB PRO A 175 15640 9552 6437 -285 1625 439 C ATOM 1097 CG PRO A 175 20.110 -19.803 -13.190 1.00 83.83 C ANISOU 1097 CG PRO A 175 15495 9762 6594 -172 1680 493 C ATOM 1098 CD PRO A 175 20.740 -18.786 -12.302 1.00 90.13 C ANISOU 1098 CD PRO A 175 15927 10794 7526 -366 1628 606 C ATOM 1099 N TYR A 176 18.352 -16.036 -13.901 1.00 95.55 N ANISOU 1099 N TYR A 176 17068 11034 8201 -883 1252 430 N ATOM 1100 CA TYR A 176 17.271 -15.140 -14.311 1.00 91.97 C ANISOU 1100 CA TYR A 176 16798 10411 7737 -1008 1092 361 C ATOM 1101 C TYR A 176 17.787 -13.896 -15.028 1.00 96.44 C ANISOU 1101 C TYR A 176 17392 11018 8231 -1137 1153 475 C ATOM 1102 O TYR A 176 17.262 -13.577 -16.109 1.00 98.97 O ANISOU 1102 O TYR A 176 17943 11231 8430 -1109 1136 454 O ATOM 1103 CB TYR A 176 16.386 -14.796 -13.108 1.00 88.65 C ANISOU 1103 CB TYR A 176 16309 9907 7468 -1120 897 280 C ATOM 1104 CG TYR A 176 15.150 -15.660 -13.003 1.00 84.36 C ANISOU 1104 CG TYR A 176 15896 9230 6927 -1041 769 133 C ATOM 1105 CD1 TYR A 176 13.983 -15.316 -13.671 1.00 85.83 C ANISOU 1105 CD1 TYR A 176 16269 9304 7038 -1055 637 59 C ATOM 1106 CD2 TYR A 176 15.152 -16.821 -12.242 1.00 91.17 C ANISOU 1106 CD2 TYR A 176 16695 10098 7848 -960 782 78 C ATOM 1107 CE1 TYR A 176 12.851 -16.102 -13.584 1.00 84.38 C ANISOU 1107 CE1 TYR A 176 16173 9049 6838 -1030 513 -66 C ATOM 1108 CE2 TYR A 176 14.023 -17.615 -12.147 1.00 90.24 C ANISOU 1108 CE2 TYR A 176 16709 9862 7717 -941 670 -53 C ATOM 1109 CZ TYR A 176 12.876 -17.250 -12.821 1.00 88.38 C ANISOU 1109 CZ TYR A 176 16626 9548 7406 -995 531 -125 C ATOM 1110 OH TYR A 176 11.750 -18.035 -12.731 1.00 97.89 O ANISOU 1110 OH TYR A 176 17930 10685 8579 -1020 410 -246 O ATOM 1111 N PRO A 177 18.779 -13.154 -14.516 1.00111.05 N ANISOU 1111 N PRO A 177 19038 13025 10132 -1300 1220 599 N ATOM 1112 CA PRO A 177 19.320 -12.036 -15.310 1.00111.76 C ANISOU 1112 CA PRO A 177 19196 13146 10123 -1450 1303 715 C ATOM 1113 C PRO A 177 20.026 -12.479 -16.580 1.00117.71 C ANISOU 1113 C PRO A 177 20003 14008 10715 -1310 1503 796 C ATOM 1114 O PRO A 177 20.152 -11.672 -17.510 1.00121.61 O ANISOU 1114 O PRO A 177 20647 14465 11095 -1392 1560 864 O ATOM 1115 CB PRO A 177 20.299 -11.344 -14.350 1.00114.77 C ANISOU 1115 CB PRO A 177 19318 13708 10582 -1694 1330 825 C ATOM 1116 CG PRO A 177 20.504 -12.280 -13.224 1.00117.34 C ANISOU 1116 CG PRO A 177 19400 14159 11024 -1606 1304 792 C ATOM 1117 CD PRO A 177 19.295 -13.142 -13.136 1.00112.60 C ANISOU 1117 CD PRO A 177 18961 13356 10466 -1406 1189 630 C ATOM 1118 N ILE A 178 20.489 -13.727 -16.653 1.00106.23 N ANISOU 1118 N ILE A 178 18460 12673 9231 -1086 1624 795 N ATOM 1119 CA ILE A 178 21.224 -14.185 -17.827 1.00102.61 C ANISOU 1119 CA ILE A 178 18062 12327 8599 -916 1841 879 C ATOM 1120 C ILE A 178 20.272 -14.512 -18.970 1.00 99.90 C ANISOU 1120 C ILE A 178 18086 11753 8120 -780 1801 766 C ATOM 1121 O ILE A 178 20.445 -14.035 -20.098 1.00101.95 O ANISOU 1121 O ILE A 178 18501 12004 8232 -783 1890 826 O ATOM 1122 CB ILE A 178 22.105 -15.397 -17.468 1.00100.83 C ANISOU 1122 CB ILE A 178 17639 12311 8360 -679 2007 934 C ATOM 1123 CG1 ILE A 178 23.031 -15.062 -16.299 1.00106.71 C ANISOU 1123 CG1 ILE A 178 17984 13336 9224 -823 2022 1055 C ATOM 1124 CG2 ILE A 178 22.908 -15.851 -18.677 1.00 96.51 C ANISOU 1124 CG2 ILE A 178 17162 11895 7613 -465 2259 1034 C ATOM 1125 CD1 ILE A 178 23.827 -16.247 -15.797 1.00107.13 C ANISOU 1125 CD1 ILE A 178 17826 13614 9265 -552 2166 1119 C ATOM 1126 N TYR A 179 19.253 -15.327 -18.699 1.00 97.42 N ANISOU 1126 N TYR A 179 17916 11262 7837 -681 1664 604 N ATOM 1127 CA TYR A 179 18.359 -15.838 -19.731 1.00 94.03 C ANISOU 1127 CA TYR A 179 17821 10650 7255 -569 1614 487 C ATOM 1128 C TYR A 179 17.037 -15.078 -19.793 1.00 95.10 C ANISOU 1128 C TYR A 179 18097 10624 7414 -706 1373 395 C ATOM 1129 O TYR A 179 15.993 -15.672 -20.084 1.00 94.90 O ANISOU 1129 O TYR A 179 18263 10472 7324 -659 1244 260 O ATOM 1130 CB TYR A 179 18.110 -17.330 -19.514 1.00 95.80 C ANISOU 1130 CB TYR A 179 18152 10800 7449 -388 1635 374 C ATOM 1131 CG TYR A 179 19.354 -18.179 -19.660 1.00101.03 C ANISOU 1131 CG TYR A 179 18751 11608 8029 -161 1900 471 C ATOM 1132 CD1 TYR A 179 19.751 -18.656 -20.903 1.00 98.82 C ANISOU 1132 CD1 TYR A 179 18707 11317 7524 26 2084 494 C ATOM 1133 CD2 TYR A 179 20.131 -18.503 -18.555 1.00101.08 C ANISOU 1133 CD2 TYR A 179 18464 11780 8161 -107 1973 548 C ATOM 1134 CE1 TYR A 179 20.887 -19.430 -21.042 1.00 97.24 C ANISOU 1134 CE1 TYR A 179 18454 11267 7227 286 2348 598 C ATOM 1135 CE2 TYR A 179 21.269 -19.278 -18.685 1.00104.16 C ANISOU 1135 CE2 TYR A 179 18777 12345 8455 151 2225 658 C ATOM 1136 CZ TYR A 179 21.642 -19.739 -19.930 1.00101.64 C ANISOU 1136 CZ TYR A 179 18697 12010 7911 360 2419 686 C ATOM 1137 OH TYR A 179 22.774 -20.510 -20.065 1.00105.19 O ANISOU 1137 OH TYR A 179 19075 12648 8244 667 2690 810 O ATOM 1138 N SER A 180 17.060 -13.774 -19.529 1.00 95.32 N ANISOU 1138 N SER A 180 18045 10662 7512 -874 1314 472 N ATOM 1139 CA SER A 180 15.888 -12.918 -19.671 1.00 99.32 C ANISOU 1139 CA SER A 180 18699 11030 8007 -948 1118 419 C ATOM 1140 C SER A 180 16.181 -11.877 -20.740 1.00100.46 C ANISOU 1140 C SER A 180 19007 11156 8007 -988 1195 529 C ATOM 1141 O SER A 180 17.130 -11.097 -20.608 1.00 98.36 O ANISOU 1141 O SER A 180 18646 10962 7766 -1116 1316 660 O ATOM 1142 CB SER A 180 15.524 -12.243 -18.347 1.00 94.11 C ANISOU 1142 CB SER A 180 17880 10343 7533 -1083 979 408 C ATOM 1143 OG SER A 180 14.819 -13.132 -17.499 1.00 92.90 O ANISOU 1143 OG SER A 180 17644 10170 7484 -1038 858 285 O ATOM 1144 N ASN A 181 15.370 -11.867 -21.795 1.00110.29 N ANISOU 1144 N ASN A 181 20503 12317 9086 -897 1123 481 N ATOM 1145 CA ASN A 181 15.562 -10.951 -22.907 1.00114.48 C ANISOU 1145 CA ASN A 181 21232 12814 9450 -905 1196 584 C ATOM 1146 C ASN A 181 14.207 -10.428 -23.364 1.00112.07 C ANISOU 1146 C ASN A 181 21133 12403 9047 -850 993 529 C ATOM 1147 O ASN A 181 13.154 -10.869 -22.895 1.00106.57 O ANISOU 1147 O ASN A 181 20400 11692 8398 -810 805 412 O ATOM 1148 CB ASN A 181 16.304 -11.627 -24.067 1.00118.71 C ANISOU 1148 CB ASN A 181 21878 13419 9808 -792 1393 620 C ATOM 1149 CG ASN A 181 17.781 -11.816 -23.781 1.00120.64 C ANISOU 1149 CG ASN A 181 21905 13826 10108 -827 1631 738 C ATOM 1150 OD1 ASN A 181 18.510 -10.850 -23.551 1.00119.36 O ANISOU 1150 OD1 ASN A 181 21635 13726 9989 -990 1715 872 O ATOM 1151 ND2 ASN A 181 18.231 -13.066 -23.790 1.00112.93 N ANISOU 1151 ND2 ASN A 181 20870 12928 9109 -675 1744 697 N ATOM 1152 N LEU A 182 14.247 -9.472 -24.288 1.00 92.51 N ANISOU 1152 N LEU A 182 18863 9871 6414 -843 1037 628 N ATOM 1153 CA LEU A 182 13.040 -8.881 -24.848 1.00 92.07 C ANISOU 1153 CA LEU A 182 19013 9744 6224 -747 862 611 C ATOM 1154 C LEU A 182 12.635 -9.643 -26.103 1.00 88.62 C ANISOU 1154 C LEU A 182 18753 9351 5566 -620 840 551 C ATOM 1155 O LEU A 182 13.456 -9.849 -27.002 1.00 95.64 O ANISOU 1155 O LEU A 182 19754 10259 6326 -599 1021 607 O ATOM 1156 CB LEU A 182 13.262 -7.403 -25.169 1.00 93.72 C ANISOU 1156 CB LEU A 182 19406 9845 6357 -792 923 757 C ATOM 1157 CG LEU A 182 13.052 -6.421 -24.015 1.00 92.28 C ANISOU 1157 CG LEU A 182 19180 9561 6323 -883 855 790 C ATOM 1158 CD1 LEU A 182 13.284 -4.989 -24.472 1.00 89.72 C ANISOU 1158 CD1 LEU A 182 19134 9083 5874 -929 936 936 C ATOM 1159 CD2 LEU A 182 11.660 -6.579 -23.424 1.00 95.01 C ANISOU 1159 CD2 LEU A 182 19470 9915 6715 -752 618 687 C ATOM 1160 N VAL A 183 11.374 -10.058 -26.160 1.00 87.80 N ANISOU 1160 N VAL A 183 18673 9284 5403 -549 620 442 N ATOM 1161 CA VAL A 183 10.844 -10.832 -27.275 1.00 89.11 C ANISOU 1161 CA VAL A 183 19014 9504 5340 -471 554 363 C ATOM 1162 C VAL A 183 9.976 -9.899 -28.120 1.00 90.64 C ANISOU 1162 C VAL A 183 19395 9713 5332 -367 423 428 C ATOM 1163 O VAL A 183 8.901 -9.478 -27.668 1.00 90.25 O ANISOU 1163 O VAL A 183 19270 9715 5304 -322 221 415 O ATOM 1164 CB VAL A 183 10.045 -12.049 -26.792 1.00 88.15 C ANISOU 1164 CB VAL A 183 18789 9447 5256 -510 392 196 C ATOM 1165 CG1 VAL A 183 9.381 -12.747 -27.967 1.00 89.93 C ANISOU 1165 CG1 VAL A 183 19234 9729 5207 -477 293 110 C ATOM 1166 CG2 VAL A 183 10.951 -13.011 -26.039 1.00 86.99 C ANISOU 1166 CG2 VAL A 183 18509 9268 5275 -569 544 144 C ATOM 1167 N PRO A 184 10.394 -9.547 -29.334 1.00 93.79 N ANISOU 1167 N PRO A 184 20033 10084 5519 -304 536 511 N ATOM 1168 CA PRO A 184 9.578 -8.655 -30.163 1.00 94.32 C ANISOU 1168 CA PRO A 184 20295 10170 5371 -176 414 587 C ATOM 1169 C PRO A 184 8.319 -9.345 -30.663 1.00 95.10 C ANISOU 1169 C PRO A 184 20416 10427 5289 -119 167 475 C ATOM 1170 O PRO A 184 8.284 -10.561 -30.867 1.00 95.08 O ANISOU 1170 O PRO A 184 20411 10477 5238 -194 143 341 O ATOM 1171 CB PRO A 184 10.513 -8.298 -31.325 1.00 96.26 C ANISOU 1171 CB PRO A 184 20791 10348 5437 -147 632 698 C ATOM 1172 CG PRO A 184 11.896 -8.593 -30.802 1.00 95.39 C ANISOU 1172 CG PRO A 184 20550 10186 5507 -273 881 725 C ATOM 1173 CD PRO A 184 11.704 -9.808 -29.952 1.00 93.56 C ANISOU 1173 CD PRO A 184 20098 10014 5435 -327 804 568 C ATOM 1174 N PHE A 185 7.274 -8.544 -30.863 1.00100.49 N ANISOU 1174 N PHE A 185 21135 11195 5853 13 -16 537 N ATOM 1175 CA PHE A 185 6.008 -9.045 -31.378 1.00104.66 C ANISOU 1175 CA PHE A 185 21648 11942 6175 58 -275 459 C ATOM 1176 C PHE A 185 5.219 -7.879 -31.954 1.00108.24 C ANISOU 1176 C PHE A 185 22185 12479 6463 277 -390 596 C ATOM 1177 O PHE A 185 5.461 -6.716 -31.620 1.00106.68 O ANISOU 1177 O PHE A 185 22067 12145 6320 390 -299 733 O ATOM 1178 CB PHE A 185 5.208 -9.778 -30.291 1.00 97.40 C ANISOU 1178 CB PHE A 185 20431 11157 5419 -46 -456 334 C ATOM 1179 CG PHE A 185 4.339 -8.879 -29.454 1.00 97.36 C ANISOU 1179 CG PHE A 185 20245 11240 5506 81 -595 410 C ATOM 1180 CD1 PHE A 185 4.853 -8.251 -28.332 1.00100.50 C ANISOU 1180 CD1 PHE A 185 20546 11475 6164 82 -476 462 C ATOM 1181 CD2 PHE A 185 3.001 -8.689 -29.767 1.00 99.96 C ANISOU 1181 CD2 PHE A 185 20497 11839 5643 204 -843 433 C ATOM 1182 CE1 PHE A 185 4.059 -7.431 -27.552 1.00107.05 C ANISOU 1182 CE1 PHE A 185 21254 12364 7058 224 -584 530 C ATOM 1183 CE2 PHE A 185 2.202 -7.869 -28.992 1.00103.66 C ANISOU 1183 CE2 PHE A 185 20802 12407 6178 372 -948 517 C ATOM 1184 CZ PHE A 185 2.732 -7.241 -27.883 1.00109.46 C ANISOU 1184 CZ PHE A 185 21486 12932 7170 391 -811 561 C ATOM 1185 N THR A 186 4.271 -8.208 -32.828 1.00101.42 N ANISOU 1185 N THR A 186 21291 11841 5403 332 -587 559 N ATOM 1186 CA THR A 186 3.427 -7.222 -33.489 1.00103.80 C ANISOU 1186 CA THR A 186 21628 12282 5529 572 -713 690 C ATOM 1187 C THR A 186 2.028 -7.250 -32.889 1.00104.13 C ANISOU 1187 C THR A 186 21424 12627 5515 650 -990 679 C ATOM 1188 O THR A 186 1.461 -8.324 -32.662 1.00105.38 O ANISOU 1188 O THR A 186 21404 12984 5651 471 -1154 540 O ATOM 1189 CB THR A 186 3.350 -7.481 -34.995 1.00106.44 C ANISOU 1189 CB THR A 186 22090 12711 5643 598 -741 682 C ATOM 1190 OG1 THR A 186 3.004 -8.852 -35.229 1.00107.99 O ANISOU 1190 OG1 THR A 186 22192 13066 5774 392 -870 507 O ATOM 1191 CG2 THR A 186 4.687 -7.181 -35.655 1.00106.64 C ANISOU 1191 CG2 THR A 186 22361 12459 5697 585 -453 740 C ATOM 1192 N LYS A 187 1.474 -6.064 -32.641 1.00152.93 N ANISOU 1192 N LYS A 187 27602 18843 11661 918 -1032 833 N ATOM 1193 CA LYS A 187 0.164 -5.950 -32.012 1.00150.68 C ANISOU 1193 CA LYS A 187 27065 18872 11314 1054 -1270 859 C ATOM 1194 C LYS A 187 -0.933 -5.706 -33.042 1.00161.55 C ANISOU 1194 C LYS A 187 28363 20608 12412 1251 -1476 939 C ATOM 1195 O LYS A 187 -1.659 -6.633 -33.415 1.00167.63 O ANISOU 1195 O LYS A 187 28946 21707 13040 1099 -1686 842 O ATOM 1196 CB LYS A 187 0.168 -4.830 -30.970 1.00148.25 C ANISOU 1196 CB LYS A 187 26792 18399 11137 1268 -1182 981 C ATOM 1197 CG LYS A 187 -0.966 -4.918 -29.962 1.00153.49 C ANISOU 1197 CG LYS A 187 27135 19348 11835 1362 -1375 977 C ATOM 1198 CD LYS A 187 -0.834 -3.859 -28.877 1.00148.51 C ANISOU 1198 CD LYS A 187 26547 18494 11386 1555 -1246 1075 C ATOM 1199 CE LYS A 187 0.539 -3.898 -28.225 1.00135.74 C ANISOU 1199 CE LYS A 187 25056 16460 10059 1308 -1002 1006 C ATOM 1200 NZ LYS A 187 0.629 -2.971 -27.063 1.00133.15 N ANISOU 1200 NZ LYS A 187 24767 15922 9903 1436 -899 1074 N ATOM 1201 N ASN A 188 -1.063 -4.464 -33.506 1.00175.89 N ANISOU 1201 N ASN A 188 30324 22367 14138 1572 -1416 1117 N ATOM 1202 CA ASN A 188 -2.138 -4.073 -34.411 1.00172.85 C ANISOU 1202 CA ASN A 188 29849 22343 13483 1819 -1604 1228 C ATOM 1203 C ASN A 188 -1.551 -3.311 -35.589 1.00170.84 C ANISOU 1203 C ASN A 188 29906 21877 13129 1960 -1449 1332 C ATOM 1204 O ASN A 188 -0.963 -2.240 -35.404 1.00177.20 O ANISOU 1204 O ASN A 188 30952 22345 14032 2128 -1244 1445 O ATOM 1205 CB ASN A 188 -3.180 -3.215 -33.687 1.00178.41 C ANISOU 1205 CB ASN A 188 30376 23261 14151 2168 -1709 1373 C ATOM 1206 CG ASN A 188 -3.973 -4.002 -32.663 1.00187.83 C ANISOU 1206 CG ASN A 188 31211 24773 15384 2045 -1904 1285 C ATOM 1207 OD1 ASN A 188 -4.142 -5.215 -32.790 1.00189.07 O ANISOU 1207 OD1 ASN A 188 31205 25134 15500 1719 -2046 1130 O ATOM 1208 ND2 ASN A 188 -4.462 -3.314 -31.637 1.00188.08 N ANISOU 1208 ND2 ASN A 188 31136 24835 15492 2302 -1900 1381 N ATOM 1209 N ASN A 189 -1.715 -3.863 -36.793 1.00132.12 N ANISOU 1209 N ASN A 189 25012 17166 8023 1872 -1546 1291 N ATOM 1210 CA ASN A 189 -1.292 -3.219 -38.037 1.00126.51 C ANISOU 1210 CA ASN A 189 24575 16318 7175 2009 -1430 1390 C ATOM 1211 C ASN A 189 0.210 -2.928 -38.028 1.00122.01 C ANISOU 1211 C ASN A 189 24320 15243 6797 1891 -1109 1381 C ATOM 1212 O ASN A 189 0.654 -1.790 -38.194 1.00122.88 O ANISOU 1212 O ASN A 189 24672 15088 6930 2077 -934 1519 O ATOM 1213 CB ASN A 189 -2.102 -1.944 -38.295 1.00127.00 C ANISOU 1213 CB ASN A 189 24659 16506 7090 2433 -1483 1601 C ATOM 1214 CG ASN A 189 -2.457 -1.764 -39.756 1.00130.68 C ANISOU 1214 CG ASN A 189 25209 17167 7276 2557 -1564 1677 C ATOM 1215 OD1 ASN A 189 -2.407 -2.712 -40.540 1.00135.35 O ANISOU 1215 OD1 ASN A 189 25767 17916 7742 2323 -1655 1562 O ATOM 1216 ND2 ASN A 189 -2.817 -0.542 -40.131 1.00135.25 N ANISOU 1216 ND2 ASN A 189 25920 17721 7746 2932 -1526 1867 N ATOM 1217 N ASN A 190 0.989 -3.995 -37.836 1.00116.70 N ANISOU 1217 N ASN A 190 23637 14454 6250 1567 -1031 1217 N ATOM 1218 CA ASN A 190 2.451 -3.922 -37.806 1.00114.98 C ANISOU 1218 CA ASN A 190 23648 13837 6202 1416 -733 1202 C ATOM 1219 C ASN A 190 2.929 -2.944 -36.732 1.00113.36 C ANISOU 1219 C ASN A 190 23520 13350 6201 1482 -570 1295 C ATOM 1220 O ASN A 190 3.778 -2.082 -36.971 1.00113.86 O ANISOU 1220 O ASN A 190 23830 13122 6309 1513 -348 1397 O ATOM 1221 CB ASN A 190 3.012 -3.554 -39.184 1.00117.35 C ANISOU 1221 CB ASN A 190 24207 14030 6351 1476 -599 1274 C ATOM 1222 CG ASN A 190 4.503 -3.825 -39.303 1.00115.94 C ANISOU 1222 CG ASN A 190 24199 13547 6307 1271 -312 1235 C ATOM 1223 OD1 ASN A 190 5.136 -4.303 -38.362 1.00113.23 O ANISOU 1223 OD1 ASN A 190 23776 13080 6168 1086 -212 1157 O ATOM 1224 ND2 ASN A 190 5.069 -3.519 -40.466 1.00118.01 N ANISOU 1224 ND2 ASN A 190 24682 13712 6443 1313 -173 1301 N ATOM 1225 N GLN A 191 2.364 -3.081 -35.535 1.00135.89 N ANISOU 1225 N GLN A 191 26168 16295 9170 1483 -684 1258 N ATOM 1226 CA GLN A 191 2.771 -2.282 -34.381 1.00132.03 C ANISOU 1226 CA GLN A 191 25744 15545 8877 1513 -548 1321 C ATOM 1227 C GLN A 191 3.806 -3.081 -33.601 1.00120.07 C ANISOU 1227 C GLN A 191 24179 13864 7577 1191 -411 1198 C ATOM 1228 O GLN A 191 3.462 -3.992 -32.845 1.00122.76 O ANISOU 1228 O GLN A 191 24295 14352 7996 1063 -532 1075 O ATOM 1229 CB GLN A 191 1.571 -1.927 -33.512 1.00135.53 C ANISOU 1229 CB GLN A 191 25999 16187 9310 1733 -734 1362 C ATOM 1230 CG GLN A 191 1.681 -0.577 -32.821 1.00139.74 C ANISOU 1230 CG GLN A 191 26719 16447 9927 1935 -601 1497 C ATOM 1231 CD GLN A 191 0.351 -0.087 -32.281 1.00143.69 C ANISOU 1231 CD GLN A 191 27060 17187 10348 2269 -778 1575 C ATOM 1232 OE1 GLN A 191 -0.693 -0.693 -32.522 1.00149.14 O ANISOU 1232 OE1 GLN A 191 27473 18296 10898 2352 -1013 1550 O ATOM 1233 NE2 GLN A 191 0.384 1.017 -31.544 1.00143.60 N ANISOU 1233 NE2 GLN A 191 27222 16923 10416 2455 -660 1671 N ATOM 1234 N THR A 192 5.079 -2.743 -33.786 1.00120.49 N ANISOU 1234 N THR A 192 24432 13630 7717 1058 -154 1239 N ATOM 1235 CA THR A 192 6.142 -3.458 -33.095 1.00126.83 C ANISOU 1235 CA THR A 192 25172 14310 8706 775 -4 1148 C ATOM 1236 C THR A 192 6.096 -3.174 -31.597 1.00127.46 C ANISOU 1236 C THR A 192 25158 14301 8971 726 -9 1144 C ATOM 1237 O THR A 192 5.897 -2.035 -31.165 1.00129.94 O ANISOU 1237 O THR A 192 25592 14472 9307 860 19 1254 O ATOM 1238 CB THR A 192 7.508 -3.083 -33.678 1.00127.48 C ANISOU 1238 CB THR A 192 25456 14169 8812 648 276 1222 C ATOM 1239 OG1 THR A 192 8.541 -3.802 -32.991 1.00133.91 O ANISOU 1239 OG1 THR A 192 26167 14921 9790 397 425 1152 O ATOM 1240 CG2 THR A 192 7.765 -1.581 -33.575 1.00128.97 C ANISOU 1240 CG2 THR A 192 25870 14118 9014 728 401 1381 C ATOM 1241 N ALA A 193 6.260 -4.230 -30.803 1.00131.54 N ANISOU 1241 N ALA A 193 25478 14891 9612 542 -42 1012 N ATOM 1242 CA ALA A 193 6.224 -4.119 -29.353 1.00129.95 C ANISOU 1242 CA ALA A 193 25072 14630 9672 471 -54 974 C ATOM 1243 C ALA A 193 7.031 -5.260 -28.752 1.00124.55 C ANISOU 1243 C ALA A 193 24158 13947 9217 212 27 838 C ATOM 1244 O ALA A 193 7.113 -6.350 -29.324 1.00127.28 O ANISOU 1244 O ALA A 193 24454 14408 9499 138 6 738 O ATOM 1245 CB ALA A 193 4.788 -4.140 -28.816 1.00123.53 C ANISOU 1245 CB ALA A 193 24063 14032 8839 650 -305 944 C ATOM 1246 N ASN A 194 7.625 -4.998 -27.594 1.00 93.37 N ANISOU 1246 N ASN A 194 20096 9865 5515 85 124 838 N ATOM 1247 CA ASN A 194 8.470 -5.965 -26.914 1.00 91.35 C ANISOU 1247 CA ASN A 194 19620 9611 5478 -131 218 736 C ATOM 1248 C ASN A 194 7.770 -6.502 -25.672 1.00 89.38 C ANISOU 1248 C ASN A 194 19085 9454 5422 -155 65 626 C ATOM 1249 O ASN A 194 6.886 -5.861 -25.099 1.00 89.41 O ANISOU 1249 O ASN A 194 19058 9476 5439 -30 -61 654 O ATOM 1250 CB ASN A 194 9.815 -5.338 -26.529 1.00 91.18 C ANISOU 1250 CB ASN A 194 19653 9411 5580 -297 452 826 C ATOM 1251 CG ASN A 194 10.788 -5.290 -27.690 1.00 92.84 C ANISOU 1251 CG ASN A 194 20051 9586 5638 -346 648 908 C ATOM 1252 OD1 ASN A 194 11.951 -4.921 -27.527 1.00 93.10 O ANISOU 1252 OD1 ASN A 194 20095 9538 5742 -511 848 988 O ATOM 1253 ND2 ASN A 194 10.317 -5.665 -28.872 1.00 94.20 N ANISOU 1253 ND2 ASN A 194 20363 9844 5584 -213 590 892 N ATOM 1254 N MET A 195 8.172 -7.704 -25.268 1.00 88.03 N ANISOU 1254 N MET A 195 18721 9342 5385 -297 90 508 N ATOM 1255 CA MET A 195 7.710 -8.289 -24.021 1.00 86.10 C ANISOU 1255 CA MET A 195 18212 9163 5340 -358 -18 406 C ATOM 1256 C MET A 195 8.883 -8.969 -23.333 1.00 84.76 C ANISOU 1256 C MET A 195 17905 8931 5368 -526 144 364 C ATOM 1257 O MET A 195 9.810 -9.454 -23.986 1.00 85.15 O ANISOU 1257 O MET A 195 18026 8962 5366 -574 300 372 O ATOM 1258 CB MET A 195 6.560 -9.285 -24.236 1.00 86.27 C ANISOU 1258 CB MET A 195 18128 9382 5270 -336 -224 288 C ATOM 1259 CG MET A 195 6.816 -10.353 -25.283 1.00 89.37 C ANISOU 1259 CG MET A 195 18634 9819 5505 -397 -194 210 C ATOM 1260 SD MET A 195 5.336 -11.339 -25.595 1.00 98.59 S ANISOU 1260 SD MET A 195 19723 11228 6508 -431 -469 81 S ATOM 1261 CE MET A 195 5.921 -12.451 -26.871 1.00 89.57 C ANISOU 1261 CE MET A 195 18834 10043 5156 -514 -376 -5 C ATOM 1262 N CYS A 196 8.837 -8.986 -22.004 1.00 97.61 N ANISOU 1262 N CYS A 196 19334 10545 7209 -591 111 329 N ATOM 1263 CA CYS A 196 9.912 -9.525 -21.180 1.00 94.70 C ANISOU 1263 CA CYS A 196 18804 10145 7031 -731 248 307 C ATOM 1264 C CYS A 196 9.551 -10.956 -20.797 1.00 93.04 C ANISOU 1264 C CYS A 196 18443 10025 6882 -759 175 168 C ATOM 1265 O CYS A 196 8.638 -11.179 -19.996 1.00 98.92 O ANISOU 1265 O CYS A 196 19051 10825 7709 -760 22 99 O ATOM 1266 CB CYS A 196 10.130 -8.649 -19.946 1.00 99.00 C ANISOU 1266 CB CYS A 196 19258 10609 7749 -800 258 355 C ATOM 1267 SG CYS A 196 11.200 -9.347 -18.668 1.00105.24 S ANISOU 1267 SG CYS A 196 19785 11424 8779 -963 364 320 S ATOM 1268 N ARG A 197 10.263 -11.922 -21.377 1.00 81.74 N ANISOU 1268 N ARG A 197 17061 8603 5394 -777 298 134 N ATOM 1269 CA ARG A 197 10.003 -13.336 -21.150 1.00 82.28 C ANISOU 1269 CA ARG A 197 17080 8708 5476 -805 260 4 C ATOM 1270 C ARG A 197 11.282 -14.041 -20.725 1.00 84.46 C ANISOU 1270 C ARG A 197 17277 8958 5856 -823 463 16 C ATOM 1271 O ARG A 197 12.373 -13.705 -21.196 1.00 82.79 O ANISOU 1271 O ARG A 197 17102 8743 5610 -799 649 116 O ATOM 1272 CB ARG A 197 9.439 -14.009 -22.409 1.00 81.89 C ANISOU 1272 CB ARG A 197 17246 8687 5181 -772 199 -68 C ATOM 1273 CG ARG A 197 8.113 -13.444 -22.880 1.00 82.72 C ANISOU 1273 CG ARG A 197 17395 8884 5149 -742 -21 -74 C ATOM 1274 CD ARG A 197 6.953 -14.158 -22.210 1.00 82.99 C ANISOU 1274 CD ARG A 197 17290 9024 5218 -825 -222 -188 C ATOM 1275 NE ARG A 197 5.664 -13.646 -22.656 1.00 84.67 N ANISOU 1275 NE ARG A 197 17491 9398 5280 -781 -438 -176 N ATOM 1276 CZ ARG A 197 5.057 -12.589 -22.135 1.00 86.84 C ANISOU 1276 CZ ARG A 197 17638 9743 5616 -683 -531 -95 C ATOM 1277 NH1 ARG A 197 5.601 -11.897 -21.146 1.00 83.15 N ANISOU 1277 NH1 ARG A 197 17072 9168 5355 -653 -436 -32 N ATOM 1278 NH2 ARG A 197 3.876 -12.215 -22.619 1.00 90.61 N ANISOU 1278 NH2 ARG A 197 18094 10412 5921 -605 -722 -71 N ATOM 1279 N PHE A 198 11.139 -15.021 -19.835 1.00 78.75 N ANISOU 1279 N PHE A 198 16440 8236 5245 -856 433 -74 N ATOM 1280 CA PHE A 198 12.258 -15.847 -19.392 1.00 78.60 C ANISOU 1280 CA PHE A 198 16351 8212 5303 -825 618 -63 C ATOM 1281 C PHE A 198 12.363 -17.051 -20.321 1.00 80.09 C ANISOU 1281 C PHE A 198 16779 8350 5301 -747 703 -137 C ATOM 1282 O PHE A 198 11.462 -17.896 -20.358 1.00 80.21 O ANISOU 1282 O PHE A 198 16913 8320 5245 -793 581 -265 O ATOM 1283 CB PHE A 198 12.069 -16.288 -17.943 1.00 76.91 C ANISOU 1283 CB PHE A 198 15932 8004 5286 -879 555 -113 C ATOM 1284 CG PHE A 198 13.224 -17.079 -17.393 1.00 76.92 C ANISOU 1284 CG PHE A 198 15840 8025 5361 -813 740 -80 C ATOM 1285 CD1 PHE A 198 14.503 -16.548 -17.379 1.00 77.47 C ANISOU 1285 CD1 PHE A 198 15782 8184 5469 -783 914 57 C ATOM 1286 CD2 PHE A 198 13.030 -18.359 -16.898 1.00 76.71 C ANISOU 1286 CD2 PHE A 198 15857 7945 5346 -782 744 -174 C ATOM 1287 CE1 PHE A 198 15.566 -17.275 -16.875 1.00 77.84 C ANISOU 1287 CE1 PHE A 198 15704 8308 5562 -690 1083 109 C ATOM 1288 CE2 PHE A 198 14.090 -19.091 -16.394 1.00 77.02 C ANISOU 1288 CE2 PHE A 198 15823 8010 5430 -669 923 -127 C ATOM 1289 CZ PHE A 198 15.359 -18.548 -16.383 1.00 77.60 C ANISOU 1289 CZ PHE A 198 15728 8216 5540 -606 1091 19 C ATOM 1290 N LEU A 199 13.460 -17.130 -21.069 1.00 96.53 N ANISOU 1290 N LEU A 199 18949 10446 7283 -639 920 -56 N ATOM 1291 CA LEU A 199 13.660 -18.188 -22.050 1.00 98.74 C ANISOU 1291 CA LEU A 199 19512 10659 7347 -530 1035 -116 C ATOM 1292 C LEU A 199 15.021 -18.835 -21.841 1.00100.56 C ANISOU 1292 C LEU A 199 19690 10924 7593 -369 1302 -39 C ATOM 1293 O LEU A 199 16.045 -18.146 -21.800 1.00102.55 O ANISOU 1293 O LEU A 199 19757 11303 7904 -331 1451 110 O ATOM 1294 CB LEU A 199 13.516 -17.641 -23.481 1.00 93.66 C ANISOU 1294 CB LEU A 199 19089 10013 6485 -503 1042 -86 C ATOM 1295 CG LEU A 199 14.205 -16.326 -23.865 1.00 94.23 C ANISOU 1295 CG LEU A 199 19065 10166 6574 -498 1137 77 C ATOM 1296 CD1 LEU A 199 15.617 -16.536 -24.389 1.00104.70 C ANISOU 1296 CD1 LEU A 199 20405 11554 7821 -365 1431 192 C ATOM 1297 CD2 LEU A 199 13.362 -15.568 -24.881 1.00 94.99 C ANISOU 1297 CD2 LEU A 199 19345 10243 6503 -527 998 75 C ATOM 1298 N LEU A 200 15.021 -20.149 -21.694 1.00 88.82 N ANISOU 1298 N LEU A 200 18371 9339 6039 -278 1365 -130 N ATOM 1299 CA LEU A 200 16.215 -20.961 -21.539 1.00 85.95 C ANISOU 1299 CA LEU A 200 18009 9003 5644 -57 1627 -62 C ATOM 1300 C LEU A 200 16.555 -21.635 -22.862 1.00 93.75 C ANISOU 1300 C LEU A 200 19370 9906 6346 120 1804 -81 C ATOM 1301 O LEU A 200 15.753 -21.623 -23.801 1.00 93.53 O ANISOU 1301 O LEU A 200 19617 9775 6145 34 1692 -178 O ATOM 1302 CB LEU A 200 15.993 -21.996 -20.431 1.00 95.21 C ANISOU 1302 CB LEU A 200 19177 10087 6913 -37 1599 -144 C ATOM 1303 CG LEU A 200 16.264 -21.506 -19.003 1.00 86.42 C ANISOU 1303 CG LEU A 200 17659 9105 6071 -104 1544 -70 C ATOM 1304 CD1 LEU A 200 15.447 -22.292 -17.992 1.00 88.96 C ANISOU 1304 CD1 LEU A 200 18015 9302 6484 -188 1406 -193 C ATOM 1305 CD2 LEU A 200 17.746 -21.583 -18.664 1.00 87.66 C ANISOU 1305 CD2 LEU A 200 17594 9447 6265 101 1790 96 C ATOM 1306 N PRO A 201 17.768 -22.219 -22.990 1.00108.05 N ANISOU 1306 N PRO A 201 21197 11780 8077 388 2090 19 N ATOM 1307 CA PRO A 201 18.153 -22.851 -24.262 1.00109.01 C ANISOU 1307 CA PRO A 201 21698 11817 7902 596 2290 9 C ATOM 1308 C PRO A 201 17.136 -23.840 -24.814 1.00110.15 C ANISOU 1308 C PRO A 201 22334 11682 7836 539 2186 -196 C ATOM 1309 O PRO A 201 16.610 -23.633 -25.912 1.00119.36 O ANISOU 1309 O PRO A 201 23758 12782 8811 460 2115 -261 O ATOM 1310 CB PRO A 201 19.472 -23.544 -23.905 1.00107.88 C ANISOU 1310 CB PRO A 201 21466 11787 7737 924 2596 138 C ATOM 1311 CG PRO A 201 20.073 -22.627 -22.903 1.00106.60 C ANISOU 1311 CG PRO A 201 20766 11895 7842 837 2573 291 C ATOM 1312 CD PRO A 201 18.908 -22.181 -22.052 1.00106.67 C ANISOU 1312 CD PRO A 201 20662 11809 8059 526 2253 173 C ATOM 1313 N ASN A 202 16.848 -24.907 -24.079 1.00110.33 N ANISOU 1313 N ASN A 202 22506 11543 7871 559 2171 -298 N ATOM 1314 CA ASN A 202 15.909 -25.924 -24.529 1.00114.83 C ANISOU 1314 CA ASN A 202 23571 11837 8222 453 2077 -496 C ATOM 1315 C ASN A 202 14.808 -26.120 -23.495 1.00104.27 C ANISOU 1315 C ASN A 202 22138 10430 7050 169 1812 -615 C ATOM 1316 O ASN A 202 14.856 -25.583 -22.386 1.00105.27 O ANISOU 1316 O ASN A 202 21847 10697 7455 110 1732 -545 O ATOM 1317 CB ASN A 202 16.622 -27.253 -24.813 1.00112.94 C ANISOU 1317 CB ASN A 202 23675 11404 7833 758 2339 -503 C ATOM 1318 CG ASN A 202 17.501 -27.706 -23.662 1.00114.55 C ANISOU 1318 CG ASN A 202 23745 11668 8111 1009 2541 -404 C ATOM 1319 OD1 ASN A 202 17.043 -27.839 -22.525 1.00115.46 O ANISOU 1319 OD1 ASN A 202 23685 11763 8422 862 2397 -444 O ATOM 1320 ND2 ASN A 202 18.770 -27.962 -23.955 1.00112.41 N ANISOU 1320 ND2 ASN A 202 23454 11497 7760 1398 2852 -253 N ATOM 1321 N ASP A 203 13.800 -26.906 -23.880 1.00119.97 N ANISOU 1321 N ASP A 203 24462 12212 8908 -29 1661 -783 N ATOM 1322 CA ASP A 203 12.685 -27.167 -22.978 1.00119.55 C ANISOU 1322 CA ASP A 203 24342 12113 8968 -327 1416 -896 C ATOM 1323 C ASP A 203 13.094 -28.078 -21.829 1.00118.99 C ANISOU 1323 C ASP A 203 24322 11916 8974 -211 1548 -897 C ATOM 1324 O ASP A 203 12.472 -28.046 -20.763 1.00121.54 O ANISOU 1324 O ASP A 203 24452 12269 9460 -399 1391 -936 O ATOM 1325 CB ASP A 203 11.515 -27.778 -23.752 1.00125.51 C ANISOU 1325 CB ASP A 203 25331 12731 9627 -606 1209 -1031 C ATOM 1326 CG ASP A 203 10.859 -26.792 -24.695 1.00134.02 C ANISOU 1326 CG ASP A 203 26298 13983 10641 -757 1016 -1033 C ATOM 1327 OD1 ASP A 203 11.363 -25.656 -24.814 1.00137.27 O ANISOU 1327 OD1 ASP A 203 26501 14576 11079 -632 1062 -927 O ATOM 1328 OD2 ASP A 203 9.838 -27.153 -25.316 1.00136.15 O ANISOU 1328 OD2 ASP A 203 26694 14217 10819 -1006 821 -1129 O ATOM 1329 N VAL A 204 14.127 -28.897 -22.026 1.00 95.08 N ANISOU 1329 N VAL A 204 21514 8755 5858 119 1833 -837 N ATOM 1330 CA VAL A 204 14.610 -29.752 -20.947 1.00 95.20 C ANISOU 1330 CA VAL A 204 21584 8661 5927 294 1982 -812 C ATOM 1331 C VAL A 204 15.197 -28.904 -19.825 1.00 92.50 C ANISOU 1331 C VAL A 204 20695 8595 5855 382 1991 -667 C ATOM 1332 O VAL A 204 14.917 -29.129 -18.642 1.00 93.41 O ANISOU 1332 O VAL A 204 20647 8699 6144 297 1909 -677 O ATOM 1333 CB VAL A 204 15.632 -30.771 -21.484 1.00 98.49 C ANISOU 1333 CB VAL A 204 22321 8901 6200 689 2289 -744 C ATOM 1334 CG1 VAL A 204 16.423 -31.387 -20.340 1.00 98.56 C ANISOU 1334 CG1 VAL A 204 22293 8896 6259 984 2489 -656 C ATOM 1335 CG2 VAL A 204 14.926 -31.851 -22.288 1.00101.39 C ANISOU 1335 CG2 VAL A 204 23156 8928 6438 539 2226 -865 C ATOM 1336 N MET A 205 16.009 -27.907 -20.182 1.00 97.24 N ANISOU 1336 N MET A 205 20960 9452 6534 524 2074 -515 N ATOM 1337 CA MET A 205 16.551 -26.992 -19.185 1.00101.11 C ANISOU 1337 CA MET A 205 20880 10220 7318 540 2047 -366 C ATOM 1338 C MET A 205 15.471 -26.124 -18.551 1.00 99.06 C ANISOU 1338 C MET A 205 20331 10030 7276 181 1733 -427 C ATOM 1339 O MET A 205 15.674 -25.613 -17.444 1.00102.28 O ANISOU 1339 O MET A 205 20349 10590 7922 147 1677 -350 O ATOM 1340 CB MET A 205 17.626 -26.107 -19.819 1.00104.37 C ANISOU 1340 CB MET A 205 21043 10885 7726 712 2206 -193 C ATOM 1341 CG MET A 205 18.981 -26.783 -19.964 1.00102.76 C ANISOU 1341 CG MET A 205 20896 10756 7392 1131 2544 -55 C ATOM 1342 SD MET A 205 20.127 -25.824 -20.976 1.00107.84 S ANISOU 1342 SD MET A 205 21308 11703 7963 1289 2741 139 S ATOM 1343 CE MET A 205 20.872 -24.769 -19.734 1.00116.33 C ANISOU 1343 CE MET A 205 21690 13158 9351 1204 2696 325 C ATOM 1344 N GLN A 206 14.332 -25.949 -19.225 1.00 91.85 N ANISOU 1344 N GLN A 206 19601 9030 6268 -72 1531 -558 N ATOM 1345 CA GLN A 206 13.238 -25.165 -18.663 1.00 88.76 C ANISOU 1345 CA GLN A 206 18946 8727 6051 -369 1244 -606 C ATOM 1346 C GLN A 206 12.472 -25.959 -17.611 1.00 96.26 C ANISOU 1346 C GLN A 206 19938 9562 7076 -521 1130 -708 C ATOM 1347 O GLN A 206 12.211 -25.457 -16.512 1.00 96.08 O ANISOU 1347 O GLN A 206 19575 9649 7282 -614 1014 -676 O ATOM 1348 CB GLN A 206 12.296 -24.704 -19.777 1.00 85.94 C ANISOU 1348 CB GLN A 206 18740 8374 5540 -556 1069 -687 C ATOM 1349 CG GLN A 206 11.240 -23.705 -19.331 1.00 86.80 C ANISOU 1349 CG GLN A 206 18545 8629 5806 -789 795 -699 C ATOM 1350 CD GLN A 206 11.749 -22.277 -19.331 1.00 91.03 C ANISOU 1350 CD GLN A 206 18757 9343 6487 -723 803 -555 C ATOM 1351 OE1 GLN A 206 12.813 -21.988 -19.876 1.00 92.86 O ANISOU 1351 OE1 GLN A 206 18995 9612 6676 -550 995 -450 O ATOM 1352 NE2 GLN A 206 10.989 -21.376 -18.719 1.00 91.66 N ANISOU 1352 NE2 GLN A 206 18570 9533 6722 -863 604 -543 N ATOM 1353 N GLN A 207 12.105 -27.202 -17.929 1.00124.89 N ANISOU 1353 N GLN A 207 24008 12953 10492 -560 1170 -833 N ATOM 1354 CA GLN A 207 11.329 -28.006 -16.994 1.00127.18 C ANISOU 1354 CA GLN A 207 24384 13117 10822 -747 1068 -931 C ATOM 1355 C GLN A 207 12.172 -28.530 -15.838 1.00127.76 C ANISOU 1355 C GLN A 207 24365 13149 11029 -525 1239 -849 C ATOM 1356 O GLN A 207 11.614 -28.883 -14.794 1.00131.99 O ANISOU 1356 O GLN A 207 24829 13644 11676 -669 1144 -890 O ATOM 1357 CB GLN A 207 10.657 -29.167 -17.730 1.00123.77 C ANISOU 1357 CB GLN A 207 24509 12426 10091 -911 1054 -1094 C ATOM 1358 CG GLN A 207 11.622 -30.103 -18.433 1.00132.86 C ANISOU 1358 CG GLN A 207 26098 13352 11031 -615 1337 -1080 C ATOM 1359 CD GLN A 207 11.050 -30.664 -19.720 1.00140.14 C ANISOU 1359 CD GLN A 207 27330 14119 11799 -768 1272 -1151 C ATOM 1360 OE1 GLN A 207 10.139 -30.086 -20.312 1.00140.24 O ANISOU 1360 OE1 GLN A 207 27229 14262 11795 -1037 1045 -1204 O ATOM 1361 NE2 GLN A 207 11.583 -31.798 -20.159 1.00145.58 N ANISOU 1361 NE2 GLN A 207 28421 14535 12356 -583 1475 -1144 N ATOM 1362 N SER A 208 13.496 -28.591 -15.996 1.00 85.92 N ANISOU 1362 N SER A 208 19050 7888 5708 -171 1490 -722 N ATOM 1363 CA SER A 208 14.360 -28.965 -14.884 1.00 85.60 C ANISOU 1363 CA SER A 208 18847 7885 5792 69 1642 -613 C ATOM 1364 C SER A 208 14.659 -27.788 -13.964 1.00 87.29 C ANISOU 1364 C SER A 208 18478 8393 6297 34 1546 -493 C ATOM 1365 O SER A 208 15.129 -27.999 -12.841 1.00 90.16 O ANISOU 1365 O SER A 208 18648 8817 6790 149 1599 -419 O ATOM 1366 CB SER A 208 15.670 -29.561 -15.404 1.00 88.09 C ANISOU 1366 CB SER A 208 19362 8173 5937 489 1960 -507 C ATOM 1367 OG SER A 208 16.565 -28.546 -15.822 1.00 87.72 O ANISOU 1367 OG SER A 208 18963 8410 5957 630 2037 -358 O ATOM 1368 N TRP A 209 14.396 -26.561 -14.414 1.00 84.47 N ANISOU 1368 N TRP A 209 17869 8203 6021 -120 1408 -473 N ATOM 1369 CA TRP A 209 14.575 -25.386 -13.569 1.00 79.35 C ANISOU 1369 CA TRP A 209 16739 7789 5621 -197 1304 -376 C ATOM 1370 C TRP A 209 13.364 -25.165 -12.671 1.00 78.65 C ANISOU 1370 C TRP A 209 16527 7678 5678 -466 1062 -469 C ATOM 1371 O TRP A 209 13.507 -24.984 -11.457 1.00 84.29 O ANISOU 1371 O TRP A 209 16980 8475 6570 -473 1027 -421 O ATOM 1372 CB TRP A 209 14.832 -24.155 -14.440 1.00 80.95 C ANISOU 1372 CB TRP A 209 16786 8147 5824 -234 1283 -306 C ATOM 1373 CG TRP A 209 14.857 -22.856 -13.691 1.00 77.98 C ANISOU 1373 CG TRP A 209 16004 7959 5666 -366 1158 -229 C ATOM 1374 CD1 TRP A 209 13.918 -21.867 -13.738 1.00 77.79 C ANISOU 1374 CD1 TRP A 209 15886 7958 5712 -578 951 -272 C ATOM 1375 CD2 TRP A 209 15.882 -22.393 -12.801 1.00 76.61 C ANISOU 1375 CD2 TRP A 209 15495 7976 5639 -291 1238 -91 C ATOM 1376 NE1 TRP A 209 14.289 -20.822 -12.927 1.00 76.16 N ANISOU 1376 NE1 TRP A 209 15355 7898 5683 -638 908 -180 N ATOM 1377 CE2 TRP A 209 15.492 -21.118 -12.342 1.00 74.92 C ANISOU 1377 CE2 TRP A 209 15039 7853 5576 -493 1071 -73 C ATOM 1378 CE3 TRP A 209 17.089 -22.933 -12.346 1.00 77.71 C ANISOU 1378 CE3 TRP A 209 15516 8236 5775 -66 1433 25 C ATOM 1379 CZ2 TRP A 209 16.264 -20.377 -11.449 1.00 74.31 C ANISOU 1379 CZ2 TRP A 209 14636 7956 5641 -527 1085 41 C ATOM 1380 CZ3 TRP A 209 17.855 -22.195 -11.460 1.00 77.09 C ANISOU 1380 CZ3 TRP A 209 15057 8390 5844 -96 1434 150 C ATOM 1381 CH2 TRP A 209 17.438 -20.932 -11.020 1.00 75.40 C ANISOU 1381 CH2 TRP A 209 14635 8237 5775 -349 1257 149 C ATOM 1382 N HIS A 210 12.162 -25.183 -13.253 1.00103.77 N ANISOU 1382 N HIS A 210 19882 10776 8770 -686 893 -593 N ATOM 1383 CA HIS A 210 10.952 -25.005 -12.457 1.00106.08 C ANISOU 1383 CA HIS A 210 20040 11091 9175 -931 672 -669 C ATOM 1384 C HIS A 210 10.729 -26.172 -11.504 1.00102.00 C ANISOU 1384 C HIS A 210 19656 10432 8669 -959 703 -726 C ATOM 1385 O HIS A 210 10.112 -25.998 -10.447 1.00102.80 O ANISOU 1385 O HIS A 210 19551 10590 8918 -1092 577 -739 O ATOM 1386 CB HIS A 210 9.743 -24.821 -13.374 1.00104.80 C ANISOU 1386 CB HIS A 210 20013 10929 8877 -1149 489 -771 C ATOM 1387 CG HIS A 210 9.830 -23.610 -14.249 1.00106.59 C ANISOU 1387 CG HIS A 210 20119 11290 9089 -1120 442 -710 C ATOM 1388 ND1 HIS A 210 9.696 -22.328 -13.761 1.00109.70 N ANISOU 1388 ND1 HIS A 210 20184 11843 9653 -1141 341 -634 N ATOM 1389 CD2 HIS A 210 10.039 -23.485 -15.581 1.00104.84 C ANISOU 1389 CD2 HIS A 210 20100 11048 8685 -1067 492 -711 C ATOM 1390 CE1 HIS A 210 9.819 -21.466 -14.754 1.00104.87 C ANISOU 1390 CE1 HIS A 210 19586 11294 8966 -1103 334 -586 C ATOM 1391 NE2 HIS A 210 10.027 -22.142 -15.869 1.00100.35 N ANISOU 1391 NE2 HIS A 210 19317 10628 8185 -1059 421 -630 N ATOM 1392 N THR A 211 11.216 -27.364 -11.858 1.00 92.83 N ANISOU 1392 N THR A 211 18865 9072 7336 -825 879 -754 N ATOM 1393 CA THR A 211 11.183 -28.477 -10.916 1.00 92.55 C ANISOU 1393 CA THR A 211 18994 8873 7297 -805 948 -784 C ATOM 1394 C THR A 211 12.171 -28.253 -9.779 1.00 94.33 C ANISOU 1394 C THR A 211 18912 9223 7707 -578 1052 -648 C ATOM 1395 O THR A 211 11.874 -28.561 -8.619 1.00102.44 O ANISOU 1395 O THR A 211 19849 10230 8842 -637 1006 -653 O ATOM 1396 CB THR A 211 11.484 -29.790 -11.639 1.00 98.12 C ANISOU 1396 CB THR A 211 20245 9300 7735 -686 1132 -845 C ATOM 1397 OG1 THR A 211 10.505 -30.010 -12.663 1.00 93.90 O ANISOU 1397 OG1 THR A 211 20007 8662 7010 -953 1009 -983 O ATOM 1398 CG2 THR A 211 11.458 -30.958 -10.662 1.00101.71 C ANISOU 1398 CG2 THR A 211 20930 9550 8166 -653 1219 -867 C ATOM 1399 N PHE A 212 13.347 -27.705 -10.094 1.00 82.34 N ANISOU 1399 N PHE A 212 17217 7857 6212 -333 1188 -520 N ATOM 1400 CA PHE A 212 14.332 -27.400 -9.062 1.00 83.67 C ANISOU 1400 CA PHE A 212 17047 8208 6535 -147 1268 -378 C ATOM 1401 C PHE A 212 13.803 -26.361 -8.081 1.00 80.80 C ANISOU 1401 C PHE A 212 16295 8005 6401 -361 1064 -371 C ATOM 1402 O PHE A 212 14.022 -26.472 -6.869 1.00 78.14 O ANISOU 1402 O PHE A 212 15778 7727 6183 -322 1058 -323 O ATOM 1403 CB PHE A 212 15.628 -26.920 -9.716 1.00 79.97 C ANISOU 1403 CB PHE A 212 16434 7925 6025 95 1437 -236 C ATOM 1404 CG PHE A 212 16.620 -26.337 -8.751 1.00 80.09 C ANISOU 1404 CG PHE A 212 16022 8213 6194 209 1477 -81 C ATOM 1405 CD1 PHE A 212 17.313 -27.149 -7.869 1.00 85.04 C ANISOU 1405 CD1 PHE A 212 16624 8873 6816 448 1607 2 C ATOM 1406 CD2 PHE A 212 16.865 -24.974 -8.734 1.00 78.00 C ANISOU 1406 CD2 PHE A 212 15403 8175 6059 68 1383 -12 C ATOM 1407 CE1 PHE A 212 18.229 -26.610 -6.985 1.00 88.05 C ANISOU 1407 CE1 PHE A 212 16590 9548 7316 531 1626 149 C ATOM 1408 CE2 PHE A 212 17.779 -24.430 -7.853 1.00 81.17 C ANISOU 1408 CE2 PHE A 212 15426 8838 6577 117 1406 125 C ATOM 1409 CZ PHE A 212 18.462 -25.249 -6.978 1.00 88.37 C ANISOU 1409 CZ PHE A 212 16274 9822 7482 342 1519 206 C ATOM 1410 N LEU A 213 13.094 -25.348 -8.584 1.00 76.52 N ANISOU 1410 N LEU A 213 15644 7529 5903 -567 900 -415 N ATOM 1411 CA LEU A 213 12.570 -24.299 -7.712 1.00 76.57 C ANISOU 1411 CA LEU A 213 15329 7668 6098 -735 723 -406 C