Browse entries in the PDBbind-CN Database
HEADER CALCIUM-BINDING PROTEIN/PROTEIN BINDING 27-JUN-12 4FTG TITLE THE CRYSTAL STRUCTURE OF AN AHNAK PEPTIDE IN COMPLEX WITH THE TITLE 2 S100A10/ANXA2 HETEROTETRAMER COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN S100-A10; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: CALPACTIN I LIGHT CHAIN, CALPACTIN-1 LIGHT CHAIN, CELLULAR COMPND 5 LIGAND OF ANNEXIN II, S100 CALCIUM-BINDING PROTEIN A10, P10 PROTEIN, COMPND 6 P11; COMPND 7 ENGINEERED: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: ANNEXIN A2; COMPND 10 CHAIN: C, D; COMPND 11 FRAGMENT: ANNEXIN A2 N-TERMINAL PEPTIDE (UNP RESIDUES 2-16); COMPND 12 SYNONYM: ANNEXIN II, ANNEXIN-2, CALPACTIN I HEAVY CHAIN, CALPACTIN-1 COMPND 13 HEAVY CHAIN, CHROMOBINDIN-8, LIPOCORTIN II, PLACENTAL ANTICOAGULANT COMPND 14 PROTEIN IV, PAP-IV, PROTEIN I, P36; COMPND 15 ENGINEERED: YES; COMPND 16 MUTATION: YES; COMPND 17 MOL_ID: 3; COMPND 18 MOLECULE: NEUROBLAST DIFFERENTIATION-ASSOCIATED PROTEIN AHNAK; COMPND 19 CHAIN: E; COMPND 20 FRAGMENT: AHNAK PEPTIDE (UNP RESIDUES 5654-5673); COMPND 21 SYNONYM: DESMOYOKIN; COMPND 22 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: ANX2LG, CAL1L, CLP11, S100A10; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 MOL_ID: 2; SOURCE 11 SYNTHETIC: YES; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_COMMON: HUMAN; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 SYNTHETIC: YES; SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 18 ORGANISM_COMMON: HUMAN; SOURCE 19 ORGANISM_TAXID: 9606 KEYWDS MEMBRANE REPAIR, SCAFFOLD, AHNAK, ANNEXIN A2, S100A10, CALCIUM KEYWDS 2 BINDING, INNER-MEMBRANE SURFACE, CALCIUM BINDING PROTEIN-PROTEIN KEYWDS 3 BINDING COMPLEX, CALCIUM-BINDING PROTEIN-PROTEIN BINDING COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR G.OZOROWSKI,H.LUECKE REVDAT 3 15-NOV-17 4FTG 1 REMARK REVDAT 2 20-FEB-13 4FTG 1 JRNL REVDAT 1 02-JAN-13 4FTG 0 JRNL AUTH G.OZOROWSKI,S.MILTON,H.LUECKE JRNL TITL STRUCTURE OF A C-TERMINAL AHNAK PEPTIDE IN A 1:2:2 COMPLEX JRNL TITL 2 WITH S100A10 AND AN ACETYLATED N-TERMINAL PEPTIDE OF ANNEXIN JRNL TITL 3 A2. JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 69 92 2013 JRNL REFN ISSN 0907-4449 JRNL PMID 23275167 JRNL DOI 10.1107/S0907444912043429 REMARK 2 REMARK 2 RESOLUTION. 2.51 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.8_1069 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) : 2.51 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.33 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3 REMARK 3 NUMBER OF REFLECTIONS : 8670 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.185 REMARK 3 R VALUE (WORKING SET) : 0.181 REMARK 3 FREE R VALUE : 0.251 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.790 REMARK 3 FREE R VALUE TEST SET COUNT : 415 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 29.3288 - 3.6119 0.98 2797 141 0.1690 0.2363 REMARK 3 2 3.6119 - 2.8676 0.99 2755 124 0.2102 0.2725 REMARK 3 3 2.8676 - 2.5054 0.98 2703 150 0.1795 0.2729 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) : 0.290 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.390 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 75.37 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 1842 REMARK 3 ANGLE : 1.223 2446 REMARK 3 CHIRALITY : 0.091 266 REMARK 3 PLANARITY : 0.005 304 REMARK 3 DIHEDRAL : 14.760 686 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 5 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN A AND RESID 1:91) REMARK 3 ORIGIN FOR THE GROUP (A): 69.7910 20.7448 48.3782 REMARK 3 T TENSOR REMARK 3 T11: 0.2955 T22: 0.1968 REMARK 3 T33: 0.3500 T12: 0.0580 REMARK 3 T13: 0.0126 T23: -0.0378 REMARK 3 L TENSOR REMARK 3 L11: 0.7510 L22: 0.8162 REMARK 3 L33: 1.7984 L12: 0.4777 REMARK 3 L13: -0.7541 L23: -0.7362 REMARK 3 S TENSOR REMARK 3 S11: -0.1474 S12: 0.0472 S13: -0.5439 REMARK 3 S21: 0.1923 S22: -0.0422 S23: -0.1518 REMARK 3 S31: 0.1132 S32: -0.1129 S33: 0.0003 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN B AND RESID 1:91) REMARK 3 ORIGIN FOR THE GROUP (A): 58.4146 34.5203 41.2357 REMARK 3 T TENSOR REMARK 3 T11: 0.3738 T22: 0.4247 REMARK 3 T33: 0.2332 T12: 0.2531 REMARK 3 T13: -0.0063 T23: 0.0055 REMARK 3 L TENSOR REMARK 3 L11: 1.5349 L22: 1.0832 REMARK 3 L33: 0.9242 L12: 0.2305 REMARK 3 L13: -0.2623 L23: -0.7129 REMARK 3 S TENSOR REMARK 3 S11: -0.2699 S12: 0.6519 S13: 0.0827 REMARK 3 S21: 0.0620 S22: 0.1971 S23: 0.0784 REMARK 3 S31: -0.5334 S32: -0.5756 S33: -0.0185 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN C AND RESID 2:13) REMARK 3 ORIGIN FOR THE GROUP (A): 52.7019 25.0789 33.3291 REMARK 3 T TENSOR REMARK 3 T11: 0.1695 T22: 0.9748 REMARK 3 T33: 0.3785 T12: -0.1566 REMARK 3 T13: -0.2341 T23: -0.1160 REMARK 3 L TENSOR REMARK 3 L11: 0.5553 L22: 0.5757 REMARK 3 L33: 0.2159 L12: 0.4968 REMARK 3 L13: -0.1473 L23: -0.2834 REMARK 3 S TENSOR REMARK 3 S11: -0.0032 S12: 0.1484 S13: 0.3068 REMARK 3 S21: -0.1857 S22: 0.1611 S23: 0.2823 REMARK 3 S31: 0.2278 S32: -0.0215 S33: 0.1697 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN D AND RESID 2:14) REMARK 3 ORIGIN FOR THE GROUP (A): 79.7553 29.2324 49.4202 REMARK 3 T TENSOR REMARK 3 T11: 0.2425 T22: 0.5081 REMARK 3 T33: 0.4105 T12: -0.0895 REMARK 3 T13: -0.0793 T23: 0.0053 REMARK 3 L TENSOR REMARK 3 L11: 0.0218 L22: 0.3857 REMARK 3 L33: 0.0361 L12: 0.0968 REMARK 3 L13: 0.0318 L23: 0.1173 REMARK 3 S TENSOR REMARK 3 S11: 0.0323 S12: -0.0834 S13: 0.0586 REMARK 3 S21: 0.3390 S22: 0.0441 S23: -0.3890 REMARK 3 S31: 0.0071 S32: 0.2641 S33: -0.0012 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: (CHAIN E AND RESID 1:16) REMARK 3 ORIGIN FOR THE GROUP (A): 58.6940 27.0583 50.8682 REMARK 3 T TENSOR REMARK 3 T11: 0.5880 T22: 0.7911 REMARK 3 T33: 0.4469 T12: 0.0375 REMARK 3 T13: 0.1580 T23: -0.0385 REMARK 3 L TENSOR REMARK 3 L11: 0.2523 L22: 0.4748 REMARK 3 L33: 0.3205 L12: 0.0283 REMARK 3 L13: -0.1991 L23: -0.2730 REMARK 3 S TENSOR REMARK 3 S11: 0.1394 S12: 0.1477 S13: -0.6522 REMARK 3 S21: 0.3589 S22: -0.0655 S23: 0.0863 REMARK 3 S31: 0.1517 S32: -0.0622 S33: -0.0008 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 4FTG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-12. REMARK 100 THE DEPOSITION ID IS D_1000073334. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-APR-12 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 8.2.1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL, SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8685 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5 REMARK 200 DATA REDUNDANCY : 3.700 REMARK 200 R MERGE (I) : 0.06500 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54 REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9 REMARK 200 DATA REDUNDANCY IN SHELL : 3.10 REMARK 200 R MERGE FOR SHELL (I) : 0.42000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.54 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 8000 (W/V), 0.1 M TRIS PH 8.5, REMARK 280 10% 2-PROPANOL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K 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 39.53600 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.60800 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 39.53600 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 27.60800 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 300 REMARK: ONE AHNAK PEPTIDE BOUND TO ANXA2/S100A10 HETEROTETRAMER, REMARK 300 FORMED BY A DIMER OF S100A10 BINDING TWO ANXA2 N-TERMINAL PEPTIDES 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: PENTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 9550 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 10600 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E 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 GLN A 92 REMARK 465 LYS A 93 REMARK 465 GLY A 94 REMARK 465 LYS A 95 REMARK 465 LYS A 96 REMARK 465 GLN B 92 REMARK 465 LYS B 93 REMARK 465 GLY B 94 REMARK 465 LYS B 95 REMARK 465 LYS B 96 REMARK 465 GLU C 14 REMARK 465 GLY C 15 REMARK 465 ASP C 16 REMARK 465 NH2 C 17 REMARK 465 GLY D 15 REMARK 465 ASP D 16 REMARK 465 NH2 D 17 REMARK 465 ACE E 0 REMARK 465 GLY E 17 REMARK 465 ARG E 18 REMARK 465 GLU E 19 REMARK 465 LEU E 20 REMARK 465 NH2 E 21 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ACE C 1 O - C - N ANGL. DEV. = 13.6 DEGREES REMARK 500 SER C 2 C - N - CA ANGL. DEV. = -15.3 DEGREES REMARK 500 SER D 2 C - N - CA ANGL. DEV. = -17.0 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 PRO B 48 11.21 -63.93 REMARK 500 HIS B 89 -82.50 -118.63 REMARK 500 MET B 90 -2.91 -52.52 REMARK 500 LYS C 10 53.22 -119.17 REMARK 500 LYS E 9 42.67 71.72 REMARK 500 PHE E 15 78.02 50.71 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A 101 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA B 101 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA E 101 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1BT6 RELATED DB: PDB REMARK 900 P11 (S100A10), LIGAND OF ANNEXIN II IN COMPLEX WITH ANNEXIN II N- REMARK 900 TERMINUS DBREF 4FTG A 1 96 UNP P60903 S10AA_HUMAN 2 97 DBREF 4FTG B 1 96 UNP P60903 S10AA_HUMAN 2 97 DBREF 4FTG C 2 16 UNP P07355 ANXA2_HUMAN 2 16 DBREF 4FTG D 2 16 UNP P07355 ANXA2_HUMAN 2 16 DBREF 4FTG E 1 20 UNP Q09666 AHNK_HUMAN 5654 5673 SEQADV 4FTG ACE C 1 UNP P07355 ACETYLATION SEQADV 4FTG SER C 9 UNP P07355 CYS 9 ENGINEERED MUTATION SEQADV 4FTG NH2 C 17 UNP P07355 AMIDATION SEQADV 4FTG ACE D 1 UNP P07355 ACETYLATION SEQADV 4FTG SER D 9 UNP P07355 CYS 9 ENGINEERED MUTATION SEQADV 4FTG NH2 D 17 UNP P07355 AMIDATION SEQADV 4FTG ACE E 0 UNP Q09666 ACETYLATION SEQADV 4FTG NH2 E 21 UNP Q09666 AMIDATION SEQRES 1 A 96 PRO SER GLN MET GLU HIS ALA MET GLU THR MET MET PHE SEQRES 2 A 96 THR PHE HIS LYS PHE ALA GLY ASP LYS GLY TYR LEU THR SEQRES 3 A 96 LYS GLU ASP LEU ARG VAL LEU MET GLU LYS GLU PHE PRO SEQRES 4 A 96 GLY PHE LEU GLU ASN GLN LYS ASP PRO LEU ALA VAL ASP SEQRES 5 A 96 LYS ILE MET LYS ASP LEU ASP GLN CYS ARG ASP GLY LYS SEQRES 6 A 96 VAL GLY PHE GLN SER PHE PHE SER LEU ILE ALA GLY LEU SEQRES 7 A 96 THR ILE ALA CYS ASN ASP TYR PHE VAL VAL HIS MET LYS SEQRES 8 A 96 GLN LYS GLY LYS LYS SEQRES 1 B 96 PRO SER GLN MET GLU HIS ALA MET GLU THR MET MET PHE SEQRES 2 B 96 THR PHE HIS LYS PHE ALA GLY ASP LYS GLY TYR LEU THR SEQRES 3 B 96 LYS GLU ASP LEU ARG VAL LEU MET GLU LYS GLU PHE PRO SEQRES 4 B 96 GLY PHE LEU GLU ASN GLN LYS ASP PRO LEU ALA VAL ASP SEQRES 5 B 96 LYS ILE MET LYS ASP LEU ASP GLN CYS ARG ASP GLY LYS SEQRES 6 B 96 VAL GLY PHE GLN SER PHE PHE SER LEU ILE ALA GLY LEU SEQRES 7 B 96 THR ILE ALA CYS ASN ASP TYR PHE VAL VAL HIS MET LYS SEQRES 8 B 96 GLN LYS GLY LYS LYS SEQRES 1 C 17 ACE SER THR VAL HIS GLU ILE LEU SER LYS LEU SER LEU SEQRES 2 C 17 GLU GLY ASP NH2 SEQRES 1 D 17 ACE SER THR VAL HIS GLU ILE LEU SER LYS LEU SER LEU SEQRES 2 D 17 GLU GLY ASP NH2 SEQRES 1 E 22 ACE GLY LYS VAL THR PHE PRO LYS MET LYS ILE PRO LYS SEQRES 2 E 22 PHE THR PHE SER GLY ARG GLU LEU NH2 HET ACE C 1 3 HET ACE D 1 3 HET IPA A 101 4 HET IPA B 101 4 HET IPA E 101 4 HETNAM ACE ACETYL GROUP HETNAM IPA ISOPROPYL ALCOHOL HETSYN IPA 2-PROPANOL FORMUL 3 ACE 2(C2 H4 O) FORMUL 6 IPA 3(C3 H8 O) FORMUL 9 HOH *8(H2 O) HELIX 1 1 SER A 2 GLY A 20 1 19 HELIX 2 2 THR A 26 PHE A 38 1 13 HELIX 3 3 PHE A 38 GLU A 43 1 6 HELIX 4 4 LEU A 49 ASP A 59 1 11 HELIX 5 5 GLY A 67 MET A 90 1 24 HELIX 6 6 SER B 2 GLY B 20 1 19 HELIX 7 7 THR B 26 PHE B 38 1 13 HELIX 8 8 PHE B 38 GLN B 45 1 8 HELIX 9 9 LEU B 49 ASP B 59 1 11 HELIX 10 10 GLY B 67 HIS B 89 1 23 HELIX 11 11 SER C 2 SER C 9 1 8 HELIX 12 12 SER D 2 SER D 9 1 8 SHEET 1 A 2 SER D 12 LEU D 13 0 SHEET 2 A 2 LYS E 2 VAL E 3 1 O VAL E 3 N SER D 12 SSBOND 1 CYS A 61 CYS A 61 1555 2757 2.05 SSBOND 2 CYS B 61 CYS B 61 1555 2757 2.04 LINK C ACE C 1 N SER C 2 1555 1555 1.34 LINK C ACE D 1 N SER D 2 1555 1555 1.34 CISPEP 1 MET E 8 LYS E 9 0 22.16 CISPEP 2 PHE E 15 SER E 16 0 -3.52 SITE 1 AC1 7 PRO A 1 HIS A 6 ALA A 7 THR A 10 SITE 2 AC1 7 GLN B 3 HIS B 6 ALA B 7 SITE 1 AC2 4 PRO A 1 HIS B 6 GLU B 9 THR B 10 SITE 1 AC3 4 GLY A 77 LYS E 2 VAL E 3 THR E 4 CRYST1 79.072 55.216 63.140 90.00 111.73 90.00 C 1 2 1 8 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 0.012647 0.000000 0.005040 0.00000 SCALE2 0.000000 0.018111 0.000000 0.00000 SCALE3 0.000000 0.000000 0.017049 0.00000 ATOM 1 N PRO A 1 61.759 28.625 26.656 1.00 56.52 N ANISOU 1 N PRO A 1 6132 8968 6375 -155 99 -1627 N ATOM 2 CA PRO A 1 61.337 29.148 27.958 1.00 50.36 C ANISOU 2 CA PRO A 1 5391 8187 5555 -11 85 -1539 C ATOM 3 C PRO A 1 62.267 30.224 28.520 1.00 47.40 C ANISOU 3 C PRO A 1 5143 7656 5211 152 47 -1437 C ATOM 4 O PRO A 1 63.323 30.511 27.952 1.00 56.69 O ANISOU 4 O PRO A 1 6373 8720 6446 149 28 -1440 O ATOM 5 CB PRO A 1 61.358 27.901 28.842 1.00 50.27 C ANISOU 5 CB PRO A 1 5407 8061 5630 -78 140 -1626 C ATOM 6 CG PRO A 1 60.931 26.817 27.921 1.00 56.68 C ANISOU 6 CG PRO A 1 6134 8956 6447 -284 178 -1745 C ATOM 7 CD PRO A 1 61.452 27.190 26.532 1.00 59.60 C ANISOU 7 CD PRO A 1 6483 9348 6813 -330 159 -1750 C ATOM 8 N SER A 2 61.860 30.813 29.641 1.00 42.77 N ANISOU 8 N SER A 2 4608 7064 4581 285 44 -1340 N ATOM 9 CA SER A 2 62.604 31.897 30.272 1.00 42.62 C ANISOU 9 CA SER A 2 4722 6903 4570 424 13 -1234 C ATOM 10 C SER A 2 63.802 31.365 31.064 1.00 41.75 C ANISOU 10 C SER A 2 4720 6565 4580 421 15 -1268 C ATOM 11 O SER A 2 63.941 30.157 31.265 1.00 36.83 O ANISOU 11 O SER A 2 4070 5883 4041 336 50 -1364 O ATOM 12 CB SER A 2 61.681 32.650 31.226 1.00 34.95 C ANISOU 12 CB SER A 2 3777 5993 3508 559 24 -1112 C ATOM 13 OG SER A 2 61.275 31.788 32.281 1.00 41.89 O ANISOU 13 OG SER A 2 4655 6846 4417 556 67 -1137 O ATOM 14 N GLN A 3 64.647 32.274 31.530 1.00 41.52 N ANISOU 14 N GLN A 3 4810 6410 4557 507 -16 -1185 N ATOM 15 CA GLN A 3 65.738 31.886 32.400 1.00 45.28 C ANISOU 15 CA GLN A 3 5380 6699 5126 515 -22 -1193 C ATOM 16 C GLN A 3 65.185 31.234 33.654 1.00 43.31 C ANISOU 16 C GLN A 3 5146 6417 4892 549 10 -1197 C ATOM 17 O GLN A 3 65.656 30.169 34.059 1.00 42.52 O ANISOU 17 O GLN A 3 5045 6214 4898 500 32 -1268 O ATOM 18 CB GLN A 3 66.611 33.083 32.744 1.00 40.41 C ANISOU 18 CB GLN A 3 4885 5986 4484 587 -61 -1096 C ATOM 19 CG GLN A 3 67.502 33.521 31.598 1.00 42.07 C ANISOU 19 CG GLN A 3 5086 6184 4714 541 -85 -1105 C ATOM 20 CD GLN A 3 68.465 32.436 31.165 1.00 56.33 C ANISOU 20 CD GLN A 3 6854 7913 6635 453 -74 -1197 C ATOM 21 OE1 GLN A 3 68.099 31.544 30.407 1.00 66.12 O ANISOU 21 OE1 GLN A 3 8000 9211 7911 372 -44 -1284 O ATOM 22 NE2 GLN A 3 69.705 32.498 31.654 1.00 49.47 N ANISOU 22 NE2 GLN A 3 6058 6917 5822 465 -95 -1177 N ATOM 23 N MET A 4 64.168 31.849 34.250 1.00 35.73 N ANISOU 23 N MET A 4 4200 5541 3833 636 23 -1115 N ATOM 24 CA MET A 4 63.553 31.281 35.459 1.00 30.66 C ANISOU 24 CA MET A 4 3572 4880 3199 677 62 -1103 C ATOM 25 C MET A 4 62.953 29.893 35.207 1.00 37.58 C ANISOU 25 C MET A 4 4328 5790 4159 549 99 -1174 C ATOM 26 O MET A 4 63.105 28.980 36.022 1.00 46.53 O ANISOU 26 O MET A 4 5484 6798 5398 512 119 -1174 O ATOM 27 CB MET A 4 62.500 32.228 36.043 1.00 29.50 C ANISOU 27 CB MET A 4 3455 4822 2931 793 81 -977 C ATOM 28 CG MET A 4 63.084 33.412 36.843 1.00 32.56 C ANISOU 28 CG MET A 4 4013 5078 3281 889 55 -862 C ATOM 29 SD MET A 4 64.306 32.889 38.083 1.00 43.84 S ANISOU 29 SD MET A 4 5571 6293 4794 887 33 -880 S ATOM 30 CE MET A 4 63.289 32.090 39.326 1.00 36.14 C ANISOU 30 CE MET A 4 4583 5298 3851 898 82 -822 C ATOM 31 N GLU A 5 62.279 29.714 34.078 1.00 38.61 N ANISOU 31 N GLU A 5 4336 6091 4241 471 111 -1234 N ATOM 32 CA GLU A 5 61.656 28.410 33.804 1.00 42.34 C ANISOU 32 CA GLU A 5 4705 6604 4777 326 152 -1307 C ATOM 33 C GLU A 5 62.709 27.327 33.666 1.00 40.42 C ANISOU 33 C GLU A 5 4494 6184 4680 229 170 -1414 C ATOM 34 O GLU A 5 62.506 26.185 34.112 1.00 42.41 O ANISOU 34 O GLU A 5 4733 6354 5027 148 214 -1443 O ATOM 35 CB GLU A 5 60.752 28.460 32.568 1.00 45.87 C ANISOU 35 CB GLU A 5 5016 7287 5125 241 155 -1350 C ATOM 36 CG GLU A 5 59.474 29.261 32.807 1.00 55.81 C ANISOU 36 CG GLU A 5 6211 8740 6255 331 155 -1225 C ATOM 37 CD GLU A 5 58.661 29.508 31.536 1.00 60.65 C ANISOU 37 CD GLU A 5 6681 9611 6753 264 144 -1242 C ATOM 38 OE1 GLU A 5 59.275 29.823 30.485 1.00 63.94 O ANISOU 38 OE1 GLU A 5 7094 10060 7140 231 118 -1314 O ATOM 39 OE2 GLU A 5 57.409 29.383 31.594 1.00 49.04 O ANISOU 39 OE2 GLU A 5 5096 8321 5217 241 162 -1177 O ATOM 40 N HIS A 6 63.840 27.695 33.059 1.00 36.97 N ANISOU 40 N HIS A 6 4101 5683 4262 244 145 -1465 N ATOM 41 CA HIS A 6 64.958 26.765 32.896 1.00 33.08 C ANISOU 41 CA HIS A 6 3639 5018 3911 176 171 -1552 C ATOM 42 C HIS A 6 65.544 26.363 34.234 1.00 35.05 C ANISOU 42 C HIS A 6 3972 5076 4270 235 174 -1481 C ATOM 43 O HIS A 6 65.646 25.177 34.532 1.00 33.62 O ANISOU 43 O HIS A 6 3786 4782 4206 165 225 -1519 O ATOM 44 CB HIS A 6 66.039 27.321 31.965 1.00 33.09 C ANISOU 44 CB HIS A 6 3665 4989 3920 179 135 -1556 C ATOM 45 CG HIS A 6 65.757 27.053 30.517 1.00 45.87 C ANISOU 45 CG HIS A 6 5199 6715 5512 60 152 -1627 C ATOM 46 ND1 HIS A 6 65.635 25.778 30.013 1.00 47.10 N ANISOU 46 ND1 HIS A 6 5312 6842 5742 -78 219 -1737 N ATOM 47 CD2 HIS A 6 65.535 27.896 29.478 1.00 37.32 C ANISOU 47 CD2 HIS A 6 4075 5769 4337 54 116 -1600 C ATOM 48 CE1 HIS A 6 65.358 25.842 28.722 1.00 38.38 C ANISOU 48 CE1 HIS A 6 4144 5858 4583 -169 221 -1776 C ATOM 49 NE2 HIS A 6 65.292 27.117 28.375 1.00 39.19 N ANISOU 49 NE2 HIS A 6 4238 6066 4587 -87 157 -1694 N ATOM 50 N ALA A 7 65.899 27.361 35.039 1.00 35.22 N ANISOU 50 N ALA A 7 4077 5062 4243 357 122 -1376 N ATOM 51 CA ALA A 7 66.390 27.150 36.389 1.00 36.63 C ANISOU 51 CA ALA A 7 4339 5083 4494 414 111 -1290 C ATOM 52 C ALA A 7 65.427 26.280 37.205 1.00 41.46 C ANISOU 52 C ALA A 7 4928 5678 5146 381 156 -1259 C ATOM 53 O ALA A 7 65.869 25.311 37.835 1.00 36.22 O ANISOU 53 O ALA A 7 4285 4869 4607 353 183 -1254 O ATOM 54 CB ALA A 7 66.616 28.493 37.075 1.00 41.98 C ANISOU 54 CB ALA A 7 5117 5765 5068 532 52 -1184 C ATOM 55 N MET A 8 64.126 26.610 37.187 1.00 35.61 N ANISOU 55 N MET A 8 4138 5090 4302 387 168 -1230 N ATOM 56 CA MET A 8 63.117 25.799 37.902 1.00 36.34 C ANISOU 56 CA MET A 8 4196 5189 4423 346 214 -1200 C ATOM 57 C MET A 8 63.108 24.339 37.472 1.00 34.02 C ANISOU 57 C MET A 8 3844 4835 4246 204 273 -1303 C ATOM 58 O MET A 8 63.124 23.414 38.310 1.00 35.64 O ANISOU 58 O MET A 8 4077 4913 4552 177 310 -1281 O ATOM 59 CB MET A 8 61.718 26.391 37.759 1.00 29.33 C ANISOU 59 CB MET A 8 3239 4504 3402 368 221 -1153 C ATOM 60 CG MET A 8 61.553 27.668 38.509 1.00 25.13 C ANISOU 60 CG MET A 8 2789 3995 2765 518 193 -1033 C ATOM 61 SD MET A 8 60.274 28.755 37.842 1.00 40.72 S ANISOU 61 SD MET A 8 4679 6226 4567 582 199 -980 S ATOM 62 CE MET A 8 58.811 27.875 38.371 1.00 31.71 C ANISOU 62 CE MET A 8 3433 5183 3432 521 255 -940 C ATOM 63 N GLU A 9 63.124 24.122 36.168 1.00 38.33 N ANISOU 63 N GLU A 9 4322 5462 4780 109 289 -1414 N ATOM 64 CA GLU A 9 63.138 22.759 35.662 1.00 37.06 C ANISOU 64 CA GLU A 9 4126 5236 4718 -38 359 -1526 C ATOM 65 C GLU A 9 64.353 21.975 36.127 1.00 45.10 C ANISOU 65 C GLU A 9 5220 6018 5897 -24 392 -1537 C ATOM 66 O GLU A 9 64.217 20.774 36.450 1.00 46.80 O ANISOU 66 O GLU A 9 5444 6123 6215 -103 462 -1568 O ATOM 67 CB GLU A 9 63.062 22.748 34.144 1.00 40.65 C ANISOU 67 CB GLU A 9 4513 5814 5119 -145 371 -1648 C ATOM 68 CG GLU A 9 63.136 21.343 33.550 1.00 52.43 C ANISOU 68 CG GLU A 9 5994 7223 6706 -311 458 -1777 C ATOM 69 CD GLU A 9 62.483 21.273 32.206 1.00 61.62 C ANISOU 69 CD GLU A 9 7075 8569 7770 -456 472 -1884 C ATOM 70 OE1 GLU A 9 61.343 21.777 32.100 1.00 63.78 O ANISOU 70 OE1 GLU A 9 7265 9053 7916 -473 436 -1838 O ATOM 71 OE2 GLU A 9 63.110 20.747 31.255 1.00 65.28 O ANISOU 71 OE2 GLU A 9 7553 8973 8275 -549 519 -2007 O ATOM 72 N THR A 10 65.532 22.624 36.164 1.00 43.49 N ANISOU 72 N THR A 10 5070 5739 5716 72 345 -1507 N ATOM 73 CA THR A 10 66.730 21.871 36.540 1.00 40.88 C ANISOU 73 CA THR A 10 4791 5201 5539 89 377 -1504 C ATOM 74 C THR A 10 66.620 21.494 37.996 1.00 37.79 C ANISOU 74 C THR A 10 4450 4702 5208 142 377 -1392 C ATOM 75 O THR A 10 67.031 20.403 38.394 1.00 51.24 O ANISOU 75 O THR A 10 6173 6249 7046 116 438 -1393 O ATOM 76 CB THR A 10 68.123 22.501 36.146 1.00 39.10 C ANISOU 76 CB THR A 10 4594 4923 5338 159 334 -1500 C ATOM 77 OG1 THR A 10 68.760 23.077 37.280 1.00 44.36 O ANISOU 77 OG1 THR A 10 5325 5518 6011 270 269 -1370 O ATOM 78 CG2 THR A 10 68.006 23.506 35.071 1.00 36.16 C ANISOU 78 CG2 THR A 10 4190 4709 4841 156 292 -1553 C ATOM 79 N MET A 11 65.999 22.365 38.776 1.00 30.62 N ANISOU 79 N MET A 11 3563 3876 4194 215 319 -1294 N ATOM 80 CA MET A 11 65.714 22.034 40.167 1.00 37.13 C ANISOU 80 CA MET A 11 4436 4617 5053 254 321 -1189 C ATOM 81 C MET A 11 64.734 20.872 40.283 1.00 44.87 C ANISOU 81 C MET A 11 5375 5589 6083 153 401 -1229 C ATOM 82 O MET A 11 64.952 19.951 41.066 1.00 53.83 O ANISOU 82 O MET A 11 6544 6578 7329 143 442 -1192 O ATOM 83 CB MET A 11 65.244 23.262 40.953 1.00 24.40 C ANISOU 83 CB MET A 11 2872 3091 3307 353 256 -1081 C ATOM 84 CG MET A 11 66.318 24.330 41.034 1.00 26.11 C ANISOU 84 CG MET A 11 3158 3283 3482 440 182 -1033 C ATOM 85 SD MET A 11 66.008 25.571 42.321 1.00 42.48 S ANISOU 85 SD MET A 11 5340 5379 5420 552 124 -892 S ATOM 86 CE MET A 11 65.674 24.410 43.627 1.00114.64 C ANISOU 86 CE MET A 11 14500 14399 14659 530 165 -824 C ATOM 87 N MET A 12 63.682 20.894 39.473 1.00 46.57 N ANISOU 87 N MET A 12 5515 5963 6216 70 423 -1301 N ATOM 88 CA MET A 12 62.748 19.775 39.441 1.00 47.27 C ANISOU 88 CA MET A 12 5560 6060 6340 -57 499 -1352 C ATOM 89 C MET A 12 63.445 18.489 39.049 1.00 45.45 C ANISOU 89 C MET A 12 5352 5658 6257 -147 582 -1443 C ATOM 90 O MET A 12 63.340 17.466 39.730 1.00 51.00 O ANISOU 90 O MET A 12 6087 6231 7058 -186 644 -1426 O ATOM 91 CB MET A 12 61.616 20.041 38.452 1.00 54.75 C ANISOU 91 CB MET A 12 6408 7230 7163 -150 501 -1418 C ATOM 92 CG MET A 12 60.395 19.159 38.689 1.00 59.81 C ANISOU 92 CG MET A 12 6998 7929 7799 -272 560 -1430 C ATOM 93 SD MET A 12 58.884 19.814 37.948 1.00 58.19 S ANISOU 93 SD MET A 12 6657 8039 7413 -336 534 -1430 S ATOM 94 CE MET A 12 59.082 19.177 36.270 1.00 56.43 C ANISOU 94 CE MET A 12 6385 7866 7190 -524 572 -1609 C ATOM 95 N PHE A 13 64.177 18.545 37.948 1.00 50.18 N ANISOU 95 N PHE A 13 5941 6251 6873 -175 591 -1538 N ATOM 96 CA PHE A 13 64.797 17.337 37.410 1.00 48.03 C ANISOU 96 CA PHE A 13 5695 5820 6733 -264 691 -1638 C ATOM 97 C PHE A 13 65.924 16.772 38.259 1.00 42.85 C ANISOU 97 C PHE A 13 5110 4939 6234 -173 721 -1564 C ATOM 98 O PHE A 13 66.106 15.559 38.311 1.00 38.00 O ANISOU 98 O PHE A 13 4529 4167 5740 -235 824 -1604 O ATOM 99 CB PHE A 13 65.230 17.564 35.969 1.00 45.61 C ANISOU 99 CB PHE A 13 5361 5577 6393 -322 702 -1761 C ATOM 100 CG PHE A 13 64.076 17.579 35.014 1.00 53.24 C ANISOU 100 CG PHE A 13 6256 6736 7234 -468 712 -1858 C ATOM 101 CD1 PHE A 13 62.786 17.350 35.479 1.00 48.81 C ANISOU 101 CD1 PHE A 13 5656 6280 6612 -537 715 -1827 C ATOM 102 CD2 PHE A 13 64.266 17.799 33.665 1.00 58.92 C ANISOU 102 CD2 PHE A 13 6946 7546 7897 -543 719 -1972 C ATOM 103 CE1 PHE A 13 61.700 17.332 34.617 1.00 54.06 C ANISOU 103 CE1 PHE A 13 6239 7145 7156 -684 719 -1902 C ATOM 104 CE2 PHE A 13 63.181 17.791 32.790 1.00 65.30 C ANISOU 104 CE2 PHE A 13 7681 8551 8579 -692 722 -2051 C ATOM 105 CZ PHE A 13 61.889 17.550 33.273 1.00 53.53 C ANISOU 105 CZ PHE A 13 6139 7173 7025 -765 720 -2012 C ATOM 106 N THR A 14 66.652 17.658 38.937 1.00 44.33 N ANISOU 106 N THR A 14 5320 5113 6410 -32 632 -1450 N ATOM 107 CA THR A 14 67.734 17.264 39.830 1.00 45.02 C ANISOU 107 CA THR A 14 5459 5020 6628 61 638 -1350 C ATOM 108 C THR A 14 67.177 16.408 40.958 1.00 48.19 C ANISOU 108 C THR A 14 5892 5326 7092 47 682 -1280 C ATOM 109 O THR A 14 67.744 15.359 41.299 1.00 46.42 O ANISOU 109 O THR A 14 5701 4923 7013 50 760 -1259 O ATOM 110 CB THR A 14 68.434 18.505 40.431 1.00 47.99 C ANISOU 110 CB THR A 14 5855 5437 6941 190 518 -1233 C ATOM 111 OG1 THR A 14 69.099 19.241 39.391 1.00 42.22 O ANISOU 111 OG1 THR A 14 5100 4774 6167 204 483 -1294 O ATOM 112 CG2 THR A 14 69.437 18.096 41.506 1.00 40.37 C ANISOU 112 CG2 THR A 14 4932 4312 6094 274 510 -1106 C ATOM 113 N PHE A 15 66.059 16.858 41.528 1.00 49.47 N ANISOU 113 N PHE A 15 6046 5607 7145 38 639 -1237 N ATOM 114 CA PHE A 15 65.371 16.084 42.552 1.00 44.56 C ANISOU 114 CA PHE A 15 5449 4917 6565 12 682 -1176 C ATOM 115 C PHE A 15 65.132 14.676 42.058 1.00 49.21 C ANISOU 115 C PHE A 15 6041 5399 7259 -115 811 -1277 C ATOM 116 O PHE A 15 65.500 13.698 42.719 1.00 57.31 O ANISOU 116 O PHE A 15 7116 6248 8414 -106 878 -1231 O ATOM 117 CB PHE A 15 64.013 16.694 42.936 1.00 40.18 C ANISOU 117 CB PHE A 15 4865 4533 5868 -6 642 -1145 C ATOM 118 CG PHE A 15 63.285 15.900 43.999 1.00 40.38 C ANISOU 118 CG PHE A 15 4915 4494 5933 -37 689 -1081 C ATOM 119 CD1 PHE A 15 63.745 15.895 45.326 1.00 39.14 C ANISOU 119 CD1 PHE A 15 4823 4226 5823 60 659 -944 C ATOM 120 CD2 PHE A 15 62.182 15.121 43.677 1.00 41.26 C ANISOU 120 CD2 PHE A 15 4987 4655 6035 -175 763 -1155 C ATOM 121 CE1 PHE A 15 63.099 15.144 46.329 1.00 35.54 C ANISOU 121 CE1 PHE A 15 4394 3704 5404 31 705 -881 C ATOM 122 CE2 PHE A 15 61.518 14.365 44.670 1.00 44.67 C ANISOU 122 CE2 PHE A 15 5443 5024 6504 -209 811 -1094 C ATOM 123 CZ PHE A 15 61.981 14.377 45.994 1.00 45.61 C ANISOU 123 CZ PHE A 15 5630 5027 6674 -101 783 -958 C ATOM 124 N HIS A 16 64.516 14.578 40.888 1.00 45.73 N ANISOU 124 N HIS A 16 5554 5065 6756 -238 848 -1413 N ATOM 125 CA HIS A 16 64.028 13.287 40.409 1.00 48.64 C ANISOU 125 CA HIS A 16 5937 5357 7188 -394 973 -1522 C ATOM 126 C HIS A 16 65.148 12.366 39.984 1.00 48.94 C ANISOU 126 C HIS A 16 6032 5182 7380 -395 1077 -1577 C ATOM 127 O HIS A 16 65.040 11.156 40.132 1.00 55.29 O ANISOU 127 O HIS A 16 6890 5833 8285 -472 1195 -1610 O ATOM 128 CB HIS A 16 62.986 13.466 39.305 1.00 45.79 C ANISOU 128 CB HIS A 16 5507 5194 6696 -545 976 -1645 C ATOM 129 CG HIS A 16 61.670 13.947 39.821 1.00 52.94 C ANISOU 129 CG HIS A 16 6353 6285 7477 -570 919 -1586 C ATOM 130 ND1 HIS A 16 60.945 13.246 40.759 1.00 59.47 N ANISOU 130 ND1 HIS A 16 7198 7063 8335 -612 962 -1530 N ATOM 131 CD2 HIS A 16 60.963 15.070 39.560 1.00 62.27 C ANISOU 131 CD2 HIS A 16 7457 7699 8506 -545 831 -1560 C ATOM 132 CE1 HIS A 16 59.837 13.906 41.042 1.00 61.97 C ANISOU 132 CE1 HIS A 16 7444 7578 8522 -616 903 -1476 C ATOM 133 NE2 HIS A 16 59.823 15.018 40.328 1.00 66.13 N ANISOU 133 NE2 HIS A 16 7911 8277 8938 -570 826 -1489 N ATOM 134 N LYS A 17 66.227 12.960 39.480 1.00 46.16 N ANISOU 134 N LYS A 17 5673 4820 7047 -304 1038 -1578 N ATOM 135 CA LYS A 17 67.430 12.246 39.120 1.00 45.21 C ANISOU 135 CA LYS A 17 5597 4506 7075 -268 1132 -1604 C ATOM 136 C LYS A 17 68.033 11.524 40.327 1.00 50.90 C ANISOU 136 C LYS A 17 6369 5030 7942 -169 1173 -1469 C ATOM 137 O LYS A 17 68.511 10.389 40.219 1.00 49.20 O ANISOU 137 O LYS A 17 6206 4620 7867 -186 1308 -1494 O ATOM 138 CB LYS A 17 68.448 13.230 38.529 1.00 53.11 C ANISOU 138 CB LYS A 17 6564 5566 8050 -171 1056 -1598 C ATOM 139 CG LYS A 17 69.834 12.636 38.215 1.00 51.74 C ANISOU 139 CG LYS A 17 6417 5216 8024 -103 1138 -1586 C ATOM 140 CD LYS A 17 70.761 13.698 37.657 1.00 51.36 C ANISOU 140 CD LYS A 17 6327 5264 7926 -19 1044 -1562 C ATOM 141 CE LYS A 17 72.149 13.156 37.371 1.00 55.74 C ANISOU 141 CE LYS A 17 6890 5702 8587 51 1097 -1492 C ATOM 142 NZ LYS A 17 73.032 14.262 36.921 1.00 62.20 N ANISOU 142 NZ LYS A 17 7663 6617 9353 127 1000 -1465 N ATOM 143 N PHE A 18 68.018 12.177 41.479 1.00 51.88 N ANISOU 143 N PHE A 18 6482 5199 8030 -66 1062 -1320 N ATOM 144 CA PHE A 18 68.538 11.532 42.677 1.00 58.36 C ANISOU 144 CA PHE A 18 7345 5854 8974 22 1089 -1178 C ATOM 145 C PHE A 18 67.478 10.836 43.530 1.00 56.56 C ANISOU 145 C PHE A 18 7150 5591 8747 -45 1131 -1147 C ATOM 146 O PHE A 18 67.818 9.972 44.343 1.00 55.92 O ANISOU 146 O PHE A 18 7116 5342 8789 -3 1195 -1057 O ATOM 147 CB PHE A 18 69.340 12.525 43.511 1.00 57.67 C ANISOU 147 CB PHE A 18 7241 5810 8860 168 953 -1022 C ATOM 148 CG PHE A 18 70.533 13.051 42.803 1.00 55.24 C ANISOU 148 CG PHE A 18 6902 5509 8577 238 923 -1030 C ATOM 149 CD1 PHE A 18 71.728 12.364 42.834 1.00 52.89 C ANISOU 149 CD1 PHE A 18 6609 5050 8437 313 993 -971 C ATOM 150 CD2 PHE A 18 70.454 14.215 42.070 1.00 53.63 C ANISOU 150 CD2 PHE A 18 6661 5474 8241 229 833 -1093 C ATOM 151 CE1 PHE A 18 72.835 12.848 42.167 1.00 50.58 C ANISOU 151 CE1 PHE A 18 6279 4773 8167 376 968 -973 C ATOM 152 CE2 PHE A 18 71.554 14.696 41.403 1.00 51.72 C ANISOU 152 CE2 PHE A 18 6391 5240 8019 286 807 -1101 C ATOM 153 CZ PHE A 18 72.746 14.008 41.451 1.00 49.10 C ANISOU 153 CZ PHE A 18 6058 4754 7844 357 874 -1042 C ATOM 154 N ALA A 19 66.209 11.208 43.363 1.00 49.90 N ANISOU 154 N ALA A 19 6279 4910 7770 -144 1097 -1210 N ATOM 155 CA ALA A 19 65.148 10.542 44.114 1.00 56.62 C ANISOU 155 CA ALA A 19 7154 5743 8616 -221 1142 -1186 C ATOM 156 C ALA A 19 64.741 9.223 43.453 1.00 69.80 C ANISOU 156 C ALA A 19 8863 7299 10359 -377 1299 -1315 C ATOM 157 O ALA A 19 64.128 8.356 44.089 1.00 72.74 O ANISOU 157 O ALA A 19 9277 7587 10774 -442 1371 -1292 O ATOM 158 CB ALA A 19 63.944 11.442 44.267 1.00 50.50 C ANISOU 158 CB ALA A 19 6324 5192 7671 -258 1051 -1182 C ATOM 159 N GLY A 20 65.080 9.081 42.177 1.00 67.99 N ANISOU 159 N GLY A 20 8631 7066 10138 -445 1356 -1453 N ATOM 160 CA GLY A 20 64.664 7.928 41.400 1.00 70.24 C ANISOU 160 CA GLY A 20 8967 7257 10463 -618 1508 -1598 C ATOM 161 C GLY A 20 63.158 7.721 41.341 1.00 70.10 C ANISOU 161 C GLY A 20 8925 7378 10331 -797 1514 -1663 C ATOM 162 O GLY A 20 62.355 8.637 41.585 1.00 68.24 O ANISOU 162 O GLY A 20 8609 7358 9960 -793 1397 -1621 O ATOM 163 N ASP A 21 62.765 6.494 41.030 1.00 68.71 N ANISOU 163 N ASP A 21 8821 7077 10209 -958 1661 -1761 N ATOM 164 CA ASP A 21 61.343 6.191 40.901 1.00 78.06 C ANISOU 164 CA ASP A 21 9979 8397 11283 -1157 1676 -1829 C ATOM 165 C ASP A 21 60.555 6.279 42.212 1.00 70.97 C ANISOU 165 C ASP A 21 9055 7551 10361 -1120 1620 -1693 C ATOM 166 O ASP A 21 59.391 6.696 42.206 1.00 63.99 O ANISOU 166 O ASP A 21 8090 6883 9341 -1214 1557 -1698 O ATOM 167 CB ASP A 21 61.135 4.846 40.199 1.00 89.72 C ANISOU 167 CB ASP A 21 11556 9721 12812 -1363 1854 -1978 C ATOM 168 CG ASP A 21 61.573 4.883 38.743 1.00 98.15 C ANISOU 168 CG ASP A 21 12629 10830 13833 -1434 1889 -2114 C ATOM 169 OD1 ASP A 21 62.790 4.766 38.489 1.00 95.85 O ANISOU 169 OD1 ASP A 21 12372 10423 13623 -1288 1918 -2066 O ATOM 170 OD2 ASP A 21 60.705 5.046 37.856 1.00104.62 O ANISOU 170 OD2 ASP A 21 13399 11843 14510 -1618 1870 -2226 O ATOM 171 N LYS A 22 61.186 5.920 43.332 1.00 69.14 N ANISOU 171 N LYS A 22 8883 7132 10253 -980 1640 -1562 N ATOM 172 CA LYS A 22 60.513 6.023 44.635 1.00 65.35 C ANISOU 172 CA LYS A 22 8388 6692 9749 -935 1588 -1426 C ATOM 173 C LYS A 22 60.026 7.444 44.934 1.00 61.00 C ANISOU 173 C LYS A 22 7732 6393 9051 -847 1426 -1350 C ATOM 174 O LYS A 22 59.151 7.650 45.779 1.00 65.33 O ANISOU 174 O LYS A 22 8251 7037 9535 -849 1385 -1267 O ATOM 175 CB LYS A 22 61.381 5.459 45.781 1.00 69.60 C ANISOU 175 CB LYS A 22 9009 6995 10442 -789 1628 -1286 C ATOM 176 CG LYS A 22 62.662 6.236 46.114 1.00 73.07 C ANISOU 176 CG LYS A 22 9435 7396 10930 -574 1538 -1176 C ATOM 177 CD LYS A 22 63.595 5.420 47.030 1.00 61.97 C ANISOU 177 CD LYS A 22 8109 5743 9693 -458 1607 -1050 C ATOM 178 CE LYS A 22 64.727 6.265 47.608 1.00 56.07 C ANISOU 178 CE LYS A 22 7334 4999 8970 -256 1492 -906 C ATOM 179 NZ LYS A 22 65.489 7.059 46.593 1.00 55.85 N ANISOU 179 NZ LYS A 22 7259 5050 8913 -208 1438 -973 N ATOM 180 N GLY A 23 60.591 8.427 44.238 1.00 58.86 N ANISOU 180 N GLY A 23 7414 6224 8727 -769 1343 -1376 N ATOM 181 CA GLY A 23 60.117 9.797 44.348 1.00 62.57 C ANISOU 181 CA GLY A 23 7796 6928 9049 -693 1207 -1320 C ATOM 182 C GLY A 23 60.492 10.576 45.600 1.00 65.44 C ANISOU 182 C GLY A 23 8175 7283 9407 -507 1112 -1152 C ATOM 183 O GLY A 23 59.901 11.618 45.867 1.00 70.09 O ANISOU 183 O GLY A 23 8710 8052 9868 -453 1022 -1096 O ATOM 184 N TYR A 24 61.455 10.087 46.376 1.00 61.36 N ANISOU 184 N TYR A 24 7734 6560 9020 -410 1137 -1066 N ATOM 185 CA TYR A 24 61.941 10.844 47.526 1.00 62.95 C ANISOU 185 CA TYR A 24 7958 6753 9207 -247 1041 -908 C ATOM 186 C TYR A 24 63.432 10.608 47.752 1.00 58.17 C ANISOU 186 C TYR A 24 7403 5966 8732 -134 1043 -844 C ATOM 187 O TYR A 24 64.043 9.763 47.108 1.00 51.02 O ANISOU 187 O TYR A 24 6520 4923 7944 -170 1136 -914 O ATOM 188 CB TYR A 24 61.160 10.493 48.796 1.00 62.73 C ANISOU 188 CB TYR A 24 7958 6706 9170 -252 1053 -803 C ATOM 189 CG TYR A 24 61.301 9.051 49.203 1.00 70.30 C ANISOU 189 CG TYR A 24 8982 7455 10275 -310 1172 -794 C ATOM 190 CD1 TYR A 24 62.371 8.625 49.982 1.00 71.17 C ANISOU 190 CD1 TYR A 24 9156 7377 10510 -201 1183 -682 C ATOM 191 CD2 TYR A 24 60.365 8.104 48.801 1.00 74.80 C ANISOU 191 CD2 TYR A 24 9550 8017 10856 -479 1277 -891 C ATOM 192 CE1 TYR A 24 62.506 7.298 50.341 1.00 70.71 C ANISOU 192 CE1 TYR A 24 9161 7118 10589 -242 1302 -663 C ATOM 193 CE2 TYR A 24 60.490 6.781 49.160 1.00 72.05 C ANISOU 193 CE2 TYR A 24 9277 7461 10639 -535 1398 -885 C ATOM 194 CZ TYR A 24 61.559 6.384 49.930 1.00 72.93 C ANISOU 194 CZ TYR A 24 9455 7377 10879 -408 1414 -769 C ATOM 195 OH TYR A 24 61.685 5.061 50.285 1.00 78.32 O ANISOU 195 OH TYR A 24 10218 7846 11697 -452 1545 -753 O ATOM 196 N LEU A 25 64.009 11.345 48.693 1.00 51.14 N ANISOU 196 N LEU A 25 6532 5079 7819 0 946 -705 N ATOM 197 CA LEU A 25 65.415 11.175 48.990 1.00 49.09 C ANISOU 197 CA LEU A 25 6302 4676 7672 106 934 -619 C ATOM 198 C LEU A 25 65.627 10.508 50.349 1.00 53.28 C ANISOU 198 C LEU A 25 6889 5070 8286 158 952 -468 C ATOM 199 O LEU A 25 64.978 10.853 51.338 1.00 58.05 O ANISOU 199 O LEU A 25 7514 5734 8809 170 902 -384 O ATOM 200 CB LEU A 25 66.136 12.526 48.941 1.00 47.35 C ANISOU 200 CB LEU A 25 6063 4563 7363 207 803 -571 C ATOM 201 CG LEU A 25 66.155 13.339 47.633 1.00 49.96 C ANISOU 201 CG LEU A 25 6343 5028 7612 182 770 -697 C ATOM 202 CD1 LEU A 25 66.871 14.675 47.820 1.00 42.24 C ANISOU 202 CD1 LEU A 25 5367 4139 6543 284 642 -626 C ATOM 203 CD2 LEU A 25 66.809 12.585 46.499 1.00 48.74 C ANISOU 203 CD2 LEU A 25 6170 4776 7572 140 863 -807 C ATOM 204 N THR A 26 66.539 9.543 50.373 1.00 54.85 N ANISOU 204 N THR A 26 7111 5083 8644 192 1031 -430 N ATOM 205 CA THR A 26 67.091 8.991 51.603 1.00 51.16 C ANISOU 205 CA THR A 26 6686 4483 8268 272 1035 -260 C ATOM 206 C THR A 26 68.301 9.832 51.930 1.00 54.43 C ANISOU 206 C THR A 26 7080 4930 8669 394 918 -142 C ATOM 207 O THR A 26 68.742 10.623 51.095 1.00 58.29 O ANISOU 207 O THR A 26 7530 5510 9108 411 863 -209 O ATOM 208 CB THR A 26 67.606 7.565 51.383 1.00 50.06 C ANISOU 208 CB THR A 26 6578 4125 8316 267 1188 -264 C ATOM 209 OG1 THR A 26 68.700 7.611 50.463 1.00 57.75 O ANISOU 209 OG1 THR A 26 7521 5056 9366 321 1210 -303 O ATOM 210 CG2 THR A 26 66.524 6.686 50.791 1.00 50.19 C ANISOU 210 CG2 THR A 26 6624 4099 8348 118 1320 -412 C ATOM 211 N LYS A 27 68.857 9.664 53.125 1.00 52.29 N ANISOU 211 N LYS A 27 6835 4594 8439 472 877 36 N ATOM 212 CA LYS A 27 70.037 10.424 53.490 1.00 56.16 C ANISOU 212 CA LYS A 27 7304 5126 8910 570 760 161 C ATOM 213 C LYS A 27 71.173 10.076 52.527 1.00 60.50 C ANISOU 213 C LYS A 27 7802 5600 9586 618 813 132 C ATOM 214 O LYS A 27 72.053 10.895 52.257 1.00 55.83 O ANISOU 214 O LYS A 27 7170 5085 8957 670 722 164 O ATOM 215 CB LYS A 27 70.427 10.163 54.945 1.00 58.86 C ANISOU 215 CB LYS A 27 7679 5411 9276 629 714 366 C ATOM 216 CG LYS A 27 71.851 10.565 55.293 1.00 58.37 C ANISOU 216 CG LYS A 27 7581 5359 9239 722 620 518 C ATOM 217 CD LYS A 27 72.060 10.737 56.795 1.00 69.19 C ANISOU 217 CD LYS A 27 8990 6745 10555 754 527 715 C ATOM 218 CE LYS A 27 72.111 9.417 57.550 1.00 73.96 C ANISOU 218 CE LYS A 27 9610 7190 11302 784 621 835 C ATOM 219 NZ LYS A 27 72.525 9.642 58.968 1.00 76.35 N ANISOU 219 NZ LYS A 27 9938 7523 11549 818 515 1044 N ATOM 220 N GLU A 28 71.125 8.864 51.980 1.00 60.58 N ANISOU 220 N GLU A 28 7820 5458 9740 594 970 66 N ATOM 221 CA GLU A 28 72.123 8.433 51.006 1.00 57.28 C ANISOU 221 CA GLU A 28 7364 4950 9449 640 1053 26 C ATOM 222 C GLU A 28 71.990 9.232 49.721 1.00 49.91 C ANISOU 222 C GLU A 28 6397 4139 8427 586 1025 -147 C ATOM 223 O GLU A 28 72.983 9.722 49.181 1.00 46.67 O ANISOU 223 O GLU A 28 5937 3762 8032 647 985 -135 O ATOM 224 CB GLU A 28 71.983 6.943 50.708 1.00 65.43 C ANISOU 224 CB GLU A 28 8433 5840 10588 598 1222 -19 C ATOM 225 CG GLU A 28 71.442 6.121 51.869 1.00 84.66 C ANISOU 225 CG GLU A 28 10922 8188 13055 588 1262 85 C ATOM 226 CD GLU A 28 72.286 6.239 53.132 1.00 99.03 C ANISOU 226 CD GLU A 28 12721 10023 14883 698 1163 316 C ATOM 227 OE1 GLU A 28 73.494 6.549 53.029 1.00 99.27 O ANISOU 227 OE1 GLU A 28 12690 10098 14931 784 1103 404 O ATOM 228 OE2 GLU A 28 71.731 6.023 54.234 1.00108.05 O ANISOU 228 OE2 GLU A 28 13905 11140 16008 689 1144 410 O ATOM 229 N ASP A 29 70.757 9.367 49.240 1.00 44.94 N ANISOU 229 N ASP A 29 5789 3585 7701 471 1046 -300 N ATOM 230 CA ASP A 29 70.489 10.158 48.044 1.00 48.26 C ANISOU 230 CA ASP A 29 6175 4142 8020 412 1014 -459 C ATOM 231 C ASP A 29 70.908 11.606 48.228 1.00 50.66 C ANISOU 231 C ASP A 29 6446 4609 8194 473 847 -399 C ATOM 232 O ASP A 29 71.478 12.229 47.327 1.00 55.75 O ANISOU 232 O ASP A 29 7052 5320 8812 487 814 -463 O ATOM 233 CB ASP A 29 69.007 10.115 47.715 1.00 49.99 C ANISOU 233 CB ASP A 29 6410 4444 8140 279 1045 -593 C ATOM 234 CG ASP A 29 68.500 8.723 47.584 1.00 53.66 C ANISOU 234 CG ASP A 29 6921 4755 8712 193 1206 -657 C ATOM 235 OD1 ASP A 29 69.236 7.897 47.005 1.00 53.22 O ANISOU 235 OD1 ASP A 29 6883 4547 8792 207 1324 -691 O ATOM 236 OD2 ASP A 29 67.380 8.457 48.065 1.00 54.96 O ANISOU 236 OD2 ASP A 29 7109 4949 8824 112 1222 -669 O ATOM 237 N LEU A 30 70.601 12.137 49.404 1.00 43.19 N ANISOU 237 N LEU A 30 5526 3722 7162 500 749 -280 N ATOM 238 CA LEU A 30 70.854 13.531 49.699 1.00 41.43 C ANISOU 238 CA LEU A 30 5301 3646 6795 541 599 -225 C ATOM 239 C LEU A 30 72.348 13.761 49.683 1.00 48.88 C ANISOU 239 C LEU A 30 6209 4561 7802 626 547 -126 C ATOM 240 O LEU A 30 72.836 14.756 49.136 1.00 51.89 O ANISOU 240 O LEU A 30 6567 5044 8103 641 467 -155 O ATOM 241 CB LEU A 30 70.297 13.868 51.071 1.00 36.06 C ANISOU 241 CB LEU A 30 4675 3001 6025 552 528 -105 C ATOM 242 CG LEU A 30 70.625 15.241 51.636 1.00 45.81 C ANISOU 242 CG LEU A 30 5939 4357 7109 593 383 -23 C ATOM 243 CD1 LEU A 30 69.888 16.316 50.844 1.00 50.12 C ANISOU 243 CD1 LEU A 30 6483 5053 7506 558 347 -150 C ATOM 244 CD2 LEU A 30 70.246 15.271 53.105 1.00 50.43 C ANISOU 244 CD2 LEU A 30 6591 4933 7638 604 339 113 C ATOM 245 N ARG A 31 73.068 12.819 50.281 1.00 50.02 N ANISOU 245 N ARG A 31 6346 4568 8089 681 597 -2 N ATOM 246 CA ARG A 31 74.507 12.921 50.396 1.00 53.48 C ANISOU 246 CA ARG A 31 6736 4985 8600 767 551 125 C ATOM 247 C ARG A 31 75.130 12.862 49.017 1.00 49.89 C ANISOU 247 C ARG A 31 6226 4517 8213 776 615 11 C ATOM 248 O ARG A 31 75.967 13.700 48.681 1.00 43.79 O ANISOU 248 O ARG A 31 5411 3832 7394 808 529 36 O ATOM 249 CB ARG A 31 75.076 11.825 51.297 1.00 56.49 C ANISOU 249 CB ARG A 31 7111 5222 9130 833 608 293 C ATOM 250 CG ARG A 31 76.592 11.931 51.455 1.00 62.35 C ANISOU 250 CG ARG A 31 7781 5964 9945 927 556 451 C ATOM 251 CD ARG A 31 77.141 10.981 52.514 1.00 60.86 C ANISOU 251 CD ARG A 31 7581 5682 9862 992 584 648 C ATOM 252 NE ARG A 31 76.704 9.615 52.289 1.00 60.03 N ANISOU 252 NE ARG A 31 7505 5452 9852 973 747 584 N ATOM 253 CZ ARG A 31 75.940 8.922 53.129 1.00 71.45 C ANISOU 253 CZ ARG A 31 9011 6829 11308 947 790 623 C ATOM 254 NH1 ARG A 31 75.527 9.471 54.274 1.00 71.46 N ANISOU 254 NH1 ARG A 31 9049 6876 11226 939 682 729 N ATOM 255 NH2 ARG A 31 75.598 7.669 52.823 1.00 72.27 N ANISOU 255 NH2 ARG A 31 9144 6815 11500 922 944 559 N ATOM 256 N VAL A 32 74.709 11.887 48.213 1.00 46.98 N ANISOU 256 N VAL A 32 5865 4040 7944 737 769 -118 N ATOM 257 CA VAL A 32 75.183 11.806 46.832 1.00 47.93 C ANISOU 257 CA VAL A 32 5949 4146 8117 730 844 -248 C ATOM 258 C VAL A 32 74.860 13.101 46.078 1.00 47.23 C ANISOU 258 C VAL A 32 5847 4237 7862 678 742 -364 C ATOM 259 O VAL A 32 75.744 13.697 45.457 1.00 50.67 O ANISOU 259 O VAL A 32 6236 4727 8290 714 700 -369 O ATOM 260 CB VAL A 32 74.627 10.563 46.079 1.00 58.84 C ANISOU 260 CB VAL A 32 7367 5409 9579 656 1022 -383 C ATOM 261 CG1 VAL A 32 74.893 10.669 44.590 1.00 58.90 C ANISOU 261 CG1 VAL A 32 7352 5464 9564 609 1073 -537 C ATOM 262 CG2 VAL A 32 75.270 9.306 46.612 1.00 59.74 C ANISOU 262 CG2 VAL A 32 7491 5399 9811 708 1111 -253 C ATOM 263 N LEU A 33 73.612 13.558 46.183 1.00 43.65 N ANISOU 263 N LEU A 33 5431 3880 7275 600 703 -443 N ATOM 264 CA LEU A 33 73.173 14.776 45.499 1.00 40.80 C ANISOU 264 CA LEU A 33 5061 3689 6751 557 616 -545 C ATOM 265 C LEU A 33 74.046 15.996 45.817 1.00 46.00 C ANISOU 265 C LEU A 33 5707 4448 7324 621 472 -444 C ATOM 266 O LEU A 33 74.345 16.790 44.931 1.00 50.63 O ANISOU 266 O LEU A 33 6268 5126 7844 614 432 -519 O ATOM 267 CB LEU A 33 71.696 15.081 45.792 1.00 36.43 C ANISOU 267 CB LEU A 33 4544 3229 6071 486 595 -600 C ATOM 268 CG LEU A 33 71.029 16.331 45.180 1.00 38.31 C ANISOU 268 CG LEU A 33 4774 3649 6132 450 516 -690 C ATOM 269 CD1 LEU A 33 69.506 16.168 45.188 1.00 42.18 C ANISOU 269 CD1 LEU A 33 5275 4207 6546 368 553 -765 C ATOM 270 CD2 LEU A 33 71.363 17.609 45.920 1.00 34.33 C ANISOU 270 CD2 LEU A 33 4301 3239 5505 514 377 -580 C ATOM 271 N MET A 34 74.441 16.166 47.070 1.00 39.80 N ANISOU 271 N MET A 34 4944 3650 6529 672 394 -276 N ATOM 272 CA MET A 34 75.224 17.346 47.408 1.00 45.80 C ANISOU 272 CA MET A 34 5705 4509 7187 707 255 -184 C ATOM 273 C MET A 34 76.692 17.160 47.055 1.00 51.10 C ANISOU 273 C MET A 34 6305 5142 7967 764 255 -114 C ATOM 274 O MET A 34 77.388 18.121 46.703 1.00 49.33 O ANISOU 274 O MET A 34 6063 5012 7670 771 168 -104 O ATOM 275 CB MET A 34 75.043 17.675 48.868 1.00 43.11 C ANISOU 275 CB MET A 34 5425 4187 6769 718 167 -38 C ATOM 276 CG MET A 34 73.570 17.845 49.197 1.00 38.64 C ANISOU 276 CG MET A 34 4923 3661 6099 670 181 -104 C ATOM 277 SD MET A 34 73.471 18.506 50.829 1.00 53.24 S ANISOU 277 SD MET A 34 6860 5546 7824 683 69 61 S ATOM 278 CE MET A 34 74.569 19.932 50.580 1.00 35.12 C ANISOU 278 CE MET A 34 4575 3360 5409 694 -63 98 C ATOM 279 N GLU A 35 77.146 15.916 47.121 1.00 43.41 N ANISOU 279 N GLU A 35 5294 4029 7171 806 362 -63 N ATOM 280 CA GLU A 35 78.471 15.585 46.627 1.00 55.78 C ANISOU 280 CA GLU A 35 6781 5550 8864 872 397 -6 C ATOM 281 C GLU A 35 78.620 15.991 45.163 1.00 53.46 C ANISOU 281 C GLU A 35 6458 5306 8550 845 433 -170 C ATOM 282 O GLU A 35 79.578 16.670 44.813 1.00 58.10 O ANISOU 282 O GLU A 35 6995 5965 9114 873 367 -131 O ATOM 283 CB GLU A 35 78.786 14.101 46.845 1.00 62.41 C ANISOU 283 CB GLU A 35 7597 6213 9903 930 540 61 C ATOM 284 CG GLU A 35 79.079 13.799 48.311 1.00 72.69 C ANISOU 284 CG GLU A 35 8901 7483 11233 979 482 274 C ATOM 285 CD GLU A 35 79.473 12.357 48.585 1.00 77.98 C ANISOU 285 CD GLU A 35 9551 8000 12075 1040 617 364 C ATOM 286 OE1 GLU A 35 79.018 11.448 47.854 1.00 81.35 O ANISOU 286 OE1 GLU A 35 10010 8344 12556 1003 762 232 O ATOM 287 OE2 GLU A 35 80.244 12.140 49.547 1.00 78.96 O ANISOU 287 OE2 GLU A 35 9639 8135 12229 1097 564 564 O ATOM 288 N LYS A 36 77.658 15.619 44.322 1.00 46.58 N ANISOU 288 N LYS A 36 5617 4408 7675 781 531 -349 N ATOM 289 CA LYS A 36 77.719 15.988 42.910 1.00 46.92 C ANISOU 289 CA LYS A 36 5636 4504 7686 743 567 -510 C ATOM 290 C LYS A 36 77.336 17.455 42.641 1.00 55.74 C ANISOU 290 C LYS A 36 6772 5799 8609 701 434 -565 C ATOM 291 O LYS A 36 77.874 18.081 41.729 1.00 61.79 O ANISOU 291 O LYS A 36 7506 6635 9339 699 412 -626 O ATOM 292 CB LYS A 36 76.844 15.062 42.058 1.00 44.30 C ANISOU 292 CB LYS A 36 5333 4093 7407 670 718 -682 C ATOM 293 CG LYS A 36 77.002 13.571 42.343 1.00 52.30 C ANISOU 293 CG LYS A 36 6362 4934 8576 689 860 -636 C ATOM 294 CD LYS A 36 78.143 12.958 41.552 1.00 63.98 C ANISOU 294 CD LYS A 36 7807 6368 10135 722 946 -620 C ATOM 295 CE LYS A 36 77.870 11.479 41.232 1.00 69.88 C ANISOU 295 CE LYS A 36 8603 6988 10960 674 1111 -666 C ATOM 296 NZ LYS A 36 78.802 10.940 40.190 1.00 71.27 N ANISOU 296 NZ LYS A 36 8762 7127 11192 687 1212 -693 N ATOM 297 N GLU A 37 76.414 18.010 43.422 1.00 45.58 N ANISOU 297 N GLU A 37 5541 4582 7197 672 355 -541 N ATOM 298 CA GLU A 37 75.896 19.325 43.087 1.00 40.23 C ANISOU 298 CA GLU A 37 4892 4055 6337 638 260 -605 C ATOM 299 C GLU A 37 76.542 20.467 43.874 1.00 45.01 C ANISOU 299 C GLU A 37 5526 4738 6835 671 117 -475 C ATOM 300 O GLU A 37 76.629 21.596 43.386 1.00 47.15 O ANISOU 300 O GLU A 37 5814 5118 6982 659 46 -516 O ATOM 301 CB GLU A 37 74.371 19.352 43.204 1.00 39.39 C ANISOU 301 CB GLU A 37 4830 3997 6140 581 279 -684 C ATOM 302 CG GLU A 37 73.655 18.446 42.195 1.00 36.43 C ANISOU 302 CG GLU A 37 4429 3587 5827 512 408 -841 C ATOM 303 CD GLU A 37 73.765 18.947 40.755 1.00 42.61 C ANISOU 303 CD GLU A 37 5176 4455 6558 474 419 -979 C ATOM 304 OE1 GLU A 37 74.115 20.134 40.530 1.00 47.23 O ANISOU 304 OE1 GLU A 37 5763 5148 7034 499 323 -965 O ATOM 305 OE2 GLU A 37 73.480 18.154 39.838 1.00 42.48 O ANISOU 305 OE2 GLU A 37 5140 4399 6603 411 528 -1104 O ATOM 306 N PHE A 38 77.003 20.194 45.083 1.00 43.22 N ANISOU 306 N PHE A 38 5314 4460 6649 706 75 -316 N ATOM 307 CA PHE A 38 77.677 21.250 45.825 1.00 42.04 C ANISOU 307 CA PHE A 38 5199 4385 6389 716 -61 -193 C ATOM 308 C PHE A 38 78.939 20.749 46.527 1.00 49.25 C ANISOU 308 C PHE A 38 6058 5245 7410 760 -90 -20 C ATOM 309 O PHE A 38 79.060 20.863 47.746 1.00 55.44 O ANISOU 309 O PHE A 38 6882 6031 8153 761 -163 120 O ATOM 310 CB PHE A 38 76.751 21.854 46.871 1.00 34.72 C ANISOU 310 CB PHE A 38 4374 3500 5318 694 -124 -150 C ATOM 311 CG PHE A 38 75.328 22.010 46.423 1.00 43.24 C ANISOU 311 CG PHE A 38 5490 4618 6322 665 -71 -286 C ATOM 312 CD1 PHE A 38 74.972 23.003 45.523 1.00 45.88 C ANISOU 312 CD1 PHE A 38 5840 5055 6537 647 -92 -394 C ATOM 313 CD2 PHE A 38 74.333 21.192 46.939 1.00 46.12 C ANISOU 313 CD2 PHE A 38 5870 4926 6728 654 -3 -293 C ATOM 314 CE1 PHE A 38 73.655 23.161 45.127 1.00 41.25 C ANISOU 314 CE1 PHE A 38 5272 4525 5877 624 -47 -498 C ATOM 315 CE2 PHE A 38 73.016 21.347 46.555 1.00 46.41 C ANISOU 315 CE2 PHE A 38 5925 5019 6688 623 40 -402 C ATOM 316 CZ PHE A 38 72.676 22.326 45.645 1.00 49.18 C ANISOU 316 CZ PHE A 38 6280 5484 6924 610 17 -501 C ATOM 317 N PRO A 39 79.894 20.219 45.761 1.00 56.94 N ANISOU 317 N PRO A 39 6938 6179 8518 797 -33 -22 N ATOM 318 CA PRO A 39 81.062 19.584 46.387 1.00 64.10 C ANISOU 318 CA PRO A 39 7771 7034 9550 854 -40 157 C ATOM 319 C PRO A 39 81.913 20.597 47.139 1.00 65.05 C ANISOU 319 C PRO A 39 7897 7264 9555 835 -198 306 C ATOM 320 O PRO A 39 82.400 20.310 48.226 1.00 69.15 O ANISOU 320 O PRO A 39 8401 7773 10100 852 -250 481 O ATOM 321 CB PRO A 39 81.832 19.027 45.197 1.00 67.57 C ANISOU 321 CB PRO A 39 8115 7427 10132 898 63 98 C ATOM 322 CG PRO A 39 81.433 19.916 44.049 1.00 66.66 C ANISOU 322 CG PRO A 39 8027 7397 9904 845 52 -80 C ATOM 323 CD PRO A 39 80.014 20.307 44.295 1.00 61.50 C ANISOU 323 CD PRO A 39 7471 6774 9121 788 34 -175 C ATOM 324 N GLY A 40 82.065 21.787 46.576 1.00 61.64 N ANISOU 324 N GLY A 40 7494 6940 8987 789 -274 237 N ATOM 325 CA GLY A 40 82.825 22.829 47.240 1.00 64.49 C ANISOU 325 CA GLY A 40 7880 7406 9216 746 -421 361 C ATOM 326 C GLY A 40 82.208 23.248 48.562 1.00 64.35 C ANISOU 326 C GLY A 40 7980 7405 9065 702 -503 440 C ATOM 327 O GLY A 40 82.881 23.818 49.427 1.00 59.72 O ANISOU 327 O GLY A 40 7419 6885 8386 658 -620 582 O ATOM 328 N PHE A 41 80.916 22.979 48.721 1.00 57.08 N ANISOU 328 N PHE A 41 7132 6431 8123 704 -441 348 N ATOM 329 CA PHE A 41 80.238 23.338 49.953 1.00 51.10 C ANISOU 329 CA PHE A 41 6492 5682 7242 668 -499 413 C ATOM 330 C PHE A 41 80.544 22.310 51.065 1.00 50.48 C ANISOU 330 C PHE A 41 6377 5535 7270 696 -496 579 C ATOM 331 O PHE A 41 80.833 22.675 52.200 1.00 47.81 O ANISOU 331 O PHE A 41 6095 5234 6838 657 -593 717 O ATOM 332 CB PHE A 41 78.732 23.462 49.725 1.00 45.51 C ANISOU 332 CB PHE A 41 5866 4957 6469 664 -432 267 C ATOM 333 CG PHE A 41 77.963 23.754 50.977 1.00 39.32 C ANISOU 333 CG PHE A 41 5202 4172 5567 638 -470 331 C ATOM 334 CD1 PHE A 41 77.931 25.038 51.502 1.00 42.77 C ANISOU 334 CD1 PHE A 41 5764 4681 5805 589 -562 358 C ATOM 335 CD2 PHE A 41 77.295 22.742 51.647 1.00 37.63 C ANISOU 335 CD2 PHE A 41 4986 3876 5436 660 -406 365 C ATOM 336 CE1 PHE A 41 77.230 25.307 52.686 1.00 48.93 C ANISOU 336 CE1 PHE A 41 6669 5453 6471 566 -586 418 C ATOM 337 CE2 PHE A 41 76.599 23.000 52.815 1.00 44.34 C ANISOU 337 CE2 PHE A 41 5947 4725 6176 637 -436 427 C ATOM 338 CZ PHE A 41 76.560 24.280 53.337 1.00 45.28 C ANISOU 338 CZ PHE A 41 6192 4916 6096 592 -524 453 C ATOM 339 N LEU A 42 80.469 21.029 50.725 1.00 45.84 N ANISOU 339 N LEU A 42 5702 4844 6870 757 -379 563 N ATOM 340 CA LEU A 42 80.825 19.959 51.644 1.00 62.32 C ANISOU 340 CA LEU A 42 7742 6855 9082 800 -357 724 C ATOM 341 C LEU A 42 82.309 20.008 52.003 1.00 68.47 C ANISOU 341 C LEU A 42 8428 7689 9898 815 -442 912 C ATOM 342 O LEU A 42 82.678 19.895 53.174 1.00 72.88 O ANISOU 342 O LEU A 42 8994 8268 10431 803 -517 1089 O ATOM 343 CB LEU A 42 80.502 18.614 51.004 1.00 65.83 C ANISOU 343 CB LEU A 42 8123 7166 9725 863 -194 651 C ATOM 344 CG LEU A 42 79.024 18.411 50.696 1.00 62.11 C ANISOU 344 CG LEU A 42 7726 6648 9224 834 -108 481 C ATOM 345 CD1 LEU A 42 78.801 17.073 50.024 1.00 69.04 C ANISOU 345 CD1 LEU A 42 8551 7391 10290 874 56 406 C ATOM 346 CD2 LEU A 42 78.212 18.512 51.978 1.00 56.59 C ANISOU 346 CD2 LEU A 42 7124 5949 8428 803 -154 551 C ATOM 347 N GLU A 43 83.150 20.205 50.990 1.00 70.76 N ANISOU 347 N GLU A 43 8629 8016 10240 836 -432 877 N ATOM 348 CA GLU A 43 84.596 20.257 51.177 1.00 74.18 C ANISOU 348 CA GLU A 43 8949 8519 10716 853 -505 1055 C ATOM 349 C GLU A 43 85.030 21.396 52.101 1.00 73.65 C ANISOU 349 C GLU A 43 8944 8588 10450 755 -681 1173 C ATOM 350 O GLU A 43 86.207 21.500 52.437 1.00 83.58 O ANISOU 350 O GLU A 43 10111 9929 11716 745 -765 1344 O ATOM 351 CB GLU A 43 85.321 20.385 49.827 1.00 80.02 C ANISOU 351 CB GLU A 43 9592 9283 11529 885 -456 973 C ATOM 352 CG GLU A 43 85.149 19.203 48.867 1.00 90.43 C ANISOU 352 CG GLU A 43 10843 10466 13051 976 -273 874 C ATOM 353 CD GLU A 43 86.056 19.301 47.640 1.00 95.33 C ANISOU 353 CD GLU A 43 11360 11115 13747 1012 -227 826 C ATOM 354 OE1 GLU A 43 85.627 18.891 46.534 1.00 92.46 O ANISOU 354 OE1 GLU A 43 10999 10673 13459 1036 -96 653 O ATOM 355 OE2 GLU A 43 87.204 19.780 47.788 1.00 96.52 O ANISOU 355 OE2 GLU A 43 11427 11370 13875 1008 -320 966 O ATOM 356 N ASN A 44 84.097 22.257 52.500 1.00 63.69 N ANISOU 356 N ASN A 44 7841 7353 9008 678 -733 1086 N ATOM 357 CA ASN A 44 84.423 23.363 53.402 1.00 59.64 C ANISOU 357 CA ASN A 44 7422 6950 8288 571 -886 1182 C ATOM 358 C ASN A 44 83.803 23.227 54.793 1.00 63.74 C ANISOU 358 C ASN A 44 8048 7446 8725 535 -924 1274 C ATOM 359 O ASN A 44 84.148 23.993 55.705 1.00 65.13 O ANISOU 359 O ASN A 44 8306 7706 8734 438 -1048 1379 O ATOM 360 CB ASN A 44 84.049 24.712 52.783 1.00 60.45 C ANISOU 360 CB ASN A 44 7642 7114 8214 502 -924 1028 C ATOM 361 CG ASN A 44 84.586 25.901 53.581 1.00 65.73 C ANISOU 361 CG ASN A 44 8414 7893 8668 378 -1074 1124 C ATOM 362 OD1 ASN A 44 83.822 26.686 54.153 1.00 64.22 O ANISOU 362 OD1 ASN A 44 8397 7705 8301 315 -1105 1077 O ATOM 363 ND2 ASN A 44 85.906 26.039 53.613 1.00 66.52 N ANISOU 363 ND2 ASN A 44 8410 8086 8777 339 -1161 1261 N ATOM 364 N GLN A 45 82.891 22.264 54.963 1.00 60.89 N ANISOU 364 N GLN A 45 7694 6970 8471 601 -817 1232 N ATOM 365 CA GLN A 45 82.397 21.935 56.303 1.00 59.69 C ANISOU 365 CA GLN A 45 7621 6788 8271 579 -842 1340 C ATOM 366 C GLN A 45 83.453 21.103 57.031 1.00 67.88 C ANISOU 366 C GLN A 45 8536 7837 9419 608 -883 1572 C ATOM 367 O GLN A 45 83.834 20.027 56.560 1.00 71.75 O ANISOU 367 O GLN A 45 8891 8256 10116 707 -790 1607 O ATOM 368 CB GLN A 45 81.069 21.170 56.260 1.00 44.09 C ANISOU 368 CB GLN A 45 5689 4692 6371 632 -713 1226 C ATOM 369 CG GLN A 45 80.032 21.760 55.315 1.00 48.67 C ANISOU 369 CG GLN A 45 6341 5264 6886 627 -649 1002 C ATOM 370 CD GLN A 45 79.863 23.264 55.471 1.00 48.24 C ANISOU 370 CD GLN A 45 6423 5304 6600 546 -742 956 C ATOM 371 OE1 GLN A 45 79.487 23.758 56.542 1.00 48.09 O ANISOU 371 OE1 GLN A 45 6533 5305 6434 490 -799 1017 O ATOM 372 NE2 GLN A 45 80.144 24.003 54.397 1.00 46.59 N ANISOU 372 NE2 GLN A 45 6199 5149 6355 537 -750 848 N ATOM 373 N LYS A 46 83.934 21.605 58.167 1.00 71.30 N ANISOU 373 N LYS A 46 9019 8361 9711 520 -1016 1734 N ATOM 374 CA LYS A 46 84.922 20.867 58.955 1.00 79.21 C ANISOU 374 CA LYS A 46 9904 9406 10788 536 -1056 1955 C ATOM 375 C LYS A 46 84.231 19.635 59.523 1.00 81.01 C ANISOU 375 C LYS A 46 10129 9511 11139 613 -949 1982 C ATOM 376 O LYS A 46 84.829 18.566 59.631 1.00 83.89 O ANISOU 376 O LYS A 46 10369 9852 