Browse entries in the PDBbind-CN Database
HEADER REPLICATION/DNA 10-APR-09 3H15 TITLE CRYSTAL STRUCTURE OF REPLICATION INITIATION FACTOR MCM10-ID BOUND TO TITLE 2 SSDNA COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN MCM10 HOMOLOG; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: UNP RESIDUES 230-427, ZINC-FINGER DOMAIN, INTERNAL DOMAIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: 5'-D(*CP*CP*CP*CP*CP*CP*CP*CP*C)-3'; COMPND 8 CHAIN: B; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS; SOURCE 3 ORGANISM_COMMON: CLAWED FROG,COMMON PLATANNA,PLATANNA; SOURCE 4 ORGANISM_TAXID: 8355; SOURCE 5 GENE: MCM10; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DE3; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET32A; SOURCE 11 MOL_ID: 2; SOURCE 12 SYNTHETIC: YES KEYWDS OB-FOLD, ZINC FINGER, CCCH, DNA REPLICATION, SSDNA, DNA-BINDING, KEYWDS 2 METAL-BINDING, NUCLEUS, ZINC-FINGER, REPLICATION-DNA COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR E.M.WARREN,B.F.EICHMAN REVDAT 3 25-SEP-13 3H15 1 REMARK VERSN REVDAT 2 15-SEP-09 3H15 1 JRNL REVDAT 1 14-JUL-09 3H15 0 JRNL AUTH E.M.WARREN,H.HUANG,E.FANNING,W.J.CHAZIN,B.F.EICHMAN JRNL TITL PHYSICAL INTERACTIONS BETWEEN MCM10, DNA, AND DNA POLYMERASE JRNL TITL 2 {ALPHA}. JRNL REF J.BIOL.CHEM. V. 284 24662 2009 JRNL REFN ISSN 0021-9258 JRNL PMID 19608746 JRNL DOI 10.1074/JBC.M109.020438 REMARK 2 REMARK 2 RESOLUTION. 2.72 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.72 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.14 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 92.6 REMARK 3 NUMBER OF REFLECTIONS : 8222 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.199 REMARK 3 R VALUE (WORKING SET) : 0.197 REMARK 3 FREE R VALUE : 0.232 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.720 REMARK 3 FREE R VALUE TEST SET COUNT : 388 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 34.1403 - 3.9129 0.98 2821 141 0.1761 0.1936 REMARK 3 2 3.9129 - 3.1065 1.00 2780 142 0.1991 0.2835 REMARK 3 3 3.1065 - 2.7200 0.80 2233 105 0.2759 0.3178 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 K_SOL : 0.34 REMARK 3 B_SOL : 84.82 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.120 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 73.50 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 73.50 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 : NULL NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 6 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (chain A and resid 230:241) REMARK 3 ORIGIN FOR THE GROUP (A): 38.0938 14.0571 -12.5387 REMARK 3 T TENSOR REMARK 3 T11: 0.7732 T22: 0.7137 REMARK 3 T33: 0.3774 T12: -0.1037 REMARK 3 T13: 0.0662 T23: -0.2563 REMARK 3 L TENSOR REMARK 3 L11: 1.3060 L22: 0.8136 REMARK 3 L33: 0.8862 L12: -1.0275 REMARK 3 L13: -0.9698 L23: 0.6661 REMARK 3 S TENSOR REMARK 3 S11: 0.4114 S12: 0.3055 S13: -0.2104 REMARK 3 S21: -1.0105 S22: -0.3220 S23: 0.0632 REMARK 3 S31: -0.7942 S32: 0.0318 S33: -0.2111 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (chain A and resid 242:260) REMARK 3 ORIGIN FOR THE GROUP (A): 42.4420 16.8317 -5.8935 REMARK 3 T TENSOR REMARK 3 T11: 0.3469 T22: 0.3300 REMARK 3 T33: 0.4780 T12: 0.0387 REMARK 3 T13: -0.0726 T23: -0.1042 REMARK 3 L TENSOR REMARK 3 L11: 2.1947 L22: 2.2130 REMARK 3 L33: 0.9767 L12: 0.1964 REMARK 3 L13: 1.0142 L23: 0.0403 REMARK 3 S TENSOR REMARK 3 S11: 0.3709 S12: 0.4991 S13: -0.4978 REMARK 3 S21: 0.1263 S22: 0.2156 S23: -1.0669 REMARK 3 S31: 0.0072 S32: 0.7940 S33: -0.5073 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (chain A and resid 261:300) REMARK 3 ORIGIN FOR THE GROUP (A): 30.8085 24.7172 5.2855 REMARK 3 T TENSOR REMARK 3 T11: 0.1865 T22: 0.1992 REMARK 3 T33: 0.3095 T12: 0.0742 REMARK 3 T13: -0.0468 T23: 0.0115 REMARK 3 L TENSOR REMARK 3 L11: 2.1540 L22: 1.0239 REMARK 3 L33: 3.4440 L12: -0.9096 REMARK 3 L13: -0.5978 L23: -1.0438 REMARK 3 S TENSOR REMARK 3 S11: 0.0390 S12: -0.0111 S13: -0.2570 REMARK 3 S21: 0.1474 S22: 0.2135 S23: 0.1304 REMARK 3 S31: -0.0454 S32: -0.0259 S33: -0.2422 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (chain A and resid 301:371) REMARK 3 ORIGIN FOR THE GROUP (A): 34.2679 32.2085 2.0463 REMARK 3 T TENSOR REMARK 3 T11: 0.1231 T22: 0.2894 REMARK 3 T33: 0.1860 T12: 0.0649 REMARK 3 T13: -0.0084 T23: -0.1208 REMARK 3 L TENSOR REMARK 3 L11: 1.8291 L22: 3.0886 REMARK 3 L33: 2.1696 L12: -0.2717 REMARK 3 L13: -0.0112 L23: 0.3192 REMARK 3 S TENSOR REMARK 3 S11: 0.0813 S12: -0.3878 S13: 0.2198 REMARK 3 S21: 0.0936 S22: 0.1624 S23: 0.2002 REMARK 3 S31: -0.1285 S32: -0.0411 S33: 0.1444 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: (chain A and resid 372:500) REMARK 3 ORIGIN FOR THE GROUP (A): 22.2125 25.9130 -17.8934 REMARK 3 T TENSOR REMARK 3 T11: 0.4646 T22: 0.6299 REMARK 3 T33: 0.3588 T12: 0.1003 REMARK 3 T13: -0.1584 T23: -0.1606 REMARK 3 L TENSOR REMARK 3 L11: 3.3915 L22: 1.4118 REMARK 3 L33: 0.0460 L12: 0.4014 REMARK 3 L13: -0.4295 L23: -0.2874 REMARK 3 S TENSOR REMARK 3 S11: -0.0798 S12: 1.1121 S13: -0.1807 REMARK 3 S21: -0.2693 S22: 0.1182 S23: -0.1810 REMARK 3 S31: -0.3485 S32: -0.2038 S33: -0.0296 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: (chain B and resid 9:14) REMARK 3 ORIGIN FOR THE GROUP (A): 31.4141 41.9531 8.8052 REMARK 3 T TENSOR REMARK 3 T11: 1.2883 T22: 1.1590 REMARK 3 T33: 1.4063 T12: 0.5913 REMARK 3 T13: 0.6995 T23: -0.2553 REMARK 3 L TENSOR REMARK 3 L11: 5.1447 L22: 0.7766 REMARK 3 L33: 8.2020 L12: 0.7658 REMARK 3 L13: -5.4745 L23: 0.4387 REMARK 3 S TENSOR REMARK 3 S11: 0.7788 S12: -1.4481 S13: 1.5889 REMARK 3 S21: 0.3654 S22: 0.4778 S23: 0.1779 REMARK 3 S31: -1.8573 S32: 0.8093 S33: -1.3955 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 3H15 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-09. REMARK 100 THE RCSB ID CODE IS RCSB052560. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 07-JAN-08; 09-APR-07 REMARK 200 TEMPERATURE (KELVIN) : 100; 100 REMARK 200 PH : 9.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y; Y REMARK 200 RADIATION SOURCE : APS; NSLS REMARK 200 BEAMLINE : 21-ID-D; X29A REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97857; 1.00 REMARK 200 MONOCHROMATOR : SI(111); SI(111) REMARK 200 OPTICS : BE LENSES/DIAMOND LAUE MONO; REMARK 200 SI(111) DOUBLE CRYSTAL REMARK 200 MONOCHROMETER REMARK 200 REMARK 200 DETECTOR TYPE : CCD; CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD; ADSC REMARK 200 QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8222 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.720 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 (%) : 92.6 REMARK 200 DATA REDUNDANCY : 5.300 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.08200 REMARK 200
FOR THE DATA SET : 11.3800 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.72 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85 REMARK 200 COMPLETENESS FOR SHELL (%) : 51.4 REMARK 200 DATA REDUNDANCY IN SHELL : 2.10 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.30500 REMARK 200
FOR SHELL : 1.550 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: PDB ENTRY 3EBE REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 61.26 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TAPS PH 9.0, 17% PEG 3350 , REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+2/3 REMARK 290 6555 -X,-X+Y,-Z+1/3 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 20.38633 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 40.77267 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 40.77267 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 20.38633 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 460 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 10940 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 SER A 230 REMARK 465 PRO A 231 REMARK 465 VAL A 232 REMARK 465 GLY A 233 REMARK 465 GLN A 234 REMARK 465 GLN A 408 REMARK 465 ALA A 409 REMARK 465 GLN A 410 REMARK 465 TYR A 411 REMARK 465 LYS A 412 REMARK 465 LYS A 413 REMARK 465 VAL A 414 REMARK 465 SER A 415 REMARK 465 SER A 416 REMARK 465 LYS A 417 REMARK 465 ARG A 418 REMARK 465 ALA A 419 REMARK 465 ASP A 420 REMARK 465 LEU A 421 REMARK 465 GLN A 422 REMARK 465 SER A 423 REMARK 465 SER A 424 REMARK 465 TYR A 425 REMARK 465 SER A 426 REMARK 465 GLY A 427 REMARK 465 DC B 12 REMARK 465 DC B 13 REMARK 465 DC B 14 REMARK 465 DC B 15 REMARK 465 DC B 16 REMARK 465 DC B 17 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 279 CE NZ REMARK 470 LYS A 353 CD CE NZ REMARK 470 ASN A 387 CG OD1 ND2 REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 HIS A 237 CG REMARK 480 MET A 260 CE 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 DC B 10 C4' - C3' - C2' ANGL. DEV. = -4.5 DEGREES REMARK 500 DC B 10 O4' - C1' - N1 ANGL. DEV. = 1.9 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 HIS A 237 148.19 1.46 REMARK 500 THR A 277 6.61 -69.54 REMARK 500 LYS A 279 46.86 -153.62 REMARK 500 PRO A 297 -164.19 -79.01 REMARK 500 SER A 299 -75.22 -156.30 REMARK 500 SER A 300 13.77 54.35 REMARK 500 ASN A 301 89.59 -59.12 REMARK 500 ASN A 302 -20.63 86.46 REMARK 500 LYS A 304 89.06 155.38 REMARK 500 LEU A 314 8.58 58.44 REMARK 500 LEU A 317 -4.38 -57.37 REMARK 500 LYS A 331 -38.77 -36.85 REMARK 500 ASN A 365 128.02 -173.67 REMARK 500 LYS A 385 103.49 -54.54 REMARK 500 LYS A 386 67.54 -36.83 REMARK 500 ASN A 387 -73.35 -178.97 REMARK 500 ASP A 389 150.71 3.86 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 HIS A 237 21.6 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 510 DISTANCE = 19.88 ANGSTROMS REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 500 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 381 SG REMARK 620 2 CYS A 391 SG 107.4 REMARK 620 3 CYS A 403 SG 100.7 121.1 REMARK 620 4 HIS A 406 ND1 91.4 122.0 107.5 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 500 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3EBE RELATED DB: PDB REMARK 900 UNLIGANDED FORM OF MCM10-ID DBREF 3H15 A 230 427 UNP Q5EAW4 MCM10_XENLA 230 427 DBREF 3H15 B 9 17 PDB 3H15 3H15 9 17 SEQRES 1 A 198 SER PRO VAL GLY GLN GLN TYR HIS VAL GLU LYS PHE SER SEQRES 2 A 198 GLY LEU ARG ILE ARG LYS PRO ARG VAL SER SER SER GLU SEQRES 3 A 198 MET GLU ARG LYS MET ASN GLY ARG LYS LEU ILE ARG LEU SEQRES 4 A 198 ALA GLN LEU GLN ASN LYS ILE ALA THR GLU LYS LEU GLU SEQRES 5 A 198 GLU GLU ASP TRP VAL THR PHE GLY VAL ILE VAL LYS LYS SEQRES 6 A 198 ILE THR PRO GLN SER SER ASN ASN GLY LYS THR PHE SER SEQRES 7 A 198 ILE TRP ARG LEU ASN ASP LEU LYS ASP LEU ASP LYS TYR SEQRES 8 A 198 ILE SER LEU PHE LEU PHE GLY ASP VAL HIS LYS GLU HIS SEQRES 9 A 198 TRP LYS THR ASP GLN GLY THR VAL ILE GLY LEU LEU ASN SEQRES 10 A 198 ALA ASN PRO MET LYS PRO LYS GLU GLY THR ASP GLU VAL SEQRES 11 A 198 CYS LEU SER VAL ASP ASN PRO GLN LYS VAL LEU LEU MET SEQRES 12 A 198 GLY ASP ALA VAL ASP LEU GLY THR CYS LYS ALA ARG LYS SEQRES 13 A 198 LYS ASN GLY ASP PRO CYS THR GLN MET VAL ASN LEU ASN SEQRES 14 A 198 ASP CYS GLU TYR CYS GLN TYR HIS VAL GLN ALA GLN TYR SEQRES 15 A 198 LYS LYS VAL SER SER LYS ARG ALA ASP LEU GLN SER SER SEQRES 16 A 198 TYR SER GLY SEQRES 1 B 9 DC DC DC DC DC DC DC DC DC HET ZN A 500 1 HETNAM ZN ZINC ION FORMUL 3 ZN ZN 2+ FORMUL 4 HOH *15(H2 O) HELIX 1 1 SER A 252 ASN A 261 1 10 HELIX 2 2 ARG A 267 ALA A 269 5 3 HELIX 3 3 GLN A 270 THR A 277 1 8 HELIX 4 4 PHE A 326 TRP A 334 1 9 HELIX 5 5 ASN A 365 GLN A 367 5 3 SHEET 1 A 5 ILE A 246 ARG A 247 0 SHEET 2 A 5 VAL A 369 ALA A 375 -1 O ASP A 374 N ARG A 247 SHEET 3 A 5 THR A 340 LEU A 345 -1 N VAL A 341 O GLY A 373 SHEET 4 A 5 TRP A 285 ILE A 295 -1 N GLY A 289 O ILE A 342 SHEET 5 A 5 LYS A 264 LEU A 265 1 N LYS A 264 O VAL A 286 SHEET 1 B 8 ILE A 246 ARG A 247 0 SHEET 2 B 8 VAL A 369 ALA A 375 -1 O ASP A 374 N ARG A 247 SHEET 3 B 8 THR A 340 LEU A 345 -1 N VAL A 341 O GLY A 373 SHEET 4 B 8 TRP A 285 ILE A 295 -1 N GLY A 289 O ILE A 342 SHEET 5 B 8 SER A 307 ASN A 312 -1 O ILE A 308 N ILE A 295 SHEET 6 B 8 ILE A 321 LEU A 325 -1 O ILE A 321 N LEU A 311 SHEET 7 B 8 CYS A 360 SER A 362 1 O LEU A 361 N PHE A 324 SHEET 8 B 8 ASN A 348 PRO A 349 -1 N ASN A 348 O SER A 362 SHEET 1 C 2 LEU A 378 THR A 380 0 SHEET 2 C 2 MET A 394 ASN A 396 -1 O VAL A 395 N GLY A 379 LINK SG CYS A 381 ZN ZN A 500 1555 1555 2.43 LINK SG CYS A 391 ZN ZN A 500 1555 1555 2.40 LINK SG CYS A 403 ZN ZN A 500 1555 1555 2.43 LINK ND1 HIS A 406 ZN ZN A 500 1555 1555 2.45 CISPEP 1 GLY A 303 LYS A 304 0 -7.20 SITE 1 AC1 4 CYS A 381 CYS A 391 CYS A 403 HIS A 406 CRYST1 95.017 95.017 61.159 90.00 90.00 120.00 P 31 2 1 6 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.010524 0.006076 0.000000 0.00000 SCALE2 0.000000 0.012153 0.000000 0.00000 SCALE3 0.000000 0.000000 0.016351 0.00000 ATOM 1 N GLN A 235 41.074 18.463 -17.133 1.00143.72 N ANISOU 1 N GLN A 235 21626 18552 14431 -824 1704 -2310 N ATOM 2 CA GLN A 235 39.903 18.827 -17.926 1.00 76.03 C ANISOU 2 CA GLN A 235 13312 9918 5656 -501 1528 -2333 C ATOM 3 C GLN A 235 39.115 17.586 -18.327 1.00 90.68 C ANISOU 3 C GLN A 235 14974 11889 7589 -314 1210 -2459 C ATOM 4 O GLN A 235 38.137 17.676 -19.066 1.00105.54 O ANISOU 4 O GLN A 235 17029 13756 9315 -26 1028 -2514 O ATOM 5 CB GLN A 235 40.330 19.622 -19.158 1.00 75.69 C ANISOU 5 CB GLN A 235 13721 9737 5299 -349 1739 -2273 C ATOM 6 CG GLN A 235 39.212 20.326 -19.890 1.00 68.76 C ANISOU 6 CG GLN A 235 13171 8784 4173 -16 1621 -2268 C ATOM 7 CD GLN A 235 39.740 21.452 -20.760 1.00127.62 C ANISOU 7 CD GLN A 235 21084 16069 11335 77 1918 -2161 C ATOM 8 OE1 GLN A 235 40.940 21.730 -20.768 1.00120.88 O ANISOU 8 OE1 GLN A 235 20293 15147 10487 -129 2218 -2097 O ATOM 9 NE2 GLN A 235 38.848 22.108 -21.494 1.00165.05 N ANISOU 9 NE2 GLN A 235 26148 20740 15822 394 1846 -2143 N ATOM 10 N TYR A 236 39.559 16.429 -17.838 1.00110.00 N ANISOU 10 N TYR A 236 17059 14454 10281 -475 1152 -2512 N ATOM 11 CA ATYR A 236 38.815 15.201 -18.075 0.72114.05 C ANISOU 11 CA ATYR A 236 17342 15070 10921 -331 864 -2642 C ATOM 12 