Browse entries in the PDBbind-CN Database
HEADER TRANSFERASE/HYDROLASE 26-OCT-15 5EG3 TITLE CRYSTAL STRUCTURE OF THE ACTIVATED FGF RECEPTOR 2 (FGFR2) KINASE TITLE 2 DOMAIN IN COMPLEX WITH THE CSH2 DOMAIN OF PHOSPHOLIPASE C GAMMA TITLE 3 (PLCGAMMA) COMPND MOL_ID: 1; COMPND 2 MOLECULE: FIBROBLAST GROWTH FACTOR RECEPTOR 2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: UNP RESIDUES 458-778; COMPND 5 SYNONYM: FGFR-2,K-SAM,KGFR,KERATINOCYTE GROWTH FACTOR RECEPTOR; COMPND 6 EC: 2.7.10.1; COMPND 7 ENGINEERED: YES; COMPND 8 MUTATION: YES; COMPND 9 OTHER_DETAILS: TYR326 IS PHOSPHORYLATED; COMPND 10 MOL_ID: 2; COMPND 11 MOLECULE: 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE COMPND 12 GAMMA-1; COMPND 13 CHAIN: B; COMPND 14 FRAGMENT: UNP RESIDUES 661-773; COMPND 15 SYNONYM: PHOSPHOINOSITIDE PHOSPHOLIPASE C-GAMMA-1,PHOSPHOLIPASE C- COMPND 16 GAMMA-1,PLC-GAMMA-1; COMPND 17 EC: 3.1.4.11; COMPND 18 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: FGFR2, BEK, KGFR, KSAM; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 10 ORGANISM_COMMON: RAT; SOURCE 11 ORGANISM_TAXID: 10116; SOURCE 12 GENE: PLCG1; SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS SIGNALING COMPLEX, TYROSINE KINASE DOMAIN, SH2 DOMAIN, RECRUITMENT, KEYWDS 2 PHOSPHORYLATION, TRANSFERASE-HYDROLASE COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR Z.HUANG,X.LI,M.MOHAMMADI REVDAT 4 11-DEC-19 5EG3 1 REMARK REVDAT 3 13-SEP-17 5EG3 1 REMARK REVDAT 2 28-DEC-16 5EG3 1 TITLE REVDAT 1 03-FEB-16 5EG3 0 JRNL AUTH Z.HUANG,W.M.MARSIGLIA,U.BASU ROY,N.RAHIMI,D.ILGHARI,H.WANG, JRNL AUTH 2 H.CHEN,W.GAI,S.BLAIS,T.A.NEUBERT,A.MANSUKHANI,N.J.TRAASETH, JRNL AUTH 3 X.LI,M.MOHAMMADI JRNL TITL TWO FGF RECEPTOR KINASE MOLECULES ACT IN CONCERT TO RECRUIT JRNL TITL 2 AND TRANSPHOSPHORYLATE PHOSPHOLIPASE C GAMMA. JRNL REF MOL.CELL V. 61 98 2016 JRNL REFN ISSN 1097-2765 JRNL PMID 26687682 JRNL DOI 10.1016/J.MOLCEL.2015.11.010 REMARK 2 REMARK 2 RESOLUTION. 2.61 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.8.4_1496 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.61 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.86 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7 REMARK 3 NUMBER OF REFLECTIONS : 15973 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.191 REMARK 3 R VALUE (WORKING SET) : 0.185 REMARK 3 FREE R VALUE : 0.237 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1597 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 37.8632 - 5.7883 1.00 1383 153 0.1532 0.1806 REMARK 3 2 5.7883 - 4.5969 1.00 1365 151 0.1572 0.1949 REMARK 3 3 4.5969 - 4.0166 1.00 1326 148 0.1423 0.1724 REMARK 3 4 4.0166 - 3.6497 1.00 1338 148 0.1628 0.2296 REMARK 3 5 3.6497 - 3.3883 0.99 1327 148 0.1900 0.2501 REMARK 3 6 3.3883 - 3.1886 0.98 1290 143 0.2056 0.2754 REMARK 3 7 3.1886 - 3.0290 0.97 1302 146 0.2266 0.2724 REMARK 3 8 3.0290 - 2.8972 0.96 1291 143 0.2380 0.3380 REMARK 3 9 2.8972 - 2.7857 0.96 1256 139 0.2452 0.3098 REMARK 3 10 2.7857 - 2.6896 0.97 1298 145 0.2419 0.3084 REMARK 3 11 2.6896 - 2.6055 0.90 1200 133 0.2385 0.3098 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.320 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.400 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.009 3430 REMARK 3 ANGLE : 1.210 4640 REMARK 3 CHIRALITY : 0.044 499 REMARK 3 PLANARITY : 0.005 596 REMARK 3 DIHEDRAL : 13.704 1312 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): 21.3631 9.0993 28.3348 REMARK 3 T TENSOR REMARK 3 T11: 0.1988 T22: 0.1981 REMARK 3 T33: 0.1730 T12: 0.0079 REMARK 3 T13: 0.0060 T23: -0.0287 REMARK 3 L TENSOR REMARK 3 L11: 0.6906 L22: 1.1122 REMARK 3 L33: 0.3941 L12: -0.3413 REMARK 3 L13: 0.1472 L23: -0.3901 REMARK 3 S TENSOR REMARK 3 S11: -0.0904 S12: -0.1781 S13: -0.0085 REMARK 3 S21: 0.1741 S22: 0.0963 S23: 0.0416 REMARK 3 S31: -0.0533 S32: -0.0516 S33: -0.0070 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 5EG3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-OCT-15. REMARK 100 THE DEPOSITION ID IS D_1000214850. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-JUL-12 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS REMARK 200 BEAMLINE : X4C REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97907 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15981 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 REMARK 200 RESOLUTION RANGE LOW (A) : 37.859 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2 REMARK 200 DATA REDUNDANCY : 6.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.09300 REMARK 200
FOR THE DATA SET : 27.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64 REMARK 200 COMPLETENESS FOR SHELL (%) : 93.5 REMARK 200 DATA REDUNDANCY IN SHELL : 4.90 REMARK 200 R MERGE FOR SHELL (I) : 0.25600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200
FOR SHELL : 5.900 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 2PVY, 2PLE REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.46 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 25 MM HEPES (PH 7.5), PEG20000 (12% REMARK 280 18%) AND 2% (W/V) BENZAMIDINE HYDROCHLORIDE, VAPOR DIFFUSION, REMARK 280 HANGING DROP, TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 39.80450 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.61550 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 39.80450 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 26.61550 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2130 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21490 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 MET A 445 REMARK 465 GLY A 446 REMARK 465 SER A 447 REMARK 465 SER A 448 REMARK 465 HIS A 449 REMARK 465 HIS A 450 REMARK 465 HIS A 451 REMARK 465 HIS A 452 REMARK 465 HIS A 453 REMARK 465 HIS A 454 REMARK 465 SER A 455 REMARK 465 GLN A 456 REMARK 465 ASP A 457 REMARK 465 PRO A 458 REMARK 465 MET A 459 REMARK 465 LEU A 460 REMARK 465 ALA A 461 REMARK 465 GLY A 462 REMARK 465 VAL A 463 REMARK 465 SER A 464 REMARK 465 GLU A 465 REMARK 465 MET A 584 REMARK 465 GLU A 585 REMARK 465 LEU A 586 REMARK 465 SER A 587 REMARK 465 PRO A 588 REMARK 465 ASP A 589 REMARK 465 ILE A 590 REMARK 465 PRO A 775 REMARK 465 LEU A 776 REMARK 465 GLU A 777 REMARK 465 GLN A 778 REMARK 465 ALA B 773 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 PHE A 492 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASP A 506 CG OD1 OD2 REMARK 470 LYS A 509 CG CD CE NZ REMARK 470 GLU A 510 CG CD OE1 OE2 REMARK 470 LYS B 749 CG CD CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O3G ACP A 801 O HOH A 901 2.12 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASP A 557 70.34 47.71 REMARK 500 VAL A 593 78.07 -117.24 REMARK 500 ASP A 626 43.63 -156.11 REMARK 500 ASP A 644 87.44 47.53 REMARK 500 ILE A 654 -35.68 -146.88 REMARK 500 ASN A 662 -135.99 -71.41 REMARK 500 ARG B 753 -51.45 -129.48 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG A 802 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ARG A 630 O REMARK 620 2 ASN A 631 OD1 73.1 REMARK 620 3 ACP A 801 O1A 103.7 71.9 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG A 803 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASN A 631 OD1 REMARK 620 2 ASP A 644 OD2 81.8 REMARK 620 3 ACP A 801 O1B 150.1 94.9 REMARK 620 4 ACP A 801 O1A 77.1 77.8 73.2 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ACP A 801 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 802 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 803 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2PVY RELATED DB: PDB REMARK 900 RELATED ID: 2PVF RELATED DB: PDB REMARK 900 RELATED ID: 2PSQ RELATED DB: PDB DBREF 5EG3 A 458 778 UNP P21802 FGFR2_HUMAN 458 778 DBREF 5EG3 B 661 773 UNP P10686 PLCG1_RAT 661 773 SEQADV 5EG3 MET A 445 UNP P21802 INITIATING METHIONINE SEQADV 5EG3 GLY A 446 UNP P21802 EXPRESSION TAG SEQADV 5EG3 SER A 447 UNP P21802 EXPRESSION TAG SEQADV 5EG3 SER A 448 UNP P21802 EXPRESSION TAG SEQADV 5EG3 HIS A 449 UNP P21802 EXPRESSION TAG SEQADV 5EG3 HIS A 450 UNP P21802 EXPRESSION TAG SEQADV 5EG3 HIS A 451 UNP P21802 EXPRESSION TAG SEQADV 5EG3 HIS A 452 UNP P21802 EXPRESSION TAG SEQADV 5EG3 HIS A 453 UNP P21802 EXPRESSION TAG SEQADV 5EG3 HIS A 454 UNP P21802 EXPRESSION TAG SEQADV 5EG3 SER A 455 UNP P21802 EXPRESSION TAG SEQADV 5EG3 GLN A 456 UNP P21802 EXPRESSION TAG SEQADV 5EG3 ASP A 457 UNP P21802 EXPRESSION TAG SEQADV 5EG3 PHE A 466 UNP P21802 TYR 466 ENGINEERED MUTATION SEQADV 5EG3 ALA A 491 UNP P21802 CYS 491 ENGINEERED MUTATION SEQADV 5EG3 ALA A 565 UNP P21802 GLU 565 ENGINEERED MUTATION SEQADV 5EG3 LEU A 586 UNP P21802 TYR 586 ENGINEERED MUTATION SEQADV 5EG3 PRO A 588 UNP P21802 TYR 588 ENGINEERED MUTATION SEQADV 5EG3 PHE A 656 UNP P21802 TYR 656 ENGINEERED MUTATION SEQADV 5EG3 PHE A 657 UNP P21802 TYR 657 ENGINEERED MUTATION SEQADV 5EG3 GLU A 659 UNP P21802 LYS 659 ENGINEERED MUTATION SEQADV 5EG3 MET B 660 UNP P10686 INITIATING METHIONINE SEQRES 1 A 334 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP SEQRES 2 A 334 PRO MET LEU ALA GLY VAL SER GLU PHE GLU LEU PRO GLU SEQRES 3 A 334 ASP PRO LYS TRP GLU PHE PRO ARG ASP LYS LEU THR LEU SEQRES 4 A 334 GLY LYS PRO LEU GLY GLU GLY ALA PHE GLY GLN VAL VAL SEQRES 5 A 334 MET ALA GLU ALA VAL GLY ILE ASP LYS ASP LYS PRO LYS SEQRES 6 A 334 GLU ALA VAL THR VAL ALA VAL LYS MET LEU LYS ASP ASP SEQRES 7 A 334 ALA THR GLU LYS ASP LEU SER ASP LEU VAL SER GLU MET SEQRES 8 A 334 GLU MET MET LYS MET ILE GLY LYS HIS LYS ASN ILE ILE SEQRES 9 A 334 ASN LEU LEU GLY ALA CYS THR GLN ASP GLY PRO LEU TYR SEQRES 10 A 334 VAL ILE VAL ALA TYR ALA SER LYS GLY ASN LEU ARG GLU SEQRES 11 A 334 TYR LEU ARG ALA ARG ARG PRO PRO GLY MET GLU LEU SER SEQRES 12 A 334 PRO ASP ILE ASN ARG VAL PRO GLU GLU GLN MET THR PHE SEQRES 13 A 334 LYS ASP LEU VAL SER CYS THR TYR GLN LEU ALA ARG GLY SEQRES 14 A 334 MET GLU TYR LEU ALA SER GLN LYS CYS ILE HIS ARG ASP SEQRES 15 A 334 LEU ALA ALA ARG ASN VAL LEU VAL THR GLU ASN ASN VAL SEQRES 16 A 334 MET LYS ILE ALA ASP PHE GLY LEU ALA ARG ASP ILE ASN SEQRES 17 A 334 ASN ILE ASP PHE PHE LYS GLU THR THR ASN GLY ARG LEU SEQRES 18 A 334 PRO VAL LYS TRP MET ALA PRO GLU ALA LEU PHE ASP ARG SEQRES 19 A 334 VAL TYR THR HIS GLN SER ASP VAL TRP SER PHE GLY VAL SEQRES 20 A 334 LEU MET TRP GLU ILE PHE THR LEU GLY GLY SER PRO TYR SEQRES 21 A 334 PRO GLY ILE PRO VAL GLU GLU LEU PHE LYS LEU LEU LYS SEQRES 22 A 334 GLU GLY HIS ARG MET ASP LYS PRO ALA ASN CYS THR ASN SEQRES 23 A 334 GLU LEU TYR MET MET MET ARG ASP CYS TRP HIS ALA VAL SEQRES 24 A 334 PRO SER GLN ARG PRO THR PHE LYS GLN LEU VAL GLU ASP SEQRES 25 A 334 LEU ASP ARG ILE LEU THR LEU THR THR ASN GLU GLU PTR SEQRES 26 A 334 LEU ASP LEU SER GLN PRO LEU GLU GLN SEQRES 1 B 114 MET ASN ALA HIS GLU SER LYS GLU TRP TYR HIS ALA SER SEQRES 2 B 114 LEU THR ARG ALA GLN ALA GLU HIS MET LEU MET ARG VAL SEQRES 3 B 114 PRO ARG ASP GLY ALA PHE LEU VAL ARG LYS ARG ASN GLU SEQRES 4 B 114 PRO ASN SER TYR ALA ILE SER PHE ARG ALA GLU GLY LYS SEQRES 5 B 114 ILE LYS HIS CYS ARG VAL GLN GLN GLU GLY GLN THR VAL SEQRES 6 B 114 MET LEU GLY ASN SER GLU PHE ASP SER LEU VAL ASP LEU SEQRES 7 B 114 ILE SER TYR TYR GLU LYS HIS PRO LEU TYR ARG LYS MET SEQRES 8 B 114 LYS LEU ARG TYR PRO ILE ASN GLU GLU ALA LEU GLU LYS SEQRES 9 B 114 ILE GLY THR ALA GLU PRO ASP TYR GLY ALA MODRES 5EG3 PTR A 769 TYR MODIFIED RESIDUE HET PTR A 769 16 HET ACP A 801 31 HET MG A 802 1 HET MG A 803 1 HETNAM PTR O-PHOSPHOTYROSINE HETNAM ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER HETNAM MG MAGNESIUM ION HETSYN PTR PHOSPHONOTYROSINE HETSYN ACP ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE FORMUL 1 PTR C9 H12 N O6 P FORMUL 3 ACP C11 H18 N5 O12 P3 FORMUL 4 MG 2(MG 2+) FORMUL 6 HOH *55(H2 O) HELIX 1 AA1 THR A 524 GLY A 542 1 19 HELIX 2 AA2 ASN A 571 ALA A 578 1 8 HELIX 3 AA3 VAL A 593 GLN A 597 5 5 HELIX 4 AA4 THR A 599 GLN A 620 1 22 HELIX 5 AA5 ALA A 628 ARG A 630 5 3 HELIX 6 AA6 PRO A 666 MET A 670 5 5 HELIX 7 AA7 ALA A 671 ARG A 678 1 8 HELIX 8 AA8 THR A 681 THR A 698 1 18 HELIX 9 AA9 PRO A 708 GLU A 718 1 11 HELIX 10 AB1 THR A 729 TRP A 740 1 12 HELIX 11 AB2 VAL A 743 ARG A 747 5 5 HELIX 12 AB3 THR A 749 GLU A 768 1 20 HELIX 13 AB4 MET B 660 LYS B 666 5 7 HELIX 14 AB5 THR B 674 MET B 683 1 10 HELIX 15 AB6 SER B 733 HIS B 744 1 12 HELIX 16 AB7 ALA B 760 GLY B 765 1 6 SHEET 1 AA1 5 LEU A 481 GLU A 489 0 SHEET 2 AA1 5 GLY A 493 VAL A 501 -1 O VAL A 495 N LEU A 487 SHEET 3 AA1 5 ALA A 511 LEU A 519 -1 O VAL A 516 N VAL A 496 SHEET 4 AA1 5 TYR A 561 ALA A 565 -1 O VAL A 564 N ALA A 515 SHEET 5 AA1 5 LEU A 550 CYS A 554 -1 N GLY A 552 O ILE A 563 SHEET 1 AA2 2 CYS A 622 ILE A 623 0 SHEET 2 AA2 2 ARG A 649 ASP A 650 -1 O ARG A 649 N ILE A 623 SHEET 1 AA3 2 VAL A 632 VAL A 634 0 SHEET 2 AA3 2 MET A 640 ILE A 642 -1 O LYS A 641 N LEU A 633 SHEET 1 AA4 2 PHE A 657 LYS A 658 0 SHEET 2 AA4 2 VAL A 679 TYR A 680 -1 O TYR A 680 N PHE A 657 SHEET 1 AA5 6 TYR B 669 HIS B 670 0 SHEET 2 AA5 6 ALA B 690 LYS B 695 1 O VAL B 693 N HIS B 670 SHEET 3 AA5 6 SER B 701 ALA B 708 -1 O SER B 705 N LEU B 692 SHEET 4 AA5 6 LYS B 711 GLU B 720 -1 O LYS B 713 N PHE B 706 SHEET 5 AA5 6 THR B 723 LEU B 726 -1 O MET B 725 N GLN B 718 SHEET 6 AA5 6 SER B 729 PHE B 731 -1 O SER B 729 N LEU B 726 SHEET 1 AA6 3 TYR B 669 HIS B 670 0 SHEET 2 AA6 3 ALA B 690 LYS B 695 1 O VAL B 693 N HIS B 670 SHEET 3 AA6 3 TYR B 754 PRO B 755 1 O TYR B 754 N PHE B 691 LINK O ARG A 630 MG MG A 802 1555 1555 2.87 LINK OD1 ASN A 631 MG MG A 802 1555 1555 2.52 LINK OD1 ASN A 631 MG MG A 803 1555 1555 2.31 LINK OD2 ASP A 644 MG MG A 803 1555 1555 2.14 LINK C GLU A 768 N PTR A 769 1555 1555 1.33 LINK C PTR A 769 N LEU A 770 1555 1555 1.32 LINK O1B ACP A 801 MG MG A 803 1555 1555 2.20 LINK O1A ACP A 801 MG MG A 802 1555 1555 2.65 LINK O1A ACP A 801 MG MG A 803 1555 1555 2.56 SITE 1 AC1 17 LEU A 487 GLY A 488 ALA A 515 LYS A 517 SITE 2 AC1 17 VAL A 564 ALA A 565 ALA A 567 ASN A 571 SITE 3 AC1 17 ARG A 630 ASN A 631 LEU A 633 ASP A 644 SITE 4 AC1 17 ARG A 664 MG A 802 MG A 803 HOH A 901 SITE 5 AC1 17 HOH A 911 SITE 1 AC2 4 ARG A 630 ASN A 631 ACP A 801 MG A 803 SITE 1 AC3 4 ASN A 631 ASP A 644 ACP A 801 MG A 802 CRYST1 79.609 53.231 127.660 90.00 100.11 90.00 C 1 2 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.012561 0.000000 0.002240 0.00000 SCALE2 0.000000 0.018786 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007957 0.00000 ATOM 1 N PHE A 466 21.489 -10.002 64.763 1.00101.42 N ANISOU 1 N PHE A 466 14197 14125 10212 1953 1025 1593 N ATOM 2 CA PHE A 466 20.419 -9.832 63.779 1.00100.20 C ANISOU 2 CA PHE A 466 13940 13947 10186 1912 1124 1614 C ATOM 3 C PHE A 466 20.098 -8.343 63.512 1.00 98.51 C ANISOU 3 C PHE A 466 13781 13732 9917 1933 1107 1485 C ATOM 4 O PHE A 466 19.437 -8.009 62.517 1.00 98.43 O ANISOU 4 O PHE A 466 13694 13697 10010 1886 1155 1473 O ATOM 5 CB PHE A 466 19.156 -10.593 64.239 1.00102.50 C ANISOU 5 CB PHE A 466 14157 14250 10538 1954 1286 1755 C ATOM 6 CG PHE A 466 17.960 -10.425 63.321 1.00102.82 C ANISOU 6 CG PHE A 466 14087 14264 10716 1916 1389 1785 C ATOM 7 CD1 PHE A 466 17.868 -11.138 62.132 1.00101.93 C ANISOU 7 CD1 PHE A 466 13847 14106 10777 1815 1396 1837 C ATOM 8 CD2 PHE A 466 16.921 -9.564 63.660 1.00103.71 C ANISOU 8 CD2 PHE A 466 14221 14394 10789 1984 1476 1765 C ATOM 9 CE1 PHE A 466 16.772 -10.983 61.293 1.00101.42 C ANISOU 9 CE1 PHE A 466 13680 14014 10842 1778 1481 1865 C ATOM 10 CE2 PHE A 466 15.823 -9.407 62.827 1.00103.18 C ANISOU 10 CE2 PHE A 466 14049 14302 10854 1950 1564 1796 C ATOM 11 CZ PHE A 466 15.748 -10.118 61.644 1.00102.04 C ANISOU 11 CZ PHE A 466 13777 14112 10880 1844 1564 1846 C ATOM 12 N GLU A 467 20.590 -7.452 64.377 1.00 96.79 N ANISOU 12 N GLU A 467 13697 13536 9544 2000 1034 1386 N ATOM 13 CA GLU A 467 20.203 -6.034 64.331 1.00 93.81 C ANISOU 13 CA GLU A 467 13383 13156 9106 2036 1026 1269 C ATOM 14 C GLU A 467 21.205 -5.141 63.588 1.00 84.64 C ANISOU 14 C GLU A 467 12260 11964 7934 1977 875 1126 C ATOM 15 O GLU A 467 22.412 -5.408 63.570 1.00 82.64 O ANISOU 15 O GLU A 467 12036 11703 7660 1940 747 1094 O ATOM 16 CB GLU A 467 20.013 -5.492 65.751 1.00 99.97 C ANISOU 16 CB GLU A 467 14289 13971 9724 2153 1043 1243 C ATOM 17 CG GLU A 467 19.362 -6.449 66.775 1.00107.58 C ANISOU 17 CG GLU A 467 15245 14972 10661 2226 1164 1382 C ATOM 18 CD GLU A 467 18.028 -7.077 66.345 1.00107.17 C ANISOU 18 CD GLU A 467 15061 14916 10744 2217 1328 1509 C ATOM 19 OE1 GLU A 467 17.546 -6.855 65.209 1.00106.15 O ANISOU 19 OE1 GLU A 467 14838 14756 10738 2150 1356 1498 O ATOM 20 OE2 GLU A 467 17.447 -7.809 67.175 1.00108.65 O ANISOU 20 OE2 GLU A 467 15236 15130 10917 2279 1429 1624 O ATOM 21 N LEU A 468 20.697 -4.063 62.998 1.00 76.62 N ANISOU 21 N LEU A 468 11244 10930 6938 1970 887 1042 N ATOM 22 CA LEU A 468 21.525 -3.146 62.215 1.00 69.45 C ANISOU 22 CA LEU A 468 10363 9989 6036 1913 753 907 C ATOM 23 C LEU A 468 21.918 -1.891 62.995 1.00 66.50 C ANISOU 23 C LEU A 468 10125 9614 5528 1974 664 776 C ATOM 24 O LEU A 468 21.114 -1.359 63.764 1.00 68.26 O ANISOU 24 O LEU A 468 10404 9854 5679 2058 740 772 O ATOM 25 CB LEU A 468 20.794 -2.742 60.931 1.00 62.78 C ANISOU 25 CB LEU A 468 9425 9118 5311 1855 812 892 C ATOM 26 CG LEU A 468 20.324 -3.905 60.059 1.00 58.44 C ANISOU 26 CG LEU A 468 8735 8561 4908 1788 899 1016 C ATOM 27 CD1 LEU A 468 19.615 -3.392 58.820 1.00 55.42 C ANISOU 27 CD1 LEU A 468 8271 8152 4635 1734 947 991 C ATOM 28 CD2 LEU A 468 21.487 -4.821 59.688 1.00 57.07 C ANISOU 28 CD2 LEU A 468 8535 8376 4773 1723 804 1044 C ATOM 29 N PRO A 469 23.158 -1.409 62.787 1.00 64.15 N ANISOU 29 N PRO A 469 9878 9291 5206 1931 498 670 N ATOM 30 CA PRO A 469 23.692 -0.203 63.434 1.00 64.13 C ANISOU 30 CA PRO A 469 9998 9273 5096 1972 385 538 C ATOM 31 C PRO A 469 22.993 1.059 62.972 1.00 64.02 C ANISOU 31 C PRO A 469 9995 9233 5098 1981 414 449 C ATOM 32 O PRO A 469 22.643 1.172 61.800 1.00 63.88 O ANISOU 32 O PRO A 469 9888 9195 5189 1918 447 446 O ATOM 33 CB PRO A 469 25.162 -0.191 63.003 1.00 62.69 C ANISOU 33 CB PRO A 469 9822 9060 4938 1897 206 469 C ATOM 34 CG PRO A 469 25.182 -0.954 61.738 1.00 60.32 C ANISOU 34 CG PRO A 469 9396 8750 4774 1811 235 531 C ATOM 35 CD PRO A 469 24.156 -2.033 61.903 1.00 60.52 C ANISOU 35 CD PRO A 469 9354 8811 4832 1838 403 678 C ATOM 36 N GLU A 470 22.805 2.000 63.888 1.00 66.81 N ANISOU 36 N GLU A 470 10457 9584 5342 2061 399 378 N ATOM 37 CA GLU A 470 22.055 3.213 63.596 1.00 67.73 C ANISOU 37 CA GLU A 470 10591 9676 5466 2084 435 300 C ATOM 38 C GLU A 470 22.870 4.216 62.786 1.00 67.26 C ANISOU 38 C GLU A 470 10541 9563 5452 2012 290 166 C ATOM 39 O GLU A 470 24.095 4.263 62.888 1.00 67.18 O ANISOU 39 O GLU A 470 10569 9532 5425 1974 139 107 O ATOM 40 CB GLU A 470 21.585 3.863 64.895 1.00 72.06 C ANISOU 40 CB GLU A 470 11259 10239 5881 2200 469 274 C ATOM 41 CG GLU A 470 20.771 2.939 65.784 1.00 75.57 C ANISOU 41 CG GLU A 470 11701 10738 6276 2281 613 406 C ATOM 42 CD GLU A 470 20.544 3.520 67.167 1.00 79.44 C ANISOU 42 CD GLU A 470 12327 11242 6614 2401 623 375 C ATOM 43 OE1 GLU A 470 21.182 4.548 67.490 1.00 80.70 O ANISOU 43 OE1 GLU A 470 12588 11370 6706 2415 499 250 O ATOM 44 OE2 GLU A 470 19.734 2.951 67.930 1.00 81.03 O ANISOU 44 OE2 GLU A 470 12534 11486 6769 2481 754 478 O ATOM 45 N ASP A 471 22.173 5.008 61.979 1.00 65.56 N ANISOU 45 N ASP A 471 10285 9322 5303 1993 337 123 N ATOM 46 CA ASP A 471 22.784 6.112 61.250 1.00 64.22 C ANISOU 46 CA ASP A 471 10127 9097 5177 1935 213 -7 C ATOM 47 C ASP A 471 21.741 7.199 61.086 1.00 63.28 C ANISOU 47 C ASP A 471 10018 8959 5064 1975 289 -52 C ATOM 48 O ASP A 471 20.997 7.204 60.103 1.00 62.13 O ANISOU 48 O ASP A 471 9781 8811 5014 1937 375 -23 O ATOM 49 CB ASP A 471 23.309 5.666 59.887 1.00 62.34 C ANISOU 49 CB ASP A 471 9781 8841 5063 1824 169 0 C ATOM 50 CG ASP A 471 24.230 6.699 59.247 1.00 62.17 C ANISOU 50 CG ASP A 471 9777 8760 5086 1760 12 -132 C ATOM 51 OD1 ASP A 471 24.368 7.805 59.816 1.00 63.73 O ANISOU 51 OD1 ASP A 471 10063 8926 5227 1798 -54 -227 O ATOM 52 OD2 ASP A 471 24.801 6.411 58.164 1.00 60.51 O ANISOU 52 OD2 ASP A 471 9489 8531 4973 1672 -42 -137 O ATOM 53 N PRO A 472 21.686 8.122 62.055 1.00 63.52 N ANISOU 53 N PRO A 472 10163 8976 4994 2053 256 -123 N ATOM 54 CA PRO A 472 20.604 9.106 62.184 1.00 62.83 C ANISOU 54 CA PRO A 472 10105 8878 4891 2116 343 -152 C ATOM 55 C PRO A 472 20.398 9.982 60.947 1.00 59.53 C ANISOU 55 C PRO A 472 9624 8413 4581 2049 324 -222 C ATOM 56 O PRO A 472 19.254 10.250 60.583 1.00 59.17 O ANISOU 56 O PRO A 472 9532 8374 4576 2073 447 -188 O ATOM 57 CB PRO A 472 21.049 9.951 63.381 1.00 65.15 C ANISOU 57 CB PRO A 472 10544 9153 5058 2193 253 -239 C ATOM 58 CG PRO A 472 21.931 9.041 64.170 1.00 66.22 C ANISOU 58 CG PRO A 472 10722 9316 5122 2201 188 -202 C ATOM 59 CD PRO A 472 22.669 8.239 63.145 1.00 64.76 C ANISOU 59 CD PRO A 472 10433 9128 5043 2089 133 -173 C ATOM 60 N LYS A 473 21.475 10.413 60.301 1.00 57.35 N ANISOU 60 N LYS A 473 9344 8091 4357 1967 175 -311 N ATOM 61 CA LYS A 473 21.332 11.328 59.170 1.00 55.46 C ANISOU 61 CA LYS A 473 9053 7803 4216 1906 149 -384 C ATOM 62 C LYS A 473 20.631 10.700 57.958 1.00 52.39 C ANISOU 62 C LYS A 473 8533 7433 3941 1848 258 -307 C ATOM 63 O LYS A 473 19.996 11.414 57.177 1.00 51.27 O ANISOU 63 O LYS A 473 8348 7266 3867 1829 299 -338 O ATOM 64 CB LYS A 473 22.701 11.882 58.758 1.00 55.82 C ANISOU 64 CB LYS A 473 9117 7792 4302 1828 -39 -489 C ATOM 65 CG LYS A 473 23.764 10.839 58.522 1.00 55.76 C ANISOU 65 CG LYS A 473 9068 7797 4322 1762 -118 -453 C ATOM 66 CD LYS A 473 25.045 11.477 58.018 1.00 55.01 C ANISOU 66 CD LYS A 473 8974 7639 4288 1681 -299 -553 C ATOM 67 CE LYS A 473 26.065 10.412 57.641 1.00 53.54 C ANISOU 67 CE LYS A 473 8732 7466 4146 1612 -371 -510 C ATOM 68 NZ LYS A 473 26.395 9.535 58.803 1.00 54.05 N ANISOU 68 NZ LYS A 473 8852 7573 4110 1665 -375 -449 N ATOM 69 N TRP A 474 20.736 9.378 57.808 1.00 50.51 N ANISOU 69 N TRP A 474 8232 7237 3723 1822 304 -207 N ATOM 70 CA TRP A 474 20.101 8.681 56.686 1.00 47.75 C ANISOU 70 CA TRP A 474 7757 6904 3482 1766 405 -127 C ATOM 71 C TRP A 474 18.787 7.986 57.062 1.00 47.60 C ANISOU 71 C TRP A 474 7693 6933 3461 1827 584 -1 C ATOM 72 O TRP A 474 18.057 7.517 56.186 1.00 45.78 O ANISOU 72 O TRP A 474 7356 6712 3328 1788 681 69 O ATOM 73 CB TRP A 474 21.047 7.639 56.083 1.00 46.12 C ANISOU 73 CB TRP A 474 7492 6705 3325 1687 341 -91 C ATOM 74 CG TRP A 474 22.178 8.195 55.278 1.00 44.39 C ANISOU 74 CG TRP A 474 7270 6436 3158 1606 186 -194 C ATOM 75 CD1 TRP A 474 23.486 8.270 55.653 1.00 44.36 C ANISOU 75 CD1 TRP A 474 7322 6411 3122 1583 32 -253 C ATOM 76 CD2 TRP A 474 22.110 8.739 53.956 1.00 43.23 C ANISOU 76 CD2 TRP A 474 7058 6254 3115 1536 170 -245 C ATOM 77 NE1 TRP A 474 24.239 8.831 54.651 1.00 43.34 N ANISOU 77 NE1 TRP A 474 7159 6231 3075 1502 -79 -335 N ATOM 78 CE2 TRP A 474 23.419 9.129 53.595 1.00 42.67 C ANISOU 78 CE2 TRP A 474 7004 6139 3071 1473 3 -334 C ATOM 79 CE3 TRP A 474 21.072 8.933 53.034 1.00 42.72 C ANISOU 79 CE3 TRP A 474 6917 6188 3128 1519 278 -222 C ATOM 80 CZ2 TRP A 474 23.718 9.706 52.359 1.00 41.91 C ANISOU 80 CZ2 TRP A 474 6835 5987 3102 1383 -55 -394 C ATOM 81 CZ3 TRP A 474 21.376 9.508 51.794 1.00 41.67 C ANISOU 81 CZ3 TRP A 474 6708 5996 3128 1423 213 -286 C ATOM 82 CH2 TRP A 474 22.685 9.890 51.475 1.00 41.29 C ANISOU 82 CH2 TRP A 474 6670 5899 3120 1355 52 -369 C ATOM 83 N GLU A 475 18.489 7.906 58.355 1.00 48.60 N ANISOU 83 N GLU A 475 7896 7087 3483 1920 627 31 N ATOM 84 CA GLU A 475 17.319 7.159 58.810 1.00 48.59 C ANISOU 84 CA GLU A 475 7851 7130 3482 1979 792 161 C ATOM 85 C GLU A 475 16.006 7.886 58.467 1.00 47.39 C ANISOU 85 C GLU A 475 7657 6968 3380 2010 905 170 C ATOM 86 O GLU A 475 15.934 9.121 58.489 1.00 47.32 O ANISOU 86 O GLU A 475 7707 6926 3345 2034 863 71 O ATOM 87 CB GLU A 475 17.416 6.900 60.318 1.00 50.19 C ANISOU 87 CB GLU A 475 8153 7364 3552 2075 803 191 C ATOM 88 CG GLU A 475 16.535 5.770 60.823 1.00 50.20 C ANISOU 88 CG GLU A 475 8100 7413 3559 2121 952 343 C ATOM 89 CD GLU A 475 16.959 4.402 60.301 1.00 48.59 C ANISOU 89 CD GLU A 475 7805 7228 3430 2047 955 435 C ATOM 90 OE1 GLU A 475 16.137 3.460 60.380 1.00 48.25 O ANISOU 90 OE1 GLU A 475 7682 7212 3438 2060 1083 566 O ATOM 91 OE2 GLU A 475 18.108 4.264 59.816 1.00 47.56 O ANISOU 91 OE2 GLU A 475 7679 7080 3313 1975 829 379 O ATOM 92 N PHE A 476 14.973 7.111 58.145 1.00 46.71 N ANISOU 92 N PHE A 476 7465 6907 3374 2008 1045 294 N ATOM 93 CA PHE A 476 13.692 7.666 57.723 1.00 46.56 C ANISOU 93 CA PHE A 476 7387 6880 3425 2029 1156 319 C ATOM 94 C PHE A 476 12.522 6.908 58.351 1.00 48.76 C ANISOU 94 C PHE A 476 7614 7196 3717 2094 1313 463 C ATOM 95 O PHE A 476 12.501 5.680 58.298 1.00 48.53 O ANISOU 95 O PHE A 476 7514 7190 3735 2064 1358 570 O ATOM 96 CB PHE A 476 13.582 7.640 56.199 1.00 44.69 C ANISOU 96 CB PHE A 476 7036 6618 3328 1927 1152 313 C ATOM 97 CG PHE A 476 12.441 8.455 55.673 1.00 44.59 C ANISOU 97 CG PHE A 476 6972 6586 3386 1940 1232 310 C ATOM 98 CD1 PHE A 476 12.523 9.838 55.634 1.00 43.98 C ANISOU 98 CD1 PHE A 476 6966 6474 3273 1963 1172 190 C ATOM 99 CD2 PHE A 476 11.275 7.846 55.243 1.00 44.94 C ANISOU 99 CD2 PHE A 476 6894 6643 3539 1931 1364 431 C ATOM 100 CE1 PHE A 476 11.459 10.602 55.165 1.00 43.94 C ANISOU 100 CE1 PHE A 476 6912 6449 3332 1979 1247 190 C ATOM 101 CE2 PHE A 476 10.217 8.601 54.770 1.00 44.99 C ANISOU 101 CE2 PHE A 476 6849 6630 3614 1944 1434 432 C ATOM 102 CZ PHE A 476 10.309 9.986 54.733 1.00 44.29 C ANISOU 102 CZ PHE A 476 6836 6510 3483 1970 1377 311 C ATOM 103 N PRO A 477 11.542 7.640 58.940 1.00 50.50 N ANISOU 103 N PRO A 477 7868 7418 3902 2183 1397 470 N ATOM 104 CA PRO A 477 10.447 7.062 59.744 1.00 53.20 C ANISOU 104 CA PRO A 477 8182 7794 4238 2265 1543 600 C ATOM 105 C PRO A 477 9.523 6.169 58.923 1.00 54.15 C ANISOU 105 C PRO A 477 8139 7919 4518 2209 1651 731 C ATOM 106 O PRO A 477 9.171 6.562 57.816 1.00 53.33 O ANISOU 106 O PRO A 477 7956 7787 4522 2145 1652 708 O ATOM 107 CB PRO A 477 9.684 8.295 60.246 1.00 53.34 C ANISOU 107 CB PRO A 477 8268 7800 4200 2357 1588 552 C ATOM 108 CG PRO A 477 10.593 9.463 60.010 1.00 52.19 C ANISOU 108 CG PRO A 477 8217 7617 3998 2334 1446 388 C ATOM 109 CD PRO A 477 11.386 9.098 58.797 1.00 50.38 C ANISOU 109 CD PRO A 477 7914 7368 3862 2209 1358 354 C ATOM 110 N ARG A 478 9.128 5.008 59.443 1.00 57.47 N ANISOU 110 N ARG A 478 8508 8368 4958 2231 1736 865 N ATOM 111 CA ARG A 478 8.353 4.043 58.652 1.00 58.56 C ANISOU 111 CA ARG A 478 8486 8503 5262 2166 1822 992 C ATOM 112 C ARG A 478 6.886 4.447 58.406 1.00 61.48 C ANISOU 112 C ARG A 478 8771 8861 5726 2197 1940 1058 C ATOM 113 O ARG A 478 6.249 3.944 57.472 1.00 61.81 O ANISOU 113 O ARG A 478 8675 8885 5926 2125 1986 1134 O ATOM 114 CB ARG A 478 8.390 2.664 59.311 1.00 58.43 C ANISOU 114 CB ARG A 478 8438 8516 5248 2179 1871 1119 C ATOM 115 CG ARG A 478 9.751 1.993 59.291 1.00 56.95 C ANISOU 115 CG ARG A 478 8290 8334 5013 2124 1762 1084 C ATOM 116 CD ARG A 478 9.679 0.606 59.904 1.00 56.98 C ANISOU 116 CD ARG A 478 8251 8364 5035 2136 1821 1220 C ATOM 117 NE ARG A 478 11.010 0.086 60.177 1.00 56.64 N ANISOU 117 NE ARG A 478 8274 8332 4913 2110 1716 1182 N ATOM 118 CZ ARG A 478 11.716 -0.629 59.311 1.00 55.63 C ANISOU 118 CZ ARG A 478 8084 8189 4864 2008 1652 1189 C ATOM 119 NH1 ARG A 478 11.204 -0.914 58.123 1.00 53.91 N ANISOU 119 NH1 ARG A 478 7738 7942 4803 1922 1683 1230 N ATOM 120 NH2 ARG A 478 12.928 -1.064 59.633 1.00 56.11 N ANISOU 120 NH2 ARG A 478 8210 8260 4848 1992 1555 1156 N ATOM 121 N ASP A 479 6.354 5.345 59.235 1.00 64.98 N ANISOU 121 N ASP A 479 9299 9313 6080 2302 1986 1031 N ATOM 122 CA ASP A 479 4.997 5.865 59.053 1.00 67.70 C ANISOU 122 CA ASP A 479 9574 9644 6502 2340 2093 1085 C ATOM 123 C ASP A 479 5.002 6.926 57.974 1.00 65.79 C ANISOU 123 C ASP A 479 9315 9366 6316 2283 2036 979 C ATOM 124 O ASP A 479 4.012 7.145 57.282 1.00 64.74 O ANISOU 124 O ASP A 479 9079 9213 6306 2261 2100 1026 O ATOM 125 CB ASP A 479 4.469 6.459 60.351 1.00 73.31 C ANISOU 125 CB ASP A 479 10389 10376 7089 2481 2164 1093 C ATOM 126 CG ASP A 479 5.003 5.746 61.561 1.00 77.65 C ANISOU 126 CG ASP A 479 11024 10963 7516 2547 2166 1131 C ATOM 127 OD1 ASP A 479 4.945 4.495 61.580 1.00 80.30 O ANISOU 127 OD1 ASP A 479 11279 11315 7918 2514 2206 1245 O ATOM 128 OD2 ASP A 479 5.501 6.433 62.481 1.00 81.42 O ANISOU 128 OD2 ASP A 479 11650 11452 7835 2629 2124 1046 O ATOM 129 N LYS A 480 6.150 7.581 57.853 1.00 64.53 N ANISOU 129 N LYS A 480 9257 9194 6067 2259 1909 837 N ATOM 130 CA LYS A 480 6.398 8.612 56.857 1.00 61.42 C ANISOU 130 CA LYS A 480 8862 8763 5711 2203 1834 719 C ATOM 131 C LYS A 480 6.369 8.035 55.434 1.00 55.87 C ANISOU 131 C LYS A 480 8019 8040 5168 2080 1820 752 C ATOM 132 O LYS A 480 6.481 8.779 54.462 1.00 52.45 O ANISOU 132 O LYS A 480 7564 7576 4788 2025 1768 671 O ATOM 133 CB LYS A 480 7.764 9.258 57.114 1.00 63.54 C ANISOU 133 CB LYS A 480 9268 9021 5854 2199 1689 570 C ATOM 134 CG LYS A 480 7.813 10.494 58.037 1.00 66.38 C ANISOU 134 CG LYS A 480 9770 9371 6079 2298 1663 473 C ATOM 135 CD LYS A 480 7.111 11.706 57.468 1.00 67.86 C ANISOU 135 CD LYS A 480 9941 9524 6317 2307 1682 417 C ATOM 136 CE LYS A 480 7.802 13.047 57.792 1.00 69.77 C ANISOU 136 CE LYS A 480 10321 9733 6455 2340 1572 260 C ATOM 137 NZ LYS A 480 9.271 13.104 57.518 1.00 70.48 N ANISOU 137 NZ LYS A 480 10469 9803 6506 2270 1413 151 N ATOM 138 N LEU A 481 6.222 6.712 55.334 1.00 51.50 N ANISOU 138 N LEU A 481 7373 7503 4690 2040 1866 872 N ATOM 139 CA LEU A 481 6.414 5.952 54.095 1.00 46.94 C ANISOU 139 CA LEU A 481 6677 6908 4250 1921 1839 906 C ATOM 140 C LEU A 481 5.227 5.044 53.730 1.00 44.70 C ANISOU 140 C LEU A 481 6239 6620 4127 1892 1947 1061 C ATOM 141 O LEU A 481 4.745 4.269 54.550 1.00 47.98 O ANISOU 141 O LEU A 481 6634 7055 4539 1941 2024 1173 O ATOM 142 CB LEU A 481 7.679 5.095 54.221 1.00 43.26 C ANISOU 142 CB LEU A 481 6250 6456 3729 1877 1756 891 C ATOM 143 CG LEU A 481 8.196 4.322 53.010 1.00 39.20 C ANISOU 143 CG LEU A 481 5643 5925 3327 1757 1707 905 C ATOM 144 CD1 LEU A 481 8.847 5.290 52.030 1.00 37.69 C ANISOU 144 CD1 LEU A 481 5479 5706 3135 1704 1610 768 C ATOM 145 CD2 LEU A 481 9.164 3.226 53.426 1.00 38.01 C ANISOU 145 CD2 LEU A 481 5520 5795 3128 1737 1662 939 C ATOM 146 N THR A 482 4.780 5.116 52.484 1.00 42.82 N ANISOU 146 N THR A 482 5887 6349 4032 1810 1946 1070 N ATOM 147 CA THR A 482 3.646 4.314 52.050 1.00 42.32 C ANISOU 147 CA THR A 482 5670 6271 4137 1773 2031 1211 C ATOM 148 C THR A 482 4.005 3.458 50.845 1.00 42.03 C ANISOU 148 C THR A 482 5528 6209 4233 1648 1981 1235 C ATOM 149 O THR A 482 4.029 3.952 49.716 1.00 40.82 O ANISOU 149 O THR A 482 5327 6027 4154 1581 1937 1177 O ATOM 150 CB THR A 482 2.451 5.204 51.689 1.00 43.87 C ANISOU 150 CB THR A 482 5810 6446 4412 1797 2091 1222 C ATOM 151 OG1 THR A 482 2.418 6.324 52.583 1.00 45.44 O ANISOU 151 OG1 THR A 482 6134 6661 4469 1904 2105 1147 O ATOM 152 CG2 THR A 482 1.145 4.415 51.765 1.00 44.43 C ANISOU 152 CG2 THR A 482 5748 6507 4625 1800 2193 1384 C ATOM 153 N LEU A 483 4.274 2.177 51.087 1.00 43.64 N ANISOU 153 N LEU A 483 5695 6420 4468 1618 1987 1323 N ATOM 154 CA LEU A 483 4.678 1.257 50.024 1.00 44.26 C ANISOU 154 CA LEU A 483 5679 6470 4667 1500 1937 1351 C ATOM 155 C LEU A 483 3.562 1.072 48.997 1.00 45.60 C ANISOU 155 C LEU A 483 5694 6596 5035 1431 1971 1424 C ATOM 156 O LEU A 483 2.394 1.171 49.343 1.00 43.42 O ANISOU 156 O LEU A 483 5364 6315 4820 1476 2050 1504 O ATOM 157 CB LEU A 483 5.087 -0.098 50.611 1.00 45.32 C ANISOU 157 CB LEU A 483 5804 6615 4799 1491 1944 1442 C ATOM 158 CG LEU A 483 6.215 -0.056 51.639 1.00 46.33 C ANISOU 158 CG LEU A 483 6079 6785 4740 1554 1903 1381 C ATOM 159 CD1 LEU A 483 6.774 -1.453 51.895 1.00 46.84 C ANISOU 159 CD1 LEU A 483 6120 6853 4826 1518 1890 1463 C ATOM 160 CD2 LEU A 483 7.310 0.890 51.176 1.00 45.44 C ANISOU 160 CD2 LEU A 483 6063 6675 4527 1536 1801 1224 C ATOM 161 N GLY A 484 3.918 0.799 47.742 1.00 47.38 N ANISOU 161 N GLY A 484 5850 6789 5365 1324 1907 1399 N ATOM 162 CA GLY A 484 2.917 0.689 46.696 1.00 50.09 C ANISOU 162 CA GLY A 484 6051 7086 5897 1252 1920 1455 C ATOM 163 C GLY A 484 3.170 -0.286 45.566 1.00 48.12 C ANISOU 163 C GLY A 484 5698 6791 5794 1128 1861 1489 C ATOM 164 O GLY A 484 3.416 -1.467 45.792 1.00 49.25 O ANISOU 164 O GLY A 484 5813 6925 5975 1096 1858 1564 O ATOM 165 N LYS A 485 3.092 0.228 44.344 1.00 48.58 N ANISOU 165 N LYS A 485 5713 6799 5947 1046 1773 1411 N ATOM 166 CA LYS A 485 3.173 -0.568 43.120 1.00 49.30 C ANISOU 166 CA LYS A 485 5713 6819 6199 915 1672 1412 C ATOM 167 C LYS A 485 4.580 -1.158 42.860 1.00 50.62 C ANISOU 167 C LYS A 485 5947 6967 6318 852 1556 1332 C ATOM 168 O LYS A 485 5.566 -0.416 42.790 1.00 50.83 O ANISOU 168 O LYS A 485 6075 7004 6232 858 1483 1203 O ATOM 169 CB LYS A 485 2.740 0.303 41.933 1.00 52.03 C ANISOU 169 CB LYS A 485 6013 7122 6632 859 1608 1339 C ATOM 170 CG LYS A 485 2.365 -0.460 40.676 1.00 54.64 C ANISOU 170 CG LYS A 485 6230 7379 7152 738 1528 1370 C ATOM 171 CD LYS A 485 2.048 0.490 39.525 1.00 56.02 C ANISOU 171 CD LYS A 485 6379 7517 7389 690 1457 1287 C ATOM 172 CE LYS A 485 1.343 -0.232 38.371 1.00 57.80 C ANISOU 172 CE LYS A 485 6480 7671 7810 585 1396 1341 C ATOM 173 NZ LYS A 485 2.096 -1.422 37.867 1.00 57.37 N ANISOU 173 NZ LYS A 485 6424 7572 7803 498 1306 1332 N ATOM 174 N PRO A 486 4.677 -2.495 42.717 1.00 49.32 N ANISOU 174 N PRO A 486 5723 6771 6246 792 1539 1410 N ATOM 175 CA PRO A 486 5.971 -3.134 42.444 1.00 48.23 C ANISOU 175 CA PRO A 486 5638 6610 6076 733 1435 1344 C ATOM 176 C PRO A 486 6.567 -2.674 41.119 1.00 45.28 C ANISOU 176 C PRO A 486 5275 6186 5743 645 1305 1213 C ATOM 177 O PRO A 486 5.826 -2.447 40.164 1.00 44.41 O ANISOU 177 O PRO A 486 5090 6034 5750 592 1280 1212 O ATOM 178 CB PRO A 486 5.632 -4.633 42.406 1.00 49.31 C ANISOU 178 CB PRO A 486 5684 6709 6342 683 1453 1469 C ATOM 179 CG PRO A 486 4.410 -4.754 43.228 1.00 51.55 C ANISOU 179 CG PRO A 486 5902 7026 6659 753 1593 1611 C ATOM 180 CD PRO A 486 3.620 -3.491 42.952 1.00 51.83 C ANISOU 180 CD PRO A 486 5924 7075 6695 787 1625 1574 C ATOM 181 N LEU A 487 7.893 -2.536 41.093 1.00 42.83 N ANISOU 181 N LEU A 487 5058 5881 5335 634 1223 1111 N ATOM 182 CA LEU A 487 8.637 -1.999 39.957 1.00 40.84 C ANISOU 182 CA LEU A 487 4832 5590 5095 565 1107 983 C ATOM 183 C LEU A 487 9.587 -3.050 39.404 1.00 44.68 C ANISOU 183 C LEU A 487 5318 6033 5625 490 1023 965 C ATOM 184 O LEU A 487 9.917 -3.061 38.221 1.00 38.66 O ANISOU 184 O LEU A 487 4539 5220 4931 413 936 899 O ATOM 185 CB LEU A 487 9.442 -0.765 40.367 1.00 38.16 C ANISOU 185 CB LEU A 487 4603 5290 4605 620 1081 871 C ATOM 186 CG LEU A 487 8.746 0.505 40.841 1.00 37.26 C ANISOU 186 CG LEU A 487 4517 5214 4425 698 1146 852 C ATOM 187 CD1 LEU A 487 9.780 1.553 41.211 1.00 36.69 C ANISOU 187 CD1 LEU A 487 4562 5167 4210 739 1094 731 C ATOM 188 CD2 LEU A 487 7.835 1.033 39.766 1.00 36.09 C ANISOU 188 CD2 LEU A 487 4293 5028 4393 652 1134 843 C ATOM 189 N GLY A 488 10.055 -3.917 40.283 1.00 54.63 N ANISOU 189 N GLY A 488 6602 7315 6841 519 1051 1023 N ATOM 190 CA GLY A 488 10.987 -4.941 39.886 1.00 64.30 C ANISOU 190 CA GLY A 488 7828 8500 8101 459 980 1011 C ATOM 191 C GLY A 488 10.972 -6.028 40.922 1.00 65.93 C ANISOU 191 C GLY A 488 8027 8728 8297 496 1042 1123 C ATOM 192 O GLY A 488 10.669 -5.790 42.093 1.00 69.73 O ANISOU 192 O GLY A 488 8540 9269 8686 581 1128 1178 O ATOM 193 N GLU A 489 11.272 -7.240 40.485 1.00 68.99 N ANISOU 193 N GLU A 489 8373 9063 8777 434 1002 1159 N ATOM 194 CA GLU A 489 11.428 -8.345 41.408 1.00 71.94 C ANISOU 194 CA GLU A 489 8742 9449 9143 462 1049 1262 C ATOM 195 C GLU A 489 12.618 -9.174 40.962 1.00 72.57 C ANISOU 195 C GLU A 489 8845 9486 9242 409 962 1219 C ATOM 196 O GLU A 489 12.754 -9.506 39.783 1.00 71.19 O ANISOU 196 O GLU A 489 8636 9246 9168 330 889 1172 O ATOM 197 CB GLU A 489 10.151 -9.190 41.485 1.00 75.94 C ANISOU 197 CB GLU A 489 9142 9927 9783 448 1122 1402 C ATOM 198 CG GLU A 489 8.918 -8.377 41.876 1.00 79.91 C ANISOU 198 CG GLU A 489 9611 10469 10282 502 1216 1453 C ATOM 199 CD GLU A 489 7.785 -9.219 42.428 1.00 83.60 C ANISOU 199 CD GLU A 489 9985 10932 10848 519 1316 1618 C ATOM 200 OE1 GLU A 489 8.026 -10.413 42.721 1.00 84.87 O ANISOU 200 OE1 GLU A 489 10121 11068 11057 501 1320 1697 O ATOM 201 OE2 GLU A 489 6.663 -8.677 42.586 1.00 85.14 O ANISOU 201 OE2 GLU A 489 10128 11146 11076 553 1394 1674 O ATOM 202 N GLY A 490 13.503 -9.459 41.909 1.00 78.59 N ANISOU 202 N GLY A 490 9671 10289 9901 457 967 1230 N ATOM 203 CA GLY A 490 14.598 -10.381 41.690 1.00 82.16 C ANISOU 203 CA GLY A 490 10138 10704 10373 419 900 1214 C ATOM 204 C GLY A 490 14.248 -11.654 42.423 1.00 77.72 C ANISOU 204 C GLY A 490 9534 10135 9861 434 960 1352 C ATOM 205 O GLY A 490 13.080 -11.900 42.722 1.00 80.55 O ANISOU 205 O GLY A 490 9830 10495 10280 448 1040 1454 O ATOM 206 N ALA A 491 15.250 -12.465 42.729 1.00 73.79 N ANISOU 206 N ALA A 491 9066 9627 9344 433 924 1362 N ATOM 207 CA ALA A 491 14.999 -13.705 43.451 1.00 77.55 C ANISOU 207 CA ALA A 491 9504 10094 9866 448 978 1496 C ATOM 208 C ALA A 491 14.767 -13.429 44.935 1.00 83.18 C ANISOU 208 C ALA A 491 10263 10894 10448 549 1069 1574 C ATOM 209 O ALA A 491 13.754 -13.840 45.511 1.00 87.27 O ANISOU 209 O ALA A 491 10730 11423 11004 578 1164 1699 O ATOM 210 CB ALA A 491 16.156 -14.670 43.260 1.00 77.59 C ANISOU 210 CB ALA A 491 9527 10058 9898 416 909 1482 C ATOM 211 N PHE A 492 15.714 -12.727 45.548 1.00 88.57 N ANISOU 211 N PHE A 492 11043 11634 10976 603 1039 1502 N ATOM 212 CA PHE A 492 15.625 -12.418 46.966 1.00 90.26 C ANISOU 212 CA PHE A 492 11321 11930 11042 705 1112 1561 C ATOM 213 C PHE A 492 15.211 -10.962 47.174 1.00 90.17 C ANISOU 213 C PHE A 492 11362 11974 10925 758 1138 1490 C ATOM 214 O PHE A 492 14.788 -10.579 48.268 1.00 90.34 O ANISOU 214 O PHE A 492 11430 12062 10832 850 1220 1542 O ATOM 215 CB PHE A 492 16.955 -12.711 47.652 1.00 90.49 C ANISOU 215 CB PHE A 492 11430 11986 10965 738 1055 1539 C ATOM 216 N GLY A 493 15.321 -10.165 46.111 1.00 88.34 N ANISOU 216 N GLY A 493 11122 11710 10731 704 1072 1374 N ATOM 217 CA GLY A 493 15.024 -8.742 46.170 1.00 81.99 C ANISOU 217 CA GLY A 493 10367 10946 9840 745 1082 1293 C ATOM 218 C GLY A 493 13.733 -8.295 45.499 1.00 74.28 C ANISOU 218 C GLY A 493 9315 9949 8958 721 1134 1308 C ATOM 219 O GLY A 493 13.185 -8.969 44.624 1.00 71.74 O ANISOU 219 O GLY A 493 8900 9566 8790 648 1129 1348 O ATOM 220 N GLN A 494 13.251 -7.133 45.918 1.00 67.53 N ANISOU 220 N GLN A 494 8505 9143 8012 786 1179 1274 N ATOM 221 CA GLN A 494 12.064 -6.533 45.342 1.00 61.30 C ANISOU 221 CA GLN A 494 7652 8339 7300 774 1227 1282 C ATOM 222 C GLN A 494 12.178 -5.022 45.432 1.00 54.26 C ANISOU 222 C GLN A 494 6837 7483 6297 821 1211 1171 C ATOM 223 O GLN A 494 12.686 -4.491 46.418 1.00 55.25 O ANISOU 223 O GLN A 494 7062 7663 6268 901 1220 1139 O ATOM 224 CB GLN A 494 10.809 -7.017 46.057 1.00 58.80 C ANISOU 224 CB GLN A 494 7274 8047 7020 826 1359 1432 C ATOM 225 CG GLN A 494 9.531 -6.578 45.397 1.00 56.32 C ANISOU 225 CG GLN A 494 6872 7709 6818 804 1406 1459 C ATOM 226 CD GLN A 494 8.367 -7.491 45.723 1.00 56.84 C ANISOU 226 CD GLN A 494 6834 7766 6996 812 1512 1626 C ATOM 227 OE1 GLN A 494 8.515 -8.447 46.485 1.00 58.06 O ANISOU 227 OE1 GLN A 494 6987 7934 7138 838 1556 1724 O ATOM 228 NE2 GLN A 494 7.200 -7.208 45.138 1.00 56.96 N ANISOU 228 NE2 GLN A 494 6757 7755 7130 788 1551 1663 N ATOM 229 N VAL A 495 11.723 -4.339 44.389 1.00 47.83 N ANISOU 229 N VAL A 495 5978 6633 5561 770 1182 1110 N ATOM 230 CA VAL A 495 11.673 -2.880 44.362 1.00 41.94 C ANISOU 230 CA VAL A 495 5292 5911 4734 809 1171 1011 C ATOM 231 C VAL A 495 10.235 -2.422 44.198 1.00 40.11 C ANISOU 231 C VAL A 495 4991 5680 4567 831 1260 1066 C ATOM 232 O VAL A 495 9.559 -2.827 43.260 1.00 38.84 O ANISOU 232 O VAL A 495 4730 5470 4556 760 1254 1103 O ATOM 233 CB VAL A 495 12.520 -2.287 43.211 1.00 39.68 C ANISOU 233 CB VAL A 495 5020 5580 4477 733 1049 878 C ATOM 234 CG1 VAL A 495 12.193 -0.830 43.008 1.00 39.03 C ANISOU 234 CG1 VAL A 495 4971 5508 4349 762 1047 794 C ATOM 235 CG2 VAL A 495 13.994 -2.446 43.491 1.00 38.85 C ANISOU 235 CG2 VAL A 495 4992 5480 4288 728 964 813 C ATOM 236 N VAL A 496 9.758 -1.582 45.108 1.00 39.42 N ANISOU 236 N VAL A 496 4960 5648 4371 932 1339 1072 N ATOM 237 CA VAL A 496 8.389 -1.105 45.015 1.00 39.12 C ANISOU 237 CA VAL A 496 4856 5614 4394 962 1432 1129 C ATOM 238 C VAL A 496 8.353 0.416 44.959 1.00 38.06 C ANISOU 238 C VAL A 496 4787 5494 4179 1007 1419 1020 C ATOM 239 O VAL A 496 9.233 1.094 45.504 1.00 39.16 O ANISOU 239 O VAL A 496 5043 5662 4176 1055 1376 928 O ATOM 240 CB VAL A 496 7.541 -1.601 46.195 1.00 39.08 C ANISOU 240 CB VAL A 496 4835 5659 4355 1055 1576 1271 C ATOM 241 CG1 VAL A 496 7.649 -3.113 46.311 1.00 38.65 C ANISOU 241 CG1 VAL A 496 4719 5586 4379 1012 1585 1381 C ATOM 242 CG2 VAL A 496 7.979 -0.934 47.487 1.00 39.64 C ANISOU 242 CG2 VAL A 496 5041 5799 4221 1176 1618 1236 C ATOM 243 N MET A 497 7.351 0.945 44.267 1.00 36.75 N ANISOU 243 N MET A 497 4547 5305 4112 989 1448 1030 N ATOM 244 CA MET A 497 7.109 2.379 44.261 1.00 35.95 C ANISOU 244 CA MET A 497 4498 5217 3947 1040 1455 945 C ATOM 245 C MET A 497 6.548 2.779 45.623 1.00 38.43 C ANISOU 245 C MET A 497 4872 5595 4136 1177 1581 998 C ATOM 246 O MET A 497 5.897 1.965 46.271 1.00 39.21 O ANISOU 246 O MET A 497 4924 5719 4255 1217 1685 1129 O ATOM 247 CB MET A 497 6.139 2.751 43.141 1.00 36.96 C ANISOU 247 CB MET A 497 4520 5300 4223 983 1453 955 C ATOM 248 CG MET A 497 5.921 4.232 42.973 1.00 38.21 C ANISOU 248 CG MET A 497 4723 5460 4334 1025 1448 863 C ATOM 249 SD MET A 497 4.741 4.546 41.670 1.00 48.98 S ANISOU 249 SD MET A 497 5955 6773 5881 957 1444 891 S ATOM 250 CE MET A 497 5.477 3.618 40.340 1.00 36.69 C ANISOU 250 CE MET A 497 4347 5154 4439 811 1309 860 C ATOM 251 N ALA A 498 6.797 4.004 46.079 1.00 40.12 N ANISOU 251 N ALA A 498 5191 5832 4221 1252 1577 902 N ATOM 252 CA ALA A 498 6.190 4.441 47.336 1.00 42.68 C ANISOU 252 CA ALA A 498 5580 6215 4422 1391 1703 948 C ATOM 253 C ALA A 498 6.053 5.957 47.460 1.00 40.29 C ANISOU 253 C ALA A 498 5357 5916 4034 1460 1704 843 C ATOM 254 O ALA A 498 6.600 6.720 46.668 1.00 39.82 O ANISOU 254 O ALA A 498 5318 5817 3993 1402 1595 725 O ATOM 255 CB ALA A 498 6.973 3.898 48.523 1.00 31.62 C ANISOU 255 CB ALA A 498 4282 4860 2871 1454 1710 962 C ATOM 256 N GLU A 499 5.287 6.376 48.461 1.00 40.32 N ANISOU 256 N GLU A 499 5399 5938 3982 1556 1779 877 N ATOM 257 CA GLU A 499 5.153 7.784 48.776 1.00 41.15 C ANISOU 257 CA GLU A 499 5592 6038 4003 1625 1770 778 C ATOM 258 C GLU A 499 5.803 8.043 50.125 1.00 42.48 C ANISOU 258 C GLU A 499 5911 6235 3994 1713 1747 728 C ATOM 259 O GLU A 499 5.472 7.399 51.127 1.00 42.74 O ANISOU 259 O GLU A 499 5957 6296 3988 1770 1811 815 O ATOM 260 CB GLU A 499 3.688 8.207 48.762 1.00 45.62 C ANISOU 260 CB GLU A 499 6081 6593 4660 1663 1866 850 C ATOM 261 CG GLU A 499 3.097 8.210 47.366 1.00 48.30 C ANISOU 261 CG GLU A 499 6282 6897 5171 1577 1866 876 C ATOM 262 CD GLU A 499 3.694 9.304 46.477 1.00 50.27 C ANISOU 262 CD GLU A 499 6572 7122 5408 1546 1783 737 C ATOM 263 OE1 GLU A 499 3.985 10.405 47.001 1.00 54.04 O ANISOU 263 OE1 GLU A 499 7165 7599 5770 1612 1755 636 O ATOM 264 OE2 GLU A 499 3.894 9.059 45.259 1.00 49.59 O ANISOU 264 OE2 GLU A 499 6404 7001 5438 1441 1716 723 O ATOM 265 N ALA A 500 6.762 8.963 50.125 1.00 42.27 N ANISOU 265 N ALA A 500 5996 6198 3866 1721 1649 586 N ATOM 266 CA ALA A 500 7.511 9.314 51.324 1.00 44.04 C ANISOU 266 CA ALA A 500 6368 6439 3924 1794 1600 519 C ATOM 267 C ALA A 500 7.350 10.790 51.594 1.00 44.63 C ANISOU 267 C ALA A 500 6531 6492 3935 1855 1576 414 C ATOM 268 O ALA A 500 7.922 11.619 50.882 1.00 43.24 O ANISOU 268 O ALA A 500 6382 6283 3764 1815 1488 301 O ATOM 269 CB ALA A 500 8.984 8.961 51.165 1.00 42.72 C ANISOU 269 CB ALA A 500 6261 6274 3697 1741 1480 446 C ATOM 270 N VAL A 501 6.566 11.135 52.608 1.00 47.92 N ANISOU 270 N VAL A 501 6990 6923 4294 1953 1655 452 N ATOM 271 CA VAL A 501 6.340 12.545 52.864 1.00 50.19 C ANISOU 271 CA VAL A 501 7358 7185 4526 2014 1639 357 C ATOM 272 C VAL A 501 7.495 13.097 53.699 1.00 51.33 C ANISOU 272 C VAL A 501 7660 7326 4518 2052 1528 240 C ATOM 273 O VAL A 501 8.045 12.410 54.562 1.00 52.97 O ANISOU 273 O VAL A 501 7926 7563 4638 2080 1513 265 O ATOM 274 CB VAL A 501 4.967 12.801 53.552 1.00 41.08 C ANISOU 274 CB VAL A 501 6186 6044 3378 2108 1771 443 C ATOM 275 CG1 VAL A 501 3.862 12.044 52.834 1.00 39.26 C ANISOU 275 CG1 VAL A 501 5791 5818 3309 2065 1873 579 C ATOM 276 CG2 VAL A 501 4.991 12.390 54.972 1.00 43.40 C ANISOU 276 CG2 VAL A 501 6567 6374 3551 2201 1812 489 C ATOM 277 N GLY A 502 7.891 14.327 53.388 1.00 52.68 N ANISOU 277 N GLY A 502 7894 7456 4668 2047 1444 112 N ATOM 278 CA GLY A 502 8.993 14.983 54.068 1.00 54.77 C ANISOU 278 CA GLY A 502 8300 7702 4808 2072 1322 -8 C ATOM 279 C GLY A 502 10.397 14.410 53.907 1.00 59.47 C ANISOU 279 C GLY A 502 8925 8296 5373 2002 1198 -57 C ATOM 280 O GLY A 502 11.269 14.705 54.729 1.00 57.85 O ANISOU 280 O GLY A 502 8835 8085 5058 2034 1107 -129 O ATOM 281 N ILE A 503 10.633 13.611 52.866 1.00 62.57 N ANISOU 281 N ILE A 503 9216 8694 5863 1910 1191 -18 N ATOM 282 CA ILE A 503 11.972 13.065 52.635 1.00 67.34 C ANISOU 282 CA ILE A 503 9843 9296 6446 1843 1074 -61 C ATOM 283 C ILE A 503 12.863 14.157 52.055 1.00 67.63 C ANISOU 283 C ILE A 503 9930 9278 6488 1796 936 -204 C ATOM 284 O ILE A 503 14.086 14.087 52.134 1.00 68.15 O ANISOU 284 O ILE A 503 10050 9330 6513 1758 812 -269 O ATOM 285 CB ILE A 503 11.959 11.825 51.704 1.00 34.37 C ANISOU 285 CB ILE A 503 5545 5142 2373 1761 1113 29 C ATOM 286 CG1 ILE A 503 13.242 11.015 51.887 1.00 32.89 C ANISOU 286 CG1 ILE A 503 5394 4967 2135 1720 1018 16 C ATOM 287 CG2 ILE A 503 11.752 12.222 50.236 1.00 31.93 C ANISOU 287 CG2 ILE A 503 5146 4799 2188 1685 1103 -3 C ATOM 288 CD1 ILE A 503 13.043 9.512 51.855 1.00 32.68 C ANISOU 288 CD1 ILE A 503 5285 4982 2150 1696 1093 148 C ATOM 289 N ASP A 504 12.236 15.175 51.482 1.00 71.88 N ANISOU 289 N ASP A 504 10447 9781 7083 1798 955 -248 N ATOM 290 CA ASP A 504 12.915 16.430 51.217 1.00 75.00 C ANISOU 290 CA ASP A 504 10908 10118 7472 1778 833 -382 C ATOM 291 C ASP A 504 12.905 17.248 52.510 1.00 80.85 C ANISOU 291 C ASP A 504 11773 10849 8096 1870 811 -433 C ATOM 292 O ASP A 504 11.851 17.427 53.126 1.00 82.07 O ANISOU 292 O ASP A 504 11937 11024 8221 1952 921 -381 O ATOM 293 CB ASP A 504 12.235 17.188 50.079 1.00 76.31 C ANISOU 293 CB ASP A 504 11000 10248 7749 1745 863 -404 C ATOM 294 CG ASP A 504 13.103 18.293 49.515 1.00 76.91 C ANISOU 294 CG ASP A 504 11117 10257 7847 1695 724 -535 C ATOM 295 OD1 ASP A 504 13.907 18.871 50.281 1.00 77.88 O ANISOU 295 OD1 ASP A 504 11345 10356 7891 1717 622 -614 O ATOM 296 OD2 ASP A 504 12.986 18.580 48.303 1.00 76.30 O ANISOU 296 OD2 ASP A 504 10966 10151 7874 1634 715 -554 O ATOM 297 N LYS A 505 14.074 17.733 52.920 1.00 85.57 N ANISOU 297 N LYS A 505 12465 11414 8633 1858 669 -531 N ATOM 298 CA LYS A 505 14.228 18.412 54.210 1.00 90.91 C ANISOU 298 CA LYS A 505 13270 12081 9192 1944 632 -583 C ATOM 299 C LYS A 505 13.815 19.875 54.086 1.00 91.24 C ANISOU 299 C LYS A 505 13349 12068 9249 1973 615 -665 C ATOM 300 O LYS A 505 13.515 20.528 55.078 1.00 94.34 O ANISOU 300 O LYS A 505 13836 12455 9554 2061 628 -692 O ATOM 301 CB LYS A 505 15.677 18.313 54.741 1.00 91.95 C ANISOU 301 CB LYS A 505 13483 12197 9259 1918 478 -650 C ATOM 302 CG LYS A 505 16.390 16.946 54.597 1.00 90.98 C ANISOU 302 CG LYS A 505 13315 12113 9141 1864 457 -589 C ATOM 303 CD LYS A 505 16.739 16.575 53.147 1.00 88.48 C ANISOU 303 CD LYS A 505 12889 11782 8947 1753 428 -587 C ATOM 304 CE LYS A 505 17.131 15.111 53.017 1.00 87.29 C ANISOU 304 CE LYS A 505 12684 11680 8802 1715 448 -502 C ATOM 305 NZ LYS A 505 17.614 14.755 51.642 1.00 85.20 N ANISOU 305 NZ LYS A 505 12327 11399 8647 1611 405 -509 N ATOM 306 N ASP A 506 13.805 20.372 52.853 1.00 93.11 N ANISOU 306 N ASP A 506 13514 12265 9599 1899 587 -703 N ATOM 307 CA ASP A 506 13.388 21.740 52.553 1.00 93.77 C ANISOU 307 CA ASP A 506 13616 12293 9718 1915 574 -775 C ATOM 308 C ASP A 506 11.870 21.826 52.394 1.00 94.86 C ANISOU 308 C ASP A 506 13695 12456 9893 1971 734 -699 C ATOM 309 O ASP A 506 11.275 22.891 52.565 1.00 97.44 O ANISOU 309 O ASP A 506 14057 12751 10215 2022 757 -738 O ATOM 310 CB ASP A 506 14.086 22.249 51.283 1.00 91.95 C ANISOU 310 CB ASP A 506 13334 12005 9599 1810 468 -846 C ATOM 311 N LYS A 507 11.248 20.698 52.063 1.00 86.80 N ANISOU 311 N LYS A 507 12577 11488 8914 1958 844 -586 N ATOM 312 CA LYS A 507 9.797 20.625 51.923 1.00 79.99 C ANISOU 312 CA LYS A 507 11641 10652 8101 2006 999 -495 C ATOM 313 C LYS A 507 9.205 19.554 52.839 1.00 74.34 C ANISOU 313 C LYS A 507 10918 10002 7327 2070 1113 -376 C ATOM 314 O LYS A 507 8.727 18.528 52.361 1.00 73.22 O ANISOU 314 O LYS A 507 10669 9895 7254 2037 1195 -272 O ATOM 315 CB LYS A 507 9.416 20.331 50.474 1.00 75.14 C ANISOU 315 CB LYS A 507 10890 10031 7630 1923 1033 -456 C ATOM 316 CG LYS A 507 9.043 21.551 49.663 1.00 72.24 C ANISOU 316 CG LYS A 507 10501 9607 7341 1909 1014 -521 C ATOM 317 CD LYS A 507 8.059 21.166 48.562 1.00 70.56 C ANISOU 317 CD LYS A 507 10145 9405 7260 1872 1113 -437 C ATOM 318 CE LYS A 507 8.755 20.866 47.244 1.00 69.24 C ANISOU 318 CE LYS A 507 9907 9216 7184 1765 1038 -465 C ATOM 319 NZ LYS A 507 8.589 21.982 46.269 1.00 69.14 N ANISOU 319 NZ LYS A 507 9868 9143 7258 1736 1000 -532 N ATOM 320 N PRO A 508 9.219 19.801 54.161 1.00 69.91 N ANISOU 320 N PRO A 508 10470 