ATOM 1412 C LEU A 213 11.422 -24.812 -6.853 1.00 81.13 C ANISOU 1412 C LEU A 213 15947 8155 6723 -904 592 -504 C ATOM 1413 O LEU A 213 11.373 -24.545 -5.647 1.00 83.48 O ANISOU 1413 O LEU A 213 16026 8527 7167 -932 537 -474 O ATOM 1414 CB LEU A 213 12.132 -23.094 -8.543 1.00 71.53 C ANISOU 1414 CB LEU A 213 14610 7109 5459 -857 607 -413 C ATOM 1415 CG LEU A 213 13.187 -21.998 -8.704 1.00 74.10 C ANISOU 1415 CG LEU A 213 14714 7597 5843 -785 674 -285 C ATOM 1416 CD1 LEU A 213 14.401 -22.523 -9.443 1.00 76.15 C ANISOU 1416 CD1 LEU A 213 15069 7882 5982 -574 892 -204 C ATOM 1417 CD2 LEU A 213 12.601 -20.796 -9.425 1.00 77.62 C ANISOU 1417 CD2 LEU A 213 15133 8078 6280 -911 552 -294 C ATOM 1418 N LEU A 214 10.485 -25.549 -7.454 1.00 86.29 N ANISOU 1418 N LEU A 214 16882 8665 7240 -1039 540 -619 N ATOM 1419 CA LEU A 214 9.409 -26.144 -6.667 1.00 89.44 C ANISOU 1419 CA LEU A 214 17326 8997 7659 -1230 432 -703 C ATOM 1420 C LEU A 214 9.954 -27.082 -5.598 1.00 91.50 C ANISOU 1420 C LEU A 214 17653 9158 7954 -1109 557 -669 C ATOM 1421 O LEU A 214 9.331 -27.253 -4.544 1.00 89.01 O ANISOU 1421 O LEU A 214 17245 8849 7727 -1228 478 -691 O ATOM 1422 CB LEU A 214 8.439 -26.892 -7.582 1.00 89.21 C ANISOU 1422 CB LEU A 214 17620 8840 7434 -1430 370 -826 C ATOM 1423 CG LEU A 214 7.300 -26.078 -8.198 1.00 95.16 C ANISOU 1423 CG LEU A 214 18249 9745 8164 -1641 163 -876 C ATOM 1424 CD1 LEU A 214 6.645 -26.858 -9.329 1.00 90.76 C ANISOU 1424 CD1 LEU A 214 18040 9081 7365 -1818 125 -985 C ATOM 1425 CD2 LEU A 214 6.277 -25.697 -7.141 1.00 85.41 C ANISOU 1425 CD2 LEU A 214 16742 8651 7058 -1807 3 -885 C ATOM 1426 N LEU A 215 11.117 -27.686 -5.847 1.00 98.99 N ANISOU 1426 N LEU A 215 18759 10031 8823 -848 759 -604 N ATOM 1427 CA LEU A 215 11.713 -28.605 -4.885 1.00 95.50 C ANISOU 1427 CA LEU A 215 18400 9501 8383 -672 895 -551 C ATOM 1428 C LEU A 215 12.491 -27.863 -3.803 1.00 96.90 C ANISOU 1428 C LEU A 215 18172 9903 8744 -543 894 -427 C ATOM 1429 O LEU A 215 12.408 -28.220 -2.623 1.00100.70 O ANISOU 1429 O LEU A 215 18588 10375 9298 -536 884 -408 O ATOM 1430 CB LEU A 215 12.612 -29.604 -5.617 1.00 98.67 C ANISOU 1430 CB LEU A 215 19162 9742 8586 -397 1128 -520 C ATOM 1431 CG LEU A 215 13.315 -30.718 -4.839 1.00102.41 C ANISOU 1431 CG LEU A 215 19822 10094 8997 -130 1314 -451 C ATOM 1432 CD1 LEU A 215 13.366 -31.980 -5.678 1.00113.06 C ANISOU 1432 CD1 LEU A 215 21747 11130 10080 -15 1486 -512 C ATOM 1433 CD2 LEU A 215 14.725 -30.298 -4.457 1.00102.92 C ANISOU 1433 CD2 LEU A 215 19565 10411 9130 203 1440 -274 C ATOM 1434 N ILE A 216 13.247 -26.827 -4.179 1.00 82.64 N ANISOU 1434 N ILE A 216 16102 8300 6998 -467 900 -341 N ATOM 1435 CA ILE A 216 14.110 -26.137 -3.222 1.00 78.11 C ANISOU 1435 CA ILE A 216 15164 7954 6562 -376 903 -219 C ATOM 1436 C ILE A 216 13.426 -24.963 -2.536 1.00 79.99 C ANISOU 1436 C ILE A 216 15128 8301 6965 -608 704 -247 C ATOM 1437 O ILE A 216 13.936 -24.473 -1.516 1.00 86.97 O ANISOU 1437 O ILE A 216 15751 9338 7956 -589 678 -172 O ATOM 1438 CB ILE A 216 15.403 -25.646 -3.906 1.00 83.12 C ANISOU 1438 CB ILE A 216 15652 8777 7154 -195 1031 -93 C ATOM 1439 CG1 ILE A 216 16.531 -25.497 -2.882 1.00 87.35 C ANISOU 1439 CG1 ILE A 216 15880 9552 7757 -42 1093 53 C ATOM 1440 CG2 ILE A 216 15.165 -24.331 -4.634 1.00 75.55 C ANISOU 1440 CG2 ILE A 216 14554 7909 6243 -379 922 -107 C ATOM 1441 CD1 ILE A 216 17.882 -25.213 -3.496 1.00 90.13 C ANISOU 1441 CD1 ILE A 216 16067 10141 8038 148 1244 201 C ATOM 1442 N LEU A 217 12.284 -24.498 -3.045 1.00 77.15 N ANISOU 1442 N LEU A 217 14828 7878 6608 -813 565 -347 N ATOM 1443 CA LEU A 217 11.615 -23.337 -2.479 1.00 75.65 C ANISOU 1443 CA LEU A 217 14412 7785 6545 -980 397 -364 C ATOM 1444 C LEU A 217 10.257 -23.637 -1.865 1.00 72.04 C ANISOU 1444 C LEU A 217 13993 7261 6118 -1142 272 -458 C ATOM 1445 O LEU A 217 9.668 -22.738 -1.255 1.00 76.44 O ANISOU 1445 O LEU A 217 14370 7904 6771 -1238 149 -465 O ATOM 1446 CB LEU A 217 11.436 -22.244 -3.546 1.00 79.71 C ANISOU 1446 CB LEU A 217 14900 8350 7035 -1050 336 -366 C ATOM 1447 CG LEU A 217 12.686 -21.515 -4.043 1.00 72.24 C ANISOU 1447 CG LEU A 217 13844 7521 6082 -961 429 -259 C ATOM 1448 CD1 LEU A 217 12.286 -20.312 -4.878 1.00 72.33 C ANISOU 1448 CD1 LEU A 217 13848 7555 6079 -1062 344 -265 C ATOM 1449 CD2 LEU A 217 13.575 -21.097 -2.884 1.00 80.09 C ANISOU 1449 CD2 LEU A 217 14589 8661 7182 -935 448 -165 C ATOM 1450 N PHE A 218 9.738 -24.857 -2.003 1.00 88.23 N ANISOU 1450 N PHE A 218 16287 9164 8073 -1181 307 -527 N ATOM 1451 CA PHE A 218 8.393 -25.139 -1.516 1.00 86.10 C ANISOU 1451 CA PHE A 218 16035 8869 7810 -1382 186 -610 C ATOM 1452 C PHE A 218 8.287 -26.525 -0.890 1.00 88.26 C ANISOU 1452 C PHE A 218 16522 8984 8027 -1395 269 -637 C ATOM 1453 O PHE A 218 7.754 -26.668 0.215 1.00 91.31 O ANISOU 1453 O PHE A 218 16815 9392 8485 -1476 220 -643 O ATOM 1454 CB PHE A 218 7.380 -24.991 -2.653 1.00 88.41 C ANISOU 1454 CB PHE A 218 16426 9168 7996 -1548 81 -689 C ATOM 1455 CG PHE A 218 7.111 -23.564 -3.038 1.00 92.88 C ANISOU 1455 CG PHE A 218 16781 9893 8618 -1553 -30 -662 C ATOM 1456 CD1 PHE A 218 6.133 -22.830 -2.388 1.00 94.64 C ANISOU 1456 CD1 PHE A 218 16798 10246 8915 -1641 -166 -669 C ATOM 1457 CD2 PHE A 218 7.839 -22.954 -4.046 1.00 99.08 C ANISOU 1457 CD2 PHE A 218 17593 10690 9363 -1451 17 -622 C ATOM 1458 CE1 PHE A 218 5.885 -21.515 -2.736 1.00 98.75 C ANISOU 1458 CE1 PHE A 218 17178 10881 9460 -1606 -250 -636 C ATOM 1459 CE2 PHE A 218 7.597 -21.639 -4.400 1.00 97.53 C ANISOU 1459 CE2 PHE A 218 17254 10605 9199 -1452 -73 -591 C ATOM 1460 CZ PHE A 218 6.619 -20.919 -3.744 1.00101.15 C ANISOU 1460 CZ PHE A 218 17543 11168 9723 -1519 -205 -599 C ATOM 1461 N LEU A 219 8.783 -27.552 -1.582 1.00 94.26 N ANISOU 1461 N LEU A 219 17602 9570 8642 -1308 406 -652 N ATOM 1462 CA LEU A 219 8.664 -28.913 -1.066 1.00 90.32 C ANISOU 1462 CA LEU A 219 17395 8869 8054 -1318 501 -679 C ATOM 1463 C LEU A 219 9.588 -29.132 0.126 1.00 93.04 C ANISOU 1463 C LEU A 219 17634 9234 8482 -1090 605 -576 C ATOM 1464 O LEU A 219 9.143 -29.539 1.206 1.00 95.02 O ANISOU 1464 O LEU A 219 17877 9450 8776 -1164 584 -580 O ATOM 1465 CB LEU A 219 8.960 -29.927 -2.172 1.00 93.23 C ANISOU 1465 CB LEU A 219 18201 9012 8211 -1261 635 -724 C ATOM 1466 CG LEU A 219 8.807 -31.390 -1.753 1.00 98.56 C ANISOU 1466 CG LEU A 219 19286 9414 8749 -1283 752 -760 C ATOM 1467 CD1 LEU A 219 7.344 -31.806 -1.774 1.00 98.62 C ANISOU 1467 CD1 LEU A 219 19435 9352 8684 -1690 617 -880 C ATOM 1468 CD2 LEU A 219 9.640 -32.301 -2.642 1.00106.20 C ANISOU 1468 CD2 LEU A 219 20687 10152 9511 -1055 956 -755 C ATOM 1469 N ILE A 220 10.886 -28.874 -0.054 1.00 80.30 N ANISOU 1469 N ILE A 220 15927 7706 6878 -813 718 -474 N ATOM 1470 CA ILE A 220 11.831 -29.036 1.053 1.00 79.74 C ANISOU 1470 CA ILE A 220 15711 7719 6867 -586 804 -359 C ATOM 1471 C ILE A 220 11.545 -28.063 2.193 1.00 82.20 C ANISOU 1471 C ILE A 220 15656 8220 7356 -701 656 -337 C ATOM 1472 O ILE A 220 11.509 -28.503 3.353 1.00 82.98 O ANISOU 1472 O ILE A 220 15736 8304 7488 -668 667 -308 O ATOM 1473 CB ILE A 220 13.277 -28.946 0.534 1.00 78.60 C ANISOU 1473 CB ILE A 220 15501 7692 6670 -279 953 -239 C ATOM 1474 CG1 ILE A 220 13.626 -30.191 -0.286 1.00 83.27 C ANISOU 1474 CG1 ILE A 220 16528 8055 7054 -81 1147 -245 C ATOM 1475 CG2 ILE A 220 14.253 -28.777 1.687 1.00 73.37 C ANISOU 1475 CG2 ILE A 220 14560 7234 6082 -83 991 -103 C ATOM 1476 CD1 ILE A 220 15.031 -30.179 -0.845 1.00 77.85 C ANISOU 1476 CD1 ILE A 220 15777 7512 6289 261 1320 -112 C ATOM 1477 N PRO A 221 11.329 -26.763 1.955 1.00 93.76 N ANISOU 1477 N PRO A 221 16860 9845 8919 -826 527 -348 N ATOM 1478 CA PRO A 221 10.927 -25.888 3.070 1.00 86.09 C ANISOU 1478 CA PRO A 221 15618 9005 8086 -937 395 -343 C ATOM 1479 C PRO A 221 9.600 -26.278 3.696 1.00 84.35 C ANISOU 1479 C PRO A 221 15469 8700 7882 -1123 313 -426 C ATOM 1480 O PRO A 221 9.324 -25.868 4.829 1.00 88.40 O ANISOU 1480 O PRO A 221 15809 9295 8485 -1165 245 -412 O ATOM 1481 CB PRO A 221 10.850 -24.499 2.420 1.00 90.41 C ANISOU 1481 CB PRO A 221 15988 9675 8687 -1027 295 -350 C ATOM 1482 CG PRO A 221 11.745 -24.587 1.240 1.00 89.31 C ANISOU 1482 CG PRO A 221 15931 9539 8464 -902 402 -308 C ATOM 1483 CD PRO A 221 11.563 -25.982 0.725 1.00 91.64 C ANISOU 1483 CD PRO A 221 16550 9640 8628 -839 511 -351 C ATOM 1484 N GLY A 222 8.775 -27.058 3.003 1.00 85.22 N ANISOU 1484 N GLY A 222 15827 8661 7890 -1252 318 -509 N ATOM 1485 CA GLY A 222 7.483 -27.450 3.529 1.00 78.56 C ANISOU 1485 CA GLY A 222 15029 7780 7041 -1472 241 -578 C ATOM 1486 C GLY A 222 7.551 -28.586 4.527 1.00 77.29 C ANISOU 1486 C GLY A 222 15036 7483 6846 -1442 335 -557 C ATOM 1487 O GLY A 222 6.888 -28.541 5.567 1.00 82.66 O ANISOU 1487 O GLY A 222 15605 8216 7587 -1547 278 -560 O ATOM 1488 N ILE A 223 8.345 -29.615 4.227 1.00 94.94 N ANISOU 1488 N ILE A 223 17561 9541 8969 -1278 491 -529 N ATOM 1489 CA ILE A 223 8.419 -30.757 5.131 1.00 98.33 C ANISOU 1489 CA ILE A 223 18216 9807 9338 -1223 599 -501 C ATOM 1490 C ILE A 223 9.269 -30.438 6.356 1.00 99.54 C ANISOU 1490 C ILE A 223 18135 10096 9591 -1000 624 -391 C ATOM 1491 O ILE A 223 8.993 -30.942 7.451 1.00101.63 O ANISOU 1491 O ILE A 223 18443 10311 9860 -1019 642 -369 O ATOM 1492 CB ILE A 223 8.940 -32.005 4.395 1.00 98.62 C ANISOU 1492 CB ILE A 223 18708 9576 9186 -1089 775 -504 C ATOM 1493 CG1 ILE A 223 10.324 -31.747 3.795 1.00107.71 C ANISOU 1493 CG1 ILE A 223 19803 10804 10319 -749 882 -415 C ATOM 1494 CG2 ILE A 223 7.951 -32.444 3.324 1.00 95.20 C ANISOU 1494 CG2 ILE A 223 18558 8990 8624 -1382 734 -629 C ATOM 1495 CD1 ILE A 223 11.028 -33.004 3.323 1.00102.97 C ANISOU 1495 CD1 ILE A 223 19649 9954 9520 -501 1097 -382 C ATOM 1496 N VAL A 224 10.301 -29.602 6.209 1.00 88.24 N ANISOU 1496 N VAL A 224 16453 8851 8225 -811 620 -316 N ATOM 1497 CA VAL A 224 11.120 -29.245 7.361 1.00 90.19 C ANISOU 1497 CA VAL A 224 16455 9269 8545 -641 621 -211 C ATOM 1498 C VAL A 224 10.390 -28.291 8.294 1.00 85.98 C ANISOU 1498 C VAL A 224 15656 8872 8142 -827 465 -242 C ATOM 1499 O VAL A 224 10.779 -28.156 9.460 1.00 90.79 O ANISOU 1499 O VAL A 224 16120 9583 8792 -744 452 -178 O ATOM 1500 CB VAL A 224 12.466 -28.639 6.919 1.00 86.72 C ANISOU 1500 CB VAL A 224 15814 9025 8112 -429 662 -112 C ATOM 1501 CG1 VAL A 224 13.138 -29.531 5.884 1.00 81.58 C ANISOU 1501 CG1 VAL A 224 15430 8251 7315 -215 833 -79 C ATOM 1502 CG2 VAL A 224 12.269 -27.232 6.380 1.00 93.15 C ANISOU 1502 CG2 VAL A 224 16380 9989 9024 -599 527 -153 C ATOM 1503 N MET A 225 9.338 -27.623 7.819 1.00 88.53 N ANISOU 1503 N MET A 225 15918 9209 8511 -1055 350 -334 N ATOM 1504 CA MET A 225 8.546 -26.759 8.683 1.00 82.68 C ANISOU 1504 CA MET A 225 14962 8585 7867 -1194 223 -361 C ATOM 1505 C MET A 225 7.386 -27.491 9.344 1.00 86.03 C ANISOU 1505 C MET A 225 15498 8924 8267 -1352 218 -407 C ATOM 1506 O MET A 225 6.963 -27.100 10.438 1.00 93.93 O ANISOU 1506 O MET A 225 16352 10011 9326 -1391 164 -397 O ATOM 1507 CB MET A 225 8.011 -25.558 7.900 1.00 74.77 C ANISOU 1507 CB MET A 225 13817 7681 6913 -1309 109 -413 C ATOM 1508 CG MET A 225 9.011 -24.423 7.765 1.00 82.02 C ANISOU 1508 CG MET A 225 14552 8728 7882 -1214 81 -360 C ATOM 1509 SD MET A 225 8.239 -22.844 7.359 1.00 89.19 S ANISOU 1509 SD MET A 225 15316 9729 8844 -1333 -56 -407 S ATOM 1510 CE MET A 225 8.220 -22.911 5.570 1.00 89.27 C ANISOU 1510 CE MET A 225 15451 9683 8783 -1353 -36 -439 C ATOM 1511 N MET A 226 6.857 -28.541 8.711 1.00 88.52 N ANISOU 1511 N MET A 226 16083 9071 8480 -1463 276 -456 N ATOM 1512 CA MET A 226 5.821 -29.334 9.362 1.00 94.66 C ANISOU 1512 CA MET A 226 16985 9770 9212 -1653 285 -488 C ATOM 1513 C MET A 226 6.393 -30.218 10.461 1.00 97.44 C ANISOU 1513 C MET A 226 17484 10009 9531 -1510 399 -417 C ATOM 1514 O MET A 226 5.729 -30.436 11.481 1.00 98.30 O ANISOU 1514 O MET A 226 17566 10132 9651 -1615 389 -411 O ATOM 1515 CB MET A 226 5.070 -30.186 8.341 1.00 89.93 C ANISOU 1515 CB MET A 226 16661 9023 8484 -1874 303 -566 C ATOM 1516 CG MET A 226 4.188 -29.378 7.405 1.00 96.34 C ANISOU 1516 CG MET A 226 17307 9992 9307 -2058 168 -632 C ATOM 1517 SD MET A 226 3.173 -30.413 6.334 1.00124.95 S ANISOU 1517 SD MET A 226 21237 13490 12750 -2395 159 -727 S ATOM 1518 CE MET A 226 2.001 -31.063 7.523 1.00103.04 C ANISOU 1518 CE MET A 226 18454 10749 9946 -2669 151 -727 C ATOM 1519 N VAL A 227 7.612 -30.733 10.280 1.00 87.22 N ANISOU 1519 N VAL A 227 16338 8619 8181 -1252 515 -351 N ATOM 1520 CA VAL A 227 8.239 -31.497 11.354 1.00 87.12 C ANISOU 1520 CA VAL A 227 16443 8534 8125 -1057 622 -262 C ATOM 1521 C VAL A 227 8.739 -30.567 12.449 1.00 89.23 C ANISOU 1521 C VAL A 227 16365 9036 8503 -939 544 -194 C ATOM 1522 O VAL A 227 8.843 -30.968 13.613 1.00 93.85 O ANISOU 1522 O VAL A 227 16971 9615 9071 -862 579 -135 O ATOM 1523 CB VAL A 227 9.372 -32.386 10.806 1.00 82.88 C ANISOU 1523 CB VAL A 227 16179 7848 7463 -770 785 -194 C ATOM 1524 CG1 VAL A 227 8.841 -33.313 9.728 1.00 86.78 C ANISOU 1524 CG1 VAL A 227 17083 8072 7819 -910 865 -276 C ATOM 1525 CG2 VAL A 227 10.512 -31.535 10.269 1.00 92.08 C ANISOU 1525 CG2 VAL A 227 17085 9221 8680 -555 767 -135 C ATOM 1526 N ALA A 228 9.052 -29.317 12.107 1.00 78.84 N ANISOU 1526 N ALA A 228 14757 7917 7282 -936 439 -202 N ATOM 1527 CA ALA A 228 9.459 -28.352 13.122 1.00 72.45 C ANISOU 1527 CA ALA A 228 13659 7315 6555 -882 352 -155 C ATOM 1528 C ALA A 228 8.253 -27.851 13.908 1.00 74.63 C ANISOU 1528 C ALA A 228 13836 7631 6890 -1079 259 -215 C ATOM 1529 O ALA A 228 8.209 -27.961 15.137 1.00 82.29 O ANISOU 1529 O ALA A 228 14768 8637 7860 -1045 259 -177 O ATOM 1530 CB ALA A 228 10.207 -27.185 12.473 1.00 69.99 C ANISOU 1530 CB ALA A 228 13123 7172 6298 -846 281 -144 C ATOM 1531 N TYR A 229 7.256 -27.306 13.207 1.00 88.74 N ANISOU 1531 N TYR A 229 15575 9430 8711 -1264 186 -299 N ATOM 1532 CA TYR A 229 6.058 -26.814 13.876 1.00 89.89 C ANISOU 1532 CA TYR A 229 15607 9654 8895 -1417 113 -341 C ATOM 1533 C TYR A 229 5.209 -27.944 14.442 1.00 91.78 C ANISOU 1533 C TYR A 229 16008 9791 9072 -1540 180 -345 C ATOM 1534 O TYR A 229 4.418 -27.706 15.362 1.00 98.19 O ANISOU 1534 O TYR A 229 16719 10688 9902 -1617 152 -347 O ATOM 1535 CB TYR A 229 5.231 -25.963 12.911 1.00 85.48 C ANISOU 1535 CB TYR A 229 14943 9173 8363 -1543 24 -407 C ATOM 1536 CG TYR A 229 5.783 -24.570 12.721 1.00 85.49 C ANISOU 1536 CG TYR A 229 14775 9284 8425 -1457 -54 -402 C ATOM 1537 CD1 TYR A 229 5.782 -23.653 13.764 1.00 85.53 C ANISOU 1537 CD1 TYR A 229 14646 9383 8467 -1414 -107 -388 C ATOM 1538 CD2 TYR A 229 6.323 -24.176 11.504 1.00 87.00 C ANISOU 1538 CD2 TYR A 229 14976 9465 8616 -1430 -66 -411 C ATOM 1539 CE1 TYR A 229 6.292 -22.379 13.597 1.00 85.73 C ANISOU 1539 CE1 TYR A 229 14580 9473 8522 -1371 -173 -388 C ATOM 1540 CE2 TYR A 229 6.836 -22.905 11.327 1.00 86.75 C ANISOU 1540 CE2 TYR A 229 14825 9514 8623 -1384 -128 -402 C ATOM 1541 CZ TYR A 229 6.819 -22.012 12.377 1.00 87.24 C ANISOU 1541 CZ TYR A 229 14783 9651 8715 -1366 -182 -392 C ATOM 1542 OH TYR A 229 7.329 -20.747 12.205 1.00 89.88 O ANISOU 1542 OH TYR A 229 15057 10030 9063 -1355 -239 -387 O ATOM 1543 N GLY A 230 5.351 -29.162 13.918 1.00 72.56 N ANISOU 1543 N GLY A 230 13849 7170 6550 -1563 280 -345 N ATOM 1544 CA GLY A 230 4.649 -30.290 14.505 1.00 74.91 C ANISOU 1544 CA GLY A 230 14358 7337 6766 -1703 358 -341 C ATOM 1545 C GLY A 230 5.262 -30.728 15.821 1.00 79.92 C ANISOU 1545 C GLY A 230 15048 7934 7385 -1529 431 -256 C ATOM 1546 O GLY A 230 4.547 -30.988 16.793 1.00 78.40 O ANISOU 1546 O GLY A 230 14857 7755 7177 -1635 446 -243 O ATOM 1547 N LEU A 231 6.594 -30.815 15.872 1.00 84.53 N ANISOU 1547 N LEU A 231 15661 8499 7957 -1254 478 -186 N ATOM 1548 CA LEU A 231 7.266 -31.155 17.121 1.00 83.90 C ANISOU 1548 CA LEU A 231 15599 8433 7847 -1056 531 -90 C ATOM 1549 C LEU A 231 7.110 -30.052 18.159 1.00 82.30 C ANISOU 1549 C LEU A 231 15094 8447 7728 -1067 418 -86 C ATOM 1550 O LEU A 231 7.066 -30.337 19.361 1.00 87.97 O ANISOU 1550 O LEU A 231 15833 9176 8414 -1017 445 -34 O ATOM 1551 CB LEU A 231 8.747 -31.438 16.863 1.00 83.35 C ANISOU 1551 CB LEU A 231 15576 8367 7727 -743 598 0 C ATOM 1552 CG LEU A 231 9.071 -32.761 16.163 1.00 85.23 C ANISOU 1552 CG LEU A 231 16205 8347 7830 -630 760 27 C ATOM 1553 CD1 LEU A 231 10.573 -32.923 15.979 1.00 80.96 C ANISOU 1553 CD1 LEU A 231 15645 7886 7232 -261 832 141 C ATOM 1554 CD2 LEU A 231 8.493 -33.936 16.934 1.00 92.66 C ANISOU 1554 CD2 LEU A 231 17477 9065 8665 -686 870 50 C ATOM 1555 N ILE A 232 7.024 -28.795 17.720 1.00 82.56 N ANISOU 1555 N ILE A 232 14883 8636 7851 -1124 301 -138 N ATOM 1556 CA ILE A 232 6.793 -27.695 18.652 1.00 75.01 C ANISOU 1556 CA ILE A 232 13703 7847 6950 -1142 203 -147 C ATOM 1557 C ILE A 232 5.406 -27.809 19.269 1.00 77.87 C ANISOU 1557 C ILE A 232 14071 8209 7308 -1311 209 -183 C ATOM 1558 O ILE A 232 5.237 -27.671 20.486 1.00 88.60 O ANISOU 1558 O ILE A 232 15385 9627 8652 -1280 207 -154 O ATOM 1559 CB ILE A 232 6.987 -26.343 17.943 1.00 74.50 C ANISOU 1559 CB ILE A 232 13449 7902 6957 -1165 95 -194 C ATOM 1560 CG1 ILE A 232 8.476 -26.049 17.754 1.00 74.91 C ANISOU 1560 CG1 ILE A 232 13428 8031 7003 -1010 80 -134 C ATOM 1561 CG2 ILE A 232 6.316 -25.223 18.723 1.00 77.48 C ANISOU 1561 CG2 ILE A 232 13679 8393 7367 -1225 10 -231 C ATOM 1562 CD1 ILE A 232 8.754 -24.946 16.762 1.00 77.59 C ANISOU 1562 CD1 ILE A 232 13648 8440 7392 -1058 4 -173 C ATOM 1563 N SER A 233 4.392 -28.074 18.440 1.00 82.82 N ANISOU 1563 N SER A 233 14742 8794 7931 -1498 217 -240 N ATOM 1564 CA SER A 233 3.034 -28.226 18.949 1.00 88.83 C ANISOU 1564 CA SER A 233 15468 9613 8672 -1681 227 -259 C ATOM 1565 C SER A 233 2.896 -29.427 19.877 1.00 91.67 C ANISOU 1565 C SER A 233 16027 9853 8952 -1718 338 -204 C ATOM 1566 O SER A 233 1.992 -29.446 20.719 1.00 89.39 O ANISOU 1566 O SER A 233 15676 9646 8642 -1822 357 -192 O ATOM 1567 CB SER A 233 2.049 -28.342 17.785 1.00 87.67 C ANISOU 1567 CB SER A 233 15312 9489 8511 -1898 202 -319 C ATOM 1568 OG SER A 233 1.957 -27.116 17.079 1.00 88.56 O ANISOU 1568 OG SER A 233 15227 9737 8685 -1855 100 -359 O ATOM 1569 N LEU A 234 3.767 -30.429 19.740 1.00 82.47 N ANISOU 1569 N LEU A 234 15113 8496 7727 -1616 426 -162 N ATOM 1570 CA LEU A 234 3.743 -31.553 20.671 1.00 80.45 C ANISOU 1570 CA LEU A 234 15093 8097 7377 -1609 543 -96 C ATOM 1571 C LEU A 234 4.222 -31.131 22.054 1.00 80.77 C ANISOU 1571 C LEU A 234 15017 8247 7426 -1422 527 -31 C ATOM 1572 O LEU A 234 3.621 -31.507 23.067 1.00 87.14 O ANISOU 1572 O LEU A 234 15876 9051 8184 -1491 580 3 O ATOM 1573 CB LEU A 234 4.599 -32.700 20.134 1.00 79.70 C ANISOU 1573 CB LEU A 234 15336 7757 7191 -1488 656 -57 C ATOM 1574 CG LEU A 234 3.994 -33.557 19.020 1.00 77.61 C ANISOU 1574 CG LEU A 234 15342 7297 6850 -1721 716 -116 C ATOM 1575 CD1 LEU A 234 4.894 -34.744 18.724 1.00 76.66 C ANISOU 1575 CD1 LEU A 234 15629 6894 6603 -1538 860 -63 C ATOM 1576 CD2 LEU A 234 2.594 -34.020 19.388 1.00 74.41 C ANISOU 1576 CD2 LEU A 234 14997 6883 6392 -2071 740 -142 C ATOM 1577 N GLU A 235 5.303 -30.349 22.117 1.00 92.60 N ANISOU 1577 N GLU A 235 16360 9854 8969 -1208 452 -10 N ATOM 1578 CA GLU A 235 5.801 -29.874 23.404 1.00 92.40 C ANISOU 1578 CA GLU A 235 16222 9955 8931 -1058 413 44 C ATOM 1579 C GLU A 235 4.817 -28.914 24.059 1.00 95.31 C ANISOU 1579 C GLU A 235 16407 10468 9340 -1179 347 -7 C ATOM 1580 O GLU A 235 4.571 -28.999 25.268 1.00102.63 O ANISOU 1580 O GLU A 235 17347 11432 10217 -1152 373 31 O ATOM 1581 CB GLU A 235 7.162 -29.202 23.225 1.00 96.34 C ANISOU 1581 CB GLU A 235 16579 10574 9450 -864 333 74 C ATOM 1582 CG GLU A 235 7.785 -28.713 24.523 1.00108.57 C ANISOU 1582 CG GLU A 235 18017 12276 10958 -737 273 130 C ATOM 1583 CD GLU A 235 9.007 -29.514 24.924 1.00115.27 C ANISOU 1583 CD GLU A 235 18948 13139 11710 -492 323 252 C ATOM 1584 OE1 GLU A 235 9.469 -30.343 24.111 1.00119.52 O ANISOU 1584 OE1 GLU A 235 19628 13566 12219 -388 411 293 O ATOM 1585 OE2 GLU A 235 9.509 -29.313 26.051 1.00109.51 O ANISOU 1585 OE2 GLU A 235 18148 12543 10916 -387 277 313 O ATOM 1586 N LEU A 236 4.246 -27.992 23.281 1.00 85.93 N ANISOU 1586 N LEU A 236 15061 9363 8226 -1284 272 -85 N ATOM 1587 CA LEU A 236 3.292 -27.039 23.833 1.00 91.71 C ANISOU 1587 CA LEU A 236 15634 10237 8975 -1345 226 -124 C ATOM 1588 C LEU A 236 2.004 -27.708 24.297 1.00 93.45 C ANISOU 1588 C LEU A 236 15889 10469 9150 -1502 314 -110 C ATOM 1589 O LEU A 236 1.315 -27.160 25.164 1.00 92.90 O ANISOU 1589 O LEU A 236 15717 10524 9058 -1496 316 -107 O ATOM 1590 CB LEU A 236 2.980 -25.948 22.805 1.00 87.91 C ANISOU 1590 CB LEU A 236 15004 9837 8562 -1384 139 -195 C ATOM 1591 CG LEU A 236 3.901 -24.723 22.793 1.00 89.04 C ANISOU 1591 CG LEU A 236 15064 10034 8734 -1264 39 -216 C ATOM 1592 CD1 LEU A 236 5.313 -25.079 22.367 1.00 80.25 C ANISOU 1592 CD1 LEU A 236 14000 8865 7626 -1180 26 -180 C ATOM 1593 CD2 LEU A 236 3.338 -23.648 21.883 1.00 93.87 C ANISOU 1593 CD2 LEU A 236 15572 10706 9389 -1302 -24 -279 C ATOM 1594 N TYR A 237 1.666 -28.876 23.748 1.00 85.88 N ANISOU 1594 N TYR A 237 15088 9385 8156 -1654 393 -98 N ATOM 1595 CA TYR A 237 0.504 -29.612 24.227 1.00 86.54 C ANISOU 1595 CA TYR A 237 15221 9485 8174 -1857 482 -73 C ATOM 1596 C TYR A 237 0.781 -30.354 25.527 1.00 96.58 C ANISOU 1596 C TYR A 237 16661 10668 9366 -1785 577 6 C ATOM 1597 O TYR A 237 -0.166 -30.685 26.249 1.00100.31 O ANISOU 1597 O TYR A 237 17129 11203 9782 -1924 649 38 O ATOM 1598 CB TYR A 237 0.021 -30.600 23.163 1.00 85.32 C ANISOU 1598 CB TYR A 237 15222 9214 7983 -2102 528 -95 C ATOM 1599 CG TYR A 237 -1.331 -31.202 23.473 1.00 84.08 C ANISOU 1599 CG TYR A 237 15059 9138 7750 -2396 598 -75 C ATOM 1600 CD1 TYR A 237 -2.501 -30.506 23.200 1.00 77.79 C ANISOU 1600 CD1 TYR A 237 13973 8615 6968 -2539 544 -99 C ATOM 1601 CD2 TYR A 237 -1.436 -32.463 24.046 1.00 81.59 C ANISOU 1601 CD2 TYR A 237 15027 8643 7331 -2529 725 -20 C ATOM 1602 CE1 TYR A 237 -3.738 -31.050 23.484 1.00 82.18 C ANISOU 1602 CE1 TYR A 237 14474 9310 7441 -2827 608 -64 C ATOM 1603 CE2 TYR A 237 -2.669 -33.015 24.335 1.00 86.11 C ANISOU 1603 CE2 TYR A 237 15588 9307 7821 -2846 793 5 C ATOM 1604 CZ TYR A 237 -3.816 -32.305 24.052 1.00 89.30 C ANISOU 1604 CZ TYR A 237 15655 10031 8245 -3005 730 -15 C ATOM 1605 OH TYR A 237 -5.046 -32.850 24.339 1.00 96.83 O ANISOU 1605 OH TYR A 237 16549 11138 9103 -3339 796 26 O ATOM 1606 N GLN A 238 2.052 -30.617 25.844 1.00110.21 N ANISOU 1606 N GLN A 238 18522 12278 11075 -1566 580 49 N ATOM 1607 CA GLN A 238 2.388 -31.238 27.119 1.00111.74 C ANISOU 1607 CA GLN A 238 18868 12410 11179 -1454 659 135 C ATOM 1608 C GLN A 238 1.988 -30.368 28.303 1.00110.73 C ANISOU 1608 C GLN A 238 18564 12466 11043 -1400 623 140 C ATOM 1609 O GLN A 238 1.879 -30.875 29.424 1.00112.17 O ANISOU 1609 O GLN A 238 18858 12625 11138 -1366 700 208 O ATOM 1610 CB GLN A 238 3.885 -31.546 27.179 1.00110.79 C ANISOU 1610 CB GLN A 238 18865 12203 11028 -1187 650 193 C ATOM 1611 CG GLN A 238 4.345 -32.587 26.173 1.00109.09 C ANISOU 1611 CG GLN A 238 18900 11771 10778 -1176 729 210 C ATOM 1612 CD GLN A 238 3.580 -33.890 26.294 1.00118.01 C ANISOU 1612 CD GLN A 238 20350 12685 11805 -1360 879 242 C ATOM 1613 OE1 GLN A 238 2.700 -34.184 25.485 1.00123.28 O ANISOU 1613 OE1 GLN A 238 21075 13288 12478 -1634 903 181 O ATOM 1614 NE2 GLN A 238 3.914 -34.681 27.308 1.00120.56 N ANISOU 1614 NE2 GLN A 238 20894 12899 12015 -1227 979 341 N ATOM 1615 N GLY A 239 1.769 -29.075 28.079 1.00 94.83 N ANISOU 1615 N GLY A 239 16313 10618 9100 -1379 518 72 N ATOM 1616 CA GLY A 239 1.293 -28.197 29.123 1.00102.46 C ANISOU 1616 CA GLY A 239 17154 11739 10037 -1320 499 67 C ATOM 1617 C GLY A 239 2.362 -27.865 30.151 1.00106.72 C ANISOU 1617 C GLY A 239 17740 12288 10520 -1118 447 99 C ATOM 1618 O GLY A 239 3.544 -28.181 30.010 1.00102.28 O ANISOU 1618 O GLY A 239 17250 11661 9950 -1005 409 132 O ATOM 1619 N ILE A 240 1.908 -27.202 31.208 1.00120.36 N ANISOU 1619 N ILE A 240 19418 14125 12190 -1069 448 95 N ATOM 1620 CA ILE A 240 2.779 -26.825 32.313 1.00118.86 C ANISOU 1620 CA ILE A 240 19277 13969 11914 -912 390 119 C ATOM 1621 C ILE A 240 3.002 -28.035 33.208 1.00114.88 C ANISOU 1621 C ILE A 240 18945 13392 11312 -864 486 222 C ATOM 1622 O ILE A 240 2.090 -28.840 33.433 1.00111.29 O ANISOU 1622 O ILE A 240 18568 12890 10828 -971 617 263 O ATOM 1623 CB ILE A 240 2.173 -25.647 33.098 1.00115.28 C ANISOU 1623 CB ILE A 240 18761 13633 11407 -870 366 68 C ATOM 1624 CG1 ILE A 240 1.820 -24.499 32.150 1.00117.03 C ANISOU 1624 CG1 ILE A 240 18858 13900 11709 -897 298 -22 C ATOM 1625 CG2 ILE A 240 3.133 -25.165 34.174 1.00118.09 C ANISOU 1625 CG2 ILE A 240 19189 14025 11655 -746 281 76 C ATOM 1626 CD1 ILE A 240 0.338 -24.352 31.893 1.00119.52 C ANISOU 1626 CD1 ILE A 240 19067 14304 12040 -959 389 -32 C ATOM 1627 N ASN A 241 4.221 -28.172 33.712 1.00116.28 N ANISOU 1627 N ASN A 241 19182 13575 11423 -711 423 273 N ATOM 1628 CA ASN A 241 4.602 -29.255 34.605 1.00116.83 C ANISOU 1628 CA ASN A 241 19431 13585 11375 -605 504 386 C ATOM 1629 C ASN A 241 5.029 -28.678 35.952 1.00113.33 C ANISOU 1629 C ASN A 241 18983 13271 10806 -484 433 406 C ATOM 1630 O ASN A 241 5.031 -27.462 36.162 1.00114.20 O ANISOU 1630 O ASN A 241 18983 13492 10916 -501 327 325 O ATOM 1631 CB ASN A 241 5.716 -30.102 33.984 1.00114.18 C ANISOU 1631 CB ASN A 241 19181 13168 11036 -482 504 458 C ATOM 1632 CG ASN A 241 6.974 -29.303 33.724 1.00123.80 C ANISOU 1632 CG ASN A 241 20237 14537 12265 -368 343 445 C ATOM 1633 OD1 ASN A 241 7.826 -29.167 34.600 1.00119.27 O ANISOU 1633 OD1 ASN A 241 19644 14094 11580 -228 269 506 O ATOM 1634 ND2 ASN A 241 7.096 -28.765 32.515 1.00124.18 N ANISOU 1634 ND2 ASN A 241 20161 14588 12433 -447 283 371 N ATOM 1635 N ILE A 242 5.398 -29.572 36.871 1.00114.68 N ANISOU 1635 N ILE A 242 19312 13413 10849 -361 496 518 N ATOM 1636 CA ILE A 242 5.775 -29.135 38.211 1.00116.03 C ANISOU 1636 CA ILE A 242 19501 13712 10872 -252 431 546 C ATOM 1637 C ILE A 242 7.124 -28.429 38.202 1.00119.65 C ANISOU 1637 C ILE A 242 19834 14334 11292 -158 241 538 C ATOM 1638 O ILE A 242 7.335 -27.471 38.957 1.00125.81 O ANISOU 1638 O ILE A 242 20571 15246 11985 -166 128 489 O ATOM 1639 CB ILE A 242 5.766 -30.329 39.184 1.00110.67 C ANISOU 1639 CB ILE A 242 19038 12960 10050 -138 556 680 C ATOM 1640 CG1 ILE A 242 6.125 -29.864 40.595 1.00112.10 C ANISOU 1640 CG1 ILE A 242 19243 13288 10061 -27 483 708 C ATOM 1641 CG2 ILE A 242 6.706 -31.432 38.708 1.00111.42 C ANISOU 1641 CG2 ILE A 242 19244 12969 10122 17 590 792 C ATOM 1642 CD1 ILE A 242 5.878 -30.898 41.646 1.00125.83 C ANISOU 1642 CD1 ILE A 242 21204 14955 11650 70 621 833 C ATOM 1643 N PHE A 243 8.055 -28.872 37.353 1.00108.45 N ANISOU 1643 N PHE A 243 18363 12924 9920 -80 207 589 N ATOM 1644 CA PHE A 243 9.372 -28.247 37.323 1.00107.92 C ANISOU 1644 CA PHE A 243 18135 13069 9802 -12 30 603 C ATOM 1645 C PHE A 243 9.295 -26.829 36.775 1.00105.93 C ANISOU 1645 C PHE A 243 17733 12879 9636 -194 -98 461 C ATOM 1646 O PHE A 243 10.050 -25.952 37.212 1.00103.74 O ANISOU 1646 O PHE A 243 17367 12781 9270 -230 -257 437 O ATOM 1647 CB PHE A 243 10.338 -29.091 36.494 1.00105.95 C ANISOU 1647 CB PHE A 243 17852 12833 9571 144 52 706 C ATOM 1648 CG PHE A 243 10.907 -30.263 37.240 1.00112.33 C ANISOU 1648 CG PHE A 243 18799 13659 10221 399 126 874 C ATOM 1649 CD1 PHE A 243 10.140 -31.398 37.454 1.00109.23 C ANISOU 1649 CD1 PHE A 243 18674 13024 9806 449 318 931 C ATOM 1650 CD2 PHE A 243 12.196 -30.228 37.741 1.00120.42 C ANISOU 1650 CD2 PHE A 243 19695 14958 11101 582 5 984 C ATOM 1651 CE1 PHE A 243 10.655 -32.480 38.142 1.00114.08 C ANISOU 1651 CE1 PHE A 243 19467 13622 10256 706 400 1094 C ATOM 1652 CE2 PHE A 243 12.714 -31.306 38.433 1.00125.52 C ANISOU 1652 CE2 PHE A 243 20475 15634 11581 864 78 1155 C ATOM 1653 CZ PHE A 243 11.944 -32.432 38.633 1.00120.81 C ANISOU 1653 CZ PHE A 243 20188 14750 10964 940 282 1209 C ATOM 1654 N GLU A 244 8.389 -26.585 35.825 1.00138.83 N ANISOU 1654 N GLU A 244 21890 16903 13957 -320 -32 370 N ATOM 1655 CA GLU A 244 8.163 -25.226 35.348 1.00139.71 C ANISOU 1655 CA GLU A 244 21911 17039 14133 -467 -129 241 C ATOM 1656 C GLU A 244 7.417 -24.392 36.381 1.00136.49 C ANISOU 1656 C GLU A 244 21589 16637 13633 -509 -136 170 C ATOM 1657 O GLU A 244 7.666 -23.187 36.500 1.00135.89 O ANISOU 1657 O GLU A 244 21506 16614 13511 -587 -253 85 O ATOM 1658 CB GLU A 244 7.392 -25.257 34.028 1.00141.81 C ANISOU 1658 CB GLU A 244 22138 17173 14569 -556 -54 181 C ATOM 1659 CG GLU A 244 7.187 -23.895 33.385 1.00145.87 C ANISOU 1659 CG GLU A 244 22580 17696 15147 -673 -141 63 C ATOM 1660 CD GLU A 244 6.424 -23.979 32.077 1.00153.44 C ANISOU 1660 CD GLU A 244 23490 18553 16256 -744 -74 18 C ATOM 1661 OE1 GLU A 244 6.197 -25.108 31.592 1.00151.48 O ANISOU 1661 OE1 GLU A 244 23268 18228 16061 -731 25 72 O ATOM 1662 OE2 GLU A 244 6.046 -22.917 31.535 1.00153.63 O ANISOU 1662 OE2 GLU A 244 23478 18567 16326 -812 -119 -70 O ATOM 1663 N MET A 245 6.508 -25.014 37.136 1.00 97.13 N ANISOU 1663 N MET A 245 16713 11590 8602 -461 -2 207 N ATOM 1664 CA MET A 245 5.770 -24.289 38.165 1.00 96.59 C ANISOU 1664 CA MET A 245 16737 11538 8426 -462 18 153 C ATOM 1665 C MET A 245 6.695 -23.838 39.289 1.00 95.41 C ANISOU 1665 C MET A 245 16654 11508 8090 -421 -114 162 C ATOM 1666 O MET A 245 6.656 -22.677 39.712 1.00 95.76 O ANISOU 1666 O MET A 245 16764 11574 8045 -474 -194 68 O ATOM 1667 CB MET A 245 4.643 -25.163 38.715 1.00 94.79 C ANISOU 1667 CB MET A 245 16589 11249 8179 -430 203 212 C ATOM 1668 CG MET A 245 4.067 -24.669 40.032 1.00 99.50 C ANISOU 1668 CG MET A 245 17299 11890 8618 -377 243 196 C ATOM 1669 SD MET A 245 2.749 -25.721 40.669 1.00 91.18 S ANISOU 1669 SD MET A 245 16313 10801 7532 -368 475 285 S ATOM 1670 CE MET A 245 3.675 -27.197 41.076 1.00 96.66 C ANISOU 1670 CE MET A 245 17118 11446 8161 -294 495 429 C ATOM 1671 N LEU A 246 7.536 -24.748 39.788 1.00 85.37 N ANISOU 1671 N LEU A 246 15385 10315 6735 -323 -136 279 N ATOM 1672 CA LEU A 246 8.468 -24.390 40.851 1.00 86.53 C ANISOU 1672 CA LEU A 246 15566 10627 6684 -292 -280 303 C ATOM 1673 C LEU A 246 9.523 -23.404 40.368 1.00 91.20 C ANISOU 1673 C LEU A 246 16039 11351 7260 -418 -479 244 C ATOM 1674 O LEU A 246 10.005 -22.580 41.155 1.00 91.86 O ANISOU 1674 O LEU A 246 16180 11548 7175 -497 -618 197 O ATOM 1675 CB LEU A 246 9.132 -25.647 41.412 1.00 85.82 C ANISOU 1675 CB LEU A 246 15490 10618 6498 -120 -252 465 C ATOM 1676 CG LEU A 246 8.327 -26.409 42.465 1.00 91.69 C ANISOU 1676 CG LEU A 246 16415 11278 7144 -17 -98 532 C ATOM 1677 CD1 LEU A 246 8.931 -27.782 42.717 1.00 89.79 C ANISOU 1677 CD1 LEU A 246 16223 11057 6835 175 -37 704 C ATOM 1678 CD2 LEU A 246 8.246 -25.608 43.756 1.00 86.33 C ANISOU 1678 CD2 LEU A 246 15846 10688 6267 -34 -173 481 C ATOM 1679 N ARG A 247 9.895 -23.470 39.088 1.00107.79 N ANISOU 1679 N ARG A 247 17991 13443 9520 -460 -495 244 N ATOM 1680 CA ARG A 247 10.842 -22.503 38.543 1.00105.55 C ANISOU 1680 CA ARG A 247 17591 13287 9228 -614 -668 191 C ATOM 1681 C ARG A 247 10.213 -21.121 38.420 1.00100.21 C ANISOU 1681 C ARG A 247 17036 12486 8553 -780 -702 32 C ATOM 1682 O ARG A 247 10.924 -20.110 38.445 1.00 97.89 O ANISOU 1682 O ARG A 247 16749 12279 8167 -951 -857 -30 O ATOM 1683 CB ARG A 247 11.358 -22.988 37.188 1.00104.88 C ANISOU 1683 CB ARG A 247 17327 13219 9303 -592 -650 243 C ATOM 1684 CG ARG A 247 12.545 -22.212 36.644 1.00108.43 C ANISOU 1684 CG ARG A 247 17610 13862 9725 -740 -822 234 C ATOM 1685 CD ARG A 247 13.022 -22.805 35.326 1.00116.82 C ANISOU 1685 CD ARG A 247 18504 14947 10936 -675 -774 300 C ATOM 1686 NE ARG A 247 13.478 -24.183 35.483 1.00116.62 N ANISOU 1686 NE ARG A 247 18428 15003 10881 -427 -695 458 N ATOM 1687 CZ ARG A 247 12.865 -25.239 34.966 1.00114.65 C ANISOU 1687 CZ ARG A 247 18266 14557 10740 -277 -521 499 C ATOM 1688 NH1 ARG A 247 11.761 -25.116 34.248 1.00114.05 N ANISOU 1688 NH1 ARG A 247 18282 14236 10816 -365 -421 398 N ATOM 1689 NH2 ARG A 247 13.373 -26.451 35.176 1.00103.42 N ANISOU 1689 NH2 ARG A 247 16854 13190 9251 -36 -445 649 N ATOM 1690 N ILE A 248 8.887 -21.058 38.289 1.00 84.92 N ANISOU 1690 N ILE A 248 15206 10357 6701 -733 -552 -27 N ATOM 1691 CA ILE A 248 8.189 -19.778 38.303 1.00 81.07 C ANISOU 1691 CA ILE A 248 14874 9749 6181 -814 -554 -161 C ATOM 1692 C ILE A 248 8.046 -19.260 39.729 1.00 88.97 C ANISOU 1692 C ILE A 248 16086 10761 6956 -802 -582 -201 C ATOM 1693 O ILE A 248 8.260 -18.073 39.996 1.00 90.15 O ANISOU 1693 O ILE A 248 16403 10875 6976 -921 -679 -302 O ATOM 1694 CB ILE A 248 6.820 -19.918 37.612 1.00 82.65 C ANISOU 1694 CB ILE A 248 15068 9801 6536 -738 -382 -188 C ATOM 1695 CG1 ILE A 248 6.993 -20.079 36.101 1.00 85.17 C ANISOU 1695 CG1 ILE A 248 15224 10090 7048 -793 -386 -185 C ATOM 1696 CG2 ILE A 248 5.929 -18.726 37.929 1.00 78.45 C ANISOU 1696 CG2 ILE A 248 14725 9163 5920 -723 -341 -296 C ATOM 1697 CD1 ILE A 248 5.727 -20.503 35.390 1.00 81.21 C ANISOU 1697 CD1 ILE A 248 14669 9497 6689 -735 -230 -184 C ATOM 1698 N ASP A 249 7.694 -20.144 40.667 1.00 97.25 N ANISOU 1698 N ASP A 249 17167 11846 7937 -666 -493 -121 N ATOM 1699 CA ASP A 249 7.435 -19.730 42.041 1.00 94.99 C ANISOU 1699 CA ASP A 249 17097 11565 7430 -629 -494 -154 C ATOM 1700 C ASP A 249 8.705 -19.351 42.793 1.00 99.11 C ANISOU 1700 C ASP A 249 17665 12248 7744 -746 -702 -155 C ATOM 1701 O ASP A 249 8.620 -18.646 43.805 1.00100.88 O ANISOU 1701 O ASP A 249 18118 12457 7754 -780 -746 -224 O ATOM 1702 CB ASP A 249 6.706 -20.845 42.793 1.00 92.61 C ANISOU 1702 CB ASP A 249 16812 11265 7112 -460 -329 -55 C ATOM 1703 CG ASP A 249 5.202 -20.794 42.601 1.00 91.23 C ANISOU 1703 CG ASP A 249 16675 10967 7023 -378 -127 -83 C ATOM 1704 OD1 ASP A 249 4.689 -19.740 42.169 1.00 88.71 O ANISOU 1704 OD1 ASP A 249 16422 10564 6721 -401 -116 -187 O ATOM 1705 OD2 ASP A 249 4.534 -21.812 42.879 1.00 89.28 O ANISOU 1705 OD2 ASP A 249 16392 10720 6811 -291 26 8 O ATOM 1706 N GLU A 250 9.872 -19.798 42.332 1.00 96.11 N ANISOU 1706 N GLU A 250 17073 12044 7401 -808 -829 -75 N ATOM 1707 CA GLU A 250 11.128 -19.563 43.033 1.00104.99 C ANISOU 1707 CA GLU A 250 18171 13406 8316 -925 -1037 -45 C ATOM 1708 C GLU A 250 12.090 -18.676 42.258 1.00113.48 C ANISOU 1708 C GLU A 250 19147 14580 9392 -1177 -1214 -100 C ATOM 1709 O GLU A 250 12.678 -17.754 42.831 1.00122.09 O ANISOU 1709 O GLU A 250 20360 15755 10272 -1392 -1380 -171 O ATOM 1710 CB GLU A 250 11.805 -20.903 43.358 1.00110.73 C ANISOU 1710 CB GLU A 250 18710 14341 9021 -752 -1041 134 C ATOM 1711 CG GLU A 250 11.073 -21.734 44.399 1.00107.55 C ANISOU 1711 CG GLU A 250 18450 13875 8540 -544 -898 201 C ATOM 1712 N GLY A 251 12.272 -18.932 40.965 1.00166.95 N ANISOU 1712 N GLY A 251 25714 21341 16378 -1179 -1181 -68 N ATOM 1713 CA GLY A 251 13.224 -18.176 40.177 1.00172.90 C ANISOU 1713 CA GLY A 251 26347 22211 17135 -1420 -1334 -99 C ATOM 1714 C GLY A 251 14.645 -18.664 40.381 1.00181.14 C ANISOU 1714 C GLY A 251 27121 23637 18068 -1461 -1494 38 C ATOM 1715 O GLY A 251 14.929 -19.568 41.169 1.00182.97 O ANISOU 1715 O GLY A 251 27278 24039 18205 -1281 -1495 157 O ATOM 1716 N LEU A 252 15.563 -18.039 39.647 1.00169.09 N ANISOU 1716 N LEU A 252 25439 22268 16538 -1697 -1628 31 N ATOM 1717 CA LEU A 252 16.973 -18.411 39.670 1.00171.91 C ANISOU 1717 CA LEU A 252 25474 23056 16788 -1750 -1783 176 C ATOM 1718 C LEU A 252 17.807 -17.208 40.086 1.00175.08 C ANISOU 1718 C LEU A 252 25913 23653 16956 -2156 -2014 106 C ATOM 1719 O LEU A 252 17.777 -16.166 39.423 1.00174.88 O ANISOU 1719 O LEU A 252 26002 23483 16961 -2431 -2050 -11 O ATOM 1720 CB LEU A 252 17.428 -18.930 38.304 1.00169.09 C ANISOU 1720 CB LEU A 252 24831 22782 16633 -1662 -1719 269 C ATOM 1721 CG LEU A 252 18.935 -19.149 38.149 1.00171.65 C ANISOU 1721 CG LEU A 252 24783 23595 16843 -1725 -1871 426 C ATOM 1722 CD1 LEU A 252 19.425 -20.229 39.103 1.00173.24 C ANISOU 1722 CD1 LEU A 252 24844 24083 16898 -1446 -1891 598 C ATOM 1723 CD2 LEU A 252 19.283 -19.502 36.711 1.00170.19 C ANISOU 1723 CD2 LEU A 252 24364 23445 16854 -1645 -1784 496 C ATOM 1724 N ARG A 253 18.549 -17.358 41.182 1.00198.58 N ANISOU 1724 N ARG A 253 28813 26957 19682 -2207 -2172 181 N ATOM 1725 CA ARG A 253 19.507 -16.358 41.643 1.00200.01 C ANISOU 1725 CA ARG A 253 28985 27412 19598 -2631 -2422 140 C ATOM 1726 C ARG A 253 20.831 -17.069 41.882 1.00204.34 C ANISOU 1726 C ARG A 253 29090 28542 20008 -2587 -2571 351 C ATOM 1727 O ARG A 253 20.929 -17.922 42.770 1.00205.22 O ANISOU 1727 O ARG A 253 29135 28830 20011 -2323 -2574 466 O ATOM 1728 CB ARG A 253 19.018 -15.660 42.913 1.00200.52 C ANISOU 1728 CB ARG A 253 29455 27311 19422 -2777 -2490 1 C ATOM 1729 CG ARG A 253 17.857 -14.701 42.695 1.00200.42 C ANISOU 1729 CG ARG A 253 29896 26776 19480 -2859 -2367 -206 C ATOM 1730 CD ARG A 253 18.251 -13.554 41.778 1.00200.91 C ANISOU 1730 CD ARG A 253 30024 26763 19548 -3246 -2446 -304 C ATOM 1731 NE ARG A 253 17.106 -12.727 41.413 1.00198.97 N ANISOU 1731 NE ARG A 253 30199 26011 19389 -3236 -2296 -476 N ATOM 1732 CZ ARG A 253 16.759 -11.609 42.036 1.00199.72 C ANISOU 1732 CZ ARG A 253 30765 25855 19266 -3454 -2338 -640 C ATOM 1733 NH1 ARG A 253 17.449 -11.150 43.068 1.00202.00 N ANISOU 1733 NH1 ARG A 253 31189 26330 19232 -3749 -2537 -674 N ATOM 1734 NH2 ARG A 253 15.694 -10.935 41.614 1.00193.92 N ANISOU 1734 NH2 ARG A 253 30388 24676 18617 -3363 -2173 -769 N ATOM 1735 N LEU A 254 21.847 -16.721 41.088 1.00196.79 N ANISOU 1735 N LEU A 254 27827 27902 19044 -2829 -2685 415 N ATOM 1736 CA LEU A 254 23.115 -17.442 41.148 1.00196.41 C ANISOU 1736 CA LEU A 254 27291 28458 18878 -2731 -2801 646 C ATOM 1737 C LEU A 254 23.825 -17.217 42.478 1.00199.11 C ANISOU 1737 C LEU A 254 27585 29206 18863 -2928 -3043 690 C ATOM 1738 O LEU A 254 24.346 -18.166 43.076 1.00202.93 O ANISOU 1738 O LEU A 254 27814 30061 19230 -2628 -3077 878 O ATOM 1739 CB LEU A 254 24.009 -17.026 39.981 1.00194.60 C ANISOU 1739 CB LEU A 254 26737 28497 18707 -2976 -2860 704 C ATOM 1740 CG LEU A 254 23.491 -17.385 38.586 1.00193.74 C ANISOU 1740 CG LEU A 254 26607 28075 18930 -2749 -2631 698 C ATOM 1741 CD1 LEU A 254 24.530 -17.064 37.521 1.00193.54 C ANISOU 1741 CD1 LEU A 254 26213 28402 18922 -2966 -2695 791 C ATOM 1742 CD2 LEU A 254 23.081 -18.850 38.520 1.00193.76 C ANISOU 1742 CD2 LEU A 254 26538 27996 19085 -2168 -2428 829 C ATOM 1743 N LYS A 255 23.861 -15.977 42.953 1.00185.90 N ANISOU 1743 N LYS A 255 26178 27464 16992 -3423 -3211 521 N ATOM 1744 CA LYS A 255 24.498 -15.685 44.226 1.00185.28 C ANISOU 1744 CA LYS A 255 26098 27753 16546 -3667 -3457 540 C ATOM 1745 C LYS A 255 23.599 -16.111 45.383 1.00183.22 C ANISOU 1745 C LYS A 255 26184 27215 16217 -3376 -3377 486 C ATOM 1746 O LYS A 255 22.379 -16.233 45.246 1.00183.76 O ANISOU 1746 O LYS A 255 26590 26741 16491 -3137 -3153 372 O ATOM 1747 CB LYS A 255 24.826 -14.196 44.338 1.00183.33 C ANISOU 1747 CB LYS A 255 26092 27484 16082 -4333 -3658 365 C ATOM 1748 CG LYS A 255 23.605 -13.290 44.351 1.00179.32 C ANISOU 1748 CG LYS A 255 26215 26272 15645 -4451 -3531 101 C ATOM 1749 N ILE A 256 24.225 -16.347 46.537 1.00174.59 N ANISOU 1749 N ILE A 256 24985 26536 14815 -3401 -3564 580 N ATOM 1750 CA ILE A 256 23.469 -16.681 47.738 1.00176.30 C ANISOU 1750 CA ILE A 256 25539 26534 14914 -3169 -3510 533 C ATOM 1751 C ILE A 256 22.629 -15.480 48.151 1.00179.49 C ANISOU 1751 C ILE A 256 26523 26447 15229 -3498 -3510 260 C ATOM 1752 O ILE A 256 23.142 -14.364 48.313 1.00177.94 O ANISOU 1752 O ILE A 256 26386 26275 14947 -3941 -3647 138 O ATOM 1753 CB ILE A 256 24.412 -17.139 48.862 1.00174.22 C ANISOU 1753 CB ILE A 256 25025 26864 14307 -3143 -3734 702 C ATOM 1754 CG1 ILE A 256 25.499 -16.095 49.133 1.00174.20 C ANISOU 1754 CG1 ILE A 256 24844 27203 14140 -3671 -3985 647 C ATOM 1755 CG2 ILE A 256 25.038 -18.483 48.517 1.00170.30 C ANISOU 1755 CG2 ILE A 256 24029 26774 13904 -2662 -3667 989 C ATOM 1756 CD1 ILE A 256 26.356 -16.406 50.339 1.00177.81 C ANISOU 1756 CD1 ILE A 256 25063 28153 14342 -3631 -4169 771 C ATOM 1757 N TYR A 257 21.325 -15.696 48.299 1.00221.16 N ANISOU 1757 N TYR A 257 32162 31196 20671 -3190 -3267 161 N ATOM 1758 CA TYR A 257 20.390 -14.619 48.580 1.00219.94 C ANISOU 1758 CA TYR A 257 32571 30537 20460 -3392 -3206 -84 C ATOM 1759 C TYR A 257 19.456 -15.018 49.712 1.00220.77 C ANISOU 1759 C TYR A 257 33000 30407 20474 -3085 -3081 -118 C ATOM 1760 O TYR A 257 19.180 -16.201 49.930 1.00221.89 O ANISOU 1760 O TYR A 257 32970 30609 20730 -2656 -2947 30 O ATOM 1761 CB TYR A 257 19.575 -14.244 47.330 1.00216.11 C ANISOU 1761 CB TYR A 257 32212 29597 20303 -3345 -2995 -190 C ATOM 1762 CG TYR A 257 18.485 -15.230 46.975 1.00215.18 C ANISOU 1762 CG TYR A 257 32076 29188 20496 -2832 -2703 -136 C ATOM 1763 CD1 TYR A 257 18.781 -16.410 46.305 1.00215.37 C ANISOU 1763 CD1 TYR A 257 31677 29412 20741 -2526 -2618 52 C ATOM 1764 CD2 TYR A 257 17.157 -14.975 47.295 1.00214.59 C ANISOU 1764 CD2 TYR A 257 32416 28647 20472 -2664 -2506 -271 C ATOM 1765 CE1 TYR A 257 17.789 -17.313 45.973 1.00215.04 C ANISOU 1765 CE1 TYR A 257 31654 29094 20959 -2117 -2358 94 C ATOM 1766 CE2 TYR A 257 16.158 -15.873 46.967 1.00215.03 C ANISOU 1766 CE2 TYR A 257 32431 28476 20793 -2251 -2248 -216 C ATOM 1767 CZ TYR A 257 16.479 -17.039 46.305 1.00216.28 C ANISOU 1767 CZ TYR A 257 32192 28820 21163 -2005 -2181 -39 C ATOM 1768 OH TYR A 257 15.488 -17.936 45.976 1.00214.97 O ANISOU 1768 OH TYR A 257 32022 28419 21237 -1650 -1932 9 O ATOM 1769 N LYS A 258 18.975 -14.008 50.431 1.00182.82 N ANISOU 1769 N LYS A 258 28581 25283 15598 -3238 -3050 -309 N ATOM 1770 CA LYS A 258 18.064 -14.220 51.546 1.00180.29 C ANISOU 1770 CA LYS A 258 28589 24731 15182 -2974 -2919 -358 C ATOM 1771 C LYS A 258 16.665 -14.527 51.027 1.00181.40 C ANISOU 1771 C LYS A 258 28972 24431 15522 -2650 -2633 -402 C ATOM 1772 O LYS A 258 16.157 -13.836 50.138 1.00181.96 O ANISOU 1772 O LYS A 258 29186 24185 15765 -2733 -2529 -518 O ATOM 1773 CB LYS A 258 18.039 -12.982 52.441 1.00174.89 C ANISOU 1773 CB LYS A 258 28243 23855 14351 -3241 -2970 -539 C ATOM 1774 CG LYS A 258 18.206 -11.682 51.669 1.00169.88 C ANISOU 1774 CG LYS A 258 27752 22983 13812 -3614 -2991 -686 C ATOM 1775 CD LYS A 258 18.501 -10.508 52.585 1.00160.96 C ANISOU 1775 CD LYS A 258 26930 21742 12487 -3940 -3088 -825 C ATOM 1776 CE LYS A 258 18.828 -9.261 51.778 1.00152.55 C ANISOU 1776 CE LYS A 258 26001 20465 11496 -4344 -3117 -932 C ATOM 1777 NZ LYS A 258 19.217 -8.115 52.644 1.00154.29 N ANISOU 1777 NZ LYS A 258 26545 20576 11503 -4708 -3218 -1049 N ATOM 1778 N ASP A 259 16.044 -15.563 51.581 1.00219.27 N ANISOU 1778 N ASP A 259 33786 29210 20315 -2271 -2491 -300 N ATOM 1779 CA ASP A 259 14.693 -15.944 51.196 1.00217.47 C ANISOU 1779 CA ASP A 259 33673 28599 20355 -1933 -2180 -320 C ATOM 1780 C ASP A 259 13.691 -15.137 52.026 1.00215.45 C ANISOU 1780 C ASP A 259 33933 28004 19926 -1914 -2068 -487 C ATOM 1781 O ASP A 259 14.038 -14.108 52.612 1.00211.76 O ANISOU 1781 O ASP A 259 33630 27500 19328 -2158 -2177 -609 O ATOM 1782 CB ASP A 259 14.518 -17.460 51.342 1.00217.70 C ANISOU 1782 CB ASP A 259 33429 28758 20529 -1542 -2044 -120 C ATOM 1783 CG ASP A 259 14.746 -17.947 52.762 1.00216.69 C ANISOU 1783 CG ASP A 259 33394 28830 20109 -1430 -2113 -40 C ATOM 1784 OD1 ASP A 259 15.157 -17.138 53.621 1.00218.31 O ANISOU 1784 OD1 ASP A 259 33831 29125 19991 -1677 -2297 -135 O ATOM 1785 OD2 ASP A 259 14.514 -19.147 53.021 1.00214.98 O ANISOU 1785 OD2 ASP A 259 33046 28669 19969 -1103 -1981 120 O ATOM 1786 N THR A 260 12.438 -15.593 52.087 1.00207.42 N ANISOU 1786 N THR A 260 33026 26731 19054 -1578 -1793 -477 N ATOM 1787 CA THR A 260 11.435 -14.878 52.868 1.00204.78 C ANISOU 1787 CA THR A 260 33101 26100 18606 -1485 -1640 -609 C ATOM 1788 C THR A 260 11.666 -15.042 54.365 1.00205.62 C ANISOU 1788 C THR A 260 33311 26347 18469 -1445 -1700 -583 C ATOM 1789 O THR A 260 11.345 -14.136 55.142 1.00206.26 O ANISOU 1789 O THR A 260 33689 26251 18429 -1496 -1671 -710 O ATOM 1790 CB THR A 260 10.033 -15.358 52.492 1.00199.77 C ANISOU 1790 CB THR A 260 32518 25227 18160 -1149 -1332 -584 C ATOM 1791 OG1 THR A 260 9.992 -16.790 52.520 1.00201.90 O ANISOU 1791 OG1 THR A 260 32455 25665 18591 -919 -1245 -396 O ATOM 1792 CG2 THR A 260 9.664 -14.873 51.098 1.00194.88 C ANISOU 1792 CG2 THR A 260 31813 24418 17814 -1190 -1253 -646 C ATOM 1793 N GLU A 261 12.218 -16.181 54.786 1.00196.73 N ANISOU 1793 N GLU A 261 31964 25528 17255 -1335 -1779 -413 N ATOM 1794 CA GLU A 261 12.515 -16.398 56.196 1.00196.33 C ANISOU 1794 CA GLU A 261 31988 25650 16960 -1289 -1853 -373 C ATOM 1795 C GLU A 261 13.803 -15.714 56.635 1.00197.50 C ANISOU 1795 C GLU A 261 32056 26070 16916 -1638 -2158 -420 C ATOM 1796 O GLU A 261 14.002 -15.509 57.837 1.00196.60 O ANISOU 1796 O GLU A 261 32077 26045 16578 -1669 -2230 -445 O ATOM 1797 CB GLU A 261 12.601 -17.899 56.490 1.00195.35 C ANISOU 1797 CB GLU A 261 31679 25742 16804 -1003 -1805 -153 C ATOM 1798 CG GLU A 261 12.379 -18.266 57.950 1.00192.63 C ANISOU 1798 CG GLU A 261 31484 25459 16247 -833 -1758 -106 C ATOM 1799 CD GLU A 261 11.112 -17.658 58.520 1.00189.73 C ANISOU 1799 CD GLU A 261 31460 24743 15886 -721 -1522 -239 C ATOM 1800 OE1 GLU A 261 10.035 -17.849 57.916 1.00184.98 O ANISOU 1800 OE1 GLU A 261 30916 23895 15474 -543 -1273 -243 O ATOM 1801 OE2 GLU A 261 11.194 -16.989 59.571 1.00185.76 O ANISOU 1801 OE2 GLU A 261 31163 24233 15185 -804 -1583 -332 O ATOM 1802 N GLY A 262 14.674 -15.353 55.694 1.00194.51 N ANISOU 1802 N GLY A 262 31453 25839 16613 -1914 -2334 -428 N ATOM 1803 CA GLY A 262 15.931 -14.699 55.989 1.00192.22 C ANISOU 1803 CA GLY A 262 31036 25843 16156 -2286 -2620 -460 C ATOM 1804 C GLY A 262 17.149 -15.575 55.795 1.00191.17 C ANISOU 1804 C GLY A 262 30446 26239 15951 -2313 -2835 -261 C ATOM 1805 O GLY A 262 18.268 -15.048 55.719 1.00191.59 O ANISOU 1805 O GLY A 262 30294 26590 15912 -2649 -3075 -269 O ATOM 1806 N TYR A 263 16.970 -16.890 55.713 1.00183.72 N ANISOU 1806 N TYR A 263 29344 25423 15040 -1960 -2746 -70 N ATOM 1807 CA TYR A 263 18.096 -17.791 55.531 1.00184.74 C ANISOU 1807 CA TYR A 263 29050 26058 15085 -1907 -2926 154 C ATOM 1808 C TYR A 263 18.649 -17.680 54.112 1.00190.53 C ANISOU 1808 C TYR A 263 29487 26898 16006 -2075 -2991 188 C ATOM 1809 O TYR A 263 17.960 -17.268 53.174 1.00192.52 O ANISOU 1809 O TYR A 263 29841 26782 16525 -2103 -2829 73 O ATOM 1810 CB TYR A 263 17.683 -19.234 55.819 1.00183.38 C ANISOU 1810 CB TYR A 263 28813 25907 14957 -1427 -2752 356 C ATOM 1811 CG TYR A 263 16.971 -19.427 57.140 1.00184.20 C ANISOU 1811 CG TYR A 263 29267 25865 14854 -1244 -2653 335 C ATOM 1812 CD1 TYR A 263 17.375 -18.740 58.277 1.00184.30 C ANISOU 1812 CD1 TYR A 263 29369 26025 14630 -1429 -2809 245 C ATOM 1813 CD2 TYR A 263 15.894 -20.297 57.248 1.00180.96 C ANISOU 1813 CD2 TYR A 263 28985 25163 14609 -863 -2352 400 C ATOM 1814 CE1 TYR A 263 16.726 -18.914 59.485 1.00185.06 C ANISOU 1814 CE1 TYR A 263 29736 25991 14586 -1242 -2692 227 C ATOM 1815 CE2 TYR A 263 15.239 -20.477 58.452 1.00175.48 C ANISOU 1815 CE2 TYR A 263 28598 24352 13724 -699 -2246 393 C ATOM 1816 CZ TYR A 263 15.659 -19.784 59.566 1.00184.64 C ANISOU 1816 CZ TYR A 263 29844 25667 14642 -876 -2408 305 C ATOM 1817 OH TYR A 263 15.010 -19.961 60.766 1.00191.52 O ANISOU 1817 OH TYR A 263 30964 26424 15380 -698 -2278 298 O ATOM 1818 N TYR A 264 19.915 -18.058 53.963 1.00218.21 N ANISOU 1818 N TYR A 264 32557 30932 19420 -2144 -3202 356 N ATOM 1819 CA TYR A 264 20.559 -18.014 52.658 1.00220.98 C ANISOU 1819 CA TYR A 264 32528 31443 19990 -2261 -3241 411 C ATOM 1820 C TYR A 264 20.068 -19.157 51.778 1.00215.99 C ANISOU 1820 C TYR A 264 31697 30642 19727 -1806 -2970 544 C ATOM 1821 O TYR A 264 20.143 -20.328 52.160 1.00214.76 O ANISOU 1821 O TYR A 264 31401 30633 19566 -1412 -2889 732 O ATOM 1822 CB TYR A 264 22.078 -18.080 52.809 1.00227.92 C ANISOU 1822 CB TYR A 264 32970 33002 20628 -2457 -3544 571 C ATOM 1823 CG TYR A 264 22.733 -16.742 53.067 1.00233.86 C ANISOU 1823 CG TYR A 264 33726 33832 21297 -2964 -3737 400 C ATOM 1824 CD1 TYR A 264 22.050 -15.555 52.833 1.00232.53 C ANISOU 1824 CD1 TYR A 264 33950 33162 21239 -3252 -3655 144 C ATOM 1825 CD2 TYR A 264 24.039 -16.665 53.533 1.00241.93 C ANISOU 1825 CD2 TYR A 264 34369 35421 22133 -3146 -3987 506 C ATOM 1826 CE1 TYR A 264 22.647 -14.329 53.063 1.00241.42 C ANISOU 1826 CE1 TYR A 264 35133 34312 22283 -3727 -3809 1 C ATOM 1827 CE2 TYR A 264 24.644 -15.445 53.766 1.00243.79 C ANISOU 1827 CE2 TYR A 264 34633 35705 22290 -3653 -4153 357 C ATOM 1828 CZ TYR A 264 23.944 -14.280 53.530 1.00245.78 C ANISOU 1828 CZ TYR A 264 35322 35419 22646 -3950 -4060 106 C ATOM 1829 OH TYR A 264 24.543 -13.063 53.760 1.00249.91 O ANISOU 1829 OH TYR A 264 35927 35952 23075 -4466 -4207 -28 O ATOM 1830 N THR A 265 19.562 -18.809 50.599 1.00203.63 N ANISOU 1830 N THR A 265 30152 28756 18464 -1867 -2828 444 N ATOM 1831 CA THR A 265 19.165 -19.776 49.589 1.00199.66 C ANISOU 1831 CA THR A 265 29462 28095 18304 -1518 -2594 549 C ATOM 1832 C THR A 265 19.937 -19.502 48.305 1.00198.32 C ANISOU 1832 C THR A 265 28958 28105 18289 -1696 -2667 579 C ATOM 1833 O THR A 265 20.415 -18.389 48.070 1.00198.94 O ANISOU 1833 O THR A 265 29047 28270 18272 -2122 -2842 465 O ATOM 1834 CB THR A 265 17.655 -19.724 49.319 1.00198.57 C ANISOU 1834 CB THR A 265 29662 27385 18400 -1381 -2319 411 C ATOM 1835 OG1 THR A 265 17.263 -18.375 49.036 1.00202.60 O ANISOU 1835 OG1 THR A 265 30431 27640 18908 -1724 -2357 191 O ATOM 1836 CG2 THR A 265 16.880 -20.228 50.528 1.00193.49 C ANISOU 1836 CG2 THR A 265 29295 26597 17625 -1141 -2203 425 C ATOM 1837 N ILE A 266 20.065 -20.536 47.473 1.00167.76 N ANISOU 1837 N ILE A 266 24818 24281 14641 -1372 -2524 735 N ATOM 1838 CA ILE A 266 20.798 -20.440 46.219 1.00166.73 C ANISOU 1838 CA ILE A 266 24351 24337 14663 -1469 -2560 791 C ATOM 1839 C ILE A 266 20.053 -21.221 45.146 1.00166.95 C ANISOU 1839 C ILE A 266 24382 24018 15032 -1161 -2286 816 C ATOM 1840 O ILE A 266 19.269 -22.129 45.432 1.00163.77 O ANISOU 1840 O ILE A 266 24140 23371 14713 -828 -2092 861 O ATOM 1841 CB ILE A 266 22.253 -20.951 46.351 1.00164.58 C ANISOU 1841 CB ILE A 266 23622 24711 14199 -1399 -2740 1023 C ATOM 1842 CG1 ILE A 266 23.158 -20.273 45.320 1.00168.53 C ANISOU 1842 CG1 ILE A 266 23803 25489 14740 -1718 -2870 1028 C ATOM 1843 CG2 ILE A 266 22.313 -22.466 46.211 1.00162.94 C ANISOU 1843 CG2 ILE A 266 23259 24568 14083 -845 -2561 1245 C ATOM 1844 CD1 ILE A 266 24.626 -20.584 45.497 1.00170.77 C ANISOU 1844 CD1 ILE A 266 23599 26492 14795 -1711 -3072 1255 C ATOM 1845 N GLY A 267 20.300 -20.844 43.895 1.00214.55 N ANISOU 1845 N GLY A 267 30248 30028 21244 -1304 -2275 784 N ATOM 1846 CA GLY A 267 19.680 -21.546 42.783 1.00212.90 C ANISOU 1846 CA GLY A 267 30031 29520 21340 -1050 -2037 804 C ATOM 1847 C GLY A 267 18.185 -21.305 42.747 1.00206.83 C ANISOU 1847 C GLY A 267 29638 28213 20736 -1045 -1857 629 C ATOM 1848 O GLY A 267 17.715 -20.162 42.738 1.00205.67 O ANISOU 1848 O GLY A 267 29698 27865 20583 -1334 -1903 447 O ATOM 1849 N ILE A 268 17.421 -22.396 42.730 1.00150.83 N ANISOU 1849 N ILE A 268 22644 20892 13773 -710 -1642 693 N ATOM 1850 CA ILE A 268 15.967 -22.323 42.656 1.00141.03 C ANISOU 1850 CA ILE A 268 21698 19200 12688 -681 -1454 560 C ATOM 1851 C ILE A 268 15.367 -22.753 43.988 1.00139.42 C ANISOU 1851 C ILE A 268 21719 18921 12332 -532 -1393 581 C ATOM 1852 O ILE A 268 14.760 -23.824 44.093 1.00134.59 O ANISOU 1852 O ILE A 268 21188 18153 11796 -271 -1207 664 O ATOM 1853 CB ILE A 268 15.429 -23.185 41.499 1.00129.20 C ANISOU 1853 CB ILE A 268 20157 17477 11457 -487 -1244 602 C ATOM 1854 CG1 ILE A 268 16.372 -23.107 40.298 1.00134.45 C ANISOU 1854 CG1 ILE A 268 20541 18326 12217 -542 -1309 654 C ATOM 1855 CG2 ILE A 268 14.028 -22.742 41.107 1.00123.54 C ANISOU 1855 CG2 ILE A 268 19660 16368 10910 -566 -1098 443 C ATOM 1856 CD1 ILE A 268 15.935 -23.948 39.121 1.00135.24 C ANISOU 1856 CD1 ILE A 268 20621 18212 12551 -361 -1114 691 C ATOM 1857 N GLY A 269 15.538 -21.922 45.013 1.00140.16 N ANISOU 1857 N GLY A 269 21942 19118 12196 -713 -1546 505 N ATOM 1858 CA GLY A 269 14.954 -22.207 46.310 1.00136.80 C ANISOU 1858 CA GLY A 269 21753 18620 11604 -587 -1490 512 C ATOM 1859 C GLY A 269 15.649 -23.294 47.098 1.00142.11 C ANISOU 1859 C GLY A 269 22319 19567 12108 -335 -1522 713 C ATOM 1860 O GLY A 269 15.011 -23.955 47.923 1.00133.81 O ANISOU 1860 O GLY A 269 21457 18393 10992 -136 -1392 762 O ATOM 1861 N HIS A 270 16.944 -23.501 46.868 1.00181.51 N ANISOU 1861 N HIS A 270 27008 24945 17013 -323 -1683 843 N ATOM 1862 CA HIS A 270 17.715 -24.497 47.604 1.00183.64 C ANISOU 1862 CA HIS A 270 27154 25532 17089 -43 -1726 1058 C ATOM 1863 C HIS A 270 18.283 -23.846 48.859 1.00187.83 C ANISOU 1863 C HIS A 270 27716 26363 17286 -217 -1963 1042 C ATOM 1864 O HIS A 270 19.229 -23.055 48.784 1.00193.44 O ANISOU 1864 O HIS A 270 28226 27407 17865 -493 -2200 1021 O ATOM 1865 CB HIS A 270 18.828 -25.077 46.735 1.00184.03 C ANISOU 1865 CB HIS A 270 26840 25898 17186 107 -1770 1231 C ATOM 1866 CG HIS A 270 19.763 -25.981 47.478 1.00185.80 C ANISOU 1866 CG HIS A 270 26905 26521 17171 416 -1838 1469 C ATOM 1867 ND1 HIS A 270 20.976 -25.553 47.972 1.00191.23 N ANISOU 1867 ND1 HIS A 270 27312 27749 17596 297 -2106 1555 N ATOM 1868 CD2 HIS A 270 19.661 -27.289 47.813 1.00185.61 C ANISOU 1868 CD2 HIS A 270 26973 26442 17109 842 -1672 1649 C ATOM 1869 CE1 HIS A 270 21.582 -26.558 48.579 1.00189.32 C ANISOU 1869 CE1 HIS A 270 26970 27797 17167 673 -2105 1786 C ATOM 1870 NE2 HIS A 270 20.805 -27.623 48.496 1.00189.64 N ANISOU 1870 NE2 HIS A 270 27256 27460 17338 1019 -1836 1846 N ATOM 1871 N LEU A 271 17.705 -24.176 50.010 1.00152.66 N ANISOU 1871 N LEU A 271 23522 21799 12681 -79 -1898 1052 N ATOM 1872 CA LEU A 271 18.186 -23.635 51.272 1.00153.43 C ANISOU 1872 CA LEU A 271 23693 22168 12437 -225 -2114 1037 C ATOM 1873 C LEU A 271 19.576 -24.174 51.588 1.00159.67 C ANISOU 1873 C LEU A 271 24143 23519 13004 -93 -2308 1258 C ATOM 1874 O LEU A 271 19.846 -25.369 51.441 1.00157.05 O ANISOU 1874 O LEU A 271 23682 23283 12708 297 -2193 1466 O ATOM 1875 CB LEU A 271 17.216 -23.982 52.402 1.00148.20 C ANISOU 1875 CB LEU A 271 23389 21257 11665 -59 -1970 1018 C ATOM 1876 CG LEU A 271 17.771 -23.934 53.827 1.00145.82 C ANISOU 1876 CG LEU A 271 23158 21268 10979 -55 -2154 1082 C ATOM 1877 CD1 LEU A 271 17.997 -22.498 54.270 1.00153.38 C ANISOU 1877 CD1 LEU A 271 24239 22306 11731 -493 -2386 886 C ATOM 1878 CD2 LEU A 271 16.842 -24.657 54.790 1.00134.90 C ANISOU 1878 CD2 LEU A 271 22087 19642 9525 218 -1951 1128 C ATOM 1879 N LEU A 272 20.465 -23.278 52.018 1.00188.07 N ANISOU 1879 N LEU A 272 27607 27502 16349 -421 -2601 1220 N ATOM 1880 CA LEU A 272 21.810 -23.691 52.401 1.00194.54 C ANISOU 1880 CA LEU A 272 28060 28944 16912 -324 -2815 1438 C ATOM 1881 C LEU A 272 21.824 -24.245 53.822 1.00194.56 C ANISOU 1881 C LEU A 272 28214 29097 16613 -98 -2856 1548 C ATOM 1882 O LEU A 272 22.173 -25.409 54.044 1.00195.46 O ANISOU 1882 O LEU A 272 28203 29397 16667 341 -2780 1784 O ATOM 1883 CB LEU A 272 22.787 -22.518 52.270 1.00200.58 C ANISOU 1883 CB LEU A 272 28594 30112 17506 -823 -3127 1363 C ATOM 1884 CG LEU A 272 23.345 -22.209 50.876 1.00194.00 C ANISOU 1884 CG LEU A 272 27430 29397 16886 -986 -3147 1369 C ATOM 1885 CD1 LEU A 272 24.055 -23.427 50.303 1.00198.45 C ANISOU 1885 CD1 LEU A 272 27602 30278 17521 -531 -3061 1646 C ATOM 1886 CD2 LEU A 272 22.271 -21.702 49.925 1.00187.96 C ANISOU 1886 CD2 LEU A 272 26928 28029 16459 -1115 -2945 1156 C ATOM 1887 N THR A 273 21.444 -23.419 54.794 1.00203.46 N ANISOU 1887 N THR A 273 29645 30130 17532 -376 -2966 1382 N ATOM 1888 CA THR A 273 21.361 -23.847 56.182 1.00212.10 C ANISOU 1888 CA THR A 273 30933 31329 18327 -189 -3000 1463 C ATOM 1889 C THR A 273 20.500 -22.856 56.951 1.00214.14 C ANISOU 1889 C THR A 273 31646 31249 18468 -488 -3009 1212 C ATOM 1890 O THR A 273 20.536 -21.653 56.681 1.00212.99 O ANISOU 1890 O THR A 273 31583 31039 18306 -928 -3141 1010 O ATOM 1891 CB THR A 273 22.750 -23.960 56.826 1.00220.44 C ANISOU 1891 CB THR A 273 31645 33096 19018 -202 -3309 1651 C ATOM 1892 OG1 THR A 273 22.612 -24.239 58.225 1.00221.04 O ANISOU 1892 OG1 THR A 273 31956 33251 18777 -62 -3358 1702 O ATOM 1893 CG2 THR A 273 23.541 -22.670 56.639 1.00227.26 C ANISOU 1893 CG2 THR A 273 32334 34284 19732 -778 -3622 1519 C ATOM 1894 N LYS A 274 19.718 -23.373 57.901 1.00207.29 N ANISOU 1894 N LYS A 274 31100 30153 17507 -234 -2853 1232 N ATOM 1895 CA LYS A 274 18.907 -22.513 58.752 1.00203.45 C ANISOU 1895 CA LYS A 274 31063 29375 16865 -448 -2841 1019 C ATOM 1896 C LYS A 274 19.707 -21.911 59.898 1.00207.19 C ANISOU 1896 C LYS A 274 31547 30240 16936 -680 -3138 992 C ATOM 1897 O LYS A 274 19.288 -20.894 60.461 1.00209.42 O ANISOU 1897 O LYS A 274 32076 30309 17184 -931 -3143 764 O ATOM 1898 CB LYS A 274 17.713 -23.292 59.309 1.00199.05 C ANISOU 1898 CB LYS A 274 30822 28430 16378 -91 -2530 1052 C ATOM 1899 CG LYS A 274 18.094 -24.514 60.128 1.00199.89 C ANISOU 1899 CG LYS A 274 30865 28788 16296 301 -2512 1307 C ATOM 1900 N SER A 275 20.839 -22.511 60.252 1.00203.40 N ANISOU 1900 N SER A 275 30731 30313 16239 -554 -3339 1211 N ATOM 1901 CA SER A 275 21.674 -21.957 61.305 1.00209.34 C ANISOU 1901 CA SER A 275 31378 31446 16715 -733 -3596 1170 C ATOM 1902 C SER A 275 22.367 -20.690 60.807 1.00215.78 C ANISOU 1902 C SER A 275 32020 32377 17588 -1245 -3811 984 C ATOM 1903 O SER A 275 22.818 -20.638 59.659 1.00214.84 O ANISOU 1903 O SER A 275 31612 32369 17648 -1360 -3850 1028 O ATOM 1904 CB SER A 275 22.715 -22.981 61.758 1.00208.79 C ANISOU 1904 CB SER A 275 30980 31922 16428 -404 -3743 1466 C ATOM 1905 OG SER A 275 23.643 -22.403 62.659 1.00208.85 O ANISOU 1905 OG SER A 275 30862 32294 16198 -615 -4027 1420 O ATOM 1906 N PRO A 276 22.465 -19.655 61.643 1.00237.95 N ANISOU 1906 N PRO A 276 35014 35149 20248 -1569 -3940 782 N ATOM 1907 CA PRO A 276 23.105 -18.408 61.199 1.00242.18 C ANISOU 1907 CA PRO A 276 35447 35741 20831 -2095 -4125 606 C ATOM 1908 C PRO A 276 24.609 -18.553 61.038 1.00255.02 C ANISOU 1908 C PRO A 276 36543 37999 22354 -2225 -4407 772 C ATOM 1909 O PRO A 276 25.381 -18.049 61.860 1.00265.24 O ANISOU 1909 O PRO A 276 37767 39586 23425 -2473 -4635 736 O ATOM 1910 CB PRO A 276 22.753 -17.410 62.315 1.00242.08 C ANISOU 1910 CB PRO A 276 35839 35499 20642 -2347 -4159 377 C ATOM 1911 CG PRO A 276 21.709 -18.098 63.166 1.00238.24 C ANISOU 1911 CG PRO A 276 35676 34762 20082 -1939 -3938 409 C ATOM 1912 CD PRO A 276 21.972 -19.558 63.024 1.00235.83 C ANISOU 1912 CD PRO A 276 35085 34763 19757 -1482 -3902 707 C ATOM 1913 N SER A 277 25.036 -19.239 59.980 1.00230.54 N ANISOU 1913 N SER A 277 33058 35120 19417 -2060 -4384 961 N ATOM 1914 CA SER A 277 26.452 -19.472 59.704 1.00231.63 C ANISOU 1914 CA SER A 277 32624 35885 19498 -2128 -4608 1153 C ATOM 1915 C SER A 277 26.712 -19.138 58.238 1.00229.82 C ANISOU 1915 C SER A 277 32128 35662 19530 -2345 -4579 1144 C ATOM 1916 O SER A 277 26.380 -19.925 57.347 1.00229.83 O ANISOU 1916 O SER A 277 32025 35587 19713 -2025 -4405 1275 O ATOM 1917 CB SER A 277 26.847 -20.910 60.024 1.00231.92 C ANISOU 1917 CB SER A 277 32402 36280 19437 -1565 -4585 1471 C ATOM 1918 OG SER A 277 26.703 -21.184 61.406 1.00237.49 O ANISOU 1918 OG SER A 277 33349 37007 19880 -1387 -4633 1487 O ATOM 1919 N LEU A 278 27.306 -17.967 57.992 1.00217.59 N ANISOU 1919 N LEU A 278 30490 34196 17990 -2900 -4739 994 N ATOM 1920 CA LEU A 278 27.634 -17.571 56.628 1.00213.46 C ANISOU 1920 CA LEU A 278 29709 33702 17694 -3147 -4722 987 C ATOM 1921 C LEU A 278 28.736 -18.432 56.027 1.00220.41 C ANISOU 1921 C LEU A 278 29944 35207 18596 -2925 -4793 1285 C ATOM 1922 O LEU A 278 28.817 -18.544 54.799 1.00217.82 O ANISOU 1922 O LEU A 278 29395 34889 18476 -2914 -4704 1342 O ATOM 1923 CB LEU A 278 28.033 -16.092 56.594 1.00204.96 C ANISOU 1923 CB LEU A 278 28730 32553 16594 -3814 -4864 770 C ATOM 1924 CG LEU A 278 29.150 -15.617 57.531 1.00204.41 C ANISOU 1924 CG LEU A 278 28451 32960 16257 -4157 -5135 794 C ATOM 1925 CD1 LEU A 278 30.524 -15.728 56.878 1.00206.41 C ANISOU 1925 CD1 LEU A 278 28037 33873 16517 -4336 -5290 998 C ATOM 1926 CD2 LEU A 278 28.887 -14.192 57.995 1.00191.38 C ANISOU 1926 CD2 LEU A 278 27262 30925 14529 -4706 -5186 510 C ATOM 1927 N ASN A 279 29.583 -19.041 56.859 1.00264.94 N ANISOU 1927 N ASN A 279 35276 41366 24022 -2725 -4938 1482 N ATOM 1928 CA ASN A 279 30.629 -19.918 56.347 1.00267.92 C ANISOU 1928 CA ASN A 279 35032 42349 24416 -2433 -4971 1788 C ATOM 1929 C ASN A 279 30.078 -21.293 55.990 1.00265.27 C ANISOU 1929 C ASN A 279 34714 41891 24187 -1747 -4735 1987 C ATOM 1930 O ASN A 279 30.511 -21.900 55.004 1.00264.25 O ANISOU 1930 O ASN A 279 34205 41999 24198 -1496 -4644 2175 O ATOM 1931 CB ASN A 279 31.758 -20.044 57.370 1.00267.34 C ANISOU 1931 CB ASN A 279 34616 42887 24074 -2462 -5202 1934 C ATOM 1932 N ALA A 280 29.125 -21.798 56.778 1.00198.72 N ANISOU 1932 N ALA A 280 26736 33084 15683 -1436 -4614 1955 N ATOM 1933 CA ALA A 280 28.517 -23.088 56.477 1.00192.54 C ANISOU 1933 CA ALA A 280 26041 32120 14996 -817 -4359 2139 C ATOM 1934 C ALA A 280 27.683 -23.050 55.205 1.00192.12 C ANISOU 1934 C ALA A 280 26137 31650 15211 -819 -4145 2056 C ATOM 1935 O ALA A 280 27.464 -24.100 54.592 1.00189.72 O ANISOU 1935 O ALA A 280 25761 31300 15024 -338 -3936 2240 O ATOM 1936 CB ALA A 280 27.655 -23.554 57.651 1.00185.05 C ANISOU 1936 CB ALA A 280 25566 30850 13893 -550 -4269 2117 C ATOM 1937 N ALA A 281 27.210 -21.869 54.799 1.00237.83 N ANISOU 1937 N ALA A 281 32154 37109 21101 -1335 -4179 1783 N ATOM 1938 CA ALA A 281 26.483 -21.762 53.538 1.00238.57 C ANISOU 1938 CA ALA A 281 32366 36829 21450 -1377 -3995 1704 C ATOM 1939 C ALA A 281 27.404 -22.017 52.352 1.00239.92 C ANISOU 1939 C ALA A 281 32007 37401 21751 -1323 -4010 1874 C ATOM 1940 O ALA A 281 26.985 -22.604 51.347 1.00239.27 O ANISOU 1940 O ALA A 281 31909 37060 21944 -1031 -3774 1924 O ATOM 1941 CB ALA A 281 25.824 -20.388 53.425 1.00238.61 C ANISOU 1941 CB ALA A 281 32758 36368 21535 -1923 -4022 1372 C ATOM 1942 N LYS A 355 28.663 -21.587 52.449 1.00202.14 N ANISOU 1942 N LYS A 355 26781 33149 16874 -1572 -4230 1938 N ATOM 1943 CA LYS A 355 29.624 -21.858 51.387 1.00196.41 C ANISOU 1943 CA LYS A 355 25508 32870 16249 -1497 -4236 2125 C ATOM 1944 C LYS A 355 30.133 -23.292 51.433 1.00202.50 C ANISOU 1944 C LYS A 355 25965 33999 16977 -809 -4125 2453 C ATOM 1945 O LYS A 355 30.394 -23.885 50.380 1.00197.81 O ANISOU 1945 O LYS A 355 25106 33532 16522 -511 -3985 2612 O ATOM 1946 CB LYS A 355 30.799 -20.882 51.478 1.00189.66 C ANISOU 1946 CB LYS A 355 24274 32485 15302 -2033 -4488 2092 C ATOM 1947 N SER A 387 30.273 -23.866 52.630 1.00254.38 N ANISOU 1947 N SER A 387 32592 40705 23356 -527 -4169 2556 N ATOM 1948 CA SER A 387 30.771 -25.233 52.742 1.00255.15 C ANISOU 1948 CA SER A 387 32442 41092 23410 154 -4044 2867 C ATOM 1949 C SER A 387 29.716 -26.241 52.303 1.00253.68 C ANISOU 1949 C SER A 387 32624 40394 23369 676 -3726 2922 C ATOM 1950 O SER A 387 30.017 -27.187 51.566 1.00252.69 O ANISOU 1950 O SER A 387 32304 40364 23344 1166 -3542 3132 O ATOM 1951 CB SER A 387 31.220 -25.511 54.177 1.00257.20 C ANISOU 1951 CB SER A 387 32684 41623 23416 277 -4184 2955 C ATOM 1952 OG SER A 387 30.107 -25.619 55.047 1.00258.82 O ANISOU 1952 OG SER A 387 33464 41320 23556 340 -4111 2825 O ATOM 1953 N GLU A 407 28.471 -26.057 52.751 1.00217.26 N ANISOU 1953 N GLU A 407 28560 35226 18762 583 -3640 2735 N ATOM 1954 CA GLU A 407 27.403 -26.971 52.358 1.00209.28 C ANISOU 1954 CA GLU A 407 27925 33621 17971 1019 -3298 2744 C ATOM 1955 C GLU A 407 27.118 -26.893 50.864 1.00206.93 C ANISOU 1955 C GLU A 407 27580 32990 18054 972 -3110 2656 C ATOM 1956 O GLU A 407 26.715 -27.892 50.258 1.00203.19 O ANISOU 1956 O GLU A 407 27231 32186 17785 1418 -2826 2746 O ATOM 1957 CB GLU A 407 26.134 -26.675 53.156 1.00203.72 C ANISOU 1957 CB GLU A 407 27786 32314 17306 863 -3211 2514 C ATOM 1958 CG GLU A 407 26.079 -27.359 54.513 1.00203.43 C ANISOU 1958 CG GLU A 407 27933 32386 16974 1184 -3227 2652 C ATOM 1959 CD GLU A 407 26.100 -28.871 54.404 1.00197.97 C ANISOU 1959 CD GLU A 407 27270 31633 16315 1875 -2974 2917 C ATOM 1960 OE1 GLU A 407 25.284 -29.425 53.638 1.00192.63 O ANISOU 1960 OE1 GLU A 407 26838 30398 15953 2066 -2673 2869 O ATOM 1961 OE2 GLU A 407 26.932 -29.505 55.087 1.00197.79 O ANISOU 1961 OE2 GLU A 407 27045 31993 16114 2178 -3045 3132 O ATOM 1962 N LEU A 420 27.318 -25.722 50.256 1.00206.79 N ANISOU 1962 N LEU A 420 27415 33038 18117 425 -3262 2482 N ATOM 1963 CA LEU A 420 27.143 -25.599 48.813 1.00203.15 C ANISOU 1963 CA LEU A 420 26878 32318 17992 371 -3103 2412 C ATOM 1964 C LEU A 420 28.249 -26.335 48.067 1.00203.61 C ANISOU 1964 C LEU A 420 26446 32894 18021 738 -3076 2694 C ATOM 1965 O LEU A 420 27.979 -27.122 47.152 1.00200.90 O ANISOU 1965 O LEU A 420 26156 32264 17914 1110 -2814 2759 O ATOM 1966 CB LEU A 420 27.109 -24.125 48.411 1.00199.58 C ANISOU 1966 CB LEU A 420 26424 31810 17597 -310 -3275 2164 C ATOM 1967 CG LEU A 420 27.257 -23.828 46.918 1.00199.62 C ANISOU 1967 CG LEU A 420 26238 31731 17878 -438 -3184 2123 C ATOM 1968 CD1 LEU A 420 25.970 -24.157 46.175 1.00191.40 C ANISOU 1968 CD1 LEU A 420 25590 29929 17205 -265 -2874 1974 C ATOM 1969 CD2 LEU A 420 27.655 -22.377 46.695 1.00199.33 C ANISOU 1969 CD2 LEU A 420 26100 31866 17772 -1123 -3423 1955 C ATOM 1970 N ASP A 421 29.506 -26.093 48.450 1.00220.91 N ANISOU 1970 N ASP A 421 28160 35872 19904 641 -3344 2871 N ATOM 1971 CA ASP A 421 30.627 -26.774 47.812 1.00220.12 C ANISOU 1971 CA ASP A 421 27547 36356 19731 1027 -3321 3169 C ATOM 1972 C ASP A 421 30.656 -28.262 48.130 1.00220.73 C ANISOU 1972 C ASP A 421 27708 36426 19735 1808 -3108 3428 C ATOM 1973 O ASP A 421 31.284 -29.028 47.391 1.00220.26 O ANISOU 1973 O ASP A 421 27381 36578 19729 2253 -2957 3639 O ATOM 1974 CB ASP A 421 31.945 -26.124 48.234 1.00224.61 C ANISOU 1974 CB ASP A 421 27579 37651 20112 692 -3611 3244 C ATOM 1975 CG ASP A 421 31.994 -24.644 47.909 1.00222.21 C ANISOU 1975 CG ASP A 421 27227 37355 19846 -101 -3817 3001 C ATOM 1976 OD1 ASP A 421 31.363 -24.231 46.914 1.00219.32 O ANISOU 1976 OD1 ASP A 421 27041 36635 19656 -302 -3727 2863 O ATOM 1977 OD2 ASP A 421 32.668 -23.893 48.646 1.00225.36 O ANISOU 1977 OD2 ASP A 421 27434 38096 20097 -528 -4058 2946 O ATOM 1978 N LYS A 422 29.999 -28.688 49.211 1.00219.82 N ANISOU 1978 N LYS A 422 27986 36007 19527 1980 -3064 3400 N ATOM 1979 CA LYS A 422 29.917 -30.113 49.512 1.00215.00 C ANISOU 1979 CA LYS A 422 27556 35232 18902 2688 -2816 3610 C ATOM 1980 C LYS A 422 29.040 -30.835 48.496 1.00213.28 C ANISOU 1980 C LYS A 422 27702 34367 18966 2994 -2470 3574 C ATOM 1981 O LYS A 422 29.337 -31.971 48.106 1.00213.18 O ANISOU 1981 O LYS A 422 27695 34368 18936 3595 -2256 3802 O ATOM 1982 CB LYS A 422 29.388 -30.315 50.934 1.00210.95 C ANISOU 1982 CB LYS A 422 27398 34514 18238 2726 -2850 3567 C ATOM 1983 CG LYS A 422 28.519 -31.548 51.128 1.00205.88 C ANISOU 1983 CG LYS A 422 27257 33308 17660 3263 -2529 3642 C ATOM 1984 CD LYS A 422 29.363 -32.794 51.342 1.00204.44 C ANISOU 1984 CD LYS A 422 26906 33365 17407 3899 -2394 3930 C ATOM 1985 CE LYS A 422 28.495 -33.999 51.667 1.00202.68 C ANISOU 1985 CE LYS A 422 27237 32535 17236 4363 -2078 3986 C ATOM 1986 NZ LYS A 422 29.293 -35.253 51.752 1.00205.07 N ANISOU 1986 NZ LYS A 422 27428 33012 17478 5011 -1906 4256 N ATOM 1987 N ALA A 423 27.964 -30.187 48.047 1.00186.76 N ANISOU 1987 N ALA A 423 24666 30386 15910 2569 -2392 3267 N ATOM 1988 CA ALA A 423 27.077 -30.800 47.064 1.00177.43 C ANISOU 1988 CA ALA A 423 23824 28536 15055 2759 -2067 3185 C ATOM 1989 C ALA A 423 27.687 -30.769 45.668 1.00178.32 C ANISOU 1989 C ALA A 423 23615 28814 15324 2804 -2006 3241 C ATOM 1990 O ALA A 423 27.760 -31.801 44.992 1.00176.45 O ANISOU 1990 O ALA A 423 23462 28426 15156 3290 -1760 3390 O ATOM 1991 CB ALA A 423 25.718 -30.097 47.073 1.00167.10 C ANISOU 1991 CB ALA A 423 22927 26572 13992 2307 -2013 2857 C ATOM 1992 N ILE A 424 28.133 -29.595 45.219 1.00214.85 N ANISOU 1992 N ILE A 424 27907 33736 19991 2297 -2217 3125 N ATOM 1993 CA ILE A 424 28.725 -29.454 43.893 1.00218.91 C ANISOU 1993 CA ILE A 424 28099 34432 20646 2287 -2168 3171 C ATOM 1994 C ILE A 424 30.158 -29.969 43.924 1.00225.57 C ANISOU 1994 C ILE A 424 28422 36074 21212 2683 -2247 3509 C ATOM 1995 O ILE A 424 30.640 -30.438 44.961 1.00222.61 O ANISOU 1995 O ILE A 424 27955 36085 20543 2968 -2340 3701 O ATOM 1996 CB ILE A 424 28.668 -27.996 43.403 1.00214.63 C ANISOU 1996 CB ILE A 424 27417 33900 20233 1585 -2354 2930 C ATOM 1997 CG1 ILE A 424 29.495 -27.090 44.316 1.00220.73 C ANISOU 1997 CG1 ILE A 424 27857 35307 20704 1183 -2706 2955 C ATOM 1998 CG2 ILE A 424 27.225 -27.517 43.326 1.00208.59 C ANISOU 1998 CG2 ILE A 424 27163 32359 19731 1270 -2252 2617 C ATOM 1999 CD1 ILE A 424 29.275 -25.611 44.074 1.00219.88 C ANISOU 1999 CD1 ILE A 424 27768 35094 20682 447 -2887 2687 C ATOM 2000 N GLY A 425 30.848 -29.883 42.791 1.00250.75 N ANISOU 2000 N GLY A 425 31257 39541 24477 2720 -2205 3595 N ATOM 2001 CA GLY A 425 32.171 -30.449 42.638 1.00254.20 C ANISOU 2001 CA GLY A 425 31185 40732 24668 3168 -2225 3937 C ATOM 2002 C GLY A 425 33.333 -29.485 42.745 1.00254.08 C ANISOU 2002 C GLY A 425 30523 41573 24442 2758 -2545 4023 C ATOM 2003 O GLY A 425 34.464 -29.874 42.431 1.00256.23 O ANISOU 2003 O GLY A 425 30304 42456 24594 3079 -2526 4279 O ATOM 2004 N ARG A 426 33.103 -28.247 43.175 1.00199.45 N ANISOU 2004 N ARG A 426 23607 34650 17524 2033 -2803 3790 N ATOM 2005 CA ARG A 426 34.187 -27.282 43.313 1.00196.23 C ANISOU 2005 CA ARG A 426 22635 34985 16938 1540 -3101 3835 C ATOM 2006 C ARG A 426 33.752 -26.186 44.274 1.00198.79 C ANISOU 2006 C ARG A 426 23174 35164 17195 864 -3363 3577 C ATOM 2007 O ARG A 426 32.578 -26.077 44.638 1.00199.73 O ANISOU 2007 O ARG A 426 23845 34634 17410 765 -3308 3365 O ATOM 2008 CB ARG A 426 34.590 -26.693 41.957 1.00189.04 C ANISOU 2008 CB ARG A 426 21419 34250 16156 1264 -3085 3824 C ATOM 2009 CG ARG A 426 33.430 -26.151 41.139 1.00182.06 C ANISOU 2009 CG ARG A 426 21020 32499 15657 925 -2935 3492 C ATOM 2010 CD ARG A 426 33.926 -25.278 39.998 1.00171.37 C ANISOU 2010 CD ARG A 426 19347 31353 14411 484 -2982 3442 C ATOM 2011 NE ARG A 426 32.830 -24.665 39.257 1.00166.54 N ANISOU 2011 NE ARG A 426 19194 29946 14138 139 -2863 3127 N ATOM 2012 CZ ARG A 426 32.987 -23.781 38.282 1.00160.79 C ANISOU 2012 CZ ARG A 426 18341 29211 13541 -310 -2891 3020 C ATOM 2013 NH1 ARG A 426 34.188 -23.380 37.900 1.00148.19 N ANISOU 2013 NH1 ARG A 426 16172 28355 11779 -515 -3028 3193 N ATOM 2014 NH2 ARG A 426 31.912 -23.285 37.676 1.00158.78 N ANISOU 2014 NH2 ARG A 426 18539 28212 13579 -558 -2775 2743 N ATOM 2015 N ASN A 427 34.724 -25.369 44.682 1.00235.58 N ANISOU 2015 N ASN A 427 27406 40371 21731 391 -3608 3577 N ATOM 2016 CA ASN A 427 34.472 -24.246 45.585 1.00234.07 C ANISOU 2016 CA ASN A 427 27416 40063 21457 -285 -3858 3330 C ATOM 2017 C ASN A 427 34.179 -23.004 44.748 1.00235.72 C ANISOU 2017 C ASN A 427 27721 40043 21797 -967 -3935 3093 C ATOM 2018 O ASN A 427 35.039 -22.156 44.501 1.00237.05 O ANISOU 2018 O ASN A 427 27521 40619 21929 -1466 -4086 3082 O ATOM 2019 CB ASN A 427 35.654 -24.033 46.523 1.00235.06 C ANISOU 2019 CB ASN A 427 27091 40857 21364 -448 -4068 3449 C ATOM 2020 CG ASN A 427 35.836 -25.177 47.500 1.00238.33 C ANISOU 2020 CG ASN A 427 27493 41427 21633 188 -4005 3651 C ATOM 2021 OD1 ASN A 427 35.363 -25.121 48.635 1.00242.82 O ANISOU 2021 OD1 ASN A 427 28397 41772 22093 125 -4099 3548 O ATOM 2022 ND2 ASN A 427 36.527 -26.224 47.063 1.00238.06 N ANISOU 2022 ND2 ASN A 427 27098 41763 21590 822 -3831 3942 N ATOM 2023 N THR A 428 32.925 -22.905 44.304 1.00232.69 N ANISOU 2023 N THR A 428 27861 38983 21566 -991 -3811 2904 N ATOM 2024 CA THR A 428 32.495 -21.768 43.499 1.00228.27 C ANISOU 2024 CA THR A 428 27493 38051 21189 -1583 -3830 2650 C ATOM 2025 C THR A 428 32.371 -20.484 44.307 1.00229.86 C ANISOU 2025 C THR A 428 27931 38137 21270 -2290 -4067 2402 C ATOM 2026 O THR A 428 32.247 -19.410 43.707 1.00226.63 O ANISOU 2026 O THR A 428 27639 37518 20953 -2841 -4117 2212 O ATOM 2027 CB THR A 428 31.156 -22.074 42.825 1.00221.31 C ANISOU 2027 CB THR A 428 27135 36255 20698 -1339 -3516 2457 C ATOM 2028 OG1 THR A 428 30.166 -22.345 43.826 1.00222.67 O ANISOU 2028 OG1 THR A 428 27793 35948 20865 -1188 -3466 2334 O ATOM 2029 CG2 THR A 428 31.283 -23.278 41.906 1.00215.08 C ANISOU 2029 CG2 THR A 428 26178 35454 20089 -686 -3240 2658 C ATOM 2030 N ASN A 429 32.400 -20.570 45.640 1.00229.70 N ANISOU 2030 N ASN A 429 28023 38173 21080 -2261 -4178 2387 N ATOM 2031 CA ASN A 429 32.260 -19.406 46.517 1.00224.90 C ANISOU 2031 CA ASN A 429 27705 37371 20376 -2865 -4362 2140 C ATOM 2032 C ASN A 429 30.948 -18.669 46.253 1.00219.66 C ANISOU 2032 C ASN A 429 27679 35925 19855 -3142 -4279 1835 C ATOM 2033 O ASN A 429 30.875 -17.441 46.334 1.00218.99 O ANISOU 2033 O ASN A 429 27823 35608 19775 -3727 -4376 1610 O ATOM 2034 CB ASN A 429 33.455 -18.459 46.382 1.00224.90 C ANISOU 2034 CB ASN A 429 27292 37861 20298 -3442 -4546 2152 C ATOM 2035 CG ASN A 429 34.711 -19.011 47.029 1.00226.37 C ANISOU 2035 CG ASN A 429 26904 38821 20287 -3254 -4662 2419 C ATOM 2036 OD1 ASN A 429 34.935 -18.833 48.226 1.00224.68 O ANISOU 2036 OD1 ASN A 429 26748 38735 19884 -3381 -4812 2389 O ATOM 2037 ND2 ASN A 429 35.537 -19.685 46.238 1.00229.62 N ANISOU 2037 ND2 ASN A 429 26759 39757 20730 -2929 -4583 2685 N ATOM 2038 