CA BTYR A 236 38.915 15.145 -18.106 0.28112.66 C ANISOU 12 CA BTYR A 236 17161 14897 10747 -341 876 -2642 C ATOM 13 C TYR A 236 38.657 14.362 -16.821 1.00100.27 C ANISOU 13 C TYR A 236 15151 13433 9515 -513 752 -2670 C ATOM 14 O TYR A 236 39.205 14.686 -15.772 1.00 86.50 O ANISOU 14 O TYR A 236 13267 11703 7897 -751 895 -2589 O ATOM 15 CB ATYR A 236 39.384 14.429 -19.268 0.72116.39 C ANISOU 15 CB ATYR A 236 17719 15390 11113 -227 879 -2706 C ATOM 16 CB BTYR A 236 39.754 14.308 -19.076 0.28116.88 C ANISOU 16 CB BTYR A 236 17718 15464 11227 -317 938 -2689 C ATOM 17 CG ATYR A 236 39.131 15.210 -20.527 0.72107.75 C ANISOU 17 CG ATYR A 236 17062 14202 9675 42 913 -2696 C ATOM 18 CG BTYR A 236 41.151 13.997 -18.579 0.28110.94 C ANISOU 18 CG BTYR A 236 16804 14746 10602 -611 1174 -2626 C ATOM 19 CD1ATYR A 236 40.155 15.898 -21.165 0.72 99.40 C ANISOU 19 CD1ATYR A 236 16310 13049 8407 4 1203 -2599 C ATOM 20 CD1BTYR A 236 41.405 12.857 -17.823 0.28105.52 C ANISOU 20 CD1BTYR A 236 15714 14179 10201 -769 1103 -2668 C ATOM 21 CD2ATYR A 236 37.843 15.323 -21.036 0.72 95.30 C ANISOU 21 CD2ATYR A 236 15597 12631 7981 341 667 -2781 C ATOM 22 CD2BTYR A 236 42.220 14.835 -18.880 0.28 82.09 C ANISOU 22 CD2BTYR A 236 13400 11005 6785 -723 1477 -2530 C ATOM 23 CE1ATYR A 236 39.911 16.640 -22.304 0.72 85.25 C ANISOU 23 CE1ATYR A 236 14933 11166 6292 271 1253 -2575 C ATOM 24 CE1BTYR A 236 42.683 12.565 -17.374 0.28 95.07 C ANISOU 24 CE1BTYR A 236 14238 12902 8980 -1021 1313 -2616 C ATOM 25 CE2ATYR A 236 37.590 16.062 -22.167 0.72 99.60 C ANISOU 25 CE2ATYR A 236 16548 13101 8193 614 701 -2766 C ATOM 26 CE2BTYR A 236 43.501 14.548 -18.436 0.28 93.14 C ANISOU 26 CE2BTYR A 236 14639 12447 8301 -989 1688 -2490 C ATOM 27 CZ ATYR A 236 38.626 16.719 -22.799 0.72 97.62 C ANISOU 27 CZ ATYR A 236 16607 12751 7731 583 998 -2656 C ATOM 28 CZ BTYR A 236 43.727 13.413 -17.684 0.28100.46 C ANISOU 28 CZ BTYR A 236 15163 13510 9496 -1132 1598 -2534 C ATOM 29 OH ATYR A 236 38.375 17.461 -23.931 0.72 78.38 O ANISOU 29 OH ATYR A 236 14589 10237 4955 875 1049 -2628 O ATOM 30 OH BTYR A 236 45.000 13.123 -17.240 0.28 59.59 O ANISOU 30 OH BTYR A 236 9824 8394 4425 -1380 1803 -2499 O ATOM 31 N HIS A 237 37.885 13.292 -16.958 1.00117.71 N ANISOU 31 N HIS A 237 17142 15717 11866 -386 499 -2792 N ATOM 32 CA HIS A 237 37.221 12.597 -15.850 0.74131.45 C ANISOU 32 CA HIS A 237 18500 17535 13910 -462 331 -2832 C ATOM 33 C HIS A 237 37.340 13.081 -14.398 1.00121.31 C ANISOU 33 C HIS A 237 17038 16267 12789 -683 419 -2729 C ATOM 34 O HIS A 237 38.341 13.618 -13.949 1.00103.34 O ANISOU 34 O HIS A 237 14796 13981 10486 -885 651 -2630 O ATOM 35 CB HIS A 237 37.321 11.074 -15.920 1.00135.47 C ANISOU 35 CB HIS A 237 18693 18135 14645 -476 221 -2934 C ATOM 36 CG HIS A 237 36.117 10.391 -15.338 0.00139.84 C ANISOU 36 CG HIS A 237 18961 18732 15439 -399 -29 -3029 C ATOM 37 ND1 HIS A 237 34.834 10.822 -15.588 0.92169.99 N ANISOU 37 ND1 HIS A 237 22888 22517 19184 -185 -232 -3103 N ATOM 38 CD2 HIS A 237 36.005 9.336 -14.497 1.00114.34 C ANISOU 38 CD2 HIS A 237 15345 15573 12527 -504 -94 -3059 C ATOM 39 CE1 HIS A 237 33.976 10.051 -14.939 0.70152.80 C ANISOU 39 CE1 HIS A 237 20396 20384 17278 -172 -415 -3185 C ATOM 40 NE2 HIS A 237 34.661 9.143 -14.271 0.65139.63 N ANISOU 40 NE2 HIS A 237 18429 18773 15852 -362 -328 -3154 N ATOM 41 N VAL A 238 36.247 12.822 -13.691 1.00 89.87 N ANISOU 41 N VAL A 238 12847 12316 8983 -629 215 -2772 N ATOM 42 CA VAL A 238 35.880 13.397 -12.405 1.00 65.71 C ANISOU 42 CA VAL A 238 9656 9263 6047 -748 221 -2696 C ATOM 43 C VAL A 238 36.907 13.240 -11.289 1.00 74.10 C ANISOU 43 C VAL A 238 10480 10397 7278 -1026 406 -2606 C ATOM 44 O VAL A 238 37.660 12.273 -11.256 1.00 99.84 O ANISOU 44 O VAL A 238 13539 13732 10665 -1123 463 -2621 O ATOM 45 CB VAL A 238 34.557 12.773 -11.955 1.00 63.83 C ANISOU 45 CB VAL A 238 9179 9059 6013 -628 -46 -2783 C ATOM 46 CG1 VAL A 238 34.245 13.130 -10.520 1.00 78.20 C ANISOU 46 CG1 VAL A 238 10800 10907 8007 -764 -41 -2704 C ATOM 47 CG2 VAL A 238 33.440 13.207 -12.875 1.00 66.28 C ANISOU 47 CG2 VAL A 238 9735 9308 6139 -352 -231 -2872 C ATOM 48 N GLU A 239 36.908 14.204 -10.368 1.00 73.68 N ANISOU 48 N GLU A 239 10447 10329 7221 -1143 495 -2519 N ATOM 49 CA GLU A 239 37.669 14.133 -9.120 1.00 75.65 C ANISOU 49 CA GLU A 239 10437 10668 7640 -1383 634 -2448 C ATOM 50 C GLU A 239 36.839 13.424 -8.050 1.00 84.73 C ANISOU 50 C GLU A 239 11237 11897 9060 -1376 461 -2460 C ATOM 51 O GLU A 239 35.674 13.763 -7.828 1.00 74.96 O ANISOU 51 O GLU A 239 10023 10618 7841 -1255 296 -2477 O ATOM 52 CB GLU A 239 38.035 15.542 -8.632 1.00 50.53 C ANISOU 52 CB GLU A 239 7439 7433 4328 -1507 813 -2365 C ATOM 53 CG GLU A 239 39.158 15.608 -7.591 1.00 75.90 C ANISOU 53 CG GLU A 239 10444 10744 7650 -1767 1013 -2310 C ATOM 54 CD GLU A 239 38.708 15.291 -6.172 1.00 85.69 C ANISOU 54 CD GLU A 239 11343 12093 9124 -1835 920 -2285 C ATOM 55 OE1 GLU A 239 37.772 15.953 -5.666 1.00 87.62 O ANISOU 55 OE1 GLU A 239 11626 12295 9371 -1777 821 -2266 O ATOM 56 OE2 GLU A 239 39.315 14.391 -5.552 1.00102.65 O ANISOU 56 OE2 GLU A 239 13188 14370 11445 -1941 957 -2280 O ATOM 57 N LYS A 240 37.454 12.459 -7.376 1.00 83.71 N ANISOU 57 N LYS A 240 10788 11882 9137 -1502 510 -2446 N ATOM 58 CA LYS A 240 36.746 11.582 -6.445 1.00 64.79 C ANISOU 58 CA LYS A 240 8046 9557 7015 -1482 368 -2454 C ATOM 59 C LYS A 240 35.877 12.296 -5.412 1.00 64.11 C ANISOU 59 C LYS A 240 7905 9464 6991 -1479 291 -2408 C ATOM 60 O LYS A 240 34.719 11.937 -5.222 1.00 80.69 O ANISOU 60 O LYS A 240 9896 11543 9220 -1350 100 -2450 O ATOM 61 CB LYS A 240 37.733 10.646 -5.731 1.00 74.80 C ANISOU 61 CB LYS A 240 9002 10954 8463 -1634 491 -2414 C ATOM 62 CG LYS A 240 37.081 9.583 -4.843 1.00 81.55 C ANISOU 62 CG LYS A 240 9496 11876 9614 -1598 373 -2414 C ATOM 63 CD LYS A 240 38.076 8.998 -3.847 1.00 92.23 C ANISOU 63 CD LYS A 240 10560 13372 11110 -1754 526 -2339 C ATOM 64 CE LYS A 240 37.445 7.884 -3.025 1.00110.38 C ANISOU 64 CE LYS A 240 12513 15723 13702 -1698 433 -2329 C ATOM 65 NZ LYS A 240 38.441 7.273 -2.103 1.00104.67 N ANISOU 65 NZ LYS A 240 11519 15151 13101 -1820 589 -2251 N ATOM 66 N PHE A 241 36.434 13.294 -4.734 1.00 82.95 N ANISOU 66 N PHE A 241 10354 11870 9294 -1623 444 -2330 N ATOM 67 CA PHE A 241 35.784 13.846 -3.547 1.00 67.99 C ANISOU 67 CA PHE A 241 8343 9999 7490 -1652 394 -2278 C ATOM 68 C PHE A 241 34.725 14.920 -3.795 1.00 76.23 C ANISOU 68 C PHE A 241 9645 10925 8394 -1529 285 -2285 C ATOM 69 O PHE A 241 33.745 15.017 -3.057 1.00 79.89 O ANISOU 69 O PHE A 241 9991 11392 8972 -1471 152 -2274 O ATOM 70 CB PHE A 241 36.838 14.339 -2.564 1.00 62.98 C ANISOU 70 CB PHE A 241 7604 9463 6860 -1863 597 -2207 C ATOM 71 CG PHE A 241 37.526 13.231 -1.832 1.00 92.79 C ANISOU 71 CG PHE A 241 11029 13392 10835 -1953 654 -2185 C ATOM 72 CD1 PHE A 241 36.849 12.506 -0.857 1.00 79.41 C ANISOU 72 CD1 PHE A 241 9030 11770 9372 -1906 540 -2159 C ATOM 73 CD2 PHE A 241 38.838 12.897 -2.125 1.00 68.69 C ANISOU 73 CD2 PHE A 241 7953 10408 7739 -2074 828 -2187 C ATOM 74 CE1 PHE A 241 37.472 11.470 -0.178 1.00 49.66 C ANISOU 74 CE1 PHE A 241 4946 8141 5781 -1966 605 -2127 C ATOM 75 CE2 PHE A 241 39.471 11.868 -1.451 1.00 77.65 C ANISOU 75 CE2 PHE A 241 8766 11691 9046 -2140 882 -2163 C ATOM 76 CZ PHE A 241 38.785 11.151 -0.477 1.00 90.42 C ANISOU 76 CZ PHE A 241 10088 13380 10886 -2080 773 -2129 C ATOM 77 N SER A 242 34.919 15.720 -4.834 1.00 60.35 N ANISOU 77 N SER A 242 8728 6453 7749 472 -893 29 N ATOM 78 CA SER A 242 34.005 16.815 -5.122 1.00 65.09 C ANISOU 78 CA SER A 242 9514 7090 8128 356 -643 193 C ATOM 79 C SER A 242 32.981 16.430 -6.184 1.00 84.22 C ANISOU 79 C SER A 242 12004 9524 10472 428 -550 224 C ATOM 80 O SER A 242 31.930 17.068 -6.303 1.00 85.54 O ANISOU 80 O SER A 242 12356 9666 10477 359 -409 397 O ATOM 81 CB SER A 242 34.792 18.033 -5.599 1.00 70.28 C ANISOU 81 CB SER A 242 10072 7905 8726 231 -402 120 C ATOM 82 OG SER A 242 35.309 17.792 -6.896 1.00 57.54 O ANISOU 82 OG SER A 242 8267 6447 7149 290 -275 -63 O ATOM 83 N GLY A 243 33.301 15.396 -6.962 1.00 60.85 N ANISOU 83 N GLY A 243 8888 6598 7636 569 -636 46 N ATOM 84 CA GLY A 243 32.434 14.949 -8.041 1.00 54.25 C ANISOU 84 CA GLY A 243 8100 5777 6737 650 -572 40 C ATOM 85 C GLY A 243 32.412 15.887 -9.235 1.00 63.17 C ANISOU 85 C GLY A 243 9218 7086 7698 575 -267 6 C ATOM 86 O GLY A 243 31.460 15.901 -10.019 1.00 83.09 O ANISOU 86 O GLY A 243 11852 9613 10104 591 -176 74 O ATOM 87 N LEU A 244 33.469 16.677 -9.367 1.00 47.05 N ANISOU 87 N LEU A 244 7040 5188 5649 485 -118 -92 N ATOM 88 CA LEU A 244 33.570 17.672 -10.421 1.00 83.12 C ANISOU 88 CA LEU A 244 11591 9935 10057 385 176 -103 C ATOM 89 C LEU A 244 34.799 17.348 -11.243 1.00 63.51 C ANISOU 89 C LEU A 244 8838 7638 7656 442 246 -368 C ATOM 90 O LEU A 244 35.776 16.843 -10.707 1.00 74.62 O ANISOU 90 O LEU A 244 10068 9035 9250 497 102 -512 O ATOM 91 CB LEU A 244 33.702 19.076 -9.812 1.00 48.61 C ANISOU 91 CB LEU A 244 7303 5570 5598 197 317 46 C ATOM 92 CG LEU A 244 32.428 19.896 -9.553 1.00 82.42 C ANISOU 92 CG LEU A 244 11847 9749 9719 102 401 299 C ATOM 93 CD1 LEU A 244 31.257 19.026 -9.106 1.00 55.36 C ANISOU 93 CD1 LEU A 244 8577 6148 6308 205 221 414 C ATOM 94 CD2 LEU A 244 32.683 21.023 -8.550 1.00 68.26 C ANISOU 94 CD2 LEU A 244 10123 7907 7904 -48 443 411 C ATOM 95 N ARG A 245 34.772 17.623 -12.540 1.00 52.06 N ANISOU 95 N ARG A 245 7350 6362 6069 429 463 -437 N ATOM 96 CA ARG A 245 35.996 17.437 -13.298 1.00 70.23 C ANISOU 96 CA ARG A 245 9383 8868 8431 466 569 -689 C ATOM 97 C ARG A 245 36.772 18.753 -13.452 1.00 72.00 C ANISOU 97 C ARG A 245 9524 9251 8582 277 817 -652 C ATOM 98 O ARG A 245 36.214 19.791 -13.789 1.00 87.26 O ANISOU 98 O ARG A 245 11607 11219 10329 134 1001 -474 O ATOM 99 CB ARG A 245 35.763 16.669 -14.607 0.79 58.64 C ANISOU 99 CB ARG A 245 7869 7520 6893 600 625 -855 C ATOM 100 CG ARG A 245 34.948 17.356 -15.648 1.00 61.19 C ANISOU 100 CG ARG A 245 8352 7945 6954 517 846 -736 C ATOM 101 CD ARG A 245 34.328 16.322 -16.572 1.00 76.56 C ANISOU 101 CD ARG A 245 10334 9900 8854 684 774 -858 C ATOM 102 NE ARG A 245 33.653 16.943 -17.705 1.00 71.59 N ANISOU 102 NE ARG A 245 9842 9396 7963 609 985 -770 N ATOM 103 CZ ARG A 245 34.144 16.971 -18.939 1.00 79.44 C ANISOU 103 CZ ARG A 245 10730 10635 8819 620 1178 -937 C ATOM 104 NH1 ARG A 245 33.462 17.564 -19.906 1.00 98.43 N ANISOU 104 NH1 ARG A 245 13288 13138 10974 540 1346 -825 N ATOM 105 NH2 ARG A 245 35.310 16.397 -19.208 1.00108.63 N ANISOU 105 NH2 ARG A 245 14166 14481 12629 713 1200 -1217 N ATOM 106 N ILE A 246 38.068 18.692 -13.169 1.00 67.05 N ANISOU 106 N ILE A 246 8648 8703 8124 275 801 -818 N ATOM 107 CA ILE A 246 38.863 19.887 -12.956 1.00 59.41 C ANISOU 107 CA ILE A 246 7593 7827 7152 89 965 -764 C ATOM 108 C ILE A 246 39.945 20.122 -14.012 1.00 41.29 C ANISOU 108 C ILE A 246 5034 5804 4851 53 1203 -946 C ATOM 109 O ILE A 246 40.861 19.321 -14.170 1.00 73.62 O ANISOU 109 O ILE A 246 8876 9981 9114 173 1145 -1190 O ATOM 110 CB ILE A 246 39.517 19.828 -11.559 1.00 58.27 C ANISOU 110 CB ILE A 246 7382 7537 7221 78 743 -768 C ATOM 111 CG1 ILE A 246 38.430 19.934 -10.488 1.00 59.95 C ANISOU 111 CG1 ILE A 246 7883 7513 7384 59 572 -543 C ATOM 112 CG2 ILE A 246 40.574 20.924 -11.395 1.00 78.99 C ANISOU 112 CG2 ILE A 246 9852 10266 9894 -97 888 -769 C ATOM 113 CD1 ILE A 246 38.776 19.258 -9.171 1.00 69.02 C ANISOU 113 CD1 ILE A 246 9006 8488 8729 132 265 -571 C ATOM 114 N ARG A 247 39.838 21.234 -14.731 1.00 76.84 N ANISOU 114 N ARG A 247 9589 10445 9161 -117 1473 -824 N ATOM 115 CA ARG A 247 40.897 21.623 -15.653 1.00 70.59 C ANISOU 115 CA ARG A 247 8549 9923 8351 -192 1724 -958 C ATOM 116 C ARG A 247 42.121 22.026 -14.850 1.00 69.77 C ANISOU 116 C ARG A 247 8221 9818 8469 -277 1686 -1015 C ATOM 117 O ARG A 247 42.033 22.845 -13.933 1.00 67.63 O ANISOU 117 O ARG A 247 8059 9404 8233 -410 1621 -842 O ATOM 118 CB ARG A 247 40.451 22.765 -16.574 1.00 73.61 C ANISOU 118 CB ARG A 247 9059 10438 8470 -375 2006 -775 C ATOM 119 CG ARG A 247 41.601 23.534 -17.215 1.00 64.62 C ANISOU 119 CG ARG A 247 7679 9549 7324 -529 2271 -828 C ATOM 120 CD ARG A 247 41.136 24.421 -18.368 1.00 82.08 C ANISOU 120 CD ARG A 247 10012 11924 9252 -683 2548 -670 C ATOM 121 NE ARG A 247 40.081 25.352 -17.972 1.00138.73 N ANISOU 121 NE ARG A 247 17487 18912 16314 -811 2518 -376 N ATOM 122 CZ ARG A 247 38.805 25.241 -18.337 1.00132.39 C ANISOU 122 CZ ARG A 247 16948 18023 15332 -765 2486 -251 C ATOM 123 NH1 ARG A 247 38.419 24.238 -19.117 1.00101.42 N ANISOU 123 NH1 ARG A 247 13040 14184 11313 -598 2472 -390 N ATOM 124 NH2 ARG A 247 37.915 26.137 -17.925 1.00 99.49 N ANISOU 124 NH2 ARG A 247 13026 13683 11094 -883 2462 6 N ATOM 125 N LYS A 248 43.257 21.424 -15.188 1.00 89.61 N ANISOU 125 N LYS A 248 10419 12487 11142 -192 1714 -1271 N ATOM 126 CA LYS A 248 44.527 21.726 -14.531 1.00 75.20 C ANISOU 126 CA LYS A 248 8335 10680 9558 -263 1677 -1355 C ATOM 127 C LYS A 248 44.456 21.618 -13.007 1.00 83.01 C ANISOU 127 C LYS A 248 9419 11395 10726 -247 1360 -1277 C ATOM 128 O LYS A 248 44.533 22.624 -12.291 1.00 72.78 O ANISOU 128 O LYS A 248 8204 10010 9439 -417 1352 -1109 O ATOM 129 CB LYS A 248 45.059 23.084 -14.996 1.00 45.90 C ANISOU 129 CB LYS A 248 4544 7136 5759 -507 1963 -1238 C ATOM 130 CG LYS A 248 45.781 22.974 -16.330 1.00 89.44 C ANISOU 130 CG LYS A 248 9806 12970 11209 -506 2252 -1411 C ATOM 131 CD LYS A 248 45.720 24.235 -17.171 1.00 71.76 C ANISOU 131 CD LYS A 248 7615 10905 8745 -740 2571 -1226 C ATOM 132 CE LYS A 248 46.009 23.883 -18.628 1.00113.97 C ANISOU 132 CE LYS A 248 12810 16566 13928 -696 2847 -1384 C ATOM 133 NZ LYS A 248 47.055 22.806 -18.754 1.00 90.48 N ANISOU 133 NZ LYS A 248 9490 13717 11172 -512 2812 -1724 N ATOM 134 N PRO A 249 44.299 20.380 -12.511 1.00 68.54 N ANISOU 134 N PRO A 249 7585 9424 9032 -43 1088 -1398 N ATOM 135 CA PRO A 249 44.222 20.078 -11.084 1.00 75.64 C ANISOU 135 CA PRO A 249 8576 10071 