9452 6639 2164 1119 -389 N ATOM 321 CA PRO A 508 8.903 18.802 55.193 1.00 67.07 C ANISOU 321 CA PRO A 508 10129 9152 6203 2229 1205 -289 C ATOM 322 C PRO A 508 7.490 18.227 55.140 1.00 64.03 C ANISOU 322 C PRO A 508 9642 8805 5881 2268 1375 -151 C ATOM 323 O PRO A 508 7.242 17.185 55.749 1.00 64.81 O ANISOU 323 O PRO A 508 9723 8952 5950 2299 1448 -49 O ATOM 324 CB PRO A 508 9.097 19.583 56.501 1.00 68.78 C ANISOU 324 CB PRO A 508 10497 9359 6279 2331 1171 -354 C ATOM 325 CG PRO A 508 9.992 20.716 56.144 1.00 68.81 C ANISOU 325 CG PRO A 508 10565 9298 6283 2288 1023 -498 C ATOM 326 CD PRO A 508 9.572 21.099 54.761 1.00 68.73 C ANISOU 326 CD PRO A 508 10445 9257 6414 2214 1037 -505 C ATOM 327 N LYS A 509 6.576 18.884 54.434 1.00 61.67 N ANISOU 327 N LYS A 509 9274 8484 5675 2265 1434 -143 N ATOM 328 CA LYS A 509 5.195 18.415 54.412 1.00 60.40 C ANISOU 328 CA LYS A 509 9013 8353 5584 2303 1591 -10 C ATOM 329 C LYS A 509 4.798 17.799 53.068 1.00 57.26 C ANISOU 329 C LYS A 509 8456 7954 5347 2205 1624 58 C ATOM 330 O LYS A 509 3.698 17.265 52.940 1.00 57.49 O ANISOU 330 O LYS A 509 8381 8005 5457 2219 1743 179 O ATOM 331 CB LYS A 509 4.245 19.557 54.773 1.00 62.10 C ANISOU 331 CB LYS A 509 9264 8548 5784 2390 1656 -27 C ATOM 332 N GLU A 510 5.690 17.858 52.079 1.00 53.97 N ANISOU 332 N GLU A 510 8017 7510 4979 2109 1516 -17 N ATOM 333 CA GLU A 510 5.369 17.390 50.724 1.00 51.01 C ANISOU 333 CA GLU A 510 7499 7128 4755 2017 1536 32 C ATOM 334 C GLU A 510 5.750 15.919 50.502 1.00 49.98 C ANISOU 334 C GLU A 510 7300 7033 4656 1955 1543 115 C ATOM 335 O GLU A 510 6.862 15.492 50.849 1.00 47.37 O ANISOU 335 O GLU A 510 7038 6713 4248 1935 1461 72 O ATOM 336 CB GLU A 510 6.055 18.287 49.671 1.00 49.42 C ANISOU 336 CB GLU A 510 7305 6874 4598 1948 1424 -91 C ATOM 337 N ALA A 511 4.815 15.157 49.924 1.00 50.18 N ANISOU 337 N ALA A 511 7187 7073 4805 1924 1638 236 N ATOM 338 CA ALA A 511 5.015 13.743 49.582 1.00 49.12 C ANISOU 338 CA ALA A 511 6967 6966 4729 1858 1654 328 C ATOM 339 C ALA A 511 5.841 13.582 48.317 1.00 44.21 C ANISOU 339 C ALA A 511 6300 6321 4175 1752 1563 269 C ATOM 340 O ALA A 511 5.588 14.241 47.310 1.00 44.41 O ANISOU 340 O ALA A 511 6273 6313 4287 1714 1546 229 O ATOM 341 CB ALA A 511 3.679 13.040 49.409 1.00 49.67 C ANISOU 341 CB ALA A 511 6901 7050 4922 1859 1779 479 C ATOM 342 N VAL A 512 6.818 12.687 48.368 1.00 42.63 N ANISOU 342 N VAL A 512 6119 6140 3939 1709 1508 270 N ATOM 343 CA VAL A 512 7.704 12.460 47.234 1.00 40.75 C ANISOU 343 CA VAL A 512 5848 5883 3753 1614 1421 216 C ATOM 344 C VAL A 512 7.570 11.041 46.709 1.00 41.13 C ANISOU 344 C VAL A 512 5772 5936 3919 1524 1436 328 C ATOM 345 O VAL A 512 7.645 10.091 47.484 1.00 40.59 O ANISOU 345 O VAL A 512 5717 5910 3796 1558 1488 406 O ATOM 346 CB VAL A 512 9.176 12.699 47.618 1.00 42.09 C ANISOU 346 CB VAL A 512 6140 6043 3808 1603 1288 102 C ATOM 347 CG1 VAL A 512 10.096 12.418 46.429 1.00 40.72 C ANISOU 347 CG1 VAL A 512 5903 5822 3748 1458 1153 57 C ATOM 348 CG2 VAL A 512 9.357 14.119 48.144 1.00 43.94 C ANISOU 348 CG2 VAL A 512 6491 6251 3955 1666 1236 -14 C ATOM 349 N THR A 513 7.378 10.881 45.405 1.00 40.65 N ANISOU 349 N THR A 513 5596 5830 4019 1411 1388 338 N ATOM 350 CA THR A 513 7.397 9.538 44.847 1.00 39.40 C ANISOU 350 CA THR A 513 5333 5666 3973 1319 1379 427 C ATOM 351 C THR A 513 8.825 8.994 44.837 1.00 37.69 C ANISOU 351 C THR A 513 5169 5442 3710 1259 1264 371 C ATOM 352 O THR A 513 9.749 9.630 44.319 1.00 35.40 O ANISOU 352 O THR A 513 4923 5118 3410 1210 1149 260 O ATOM 353 CB THR A 513 6.819 9.486 43.441 1.00 37.14 C ANISOU 353 CB THR A 513 4918 5331 3863 1218 1351 448 C ATOM 354 OG1 THR A 513 5.430 9.834 43.494 1.00 37.56 O ANISOU 354 OG1 THR A 513 4906 5393 3974 1273 1464 521 O ATOM 355 CG2 THR A 513 6.938 8.085 42.897 1.00 35.55 C ANISOU 355 CG2 THR A 513 4624 5116 3766 1124 1329 527 C ATOM 356 N VAL A 514 8.991 7.820 45.442 1.00 37.90 N ANISOU 356 N VAL A 514 5189 5500 3712 1267 1300 454 N ATOM 357 CA VAL A 514 10.288 7.181 45.581 1.00 37.15 C ANISOU 357 CA VAL A 514 5141 5404 3571 1222 1205 419 C ATOM 358 C VAL A 514 10.202 5.698 45.176 1.00 36.05 C ANISOU 358 C VAL A 514 4900 5257 3541 1148 1218 524 C ATOM 359 O VAL A 514 9.124 5.181 44.884 1.00 36.20 O ANISOU 359 O VAL A 514 4818 5273 3664 1135 1300 624 O ATOM 360 CB VAL A 514 10.836 7.293 47.048 1.00 28.69 C ANISOU 360 CB VAL A 514 4205 4383 2313 1330 1221 401 C ATOM 361 CG1 VAL A 514 10.888 8.728 47.510 1.00 29.20 C ANISOU 361 CG1 VAL A 514 4378 4450 2266 1411 1207 296 C ATOM 362 CG2 VAL A 514 9.992 6.491 48.002 1.00 29.81 C ANISOU 362 CG2 VAL A 514 4332 4578 2417 1411 1360 533 C ATOM 363 N ALA A 515 11.351 5.029 45.150 1.00 34.91 N ANISOU 363 N ALA A 515 4781 5104 3378 1098 1132 499 N ATOM 364 CA ALA A 515 11.423 3.592 44.940 1.00 33.98 C ANISOU 364 CA ALA A 515 4588 4980 3344 1039 1140 592 C ATOM 365 C ALA A 515 12.063 2.972 46.169 1.00 33.99 C ANISOU 365 C ALA A 515 4668 5026 3221 1102 1154 626 C ATOM 366 O ALA A 515 12.970 3.558 46.763 1.00 34.30 O ANISOU 366 O ALA A 515 4816 5081 3134 1143 1092 542 O ATOM 367 CB ALA A 515 12.215 3.262 43.696 1.00 32.65 C ANISOU 367 CB ALA A 515 4372 4756 3279 920 1026 539 C ATOM 368 N VAL A 516 11.588 1.798 46.567 1.00 34.21 N ANISOU 368 N VAL A 516 4641 5072 3285 1110 1231 752 N ATOM 369 CA VAL A 516 12.093 1.178 47.776 1.00 35.06 C ANISOU 369 CA VAL A 516 4822 5226 3274 1177 1255 800 C ATOM 370 C VAL A 516 12.567 -0.233 47.476 1.00 32.96 C ANISOU 370 C VAL A 516 4492 4938 3095 1103 1224 868 C ATOM 371 O VAL A 516 11.787 -1.070 47.024 1.00 31.53 O ANISOU 371 O VAL A 516 4204 4734 3043 1059 1279 966 O ATOM 372 CB VAL A 516 11.021 1.145 48.888 1.00 36.36 C ANISOU 372 CB VAL A 516 5002 5447 3365 1293 1405 904 C ATOM 373 CG1 VAL A 516 11.625 0.686 50.193 1.00 31.03 C ANISOU 373 CG1 VAL A 516 4427 4825 2537 1375 1422 938 C ATOM 374 CG2 VAL A 516 10.396 2.522 49.061 1.00 37.32 C ANISOU 374 CG2 VAL A 516 5174 5585 3423 1366 1448 842 C ATOM 375 N LYS A 517 13.851 -0.482 47.718 1.00 33.14 N ANISOU 375 N LYS A 517 4580 4960 3052 1088 1130 815 N ATOM 376 CA LYS A 517 14.426 -1.813 47.592 1.00 35.28 C ANISOU 376 CA LYS A 517 4807 5213 3386 1032 1100 877 C ATOM 377 C LYS A 517 14.333 -2.544 48.922 1.00 36.22 C ANISOU 377 C LYS A 517 4969 5385 3407 1117 1177 981 C ATOM 378 O LYS A 517 14.532 -1.943 49.981 1.00 38.97 O ANISOU 378 O LYS A 517 5426 5786 3595 1213 1193 956 O ATOM 379 CB LYS A 517 15.879 -1.725 47.125 1.00 34.74 C ANISOU 379 CB LYS A 517 4777 5114 3308 972 961 773 C ATOM 380 CG LYS A 517 16.505 -3.036 46.651 1.00 26.40 C ANISOU 380 CG LYS A 517 3661 4021 2349 896 916 819 C ATOM 381 CD LYS A 517 17.606 -2.742 45.645 1.00 25.27 C ANISOU 381 CD LYS A 517 3516 3831 2255 815 792 709 C ATOM 382 CE LYS A 517 18.329 -3.991 45.135 1.00 25.51 C ANISOU 382 CE LYS A 517 3495 3821 2377 744 745 743 C ATOM 383 NZ LYS A 517 19.314 -3.658 44.010 1.00 24.49 N ANISOU 383 NZ LYS A 517 3356 3643 2308 666 637 640 N ATOM 384 N MET A 518 14.026 -3.838 48.864 1.00 37.53 N ANISOU 384 N MET A 518 5055 5538 3669 1084 1222 1098 N ATOM 385 CA MET A 518 13.825 -4.638 50.076 1.00 40.28 C ANISOU 385 CA MET A 518 5428 5935 3942 1162 1308 1219 C ATOM 386 C MET A 518 13.921 -6.118 49.733 1.00 43.78 C ANISOU 386 C MET A 518 5782 6339 4515 1092 1306 1318 C ATOM 387 O MET A 518 14.003 -6.477 48.563 1.00 43.12 O ANISOU 387 O MET A 518 5617 6191 4576 990 1247 1292 O ATOM 388 CB MET A 518 12.467 -4.334 50.712 1.00 42.23 C ANISOU 388 CB MET A 518 5661 6223 4159 1249 1455 1309 C ATOM 389 CG MET A 518 11.305 -4.901 49.907 1.00 43.12 C ANISOU 389 CG MET A 518 5628 6294 4461 1186 1523 1404 C ATOM 390 SD MET A 518 9.689 -4.238 50.346 1.00 48.56 S ANISOU 390 SD MET A 518 6283 7021 5147 1275 1683 1485 S ATOM 391 CE MET A 518 9.954 -2.495 50.055 1.00 72.13 C ANISOU 391 CE MET A 518 9358 10013 8034 1302 1620 1311 C ATOM 392 N LEU A 519 13.900 -6.975 50.742 1.00 48.28 N ANISOU 392 N LEU A 519 6369 6945 5031 1149 1369 1431 N ATOM 393 CA LEU A 519 14.019 -8.404 50.504 1.00 51.82 C ANISOU 393 CA LEU A 519 6737 7353 5600 1088 1367 1528 C ATOM 394 C LEU A 519 12.645 -9.076 50.424 1.00 57.21 C ANISOU 394 C LEU A 519 7307 8021 6411 1082 1487 1672 C ATOM 395 O LEU A 519 11.649 -8.520 50.894 1.00 57.18 O ANISOU 395 O LEU A 519 7300 8056 6369 1151 1592 1720 O ATOM 396 CB LEU A 519 14.860 -9.048 51.612 1.00 49.26 C ANISOU 396 CB LEU A 519 6489 7069 5157 1146 1359 1577 C ATOM 397 CG LEU A 519 16.278 -8.484 51.771 1.00 46.15 C ANISOU 397 CG LEU A 519 6202 6687 4644 1152 1232 1447 C ATOM 398 CD1 LEU A 519 16.905 -8.907 53.080 1.00 45.30 C ANISOU 398 CD1 LEU A 519 6186 6635 4389 1236 1237 1501 C ATOM 399 CD2 LEU A 519 17.160 -8.892 50.606 1.00 44.81 C ANISOU 399 CD2 LEU A 519 5980 6446 4599 1038 1114 1375 C ATOM 400 N LYS A 520 12.588 -10.257 49.809 1.00 64.16 N ANISOU 400 N LYS A 520 8089 8838 7449 999 1469 1741 N ATOM 401 CA LYS A 520 11.446 -11.155 49.995 1.00 72.25 C ANISOU 401 CA LYS A 520 9011 9848 8592 1000 1579 1905 C ATOM 402 C LYS A 520 11.555 -11.778 51.380 1.00 82.61 C ANISOU 402 C LYS A 520 10370 11210 9808 1087 1642 2003 C ATOM 403 O LYS A 520 12.579 -11.644 52.020 1.00 85.26 O ANISOU 403 O LYS A 520 10811 11587 9996 1133 1599 1959 O ATOM 404 CB LYS A 520 11.406 -12.230 48.891 1.00 68.67 C ANISOU 404 CB LYS A 520 8447 9301 8343 880 1520 1932 C ATOM 405 CG LYS A 520 11.847 -11.741 47.544 1.00 64.36 C ANISOU 405 CG LYS A 520 7890 8698 7865 789 1401 1788 C ATOM 406 CD LYS A 520 10.746 -11.845 46.502 1.00 61.37 C ANISOU 406 CD LYS A 520 7395 8256 7665 716 1412 1815 C ATOM 407 CE LYS A 520 11.276 -11.502 45.122 1.00 58.41 C ANISOU 407 CE LYS A 520 7016 7822 7356 624 1289 1676 C ATOM 408 NZ LYS A 520 10.264 -11.779 44.065 1.00 57.49 N ANISOU 408 NZ LYS A 520 6788 7635 7421 546 1282 1706 N ATOM 409 N ASP A 521 10.527 -12.481 51.831 1.00 94.74 N ANISOU 409 N ASP A 521 11824 12730 11442 1103 1717 2115 N ATOM 410 CA ASP A 521 10.574 -13.065 53.158 1.00 99.73 C ANISOU 410 CA ASP A 521 12496 13400 11997 1184 1763 2189 C ATOM 411 C ASP A 521 11.561 -14.251 53.177 1.00 96.83 C ANISOU 411 C ASP A 521 12129 13006 11656 1141 1705 2229 C ATOM 412 O ASP A 521 12.185 -14.557 54.206 1.00 97.01 O ANISOU 412 O ASP A 521 12227 13071 11562 1204 1704 2249 O ATOM 413 CB ASP A 521 9.185 -13.490 53.603 1.00108.48 C ANISOU 413 CB ASP A 521 13510 14497 13209 1216 1862 2304 C ATOM 414 CG ASP A 521 8.361 -14.122 52.489 1.00116.07 C ANISOU 414 CG ASP A 521 14324 15376 14400 1115 1858 2361 C ATOM 415 OD1 ASP A 521 8.908 -14.405 51.408 1.00117.27 O ANISOU 415 OD1 ASP A 521 14446 15476 14635 1018 1780 2320 O ATOM 416 OD2 ASP A 521 7.136 -14.336 52.718 1.00119.15 O ANISOU 416 OD2 ASP A 521 14629 15752 14890 1137 1932 2449 O ATOM 417 N ASP A 522 11.722 -14.897 52.020 1.00 90.15 N ANISOU 417 N ASP A 522 11201 12086 10965 1033 1652 2238 N ATOM 418 CA ASP A 522 12.618 -16.045 51.869 1.00 85.91 C ANISOU 418 CA ASP A 522 10654 11507 10480 982 1593 2275 C ATOM 419 C ASP A 522 14.086 -15.667 51.682 1.00 79.59 C ANISOU 419 C ASP A 522 9957 10728 9557 977 1502 2182 C ATOM 420 O ASP A 522 14.895 -16.493 51.246 1.00 78.03 O ANISOU 420 O ASP A 522 9742 10476 9430 915 1422 2169 O ATOM 421 CB ASP A 522 12.162 -16.909 50.703 1.00 84.33 C ANISOU 421 CB ASP A 522 10329 11209 10504 870 1568 2318 C ATOM 422 CG ASP A 522 10.968 -17.789 51.057 1.00 84.78 C ANISOU 422 CG ASP A 522 10279 11233 10701 872 1636 2438 C ATOM 423 OD1 ASP A 522 10.622 -17.923 52.263 1.00 86.13 O ANISOU 423 OD1 ASP A 522 10472 11456 10797 960 1707 2504 O ATOM 424 OD2 ASP A 522 10.427 -18.419 50.116 1.00 83.98 O ANISOU 424 OD2 ASP A 522 10072 11047 10788 784 1611 2468 O ATOM 425 N ALA A 523 14.429 -14.428 52.017 1.00 74.18 N ANISOU 425 N ALA A 523 9371 10105 8709 1036 1484 2076 N ATOM 426 CA ALA A 523 15.815 -13.989 51.939 1.00 68.85 C ANISOU 426 CA ALA A 523 8789 9438 7934 1028 1360 1941 C ATOM 427 C ALA A 523 16.563 -14.501 53.162 1.00 66.41 C ANISOU 427 C ALA A 523 8560 9180 7493 1104 1363 2004 C ATOM 428 O ALA A 523 15.976 -14.627 54.238 1.00 67.26 O ANISOU 428 O ALA A 523 8689 9336 7533 1184 1449 2085 O ATOM 429 CB ALA A 523 15.904 -12.471 51.833 1.00 67.38 C ANISOU 429 CB ALA A 523 8676 9290 7635 1059 1328 1804 C ATOM 430 N THR A 524 17.851 -14.795 52.996 1.00 63.25 N ANISOU 430 N THR A 524 8196 8757 7077 1070 1249 1937 N ATOM 431 CA THR A 524 18.679 -15.289 54.095 1.00 61.96 C ANISOU 431 CA THR A 524 8109 8638 6793 1135 1231 1989 C ATOM 432 C THR A 524 19.344 -14.146 54.882 1.00 60.98 C ANISOU 432 C THR A 524 8122 8587 6460 1216 1182 1891 C ATOM 433 O THR A 524 19.108 -12.971 54.608 1.00 58.62 O ANISOU 433 O THR A 524 7858 8305 6112 1225 1171 1788 O ATOM 434 CB THR A 524 19.774 -16.258 53.573 1.00 56.79 C ANISOU 434 CB THR A 524 7422 7920 6236 1062 1131 1976 C ATOM 435 OG1 THR A 524 20.851 -15.513 52.991 1.00 54.62 O ANISOU 435 OG1 THR A 524 7191 7631 5930 1025 1005 1819 O ATOM 436 CG2 THR A 524 19.200 -17.222 52.535 1.00 57.29 C ANISOU 436 CG2 THR A 524 7356 7894 6516 967 1151 2031 C ATOM 437 N GLU A 525 20.164 -14.500 55.867 1.00 63.32 N ANISOU 437 N GLU A 525 8499 8924 6636 1276 1149 1924 N ATOM 438 CA GLU A 525 20.920 -13.511 56.621 1.00 65.56 C ANISOU 438 CA GLU A 525 8916 9268 6726 1349 1079 1829 C ATOM 439 C GLU A 525 21.914 -12.862 55.673 1.00 59.89 C ANISOU 439 C GLU A 525 8200 8504 6052 1271 937 1669 C ATOM 440 O GLU A 525 22.135 -11.654 55.707 1.00 60.19 O ANISOU 440 O GLU A 525 8310 8566 5994 1295 887 1551 O ATOM 441 CB GLU A 525 21.629 -14.153 57.825 1.00 71.15 C ANISOU 441 CB GLU A 525 9690 10008 7338 1407 1047 1878 C ATOM 442 CG GLU A 525 23.060 -13.633 58.112 1.00 69.93 C ANISOU 442 CG GLU A 525 9640 9875 7055 1427 903 1781 C ATOM 443 CD GLU A 525 23.754 -14.332 59.307 1.00 70.14 C ANISOU 443 CD GLU A 525 9724 9927 6999 1478 865 1832 C ATOM 444 OE1 GLU A 525 23.050 -14.818 60.223 1.00 70.54 O ANISOU 444 OE1 GLU A 525 9774 10001 7027 1529 956 1915 O ATOM 445 OE2 GLU A 525 25.008 -14.384 59.334 1.00 70.64 O ANISOU 445 OE2 GLU A 525 9830 9987 7021 1468 741 1791 O ATOM 446 N LYS A 526 22.493 -13.673 54.800 1.00 57.38 N ANISOU 446 N LYS A 526 7799 8117 5886 1179 877 1667 N ATOM 447 CA LYS A 526 23.481 -13.182 53.858 1.00 55.80 C ANISOU 447 CA LYS A 526 7590 7871 5741 1105 751 1530 C ATOM 448 C LYS A 526 22.844 -12.253 52.831 1.00 55.72 C ANISOU 448 C LYS A 526 7541 7834 5796 1055 762 1438 C ATOM 449 O LYS A 526 23.469 -11.292 52.383 1.00 54.33 O ANISOU 449 O LYS A 526 7398 7649 5595 1032 674 1310 O ATOM 450 CB LYS A 526 24.169 -14.346 53.157 1.00 57.53 C ANISOU 450 CB LYS A 526 7728 8021 6109 1026 702 1560 C ATOM 451 CG LYS A 526 25.313 -13.922 52.262 1.00 58.78 C ANISOU 451 CG LYS A 526 7880 8135 6319 959 576 1432 C ATOM 452 CD LYS A 526 26.019 -15.110 51.642 1.00 59.56 C ANISOU 452 CD LYS A 526 7907 8168 6556 895 535 1466 C ATOM 453 CE LYS A 526 27.037 -14.629 50.627 1.00 58.88 C ANISOU 453 CE LYS A 526 7805 8036 6532 829 429 1342 C ATOM 454 NZ LYS A 526 26.398 -13.735 49.607 1.00 57.81 N ANISOU 454 NZ LYS A 526 7640 7879 6448 783 443 1254 N ATOM 455 N ASP A 527 21.602 -12.542 52.458 1.00 55.40 N ANISOU 455 N ASP A 527 7426 7777 5847 1038 867 1507 N ATOM 456 CA ASP A 527 20.862 -11.692 51.535 1.00 53.87 C ANISOU 456 CA ASP A 527 7193 7561 5716 997 885 1434 C ATOM 457 C ASP A 527 20.725 -10.297 52.106 1.00 52.07 C ANISOU 457 C ASP A 527 7060 7391 5333 1068 886 1354 C ATOM 458 O ASP A 527 20.661 -9.319 51.370 1.00 50.04 O ANISOU 458 O ASP A 527 6801 7117 5097 1035 849 1248 O ATOM 459 CB ASP A 527 19.476 -12.271 51.258 1.00 54.49 C ANISOU 459 CB ASP A 527 7177 7618 5907 980 1002 1543 C ATOM 460 CG ASP A 527 19.498 -13.389 50.242 1.00 53.85 C ANISOU 460 CG ASP A 527 6990 7454 6014 884 982 1580 C ATOM 461 OD1 ASP A 527 19.950 -13.129 49.104 1.00 52.25 O ANISOU 461 OD1 ASP A 527 6759 7199 5893 807 902 1478 O ATOM 462 OD2 ASP A 527 19.064 -14.519 50.579 1.00 54.81 O ANISOU 462 OD2 ASP A 527 7061 7562 6201 887 1045 1710 O ATOM 463 N LEU A 528 20.672 -10.224 53.430 1.00 51.88 N ANISOU 463 N LEU A 528 7124 7435 5153 1171 928 1408 N ATOM 464 CA LEU A 528 20.487 -8.965 54.139 1.00 51.25 C ANISOU 464 CA LEU A 528 7150 7413 4909 1256 937 1340 C ATOM 465 C LEU A 528 21.777 -8.154 54.207 1.00 50.47 C ANISOU 465 C LEU A 528 7138 7315 4722 1254 793 1205 C ATOM 466 O LEU A 528 21.777 -6.941 53.985 1.00 51.84 O ANISOU 466 O LEU A 528 7357 7491 4848 1261 755 1094 O ATOM 467 CB LEU A 528 19.964 -9.224 55.551 1.00 50.36 C ANISOU 467 CB LEU A 528 7110 7374 4652 1375 1037 1450 C ATOM 468 CG LEU A 528 19.925 -7.999 56.461 1.00 49.20 C ANISOU 468 CG LEU A 528 7098 7289 4305 1480 1037 1379 C ATOM 469 CD1 LEU A 528 18.942 -6.971 55.923 1.00 47.21 C ANISOU 469 CD1 LEU A 528 6825 7032 4081 1481 1096 1323 C ATOM 470 CD2 LEU A 528 19.577 -8.402 57.893 1.00 50.66 C ANISOU 470 CD2 LEU A 528 7332 7513 4404 1568 1098 1449 C ATOM 471 N SER A 529 22.876 -8.829 54.523 1.00 50.92 N ANISOU 471 N SER A 529 7216 7368 4765 1244 711 1219 N ATOM 472 CA SER A 529 24.165 -8.163 54.609 1.00 50.89 C ANISOU 472 CA SER A 529 7282 7360 4694 1238 566 1104 C ATOM 473 C SER A 529 24.550 -7.641 53.231 1.00 50.67 C ANISOU 473 C SER A 529 7186 7267 4797 1137 493 996 C ATOM 474 O SER A 529 25.222 -6.625 53.110 1.00 49.66 O ANISOU 474 O SER A 529 7110 7133 4623 1131 397 880 O ATOM 475 CB SER A 529 25.229 -9.111 55.149 1.00 52.58 C ANISOU 475 CB SER A 529 7513 7576 4890 1242 497 1156 C ATOM 476 OG SER A 529 25.505 -10.114 54.192 1.00 52.97 O ANISOU 476 OG SER A 529 7448 7563 5114 1150 488 1193 O ATOM 477 N ASP A 530 24.109 -8.335 52.190 1.00 49.97 N ANISOU 477 N ASP A 530 6984 7128 4873 1058 538 1036 N ATOM 478 CA ASP A 530 24.350 -7.879 50.825 1.00 48.68 C ANISOU 478 CA ASP A 530 6757 6906 4834 967 484 942 C ATOM 479 C ASP A 530 23.671 -6.546 50.547 1.00 43.97 C ANISOU 479 C ASP A 530 6186 6319 4201 980 503 859 C ATOM 480 O ASP A 530 24.283 -5.643 49.989 1.00 41.70 O ANISOU 480 O ASP A 530 5915 6009 3922 945 417 748 O ATOM 481 CB ASP A 530 23.871 -8.919 49.813 1.00 50.93 C ANISOU 481 CB ASP A 530 6924 7134 5291 889 534 1006 C ATOM 482 CG ASP A 530 24.730 -10.174 49.810 1.00 53.81 C ANISOU 482 CG ASP A 530 7256 7471 5720 859 494 1064 C ATOM 483 OD1 ASP A 530 25.868 -10.132 50.342 1.00 56.92 O ANISOU 483 OD1 ASP A 530 7704 7879 6045 881 408 1036 O ATOM 484 OD2 ASP A 530 24.263 -11.203 49.267 1.00 57.37 O ANISOU 484 OD2 ASP A 530 7624 7880 6294 814 545 1138 O ATOM 485 N LEU A 531 22.404 -6.438 50.934 1.00 40.31 N ANISOU 485 N LEU A 531 5724 5887 3705 1030 618 919 N ATOM 486 CA LEU A 531 21.635 -5.204 50.778 1.00 36.69 C ANISOU 486 CA LEU A 531 5291 5442 3207 1056 652 853 C ATOM 487 C LEU A 531 22.171 -4.061 51.642 1.00 35.45 C ANISOU 487 C LEU A 531 5261 5324 2884 1130 589 764 C ATOM 488 O LEU A 531 22.137 -2.899 51.235 1.00 35.26 O ANISOU 488 O LEU A 531 5262 5288 2849 1122 552 662 O ATOM 489 CB LEU A 531 20.163 -5.446 51.117 1.00 34.53 C ANISOU 489 CB LEU A 531 4986 5196 2936 1104 798 955 C ATOM 490 CG LEU A 531 19.238 -4.244 50.924 1.00 32.49 C ANISOU 490 CG LEU A 531 4742 4949 2652 1133 848 901 C ATOM 491 CD1 LEU A 531 19.450 -3.617 49.551 1.00 30.06 C ANISOU 491 CD1 LEU A 531 4379 4583 2459 1039 777 799 C ATOM 492 CD2 LEU A 531 17.785 -4.654 51.118 1.00 32.29 C ANISOU 492 CD2 LEU A 531 4659 4943 2667 1168 996 1019 C ATOM 493 N VAL A 532 22.659 -4.385 52.836 1.00 36.32 N ANISOU 493 N VAL A 532 5456 5480 2866 1203 573 802 N ATOM 494 CA VAL A 532 23.289 -3.371 53.675 1.00 36.39 C ANISOU 494 CA VAL A 532 5593 5519 2715 1271 492 712 C ATOM 495 C VAL A 532 24.555 -2.827 53.006 1.00 37.47 C ANISOU 495 C VAL A 532 5727 5607 2902 1199 339 596 C ATOM 496 O VAL A 532 24.765 -1.618 52.954 1.00 39.67 O ANISOU 496 O VAL A 532 6063 5878 3131 1209 276 487 O ATOM 497 CB VAL A 532 23.648 -3.913 55.055 1.00 36.81 C ANISOU 497 CB VAL A 532 5739 5628 2621 1361 491 777 C ATOM 498 CG1 VAL A 532 24.337 -2.830 55.865 1.00 37.56 C ANISOU 498 CG1 VAL A 532 5973 5746 2553 1427 388 672 C ATOM 499 CG2 VAL A 532 22.407 -4.416 55.756 1.00 37.43 C ANISOU 499 CG2 VAL A 532 5821 5756 2645 1439 650 900 C ATOM 500 N SER A 533 25.380 -3.723 52.477 1.00 38.31 N ANISOU 500 N SER A 533 5763 5678 3114 1126 283 622 N ATOM 501 CA SER A 533 26.604 -3.333 51.796 1.00 38.82 C ANISOU 501 CA SER A 533 5810 5696 3244 1056 149 530 C ATOM 502 C SER A 533 26.331 -2.450 50.588 1.00 38.42 C ANISOU 502 C SER A 533 5707 5601 3291 991 142 446 C ATOM 503 O SER A 533 26.985 -1.426 50.407 1.00 38.53 O ANISOU 503 O SER A 533 5757 5595 3288 977 47 343 O ATOM 504 CB SER A 533 27.384 -4.572 51.369 1.00 38.23 C ANISOU 504 CB SER A 533 5657 5589 3278 995 118 589 C ATOM 505 OG SER A 533 27.720 -5.361 52.502 1.00 38.68 O ANISOU 505 OG SER A 533 5766 5687 3245 1055 114 667 O ATOM 506 N GLU A 534 25.370 -2.850 49.762 1.00 38.06 N ANISOU 506 N GLU A 534 5574 5537 3350 950 238 492 N ATOM 507 CA GLU A 534 24.956 -2.056 48.608 1.00 37.19 C ANISOU 507 CA GLU A 534 5413 5387 3329 893 243 423 C ATOM 508 C GLU A 534 24.522 -0.653 49.046 1.00 37.39 C ANISOU 508 C GLU A 534 5520 5435 3251 951 241 346 C ATOM 509 O GLU A 534 24.837 0.334 48.386 1.00 36.14 O ANISOU 509 O GLU A 534 5361 5243 3126 914 178 251 O ATOM 510 CB GLU A 534 23.825 -2.760 47.845 1.00 37.36 C ANISOU 510 CB GLU A 534 5339 5392 3463 855 351 498 C ATOM 511 CG GLU A 534 23.232 -1.932 46.716 1.00 37.61 C ANISOU 511 CG GLU A 534 5324 5390 3576 805 364 436 C ATOM 512 CD GLU A 534 22.056 -2.613 46.004 1.00 38.45 C ANISOU 512 CD GLU A 534 5339 5478 3793 770 462 510 C ATOM 513 OE1 GLU A 534 21.759 -3.791 46.326 1.00 38.73 O ANISOU 513 OE1 GLU A 534 5340 5520 3855 775 518 612 O ATOM 514 OE2 GLU A 534 21.443 -1.957 45.117 1.00 39.35 O ANISOU 514 OE2 GLU A 534 5415 5567 3970 734 477 469 O ATOM 515 N MET A 535 23.824 -0.561 50.175 1.00 38.61 N ANISOU 515 N MET A 535 5749 5643 3277 1047 310 386 N ATOM 516 CA MET A 535 23.419 0.747 50.680 1.00 38.84 C ANISOU 516 CA MET A 535 5868 5692 3196 1114 311 311 C ATOM 517 C MET A 535 24.617 1.587 51.112 1.00 40.02 C ANISOU 517 C MET A 535 6108 5833 3266 1127 168 207 C ATOM 518 O MET A 535 24.678 2.782 50.820 1.00 39.20 O ANISOU 518 O MET A 535 6036 5704 3154 1122 118 109 O ATOM 519 CB MET A 535 22.455 0.616 51.849 1.00 39.17 C ANISOU 519 CB MET A 535 5978 5798 3108 1224 422 382 C ATOM 520 CG MET A 535 22.193 1.935 52.550 1.00 39.02 C ANISOU 520 CG MET A 535 6075 5800 2949 1311 413 299 C ATOM 521 SD MET A 535 21.189 1.713 54.023 1.00 48.86 S ANISOU 521 SD MET A 535 7415 7126 4025 1456 547 388 S ATOM 522 CE MET A 535 22.119 0.443 54.895 1.00 39.34 C ANISOU 522 CE MET A 535 6240 5951 2756 1474 503 469 C ATOM 523 N GLU A 536 25.567 0.972 51.811 1.00 41.71 N ANISOU 523 N GLU A 536 6361 6061 3425 1143 98 230 N ATOM 524 CA GLU A 536 26.744 1.702 52.255 1.00 43.68 C ANISOU 524 CA GLU A 536 6691 6297 3607 1152 -50 137 C ATOM 525 C GLU A 536 27.598 2.155 51.067 1.00 41.63 C ANISOU 525 C GLU A 536 6358 5973 3488 1049 -148 63 C ATOM 526 O GLU A 536 28.176 3.242 51.097 1.00 42.51 O ANISOU 526 O GLU A 536 6520 6058 3573 1047 -250 -36 O ATOM 527 CB GLU A 536 27.565 0.860 53.229 1.00 47.11 C ANISOU 527 CB GLU A 536 7174 6761 3964 1188 -106 189 C ATOM 528 CG GLU A 536 26.844 0.567 54.547 1.00 50.86 C ANISOU 528 CG GLU A 536 7746 7305 4274 1304 -21 255 C ATOM 529 CD GLU A 536 26.513 1.829 55.340 1.00 53.90 C ANISOU 529 CD GLU A 536 8265 7711 4503 1395 -39 170 C ATOM 530 OE1 GLU A 536 27.329 2.776 55.334 1.00 56.15 O ANISOU 530 OE1 GLU A 536 8603 7963 4768 1381 -173 60 O ATOM 531 OE2 GLU A 536 25.438 1.872 55.978 1.00 56.24 O ANISOU 531 OE2 GLU A 536 8614 8056 4701 1483 81 216 O ATOM 532 N MET A 537 27.657 1.343 50.016 1.00 39.17 N ANISOU 532 N MET A 537 5928 5631 3322 967 -116 111 N ATOM 533 CA MET A 537 28.323 1.771 48.787 1.00 37.25 C ANISOU 533 CA MET A 537 5611 5328 3213 874 -185 49 C ATOM 534 C MET A 537 27.737 3.089 48.296 1.00 35.93 C ANISOU 534 C MET A 537 5460 5142 3051 871 -177 -33 C ATOM 535 O MET A 537 28.473 4.016 47.987 1.00 35.28 O ANISOU 535 O MET A 537 5390 5022 2992 841 -276 -118 O ATOM 536 CB MET A 537 28.214 0.715 47.679 1.00 36.19 C ANISOU 536 CB MET A 537 5357 5168 3226 798 -127 114 C ATOM 537 CG MET A 537 29.218 -0.438 47.787 1.00 36.43 C ANISOU 537 CG MET A 537 5352 5191 3298 772 -173 169 C ATOM 538 SD MET A 537 30.931 0.124 47.971 1.00 40.02 S ANISOU 538 SD MET A 537 5834 5617 3754 750 -343 96 S ATOM 539 CE MET A 537 31.084 1.293 46.628 1.00 32.58 C ANISOU 539 CE MET A 537 4839 4618 2920 678 -378 3 C ATOM 540 N MET A 538 26.409 3.174 48.257 1.00 35.49 N ANISOU 540 N MET A 538 5399 5108 2977 904 -59 -3 N ATOM 541 CA MET A 538 25.727 4.377 47.779 1.00 34.51 C ANISOU 541 CA MET A 538 5284 4966 2862 905 -39 -71 C ATOM 542 C MET A 538 25.949 5.603 48.685 1.00 34.62 C ANISOU 542 C MET A 538 5419 4987 2748 975 -109 -159 C ATOM 543 O MET A 538 25.966 6.733 48.207 1.00 34.51 O ANISOU 543 O MET A 538 5414 4937 2761 956 -151 -242 O ATOM 544 CB MET A 538 24.230 4.099 47.625 1.00 33.90 C ANISOU 544 CB MET A 538 5171 4914 2796 931 106 -5 C ATOM 545 CG MET A 538 23.912 2.958 46.670 1.00 32.61 C ANISOU 545 CG MET A 538 4890 4733 2765 859 167 75 C ATOM 546 SD MET A 538 22.142 2.609 46.581 1.00 45.11 S ANISOU 546 SD MET A 538 6426 6342 4371 890 327 161 S ATOM 547 CE MET A 538 21.630 3.965 45.525 1.00 24.26 C ANISOU 547 CE MET A 538 3760 3663 1794 854 319 74 C ATOM 548 N LYS A 539 26.124 5.377 49.984 1.00 34.56 N ANISOU 548 N LYS A 539 5508 5022 2601 1056 -123 -143 N ATOM 549 CA LYS A 539 26.499 6.451 50.904 1.00 34.65 C ANISOU 549 CA LYS A 539 5647 5035 2484 1124 -210 -232 C ATOM 550 C LYS A 539 27.894 7.000 50.591 1.00 34.62 C ANISOU 550 C LYS A 539 5642 4978 2535 1062 -375 -313 C ATOM 551 O LYS A 539 28.102 8.213 50.518 1.00 34.02 O ANISOU 551 O LYS A 539 5612 4865 2448 1063 -450 -409 O ATOM 552 CB LYS A 539 26.467 5.962 52.347 1.00 35.10 C ANISOU 552 CB LYS A 539 5809 5150 2375 1225 -197 -190 C ATOM 553 CG LYS A 539 25.104 5.585 52.865 1.00 35.43 C ANISOU 553 CG LYS A 539 5872 5249 2342 1305 -35 -111 C ATOM 554 CD LYS A 539 25.195 5.271 54.358 1.00 36.73 C ANISOU 554 CD LYS A 539 6162 5471 2324 1415 -34 -81 C ATOM 555 CE LYS A 539 23.947 4.593 54.887 1.00 37.16 C ANISOU 555 CE LYS A 539 6216 5585 2317 1491 138 29 C ATOM 556 NZ LYS A 539 24.091 4.254 56.326 1.00 38.56 N ANISOU 556 NZ LYS A 539 6488 5800 2364 1575 137 64 N ATOM 557 N MET A 540 28.841 6.083 50.410 1.00 34.98 N ANISOU 557 N MET A 540 5630 5015 2645 1009 -430 -269 N ATOM 558 CA MET A 540 30.231 6.422 50.139 1.00 35.79 C ANISOU 558 CA MET A 540 5716 5070 2813 949 -581 -325 C ATOM 559 C MET A 540 30.441 7.071 48.769 1.00 35.54 C ANISOU 559 C MET A 540 5593 4978 2933 859 -603 -371 C ATOM 560 O MET A 540 31.262 7.975 48.629 1.00 36.71 O ANISOU 560 O MET A 540 5756 5080 3113 830 -721 -448 O ATOM 561 CB MET A 540 31.092 5.167 50.253 1.00 34.86 C ANISOU 561 CB MET A 540 5549 4962 2735 920 -613 -251 C ATOM 562 CG MET A 540 32.418 5.254 49.521 1.00 33.97 C ANISOU 562 CG MET A 540 5363 4793 2751 834 -730 -279 C ATOM 563 SD MET A 540 33.411 3.754 49.697 1.00 68.57 S ANISOU 563 SD MET A 540 9687 9187 7180 809 -762 -188 S ATOM 564 CE MET A 540 33.669 3.712 51.469 1.00 43.20 C ANISOU 564 CE MET A 540 6618 6022 3776 911 -835 -188 C ATOM 565 N ILE A 541 29.704 6.610 47.759 1.00 35.69 N ANISOU 565 N ILE A 541 5518 4996 3047 815 -492 -323 N ATOM 566 CA ILE A 541 29.920 7.080 46.387 1.00 35.59 C ANISOU 566 CA ILE A 541 5415 4929 3177 729 -506 -355 C ATOM 567 C ILE A 541 29.576 8.563 46.279 1.00 36.93 C ANISOU 567 C ILE A 541 5633 5071 3328 743 -535 -445 C ATOM 568 O ILE A 541 30.254 9.328 45.590 1.00 36.05 O ANISOU 568 O ILE A 541 5488 4906 3302 687 -614 -500 O ATOM 569 CB ILE A 541 29.081 6.293 45.364 1.00 35.96 C ANISOU 569 CB ILE A 541 5366 4981 3317 686 -383 -287 C ATOM 570 CG1 ILE A 541 29.508 4.820 45.290 1.00 35.71 C ANISOU 570 CG1 ILE A 541 5276 4963 3329 661 -360 -202 C ATOM 571 CG2 ILE A 541 29.215 6.910 43.998 1.00 35.87 C ANISOU 571 CG2 ILE A 541 5280 4919 3431 611 -395 -326 C ATOM 572 CD1 ILE A 541 30.655 4.533 44.367 1.00 35.18 C ANISOU 572 CD1 ILE A 541 5129 4851 3387 582 -426 -204 C ATOM 573 N GLY A 542 28.526 8.968 46.986 1.00 38.11 N ANISOU 573 N GLY A 542 5860 5253 3367 822 -469 -456 N ATOM 574 CA GLY A 542 28.112 10.354 46.976 1.00 39.01 C ANISOU 574 CA GLY A 542 6028 5340 3452 847 -489 -541 C ATOM 575 C GLY A 542 27.238 10.655 45.776 1.00 37.97 C ANISOU 575 C GLY A 542 5816 5190 3422 802 -402 -533 C ATOM 576 O GLY A 542 26.919 9.769 44.978 1.00 37.78 O ANISOU 576 O GLY A 542 5699 5173 3482 754 -327 -463 O ATOM 577 N LYS A 543 26.867 11.922 45.638 1.00 37.61 N ANISOU 577 N LYS A 543 5807 5113 3368 818 -419 -606 N ATOM 578 CA LYS A 543 25.840 12.303 44.693 1.00 36.91 C ANISOU 578 CA LYS A 543 5661 5014 3350 797 -329 -598 C ATOM 579 C LYS A 543 26.465 12.712 43.374 1.00 35.12 C ANISOU 579 C LYS A 543 5348 4730 3267 700 -383 -623 C ATOM 580 O LYS A 543 27.543 13.292 43.351 1.00 34.02 O ANISOU 580 O LYS A 543 5221 4548 3156 670 -499 -677 O ATOM 581 CB LYS A 543 24.982 13.433 45.275 1.00 40.39 C ANISOU 581 CB LYS A 543 6189 5455 3703 876 -302 -657 C ATOM 582 CG LYS A 543 24.245 13.038 46.572 1.00 44.66 C ANISOU 582 CG LYS A 543 6818 6057 4093 984 -226 -624 C ATOM 583 CD LYS A 543 22.913 13.775 46.752 1.00 47.48 C ANISOU 583 CD LYS A 543 7213 6427 4401 1055 -127 -637 C ATOM 584 CE LYS A 543 22.846 15.051 45.902 1.00 48.23 C ANISOU 584 CE LYS A 543 7288 6460 4576 1017 -168 -713 C ATOM 585 NZ LYS A 543 21.451 15.480 45.564 1.00 51.07 N ANISOU 585 NZ LYS A 543 7624 6828 4951 1052 -50 -694 N ATOM 586 N HIS A 544 25.788 12.366 42.283 1.00 33.01 N ANISOU 586 N HIS A 544 4992 4461 3090 654 -300 -577 N ATOM 587 CA HIS A 544 26.171 12.764 40.932 1.00 30.56 C ANISOU 587 CA HIS A 544 4602 4101 2909 570 -329 -593 C ATOM 588 C HIS A 544 24.927 12.696 40.078 1.00 30.71 C ANISOU 588 C HIS A 544 4564 4127 2977 558 -223 -556 C ATOM 589 O HIS A 544 24.050 11.867 40.324 1.00 30.94 O ANISOU 589 O HIS A 544 4581 4198 2977 587 -131 -494 O ATOM 590 CB HIS A 544 27.264 11.866 40.348 1.00 27.31 C ANISOU 590 CB HIS A 544 4121 3677 2578 501 -370 -555 C ATOM 591 CG HIS A 544 27.792 12.336 39.026 1.00 23.87 C ANISOU 591 CG HIS A 544 3613 3191 2266 424 -404 -572 C ATOM 592 ND1 HIS A 544 27.263 11.928 37.823 1.00 21.47 N ANISOU 592 ND1 HIS A 544 3233 2883 2043 378 -333 -532 N ATOM 593 CD2 HIS A 544 28.805 13.183 38.719 1.00 21.91 C ANISOU 593 CD2 HIS A 544 3358 2893 2072 388 -500 -621 C ATOM 594 CE1 HIS A 544 27.923 12.500 36.832 1.00 20.15 C ANISOU 594 CE1 HIS A 544 3020 2670 1966 320 -378 -555 C ATOM 595 NE2 HIS A 544 28.860 13.273 37.352 1.00 21.30 N ANISOU 595 NE2 HIS A 544 3203 2787 2104 324 -477 -606 N ATOM 596 N LYS A 545 24.849 13.556 39.071 1.00 31.24 N ANISOU 596 N LYS A 545 4594 4152 3124 515 -237 -590 N ATOM 597 CA LYS A 545 23.643 13.666 38.258 1.00 32.64 C ANISOU 597 CA LYS A 545 4723 4331 3347 505 -150 -563 C ATOM 598 C LYS A 545 23.394 12.410 37.435 1.00 30.64 C ANISOU 598 C LYS A 545 4388 4093 3162 456 -91 -487 C ATOM 599 O LYS A 545 22.314 12.229 36.897 1.00 31.64 O ANISOU 599 O LYS A 545 4474 4228 3321 452 -16 -451 O ATOM 600 CB LYS A 545 23.731 14.882 37.332 1.00 36.30 C ANISOU 600 CB LYS A 545 5167 4742 3883 468 -189 -614 C ATOM 601 CG LYS A 545 24.965 14.883 36.433 1.00 40.24 C ANISOU 601 CG LYS A 545 5616 5201 4473 391 -263 -623 C ATOM 602 CD LYS A 545 25.174 16.231 35.746 1.00 43.85 C ANISOU 602 CD LYS A 545 6067 5604 4989 364 -313 -677 C ATOM 603 CE LYS A 545 26.650 16.434 35.391 1.00 47.33 C ANISOU 603 CE LYS A 545 6484 6003 5494 310 -408 -696 C ATOM 604 NZ LYS A 545 26.932 17.802 34.870 1.00 52.71 N ANISOU 604 NZ LYS A 545 7165 6628 6236 287 -464 -746 N ATOM 605 N ASN A 546 24.391 11.542 37.325 1.00 29.04 N ANISOU 605 N ASN A 546 4160 3889 2985 418 -129 -464 N ATOM 606 CA ASN A 546 24.226 10.338 36.522 1.00 26.12 C ANISOU 606 CA ASN A 546 3719 3525 2680 372 -80 -399 C ATOM 607 C ASN A 546 24.311 9.042 37.332 1.00 25.31 C ANISOU 607 C ASN A 546 3623 3460 2532 397 -52 -341 C ATOM 608 O ASN A 546 24.477 7.953 36.777 1.00 23.50 O ANISOU 608 O ASN A 546 3341 3229 2358 357 -32 -291 O ATOM 609 CB ASN A 546 25.246 10.343 35.389 1.00 25.97 C ANISOU 609 CB ASN A 546 3650 3466 2753 301 -133 -411 C ATOM 610 CG ASN A 546 24.918 11.386 34.327 1.00 25.58 C ANISOU 610 CG ASN A 546 3576 3382 2763 270 -137 -445 C ATOM 611 OD1 ASN A 546 25.749 12.225 33.976 1.00 25.73 O ANISOU 611 OD1 ASN A 546 3595 3365 2816 245 -201 -488 O ATOM 612 ND2 ASN A 546 23.687 11.337 33.819 1.00 25.22 N ANISOU 612 ND2 ASN A 546 3505 3343 2735 271 -68 -420 N ATOM 613 N ILE A 547 24.168 9.181 38.647 1.00 24.96 N ANISOU 613 N ILE A 547 3649 3449 2386 466 -51 -347 N ATOM 614 CA ILE A 547 24.050 8.056 39.567 1.00 25.14 C ANISOU 614 CA ILE A 547 3687 3513 2350 504 -12 -285 C ATOM 615 C ILE A 547 22.752 8.189 40.349 1.00 26.15 C ANISOU 615 C ILE A 547 3852 3680 2405 576 75 -258 C ATOM 616 O ILE A 547 22.455 9.276 40.850 1.00 25.74 O ANISOU 616 O ILE A 547 3860 3630 2290 625 66 -311 O ATOM 617 CB ILE A 547 25.237 8.000 40.546 1.00 24.94 C ANISOU 617 CB ILE A 547 3721 3496 2258 529 -94 -309 C ATOM 618 CG1 ILE A 547 26.507 7.526 39.816 1.00 23.53 C ANISOU 618 CG1 ILE A 547 3490 3285 2165 459 -162 -308 C ATOM 619 CG2 ILE A 547 24.913 7.104 41.727 1.00 25.09 C ANISOU 619 CG2 ILE A 547 3781 3566 2188 591 -48 -250 C ATOM 620 CD1 ILE A 547 27.732 7.529 40.692 1.00 23.58 C ANISOU 620 CD1 ILE A 547 3544 3293 2124 477 -256 -331 C ATOM 621 N ILE A 548 21.982 7.104 40.446 1.00 27.89 N ANISOU 621 N ILE A 548 4034 3927 2637 584 158 -175 N ATOM 622 CA ILE A 548 20.667 7.158 41.084 1.00 30.75 C ANISOU 622 CA ILE A 548 4412 4325 2947 650 255 -133 C ATOM 623 C ILE A 548 20.840 7.625 42.511 1.00 33.34 C ANISOU 623 C ILE A 548 4843 4688 3136 740 246 -158 C ATOM 624 O ILE A 548 21.787 7.238 43.190 1.00 35.16 O ANISOU 624 O ILE A 548 5118 4931 3311 753 189 -163 O ATOM 625 CB ILE A 548 19.922 5.797 41.055 1.00 21.72 C ANISOU 625 CB ILE A 548 3206 3202 1846 642 340 -28 C ATOM 626 CG1 ILE A 548 18.483 5.961 41.533 1.00 22.55 C ANISOU 626 CG1 ILE A 548 3308 3337 1922 704 447 22 C ATOM 627 CG2 ILE A 548 20.617 4.749 41.921 1.00 22.23 C ANISOU 627 CG2 ILE A 548 3296 3293 1858 663 329 19 C ATOM 628 CD1 ILE A 548 17.579 6.713 40.583 1.00 22.32 C ANISOU 628 CD1 ILE A 548 3231 3282 1969 679 474 4 C ATOM 629 N ASN A 549 19.931 8.475 42.963 1.00 36.19 N ANISOU 629 N ASN A 549 5246 5064 3439 805 298 -176 N ATOM 630 CA ASN A 549 20.091 9.144 44.240 1.00 38.63 C ANISOU 630 CA ASN A 549 5669 5400 3609 897 282 -221 C ATOM 631 C ASN A 549 19.627 8.310 45.436 1.00 39.16 C ANISOU 631 C ASN A 549 5777 5526 3577 977 361 -143 C ATOM 632 O ASN A 549 18.491 7.848 45.461 1.00 40.93 O ANISOU 632 O ASN A 549 5956 5774 3820 1002 474 -64 O ATOM 633 CB ASN A 549 19.328 10.457 44.195 1.00 43.73 C ANISOU 633 CB ASN A 549 6349 6033 4234 940 307 -277 C ATOM 634 CG ASN A 549 19.921 11.491 45.092 1.00 49.93 C ANISOU 634 CG ASN A 549 7253 6813 4905 1003 232 -369 C ATOM 635 OD1 ASN A 549 21.114 11.448 45.394 1.00 51.19 O ANISOU 635 OD1 ASN A 549 7454 6960 5035 985 128 -410 O ATOM 636 ND2 ASN A 549 19.101 12.439 45.528 1.00 55.18 N ANISOU 636 ND2 ASN A 549 7976 7483 5508 1079 281 -403 N ATOM 637 N LEU A 550 20.490 8.108 46.426 1.00 37.99 N ANISOU 637 N LEU A 550 5710 5399 3326 1018 303 -158 N ATOM 638 CA LEU A 550 20.050 7.481 47.680 1.00 37.56 C ANISOU 638 CA LEU A 550 5715 5404 3154 1109 379 -89 C ATOM 639 C LEU A 550 19.338 8.506 48.588 1.00 35.97 C ANISOU 639 C LEU A 550 5615 5227 2824 1221 427 -129 C ATOM 640 O LEU A 550 19.907 9.549 48.929 1.00 35.33 O ANISOU 640 O LEU A 550 5624 5126 2673 1249 340 -230 O ATOM 641 CB LEU A 550 21.229 6.850 48.424 1.00 36.61 C ANISOU 641 CB LEU A 550 5647 5298 2964 1117 297 -87 C ATOM 642 CG LEU A 550 20.872 6.151 49.742 1.00 36.53 C ANISOU 642 CG LEU A 550 5705 5352 2825 1213 370 -10 C ATOM 643 CD1 LEU A 550 19.917 5.003 49.497 1.00 35.61 C ANISOU 643 CD1 LEU A 550 5492 5257 2780 1201 497 117 C ATOM 644 CD2 LEU A 550 22.108 5.654 50.471 1.00 36.47 C ANISOU 644 CD2 LEU A 550 5756 5354 2745 1221 270 -18 C ATOM 645 N LEU A 551 18.099 8.217 48.981 1.00 35.56 N ANISOU 645 N LEU A 551 5550 5215 2746 1286 566 -48 N ATOM 646 CA LEU A 551 17.318 9.190 49.735 1.00 35.04 C ANISOU 646 CA LEU A 551 5573 5171 2569 1395 629 -81 C ATOM 647 C LEU A 551 17.378 8.918 51.223 1.00 37.34 C ANISOU 647 C LEU A 551 5983 5521 2686 1510 663 -54 C ATOM 648 O LEU A 551 17.350 9.853 52.028 1.00 35.62 O ANISOU 648 O LEU A 551 5872 5301 2361 1589 642 -122 O ATOM 649 CB LEU A 551 15.860 9.202 49.265 1.00 34.39 C ANISOU 649 CB LEU A 551 5405 5096 2565 1407 767 -10 C ATOM 650 CG LEU A 551 15.708 9.525 47.776 1.00 32.25 C ANISOU 650 CG LEU A 551 5024 4770 2461 1299 734 -37 C ATOM 651 CD1 LEU A 551 14.269 9.666 47.395 1.00 32.53 C ANISOU 651 CD1 LEU A 551 4985 4810 2565 1319 857 26 C ATOM 652 CD2 LEU A 551 16.472 10.780 47.432 1.00 31.19 C ANISOU 652 CD2 LEU A 551 4947 4587 2317 1276 614 -169 C ATOM 653 N GLY A 552 17.457 7.647 51.598 1.00 38.88 N ANISOU 653 N GLY A 552 6146 5752 2875 1509 705 49 N ATOM 654 CA GLY A 552 17.441 7.289 53.004 1.00 32.24 C ANISOU 654 CA GLY A 552 5400 4960 1891 1609 741 92 C ATOM 655 C GLY A 552 17.066 5.838 53.233 1.00 37.13 C ANISOU 655 C GLY A 552 5952 5621 2534 1610 839 237 C ATOM 656 O GLY A 552 16.908 5.077 52.271 1.00 36.72 O ANISOU 656 O GLY A 552 5777 5552 2623 1522 862 298 O ATOM 657 N ALA A 553 16.931 5.444 54.503 1.00 38.90 N ANISOU 657 N ALA A 553 6233 5877 2672 1684 875 291 N ATOM 658 CA ALA A 553 16.637 4.051 54.814 1.00 39.46 C ANISOU 658 CA ALA A 553 6244 5982 2767 1687 960 431 C ATOM 659 C ALA A 553 15.787 3.848 56.050 1.00 41.58 C ANISOU 659 C ALA A 553 6543 6282 2973 1783 1064 509 C ATOM 660 O ALA A 553 15.722 4.691 56.935 1.00 43.20 O ANISOU 660 O ALA A 553 6848 6488 3078 1859 1047 447 O ATOM 661 CB ALA A 553 17.926 3.270 54.967 1.00 39.75 C ANISOU 661 CB ALA A 553 6309 6026 2768 1651 857 432 C ATOM 662 N CYS A 554 15.136 2.695 56.078 1.00 43.08 N ANISOU 662 N CYS A 554 6644 6493 3230 1777 1170 648 N ATOM 663 CA CYS A 554 14.501 2.172 57.265 1.00 45.44 C ANISOU 663 CA CYS A 554 6963 6825 3477 1861 1264 744 C ATOM 664 C CYS A 554 15.304 0.961 57.710 1.00 46.49 C ANISOU 664 C CYS A 554 7101 6979 3585 1846 1230 810 C ATOM 665 O CYS A 554 15.190 -0.118 57.121 1.00 45.72 O ANISOU 665 O CYS A 554 6900 6879 3592 1784 1270 908 O ATOM 666 CB CYS A 554 13.050 1.777 56.988 1.00 46.37 C ANISOU 666 CB CYS A 554 6963 6945 3709 1868 1415 863 C ATOM 667 SG CYS A 554 11.961 3.117 56.470 1.00 68.01 S ANISOU 667 SG CYS A 554 9683 9661 6494 1889 1469 806 S ATOM 668 N THR A 555 16.130 1.137 58.733 1.00 48.07 N ANISOU 668 N THR A 555 7420 7194 3650 1900 1151 758 N ATOM 669 CA THR A 555 16.987 0.053 59.200 1.00 49.94 C ANISOU 669 CA THR A 555 7670 7450 3855 1888 1105 814 C ATOM 670 C THR A 555 16.535 -0.468 60.550 1.00 52.33 C ANISOU 670 C THR A 555 8016 7789 4078 1982 1186 901 C ATOM 671 O THR A 555 16.941 -1.551 60.969 1.00 53.91 O ANISOU 671 O THR A 555 8204 8008 4273 1978 1185 982 O ATOM 672 CB THR A 555 18.464 0.502 59.314 1.00 48.91 C ANISOU 672 CB THR A 555 7637 7307 3641 1866 933 694 C ATOM 673 OG1 THR A 555 18.574 1.574 60.260 1.00 51.27 O ANISOU 673 OG1 THR A 555 8061 7607 3814 1946 888 599 O ATOM 674 CG2 THR A 555 18.991 0.961 57.968 1.00 46.81 C ANISOU 674 CG2 THR A 555 7327 7004 3456 1773 850 612 C ATOM 675 N GLN A 556 15.683 0.305 61.216 1.00 54.80 N ANISOU 675 N GLN A 556 8378 8112 4332 2069 1256 886 N ATOM 676 CA GLN A 556 15.390 0.094 62.628 1.00 58.20 C ANISOU 676 CA GLN A 556 8884 8577 4651 2176 1314 939 C ATOM 677 C GLN A 556 14.004 -0.461 62.903 1.00 60.80 C ANISOU 677 C GLN A 556 9132 8925 5044 2224 1484 1077 C ATOM 678 O GLN A 556 13.016 0.030 62.354 1.00 62.18 O ANISOU 678 O GLN A 556 9243 9085 5298 2222 1561 1087 O ATOM 679 CB GLN A 556 15.563 1.406 63.386 1.00 59.41 C ANISOU 679 CB GLN A 556 9178 8727 4668 2256 1258 817 C ATOM 680 CG GLN A 556 16.955 1.977 63.281 1.00 59.16 C ANISOU 680 CG GLN A 556 9233 8673 4572 2215 1080 681 C ATOM 681 CD GLN A 556 18.006 1.032 63.838 1.00 59.69 C ANISOU 681 CD GLN A 556 9334 8759 4585 2204 1004 714 C ATOM 682 OE1 GLN A 556 17.700 0.123 64.613 1.00 60.50 O ANISOU 682 OE1 GLN A 556 9432 8897 4659 2253 1082 824 O ATOM 683 NE2 GLN A 556 19.257 1.246 63.447 1.00 59.20 N ANISOU 683 NE2 GLN A 556 9305 8674 4516 2139 848 622 N ATOM 684 N ASP A 557 13.948 -1.476 63.767 1.00 62.77 N ANISOU 684 N ASP A 557 9382 9206 5263 2268 1538 1185 N ATOM 685 CA ASP A 557 12.697 -2.110 64.206 1.00 64.73 C ANISOU 685 CA ASP A 557 9557 9472 5567 2323 1697 1329 C ATOM 686 C ASP A 557 11.725 -2.469 63.072 1.00 63.60 C ANISOU 686 C ASP A 557 9251 9302 5611 2251 1781 1408 C ATOM 687 O ASP A 557 10.656 -1.866 62.943 1.00 62.61 O ANISOU 687 O ASP A 557 9091 9169 5527 2286 1866 1421 O ATOM 688 CB ASP A 557 11.980 -1.216 65.230 1.00 69.12 C ANISOU 688 CB ASP A 557 10207 10048 6009 2450 1764 1307 C ATOM 689 CG ASP A 557 12.936 -0.592 66.250 1.00 72.39 C ANISOU 689 CG ASP A 557 10792 10479 6235 2519 1662 1201 C ATOM 690 OD1 ASP A 557 13.894 -1.282 66.680 1.00 73.95 O ANISOU 690 OD1 ASP A 557 11030 10691 6375 2506 1590 1209 O ATOM 691 OD2 ASP A 557 12.694 0.569 66.658 1.00 74.03 O ANISOU 691 OD2 ASP A 557 11092 10681 6354 2589 1656 1114 O ATOM 692 N GLY A 558 12.094 -3.471 62.278 1.00 60.96 N ANISOU 692 N GLY A 558 8819 8950 5393 2151 1756 1463 N ATOM 693 CA GLY A 558 11.324 -3.854 61.107 1.00 59.01 C ANISOU 693 CA GLY A 558 8420 8670 5332 2068 1812 1529 C ATOM 694 C GLY A 558 12.237 -4.145 59.929 1.00 54.05 C ANISOU 694 C GLY A 558 7747 8012 4778 1948 1709 1480 C ATOM 695 O GLY A 558 13.462 -4.081 60.069 1.00 54.01 O ANISOU 695 O GLY A 558 7827 8014 4682 1934 1596 1402 O ATOM 696 N PRO A 559 11.652 -4.458 58.755 1.00 50.87 N ANISOU 696 N PRO A 559 7212 7573 4543 1862 1743 1525 N ATOM 697 CA PRO A 559 12.433 -4.855 57.569 1.00 46.68 C ANISOU 697 CA PRO A 559 6627 7011 4098 1748 1658 1496 C ATOM 698 C PRO A 559 13.256 -3.714 56.972 1.00 44.83 C ANISOU 698 C PRO A 559 6469 6769 3795 1721 1548 1339 C ATOM 699 O PRO A 559 12.861 -2.549 57.040 1.00 43.50 O ANISOU 699 O PRO A 559 6349 6603 3575 1765 1556 1259 O ATOM 700 CB PRO A 559 11.359 -5.328 56.579 1.00 46.94 C ANISOU 700 CB PRO A 559 6503 7006 4326 1678 1735 1585 C ATOM 701 CG PRO A 559 10.108 -4.635 57.010 1.00 48.75 C ANISOU 701 CG PRO A 559 6722 7244 4555 1753 1834 1607 C ATOM 702 CD PRO A 559 10.198 -4.491 58.503 1.00 50.42 C ANISOU 702 CD PRO A 559 7046 7501 4609 1870 1862 1614 C ATOM 703 N LEU A 560 14.398 -4.056 56.391 1.00 42.42 N ANISOU 703 N LEU A 560 6172 6451 3493 1652 1445 1297 N ATOM 704 CA LEU A 560 15.274 -3.051 55.826 1.00 41.88 C ANISOU 704 CA LEU A 560 6174 6373 3365 1625 1332 1153 C ATOM 705 C LEU A 560 14.690 -2.473 54.543 1.00 39.34 C ANISOU 705 C LEU A 560 5773 6021 3155 1562 1352 1118 C ATOM 706 O LEU A 560 14.530 -3.181 53.549 1.00 39.83 O ANISOU 706 O LEU A 560 5727 6056 3352 1479 1370 1178 O ATOM 707 CB LEU A 560 16.658 -3.642 55.560 1.00 39.42 C ANISOU 707 CB LEU A 560 5888 6056 3035 1570 1218 1130 C ATOM 708 CG LEU A 560 17.540 -2.700 54.744 1.00 37.16 C ANISOU 708 CG LEU A 560 5640 5744 2734 1520 1092 985 C ATOM 709 CD1 LEU A 560 17.708 -1.382 55.474 1.00 34.09 C ANISOU 709 CD1 LEU A 560 5380 5374 2198 1599 1047 869 C ATOM 710 CD2 LEU A 560 18.892 -3.332 54.440 1.00 35.22 C ANISOU 710 CD2 LEU A 560 5385 5466 2531 1443 958 953 C ATOM 711 N TYR A 561 14.379 -1.181 54.571 1.00 39.45 N ANISOU 711 N TYR A 561 5842 6035 3114 1602 1346 1020 N ATOM 712 CA TYR A 561 13.921 -0.462 53.378 1.00 38.06 C ANISOU 712 CA TYR A 561 5605 5829 3027 1549 1352 968 C ATOM 713 C TYR A 561 14.986 0.514 52.882 1.00 36.66 C ANISOU 713 C TYR A 561 5498 5627 2803 1513 1210 809 C ATOM 714 O TYR A 561 15.352 1.449 53.585 1.00 35.87 O ANISOU 714 O TYR A 561 5519 5546 2565 1584 1167 720 O ATOM 715 CB TYR A 561 12.624 0.307 53.664 1.00 41.33 C ANISOU 715 CB TYR A 561 6003 6244 3455 1610 1448 978 C ATOM 716 CG TYR A 561 11.432 -0.558 54.015 1.00 44.04 C ANISOU 716 CG TYR A 561 6250 6593 3889 1630 1576 1129 C ATOM 717 CD1 TYR A 561 11.280 -1.821 53.463 1.00 44.02 C ANISOU 717 CD1 TYR A 561 6134 6574 4019 1557 1605 1240 C ATOM 718 CD2 TYR A 561 10.456 -0.108 54.901 1.00 46.12 C ANISOU 718 CD2 TYR A 561 6537 6873 4113 1723 1663 1162 C ATOM 719 CE1 TYR A 561 10.192 -2.616 53.782 1.00 44.99 C ANISOU 719 CE1 TYR A 561 6164 6693 4238 1572 1712 1377 C ATOM 720 CE2 TYR A 561 9.364 -0.898 55.228 1.00 47.15 C ANISOU 720 CE2 TYR A 561 6576 7006 4333 1744 1777 1303 C ATOM 721 CZ TYR A 561 9.240 -2.153 54.664 1.00 46.59 C ANISOU 721 CZ TYR A 561 6388 6915 4399 1666 1798 1410 C ATOM 722 OH TYR A 561 8.164 -2.954 54.979 1.00 47.65 O ANISOU 722 OH TYR A 561 6426 7044 4636 1682 1901 1551 O ATOM 723 N VAL A 562 15.486 0.301 51.675 1.00 35.33 N ANISOU 723 N VAL A 562 5244 5399 2780 1390 1120 765 N ATOM 724 CA VAL A 562 16.449 1.223 51.098 1.00 34.53 C ANISOU 724 CA VAL A 562 5185 5260 2674 1340 983 619 C ATOM 725 C VAL A 562 15.707 2.163 50.151 1.00 29.50 C ANISOU 725 C VAL A 562 4495 4589 2124 1306 1000 564 C ATOM 726 O VAL A 562 15.155 1.735 49.138 1.00 28.75 O ANISOU 726 O VAL A 562 4283 4459 2182 1228 1027 606 O ATOM 727 CB VAL A 562 17.574 0.471 50.367 1.00 33.10 C ANISOU 727 CB VAL A 562 4953 5037 2588 1234 871 600 C ATOM 728 CG1 VAL A 562 18.713 1.407 50.015 1.00 28.52 C ANISOU 728 CG1 VAL A 562 4430 4425 1982 1198 729 460 C ATOM 729 CG2 VAL A 562 18.091 -0.643 51.245 1.00 33.03 C ANISOU 729 CG2 VAL A 562 4971 5059 2519 1264 875 683 C ATOM 730 N ILE A 563 15.680 3.446 50.490 1.00 29.88 N ANISOU 730 N ILE A 563 4633 4645 2073 1368 982 470 N ATOM 731 CA ILE A 563 14.860 4.413 49.754 1.00 36.46 C ANISOU 731 CA ILE A 563 5427 5453 2974 1356 1013 426 C ATOM 732 C ILE A 563 15.704 5.197 48.750 1.00 33.79 C ANISOU 732 C ILE A 563 5084 5058 2697 1270 879 301 C ATOM 733 O ILE A 563 16.765 5.720 49.069 1.00 33.34 O ANISOU 733 O ILE A 563 5114 4993 2560 1277 773 209 O ATOM 734 CB ILE A 563 14.135 5.377 50.722 1.00 30.71 C ANISOU 734 CB ILE A 563 4796 4765 2108 1486 1094 409 C ATOM 735 CG1 ILE A 563 13.324 4.567 51.739 1.00 31.93 C ANISOU 735 CG1 ILE A 563 4955 4980 2198 1577 1237 544 C ATOM 736 CG2 ILE A 563 13.252 6.350 49.966 1.00 30.37 C ANISOU 736 CG2 ILE A 563 4705 4693 2141 1476 1131 371 C ATOM 737 CD1 ILE A 563 12.680 5.387 52.842 1.00 33.34 C ANISOU 737 CD1 ILE A 563 5211 5169 2289 1680 1282 525 C ATOM 738 N VAL A 564 15.210 5.278 47.525 1.00 33.22 N ANISOU 738 N VAL A 564 4907 4944 2772 1189 885 303 N ATOM 739 CA VAL A 564 16.001 5.767 46.413 1.00 32.63 C ANISOU 739 CA VAL A 564 4805 4813 2778 1094 768 209 C ATOM 740 C VAL A 564 15.122 6.594 45.452 1.00 33.33 C ANISOU 740 C VAL A 564 4833 4870 2959 1066 796 182 C ATOM 741 O VAL A 564 13.898 6.469 45.468 1.00 35.72 O ANISOU 741 O VAL A 564 5084 5188 3299 1096 904 256 O ATOM 742 CB VAL A 564 16.685 4.564 45.722 1.00 30.56 C ANISOU 742 CB VAL A 564 4467 4527 2618 998 719 249 C ATOM 743 CG1 VAL A 564 16.368 4.493 44.256 1.00 30.40 C ANISOU 743 CG1 VAL A 564 4341 4456 2754 900 704 246 C ATOM 744 CG2 VAL A 564 18.162 4.624 45.955 1.00 30.18 C ANISOU 744 CG2 VAL A 564 4483 4469 2515 980 599 179 C ATOM 745 N ALA A 565 15.739 7.476 44.664 1.00 33.86 N ANISOU 745 N ALA A 565 4908 4893 3062 1012 700 81 N ATOM 746 CA ALA A 565 14.997 8.314 43.721 1.00 34.47 C ANISOU 746 CA ALA A 565 4934 4938 3225 984 715 51 C ATOM 747 C ALA A 565 14.230 7.460 42.723 1.00 35.46 C ANISOU 747 C ALA A 565 4933 5045 3493 912 763 135 C ATOM 748 O ALA A 565 14.757 6.464 42.213 1.00 36.75 O ANISOU 748 O ALA A 565 5047 5194 3724 841 725 165 O ATOM 749 CB ALA A 565 15.939 9.271 42.984 1.00 34.64 C ANISOU 749 CB ALA A 565 4979 4912 3270 928 597 -62 C ATOM 750 N TYR A 566 12.989 7.857 42.451 1.00 36.37 N ANISOU 750 N TYR A 566 4999 5160 3659 933 841 170 N ATOM 751 CA TYR A 566 12.140 7.165 41.488 1.00 35.72 C ANISOU 751 CA TYR A 566 4797 5055 3719 867 879 246 C ATOM 752 C TYR A 566 12.466 7.592 40.074 1.00 34.73 C ANISOU 752 C TYR A 566 4628 4876 3691 774 793 182 C ATOM 753 O TYR A 566 12.478 8.779 39.753 1.00 33.29 O ANISOU 753 O TYR A 566 4475 4676 3499 782 762 107 O ATOM 754 CB TYR A 566 10.655 7.428 41.784 1.00 36.75 C ANISOU 754 CB TYR A 566 4886 5207 3871 929 997 317 C ATOM 755 CG TYR A 566 9.706 6.874 40.740 1.00 36.38 C ANISOU 755 CG TYR A 566 4713 5129 3981 860 1023 390 C ATOM 756 CD1 TYR A 566 9.639 5.515 40.497 1.00 36.59 C ANISOU 756 CD1 TYR A 566 4668 5147 4086 805 1030 474 C ATOM 757 CD2 TYR A 566 8.869 7.707 40.013 1.00 36.72 C ANISOU 757 CD2 TYR A 566 4709 5149 4096 850 1035 376 C ATOM 758 CE1 TYR A 566 8.790 4.992 39.548 1.00 36.60 C ANISOU 758 CE1 TYR A 566 4559 5115 4233 740 1041 536 C ATOM 759 CE2 TYR A 566 8.003 7.192 39.059 1.00 36.84 C ANISOU 759 CE2 TYR A 566 4610 5133 4255 785 1047 442 C ATOM 760 CZ TYR A 566 7.971 5.826 38.831 1.00 36.58 C ANISOU 760 CZ TYR A 566 4511 5090 4298 730 1047 520 C ATOM 761 OH TYR A 566 7.123 5.280 37.888 1.00 35.92 O ANISOU 761 OH TYR A 566 4318 4970 4360 663 1046 583 O ATOM 762 N ALA A 567 12.736 6.621 39.222 1.00 33.59 N ANISOU 762 N ALA A 567 4417 4704 3641 689 756 213 N ATOM 763 CA ALA A 567 12.945 6.904 37.815 1.00 32.21 C ANISOU 763 CA ALA A 567 4198 4481 3561 603 685 165 C ATOM 764 C ALA A 567 11.722 6.440 37.042 1.00 31.07 C ANISOU 764 C ALA A 567 3953 4317 3536 566 731 239 C ATOM 765 O ALA A 567 11.459 5.247 36.943 1.00 32.84 O ANISOU 765 O ALA A 567 4122 4537 3820 534 752 314 O ATOM 766 CB ALA A 567 14.192 6.220 37.308 1.00 30.58 C ANISOU 766 CB ALA A 567 3995 4251 3371 536 602 135 C ATOM 767 N SER A 568 10.966 7.377 36.487 1.00 30.49 N ANISOU 767 N SER A 568 3854 4228 3503 568 740 218 N ATOM 768 CA SER A 568 9.671 7.018 35.920 1.00 30.07 C ANISOU 768 CA SER A 568 3705 4160 3561 545 787 296 C ATOM 769 C SER A 568 9.758 6.353 34.540 1.00 29.83 C ANISOU 