N GLY A 430 29.902 -19.427 45.934 1.00165.23 N ANISOU 2038 N GLY A 430 21090 28616 13075 -2708 -4078 1835 N ATOM 2039 CA GLY A 430 28.600 -18.859 45.662 1.00155.66 C ANISOU 2039 CA GLY A 430 20457 26577 12109 -2848 -3913 1547 C ATOM 2040 C GLY A 430 28.318 -18.544 44.211 1.00156.16 C ANISOU 2040 C GLY A 430 20525 26311 12497 -2929 -3744 1464 C ATOM 2041 O GLY A 430 27.306 -17.893 43.924 1.00151.52 O ANISOU 2041 O GLY A 430 20392 25090 12087 -3108 -3635 1223 O ATOM 2042 N VAL A 431 29.172 -18.982 43.287 1.00218.42 N ANISOU 2042 N VAL A 431 27922 34618 20451 -2781 -3711 1663 N ATOM 2043 CA VAL A 431 28.979 -18.705 41.868 1.00220.62 C ANISOU 2043 CA VAL A 431 28183 34622 21020 -2853 -3553 1598 C ATOM 2044 C VAL A 431 28.693 -20.007 41.132 1.00216.99 C ANISOU 2044 C VAL A 431 27628 34005 20814 -2184 -3268 1744 C ATOM 2045 O VAL A 431 29.558 -20.539 40.426 1.00215.02 O ANISOU 2045 O VAL A 431 26933 34194 20572 -1965 -3229 1957 O ATOM 2046 CB VAL A 431 30.201 -17.987 41.266 1.00222.25 C ANISOU 2046 CB VAL A 431 27937 35419 21090 -3313 -3739 1688 C ATOM 2047 CG1 VAL A 431 29.856 -17.399 39.904 1.00222.29 C ANISOU 2047 CG1 VAL A 431 28053 35037 21370 -3515 -3597 1560 C ATOM 2048 CG2 VAL A 431 30.698 -16.903 42.210 1.00222.32 C ANISOU 2048 CG2 VAL A 431 27991 35726 20754 -3962 -4057 1598 C ATOM 2049 N ILE A 432 27.483 -20.529 41.293 1.00208.87 N ANISOU 2049 N ILE A 432 27028 32358 19976 -1864 -3061 1635 N ATOM 2050 CA ILE A 432 27.084 -21.752 40.608 1.00206.08 C ANISOU 2050 CA ILE A 432 26684 31765 19853 -1282 -2782 1744 C ATOM 2051 C ILE A 432 26.632 -21.409 39.196 1.00202.21 C ANISOU 2051 C ILE A 432 26276 30894 19661 -1386 -2625 1625 C ATOM 2052 O ILE A 432 25.923 -20.420 38.975 1.00201.81 O ANISOU 2052 O ILE A 432 26525 30437 19716 -1767 -2640 1393 O ATOM 2053 CB ILE A 432 25.972 -22.475 41.389 1.00205.61 C ANISOU 2053 CB ILE A 432 27044 31229 19850 -944 -2629 1685 C ATOM 2054 CG1 ILE A 432 24.896 -21.481 41.832 1.00202.07 C ANISOU 2054 CG1 ILE A 432 27052 30277 19449 -1322 -2660 1403 C ATOM 2055 CG2 ILE A 432 26.554 -23.209 42.587 1.00205.70 C ANISOU 2055 CG2 ILE A 432 26915 31665 19577 -656 -2726 1882 C ATOM 2056 CD1 ILE A 432 23.563 -22.124 42.144 1.00199.34 C ANISOU 2056 CD1 ILE A 432 27125 29356 19261 -1016 -2436 1317 C ATOM 2057 N THR A 433 27.048 -22.224 38.231 1.00206.26 N ANISOU 2057 N THR A 433 26540 31537 20291 -1026 -2468 1789 N ATOM 2058 CA THR A 433 26.611 -22.026 36.860 1.00206.71 C ANISOU 2058 CA THR A 433 26682 31235 20625 -1074 -2305 1690 C ATOM 2059 C THR A 433 25.142 -22.421 36.714 1.00202.83 C ANISOU 2059 C THR A 433 26671 30021 20373 -882 -2089 1526 C ATOM 2060 O THR A 433 24.542 -23.041 37.597 1.00201.79 O ANISOU 2060 O THR A 433 26772 29696 20203 -643 -2032 1526 O ATOM 2061 CB THR A 433 27.482 -22.829 35.894 1.00205.44 C ANISOU 2061 CB THR A 433 26143 31422 20492 -717 -2186 1916 C ATOM 2062 OG1 THR A 433 27.709 -24.139 36.428 1.00215.39 O ANISOU 2062 OG1 THR A 433 27348 32842 21650 -147 -2085 2122 O ATOM 2063 CG2 THR A 433 28.819 -22.134 35.680 1.00201.22 C ANISOU 2063 CG2 THR A 433 25111 31572 19773 -1039 -2386 2041 C ATOM 2064 N LYS A 434 24.558 -22.049 35.572 1.00190.62 N ANISOU 2064 N LYS A 434 25262 28098 19066 -1001 -1970 1392 N ATOM 2065 CA LYS A 434 23.135 -22.296 35.363 1.00188.55 C ANISOU 2065 CA LYS A 434 25420 27199 19023 -885 -1785 1231 C ATOM 2066 C LYS A 434 22.831 -23.781 35.210 1.00192.02 C ANISOU 2066 C LYS A 434 25933 27485 19539 -357 -1566 1358 C ATOM 2067 O LYS A 434 21.747 -24.231 35.597 1.00192.19 O ANISOU 2067 O LYS A 434 26286 27095 19644 -226 -1443 1276 O ATOM 2068 CB LYS A 434 22.640 -21.516 34.145 1.00186.79 C ANISOU 2068 CB LYS A 434 25300 26662 19010 -1137 -1727 1074 C ATOM 2069 CG LYS A 434 22.642 -20.009 34.348 1.00189.02 C ANISOU 2069 CG LYS A 434 25671 26928 19219 -1662 -1907 911 C ATOM 2070 CD LYS A 434 22.115 -19.276 33.126 1.00185.31 C ANISOU 2070 CD LYS A 434 25337 26125 18948 -1862 -1831 770 C ATOM 2071 CE LYS A 434 22.194 -17.770 33.317 1.00177.77 C ANISOU 2071 CE LYS A 434 24520 25137 17887 -2375 -1998 620 C ATOM 2072 NZ LYS A 434 21.282 -17.298 34.396 1.00176.55 N ANISOU 2072 NZ LYS A 434 24744 24678 17658 -2463 -2033 466 N ATOM 2073 N ASP A 435 23.763 -24.556 34.652 1.00207.67 N ANISOU 2073 N ASP A 435 27634 29792 21480 -52 -1502 1562 N ATOM 2074 CA ASP A 435 23.571 -25.999 34.571 1.00206.06 C ANISOU 2074 CA ASP A 435 27556 29438 21299 467 -1288 1696 C ATOM 2075 C ASP A 435 23.829 -26.693 35.901 1.00202.18 C ANISOU 2075 C ASP A 435 27081 29150 20589 735 -1327 1837 C ATOM 2076 O ASP A 435 23.333 -27.806 36.111 1.00198.90 O ANISOU 2076 O ASP A 435 26921 28466 20187 1106 -1145 1901 O ATOM 2077 CB ASP A 435 24.474 -26.597 33.489 1.00210.08 C ANISOU 2077 CB ASP A 435 27805 30202 21815 755 -1179 1871 C ATOM 2078 CG ASP A 435 25.948 -26.373 33.764 1.00217.13 C ANISOU 2078 CG ASP A 435 28209 31816 22476 769 -1345 2074 C ATOM 2079 OD1 ASP A 435 26.275 -25.509 34.603 1.00216.29 O ANISOU 2079 OD1 ASP A 435 27955 31997 22227 423 -1577 2039 O ATOM 2080 OD2 ASP A 435 26.781 -27.064 33.141 1.00221.17 O ANISOU 2080 OD2 ASP A 435 28484 32621 22928 1125 -1242 2275 O ATOM 2081 N GLU A 436 24.592 -26.065 36.799 1.00179.37 N ANISOU 2081 N GLU A 436 23945 26725 17482 539 -1561 1890 N ATOM 2082 CA GLU A 436 24.805 -26.640 38.123 1.00174.61 C ANISOU 2082 CA GLU A 436 23365 26326 16651 771 -1619 2017 C ATOM 2083 C GLU A 436 23.557 -26.508 38.986 1.00166.29 C ANISOU 2083 C GLU A 436 22739 24800 15645 649 -1592 1839 C ATOM 2084 O GLU A 436 23.250 -27.401 39.784 1.00162.19 O ANISOU 2084 O GLU A 436 22414 24175 15035 965 -1501 1926 O ATOM 2085 CB GLU A 436 25.997 -25.967 38.802 1.00176.44 C ANISOU 2085 CB GLU A 436 23192 27233 16614 556 -1898 2123 C ATOM 2086 CG GLU A 436 27.329 -26.657 38.561 1.00179.06 C ANISOU 2086 CG GLU A 436 23081 28183 16772 925 -1904 2419 C ATOM 2087 CD GLU A 436 28.507 -25.821 39.024 1.00182.70 C ANISOU 2087 CD GLU A 436 23075 29363 16980 598 -2199 2510 C ATOM 2088 OE1 GLU A 436 28.285 -24.679 39.479 1.00182.20 O ANISOU 2088 OE1 GLU A 436 23084 29263 16881 53 -2396 2323 O ATOM 2089 OE2 GLU A 436 29.655 -26.306 38.934 1.00182.70 O ANISOU 2089 OE2 GLU A 436 22645 29975 16798 884 -2231 2773 O ATOM 2090 N ALA A 437 22.826 -25.400 38.841 1.00165.20 N ANISOU 2090 N ALA A 437 22761 24377 15631 209 -1656 1601 N ATOM 2091 CA ALA A 437 21.613 -25.206 39.627 1.00159.73 C ANISOU 2091 CA ALA A 437 22455 23261 14975 105 -1615 1436 C ATOM 2092 C ALA A 437 20.503 -26.152 39.192 1.00155.81 C ANISOU 2092 C ALA A 437 22266 22257 14679 371 -1345 1407 C ATOM 2093 O ALA A 437 19.670 -26.546 40.016 1.00153.63 O ANISOU 2093 O ALA A 437 22270 21727 14377 463 -1263 1374 O ATOM 2094 CB ALA A 437 21.146 -23.755 39.525 1.00156.58 C ANISOU 2094 CB ALA A 437 22163 22697 14634 -389 -1736 1202 C ATOM 2095 N GLU A 438 20.471 -26.527 37.911 1.00149.98 N ANISOU 2095 N GLU A 438 21486 21374 14125 475 -1204 1420 N ATOM 2096 CA GLU A 438 19.447 -27.454 37.441 1.00145.40 C ANISOU 2096 CA GLU A 438 21206 20326 13713 682 -957 1392 C ATOM 2097 C GLU A 438 19.672 -28.861 37.980 1.00151.44 C ANISOU 2097 C GLU A 438 22082 21110 14347 1129 -822 1590 C ATOM 2098 O GLU A 438 18.705 -29.588 38.231 1.00152.40 O ANISOU 2098 O GLU A 438 22532 20852 14520 1242 -652 1564 O ATOM 2099 CB GLU A 438 19.408 -27.470 35.913 1.00150.19 C ANISOU 2099 CB GLU A 438 21758 20785 14521 662 -855 1351 C ATOM 2100 CG GLU A 438 18.503 -26.410 35.308 1.00145.67 C ANISOU 2100 CG GLU A 438 21282 19928 14138 290 -877 1125 C ATOM 2101 CD GLU A 438 17.032 -26.701 35.537 1.00138.66 C ANISOU 2101 CD GLU A 438 20733 18588 13362 271 -733 1006 C ATOM 2102 OE1 GLU A 438 16.642 -27.886 35.469 1.00140.56 O ANISOU 2102 OE1 GLU A 438 21153 18628 13624 525 -554 1082 O ATOM 2103 OE2 GLU A 438 16.266 -25.746 35.784 1.00134.00 O ANISOU 2103 OE2 GLU A 438 20241 17852 12822 3 -791 843 O ATOM 2104 N LYS A 439 20.932 -29.263 38.160 1.00168.02 N ANISOU 2104 N LYS A 439 23920 23658 16261 1390 -888 1799 N ATOM 2105 CA LYS A 439 21.209 -30.568 38.753 1.00166.01 C ANISOU 2105 CA LYS A 439 23796 23439 15843 1859 -761 2006 C ATOM 2106 C LYS A 439 20.822 -30.592 40.226 1.00166.64 C ANISOU 2106 C LYS A 439 24041 23512 15763 1845 -826 2007 C ATOM 2107 O LYS A 439 20.323 -31.606 40.727 1.00170.60 O ANISOU 2107 O LYS A 439 24854 23757 16210 2116 -658 2083 O ATOM 2108 CB LYS A 439 22.685 -30.924 38.577 1.00164.30 C ANISOU 2108 CB LYS A 439 23217 23767 15443 2176 -820 2248 C ATOM 2109 N LEU A 440 21.044 -29.483 40.936 1.00148.24 N ANISOU 2109 N LEU A 440 21539 21447 13338 1519 -1063 1921 N ATOM 2110 CA LEU A 440 20.637 -29.407 42.334 1.00148.22 C ANISOU 2110 CA LEU A 440 21714 21428 13175 1480 -1129 1902 C ATOM 2111 C LEU A 440 19.130 -29.234 42.468 1.00149.71 C ANISOU 2111 C LEU A 440 22273 21078 13531 1284 -998 1702 C ATOM 2112 O LEU A 440 18.537 -29.705 43.445 1.00151.22 O ANISOU 2112 O LEU A 440 22720 21109 13626 1392 -924 1723 O ATOM 2113 CB LEU A 440 21.370 -28.260 43.030 1.00147.77 C ANISOU 2113 CB LEU A 440 21392 21819 12934 1171 -1427 1866 C ATOM 2114 CG LEU A 440 21.185 -28.128 44.543 1.00155.33 C ANISOU 2114 CG LEU A 440 22497 22858 13663 1138 -1533 1864 C ATOM 2115 CD1 LEU A 440 21.401 -29.466 45.235 1.00157.83 C ANISOU 2115 CD1 LEU A 440 22921 23238 13811 1631 -1414 2093 C ATOM 2116 CD2 LEU A 440 22.127 -27.073 45.102 1.00156.60 C ANISOU 2116 CD2 LEU A 440 22370 23526 13604 827 -1844 1853 C ATOM 2117 N PHE A 441 18.494 -28.568 41.500 1.00134.43 N ANISOU 2117 N PHE A 441 20360 18885 11832 1008 -964 1520 N ATOM 2118 CA PHE A 441 17.045 -28.404 41.547 1.00129.74 C ANISOU 2118 CA PHE A 441 20072 17833 11392 844 -833 1348 C ATOM 2119 C PHE A 441 16.336 -29.725 41.276 1.00131.52 C ANISOU 2119 C PHE A 441 20562 17710 11701 1102 -571 1421 C ATOM 2120 O PHE A 441 15.280 -30.000 41.858 1.00134.84 O ANISOU 2120 O PHE A 441 21249 17850 12133 1073 -451 1369 O ATOM 2121 CB PHE A 441 16.608 -27.338 40.542 1.00121.17 C ANISOU 2121 CB PHE A 441 18923 16603 10512 513 -870 1155 C ATOM 2122 CG PHE A 441 15.118 -27.194 40.416 1.00115.66 C ANISOU 2122 CG PHE A 441 18486 15482 9976 381 -724 999 C ATOM 2123 CD1 PHE A 441 14.333 -26.963 41.533 1.00116.45 C ANISOU 2123 CD1 PHE A 441 18786 15474 9985 320 -710 936 C ATOM 2124 CD2 PHE A 441 14.503 -27.281 39.178 1.00115.57 C ANISOU 2124 CD2 PHE A 441 18505 15216 10192 321 -601 923 C ATOM 2125 CE1 PHE A 441 12.962 -26.827 41.419 1.00111.02 C ANISOU 2125 CE1 PHE A 441 18294 14458 9431 216 -568 813 C ATOM 2126 CE2 PHE A 441 13.133 -27.146 39.057 1.00112.41 C ANISOU 2126 CE2 PHE A 441 18297 14494 9921 198 -476 796 C ATOM 2127 CZ PHE A 441 12.362 -26.919 40.179 1.00112.54 C ANISOU 2127 CZ PHE A 441 18481 14433 9846 152 -456 747 C ATOM 2128 N ASN A 442 16.903 -30.558 40.399 1.00157.33 N ANISOU 2128 N ASN A 442 23780 20991 15009 1347 -471 1544 N ATOM 2129 CA ASN A 442 16.325 -31.874 40.153 1.00159.20 C ANISOU 2129 CA ASN A 442 24327 20879 15281 1586 -220 1621 C ATOM 2130 C ASN A 442 16.477 -32.785 41.364 1.00164.67 C ANISOU 2130 C ASN A 442 25213 21607 15748 1881 -157 1789 C ATOM 2131 O ASN A 442 15.594 -33.607 41.635 1.00163.34 O ANISOU 2131 O ASN A 442 25388 21089 15585 1940 35 1801 O ATOM 2132 CB ASN A 442 16.974 -32.517 38.927 1.00162.13 C ANISOU 2132 CB ASN A 442 24639 21250 15713 1803 -124 1714 C ATOM 2133 CG ASN A 442 16.648 -31.785 37.639 1.00162.49 C ANISOU 2133 CG ASN A 442 24567 21181 15992 1525 -142 1549 C ATOM 2134 OD1 ASN A 442 15.661 -31.055 37.558 1.00157.88 O ANISOU 2134 OD1 ASN A 442 24036 20404 15548 1203 -163 1367 O ATOM 2135 ND2 ASN A 442 17.480 -31.979 36.623 1.00164.31 N ANISOU 2135 ND2 ASN A 442 24637 21545 16250 1673 -125 1623 N ATOM 2136 N GLN A 443 17.583 -32.653 42.100 1.00201.75 N ANISOU 2136 N GLN A 443 29692 26735 20227 2053 -318 1927 N ATOM 2137 CA GLN A 443 17.794 -33.482 43.281 1.00202.20 C ANISOU 2137 CA GLN A 443 29922 26862 20042 2360 -273 2102 C ATOM 2138 C GLN A 443 16.879 -33.067 44.427 1.00201.38 C ANISOU 2138 C GLN A 443 29999 26628 19890 2144 -300 1995 C ATOM 2139 O GLN A 443 16.424 -33.922 45.196 1.00203.22 O ANISOU 2139 O GLN A 443 30535 26670 20008 2325 -155 2085 O ATOM 2140 CB GLN A 443 19.261 -33.410 43.709 1.00204.76 C ANISOU 2140 CB GLN A 443 29914 27754 20131 2603 -458 2289 C ATOM 2141 CG GLN A 443 19.566 -34.055 45.052 1.00216.21 C ANISOU 2141 CG GLN A 443 31490 29366 21295 2904 -466 2470 C ATOM 2142 CD GLN A 443 19.414 -35.563 45.023 1.00220.63 C ANISOU 2142 CD GLN A 443 32420 29628 21780 3346 -193 2649 C ATOM 2143 OE1 GLN A 443 18.525 -36.122 45.664 1.00215.77 O ANISOU 2143 OE1 GLN A 443 32187 28659 21135 3359 -42 2639 O ATOM 2144 NE2 GLN A 443 20.285 -36.231 44.275 1.00220.94 N ANISOU 2144 NE2 GLN A 443 32371 29804 21772 3713 -117 2818 N ATOM 2145 N ASP A 444 16.592 -31.769 44.552 1.00169.80 N ANISOU 2145 N ASP A 444 25847 22711 15960 1769 -468 1807 N ATOM 2146 CA ASP A 444 15.731 -31.302 45.634 1.00167.18 C ANISOU 2146 CA ASP A 444 25694 22265 15563 1586 -484 1703 C ATOM 2147 C ASP A 444 14.295 -31.777 45.447 1.00163.78 C ANISOU 2147 C ASP A 444 25577 21361 15292 1504 -241 1619 C ATOM 2148 O ASP A 444 13.606 -32.085 46.426 1.00164.76 O ANISOU 2148 O ASP A 444 25936 21352 15314 1527 -150 1635 O ATOM 2149 CB ASP A 444 15.783 -29.777 45.724 1.00164.22 C ANISOU 2149 CB ASP A 444 25131 22059 15206 1221 -705 1519 C ATOM 2150 CG ASP A 444 17.116 -29.269 46.235 1.00172.17 C ANISOU 2150 CG ASP A 444 25859 23568 15989 1227 -966 1602 C ATOM 2151 OD1 ASP A 444 17.759 -29.980 47.035 1.00173.12 O ANISOU 2151 OD1 ASP A 444 25974 23921 15884 1510 -992 1788 O ATOM 2152 OD2 ASP A 444 17.521 -28.159 45.831 1.00175.93 O ANISOU 2152 OD2 ASP A 444 26126 24220 16501 938 -1146 1486 O ATOM 2153 N VAL A 445 13.826 -31.838 44.199 1.00110.01 N ANISOU 2153 N VAL A 445 18764 14318 8718 1394 -136 1534 N ATOM 2154 CA VAL A 445 12.470 -32.313 43.942 1.00103.94 C ANISOU 2154 CA VAL A 445 18255 13148 8088 1280 84 1464 C ATOM 2155 C VAL A 445 12.357 -33.798 44.266 1.00106.30 C ANISOU 2155 C VAL A 445 18865 13246 8280 1547 293 1637 C ATOM 2156 O VAL A 445 11.336 -34.258 44.793 1.00103.49 O ANISOU 2156 O VAL A 445 18768 12648 7907 1477 453 1631 O ATOM 2157 CB VAL A 445 12.066 -32.012 42.487 1.00 97.48 C ANISOU 2157 CB VAL A 445 17346 12167 7525 1090 123 1338 C ATOM 2158 CG1 VAL A 445 10.701 -32.606 42.175 1.00 86.26 C ANISOU 2158 CG1 VAL A 445 16170 10380 6224 959 343 1285 C ATOM 2159 CG2 VAL A 445 12.065 -30.512 42.238 1.00 96.01 C ANISOU 2159 CG2 VAL A 445 16919 12133 7427 824 -63 1167 C ATOM 2160 N ASP A 446 13.403 -34.571 43.963 1.00153.24 N ANISOU 2160 N ASP A 446 24802 19291 14130 1864 306 1803 N ATOM 2161 CA ASP A 446 13.398 -35.987 44.313 1.00153.50 C ANISOU 2161 CA ASP A 446 25187 19117 14018 2164 511 1984 C ATOM 2162 C ASP A 446 13.382 -36.174 45.825 1.00153.69 C ANISOU 2162 C ASP A 446 25345 19240 13809 2290 498 2084 C ATOM 2163 O ASP A 446 12.751 -37.106 46.338 1.00153.07 O ANISOU 2163 O ASP A 446 25632 18885 13644 2367 697 2164 O ATOM 2164 CB ASP A 446 14.610 -36.685 43.694 1.00161.97 C ANISOU 2164 CB ASP A 446 26216 20316 15008 2541 526 2154 C ATOM 2165 CG ASP A 446 14.467 -38.196 43.669 1.00165.44 C ANISOU 2165 CG ASP A 446 27111 20416 15334 2834 790 2314 C ATOM 2166 OD1 ASP A 446 13.389 -38.702 44.046 1.00165.77 O ANISOU 2166 OD1 ASP A 446 27495 20110 15381 2683 958 2282 O ATOM 2167 OD2 ASP A 446 15.434 -38.878 43.271 1.00166.60 O ANISOU 2167 OD2 ASP A 446 27288 20643 15370 3219 838 2478 O ATOM 2168 N ALA A 447 14.065 -35.291 46.557 1.00135.92 N ANISOU 2168 N ALA A 447 22823 17383 11439 2288 263 2079 N ATOM 2169 CA ALA A 447 14.042 -35.352 48.014 1.00135.52 C ANISOU 2169 CA ALA A 447 22890 17449 11152 2383 227 2157 C ATOM 2170 C ALA A 447 12.699 -34.919 48.588 1.00129.22 C ANISOU 2170 C ALA A 447 22255 16426 10416 2080 306 2007 C ATOM 2171 O ALA A 447 12.360 -35.320 49.706 1.00128.01 O ANISOU 2171 O ALA A 447 22326 16227 10085 2169 380 2086 O ATOM 2172 CB ALA A 447 15.165 -34.492 48.593 1.00136.84 C ANISOU 2172 CB ALA A 447 22721 18120 11153 2422 -64 2183 C ATOM 2173 N ALA A 448 11.931 -34.119 47.848 1.00129.09 N ANISOU 2173 N ALA A 448 22128 16286 10634 1749 300 1808 N ATOM 2174 CA ALA A 448 10.608 -33.688 48.283 1.00128.25 C ANISOU 2174 CA ALA A 448 22143 15997 10590 1489 394 1676 C ATOM 2175 C ALA A 448 9.518 -34.700 47.961 1.00126.79 C ANISOU 2175 C ALA A 448 22241 15439 10495 1430 672 1706 C ATOM 2176 O ALA A 448 8.552 -34.820 48.723 1.00122.88 O ANISOU 2176 O ALA A 448 21921 14824 9942 1330 800 1698 O ATOM 2177 CB ALA A 448 10.251 -32.344 47.643 1.00125.98 C ANISOU 2177 CB ALA A 448 21616 15764 10486 1191 269 1462 C ATOM 2178 N VAL A 449 9.648 -35.430 46.852 1.00118.14 N ANISOU 2178 N VAL A 449 21204 14164 9520 1473 771 1743 N ATOM 2179 CA VAL A 449 8.639 -36.426 46.511 1.00113.65 C ANISOU 2179 CA VAL A 449 20937 13234 9010 1365 1027 1769 C ATOM 2180 C VAL A 449 8.856 -37.715 47.296 1.00114.20 C ANISOU 2180 C VAL A 449 21381 13156 8854 1629 1189 1975 C ATOM 2181 O VAL A 449 7.893 -38.429 47.597 1.00109.03 O ANISOU 2181 O VAL A 449 21023 12239 8166 1501 1399 2009 O ATOM 2182 CB VAL A 449 8.619 -36.679 44.992 1.00111.71 C ANISOU 2182 CB VAL A 449 20659 12823 8964 1272 1074 1711 C ATOM 2183 CG1 VAL A 449 9.863 -37.435 44.548 1.00120.92 C ANISOU 2183 CG1 VAL A 449 21897 14004 10043 1619 1068 1856 C ATOM 2184 CG2 VAL A 449 7.357 -37.435 44.591 1.00104.39 C ANISOU 2184 CG2 VAL A 449 19998 11554 8112 1022 1305 1686 C ATOM 2185 N ARG A 450 10.103 -38.031 47.653 1.00144.46 N ANISOU 2185 N ARG A 450 25207 17169 12512 1997 1100 2125 N ATOM 2186 CA ARG A 450 10.359 -39.198 48.487 1.00142.02 C ANISOU 2186 CA ARG A 450 25267 16740 11956 2300 1248 2335 C ATOM 2187 C ARG A 450 10.119 -38.915 49.963 1.00139.00 C ANISOU 2187 C ARG A 450 24927 16500 11385 2317 1211 2373 C ATOM 2188 O ARG A 450 9.969 -39.860 50.745 1.00143.60 O ANISOU 2188 O ARG A 450 25868 16922 11771 2486 1375 2530 O ATOM 2189 CB ARG A 450 11.786 -39.709 48.269 1.00149.60 C ANISOU 2189 CB ARG A 450 26201 17866 12776 2746 1183 2509 C ATOM 2190 CG ARG A 450 12.865 -38.959 49.033 1.00153.64 C ANISOU 2190 CG ARG A 450 26376 18868 13133 2944 920 2563 C ATOM 2191 CD ARG A 450 14.173 -39.739 49.014 1.00156.11 C ANISOU 2191 CD ARG A 450 26718 19355 13243 3450 911 2796 C ATOM 2192 NE ARG A 450 15.335 -38.887 49.237 1.00160.00 N ANISOU 2192 NE ARG A 450 26754 20390 13649 3567 623 2823 N ATOM 2193 CZ ARG A 450 16.097 -38.396 48.269 1.00159.22 C ANISOU 2193 CZ ARG A 450 26306 20526 13665 3572 489 2787 C ATOM 2194 NH1 ARG A 450 15.846 -38.650 46.995 1.00156.35 N ANISOU 2194 NH1 ARG A 450 25997 19898 13509 3496 613 2718 N ATOM 2195 NH2 ARG A 450 17.137 -37.630 48.587 1.00162.84 N ANISOU 2195 NH2 ARG A 450 26352 21509 14011 3633 223 2824 N ATOM 2196 N GLY A 451 10.079 -37.641 50.359 1.00115.60 N ANISOU 2196 N GLY A 451 21645 13817 8460 2147 1009 2235 N ATOM 2197 CA GLY A 451 9.638 -37.308 51.701 1.00114.01 C ANISOU 2197 CA GLY A 451 21519 13707 8091 2109 999 2238 C ATOM 2198 C GLY A 451 8.140 -37.445 51.869 1.00109.18 C ANISOU 2198 C GLY A 451 21096 12827 7562 1817 1215 2164 C ATOM 2199 O GLY A 451 7.655 -37.687 52.978 1.00117.44 O ANISOU 2199 O GLY A 451 22344 13842 8436 1838 1315 2231 O ATOM 2200 N ILE A 452 7.387 -37.294 50.778 1.00103.16 N ANISOU 2200 N ILE A 452 20253 11895 7048 1542 1291 2036 N ATOM 2201 CA ILE A 452 5.947 -37.523 50.827 1.00 99.86 C ANISOU 2201 CA ILE A 452 19977 11263 6701 1250 1505 1989 C ATOM 2202 C ILE A 452 5.652 -39.013 50.935 1.00107.34 C ANISOU 2202 C ILE A 452 21353 11893 7540 1300 1759 2156 C ATOM 2203 O ILE A 452 4.731 -39.430 51.649 1.00107.07 O ANISOU 2203 O ILE A 452 21532 11738 7412 1165 1944 2207 O ATOM 2204 CB ILE A 452 5.269 -36.898 49.592 1.00 99.92 C ANISOU 2204 CB ILE A 452 19746 11233 6987 946 1489 1813 C ATOM 2205 CG1 ILE A 452 5.409 -35.375 49.614 1.00100.27 C ANISOU 2205 CG1 ILE A 452 19439 11551 7109 882 1269 1648 C ATOM 2206 CG2 ILE A 452 3.802 -37.295 49.518 1.00 95.91 C ANISOU 2206 CG2 ILE A 452 19361 10540 6540 638 1719 1793 C ATOM 2207 CD1 ILE A 452 5.014 -34.709 48.312 1.00 93.47 C ANISOU 2207 CD1 ILE A 452 18332 10676 6505 658 1219 1490 C ATOM 2208 N LEU A 453 6.437 -39.841 50.240 1.00111.54 N ANISOU 2208 N LEU A 453 22042 12278 8061 1499 1785 2251 N ATOM 2209 CA LEU A 453 6.189 -41.279 50.237 1.00106.03 C ANISOU 2209 CA LEU A 453 21827 11218 7243 1546 2039 2404 C ATOM 2210 C LEU A 453 6.464 -41.906 51.598 1.00115.13 C ANISOU 2210 C LEU A 453 23206 12371 8168 1804 2104 2560 C ATOM 2211 O LEU A 453 5.770 -42.851 51.992 1.00124.58 O ANISOU 2211 O LEU A 453 24688 13299 9347 1693 2313 2608 O ATOM 2212 CB LEU A 453 7.039 -41.952 49.158 1.00115.16 C ANISOU 2212 CB LEU A 453 23105 12217 8432 1752 2050 2459 C ATOM 2213 CG LEU A 453 6.778 -41.502 47.717 1.00114.18 C ANISOU 2213 CG LEU A 453 22748 12056 8580 1492 1994 2287 C ATOM 2214 CD1 LEU A 453 7.694 -42.232 46.746 1.00103.61 C ANISOU 2214 CD1 LEU A 453 21575 10561 7230 1753 2024 2361 C ATOM 2215 CD2 LEU A 453 5.318 -41.703 47.335 1.00102.68 C ANISOU 2215 CD2 LEU A 453 21400 10372 7241 1019 2163 2192 C ATOM 2216 N ARG A 454 7.461 -41.403 52.329 1.00124.14 N ANISOU 2216 N ARG A 454 24166 13827 9173 2119 1908 2614 N ATOM 2217 CA ARG A 454 7.760 -41.941 53.650 1.00116.94 C ANISOU 2217 CA ARG A 454 23383 12960 8088 2364 1934 2737 C ATOM 2218 C ARG A 454 6.824 -41.409 54.727 1.00118.69 C ANISOU 2218 C ARG A 454 23587 13264 8245 2151 1970 2687 C ATOM 2219 O ARG A 454 6.734 -42.010 55.803 1.00129.02 O ANISOU 2219 O ARG A 454 25072 14523 9426 2269 2059 2783 O ATOM 2220 CB ARG A 454 9.209 -41.632 54.037 1.00117.24 C ANISOU 2220 CB ARG A 454 23208 13351 7985 2769 1699 2824 C ATOM 2221 CG ARG A 454 9.507 -40.152 54.218 1.00119.66 C ANISOU 2221 CG ARG A 454 23159 14057 8251 2686 1433 2719 C ATOM 2222 CD ARG A 454 10.944 -39.928 54.665 1.00121.31 C ANISOU 2222 CD ARG A 454 23144 14655 8294 3043 1193 2819 C ATOM 2223 NE ARG A 454 11.885 -40.759 53.924 1.00130.92 N ANISOU 2223 NE ARG A 454 24376 15838 9528 3358 1218 2944 N ATOM 2224 CZ ARG A 454 12.571 -40.353 52.865 1.00139.57 C ANISOU 2224 CZ ARG A 454 25248 17088 10694 3408 1093 2923 C ATOM 2225 NH1 ARG A 454 12.451 -39.122 52.394 1.00138.61 N ANISOU 2225 NH1 ARG A 454 24824 17153 10689 3126 916 2751 N ATOM 2226 NH2 ARG A 454 13.399 -41.202 52.262 1.00134.22 N ANISOU 2226 NH2 ARG A 454 24606 16372 10018 3736 1150 3049 N ATOM 2227 N ASN A 455 6.128 -40.306 54.466 1.00119.91 N ANISOU 2227 N ASN A 455 23543 13544 8474 1861 1913 2543 N ATOM 2228 CA ASN A 455 5.221 -39.727 55.447 1.00119.89 C ANISOU 2228 CA ASN A 455 23511 13639 8403 1686 1960 2489 C ATOM 2229 C ASN A 455 3.889 -40.468 55.431 1.00117.81 C ANISOU 2229 C ASN A 455 23452 13099 8210 1386 2245 2504 C ATOM 2230 O ASN A 455 3.282 -40.648 54.371 1.00121.17 O ANISOU 2230 O ASN A 455 23893 13358 8788 1124 2346 2450 O ATOM 2231 CB ASN A 455 5.010 -38.241 55.162 1.00119.50 C ANISOU 2231 CB ASN A 455 23115 13836 8454 1515 1784 2299 C ATOM 2232 CG ASN A 455 4.372 -37.510 56.324 1.00124.76 C ANISOU 2232 CG ASN A 455 23756 14659 8988 1451 1793 2251 C ATOM 2233 OD1 ASN A 455 3.190 -37.691 56.613 1.00125.52 O ANISOU 2233 OD1 ASN A 455 23952 14651 9090 1247 2006 2253 O ATOM 2234 ND2 ASN A 455 5.154 -36.677 57.001 1.00129.32 N ANISOU 2234 ND2 ASN A 455 24204 15504 9429 1616 1565 2212 N ATOM 2235 N ALA A 456 3.436 -40.894 56.609 1.00109.72 N ANISOU 2235 N ALA A 456 22577 12046 7065 1403 2368 2579 N ATOM 2236 CA ALA A 456 2.191 -41.643 56.732 1.00111.22 C ANISOU 2236 CA ALA A 456 22955 12012 7291 1104 2637 2611 C ATOM 2237 C ALA A 456 0.952 -40.762 56.656 1.00109.67 C ANISOU 2237 C ALA A 456 22561 11958 7152 767 2711 2507 C ATOM 2238 O ALA A 456 -0.166 -41.290 56.682 1.00110.97 O ANISOU 2238 O ALA A 456 22814 12003 7345 469 2931 2535 O ATOM 2239 CB ALA A 456 2.181 -42.434 58.042 1.00114.60 C ANISOU 2239 CB ALA A 456 23618 12368 7555 1256 2748 2740 C ATOM 2240 N LYS A 457 1.116 -39.443 56.570 1.00108.27 N ANISOU 2240 N LYS A 457 22119 12044 6975 807 2537 2389 N ATOM 2241 CA LYS A 457 -0.002 -38.520 56.431 1.00107.20 C ANISOU 2241 CA LYS A 457 21764 12064 6904 548 2599 2277 C ATOM 2242 C LYS A 457 -0.089 -37.884 55.054 1.00107.68 C ANISOU 2242 C LYS A 457 21498 12165 7249 382 2476 2111 C ATOM 2243 O LYS A 457 -1.189 -37.558 54.605 1.00108.40 O ANISOU 2243 O LYS A 457 21400 12316 7471 107 2576 2038 O ATOM 2244 CB LYS A 457 0.091 -37.412 57.490 1.00112.23 C ANISOU 2244 CB LYS A 457 22274 12966 7403 714 2482 2211 C ATOM 2245 CG LYS A 457 -1.122 -36.494 57.567 1.00114.86 C ANISOU 2245 CG LYS A 457 22365 13470 7806 518 2569 2098 C ATOM 2246 CD LYS A 457 -2.413 -37.275 57.755 1.00115.56 C ANISOU 2246 CD LYS A 457 22559 13485 7862 258 2880 2207 C ATOM 2247 CE LYS A 457 -2.447 -37.973 59.105 1.00119.90 C ANISOU 2247 CE LYS A 457 23356 13991 8208 375 3003 2347 C ATOM 2248 NZ LYS A 457 -3.689 -38.774 59.288 1.00118.76 N ANISOU 2248 NZ LYS A 457 23267 13788 8067 82 3290 2447 N ATOM 2249 N LEU A 458 1.043 -37.712 54.371 1.00101.57 N ANISOU 2249 N LEU A 458 20644 11386 6562 551 2265 2064 N ATOM 2250 CA LEU A 458 1.067 -37.105 53.047 1.00 98.92 C ANISOU 2250 CA LEU A 458 20015 11083 6486 414 2140 1913 C ATOM 2251 C LEU A 458 0.871 -38.116 51.927 1.00 99.02 C ANISOU 2251 C LEU A 458 20157 10840 6625 236 2258 1952 C ATOM 2252 O LEU A 458 0.319 -37.767 50.878 1.00 97.36 O ANISOU 2252 O LEU A 458 19731 10640 6620 1 2246 1839 O ATOM 2253 CB LEU A 458 2.391 -36.369 52.830 1.00 97.43 C ANISOU 2253 CB LEU A 458 19660 11040 6319 655 1857 1844 C ATOM 2254 CG LEU A 458 2.656 -35.143 53.702 1.00 97.08 C ANISOU 2254 CG LEU A 458 19466 11253 6168 770 1688 1756 C ATOM 2255 CD1 LEU A 458 4.076 -34.647 53.491 1.00 96.31 C ANISOU 2255 CD1 LEU A 458 19240 11299 6056 966 1413 1722 C ATOM 2256 CD2 LEU A 458 1.648 -34.045 53.403 1.00 95.51 C ANISOU 2256 CD2 LEU A 458 19028 11159 6104 567 1701 1594 C ATOM 2257 N LYS A 459 1.314 -39.356 52.120 1.00103.85 N ANISOU 2257 N LYS A 459 21144 11213 7100 349 2373 2110 N ATOM 2258 CA LYS A 459 1.209 -40.381 51.088 1.00105.78 C ANISOU 2258 CA LYS A 459 21604 11164 7422 195 2494 2148 C ATOM 2259 C LYS A 459 -0.241 -40.774 50.801 1.00107.85 C ANISOU 2259 C LYS A 459 21908 11330 7740 -252 2707 2136 C ATOM 2260 O LYS A 459 -0.593 -40.957 49.628 1.00111.19 O ANISOU 2260 O LYS A 459 22275 11650 8322 -500 2722 2063 O ATOM 2261 CB LYS A 459 2.027 -41.617 51.474 1.00105.57 C ANISOU 2261 CB LYS A 459 22039 10884 7188 468 2590 2335 C ATOM 2262 CG LYS A 459 2.372 -42.517 50.298 1.00105.80 C ANISOU 2262 CG LYS A 459 22281 10616 7304 443 2645 2347 C ATOM 2263 CD LYS A 459 2.817 -43.896 50.759 1.00120.01 C ANISOU 2263 CD LYS A 459 24455 12133 9012 654 2769 2468 C ATOM 2264 CE LYS A 459 1.634 -44.738 51.208 1.00122.10 C ANISOU 2264 CE LYS A 459 24957 12184 9251 313 3000 2494 C ATOM 2265 NZ LYS A 459 0.728 -45.066 50.072 1.00114.04 N ANISOU 2265 NZ LYS A 459 23993 10979 8359 -144 3107 2409 N ATOM 2266 N PRO A 460 -1.110 -40.935 51.812 1.00104.46 N ANISOU 2266 N PRO A 460 21569 10951 7171 -381 2876 2213 N ATOM 2267 CA PRO A 460 -2.513 -41.261 51.495 1.00105.56 C ANISOU 2267 CA PRO A 460 21679 11072 7358 -843 3071 2210 C ATOM 2268 C PRO A 460 -3.204 -40.227 50.622 1.00103.17 C ANISOU 2268 C PRO A 460 20895 11022 7281 -1059 2970 2043 C ATOM 2269 O PRO A 460 -3.987 -40.599 49.739 1.00103.55 O ANISOU 2269 O PRO A 460 20901 11018 7426 -1428 3054 2016 O ATOM 2270 CB PRO A 460 -3.159 -41.360 52.882 1.00107.84 C ANISOU 2270 CB PRO A 460 22071 11461 7443 -857 3238 2322 C ATOM 2271 CG PRO A 460 -2.061 -41.838 53.743 1.00109.05 C ANISOU 2271 CG PRO A 460 22472 11487 7474 -456 3175 2406 C ATOM 2272 CD PRO A 460 -0.855 -41.080 53.259 1.00106.36 C ANISOU 2272 CD PRO A 460 22008 11234 7169 -137 2930 2337 C ATOM 2273 N VAL A 461 -2.944 -38.936 50.839 1.00101.66 N ANISOU 2273 N VAL A 461 20363 11104 7160 -845 2791 1934 N ATOM 2274 CA VAL A 461 -3.593 -37.915 50.022 1.00104.90 C ANISOU 2274 CA VAL A 461 20346 11744 7766 -1003 2704 1786 C ATOM 2275 C VAL A 461 -2.883 -37.708 48.691 1.00101.38 C ANISOU 2275 C VAL A 461 19791 11214 7515 -979 2524 1676 C ATOM 2276 O VAL A 461 -3.499 -37.210 47.741 1.00 99.56 O ANISOU 2276 O VAL A 461 19280 11099 7449 -1183 2486 1575 O ATOM 2277 CB VAL A 461 -3.691 -36.577 50.775 1.00 97.87 C ANISOU 2277 CB VAL A 461 19192 11147 6848 -795 2611 1709 C ATOM 2278 CG1 VAL A 461 -4.513 -36.742 52.042 1.00108.02 C ANISOU 2278 CG1 VAL A 461 20565 12541 7938 -826 2811 1816 C ATOM 2279 CG2 VAL A 461 -2.309 -36.034 51.095 1.00 96.48 C ANISOU 2279 CG2 VAL A 461 19060 10961 6636 -434 2389 1663 C ATOM 2280 N TYR A 462 -1.605 -38.079 48.593 1.00116.11 N ANISOU 2280 N TYR A 462 21861 12905 9351 -720 2417 1704 N ATOM 2281 CA TYR A 462 -0.885 -37.919 47.333 1.00111.07 C ANISOU 2281 CA TYR A 462 21124 12196 8883 -681 2262 1613 C ATOM 2282 C TYR A 462 -1.359 -38.927 46.294 1.00118.78 C ANISOU 2282 C TYR A 462 22278 12934 9920 -982 2388 1630 C ATOM 2283 O TYR A 462 -1.448 -38.604 45.103 1.00122.48 O ANISOU 2283 O TYR A 462 22557 13419 10561 -1118 2302 1522 O ATOM 2284 CB TYR A 462 0.620 -38.054 47.571 1.00108.17 C ANISOU 2284 CB TYR A 462 20897 11763 8438 -298 2127 1662 C ATOM 2285 CG TYR A 462 1.456 -37.974 46.313 1.00113.67 C ANISOU 2285 CG TYR A 462 21508 12397 9285 -226 1986 1593 C ATOM 2286 CD1 TYR A 462 1.846 -36.747 45.792 1.00113.96 C ANISOU 2286 CD1 TYR A 462 21186 12645 9469 -169 1776 1455 C ATOM 2287 CD2 TYR A 462 1.863 -39.126 45.651 1.00121.33 C ANISOU 2287 CD2 TYR A 462 22787 13081 10230 -208 2077 1669 C ATOM 2288 CE1 TYR A 462 2.612 -36.670 44.643 1.00119.45 C ANISOU 2288 CE1 TYR A 462 21796 13296 10292 -109 1659 1400 C ATOM 2289 CE2 TYR A 462 2.627 -39.058 44.502 1.00122.83 C ANISOU 2289 CE2 TYR A 462 22904 13223 10542 -120 1966 1611 C ATOM 2290 CZ TYR A 462 2.999 -37.829 44.003 1.00118.59 C ANISOU 2290 CZ TYR A 462 21971 12927 10160 -76 1755 1480 C ATOM 2291 OH TYR A 462 3.762 -37.760 42.860 1.00117.46 O ANISOU 2291 OH TYR A 462 21749 12751 10131 6 1654 1432 O ATOM 2292 N ASP A 463 -1.673 -40.151 46.723 1.00122.18 N ANISOU 2292 N ASP A 463 23102 13128 10192 -1107 2593 1764 N ATOM 2293 CA ASP A 463 -2.069 -41.192 45.783 1.00119.76 C ANISOU 2293 CA ASP A 463 23057 12546 9900 -1419 2720 1781 C ATOM 2294 C ASP A 463 -3.470 -40.979 45.226 1.00125.56 C ANISOU 2294 C ASP A 463 23539 13440 10729 -1893 2785 1714 C ATOM 2295 O ASP A 463 -3.822 -41.603 44.219 1.00134.73 O ANISOU 2295 O ASP A 463 24826 14433 11932 -2202 2835 1686 O ATOM 2296 CB ASP A 463 -1.984 -42.564 46.453 1.00115.62 C ANISOU 2296 CB ASP A 463 23092 11693 9146 -1424 2932 1951 C ATOM 2297 CG ASP A 463 -0.558 -42.977 46.754 1.00121.46 C ANISOU 2297 CG ASP A 463 24120 12253 9776 -941 2879 2038 C ATOM 2298 OD1 ASP A 463 0.367 -42.429 46.119 1.00118.21 O ANISOU 2298 OD1 ASP A 463 23512 11919 9482 -685 2692 1962 O ATOM 2299 OD2 ASP A 463 -0.362 -43.851 47.625 1.00129.11 O ANISOU 2299 OD2 ASP A 463 25464 13033 10560 -807 3015 2175 O ATOM 2300 N SER A 464 -4.274 -40.116 45.848 1.00103.25 N ANISOU 2300 N SER A 464 20363 10950 7919 -1949 2788 1693 N ATOM 2301 CA SER A 464 -5.654 -39.897 45.434 1.00102.24 C ANISOU 2301 CA SER A 464 19945 11051 7849 -2364 2862 1661 C ATOM 2302 C SER A 464 -5.875 -38.507 44.848 1.00108.80 C ANISOU 2302 C SER A 464 20264 12212 8863 -2284 2688 1520 C ATOM 2303 O SER A 464 -7.006 -38.011 44.851 1.00113.23 O ANISOU 2303 O SER A 464 20500 13079 9444 -2487 2742 1511 O ATOM 2304 CB SER A 464 -6.600 -40.129 46.612 1.00112.72 C ANISOU 2304 CB SER A 464 21293 12525 9011 -2513 3061 1780 C ATOM 2305 OG SER A 464 -6.586 -39.025 47.499 1.00116.96 O ANISOU 2305 OG SER A 464 21558 13345 9537 -2208 3001 1758 O ATOM 2306 N LEU A 465 -4.823 -37.872 44.342 1.00123.97 N ANISOU 2306 N LEU A 465 22112 14089 10902 -1985 2490 1423 N ATOM 2307 CA LEU A 465 -4.913 -36.538 43.771 1.00123.60 C ANISOU 2307 CA LEU A 465 21645 14302 11014 -1887 2323 1290 C ATOM 2308 C LEU A 465 -4.640 -36.579 42.274 1.00127.88 C ANISOU 2308 C LEU A 465 22127 14746 11716 -2006 2210 1196 C ATOM 2309 O LEU A 465 -3.998 -37.498 41.758 1.00127.22 O ANISOU 2309 O LEU A 465 22348 14368 11620 -2035 2221 1218 O ATOM 2310 CB LEU A 465 -3.929 -35.579 44.451 1.00123.34 C ANISOU 2310 CB LEU A 465 21556 14335 10972 -1470 2173 1245 C ATOM 2311 CG LEU A 465 -4.415 -34.862 45.711 1.00128.02 C ANISOU 2311 CG LEU A 465 22039 15155 11448 -1333 2228 1271 C ATOM 2312 CD1 LEU A 465 -3.372 -33.865 46.196 1.00124.13 C ANISOU 2312 CD1 LEU A 465 21513 14709 10942 -975 2045 1200 C ATOM 2313 CD2 LEU A 465 -5.744 -34.172 45.456 1.00130.38 C ANISOU 2313 CD2 LEU A 465 21991 15750 11797 -1508 2294 1235 C ATOM 2314 N ASP A 466 -5.142 -35.561 41.579 1.00131.69 N ANISOU 2314 N ASP A 466 22231 15476 12331 -2049 2110 1094 N ATOM 2315 CA ASP A 466 -4.876 -35.416 40.158 1.00125.64 C ANISOU 2315 CA ASP A 466 21370 14651 11715 -2130 1985 996 C ATOM 2316 C ASP A 466 -3.425 -35.003 39.930 1.00119.37 C ANISOU 2316 C ASP A 466 20650 13717 10989 -1790 1818 937 C ATOM 2317 O ASP A 466 -2.737 -34.528 40.837 1.00121.50 O ANISOU 2317 O ASP A 466 20944 14017 11202 -1500 1764 951 O ATOM 2318 CB ASP A 466 -5.815 -34.380 39.538 1.00131.38 C ANISOU 2318 CB ASP A 466 21671 15704 12545 -2229 1927 919 C ATOM 2319 CG ASP A 466 -7.267 -34.809 39.583 1.00144.49 C ANISOU 2319 CG ASP A 466 23190 17576 14135 -2596 2079 989 C ATOM 2320 OD1 ASP A 466 -7.530 -36.029 39.556 1.00150.84 O ANISOU 2320 OD1 ASP A 466 24249 18209 14853 -2898 2202 1062 O ATOM 2321 OD2 ASP A 466 -8.146 -33.923 39.647 1.00146.25 O ANISOU 2321 OD2 ASP A 466 23053 18145 14372 -2582 2083 979 O ATOM 2322 N ALA A 467 -2.963 -35.190 38.690 1.00109.47 N ANISOU 2322 N ALA A 467 19422 12329 9841 -1844 1735 874 N ATOM 2323 CA ALA A 467 -1.601 -34.795 38.342 1.00104.35 C ANISOU 2323 CA ALA A 467 18799 11593 9258 -1548 1581 827 C ATOM 2324 C ALA A 467 -1.370 -33.309 38.579 1.00106.03 C ANISOU 2324 C ALA A 467 18711 12040 9537 -1345 1430 744 C ATOM 2325 O ALA A 467 -0.267 -32.905 38.966 1.00100.05 O ANISOU 2325 O ALA A 467 17981 11273 8759 -1082 1321 739 O ATOM 2326 CB ALA A 467 -1.306 -35.152 36.886 1.00117.01 C ANISOU 2326 CB ALA A 467 20447 13048 10962 -1659 1532 769 C ATOM 2327 N VAL A 468 -2.394 -32.483 38.355 1.00100.46 N ANISOU 2327 N VAL A 468 17729 11554 8889 -1463 1425 684 N ATOM 2328 CA VAL A 468 -2.269 -31.055 38.625 1.00 95.95 C ANISOU 2328 CA VAL A 468 16940 11167 8348 -1267 1308 606 C ATOM 2329 C VAL A 468 -2.239 -30.799 40.126 1.00 96.27 C ANISOU 2329 C VAL A 468 17058 11278 8243 -1098 1355 656 C ATOM 2330 O VAL A 468 -1.455 -29.977 40.615 1.00 94.11 O ANISOU 2330 O VAL A 468 16785 11034 7937 -881 1237 612 O ATOM 2331 CB VAL A 468 -3.411 -30.283 37.942 1.00 99.69 C ANISOU 2331 CB VAL A 468 17124 11855 8899 -1393 1311 547 C ATOM 2332 CG1 VAL A 468 -3.151 -28.785 38.001 1.00103.52 C ANISOU 2332 CG1 VAL A 468 17458 12462 9414 -1170 1186 455 C ATOM 2333 CG2 VAL A 468 -3.583 -30.751 36.505 1.00102.93 C ANISOU 2333 CG2 VAL A 468 17486 12202 9422 -1611 1283 513 C ATOM 2334 N ARG A 469 -3.089 -31.498 40.880 1.00 96.55 N ANISOU 2334 N ARG A 469 17169 11344 8170 -1217 1529 750 N ATOM 2335 CA ARG A 469 -3.138 -31.314 42.325 1.00 94.84 C ANISOU 2335 CA ARG A 469 17042 11195 7797 -1061 1593 805 C ATOM 2336 C ARG A 469 -1.978 -32.003 43.031 1.00 93.93 C ANISOU 2336 C ARG A 469 17211 10899 7581 -900 1566 874 C ATOM 2337 O ARG A 469 -1.568 -31.561 44.111 1.00 94.55 O ANISOU 2337 O ARG A 469 17354 11033 7537 -702 1532 887 O ATOM 2338 CB ARG A 469 -4.473 -31.823 42.871 1.00 93.80 C ANISOU 2338 CB ARG A 469 16877 11188 7575 -1251 1801 896 C ATOM 2339 CG ARG A 469 -5.653 -30.947 42.487 1.00 95.78 C ANISOU 2339 CG ARG A 469 16800 11720 7873 -1320 1834 853 C ATOM 2340 CD ARG A 469 -6.965 -31.708 42.532 1.00 99.33 C ANISOU 2340 CD ARG A 469 17155 12318 8267 -1619 2027 954 C ATOM 2341 NE ARG A 469 -8.104 -30.815 42.362 1.00103.90 N ANISOU 2341 NE ARG A 469 17386 13240 8851 -1616 2072 942 N ATOM 2342 CZ ARG A 469 -9.279 -31.182 41.870 1.00109.30 C ANISOU 2342 CZ ARG A 469 17842 14152 9534 -1902 2176 1002 C ATOM 2343 NH1 ARG A 469 -9.508 -32.426 41.481 1.00113.00 N ANISOU 2343 NH1 ARG A 469 18424 14513 9998 -2267 2245 1064 N ATOM 2344 NH2 ARG A 469 -10.248 -30.277 41.761 1.00109.05 N ANISOU 2344 NH2 ARG A 469 17471 14474 9488 -1821 2213 1005 N ATOM 2345 N ARG A 470 -1.442 -33.079 42.449 1.00 83.05 N ANISOU 2345 N ARG A 470 16017 9309 6229 -966 1584 925 N ATOM 2346 CA ARG A 470 -0.264 -33.717 43.029 1.00 83.65 C ANISOU 2346 CA ARG A 470 16348 9237 6198 -753 1555 1006 C ATOM 2347 C ARG A 470 0.938 -32.785 42.985 1.00 82.03 C ANISOU 2347 C ARG A 470 16028 9118 6020 -513 1339 937 C ATOM 2348 O ARG A 470 1.723 -32.726 43.938 1.00 82.68 O ANISOU 2348 O ARG A 470 16207 9238 5968 -304 1280 988 O ATOM 2349 CB ARG A 470 0.047 -35.022 42.298 1.00 84.49 C ANISOU 2349 CB ARG A 470 16702 9085 6315 -838 1635 1073 C ATOM 2350 CG ARG A 470 -0.795 -36.204 42.738 1.00 87.00 C ANISOU 2350 CG