10091 -7 764 -1335 C ATOM 136 C PRO A 249 45.478 20.537 -10.375 1.00 68.57 C ANISOU 136 C PRO A 249 7454 9180 9419 -100 701 -1397 C ATOM 137 O PRO A 249 46.539 20.633 -10.983 1.00 81.67 O ANISOU 137 O PRO A 249 8812 11028 11191 -121 852 -1564 O ATOM 138 CB PRO A 249 44.141 18.554 -11.059 1.00 47.62 C ANISOU 138 CB PRO A 249 4963 6447 6684 237 531 -1515 C ATOM 139 CG PRO A 249 43.548 18.206 -12.345 1.00 65.80 C ANISOU 139 CG PRO A 249 7303 8890 8806 315 717 -1578 C ATOM 140 CD PRO A 249 44.113 19.171 -13.322 1.00 48.80 C ANISOU 140 CD PRO A 249 5013 6996 6532 166 1068 -1597 C ATOM 141 N ARG A 250 45.340 20.781 -9.083 1.00 61.04 N ANISOU 141 N ARG A 250 6645 8018 8529 -151 471 -1268 N ATOM 142 CA ARG A 250 46.366 21.428 -8.297 1.00 67.27 C ANISOU 142 CA ARG A 250 7285 8778 9495 -273 397 -1278 C ATOM 143 C ARG A 250 46.830 20.516 -7.158 1.00 65.37 C ANISOU 143 C ARG A 250 6979 8361 9498 -148 23 -1370 C ATOM 144 O ARG A 250 47.808 20.824 -6.470 1.00 63.57 O ANISOU 144 O ARG A 250 6589 8099 9464 -216 -98 -1419 O ATOM 145 CB ARG A 250 45.793 22.726 -7.715 1.00 58.00 C ANISOU 145 CB ARG A 250 6372 7509 8158 -471 454 -1028 C ATOM 146 CG ARG A 250 46.638 23.951 -7.931 1.00 59.24 C ANISOU 146 CG ARG A 250 6373 7779 8356 -677 646 -1004 C ATOM 147 CD ARG A 250 46.369 24.970 -6.842 1.00114.57 C ANISOU 147 CD ARG A 250 13596 14613 15322 -830 543 -819 C ATOM 148 NE ARG A 250 46.869 26.294 -7.199 1.00134.40 N ANISOU 148 NE ARG A 250 16026 17217 17822 -1048 760 -745 N ATOM 149 CZ ARG A 250 46.198 27.171 -7.941 1.00113.69 C ANISOU 149 CZ ARG A 250 13548 14659 14989 -1170 1013 -590 C ATOM 150 NH1 ARG A 250 44.994 26.872 -8.410 1.00 98.71 N ANISOU 150 NH1 ARG A 250 11882 12748 12874 -1092 1084 -500 N ATOM 151 NH2 ARG A 250 46.733 28.352 -8.214 1.00157.53 N ANISOU 151 NH2 ARG A 250 19010 20280 20563 -1376 1183 -517 N ATOM 152 N VAL A 251 46.127 19.401 -6.967 1.00 52.43 N ANISOU 152 N VAL A 251 5466 6603 7853 26 -173 -1383 N ATOM 153 CA VAL A 251 46.376 18.511 -5.834 1.00 73.17 C ANISOU 153 CA VAL A 251 8087 9035 10679 138 -553 -1423 C ATOM 154 C VAL A 251 46.467 17.045 -6.240 1.00 85.02 C ANISOU 154 C VAL A 251 9443 10522 12339 368 -706 -1617 C ATOM 155 O VAL A 251 45.544 16.499 -6.847 1.00 74.64 O ANISOU 155 O VAL A 251 8263 9207 10889 466 -653 -1596 O ATOM 156 CB VAL A 251 45.261 18.625 -4.794 1.00 71.29 C ANISOU 156 CB VAL A 251 8219 8591 10276 103 -723 -1181 C ATOM 157 CG1 VAL A 251 45.369 19.932 -4.068 1.00 44.97 C ANISOU 157 CG1 VAL A 251 5007 5223 6858 -100 -674 -1031 C ATOM 158 CG2 VAL A 251 43.900 18.520 -5.479 0.62 85.24 C ANISOU 158 CG2 VAL A 251 10226 10369 11793 138 -566 -1060 C ATOM 159 N SER A 252 47.576 16.407 -5.878 1.00 88.63 N ANISOU 159 N SER A 252 9624 10951 13100 458 -915 -1806 N ATOM 160 CA SER A 252 47.789 14.998 -6.188 1.00 53.80 C ANISOU 160 CA SER A 252 5046 6503 8892 686 -1097 -2014 C ATOM 161 C SER A 252 46.581 14.192 -5.758 1.00 75.60 C ANISOU 161 C SER A 252 8101 9070 11554 785 -1311 -1872 C ATOM 162 O SER A 252 45.948 14.497 -4.745 1.00 75.51 O ANISOU 162 O SER A 252 8360 8901 11429 699 -1454 -1643 O ATOM 163 CB SER A 252 49.007 14.482 -5.441 1.00 54.83 C ANISOU 163 CB SER A 252 4909 6548 9375 751 -1388 -2170 C ATOM 164 OG SER A 252 49.724 15.568 -4.880 1.00107.55 O ANISOU 164 OG SER A 252 11523 13255 16085 567 -1343 -2105 O ATOM 165 N SER A 253 46.258 13.158 -6.523 1.00 80.72 N ANISOU 165 N SER A 253 8695 9730 12247 966 -1333 -2013 N ATOM 166 CA SER A 253 45.199 12.250 -6.120 1.00 63.52 C ANISOU 166 CA SER A 253 6753 7351 10030 1072 -1572 -1894 C ATOM 167 C SER A 253 45.512 11.713 -4.724 1.00 77.09 C ANISOU 167 C SER A 253 8501 8841 11949 1096 -1978 -1824 C ATOM 168 O SER A 253 44.664 11.724 -3.832 1.00 69.34 O ANISOU 168 O SER A 253 7807 7697 10842 1041 -2132 -1581 O ATOM 169 CB SER A 253 45.076 11.112 -7.125 1.00 77.06 C ANISOU 169 CB SER A 253 8338 9099 11842 1281 -1588 -2112 C ATOM 170 OG SER A 253 43.959 10.301 -6.831 1.00100.22 O ANISOU 170 OG SER A 253 11511 11841 14728 1367 -1796 -1977 O ATOM 171 N SER A 254 46.749 11.262 -4.541 1.00 65.90 N ANISOU 171 N SER A 254 6778 7418 10842 1175 -2146 -2035 N ATOM 172 CA SER A 254 47.205 10.768 -3.251 1.00 85.17 C ANISOU 172 CA SER A 254 9215 9651 13495 1195 -2548 -1985 C ATOM 173 C SER A 254 47.076 11.829 -2.162 1.00 75.55 C ANISOU 173 C SER A 254 8215 8381 12111 990 -2567 -1741 C ATOM 174 O SER A 254 46.515 11.576 -1.098 1.00 96.14 O ANISOU 174 O SER A 254 11064 10803 14660 964 -2822 -1541 O ATOM 175 CB SER A 254 48.660 10.311 -3.346 1.00 68.25 C ANISOU 175 CB SER A 254 6671 7540 11722 1296 -2680 -2269 C ATOM 176 OG SER A 254 49.532 11.426 -3.424 1.00 95.29 O ANISOU 176 OG SER A 254 9931 11125 15148 1149 -2467 -2315 O ATOM 177 N GLU A 255 47.599 13.017 -2.435 1.00 70.75 N ANISOU 177 N GLU A 255 7520 7938 11426 841 -2297 -1761 N ATOM 178 CA GLU A 255 47.581 14.102 -1.461 1.00 68.80 C ANISOU 178 CA GLU A 255 7454 7647 11039 647 -2307 -1566 C ATOM 179 C GLU A 255 46.160 14.516 -1.072 1.00 70.54 C ANISOU 179 C GLU A 255 8081 7795 10925 561 -2238 -1288 C ATOM 180 O GLU A 255 45.955 15.138 -0.033 1.00 59.65 O ANISOU 180 O GLU A 255 6910 6327 9428 436 -2333 -1113 O ATOM 181 CB GLU A 255 48.348 15.311 -1.999 1.00 62.27 C ANISOU 181 CB GLU A 255 6448 7014 10198 501 -2003 -1641 C ATOM 182 CG GLU A 255 48.810 16.280 -0.930 1.00 85.79 C ANISOU 182 CG GLU A 255 9497 9930 13167 328 -2099 -1529 C ATOM 183 CD GLU A 255 50.087 15.829 -0.240 1.00127.27 C ANISOU 183 CD GLU A 255 14490 15104 18761 373 -2414 -1675 C ATOM 184 OE1 GLU A 255 50.360 14.607 -0.216 1.00116.51 O ANISOU 184 OE1 GLU A 255 12989 13659 17621 550 -2658 -1802 O ATOM 185 OE2 GLU A 255 50.821 16.702 0.279 1.00136.20 O ANISOU 185 OE2 GLU A 255 15553 16245 19952 232 -2431 -1666 O ATOM 186 N MET A 256 45.179 14.186 -1.909 1.00 72.72 N ANISOU 186 N MET A 256 8467 8111 11051 629 -2073 -1255 N ATOM 187 CA MET A 256 43.787 14.494 -1.578 1.00 53.36 C ANISOU 187 CA MET A 256 6380 5586 8310 563 -2013 -998 C ATOM 188 C MET A 256 43.248 13.502 -0.578 1.00 54.38 C ANISOU 188 C MET A 256 6679 5502 8480 642 -2364 -870 C ATOM 189 O MET A 256 42.610 13.878 0.401 1.00 92.74 O ANISOU 189 O MET A 256 11806 10263 13169 546 -2441 -652 O ATOM 190 CB MET A 256 42.897 14.519 -2.817 1.00 53.11 C ANISOU 190 CB MET A 256 6409 5662 8107 600 -1726 -995 C ATOM 191 CG MET A 256 42.762 15.899 -3.436 1.00 79.56 C ANISOU 191 CG MET A 256 9804 9177 11249 440 -1357 -939 C ATOM 192 SD MET A 256 41.905 17.043 -2.344 1.00 81.10 S ANISOU 192 SD MET A 256 10353 9273 11189 255 -1327 -646 S ATOM 193 CE MET A 256 40.293 16.261 -2.267 1.00 54.86 C ANISOU 193 CE MET A 256 7317 5819 7707 346 -1399 -463 C ATOM 194 N GLU A 257 43.511 12.228 -0.834 1.00 92.27 N ANISOU 194 N GLU A 257 11319 10230 13508 817 -2578 -1009 N ATOM 195 CA GLU A 257 43.103 11.185 0.080 1.00 77.92 C ANISOU 195 CA GLU A 257 9634 8202 11772 894 -2943 -891 C ATOM 196 C GLU A 257 43.752 11.440 1.433 1.00 71.21 C ANISOU 196 C GLU A 257 8824 7252 10979 805 -3200 -810 C ATOM 197 O GLU A 257 43.184 11.142 2.487 1.00 71.39 O ANISOU 197 O GLU A 257 9081 7126 10917 773 -3425 -604 O ATOM 198 CB AGLU A 257 43.428 9.790 -0.448 0.42 70.18 C ANISOU 198 CB AGLU A 257 8441 7150 11075 1101 -3152 -1082 C ATOM 199 CB BGLU A 257 43.609 9.851 -0.459 0.58 62.79 C ANISOU 199 CB BGLU A 257 7468 6228 10161 1098 -3148 -1109 C ATOM 200 CG AGLU A 257 42.395 8.750 -0.020 0.42 73.87 C ANISOU 200 CG AGLU A 257 9114 7423 11530 1179 -3398 -910 C ATOM 201 CG BGLU A 257 42.748 8.665 -0.106 0.58 68.26 C ANISOU 201 CG BGLU A 257 8314 6724 10896 1203 -3422 -984 C ATOM 202 CD AGLU A 257 42.133 8.762 1.483 0.42107.50 C ANISOU 202 CD AGLU A 257 13605 11523 15715 1080 -3663 -656 C ATOM 203 CD BGLU A 257 41.605 8.488 -1.070 0.58 45.37 C ANISOU 203 CD BGLU A 257 5534 3868 7837 1252 -3212 -944 C ATOM 204 OE1AGLU A 257 42.882 8.084 2.219 0.42 96.88 O ANISOU 204 OE1AGLU A 257 12159 10049 14603 1133 -4012 -696 O ATOM 205 OE1BGLU A 257 40.600 7.856 -0.689 0.58 71.61 O ANISOU 205 OE1BGLU A 257 9064 7042 11104 1276 -3365 -756 O ATOM 206 OE2AGLU A 257 41.177 9.444 1.930 0.42 37.90 O ANISOU 206 OE2AGLU A 257 5075 2715 6611 953 -3525 -419 O ATOM 207 OE2BGLU A 257 41.711 8.981 -2.212 0.58 83.20 O ANISOU 207 OE2BGLU A 257 10210 8842 12558 1259 -2897 -1094 O ATOM 208 N ARG A 258 44.948 12.011 1.389 1.00 76.15 N ANISOU 208 N ARG A 258 9220 7969 11745 758 -3161 -972 N ATOM 209 CA ARG A 258 45.728 12.260 2.589 1.00 53.18 C ANISOU 209 CA ARG A 258 6309 4972 8927 680 -3420 -935 C ATOM 210 C ARG A 258 45.032 13.316 3.440 1.00 69.76 C ANISOU 210 C ARG A 258 8736 7060 10709 501 -3331 -695 C ATOM 211 O ARG A 258 44.717 13.077 4.605 1.00 85.89 O ANISOU 211 O ARG A 258 10994 8965 12678 466 -3588 -524 O ATOM 212 CB ARG A 258 47.139 12.696 2.186 1.00 78.05 C ANISOU 212 CB ARG A 258 9109 8236 12309 667 -3357 -1174 C ATOM 213 CG ARG A 258 48.247 12.425 3.201 1.00 48.93 C ANISOU 213 CG ARG A 258 5285 4431 8875 667 -3727 -1232 C ATOM 214 CD ARG A 258 48.780 13.729 3.764 1.00 71.24 C ANISOU 214 CD ARG A 258 8142 7313 11613 480 -3646 -1189 C ATOM 215 NE ARG A 258 50.146 13.610 4.270 1.00 97.96 N ANISOU 215 NE ARG A 258 11262 10649 15310 488 -3910 -1336 N ATOM 216 CZ ARG A 258 50.981 14.635 4.428 1.00102.96 C ANISOU 216 CZ ARG A 258 11771 11356 15991 355 -3829 -1394 C ATOM 217 NH1 ARG A 258 52.206 14.429 4.891 1.00119.19 N ANISOU 217 NH1 ARG A 258 13573 13354 18359 372 -4097 -1529 N ATOM 218 NH2 ARG A 258 50.597 15.866 4.112 1.00105.83 N ANISOU 218 NH2 ARG A 258 12256 11844 16113 203 -3490 -1317 N ATOM 219 N LYS A 259 44.769 14.473 2.838 1.00100.48 N ANISOU 219 N LYS A 259 12669 11097 14410 389 -2965 -682 N ATOM 220 CA LYS A 259 44.089 15.578 3.513 1.00 67.61 C ANISOU 220 CA LYS A 259 8802 6932 9953 226 -2841 -483 C ATOM 221 C LYS A 259 42.685 15.168 3.939 1.00 63.83 C ANISOU 221 C LYS A 259 8643 6358 9251 244 -2875 -257 C ATOM 222 O LYS A 259 42.189 15.569 4.995 1.00 69.37 O ANISOU 222 O LYS A 259 9606 6989 9763 151 -2954 -79 O ATOM 223 CB LYS A 259 43.999 16.777 2.573 1.00 72.90 C ANISOU 223 CB LYS A 259 9434 7770 10494 124 -2436 -518 C ATOM 224 CG LYS A 259 43.568 18.075 3.236 1.00 91.37 C ANISOU 224 CG LYS A 259 12021 10108 12589 -49 -2311 -363 C ATOM 225 CD LYS A 259 44.761 18.978 3.542 1.00 95.53 C ANISOU 225 CD LYS A 259 12389 10675 13232 -167 -2325 -467 C ATOM 226 CE LYS A 259 44.295 20.345 4.037 1.00 94.96 C ANISOU 226 CE LYS A 259 12555 10603 12921 -335 -2170 -335 C ATOM 227 NZ LYS A 259 45.367 21.382 4.030 1.00 90.61 N ANISOU 227 NZ LYS A 259 11834 10111 12483 -465 -2109 -437 N ATOM 228 N MET A 260 42.045 14.366 3.099 1.00 66.03 N ANISOU 228 N MET A 260 8894 6640 9555 364 -2812 -271 N ATOM 229 CA MET A 260 40.674 13.921 3.330 1.00 59.48 C ANISOU 229 CA MET A 260 8332 5726 8543 387 -2823 -61 C ATOM 230 C MET A 260 40.562 12.883 4.454 1.00 77.98 C ANISOU 230 C MET A 260 10783 7892 10955 436 -3212 60 C ATOM 231 O MET A 260 39.478 12.624 4.976 1.00 68.28 O ANISOU 231 O MET A 260 9803 6584 9554 418 -3252 275 O ATOM 232 CB MET A 260 40.113 13.334 2.039 1.00 67.57 C ANISOU 232 CB MET A 260 9271 6799 9605 503 -2665 -132 C ATOM 233 CG MET A 260 38.667 13.621 1.842 1.00 72.76 C ANISOU 233 CG MET A 260 10184 7455 10008 465 -2469 63 C ATOM 234 SD MET A 260 38.431 15.389 1.882 1.00 79.46 S ANISOU 234 SD MET A 260 11174 8421 10595 279 -2129 142 S ATOM 235 CE MET A 260 36.645 15.464 1.821 0.00 62.04 C ANISOU 235 CE MET A 260 9268 6170 8134 262 -1973 385 C ATOM 236 N ASN A 261 41.691 12.297 4.828 1.00 81.53 N ANISOU 236 N ASN A 261 10038 9856 11084 2009 -680 -167 N ATOM 237 CA ASN A 261 41.695 11.197 5.778 1.00 66.70 C ANISOU 237 CA ASN A 261 8240 7848 9254 2149 -623 -48 C ATOM 238 C ASN A 261 41.152 11.519 7.160 1.00 75.75 C ANISOU 238 C ASN A 261 9332 9021 10427 2083 -604 81 C ATOM 239 O ASN A 261 41.616 12.448 7.822 1.00 83.63 O ANISOU 239 O ASN A 261 10196 10266 11315 2056 -617 115 O ATOM 240 CB ASN A 261 43.100 10.644 5.935 1.00 76.02 C ANISOU 240 CB ASN A 261 9388 9193 10302 2408 -575 6 C ATOM 241 CG ASN A 261 43.114 9.326 6.663 1.00 67.62 C ANISOU 241 CG ASN A 261 8449 7950 9293 2594 -497 125 C ATOM 242 OD1 ASN A 261 43.450 9.261 7.842 1.00 89.71 O ANISOU 242 OD1 ASN A 261 11175 10874 12038 2687 -457 266 O ATOM 243 ND2 ASN A 261 42.723 8.263 5.969 1.00 95.20 N ANISOU 243 ND2 ASN A 261 12140 11140 12892 2646 -475 69 N ATOM 244 N GLY A 262 40.182 10.721 7.599 1.00 71.85 N ANISOU 244 N GLY A 262 8948 8273 10077 2056 -573 155 N ATOM 245 CA GLY A 262 39.646 10.826 8.946 1.00 51.08 C ANISOU 245 CA GLY A 262 6279 5655 7472 2035 -538 304 C ATOM 246 C GLY A 262 38.646 11.943 9.133 1.00 64.52 C ANISOU 246 C GLY A 262 7915 7397 9201 1824 -575 292 C ATOM 247 O GLY A 262 38.137 12.160 10.234 1.00 70.70 O ANISOU 247 O GLY A 262 8665 8210 9989 1809 -545 411 O ATOM 248 N ARG A 263 38.353 12.644 8.045 1.00 58.84 N ANISOU 248 N ARG A 263 7183 6685 8490 1682 -632 157 N ATOM 249 CA ARG A 263 37.425 13.758 8.091 1.00 85.23 C ANISOU 249 CA ARG A 263 10471 10068 11846 1505 -656 146 C ATOM 250 C ARG A 263 36.041 13.363 7.586 1.00 68.27 C ANISOU 250 C ARG A 263 8385 7699 9856 1366 -670 148 C ATOM 251 O ARG A 263 35.892 12.374 6.881 1.00 60.02 O ANISOU 251 O ARG A 263 7433 6470 8904 1370 -685 101 O ATOM 252 CB ARG A 263 37.992 14.917 7.276 1.00 61.81 C ANISOU 252 CB ARG A 263 7432 7279 8772 1441 -698 20 C ATOM 253 CG ARG A 263 39.379 15.323 7.724 1.00 60.77 C ANISOU 253 CG ARG A 263 7216 7386 8486 1542 -696 19 C ATOM 254 CD ARG A 263 39.617 16.808 7.501 1.00 75.20 C ANISOU 254 CD ARG A 263 8964 9389 10220 1418 -724 -52 C ATOM 255 NE ARG A 263 40.483 17.401 8.524 1.00 51.33 N ANISOU 255 NE ARG A 263 5859 6583 7062 1446 -725 -17 N ATOM 256 CZ ARG A 263 41.724 17.814 8.296 1.00 63.96 C ANISOU 256 CZ ARG A 263 7366 8394 8543 1465 -751 -62 C ATOM 257 NH1 ARG A 263 42.238 17.696 7.079 1.00 54.61 N ANISOU 257 NH1 ARG A 263 6161 7230 7359 1483 -763 -133 N ATOM 258 NH2 ARG A 263 42.452 18.346 9.274 1.00 55.54 N ANISOU 258 NH2 ARG A 263 6219 7534 7351 1463 -766 -36 N ATOM 259 N LYS A 264 35.032 14.143 7.956 