769 C SER A 568 3611 4081 3643 444 719 300 C ATOM 770 O SER A 568 8.743 5.918 34.014 1.00 29.06 O ANISOU 770 O SER A 568 3431 3964 3646 415 741 365 O ATOM 771 CB SER A 568 8.778 8.252 35.829 1.00 30.78 C ANISOU 771 CB SER A 568 3787 4249 3659 587 823 279 C ATOM 772 OG SER A 568 9.412 9.247 35.052 1.00 30.71 O ANISOU 772 OG SER A 568 3814 4212 3643 555 743 182 O ATOM 773 N LYS A 569 10.936 6.258 33.937 1.00 29.97 N ANISOU 773 N LYS A 569 3663 4076 3647 392 635 232 N ATOM 774 CA LYS A 569 10.965 5.613 32.626 1.00 29.49 C ANISOU 774 CA LYS A 569 3551 3970 3685 306 577 236 C ATOM 775 C LYS A 569 11.590 4.222 32.618 1.00 27.87 C ANISOU 775 C LYS A 569 3337 3753 3498 268 556 268 C ATOM 776 O LYS A 569 11.916 3.693 31.541 1.00 27.61 O ANISOU 776 O LYS A 569 3284 3680 3527 200 497 251 O ATOM 777 CB LYS A 569 11.666 6.501 31.617 1.00 29.05 C ANISOU 777 CB LYS A 569 3525 3885 3625 268 501 146 C ATOM 778 CG LYS A 569 10.760 7.599 31.156 1.00 28.93 C ANISOU 778 CG LYS A 569 3487 3862 3644 279 511 134 C ATOM 779 CD LYS A 569 11.303 8.315 29.967 1.00 28.35 C ANISOU 779 CD LYS A 569 3428 3754 3588 231 437 63 C ATOM 780 CE LYS A 569 10.485 9.568 29.716 1.00 28.80 C ANISOU 780 CE LYS A 569 3474 3807 3663 256 450 47 C ATOM 781 NZ LYS A 569 11.081 10.363 28.609 1.00 28.42 N ANISOU 781 NZ LYS A 569 3445 3727 3625 214 380 -20 N ATOM 782 N GLY A 570 11.724 3.632 33.811 1.00 26.62 N ANISOU 782 N GLY A 570 3198 3629 3286 315 607 315 N ATOM 783 CA GLY A 570 12.190 2.265 33.969 1.00 25.11 C ANISOU 783 CA GLY A 570 2994 3429 3116 288 600 360 C ATOM 784 C GLY A 570 13.674 2.117 33.675 1.00 24.89 C ANISOU 784 C GLY A 570 3020 3390 3047 259 528 291 C ATOM 785 O GLY A 570 14.412 3.106 33.653 1.00 22.75 O ANISOU 785 O GLY A 570 2803 3128 2715 272 491 213 O ATOM 786 N ASN A 571 14.115 0.889 33.427 1.00 24.41 N ANISOU 786 N ASN A 571 2940 3305 3029 219 506 321 N ATOM 787 CA ASN A 571 15.517 0.673 33.122 1.00 23.55 C ANISOU 787 CA ASN A 571 2874 3183 2892 193 443 263 C ATOM 788 C ASN A 571 15.789 0.892 31.647 1.00 21.19 C ANISOU 788 C ASN A 571 2563 2837 2650 131 381 206 C ATOM 789 O ASN A 571 14.914 0.732 30.818 1.00 20.13 O ANISOU 789 O ASN A 571 2383 2673 2593 96 378 226 O ATOM 790 CB ASN A 571 15.979 -0.735 33.557 1.00 23.36 C ANISOU 790 CB ASN A 571 2841 3152 2882 186 449 318 C ATOM 791 CG ASN A 571 15.324 -1.844 32.757 1.00 22.40 C ANISOU 791 CG ASN A 571 2657 2983 2872 132 446 370 C ATOM 792 OD1 ASN A 571 15.699 -2.086 31.609 1.00 20.96 O ANISOU 792 OD1 ASN A 571 2469 2755 2740 78 391 330 O ATOM 793 ND2 ASN A 571 14.334 -2.519 33.349 1.00 23.41 N ANISOU 793 ND2 ASN A 571 2738 3116 3041 147 504 462 N ATOM 794 N LEU A 572 17.025 1.249 31.338 1.00 20.82 N ANISOU 794 N LEU A 572 2558 2785 2566 120 330 140 N ATOM 795 CA LEU A 572 17.466 1.536 29.985 1.00 20.02 C ANISOU 795 CA LEU A 572 2458 2645 2504 70 276 84 C ATOM 796 C LEU A 572 17.100 0.476 28.937 1.00 20.40 C ANISOU 796 C LEU A 572 2468 2646 2638 17 258 110 C ATOM 797 O LEU A 572 16.840 0.825 27.793 1.00 19.71 O ANISOU 797 O LEU A 572 2371 2528 2588 -17 228 79 O ATOM 798 CB LEU A 572 18.977 1.746 30.010 1.00 20.02 C ANISOU 798 CB LEU A 572 2501 2648 2459 70 235 31 C ATOM 799 CG LEU A 572 19.733 2.138 28.751 1.00 15.49 C ANISOU 799 CG LEU A 572 1936 2040 1909 31 186 -26 C ATOM 800 CD1 LEU A 572 19.089 3.339 28.128 1.00 15.32 C ANISOU 800 CD1 LEU A 572 1911 2015 1895 26 179 -59 C ATOM 801 CD2 LEU A 572 21.206 2.398 29.084 1.00 15.35 C ANISOU 801 CD2 LEU A 572 1953 2032 1849 42 153 -63 C ATOM 802 N ARG A 573 17.068 -0.808 29.298 1.00 21.97 N ANISOU 802 N ARG A 573 2647 2833 2866 11 273 165 N ATOM 803 CA ARG A 573 16.691 -1.815 28.304 1.00 23.79 C ANISOU 803 CA ARG A 573 2847 3010 3181 -38 248 184 C ATOM 804 C ARG A 573 15.221 -1.682 27.887 1.00 26.04 C ANISOU 804 C ARG A 573 3083 3278 3532 -56 257 219 C ATOM 805 O ARG A 573 14.929 -1.612 26.699 1.00 25.57 O ANISOU 805 O ARG A 573 3016 3180 3519 -96 215 191 O ATOM 806 CB ARG A 573 16.959 -3.235 28.800 1.00 24.60 C ANISOU 806 CB ARG A 573 2938 3097 3311 -41 259 237 C ATOM 807 CG ARG A 573 16.528 -4.311 27.790 1.00 25.44 C ANISOU 807 CG ARG A 573 3017 3138 3510 -92 227 254 C ATOM 808 CD ARG A 573 16.886 -5.714 28.227 1.00 26.60 C ANISOU 808 CD ARG A 573 3156 3262 3690 -96 233 303 C ATOM 809 NE ARG A 573 18.301 -5.987 28.020 1.00 27.29 N ANISOU 809 NE ARG A 573 3287 3342 3740 -93 208 257 N ATOM 810 CZ ARG A 573 18.860 -7.196 28.075 1.00 27.81 C ANISOU 810 CZ ARG A 573 3356 3375 3837 -101 201 280 C ATOM 811 NH1 ARG A 573 18.128 -8.274 28.341 1.00 28.55 N ANISOU 811 NH1 ARG A 573 3411 3436 4000 -115 213 349 N ATOM 812 NH2 ARG A 573 20.160 -7.325 27.855 1.00 27.32 N ANISOU 812 NH2 ARG A 573 3330 3308 3743 -94 181 238 N ATOM 813 N GLU A 574 14.308 -1.650 28.858 1.00 29.34 N ANISOU 813 N GLU A 574 3468 3726 3956 -24 313 283 N ATOM 814 CA GLU A 574 12.887 -1.372 28.604 1.00 32.71 C ANISOU 814 CA GLU A 574 3839 4143 4447 -33 330 324 C ATOM 815 C GLU A 574 12.665 -0.066 27.814 1.00 28.84 C ANISOU 815 C GLU A 574 3360 3654 3944 -38 303 263 C ATOM 816 O GLU A 574 11.872 0.006 26.863 1.00 27.51 O ANISOU 816 O GLU A 574 3158 3450 3843 -75 271 266 O ATOM 817 CB GLU A 574 12.120 -1.255 29.924 1.00 40.32 C ANISOU 817 CB GLU A 574 4774 5152 5393 21 410 397 C ATOM 818 CG GLU A 574 11.834 -2.535 30.671 1.00 46.87 C ANISOU 818 CG GLU A 574 5568 5976 6264 26 450 486 C ATOM 819 CD GLU A 574 11.177 -2.271 32.041 1.00 56.40 C ANISOU 819 CD GLU A 574 6759 7238 7432 93 540 557 C ATOM 820 OE1 GLU A 574 11.041 -1.081 32.426 1.00 57.09 O ANISOU 820 OE1 GLU A 574 6873 7366 7452 139 569 525 O ATOM 821 OE2 GLU A 574 10.795 -3.256 32.726 1.00 61.43 O ANISOU 821 OE2 GLU A 574 7360 7876 8106 103 585 646 O ATOM 822 N TYR A 575 13.348 0.976 28.272 1.00 25.44 N ANISOU 822 N TYR A 575 2977 3262 3426 0 314 212 N ATOM 823 CA TYR A 575 13.252 2.292 27.710 1.00 22.77 C ANISOU 823 CA TYR A 575 2655 2928 3068 3 295 157 C ATOM 824 C TYR A 575 13.601 2.280 26.243 1.00 20.72 C ANISOU 824 C TYR A 575 2405 2625 2842 -50 228 109 C ATOM 825 O TYR A 575 12.872 2.856 25.437 1.00 19.10 O ANISOU 825 O TYR A 575 2180 2402 2674 -69 207 100 O ATOM 826 CB TYR A 575 14.172 3.227 28.470 1.00 22.59 C ANISOU 826 CB TYR A 575 2689 2945 2951 47 305 107 C ATOM 827 CG TYR A 575 14.294 4.598 27.898 1.00 21.93 C ANISOU 827 CG TYR A 575 2628 2859 2845 49 279 45 C ATOM 828 CD1 TYR A 575 13.391 5.582 28.229 1.00 22.38 C ANISOU 828 CD1 TYR A 575 2673 2934 2897 83 311 51 C ATOM 829 CD2 TYR A 575 15.335 4.927 27.050 1.00 21.94 C ANISOU 829 CD2 TYR A 575 2662 2840 2832 20 226 -16 C ATOM 830 CE1 TYR A 575 13.512 6.851 27.719 1.00 22.02 C ANISOU 830 CE1 TYR A 575 2648 2883 2835 86 286 -5 C ATOM 831 CE2 TYR A 575 15.453 6.190 26.530 1.00 21.55 C ANISOU 831 CE2 TYR A 575 2631 2787 2769 21 204 -67 C ATOM 832 CZ TYR A 575 14.540 7.141 26.878 1.00 21.34 C ANISOU 832 CZ TYR A 575 2593 2776 2740 53 232 -61 C ATOM 833 OH TYR A 575 14.650 8.402 26.382 1.00 21.43 O ANISOU 833 OH TYR A 575 2621 2779 2742 55 209 -109 O ATOM 834 N LEU A 576 14.711 1.631 25.895 1.00 19.59 N ANISOU 834 N LEU A 576 2295 2464 2684 -71 197 80 N ATOM 835 CA LEU A 576 15.143 1.582 24.511 1.00 18.41 C ANISOU 835 CA LEU A 576 2166 2276 2555 -112 141 34 C ATOM 836 C LEU A 576 14.175 0.761 23.654 1.00 18.99 C ANISOU 836 C LEU A 576 2203 2302 2710 -154 111 65 C ATOM 837 O LEU A 576 13.829 1.159 22.536 1.00 16.94 O ANISOU 837 O LEU A 576 1948 2017 2473 -180 69 38 O ATOM 838 CB LEU A 576 16.562 1.007 24.410 1.00 18.36 C ANISOU 838 CB LEU A 576 2199 2261 2514 -116 125 3 C ATOM 839 CG LEU A 576 17.697 1.880 24.982 1.00 17.74 C ANISOU 839 CG LEU A 576 2157 2217 2364 -85 132 -38 C ATOM 840 CD1 LEU A 576 19.046 1.189 24.922 1.00 17.10 C ANISOU 840 CD1 LEU A 576 2104 2127 2267 -89 118 -55 C ATOM 841 CD2 LEU A 576 17.771 3.268 24.306 1.00 16.78 C ANISOU 841 CD2 LEU A 576 2053 2098 2225 -86 112 -87 C ATOM 842 N ARG A 577 13.733 -0.382 24.183 1.00 19.70 N ANISOU 842 N ARG A 577 2260 2379 2847 -160 127 124 N ATOM 843 CA ARG A 577 12.890 -1.298 23.411 1.00 21.62 C ANISOU 843 CA ARG A 577 2469 2567 3178 -204 88 154 C ATOM 844 C ARG A 577 11.543 -0.702 23.002 1.00 21.79 C ANISOU 844 C ARG A 577 2443 2581 3257 -217 75 178 C ATOM 845 O ARG A 577 11.019 -1.015 21.932 1.00 21.35 O ANISOU 845 O ARG A 577 2378 2476 3257 -257 15 172 O ATOM 846 CB ARG A 577 12.662 -2.597 24.181 1.00 21.81 C ANISOU 846 CB ARG A 577 2459 2577 3250 -206 112 222 C ATOM 847 CG ARG A 577 13.887 -3.438 24.202 1.00 21.48 C ANISOU 847 CG ARG A 577 2461 2522 3178 -207 102 197 C ATOM 848 CD ARG A 577 13.627 -4.786 24.717 1.00 21.40 C ANISOU 848 CD ARG A 577 2418 2483 3229 -218 113 262 C ATOM 849 NE ARG A 577 14.866 -5.549 24.692 1.00 21.79 N ANISOU 849 NE ARG A 577 2512 2518 3249 -216 102 235 N ATOM 850 CZ ARG A 577 14.991 -6.793 25.143 1.00 22.52 C ANISOU 850 CZ ARG A 577 2591 2584 3383 -221 110 282 C ATOM 851 NH1 ARG A 577 13.953 -7.437 25.654 1.00 23.59 N ANISOU 851 NH1 ARG A 577 2666 2702 3594 -232 128 362 N ATOM 852 NH2 ARG A 577 16.166 -7.389 25.077 1.00 22.76 N ANISOU 852 NH2 ARG A 577 2662 2600 3385 -215 101 254 N ATOM 853 N ALA A 578 10.997 0.168 23.841 1.00 23.38 N ANISOU 853 N ALA A 578 2617 2827 3441 -179 129 205 N ATOM 854 CA ALA A 578 9.736 0.797 23.528 1.00 23.46 C ANISOU 854 CA ALA A 578 2577 2832 3507 -185 125 233 C ATOM 855 C ALA A 578 9.925 2.035 22.652 1.00 24.35 C ANISOU 855 C ALA A 578 2723 2948 3581 -186 90 168 C ATOM 856 O ALA A 578 8.958 2.715 22.310 1.00 26.19 O ANISOU 856 O ALA A 578 2919 3177 3854 -188 82 184 O ATOM 857 CB ALA A 578 9.017 1.152 24.790 1.00 23.80 C ANISOU 857 CB ALA A 578 2574 2917 3550 -137 204 295 C ATOM 858 N ARG A 579 11.162 2.315 22.269 1.00 23.79 N ANISOU 858 N ARG A 579 2718 2881 3439 -185 71 101 N ATOM 859 CA ARG A 579 11.454 3.524 21.518 1.00 23.22 C ANISOU 859 CA ARG A 579 2679 2815 3328 -183 46 44 C ATOM 860 C ARG A 579 12.211 3.200 20.228 1.00 21.15 C ANISOU 860 C ARG A 579 2466 2517 3053 -217 -14 -6 C ATOM 861 O ARG A 579 12.952 4.030 19.673 1.00 19.06 O ANISOU 861 O ARG A 579 2245 2260 2738 -211 -27 -57 O ATOM 862 CB ARG A 579 12.226 4.509 22.398 1.00 22.89 C ANISOU 862 CB ARG A 579 2669 2820 3208 -137 91 14 C ATOM 863 CG ARG A 579 11.294 5.419 23.182 1.00 23.00 C ANISOU 863 CG ARG A 579 2648 2863 3226 -99 137 43 C ATOM 864 CD ARG A 579 11.910 6.005 24.438 1.00 22.60 C ANISOU 864 CD ARG A 579 2627 2857 3102 -46 188 28 C ATOM 865 NE ARG A 579 11.559 5.142 25.555 1.00 23.72 N ANISOU 865 NE ARG A 579 2743 3019 3250 -22 239 87 N ATOM 866 CZ ARG A 579 10.642 5.421 26.468 1.00 24.07 C ANISOU 866 CZ ARG A 579 2755 3090 3302 20 299 135 C ATOM 867 NH1 ARG A 579 9.991 6.570 26.443 1.00 24.38 N ANISOU 867 NH1 ARG A 579 2783 3138 3341 46 314 126 N ATOM 868 NH2 ARG A 579 10.407 4.545 27.427 1.00 24.58 N ANISOU 868 NH2 ARG A 579 2799 3172 3370 41 347 195 N ATOM 869 N ARG A 580 11.974 1.982 19.755 1.00 21.07 N ANISOU 869 N ARG A 580 2450 2466 3092 -249 -50 12 N ATOM 870 CA ARG A 580 12.500 1.493 18.488 1.00 21.45 C ANISOU 870 CA ARG A 580 2547 2472 3132 -278 -109 -32 C ATOM 871 C ARG A 580 11.691 2.027 17.311 1.00 22.69 C ANISOU 871 C ARG A 580 2704 2602 3316 -302 -168 -44 C ATOM 872 O ARG A 580 10.592 2.555 17.493 1.00 22.05 O ANISOU 872 O ARG A 580 2570 2527 3280 -303 -167 -9 O ATOM 873 CB ARG A 580 12.495 -0.048 18.453 1.00 20.89 C ANISOU 873 CB ARG A 580 2473 2357 3107 -302 -132 -10 C ATOM 874 CG ARG A 580 13.425 -0.695 19.430 1.00 19.92 C ANISOU 874 CG ARG A 580 2360 2254 2956 -281 -84 -1 C ATOM 875 CD ARG A 580 13.501 -2.165 19.213 1.00 19.30 C ANISOU 875 CD ARG A 580 2286 2125 2922 -306 -113 13 C ATOM 876 NE ARG A 580 14.563 -2.736 20.026 1.00 18.73 N ANISOU 876 NE ARG A 580 2232 2070 2816 -283 -71 16 N ATOM 877 CZ ARG A 580 14.697 -4.030 20.297 1.00 19.08 C ANISOU 877 CZ ARG A 580 2269 2080 2899 -294 -74 43 C ATOM 878 NH1 ARG A 580 13.824 -4.912 19.818 1.00 19.21 N ANISOU 878 NH1 ARG A 580 2264 2040 2995 -329 -121 68 N ATOM 879 NH2 ARG A 580 15.700 -4.438 21.072 1.00 19.46 N ANISOU 879 NH2 ARG A 580 2333 2150 2912 -269 -36 47 N ATOM 880 N PRO A 581 12.225 1.878 16.090 1.00 25.53 N ANISOU 880 N PRO A 581 3123 2932 3647 -317 -217 -91 N ATOM 881 CA PRO A 581 11.367 2.157 14.935 1.00 28.61 C ANISOU 881 CA PRO A 581 3516 3290 4065 -341 -286 -98 C ATOM 882 C PRO A 581 10.208 1.157 14.890 1.00 32.83 C ANISOU 882 C PRO A 581 4002 3779 4692 -376 -334 -54 C ATOM 883 O PRO A 581 10.254 0.130 15.581 1.00 32.81 O ANISOU 883 O PRO A 581 3978 3764 4725 -382 -316 -25 O ATOM 884 CB PRO A 581 12.308 1.984 13.738 1.00 27.16 C ANISOU 884 CB PRO A 581 3417 3084 3820 -343 -321 -155 C ATOM 885 CG PRO A 581 13.689 2.064 14.312 1.00 26.24 C ANISOU 885 CG PRO A 581 3328 2999 3642 -314 -258 -177 C ATOM 886 CD PRO A 581 13.597 1.518 15.693 1.00 25.88 C ANISOU 886 CD PRO A 581 3233 2971 3629 -307 -212 -137 C ATOM 887 N PRO A 582 9.161 1.463 14.106 1.00 38.12 N ANISOU 887 N PRO A 582 4653 4423 5409 -399 -398 -43 N ATOM 888 CA PRO A 582 7.964 0.608 14.031 1.00 42.68 C ANISOU 888 CA PRO A 582 5173 4951 6091 -436 -454 5 C ATOM 889 C PRO A 582 8.213 -0.794 13.471 1.00 47.28 C ANISOU 889 C PRO A 582 5798 5473 6695 -465 -516 -15 C ATOM 890 O PRO A 582 9.231 -1.048 12.848 1.00 49.42 O ANISOU 890 O PRO A 582 6151 5733 6892 -456 -526 -74 O ATOM 891 CB PRO A 582 7.029 1.402 13.110 1.00 41.54 C ANISOU 891 CB PRO A 582 5017 4794 5974 -451 -520 6 C ATOM 892 CG PRO A 582 7.886 2.445 12.450 1.00 39.51 C ANISOU 892 CG PRO A 582 4831 4566 5614 -426 -509 -52 C ATOM 893 CD PRO A 582 8.957 2.758 13.428 1.00 37.87 C ANISOU 893 CD PRO A 582 4635 4409 5344 -389 -414 -63 C ATOM 894 N GLY A 583 7.280 -1.704 13.711 1.00 53.91 N ANISOU 894 N GLY A 583 6577 6268 7640 -498 -554 36 N ATOM 895 CA GLY A 583 7.376 -3.048 13.164 1.00 59.22 C ANISOU 895 CA GLY A 583 7285 6869 8346 -529 -624 18 C ATOM 896 C GLY A 583 6.660 -3.206 11.833 1.00 66.65 C ANISOU 896 C GLY A 583 8255 7747 9320 -564 -747 -8 C ATOM 897 O GLY A 583 5.738 -2.446 11.514 1.00 71.80 O ANISOU 897 O GLY A 583 8866 8405 10009 -576 -783 15 O ATOM 898 N ASN A 591 3.064 -1.112 24.416 1.00 63.93 N ANISOU 898 N ASN A 591 7250 7855 9187 -246 185 674 N ATOM 899 CA ASN A 591 4.308 -0.763 25.112 1.00 63.19 C ANISOU 899 CA ASN A 591 7241 7815 8952 -198 238 616 C ATOM 900 C ASN A 591 5.066 0.372 24.472 1.00 57.93 C ANISOU 900 C ASN A 591 6653 7168 8189 -189 205 512 C ATOM 901 O ASN A 591 5.746 1.150 25.145 1.00 56.23 O ANISOU 901 O ASN A 591 6490 7006 7871 -138 258 474 O ATOM 902 CB ASN A 591 5.263 -1.948 25.174 1.00 67.44 C ANISOU 902 CB ASN A 591 7823 8331 9471 -222 215 600 C ATOM 903 CG ASN A 591 4.651 -3.148 25.805 1.00 72.41 C ANISOU 903 CG ASN A 591 8381 8935 10195 -234 244 703 C ATOM 904 OD1 ASN A 591 4.688 -4.235 25.235 1.00 77.85 O ANISOU 904 OD1 ASN A 591 9061 9562 10956 -287 179 710 O ATOM 905 ND2 ASN A 591 4.076 -2.971 26.995 1.00 73.82 N ANISOU 905 ND2 ASN A 591 8510 9159 10378 -182 345 785 N ATOM 906 N ARG A 592 4.974 0.426 23.153 1.00 51.75 N ANISOU 906 N ARG A 592 5883 6340 7441 -239 111 468 N ATOM 907 CA ARG A 592 5.802 1.308 22.365 1.00 45.43 C ANISOU 907 CA ARG A 592 5160 5548 6555 -239 70 372 C ATOM 908 C ARG A 592 5.476 2.785 22.618 1.00 39.55 C ANISOU 908 C ARG A 592 4411 4846 5771 -195 112 359 C ATOM 909 O ARG A 592 4.314 3.150 22.824 1.00 38.23 O ANISOU 909 O ARG A 592 4172 4680 5672 -183 137 418 O ATOM 910 CB ARG A 592 5.644 0.954 20.889 1.00 45.10 C ANISOU 910 CB ARG A 592 5130 5444 6560 -299 -38 337 C ATOM 911 CG ARG A 592 6.608 1.673 20.015 1.00 45.06 C ANISOU 911 CG ARG A 592 5210 5445 6466 -300 -77 245 C ATOM 912 CD ARG A 592 6.817 0.956 18.706 1.00 45.89 C ANISOU 912 CD ARG A 592 5354 5491 6591 -350 -174 205 C ATOM 913 NE ARG A 592 7.366 1.897 17.742 1.00 45.93 N ANISOU 913 NE ARG A 592 5423 5502 6527 -347 -210 134 N ATOM 914 CZ ARG A 592 6.616 2.632 16.926 1.00 45.79 C ANISOU 914 CZ ARG A 592 5390 5471 6536 -360 -258 131 C ATOM 915 NH1 ARG A 592 5.295 2.501 16.941 1.00 45.87 N ANISOU 915 NH1 ARG A 592 5322 5459 6648 -378 -281 194 N ATOM 916 NH2 ARG A 592 7.187 3.485 16.085 1.00 45.65 N ANISOU 916 NH2 ARG A 592 5434 5461 6451 -354 -284 72 N ATOM 917 N VAL A 593 6.505 3.629 22.618 1.00 33.25 N ANISOU 917 N VAL A 593 3686 4078 4869 -169 121 284 N ATOM 918 CA VAL A 593 6.299 5.064 22.769 1.00 28.54 C ANISOU 918 CA VAL A 593 3096 3513 4234 -129 150 262 C ATOM 919 C VAL A 593 6.782 5.779 21.505 1.00 25.62 C ANISOU 919 C VAL A 593 2777 3123 3836 -156 79 189 C ATOM 920 O VAL A 593 7.861 6.371 21.485 1.00 25.64 O ANISOU 920 O VAL A 593 2844 3143 3755 -140 81 126 O ATOM 921 CB VAL A 593 7.022 5.608 24.020 1.00 25.51 C ANISOU 921 CB VAL A 593 2755 3183 3756 -67 226 242 C ATOM 922 CG1 VAL A 593 6.694 7.073 24.241 1.00 24.55 C ANISOU 922 CG1 VAL A 593 2638 3086 3604 -22 257 221 C ATOM 923 CG2 VAL A 593 6.621 4.801 25.234 1.00 23.32 C ANISOU 923 CG2 VAL A 593 2438 2926 3496 -38 297 316 C ATOM 924 N PRO A 594 5.963 5.734 20.447 1.00 24.34 N ANISOU 924 N PRO A 594 2580 2921 3745 -195 15 204 N ATOM 925 CA PRO A 594 6.344 6.211 19.114 1.00 24.12 C ANISOU 925 CA PRO A 594 2601 2869 3695 -224 -60 145 C ATOM 926 C PRO A 594 6.800 7.671 19.055 1.00 25.06 C ANISOU 926 C PRO A 594 2758 3016 3747 -191 -41 97 C ATOM 927 O PRO A 594 7.668 8.005 18.243 1.00 25.09 O ANISOU 927 O PRO A 594 2823 3012 3698 -204 -79 39 O ATOM 928 CB PRO A 594 5.058 6.007 18.283 1.00 23.56 C ANISOU 928 CB PRO A 594 2470 2757 3725 -261 -124 188 C ATOM 929 CG PRO A 594 3.965 5.800 19.263 1.00 23.35 C ANISOU 929 CG PRO A 594 2354 2741 3776 -242 -67 271 C ATOM 930 CD PRO A 594 4.586 5.202 20.470 1.00 23.57 C ANISOU 930 CD PRO A 594 2394 2800 3763 -214 7 284 C ATOM 931 N GLU A 595 6.237 8.533 19.890 1.00 27.31 N ANISOU 931 N GLU A 595 3009 3330 4037 -146 19 121 N ATOM 932 CA GLU A 595 6.608 9.943 19.833 1.00 28.46 C ANISOU 932 CA GLU A 595 3191 3494 4130 -115 31 75 C ATOM 933 C GLU A 595 7.961 10.165 20.501 1.00 28.95 C ANISOU 933 C GLU A 595 3317 3582 4099 -90 64 23 C ATOM 934 O GLU A 595 8.521 11.266 20.437 1.00 28.34 O ANISOU 934 O GLU A 595 3278 3513 3975 -69 66 -23 O ATOM 935 CB GLU A 595 5.535 10.831 20.479 1.00 30.14 C ANISOU 935 CB GLU A 595 3349 3723 4379 -71 83 115 C ATOM 936 CG GLU A 595 5.557 10.868 21.992 1.00 31.62 C ANISOU 936 CG GLU A 595 3533 3950 4533 -14 172 134 C ATOM 937 CD GLU A 595 4.845 9.679 22.644 1.00 32.82 C ANISOU 937 CD GLU A 595 3623 4104 4742 -16 208 210 C ATOM 938 OE1 GLU A 595 4.382 8.773 21.909 1.00 32.47 O ANISOU 938 OE1 GLU A 595 3540 4026 4770 -68 156 244 O ATOM 939 OE2 GLU A 595 4.757 9.657 23.899 1.00 33.95 O ANISOU 939 OE2 GLU A 595 3761 4282 4856 37 288 238 O ATOM 940 N GLU A 596 8.493 9.129 21.142 1.00 29.71 N ANISOU 940 N GLU A 596 3425 3689 4176 -91 86 32 N ATOM 941 CA GLU A 596 9.800 9.260 21.770 1.00 30.65 C ANISOU 941 CA GLU A 596 3602 3830 4213 -70 108 -14 C ATOM 942 C GLU A 596 10.829 8.336 21.116 1.00 29.40 C ANISOU 942 C GLU A 596 3482 3653 4036 -109 66 -41 C ATOM 943 O GLU A 596 11.859 8.028 21.722 1.00 29.54 O ANISOU 943 O GLU A 596 3534 3686 4002 -96 84 -62 O ATOM 944 CB GLU A 596 9.715 8.987 23.275 1.00 32.45 C ANISOU 944 CB GLU A 596 3820 4094 4416 -23 177 16 C ATOM 945 CG GLU A 596 9.057 10.109 24.080 1.00 33.89 C ANISOU 945 CG GLU A 596 3990 4301 4585 33 230 24 C ATOM 946 CD GLU A 596 9.065 9.868 25.598 1.00 35.28 C ANISOU 946 CD GLU A 596 4173 4516 4717 89 302 49 C ATOM 947 OE1 GLU A 596 10.067 9.332 26.135 1.00 36.10 O ANISOU 947 OE1 GLU A 596 4318 4633 4765 93 303 30 O ATOM 948 OE2 GLU A 596 8.058 10.222 26.261 1.00 36.26 O ANISOU 948 OE2 GLU A 596 4261 4656 4859 134 359 92 O ATOM 949 N GLN A 597 10.553 7.910 19.880 1.00 27.57 N ANISOU 949 N GLN A 597 3247 3386 3844 -152 9 -41 N ATOM 950 CA GLN A 597 11.480 7.072 19.123 1.00 26.45 C ANISOU 950 CA GLN A 597 3148 3221 3682 -183 -30 -70 C ATOM 951 C GLN A 597 12.916 7.636 19.158 1.00 24.39 C ANISOU 951 C GLN A 597 2942 2975 3349 -168 -20 -123 C ATOM 952 O GLN A 597 13.111 8.836 18.938 1.00 23.51 O ANISOU 952 O GLN A 597 2846 2872 3215 -155 -21 -149 O ATOM 953 CB GLN A 597 11.003 6.922 17.679 1.00 27.34 C ANISOU 953 CB GLN A 597 3266 3295 3828 -221 -97 -76 C ATOM 954 CG GLN A 597 11.952 6.104 16.815 1.00 28.25 C ANISOU 954 CG GLN A 597 3436 3384 3915 -245 -134 -110 C ATOM 955 CD GLN A 597 11.409 5.810 15.422 1.00 28.92 C ANISOU 955 CD GLN A 597 3536 3427 4026 -279 -206 -117 C ATOM 956 OE1 GLN A 597 10.198 5.659 15.225 1.00 29.01 O ANISOU 956 OE1 GLN A 597 3503 3419 4102 -297 -239 -82 O ATOM 957 NE2 GLN A 597 12.308 5.725 14.444 1.00 29.43 N ANISOU 957 NE2 GLN A 597 3664 3476 4041 -284 -232 -159 N ATOM 958 N MET A 598 13.896 6.769 19.446 1.00 22.90 N ANISOU 958 N MET A 598 2779 2788 3133 -171 -13 -133 N ATOM 959 CA MET A 598 15.296 7.176 19.646 1.00 21.38 C ANISOU 959 CA MET A 598 2628 2610 2885 -156 -2 -173 C ATOM 960 C MET A 598 15.929 7.657 18.349 1.00 20.53 C ANISOU 960 C MET A 598 2556 2482 2761 -173 -35 -208 C ATOM 961 O MET A 598 15.729 7.044 17.301 1.00 21.37 O ANISOU 961 O MET A 598 2675 2560 2883 -198 -68 -208 O ATOM 962 CB MET A 598 16.154 6.020 20.197 1.00 21.15 C ANISOU 962 CB MET A 598 2612 2584 2841 -155 12 -168 C ATOM 963 CG MET A 598 15.717 5.421 21.512 1.00 21.19 C ANISOU 963 CG MET A 598 2588 2610 2853 -135 49 -128 C ATOM 964 SD MET A 598 15.710 6.636 22.825 1.00 26.67 S ANISOU 964 SD MET A 598 3283 3348 3503 -86 89 -134 S ATOM 965 CE MET A 598 17.451 7.045 22.899 1.00 30.52 C ANISOU 965 CE MET A 598 3818 3842 3937 -80 75 -185 C ATOM 966 N THR A 599 16.692 8.745 18.428 1.00 20.69 N ANISOU 966 N THR A 599 2594 2515 2751 -157 -27 -236 N ATOM 967 CA THR A 599 17.546 9.194 17.320 1.00 20.57 C ANISOU 967 CA THR A 599 2613 2484 2718 -168 -46 -262 C ATOM 968 C THR A 599 19.022 8.887 17.605 1.00 20.91 C ANISOU 968 C THR A 599 2678 2533 2735 -161 -32 -279 C ATOM 969 O THR A 599 19.398 8.572 18.742 1.00 20.70 O ANISOU 969 O THR A 599 2643 2525 2699 -146 -12 -275 O ATOM 970 CB THR A 599 17.417 10.708 17.073 1.00 18.96 C ANISOU 970 CB THR A 599 2408 2282 2513 -158 -51 -276 C ATOM 971 OG1 THR A 599 17.868 11.406 18.238 1.00 18.18 O ANISOU 971 OG1 THR A 599 2304 2204 2400 -134 -29 -288 O ATOM 972 CG2 THR A 599 15.984 11.088 16.805 1.00 18.72 C ANISOU 972 CG2 THR A 599 2353 2248 2514 -162 -65 -256 C ATOM 973 N PHE A 600 19.862 9.011 16.579 1.00 21.66 N ANISOU 973 N PHE A 600 2800 2612 2817 -168 -39 -293 N ATOM 974 CA PHE A 600 21.290 8.775 16.753 1.00 22.61 C ANISOU 974 CA PHE A 600 2932 2734 2923 -161 -24 -301 C ATOM 975 C PHE A 600 21.899 9.674 17.828 1.00 24.02 C ANISOU 975 C PHE A 600 3096 2931 3099 -145 -16 -311 C ATOM 976 O PHE A 600 22.647 9.207 18.678 1.00 23.26 O ANISOU 976 O PHE A 600 2995 2846 2996 -136 -8 -310 O ATOM 977 CB PHE A 600 22.047 8.972 15.445 1.00 22.63 C ANISOU 977 CB PHE A 600 2963 2719 2916 -165 -24 -308 C ATOM 978 CG PHE A 600 23.539 8.890 15.605 1.00 22.54 C ANISOU 978 CG PHE A 600 2954 2710 2902 -155 -4 -309 C ATOM 979 CD1 PHE A 600 24.149 7.686 15.921 1.00 23.11 C ANISOU 979 CD1 PHE A 600 3029 2779 2972 -150 9 -304 C ATOM 980 CD2 PHE A 600 24.326 10.017 15.471 1.00 21.85 C ANISOU 980 CD2 PHE A 600 2858 2622 2823 -151 1 -311 C ATOM 981 CE1 PHE A 600 25.518 7.606 16.077 1.00 23.02 C ANISOU 981 CE1 PHE A 600 3012 2768 2966 -140 27 -300 C ATOM 982 CE2 PHE A 600 25.700 9.941 15.627 1.00 21.89 C ANISOU 982 CE2 PHE A 600 2854 2625 2837 -144 17 -305 C ATOM 983 CZ PHE A 600 26.296 8.738 15.927 1.00 22.31 C ANISOU 983 CZ PHE A 600 2910 2679 2889 -138 30 -300 C ATOM 984 N LYS A 601 21.578 10.956 17.783 1.00 26.83 N ANISOU 984 N LYS A 601 3446 3288 3460 -141 -24 -320 N ATOM 985 CA LYS A 601 22.036 11.902 18.779 1.00 29.46 C ANISOU 985 CA LYS A 601 3772 3631 3792 -125 -27 -336 C ATOM 986 C LYS A 601 21.593 11.509 20.210 1.00 28.65 C ANISOU 986 C LYS A 601 3662 3551 3672 -105 -18 -334 C ATOM 987 O LYS A 601 22.369 11.619 21.162 1.00 28.44 O ANISOU 987 O LYS A 601 3640 3535 3632 -91 -22 -346 O ATOM 988 CB LYS A 601 21.537 13.292 18.401 1.00 32.28 C ANISOU 988 CB LYS A 601 4127 3978 4162 -124 -39 -345 C ATOM 989 CG LYS A 601 21.632 14.335 19.467 1.00 35.20 C ANISOU 989 CG LYS A 601 4494 4351 4530 -103 -47 -367 C ATOM 990 CD LYS A 601 20.635 15.407 19.113 1.00 37.27 C ANISOU 990 CD LYS A 601 4751 4602 4806 -98 -52 -370 C ATOM 991 CE LYS A 601 20.330 16.362 20.231 1.00 39.55 C ANISOU 991 CE LYS A 601 5043 4894 5089 -69 -56 -393 C ATOM 992 NZ LYS A 601 19.018 16.987 19.873 1.00 42.39 N ANISOU 992 NZ LYS A 601 5392 5249 5464 -61 -50 -385 N ATOM 993 N ASP A 602 20.366 11.029 20.366 1.00 28.23 N ANISOU 993 N ASP A 602 3598 3506 3621 -102 -6 -316 N ATOM 994 CA ASP A 602 19.900 10.563 21.678 1.00 27.75 C ANISOU 994 CA ASP A 602 3530 3470 3544 -79 13 -304 C ATOM 995 C ASP A 602 20.730 9.402 22.194 1.00 24.19 C ANISOU 995 C ASP A 602 3084 3027 3080 -79 19 -294 C ATOM 996 O ASP A 602 21.101 9.364 23.360 1.00 23.99 O ANISOU 996 O ASP A 602 3066 3022 3028 -55 25 -296 O ATOM 997 CB ASP A 602 18.437 10.120 21.620 1.00 30.06 C ANISOU 997 CB ASP A 602 3798 3765 3856 -79 29 -273 C ATOM 998 CG ASP A 602 17.506 11.227 21.197 1.00 31.96 C ANISOU 998 CG ASP A 602 4028 4000 4115 -75 24 -277 C ATOM 999 OD1 ASP A 602 17.763 12.402 21.580 1.00 34.03 O ANISOU 999 OD1 ASP A 602 4302 4264 4364 -55 22 -304 O ATOM 1000 OD2 ASP A 602 16.531 10.904 20.465 1.00 33.48 O ANISOU 1000 OD2 ASP A 602 4200 4180 4340 -93 18 -254 O ATOM 1001 N LEU A 603 20.976 8.431 21.322 1.00 21.28 N ANISOU 1001 N LEU A 603 2716 2641 2728 -102 16 -282 N ATOM 1002 CA LEU A 603 21.795 7.284 21.665 1.00 18.43 C ANISOU 1002 CA LEU A 603 2360 2282 2363 -103 22 -271 C ATOM 1003 C LEU A 603 23.187 7.699 22.174 1.00 18.47 C ANISOU 1003 C LEU A 603 2373 2293 2352 -92 12 -289 C ATOM 1004 O LEU A 603 23.665 7.190 23.197 1.00 16.90 O ANISOU 1004 O LEU A 603 2175 2110 2136 -76 15 -280 O ATOM 1005 CB LEU A 603 21.929 6.368 20.453 1.00 17.05 C ANISOU 1005 CB LEU A 603 2192 2079 2207 -126 17 -265 C ATOM 1006 CG LEU A 603 20.697 5.592 19.987 1.00 16.32 C ANISOU 1006 CG LEU A 603 2092 1972 2138 -142 14 -244 C ATOM 1007 CD1 LEU A 603 21.050 4.701 18.815 1.00 16.17 C ANISOU 1007 CD1 LEU A 603 2095 1920 2129 -160 1 -249 C ATOM 1008 CD2 LEU A 603 20.136 4.770 21.124 1.00 16.11 C ANISOU 1008 CD2 LEU A 603 2044 1960 2118 -133 32 -212 C ATOM 1009 N VAL A 604 23.823 8.623 21.461 1.00 18.06 N ANISOU 1009 N VAL A 604 2325 2227 2310 -100 -2 -309 N ATOM 1010 CA VAL A 604 25.109 9.157 21.880 1.00 18.36 C ANISOU 1010 CA VAL A 604 2362 2264 2349 -94 -19 -322 C ATOM 1011 C VAL A 604 25.004 9.899 23.201 1.00 17.44 C ANISOU 1011 C VAL A 604 2252 2166 2209 -71 -36 -339 C ATOM 1012 O VAL A 604 25.896 9.819 24.040 1.00 18.61 O ANISOU 1012 O VAL A 604 2403 2320 2347 -60 -54 -344 O ATOM 1013 CB VAL A 604 25.700 10.105 20.830 1.00 17.20 C ANISOU 1013 CB VAL A 604 2213 2095 2228 -108 -28 -333 C ATOM 1014 CG1 VAL A 604 26.950 10.774 21.375 1.00 16.00 C ANISOU 1014 CG1 VAL A 604 2051 1937 2091 -105 -53 -343 C ATOM 1015 CG2 VAL A 604 25.991 9.347 19.526 1.00 17.09 C ANISOU 1015 CG2 VAL A 604 2203 2064 2226 -122 -9 -317 C ATOM 1016 N SER A 605 23.911 10.624 23.387 1.00 18.04 N ANISOU 1016 N SER A 605 2333 2247 2273 -60 -31 -349 N ATOM 1017 CA SER A 605 23.700 11.350 24.633 1.00 18.08 C ANISOU 1017 CA SER A 605 2355 2269 2247 -29 -41 -369 C ATOM 1018 C SER A 605 23.617 10.396 25.832 1.00 18.66 C ANISOU 1018 C SER A 605 2437 2370 2282 -4 -27 -351 C ATOM 1019 O SER A 605 24.264 10.637 26.861 1.00 18.42 O ANISOU 1019 O SER A 605 2427 2350 2221 19 -51 -367 O ATOM 1020 CB SER A 605 22.441 12.206 24.554 1.00 18.94 C ANISOU 1020 CB SER A 605 2465 2378 2353 -16 -28 -376 C ATOM 1021 OG SER A 605 22.233 12.845 25.807 1.00 20.55 O ANISOU 1021 OG SER A 605 2693 2597 2518 23 -33 -398 O ATOM 1022 N CYS A 606 22.824 9.328 25.695 1.00 18.36 N ANISOU 1022 N CYS A 606 2386 2343 2248 -8 6 -316 N ATOM 1023 CA CYS A 606 22.796 8.220 26.661 1.00 18.92 C ANISOU 1023 CA CYS A 606 2459 2437 2294 11 25 -286 C ATOM 1024 C CYS A 606 24.176 7.768 27.060 1.00 18.56 C ANISOU 1024 C CYS A 606 2422 2391 2240 10 -1 -290 C ATOM 1025 O CYS A 606 24.490 7.688 28.245 1.00 18.56 O ANISOU 1025 O CYS A 606 2440 2412 2198 40 -10 -289 O ATOM 1026 CB CYS A 606 22.072 7.005 26.094 1.00 17.91 C ANISOU 1026 CB CYS A 606 2307 2303 2195 -9 54 -246 C ATOM 1027 SG CYS A 606 20.326 7.164 26.044 1.00 33.63 S ANISOU 1027 SG CYS A 606 4279 4301 4200 -1 87 -221 S ATOM 1028 N THR A 607 24.983 7.465 26.047 1.00 18.59 N ANISOU 1028 N THR A 607 2410 2370 2282 -20 -12 -290 N ATOM 1029 CA THR A 607 26.318 6.917 26.233 1.00 18.93 C ANISOU 1029 CA THR A 607 2450 2408 2334 -23 -32 -285 C ATOM 1030 C THR A 607 27.256 7.885 26.925 1.00 19.67 C ANISOU 1030 C THR A 607 2555 2503 2417 -12 -77 -313 C ATOM 1031 O THR A 607 28.011 7.498 27.817 1.00 19.35 O ANISOU 1031 O THR A 607 2520 2473 2359 3 -100 -307 O ATOM 1032 CB THR A 607 26.932 6.506 24.892 1.00 19.04 C ANISOU 1032 CB THR A 607 2448 2394 2394 -52 -26 -279 C ATOM 1033 OG1 THR A 607 25.989 5.691 24.174 1.00 18.80 O ANISOU 1033 OG1 THR A 607 2414 2354 2373 -64 4 -261 O ATOM 1034 CG2 THR A 607 28.233 5.719 25.109 1.00 19.06 C ANISOU 1034 CG2 THR A 607 2439 2390 2411 -51 -36 -263 C ATOM 1035 N TYR A 608 27.200 9.147 26.521 1.00 19.94 N ANISOU 1035 N TYR A 608 2591 2522 2463 -19 -95 -343 N ATOM 1036 CA TYR A 608 27.987 10.184 27.165 1.00 20.63 C ANISOU 1036 CA TYR A 608 2690 2602 2547 -10 -147 -374 C ATOM 1037 C TYR A 608 27.614 10.350 28.637 1.00 21.02 C ANISOU 1037 C TYR A 608 2777 2677 2532 30 -163 -390 C ATOM 1038 O TYR A 608 28.487 10.464 29.475 1.00 21.09 O ANISOU 1038 O TYR A 608 2800 2687 2526 43 -210 -402 O ATOM 1039 CB TYR A 608 27.809 11.504 26.432 1.00 21.76 C ANISOU 1039 CB TYR A 608 2830 2719 2719 -24 -160 -401 C ATOM 1040 CG TYR A 608 28.339 12.688 27.184 1.00 23.51 C ANISOU 1040 CG TYR A 608 3069 2926 2936 -12 -217 -438 C ATOM 1041 CD1 TYR A 608 29.699 12.977 27.193 1.00 24.28 C ANISOU 1041 CD1 TYR A 608 3148 3000 3078 -29 -267 -441 C ATOM 1042 CD2 TYR A 608 27.476 13.527 27.888 1.00 24.67 C ANISOU 1042 CD2 TYR A 608 3252 3080 3042 17 -224 -471 C ATOM 1043 CE1 TYR A 608 30.191 14.065 27.879 1.00 25.14 C ANISOU 1043 CE1 TYR A 608 3274 3087 3191 -22 -332 -478 C ATOM 1044 CE2 TYR A 608 27.963 14.628 28.588 1.00 25.26 C ANISOU 1044 CE2 TYR A 608 3352 3135 3112 30 -284 -513 C ATOM 1045 CZ TYR A 608 29.322 14.886 28.570 1.00 25.07 C ANISOU 1045 CZ TYR A 608 3309 3082 3134 8 -343 -517 C ATOM 1046 OH TYR A 608 29.806 15.964 29.259 1.00 26.94 O ANISOU 1046 OH TYR A 608 3571 3291 3373 17 -414 -560 O ATOM 1047 N GLN A 609 26.325 10.367 28.955 1.00 20.74 N ANISOU 1047 N GLN A 609 2759 2662 2459 54 -124 -387 N ATOM 1048 CA GLN A 609 25.914 10.496 30.350 1.00 20.82 C ANISOU 1048 CA GLN A 609 2810 2700 2398 102 -127 -396 C ATOM 1049 C GLN A 609 26.438 9.360 31.208 1.00 20.33 C ANISOU 1049 C GLN A 609 2757 2663 2305 118 -129 -367 C ATOM 1050 O GLN A 609 26.890 9.569 32.318 1.00 20.99 O ANISOU 1050 O GLN A 609 2877 2759 2338 149 -166 -383 O ATOM 1051 CB GLN A 609 24.396 10.531 30.470 1.00 20.42 C ANISOU 1051 CB GLN A 609 2766 2671 2323 126 -69 -383 C ATOM 1052 CG GLN A 609 23.754 11.655 29.744 1.00 19.65 C ANISOU 1052 CG GLN A 609 2662 2551 2252 118 -65 -408 C ATOM 1053 CD GLN A 609 22.264 11.622 29.887 1.00 19.63 C ANISOU 1053 CD GLN A 609 2657 2569 2234 144 -8 -387 C ATOM 1054 OE1 GLN A 609 21.742 11.658 30.993 1.00 20.20 O ANISOU 1054 OE1 GLN A 609 2759 2668 2248 193 16 -384 O ATOM 1055 NE2 GLN A 609 21.558 11.539 28.762 1.00 19.72 N ANISOU 1055 NE2 GLN A 609 2631 2566 2295 113 17 -368 N ATOM 1056 N LEU A 610 26.350 8.142 30.696 1.00 20.98 N ANISOU 1056 N LEU A 610 2808 2749 2416 97 -92 -323 N ATOM 1057 CA LEU A 610 26.802 6.981 31.441 1.00 21.52 C ANISOU 1057 CA LEU A 610 2879 2836 2462 111 -90 -287 C ATOM 1058 C LEU A 610 28.322 6.993 31.565 1.00 22.14 C ANISOU 1058 C LEU A 610 2952 2899 2561 99 -150 -299 C ATOM 1059 O LEU A 610 28.884 6.547 32.564 1.00 22.87 O ANISOU 1059 O LEU A 610 3064 3009 2617 123 -177 -287 O ATOM 1060 CB LEU A 610 26.306 5.704 30.769 1.00 20.65 C ANISOU 1060 CB LEU A 610 2735 2722 2389 90 -40 -239 C ATOM 1061 CG LEU A 610 24.786 5.622 30.864 1.00 20.40 C ANISOU 1061 CG LEU A 610 2703 2707 2342 105 14 -218 C ATOM 1062 CD1 LEU A 610 24.215 4.520 29.976 1.00 19.81 C ANISOU 1062 CD1 LEU A 610 2592 2616 2320 74 51 -178 C ATOM 1063 CD2 LEU A 610 24.422 5.411 32.319 1.00 21.02 C ANISOU 1063 CD2 LEU A 610 2813 2824 2350 156 32 -197 C ATOM 1064 N ALA A 611 28.983 7.530 30.552 1.00 22.56 N ANISOU 1064 N ALA A 611 2978 2920 2675 64 -173 -317 N ATOM 1065 CA ALA A 611 30.417 7.683 30.614 1.00 22.79 C ANISOU 1065 CA ALA A 611 2992 2930 2738 51 -230 -324 C ATOM 1066 C ALA A 611 30.769 8.634 31.743 1.00 24.98 C ANISOU 1066 C ALA A 611 3308 3211 2972 77 -296 -362 C ATOM 1067 O ALA A 611 31.719 8.386 32.488 1.00 25.09 O ANISOU 1067 O ALA A 611 3327 3227 2979 86 -348 -358 O ATOM 1068 CB ALA A 611 30.961 8.188 29.291 1.00 22.68 C ANISOU 1068 CB ALA A 611 2940 2880 2798 13 -231 -330 C ATOM 1069 N ARG A 612 30.007 9.713 31.885 1.00 26.33 N ANISOU 1069 N ARG A 612 3510 3381 3114 91 -298 -400 N ATOM 1070 CA ARG A 612 30.277 10.681 32.941 1.00 28.86 C ANISOU 1070 CA ARG A 612 3879 3699 3389 120 -365 -445 C ATOM 1071 C ARG A 612 30.038 10.127 34.338 1.00 26.03 C ANISOU 1071 C ARG A 612 3572 3380 2939 171 -369 -438 C ATOM 1072 O ARG A 612 30.774 10.445 35.270 1.00 26.21 O ANISOU 1072 O ARG A 612 3630 3400 2928 191 -442 -463 O ATOM 1073 CB ARG A 612 29.431 11.921 32.746 1.00 32.01 C ANISOU 1073 CB ARG A 612 4302 4085 3777 129 -359 -488 C ATOM 1074 CG ARG A 612 30.003 12.846 31.731 1.00 35.34 C ANISOU 1074 CG ARG A 612 4687 4461 4280 87 -390 -506 C ATOM 1075 CD ARG A 612 29.193 14.099 31.709 1.00 39.26 C ANISOU 1075 CD ARG A 612 5213 4942 4762 102 -392 -549 C ATOM 1076 NE ARG A 612 29.297 14.844 32.951 1.00 43.21 N ANISOU 1076 NE ARG A 612 5777 5440 5202 143 -453 -599 N ATOM 1077 CZ ARG A 612 30.230 15.761 33.173 1.00 46.86 C ANISOU 1077 CZ ARG A 612 6248 5860 5697 131 -541 -637 C ATOM 1078 NH1 ARG A 612 31.129 16.023 32.229 1.00 47.42 N ANISOU 1078 NH1 ARG A 612 6260 5893 5866 79 -569 -623 N ATOM 1079 NH2 ARG A 612 30.270 16.405 34.334 1.00 51.81 N ANISOU 1079 NH2 ARG A 612 6944 6481 6260 173 -603 -688 N ATOM 1080 N GLY A 613 28.994 9.316 34.480 1.00 23.51 N ANISOU 1080 N GLY A 613 3258 3094 2581 192 -293 -402 N ATOM 1081 CA GLY A 613 28.641 8.719 35.755 1.00 22.29 C ANISOU 1081 CA GLY A 613 3151 2981 2338 245 -278 -382 C ATOM 1082 C GLY A 613 29.735 7.780 36.188 1.00 21.92 C ANISOU 1082 C GLY A 613 3093 2939 2296 240 -317 -352 C ATOM 1083 O GLY A 613 30.154 7.775 37.351 1.00 23.36 O ANISOU 1083 O GLY A 613 3324 3140 2412 278 -365 -360 O ATOM 1084 N MET A 614 30.229 7.004 35.231 1.00 21.28 N ANISOU 1084 N MET A 614 2950 2839 2294 195 -300 -318 N ATOM 1085 CA MET A 614 31.325 6.066 35.483 1.00 21.60 C ANISOU 1085 CA MET A 614 2970 2880 2358 187 -333 -284 C ATOM 1086 C MET A 614 32.639 6.786 35.802 1.00 22.96 C ANISOU 1086 C MET A 614 3145 3028 2553 178 -433 -317 C ATOM 1087 O MET A 614 33.403 6.347 36.661 1.00 22.52 O ANISOU 1087 O MET A 614 3103 2983 2472 196 -484 -302 O ATOM 1088 CB MET A 614 31.504 5.133 34.287 1.00 20.32 C ANISOU 1088 CB MET A 614 2744 2698 2278 145 -286 -245 C ATOM 1089 CG MET A 614 30.486 4.012 34.233 1.00 20.51 C ANISOU 1089 CG MET A 614 2763 2742 2286 155 -207 -197 C ATOM 1090 SD MET A 614 30.245 3.207 35.851 1.00 27.96 S ANISOU 1090 SD MET A 614 3753 3731 3140 210 -202 -157 S ATOM 1091 CE MET A 614 31.829 2.399 36.132 1.00 19.98 C ANISOU 1091 CE MET A 614 2719 2709 2164 202 -261 -130 C ATOM 1092 N GLU A 615 32.886 7.899 35.120 1.00 25.30 N ANISOU 1092 N GLU A 615 3425 3290 2899 150 -464 -358 N ATOM 1093 CA GLU A 615 34.084 8.696 35.358 1.00 28.10 C ANISOU 1093 CA GLU A 615 3774 3612 3290 136 -563 -388 C ATOM 1094 C GLU A 615 34.097 9.225 36.788 1.00 27.38 C ANISOU 1094 C GLU A 615 3759 3535 3108 182 -635 -426 C ATOM 1095 O GLU A 615 35.147 9.274 37.437 1.00 27.71 O ANISOU 1095 O GLU A 615 3807 3566 3156 184 -725 -432 O ATOM 1096 CB GLU A 615 34.167 9.849 34.354 1.00 30.84 C ANISOU 1096 CB GLU A 615 4092 3918 3708 99 -574 -420 C ATOM 1097 CG GLU A 615 35.407 10.706 34.492 1.00 32.71 C ANISOU 1097 CG GLU A 615 4310 4113 4005 77 -677 -444 C ATOM 1098 CD GLU A 615 35.301 12.064 33.786 1.00 33.83 C ANISOU 1098 CD GLU A 615 4442 4214 4199 52 -695 -483 C ATOM 1099 OE1 GLU A 615 34.179 12.472 33.400 1.00 35.23 O ANISOU 1099 OE1 GLU A 615 4642 4400 4346 60 -636 -502 O ATOM 1100 OE2 GLU A 615 36.354 12.732 33.631 1.00 35.37 O ANISOU 1100 OE2 GLU A 615 4602 4366 4472 23 -770 -491 O ATOM 1101 N TYR A 616 32.923 9.602 37.285 1.00 26.47 N ANISOU 1101 N TYR A 616 3704 3445 2906 223 -596 -451 N ATOM 1102 CA TYR A 616 32.799 10.021 38.675 1.00 26.97 C ANISOU 1102 CA TYR A 616 3855 3529 2863 280 -649 -487 C ATOM 1103 C TYR A 616 32.978 8.834 39.617 1.00 27.94 C ANISOU 1103 C TYR A 616 4002 3694 2922 315 -644 -440 C ATOM 1104 O TYR A 616 33.699 8.924 40.612 1.00 29.21 O ANISOU 1104 O TYR A 616 4207 3857 3034 341 -731 -456 O ATOM 1105 CB TYR A 616 31.447 10.688 38.937 1.00 26.14 C ANISOU 1105 CB TYR A 616 3807 3442 2683 323 -593 -519 C ATOM 1106 CG TYR A 616 31.203 10.967 40.407 1.00 26.57 C ANISOU 1106 CG TYR A 616 3962 3525 2610 396 -628 -550 C ATOM 1107 CD1 TYR A 616 31.845 12.030 41.044 1.00 27.02 C ANISOU 1107 CD1 TYR A 616 4077 3550 2639 411 -740 -619 C ATOM 1108 CD2 TYR A 616 30.351 10.161 41.161 1.00 26.21 C ANISOU 1108 CD2 TYR A 616 3955 3533 2469 451 -552 -509 C ATOM 1109 CE1 TYR A 616 31.649 12.285 42.380 1.00 27.75 C ANISOU 1109 CE1 TYR A 616 4272 3666 2604 484 -777 -652 C ATOM 1110 CE2 TYR A 616 30.139 10.412 42.498 1.00 27.31 C ANISOU 1110 CE2 TYR A 616 4194 3701 2482 526 -578 -535 C ATOM 1111 CZ TYR A 616 30.793 11.477 43.108 1.00 28.39 C ANISOU 1111 CZ TYR A 616 4396 3807 2582 544 -692 -610 C ATOM 1112 OH TYR A 616 30.601 11.741 44.451 1.00 29.46 O ANISOU 1112 OH TYR A 616 4643 3969 2580 625 -723 -642 O ATOM 1113 N LEU A 617 32.310 7.730 39.301 1.00 28.11 N ANISOU 1113 N LEU A 617 3993 3745 2944 316 -547 -381 N ATOM 1114 CA LEU A 617 32.383 6.529 40.120 1.00 28.64 C ANISOU 1114 CA LEU A 617 4076 3849 2957 348 -529 -326 C ATOM 1115 C LEU A 617 33.839 6.082 40.288 1.00 28.32 C ANISOU 1115 C LEU A 617 4005 3790 2964 325 -615 -309 C ATOM 1116 O LEU A 617 34.303 5.810 41.408 1.00 28.65 O ANISOU 1116 O LEU A 617 4095 3853 2938 363 -672 -302 O ATOM 1117 CB LEU A 617 31.528 5.428 39.496 1.00 29.45 C ANISOU 1117 CB LEU A 617 4133 3970 3088 336 -417 -263 C ATOM 1118 CG LEU A 617 30.913 4.402 40.451 1.00 30.99 C ANISOU 1118 CG LEU A 617 4361 4212 3203 386 -362 -206 C ATOM 1119 CD1 LEU A 617 29.554 3.981 39.961 1.00 31.14 C ANISOU 1119 CD1 LEU A 617 4356 4245 3230 386 -252 -170 C ATOM 1120 CD2 LEU A 617 31.810 3.181 40.566 1.00 30.85 C ANISOU 1120 CD2 LEU A 617 4307 4193 3220 372 -381 -150 C ATOM 1121 N ALA A 618 34.568 6.069 39.172 1.00 27.07 N ANISOU 1121 N ALA A 618 3770 3593 2923 267 -625 -303 N ATOM 1122 CA ALA A 618 35.995 5.726 39.154 1.00 27.04 C ANISOU 1122 CA ALA A 618 3720 3565 2988 241 -701 -282 C ATOM 1123 C ALA A 618 36.864 6.747 39.907 1.00 27.03 C ANISOU 1123 C ALA A 618 3755 3542 2973 248 -831 -333 C ATOM 1124 O ALA A 618 37.926 6.405 40.439 1.00 26.86 O ANISOU 1124 O ALA A 618 3722 3514 2971 248 -911 -314 O ATOM 1125 CB ALA A 618 36.477 5.589 37.721 1.00 26.78 C ANISOU 1125 CB ALA A 618 3599 3496 3082 184 -668 -264 C ATOM 1126 N SER A 619 36.420 7.998 39.947 1.00 27.10 N ANISOU 1126 N SER A 619 3805 3535 2955 254 -857 -397 N ATOM 1127 CA SER A 619 37.181 9.030 40.641 1.00 28.47 C ANISOU 1127 CA SER A 619 4019 3679 3120 259 -987 -452 C ATOM 1128 C SER A 619 36.940 8.923 42.136 1.00 29.67 C ANISOU 1128 C SER A 619 4273 3868 3131 327 -1033 -470 C ATOM 1129 O SER A 619 37.654 9.518 42.936 1.00 30.26 O ANISOU 1129 O SER A 619 4394 3923 3180 340 -1155 -510 O ATOM 1130 CB SER A 619 36.804 10.421 40.144 1.00 28.37 C ANISOU 1130 CB SER A 619 4018 3629 3131 243 -1002 -516 C ATOM 1131 OG SER A 619 35.518 10.770 40.618 1.00 28.66 O ANISOU 1131 OG SER A 619 4134 3697 3059 293 -945 -548 O ATOM 1132 N GLN A 620 35.927 8.161 42.519 1.00 30.63 N ANISOU 1132 N GLN A 620 4433 4042 3163 371 -936 -437 N ATOM 1133 CA GLN A 620 35.708 7.904 43.932 1.00 32.41 C ANISOU 1133 CA GLN A 620 4755 4310 3250 442 -964 -439 C ATOM 1134 C GLN A 620 36.411 6.608 44.323 1.00 32.45 C ANISOU 1134 C GLN A 620 4732 4338 3261 444 -976 -368 C ATOM 1135 O GLN A 620 36.235 6.100 45.420 1.00 34.08 O ANISOU 1135 O GLN A 620 5007 4585 3357 502 -982 -347 O ATOM 1136 CB GLN A 620 34.211 7.847 44.235 1.00 32.98 C ANISOU 1136 CB GLN A 620 4885 4427 3219 497 -849 -435 C ATOM 1137 CG GLN A 620 33.495 9.175 43.990 1.00 32.78 C ANISOU 1137 CG GLN A 620 4897 4380 3177 505 -842 -507 C ATOM 1138 CD GLN A 620 34.106 10.308 44.794 1.00 33.52 C ANISOU 1138 CD GLN A 620 5071 4444 3220 530 -976 -587 C ATOM 1139 OE1 GLN A 620 34.739 11.204 44.238 1.00 32.72 O ANISOU 1139 OE1 GLN A 620 4939 4288 3207 483 -1053 -634 O ATOM 1140 NE2 GLN A 620 33.931 10.267 46.110 1.00 34.78 N ANISOU 1140 NE2 GLN A 620 5338 4640 3239 606 -1006 -603 N ATOM 1141 N LYS A 621 37.217 6.096 43.398 1.00 32.25 N ANISOU 1141 N LYS A 621 4606 4282 3366 384 -977 -330 N ATOM 1142 CA LYS A 621 38.018 4.887 43.581 1.00 32.42 C ANISOU 1142 CA LYS A 621 4583 4313 3422 378 -991 -261 C ATOM 1143 C LYS A 621 37.136 3.697 43.945 1.00 32.04 C ANISOU 1143 C LYS A 621 4554 4315 3302 417 -884 -198 C ATOM 1144 O LYS A 621 37.483 2.895 44.808 1.00 32.26 O ANISOU 1144 O LYS A 621 4608 4371 3279 450 -910 -154 O ATOM 1145 CB LYS A 621 39.120 5.108 44.624 1.00 35.13 C ANISOU 1145 CB LYS A 621 4965 4648 3736 396 -1138 -276 C ATOM 1146 CG LYS A 621 39.977 6.341 44.350 1.00 36.98 C ANISOU 1146 CG LYS A 621 5179 4825 4047 357 -1255 -338 C ATOM 1147 CD LYS A 621 40.311 7.083 45.640 1.00 39.47 C ANISOU 1147 CD LYS A 621 5596 5139 4263 400 -1391 -394 C ATOM 1148 CE LYS A 621 39.366 8.283 45.868 1.00 40.54 C ANISOU 1148 CE LYS A 621 5819 5272 4312 431 -1385 -476 C ATOM 1149 NZ LYS A 621 39.643 9.091 47.099 1.00 42.18 N ANISOU 1149 NZ LYS A 621 6140 5472 4416 479 -1521 -544 N ATOM 1150 N CYS A 622 36.004 3.585 43.252 1.00 30.91 N ANISOU 1150 N CYS A 622 4396 4183 3165 411 -767 -190 N ATOM 1151 CA CYS A 622 35.111 2.438 43.397 1.00 30.15 C ANISOU 1151 CA CYS A 622 4300 4125 3030 436 -658 -123 C ATOM 1152 C CYS A 622 34.881 1.793 42.045 1.00 26.74 C ANISOU 1152 C CYS A 622 3779 3669 2713 383 -574 -90 C ATOM 1153 O CYS A 622 35.039 2.432 41.014 1.00 25.37 O ANISOU 1153 O CYS A 622 3562 3460 2619 337 -576 -126 O ATOM 1154 CB CYS A 622 33.767 2.852 44.008 1.00 30.26 C ANISOU 1154 CB CYS A 622 4389 4177 2929 491 -593 -139 C ATOM 1155 SG CYS A 622 33.865 3.434 45.722 1.00 59.04 S ANISOU 1155 SG CYS A 622 8163 7861 6410 575 -674 -173 S ATOM 1156 N ILE A 623 34.528 0.518 42.039 1.00 25.98 N ANISOU 1156 N ILE A 623 3658 3589 2623 389 -502 -20 N ATOM 1157 CA ILE A 623 34.202 -0.130 40.783 1.00 24.33 C ANISOU 1157 CA ILE A 623 3377 3354 2513 344 -423 8 C ATOM 1158 C ILE A 623 32.777 -0.618 40.865 1.00 24.68 C ANISOU 1158 C ILE A 623 3437 3425 2515 365 -321 43 C ATOM 1159 O ILE A 623 32.294 -0.964 41.951 1.00 25.84 O ANISOU 1159 O ILE A 623 3633 3612 2571 417 -301 77 O ATOM 1160 CB ILE A 623 35.148 -1.298 40.467 1.00 23.63 C ANISOU 1160 CB ILE A 623 3230 3245 2504 322 -431 61 C ATOM 1161 CG1 ILE A 623 35.111 -2.328 41.586 1.00 24.51 C ANISOU 1161 CG1 ILE A 623 3371 3389 2552 366 -424 126 C ATOM 1162 CG2 ILE A 623 36.560 -0.797 40.281 1.00 23.00 C ANISOU 1162 CG2 ILE A 623 3120 3134 2484 298 -526 34 C ATOM 1163 CD1 ILE A 623 35.946 -3.516 41.315 1.00 24.81 C ANISOU 1163 CD1 ILE A 623 3355 3405 2668 350 -426 182 C ATOM 1164 N HIS A 624 32.095 -0.633 39.728 1.00 23.75 N ANISOU 1164 N HIS A 624 3277 3285 2463 328 -257 37 N ATOM 1165 CA HIS A 624 30.693 -1.015 39.712 1.00 23.42 C ANISOU 1165 CA HIS A 624 3239 3262 2399 342 -165 71 C ATOM 1166 C HIS A 624 30.485 -2.539 39.653 1.00 23.88 C ANISOU 1166 C HIS A 624 3261 3315 2496 337 -111 150 C ATOM 1167 O HIS A 624 29.649 -3.065 40.382 1.00 24.11 O ANISOU 1167 O HIS A 624 3310 3374 2475 372 -57 202 O ATOM 1168 CB HIS A 624 29.977 -0.353 38.542 1.00 23.05 C ANISOU 1168 CB HIS A 624 3164 3190 2403 304 -129 32 C ATOM 1169 CG HIS A 624 28.488 -0.458 38.626 1.00 23.95 C ANISOU 1169 CG HIS A 624 3284 3324 2491 322 -47 59 C ATOM 1170 ND1 HIS A 624 27.788 -1.526 38.107 1.00 24.00 N ANISOU 1170 ND1 HIS A 624 3247 3317 2554 302 18 115 N ATOM 1171 CD2 HIS A 624 27.571 0.348 39.207 1.00 24.42 C ANISOU 1171 CD2 HIS A 624 3386 3414 2479 362 -20 42 C ATOM 1172 CE1 HIS A 624 26.500 -1.364 38.350 1.00 24.32 C ANISOU 1172 CE1 HIS A 624 3296 3379 2566 324 81 136 C ATOM 1173 NE2 HIS A 624 26.343 -0.239 39.023 1.00 24.92 N ANISOU 1173 NE2 HIS A 624 3424 3484 2562 363 64 94 N ATOM 1174 N ARG A 625 31.237 -3.219 38.780 1.00 23.96 N ANISOU 1174 N ARG A 625 3219 3286 2599 295 -121 160 N ATOM 1175 CA ARG A 625 31.163 -4.676 38.549 1.00 25.45 C ANISOU 1175 CA ARG A 625 3370 3456 2844 285 -78 227 C ATOM 1176 C ARG A 625 29.828 -5.209 38.023 1.00 24.22 C ANISOU 1176 C ARG A 625 3193 3289 2720 270 3 258 C ATOM 1177 O ARG A 625 29.622 -6.416 37.977 1.00 24.84 O ANISOU 1177 O ARG A 625 3247 3351 2840 265 38 318 O ATOM 1178 CB ARG A 625 31.506 -5.442 39.823 1.00 25.61 C ANISOU 1178 CB ARG A 625 3416 3506 2809 329 -91 288 C ATOM 1179 CG ARG A 625 32.954 -5.441 40.193 1.00 25.98 C ANISOU 1179 CG ARG A 625 3464 3549 2860 334 -172 280 C ATOM 1180 CD ARG A 625 33.157 -6.160 41.507 1.00 25.08 C ANISOU 1180 CD ARG A 625 3382 3468 2679 382 -185 343 C ATOM 1181 NE ARG A 625 33.019 -7.597 41.330 1.00 25.34 N ANISOU 1181 NE ARG A 625 3377 3480 2771 375 -135 417 N ATOM 1182 CZ ARG A 625 32.521 -8.427 42.239 1.00 27.11 C ANISOU 1182 CZ ARG A 625 3621 3731 2950 412 -97 491 C ATOM 1183 NH1 ARG A 625 32.096 -7.972 43.415 1.00 28.28 N ANISOU 1183 NH1 ARG A 625 3831 3933 2983 465 -98 503 N ATOM 1184 NH2 ARG A 625 32.449 -9.719 41.962 1.00 27.36 N ANISOU 1184 NH2 ARG A 625 3612 3732 3053 399 -56 555 N ATOM 1185 N ASP A 626 28.912 -4.338 37.627 1.00 24.45 N ANISOU 1185 N ASP A 626 3229 3324 2736 262 28 222 N ATOM 1186 CA ASP A 626 27.644 -4.816 37.077 1.00 24.24 C ANISOU 1186 CA ASP A 626 3176 3283 2752 244 96 253 C ATOM 1187 C ASP A 626 27.021 -3.745 36.173 1.00 24.95 C ANISOU 1187 C ASP A 626 3260 3362 2858 219 101 194 C ATOM 1188 O ASP A 626 25.812 -3.474 36.256 1.00 23.55 O ANISOU 1188 O ASP A 626 3082 3198 2667 228 148 208 O ATOM 1189 CB ASP A 626 26.670 -5.217 38.212 1.00 24.56 C ANISOU 1189 CB ASP A 626 3234 3363 2736 289 150 321 C ATOM 1190 CG ASP A 626 25.600 -6.236 37.764 1.00 24.30 C ANISOU 1190 CG ASP A 626 3156 3304 2774 267 213 383 C ATOM 1191 OD1 ASP A 626 25.564 -6.597 36.557 1.00 23.41 O ANISOU 1191 OD1 ASP A 626 3006 3141 2749 217 209 365 O ATOM 1192 OD2 ASP A 626 24.792 -6.673 38.630 1.00 23.99 O ANISOU 1192 OD2 ASP A 626 3119 3292 2705 301 265 452 O ATOM 1193 N LEU A 627 27.841 -3.117 35.331 1.00 24.73 N ANISOU 1193 N LEU A 627 3225 3310 2861 190 57 135 N ATOM 1194 CA LEU A 627 27.292 -2.241 34.310 1.00 25.08 C ANISOU 1194 CA LEU A 627 3260 3337 2933 162 63 86 C ATOM 1195 C LEU A 627 26.518 -3.050 33.295 1.00 25.14 C ANISOU 1195 C LEU A 627 3232 3308 3013 126 103 110 C ATOM 1196 O LEU A 627 27.063 -3.960 32.687 1.00 22.38 O ANISOU 1196 O LEU A 627 2861 2924 2718 104 98 123 O ATOM 1197 CB LEU A 627 28.364 -1.465 33.575 1.00 26.47 C ANISOU 1197 CB LEU A 627 3432 3491 3133 138 12 28 C ATOM 1198 CG LEU A 627 28.960 -0.204 34.168 1.00 27.14 C ANISOU 1198 CG LEU A 627 3549 3597 3167 158 -40 -20 C ATOM 1199 CD1 LEU A 627 30.212 -0.575 34.922 1.00 28.52 C ANISOU 1199 CD1 LEU A 627 3730 3778 3328 174 -90 -6 C ATOM 1200 CD2 LEU A 627 29.270 0.751 33.032 1.00 27.37 C ANISOU 1200 CD2 LEU A 627 3563 3598 3241 124 -61 -73 C ATOM 1201 N ALA A 628 25.256 -2.699 33.097 1.00 22.35 N ANISOU 1201 N ALA A 628 2872 2960 2661 123 138 114 N ATOM 1202 CA ALA A 628 24.409 -3.366 32.129 1.00 25.15 C ANISOU 1202 CA ALA A 628 3193 3277 3086 87 165 133 C ATOM 1203 C ALA A 628 23.163 -2.512 31.974 1.00 20.63 C ANISOU 1203 C ALA A 628 2616 2717 2506 88 189 124 C ATOM 1204 O ALA A 628 22.852 -1.731 32.868 1.00 24.86 O ANISOU 1204 O ALA A 628 3173 3293 2979 126 202 122 O ATOM 1205 CB ALA A 628 24.062 -4.774 32.594 1.00 22.08 C ANISOU 1205 CB ALA A 628 2785 2878 2728 91 194 207 C ATOM 1206 N ALA A 629 22.437 -2.654 30.872 1.00 22.10 N ANISOU 1206 N ALA A 629 2776 2867 2753 51 194 119 N ATOM 1207 CA ALA A 629 21.258 -1.817 30.652 1.00 20.82 C ANISOU 1207 CA ALA A 629 2603 2715 2594 50 214 112 C ATOM 1208 C ALA A 629 20.140 -2.104 31.675 1.00 23.17 C ANISOU 1208 C ALA A 629 2883 3041 2880 81 267 179 C ATOM 1209 O ALA A 629 19.323 -1.222 31.978 1.00 24.09 O ANISOU 1209 O ALA A 629 3000 3183 2971 104 292 177 O ATOM 1210 CB ALA A 629 20.749 -2.000 29.245 1.00 22.23 C ANISOU 1210 CB ALA A 629 2759 2847 2842 3 198 96 C ATOM 1211 N ARG A 630 20.118 -3.322 32.213 1.00 22.88 N ANISOU 1211 N ARG A 630 2831 2999 2864 86 288 242 N ATOM 1212 CA ARG A 630 19.159 -3.689 33.247 1.00 23.02 C ANISOU 1212 CA ARG A 630 2830 3045 2872 120 347 319 C ATOM 1213 C ARG A 630 19.419 -2.944 34.560 1.00 22.27 C ANISOU 1213 C ARG A 630 2780 3011 2671 184 368 317 C ATOM 1214 O ARG A 630 18.566 -2.929 35.445 1.00 23.10 O ANISOU 1214 O ARG A 630 2879 3148 2748 226 426 372 O ATOM 1215 CB ARG A 630 19.189 -5.205 33.488 1.00 22.42 C ANISOU 1215 CB ARG A 630 2727 2944 2847 109 361 390 C ATOM 1216 CG ARG A 630 20.476 -5.700 34.123 1.00 21.64 C ANISOU 1216 CG ARG A 630 2662 2858 2703 129 340 390 C ATOM 1217 CD ARG A 630 20.491 -7.207 34.377 1.00 21.06 C ANISOU 1217 CD ARG A 630 2562 2756 2684 120 355 465 C ATOM 1218 NE ARG A 630 21.831 -7.618 34.787 1.00 21.04 N ANISOU 1218 NE ARG A 630 2590 2759 2646 135 325 455 N ATOM 1219 CZ ARG A 630 22.828 -7.868 33.940 1.00 20.50 C ANISOU 1219 CZ ARG A 630 2527 2652 2608 105 278 406 C