11655 687 -883 2075 O ATOM 377 CB LYS A 46 85.501 21.727 60.089 1.00 77.92 C ANISOU 377 CB LYS A 46 9815 9394 10395 389 -1188 2044 C ATOM 378 CG LYS A 46 86.079 23.069 59.650 1.00 76.10 C ANISOU 378 CG LYS A 46 9628 9284 10004 282 -1288 1995 C ATOM 379 CD LYS A 46 86.470 23.932 60.848 1.00 83.96 C ANISOU 379 CD LYS A 46 10729 10405 10768 122 -1387 2046 C ATOM 380 CE LYS A 46 87.701 23.385 61.562 1.00 92.29 C ANISOU 380 CE LYS A 46 11635 11565 11867 96 -1431 2223 C ATOM 381 NZ LYS A 46 88.115 24.218 62.730 1.00 92.84 N ANISOU 381 NZ LYS A 46 11798 11754 11723 -72 -1525 2266 N ATOM 382 N ASP A 47 82.956 19.806 59.864 1.00 77.61 N ANISOU 382 N ASP A 47 9845 9004 10640 593 -925 1896 N ATOM 383 CA ASP A 47 82.097 18.731 60.356 1.00 73.63 C ANISOU 383 CA ASP A 47 9362 8376 10237 653 -818 1896 C ATOM 384 C ASP A 47 81.984 17.579 59.338 1.00 75.38 C ANISOU 384 C ASP A 47 9470 8465 10708 777 -661 1826 C ATOM 385 O ASP A 47 81.726 17.806 58.158 1.00 82.24 O ANISOU 385 O ASP A 47 10326 9314 11608 795 -594 1645 O ATOM 386 CB ASP A 47 80.712 19.314 60.677 1.00 65.99 C ANISOU 386 CB ASP A 47 8572 7377 9123 598 -802 1759 C ATOM 387 CG ASP A 47 79.896 18.436 61.611 1.00 71.63 C ANISOU 387 CG ASP A 47 9336 7999 9881 621 -740 1815 C ATOM 388 OD1 ASP A 47 79.796 17.211 61.371 1.00 70.76 O ANISOU 388 OD1 ASP A 47 9137 7779 9969 709 -628 1831 O ATOM 389 OD2 ASP A 47 79.341 18.984 62.587 1.00 74.00 O ANISOU 389 OD2 ASP A 47 9774 8331 10012 546 -796 1841 O ATOM 390 N PRO A 48 82.201 16.335 59.794 1.00 67.11 N ANISOU 390 N PRO A 48 8355 7358 9786 836 -577 1910 N ATOM 391 CA PRO A 48 82.020 15.154 58.936 1.00 64.10 C ANISOU 391 CA PRO A 48 7900 6837 9620 937 -406 1830 C ATOM 392 C PRO A 48 80.592 14.604 58.972 1.00 61.71 C ANISOU 392 C PRO A 48 7692 6397 9359 944 -295 1711 C ATOM 393 O PRO A 48 80.195 13.779 58.135 1.00 59.47 O ANISOU 393 O PRO A 48 7381 5994 9223 997 -148 1594 O ATOM 394 CB PRO A 48 83.012 14.130 59.518 1.00 58.46 C ANISOU 394 CB PRO A 48 7080 6136 8997 987 -376 1994 C ATOM 395 CG PRO A 48 83.437 14.680 60.872 1.00 62.92 C ANISOU 395 CG PRO A 48 7677 6837 9392 905 -528 2152 C ATOM 396 CD PRO A 48 82.754 15.995 61.116 1.00 61.91 C ANISOU 396 CD PRO A 48 7686 6770 9065 803 -639 2083 C ATOM 397 N LEU A 49 79.820 15.057 59.947 1.00 54.26 N ANISOU 397 N LEU A 49 6865 5476 8275 879 -362 1736 N ATOM 398 CA LEU A 49 78.444 14.619 60.054 1.00 50.46 C ANISOU 398 CA LEU A 49 6472 4887 7815 875 -263 1631 C ATOM 399 C LEU A 49 77.502 15.675 59.464 1.00 60.86 C ANISOU 399 C LEU A 49 7880 6267 8978 809 -276 1421 C ATOM 400 O LEU A 49 76.282 15.605 59.654 1.00 65.93 O ANISOU 400 O LEU A 49 8606 6874 9572 781 -219 1323 O ATOM 401 CB LEU A 49 78.104 14.353 61.512 1.00 42.41 C ANISOU 401 CB LEU A 49 5528 3878 6709 837 -303 1753 C ATOM 402 CG LEU A 49 78.980 13.307 62.200 1.00 45.99 C ANISOU 402 CG LEU A 49 5902 4331 7241 875 -286 1904 C ATOM 403 CD1 LEU A 49 78.391 12.973 63.554 1.00 50.43 C ANISOU 403 CD1 LEU A 49 6552 4885 7724 836 -302 1986 C ATOM 404 CD2 LEU A 49 79.086 12.056 61.343 1.00 45.38 C ANISOU 404 CD2 LEU A 49 5738 4128 7376 959 -125 1845 C ATOM 405 N ALA A 50 78.068 16.639 58.740 1.00 50.82 N ANISOU 405 N ALA A 50 6587 5092 7632 788 -345 1361 N ATOM 406 CA ALA A 50 77.280 17.756 58.218 1.00 52.22 C ANISOU 406 CA ALA A 50 6852 5338 7650 734 -365 1187 C ATOM 407 C ALA A 50 76.085 17.337 57.359 1.00 46.28 C ANISOU 407 C ALA A 50 6108 4521 6956 746 -233 992 C ATOM 408 O ALA A 50 75.001 17.940 57.463 1.00 41.79 O ANISOU 408 O ALA A 50 5631 3988 6257 707 -229 894 O ATOM 409 CB ALA A 50 78.163 18.742 57.459 1.00 55.24 C ANISOU 409 CB ALA A 50 7200 5821 7967 716 -446 1155 C ATOM 410 N VAL A 51 76.264 16.317 56.516 1.00 43.49 N ANISOU 410 N VAL A 51 5660 4075 6789 795 -120 939 N ATOM 411 CA VAL A 51 75.132 15.833 55.729 1.00 43.95 C ANISOU 411 CA VAL A 51 5727 4076 6898 784 5 760 C ATOM 412 C VAL A 51 74.070 15.283 56.657 1.00 46.90 C ANISOU 412 C VAL A 51 6169 4394 7257 762 51 786 C ATOM 413 O VAL A 51 72.891 15.558 56.474 1.00 44.18 O ANISOU 413 O VAL A 51 5875 4079 6831 721 87 665 O ATOM 414 CB VAL A 51 75.507 14.750 54.732 1.00 44.42 C ANISOU 414 CB VAL A 51 5696 4027 7155 827 132 699 C ATOM 415 CG1 VAL A 51 74.247 14.092 54.180 1.00 52.63 C ANISOU 415 CG1 VAL A 51 6760 5001 8236 788 262 537 C ATOM 416 CG2 VAL A 51 76.291 15.344 53.610 1.00 46.76 C ANISOU 416 CG2 VAL A 51 5930 4384 7452 839 107 627 C ATOM 417 N ASP A 52 74.510 14.520 57.656 1.00 52.60 N ANISOU 417 N ASP A 52 6886 5044 8056 791 50 956 N ATOM 418 CA ASP A 52 73.618 13.916 58.641 1.00 48.35 C ANISOU 418 CA ASP A 52 6412 4445 7514 772 93 1006 C ATOM 419 C ASP A 52 72.820 14.971 59.364 1.00 43.26 C ANISOU 419 C ASP A 52 5873 3901 6661 719 14 994 C ATOM 420 O ASP A 52 71.626 14.795 59.637 1.00 49.15 O ANISOU 420 O ASP A 52 6675 4633 7368 689 73 932 O ATOM 421 CB ASP A 52 74.423 13.064 59.631 1.00 48.62 C ANISOU 421 CB ASP A 52 6420 4402 7651 819 84 1218 C ATOM 422 CG ASP A 52 75.263 12.005 58.926 1.00 55.95 C ANISOU 422 CG ASP A 52 7247 5219 8794 892 182 1245 C ATOM 423 OD1 ASP A 52 76.447 12.292 58.664 1.00 68.88 O ANISOU 423 OD1 ASP A 52 8810 6901 10461 934 121 1326 O ATOM 424 OD2 ASP A 52 74.738 10.909 58.594 1.00 52.08 O ANISOU 424 OD2 ASP A 52 6753 4594 8438 904 327 1181 O ATOM 425 N LYS A 53 73.473 16.094 59.635 1.00 44.74 N ANISOU 425 N LYS A 53 6094 4192 6712 705 -113 1051 N ATOM 426 CA LYS A 53 72.838 17.190 60.354 1.00 48.08 C ANISOU 426 CA LYS A 53 6640 4703 6925 657 -184 1049 C ATOM 427 C LYS A 53 71.846 17.958 59.483 1.00 50.80 C ANISOU 427 C LYS A 53 7016 5109 7178 642 -144 863 C ATOM 428 O LYS A 53 70.858 18.515 59.986 1.00 52.31 O ANISOU 428 O LYS A 53 7302 5339 7234 619 -138 834 O ATOM 429 CB LYS A 53 73.900 18.124 60.931 1.00 49.96 C ANISOU 429 CB LYS A 53 6918 5024 7039 630 -326 1172 C ATOM 430 CG LYS A 53 74.827 17.418 61.893 1.00 57.07 C ANISOU 430 CG LYS A 53 7782 5891 8010 639 -377 1379 C ATOM 431 CD LYS A 53 75.812 18.389 62.509 1.00 65.37 C ANISOU 431 CD LYS A 53 8878 7047 8914 585 -527 1502 C ATOM 432 CE LYS A 53 76.655 17.707 63.576 1.00 70.55 C ANISOU 432 CE LYS A 53 9494 7693 9620 585 -587 1729 C ATOM 433 NZ LYS A 53 77.470 18.689 64.345 1.00 75.52 N ANISOU 433 NZ LYS A 53 10186 8444 10064 500 -738 1846 N ATOM 434 N ILE A 54 72.105 17.986 58.178 1.00 44.27 N ANISOU 434 N ILE A 54 6107 4294 6421 658 -113 745 N ATOM 435 CA ILE A 54 71.187 18.628 57.248 1.00 42.18 C ANISOU 435 CA ILE A 54 5851 4095 6081 646 -72 575 C ATOM 436 C ILE A 54 69.965 17.735 57.085 1.00 40.04 C ANISOU 436 C ILE A 54 5557 3776 5881 634 47 494 C ATOM 437 O ILE A 54 68.829 18.205 57.091 1.00 41.29 O ANISOU 437 O ILE A 54 5758 3995 5934 617 75 424 O ATOM 438 CB ILE A 54 71.863 18.888 55.894 1.00 48.82 C ANISOU 438 CB ILE A 54 6610 4967 6972 659 -76 477 C ATOM 439 CG1 ILE A 54 72.808 20.079 56.023 1.00 50.78 C ANISOU 439 CG1 ILE A 54 6902 5295 7098 653 -198 535 C ATOM 440 CG2 ILE A 54 70.837 19.143 54.815 1.00 46.11 C ANISOU 440 CG2 ILE A 54 6246 4677 6598 645 -7 302 C ATOM 441 CD1 ILE A 54 73.912 20.116 54.976 1.00 48.84 C ANISOU 441 CD1 ILE A 54 6561 5060 6935 670 -217 503 C ATOM 442 N MET A 55 70.211 16.438 56.968 1.00 41.82 N ANISOU 442 N MET A 55 5715 3890 6282 641 122 514 N ATOM 443 CA MET A 55 69.151 15.450 56.941 1.00 47.60 C ANISOU 443 CA MET A 55 6435 4560 7090 612 237 455 C ATOM 444 C MET A 55 68.221 15.587 58.153 1.00 59.79 C ANISOU 444 C MET A 55 8064 6122 8531 594 231 524 C ATOM 445 O MET A 55 66.999 15.495 58.026 1.00 64.25 O ANISOU 445 O MET A 55 8635 6720 9058 560 297 442 O ATOM 446 CB MET A 55 69.759 14.056 56.920 1.00 43.63 C ANISOU 446 CB MET A 55 5880 3911 6787 629 314 507 C ATOM 447 CG MET A 55 68.732 12.948 56.720 1.00 46.50 C ANISOU 447 CG MET A 55 6234 4193 7239 582 448 427 C ATOM 448 SD MET A 55 67.861 13.101 55.147 1.00 53.58 S ANISOU 448 SD MET A 55 7079 5163 8114 516 519 198 S ATOM 449 CE MET A 55 66.756 11.686 55.242 1.00 44.39 C ANISOU 449 CE MET A 55 5920 3896 7049 438 667 146 C ATOM 450 N LYS A 56 68.799 15.801 59.329 1.00 59.34 N ANISOU 450 N LYS A 56 8070 6052 8426 612 153 680 N ATOM 451 CA LYS A 56 67.992 15.904 60.540 1.00 55.74 C ANISOU 451 CA LYS A 56 7705 5604 7870 594 152 754 C ATOM 452 C LYS A 56 67.079 17.127 60.489 1.00 54.10 C ANISOU 452 C LYS A 56 7565 5514 7477 585 135 679 C ATOM 453 O LYS A 56 65.915 17.040 60.868 1.00 54.15 O ANISOU 453 O LYS A 56 7604 5539 7433 569 196 657 O ATOM 454 CB LYS A 56 68.877 15.949 61.787 1.00 48.61 C ANISOU 454 CB LYS A 56 6861 4674 6935 603 64 940 C ATOM 455 CG LYS A 56 68.120 16.204 63.081 1.00 43.64 C ANISOU 455 CG LYS A 56 6344 4059 6177 580 54 1019 C ATOM 456 CD LYS A 56 69.060 16.731 64.176 1.00 57.24 C ANISOU 456 CD LYS A 56 8145 5804 7800 569 -65 1182 C ATOM 457 CE LYS A 56 68.479 16.585 65.586 1.00 62.01 C ANISOU 457 CE LYS A 56 8854 6389 8318 543 -62 1291 C ATOM 458 NZ LYS A 56 67.370 17.543 65.860 1.00 62.61 N ANISOU 458 NZ LYS A 56 9041 6533 8216 527 -38 1219 N ATOM 459 N ASP A 57 67.616 18.252 60.015 1.00 50.76 N ANISOU 459 N ASP A 57 7163 5169 6956 598 60 646 N ATOM 460 CA ASP A 57 66.837 19.480 59.802 1.00 50.86 C ANISOU 460 CA ASP A 57 7240 5287 6798 605 55 572 C ATOM 461 C ASP A 57 65.744 19.324 58.745 1.00 50.95 C ANISOU 461 C ASP A 57 7172 5352 6836 603 145 427 C ATOM 462 O ASP A 57 64.646 19.861 58.890 1.00 53.75 O ANISOU 462 O ASP A 57 7564 5777 7080 611 185 396 O ATOM 463 CB ASP A 57 67.754 20.643 59.406 1.00 55.84 C ANISOU 463 CB ASP A 57 7908 5975 7332 615 -38 565 C ATOM 464 CG ASP A 57 68.474 21.257 60.601 1.00 72.17 C ANISOU 464 CG ASP A 57 10099 8038 9283 597 -132 701 C ATOM 465 OD1 ASP A 57 67.926 21.193 61.723 1.00 79.91 O ANISOU 465 OD1 ASP A 57 11169 8998 10193 585 -118 777 O ATOM 466 OD2 ASP A 57 69.586 21.805 60.423 1.00 78.22 O ANISOU 466 OD2 ASP A 57 10874 8826 10019 585 -221 734 O ATOM 467 N LEU A 58 66.047 18.585 57.683 1.00 51.29 N ANISOU 467 N LEU A 58 7103 5364 7021 589 182 344 N ATOM 468 CA LEU A 58 65.084 18.368 56.606 1.00 54.18 C ANISOU 468 CA LEU A 58 7386 5789 7410 563 262 206 C ATOM 469 C LEU A 58 63.973 17.371 56.964 1.00 61.10 C ANISOU 469 C LEU A 58 8237 6636 8342 520 357 198 C ATOM 470 O LEU A 58 62.818 17.542 56.567 1.00 65.77 O ANISOU 470 O LEU A 58 8793 7321 8874 498 409 126 O ATOM 471 CB LEU A 58 65.801 17.901 55.339 1.00 41.70 C ANISOU 471 CB LEU A 58 5710 4180 5953 548 276 113 C ATOM 472 CG LEU A 58 66.707 18.962 54.713 1.00 40.12 C ANISOU 472 CG LEU A 58 5516 4038 5689 582 194 90 C ATOM 473 CD1 LEU A 58 67.342 18.422 53.455 1.00 45.59 C ANISOU 473 CD1 LEU A 58 6114 4701 6508 566 224 -5 C ATOM 474 CD2 LEU A 58 65.975 20.278 54.428 1.00 34.19 C ANISOU 474 CD2 LEU A 58 4805 3422 4764 602 171 40 C ATOM 475 N ASP A 59 64.323 16.338 57.718 1.00 55.07 N ANISOU 475 N ASP A 59 7486 5749 7687 507 379 283 N ATOM 476 CA ASP A 59 63.408 15.224 57.940 1.00 57.94 C ANISOU 476 CA ASP A 59 7823 6064 8128 453 478 269 C ATOM 477 C ASP A 59 62.375 15.508 59.042 1.00 51.13 C ANISOU 477 C ASP A 59 7026 5248 7154 454 492 338 C ATOM 478 O ASP A 59 62.423 14.935 60.135 1.00 55.87 O ANISOU 478 O ASP A 59 7680 5764 7784 452 501 446 O ATOM 479 CB ASP A 59 64.202 13.944 58.232 1.00 55.38 C ANISOU 479 CB ASP A 59 7489 5575 7977 445 513 331 C ATOM 480 CG ASP A 59 63.339 12.717 58.202 1.00 61.65 C ANISOU 480 CG ASP A 59 8255 6302 8867 374 629 290 C ATOM 481 OD1 ASP A 59 62.202 12.808 57.685 1.00 67.30 O ANISOU 481 OD1 ASP A 59 8932 7113 9527 317 679 190 O ATOM 482 OD2 ASP A 59 63.794 11.662 58.690 1.00 67.88 O ANISOU 482 OD2 ASP A 59 9060 6948 9784 373 673 363 O ATOM 483 N GLN A 60 61.435 16.386 58.732 1.00 46.88 N ANISOU 483 N GLN A 60 6480 4846 6486 462 500 281 N ATOM 484 CA GLN A 60 60.440 16.835 59.702 1.00 58.91 C ANISOU 484 CA GLN A 60 8067 6429 7886 479 522 346 C ATOM 485 C GLN A 60 59.538 15.711 60.200 1.00 57.07 C ANISOU 485 C GLN A 60 7807 6155 7721 418 610 365 C ATOM 486 O GLN A 60 59.130 15.711 61.351 1.00 58.94 O ANISOU 486 O GLN A 60 8118 6375 7904 430 623 461 O ATOM 487 CB GLN A 60 59.566 17.933 59.095 1.00 71.40 C ANISOU 487 CB GLN A 60 9625 8172 9332 510 533 281 C ATOM 488 CG GLN A 60 60.189 19.311 59.085 1.00 83.01 C ANISOU 488 CG GLN A 60 11177 9684 10677 583 456 299 C ATOM 489 CD GLN A 60 59.144 20.395 58.913 1.00 98.19 C ANISOU 489 CD GLN A 60 13111 11749 12449 635 490 279 C ATOM 490 OE1 GLN A 60 58.034 20.129 58.440 1.00107.38 O ANISOU 490 OE1 GLN A 60 14178 13007 13614 613 560 232 O ATOM 491 NE2 GLN A 60 59.483 21.619 59.310 1.00 98.84 N ANISOU 491 NE2 GLN A 60 13313 11846 12394 701 447 323 N ATOM 492 N CYS A 61 59.218 14.761 59.332 1.00 48.27 N ANISOU 492 N CYS A 61 6595 5027 6720 344 676 272 N ATOM 493 CA CYS A 61 58.331 13.691 59.731 1.00 56.21 C ANISOU 493 CA CYS A 61 7577 5997 7785 269 765 281 C ATOM 494 C CYS A 61 59.097 12.531 60.357 1.00 63.92 C ANISOU 494 C CYS A 61 8597 6786 8904 250 784 352 C ATOM 495 O CYS A 61 58.496 11.550 60.794 1.00 71.71 O ANISOU 495 O CYS A 61 9582 7711 9952 187 861 373 O ATOM 496 CB CYS A 61 57.500 13.241 58.533 1.00 55.03 C ANISOU 496 CB CYS A 61 7313 5932 7666 176 833 147 C ATOM 497 SG CYS A 61 56.437 14.577 57.943 1.00 67.18 S ANISOU 497 SG CYS A 61 8786 7710 9028 208 818 99 S ATOM 498 N ARG A 62 60.421 12.661 60.400 1.00 58.53 N ANISOU 498 N ARG A 62 7949 6019 8271 307 717 399 N ATOM 499 CA ARG A 62 61.301 11.619 60.936 1.00 53.91 C ANISOU 499 CA ARG A 62 7394 5262 7828 312 731 486 C ATOM 500 C ARG A 62 61.016 10.252 60.338 1.00 53.54 C ANISOU 500 C ARG A 62 7298 5113 7932 231 846 412 C ATOM 501 O ARG A 62 60.963 9.268 61.060 1.00 58.80 O ANISOU 501 O ARG A 62 8000 5659 8683 209 903 486 O ATOM 502 CB ARG A 62 61.208 11.546 62.462 1.00 58.60 C ANISOU 502 CB ARG A 62 8077 5813 8376 336 712 640 C ATOM 503 CG ARG A 62 61.709 12.806 63.172 1.00 76.63 C ANISOU 503 CG ARG A 62 10438 8165 10512 404 600 728 C ATOM 504 CD ARG A 62 61.508 12.737 64.689 1.00 87.39 C ANISOU 504 CD ARG A 62 11899 9495 11811 411 587 873 C ATOM 505 NE ARG A 62 60.138 13.047 65.096 1.00 92.62 N ANISOU 505 NE ARG A 62 12586 10243 12363 389 643 853 N ATOM 506 CZ ARG A 62 59.677 12.908 66.336 1.00 95.85 C ANISOU 506 CZ ARG A 62 13074 10631 12713 383 661 958 C ATOM 507 NH1 ARG A 62 60.478 12.460 67.296 1.00 90.73 N ANISOU 507 NH1 ARG A 62 12490 9882 12102 392 620 1092 N ATOM 508 NH2 ARG A 62 58.414 13.212 66.618 1.00 99.86 N ANISOU 508 NH2 ARG A 62 13592 11226 13123 369 722 937 N ATOM 509 N ASP A 63 60.809 10.192 59.028 1.00 60.37 N ANISOU 509 N ASP A 63 8091 6025 8824 179 884 264 N ATOM 510 CA ASP A 63 60.578 8.913 58.357 1.00 62.48 C ANISOU 510 CA ASP A 63 8328 6187 9223 84 1001 175 C ATOM 511 C ASP A 63 61.696 8.572 57.377 1.00 62.83 C ANISOU 511 C ASP A 63 8351 6137 9386 103 1017 114 C ATOM 512 O ASP A 63 61.561 7.648 56.581 1.00 58.85 O ANISOU 512 O ASP A 63 7830 5553 8979 20 1119 12 O ATOM 513 CB ASP A 63 59.201 8.859 57.666 1.00 62.64 C ANISOU 513 CB ASP A 63 8287 6338 9177 -34 1061 49 C ATOM 514 CG ASP A 63 58.979 9.989 56.662 1.00 67.52 C ANISOU 514 CG ASP A 63 8836 7139 9681 -25 1000 -49 C ATOM 515 OD1 ASP A 63 59.958 10.545 56.116 1.00 65.46 O ANISOU 515 OD1 ASP A 63 8570 6872 9429 42 940 -69 O ATOM 516 OD2 ASP A 63 57.800 10.315 56.407 1.00 71.63 O ANISOU 516 OD2 ASP A 63 9301 7815 10102 -85 1016 -100 O ATOM 517 N GLY A 64 62.787 9.339 57.436 1.00 60.24 N ANISOU 517 N GLY A 64 8027 5820 9042 206 919 175 N ATOM 518 CA GLY A 64 63.974 9.086 56.632 1.00 52.78 C ANISOU 518 CA GLY A 64 7058 4787 8209 245 928 145 C ATOM 519 C GLY A 64 63.811 9.494 55.176 1.00 62.21 C ANISOU 519 C GLY A 64 8191 6076 9372 196 938 -26 C ATOM 520 O GLY A 64 64.724 9.346 54.361 1.00 61.40 O ANISOU 520 O GLY A 64 8064 5914 9350 222 953 -72 O ATOM 521 N LYS A 65 62.634 10.010 54.846 1.00 61.87 N ANISOU 521 N LYS A 65 8116 6186 9205 128 933 -112 N ATOM 522 CA LYS A 65 62.321 10.386 53.482 1.00 57.90 C ANISOU 522 CA LYS A 65 7549 5794 8656 67 942 -268 C ATOM 523 C LYS A 65 62.319 11.902 53.365 1.00 57.71 C ANISOU 523 C LYS A 65 7503 5943 8480 137 825 -260 C ATOM 524 O LYS A 65 61.844 12.607 54.256 1.00 70.58 O ANISOU 524 O LYS A 65 9163 7652 10002 181 769 -174 O ATOM 525 CB LYS A 65 60.962 9.810 53.086 1.00 58.23 C ANISOU 525 CB LYS A 65 7557 5900 8670 -73 1028 -368 C ATOM 526 CG LYS A 65 60.882 8.295 53.213 1.00 62.97 C ANISOU 526 CG LYS A 65 8197 6318 9409 -159 1156 -384 C ATOM 527 CD LYS A 65 59.476 7.794 52.913 1.00 69.76 C ANISOU 527 CD LYS A 65 9025 7261 10219 -317 1231 -473 C ATOM 528 CE LYS A 65 59.398 6.275 53.012 1.00 69.58 C ANISOU 528 CE LYS A 65 9062 7045 10331 -418 1369 -498 C ATOM 529 NZ LYS A 65 57.989 5.810 53.150 1.00 70.09 N ANISOU 529 NZ LYS A 65 9106 7192 10335 -568 1428 -537 N ATOM 530 N VAL A 66 62.874 12.404 52.274 1.00 45.63 N ANISOU 530 N VAL A 66 5933 4463 6942 148 796 -347 N ATOM 531 CA VAL A 66 62.874 13.835 52.036 1.00 46.52 C ANISOU 531 CA VAL A 66 6032 4733 6911 208 696 -349 C ATOM 532 C VAL A 66 62.237 14.121 50.684 1.00 44.15 C ANISOU 532 C VAL A 66 5654 4569 6551 135 718 -496 C ATOM 533 O VAL A 66 62.720 13.685 49.647 1.00 45.27 O ANISOU 533 O VAL A 66 5764 4670 6767 90 757 -597 O ATOM 534 CB VAL A 66 64.303 14.416 52.126 1.00 53.71 C ANISOU 534 CB VAL A 66 6972 5592 7843 306 614 -284 C ATOM 535 CG1 VAL A 66 64.394 15.785 51.433 1.00 43.80 C ANISOU 535 CG1 VAL A 66 5698 4487 6458 344 533 -332 C ATOM 536 CG2 VAL A 66 64.729 14.514 53.586 1.00 54.79 C ANISOU 536 CG2 VAL A 66 7183 5660 7973 374 561 -119 C ATOM 537 N GLY A 67 61.121 14.829 50.705 1.00 46.18 N ANISOU 537 N GLY A 67 5880 4994 6673 123 699 -504 N ATOM 538 CA GLY A 67 60.394 15.078 49.486 1.00 34.60 C ANISOU 538 CA GLY A 67 4327 3681 5139 48 717 -625 C ATOM 539 C GLY A 67 60.782 16.407 48.880 1.00 37.89 C ANISOU 539 C GLY A 67 4729 4214 5453 127 634 -640 C ATOM 540 O GLY A 67 61.653 17.122 49.395 1.00 41.68 O ANISOU 540 O GLY A 67 5273 4648 5914 231 565 -563 O ATOM 541 N PHE A 68 60.087 16.752 47.805 1.00 33.85 N ANISOU 541 N PHE A 68 4135 3864 4864 69 641 -733 N ATOM 542 CA PHE A 68 60.484 17.837 46.949 1.00 38.20 C ANISOU 542 CA PHE A 68 4663 4518 5334 122 579 -772 C ATOM 543 C PHE A 68 60.426 19.158 47.695 1.00 44.35 C ANISOU 543 C PHE A 68 5497 5364 5991 253 510 -665 C ATOM 544 O PHE A 68 61.337 19.974 47.604 1.00 51.21 O ANISOU 544 O PHE A 68 6415 6211 6833 331 447 -646 O ATOM 545 CB PHE A 68 59.644 17.864 45.667 1.00 36.31 C ANISOU 545 CB PHE A 68 4316 4450 5030 23 604 -883 C ATOM 546 CG PHE A 68 60.086 18.915 44.706 1.00 37.71 C ANISOU 546 CG PHE A 68 4469 4728 5130 73 546 -927 C ATOM 547 CD1 PHE A 68 61.365 18.892 44.191 1.00 44.10 C ANISOU 547 CD1 PHE A 68 5313 5429 6013 92 525 -974 C ATOM 548 CD2 PHE A 68 59.252 19.947 44.352 1.00 32.56 C ANISOU 548 CD2 PHE A 68 3761 4276 4333 110 515 -909 C ATOM 549 CE1 PHE A 68 61.797 19.873 43.331 1.00 39.47 C ANISOU 549 CE1 PHE A 68 4710 4931 5354 137 471 -1012 C ATOM 550 CE2 PHE A 68 59.685 20.929 43.491 1.00 41.41 C ANISOU 550 CE2 PHE A 68 4870 5482 5383 161 464 -942 C ATOM 551 CZ PHE A 68 60.962 20.883 42.977 1.00 38.69 C ANISOU 551 CZ PHE A 68 4564 5025 5111 168 440 -998 C ATOM 552 N GLN A 69 59.370 19.346 48.464 1.00 42.66 N ANISOU 552 N GLN A 69 5283 5225 5702 271 530 -594 N ATOM 553 CA GLN A 69 59.221 20.556 49.257 1.00 37.91 C ANISOU 553 CA GLN A 69 4754 4672 4979 393 487 -491 C ATOM 554 C GLN A 69 60.367 20.703 50.256 1.00 36.67 C ANISOU 554 C GLN A 69 4721 4352 4858 460 438 -408 C ATOM 555 O GLN A 69 60.946 21.784 50.366 1.00 44.36 O ANISOU 555 O GLN A 69 5768 5335 5753 542 379 -372 O ATOM 556 CB GLN A 69 57.868 20.564 49.970 1.00 32.71 C ANISOU 556 CB GLN A 69 4072 4107 4248 398 537 -424 C ATOM 557 CG GLN A 69 57.409 21.932 50.437 1.00 47.54 C ANISOU 557 CG GLN A 69 6005 6084 5975 523 520 -339 C ATOM 558 CD GLN A 69 55.986 21.912 50.988 1.00 55.61 C ANISOU 558 CD GLN A 69 6980 7221 6929 531 585 -274 C ATOM 559 OE1 GLN A 69 55.317 22.938 51.021 1.00 61.15 O ANISOU 559 OE1 GLN A 69 7681 8048 7506 622 599 -221 O ATOM 560 NE2 GLN A 69 55.524 20.741 51.418 1.00 51.54 N ANISOU 560 NE2 GLN A 69 6427 6661 6495 438 632 -273 N ATOM 561 N SER A 70 60.700 19.633 50.981 1.00 34.72 N ANISOU 561 N SER A 70 4504 3962 4728 421 462 -373 N ATOM 562 CA SER A 70 61.897 19.668 51.822 1.00 39.64 C ANISOU 562 CA SER A 70 5224 4442 5395 472 409 -290 C ATOM 563 C SER A 70 63.163 19.974 51.010 1.00 45.20 C ANISOU 563 C SER A 70 5922 5111 6140 488 354 -336 C ATOM 564 O SER A 70 64.001 20.776 51.418 1.00 51.66 O ANISOU 564 O SER A 70 6816 5905 6906 549 282 -273 O ATOM 565 CB SER A 70 62.071 18.365 52.587 1.00 35.55 C ANISOU 565 CB SER A 70 4720 3779 5009 428 452 -243 C ATOM 566 OG SER A 70 60.974 18.170 53.452 1.00 47.05 O ANISOU 566 OG SER A 70 6194 5265 6419 417 496 -187 O ATOM 567 N PHE A 71 63.291 19.328 49.862 1.00 36.38 N ANISOU 567 N PHE A 71 4720 3994 5109 424 393 -447 N ATOM 568 CA PHE A 71 64.428 19.555 49.000 1.00 44.42 C ANISOU 568 CA PHE A 71 5722 4985 6171 436 356 -499 C ATOM 569 C PHE A 71 64.556 21.051 48.702 1.00 48.69 C ANISOU 569 C PHE A 71 6294 5639 6565 501 283 -494 C ATOM 570 O PHE A 71 65.618 21.661 48.865 1.00 49.45 O ANISOU 570 O PHE A 71 6445 5697 6647 549 215 -449 O ATOM 571 CB PHE A 71 64.235 18.758 47.710 1.00 41.56 C ANISOU 571 CB PHE A 71 5268 4635 5887 347 424 -636 C ATOM 572 CG PHE A 71 65.183 19.136 46.614 1.00 42.67 C ANISOU 572 CG PHE A 71 5382 4786 6046 355 395 -709 C ATOM 573 CD1 PHE A 71 66.552 18.922 46.754 1.00 44.01 C ANISOU 573 CD1 PHE A 71 5578 4831 6312 396 371 -667 C ATOM 574 CD2 PHE A 71 64.706 19.686 45.432 1.00 42.94 C ANISOU 574 CD2 PHE A 71 5356 4962 5998 322 395 -812 C ATOM 575 CE1 PHE A 71 67.435 19.261 45.737 1.00 40.44 C ANISOU 575 CE1 PHE A 71 5096 4392 5878 404 350 -731 C ATOM 576 CE2 PHE A 71 65.583 20.032 44.400 1.00 42.15 C ANISOU 576 CE2 PHE A 71 5233 4872 5911 327 371 -881 C ATOM 577 CZ PHE A 71 66.948 19.819 44.560 1.00 42.20 C ANISOU 577 CZ PHE A 71 5270 4748 6017 368 351 -843 C ATOM 578 N PHE A 72 63.445 21.641 48.295 1.00 42.42 N ANISOU 578 N PHE A 72 5466 4990 5660 501 302 -531 N ATOM 579 CA PHE A 72 63.423 23.053 47.973 1.00 39.25 C ANISOU 579 CA PHE A 72 5099 4697 5117 569 252 -524 C ATOM 580 C PHE A 72 63.751 23.939 49.175 1.00 37.40 C ANISOU 580 C PHE A 72 4999 4419 4791 648 202 -407 C ATOM 581 O PHE A 72 64.311 25.022 49.025 1.00 43.83 O ANISOU 581 O PHE A 72 5878 5257 5517 698 149 -393 O ATOM 582 CB PHE A 72 62.079 23.441 47.373 1.00 36.16 C ANISOU 582 CB PHE A 72 4634 4475 4628 564 293 -564 C ATOM 583 CG PHE A 72 62.207 24.404 46.268 1.00 40.27 C ANISOU 583 CG PHE A 72 5126 5108 5065 591 263 -621 C ATOM 584 CD1 PHE A 72 62.317 23.961 44.968 1.00 35.35 C ANISOU 584 CD1 PHE A 72 4403 4535 4493 516 276 -735 C ATOM 585 CD2 PHE A 72 62.278 25.761 46.526 1.00 51.89 C ANISOU 585 CD2 PHE A 72 6686 6624 6406 688 226 -562 C ATOM 586 CE1 PHE A 72 62.454 24.857 43.927 1.00 38.52 C ANISOU 586 CE1 PHE A 72 4778 5045 4815 540 247 -784 C ATOM 587 CE2 PHE A 72 62.429 26.667 45.490 1.00 57.46 C ANISOU 587 CE2 PHE A 72 7371 7426 7035 717 202 -609 C ATOM 588 CZ PHE A 72 62.520 26.209 44.186 1.00 52.52 C ANISOU 588 CZ PHE A 72 6631 6862 6461 644 208 -718 C ATOM 589 N SER A 73 63.401 23.473 50.363 1.00 30.13 N ANISOU 589 N SER A 73 4129 3434 3886 650 223 -325 N ATOM 590 CA SER A 73 63.767 24.171 51.588 1.00 41.05 C ANISOU 590 CA SER A 73 5651 4763 5184 704 179 -213 C ATOM 591 C SER A 73 65.300 24.202 51.750 1.00 42.09 C ANISOU 591 C SER A 73 5829 4795 5367 697 101 -179 C ATOM 592 O SER A 73 65.876 25.230 52.135 1.00 41.55 O ANISOU 592 O SER A 73 5868 4726 5193 730 41 -128 O ATOM 593 CB SER A 73 63.094 23.507 52.790 1.00 48.93 C ANISOU 593 CB SER A 73 6683 5710 6200 695 222 -135 C ATOM 594 OG SER A 73 63.903 23.577 53.954 1.00 56.18 O ANISOU 594 OG SER A 73 7715 6523 7109 706 170 -31 O ATOM 595 N LEU A 74 65.955 23.091 51.418 1.00 32.19 N ANISOU 595 N LEU A 74 4497 3462 4272 652 108 -205 N ATOM 596 CA LEU A 74 67.419 23.035 51.374 1.00 39.81 C ANISOU 596 CA LEU A 74 5470 4353 5304 650 43 -171 C ATOM 597 C LEU A 74 68.005 24.060 50.415 1.00 38.03 C ANISOU 597 C LEU A 74 5244 4198 5009 667 -6 -229 C ATOM 598 O LEU A 74 68.853 24.888 50.797 1.00 37.61 O ANISOU 598 O LEU A 74 5271 4137 4881 683 -82 -167 O ATOM 599 CB LEU A 74 67.893 21.644 50.955 1.00 44.85 C ANISOU 599 CB LEU A 74 6011 4899 6131 613 90 -203 C ATOM 600 CG LEU A 74 69.353 21.582 50.531 1.00 42.38 C ANISOU 600 CG LEU A 74 5668 4535 5899 621 42 -188 C ATOM 601 CD1 LEU A 74 70.217 21.990 51.710 1.00 35.97 C ANISOU 601 CD1 LEU A 74 4940 3684 5044 643 -45 -42 C ATOM 602 CD2 LEU A 74 69.732 20.178 50.032 1.00 37.04 C ANISOU 602 CD2 LEU A 74 4902 3758 5414 596 117 -226 C ATOM 603 N ILE A 75 67.555 23.998 49.166 1.00 29.16 N ANISOU 603 N ILE A 75 4032 3145 3903 652 37 -347 N ATOM 604 CA ILE A 75 68.054 24.912 48.154 1.00 28.39 C ANISOU 604 CA ILE A 75 3926 3117 3744 665 -1 -409 C ATOM 605 C ILE A 75 67.795 26.359 48.568 1.00 33.57 C ANISOU 605 C ILE A 75 4699 3839 4218 715 -42 -362 C ATOM 606 O ILE A 75 68.611 27.243 48.322 1.00 33.31 O ANISOU 606 O ILE A 75 4719 3818 4121 727 -102 -355 O ATOM 607 CB ILE A 75 67.366 24.698 46.807 1.00 27.36 C ANISOU 607 CB ILE A 75 3689 3076 3631 636 55 -537 C ATOM 608 CG1 ILE A 75 67.399 23.223 46.397 1.00 29.72 C ANISOU 608 CG1 ILE A 75 3893 3304 4096 573 121 -597 C ATOM 609 CG2 ILE A 75 68.027 25.598 45.752 1.00 20.19 C ANISOU 609 CG2 ILE A 75 2772 2231 2668 649 12 -596 C ATOM 610 CD1 ILE A 75 68.798 22.609 46.422 1.00 33.94 C ANISOU 610 CD1 ILE A 75 4417 3717 4764 570 103 -570 C ATOM 611 N ALA A 76 66.637 26.581 49.178 1.00 35.05 N ANISOU 611 N ALA A 76 4929 4065 4323 742 0 -331 N ATOM 612 CA ALA A 76 66.277 27.869 49.752 1.00 42.68 C ANISOU 612 CA ALA A 76 6029 5070 5118 799 -13 -275 C ATOM 613 C ALA A 76 67.358 28.350 50.702 1.00 46.58 C ANISOU 613 C ALA A 76 6655 5479 5563 790 -87 -186 C ATOM 614 O ALA A 76 67.975 29.393 50.496 1.00 45.34 O ANISOU 614 O ALA A 76 6581 5337 5309 800 -135 -183 O ATOM 615 CB ALA A 76 64.934 27.752 50.495 1.00 34.77 C ANISOU 615 CB ALA A 76 5049 4099 4065 830 57 -233 C ATOM 616 N GLY A 77 67.580 27.565 51.746 1.00 43.95 N ANISOU 616 N GLY A 77 6342 5062 5295 763 -98 -109 N ATOM 617 CA GLY A 77 68.580 27.884 52.731 1.00 32.75 C ANISOU 617 CA GLY A 77 5036 3576 3831 737 -174 -10 C ATOM 618 C GLY A 77 69.915 28.182 52.095 1.00 31.66 C ANISOU 618 C GLY A 77 4873 3436 3719 708 -250 -23 C ATOM 619 O GLY A 77 70.562 29.178 52.431 1.00 31.72 O ANISOU 619 O GLY A 77 4999 3447 3606 691 -313 21 O ATOM 620 N LEU A 78 70.328 27.343 51.157 1.00 33.26 N ANISOU 620 N LEU A 78 4929 3635 4074 696 -239 -85 N ATOM 621 CA LEU A 78 71.582 27.618 50.458 1.00 36.59 C ANISOU 621 CA