1.00 63.77 N ANISOU 259 N LYS A 264 7766 7156 9309 1246 -666 204 N ATOM 260 CA LYS A 264 33.685 13.932 7.454 1.00 53.04 C ANISOU 260 CA LYS A 264 6425 5648 8081 1097 -686 219 C ATOM 261 C LYS A 264 33.359 14.834 6.263 1.00 64.02 C ANISOU 261 C LYS A 264 7777 7109 9439 983 -738 94 C ATOM 262 O LYS A 264 33.426 16.060 6.349 1.00 70.41 O ANISOU 262 O LYS A 264 8526 8075 10152 963 -727 83 O ATOM 263 CB LYS A 264 32.647 14.154 8.555 1.00 65.50 C ANISOU 263 CB LYS A 264 7959 7225 9703 1056 -637 389 C ATOM 264 CG LYS A 264 31.277 13.650 8.155 1.00 79.65 C ANISOU 264 CG LYS A 264 9751 8866 11647 906 -655 442 C ATOM 265 CD LYS A 264 30.197 13.894 9.191 1.00 78.82 C ANISOU 265 CD LYS A 264 9581 8787 11579 874 -598 635 C ATOM 266 CE LYS A 264 28.958 13.085 8.809 1.00 94.08 C ANISOU 266 CE LYS A 264 11503 10560 13684 715 -621 705 C ATOM 267 NZ LYS A 264 27.737 13.487 9.549 1.00116.20 N ANISOU 267 NZ LYS A 264 14205 13431 16514 662 -570 896 N ATOM 268 N LEU A 265 32.996 14.215 5.150 1.00 55.51 N ANISOU 268 N LEU A 265 6746 5910 8437 912 -791 0 N ATOM 269 CA LEU A 265 32.555 14.958 3.984 1.00 80.10 C ANISOU 269 CA LEU A 265 9818 9096 11521 812 -840 -102 C ATOM 270 C LEU A 265 31.108 15.420 4.187 1.00 70.86 C ANISOU 270 C LEU A 265 8579 7935 10410 679 -835 -1 C ATOM 271 O LEU A 265 30.166 14.616 4.194 1.00 65.54 O ANISOU 271 O LEU A 265 7914 7130 9859 581 -858 54 O ATOM 272 CB LEU A 265 32.689 14.091 2.722 1.00 52.59 C ANISOU 272 CB LEU A 265 6411 5497 8072 794 -907 -250 C ATOM 273 CG LEU A 265 33.006 14.810 1.410 1.00 58.21 C ANISOU 273 CG LEU A 265 7092 6339 8685 789 -949 -391 C ATOM 274 CD1 LEU A 265 33.016 13.810 0.280 0.53 31.14 C ANISOU 274 CD1 LEU A 265 3761 2782 5289 780 -1018 -536 C ATOM 275 CD2 LEU A 265 32.003 15.932 1.138 0.76 47.40 C ANISOU 275 CD2 LEU A 265 5623 5091 7297 673 -952 -352 C ATOM 276 N ILE A 266 30.936 16.720 4.371 1.00 54.23 N ANISOU 276 N ILE A 266 6405 5987 8214 677 -800 34 N ATOM 277 CA ILE A 266 29.602 17.286 4.509 1.00 67.07 C ANISOU 277 CA ILE A 266 7959 7657 9867 588 -780 141 C ATOM 278 C ILE A 266 29.253 18.087 3.268 1.00 58.11 C ANISOU 278 C ILE A 266 6777 6625 8676 531 -811 57 C ATOM 279 O ILE A 266 29.896 19.091 2.989 1.00 73.05 O ANISOU 279 O ILE A 266 8670 8624 10462 584 -785 0 O ATOM 280 CB ILE A 266 29.515 18.244 5.701 1.00 57.39 C ANISOU 280 CB ILE A 266 6712 6528 8566 655 -696 261 C ATOM 281 CG1 ILE A 266 29.738 17.496 7.012 1.00 54.55 C ANISOU 281 CG1 ILE A 266 6382 6099 8245 726 -658 370 C ATOM 282 CG2 ILE A 266 28.161 18.962 5.709 1.00 52.49 C ANISOU 282 CG2 ILE A 266 6018 5979 7946 598 -661 375 C ATOM 283 CD1 ILE A 266 29.927 18.433 8.203 1.00 57.57 C ANISOU 283 CD1 ILE A 266 6765 6592 8517 816 -586 450 C ATOM 284 N ARG A 267 28.241 17.664 2.521 1.00 68.94 N ANISOU 284 N ARG A 267 8104 7974 10115 419 -867 54 N ATOM 285 CA ARG A 267 27.857 18.442 1.349 1.00 60.05 C ANISOU 285 CA ARG A 267 6919 6977 8918 384 -893 -9 C ATOM 286 C ARG A 267 27.369 19.820 1.765 1.00 54.85 C ANISOU 286 C ARG A 267 6205 6458 8177 427 -805 107 C ATOM 287 O ARG A 267 26.717 19.992 2.796 1.00 65.57 O ANISOU 287 O ARG A 267 7536 7819 9557 437 -745 258 O ATOM 288 CB ARG A 267 26.808 17.730 0.496 1.00 35.48 C ANISOU 288 CB ARG A 267 3754 3848 5878 244 -983 -33 C ATOM 289 CG ARG A 267 27.250 16.378 -0.011 1.00 68.07 C ANISOU 289 CG ARG A 267 7975 7807 10082 197 -1071 -172 C ATOM 290 CD ARG A 267 28.336 16.489 -1.066 0.52 38.54 C ANISOU 290 CD ARG A 267 4299 4099 6244 284 -1103 -356 C ATOM 291 NE ARG A 267 28.987 15.200 -1.282 1.00 67.80 N ANISOU 291 NE ARG A 267 8133 7620 10007 299 -1156 -477 N ATOM 292 CZ ARG A 267 30.175 15.041 -1.863 1.00 84.21 C ANISOU 292 CZ ARG A 267 10293 9695 12010 422 -1162 -611 C ATOM 293 NH1 ARG A 267 30.858 16.093 -2.298 1.00 83.71 N ANISOU 293 NH1 ARG A 267 10180 9806 11819 517 -1124 -639 N ATOM 294 NH2 ARG A 267 30.684 13.825 -2.006 1.00 88.39 N ANISOU 294 NH2 ARG A 267 10957 10042 12588 457 -1197 -706 N ATOM 295 N LEU A 268 27.712 20.798 0.947 1.00 59.20 N ANISOU 295 N LEU A 268 6749 7118 8627 468 -787 40 N ATOM 296 CA LEU A 268 27.378 22.189 1.183 1.00 60.52 C ANISOU 296 CA LEU A 268 6898 7392 8704 525 -691 130 C ATOM 297 C LEU A 268 25.914 22.389 1.607 1.00 59.23 C ANISOU 297 C LEU A 268 6653 7290 8561 503 -651 302 C ATOM 298 O LEU A 268 25.607 23.206 2.475 1.00 73.40 O ANISOU 298 O LEU A 268 8468 9114 10306 576 -554 419 O ATOM 299 CB LEU A 268 27.719 22.959 -0.093 1.00 57.09 C ANISOU 299 CB LEU A 268 6451 7058 8181 548 -690 41 C ATOM 300 CG LEU A 268 27.559 24.458 -0.221 1.00 62.20 C ANISOU 300 CG LEU A 268 7105 7799 8728 614 -586 106 C ATOM 301 CD1 LEU A 268 28.559 24.984 -1.244 1.00 56.64 C ANISOU 301 CD1 LEU A 268 6424 7142 7954 643 -584 -7 C ATOM 302 CD2 LEU A 268 26.140 24.755 -0.633 0.57 36.94 C ANISOU 302 CD2 LEU A 268 3810 4712 5512 610 -566 224 C ATOM 303 N ALA A 269 25.012 21.623 1.008 1.00 71.93 N ANISOU 303 N ALA A 269 8170 8923 10236 403 -728 320 N ATOM 304 CA ALA A 269 23.585 21.738 1.320 1.00 75.11 C ANISOU 304 CA ALA A 269 8458 9424 10658 370 -699 501 C ATOM 305 C ALA A 269 23.218 21.266 2.733 1.00 60.00 C ANISOU 305 C ALA A 269 6545 7434 8818 374 -653 649 C ATOM 306 O ALA A 269 22.157 21.594 3.251 1.00 76.11 O ANISOU 306 O ALA A 269 8498 9571 10848 395 -592 832 O ATOM 307 CB ALA A 269 22.762 20.981 0.285 1.00 43.96 C ANISOU 307 CB ALA A 269 4397 5542 6762 228 -813 470 C ATOM 308 N GLN A 270 24.092 20.483 3.348 1.00 83.10 N ANISOU 308 N GLN A 270 9562 10203 11808 372 -676 585 N ATOM 309 CA GLN A 270 23.825 19.968 4.683 1.00 58.99 C ANISOU 309 CA GLN A 270 6513 7081 8821 392 -630 730 C ATOM 310 C GLN A 270 24.295 20.918 5.777 1.00 63.07 C ANISOU 310 C GLN A 270 7107 7625 9233 546 -520 786 C ATOM 311 O GLN A 270 24.043 20.689 6.959 1.00 62.50 O ANISOU 311 O GLN A 270 7037 7531 9178 598 -464 920 O ATOM 312 CB GLN A 270 24.491 18.605 4.879 1.00 63.44 C ANISOU 312 CB GLN A 270 7141 7463 9500 334 -696 656 C ATOM 313 CG GLN A 270 23.795 17.462 4.158 1.00 64.66 C ANISOU 313 CG GLN A 270 7240 7544 9785 160 -796 638 C ATOM 314 CD GLN A 270 24.588 16.948 2.977 0.12 83.77 C ANISOU 314 CD GLN A 270 9737 9883 12210 115 -895 411 C ATOM 315 OE1 GLN A 270 25.722 16.468 3.127 1.00 83.36 O ANISOU 315 OE1 GLN A 270 9801 9708 12162 184 -900 307 O ATOM 316 NE2 GLN A 270 23.992 17.030 1.791 0.83 89.27 N ANISOU 316 NE2 GLN A 270 10363 10666 12889 14 -971 338 N ATOM 317 N LEU A 271 24.994 21.976 5.391 1.00 67.06 N ANISOU 317 N LEU A 271 7681 8175 9625 614 -490 681 N ATOM 318 CA LEU A 271 25.574 22.867 6.382 1.00 53.35 C ANISOU 318 CA LEU A 271 6042 6442 7784 732 -404 693 C ATOM 319 C LEU A 271 24.496 23.599 7.180 1.00 62.97 C ANISOU 319 C LEU A 271 7243 7742 8941 822 -297 877 C ATOM 320 O LEU A 271 24.529 23.606 8.408 1.00 53.84 O ANISOU 320 O LEU A 271 6132 6571 7753 904 -242 958 O ATOM 321 CB LEU A 271 26.530 23.869 5.731 1.00 48.22 C ANISOU 321 CB LEU A 271 5471 5810 7039 755 -395 545 C ATOM 322 CG LEU A 271 27.851 23.363 5.157 1.00 60.26 C ANISOU 322 CG LEU A 271 7029 7284 8584 712 -475 371 C ATOM 323 CD1 LEU A 271 28.584 24.531 4.520 1.00 64.18 C ANISOU 323 CD1 LEU A 271 7579 7825 8984 727 -445 272 C ATOM 324 CD2 LEU A 271 28.725 22.700 6.224 1.00 47.37 C ANISOU 324 CD2 LEU A 271 5444 5589 6964 746 -491 355 C ATOM 325 N GLN A 272 23.536 24.210 6.492 1.00 63.00 N ANISOU 325 N GLN A 272 7176 7849 8912 828 -262 952 N ATOM 326 CA GLN A 272 22.535 24.998 7.204 1.00 61.62 C ANISOU 326 CA GLN A 272 6992 7767 8655 951 -142 1136 C ATOM 327 C GLN A 272 21.962 24.232 8.391 1.00 58.66 C ANISOU 327 C GLN A 272 6563 7392 8333 976 -118 1302 C ATOM 328 O GLN A 272 21.975 24.715 9.525 1.00 76.76 O ANISOU 328 O GLN A 272 8937 9688 10539 1109 -28 1376 O ATOM 329 CB GLN A 272 21.418 25.454 6.278 1.00 58.25 C ANISOU 329 CB GLN A 272 6446 7484 8202 953 -117 1236 C ATOM 330 CG GLN A 272 20.162 25.803 7.029 1.00 71.03 C ANISOU 330 CG GLN A 272 7995 9226 9768 1069 -8 1478 C ATOM 331 CD GLN A 272 19.385 26.903 6.371 1.00 78.32 C ANISOU 331 CD GLN A 272 8886 10293 10580 1176 82 1568 C ATOM 332 OE1 GLN A 272 19.573 27.191 5.188 1.00 87.41 O ANISOU 332 OE1 GLN A 272 10016 11477 11719 1128 41 1471 O ATOM 333 NE2 GLN A 272 18.506 27.541 7.138 1.00 90.39 N ANISOU 333 NE2 GLN A 272 10412 11918 12013 1345 216 1767 N ATOM 334 N ASN A 273 21.487 23.020 8.132 1.00 60.25 N ANISOU 334 N ASN A 273 6635 7582 8675 844 -199 1357 N ATOM 335 CA ASN A 273 20.908 22.199 9.189 1.00 64.68 C ANISOU 335 CA ASN A 273 7130 8137 9309 849 -173 1539 C ATOM 336 C ASN A 273 21.860 21.776 10.311 1.00 73.99 C ANISOU 336 C ASN A 273 8421 9204 10487 916 -160 1503 C ATOM 337 O ASN A 273 21.451 21.691 11.471 1.00 70.86 O ANISOU 337 O ASN A 273 8015 8844 10066 1018 -82 1670 O ATOM 338 CB ASN A 273 20.224 20.960 8.611 1.00 68.78 C ANISOU 338 CB ASN A 273 7498 8640 9995 658 -268 1596 C ATOM 339 CG ASN A 273 19.613 20.089 9.690 1.00 84.69 C ANISOU 339 CG ASN A 273 9438 10638 12103 648 -231 1807 C ATOM 340 OD1 ASN A 273 18.394 20.060 9.858 1.00 94.68 O ANISOU 340 OD1 ASN A 273 10550 12036 13387 629 -190 2021 O ATOM 341 ND2 ASN A 273 20.462 19.392 10.448 1.00 80.56 N ANISOU 341 ND2 ASN A 273 9011 9969 11628 672 -237 1767 N ATOM 342 N LYS A 274 23.114 21.482 9.979 1.00 61.23 N ANISOU 342 N LYS A 274 6899 7477 8889 873 -234 1301 N ATOM 343 CA LYS A 274 24.064 21.067 11.011 1.00 61.74 C ANISOU 343 CA LYS A 274 7053 7470 8937 946 -226 1272 C ATOM 344 C LYS A 274 24.427 22.222 11.951 1.00 66.40 C ANISOU 344 C LYS A 274 7752 8126 9351 1106 -140 1266 C ATOM 345 O LYS A 274 24.724 22.021 13.124 1.00 70.87 O ANISOU 345 O LYS A 274 8361 8698 9870 1205 -102 1326 O ATOM 346 CB LYS A 274 25.316 20.451 10.390 1.00 64.95 C ANISOU 346 CB LYS A 274 7515 7769 9392 877 -322 1073 C ATOM 347 CG LYS A 274 25.017 19.313 9.434 1.00 76.07 C ANISOU 347 CG LYS A 274 8857 9085 10960 726 -409 1047 C ATOM 348 CD LYS A 274 25.975 18.150 9.627 1.00 61.90 C ANISOU 348 CD LYS A 274 7122 7154 9244 720 -457 978 C ATOM 349 CE LYS A 274 25.673 17.405 10.924 1.00 87.64 C ANISOU 349 CE LYS A 274 10369 10372 12557 782 -398 1167 C ATOM 350 NZ LYS A 274 26.549 16.216 11.122 1.00 80.69 N ANISOU 350 NZ LYS A 274 9552 9350 11756 799 -427 1127 N ATOM 351 N ILE A 275 24.389 23.436 11.428 1.00 83.81 N ANISOU 351 N ILE A 275 10012 10378 11454 1132 -107 1193 N ATOM 352 CA ILE A 275 24.654 24.605 12.240 1.00 59.63 C ANISOU 352 CA ILE A 275 7084 7351 8224 1266 -24 1171 C ATOM 353 C ILE A 275 23.434 24.890 13.089 1.00 62.36 C ANISOU 353 C ILE A 275 7401 7783 8511 1401 88 1391 C ATOM 354 O ILE A 275 23.537 25.221 14.268 1.00 70.81 O ANISOU 354 O ILE A 275 8558 8880 9467 1537 152 1435 O ATOM 355 CB ILE A 275 24.944 25.808 11.356 1.00 59.55 C ANISOU 355 CB ILE A 275 7156 7334 8136 1248 -9 1039 C ATOM 356 CG1 ILE A 275 26.184 25.532 10.505 1.00 65.89 C ANISOU 356 CG1 ILE A 275 7971 8075 8988 1125 -112 838 C ATOM 357 CG2 ILE A 275 25.142 27.050 12.197 1.00 37.61 C ANISOU 357 CG2 ILE A 275 4546 4559 5186 1374 83 1011 C ATOM 358 CD1 ILE A 275 26.271 26.385 9.249 1.00 49.24 C ANISOU 358 CD1 ILE A 275 5881 5968 6858 1074 -110 745 C ATOM 359 N ALA A 276 22.267 24.757 12.477 1.00 76.14 N ANISOU 359 N ALA A 276 9014 9594 10321 1370 109 1534 N ATOM 360 CA ALA A 276 21.019 24.973 13.194 1.00 86.75 C ANISOU 360 CA ALA A 276 10294 11055 11612 1503 220 1777 C ATOM 361 C ALA A 276 20.853 23.960 14.330 1.00 88.32 C ANISOU 361 C ALA A 276 10431 11262 11866 1539 232 1928 C ATOM 362 O ALA A 276 20.631 24.347 15.478 1.00 72.17 O ANISOU 362 O ALA A 276 8447 9277 9698 1716 329 2036 O ATOM 363 CB ALA A 276 19.831 24.931 12.238 0.87 50.19 C ANISOU 363 CB ALA A 276 5495 6530 7046 1440 225 1909 C ATOM 364 N THR A 277 20.964 22.669 14.014 1.00 78.35 N ANISOU 364 N THR A 277 9060 9930 10779 1382 140 1939 N ATOM 365 CA THR A 277 20.912 21.627 15.044 1.00 67.44 C ANISOU 365 CA THR A 277 7630 8527 9467 1408 156 2085 C ATOM 366 C THR A 277 22.154 21.659 15.928 1.00 78.08 C ANISOU 366 C THR A 277 9124 9821 10720 1509 151 1962 C ATOM 367 O THR A 277 22.355 20.774 16.759 1.00 71.82 O ANISOU 367 O THR A 277 8310 9005 9974 1546 160 2058 O ATOM 368 CB THR A 277 20.745 20.215 14.449 1.00 75.43 C ANISOU 368 CB THR A 277 8520 9440 10700 1206 65 2120 C ATOM 369 OG1 THR A 277 21.934 19.828 13.747 1.00 76.18 O ANISOU 369 OG1 THR A 277 8701 9395 10847 1105 -42 1877 O ATOM 370 CG2 THR A 277 19.555 20.177 13.508 1.00 76.32 C ANISOU 370 CG2 THR A 277 8473 9629 10895 1074 44 2219 C ATOM 371 N GLU A 278 22.986 22.678 15.720 1.00 78.62 N ANISOU 371 N GLU A 278 9334 9880 10657 1545 137 1755 N ATOM 372 CA GLU A 278 24.118 22.961 16.593 1.00 80.99 C ANISOU 372 CA GLU A 278 9769 10176 10827 1639 131 1631 C ATOM 373 C GLU A 278 24.961 21.727 16.893 1.00 86.49 C ANISOU 373 C GLU A 278 10433 10811 11617 1597 63 1610 C ATOM 374 O GLU A 278 25.161 21.365 18.048 1.00103.12 O ANISOU 374 O GLU A 278 12553 12965 13662 1720 100 1701 O ATOM 375 CB GLU A 278 23.616 23.578 17.895 1.00 90.10 C ANISOU 375 CB GLU A 278 10986 11435 11812 1847 245 1764 C ATOM 376 CG GLU A 278 24.634 24.416 18.636 1.00 95.28 C ANISOU 376 CG GLU A 278 11819 12111 12274 1940 241 1590 C ATOM 377 CD GLU A 278 24.000 25.222 19.756 1.00119.84 C ANISOU 377 CD GLU A 278 15025 15317 15192 2155 360 1696 C ATOM 378 OE1 GLU A 278 24.721 26.008 20.405 1.00127.84 O ANISOU 378 OE1 GLU A 278 16204 16346 16025 2229 359 1546 O ATOM 379 OE2 GLU A 278 22.777 25.072 19.986 1.00116.65 O ANISOU 379 OE2 GLU A 278 14530 14982 14810 2249 454 1931 O ATOM 380 N LYS A 279 25.453 21.085 15.842 1.00 83.12 N ANISOU 380 N LYS A 279 9970 10285 11325 1443 -31 1496 N ATOM 381 CA LYS A 279 26.335 19.941 15.994 1.00 92.68 C ANISOU 381 CA LYS A 279 11173 11424 12619 1421 -88 1462 C ATOM 382 C LYS A 279 27.250 19.786 14.782 1.00103.76 C ANISOU 382 C LYS A 279 12598 12747 14079 1295 -188 1250 C ATOM 383 O LYS A 279 27.408 18.692 14.232 1.00 88.88 O ANISOU 383 O LYS A 279 10677 10754 12338 1216 -239 1243 O ATOM 384 CB LYS A 279 25.526 18.668 16.241 1.00108.71 C ANISOU 384 CB LYS A 279 13103 13386 14815 1392 -62 1674 C ATOM 385 CG LYS A 279 24.443 18.391 