ATOM 1220 NH1 ARG A 630 22.624 -7.774 32.630 1.00 19.36 N ANISOU 1220 NH1 ARG A 630 2369 2463 2524 61 257 361 N ATOM 1221 NH2 ARG A 630 24.024 -8.216 34.399 1.00 20.66 N ANISOU 1221 NH2 ARG A 630 2568 2681 2601 123 254 405 N ATOM 1222 N ASN A 631 20.598 -2.338 34.692 1.00 21.75 N ANISOU 1222 N ASN A 631 2760 2957 2548 195 321 254 N ATOM 1223 CA ASN A 631 20.966 -1.597 35.910 1.00 21.79 C ANISOU 1223 CA ASN A 631 2819 3013 2448 255 323 240 C ATOM 1224 C ASN A 631 21.191 -0.109 35.667 1.00 20.85 C ANISOU 1224 C ASN A 631 2732 2901 2288 262 289 157 C ATOM 1225 O ASN A 631 21.886 0.560 36.423 1.00 21.47 O ANISOU 1225 O ASN A 631 2863 3006 2290 298 259 120 O ATOM 1226 CB ASN A 631 22.216 -2.188 36.554 1.00 22.04 C ANISOU 1226 CB ASN A 631 2879 3053 2442 269 287 245 C ATOM 1227 CG ASN A 631 21.980 -3.569 37.106 1.00 22.72 C ANISOU 1227 CG ASN A 631 2942 3140 2549 278 327 334 C ATOM 1228 OD1 ASN A 631 20.859 -3.915 37.483 1.00 22.74 O ANISOU 1228 OD1 ASN A 631 2921 3155 2562 296 390 399 O ATOM 1229 ND2 ASN A 631 23.038 -4.372 37.166 1.00 23.19 N ANISOU 1229 ND2 ASN A 631 3005 3185 2621 267 291 343 N ATOM 1230 N VAL A 632 20.604 0.404 34.599 1.00 19.85 N ANISOU 1230 N VAL A 632 2577 2747 2217 226 288 129 N ATOM 1231 CA VAL A 632 20.580 1.837 34.380 1.00 19.50 C ANISOU 1231 CA VAL A 632 2558 2708 2143 235 266 62 C ATOM 1232 C VAL A 632 19.136 2.287 34.398 1.00 20.27 C ANISOU 1232 C VAL A 632 2635 2816 2251 253 322 87 C ATOM 1233 O VAL A 632 18.288 1.644 33.795 1.00 18.98 O ANISOU 1233 O VAL A 632 2419 2632 2160 223 350 132 O ATOM 1234 CB VAL A 632 21.238 2.222 33.057 1.00 18.70 C ANISOU 1234 CB VAL A 632 2444 2567 2096 180 213 5 C ATOM 1235 CG1 VAL A 632 21.029 3.681 32.790 1.00 18.67 C ANISOU 1235 CG1 VAL A 632 2458 2562 2072 188 197 -53 C ATOM 1236 CG2 VAL A 632 22.718 1.900 33.120 1.00 18.48 C ANISOU 1236 CG2 VAL A 632 2434 2530 2058 170 162 -17 C ATOM 1237 N LEU A 633 18.845 3.361 35.115 1.00 22.02 N ANISOU 1237 N LEU A 633 2896 3067 2404 305 337 60 N ATOM 1238 CA LEU A 633 17.491 3.891 35.128 1.00 21.96 C ANISOU 1238 CA LEU A 633 2866 3069 2409 328 394 83 C ATOM 1239 C LEU A 633 17.386 5.166 34.314 1.00 21.76 C ANISOU 1239 C LEU A 633 2844 3022 2401 311 362 15 C ATOM 1240 O LEU A 633 18.349 5.899 34.133 1.00 20.76 O ANISOU 1240 O LEU A 633 2756 2886 2248 303 304 -53 O ATOM 1241 CB LEU A 633 17.027 4.135 36.549 1.00 23.38 C ANISOU 1241 CB LEU A 633 3087 3297 2499 411 451 112 C ATOM 1242 CG LEU A 633 17.112 2.844 37.364 1.00 22.63 C ANISOU 1242 CG LEU A 633 2987 3225 2387 429 487 189 C ATOM 1243 CD1 LEU A 633 16.819 3.099 38.832 1.00 22.27 C ANISOU 1243 CD1 LEU A 633 2997 3231 2232 519 542 215 C ATOM 1244 CD2 LEU A 633 16.184 1.761 36.804 1.00 22.09 C ANISOU 1244 CD2 LEU A 633 2838 3135 2422 390 531 271 C ATOM 1245 N VAL A 634 16.195 5.412 33.804 1.00 21.91 N ANISOU 1245 N VAL A 634 2819 3032 2472 305 399 40 N ATOM 1246 CA VAL A 634 15.956 6.589 33.012 1.00 22.45 C ANISOU 1246 CA VAL A 634 2887 3080 2564 290 374 -14 C ATOM 1247 C VAL A 634 14.890 7.373 33.724 1.00 25.71 C ANISOU 1247 C VAL A 634 3306 3518 2943 353 435 1 C ATOM 1248 O VAL A 634 13.852 6.816 34.059 1.00 24.03 O ANISOU 1248 O VAL A 634 3053 3321 2757 373 500 73 O ATOM 1249 CB VAL A 634 15.505 6.241 31.594 1.00 23.19 C ANISOU 1249 CB VAL A 634 2920 3134 2756 223 355 -1 C ATOM 1250 CG1 VAL A 634 15.360 7.504 30.779 1.00 22.34 C ANISOU 1250 CG1 VAL A 634 2817 3006 2666 210 325 -56 C ATOM 1251 CG2 VAL A 634 16.490 5.269 30.950 1.00 24.02 C ANISOU 1251 CG2 VAL A 634 3021 3214 2891 170 309 -6 C ATOM 1252 N THR A 635 15.157 8.652 33.970 1.00 28.35 N ANISOU 1252 N THR A 635 3691 3854 3225 386 414 -65 N ATOM 1253 CA THR A 635 14.209 9.529 34.645 1.00 31.30 C ANISOU 1253 CA THR A 635 4082 4249 3561 455 471 -63 C ATOM 1254 C THR A 635 13.221 10.157 33.662 1.00 33.05 C ANISOU 1254 C THR A 635 4251 4445 3863 432 482 -58 C ATOM 1255 O THR A 635 13.283 9.913 32.455 1.00 34.44 O ANISOU 1255 O THR A 635 4382 4589 4116 362 440 -60 O ATOM 1256 CB THR A 635 14.924 10.654 35.411 1.00 27.73 C ANISOU 1256 CB THR A 635 3717 3804 3015 506 438 -141 C ATOM 1257 OG1 THR A 635 15.555 11.554 34.482 1.00 26.09 O ANISOU 1257 OG1 THR A 635 3515 3557 2841 461 365 -211 O ATOM 1258 CG2 THR A 635 15.956 10.073 36.333 1.00 26.54 C ANISOU 1258 CG2 THR A 635 3621 3676 2788 526 412 -148 C ATOM 1259 N GLU A 636 12.315 10.974 34.195 1.00 37.72 N ANISOU 1259 N GLU A 636 4851 5052 4431 495 537 -53 N ATOM 1260 CA GLU A 636 11.280 11.613 33.391 1.00 42.15 C ANISOU 1260 CA GLU A 636 5358 5590 5066 483 553 -42 C ATOM 1261 C GLU A 636 11.856 12.597 32.373 1.00 43.59 C ANISOU 1261 C GLU A 636 5555 5734 5274 439 476 -117 C ATOM 1262 O GLU A 636 11.314 12.731 31.280 1.00 44.42 O ANISOU 1262 O GLU A 636 5606 5812 5460 394 460 -104 O ATOM 1263 CB GLU A 636 10.265 12.316 34.298 1.00 48.61 C ANISOU 1263 CB GLU A 636 6189 6434 5847 573 635 -21 C ATOM 1264 CG GLU A 636 8.969 12.718 33.590 1.00 54.13 C ANISOU 1264 CG GLU A 636 6813 7116 6638 567 670 20 C ATOM 1265 CD GLU A 636 8.053 11.536 33.234 1.00 59.51 C ANISOU 1265 CD GLU A 636 7400 7799 7413 531 709 121 C ATOM 1266 OE1 GLU A 636 8.494 10.362 33.277 1.00 62.33 O ANISOU 1266 OE1 GLU A 636 7744 8160 7777 494 696 153 O ATOM 1267 OE2 GLU A 636 6.877 11.789 32.894 1.00 61.94 O ANISOU 1267 OE2 GLU A 636 7642 8098 7796 539 748 169 O ATOM 1268 N ASN A 637 12.962 13.258 32.725 1.00 43.67 N ANISOU 1268 N ASN A 637 5636 5738 5217 452 426 -192 N ATOM 1269 CA ASN A 637 13.653 14.158 31.801 1.00 42.98 C ANISOU 1269 CA ASN A 637 5561 5611 5157 408 352 -257 C ATOM 1270 C ASN A 637 14.729 13.473 30.975 1.00 39.97 C ANISOU 1270 C ASN A 637 5168 5212 4807 334 290 -267 C ATOM 1271 O ASN A 637 15.633 14.135 30.487 1.00 39.31 O ANISOU 1271 O ASN A 637 5108 5102 4726 307 229 -322 O ATOM 1272 CB ASN A 637 14.298 15.322 32.552 1.00 45.69 C ANISOU 1272 CB ASN A 637 5983 5948 5427 457 322 -333 C ATOM 1273 CG ASN A 637 13.304 16.109 33.367 1.00 48.61 C ANISOU 1273 CG ASN A 637 6379 6332 5758 539 384 -334 C ATOM 1274 OD1 ASN A 637 12.097 16.042 33.126 1.00 49.93 O ANISOU 1274 OD1 ASN A 637 6493 6507 5973 553 445 -281 O ATOM 1275 ND2 ASN A 637 13.801 16.867 34.343 1.00 50.63 N ANISOU 1275 ND2 ASN A 637 6717 6590 5929 598 367 -394 N ATOM 1276 N ASN A 638 14.642 12.156 30.832 1.00 36.70 N ANISOU 1276 N ASN A 638 4717 4809 4418 305 307 -212 N ATOM 1277 CA ASN A 638 15.621 11.373 30.063 1.00 33.56 C ANISOU 1277 CA ASN A 638 4308 4394 4049 241 256 -217 C ATOM 1278 C ASN A 638 17.047 11.443 30.596 1.00 30.23 C ANISOU 1278 C ASN A 638 3938 3974 3572 245 210 -263 C ATOM 1279 O ASN A 638 17.996 11.483 29.827 1.00 29.51 O ANISOU 1279 O ASN A 638 3847 3858 3507 200 158 -291 O ATOM 1280 CB ASN A 638 15.628 11.807 28.596 1.00 33.19 C ANISOU 1280 CB ASN A 638 4233 4309 4068 186 216 -236 C ATOM 1281 CG ASN A 638 14.291 11.609 27.928 1.00 33.93 C ANISOU 1281 CG ASN A 638 4271 4396 4226 172 245 -189 C ATOM 1282 OD1 ASN A 638 13.555 10.677 28.251 1.00 34.66 O ANISOU 1282 OD1 ASN A 638 4328 4502 4338 177 285 -130 O ATOM 1283 ND2 ASN A 638 13.968 12.480 26.985 1.00 34.00 N ANISOU 1283 ND2 ASN A 638 4266 4379 4273 152 221 -209 N ATOM 1284 N VAL A 639 17.200 11.458 31.912 1.00 27.86 N ANISOU 1284 N VAL A 639 3683 3703 3198 302 229 -267 N ATOM 1285 CA VAL A 639 18.529 11.434 32.501 1.00 25.26 C ANISOU 1285 CA VAL A 639 3402 3376 2818 306 177 -304 C ATOM 1286 C VAL A 639 18.920 10.003 32.833 1.00 23.80 C ANISOU 1286 C VAL A 639 3204 3211 2627 295 189 -256 C ATOM 1287 O VAL A 639 18.123 9.262 33.416 1.00 23.96 O ANISOU 1287 O VAL A 639 3212 3260 2634 323 249 -199 O ATOM 1288 CB VAL A 639 18.598 12.282 33.780 1.00 25.05 C ANISOU 1288 CB VAL A 639 3445 3368 2703 378 176 -344 C ATOM 1289 CG1 VAL A 639 20.029 12.368 34.266 1.00 24.53 C ANISOU 1289 CG1 VAL A 639 3426 3295 2598 374 103 -388 C ATOM 1290 CG2 VAL A 639 17.988 13.669 33.537 1.00 24.37 C ANISOU 1290 CG2 VAL A 639 3372 3261 2626 399 177 -386 C ATOM 1291 N MET A 640 20.134 9.610 32.459 1.00 22.37 N ANISOU 1291 N MET A 640 3023 3014 2463 255 136 -272 N ATOM 1292 CA MET A 640 20.624 8.270 32.769 1.00 21.56 C ANISOU 1292 CA MET A 640 2910 2924 2357 245 141 -229 C ATOM 1293 C MET A 640 21.126 8.211 34.202 1.00 22.20 C ANISOU 1293 C MET A 640 3046 3037 2352 299 133 -234 C ATOM 1294 O MET A 640 21.943 9.037 34.616 1.00 21.69 O ANISOU 1294 O MET A 640 3027 2967 2249 314 77 -289 O ATOM 1295 CB MET A 640 21.735 7.858 31.801 1.00 21.05 C ANISOU 1295 CB MET A 640 2823 2829 2346 187 92 -242 C ATOM 1296 CG MET A 640 21.428 8.177 30.325 1.00 20.52 C ANISOU 1296 CG MET A 640 2719 2729 2351 138 87 -253 C ATOM 1297 SD MET A 640 19.996 7.271 29.701 1.00 31.66 S ANISOU 1297 SD MET A 640 4080 4137 3812 120 143 -193 S ATOM 1298 CE MET A 640 20.617 5.667 30.026 1.00 31.27 C ANISOU 1298 CE MET A 640 4021 4091 3767 109 148 -149 C ATOM 1299 N LYS A 641 20.624 7.248 34.965 1.00 22.70 N ANISOU 1299 N LYS A 641 3107 3131 2385 329 184 -174 N ATOM 1300 CA LYS A 641 21.064 7.042 36.343 1.00 22.71 C ANISOU 1300 CA LYS A 641 3165 3166 2296 385 180 -168 C ATOM 1301 C LYS A 641 21.666 5.661 36.482 1.00 23.41 C ANISOU 1301 C LYS A 641 3234 3262 2401 365 178 -117 C ATOM 1302 O LYS A 641 20.950 4.672 36.358 1.00 23.20 O ANISOU 1302 O LYS A 641 3165 3241 2410 357 234 -51 O ATOM 1303 CB LYS A 641 19.900 7.193 37.336 1.00 22.56 C ANISOU 1303 CB LYS A 641 3172 3186 2212 457 256 -135 C ATOM 1304 CG LYS A 641 19.138 8.506 37.245 1.00 23.43 C ANISOU 1304 CG LYS A 641 3301 3292 2311 487 272 -177 C ATOM 1305 CD LYS A 641 19.956 9.712 37.675 1.00 23.72 C ANISOU 1305 CD LYS A 641 3409 3317 2287 512 201 -263 C ATOM 1306 CE LYS A 641 19.079 10.965 37.710 1.00 19.81 C ANISOU 1306 CE LYS A 641 2936 2815 1774 552 228 -300 C ATOM 1307 NZ LYS A 641 19.716 12.115 38.419 1.00 20.31 N ANISOU 1307 NZ LYS A 641 3085 2870 1763 595 165 -382 N ATOM 1308 N ILE A 642 22.973 5.581 36.728 1.00 25.21 N ANISOU 1308 N ILE A 642 3485 3482 2610 356 110 -145 N ATOM 1309 CA ILE A 642 23.599 4.303 37.057 1.00 26.29 C ANISOU 1309 CA ILE A 642 3610 3627 2751 349 106 -96 C ATOM 1310 C ILE A 642 23.048 3.766 38.378 1.00 25.72 C ANISOU 1310 C ILE A 642 3574 3602 2598 414 157 -42 C ATOM 1311 O ILE A 642 22.957 4.500 39.359 1.00 28.68 O ANISOU 1311 O ILE A 642 4012 4003 2881 473 152 -68 O ATOM 1312 CB ILE A 642 25.114 4.439 37.151 1.00 18.39 C ANISOU 1312 CB ILE A 642 2629 2612 1747 333 21 -135 C ATOM 1313 CG1 ILE A 642 25.713 4.733 35.768 1.00 18.72 C ANISOU 1313 CG1 ILE A 642 2626 2609 1879 269 -15 -169 C ATOM 1314 CG2 ILE A 642 25.722 3.188 37.771 1.00 18.67 C ANISOU 1314 CG2 ILE A 642 2663 2662 1769 342 17 -81 C ATOM 1315 CD1 ILE A 642 27.212 5.145 35.795 1.00 17.69 C ANISOU 1315 CD1 ILE A 642 2505 2458 1758 252 -102 -210 C ATOM 1316 N ALA A 643 22.666 2.491 38.408 1.00 25.30 N ANISOU 1316 N ALA A 643 3481 3554 2577 406 207 35 N ATOM 1317 CA ALA A 643 22.047 1.908 39.605 1.00 25.34 C ANISOU 1317 CA ALA A 643 3512 3603 2514 467 268 102 C ATOM 1318 C ALA A 643 22.561 0.493 39.899 1.00 27.46 C ANISOU 1318 C ALA A 643 3760 3873 2801 457 270 168 C ATOM 1319 O ALA A 643 23.574 0.072 39.329 1.00 28.76 O ANISOU 1319 O ALA A 643 3905 4008 3016 411 214 151 O ATOM 1320 CB ALA A 643 20.541 1.907 39.460 1.00 26.34 C ANISOU 1320 CB ALA A 643 3603 3738 2668 481 356 149 C ATOM 1321 N ASP A 644 21.859 -0.214 40.794 1.00 29.03 N ANISOU 1321 N ASP A 644 3964 4106 2962 504 339 248 N ATOM 1322 CA ASP A 644 22.230 -1.549 41.304 1.00 30.19 C ANISOU 1322 CA ASP A 644 4098 4259 3113 508 351 323 C ATOM 1323 C ASP A 644 23.706 -1.642 41.740 1.00 29.46 C ANISOU 1323 C ASP A 644 4047 4168 2976 512 266 291 C ATOM 1324 O ASP A 644 24.589 -2.035 40.971 1.00 28.81 O ANISOU 1324 O ASP A 644 3933 4049 2966 458 213 270 O ATOM 1325 CB ASP A 644 21.908 -2.618 40.258 1.00 29.58 C ANISOU 1325 CB ASP A 644 3939 4136 3163 442 372 370 C ATOM 1326 CG ASP A 644 21.951 -4.033 40.821 1.00 29.55 C ANISOU 1326 CG ASP A 644 3915 4135 3175 451 404 464 C ATOM 1327 OD1 ASP A 644 22.456 -4.223 41.946 1.00 29.99 O ANISOU 1327 OD1 ASP A 644 4020 4229 3144 503 398 489 O ATOM 1328 OD2 ASP A 644 21.482 -4.964 40.128 1.00 29.28 O ANISOU 1328 OD2 ASP A 644 3818 4064 3243 406 431 512 O ATOM 1329 N PHE A 645 23.959 -1.289 42.992 1.00 30.16 N ANISOU 1329 N PHE A 645 4211 4301 2947 581 254 288 N ATOM 1330 CA PHE A 645 25.320 -1.232 43.511 1.00 30.32 C ANISOU 1330 CA PHE A 645 4277 4325 2919 590 163 254 C ATOM 1331 C PHE A 645 25.667 -2.453 44.321 1.00 29.79 C ANISOU 1331 C PHE A 645 4215 4278 2825 616 174 336 C ATOM 1332 O PHE A 645 26.507 -2.386 45.207 1.00 31.01 O ANISOU 1332 O PHE A 645 4427 4455 2899 654 114 326 O ATOM 1333 CB PHE A 645 25.513 0.038 44.341 1.00 31.42 C ANISOU 1333 CB PHE A 645 4506 4493 2941 648 118 184 C ATOM 1334 CG PHE A 645 25.615 1.257 43.494 1.00 31.57 C ANISOU 1334 CG PHE A 645 4518 4479 2997 612 74 93 C ATOM 1335 CD1 PHE A 645 24.476 1.881 43.023 1.00 30.86 C ANISOU 1335 CD1 PHE A 645 4412 4387 2926 613 137 81 C ATOM 1336 CD2 PHE A 645 26.852 1.729 43.086 1.00 31.66 C ANISOU 1336 CD2 PHE A 645 4529 4458 3042 572 -28 28 C ATOM 1337 CE1 PHE A 645 24.576 2.986 42.195 1.00 30.41 C ANISOU 1337 CE1 PHE A 645 4347 4297 2910 578 97 2 C ATOM 1338 CE2 PHE A 645 26.960 2.829 42.263 1.00 31.09 C ANISOU 1338 CE2 PHE A 645 4446 4353 3014 536 -66 -47 C ATOM 1339 CZ PHE A 645 25.827 3.459 41.816 1.00 30.55 C ANISOU 1339 CZ PHE A 645 4367 4283 2956 539 -4 -61 C ATOM 1340 N GLY A 646 25.035 -3.575 43.985 1.00 28.82 N ANISOU 1340 N GLY A 646 4030 4143 2776 594 244 417 N ATOM 1341 CA GLY A 646 25.166 -4.794 44.759 1.00 28.25 C ANISOU 1341 CA GLY A 646 3958 4089 2688 621 271 510 C ATOM 1342 C GLY A 646 26.456 -5.559 44.527 1.00 28.03 C ANISOU 1342 C GLY A 646 3908 4031 2710 585 199 513 C ATOM 1343 O GLY A 646 26.798 -6.448 45.293 1.00 28.06 O ANISOU 1343 O GLY A 646 3923 4051 2686 613 201 581 O ATOM 1344 N LEU A 647 27.176 -5.239 43.464 1.00 26.44 N ANISOU 1344 N LEU A 647 3674 3786 2588 525 139 445 N ATOM 1345 CA LEU A 647 28.448 -5.901 43.216 1.00 25.22 C ANISOU 1345 CA LEU A 647 3495 3602 2486 495 74 447 C ATOM 1346 C LEU A 647 29.602 -4.926 43.404 1.00 24.58 C ANISOU 1346 C LEU A 647 3453 3524 2362 499 -26 369 C ATOM 1347 O LEU A 647 30.774 -5.311 43.385 1.00 24.48 O ANISOU 1347 O LEU A 647 3426 3493 2381 485 -90 369 O ATOM 1348 CB LEU A 647 28.459 -6.500 41.811 1.00 23.88 C ANISOU 1348 CB LEU A 647 3249 3373 2451 425 89 444 C ATOM 1349 CG LEU A 647 27.750 -7.852 41.708 1.00 23.90 C ANISOU 1349 CG LEU A 647 3208 3356 2515 415 159 534 C ATOM 1350 CD1 LEU A 647 27.794 -8.376 40.286 1.00 23.43 C ANISOU 1350 CD1 LEU A 647 3087 3233 2581 349 163 518 C ATOM 1351 CD2 LEU A 647 28.423 -8.820 42.662 1.00 23.92 C ANISOU 1351 CD2 LEU A 647 3225 3374 2491 448 145 603 C ATOM 1352 N ALA A 648 29.236 -3.660 43.589 1.00 24.32 N ANISOU 1352 N ALA A 648 3465 3510 2264 520 -38 305 N ATOM 1353 CA ALA A 648 30.173 -2.549 43.685 1.00 24.97 C ANISOU 1353 CA ALA A 648 3584 3588 2315 519 -135 223 C ATOM 1354 C ALA A 648 31.146 -2.717 44.840 1.00 26.93 C ANISOU 1354 C ALA A 648 3884 3860 2487 562 -212 235 C ATOM 1355 O ALA A 648 30.795 -3.257 45.886 1.00 27.07 O ANISOU 1355 O ALA A 648 3947 3919 2420 618 -182 293 O ATOM 1356 CB ALA A 648 29.413 -1.251 43.832 1.00 25.26 C ANISOU 1356 CB ALA A 648 3670 3642 2287 545 -124 162 C ATOM 1357 N ARG A 649 32.376 -2.256 44.663 1.00 28.35 N ANISOU 1357 N ARG A 649 4059 4015 2699 537 -314 185 N ATOM 1358 CA ARG A 649 33.359 -2.384 45.732 1.00 30.10 C ANISOU 1358 CA ARG A 649 4327 4255 2855 573 -403 194 C ATOM 1359 C ARG A 649 34.228 -1.140 45.854 1.00 31.95 C ANISOU 1359 C ARG A 649 4594 4473 3073 567 -520 109 C ATOM 1360 O ARG A 649 34.461 -0.422 44.878 1.00 32.82 O ANISOU 1360 O ARG A 649 4662 4545 3265 516 -540 54 O ATOM 1361 CB ARG A 649 34.243 -3.616 45.500 1.00 29.41 C ANISOU 1361 CB ARG A 649 4177 4145 2851 546 -419 257 C ATOM 1362 CG ARG A 649 33.535 -4.970 45.587 1.00 29.36 C ANISOU 1362 CG ARG A 649 4145 4151 2858 558 -321 350 C ATOM 1363 CD ARG A 649 33.090 -5.269 47.001 1.00 28.73 C ANISOU 1363 CD ARG A 649 4142 4127 2648 633 -304 403 C ATOM 1364 NE ARG A 649 32.517 -6.602 47.111 1.00 29.78 N ANISOU 1364 NE ARG A 649 4243 4267 2807 641 -216 502 N ATOM 1365 CZ ARG A 649 31.265 -6.897 46.785 1.00 28.98 C ANISOU 1365 CZ ARG A 649 4120 4168 2724 638 -109 537 C ATOM 1366 NH1 ARG A 649 30.458 -5.947 46.330 1.00 28.94 N ANISOU 1366 NH1 ARG A 649 4122 4165 2710 630 -75 482 N ATOM 1367 NH2 ARG A 649 30.822 -8.142 46.902 1.00 29.08 N ANISOU 1367 NH2 ARG A 649 4099 4179 2772 642 -40 632 N ATOM 1368 N ASP A 650 34.694 -0.883 47.069 1.00 34.61 N ANISOU 1368 N ASP A 650 5009 4837 3305 619 -600 99 N ATOM 1369 CA ASP A 650 35.726 0.116 47.297 1.00 36.37 C ANISOU 1369 CA ASP A 650 5259 5036 3524 611 -735 27 C ATOM 1370 C ASP A 650 37.077 -0.498 46.958 1.00 37.14 C ANISOU 1370 C ASP A 650 5283 5100 3728 567 -808 56 C ATOM 1371 O ASP A 650 37.410 -1.556 47.497 1.00 37.52 O ANISOU 1371 O ASP A 650 5327 5166 3762 588 -808 126 O ATOM 1372 CB ASP A 650 35.717 0.584 48.752 1.00 39.72 C ANISOU 1372 CB ASP A 650 5803 5500 3790 688 -802 3 C ATOM 1373 CG ASP A 650 36.619 1.776 48.985 1.00 42.30 C ANISOU 1373 CG ASP A 650 6167 5794 4110 679 -947 -84 C ATOM 1374 OD1 ASP A 650 37.305 2.193 48.027 1.00 42.58 O ANISOU 1374 OD1 ASP A 650 6127 5780 4274 611 -992 -115 O ATOM 1375 OD2 ASP A 650 36.648 2.297 50.122 1.00 44.31 O ANISOU 1375 OD2 ASP A 650 6529 6072 4233 741 -1017 -119 O ATOM 1376 N ILE A 651 37.846 0.142 46.073 1.00 37.50 N ANISOU 1376 N ILE A 651 5268 5096 3884 508 -866 11 N ATOM 1377 CA ILE A 651 39.216 -0.302 45.799 1.00 37.73 C ANISOU 1377 CA ILE A 651 5226 5091 4017 471 -943 38 C ATOM 1378 C ILE A 651 40.252 0.801 46.006 1.00 38.06 C ANISOU 1378 C ILE A 651 5276 5102 4085 454 -1086 -24 C ATOM 1379 O ILE A 651 41.319 0.802 45.378 1.00 36.38 O ANISOU 1379 O ILE A 651 4981 4846 3995 407 -1140 -17 O ATOM 1380 CB ILE A 651 39.382 -0.864 44.365 1.00 35.72 C ANISOU 1380 CB ILE A 651 4863 4800 3909 411 -868 66 C ATOM 1381 CG1 ILE A 651 39.156 0.216 43.306 1.00 33.97 C ANISOU 1381 CG1 ILE A 651 4613 4546 3750 368 -853 2 C ATOM 1382 CG2 ILE A 651 38.473 -2.063 44.155 1.00 35.30 C ANISOU 1382 CG2 ILE A 651 4797 4768 3849 423 -743 131 C ATOM 1383 CD1 ILE A 651 39.859 -0.080 42.003 1.00 32.58 C ANISOU 1383 CD1 ILE A 651 4333 4324 3722 311 -829 20 C ATOM 1384 N ASN A 652 39.941 1.729 46.901 1.00 39.20 N ANISOU 1384 N ASN A 652 5518 5262 4112 496 -1149 -84 N ATOM 1385 CA ASN A 652 40.890 2.770 47.264 1.00 41.43 C ANISOU 1385 CA ASN A 652 5822 5510 4409 485 -1301 -145 C ATOM 1386 C ASN A 652 42.189 2.170 47.807 1.00 43.46 C ANISOU 1386 C ASN A 652 6051 5758 4706 482 -1413 -101 C ATOM 1387 O ASN A 652 42.160 1.231 48.595 1.00 46.90 O ANISOU 1387 O ASN A 652 6520 6231 5068 526 -1404 -45 O ATOM 1388 CB ASN A 652 40.270 3.716 48.291 1.00 40.72 C ANISOU 1388 CB ASN A 652 5863 5443 4166 544 -1349 -214 C ATOM 1389 CG ASN A 652 41.136 4.927 48.561 1.00 41.04 C ANISOU 1389 CG ASN A 652 5929 5436 4227 528 -1509 -290 C ATOM 1390 OD1 ASN A 652 41.809 5.434 47.661 1.00 40.06 O ANISOU 1390 OD1 ASN A 652 5719 5258 4244 462 -1549 -308 O ATOM 1391 ND2 ASN A 652 41.150 5.382 49.813 1.00 42.16 N ANISOU 1391 ND2 ASN A 652 6190 5595 4233 588 -1606 -334 N ATOM 1392 N ASN A 653 43.319 2.705 47.359 1.00 45.41 N ANISOU 1392 N ASN A 653 6228 5950 5075 431 -1515 -120 N ATOM 1393 CA ASN A 653 44.645 2.280 47.828 1.00 48.63 C ANISOU 1393 CA ASN A 653 6598 6341 5541 423 -1637 -80 C ATOM 1394 C ASN A 653 44.969 0.797 47.650 1.00 53.08 C ANISOU 1394 C ASN A 653 7092 6921 6157 423 -1571 16 C ATOM 1395 O ASN A 653 45.755 0.243 48.420 1.00 51.65 O ANISOU 1395 O ASN A 653 6914 6746 5966 443 -1658 58 O ATOM 1396 CB ASN A 653 44.833 2.628 49.314 1.00 51.13 C ANISOU 1396 CB ASN A 653 7032 6678 5718 480 -1771 -113 C ATOM 1397 CG ASN A 653 45.023 4.109 49.551 1.00 53.24 C ANISOU 1397 CG ASN A 653 7352 6906 5969 471 -1893 -209 C ATOM 1398 OD1 ASN A 653 45.541 4.829 48.698 1.00 53.53 O ANISOU 1398 OD1 ASN A 653 7311 6888 6140 410 -1927 -236 O ATOM 1399 ND2 ASN A 653 44.595 4.573 50.716 1.00 54.99 N ANISOU 1399 ND2 ASN A 653 7712 7156 6026 535 -1957 -261 N ATOM 1400 N ILE A 654 44.376 0.151 46.655 1.00 56.91 N ANISOU 1400 N ILE A 654 7518 7408 6696 403 -1423 52 N ATOM 1401 CA ILE A 654 44.711 -1.243 46.378 1.00 60.97 C ANISOU 1401 CA ILE A 654 7964 7927 7275 400 -1360 139 C ATOM 1402 C ILE A 654 44.602 -1.476 44.866 1.00 59.63 C ANISOU 1402 C ILE A 654 7697 7725 7235 350 -1248 152 C ATOM 1403 O ILE A 654 45.393 -2.212 44.282 1.00 60.82 O ANISOU 1403 O ILE A 654 7759 7850 7501 327 -1233 205 O ATOM 1404 CB ILE A 654 43.813 -2.221 47.205 1.00 50.75 C ANISOU 1404 CB ILE A 654 6742 6689 5852 459 -1287 187 C ATOM 1405 CG1 ILE A 654 44.269 -3.673 47.034 1.00 51.75 C ANISOU 1405 CG1 ILE A 654 6800 6813 6048 458 -1240 279 C ATOM 1406 CG2 ILE A 654 42.343 -2.064 46.873 1.00 49.37 C ANISOU 1406 CG2 ILE A 654 6612 6541 5608 470 -1158 162 C ATOM 1407 CD1 ILE A 654 43.587 -4.655 47.991 1.00 52.73 C ANISOU 1407 CD1 ILE A 654 6992 6988 6056 517 -1190 338 C ATOM 1408 N ASP A 655 43.628 -0.807 44.253 1.00 60.30 N ANISOU 1408 N ASP A 655 7804 7811 7295 337 -1173 101 N ATOM 1409 CA ASP A 655 43.456 -0.696 42.796 1.00 61.50 C ANISOU 1409 CA ASP A 655 7882 7932 7554 290 -1083 94 C ATOM 1410 C ASP A 655 43.158 -1.990 42.044 1.00 58.30 C ANISOU 1410 C ASP A 655 7426 7526 7200 285 -961 155 C ATOM 1411 O ASP A 655 43.330 -2.069 40.828 1.00 56.90 O ANISOU 1411 O ASP A 655 7179 7316 7124 249 -901 159 O ATOM 1412 CB ASP A 655 44.676 -0.019 42.180 1.00 68.87 C ANISOU 1412 CB ASP A 655 8735 8814 8619 245 -1160 82 C ATOM 1413 CG ASP A 655 44.530 1.489 42.146 1.00 77.62 C ANISOU 1413 CG ASP A 655 9876 9904 9714 227 -1223 4 C ATOM 1414 OD1 ASP A 655 43.981 2.014 41.147 1.00 83.58 O ANISOU 1414 OD1 ASP A 655 10610 10644 10503 200 -1149 -25 O ATOM 1415 OD2 ASP A 655 44.938 2.144 43.132 1.00 79.98 O ANISOU 1415 OD2 ASP A 655 10224 10202 9963 243 -1348 -28 O ATOM 1416 N PHE A 656 42.684 -2.987 42.777 1.00 55.25 N ANISOU 1416 N PHE A 656 7079 7174 6739 324 -926 202 N ATOM 1417 CA PHE A 656 42.052 -4.157 42.192 1.00 50.36 C ANISOU 1417 CA PHE A 656 6434 6556 6144 324 -806 251 C ATOM 1418 C PHE A 656 41.160 -4.735 43.277 1.00 45.26 C ANISOU 1418 C PHE A 656 5863 5958 5374 373 -777 282 C ATOM 1419 O PHE A 656 41.430 -4.540 44.459 1.00 43.43 O ANISOU 1419 O PHE A 656 5689 5755 5059 410 -857 285 O ATOM 1420 CB PHE A 656 43.084 -5.184 41.702 1.00 50.72 C ANISOU 1420 CB PHE A 656 6398 6569 6306 311 -800 311 C ATOM 1421 CG PHE A 656 43.795 -5.899 42.806 1.00 51.38 C ANISOU 1421 CG PHE A 656 6489 6667 6364 345 -870 367 C ATOM 1422 CD1 PHE A 656 44.894 -5.324 43.429 1.00 52.96 C ANISOU 1422 CD1 PHE A 656 6682 6861 6579 346 -1000 359 C ATOM 1423 CD2 PHE A 656 43.370 -7.148 43.228 1.00 50.60 C ANISOU 1423 CD2 PHE A 656 6407 6587 6234 375 -813 431 C ATOM 1424 CE1 PHE A 656 45.551 -5.980 44.463 1.00 53.72 C ANISOU 1424 CE1 PHE A 656 6789 6973 6651 379 -1073 412 C ATOM 1425 CE2 PHE A 656 44.030 -7.812 44.256 1.00 51.49 C ANISOU 1425 CE2 PHE A 656 6529 6714 6322 408 -879 488 C ATOM 1426 CZ PHE A 656 45.120 -7.223 44.872 1.00 53.05 C ANISOU 1426 CZ PHE A 656 6722 6909 6528 411 -1010 478 C ATOM 1427 N PHE A 657 40.084 -5.407 42.884 1.00 40.15 N ANISOU 1427 N PHE A 657 5220 5319 4716 376 -664 307 N ATOM 1428 CA PHE A 657 39.308 -6.185 43.830 1.00 37.21 C ANISOU 1428 CA PHE A 657 4900 4987 4250 421 -622 360 C ATOM 1429 C PHE A 657 39.418 -7.643 43.431 1.00 37.01 C ANISOU 1429 C PHE A 657 4820 4939 4302 414 -559 434 C ATOM 1430 O PHE A 657 39.177 -7.991 42.286 1.00 34.59 O ANISOU 1430 O PHE A 657 4464 4597 4081 379 -491 431 O ATOM 1431 CB PHE A 657 37.846 -5.741 43.873 1.00 33.64 C ANISOU 1431 CB PHE A 657 4499 4563 3718 435 -545 335 C ATOM 1432 CG PHE A 657 37.006 -6.535 44.841 1.00 31.25 C ANISOU 1432 CG PHE A 657 4246 4303 3326 484 -490 400 C ATOM 1433 CD1 PHE A 657 37.132 -6.337 46.215 1.00 30.76 C ANISOU 1433 CD1 PHE A 657 4260 4286 3144 541 -547 412 C ATOM 1434 CD2 PHE A 657 36.105 -7.490 44.379 1.00 29.56 C ANISOU 1434 CD2 PHE A 657 4001 4080 3149 476 -384 452 C ATOM 1435 CE1 PHE A 657 36.371 -7.081 47.117 1.00 30.29 C ANISOU 1435 CE1 PHE A 657 4244 4267 2998 592 -489 481 C ATOM 1436 CE2 PHE A 657 35.339 -8.229 45.265 1.00 29.29 C ANISOU 1436 CE2 PHE A 657 4004 4082 3043 520 -330 522 C ATOM 1437 CZ PHE A 657 35.480 -8.031 46.643 1.00 29.64 C ANISOU 1437 CZ PHE A 657 4122 4175 2963 581 -377 540 C ATOM 1438 N LYS A 658 39.811 -8.493 44.372 1.00 40.28 N ANISOU 1438 N LYS A 658 5248 5371 4684 450 -587 500 N ATOM 1439 CA LYS A 658 39.954 -9.912 44.094 1.00 42.54 C ANISOU 1439 CA LYS A 658 5487 5632 5045 448 -533 574 C ATOM 1440 C LYS A 658 38.843 -10.688 44.777 1.00 47.16 C ANISOU 1440 C LYS A 658 6114 6248 5556 482 -460 634 C ATOM 1441 O LYS A 658 38.788 -10.775 46.004 1.00 48.81 O ANISOU 1441 O LYS A 658 6379 6501 5665 530 -491 670 O ATOM 1442 CB LYS A 658 41.319 -10.418 44.546 1.00 40.36 C ANISOU 1442 CB LYS A 658 5179 5343 4812 460 -616 616 C ATOM 1443 CG LYS A 658 41.557 -11.862 44.202 1.00 37.27 C ANISOU 1443 CG LYS A 658 4736 4919 4508 459 -563 689 C ATOM 1444 CD LYS A 658 42.772 -12.385 44.916 1.00 35.13 C ANISOU 1444 CD LYS A 658 4443 4645 4259 483 -646 742 C ATOM 1445 CE LYS A 658 43.096 -13.785 44.437 1.00 33.02 C ANISOU 1445 CE LYS A 658 4118 4335 4095 481 -592 810 C ATOM 1446 NZ LYS A 658 44.213 -14.410 45.197 1.00 32.67 N ANISOU 1446 NZ LYS A 658 4052 4289 4074 509 -668 874 N ATOM 1447 N GLU A 659 37.951 -11.238 43.963 1.00 53.21 N ANISOU 1447 N GLU A 659 6853 6990 6375 459 -363 647 N ATOM 1448 CA GLU A 659 36.813 -11.992 44.455 1.00 60.69 C ANISOU 1448 CA GLU A 659 7824 7957 7278 483 -284 711 C ATOM 1449 C GLU A 659 37.249 -13.391 44.875 1.00 67.18 C ANISOU 1449 C GLU A 659 8622 8763 8140 502 -276 802 C ATOM 1450 O GLU A 659 37.809 -14.142 44.073 1.00 68.78 O ANISOU 1450 O GLU A 659 8766 8913 8454 474 -267 816 O ATOM 1451 CB GLU A 659 35.729 -12.060 43.380 1.00 63.26 C ANISOU 1451 CB GLU A 659 8123 8254 7660 445 -196 691 C ATOM 1452 CG GLU A 659 34.483 -12.783 43.806 1.00 66.78 C ANISOU 1452 CG GLU A 659 8581 8714 8077 464 -113 759 C ATOM 1453 CD GLU A 659 33.838 -12.159 45.026 1.00 69.78 C ANISOU 1453 CD GLU A 659 9031 9161 8320 516 -108 772 C ATOM 1454 OE1 GLU A 659 33.954 -10.925 45.207 1.00 71.26 O ANISOU 1454 OE1 GLU A 659 9260 9378 8439 526 -153 701 O ATOM 1455 OE2 GLU A 659 33.227 -12.911 45.813 1.00 73.35 O ANISOU 1455 OE2 GLU A 659 9500 9637 8733 552 -58 855 O ATOM 1456 N THR A 660 37.008 -13.737 46.136 1.00 72.87 N ANISOU 1456 N THR A 660 9391 9529 8767 553 -279 867 N ATOM 1457 CA THR A 660 37.466 -15.023 46.656 1.00 78.12 C ANISOU 1457 CA THR A 660 10037 10182 9462 575 -280 960 C ATOM 1458 C THR A 660 36.325 -16.045 46.734 1.00 83.38 C ANISOU 1458 C THR A 660 10695 10840 10144 581 -178 1039 C ATOM 1459 O THR A 660 36.546 -17.250 46.594 1.00 82.99 O ANISOU 1459 O THR A 660 10606 10751 10176 577 -155 1107 O ATOM 1460 CB THR A 660 38.130 -14.856 48.040 1.00 79.88 C ANISOU 1460 CB THR A 660 10317 10456 9576 631 -362 991 C ATOM 1461 OG1 THR A 660 37.178 -14.324 48.970 1.00 81.46 O ANISOU 1461 OG1 THR A 660 10595 10719 9638 676 -334 998 O ATOM 1462 CG2 THR A 660 39.347 -13.928 47.948 1.00 79.42 C ANISOU 1462 CG2 THR A 660 10255 10395 9524 618 -475 919 C ATOM 1463 N THR A 661 35.111 -15.550 46.957 1.00 87.72 N ANISOU 1463 N THR A 661 11281 11424 10624 593 -119 1034 N ATOM 1464 CA THR A 661 33.899 -16.365 46.894 1.00 92.10 C ANISOU 1464 CA THR A 661 11817 11967 11209 590 -19 1104 C ATOM 1465 C THR A 661 33.562 -16.516 45.418 1.00 93.16 C ANISOU 1465 C THR A 661 11892 12035 11469 526 17 1058 C ATOM 1466 O THR A 661 34.025 -15.719 44.612 1.00 94.77 O ANISOU 1466 O THR A 661 12085 12223 11698 494 -21 968 O ATOM 1467 CB THR A 661 32.742 -15.705 47.709 1.00 84.57 C ANISOU 1467 CB THR A 661 10922 11078 10134 632 33 1119 C ATOM 1468 OG1 THR A 661 32.758 -16.217 49.046 1.00 85.79 O ANISOU 1468 OG1 THR A 661 11121 11278 10196 696 39 1210 O ATOM 1469 CG2 THR A 661 31.364 -15.939 47.103 1.00 84.10 C ANISOU 1469 CG2 THR A 661 10827 10995 10131 605 131 1141 C ATOM 1470 N ASN A 662 32.821 -17.549 45.028 1.00 96.62 N ANISOU 1470 N ASN A 662 12291 12430 11991 505 85 1118 N ATOM 1471 CA ASN A 662 32.295 -17.582 43.661 1.00 98.57 C ANISOU 1471 CA ASN A 662 12495 12618 12340 448 118 1067 C ATOM 1472 C ASN A 662 31.181 -16.530 43.525 1.00 94.08 C ANISOU 1472 C ASN A 662 11946 12083 11716 442 154 1023 C ATOM 1473 O ASN A 662 31.357 -15.397 43.980 1.00 95.26 O ANISOU 1473 O ASN A 662 12140 12286 11767 466 122 972 O ATOM 1474 CB ASN A 662 31.866 -19.021 43.281 1.00101.86 C ANISOU 1474 CB ASN A 662 12865 12967 12869 426 166 1142 C ATOM 1475 CG ASN A 662 30.542 -19.458 43.909 1.00105.65 C ANISOU 1475 CG ASN A 662 13344 13464 13335 441 239 1230 C ATOM 1476 OD1 ASN A 662 29.925 -18.727 44.684 1.00107.13 O ANISOU 1476 OD1 ASN A 662 13567 13718 13420 475 264 1241 O ATOM 1477 ND2 ASN A 662 30.107 -20.662 43.568 1.00108.27 N ANISOU 1477 ND2 ASN A 662 13632 13732 13773 418 276 1294 N ATOM 1478 N GLY A 663 30.062 -16.858 42.893 1.00 86.49 N ANISOU 1478 N GLY A 663 10954 11088 10820 410 214 1038 N ATOM 1479 CA GLY A 663 28.928 -15.965 42.981 1.00 82.16 C ANISOU 1479 CA GLY A 663 10422 10578 10217 414 256 1019 C ATOM 1480 C GLY A 663 28.130 -15.675 41.732 1.00 74.50 C ANISOU 1480 C GLY A 663 9419 9565 9324 360 279 966 C ATOM 1481 O GLY A 663 28.283 -16.312 40.687 1.00 74.76 O ANISOU 1481 O GLY A 663 9414 9528 9462 315 271 947 O ATOM 1482 N ARG A 664 27.227 -14.714 41.874 1.00 67.41 N ANISOU 1482 N ARG A 664 8537 8707 8368 370 309 943 N ATOM 1483 CA ARG A 664 26.485 -14.197 40.752 1.00 60.54 C ANISOU 1483 CA ARG A 664 7642 7806 7554 324 322 884 C ATOM 1484 C ARG A 664 27.496 -13.486 39.861 1.00 54.51 C ANISOU 1484 C ARG A 664 6889 7025 6797 297 258 780 C ATOM 1485 O ARG A 664 28.242 -12.612 40.293 1.00 54.20 O ANISOU 1485 O ARG A 664 6887 7027 6679 323 216 733 O ATOM 1486 CB ARG A 664 25.341 -13.295 41.246 1.00 61.49 C ANISOU 1486 CB ARG A 664 7778 7978 7605 350 371 891 C ATOM 1487 CG ARG A 664 25.671 -11.820 41.429 1.00 62.24 C ANISOU 1487 CG ARG A 664 7924 8124 7600 374 337 805 C ATOM 1488 CD ARG A 664 24.484 -11.040 41.974 1.00 63.51 C ANISOU 1488 CD ARG A 664 8102 8333 7696 408 396 821 C ATOM 1489 NE ARG A 664 23.336 -11.121 41.076 1.00 63.71 N ANISOU 1489 NE ARG A 664 8075 8321 7812 365 438 828 N ATOM 1490 CZ ARG A 664 22.113 -11.470 41.451 1.00 64.44 C ANISOU 1490 CZ ARG A 664 8137 8421 7925 379 512 910 C ATOM 1491 NH1 ARG A 664 21.858 -11.752 42.719 1.00 65.07 N ANISOU 1491 NH1 ARG A 664 8239 8550 7933 440 562 993 N ATOM 1492 NH2 ARG A 664 21.141 -11.519 40.559 1.00 65.24 N ANISOU 1492 NH2 ARG A 664 8185 8482 8119 334 535 911 N ATOM 1493 N LEU A 665 27.592 -13.939 38.627 1.00 49.04 N ANISOU 1493 N LEU A 665 6162 6266 6203 249 247 747 N ATOM 1494 CA LEU A 665 28.537 -13.347 37.707 1.00 43.52 C ANISOU 1494 CA LEU A 665 5469 5547 5519 226 198 658 C ATOM 1495 C LEU A 665 27.804 -12.999 36.445 1.00 38.45 C ANISOU 1495 C LEU A 665 4810 4868 4931 181 209 605 C ATOM 1496 O LEU A 665 27.241 -13.877 35.800 1.00 39.60 O ANISOU 1496 O LEU A 665 4929 4959 5160 151 228 629 O ATOM 1497 CB LEU A 665 29.682 -14.300 37.398 1.00 42.51 C ANISOU 1497 CB LEU A 665 5326 5374 5451 220 169 668 C ATOM 1498 CG LEU A 665 30.591 -14.753 38.537 1.00 42.46 C ANISOU 1498 CG LEU A 665 5332 5396 5405 262 146 722 C ATOM 1499 CD1 LEU A 665 31.545 -15.830 38.000 1.00 42.14 C ANISOU 1499 CD1 LEU A 665 5265 5295 5451 251 129 735 C ATOM 1500 CD2 LEU A 665 31.352 -13.577 39.170 1.00 42.41 C ANISOU 1500 CD2 LEU A 665 5360 5448 5305 290 97 677 C ATOM 1501 N PRO A 666 27.791 -11.712 36.095 1.00 34.97 N ANISOU 1501 N PRO A 666 4387 4453 4446 176 192 534 N ATOM 1502 CA PRO A 666 27.164 -11.246 34.856 1.00 30.84 C ANISOU 1502 CA PRO A 666 3853 3899 3967 135 196 479 C ATOM 1503 C PRO A 666 28.106 -11.503 33.682 1.00 29.85 C ANISOU 1503 C PRO A 666 3721 3722 3898 109 165 427 C ATOM 1504 O PRO A 666 28.632 -10.576 33.052 1.00 28.88 O ANISOU 1504 O PRO A 666 3609 3604 3760 100 140 360 O ATOM 1505 CB PRO A 666 26.951 -9.762 35.120 1.00 31.58 C ANISOU 1505 CB PRO A 666 3971 4045 3982 150 188 429 C ATOM 1506 CG PRO A 666 28.092 -9.405 36.045 1.00 32.60 C ANISOU 1506 CG PRO A 666 4128 4214 4044 186 152 424 C ATOM 1507 CD PRO A 666 28.356 -10.604 36.887 1.00 33.65 C ANISOU 1507 CD PRO A 666 4255 4346 4184 210 163 502 C ATOM 1508 N VAL A 667 28.303 -12.786 33.408 1.00 29.34 N ANISOU 1508 N VAL A 667 3641 3605 3902 100 171 463 N ATOM 1509 CA VAL A 667 29.344 -13.278 32.517 1.00 28.82 C ANISOU 1509 CA VAL A 667 3572 3489 3887 90 150 430 C ATOM 1510 C VAL A 667 29.435 -12.553 31.175 1.00 23.54 C ANISOU 1510 C VAL A 667 2913 2798 3232 65 139 351 C ATOM 1511 O VAL A 667 30.533 -12.279 30.700 1.00 22.94 O ANISOU 1511 O VAL A 667 2842 2717 3159 71 121 313 O ATOM 1512 CB VAL A 667 29.154 -14.806 32.289 1.00 19.33 C ANISOU 1512 CB VAL A 667 2356 2223 2766 81 164 479 C ATOM 1513 CG1 VAL A 667 30.044 -15.330 31.180 1.00 18.73 C ANISOU 1513 CG1 VAL A 667 2285 2087 2746 73 150 437 C ATOM 1514 CG2 VAL A 667 29.417 -15.568 33.604 1.00 19.47 C ANISOU 1514 CG2 VAL A 667 2365 2262 2773 112 172 561 C ATOM 1515 N LYS A 668 28.306 -12.200 30.570 1.00 21.31 N ANISOU 1515 N LYS A 668 2632 2506 2959 38 149 330 N ATOM 1516 CA LYS A 668 28.378 -11.574 29.256 1.00 19.45 C ANISOU 1516 CA LYS A 668 2410 2247 2734 16 137 259 C ATOM 1517 C LYS A 668 28.770 -10.106 29.303 1.00 19.58 C ANISOU 1517 C LYS A 668 2436 2314 2690 23 124 213 C ATOM 1518 O LYS A 668 28.897 -9.479 28.259 1.00 19.27 O ANISOU 1518 O LYS A 668 2407 2261 2655 8 117 159 O ATOM 1519 CB LYS A 668 27.066 -11.727 28.514 1.00 20.79 C ANISOU 1519 CB LYS A 668 2578 2383 2940 -16 142 251 C ATOM 1520 CG LYS A 668 26.842 -13.130 28.023 1.00 22.44 C ANISOU 1520 CG LYS A 668 2784 2520 3223 -31 141 274 C ATOM 1521 CD LYS A 668 25.751 -13.188 27.000 1.00 22.80 C ANISOU 1521 CD LYS A 668 2834 2520 3308 -67 128 248 C ATOM 1522 CE LYS A 668 25.573 -14.628 26.529 1.00 22.98 C ANISOU 1522 CE LYS A 668 2860 2462 3410 -81 117 267 C ATOM 1523 NZ LYS A 668 24.636 -14.781 25.370 1.00 22.33 N ANISOU 1523 NZ LYS A 668 2790 2322 3371 -117 88 232 N ATOM 1524 N TRP A 669 29.001 -9.562 30.498 1.00 20.46 N ANISOU 1524 N TRP A 669 2548 2480 2746 48 118 233 N ATOM 1525 CA TRP A 669 29.467 -8.178 30.610 1.00 20.38 C ANISOU 1525 CA TRP A 669 2549 2511 2684 56 96 188 C ATOM 1526 C TRP A 669 30.905 -8.113 31.168 1.00 19.91 C ANISOU 1526 C TRP A 669 2486 2466 2612 79 66 191 C ATOM 1527 O TRP A 669 31.477 -7.026 31.327 1.00 18.89 O ANISOU 1527 O TRP A 669 2363 2365 2451 84 37 157 O ATOM 1528 CB TRP A 669 28.515 -7.362 31.488 1.00 21.23 C ANISOU 1528 CB TRP A 669 2667 2669 2732 68 104 196 C ATOM 1529 CG TRP A 669 27.217 -6.984 30.825 1.00 16.59 C ANISOU 1529 CG TRP A 669 2076 2072 2157 45 126 180 C ATOM 1530 CD1 TRP A 669 26.885 -5.757 30.290 1.00 16.23 C ANISOU 1530 CD1 TRP A 669 2039 2038 2091 34 118 129 C ATOM 1531 CD2 TRP A 669 26.066 -7.823 30.628 1.00 16.77 C ANISOU 1531 CD2 TRP A 669 2082 2067 2224 28 153 220 C ATOM 1532 NE1 TRP A 669 25.616 -5.791 29.775 1.00 16.23 N ANISOU 1532 NE1 TRP A 669 2028 2022 2116 13 138 134 N ATOM 1533 CE2 TRP A 669 25.091 -7.047 29.960 1.00 16.51 C ANISOU 1533 CE2 TRP A 669 2046 2032 2194 8 158 189 C ATOM 1534 CE3 TRP A 669 25.768 -9.155 30.942 1.00 17.18 C ANISOU 1534 CE3 TRP A 669 2117 2091 2320 27 171 281 C ATOM 1535 CZ2 TRP A 669 23.841 -7.556 29.614 1.00 16.66 C ANISOU 1535 CZ2 TRP A 669 2044 2024 2262 -15 176 219 C ATOM 1536 CZ3 TRP A 669 24.528 -9.658 30.590 1.00 17.33 C ANISOU 1536 CZ3 TRP A 669 2115 2081 2390 3 190 310 C ATOM 1537 CH2 TRP A 669 23.585 -8.865 29.932 1.00 17.08 C ANISOU 1537 CH2 TRP A 669 2079 2048 2364 -18 190 279 C ATOM 1538 N MET A 670 31.498 -9.269 31.460 1.00 19.25 N ANISOU 1538 N MET A 670 2392 2362 2562 91 68 234 N ATOM 1539 CA MET A 670 32.802 -9.284 32.136 1.00 19.04 C ANISOU 1539 CA MET A 670 2356 2351 2526 115 35 249 C ATOM 1540 C MET A 670 34.022 -9.355 31.206 1.00 18.91 C ANISOU 1540 C MET A 670 2320 2299 2565 110 25 225 C ATOM 1541 O MET A 670 34.035 -10.088 30.218 1.00 17.31 O ANISOU 1541 O MET A 670 2113 2049 2416 100 52 219 O ATOM 1542 CB MET A 670 32.856 -10.445 33.124 1.00 20.00 C ANISOU 1542 CB MET A 670 2474 2474 2650 138 40 319 C ATOM 1543 CG MET A 670 31.962 -10.253 34.328 1.00 20.50 C ANISOU 1543 CG MET A 670 2558 2587 2646 157 48 354 C ATOM 1544 SD MET A 670 31.818 -11.697 35.394 1.00 31.80 S ANISOU 1544 SD MET A 670 3984 4016 4082 183 67 448 S ATOM 1545 CE MET A 670 33.537 -11.900 35.918 1.00 33.96 C ANISOU 1545 CE MET A 670 4249 4294 4359 209 14 460 C ATOM 1546 N ALA A 671 35.052 -8.582 31.532 1.00 19.41 N ANISOU 1546 N ALA A 671 2373 2385 2617 120 -14 211 N ATOM 1547 CA ALA A 671 36.319 -8.685 30.824 1.00 17.51 C ANISOU 1547 CA ALA A 671 2104 2115 2436 122 -20 204 C ATOM 1548 C ALA A 671 36.877 -10.102 30.999 1.00 25.01 C ANISOU 1548 C ALA A 671 3037 3033 3432 141 -7 254 C ATOM 1549 O ALA A 671 36.545 -10.782 31.974 1.00 18.24 O ANISOU 1549 O ALA A 671 2187 2189 2553 155 -12 299 O ATOM 1550 CB ALA A 671 37.289 -7.646 31.333 1.00 17.66 C ANISOU 1550 CB ALA A 671 2106 2161 2443 128 -73 192 C ATOM 1551 N PRO A 672 37.703 -10.569 30.046 1.00 24.26 N ANISOU 1551 N PRO A 672 2921 2895 3402 146 15 251 N ATOM 1552 CA PRO A 672 38.232 -11.937 30.190 1.00 23.99 C ANISOU 1552 CA PRO A 672 2872 2826 3417 168 29 298 C ATOM 1553 C PRO A 672 39.087 -12.131 31.457 1.00 26.07 C ANISOU 1553 C PRO A 672 3111 3116 3678 191 -16 348 C ATOM 1554 O PRO A 672 39.003 -13.202 32.068 1.00 26.98 O ANISOU 1554 O PRO A 672 3227 3220 3804 207 -12 397 O ATOM 1555 CB PRO A 672 39.067 -12.124 28.919 1.00 23.00 C ANISOU 1555 CB PRO A 672 2730 2655 3353 175 62 277 C ATOM 1556 CG PRO A 672 38.475 -11.159 27.930 1.00 21.81 C ANISOU 1556 CG PRO A 672 2601 2507 3178 152 79 220 C ATOM 1557 CD PRO A 672 38.080 -9.963 28.755 1.00 21.62 C ANISOU 1557 CD PRO A 672 2580 2539 3096 136 37 207 C ATOM 1558 N GLU A 673 39.860 -11.119 31.864 1.00 27.79 N ANISOU 1558 N GLU A 673 3310 3366 3883 192 -64 338 N ATOM 1559 CA GLU A 673 40.666 -11.232 33.089 1.00 29.94 C ANISOU 1559 CA GLU A 673 3565 3664 4149 213 -121 383 C ATOM 1560 C GLU A 673 39.799 -11.419 34.313 1.00 30.18 C ANISOU 1560 C GLU A 673 3633 3733 4102 222 -139 409 C ATOM 1561 O GLU A 673 40.235 -12.013 35.281 1.00 29.51 O ANISOU 1561 O GLU A 673 3543 3660 4010 246 -170 460 O ATOM 1562 CB GLU A 673 41.546 -10.009 33.327 1.00 32.69 C ANISOU 1562 CB GLU A 673 3888 4035 4497 208 -183 362 C ATOM 1563 CG GLU A 673 41.824 -9.200 32.108 1.00 35.08 C ANISOU 1563 CG GLU A 673 4171 4318 4840 188 -159 317 C ATOM 1564 CD GLU A 673 40.756 -8.155 31.832 1.00 37.52 C ANISOU 1564 CD GLU A 673 4519 4649 5088 164 -152 262 C ATOM 1565 OE1 GLU A 673 40.479 -7.292 32.708 1.00 38.69 O ANISOU 1565 OE1 GLU A 673 4689 4836 5176 160 -204 246 O ATOM 1566 OE2 GLU A 673 40.173 -8.244 30.728 1.00 40.16 O ANISOU 1566 OE2 GLU A 673 4865 4960 5434 151 -95 235 O ATOM 1567 N ALA A 674 38.590 -10.879 34.300 1.00 29.66 N ANISOU 1567 N ALA A 674 3604 3689 3977 207 -120 378 N ATOM 1568 CA ALA A 674 37.724 -11.019 35.459 1.00 29.48 C ANISOU 1568 CA ALA A 674 3617 3706 3879 223 -125 408 C ATOM 1569 C ALA A 674 37.082 -12.414 35.459 1.00 29.94 C ANISOU 1569 C ALA A 674 3676 3736 3965 228 -74 460 C ATOM 1570 O ALA A 674 36.934 -13.033 36.513 1.00 30.72 O ANISOU 1570 O ALA A 674 3785 3854 4032 252 -81 517 O ATOM 1571 CB ALA A 674 36.675 -9.926 35.474 1.00 28.09 C ANISOU 1571 CB ALA A 674 3474 3561 3636 209 -118 362 C ATOM 1572 N LEU A 675 36.729 -12.910 34.270 1.00 29.54 N ANISOU 1572 N LEU A 675 3615 3634 3973 207 -28 441 N ATOM 1573 CA LEU A 675 36.176 -14.253 34.117 1.00 30.17 C ANISOU 1573 CA LEU A 675 3694 3673 4098 207 13 484 C ATOM 1574 C LEU A 675 37.179 -15.273 34.614 1.00 32.14 C ANISOU 1574 C LEU A 675 3921 3902 4390 234 -1 541 C ATOM 1575 O LEU A 675 36.814 -16.274 35.239 1.00 32.54 O ANISOU 1575 O LEU A 675 3973 3943 4449 246 13 602 O ATOM 1576 CB LEU A 675 35.799 -14.541 32.648 1.00 28.89 C ANISOU 1576 CB LEU A 675 3532 3453 3993 181 52 441 C ATOM 1577 CG LEU A 675 34.512 -13.842 32.171 1.00 28.05 C ANISOU 1577 CG LEU A 675 3448 3357 3854 153 70 400 C ATOM 1578 CD1 LEU A 675 34.188 -14.065 30.696 1.00 26.96 C ANISOU 1578 CD1 LEU A 675 3317 3163 3765 130 96 354 C ATOM 1579 CD2 LEU A 675 33.333 -14.254 33.044 1.00 27.96 C ANISOU 1579 CD2 LEU A 675 3446 3364 3815 153 86 450 C ATOM 1580 N PHE A 676 38.452 -14.996 34.358 1.00 34.99 N ANISOU 1580 N PHE A 676 4255 4257 4783 244 -29 527 N ATOM 1581 CA PHE A 676 39.499 -15.971 34.611 1.00 37.27 C ANISOU 1581 CA PHE A 676 4514 4518 5130 270 -39 578 C ATOM 1582 C PHE A 676 40.168 -15.841 35.981 1.00 39.56 C ANISOU 1582 C PHE A 676 4798 4854 5380 296 -98 626 C ATOM 1583 O PHE A 676 40.231 -16.810 36.724 1.00 39.51 O ANISOU 1583 O PHE A 676 4789 4842 5381 318 -101 691 O ATOM 1584 CB PHE A 676 40.558 -15.887 33.517 1.00 38.16 C ANISOU 1584 CB PHE A 676 4594 4591 5313 271 -29 547 C ATOM 1585 CG PHE A 676 41.541 -17.016 33.558 1.00 39.77 C ANISOU 1585 CG PHE A 676 4766 4754 5593 300 -25 598 C ATOM 1586 CD1 PHE A 676 41.147 -18.300 33.209 1.00 40.16 C ANISOU 1586 CD1 PHE A 676 4825 4747 5688 308 18 622 C ATOM 1587 CD2 PHE A 676 42.857 -16.800 33.957 1.00 41.00 C ANISOU 1587 CD2 PHE A 676 4879 4921 5778 321 -67 623 C ATOM 1588 CE1 PHE A 676 42.047 -19.348 33.252 1.00 41.30 C ANISOU 1588 CE1 PHE A 676 4939 4848 5903 338 24 669 C ATOM 1589 CE2 PHE A 676 43.771 -17.841 34.000 1.00 42.12 C ANISOU 1589 CE2 PHE A 676 4986 5023 5995 351 -62 674 C ATOM 1590 CZ PHE A 676 43.367 -19.119 33.646 1.00 42.18 C ANISOU 1590 CZ PHE A 676 5006 4976 6044 361 -13 696 C ATOM 1591 N ASP A 677 40.678 -14.655 36.303 1.00 40.60 N ANISOU 1591 N ASP A 677 4927 5026 5472 294 -151 595 N ATOM 1592 CA ASP A 677 41.390 -14.435 37.558 1.00 43.02 C ANISOU 1592 CA ASP A 677 5233 5374 5738 318 -223 631 C ATOM 1593 C ASP A 677 40.475 -14.019 38.696 1.00 43.22 C ANISOU 1593 C ASP A 677 5312 5456 5653 330 -241 640 C ATOM 1594 O ASP A 677 40.920 -13.920 39.832 1.00 45.30 O ANISOU 1594 O ASP A 677 5591 5756 5866 356 -300 673 O ATOM 1595 CB ASP A 677 42.451 -13.353 37.388 1.00 44.27 C ANISOU 1595 CB ASP A 677 5363 5542 5916 311 -283 594 C ATOM 1596 CG ASP A 677 43.380 -13.619 36.224 1.00 46.10 C ANISOU 1596 CG ASP A 677 5539 5722 6255 305 -256 587 C ATOM 1597 OD1 ASP A 677 43.750 -14.793 36.007 1.00 49.16 O ANISOU 1597 OD1 ASP A 677 5902 6069 6706 322 -224 631 O ATOM 1598 OD2 ASP A 677 43.739 -12.649 35.519 1.00 47.02 O ANISOU 1598 OD2 ASP A 677 5636 5834 6394 285 -263 539 O ATOM 1599 N ARG A 678 39.213 -13.736 38.384 1.00 42.33 N ANISOU 1599 N ARG A 678 5231 5352 5501 313 -191 612 N ATOM 1600 CA ARG A 678 38.274 -13.201 39.364 1.00 42.05 C ANISOU 1600 CA ARG A 678 5246 5372 5359 327 -196 615 C ATOM 1601 C ARG A 678 38.781 -11.891 39.975 1.00 40.71 C ANISOU 1601 C ARG A 678 5100 5246 5122 336 -271 572 C ATOM 1602 O ARG A 678 38.547 -11.604 41.152 1.00 40.79 O ANISOU 1602 O ARG A 678 5156 5304 5038 367 -303 590 O ATOM 1603 CB ARG A 678 37.996 -14.231 40.463 1.00 45.81 C ANISOU 1603 CB ARG A 678 5739 5865 5802 361 -185 700 C ATOM 1604 CG ARG A 678 37.208 -15.424 39.985 1.00 49.18 C ANISOU 1604 CG ARG A 678 6149 6248 6287 350 -111 743 C ATOM 1605 CD ARG A 678 35.880 -14.950 39.411 1.00 52.30 C ANISOU 1605 CD ARG A 678 6561 6645 6666 324 -58 705 C ATOM 1606 NE ARG A 678 35.563 -15.602 38.146 1.00 54.51 N ANISOU 1606 NE ARG A 678 6812 6860 7039 291 -13 690 N ATOM 1607 CZ ARG A 678 34.881 -16.739 38.040 1.00 56.54 C ANISOU 1607 CZ ARG A 678 7059 7078 7345 285 33 741 C ATOM 1608 NH1 ARG A 678 34.643 -17.253 36.841 1.00 56.98 N ANISOU 1608 NH1 ARG A 678 7097 7070 7483 256 62 715 N ATOM 1609 NH2 ARG A 678 34.429 -17.361 39.128 1.00 57.83 N ANISOU 1609 NH2 ARG A 678 7232 7264 7475 311 48 821 N ATOM 1610 N VAL A 679 39.475 -11.096 39.169 1.00 37.99 N ANISOU 1610 N VAL A 679 4727 4882 4825 311 -299 516 N ATOM 1611 CA VAL A 679 39.991 -9.816 39.633 1.00 36.19 C ANISOU 1611 CA VAL A 679 4516 4683 4551 313 -377 471 C ATOM 1612 C VAL A 679 39.374 -8.665 38.829 1.00 33.41 C ANISOU 1612 C VAL A 679 4174 4330 4189 283 -357 397 C ATOM 1613 O VAL A 679 39.226 -8.741 37.613 1.00 32.87 O ANISOU 1613 O VAL A 679 4075 4226 4186 255 -306 375 O ATOM 1614 CB VAL A 679 41.536 -9.771 39.551 1.00 35.66 C ANISOU 1614 CB VAL A 679 4397 4593 4558 310 -447 479 C ATOM 1615 CG1 VAL A 679 42.057 -8.437 40.058 1.00 35.21 C ANISOU 1615 CG1 VAL A 679 4358 4560 4462 308 -540 433 C ATOM 1616 CG2 VAL A 679 42.140 -10.910 40.365 1.00 36.10 C ANISOU 1616 CG2 VAL A 679 4442 4650 4625 342 -471 555 C ATOM 1617 N TYR A 680 39.006 -7.599 39.526 1.00 32.11 N ANISOU 1617 N TYR A 680 4058 4204 3937 294 -398 360 N ATOM 1618 CA TYR A 680 38.270 -6.502 38.922 1.00 30.13 C ANISOU 1618 CA TYR A 680 3824 3957 3667 272 -377 295 C ATOM 1619 C TYR A 680 39.002 -5.179 39.161 1.00 29.98 C ANISOU 1619 C TYR A 680 3814 3944 3635 267 -465 242 C ATOM 1620 O TYR A 680 39.523 -4.905 40.247 1.00 31.86 O ANISOU 1620 O TYR A 680 4081 4205 3819 293 -544 246 O ATOM 1621 CB TYR A 680 36.846 -6.459 39.476 1.00 30.11 C ANISOU 1621 CB TYR A 680 3877 3991 3574 293 -326 299 C ATOM 1622 CG TYR A 680 36.152 -7.810 39.460 1.00 31.36 C ANISOU 1622 CG TYR A 680 4025 4142 3748 300 -252 364 C ATOM 1623 CD1 TYR A 680 36.464 -8.783 40.397 1.00 32.09 C ANISOU 1623 CD1 TYR A 680 4124 4247 3820 332 -263 432 C ATOM 1624 CD2 TYR A 680 35.180 -8.113 38.510 1.00 31.62 C ANISOU 1624 CD2 TYR A 680 4042 4151 3821 274 -176 359 C ATOM 1625 CE1 TYR A 680 35.846 -10.016 40.384 1.00 32.73 C ANISOU 1625 CE1 TYR A 680 4194 4316 3926 337 -197 495 C ATOM 1626 CE2 TYR A 680 34.549 -9.360 38.498 1.00 31.92 C ANISOU 1626 CE2 TYR A 680 4069 4175 3887 277 -117 420 C ATOM 1627 CZ TYR A 680 34.888 -10.304 39.439 1.00 31.71 C ANISOU 1627 CZ TYR A 680 4047 4159 3844 308 -126 488 C ATOM 1628 OH TYR A 680 34.286 -11.550 39.460 1.00 31.11 O ANISOU 1628 OH TYR A 680 3956 4062 3802 310 -70 554 O ATOM 1629 N THR A 681 39.068 -4.374 38.112 1.00 28.59 N ANISOU 1629 N THR A 681 3610 3742 3511 232 -456 193 N ATOM 1630 CA THR A 681 39.735 -3.085 38.146 1.00 27.28 C ANISOU 1630 CA THR A 681 3442 3570 3354 219 -534 144 C ATOM 1631 C THR A 681 38.888 -2.070 37.395 1.00 26.68 C ANISOU 1631 C THR A 681 3380 3489 3266 197 -498 86 C ATOM 1632 O THR A 681 37.865 -2.427 36.808 1.00 25.61 O ANISOU 1632 O THR A 681 3251 3355 3124 191 -415 88 O ATOM 1633 CB THR A 681 41.101 -3.148 37.473 1.00 27.62 C ANISOU 1633 CB THR A 681 3411 3573 3511 195 -567 158 C ATOM 1634 OG1 THR A 681 40.898 -3.289 36.067 1.00 26.65 O ANISOU 1634 OG1 THR A 681 3248 3419 3457 168 -488 151 O ATOM 1635 CG2 THR A 681 41.916 -4.332 37.983 1.00 28.29 C ANISOU 1635 CG2 THR A 681 3467 3654 3627 215 -586 223 C ATOM 1636 N HIS A 682 39.334 -0.817 37.362 1.00 27.00 N ANISOU 1636 N HIS A 682 3421 3520 3317 182 -563 38 N ATOM 1637 CA HIS A 682 38.661 0.182 36.541 1.00 26.24 C ANISOU 1637 CA HIS A 682 3330 3413 3226 159 -532 -13 C ATOM 1638 C HIS A 682 38.671 -0.261 35.090 1.00 25.51 C ANISOU 1638 C HIS A 682 3184 3290 3219 128 -456 0 C ATOM 1639 O HIS A 682 37.773 0.083 34.334 1.00 24.70 O ANISOU 1639 O HIS A 682 3091 3184 3110 114 -400 -25 O ATOM 1640 CB HIS A 682 39.319 1.550 36.681 1.00 25.92 C ANISOU 1640 CB HIS A 682 3290 3356 3203 144 -620 -61 C ATOM 1641 CG HIS A 682 39.172 2.142 38.040 1.00 26.04 C ANISOU 1641 CG HIS A 682 3375 3397 3121 178 -698 -90 C ATOM 1642 ND1 HIS A 682 37.978 2.166 38.719 1.00 25.90 N ANISOU 1642 ND1 HIS A 682 3430 3418 2994 213 -661 -104 N ATOM 1643 CD2 HIS A 682 40.084 2.731 38.863 1.00 26.80 C ANISOU 1643 CD2 HIS A 682 3485 3486 3212 184 -813 -108 C ATOM 1644 CE1 HIS A 682 38.145 2.753 39.895 1.00 26.35 C ANISOU 1644 CE1 HIS A 682 3549 3492 2972 246 -745 -132 C ATOM 1645 NE2 HIS A 682 39.418 3.099 40.001 1.00 27.19 N ANISOU 1645 NE2 HIS A 682 3623 3569 3140 227 -844 -138 N ATOM 1646 N GLN A 683 39.677 -1.039 34.706 1.00 26.15 N ANISOU 1646 N GLN A 683 3211 3347 3377 122 -454 41 N ATOM 1647 CA GLN A 683 39.765 -1.518 33.336 1.00 26.59 C ANISOU 1647 CA GLN A 683 3224 3372 3508 102 -381 53 C ATOM 1648 C GLN A 683 38.674 -2.529 32.970 1.00 25.10 C ANISOU 1648 C GLN A 683 3058 3188 3292 108 -298 69 C ATOM 1649 O GLN A 683 38.148 -2.488 31.850 1.00 23.30 O ANISOU 1649 O GLN A 683 2826 2942 3087 91 -240 51 O ATOM 1650 CB GLN A 683 41.138 -2.120 33.070 1.00 30.22 C ANISOU 1650 CB GLN A 683 3621 3805 4058 103 -396 96 C ATOM 1651 CG GLN A 683 42.176 -1.084 32.689 1.00 33.33 C ANISOU 1651 CG GLN A 683 3967 4176 4523 82 -446 84 C ATOM 1652 CD GLN A 683 43.070 -0.678 33.831 1.00 36.28 C ANISOU 1652 CD GLN A 683 4330 4554 4901 88 -554 92 C ATOM 1653 OE1 GLN A 683 42.616 -0.514 34.964 1.00 39.85 O ANISOU 1653 OE1 GLN A 683 4837 5036 5267 105 -606 76 O ATOM 1654 NE2 GLN A 683 44.365 -0.515 33.539 1.00 39.04 N ANISOU 1654 NE2 GLN A 683 4608 4874 5351 77 -591 120 N ATOM 1655 N SER A 684 38.303 -3.421 33.887 1.00 23.91 N ANISOU 1655 N SER A 684 2932 3058 3094 133 -294 103 N ATOM 1656 CA SER A 684 37.237 -4.358 33.547 1.00 22.62 C ANISOU 1656 CA SER A 684 2784 2892 2917 135 -221 121 C ATOM 1657 C SER A 684 35.872 -3.668 33.509 1.00 20.90 C ANISOU 1657 C SER A 684 2607 2695 2641 129 -193 87 C ATOM 1658 O SER A 684 34.989 -4.108 32.785 1.00 19.91 O ANISOU 1658 O SER A 684 2482 2555 2526 116 -135 88 O ATOM 1659 CB SER A 684 37.206 -5.552 34.507 1.00 22.03 C ANISOU 1659 CB SER A 684 2719 2830 2820 162 -218 178 C ATOM 1660 OG SER A 684 37.166 -5.144 35.858 1.00 21.82 O ANISOU 1660 OG SER A 684 2730 2845 2717 188 -270 183 O ATOM 1661 N ASP A 685 35.691 -2.595 34.273 1.00 21.63 N ANISOU 1661 N ASP A 685 2730 2816 2672 139 -238 56 N ATOM 1662 CA ASP A 685 34.454 -1.812 34.192 1.00 21.41 C ANISOU 1662 CA ASP A 685 2736 2806 2594 137 -211 