LEU A 78 5313 4063 4526 674 -301 -99 C ATOM 622 C LEU A 78 71.545 28.903 49.622 1.00 40.59 C ANISOU 622 C LEU A 78 5870 4649 4902 690 -316 -167 C ATOM 623 O LEU A 78 72.499 29.694 49.650 1.00 40.24 O ANISOU 623 O LEU A 78 5892 4611 4787 664 -387 -134 O ATOM 624 CB LEU A 78 72.003 26.426 49.591 1.00 36.68 C ANISOU 624 CB LEU A 78 5165 4044 4729 665 -265 -156 C ATOM 625 CG LEU A 78 72.408 25.173 50.372 1.00 38.67 C ANISOU 625 CG LEU A 78 5368 4200 5123 655 -256 -70 C ATOM 626 CD1 LEU A 78 72.640 23.998 49.426 1.00 30.61 C ANISOU 626 CD1 LEU A 78 4208 3134 4286 653 -188 -143 C ATOM 627 CD2 LEU A 78 73.656 25.471 51.256 1.00 35.64 C ANISOU 627 CD2 LEU A 78 5037 3792 4714 634 -356 68 C ATOM 628 N THR A 79 70.455 29.130 48.891 1.00 40.10 N ANISOU 628 N THR A 79 5779 4654 4805 726 -249 -254 N ATOM 629 CA THR A 79 70.445 30.237 47.933 1.00 29.86 C ANISOU 629 CA THR A 79 4508 3433 3404 748 -255 -319 C ATOM 630 C THR A 79 70.303 31.561 48.640 1.00 33.57 C ANISOU 630 C THR A 79 5161 3907 3688 771 -274 -261 C ATOM 631 O THR A 79 70.861 32.565 48.219 1.00 33.07 O ANISOU 631 O THR A 79 5168 3867 3531 767 -311 -274 O ATOM 632 CB THR A 79 69.397 30.052 46.834 1.00 28.80 C ANISOU 632 CB THR A 79 4268 3386 3290 776 -183 -421 C ATOM 633 OG1 THR A 79 69.542 28.737 46.274 1.00 26.78 O ANISOU 633 OG1 THR A 79 3865 3107 3203 736 -155 -478 O ATOM 634 CG2 THR A 79 69.597 31.094 45.707 1.00 20.23 C ANISOU 634 CG2 THR A 79 3189 2379 2117 794 -197 -485 C ATOM 635 N ILE A 80 69.595 31.545 49.757 1.00 38.83 N ANISOU 635 N ILE A 80 5916 4541 4297 790 -244 -195 N ATOM 636 CA ILE A 80 69.401 32.744 50.538 1.00 34.07 C ANISOU 636 CA ILE A 80 5510 3922 3512 810 -243 -139 C ATOM 637 C ILE A 80 70.687 33.146 51.251 1.00 44.37 C ANISOU 637 C ILE A 80 6929 5168 4762 735 -336 -68 C ATOM 638 O ILE A 80 70.988 34.331 51.345 1.00 44.69 O ANISOU 638 O ILE A 80 7122 5206 4653 724 -355 -57 O ATOM 639 CB ILE A 80 68.231 32.546 51.511 1.00 43.22 C ANISOU 639 CB ILE A 80 6727 5066 4630 852 -172 -90 C ATOM 640 CG1 ILE A 80 66.908 32.576 50.723 1.00 36.74 C ANISOU 640 CG1 ILE A 80 5816 4336 3808 930 -80 -151 C ATOM 641 CG2 ILE A 80 68.234 33.592 52.635 1.00 36.76 C ANISOU 641 CG2 ILE A 80 6140 4196 3633 853 -170 -14 C ATOM 642 CD1 ILE A 80 65.747 31.982 51.476 1.00 32.41 C ANISOU 642 CD1 ILE A 80 5251 3790 3274 962 -8 -111 C ATOM 643 N ALA A 81 71.461 32.167 51.726 1.00 42.07 N ANISOU 643 N ALA A 81 6563 4834 4590 679 -392 -15 N ATOM 644 CA ALA A 81 72.767 32.470 52.323 1.00 36.48 C ANISOU 644 CA ALA A 81 5928 4095 3838 596 -493 65 C ATOM 645 C ALA A 81 73.733 33.023 51.285 1.00 36.80 C ANISOU 645 C ALA A 81 5928 4177 3876 568 -545 18 C ATOM 646 O ALA A 81 74.438 33.986 51.566 1.00 42.03 O ANISOU 646 O ALA A 81 6721 4841 4408 509 -604 54 O ATOM 647 CB ALA A 81 73.368 31.248 53.045 1.00 36.89 C ANISOU 647 CB ALA A 81 5887 4102 4026 556 -537 151 C ATOM 648 N CYS A 82 73.751 32.438 50.085 1.00 31.77 N ANISOU 648 N CYS A 82 5121 3575 3374 601 -518 -66 N ATOM 649 CA CYS A 82 74.554 32.983 48.987 1.00 29.67 C ANISOU 649 CA CYS A 82 4814 3355 3105 583 -553 -122 C ATOM 650 C CYS A 82 74.203 34.424 48.681 1.00 37.21 C ANISOU 650 C CYS A 82 5919 4341 3877 599 -538 -160 C ATOM 651 O CYS A 82 75.078 35.272 48.511 1.00 38.78 O ANISOU 651 O CYS A 82 6193 4552 3989 547 -596 -148 O ATOM 652 CB CYS A 82 74.360 32.180 47.711 1.00 27.88 C ANISOU 652 CB CYS A 82 4402 3160 3030 621 -503 -222 C ATOM 653 SG CYS A 82 75.126 30.585 47.827 1.00 40.51 S ANISOU 653 SG CYS A 82 5834 4707 4852 600 -513 -181 S ATOM 654 N ASN A 83 72.909 34.694 48.608 1.00 42.60 N ANISOU 654 N ASN A 83 6643 5041 4503 674 -453 -199 N ATOM 655 CA ASN A 83 72.460 36.020 48.257 1.00 41.59 C ANISOU 655 CA ASN A 83 6651 4940 4212 713 -416 -229 C ATOM 656 C ASN A 83 72.824 37.011 49.354 1.00 42.36 C ANISOU 656 C ASN A 83 6941 4975 4181 652 -433 -148 C ATOM 657 O ASN A 83 73.203 38.137 49.078 1.00 45.05 O ANISOU 657 O ASN A 83 7297 5308 4512 602 -412 -145 O ATOM 658 CB ASN A 83 70.959 36.030 48.005 1.00 44.74 C ANISOU 658 CB ASN A 83 7028 5380 4593 814 -313 -265 C ATOM 659 CG ASN A 83 70.435 37.424 47.728 1.00 48.78 C ANISOU 659 CG ASN A 83 7600 5904 5029 840 -248 -246 C ATOM 660 OD1 ASN A 83 70.667 37.990 46.643 1.00 43.45 O ANISOU 660 OD1 ASN A 83 6848 5277 4386 831 -245 -280 O ATOM 661 ND2 ASN A 83 69.744 37.998 48.709 1.00 43.47 N ANISOU 661 ND2 ASN A 83 7033 5179 4307 857 -188 -180 N ATOM 662 N ASP A 84 72.710 36.581 50.603 1.00 44.96 N ANISOU 662 N ASP A 84 7352 5251 4479 629 -449 -76 N ATOM 663 CA ASP A 84 73.128 37.407 51.735 1.00 46.13 C ANISOU 663 CA ASP A 84 7606 5338 4584 528 -445 -10 C ATOM 664 C ASP A 84 74.600 37.801 51.627 1.00 49.21 C ANISOU 664 C ASP A 84 7981 5738 4980 409 -532 11 C ATOM 665 O ASP A 84 74.934 38.985 51.671 1.00 55.41 O ANISOU 665 O ASP A 84 8813 6506 5734 346 -503 7 O ATOM 666 CB ASP A 84 72.853 36.693 53.058 1.00 41.86 C ANISOU 666 CB ASP A 84 7127 4753 4025 512 -456 63 C ATOM 667 CG ASP A 84 71.398 36.822 53.500 1.00 47.08 C ANISOU 667 CG ASP A 84 7841 5391 4656 601 -342 55 C ATOM 668 OD1 ASP A 84 70.644 37.626 52.869 1.00 38.64 O ANISOU 668 OD1 ASP A 84 6765 4337 3580 669 -256 7 O ATOM 669 OD2 ASP A 84 71.021 36.124 54.478 1.00 52.48 O ANISOU 669 OD2 ASP A 84 8561 6045 5333 603 -338 111 O ATOM 670 N TYR A 85 75.464 36.804 51.455 1.00 42.08 N ANISOU 670 N TYR A 85 7004 4863 4121 385 -641 43 N ATOM 671 CA TYR A 85 76.879 37.040 51.219 1.00 39.59 C ANISOU 671 CA TYR A 85 6641 4580 3822 282 -729 72 C ATOM 672 C TYR A 85 77.081 37.911 49.984 1.00 47.35 C ANISOU 672 C TYR A 85 7582 5598 4809 290 -692 -8 C ATOM 673 O TYR A 85 77.904 38.822 49.989 1.00 59.67 O ANISOU 673 O TYR A 85 9159 7169 6344 197 -701 7 O ATOM 674 CB TYR A 85 77.617 35.706 51.072 1.00 42.93 C ANISOU 674 CB TYR A 85 6930 5023 4357 287 -831 125 C ATOM 675 CG TYR A 85 79.113 35.836 50.950 1.00 45.73 C ANISOU 675 CG TYR A 85 7233 5423 4720 186 -938 186 C ATOM 676 CD1 TYR A 85 79.701 36.147 49.738 1.00 45.34 C ANISOU 676 CD1 TYR A 85 7100 5422 4707 187 -949 121 C ATOM 677 CD2 TYR A 85 79.937 35.627 52.037 1.00 53.36 C ANISOU 677 CD2 TYR A 85 8204 6396 5676 84 -1014 310 C ATOM 678 CE1 TYR A 85 81.062 36.267 49.606 1.00 51.02 C ANISOU 678 CE1 TYR A 85 7760 6193 5434 96 -1044 183 C ATOM 679 CE2 TYR A 85 81.312 35.738 51.914 1.00 60.86 C ANISOU 679 CE2 TYR A 85 9068 7408 6647 -11 -1098 373 C ATOM 680 CZ TYR A 85 81.867 36.060 50.691 1.00 62.26 C ANISOU 680 CZ TYR A 85 9177 7630 6848 -3 -1116 312 C ATOM 681 OH TYR A 85 83.231 36.188 50.535 1.00 72.46 O ANISOU 681 OH TYR A 85 10376 8994 8163 -94 -1193 379 O ATOM 682 N PHE A 86 76.328 37.625 48.928 1.00 51.17 N ANISOU 682 N PHE A 86 8005 6109 5327 400 -648 -91 N ATOM 683 CA PHE A 86 76.418 38.388 47.681 1.00 50.31 C ANISOU 683 CA PHE A 86 7835 6043 5238 414 -605 -160 C ATOM 684 C PHE A 86 76.221 39.881 47.897 1.00 55.43 C ANISOU 684 C PHE A 86 8562 6660 5838 373 -526 -141 C ATOM 685 O PHE A 86 77.049 40.696 47.504 1.00 58.40 O ANISOU 685 O PHE A 86 8932 7051 6206 303 -538 -138 O ATOM 686 CB PHE A 86 75.344 37.927 46.721 1.00 41.53 C ANISOU 686 CB PHE A 86 6642 4971 4167 533 -544 -245 C ATOM 687 CG PHE A 86 75.346 38.668 45.412 1.00 42.27 C ANISOU 687 CG PHE A 86 6653 5117 4289 543 -498 -299 C ATOM 688 CD1 PHE A 86 76.369 38.490 44.508 1.00 34.07 C ANISOU 688 CD1 PHE A 86 5529 4121 3295 506 -555 -339 C ATOM 689 CD2 PHE A 86 74.306 39.513 45.079 1.00 40.51 C ANISOU 689 CD2 PHE A 86 6436 4905 4052 593 -402 -300 C ATOM 690 CE1 PHE A 86 76.370 39.145 43.318 1.00 40.13 C ANISOU 690 CE1 PHE A 86 6223 4938 4086 508 -510 -380 C ATOM 691 CE2 PHE A 86 74.308 40.182 43.879 1.00 44.32 C ANISOU 691 CE2 PHE A 86 6843 5439 4558 597 -370 -332 C ATOM 692 CZ PHE A 86 75.346 39.996 42.995 1.00 42.71 C ANISOU 692 CZ PHE A 86 6559 5276 4394 549 -420 -373 C ATOM 693 N VAL A 87 75.098 40.231 48.505 1.00 56.36 N ANISOU 693 N VAL A 87 8756 6733 5926 426 -447 -128 N ATOM 694 CA VAL A 87 74.817 41.615 48.830 1.00 55.79 C ANISOU 694 CA VAL A 87 8777 6609 5811 405 -377 -109 C ATOM 695 C VAL A 87 75.940 42.241 49.666 1.00 58.65 C ANISOU 695 C VAL A 87 9223 6934 6129 270 -424 -67 C ATOM 696 O VAL A 87 76.482 43.274 49.286 1.00 58.81 O ANISOU 696 O VAL A 87 9263 6949 6133 219 -414 -72 O ATOM 697 CB VAL A 87 73.479 41.758 49.558 1.00 48.51 C ANISOU 697 CB VAL A 87 7933 5636 4863 484 -294 -92 C ATOM 698 CG1 VAL A 87 73.250 43.195 49.905 1.00 54.60 C ANISOU 698 CG1 VAL A 87 8816 6338 5593 467 -230 -75 C ATOM 699 CG2 VAL A 87 72.362 41.244 48.677 1.00 45.69 C ANISOU 699 CG2 VAL A 87 7479 5338 4543 610 -246 -127 C ATOM 700 N VAL A 88 76.306 41.606 50.776 1.00 52.05 N ANISOU 700 N VAL A 88 8427 6079 5271 209 -478 -22 N ATOM 701 CA VAL A 88 77.312 42.178 51.663 1.00 53.49 C ANISOU 701 CA VAL A 88 8682 6239 5404 72 -523 23 C ATOM 702 C VAL A 88 78.665 42.443 50.979 1.00 58.90 C ANISOU 702 C VAL A 88 9297 6984 6099 -13 -591 27 C ATOM 703 O VAL A 88 79.195 43.548 51.083 1.00 53.64 O ANISOU 703 O VAL A 88 8693 6295 5391 -90 -579 31 O ATOM 704 CB VAL A 88 77.560 41.300 52.912 1.00 56.11 C ANISOU 704 CB VAL A 88 9037 6565 5717 14 -584 85 C ATOM 705 CG1 VAL A 88 78.765 41.835 53.705 1.00 47.08 C ANISOU 705 CG1 VAL A 88 7939 5427 4524 -140 -646 136 C ATOM 706 CG2 VAL A 88 76.294 41.199 53.788 1.00 48.74 C ANISOU 706 CG2 VAL A 88 8194 5566 4759 80 -509 86 C ATOM 707 N HIS A 89 79.217 41.440 50.286 1.00 62.33 N ANISOU 707 N HIS A 89 9607 7489 6587 2 -664 27 N ATOM 708 CA HIS A 89 80.597 41.521 49.781 1.00 52.72 C ANISOU 708 CA HIS A 89 8314 6338 5380 -84 -741 47 C ATOM 709 C HIS A 89 80.738 41.738 48.284 1.00 58.93 C ANISOU 709 C HIS A 89 9011 7172 6209 -33 -722 -17 C ATOM 710 O HIS A 89 81.825 42.062 47.816 1.00 56.95 O ANISOU 710 O HIS A 89 8710 6971 5958 -103 -766 -7 O ATOM 711 CB HIS A 89 81.389 40.254 50.108 1.00 40.89 C ANISOU 711 CB HIS A 89 6728 4890 3918 -118 -855 114 C ATOM 712 CG HIS A 89 81.412 39.903 51.558 1.00 54.15 C ANISOU 712 CG HIS A 89 8466 6544 5565 -179 -888 194 C ATOM 713 ND1 HIS A 89 80.454 39.103 52.144 1.00 58.98 N ANISOU 713 ND1 HIS A 89 9106 7113 6190 -107 -870 205 N ATOM 714 CD2 HIS A 89 82.280 40.232 52.541 1.00 56.46 C ANISOU 714 CD2 HIS A 89 8791 6852 5810 -306 -937 266 C ATOM 715 CE1 HIS A 89 80.734 38.954 53.428 1.00 56.30 C ANISOU 715 CE1 HIS A 89 8810 6765 5816 -188 -905 283 C ATOM 716 NE2 HIS A 89 81.832 39.637 53.695 1.00 56.58 N ANISOU 716 NE2 HIS A 89 8848 6836 5812 -310 -946 319 N ATOM 717 N MET A 90 79.671 41.528 47.522 1.00 63.96 N ANISOU 717 N MET A 90 9618 7802 6880 84 -659 -79 N ATOM 718 CA MET A 90 79.830 41.455 46.072 1.00 62.34 C ANISOU 718 CA MET A 90 9305 7656 6726 130 -653 -142 C ATOM 719 C MET A 90 79.028 42.428 45.216 1.00 64.16 C ANISOU 719 C MET A 90 9538 7884 6958 190 -555 -189 C ATOM 720 O MET A 90 79.490 42.815 44.159 1.00 69.55 O ANISOU 720 O MET A 90 10151 8614 7659 180 -551 -221 O ATOM 721 CB MET A 90 79.601 40.025 45.595 1.00 64.63 C ANISOU 721 CB MET A 90 9502 7974 7080 209 -701 -179 C ATOM 722 CG MET A 90 80.720 39.090 45.987 1.00 64.61 C ANISOU 722 CG MET A 90 9452 7994 7103 152 -826 -124 C ATOM 723 SD MET A 90 80.368 37.438 45.390 1.00 70.14 S ANISOU 723 SD MET A 90 10036 8704 7909 268 -882 -182 S ATOM 724 CE MET A 90 82.021 36.754 45.239 1.00 56.12 C ANISOU 724 CE MET A 90 8085 6973 6267 194 -971 -104 C ATOM 725 N LYS A 91 77.834 42.816 45.650 1.00 70.58 N ANISOU 725 N LYS A 91 10423 8645 7750 253 -480 -184 N ATOM 726 CA LYS A 91 77.005 43.721 44.852 1.00 68.72 C ANISOU 726 CA LYS A 91 10182 8412 7518 317 -397 -209 C ATOM 727 C LYS A 91 77.433 45.171 45.049 1.00 73.67 C ANISOU 727 C LYS A 91 10904 8991 8096 254 -371 -182 C ATOM 728 O LYS A 91 77.813 45.850 44.093 1.00 79.38 O ANISOU 728 O LYS A 91 11587 9747 8827 241 -360 -202 O ATOM 729 CB LYS A 91 75.528 43.553 45.212 1.00 66.21 C ANISOU 729 CB LYS A 91 9897 8063 7198 421 -331 -205 C ATOM 730 CG LYS A 91 74.556 44.381 44.377 1.00 68.13 C ANISOU 730 CG LYS A 91 10121 8320 7445 500 -255 -215 C ATOM 731 CD LYS A 91 73.152 44.358 45.000 1.00 72.87 C ANISOU 731 CD LYS A 91 10778 8884 8027 596 -190 -190 C ATOM 732 CE LYS A 91 72.088 44.944 44.077 1.00 75.06 C ANISOU 732 CE LYS A 91 11010 9198 8311 690 -125 -193 C ATOM 733 NZ LYS A 91 70.744 44.902 44.720 1.00 78.47 N ANISOU 733 NZ LYS A 91 11490 9604 8721 789 -62 -160 N TER 734 LYS A 91 ATOM 735 N PRO B 1 80.947 24.853 37.279 1.00 42.39 N ANISOU 735 N PRO B 1 4979 4626 6501 -95 1086 -442 N ATOM 736 CA PRO B 1 79.805 24.868 38.193 1.00 33.50 C ANISOU 736 CA PRO B 1 3915 3488 5323 15 999 -488 C ATOM 737 C PRO B 1 78.738 23.857 37.796 1.00 40.52 C ANISOU 737 C PRO B 1 4690 4545 6160 12 1126 -700 C ATOM 738 O PRO B 1 78.482 23.652 36.610 1.00 51.63 O ANISOU 738 O PRO B 1 6027 6143 7448 -46 1216 -802 O ATOM 739 CB PRO B 1 79.286 26.292 38.042 1.00 42.43 C ANISOU 739 CB PRO B 1 5202 4674 6245 101 825 -374 C ATOM 740 CG PRO B 1 80.529 27.119 37.720 1.00 45.71 C ANISOU 740 CG PRO B 1 5674 4996 6696 42 766 -200 C ATOM 741 CD PRO B 1 81.623 26.161 37.263 1.00 44.21 C ANISOU 741 CD PRO B 1 5337 4779 6681 -84 936 -238 C ATOM 742 N SER B 2 78.128 23.226 38.797 1.00 34.46 N ANISOU 742 N SER B 2 3904 3709 5482 67 1129 -763 N ATOM 743 CA SER B 2 77.087 22.235 38.579 1.00 34.50 C ANISOU 743 CA SER B 2 3830 3868 5409 40 1164 -900 C ATOM 744 C SER B 2 75.858 22.914 38.043 1.00 36.04 C ANISOU 744 C SER B 2 4056 4251 5386 128 1131 -967 C ATOM 745 O SER B 2 75.761 24.146 38.036 1.00 33.22 O ANISOU 745 O SER B 2 3818 3896 4907 207 1009 -853 O ATOM 746 CB SER B 2 76.713 21.565 39.895 1.00 35.94 C ANISOU 746 CB SER B 2 4033 3961 5662 57 1076 -847 C ATOM 747 OG SER B 2 76.212 22.528 40.809 1.00 39.27 O ANISOU 747 OG SER B 2 4571 4323 6028 197 959 -770 O ATOM 748 N GLN B 3 74.914 22.100 37.594 1.00 36.79 N ANISOU 748 N GLN B 3 4093 4510 5377 84 1125 -1052 N ATOM 749 CA GLN B 3 73.664 22.621 37.081 1.00 39.28 C ANISOU 749 CA GLN B 3 4415 5024 5486 157 1089 -1107 C ATOM 750 C GLN B 3 72.873 23.379 38.144 1.00 41.35 C ANISOU 750 C GLN B 3 4769 5229 5712 319 985 -1048 C ATOM 751 O GLN B 3 72.385 24.483 37.886 1.00 45.90 O ANISOU 751 O GLN B 3 5422 5887 6131 411 903 -996 O ATOM 752 CB GLN B 3 72.842 21.505 36.496 1.00 34.93 C ANISOU 752 CB GLN B 3 3788 4609 4875 73 1097 -1192 C ATOM 753 CG GLN B 3 73.129 21.263 35.039 1.00 40.13 C ANISOU 753 CG GLN B 3 4386 5414 5448 -41 1175 -1276 C ATOM 754 CD GLN B 3 72.047 20.407 34.424 1.00 56.37 C ANISOU 754 CD GLN B 3 6385 7614 7421 -99 1164 -1372 C ATOM 755 OE1 GLN B 3 70.926 20.883 34.174 1.00 64.27 O ANISOU 755 OE1 GLN B 3 7380 8775 8265 -41 1117 -1391 O ATOM 756 NE2 GLN B 3 72.357 19.130 34.203 1.00 50.87 N ANISOU 756 NE2 GLN B 3 5643 6851 6835 -215 1207 -1437 N ATOM 757 N MET B 4 72.787 22.801 39.341 1.00 36.05 N ANISOU 757 N MET B 4 4124 4423 5149 338 927 -985 N ATOM 758 CA MET B 4 72.100 23.438 40.466 1.00 31.97 C ANISOU 758 CA MET B 4 3711 3838 4598 487 822 -910 C ATOM 759 C MET B 4 72.722 24.776 40.792 1.00 31.56 C ANISOU 759 C MET B 4 3793 3632 4567 587 761 -827 C ATOM 760 O MET B 4 72.023 25.761 41.061 1.00 39.72 O ANISOU 760 O MET B 4 4943 4687 5461 709 640 -746 O ATOM 761 CB MET B 4 72.141 22.543 41.709 1.00 39.37 C ANISOU 761 CB MET B 4 4653 4671 5636 458 777 -843 C ATOM 762 CG MET B 4 71.109 21.413 41.732 1.00 43.03 C ANISOU 762 CG MET B 4 5038 5247 6064 414 791 -888 C ATOM 763 SD MET B 4 69.344 21.878 41.564 1.00 47.52 S ANISOU 763 SD MET B 4 5625 5981 6451 542 758 -907 S ATOM 764 CE MET B 4 69.054 23.027 42.905 1.00 37.89 C ANISOU 764 CE MET B 4 4567 4647 5183 727 660 -788 C ATOM 765 N GLU B 5 74.047 24.838 40.771 1.00 39.44 N ANISOU 765 N GLU B 5 4811 4491 5684 503 771 -754 N ATOM 766 CA GLU B 5 74.715 26.120 41.029 1.00 43.54 C ANISOU 766 CA GLU B 5 5496 4882 6163 544 626 -576 C ATOM 767 C GLU B 5 74.294 27.188 40.025 1.00 39.41 C ANISOU 767 C GLU B 5 5035 4512 5427 579 552 -521 C ATOM 768 O GLU B 5 74.100 28.348 40.398 1.00 37.61 O ANISOU 768 O GLU B 5 4961 4219 5110 679 412 -397 O ATOM 769 CB GLU B 5 76.241 25.966 41.059 1.00 38.82 C ANISOU 769 CB GLU B 5 4887 4128 5736 433 654 -500 C ATOM 770 CG GLU B 5 76.744 25.374 42.369 1.00 39.02 C ANISOU 770 CG GLU B 5 4914 3951 5962 432 656 -473 C ATOM 771 CD GLU B 5 78.154 24.826 42.281 1.00 45.07 C ANISOU 771 CD GLU B 5 5600 4621 6905 298 720 -421 C ATOM 772 OE1 GLU B 5 78.619 24.514 41.159 1.00 48.15 O ANISOU 772 OE1 GLU B 5 5890 5083 7321 210 840 -477 O ATOM 773 OE2 GLU B 5 78.799 24.704 43.342 1.00 48.49 O ANISOU 773 OE2 GLU B 5 6061 4989 7373 261 624 -306 O ATOM 774 N HIS B 6 74.156 26.782 38.758 1.00 37.49 N ANISOU 774 N HIS B 6 4672 4468 5103 494 650 -613 N ATOM 775 CA HIS B 6 73.738 27.680 37.684 1.00 35.52 C ANISOU 775 CA HIS B 6 4454 4397 4644 513 593 -563 C ATOM 776 C HIS B 6 72.307 28.118 37.907 1.00 33.88 C ANISOU 776 C HIS B 6 4285 4300 4287 649 517 -569 C ATOM 777 O HIS B 6 71.977 29.286 37.769 1.00 42.03 O ANISOU 777 O HIS B 6 5428 5353 5189 739 400 -447 O ATOM 778 CB HIS B 6 73.866 27.001 36.323 1.00 35.27 C ANISOU 778 CB HIS B 6 4277 4570 4554 382 726 -680 C ATOM 779 CG HIS B 6 75.247 27.057 35.746 1.00 31.06 C ANISOU 779 CG HIS B 6 3732 3973 4097 267 777 -621 C ATOM 780 ND1 HIS B 6 75.845 28.237 35.364 1.00 38.54 N ANISOU 780 ND1 HIS B 6 4783 4890 4972 275 677 -451 N ATOM 781 CD2 HIS B 6 76.148 26.076 35.500 1.00 33.07 C ANISOU 781 CD2 HIS B 6 3880 4184 4503 145 923 -703 C ATOM 782 CE1 HIS B 6 77.056 27.982 34.897 1.00 36.82 C ANISOU 782 CE1 HIS B 6 4517 4622 4852 160 757 -427 C ATOM 783 NE2 HIS B 6 77.262 26.675 34.964 1.00 39.09 N ANISOU 783 NE2 HIS B 6 4677 4900 5276 83 911 -580 N ATOM 784 N ALA B 7 71.465 27.162 38.274 1.00 33.43 N ANISOU 784 N ALA B 7 4130 4308 4263 666 590 -705 N ATOM 785 CA ALA B 7 70.078 27.439 38.601 1.00 33.34 C ANISOU 785 CA ALA B 7 4135 4396 4136 798 532 -713 C ATOM 786 C ALA B 7 69.991 28.462 39.729 1.00 37.71 C ANISOU 786 C ALA B 7 4869 4765 4694 948 399 -572 C ATOM 787 O ALA B 7 69.227 29.450 39.660 1.00 35.66 O ANISOU 787 O ALA B 7 4694 4565 4292 1070 303 -486 O ATOM 788 CB ALA B 7 69.384 26.150 38.982 1.00 34.19 C ANISOU 788 CB ALA B 7 4107 4559 4325 779 638 -874 C ATOM 789 N MET B 8 70.792 28.244 40.765 1.00 35.36 N ANISOU 789 N MET B 8 4634 4240 4562 939 393 -544 N ATOM 790 CA MET B 8 70.711 29.107 41.934 1.00 26.72 C ANISOU 790 CA MET B 8 3717 2963 3473 1071 274 -433 C ATOM 791 C MET B 8 71.155 30.488 41.553 1.00 30.21 C ANISOU 791 C MET B 8 4307 3350 3823 1102 155 -283 C ATOM 792 O MET B 8 70.463 31.468 41.841 1.00 38.83 O ANISOU 792 O MET B 8 5520 4428 4806 1241 59 -204 O ATOM 793 CB MET B 8 71.534 28.540 43.071 1.00 25.53 C ANISOU 793 CB MET B 8 3593 2596 3511 1033 289 -432 C ATOM 794 CG MET B 8 70.935 27.272 43.657 1.00 28.96 C ANISOU 794 CG MET B 8 3882 3078 4044 997 386 -550 C ATOM 795 SD MET B 8 72.192 26.323 44.530 1.00 36.87 S ANISOU 795 SD MET B 8 4852 3950 5209 868 367 -533 S ATOM 796 CE MET B 8 72.530 27.434 45.915 1.00 19.88 C ANISOU 796 CE MET B 8 2805 1620 3129 849 211 -390 C ATOM 797 N GLU B 9 72.275 30.567 40.839 1.00 32.07 N ANISOU 797 N GLU B 9 4522 3562 4100 976 168 -240 N ATOM 798 CA GLU B 9 72.791 31.860 40.374 1.00 37.74 C ANISOU 798 CA GLU B 9 5367 4230 4741 987 60 -87 C ATOM 799 C GLU B 9 71.784 32.604 39.497 1.00 34.53 C ANISOU 799 C GLU B 9 4962 4020 4138 1070 20 -51 C ATOM 800 O GLU B 9 71.634 33.815 39.594 1.00 46.58 O ANISOU 800 O GLU B 9 6632 5479 5588 1166 -94 78 O ATOM 801 CB GLU B 9 74.104 31.663 39.615 1.00 42.40 C ANISOU 801 CB GLU B 9 5898 4803 5409 827 107 -56 C ATOM 802 CG GLU B 9 74.762 32.950 39.147 1.00 39.36 C ANISOU 802 CG GLU B 9 5634 4353 4967 822 -2 113 C ATOM 803 CD GLU B 9 76.256 32.781 38.891 1.00 45.00 C ANISOU 803 CD GLU B 9 6321 4963 5815 675 26 171 C ATOM 804 OE1 GLU B 9 76.965 32.199 39.762 1.00 48.86 O ANISOU 804 OE1 GLU B 9 6805 5284 6473 627 45 156 O ATOM 805 OE2 GLU B 9 76.723 33.237 37.822 1.00 47.26 O ANISOU 805 OE2 GLU B 9 6582 5338 6036 609 30 243 O ATOM 806 N THR B 10 71.084 31.867 38.653 1.00 32.79 N ANISOU 806 N THR B 10 4580 4040 3839 1030 114 -164 N ATOM 807 CA THR B 10 70.035 32.443 37.812 1.00 40.19 C ANISOU 807 CA THR B 10 5490 5194 4586 1102 80 -133 C ATOM 808 C THR B 10 68.888 33.089 38.595 1.00 37.41 C ANISOU 808 C THR B 10 5232 4812 4169 1291 1 -84 C ATOM 809 O THR B 10 68.485 34.220 38.319 1.00 45.84 O ANISOU 809 O THR B 10 6388 5903 5125 1391 -90 42 O ATOM 810 CB THR B 10 69.489 31.389 36.826 1.00 36.85 C ANISOU 810 CB THR B 10 4868 5040 4095 1005 198 -283 C ATOM 811 OG1 THR B 10 70.487 31.135 35.832 1.00 37.06 O ANISOU 811 OG1 THR B 10 4829 5124 4127 848 261 -296 O ATOM 812 CG2 THR B 10 68.195 31.890 36.152 1.00 30.21 C ANISOU 812 CG2 THR B 10 3987 4435 3059 1093 153 -252 C ATOM 813 N MET B 11 68.362 32.371 39.570 1.00 32.73 N ANISOU 813 N MET B 11 4616 4168 3653 1345 42 -178 N ATOM 814 CA MET B 11 67.344 32.930 40.447 1.00 33.49 C ANISOU 814 CA MET B 11 4806 4214 3703 1529 -19 -135 C ATOM 815 C MET B 11 67.838 34.180 41.154 1.00 41.81 C ANISOU 815 C MET B 11 6083 5030 4772 1623 -136 8 C ATOM 816 O MET B 11 67.129 35.201 41.230 1.00 39.57 O ANISOU 816 O MET B 11 5899 4744 4392 1771 -211 103 O ATOM 817 CB MET B 11 66.938 31.875 41.456 1.00 27.85 C ANISOU 817 CB MET B 11 4033 3457 3092 1549 54 -254 C ATOM 818 CG MET B 11 66.494 30.585 40.762 1.00 32.20 C ANISOU 818 CG MET B 11 4364 4226 3646 1441 174 -406 C ATOM 819 SD MET B 11 65.372 29.593 41.756 1.00 52.83 S ANISOU 819 SD MET B 11 6886 6870 6317 1521 243 -517 S ATOM 820 CE MET B 11 64.763 28.457 40.512 1.00 43.06 C ANISOU 820 CE MET B 11 5403 5929 5028 1386 352 -668 C ATOM 821 N MET B 12 69.069 34.096 41.645 1.00 43.87 N ANISOU 821 N MET B 12 6419 5090 5161 1533 -152 24 N ATOM 822 CA MET B 12 69.689 35.200 42.368 1.00 47.08 C ANISOU 822 CA MET B 12 7007 5281 5599 1533 -258 138 C ATOM 823 C MET B 12 69.853 36.378 41.433 1.00 43.98 C ANISOU 823 C MET B 12 6692 4909 5110 1568 -337 273 C ATOM 824 O MET B 12 69.536 37.522 41.789 1.00 45.72 O ANISOU 824 O MET B 12 6979 5092 5300 1557 -390 330 O ATOM 825 CB MET B 12 71.048 34.772 42.907 1.00 55.64 C ANISOU 825 CB MET B 12 8093 6208 6842 1369 -252 130 C ATOM 826 CG MET B 12 71.539 35.520 44.131 1.00 62.02 C ANISOU 826 CG MET B 12 8952 6899 7713 1248 -310 174 C ATOM 827 SD MET B 12 73.140 34.863 44.694 1.00 46.77 S ANISOU 827 SD MET B 12 6962 4839 5970 1067 -296 180 S ATOM 828 CE MET B 12 74.270 35.826 43.726 1.00 52.74 C ANISOU 828 CE MET B 12 7785 5521 6731 1010 -365 307 C ATOM 829 N PHE B 13 70.318 36.107 40.218 1.00 40.98 N ANISOU 829 N PHE B 13 6207 4663 4698 1473 -301 283 N ATOM 830 CA PHE B 13 70.527 37.200 39.252 1.00 43.04 C ANISOU 830 CA PHE B 13 6518 4972 4865 1473 -371 426 C ATOM 831 C PHE B 13 69.207 37.782 38.718 1.00 44.75 C ANISOU 831 C PHE B 13 6712 5371 4922 1611 -394 472 C ATOM 832 O PHE B 13 69.087 38.998 38.518 1.00 46.30 O ANISOU 832 O PHE B 13 7020 5513 5057 1693 -483 615 O ATOM 833 CB PHE B 13 71.488 36.791 38.125 1.00 37.62 C ANISOU 833 CB PHE B 13 5712 4392 4189 1292 -314 426 C ATOM 834 CG PHE B 13 72.956 36.731 38.559 1.00 55.13 C ANISOU 834 CG PHE B 13 7993 6390 6564 1175 -331 463 C ATOM 835 CD1 PHE B 13 73.335 37.080 39.859 1.00 54.35 C ANISOU 835 CD1 PHE B 13 8055 6026 6571 1225 -409 497 C ATOM 836 CD2 PHE B 13 73.958 36.340 37.662 1.00 66.12 C ANISOU 836 CD2 PHE B 13 9282 7847 7992 1013 -269 470 C ATOM 837 CE1 PHE B 13 74.681 37.031 40.256 1.00 57.48 C ANISOU 837 CE1 PHE B 13 8500 6231 7111 1110 -436 544 C ATOM 838 CE2 PHE B 13 75.304 36.289 38.051 1.00 65.80 C ANISOU 838 CE2 PHE B 13 9285 7611 8104 907 -284 520 C ATOM 839 CZ PHE B 13 75.663 36.633 39.351 1.00 62.65 C ANISOU 839 CZ PHE B 13 9037 6952 7813 952 -373 561 C ATOM 840 N THR B 14 68.211 36.923 38.512 1.00 45.33 N ANISOU 840 N THR B 14 6632 5653 4937 1630 -313 356 N ATOM 841 CA THR B 14 66.887 37.398 38.131 1.00 43.70 C ANISOU 841 CA THR B 14 6390 5623 4592 1767 -335 403 C ATOM 842 C THR B 14 66.306 38.336 39.193 1.00 39.96 C ANISOU 842 C THR B 14 6078 4967 4137 1932 -400 469 C ATOM 843 O THR B 14 65.759 39.361 38.854 1.00 43.39 O ANISOU 843 O THR B 14 6528 5438 4520 1959 -431 555 O ATOM 844 CB THR B 14 65.897 36.253 37.917 1.00 41.08 C ANISOU 844 CB THR B 14 5867 5526 4216 1752 -241 258 C ATOM 845 OG1 THR B 14 66.356 35.414 36.860 1.00 40.13 O ANISOU 845 OG1 THR B 14 5588 5588 4072 1570 -165 173 O ATOM 846 CG2 THR B 14 64.539 36.808 37.569 1.00 45.15 C ANISOU 846 CG2 THR B 14 6343 6219 4595 1898 -275 329 C ATOM 847 N PHE B 15 66.447 38.007 40.476 1.00 42.94 N ANISOU 847 N PHE B 15 6506 5174 4636 1888 -367 371 N ATOM 848 CA PHE B 15 65.915 38.899 41.507 1.00 44.73 C ANISOU 848 CA PHE B 15 6811 5286 4900 1879 -373 368 C ATOM 849 C PHE B 15 66.533 40.278 41.390 1.00 51.93 C ANISOU 849 C PHE B 15 7815 6069 5846 1813 -440 469 C ATOM 850 O PHE B 15 65.823 41.282 41.311 1.00 56.92 O ANISOU 850 O PHE B 15 8472 6714 6443 1871 -458 528 O ATOM 851 CB PHE B 15 66.149 38.362 42.913 1.00 44.30 C ANISOU 851 CB PHE B 15 6783 5105 4942 1802 -341 268 C ATOM 852 CG PHE B 15 65.742 39.333 44.020 1.00 46.64 C ANISOU 852 CG PHE B 15 7164 5302 5255 1792 -354 271 C ATOM 853 CD1 PHE B 15 66.703 40.108 44.680 1.00 43.08 C ANISOU 853 CD1 PHE B 15 6798 4689 4880 1684 -402 295 C ATOM 854 CD2 PHE B 15 64.409 39.462 44.402 1.00 41.95 C ANISOU 854 CD2 PHE B 15 6554 4789 4595 1896 -317 252 C ATOM 855 CE1 PHE B 15 66.353 40.998 45.697 1.00 40.07 C ANISOU 855 CE1 PHE B 15 6494 4231 4501 1692 -413 290 C ATOM 856 CE2 PHE B 15 64.047 40.351 45.435 1.00 49.27 C ANISOU 856 CE2 PHE B 15 7567 5626 5530 1900 -324 253 C ATOM 857 CZ PHE B 15 65.021 41.119 46.079 1.00 46.29 C ANISOU 857 CZ PHE B 15 7281 5090 5218 1804 -372 267 C ATOM 858 N HIS B 16 67.860 40.324 41.369 1.00 44.64 N ANISOU 858 N HIS B 16 6932 5024 5004 1691 -475 494 N ATOM 859 CA HIS B 16 68.534 41.599 41.319 1.00 41.32 C ANISOU 859 CA HIS B 16 6581 4485 4636 1618 -537 588 C ATOM 860 C HIS B 16 68.266 42.363 40.029 1.00 49.41 C ANISOU 860 C HIS B 16 7583 5610 5579 1665 -574 717 C ATOM 861 O HIS B 16 68.264 43.584 40.030 1.00 51.50 O ANISOU 861 O HIS B 16 7892 5804 5872 1655 -615 796 O ATOM 862 CB HIS B 16 70.018 41.424 41.615 1.00 41.97 C ANISOU 862 CB HIS B 16 6685 4433 4830 1470 -561 592 C ATOM 863 CG HIS B 16 70.276 41.105 43.055 1.00 53.05 C ANISOU 863 CG HIS B 16 8107 5734 6315 1406 -541 497 C ATOM 864 ND1 HIS B 16 70.058 42.019 44.063 1.00 63.68 N ANISOU 864 ND1 HIS B 16 9514 7000 7680 1402 -558 485 N ATOM 865 CD2 HIS B 16 70.665 39.962 43.660 1.00 45.11 C ANISOU 865 CD2 HIS B 16 7059 4713 5366 1351 -502 415 C ATOM 866 CE1 HIS B 16 70.326 41.455 45.229 1.00 60.60 C ANISOU 866 CE1 HIS B 16 9121 6565 7338 1344 -537 406 C ATOM 867 NE2 HIS B 16 70.691 