15.219 1.00 88.63 C ANISOU 385 CG LYS A 279 10463 10790 12424 1232 -84 1734 C ATOM 386 CD LYS A 279 23.699 17.117 15.580 1.00 83.61 C ANISOU 386 CD LYS A 279 9734 10076 11957 1179 -60 1949 C ATOM 387 N LEU A 280 27.844 20.901 14.372 1.00 78.90 N ANISOU 387 N LEU A 280 9518 9646 10814 1283 -209 1081 N ATOM 388 CA LEU A 280 28.822 20.912 13.299 1.00 69.38 C ANISOU 388 CA LEU A 280 8329 8400 9630 1189 -292 887 C ATOM 389 C LEU A 280 30.219 20.971 13.914 1.00 81.50 C ANISOU 389 C LEU A 280 9914 9996 11054 1250 -324 781 C ATOM 390 O LEU A 280 31.166 20.376 13.400 1.00 63.58 O ANISOU 390 O LEU A 280 7631 7703 8822 1220 -386 685 O ATOM 391 CB LEU A 280 28.583 22.118 12.395 1.00 60.94 C ANISOU 391 CB LEU A 280 7290 7355 8510 1127 -287 791 C ATOM 392 CG LEU A 280 29.435 22.291 11.138 1.00 55.74 C ANISOU 392 CG LEU A 280 6637 6674 7869 1031 -359 610 C ATOM 393 CD1 LEU A 280 28.873 21.478 9.994 0.65 48.82 C ANISOU 393 CD1 LEU A 280 5686 5728 7137 938 -406 616 C ATOM 394 CD2 LEU A 280 29.504 23.768 10.762 0.62 25.67 C ANISOU 394 CD2 LEU A 280 2894 2907 3950 1017 -324 526 C ATOM 395 N GLU A 281 30.327 21.680 15.035 1.00 73.30 N ANISOU 395 N GLU A 281 8932 9053 9867 1346 -280 803 N ATOM 396 CA GLU A 281 31.601 21.880 15.725 1.00 60.90 C ANISOU 396 CA GLU A 281 7398 7582 8160 1394 -318 702 C ATOM 397 C GLU A 281 32.332 20.584 16.043 1.00 68.13 C ANISOU 397 C GLU A 281 8254 8507 9124 1454 -350 747 C ATOM 398 O GLU A 281 33.552 20.495 15.904 1.00 58.98 O ANISOU 398 O GLU A 281 7082 7418 7909 1447 -410 635 O ATOM 399 CB GLU A 281 31.374 22.644 17.028 1.00 73.61 C ANISOU 399 CB GLU A 281 9079 9288 9600 1503 -263 745 C ATOM 400 CG GLU A 281 32.659 23.144 17.663 1.00 91.90 C ANISOU 400 CG GLU A 281 11440 11732 11746 1515 -318 604 C ATOM 401 CD GLU A 281 33.319 24.229 16.832 1.00 93.28 C ANISOU 401 CD GLU A 281 11670 11898 11875 1372 -366 409 C ATOM 402 OE1 GLU A 281 34.556 24.393 16.920 0.28 43.81 O ANISOU 402 OE1 GLU A 281 5391 5731 5524 1321 -438 284 O ATOM 403 OE2 GLU A 281 32.594 24.920 16.085 0.21 89.29 O ANISOU 403 OE2 GLU A 281 11211 11297 11417 1311 -326 396 O ATOM 404 N GLU A 282 31.568 19.590 16.485 1.00 73.65 N ANISOU 404 N GLU A 282 8915 9143 9927 1519 -301 928 N ATOM 405 CA GLU A 282 32.103 18.306 16.915 1.00 60.91 C ANISOU 405 CA GLU A 282 7267 7512 8366 1606 -302 1012 C ATOM 406 C GLU A 282 32.566 17.466 15.737 1.00 68.90 C ANISOU 406 C GLU A 282 8264 8399 9515 1529 -356 935 C ATOM 407 O GLU A 282 33.069 16.361 15.910 1.00 70.94 O ANISOU 407 O GLU A 282 8515 8611 9827 1606 -352 991 O ATOM 408 CB GLU A 282 31.019 17.542 17.651 1.00 75.52 C ANISOU 408 CB GLU A 282 9088 9300 10307 1677 -221 1245 C ATOM 409 CG GLU A 282 29.896 17.114 16.735 1.00 87.87 C ANISOU 409 CG GLU A 282 10621 10702 12064 1545 -214 1308 C ATOM 410 CD GLU A 282 28.542 17.295 17.370 1.00111.45 C ANISOU 410 CD GLU A 282 13567 13708 15070 1573 -132 1506 C ATOM 411 OE1 GLU A 282 27.820 16.288 17.514 1.00 96.15 O ANISOU 411 OE1 GLU A 282 11579 11671 13283 1554 -93 1684 O ATOM 412 OE2 GLU A 282 28.208 18.445 17.732 1.00133.11 O ANISOU 412 OE2 GLU A 282 16335 16564 17675 1616 -100 1491 O ATOM 413 N GLU A 283 32.374 17.983 14.534 1.00 71.34 N ANISOU 413 N GLU A 283 8580 8653 9874 1396 -397 812 N ATOM 414 CA GLU A 283 32.823 17.292 13.342 1.00 58.10 C ANISOU 414 CA GLU A 283 6902 6873 8301 1332 -452 715 C ATOM 415 C GLU A 283 34.174 17.840 12.879 1.00 59.32 C ANISOU 415 C GLU A 283 7054 7145 8340 1332 -507 546 C ATOM 416 O GLU A 283 34.425 19.043 12.950 1.00 63.58 O ANISOU 416 O GLU A 283 7598 7797 8762 1290 -518 464 O ATOM 417 CB GLU A 283 31.781 17.440 12.230 1.00 46.72 C ANISOU 417 CB GLU A 283 5453 5323 6976 1191 -468 691 C ATOM 418 CG GLU A 283 30.455 16.775 12.530 1.00 74.94 C ANISOU 418 CG GLU A 283 9001 8790 10683 1158 -425 865 C ATOM 419 CD GLU A 283 30.574 15.261 12.608 1.00115.18 C ANISOU 419 CD GLU A 283 14118 13730 15914 1181 -424 937 C ATOM 420 OE1 GLU A 283 29.594 14.603 13.012 0.87122.97 O ANISOU 420 OE1 GLU A 283 15082 14624 17018 1150 -383 1102 O ATOM 421 OE2 GLU A 283 31.650 14.726 12.266 1.00123.53 O ANISOU 421 OE2 GLU A 283 15218 14757 16960 1234 -456 839 O ATOM 422 N ASP A 284 35.045 16.941 12.436 1.00 53.66 N ANISOU 422 N ASP A 284 6334 6400 7654 1383 -536 505 N ATOM 423 CA ASP A 284 36.255 17.300 11.701 1.00 56.54 C ANISOU 423 CA ASP A 284 6675 6871 7936 1374 -588 358 C ATOM 424 C ASP A 284 35.889 17.237 10.219 1.00 68.81 C ANISOU 424 C ASP A 284 8247 8306 9591 1272 -621 262 C ATOM 425 O ASP A 284 36.111 16.215 9.552 1.00 55.25 O ANISOU 425 O ASP A 284 6558 6482 7952 1309 -635 239 O ATOM 426 CB ASP A 284 37.378 16.297 12.003 1.00 57.65 C ANISOU 426 CB ASP A 284 6798 7065 8041 1524 -589 386 C ATOM 427 CG ASP A 284 38.712 16.706 11.408 1.00 63.87 C ANISOU 427 CG ASP A 284 7529 8021 8717 1533 -637 265 C ATOM 428 OD1 ASP A 284 38.874 17.894 11.053 1.00 75.66 O ANISOU 428 OD1 ASP A 284 8994 9611 10142 1416 -668 168 O ATOM 429 OD2 ASP A 284 39.609 15.841 11.312 1.00 92.65 O ANISOU 429 OD2 ASP A 284 11158 11705 12341 1664 -635 280 O ATOM 430 N TRP A 285 35.324 18.324 9.705 1.00 61.61 N ANISOU 430 N TRP A 285 7331 7414 8665 1157 -627 206 N ATOM 431 CA TRP A 285 34.616 18.261 8.434 1.00 58.39 C ANISOU 431 CA TRP A 285 6932 6900 8352 1062 -650 151 C ATOM 432 C TRP A 285 35.279 18.976 7.264 1.00 67.89 C ANISOU 432 C TRP A 285 8116 8182 9497 1013 -685 12 C ATOM 433 O TRP A 285 36.072 19.912 7.431 1.00 62.54 O ANISOU 433 O TRP A 285 7415 7640 8709 1005 -684 -37 O ATOM 434 CB TRP A 285 33.184 18.769 8.607 1.00 44.14 C ANISOU 434 CB TRP A 285 5126 5048 6596 987 -617 234 C ATOM 435 CG TRP A 285 33.102 20.190 9.007 1.00 57.61 C ANISOU 435 CG TRP A 285 6836 6864 8190 967 -583 227 C ATOM 436 CD1 TRP A 285 33.239 20.695 10.264 1.00 60.74 C ANISOU 436 CD1 TRP A 285 7253 7335 8492 1025 -544 283 C ATOM 437 CD2 TRP A 285 32.850 21.306 8.148 1.00 60.49 C ANISOU 437 CD2 TRP A 285 7203 7263 8518 892 -577 158 C ATOM 438 NE1 TRP A 285 33.088 22.059 10.243 1.00 56.91 N ANISOU 438 NE1 TRP A 285 6802 6905 7916 982 -516 240 N ATOM 439 CE2 TRP A 285 32.851 22.458 8.954 1.00 63.34 C ANISOU 439 CE2 TRP A 285 7604 7691 8769 904 -529 174 C ATOM 440 CE3 TRP A 285 32.629 21.443 6.776 1.00 52.42 C ANISOU 440 CE3 TRP A 285 6159 6222 7534 827 -604 87 C ATOM 441 CZ2 TRP A 285 32.643 23.731 8.434 1.00 69.23 C ANISOU 441 CZ2 TRP A 285 8385 8462 9459 852 -496 128 C ATOM 442 CZ3 TRP A 285 32.422 22.710 6.263 1.00 48.06 C ANISOU 442 CZ3 TRP A 285 5618 5723 6920 785 -572 55 C ATOM 443 CH2 TRP A 285 32.435 23.837 7.091 1.00 59.76 C ANISOU 443 CH2 TRP A 285 7154 7246 8307 797 -513 79 C ATOM 444 N VAL A 286 34.927 18.509 6.073 1.00 61.18 N ANISOU 444 N VAL A 286 7277 7247 8723 974 -717 -49 N ATOM 445 CA VAL A 286 35.391 19.096 4.831 1.00 76.68 C ANISOU 445 CA VAL A 286 9218 9280 10638 939 -744 -164 C ATOM 446 C VAL A 286 34.220 19.274 3.883 1.00 53.80 C ANISOU 446 C VAL A 286 6318 6320 7802 849 -758 -180 C ATOM 447 O VAL A 286 33.321 18.432 3.815 1.00 76.12 O ANISOU 447 O VAL A 286 9164 9026 10731 815 -778 -144 O ATOM 448 CB VAL A 286 36.433 18.207 4.142 1.00 53.61 C ANISOU 448 CB VAL A 286 6306 6361 7703 1028 -777 -244 C ATOM 449 CG1 VAL A 286 36.799 18.795 2.797 1.00 54.33 C ANISOU 449 CG1 VAL A 286 6367 6535 7742 1002 -798 -349 C ATOM 450 CG2 VAL A 286 37.663 18.069 5.018 0.48 67.80 C ANISOU 450 CG2 VAL A 286 8074 8269 9416 1130 -763 -215 C ATOM 451 N THR A 287 34.240 20.373 3.146 1.00 56.47 N ANISOU 451 N THR A 287 6628 6751 8077 805 -748 -227 N ATOM 452 CA THR A 287 33.222 20.619 2.144 1.00 62.68 C ANISOU 452 CA THR A 287 7396 7525 8895 740 -761 -241 C ATOM 453 C THR A 287 33.833 21.182 0.868 1.00 64.58 C ANISOU 453 C THR A 287 7612 7862 9065 748 -772 -339 C ATOM 454 O THR A 287 34.990 21.606 0.855 1.00 74.75 O ANISOU 454 O THR A 287 8889 9233 10280 784 -757 -377 O ATOM 455 CB THR A 287 32.145 21.574 2.659 1.00 60.84 C ANISOU 455 CB THR A 287 7149 7313 8655 696 -703 -136 C ATOM 456 OG1 THR A 287 31.004 21.485 1.806 1.00 53.13 O ANISOU 456 OG1 THR A 287 6132 6334 7720 641 -725 -121 O ATOM 457 CG2 THR A 287 32.663 23.018 2.681 1.00 60.73 C ANISOU 457 CG2 THR A 287 7146 7391 8538 699 -644 -148 C ATOM 458 N PHE A 288 33.042 21.193 -0.198 1.00 55.52 N ANISOU 458 N PHE A 288 6441 6723 7930 711 -798 -368 N ATOM 459 CA PHE A 288 33.547 21.543 -1.517 1.00 61.84 C ANISOU 459 CA PHE A 288 7216 7619 8660 738 -811 -457 C ATOM 460 C PHE A 288 32.633 22.494 -2.255 1.00 46.33 C ANISOU 460 C PHE A 288 5207 5734 6661 701 -782 -421 C ATOM 461 O PHE A 288 31.438 22.266 -2.350 1.00 64.38 O ANISOU 461 O PHE A 288 7471 8000 8992 652 -804 -379 O ATOM 462 CB PHE A 288 33.723 20.286 -2.352 1.00 40.19 C ANISOU 462 CB PHE A 288 4503 4825 5941 772 -890 -565 C ATOM 463 CG PHE A 288 34.796 19.389 -1.849 1.00 59.99 C ANISOU 463 CG PHE A 288 7060 7274 8458 854 -902 -600 C ATOM 464 CD1 PHE A 288 36.132 19.701 -2.067 1.00 62.95 C ANISOU 464 CD1 PHE A 288 7411 7762 8745 940 -877 -632 C ATOM 465 CD2 PHE A 288 34.478 18.236 -1.153 1.00 69.85 C ANISOU 465 CD2 PHE A 288 8372 8367 9801 851 -929 -581 C ATOM 466 CE1 PHE A 288 37.135 18.881 -1.596 1.00 47.79 C ANISOU 466 CE1 PHE A 288 5520 5822 6816 1040 -881 -645 C ATOM 467 CE2 PHE A 288 35.472 17.404 -0.676 1.00 76.29 C ANISOU 467 CE2 PHE A 288 9238 9134 10615 955 -924 -595 C ATOM 468 CZ PHE A 288 36.808 17.723 -0.898 1.00 67.50 C ANISOU 468 CZ PHE A 288 8092 8156 9399 1060 -901 -626 C ATOM 469 N GLY A 289 33.206 23.555 -2.798 1.00 67.44 N ANISOU 469 N GLY A 289 7860 8510 9253 726 -727 -425 N ATOM 470 CA GLY A 289 32.427 24.523 -3.536 1.00 56.69 C ANISOU 470 CA GLY A 289 6463 7231 7846 721 -680 -374 C ATOM 471 C GLY A 289 33.198 25.079 -4.707 1.00 54.02 C ANISOU 471 C GLY A 289 6094 7008 7425 770 -657 -421 C ATOM 472 O GLY A 289 34.428 25.006 -4.741 1.00 66.60 O ANISOU 472 O GLY A 289 7689 8625 8991 797 -657 -470 O ATOM 473 N VAL A 290 32.463 25.612 -5.679 1.00 47.81 N ANISOU 473 N VAL A 290 5264 6314 6589 792 -634 -392 N ATOM 474 CA VAL A 290 33.050 26.349 -6.789 1.00 67.50 C ANISOU 474 CA VAL A 290 7721 8931 8994 851 -586 -398 C ATOM 475 C VAL A 290 32.826 27.839 -6.543 1.00 58.10 C ANISOU 475 C VAL A 290 6552 7745 7777 844 -456 -275 C ATOM 476 O VAL A 290 31.731 28.256 -6.156 1.00 53.08 O ANISOU 476 O VAL A 290 5930 7084 7154 838 -415 -188 O ATOM 477 CB VAL A 290 32.412 25.946 -8.148 1.00 46.32 C ANISOU 477 CB VAL A 290 4978 6370 6252 903 -644 -447 C ATOM 478 CG1 VAL A 290 32.946 26.825 -9.283 1.00 43.29 C ANISOU 478 CG1 VAL A 290 4551 6133 5766 986 -572 -422 C ATOM 479 CG2 VAL A 290 32.672 24.475 -8.444 0.81 42.80 C ANISOU 479 CG2 VAL A 290 4549 5887 5825 910 -769 -591 C ATOM 480 N ILE A 291 33.859 28.648 -6.744 1.00 42.90 N ANISOU 480 N ILE A 291 4636 5847 5816 847 -385 -260 N ATOM 481 CA ILE A 291 33.687 30.087 -6.567 1.00 45.42 C ANISOU 481 CA ILE A 291 5008 6136 6114 834 -253 -150 C ATOM 482 C ILE A 291 32.836 30.615 -7.696 1.00 60.06 C ANISOU 482 C ILE A 291 6817 8100 7904 922 -196 -77 C ATOM 483 O ILE A 291 33.321 30.851 -8.798 1.00 46.51 O ANISOU 483 O ILE A 291 5046 6498 6127 978 -172 -76 O ATOM 484 CB ILE A 291 35.004 30.848 -6.566 1.00 43.76 C ANISOU 484 CB ILE A 291 4813 5925 5889 785 -191 -146 C ATOM 485 CG1 ILE A 291 35.902 30.339 -5.445 0.72 44.23 C ANISOU 485 CG1 ILE A 291 4895 5919 5991 702 -253 -214 C ATOM 486 CG2 ILE A 291 34.732 32.325 -6.395 1.00 42.41 C ANISOU 486 CG2 ILE A 291 4730 5679 5705 762 -48 -38 C ATOM 487 CD1 ILE A 291 37.280 30.893 -5.498 1.00 43.04 C ANISOU 487 CD1 ILE A 291 4720 5813 5822 636 -221 -216 C ATOM 488 N VAL A 292 31.553 30.781 -7.424 1.00 55.36 N ANISOU 488 N VAL A 292 6231 7492 7309 947 -173 -2 N ATOM 489 CA VAL A 292 30.642 31.234 -8.448 1.00 44.61 C ANISOU 489 CA VAL A 292 4808 6269 5873 1044 -123 83 C ATOM 490 C VAL A 292 30.716 32.750 -8.583 1.00 58.33 C ANISOU 490 C VAL A 292 6617 7976 7568 1096 52 214 C ATOM 491 O VAL A 292 30.481 33.306 -9.651 1.00 44.80 O ANISOU 491 O VAL A 292 4856 6390 5778 1194 121 289 O ATOM 492 CB VAL A 292 29.218 30.794 -8.124 1.00 45.07 C ANISOU 492 CB VAL A 292 4823 6361 5941 1054 -166 133 C ATOM 493 CG1 VAL A 292 28.227 31.747 -8.731 1.00 62.98 C ANISOU 493 CG1 VAL A 292 7057 8749 8123 1166 -55 283 C ATOM 494 CG2 VAL A 292 28.997 29.392 -8.635 1.00 51.18 C ANISOU 494 CG2 VAL A 292 5505 7215 6727 1017 -332 12 C ATOM 495 N LYS A 293 31.053 33.423 -7.491 1.00 56.37 N ANISOU 495 N LYS A 293 6496 7555 7366 1033 127 240 N ATOM 496 CA LYS A 293 31.085 34.867 -7.514 1.00 44.44 C ANISOU 496 CA LYS A 293 5095 5965 5825 1068 299 356 C ATOM 497 C LYS A 293 31.964 35.430 -6.430 1.00 51.15 C ANISOU 497 C LYS A 293 6086 6622 6727 946 340 318 C ATOM 498 O LYS A 293 31.954 34.945 -5.309 1.00 55.23 O ANISOU 498 O LYS A 293 6646 7053 7287 880 273 255 O ATOM 499 CB LYS A 293 29.687 35.422 -7.327 1.00 53.72 C ANISOU 499 CB LYS A 293 6308 7145 6958 1183 395 493 C ATOM 500 CG LYS A 293 29.612 36.905 -7.636 1.00 53.64 C ANISOU 500 CG LYS A 293 6416 7066 6900 1266 593 631 C ATOM 501 CD LYS A 293 28.285 37.513 -7.241 1.00 70.85 C ANISOU 501 CD LYS A 293 8662 9229 9028 1403 709 777 C ATOM 502 CE LYS A 293 27.989 38.721 -8.102 1.00 55.15 C ANISOU 502 CE LYS A 293 6726 7266 6963 1552 896 940 C ATOM 503 NZ LYS A 293 29.207 39.548 -8.279 1.00 72.39 N ANISOU 503 NZ LYS A 293 9030 9293 9182 1465 984 919 N ATOM 504 N LYS A 294 32.703 36.481 -6.757 1.00 43.79 N ANISOU 504 N LYS A 294 5226 5626 5787 912 452 362 N ATOM 505 CA LYS A 294 33.544 37.127 -5.758 1.00 60.84 C ANISOU 505 CA LYS A 294 7527 7603 7988 767 488 318 C ATOM 506 C LYS A 294 33.079 38.542 -5.487 1.00 43.63 C ANISOU 506 C LYS A 294 5542 5249 5787 799 669 425 C ATOM 507 O LYS A 294 32.916 39.331 -6.404 1.00 64.06 O ANISOU 507 O LYS A 294 8145 7851 8343 880 796 538 O ATOM 508 CB LYS A 294 35.004 37.161 -6.205 1.00 43.69 C ANISOU 508 CB LYS A 294 5287 5475 5837 647 458 267 C ATOM 509 CG LYS A 294 35.503 35.853 -6.760 1.00 59.45 C ANISOU 509 CG LYS A 294 7099 7658 7832 666 311 183 C ATOM 510 CD LYS A 294 36.999 35.726 -6.576 1.00 56.56 C ANISOU 510 CD LYS A 294 6680 7319 7489 527 257 