22 C ATOM 1663 C ASP A 685 34.301 -1.204 32.793 1.00 20.34 C ANISOU 1663 C ASP A 685 2577 2640 2510 102 -186 -15 C ATOM 1664 O ASP A 685 33.191 -1.166 32.225 1.00 19.14 O ANISOU 1664 O ASP A 685 2435 2487 2351 92 -137 -25 O ATOM 1665 CB ASP A 685 34.427 -0.702 35.253 1.00 22.95 C ANISOU 1665 CB ASP A 685 2973 3031 2714 160 -269 -11 C ATOM 1666 CG ASP A 685 33.641 -1.093 36.503 1.00 24.03 C ANISOU 1666 CG ASP A 685 3158 3210 2762 202 -254 17 C ATOM 1667 OD1 ASP A 685 33.064 -2.202 36.552 1.00 24.21 O ANISOU 1667 OD1 ASP A 685 3174 3237 2787 209 -198 67 O ATOM 1668 OD2 ASP A 685 33.569 -0.276 37.441 1.00 24.40 O ANISOU 1668 OD2 ASP A 685 3253 3283 2734 231 -298 -10 O ATOM 1669 N VAL A 686 35.431 -0.746 32.248 1.00 18.91 N ANISOU 1669 N VAL A 686 2364 2436 2386 86 -219 -29 N ATOM 1670 CA VAL A 686 35.478 -0.164 30.910 1.00 18.09 C ANISOU 1670 CA VAL A 686 2237 2303 2332 58 -195 -56 C ATOM 1671 C VAL A 686 35.074 -1.201 29.860 1.00 17.83 C ANISOU 1671 C VAL A 686 2193 2247 2334 48 -128 -38 C ATOM 1672 O VAL A 686 34.378 -0.875 28.891 1.00 17.27 O ANISOU 1672 O VAL A 686 2129 2164 2269 31 -93 -61 O ATOM 1673 CB VAL A 686 36.877 0.419 30.598 1.00 18.42 C ANISOU 1673 CB VAL A 686 2239 2324 2438 46 -239 -60 C ATOM 1674 CG1 VAL A 686 37.017 0.744 29.133 1.00 17.85 C ANISOU 1674 CG1 VAL A 686 2139 2221 2421 24 -198 -72 C ATOM 1675 CG2 VAL A 686 37.113 1.692 31.429 1.00 18.19 C ANISOU 1675 CG2 VAL A 686 2225 2307 2379 48 -314 -93 C ATOM 1676 N TRP A 687 35.483 -2.449 30.067 1.00 17.98 N ANISOU 1676 N TRP A 687 2199 2256 2375 61 -114 3 N ATOM 1677 CA TRP A 687 35.042 -3.546 29.208 1.00 17.89 C ANISOU 1677 CA TRP A 687 2187 2218 2393 55 -58 19 C ATOM 1678 C TRP A 687 33.529 -3.684 29.254 1.00 18.63 C ANISOU 1678 C TRP A 687 2311 2322 2447 49 -28 14 C ATOM 1679 O TRP A 687 32.883 -3.833 28.219 1.00 18.56 O ANISOU 1679 O TRP A 687 2308 2290 2456 32 5 -1 O ATOM 1680 CB TRP A 687 35.678 -4.881 29.625 1.00 17.62 C ANISOU 1680 CB TRP A 687 2137 2170 2387 74 -53 67 C ATOM 1681 CG TRP A 687 35.157 -6.066 28.830 1.00 17.57 C ANISOU 1681 CG TRP A 687 2137 2128 2410 70 -2 80 C ATOM 1682 CD1 TRP A 687 33.925 -6.646 28.932 1.00 17.26 C ANISOU 1682 CD1 TRP A 687 2120 2087 2351 64 23 90 C ATOM 1683 CD2 TRP A 687 35.863 -6.805 27.821 1.00 16.98 C ANISOU 1683 CD2 TRP A 687 2047 2010 2394 73 28 85 C ATOM 1684 NE1 TRP A 687 33.817 -7.683 28.045 1.00 16.37 N ANISOU 1684 NE1 TRP A 687 2008 1928 2282 60 56 96 N ATOM 1685 CE2 TRP A 687 34.993 -7.804 27.351 1.00 16.43 C ANISOU 1685 CE2 TRP A 687 1999 1911 2334 69 62 90 C ATOM 1686 CE3 TRP A 687 37.146 -6.714 27.267 1.00 17.41 C ANISOU 1686 CE3 TRP A 687 2072 2046 2498 83 30 88 C ATOM 1687 CZ2 TRP A 687 35.366 -8.717 26.362 1.00 16.53 C ANISOU 1687 CZ2 TRP A 687 2014 1874 2393 76 94 90 C ATOM 1688 CZ3 TRP A 687 37.505 -7.608 26.266 1.00 17.23 C ANISOU 1688 CZ3 TRP A 687 2048 1978 2519 94 74 92 C ATOM 1689 CH2 TRP A 687 36.618 -8.595 25.826 1.00 16.67 C ANISOU 1689 CH2 TRP A 687 2009 1877 2447 92 103 89 C ATOM 1690 N SER A 688 32.977 -3.668 30.464 1.00 19.09 N ANISOU 1690 N SER A 688 2387 2414 2451 66 -41 31 N ATOM 1691 CA SER A 688 31.540 -3.735 30.643 1.00 18.68 C ANISOU 1691 CA SER A 688 2355 2376 2367 65 -10 36 C ATOM 1692 C SER A 688 30.868 -2.541 29.981 1.00 18.63 C ANISOU 1692 C SER A 688 2358 2373 2348 48 -7 -10 C ATOM 1693 O SER A 688 29.765 -2.677 29.444 1.00 17.67 O ANISOU 1693 O SER A 688 2240 2242 2232 34 24 -12 O ATOM 1694 CB SER A 688 31.178 -3.793 32.128 1.00 19.14 C ANISOU 1694 CB SER A 688 2435 2477 2363 96 -20 66 C ATOM 1695 OG SER A 688 31.834 -4.888 32.744 1.00 19.49 O ANISOU 1695 OG SER A 688 2470 2518 2419 113 -26 114 O ATOM 1696 N PHE A 689 31.540 -1.383 30.014 1.00 17.84 N ANISOU 1696 N PHE A 689 2259 2282 2238 47 -44 -45 N ATOM 1697 CA PHE A 689 31.000 -0.168 29.418 1.00 17.53 C ANISOU 1697 CA PHE A 689 2227 2242 2190 32 -45 -88 C ATOM 1698 C PHE A 689 30.805 -0.342 27.910 1.00 17.14 C ANISOU 1698 C PHE A 689 2166 2158 2188 6 -15 -101 C ATOM 1699 O PHE A 689 29.866 0.190 27.302 1.00 14.81 O ANISOU 1699 O PHE A 689 1880 1861 1887 -8 0 -121 O ATOM 1700 CB PHE A 689 31.899 1.046 29.697 1.00 17.58 C ANISOU 1700 CB PHE A 689 2233 2254 2191 34 -97 -120 C ATOM 1701 CG PHE A 689 31.318 2.340 29.190 1.00 17.32 C ANISOU 1701 CG PHE A 689 2210 2220 2150 22 -100 -162 C ATOM 1702 CD1 PHE A 689 30.408 3.060 29.960 1.00 17.66 C ANISOU 1702 CD1 PHE A 689 2284 2290 2137 40 -105 -180 C ATOM 1703 CD2 PHE A 689 31.625 2.809 27.926 1.00 17.04 C ANISOU 1703 CD2 PHE A 689 2156 2157 2161 -3 -91 -180 C ATOM 1704 CE1 PHE A 689 29.826 4.244 29.479 1.00 17.63 C ANISOU 1704 CE1 PHE A 689 2287 2280 2129 30 -106 -217 C ATOM 1705 CE2 PHE A 689 31.049 4.001 27.445 1.00 17.49 C ANISOU 1705 CE2 PHE A 689 2221 2211 2212 -14 -94 -214 C ATOM 1706 CZ PHE A 689 30.148 4.712 28.230 1.00 17.15 C ANISOU 1706 CZ PHE A 689 2206 2191 2119 2 -103 -233 C ATOM 1707 N GLY A 690 31.693 -1.108 27.307 1.00 16.87 N ANISOU 1707 N GLY A 690 2115 2096 2197 2 -7 -87 N ATOM 1708 CA GLY A 690 31.625 -1.313 25.879 1.00 14.83 C ANISOU 1708 CA GLY A 690 1856 1805 1975 -15 21 -100 C ATOM 1709 C GLY A 690 30.460 -2.187 25.522 1.00 14.76 C ANISOU 1709 C GLY A 690 1862 1781 1966 -23 48 -90 C ATOM 1710 O GLY A 690 29.854 -2.019 24.481 1.00 14.56 O ANISOU 1710 O GLY A 690 1847 1736 1948 -39 61 -111 O ATOM 1711 N VAL A 691 30.156 -3.141 26.390 1.00 16.76 N ANISOU 1711 N VAL A 691 2114 2040 2215 -13 53 -55 N ATOM 1712 CA VAL A 691 29.026 -4.040 26.173 1.00 16.22 C ANISOU 1712 CA VAL A 691 2052 1953 2159 -23 74 -36 C ATOM 1713 C VAL A 691 27.741 -3.234 26.362 1.00 16.04 C ANISOU 1713 C VAL A 691 2033 1952 2109 -32 77 -45 C ATOM 1714 O VAL A 691 26.791 -3.379 25.604 1.00 15.40 O ANISOU 1714 O VAL A 691 1955 1849 2046 -51 85 -51 O ATOM 1715 CB VAL A 691 29.070 -5.253 27.128 1.00 15.41 C ANISOU 1715 CB VAL A 691 1941 1850 2065 -8 81 14 C ATOM 1716 CG1 VAL A 691 27.820 -6.102 26.975 1.00 15.53 C ANISOU 1716 CG1 VAL A 691 1955 1842 2105 -23 100 40 C ATOM 1717 CG2 VAL A 691 30.329 -6.073 26.878 1.00 15.56 C ANISOU 1717 CG2 VAL A 691 1953 1842 2119 2 81 24 C ATOM 1718 N LEU A 692 27.748 -2.354 27.356 1.00 15.00 N ANISOU 1718 N LEU A 692 1903 1862 1933 -14 66 -48 N ATOM 1719 CA LEU A 692 26.647 -1.442 27.576 1.00 14.93 C ANISOU 1719 CA LEU A 692 1900 1877 1897 -14 71 -59 C ATOM 1720 C LEU A 692 26.403 -0.559 26.324 1.00 23.48 C ANISOU 1720 C LEU A 692 2986 2942 2995 -37 65 -101 C ATOM 1721 O LEU A 692 25.247 -0.306 25.939 1.00 23.44 O ANISOU 1721 O LEU A 692 2979 2933 2995 -49 75 -103 O ATOM 1722 CB LEU A 692 26.926 -0.585 28.818 1.00 15.14 C ANISOU 1722 CB LEU A 692 1939 1946 1868 15 55 -65 C ATOM 1723 CG LEU A 692 25.899 0.470 29.229 1.00 15.18 C ANISOU 1723 CG LEU A 692 1956 1978 1835 28 64 -79 C ATOM 1724 CD1 LEU A 692 24.523 -0.153 29.456 1.00 15.36 C ANISOU 1724 CD1 LEU A 692 1966 2005 1865 30 104 -37 C ATOM 1725 CD2 LEU A 692 26.353 1.221 30.467 1.00 15.75 C ANISOU 1725 CD2 LEU A 692 2053 2086 1847 63 41 -92 C ATOM 1726 N MET A 693 27.489 -0.101 25.697 1.00 22.64 N ANISOU 1726 N MET A 693 2881 2822 2898 -42 49 -129 N ATOM 1727 CA MET A 693 27.391 0.721 24.492 1.00 21.28 C ANISOU 1727 CA MET A 693 2714 2633 2738 -60 46 -163 C ATOM 1728 C MET A 693 26.676 -0.052 23.410 1.00 19.77 C ANISOU 1728 C MET A 693 2530 2409 2573 -79 60 -160 C ATOM 1729 O MET A 693 25.854 0.496 22.685 1.00 19.88 O ANISOU 1729 O MET A 693 2550 2415 2587 -93 58 -177 O ATOM 1730 CB MET A 693 28.765 1.127 23.968 1.00 22.41 C ANISOU 1730 CB MET A 693 2853 2766 2898 -59 36 -178 C ATOM 1731 CG MET A 693 29.412 2.279 24.662 1.00 23.07 C ANISOU 1731 CG MET A 693 2928 2870 2966 -51 8 -193 C ATOM 1732 SD MET A 693 30.913 2.759 23.783 1.00 50.73 S ANISOU 1732 SD MET A 693 6413 6351 6511 -57 2 -201 S ATOM 1733 CE MET A 693 30.183 3.249 22.228 1.00 13.87 C ANISOU 1733 CE MET A 693 1760 1663 1848 -74 25 -221 C ATOM 1734 N TRP A 694 27.025 -1.331 23.300 1.00 18.33 N ANISOU 1734 N TRP A 694 2348 2202 2412 -77 69 -140 N ATOM 1735 CA TRP A 694 26.425 -2.208 22.323 1.00 17.26 C ANISOU 1735 CA TRP A 694 2226 2027 2304 -93 73 -141 C ATOM 1736 C TRP A 694 24.937 -2.361 22.613 1.00 16.81 C ANISOU 1736 C TRP A 694 2160 1972 2255 -107 70 -123 C ATOM 1737 O TRP A 694 24.110 -2.308 21.712 1.00 16.84 O ANISOU 1737 O TRP A 694 2173 1953 2273 -127 59 -136 O ATOM 1738 CB TRP A 694 27.129 -3.549 22.340 1.00 16.32 C ANISOU 1738 CB TRP A 694 2112 1880 2211 -84 81 -122 C ATOM 1739 CG TRP A 694 26.736 -4.479 21.233 1.00 15.98 C ANISOU 1739 CG TRP A 694 2093 1786 2194 -96 79 -133 C ATOM 1740 CD1 TRP A 694 27.344 -4.618 20.014 1.00 14.68 C ANISOU 1740 CD1 TRP A 694 1959 1589 2030 -91 83 -162 C ATOM 1741 CD2 TRP A 694 25.661 -5.431 21.254 1.00 14.90 C ANISOU 1741 CD2 TRP A 694 1955 1618 2088 -113 68 -113 C ATOM 1742 NE1 TRP A 694 26.709 -5.594 19.278 1.00 15.80 N ANISOU 1742 NE1 TRP A 694 2128 1682 2194 -102 71 -170 N ATOM 1743 CE2 TRP A 694 25.670 -6.100 20.017 1.00 15.06 C ANISOU 1743 CE2 TRP A 694 2012 1586 2125 -119 57 -140 C ATOM 1744 CE3 TRP A 694 24.702 -5.781 22.203 1.00 15.07 C ANISOU 1744 CE3 TRP A 694 1948 1651 2126 -122 68 -73 C ATOM 1745 CZ2 TRP A 694 24.762 -7.099 19.709 1.00 15.39 C ANISOU 1745 CZ2 TRP A 694 2061 1580 2205 -139 35 -131 C ATOM 1746 CZ3 TRP A 694 23.798 -6.771 21.890 1.00 16.21 C ANISOU 1746 CZ3 TRP A 694 2092 1750 2316 -143 53 -56 C ATOM 1747 CH2 TRP A 694 23.835 -7.421 20.653 1.00 15.80 C ANISOU 1747 CH2 TRP A 694 2076 1640 2286 -153 31 -87 C ATOM 1748 N GLU A 695 24.596 -2.537 23.879 1.00 15.82 N ANISOU 1748 N GLU A 695 2015 1875 2121 -95 80 -88 N ATOM 1749 CA GLU A 695 23.206 -2.658 24.253 1.00 15.82 C ANISOU 1749 CA GLU A 695 1997 1879 2135 -103 87 -59 C ATOM 1750 C GLU A 695 22.413 -1.424 23.838 1.00 15.28 C ANISOU 1750 C GLU A 695 1928 1825 2055 -111 81 -83 C ATOM 1751 O GLU A 695 21.263 -1.516 23.410 1.00 14.96 O ANISOU 1751 O GLU A 695 1873 1767 2042 -130 76 -72 O ATOM 1752 CB GLU A 695 23.083 -2.872 25.750 1.00 16.10 C ANISOU 1752 CB GLU A 695 2017 1951 2150 -78 109 -15 C ATOM 1753 CG GLU A 695 23.535 -4.221 26.227 1.00 16.87 C ANISOU 1753 CG GLU A 695 2109 2032 2269 -73 116 24 C ATOM 1754 CD GLU A 695 23.100 -4.459 27.652 1.00 18.05 C ANISOU 1754 CD GLU A 695 2243 2218 2398 -47 142 77 C ATOM 1755 OE1 GLU A 695 21.995 -5.037 27.826 1.00 18.10 O ANISOU 1755 OE1 GLU A 695 2225 2213 2439 -56 160 122 O ATOM 1756 OE2 GLU A 695 23.844 -4.047 28.585 1.00 18.18 O ANISOU 1756 OE2 GLU A 695 2272 2272 2363 -18 143 77 O ATOM 1757 N ILE A 696 23.038 -0.270 23.974 1.00 14.49 N ANISOU 1757 N ILE A 696 1837 1752 1917 -98 77 -114 N ATOM 1758 CA ILE A 696 22.390 0.978 23.652 1.00 14.75 C ANISOU 1758 CA ILE A 696 1870 1797 1938 -101 72 -137 C ATOM 1759 C ILE A 696 22.129 1.118 22.145 1.00 15.35 C ANISOU 1759 C ILE A 696 1957 1838 2036 -127 53 -163 C ATOM 1760 O ILE A 696 21.035 1.491 21.722 1.00 15.77 O ANISOU 1760 O ILE A 696 2002 1886 2105 -140 46 -161 O ATOM 1761 CB ILE A 696 23.249 2.156 24.159 1.00 15.36 C ANISOU 1761 CB ILE A 696 1957 1902 1976 -81 65 -165 C ATOM 1762 CG1 ILE A 696 23.245 2.173 25.692 1.00 14.31 C ANISOU 1762 CG1 ILE A 696 1823 1806 1809 -50 78 -144 C ATOM 1763 CG2 ILE A 696 22.776 3.457 23.576 1.00 13.88 C ANISOU 1763 CG2 ILE A 696 1773 1716 1784 -87 56 -194 C ATOM 1764 CD1 ILE A 696 24.178 3.171 26.304 1.00 14.32 C ANISOU 1764 CD1 ILE A 696 1839 1827 1773 -30 58 -173 C ATOM 1765 N PHE A 697 23.126 0.791 21.331 1.00 15.69 N ANISOU 1765 N PHE A 697 2022 1858 2081 -131 46 -183 N ATOM 1766 CA PHE A 697 23.035 1.046 19.908 1.00 14.86 C ANISOU 1766 CA PHE A 697 1939 1726 1981 -147 31 -210 C ATOM 1767 C PHE A 697 22.275 -0.043 19.157 1.00 15.26 C ANISOU 1767 C PHE A 697 2001 1736 2062 -166 14 -203 C ATOM 1768 O PHE A 697 21.892 0.123 17.990 1.00 14.78 O ANISOU 1768 O PHE A 697 1964 1650 2001 -179 -7 -224 O ATOM 1769 CB PHE A 697 24.432 1.249 19.339 1.00 14.57 C ANISOU 1769 CB PHE A 697 1921 1683 1931 -136 38 -230 C ATOM 1770 CG PHE A 697 24.965 2.634 19.583 1.00 13.52 C ANISOU 1770 CG PHE A 697 1780 1577 1781 -128 39 -244 C ATOM 1771 CD1 PHE A 697 24.658 3.670 18.711 1.00 13.48 C ANISOU 1771 CD1 PHE A 697 1785 1569 1769 -135 31 -263 C ATOM 1772 CD2 PHE A 697 25.733 2.912 20.701 1.00 13.53 C ANISOU 1772 CD2 PHE A 697 1765 1603 1774 -112 42 -238 C ATOM 1773 CE1 PHE A 697 25.140 4.956 18.939 1.00 13.57 C ANISOU 1773 CE1 PHE A 697 1785 1597 1773 -130 29 -274 C ATOM 1774 CE2 PHE A 697 26.225 4.195 20.941 1.00 13.45 C ANISOU 1774 CE2 PHE A 697 1748 1609 1755 -107 33 -254 C ATOM 1775 CZ PHE A 697 25.929 5.218 20.061 1.00 13.50 C ANISOU 1775 CZ PHE A 697 1759 1608 1761 -116 27 -271 C ATOM 1776 N THR A 698 22.036 -1.149 19.842 1.00 15.98 N ANISOU 1776 N THR A 698 2077 1817 2177 -167 19 -173 N ATOM 1777 CA THR A 698 21.164 -2.186 19.336 1.00 16.40 C ANISOU 1777 CA THR A 698 2132 1826 2272 -189 -4 -160 C ATOM 1778 C THR A 698 19.798 -1.926 19.938 1.00 17.79 C ANISOU 1778 C THR A 698 2268 2017 2476 -201 -6 -126 C ATOM 1779 O THR A 698 18.896 -2.767 19.831 1.00 17.57 O ANISOU 1779 O THR A 698 2223 1956 2498 -222 -25 -100 O ATOM 1780 CB THR A 698 21.636 -3.568 19.728 1.00 16.81 C ANISOU 1780 CB THR A 698 2186 1853 2348 -185 3 -139 C ATOM 1781 OG1 THR A 698 21.798 -3.590 21.148 1.00 16.90 O ANISOU 1781 OG1 THR A 698 2165 1903 2354 -169 32 -102 O ATOM 1782 CG2 THR A 698 22.955 -3.888 19.076 1.00 14.74 C ANISOU 1782 CG2 THR A 698 1962 1573 2066 -169 10 -169 C ATOM 1783 N LEU A 699 19.670 -0.760 20.584 1.00 18.16 N ANISOU 1783 N LEU A 699 2297 2109 2495 -186 13 -125 N ATOM 1784 CA LEU A 699 18.433 -0.351 21.247 1.00 19.21 C ANISOU 1784 CA LEU A 699 2390 2262 2647 -186 24 -91 C ATOM 1785 C LEU A 699 17.841 -1.462 22.124 1.00 19.18 C ANISOU 1785 C LEU A 699 2352 2252 2684 -187 41 -34 C ATOM 1786 O LEU A 699 16.715 -1.897 21.893 1.00 18.27 O ANISOU 1786 O LEU A 699 2207 2111 2625 -209 27 -3 O ATOM 1787 CB LEU A 699 17.401 0.083 20.216 1.00 20.94 C ANISOU 1787 CB LEU A 699 2603 2458 2894 -210 -9 -101 C ATOM 1788 CG LEU A 699 17.881 0.988 19.084 1.00 21.34 C ANISOU 1788 CG LEU A 699 2692 2504 2913 -213 -32 -151 C ATOM 1789 CD1 LEU A 699 16.751 1.173 18.077 1.00 22.36 C ANISOU 1789 CD1 LEU A 699 2817 2605 3075 -238 -74 -152 C ATOM 1790 CD2 LEU A 699 18.276 2.304 19.607 1.00 22.08 C ANISOU 1790 CD2 LEU A 699 2783 2639 2966 -189 -8 -166 C ATOM 1791 N GLY A 700 18.619 -1.924 23.106 1.00 18.85 N ANISOU 1791 N GLY A 700 2312 2231 2618 -164 69 -17 N ATOM 1792 CA GLY A 700 18.170 -2.904 24.072 1.00 19.02 C ANISOU 1792 CA GLY A 700 2303 2253 2671 -159 94 44 C ATOM 1793 C GLY A 700 18.340 -4.360 23.687 1.00 20.28 C ANISOU 1793 C GLY A 700 2464 2360 2881 -181 75 61 C ATOM 1794 O GLY A 700 17.632 -5.215 24.216 1.00 18.61 O ANISOU 1794 O GLY A 700 2218 2134 2719 -188 86 119 O ATOM 1795 N GLY A 701 19.266 -4.654 22.773 1.00 22.37 N ANISOU 1795 N GLY A 701 2770 2595 3136 -189 48 15 N ATOM 1796 CA GLY A 701 19.525 -6.020 22.351 1.00 24.11 C ANISOU 1796 CA GLY A 701 3002 2760 3400 -204 29 22 C ATOM 1797 C GLY A 701 20.281 -6.801 23.405 1.00 24.14 C ANISOU 1797 C GLY A 701 2998 2775 3398 -182 58 58 C ATOM 1798 O GLY A 701 20.859 -6.207 24.299 1.00 25.21 O ANISOU 1798 O GLY A 701 3133 2963 3484 -153 87 64 O ATOM 1799 N SER A 702 20.273 -8.130 23.303 1.00 25.71 N ANISOU 1799 N SER A 702 3196 2924 3651 -194 47 82 N ATOM 1800 CA SER A 702 20.963 -9.005 24.258 1.00 23.42 C ANISOU 1800 CA SER A 702 2897 2637 3363 -174 72 124 C ATOM 1801 C SER A 702 22.279 -9.452 23.697 1.00 22.05 C ANISOU 1801 C SER A 702 2764 2439 3176 -162 63 83 C ATOM 1802 O SER A 702 22.322 -10.027 22.620 1.00 21.94 O ANISOU 1802 O SER A 702 2778 2367 3191 -177 34 51 O ATOM 1803 CB SER A 702 20.126 -10.237 24.604 1.00 25.82 C ANISOU 1803 CB SER A 702 3167 2897 3745 -193 69 187 C ATOM 1804 OG SER A 702 18.815 -9.858 24.976 1.00 27.63 O ANISOU 1804 OG SER A 702 3353 3143 4002 -206 79 229 O ATOM 1805 N PRO A 703 23.362 -9.194 24.436 1.00 20.92 N ANISOU 1805 N PRO A 703 2625 2338 2988 -131 87 87 N ATOM 1806 CA PRO A 703 24.733 -9.498 24.011 1.00 20.35 C ANISOU 1806 CA PRO A 703 2580 2249 2904 -113 86 56 C ATOM 1807 C PRO A 703 25.000 -10.959 23.655 1.00 18.75 C ANISOU 1807 C PRO A 703 2390 1981 2755 -116 78 68 C ATOM 1808 O PRO A 703 24.375 -11.875 24.169 1.00 19.11 O ANISOU 1808 O PRO A 703 2414 2001 2848 -126 77 117 O ATOM 1809 CB PRO A 703 25.577 -9.074 25.221 1.00 20.40 C ANISOU 1809 CB PRO A 703 2573 2313 2867 -83 106 80 C ATOM 1810 CG PRO A 703 24.615 -8.847 26.331 1.00 21.24 C ANISOU 1810 CG PRO A 703 2651 2458 2961 -80 121 128 C ATOM 1811 CD PRO A 703 23.329 -8.467 25.714 1.00 21.63 C ANISOU 1811 CD PRO A 703 2692 2494 3031 -108 113 118 C ATOM 1812 N TYR A 704 25.956 -11.133 22.746 1.00 18.67 N ANISOU 1812 N TYR A 704 2414 1941 2739 -103 75 24 N ATOM 1813 CA TYR A 704 26.438 -12.427 22.223 1.00 18.77 C ANISOU 1813 CA TYR A 704 2451 1887 2795 -96 69 20 C ATOM 1814 C TYR A 704 25.318 -13.348 21.763 1.00 20.18 C ANISOU 1814 C TYR A 704 2637 1998 3032 -126 38 26 C ATOM 1815 O TYR A 704 25.199 -14.474 22.238 1.00 20.88 O ANISOU 1815 O TYR A 704 2712 2048 3173 -128 35 67 O ATOM 1816 CB TYR A 704 27.340 -13.103 23.271 1.00 18.54 C ANISOU 1816 CB TYR A 704 2398 1868 2777 -69 92 67 C ATOM 1817 CG TYR A 704 28.519 -12.202 23.608 1.00 18.06 C ANISOU 1817 CG TYR A 704 2330 1864 2667 -42 110 57 C ATOM 1818 CD1 TYR A 704 29.568 -12.025 22.698 1.00 17.10 C ANISOU 1818 CD1 TYR A 704 2234 1727 2535 -22 120 15 C ATOM 1819 CD2 TYR A 704 28.549 -11.467 24.798 1.00 17.04 C ANISOU 1819 CD2 TYR A 704 2171 1801 2502 -35 116 88 C ATOM 1820 CE1 TYR A 704 30.623 -11.182 22.975 1.00 16.43 C ANISOU 1820 CE1 TYR A 704 2134 1689 2421 -2 133 11 C ATOM 1821 CE2 TYR A 704 29.598 -10.617 25.077 1.00 16.42 C ANISOU 1821 CE2 TYR A 704 2086 1765 2386 -15 120 75 C ATOM 1822 CZ TYR A 704 30.639 -10.481 24.163 1.00 16.37 C ANISOU 1822 CZ TYR A 704 2095 1741 2386 -1 127 39 C ATOM 1823 OH TYR A 704 31.693 -9.630 24.444 1.00 16.13 O ANISOU 1823 OH TYR A 704 2049 1749 2333 16 127 34 O ATOM 1824 N PRO A 705 24.504 -12.872 20.807 1.00 21.48 N ANISOU 1824 N PRO A 705 2823 2145 3192 -150 8 -14 N ATOM 1825 CA PRO A 705 23.335 -13.659 20.398 1.00 23.15 C ANISOU 1825 CA PRO A 705 3035 2292 3467 -184 -35 -6 C ATOM 1826 C PRO A 705 23.685 -15.062 19.902 1.00 23.98 C ANISOU 1826 C PRO A 705 3176 2313 3622 -179 -56 -17 C ATOM 1827 O PRO A 705 24.619 -15.248 19.123 1.00 25.22 O ANISOU 1827 O PRO A 705 3385 2446 3751 -151 -50 -65 O ATOM 1828 CB PRO A 705 22.700 -12.808 19.288 1.00 22.21 C ANISOU 1828 CB PRO A 705 2946 2171 3321 -202 -68 -58 C ATOM 1829 CG PRO A 705 23.721 -11.799 18.908 1.00 21.45 C ANISOU 1829 CG PRO A 705 2877 2123 3150 -172 -38 -100 C ATOM 1830 CD PRO A 705 24.589 -11.584 20.092 1.00 21.17 C ANISOU 1830 CD PRO A 705 2805 2143 3095 -147 8 -62 C ATOM 1831 N GLY A 706 22.940 -16.043 20.405 1.00 24.59 N ANISOU 1831 N GLY A 706 3223 2345 3776 -203 -76 34 N ATOM 1832 CA GLY A 706 23.122 -17.432 20.018 1.00 25.51 C ANISOU 1832 CA GLY A 706 3369 2371 3954 -203 -102 28 C ATOM 1833 C GLY A 706 24.321 -18.117 20.656 1.00 27.19 C ANISOU 1833 C GLY A 706 3579 2584 4167 -165 -61 53 C ATOM 1834 O GLY A 706 24.634 -19.270 20.335 1.00 27.66 O ANISOU 1834 O GLY A 706 3667 2567 4274 -157 -77 46 O ATOM 1835 N ILE A 707 24.996 -17.412 21.562 1.00 27.43 N ANISOU 1835 N ILE A 707 3578 2698 4148 -141 -12 83 N ATOM 1836 CA ILE A 707 26.164 -17.968 22.237 1.00 27.72 C ANISOU 1836 CA ILE A 707 3606 2742 4184 -105 23 112 C ATOM 1837 C ILE A 707 25.889 -18.178 23.726 1.00 28.73 C ANISOU 1837 C ILE A 707 3673 2910 4332 -108 45 200 C ATOM 1838 O ILE A 707 25.467 -17.249 24.431 1.00 27.95 O ANISOU 1838 O ILE A 707 3543 2884 4194 -113 60 225 O ATOM 1839 CB ILE A 707 27.387 -17.060 22.041 1.00 26.95 C ANISOU 1839 CB ILE A 707 3525 2701 4014 -69 55 75 C ATOM 1840 CG1 ILE A 707 27.679 -16.889 20.539 1.00 25.50 C ANISOU 1840 CG1 ILE A 707 3405 2479 3806 -58 43 -4 C ATOM 1841 CG2 ILE A 707 28.586 -17.607 22.796 1.00 27.19 C ANISOU 1841 CG2 ILE A 707 3538 2742 4052 -32 86 112 C ATOM 1842 CD1 ILE A 707 28.713 -15.831 20.227 1.00 24.47 C ANISOU 1842 CD1 ILE A 707 3284 2404 3610 -29 76 -36 C ATOM 1843 N PRO A 708 26.103 -19.416 24.205 1.00 29.78 N ANISOU 1843 N PRO A 708 3795 2995 4526 -101 47 248 N ATOM 1844 CA PRO A 708 25.885 -19.759 25.617 1.00 30.92 C ANISOU 1844 CA PRO A 708 3886 3171 4689 -98 70 339 C ATOM 1845 C PRO A 708 27.046 -19.270 26.444 1.00 32.01 C ANISOU 1845 C PRO A 708 4016 3382 4764 -57 104 355 C ATOM 1846 O PRO A 708 28.111 -19.121 25.871 1.00 32.13 O ANISOU 1846 O PRO A 708 4060 3394 4755 -33 107 306 O ATOM 1847 CB PRO A 708 25.820 -21.286 25.602 1.00 31.09 C ANISOU 1847 CB PRO A 708 3907 3101 4803 -103 55 375 C ATOM 1848 CG PRO A 708 26.689 -21.662 24.444 1.00 30.82 C ANISOU 1848 CG PRO A 708 3932 3009 4771 -84 40 299 C ATOM 1849 CD PRO A 708 26.488 -20.592 23.405 1.00 30.06 C ANISOU 1849 CD PRO A 708 3871 2934 4617 -93 26 219 C ATOM 1850 N VAL A 709 26.857 -19.039 27.741 1.00 33.73 N ANISOU 1850 N VAL A 709 4197 3662 4957 -48 126 424 N ATOM 1851 CA VAL A 709 27.907 -18.442 28.552 1.00 34.91 C ANISOU 1851 CA VAL A 709 4341 3883 5039 -11 145 434 C ATOM 1852 C VAL A 709 29.089 -19.379 28.725 1.00 37.04 C ANISOU 1852 C VAL A 709 4615 4121 5338 19 147 454 C ATOM 1853 O VAL A 709 30.234 -18.920 28.811 1.00 36.58 O ANISOU 1853 O VAL A 709 4562 4097 5240 47 150 432 O ATOM 1854 CB VAL A 709 27.397 -17.993 29.953 1.00 23.81 C ANISOU 1854 CB VAL A 709 2906 2552 3588 -1 166 502 C ATOM 1855 CG1 VAL A 709 26.303 -16.930 29.806 1.00 22.73 C ANISOU 1855 CG1 VAL A 709 2765 2453 3419 -23 169 481 C ATOM 1856 CG2 VAL A 709 26.913 -19.166 30.801 1.00 25.25 C ANISOU 1856 CG2 VAL A 709 3061 2707 3827 0 181 595 C ATOM 1857 N GLU A 710 28.842 -20.682 28.745 1.00 39.98 N ANISOU 1857 N GLU A 710 4980 4422 5787 13 144 495 N ATOM 1858 CA GLU A 710 29.935 -21.632 28.944 1.00 42.81 C ANISOU 1858 CA GLU A 710 5340 4745 6181 44 149 520 C ATOM 1859 C GLU A 710 30.967 -21.534 27.819 1.00 43.20 C ANISOU 1859 C GLU A 710 5422 4763 6227 63 146 443 C ATOM 1860 O GLU A 710 32.111 -21.933 27.991 1.00 43.81 O ANISOU 1860 O GLU A 710 5496 4833 6314 98 155 455 O ATOM 1861 CB GLU A 710 29.397 -23.065 29.069 1.00 44.89 C ANISOU 1861 CB GLU A 710 5593 4927 6538 31 144 575 C ATOM 1862 CG GLU A 710 28.193 -23.368 28.177 1.00 46.85 C ANISOU 1862 CG GLU A 710 5853 5106 6842 -13 120 547 C ATOM 1863 CD GLU A 710 26.851 -23.143 28.877 1.00 48.04 C ANISOU 1863 CD GLU A 710 5964 5286 7002 -44 125 608 C ATOM 1864 OE1 GLU A 710 26.804 -22.361 29.853 1.00 47.60 O ANISOU 1864 OE1 GLU A 710 5886 5320 6880 -29 151 647 O ATOM 1865 OE2 GLU A 710 25.838 -23.727 28.427 1.00 49.42 O ANISOU 1865 OE2 GLU A 710 6132 5392 7254 -81 102 618 O ATOM 1866 N GLU A 711 30.578 -20.963 26.684 1.00 43.39 N ANISOU 1866 N GLU A 711 5478 4771 6236 44 135 369 N ATOM 1867 CA GLU A 711 31.473 -20.884 25.536 1.00 44.06 C ANISOU 1867 CA GLU A 711 5600 4825 6314 67 141 299 C ATOM 1868 C GLU A 711 32.115 -19.515 25.316 1.00 40.74 C ANISOU 1868 C GLU A 711 5181 4477 5823 79 152 258 C ATOM 1869 O GLU A 711 33.057 -19.392 24.537 1.00 40.38 O ANISOU 1869 O GLU A 711 5155 4416 5771 106 167 216 O ATOM 1870 CB GLU A 711 30.723 -21.297 24.280 1.00 48.27 C ANISOU 1870 CB GLU A 711 6180 5281 6880 45 119 242 C ATOM 1871 CG GLU A 711 30.691 -22.789 24.099 1.00 52.98 C ANISOU 1871 CG GLU A 711 6792 5780 7557 50 107 259 C ATOM 1872 CD GLU A 711 29.662 -23.228 23.085 1.00 58.01 C ANISOU 1872 CD GLU A 711 7471 6338 8232 18 68 212 C ATOM 1873 OE1 GLU A 711 29.169 -22.361 22.322 1.00 60.69 O ANISOU 1873 OE1 GLU A 711 7836 6697 8527 0 54 156 O ATOM 1874 OE2 GLU A 711 29.340 -24.441 23.057 1.00 62.13 O ANISOU 1874 OE2 GLU A 711 8000 6774 8831 10 46 233 O ATOM 1875 N LEU A 712 31.630 -18.495 26.011 1.00 37.19 N ANISOU 1875 N LEU A 712 4707 4100 5322 62 148 272 N ATOM 1876 CA LEU A 712 32.066 -17.125 25.744 1.00 33.04 C ANISOU 1876 CA LEU A 712 4183 3635 4734 66 151 230 C ATOM 1877 C LEU A 712 33.568 -16.881 25.991 1.00 29.11 C ANISOU 1877 C LEU A 712 3668 3164 4228 102 163 236 C ATOM 1878 O LEU A 712 34.234 -16.231 25.175 1.00 28.65 O ANISOU 1878 O LEU A 712 3622 3112 4154 114 174 191 O ATOM 1879 CB LEU A 712 31.242 -16.140 26.580 1.00 31.64 C ANISOU 1879 CB LEU A 712 3986 3527 4508 45 143 248 C ATOM 1880 CG LEU A 712 31.357 -14.678 26.152 1.00 29.81 C ANISOU 1880 CG LEU A 712 3762 3346 4220 40 140 196 C ATOM 1881 CD1 LEU A 712 31.065 -14.550 24.667 1.00 29.73 C ANISOU 1881 CD1 LEU A 712 3788 3291 4217 27 140 133 C ATOM 1882 CD2 LEU A 712 30.397 -13.819 26.963 1.00 28.37 C ANISOU 1882 CD2 LEU A 712 3565 3222 3993 23 134 213 C ATOM 1883 N PHE A 713 34.103 -17.405 27.096 1.00 27.84 N ANISOU 1883 N PHE A 713 3478 3019 4082 122 161 297 N ATOM 1884 CA PHE A 713 35.489 -17.113 27.483 1.00 26.02 C ANISOU 1884 CA PHE A 713 3222 2819 3847 153 161 311 C ATOM 1885 C PHE A 713 36.506 -17.565 26.435 1.00 27.12 C ANISOU 1885 C PHE A 713 3369 2905 4029 181 185 284 C ATOM 1886 O PHE A 713 37.364 -16.781 26.010 1.00 25.73 O ANISOU 1886 O PHE A 713 3182 2752 3841 195 194 260 O ATOM 1887 CB PHE A 713 35.834 -17.760 28.819 1.00 24.94 C ANISOU 1887 CB PHE A 713 3056 2699 3721 171 148 385 C ATOM 1888 CG PHE A 713 37.255 -17.519 29.242 1.00 24.28 C ANISOU 1888 CG PHE A 713 2941 2640 3642 201 138 405 C ATOM 1889 CD1 PHE A 713 37.635 -16.282 29.771 1.00 23.80 C ANISOU 1889 CD1 PHE A 713 2865 2647 3531 199 111 396 C ATOM 1890 CD2 PHE A 713 38.221 -18.511 29.093 1.00 24.10 C ANISOU 1890 CD2 PHE A 713 2904 2572 3682 233 150 432 C ATOM 1891 CE1 PHE A 713 38.949 -16.033 30.157 1.00 23.63 C ANISOU 1891 CE1 PHE A 713 2809 2644 3524 224 91 416 C ATOM 1892 CE2 PHE A 713 39.551 -18.268 29.478 1.00 24.43 C ANISOU 1892 CE2 PHE A 713 2908 2636 3739 260 137 455 C ATOM 1893 CZ PHE A 713 39.911 -17.019 30.006 1.00 24.29 C ANISOU 1893 CZ PHE A 713 2870 2684 3673 253 104 448 C ATOM 1894 N LYS A 714 36.410 -18.823 26.027 1.00 27.50 N ANISOU 1894 N LYS A 714 3436 2882 4129 192 198 291 N ATOM 1895 CA LYS A 714 37.265 -19.323 24.982 1.00 27.75 C ANISOU 1895 CA LYS A 714 3488 2859 4198 226 228 261 C ATOM 1896 C LYS A 714 37.114 -18.464 23.734 1.00 25.97 C ANISOU 1896 C LYS A 714 3297 2635 3935 220 244 191 C ATOM 1897 O LYS A 714 38.108 -18.065 23.112 1.00 25.79 O ANISOU 1897 O LYS A 714 3269 2616 3913 250 273 173 O ATOM 1898 CB LYS A 714 36.944 -20.782 24.665 1.00 29.09 C ANISOU 1898 CB LYS A 714 3687 2943 4425 235 233 267 C ATOM 1899 CG LYS A 714 38.060 -21.467 23.892 1.00 30.12 C ANISOU 1899 CG LYS A 714 3830 3016 4596 286 269 253 C ATOM 1900 CD LYS A 714 37.603 -22.761 23.278 1.00 31.25 C ANISOU 1900 CD LYS A 714 4021 3064 4787 293 270 234 C ATOM 1901 CE LYS A 714 38.613 -23.295 22.289 1.00 32.67 C ANISOU 1901 CE LYS A 714 4231 3187 4994 350 313 203 C ATOM 1902 NZ LYS A 714 37.973 -24.321 21.426 1.00 33.72 N ANISOU 1902 NZ LYS A 714 4434 3223 5154 354 306 158 N ATOM 1903 N LEU A 715 35.865 -18.170 23.382 1.00 25.18 N ANISOU 1903 N LEU A 715 3228 2532 3806 183 225 158 N ATOM 1904 CA LEU A 715 35.574 -17.356 22.214 1.00 24.41 C ANISOU 1904 CA LEU A 715 3168 2436 3670 175 233 94 C ATOM 1905 C LEU A 715 36.236 -16.006 22.338 1.00 25.00 C ANISOU 1905 C LEU A 715 3211 2580 3706 178 242 91 C ATOM 1906 O LEU A 715 36.804 -15.503 21.371 1.00 23.96 O ANISOU 1906 O LEU A 715 3096 2446 3561 198 269 57 O ATOM 1907 CB LEU A 715 34.071 -17.195 22.030 1.00 24.34 C ANISOU 1907 CB LEU A 715 3186 2421 3642 130 202 71 C ATOM 1908 CG LEU A 715 33.443 -18.368 21.284 1.00 25.34 C ANISOU 1908 CG LEU A 715 3361 2460 3806 127 190 47 C ATOM 1909 CD1 LEU A 715 31.913 -18.406 21.424 1.00 25.77 C ANISOU 1909 CD1 LEU A 715 3421 2504 3866 78 150 48 C ATOM 1910 CD2 LEU A 715 33.831 -18.264 19.832 1.00 24.98 C ANISOU 1910 CD2 LEU A 715 3375 2378 3739 154 210 -19 C ATOM 1911 N LEU A 716 36.175 -15.426 23.533 1.00 25.09 N ANISOU 1911 N LEU A 716 3180 2651 3701 161 217 128 N ATOM 1912 CA LEU A 716 36.752 -14.099 23.762 1.00 24.88 C ANISOU 1912 CA LEU A 716 3124 2687 3644 159 213 124 C ATOM 1913 C LEU A 716 38.282 -14.097 23.698 1.00 25.47 C ANISOU 1913 C LEU A 716 3163 2761 3753 196 234 145 C ATOM 1914 O LEU A 716 38.858 -13.211 23.072 1.00 25.02 O ANISOU 1914 O LEU A 716 3097 2720 3688 203 250 124 O ATOM 1915 CB LEU A 716 36.286 -13.520 25.104 1.00 23.00 C ANISOU 1915 CB LEU A 716 2858 2508 3373 137 176 155 C ATOM 1916 CG LEU A 716 34.853 -12.992 25.196 1.00 21.17 C ANISOU 1916 CG LEU A 716 2647 2297 3100 101 160 135 C ATOM 1917 CD1 LEU A 716 34.599 -12.455 26.592 1.00 20.42 C ANISOU 1917 CD1 LEU A 716 2528 2261 2969 95 133 170 C ATOM 1918 CD2 LEU A 716 34.595 -11.930 24.119 1.00 20.10 C ANISOU 1918 CD2 LEU A 716 2533 2169 2936 87 167 79 C ATOM 1919 N LYS A 717 38.933 -15.082 24.322 1.00 28.42 N ANISOU 1919 N LYS A 717 3513 3114 4170 221 234 191 N ATOM 1920 CA LYS A 717 40.400 -15.227 24.231 1.00 30.52 C ANISOU 1920 CA LYS A 717 3739 3372 4484 260 257 218 C ATOM 1921 C LYS A 717 40.909 -15.440 22.810 1.00 31.57 C ANISOU 1921 C LYS A 717 3898 3459 4637 292 313 185 C ATOM 1922 O LYS A 717 42.033 -15.072 22.478 1.00 31.98 O ANISOU 1922 O LYS A 717 3916 3517 4719 321 341 199 O ATOM 1923 CB LYS A 717 40.895 -16.392 25.088 1.00 30.99 C ANISOU 1923 CB LYS A 717 3774 3410 4592 283 248 274 C ATOM 1924 CG LYS A 717 40.690 -16.196 26.563 1.00 31.16 C ANISOU 1924 CG LYS A 717 3767 3480 4591 264 197 318 C ATOM 1925 CD LYS A 717 41.436 -14.975 27.046 1.00 31.10 C ANISOU 1925 CD LYS A 717 3716 3529 4569 260 166 325 C ATOM 1926 CE LYS A 717 42.939 -15.200 27.030 1.00 31.48 C ANISOU 1926 CE LYS A 717 3713 3565 4684 295 174 362 C ATOM 1927 NZ LYS A 717 43.651 -14.027 27.590 1.00 31.48 N ANISOU 1927 NZ LYS A 717 3667 3615 4681 286 130 374 N ATOM 1928 N GLU A 718 40.102 -16.051 21.965 1.00 33.09 N ANISOU 1928 N GLU A 718 4153 3604 4816 292 330 144 N ATOM 1929 CA GLU A 718 40.567 -16.319 20.621 1.00 34.60 C ANISOU 1929 CA GLU A 718 4383 3750 5014 332 384 110 C ATOM 1930 C GLU A 718 40.102 -15.261 19.635 1.00 32.37 C ANISOU 1930 C GLU A 718 4135 3486 4676 317 395 60 C ATOM 1931 O GLU A 718 40.196 -15.452 18.430 1.00 32.13 O ANISOU 1931 O GLU A 718 4156 3419 4631 347 436 22 O ATOM 1932 CB GLU A 718 40.130 -17.710 20.195 1.00 38.00 C ANISOU 1932 CB GLU A 718 4869 4105 5465 350 392 92 C ATOM 1933 CG GLU A 718 40.940 -18.778 20.911 1.00 41.09 C ANISOU 1933 CG GLU A 718 5223 4467 5921 382 400 146 C ATOM 1934 CD GLU A 718 40.315 -20.151 20.821 1.00 43.43 C ANISOU 1934 CD GLU A 718 5567 4689 6245 386 390 137 C ATOM 1935 OE1 GLU A 718 39.198 -20.237 20.261 1.00 44.42 O ANISOU 1935 OE1 GLU A 718 5750 4788 6340 359 370 90 O ATOM 1936 OE2 GLU A 718 40.937 -21.135 21.304 1.00 45.69 O ANISOU 1936 OE2 GLU A 718 5830 4941 6588 416 399 179 O ATOM 1937 N GLY A 719 39.611 -14.138 20.152 1.00 30.73 N ANISOU 1937 N GLY A 719 3904 3337 4435 274 359 59 N ATOM 1938 CA GLY A 719 39.464 -12.938 19.351 1.00 28.69 C ANISOU 1938 CA GLY A 719 3659 3106 4135 264 371 25 C ATOM 1939 C GLY A 719 38.052 -12.486 19.040 1.00 26.55 C ANISOU 1939 C GLY A 719 3435 2842 3811 223 340 -19 C ATOM 1940 O GLY A 719 37.847 -11.414 18.464 1.00 25.93 O ANISOU 1940 O GLY A 719 3365 2790 3697 210 344 -43 O ATOM 1941 N HIS A 720 37.068 -13.285 19.424 1.00 24.40 N ANISOU 1941 N HIS A 720 3187 2545 3539 201 308 -23 N ATOM 1942 CA HIS A 720 35.684 -12.950 19.098 1.00 22.84 C ANISOU 1942 CA HIS A 720 3028 2348 3303 162 277 -59 C ATOM 1943 C HIS A 720 35.174 -11.711 19.812 1.00 21.99 C ANISOU 1943 C HIS A 720 2886 2305 3166 125 247 -52 C ATOM 1944 O HIS A 720 35.357 -11.558 21.019 1.00 20.19 O ANISOU 1944 O HIS A 720 2611 2113 2947 116 228 -13 O ATOM 1945 CB HIS A 720 34.760 -14.116 19.414 1.00 22.62 C ANISOU 1945 CB HIS A 720 3022 2275 3299 145 248 -55 C ATOM 1946 CG HIS A 720 33.315 -13.804 19.208 1.00 23.01 C ANISOU 1946 CG HIS A 720 3096 2323 3323 102 211 -81 C ATOM 1947 ND1 HIS A 720 32.703 -13.901 17.979 1.00 23.24 N ANISOU 1947 ND1 HIS A 720 3187 2310 3332 100 203 -133 N ATOM 1948 CD2 HIS A 720 32.356 -13.396 20.078 1.00 22.81 C ANISOU 1948 CD2 HIS A 720 3042 2334 3292 64 179 -59 C ATOM 1949 CE1 HIS A 720 31.430 -13.564 18.094 1.00 23.25 C ANISOU 1949 CE1 HIS A 720 3190 2320 3323 57 163 -140 C ATOM 1950 NE2 HIS A 720 31.196 -13.264 19.361 1.00 23.29 N ANISOU 1950 NE2 HIS A 720 3139 2373 3338 36 153 -94 N ATOM 1951 N ARG A 721 34.526 -10.842 19.036 1.00 22.51 N ANISOU 1951 N ARG A 721 2979 2382 3192 107 242 -90 N ATOM 1952 CA ARG A 721 33.873 -9.630 19.521 1.00 16.38 C ANISOU 1952 CA ARG A 721 2180 1658 2385 74 215 -92 C ATOM 1953 C ARG A 721 32.547 -9.456 18.803 1.00 21.36 C ANISOU 1953 C ARG A 721 2854 2273 2988 47 194 -129 C ATOM 1954 O ARG A 721 32.401 -9.901 17.673 1.00 22.92 O ANISOU 1954 O ARG A 721 3103 2427 3179 58 203 -162 O ATOM 1955 CB ARG A 721 34.748 -8.415 19.277 1.00 16.21 C ANISOU 1955 CB ARG A 721 2135 1673 2352 83 233 -94 C ATOM 1956 CG ARG A 721 36.124 -8.501 19.899 1.00 16.44 C ANISOU 1956 CG ARG A 721 2114 1714 2418 108 247 -56 C ATOM 1957 CD ARG A 721 36.013 -8.442 21.390 1.00 16.34 C ANISOU 1957 CD ARG A 721 2062 1736 2409 92 209 -24 C ATOM 1958 NE ARG A 721 37.305 -8.240 22.027 1.00 17.87 N ANISOU 1958 NE ARG A 721 2205 1948 2636 110 206 11 N ATOM 1959 CZ ARG A 721 38.080 -9.209 22.504 1.00 16.93 C ANISOU 1959 CZ ARG A 721 2064 1812 2557 135 213 47 C ATOM 1960 NH1 ARG A 721 37.700 -10.472 22.400 1.00 17.14 N ANISOU 1960 NH1 ARG A 721 2118 1799 2596 145 225 52 N ATOM 1961 NH2 ARG A 721 39.243 -8.901 23.080 1.00 17.16 N ANISOU 1961 NH2 ARG A 721 2041 1858 2619 148 201 80 N ATOM 1962 N MET A 722 31.584 -8.798 19.437 1.00 21.54 N ANISOU 1962 N MET A 722 2858 2330 2995 14 165 -124 N ATOM 1963 CA MET A 722 30.303 -8.544 18.789 1.00 21.83 C ANISOU 1963 CA MET A 722 2926 2355 3014 -13 141 -153 C ATOM 1964 C MET A 722 30.450 -7.658 17.552 1.00 24.13 C ANISOU 1964 C MET A 722 3250 2647 3270 -7 152 -192 C ATOM 1965 O MET A 722 31.354 -6.831 17.466 1.00 24.34 O ANISOU 1965 O MET A 722 3260 2703 3286 9 176 -190 O ATOM 1966 CB MET A 722 29.314 -7.924 19.781 1.00 21.00 C ANISOU 1966 CB MET A 722 2787 2290 2901 -43 117 -133 C ATOM 1967 CG MET A 722 28.806 -8.953 20.786 1.00 21.56 C ANISOU 1967 CG MET A 722 2836 2350 3004 -51 108 -92 C ATOM 1968 SD MET A 722 27.578 -8.372 21.986 1.00 25.81 S ANISOU 1968 SD MET A 722 3338 2935 3533 -74 93 -59 S ATOM 1969 CE MET A 722 28.591 -7.274 23.015 1.00 16.05 C ANISOU 1969 CE MET A 722 2074 1766 2258 -53 104 -49 C ATOM 1970 N ASP A 723 29.560 -7.862 16.589 1.00 27.20 N ANISOU 1970 N ASP A 723 3687 3002 3647 -19 131 -225 N ATOM 1971 CA ASP A 723 29.536 -7.073 15.367 1.00 29.48 C ANISOU 1971 CA ASP A 723 4015 3290 3895 -12 137 -260 C ATOM 1972 C ASP A 723 29.039 -5.655 15.609 1.00 26.88 C ANISOU 1972 C ASP A 723 3657 3011 3545 -36 125 -258 C ATOM 1973 O ASP A 723 28.350 -5.383 16.592 1.00 24.83 O ANISOU 1973 O ASP A 723 3359 2778 3299 -61 104 -238 O ATOM 1974 CB ASP A 723 28.648 -7.747 14.333 1.00 34.08 C ANISOU 1974 CB ASP A 723 4661 3819 4468 -19 105 -296 C ATOM 1975 CG ASP A 723 29.164 -9.098 13.934 1.00 40.54 C ANISOU 1975 CG ASP A 723 5522 4580 5303 10 115 -307 C ATOM 1976 OD1 ASP A 723 30.406 -9.262 13.882 1.00 42.17 O ANISOU 1976 OD1 ASP A 723 5725 4788 5508 49 164 -298 O ATOM 1977 OD2 ASP A 723 28.331 -10.000 13.691 1.00 45.40 O ANISOU 1977 OD2 ASP A 723 6169 5143 5938 -6 73 -323 O ATOM 1978 N LYS A 724 29.379 -4.764 14.690 1.00 24.97 N ANISOU 1978 N LYS A 724 3437 2781 3271 -24 142 -277 N ATOM 1979 CA LYS A 724 28.884 -3.402 14.727 1.00 22.98 C ANISOU 1979 CA LYS A 724 3165 2566 3000 -44 129 -279 C ATOM 1980 C LYS A 724 27.365 -3.361 14.554 1.00 20.98 C ANISOU 1980 C LYS A 724 2926 2303 2743 -76 82 -293 C ATOM 1981 O LYS A 724 26.851 -3.855 13.555 1.00 20.01 O ANISOU 1981 O LYS A 724 2855 2142 2606 -76 62 -318 O ATOM 1982 CB LYS A 724 29.565 -2.567 13.637 1.00 21.83 C ANISOU 1982 CB LYS A 724 3044 2427 2825 -22 159 -291 C ATOM 1983 CG LYS A 724 29.168 -1.134 13.663 1.00 21.37 C ANISOU 1983 CG LYS A 724 2963 2402 2753 -41 147 -290 C ATOM 1984 CD LYS A 724 30.060 -0.249 12.790 1.00 21.06 C ANISOU 1984 CD LYS A 724 2933 2373 2697 -18 185 -286 C ATOM 1985 CE LYS A 724 29.362 0.134 11.501 1.00 21.23 C ANISOU 1985 CE LYS A 724 3011 2381 2674 -17 176 -309 C ATOM 1986 NZ LYS A 724 27.933 0.530 11.697 1.00 20.80 N ANISOU 1986 NZ LYS A 724 2954 2332 2616 -52 122 -322 N ATOM 1987 N PRO A 725 26.641 -2.779 15.524 1.00 19.65 N ANISOU 1987 N PRO A 725 2713 2167 2587 -100 64 -276 N ATOM 1988 CA PRO A 725 25.226 -2.445 15.301 1.00 19.21 C ANISOU 1988 CA PRO A 725 2659 2107 2531 -128 26 -283 C ATOM 1989 C PRO A 725 25.068 -1.391 14.200 1.00 19.83 C ANISOU 1989 C PRO A 725 2767 2191 2576 -128 20 -306 C ATOM 1990 O PRO A 725 25.925 -0.518 14.078 1.00 20.64 O ANISOU 1990 O PRO A 725 2863 2319 2662 -112 48 -306 O ATOM 1991 CB PRO A 725 24.765 -1.879 16.653 1.00 19.02 C ANISOU 1991 CB PRO A 725 2580 2124 2522 -141 26 -255 C ATOM 1992 CG PRO A 725 25.810 -2.285 17.625 1.00 19.48 C ANISOU 1992 CG PRO A 725 2614 2198 2589 -123 52 -234 C ATOM 1993 CD PRO A 725 27.094 -2.386 16.866 1.00 19.33 C ANISOU 1993 CD PRO A 725 2620 2166 2559 -99 77 -248 C ATOM 1994 N ALA A 726 23.996 -1.472 13.415 1.00 20.21 N ANISOU 1994 N ALA A 726 2844 2214 2620 -145 -20 -322 N ATOM 1995 CA ALA A 726 23.742 -0.525 12.338 1.00 20.54 C ANISOU 1995 CA ALA A 726 2917 2259 2627 -143 -32 -342 C ATOM 1996 C ALA A 726 23.585 0.912 12.810 1.00 19.73 C ANISOU 1996 C ALA A 726 2772 2201 2523 -151 -23 -329 C ATOM 1997 O ALA A 726 23.853 1.836 12.051 1.00 19.19 O ANISOU 1997 O ALA A 726 2723 2143 2427 -142 -14 -337 O ATOM 1998 CB ALA A 726 22.515 -0.931 11.588 1.00 15.05 C ANISOU 1998 CB ALA A 726 2254 1528 1935 -164 -89 -357 C ATOM 1999 N ASN A 727 23.131 1.124 14.042 1.00 20.42 N ANISOU 1999 N ASN A 727 2806 2313 2639 -165 -24 -308 N ATOM 2000 CA ASN A 727 22.885 2.491 14.494 1.00 21.09 C ANISOU 2000 CA ASN A 727 2858 2434 2722 -169 -20 -301 C ATOM 2001 C ASN A 727 24.183 3.129 14.919 1.00 21.77 C ANISOU 2001 C ASN A 727 2929 2543 2799 -150 14 -299 C ATOM 2002 O ASN A 727 24.240 4.289 15.308 1.00 22.71 O ANISOU 2002 O ASN A 727 3025 2687 2917 -150 17 -297 O ATOM 2003 CB ASN A 727 21.862 2.518 15.626 1.00 20.73 C ANISOU 2003 CB ASN A 727 2768 2404 2704 -182 -31 -280 C ATOM 2004 CG ASN A 727 20.450 2.239 15.137 1.00 20.86 C ANISOU 2004 CG ASN A 727 2785 2399 2744 -205 -70 -276 C ATOM 2005 OD1 ASN A 727 20.018 2.769 14.120 1.00 21.19 O ANISOU 2005 OD1 ASN A 727 2850 2428 2773 -211 -95 -290 O ATOM 2006 ND2 ASN A 727 19.732 1.387 15.854 1.00 21.03 N ANISOU 2006 ND2 ASN A 727 2778 2411 2801 -216 -78 -251 N ATOM 2007 N CYS A 728 25.241 2.358 14.775 1.00 23.11 N ANISOU 2007 N CYS A 728 3114 2701 2967 -134 37 -298 N ATOM 2008 CA CYS A 728 26.538 2.709 15.302 1.00 23.96 C ANISOU 2008 CA CYS A 728 3198 2826 3081 -118 65 -288 C ATOM 2009 C CYS A 728 27.441 3.198 14.172 1.00 27.14 C ANISOU 2009 C CYS A 728 3623 3220 3469 -101 91 -291 C ATOM 2010 O CYS A 728 27.472 2.573 13.109 1.00 29.52 O ANISOU 2010 O CYS A 728 3970 3497 3750 -89 100 -301 O ATOM 2011 CB CYS A 728 27.118 1.476 15.993 1.00 24.44 C ANISOU 2011 CB CYS A 728 3251 2879 3158 -108 77 -275 C ATOM 2012 SG CYS A 728 28.396 1.786 17.098 1.00 49.54 S ANISOU 2012 SG CYS A 728 6387 6082 6353 -95 92 -257 S ATOM 2013 N THR A 729 28.158 4.305 14.373 1.00 26.53 N ANISOU 2013 N THR A 729 3517 3161 3402 -98 103 -282 N ATOM 2014 CA THR A 729 29.141 4.737 13.366 1.00 28.25 C ANISOU 2014 CA THR A 729 3746 3371 3617 -79 138 -272 C ATOM 2015 C THR A 729 30.402 3.898 13.504 1.00 26.21 C ANISOU 2015 C THR A 729 3477 3104 3377 -56 172 -255 C ATOM 2016 O THR A 729 30.578 3.223 14.501 1.00 26.82 O ANISOU 2016 O THR A 729 3532 3185 3472 -59 163 -251 O ATOM 2017 CB THR A 729 29.514 6.250 13.479 1.00 15.31 C ANISOU 2017 CB THR A 729 2073 1746 1997 -87 137 -260 C ATOM 2018 OG1 THR A 729 30.111 6.531 14.756 1.00 14.60 O ANISOU 2018 OG1 THR A 729 1935 1670 1941 -93 124 -252 O ATOM 2019 CG2 THR A 729 28.287 7.126 13.295 1.00 14.76 C ANISOU 2019 CG2 THR A 729 2014 1683 1913 -105 106 -275 C ATOM 2020 N ASN A 730 31.277 3.934 12.508 1.00 26.39 N ANISOU 2020 N ASN A 730 3517 3116 3396 -31 216 -241 N ATOM 2021 CA ASN A 730 32.552 3.237 12.606 1.00 26.54 C ANISOU 2021 CA ASN A 730 3517 3125 3440 -4 255 -219 C ATOM 2022 C ASN A 730 33.347 3.714 13.793 1.00 27.58 C ANISOU 2022 C ASN A 730 3581 3274 3625 -16 243 -196 C ATOM 2023 O ASN A 730 33.991 2.918 14.491 1.00 26.29 O ANISOU 2023 O ASN A 730 3394 3108 3487 -6 246 -184 O ATOM 2024 CB ASN A 730 33.378 3.434 11.350 1.00 28.83 C ANISOU 2024 CB ASN A 730 3828 3405 3720 30 313 -199 C ATOM 2025 CG ASN A 730 32.943 2.529 10.220 1.00 30.99 C ANISOU 2025 CG ASN A 730 4182 3656 3939 57 332 -223 C ATOM 2026 OD1 ASN A 730 32.361 1.456 10.442 1.00 33.24 O ANISOU 2026 OD1 ASN A 730 4496 3924 4209 54 307 -249 O ATOM 2027 ND2 ASN A 730 33.242 2.945 8.990 1.00 32.15 N ANISOU 2027 ND2 ASN A 730 4365 3798 4052 86 374 -213 N ATOM 2028 N GLU A 731 33.298 5.025 14.009 1.00 27.74 N ANISOU 2028 N GLU A 731 3571 3307 3661 -35 222 -192 N ATOM 2029 CA GLU A 731 34.024 5.635 15.093 1.00 27.91 C ANISOU 2029 CA GLU A 731 3534 3339 3731 -47 197 -176 C ATOM 2030 C GLU A 731 33.541 5.131 16.445 1.00 25.57 C ANISOU 2030 C GLU A 731 3231 3057 3429 -59 154 -192 C ATOM 2031 O GLU A 731 34.345 4.779 17.299 1.00 26.15 O ANISOU 2031 O GLU A 731 3270 3133 3533 -55 143 -177 O ATOM 2032 CB GLU A 731 33.914 7.152 15.028 1.00 28.62 C ANISOU 2032 CB GLU A 731 3602 3432 3838 -66 177 -174 C ATOM 2033 CG GLU A 731 34.657 7.817 16.150 1.00 29.66 C ANISOU 2033 CG GLU A 731 3679 3567 4021 -79 139 -164 C ATOM 2034 CD GLU A 731 34.776 9.317 15.976 1.00 32.01 C ANISOU 2034 CD GLU A 731 3953 3858 4351 -96 121 -158 C ATOM 2035 OE1 GLU A 731 33.980 9.903 15.196 1.00 33.48 O ANISOU 2035 OE1 GLU A 731 4168 4043 4510 -100 130 -168 O ATOM 2036 OE2 GLU A 731 35.676 9.913 16.621 1.00 32.57 O ANISOU 2036 OE2 GLU A 731 3975 3921 4481 -105 92 -142 O ATOM 2037 N LEU A 732 32.230 5.098 16.648 1.00 24.52 N ANISOU 2037 N LEU A 732 3126 2931 3257 -73 130 -219 N ATOM 2038 CA LEU A 732 31.696 4.632 17.919 1.00 23.15 C ANISOU 2038 CA LEU A 732 2948 2774 3075 -80 99 -227 C ATOM 2039 C LEU A 732 31.925 3.130 18.105 1.00 22.58 C ANISOU 2039 C LEU A 732 2884 2692 3003 -66 114 -217 C ATOM 2040 O LEU A 732 32.153 2.648 19.222 1.00 23.69 O ANISOU 2040 O LEU A 732 3007 2844 3151 -64 97 -207 O ATOM 2041 CB LEU A 732 30.222 4.964 18.016 1.00 24.40 C ANISOU 2041 CB LEU A 732 3129 2942 3202 -95 78 -249 C ATOM 2042 CG LEU A 732 30.007 6.447 18.253 1.00 25.56 C ANISOU 2042 CG LEU A 732 3262 3100 3352 -105 55 -261 C ATOM 2043 CD1 LEU A 732 28.584 6.853 17.905 1.00 25.67 C ANISOU 2043 CD1 LEU A 732 3297 3116 3340 -116 46 -278 C ATOM 2044 CD2 LEU A 732 30.306 6.757 19.705 1.00 25.95 C ANISOU 2044 CD2 LEU A 732 3287 3166 3407 -103 23 -263 C ATOM 2045 N TYR A 733 31.879 2.389 17.012 1.00 20.96 N ANISOU 2045 N TYR A 733 2712 2465 2788 -55 145 -219 N ATOM 2046 CA TYR A 733 32.223 0.982 17.081 1.00 19.93 C ANISOU 2046 CA TYR A 733 2592 2317 2665 -38 162 -209 C ATOM 2047 C TYR A 733 33.701 0.807 17.472 1.00 18.57 C ANISOU 2047 C TYR A 733 2379 2144 2532 -19 180 -180 C ATOM 2048 O TYR A 733 34.027 -0.030 18.312 1.00 17.72 O ANISOU 2048 O TYR A 733 2256 2036 2441 -13 172 -166 O ATOM 2049 CB TYR A 733 31.930 0.280 15.750 1.00 17.84 C ANISOU 2049 CB TYR A 733 2379 2021 2377 -25 189 -224 C ATOM 2050 CG TYR A 733 32.167 -1.215 15.796 1.00 17.01 C ANISOU 2050 CG TYR A 733 2291 1889 2281 -7 202 -220 C ATOM 2051 CD1 TYR A 733 31.549 -2.004 16.760 1.00 16.01 C ANISOU 2051 CD1 TYR A 733 2158 1762 2163 -20 175 -216 C ATOM 2052 CD2 TYR A 733 32.998 -1.842 14.869 1.00 16.38 C ANISOU 2052 CD2 TYR A 733 2238 1782 2203 27 245 -217 C ATOM 2053 CE1 TYR A 733 31.751 -3.364 16.802 1.00 16.12 C ANISOU 2053 CE1 TYR A 733 2186 1746 2192 -5 185 -209 C ATOM 2054 CE2 TYR A 733 33.201 -3.197 14.904 1.00 16.38 C ANISOU 2054 CE2 TYR A 733 2257 1752 2214 46 256 -216 C ATOM 2055 CZ TYR A 733 32.579 -3.957 15.875 1.00 16.31 C ANISOU 2055 CZ TYR A 733 2238 1741 2220 27 223 -213 C ATOM 2056 OH TYR A 733 32.794 -5.326 15.919 1.00 16.32 O ANISOU 2056 OH TYR A 733 2257 1706 2239 45 233 -209 O ATOM 2057 N MET A 734 34.594 1.584 16.864 1.00 18.02 N ANISOU 2057 N MET A 734 2289 2072 2485 -11 203 -166 N ATOM 2058 CA MET A 734 36.002 1.482 17.197 1.00 18.21 C ANISOU 2058 CA MET A 734 2265 2094 2561 6 217 -132 C ATOM 2059 C MET A 734 36.212 1.806 18.673 1.00 18.36 C ANISOU 2059 C MET A 734 2243 2133 2600 -11 164 -125 C ATOM 2060 O MET A 734 37.013 1.176 19.348 1.00 19.03 O ANISOU 2060 O MET A 734 2299 2217 2717 1 158 -101 O ATOM 2061 CB MET A 734 36.834 2.391 16.301 1.00 17.66 C ANISOU 2061 CB MET A 734 2173 2017 2519 15 252 -110 C ATOM 2062 CG MET A 734 37.014 1.801 14.912 1.00 17.89 C ANISOU 2062 CG MET A 734 2243 2025 2528 48 317 -107 C ATOM 2063 SD MET A 734 37.689 0.136 15.046 1.00 44.81 S ANISOU 2063 SD MET A 734 5659 5414 5955 84 349 -93 S ATOM 2064 CE MET A 734 37.293 -0.565 13.440 1.00 76.06 C ANISOU 2064 CE MET A 734 9701 9344 9856 120 406 -116 C ATOM 2065 N MET A 735 35.459 2.762 19.182 1.00 19.02 N ANISOU 2065 N MET A 735 2330 2235 2663 -34 124 -147 N ATOM 2066 CA MET A 735 35.475 3.045 20.608 1.00 19.77 C ANISOU 2066 CA MET A 735 2404 2350 2758 -44 70 -148 C ATOM 2067 C MET A 735 35.095 1.785 21.385 1.00 20.85 C ANISOU 2067 C MET A 735 2557 2494 2873 -34 66 -143 C ATOM 2068 O MET A 735 35.795 1.354 22.315 1.00 20.03 O ANISOU 2068 O MET A 735 2427 2395 2787 -25 44 -123 O ATOM 2069 CB MET A 735 34.521 4.196 20.929 1.00 19.62 C ANISOU 2069 CB MET A 735 2399 2346 2708 -63 37 -178 C ATOM 2070 CG MET A 735 34.414 4.533 22.395 1.00 20.25 C ANISOU 2070 CG MET A 735 2473 2447 2773 -65 -16 -187 C ATOM 2071 SD MET A 735 33.478 6.068 22.655 1.00 36.79 S ANISOU 2071 SD MET A 735 4585 4553 4841 -79 -50 -224 S ATOM 2072 CE MET A 735 34.448 7.167 21.618 1.00 26.08 C ANISOU 2072 CE MET A 735 3195 3169 3544 -92 -45 -214 C ATOM 2073 N MET A 736 33.970 1.213 20.978 1.00 21.27 N ANISOU 2073 N MET A 736 2648 2542 2891 -37 84 -159 N ATOM 2074 CA MET A 736 33.458 -0.040 21.495 1.00 21.87 C ANISOU 2074 CA MET A 736 2739 2616 2953 -31 87 -150 C ATOM 2075 C MET A 736 34.553 -1.127 21.473 1.00 21.97 C ANISOU 2075 C MET A 736 2737 2610 3002 -10 107 -122 C ATOM 2076 O MET A 736 34.893 -1.685 22.503 1.00 21.51 O ANISOU 2076 O MET A 736 2661 2560 2951 -2 89 -100 O ATOM 2077 CB MET A 736 32.240 -0.426 20.652 1.00 21.70 C ANISOU 2077 CB MET A 736 2758 2580 2908 -41 104 -169 C ATOM 2078 CG MET A 736 31.176 -1.264 21.281 1.00 21.36 C ANISOU 2078 CG MET A 736 2728 2539 2850 -47 95 -163 C ATOM 2079 SD MET A 736 29.816 -1.533 20.106 1.00 34.63 S ANISOU 2079 SD MET A 736 4449 4193 4518 -64 101 -186 S ATOM 2080 CE MET A 736 28.955 0.038 20.132 1.00 13.94 C ANISOU 2080 CE MET A 736 1824 1601 1872 -81 82 -207 C ATOM 2081 N ARG A 737 35.121 -1.399 20.301 1.00 22.86 N ANISOU 2081 N ARG A 737 2855 2696 3134 4 148 -120 N ATOM 2082 CA ARG A 737 36.200 -2.379 20.161 1.00 24.57 C ANISOU 2082 CA ARG A 737 3056 2890 3388 31 176 -93 C ATOM 2083 C ARG A 737 37.424 -2.051 21.040 1.00 25.01 C ANISOU 2083 C ARG A 737 3054 2959 3487 37 153 -60 C ATOM 2084 O ARG A 737 38.149 -2.948 21.464 1.00 24.51 O ANISOU 2084 O ARG A 737 2972 2887 3456 56 158 -32 O ATOM 2085 CB ARG A 737 36.649 -2.488 18.697 1.00 26.00 C ANISOU 2085 CB ARG A 737 3257 3043 3577 52 230 -97 C ATOM 2086 CG ARG A 737 35.618 -3.016 17.691 1.00 27.12 C ANISOU 2086 CG ARG A 737 3464 3162 3679 53 248 -130 C ATOM 2087 CD ARG A 737 35.408 -4.518 17.804 1.00 28.31 C ANISOU 2087 CD ARG A 737 3640 3282 3834 67 254 -129 C ATOM 2088 NE ARG A 737 36.618 -5.278 17.483 1.00 29.61 N ANISOU 2088 NE ARG A 737 3794 3423 4034 106 296 -106 N ATOM 2089 CZ ARG A 737 36.644 -6.358 16.709 1.00 30.89 C ANISOU 2089 CZ ARG A 737 4002 3543 4193 134 328 -118 C ATOM 2090 NH1 ARG A 737 35.521 -6.816 16.161 1.00 31.05 N ANISOU 2090 NH1 ARG A 737 4081 3538 4177 123 313 -154 N ATOM 2091 NH2 ARG A 737 37.799 -6.979 16.489 1.00 32.11 N ANISOU 2091 NH2 ARG A 737 4141 3676 4382 175 372 -93 N ATOM 2092 N ASP A 738 37.658 -0.770 21.301 1.00 25.73 N ANISOU 2092 N ASP A 738 3120 3070 3587 21 123 -64 N ATOM 2093 CA ASP A 738 38.776 -0.366 22.145 1.00 27.05 C ANISOU 2093 CA ASP A 738 3233 3244 3799 22 86 -37 C ATOM 2094 C ASP A 738 38.558 -0.686 23.629 1.00 25.67 C ANISOU 2094 C ASP A 738 3059 3092 3602 19 31 -33 C ATOM 2095 O ASP A 738 39.523 -1.007 24.329 1.00 25.02 O ANISOU 2095 O ASP A 738 2940 3010 3558 30 5 -2 O ATOM 2096 CB ASP A 738 39.053 1.128 21.983 1.00 29.30 C ANISOU 2096 CB ASP A 738 3493 3535 4103 3 61 -45 C ATOM 2097 CG ASP A 738 39.767 1.445 20.692 1.00 31.33 C ANISOU 2097 CG ASP A 738 3730 3771 4405 13 115 -26 C ATOM 2098 OD1 ASP A 738 40.401 0.516 20.145 1.00 34.07 O ANISOU 2098 OD1 ASP A 738 4068 4099 4777 40 165 0 O ATOM 2099 OD2 ASP A 738 39.683 2.610 20.224 1.00 34.05 O ANISOU 2099 OD2 ASP A 738 4066 4115 4755 -3 111 -35 O ATOM 2100 N CYS A 739 37.309 -0.564 24.105 1.00 23.77 N ANISOU 2100 N CYS A 739 2858 2871 3301 8 15 -60 N ATOM 2101 CA CYS A 739 36.932 -1.004 25.453 1.00 22.33 C ANISOU 2101 CA CYS A 739 2687 2712 3085 13 -22 -52 C ATOM 2102 C CYS A 739 37.115 -2.506 25.614 1.00 21.76 C ANISOU 2102 C CYS A 739 2614 2626 3026 31 2 -20 C ATOM 2103 O CYS A 739 37.345 -2.995 26.712 1.00 21.08 O ANISOU 2103 O CYS A 739 2523 2555 2932 43 -27 4 O ATOM 2104 CB CYS A 739 35.479 -0.653 25.771 1.00 21.94 C ANISOU 2104 CB CYS A 739 2677 2684 2974 2 -26 -79 C ATOM 2105 SG CYS A 739 35.087 1.100 25.748 1.00 23.84 S ANISOU 2105 SG CYS A 739 2926 2940 3194 -15 -57 -119 S ATOM 2106 N TRP A 740 36.979 -3.228 24.512 1.00 21.65 N ANISOU 2106 N TRP A 740 2614 2582 3029 36 54 -21 N ATOM 2107 CA TRP A 740 37.132 -4.676 24.504 1.00 21.60 C ANISOU 2107 CA TRP A 740 2612 2553 3043 55 79 4 C ATOM 2108 C TRP A 740 38.547 -5.111 24.128 1.00 21.09 C ANISOU 2108 C TRP A 740 2511 2465 3039 78 99 33 C ATOM 2109 O TRP A 740 38.748 -6.209 23.611 1.00 20.73 O ANISOU 2109 O TRP A 740 2474 2387 3016 98 138 45 O ATOM 2110 CB TRP A 740 36.143 -5.317 23.522 1.00 19.97 C ANISOU 2110 CB TRP A 740 2449 2319 2821 50 118 -17 C ATOM 2111 CG TRP A 740 34.735 -5.091 23.884 1.00 18.91 C ANISOU 2111 CG TRP A 740 2341 2202 2642 29 102 -34 C ATOM 2112 CD1 TRP A 740 34.229 -4.904 25.140 1.00 18.14 C ANISOU 2112 CD1 TRP A 740 2240 2138 2513 25 71 -21 C ATOM 2113 CD2 TRP A 740 33.624 -5.010 22.982 1.00 18.11 C ANISOU 2113 CD2 TRP A 740 2274 2086 2521 13 117 -64 C ATOM 2114 NE1 TRP A 740 32.873 -4.714 25.070 1.00 17.97 N ANISOU 2114 NE1 TRP A 740 2243 2124 2461 8 74 -37 N ATOM 2115 CE2 TRP A 740 32.476 -4.782 23.763 1.00 17.44 C ANISOU 2115 CE2 TRP A 740 2196 2026 2404 -3 97 -63 C ATOM 2116 CE3 TRP A 740 33.494 -5.120 21.601 1.00 18.03 C ANISOU 2116 CE3 TRP A 740 2292 2043 2515 13 144 -90 C ATOM 2117 CZ2 TRP A 740 31.210 -4.655 23.203 1.00 17.35 C ANISOU 2117 CZ2 TRP A 740 2209 2007 2378 -22 100 -84 C ATOM 2118 CZ3 TRP A 740 32.235 -4.990 21.047 1.00 17.76 C ANISOU 2118 CZ3 TRP A 740 2289 2001 2458 -7 139 -115 C ATOM 2119 CH2 TRP A 740 31.108 -4.761 21.848 1.00 17.21 C ANISOU 2119 CH2 TRP A 740 2216 1955 2368 -27 116 -111 C ATOM 2120 N HIS A 741 39.528 -4.252 24.354 1.00 21.39 N ANISOU 2120 N HIS A 741 2505 2514 3108 77 74 45 N ATOM 2121 CA HIS A 741 40.875 -4.642 24.004 1.00 21.32 C ANISOU 2121 CA HIS A 741 2451 2483 3167 101 97 81 C ATOM 2122 C HIS A 741 41.318 -5.823 24.866 1.00 21.18 C ANISOU 2122 C HIS A 741 2419 2459 3171 121 83 119 C ATOM 2123 O HIS A 741 40.997 -5.881 26.059 1.00 20.30 O ANISOU 2123 O HIS A 741 2312 2372 3029 114 33 126 O ATOM 2124 CB HIS A 741 41.842 -3.483 24.160 1.00 21.77 C ANISOU 2124 CB HIS A 741 2454 2549 3268 91 63 94 C ATOM 2125 CG HIS A 741 43.071 -3.645 23.337 1.00 22.64 C ANISOU 2125 CG HIS A 741 2516 2633 3453 115 109 130 C ATOM 2126 ND1 HIS A 741 44.109 -4.466 23.715 1.00 23.86 N ANISOU 2126 ND1 HIS A 741 2626 2773 3667 140 111 176 N ATOM 2127 CD2 HIS A 741 43.411 -3.131 22.136 1.00 23.38 C ANISOU 2127 CD2 HIS A 741 2600 2712 3573 122 163 130 C ATOM 2128 CE1 HIS A 741 45.047 -4.437 22.785 1.00 24.58 C ANISOU 2128 CE1 HIS A 741 2677 2841 3821 162 166 205 C ATOM 2129 NE2 HIS A 741 44.651 -3.635 21.816 1.00 24.20 N ANISOU 2129 NE2 HIS A 741 2651 2793 3752 153 201 179 N ATOM 2130 N ALA A 742 42.042 -6.764 24.263 1.00 21.52 N ANISOU 2130 N ALA A 742 2446 2468 3262 151 131 144 N ATOM 2131 CA ALA A 742 42.519 -7.928 25.011 1.00 21.74 C ANISOU 2131 CA ALA A 742 2457 2485 3318 173 122 185 C ATOM 2132 C ALA A 742 43.463 -7.523 26.156 1.00 21.14 C ANISOU 2132 C ALA A 742 2325 2432 3276 172 56 222 C ATOM 2133 O ALA A 742 43.441 -8.127 27.223 1.00 19.69 O ANISOU 2133 O ALA A 742 2141 2259 3081 178 17 247 O ATOM 2134 CB ALA A 742 43.195 -8.918 24.084 1.00 22.08 C ANISOU 2134 CB ALA A 742 2494 2484 3413 210 188 203 C ATOM 2135 N VAL A 743 44.269 -6.491 25.951 1.00 21.07 N ANISOU 2135 N VAL A 743 2269 2428 3307 164 38 228 N ATOM 2136 CA VAL A 743 45.162 -6.003 26.999 1.00 21.59 C ANISOU 2136 CA VAL A 743 2283 2511 3410 158 -38 259 C ATOM 2137 C VAL A 743 44.534 -4.832 27.776 1.00 21.21 C ANISOU 2137 C VAL A 743 2259 2497 3302 126 -110 223 C ATOM 2138 O VAL A 743 44.288 -3.782 27.200 1.00 21.54 O ANISOU 2138 O VAL A 743 2304 2541 3338 106 -105 192 O ATOM 2139 CB VAL A 743 46.507 -5.558 26.383 1.00 21.24 C ANISOU 2139 CB VAL A 743 2163 2445 3463 167 -24 294 C ATOM 2140 CG1 VAL A 743 47.489 -5.121 27.459 1.00 20.75 C ANISOU 2140 CG1 VAL A 743 2039 2391 3452 159 -115 330 C ATOM 2141 CG2 VAL A 743 47.080 -6.670 25.527 1.00 20.65 C ANISOU 2141 CG2 VAL A 743 2071 2335 3441 207 60 327 C ATOM 2142 N PRO A 744 44.277 -5.006 29.088 1.00 22.73 N ANISOU 2142 N PRO A 744 2471 2716 3449 126 -175 228 N ATOM 2143 CA PRO A 744 43.530 -4.013 29.879 1.00 22.10 C ANISOU 2143 CA PRO A 744 2432 2669 3297 106 -235 188 C ATOM 2144 C PRO A 744 44.102 -2.601 29.833 1.00 23.46 C ANISOU 2144 C PRO A 744 2572 2840 3502 84 -290 170 C ATOM 2145 O PRO A 744 43.336 -1.630 29.867 1.00 23.36 O ANISOU 2145 O PRO A 744 2595 2841 3437 66 -307 125 O ATOM 2146 CB PRO A 744 43.605 -4.578 31.298 1.00 23.17 C ANISOU 2146 CB PRO A 744 2581 2827 3394 123 -296 214 C ATOM 2147 CG PRO A 744 43.694 -6.041 31.105 1.00 22.54 C ANISOU 2147 CG PRO A 744 2495 2729 3338 146 -242 255 C ATOM 2148 CD PRO A 744 44.567 -6.217 29.880 1.00 22.17 C ANISOU 2148 CD PRO A 744 2397 2645 3384 151 -188 271 C ATOM 2149 N SER A 745 45.423 -2.477 29.719 1.00 25.09 N ANISOU 2149 N SER A 745 2707 3024 3800 85 -315 208 N ATOM 2150 CA SER A 745 46.050 -1.157 29.736 1.00 26.14 C ANISOU 2150 CA SER A 745 2801 3148 3982 61 -377 199 C ATOM 2151 C SER A 745 45.822 -0.395 28.428 1.00 27.77 C ANISOU 2151 C SER A 745 2999 3338 4213 44 -314 179 C ATOM 2152 O SER A 745 45.964 0.829 28.385 1.00 26.77 O ANISOU 2152 O SER A 745 2857 3205 4108 20 -358 159 O ATOM 2153 CB SER A 745 47.543 -1.278 30.020 1.00 27.17 C ANISOU 2153 CB SER A 745 2848 3257 4218 65 -427 255 C ATOM 2154 OG SER A 745 48.201 -2.069 29.044 1.00 27.43 O ANISOU 2154 OG SER A 745 2830 3264 4327 86 -342 301 O ATOM 2155 N GLN A 746 45.477 -1.119 27.367 1.00 28.83 N ANISOU 2155 N GLN A 746 3147 3464 4344 60 -214 183 N ATOM 2156 CA GLN A 746 45.216 -0.514 26.061 1.00 29.39 C ANISOU 2156 CA GLN A 746 3220 3521 4426 51 -147 167 C ATOM 2157 C GLN A 746 43.780 -0.025 25.928 1.00 26.83 C ANISOU 2157 C GLN A 746 2969 3217 4010 35 -138 109 C ATOM 2158 O GLN A 746 43.388 0.517 24.890 1.00 26.23 O ANISOU 2158 O GLN A 746 2906 3133 3929 27 -90 90 O ATOM 2159 CB GLN A 746 45.477 -1.503 24.941 1.00 31.40 C ANISOU 2159 CB GLN A 746 3467 3754 4709 81 -48 193 C ATOM 2160 CG GLN A 746 46.735 -2.266 25.071 1.00 33.32 C ANISOU 2160 CG GLN A 746 3645 3978 5036 106 -40 253 C ATOM 2161 CD GLN A 746 47.874 -1.517 24.505 1.00 35.27 C ANISOU 2161 CD GLN A 746 3813 4204 5383 104 -31 294 C ATOM 2162 OE1 GLN A 746 48.690 -0.982 25.244 1.00 37.88 O ANISOU 2162 OE1 GLN A 746 4084 4532 5778 88 -108 321 O ATOM 2163 NE2 GLN A 746 47.945 -1.454 23.177 1.00 36.30 N ANISOU 2163 NE2 GLN A 746 3942 4319 5531 120 62 301 N ATOM 2164 N ARG A 747 42.974 -0.265 26.952 1.00 24.36 N ANISOU 2164 N ARG A 747 2704 2929 3622 35 -180 85 N ATOM 2165 CA ARG A 747 41.627 0.251 26.921 1.00 22.60 C ANISOU 2165 CA ARG A 747 2542 2725 3319 21 -173 36 C ATOM 2166 C ARG A 747 41.667 1.712 27.327 1.00 22.06 C ANISOU 2166 C ARG A 747 2470 2662 3251 -1 -240 7 C ATOM 2167 O ARG A 747 42.602 2.140 28.009 1.00 23.15 O ANISOU 2167 O ARG A 747 2570 2793 3433 -5 -310 22 O ATOM 2168 CB ARG A 747 40.716 -0.547 27.842 1.00 22.00 C ANISOU 2168 CB ARG A 747 2517 2675 3168 34 -182 28 C ATOM 2169 CG ARG A 747 40.625 -1.997 27.479 1.00 21.79 C ANISOU 2169 CG ARG A 747 2496 2636 3148 53 -123 56 C ATOM 2170 CD ARG A 747 39.867 -2.757 28.526 1.00 21.64 C ANISOU 2170 CD ARG A 747 2514 2639 3068 64 -138 62 C ATOM 2171 NE ARG A 747 40.107 -4.167 28.326 1.00 21.93 N ANISOU 2171 NE ARG A 747 2543 2656 3132 83 -97 97 N ATOM 2172 CZ ARG A 747 40.013 -5.087 29.270 1.00 21.84 C ANISOU 2172 CZ ARG A 747 2543 2656 3102 100 -112 127 C ATOM 2173 NH1 ARG A 747 39.663 -4.744 30.500 1.00 21.58 N ANISOU 2173 NH1 ARG A 747 2532 2658 3012 103 -164 127 N ATOM 2174 NH2 ARG A 747 40.275 -6.352 28.972 1.00 22.11 N ANISOU 2174 NH2 ARG A 747 2568 2663 3172 117 -72 159 N ATOM 2175 N PRO A 748 40.662 2.486 26.888 1.00 21.61 N ANISOU 2175 N PRO A 748 2451 2611 3149 -15 -223 -33 N ATOM 2176 CA PRO A 748 40.553 3.878 27.342 1.00 20.94 C ANISOU 2176 CA PRO A 748 2372 2528 3057 -33 -287 -67 C ATOM 2177 C PRO A 748 40.057 3.928 28.773 1.00 20.82 C ANISOU 2177 C PRO A 748 2402 2540 2969 -22 -351 -91 C ATOM 2178 O PRO A 748 39.396 2.993 29.210 1.00 20.40 O ANISOU 2178 O PRO A 748 2384 2510 2859 -4 -325 -85 O ATOM 2179 CB PRO A 748 39.537 4.498 26.372 1.00 20.67 C ANISOU 2179 CB PRO A 748 2367 2492 2993 -45 -237 -98 C ATOM 2180 CG PRO A 748 38.779 3.331 25.784 1.00 20.16 C ANISOU 2180 CG PRO A 748 2332 2436 2893 -32 -163 -91 C ATOM 2181 CD PRO A 748 39.724 2.166 25.790 1.00 20.38 C ANISOU 2181 CD PRO A 748 2327 2453 2963 -14 -144 -48 C ATOM 2182 N THR A 749 40.399 4.990 29.490 1.00 21.29 N ANISOU 2182 N THR A 749 2462 2594 3033 -31 -433 -114 N ATOM 2183 CA THR A 749 39.854 5.237 30.818 1.00 21.77 C ANISOU 2183 CA THR A 749 2580 2682 3012 -14 -494 -146 C ATOM 2184 C THR A 749 38.504 5.903 30.655 1.00 21.32 C ANISOU 2184 C THR A 749 2575 2638 2887 -13 -463 -191 C ATOM 2185 O THR A 749 38.197 6.395 29.576 1.00 19.86 O ANISOU 2185 O THR A 749 2377 2437 2732 -32 -419 -199 O ATOM 2186 CB THR A 749 40.768 6.143 31.650 1.00 22.97 C ANISOU 2186 CB THR A 749 2720 2816 3193 -21 -605 -161 C ATOM 2187 OG1 THR A 749 40.749 7.473 31.093 1.00 21.35 O ANISOU 2187 OG1 THR A 749 2504 2583 3027 -46 -625 -192 O ATOM 2188 CG2 THR A 749 42.183 5.589 31.663 1.00 24.25 C ANISOU 2188 CG2 THR A 749 2813 2958 3444 -26 -638 -109 C ATOM 2189 N PHE A 750 37.694 5.940 31.703 1.00 22.43 N ANISOU 2189 N PHE A 750 2777 2808 2937 12 -483 -216 N ATOM 2190 CA PHE A 750 36.417 6.631 31.581 1.00 22.94 C ANISOU 2190 CA PHE A 750 2886 2885 2945 16 -453 -255 C ATOM 2191 C PHE A 750 36.598 8.122 31.272 1.00 23.91 C ANISOU 2191 C PHE A 750 3004 2978 3102 -4 -498 -295 C ATOM 2192 O PHE A 750 35.812 8.708 30.515 1.00 23.74 O ANISOU 2192 O PHE A 750 2990 2951 3080 -14 -456 -315 O ATOM 2193 CB PHE A 750 35.585 6.434 32.839 1.00 21.76 C ANISOU 2193 CB PHE A 750 2801 2773 2693 54 -463 -269 C ATOM 2194 CG PHE A 750 35.014 5.071 32.945 1.00 20.45 C ANISOU 2194 CG PHE A 750 2641 2634 2495 71 -398 -228 C ATOM 2195 CD1 PHE A 750 34.074 4.634 32.023 1.00 19.89 C ANISOU 2195 CD1 PHE A 750 2562 2564 2432 60 -317 -217 C ATOM 2196 CD2 PHE A 750 35.433 4.202 33.944 1.00 19.24 C ANISOU 2196 CD2 PHE A 750 2500 2502 2310 96 -422 -197 C ATOM 2197 CE1 PHE A 750 33.545 3.355 32.105 1.00 16.60 C ANISOU 2197 CE1 PHE A 750 2147 2163 1997 71 -263 -177 C ATOM 2198 CE2 PHE A 750 34.898 2.930 34.034 1.00 18.19 C ANISOU 2198 CE2 PHE A 750 2368 2387 2155 110 -361 -154 C ATOM 2199 CZ PHE A 750 33.957 2.502 33.107 1.00 17.12 C ANISOU 2199 CZ PHE A 750 2222 2247 2035 96 -282 -144 C ATOM 2200 N LYS A 751 37.641 8.721 31.831 1.00 25.68 N ANISOU 2200 N LYS A 751 3215 3181 3363 -10 -588 -304 N ATOM 2201 CA LYS A 751 37.999 10.095 31.491 1.00 27.18 C ANISOU 2201 CA LYS A 751 3388 3331 3607 -35 -638 -335 C ATOM 2202 C LYS A 751 38.154 10.300 29.972 1.00 26.27 C ANISOU 2202 C LYS A 751 3217 3191 3574 -66 -576 -310 C ATOM 2203 O LYS A 751 37.583 11.230 29.398 1.00 25.86 O ANISOU 2203 O LYS A 751 3174 3125 3528 -78 -560 -335 O ATOM 2204 CB LYS A 751 39.284 10.491 32.209 1.00 29.59 C ANISOU 2204 CB LYS A 751 3670 3608 3964 -44 -748 -335 C ATOM 2205 CG LYS A 751 39.680 11.927 32.006 1.00 31.83 C ANISOU 2205 CG LYS A 751 3938 3844 4311 -70 -815 -366 C ATOM 2206 CD LYS A 751 39.775 12.663 33.324 1.00 34.33 C ANISOU 2206 CD LYS A 751 4314 4151 4579 -52 -929 -419 C ATOM 2207 CE LYS A 751 40.514 13.982 33.144 1.00 35.71 C ANISOU 2207 CE LYS A 751 4456 4263 4847 -86 -1017 -440 C ATOM 2208 NZ LYS A 751 41.803 13.777 32.408 1.00 36.39 N ANISOU 2208 NZ LYS A 751 4440 4318 5070 -124 -1026 -378 N ATOM 2209 N GLN A 752 38.910 9.421 29.322 1.00 25.45 N ANISOU 2209 N GLN A 752 3058 3082 3530 -76 -536 -259 N ATOM 2210 CA GLN A 752 39.075 9.493 27.874 1.00 24.87 C ANISOU 2210 CA GLN A 752 2939 2989 3521 -96 -468 -231 C ATOM 2211 C GLN A 752 37.772 9.215 27.127 1.00 24.11 C ANISOU 2211 C GLN A 752 2881 2914 3367 -89 -384 -243 C ATOM 2212 O GLN A 752 37.506 9.816 26.085 1.00 23.98 O ANISOU 2212 O GLN A 752 2853 2881 3376 -104 -347 -244 O ATOM 2213 CB GLN A 752 40.158 8.528 27.423 1.00 24.71 C ANISOU 2213 CB GLN A 752 2860 2960 3568 -97 -439 -174 C ATOM 2214 CG GLN A 752 41.564 9.026 27.691 1.00 25.90 C ANISOU 2214 CG GLN A 752 2948 3078 3815 -113 -512 -148 C ATOM 2215 CD GLN A 752 42.544 7.881 27.796 1.00 26.79 C ANISOU 2215 CD GLN A 752 3014 3192 3972 -102 -501 -95 C ATOM 2216 OE1 GLN A 752 42.144 6.740 28.000 1.00 26.70 O ANISOU 2216 OE1 GLN A 752 3030 3208 3906 -79 -460 -88 O ATOM 2217 NE2 GLN A 752 43.830 8.172 27.657 1.00 27.90 N ANISOU 2217 NE2 GLN A 752 3079 3300 4221 -117 -539 -55 N ATOM 2218 N LEU A 753 36.956 8.309 27.655 1.00 23.69 N ANISOU 2218 N LEU A 753 2869 2893 3239 -67 -357 -248 N ATOM 2219 CA LEU A 753 35.651 8.073 27.062 1.00 22.85 C ANISOU 2219 CA LEU A 753 2796 2804 3084 -63 -291 -259 C ATOM 2220 C LEU A 753 34.821 9.357 27.089 1.00 23.17 C ANISOU 2220 C LEU A 753 2865 2840 3098 -67 -309 -302 C ATOM 2221 O LEU A 753 34.232 9.742 26.088 1.00 21.70 O ANISOU 2221 O LEU A 753 2678 2645 2921 -79 -267 -306 O ATOM 2222 CB LEU A 753 34.930 6.941 27.781 1.00 22.32 C ANISOU 2222 CB LEU A 753 2761 2768 2950 -40 -267 -252 C ATOM 2223 CG LEU A 753 35.523 5.575 27.406 1.00 22.80 C ANISOU 2223 CG LEU A 753 2795 2826 3040 -37 -230 -209 C ATOM 2224 CD1 LEU A 753 34.856 4.433 28.201 1.00 22.59 C ANISOU 2224 CD1 LEU A 753 2798 2827 2957 -15 -211 -194 C ATOM 2225 CD2 LEU A 753 35.435 5.343 25.894 1.00 21.49 C ANISOU 2225 CD2 LEU A 753 2613 2641 2912 -51 -166 -197 C ATOM 2226 N VAL A 754 34.802 10.036 28.228 1.00 25.43 N ANISOU 2226 N VAL A 754 3179 3130 3352 -55 -373 -334 N ATOM 2227 CA VAL A 754 34.018 11.251 28.350 1.00 26.66 C ANISOU 2227 CA VAL A 754 3369 3280 3483 -52 -391 -377 C ATOM 2228 C VAL A 754 34.454 12.289 27.319 1.00 29.39 C ANISOU 2228 C VAL A 754 3677 3585 3903 -82 -398 -378 C ATOM 2229 O VAL A 754 33.626 12.779 26.546 1.00 28.57 O ANISOU 2229 O VAL A 754 3582 3478 3796 -88 -358 -387 O ATOM 2230 CB VAL A 754 34.110 11.824 29.761 1.00 25.64 C ANISOU 2230 CB VAL A 754 3282 3154 3307 -28 -467 -415 C ATOM 2231 CG1 VAL A 754 33.552 13.217 29.798 1.00 24.43 C ANISOU 2231 CG1 VAL A 754 3157 2981 3146 -26 -494 -462 C ATOM 2232 CG2 VAL A 754 33.344 10.931 30.715 1.00 25.90 C ANISOU 2232 CG2 VAL A 754 3359 3231 3249 9 -442 -412 C ATOM 2233 N GLU A 755 35.748 12.589 27.270 1.00 32.59 N ANISOU 2233 N GLU A 755 4039 3961 4383 -101 -446 -361 N ATOM 2234 CA GLU A 755 36.258 13.580 26.319 1.00 36.03 C ANISOU 2234 CA GLU A 755 4432 4356 4900 -129 -450 -351 C ATOM 2235 C GLU A 755 35.882 13.274 24.869 1.00 35.09 C ANISOU 2235 C GLU A 755 4296 4241 4798 -139 -362 -320 C ATOM 2236 O GLU A 755 35.505 14.174 24.119 1.00 35.70 O ANISOU 2236 O GLU A 755 4370 4299 4894 -151 -348 -326 O ATOM 2237 CB GLU A 755 37.783 13.706 26.453 1.00 40.04 C ANISOU 2237 CB GLU A 755 4881 4832 5498 -148 -506 -321 C ATOM 2238 CG GLU A 755 38.220 14.287 27.790 1.00 43.67 C ANISOU 2238 CG GLU A 755 5362 5277 5955 -144 -615 -357 C ATOM 2239 CD GLU A 755 39.660 13.957 28.146 1.00 46.92 C ANISOU 2239 CD GLU A 755 5717 5668 6442 -157 -672 -321 C ATOM 2240 OE1 GLU A 755 40.180 14.549 29.127 1.00 49.94 O ANISOU 2240 OE1 GLU A 755 6109 6027 6839 -160 -777 -348 O ATOM 2241 OE2 GLU A 755 40.264 13.102 27.454 1.00 50.33 O ANISOU 2241 OE2 GLU A 755 6097 6105 6920 -162 -617 -266 O ATOM 2242 N ASP A 756 35.961 12.007 24.482 1.00 34.64 N ANISOU 2242 N ASP A 756 4231 4205 4727 -130 -306 -289 N ATOM 2243 CA ASP A 756 35.766 11.640 23.091 1.00 34.74 C ANISOU 2243 CA ASP A 756 4232 4216 4752 -135 -230 -261 C ATOM 2244 C ASP A 756 34.268 11.634 22.745 1.00 32.71 C ANISOU 2244 C ASP A 756 4022 3978 4427 -128 -193 -287 C ATOM 2245 O ASP A 756 33.864 11.981 21.621 1.00 31.08 O ANISOU 2245 O ASP A 756 3817 3763 4229 -136 -153 -279 O ATOM 2246 CB ASP A 756 36.397 10.277 22.818 1.00 37.90 C ANISOU 2246 CB ASP A 756 4613 4626 5163 -124 -188 -223 C ATOM 2247 CG ASP A 756 37.075 10.201 21.453 1.00 41.64 C ANISOU 2247 CG ASP A 756 5051 5080 5691 -128 -130 -182 C ATOM 2248 OD1 ASP A 756 37.897 11.094 21.135 1.00 46.18 O ANISOU 2248 OD1 ASP A 756 5582 5628 6336 -142 -147 -161 O ATOM 2249 OD2 ASP A 756 36.787 9.254 20.688 1.00 44.68 O ANISOU 2249 OD2 ASP A 756 5454 5474 6049 -115 -68 -169 O ATOM 2250 N LEU A 757 33.443 11.275 23.727 1.00 30.49 N ANISOU 2250 N LEU A 757 3779 3723 4084 -112 -207 -313 N ATOM 2251 CA LEU A 757 31.999 11.255 23.541 1.00 28.50 C ANISOU 2251 CA LEU A 757 3562 3488 3777 -105 -176 -331 C ATOM 2252 C LEU A 757 31.410 12.672 23.560 1.00 29.00 C ANISOU 2252 C LEU A 757 3640 3539 3841 -108 -201 -362 C ATOM 2253 O LEU A 757 30.451 12.967 22.858 1.00 29.40 O ANISOU 2253 O LEU A 757 3703 3590 3878 -111 -171 -367 O ATOM 2254 CB LEU A 757 31.350 10.378 24.611 1.00 24.75 C ANISOU 2254 CB LEU A 757 3116 3045 3242 -83 -174 -337 C ATOM 2255 CG LEU A 757 31.495 8.872 24.376 1.00 21.32 C ANISOU 2255 CG LEU A 757 2675 2621 2804 -79 -135 -306 C ATOM 2256 CD1 LEU A 757 31.054 8.060 25.590 1.00 20.20 C ANISOU 2256 CD1 LEU A 757 2555 2508 2612 -57 -140 -303 C ATOM 2257 CD2 LEU A 757 30.703 8.477 23.144 1.00 19.46 C ANISOU 2257 CD2 LEU A 757 2446 2381 2566 -89 -85 -297 C ATOM 2258 N ASP A 758 31.987 13.540 24.375 1.00 31.90 N ANISOU 2258 N ASP A 758 4006 3891 4226 -107 -261 -384 N ATOM 2259 CA ASP A 758 31.647 14.954 24.363 1.00 34.23 C ANISOU 2259 CA ASP A 758 4310 4161 4535 -111 -292 -414 C ATOM 2260 C ASP A 758 31.866 15.523 22.959 1.00 34.21 C ANISOU 2260 C ASP A 758 4276 4132 4590 -136 -264 -389 C ATOM 2261 O ASP A 758 31.001 16.200 22.394 1.00 32.54 O ANISOU 2261 O ASP A 758 4078 3915 4372 -137 -247 -399 O ATOM 2262 CB ASP A 758 32.494 15.700 25.402 1.00 38.39 C ANISOU 2262 CB ASP A 758 4838 4664 5083 -110 -373 -440 C ATOM 2263 CG ASP A 758 32.123 17.160 25.529 1.00 42.33 C ANISOU 2263 CG ASP A 758 5355 5132 5596 -110 -413 -478 C ATOM 2264 OD1 ASP A 758 31.198 17.471 26.305 1.00 47.46 O ANISOU 2264 OD1 ASP A 758 6053 5795 6184 -82 -421 -517 O ATOM 2265 OD2 ASP A 758 32.765 18.007 24.872 1.00 44.94 O ANISOU 2265 OD2 ASP A 758 5651 5423 6002 -136 -433 -466 O ATOM 2266 N ARG A 759 33.031 15.231 22.399 1.00 33.77 N ANISOU 2266 N ARG A 759 4178 4061 4591 -151 -257 -352 N ATOM 2267 CA ARG A 759 33.361 15.673 21.065 1.00 33.52 C ANISOU 2267 CA ARG A 759 4118 4007 4611 -168 -222 -318 C ATOM 2268 C ARG A 759 32.370 15.144 20.037 1.00 30.16 C ANISOU 2268 C ARG A 759 3717 3602 4141 -162 -158 -309 C ATOM 2269 O ARG A 759 31.889 15.886 19.189 1.00 31.07 O ANISOU 2269 O ARG A 759 3836 3704 4264 -168 -141 -305 O ATOM 2270 CB ARG A 759 34.766 15.225 20.702 1.00 34.92 C ANISOU 2270 CB ARG A 759 4245 4171 4851 -177 -212 -273 C ATOM 2271 CG ARG A 759 35.394 16.032 19.607 1.00 36.56 C ANISOU 2271 CG ARG A 759 4413 4347 5131 -193 -191 -233 C ATOM 2272 CD ARG A 759 36.673 15.376 19.099 1.00 38.47 C ANISOU 2272 CD ARG A 759 4605 4581 5429 -193 -157 -178 C ATOM 2273 NE ARG A 759 36.344 14.375 18.093 1.00 39.98 N ANISOU 2273 NE ARG A 759 4818 4796 5575 -174 -78 -158 N ATOM 2274 CZ ARG A 759 36.336 13.063 18.302 1.00 40.90 C ANISOU 2274 CZ ARG A 759 4951 4937 5651 -158 -53 -159 C ATOM 2275 NH1 ARG A 759 36.003 12.248 17.314 1.00 41.73 N ANISOU 2275 NH1 ARG A 759 5084 5055 5717 -141 12 -146 N ATOM 2276 NH2 ARG A 759 36.672 12.558 19.483 1.00 42.06 N ANISOU 2276 NH2 ARG A 759 5091 5092 5797 -156 -98 -173 N ATOM 2277 N ILE A 760 32.078 13.852 20.100 1.00 27.19 N ANISOU 2277 N ILE A 760 3357 3253 3720 -150 -126 -304 N ATOM 2278 CA ILE A 760 31.197 13.231 19.117 1.00 23.94 C ANISOU 2278 CA ILE A 760 2970 2855 3271 -146 -76 -297 C ATOM 2279 C ILE A 760 29.771 13.752 19.254 1.00 22.99 C ANISOU 2279 C ILE A 760 2879 2743 3112 -143 -84 -325 C ATOM 2280 O ILE A 760 29.112 14.007 18.244 1.00 22.93 O ANISOU 2280 O ILE A 760 2883 2731 3097 -147 -61 -319 O ATOM 2281 CB ILE A 760 31.216 11.670 19.231 1.00 18.60 C ANISOU 2281 CB ILE A 760 2305 2198 2564 -134 -48 -287 C ATOM 2282 CG1 ILE A 760 32.571 11.133 18.771 1.00 18.68 C ANISOU 2282 CG1 ILE A 760 2286 2197 2616 -132 -25 -252 C ATOM 2283 CG2 ILE A 760 30.149 11.049 18.388 1.00 18.26 C ANISOU 2283 CG2 ILE A 760 2293 2163 2482 -132 -14 -288 C ATOM 2284 CD1 ILE A 760 32.898 9.720 19.252 1.00 18.66 C ANISOU 2284 CD1 ILE A 760 2285 2207 2599 -120 -13 -243 C ATOM 2285 N LEU A 761 29.308 13.927 20.490 1.00 21.93 N ANISOU 2285 N LEU A 761 2758 2621 2953 -132 -115 -354 N ATOM 2286 CA LEU A 761 27.963 14.441 20.734 1.00 21.44 C ANISOU 2286 CA LEU A 761 2719 2568 2859 -123 -117 -377 C ATOM 2287 C LEU A 761 27.753 15.836 20.141 1.00 20.55 C ANISOU 2287 C LEU A 761 2602 2430 2777 -131 -130 -384 C ATOM 2288 O LEU A 761 26.755 16.069 19.442 1.00 19.54 O ANISOU 2288 O LEU A 761 2483 2302 2637 -132 -111 -381 O ATOM 2289 CB LEU A 761 27.662 14.465 22.233 1.00 20.41 C ANISOU 2289 CB LEU A 761 2606 2455 2694 -101 -144 -404 C ATOM 2290 CG LEU A 761 26.273 14.955 22.651 1.00 19.22 C ANISOU 2290 CG LEU A 761 2478 2316 2510 -82 -137 -424 C ATOM 2291 CD1 LEU A 761 25.217 14.245 21.837 1.00 13.76 C ANISOU 2291 CD1 LEU A 761 1784 1637 1806 -88 -96 -402 C ATOM 2292 CD2 LEU A 761 26.048 14.696 24.125 1.00 14.30 C ANISOU 2292 CD2 LEU A 761 1878 1716 1840 -52 -149 -443 C ATOM 2293 N THR A 762 28.695 16.742 20.424 1.00 21.66 N ANISOU 2293 N THR A 762 2726 2544 2961 -139 -166 -390 N ATOM 2294 CA THR A 762 28.716 18.110 19.903 1.00 21.90 C ANISOU 2294 CA THR A 762 2746 2539 3034 -149 -184 -392 C ATOM 2295 C THR A 762 28.737 18.200 18.383 1.00 24.27 C ANISOU 2295 C THR A 762 3034 2830 3356 -163 -145 -354 C ATOM 2296 O THR A 762 27.964 18.957 17.791 1.00 25.21 O ANISOU 2296 O THR A 762 3161 2939 3477 -164 -139 -355 O ATOM 2297 CB THR A 762 29.933 18.858 20.421 1.00 21.76 C ANISOU 2297 CB THR A 762 2705 2489 3073 -160 -234 -397 C ATOM 2298 OG1 THR A 762 29.893 18.870 21.846 1.00 21.56 O ANISOU 2298 OG1 THR A 762 2703 2471 3019 -143 -279 -438 O ATOM 2299 CG2 THR A 762 29.963 20.292 19.903 1.00 21.25 C ANISOU 2299 CG2 THR A 762 2627 2382 3063 -173 -254 -396 C ATOM 2300 N LEU A 763 29.649 17.456 17.756 1.00 26.11 N ANISOU 2300 N LEU A 763 3250 3067 3605 -170 -116 -320 N ATOM 2301 CA LEU A 763 29.666 17.312 16.301 1.00 27.91 C ANISOU 2301 CA LEU A 763 3478 3292 3834 -173 -71 -284 C ATOM 2302 C LEU A 763 28.311 16.859 15.723 1.00 29.17 C ANISOU 2302 C LEU A 763 3674 3472 3938 -166 -49 -292 C ATOM 2303 O LEU A 763 27.804 17.429 14.759 1.00 29.13 O ANISOU 2303 O LEU A 763 3678 3458 3931 -168 -38 -279 O ATOM 2304 CB LEU A 763 30.739 16.321 15.900 1.00 29.70 C ANISOU 2304 CB LEU A 763 3690 3524 4071 -171 -37 -252 C ATOM 2305 CG LEU A 763 32.092 16.951 15.643 1.00 32.12 C ANISOU 2305 CG LEU A 763 3951 3803 4451 -180 -37 -215 C ATOM 2306 CD1 LEU A 763 33.135 15.871 15.363 1.00 32.67 C ANISOU 2306 CD1 LEU A 763 4002 3880 4531 -171 2 -182 C ATOM 2307 CD2 LEU A 763 31.964 17.922 14.473 1.00 32.58 C ANISOU 2307 CD2 LEU A 763 4006 3842 4532 -185 -14 -185 C ATOM 2308 N THR A 764 27.736 15.821 16.313 1.00 29.43 N ANISOU 2308 N THR A 764 3724 3530 3929 -158 -48 -310 N ATOM 2309 CA THR A 764 26.443 15.326 15.879 1.00 29.73 C ANISOU 2309 CA THR A 764 3788 3582 3926 -154 -36 -316 C ATOM 2310 C THR A 764 25.348 16.361 16.084 1.00 29.74 C ANISOU 2310 C THR A 764 3792 3580 3929 -153 -57 -332 C ATOM 2311 O THR A 764 24.465 16.523 15.244 1.00 31.36 O ANISOU 2311 O THR A 764 4010 3783 4123 -155 -52 -324 O ATOM 2312 CB THR A 764 26.033 14.079 16.636 1.00 30.44 C ANISOU 2312 CB THR A 764 3887 3695 3985 -148 -33 -327 C ATOM 2313 OG1 THR A 764 27.158 13.199 16.763 1.00 31.13 O ANISOU 2313 OG1 THR A 764 3966 3784 4077 -146 -20 -315 O ATOM 2314 CG2 THR A 764 24.925 13.409 15.895 1.00 30.54 C ANISOU 2314 CG2 THR A 764 3921 3714 3969 -150 -23 -322 C ATOM 2315 N THR A 765 25.397 17.044 17.220 1.00 29.34 N ANISOU 2315 N THR A 765 3732 3525 3890 -146 -83 -356 N ATOM 2316 CA THR A 765 24.365 18.006 17.551 1.00 29.56 C ANISOU 2316 CA THR A 765 3765 3546 3919 -136 -99 -375 C ATOM 2317 C THR A 765 24.443 19.196 16.592 1.00 29.43 C ANISOU 2317 C THR A 765 3742 3501 3938 -146 -105 -361 C ATOM 2318 O THR A 765 23.431 19.598 16.013 1.00 29.21 O ANISOU 2318 O THR A 765 3721 3472 3907 -143 -101 -355 O ATOM 2319 CB THR A 765 24.481 18.443 19.025 1.00 29.39 C ANISOU 2319 CB THR A 765 3747 3526 3894 -119 -125 -409 C ATOM 2320 OG1 THR A 765 24.040 17.359 19.850 1.00 29.18 O ANISOU 2320 OG1 THR A 765 3731 3531 3826 -104 -112 -414 O ATOM 2321 CG2 THR A 765 23.606 19.630 19.313 1.00 29.17 C ANISOU 2321 CG2 THR A 765 3727 3483 3874 -103 -139 -430 C ATOM 2322 N ASN A 766 25.642 19.719 16.375 1.00 29.96 N ANISOU 2322 N ASN A 766 3793 3545 4047 -157 -113 -348 N ATOM 2323 CA ASN A 766 25.819 20.856 15.479 1.00 29.67 C ANISOU 2323 CA ASN A 766 3745 3478 4051 -166 -115 -326 C ATOM 2324 C ASN A 766 25.616 20.557 14.009 1.00 30.79 C ANISOU 2324 C ASN A 766 3897 3625 4177 -171 -82 -288 C ATOM 2325 O ASN A 766 25.521 21.480 13.206 1.00 30.13 O ANISOU 2325 O ASN A 766 3810 3521 4118 -174 -81 -265 O ATOM 2326 CB ASN A 766 27.205 21.448 15.649 1.00 28.80 C ANISOU 2326 CB ASN A 766 3606 3337 3999 -179 -132 -314 C ATOM 2327 CG ASN A 766 27.444 21.960 17.043 1.00 27.46 C ANISOU 2327 CG ASN A 766 3435 3152 3848 -175 -180 -356 C ATOM 2328 OD1 ASN A 766 26.500 22.248 17.781 1.00 26.35 O ANISOU 2328 OD1 ASN A 766 3316 3016 3679 -157 -196 -393 O ATOM 2329 ND2 ASN A 766 28.708 22.070 17.420 1.00 27.66 N ANISOU 2329 ND2 ASN A 766 3434 3156 3919 -187 -204 -349 N ATOM 2330 N GLU A 767 25.568 19.287 13.634 1.00 32.27 N ANISOU 2330 N GLU A 767 4101 3838 4322 -168 -57 -281 N ATOM 2331 CA GLU A 767 25.446 18.960 12.217 1.00 34.81 C ANISOU 2331 CA GLU A 767 4443 4163 4618 -167 -30 -249 C ATOM 2332 C GLU A 767 24.079 18.413 11.809 1.00 33.69 C ANISOU 2332 C GLU A 767 4330 4037 4432 -163 -37 -259 C ATOM 2333 O GLU A 767 23.872 18.086 10.652 1.00 33.61 O ANISOU 2333 O GLU A 767 4347 4029 4393 -160 -25 -239 O ATOM 2334 CB GLU A 767 26.546 17.978 11.819 1.00 37.97 C ANISOU 2334 CB GLU A 767 4847 4571 5009 -163 4 -230 C ATOM 2335 CG GLU A 767 27.915 18.646 11.744 1.00 42.24 C ANISOU 2335 CG GLU A 767 5353 5090 5604 -168 17 -200 C ATOM 2336 CD GLU A 767 29.070 17.658 11.670 1.00 47.71 C ANISOU 2336 CD GLU A 767 6037 5790 6299 -161 51 -181 C ATOM 2337 OE1 GLU A 767 28.805 16.436 11.546 1.00 52.33 O ANISOU 2337 OE1 GLU A 767 6651 6395 6835 -151 66 -193 O ATOM 2338 OE2 GLU A 767 30.240 18.107 11.748 1.00 48.13 O ANISOU 2338 OE2 GLU A 767 6052 5825 6408 -165 60 -153 O ATOM 2339 N GLU A 768 23.155 18.318 12.756 1.00 32.86 N ANISOU 2339 N GLU A 768 4218 3942 4323 -161 -57 -286 N ATOM 2340 CA GLU A 768 21.776 17.944 12.462 1.00 32.50 C ANISOU 2340 CA GLU A 768 4186 3907 4255 -160 -69 -289 C ATOM 2341 C GLU A 768 21.036 18.991 11.638 1.00 29.49 C ANISOU 2341 C GLU A 768 3807 3511 3885 -160 -84 -273 C ATOM 2342 O GLU A 768 20.949 20.165 12.019 1.00 29.57 O ANISOU 2342 O GLU A 768 3800 3506 3930 -156 -94 -277 O ATOM 2343 CB GLU A 768 20.988 17.709 13.751 1.00 34.92 C ANISOU 2343 CB GLU A 768 4477 4228 4564 -153 -79 -312 C ATOM 2344 CG GLU A 768 21.197 16.356 14.383 1.00 37.49 C ANISOU 2344 CG GLU A 768 4805 4571 4867 -153 -68 -320 C ATOM 2345 CD GLU A 768 20.328 16.132 15.618 1.00 40.80 C ANISOU 2345 CD GLU A 768 5210 5008 5286 -141 -70 -333 C ATOM 2346 OE1 GLU A 768 19.776 17.119 16.171 1.00 42.41 O ANISOU 2346 OE1 GLU A 768 5401 5207 5504 -128 -76 -343 O ATOM 2347 OE2 GLU A 768 20.206 14.958 16.039 1.00 45.44 O ANISOU 2347 OE2 GLU A 768 5797 5610 5858 -142 -61 -331 O HETATM 2348 N PTR A 769 20.496 18.548 10.510 1.00 26.62 N ANISOU 2348 N PTR A 769 3470 3150 3494 -163 -90 -256 N HETATM 2349 CA PTR A 769 19.551 19.342 9.753 1.00 24.80 C ANISOU 2349 CA PTR A 769 3243 2909 3270 -162 -112 -239 C HETATM 2350 C PTR A 769 18.331 18.465 9.526 1.00 25.74 C ANISOU 2350 C PTR A 769 3371 3037 3370 -166 -138 -242 C HETATM 2351 O PTR A 769 18.454 17.292 9.212 1.00 24.24 O ANISOU 2351 O PTR A 769 3206 2855 3149 -171 -139 -247 O HETATM 2352 CB PTR A 769 20.098 19.814 8.407 1.00 23.49 C ANISOU 2352 CB PTR A 769 3105 2732 3089 -159 -103 -208 C HETATM 2353 CG PTR A 769 21.102 20.948 8.459 1.00 23.56 C ANISOU 2353 CG PTR A 769 3094 2723 3135 -157 -83 -191 C HETATM 2354 CD1 PTR A 769 22.468 20.686 8.516 1.00 23.18 C ANISOU 2354 CD1 PTR A 769 3043 2674 3091 -157 -51 -183 C HETATM 2355 CD2 PTR A 769 20.694 22.278 8.416 1.00 23.80 C ANISOU 2355 CD2 PTR A 769 3107 2733 3205 -156 -98 -179 C HETATM 2356 CE1 PTR A 769 23.393 21.711 8.544 1.00 23.37 C ANISOU 2356 CE1 PTR A 769 3042 2676 3163 -159 -37 -161 C HETATM 2357 CE2 PTR A 769 21.620 23.312 8.441 1.00 24.19 C ANISOU 2357 CE2 PTR A 769 3136 2758 3298 -157 -85 -161 C HETATM 2358 CZ PTR A 769 22.970 23.019 8.519 1.00 23.37 C ANISOU 2358 CZ PTR A 769 3024 2652 3203 -161 -57 -151 C HETATM 2359 OH PTR A 769 23.885 23.946 8.524 1.00 22.87 O ANISOU 2359 OH PTR A 769 2935 2561 3192 -166 -48 -128 O HETATM 2360 P PTR A 769 24.180 25.055 9.653 1.00 22.19 P ANISOU 2360 P PTR A 769 2810 2441 3179 -175 -76 -149 P HETATM 2361 O1P PTR A 769 24.370 26.393 8.911 1.00 22.09 O ANISOU 2361 O1P PTR A 769 2783 2391 3218 -178 -76 -105 O HETATM 2362 O2P PTR A 769 25.429 24.677 10.356 1.00 21.20 O ANISOU 2362 O2P PTR A 769 2663 2313 3080 -183 -69 -157 O HETATM 2363 O3P PTR A 769 23.066 25.170 10.697 1.00 21.68 O ANISOU 2363 O3P PTR A 769 2747 2380 3110 -168 -109 -200 O ATOM 2364 N LEU A 770 17.152 19.035 9.693 1.00 27.79 N ANISOU 2364 N LEU A 770 3609 3293 3656 -165 -162 -238 N ATOM 2365 CA LEU A 770 15.922 18.313 9.450 1.00 29.99 C ANISOU 2365 CA LEU A 770 3885 3575 3933 -172 -193 -232 C ATOM 2366 C LEU A 770 15.785 18.037 7.964 1.00 33.00 C ANISOU 2366 C LEU A 770 4311 3949 4280 -178 -222 -216 C ATOM 2367 O LEU A 770 16.018 18.929 7.161 1.00 34.35 O ANISOU 2367 O LEU A 770 4498 4110 4443 -171 -224 -198 O ATOM 2368 CB LEU A 770 14.739 19.127 9.963 1.00 27.95 C ANISOU 2368 CB LEU A 770 3586 3313 3720 -164 -207 -224 C ATOM 2369 CG LEU A 770 13.354 18.510 9.863 1.00 26.51 C ANISOU 2369 CG LEU A 770 3383 3132 3559 -172 -240 -210 C ATOM 2370 CD1 LEU A 770 13.341 17.164 10.583 1.00 25.52 C ANISOU 2370 CD1 LEU A 770 3250 3020 3428 -180 -230 -220 C ATOM 2371 CD2 LEU A 770 12.341 19.474 10.463 1.00 26.08 C ANISOU 2371 CD2 LEU A 770 3282 3074 3554 -156 -239 -198 C ATOM 2372 N ASP A 771 15.432 16.810 7.590 1.00 37.20 N ANISOU 2372 N ASP A 771 4866 4481 4789 -188 -247 -222 N ATOM 2373 CA ASP A 771 15.225 16.484 6.177 1.00 41.55 C ANISOU 2373 CA ASP A 771 5470 5022 5297 -190 -284 -212 C ATOM 2374 C ASP A 771 13.730 16.402 5.798 1.00 43.46 C ANISOU 2374 C ASP A 771 5698 5252 5564 -202 -349 -199 C ATOM 2375 O ASP A 771 13.023 15.462 6.178 1.00 42.40 O ANISOU 2375 O ASP A 771 5546 5114 5452 -217 -376 -205 O ATOM 2376 CB ASP A 771 15.933 15.175 5.832 1.00 45.99 C ANISOU 2376 CB ASP A 771 6080 5583 5812 -190 -277 -231 C ATOM 2377 CG ASP A 771 15.785 14.796 4.362 1.00 51.87 C ANISOU 2377 CG ASP A 771 6896 6315 6499 -184 -316 -229 C ATOM 2378 OD1 ASP A 771 15.604 15.704 3.517 1.00 53.13 O ANISOU 2378 OD1 ASP A 771 7075 6472 6642 -174 -331 -208 O ATOM 2379 OD2 ASP A 771 15.859 13.585 4.049 1.00 58.01 O ANISOU 2379 OD2 ASP A 771 7714 7082 7246 -186 -334 -249 O ATOM 2380 N LEU A 772 13.259 17.391 5.040 1.00 44.39 N ANISOU 2380 N LEU A 772 5820 5362 5683 -196 -375 -177 N ATOM 2381 CA LEU A 772 11.851 17.463 4.653 1.00 45.83 C ANISOU 2381 CA LEU A 772 5984 5532 5898 -207 -440 -158 C ATOM 2382 C LEU A 772 11.563 16.751 3.332 1.00 49.42 C ANISOU 2382 C LEU A 772 6503 5972 6301 -213 -505 -159 C ATOM 2383 O LEU A 772 10.489 16.914 2.761 1.00 49.61 O ANISOU 2383 O LEU A 772 6521 5983 6345 -221 -571 -140 O ATOM 2384 CB LEU A 772 11.404 18.920 4.541 1.00 43.63 C ANISOU 2384 CB LEU A 772 5674 5250 5653 -196 -442 -131 C ATOM 2385 CG LEU A 772 11.565 19.812 5.773 1.00 41.59 C ANISOU 2385 CG LEU A 772 5359 4998 5444 -185 -388 -133 C ATOM 2386 CD1 LEU A 772 11.357 21.245 5.375 1.00 41.00 C ANISOU 2386 CD1 LEU A 772 5274 4912 5391 -171 -392 -108 C ATOM 2387 CD2 LEU A 772 10.605 19.425 6.889 1.00 40.87 C ANISOU 2387 CD2 LEU A 772 5207 4911 5411 -189 -388 -134 C ATOM 2388 N SER A 773 12.528 15.996 2.822 1.00 53.04 N ANISOU 2388 N SER A 773 7027 6432 6693 -205 -488 -180 N ATOM 2389 CA SER A 773 12.259 15.130 1.690 1.00 57.53 C ANISOU 2389 CA SER A 773 7668 6984 7208 -207 -552 -192 C ATOM 2390 C SER A 773 11.324 14.037 2.177 1.00 61.58 C ANISOU 2390 C SER A 773 8149 7478 7769 -235 -605 -204 C ATOM 2391 O SER A 773 10.436 13.582 1.449 1.00 63.31 O ANISOU 2391 O SER A 773 8392 7674 7988 -248 -690 -203 O ATOM 2392 CB SER A 773 13.547 14.544 1.121 1.00 57.29 C ANISOU 2392 CB SER A 773 7715 6958 7096 -184 -510 -213 C ATOM 2393 OG SER A 773 14.365 15.561 0.572 1.00 57.04 O ANISOU 2393 OG SER A 773 7708 6939 7025 -158 -461 -191 O ATOM 2394 N GLN A 774 11.522 13.637 3.430 1.00 65.58 N ANISOU 2394 N GLN A 774 8601 7996 8323 -244 -558 -211 N ATOM 2395 CA GLN A 774 10.615 12.714 4.091 1.00 69.11 C ANISOU 2395 CA GLN A 774 8999 8427 8832 -270 -594 -210 C ATOM 2396 C GLN A 774 10.771 12.827 5.602 1.00 71.03 C ANISOU 2396 C GLN A 774 9169 8691 9127 -269 -525 -204 C ATOM 2397 O GLN A 774 9.820 12.614 6.354 1.00 74.68 O ANISOU 2397 O GLN A 774 9565 9150 9660 -283 -537 -184 O ATOM 2398 CB GLN A 774 10.873 11.280 3.630 1.00 71.88 C ANISOU 2398 CB GLN A 774 9410 8755 9148 -279 -630 -240 C ATOM 2399 CG GLN A 774 9.633 10.390 3.626 1.00 74.20 C ANISOU 2399 CG GLN A 774 9674 9015 9504 -311 -713 -232 C ATOM 2400 CD GLN A 774 9.345 9.747 4.970 1.00 75.17 C ANISOU 2400 CD GLN A 774 9719 9140 9702 -328 -680 -219 C ATOM 2401 OE1 GLN A 774 10.060 9.959 5.954 1.00 74.77 O ANISOU 2401 OE1 GLN A 774 9640 9118 9650 -314 -597 -220 O ATOM 2402 NE2 GLN A 774 8.291 8.944 5.014 1.00 76.24 N ANISOU 2402 NE2 GLN A 774 9820 9243 9904 -358 -749 -204 N TER 2403 GLN A 774 ATOM 2404 N MET B 660 13.335 39.236 -6.315 1.00 72.36 N ANISOU 2404 N MET B 660 9341 8547 9605 36 -369 744 N ATOM 2405 CA MET B 660 13.814 37.965 -5.790 1.00 70.76 C ANISOU 2405 CA MET B 660 9155 8382 9347 21 -348 674 C ATOM 2406 C MET B 660 14.582 38.156 -4.490 1.00 67.97 C ANISOU 2406 C MET B 660 8746 7999 9080 -1 -308 624 C ATOM 2407 O MET B 660 14.375 37.409 -3.531 1.00 68.59 O ANISOU 2407 O MET B 660 8809 8093 9160 -16 -317 546 O ATOM 2408 CB MET B 660 14.706 37.242 -6.805 1.00 71.82 C ANISOU 2408 CB MET B 660 9360 8557 9371 36 -305 711 C ATOM 2409 CG MET B 660 15.088 35.833 -6.357 1.00 71.38 C ANISOU 2409 CG MET B 660 9329 8542 9251 26 -290 639 C ATOM 2410 SD MET B 660 16.253 34.941 -7.407 1.00 75.10 S ANISOU 2410 SD MET B 660 9882 9056 9597 50 -227 673 S ATOM 2411 CE MET B 660 16.015 33.273 -6.796 1.00 48.64 C ANISOU 2411 CE MET B 660 6555 5743 6182 36 -251 572 C ATOM 2412 N ASN B 661 15.475 39.145 -4.457 1.00 65.93 N ANISOU 2412 N ASN B 661 8459 7698 8895 -5 -267 669 N ATOM 2413 CA ASN B 661 16.241 39.433 -3.244 1.00 62.42 C ANISOU 2413 CA ASN B 661 7962 7216 8538 -28 -241 623 C ATOM 2414 C ASN B 661 15.474 40.376 -2.304 1.00 56.99 C ANISOU 2414 C ASN B 661 7223 6475 7954 -30 -280 587 C ATOM 2415 O ASN B 661 16.062 41.088 -1.488 1.00 54.57 O ANISOU 2415 O ASN B 661 6877 6117 7740 -43 -268 569 O ATOM 2416 CB ASN B 661 17.619 40.015 -3.594 1.00 65.93 C ANISOU 2416 CB ASN B 661 8393 7633 9026 -34 -184 689 C ATOM 2417 CG ASN B 661 17.532 41.307 -4.390 1.00 68.61 C ANISOU 2417 CG ASN B 661 8721 7927 9420 -22 -184 781 C ATOM 2418 OD1 ASN B 661 16.497 41.628 -4.983 1.00 71.48 O ANISOU 2418 OD1 ASN B 661 9103 8295 9761 -3 -223 808 O ATOM 2419 ND2 ASN B 661 18.629 42.058 -4.408 1.00 69.85 N ANISOU 2419 ND2 ASN B 661 8844 8040 9657 -33 -142 834 N ATOM 2420 N ALA B 662 14.150 40.358 -2.421 1.00 51.60 N ANISOU 2420 N ALA B 662 6545 5804 7257 -15 -328 577 N ATOM 2421 CA ALA B 662 13.279 41.129 -1.542 1.00 47.52 C ANISOU 2421 CA ALA B 662 5983 5243 6828 -8 -359 541 C ATOM 2422 C ALA B 662 13.335 40.638 -0.087 1.00 42.05 C ANISOU 2422 C ALA B 662 5268 4550 6158 -18 -354 445 C ATOM 2423 O ALA B 662 12.839 41.307 0.817 1.00 41.01 O ANISOU 2423 O ALA B 662 5104 4378 6101 -8 -368 407 O ATOM 2424 CB ALA B 662 11.853 41.081 -2.059 1.00 47.35 C ANISOU 2424 CB ALA B 662 5968 5240 6784 11 -409 559 C ATOM 2425 N HIS B 663 13.928 39.468 0.131 1.00 38.16 N ANISOU 2425 N HIS B 663 4797 4104 5597 -33 -332 408 N ATOM 2426 CA HIS B 663 14.075 38.923 1.475 1.00 35.30 C ANISOU 2426 CA HIS B 663 4418 3748 5247 -41 -324 324 C ATOM 2427 C HIS B 663 15.003 39.778 2.330 1.00 36.21 C ANISOU 2427 C HIS B 663 4506 3805 5446 -50 -309 301 C ATOM 2428 O HIS B 663 14.835 39.863 3.542 1.00 37.28 O ANISOU 2428 O HIS B 663 4625 3921 5617 -45 -317 233 O ATOM 2429 CB HIS B 663 14.597 37.493 1.412 1.00 31.54 C ANISOU 2429 CB HIS B 663 3972 3331 4682 -55 -304 298 C ATOM 2430 CG HIS B 663 15.943 37.375 0.773 1.00 29.33 C ANISOU 2430 CG HIS B 663 3710 3054 4378 -67 -265 340 C ATOM 2431 ND1 HIS B 663 16.107 37.103 -0.568 1.00 28.80 N ANISOU 2431 ND1 HIS B 663 3683 3015 4243 -60 -253 405 N ATOM 2432 CD2 HIS B 663 17.189 37.492 1.289 1.00 28.37 C ANISOU 2432 CD2 HIS B 663 3573 2913 4295 -84 -233 331 C ATOM 2433 CE1 HIS B 663 17.397 37.059 -0.851 1.00 28.61 C ANISOU 2433 CE1 HIS B 663 3664 2990 4217 -68 -206 437 C ATOM 2434 NE2 HIS B 663 18.076 37.284 0.260 1.00 28.42 N ANISOU 2434 NE2 HIS B 663 3601 2935 4261 -85 -196 394 N ATOM 2435 N GLU B 664 15.971 40.425 1.688 1.00 38.89 N ANISOU 2435 N GLU B 664 4844 4114 5820 -61 -290 361 N ATOM 2436 CA GLU B 664 16.962 41.239 2.391 1.00 41.59 C ANISOU 2436 CA GLU B 664 5157 4393 6253 -76 -284 349 C ATOM 2437 C GLU B 664 16.334 42.364 3.225 1.00 41.81 C ANISOU 2437 C GLU B 664 5160 4354 6370 -61 -317 312 C ATOM 2438 O GLU B 664 16.990 42.938 4.080 1.00 41.47 O ANISOU 2438 O GLU B 664 5100 4256 6399 -71 -326 276 O ATOM 2439 CB GLU B 664 17.972 41.825 1.394 1.00 46.65 C ANISOU 2439 CB GLU B 664 5791 5008 6926 -89 -257 440 C ATOM 2440 CG GLU B 664 18.832 40.776 0.678 1.00 49.99 C ANISOU 2440 CG GLU B 664 6238 5489 7266 -98 -212 475 C ATOM 2441 CD GLU B 664 19.924 41.383 -0.214 1.00 53.60 C ANISOU 2441 CD GLU B 664 6682 5918 7765 -106 -173 571 C ATOM 2442 OE1 GLU B 664 19.587 42.184 -1.123 1.00 55.36 O ANISOU 2442 OE1 GLU B 664 6907 6120 8005 -93 -173 646 O ATOM 2443 OE2 GLU B 664 21.122 41.058 -0.004 1.00 56.03 O ANISOU 2443 OE2 GLU B 664 6974 6226 8091 -125 -140 577 O ATOM 2444 N SER B 665 15.061 42.659 2.996 1.00 42.50 N ANISOU 2444 N SER B 665 5248 4443 6455 -36 -338 320 N ATOM 2445 CA SER B 665 14.358 43.686 3.762 1.00 42.42 C ANISOU 2445 CA SER B 665 5218 4373 6527 -12 -364 285 C ATOM 2446 C SER B 665 13.571 43.129 4.942 1.00 40.44 C ANISOU 2446 C SER B 665 4969 4145 6250 9 -369 198 C ATOM 2447 O SER B 665 13.300 43.841 5.900 1.00 41.07 O ANISOU 2447 O SER B 665 5041 4175 6390 31 -381 147 O ATOM 2448 CB SER B 665 13.401 44.464 2.856 1.00 41.62 C ANISOU 2448 CB SER B 665 5109 4252 6454 9 -381 352 C ATOM 2449 OG SER B 665 14.114 45.149 1.849 1.00 41.13 O ANISOU 2449 OG SER B 665 5044 4159 6425 -5 -374 437 O ATOM 2450 N LYS B 666 13.199 41.857 4.868 1.00 39.21 N ANISOU 2450 N LYS B 666 4826 4064 6007 6 -359 183 N ATOM 2451 CA LYS B 666 12.261 41.275 5.825 1.00 38.22 C ANISOU 2451 CA LYS B 666 4697 3968 5857 30 -359 120 C ATOM 2452 C LYS B 666 12.842 41.067 7.228 1.00 38.15 C ANISOU 2452 C LYS B 666 4695 3948 5851 32 -348 37 C ATOM 2453 O LYS B 666 14.051 40.901 7.404 1.00 37.46 O ANISOU 2453 O LYS B 666 4618 3853 5761 6 -343 24 O ATOM 2454 CB LYS B 666 11.733 39.952 5.280 1.00 38.71 C ANISOU 2454 CB LYS B 666 4769 4107 5833 22 -356 134 C ATOM 2455 CG LYS B 666 11.046 40.098 3.947 1.00 40.59 C ANISOU 2455 CG LYS B 666 5007 4356 6058 24 -378 209 C ATOM 2456 CD LYS B 666 9.890 41.060 4.044 1.00 42.74 C ANISOU 2456 CD LYS B 666 5251 4591 6399 56 -399 224 C ATOM 2457 CE LYS B 666 8.851 40.785 2.962 1.00 43.78 C ANISOU 2457 CE LYS B 666 5379 4754 6504 61 -430 283 C ATOM 2458 NZ LYS B 666 8.107 39.501 3.199 1.00 43.59 N ANISOU 2458 NZ LYS B 666 5350 4788 6425 59 -438 257 N ATOM 2459 N GLU B 667 11.951 41.073 8.214 1.00 37.75 N ANISOU 2459 N GLU B 667 4640 3897 5807 67 -345 -16 N ATOM 2460 CA GLU B 667 12.303 41.020 9.626 1.00 37.15 C ANISOU 2460 CA GLU B 667 4577 3806 5730 83 -338 -97 C ATOM 2461 C GLU B 667 12.885 39.674 10.023 1.00 32.64 C ANISOU 2461 C GLU B 667 4021 3297 5083 61 -321 -128 C ATOM 2462 O GLU B 667 13.631 39.564 10.989 1.00 31.91 O ANISOU 2462 O GLU B 667 3945 3193 4984 59 -322 -184 O ATOM 2463 CB GLU B 667 11.065 41.322 10.467 1.00 39.50 C ANISOU 2463 CB GLU B 667 4867 4095 6044 136 -328 -134 C ATOM 2464 CG GLU B 667 9.841 40.599 9.935 1.00 41.65 C ANISOU 2464 CG GLU B 667 5115 4425 6286 146 -317 -94 C ATOM 2465 CD GLU B 667 8.552 40.957 10.653 1.00 44.32 C ANISOU 2465 CD GLU B 667 5433 4753 6653 202 -301 -113 C ATOM 2466 OE1 GLU B 667 8.632 41.599 11.727 1.00 47.54 O ANISOU 2466 OE1 GLU B 667 5859 5119 7086 239 -290 -172 O ATOM 2467 OE2 GLU B 667 7.462 40.594 10.133 1.00 45.55 O ANISOU 2467 OE2 GLU B 667 5557 4940 6808 211 -300 -69 O ATOM 2468 N TRP B 668 12.538 38.645 9.270 1.00 29.33 N ANISOU 2468 N TRP B 668 3597 2939 4606 44 -312 -90 N ATOM 2469 CA TRP B 668 12.972 37.304 9.592 1.00 25.60 C ANISOU 2469 CA TRP B 668 3138 2525 4064 26 -296 -116 C ATOM 2470 C TRP B 668 14.278 36.906 8.906 1.00 24.42 C ANISOU 2470 C TRP B 668 3001 2385 3891 -15 -293 -89 C ATOM 2471 O TRP B 668 14.826 35.841 9.183 1.00 24.04 O ANISOU 2471 O TRP B 668 2965 2379 3792 -31 -279 -110 O ATOM 2472 CB TRP B 668 11.865 36.307 9.238 1.00 23.44 C ANISOU 2472 CB TRP B 668 2854 2309 3745 31 -291 -96 C ATOM 2473 CG TRP B 668 11.162 36.565 7.932 1.00 21.88 C ANISOU 2473 CG TRP B 668 2645 2112 3556 27 -311 -28 C ATOM 2474 CD1 TRP B 668 9.917 37.108 7.764 1.00 21.79 C ANISOU 2474 CD1 TRP B 668 2607 2087 3584 54 -324 -5 C ATOM 2475 CD2 TRP B 668 11.651 36.273 6.614 1.00 21.36 C ANISOU 2475 CD2 TRP B 668 2596 2063 3456 -2 -322 26 C ATOM 2476 NE1 TRP B 668 9.600 37.171 6.427 1.00 21.67 N ANISOU 2476 NE1 TRP B 668 2593 2079 3562 41 -350 60 N ATOM 2477 CE2 TRP B 668 10.644 36.666 5.697 1.00 21.60 C ANISOU 2477 CE2 TRP B 668 2615 2089 3502 9 -348 78 C ATOM 2478 CE3 TRP B 668 12.836 35.715 6.120 1.00 20.33 C ANISOU 2478 CE3 TRP B 668 2492 1951 3282 -31 -310 36 C ATOM 2479 CZ2 TRP B 668 10.786 36.518 4.319 1.00 21.41 C ANISOU 2479 CZ2 TRP B 668 2613 2081 3443 -8 -366 138 C ATOM 2480 CZ3 TRP B 668 12.976 35.565 4.762 1.00 21.64 C ANISOU 2480 CZ3 TRP B 668 2677 2131 3413 -43 -318 96 C ATOM 2481 CH2 TRP B 668 11.955 35.972 3.869 1.00 22.34 C ANISOU 2481 CH2 TRP B 668 2762 2217 3509 -31 -348 145 C ATOM 2482 N TYR B 669 14.781 37.750 8.013 1.00 23.70 N ANISOU 2482 N TYR B 669 2907 2257 3842 -28 -302 -37 N ATOM 2483 CA TYR B 669 16.007 37.401 7.306 1.00 22.34 C ANISOU 2483 CA TYR B 669 2743 2095 3652 -61 -289 -1 C ATOM 2484 C TYR B 669 17.234 37.965 8.007 1.00 21.50 C ANISOU 2484 C TYR B 669 2629 1939 3601 -75 -294 -27 C ATOM 2485 O TYR B 669 17.227 39.104 8.460 1.00 21.38 O ANISOU 2485 O TYR B 669 2603 1860 3658 -65 -316 -41 O ATOM 2486 CB TYR B 669 15.962 37.887 5.854 1.00 22.58 C ANISOU 2486 CB TYR B 669 2773 2117 3689 -67 -289 81 C ATOM 2487 CG TYR B 669 17.226 37.550 5.127 1.00 22.90 C ANISOU 2487 CG TYR B 669 2822 2168 3710 -92 -264 125 C ATOM 2488 CD1 TYR B 669 17.471 36.247 4.702 1.00 22.21 C ANISOU 2488 CD1 TYR B 669 2759 2142 3538 -100 -243 128 C ATOM 2489 CD2 TYR B 669 18.203 38.519 4.901 1.00 24.04 C ANISOU 2489 CD2 TYR B 669 2948 2258 3927 -105 -260 164 C ATOM 2490 CE1 TYR B 669 18.646 35.915 4.059 1.00 22.19 C ANISOU 2490 CE1 TYR B 669 2765 2151 3517 -116 -212 169 C ATOM 2491 CE2 TYR B 669 19.392 38.202 4.253 1.00 24.11 C ANISOU 2491 CE2 TYR B 669 2959 2278 3925 -124 -228 212 C ATOM 2492 CZ TYR B 669 19.605 36.889 3.831 1.00 23.37 C ANISOU 2492 CZ TYR B 669 2890 2249 3739 -127 -201 214 C ATOM 2493 OH TYR B 669 20.778 36.552 3.180 1.00 23.06 O ANISOU 2493 OH TYR B 669 2853 2222 3687 -138 -161 264 O ATOM 2494 N HIS B 670 18.280 37.151 8.099 1.00 20.83 N ANISOU 2494 N HIS B 670 2549 1881 3485 -98 -278 -32 N ATOM 2495 CA HIS B 670 19.555 37.568 8.683 1.00 20.79 C ANISOU 2495 CA HIS B 670 2531 1832 3537 -118 -289 -48 C ATOM 2496 C HIS B 670 20.707 37.237 7.734 1.00 20.35 C ANISOU 2496 C HIS B 670 2464 1787 3479 -145 -261 17 C ATOM 2497 O HIS B 670 20.988 36.077 7.479 1.00 20.60 O ANISOU 2497 O HIS B 670 2509 1876 3443 -152 -234 21 O ATOM 2498 CB HIS B 670 19.773 36.897 10.046 1.00 19.95 C ANISOU 2498 CB HIS B 670 2435 1742 3402 -114 -298 -127 C ATOM 2499 CG HIS B 670 18.679 37.174 11.035 1.00 19.78 C ANISOU 2499 CG HIS B 670 2428 1713 3375 -78 -314 -189 C ATOM 2500 ND1 HIS B 670 18.780 38.153 12.004 1.00 19.90 N ANISOU 2500 ND1 HIS B 670 2448 1666 3447 -63 -348 -240 N ATOM 2501 CD2 HIS B 670 17.459 36.613 11.194 1.00 19.34 C ANISOU 2501 CD2 HIS B 670 2381 1702 3266 -52 -300 -205 C ATOM 2502 CE1 HIS B 670 17.669 38.178 12.718 1.00 19.84 C ANISOU 2502 CE1 HIS B 670 2456 1669 3414 -23 -345 -285 C ATOM 2503 NE2 HIS B 670 16.848 37.258 12.245 1.00 19.69 N ANISOU 2503 NE2 HIS B 670 2434 1714 3333 -18 -314 -261 N ATOM 2504 N ALA B 671 21.359 38.267 7.204 1.00 21.49 N ANISOU 2504 N ALA B 671 2586 1877 3704 -159 -264 72 N ATOM 2505 CA ALA B 671 22.462 38.099 6.243 1.00 22.21 C ANISOU 2505 CA ALA B 671 2661 1973 3803 -179 -228 148 C ATOM 2506 C ALA B 671 23.727 37.548 6.903 1.00 21.88 C ANISOU 2506 C ALA B 671 2601 1932 3781 -202 -224 127 C ATOM 2507 O ALA B 671 24.558 36.916 6.257 1.00 22.78 O ANISOU 2507 O ALA B 671 2708 2075 3872 -211 -183 176 O ATOM 2508 CB ALA B 671 22.766 39.424 5.558 1.00 22.93 C ANISOU 2508 CB ALA B 671 2725 1999 3987 -187 -232 219 C ATOM 2509 N SER B 672 23.854 37.809 8.198 1.00 22.27 N ANISOU 2509 N SER B 672 2644 1946 3870 -206 -269 54 N ATOM 2510 CA SER B 672 25.014 37.399 8.979 1.00 22.36 C ANISOU 2510 CA SER B 672 2638 1950 3909 -227 -282 28 C ATOM 2511 C SER B 672 24.572 36.960 10.373 1.00 22.81 C ANISOU 2511 C SER B 672 2722 2021 3926 -213 -318 -72 C ATOM 2512 O SER B 672 24.250 37.789 11.229 1.00 21.94 O ANISOU 2512 O SER B 672 2618 1858 3858 -204 -365 -125 O ATOM 2513 CB SER B 672 26.014 38.538 9.072 1.00 23.53 C ANISOU 2513 CB SER B 672 2743 2015 4185 -253 -314 60 C ATOM 2514 OG SER B 672 27.247 38.069 9.564 1.00 25.04 O ANISOU 2514 OG SER B 672 2905 2200 4407 -278 -322 56 O ATOM 2515 N LEU B 673 24.535 35.650 10.574 1.00 22.18 N ANISOU 2515 N LEU B 673 2659 2008 3760 -208 -292 -95 N ATOM 2516 CA LEU B 673 24.021 35.040 11.788 1.00 21.45 C ANISOU 2516 CA LEU B 673 2595 1943 3612 -190 -312 -177 C ATOM 2517 C LEU B 673 24.427 33.577 11.808 1.00 21.01 C ANISOU 2517 C LEU B 673 2545 1952 3484 -195 -280 -178 C ATOM 2518 O LEU B 673 24.155 32.852 10.844 1.00 20.25 O ANISOU 2518 O LEU B 673 2457 1904 3334 -193 -237 -137 O ATOM 2519 CB LEU B 673 22.495 35.148 11.858 1.00 20.42 C ANISOU 2519 CB LEU B 673 2492 1832 3436 -157 -308 -204 C ATOM 2520 CG LEU B 673 21.893 34.726 13.204 1.00 19.08 C ANISOU 2520 CG LEU B 673 2350 1682 3219 -131 -324 -285 C ATOM 2521 CD1 LEU B 673 22.128 35.823 14.221 1.00 18.34 C ANISOU 2521 CD1 LEU B 673 2263 1519 3187 -121 -376 -338 C ATOM 2522 CD2 LEU B 673 20.435 34.384 13.105 1.00 18.24 C ANISOU 2522 CD2 LEU B 673 2259 1616 3056 -101 -302 -293 C ATOM 2523 N THR B 674 25.055 33.133 12.895 1.00 21.12 N ANISOU 2523 N THR B 674 2560 1968 3495 -199 -304 -227 N ATOM 2524 CA THR B 674 25.486 31.735 12.982 1.00 20.81 C ANISOU 2524 CA THR B 674 2526 1987 3395 -203 -276 -228 C ATOM 2525 C THR B 674 24.366 30.834 13.471 1.00 19.20 C ANISOU 2525 C THR B 674 2356 1837 3101 -178 -262 -272 C ATOM 2526 O THR B 674 23.340 31.295 13.936 1.00 20.40 O ANISOU 2526 O THR B 674 2526 1983 3243 -155 -276 -307 O ATOM 2527 CB THR B 674 26.731 31.551 13.916 1.00 20.58 C ANISOU 2527 CB THR B 674 2478 1938 3403 -220 -309 -252 C ATOM 2528 OG1 THR B 674 26.361 31.715 15.291 1.00 20.91 O ANISOU 2528 OG1 THR B 674 2547 1968 3428 -203 -356 -330 O ATOM 2529 CG2 THR B 674 27.804 32.555 13.580 1.00 21.29 C ANISOU 2529 CG2 THR B 674 2525 1962 3601 -248 -333 -209 C ATOM 2530 N ARG B 675 24.589 29.533 13.358 1.00 18.89 N ANISOU 2530 N ARG B 675 2323 1851 3005 -181 -232 -266 N ATOM 2531 CA ARG B 675 23.665 28.533 13.865 1.00 17.89 C ANISOU 2531 CA ARG B 675 2222 1774 2802 -162 -219 -301 C ATOM 2532 C ARG B 675 23.486 28.666 15.377 1.00 18.21 C ANISOU 2532 C ARG B 675 2278 1808 2836 -143 -251 -366 C ATOM 2533 O ARG B 675 22.373 28.537 15.902 1.00 17.59 O ANISOU 2533 O ARG B 675 2218 1748 2718 -117 -247 -396 O ATOM 2534 CB ARG B 675 24.169 27.140 13.500 1.00 18.90 C ANISOU 2534 CB ARG B 675 2351 1947 2882 -171 -186 -281 C ATOM 2535 CG ARG B 675 23.267 25.978 13.968 1.00 19.82 C ANISOU 2535 CG ARG B 675 2490 2113 2928 -155 -172 -309 C ATOM 2536 CD ARG B 675 24.016 24.677 13.777 1.00 19.44 C ANISOU 2536 CD ARG B 675 2443 2097 2846 -165 -147 -296 C ATOM 2537 NE ARG B 675 23.294 23.509 14.245 1.00 18.92 N ANISOU 2537 NE ARG B 675 2394 2072 2722 -154 -136 -318 N ATOM 2538 CZ ARG B 675 22.637 22.661 13.455 1.00 18.65 C ANISOU 2538 CZ ARG B 675 2375 2065 2648 -154 -116 -299 C ATOM 2539 NH1 ARG B 675 22.597 22.854 12.133 1.00 17.24 N ANISOU 2539 NH1 ARG B 675 2204 1881 2468 -160 -104 -261 N ATOM 2540 NH2 ARG B 675 22.022 21.617 13.994 1.00 18.02 N ANISOU 2540 NH2 ARG B 675 2304 2016 2528 -147 -110 -317 N ATOM 2541 N ALA B 676 24.587 28.939 16.074 1.00 17.93 N ANISOU 2541 N ALA B 676 2233 1742 2838 -155 -285 -385 N ATOM 2542 CA ALA B 676 24.561 29.036 17.531 1.00 18.51 C ANISOU 2542 CA ALA B 676 2331 1808 2896 -134 -323 -450 C ATOM 2543 C ALA B 676 23.830 30.302 17.975 1.00 18.36 C ANISOU 2543 C ALA B 676 2329 1744 2902 -110 -352 -486 C ATOM 2544 O ALA B 676 23.122 30.312 18.983 1.00 17.52 O ANISOU 2544 O ALA B 676 2256 1647 2753 -74 -358 -537 O ATOM 2545 CB ALA B 676 25.960 29.001 18.082 1.00 18.88 C ANISOU 2545 CB ALA B 676 2363 1830 2980 -155 -362 -458 C ATOM 2546 N GLN B 677 23.996 31.373 17.216 1.00 17.65 N ANISOU 2546 N GLN B 677 2219 1604 2882 -125 -365 -457 N ATOM 2547 CA GLN B 677 23.252 32.585 17.488 1.00 18.65 C ANISOU 2547 CA GLN B 677 2362 1684 3039 -101 -388 -485 C ATOM 2548 C GLN B 677 21.754 32.390 17.285 1.00 19.23 C ANISOU 2548 C GLN B 677 2449 1794 3062 -69 -347 -484 C ATOM 2549 O GLN B 677 20.956 32.895 18.063 1.00 18.71 O ANISOU 2549 O GLN B 677 2410 1715 2984 -31 -356 -529 O ATOM 2550 CB GLN B 677 23.740 33.715 16.597 1.00 18.98 C ANISOU 2550 CB GLN B 