40.203 45.009 1.00 47.76 N ANISOU 867 NE2 HIS B 16 7425 4978 5745 1307 -503 367 N ATOM 868 N LYS B 17 68.009 41.644 38.940 1.00 53.19 N ANISOU 868 N LYS B 17 7983 6278 5950 1718 -558 741 N ATOM 869 CA LYS B 17 67.753 42.297 37.664 1.00 54.38 C ANISOU 869 CA LYS B 17 8089 6574 5998 1744 -593 872 C ATOM 870 C LYS B 17 66.484 43.161 37.726 1.00 56.74 C ANISOU 870 C LYS B 17 8376 6922 6262 1843 -596 909 C ATOM 871 O LYS B 17 66.454 44.265 37.201 1.00 62.73 O ANISOU 871 O LYS B 17 9148 7667 7020 1834 -643 1029 O ATOM 872 CB LYS B 17 67.655 41.259 36.550 1.00 55.32 C ANISOU 872 CB LYS B 17 8099 6952 5966 1775 -565 876 C ATOM 873 CG LYS B 17 67.341 41.837 35.178 1.00 55.93 C ANISOU 873 CG LYS B 17 8101 7245 5905 1777 -595 1008 C ATOM 874 CD LYS B 17 67.119 40.738 34.143 1.00 48.73 C ANISOU 874 CD LYS B 17 7026 6662 4829 1749 -540 960 C ATOM 875 CE LYS B 17 66.598 41.324 32.842 1.00 61.33 C ANISOU 875 CE LYS B 17 8531 8513 6257 1757 -571 1092 C ATOM 876 NZ LYS B 17 66.601 40.307 31.744 1.00 72.63 N ANISOU 876 NZ LYS B 17 9763 10247 7586 1592 -486 983 N ATOM 877 N PHE B 18 65.449 42.669 38.396 1.00 52.71 N ANISOU 877 N PHE B 18 7839 6458 5731 1937 -544 813 N ATOM 878 CA PHE B 18 64.159 43.360 38.431 1.00 54.58 C ANISOU 878 CA PHE B 18 8053 6758 5928 2043 -534 850 C ATOM 879 C PHE B 18 63.928 44.205 39.680 1.00 59.03 C ANISOU 879 C PHE B 18 8723 7121 6587 2055 -530 817 C ATOM 880 O PHE B 18 62.998 45.005 39.722 1.00 67.17 O ANISOU 880 O PHE B 18 9756 8166 7601 2139 -528 867 O ATOM 881 CB PHE B 18 63.014 42.359 38.263 1.00 55.62 C ANISOU 881 CB PHE B 18 8064 7110 5960 2146 -476 787 C ATOM 882 CG PHE B 18 62.895 41.821 36.876 1.00 61.92 C ANISOU 882 CG PHE B 18 8725 8183 6621 2148 -486 842 C ATOM 883 CD1 PHE B 18 62.246 42.548 35.892 1.00 66.17 C ANISOU 883 CD1 PHE B 18 9191 8877 7076 2176 -516 965 C ATOM 884 CD2 PHE B 18 63.453 40.601 36.543 1.00 65.51 C ANISOU 884 CD2 PHE B 18 9113 8759 7021 2109 -467 772 C ATOM 885 CE1 PHE B 18 62.144 42.057 34.598 1.00 71.31 C ANISOU 885 CE1 PHE B 18 9698 9820 7576 2144 -525 1010 C ATOM 886 CE2 PHE B 18 63.352 40.099 35.255 1.00 66.53 C ANISOU 886 CE2 PHE B 18 9098 9193 6988 2082 -473 807 C ATOM 887 CZ PHE B 18 62.699 40.829 34.282 1.00 69.22 C ANISOU 887 CZ PHE B 18 9362 9704 7236 2087 -501 922 C ATOM 888 N ALA B 19 64.771 44.019 40.689 1.00 56.43 N ANISOU 888 N ALA B 19 8472 6623 6347 1969 -528 735 N ATOM 889 CA ALA B 19 64.647 44.734 41.950 1.00 55.11 C ANISOU 889 CA ALA B 19 8399 6296 6243 1966 -524 692 C ATOM 890 C ALA B 19 65.540 45.975 41.976 1.00 61.75 C ANISOU 890 C ALA B 19 9317 6981 7164 1889 -587 773 C ATOM 891 O ALA B 19 65.251 46.938 42.697 1.00 64.24 O ANISOU 891 O ALA B 19 9707 7191 7510 1920 -593 778 O ATOM 892 CB ALA B 19 65.010 43.818 43.105 1.00 46.14 C ANISOU 892 CB ALA B 19 7286 5099 5145 1908 -488 562 C ATOM 893 N GLY B 20 66.638 45.928 41.219 1.00 57.16 N ANISOU 893 N GLY B 20 8717 6387 6613 1792 -629 837 N ATOM 894 CA GLY B 20 67.590 47.026 41.148 1.00 53.49 C ANISOU 894 CA GLY B 20 8304 5788 6230 1709 -687 926 C ATOM 895 C GLY B 20 68.409 47.224 42.405 1.00 61.63 C ANISOU 895 C GLY B 20 9410 6658 7348 1625 -693 853 C ATOM 896 O GLY B 20 68.396 46.391 43.313 1.00 65.22 O ANISOU 896 O GLY B 20 9873 7105 7802 1608 -657 736 O ATOM 897 N ASP B 21 69.125 48.340 42.467 1.00 65.52 N ANISOU 897 N ASP B 21 9952 7032 7910 1572 -738 928 N ATOM 898 CA ASP B 21 69.927 48.662 43.645 1.00 69.00 C ANISOU 898 CA ASP B 21 10486 7327 8404 1506 -754 862 C ATOM 899 C ASP B 21 69.088 48.813 44.914 1.00 67.81 C ANISOU 899 C ASP B 21 10448 7126 8191 1597 -733 749 C ATOM 900 O ASP B 21 69.593 48.610 46.012 1.00 66.81 O ANISOU 900 O ASP B 21 10408 6921 8056 1555 -744 656 O ATOM 901 CB ASP B 21 70.751 49.924 43.411 1.00 76.30 C ANISOU 901 CB ASP B 21 11482 8129 9378 1468 -813 960 C ATOM 902 CG ASP B 21 71.754 49.759 42.297 1.00 86.52 C ANISOU 902 CG ASP B 21 12673 9468 10731 1366 -829 1074 C ATOM 903 OD1 ASP B 21 71.443 50.144 41.153 1.00 94.29 O ANISOU 903 OD1 ASP B 21 13590 10529 11705 1394 -840 1200 O ATOM 904 OD2 ASP B 21 72.855 49.241 42.561 1.00 92.96 O ANISOU 904 OD2 ASP B 21 13484 10246 11590 1263 -834 1041 O ATOM 905 N LYS B 22 67.811 49.162 44.769 1.00 67.43 N ANISOU 905 N LYS B 22 10395 7131 8093 1722 -704 765 N ATOM 906 CA LYS B 22 66.915 49.211 45.920 1.00 69.78 C ANISOU 906 CA LYS B 22 10786 7403 8322 1819 -668 666 C ATOM 907 C LYS B 22 66.888 47.881 46.706 1.00 72.30 C ANISOU 907 C LYS B 22 11077 7784 8610 1785 -627 546 C ATOM 908 O LYS B 22 66.512 47.849 47.882 1.00 71.69 O ANISOU 908 O LYS B 22 11095 7670 8476 1830 -609 460 O ATOM 909 CB LYS B 22 65.510 49.645 45.493 1.00 75.78 C ANISOU 909 CB LYS B 22 11513 8238 9042 1959 -632 717 C ATOM 910 CG LYS B 22 65.492 51.045 44.886 1.00 92.86 C ANISOU 910 CG LYS B 22 13718 10323 11242 2002 -675 841 C ATOM 911 CD LYS B 22 64.101 51.681 44.902 1.00 96.91 C ANISOU 911 CD LYS B 22 14244 10862 11715 2158 -639 875 C ATOM 912 CE LYS B 22 64.172 53.209 44.759 1.00 93.37 C ANISOU 912 CE LYS B 22 13888 10277 11311 2206 -680 974 C ATOM 913 NZ LYS B 22 62.820 53.837 44.657 1.00 88.77 N ANISOU 913 NZ LYS B 22 13302 9723 10705 2361 -644 1027 N ATOM 914 N GLY B 23 67.287 46.791 46.054 1.00 69.17 N ANISOU 914 N GLY B 23 10548 7481 8250 1707 -611 549 N ATOM 915 CA GLY B 23 67.478 45.524 46.734 1.00 67.26 C ANISOU 915 CA GLY B 23 10269 7281 8005 1656 -578 451 C ATOM 916 C GLY B 23 66.189 44.839 47.136 1.00 59.78 C ANISOU 916 C GLY B 23 9282 6438 6992 1751 -511 388 C ATOM 917 O GLY B 23 66.183 43.974 48.022 1.00 51.74 O ANISOU 917 O GLY B 23 8266 5436 5958 1728 -483 304 O ATOM 918 N TYR B 24 65.100 45.230 46.479 1.00 52.98 N ANISOU 918 N TYR B 24 8386 5653 6090 1861 -489 437 N ATOM 919 CA TYR B 24 63.797 44.618 46.707 1.00 58.40 C ANISOU 919 CA TYR B 24 9030 6456 6706 1968 -423 392 C ATOM 920 C TYR B 24 62.831 44.902 45.544 1.00 57.58 C ANISOU 920 C TYR B 24 8862 6467 6549 2085 -410 470 C ATOM 921 O TYR B 24 63.121 45.693 44.646 1.00 45.06 O ANISOU 921 O TYR B 24 7278 4862 4981 2085 -455 566 O ATOM 922 CB TYR B 24 63.192 45.063 48.048 1.00 63.94 C ANISOU 922 CB TYR B 24 9838 7096 7359 2033 -399 338 C ATOM 923 CG TYR B 24 62.678 46.489 48.052 1.00 63.93 C ANISOU 923 CG TYR B 24 9937 7022 7333 2136 -414 396 C ATOM 924 CD1 TYR B 24 61.385 46.784 47.631 1.00 74.10 C ANISOU 924 CD1 TYR B 24 11173 8396 8587 2261 -372 444 C ATOM 925 CD2 TYR B 24 63.488 47.536 48.471 1.00 58.85 C ANISOU 925 CD2 TYR B 24 9435 6222 6705 2107 -471 408 C ATOM 926 CE1 TYR B 24 60.915 48.086 47.619 1.00 79.24 C ANISOU 926 CE1 TYR B 24 11907 8973 9228 2360 -381 507 C ATOM 927 CE2 TYR B 24 63.034 48.829 48.469 1.00 69.41 C ANISOU 927 CE2 TYR B 24 10863 7481 8031 2201 -482 463 C ATOM 928 CZ TYR B 24 61.744 49.103 48.047 1.00 79.13 C ANISOU 928 CZ TYR B 24 12038 8793 9235 2330 -434 514 C ATOM 929 OH TYR B 24 61.284 50.398 48.043 1.00 82.31 O ANISOU 929 OH TYR B 24 12526 9109 9638 2430 -441 577 O ATOM 930 N LEU B 25 61.684 44.237 45.569 1.00 59.49 N ANISOU 930 N LEU B 25 9037 6841 6728 2179 -351 439 N ATOM 931 CA LEU B 25 60.723 44.352 44.494 1.00 58.32 C ANISOU 931 CA LEU B 25 8802 6837 6521 2289 -336 513 C ATOM 932 C LEU B 25 59.483 45.028 45.013 1.00 54.53 C ANISOU 932 C LEU B 25 8346 6365 6008 2410 -298 533 C ATOM 933 O LEU B 25 59.029 44.725 46.125 1.00 51.06 O ANISOU 933 O LEU B 25 7940 5905 5557 2428 -253 461 O ATOM 934 CB LEU B 25 60.301 42.965 44.026 1.00 52.75 C ANISOU 934 CB LEU B 25 7971 6309 5763 2312 -293 468 C ATOM 935 CG LEU B 25 61.306 41.962 43.478 1.00 51.63 C ANISOU 935 CG LEU B 25 7779 6199 5637 2222 -309 434 C ATOM 936 CD1 LEU B 25 60.581 40.634 43.359 1.00 45.96 C ANISOU 936 CD1 LEU B 25 6940 5656 4868 2272 -250 370 C ATOM 937 CD2 LEU B 25 61.856 42.397 42.128 1.00 50.71 C ANISOU 937 CD2 LEU B 25 7634 6129 5504 2206 -363 534 C ATOM 938 N THR B 26 58.913 45.911 44.201 1.00 54.92 N ANISOU 938 N THR B 26 8370 6453 6042 2493 -314 641 N ATOM 939 CA THR B 26 57.564 46.409 44.464 1.00 60.04 C ANISOU 939 CA THR B 26 9008 7150 6657 2628 -268 676 C ATOM 940 C THR B 26 56.600 45.590 43.637 1.00 60.05 C ANISOU 940 C THR B 26 8853 7377 6587 2702 -232 704 C ATOM 941 O THR B 26 57.021 44.701 42.893 1.00 56.44 O ANISOU 941 O THR B 26 8310 7031 6104 2651 -245 690 O ATOM 942 CB THR B 26 57.396 47.871 44.079 1.00 56.39 C ANISOU 942 CB THR B 26 8595 6605 6227 2685 -306 791 C ATOM 943 OG1 THR B 26 58.083 48.104 42.852 1.00 65.90 O ANISOU 943 OG1 THR B 26 9754 7840 7445 2628 -371 882 O ATOM 944 CG2 THR B 26 57.975 48.781 45.151 1.00 60.03 C ANISOU 944 CG2 THR B 26 9211 6852 6745 2651 -324 756 C ATOM 945 N LYS B 27 55.310 45.879 43.776 1.00 60.15 N ANISOU 945 N LYS B 27 8823 7465 6566 2825 -185 746 N ATOM 946 CA LYS B 27 54.308 45.170 43.003 1.00 59.69 C ANISOU 946 CA LYS B 27 8601 7640 6440 2897 -153 784 C ATOM 947 C LYS B 27 54.696 45.237 41.533 1.00 67.87 C ANISOU 947 C LYS B 27 9546 8794 7448 2868 -213 876 C ATOM 948 O LYS B 27 54.715 44.224 40.836 1.00 74.31 O ANISOU 948 O LYS B 27 10238 9788 8207 2842 -212 856 O ATOM 949 CB LYS B 27 52.925 45.780 43.219 1.00 58.73 C ANISOU 949 CB LYS B 27 8448 7568 6300 3033 -107 853 C ATOM 950 CG LYS B 27 51.837 45.140 42.376 1.00 56.02 C ANISOU 950 CG LYS B 27 7916 7482 5888 3104 -81 911 C ATOM 951 CD LYS B 27 50.567 44.873 43.180 1.00 57.64 C ANISOU 951 CD LYS B 27 8082 7746 6074 3197 -3 895 C ATOM 952 CE LYS B 27 49.590 46.032 43.100 1.00 62.07 C ANISOU 952 CE LYS B 27 8643 8297 6646 3323 13 1015 C ATOM 953 NZ LYS B 27 48.320 45.700 43.824 1.00 59.43 N ANISOU 953 NZ LYS B 27 8254 8037 6289 3415 92 1010 N ATOM 954 N GLU B 28 55.060 46.434 41.090 1.00 64.29 N ANISOU 954 N GLU B 28 9154 8242 7033 2864 -269 976 N ATOM 955 CA GLU B 28 55.351 46.694 39.684 1.00 73.83 C ANISOU 955 CA GLU B 28 10280 9565 8208 2835 -332 1093 C ATOM 956 C GLU B 28 56.584 45.919 39.197 1.00 69.32 C ANISOU 956 C GLU B 28 9701 9014 7624 2709 -369 1044 C ATOM 957 O GLU B 28 56.580 45.365 38.097 1.00 67.03 O ANISOU 957 O GLU B 28 9285 8928 7255 2686 -391 1087 O ATOM 958 CB GLU B 28 55.511 48.210 39.449 1.00 83.89 C ANISOU 958 CB GLU B 28 11635 10698 9541 2851 -386 1216 C ATOM 959 CG GLU B 28 56.668 48.840 40.249 1.00 91.16 C ANISOU 959 CG GLU B 28 12724 11356 10557 2768 -417 1167 C ATOM 960 CD GLU B 28 56.438 50.289 40.648 1.00 94.47 C ANISOU 960 CD GLU B 28 13241 11607 11047 2828 -433 1240 C ATOM 961 OE1 GLU B 28 56.350 51.150 39.743 1.00 96.90 O ANISOU 961 OE1 GLU B 28 13518 11933 11367 2847 -486 1383 O ATOM 962 OE2 GLU B 28 56.366 50.564 41.872 1.00 90.10 O ANISOU 962 OE2 GLU B 28 12796 10906 10532 2853 -396 1157 O ATOM 963 N ASP B 29 57.636 45.889 40.014 1.00 61.98 N ANISOU 963 N ASP B 29 8899 7885 6767 2624 -378 958 N ATOM 964 CA ASP B 29 58.808 45.081 39.708 1.00 55.33 C ANISOU 964 CA ASP B 29 8053 7045 5925 2511 -402 905 C ATOM 965 C ASP B 29 58.352 43.646 39.544 1.00 51.94 C ANISOU 965 C ASP B 29 7499 6814 5422 2534 -352 823 C ATOM 966 O ASP B 29 58.627 43.011 38.515 1.00 51.02 O ANISOU 966 O ASP B 29 7277 6872 5235 2501 -373 845 O ATOM 967 CB ASP B 29 59.830 45.173 40.831 1.00 53.10 C ANISOU 967 CB ASP B 29 7912 6528 5736 2422 -407 815 C ATOM 968 CG ASP B 29 60.324 46.585 41.047 1.00 53.48 C ANISOU 968 CG ASP B 29 8073 6388 5860 2393 -459 888 C ATOM 969 OD1 ASP B 29 60.362 47.342 40.061 1.00 49.03 O ANISOU 969 OD1 ASP B 29 7481 5860 5289 2398 -508 1017 O ATOM 970 OD2 ASP B 29 60.671 46.937 42.200 1.00 58.61 O ANISOU 970 OD2 ASP B 29 8832 6866 6571 2362 -452 821 O ATOM 971 N LEU B 30 57.638 43.151 40.557 1.00 47.28 N ANISOU 971 N LEU B 30 6912 6211 4840 2587 -289 732 N ATOM 972 CA LEU B 30 57.080 41.803 40.527 1.00 46.53 C ANISOU 972 CA LEU B 30 6689 6300 4689 2614 -238 653 C ATOM 973 C LEU B 30 56.287 41.571 39.249 1.00 52.38 C ANISOU 973 C LEU B 30 7251 7324 5326 2668 -249 734 C ATOM 974 O LEU B 30 56.521 40.585 38.555 1.00 62.44 O ANISOU 974 O LEU B 30 8406 8780 6538 2632 -255 698 O ATOM 975 CB LEU B 30 56.204 41.527 41.763 1.00 54.36 C ANISOU 975 CB LEU B 30 7704 7249 5700 2667 -171 581 C ATOM 976 CG LEU B 30 55.572 40.126 41.880 1.00 53.89 C ANISOU 976 CG LEU B 30 7510 7365 5600 2684 -118 500 C ATOM 977 CD1 LEU B 30 56.646 39.032 41.765 1.00 59.56 C ANISOU 977 CD1 LEU B 30 8207 8082 6341 2589 -128 408 C ATOM 978 CD2 LEU B 30 54.796 39.946 43.175 1.00 41.75 C ANISOU 978 CD2 LEU B 30 6012 5762 4088 2712 -59 447 C ATOM 979 N ARG B 31 55.388 42.497 38.910 1.00 50.98 N ANISOU 979 N ARG B 31 7046 7197 5128 2744 -256 846 N ATOM 980 CA ARG B 31 54.549 42.356 37.709 1.00 57.89 C ANISOU 980 CA ARG B 31 7737 8358 5900 2780 -272 937 C ATOM 981 C ARG B 31 55.344 42.284 36.405 1.00 58.28 C ANISOU 981 C ARG B 31 7721 8543 5878 2686 -338 996 C ATOM 982 O ARG B 31 55.045 41.469 35.533 1.00 63.89 O ANISOU 982 O ARG B 31 8261 9532 6481 2654 -345 989 O ATOM 983 CB ARG B 31 53.522 43.481 37.610 1.00 61.37 C ANISOU 983 CB ARG B 31 8171 8799 6347 2874 -273 1063 C ATOM 984 CG ARG B 31 52.494 43.267 36.516 1.00 65.46 C ANISOU 984 CG ARG B 31 8486 9625 6762 2907 -284 1156 C ATOM 985 CD ARG B 31 51.855 44.584 36.113 1.00 75.98 C ANISOU 985 CD ARG B 31 9824 10937 8107 2975 -311 1315 C ATOM 986 NE ARG B 31 51.825 45.544 37.219 1.00 84.93 N ANISOU 986 NE ARG B 31 11131 11790 9349 3043 -285 1312 N ATOM 987 CZ ARG B 31 52.528 46.680 37.248 1.00 88.24 C ANISOU 987 CZ ARG B 31 11687 12003 9836 3022 -331 1372 C ATOM 988 NH1 ARG B 31 53.315 47.005 36.224 1.00 86.52 N ANISOU 988 NH1 ARG B 31 11459 11821 9595 2939 -404 1451 N ATOM 989 NH2 ARG B 31 52.439 47.497 38.299 1.00 82.18 N ANISOU 989 NH2 ARG B 31 11064 11005 9157 3079 -305 1354 N ATOM 990 N VAL B 32 56.340 43.147 36.263 1.00 55.84 N ANISOU 990 N VAL B 32 7542 8054 5622 2627 -388 1053 N ATOM 991 CA VAL B 32 57.221 43.081 35.111 1.00 55.90 C ANISOU 991 CA VAL B 32 7508 8171 5562 2522 -444 1108 C ATOM 992 C VAL B 32 57.940 41.746 35.104 1.00 58.51 C ANISOU 992 C VAL B 32 7793 8585 5853 2451 -425 981 C ATOM 993 O VAL B 32 57.991 41.050 34.079 1.00 64.46 O ANISOU 993 O VAL B 32 8403 9607 6482 2383 -438 977 O ATOM 994 CB VAL B 32 58.275 44.185 35.148 1.00 53.85 C ANISOU 994 CB VAL B 32 7406 7667 5388 2464 -497 1181 C ATOM 995 CG1 VAL B 32 59.249 43.997 34.002 1.00 49.14 C ANISOU 995 CG1 VAL B 32 6768 7188 4715 2345 -545 1232 C ATOM 996 CG2 VAL B 32 57.607 45.532 35.035 1.00 59.61 C ANISOU 996 CG2 VAL B 32 8167 8330 6153 2530 -524 1312 C ATOM 997 N LEU B 33 58.489 41.394 36.262 1.00 52.99 N ANISOU 997 N LEU B 33 7213 7665 5256 2453 -393 871 N ATOM 998 CA LEU B 33 59.293 40.195 36.389 1.00 51.90 C ANISOU 998 CA LEU B 33 7055 7556 5110 2393 -377 755 C ATOM 999 C LEU B 33 58.461 38.989 35.964 1.00 52.90 C ANISOU 999 C LEU B 33 6979 7996 5126 2415 -347 682 C ATOM 1000 O LEU B 33 58.955 38.145 35.228 1.00 47.97 O ANISOU 1000 O LEU B 33 6253 7569 4405 2332 -358 632 O ATOM 1001 CB LEU B 33 59.833 40.052 37.828 1.00 51.46 C ANISOU 1001 CB LEU B 33 7152 7207 5194 2392 -345 653 C ATOM 1002 CG LEU B 33 60.866 38.956 38.180 1.00 46.70 C ANISOU 1002 CG LEU B 33 6566 6544 4634 2328 -331 541 C ATOM 1003 CD1 LEU B 33 61.556 39.231 39.511 1.00 42.15 C ANISOU 1003 CD1 LEU B 33 6161 5650 4203 2277 -318 482 C ATOM 1004 CD2 LEU B 33 60.253 37.568 38.195 1.00 46.34 C ANISOU 1004 CD2 LEU B 33 6358 6709 4540 2373 -284 430 C ATOM 1005 N MET B 34 57.206 38.909 36.416 1.00 49.51 N ANISOU 1005 N MET B 34 6483 7627 4702 2509 -307 669 N ATOM 1006 CA MET B 34 56.359 37.770 36.067 1.00 47.63 C ANISOU 1006 CA MET B 34 6036 7688 4372 2517 -283 595 C ATOM 1007 C MET B 34 56.080 37.790 34.569 1.00 54.08 C ANISOU 1007 C MET B 34 6689 8827 5031 2434 -327 665 C ATOM 1008 O MET B 34 55.990 36.737 33.931 1.00 62.13 O ANISOU 1008 O MET B 34 7543 10120 5943 2336 -324 570 O ATOM 1009 CB MET B 34 55.021 37.804 36.806 1.00 58.99 C ANISOU 1009 CB MET B 34 7438 9127 5850 2625 -230 594 C ATOM 1010 CG MET B 34 55.068 37.993 38.302 1.00 61.56 C ANISOU 1010 CG MET B 34 7934 9149 6306 2674 -177 537 C ATOM 1011 SD MET B 34 54.910 36.503 39.273 1.00 76.85 S ANISOU 1011 SD MET B 34 9809 11088 8301 2660 -109 368 S ATOM 1012 CE MET B 34 53.753 35.527 38.321 1.00 36.83 C ANISOU 1012 CE MET B 34 4443 6430 3123 2667 -104 346 C ATOM 1013 N GLU B 35 55.934 38.991 34.012 1.00 54.32 N ANISOU 1013 N GLU B 35 6767 8822 5052 2443 -363 816 N ATOM 1014 CA GLU B 35 55.629 39.148 32.590 1.00 59.02 C ANISOU 1014 CA GLU B 35 7216 9703 5506 2355 -405 900 C ATOM 1015 C GLU B 35 56.767 38.681 31.708 1.00 61.93 C ANISOU 1015 C GLU B 35 7563 10189 5779 2192 -426 855 C ATOM 1016 O GLU B 35 56.541 37.996 30.713 1.00 68.86 O ANISOU 1016 O GLU B 35 8273 11374 6515 2068 -426 804 O ATOM 1017 CB GLU B 35 55.214 40.590 32.251 1.00 60.35 C ANISOU 1017 CB GLU B 35 7442 9786 5702 2413 -440 1081 C ATOM 1018 CG GLU B 35 53.698 40.774 32.298 1.00 66.73 C ANISOU 1018 CG GLU B 35 8137 10720 6497 2512 -422 1140 C ATOM 1019 CD GLU B 35 53.266 42.210 32.462 1.00 78.06 C ANISOU 1019 CD GLU B 35 9670 11982 8007 2609 -439 1291 C ATOM 1020 OE1 GLU B 35 54.079 43.103 32.141 1.00 83.11 O ANISOU 1020 OE1 GLU B 35 10423 12478 8677 2572 -483 1373 O ATOM 1021 OE2 GLU B 35 52.114 42.440 32.912 1.00 78.08 O ANISOU 1021 OE2 GLU B 35 9632 11995 8040 2719 -406 1327 O ATOM 1022 N LYS B 36 57.991 39.033 32.085 1.00 61.64 N ANISOU 1022 N LYS B 36 7695 9905 5820 2175 -436 861 N ATOM 1023 CA LYS B 36 59.167 38.602 31.332 1.00 61.49 C ANISOU 1023 CA LYS B 36 7671 9976 5717 2021 -441 820 C ATOM 1024 C LYS B 36 59.498 37.122 31.523 1.00 59.65 C ANISOU 1024 C LYS B 36 7351 9785 5528 1868 -347 578 C ATOM 1025 O LYS B 36 59.889 36.452 30.568 1.00 51.93 O ANISOU 1025 O LYS B 36 6266 8994 4471 1681 -307 484 O ATOM 1026 CB LYS B 36 60.384 39.473 31.665 1.00 57.51 C ANISOU 1026 CB LYS B 36 7367 9163 5322 2023 -470 904 C ATOM 1027 CG LYS B 36 60.241 40.913 31.185 1.00 64.86 C ANISOU 1027 CG LYS B 36 8357 10005 6282 2047 -523 1088 C ATOM 1028 CD LYS B 36 59.984 40.973 29.688 1.00 68.73 C ANISOU 1028 CD LYS B 36 8697 10807 6608 1942 -543 1160 C ATOM 1029 CE LYS B 36 59.643 42.385 29.240 1.00 72.50 C ANISOU 1029 CE LYS B 36 9217 11212 7117 1986 -598 1347 C ATOM 1030 NZ LYS B 36 60.511 43.372 29.948 1.00 75.97 N ANISOU 1030 NZ LYS B 36 9860 11293 7713 2020 -629 1413 N ATOM 1031 N GLU B 37 59.327 36.605 32.742 1.00 57.47 N ANISOU 1031 N GLU B 37 7119 9326 5391 1938 -302 472 N ATOM 1032 CA GLU B 37 59.717 35.222 33.035 1.00 52.38 C ANISOU 1032 CA GLU B 37 6402 8666 4836 1790 -202 247 C ATOM 1033 C GLU B 37 58.588 34.169 32.972 1.00 60.72 C ANISOU 1033 C GLU B 37 7269 9946 5855 1759 -150 116 C ATOM 1034 O GLU B 37 58.829 33.017 32.580 1.00 54.53 O ANISOU 1034 O GLU B 37 6371 9268 5080 1582 -72 -63 O ATOM 1035 CB GLU B 37 60.462 35.151 34.364 1.00 36.78 C ANISOU 1035 CB GLU B 37 4583 6347 3046 1841 -176 200 C ATOM 1036 CG GLU B 37 61.696 36.061 34.408 1.00 37.38 C ANISOU 1036 CG GLU B 37 4836 6197 3171 1834 -227 310 C ATOM 1037 CD GLU B 37 62.845 35.539 33.542 1.00 51.19 C ANISOU 1037 CD GLU B 37 6538 7997 4916 1620 -179 237 C ATOM 1038 OE1 GLU B 37 63.098 34.319 33.573 1.00 58.76 O ANISOU 1038 OE1 GLU B 37 7399 8992 5936 1488 -85 57 O ATOM 1039 OE2 GLU B 37 63.487 36.338 32.819 1.00 58.39 O ANISOU 1039 OE2 GLU B 37 7506 8913 5768 1584 -229 363 O ATOM 1040 N PHE B 38 57.363 34.548 33.331 1.00 59.47 N ANISOU 1040 N PHE B 38 7073 9861 5662 1926 -189 204 N ATOM 1041 CA PHE B 38 56.281 33.563 33.338 1.00 54.33 C ANISOU 1041 CA PHE B 38 6240 9413 4989 1897 -145 91 C ATOM 1042 C PHE B 38 54.999 33.968 32.587 1.00 60.93 C ANISOU 1042 C PHE B 38 6935 10549 5666 1963 -210 213 C ATOM 1043 O PHE B 38 53.906 33.923 33.163 1.00 61.26 O ANISOU 1043 O PHE B 38 6914 10634 5728 2096 -212 246 O ATOM 1044 CB PHE B 38 55.905 33.226 34.775 1.00 49.43 C ANISOU 1044 CB PHE B 38 5668 8592 4520 2027 -100 39 C ATOM 1045 CG PHE B 38 57.067 32.937 35.659 1.00 48.01 C ANISOU 1045 CG PHE B 38 5632 8110 4499 1991 -52 -50 C ATOM 1046 CD1 PHE B 38 57.810 31.783 35.494 1.00 49.95 C ANISOU 1046 CD1 PHE B 38 5815 8348 4816 1796 30 -232 C ATOM 1047 CD2 PHE B 38 57.391 33.798 36.690 1.00 39.10 C ANISOU 1047 CD2 PHE B 38 4699 6703 3454 2154 -85 50 C ATOM 1048 CE1 PHE B 38 58.873 31.520 36.319 1.00 52.22 C ANISOU 1048 CE1 PHE B 38 6221 8362 5257 1766 72 -295 C ATOM 1049 CE2 PHE B 38 58.442 33.539 37.513 1.00 29.93 C ANISOU 1049 CE2 PHE B 38 3663 5276 2431 2114 -52 -21 C ATOM 1050 CZ PHE B 38 59.190 32.403 37.333 1.00 46.56 C ANISOU 1050 CZ PHE B 38 5694 7383 4611 1922 24 -185 C ATOM 1051 N PRO B 39 55.119 34.317 31.296 1.00 61.66 N ANISOU 1051 N PRO B 39 6966 10862 5598 1863 -260 283 N ATOM 1052 CA PRO B 39 53.998 34.918 30.540 1.00 59.56 C ANISOU 1052 CA PRO B 39 6582 10875 5174 1936 -341 447 C ATOM 1053 C PRO B 39 52.784 33.990 30.349 1.00 68.44 C ANISOU 1053 C PRO B 39 7493 12268 6245 1885 -324 356 C ATOM 1054 O PRO B 39 51.631 34.423 30.481 1.00 70.78 O ANISOU 1054 O PRO B 39 7717 12633 6543 2010 -350 479 O ATOM 1055 CB PRO B 39 54.627 35.239 29.188 1.00 48.39 C ANISOU 1055 CB PRO B 39 5149 9610 3629 1776 -371 492 C ATOM 1056 CG PRO B 39 55.714 34.177 29.035 1.00 50.68 C ANISOU 1056 CG PRO B 39 5447 9862 3947 1571 -288 269 C ATOM 1057 CD PRO B 39 56.255 33.946 30.426 1.00 54.33 C ANISOU 1057 CD PRO B 39 6045 9972 4625 1652 -229 189 C ATOM 1058 N GLY B 40 53.051 32.726 30.039 1.00 66.84 N ANISOU 1058 N GLY B 40 7194 12157 6046 1676 -253 131 N ATOM 1059 CA GLY B 40 52.007 31.736 29.891 1.00 65.30 C ANISOU 1059 CA GLY B 40 6801 12192 5817 1599 -233 19 C ATOM 1060 C GLY B 40 51.300 31.488 31.202 1.00 70.67 C ANISOU 1060 C GLY B 40 7479 12719 6652 1760 -196 9 C ATOM 1061 O GLY B 40 50.103 31.216 31.221 1.00 75.89 O ANISOU 1061 O GLY B 40 7987 13567 7280 1801 -215 35 O ATOM 1062 N PHE B 41 52.032 31.570 32.307 1.00 67.99 N ANISOU 1062 N PHE B 41 7306 12048 6479 1847 -143 -23 N ATOM 1063 CA PHE B 41 51.383 31.412 33.590 1.00 65.54 C ANISOU 1063 CA PHE B 41 7009 11589 6304 2012 -106 -20 C ATOM 1064 C PHE B 41 50.347 32.503 33.811 1.00 70.01 C ANISOU 1064 C PHE B 41 7574 12208 6820 2247 -176 208 C ATOM 1065 O PHE B 41 49.232 32.214 34.245 1.00 72.96 O ANISOU 1065 O PHE B 41 7829 12676 7216 2338 -164 228 O ATOM 1066 CB PHE B 41 52.354 31.410 34.770 1.00 62.84 C ANISOU 1066 CB PHE B 41 6858 10883 6135 2072 -49 -76 C ATOM 1067 CG PHE B 41 51.646 31.443 36.097 1.00 52.48 C ANISOU 1067 CG PHE B 41 5578 9425 4936 2268 -18 -41 C ATOM 1068 CD1 PHE B 41 50.999 30.303 36.578 1.00 53.72 C ANISOU 1068 CD1 PHE B 41 5596 9645 5171 2224 52 -170 C ATOM 1069 CD2 PHE B 41 51.575 32.609 36.835 1.00 39.38 C ANISOU 1069 CD2 PHE B 41 4082 7577 3302 2494 -54 122 C ATOM 1070 CE1 PHE B 41 50.313 30.315 37.790 1.00 50.47 C ANISOU 1070 CE1 PHE B 41 5281 9036 4860 2309 70 -121 C ATOM 1071 CE2 PHE B 41 50.876 32.630 38.047 1.00 48.47 C ANISOU 1071 CE2 PHE B 41 5330 8539 4545 2569 -4 140 C ATOM 1072 CZ PHE B 41 50.249 31.480 38.521 1.00 47.81 C ANISOU 1072 CZ PHE B 41 5143 8490 4533 2475 48 29 C ATOM 1073 N LEU B 42 50.719 33.752 33.533 1.00 70.86 N ANISOU 1073 N LEU B 42 7811 12244 6870 2350 -243 383 N ATOM 1074 CA LEU B 42 49.800 34.881 33.722 1.00 74.39 C ANISOU 1074 CA LEU B 42 8314 12608 7344 2493 -240 569 C ATOM 1075 C LEU B 42 48.568 34.819 32.785 1.00 77.60 C ANISOU 1075 C LEU B 42 8513 13330 7641 2440 -267 643 C ATOM 1076 O LEU B 42 47.431 35.021 33.212 1.00 75.54 O ANISOU 1076 O LEU B 42 8209 13074 7417 2539 -237 719 O ATOM 1077 CB LEU B 42 50.522 36.217 33.514 1.00 72.10 C ANISOU 1077 CB LEU B 42 8212 12109 7072 2533 -270 703 C ATOM 1078 CG LEU B 42 51.682 36.714 34.376 1.00 61.96 C ANISOU 1078 CG LEU B 42 7169 10471 5902 2587 -255 685 C ATOM 1079 CD1 LEU B 42 52.028 38.159 33.965 1.00 49.98 C ANISOU 1079 CD1 LEU B 42 5787 8805 4396 2610 -294 845 C ATOM 1080 CD2 LEU B 42 51.363 36.637 35.861 1.00 63.71 C ANISOU 1080 CD2 LEU B 42 7505 10445 6258 2704 -185 634 C ATOM 1081 N GLU B 43 48.808 34.547 31.506 1.00 80.17 N ANISOU 1081 N GLU B 43 8720 13911 7828 2268 -318 621 N ATOM 1082 CA GLU B 43 47.736 34.503 30.522 1.00 87.78 C ANISOU 1082 CA GLU B 43 9495 15174 8684 2191 -350 691 C ATOM 1083 C GLU B 43 46.704 33.388 30.768 1.00 87.97 C ANISOU 1083 C GLU B 43 9330 15393 8702 2152 -326 590 C ATOM 1084 O GLU B 43 45.544 33.527 30.383 1.00 87.09 O ANISOU 1084 O GLU B 43 9091 15452 8547 2158 -340 690 O ATOM 1085 CB GLU B 43 48.331 34.437 29.112 1.00 94.01 C ANISOU 1085 CB GLU B 43 10225 16165 9329 1988 -399 670 C ATOM 1086 CG GLU B 43 49.200 35.655 28.795 1.00102.94 C ANISOU 1086 CG GLU B 43 11529 17112 10473 2029 -426 806 C ATOM 1087 CD GLU B 43 49.827 35.612 27.412 1.00111.48 C ANISOU 1087 CD GLU B 43 12563 18378 11418 1827 -462 791 C ATOM 1088 OE1 GLU B 43 49.830 34.529 26.790 1.00116.12 O ANISOU 1088 OE1 GLU B 43 13016 19195 11908 1638 -453 629 O ATOM 1089 OE2 GLU B 43 50.319 36.665 26.946 1.00112.36 O ANISOU 1089 OE2 GLU B 43 12776 18393 11524 1850 -495 933 O ATOM 1090 N ASN B 44 47.128 32.301 31.418 1.00 89.08 N ANISOU 1090 N ASN B 44 9450 15497 8899 2108 -290 397 N ATOM 1091 CA ASN B 44 46.244 31.178 31.779 1.00 89.75 C ANISOU 1091 CA ASN B 44 9365 15716 9020 2059 -256 281 C ATOM 1092 C ASN B 44 45.348 31.494 32.984 1.00 84.19 C ANISOU 1092 C ASN B 44 8729 14814 8447 2250 -198 377 C ATOM 1093 O ASN B 44 44.321 30.848 33.194 1.00 88.14 O ANISOU 1093 O ASN B 44 9104 15418 8967 2222 -176 353 O ATOM 1094 CB ASN B 44 47.055 29.883 32.003 1.00 92.57 C ANISOU 1094 CB ASN B 44 9686 16042 9445 1900 -202 18 C ATOM 1095 CG ASN B 44 46.196 28.708 32.491 1.00 95.65 C ANISOU 1095 CG ASN B 44 9909 16511 9923 1845 -147 -111 C ATOM 1096 OD1 ASN B 44 46.303 28.282 33.643 1.00 91.67 O ANISOU 1096 OD1 ASN B 44 9507 15736 9588 1894 -65 -180 O ATOM 1097 ND2 ASN B 44 45.358 28.173 31.606 1.00 99.15 N ANISOU 1097 ND2 ASN B 44 10168 17254 10252 1690 -185 -140 N ATOM 1098 N GLN B 45 45.750 32.481 33.777 1.00 79.66 N ANISOU 1098 N GLN B 45 8371 13937 7958 2420 -172 477 N ATOM 1099 CA GLN B 45 44.851 33.080 34.746 1.00 84.35 C ANISOU 1099 CA GLN B 45 9058 14351 8641 2583 -122 595 C ATOM 1100 C GLN B 45 44.133 34.174 33.987 1.00101.53 C ANISOU 1100 C GLN B 45 11199 16636 10743 2639 -161 795 C ATOM 1101 O GLN B 45 44.746 35.164 33.584 1.00108.27 O ANISOU 1101 O GLN B 45 12163 17398 11579 2671 -192 885 O ATOM 1102 CB GLN B 45 45.604 33.724 35.915 1.00 72.08 C ANISOU 1102 CB GLN B 45 7766 12415 7206 2706 -74 599 C ATOM 1103 CG GLN B 45 46.967 33.147 36.203 1.00 71.85 C ANISOU 1103 CG GLN B 45 7823 12250 7228 2639 -68 443 C ATOM 1104 CD GLN B 45 46.902 31.757 36.794 1.00 71.07 C ANISOU 1104 CD GLN B 45 7646 12147 7212 2540 -20 266 C ATOM 1105 OE1 GLN B 45 46.168 31.508 37.758 1.00 70.33 O ANISOU 1105 OE1 GLN B 45 7591 11927 7202 2575 27 271 O ATOM 1106 NE2 GLN B 45 