116 C ATOM 511 CE LYS A 294 37.738 36.916 -7.128 1.00 45.88 C ANISOU 511 CE LYS A 294 5356 5940 6137 454 382 202 C ATOM 512 NZ LYS A 294 39.206 36.818 -6.872 1.00 49.23 N ANISOU 512 NZ LYS A 294 5705 6419 6583 296 324 151 N ATOM 513 N ILE A 295 32.851 38.859 -4.222 1.00 77.06 N ANISOU 513 N ILE A 295 9936 9315 10030 754 688 392 N ATOM 514 CA ILE A 295 32.596 40.237 -3.838 1.00 72.87 C ANISOU 514 CA ILE A 295 9638 8572 9476 769 861 465 C ATOM 515 C ILE A 295 33.797 40.724 -3.044 1.00 72.50 C ANISOU 515 C ILE A 295 9716 8362 9467 549 841 353 C ATOM 516 O ILE A 295 34.322 40.004 -2.194 1.00 63.94 O ANISOU 516 O ILE A 295 8590 7301 8402 439 702 229 O ATOM 517 CB ILE A 295 31.314 40.394 -2.973 1.00 51.86 C ANISOU 517 CB ILE A 295 7102 5836 6768 912 923 521 C ATOM 518 CG1 ILE A 295 30.090 39.786 -3.672 1.00 54.32 C ANISOU 518 CG1 ILE A 295 7248 6351 7038 1104 915 632 C ATOM 519 CG2 ILE A 295 31.068 41.858 -2.680 1.00 45.72 C ANISOU 519 CG2 ILE A 295 6594 4824 5953 959 1122 597 C ATOM 520 CD1 ILE A 295 29.937 38.282 -3.475 1.00 85.10 C ANISOU 520 CD1 ILE A 295 10951 10414 10969 1072 723 549 C ATOM 521 N THR A 296 34.247 41.937 -3.331 1.00 65.42 N ANISOU 521 N THR A 296 8969 7307 8580 479 978 401 N ATOM 522 CA THR A 296 35.334 42.521 -2.564 1.00 84.47 C ANISOU 522 CA THR A 296 11515 9554 11025 240 962 294 C ATOM 523 C THR A 296 34.909 43.881 -2.016 1.00 91.02 C ANISOU 523 C THR A 296 12666 10088 11830 247 1135 329 C ATOM 524 O THR A 296 35.402 44.914 -2.460 1.00103.49 O ANISOU 524 O THR A 296 14367 11516 13439 152 1257 378 O ATOM 525 CB THR A 296 36.607 42.649 -3.415 1.00 83.93 C ANISOU 525 CB THR A 296 11314 9567 11008 76 942 300 C ATOM 526 OG1 THR A 296 37.620 43.321 -2.658 0.56 98.56 O ANISOU 526 OG1 THR A 296 13297 11262 12891 -183 928 205 O ATOM 527 CG2 THR A 296 36.314 43.429 -4.695 1.00 83.51 C ANISOU 527 CG2 THR A 296 11272 9503 10956 189 1114 470 C ATOM 528 N PRO A 297 33.998 43.879 -1.027 1.00107.67 N ANISOU 528 N PRO A 297 14923 12106 13882 364 1153 306 N ATOM 529 CA PRO A 297 33.284 45.091 -0.615 1.00111.77 C ANISOU 529 CA PRO A 297 15757 12361 14351 467 1345 367 C ATOM 530 C PRO A 297 34.084 46.028 0.285 1.00118.55 C ANISOU 530 C PRO A 297 16889 12940 15213 243 1369 235 C ATOM 531 O PRO A 297 35.298 45.913 0.410 1.00105.63 O ANISOU 531 O PRO A 297 15183 11324 13630 -21 1254 120 O ATOM 532 CB PRO A 297 32.083 44.539 0.152 1.00 97.40 C ANISOU 532 CB PRO A 297 13948 10603 12458 679 1328 388 C ATOM 533 CG PRO A 297 32.559 43.249 0.724 1.00 91.30 C ANISOU 533 CG PRO A 297 12968 10013 11710 570 1107 260 C ATOM 534 CD PRO A 297 33.671 42.728 -0.164 1.00116.27 C ANISOU 534 CD PRO A 297 15901 13329 14947 404 998 223 C ATOM 535 N GLN A 298 33.363 46.942 0.924 1.00158.34 N ANISOU 535 N GLN A 298 22244 17732 20187 358 1520 253 N ATOM 536 CA GLN A 298 33.947 48.058 1.654 1.00155.50 C ANISOU 536 CA GLN A 298 22216 17049 19819 170 1586 137 C ATOM 537 C GLN A 298 34.111 47.816 3.141 1.00159.09 C ANISOU 537 C GLN A 298 22793 17449 20206 80 1462 -54 C ATOM 538 O GLN A 298 33.174 47.414 3.812 1.00171.19 O ANISOU 538 O GLN A 298 24356 19034 21654 296 1463 -38 O ATOM 539 CB GLN A 298 33.042 49.277 1.488 1.00128.05 C ANISOU 539 CB GLN A 298 19063 13299 16292 381 1846 267 C ATOM 540 CG GLN A 298 32.619 49.491 0.076 1.00140.70 C ANISOU 540 CG GLN A 298 20545 14987 17929 551 1989 488 C ATOM 541 CD GLN A 298 33.813 49.535 -0.827 1.00153.14 C ANISOU 541 CD GLN A 298 21958 16615 19615 300 1940 488 C ATOM 542 OE1 GLN A 298 33.819 48.943 -1.906 1.00143.74 O ANISOU 542 OE1 GLN A 298 20478 15682 18456 373 1910 600 O ATOM 543 NE2 GLN A 298 34.860 50.211 -0.374 1.00148.84 N ANISOU 543 NE2 GLN A 298 21588 15842 19121 -6 1922 357 N ATOM 544 N SER A 299 35.297 48.095 3.661 1.00162.40 N ANISOU 544 N SER A 299 23280 17775 20651 -239 1358 -226 N ATOM 545 CA SER A 299 35.453 48.275 5.100 1.00192.92 C ANISOU 545 CA SER A 299 27362 21513 24424 -331 1284 -416 C ATOM 546 C SER A 299 36.681 49.129 5.453 0.62241.39 C ANISOU 546 C SER A 299 33679 27447 30591 -704 1241 -583 C ATOM 547 O SER A 299 36.543 50.304 5.805 1.00280.12 O ANISOU 547 O SER A 299 38962 32011 35461 -744 1377 -636 O ATOM 548 CB SER A 299 35.440 46.939 5.859 1.00168.70 C ANISOU 548 CB SER A 299 24053 18734 21311 -287 1085 -489 C ATOM 549 OG SER A 299 34.153 46.580 6.310 1.00167.30 O ANISOU 549 OG SER A 299 23918 18597 21051 30 1147 -407 O ATOM 550 N SER A 300 37.874 48.552 5.348 1.00247.79 N ANISOU 550 N SER A 300 34224 28463 31460 -975 1058 -662 N ATOM 551 CA SER A 300 39.075 49.234 5.813 1.00250.14 C ANISOU 551 CA SER A 300 34642 28627 31772 -1360 979 -830 C ATOM 552 C SER A 300 38.885 49.647 7.266 1.00274.64 C ANISOU 552 C SER A 300 38062 31549 34741 -1391 942 -1029 C ATOM 553 O SER A 300 39.644 50.456 7.802 1.00281.63 O ANISOU 553 O SER A 300 39159 32239 35609 -1692 906 -1193 O ATOM 554 CB SER A 300 39.386 50.458 4.951 1.00231.75 C ANISOU 554 CB SER A 300 32497 26020 29540 -1511 1151 -751 C ATOM 555 OG SER A 300 39.395 50.123 3.579 1.00212.37 O ANISOU 555 OG SER A 300 29772 23735 27186 -1418 1212 -547 O ATOM 556 N ASN A 301 37.855 49.085 7.891 1.00274.92 N ANISOU 556 N ASN A 301 34738 34458 35261 417 809 -3410 N ATOM 557 CA ASN A 301 37.521 49.392 9.272 1.00271.74 C ANISOU 557 CA ASN A 301 34384 34133 34734 494 831 -3602 C ATOM 558 C ASN A 301 38.686 49.061 10.198 1.00278.78 C ANISOU 558 C ASN A 301 35243 35190 35489 379 714 -3791 C ATOM 559 O ASN A 301 38.779 47.937 10.684 1.00281.99 O ANISOU 559 O ASN A 301 35579 35839 35727 409 635 -3735 O ATOM 560 CB ASN A 301 36.281 48.598 9.713 1.00257.17 C ANISOU 560 CB ASN A 301 32496 32454 32763 671 873 -3472 C ATOM 561 CG ASN A 301 35.068 48.834 8.817 1.00235.10 C ANISOU 561 CG ASN A 301 29697 29520 30109 798 961 -3282 C ATOM 562 OD1 ASN A 301 34.292 47.915 8.548 1.00214.06 O ANISOU 562 OD1 ASN A 301 26946 26978 27408 882 957 -3091 O ATOM 563 ND2 ASN A 301 34.897 50.068 8.360 1.00233.71 N ANISOU 563 ND2 ASN A 301 29617 29080 30102 811 1031 -3336 N ATOM 564 N ASN A 302 39.581 50.022 10.421 1.00286.54 N ANISOU 564 N ASN A 302 36278 36040 36554 247 693 -4010 N ATOM 565 CA ASN A 302 40.653 49.862 11.408 1.00292.78 C ANISOU 565 CA ASN A 302 37039 36980 37224 145 561 -4228 C ATOM 566 C ASN A 302 41.914 49.173 10.869 1.00300.38 C ANISOU 566 C ASN A 302 37859 38039 38232 -8 439 -4188 C ATOM 567 O ASN A 302 42.996 49.301 11.445 1.00305.29 O ANISOU 567 O ASN A 302 38436 38724 38835 -130 322 -4386 O ATOM 568 CB ASN A 302 40.124 49.097 12.628 1.00283.55 C ANISOU 568 CB ASN A 302 35888 36060 35786 282 523 -4256 C ATOM 569 CG ASN A 302 40.779 49.524 13.925 1.00272.78 C ANISOU 569 CG ASN A 302 34594 34770 34279 235 429 -4552 C ATOM 570 OD1 ASN A 302 41.967 49.292 14.147 1.00268.90 O ANISOU 570 OD1 ASN A 302 34031 34370 33769 105 272 -4665 O ATOM 571 ND2 ASN A 302 39.993 50.132 14.806 1.00269.36 N ANISOU 571 ND2 ASN A 302 34298 34305 33741 350 519 -4686 N ATOM 572 N GLY A 303 41.769 48.439 9.769 1.00294.42 N ANISOU 572 N GLY A 303 37029 37299 37540 3 463 -3940 N ATOM 573 CA GLY A 303 42.881 47.709 9.181 1.00273.77 C ANISOU 573 CA GLY A 303 34274 34777 34969 -116 372 -3885 C ATOM 574 C GLY A 303 43.038 47.999 7.701 1.00245.46 C ANISOU 574 C GLY A 303 30679 31003 31581 -198 469 -3733 C ATOM 575 O GLY A 303 43.754 48.941 7.365 1.00243.07 O ANISOU 575 O GLY A 303 30389 30524 31441 -348 512 -3847 O ATOM 576 N LYS A 304 42.420 47.227 6.798 1.00216.36 N ANISOU 576 N LYS A 304 26980 27344 27884 -114 504 -3483 N ATOM 577 CA LYS A 304 41.668 45.974 7.018 1.00187.38 C ANISOU 577 CA LYS A 304 23273 23874 24050 33 452 -3323 C ATOM 578 C LYS A 304 40.654 45.755 5.895 1.00156.72 C ANISOU 578 C LYS A 304 19432 19894 20220 120 531 -3079 C ATOM 579 O LYS A 304 39.502 46.180 5.989 1.00145.95 O ANISOU 579 O LYS A 304 18143 18450 18861 235 599 -3029 O ATOM 580 CB LYS A 304 40.947 45.884 8.367 1.00189.25 C ANISOU 580 CB LYS A 304 23555 24235 24116 154 430 -3413 C ATOM 581 CG LYS A 304 41.644 44.977 9.381 1.00181.05 C ANISOU 581 CG LYS A 304 22444 23444 22901 150 287 -3499 C ATOM 582 CD LYS A 304 42.210 43.733 8.720 1.00167.72 C ANISOU 582 CD LYS A 304 20642 21881 21204 129 204 -3344 C ATOM 583 CE LYS A 304 43.341 43.151 9.548 1.00160.63 C ANISOU 583 CE LYS A 304 19658 21172 20202 84 43 -3477 C ATOM 584 NZ LYS A 304 44.419 44.154 9.784 1.00148.49 N ANISOU 584 NZ LYS A 304 18088 19557 18774 -62 6 -3717 N ATOM 585 N THR A 305 41.087 45.088 4.834 1.00125.72 N ANISOU 585 N THR A 305 15453 15980 16334 71 515 -2934 N ATOM 586 CA THR A 305 40.196 44.770 3.731 1.00103.84 C ANISOU 586 CA THR A 305 12728 13136 13593 149 557 -2706 C ATOM 587 C THR A 305 39.809 43.293 3.807 1.00108.46 C ANISOU 587 C THR A 305 13238 13923 14048 234 472 -2567 C ATOM 588 O THR A 305 40.553 42.471 4.352 1.00 83.07 O ANISOU 588 O THR A 305 9938 10879 10746 206 386 -2621 O ATOM 589 CB THR A 305 40.849 45.108 2.370 1.00102.05 C ANISOU 589 CB THR A 305 12534 12752 13487 39 616 -2630 C ATOM 590 OG1 THR A 305 39.910 44.895 1.308 1.00 91.49 O ANISOU 590 OG1 THR A 305 11269 11333 12161 127 640 -2416 O ATOM 591 CG2 THR A 305 42.099 44.255 2.137 1.00 93.20 C ANISOU 591 CG2 THR A 305 11299 11767 12347 -62 564 -2651 C ATOM 592 N PHE A 306 38.633 42.962 3.282 1.00 70.90 N ANISOU 592 N PHE A 306 8513 9140 9288 341 486 -2391 N ATOM 593 CA PHE A 306 38.152 41.587 3.307 1.00 65.00 C ANISOU 593 CA PHE A 306 7703 8555 8438 412 411 -2252 C ATOM 594 C PHE A 306 37.374 41.295 2.034 1.00 77.74 C ANISOU 594 C PHE A 306 9352 10079 10106 458 411 -2052 C ATOM 595 O PHE A 306 37.068 42.207 1.263 1.00 71.74 O ANISOU 595 O PHE A 306 8672 9139 9446 460 468 -2016 O ATOM 596 CB PHE A 306 37.263 41.349 4.526 1.00 67.93 C ANISOU 596 CB PHE A 306 8052 9045 8712 513 413 -2276 C ATOM 597 CG PHE A 306 35.860 41.864 4.358 1.00 60.63 C ANISOU 597 CG PHE A 306 7157 8026 7853 621 483 -2193 C ATOM 598 CD1 PHE A 306 34.858 41.042 3.861 1.00 66.96 C ANISOU 598 CD1 PHE A 306 7916 8866 8658 693 455 -2008 C ATOM 599 CD2 PHE A 306 35.542 43.163 4.689 1.00 50.16 C ANISOU 599 CD2 PHE A 306 5893 6565 6601 652 571 -2307 C ATOM 600 CE1 PHE A 306 33.561 41.508 3.696 1.00 74.31 C ANISOU 600 CE1 PHE A 306 8842 9719 9672 799 508 -1935 C ATOM 601 CE2 PHE A 306 34.241 43.641 4.524 1.00 65.04 C ANISOU 601 CE2 PHE A 306 7787 8360 8564 773 633 -2233 C ATOM 602 CZ PHE A 306 33.253 42.811 4.025 1.00 55.96 C ANISOU 602 CZ PHE A 306 6572 7267 7425 847 598 -2045 C ATOM 603 N SER A 307 37.059 40.024 1.813 1.00 56.49 N ANISOU 603 N SER A 307 6613 7505 7346 494 336 -1923 N ATOM 604 CA SER A 307 36.327 39.637 0.617 1.00 59.17 C ANISOU 604 CA SER A 307 6986 7774 7723 534 307 -1745 C ATOM 605 C SER A 307 35.334 38.521 0.899 1.00 50.15 C ANISOU 605 C SER A 307 5779 6751 6527 610 242 -1627 C ATOM 606 O SER A 307 35.377 37.880 1.954 1.00 56.13 O ANISOU 606 O SER A 307 6475 7653 7199 622 225 -1665 O ATOM 607 CB SER A 307 37.280 39.256 -0.520 1.00 59.63 C ANISOU 607 CB SER A 307 7082 7793 7782 454 287 -1702 C ATOM 608 OG SER A 307 37.886 37.998 -0.296 1.00 57.52 O ANISOU 608 OG SER A 307 6748 7676 7431 434 216 -1697 O ATOM 609 N ILE A 308 34.428 38.311 -0.049 1.00 45.70 N ANISOU 609 N ILE A 308 5234 6118 6013 657 202 -1480 N ATOM 610 CA ILE A 308 33.348 37.335 0.091 1.00 46.43 C ANISOU 610 CA ILE A 308 5253 6297 6092 715 141 -1361 C ATOM 611 C ILE A 308 33.297 36.475 -1.161 1.00 33.21 C ANISOU 611 C ILE A 308 3614 4591 4412 695 40 -1232 C ATOM 612 O ILE A 308 33.456 36.980 -2.272 1.00 66.63 O ANISOU 612 O ILE A 308 7939 8699 8679 685 30 -1196 O ATOM 613 CB ILE A 308 31.980 38.032 0.267 1.00 41.87 C ANISOU 613 CB ILE A 308 4634 5665 5610 812 180 -1322 C ATOM 614 CG1 ILE A 308 32.026 39.029 1.417 1.00 49.61 C ANISOU 614 CG1 ILE A 308 5607 6648 6593 842 294 -1468 C ATOM 615 CG2 ILE A 308 30.893 37.031 0.547 1.00 33.40 C ANISOU 615 CG2 ILE A 308 3454 4694 4543 852 136 -1212 C ATOM 616 CD1 ILE A 308 30.676 39.586 1.758 1.00 55.09 C ANISOU 616 CD1 ILE A 308 6238 7314 7380 955 351 -1442 C ATOM 617 N TRP A 309 33.107 35.172 -0.983 1.00 61.57 N ANISOU 617 N TRP A 309 7153 8288 7952 687 -32 -1164 N ATOM 618 CA TRP A 309 32.941 34.266 -2.116 1.00 46.89 C ANISOU 618 CA TRP A 309 5333 6397 6085 672 -139 -1052 C ATOM 619 C TRP A 309 31.607 33.545 -2.036 1.00 54.12 C ANISOU 619 C TRP A 309 6166 7349 7049 708 -209 -938 C ATOM 620 O TRP A 309 31.264 32.993 -0.993 1.00 71.75 O ANISOU 620 O TRP A 309 8311 9686 9264 711 -183 -934 O ATOM 621 CB TRP A 309 34.044 33.217 -2.143 1.00 43.12 C ANISOU 621 CB TRP A 309 4878 5987 5518 619 -175 -1077 C ATOM 622 CG TRP A 309 35.406 33.743 -2.420 1.00 63.28 C ANISOU 622 CG TRP A 309 7488 8511 8045 571 -116 -1180 C ATOM 623 CD1 TRP A 309 35.740 35.002 -2.826 1.00 58.88 C ANISOU 623 CD1 TRP A 309 6988 7849 7533 553 -37 -1235 C ATOM 624 CD2 TRP A 309 36.628 33.001 -2.357 1.00 57.79 C ANISOU 624 CD2 TRP A 309 6788 7881 7288 533 -129 -1237 C ATOM 625 NE1 TRP A 309 37.105 35.094 -2.999 1.00 50.67 N ANISOU 625 NE1 TRP A 309 5969 6815 6470 488 12 -1326 N ATOM 626 CE2 TRP A 309 37.669 33.879 -2.716 1.00 56.19 C ANISOU 626 CE2 TRP A 309 6619 7624 7106 483 -47 -1333 C ATOM 627 CE3 TRP A 309 36.941 31.677 -2.018 1.00 50.30 C ANISOU 627 CE3 TRP A 309 5807 7024 6279 540 -201 -1215 C ATOM 628 CZ2 TRP A 309 39.000 33.478 -2.750 1.00 62.61 C ANISOU 628 CZ2 TRP A 309 7407 8488 7894 441 -33 -1415 C ATOM 629 CZ3 TRP A 309 38.264 31.281 -2.042 1.00 46.78 C ANISOU 629 CZ3 TRP A 309 5352 6622 5800 517 -198 -1295 C ATOM 630 CH2 TRP A 309 39.277 32.177 -2.413 1.00 56.98 C ANISOU 630 CH2 TRP A 309 6651 7874 7124 469 -114 -1396 C ATOM 631 N ARG A 310 30.853 33.557 -3.133 1.00 51.83 N ANISOU 631 N ARG A 310 5902 6972 6817 732 -298 -845 N ATOM 632 CA ARG A 310 29.639 32.747 -3.234 1.00 48.02 C ANISOU 632 CA ARG A 310 5327 6519 6400 745 -392 -739 C ATOM 633 C ARG A 310 29.952 31.367 -3.788 1.00 49.30 C ANISOU 633 C ARG A 310 5535 6698 6500 685 -503 -688 C ATOM 634 O ARG A 310 30.520 31.242 -4.879 1.00 48.83 O ANISOU 634 O ARG A 310 5600 6566 6386 669 -566 -684 O ATOM 635 CB ARG A 310 28.595 33.423 -4.113 1.00 50.32 C