677 2375 1665 3173 -127 -407 -442 C ATOM 2551 CG GLN B 677 25.060 34.346 16.999 1.00 19.05 C ANISOU 2551 CG GLN B 677 2367 1612 3261 -154 -464 -451 C ATOM 2552 CD GLN B 677 25.425 35.466 16.059 1.00 19.29 C ANISOU 2552 CD GLN B 677 2362 1580 3388 -179 -475 -397 C ATOM 2553 OE1 GLN B 677 25.789 35.224 14.896 1.00 18.71 O ANISOU 2553 OE1 GLN B 677 2254 1523 3331 -203 -434 -322 O ATOM 2554 NE2 GLN B 677 25.301 36.710 16.542 1.00 19.71 N ANISOU 2554 NE2 GLN B 677 2427 1559 3503 -170 -528 -432 N ATOM 2555 N ALA B 678 21.374 31.664 16.234 1.00 19.59 N ANISOU 2555 N ALA B 678 2477 1883 3081 -83 -305 -432 N ATOM 2556 CA ALA B 678 19.968 31.441 15.948 1.00 20.81 C ANISOU 2556 CA ALA B 678 2637 2070 3201 -58 -275 -422 C ATOM 2557 C ALA B 678 19.380 30.575 17.037 1.00 21.30 C ANISOU 2557 C ALA B 678 2719 2176 3199 -29 -258 -463 C ATOM 2558 O ALA B 678 18.229 30.741 17.418 1.00 22.44 O ANISOU 2558 O ALA B 678 2871 2329 3328 6 -243 -477 O ATOM 2559 CB ALA B 678 19.782 30.808 14.588 1.00 20.28 C ANISOU 2559 CB ALA B 678 2553 2035 3117 -81 -246 -361 C ATOM 2560 N GLU B 679 20.187 29.664 17.560 1.00 23.33 N ANISOU 2560 N GLU B 679 2982 2459 3422 -41 -259 -477 N ATOM 2561 CA GLU B 679 19.760 28.847 18.683 1.00 25.38 C ANISOU 2561 CA GLU B 679 3263 2759 3622 -12 -244 -513 C ATOM 2562 C GLU B 679 19.572 29.694 19.924 1.00 25.23 C ANISOU 2562 C GLU B 679 3276 2709 3601 29 -268 -572 C ATOM 2563 O GLU B 679 18.600 29.528 20.664 1.00 23.90 O ANISOU 2563 O GLU B 679 3126 2564 3392 72 -242 -593 O ATOM 2564 CB GLU B 679 20.769 27.753 18.952 1.00 29.75 C ANISOU 2564 CB GLU B 679 3817 3341 4146 -34 -245 -512 C ATOM 2565 CG GLU B 679 20.906 26.817 17.795 1.00 33.48 C ANISOU 2565 CG GLU B 679 4268 3845 4610 -65 -217 -461 C ATOM 2566 CD GLU B 679 20.650 25.390 18.183 1.00 37.45 C ANISOU 2566 CD GLU B 679 4775 4400 5054 -60 -190 -460 C ATOM 2567 OE1 GLU B 679 20.441 24.558 17.270 1.00 37.14 O ANISOU 2567 OE1 GLU B 679 4725 4386 5001 -78 -167 -423 O ATOM 2568 OE2 GLU B 679 20.660 25.107 19.405 1.00 42.81 O ANISOU 2568 OE2 GLU B 679 5472 5092 5702 -37 -194 -495 O ATOM 2569 N HIS B 680 20.502 30.612 20.147 1.00 24.27 N ANISOU 2569 N HIS B 680 3164 2532 3525 18 -317 -597 N ATOM 2570 CA HIS B 680 20.410 31.506 21.279 1.00 23.53 C ANISOU 2570 CA HIS B 680 3111 2399 3432 58 -351 -660 C ATOM 2571 C HIS B 680 19.128 32.361 21.228 1.00 22.34 C ANISOU 2571 C HIS B 680 2968 2229 3293 100 -330 -667 C ATOM 2572 O HIS B 680 18.482 32.595 22.253 1.00 21.17 O ANISOU 2572 O HIS B 680 2857 2080 3105 154 -321 -713 O ATOM 2573 CB HIS B 680 21.638 32.392 21.325 1.00 24.05 C ANISOU 2573 CB HIS B 680 3177 2398 3564 30 -417 -678 C ATOM 2574 CG HIS B 680 21.709 33.252 22.541 1.00 24.64 C ANISOU 2574 CG HIS B 680 3303 2423 3635 69 -468 -752 C ATOM 2575 ND1 HIS B 680 21.065 34.467 22.628 1.00 25.29 N ANISOU 2575 ND1 HIS B 680 3406 2452 3751 100 -481 -779 N ATOM 2576 CD2 HIS B 680 22.350 33.076 23.721 1.00 25.05 C ANISOU 2576 CD2 HIS B 680 3397 2470 3650 85 -513 -807 C ATOM 2577 CE1 HIS B 680 21.312 35.006 23.809 1.00 26.35 C ANISOU 2577 CE1 HIS B 680 3596 2548 3868 135 -532 -852 C ATOM 2578 NE2 HIS B 680 22.091 34.185 24.490 1.00 26.13 N ANISOU 2578 NE2 HIS B 680 3584 2550 3795 126 -554 -871 N ATOM 2579 N MET B 681 18.754 32.806 20.034 1.00 20.16 N ANISOU 2579 N MET B 681 2656 1937 3066 78 -318 -618 N ATOM 2580 CA MET B 681 17.545 33.584 19.866 1.00 20.64 C ANISOU 2580 CA MET B 681 2716 1980 3147 114 -298 -614 C ATOM 2581 C MET B 681 16.274 32.744 20.019 1.00 20.74 C ANISOU 2581 C MET B 681 2720 2053 3107 146 -241 -597 C ATOM 2582 O MET B 681 15.335 33.152 20.718 1.00 20.74 O ANISOU 2582 O MET B 681 2737 2050 3094 201 -219 -622 O ATOM 2583 CB MET B 681 17.553 34.261 18.503 1.00 20.19 C ANISOU 2583 CB MET B 681 2623 1890 3158 81 -306 -560 C ATOM 2584 CG MET B 681 18.734 35.189 18.285 1.00 20.45 C ANISOU 2584 CG MET B 681 2655 1857 3260 49 -358 -564 C ATOM 2585 SD MET B 681 18.999 35.509 16.535 1.00 23.94 S ANISOU 2585 SD MET B 681 3051 2284 3763 1 -352 -478 S ATOM 2586 CE MET B 681 17.757 36.787 16.279 1.00 18.74 C ANISOU 2586 CE MET B 681 2390 1579 3150 39 -352 -473 C ATOM 2587 N LEU B 682 16.251 31.573 19.375 1.00 20.32 N ANISOU 2587 N LEU B 682 2639 2053 3027 114 -217 -552 N ATOM 2588 CA LEU B 682 15.064 30.733 19.392 1.00 20.59 C ANISOU 2588 CA LEU B 682 2655 2139 3028 134 -170 -526 C ATOM 2589 C LEU B 682 14.823 30.124 20.762 1.00 21.98 C ANISOU 2589 C LEU B 682 2858 2348 3144 177 -143 -562 C ATOM 2590 O LEU B 682 13.683 29.829 21.125 1.00 22.69 O ANISOU 2590 O LEU B 682 2937 2466 3218 214 -100 -549 O ATOM 2591 CB LEU B 682 15.167 29.633 18.343 1.00 19.20 C ANISOU 2591 CB LEU B 682 2451 2003 2843 87 -161 -474 C ATOM 2592 CG LEU B 682 14.984 30.161 16.921 1.00 18.55 C ANISOU 2592 CG LEU B 682 2344 1899 2807 58 -176 -427 C ATOM 2593 CD1 LEU B 682 15.061 29.026 15.939 1.00 17.36 C ANISOU 2593 CD1 LEU B 682 2177 1786 2633 20 -169 -383 C ATOM 2594 CD2 LEU B 682 13.689 30.934 16.778 1.00 18.37 C ANISOU 2594 CD2 LEU B 682 2304 1860 2818 92 -165 -412 C ATOM 2595 N MET B 683 15.894 29.927 21.523 1.00 23.09 N ANISOU 2595 N MET B 683 3032 2486 3255 172 -168 -603 N ATOM 2596 CA MET B 683 15.758 29.375 22.856 1.00 23.89 C ANISOU 2596 CA MET B 683 3167 2618 3290 216 -146 -637 C ATOM 2597 C MET B 683 15.032 30.372 23.741 1.00 27.37 C ANISOU 2597 C MET B 683 3644 3032 3723 285 -134 -679 C ATOM 2598 O MET B 683 14.444 29.987 24.758 1.00 26.13 O ANISOU 2598 O MET B 683 3510 2907 3510 339 -94 -695 O ATOM 2599 CB MET B 683 17.118 29.007 23.450 1.00 24.42 C ANISOU 2599 CB MET B 683 3265 2685 3330 197 -186 -671 C ATOM 2600 CG MET B 683 17.634 27.659 22.970 1.00 24.09 C ANISOU 2600 CG MET B 683 3195 2687 3270 151 -176 -631 C ATOM 2601 SD MET B 683 19.031 26.965 23.880 1.00 74.55 S ANISOU 2601 SD MET B 683 9616 9090 9620 139 -211 -663 S ATOM 2602 CE MET B 683 20.386 28.039 23.412 1.00 35.61 C ANISOU 2602 CE MET B 683 4682 4090 4757 98 -284 -681 C ATOM 2603 N ARG B 684 15.047 31.644 23.344 1.00 29.94 N ANISOU 2603 N ARG B 684 3972 3298 4105 287 -165 -695 N ATOM 2604 CA ARG B 684 14.392 32.677 24.134 1.00 33.74 C ANISOU 2604 CA ARG B 684 4492 3743 4583 356 -157 -740 C ATOM 2605 C ARG B 684 12.924 32.853 23.758 1.00 37.16 C ANISOU 2605 C ARG B 684 4888 4190 5040 390 -100 -698 C ATOM 2606 O ARG B 684 12.219 33.615 24.406 1.00 36.43 O ANISOU 2606 O ARG B 684 4822 4074 4944 456 -77 -728 O ATOM 2607 CB ARG B 684 15.137 34.012 24.000 1.00 33.56 C ANISOU 2607 CB ARG B 684 4494 3640 4616 345 -223 -781 C ATOM 2608 CG ARG B 684 16.507 34.009 24.685 1.00 33.61 C ANISOU 2608 CG ARG B 684 4545 3623 4602 327 -286 -833 C ATOM 2609 CD ARG B 684 17.308 35.231 24.357 1.00 34.24 C ANISOU 2609 CD ARG B 684 4632 3619 4757 300 -358 -859 C ATOM 2610 NE ARG B 684 16.622 36.400 24.874 1.00 36.21 N ANISOU 2610 NE ARG B 684 4923 3815 5020 362 -361 -906 N ATOM 2611 CZ ARG B 684 16.757 37.625 24.377 1.00 37.21 C ANISOU 2611 CZ ARG B 684 5045 3865 5228 351 -403 -912 C ATOM 2612 NH1 ARG B 684 17.561 37.822 23.332 1.00 37.00 N ANISOU 2612 NH1 ARG B 684 4971 3810 5277 280 -440 -869 N ATOM 2613 NH2 ARG B 684 16.075 38.640 24.913 1.00 37.71 N ANISOU 2613 NH2 ARG B 684 5150 3879 5299 416 -402 -959 N ATOM 2614 N VAL B 685 12.465 32.155 22.717 1.00 41.04 N ANISOU 2614 N VAL B 685 5319 4715 5558 348 -80 -631 N ATOM 2615 CA VAL B 685 11.047 32.195 22.331 1.00 46.14 C ANISOU 2615 CA VAL B 685 5920 5376 6233 375 -32 -583 C ATOM 2616 C VAL B 685 10.434 30.820 22.288 1.00 52.81 C ANISOU 2616 C VAL B 685 6727 6287 7052 365 11 -533 C ATOM 2617 O VAL B 685 10.303 30.251 21.219 1.00 55.01 O ANISOU 2617 O VAL B 685 6961 6582 7359 313 0 -482 O ATOM 2618 CB VAL B 685 10.812 32.787 20.942 1.00 42.38 C ANISOU 2618 CB VAL B 685 5402 4870 5831 335 -59 -538 C ATOM 2619 CG1 VAL B 685 9.383 33.274 20.819 1.00 41.93 C ANISOU 2619 CG1 VAL B 685 5310 4808 5814 381 -21 -507 C ATOM 2620 CG2 VAL B 685 11.739 33.882 20.687 1.00 41.12 C ANISOU 2620 CG2 VAL B 685 5270 4648 5707 317 -113 -572 C ATOM 2621 N PRO B 686 10.040 30.282 23.441 1.00 61.26 N ANISOU 2621 N PRO B 686 7815 7392 8068 416 60 -545 N ATOM 2622 CA PRO B 686 9.470 28.930 23.458 1.00 62.18 C ANISOU 2622 CA PRO B 686 7891 7568 8168 405 102 -493 C ATOM 2623 C PRO B 686 8.051 28.866 22.878 1.00 58.51 C ANISOU 2623 C PRO B 686 7359 7113 7761 415 137 -428 C ATOM 2624 O PRO B 686 7.103 28.569 23.595 1.00 61.21 O ANISOU 2624 O PRO B 686 7681 7481 8096 467 199 -404 O ATOM 2625 CB PRO B 686 9.474 28.577 24.951 1.00 63.36 C ANISOU 2625 CB PRO B 686 8086 7746 8244 467 147 -524 C ATOM 2626 CG PRO B 686 10.452 29.534 25.581 1.00 63.92 C ANISOU 2626 CG PRO B 686 8231 7775 8283 489 105 -603 C ATOM 2627 CD PRO B 686 10.274 30.793 24.799 1.00 63.69 C ANISOU 2627 CD PRO B 686 8190 7688 8322 483 73 -610 C ATOM 2628 N ARG B 687 7.924 29.166 21.590 1.00 50.30 N ANISOU 2628 N ARG B 687 6282 6050 6779 368 97 -397 N ATOM 2629 CA ARG B 687 6.676 29.012 20.846 1.00 45.53 C ANISOU 2629 CA ARG B 687 5610 5453 6237 363 110 -330 C ATOM 2630 C ARG B 687 6.967 28.275 19.550 1.00 41.96 C ANISOU 2630 C ARG B 687 5131 5010 5802 285 61 -294 C ATOM 2631 O ARG B 687 7.893 28.636 18.832 1.00 42.08 O ANISOU 2631 O ARG B 687 5173 5002 5815 245 13 -313 O ATOM 2632 CB ARG B 687 6.035 30.367 20.521 1.00 42.13 C ANISOU 2632 CB ARG B 687 5167 4978 5863 396 107 -328 C ATOM 2633 CG ARG B 687 5.864 31.301 21.692 1.00 40.23 C ANISOU 2633 CG ARG B 687 4967 4715 5603 477 148 -376 C ATOM 2634 CD ARG B 687 5.409 32.706 21.245 1.00 39.19 C ANISOU 2634 CD ARG B 687 4828 4528 5534 504 134 -379 C ATOM 2635 NE ARG B 687 5.190 33.578 22.394 1.00 38.64 N ANISOU 2635 NE ARG B 687 4804 4433 5444 589 175 -429 N ATOM 2636 CZ ARG B 687 4.562 34.743 22.356 1.00 38.18 C ANISOU 2636 CZ ARG B 687 4742 4330 5436 638 185 -433 C ATOM 2637 NH1 ARG B 687 4.071 35.203 21.216 1.00 37.72 N ANISOU 2637 NH1 ARG B 687 4631 4247 5454 608 156 -385 N ATOM 2638 NH2 ARG B 687 4.422 35.448 23.468 1.00 38.71 N ANISOU 2638 NH2 ARG B 687 4862 4374 5473 720 224 -486 N ATOM 2639 N ASP B 688 6.184 27.252 19.243 1.00 39.16 N ANISOU 2639 N ASP B 688 4726 4685 5467 266 71 -240 N ATOM 2640 CA ASP B 688 6.279 26.618 17.933 1.00 35.91 C ANISOU 2640 CA ASP B 688 4294 4276 5074 200 19 -206 C ATOM 2641 C ASP B 688 5.847 27.600 16.826 1.00 31.58 C ANISOU 2641 C ASP B 688 3726 3693 4580 189 -21 -183 C ATOM 2642 O ASP B 688 4.924 28.395 17.002 1.00 33.11 O ANISOU 2642 O ASP B 688 3891 3870 4821 231 -1 -165 O ATOM 2643 CB ASP B 688 5.439 25.344 17.892 1.00 36.56 C ANISOU 2643 CB ASP B 688 4326 4390 5177 183 31 -154 C ATOM 2644 CG ASP B 688 5.848 24.328 18.967 1.00 36.22 C ANISOU 2644 CG ASP B 688 4299 4381 5082 193 72 -168 C ATOM 2645 OD1 ASP B 688 7.003 24.355 19.445 1.00 36.58 O ANISOU 2645 OD1 ASP B 688 4400 4430 5070 193 71 -219 O ATOM 2646 OD2 ASP B 688 5.009 23.491 19.345 1.00 36.80 O ANISOU 2646 OD2 ASP B 688 4326 4478 5180 202 103 -124 O ATOM 2647 N GLY B 689 6.542 27.562 15.693 1.00 27.71 N ANISOU 2647 N GLY B 689 3257 3192 4081 138 -73 -181 N ATOM 2648 CA GLY B 689 6.300 28.513 14.622 1.00 24.42 C ANISOU 2648 CA GLY B 689 2833 2742 3705 129 -113 -158 C ATOM 2649 C GLY B 689 7.208 29.737 14.651 1.00 24.65 C ANISOU 2649 C GLY B 689 2902 2733 3730 139 -120 -196 C ATOM 2650 O GLY B 689 7.209 30.527 13.704 1.00 22.94 O ANISOU 2650 O GLY B 689 2686 2488 3543 127 -153 -176 O ATOM 2651 N ALA B 690 7.948 29.923 15.743 1.00 23.63 N ANISOU 2651 N ALA B 690 2809 2602 3568 163 -93 -249 N ATOM 2652 CA ALA B 690 9.017 30.906 15.763 1.00 24.14 C ANISOU 2652 CA ALA B 690 2914 2628 3632 161 -112 -287 C ATOM 2653 C ALA B 690 10.110 30.474 14.745 1.00 19.13 C ANISOU 2653 C ALA B 690 2298 1996 2974 102 -147 -276 C ATOM 2654 O ALA B 690 10.464 29.294 14.646 1.00 16.74 O ANISOU 2654 O ALA B 690 1999 1729 2632 74 -145 -272 O ATOM 2655 CB ALA B 690 9.579 31.051 17.169 1.00 22.46 C ANISOU 2655 CB ALA B 690 2738 2412 3384 196 -86 -348 C ATOM 2656 N PHE B 691 10.620 31.414 13.961 1.00 17.22 N ANISOU 2656 N PHE B 691 2065 1716 2760 87 -175 -266 N ATOM 2657 CA PHE B 691 11.540 31.059 12.896 1.00 16.90 C ANISOU 2657 CA PHE B 691 2039 1679 2701 39 -199 -244 C ATOM 2658 C PHE B 691 12.365 32.233 12.432 1.00 17.15 C ANISOU 2658 C PHE B 691 2085 1664 2768 31 -218 -241 C ATOM 2659 O PHE B 691 12.023 33.381 12.661 1.00 17.49 O ANISOU 2659 O PHE B 691 2123 1665 2858 57 -223 -248 O ATOM 2660 CB PHE B 691 10.788 30.507 11.693 1.00 16.86 C ANISOU 2660 CB PHE B 691 2017 1696 2693 19 -217 -191 C ATOM 2661 CG PHE B 691 10.125 31.574 10.862 1.00 18.45 C ANISOU 2661 CG PHE B 691 2202 1865 2942 28 -240 -152 C ATOM 2662 CD1 PHE B 691 8.909 32.132 11.257 1.00 18.84 C ANISOU 2662 CD1 PHE B 691 2218 1902 3037 64 -234 -144 C ATOM 2663 CD2 PHE B 691 10.719 32.039 9.694 1.00 18.43 C ANISOU 2663 CD2 PHE B 691 2216 1845 2942 4 -264 -119 C ATOM 2664 CE1 PHE B 691 8.290 33.136 10.491 1.00 18.84 C ANISOU 2664 CE1 PHE B 691 2201 1870 3087 74 -257 -105 C ATOM 2665 CE2 PHE B 691 10.109 33.031 8.935 1.00 18.75 C ANISOU 2665 CE2 PHE B 691 2243 1855 3026 14 -286 -79 C ATOM 2666 CZ PHE B 691 8.892 33.576 9.334 1.00 18.10 C ANISOU 2666 CZ PHE B 691 2126 1758 2992 48 -285 -73 C ATOM 2667 N LEU B 692 13.437 31.927 11.722 1.00 17.17 N ANISOU 2667 N LEU B 692 2103 1669 2751 -6 -227 -225 N ATOM 2668 CA LEU B 692 14.218 32.939 11.038 1.00 17.63 C ANISOU 2668 CA LEU B 692 2166 1684 2848 -20 -242 -203 C ATOM 2669 C LEU B 692 14.929 32.261 9.887 1.00 18.38 C ANISOU 2669 C LEU B 692 2273 1803 2908 -54 -241 -162 C ATOM 2670 O LEU B 692 15.020 31.031 9.841 1.00 17.86 O ANISOU 2670 O LEU B 692 2216 1780 2789 -66 -231 -166 O ATOM 2671 CB LEU B 692 15.215 33.628 11.988 1.00 17.70 C ANISOU 2671 CB LEU B 692 2185 1653 2887 -16 -248 -248 C ATOM 2672 CG LEU B 692 16.168 32.803 12.869 1.00 16.94 C ANISOU 2672 CG LEU B 692 2104 1578 2755 -27 -241 -289 C ATOM 2673 CD1 LEU B 692 17.350 32.213 12.086 1.00 16.68 C ANISOU 2673 CD1 LEU B 692 2074 1559 2706 -65 -237 -258 C ATOM 2674 CD2 LEU B 692 16.654 33.643 14.036 1.00 17.26 C ANISOU 2674 CD2 LEU B 692 2158 1573 2828 -8 -259 -344 C ATOM 2675 N VAL B 693 15.416 33.066 8.953 1.00 19.41 N ANISOU 2675 N VAL B 693 2405 1903 3068 -65 -249 -119 N ATOM 2676 CA VAL B 693 16.190 32.560 7.837 1.00 19.94 C ANISOU 2676 CA VAL B 693 2488 1989 3100 -89 -240 -75 C ATOM 2677 C VAL B 693 17.560 33.178 7.948 1.00 20.79 C ANISOU 2677 C VAL B 693 2590 2060 3248 -103 -231 -70 C ATOM 2678 O VAL B 693 17.679 34.364 8.226 1.00 20.45 O ANISOU 2678 O VAL B 693 2533 1966 3272 -98 -245 -70 O ATOM 2679 CB VAL B 693 15.557 32.913 6.484 1.00 20.18 C ANISOU 2679 CB VAL B 693 2525 2019 3124 -86 -252 -15 C ATOM 2680 CG1 VAL B 693 16.429 32.416 5.328 1.00 20.37 C ANISOU 2680 CG1 VAL B 693 2577 2063 3102 -102 -235 30 C ATOM 2681 CG2 VAL B 693 14.136 32.349 6.407 1.00 19.61 C ANISOU 2681 CG2 VAL B 693 2449 1975 3026 -74 -272 -19 C ATOM 2682 N ARG B 694 18.593 32.381 7.750 1.00 21.60 N ANISOU 2682 N ARG B 694 2702 2185 3318 -121 -210 -63 N ATOM 2683 CA ARG B 694 19.946 32.907 7.801 1.00 22.52 C ANISOU 2683 CA ARG B 694 2805 2268 3484 -138 -202 -47 C ATOM 2684 C ARG B 694 20.726 32.498 6.575 1.00 24.75 C ANISOU 2684 C ARG B 694 3098 2569 3738 -148 -169 15 C ATOM 2685 O ARG B 694 20.544 31.393 6.056 1.00 24.32 O ANISOU 2685 O ARG B 694 3070 2562 3609 -145 -152 20 O ATOM 2686 CB ARG B 694 20.662 32.426 9.060 1.00 20.37 C ANISOU 2686 CB ARG B 694 2526 1997 3216 -144 -206 -103 C ATOM 2687 CG ARG B 694 20.572 30.927 9.289 1.00 18.54 C ANISOU 2687 CG ARG B 694 2312 1824 2908 -144 -188 -128 C ATOM 2688 CD ARG B 694 21.089 30.573 10.681 1.00 17.94 C ANISOU 2688 CD ARG B 694 2231 1747 2836 -145 -199 -186 C ATOM 2689 NE ARG B 694 20.727 29.214 11.054 1.00 17.33 N ANISOU 2689 NE ARG B 694 2170 1724 2692 -140 -185 -212 N ATOM 2690 CZ ARG B 694 21.476 28.157 10.777 1.00 17.36 C ANISOU 2690 CZ ARG B 694 2179 1756 2659 -152 -163 -200 C ATOM 2691 NH1 ARG B 694 22.623 28.316 10.124 1.00 17.15 N ANISOU 2691 NH1 ARG B 694 2143 1715 2657 -167 -147 -161 N ATOM 2692 NH2 ARG B 694 21.078 26.948 11.151 1.00 16.66 N ANISOU 2692 NH2 ARG B 694 2105 1710 2516 -148 -154 -224 N ATOM 2693 N LYS B 695 21.586 33.388 6.104 1.00 27.23 N ANISOU 2693 N LYS B 695 3392 2843 4111 -158 -159 65 N ATOM 2694 CA LYS B 695 22.535 33.007 5.076 1.00 29.74 C ANISOU 2694 CA LYS B 695 3716 3177 4407 -163 -116 127 C ATOM 2695 C LYS B 695 23.576 32.044 5.682 1.00 30.39 C ANISOU 2695 C LYS B 695 3790 3279 4476 -174 -96 101 C ATOM 2696 O LYS B 695 23.984 32.200 6.832 1.00 29.18 O ANISOU 2696 O LYS B 695 3613 3104 4371 -186 -120 55 O ATOM 2697 CB LYS B 695 23.195 34.245 4.472 1.00 31.86 C ANISOU 2697 CB LYS B 695 3956 3394 4755 -170 -106 196 C ATOM 2698 CG LYS B 695 23.938 33.965 3.183 1.00 34.18 C ANISOU 2698 CG LYS B 695 4262 3708 5016 -163 -51 277 C ATOM 2699 CD LYS B 695 24.424 35.239 2.535 1.00 36.47 C ANISOU 2699 CD LYS B 695 4522 3947 5387 -167 -39 356 C ATOM 2700 CE LYS B 695 25.235 34.936 1.287 1.00 38.00 C ANISOU 2700 CE LYS B 695 4728 4165 5545 -154 28 443 C ATOM 2701 NZ LYS B 695 24.510 34.021 0.349 1.00 40.74 N ANISOU 2701 NZ LYS B 695 5142 4573 5764 -126 45 447 N ATOM 2702 N ARG B 696 23.970 31.025 4.924 1.00 32.39 N ANISOU 2702 N ARG B 696 4068 3575 4662 -167 -56 127 N ATOM 2703 CA ARG B 696 25.066 30.150 5.338 1.00 34.82 C ANISOU 2703 CA ARG B 696 4366 3900 4965 -175 -30 117 C ATOM 2704 C ARG B 696 26.380 30.545 4.644 1.00 38.85 C ANISOU 2704 C ARG B 696 4847 4389 5524 -179 16 192 C ATOM 2705 O ARG B 696 26.400 31.377 3.731 1.00 41.46 O ANISOU 2705 O ARG B 696 5175 4700 5878 -173 34 257 O ATOM 2706 CB ARG B 696 24.724 28.694 5.053 1.00 32.36 C ANISOU 2706 CB ARG B 696 4098 3644 4554 -162 -11 94 C ATOM 2707 CG ARG B 696 23.342 28.291 5.538 1.00 30.67 C ANISOU 2707 CG ARG B 696 3907 3451 4296 -157 -51 37 C ATOM 2708 CD ARG B 696 23.297 26.852 6.017 1.00 29.03 C ANISOU 2708 CD ARG B 696 3719 3283 4030 -156 -47 -8 C ATOM 2709 NE ARG B 696 23.557 25.902 4.949 1.00 28.46 N ANISOU 2709 NE ARG B 696 3688 3240 3886 -143 -12 19 N ATOM 2710 CZ ARG B 696 24.361 24.855 5.064 1.00 27.41 C ANISOU 2710 CZ ARG B 696 3562 3127 3725 -141 18 11 C ATOM 2711 NH1 ARG B 696 24.993 24.617 6.202 1.00 27.00 N ANISOU 2711 NH1 ARG B 696 3476 3070 3712 -153 15 -20 N ATOM 2712 NH2 ARG B 696 24.539 24.048 4.034 1.00 27.34 N ANISOU 2712 NH2 ARG B 696 3599 3141 3647 -122 49 34 N ATOM 2713 N ASN B 697 27.487 29.961 5.087 1.00 43.87 N ANISOU 2713 N ASN B 697 5458 5029 6182 -188 37 191 N ATOM 2714 CA ASN B 697 28.783 30.348 4.544 1.00 48.89 C ANISOU 2714 CA ASN B 697 6054 5641 6882 -192 82 268 C ATOM 2715 C ASN B 697 28.983 29.847 3.138 1.00 52.14 C ANISOU 2715 C ASN B 697 6501 6088 7222 -162 153 334 C ATOM 2716 O ASN B 697 29.464 30.583 2.280 1.00 55.84 O ANISOU 2716 O ASN B 697 6953 6536 7729 -155 191 415 O ATOM 2717 CB ASN B 697 29.884 29.863 5.455 1.00 52.01 C ANISOU 2717 CB ASN B 697 6407 6029 7326 -208 80 250 C ATOM 2718 CG ASN B 697 30.007 30.731 6.672 1.00 54.39 C ANISOU 2718 CG ASN B 697 6667 6278 7722 -237 11 208 C ATOM 2719 OD1 ASN B 697 30.216 31.944 6.557 1.00 55.53 O ANISOU 2719 OD1 ASN B 697 6777 6368 7954 -251 -8 244 O ATOM 2720 ND2 ASN B 697 29.814 30.140 7.847 1.00 56.45 N ANISOU 2720 ND2 ASN B 697 6936 6551 7961 -242 -31 130 N ATOM 2721 N GLU B 698 28.587 28.604 2.905 1.00 53.93 N ANISOU 2721 N GLU B 698 6781 6365 7345 -142 168 300 N ATOM 2722 CA GLU B 698 28.513 28.055 1.558 1.00 55.40 C ANISOU 2722 CA GLU B 698 7025 6587 7439 -107 223 345 C ATOM 2723 C GLU B 698 27.727 28.992 0.639 1.00 51.76 C ANISOU 2723 C GLU B 698 6590 6115 6962 -96 214 387 C ATOM 2724 O GLU B 698 26.712 29.548 1.046 1.00 51.59 O ANISOU 2724 O GLU B 698 6567 6078 6955 -110 155 350 O ATOM 2725 CB GLU B 698 27.867 26.666 1.599 1.00 60.66 C ANISOU 2725 CB GLU B 698 7751 7297 7999 -93 212 282 C ATOM 2726 CG GLU B 698 27.702 26.001 0.246 1.00 65.70 C ANISOU 2726 CG GLU B 698 8464 7970 8529 -53 256 313 C ATOM 2727 CD GLU B 698 27.111 24.611 0.361 1.00 70.29 C ANISOU 2727 CD GLU B 698 9102 8585 9021 -43 236 246 C ATOM 2728 OE1 GLU B 698 27.149 24.046 1.482 1.00 73.18 O ANISOU 2728 OE1 GLU B 698 9439 8952 9413 -65 210 190 O ATOM 2729 OE2 GLU B 698 26.610 24.084 -0.662 1.00 72.17 O ANISOU 2729 OE2 GLU B 698 9413 8845 9162 -14 242 251 O ATOM 2730 N PRO B 699 28.208 29.190 -0.597 1.00 47.85 N ANISOU 2730 N PRO B 699 6115 5626 6438 -67 276 470 N ATOM 2731 CA PRO B 699 27.494 30.061 -1.544 1.00 46.78 C ANISOU 2731 CA PRO B 699 6008 5483 6281 -52 270 518 C ATOM 2732 C PRO B 699 26.091 29.543 -1.859 1.00 42.81 C ANISOU 2732 C PRO B 699 5577 5012 5677 -40 219 465 C ATOM 2733 O PRO B 699 25.886 28.326 -1.863 1.00 43.54 O ANISOU 2733 O PRO B 699 5715 5139 5687 -28 217 417 O ATOM 2734 CB PRO B 699 28.384 30.030 -2.789 1.00 47.09 C ANISOU 2734 CB PRO B 699 6070 5537 6285 -14 358 613 C ATOM 2735 CG PRO B 699 29.752 29.688 -2.260 1.00 47.70 C ANISOU 2735 CG PRO B 699 6089 5605 6431 -22 408 631 C ATOM 2736 CD PRO B 699 29.497 28.725 -1.138 1.00 48.41 C ANISOU 2736 CD PRO B 699 6178 5710 6506 -43 361 531 C ATOM 2737 N ASN B 700 25.143 30.454 -2.073 1.00 39.61 N ANISOU 2737 N ASN B 700 5175 4588 5288 -45 173 476 N ATOM 2738 CA ASN B 700 23.767 30.085 -2.413 1.00 36.72 C ANISOU 2738 CA ASN B 700 4866 4246 4842 -36 118 436 C ATOM 2739 C ASN B 700 23.033 29.198 -1.402 1.00 34.29 C ANISOU 2739 C ASN B 700 4557 3952 4518 -55 65 342 C ATOM 2740 O ASN B 700 22.150 28.427 -1.772 1.00 33.92 O ANISOU 2740 O ASN B 700 4564 3933 4391 -44 32 310 O ATOM 2741 CB ASN B 700 23.760 29.387 -3.772 1.00 37.51 C ANISOU 2741 CB ASN B 700 5050 4383 4819 6 150 471 C ATOM 2742 CG ASN B 700 24.275 30.275 -4.861 1.00 39.30 C ANISOU 2742 CG ASN B 700 5286 4600 5046 32 202 571 C ATOM 2743 OD1 ASN B 700 23.763 31.381 -5.052 1.00 39.54 O ANISOU 2743 OD1 ASN B 700 5297 4604 5123 26 175 607 O ATOM 2744 ND2 ASN B 700 25.317 29.829 -5.558 1.00 40.72 N ANISOU 2744 ND2 ASN B 700 5493 4800 5180 64 282 621 N ATOM 2745 N SER B 701 23.400 29.282 -0.133 1.00 32.58 N ANISOU 2745 N SER B 701 4283 3717 4378 -81 56 300 N ATOM 2746 CA SER B 701 22.761 28.441 0.861 1.00 30.68 C ANISOU 2746 CA SER B 701 4041 3492 4122 -96 15 219 C ATOM 2747 C SER B 701 22.161 29.307 1.927 1.00 29.20 C ANISOU 2747 C SER B 701 3806 3274 4016 -116 -30 184 C ATOM 2748 O SER B 701 22.659 30.386 2.231 1.00 27.89 O ANISOU 2748 O SER B 701 3597 3068 3932 -126 -27 208 O ATOM 2749 CB SER B 701 23.743 27.450 1.481 1.00 29.86 C ANISOU 2749 CB SER B 701 3928 3404 4014 -101 48 190 C ATOM 2750 OG SER B 701 24.197 26.533 0.508 1.00 29.99 O ANISOU 2750 OG SER B 701 3997 3450 3947 -75 91 214 O ATOM 2751 N TYR B 702 21.071 28.827 2.486 1.00 27.94 N ANISOU 2751 N TYR B 702 3654 3129 3834 -119 -73 129 N ATOM 2752 CA TYR B 702 20.426 29.510 3.571 1.00 26.53 C ANISOU 2752 CA TYR B 702 3436 2925 3720 -129 -110 90 C ATOM 2753 C TYR B 702 20.002 28.411 4.497 1.00 23.56 C ANISOU 2753 C TYR B 702 3062 2577 3314 -134 -124 27 C ATOM 2754 O TYR B 702 20.096 27.229 4.152 1.00 22.91 O ANISOU 2754 O TYR B 702 3011 2527 3166 -132 -113 18 O ATOM 2755 CB TYR B 702 19.230 30.345 3.091 1.00 27.87 C ANISOU 2755 CB TYR B 702 3608 3080 3902 -120 -145 111 C ATOM 2756 CG TYR B 702 19.594 31.396 2.068 1.00 29.00 C ANISOU 2756 CG TYR B 702 3752 3197 4068 -113 -130 182 C ATOM 2757 CD1 TYR B 702 19.663 31.083 0.712 1.00 29.95 C ANISOU 2757 CD1 TYR B 702 3920 3340 4118 -97 -113 235 C ATOM 2758 CD2 TYR B 702 19.881 32.695 2.457 1.00 28.72 C ANISOU 2758 CD2 TYR B 702 3677 3112 4124 -119 -134 199 C ATOM 2759 CE1 TYR B 702 20.006 32.035 -0.229 1.00 30.93 C ANISOU 2759 CE1 TYR B 702 4047 3443 4260 -87 -94 308 C ATOM 2760 CE2 TYR B 702 20.227 33.656 1.527 1.00 29.70 C ANISOU 2760 CE2 TYR B 702 3798 3209 4277 -114 -118 273 C ATOM 2761 CZ TYR B 702 20.287 33.329 0.179 1.00 30.77 C ANISOU 2761 CZ TYR B 702 3978 3373 4341 -97 -95 331 C ATOM 2762 OH TYR B 702 20.633 34.298 -0.757 1.00 31.56 O ANISOU 2762 OH TYR B 702 4077 3448 4466 -87 -73 412 O ATOM 2763 N ALA B 703 19.553 28.781 5.680 1.00 21.23 N ANISOU 2763 N ALA B 703 2735 2266 3064 -138 -146 -17 N ATOM 2764 CA ALA B 703 18.908 27.809 6.528 1.00 20.64 C ANISOU 2764 CA ALA B 703 2662 2219 2962 -137 -159 -68 C ATOM 2765 C ALA B 703 17.731 28.492 7.163 1.00 19.80 C ANISOU 2765 C ALA B 703 2534 2098 2893 -127 -188 -88 C ATOM 2766 O ALA B 703 17.825 29.661 7.584 1.00 19.93 O ANISOU 2766 O ALA B 703 2528 2076 2968 -123 -195 -90 O ATOM 2767 CB ALA B 703 19.870 27.253 7.588 1.00 20.30 C ANISOU 2767 CB ALA B 703 2606 2181 2925 -145 -142 -105 C ATOM 2768 N ILE B 704 16.615 27.790 7.227 1.00 19.71 N ANISOU 2768 N ILE B 704 2525 2110 2852 -123 -205 -102 N ATOM 2769 CA ILE B 704 15.543 28.276 8.061 1.00 20.47 C ANISOU 2769 CA ILE B 704 2594 2197 2986 -108 -221 -124 C ATOM 2770 C ILE B 704 15.663 27.575 9.421 1.00 19.90 C ANISOU 2770 C ILE B 704 2513 2142 2907 -104 -206 -173 C ATOM 2771 O ILE B 704 15.774 26.350 9.505 1.00 19.94 O ANISOU 2771 O ILE B 704 2529 2178 2870 -114 -199 -183 O ATOM 2772 CB ILE B 704 14.155 28.082 7.381 1.00 21.26 C ANISOU 2772 CB ILE B 704 2693 2309 3078 -103 -250 -99 C ATOM 2773 CG1 ILE B 704 13.041 28.513 8.317 1.00 21.31 C ANISOU 2773 CG1 ILE B 704 2662 2306 3128 -83 -256 -117 C ATOM 2774 CG2 ILE B 704 13.941 26.666 6.900 1.00 20.77 C ANISOU 2774 CG2 ILE B 704 2652 2280 2959 -116 -260 -99 C ATOM 2775 CD1 ILE B 704 11.715 28.691 7.597 1.00 21.93 C ANISOU 2775 CD1 ILE B 704 2726 2384 3224 -77 -289 -82 C ATOM 2776 N SER B 705 15.732 28.371 10.481 1.00 20.37 N ANISOU 2776 N SER B 705 2557 2178 3005 -89 -203 -204 N ATOM 2777 CA SER B 705 15.778 27.844 11.840 1.00 19.89 C ANISOU 2777 CA SER B 705 2492 2132 2932 -77 -190 -250 C ATOM 2778 C SER B 705 14.426 28.093 12.493 1.00 20.75 C ANISOU 2778 C SER B 705 2583 2244 3059 -48 -189 -260 C ATOM 2779 O SER B 705 13.995 29.230 12.581 1.00 19.41 O ANISOU 2779 O SER B 705 2403 2042 2930 -29 -196 -260 O ATOM 2780 CB SER B 705 16.885 28.509 12.669 1.00 19.57 C ANISOU 2780 CB SER B 705 2456 2063 2916 -75 -191 -282 C ATOM 2781 OG SER B 705 18.163 28.315 12.099 1.00 19.48 O ANISOU 2781 OG SER B 705 2452 2048 2902 -101 -188 -264 O ATOM 2782 N PHE B 706 13.763 27.055 12.975 1.00 21.39 N ANISOU 2782 N PHE B 706 2654 2359 3112 -42 -176 -266 N ATOM 2783 CA PHE B 706 12.453 27.256 13.554 1.00 22.35 C ANISOU 2783 CA PHE B 706 2751 2484 3257 -12 -167 -265 C ATOM 2784 C PHE B 706 12.181 26.321 14.723 1.00 23.46 C ANISOU 2784 C PHE B 706 2886 2657 3371 5 -139 -286 C ATOM 2785 O PHE B 706 12.916 25.365 14.969 1.00 23.28 O ANISOU 2785 O PHE B 706 2879 2657 3312 -13 -132 -298 O ATOM 2786 CB PHE B 706 11.384 27.061 12.486 1.00 21.35 C ANISOU 2786 CB PHE B 706 2602 2363 3147 -22 -188 -218 C ATOM 2787 CG PHE B 706 11.426 25.711 11.855 1.00 19.70 C ANISOU 2787 CG PHE B 706 2401 2183 2902 -53 -200 -201 C ATOM 2788 CD1 PHE B 706 12.238 25.471 10.777 1.00 19.57 C ANISOU 2788 CD1 PHE B 706 2414 2164 2855 -80 -218 -189 C ATOM 2789 CD2 PHE B 706 10.682 24.668 12.371 1.00 19.28 C ANISOU 2789 CD2 PHE B 706 2325 2155 2844 -51 -191 -197 C ATOM 2790 CE1 PHE B 706 12.299 24.215 10.203 1.00 19.57 C ANISOU 2790 CE1 PHE B 706 2431 2187 2818 -103 -231 -180 C ATOM 2791 CE2 PHE B 706 10.733 23.409 11.807 1.00 19.31 C ANISOU 2791 CE2 PHE B 706 2339 2177 2819 -80 -208 -186 C ATOM 2792 CZ PHE B 706 11.549 23.181 10.718 1.00 19.00 C ANISOU 2792 CZ PHE B 706 2338 2135 2746 -105 -230 -181 C ATOM 2793 N ARG B 707 11.104 26.605 15.438 1.00 24.91 N ANISOU 2793 N ARG B 707 3046 2843 3577 42 -118 -285 N ATOM 2794 CA ARG B 707 10.671 25.759 16.530 1.00 26.86 C ANISOU 2794 CA ARG B 707 3283 3121 3801 64 -82 -293 C ATOM 2795 C ARG B 707 9.443 24.956 16.130 1.00 30.78 C ANISOU 2795 C ARG B 707 3736 3639 4322 57 -80 -245 C ATOM 2796 O ARG B 707 8.512 25.486 15.520 1.00 27.89 O ANISOU 2796 O ARG B 707 3340 3258 4001 62 -94 -214 O ATOM 2797 CB ARG B 707 10.367 26.596 17.757 1.00 27.31 C ANISOU 2797 CB ARG B 707 3348 3168 3862 120 -51 -324 C ATOM 2798 CG ARG B 707 11.519 27.398 18.249 1.00 27.81 C ANISOU 2798 CG ARG B 707 3455 3204 3909 128 -64 -376 C ATOM 2799 CD ARG B 707 11.187 27.914 19.607 1.00 28.96 C ANISOU 2799 CD ARG B 707 3620 3346 4039 188 -33 -413 C ATOM 2800 NE ARG B 707 10.979 26.824 20.549 1.00 29.82 N ANISOU 2800 NE ARG B 707 3729 3498 4102 207 5 -412 N ATOM 2801 CZ ARG B 707 11.817 26.515 21.530 1.00 30.43 C ANISOU 2801 CZ ARG B 707 3847 3588 4128 220 9 -453 C ATOM 2802 NH1 ARG B 707 12.915 27.234 21.723 1.00 30.58 N ANISOU 2802 NH1 ARG B 707 3906 3574 4138 215 -29 -499 N ATOM 2803 NH2 ARG B 707 11.545 25.495 22.330 1.00 30.84 N ANISOU 2803 NH2 ARG B 707 3897 3681 4140 239 46 -442 N ATOM 2804 N ALA B 708 9.451 23.673 16.469 1.00 36.27 N ANISOU 2804 N ALA B 708 4424 4363 4992 44 -67 -237 N ATOM 2805 CA ALA B 708 8.335 22.792 16.178 1.00 41.25 C ANISOU 2805 CA ALA B 708 5010 5009 5654 32 -70 -191 C ATOM 2806 C ALA B 708 8.315 21.674 17.191 1.00 42.50 C ANISOU 2806 C ALA B 708 5161 5197 5789 41 -33 -189 C ATOM 2807 O ALA B 708 9.348 21.087 17.504 1.00 43.30 O ANISOU 2807 O ALA B 708 5297 5310 5844 28 -29 -216 O ATOM 2808 CB ALA B 708 8.426 22.239 14.780 1.00 41.49 C ANISOU 2808 CB ALA B 708 5046 5032 5686 -17 -123 -170 C ATOM 2809 N GLU B 709 7.119 21.401 17.695 1.00 47.65 N ANISOU 2809 N GLU B 709 5763 5860 6480 65 -3 -151 N ATOM 2810 CA GLU B 709 6.893 20.462 18.784 1.00 51.59 C ANISOU 2810 CA GLU B 709 6246 6389 6967 84 45 -136 C ATOM 2811 C GLU B 709 7.939 20.586 19.887 1.00 50.52 C ANISOU 2811 C GLU B 709 6164 6268 6764 113 78 -186 C ATOM 2812 O GLU B 709 8.516 19.590 20.330 1.00 51.62 O ANISOU 2812 O GLU B 709 6318 6428 6868 101 87 -190 O ATOM 2813 CB GLU B 709 6.812 19.033 18.240 1.00 59.93 C ANISOU 2813 CB GLU B 709 7284 7452 8036 35 17 -106 C ATOM 2814 CG GLU B 709 5.378 18.711 17.768 1.00 67.62 C ANISOU 2814 CG GLU B 709 8187 8417 9090 24 2 -43 C ATOM 2815 CD GLU B 709 5.104 17.237 17.507 1.00 74.11 C ANISOU 2815 CD GLU B 709 8982 9240 9935 -17 -22 -9 C ATOM 2816 OE1 GLU B 709 6.065 16.455 17.311 1.00 76.06 O ANISOU 2816 OE1 GLU B 709 9272 9490 10137 -47 -41 -36 O ATOM 2817 OE2 GLU B 709 3.907 16.865 17.530 1.00 77.36 O ANISOU 2817 OE2 GLU B 709 9326 9648 10420 -18 -20 49 O ATOM 2818 N GLY B 710 8.160 21.833 20.309 1.00 48.83 N ANISOU 2818 N GLY B 710 5977 6040 6537 152 90 -222 N ATOM 2819 CA GLY B 710 8.969 22.150 21.467 1.00 48.28 C ANISOU 2819 CA GLY B 710 5958 5978 6407 190 115 -272 C ATOM 2820 C GLY B 710 10.462 22.262 21.248 1.00 41.23 C ANISOU 2820 C GLY B 710 5116 5073 5475 159 74 -319 C ATOM 2821 O GLY B 710 11.175 22.744 22.124 1.00 41.91 O ANISOU 2821 O GLY B 710 5246 5157 5521 188 79 -365 O ATOM 2822 N LYS B 711 10.942 21.823 20.090 1.00 36.54 N ANISOU 2822 N LYS B 711 4518 4471 4896 103 32 -308 N ATOM 2823 CA LYS B 711 12.381 21.733 19.843 1.00 32.61 C ANISOU 2823 CA LYS B 711 4059 3966 4367 72 1 -341 C ATOM 2824 C LYS B 711 12.827 22.659 18.722 1.00 30.37 C ANISOU 2824 C LYS B 711 3783 3648 4110 46 -38 -347 C ATOM 2825 O LYS B 711 12.021 23.053 17.878 1.00 29.74 O ANISOU 2825 O LYS B 711 3678 3555 4067 39 -49 -319 O ATOM 2826 CB LYS B 711 12.762 20.297 19.501 1.00 34.10 C ANISOU 2826 CB LYS B 711 4243 4175 4540 34 -4 -321 C ATOM 2827 CG LYS B 711 12.336 19.303 20.545 1.00 36.16 C ANISOU 2827 CG LYS B 711 4492 4467 4780 55 35 -305 C ATOM 2828 CD LYS B 711 12.614 17.882 20.115 1.00 36.82 C ANISOU 2828 CD LYS B 711 4567 4563 4859 16 25 -282 C ATOM 2829 CE LYS B 711 12.215 16.914 21.217 1.00 36.92 C ANISOU 2829 CE LYS B 711 4567 4605 4856 39 66 -260 C ATOM 2830 NZ LYS B 711 12.368 15.499 20.790 1.00 37.52 N ANISOU 2830 NZ LYS B 711 4632 4686 4939 0 55 -235 N ATOM 2831 N ILE B 712 14.111 22.996 18.703 1.00 28.02 N ANISOU 2831 N ILE B 712 3516 3335 3796 32 -59 -378 N ATOM 2832 CA ILE B 712 14.669 23.812 17.632 1.00 26.36 C ANISOU 2832 CA ILE B 712 3311 3093 3612 6 -90 -375 C ATOM 2833 C ILE B 712 15.177 22.961 16.446 1.00 25.50 C ANISOU 2833 C ILE B 712 3202 2991 3495 -38 -105 -348 C ATOM 2834 O ILE B 712 15.930 22.004 16.631 1.00 25.39 O ANISOU 2834 O ILE B 712 3200 2996 3453 -52 -100 -353 O ATOM 2835 CB ILE B 712 15.813 24.697 18.162 1.00 25.02 C ANISOU 2835 CB ILE B 712 3168 2895 3443 13 -108 -415 C ATOM 2836 CG1 ILE B 712 15.269 25.738 19.142 1.00 24.33 C ANISOU 2836 CG1 ILE B 712 3091 2789 3364 60 -101 -447 C ATOM 2837 CG2 ILE B 712 16.581 25.365 17.017 1.00 24.66 C ANISOU 2837 CG2 ILE B 712 3122 2817 3429 -19 -135 -401 C ATOM 2838 CD1 ILE B 712 16.350 26.572 19.788 1.00 23.86 C ANISOU 2838 CD1 ILE B 712 3063 2695 3306 68 -130 -493 C ATOM 2839 N LYS B 713 14.752 23.324 15.235 1.00 24.83 N ANISOU 2839 N LYS B 713 3108 2892 3433 -54 -123 -319 N ATOM 2840 CA LYS B 713 15.157 22.637 14.016 1.00 24.74 C ANISOU 2840 CA LYS B 713 3108 2885 3406 -87 -137 -295 C ATOM 2841 C LYS B 713 15.846 23.585 13.006 1.00 24.30 C ANISOU 2841 C LYS B 713 3066 2802 3365 -99 -152 -282 C ATOM 2842 O LYS B 713 15.571 24.790 12.966 1.00 24.64 O ANISOU 2842 O LYS B 713 3100 2819 3442 -86 -160 -280 O ATOM 2843 CB LYS B 713 13.948 21.984 13.339 1.00 26.68 C ANISOU 2843 CB LYS B 713 3339 3142 3657 -95 -150 -264 C ATOM 2844 CG LYS B 713 12.965 21.284 14.258 1.00 28.77 C ANISOU 2844 CG LYS B 713 3576 3427 3929 -81 -134 -261 C ATOM 2845 CD LYS B 713 13.563 20.053 14.864 1.00 30.24 C ANISOU 2845 CD LYS B 713 3772 3635 4083 -89 -117 -273 C ATOM 2846 CE LYS B 713 12.466 19.067 15.214 1.00 31.61 C ANISOU 2846 CE LYS B 713 3915 3825 4270 -88 -110 -249 C ATOM 2847 NZ LYS B 713 13.041 17.818 15.781 1.00 31.84 N ANISOU 2847 NZ LYS B 713 3954 3873 4271 -97 -95 -257 N ATOM 2848 N HIS B 714 16.719 23.013 12.182 1.00 23.01 N ANISOU 2848 N HIS B 714 2923 2643 3178 -120 -152 -269 N ATOM 2849 CA HIS B 714 17.367 23.712 11.082 1.00 21.84 C ANISOU 2849 CA HIS B 714 2787 2474 3037 -130 -157 -244 C ATOM 2850 C HIS B 714 17.172 22.950 9.787 1.00 21.33 C ANISOU 2850 C HIS B 714 2747 2422 2936 -142 -165 -216 C ATOM 2851 O HIS B 714 17.293 21.736 9.763 1.00 21.26 O ANISOU 2851 O HIS B 714 2753 2433 2893 -149 -160 -223 O ATOM 2852 CB HIS B 714 18.840 23.888 11.387 1.00 21.01 C ANISOU 2852 CB HIS B 714 2685 2358 2939 -137 -142 -253 C ATOM 2853 CG HIS B 714 19.086 24.510 12.725 1.00 20.31 C ANISOU 2853 CG HIS B 714 2582 2256 2879 -124 -146 -289 C ATOM 2854 ND1 HIS B 714 19.058 25.876 12.920 1.00 20.56 N ANISOU 2854 ND1 HIS B 714 2604 2251 2956 -116 -161 -294 N ATOM 2855 CD2 HIS B 714 19.318 23.961 13.934 1.00 19.94 C ANISOU 2855 CD2 HIS B 714 2535 2224 2818 -116 -142 -323 C ATOM 2856 CE1 HIS B 714 19.283 26.139 14.195 1.00 20.47 C ANISOU 2856 CE1 HIS B 714 2592 2231 2954 -102 -168 -335 C ATOM 2857 NE2 HIS B 714 19.446 24.998 14.836 1.00 20.28 N ANISOU 2857 NE2 HIS B 714 2573 2240 2891 -101 -156 -352 N ATOM 2858 N CYS B 715 16.855 23.665 8.714 1.00 21.73 N ANISOU 2858 N CYS B 715 2807 2458 2992 -142 -180 -184 N ATOM 2859 CA CYS B 715 16.685 23.067 7.384 1.00 21.84 C ANISOU 2859 CA CYS B 715 2857 2481 2962 -147 -194 -158 C ATOM 2860 C CYS B 715 17.526 23.796 6.362 1.00 22.65 C ANISOU 2860 C CYS B 715 2980 2569 3056 -144 -179 -124 C ATOM 2861 O CYS B 715 17.504 25.025 6.327 1.00 22.64 O ANISOU 2861 O CYS B 715 2960 2544 3097 -140 -181 -107 O ATOM 2862 CB CYS B 715 15.228 23.122 6.914 1.00 21.41 C ANISOU 2862 CB CYS B 715 2796 2425 2912 -146 -235 -144 C ATOM 2863 SG CYS B 715 14.118 21.990 7.690 1.00 54.26 S ANISOU 2863 SG CYS B 715 6934 6603 7080 -152 -253 -164 S ATOM 2864 N ARG B 716 18.211 23.050 5.497 1.00 24.04 N ANISOU 2864 N ARG B 716 3198 2757 3181 -144 -163 -111 N ATOM 2865 CA ARG B 716 18.926 23.659 4.381 1.00 24.90 C ANISOU 2865 CA ARG B 716 3331 2855 3273 -135 -143 -67 C ATOM 2866 C ARG B 716 17.972 24.216 3.326 1.00 23.88 C ANISOU 2866 C ARG B 716 3224 2720 3127 -127 -177 -35 C ATOM 2867 O ARG B 716 16.956 23.615 3.025 1.00 22.72 O ANISOU 2867 O ARG B 716 3095 2583 2953 -129 -218 -46 O ATOM 2868 CB ARG B 716 19.843 22.654 3.722 1.00 27.77 C ANISOU 2868 CB ARG B 716 3738 3236 3578 -126 -110 -61 C ATOM 2869 CG ARG B 716 20.960 22.155 4.570 1.00 30.62 C ANISOU 2869 CG ARG B 716 4077 3600 3956 -131 -73 -80 C ATOM 2870 CD ARG B 716 21.836 21.276 3.712 1.00 33.83 C ANISOU 2870 CD ARG B 716 4529 4019 4304 -115 -35 -65 C ATOM 2871 NE ARG B 716 23.033 20.864 4.417 1.00 36.28 N ANISOU 2871 NE ARG B 716 4814 4332 4638 -118 5 -72 N ATOM 2872 CZ ARG B 716 23.081 19.823 5.242 1.00 37.63 C ANISOU 2872 CZ ARG B 716 4979 4514 4803 -125 0 -111 C ATOM 2873 NH1 ARG B 716 21.988 19.097 5.462 1.00 39.01 N ANISOU 2873 NH1 ARG B 716 5170 4699 4953 -131 -39 -143 N ATOM 2874 NH2 ARG B 716 24.222 19.508 5.843 1.00 38.41 N ANISOU 2874 NH2 ARG B 716 5054 4614 4927 -125 34 -112 N ATOM 2875 N VAL B 717 18.322 25.362 2.756 1.00 23.52 N ANISOU 2875 N VAL B 717 3175 2657 3105 -119 -164 7 N ATOM 2876 CA VAL B 717 17.571 25.951 1.655 1.00 23.83 C ANISOU 2876 CA VAL B 717 3239 2690 3124 -109 -194 47 C ATOM 2877 C VAL B 717 18.545 26.375 0.554 1.00 24.74 C ANISOU 2877 C VAL B 717 3389 2803 3209 -92 -153 101 C ATOM 2878 O VAL B 717 19.366 27.260 0.742 1.00 25.12 O ANISOU 2878 O VAL B 717 3406 2831 3310 -93 -118 129 O ATOM 2879 CB VAL B 717 16.724 27.161 2.114 1.00 21.97 C ANISOU 2879 CB VAL B 717 2958 2429 2961 -111 -222 53 C ATOM 2880 CG1 VAL B 717 16.177 27.884 0.927 1.00 21.34 C ANISOU 2880 CG1 VAL B 717 2902 2340 2866 -99 -247 105 C ATOM 2881 CG2 VAL B 717 15.586 26.707 2.991 1.00 16.71 C ANISOU 2881 CG2 VAL B 717 2263 1769 2316 -119 -258 12 C ATOM 2882 N GLN B 718 18.457 25.741 -0.603 1.00 27.48 N ANISOU 2882 N GLN B 718 3802 3168 3472 -74 -158 119 N ATOM 2883 CA GLN B 718 19.433 25.984 -1.640 1.00 30.13 C ANISOU 2883 CA GLN B 718 4176 3507 3765 -50 -107 173 C ATOM 2884 C GLN B 718 18.817 26.858 -2.722 1.00 31.63 C ANISOU 2884 C GLN B 718 4394 3689 3933 -34 -132 226 C ATOM 2885 O GLN B 718 17.651 26.714 -3.065 1.00 31.82 O ANISOU 2885 O GLN B 718 4441 3717 3931 -34 -196 215 O ATOM 2886 CB GLN B 718 19.944 24.655 -2.209 1.00 32.86 C ANISOU 2886 CB GLN B 718 4588 3879 4020 -31 -83 157 C ATOM 2887 CG GLN B 718 20.946 24.773 -3.372 1.00 35.88 C ANISOU 2887 CG GLN B 718 5022 4270 4343 5 -19 215 C ATOM 2888 CD GLN B 718 22.341 25.304 -2.977 1.00 37.66 C ANISOU 2888 CD GLN B 718 5194 4484 4633 5 59 253 C ATOM 2889 OE1 GLN B 718 22.675 25.445 -1.791 1.00 39.81 O ANISOU 2889 OE1 GLN B 718 5397 4742 4986 -24 61 226 O ATOM 2890 NE2 GLN B 718 23.165 25.582 -3.988 1.00 39.05 N ANISOU 2890 NE2 GLN B 718 5401 4664 4771 38 122 319 N ATOM 2891 N GLN B 719 19.600 27.799 -3.229 1.00 32.92 N ANISOU 2891 N GLN B 719 4550 3840 4118 -20 -84 289 N ATOM 2892 CA GLN B 719 19.190 28.577 -4.377 1.00 34.71 C ANISOU 2892 CA GLN B 719 4813 4063 4314 2 -97 351 C ATOM 2893 C GLN B 719 19.966 28.100 -5.584 1.00 35.43 C ANISOU 2893 C GLN B 719 4979 4177 4304 40 -45 394 C ATOM 2894 O GLN B 719 21.119 27.694 -5.470 1.00 35.09 O ANISOU 2894 O GLN B 719 4933 4141 4258 49 24 401 O ATOM 2895 CB GLN B 719 19.432 30.057 -4.149 1.00 36.81 C ANISOU 2895 CB GLN B 719 5016 4293 4677 -7 -80 401 C ATOM 2896 CG GLN B 719 19.230 30.917 -5.376 1.00 39.16 C ANISOU 2896 CG GLN B 719 5348 4584 4946 19 -79 480 C ATOM 2897 CD GLN B 719 19.637 32.345 -5.134 1.00 40.88 C ANISOU 2897 CD GLN B 719 5502 4760 5271 9 -55 534 C ATOM 2898 OE1 GLN B 719 20.383 32.644 -4.192 1.00 41.67 O ANISOU 2898 OE1 GLN B 719 5539 4835 5457 -14 -27 519 O ATOM 2899 NE2 GLN B 719 19.156 33.246 -5.982 1.00 42.62 N ANISOU 2899 NE2 GLN B 719 5737 4968 5489 25 -72 597 N ATOM 2900 N GLU B 720 19.317 28.119 -6.736 1.00 36.79 N ANISOU 2900 N GLU B 720 5222 4361 4394 67 -79 423 N ATOM 2901 CA GLU B 720 19.962 27.789 -7.989 1.00 38.33 C ANISOU 2901 CA GLU B 720 5503 4579 4481 115 -29 469 C ATOM 2902 C GLU B 720 19.203 28.510 -9.095 1.00 35.75 C ANISOU 2902 C GLU B 720 5226 4252 4105 139 -70 524 C ATOM 2903 O GLU B 720 18.014 28.275 -9.312 1.00 33.03 O ANISOU 2903 O GLU B 720 4912 3911 3728 133 -160 493 O ATOM 2904 CB GLU B 720 19.985 26.284 -8.206 1.00 43.21 C ANISOU 2904 CB GLU B 720 6195 5223 5000 131 -39 410 C ATOM 2905 CG GLU B 720 20.862 25.834 -9.339 1.00 47.77 C ANISOU 2905 CG GLU B 720 6861 5822 5466 187 31 449 C ATOM 2906 CD GLU B 720 20.422 24.491 -9.893 1.00 53.46 C ANISOU 2906 CD GLU B 720 7684 6560 6066 211 -15 390 C ATOM 2907 OE1 GLU B 720 20.109 23.578 -9.084 1.00 55.89 O ANISOU 2907 OE1 GLU B 720 7974 6865 6397 180 -55 315 O ATOM 2908 OE2 GLU B 720 20.396 24.348 -11.139 1.00 56.71 O ANISOU 2908 OE2 GLU B 720 8199 6988 6360 261 -12 419 O ATOM 2909 N GLY B 721 19.894 29.422 -9.758 1.00 34.57 N ANISOU 2909 N GLY B 721 5078 4099 3960 165 -6 611 N ATOM 2910 CA GLY B 721 19.296 30.217 -10.797 1.00 34.08 C ANISOU 2910 CA GLY B 721 5057 4035 3855 191 -36 675 C ATOM 2911 C GLY B 721 18.144 31.010 -10.242 1.00 31.06 C ANISOU 2911 C GLY B 721 4613 3624 3563 154 -119 662 C ATOM 2912 O GLY B 721 18.311 31.839 -9.360 1.00 30.72 O ANISOU 2912 O GLY B 721 4479 3551 3644 123 -104 668 O ATOM 2913 N GLN B 722 16.956 30.717 -10.748 1.00 30.32 N ANISOU 2913 N GLN B 722 4571 3541 3409 160 -210 641 N ATOM 2914 CA GLN B 722 15.780 31.486 -10.433 1.00 29.23 C ANISOU 2914 CA GLN B 722 4381 3378 3347 135 -289 641 C ATOM 2915 C GLN B 722 14.895 30.785 -9.406 1.00 28.59 C ANISOU 2915 C GLN B 722 4257 3293 3314 97 -358 553 C ATOM 2916 O GLN B 722 13.709 31.088 -9.287 1.00 27.92 O ANISOU 2916 O GLN B 722 4146 3195 3268 83 -437 545 O ATOM 2917 CB GLN B 722 15.014 31.744 -11.720 1.00 32.00 C ANISOU 2917 CB GLN B 722 4809 3739 3611 168 -350 690 C ATOM 2918 CG GLN B 722 14.533 33.144 -11.844 1.00 33.84 C ANISOU 2918 CG GLN B 722 4992 3943 3922 166 -368 757 C ATOM 2919 CD GLN B 722 15.655 34.137 -11.964 1.00 34.27 C ANISOU 2919 CD GLN B 722 5014 3981 4024 178 -270 835 C ATOM 2920 OE1 GLN B 722 16.763 33.806 -12.404 1.00 34.45 O ANISOU 2920 OE1 GLN B 722 5079 4024 3988 204 -188 864 O ATOM 2921 NE2 GLN B 722 15.382 35.368 -11.554 1.00 35.06 N ANISOU 2921 NE2 GLN B 722 5038 4042 4242 161 -277 872 N ATOM 2922 N THR B 723 15.470 29.852 -8.656 1.00 28.05 N ANISOU 2922 N THR B 723 4177 3235 3247 81 -324 493 N ATOM 2923 CA THR B 723 14.664 28.969 -7.832 1.00 27.90 C ANISOU 2923 CA THR B 723 4133 3217 3250 51 -385 415 C ATOM 2924 C THR B 723 15.282 28.750 -6.463 1.00 26.59 C ANISOU 2924 C THR B 723 3895 3044 3164 23 -335 368 C ATOM 2925 O THR B 723 16.490 28.559 -6.360 1.00 25.85 O ANISOU 2925 O THR B 723 3806 2957 3060 30 -259 374 O ATOM 2926 CB THR B 723 14.463 27.575 -8.529 1.00 22.58 C ANISOU 2926 CB THR B 723 3554 2569 2458 66 -426 375 C ATOM 2927 OG1 THR B 723 13.850 27.748 -9.817 1.00 22.92 O ANISOU 2927 OG1 THR B 723 3674 2617 2416 95 -485 414 O ATOM 2928 CG2 THR B 723 13.606 26.626 -7.678 1.00 22.07 C ANISOU 2928 CG2 THR B 723 3457 2501 2427 32 -491 301 C ATOM 2929 N VAL B 724 14.467 28.775 -5.412 1.00 26.03 N ANISOU 2929 N VAL B 724 3756 2959 3174 -7 -376 325 N ATOM 2930 CA VAL B 724 14.929 28.298 -4.110 1.00 25.34 C ANISOU 2930 CA VAL B 724 3617 2871 3141 -30 -341 270 C ATOM 2931 C VAL B 724 14.256 26.944 -3.820 1.00 23.78 C ANISOU 2931 C VAL B 724 3437 2690 2908 -44 -390 210 C ATOM 2932 O VAL B 724 13.132 26.709 -4.245 1.00 24.02 O ANISOU 2932 O VAL B 724 3483 2720 2921 -46 -465 208 O ATOM 2933 CB VAL B 724 14.657 29.340 -2.984 1.00 23.03 C ANISOU 2933 CB VAL B 724 3236 2550 2966 -48 -337 265 C ATOM 2934 CG1 VAL B 724 15.161 30.720 -3.419 1.00 23.00 C ANISOU 2934 CG1 VAL B 724 3216 2519 3001 -36 -305 330 C ATOM 2935 CG2 VAL B 724 13.192 29.407 -2.622 1.00 23.08 C ANISOU 2935 CG2 VAL B 724 3208 2548 3013 -58 -407 246 C ATOM 2936 N MET B 725 14.965 26.044 -3.141 1.00 23.15 N ANISOU 2936 N MET B 725 3354 2622 2820 -53 -352 167 N ATOM 2937 CA MET B 725 14.476 24.686 -2.893 1.00 23.32 C ANISOU 2937 CA MET B 725 3395 2656 2809 -65 -391 114 C ATOM 2938 C MET B 725 14.499 24.342 -1.408 1.00 24.73 C ANISOU 2938 C MET B 725 3505 2833 3058 -90 -372 68 C ATOM 2939 O MET B 725 15.450 24.666 -0.697 1.00 23.23 O ANISOU 2939 O MET B 725 3282 2640 2903 -92 -312 64 O ATOM 2940 CB MET B 725 15.306 23.638 -3.657 1.00 23.83 C ANISOU 2940 CB MET B 725 3543 2737 2774 -45 -366 103 C ATOM 2941 CG MET B 725 15.311 23.748 -5.202 1.00 24.92 C ANISOU 2941 CG MET B 725 3771 2881 2814 -12 -383 142 C ATOM 2942 SD MET B 725 16.657 24.760 -5.904 1.00123.53 S ANISOU 2942 SD MET B 725 16280 15375 15280 23 -287 213 S ATOM 2943 CE MET B 725 17.945 23.571 -6.318 1.00 23.01 C ANISOU 2943 CE MET B 725 3621 2664 2457 54 -216 196 C ATOM 2944 N LEU B 726 13.455 23.665 -0.951 1.00 26.27 N ANISOU 2944 N LEU B 726 3680 3028 3275 -107 -427 37 N ATOM 2945 CA LEU B 726 13.382 23.162 0.406 1.00 27.11 C ANISOU 2945 CA LEU B 726 3729 3136 3433 -126 -410 -3 C ATOM 2946 C LEU B 726 12.693 21.808 0.373 1.00 29.00 C ANISOU 2946 C LEU B 726 3988 3381 3649 -139 -460 -33 C ATOM 2947 O LEU B 726 11.503 21.720 0.057 1.00 30.43 O ANISOU 2947 O LEU B 726 4161 3554 3846 -148 -529 -25 O ATOM 2948 CB LEU B 726 12.628 24.129 1.303 1.00 25.43 C ANISOU 2948 CB LEU B 726 3442 2910 3309 -131 -415 3 C ATOM 2949 CG LEU B 726 12.320 23.580 2.695 1.00 23.51 C ANISOU 2949 CG LEU B 726 3145 2672 3114 -143 -403 -35 C ATOM 2950 CD1 LEU B 726 13.613 23.171 3.414 1.00 22.06 C ANISOU 2950 CD1 LEU B 726 2966 2499 2917 -145 -342 -64 C ATOM 2951 CD2 LEU B 726 11.569 24.617 3.503 1.00 22.86 C ANISOU 2951 CD2 LEU B 726 2998 2576 3111 -138 -402 -28 C ATOM 2952 N GLY B 727 13.437 20.749 0.676 1.00 30.73 N ANISOU 2952 N GLY B 727 4230 3610 3835 -143 -431 -65 N ATOM 2953 CA GLY B 727 12.965 19.400 0.418 1.00 33.13 C ANISOU 2953 CA GLY B 727 4569 3912 4106 -153 -479 -92 C ATOM 2954 C GLY B 727 12.589 19.205 -1.044 1.00 36.28 C ANISOU 2954 C GLY B 727 5047 4304 4434 -142 -541 -80 C ATOM 2955 O GLY B 727 13.436 19.272 -1.941 1.00 38.57 O ANISOU 2955 O GLY B 727 5406 4601 4649 -116 -512 -70 O ATOM 2956 N ASN B 728 11.303 18.984 -1.289 1.00 38.14 N ANISOU 2956 N ASN B 728 5271 4526 4694 -158 -626 -77 N ATOM 2957 CA ASN B 728 10.804 18.751 -2.646 1.00 40.11 C ANISOU 2957 CA ASN B 728 5598 4765 4877 -148 -704 -69 C ATOM 2958 C ASN B 728 10.097 19.968 -3.206 1.00 39.97 C ANISOU 2958 C ASN B 728 5565 4744 4880 -141 -742 -23 C ATOM 2959 O ASN B 728 9.580 19.939 -4.316 1.00 39.07 O ANISOU 2959 O ASN B 728 5510 4621 4714 -132 -815 -10 O ATOM 2960 CB ASN B 728 9.856 17.549 -2.668 1.00 42.07 C ANISOU 2960 CB ASN B 728 5852 4993 5141 -174 -793 -96 C ATOM 2961 CG ASN B 728 10.530 16.285 -2.186 1.00 43.59 C ANISOU 2961 CG ASN B 728 6066 5185 5313 -180 -761 -140 C ATOM 2962 OD1 ASN B 728 11.688 16.026 -2.530 1.00 43.70 O ANISOU 2962 OD1 ASN B 728 6142 5209 5253 -154 -704 -155 O ATOM 2963 ND2 ASN B 728 9.830 15.507 -1.354 1.00 44.67 N ANISOU 2963 ND2 ASN B 728 6145 5308 5521 -211 -792 -155 N ATOM 2964 N SER B 729 10.082 21.041 -2.430 1.00 39.25 N ANISOU 2964 N SER B 729 5397 4656 4861 -143 -694 0 N ATOM 2965 CA SER B 729 9.369 22.244 -2.818 1.00 39.38 C ANISOU 2965 CA SER B 729 5385 4663 4913 -136 -726 46 C ATOM 2966 C SER B 729 10.305 23.264 -3.435 1.00 39.04 C ANISOU 2966 C SER B 729 5379 4628 4827 -108 -670 80 C ATOM 2967 O SER B 729 11.456 23.417 -3.012 1.00 38.92 O ANISOU 2967 O SER B 729 5361 4621 4804 -100 -587 73 O ATOM 2968 CB SER B 729 8.654 22.837 -1.613 1.00 37.68 C ANISOU 2968 CB SER B 729 5065 4441 4809 -150 -713 52 C ATOM 2969 OG SER B 729 7.870 21.830 -0.996 1.00 36.57 O ANISOU 2969 OG SER B 729 4886 4296 4711 -174 -752 28 O ATOM 2970 N GLU B 730 9.790 23.954 -4.445 1.00 40.45 N ANISOU 2970 N GLU B 730 5588 4800 4982 -94 -719 121 N ATOM 2971 CA GLU B 730 10.565 24.891 -5.231 1.00 42.07 C ANISOU 2971 CA GLU B 730 5834 5009 5141 -65 -675 166 C ATOM 2972 C GLU B 730 9.781 26.184 -5.302 1.00 37.85 C ANISOU 2972 C GLU B 730 5248 4459 4674 -62 -702 213 C ATOM 2973 O GLU B 730 8.567 26.160 -5.388 1.00 36.54 O ANISOU 2973 O GLU B 730 5057 4283 4545 -74 -783 219 O ATOM 2974 CB GLU B 730 10.825 24.328 -6.623 1.00 50.33 C ANISOU 2974 CB GLU B 730 6995 6066 6063 -38 -706 173 C ATOM 2975 CG GLU B 730 9.721 23.351 -7.040 1.00 59.02 C ANISOU 2975 CG GLU B 730 8129 7157 7139 -53 -818 144 C ATOM 2976 CD GLU B 730 10.089 22.436 -8.207 1.00 69.46 C ANISOU 2976 CD GLU B 730 9576 8486 8329 -26 -850 126 C ATOM 2977 OE1 GLU B 730 10.670 22.939 -9.200 1.00 70.63 O ANISOU 2977 OE1 GLU B 730 9798 8646 8393 12 -821 163 O ATOM 2978 OE2 GLU B 730 9.772 21.217 -8.124 1.00 75.54 O ANISOU 2978 OE2 GLU B 730 10373 9248 9081 -42 -903 76 O ATOM 2979 N PHE B 731 10.473 27.315 -5.247 1.00 34.20 N ANISOU 2979 N PHE B 731 4766 3991 4237 -48 -638 250 N ATOM 2980 CA PHE B 731 9.828 28.620 -5.233 1.00 30.55 C ANISOU 2980 CA PHE B 731 4253 3509 3848 -44 -655 295 C ATOM 2981 C PHE B 731 10.629 29.588 -6.055 1.00 28.26 C ANISOU 2981 C PHE B 731 3998 3214 3524 -18 -611 354 C ATOM 2982 O PHE B 731 11.771 29.298 -6.378 1.00 29.28 O ANISOU 2982 O PHE B 731 4175 3358 3592 -6 -550 356 O ATOM 2983 CB PHE B 731 9.678 29.114 -3.801 1.00 27.50 C ANISOU 2983 CB PHE B 731 3771 3106 3572 -60 -619 272 C ATOM 2984 CG PHE B 731 8.948 28.142 -2.921 1.00 24.82 C ANISOU 2984 CG PHE B 731 3392 2773 3267 -81 -648 222 C ATOM 2985 CD1 PHE B 731 7.562 28.122 -2.892 1.00 20.23 C ANISOU 2985 CD1 PHE B 731 2770 2182 2735 -89 -721 232 C ATOM 2986 CD2 PHE B 731 9.646 27.228 -2.147 1.00 22.47 C ANISOU 2986 CD2 PHE B 731 3095 2489 2954 -93 -603 173 C ATOM 2987 CE1 PHE B 731 6.881 27.205 -2.100 1.00 21.07 C ANISOU 2987 CE1 PHE B 731 2834 2292 2879 -108 -744 196 C ATOM 2988 CE2 PHE B 731 8.972 26.310 -1.352 1.00 21.52 C ANISOU 2988 CE2 PHE B 731 2937 2373 2865 -112 -627 134 C ATOM 2989 CZ PHE B 731 7.584 26.298 -1.329 1.00 19.42 C ANISOU 2989 CZ PHE B 731 2629 2097 2652 -120 -696 148 C ATOM 2990 N ASP B 732 10.028 30.722 -6.423 1.00 27.67 N ANISOU 2990 N ASP B 732 3900 3121 3494 -9 -639 406 N ATOM 2991 CA ASP B 732 10.755 31.783 -7.129 1.00 27.08 C ANISOU 2991 CA ASP B 732 3847 3037 3407 15 -593 472 C ATOM 2992 C ASP B 732 11.758 32.508 -6.218 1.00 26.64 C ANISOU 2992 C ASP B 732 3734 2960 3428 7 -506 471 C ATOM 2993 O ASP B 732 12.810 32.947 -6.664 1.00 26.27 O ANISOU 2993 O ASP B 732 3710 2912 3361 21 -445 513 O ATOM 2994 CB ASP B 732 