47.673 30.835 36.217 1.00 66.03 N ANISOU 1106 NE2 GLN B 45 6898 11627 6563 2389 -24 104 N ATOM 1107 N LYS B 46 42.841 34.005 33.762 1.00103.65 N ANISOU 1107 N LYS B 46 11311 17094 10979 2638 -163 869 N ATOM 1108 CA LYS B 46 42.073 35.107 33.216 1.00102.16 C ANISOU 1108 CA LYS B 46 11096 16969 10752 2713 -189 1072 C ATOM 1109 C LYS B 46 41.690 36.037 34.368 1.00 98.42 C ANISOU 1109 C LYS B 46 10796 16201 10397 2905 -122 1169 C ATOM 1110 O LYS B 46 40.541 36.079 34.807 1.00 97.69 O ANISOU 1110 O LYS B 46 10645 16133 10338 2979 -86 1244 O ATOM 1111 CB LYS B 46 40.866 34.601 32.424 1.00104.59 C ANISOU 1111 CB LYS B 46 11161 17608 10970 2624 -225 1124 C ATOM 1112 CG LYS B 46 41.213 34.129 31.004 1.00107.93 C ANISOU 1112 CG LYS B 46 11435 18330 11245 2418 -303 1072 C ATOM 1113 CD LYS B 46 41.705 35.281 30.125 1.00107.87 C ANISOU 1113 CD LYS B 46 11494 18313 11179 2425 -354 1209 C ATOM 1114 CE LYS B 46 40.951 35.353 28.796 1.00108.05 C ANISOU 1114 CE LYS B 46 11328 18659 11066 2302 -423 1311 C ATOM 1115 NZ LYS B 46 41.483 34.426 27.757 1.00107.13 N ANISOU 1115 NZ LYS B 46 11101 18788 10816 2059 -469 1161 N ATOM 1116 N ASP B 47 42.692 36.754 34.872 1.00 94.06 N ANISOU 1116 N ASP B 47 10461 15368 9909 2970 -106 1156 N ATOM 1117 CA ASP B 47 42.507 37.752 35.919 1.00 92.88 C ANISOU 1117 CA ASP B 47 10502 14925 9864 3123 -48 1226 C ATOM 1118 C ASP B 47 43.579 38.826 35.800 1.00 95.62 C ANISOU 1118 C ASP B 47 11035 15058 10238 3149 -73 1261 C ATOM 1119 O ASP B 47 44.748 38.574 36.070 1.00 91.62 O ANISOU 1119 O ASP B 47 10649 14407 9756 3099 -78 1150 O ATOM 1120 CB ASP B 47 42.555 37.119 37.318 1.00 84.32 C ANISOU 1120 CB ASP B 47 9526 13641 8869 3151 26 1101 C ATOM 1121 CG ASP B 47 42.493 38.162 38.449 1.00 82.17 C ANISOU 1121 CG ASP B 47 9470 13060 8690 3279 84 1148 C ATOM 1122 OD1 ASP B 47 42.178 39.341 38.195 1.00 85.26 O ANISOU 1122 OD1 ASP B 47 9903 13406 9088 3364 77 1281 O ATOM 1123 OD2 ASP B 47 42.740 37.800 39.614 1.00 81.86 O ANISOU 1123 OD2 ASP B 47 9557 12827 8719 3282 136 1047 O ATOM 1124 N PRO B 48 43.171 40.050 35.435 1.00 99.86 N ANISOU 1124 N PRO B 48 11598 15561 10781 3226 -91 1422 N ATOM 1125 CA PRO B 48 44.073 41.207 35.372 1.00 93.23 C ANISOU 1125 CA PRO B 48 10940 14498 9985 3253 -117 1473 C ATOM 1126 C PRO B 48 44.647 41.593 36.736 1.00 82.54 C ANISOU 1126 C PRO B 48 9824 12796 8741 3318 -60 1389 C ATOM 1127 O PRO B 48 45.231 42.671 36.862 1.00 79.10 O ANISOU 1127 O PRO B 48 9547 12150 8359 3350 -77 1435 O ATOM 1128 CB PRO B 48 43.156 42.330 34.870 1.00 92.14 C ANISOU 1128 CB PRO B 48 10749 14413 9846 3340 -134 1665 C ATOM 1129 CG PRO B 48 41.776 41.898 35.255 1.00 94.87 C ANISOU 1129 CG PRO B 48 10962 14894 10192 3405 -82 1698 C ATOM 1130 CD PRO B 48 41.783 40.412 35.095 1.00 97.94 C ANISOU 1130 CD PRO B 48 11209 15487 10516 3293 -87 1571 C ATOM 1131 N LEU B 49 44.467 40.740 37.741 1.00 81.88 N ANISOU 1131 N LEU B 49 9763 12659 8691 3322 1 1269 N ATOM 1132 CA LEU B 49 44.851 41.065 39.113 1.00 80.75 C ANISOU 1132 CA LEU B 49 9833 12210 8637 3366 57 1192 C ATOM 1133 C LEU B 49 45.557 39.898 39.790 1.00 78.16 C ANISOU 1133 C LEU B 49 9550 11822 8327 3281 78 1023 C ATOM 1134 O LEU B 49 45.552 39.786 41.016 1.00 79.38 O ANISOU 1134 O LEU B 49 9827 11795 8540 3296 131 952 O ATOM 1135 CB LEU B 49 43.626 41.491 39.935 1.00 80.10 C ANISOU 1135 CB LEU B 49 9760 12083 8593 3481 124 1254 C ATOM 1136 CG LEU B 49 42.990 42.842 39.585 1.00 84.56 C ANISOU 1136 CG LEU B 49 10330 12624 9173 3588 117 1417 C ATOM 1137 CD1 LEU B 49 41.571 42.940 40.137 1.00 84.42 C ANISOU 1137 CD1 LEU B 49 10242 12662 9171 3695 184 1488 C ATOM 1138 CD2 LEU B 49 43.840 43.997 40.105 1.00 84.97 C ANISOU 1138 CD2 LEU B 49 10609 12383 9293 3614 111 1409 C ATOM 1139 N ALA B 50 46.159 39.026 38.988 1.00 78.88 N ANISOU 1139 N ALA B 50 9533 12073 8364 3183 34 961 N ATOM 1140 CA ALA B 50 46.903 37.885 39.522 1.00 72.29 C ANISOU 1140 CA ALA B 50 8725 11188 7555 3097 49 802 C ATOM 1141 C ALA B 50 48.123 38.355 40.321 1.00 60.04 C ANISOU 1141 C ALA B 50 7409 9326 6077 3075 51 738 C ATOM 1142 O ALA B 50 48.439 37.809 41.385 1.00 58.21 O ANISOU 1142 O ALA B 50 7270 8943 5905 3037 87 636 O ATOM 1143 CB ALA B 50 47.321 36.947 38.392 1.00 73.55 C ANISOU 1143 CB ALA B 50 8709 11601 7637 2997 -2 748 C ATOM 1144 N VAL B 51 48.780 39.395 39.813 1.00 56.41 N ANISOU 1144 N VAL B 51 7041 8773 5618 3084 6 809 N ATOM 1145 CA VAL B 51 49.989 39.933 40.424 1.00 62.63 C ANISOU 1145 CA VAL B 51 8040 9282 6474 3045 -7 760 C ATOM 1146 C VAL B 51 49.617 40.538 41.759 1.00 66.14 C ANISOU 1146 C VAL B 51 8636 9512 6984 3097 43 750 C ATOM 1147 O VAL B 51 50.421 40.575 42.697 1.00 66.09 O ANISOU 1147 O VAL B 51 8785 9293 7033 3042 50 668 O ATOM 1148 CB VAL B 51 50.708 40.968 39.491 1.00 67.56 C ANISOU 1148 CB VAL B 51 8715 9865 7089 3029 -76 857 C ATOM 1149 CG1 VAL B 51 51.792 41.735 40.240 1.00 73.54 C ANISOU 1149 CG1 VAL B 51 9695 10317 7931 2992 -90 824 C ATOM 1150 CG2 VAL B 51 51.306 40.268 38.264 1.00 55.56 C ANISOU 1150 CG2 VAL B 51 7063 8553 5494 2945 -129 849 C ATOM 1151 N ASP B 52 48.370 40.984 41.841 1.00 67.73 N ANISOU 1151 N ASP B 52 8777 9788 7169 3196 77 835 N ATOM 1152 CA ASP B 52 47.817 41.521 43.071 1.00 60.89 C ANISOU 1152 CA ASP B 52 8026 8763 6347 3258 131 833 C ATOM 1153 C ASP B 52 47.491 40.431 44.083 1.00 53.93 C ANISOU 1153 C ASP B 52 7130 7884 5478 3220 182 736 C ATOM 1154 O ASP B 52 47.799 40.575 45.252 1.00 50.44 O ANISOU 1154 O ASP B 52 6830 7258 5076 3196 205 675 O ATOM 1155 CB ASP B 52 46.584 42.341 42.741 1.00 70.31 C ANISOU 1155 CB ASP B 52 9146 10045 7524 3382 151 968 C ATOM 1156 CG ASP B 52 46.901 43.472 41.805 1.00 73.68 C ANISOU 1156 CG ASP B 52 9591 10450 7952 3409 94 1078 C ATOM 1157 OD1 ASP B 52 46.925 43.245 40.579 1.00 74.13 O ANISOU 1157 OD1 ASP B 52 9510 10697 7958 3381 45 1139 O ATOM 1158 OD2 ASP B 52 47.155 44.582 42.304 1.00 74.81 O ANISOU 1158 OD2 ASP B 52 9885 10390 8147 3446 93 1103 O ATOM 1159 N LYS B 53 46.862 39.348 43.632 1.00 63.97 N ANISOU 1159 N LYS B 53 8221 9371 6714 3204 192 726 N ATOM 1160 CA LYS B 53 46.651 38.174 44.476 1.00 68.86 C ANISOU 1160 CA LYS B 53 8808 9994 7361 3140 226 635 C ATOM 1161 C LYS B 53 47.998 37.693 45.010 1.00 69.82 C ANISOU 1161 C LYS B 53 9047 9950 7530 3021 205 520 C ATOM 1162 O LYS B 53 48.178 37.487 46.206 1.00 61.45 O ANISOU 1162 O LYS B 53 8087 8740 6520 2976 228 464 O ATOM 1163 CB LYS B 53 45.982 37.042 43.683 1.00 76.51 C ANISOU 1163 CB LYS B 53 9549 11229 8293 3113 221 631 C ATOM 1164 CG LYS B 53 44.461 37.156 43.524 1.00 78.66 C ANISOU 1164 CG LYS B 53 9683 11669 8536 3204 253 733 C ATOM 1165 CD LYS B 53 43.871 35.828 43.051 1.00 77.01 C ANISOU 1165 CD LYS B 53 9259 11692 8310 3137 246 695 C ATOM 1166 CE LYS B 53 42.358 35.876 42.974 1.00 83.04 C ANISOU 1166 CE LYS B 53 9882 12617 9054 3214 276 799 C ATOM 1167 NZ LYS B 53 41.877 36.886 41.985 1.00 88.77 N ANISOU 1167 NZ LYS B 53 10540 13472 9716 3305 253 939 N ATOM 1168 N ILE B 54 48.957 37.533 44.111 1.00 71.40 N ANISOU 1168 N ILE B 54 9227 10185 7716 2969 157 493 N ATOM 1169 CA ILE B 54 50.278 37.080 44.511 1.00 62.20 C ANISOU 1169 CA ILE B 54 8160 8870 6603 2855 134 395 C ATOM 1170 C ILE B 54 50.994 38.083 45.426 1.00 62.37 C ANISOU 1170 C ILE B 54 8396 8636 6667 2843 127 392 C ATOM 1171 O ILE B 54 51.524 37.694 46.465 1.00 65.56 O ANISOU 1171 O ILE B 54 8882 8901 7124 2760 134 323 O ATOM 1172 CB ILE B 54 51.123 36.748 43.276 1.00 64.26 C ANISOU 1172 CB ILE B 54 8345 9237 6833 2815 87 376 C ATOM 1173 CG1 ILE B 54 50.437 35.630 42.490 1.00 63.73 C ANISOU 1173 CG1 ILE B 54 8048 9444 6722 2802 92 351 C ATOM 1174 CG2 ILE B 54 52.545 36.351 43.675 1.00 58.51 C ANISOU 1174 CG2 ILE B 54 7721 8338 6171 2702 66 285 C ATOM 1175 CD1 ILE B 54 50.908 35.505 41.064 1.00 63.56 C ANISOU 1175 CD1 ILE B 54 7904 9618 6627 2791 45 360 C ATOM 1176 N MET B 55 50.997 39.366 45.067 1.00 60.73 N ANISOU 1176 N MET B 55 8263 8372 6441 2916 108 471 N ATOM 1177 CA MET B 55 51.652 40.371 45.907 1.00 66.12 C ANISOU 1177 CA MET B 55 9136 8823 7165 2898 95 463 C ATOM 1178 C MET B 55 51.117 40.307 47.323 1.00 75.79 C ANISOU 1178 C MET B 55 10427 9964 8406 2906 142 430 C ATOM 1179 O MET B 55 51.853 40.485 48.296 1.00 80.20 O ANISOU 1179 O MET B 55 11115 10360 8999 2838 131 376 O ATOM 1180 CB MET B 55 51.403 41.775 45.374 1.00 63.47 C ANISOU 1180 CB MET B 55 8846 8449 6819 2989 75 566 C ATOM 1181 CG MET B 55 52.189 42.846 46.086 1.00 58.20 C ANISOU 1181 CG MET B 55 8363 7550 6198 2961 49 555 C ATOM 1182 SD MET B 55 53.934 42.474 45.969 1.00 74.40 S ANISOU 1182 SD MET B 55 10487 9487 8295 2806 -14 481 S ATOM 1183 CE MET B 55 54.684 44.005 46.520 1.00 46.08 C ANISOU 1183 CE MET B 55 7088 5662 4759 2789 -58 504 C ATOM 1184 N LYS B 56 49.823 40.032 47.425 1.00 76.43 N ANISOU 1184 N LYS B 56 10408 10174 8460 2987 192 469 N ATOM 1185 CA LYS B 56 49.127 40.117 48.696 1.00 73.49 C ANISOU 1185 CA LYS B 56 10090 9739 8093 3021 241 461 C ATOM 1186 C LYS B 56 49.752 39.225 49.768 1.00 74.88 C ANISOU 1186 C LYS B 56 10310 9830 8310 2900 241 370 C ATOM 1187 O LYS B 56 50.014 39.687 50.875 1.00 73.99 O ANISOU 1187 O LYS B 56 10327 9580 8207 2888 247 346 O ATOM 1188 CB LYS B 56 47.640 39.801 48.522 1.00 68.37 C ANISOU 1188 CB LYS B 56 9300 9260 7416 3117 293 525 C ATOM 1189 CG LYS B 56 46.815 40.099 49.760 1.00 77.58 C ANISOU 1189 CG LYS B 56 10528 10365 8584 3180 349 539 C ATOM 1190 CD LYS B 56 45.355 39.735 49.563 1.00 82.31 C ANISOU 1190 CD LYS B 56 10975 11134 9164 3269 400 608 C ATOM 1191 CE LYS B 56 44.621 39.773 50.892 1.00 91.57 C ANISOU 1191 CE LYS B 56 12201 12248 10343 3314 459 610 C ATOM 1192 NZ LYS B 56 43.303 39.078 50.843 1.00 95.56 N ANISOU 1192 NZ LYS B 56 12545 12916 10847 3364 505 661 N ATOM 1193 N ASP B 57 50.015 37.961 49.447 1.00 73.09 N ANISOU 1193 N ASP B 57 9972 9688 8112 2808 230 322 N ATOM 1194 CA ASP B 57 50.487 37.049 50.480 1.00 74.05 C ANISOU 1194 CA ASP B 57 10108 9735 8292 2692 233 251 C ATOM 1195 C ASP B 57 51.989 36.895 50.503 1.00 70.68 C ANISOU 1195 C ASP B 57 9754 9192 7911 2571 184 192 C ATOM 1196 O ASP B 57 52.515 36.120 51.292 1.00 82.00 O ANISOU 1196 O ASP B 57 11193 10567 9398 2471 183 141 O ATOM 1197 CB ASP B 57 49.835 35.686 50.354 1.00 73.78 C ANISOU 1197 CB ASP B 57 9904 9834 8296 2650 257 230 C ATOM 1198 CG ASP B 57 49.800 35.221 48.954 1.00 72.69 C ANISOU 1198 CG ASP B 57 9630 9849 8141 2653 238 232 C ATOM 1199 OD1 ASP B 57 49.648 36.093 48.073 1.00 66.76 O ANISOU 1199 OD1 ASP B 57 8887 9155 7323 2745 225 290 O ATOM 1200 OD2 ASP B 57 49.937 33.999 48.739 1.00 75.97 O ANISOU 1200 OD2 ASP B 57 9924 10329 8614 2560 237 175 O ATOM 1201 N LEU B 58 52.679 37.619 49.638 1.00 61.00 N ANISOU 1201 N LEU B 58 8578 7936 6663 2585 145 209 N ATOM 1202 CA LEU B 58 54.113 37.763 49.785 1.00 50.15 C ANISOU 1202 CA LEU B 58 7300 6424 5332 2481 98 167 C ATOM 1203 C LEU B 58 54.331 38.882 50.781 1.00 55.13 C ANISOU 1203 C LEU B 58 8092 6904 5950 2501 89 176 C ATOM 1204 O LEU B 58 55.232 38.833 51.613 1.00 64.58 O ANISOU 1204 O LEU B 58 9394 7994 7152 2436 68 135 O ATOM 1205 CB LEU B 58 54.756 38.137 48.459 1.00 47.04 C ANISOU 1205 CB LEU B 58 6896 6054 4923 2490 57 188 C ATOM 1206 CG LEU B 58 54.734 37.069 47.379 1.00 42.41 C ANISOU 1206 CG LEU B 58 6154 5625 4336 2473 59 169 C ATOM 1207 CD1 LEU B 58 55.339 37.643 46.105 1.00 45.42 C ANISOU 1207 CD1 LEU B 58 6539 6033 4684 2502 17 207 C ATOM 1208 CD2 LEU B 58 55.494 35.833 47.841 1.00 33.20 C ANISOU 1208 CD2 LEU B 58 4943 4418 3253 2336 59 91 C ATOM 1209 N ASP B 59 53.486 39.896 50.694 1.00 60.35 N ANISOU 1209 N ASP B 59 8795 7575 6561 2626 110 232 N ATOM 1210 CA ASP B 59 53.605 41.038 51.576 1.00 69.55 C ANISOU 1210 CA ASP B 59 10142 8611 7674 2696 110 240 C ATOM 1211 C ASP B 59 52.885 40.789 52.892 1.00 69.56 C ANISOU 1211 C ASP B 59 10197 8617 7615 2758 164 227 C ATOM 1212 O ASP B 59 51.852 41.400 53.157 1.00 73.02 O ANISOU 1212 O ASP B 59 10660 9077 8006 2887 211 273 O ATOM 1213 CB ASP B 59 53.019 42.268 50.901 1.00 77.25 C ANISOU 1213 CB ASP B 59 11135 9581 8636 2809 113 313 C ATOM 1214 CG ASP B 59 53.718 43.532 51.314 1.00 82.70 C ANISOU 1214 CG ASP B 59 12007 10103 9313 2830 79 315 C ATOM 1215 OD1 ASP B 59 54.881 43.423 51.766 1.00 83.81 O ANISOU 1215 OD1 ASP B 59 12236 10143 9466 2730 35 260 O ATOM 1216 OD2 ASP B 59 53.119 44.624 51.187 1.00 83.57 O ANISOU 1216 OD2 ASP B 59 12169 10180 9406 2945 94 374 O ATOM 1217 N GLN B 60 53.435 39.903 53.716 1.00 71.94 N ANISOU 1217 N GLN B 60 10513 8896 7926 2671 158 175 N ATOM 1218 CA GLN B 60 52.838 39.578 55.011 1.00 72.86 C ANISOU 1218 CA GLN B 60 10677 9017 7989 2721 203 170 C ATOM 1219 C GLN B 60 52.800 40.830 55.871 1.00 70.47 C ANISOU 1219 C GLN B 60 10566 8601 7607 2818 210 178 C ATOM 1220 O GLN B 60 51.745 41.214 56.361 1.00 75.50 O ANISOU 1220 O GLN B 60 11232 9265 8189 2942 267 214 O ATOM 1221 CB GLN B 60 53.632 38.467 55.698 1.00 83.59 C ANISOU 1221 CB GLN B 60 12020 10356 9384 2599 184 120 C ATOM 1222 CG GLN B 60 53.865 37.241 54.794 1.00 98.25 C ANISOU 1222 CG GLN B 60 13694 12299 11338 2489 173 101 C ATOM 1223 CD GLN B 60 54.995 36.331 55.278 1.00106.34 C ANISOU 1223 CD GLN B 60 14711 13268 12425 2354 143 53 C ATOM 1224 OE1 GLN B 60 55.590 35.587 54.486 1.00107.36 O ANISOU 1224 OE1 GLN B 60 14730 13420 12642 2252 123 30 O ATOM 1225 NE2 GLN B 60 55.293 36.385 56.579 1.00104.97 N ANISOU 1225 NE2 GLN B 60 14652 13022 12210 2356 143 41 N ATOM 1226 N CYS B 61 53.958 41.458 56.059 1.00 64.87 N ANISOU 1226 N CYS B 61 9988 7762 6897 2761 151 145 N ATOM 1227 CA CYS B 61 54.012 42.839 56.502 1.00 68.53 C ANISOU 1227 CA CYS B 61 10628 8107 7305 2848 143 154 C ATOM 1228 C CYS B 61 53.498 43.616 55.312 1.00 83.78 C ANISOU 1228 C CYS B 61 12503 10063 9267 2919 151 209 C ATOM 1229 O CYS B 61 53.762 43.237 54.186 1.00102.70 O ANISOU 1229 O CYS B 61 14774 12518 11728 2853 125 221 O ATOM 1230 CB CYS B 61 55.452 43.237 56.757 1.00 67.37 C ANISOU 1230 CB CYS B 61 10604 7824 7171 2747 64 109 C ATOM 1231 SG CYS B 61 56.332 42.084 57.855 1.00 89.95 S ANISOU 1231 SG CYS B 61 13478 10671 10028 2623 36 53 S ATOM 1232 N ARG B 62 52.745 44.682 55.514 1.00 81.37 N ANISOU 1232 N ARG B 62 12280 9716 8921 3056 188 250 N ATOM 1233 CA ARG B 62 52.234 45.395 54.346 1.00 79.06 C ANISOU 1233 CA ARG B 62 11916 9453 8669 3126 193 318 C ATOM 1234 C ARG B 62 53.106 46.607 54.076 1.00 79.90 C ANISOU 1234 C ARG B 62 12151 9406 8802 3114 133 323 C ATOM 1235 O ARG B 62 52.675 47.743 54.262 1.00 87.68 O ANISOU 1235 O ARG B 62 13234 10310 9770 3228 154 361 O ATOM 1236 CB ARG B 62 50.781 45.827 54.538 1.00 77.89 C ANISOU 1236 CB ARG B 62 11747 9364 8485 3291 275 382 C ATOM 1237 CG ARG B 62 49.823 44.709 54.934 1.00 87.09 C ANISOU 1237 CG ARG B 62 12794 10673 9624 3313 337 386 C ATOM 1238 CD ARG B 62 48.490 45.313 55.352 1.00105.36 C ANISOU 1238 CD ARG B 62 15123 13012 11895 3484 420 450 C ATOM 1239 NE ARG B 62 47.721 44.444 56.237 1.00116.64 N ANISOU 1239 NE ARG B 62 16512 14527 13281 3514 481 447 N ATOM 1240 CZ ARG B 62 46.596 44.808 56.845 1.00124.67 C ANISOU 1240 CZ ARG B 62 17550 15564 14253 3658 562 497 C ATOM 1241 NH1 ARG B 62 46.107 46.028 56.666 1.00126.41 N ANISOU 1241 NH1 ARG B 62 17834 15724 14471 3788 593 552 N ATOM 1242 NH2 ARG B 62 45.962 43.952 57.635 1.00126.98 N ANISOU 1242 NH2 ARG B 62 17799 15934 14514 3674 613 498 N ATOM 1243 N ASP B 63 54.336 46.367 53.638 1.00 70.57 N ANISOU 1243 N ASP B 63 10965 8179 7668 2977 61 290 N ATOM 1244 CA ASP B 63 55.250 47.465 53.315 1.00 71.27 C ANISOU 1244 CA ASP B 63 11164 8123 7795 2948 -5 302 C ATOM 1245 C ASP B 63 55.523 47.627 51.806 1.00 61.25 C ANISOU 1245 C ASP B 63 9774 6890 6608 2907 -46 366 C ATOM 1246 O ASP B 63 56.414 48.386 51.419 1.00 58.49 O ANISOU 1246 O ASP B 63 9491 6429 6304 2856 -109 385 O ATOM 1247 CB ASP B 63 56.567 47.309 54.087 1.00 79.88 C ANISOU 1247 CB ASP B 63 12372 9104 8876 2826 -68 228 C ATOM 1248 CG ASP B 63 57.301 46.029 53.738 1.00 91.25 C ANISOU 1248 CG ASP B 63 13692 10620 10358 2683 -95 192 C ATOM 1249 OD1 ASP B 63 56.661 45.092 53.206 1.00 93.59 O ANISOU 1249 OD1 ASP B 63 13829 11060 10671 2684 -54 205 O ATOM 1250 OD2 ASP B 63 58.521 45.958 54.003 1.00 98.86 O ANISOU 1250 OD2 ASP B 63 14719 11499 11344 2569 -158 153 O ATOM 1251 N GLY B 64 54.766 46.910 50.969 1.00 57.90 N ANISOU 1251 N GLY B 64 9172 6625 6201 2924 -13 404 N ATOM 1252 CA GLY B 64 54.917 46.967 49.520 1.00 64.20 C ANISOU 1252 CA GLY B 64 9844 7486 7065 2890 -52 474 C ATOM 1253 C GLY B 64 56.241 46.453 48.967 1.00 74.63 C ANISOU 1253 C GLY B 64 11134 8783 8439 2733 -118 445 C ATOM 1254 O GLY B 64 56.470 46.486 47.752 1.00 76.12 O ANISOU 1254 O GLY B 64 11229 9024 8668 2703 -155 507 O ATOM 1255 N LYS B 65 57.112 45.979 49.859 1.00 76.42 N ANISOU 1255 N LYS B 65 11444 8938 8656 2643 -134 360 N ATOM 1256 CA LYS B 65 58.454 45.520 49.490 1.00 72.61 C ANISOU 1256 CA LYS B 65 10945 8415 8230 2494 -192 332 C ATOM 1257 C LYS B 65 58.510 43.999 49.478 1.00 67.64 C ANISOU 1257 C LYS B 65 10191 7898 7610 2416 -167 278 C ATOM 1258 O LYS B 65 58.058 43.347 50.415 1.00 71.53 O ANISOU 1258 O LYS B 65 10692 8426 8060 2433 -124 227 O ATOM 1259 CB LYS B 65 59.504 46.041 50.488 1.00 70.26 C ANISOU 1259 CB LYS B 65 10819 7954 7924 2436 -238 283 C ATOM 1260 CG LYS B 65 59.512 47.553 50.714 1.00 74.94 C ANISOU 1260 CG LYS B 65 11560 8409 8506 2509 -264 323 C ATOM 1261 CD LYS B 65 60.320 47.914 51.959 1.00 73.83 C ANISOU 1261 CD LYS B 65 11593 8127 8330 2465 -302 258 C ATOM 1262 CE LYS B 65 60.318 49.413 52.219 1.00 76.81 C ANISOU 1262 CE LYS B 65 12127 8359 8699 2540 -328 291 C ATOM 1263 NZ LYS B 65 61.008 49.781 53.494 1.00 74.74 N ANISOU 1263 NZ LYS B 65 12044 7966 8387 2506 -367 224 N ATOM 1264 N VAL B 66 59.064 43.419 48.426 1.00 63.23 N ANISOU 1264 N VAL B 66 9532 7397 7095 2345 -192 293 N ATOM 1265 CA VAL B 66 59.329 41.983 48.451 1.00 57.20 C ANISOU 1265 CA VAL B 66 8678 6715 6342 2272 -172 233 C ATOM 1266 C VAL B 66 60.822 41.735 48.310 1.00 52.81 C ANISOU 1266 C VAL B 66 8143 6070 5852 2135 -224 212 C ATOM 1267 O VAL B 66 61.416 42.079 47.281 1.00 51.81 O ANISOU 1267 O VAL B 66 8008 5933 5744 2117 -265 260 O ATOM 1268 CB VAL B 66 58.587 41.237 47.339 1.00 55.57 C ANISOU 1268 CB VAL B 66 8332 6687 6095 2340 -141 255 C ATOM 1269 CG1 VAL B 66 58.912 39.774 47.399 1.00 46.35 C ANISOU 1269 CG1 VAL B 66 7073 5587 4950 2263 -121 189 C ATOM 1270 CG2 VAL B 66 57.099 41.430 47.478 1.00 63.46 C ANISOU 1270 CG2 VAL B 66 9289 7786 7035 2469 -88 286 C ATOM 1271 N GLY B 67 61.416 41.152 49.351 1.00 50.69 N ANISOU 1271 N GLY B 67 7894 5744 5620 2039 -225 152 N ATOM 1272 CA GLY B 67 62.837 40.845 49.381 1.00 48.53 C ANISOU 1272 CA GLY B 67 7634 5389 5418 1907 -269 135 C ATOM 1273 C GLY B 67 63.141 39.500 48.747 1.00 55.35 C ANISOU 1273 C GLY B 67 8375 6336 6319 1854 -247 109 C ATOM 1274 O GLY B 67 62.229 38.788 48.284 1.00 43.87 O ANISOU 1274 O GLY B 67 6829 5013 4825 1925 -200 98 O ATOM 1275 N PHE B 68 64.422 39.134 48.747 1.00 52.88 N ANISOU 1275 N PHE B 68 8055 5951 6084 1733 -277 100 N ATOM 1276 CA PHE B 68 64.849 37.934 48.051 1.00 45.24 C ANISOU 1276 CA PHE B 68 6983 5043 5162 1688 -256 77 C ATOM 1277 C PHE B 68 64.213 36.682 48.611 1.00 46.17 C ANISOU 1277 C PHE B 68 7002 5243 5296 1684 -195 20 C ATOM 1278 O PHE B 68 63.799 35.791 47.869 1.00 41.45 O ANISOU 1278 O PHE B 68 6301 4754 4695 1718 -156 -5 O ATOM 1279 CB PHE B 68 66.357 37.769 48.096 1.00 37.44 C ANISOU 1279 CB PHE B 68 6003 3952 4272 1555 -292 83 C ATOM 1280 CG PHE B 68 66.837 36.583 47.326 1.00 32.50 C ANISOU 1280 CG PHE B 68 5275 3372 3702 1517 -262 58 C ATOM 1281 CD1 PHE B 68 66.648 36.517 45.951 1.00 37.66 C ANISOU 1281 CD1 PHE B 68 5899 4106 4304 1595 -258 78 C ATOM 1282 CD2 PHE B 68 67.451 35.539 47.955 1.00 28.91 C ANISOU 1282 CD2 PHE B 68 4748 2887 3349 1416 -233 17 C ATOM 1283 CE1 PHE B 68 67.082 35.428 45.225 1.00 40.03 C ANISOU 1283 CE1 PHE B 68 6108 4453 4650 1578 -221 40 C ATOM 1284 CE2 PHE B 68 67.893 34.437 47.233 1.00 28.04 C ANISOU 1284 CE2 PHE B 68 4538 2808 3308 1383 -190 -17 C ATOM 1285 CZ PHE B 68 67.708 34.384 45.869 1.00 35.40 C ANISOU 1285 CZ PHE B 68 5450 3816 4184 1467 -181 -16 C ATOM 1286 N GLN B 69 64.135 36.605 49.927 1.00 41.32 N ANISOU 1286 N GLN B 69 6413 4583 4704 1642 -187 0 N ATOM 1287 CA GLN B 69 63.634 35.387 50.531 1.00 43.32 C ANISOU 1287 CA GLN B 69 6566 4899 4994 1619 -133 -42 C ATOM 1288 C GLN B 69 62.157 35.171 50.170 1.00 43.01 C ANISOU 1288 C GLN B 69 6465 4991 4885 1730 -88 -44 C ATOM 1289 O GLN B 69 61.734 34.080 49.775 1.00 52.62 O ANISOU 1289 O GLN B 69 7555 6302 6138 1724 -44 -76 O ATOM 1290 CB GLN B 69 63.854 35.424 52.040 1.00 32.13 C ANISOU 1290 CB GLN B 69 5250 3415 3543 1609 -146 -55 C ATOM 1291 CG GLN B 69 63.202 34.265 52.742 1.00 43.28 C ANISOU 1291 CG GLN B 69 6577 4892 4977 1608 -92 -83 C ATOM 1292 CD GLN B 69 63.525 34.244 54.212 1.00 59.36 C ANISOU 1292 CD GLN B 69 8707 6864 6984 1594 -107 -89 C ATOM 1293 OE1 GLN B 69 64.326 35.053 54.687 1.00 62.80 O ANISOU 1293 OE1 GLN B 69 9269 7205 7387 1575 -162 -81 O ATOM 1294 NE2 GLN B 69 62.905 33.320 54.947 1.00 55.73 N ANISOU 1294 NE2 GLN B 69 8184 6454 6537 1603 -60 -104 N ATOM 1295 N SER B 70 61.379 36.231 50.289 1.00 40.32 N ANISOU 1295 N SER B 70 6209 4658 4452 1832 -97 -11 N ATOM 1296 CA SER B 70 59.998 36.199 49.858 1.00 44.18 C ANISOU 1296 CA SER B 70 6642 5275 4868 1951 -59 4 C ATOM 1297 C SER B 70 59.902 35.850 48.364 1.00 41.53 C ANISOU 1297 C SER B 70 6216 5052 4510 1997 -55 9 C ATOM 1298 O SER B 70 59.074 35.020 47.963 1.00 39.64 O ANISOU 1298 O SER B 70 5851 4951 4260 2034 -15 -10 O ATOM 1299 CB SER B 70 59.343 37.549 50.138 1.00 52.26 C ANISOU 1299 CB SER B 70 7777 6267 5811 2054 -67 47 C ATOM 1300 OG SER B 70 57.972 37.389 50.475 1.00 67.41 O ANISOU 1300 OG SER B 70 9651 8280 7682 2144 -18 58 O ATOM 1301 N PHE B 71 60.742 36.487 47.546 1.00 35.81 N ANISOU 1301 N PHE B 71 5548 4280 3778 1994 -99 36 N ATOM 1302 CA PHE B 71 60.839 36.137 46.134 1.00 38.45 C ANISOU 1302 CA PHE B 71 5799 4727 4084 2038 -100 42 C ATOM 1303 C PHE B 71 61.044 34.632 45.953 1.00 44.97 C ANISOU 1303 C PHE B 71 6484 5626 4978 1971 -59 -34 C ATOM 1304 O PHE B 71 60.432 34.010 45.080 1.00 49.24 O ANISOU 1304 O PHE B 71 6893 6337 5480 2028 -29 -59 O ATOM 1305 CB PHE B 71 61.981 36.900 45.447 1.00 35.12 C ANISOU 1305 CB PHE B 71 5459 4212 3673 2009 -158 85 C ATOM 1306 CG PHE B 71 62.269 36.409 44.069 1.00 40.18 C ANISOU 1306 CG PHE B 71 6010 4971 4284 2046 -160 90 C ATOM 1307 CD1 PHE B 71 61.376 36.626 43.049 1.00 40.42 C ANISOU 1307 CD1 PHE B 71 5962 5186 4211 2170 -158 135 C ATOM 1308 CD2 PHE B 71 63.418 35.693 43.798 1.00 46.39 C ANISOU 1308 CD2 PHE B 71 6772 5707 5146 1959 -160 50 C ATOM 1309 CE1 PHE B 71 61.634 36.142 41.770 1.00 44.82 C ANISOU 1309 CE1 PHE B 71 6408 5903 4718 2210 -166 140 C ATOM 1310 CE2 PHE B 71 63.672 35.218 42.530 1.00 40.93 C ANISOU 1310 CE2 PHE B 71 5986 5146 4419 2010 -153 43 C ATOM 1311 CZ PHE B 71 62.778 35.439 41.520 1.00 40.17 C ANISOU 1311 CZ PHE B 71 5800 5264 4198 2139 -161 86 C ATOM 1312 N PHE B 72 61.896 34.052 46.793 1.00 35.57 N ANISOU 1312 N PHE B 72 5301 4315 3898 1840 -53 -72 N ATOM 1313 CA PHE B 72 62.198 32.632 46.704 1.00 39.81 C ANISOU 1313 CA PHE B 72 5697 4887 4540 1748 0 -149 C ATOM 1314 C PHE B 72 61.000 31.772 47.085 1.00 40.38 C ANISOU 1314 C PHE B 72 5646 5068 4627 1751 55 -187 C ATOM 1315 O PHE B 72 60.832 30.660 46.586 1.00 48.18 O ANISOU 1315 O PHE B 72 6483 6147 5675 1700 110 -259 O ATOM 1316 CB PHE B 72 63.402 32.262 47.568 1.00 39.74 C ANISOU 1316 CB PHE B 72 5716 4723 4659 1605 -4 -163 C ATOM 1317 CG PHE B 72 64.094 31.042 47.096 1.00 38.13 C ANISOU 1317 CG PHE B 72 5385 4527 4574 1508 52 -236 C ATOM 1318 CD1 PHE B 72 65.045 31.124 46.090 1.00 28.60 C ANISOU 1318 CD1 PHE B 72 4186 3303 3377 1501 46 -247 C ATOM 1319 CD2 PHE B 72 63.771 29.797 47.620 1.00 47.79 C ANISOU 1319 CD2 PHE B 72 6474 5776 5907 1420 122 -299 C ATOM 1320 CE1 PHE B 72 65.652 30.000 45.611 1.00 31.23 C ANISOU 1320 CE1 PHE B 72 4394 3652 3820 1409 121 -333 C ATOM 1321 CE2 PHE B 72 64.395 28.658 47.156 1.00 42.06 C ANISOU 1321 CE2 PHE B 72 5622 5053 5306 1314 194 -379 C ATOM 1322 CZ PHE B 72 65.336 28.760 46.148 1.00 35.82 C ANISOU 1322 CZ PHE B 72 4838 4254 4518 1307 199 -403 C ATOM 1323 N SER B 73 60.157 32.281 47.970 1.00 38.88 N ANISOU 1323 N SER B 73 5517 4867 4390 1801 47 -145 N ATOM 1324 CA SER B 73 58.948 31.541 48.317 1.00 45.62 C ANISOU 1324 CA SER B 73 6260 5820 5255 1814 94 -166 C ATOM 1325 C SER B 73 57.922 31.546 47.167 1.00 50.70 C ANISOU 1325 C SER B 73 6806 6654 5805 1922 106 -162 C ATOM 1326 O SER B 73 57.104 30.632 47.049 1.00 55.61 O ANISOU 1326 O SER B 73 7286 7386 6458 1901 149 -203 O ATOM 1327 CB SER B 73 58.339 32.047 49.628 1.00 51.92 C ANISOU 1327 CB SER B 73 7143 6556 6027 1841 92 -125 C ATOM 1328 OG SER B 73 57.843 33.367 49.484 1.00 65.19 O ANISOU 1328 OG SER B 73 8937 8246 7585 1966 64 -64 O ATOM 1329 N LEU B 74 57.974 32.555 46.308 1.00 46.11 N ANISOU 1329 N LEU B 74 6289 6117 5112 2031 67 -112 N ATOM 1330 CA LEU B 74 57.137 32.545 45.111 1.00 49.61 C ANISOU 1330 CA LEU B 74 6616 6776 5459 2133 72 -102 C ATOM 1331 C LEU B 74 57.590 31.470 44.125 1.00 48.73 C ANISOU 1331 C LEU B 74 6342 6785 5387 2056 102 -198 C ATOM 1332 O LEU B 74 56.787 30.661 43.636 1.00 50.73 O ANISOU 1332 O LEU B 74 6425 7218 5633 2036 138 -252 O ATOM 1333 CB LEU B 74 57.192 33.901 44.430 1.00 55.17 C ANISOU 1333 CB LEU B 74 7421 7495 6048 2257 26 -14 C ATOM 1334 CG LEU B 74 56.569 33.962 43.042 1.00 53.42 C ANISOU 1334 CG LEU B 74 7061 7521 5716 2361 19 14 C ATOM 1335 CD1 LEU B 74 55.067 33.735 43.123 1.00 50.34 C ANISOU 1335 CD1 LEU B 74 6557 7292 5278 2422 49 36 C ATOM 1336 CD2 LEU B 74 56.877 35.304 42.412 1.00 54.25 C ANISOU 1336 CD2 LEU B 74 7272 7597 5746 2446 -32 119 C ATOM 1337 N ILE B 75 58.886 31.465 43.835 1.00 34.99 N ANISOU 1337 N ILE B 75 4652 4950 3694 1995 93 -228 N ATOM 1338 CA ILE B 75 59.447 30.471 42.951 1.00 27.09 C ANISOU 1338 CA ILE B 75 3505 4050 2739 1894 145 -340 C ATOM 1339 C ILE B 75 59.242 29.073 43.521 1.00 35.54 C ANISOU 1339 C ILE B 75 4456 5094 3952 1732 216 -434 C ATOM 1340 O ILE B 75 58.932 28.127 42.787 1.00 39.52 O ANISOU 1340 O ILE B 75 4796 5751 4470 1645 273 -530 O ATOM 1341 CB ILE B 75 60.930 30.733 42.747 1.00 33.31 C ANISOU 1341 CB ILE B 75 4388 4699 3571 1852 133 -346 C ATOM 1342 CG1 ILE B 75 61.105 32.093 42.076 1.00 44.89 C ANISOU 1342 CG1 ILE B 75 5966 6184 4905 2012 60 -240 C ATOM 1343 CG2 ILE B 75 61.535 29.631 41.916 1.00 22.81 C ANISOU 1343 CG2 ILE B 75 2905 3466 2295 1712 214 -481 C ATOM 1344 CD1 ILE B 75 60.102 32.344 