ANISOU 635 CB ARG A 310 5611 6714 6795 809 -467 -670 C ATOM 636 CG ARG A 310 27.428 33.994 -3.334 1.00 71.47 C ANISOU 636 CG ARG A 310 8133 9423 9599 880 -409 -659 C ATOM 637 CD ARG A 310 27.731 35.387 -2.831 1.00 83.66 C ANISOU 637 CD ARG A 310 9709 10919 11160 938 -274 -753 C ATOM 638 NE ARG A 310 27.044 35.662 -1.578 0.71 62.48 N ANISOU 638 NE ARG A 310 6885 8318 8537 986 -157 -792 N ATOM 639 CZ ARG A 310 26.600 36.861 -1.226 0.22 75.05 C ANISOU 639 CZ ARG A 310 8449 9854 10211 1077 -67 -846 C ATOM 640 NH1 ARG A 310 25.990 37.031 -0.061 1.00101.50 N ANISOU 640 NH1 ARG A 310 11676 13289 13600 1124 57 -890 N ATOM 641 NH2 ARG A 310 26.759 37.887 -2.048 1.00 70.28 N ANISOU 641 NH2 ARG A 310 7954 9102 9647 1126 -93 -852 N ATOM 642 N LEU A 311 29.571 30.333 -3.045 1.00 55.03 N ANISOU 642 N LEU A 311 6172 7508 7230 655 -516 -647 N ATOM 643 CA LEU A 311 29.922 28.964 -3.417 1.00 45.70 C ANISOU 643 CA LEU A 311 5042 6329 5994 600 -612 -608 C ATOM 644 C LEU A 311 28.726 28.073 -3.762 1.00 61.04 C ANISOU 644 C LEU A 311 6913 8254 8027 568 -731 -503 C ATOM 645 O LEU A 311 27.662 28.139 -3.134 1.00 70.16 O ANISOU 645 O LEU A 311 7924 9452 9281 571 -701 -455 O ATOM 646 CB LEU A 311 30.745 28.314 -2.311 1.00 52.56 C ANISOU 646 CB LEU A 311 5904 7289 6777 578 -544 -647 C ATOM 647 CG LEU A 311 31.976 29.082 -1.823 1.00 59.17 C ANISOU 647 CG LEU A 311 6785 8161 7536 596 -445 -765 C ATOM 648 CD1 LEU A 311 32.785 28.206 -0.896 1.00 40.86 C ANISOU 648 CD1 LEU A 311 4470 5930 5127 583 -434 -791 C ATOM 649 CD2 LEU A 311 32.831 29.513 -2.991 1.00 62.50 C ANISOU 649 CD2 LEU A 311 7316 8499 7931 592 -465 -814 C ATOM 650 N ASN A 312 28.925 27.242 -4.778 1.00 46.14 N ANISOU 650 N ASN A 312 5124 6301 6106 534 -861 -479 N ATOM 651 CA ASN A 312 27.945 26.255 -5.204 1.00 54.79 C ANISOU 651 CA ASN A 312 6172 7364 7282 483 -1001 -397 C ATOM 652 C ASN A 312 28.712 25.023 -5.641 1.00 41.09 C ANISOU 652 C ASN A 312 4565 5587 5459 438 -1077 -407 C ATOM 653 O ASN A 312 29.792 25.141 -6.220 1.00 56.96 O ANISOU 653 O ASN A 312 6714 7566 7361 463 -1065 -472 O ATOM 654 CB ASN A 312 27.091 26.785 -6.363 1.00 49.14 C ANISOU 654 CB ASN A 312 5461 6575 6636 510 -1135 -365 C ATOM 655 CG ASN A 312 25.970 25.828 -6.755 1.00 66.14 C ANISOU 655 CG ASN A 312 7532 8700 8900 448 -1299 -292 C ATOM 656 OD1 ASN A 312 26.192 24.837 -7.448 1.00 70.93 O ANISOU 656 OD1 ASN A 312 8244 9247 9457 396 -1422 -291 O ATOM 657 ND2 ASN A 312 24.754 26.138 -6.325 1.00 77.25 N ANISOU 657 ND2 ASN A 312 8742 10145 10466 452 -1300 -240 N ATOM 658 N ASP A 313 28.151 23.849 -5.366 1.00 67.02 N ANISOU 658 N ASP A 313 7801 8864 8801 371 -1143 -345 N ATOM 659 CA ASP A 313 28.842 22.579 -5.592 1.00 43.19 C ANISOU 659 CA ASP A 313 4902 5794 5715 334 -1205 -353 C ATOM 660 C ASP A 313 28.544 21.943 -6.957 1.00 51.45 C ANISOU 660 C ASP A 313 6055 6728 6765 302 -1388 -353 C ATOM 661 O ASP A 313 29.028 20.851 -7.275 1.00 55.84 O ANISOU 661 O ASP A 313 6724 7219 7274 275 -1453 -369 O ATOM 662 CB ASP A 313 28.544 21.603 -4.444 1.00 44.12 C ANISOU 662 CB ASP A 313 4942 5945 5875 277 -1163 -284 C ATOM 663 CG ASP A 313 27.071 21.273 -4.312 1.00 78.20 C ANISOU 663 CG ASP A 313 9110 10250 10351 197 -1216 -192 C ATOM 664 OD1 ASP A 313 26.233 21.956 -4.949 1.00 94.11 O ANISOU 664 OD1 ASP A 313 11048 12256 12455 205 -1283 -188 O ATOM 665 OD2 ASP A 313 26.757 20.327 -3.551 1.00 79.94 O ANISOU 665 OD2 ASP A 313 9289 10470 10615 127 -1190 -120 O ATOM 666 N LEU A 314 27.762 22.650 -7.766 1.00 50.41 N ANISOU 666 N LEU A 314 5900 6571 6683 315 -1478 -342 N ATOM 667 CA LEU A 314 27.340 22.167 -9.080 1.00 45.87 C ANISOU 667 CA LEU A 314 5429 5899 6102 288 -1676 -346 C ATOM 668 C LEU A 314 26.579 20.843 -8.998 1.00 65.06 C ANISOU 668 C LEU A 314 7808 8276 8637 185 -1803 -300 C ATOM 669 O LEU A 314 26.283 20.217 -10.016 1.00 72.05 O ANISOU 669 O LEU A 314 8792 9070 9513 147 -1983 -318 O ATOM 670 CB LEU A 314 28.534 22.063 -10.035 1.00 65.98 C ANISOU 670 CB LEU A 314 8208 8388 8474 333 -1681 -425 C ATOM 671 CG LEU A 314 29.243 23.385 -10.349 1.00 57.65 C ANISOU 671 CG LEU A 314 7221 7359 7323 414 -1566 -466 C ATOM 672 CD1 LEU A 314 30.010 23.280 -11.645 1.00 61.57 C ANISOU 672 CD1 LEU A 314 7948 7782 7663 443 -1609 -525 C ATOM 673 CD2 LEU A 314 28.254 24.533 -10.427 1.00 59.70 C ANISOU 673 CD2 LEU A 314 7378 7636 7669 445 -1595 -416 C ATOM 674 N LYS A 315 26.259 20.422 -7.781 1.00 66.08 N ANISOU 674 N LYS A 315 7792 8455 8859 133 -1705 -241 N ATOM 675 CA LYS A 315 25.428 19.240 -7.591 1.00 66.19 C ANISOU 675 CA LYS A 315 7734 8414 9003 15 -1800 -181 C ATOM 676 C LYS A 315 24.033 19.624 -7.093 1.00 67.51 C ANISOU 676 C LYS A 315 7647 8639 9362 -37 -1795 -104 C ATOM 677 O LYS A 315 23.036 19.249 -7.700 1.00 79.36 O ANISOU 677 O LYS A 315 9070 10088 10996 -112 -1963 -83 O ATOM 678 CB LYS A 315 26.118 18.244 -6.668 1.00 58.15 C ANISOU 678 CB LYS A 315 6770 7382 7942 -16 -1699 -156 C ATOM 679 CG LYS A 315 27.401 17.692 -7.266 1.00 65.01 C ANISOU 679 CG LYS A 315 7867 8178 8656 37 -1730 -237 C ATOM 680 CD LYS A 315 27.153 17.170 -8.675 1.00 67.07 C ANISOU 680 CD LYS A 315 8259 8316 8908 5 -1935 -289 C ATOM 681 CE LYS A 315 28.300 16.291 -9.153 1.00 80.26 C ANISOU 681 CE LYS A 315 10150 9894 10452 45 -1956 -364 C ATOM 682 NZ LYS A 315 27.909 15.449 -10.318 1.00 74.38 N ANISOU 682 NZ LYS A 315 9539 9008 9713 -12 -2161 -411 N ATOM 683 N ASP A 316 23.966 20.382 -6.003 1.00 63.88 N ANISOU 683 N ASP A 316 7057 8292 8924 7 -1604 -75 N ATOM 684 CA ASP A 316 22.723 21.036 -5.609 1.00 72.84 C ANISOU 684 CA ASP A 316 7948 9496 10232 -2 -1569 -23 C ATOM 685 C ASP A 316 22.721 22.471 -6.109 1.00 60.07 C ANISOU 685 C ASP A 316 6324 7913 8588 123 -1572 -71 C ATOM 686 O ASP A 316 22.992 23.395 -5.350 1.00 77.13 O ANISOU 686 O ASP A 316 8441 10152 10712 201 -1398 -88 O ATOM 687 CB ASP A 316 22.564 21.031 -4.097 1.00 89.32 C ANISOU 687 CB ASP A 316 9906 11681 12352 -22 -1343 34 C ATOM 688 CG ASP A 316 22.437 19.643 -3.540 1.00 91.13 C ANISOU 688 CG ASP A 316 10139 11865 12620 -150 -1329 109 C ATOM 689 OD1 ASP A 316 21.477 18.943 -3.916 1.00 96.94 O ANISOU 689 OD1 ASP A 316 10770 12541 13523 -264 -1448 157 O ATOM 690 OD2 ASP A 316 23.295 19.253 -2.722 1.00102.27 O ANISOU 690 OD2 ASP A 316 11661 13297 13901 -138 -1206 120 O ATOM 691 N LEU A 317 22.413 22.648 -7.389 1.00 54.59 N ANISOU 691 N LEU A 317 5690 7149 7904 143 -1776 -94 N ATOM 692 CA LEU A 317 22.472 23.957 -8.039 1.00 60.95 C ANISOU 692 CA LEU A 317 6539 7955 8664 265 -1803 -127 C ATOM 693 C LEU A 317 21.608 25.035 -7.383 1.00 56.04 C ANISOU 693 C LEU A 317 5694 7411 8188 335 -1703 -98 C ATOM 694 O LEU A 317 21.627 26.186 -7.801 1.00 81.71 O ANISOU 694 O LEU A 317 8979 10651 11417 446 -1708 -118 O ATOM 695 CB LEU A 317 22.080 23.829 -9.513 1.00 45.55 C ANISOU 695 CB LEU A 317 4687 5917 6704 268 -2068 -137 C ATOM 696 CG LEU A 317 22.696 22.650 -10.277 1.00 57.72 C ANISOU 696 CG LEU A 317 6439 7369 8124 195 -2196 -176 C ATOM 697 CD1 LEU A 317 21.888 22.334 -11.527 0.38 33.58 C ANISOU 697 CD1 LEU A 317 3413 4237 5108 167 -2486 -180 C ATOM 698 CD2 LEU A 317 24.148 22.919 -10.633 0.76 52.08 C ANISOU 698 CD2 LEU A 317 5979 6630 7180 262 -2099 -241 C ATOM 699 N ASP A 318 20.835 24.676 -6.369 1.00 88.09 N ANISOU 699 N ASP A 318 9533 11539 12399 274 -1602 -49 N ATOM 700 CA ASP A 318 20.035 25.681 -5.672 1.00 90.25 C ANISOU 700 CA ASP A 318 9589 11891 12811 352 -1475 -33 C ATOM 701 C ASP A 318 20.697 26.159 -4.379 1.00 73.06 C ANISOU 701 C ASP A 318 7426 9794 10539 394 -1202 -61 C ATOM 702 O ASP A 318 20.388 27.232 -3.883 1.00 79.53 O ANISOU 702 O ASP A 318 8146 10661 11409 492 -1078 -82 O ATOM 703 CB ASP A 318 18.621 25.163 -5.388 1.00 54.31 C ANISOU 703 CB ASP A 318 4750 7378 8508 272 -1517 33 C ATOM 704 CG ASP A 318 18.609 23.716 -4.907 0.06 67.47 C ANISOU 704 CG ASP A 318 6402 9038 10195 106 -1494 82 C ATOM 705 OD1 ASP A 318 17.497 23.158 -4.840 1.00 79.46 O ANISOU 705 OD1 ASP A 318 7699 10567 11925 9 -1552 136 O ATOM 706 OD2 ASP A 318 19.686 23.135 -4.604 1.00 63.28 O ANISOU 706 OD2 ASP A 318 6072 8485 9485 71 -1424 67 O ATOM 707 N LYS A 319 21.608 25.359 -3.839 1.00 61.49 N ANISOU 707 N LYS A 319 6091 8339 8935 327 -1120 -66 N ATOM 708 CA LYS A 319 22.223 25.677 -2.557 1.00 75.70 C ANISOU 708 CA LYS A 319 7908 10223 10632 357 -887 -92 C ATOM 709 C LYS A 319 23.519 26.450 -2.720 1.00 66.39 C ANISOU 709 C LYS A 319 6926 9027 9274 440 -845 -183 C ATOM 710 O LYS A 319 24.431 26.027 -3.440 1.00 86.17 O ANISOU 710 O LYS A 319 9610 11469 11663 422 -941 -211 O ATOM 711 CB LYS A 319 22.442 24.410 -1.717 1.00 58.31 C ANISOU 711 CB LYS A 319 5724 8049 8384 249 -816 -37 C ATOM 712 CG LYS A 319 21.162 23.634 -1.459 1.00 73.11 C ANISOU 712 CG LYS A 319 7394 9934 10450 143 -824 60 C ATOM 713 CD LYS A 319 19.956 24.582 -1.347 1.00 61.70 C ANISOU 713 CD LYS A 319 5705 8546 9192 201 -772 66 C ATOM 714 CE LYS A 319 18.781 23.933 -0.630 1.00 52.91 C ANISOU 714 CE LYS A 319 4353 7486 8262 97 -675 157 C ATOM 715 NZ LYS A 319 18.431 22.610 -1.224 1.00103.59 N ANISOU 715 NZ LYS A 319 10763 13821 14777 -58 -846 223 N ATOM 716 N TYR A 320 23.579 27.589 -2.038 1.00 50.75 N ANISOU 716 N TYR A 320 4904 7098 7281 527 -692 -235 N ATOM 717 CA TYR A 320 24.735 28.473 -2.063 1.00 60.56 C ANISOU 717 CA TYR A 320 6303 8325 8384 594 -630 -329 C ATOM 718 C TYR A 320 25.212 28.747 -0.641 1.00 61.92 C ANISOU 718 C TYR A 320 6466 8593 8467 611 -432 -381 C ATOM 719 O TYR A 320 24.403 28.785 0.283 1.00 59.96 O ANISOU 719 O TYR A 320 6076 8420 8285 617 -314 -353 O ATOM 720 CB TYR A 320 24.336 29.807 -2.679 1.00 33.32 C ANISOU 720 CB TYR A 320 2835 4817 5010 694 -651 -359 C ATOM 721 CG TYR A 320 24.079 29.802 -4.170 1.00 50.36 C ANISOU 721 CG TYR A 320 5058 6871 7204 703 -856 -322 C ATOM 722 CD1 TYR A 320 25.110 30.034 -5.073 1.00 60.76 C ANISOU 722 CD1 TYR A 320 6587 8111 8390 711 -913 -361 C ATOM 723 CD2 TYR A 320 22.801 29.626 -4.672 1.00 63.13 C ANISOU 723 CD2 TYR A 320 6528 8473 8985 708 -988 -252 C ATOM 724 CE1 TYR A 320 24.876 30.066 -6.429 1.00 65.69 C ANISOU 724 CE1 TYR A 320 7301 8643 9014 727 -1093 -325 C ATOM 725 CE2 TYR A 320 22.553 29.658 -6.037 1.00 63.30 C ANISOU 725 CE2 TYR A 320 6629 8405 9019 727 -1199 -222 C ATOM 726 CZ TYR A 320 23.595 29.877 -6.909 1.00 86.21 C ANISOU 726 CZ TYR A 320 9771 11229 11758 739 -1247 -257 C ATOM 727 OH TYR A 320 23.357 29.908 -8.266 1.00 77.90 O ANISOU 727 OH TYR A 320 8827 10089 10684 762 -1450 -225 O ATOM 728 N ILE A 321 26.512 28.951 -0.447 1.00 49.17 N ANISOU 728 N ILE A 321 4998 6983 6701 621 -393 -463 N ATOM 729 CA ILE A 321 26.971 29.510 0.827 1.00 58.60 C ANISOU 729 CA ILE A 321 6194 8263 7806 655 -228 -539 C ATOM 730 C ILE A 321 27.926 30.661 0.559 1.00 48.31 C ANISOU 730 C ILE A 321 4997 6915 6445 705 -201 -657 C ATOM 731 O ILE A 321 28.485 30.762 -0.531 1.00 67.64 O ANISOU 731 O ILE A 321 7540 9277 8883 696 -297 -667 O ATOM 732 CB ILE A 321 27.635 28.467 1.766 1.00 51.82 C ANISOU 732 CB ILE A 321 5389 7486 6814 605 -191 -525 C ATOM 733 CG1 ILE A 321 29.076 28.197 1.342 1.00 55.28 C ANISOU 733 CG1 ILE A 321 5974 7895 7134 593 -267 -587 C ATOM 734 CG2 ILE A 321 26.811 27.170 1.828 1.00 38.53 C ANISOU 734 CG2 ILE A 321 3635 5811 5193 530 -235 -393 C ATOM 735 CD1 ILE A 321 29.648 26.930 1.936 1.00 78.69 C ANISOU 735 CD1 ILE A 321 8994 10907 9995 552 -292 -544 C ATOM 736 N SER A 322 28.099 31.530 1.549 1.00 60.80 N ANISOU 736 N SER A 322 6567 8547 7986 751 -64 -747 N ATOM 737 CA SER A 322 29.015 32.661 1.434 1.00 45.11 C ANISOU 737 CA SER A 322 4674 6509 5957 780 -26 -871 C ATOM 738 C SER A 322 30.205 32.461 2.355 1.00 46.13 C ANISOU 738 C SER A 322 4871 6722 5936 752 18 -964 C ATOM 739 O SER A 322 30.038 32.281 3.563 1.00 60.42 O ANISOU 739 O SER A 322 6649 8635 7673 763 102 -984 O ATOM 740 CB SER A 322 28.308 33.971 1.791 1.00 38.04 C ANISOU 740 CB SER A 322 3724 5581 5147 862 80 -928 C ATOM 741 OG SER A 322 27.277 34.260 0.864 1.00 60.14 O ANISOU 741 OG SER A 322 6459 8295 8096 908 16 -846 O ATOM 742 N LEU A 323 31.402 32.498 1.777 1.00 54.80 N ANISOU 742 N LEU A 323 6061 7778 6984 718 -38 -1022 N ATOM 743 CA LEU A 323 32.643 32.391 2.542 1.00 57.57 C ANISOU 743 CA LEU A 323 6457 8203 7212 695 -23 -1126 C ATOM 744 C LEU A 323 33.286 33.747 2.760 1.00 46.78 C ANISOU 744 C LEU A 323 5125 6798 5851 702 48 -1276 C ATOM 745 O LEU A 323 33.677 34.415 1.804 1.00 54.54 O ANISOU 745 O LEU A 323 6155 7671 6898 683 40 -1304 O ATOM 746 CB LEU A 323 33.649 31.490 1.824 1.00 62.24 C ANISOU 746 CB LEU A 323 7102 8783 7763 652 -123 -1108 C ATOM 747 CG LEU A 323 35.028 31.341 2.472 1.00 56.19 C ANISOU 747 CG LEU A 323 6361 8093 6897 636 -134 -1218 C ATOM 748 CD1 LEU A 323 34.917 30.645 3.826 1.00 50.29 C ANISOU 748 CD1 LEU A 323 5598 7474 6039 659 -131 -1202 C ATOM 749 CD2 LEU A 323 35.967 30.580 1.551 1.00 60.27 C ANISOU 749 CD2 LEU A 323 6915 8578 7409 610 -217 -1206 C ATOM 750 N PHE A 324 33.414 34.139 4.020 1.00 50.04 N ANISOU 750 N PHE A 324 5530 7294 6187 722 120 -1374 N ATOM 751 CA PHE A 324 34.101 35.375 4.369 1.00 56.44 C ANISOU 751 CA PHE A 324 6378 8068 6997 715 177 -1540 C ATOM 752 C PHE A 324 35.596 35.164 4.590 1.00 53.93 C ANISOU 752 C PHE A 324 6086 7803 6602 659 117 -1646 C ATOM 753 O PHE A 324 36.004 34.380 5.443 1.00 65.40 O ANISOU 753 O PHE A 324 7533 9382 7935 664 72 -1657 O ATOM 754 CB PHE A 324 33.445 36.014 5.594 1.00 48.48 C ANISOU 754 CB PHE A 324 5359 7115 5946 773 283 -1617 C ATOM 755 CG PHE A 324 32.147 36.698 5.277 1.00 57.91 C ANISOU 755 CG PHE A 324 6515 8223 7266 839 362 -1565 C ATOM 756 CD1 PHE A 324 31.069 35.968 4.798 1.00 79.27 C ANISOU 756 CD1 PHE A 324 9146 10934 10040 863 341 -1401 C ATOM 757 CD2 PHE A 324 32.010 38.069 5.429 1.00 45.20 C ANISOU 757 CD2 PHE A 324 4936 6517 5721 878 447 -1683 C ATOM 758 CE1 PHE A 324 29.871 36.587 4.490 1.00 54.46 C ANISOU 758 CE1 PHE A 324 5940 7720 7032 935 396 -1355 C ATOM 759 CE2 PHE A 324 30.817 38.700 5.109 1.00 52.31 C ANISOU 759 CE2 PHE A 324 5793 7331 6752 961 510 -1633 C ATOM 760 CZ PHE A 324 29.745 37.955 4.642 1.00 61.44 C