ARG A 470 17283 9257 6517 -1044 1858 1184 C ATOM 2351 CD ARG A 470 -0.181 -37.516 42.282 1.00 88.32 C ANISOU 2351 CD ARG A 470 17822 9108 6627 -1030 1938 1266 C ATOM 2352 NE ARG A 470 -1.147 -38.607 42.317 1.00 90.76 N ANISOU 2352 NE ARG A 470 18391 9243 6850 -1348 2149 1340 N ATOM 2353 CZ ARG A 470 -0.839 -39.885 42.142 1.00 92.77 C ANISOU 2353 CZ ARG A 470 19080 9171 6996 -1375 2276 1430 C ATOM 2354 NH1 ARG A 470 0.405 -40.271 41.916 1.00 92.68 N ANISOU 2354 NH1 ARG A 470 19276 8988 6949 -1053 2226 1471 N ATOM 2355 NH2 ARG A 470 -1.805 -40.798 42.197 1.00 95.24 N ANISOU 2355 NH2 ARG A 470 19638 9332 7217 -1731 2467 1489 N ATOM 2356 N ALA A 471 1.098 -32.047 41.885 1.00 94.96 N ANISOU 2356 N ALA A 471 17460 10803 7817 -560 1216 826 N ATOM 2357 CA ALA A 471 2.215 -31.117 41.777 1.00100.53 C ANISOU 2357 CA ALA A 471 18051 11602 8544 -390 1012 760 C ATOM 2358 C ALA A 471 2.114 -30.000 42.806 1.00 96.60 C ANISOU 2358 C ALA A 471 17490 11268 7946 -303 943 707 C ATOM 2359 O ALA A 471 3.140 -29.514 43.298 1.00 95.89 O ANISOU 2359 O ALA A 471 17408 11254 7772 -158 795 699 O ATOM 2360 CB ALA A 471 2.281 -30.539 40.364 1.00 90.87 C ANISOU 2360 CB ALA A 471 16639 10383 7503 -485 917 654 C ATOM 2361 N ALA A 472 0.893 -29.584 43.148 1.00 81.59 N ANISOU 2361 N ALA A 472 15531 9439 6032 -391 1050 677 N ATOM 2362 CA ALA A 472 0.723 -28.526 44.138 1.00 80.17 C ANISOU 2362 CA ALA A 472 15344 9387 5730 -286 1012 624 C ATOM 2363 C ALA A 472 1.145 -28.994 45.525 1.00 83.69 C ANISOU 2363 C ALA A 472 15990 9838 5971 -153 1041 717 C ATOM 2364 O ALA A 472 1.686 -28.209 46.312 1.00 82.20 O ANISOU 2364 O ALA A 472 15849 9731 5653 -34 926 674 O ATOM 2365 CB ALA A 472 -0.728 -28.047 44.146 1.00 80.55 C ANISOU 2365 CB ALA A 472 15278 9534 5795 -364 1151 593 C ATOM 2366 N LEU A 473 0.907 -30.270 45.841 1.00 82.71 N ANISOU 2366 N LEU A 473 16012 9619 5796 -183 1192 845 N ATOM 2367 CA LEU A 473 1.329 -30.801 47.134 1.00 84.50 C ANISOU 2367 CA LEU A 473 16450 9841 5815 -38 1226 952 C ATOM 2368 C LEU A 473 2.848 -30.852 47.239 1.00 84.43 C ANISOU 2368 C LEU A 473 16488 9848 5744 136 1039 979 C ATOM 2369 O LEU A 473 3.410 -30.596 48.310 1.00 85.54 O ANISOU 2369 O LEU A 473 16716 10086 5700 280 960 1007 O ATOM 2370 CB LEU A 473 0.724 -32.188 47.354 1.00 86.14 C ANISOU 2370 CB LEU A 473 16842 9912 5977 -125 1444 1091 C ATOM 2371 CG LEU A 473 0.990 -32.844 48.711 1.00 88.31 C ANISOU 2371 CG LEU A 473 17368 10164 6023 23 1520 1222 C ATOM 2372 CD1 LEU A 473 0.381 -32.017 49.831 1.00 89.10 C ANISOU 2372 CD1 LEU A 473 17449 10421 5984 71 1555 1188 C ATOM 2373 CD2 LEU A 473 0.451 -34.268 48.745 1.00 90.06 C ANISOU 2373 CD2 LEU A 473 17817 10198 6204 -94 1742 1360 C ATOM 2374 N ILE A 474 3.531 -31.177 46.138 1.00 95.20 N ANISOU 2374 N ILE A 474 17783 11147 7241 128 965 977 N ATOM 2375 CA ILE A 474 4.990 -31.202 46.156 1.00 96.07 C ANISOU 2375 CA ILE A 474 17880 11335 7288 304 789 1019 C ATOM 2376 C ILE A 474 5.553 -29.788 46.171 1.00 94.83 C ANISOU 2376 C ILE A 474 17546 11359 7127 291 571 892 C ATOM 2377 O ILE A 474 6.637 -29.550 46.719 1.00 99.05 O ANISOU 2377 O ILE A 474 18067 12045 7523 411 410 924 O ATOM 2378 CB ILE A 474 5.528 -32.008 44.960 1.00 91.26 C ANISOU 2378 CB ILE A 474 17264 10606 6806 323 803 1067 C ATOM 2379 CG1 ILE A 474 4.709 -33.284 44.761 1.00 99.70 C ANISOU 2379 CG1 ILE A 474 18551 11441 7891 244 1038 1154 C ATOM 2380 CG2 ILE A 474 6.999 -32.343 45.156 1.00101.50 C ANISOU 2380 CG2 ILE A 474 18567 12011 7987 567 676 1170 C ATOM 2381 CD1 ILE A 474 5.023 -34.016 43.475 1.00100.41 C ANISOU 2381 CD1 ILE A 474 18681 11367 8103 222 1075 1172 C ATOM 2382 N ASN A 475 4.842 -28.832 45.568 1.00 90.77 N ANISOU 2382 N ASN A 475 16905 10839 6744 140 561 753 N ATOM 2383 CA ASN A 475 5.264 -27.437 45.646 1.00 87.95 C ANISOU 2383 CA ASN A 475 16457 10605 6354 107 377 626 C ATOM 2384 C ASN A 475 5.293 -26.964 47.094 1.00 93.71 C ANISOU 2384 C ASN A 475 17330 11429 6847 180 341 622 C ATOM 2385 O ASN A 475 6.173 -26.189 47.487 1.00 91.81 O ANISOU 2385 O ASN A 475 17085 11315 6484 182 149 571 O ATOM 2386 CB ASN A 475 4.331 -26.566 44.801 1.00 85.96 C ANISOU 2386 CB ASN A 475 16099 10301 6259 -27 415 495 C ATOM 2387 CG ASN A 475 4.847 -25.145 44.620 1.00 90.60 C ANISOU 2387 CG ASN A 475 16637 10958 6827 -77 231 361 C ATOM 2388 OD1 ASN A 475 5.139 -24.443 45.587 1.00 97.30 O ANISOU 2388 OD1 ASN A 475 17599 11878 7492 -48 144 320 O ATOM 2389 ND2 ASN A 475 4.957 -24.717 43.368 1.00 89.72 N ANISOU 2389 ND2 ASN A 475 16386 10813 6889 -169 173 292 N ATOM 2390 N MET A 476 4.345 -27.436 47.906 1.00 87.28 N ANISOU 2390 N MET A 476 16650 10564 5947 219 525 678 N ATOM 2391 CA MET A 476 4.316 -27.061 49.315 1.00 85.03 C ANISOU 2391 CA MET A 476 16530 10359 5419 304 513 681 C ATOM 2392 C MET A 476 5.448 -27.725 50.087 1.00 86.60 C ANISOU 2392 C MET A 476 16814 10652 5439 437 409 801 C ATOM 2393 O MET A 476 6.067 -27.097 50.955 1.00 89.84 O ANISOU 2393 O MET A 476 17293 11196 5648 474 258 770 O ATOM 2394 CB MET A 476 2.961 -27.426 49.919 1.00 85.88 C ANISOU 2394 CB MET A 476 16739 10409 5484 313 760 724 C ATOM 2395 CG MET A 476 1.795 -26.662 49.317 1.00 84.90 C ANISOU 2395 CG MET A 476 16507 10266 5487 224 862 620 C ATOM 2396 SD MET A 476 0.332 -26.655 50.368 1.00 86.68 S ANISOU 2396 SD MET A 476 16832 10533 5569 275 1118 660 S ATOM 2397 CE MET A 476 -0.224 -28.347 50.185 1.00 87.27 C ANISOU 2397 CE MET A 476 16903 10535 5721 179 1327 833 C ATOM 2398 N VAL A 477 5.733 -28.996 49.788 1.00 91.94 N ANISOU 2398 N VAL A 477 17505 11264 6163 516 489 944 N ATOM 2399 CA VAL A 477 6.833 -29.688 50.455 1.00 95.36 C ANISOU 2399 CA VAL A 477 18012 11805 6415 699 401 1084 C ATOM 2400 C VAL A 477 8.169 -29.064 50.075 1.00 98.38 C ANISOU 2400 C VAL A 477 18210 12391 6780 706 136 1050 C ATOM 2401 O VAL A 477 9.105 -29.037 50.884 1.00101.24 O ANISOU 2401 O VAL A 477 18583 12956 6928 816 -14 1118 O ATOM 2402 CB VAL A 477 6.794 -31.191 50.120 1.00 99.40 C ANISOU 2402 CB VAL A 477 18633 12160 6974 807 574 1247 C ATOM 2403 CG1 VAL A 477 7.922 -31.931 50.824 1.00101.49 C ANISOU 2403 CG1 VAL A 477 18988 12545 7028 1061 500 1416 C ATOM 2404 CG2 VAL A 477 5.448 -31.783 50.498 1.00 94.09 C ANISOU 2404 CG2 VAL A 477 18139 11306 6305 732 835 1283 C ATOM 2405 N PHE A 478 8.282 -28.546 48.849 1.00106.66 N ANISOU 2405 N PHE A 478 19075 13415 8036 575 72 952 N ATOM 2406 CA PHE A 478 9.518 -27.895 48.428 1.00109.06 C ANISOU 2406 CA PHE A 478 19184 13928 8324 538 -171 920 C ATOM 2407 C PHE A 478 9.786 -26.637 49.243 1.00111.43 C ANISOU 2407 C PHE A 478 19512 14383 8442 418 -354 805 C ATOM 2408 O PHE A 478 10.939 -26.339 49.580 1.00115.05 O ANISOU 2408 O PHE A 478 19875 15094 8743 414 -568 837 O ATOM 2409 CB PHE A 478 9.448 -27.563 46.937 1.00105.13 C ANISOU 2409 CB PHE A 478 18515 13345 8086 407 -176 833 C ATOM 2410 CG PHE A 478 10.781 -27.248 46.320 1.00109.54 C ANISOU 2410 CG PHE A 478 18853 14120 8648 392 -380 850 C ATOM 2411 CD1 PHE A 478 11.277 -25.954 46.332 1.00112.32 C ANISOU 2411 CD1 PHE A 478 19111 14621 8943 203 -584 728 C ATOM 2412 CD2 PHE A 478 11.537 -28.244 45.726 1.00112.61 C ANISOU 2412 CD2 PHE A 478 19145 14564 9078 565 -357 995 C ATOM 2413 CE1 PHE A 478 12.503 -25.661 45.765 1.00114.80 C ANISOU 2413 CE1 PHE A 478 19198 15171 9250 152 -769 756 C ATOM 2414 CE2 PHE A 478 12.763 -27.957 45.157 1.00115.67 C ANISOU 2414 CE2 PHE A 478 19294 15199 9458 566 -532 1028 C ATOM 2415 CZ PHE A 478 13.247 -26.664 45.176 1.00114.43 C ANISOU 2415 CZ PHE A 478 19003 15223 9251 342 -742 911 C ATOM 2416 N GLN A 479 8.735 -25.889 49.575 1.00103.26 N ANISOU 2416 N GLN A 479 18617 13211 7405 318 -271 676 N ATOM 2417 CA GLN A 479 8.878 -24.625 50.285 1.00 95.69 C ANISOU 2417 CA GLN A 479 17763 12332 6261 196 -420 545 C ATOM 2418 C GLN A 479 8.895 -24.798 51.798 1.00100.66 C ANISOU 2418 C GLN A 479 18595 13048 6602 300 -425 600 C ATOM 2419 O GLN A 479 9.685 -24.142 52.486 1.00109.21 O ANISOU 2419 O GLN A 479 19726 14309 7459 225 -632 560 O ATOM 2420 CB GLN A 479 7.744 -23.674 49.892 1.00 92.78 C ANISOU 2420 CB GLN A 479 17480 11771 6002 90 -313 384 C ATOM 2421 CG GLN A 479 7.923 -22.249 50.387 1.00 94.77 C ANISOU 2421 CG GLN A 479 17892 12044 6072 -48 -461 226 C ATOM 2422 CD GLN A 479 6.713 -21.379 50.106 1.00 92.59 C ANISOU 2422 CD GLN A 479 17745 11568 5866 -67 -315 93 C ATOM 2423 OE1 GLN A 479 5.735 -21.830 49.511 1.00 88.20 O ANISOU 2423 OE1 GLN A 479 17105 10903 5504 5 -117 122 O ATOM 2424 NE2 GLN A 479 6.775 -20.123 50.533 1.00 92.99 N ANISOU 2424 NE2 GLN A 479 18015 11580 5738 -163 -410 -50 N ATOM 2425 N MET A 480 8.042 -25.671 52.332 1.00113.60 N ANISOU 2425 N MET A 480 20362 14572 8229 448 -204 692 N ATOM 2426 CA MET A 480 7.864 -25.791 53.773 1.00117.15 C ANISOU 2426 CA MET A 480 21033 15073 8404 551 -171 738 C ATOM 2427 C MET A 480 8.530 -27.019 54.374 1.00118.00 C ANISOU 2427 C MET A 480 21159 15297 8380 746 -172 941 C ATOM 2428 O MET A 480 8.928 -26.981 55.543 1.00125.54 O ANISOU 2428 O MET A 480 22248 16395 9057 820 -259 985 O ATOM 2429 CB MET A 480 6.370 -25.815 54.116 1.00116.18 C ANISOU 2429 CB MET A 480 21069 14763 8312 583 96 708 C ATOM 2430 CG MET A 480 5.676 -24.476 53.932 1.00118.79 C ANISOU 2430 CG MET A 480 21461 15010 8662 470 105 520 C ATOM 2431 SD MET A 480 3.914 -24.551 54.297 1.00128.77 S ANISOU 2431 SD MET A 480 22843 16136 9948 552 437 520 S ATOM 2432 CE MET A 480 3.260 -25.016 52.696 1.00114.74 C ANISOU 2432 CE MET A 480 20800 14254 8541 468 566 534 C ATOM 2433 N GLY A 481 8.661 -28.100 53.617 1.00115.56 N ANISOU 2433 N GLY A 481 20747 14921 8238 843 -74 1067 N ATOM 2434 CA GLY A 481 9.223 -29.333 54.127 1.00117.91 C ANISOU 2434 CA GLY A 481 21112 15285 8404 1075 -36 1274 C ATOM 2435 C GLY A 481 8.154 -30.376 54.406 1.00119.55 C ANISOU 2435 C GLY A 481 21529 15253 8642 1161 261 1374 C ATOM 2436 O GLY A 481 6.952 -30.099 54.442 1.00118.80 O ANISOU 2436 O GLY A 481 21512 15001 8626 1041 430 1290 O ATOM 2437 N GLU A 482 8.622 -31.609 54.611 1.00117.73 N ANISOU 2437 N GLU A 482 21397 15008 8326 1377 332 1569 N ATOM 2438 CA GLU A 482 7.705 -32.726 54.816 1.00116.64 C ANISOU 2438 CA GLU A 482 21496 14619 8201 1432 620 1683 C ATOM 2439 C GLU A 482 6.931 -32.576 56.120 1.00116.70 C ANISOU 2439 C GLU A 482 21713 14619 8010 1431 728 1688 C ATOM 2440 O GLU A 482 5.709 -32.763 56.153 1.00116.88 O ANISOU 2440 O GLU A 482 21836 14465 8108 1311 956 1668 O ATOM 2441 CB GLU A 482 8.478 -34.046 54.796 1.00116.84 C ANISOU 2441 CB GLU A 482 21646 14612 8137 1697 671 1899 C ATOM 2442 CG GLU A 482 7.703 -35.224 55.364 1.00121.17 C ANISOU 2442 CG GLU A 482 22532 14914 8594 1772 952 2045 C ATOM 2443 CD GLU A 482 8.583 -36.430 55.635 1.00119.06 C ANISOU 2443 CD GLU A 482 22458 14630 8149 2104 988 2273 C ATOM 2444 OE1 GLU A 482 9.707 -36.484 55.094 1.00123.25 O ANISOU 2444 OE1 GLU A 482 22825 15319 8684 2277 829 2324 O ATOM 2445 OE2 GLU A 482 8.146 -37.326 56.387 1.00112.87 O ANISOU 2445 OE2 GLU A 482 21996 13682 7207 2204 1186 2414 O ATOM 2446 N THR A 483 7.625 -32.233 57.208 1.00115.47 N ANISOU 2446 N THR A 483 21613 14679 7583 1556 566 1719 N ATOM 2447 CA THR A 483 6.963 -32.132 58.504 1.00118.14 C ANISOU 2447 CA THR A 483 22177 15013 7697 1585 671 1734 C ATOM 2448 C THR A 483 6.024 -30.935 58.573 1.00109.06 C ANISOU 2448 C THR A 483 20996 13839 6603 1385 700 1535 C ATOM 2449 O THR A 483 5.004 -30.991 59.269 1.00107.76 O ANISOU 2449 O THR A 483 20998 13590 6356 1373 902 1543 O ATOM 2450 CB THR A 483 8.001 -32.047 59.624 1.00123.46 C ANISOU 2450 CB THR A 483 22924 15944 8042 1766 467 1814 C ATOM 2451 OG1 THR A 483 8.869 -30.931 59.389 1.00131.44 O ANISOU 2451 OG1 THR A 483 23720 17191 9032 1661 165 1680 O ATOM 2452 CG2 THR A 483 8.828 -33.323 59.684 1.00123.16 C ANISOU 2452 CG2 THR A 483 22953 15936 7907 2039 481 2048 C ATOM 2453 N GLY A 484 6.345 -29.851 57.865 1.00100.13 N ANISOU 2453 N GLY A 484 19669 12783 5594 1243 515 1366 N ATOM 2454 CA GLY A 484 5.510 -28.662 57.938 1.00 99.36 C ANISOU 2454 CA GLY A 484 19585 12650 5516 1101 545 1182 C ATOM 2455 C GLY A 484 4.150 -28.861 57.295 1.00 98.50 C ANISOU 2455 C GLY A 484 19434 12359 5633 1010 813 1160 C ATOM 2456 O GLY A 484 3.118 -28.518 57.877 1.00 98.58 O ANISOU 2456 O GLY A 484 19552 12338 5567 1005 982 1124 O ATOM 2457 N VAL A 485 4.129 -29.421 56.083 1.00103.18 N ANISOU 2457 N VAL A 485 19861 12854 6487 938 855 1189 N ATOM 2458 CA VAL A 485 2.864 -29.597 55.377 1.00104.33 C ANISOU 2458 CA VAL A 485 19931 12868 6841 811 1083 1167 C ATOM 2459 C VAL A 485 2.067 -30.754 55.970 1.00102.87 C ANISOU 2459 C VAL A 485 19912 12591 6584 835 1349 1327 C ATOM 2460 O VAL A 485 0.830 -30.755 55.921 1.00102.13 O ANISOU 2460 O VAL A 485 19791 12464 6549 731 1561 1321 O ATOM 2461 CB VAL A 485 3.123 -29.787 53.870 1.00 97.32 C ANISOU 2461 CB VAL A 485 18835 11906 6236 702 1027 1135 C ATOM 2462 CG1 VAL A 485 3.933 -31.044 53.627 1.00108.93 C ANISOU 2462 CG1 VAL A 485 20364 13313 7713 794 1021 1289 C ATOM 2463 CG2 VAL A 485 1.812 -29.824 53.094 1.00 95.56 C ANISOU 2463 CG2 VAL A 485 18503 11594 6213 542 1227 1097 C ATOM 2464 N ALA A 486 2.748 -31.744 56.554 1.00116.33 N ANISOU 2464 N ALA A 486 21791 14269 8140 973 1349 1483 N ATOM 2465 CA ALA A 486 2.047 -32.849 57.198 1.00111.35 C ANISOU 2465 CA ALA A 486 21376 13528 7405 987 1606 1645 C ATOM 2466 C ALA A 486 1.229 -32.389 58.398 1.00123.68 C ANISOU 2466 C ALA A 486 23056 15172 8765 1014 1734 1637 C ATOM 2467 O ALA A 486 0.311 -33.101 58.820 1.00124.36 O ANISOU 2467 O ALA A 486 23266 15187 8797 957 1989 1746 O ATOM 2468 CB ALA A 486 3.042 -33.929 57.623 1.00112.38 C ANISOU 2468 CB ALA A 486 21709 13610 7382 1184 1570 1820 C ATOM 2469 N GLY A 487 1.542 -31.221 58.957 1.00108.56 N ANISOU 2469 N GLY A 487 21126 13401 6719 1088 1570 1512 N ATOM 2470 CA GLY A 487 0.738 -30.647 60.017 1.00103.15 C ANISOU 2470 CA GLY A 487 20566 12790 5838 1132 1697 1483 C ATOM 2471 C GLY A 487 -0.545 -29.991 59.567 1.00102.35 C ANISOU 2471 C GLY A 487 20313 12703 5872 1016 1867 1389 C ATOM 2472 O GLY A 487 -1.362 -29.618 60.414 1.00103.92 O ANISOU 2472 O GLY A 487 20607 12970 5907 1075 2028 1389 O ATOM 2473 N PHE A 488 -0.750 -29.850 58.258 1.00117.80 N ANISOU 2473 N PHE A 488 22031 14618 8108 874 1843 1320 N ATOM 2474 CA PHE A 488 -2.000 -29.321 57.729 1.00117.61 C ANISOU 2474 CA PHE A 488 21825 14645 8217 777 2009 1257 C ATOM 2475 C PHE A 488 -3.075 -30.398 57.745 1.00117.49 C ANISOU 2475 C PHE A 488 21785 14617 8238 645 2298 1411 C ATOM 2476 O PHE A 488 -3.691 -30.676 56.713 1.00120.62 O ANISOU 2476 O PHE A 488 21976 15005 8849 463 2377 1414 O ATOM 2477 CB PHE A 488 -1.799 -28.796 56.309 1.00114.53 C ANISOU 2477 CB PHE A 488 21194 14227 8095 668 1867 1135 C ATOM 2478 CG PHE A 488 -1.080 -27.473 56.241 1.00112.35 C ANISOU 2478 CG PHE A 488 20927 13982 7779 748 1630 964 C ATOM 2479 CD1 PHE A 488 0.267 -27.385 56.559 1.00111.89 C ANISOU 2479 CD1 PHE A 488 20980 13917 7615 804 1385 943 C ATOM 2480 CD2 PHE A 488 -1.749 -26.322 55.852 1.00114.33 C ANISOU 2480 CD2 PHE A 488 21084 14277 8079 761 1655 835 C ATOM 2481 CE1 PHE A 488 0.931 -26.179 56.487 1.00115.02 C ANISOU 2481 CE1 PHE A 488 21400 14345 7957 813 1164 786 C ATOM 2482 CE2 PHE A 488 -1.087 -25.113 55.782 1.00113.66 C ANISOU 2482 CE2 PHE A 488 21070 14179 7937 805 1447 676 C ATOM 2483 CZ PHE A 488 0.254 -25.044 56.100 1.00113.38 C ANISOU 2483 CZ PHE A 488 21153 14130 7798 802 1199 648 C ATOM 2484 N THR A 489 -3.325 -30.985 58.921 1.00111.49 N ANISOU 2484 N THR A 489 21240 13869 7252 714 2455 1539 N ATOM 2485 CA THR A 489 -4.208 -32.144 59.003 1.00116.49 C ANISOU 2485 CA THR A 489 21901 14471 7890 549 2724 1705 C ATOM 2486 C THR A 489 -5.633 -31.810 58.580 1.00119.63 C ANISOU 2486 C THR A 489 22037 15032 8385 399 2931 1696 C ATOM 2487 O THR A 489 -6.321 -32.660 58.001 1.00124.95 O ANISOU 2487 O THR A 489 22611 15691 9173 150 3087 1789 O ATOM 2488 CB THR A 489 -4.202 -32.711 60.421 1.00120.75 C ANISOU 2488 CB THR A 489 22737 15003 8141 669 2856 1844 C ATOM 2489 OG1 THR A 489 -4.537 -31.675 61.352 1.00132.43 O ANISOU 2489 OG1 THR A 489 24253 16639 9424 847 2882 1774 O ATOM 2490 CG2 THR A 489 -2.830 -33.266 60.766 1.00118.49 C ANISOU 2490 CG2 THR A 489 22690 14580 7752 815 2669 1896 C ATOM 2491 N ASN A 490 -6.100 -30.593 58.867 1.00116.94 N ANISOU 2491 N ASN A 490 21595 14860 7977 549 2939 1592 N ATOM 2492 CA ASN A 490 -7.448 -30.212 58.457 1.00121.05 C ANISOU 2492 CA ASN A 490 21832 15592 8570 464 3136 1599 C ATOM 2493 C ASN A 490 -7.545 -30.070 56.943 1.00123.53 C ANISOU 2493 C ASN A 490 21861 15903 9173 293 3033 1521 C ATOM 2494 O ASN A 490 -8.512 -30.538 56.331 1.00129.92 O ANISOU 2494 O ASN A 490 22438 16836 10091 70 3190 1596 O ATOM 2495 CB ASN A 490 -7.864 -28.915 59.149 1.00131.92 C ANISOU 2495 CB ASN A 490 23222 17128 9773 734 3180 1512 C ATOM 2496 CG ASN A 490 -7.827 -29.022 60.662 1.00135.08 C ANISOU 2496 CG ASN A 490 23917 17542 9865 906 3291 1584 C ATOM 2497 OD1 ASN A 490 -8.273 -30.015 61.235 1.00137.84 O ANISOU 2497 OD1 ASN A 490 24334 17918 10120 801 3490 1750 O ATOM 2498 ND2 ASN A 490 -7.297 -27.995 61.316 1.00131.97 N ANISOU 2498 ND2 ASN A 490 23726 17121 9294 1154 3166 1460 N ATOM 2499 N SER A 491 -6.551 -29.431 56.320 1.00111.97 N ANISOU 2499 N SER A 491 20405 14316 7821 374 2768 1376 N ATOM 2500 CA SER A 491 -6.572 -29.273 54.870 1.00102.10 C ANISOU 2500 CA SER A 491 18905 13052 6837 226 2662 1299 C ATOM 2501 C SER A 491 -6.245 -30.578 54.154 1.00 99.73 C ANISOU 2501 C SER A 491 18620 12590 6681 -23 2650 1382 C ATOM 2502 O SER A 491 -6.786 -30.840 53.074 1.00108.02 O ANISOU 2502 O SER A 491 19453 13677 7914 -237 2683 1382 O ATOM 2503 CB SER A 491 -5.595 -28.178 54.444 1.00 96.89 C ANISOU 2503 CB SER A 491 18269 12310 6235 375 2394 1125 C ATOM 2504 OG SER A 491 -5.835 -26.975 55.153 1.00107.28 O ANISOU 2504 OG SER A 491 19662 13720 7380 605 2408 1041 O ATOM 2505 N LEU A 492 -5.367 -31.401 54.733 1.00105.23 N ANISOU 2505 N LEU A 492 19594 13108 7281 13 2607 1456 N ATOM 2506 CA LEU A 492 -5.008 -32.663 54.093 1.00103.93 C ANISOU 2506 CA LEU A 492 19521 12748 7219 -177 2615 1541 C ATOM 2507 C LEU A 492 -6.205 -33.600 54.010 1.00106.72 C ANISOU 2507 C LEU A 492 19837 13142 7570 -466 2877 1671 C ATOM 2508 O LEU A 492 -6.397 -34.286 52.999 1.00110.87 O ANISOU 2508 O LEU A 492 20307 13575 8245 -720 2898 1689 O ATOM 2509 CB LEU A 492 -3.856 -33.328 54.846 1.00 99.40 C ANISOU 2509 CB LEU A 492 19272 11999 6496 -15 2537 1617 C ATOM 2510 CG LEU A 492 -2.464 -32.737 54.608 1.00103.30 C ANISOU 2510 CG LEU A 492 19779 12447 7022 183 2247 1514 C ATOM 2511 CD1 LEU A 492 -1.434 -33.423 55.492 1.00100.70 C ANISOU 2511 CD1 LEU A 492 19741 12022 6500 370 2190 1623 C ATOM 2512 CD2 LEU A 492 -2.073 -32.835 53.140 1.00 98.07 C ANISOU 2512 CD2 LEU A 492 18960 11692 6609 64 2125 1446 C ATOM 2513 N ARG A 493 -7.026 -33.642 55.061 1.00125.82 N ANISOU 2513 N ARG A 493 22292 15708 9804 -453 3083 1765 N ATOM 2514 CA ARG A 493 -8.231 -34.462 55.011 1.00129.41 C ANISOU 2514 CA ARG A 493 22673 16258 10238 -770 3340 1897 C ATOM 2515 C ARG A 493 -9.261 -33.866 54.061 1.00131.31 C ANISOU 2515 C ARG A 493 22497 16762 10632 -937 3373 1840 C ATOM 2516 O ARG A 493 -9.983 -34.602 53.380 1.00136.41 O ANISOU 2516 O ARG A 493 23027 17449 11352 -1291 3482 1907 O ATOM 2517 CB ARG A 493 -8.821 -34.624 56.411 1.00130.70 C ANISOU 2517 CB ARG A 493 22967 16544 10149 -699 3560 2024 C ATOM 2518 CG ARG A 493 -9.852 -35.736 56.515 1.00138.53 C ANISOU 2518 CG ARG A 493 23976 17583 11076 -1066 3831 2195 C ATOM 2519 CD ARG A 493 -10.849 -35.466 57.628 1.00142.20 C ANISOU 2519 CD ARG A 493 24362 18335 11334 -1014 4071 2296 C ATOM 2520 NE ARG A 493 -11.796 -34.419 57.264 1.00152.88 N ANISOU 2520 NE ARG A 493 25281 20060 12748 -973 4112 2237 N ATOM 2521 CZ ARG A 493 -11.800 -33.199 57.785 1.00155.35 C ANISOU 2521 CZ ARG A 493 25510 20534 12981 -608 4074 2151 C ATOM 2522 NH1 ARG A 493 -10.921 -32.838 58.706 1.00151.87 N ANISOU 2522 NH1 ARG A 493 25373 19935 12396 -293 3979 2102 N ATOM 2523 NH2 ARG A 493 -12.708 -32.320 57.371 1.00154.78 N ANISOU 2523 NH2 ARG A 493 25059 20794 12955 -554 4133 2116 N ATOM 2524 N MET A 494 -9.342 -32.533 54.000 1.00124.42 N ANISOU 2524 N MET A 494 21415 16071 9788 -690 3279 1720 N ATOM 2525 CA MET A 494 -10.260 -31.891 53.065 1.00123.30 C ANISOU 2525 CA MET A 494 20878 16192 9780 -784 3298 1671 C ATOM 2526 C MET A 494 -9.883 -32.204 51.623 1.00125.79 C ANISOU 2526 C MET A 494 21098 16366 10329 -998 3137 1599 C ATOM 2527 O MET A 494 -10.759 -32.379 50.768 1.00127.37 O ANISOU 2527 O MET A 494 21020 16748 10627 -1258 3200 1625 O ATOM 2528 CB MET A 494 -10.279 -30.380 53.298 1.00124.11 C ANISOU 2528 CB MET A 494 20868 16448 9842 -425 3226 1553 C ATOM 2529 CG MET A 494 -11.103 -29.940 54.497 1.00134.22 C ANISOU 2529 CG MET A 494 22137 17972 10890 -232 3443 1630 C ATOM 2530 SD MET A 494 -10.946 -28.174 54.837 1.00138.32 S ANISOU 2530 SD MET A 494 22673 18566 11315 226 3355 1476 S ATOM 2531 CE MET A 494 -12.103 -27.983 56.190 1.00137.44 C ANISOU 2531 CE MET A 494 22546 18761 10914 410 3678 1610 C ATOM 2532 N LEU A 495 -8.582 -32.274 51.332 1.00104.21 N ANISOU 2532 N LEU A 495 18583 13339 7673 -891 2929 1515 N ATOM 2533 CA LEU A 495 -8.148 -32.674 49.997 1.00105.66 C ANISOU 2533 CA LEU A 495 18723 13364 8060 -1079 2793 1457 C ATOM 2534 C LEU A 495 -8.497 -34.131 49.722 1.00109.26 C ANISOU 2534 C LEU A 495 19317 13687 8509 -1444 2932 1578 C ATOM 2535 O LEU A 495 -8.918 -34.476 48.612 1.00111.66 O ANISOU 2535 O LEU A 495 19476 14007 8944 -1727 2923 1561 O ATOM 2536 CB LEU A 495 -6.646 -32.438 49.837 1.00102.15 C ANISOU 2536 CB LEU A 495 18472 12671 7670 -858 2557 1361 C ATOM 2537 CG LEU A 495 -6.214 -30.997 49.553 1.00 96.04 C ANISOU 2537 CG LEU A 495 17548 11980 6963 -615 2369 1207 C ATOM 2538 CD1 LEU A 495 -4.698 -30.877 49.551 1.00 91.11 C ANISOU 2538 CD1 LEU A 495 17114 11151 6353 -442 2147 1141 C ATOM 2539 CD2 LEU A 495 -6.794 -30.518 48.232 1.00 91.61 C ANISOU 2539 CD2 LEU A 495 16679 11538 6590 -749 2324 1131 C ATOM 2540 N GLN A 496 -8.332 -35.001 50.722 1.00132.46 N ANISOU 2540 N GLN A 496 22568 16482 11277 -1453 3062 1700 N ATOM 2541 CA GLN A 496 -8.729 -36.395 50.556 1.00134.01 C ANISOU 2541 CA GLN A 496 22966 16523 11428 -1819 3224 1823 C ATOM 2542 C GLN A 496 -10.244 -36.539 50.495 1.00143.69 C ANISOU 2542 C GLN A 496 23917 18061 12616 -2165 3425 1905 C ATOM 2543 O GLN A 496 -10.751 -37.502 49.910 1.00151.47 O ANISOU 2543 O GLN A 496 24961 18980 13611 -2579 3519 1968 O ATOM 2544 CB GLN A 496 -8.157 -37.247 51.689 1.00130.59 C ANISOU 2544 CB GLN A 496 22968 15852 10800 -1708 3321 1945 C ATOM 2545 CG GLN A 496 -7.819 -38.672 51.279 1.00137.10 C ANISOU 2545 CG GLN A 496 24172 16318 11600 -1945 3390 2028 C ATOM 2546 CD GLN A 496 -6.887 -39.363 52.258 1.00140.08 C ANISOU 2546 CD GLN A 496 25002 16423 11799 -1696 3422 2131 C ATOM 2547 OE1 GLN A 496 -6.777 -38.963 53.418 1.00140.07 O ANISOU 2547 OE1 GLN A 496 25037 16532 11653 -1446 3449 2172 O ATOM 2548 NE2 GLN A 496 -6.212 -40.408 51.793 1.00137.88 N ANISOU 2548 NE2 GLN A 496 25091 15787 11509 -1744 3424 2177 N ATOM 2549 N GLN A 497 -10.978 -35.597 51.087 1.00153.03 N ANISOU 2549 N GLN A 497 24810 19599 13736 -2007 3495 1910 N ATOM 2550 CA GLN A 497 -12.433 -35.577 51.004 1.00156.29 C ANISOU 2550 CA GLN A 497 24871 20407 14105 -2283 3679 1998 C ATOM 2551 C GLN A 497 -12.938 -35.021 49.679 1.00153.31 C ANISOU 2551 C GLN A 497 24091 20255 13906 -2417 3570 1911 C ATOM 2552 O GLN A 497 -14.152 -34.862 49.520 1.00154.86 O ANISOU 2552 O GLN A 497 23917 20858 14066 -2610 3697 1985 O ATOM 2553 CB GLN A 497 -13.014 -34.756 52.160 1.00155.70 C ANISOU 2553 CB GLN A 497 24647 20643 13870 -1996 3816 2049 C ATOM 2554 CG GLN A 497 -13.042 -35.481 53.498 1.00160.78 C ANISOU 2554 CG GLN A 497 25604 21195 14290 -2000 4010 2191 C ATOM 2555 CD GLN A 497 -13.947 -36.695 53.491 1.00169.48 C ANISOU 2555 CD GLN A 497 26722 22365 15306 -2508 4232 2357 C ATOM 2556 OE1 GLN A 497 -15.089 -36.629 53.035 1.00174.50 O ANISOU 2556 OE1 GLN A 497 26971 23378 15954 -2786 4337 2414 O ATOM 2557 NE2 GLN A 497 -13.443 -37.812 54.002 1.00170.13 N ANISOU 2557 NE2 GLN A 497 27263 22096 15283 -2638 4307 2444 N ATOM 2558 N LYS A 498 -12.033 -34.701 48.751 1.00140.55 N ANISOU 2558 N LYS A 498 22522 18416 12464 -2302 3340 1769 N ATOM 2559 CA LYS A 498 -12.333 -34.185 47.416 1.00142.60 C ANISOU 2559 CA LYS A 498 22453 18831 12896 -2403 3209 1675 C ATOM 2560 C LYS A 498 -13.147 -32.892 47.463 1.00143.11 C ANISOU 2560 C LYS A 498 22094 19329 12951 -2165 3229 1656 C ATOM 2561 O LYS A 498 -13.539 -32.363 46.419 1.00140.49 O ANISOU 2561 O LYS A 498 21451 19192 12737 -2212 3139 1598 O ATOM 2562 CB LYS A 498 -13.035 -35.256 46.567 1.00143.76 C ANISOU 2562 CB LYS A 498 22544 19013 13066 -2948 3278 1742 C ATOM 2563 CG LYS A 498 -14.564 -35.221 46.542 1.00150.85 C ANISOU 2563 CG LYS A 498 23016 20419 13880 -3236 3443 1855 C ATOM 2564 CD LYS A 498 -15.135 -36.593 46.224 1.00157.84 C ANISOU 2564 CD LYS A 498 24021 21257 14695 -3840 3562 1958 C ATOM 2565 CE LYS A 498 -16.637 -36.649 46.449 1.00159.30 C ANISOU 2565 CE LYS A 498 23785 21993 14749 -4153 3752 2107 C ATOM 2566 NZ LYS A 498 -17.176 -38.022 46.222 1.00148.66 N ANISOU 2566 NZ LYS A 498 22601 20582 13301 -4806 3873 2210 N ATOM 2567 N ARG A 499 -13.375 -32.355 48.661 1.00132.00 N ANISOU 2567 N ARG A 499 20698 18065 11390 -1877 3351 1705 N ATOM 2568 CA ARG A 499 -14.041 -31.064 48.827 1.00128.49 C ANISOU 2568 CA ARG A 499 19937 17983 10900 -1556 3388 1686 C ATOM 2569 C ARG A 499 -12.993 -29.977 48.620 1.00127.40 C ANISOU 2569 C ARG A 499 19938 17620 10849 -1166 3171 1512 C ATOM 2570 O ARG A 499 -12.278 -29.582 49.542 1.00123.56 O ANISOU 2570 O ARG A 499 19727 16953 10267 -877 3143 1468 O ATOM 2571 CB ARG A 499 -14.705 -30.970 50.194 1.00139.71 C ANISOU 2571 CB ARG A 499 21360 19630 12095 -1406 3624 1809 C ATOM 2572 CG ARG A 499 -15.850 -31.954 50.386 1.00140.99 C ANISOU 2572 CG ARG A 499 21331 20083 12154 -1820 3855 1995 C ATOM 2573 CD ARG A 499 -16.215 -32.130 51.852 1.00144.44 C ANISOU 2573 CD ARG A 499 21897 20622 12360 -1703 4087 2123 C ATOM 2574 NE ARG A 499 -16.506 -30.864 52.515 1.00152.42 N ANISOU 2574 NE ARG A 499 22790 21869 13255 -1212 4153 2101 N ATOM 2575 CZ ARG A 499 -15.847 -30.404 53.570 1.00151.36 C ANISOU 2575 CZ ARG A 499 22985 21530 12996 -847 4152 2051 C ATOM 2576 NH1 ARG A 499 -14.845 -31.080 54.108 1.00147.39 N ANISOU 2576 NH1 ARG A 499 22910 20620 12471 -893 4081 2030 N ATOM 2577 NH2 ARG A 499 -16.203 -29.237 54.098 1.00146.79 N ANISOU 2577 NH2 ARG A 499 22321 21164 12290 -416 4226 2027 N ATOM 2578 N TRP A 500 -12.904 -29.488 47.381 1.00131.07 N ANISOU 2578 N TRP A 500 20213 18104 11482 -1183 3013 1416 N ATOM 2579 CA TRP A 500 -11.802 -28.614 46.992 1.00121.95 C ANISOU 2579 CA TRP A 500 19214 16693 10430 -910 2789 1251 C ATOM 2580 C TRP A 500 -12.030 -27.176 47.443 1.00124.24 C ANISOU 2580 C TRP A 500 19446 17138 10622 -488 2806 1194 C ATOM 2581 O TRP A 500 -11.114 -26.533 47.967 1.00121.49 O ANISOU 2581 O TRP A 500 19374 16560 10226 -230 2699 1094 O ATOM 2582 CB TRP A 500 -11.602 -28.672 45.478 1.00114.20 C ANISOU 2582 CB TRP A 500 18084 15653 9654 -1097 2624 1175 C ATOM 2583 CG TRP A 500 -11.646 -30.060 44.925 1.00112.65 C ANISOU 2583 CG TRP A 500 17930 15347 9523 -1534 2643 1237 C ATOM 2584 CD1 TRP A 500 -12.606 -30.589 44.114 1.00114.19 C ANISOU 2584 CD1 TRP A 500 17853 15778 9756 -1885 2703 1303 C ATOM 2585 CD2 TRP A 500 -10.692 -31.104 45.153 1.00113.45 C ANISOU 2585 CD2 TRP A 500 18400 15073 9633 -1666 2607 1244 C ATOM 2586 NE1 TRP A 500 -12.306 -31.897 43.816 1.00118.42 N ANISOU 2586 NE1 TRP A 500 18608 16067 10319 -2253 2709 1336 N ATOM 2587 CE2 TRP A 500 -11.136 -32.237 44.443 1.00117.46 C ANISOU 2587 CE2 TRP A 500 18889 15560 10180 -2098 2661 1307 C ATOM 2588 CE3 TRP A 500 -9.505 -31.190 45.886 1.00111.76 C ANISOU 2588 CE3 TRP A 500 18536 14553 9376 -1453 2535 1211 C ATOM 2589 CZ2 TRP A 500 -10.435 -33.441 44.445 1.00120.02 C ANISOU 2589 CZ2 TRP A 500 19578 15527 10499 -2289 2664 1335 C ATOM 2590 CZ3 TRP A 500 -8.811 -32.385 45.887 1.00113.82 C ANISOU 2590 CZ3 TRP A 500 19102 14507 9637 -1620 2531 1254 C ATOM 2591 CH2 TRP A 500 -9.278 -33.494 45.171 1.00117.73 C ANISOU 2591 CH2 TRP A 500 19616 14947 10168 -2018 2605 1314 C ATOM 2592 N ASP A 501 -13.241 -26.652 47.237 1.00158.32 N ANISOU 2592 N ASP A 501 23419 21851 14886 -412 2939 1261 N ATOM 2593 CA ASP A 501 -13.506 -25.257 47.578 1.00158.86 C ANISOU 2593 CA ASP A 501 23469 22048 14841 30 2975 1211 C ATOM 2594 C ASP A 501 -13.373 -25.010 49.075 1.00160.81 C ANISOU 2594 C ASP A 501 23994 22237 14869 284 3100 1232 C ATOM 2595 O ASP A 501 -12.997 -23.908 49.491 1.00160.67 O ANISOU 2595 O ASP A 501 24187 22109 14753 639 3058 1132 O ATOM 2596 CB ASP A 501 -14.897 -24.850 47.090 1.00162.27 C ANISOU 2596 CB ASP A 501 23453 22969 15234 92 3121 1314 C ATOM 2597 CG ASP A 501 -15.273 -23.440 47.508 1.00165.42 C ANISOU 2597 CG ASP A 501 23869 23508 15476 604 3204 1287 C ATOM 2598 OD1 ASP A 501 -14.556 -22.492 47.121 1.00163.56 O ANISOU 2598 OD1 ASP A 501 23837 23021 15286 833 3046 1140 O ATOM 2599 OD2 ASP A 501 -16.284 -23.279 48.222 1.00167.96 O ANISOU 2599 OD2 ASP A 501 24020 24186 15611 778 3440 1417 O ATOM 2600 N GLU A 502 -13.667 -26.019 49.897 1.00147.94 N ANISOU 2600 N GLU A 502 22403 20663 13143 94 3254 1358 N ATOM 2601 CA GLU A 502 -13.521 -25.867 51.340 1.00144.94 C ANISOU 2601 CA GLU A 502 22304 20225 12542 321 3373 1384 C ATOM 2602 C GLU A 502 -12.059 -25.941 51.764 1.00135.60 C ANISOU 2602 C GLU A 502 21550 18605 11366 360 3174 1266 C ATOM 2603 O GLU A 502 -11.646 -25.245 52.699 1.00134.91 O ANISOU 2603 O GLU A 502 21738 18413 11108 647 3169 1205 O ATOM 2604 CB GLU A 502 -14.344 -26.933 52.064 1.00152.18 C ANISOU 2604 CB GLU A 502 23120 21359 13341 95 3614 1572 C ATOM 2605 CG GLU A 502 -15.848 -26.765 51.909 1.00158.50 C ANISOU 2605 CG GLU A 502 23472 22684 14067 95 3841 1715 C ATOM 2606 CD GLU A 502 -16.389 -27.432 50.658 1.00163.51 C ANISOU 2606 CD GLU A 502 23739 23508 14878 -313 3800 1771 C ATOM 2607 OE1 GLU A 502 -15.582 -27.807 49.781 1.00159.19 O ANISOU 2607 OE1 GLU A 502 23301 22659 14525 -525 3586 1670 O ATOM 2608 OE2 GLU A 502 -17.624 -27.582 50.551 1.00169.95 O ANISOU 2608 OE2 GLU A 502 24154 24796 15623 -426 3984 1920 O ATOM 2609 N ALA A 503 -11.264 -26.777 51.091 1.00108.40 N ANISOU 2609 N ALA A 503 18169 14921 8097 80 3012 1239 N ATOM 2610 CA ALA A 503 -9.840 -26.850 51.400 1.00103.67 C ANISOU 2610 CA ALA A 503 17920 13967 7504 132 2812 1144 C ATOM 2611 C ALA A 503 -9.121 -25.561 51.029 1.00102.29 C ANISOU 2611 C ALA A 503 17835 13669 7362 367 2611 972 C ATOM 2612 O ALA A 503 -8.088 -25.234 51.625 1.00 97.02 O ANISOU 2612 O ALA A 503 17460 12796 6608 491 2472 891 O ATOM 2613 CB ALA A 503 -9.204 -28.038 50.680 1.00 96.93 C ANISOU 2613 CB ALA A 503 17102 12909 6819 -181 2708 1169 C ATOM 2614 N ALA A 504 -9.646 -24.819 50.051 1.00118.93 N ANISOU 2614 N ALA A 504 19703 15907 9578 416 2591 920 N ATOM 2615 CA ALA A 504 -9.036 -23.548 49.678 1.00113.73 C ANISOU 2615 CA ALA A 504 19163 15116 8932 629 2422 763 C ATOM 2616 C ALA A 504 -9.215 -22.508 50.776 1.00105.55 C ANISOU 2616 C ALA A 504 18360 14102 7642 965 2509 720 C ATOM 2617 O ALA A 504 -8.289 -21.744 51.073 1.00102.58 O ANISOU 2617 O ALA A 504 18280 13507 7187 1087 2351 591 O ATOM 2618 CB ALA A 504 -9.628 -23.049 48.360 1.00108.60 C ANISOU 2618 CB ALA A 504 18216 14607 8441 617 2399 736 C ATOM 2619 N VAL A 505 -10.399 -22.464 51.392 1.00 98.36 N ANISOU 2619 N VAL A 505 17329 13462 6581 1109 2764 831 N ATOM 2620 CA VAL A 505 -10.642 -21.505 52.465 1.00100.48 C ANISOU 2620 CA VAL A 505 17848 13749 6579 1460 2880 798 C ATOM 2621 C VAL A 505 -9.820 -21.862 53.697 1.00100.83 C ANISOU 2621 C VAL A 505 18251 13602 6458 1451 2835 782 C ATOM 2622 O VAL A 505 -9.335 -20.978 54.413 1.00101.48 O ANISOU 2622 O VAL A 505 18680 13533 6344 1666 2781 675 O ATOM 2623 CB VAL A 505 -12.146 -21.434 52.786 1.00103.56 C ANISOU 2623 CB VAL A 505 17978 14528 6842 1635 3185 945 C ATOM 2624 CG1 VAL A 505 -12.441 -20.246 53.690 1.00105.86 C ANISOU 2624 CG1 VAL A 505 18547 14828 6848 2070 3315 897 C ATOM 2625 CG2 VAL A 505 -12.958 -21.349 51.504 1.00103.35 C ANISOU 2625 CG2 VAL A 505 17523 14756 6991 1577 3212 994 C ATOM 2626 N ASN A 506 -9.649 -23.158 53.965 1.00105.47 N ANISOU 2626 N ASN A 506 18788 14186 7100 1199 2857 890 N ATOM 2627 CA ASN A 506 -8.850 -23.574 55.112 1.00104.63 C ANISOU 2627 CA ASN A 506 19010 13916 6828 1202 2809 895 C ATOM 2628 C ASN A 506 -7.371 -23.270 54.909 1.00102.28 C ANISOU 2628 C ASN A 506 18945 13340 6577 1156 2502 753 C ATOM 2629 O ASN A 506 -6.664 -22.971 55.877 1.00104.55 O ANISOU 2629 O ASN A 506 19550 13511 6662 1261 2419 699 O ATOM 2630 CB ASN A 506 -9.053 -25.064 55.384 1.00109.25 C ANISOU 2630 CB ASN A 506 19509 14551 7451 957 2923 1061 C ATOM 2631 CG ASN A 506 -8.529 -25.485 56.743 1.00113.35 C ANISOU 2631 CG ASN A 506 20354 14970 7743 1024 2945 1107 C ATOM 2632 OD1 ASN A 506 -7.326 -25.673 56.927 1.00110.58 O ANISOU 2632 OD1 ASN A 506 20222 14409 7383 991 2735 1050 O ATOM 2633 ND2 ASN A 506 -9.432 -25.633 57.706 1.00121.76 N ANISOU 2633 ND2 ASN A 506 21440 16216 8609 1127 3203 1220 N ATOM 2634 N LEU A 507 -6.887 -23.340 53.668 1.00 99.02 N ANISOU 2634 N LEU A 507 18369 12842 6412 991 2329 696 N ATOM 2635 CA LEU A 507 -5.487 -23.044 53.392 1.00 94.64 C ANISOU 2635 CA LEU A 507 17982 12072 5904 933 2043 576 C ATOM 2636 C LEU A 507 -5.206 -21.550 53.319 1.00 94.62 C ANISOU 2636 C LEU A 507 18158 11986 5807 1098 1931 411 C ATOM 2637 O LEU A 507 -4.055 -21.140 53.505 1.00 94.03 O ANISOU 2637 O LEU A 507 18299 11760 5667 1062 1709 309 O ATOM 2638 CB LEU A 507 -5.052 -23.716 52.089 1.00 92.24 C ANISOU 2638 CB LEU A 507 17452 11708 5886 701 1917 585 C ATOM 2639 CG LEU A 507 -4.707 -25.204 52.190 1.00 92.08 C ANISOU 2639 CG LEU A 507 17414 11643 5928 521 1934 714 C ATOM 2640 CD1 LEU A 507 -4.985 -25.922 50.876 1.00 91.05 C ANISOU 2640 CD1 LEU A 507 17025 11515 6055 304 1943 755 C ATOM 2641 CD2 LEU A 507 -3.258 -25.390 52.611 1.00 91.50 C ANISOU 2641 CD2 LEU A 507 17555 11424 5785 529 1718 684 C ATOM 2642 N ALA A 508 -6.223 -20.731 53.059 1.00 95.58 N ANISOU 2642 N ALA A 508 18206 12210 5899 1275 2082 390 N ATOM 2643 CA ALA A 508 -6.067 -19.284 52.995 1.00 96.03 C ANISOU 2643 CA ALA A 508 18499 12152 5836 1459 2014 240 C ATOM 2644 C ALA A 508 -6.021 -18.629 54.371 1.00 98.54 C ANISOU 2644 C ALA A 508 19215 12409 5815 1667 2075 189 C ATOM 2645 O ALA A 508 -6.010 -17.397 54.454 1.00 99.58 O ANISOU 2645 O ALA A 508 19621 12423 5791 1843 2059 66 O ATOM 2646 CB ALA A 508 -7.198 -18.669 52.167 1.00 96.45 C ANISOU 2646 CB ALA A 508 18337 12345 5965 1622 2168 255 C ATOM 2647 N LYS A 509 -5.995 -19.420 55.444 1.00 99.73 N ANISOU 2647 N LYS A 509 19441 12620 5831 1653 2151 281 N ATOM 2648 CA LYS A 509 -5.957 -18.895 56.803 1.00102.28 C ANISOU 2648 CA LYS A 509 20153 12895 5814 1843 2213 240 C ATOM 2649 C LYS A 509 -4.721 -19.349 57.569 1.00102.14 C ANISOU 2649 C LYS A 509 20356 12769 5684 1687 2002 216 C ATOM 2650 O LYS A 509 -4.678 -19.205 58.796 1.00104.36 O ANISOU 2650 O LYS A 509 20935 13040 5676 1806 2055 212 O ATOM 2651 CB LYS A 509 -7.220 -19.307 57.566 1.00104.66 C ANISOU 2651 CB LYS A 509 20366 13416 5984 2033 2542 388 C ATOM 2652 CG LYS A 509 -8.520 -18.961 56.858 1.00105.31 C ANISOU 2652 CG LYS A 509 20158 13699 6156 2200 2766 449 C ATOM 2653 CD LYS A 509 -9.726 -19.376 57.687 1.00108.10 C ANISOU 2653 CD LYS A 509 20400 14321 6351 2374 3094 612 C ATOM 2654 CE LYS A 509 -9.857 -20.891 57.755 1.00110.82 C ANISOU 2654 CE LYS A 509 20472 14799 6835 2095 3151 778 C ATOM 2655 NZ LYS A 509 -11.258 -21.318 58.029 1.00110.02 N ANISOU 2655 NZ LYS A 509 20087 15040 6677 2180 3479 959 N ATOM 2656 N SER A 510 -3.716 -19.886 56.884 1.00 99.85 N ANISOU 2656 N SER A 510 19924 12419 5594 1443 1768 209 N ATOM 2657 CA SER A 510 -2.535 -20.420 57.540 1.00 99.91 C ANISOU 2657 CA SER A 510 20074 12387 5500 1317 1567 220 C ATOM 2658 C SER A 510 -1.422 -19.376 57.583 1.00100.04 C ANISOU 2658 C SER A 510 20355 12273 5383 1238 1290 47 C ATOM 2659 O SER A 510 -1.545 -18.269 57.053 1.00 99.95 O ANISOU 2659 O SER A 510 20446 12159 5371 1266 1258 -84 O ATOM 2660 CB SER A 510 -2.062 -21.688 56.829 1.00 97.85 C ANISOU 2660 CB SER A 510 19515 12162 5501 1128 1492 336 C ATOM 2661 OG SER A 510 -1.541 -21.388 55.546 1.00 95.56 O ANISOU 2661 OG SER A 510 19050 11809 5448 989 1321 259 O ATOM 2662 N ARG A 511 -0.314 -19.736 58.237 1.00102.22 N ANISOU 2662 N ARG A 511 20752 12566 5522 1130 1087 56 N ATOM 2663 CA ARG A 511 0.854 -18.863 58.253 1.00102.59 C ANISOU 2663 CA ARG A 511 20962 12541 5477 975 789 -90 C ATOM 2664 C ARG A 511 1.536 -18.822 56.893 1.00102.24 C ANISOU 2664 C ARG A 511 20693 12476 5676 785 610 -125 C ATOM 2665 O ARG A 511 2.090 -17.786 56.507 1.00105.59 O ANISOU 2665 O ARG A 511 21258 12808 6055 661 439 -270 O