9.776 32.804 -7.721 1.00 29.48 C ANISOU 2994 CB ASP B 732 4136 3320 3745 27 -652 530 C ATOM 2995 CG ASP B 732 9.126 32.324 -9.024 1.00 32.18 C ANISOU 2995 CG ASP B 732 4560 3681 3987 44 -733 555 C ATOM 2996 OD1 ASP B 732 9.643 31.364 -9.641 1.00 32.43 O ANISOU 2996 OD1 ASP B 732 4674 3738 3908 55 -729 536 O ATOM 2997 OD2 ASP B 732 8.099 32.911 -9.442 1.00 33.66 O ANISOU 2997 OD2 ASP B 732 4732 3854 4203 50 -804 592 O ATOM 2998 N SER B 733 11.430 32.629 -4.939 1.00 25.74 N ANISOU 2998 N SER B 733 3546 2830 3405 -13 -503 425 N ATOM 2999 CA SER B 733 12.195 33.466 -4.039 1.00 25.30 C ANISOU 2999 CA SER B 733 3435 2745 3433 -20 -442 422 C ATOM 3000 C SER B 733 12.058 32.995 -2.603 1.00 23.70 C ANISOU 3000 C SER B 733 3180 2541 3284 -39 -433 350 C ATOM 3001 O SER B 733 11.182 32.182 -2.294 1.00 23.85 O ANISOU 3001 O SER B 733 3193 2578 3293 -47 -475 313 O ATOM 3002 CB SER B 733 11.728 34.907 -4.150 1.00 24.69 C ANISOU 3002 CB SER B 733 3319 2628 3435 -10 -456 472 C ATOM 3003 OG SER B 733 10.375 35.018 -3.739 1.00 24.12 O ANISOU 3003 OG SER B 733 3206 2546 3412 -11 -514 454 O ATOM 3004 N LEU B 734 12.924 33.497 -1.725 1.00 22.38 N ANISOU 3004 N LEU B 734 2977 2352 3175 -46 -381 332 N ATOM 3005 CA LEU B 734 12.804 33.181 -0.304 1.00 21.92 C ANISOU 3005 CA LEU B 734 2874 2291 3166 -58 -372 265 C ATOM 3006 C LEU B 734 11.507 33.754 0.274 1.00 23.12 C ANISOU 3006 C LEU B 734 2977 2422 3386 -50 -409 255 C ATOM 3007 O LEU B 734 10.865 33.119 1.101 1.00 21.79 O ANISOU 3007 O LEU B 734 2784 2267 3228 -54 -421 210 O ATOM 3008 CB LEU B 734 13.993 33.714 0.482 1.00 21.92 C ANISOU 3008 CB LEU B 734 2848 2264 3215 -66 -320 250 C ATOM 3009 CG LEU B 734 15.290 32.925 0.463 1.00 22.52 C ANISOU 3009 CG LEU B 734 2951 2363 3245 -76 -275 239 C ATOM 3010 CD1 LEU B 734 16.385 33.788 1.046 1.00 22.15 C ANISOU 3010 CD1 LEU B 734 2870 2277 3268 -83 -238 244 C ATOM 3011 CD2 LEU B 734 15.137 31.626 1.248 1.00 22.65 C ANISOU 3011 CD2 LEU B 734 2969 2411 3224 -86 -278 175 C ATOM 3012 N VAL B 735 11.138 34.959 -0.150 1.00 24.77 N ANISOU 3012 N VAL B 735 3170 2597 3645 -37 -424 302 N ATOM 3013 CA VAL B 735 9.919 35.595 0.340 1.00 25.94 C ANISOU 3013 CA VAL B 735 3270 2721 3864 -23 -455 299 C ATOM 3014 C VAL B 735 8.707 34.734 -0.017 1.00 27.07 C ANISOU 3014 C VAL B 735 3414 2895 3976 -24 -509 301 C ATOM 3015 O VAL B 735 7.818 34.554 0.802 1.00 26.85 O ANISOU 3015 O VAL B 735 3342 2867 3992 -18 -519 273 O ATOM 3016 CB VAL B 735 9.763 37.022 -0.227 1.00 25.04 C ANISOU 3016 CB VAL B 735 3144 2563 3807 -7 -465 358 C ATOM 3017 CG1 VAL B 735 8.399 37.556 0.037 1.00 24.32 C ANISOU 3017 CG1 VAL B 735 3009 2453 3780 12 -502 365 C ATOM 3018 CG2 VAL B 735 10.758 37.942 0.417 1.00 25.75 C ANISOU 3018 CG2 VAL B 735 3217 2609 3958 -8 -421 347 C ATOM 3019 N ASP B 736 8.701 34.172 -1.224 1.00 29.56 N ANISOU 3019 N ASP B 736 3781 3236 4215 -28 -542 334 N ATOM 3020 CA ASP B 736 7.663 33.223 -1.644 1.00 31.11 C ANISOU 3020 CA ASP B 736 3986 3458 4377 -35 -605 332 C ATOM 3021 C ASP B 736 7.649 31.938 -0.837 1.00 28.16 C ANISOU 3021 C ASP B 736 3604 3110 3984 -52 -596 273 C ATOM 3022 O ASP B 736 6.589 31.395 -0.548 1.00 28.40 O ANISOU 3022 O ASP B 736 3602 3147 4041 -57 -637 264 O ATOM 3023 CB ASP B 736 7.825 32.855 -3.113 1.00 34.81 C ANISOU 3023 CB ASP B 736 4528 3945 4752 -33 -644 372 C ATOM 3024 CG ASP B 736 7.221 33.877 -4.037 1.00 38.28 C ANISOU 3024 CG ASP B 736 4970 4365 5210 -15 -687 439 C ATOM 3025 OD1 ASP B 736 6.365 34.678 -3.595 1.00 40.92 O ANISOU 3025 OD1 ASP B 736 5242 4671 5633 -7 -704 454 O ATOM 3026 OD2 ASP B 736 7.604 33.872 -5.224 1.00 43.45 O ANISOU 3026 OD2 ASP B 736 5692 5031 5787 -5 -701 480 O ATOM 3027 N LEU B 737 8.829 31.433 -0.508 1.00 25.39 N ANISOU 3027 N LEU B 737 3283 2774 3591 -61 -544 240 N ATOM 3028 CA LEU B 737 8.941 30.234 0.298 1.00 23.17 C ANISOU 3028 CA LEU B 737 2995 2515 3292 -76 -530 186 C ATOM 3029 C LEU B 737 8.342 30.456 1.694 1.00 23.48 C ANISOU 3029 C LEU B 737 2966 2544 3412 -71 -511 155 C ATOM 3030 O LEU B 737 7.613 29.607 2.205 1.00 21.25 O ANISOU 3030 O LEU B 737 2657 2277 3140 -79 -528 134 O ATOM 3031 CB LEU B 737 10.403 29.811 0.382 1.00 22.44 C ANISOU 3031 CB LEU B 737 2943 2436 3147 -82 -474 164 C ATOM 3032 CG LEU B 737 10.861 28.584 1.166 1.00 22.41 C ANISOU 3032 CG LEU B 737 2943 2455 3117 -97 -449 111 C ATOM 3033 CD1 LEU B 737 12.211 28.141 0.631 1.00 22.40 C ANISOU 3033 CD1 LEU B 737 2996 2467 3047 -98 -410 111 C ATOM 3034 CD2 LEU B 737 10.980 28.880 2.651 1.00 22.02 C ANISOU 3034 CD2 LEU B 737 2840 2397 3131 -96 -409 73 C ATOM 3035 N ILE B 738 8.633 31.607 2.292 1.00 24.41 N ANISOU 3035 N ILE B 738 3056 2634 3586 -56 -475 154 N ATOM 3036 CA ILE B 738 8.198 31.906 3.646 1.00 25.08 C ANISOU 3036 CA ILE B 738 3088 2707 3736 -42 -448 120 C ATOM 3037 C ILE B 738 6.705 32.137 3.681 1.00 24.10 C ANISOU 3037 C ILE B 738 2915 2575 3667 -27 -484 145 C ATOM 3038 O ILE B 738 5.990 31.588 4.523 1.00 24.53 O ANISOU 3038 O ILE B 738 2930 2641 3748 -22 -477 125 O ATOM 3039 CB ILE B 738 8.935 33.144 4.207 1.00 18.58 C ANISOU 3039 CB ILE B 738 2257 1846 2958 -28 -409 110 C ATOM 3040 CG1 ILE B 738 10.412 32.828 4.401 1.00 18.20 C ANISOU 3040 CG1 ILE B 738 2242 1804 2870 -44 -372 84 C ATOM 3041 CG2 ILE B 738 8.344 33.575 5.532 1.00 18.58 C ANISOU 3041 CG2 ILE B 738 2212 1829 3019 -3 -386 75 C ATOM 3042 CD1 ILE B 738 10.623 31.576 5.200 1.00 17.72 C ANISOU 3042 CD1 ILE B 738 2184 1778 2771 -55 -354 36 C ATOM 3043 N SER B 739 6.241 32.962 2.754 1.00 24.21 N ANISOU 3043 N SER B 739 2928 2568 3703 -19 -521 195 N ATOM 3044 CA SER B 739 4.821 33.249 2.569 1.00 23.94 C ANISOU 3044 CA SER B 739 2846 2524 3726 -5 -564 231 C ATOM 3045 C SER B 739 3.979 31.969 2.381 1.00 24.77 C ANISOU 3045 C SER B 739 2939 2659 3816 -24 -611 234 C ATOM 3046 O SER B 739 2.872 31.833 2.911 1.00 25.71 O ANISOU 3046 O SER B 739 2995 2775 3996 -14 -622 244 O ATOM 3047 CB SER B 739 4.671 34.181 1.377 1.00 25.66 C ANISOU 3047 CB SER B 739 3080 2719 3949 2 -605 289 C ATOM 3048 OG SER B 739 3.327 34.325 1.015 1.00 27.58 O ANISOU 3048 OG SER B 739 3282 2956 4242 11 -660 330 O ATOM 3049 N TYR B 740 4.526 31.019 1.637 1.00 23.30 N ANISOU 3049 N TYR B 740 2808 2495 3548 -50 -637 228 N ATOM 3050 CA TYR B 740 3.898 29.724 1.446 1.00 25.26 C ANISOU 3050 CA TYR B 740 3055 2765 3777 -72 -686 223 C ATOM 3051 C TYR B 740 3.821 28.932 2.762 1.00 25.11 C ANISOU 3051 C TYR B 740 2996 2760 3783 -76 -641 182 C ATOM 3052 O TYR B 740 2.777 28.365 3.089 1.00 24.46 O ANISOU 3052 O TYR B 740 2862 2682 3751 -81 -668 194 O ATOM 3053 CB TYR B 740 4.665 28.952 0.369 1.00 25.54 C ANISOU 3053 CB TYR B 740 3174 2818 3712 -91 -716 218 C ATOM 3054 CG TYR B 740 4.134 27.590 0.015 1.00 25.37 C ANISOU 3054 CG TYR B 740 3167 2810 3662 -116 -778 208 C ATOM 3055 CD1 TYR B 740 3.089 27.432 -0.904 1.00 25.35 C ANISOU 3055 CD1 TYR B 740 3165 2799 3670 -123 -873 245 C ATOM 3056 CD2 TYR B 740 4.697 26.444 0.580 1.00 23.81 C ANISOU 3056 CD2 TYR B 740 2986 2630 3429 -132 -749 162 C ATOM 3057 CE1 TYR B 740 2.604 26.159 -1.230 1.00 24.43 C ANISOU 3057 CE1 TYR B 740 3063 2687 3533 -149 -941 233 C ATOM 3058 CE2 TYR B 740 4.232 25.172 0.263 1.00 21.75 C ANISOU 3058 CE2 TYR B 740 2740 2375 3148 -156 -809 152 C ATOM 3059 CZ TYR B 740 3.192 25.033 -0.643 1.00 22.87 C ANISOU 3059 CZ TYR B 740 2882 2503 3304 -165 -907 185 C ATOM 3060 OH TYR B 740 2.753 23.756 -0.945 1.00 23.25 O ANISOU 3060 OH TYR B 740 2946 2549 3338 -191 -975 172 O ATOM 3061 N TYR B 741 4.897 28.907 3.544 1.00 26.62 N ANISOU 3061 N TYR B 741 3207 2960 3948 -72 -573 139 N ATOM 3062 CA TYR B 741 4.885 28.048 4.728 1.00 28.64 C ANISOU 3062 CA TYR B 741 3435 3233 4213 -75 -533 102 C ATOM 3063 C TYR B 741 4.238 28.743 5.922 1.00 31.39 C ANISOU 3063 C TYR B 741 3720 3570 4636 -43 -488 100 C ATOM 3064 O TYR B 741 4.232 28.219 7.029 1.00 32.69 O ANISOU 3064 O TYR B 741 3862 3749 4809 -35 -444 72 O ATOM 3065 CB TYR B 741 6.303 27.536 5.044 1.00 25.88 C ANISOU 3065 CB TYR B 741 3138 2900 3797 -86 -488 58 C ATOM 3066 CG TYR B 741 6.695 26.420 4.084 1.00 23.69 C ANISOU 3066 CG TYR B 741 2915 2638 3448 -114 -527 56 C ATOM 3067 CD1 TYR B 741 5.916 25.261 3.984 1.00 22.89 C ANISOU 3067 CD1 TYR B 741 2801 2547 3350 -133 -571 59 C ATOM 3068 CD2 TYR B 741 7.792 26.542 3.239 1.00 21.84 C ANISOU 3068 CD2 TYR B 741 2746 2406 3148 -118 -521 55 C ATOM 3069 CE1 TYR B 741 6.242 24.249 3.092 1.00 22.21 C ANISOU 3069 CE1 TYR B 741 2773 2468 3198 -154 -613 51 C ATOM 3070 CE2 TYR B 741 8.119 25.539 2.346 1.00 21.18 C ANISOU 3070 CE2 TYR B 741 2720 2335 2992 -134 -553 52 C ATOM 3071 CZ TYR B 741 7.339 24.399 2.275 1.00 21.65 C ANISOU 3071 CZ TYR B 741 2773 2401 3051 -152 -602 45 C ATOM 3072 OH TYR B 741 7.656 23.403 1.388 1.00 21.39 O ANISOU 3072 OH TYR B 741 2806 2375 2947 -164 -639 35 O ATOM 3073 N GLU B 742 3.646 29.905 5.671 1.00 35.57 N ANISOU 3073 N GLU B 742 4222 4074 5219 -20 -499 131 N ATOM 3074 CA GLU B 742 2.755 30.531 6.643 1.00 39.14 C ANISOU 3074 CA GLU B 742 4611 4513 5749 18 -464 138 C ATOM 3075 C GLU B 742 1.329 30.007 6.500 1.00 40.78 C ANISOU 3075 C GLU B 742 4753 4725 6016 16 -504 183 C ATOM 3076 O GLU B 742 0.571 29.963 7.474 1.00 42.84 O ANISOU 3076 O GLU B 742 4956 4989 6334 43 -464 188 O ATOM 3077 CB GLU B 742 2.776 32.050 6.495 1.00 45.39 C ANISOU 3077 CB GLU B 742 5400 5267 6579 48 -456 151 C ATOM 3078 CG GLU B 742 4.094 32.659 6.940 1.00 50.73 C ANISOU 3078 CG GLU B 742 6123 5929 7221 54 -411 105 C ATOM 3079 CD GLU B 742 4.147 34.171 6.799 1.00 56.73 C ANISOU 3079 CD GLU B 742 6882 6645 8029 81 -407 118 C ATOM 3080 OE1 GLU B 742 3.206 34.752 6.198 1.00 61.12 O ANISOU 3080 OE1 GLU B 742 7405 7182 8635 94 -440 166 O ATOM 3081 OE2 GLU B 742 5.134 34.771 7.300 1.00 57.39 O ANISOU 3081 OE2 GLU B 742 6995 6708 8104 88 -374 81 O ATOM 3082 N LYS B 743 0.966 29.614 5.282 1.00 39.95 N ANISOU 3082 N LYS B 743 4659 4620 5899 -14 -583 218 N ATOM 3083 CA LYS B 743 -0.396 29.186 4.992 1.00 40.45 C ANISOU 3083 CA LYS B 743 4659 4680 6030 -21 -639 267 C ATOM 3084 C LYS B 743 -0.418 27.681 4.775 1.00 38.58 C ANISOU 3084 C LYS B 743 4434 4463 5762 -62 -680 259 C ATOM 3085 O LYS B 743 -1.454 27.082 4.553 1.00 39.65 O ANISOU 3085 O LYS B 743 4519 4595 5953 -78 -736 296 O ATOM 3086 CB LYS B 743 -0.943 29.921 3.767 1.00 40.59 C ANISOU 3086 CB LYS B 743 4676 4676 6069 -22 -715 317 C ATOM 3087 CG LYS B 743 -0.960 31.436 3.916 1.00 40.18 C ANISOU 3087 CG LYS B 743 4611 4598 6059 18 -679 330 C ATOM 3088 CD LYS B 743 -1.654 31.794 5.217 1.00 40.36 C ANISOU 3088 CD LYS B 743 4560 4614 6162 59 -611 330 C ATOM 3089 CE LYS B 743 -2.079 33.244 5.283 1.00 41.12 C ANISOU 3089 CE LYS B 743 4625 4675 6323 103 -592 355 C ATOM 3090 NZ LYS B 743 -2.829 33.505 6.554 1.00 41.68 N ANISOU 3090 NZ LYS B 743 4628 4741 6468 151 -521 355 N ATOM 3091 N HIS B 744 0.747 27.068 4.846 1.00 36.76 N ANISOU 3091 N HIS B 744 4269 4250 5446 -79 -655 211 N ATOM 3092 CA HIS B 744 0.845 25.654 4.586 1.00 35.05 C ANISOU 3092 CA HIS B 744 4077 4048 5195 -116 -694 198 C ATOM 3093 C HIS B 744 1.848 25.066 5.569 1.00 32.71 C ANISOU 3093 C HIS B 744 3805 3772 4851 -116 -619 147 C ATOM 3094 O HIS B 744 2.882 25.681 5.830 1.00 32.08 O ANISOU 3094 O HIS B 744 3767 3696 4727 -100 -567 115 O ATOM 3095 CB HIS B 744 1.252 25.416 3.134 1.00 36.57 C ANISOU 3095 CB HIS B 744 4346 4235 5314 -141 -771 199 C ATOM 3096 CG HIS B 744 0.930 24.047 2.650 1.00 38.23 C ANISOU 3096 CG HIS B 744 4571 4446 5508 -177 -842 196 C ATOM 3097 ND1 HIS B 744 1.809 22.989 2.766 1.00 38.13 N ANISOU 3097 ND1 HIS B 744 4613 4448 5428 -195 -825 152 N ATOM 3098 CD2 HIS B 744 -0.200 23.542 2.100 1.00 39.34 C ANISOU 3098 CD2 HIS B 744 4677 4570 5700 -198 -934 232 C ATOM 3099 CE1 HIS B 744 1.242 21.895 2.283 1.00 38.57 C ANISOU 3099 CE1 HIS B 744 4671 4492 5490 -225 -903 158 C ATOM 3100 NE2 HIS B 744 0.020 22.204 1.878 1.00 39.40 N ANISOU 3100 NE2 HIS B 744 4722 4578 5669 -230 -974 205 N ATOM 3101 N PRO B 745 1.535 23.887 6.144 1.00 31.74 N ANISOU 3101 N PRO B 745 3654 3661 4746 -133 -616 143 N ATOM 3102 CA PRO B 745 2.399 23.283 7.174 1.00 30.47 C ANISOU 3102 CA PRO B 745 3511 3521 4546 -130 -545 100 C ATOM 3103 C PRO B 745 3.809 23.006 6.659 1.00 30.53 C ANISOU 3103 C PRO B 745 3607 3536 4457 -145 -541 57 C ATOM 3104 O PRO B 745 3.976 22.482 5.546 1.00 28.73 O ANISOU 3104 O PRO B 745 3428 3303 4186 -170 -604 58 O ATOM 3105 CB PRO B 745 1.688 21.964 7.514 1.00 30.63 C ANISOU 3105 CB PRO B 745 3487 3545 4606 -153 -566 117 C ATOM 3106 CG PRO B 745 0.310 22.141 7.037 1.00 31.65 C ANISOU 3106 CG PRO B 745 3551 3654 4820 -158 -627 173 C ATOM 3107 CD PRO B 745 0.366 23.044 5.853 1.00 31.68 C ANISOU 3107 CD PRO B 745 3594 3643 4800 -157 -683 182 C ATOM 3108 N LEU B 746 4.812 23.352 7.459 1.00 31.32 N ANISOU 3108 N LEU B 746 3728 3647 4524 -127 -471 21 N ATOM 3109 CA LEU B 746 6.196 23.104 7.076 1.00 32.34 C ANISOU 3109 CA LEU B 746 3930 3785 4574 -138 -458 -14 C ATOM 3110 C LEU B 746 6.706 21.784 7.646 1.00 34.57 C ANISOU 3110 C LEU B 746 4226 4085 4825 -155 -438 -42 C ATOM 3111 O LEU B 746 7.464 21.078 6.998 1.00 35.70 O ANISOU 3111 O LEU B 746 4424 4231 4909 -173 -455 -59 O ATOM 3112 CB LEU B 746 7.093 24.249 7.531 1.00 28.89 C ANISOU 3112 CB LEU B 746 3508 3343 4126 -114 -405 -35 C ATOM 3113 CG LEU B 746 8.580 23.984 7.270 1.00 25.80 C ANISOU 3113 CG LEU B 746 3179 2960 3666 -125 -384 -64 C ATOM 3114 CD1 LEU B 746 8.859 23.832 5.768 1.00 23.90 C ANISOU 3114 CD1 LEU B 746 2991 2713 3376 -141 -430 -46 C ATOM 3115 CD2 LEU B 746 9.443 25.066 7.913 1.00 24.66 C ANISOU 3115 CD2 LEU B 746 3037 2805 3527 -105 -335 -84 C ATOM 3116 N TYR B 747 6.275 21.456 8.858 1.00 38.39 N ANISOU 3116 N TYR B 747 4661 4579 5347 -143 -397 -43 N ATOM 3117 CA TYR B 747 6.708 20.238 9.536 1.00 41.63 C ANISOU 3117 CA TYR B 747 5077 5006 5735 -155 -373 -63 C ATOM 3118 C TYR B 747 5.712 19.835 10.623 1.00 44.72 C ANISOU 3118 C TYR B 747 5399 5405 6187 -143 -345 -40 C ATOM 3119 O TYR B 747 5.567 20.535 11.623 1.00 47.87 O ANISOU 3119 O TYR B 747 5769 5812 6606 -108 -290 -42 O ATOM 3120 CB TYR B 747 8.089 20.440 10.136 1.00 43.48 C ANISOU 3120 CB TYR B 747 5352 5253 5917 -143 -319 -105 C ATOM 3121 CG TYR B 747 8.610 19.247 10.879 1.00 45.97 C ANISOU 3121 CG TYR B 747 5673 5585 6207 -152 -291 -124 C ATOM 3122 CD1 TYR B 747 8.930 18.075 10.206 1.00 46.98 C ANISOU 3122 CD1 TYR B 747 5835 5711 6304 -181 -324 -129 C ATOM 3123 CD2 TYR B 747 8.808 19.292 12.252 1.00 47.35 C ANISOU 3123 CD2 TYR B 747 5828 5776 6385 -128 -234 -139 C ATOM 3124 CE1 TYR B 747 9.425 16.978 10.879 1.00 47.47 C ANISOU 3124 CE1 TYR B 747 5903 5786 6348 -188 -299 -145 C ATOM 3125 CE2 TYR B 747 9.309 18.196 12.941 1.00 47.86 C ANISOU 3125 CE2 TYR B 747 5900 5857 6426 -134 -209 -152 C ATOM 3126 CZ TYR B 747 9.617 17.044 12.246 1.00 47.81 C ANISOU 3126 CZ TYR B 747 5921 5847 6398 -165 -242 -154 C ATOM 3127 OH TYR B 747 10.104 15.947 12.917 1.00 47.77 O ANISOU 3127 OH TYR B 747 5921 5854 6374 -171 -218 -164 O ATOM 3128 N ARG B 748 5.026 18.715 10.410 1.00 47.56 N ANISOU 3128 N ARG B 748 5733 5760 6577 -169 -383 -16 N ATOM 3129 CA ARG B 748 4.012 18.220 11.339 1.00 49.50 C ANISOU 3129 CA ARG B 748 5905 6011 6891 -161 -358 20 C ATOM 3130 C ARG B 748 2.921 19.252 11.666 1.00 48.54 C ANISOU 3130 C ARG B 748 5718 5885 6839 -129 -339 58 C ATOM 3131 O ARG B 748 2.779 19.663 12.823 1.00 47.84 O ANISOU 3131 O ARG B 748 5600 5812 6764 -89 -267 61 O ATOM 3132 CB ARG B 748 4.666 17.746 12.645 1.00 51.74 C ANISOU 3132 CB ARG B 748 6193 6321 7146 -142 -282 -1 C ATOM 3133 CG ARG B 748 5.696 16.661 12.471 1.00 53.72 C ANISOU 3133 CG ARG B 748 6498 6576 7338 -169 -293 -33 C ATOM 3134 CD ARG B 748 5.742 15.756 13.686 1.00 56.39 C ANISOU 3134 CD ARG B 748 6812 6932 7683 -161 -240 -26 C ATOM 3135 NE ARG B 748 6.553 14.570 13.424 1.00 58.47 N ANISOU 3135 NE ARG B 748 7118 7193 7906 -191 -259 -48 N ATOM 3136 CZ ARG B 748 7.738 14.331 13.983 1.00 59.26 C ANISOU 3136 CZ ARG B 748 7260 7310 7946 -181 -219 -84 C ATOM 3137 NH1 ARG B 748 8.415 13.229 13.670 1.00 59.84 N ANISOU 3137 NH1 ARG B 748 7369 7377 7990 -206 -238 -101 N ATOM 3138 NH2 ARG B 748 8.249 15.191 14.858 1.00 59.47 N ANISOU 3138 NH2 ARG B 748 7295 7357 7945 -146 -164 -105 N ATOM 3139 N LYS B 749 2.163 19.674 10.658 1.00 45.97 N ANISOU 3139 N LYS B 749 5374 5538 6555 -142 -405 88 N ATOM 3140 CA LYS B 749 1.025 20.582 10.871 1.00 44.22 C ANISOU 3140 CA LYS B 749 5082 5308 6412 -112 -394 133 C ATOM 3141 C LYS B 749 1.413 21.953 11.460 1.00 41.21 C ANISOU 3141 C LYS B 749 4715 4932 6010 -63 -330 109 C ATOM 3142 O LYS B 749 0.545 22.788 11.756 1.00 41.12 O ANISOU 3142 O LYS B 749 4650 4912 6060 -28 -308 140 O ATOM 3143 CB LYS B 749 -0.031 19.912 11.769 1.00 43.93 C ANISOU 3143 CB LYS B 749 4958 5277 6456 -103 -362 183 C ATOM 3144 N MET B 750 2.718 22.175 11.609 1.00 38.22 N ANISOU 3144 N MET B 750 4408 4563 5553 -60 -304 54 N ATOM 3145 CA MET B 750 3.268 23.451 12.066 1.00 35.59 C ANISOU 3145 CA MET B 750 4099 4225 5197 -21 -258 23 C ATOM 3146 C MET B 750 3.467 24.434 10.907 1.00 33.74 C ANISOU 3146 C MET B 750 3894 3967 4957 -30 -307 25 C ATOM 3147 O MET B 750 4.204 24.159 9.958 1.00 34.26 O ANISOU 3147 O MET B 750 4012 4031 4974 -62 -349 12 O ATOM 3148 CB MET B 750 4.597 23.216 12.796 1.00 34.06 C ANISOU 3148 CB MET B 750 3962 4048 4931 -17 -214 -31 C ATOM 3149 CG MET B 750 5.139 24.417 13.588 1.00 33.30 C ANISOU 3149 CG MET B 750 3888 3945 4819 26 -165 -68 C ATOM 3150 SD MET B 750 6.086 25.629 12.637 1.00 79.80 S ANISOU 3150 SD MET B 750 9829 9805 10685 16 -199 -91 S ATOM 3151 CE MET B 750 7.348 24.584 11.939 1.00 31.29 C ANISOU 3151 CE MET B 750 3740 3675 4472 -32 -226 -111 C ATOM 3152 N LYS B 751 2.795 25.577 10.993 1.00 32.00 N ANISOU 3152 N LYS B 751 3641 3730 4789 4 -297 45 N ATOM 3153 CA LYS B 751 2.996 26.669 10.046 1.00 29.64 C ANISOU 3153 CA LYS B 751 3367 3405 4489 4 -333 50 C ATOM 3154 C LYS B 751 3.905 27.731 10.671 1.00 28.58 C ANISOU 3154 C LYS B 751 3269 3259 4331 34 -284 7 C ATOM 3155 O LYS B 751 3.934 27.874 11.890 1.00 30.85 O ANISOU 3155 O LYS B 751 3547 3553 4622 69 -226 -18 O ATOM 3156 CB LYS B 751 1.649 27.277 9.629 1.00 30.28 C ANISOU 3156 CB LYS B 751 3385 3467 4652 20 -363 105 C ATOM 3157 CG LYS B 751 0.677 26.265 9.072 1.00 30.67 C ANISOU 3157 CG LYS B 751 3390 3521 4740 -12 -421 151 C ATOM 3158 CD LYS B 751 -0.692 26.867 8.765 1.00 31.32 C ANISOU 3158 CD LYS B 751 3400 3585 4916 6 -451 210 C ATOM 3159 CE LYS B 751 -1.641 25.776 8.251 1.00 31.51 C ANISOU 3159 CE LYS B 751 3376 3610 4989 -31 -519 256 C ATOM 3160 NZ LYS B 751 -2.969 26.288 7.800 1.00 32.28 N ANISOU 3160 NZ LYS B 751 3396 3684 5183 -21 -564 321 N ATOM 3161 N LEU B 752 4.660 28.460 9.848 1.00 27.28 N ANISOU 3161 N LEU B 752 3147 3075 4142 22 -310 0 N ATOM 3162 CA LEU B 752 5.482 29.571 10.340 1.00 25.91 C ANISOU 3162 CA LEU B 752 3003 2879 3964 47 -277 -35 C ATOM 3163 C LEU B 752 4.603 30.678 10.933 1.00 25.84 C ANISOU 3163 C LEU B 752 2955 2844 4020 96 -252 -26 C ATOM 3164 O LEU B 752 3.627 31.082 10.314 1.00 26.55 O ANISOU 3164 O LEU B 752 3007 2921 4161 103 -280 19 O ATOM 3165 CB LEU B 752 6.349 30.121 9.217 1.00 24.19 C ANISOU 3165 CB LEU B 752 2828 2642 3720 22 -310 -27 C ATOM 3166 CG LEU B 752 7.311 29.112 8.593 1.00 22.17 C ANISOU 3166 CG LEU B 752 2617 2409 3396 -17 -326 -36 C ATOM 3167 CD1 LEU B 752 8.134 29.779 7.507 1.00 21.68 C ANISOU 3167 CD1 LEU B 752 2595 2328 3313 -32 -347 -20 C ATOM 3168 CD2 LEU B 752 8.216 28.468 9.641 1.00 20.80 C ANISOU 3168 CD2 LEU B 752 2462 2254 3185 -19 -284 -85 C ATOM 3169 N ARG B 753 4.946 31.164 12.129 1.00 25.88 N ANISOU 3169 N ARG B 753 2972 2840 4021 134 -202 -70 N ATOM 3170 CA ARG B 753 4.079 32.092 12.863 1.00 26.13 C ANISOU 3170 CA ARG B 753 2972 2849 4108 191 -167 -69 C ATOM 3171 C ARG B 753 4.767 33.364 13.369 1.00 26.63 C ANISOU 3171 C ARG B 753 3074 2870 4175 222 -152 -115 C ATOM 3172 O ARG B 753 4.268 34.476 13.164 1.00 26.71 O ANISOU 3172 O ARG B 753 3069 2841 4239 251 -157 -100 O ATOM 3173 CB ARG B 753 3.450 31.389 14.067 1.00 26.45 C ANISOU 3173 CB ARG B 753 2985 2920 4146 226 -112 -76 C ATOM 3174 CG ARG B 753 2.416 30.341 13.738 1.00 27.05 C ANISOU 3174 CG ARG B 753 3002 3025 4251 208 -122 -20 C ATOM 3175 CD ARG B 753 1.377 30.213 14.867 1.00 27.54 C ANISOU 3175 CD ARG B 753 3014 3101 4350 264 -57 -3 C ATOM 3176 NE ARG B 753 1.938 29.560 16.040 1.00 27.38 N ANISOU 3176 NE ARG B 753 3024 3109 4270 281 -4 -44 N ATOM 3177 CZ ARG B 753 1.422 29.615 17.261 1.00 28.05 C ANISOU 3177 CZ ARG B 753 3095 3206 4358 343 69 -48 C ATOM 3178 NH1 ARG B 753 0.313 30.309 17.505 1.00 28.60 N ANISOU 3178 NH1 ARG B 753 3116 3261 4492 397 104 -14 N ATOM 3179 NH2 ARG B 753 2.043 28.974 18.244 1.00 28.04 N ANISOU 3179 NH2 ARG B 753 3131 3233 4293 354 108 -84 N ATOM 3180 N TYR B 754 5.887 33.195 14.067 1.00 26.61 N ANISOU 3180 N TYR B 754 3119 2870 4121 218 -137 -170 N ATOM 3181 CA TYR B 754 6.538 34.321 14.731 1.00 27.17 C ANISOU 3181 CA TYR B 754 3227 2896 4198 248 -128 -221 C ATOM 3182 C TYR B 754 7.910 34.587 14.147 1.00 25.71 C ANISOU 3182 C TYR B 754 3082 2690 3997 203 -165 -237 C ATOM 3183 O TYR B 754 8.871 33.897 14.494 1.00 24.84 O ANISOU 3183 O TYR B 754 3000 2602 3837 179 -163 -267 O ATOM 3184 CB TYR B 754 6.667 34.065 16.232 1.00 28.27 C ANISOU 3184 CB TYR B 754 3392 3050 4298 292 -81 -276 C ATOM 3185 CG TYR B 754 5.352 33.783 16.916 1.00 29.60 C ANISOU 3185 CG TYR B 754 3521 3242 4483 344 -30 -255 C ATOM 3186 CD1 TYR B 754 4.485 34.819 17.234 1.00 31.02 C ANISOU 3186 CD1 TYR B 754 3685 3388 4714 404 -6 -252 C ATOM 3187 CD2 TYR B 754 4.973 32.480 17.243 1.00 29.70 C ANISOU 3187 CD2 TYR B 754 3509 3308 4466 336 -3 -234 C ATOM 3188 CE1 TYR B 754 3.271 34.581 17.866 1.00 31.86 C ANISOU 3188 CE1 TYR B 754 3750 3517 4841 458 50 -225 C ATOM 3189 CE2 TYR B 754 3.756 32.225 17.869 1.00 30.71 C ANISOU 3189 CE2 TYR B 754 3592 3457 4618 385 49 -204 C ATOM 3190 CZ TYR B 754 2.904 33.288 18.177 1.00 32.07 C ANISOU 3190 CZ TYR B 754 3747 3598 4841 448 79 -198 C ATOM 3191 OH TYR B 754 1.685 33.070 18.800 1.00 33.04 O ANISOU 3191 OH TYR B 754 3819 3740 4994 503 140 -161 O ATOM 3192 N PRO B 755 8.005 35.577 13.240 1.00 25.74 N ANISOU 3192 N PRO B 755 3083 2652 4046 192 -196 -209 N ATOM 3193 CA PRO B 755 9.319 35.977 12.704 1.00 24.47 C ANISOU 3193 CA PRO B 755 2953 2464 3882 154 -224 -215 C ATOM 3194 C PRO B 755 10.201 36.528 13.818 1.00 23.50 C ANISOU 3194 C PRO B 755 2865 2305 3757 172 -219 -282 C ATOM 3195 O PRO B 755 9.758 37.359 14.599 1.00 23.17 O ANISOU 3195 O PRO B 755 2830 2227 3745 220 -209 -315 O ATOM 3196 CB PRO B 755 8.972 37.049 11.660 1.00 25.13 C ANISOU 3196 CB PRO B 755 3020 2504 4024 153 -251 -167 C ATOM 3197 CG PRO B 755 7.607 37.530 12.046 1.00 25.70 C ANISOU 3197 CG PRO B 755 3061 2566 4139 204 -235 -159 C ATOM 3198 CD PRO B 755 6.898 36.360 12.662 1.00 25.29 C ANISOU 3198 CD PRO B 755 2990 2570 4050 216 -205 -165 C ATOM 3199 N ILE B 756 11.433 36.052 13.903 1.00 23.45 N ANISOU 3199 N ILE B 756 2884 2309 3719 137 -229 -303 N ATOM 3200 CA ILE B 756 12.290 36.375 15.030 1.00 23.03 C ANISOU 3200 CA ILE B 756 2865 2228 3658 150 -234 -368 C ATOM 3201 C ILE B 756 13.519 37.163 14.584 1.00 22.96 C ANISOU 3201 C ILE B 756 2866 2165 3692 116 -271 -366 C ATOM 3202 O ILE B 756 14.196 36.772 13.632 1.00 21.22 O ANISOU 3202 O ILE B 756 2636 1960 3467 71 -279 -323 O ATOM 3203 CB ILE B 756 12.746 35.082 15.773 1.00 21.73 C ANISOU 3203 CB ILE B 756 2716 2118 3423 142 -217 -398 C ATOM 3204 CG1 ILE B 756 11.529 34.291 16.281 1.00 21.49 C ANISOU 3204 CG1 ILE B 756 2669 2136 3358 176 -176 -393 C ATOM 3205 CG2 ILE B 756 13.718 35.407 16.917 1.00 21.66 C ANISOU 3205 CG2 ILE B 756 2747 2080 3404 153 -233 -465 C ATOM 3206 CD1 ILE B 756 10.496 35.150 17.003 1.00 22.25 C ANISOU 3206 CD1 ILE B 756 2765 2207 3483 240 -154 -413 C ATOM 3207 N ASN B 757 13.765 38.286 15.268 1.00 24.18 N ANISOU 3207 N ASN B 757 3042 2255 3891 141 -293 -410 N ATOM 3208 CA ASN B 757 15.017 39.042 15.245 1.00 24.45 C ANISOU 3208 CA ASN B 757 3088 2229 3974 113 -334 -423 C ATOM 3209 C ASN B 757 15.208 39.677 16.625 1.00 25.87 C ANISOU 3209 C ASN B 757 3308 2360 4160 152 -357 -506 C ATOM 3210 O ASN B 757 14.354 39.505 17.482 1.00 25.67 O ANISOU 3210 O ASN B 757 3303 2355 4094 204 -330 -545 O ATOM 3211 CB ASN B 757 15.004 40.097 14.149 1.00 23.92 C ANISOU 3211 CB ASN B 757 2997 2109 3983 96 -352 -367 C ATOM 3212 CG ASN B 757 13.869 41.116 14.313 1.00 22.87 C ANISOU 3212 CG ASN B 757 2863 1933 3894 146 -350 -375 C ATOM 3213 OD1 ASN B 757 13.271 41.256 15.379 1.00 22.43 O ANISOU 3213 OD1 ASN B 757 2831 1871 3820 197 -339 -433 O ATOM 3214 ND2 ASN B 757 13.588 41.845 13.243 1.00 21.94 N ANISOU 3214 ND2 ASN B 757 2720 1785 3833 136 -358 -313 N ATOM 3215 N GLU B 758 16.283 40.429 16.856 1.00 28.80 N ANISOU 3215 N GLU B 758 3694 2665 4583 132 -406 -532 N ATOM 3216 CA GLU B 758 16.552 40.929 18.216 1.00 32.12 C ANISOU 3216 CA GLU B 758 4165 3040 4999 169 -439 -620 C ATOM 3217 C GLU B 758 15.504 41.915 18.721 1.00 34.84 C ANISOU 3217 C GLU B 758 4535 3339 5365 234 -433 -657 C ATOM 3218 O GLU B 758 15.346 42.087 19.928 1.00 36.44 O ANISOU 3218 O GLU B 758 4790 3526 5531 285 -440 -733 O ATOM 3219 CB GLU B 758 17.940 41.574 18.309 1.00 32.57 C ANISOU 3219 CB GLU B 758 4228 3026 5123 128 -506 -637 C ATOM 3220 CG GLU B 758 19.094 40.561 18.280 1.00 33.13 C ANISOU 3220 CG GLU B 758 4284 3138 5164 78 -516 -623 C ATOM 3221 CD GLU B 758 19.167 39.640 19.524 1.00 33.63 C ANISOU 3221 CD GLU B 758 4390 3251 5137 105 -512 -688 C ATOM 3222 OE1 GLU B 758 18.887 40.125 20.651 1.00 34.15 O ANISOU 3222 OE1 GLU B 758 4509 3284 5182 155 -535 -764 O ATOM 3223 OE2 GLU B 758 19.523 38.441 19.372 1.00 34.09 O ANISOU 3223 OE2 GLU B 758 4433 3378 5143 79 -486 -663 O ATOM 3224 N GLU B 759 14.780 42.554 17.813 1.00 37.53 N ANISOU 3224 N GLU B 759 4842 3657 5759 238 -419 -604 N ATOM 3225 CA GLU B 759 13.741 43.485 18.228 1.00 40.29 C ANISOU 3225 CA GLU B 759 5210 3963 6135 304 -407 -632 C ATOM 3226 C GLU B 759 12.449 42.739 18.569 1.00 38.59 C ANISOU 3226 C GLU B 759 4988 3819 5854 355 -341 -627 C ATOM 3227 O GLU B 759 11.748 43.115 19.496 1.00 37.05 O ANISOU 3227 O GLU B 759 4828 3609 5641 425 -319 -679 O ATOM 3228 CB GLU B 759 13.506 44.539 17.145 1.00 46.59 C ANISOU 3228 CB GLU B 759 5973 4702 7028 289 -423 -574 C ATOM 3229 CG GLU B 759 12.269 45.395 17.340 1.00 52.60 C ANISOU 3229 CG GLU B 759 6739 5426 7821 356 -401 -583 C ATOM 3230 CD GLU B 759 12.184 46.570 16.356 1.00 59.23 C ANISOU 3230 CD GLU B 759 7549 6192 8763 342 -427 -530 C ATOM 3231 OE1 GLU B 759 12.991 46.607 15.399 1.00 60.96 O ANISOU 3231 OE1 GLU B 759 7739 6403 9021 278 -453 -472 O ATOM 3232 OE2 GLU B 759 11.315 47.461 16.550 1.00 64.53 O ANISOU 3232 OE2 GLU B 759 8227 6815 9478 398 -419 -543 O ATOM 3233 N ALA B 760 12.140 41.670 17.844 1.00 36.08 N ANISOU 3233 N ALA B 760 4628 3579 5501 323 -308 -566 N ATOM 3234 CA ALA B 760 11.022 40.818 18.221 1.00 35.11 C ANISOU 3234 CA ALA B 760 4493 3526 5321 363 -249 -557 C ATOM 3235 C ALA B 760 11.278 40.201 19.593 1.00 32.54 C ANISOU 3235 C ALA B 760 4216 3230 4919 397 -233 -626 C ATOM 3236 O ALA B 760 10.379 40.136 20.423 1.00 32.86 O ANISOU 3236 O ALA B 760 4271 3287 4926 464 -187 -651 O ATOM 3237 CB ALA B 760 10.779 39.704 17.161 1.00 20.66 C ANISOU 3237 CB ALA B 760 2613 1768 3470 314 -231 -482 C ATOM 3238 N LEU B 761 12.501 39.730 19.822 1.00 30.44 N ANISOU 3238 N LEU B 761 3973 2971 4624 354 -267 -652 N ATOM 3239 CA LEU B 761 12.867 39.155 21.112 1.00 29.56 C ANISOU 3239 CA LEU B 761 3912 2885 4437 384 -261 -716 C ATOM 3240 C LEU B 761 12.704 40.146 22.275 1.00 31.74 C ANISOU 3240 C LEU B 761 4252 3101 4707 456 -274 -797 C ATOM 3241 O LEU B 761 12.563 39.742 23.416 1.00 32.57 O ANISOU 3241 O LEU B 761 4404 3233 4738 506 -251 -847 O ATOM 3242 CB LEU B 761 14.308 38.649 21.080 1.00 28.44 C ANISOU 3242 CB LEU B 761 3779 2746 4282 322 -308 -727 C ATOM 3243 CG LEU B 761 14.712 37.505 20.144 1.00 26.83 C ANISOU 3243 CG LEU B 761 3528 2603 4064 257 -296 -663 C ATOM 3244 CD1 LEU B 761 16.166 37.155 20.335 1.00 26.54 C ANISOU 3244 CD1 LEU B 761 3505 2560 4020 211 -341 -683 C ATOM 3245 CD2 LEU B 761 13.889 36.318 20.426 1.00 26.27 C ANISOU 3245 CD2 LEU B 761 3445 2611 3924 278 -239 -645 C ATOM 3246 N GLU B 762 12.742 41.443 22.004 1.00 33.27 N ANISOU 3246 N GLU B 762 4454 3211 4977 464 -311 -811 N ATOM 3247 CA GLU B 762 12.531 42.411 23.072 1.00 34.94 C ANISOU 3247 CA GLU B 762 4733 3359 5183 538 -324 -891 C ATOM 3248 C GLU B 762 11.079 42.365 23.572 1.00 36.16 C ANISOU 3248 C GLU B 762 4892 3547 5302 624 -244 -890 C ATOM 3249 O GLU B 762 10.770 42.858 24.655 1.00 37.87 O ANISOU 3249 O GLU B 762 5173 3733 5480 703 -232 -959 O ATOM 3250 CB GLU B 762 12.865 43.838 22.606 1.00 35.31 C ANISOU 3250 CB GLU B 762 4784 3300 5331 526 -384 -902 C ATOM 3251 CG GLU B 762 14.321 44.118 22.228 1.00 37.00 C ANISOU 3251 CG GLU B 762 4995 3463 5600 449 -467 -905 C ATOM 3252 CD GLU B 762 14.526 45.550 21.668 1.00 46.64 C ANISOU 3252 CD GLU B 762 6208 4578 6936 436 -520 -900 C ATOM 3253 OE1 GLU B 762 13.524 46.253 21.390 1.00 46.79 O ANISOU 3253 OE1 GLU B 762 6217 4569 6993 480 -489 -884 O ATOM 3254 OE2 GLU B 762 15.695 45.975 21.501 1.00 47.34 O ANISOU 3254 OE2 GLU B 762 6297 4606 7084 382 -592 -908 O ATOM 3255 N LYS B 763 10.196 41.775 22.773 1.00 35.73 N ANISOU 3255 N LYS B 763 4766 3549 5259 611 -190 -809 N ATOM 3256 CA LYS B 763 8.760 41.890 22.990 1.00 35.68 C ANISOU 3256 CA LYS B 763 4741 3563 5253 685 -116 -787 C ATOM 3257 C LYS B 763 8.079 40.562 23.352 1.00 34.00 C ANISOU 3257 C LYS B 763 4501 3445 4971 702 -45 -752 C ATOM 3258 O LYS B 763 7.113 40.547 24.115 1.00 33.60 O ANISOU 3258 O LYS B 763 4460 3413 4892 783 22 -760 O ATOM 3259 CB LYS B 763 8.094 42.483 21.742 1.00 37.35 C ANISOU 3259 CB LYS B 763 4884 3748 5558 663 -118 -715 C ATOM 3260 CG LYS B 763 8.619 43.856 21.321 1.00 39.01 C ANISOU 3260 CG LYS B 763 5112 3859 5849 649 -181 -736 C ATOM 3261 CD LYS B 763 8.101 44.251 19.927 1.00 39.33 C ANISOU 3261 CD LYS B 763 5082 3887 5975 613 -187 -650 C ATOM 3262 CE LYS B 763 8.462 45.693 19.546 1.00 40.03 C ANISOU 3262 CE LYS B 763 5184 3872 6153 610 -241 -663 C ATOM 3263 NZ LYS B 763 9.928 45.997 19.612 1.00 39.93 N ANISOU 3263 NZ LYS B 763 5208 3809 6153 556 -312 -703 N ATOM 3264 N ILE B 764 8.558 39.452 22.800 1.00 31.23 N ANISOU 3264 N ILE B 764 4114 3152 4599 630 -55 -710 N ATOM 3265 CA ILE B 764 7.959 38.161 23.088 1.00 28.93 C ANISOU 3265 CA ILE B 764 3793 2945 4253 639 5 -672 C ATOM 3266 C ILE B 764 8.996 37.179 23.601 1.00 28.92 C ANISOU 3266 C ILE B 764 3826 2985 4178 604 -14 -701 C ATOM 3267 O ILE B 764 8.702 35.990 23.785 1.00 25.66 O ANISOU 3267 O ILE B 764 3389 2640 3720 598 28 -668 O ATOM 3268 CB ILE B 764 7.301 37.544 21.848 1.00 28.02 C ANISOU 3268 CB ILE B 764 3593 2869 4185 587 16 -581 C ATOM 3269 CG1 ILE B 764 8.378 37.187 20.810 1.00 26.93 C ANISOU 3269 CG1 ILE B 764 3441 2732 4060 493 -46 -560 C ATOM 3270 CG2 ILE B 764 6.221 38.466 21.293 1.00 27.91 C ANISOU 3270 CG2 ILE B 764 3538 2819 4249 621 31 -543 C ATOM 3271 CD1 ILE B 764 7.850 36.509 19.560 1.00 26.33 C ANISOU 3271 CD1 ILE B 764 3296 2694 4014 442 -46 -477 C ATOM 3272 N GLY B 765 10.213 37.667 23.816 1.00 30.36 N ANISOU 3272 N GLY B 765 4059 3120 4355 579 -79 -759 N ATOM 3273 CA GLY B 765 11.309 36.805 24.225 1.00 30.76 C ANISOU 3273 CA GLY B 765 4138 3202 4348 540 -108 -783 C ATOM 3274 C GLY B 765 11.559 36.794 25.722 1.00 30.91 C ANISOU 3274 C GLY B 765 4236 3222 4285 605 -102 -859 C ATOM 3275 O GLY B 765 11.311 37.769 26.412 1.00 31.94 O ANISOU 3275 O GLY B 765 4421 3302 4412 670 -106 -915 O ATOM 3276 N THR B 766 12.048 35.683 26.243 1.00 30.04 N ANISOU 3276 N THR B 766 4140 3168 4106 591 -95 -861 N ATOM 3277 CA THR B 766 12.420 35.683 27.636 1.00 32.15 C ANISOU 3277 CA THR B 766 4491 3435 4289 649 -102 -934 C ATOM 3278 C THR B 766 13.664 36.557 27.816 1.00 35.00 C ANISOU 3278 C THR B 766 4904 3720 4673 624 -200 -1002 C ATOM 3279 O THR B 766 14.565 36.575 26.974 1.00 33.38 O ANISOU 3279 O THR B 766 4664 3493 4527 544 -257 -982 O ATOM 3280 CB THR B 766 12.671 34.277 28.164 1.00 33.57 C ANISOU 3280 CB THR B 766 4673 3692 4392 640 -73 -916 C ATOM 3281 OG1 THR B 766 13.024 34.364 29.544 1.00 34.99 O ANISOU 3281 OG1 THR B 766 4942 3869 4484 704 -84 -987 O ATOM 3282 CG2 THR B 766 13.813 33.619 27.427 1.00 34.16 C ANISOU 3282 CG2 THR B 766 4712 3776 4492 545 -128 -891 C ATOM 3283 N ALA B 767 13.687 37.316 28.901 1.00 38.61 N ANISOU 3283 N ALA B 767 5447 4135 5087 696 -220 -1082 N ATOM 3284 CA ALA B 767 14.778 38.243 29.140 1.00 40.88 C ANISOU 3284 CA ALA B 767 5788 4339 5405 677 -323 -1153 C ATOM 3285 C ALA B 767 16.089 37.489 29.342 1.00 42.10 C ANISOU 3285 C ALA B 767 5949 4512 5534 616 -386 -1163 C ATOM 3286 O ALA B 767 16.138 36.452 30.013 1.00 43.97 O ANISOU 3286 O ALA B 767 6205 4816 5684 634 -356 -1161 O ATOM 3287 CB ALA B 767 14.474 39.117 30.334 1.00 40.56 C ANISOU 3287 CB ALA B 767 5849 4250 5311 774 -333 -1242 C ATOM 3288 N GLU B 768 17.149 38.001 28.730 1.00 42.62 N ANISOU 3288 N GLU B 768 5993 4518 5683 545 -471 -1165 N ATOM 3289 CA GLU B 768 18.472 37.433 28.926 1.00 43.03 C ANISOU 3289 CA GLU B 768 6048 4574 5727 489 -540 -1175 C ATOM 3290 C GLU B 768 18.997 37.971 30.259 1.00 43.78 C ANISOU 3290 C GLU B 768 6246 4621 5768 540 -615 -1275 C ATOM 3291 O GLU B 768 18.935 39.174 30.513 1.00 44.89 O ANISOU 3291 O GLU B 768 6434 4678 5943 572 -663 -1333 O ATOM 3292 CB GLU B 768 19.397 37.792 27.755 1.00 45.41 C ANISOU 3292 CB GLU B 768 6280 4828 6145 396 -596 -1131 C ATOM 3293 CG GLU B 768 20.685 36.981 27.685 1.00 48.24 C ANISOU 3293 CG GLU B 768 6613 5208 6509 330 -644 -1113 C ATOM 3294 CD GLU B 768 21.705 37.562 26.700 1.00 50.27 C ANISOU 3294 CD GLU B 768 6811 5401 6888 250 -707 -1077 C ATOM 3295 OE1 GLU B 768 21.477 38.672 26.157 1.00 51.72 O ANISOU 3295 OE1 GLU B 768 6982 5517 7151 246 -724 -1074 O ATOM 3296 OE2 GLU B 768 22.741 36.900 26.477 1.00 51.26 O ANISOU 3296 OE2 GLU B 768 6901 5544 7031 193 -735 -1048 O ATOM 3297 N PRO B 769 19.487 37.076 31.129 1.00 42.01 N ANISOU 3297 N PRO B 769 6061 4444 5455 552 -627 -1297 N ATOM 3298 CA PRO B 769 19.984 37.498 32.447 1.00 42.94 C ANISOU 3298 CA PRO B 769 6288 4523 5506 605 -704 -1394 C ATOM 3299 C PRO B 769 21.217 38.405 32.337 1.00 42.01 C ANISOU 3299 C PRO B 769 6171 4312 5479 545 -832 -1426 C ATOM 3300 O PRO B 769 22.210 38.038 31.704 1.00 41.61 O ANISOU 3300 O PRO B 769 6058 4252 5500 463 -882 -1390 O ATOM 3301 CB PRO B 769 20.344 36.173 33.139 1.00 41.91 C ANISOU 3301 CB PRO B 769 6173 4474 5275 610 -688 -1383 C ATOM 3302 CG PRO B 769 19.690 35.106 32.328 1.00 40.85 C ANISOU 3302 CG PRO B 769 5951 4426 5143 582 -581 -1287 C ATOM 3303 CD PRO B 769 19.625 35.626 30.922 1.00 40.83 C ANISOU 3303 CD PRO B 769 5863 4388 5265 517 -576 -1233 C ATOM 3304 N ASP B 770 21.144 39.580 32.946 1.00 42.31 N ANISOU 3304 N ASP B 770 6264 4293 5517 581 -871 -1470 N ATOM 3305 CA ASP B 770 22.248 40.525 32.906 1.00 41.37 C ANISOU 3305 CA ASP B 770 6134 4096 5487 523 -982 -1479 C ATOM 3306 C ASP B 770 23.416 40.097 33.815 1.00 40.28 C ANISOU 3306 C ASP B 770 6027 3973 5305 501 -1066 -1498 C ATOM 3307 O ASP B 770 24.561 40.498 33.597 1.00 37.98 O ANISOU 3307 O ASP B 770 5698 3631 5103 434 -1158 -1485 O ATOM 3308 CB ASP B 770 21.753 41.920 33.298 1.00 43.30 C ANISOU 3308 CB ASP B 770 6433 4273 5745 572 -1000 -1525 C ATOM 3309 CG ASP B 770 20.622 42.420 32.397 1.00 43.58 C ANISOU 3309 CG ASP B 770 6436 4288 5836 594 -923 -1503 C ATOM 3310 OD1 ASP B 770 20.452 41.896 31.265 1.00 42.86 O ANISOU 3310 OD1 ASP B 770 6265 4213 5806 551 -882 -1447 O ATOM 3311 OD2 ASP B 770 19.898 43.345 32.831 1.00 44.30 O ANISOU 3311 OD2 ASP B 770 6580 4342 5909 658 -906 -1542 O ATOM 3312 N TYR B 771 23.122 39.266 34.811 1.00 38.55 N ANISOU 3312 N TYR B 771 5872 3824 4953 560 -1030 -1523 N ATOM 3313 CA TYR B 771 24.093 38.906 35.847 1.00 38.24 C ANISOU 3313 CA TYR B 771 5876 3798 4854 558 -1108 -1547 C ATOM 3314 C TYR B 771 24.337 37.389 35.908 1.00 37.23 C ANISOU 3314 C TYR B 771 5727 3754 4666 544 -1073 -1513 C ATOM 3315 O TYR B 771 23.487 36.599 35.504 1.00 39.23 O ANISOU 3315 O TYR B 771 5960 4065 4879 566 -974 -1487 O ATOM 3316 CB TYR B 771 23.616 39.410 37.213 1.00 37.22 C ANISOU 3316 CB TYR B 771 5862 3670 4611 650 -1112 -1611 C ATOM 3317 CG TYR B 771 23.482 40.911 37.343 1.00 36.37 C ANISOU 3317 CG TYR B 771 5790 3477 4555 668 -1160 -1654 C ATOM 3318 CD1 TYR B 771 22.297 41.561 37.005 1.00 36.90 C ANISOU 3318 CD1 TYR B 771 5867 3527 4628 717 -1081 -1663 C ATOM 3319 CD2 TYR B 771 24.539 41.688 37.826 1.00 32.23 C ANISOU 3319 CD2 TYR B 771 5288 2884 4075 640 -1286 -1686 C ATOM 3320 CE1 TYR B 771 22.172 42.957 37.142 1.00 32.27 C ANISOU 3320 CE1 TYR B 771 5315 2858 4089 736 -1126 -1704 C ATOM 3321 CE2 TYR B 771 24.419 43.073 37.964 1.00 33.29 C ANISOU 3321 CE2 TYR B 771 5457 2936 4256 658 -1334 -1727 C ATOM 3322 CZ TYR B 771 23.235 43.699 37.624 1.00 33.29 C ANISOU 3322 CZ TYR B 771 5470 2921 4259 706 -1253 -1737 C ATOM 3323 OH TYR B 771 23.120 45.065 37.758 1.00 34.38 O ANISOU 3323 OH TYR B 771 5642 2974 4445 725 -1300 -1778 O ATOM 3324 N GLY B 772 25.496 36.973 36.410 1.00 37.62 N ANISOU 3324 N GLY B 772 5777 3806 4710 508 -1156 -1512 N ATOM 3325 CA GLY B 772 25.807 35.550 36.445 1.00 36.14 C ANISOU 3325 CA GLY B 772 5565 3692 4473 492 -1130 -1479 C ATOM 3326 C GLY B 772 27.218 35.227 36.896 1.00 37.82 C ANISOU 3326 C GLY B 772 5768 3895 4708 444 -1235 -1473 C ATOM 3327 O GLY B 772 27.665 35.705 37.937 1.00 40.11 O ANISOU 3327 O GLY B 772 6124 4159 4957 473 -1311 -1515 O TER 3328 GLY B 772 HETATM 3329 PG ACP A 801 20.197 -7.740 42.993 1.00 74.33 P ANISOU 3329 PG ACP A 801 9505 9841 8897 525 614 826 P HETATM 3330 O1G ACP A 801 21.110 -7.915 41.727 1.00 65.50 O ANISOU 3330 O1G ACP A 801 8361 8661 7865 447 530 751 O HETATM 3331 O2G ACP A 801 20.762 -8.616 44.155 1.00 56.49 O ANISOU 3331 O2G ACP A 801 7279 7611 6575 573 625 903 O HETATM 3332 O3G ACP A 801 20.219 -6.312 43.429 1.00 74.33 O ANISOU 3332 O3G ACP A 801 9573 9887 8783 574 605 752 O HETATM 3333 PB ACP A 801 17.975 -6.745 41.424 1.00 50.45 P ANISOU 3333 PB ACP A 801 6383 6775 6010 467 681 806 P HETATM 3334 O1B ACP A 801 18.815 -6.720 40.111 1.00 21.76 O ANISOU 3334 O1B ACP A 801 2737 3086 2446 392 592 717 O HETATM 3335 O2B ACP A 801 16.565 -7.084 41.091 1.00 51.06 O ANISOU 3335 O2B ACP A 801 6384 6832 6185 449 750 881 O HETATM 3336 C3B ACP A 801 18.457 -8.150 42.562 1.00 23.59 C ANISOU 3336 C3B ACP A 801 2991 3391 2582 503 708 914 C HETATM 3337 PA ACP A 801 17.836 -3.905 40.887 1.00 25.32 P ANISOU 3337 PA ACP A 801 3270 3624 2726 492 640 624 P HETATM 3338 O1A ACP A 801 18.752 -3.907 39.672 1.00 23.75 O ANISOU 3338 O1A ACP A 801 3058 3373 2591 417 551 545 O HETATM 3339 O2A ACP A 801 18.029 -2.601 41.630 1.00 24.17 O ANISOU 3339 O2A ACP A 801 3205 3526 2453 558 635 560 O HETATM 3340 O3A ACP A 801 18.141 -5.209 41.870 1.00 25.01 O ANISOU 3340 O3A ACP A 801 3235 3602 2665 521 670 721 O HETATM 3341 O5' ACP A 801 16.360 -3.859 40.308 1.00 30.32 O ANISOU 3341 O5' ACP A 801 3831 4239 3452 472 702 670 O HETATM 3342 C5' ACP A 801 16.303 -3.181 39.081 1.00 30.06 C ANISOU 3342 C5' ACP A 801 3776 4167 3478 416 653 593 C HETATM 3343 C4' ACP A 801 15.016 -3.226 38.359 1.00 29.30 C ANISOU 3343 C4' ACP A 801 3604 4043 3485 384 691 633 C HETATM 3344 O4' ACP A 801 13.851 -2.833 39.192 1.00 30.27 O ANISOU 3344 O4' ACP A 801 3715 4207 3579 449 784 699 O HETATM 3345 C3' ACP A 801 15.171 -2.244 37.312 1.00 28.05 C ANISOU 3345 C3' ACP A 801 3453 3861 3345 347 634 539 C HETATM 3346 O3' ACP A 801 15.407 -2.944 36.102 1.00 29.09 O ANISOU 3346 O3' ACP A 801 3543 3933 3577 269 579 524 O HETATM 3347 C2' ACP A 801 13.977 -1.480 37.269 1.00 28.65 C ANISOU 3347 C2' ACP A 801 3500 3948 3437 369 684 554 C HETATM 3348 O2' ACP A 801 13.115 -2.079 36.287 1.00 29.02 O ANISOU 3348 O2' ACP A 801 3465 3946 3616 307 683 597 O HETATM 3349 C1' ACP A 801 13.414 -1.528 38.622 1.00 29.18 C ANISOU 3349 C1' ACP A 801 3582 4068 3436 449 773 628 C HETATM 3350 N9 ACP A 801 13.884 -0.450 39.415 1.00 27.90 N ANISOU 3350 N9 ACP A 801 3505 3952 3145 516 774 567 N HETATM 3351 C8 ACP A 801 14.867 -0.466 40.341 1.00 27.99 C ANISOU 3351 C8 ACP A 801 3593 3996 3045 561 755 545 C HETATM 3352 N7 ACP A 801 15.032 0.757 40.857 1.00 27.73 N ANISOU 3352 N7 ACP A 801 3632 3994 2910 618 750 477 N HETATM 3353 C5 ACP A 801 14.169 1.610 40.302 1.00 26.78 C ANISOU 3353 C5 ACP A 801 3482 3862 2829 615 772 456 C HETATM 3354 C6 ACP A 801 13.884 2.987 40.435 1.00 27.75 C ANISOU 3354 C6 ACP A 801 3650 4000 2895 659 778 391 C HETATM 3355 N6 ACP A 801 14.606 3.844 41.357 1.00 27.75 N ANISOU 3355 N6 ACP A 801 3755 4031 2759 726 752 322 N HETATM 3356 N1 ACP A 801 12.924 3.540 39.693 1.00 27.79 N ANISOU 3356 N1 ACP A 801 3600 3983 2974 641 802 391 N HETATM 3357 C2 ACP A 801 12.219 2.817 38.805 1.00 25.63 C ANISOU 3357 C2 ACP A 801 3232 3676 2830 578 814 450 C HETATM 3358 N3 ACP A 801 12.459 1.491 38.643 1.00 25.51 N ANISOU 3358 N3 ACP A 801 3176 3643 2873 532 804 509 N HETATM 3359 C4 ACP A 801 13.416 0.858 39.367 1.00 25.40 C ANISOU 3359 C4 ACP A 801 3211 3649 2791 549 787 514 C HETATM 3360 MG MG A 802 18.643 -5.108 37.313 1.00 37.67 MG ANISOU 3360 MG MG A 802 4716 5023 4576 278 497 536 MG HETATM 3361 MG MG A 803 20.166 -5.778 38.656 1.00 28.44 MG ANISOU 3361 MG MG A 803 3608 3889 3307 327 472 558 MG HETATM 3362 O HOH A 901 21.975 -5.658 44.428 1.00 49.10 O ANISOU 3362 O HOH A 901 6492 6733 5431 626 503 670 O HETATM 3363 O HOH A 902 36.857 8.438 18.628 1.00 18.43 O ANISOU 3363 O HOH A 902 2142 2140 2721 -96 43 -133 O HETATM 3364 O HOH A 903 11.759 10.399 43.740 1.00 34.17 O ANISOU 3364 O HOH A 903 4859 4911 3213 1128 939 83 O HETATM 3365 O HOH A 904 8.434 5.322 16.863 1.00 50.54 O ANISOU 3365 O HOH A 904 6102 6160 6942 -287 -187 19 O HETATM 3366 O HOH A 905 20.889 11.478 40.453 1.00 21.42 O ANISOU 3366 O HOH A 905 3342 3057 1740 673 116 -389 O HETATM 3367 O HOH A 906 7.744 -5.262 54.216 1.00 37.24 O ANISOU 3367 O HOH A 906 4896 5673 3581 1555 1938 1756 O HETATM 3368 O HOH A 907 18.233 -3.763 62.872 1.00 53.95 O ANISOU 3368 O HOH A 907 8275 8068 4154 2032 1147 1139 O HETATM 3369 O HOH A 908 19.649 -4.620 26.427 1.00 16.12 O ANISOU 3369 O HOH A 908 1935 1920 2269 -108 150 123 O HETATM 3370 O HOH A 909 6.145 16.088 45.702 1.00 50.41 O ANISOU 3370 O HOH A 909 7051 6992 5110 1655 1415 40 O HETATM 3371 O HOH A 910 42.141 -9.472 28.916 1.00 39.85 O ANISOU 3371 O HOH A 910 4752 4836 5554 181 -19 271 O HETATM 3372 O HOH A 911 11.533 -0.618 34.940 1.00 46.19 O ANISOU 3372 O HOH A 911 5575 6092 5884 277 681 560 O HETATM 3373 O HOH A 912 32.736 -18.836 29.331 1.00 29.87 O ANISOU 3373 O HOH A 912 3700 3283 4365 110 152 438 O HETATM 3374 O HOH A 913 17.685 20.152 5.629 1.00 24.62 O ANISOU 3374 O HOH A 913 3314 2865 3173 -154 -185 -159 O HETATM 3375 O HOH A 914 21.773 -0.747 15.536 1.00 20.02 O ANISOU 3375 O HOH A 914 2709 2238 2660 -193 -52 -268 O HETATM 3376 O HOH A 915 30.413 1.029 8.734 1.00 27.12 O ANISOU 3376 O HOH A 915 3854 3116 3336 52 256 -310 O HETATM 3377 O HOH A 916 38.146 -5.457 20.640 1.00 19.19 O ANISOU 3377 O HOH A 916 2344 2152 2795 99 225 -21 O HETATM 3378 O HOH A 917 19.574 5.070 62.478 1.00 42.39 O ANISOU 3378 O HOH A 917 7312 6434 2359 2122 645 251 O HETATM 3379 O HOH A 918 41.026 -5.597 34.723 1.00 37.92 O ANISOU 3379 O HOH A 918 4617 4801 4991 170 -356 226 O HETATM 3380 O HOH A 919 32.227 -8.145 21.950 1.00 20.13 O ANISOU 3380 O HOH A 919 2594 2237 2818 13 148 -57 O HETATM 3381 O HOH A 920 31.761 -9.393 27.108 1.00 16.37 O ANISOU 3381 O HOH A 920 2039 1862 2320 33 103 109 O HETATM 3382 O HOH A 921 26.140 14.363 32.378 1.00 33.95 O ANISOU 3382 O HOH A 921 4605 4325 3967 187 -263 -556 O HETATM 3383 O HOH A 922 27.176 -3.423 41.432 1.00 20.97 O ANISOU 3383 O HOH A 922 2944 3037 1989 440 92 291 O HETATM 3384 O HOH A 923 25.936 28.654 8.892 1.00 23.53 O ANISOU 3384 O HOH A 923 2899 2482 3560 -200 -90 -48 O HETATM 3385 O HOH A 924 32.148 -11.320 28.635 1.00 17.11 O ANISOU 3385 O HOH A 924 2112 1942 2447 62 106 205 O HETATM 3386 O HOH A 925 30.999 -3.606 35.333 1.00 37.42 O ANISOU 3386 O HOH A 925 4815 4886 4517 181 -57 119 O HETATM 3387 O HOH A 926 34.152 -7.100 33.795 1.00 36.68 O ANISOU 3387 O HOH A 926 4610 4672 4653 149 -66 212 O HETATM 3388 O HOH A 927 34.745 -21.186 27.187 1.00 23.79 O ANISOU 3388 O HOH A 927 2968 2326 3744 166 178 388 O HETATM 3389 O HOH A 928 21.020 -5.504 30.599 1.00 16.91 O ANISOU 3389 O HOH A 928 2049 2140 2238 10 238 249 O HETATM 3390 O HOH A 929 18.891 9.539 13.932 1.00 28.24 O ANISOU 3390 O HOH A 929 3674 3407 3649 -192 -89 -295 O HETATM 3391 O HOH A 930 21.808 12.480 42.808 1.00 45.14 O ANISOU 3391 O HOH A 930 6547 6085 4518 807 22 -487 O HETATM 3392 O HOH A 931 24.519 -6.191 41.462 1.00 34.00 O ANISOU 3392 O HOH A 931 4487 4676 3754 437 306 521 O HETATM 3393 O HOH A 932 11.612 10.185 37.011 1.00 24.36 O ANISOU 3393 O HOH A 932 3223 3453 2580 658 692 43 O HETATM 3394 O HOH A 933 41.798 -23.934 21.210 1.00 29.41 O ANISOU 3394 O HOH A 933 3797 2724 4653 501 436 215 O HETATM 3395 O HOH A 934 33.167 6.819 11.626 1.00 19.82 O ANISOU 3395 O HOH A 934 2607 2296 2627 -22 272 -173 O HETATM 3396 O HOH A 935 18.469 10.483 41.184 1.00 30.36 O ANISOU 3396 O HOH A 935 4440 4264 2833 766 332 -250 O HETATM 3397 O HOH A 936 28.358 2.839 9.730 1.00 19.52 O ANISOU 3397 O HOH A 936 2828 2193 2395 -30 159 -316 O HETATM 3398 O HOH A 937 9.369 19.394 1.306 1.00 40.96 O ANISOU 3398 O HOH A 937 5418 4876 5268 -200 -633 -69 O HETATM 3399 O HOH A 938 38.898 4.830 34.448 1.00 18.89 O ANISOU 3399 O HOH A 938 2367 2397 2413 66 -621 -183 O HETATM 3400 O HOH A 939 8.410 1.960 33.841 1.00 34.07 O ANISOU 3400 O HOH A 939 3924 4550 4471 302 749 572 O HETATM 3401 O HOH B 801 19.522 45.087 31.254 1.00 32.65 O ANISOU 3401 O HOH B 801 5027 2743 4635 614 -922 -1503 O HETATM 3402 O HOH B 802 25.294 31.564 0.942 1.00 74.78 O ANISOU 3402 O HOH B 802 9487 8961 9965 -122 84 369 O HETATM 3403 O HOH B 803 1.159 30.963 9.946 1.00 26.22 O ANISOU 3403 O HOH B 803 2849 2878 4237 125 -312 113 O HETATM 3404 O HOH B 804 22.449 39.167 10.160 1.00 25.69 O ANISOU 3404 O HOH B 804 3105 2302 4356 -170 -358 -82 O HETATM 3405 O HOH B 805 27.535 33.298 2.518 1.00 35.92 O ANISOU 3405 O HOH B 805 4414 3924 5309 -179 77 405 O HETATM 3406 O HOH B 806 13.181 36.578 -1.431 1.00 27.81 O ANISOU 3406 O HOH B 806 3586 2935 4047 -33 -359 407 O HETATM 3407 O HOH B 807 21.994 38.717 2.247 1.00 33.44 O ANISOU 3407 O HOH B 807 4115 3434 5158 -152 -142 394 O HETATM 3408 O HOH B 808 26.942 27.929 15.256 1.00 32.87 O ANISOU 3408 O HOH B 808 4075 3641 4774 -202 -263 -313 O HETATM 3409 O HOH B 809 19.391 32.435 24.793 1.00 23.30 O ANISOU 3409 O HOH B 809 3231 2346 3277 215 -377 -832 O HETATM 3410 O HOH B 810 24.159 30.684 9.131 1.00 24.92 O ANISOU 3410 O HOH B 810 3078 2602 3790 -190 -151 -72 O HETATM 3411 O HOH B 811 5.702 21.388 1.524 1.00 21.55 O ANISOU 3411 O HOH B 811 2778 2384 3027 -207 -759 33 O HETATM 3412 O HOH B 812 7.272 38.118 15.669 1.00 29.05 O ANISOU 3412 O HOH B 812 3536 2960 4540 339 -146 -316 O HETATM 3413 O HOH B 813 15.518 34.750 -3.439 1.00 21.38 O ANISOU 3413 O HOH B 813 2901 2202 3021 -28 -270 468 O HETATM 3414 O HOH B 814 20.392 42.661 28.399 1.00 32.94 O ANISOU 3414 O HOH B 814 4835 2868 4811 432 -872 -1329 O HETATM 3415 O HOH B 815 26.780 28.529 11.475 1.00 16.37 O ANISOU 3415 O HOH B 815 1963 1550 2707 -215 -158 -146 O HETATM 3416 O HOH B 816 27.990 28.663 13.434 1.00 40.51 O ANISOU 3416 O HOH B 816 4993 4571 5827 -230 -226 -209 O CONECT 1214 3360 CONECT 1228 3360 3361 CONECT 1328 3361 CONECT 2341 2348 CONECT 2348 2341 2349 CONECT 2349 2348 2350 2352 CONECT 2350 2349 2351 2364 CONECT 2351 2350 CONECT 2352 2349 2353 CONECT 2353 2352 2354 2355 CONECT 2354 2353 2356 CONECT 2355 2353 2357 CONECT 2356 2354 2358 CONECT 2357 2355 2358 CONECT 2358 2356 2357 2359 CONECT 2359 2358 2360 CONECT 2360 2359 2361 2362 2363 CONECT 2361 2360 CONECT 2362 2360 CONECT 2363 2360 CONECT 2364 2350 CONECT 3329 3330 3331 3332 3336 CONECT 3330 3329 CONECT 3331 3329 CONECT 3332 3329 CONECT 3333 3334 3335 3336 3340 CONECT 3334 3333 3361 CONECT 3335 3333 CONECT 3336 3329 3333 CONECT 3337 3338 3339 3340 3341 CONECT 3338 3337 3360 3361 CONECT 3339 3337 CONECT 3340 3333 3337 CONECT 3341 3337 3342 CONECT 3342 3341 3343 CONECT 3343 3342 3344 3345 CONECT 3344 3343 3349 CONECT 3345 3343 3346 3347 CONECT 3346 3345 CONECT 3347 3345 3348 3349 CONECT 3348 3347 CONECT 3349 3344 3347 3350 CONECT 3350 3349 3351 3359 CONECT 3351 3350 3352 CONECT 3352 3351 3353 CONECT 3353 3352 3354 3359 CONECT 3354 3353 3355 3356 CONECT 3355 3354 CONECT 3356 3354 3357 CONECT 3357 3356 3358 CONECT 3358 3357 3359 CONECT 3359 3350 3353 3358 CONECT 3360 1214 1228 3338 CONECT 3361 1228 1328 3334 3338 MASTER 342 0 4 16 20 0 7 6 3414 2 54 35 END
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Related entries of code: 5eg3
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
Check Database
Protein Sequence Similarity
2fci
RCSB PDB
PDBbind
105aa, >2FCI_2|Chain... at 92%
3gqi
RCSB PDB
PDBbind
226aa, >3GQI_2|Chain... *
Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
No complexes with the same small molecule ligand are found!
Entry Information
PDB ID
5eg3
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
Fibroblast growth factor receptor 2
Ligand Name
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
EC.Number
E.C.2.7.10.1
Resolution
2.61(Å)
Affinity (Kd/Ki/IC50)
Kd=0.135uM
Release Year
2016
Protein/NA Sequence
Check fasta file
Primary Reference
(2016) Mol.Cell Vol. 61: pp. 98-110
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
P10686
P21802
Entrez Gene ID
NCBI Entrez Gene ID:
25738
2263
ASD
Information of known allosteric effects of PDB entries
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