40.937 1.00 47.00 C ANISOU 1344 CD1 ILE B 75 6100 6739 5017 2138 58 -219 C ATOM 1345 N ALA B 76 59.408 28.949 44.834 1.00 33.64 N ANISOU 1345 N ALA B 76 4298 4668 3817 1679 215 -403 N ATOM 1346 CA ALA B 76 59.190 27.677 45.503 1.00 38.75 C ANISOU 1346 CA ALA B 76 4844 5272 4609 1541 284 -466 C ATOM 1347 C ALA B 76 57.764 27.175 45.269 1.00 40.00 C ANISOU 1347 C ALA B 76 4876 5594 4729 1567 310 -486 C ATOM 1348 O ALA B 76 57.568 26.036 44.884 1.00 43.38 O ANISOU 1348 O ALA B 76 5167 6084 5230 1455 377 -571 O ATOM 1349 CB ALA B 76 59.489 27.792 47.010 1.00 32.21 C ANISOU 1349 CB ALA B 76 4116 4256 3865 1505 269 -414 C ATOM 1350 N GLY B 77 56.771 28.034 45.484 1.00 38.51 N ANISOU 1350 N GLY B 77 4737 5470 4425 1710 262 -402 N ATOM 1351 CA GLY B 77 55.380 27.641 45.324 1.00 43.72 C ANISOU 1351 CA GLY B 77 5278 6288 5047 1746 281 -404 C ATOM 1352 C GLY B 77 55.047 27.153 43.922 1.00 54.73 C ANISOU 1352 C GLY B 77 6508 7912 6377 1723 297 -477 C ATOM 1353 O GLY B 77 54.424 26.104 43.763 1.00 60.23 O ANISOU 1353 O GLY B 77 7066 8690 7129 1632 345 -544 O ATOM 1354 N LEU B 78 55.466 27.909 42.907 1.00 48.28 N ANISOU 1354 N LEU B 78 5702 7205 5437 1798 259 -463 N ATOM 1355 CA LEU B 78 55.304 27.484 41.517 1.00 47.80 C ANISOU 1355 CA LEU B 78 5474 7395 5292 1747 274 -545 C ATOM 1356 C LEU B 78 55.976 26.155 41.209 1.00 54.09 C ANISOU 1356 C LEU B 78 6180 8159 6212 1531 349 -689 C ATOM 1357 O LEU B 78 55.362 25.249 40.637 1.00 61.63 O ANISOU 1357 O LEU B 78 6985 9265 7167 1428 382 -773 O ATOM 1358 CB LEU B 78 55.860 28.549 40.570 1.00 40.00 C ANISOU 1358 CB LEU B 78 4526 6515 4156 1854 230 -499 C ATOM 1359 CG LEU B 78 55.103 29.872 40.667 1.00 42.01 C ANISOU 1359 CG LEU B 78 4860 6819 4282 2076 164 -341 C ATOM 1360 CD1 LEU B 78 55.785 30.973 39.869 1.00 32.95 C ANISOU 1360 CD1 LEU B 78 3778 5722 3018 2194 120 -268 C ATOM 1361 CD2 LEU B 78 53.654 29.656 40.207 1.00 45.35 C ANISOU 1361 CD2 LEU B 78 5114 7500 4616 2116 160 -319 C ATOM 1362 N THR B 79 57.248 26.047 41.567 1.00 42.60 N ANISOU 1362 N THR B 79 4821 6504 4863 1458 375 -710 N ATOM 1363 CA THR B 79 58.003 24.862 41.220 1.00 38.26 C ANISOU 1363 CA THR B 79 4204 5905 4430 1262 456 -826 C ATOM 1364 C THR B 79 57.409 23.654 41.909 1.00 45.22 C ANISOU 1364 C THR B 79 5027 6709 5448 1166 514 -851 C ATOM 1365 O THR B 79 57.389 22.560 41.357 1.00 45.43 O ANISOU 1365 O THR B 79 4954 6787 5520 1031 570 -941 O ATOM 1366 CB THR B 79 59.476 25.021 41.620 1.00 29.82 C ANISOU 1366 CB THR B 79 3252 4621 3458 1220 476 -815 C ATOM 1367 OG1 THR B 79 59.991 26.201 41.007 1.00 36.10 O ANISOU 1367 OG1 THR B 79 4116 5481 4120 1331 417 -776 O ATOM 1368 CG2 THR B 79 60.310 23.826 41.169 1.00 26.02 C ANISOU 1368 CG2 THR B 79 2708 4091 3088 1033 567 -912 C ATOM 1369 N ILE B 80 56.903 23.858 43.117 1.00 49.91 N ANISOU 1369 N ILE B 80 5687 7180 6097 1238 500 -767 N ATOM 1370 CA ILE B 80 56.290 22.759 43.843 1.00 51.52 C ANISOU 1370 CA ILE B 80 5840 7313 6423 1164 560 -771 C ATOM 1371 C ILE B 80 55.007 22.298 43.145 1.00 46.95 C ANISOU 1371 C ILE B 80 5115 6954 5770 1163 554 -818 C ATOM 1372 O ILE B 80 54.823 21.099 42.929 1.00 43.38 O ANISOU 1372 O ILE B 80 4577 6516 5389 1047 610 -882 O ATOM 1373 CB ILE B 80 56.073 23.109 45.325 1.00 52.11 C ANISOU 1373 CB ILE B 80 6012 7221 6568 1222 548 -679 C ATOM 1374 CG1 ILE B 80 57.436 23.080 46.031 1.00 55.26 C ANISOU 1374 CG1 ILE B 80 6512 7405 7079 1155 574 -658 C ATOM 1375 CG2 ILE B 80 55.104 22.119 45.975 1.00 48.06 C ANISOU 1375 CG2 ILE B 80 5426 6690 6144 1180 604 -672 C ATOM 1376 CD1 ILE B 80 57.580 24.031 47.206 1.00 50.62 C ANISOU 1376 CD1 ILE B 80 6046 6703 6486 1231 507 -582 C ATOM 1377 N ALA B 81 54.154 23.247 42.756 1.00 31.37 N ANISOU 1377 N ALA B 81 3115 5161 3642 1298 483 -775 N ATOM 1378 CA ALA B 81 52.936 22.918 42.026 1.00 44.11 C ANISOU 1378 CA ALA B 81 4575 7018 5166 1302 468 -810 C ATOM 1379 C ALA B 81 53.237 22.243 40.681 1.00 54.43 C ANISOU 1379 C ALA B 81 5759 8497 6425 1159 486 -943 C ATOM 1380 O ALA B 81 52.521 21.338 40.272 1.00 60.45 O ANISOU 1380 O ALA B 81 6393 9382 7194 1068 504 -1018 O ATOM 1381 CB ALA B 81 52.079 24.161 41.829 1.00 54.05 C ANISOU 1381 CB ALA B 81 5836 8444 6256 1490 391 -707 C ATOM 1382 N CYS B 82 54.295 22.676 40.002 1.00 52.40 N ANISOU 1382 N CYS B 82 5544 8249 6117 1131 479 -978 N ATOM 1383 CA CYS B 82 54.710 22.028 38.765 1.00 48.38 C ANISOU 1383 CA CYS B 82 4936 7881 5566 970 504 -1112 C ATOM 1384 C CYS B 82 55.135 20.592 39.010 1.00 53.94 C ANISOU 1384 C CYS B 82 5628 8425 6443 800 579 -1200 C ATOM 1385 O CYS B 82 54.837 19.691 38.224 1.00 53.25 O ANISOU 1385 O CYS B 82 5426 8464 6341 663 596 -1321 O ATOM 1386 CB CYS B 82 55.879 22.764 38.128 1.00 42.88 C ANISOU 1386 CB CYS B 82 4306 7186 4801 969 498 -1117 C ATOM 1387 SG CYS B 82 55.491 24.349 37.406 1.00 56.56 S ANISOU 1387 SG CYS B 82 6031 9172 6287 1151 412 -1019 S ATOM 1388 N ASN B 83 55.865 20.381 40.091 1.00 59.17 N ANISOU 1388 N ASN B 83 6411 8816 7257 811 619 -1135 N ATOM 1389 CA ASN B 83 56.326 19.040 40.409 1.00 56.52 C ANISOU 1389 CA ASN B 83 6072 8330 7071 681 681 -1179 C ATOM 1390 C ASN B 83 55.136 18.120 40.717 1.00 62.68 C ANISOU 1390 C ASN B 83 6760 9162 7893 655 692 -1200 C ATOM 1391 O ASN B 83 55.082 16.987 40.231 1.00 66.72 O ANISOU 1391 O ASN B 83 7191 9709 8450 519 717 -1311 O ATOM 1392 CB ASN B 83 57.323 19.059 41.573 1.00 36.46 C ANISOU 1392 CB ASN B 83 3674 5525 4654 716 713 -1071 C ATOM 1393 CG ASN B 83 57.845 17.682 41.907 1.00 43.76 C ANISOU 1393 CG ASN B 83 4592 6329 5705 604 756 -1095 C ATOM 1394 OD1 ASN B 83 58.618 17.089 41.145 1.00 50.94 O ANISOU 1394 OD1 ASN B 83 5469 7245 6642 482 772 -1193 O ATOM 1395 ND2 ASN B 83 57.432 17.161 43.050 1.00 44.52 N ANISOU 1395 ND2 ASN B 83 4706 6332 5876 641 768 -1025 N ATOM 1396 N ASP B 84 54.185 18.610 41.514 1.00 52.96 N ANISOU 1396 N ASP B 84 5541 7933 6650 780 673 -1101 N ATOM 1397 CA ASP B 84 53.012 17.817 41.843 1.00 56.56 C ANISOU 1397 CA ASP B 84 5906 8441 7145 767 686 -1106 C ATOM 1398 C ASP B 84 52.296 17.420 40.546 1.00 65.99 C ANISOU 1398 C ASP B 84 6937 9901 8234 675 658 -1246 C ATOM 1399 O ASP B 84 52.045 16.234 40.314 1.00 63.62 O ANISOU 1399 O ASP B 84 6559 9619 7997 551 687 -1342 O ATOM 1400 CB ASP B 84 52.079 18.580 42.778 1.00 50.96 C ANISOU 1400 CB ASP B 84 5227 7714 6421 918 666 -979 C ATOM 1401 CG ASP B 84 52.678 18.797 44.154 1.00 58.58 C ANISOU 1401 CG ASP B 84 6341 8418 7500 972 703 -861 C ATOM 1402 OD1 ASP B 84 53.442 17.925 44.621 1.00 63.09 O ANISOU 1402 OD1 ASP B 84 6952 8846 8172 901 752 -860 O ATOM 1403 OD2 ASP B 84 52.380 19.842 44.773 1.00 64.43 O ANISOU 1403 OD2 ASP B 84 7149 9127 8205 1088 668 -782 O ATOM 1404 N TYR B 85 52.008 18.412 39.701 1.00 63.12 N ANISOU 1404 N TYR B 85 6526 9755 7702 732 600 -1256 N ATOM 1405 CA TYR B 85 51.458 18.160 38.378 1.00 63.70 C ANISOU 1405 CA TYR B 85 6446 10118 7640 633 569 -1383 C ATOM 1406 C TYR B 85 52.239 17.052 37.685 1.00 67.28 C ANISOU 1406 C TYR B 85 6876 10532 8157 430 616 -1546 C ATOM 1407 O TYR B 85 51.673 16.040 37.288 1.00 74.73 O ANISOU 1407 O TYR B 85 7714 11563 9118 306 630 -1664 O ATOM 1408 CB TYR B 85 51.489 19.428 37.517 1.00 60.72 C ANISOU 1408 CB TYR B 85 6047 9962 7061 714 506 -1350 C ATOM 1409 CG TYR B 85 50.749 19.258 36.216 1.00 65.27 C ANISOU 1409 CG TYR B 85 6451 10884 7465 620 467 -1451 C ATOM 1410 CD1 TYR B 85 51.315 18.560 35.157 1.00 74.87 C ANISOU 1410 CD1 TYR B 85 7614 12184 8650 422 492 -1619 C ATOM 1411 CD2 TYR B 85 49.474 19.774 36.047 1.00 71.18 C ANISOU 1411 CD2 TYR B 85 7088 11879 8077 721 407 -1372 C ATOM 1412 CE1 TYR B 85 50.633 18.378 33.958 1.00 80.68 C ANISOU 1412 CE1 TYR B 85 8192 13252 9211 311 457 -1720 C ATOM 1413 CE2 TYR B 85 48.781 19.603 34.848 1.00 79.16 C ANISOU 1413 CE2 TYR B 85 7929 13233 8914 619 367 -1452 C ATOM 1414 CZ TYR B 85 49.369 18.901 33.811 1.00 84.58 C ANISOU 1414 CZ TYR B 85 8567 14007 9560 407 391 -1633 C ATOM 1415 OH TYR B 85 48.701 18.717 32.627 1.00 89.05 O ANISOU 1415 OH TYR B 85 8970 14924 9940 285 352 -1721 O ATOM 1416 N PHE B 86 53.543 17.266 37.558 1.00 65.15 N ANISOU 1416 N PHE B 86 6707 10125 7924 400 640 -1551 N ATOM 1417 CA PHE B 86 54.469 16.351 36.901 1.00 69.19 C ANISOU 1417 CA PHE B 86 7215 10573 8500 222 686 -1688 C ATOM 1418 C PHE B 86 54.376 14.918 37.414 1.00 80.69 C ANISOU 1418 C PHE B 86 8656 11880 10122 122 734 -1751 C ATOM 1419 O PHE B 86 54.449 13.976 36.634 1.00 88.21 O ANISOU 1419 O PHE B 86 9539 12889 11090 -42 760 -1915 O ATOM 1420 CB PHE B 86 55.894 16.882 37.109 1.00 68.57 C ANISOU 1420 CB PHE B 86 7271 10311 8473 251 708 -1622 C ATOM 1421 CG PHE B 86 56.971 16.041 36.495 1.00 68.01 C ANISOU 1421 CG PHE B 86 7209 10154 8478 87 759 -1736 C ATOM 1422 CD1 PHE B 86 57.273 16.150 35.152 1.00 71.90 C ANISOU 1422 CD1 PHE B 86 7644 10820 8854 -23 762 -1855 C ATOM 1423 CD2 PHE B 86 57.713 15.170 37.271 1.00 74.26 C ANISOU 1423 CD2 PHE B 86 8067 10700 9450 47 803 -1714 C ATOM 1424 CE1 PHE B 86 58.281 15.387 34.591 1.00 74.22 C ANISOU 1424 CE1 PHE B 86 7951 11025 9226 -170 818 -1957 C ATOM 1425 CE2 PHE B 86 58.730 14.399 36.713 1.00 76.37 C ANISOU 1425 CE2 PHE B 86 8339 10885 9794 -96 850 -1814 C ATOM 1426 CZ PHE B 86 59.012 14.510 35.374 1.00 75.63 C ANISOU 1426 CZ PHE B 86 8192 10947 9599 -203 862 -1938 C ATOM 1427 N VAL B 87 54.232 14.754 38.726 1.00 84.48 N ANISOU 1427 N VAL B 87 9205 12173 10720 219 747 -1621 N ATOM 1428 CA VAL B 87 54.211 13.422 39.329 1.00 88.81 C ANISOU 1428 CA VAL B 87 9748 12574 11421 141 789 -1652 C ATOM 1429 C VAL B 87 52.906 12.701 39.022 1.00 92.35 C ANISOU 1429 C VAL B 87 10062 13179 11848 81 786 -1749 C ATOM 1430 O VAL B 87 52.895 11.513 38.693 1.00 94.98 O ANISOU 1430 O VAL B 87 10341 13491 12255 -62 819 -1890 O ATOM 1431 CB VAL B 87 54.440 13.484 40.859 1.00 88.18 C ANISOU 1431 CB VAL B 87 9780 12278 11447 263 802 -1467 C ATOM 1432 CG1 VAL B 87 53.928 12.215 41.546 1.00 84.33 C ANISOU 1432 CG1 VAL B 87 9244 11718 11078 210 830 -1496 C ATOM 1433 CG2 VAL B 87 55.924 13.725 41.165 1.00 84.55 C ANISOU 1433 CG2 VAL B 87 9436 11648 11042 263 812 -1417 C ATOM 1434 N VAL B 88 51.810 13.442 39.118 1.00 91.47 N ANISOU 1434 N VAL B 88 9895 13225 11636 191 747 -1676 N ATOM 1435 CA VAL B 88 50.480 12.909 38.866 1.00 89.14 C ANISOU 1435 CA VAL B 88 9461 13104 11306 152 736 -1741 C ATOM 1436 C VAL B 88 50.311 12.501 37.408 1.00 87.54 C ANISOU 1436 C VAL B 88 9138 13132 10990 -18 724 -1953 C ATOM 1437 O VAL B 88 49.589 11.551 37.104 1.00 87.52 O ANISOU 1437 O VAL B 88 9033 13215 11005 -127 739 -2073 O ATOM 1438 CB VAL B 88 49.405 13.951 39.224 1.00 87.42 C ANISOU 1438 CB VAL B 88 9206 13020 10989 319 689 -1598 C ATOM 1439 CG1 VAL B 88 47.998 13.393 38.992 1.00 90.55 C ANISOU 1439 CG1 VAL B 88 9447 13605 11352 282 676 -1643 C ATOM 1440 CG2 VAL B 88 49.580 14.401 40.662 1.00 80.45 C ANISOU 1440 CG2 VAL B 88 8454 11907 10208 476 711 -1403 C ATOM 1441 N HIS B 89 50.989 13.210 36.509 1.00 82.00 N ANISOU 1441 N HIS B 89 8452 12536 10168 -46 701 -1999 N ATOM 1442 CA HIS B 89 50.803 12.996 35.077 1.00 73.79 C ANISOU 1442 CA HIS B 89 7299 11759 8980 -206 686 -2186 C ATOM 1443 C HIS B 89 52.080 12.540 34.359 1.00 78.07 C ANISOU 1443 C HIS B 89 7893 12208 9560 -356 732 -2323 C ATOM 1444 O HIS B 89 52.302 11.346 34.144 1.00 79.48 O ANISOU 1444 O HIS B 89 8056 12302 9841 -508 785 -2478 O ATOM 1445 CB HIS B 89 50.259 14.268 34.408 1.00 68.45 C ANISOU 1445 CB HIS B 89 6553 11379 8074 -120 612 -2119 C ATOM 1446 CG HIS B 89 48.971 14.763 34.991 1.00 72.85 C ANISOU 1446 CG HIS B 89 7045 12053 8583 29 564 -1979 C ATOM 1447 ND1 HIS B 89 48.904 15.418 36.202 1.00 76.26 N ANISOU 1447 ND1 HIS B 89 7572 12303 9100 224 561 -1784 N ATOM 1448 CD2 HIS B 89 47.701 14.704 34.528 1.00 83.14 C ANISOU 1448 CD2 HIS B 89 8195 13634 9761 9 520 -1997 C ATOM 1449 CE1 HIS B 89 47.649 15.745 36.459 1.00 79.25 C ANISOU 1449 CE1 HIS B 89 7863 12832 9418 324 520 -1688 C ATOM 1450 NE2 HIS B 89 46.897 15.318 35.461 1.00 83.71 N ANISOU 1450 NE2 HIS B 89 8271 13677 9858 199 492 -1805 N ATOM 1451 N MET B 90 52.926 13.507 34.018 1.00 82.75 N ANISOU 1451 N MET B 90 8553 12809 10079 -305 717 -2258 N ATOM 1452 CA MET B 90 53.975 13.345 33.000 1.00 82.70 C ANISOU 1452 CA MET B 90 8564 12815 10044 -448 750 -2379 C ATOM 1453 C MET B 90 54.961 12.162 33.099 1.00 90.95 C ANISOU 1453 C MET B 90 9667 13608 11282 -578 828 -2482 C ATOM 1454 O MET B 90 55.797 11.987 32.206 1.00 91.13 O ANISOU 1454 O MET B 90 9694 13645 11285 -700 864 -2584 O ATOM 1455 CB MET B 90 54.712 14.678 32.781 1.00 79.32 C ANISOU 1455 CB MET B 90 8210 12414 9515 -341 723 -2252 C ATOM 1456 CG MET B 90 53.756 15.831 32.463 1.00 83.65 C ANISOU 1456 CG MET B 90 8684 13251 9847 -227 643 -2164 C ATOM 1457 SD MET B 90 54.518 17.393 31.962 1.00 96.20 S ANISOU 1457 SD MET B 90 10344 14929 11279 -119 609 -2037 S ATOM 1458 CE MET B 90 53.072 18.279 31.365 1.00 91.81 C ANISOU 1458 CE MET B 90 9640 14789 10455 -37 512 -1976 C ATOM 1459 N LYS B 91 54.864 11.348 34.151 1.00 99.84 N ANISOU 1459 N LYS B 91 10830 14514 12588 -552 857 -2448 N ATOM 1460 CA LYS B 91 55.612 10.088 34.187 1.00108.70 C ANISOU 1460 CA LYS B 91 11982 15434 13886 -686 928 -2562 C ATOM 1461 C LYS B 91 54.725 8.901 34.563 1.00109.34 C ANISOU 1461 C LYS B 91 12002 15483 14061 -751 951 -2662 C ATOM 1462 O LYS B 91 54.817 7.832 33.957 1.00110.64 O ANISOU 1462 O LYS B 91 12121 15637 14280 -921 1004 -2862 O ATOM 1463 CB LYS B 91 56.819 10.173 35.126 1.00113.23 C ANISOU 1463 CB LYS B 91 12689 15720 14612 -603 951 -2409 C ATOM 1464 CG LYS B 91 57.769 8.974 35.012 1.00116.38 C ANISOU 1464 CG LYS B 91 13114 15927 15180 -743 1023 -2518 C ATOM 1465 CD LYS B 91 58.899 9.048 36.039 1.00117.40 C ANISOU 1465 CD LYS B 91 13361 15799 15447 -658 1035 -2350 C ATOM 1466 CE LYS B 91 59.785 7.807 35.976 1.00119.59 C ANISOU 1466 CE LYS B 91 13652 15887 15899 -791 1107 -2451 C ATOM 1467 NZ LYS B 91 60.901 7.851 36.966 1.00117.99 N ANISOU 1467 NZ LYS B 91 13533 15462 15837 -741 1119 -2330 N TER 1468 LYS B 91 HETATM 1469 C ACE C 1 61.145 24.221 30.236 1.00 46.39 C HETATM 1470 O ACE C 1 60.109 24.778 30.622 1.00 51.69 O HETATM 1471 CH3 ACE C 1 62.473 24.451 30.905 1.00 39.43 C ATOM 1472 N SER C 2 61.484 23.395 29.244 1.00 68.20 N ANISOU 1472 N SER C 2 6918 11637 7359 -783 -1221 -878 N ATOM 1473 CA SER C 2 60.308 23.271 28.390 1.00 58.53 C ANISOU 1473 CA SER C 2 5708 10384 6145 -836 -1294 -823 C ATOM 1474 C SER C 2 59.153 22.478 29.022 1.00 53.70 C ANISOU 1474 C SER C 2 5114 9737 5552 -852 -1323 -815 C ATOM 1475 O SER C 2 57.994 22.748 28.723 1.00 54.96 O ANISOU 1475 O SER C 2 5255 9869 5757 -890 -1375 -766 O ATOM 1476 CB SER C 2 60.680 22.649 27.051 1.00 58.11 C ANISOU 1476 CB SER C 2 5716 10346 6016 -862 -1327 -816 C ATOM 1477 OG SER C 2 61.209 21.356 27.260 1.00 58.69 O ANISOU 1477 OG SER C 2 5852 10424 6022 -843 -1308 -863 O ATOM 1478 N THR C 3 59.449 21.512 29.892 1.00 55.17 N ANISOU 1478 N THR C 3 5332 9925 5705 -824 -1290 -861 N ATOM 1479 CA THR C 3 58.368 20.819 30.601 1.00 60.23 C ANISOU 1479 CA THR C 3 5984 10533 6366 -837 -1312 -855 C ATOM 1480 C THR C 3 57.760 21.676 31.731 1.00 58.69 C ANISOU 1480 C THR C 3 5720 10323 6255 -828 -1290 -850 C ATOM 1481 O THR C 3 56.533 21.668 31.910 1.00 52.26 O ANISOU 1481 O THR C 3 4891 9476 5489 -856 -1330 -816 O ATOM 1482 CB THR C 3 58.759 19.407 31.098 1.00 69.15 C ANISOU 1482 CB THR C 3 7174 11664 7436 -816 -1294 -900 C ATOM 1483 OG1 THR C 3 59.395 19.494 32.373 1.00 86.37 O ANISOU 1483 OG1 THR C 3 9327 13859 9630 -771 -1230 -944 O ATOM 1484 CG2 THR C 3 59.690 18.720 30.113 1.00 65.36 C ANISOU 1484 CG2 THR C 3 6753 11203 6877 -813 -1298 -919 C ATOM 1485 N VAL C 4 58.603 22.432 32.454 1.00 50.28 N ANISOU 1485 N VAL C 4 4613 9280 5209 -791 -1228 -883 N ATOM 1486 CA VAL C 4 58.117 23.418 33.434 1.00 48.99 C ANISOU 1486 CA VAL C 4 4384 9104 5126 -786 -1204 -880 C ATOM 1487 C VAL C 4 57.195 24.469 32.796 1.00 56.19 C ANISOU 1487 C VAL C 4 5245 9988 6116 -821 -1251 -820 C ATOM 1488 O VAL C 4 56.161 24.820 33.360 1.00 63.31 O ANISOU 1488 O VAL C 4 6106 10858 7089 -837 -1266 -799 O ATOM 1489 CB VAL C 4 59.286 24.105 34.207 1.00 43.44 C ANISOU 1489 CB VAL C 4 3650 8432 4422 -743 -1129 -928 C ATOM 1490 CG1 VAL C 4 59.000 25.595 34.506 1.00 38.76 C ANISOU 1490 CG1 VAL C 4 2984 7828 3915 -748 -1116 -910 C ATOM 1491 CG2 VAL C 4 59.590 23.341 35.473 1.00 45.56 C ANISOU 1491 CG2 VAL C 4 3936 8710 4663 -716 -1084 -979 C ATOM 1492 N HIS C 5 57.576 24.953 31.617 1.00 58.41 N ANISOU 1492 N HIS C 5 5526 10281 6386 -834 -1275 -792 N ATOM 1493 CA HIS C 5 56.791 25.939 30.876 1.00 58.85 C ANISOU 1493 CA HIS C 5 5532 10313 6516 -868 -1325 -729 C ATOM 1494 C HIS C 5 55.419 25.375 30.504 1.00 58.98 C ANISOU 1494 C HIS C 5 5561 10294 6556 -910 -1395 -682 C ATOM 1495 O HIS C 5 54.404 26.074 30.569 1.00 57.32 O ANISOU 1495 O HIS C 5 5292 10050 6439 -932 -1427 -638 O ATOM 1496 CB HIS C 5 57.544 26.362 29.610 1.00 56.07 C ANISOU 1496 CB HIS C 5 5189 9986 6128 -876 -1340 -710 C ATOM 1497 CG HIS C 5 56.858 27.435 28.824 1.00 58.88 C ANISOU 1497 CG HIS C 5 5489 10319 6562 -909 -1389 -644 C ATOM 1498 ND1 HIS C 5 56.631 28.697 29.330 1.00 63.92 N ANISOU 1498 ND1 HIS C 5 6049 10937 7302 -901 -1372 -629 N ATOM 1499 CD2 HIS C 5 56.356 27.438 27.567 1.00 47.09 C ANISOU 1499 CD2 HIS C 5 4007 8822 5064 -952 -1455 -590 C ATOM 1500 CE1 HIS C 5 56.020 29.432 28.416 1.00 50.40 C ANISOU 1500 CE1 HIS C 5 4295 9204 5650 -935 -1427 -565 C ATOM 1501 NE2 HIS C 5 55.841 28.690 27.339 1.00 44.14 N ANISOU 1501 NE2 HIS C 5 3557 8425 4792 -967 -1478 -540 N ATOM 1502 N GLU C 6 55.394 24.110 30.102 1.00 59.03 N ANISOU 1502 N GLU C 6 5641 10308 6482 -922 -1419 -692 N ATOM 1503 CA GLU C 6 54.133 23.441 29.772 1.00 65.09 C ANISOU 1503 CA GLU C 6 6428 11044 7258 -962 -1485 -653 C ATOM 1504 C GLU C 6 53.184 23.417 30.988 1.00 61.95 C ANISOU 1504 C GLU C 6 5993 10614 6930 -958 -1477 -655 C ATOM 1505 O GLU C 6 52.032 23.867 30.905 1.00 61.45 O ANISOU 1505 O GLU C 6 5883 10517 6948 -986 -1521 -606 O ATOM 1506 CB GLU C 6 54.404 22.018 29.251 1.00 72.41 C ANISOU 1506 CB GLU C 6 7448 11984 8081 -971 -1502 -674 C ATOM 1507 CG GLU C 6 53.174 21.257 28.751 1.00 82.39 C ANISOU 1507 CG GLU C 6 8744 13221 9340 -1016 -1573 -634 C ATOM 1508 CD GLU C 6 52.738 21.682 27.355 1.00 92.75 C ANISOU 1508 CD GLU C 6 10053 14534 10654 -1064 -1635 -576 C ATOM 1509 OE1 GLU C 6 53.551 22.293 26.626 1.00 97.91 O ANISOU 1509 OE1 GLU C 6 10700 15213 11286 -1062 -1625 -573 O ATOM 1510 OE2 GLU C 6 51.578 21.402 26.986 1.00 96.92 O ANISOU 1510 OE2 GLU C 6 10582 15039 11202 -1104 -1695 -531 O ATOM 1511 N ILE C 7 53.693 22.904 32.109 1.00 57.28 N ANISOU 1511 N ILE C 7 5420 10034 6308 -923 -1420 -712 N ATOM 1512 CA ILE C 7 52.944 22.784 33.356 1.00 61.31 C ANISOU 1512 CA ILE C 7 5904 10522 6870 -918 -1403 -724 C ATOM 1513 C ILE C 7 52.461 24.126 33.904 1.00 60.01 C ANISOU 1513 C ILE C 7 5649 10335 6816 -918 -1389 -705 C ATOM 1514 O ILE C 7 51.332 24.229 34.391 1.00 66.97 O ANISOU 1514 O ILE C 7 6493 11182 7770 -937 -1411 -682 O ATOM 1515 CB ILE C 7 53.779 22.077 34.427 1.00 65.41 C ANISOU 1515 CB ILE C 7 6457 11066 7331 -879 -1339 -792 C ATOM 1516 CG1 ILE C 7 54.124 20.655 33.972 1.00 61.21 C ANISOU 1516 CG1 ILE C 7 6010 10544 6704 -879 -1356 -809 C ATOM 1517 CG2 ILE C 7 53.033 22.053 35.744 1.00 64.38 C ANISOU 1517 CG2 ILE C 7 6296 10916 7252 -877 -1318 -806 C ATOM 1518 CD1 ILE C 7 55.345 20.086 34.662 1.00 50.42 C ANISOU 1518 CD1 ILE C 7 4673 9208 5275 -836 -1293 -871 C ATOM 1519 N LEU C 8 53.299 25.154 33.804 1.00 51.56 N ANISOU 1519 N LEU C 8 4543 9283 5765 -899 -1352 -715 N ATOM 1520 CA LEU C 8 52.926 26.483 34.285 1.00 54.73 C ANISOU 1520 CA LEU C 8 4858 9659 6277 -899 -1335 -699 C ATOM 1521 C LEU C 8 51.666 27.019 33.607 1.00 60.55 C ANISOU 1521 C LEU C 8 5541 10351 7113 -938 -1404 -626 C ATOM 1522 O LEU C 8 50.938 27.811 34.193 1.00 69.90 O ANISOU 1522 O LEU C 8 6653 11499 8408 -944 -1399 -608 O ATOM 1523 CB LEU C 8 54.078 27.484 34.122 1.00 51.01 C ANISOU 1523 CB LEU C 8 4362 9214 5805 -874 -1291 -717 C ATOM 1524 CG LEU C 8 55.263 27.414 35.108 1.00 57.77 C ANISOU 1524 CG LEU C 8 5237 10109 6603 -832 -1210 -791 C ATOM 1525 CD1 LEU C 8 56.354 28.451 34.787 1.00 50.07 C ANISOU 1525 CD1 LEU C 8 4237 9159 5631 -811 -1175 -802 C ATOM 1526 CD2 LEU C 8 54.806 27.572 36.555 1.00 55.57 C ANISOU 1526 CD2 LEU C 8 4926 9815 6372 -825 -1168 -824 C ATOM 1527 N SER C 9 51.402 26.587 32.379 1.00 53.17 N ANISOU 1527 N SER C 9 4640 9418 6143 -965 -1467 -584 N ATOM 1528 CA SER C 9 50.224 27.082 31.653 1.00 64.68 C ANISOU 1528 CA SER C 9 6045 10837 7693 -1003 -1535 -512 C ATOM 1529 C SER C 9 48.941 26.276 31.934 1.00 65.40 C ANISOU 1529 C SER C 9 6143 10899 7809 -1028 -1578 -492 C ATOM 1530 O SER C 9 47.881 26.592 31.427 1.00 65.94 O ANISOU 1530 O SER C 9 6164 10934 7955 -1059 -1633 -435 O ATOM 1531 CB SER C 9 50.491 27.098 30.148 1.00 64.06 C ANISOU 1531 CB SER C 9 5995 10779 7567 -1028 -1585 -474 C ATOM 1532 OG SER C 9 50.564 25.776 29.656 1.00 67.27 O ANISOU 1532 OG SER C 9 6491 11207 7860 -1042 -1611 -485 O ATOM 1533 N LYS C 10 49.066 25.222 32.726 1.00 72.37 N ANISOU 1533 N LYS C 10 7083 11793 8621 -1014 -1552 -539 N ATOM 1534 CA LYS C 10 47.940 24.407 33.137 1.00 72.21 C ANISOU 1534 CA LYS C 10 7074 11747 8617 -1034 -1584 -527 C ATOM 1535 C LYS C 10 47.879 24.497 34.643 1.00 72.43 C ANISOU 1535 C LYS C 10 7073 11765 8682 -1010 -1525 -571 C ATOM 1536 O LYS C 10 47.881 23.477 35.317 1.00 79.99 O ANISOU 1536 O LYS C 10 8083 12733 9577 -1003 -1508 -607 O ATOM 1537 CB LYS C 10 48.180 22.938 32.765 1.00 73.77 C ANISOU 1537 CB LYS C 10 7372 11968 8689 -1040 -1604 -547 C ATOM 1538 CG LYS C 10 48.298 22.643 31.283 1.00 76.19 C ANISOU 1538 CG LYS C 10 7724 12290 8935 -1068 -1658 -513 C ATOM 1539 CD LYS C 10 48.999 21.307 31.083 1.00 79.29 C ANISOU 1539 CD LYS C 10 8219 12710 9199 -1061 -1650 -554 C ATOM 1540 CE LYS C 10 48.819 20.768 29.663 1.00 86.87 C ANISOU 1540 CE LYS C 10 9233 13679 10095 -1100 -1712 -519 C ATOM 1541 NZ LYS C 10 49.052 19.293 29.603 1.00 87.60 N ANISOU 1541 NZ LYS C 10 9421 13780 10084 -1102 -1716 -553 N ATOM 1542 N LEU C 11 47.849 25.710 35.179 1.00 69.20 N ANISOU 1542 N LEU C 11 6582 11337 8373 -1000 -1490 -569 N ATOM 1543 CA LEU C 11 48.053 25.887 36.611 1.00 71.18 C ANISOU 1543 CA LEU C 11 6812 11591 8642 -978 -1420 -621 C ATOM 1544 C LEU C 11 47.471 27.222 37.038 1.00 75.46 C ANISOU 1544 C LEU C 11 7249 12090 9332 -983 -1404 -597 C ATOM 1545 O LEU C 11 47.574 28.200 36.290 1.00 77.67 O ANISOU 1545 O LEU C 11 7479 12355 9676 -987 -1421 -560 O ATOM 1546 CB LEU C 11 49.556 25.867 36.916 1.00 66.62 C ANISOU 1546 CB LEU C 11 6279 11064 7970 -941 -1355 -683 C ATOM 1547 CG LEU C 11 50.114 25.334 38.233 1.00 58.26 C ANISOU 1547 CG LEU C 11 5252 10033 6852 -915 -1287 -754 C ATOM 1548 CD1 LEU C 11 49.915 23.838 38.303 1.00 57.14 C ANISOU 1548 CD1 LEU C 11 5187 9901 6625 -919 -1309 -767 C ATOM 1549 CD2 LEU C 11 51.604 25.674 38.340 1.00 58.31 C ANISOU 1549 CD2 LEU C 11 5278 10084 6794 -880 -1227 -803 C ATOM 1550 N SER C 12 46.880 27.275 38.237 1.00 71.02 N ANISOU 1550 N SER C 12 6650 11507 8827 -984 -1370 -619 N ATOM 1551 CA SER C 12 46.190 28.488 38.694 1.00 66.36 C ANISOU 1551 CA SER C 12 5954 10867 8394 -993 -1352 -594 C ATOM 1552 C SER C 12 46.321 28.796 40.183 1.00 69.94 C ANISOU 1552 C SER C 12 6382 11322 8869 -981 -1272 -651 C ATOM 1553 O SER C 12 46.611 27.916 40.988 1.00 60.56 O ANISOU 1553 O SER C 12 5255 10169 7586 -972 -1241 -705 O ATOM 1554 CB SER C 12 44.709 28.439 38.308 1.00 63.96 C ANISOU 1554 CB SER C 12 5594 10506 8201 -1024 -1416 -529 C ATOM 1555 OG SER C 12 44.358 27.161 37.797 1.00 60.99 O ANISOU 1555 OG SER C 12 5293 10147 7734 -1038 -1473 -519 O ATOM 1556 N LEU C 13 46.097 30.061 40.532 1.00 81.51 N ANISOU 1556 N LEU C 13 7756 12750 10464 -984 -1238 -637 N ATOM 1557 CA LEU C 13 46.160 30.516 41.916 1.00 82.67 C ANISOU 1557 CA LEU C 13 7870 12896 10644 -979 -1158 -690 C ATOM 1558 C LEU C 13 45.134 29.801 42.786 1.00 84.12 C ANISOU 1558 C LEU C 13 8051 13062 10848 -998 -1158 -698 C ATOM 1559 O LEU C 13 45.177 29.893 44.014 1.00 86.33 O ANISOU 1559 O LEU C 13 8323 13352 11126 -998 -1092 -752 O ATOM 1560 CB LEU C 13 45.920 32.022 41.977 1.00 81.73 C ANISOU 1560 CB LEU C 13 7644 12726 10683 -984 -1128 -659 C ATOM 1561 CG LEU C 13 46.777 32.846 41.011 1.00 86.93 C ANISOU 1561 CG LEU C 13 8293 13392 11346 -969 -1137 -638 C ATOM 1562 CD1 LEU C 13 46.362 34.301 41.002 1.00 92.60 C ANISOU 1562 CD1 LEU C 13 8895 14045 12242 -976 -1114 -594 C ATOM 1563 CD2 LEU C 13 48.236 32.738 41.379 1.00 85.20 C ANISOU 1563 CD2 LEU C 13 8145 13241 10987 -940 -1083 -714 C TER 1564 LEU C 13 HETATM 1565 C ACE D 1 78.285 29.604 38.877 1.00 39.70 C HETATM 1566 O ACE D 1 78.611 29.149 39.980 1.00 41.03 O HETATM 1567 CH3 ACE D 1 76.923 29.337 38.278 1.00 37.40 C ATOM 1568 N SER D 2 78.965 30.679 38.468 1.00 45.15 N ANISOU 1568 N SER D 2 3838 6910 6409 -916 15 132 N ATOM 1569 CA SER D 2 80.301 30.496 39.006 1.00 41.56 C ANISOU 1569 CA SER D 2 3292 6491 6009 -920 -80 102 C ATOM 1570 C SER D 2 80.525 31.413 40.194 1.00 43.15 C ANISOU 1570 C SER D 2 3484 6722 6188 -980 -158 83 C ATOM 1571 O SER D 2 81.456 31.209 40.960 1.00 42.33 O ANISOU 1571 O SER D 2 3320 6655 6106 -985 -258 60 O ATOM 1572 CB SER D 2 81.360 30.749 37.943 1.00 35.99 C ANISOU 1572 CB SER D 2 2528 5736 5411 -902 -50 73 C ATOM 1573 OG SER D 2 81.405 32.121 37.628 1.00 51.05 O ANISOU 1573 OG SER D 2 4449 7598 7350 -940 -12 58 O ATOM 1574 N THR D 3 79.675 32.421 40.358 1.00 35.83 N ANISOU 1574 N THR D 3 2623 5775 5217 -1022 -115 89 N ATOM 1575 CA THR D 3 79.767 33.225 41.561 1.00 42.65 C ANISOU 1575 CA THR D 3 3491 6667 6048 -1082 -189 71 C ATOM 1576 C THR D 3 79.080 32.477 42.722 1.00 45.64 C ANISOU 1576 C THR D 3 3940 7072 6329 -1073 -250 91 C ATOM 1577 O THR D 3 79.588 32.467 43.831 1.00 47.91 O ANISOU 1577 O THR D 3 4254 7352 6598 -1066 -349 68 O ATOM 1578 CB THR D 3 79.253 34.681 41.366 1.00 51.28 C ANISOU 1578 CB THR D 3 4635 7712 7138 -1127 -128 62 C ATOM 1579 OG1 THR D 3 77.874 34.778 41.724 1.00 59.34 O ANISOU 1579 OG1 THR D 3 5745 8732 8069 -1148 -87 90 O ATOM 1580 CG2 THR D 3 79.440 35.141 39.923 1.00 46.78 C ANISOU 1580 CG2 THR D 3 4059 7072 6642 -1098 -35 59 C ATOM 1581 N VAL D 4 77.947 31.827 42.459 1.00 39.38 N ANISOU 1581 N VAL D 4 3220 6267 5475 -1042 -186 128 N ATOM 1582 CA VAL D 4 77.351 30.954 43.464 1.00 33.74 C ANISOU 1582 CA VAL D 4 2613 5534 4672 -996 -235 142 C ATOM 1583 C VAL D 4 78.354 29.888 43.915 1.00 40.72 C ANISOU 1583 C VAL D 4 3456 6438 5577 -945 -334 131 C ATOM 1584 O VAL D 4 78.543 29.651 45.107 1.00 46.74 O ANISOU 1584 