ATOM 2666 CB ARG A 511 1.842 -19.326 59.325 1.00104.18 C ANISOU 2666 CB ARG A 511 21229 12836 5518 905 609 -45 C ATOM 2667 CG ARG A 511 3.058 -18.429 59.480 1.00105.23 C ANISOU 2667 CG ARG A 511 21478 12952 5552 700 294 -184 C ATOM 2668 CD ARG A 511 3.834 -18.754 60.744 1.00107.59 C ANISOU 2668 CD ARG A 511 21859 13381 5638 669 149 -142 C ATOM 2669 NE ARG A 511 5.132 -18.092 60.770 1.00108.63 N ANISOU 2669 NE ARG A 511 22022 13576 5676 418 -178 -242 N ATOM 2670 CZ ARG A 511 5.325 -16.838 61.157 1.00112.94 C ANISOU 2670 CZ ARG A 511 22802 14010 6101 298 -277 -409 C ATOM 2671 NH1 ARG A 511 4.323 -16.080 61.570 1.00114.42 N ANISOU 2671 NH1 ARG A 511 23237 13999 6239 450 -77 -495 N ATOM 2672 NH2 ARG A 511 6.555 -16.333 61.130 1.00117.92 N ANISOU 2672 NH2 ARG A 511 23422 14736 6646 19 -579 -481 N ATOM 2673 N TRP A 512 1.503 -19.934 56.155 1.00 96.43 N ANISOU 2673 N TRP A 512 19607 11812 5219 745 651 6 N ATOM 2674 CA TRP A 512 2.133 -19.975 54.841 1.00 94.11 C ANISOU 2674 CA TRP A 512 19061 11505 5193 581 497 -16 C ATOM 2675 C TRP A 512 1.454 -19.026 53.863 1.00 93.10 C ANISOU 2675 C TRP A 512 18904 11265 5203 592 567 -124 C ATOM 2676 O TRP A 512 2.116 -18.465 52.982 1.00 91.96 O ANISOU 2676 O TRP A 512 18707 11068 5166 444 394 -210 O ATOM 2677 CB TRP A 512 2.115 -21.409 54.307 1.00 95.94 C ANISOU 2677 CB TRP A 512 18987 11805 5659 565 566 148 C ATOM 2678 CG TRP A 512 2.308 -21.528 52.828 1.00 90.12 C ANISOU 2678 CG TRP A 512 17978 11037 5227 448 507 137 C ATOM 2679 CD1 TRP A 512 3.413 -21.169 52.113 1.00 92.90 C ANISOU 2679 CD1 TRP A 512 18248 11395 5653 301 270 76 C ATOM 2680 CD2 TRP A 512 1.371 -22.055 51.882 1.00 88.59 C ANISOU 2680 CD2 TRP A 512 17555 10819 5286 453 687 193 C ATOM 2681 NE1 TRP A 512 3.220 -21.435 50.778 1.00 90.98 N ANISOU 2681 NE1 TRP A 512 17757 11113 5698 239 301 88 N ATOM 2682 CE2 TRP A 512 1.974 -21.980 50.611 1.00 88.67 C ANISOU 2682 CE2 TRP A 512 17376 10798 5515 323 547 155 C ATOM 2683 CE3 TRP A 512 0.079 -22.580 51.987 1.00 88.94 C ANISOU 2683 CE3 TRP A 512 17525 10889 5378 533 949 277 C ATOM 2684 CZ2 TRP A 512 1.329 -22.411 49.454 1.00 87.26 C ANISOU 2684 CZ2 TRP A 512 16966 10596 5594 279 654 188 C ATOM 2685 CZ3 TRP A 512 -0.558 -23.007 50.838 1.00 87.41 C ANISOU 2685 CZ3 TRP A 512 17079 10696 5438 461 1046 313 C ATOM 2686 CH2 TRP A 512 0.067 -22.920 49.588 1.00 85.57 C ANISOU 2686 CH2 TRP A 512 16687 10412 5413 339 895 264 C ATOM 2687 N TYR A 513 0.142 -18.824 54.004 1.00 98.44 N ANISOU 2687 N TYR A 513 19611 11927 5864 778 824 -110 N ATOM 2688 CA TYR A 513 -0.554 -17.897 53.119 1.00 98.05 C ANISOU 2688 CA TYR A 513 19543 11796 5915 845 903 -195 C ATOM 2689 C TYR A 513 -0.207 -16.449 53.438 1.00104.53 C ANISOU 2689 C TYR A 513 20760 12459 6498 862 802 -367 C ATOM 2690 O TYR A 513 -0.154 -15.614 52.529 1.00107.32 O ANISOU 2690 O TYR A 513 21140 12700 6937 822 744 -461 O ATOM 2691 CB TYR A 513 -2.067 -18.116 53.206 1.00100.71 C ANISOU 2691 CB TYR A 513 19762 12226 6277 1062 1213 -107 C ATOM 2692 CG TYR A 513 -2.868 -17.326 52.191 1.00 98.80 C ANISOU 2692 CG TYR A 513 19424 11961 6156 1167 1309 -156 C ATOM 2693 CD1 TYR A 513 -3.267 -16.020 52.450 1.00101.70 C ANISOU 2693 CD1 TYR A 513 20105 12219 6317 1369 1377 -264 C ATOM 2694 CD2 TYR A 513 -3.225 -17.887 50.973 1.00 99.00 C ANISOU 2694 CD2 TYR A 513 19072 12066 6478 1079 1335 -89 C ATOM 2695 CE1 TYR A 513 -3.997 -15.297 51.526 1.00 99.91 C ANISOU 2695 CE1 TYR A 513 19802 11978 6180 1510 1471 -291 C ATOM 2696 CE2 TYR A 513 -3.955 -17.171 50.041 1.00108.21 C ANISOU 2696 CE2 TYR A 513 20136 13239 7738 1190 1413 -122 C ATOM 2697 CZ TYR A 513 -4.338 -15.877 50.324 1.00105.12 C ANISOU 2697 CZ TYR A 513 20045 12753 7141 1420 1483 -216 C ATOM 2698 OH TYR A 513 -5.065 -15.162 49.399 1.00107.71 O ANISOU 2698 OH TYR A 513 20285 13096 7543 1574 1568 -233 O ATOM 2699 N ASN A 514 0.029 -16.127 54.710 1.00110.22 N ANISOU 2699 N ASN A 514 21826 13151 6902 911 782 -410 N ATOM 2700 CA ASN A 514 0.352 -14.754 55.077 1.00112.11 C ANISOU 2700 CA ASN A 514 22434 13207 6955 891 683 -575 C ATOM 2701 C ASN A 514 1.833 -14.438 54.920 1.00112.66 C ANISOU 2701 C ASN A 514 22543 13242 7019 563 351 -660 C ATOM 2702 O ASN A 514 2.185 -13.267 54.741 1.00117.95 O ANISOU 2702 O ASN A 514 23419 13738 7657 455 244 -793 O ATOM 2703 CB ASN A 514 -0.091 -14.476 56.515 1.00121.85 C ANISOU 2703 CB ASN A 514 23897 14417 7982 1064 799 -580 C ATOM 2704 CG ASN A 514 -1.596 -14.357 56.645 1.00118.64 C ANISOU 2704 CG ASN A 514 23489 14033 7555 1407 1133 -521 C ATOM 2705 OD1 ASN A 514 -2.268 -15.287 57.090 1.00119.99 O ANISOU 2705 OD1 ASN A 514 23507 14375 7710 1537 1320 -385 O ATOM 2706 ND2 ASN A 514 -2.135 -13.206 56.256 1.00114.88 N ANISOU 2706 ND2 ASN A 514 23180 13398 7070 1558 1218 -610 N ATOM 2707 N GLN A 515 2.705 -15.447 54.980 1.00120.99 N ANISOU 2707 N GLN A 515 23407 14471 8093 407 195 -571 N ATOM 2708 CA GLN A 515 4.128 -15.206 54.770 1.00123.79 C ANISOU 2708 CA GLN A 515 23729 14872 8433 101 -119 -626 C ATOM 2709 C GLN A 515 4.439 -14.969 53.296 1.00125.07 C ANISOU 2709 C GLN A 515 23730 14990 8800 -46 -204 -661 C ATOM 2710 O GLN A 515 5.260 -14.107 52.962 1.00127.03 O ANISOU 2710 O GLN A 515 24063 15175 9028 -284 -401 -767 O ATOM 2711 CB GLN A 515 4.945 -16.382 55.308 1.00123.77 C ANISOU 2711 CB GLN A 515 23555 15104 8369 40 -246 -493 C ATOM 2712 CG GLN A 515 5.042 -16.432 56.826 1.00122.80 C ANISOU 2712 CG GLN A 515 23597 15040 8021 101 -255 -480 C ATOM 2713 CD GLN A 515 5.832 -15.274 57.403 1.00129.36 C ANISOU 2713 CD GLN A 515 24642 15820 8688 -115 -467 -625 C ATOM 2714 OE1 GLN A 515 5.284 -14.422 58.103 1.00134.81 O ANISOU 2714 OE1 GLN A 515 25620 16343 9260 -36 -371 -721 O ATOM 2715 NE2 GLN A 515 7.128 -15.239 57.114 1.00132.14 N ANISOU 2715 NE2 GLN A 515 24859 16327 9020 -394 -751 -632 N ATOM 2716 N THR A 516 3.795 -15.721 52.405 1.00100.13 N ANISOU 2716 N THR A 516 20221 11867 5955 72 -53 -559 N ATOM 2717 CA THR A 516 3.963 -15.560 50.960 1.00102.45 C ANISOU 2717 CA THR A 516 20281 12120 6526 -37 -105 -577 C ATOM 2718 C THR A 516 2.589 -15.601 50.311 1.00101.07 C ANISOU 2718 C THR A 516 19989 11880 6533 185 154 -546 C ATOM 2719 O THR A 516 2.132 -16.652 49.844 1.00 96.37 O ANISOU 2719 O THR A 516 19066 11388 6163 247 265 -424 O ATOM 2720 CB THR A 516 4.878 -16.643 50.382 1.00107.99 C ANISOU 2720 CB THR A 516 20602 12996 7433 -173 -244 -463 C ATOM 2721 OG1 THR A 516 4.492 -17.923 50.896 1.00110.94 O ANISOU 2721 OG1 THR A 516 20815 13484 7853 -22 -112 -314 O ATOM 2722 CG2 THR A 516 6.329 -16.371 50.751 1.00109.86 C ANISOU 2722 CG2 THR A 516 20899 13347 7497 -417 -531 -497 C ATOM 2723 N PRO A 517 1.892 -14.461 50.264 1.00 98.62 N ANISOU 2723 N PRO A 517 19956 11407 6108 311 259 -651 N ATOM 2724 CA PRO A 517 0.522 -14.473 49.722 1.00 94.21 C ANISOU 2724 CA PRO A 517 19260 10851 5686 560 512 -601 C ATOM 2725 C PRO A 517 0.456 -14.790 48.240 1.00 97.87 C ANISOU 2725 C PRO A 517 19366 11347 6475 483 492 -562 C ATOM 2726 O PRO A 517 -0.439 -15.530 47.812 1.00 95.11 O ANISOU 2726 O PRO A 517 18717 11118 6302 593 656 -456 O ATOM 2727 CB PRO A 517 0.015 -13.054 50.024 1.00 96.04 C ANISOU 2727 CB PRO A 517 19932 10887 5673 731 600 -726 C ATOM 2728 CG PRO A 517 0.919 -12.541 51.107 1.00 98.20 C ANISOU 2728 CG PRO A 517 20610 11065 5637 588 440 -827 C ATOM 2729 CD PRO A 517 2.254 -13.147 50.818 1.00 98.64 C ANISOU 2729 CD PRO A 517 20443 11226 5811 256 171 -807 C ATOM 2730 N ASN A 518 1.376 -14.248 47.439 1.00 97.96 N ANISOU 2730 N ASN A 518 19403 11264 6554 275 296 -643 N ATOM 2731 CA ASN A 518 1.304 -14.448 45.995 1.00 96.09 C ANISOU 2731 CA ASN A 518 18863 11042 6605 214 282 -615 C ATOM 2732 C ASN A 518 1.582 -15.898 45.620 1.00 92.88 C ANISOU 2732 C ASN A 518 18063 10802 6427 118 258 -488 C ATOM 2733 O ASN A 518 0.877 -16.473 44.782 1.00 90.37 O ANISOU 2733 O ASN A 518 17470 10547 6320 170 369 -417 O ATOM 2734 CB ASN A 518 2.280 -13.508 45.289 1.00 98.25 C ANISOU 2734 CB ASN A 518 19283 11176 6871 1 84 -726 C ATOM 2735 CG ASN A 518 1.924 -12.048 45.486 1.00 99.41 C ANISOU 2735 CG ASN A 518 19876 11101 6793 99 132 -853 C ATOM 2736 OD1 ASN A 518 0.823 -11.614 45.145 1.00 98.72 O ANISOU 2736 OD1 ASN A 518 19832 10958 6718 356 318 -849 O ATOM 2737 ND2 ASN A 518 2.855 -11.281 46.040 1.00 95.52 N ANISOU 2737 ND2 ASN A 518 19733 10488 6072 -102 -35 -962 N ATOM 2738 N ARG A 519 2.602 -16.506 46.229 1.00 92.93 N ANISOU 2738 N ARG A 519 18056 10884 6371 -17 115 -453 N ATOM 2739 CA ARG A 519 2.893 -17.909 45.952 1.00 89.29 C ANISOU 2739 CA ARG A 519 17289 10550 6087 -64 112 -323 C ATOM 2740 C ARG A 519 1.769 -18.814 46.441 1.00 92.93 C ANISOU 2740 C ARG A 519 17662 11078 6568 94 339 -215 C ATOM 2741 O ARG A 519 1.441 -19.812 45.790 1.00 93.96 O ANISOU 2741 O ARG A 519 17547 11260 6895 73 418 -122 O ATOM 2742 CB ARG A 519 4.221 -18.307 46.598 1.00 89.95 C ANISOU 2742 CB ARG A 519 17396 10727 6054 -188 -81 -291 C ATOM 2743 CG ARG A 519 4.585 -19.773 46.418 1.00 89.00 C ANISOU 2743 CG ARG A 519 17025 10719 6072 -182 -69 -144 C ATOM 2744 CD ARG A 519 6.057 -20.020 46.704 1.00 94.73 C ANISOU 2744 CD ARG A 519 17711 11578 6705 -289 -288 -107 C ATOM 2745 NE ARG A 519 6.409 -21.428 46.564 1.00 95.93 N ANISOU 2745 NE ARG A 519 17672 11818 6958 -222 -255 46 N ATOM 2746 CZ ARG A 519 7.649 -21.895 46.579 1.00 99.14 C ANISOU 2746 CZ ARG A 519 17965 12378 7325 -255 -414 123 C ATOM 2747 NH1 ARG A 519 8.689 -21.091 46.726 1.00101.36 N ANISOU 2747 NH1 ARG A 519 18259 12781 7473 -399 -634 65 N ATOM 2748 NH2 ARG A 519 7.852 -23.203 46.446 1.00 99.28 N ANISOU 2748 NH2 ARG A 519 17864 12438 7419 -140 -344 269 N ATOM 2749 N ALA A 520 1.159 -18.475 47.580 1.00 92.96 N ANISOU 2749 N ALA A 520 17883 11082 6356 238 452 -226 N ATOM 2750 CA ALA A 520 0.130 -19.337 48.151 1.00 88.49 C ANISOU 2750 CA ALA A 520 17233 10608 5781 366 674 -112 C ATOM 2751 C ALA A 520 -1.169 -19.281 47.358 1.00 90.09 C ANISOU 2751 C ALA A 520 17245 10857 6129 453 863 -84 C ATOM 2752 O ALA A 520 -1.885 -20.285 47.279 1.00 90.67 O ANISOU 2752 O ALA A 520 17116 11035 6299 445 1011 32 O ATOM 2753 CB ALA A 520 -0.125 -18.959 49.608 1.00 95.57 C ANISOU 2753 CB ALA A 520 18419 11509 6384 506 748 -127 C ATOM 2754 N LYS A 521 -1.496 -18.126 46.772 1.00 99.18 N ANISOU 2754 N LYS A 521 18463 11943 7278 529 861 -180 N ATOM 2755 CA LYS A 521 -2.735 -18.019 46.007 1.00 99.53 C ANISOU 2755 CA LYS A 521 18299 12079 7437 640 1030 -141 C ATOM 2756 C LYS A 521 -2.687 -18.889 44.756 1.00104.66 C ANISOU 2756 C LYS A 521 18621 12782 8364 462 989 -83 C ATOM 2757 O LYS A 521 -3.699 -19.488 44.371 1.00104.90 O ANISOU 2757 O LYS A 521 18406 12960 8491 469 1140 7 O ATOM 2758 CB LYS A 521 -3.005 -16.561 45.637 1.00104.85 C ANISOU 2758 CB LYS A 521 19160 12653 8025 797 1032 -250 C ATOM 2759 CG LYS A 521 -4.246 -16.364 44.777 1.00115.34 C ANISOU 2759 CG LYS A 521 20253 14116 9454 948 1192 -198 C ATOM 2760 CD LYS A 521 -4.374 -14.929 44.292 1.00124.22 C ANISOU 2760 CD LYS A 521 21598 15107 10494 1122 1181 -299 C ATOM 2761 CE LYS A 521 -5.478 -14.796 43.255 1.00128.78 C ANISOU 2761 CE LYS A 521 21889 15851 11189 1266 1304 -233 C ATOM 2762 NZ LYS A 521 -6.813 -15.160 43.807 1.00131.27 N ANISOU 2762 NZ LYS A 521 22013 16443 11422 1476 1548 -108 N ATOM 2763 N ARG A 522 -1.521 -18.979 44.114 1.00 80.62 N ANISOU 2763 N ARG A 522 15568 9632 5431 291 789 -130 N ATOM 2764 CA ARG A 522 -1.398 -19.792 42.909 1.00 78.39 C ANISOU 2764 CA ARG A 522 15019 9373 5391 135 751 -84 C ATOM 2765 C ARG A 522 -1.544 -21.275 43.229 1.00 78.42 C ANISOU 2765 C ARG A 522 14904 9446 5445 49 837 41 C ATOM 2766 O ARG A 522 -2.260 -22.002 42.531 1.00 80.94 O ANISOU 2766 O ARG A 522 15017 9837 5900 -32 935 108 O ATOM 2767 CB ARG A 522 -0.057 -19.518 42.227 1.00 77.29 C ANISOU 2767 CB ARG A 522 14912 9123 5331 -2 531 -153 C ATOM 2768 CG ARG A 522 0.067 -18.124 41.635 1.00 76.90 C ANISOU 2768 CG ARG A 522 14980 8979 5261 28 451 -271 C ATOM 2769 CD ARG A 522 1.261 -18.027 40.701 1.00 75.45 C ANISOU 2769 CD ARG A 522 14743 8728 5197 -149 259 -313 C ATOM 2770 NE ARG A 522 2.520 -17.957 41.433 1.00 76.05 N ANISOU 2770 NE ARG A 522 14960 8789 5146 -248 98 -336 N ATOM 2771 CZ ARG A 522 3.115 -16.828 41.795 1.00 77.13 C ANISOU 2771 CZ ARG A 522 15339 8845 5120 -300 -20 -437 C ATOM 2772 NH1 ARG A 522 2.588 -15.648 41.513 1.00 77.73 N ANISOU 2772 NH1 ARG A 522 15597 8801 5135 -233 19 -528 N ATOM 2773 NH2 ARG A 522 4.266 -16.885 42.459 1.00 77.92 N ANISOU 2773 NH2 ARG A 522 15519 8991 5096 -424 -179 -441 N ATOM 2774 N VAL A 523 -0.875 -21.739 44.287 1.00 79.17 N ANISOU 2774 N VAL A 523 15151 9518 5411 54 802 77 N ATOM 2775 CA VAL A 523 -0.938 -23.153 44.647 1.00 79.49 C ANISOU 2775 CA VAL A 523 15146 9586 5471 -11 891 204 C ATOM 2776 C VAL A 523 -2.343 -23.538 45.098 1.00 80.90 C ANISOU 2776 C VAL A 523 15255 9882 5602 26 1125 285 C ATOM 2777 O VAL A 523 -2.764 -24.689 44.930 1.00 81.12 O ANISOU 2777 O VAL A 523 15189 9935 5698 -94 1234 388 O ATOM 2778 CB VAL A 523 0.116 -23.468 45.726 1.00 80.29 C ANISOU 2778 CB VAL A 523 15437 9656 5413 27 796 233 C ATOM 2779 CG1 VAL A 523 0.130 -24.954 46.053 1.00 80.80 C ANISOU 2779 CG1 VAL A 523 15501 9714 5484 -14 893 374 C ATOM 2780 CG2 VAL A 523 1.493 -23.009 45.272 1.00 79.30 C ANISOU 2780 CG2 VAL A 523 15330 9486 5316 -27 559 163 C ATOM 2781 N ILE A 524 -3.096 -22.590 45.657 1.00 82.17 N ANISOU 2781 N ILE A 524 15471 10121 5628 185 1216 247 N ATOM 2782 CA ILE A 524 -4.449 -22.890 46.116 1.00 83.88 C ANISOU 2782 CA ILE A 524 15584 10508 5779 239 1450 340 C ATOM 2783 C ILE A 524 -5.414 -22.993 44.939 1.00 83.49 C ANISOU 2783 C ILE A 524 15237 10594 5893 152 1527 369 C ATOM 2784 O ILE A 524 -6.278 -23.878 44.909 1.00 84.47 O ANISOU 2784 O ILE A 524 15191 10861 6043 29 1679 480 O ATOM 2785 CB ILE A 524 -4.901 -21.834 47.142 1.00 85.72 C ANISOU 2785 CB ILE A 524 15993 10793 5784 487 1537 299 C ATOM 2786 CG1 ILE A 524 -4.293 -22.134 48.514 1.00 86.84 C ANISOU 2786 CG1 ILE A 524 16395 10870 5729 533 1526 321 C ATOM 2787 CG2 ILE A 524 -6.417 -21.777 47.235 1.00 87.50 C ANISOU 2787 CG2 ILE A 524 16028 11256 5963 592 1778 384 C ATOM 2788 CD1 ILE A 524 -4.388 -20.984 49.489 1.00 88.53 C ANISOU 2788 CD1 ILE A 524 16876 11065 5697 760 1554 243 C ATOM 2789 N THR A 525 -5.279 -22.105 43.949 1.00104.77 N ANISOU 2789 N THR A 525 17868 13256 8684 193 1420 275 N ATOM 2790 CA THR A 525 -6.169 -22.148 42.791 1.00102.54 C ANISOU 2790 CA THR A 525 17296 13124 8540 122 1473 304 C ATOM 2791 C THR A 525 -5.978 -23.419 41.972 1.00 98.19 C ANISOU 2791 C THR A 525 16607 12540 8160 -166 1438 357 C ATOM 2792 O THR A 525 -6.919 -23.871 41.310 1.00104.53 O ANISOU 2792 O THR A 525 17166 13516 9033 -299 1526 421 O ATOM 2793 CB THR A 525 -5.956 -20.916 41.911 1.00 96.17 C ANISOU 2793 CB THR A 525 16499 12258 7784 243 1358 194 C ATOM 2794 OG1 THR A 525 -4.572 -20.811 41.557 1.00 98.17 O ANISOU 2794 OG1 THR A 525 16909 12278 8113 149 1152 105 O ATOM 2795 CG2 THR A 525 -6.397 -19.655 42.641 1.00112.04 C ANISOU 2795 CG2 THR A 525 18675 14299 9596 547 1438 151 C ATOM 2796 N THR A 526 -4.779 -24.005 41.996 1.00 80.30 N ANISOU 2796 N THR A 526 14500 10066 5943 -263 1312 337 N ATOM 2797 CA THR A 526 -4.590 -25.300 41.351 1.00 83.14 C ANISOU 2797 CA THR A 526 14807 10358 6424 -502 1311 397 C ATOM 2798 C THR A 526 -5.266 -26.418 42.135 1.00 87.55 C ANISOU 2798 C THR A 526 15387 10982 6895 -618 1491 523 C ATOM 2799 O THR A 526 -5.753 -27.383 41.538 1.00 87.95 O ANISOU 2799 O THR A 526 15348 11052 7016 -853 1561 586 O ATOM 2800 CB THR A 526 -3.100 -25.600 41.178 1.00 82.83 C ANISOU 2800 CB THR A 526 14933 10102 6435 -514 1146 359 C ATOM 2801 OG1 THR A 526 -2.504 -25.826 42.462 1.00 94.57 O ANISOU 2801 OG1 THR A 526 16626 11535 7771 -412 1149 397 O ATOM 2802 CG2 THR A 526 -2.397 -24.441 40.488 1.00 83.10 C ANISOU 2802 CG2 THR A 526 14956 10085 6535 -429 973 240 C ATOM 2803 N PHE A 527 -5.302 -26.308 43.467 1.00 88.76 N ANISOU 2803 N PHE A 527 15685 11162 6879 -477 1570 561 N ATOM 2804 CA PHE A 527 -6.035 -27.283 44.269 1.00 85.88 C ANISOU 2804 CA PHE A 527 15344 10876 6410 -584 1762 690 C ATOM 2805 C PHE A 527 -7.537 -27.163 44.044 1.00 90.07 C ANISOU 2805 C PHE A 527 15599 11696 6929 -663 1928 750 C ATOM 2806 O PHE A 527 -8.246 -28.175 43.992 1.00 93.27 O ANISOU 2806 O PHE A 527 15926 12186 7328 -911 2061 855 O ATOM 2807 CB PHE A 527 -5.711 -27.099 45.752 1.00 85.53 C ANISOU 2807 CB PHE A 527 15523 10806 6170 -391 1805 715 C ATOM 2808 CG PHE A 527 -4.497 -27.856 46.212 1.00 86.18 C ANISOU 2808 CG PHE A 527 15857 10672 6215 -390 1715 741 C ATOM 2809 CD1 PHE A 527 -4.364 -29.208 45.947 1.00 90.25 C ANISOU 2809 CD1 PHE A 527 16448 11067 6777 -580 1772 834 C ATOM 2810 CD2 PHE A 527 -3.498 -27.216 46.927 1.00 84.73 C ANISOU 2810 CD2 PHE A 527 15851 10417 5926 -195 1578 681 C ATOM 2811 CE1 PHE A 527 -3.250 -29.907 46.376 1.00 90.06 C ANISOU 2811 CE1 PHE A 527 16663 10860 6696 -519 1704 878 C ATOM 2812 CE2 PHE A 527 -2.383 -27.908 47.359 1.00 84.69 C ANISOU 2812 CE2 PHE A 527 16038 10273 5866 -168 1491 725 C ATOM 2813 CZ PHE A 527 -2.259 -29.256 47.084 1.00 85.03 C ANISOU 2813 CZ PHE A 527 16145 10204 5957 -301 1560 830 C ATOM 2814 N ARG A 528 -8.038 -25.933 43.909 1.00 92.33 N ANISOU 2814 N ARG A 528 15742 12148 7191 -458 1925 694 N ATOM 2815 CA ARG A 528 -9.477 -25.723 43.787 1.00 97.02 C ANISOU 2815 CA ARG A 528 16039 13086 7739 -464 2091 772 C ATOM 2816 C ARG A 528 -9.994 -26.159 42.422 1.00103.52 C ANISOU 2816 C ARG A 528 16591 14027 8714 -728 2057 788 C ATOM 2817 O ARG A 528 -11.038 -26.816 42.329 1.00 97.32 O ANISOU 2817 O ARG A 528 15584 13494 7899 -948 2196 899 O ATOM 2818 CB ARG A 528 -9.808 -24.253 44.041 1.00 98.02 C ANISOU 2818 CB ARG A 528 16139 13335 7768 -104 2107 714 C ATOM 2819 CG ARG A 528 -11.295 -23.948 44.099 1.00108.00 C ANISOU 2819 CG ARG A 528 17091 15006 8937 -14 2303 819 C ATOM 2820 CD ARG A 528 -11.582 -22.537 43.609 1.00115.12 C ANISOU 2820 CD ARG A 528 17921 16004 9816 310 2273 751 C ATOM 2821 NE ARG A 528 -10.587 -21.581 44.082 1.00118.12 N ANISOU 2821 NE ARG A 528 18668 16082 10131 561 2163 618 N ATOM 2822 CZ ARG A 528 -10.425 -20.362 43.586 1.00118.50 C ANISOU 2822 CZ ARG A 528 18796 16059 10170 801 2085 522 C ATOM 2823 NH1 ARG A 528 -11.177 -19.913 42.593 1.00124.44 N ANISOU 2823 NH1 ARG A 528 19280 17023 10978 876 2104 548 N ATOM 2824 NH2 ARG A 528 -9.486 -19.572 44.099 1.00103.30 N ANISOU 2824 NH2 ARG A 528 17242 13847 8161 959 1984 400 N ATOM 2825 N THR A 529 -9.280 -25.807 41.352 1.00108.82 N ANISOU 2825 N THR A 529 17277 14535 9535 -734 1874 682 N ATOM 2826 CA THR A 529 -9.751 -26.058 39.996 1.00102.93 C ANISOU 2826 CA THR A 529 16286 13905 8918 -953 1825 682 C ATOM 2827 C THR A 529 -9.149 -27.303 39.360 1.00101.81 C ANISOU 2827 C THR A 529 16267 13533 8884 -1279 1759 681 C ATOM 2828 O THR A 529 -9.749 -27.851 38.429 1.00105.30 O ANISOU 2828 O THR A 529 16531 14092 9387 -1553 1764 710 O ATOM 2829 CB THR A 529 -9.448 -24.855 39.095 1.00 97.38 C ANISOU 2829 CB THR A 529 15522 13180 8299 -748 1681 573 C ATOM 2830 OG1 THR A 529 -8.031 -24.653 39.026 1.00 91.98 O ANISOU 2830 OG1 THR A 529 15112 12152 7683 -678 1518 467 O ATOM 2831 CG2 THR A 529 -10.105 -23.599 39.647 1.00106.05 C ANISOU 2831 CG2 THR A 529 16546 14483 9265 -395 1765 578 C ATOM 2832 N GLY A 530 -7.991 -27.759 39.828 1.00107.28 N ANISOU 2832 N GLY A 530 17268 13913 9581 -1248 1699 654 N ATOM 2833 CA GLY A 530 -7.332 -28.872 39.176 1.00112.76 C ANISOU 2833 CA GLY A 530 18119 14363 10360 -1484 1645 653 C ATOM 2834 C GLY A 530 -6.761 -28.544 37.818 1.00110.39 C ANISOU 2834 C GLY A 530 17768 13961 10213 -1503 1480 555 C ATOM 2835 O GLY A 530 -6.522 -29.452 37.018 1.00107.24 O ANISOU 2835 O GLY A 530 17449 13417 9881 -1728 1457 556 O ATOM 2836 N THR A 531 -6.544 -27.263 37.531 1.00 97.30 N ANISOU 2836 N THR A 531 16011 12362 8598 -1271 1374 469 N ATOM 2837 CA THR A 531 -6.002 -26.810 36.261 1.00 89.03 C ANISOU 2837 CA THR A 531 14913 11229 7685 -1268 1221 378 C ATOM 2838 C THR A 531 -4.748 -25.981 36.504 1.00 91.59 C ANISOU 2838 C THR A 531 15400 11377 8023 -1031 1086 294 C ATOM 2839 O THR A 531 -4.515 -25.472 37.605 1.00 92.24 O ANISOU 2839 O THR A 531 15592 11456 7998 -849 1102 293 O ATOM 2840 CB THR A 531 -7.027 -25.979 35.477 1.00 93.60 C ANISOU 2840 CB THR A 531 15201 12073 8290 -1246 1220 362 C ATOM 2841 OG1 THR A 531 -7.238 -24.726 36.140 1.00 90.44 O ANISOU 2841 OG1 THR A 531 14776 11781 7807 -941 1237 339 O ATOM 2842 CG2 THR A 531 -8.352 -26.720 35.373 1.00 92.03 C ANISOU 2842 CG2 THR A 531 14787 12139 8042 -1496 1353 462 C ATOM 2843 N TRP A 532 -3.939 -25.846 35.454 1.00 95.92 N ANISOU 2843 N TRP A 532 15965 11791 8688 -1057 951 227 N ATOM 2844 CA TRP A 532 -2.717 -25.057 35.501 1.00 94.35 C ANISOU 2844 CA TRP A 532 15886 11458 8505 -893 808 151 C ATOM 2845 C TRP A 532 -2.953 -23.589 35.163 1.00 87.65 C ANISOU 2845 C TRP A 532 14958 10688 7657 -743 746 72 C ATOM 2846 O TRP A 532 -2.007 -22.894 34.775 1.00 86.51 O ANISOU 2846 O TRP A 532 14887 10433 7550 -683 614 0 O ATOM 2847 CB TRP A 532 -1.673 -25.644 34.550 1.00 92.42 C ANISOU 2847 CB TRP A 532 15701 11045 8369 -982 710 132 C ATOM 2848 CG TRP A 532 -1.233 -27.033 34.893 1.00 93.84 C ANISOU 2848 CG TRP A 532 16037 11096 8521 -1066 771 211 C ATOM 2849 CD1 TRP A 532 -1.736 -28.198 34.393 1.00 94.16 C ANISOU 2849 CD1 TRP A 532 16109 11084 8585 -1266 864 262 C ATOM 2850 CD2 TRP A 532 -0.190 -27.403 35.802 1.00 94.91 C ANISOU 2850 CD2 TRP A 532 16350 11135 8576 -946 746 253 C ATOM 2851 NE1 TRP A 532 -1.074 -29.271 34.938 1.00 99.31 N ANISOU 2851 NE1 TRP A 532 16984 11575 9174 -1255 915 334 N ATOM 2852 CE2 TRP A 532 -0.121 -28.810 35.807 1.00 95.62 C ANISOU 2852 CE2 TRP A 532 16589 11099 8645 -1041 843 337 C ATOM 2853 CE3 TRP A 532 0.690 -26.682 36.615 1.00 94.74 C ANISOU 2853 CE3 TRP A 532 16389 11130 8479 -777 648 231 C ATOM 2854 CZ2 TRP A 532 0.793 -29.509 36.592 1.00 93.11 C ANISOU 2854 CZ2 TRP A 532 16465 10679 8235 -922 852 413 C ATOM 2855 CZ3 TRP A 532 1.596 -27.378 37.393 1.00 90.20 C ANISOU 2855 CZ3 TRP A 532 15966 10491 7813 -690 640 304 C ATOM 2856 CH2 TRP A 532 1.641 -28.777 37.375 1.00 92.84 C ANISOU 2856 CH2 TRP A 532 16435 10709 8132 -738 745 399 C ATOM 2857 N ASP A 533 -4.191 -23.105 35.305 1.00 98.41 N ANISOU 2857 N ASP A 533 16182 12246 8964 -675 848 95 N ATOM 2858 CA ASP A 533 -4.520 -21.741 34.904 1.00101.74 C ANISOU 2858 CA ASP A 533 16557 12733 9367 -495 813 35 C ATOM 2859 C ASP A 533 -3.740 -20.693 35.687 1.00101.30 C ANISOU 2859 C ASP A 533 16739 12542 9210 -310 748 -37 C ATOM 2860 O ASP A 533 -3.548 -19.580 35.187 1.00 98.32 O ANISOU 2860 O ASP A 533 16423 12107 8828 -200 677 -109 O ATOM 2861 CB ASP A 533 -6.022 -21.497 35.064 1.00104.52 C ANISOU 2861 CB ASP A 533 16707 13365 9639 -406 959 103 C ATOM 2862 CG ASP A 533 -6.852 -22.319 34.098 1.00111.63 C ANISOU 2862 CG ASP A 533 17345 14446 10624 -627 994 164 C ATOM 2863 OD1 ASP A 533 -6.263 -22.968 33.207 1.00110.82 O ANISOU 2863 OD1 ASP A 533 17255 14210 10641 -827 902 136 O ATOM 2864 OD2 ASP A 533 -8.094 -22.318 34.228 1.00116.60 O ANISOU 2864 OD2 ASP A 533 17754 15368 11181 -606 1114 244 O ATOM 2865 N ALA A 534 -3.289 -21.020 36.900 1.00108.28 N ANISOU 2865 N ALA A 534 17781 13367 9992 -287 769 -19 N ATOM 2866 CA ALA A 534 -2.514 -20.068 37.686 1.00100.83 C ANISOU 2866 CA ALA A 534 17083 12304 8925 -159 691 -92 C ATOM 2867 C ALA A 534 -1.122 -19.840 37.113 1.00 98.08 C ANISOU 2867 C ALA A 534 16822 11797 8648 -259 504 -160 C ATOM 2868 O ALA A 534 -0.525 -18.789 37.369 1.00101.31 O ANISOU 2868 O ALA A 534 17416 12113 8966 -202 414 -241 O ATOM 2869 CB ALA A 534 -2.407 -20.545 39.135 1.00 99.77 C ANISOU 2869 CB ALA A 534 17084 12178 8646 -120 755 -46 C ATOM 2870 N TYR A 535 -0.593 -20.795 36.347 1.00 99.03 N ANISOU 2870 N TYR A 535 16828 11888 8911 -413 453 -126 N ATOM 2871 CA TYR A 535 0.733 -20.674 35.752 1.00102.19 C ANISOU 2871 CA TYR A 535 17265 12186 9376 -497 292 -168 C ATOM 2872 C TYR A 535 0.696 -20.716 34.229 1.00104.71 C ANISOU 2872 C TYR A 535 17440 12487 9858 -582 256 -186 C ATOM 2873 O TYR A 535 1.757 -20.731 33.594 1.00100.41 O ANISOU 2873 O TYR A 535 16894 11878 9380 -655 142 -206 O ATOM 2874 CB TYR A 535 1.662 -21.771 36.284 1.00100.89 C ANISOU 2874 CB TYR A 535 17134 12002 9198 -551 259 -101 C ATOM 2875 CG TYR A 535 1.752 -21.835 37.794 1.00100.74 C ANISOU 2875 CG TYR A 535 17259 12011 9006 -470 288 -72 C ATOM 2876 CD1 TYR A 535 2.804 -21.229 38.470 1.00101.24 C ANISOU 2876 CD1 TYR A 535 17454 12065 8948 -456 153 -110 C ATOM 2877 CD2 TYR A 535 0.798 -22.514 38.543 1.00 98.06 C ANISOU 2877 CD2 TYR A 535 16923 11724 8610 -431 445 -2 C ATOM 2878 CE1 TYR A 535 2.895 -21.286 39.848 1.00 98.26 C ANISOU 2878 CE1 TYR A 535 17220 11721 8393 -387 168 -86 C ATOM 2879 CE2 TYR A 535 0.881 -22.575 39.922 1.00 98.80 C ANISOU 2879 CE2 TYR A 535 17163 11843 8535 -348 477 28 C ATOM 2880 CZ TYR A 535 1.933 -21.959 40.569 1.00 98.18 C ANISOU 2880 CZ TYR A 535 17225 11745 8334 -317 334 -17 C ATOM 2881 OH TYR A 535 2.024 -22.018 41.940 1.00 98.80 O ANISOU 2881 OH TYR A 535 17459 11855 8224 -240 356 10 O ATOM 2882 N ALA A 536 -0.494 -20.733 33.627 1.00100.27 N ANISOU 2882 N ALA A 536 16743 12008 9347 -573 349 -172 N ATOM 2883 CA ALA A 536 -0.628 -20.778 32.170 1.00 95.52 C ANISOU 2883 CA ALA A 536 16007 11407 8881 -656 313 -188 C ATOM 2884 C ALA A 536 -0.562 -19.358 31.607 1.00 97.85 C ANISOU 2884 C ALA A 536 16354 11663 9161 -562 244 -265 C ATOM 2885 O ALA A 536 -1.539 -18.792 31.113 1.00 97.52 O ANISOU 2885 O ALA A 536 16232 11708 9115 -474 296 -268 O ATOM 2886 CB ALA A 536 -1.921 -21.481 31.776 1.00 90.88 C ANISOU 2886 CB ALA A 536 15238 10963 8328 -721 429 -129 C ATOM 2887 N ALA A 537 0.639 -18.780 31.693 1.00111.05 N ANISOU 2887 N ALA A 537 18170 13213 10810 -585 126 -318 N ATOM 2888 CA ALA A 537 0.885 -17.432 31.188 1.00110.89 C ANISOU 2888 CA ALA A 537 18268 13109 10758 -539 55 -393 C ATOM 2889 C ALA A 537 1.951 -17.449 30.101 1.00112.59 C ANISOU 2889 C ALA A 537 18445 13254 11080 -678 -61 -414 C ATOM 2890 O ALA A 537 1.647 -17.128 28.949 1.00112.72 O ANISOU 2890 O ALA A 537 18395 13260 11172 -680 -68 -429 O ATOM 2891 CB ALA A 537 1.268 -16.497 32.336 1.00120.22 C ANISOU 2891 CB ALA A 537 19701 14213 11765 -473 26 -445 C ATOM 2892 N ASN A 538 3.195 -17.813 30.426 1.00113.42 N ANISOU 2892 N ASN A 538 18577 13337 11179 -781 -150 -405 N ATOM 2893 CA ASN A 538 4.237 -17.868 29.407 1.00108.84 C ANISOU 2893 CA ASN A 538 17933 12732 10688 -898 -245 -407 C ATOM 2894 C ASN A 538 3.974 -18.971 28.392 1.00106.43 C ANISOU 2894 C ASN A 538 17459 12455 10526 -926 -193 -358 C ATOM 2895 O ASN A 538 4.390 -18.857 27.233 1.00111.43 O ANISOU 2895 O ASN A 538 18037 13060 11240 -985 -236 -370 O ATOM 2896 CB ASN A 538 5.605 -18.061 30.061 1.00110.71 C ANISOU 2896 CB ASN A 538 18194 13008 10861 -979 -344 -384 C ATOM 2897 CG ASN A 538 5.936 -16.961 31.050 1.00117.44 C ANISOU 2897 CG ASN A 538 19243 13831 11546 -1007 -415 -442 C ATOM 2898 OD1 ASN A 538 5.260 -15.934 31.101 1.00112.55 O ANISOU 2898 OD1 ASN A 538 18785 13117 10860 -957 -387 -509 O ATOM 2899 ND2 ASN A 538 6.982 -17.171 31.841 1.00125.74 N ANISOU 2899 ND2 ASN A 538 20301 14967 12506 -1080 -506 -414 N ATOM 2900 N LEU A 539 3.292 -20.043 28.801 1.00 95.85 N ANISOU 2900 N LEU A 539 16062 11158 9199 -902 -97 -305 N ATOM 2901 CA LEU A 539 2.916 -21.077 27.844 1.00 90.39 C ANISOU 2901 CA LEU A 539 15265 10467 8611 -964 -42 -270 C ATOM 2902 C LEU A 539 1.872 -20.558 26.863 1.00 88.16 C ANISOU 2902 C LEU A 539 14903 10219 8376 -967 -20 -304 C ATOM 2903 O LEU A 539 1.913 -20.887 25.673 1.00 94.70 O ANISOU 2903 O LEU A 539 15667 11028 9286 -1038 -34 -308 O ATOM 2904 CB LEU A 539 2.394 -22.313 28.574 1.00 91.31 C ANISOU 2904 CB LEU A 539 15385 10605 8702 -977 62 -205 C ATOM 2905 CG LEU A 539 2.065 -23.506 27.672 1.00 88.46 C ANISOU 2905 CG LEU A 539 14987 10210 8415 -1084 124 -171 C ATOM 2906 CD1 LEU A 539 3.333 -24.075 27.051 1.00 92.30 C ANISOU 2906 CD1 LEU A 539 15520 10608 8943 -1086 81 -151 C ATOM 2907 CD2 LEU A 539 1.298 -24.580 28.424 1.00 90.90 C ANISOU 2907 CD2 LEU A 539 15332 10533 8674 -1138 243 -110 C ATOM 2908 N MET A 540 0.931 -19.741 27.344 1.00 94.59 N ANISOU 2908 N MET A 540 15723 11095 9120 -869 19 -322 N ATOM 2909 CA MET A 540 -0.091 -19.193 26.458 1.00101.52 C ANISOU 2909 CA MET A 540 16506 12051 10016 -825 41 -335 C ATOM 2910 C MET A 540 0.477 -18.116 25.542 1.00103.08 C ANISOU 2910 C MET A 540 16773 12159 10233 -798 -46 -388 C ATOM 2911 O MET A 540 -0.053 -17.894 24.447 1.00 96.46 O ANISOU 2911 O MET A 540 15850 11364 9435 -791 -52 -391 O ATOM 2912 CB MET A 540 -1.257 -18.641 27.278 1.00102.49 C ANISOU 2912 CB MET A 540 16613 12296 10034 -673 129 -317 C ATOM 2913 CG MET A 540 -2.083 -19.714 27.970 1.00 99.75 C ANISOU 2913 CG MET A 540 16151 12084 9665 -727 234 -249 C ATOM 2914 SD MET A 540 -2.637 -20.996 26.829 1.00126.51 S ANISOU 2914 SD MET A 540 19353 15563 13151 -949 252 -209 S ATOM 2915 CE MET A 540 -3.351 -22.181 27.966 1.00110.11 C ANISOU 2915 CE MET A 540 17236 13589 11013 -1050 381 -130 C ATOM 2916 N ALA A 541 1.545 -17.439 25.970 1.00120.07 N ANISOU 2916 N ALA A 541 19084 14197 12342 -801 -116 -426 N ATOM 2917 CA ALA A 541 2.230 -16.492 25.097 1.00112.24 C ANISOU 2917 CA ALA A 541 18178 13107 11362 -831 -197 -469 C ATOM 2918 C ALA A 541 3.061 -17.201 24.037 1.00111.18 C ANISOU 2918 C ALA A 541 17945 12959 11341 -962 -246 -453 C ATOM 2919 O ALA A 541 3.176 -16.705 22.911 1.00113.50 O ANISOU 2919 O ALA A 541 18237 13214 11673 -982 -279 -472 O ATOM 2920 CB ALA A 541 3.119 -15.561 25.921 1.00111.04 C ANISOU 2920 CB ALA A 541 18233 12855 11101 -852 -261 -513 C ATOM 2921 N LYS A 542 3.647 -18.351 24.377 1.00 89.30 N ANISOU 2921 N LYS A 542 15111 10213 8607 -1028 -239 -412 N ATOM 2922 CA LYS A 542 4.359 -19.142 23.380 1.00 83.69 C ANISOU 2922 CA LYS A 542 14327 9489 7984 -1106 -255 -387 C ATOM 2923 C LYS A 542 3.396 -19.781 22.388 1.00 77.68 C ANISOU 2923 C LYS A 542 13480 8748 7285 -1130 -201 -382 C ATOM 2924 O LYS A 542 3.757 -19.993 21.225 1.00 81.64 O ANISOU 2924 O LYS A 542 13957 9220 7844 -1180 -220 -385 O ATOM 2925 CB LYS A 542 5.206 -20.213 24.065 1.00 84.61 C ANISOU 2925 CB LYS A 542 14435 9623 8091 -1117 -243 -330 C ATOM 2926 CG LYS A 542 6.518 -19.700 24.639 1.00 82.74 C ANISOU 2926 CG LYS A 542 14226 9417 7794 -1135 -329 -319 C ATOM 2927 CD LYS A 542 7.294 -20.817 25.321 1.00 90.89 C ANISOU 2927 CD LYS A 542 15231 10506 8798 -1094 -311 -241 C ATOM 2928 CE LYS A 542 8.701 -20.373 25.688 1.00 96.72 C ANISOU 2928 CE LYS A 542 15932 11348 9468 -1128 -412 -211 C ATOM 2929 NZ LYS A 542 9.507 -21.497 26.243 1.00 90.51 N ANISOU 2929 NZ LYS A 542 15096 10654 8640 -1038 -392 -111 N ATOM 2930 N LYS A 543 2.175 -20.095 22.827 1.00 87.06 N ANISOU 2930 N LYS A 543 14620 10009 8448 -1110 -135 -370 N ATOM 2931 CA LYS A 543 1.170 -20.620 21.910 1.00 89.86 C ANISOU 2931 CA LYS A 543 14875 10431 8835 -1176 -100 -364 C ATOM 2932 C LYS A 543 0.676 -19.547 20.949 1.00 93.86 C ANISOU 2932 C LYS A 543 15340 10982 9340 -1117 -143 -394 C ATOM 2933 O LYS A 543 0.285 -19.860 19.819 1.00100.08 O ANISOU 2933 O LYS A 543 16058 11809 10160 -1187 -155 -396 O ATOM 2934 CB LYS A 543 -0.006 -21.205 22.692 1.00 95.40 C ANISOU 2934 CB LYS A 543 15505 11253 9491 -1197 -18 -328 C ATOM 2935 CG LYS A 543 0.282 -22.535 23.368 1.00 94.23 C ANISOU 2935 CG LYS A 543 15418 11047 9337 -1288 44 -287 C ATOM 2936 CD LYS A 543 -0.923 -23.024 24.154 1.00103.60 C ANISOU 2936 CD LYS A 543 16534 12364 10466 -1337 133 -245 C ATOM 2937 CE LYS A 543 -0.706 -24.433 24.680 1.00107.82 C ANISOU 2937 CE LYS A 543 17174 12809 10982 -1453 207 -200 C ATOM 2938 NZ LYS A 543 -1.870 -24.914 25.474 1.00117.64 N ANISOU 2938 NZ LYS A 543 18353 14187 12158 -1535 303 -150 N ATOM 2939 N ARG A 544 0.684 -18.284 21.379 1.00 95.45 N ANISOU 2939 N ARG A 544 15615 11166 9486 -986 -164 -415 N ATOM 2940 CA ARG A 544 0.214 -17.204 20.519 1.00 93.48 C ANISOU 2940 CA ARG A 544 15373 10934 9210 -889 -190 -432 C ATOM 2941 C ARG A 544 1.210 -16.914 19.403 1.00 93.10 C ANISOU 2941 C ARG A 544 15390 10769 9215 -959 -258 -457 C ATOM 2942 O ARG A 544 0.813 -16.607 18.272 1.00 92.95 O ANISOU 2942 O ARG A 544 15333 10781 9204 -940 -278 -458 O ATOM 2943 CB ARG A 544 -0.041 -15.949 21.353 1.00 95.08 C ANISOU 2943 CB ARG A 544 15714 11105 9308 -713 -171 -447 C ATOM 2944 CG ARG A 544 -1.080 -15.008 20.771 1.00107.82 C ANISOU 2944 CG ARG A 544 17316 12800 10851 -527 -148 -432 C ATOM 2945 CD ARG A 544 -1.482 -13.946 21.783 1.00108.67 C ANISOU 2945 CD ARG A 544 17594 12873 10824 -312 -92 -437 C ATOM 2946 NE ARG A 544 -2.283 -14.500 22.867 1.00121.09 N ANISOU 2946 NE ARG A 544 19053 14602 12353 -250 -10 -399 N ATOM 2947 CZ ARG A 544 -1.897 -14.551 24.135 1.00120.22 C ANISOU 2947 CZ ARG A 544 19065 14419 12195 -254 16 -418 C ATOM 2948 NH1 ARG A 544 -0.718 -14.089 24.518 1.00119.95 N ANISOU 2948 NH1 ARG A 544 19256 14178 12142 -333 -47 -475 N ATOM 2949 NH2 ARG A 544 -2.714 -15.080 25.042 1.00112.18 N ANISOU 2949 NH2 ARG A 544 17931 13560 11132 -194 104 -372 N ATOM 2950 N VAL A 545 2.507 -17.008 19.701 1.00 78.39 N ANISOU 2950 N VAL A 545 13609 8801 7375 -1038 -292 -467 N ATOM 2951 CA VAL A 545 3.524 -16.726 18.693 1.00 73.98 C ANISOU 2951 CA VAL A 545 13090 8164 6855 -1111 -344 -477 C ATOM 2952 C VAL A 545 3.549 -17.823 17.636 1.00 80.68 C ANISOU 2952 C VAL A 545 13840 9039 7775 -1186 -329 -460 C ATOM 2953 O VAL A 545 3.650 -17.543 16.435 1.00 87.63 O ANISOU 2953 O VAL A 545 14723 9897 8674 -1204 -352 -469 O ATOM 2954 CB VAL A 545 4.900 -16.551 19.363 1.00 69.95 C ANISOU 2954 CB VAL A 545 12649 7602 6327 -1184 -385 -474 C ATOM 2955 CG1 VAL A 545 5.988 -16.388 18.313 1.00 78.01 C ANISOU 2955 CG1 VAL A 545 13666 8592 7382 -1273 -425 -465 C ATOM 2956 CG2 VAL A 545 4.881 -15.361 20.307 1.00 70.43 C ANISOU 2956 CG2 VAL A 545 12867 7606 6286 -1146 -409 -507 C ATOM 2957 N ILE A 546 3.452 -19.085 18.060 1.00 65.72 N ANISOU 2957 N ILE A 546 11895 7173 5904 -1232 -284 -437 N ATOM 2958 CA ILE A 546 3.522 -20.194 17.114 1.00 64.98 C ANISOU 2958 CA ILE A 546 11780 7062 5849 -1311 -258 -428 C ATOM 2959 C ILE A 546 2.304 -20.198 16.196 1.00 68.97 C ANISOU 2959 C ILE A 546 12220 7642 6343 -1348 -262 -445 C ATOM 2960 O ILE A 546 2.418 -20.467 14.995 1.00 73.47 O ANISOU 2960 O ILE A 546 12802 8187 6926 -1404 -276 -457 O ATOM 2961 CB ILE A 546 3.675 -21.527 17.868 1.00 60.40 C ANISOU 2961 CB ILE A 546 11226 6458 5266 -1347 -194 -395 C ATOM 2962 CG1 ILE A 546 5.019 -21.570 18.597 1.00 64.86 C ANISOU 2962 CG1 ILE A 546 11829 6990 5826 -1289 -201 -360 C ATOM 2963 CG2 ILE A 546 3.557 -22.704 16.913 1.00 64.89 C ANISOU 2963 CG2 ILE A 546 11843 6972 5842 -1437 -150 -394 C ATOM 2964 CD1 ILE A 546 6.202 -21.211 17.722 1.00 59.30 C ANISOU 2964 CD1 ILE A 546 11124 6267 5142 -1281 -235 -351 C ATOM 2965 N ARG A 547 1.123 -19.893 16.740 1.00 92.20 N ANISOU 2965 N ARG A 547 15083 10705 9245 -1310 -251 -439 N ATOM 2966 CA ARG A 547 -0.074 -19.838 15.907 1.00 92.31 C ANISOU 2966 CA ARG A 547 14985 10863 9226 -1337 -267 -438 C ATOM 2967 C ARG A 547 0.021 -18.733 14.863 1.00 97.25 C ANISOU 2967 C ARG A 547 15631 11480 9840 -1245 -324 -451 C ATOM 2968 O ARG A 547 -0.495 -18.886 13.750 1.00 98.16 O ANISOU 2968 O ARG A 547 15687 11673 9935 -1297 -355 -453 O ATOM 2969 CB ARG A 547 -1.318 -19.641 16.774 1.00 99.28 C ANISOU 2969 CB ARG A 547 15743 11930 10050 -1277 -233 -406 C ATOM 2970 CG ARG A 547 -2.093 -20.920 17.042 1.00110.34 C ANISOU 2970 CG ARG A 547 17052 13441 11430 -1457 -187 -382 C ATOM 2971 CD ARG A 547 -3.356 -20.642 17.840 1.00120.85 C ANISOU 2971 CD ARG A 547 18216 15011 12691 -1391 -145 -335 C ATOM 2972 NE ARG A 547 -4.275 -19.769 17.121 1.00123.34 N ANISOU 2972 NE ARG A 547 18380 15539 12946 -1273 -183 -311 N ATOM 2973 CZ ARG A 547 -5.301 -20.194 16.397 1.00121.54 C ANISOU 2973 CZ ARG A 547 17961 15555 12663 -1401 -208 -280 C ATOM 2974 NH1 ARG A 547 -5.571 -21.483 16.270 1.00121.65 N ANISOU 2974 NH1 ARG A 547 17945 15607 12671 -1692 -198 -281 N ATOM 2975 NH2 ARG A 547 -6.077 -19.304 15.784 1.00124.23 N ANISOU 2975 NH2 ARG A 547 18155 16113 12932 -1239 -246 -242 N ATOM 2976 N MET A 548 0.671 -17.617 15.199 1.00 92.91 N ANISOU 2976 N MET A 548 15187 10831 9284 -1126 -338 -460 N ATOM 2977 CA MET A 548 0.880 -16.564 14.212 1.00 88.31 C ANISOU 2977 CA MET A 548 14678 10197 8678 -1053 -380 -468 C ATOM 2978 C MET A 548 1.879 -17.001 13.150 1.00 88.69 C ANISOU 2978 C MET A 548 14772 10149 8779 -1167 -401 -480 C ATOM 2979 O MET A 548 1.666 -16.767 11.954 1.00 90.66 O ANISOU 2979 O MET A 548 15020 10416 9009 -1164 -429 -481 O ATOM 2980 CB MET A 548 1.356 -15.284 14.900 1.00 87.84 C ANISOU 2980 CB MET A 548 14778 10023 8574 -942 -381 -477 C ATOM 2981 CG MET A 548 1.930 -14.248 13.945 1.00 91.93 C ANISOU 2981 CG MET A 548 15439 10423 9066 -917 -414 -484 C ATOM 2982 SD MET A 548 2.597 -12.796 14.782 1.00 99.47 S ANISOU 2982 SD MET A 548 16657 11198 9938 -865 -414 -504 S ATOM 2983 CE MET A 548 4.219 -13.392 15.254 1.00 77.81 C ANISOU 2983 CE MET A 548 13905 8397 7264 -1087 -443 -515 C ATOM 2984 N LEU A 549 2.972 -17.644 13.568 1.00 79.07 N ANISOU 2984 N LEU A 549 13589 8844 7609 -1247 -381 -481 N ATOM 2985 CA LEU A 549 3.986 -18.082 12.616 1.00 79.73 C ANISOU 2985 CA LEU A 549 13710 8858 7726 -1316 -379 -478 C ATOM 2986 C LEU A 549 3.449 -19.152 11.674 1.00 84.41 C ANISOU 2986 C LEU A 549 14275 9480 8316 -1391 -363 -488 C ATOM 2987 O LEU A 549 3.894 -19.247 10.525 1.00 84.29 O ANISOU 2987 O LEU A 549 14306 9424 8298 -1417 -366 -493 O ATOM 2988 CB LEU A 549 5.214 -18.601 13.364 1.00 75.87 C ANISOU 2988 CB LEU A 549 13238 8325 7266 -1343 -352 -454 C ATOM 2989 CG LEU A 549 6.063 -17.551 14.082 1.00 75.39 C ANISOU 2989 CG LEU A 549 13217 8242 7187 -1335 -386 -445 C ATOM 2990 CD1 LEU A 549 7.421 -18.124 14.460 1.00 77.69 C ANISOU 2990 CD1 LEU A 549 13475 8554 7490 -1367 -371 -402 C ATOM 2991 CD2 LEU A 549 6.220 -16.302 13.228 1.00 81.63 C ANISOU 2991 CD2 LEU A 549 14085 8983 7948 -1340 -421 -456 C ATOM 2992 N ILE A 550 2.498 -19.964 12.139 1.00 80.90 N ANISOU 2992 N ILE A 550 13774 9108 7856 -1446 -344 -491 N ATOM 2993 CA ILE A 550 1.909 -20.980 11.275 1.00 74.69 C ANISOU 2993 CA ILE A 550 12994 8348 7038 -1573 -338 -509 C ATOM 2994 C ILE A 550 0.995 -20.338 10.239 1.00 75.88 C ANISOU 2994 C ILE A 550 13071 8624 7137 -1571 -404 -518 C ATOM 2995 O ILE A 550 0.908 -20.809 9.098 1.00 75.52 O ANISOU 2995 O ILE A 550 13070 8572 7054 -1662 -423 -539 O ATOM 2996 CB ILE A 550 1.173 -22.030 12.131 1.00 73.62 C ANISOU 2996 CB ILE A 550 12832 8258 6882 -1682 -297 -503 C ATOM 2997 CG1 ILE A 550 2.179 -22.995 12.761 1.00 72.66 C ANISOU 2997 CG1 ILE A 550 12842 7981 6785 -1686 -222 -488 C ATOM 2998 CG2 ILE A 550 0.145 -22.795 11.308 1.00 71.66 C ANISOU 2998 CG2 ILE A 550 12563 8099 6564 -1865 -316 -523 C ATOM 2999 CD1 ILE A 550 1.595 -23.860 13.854 1.00 79.01 C ANISOU 2999 CD1 ILE A 550 13653 8801 7567 -1765 -168 -470 C ATOM 3000 N VAL A 551 0.323 -19.243 10.602 1.00 85.13 N ANISOU 3000 N VAL A 551 14151 9909 8285 -1445 -436 -497 N ATOM 3001 CA VAL A 551 -0.591 -18.589 9.670 1.00 87.97 C ANISOU 3001 CA VAL A 551 14429 10421 8574 -1390 -495 -485 C ATOM 3002 C VAL A 551 0.180 -17.912 8.542 1.00 87.28 C ANISOU 3002 C VAL A 551 14459 10218 8485 -1335 -520 -493 C ATOM 3003 O VAL A 551 -0.206 -18.002 7.370 1.00 91.09 O ANISOU 3003 O VAL A 551 14927 10771 8911 -1375 -565 -497 O ATOM 3004 CB VAL A 551 -1.494 -17.593 10.420 1.00 85.94 C ANISOU 3004 CB VAL A 551 14071 10313 8270 -1208 -496 -445 C ATOM 3005 CG1 VAL A 551 -2.171 -16.644 9.443 1.00 87.77 C ANISOU 3005 CG1 VAL A 551 14260 10673 8415 -1064 -549 -413 C ATOM 3006 CG2 VAL A 551 -2.533 -18.339 11.240 1.00 88.61 C ANISOU 3006 CG2 VAL A 551 14240 10847 8580 -1286 -473 -422 C ATOM 3007 N ILE A 552 1.281 -17.231 8.869 1.00 88.26 N ANISOU 3007 N ILE A 552 14701 10179 8656 -1264 -495 -491 N ATOM 3008 CA ILE A 552 2.034 -16.529 7.834 1.00 90.92 C ANISOU 3008 CA ILE A 552 15149 10414 8981 -1233 -507 -488 C ATOM 3009 C ILE A 552 2.690 -17.515 6.875 1.00 93.10 C ANISOU 3009 C ILE A 552 15469 10633 9272 -1354 -490 -507 C ATOM 3010 O ILE A 552 2.953 -17.177 5.714 1.00 93.50 O ANISOU 3010 O ILE A 552 15584 10654 9287 -1345 -504 -503 O ATOM 3011 CB ILE A 552 3.071 -15.580 8.465 1.00 92.81 C ANISOU 3011 CB ILE A 552 15502 10516 9247 -1186 -486 -478 C ATOM 3012 CG1 ILE A 552 4.155 -16.369 9.199 1.00 97.22 C ANISOU 3012 CG1 ILE A 552 16052 11012 9874 -1281 -446 -481 C ATOM 3013 CG2 ILE A 552 2.395 -14.606 9.414 1.00 93.59 C ANISOU 3013 CG2 ILE A 552 15624 10634 9301 -1053 -490 -468 C ATOM 3014 CD1 ILE A 552 5.326 -15.522 9.642 1.00102.95 C ANISOU 3014 CD1 ILE A 552 16863 11647 10607 -1298 -442 -466 C ATOM 3015 N VAL A 553 2.961 -18.741 7.329 1.00 80.97 N ANISOU 3015 N VAL A 553 13928 9067 7771 -1450 -447 -522 N ATOM 3016 CA VAL A 553 3.528 -19.750 6.440 1.00 77.22 C ANISOU 3016 CA VAL A 553 13545 8515 7281 -1532 -410 -539 C ATOM 3017 C VAL A 553 2.463 -20.284 5.490 1.00 76.72 C ANISOU 3017 C VAL A 553 13479 8537 7134 -1635 -456 -571 C ATOM 3018 O VAL A 553 2.709 -20.448 4.289 1.00 75.89 O ANISOU 3018 O VAL A 553 13466 8393 6977 -1664 -460 -587 O ATOM 3019 CB VAL A 553 4.180 -20.879 7.260 1.00 73.67 C ANISOU 3019 CB VAL A 553 13142 7982 6867 -1566 -334 -535 C ATOM 3020 CG1 VAL A 553 4.499 -22.069 6.370 1.00 72.79 C ANISOU 3020 CG1 VAL A 553 13177 7777 6704 -1631 -277 -556 C ATOM 3021 CG2 VAL A 553 5.443 -20.374 7.938 1.00 76.53 C ANISOU 3021 CG2 VAL A 553 13493 8300 7286 -1476 -300 -493 C ATOM 3022 N VAL A 554 1.265 -20.558 6.008 1.00 78.15 N ANISOU 3022 N VAL A 554 13547 8860 7286 -1706 -494 -577 N ATOM 3023 CA VAL A 554 0.178 -21.037 5.160 1.00 74.02 C ANISOU 3023 CA VAL A 554 12983 8480 6660 -1848 -558 -599 C ATOM 3024 C VAL A 554 -0.240 -19.960 4.167 1.00 83.66 C ANISOU 3024 C VAL A 554 14145 9821 7820 -1743 -636 -579 C ATOM 3025 O VAL A 554 -0.500 -20.247 2.992 1.00 89.88 O ANISOU 3025 O VAL A 554 14981 10653 8518 -1832 -684 -601 O ATOM 3026 CB VAL A 554 -1.006 -21.502 6.027 1.00 77.05 C ANISOU 3026 CB VAL A 554 13215 9045 7016 -1961 -578 -590 C ATOM 3027 CG1 VAL A 554 -2.205 -21.844 5.156 1.00 80.37 C ANISOU 3027 CG1 VAL A 554 13538 9690 7308 -2134 -667 -599 C ATOM 3028 CG2 VAL A 554 -0.601 -22.696 6.879 1.00 80.20 C ANISOU 3028 CG2 VAL A 554 13727 9296 7451 -2082 -494 -608 C ATOM 3029 N LEU A 555 -0.309 -18.704 4.616 1.00 82.62 N ANISOU 3029 N LEU A 555 13944 9732 7716 -1547 -646 -535 N ATOM 3030 CA LEU A 555 -0.684 -17.618 3.716 1.00 85.16 C ANISOU 3030 CA LEU A 555 14252 10143 7963 -1407 -704 -501 C ATOM 3031 C LEU A 555 0.385 -17.383 2.655 1.00 88.65 C ANISOU 3031 C LEU A 555 14871 10406 8405 -1395 -683 -513 C ATOM 3032 O LEU A 555 0.064 -17.064 1.504 1.00 87.84 O ANISOU 3032 O LEU A 555 14792 10373 8211 -1369 -736 -502 O ATOM 3033 CB LEU A 555 -0.946 -16.339 4.512 1.00 83.45 C ANISOU 3033 CB LEU A 555 13998 9957 7754 -1182 -694 -451 C ATOM 3034 CG LEU A 555 -2.386 -16.062 4.960 1.00 84.60 C ANISOU 3034 CG LEU A 555 13939 10386 7820 -1081 -734 -403 C ATOM 3035 CD1 LEU A 555 -3.278 -15.819 3.753 1.00 93.11 C ANISOU 3035 CD1 LEU A 555 14922 11692 8764 -1035 -820 -366 C ATOM 3036 CD2 LEU A 555 -2.942 -17.193 5.814 1.00 92.93 C ANISOU 3036 CD2 LEU A 555 14845 11564 8900 -1258 -722 -420 C ATOM 3037 N PHE A 556 1.660 -17.539 3.019 1.00 92.13 N ANISOU 3037 N PHE A 556 15422 10648 8936 -1410 -605 -524 N ATOM 3038 CA PHE A 556 2.731 -17.354 2.046 1.00 88.21 C ANISOU 3038 CA PHE A 556 15067 10016 8433 -1402 -567 -520 C ATOM 3039 C PHE A 556 2.700 -18.437 0.975 1.00 85.03 C ANISOU 3039 C PHE A 556 14739 9608 7961 -1522 -567 -560 C ATOM 3040 O PHE A 556 2.895 -18.151 -0.211 1.00 93.69 O ANISOU 3040 O PHE A 556 15923 10688 8987 -1502 -578 -556 O ATOM 3041 CB PHE A 556 4.086 -17.340 2.751 1.00 87.57 C ANISOU 3041 CB PHE A 556 15034 9793 8445 -1397 -484 -505 C ATOM 3042 CG PHE A 556 5.212 -16.865 1.883 1.00 90.64 C ANISOU 3042 CG PHE A 556 15526 10090 8822 -1377 -437 -477 C ATOM 3043 CD1 PHE A 556 5.448 -15.512 1.709 1.00 99.75 C ANISOU 3043 CD1 PHE A 556 16734 11208 9957 -1314 -449 -438 C ATOM 3044 CD2 PHE A 556 6.029 -17.772 1.230 1.00 90.21 C ANISOU 3044 CD2 PHE A 556 15538 9982 8757 -1419 -368 -482 C ATOM 3045 CE1 PHE A 556 6.483 -15.072 0.908 1.00 98.19 C ANISOU 3045 CE1 PHE A 556 16627 10941 9739 -1330 -399 -403 C ATOM 3046 CE2 PHE A 556 7.063 -17.339 0.426 1.00 91.46 C ANISOU 3046 CE2 PHE A 556 15765 10092 8894 -1396 -312 -442 C ATOM 3047 CZ PHE A 556 7.291 -15.988 0.265 1.00 95.66 C ANISOU 3047 CZ PHE A 556 16323 10608 9416 -1371 -330 -401 C ATOM 3048 N PHE A 557 2.460 -19.688 1.374 1.00 81.24 N ANISOU 3048 N PHE A 557 14264 9123 7482 -1653 -548 -601 N ATOM 3049 CA PHE A 557 2.405 -20.772 0.400 1.00 75.15 C ANISOU 3049 CA PHE A 557 13632 8307 6615 -1788 -540 -650 C ATOM 3050 C PHE A 557 1.152 -20.677 -0.460 1.00 79.29 C ANISOU 3050 C PHE A 557 14096 9019 7011 -1880 -658 -668 C ATOM 3051 O PHE A 557 1.190 -20.982 -1.657 1.00 84.94 O ANISOU 3051 O PHE A 557 14941 9713 7619 -1943 -677 -698 O ATOM 3052 CB PHE A 557 2.466 -22.126 1.110 1.00 74.73 C ANISOU 3052 CB PHE A 557 13658 8163 6572 -1913 -477 -686 C ATOM 3053 CG PHE A 557 3.863 -22.587 1.427 1.00 77.18 C ANISOU 3053 CG PHE A 557 14096 8285 6944 -1816 -347 -667 C ATOM 3054 CD1 PHE A 557 4.858 -21.674 1.737 1.00 83.35 C ANISOU 3054 CD1 PHE A 557 14806 9050 7814 -1659 -309 -610 C ATOM 3055 CD2 PHE A 557 4.181 -23.935 1.409 1.00 76.65 C ANISOU 3055 CD2 PHE A 557 14231 8070 6821 -1883 -259 -699 C ATOM 3056 CE1 PHE A 557 6.142 -22.096 2.029 1.00 81.55 C ANISOU 3056 CE1 PHE A 557 14641 8721 7623 -1567 -197 -574 C ATOM 3057 CE2 PHE A 557 5.465 -24.363 1.699 1.00 81.36 C ANISOU 3057 CE2 PHE A 557 14927 8534 7453 -1740 -131 -660 C ATOM 3058 CZ PHE A 557 6.445 -23.441 2.010 1.00 76.89 C ANISOU 3058 CZ PHE A 557 14224 8013 6979 -1580 -105 -593 C ATOM 3059 N LEU A 558 0.032 -20.249 0.129 1.00 82.56 N ANISOU 3059 N LEU A 558 14306 9645 7418 -1878 -738 -642 N ATOM 3060 CA LEU A 558 -1.206 -20.134 -0.636 1.00 89.80 C ANISOU 3060 CA LEU A 558 15107 10819 8195 -1952 -862 -637 C ATOM 3061 C LEU A 558 -1.103 -19.080 -1.732 1.00 93.10 C ANISOU 3061 C LEU A 558 15556 11272 8546 -1787 -906 -599 C ATOM 3062 O LEU A 558 -1.810 -19.164 -2.742 1.00 89.39 O ANISOU 3062 O LEU A 558 15063 10971 7931 -1859 -1002 -603 O ATOM 3063 CB LEU A 558 -2.374 -19.807 0.294 1.00 87.37 C ANISOU 3063 CB LEU A 558 14537 10774 7887 -1929 -918 -590 C ATOM 3064 CG LEU A 558 -3.091 -20.984 0.954 1.00 83.11 C ANISOU 3064 CG LEU A 558 13919 10337 7321 -2189 -927 -621 C ATOM 3065 CD1 LEU A 558 -4.376 -20.509 1.608 1.00 85.84 C ANISOU 3065 CD1 LEU A 558 13957 11032 7626 -2143 -991 -553 C ATOM 3066 CD2 LEU A 558 -3.373 -22.073 -0.067 1.00 86.28 C ANISOU 3066 CD2 LEU A 558 14451 10751 7581 -2481 -980 -687 C ATOM 3067 N CYS A 559 -0.231 -18.088 -1.553 1.00112.03 N ANISOU 3067 N CYS A 559 18018 13517 11030 -1586 -840 -559 N ATOM 3068 CA CYS A 559 -0.078 -17.003 -2.514 1.00105.46 C ANISOU 3068 CA CYS A 559 17254 12684 10131 -1424 -863 -513 C ATOM 3069 C CYS A 559 0.872 -17.351 -3.654 1.00103.88 C ANISOU 3069 C CYS A 559 17259 12318 9891 -1480 -814 -542 C ATOM 3070 O CYS A 559 0.619 -16.972 -4.802 1.00109.08 O ANISOU 3070 O CYS A 559 17975 13043 10428 -1440 -868 -525 O ATOM 3071 CB CYS A 559 0.417 -15.742 -1.805 1.00106.09 C ANISOU 3071 CB CYS A 559 17357 12657 10295 -1222 -807 -456 C ATOM 3072 SG CYS A 559 -0.807 -14.950 -0.739 1.00110.67 S ANISOU 3072 SG CYS A 559 17749 13441 10861 -1050 -855 -400 S ATOM 3073 N TRP A 560 1.961 -18.065 -3.365 1.00 75.44 N ANISOU 3073 N TRP A 560 13769 8521 6375 -1548 -707 -576 N ATOM 3074 CA TRP A 560 3.001 -18.319 -4.353 1.00 79.67 C ANISOU 3074 CA TRP A 560 14493 8904 6873 -1550 -628 -586 C ATOM 3075 C TRP A 560 2.897 -19.685 -5.019 1.00 81.74 C ANISOU 3075 C TRP A 560 14896 9129 7034 -1710 -619 -660 C ATOM 3076 O TRP A 560 3.675 -19.967 -5.935 1.00 80.54 O ANISOU 3076 O TRP A 560 14924 8860 6819 -1693 -546 -670 O ATOM 3077 CB TRP A 560 4.385 -18.175 -3.711 1.00 72.87 C ANISOU 3077 CB TRP A 560 13666 7883 6139 -1485 -499 -554 C ATOM 3078 CG TRP A 560 4.762 -16.753 -3.461 1.00 82.12 C ANISOU 3078 CG TRP A 560 14802 9038 7360 -1368 -492 -485 C ATOM 3079 CD1 TRP A 560 4.667 -16.075 -2.282 1.00 79.56 C ANISOU 3079 CD1 TRP A 560 14383 8722 7126 -1321 -504 -460 C ATOM 3080 CD2 TRP A 560 5.282 -15.823 -4.419 1.00 87.52 C ANISOU 3080 CD2 TRP A 560 15592 9676 7987 -1300 -466 -435 C ATOM 3081 NE1 TRP A 560 5.101 -14.782 -2.444 1.00 87.27 N ANISOU 3081 NE1 TRP A 560 15428 9638 8094 -1242 -487 -404 N ATOM 3082 CE2 TRP A 560 5.484 -14.602 -3.747 1.00 79.86 C ANISOU 3082 CE2 TRP A 560 14608 8667 7070 -1232 -462 -383 C ATOM 3083 CE3 TRP A 560 5.600 -15.906 -5.778 1.00 85.39 C ANISOU 3083 CE3 TRP A 560 15455 9381 7610 -1296 -439 -429 C ATOM 3084 CZ2 TRP A 560 5.989 -13.473 -4.387 1.00 79.97 C ANISOU 3084 CZ2 TRP A 560 14746 8607 7031 -1182 -430 -322 C ATOM 3085 CZ3 TRP A 560 6.100 -14.783 -6.412 1.00 88.18 C ANISOU 3085 CZ3 TRP A 560 15900 9683 7922 -1228 -406 -362 C ATOM 3086 CH2 TRP A 560 6.289 -13.583 -5.717 1.00 84.60 C ANISOU 3086 CH2 TRP A 560 15440 9181 7522 -1182 -401 -308 C ATOM 3087 N MET A 561 1.972 -20.534 -4.589 1.00105.90 N ANISOU 3087 N MET A 561 17904 12276 10057 -1873 -683 -710 N ATOM 3088 CA MET A 561 1.795 -21.832 -5.232 1.00106.81 C ANISOU 3088 CA MET A 561 18214 12327 10041 -2068 -680 -789 C ATOM 3089 C MET A 561 1.117 -21.713 -6.597 1.00109.00 C ANISOU 3089 C MET A 561 18552 12732 10130 -2147 -791 -813 C ATOM 3090 O MET A 561 1.528 -22.412 -7.533 1.00114.75 O ANISOU 3090 O MET A 561 19535 13327 10737 -2218 -746 -867 O ATOM 3091 CB MET A 561 1.002 -22.782 -4.329 1.00109.20 C ANISOU 3091 CB MET A 561 18467 12680 10344 -2271 -712 -833 C ATOM 3092 CG MET A 561 1.861 -23.548 -3.332 1.00111.41 C ANISOU 3092 CG MET A 561 18851 12746 10733 -2244 -570 -839 C ATOM 3093 SD MET A 561 3.285 -24.350 -4.095 1.00115.30 S ANISOU 3093 SD MET A 561 19692 12948 11168 -2152 -400 -863 S ATOM 3094 CE MET A 561 3.699 -25.571 -2.853 1.00108.89 C ANISOU 3094 CE MET A 561 19007 11954 10413 -2179 -274 -874 C ATOM 3095 N PRO A 562 0.082 -20.873 -6.767 1.00 92.77 N ANISOU 3095 N PRO A 562 16283 10940 8024 -2122 -932 -770 N ATOM 3096 CA PRO A 562 -0.532 -20.766 -8.103 1.00 97.37 C ANISOU 3096 CA PRO A 562 16917 11673 8405 -2186 -1047 -782 C ATOM 3097 C PRO A 562 0.437 -20.354 -9.199 1.00 94.75 C ANISOU 3097 C PRO A 562 16797 11177 8027 -2043 -972 -769 C ATOM 3098 O PRO A 562 0.319 -20.839 -10.330 1.00 92.13 O ANISOU 3098 O PRO A 562 16646 10844 7516 -2153 -1011 -819 O ATOM 3099 CB PRO A 562 -1.629 -19.715 -7.890 1.00 91.26 C ANISOU 3099 CB PRO A 562 15843 11219 7611 -2073 -1180 -699 C ATOM 3100 CG PRO A 562 -2.021 -19.902 -6.480 1.00 93.95 C ANISOU 3100 CG PRO A 562 15994 11623 8081 -2109 -1166 -689 C ATOM 3101 CD PRO A 562 -0.724 -20.148 -5.764 1.00 92.58 C ANISOU 3101 CD PRO A 562 15970 11123 8082 -2044 -999 -709 C ATOM 3102 N ILE A 563 1.396 -19.477 -8.901 1.00106.85 N ANISOU 3102 N ILE A 563 18323 12577 9698 -1823 -863 -703 N ATOM 3103 CA ILE A 563 2.298 -19.000 -9.945 1.00103.39 C ANISOU 3103 CA ILE A 563 18062 12015 9207 -1699 -784 -673 C ATOM 3104 C ILE A 563 3.399 -20.018 -10.228 1.00103.58 C ANISOU 3104 C ILE A 563 18322 11810 9222 -1741 -631 -724 C ATOM 3105 O ILE A 563 3.804 -20.201 -11.382 1.00111.38 O ANISOU 3105 O ILE A 563 19514 12729 10075 -1728 -588 -739 O ATOM 3106 CB ILE A 563 2.871 -17.620 -9.570 1.00106.41 C ANISOU 3106 CB ILE A 563 18362 12358 9710 -1490 -729 -574 C ATOM 3107 CG1 ILE A 563 3.785 -17.101 -10.682 1.00111.32 C ANISOU 3107 CG1 ILE A 563 19164 12869 10262 -1393 -641 -531 C ATOM 3108 CG2 ILE A 563 3.602 -17.671 -8.235 1.00107.65 C ANISOU 3108 CG2 ILE A 563 18437 12401 10063 -1468 -628 -562 C ATOM 3109 CD1 ILE A 563 3.079 -16.903 -12.004 1.00113.43 C ANISOU 3109 CD1 ILE A 563 19520 13256 10323 -1388 -746 -531 C ATOM 3110 N PHE A 564 3.894 -20.703 -9.195 1.00107.71 N ANISOU 3110 N PHE A 564 18835 12219 9871 -1766 -538 -743 N ATOM 3111 CA PHE A 564 4.940 -21.698 -9.416 1.00111.19 C ANISOU 3111 CA PHE A 564 19508 12456 10285 -1748 -375 -774 C ATOM 3112 C PHE A 564 4.384 -22.945 -10.093 1.00109.32 C ANISOU 3112 C PHE A 564 19526 12156 9855 -1935 -405 -879 C ATOM 3113 O PHE A 564 5.070 -23.570 -10.910 1.00104.65 O ANISOU 3113 O PHE A 564 19212 11408 9142 -1895 -290 -908 O ATOM 3114 CB PHE A 564 5.616 -22.057 -8.093 1.00111.81 C ANISOU 3114 CB PHE A 564 19503 12448 10531 -1691 -270 -749 C ATOM 3115 CG PHE A 564 6.751 -21.144 -7.728 1.00112.26 C ANISOU 3115 CG PHE A 564 19433 12498 10723 -1515 -171 -651 C ATOM 3116 CD1 PHE A 564 6.509 -19.854 -7.286 1.00110.62 C ANISOU 3116 CD1 PHE A 564 19023 12396 10612 -1476 -249 -593 C ATOM 3117 CD2 PHE A 564 8.064 -21.576 -7.832 1.00114.57 C ANISOU 3117 CD2 PHE A 564 19819 12690 11021 -1392 4 -610 C ATOM 3118 CE1 PHE A 564 7.553 -19.013 -6.950 1.00107.98 C ANISOU 3118 CE1 PHE A 564 18603 12048 10376 -1374 -165 -509 C ATOM 3119 CE2 PHE A 564 9.112 -20.740 -7.498 1.00115.35 C ANISOU 3119 CE2 PHE A 564 19770 12832 11225 -1279 84 -512 C ATOM 3120 CZ PHE A 564 8.857 -19.457 -7.056 1.00109.79 C ANISOU 3120 CZ PHE A 564 18886 12216 10615 -1299 -7 -467 C ATOM 3121 N SER A 565 3.146 -23.321 -9.767 1.00100.38 N ANISOU 3121 N SER A 565 18318 11150 8673 -2150 -552 -934 N ATOM 3122 CA SER A 565 2.525 -24.458 -10.437 1.00100.88 C ANISOU 3122 CA SER A 565 18640 11168 8522 -2400 -604 -1039 C ATOM 3123 C SER A 565 2.175 -24.121 -11.882 1.00100.47 C ANISOU 3123 C SER A 565 18692 11212 8269 -2436 -698 -1059 C ATOM 3124 O SER A 565 2.298 -24.972 -12.770 1.00100.90 O ANISOU 3124 O SER A 565 19084 11128 8125 -2548 -664 -1139 O ATOM 3125 CB SER A 565 1.281 -24.904 -9.669 1.00 99.35 C ANISOU 3125 CB SER A 565 18297 11134 8319 -2664 -742 -1078 C ATOM 3126 OG SER A 565 0.188 -24.037 -9.921 1.00111.32 O ANISOU 3126 OG SER A 565 19527 12977 9792 -2713 -933 -1040 O ATOM 3127 N ALA A 566 1.740 -22.885 -12.136 1.00 95.75 N ANISOU 3127 N ALA A 566 17841 10839 7699 -2329 -811 -983 N ATOM 3128 CA ALA A 566 1.441 -22.476 -13.505 1.00 90.49 C ANISOU 3128 CA ALA A 566 17267 10278 6837 -2327 -900 -983 C ATOM 3129 C ALA A 566 2.707 -22.350 -14.340 1.00 94.58 C ANISOU 3129 C ALA A 566 18031 10581 7324 -2135 -728 -963 C ATOM 3130 O ALA A 566 2.668 -22.561 -15.558 1.00 93.10 O ANISOU 3130 O ALA A 566 18070 10377 6925 -2179 -750 -1003 O ATOM 3131 CB ALA A 566 0.670 -21.157 -13.508 1.00 85.05 C ANISOU 3131 CB ALA A 566 16264 9876 6175 -2210 -1047 -888 C ATOM 3132 N ASN A 567 3.834 -22.004 -13.712 1.00 91.97 N ANISOU 3132 N ASN A 567 17650 10110 7185 -1931 -558 -896 N ATOM 3133 CA ASN A 567 5.094 -21.953 -14.443 1.00 92.80 C ANISOU 3133 CA ASN A 567 17953 10050 7255 -1756 -375 -861 C ATOM 3134 C ASN A 567 5.588 -23.348 -14.803 1.00 94.23 C ANISOU 3134 C ASN A 567 18486 10018 7301 -1805 -242 -948 C ATOM 3135 O ASN A 567 6.277 -23.519 -15.815 1.00 94.46 O ANISOU 3135 O ASN A 567 18758 9942 7189 -1702 -125 -948 O ATOM 3136 CB ASN A 567 6.149 -21.207 -13.626 1.00 91.56 C ANISOU 3136 CB ASN A 567 17609 9858 7321 -1562 -241 -755 C ATOM 3137 CG ASN A 567 5.994 -19.702 -13.714 1.00 92.50 C ANISOU 3137 CG ASN A 567 17531 10108 7505 -1469 -313 -660 C ATOM 3138 OD1 ASN A 567 5.112 -19.198 -14.409 1.00100.35 O ANISOU 3138 OD1 ASN A 567 18519 11230 8379 -1499 -455 -661 O ATOM 3139 ND2 ASN A 567 6.857 -18.976 -13.014 1.00 94.37 N ANISOU 3139 ND2 ASN A 567 17626 10317 7912 -1356 -215 -573 N ATOM 3140 N ALA A 568 5.252 -24.352 -13.990 1.00108.30 N ANISOU 3140 N ALA A 568 20329 11717 9103 -1948 -245 -1018 N ATOM 3141 CA ALA A 568 5.587 -25.727 -14.343 1.00109.41 C ANISOU 3141 CA ALA A 568 20881 11617 9074 -2003 -121 -1109 C ATOM 3142 C ALA A 568 4.703 -26.230 -15.477 1.00114.94 C ANISOU 3142 C ALA A 568 21855 12326 9492 -2246 -251 -1219 C ATOM 3143 O ALA A 568 5.171 -26.953 -16.365 1.00117.12 O ANISOU 3143 O ALA A 568 22532 12407 9562 -2219 -135 -1277 O ATOM 3144 CB ALA A 568 5.462 -26.632 -13.118 1.00105.73 C ANISOU 3144 CB ALA A 568 20436 11039 8696 -2095 -82 -1144 C ATOM 3145 N TRP A 569 3.419 -25.862 -15.459 1.00 87.39 N ANISOU 3145 N TRP A 569 18155 9081 5969 -2480 -490 -1243 N ATOM 3146 CA TRP A 569 2.534 -26.200 -16.569 1.00 85.34 C ANISOU 3146 CA TRP A 569 18094 8907 5426 -2733 -649 -1333 C ATOM 3147 C TRP A 569 3.010 -25.549 -17.859 1.00 85.91 C ANISOU 3147 C TRP A 569 18275 8994 5371 -2553 -618 -1297 C ATOM 3148 O TRP A 569 2.914 -26.144 -18.939 1.00 88.33 O ANISOU 3148 O TRP A 569 18862 9218 5480 -2647 -618 -1356 O ATOM 3149 CB TRP A 569 1.105 -25.765 -16.248 1.00 85.71 C ANISOU 3149 CB TRP A 569 17792 9303 5470 -2969 -912 -1326 C ATOM 3150 CG TRP A 569 0.084 -26.281 -17.208 1.00 88.87 C ANISOU 3150 CG TRP A 569 18304 9848 5616 -3283 -1090 -1401 C ATOM 3151 CD1 TRP A 569 0.204 -27.359 -18.034 1.00 91.46 C ANISOU 3151 CD1 TRP A 569 18963 9965 5824 -3415 -1018 -1464 C ATOM 3152 CD2 TRP A 569 -1.218 -25.734 -17.449 1.00 90.15 C ANISOU 3152 CD2 TRP A 569 18161 10422 5669 -3466 -1355 -1379 C ATOM 3153 NE1 TRP A 569 -0.944 -27.521 -18.771 1.00 94.26 N ANISOU 3153 NE1 TRP A 569 19237 10570 6009 -3705 -1228 -1493 N ATOM 3154 CE2 TRP A 569 -1.832 -26.535 -18.431 1.00 93.54 C ANISOU 3154 CE2 TRP A 569 18734 10887 5919 -3735 -1440 -1438 C ATOM 3155 CE3 TRP A 569 -1.924 -24.646 -16.928 1.00 89.04 C ANISOU 3155 CE3 TRP A 569 17574 10637 5621 -3377 -1504 -1280 C ATOM 3156 CZ2 TRP A 569 -3.118 -26.283 -18.903 1.00 95.87 C ANISOU 3156 CZ2 TRP A 569 18772 11598 6055 -3962 -1696 -1425 C ATOM 3157 CZ3 TRP A 569 -3.201 -24.397 -17.398 1.00 91.36 C ANISOU 3157 CZ3 TRP A 569 17644 11344 5724 -3575 -1755 -1264 C ATOM 3158 CH2 TRP A 569 -3.785 -25.212 -18.375 1.00 94.74 C ANISOU 3158 CH2 TRP A 569 18230 11839 5929 -3879 -1859 -1341 C ATOM 3159 N ARG A 570 3.532 -24.325 -17.765 1.00114.62 N ANISOU 3159 N ARG A 570 21638 12729 9185 -2282 -576 -1170 N ATOM 3160 CA ARG A 570 4.039 -23.638 -18.946 1.00111.20 C ANISOU 3160 CA ARG A 570 21306 12305 8640 -2106 -528 -1118 C ATOM 3161 C ARG A 570 5.336 -24.267 -19.442 1.00116.78 C ANISOU 3161 C ARG A 570 22358 12736 9277 -1932 -267 -1129 C ATOM 3162 O ARG A 570 5.649 -24.182 -20.635 1.00126.85 O ANISOU 3162 O ARG A 570 23865 13973 10359 -1860 -218 -1132 O ATOM 3163 CB ARG A 570 4.231 -22.152 -18.626 1.00109.61 C ANISOU 3163 CB ARG A 570 20751 12260 8637 -1895 -544 -976 C ATOM 3164 CG ARG A 570 4.909 -21.332 -19.710 1.00114.06 C ANISOU 3164 CG ARG A 570 21410 12812 9117 -1697 -459 -896 C ATOM 3165 CD ARG A 570 5.737 -20.214 -19.098 1.00119.32 C ANISOU 3165 CD ARG A 570 21841 13477 10020 -1484 -344 -760 C ATOM 3166 NE ARG A 570 6.251 -19.297 -20.108 1.00126.85 N ANISOU 3166 NE ARG A 570 22869 14442 10887 -1331 -280 -669 N ATOM 3167 CZ ARG A 570 5.602 -18.228 -20.549 1.00120.47 C ANISOU 3167 CZ ARG A 570 21966 13786 10023 -1289 -416 -603 C ATOM 3168 NH1 ARG A 570 4.398 -17.916 -20.099 1.00119.12 N ANISOU 3168 NH1 ARG A 570 21595 13801 9866 -1362 -626 -611 N ATOM 3169 NH2 ARG A 570 6.174 -17.455 -21.467 1.00124.08 N ANISOU 3169 NH2 ARG A 570 22535 14218 10392 -1153 -330 -516 N ATOM 3170 N ALA A 571 6.093 -24.912 -18.553 1.00105.01 N ANISOU 3170 N ALA A 571 20908 11069 7922 -1841 -92 -1125 N ATOM 3171 CA ALA A 571 7.343 -25.549 -18.950 1.00103.60 C ANISOU 3171 CA ALA A 571 21034 10663 7666 -1623 176 -1114 C ATOM 3172 C ALA A 571 7.136 -26.928 -19.562 1.00105.32 C ANISOU 3172 C ALA A 571 21738 10653 7625 -1753 222 -1246 C ATOM 3173 O ALA A 571 7.991 -27.385 -20.328 1.00111.85 O ANISOU 3173 O ALA A 571 22838 11314 8345 -1557 422 -1228 O ATOM 3174 CB ALA A 571 8.284 -25.652 -17.748 1.00111.97 C ANISOU 3174 CB ALA A 571 21917 11662 8964 -1431 349 -1031 C ATOM 3175 N TYR A 572 6.031 -27.601 -19.244 1.00109.82 N ANISOU 3175 N TYR A 572 22302 11227 8199 -2060 53 -1326 N ATOM 3176 CA TYR A 572 5.735 -28.913 -19.806 1.00113.00 C ANISOU 3176 CA TYR A 572 23049 11415 8471 -2220 83 -1397 C ATOM 3177 C TYR A 572 4.767 -28.862 -20.978 1.00108.37 C ANISOU 3177 C TYR A 572 22499 10957 7718 -2462 -113 -1445 C ATOM 3178 O TYR A 572 4.880 -29.681 -21.896 1.00108.81 O ANISOU 3178 O TYR A 572 22903 10824 7614 -2497 -41 -1484 O ATOM 3179 CB TYR A 572 5.162 -29.838 -18.725 1.00111.73 C ANISOU 3179 CB TYR A 572 22905 11160 8386 -2445 47 -1444 C ATOM 3180 CG TYR A 572 6.205 -30.424 -17.799 1.00108.06 C ANISOU 3180 CG TYR A 572 22584 10462 8013 -2196 292 -1409 C ATOM 3181 CD1 TYR A 572 6.927 -31.555 -18.161 1.00116.40 C ANISOU 3181 CD1 TYR A 572 24070 11199 8958 -2043 516 -1407 C ATOM 3182 CD2 TYR A 572 6.467 -29.848 -16.564 1.00109.57 C ANISOU 3182 CD2 TYR A 572 22492 10759 8381 -2095 300 -1370 C ATOM 3183 CE1 TYR A 572 7.881 -32.094 -17.319 1.00118.89 C ANISOU 3183 CE1 TYR A 572 24512 11329 9332 -1771 744 -1360 C ATOM 3184 CE2 TYR A 572 7.419 -30.379 -15.715 1.00112.45 C ANISOU 3184 CE2 TYR A 572 22974 10942 8808 -1854 519 -1333 C ATOM 3185 CZ TYR A 572 8.122 -31.502 -16.097 1.00118.16 C ANISOU 3185 CZ TYR A 572 24109 11372 9414 -1680 741 -1324 C ATOM 3186 OH TYR A 572 9.071 -32.035 -15.255 1.00123.19 O ANISOU 3186 OH TYR A 572 24859 11857 10090 -1396 964 -1271 O ATOM 3187 N ASP A 573 3.815 -27.919 -20.970 1.00104.56 N ANISOU 3187 N ASP A 573 21674 10802 7251 -2614 -359 -1436 N ATOM 3188 CA ASP A 573 2.828 -27.762 -22.041 1.00100.27 C ANISOU 3188 CA ASP A 573 21106 10458 6535 -2831 -570 -1469 C ATOM 3189 C ASP A 573 2.631 -26.257 -22.240 1.00104.07 C ANISOU 3189 C ASP A 573 21268 11243 7030 -2692 -701 -1392 C ATOM 3190 O ASP A 573 1.659 -25.665 -21.767 1.00111.14 O ANISOU 3190 O ASP A 573 21841 12434 7955 -2829 -914 -1374 O ATOM 3191 CB ASP A 573 1.517 -28.475 -21.704 1.00105.61 C ANISOU 3191 CB ASP A 573 21700 11261 7167 -3247 -771 -1537 C ATOM 3192 CG ASP A 573 0.602 -28.623 -22.907 1.00119.49 C ANISOU 3192 CG ASP A 573 23508 13189 8702 -3495 -958 -1580 C ATOM 3193 OD1 ASP A 573 0.766 -27.867 -23.888 1.00109.52 O ANISOU 3193 OD1 ASP A 573 22236 12038 7340 -3337 -993 -1548 O ATOM 3194 OD2 ASP A 573 -0.284 -29.503 -22.871 1.00132.21 O ANISOU 3194 OD2 ASP A 573 25175 14832 10227 -3861 -1069 -1641 O ATOM 3195 N THR A 574 3.574 -25.638 -22.956 1.00106.13 N ANISOU 3195 N THR A 574 21638 11432 7255 -2404 -558 -1330 N ATOM 3196 CA THR A 574 3.551 -24.188 -23.124 1.00103.43 C ANISOU 3196 CA THR A 574 21057 11318 6922 -2239 -638 -1233 C ATOM 3197 C THR A 574 2.334 -23.727 -23.915 1.00107.43 C ANISOU 3197 C THR A 574 21424 12128 7267 -2398 -906 -1234 C ATOM 3198 O THR A 574 1.807 -22.638 -23.661 1.00113.75 O ANISOU 3198 O THR A 574 21951 13187 8081 -2338 -1053 -1157 O ATOM 3199 CB THR A 574 4.834 -23.718 -23.810 1.00105.16 C ANISOU 3199 CB THR A 574 21452 11391 7113 -1930 -409 -1159 C ATOM 3200 OG1 THR A 574 5.954 -24.437 -23.279 1.00105.14 O ANISOU 3200 OG1 THR A 574 21622 11128 7200 -1788 -149 -1165 O ATOM 3201 CG2 THR A 574 5.046 -22.228 -23.580 1.00109.49 C ANISOU 3201 CG2 THR A 574 21755 12105 7742 -1745 -429 -1032 C ATOM 3202 N ALA A 575 1.873 -24.535 -24.871 1.00115.43 N ANISOU 3202 N ALA A 575 22630 13123 8107 -2587 -971 -1311 N ATOM 3203 CA ALA A 575 0.745 -24.127 -25.703 1.00116.03 C ANISOU 3203 CA ALA A 575 22565 13524 7996 -2733 -1228 -1307 C ATOM 3204 C ALA A 575 -0.552 -24.097 -24.904 1.00119.97 C ANISOU 3204 C ALA A 575 22720 14348 8514 -2986 -1474 -1316 C ATOM 3205 O ALA A 575 -1.317 -23.130 -24.982 1.00118.02 O ANISOU 3205 O ALA A 575 22187 14456 8200 -2942 -1668 -1239 O ATOM 3206 CB ALA A 575 0.616 -25.063 -26.905 1.00111.99 C ANISOU 3206 CB ALA A 575 22366 12903 7281 -2897 -1230 -1393 C ATOM 3207 N SER A 576 -0.816 -25.151 -24.128 1.00144.49 N ANISOU 3207 N SER A 576 25855 17348 11698 -3238 -1460 -1395 N ATOM 3208 CA SER A 576 -2.085 -25.232 -23.410 1.00142.41 C ANISOU 3208 CA SER A 576 25259 17415 11435 -3518 -1686 -1402 C ATOM 3209 C SER A 576 -2.104 -24.302 -22.204 1.00142.91 C ANISOU 3209 C SER A 576 25006 17622 11672 -3347 -1706 -1318 C ATOM 3210 O SER A 576 -3.150 -23.732 -21.873 1.00146.02 O ANISOU 3210 O SER A 576 25049 18414 12019 -3424 -1920 -1264 O ATOM 3211 CB SER A 576 -2.352 -26.675 -22.982 1.00145.74 C ANISOU 3211 CB SER A 576 25847 17654 11873 -3861 -1647 -1502 C ATOM 3212 OG SER A 576 -2.563 -27.505 -24.111 1.00150.23 O ANISOU 3212 OG SER A 576 26703 18135 12241 -4069 -1670 -1573 O ATOM 3213 N ALA A 577 -0.962 -24.138 -21.535 1.00112.57 N ANISOU 3213 N ALA A 577 21279 13479 8014 -3107 -1484 -1298 N ATOM 3214 CA ALA A 577 -0.913 -23.274 -20.359 1.00103.23 C ANISOU 3214 CA ALA A 577 19831 12395 6998 -2950 -1489 -1222 C ATOM 3215 C ALA A 577 -1.101 -21.811 -20.739 1.00107.32 C ANISOU 3215 C ALA A 577 20079 13150 7548 -2665 -1563 -1078 C ATOM 3216 O ALA A 577 -1.853 -21.084 -20.080 1.00111.16 O ANISOU 3216 O ALA A 577 20185 13913 8139 -2600 -1683 -989 O ATOM 3217 CB ALA A 577 0.407 -23.474 -19.616 1.00 99.54 C ANISOU 3217 CB ALA A 577 19482 11561 6776 -2743 -1213 -1212 C ATOM 3218 N GLU A 578 -0.427 -21.363 -21.800 1.00110.54 N ANISOU 3218 N GLU A 578 20705 13446 7849 -2476 -1480 -1046 N ATOM 3219 CA GLU A 578 -0.571 -19.979 -22.237 1.00110.80 C ANISOU 3219 CA GLU A 578 20554 13664 7880 -2202 -1536 -904 C ATOM 3220 C GLU A 578 -1.946 -19.720 -22.841 1.00113.20 C ANISOU 3220 C GLU A 578 20681 14391 7939 -2315 -1817 -879 C ATOM 3221 O GLU A 578 -2.454 -18.597 -22.760 1.00108.45 O ANISOU 3221 O GLU A 578 19810 14032 7364 -2093 -1906 -745 O ATOM 3222 CB GLU A 578 0.525 -19.632 -23.243 1.00108.25 C ANISOU 3222 CB GLU A 578 20532 13111 7488 -1998 -1362 -873 C ATOM 3223 CG GLU A 578 1.862 -19.285 -22.611 1.00105.48 C ANISOU 3223 CG GLU A 578 20201 12472 7404 -1780 -1097 -814 C ATOM 3224 CD GLU A 578 2.890 -18.842 -23.633 1.00113.86 C ANISOU 3224 CD GLU A 578 21510 13370 8381 -1587 -927 -758 C ATOM 3225 OE1 GLU A 578 2.540 -18.747 -24.829 1.00112.73 O ANISOU 3225 OE1 GLU A 578 21536 13320 7975 -1598 -1015 -764 O ATOM 3226 OE2 GLU A 578 4.049 -18.590 -23.242 1.00118.69 O ANISOU 3226 OE2 GLU A 578 22136 13784 9175 -1435 -706 -701 O ATOM 3227 N ARG A 579 -2.563 -20.739 -23.441 1.00132.29 N ANISOU 3227 N ARG A 579 23256 16912 10095 -2656 -1960 -1000 N ATOM 3228 CA ARG A 579 -3.867 -20.546 -24.068 1.00137.81 C ANISOU 3228 CA ARG A 579 23725 18070 10565 -2780 -2233 -964 C ATOM 3229 C ARG A 579 -4.964 -20.350 -23.028 1.00143.53 C ANISOU 3229 C ARG A 579 24015 19171 11348 -2873 -2404 -908 C ATOM 3230 O ARG A 579 -5.811 -19.461 -23.172 1.00145.24 O ANISOU 3230 O ARG A 579 23911 19790 11484 -2709 -2565 -777 O ATOM 3231 CB ARG A 579 -4.191 -21.735 -24.971 1.00139.44 C ANISOU 3231 CB ARG A 579 24092 18260 10630 -3104 -2284 -1089 C ATOM 3232 CG ARG A 579 -5.605 -21.743 -25.522 1.00142.63 C ANISOU 3232 CG ARG A 579 24214 19178 10800 -3311 -2577 -1067 C ATOM 3233 CD ARG A 579 -5.893 -23.047 -26.248 1.00149.33 C ANISOU 3233 CD ARG A 579 25258 19953 11528 -3692 -2611 -1205 C ATOM 3234 NE ARG A 579 -6.048 -24.158 -25.317 1.00158.65 N ANISOU 3234 NE ARG A 579 26452 20986 12840 -4019 -2562 -1299 N ATOM 3235 CZ ARG A 579 -5.872 -25.433 -25.635 1.00156.73 C ANISOU 3235 CZ ARG A 579 26528 20456 12568 -4312 -2479 -1421 C ATOM 3236 NH1 ARG A 579 -5.532 -25.799 -26.860 1.00143.79 N ANISOU 3236 NH1 ARG A 579 25216 18645 10771 -4327 -2437 -1477 N ATOM 3237 NH2 ARG A 579 -6.039 -26.364 -24.700 1.00160.06 N ANISOU 3237 NH2 ARG A 579 26964 20743 13107 -4586 -2427 -1481 N ATOM 3238 N ARG A 580 -4.965 -21.167 -21.973 1.00146.95 N ANISOU 3238 N ARG A 580 24407 19486 11941 -3095 -2348 -987 N ATOM 3239 CA ARG A 580 -6.059 -21.133 -21.008 1.00140.92 C ANISOU 3239 CA ARG A 580 23207 19098 11239 -3219 -2496 -937 C ATOM 3240 C ARG A 580 -5.950 -19.960 -20.045 1.00138.25 C ANISOU 3240 C ARG A 580 22549 18800 11180 -2815 -2409 -788 C ATOM 3241 O ARG A 580 -6.976 -19.435 -19.597 1.00141.08 O ANISOU 3241 O ARG A 580 22504 19579 11521 -2751 -2553 -684 O ATOM 3242 CB ARG A 580 -6.111 -22.445 -20.224 1.00139.01 C ANISOU 3242 CB ARG A 580 23068 18699 11049 -3618 -2459 -1072 C ATOM 3243 CG ARG A 580 -6.406 -23.664 -21.084 1.00150.25 C ANISOU 3243 CG ARG A 580 24686 20064 12337 -3984 -2496 -1190 C ATOM 3244 CD ARG A 580 -6.865 -24.841 -20.237 1.00154.43 C ANISOU 3244 CD ARG A 580 25178 20553 12947 -4376 -2488 -1270 C ATOM 3245 NE ARG A 580 -6.667 -26.117 -20.916 1.00158.68 N ANISOU 3245 NE ARG A 580 26083 20792 13417 -4664 -2410 -1388 N ATOM 3246 CZ ARG A 580 -6.788 -27.302 -20.333 1.00161.14 C ANISOU 3246 CZ ARG A 580 26532 20907 13787 -4989 -2336 -1462 C ATOM 3247 NH1 ARG A 580 -7.101 -27.414 -19.052 1.00152.80 N ANISOU 3247 NH1 ARG A 580 25257 19928 12871 -5083 -2330 -1440 N ATOM 3248 NH2 ARG A 580 -6.593 -28.402 -21.054 1.00169.42 N ANISOU 3248 NH2 ARG A 580 27972 21663 14735 -5218 -2259 -1551 N ATOM 3249 N LEU A 581 -4.734 -19.535 -19.716 1.00122.14 N ANISOU 3249 N LEU A 581 20685 16346 9375 -2545 -2174 -772 N ATOM 3250 CA LEU A 581 -4.524 -18.475 -18.732 1.00121.15 C ANISOU 3250 CA LEU A 581 20329 16194 9510 -2206 -2076 -651 C ATOM 3251 C LEU A 581 -3.404 -17.566 -19.233 1.00121.69 C ANISOU 3251 C LEU A 581 20621 15962 9652 -1879 -1906 -586 C ATOM 3252 O LEU A 581 -2.226 -17.930 -19.192 1.00119.56 O ANISOU 3252 O LEU A 581 20611 15314 9504 -1884 -1713 -647 O ATOM 3253 CB LEU A 581 -4.245 -19.076 -17.351 1.00121.80 C ANISOU 3253 CB LEU A 581 20338 16099 9843 -2323 -1965 -706 C ATOM 3254 CG LEU A 581 -3.065 -19.995 -16.994 1.00114.31 C ANISOU 3254 CG LEU A 581 19695 14699 9039 -2439 -1761 -819 C ATOM 3255 CD1 LEU A 581 -1.859 -19.241 -16.449 1.00115.48 C ANISOU 3255 CD1 LEU A 581 19895 14543 9441 -2130 -1548 -756 C ATOM 3256 CD2 LEU A 581 -3.523 -21.079 -16.003 1.00102.17 C ANISOU 3256 CD2 LEU A 581 18077 13181 7561 -2747 -1784 -903 C ATOM 3257 N SER A 582 -3.785 -16.394 -19.744 1.00114.81 N ANISOU 3257 N SER A 582 19656 15282 8684 -1596 -1974 -454 N ATOM 3258 CA SER A 582 -2.806 -15.417 -20.205 1.00107.97 C ANISOU 3258 CA SER A 582 19003 14149 7870 -1303 -1815 -374 C ATOM 3259 C SER A 582 -3.371 -14.004 -20.173 1.00105.37 C ANISOU 3259 C SER A 582 18517 14015 7505 -950 -1869 -206 C ATOM 3260 O SER A 582 -2.612 -13.030 -20.151 1.00 99.39 O ANISOU 3260 O SER A 582 17907 13014 6843 -703 -1719 -124 O ATOM 3261 CB SER A 582 -2.326 -15.747 -21.617 1.00 97.80 C ANISOU 3261 CB SER A 582 18036 12755 6368 -1369 -1800 -422 C ATOM 3262 OG SER A 582 -1.397 -14.775 -22.054 1.00103.71 O ANISOU 3262 OG SER A 582 18977 13268 7159 -1104 -1640 -331 O ATOM 3263 N GLY A 583 -4.694 -13.881 -20.179 1.00114.03 N ANISOU 3263 N GLY A 583 19328 15554 8443 -925 -2074 -146 N ATOM 3264 CA GLY A 583 -5.337 -12.586 -20.086 1.00123.28 C ANISOU 3264 CA GLY A 583 20348 16939 9553 -540 -2120 26 C ATOM 3265 C GLY A 583 -5.670 -12.216 -18.656 1.00128.75 C ANISOU 3265 C GLY A 583 20794 17675 10449 -413 -2075 73 C ATOM 3266 O GLY A 583 -4.828 -11.676 -17.934 1.00125.28 O ANISOU 3266 O GLY A 583 20489 16885 10228 -283 -1893 85 O ATOM 3267 N THR A 584 -6.898 -12.512 -18.235 1.00136.35 N ANISOU 3267 N THR A 584 21393 19087 11326 -467 -2241 103 N ATOM 3268 CA THR A 584 -7.356 -12.214 -16.882 1.00134.56 C ANISOU 3268 CA THR A 584 20906 18960 11259 -340 -2205 154 C ATOM 3269 C THR A 584 -6.955 -13.265 -15.842 1.00131.36 C ANISOU 3269 C THR A 584 20455 18368 11086 -678 -2133 13 C ATOM 3270 O THR A 584 -6.677 -12.890 -14.696 1.00129.96 O ANISOU 3270 O THR A 584 20239 18021 11119 -550 -2011 31 O ATOM 3271 CB THR A 584 -8.876 -12.019 -16.873 1.00139.82 C ANISOU 3271 CB THR A 584 21164 20247 11714 -215 -2401 276 C ATOM 3272 OG1 THR A 584 -9.533 -13.237 -17.243 1.00138.16 O ANISOU 3272 OG1 THR A 584 20761 20371 11362 -646 -2583 187 O ATOM 3273 CG2 THR A 584 -9.271 -10.924 -17.854 1.00148.59 C ANISOU 3273 CG2 THR A 584 22330 21548 12581 185 -2462 438 C ATOM 3274 N PRO A 585 -6.913 -14.570 -16.162 1.00127.02 N ANISOU 3274 N PRO A 585 19941 17826 10494 -1100 -2199 -126 N ATOM 3275 CA PRO A 585 -6.531 -15.539 -15.115 1.00124.45 C ANISOU 3275 CA PRO A 585 19605 17300 10379 -1380 -2113 -244 C ATOM 3276 C PRO A 585 -5.120 -15.337 -14.585 1.00121.72 C ANISOU 3276 C PRO A 585 19527 16433 10288 -1287 -1885 -287 C ATOM 3277 O PRO A 585 -4.919 -15.315 -13.364 1.00124.17 O ANISOU 3277 O PRO A 585 19745 16628 10805 -1260 -1793 -292 O ATOM 3278 CB PRO A 585 -6.696 -16.893 -15.821 1.00128.18 C ANISOU 3278 CB PRO A 585 20178 17831 10694 -1823 -2216 -379 C ATOM 3279 CG PRO A 585 -7.673 -16.630 -16.900 1.00132.31 C ANISOU 3279 CG PRO A 585 20568 18791 10914 -1807 -2424 -309 C ATOM 3280 CD PRO A 585 -7.288 -15.279 -17.400 1.00132.16 C ANISOU 3280 CD PRO A 585 20656 18676 10883 -1357 -2357 -183 C ATOM 3281 N ILE A 586 -4.129 -15.192 -15.470 1.00105.70 N ANISOU 3281 N ILE A 586 17814 14111 8236 -1245 -1792 -311 N ATOM 3282 CA ILE A 586 -2.772 -14.909 -15.012 1.00100.61 C ANISOU 3282 CA ILE A 586 17380 13036 7810 -1154 -1580 -327 C ATOM 3283 C ILE A 586 -2.652 -13.516 -14.409 1.00101.54 C ANISOU 3283 C ILE A 586 17460 13090 8029 -821 -1506 -205 C ATOM 3284 O ILE A 586 -1.729 -13.265 -13.626 1.00 95.48 O ANISOU 3284 O ILE A 586 16778 12036 7464 -784 -1354 -212 O ATOM 3285 CB ILE A 586 -1.754 -15.099 -16.154 1.00103.23 C ANISOU 3285 CB ILE A 586 18038 13116 8067 -1192 -1488 -367 C ATOM 3286 CG1 ILE A 586 -0.352 -15.342 -15.585 1.00 98.84 C ANISOU 3286 CG1 ILE A 586 17644 12181 7730 -1220 -1276 -411 C ATOM 3287 CG2 ILE A 586 -1.746 -13.895 -17.079 1.00102.52 C ANISOU 3287 CG2 ILE A 586 18056 13055 7842 -922 -1496 -250 C ATOM 3288 CD1 ILE A 586 -0.220 -16.592 -14.752 1.00 91.88 C ANISOU 3288 CD1 ILE A 586 16722 11225 6963 -1458 -1243 -521 C ATOM 3289 N SER A 587 -3.562 -12.598 -14.743 1.00119.56 N ANISOU 3289 N SER A 587 19635 15635 10158 -572 -1607 -87 N ATOM 3290 CA SER A 587 -3.521 -11.277 -14.125 1.00119.05 C ANISOU 3290 CA SER A 587 19593 15480 10159 -239 -1526 28 C ATOM 3291 C SER A 587 -3.916 -11.339 -12.656 1.00122.39 C ANISOU 3291 C SER A 587 19794 15965 10742 -226 -1508 23 C ATOM 3292 O SER A 587 -3.408 -10.557 -11.843 1.00115.62 O ANISOU 3292 O