O VAL D 4 4279 7187 6294 -928 -427 118 O ATOM 1585 CB VAL D 4 76.096 30.267 42.951 1.00 29.77 C ANISOU 1585 CB VAL D 4 2177 5021 4114 -965 -148 183 C ATOM 1586 CG1 VAL D 4 75.888 28.964 43.671 1.00 32.26 C ANISOU 1586 CG1 VAL D 4 2558 5332 4367 -901 -204 198 C ATOM 1587 CG2 VAL D 4 74.908 31.154 43.148 1.00 34.05 C ANISOU 1587 CG2 VAL D 4 2811 5528 4597 -1003 -86 192 C ATOM 1588 N HIS D 5 79.026 29.273 42.956 1.00 42.96 N ANISOU 1588 N HIS D 5 3635 6753 5933 -922 -315 135 N ATOM 1589 CA HIS D 5 80.001 28.231 43.260 1.00 46.38 C ANISOU 1589 CA HIS D 5 4018 7206 6398 -872 -404 125 C ATOM 1590 C HIS D 5 81.090 28.729 44.210 1.00 45.93 C ANISOU 1590 C HIS D 5 3933 7148 6372 -891 -519 83 C ATOM 1591 O HIS D 5 81.521 28.023 45.124 1.00 48.44 O ANISOU 1591 O HIS D 5 4278 7462 6666 -853 -619 74 O ATOM 1592 CB HIS D 5 80.649 27.753 41.977 1.00 42.46 C ANISOU 1592 CB HIS D 5 3397 6744 5990 -859 -358 129 C ATOM 1593 CG HIS D 5 81.759 26.790 42.204 1.00 46.98 C ANISOU 1593 CG HIS D 5 3902 7338 6611 -813 -448 113 C ATOM 1594 ND1 HIS D 5 81.539 25.506 42.653 1.00 45.50 N ANISOU 1594 ND1 HIS D 5 3765 7148 6374 -750 -491 132 N ATOM 1595 CD2 HIS D 5 83.100 26.927 42.076 1.00 45.99 C ANISOU 1595 CD2 HIS D 5 3662 7233 6579 -822 -505 78 C ATOM 1596 CE1 HIS D 5 82.702 24.888 42.786 1.00 47.00 C ANISOU 1596 CE1 HIS D 5 3874 7357 6626 -721 -574 110 C ATOM 1597 NE2 HIS D 5 83.663 25.730 42.443 1.00 49.60 N ANISOU 1597 NE2 HIS D 5 4101 7700 7043 -763 -583 77 N ATOM 1598 N GLU D 6 81.527 29.956 43.980 1.00 38.81 N ANISOU 1598 N GLU D 6 2976 6249 5523 -950 -504 57 N ATOM 1599 CA GLU D 6 82.537 30.551 44.820 1.00 46.26 C ANISOU 1599 CA GLU D 6 3888 7190 6499 -974 -605 17 C ATOM 1600 C GLU D 6 81.979 30.834 46.205 1.00 54.37 C ANISOU 1600 C GLU D 6 5044 8183 7432 -979 -668 13 C ATOM 1601 O GLU D 6 82.632 30.557 47.204 1.00 60.45 O ANISOU 1601 O GLU D 6 5830 8946 8193 -962 -779 -8 O ATOM 1602 CB GLU D 6 83.089 31.835 44.200 1.00 43.94 C ANISOU 1602 CB GLU D 6 3506 6905 6282 -1038 -567 -9 C ATOM 1603 CG GLU D 6 84.107 32.507 45.091 1.00 56.23 C ANISOU 1603 CG GLU D 6 5033 8458 7873 -1065 -672 -52 C ATOM 1604 CD GLU D 6 84.752 33.721 44.464 1.00 75.46 C ANISOU 1604 CD GLU D 6 7379 10901 10393 -1123 -637 -80 C ATOM 1605 OE1 GLU D 6 84.444 34.046 43.294 1.00 76.69 O ANISOU 1605 OE1 GLU D 6 7539 11018 10583 -1114 -520 -70 O ATOM 1606 OE2 GLU D 6 85.583 34.350 45.154 1.00 90.64 O ANISOU 1606 OE2 GLU D 6 9271 12821 12346 -1150 -719 -116 O ATOM 1607 N ILE D 7 80.770 31.380 46.264 1.00 55.19 N ANISOU 1607 N ILE D 7 5242 8262 7466 -1004 -595 32 N ATOM 1608 CA ILE D 7 80.172 31.769 47.542 1.00 49.87 C ANISOU 1608 CA ILE D 7 4693 7553 6702 -1017 -642 27 C ATOM 1609 C ILE D 7 79.888 30.545 48.420 1.00 49.63 C ANISOU 1609 C ILE D 7 4751 7510 6596 -958 -708 41 C ATOM 1610 O ILE D 7 80.095 30.580 49.631 1.00 48.81 O ANISOU 1610 O ILE D 7 4714 7385 6446 -956 -801 24 O ATOM 1611 CB ILE D 7 78.884 32.591 47.346 1.00 43.96 C ANISOU 1611 CB ILE D 7 4023 6780 5899 -1056 -543 44 C ATOM 1612 CG1 ILE D 7 79.179 33.898 46.619 1.00 40.31 C ANISOU 1612 CG1 ILE D 7 3483 6327 5506 -1119 -489 27 C ATOM 1613 CG2 ILE D 7 78.190 32.861 48.683 1.00 34.23 C ANISOU 1613 CG2 ILE D 7 2927 5510 4569 -1065 -586 40 C ATOM 1614 CD1 ILE D 7 77.931 34.700 46.350 1.00 48.00 C ANISOU 1614 CD1 ILE D 7 4528 7276 6435 -1157 -390 44 C ATOM 1615 N LEU D 8 79.414 29.470 47.804 1.00 48.79 N ANISOU 1615 N LEU D 8 4648 7414 6475 -910 -659 73 N ATOM 1616 CA LEU D 8 79.123 28.237 48.521 1.00 42.84 C ANISOU 1616 CA LEU D 8 3975 6649 5652 -852 -713 90 C ATOM 1617 C LEU D 8 80.321 27.756 49.330 1.00 49.02 C ANISOU 1617 C LEU D 8 4726 7438 6461 -826 -848 63 C ATOM 1618 O LEU D 8 80.176 27.335 50.475 1.00 57.23 O ANISOU 1618 O LEU D 8 5862 8455 7429 -805 -927 61 O ATOM 1619 CB LEU D 8 78.718 27.151 47.542 1.00 35.99 C ANISOU 1619 CB LEU D 8 3081 5802 4793 -804 -644 125 C ATOM 1620 CG LEU D 8 77.313 27.272 46.995 1.00 36.52 C ANISOU 1620 CG LEU D 8 3215 5853 4806 -812 -525 158 C ATOM 1621 CD1 LEU D 8 77.035 26.140 46.017 1.00 36.71 C ANISOU 1621 CD1 LEU D 8 3205 5899 4845 -763 -465 190 C ATOM 1622 CD2 LEU D 8 76.356 27.240 48.161 1.00 35.95 C ANISOU 1622 CD2 LEU D 8 3293 5743 4625 -809 -546 164 C ATOM 1623 N SER D 9 81.512 27.857 48.757 1.00 50.18 N ANISOU 1623 N SER D 9 4741 7615 6712 -831 -877 41 N ATOM 1624 CA SER D 9 82.704 27.331 49.424 1.00 48.49 C ANISOU 1624 CA SER D 9 4483 7407 6533 -803 -1006 15 C ATOM 1625 C SER D 9 83.142 28.203 50.588 1.00 53.91 C ANISOU 1625 C SER D 9 5211 8070 7202 -840 -1098 -18 C ATOM 1626 O SER D 9 84.102 27.892 51.288 1.00 58.43 O ANISOU 1626 O SER D 9 5761 8642 7799 -822 -1215 -43 O ATOM 1627 CB SER D 9 83.839 27.230 48.432 1.00 42.09 C ANISOU 1627 CB SER D 9 3515 6633 5845 -800 -1003 -2 C ATOM 1628 OG SER D 9 84.266 28.528 48.083 1.00 49.04 O ANISOU 1628 OG SER D 9 4328 7519 6787 -862 -976 -27 O ATOM 1629 N LYS D 10 82.443 29.308 50.787 1.00 56.60 N ANISOU 1629 N LYS D 10 5611 8391 7503 -892 -1047 -20 N ATOM 1630 CA LYS D 10 82.736 30.176 51.910 1.00 58.99 C ANISOU 1630 CA LYS D 10 5964 8670 7780 -929 -1127 -50 C ATOM 1631 C LYS D 10 81.642 30.089 52.976 1.00 53.81 C ANISOU 1631 C LYS D 10 5472 7974 6998 -926 -1136 -35 C ATOM 1632 O LYS D 10 81.697 30.801 53.967 1.00 58.45 O ANISOU 1632 O LYS D 10 6124 8537 7549 -958 -1194 -56 O ATOM 1633 CB LYS D 10 82.927 31.632 51.447 1.00 59.78 C ANISOU 1633 CB LYS D 10 6003 8775 7935 -997 -1076 -71 C ATOM 1634 CG LYS D 10 84.025 31.819 50.417 1.00 57.41 C ANISOU 1634 CG LYS D 10 5543 8511 7760 -1007 -1065 -89 C ATOM 1635 CD LYS D 10 84.722 33.160 50.557 1.00 56.10 C ANISOU 1635 CD LYS D 10 5321 8345 7650 -1068 -1089 -126 C ATOM 1636 CE LYS D 10 86.029 33.181 49.760 1.00 67.05 C ANISOU 1636 CE LYS D 10 6549 9765 9163 -1070 -1107 -151 C ATOM 1637 NZ LYS D 10 85.807 33.151 48.269 1.00 68.78 N ANISOU 1637 NZ LYS D 10 6686 10011 9437 -1076 -984 -132 N ATOM 1638 N LEU D 11 80.649 29.227 52.779 1.00 46.21 N ANISOU 1638 N LEU D 11 4580 7005 5971 -889 -1077 1 N ATOM 1639 CA LEU D 11 79.576 29.114 53.768 1.00 48.89 C ANISOU 1639 CA LEU D 11 5076 7306 6192 -887 -1079 14 C ATOM 1640 C LEU D 11 79.707 27.905 54.717 1.00 53.17 C ANISOU 1640 C LEU D 11 5695 7834 6673 -832 -1176 20 C ATOM 1641 O LEU D 11 80.508 26.986 54.498 1.00 53.12 O ANISOU 1641 O LEU D 11 5620 7849 6713 -787 -1233 19 O ATOM 1642 CB LEU D 11 78.192 29.150 53.094 1.00 48.53 C ANISOU 1642 CB LEU D 11 5083 7253 6102 -892 -944 47 C ATOM 1643 CG LEU D 11 77.935 30.332 52.142 1.00 49.14 C ANISOU 1643 CG LEU D 11 5098 7341 6233 -946 -843 44 C ATOM 1644 CD1 LEU D 11 76.515 30.306 51.580 1.00 47.52 C ANISOU 1644 CD1 LEU D 11 4956 7122 5976 -947 -720 77 C ATOM 1645 CD2 LEU D 11 78.225 31.668 52.827 1.00 50.91 C ANISOU 1645 CD2 LEU D 11 5336 7547 6459 -1006 -880 12 C ATOM 1646 N SER D 12 78.921 27.926 55.786 1.00 59.18 N ANISOU 1646 N SER D 12 6599 8556 7329 -837 -1196 23 N ATOM 1647 CA SER D 12 78.963 26.861 56.774 1.00 63.69 C ANISOU 1647 CA SER D 12 7259 9108 7831 -791 -1288 28 C ATOM 1648 C SER D 12 77.592 26.694 57.407 1.00 65.72 C ANISOU 1648 C SER D 12 7674 9329 7969 -792 -1239 49 C ATOM 1649 O SER D 12 76.697 27.507 57.192 1.00 67.06 O ANISOU 1649 O SER D 12 7880 9485 8113 -831 -1146 54 O ATOM 1650 CB SER D 12 80.007 27.175 57.841 1.00 60.97 C ANISOU 1650 CB SER D 12 6920 8751 7495 -804 -1426 -7 C ATOM 1651 OG SER D 12 79.681 28.386 58.494 1.00 66.33 O ANISOU 1651 OG SER D 12 7662 9403 8137 -863 -1422 -26 O ATOM 1652 N LEU D 13 77.430 25.640 58.196 1.00 64.40 N ANISOU 1652 N LEU D 13 7597 9142 7729 -748 -1302 59 N ATOM 1653 CA LEU D 13 76.131 25.330 58.776 1.00 58.38 C ANISOU 1653 CA LEU D 13 6984 8345 6853 -743 -1255 79 C ATOM 1654 C LEU D 13 75.937 25.916 60.177 1.00 66.01 C ANISOU 1654 C LEU D 13 8077 9267 7737 -778 -1319 58 C ATOM 1655 O LEU D 13 76.889 26.436 60.781 1.00 60.69 O ANISOU 1655 O LEU D 13 7378 8590 7091 -800 -1416 28 O ATOM 1656 CB LEU D 13 75.932 23.823 58.805 1.00 54.07 C ANISOU 1656 CB LEU D 13 6476 7801 6267 -677 -1274 106 C ATOM 1657 CG LEU D 13 75.890 23.171 57.431 1.00 52.11 C ANISOU 1657 CG LEU D 13 6123 7591 6084 -641 -1196 132 C ATOM 1658 CD1 LEU D 13 76.126 21.679 57.556 1.00 49.14 C ANISOU 1658 CD1 LEU D 13 5762 7222 5688 -574 -1253 149 C ATOM 1659 CD2 LEU D 13 74.550 23.464 56.805 1.00 57.09 C ANISOU 1659 CD2 LEU D 13 6796 8215 6682 -657 -1055 156 C ATOM 1660 N GLU D 14 74.685 25.824 60.647 1.00 76.62 N ANISOU 1660 N GLU D 14 9553 10577 8982 -784 -1259 73 N ATOM 1661 CA GLU D 14 74.187 26.250 61.977 1.00 84.80 C ANISOU 1661 CA GLU D 14 10736 11565 9920 -815 -1296 58 C ATOM 1662 C GLU D 14 73.674 27.694 62.029 1.00 91.00 C ANISOU 1662 C GLU D 14 11539 12334 10703 -883 -1230 41 C ATOM 1663 O GLU D 14 73.120 28.132 63.045 1.00 91.77 O ANISOU 1663 O GLU D 14 11758 12390 10719 -914 -1242 29 O ATOM 1664 CB GLU D 14 75.184 25.992 63.116 1.00 82.11 C ANISOU 1664 CB GLU D 14 10431 11209 9558 -807 -1449 35 C ATOM 1665 CG GLU D 14 75.759 24.594 63.153 1.00 78.91 C ANISOU 1665 CG GLU D 14 10010 10816 9156 -741 -1526 48 C ATOM 1666 CD GLU D 14 77.268 24.630 63.109 1.00 85.62 C ANISOU 1666 CD GLU D 14 10745 11691 10096 -732 -1639 25 C ATOM 1667 OE1 GLU D 14 77.823 25.734 63.322 1.00 89.87 O ANISOU 1667 OE1 GLU D 14 11244 12228 10675 -779 -1670 -3 O ATOM 1668 OE2 GLU D 14 77.895 23.574 62.857 1.00 82.83 O ANISOU 1668 OE2 GLU D 14 10339 11358 9777 -679 -1694 35 O TER 1669 GLU D 14 ATOM 1670 N GLY E 1 77.601 34.419 57.285 1.00 80.39 N ANISOU 1670 N GLY E 1 11019 12231 7293 457 512 694 N ATOM 1671 CA GLY E 1 78.078 33.314 56.470 1.00 78.45 C ANISOU 1671 CA GLY E 1 10618 11950 7240 523 452 607 C ATOM 1672 C GLY E 1 77.497 31.997 56.950 1.00 77.84 C ANISOU 1672 C GLY E 1 10533 11727 7318 502 453 631 C ATOM 1673 O GLY E 1 78.103 30.941 56.773 1.00 68.08 O ANISOU 1673 O GLY E 1 9213 10415 6240 534 381 619 O ATOM 1674 N LYS E 2 76.311 32.069 57.552 1.00 84.79 N ANISOU 1674 N LYS E 2 11498 12565 8152 448 538 668 N ATOM 1675 CA LYS E 2 75.676 30.911 58.188 1.00 82.78 C ANISOU 1675 CA LYS E 2 11260 12167 8026 416 547 712 C ATOM 1676 C LYS E 2 74.426 30.449 57.429 1.00 73.57 C ANISOU 1676 C LYS E 2 10003 11001 6951 439 635 591 C ATOM 1677 O LYS E 2 73.593 31.262 57.022 1.00 76.76 O ANISOU 1677 O LYS E 2 10413 11496 7256 439 724 537 O ATOM 1678 CB LYS E 2 75.312 31.235 59.639 1.00 81.42 C ANISOU 1678 CB LYS E 2 11269 11926 7741 329 572 869 C ATOM 1679 CG LYS E 2 75.857 30.262 60.679 1.00 91.16 C ANISOU 1679 CG LYS E 2 12558 13015 9064 292 492 991 C ATOM 1680 CD LYS E 2 75.346 30.637 62.085 1.00 97.86 C ANISOU 1680 CD LYS E 2 13592 13800 9788 205 531 1139 C ATOM 1681 CE LYS E 2 76.010 29.834 63.198 1.00 99.73 C ANISOU 1681 CE LYS E 2 13901 13906 10086 164 443 1277 C ATOM 1682 NZ LYS E 2 75.416 30.180 64.522 1.00 99.24 N ANISOU 1682 NZ LYS E 2 14021 13783 9904 80 491 1413 N ATOM 1683 N VAL E 3 74.300 29.134 57.269 1.00 61.45 N ANISOU 1683 N VAL E 3 8385 9360 5604 455 609 555 N ATOM 1684 CA VAL E 3 73.220 28.529 56.500 1.00 54.70 C ANISOU 1684 CA VAL E 3 7430 8495 4860 478 676 436 C ATOM 1685 C VAL E 3 72.213 27.813 57.389 1.00 53.33 C ANISOU 1685 C VAL E 3 7322 8194 4748 418 724 506 C ATOM 1686 O VAL E 3 72.545 26.841 58.072 1.00 59.02 O ANISOU 1686 O VAL E 3 8063 8784 5577 398 671 580 O ATOM 1687 CB VAL E 3 73.780 27.525 55.471 1.00 48.35 C ANISOU 1687 CB VAL E 3 6466 7669 4237 547 616 318 C ATOM 1688 CG1 VAL E 3 72.654 26.871 54.699 1.00 52.92 C ANISOU 1688 CG1 VAL E 3 6945 8232 4929 563 681 194 C ATOM 1689 CG2 VAL E 3 74.740 28.217 54.555 1.00 47.66 C ANISOU 1689 CG2 VAL E 3 6309 7706 4092 609 574 246 C ATOM 1690 N THR E 4 70.986 28.312 57.370 1.00 48.84 N ANISOU 1690 N THR E 4 6783 7664 4109 391 828 486 N ATOM 1691 CA THR E 4 69.869 27.736 58.116 1.00 52.81 C ANISOU 1691 CA THR E 4 7342 8061 4664 337 892 544 C ATOM 1692 C THR E 4 68.854 27.173 57.117 1.00 56.99 C ANISOU 1692 C THR E 4 7740 8601 5311 364 949 404 C ATOM 1693 O THR E 4 68.742 27.653 55.975 1.00 56.75 O ANISOU 1693 O THR E 4 7613 8692 5258 412 971 279 O ATOM 1694 CB THR E 4 69.159 28.841 58.925 1.00 63.54 C ANISOU 1694 CB THR E 4 8847 9459 5837 281 978 639 C ATOM 1695 OG1 THR E 4 70.143 29.675 59.543 1.00 74.28 O ANISOU 1695 OG1 THR E 4 10315 10855 7052 264 929 735 O ATOM 1696 CG2 THR E 4 68.230 28.265 59.991 1.00 64.63 C ANISOU 1696 CG2 THR E 4 9074 9467 6014 217 1032 738 C ATOM 1697 N PHE E 5 68.084 26.178 57.518 1.00 56.30 N ANISOU 1697 N PHE E 5 7648 8394 5350 332 976 424 N ATOM 1698 CA PHE E 5 67.114 25.667 56.566 1.00 63.39 C ANISOU 1698 CA PHE E 5 8422 9306 6357 353 1028 292 C ATOM 1699 C PHE E 5 65.696 26.082 56.850 1.00 62.82 C ANISOU 1699 C PHE E 5 8396 9249 6226 308 1140 313 C ATOM 1700 O PHE E 5 65.055 25.574 57.773 1.00 66.61 O ANISOU 1700 O PHE E 5 8947 9616 6747 255 1175 404 O ATOM 1701 CB PHE E 5 67.314 24.185 56.320 1.00 64.06 C ANISOU 1701 CB PHE E 5 8414 9269 6656 369 972 242 C ATOM 1702 CG PHE E 5 68.670 23.900 55.803 1.00 67.86 C ANISOU 1702 CG PHE E 5 8830 9762 7191 426 872 199 C ATOM 1703 CD1 PHE E 5 69.054 24.424 54.579 1.00 63.52 C ANISOU 1703 CD1 PHE E 5 8181 9343 6609 487 859 71 C ATOM 1704 CD2 PHE E 5 69.606 23.210 56.564 1.00 72.92 C ANISOU 1704 CD2 PHE E 5 9515 10290 7901 418 791 295 C ATOM 1705 CE1 PHE E 5 70.338 24.224 54.077 1.00 65.25 C ANISOU 1705 CE1 PHE E 5 8341 9579 6873 544 771 33 C ATOM 1706 CE2 PHE E 5 70.894 22.993 56.068 1.00 78.00 C ANISOU 1706 CE2 PHE E 5 10095 10949 8592 474 701 260 C ATOM 1707 CZ PHE E 5 71.260 23.501 54.815 1.00 72.05 C ANISOU 1707 CZ PHE E 5 9239 10326 7811 537 692 127 C ATOM 1708 N PRO E 6 65.208 27.015 56.022 1.00 65.27 N ANISOU 1708 N PRO E 6 8660 9700 6438 333 1200 229 N ATOM 1709 CA PRO E 6 63.951 27.730 56.201 1.00 69.62 C ANISOU 1709 CA PRO E 6 9257 10302 6895 299 1313 252 C ATOM 1710 C PRO E 6 62.812 26.743 56.144 1.00 70.11 C ANISOU 1710 C PRO E 6 9258 10277 7105 274 1360 219 C ATOM 1711 O PRO E 6 62.813 25.852 55.293 1.00 75.08 O ANISOU 1711 O PRO E 6 9757 10885 7885 304 1322 104 O ATOM 1712 CB PRO E 6 63.892 28.651 54.964 1.00 68.72 C ANISOU 1712 CB PRO E 6 9054 10360 6697 352 1340 129 C ATOM 1713 CG PRO E 6 65.238 28.569 54.311 1.00 59.05 C ANISOU 1713 CG PRO E 6 7765 9175 5496 409 1239 64 C ATOM 1714 CD PRO E 6 65.731 27.202 54.660 1.00 61.51 C ANISOU 1714 CD PRO E 6 8053 9339 5980 403 1162 82 C ATOM 1715 N LYS E 7 61.867 26.877 57.057 1.00 72.53 N ANISOU 1715 N LYS E 7 9660 10527 7371 217 1440 321 N ATOM 1716 CA LYS E 7 60.640 26.125 56.947 1.00 80.39 C ANISOU 1716 CA LYS E 7 10595 11461 8489 191 1499 290 C ATOM 1717 C LYS E 7 59.593 27.125 56.482 1.00 86.61 C ANISOU 1717 C LYS E 7 11366 12373 9168 192 1604 255 C ATOM 1718 O LYS E 7 59.038 27.868 57.283 1.00 97.66 O ANISOU 1718 O LYS E 7 12881 13779 10447 155 1683 362 O ATOM 1719 CB LYS E 7 60.289 25.493 58.291 1.00 81.06 C ANISOU 1719 CB LYS E 7 10792 11389 8620 130 1519 431 C ATOM 1720 CG LYS E 7 61.458 24.717 58.910 1.00 86.41 C ANISOU 1720 CG LYS E 7 11511 11952 9367 129 1416 493 C ATOM 1721 CD LYS E 7 61.194 24.305 60.366 1.00 96.82 C ANISOU 1721 CD LYS E 7 12966 13127 10693 67 1438 653 C ATOM 1722 CE LYS E 7 61.588 25.395 61.376 1.00100.65 C ANISOU 1722 CE LYS E 7 13622 13641 10981 38 1455 790 C ATOM 1723 NZ LYS E 7 63.061 25.474 61.645 1.00 99.61 N ANISOU 1723 NZ LYS E 7 13535 13505 10808 56 1348 832 N ATOM 1724 N MET E 8 59.368 27.165 55.173 1.00 83.25 N ANISOU 1724 N MET E 8 10798 12050 8783 236 1603 107 N ATOM 1725 CA MET E 8 58.483 28.145 54.554 1.00 85.44 C ANISOU 1725 CA MET E 8 11041 12464 8959 247 1692 60 C ATOM 1726 C MET E 8 57.010 27.713 54.719 1.00 89.29 C ANISOU 1726 C MET E 8 11501 12903 9523 204 1779 73 C ATOM 1727 O MET E 8 56.768 26.508 54.824 1.00 94.32 O ANISOU 1727 O MET E 8 12091 13422 10325 182 1750 57 O ATOM 1728 CB MET E 8 58.875 28.312 53.087 1.00 86.59 C ANISOU 1728 CB MET E 8 11045 12737 9120 311 1649 -103 C ATOM 1729 CG MET E 8 60.374 28.556 52.867 1.00 86.69 C ANISOU 1729 CG MET E 8 11068 12785 9087 357 1555 -123 C ATOM 1730 SD MET E 8 60.872 28.450 51.130 1.00115.39 S ANISOU 1730 SD MET E 8 14526 16540 12779 435 1497 -321 S ATOM 1731 CE MET E 8 60.780 26.675 50.847 1.00 53.97 C ANISOU 1731 CE MET E 8 6643 8616 5246 428 1436 -396 C ATOM 1732 N LYS E 9 56.006 28.608 54.707 1.00 84.77 N ANISOU 1732 N LYS E 9 10949 12414 8847 191 1884 99 N ATOM 1733 CA LYS E 9 55.956 29.974 54.136 1.00 79.76 C ANISOU 1733 CA LYS E 9 10313 11945 8045 226 1935 69 C ATOM 1734 C LYS E 9 55.922 29.918 52.599 1.00 75.82 C ANISOU 1734 C LYS E 9 9644 11564 7599 279 1905 -103 C ATOM 1735 O LYS E 9 56.578 30.705 51.906 1.00 76.24 O ANISOU 1735 O LYS E 9 9672 11740 7555 329 1882 -165 O ATOM 1736 CB LYS E 9 57.016 30.961 54.683 1.00 78.38 C ANISOU 1736 CB LYS E 9 10266 11811 7703 238 1913 146 C ATOM 1737 CG LYS E 9 56.674 32.432 54.505 1.00 80.45 C ANISOU 1737 CG LYS E 9 10573 12215 7779 254 2000 165 C ATOM 1738 CD LYS E 9 57.839 33.336 54.894 1.00 80.49 C ANISOU 1738 CD LYS E 9 10689 12264 7631 268 1964 220 C ATOM 1739 CE LYS E 9 58.680 33.716 53.679 1.00 77.48 C ANISOU 1739 CE LYS E 9 10203 12011 7226 335 1900 92 C ATOM 1740 NZ LYS E 9 57.863 34.430 52.658 1.00 74.15 N ANISOU 1740 NZ LYS E 9 9701 11643 6831 343 1933 -3 N ATOM 1741 N ILE E 10 55.122 28.995 52.073 1.00 71.48 N ANISOU 1741 N ILE E 10 8980 10977 7201 267 1909 -180 N ATOM 1742 CA ILE E 10 55.027 28.796 50.629 1.00 72.79 C ANISOU 1742 CA ILE E 10 8984 11241 7431 311 1877 -347 C ATOM 1743 C ILE E 10 53.629 29.118 50.105 1.00 74.09 C ANISOU 1743 C ILE E 10 9073 11486 7591 299 1968 -382 C ATOM 1744 O ILE E 10 52.655 28.506 50.537 1.00 74.42 O ANISOU 1744 O ILE E 10 9109 11444 7724 250 2013 -341 O ATOM 1745 CB ILE E 10 55.366 27.331 50.239 1.00 71.26 C ANISOU 1745 CB ILE E 10 8699 10942 7436 312 1787 -435 C ATOM 1746 CG1 ILE E 10 56.792 26.976 50.645 1.00 80.19 C ANISOU 1746 CG1 ILE E 10 9888 12000 8582 331 1692 -407 C ATOM 1747 CG2 ILE E 10 55.238 27.116 48.764 1.00 58.09 C ANISOU 1747 CG2 ILE E 10 6872 9371 5830 353 1757 -607 C ATOM 1748 CD1 ILE E 10 57.151 25.524 50.423 1.00 81.26 C ANISOU 1748 CD1 ILE E 10 9951 12012 8912 330 1611 -473 C ATOM 1749 N PRO E 11 53.526 30.081 49.165 1.00 76.87 N ANISOU 1749 N PRO E 11 9365 12004 7839 343 1996 -457 N ATOM 1750 CA PRO E 11 52.270 30.330 48.434 1.00 69.61 C ANISOU 1750 CA PRO E 11 8344 11177 6926 339 2068 -514 C ATOM 1751 C PRO E 11 51.841 29.115 47.608 1.00 73.15 C ANISOU 1751 C PRO E 11 8648 11586 7558 331 2018 -639 C ATOM 1752 O PRO E 11 52.668 28.526 46.913 1.00 71.97 O ANISOU 1752 O PRO E 11 8432 11432 7482 364 1926 -747 O ATOM 1753 CB PRO E 11 52.622 31.503 47.506 1.00 57.50 C ANISOU 1753 CB PRO E 11 6772 9824 5251 400 2079 -584 C ATOM 1754 CG PRO E 11 54.110 31.557 47.470 1.00 62.83 C ANISOU 1754 CG PRO E 11 7486 10493 5892 440 1989 -606 C ATOM 1755 CD PRO E 11 54.579 31.046 48.796 1.00 68.36 C ANISOU 1755 CD PRO E 11 8316 11036 6623 397 1965 -481 C ATOM 1756 N LYS E 12 50.569 28.733 47.674 1.00 76.13 N ANISOU 1756 N LYS E 12 8979 11935 8012 287 2078 -624 N ATOM 1757 CA LYS E 12 50.139 27.552 46.922 1.00 76.67 C ANISOU 1757 CA LYS E 12 8915 11960 8257 271 2030 -741 C ATOM 1758 C LYS E 12 49.295 27.806 45.668 1.00 75.02 C ANISOU 1758 C LYS E 12 8562 11890 8052 287 2054 -859 C ATOM 1759 O LYS E 12 48.501 28.744 45.597 1.00 77.80 O ANISOU 1759 O LYS E 12 8912 12346 8302 287 2140 -819 O ATOM 1760 CB LYS E 12 49.510 26.481 47.830 1.00 76.57 C ANISOU 1760 CB LYS E 12 8933 11777 8385 204 2044 -664 C ATOM 1761 CG LYS E 12 48.437 26.936 48.804 1.00 78.69 C ANISOU 1761 CG LYS E 12 9279 12016 8602 157 2155 -520 C ATOM 1762 CD LYS E 12 48.550 26.117 50.102 1.00 83.75 C ANISOU 1762 CD LYS E 12 10025 12470 9325 107 2150 -402 C ATOM 1763 CE LYS E 12 47.222 25.918 50.811 1.00 88.39 C ANISOU 1763 CE LYS E 12 10632 12990 9961 48 2244 -303 C ATOM 1764 NZ LYS E 12 46.427 24.814 50.204 1.00 91.08 N ANISOU 1764 NZ LYS E 12 10839 13284 10482 15 2223 -393 N ATOM 1765 N PHE E 13 49.499 26.944 44.680 1.00 68.47 N ANISOU 1765 N PHE E 13 7615 11058 7342 300 1976 -1005 N ATOM 1766 CA PHE E 13 48.854 27.043 43.381 1.00 63.74 C ANISOU 1766 CA PHE E 13 6873 10587 6758 316 1976 -1137 C ATOM 1767 C PHE E 13 48.260 25.680 43.099 1.00 71.22 C ANISOU 1767 C PHE E 13 7730 11433 7897 269 1938 -1209 C ATOM 1768 O PHE E 13 48.685 24.692 43.686 1.00 73.63 O ANISOU 1768 O PHE E 13 8075 11584 8315 244 1892 -1187 O ATOM 1769 CB PHE E 13 49.889 27.402 42.308 1.00 64.20 C ANISOU 1769 CB PHE E 13 6879 10755 6757 388 1909 -1263 C ATOM 1770 CG PHE E 13 50.666 28.652 42.617 1.00 71.65 C ANISOU 1770 CG PHE E 13 7918 11784 7523 435 1933 -1194 C ATOM 1771 CD1 PHE E 13 50.308 29.866 42.051 1.00 74.94 C ANISOU 1771 CD1 PHE E 13 8325 12331 7818 464 1973 -1191 C ATOM 1772 CD2 PHE E 13 51.746 28.618 43.484 1.00 76.35 C ANISOU 1772 CD2 PHE E 13 8629 12289 8092 442 1897 -1115 C ATOM 1773 CE1 PHE E 13 51.017 31.019 42.337 1.00 73.78 C ANISOU 1773 CE1 PHE E 13 8321 12127 7587 487 1931 -1080 C ATOM 1774 CE2 PHE E 13 52.460 29.773 43.778 1.00 79.78 C ANISOU 1774 CE2 PHE E 13 9153 12800 8361 480 1918 -1052 C ATOM 1775 CZ PHE E 13 52.096 30.973 43.203 1.00 75.97 C ANISOU 1775 CZ PHE E 13 8684 12382 7799 499 1929 -1032 C ATOM 1776 N THR E 14 47.289 25.604 42.200 1.00 83.67 N ANISOU 1776 N THR E 14 9185 13093 9514 255 1955 -1296 N ATOM 1777 CA THR E 14 46.533 24.360 42.062 1.00 88.19 C ANISOU 1777 CA THR E 14 9680 13565 10265 197 1933 -1345 C ATOM 1778 C THR E 14 46.289 23.814 40.646 1.00 90.51 C ANISOU 1778 C THR E 14 9822 13926 10640 203 1875 -1525 C ATOM 1779 O THR E 14 46.518 24.484 39.633 1.00 83.90 O ANISOU 1779 O THR E 14 8924 13241 9715 254 1860 -1619 O ATOM 1780 CB THR E 14 45.196 24.452 42.813 1.00 90.46 C ANISOU 1780 CB THR E 14 9983 13818 10571 134 2027 -1226 C ATOM 1781 OG1 THR E 14 44.641 25.759 42.631 1.00 88.73 O ANISOU 1781 OG1 THR E 14 9761 13753 10199 157 2107 -1181 O ATOM 1782 CG2 THR E 14 45.412 24.218 44.301 1.00 95.75 C ANISOU 1782 CG2 THR E 14 10792 14333 11254 103 2056 -1069 C ATOM 1783 N PHE E 15 45.832 22.565 40.623 1.00 99.03 N ANISOU 1783 N PHE E 15 10848 14887 11890 149 1842 -1570 N ATOM 1784 CA PHE E 15 45.473 21.835 39.412 1.00101.98 C ANISOU 1784 CA PHE E 15 11086 15293 12367 137 1786 -1734 C ATOM 1785 C PHE E 15 46.553 21.863 38.338 1.00101.62 C ANISOU 1785 C PHE E 15 10998 15321 12292 204 1708 -1880 C ATOM 1786 O PHE E 15 46.439 22.619 37.380 1.00105.71 O ANISOU 1786 O PHE E 15 11450 16002 12715 242 1712 -1957 O ATOM 1787 CB PHE E 15 44.157 22.371 38.840 1.00104.30 C ANISOU 1787 CB PHE E 15 11286 15717 12626 111 1844 -1748 C ATOM 1788 CG PHE E 15 43.418 21.373 37.996 1.00112.76 C ANISOU 1788 CG PHE E 15 12231 16770 13841 62 1801 -1873 C ATOM 1789 CD1 PHE E 15 43.578 20.011 38.212 1.00114.21 C ANISOU 1789 CD1 PHE E 15 12413 16787 14196 20 1746 -1912 C ATOM 1790 CD2 PHE E 15 42.576 21.792 36.979 1.00114.17 C ANISOU 1790 CD2 PHE E 15 12295 17099 13985 58 1813 -1951 C ATOM 1791 CE1 PHE E 15 42.904 19.088 37.437 1.00113.24 C ANISOU 1791 CE1 PHE E 15 12178 16644 14205 -29 1706 -2030 C ATOM 1792 CE2 PHE E 15 41.906 20.874 36.197 1.00113.10 C ANISOU 1792 CE2 PHE E 15 12045 16948 13979 8 1769 -2067 C ATOM 1793 CZ PHE E 15 42.071 19.519 36.427 1.00112.95 C ANISOU 1793 CZ PHE E 15 12028 16758 14128 -36 1716 -2108 C ATOM 1794 N SER E 16 47.599 21.052 38.485 1.00100.74 N ANISOU 1794 N SER E 16 10924 15092 12262 221 1639 -1917 N ATOM 1795 CA SER E 16 47.810 20.193 39.647 1.00103.53 C ANISOU 1795 CA SER E 16 11360 15253 12722 182 1634 -1819 C ATOM 1796 C SER E 16 49.214 20.401 40.217 1.00108.44 C ANISOU 1796 C SER E 16 12087 15827 13287 234 1600 -1765 C ATOM 1797 O SER E 16 49.468 21.350 40.965 1.00109.66 O ANISOU 1797 O SER E 16 12335 16018 13312 253 1645 -1643 O ATOM 1798 CB SER E 16 47.625 18.719 39.271 1.00101.66 C ANISOU 1798 CB SER E 16 11055 14892 12680 139 1576 -1921 C ATOM 1799 OG SER E 16 48.180 17.861 40.260 1.00 97.22 O ANISOU 1799 OG SER E 16 10575 14146 12218 120 1554 -1847 O TER 1800 SER E 16 HETATM 1801 C1 IPA A 101 63.719 25.441 23.753 1.00 56.36 C HETATM 1802 C2 IPA A 101 64.376 26.563 24.549 1.00 61.67 C HETATM 1803 C3 IPA A 101 65.411 25.955 25.462 1.00 59.00 C HETATM 1804 O2 IPA A 101 65.016 27.489 23.703 1.00 63.26 O HETATM 1805 C1 IPA B 101 73.366 30.616 35.220 1.00 51.45 C HETATM 1806 C2 IPA B 101 74.391 31.414 34.449 1.00 59.74 C HETATM 1807 C3 IPA B 101 74.981 32.515 35.331 1.00 54.73 C HETATM 1808 O2 IPA B 101 75.372 30.490 34.070 1.00 60.61 O HETATM 1809 C1 IPA E 101 68.294 31.077 55.390 1.00 37.20 C HETATM 1810 C2 IPA E 101 69.790 31.157 55.111 1.00 49.02 C HETATM 1811 C3 IPA E 101 70.524 32.168 56.011 1.00 48.26 C HETATM 1812 O2 IPA E 101 70.323 29.861 55.267 1.00 52.06 O HETATM 1813 O HOH A 201 62.379 19.196 28.905 1.00 64.61 O HETATM 1814 O HOH A 202 55.216 18.716 58.440 0.50 81.19 O HETATM 1815 O HOH A 203 60.084 13.947 56.920 1.00 57.01 O HETATM 1816 O HOH A 204 78.626 14.540 55.664 1.00 55.45 O HETATM 1817 O HOH A 205 74.964 19.094 37.739 1.00 50.52 O HETATM 1818 O HOH A 206 71.918 18.463 38.088 1.00 48.86 O HETATM 1819 O HOH A 207 69.234 37.017 50.787 1.00 36.70 O HETATM 1820 O HOH B 201 64.678 35.042 30.950 1.00 45.85 O CONECT 1469 1470 1471 1472 CONECT 1470 1469 CONECT 1471 1469 CONECT 1472 1469 CONECT 1565 1566 1567 1568 CONECT 1566 1565 CONECT 1567 1565 CONECT 1568 1565 CONECT 1801 1802 CONECT 1802 1801 1803 1804 CONECT 1803 1802 CONECT 1804 1802 CONECT 1805 1806 CONECT 1806 1805 1807 1808 CONECT 1807 1806 CONECT 1808 1806 CONECT 1809 1810 CONECT 1810 1809 1811 1812 CONECT 1811 1810 CONECT 1812 1810 MASTER 363 0 5 12 2 0 4 6 1815 5 20 22 END
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Related entries of code: 4ftg
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
Check Database
Protein Sequence Similarity
1bt6
RCSB PDB
PDBbind
14aa, >1BT6_2|Chains... at 100%
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
4ftg
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
Protein S100-A10 & Annexin A2 (C9S mutation)
Ligand Name
Neuroblast differentiation-associated protein AHNAK
EC.Number
E.C.-.-.-.-
Resolution
2.51(Å)
Affinity (Kd/Ki/IC50)
Kd=30nM
Release Year
2013
Protein/NA Sequence
Check fasta file
Primary Reference
(2013) Acta Crystallogr.,Sect.D Vol. 69: pp. 92-104
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):
P60903
Q09666
P07355
Entrez Gene ID
NCBI Entrez Gene ID:
6281
79026
302
ASD
Information of known allosteric effects of PDB entries
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times since Nov 2007.
Copyright ©2007-2024 涓婃捣鐩堣禌鎬濅俊鎭鎶鏈夐檺鍏徃 缃戠珯澶囨鍙凤細
娌狪CP澶2021015625鍙-3
娌叕缃戝畨澶囷細
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