SER A 587 19037 14873 10019 -67 -1384 58 O ATOM 3293 CB SER A 587 -4.431 -10.312 -14.884 1.00128.16 C ANISOU 3293 CB SER A 587 20717 16904 11075 76 -1628 168 C ATOM 3294 OG SER A 587 -4.075 -10.250 -16.254 1.00137.96 O ANISOU 3294 OG SER A 587 22174 18090 12153 66 -1646 177 O ATOM 3295 N PHE A 588 -4.814 -12.258 -12.298 1.00123.51 N ANISOU 3295 N PHE A 588 19653 16419 10858 -414 -1627 -22 N ATOM 3296 CA PHE A 588 -5.210 -12.452 -10.909 1.00118.94 C ANISOU 3296 CA PHE A 588 18854 15917 10422 -432 -1606 -30 C ATOM 3297 C PHE A 588 -4.274 -13.391 -10.164 1.00107.17 C ANISOU 3297 C PHE A 588 17446 14125 9147 -713 -1500 -157 C ATOM 3298 O PHE A 588 -4.101 -13.243 -8.948 1.00108.89 O ANISOU 3298 O PHE A 588 17606 14240 9528 -668 -1419 -158 O ATOM 3299 CB PHE A 588 -6.641 -12.994 -10.837 1.00125.83 C ANISOU 3299 CB PHE A 588 19360 17300 11149 -522 -1776 -1 C ATOM 3300 CG PHE A 588 -7.698 -11.933 -10.965 1.00137.11 C ANISOU 3300 CG PHE A 588 20602 19090 12404 -141 -1850 162 C ATOM 3301 CD1 PHE A 588 -7.900 -11.279 -12.171 1.00133.03 C ANISOU 3301 CD1 PHE A 588 20182 18686 11679 63 -1918 248 C ATOM 3302 CD2 PHE A 588 -8.483 -11.581 -9.878 1.00139.46 C ANISOU 3302 CD2 PHE A 588 20640 19619 12730 47 -1839 241 C ATOM 3303 CE1 PHE A 588 -8.869 -10.302 -12.291 1.00133.48 C ANISOU 3303 CE1 PHE A 588 20080 19084 11553 466 -1976 415 C ATOM 3304 CE2 PHE A 588 -9.453 -10.602 -9.993 1.00139.37 C ANISOU 3304 CE2 PHE A 588 20465 19953 12535 456 -1887 407 C ATOM 3305 CZ PHE A 588 -9.645 -9.963 -11.202 1.00138.38 C ANISOU 3305 CZ PHE A 588 20440 19940 12198 676 -1956 498 C ATOM 3306 N ILE A 589 -3.668 -14.353 -10.865 1.00 78.71 N ANISOU 3306 N ILE A 589 13996 10382 5527 -979 -1494 -257 N ATOM 3307 CA ILE A 589 -2.703 -15.247 -10.230 1.00 76.59 C ANISOU 3307 CA ILE A 589 13839 9822 5440 -1191 -1377 -361 C ATOM 3308 C ILE A 589 -1.500 -14.459 -9.732 1.00 74.54 C ANISOU 3308 C ILE A 589 13744 9227 5349 -1028 -1212 -332 C ATOM 3309 O ILE A 589 -1.021 -14.668 -8.610 1.00 77.23 O ANISOU 3309 O ILE A 589 14053 9426 5865 -1070 -1127 -361 O ATOM 3310 CB ILE A 589 -2.288 -16.362 -11.207 1.00 77.09 C ANISOU 3310 CB ILE A 589 14090 9791 5408 -1448 -1384 -461 C ATOM 3311 CG1 ILE A 589 -3.399 -17.405 -11.332 1.00 79.04 C ANISOU 3311 CG1 ILE A 589 14189 10327 5514 -1728 -1536 -520 C ATOM 3312 CG2 ILE A 589 -0.989 -17.019 -10.758 1.00 75.04 C ANISOU 3312 CG2 ILE A 589 14019 9177 5316 -1544 -1216 -534 C ATOM 3313 CD1 ILE A 589 -3.118 -18.471 -12.368 1.00 80.12 C ANISOU 3313 CD1 ILE A 589 14570 10367 5505 -1989 -1555 -625 C ATOM 3314 N LEU A 590 -0.992 -13.538 -10.556 1.00 83.88 N ANISOU 3314 N LEU A 590 15110 10292 6467 -859 -1169 -271 N ATOM 3315 CA LEU A 590 0.108 -12.685 -10.118 1.00 85.92 C ANISOU 3315 CA LEU A 590 15527 10261 6856 -745 -1023 -232 C ATOM 3316 C LEU A 590 -0.328 -11.741 -9.006 1.00 86.84 C ANISOU 3316 C LEU A 590 15559 10399 7039 -556 -1014 -168 C ATOM 3317 O LEU A 590 0.467 -11.432 -8.112 1.00 88.97 O ANISOU 3317 O LEU A 590 15891 10456 7456 -565 -909 -174 O ATOM 3318 CB LEU A 590 0.667 -11.888 -11.297 1.00 87.55 C ANISOU 3318 CB LEU A 590 15967 10347 6950 -633 -976 -171 C ATOM 3319 CG LEU A 590 1.799 -12.511 -12.120 1.00 86.02 C ANISOU 3319 CG LEU A 590 15949 9978 6756 -783 -881 -219 C ATOM 3320 CD1 LEU A 590 3.030 -12.745 -11.254 1.00 87.08 C ANISOU 3320 CD1 LEU A 590 16108 9893 7087 -880 -735 -247 C ATOM 3321 CD2 LEU A 590 1.360 -13.799 -12.793 1.00 83.29 C ANISOU 3321 CD2 LEU A 590 15575 9766 6305 -960 -964 -308 C ATOM 3322 N LEU A 591 -1.579 -11.275 -9.045 1.00 82.53 N ANISOU 3322 N LEU A 591 14871 10120 6365 -374 -1120 -101 N ATOM 3323 CA LEU A 591 -2.073 -10.390 -7.996 1.00 83.97 C ANISOU 3323 CA LEU A 591 14994 10330 6579 -147 -1096 -35 C ATOM 3324 C LEU A 591 -2.107 -11.100 -6.649 1.00 89.43 C ANISOU 3324 C LEU A 591 15511 11033 7436 -291 -1074 -101 C ATOM 3325 O LEU A 591 -1.837 -10.490 -5.608 1.00 90.08 O ANISOU 3325 O LEU A 591 15647 10967 7613 -189 -995 -85 O ATOM 3326 CB LEU A 591 -3.460 -9.866 -8.368 1.00 87.30 C ANISOU 3326 CB LEU A 591 15263 11103 6803 111 -1209 66 C ATOM 3327 CG LEU A 591 -4.256 -9.141 -7.282 1.00 85.11 C ANISOU 3327 CG LEU A 591 14872 10948 6519 382 -1192 142 C ATOM 3328 CD1 LEU A 591 -3.787 -7.701 -7.144 1.00 89.67 C ANISOU 3328 CD1 LEU A 591 15777 11230 7064 671 -1076 219 C ATOM 3329 CD2 LEU A 591 -5.745 -9.199 -7.583 1.00 83.74 C ANISOU 3329 CD2 LEU A 591 14394 11267 6157 547 -1327 229 C ATOM 3330 N LEU A 592 -2.432 -12.395 -6.651 1.00 93.52 N ANISOU 3330 N LEU A 592 15852 11710 7973 -538 -1141 -177 N ATOM 3331 CA LEU A 592 -2.415 -13.165 -5.412 1.00 86.13 C ANISOU 3331 CA LEU A 592 14777 10763 7184 -692 -1110 -237 C ATOM 3332 C LEU A 592 -1.000 -13.291 -4.861 1.00 82.91 C ANISOU 3332 C LEU A 592 14545 10007 6949 -789 -980 -290 C ATOM 3333 O LEU A 592 -0.798 -13.271 -3.642 1.00 93.35 O ANISOU 3333 O LEU A 592 15820 11253 8394 -789 -925 -302 O ATOM 3334 CB LEU A 592 -3.023 -14.547 -5.646 1.00 90.37 C ANISOU 3334 CB LEU A 592 15154 11508 7674 -969 -1200 -306 C ATOM 3335 CG LEU A 592 -3.684 -15.217 -4.442 1.00 91.27 C ANISOU 3335 CG LEU A 592 15044 11777 7857 -1085 -1214 -327 C ATOM 3336 CD1 LEU A 592 -4.965 -14.493 -4.061 1.00 92.39 C ANISOU 3336 CD1 LEU A 592 14936 12266 7901 -867 -1283 -226 C ATOM 3337 CD2 LEU A 592 -3.955 -16.686 -4.729 1.00 91.44 C ANISOU 3337 CD2 LEU A 592 15022 11886 7835 -1435 -1273 -413 C ATOM 3338 N SER A 593 -0.008 -13.419 -5.745 1.00 90.77 N ANISOU 3338 N SER A 593 15729 10818 7942 -867 -928 -312 N ATOM 3339 CA SER A 593 1.372 -13.555 -5.293 1.00 94.57 C ANISOU 3339 CA SER A 593 16333 11035 8565 -954 -805 -342 C ATOM 3340 C SER A 593 1.905 -12.254 -4.708 1.00 96.85 C ANISOU 3340 C SER A 593 16733 11164 8903 -813 -736 -282 C ATOM 3341 O SER A 593 2.823 -12.281 -3.880 1.00 98.66 O ANISOU 3341 O SER A 593 16989 11242 9254 -889 -657 -299 O ATOM 3342 CB SER A 593 2.259 -14.021 -6.448 1.00 98.77 C ANISOU 3342 CB SER A 593 17020 11455 9054 -1050 -754 -365 C ATOM 3343 OG SER A 593 2.690 -12.925 -7.238 1.00 98.72 O ANISOU 3343 OG SER A 593 17177 11357 8977 -929 -719 -297 O ATOM 3344 N TYR A 594 1.351 -11.114 -5.119 1.00129.07 N ANISOU 3344 N TYR A 594 20900 15272 12868 -611 -765 -210 N ATOM 3345 CA TYR A 594 1.793 -9.825 -4.606 1.00129.47 C ANISOU 3345 CA TYR A 594 21135 15131 12926 -487 -694 -156 C ATOM 3346 C TYR A 594 1.099 -9.427 -3.313 1.00130.23 C ANISOU 3346 C TYR A 594 21157 15273 13051 -358 -703 -147 C ATOM 3347 O TYR A 594 1.632 -8.594 -2.572 1.00130.19 O ANISOU 3347 O TYR A 594 21319 15071 13078 -327 -634 -133 O ATOM 3348 CB TYR A 594 1.579 -8.737 -5.662 1.00131.93 C ANISOU 3348 CB TYR A 594 21653 15400 13073 -302 -695 -74 C ATOM 3349 CG TYR A 594 2.616 -8.762 -6.761 1.00134.71 C ANISOU 3349 CG TYR A 594 22164 15616 13402 -427 -638 -68 C ATOM 3350 CD1 TYR A 594 3.968 -8.693 -6.460 1.00132.26 C ANISOU 3350 CD1 TYR A 594 21952 15106 13195 -605 -535 -81 C ATOM 3351 CD2 TYR A 594 2.245 -8.862 -8.095 1.00136.02 C ANISOU 3351 CD2 TYR A 594 22367 15886 13429 -369 -688 -41 C ATOM 3352 CE1 TYR A 594 4.924 -8.719 -7.454 1.00131.88 C ANISOU 3352 CE1 TYR A 594 22022 14971 13116 -711 -466 -61 C ATOM 3353 CE2 TYR A 594 3.196 -8.888 -9.099 1.00140.15 C ANISOU 3353 CE2 TYR A 594 23043 16289 13920 -471 -620 -31 C ATOM 3354 CZ TYR A 594 4.534 -8.816 -8.771 1.00142.83 C ANISOU 3354 CZ TYR A 594 23465 16436 14367 -636 -502 -38 C ATOM 3355 OH TYR A 594 5.489 -8.842 -9.760 1.00153.76 O ANISOU 3355 OH TYR A 594 24974 17737 15709 -729 -420 -13 O ATOM 3356 N THR A 595 -0.072 -9.999 -3.023 1.00 90.81 N ANISOU 3356 N THR A 595 15927 10545 8033 -299 -782 -153 N ATOM 3357 CA THR A 595 -0.730 -9.748 -1.747 1.00 89.47 C ANISOU 3357 CA THR A 595 15659 10447 7890 -177 -776 -142 C ATOM 3358 C THR A 595 0.058 -10.329 -0.579 1.00 90.41 C ANISOU 3358 C THR A 595 15745 10430 8176 -370 -721 -212 C ATOM 3359 O THR A 595 -0.077 -9.844 0.550 1.00 89.87 O ANISOU 3359 O THR A 595 15703 10309 8133 -278 -684 -205 O ATOM 3360 CB THR A 595 -2.150 -10.324 -1.773 1.00 86.98 C ANISOU 3360 CB THR A 595 15050 10503 7497 -107 -871 -119 C ATOM 3361 OG1 THR A 595 -2.833 -9.857 -2.943 1.00 83.92 O ANISOU 3361 OG1 THR A 595 14667 10284 6935 64 -937 -46 O ATOM 3362 CG2 THR A 595 -2.939 -9.891 -0.545 1.00 94.48 C ANISOU 3362 CG2 THR A 595 15900 11561 8437 88 -847 -81 C ATOM 3363 N SER A 596 0.897 -11.337 -0.832 1.00 96.14 N ANISOU 3363 N SER A 596 16434 11097 8996 -612 -708 -271 N ATOM 3364 CA SER A 596 1.681 -11.956 0.231 1.00100.71 C ANISOU 3364 CA SER A 596 16972 11575 9717 -770 -658 -323 C ATOM 3365 C SER A 596 2.634 -10.976 0.905 1.00 97.76 C ANISOU 3365 C SER A 596 16783 10981 9382 -762 -589 -307 C ATOM 3366 O SER A 596 3.048 -11.218 2.044 1.00101.87 O ANISOU 3366 O SER A 596 17262 11453 9990 -838 -562 -336 O ATOM 3367 CB SER A 596 2.474 -13.138 -0.326 1.00100.15 C ANISOU 3367 CB SER A 596 16874 11474 9706 -971 -637 -369 C ATOM 3368 OG SER A 596 3.634 -12.691 -1.007 1.00 96.34 O ANISOU 3368 OG SER A 596 16552 10832 9222 -1010 -577 -349 O ATOM 3369 N SER A 597 2.993 -9.882 0.232 1.00100.89 N ANISOU 3369 N SER A 597 17396 11241 9695 -692 -563 -262 N ATOM 3370 CA SER A 597 3.928 -8.927 0.815 1.00107.47 C ANISOU 3370 CA SER A 597 18441 11856 10536 -748 -502 -250 C ATOM 3371 C SER A 597 3.279 -8.064 1.890 1.00109.32 C ANISOU 3371 C SER A 597 18784 12033 10718 -586 -495 -241 C ATOM 3372 O SER A 597 3.975 -7.582 2.790 1.00110.64 O ANISOU 3372 O SER A 597 19084 12046 10907 -683 -459 -258 O ATOM 3373 CB SER A 597 4.523 -8.036 -0.276 1.00107.57 C ANISOU 3373 CB SER A 597 18692 11723 10457 -758 -464 -200 C ATOM 3374 OG SER A 597 3.505 -7.395 -1.025 1.00110.02 O ANISOU 3374 OG SER A 597 19102 12071 10630 -520 -491 -150 O ATOM 3375 N CYS A 598 1.963 -7.858 1.820 1.00100.46 N ANISOU 3375 N CYS A 598 17610 11052 9509 -336 -527 -210 N ATOM 3376 CA CYS A 598 1.284 -6.980 2.763 1.00 99.50 C ANISOU 3376 CA CYS A 598 17619 10881 9305 -115 -498 -188 C ATOM 3377 C CYS A 598 0.539 -7.721 3.863 1.00 97.56 C ANISOU 3377 C CYS A 598 17119 10827 9122 -76 -517 -215 C ATOM 3378 O CYS A 598 0.161 -7.094 4.857 1.00103.60 O ANISOU 3378 O CYS A 598 17995 11536 9833 79 -477 -208 O ATOM 3379 CB CYS A 598 0.293 -6.067 2.030 1.00 95.72 C ANISOU 3379 CB CYS A 598 17272 10448 8648 212 -497 -104 C ATOM 3380 SG CYS A 598 -1.149 -6.917 1.346 1.00 96.14 S ANISOU 3380 SG CYS A 598 16941 10930 8656 371 -589 -62 S ATOM 3381 N VAL A 599 0.320 -9.031 3.718 1.00102.43 N ANISOU 3381 N VAL A 599 17433 11654 9833 -217 -568 -246 N ATOM 3382 CA VAL A 599 -0.466 -9.752 4.714 1.00103.10 C ANISOU 3382 CA VAL A 599 17280 11932 9960 -197 -580 -261 C ATOM 3383 C VAL A 599 0.314 -9.930 6.010 1.00105.83 C ANISOU 3383 C VAL A 599 17675 12130 10404 -333 -538 -312 C ATOM 3384 O VAL A 599 -0.283 -10.040 7.088 1.00106.59 O ANISOU 3384 O VAL A 599 17687 12312 10500 -252 -519 -314 O ATOM 3385 CB VAL A 599 -0.939 -11.106 4.154 1.00 99.47 C ANISOU 3385 CB VAL A 599 16536 11713 9545 -348 -643 -279 C ATOM 3386 CG1 VAL A 599 -1.929 -10.895 3.020 1.00104.85 C ANISOU 3386 CG1 VAL A 599 17132 12611 10095 -202 -705 -221 C ATOM 3387 CG2 VAL A 599 0.248 -11.932 3.685 1.00102.83 C ANISOU 3387 CG2 VAL A 599 16992 12003 10075 -612 -639 -334 C ATOM 3388 N ASN A 600 1.650 -9.962 5.939 1.00106.48 N ANISOU 3388 N ASN A 600 17879 12021 10558 -537 -521 -346 N ATOM 3389 CA ASN A 600 2.433 -10.130 7.163 1.00104.57 C ANISOU 3389 CA ASN A 600 17662 11679 10389 -671 -497 -385 C ATOM 3390 C ASN A 600 2.318 -8.925 8.089 1.00107.16 C ANISOU 3390 C ASN A 600 18232 11859 10625 -543 -461 -382 C ATOM 3391 O ASN A 600 2.120 -9.125 9.301 1.00105.28 O ANISOU 3391 O ASN A 600 17951 11647 10405 -528 -447 -405 O ATOM 3392 CB ASN A 600 3.890 -10.451 6.814 1.00100.45 C ANISOU 3392 CB ASN A 600 17169 11055 9942 -908 -490 -400 C ATOM 3393 CG ASN A 600 4.042 -11.786 6.115 1.00106.36 C ANISOU 3393 CG ASN A 600 17715 11927 10770 -1011 -503 -410 C ATOM 3394 OD1 ASN A 600 3.219 -12.686 6.287 1.00107.54 O ANISOU 3394 OD1 ASN A 600 17696 12221 10945 -987 -521 -424 O ATOM 3395 ND2 ASN A 600 5.097 -11.922 5.320 1.00115.00 N ANISOU 3395 ND2 ASN A 600 18845 12962 11886 -1135 -484 -399 N ATOM 3396 N PRO A 601 2.435 -7.675 7.621 1.00100.60 N ANISOU 3396 N PRO A 601 17695 10850 9677 -449 -435 -355 N ATOM 3397 CA PRO A 601 2.204 -6.546 8.537 1.00 96.99 C ANISOU 3397 CA PRO A 601 17532 10222 9098 -304 -387 -358 C ATOM 3398 C PRO A 601 0.795 -6.496 9.101 1.00 98.01 C ANISOU 3398 C PRO A 601 17575 10510 9156 11 -361 -328 C ATOM 3399 O PRO A 601 0.612 -6.044 10.239 1.00 93.92 O ANISOU 3399 O PRO A 601 17203 9908 8573 104 -316 -347 O ATOM 3400 CB PRO A 601 2.502 -5.326 7.656 1.00 98.17 C ANISOU 3400 CB PRO A 601 18034 10148 9118 -254 -357 -323 C ATOM 3401 CG PRO A 601 3.498 -5.829 6.680 1.00 97.73 C ANISOU 3401 CG PRO A 601 17873 10103 9156 -515 -389 -324 C ATOM 3402 CD PRO A 601 3.009 -7.209 6.344 1.00 99.65 C ANISOU 3402 CD PRO A 601 17716 10625 9521 -513 -436 -328 C ATOM 3403 N ILE A 602 -0.209 -6.942 8.342 1.00101.43 N ANISOU 3403 N ILE A 602 17766 11192 9579 173 -385 -278 N ATOM 3404 CA ILE A 602 -1.582 -6.921 8.839 1.00105.87 C ANISOU 3404 CA ILE A 602 18183 11983 10059 471 -358 -228 C ATOM 3405 C ILE A 602 -1.739 -7.868 10.023 1.00105.46 C ANISOU 3405 C ILE A 602 17897 12068 10106 360 -356 -266 C ATOM 3406 O ILE A 602 -2.472 -7.576 10.976 1.00108.52 O ANISOU 3406 O ILE A 602 18291 12525 10415 569 -299 -245 O ATOM 3407 CB ILE A 602 -2.569 -7.262 7.707 1.00104.32 C ANISOU 3407 CB ILE A 602 17732 12084 9819 611 -406 -158 C ATOM 3408 CG1 ILE A 602 -2.366 -6.324 6.518 1.00 93.97 C ANISOU 3408 CG1 ILE A 602 16675 10627 8401 731 -406 -113 C ATOM 3409 CG2 ILE A 602 -4.006 -7.182 8.204 1.00108.98 C ANISOU 3409 CG2 ILE A 602 18129 12978 10300 929 -376 -82 C ATOM 3410 CD1 ILE A 602 -2.599 -4.868 6.844 1.00103.96 C ANISOU 3410 CD1 ILE A 602 18338 11677 9484 1054 -315 -66 C ATOM 3411 N ILE A 603 -1.050 -9.010 9.987 1.00 98.99 N ANISOU 3411 N ILE A 603 16889 11281 9441 51 -405 -316 N ATOM 3412 CA ILE A 603 -1.156 -9.970 11.081 1.00100.03 C ANISOU 3412 CA ILE A 603 16825 11523 9658 -61 -398 -346 C ATOM 3413 C ILE A 603 -0.467 -9.436 12.332 1.00103.94 C ANISOU 3413 C ILE A 603 17550 11804 10137 -88 -357 -388 C ATOM 3414 O ILE A 603 -0.957 -9.626 13.451 1.00107.85 O ANISOU 3414 O ILE A 603 17987 12376 10614 -12 -319 -390 O ATOM 3415 CB ILE A 603 -0.589 -11.334 10.647 1.00 93.80 C ANISOU 3415 CB ILE A 603 15831 10799 9011 -349 -448 -379 C ATOM 3416 CG1 ILE A 603 -1.467 -11.940 9.549 1.00 98.05 C ANISOU 3416 CG1 ILE A 603 16147 11574 9532 -342 -493 -345 C ATOM 3417 CG2 ILE A 603 -0.491 -12.283 11.832 1.00 89.16 C ANISOU 3417 CG2 ILE A 603 15114 10261 8500 -473 -429 -406 C ATOM 3418 CD1 ILE A 603 -0.816 -13.075 8.797 1.00 93.25 C ANISOU 3418 CD1 ILE A 603 15454 10956 9021 -602 -532 -382 C ATOM 3419 N TYR A 604 0.670 -8.752 12.165 1.00 98.53 N ANISOU 3419 N TYR A 604 17132 10863 9442 -216 -366 -421 N ATOM 3420 CA TYR A 604 1.353 -8.158 13.312 1.00 92.15 C ANISOU 3420 CA TYR A 604 16569 9857 8586 -283 -344 -465 C ATOM 3421 C TYR A 604 0.436 -7.201 14.063 1.00 99.66 C ANISOU 3421 C TYR A 604 17737 10754 9375 18 -271 -450 C ATOM 3422 O TYR A 604 0.453 -7.152 15.299 1.00108.09 O ANISOU 3422 O TYR A 604 18883 11781 10406 27 -242 -481 O ATOM 3423 CB TYR A 604 2.615 -7.422 12.861 1.00 90.53 C ANISOU 3423 CB TYR A 604 16628 9413 8356 -487 -368 -488 C ATOM 3424 CG TYR A 604 3.643 -8.281 12.164 1.00 87.51 C ANISOU 3424 CG TYR A 604 16048 9091 8110 -756 -420 -491 C ATOM 3425 CD1 TYR A 604 3.684 -9.655 12.359 1.00 88.38 C ANISOU 3425 CD1 TYR A 604 15842 9387 8351 -843 -442 -494 C ATOM 3426 CD2 TYR A 604 4.574 -7.712 11.306 1.00 93.67 C ANISOU 3426 CD2 TYR A 604 16983 9737 8869 -912 -432 -482 C ATOM 3427 CE1 TYR A 604 4.627 -10.438 11.718 1.00 90.34 C ANISOU 3427 CE1 TYR A 604 15946 9680 8699 -1036 -468 -488 C ATOM 3428 CE2 TYR A 604 5.517 -8.484 10.662 1.00 95.74 C ANISOU 3428 CE2 TYR A 604 17060 10078 9238 -1120 -461 -472 C ATOM 3429 CZ TYR A 604 5.540 -9.845 10.871 1.00 92.35 C ANISOU 3429 CZ TYR A 604 16329 9829 8931 -1161 -475 -475 C ATOM 3430 OH TYR A 604 6.481 -10.612 10.227 1.00 97.29 O ANISOU 3430 OH TYR A 604 16804 10523 9639 -1318 -483 -457 O ATOM 3431 N CYS A 605 -0.371 -6.431 13.331 1.00106.13 N ANISOU 3431 N CYS A 605 18667 11578 10078 294 -233 -394 N ATOM 3432 CA CYS A 605 -1.277 -5.485 13.972 1.00111.83 C ANISOU 3432 CA CYS A 605 19618 12254 10618 651 -140 -363 C ATOM 3433 C CYS A 605 -2.395 -6.212 14.707 1.00119.37 C ANISOU 3433 C CYS A 605 20246 13524 11586 827 -104 -324 C ATOM 3434 O CYS A 605 -2.685 -5.911 15.870 1.00129.22 O ANISOU 3434 O CYS A 605 21623 14730 12745 964 -33 -337 O ATOM 3435 CB CYS A 605 -1.854 -4.524 12.932 1.00115.00 C ANISOU 3435 CB CYS A 605 20209 12609 10877 943 -102 -291 C ATOM 3436 SG CYS A 605 -0.664 -3.330 12.276 1.00113.32 S ANISOU 3436 SG CYS A 605 20521 11960 10576 782 -101 -325 S ATOM 3437 N PHE A 606 -3.017 -7.194 14.052 1.00117.37 N ANISOU 3437 N PHE A 606 19578 13589 11429 798 -149 -279 N ATOM 3438 CA PHE A 606 -4.198 -7.869 14.585 1.00123.66 C ANISOU 3438 CA PHE A 606 20034 14735 12216 942 -114 -222 C ATOM 3439 C PHE A 606 -3.897 -8.688 15.837 1.00127.08 C ANISOU 3439 C PHE A 606 20367 15179 12738 750 -103 -273 C ATOM 3440 O PHE A 606 -4.804 -9.299 16.413 1.00131.19 O ANISOU 3440 O PHE A 606 20619 15976 13251 825 -63 -228 O ATOM 3441 CB PHE A 606 -4.816 -8.772 13.515 1.00123.38 C ANISOU 3441 CB PHE A 606 19606 15024 12250 860 -185 -172 C ATOM 3442 CG PHE A 606 -5.863 -8.097 12.674 1.00127.35 C ANISOU 3442 CG PHE A 606 20049 15736 12603 1197 -170 -70 C ATOM 3443 CD1 PHE A 606 -5.556 -6.989 11.904 1.00127.30 C ANISOU 3443 CD1 PHE A 606 20364 15507 12498 1369 -162 -54 C ATOM 3444 CD2 PHE A 606 -7.161 -8.579 12.657 1.00130.97 C ANISOU 3444 CD2 PHE A 606 20122 16638 13002 1339 -163 22 C ATOM 3445 CE1 PHE A 606 -6.524 -6.373 11.132 1.00129.52 C ANISOU 3445 CE1 PHE A 606 20597 15994 12622 1719 -145 55 C ATOM 3446 CE2 PHE A 606 -8.136 -7.969 11.886 1.00133.57 C ANISOU 3446 CE2 PHE A 606 20356 17220 13173 1672 -157 135 C ATOM 3447 CZ PHE A 606 -7.815 -6.862 11.122 1.00130.69 C ANISOU 3447 CZ PHE A 606 20328 16621 12709 1885 -147 153 C ATOM 3448 N MET A 607 -2.635 -8.716 16.269 1.00144.63 N ANISOU 3448 N MET A 607 22791 17131 15032 497 -137 -356 N ATOM 3449 CA MET A 607 -2.288 -9.464 17.471 1.00146.89 C ANISOU 3449 CA MET A 607 23003 17426 15384 334 -131 -397 C ATOM 3450 C MET A 607 -2.541 -8.651 18.736 1.00155.45 C ANISOU 3450 C MET A 607 24346 18400 16318 540 -45 -409 C ATOM 3451 O MET A 607 -2.986 -9.200 19.750 1.00161.50 O ANISOU 3451 O MET A 607 24978 19303 17081 570 1 -399 O ATOM 3452 CB MET A 607 -0.826 -9.913 17.410 1.00145.24 C ANISOU 3452 CB MET A 607 22852 17037 15295 -9 -210 -462 C ATOM 3453 CG MET A 607 -0.513 -10.875 16.277 1.00140.00 C ANISOU 3453 CG MET A 607 21950 16472 14771 -206 -276 -453 C ATOM 3454 SD MET A 607 -1.079 -12.556 16.590 1.00150.75 S ANISOU 3454 SD MET A 607 22942 18094 16241 -333 -273 -431 S ATOM 3455 CE MET A 607 -2.401 -12.702 15.388 1.00142.63 C ANISOU 3455 CE MET A 607 21681 17333 15179 -213 -281 -368 C ATOM 3456 N ASN A 608 -2.270 -7.348 18.700 1.00153.91 N ANISOU 3456 N ASN A 608 24556 17943 15981 679 -14 -431 N ATOM 3457 CA ASN A 608 -2.340 -6.498 19.888 1.00151.27 C ANISOU 3457 CA ASN A 608 24571 17429 15474 846 68 -462 C ATOM 3458 C ASN A 608 -3.369 -5.386 19.681 1.00159.38 C ANISOU 3458 C ASN A 608 25821 18440 16298 1294 182 -398 C ATOM 3459 O ASN A 608 -3.070 -4.340 19.100 1.00161.55 O ANISOU 3459 O ASN A 608 26462 18457 16461 1375 194 -407 O ATOM 3460 CB ASN A 608 -0.950 -5.935 20.235 1.00150.31 C ANISOU 3460 CB ASN A 608 24823 16965 15322 563 7 -556 C ATOM 3461 CG ASN A 608 -0.236 -5.347 19.031 1.00157.22 C ANISOU 3461 CG ASN A 608 25870 17657 16209 427 -49 -566 C ATOM 3462 OD1 ASN A 608 -0.770 -5.325 17.924 1.00160.32 O ANISOU 3462 OD1 ASN A 608 26132 18155 16629 567 -44 -506 O ATOM 3463 ND2 ASN A 608 0.982 -4.863 19.247 1.00156.77 N ANISOU 3463 ND2 ASN A 608 26102 17347 16118 136 -107 -635 N ATOM 3464 N LYS A 609 -4.589 -5.630 20.160 1.00164.47 N ANISOU 3464 N LYS A 609 26240 19372 16878 1595 276 -321 N ATOM 3465 CA LYS A 609 -5.652 -4.642 20.340 1.00170.09 C ANISOU 3465 CA LYS A 609 27147 20121 17359 2099 419 -244 C ATOM 3466 C LYS A 609 -6.080 -3.944 19.048 1.00175.95 C ANISOU 3466 C LYS A 609 27950 20881 18023 2347 427 -168 C ATOM 3467 O LYS A 609 -6.902 -3.019 19.097 1.00179.25 O ANISOU 3467 O LYS A 609 28578 21305 18222 2815 554 -90 O ATOM 3468 CB LYS A 609 -5.263 -3.607 21.412 1.00156.47 C ANISOU 3468 CB LYS A 609 25996 18021 15435 2218 508 -315 C ATOM 3469 CG LYS A 609 -4.605 -2.327 20.912 1.00163.14 C ANISOU 3469 CG LYS A 609 27419 18431 16134 2244 514 -363 C ATOM 3470 CD LYS A 609 -4.288 -1.395 22.071 1.00164.91 C ANISOU 3470 CD LYS A 609 28232 18292 16135 2324 603 -442 C ATOM 3471 CE LYS A 609 -3.609 -0.121 21.597 1.00161.30 C ANISOU 3471 CE LYS A 609 28408 17369 15509 2291 613 -494 C ATOM 3472 NZ LYS A 609 -3.180 0.728 22.742 1.00141.34 N ANISOU 3472 NZ LYS A 609 26496 14455 12750 2272 679 -592 N ATOM 3473 N ARG A 610 -5.580 -4.372 17.885 1.00169.64 N ANISOU 3473 N ARG A 610 26974 20103 17377 2081 304 -177 N ATOM 3474 CA ARG A 610 -6.096 -3.817 16.636 1.00167.82 C ANISOU 3474 CA ARG A 610 26748 19949 17067 2329 307 -90 C ATOM 3475 C ARG A 610 -7.551 -4.209 16.413 1.00175.57 C ANISOU 3475 C ARG A 610 27276 21438 17993 2655 350 47 C ATOM 3476 O ARG A 610 -8.283 -3.498 15.716 1.00177.86 O ANISOU 3476 O ARG A 610 27613 21841 18126 3039 400 152 O ATOM 3477 CB ARG A 610 -5.241 -4.266 15.453 1.00157.69 C ANISOU 3477 CB ARG A 610 25361 18599 15955 1960 169 -130 C ATOM 3478 CG ARG A 610 -5.433 -3.435 14.191 1.00152.73 C ANISOU 3478 CG ARG A 610 24909 17905 15218 2176 171 -63 C ATOM 3479 CD ARG A 610 -4.953 -2.006 14.384 1.00153.92 C ANISOU 3479 CD ARG A 610 25714 17594 15174 2339 259 -91 C ATOM 3480 NE ARG A 610 -3.532 -1.942 14.700 1.00150.42 N ANISOU 3480 NE ARG A 610 25551 16787 14816 1894 200 -216 N ATOM 3481 CZ ARG A 610 -2.920 -0.872 15.189 1.00145.49 C ANISOU 3481 CZ ARG A 610 25505 15741 14034 1881 260 -274 C ATOM 3482 NH1 ARG A 610 -3.580 0.248 15.435 1.00150.65 N ANISOU 3482 NH1 ARG A 610 26587 16223 14431 2316 397 -226 N ATOM 3483 NH2 ARG A 610 -1.616 -0.928 15.440 1.00134.94 N ANISOU 3483 NH2 ARG A 610 24333 14159 12779 1420 185 -377 N ATOM 3484 N PHE A 611 -7.985 -5.328 16.996 1.00186.12 N ANISOU 3484 N PHE A 611 28173 23103 19440 2503 334 59 N ATOM 3485 CA PHE A 611 -9.386 -5.727 16.938 1.00189.61 C ANISOU 3485 CA PHE A 611 28157 24076 19811 2764 380 195 C ATOM 3486 C PHE A 611 -10.300 -4.788 17.715 1.00193.33 C ANISOU 3486 C PHE A 611 28795 24629 20031 3317 558 290 C ATOM 3487 O PHE A 611 -11.524 -4.903 17.592 1.00192.33 O ANISOU 3487 O PHE A 611 28297 24983 19798 3619 614 434 O ATOM 3488 CB PHE A 611 -9.540 -7.161 17.453 1.00186.89 C ANISOU 3488 CB PHE A 611 27362 24014 19634 2408 330 178 C ATOM 3489 CG PHE A 611 -8.848 -7.416 18.764 1.00189.18 C ANISOU 3489 CG PHE A 611 27844 24051 19983 2223 369 79 C ATOM 3490 CD1 PHE A 611 -9.490 -7.168 19.965 1.00193.20 C ANISOU 3490 CD1 PHE A 611 28386 24663 20359 2495 509 122 C ATOM 3491 CD2 PHE A 611 -7.554 -7.915 18.792 1.00183.42 C ANISOU 3491 CD2 PHE A 611 27252 23010 19428 1795 268 -46 C ATOM 3492 CE1 PHE A 611 -8.854 -7.404 21.170 1.00187.03 C ANISOU 3492 CE1 PHE A 611 27791 23657 19616 2324 537 32 C ATOM 3493 CE2 PHE A 611 -6.913 -8.153 19.993 1.00184.60 C ANISOU 3493 CE2 PHE A 611 27560 22965 19614 1634 292 -126 C ATOM 3494 CZ PHE A 611 -7.564 -7.898 21.183 1.00184.34 C ANISOU 3494 CZ PHE A 611 27576 23017 19446 1890 420 -91 C ATOM 3495 N ARG A 612 -9.740 -3.872 18.511 1.00220.82 N ANISOU 3495 N ARG A 612 32830 27673 23400 3453 652 217 N ATOM 3496 CA ARG A 612 -10.555 -2.859 19.171 1.00226.12 C ANISOU 3496 CA ARG A 612 33767 28354 23795 4030 842 303 C ATOM 3497 C ARG A 612 -11.128 -1.863 18.171 1.00226.78 C ANISOU 3497 C ARG A 612 34011 28472 23684 4495 896 421 C ATOM 3498 O ARG A 612 -12.254 -1.384 18.349 1.00230.55 O ANISOU 3498 O ARG A 612 34409 29247 23944 5042 1039 569 O ATOM 3499 CB ARG A 612 -9.724 -2.133 20.231 1.00226.78 C ANISOU 3499 CB ARG A 612 34476 27906 23785 4004 917 177 C ATOM 3500 CG ARG A 612 -10.384 -0.897 20.822 1.00234.40 C ANISOU 3500 CG ARG A 612 35899 28737 24425 4614 1127 243 C ATOM 3501 CD ARG A 612 -9.522 -0.284 21.913 1.00234.53 C ANISOU 3501 CD ARG A 612 36547 28223 24341 4502 1183 98 C ATOM 3502 NE ARG A 612 -8.183 0.036 21.432 1.00232.85 N ANISOU 3502 NE ARG A 612 36724 27534 24215 4066 1053 -38 N ATOM 3503 CZ ARG A 612 -7.844 1.188 20.869 1.00226.02 C ANISOU 3503 CZ ARG A 612 36427 26271 23180 4213 1093 -51 C ATOM 3504 NH1 ARG A 612 -8.725 2.161 20.701 1.00220.64 N ANISOU 3504 NH1 ARG A 612 36039 25571 22225 4823 1264 62 N ATOM 3505 NH2 ARG A 612 -6.591 1.369 20.463 1.00219.79 N ANISOU 3505 NH2 ARG A 612 35925 25102 22484 3745 968 -169 N ATOM 3506 N LEU A 613 -10.376 -1.549 17.118 1.00188.34 N ANISOU 3506 N LEU A 613 29359 23324 18876 4306 792 372 N ATOM 3507 CA LEU A 613 -10.828 -0.582 16.128 1.00182.92 C ANISOU 3507 CA LEU A 613 28879 22625 17998 4736 840 483 C ATOM 3508 C LEU A 613 -12.064 -1.093 15.396 1.00177.66 C ANISOU 3508 C LEU A 613 27578 22622 17304 4978 810 657 C ATOM 3509 O LEU A 613 -12.254 -2.299 15.212 1.00176.79 O ANISOU 3509 O LEU A 613 26892 22896 17386 4622 688 656 O ATOM 3510 CB LEU A 613 -9.710 -0.289 15.125 1.00178.14 C ANISOU 3510 CB LEU A 613 28588 21612 17486 4404 724 393 C ATOM 3511 CG LEU A 613 -8.781 0.885 15.440 1.00173.26 C ANISOU 3511 CG LEU A 613 28765 20334 16731 4407 800 295 C ATOM 3512 CD1 LEU A 613 -7.818 0.531 16.563 1.00172.69 C ANISOU 3512 CD1 LEU A 613 28855 19980 16781 3965 769 132 C ATOM 3513 CD2 LEU A 613 -8.019 1.312 14.194 1.00163.05 C ANISOU 3513 CD2 LEU A 613 27724 18760 15468 4216 714 272 C ATOM 3514 N GLY A 614 -12.911 -0.158 14.979 1.00142.76 N ANISOU 3514 N GLY A 614 23285 18338 12620 5589 924 813 N ATOM 3515 CA GLY A 614 -14.131 -0.493 14.269 1.00133.81 C ANISOU 3515 CA GLY A 614 21557 17880 11406 5874 897 1003 C ATOM 3516 C GLY A 614 -14.818 0.713 13.659 1.00125.39 C ANISOU 3516 C GLY A 614 20756 16858 10030 6570 1016 1173 C ATOM 3517 O GLY A 614 -16.043 0.829 13.699 1.00122.29 O ANISOU 3517 O GLY A 614 20009 17015 9442 7074 1106 1366 O TER 3518 GLY A 614 ATOM 3519 N ASP C 1 -2.955 -10.031 -27.574 1.00153.75 N ANISOU 3519 N ASP C 1 25897 20265 12256 160 -1956 322 N ATOM 3520 CA ASP C 1 -2.004 -11.071 -27.946 1.00156.05 C ANISOU 3520 CA ASP C 1 26404 20296 12591 -140 -1842 165 C ATOM 3521 C ASP C 1 -0.709 -10.912 -27.153 1.00155.24 C ANISOU 3521 C ASP C 1 26414 19766 12806 -150 -1569 147 C ATOM 3522 O ASP C 1 0.384 -11.180 -27.654 1.00152.43 O ANISOU 3522 O ASP C 1 26314 19135 12467 -225 -1390 105 O ATOM 3523 CB ASP C 1 -1.724 -11.033 -29.452 1.00160.36 C ANISOU 3523 CB ASP C 1 27259 20821 12848 -109 -1841 183 C ATOM 3524 CG ASP C 1 -0.977 -12.262 -29.941 1.00159.98 C ANISOU 3524 CG ASP C 1 27435 20579 12770 -408 -1757 12 C ATOM 3525 OD1 ASP C 1 -1.537 -13.375 -29.855 1.00162.00 O ANISOU 3525 OD1 ASP C 1 27600 20997 12955 -693 -1904 -127 O ATOM 3526 OD2 ASP C 1 0.171 -12.112 -30.409 1.00159.68 O ANISOU 3526 OD2 ASP C 1 27681 20228 12764 -359 -1532 23 O HETATM 3527 N SMF C 2 -0.838 -10.465 -25.910 1.00123.09 N ANISOU 3527 N SMF C 2 22138 15664 8966 -68 -1537 185 N HETATM 3528 CA SMF C 2 0.303 -10.402 -25.015 1.00119.17 C ANISOU 3528 CA SMF C 2 21694 14820 8767 -122 -1312 159 C HETATM 3529 CB SMF C 2 -0.047 -9.746 -23.676 1.00117.87 C ANISOU 3529 CB SMF C 2 21317 14663 8806 2 -1311 217 C HETATM 3530 CG SMF C 2 1.097 -9.139 -22.947 1.00111.53 C ANISOU 3530 CG SMF C 2 20627 13512 8236 27 -1087 252 C HETATM 3531 CD1 SMF C 2 2.300 -8.871 -23.613 1.00113.10 C ANISOU 3531 CD1 SMF C 2 21098 13449 8426 2 -898 282 C HETATM 3532 CE1 SMF C 2 3.378 -8.304 -22.941 1.00109.79 C ANISOU 3532 CE1 SMF C 2 20758 12753 8203 -23 -701 323 C HETATM 3533 CD2 SMF C 2 0.999 -8.821 -21.588 1.00108.16 C ANISOU 3533 CD2 SMF C 2 20034 13037 8025 58 -1062 259 C HETATM 3534 CE2 SMF C 2 2.076 -8.254 -20.912 1.00102.40 C ANISOU 3534 CE2 SMF C 2 19416 12002 7488 40 -870 288 C HETATM 3535 CZ SMF C 2 3.277 -7.984 -21.581 1.00 99.74 C ANISOU 3535 CZ SMF C 2 19329 11430 7139 -15 -693 323 C HETATM 3536 CH SMF C 2 4.412 -7.395 -20.854 1.00 95.79 C ANISOU 3536 CH SMF C 2 18912 10660 6822 -86 -504 360 C HETATM 3537 S SMF C 2 5.548 -8.528 -20.069 1.00 96.23 S ANISOU 3537 S SMF C 2 18812 10629 7123 -358 -381 247 S HETATM 3538 O1 SMF C 2 4.923 -9.794 -20.117 1.00 91.32 O ANISOU 3538 O1 SMF C 2 18032 10182 6483 -435 -501 129 O HETATM 3539 O2 SMF C 2 6.776 -8.450 -20.766 1.00 99.23 O ANISOU 3539 O2 SMF C 2 19358 10870 7473 -438 -200 290 O HETATM 3540 O3 SMF C 2 5.624 -8.000 -18.749 1.00109.49 O ANISOU 3540 O3 SMF C 2 20395 12223 8984 -367 -359 261 O HETATM 3541 C SMF C 2 0.876 -11.836 -24.758 1.00116.88 C ANISOU 3541 C SMF C 2 21402 14419 8588 -434 -1254 -12 C HETATM 3542 O SMF C 2 2.120 -11.985 -24.581 1.00117.64 O ANISOU 3542 O SMF C 2 21635 14224 8837 -487 -1038 -35 O HETATM 3543 N NLE C 3 -0.020 -12.825 -24.767 1.00 91.51 N ANISOU 3543 N NLE C 3 18048 11447 5275 -626 -1439 -116 N HETATM 3544 CA NLE C 3 0.256 -14.262 -24.584 1.00 90.93 C ANISOU 3544 CA NLE C 3 18018 11290 5241 -925 -1417 -283 C HETATM 3545 C NLE C 3 1.500 -14.697 -23.799 1.00 89.61 C ANISOU 3545 C NLE C 3 17918 10793 5336 -985 -1182 -336 C HETATM 3546 O NLE C 3 2.637 -14.473 -24.213 1.00 87.83 O ANISOU 3546 O NLE C 3 17896 10336 5141 -906 -984 -303 O HETATM 3547 CB NLE C 3 0.169 -15.023 -25.911 1.00 93.27 C ANISOU 3547 CB NLE C 3 18564 11632 5241 -1069 -1483 -365 C HETATM 3548 CG NLE C 3 0.322 -16.529 -25.753 1.00 93.27 C ANISOU 3548 CG NLE C 3 18676 11531 5233 -1377 -1468 -541 C HETATM 3549 CD NLE C 3 -0.754 -17.285 -26.517 1.00 96.28 C ANISOU 3549 CD NLE C 3 19097 12182 5303 -1621 -1710 -632 C HETATM 3550 CE NLE C 3 -2.140 -16.963 -25.982 1.00 97.26 C ANISOU 3550 CE NLE C 3 18831 12721 5401 -1661 -1961 -578 C ATOM 3551 N GLY C 4 1.258 -15.378 -22.685 1.00112.42 N ANISOU 3551 N GLY C 4 20625 13696 8395 -1133 -1209 -412 N ATOM 3552 CA GLY C 4 2.318 -15.757 -21.776 1.00108.50 C ANISOU 3552 CA GLY C 4 20138 12939 8148 -1165 -1010 -446 C ATOM 3553 C GLY C 4 2.346 -14.771 -20.632 1.00106.00 C ANISOU 3553 C GLY C 4 19599 12616 8062 -1024 -981 -351 C ATOM 3554 O GLY C 4 1.355 -14.083 -20.383 1.00107.77 O ANISOU 3554 O GLY C 4 19647 13047 8255 -928 -1127 -288 O ATOM 3555 N TRP C 5 3.476 -14.692 -19.941 1.00 81.10 N ANISOU 3555 N TRP C 5 16459 9239 5118 -1000 -789 -335 N ATOM 3556 CA TRP C 5 3.611 -13.761 -18.833 1.00 79.56 C ANISOU 3556 CA TRP C 5 16100 9003 5126 -896 -751 -256 C ATOM 3557 C TRP C 5 5.064 -13.575 -18.425 1.00 78.13 C ANISOU 3557 C TRP C 5 15980 8595 5112 -890 -530 -220 C ATOM 3558 O TRP C 5 5.908 -14.442 -18.656 1.00 77.97 O ANISOU 3558 O TRP C 5 16052 8473 5099 -965 -405 -271 O ATOM 3559 CB TRP C 5 2.780 -14.232 -17.633 1.00 79.79 C ANISOU 3559 CB TRP C 5 15883 9157 5277 -982 -864 -313 C ATOM 3560 CG TRP C 5 3.112 -15.617 -17.174 1.00 80.64 C ANISOU 3560 CG TRP C 5 15993 9188 5460 -1177 -815 -431 C ATOM 3561 CD1 TRP C 5 4.114 -15.982 -16.324 1.00 82.42 C ANISOU 3561 CD1 TRP C 5 16204 9234 5876 -1204 -658 -447 C ATOM 3562 CD2 TRP C 5 2.435 -16.826 -17.539 1.00 79.23 C ANISOU 3562 CD2 TRP C 5 15858 9104 5140 -1372 -920 -543 C ATOM 3563 NE1 TRP C 5 4.106 -17.343 -16.140 1.00 77.93 N ANISOU 3563 NE1 TRP C 5 15688 8625 5297 -1363 -647 -556 N ATOM 3564 CE2 TRP C 5 3.085 -17.885 -16.875 1.00 78.20 C ANISOU 3564 CE2 TRP C 5 15781 8805 5127 -1488 -803 -623 C ATOM 3565 CE3 TRP C 5 1.344 -17.116 -18.365 1.00 81.42 C ANISOU 3565 CE3 TRP C 5 16148 9602 5185 -1473 -1106 -580 C ATOM 3566 CZ2 TRP C 5 2.679 -19.211 -17.009 1.00 83.57 C ANISOU 3566 CZ2 TRP C 5 16576 9479 5696 -1705 -852 -743 C ATOM 3567 CZ3 TRP C 5 0.945 -18.433 -18.498 1.00 83.86 C ANISOU 3567 CZ3 TRP C 5 16545 9933 5384 -1732 -1170 -705 C ATOM 3568 CH2 TRP C 5 1.610 -19.464 -17.823 1.00 85.89 C ANISOU 3568 CH2 TRP C 5 16904 9969 5760 -1848 -1036 -789 C HETATM 3569 N NLE C 6 5.340 -12.419 -17.832 1.00 88.20 N ANISOU 3569 N NLE C 6 17212 9803 6498 -795 -482 -125 N HETATM 3570 CA NLE C 6 6.641 -12.122 -17.254 1.00 89.34 C ANISOU 3570 CA NLE C 6 17360 9784 6803 -831 -301 -80 C HETATM 3571 C NLE C 6 6.954 -13.135 -16.158 1.00 94.56 C ANISOU 3571 C NLE C 6 17857 10434 7638 -941 -268 -161 C HETATM 3572 O NLE C 6 6.057 -13.545 -15.425 1.00 96.73 O ANISOU 3572 O NLE C 6 17991 10797 7966 -972 -392 -222 O HETATM 3573 CB NLE C 6 6.654 -10.694 -16.700 1.00 91.04 C ANISOU 3573 CB NLE C 6 17586 9928 7077 -750 -290 20 C HETATM 3574 CG NLE C 6 7.987 -10.226 -16.147 1.00 90.90 C ANISOU 3574 CG NLE C 6 17579 9767 7192 -838 -120 79 C HETATM 3575 CD NLE C 6 7.884 -8.800 -15.633 1.00 91.09 C ANISOU 3575 CD NLE C 6 17691 9686 7233 -788 -121 165 C HETATM 3576 CE NLE C 6 9.203 -8.329 -15.051 1.00 93.76 C ANISOU 3576 CE NLE C 6 18037 9906 7682 -943 30 220 C HETATM 3577 C OEM C 7 8.351 -13.961 -13.578 1.00115.55 C ANISOU 3577 C OEM C 7 20203 13001 10698 -1079 -111 -194 C HETATM 3578 N OEM C 7 8.217 -13.546 -16.063 1.00102.55 N ANISOU 3578 N OEM C 7 18882 11359 8722 -987 -97 -148 N HETATM 3579 O OEM C 7 9.058 -12.975 -13.214 1.00120.54 O ANISOU 3579 O OEM C 7 20819 13582 11399 -1085 -39 -109 O HETATM 3580 CA OEM C 7 8.655 -14.510 -15.035 1.00106.55 C ANISOU 3580 CA OEM C 7 19253 11852 9379 -1054 -44 -205 C HETATM 3581 CB OEM C 7 8.310 -15.958 -15.435 1.00105.35 C ANISOU 3581 CB OEM C 7 19186 11709 9135 -1094 -63 -314 C HETATM 3582 CG OEM C 7 9.075 -17.055 -14.698 1.00109.27 C ANISOU 3582 CG OEM C 7 19639 12147 9731 -1114 58 -351 C HETATM 3583 CAA OEM C 7 9.138 -13.481 -17.162 1.00 97.25 C ANISOU 3583 CAA OEM C 7 18373 10640 7937 -960 48 -94 C HETATM 3584 OD1 OEM C 7 9.603 -18.018 -15.343 1.00105.84 O ANISOU 3584 OD1 OEM C 7 19371 11652 9190 -1083 173 -385 O HETATM 3585 OD2 OEM C 7 9.171 -16.988 -13.432 1.00116.78 O ANISOU 3585 OD2 OEM C 7 20408 13108 10855 -1140 48 -343 O HETATM 3586 C1 MEA C 8 6.280 -15.399 -12.996 1.00120.42 C ANISOU 3586 C1 MEA C 8 20695 13772 11287 -1160 -361 -361 C HETATM 3587 N MEA C 8 7.398 -14.502 -12.802 1.00121.90 N ANISOU 3587 N MEA C 8 20891 13868 11558 -1111 -232 -269 N HETATM 3588 CA MEA C 8 7.125 -13.946 -11.474 1.00117.98 C ANISOU 3588 CA MEA C 8 20239 13379 11208 -1113 -281 -254 C HETATM 3589 C MEA C 8 6.618 -12.517 -11.644 1.00117.62 C ANISOU 3589 C MEA C 8 20252 13330 11108 -1016 -340 -181 C HETATM 3590 O MEA C 8 5.981 -12.131 -12.628 1.00113.83 O ANISOU 3590 O MEA C 8 19875 12901 10476 -934 -406 -158 O HETATM 3591 CB MEA C 8 8.330 -13.946 -10.511 1.00116.62 C ANISOU 3591 CB MEA C 8 19979 13140 11191 -1164 -157 -222 C HETATM 3592 CG MEA C 8 8.925 -15.291 -10.297 1.00116.59 C ANISOU 3592 CG MEA C 8 19937 13134 11227 -1200 -74 -270 C HETATM 3593 CD1 MEA C 8 10.314 -15.429 -10.186 1.00115.27 C ANISOU 3593 CD1 MEA C 8 19739 12952 11107 -1202 83 -210 C HETATM 3594 CE1 MEA C 8 10.883 -16.684 -9.982 1.00114.12 C ANISOU 3594 CE1 MEA C 8 19577 12806 10976 -1175 178 -237 C HETATM 3595 CZ MEA C 8 10.068 -17.813 -9.890 1.00114.90 C ANISOU 3595 CZ MEA C 8 19741 12874 11042 -1186 119 -338 C HETATM 3596 CE2 MEA C 8 8.683 -17.682 -10.000 1.00114.40 C ANISOU 3596 CE2 MEA C 8 19698 12835 10935 -1245 -47 -405 C HETATM 3597 CD2 MEA C 8 8.112 -16.427 -10.201 1.00114.11 C ANISOU 3597 CD2 MEA C 8 19628 12844 10885 -1233 -144 -365 C HETATM 3598 N NH2 C 9 6.916 -11.703 -10.638 1.00174.01 N ANISOU 3598 N NH2 C 9 27353 20404 18360 -1015 -314 -139 N TER 3599 NH2 C 9 CONECT 620 1267 CONECT 1267 620 CONECT 3521 3527 CONECT 3527 3521 3528 CONECT 3528 3527 3529 3541 CONECT 3529 3528 3530 CONECT 3530 3529 3531 3533 CONECT 3531 3530 3532 CONECT 3532 3531 3535 CONECT 3533 3530 3534 CONECT 3534 3533 3535 CONECT 3535 3532 3534 3536 CONECT 3536 3535 3537 CONECT 3537 3536 3538 3539 3540 CONECT 3538 3537 CONECT 3539 3537 CONECT 3540 3537 CONECT 3541 3528 3542 3543 CONECT 3542 3541 CONECT 3543 3541 3544 CONECT 3544 3543 3545 3547 CONECT 3545 3544 3546 3551 CONECT 3546 3545 CONECT 3547 3544 3548 CONECT 3548 3547 3549 CONECT 3549 3548 3550 CONECT 3550 3549 CONECT 3551 3545 CONECT 3557 3569 CONECT 3569 3557 3570 CONECT 3570 3569 3571 3573 CONECT 3571 3570 3572 3578 CONECT 3572 3571 CONECT 3573 3570 3574 CONECT 3574 3573 3575 CONECT 3575 3574 3576 CONECT 3576 3575 CONECT 3577 3579 3580 3587 CONECT 3578 3571 3580 3583 CONECT 3579 3577 CONECT 3580 3577 3578 3581 CONECT 3581 3580 3582 CONECT 3582 3581 3584 3585 CONECT 3583 3578 CONECT 3584 3582 CONECT 3585 3582 CONECT 3586 3587 CONECT 3587 3577 3586 3588 CONECT 3588 3587 3589 3591 CONECT 3589 3588 3590 3598 CONECT 3590 3589 CONECT 3591 3588 3592 CONECT 3592 3591 3593 3597 CONECT 3593 3592 3594 CONECT 3594 3593 3595 CONECT 3595 3594 3596 CONECT 3596 3595 3597 CONECT 3597 3592 3596 CONECT 3598 3589 MASTER 336 0 6 23 5 0 0 6 3597 2 59 43 END