ANISOU 760 CZ PHE A 324 6854 8511 7979 994 480 -1468 C ATOM 761 N LEU A 325 36.400 35.866 3.798 1.00 60.76 N ANISOU 761 N LEU A 325 6977 8568 7542 606 117 -1717 N ATOM 762 CA LEU A 325 37.850 35.870 3.951 1.00 47.82 C ANISOU 762 CA LEU A 325 5329 6969 5871 544 75 -1840 C ATOM 763 C LEU A 325 38.304 37.173 4.624 1.00 54.81 C ANISOU 763 C LEU A 325 6229 7821 6774 513 134 -2025 C ATOM 764 O LEU A 325 38.069 38.264 4.101 1.00 70.28 O ANISOU 764 O LEU A 325 8227 9637 8838 495 209 -2057 O ATOM 765 CB LEU A 325 38.539 35.732 2.587 1.00 62.67 C ANISOU 765 CB LEU A 325 7220 8761 7831 489 57 -1801 C ATOM 766 CG LEU A 325 38.344 34.475 1.729 1.00 56.02 C ANISOU 766 CG LEU A 325 6383 7927 6974 507 -11 -1649 C ATOM 767 CD1 LEU A 325 37.034 34.519 0.994 1.00 59.24 C ANISOU 767 CD1 LEU A 325 6828 8246 7434 544 1 -1512 C ATOM 768 CD2 LEU A 325 39.473 34.354 0.725 1.00 69.41 C ANISOU 768 CD2 LEU A 325 8085 9578 8709 450 -15 -1677 C ATOM 769 N PHE A 326 38.942 37.055 5.785 1.00 70.81 N ANISOU 769 N PHE A 326 8238 9973 8696 510 89 -2148 N ATOM 770 CA PHE A 326 39.493 38.215 6.481 1.00 91.34 C ANISOU 770 CA PHE A 326 10854 12548 11303 468 118 -2350 C ATOM 771 C PHE A 326 41.006 38.134 6.609 1.00 90.86 C ANISOU 771 C PHE A 326 10733 12545 11245 387 30 -2483 C ATOM 772 O PHE A 326 41.595 37.067 6.437 1.00 86.81 O ANISOU 772 O PHE A 326 10165 12124 10693 393 -60 -2424 O ATOM 773 CB PHE A 326 38.935 38.322 7.891 1.00 85.97 C ANISOU 773 CB PHE A 326 10212 11972 10481 536 134 -2421 C ATOM 774 CG PHE A 326 37.446 38.377 7.960 0.65 47.82 C ANISOU 774 CG PHE A 326 5410 7111 5651 622 234 -2307 C ATOM 775 CD1 PHE A 326 36.733 37.316 8.492 1.00 61.78 C ANISOU 775 CD1 PHE A 326 7169 9003 7302 687 227 -2179 C ATOM 776 CD2 PHE A 326 36.760 39.497 7.530 1.00 65.12 C ANISOU 776 CD2 PHE A 326 7629 9146 7966 640 338 -2329 C ATOM 777 CE1 PHE A 326 35.355 37.367 8.587 1.00 72.11 C ANISOU 777 CE1 PHE A 326 8472 10294 8633 758 331 -2080 C ATOM 778 CE2 PHE A 326 35.375 39.562 7.624 1.00 62.12 C ANISOU 778 CE2 PHE A 326 7246 8748 7607 732 428 -2233 C ATOM 779 CZ PHE A 326 34.672 38.490 8.148 1.00 64.08 C ANISOU 779 CZ PHE A 326 7461 9135 7752 786 428 -2112 C ATOM 780 N GLY A 327 41.615 39.268 6.952 1.00 85.89 N ANISOU 780 N GLY A 327 10106 11856 10670 315 52 -2672 N ATOM 781 CA GLY A 327 43.045 39.367 7.195 1.00 47.14 C ANISOU 781 CA GLY A 327 5116 7004 5790 226 -34 -2832 C ATOM 782 C GLY A 327 43.932 38.379 6.452 1.00 81.95 C ANISOU 782 C GLY A 327 9425 11472 10240 201 -102 -2759 C ATOM 783 O GLY A 327 44.013 38.411 5.221 1.00 69.71 O ANISOU 783 O GLY A 327 7867 9813 8806 158 -28 -2670 O ATOM 784 N ASP A 328 44.610 37.519 7.216 1.00 88.37 N ANISOU 784 N ASP A 328 10172 12455 10949 238 -242 -2802 N ATOM 785 CA ASP A 328 45.528 36.506 6.687 1.00 65.53 C ANISOU 785 CA ASP A 328 7173 9634 8091 241 -322 -2754 C ATOM 786 C ASP A 328 44.952 35.813 5.475 1.00 79.14 C ANISOU 786 C ASP A 328 8932 11283 9856 274 -251 -2552 C ATOM 787 O ASP A 328 45.579 35.735 4.417 1.00 68.08 O ANISOU 787 O ASP A 328 7476 9822 8571 221 -206 -2534 O ATOM 788 CB ASP A 328 45.792 35.436 7.750 1.00 92.99 C ANISOU 788 CB ASP A 328 10632 13296 11403 339 -487 -2750 C ATOM 789 CG ASP A 328 47.182 35.525 8.339 0.07113.96 C ANISOU 789 CG ASP A 328 13158 16057 14082 300 -627 -2936 C ATOM 790 OD1 ASP A 328 47.819 34.460 8.494 1.00128.51 O ANISOU 790 OD1 ASP A 328 14930 18015 15884 369 -757 -2901 O ATOM 791 OD2 ASP A 328 47.637 36.651 8.640 0.69113.78 O ANISOU 791 OD2 ASP A 328 13103 15999 14131 202 -615 -3121 O ATOM 792 N VAL A 329 43.744 35.298 5.653 1.00 62.93 N ANISOU 792 N VAL A 329 6972 9235 7703 360 -240 -2406 N ATOM 793 CA VAL A 329 43.109 34.471 4.652 1.00 66.07 C ANISOU 793 CA VAL A 329 7407 9579 8117 399 -211 -2216 C ATOM 794 C VAL A 329 42.831 35.259 3.370 1.00 50.13 C ANISOU 794 C VAL A 329 5427 7392 6227 337 -89 -2176 C ATOM 795 O VAL A 329 43.087 34.772 2.275 1.00 62.79 O ANISOU 795 O VAL A 329 7030 8946 7880 325 -72 -2097 O ATOM 796 CB VAL A 329 41.828 33.858 5.215 1.00 76.58 C ANISOU 796 CB VAL A 329 8812 10951 9333 485 -221 -2082 C ATOM 797 CG1 VAL A 329 41.397 32.696 4.355 1.00 47.73 C ANISOU 797 CG1 VAL A 329 5178 7271 5685 522 -245 -1904 C ATOM 798 CG2 VAL A 329 42.055 33.424 6.683 1.00 39.11 C ANISOU 798 CG2 VAL A 329 4066 6361 4432 539 -315 -2141 C ATOM 799 N HIS A 330 42.325 36.480 3.513 1.00 60.26 N ANISOU 799 N HIS A 330 6760 8580 7556 305 -4 -2234 N ATOM 800 CA HIS A 330 42.148 37.382 2.376 1.00 43.42 C ANISOU 800 CA HIS A 330 4683 6272 5543 247 107 -2203 C ATOM 801 C HIS A 330 43.488 37.636 1.698 1.00 53.98 C ANISOU 801 C HIS A 330 5960 7574 6977 142 142 -2287 C ATOM 802 O HIS A 330 43.690 37.294 0.528 1.00 57.40 O ANISOU 802 O HIS A 330 6413 7948 7447 124 186 -2195 O ATOM 803 CB HIS A 330 41.544 38.718 2.830 1.00 42.67 C ANISOU 803 CB HIS A 330 4649 6074 5489 236 183 -2281 C ATOM 804 CG HIS A 330 41.330 39.689 1.709 1.00 70.20 C ANISOU 804 CG HIS A 330 8216 9362 9094 188 291 -2236 C ATOM 805 ND1 HIS A 330 42.227 40.692 1.413 1.00 73.09 N ANISOU 805 ND1 HIS A 330 8584 9618 9568 72 365 -2352 N ATOM 806 CD2 HIS A 330 40.330 39.790 0.801 1.00 56.08 C ANISOU 806 CD2 HIS A 330 6515 7461 7332 240 329 -2081 C ATOM 807 CE1 HIS A 330 41.782 41.382 0.374 1.00 69.32 C ANISOU 807 CE1 HIS A 330 8212 8960 9166 57 456 -2259 C ATOM 808 NE2 HIS A 330 40.636 40.855 -0.013 1.00 80.11 N ANISOU 808 NE2 HIS A 330 9631 10326 10479 166 425 -2097 N ATOM 809 N LYS A 331 44.402 38.236 2.452 1.00 55.54 N ANISOU 809 N LYS A 331 6080 7812 7213 71 126 -2469 N ATOM 810 CA LYS A 331 45.751 38.508 1.984 1.00 62.08 C ANISOU 810 CA LYS A 331 6807 8625 8156 -43 162 -2574 C ATOM 811 C LYS A 331 46.254 37.380 1.104 1.00 58.83 C ANISOU 811 C LYS A 331 6345 8267 7741 -16 152 -2477 C ATOM 812 O LYS A 331 46.919 37.617 0.098 1.00 80.39 O ANISOU 812 O LYS A 331 9055 10922 10569 -96 256 -2475 O ATOM 813 CB LYS A 331 46.694 38.668 3.175 1.00 72.08 C ANISOU 813 CB LYS A 331 7949 10015 9424 -84 60 -2774 C ATOM 814 CG LYS A 331 47.636 39.857 3.083 1.00 82.93 C ANISOU 814 CG LYS A 331 9255 11297 10956 -243 132 -2946 C ATOM 815 CD LYS A 331 47.102 41.058 3.864 1.00 98.44 C ANISOU 815 CD LYS A 331 11311 13171 12923 -276 152 -3059 C ATOM 816 CE LYS A 331 45.788 41.591 3.291 1.00100.42 C ANISOU 816 CE LYS A 331 11736 13254 13164 -224 267 -2917 C ATOM 817 NZ LYS A 331 45.979 42.170 1.930 1.00108.88 N ANISOU 817 NZ LYS A 331 12858 14143 14369 -316 416 -2838 N ATOM 818 N GLU A 332 45.918 36.151 1.484 1.00 74.05 N ANISOU 818 N GLU A 332 8266 10316 9555 98 38 -2395 N ATOM 819 CA GLU A 332 46.470 34.953 0.849 1.00 61.19 C ANISOU 819 CA GLU A 332 6584 8748 7916 144 3 -2328 C ATOM 820 C GLU A 332 45.706 34.467 -0.390 1.00 60.79 C ANISOU 820 C GLU A 332 6657 8600 7841 181 64 -2153 C ATOM 821 O GLU A 332 46.313 34.054 -1.367 1.00 61.54 O ANISOU 821 O GLU A 332 6737 8671 7972 166 118 -2128 O ATOM 822 CB GLU A 332 46.553 33.822 1.877 1.00 69.01 C ANISOU 822 CB GLU A 332 7522 9898 8799 249 -160 -2326 C ATOM 823 CG GLU A 332 46.999 32.495 1.311 1.00 55.12 C ANISOU 823 CG GLU A 332 5729 8188 7027 322 -210 -2250 C ATOM 824 CD GLU A 332 48.500 32.345 1.317 0.49 66.03 C ANISOU 824 CD GLU A 332 6936 9650 8503 298 -235 -2386 C ATOM 825 OE1 GLU A 332 49.155 33.005 2.150 0.53 81.50 O ANISOU 825 OE1 GLU A 332 8789 11674 10504 245 -281 -2539 O ATOM 826 OE2 GLU A 332 49.023 31.567 0.494 0.54 56.42 O ANISOU 826 OE2 GLU A 332 5683 8431 7323 334 -210 -2349 O ATOM 827 N HIS A 333 44.380 34.530 -0.362 1.00 62.58 N ANISOU 827 N HIS A 333 7000 8772 8006 231 55 -2038 N ATOM 828 CA HIS A 333 43.582 33.861 -1.389 1.00 47.66 C ANISOU 828 CA HIS A 333 5217 6816 6077 280 58 -1875 C ATOM 829 C HIS A 333 42.688 34.756 -2.239 1.00 73.12 C ANISOU 829 C HIS A 333 8567 9886 9331 256 143 -1792 C ATOM 830 O HIS A 333 42.017 34.262 -3.152 1.00 43.76 O ANISOU 830 O HIS A 333 4941 6109 5577 294 128 -1663 O ATOM 831 CB HIS A 333 42.680 32.814 -0.736 1.00 47.68 C ANISOU 831 CB HIS A 333 5236 6896 5985 375 -58 -1779 C ATOM 832 CG HIS A 333 43.419 31.686 -0.093 1.00 71.94 C ANISOU 832 CG HIS A 333 8227 10098 9009 426 -159 -1811 C ATOM 833 ND1 HIS A 333 44.172 30.781 -0.811 1.00 60.99 N ANISOU 833 ND1 HIS A 333 6820 8721 7634 448 -178 -1798 N ATOM 834 CD2 HIS A 333 43.490 31.295 1.201 1.00 59.85 C ANISOU 834 CD2 HIS A 333 6646 8686 7410 472 -252 -1848 C ATOM 835 CE1 HIS A 333 44.689 29.892 0.016 1.00 62.54 C ANISOU 835 CE1 HIS A 333 6947 9030 7787 512 -285 -1825 C ATOM 836 NE2 HIS A 333 44.287 30.176 1.242 1.00 53.91 N ANISOU 836 NE2 HIS A 333 5842 8006 6637 525 -336 -1849 N ATOM 837 N TRP A 334 42.643 36.052 -1.940 1.00 49.99 N ANISOU 837 N TRP A 334 5648 6882 6464 201 216 -1865 N ATOM 838 CA TRP A 334 41.624 36.903 -2.550 1.00 46.15 C ANISOU 838 CA TRP A 334 5286 6247 6004 210 272 -1776 C ATOM 839 C TRP A 334 41.720 37.102 -4.061 1.00 48.64 C ANISOU 839 C TRP A 334 5718 6432 6331 177 348 -1684 C ATOM 840 O TRP A 334 40.750 37.520 -4.682 1.00 63.66 O ANISOU 840 O TRP A 334 7736 8222 8229 215 351 -1576 O ATOM 841 CB TRP A 334 41.560 38.254 -1.853 1.00 63.71 C ANISOU 841 CB TRP A 334 7510 8401 8297 168 335 -1883 C ATOM 842 CG TRP A 334 42.668 39.167 -2.191 1.00 69.81 C ANISOU 842 CG TRP A 334 8275 9088 9162 45 443 -1989 C ATOM 843 CD1 TRP A 334 43.949 39.100 -1.741 1.00 58.09 C ANISOU 843 CD1 TRP A 334 6664 7688 7718 -36 449 -2133 C ATOM 844 CD2 TRP A 334 42.595 40.320 -3.033 1.00 78.80 C ANISOU 844 CD2 TRP A 334 9532 10032 10377 -16 563 -1957 C ATOM 845 NE1 TRP A 334 44.685 40.138 -2.256 1.00 75.92 N ANISOU 845 NE1 TRP A 334 8940 9818 10087 -162 578 -2199 N ATOM 846 CE2 TRP A 334 43.876 40.904 -3.052 1.00 57.17 C ANISOU 846 CE2 TRP A 334 6729 7262 7729 -153 656 -2087 C ATOM 847 CE3 TRP A 334 41.569 40.913 -3.779 1.00 65.26 C ANISOU 847 CE3 TRP A 334 7969 8159 8666 33 593 -1827 C ATOM 848 CZ2 TRP A 334 44.166 42.052 -3.788 1.00 71.75 C ANISOU 848 CZ2 TRP A 334 8676 8917 9669 -255 798 -2083 C ATOM 849 CZ3 TRP A 334 41.855 42.057 -4.507 1.00 59.85 C ANISOU 849 CZ3 TRP A 334 7397 7283 8060 -48 719 -1819 C ATOM 850 CH2 TRP A 334 43.146 42.612 -4.509 1.00 55.99 C ANISOU 850 CH2 TRP A 334 6857 6757 7657 -198 830 -1942 C ATOM 851 N LYS A 335 42.876 36.811 -4.653 1.00 62.93 N ANISOU 851 N LYS A 335 7499 8258 8151 114 410 -1726 N ATOM 852 CA LYS A 335 43.028 36.961 -6.103 1.00 34.34 C ANISOU 852 CA LYS A 335 4011 4522 4514 83 503 -1639 C ATOM 853 C LYS A 335 42.703 35.665 -6.841 1.00 60.84 C ANISOU 853 C LYS A 335 7425 7922 7768 159 423 -1536 C ATOM 854 O LYS A 335 42.962 35.533 -8.038 1.00 48.29 O ANISOU 854 O LYS A 335 5949 6268 6132 144 491 -1478 O ATOM 855 CB LYS A 335 44.431 37.449 -6.469 1.00 39.80 C ANISOU 855 CB LYS A 335 4653 5191 5280 -37 654 -1738 C ATOM 856 CG LYS A 335 44.845 38.762 -5.797 1.00 62.17 C ANISOU 856 CG LYS A 335 7432 7958 8232 -139 733 -1856 C ATOM 857 CD LYS A 335 46.215 39.219 -6.267 1.00 40.36 C ANISOU 857 CD LYS A 335 4608 5164 5564 -278 894 -1945 C ATOM 858 CE LYS A 335 46.667 40.496 -5.566 1.00 57.56 C ANISOU 858 CE LYS A 335 6725 7267 7878 -398 960 -2079 C ATOM 859 NZ LYS A 335 47.908 41.065 -6.182 1.00 56.93 N ANISOU 859 NZ LYS A 335 6595 7122 7913 -559 1144 -2145 N ATOM 860 N THR A 336 42.135 34.705 -6.121 1.00 47.93 N ANISOU 860 N THR A 336 5726 6394 6093 238 284 -1515 N ATOM 861 CA THR A 336 41.789 33.437 -6.735 1.00 45.98 C ANISOU 861 CA THR A 336 5533 6174 5763 303 195 -1428 C ATOM 862 C THR A 336 40.749 33.676 -7.826 1.00 46.48 C ANISOU 862 C THR A 336 5767 6115 5777 330 172 -1295 C ATOM 863 O THR A 336 39.878 34.519 -7.690 1.00 51.56 O ANISOU 863 O THR A 336 6448 6689 6454 342 160 -1249 O ATOM 864 CB THR A 336 41.317 32.404 -5.697 1.00 49.77 C ANISOU 864 CB THR A 336 5920 6770 6219 370 57 -1419 C ATOM 865 OG1 THR A 336 42.389 32.142 -4.779 1.00 54.62 O ANISOU 865 OG1 THR A 336 6395 7498 6861 358 62 -1538 O ATOM 866 CG2 THR A 336 40.928 31.108 -6.382 1.00 42.10 C ANISOU 866 CG2 THR A 336 5019 5798 5178 424 -36 -1330 C ATOM 867 N ASP A 337 40.873 32.951 -8.926 1.00 65.45 N ANISOU 867 N ASP A 337 8279 8489 8099 348 160 -1243 N ATOM 868 CA ASP A 337 39.982 33.140 -10.052 1.00 52.09 C ANISOU 868 CA ASP A 337 6768 6687 6339 375 118 -1124 C ATOM 869 C ASP A 337 38.608 32.595 -9.753 1.00 52.26 C ANISOU 869 C ASP A 337 6774 6723 6359 442 -58 -1040 C ATOM 870 O ASP A 337 38.473 31.488 -9.232 1.00 57.40 O ANISOU 870 O ASP A 337 7344 7459 7006 468 -151 -1048 O ATOM 871 CB ASP A 337 40.533 32.432 -11.283 1.00 76.48 C ANISOU 871 CB ASP A 337 9990 9750 9318 378 150 -1108 C ATOM 872 CG ASP A 337 41.735 33.127 -11.855 1.00 83.08 C ANISOU 872 CG ASP A 337 10868 10545 10152 305 354 -1163 C ATOM 873 OD1 ASP A 337 41.609 33.688 -12.961 1.00 84.08 O ANISOU 873 OD1 ASP A 337 11185 10562 10200 290 421 -1091 O ATOM 874 OD2 ASP A 337 42.798 33.124 -11.195 1.00113.73 O ANISOU 874 OD2 ASP A 337 14595 14506 14113 261 446 -1277 O ATOM 875 N GLN A 338 37.584 33.370 -10.093 1.00 56.49 N ANISOU 875 N GLN A 338 7384 7170 6911 469 -102 -955 N ATOM 876 CA GLN A 338 36.218 32.866 -10.037 1.00 64.94 C ANISOU 876 CA GLN A 338 8436 8246 7993 528 -271 -867 C ATOM 877 C GLN A 338 36.151 31.565 -10.864 1.00 52.89 C ANISOU 877 C GLN A 338 6994 6730 6373 541 -382 -832 C ATOM 878 O GLN A 338 36.847 31.428 -11.866 1.00 57.48 O ANISOU 878 O GLN A 338 7717 7266 6855 526 -330 -841 O ATOM 879 CB GLN A 338 35.257 33.944 -10.555 1.00 58.40 C ANISOU 879 CB GLN A 338 7693 7304 7193 569 -305 -781 C ATOM 880 CG GLN A 338 33.781 33.597 -10.500 1.00 63.16 C ANISOU 880 CG GLN A 338 8241 7912 7843 633 -479 -694 C ATOM 881 CD GLN A 338 33.305 32.921 -11.766 1.00 61.20 C ANISOU 881 CD GLN A 338 8136 7615 7500 656 -628 -615 C ATOM 882 OE1 GLN A 338 34.062 32.776 -12.720 1.00 65.12 O ANISOU 882 OE1 GLN A 338 8799 8069 7876 633 -586 -621 O ATOM 883 NE2 GLN A 338 32.044 32.499 -11.780 1.00 95.41 N ANISOU 883 NE2 GLN A 338 12403 11959 11889 697 -801 -547 N ATOM 884 N GLY A 339 35.349 30.598 -10.430 1.00 55.42 N ANISOU 884 N GLY A 339 7232 7103 6723 563 -520 -799 N ATOM 885 CA GLY A 339 35.267 29.320 -11.128 1.00 40.93 C ANISOU 885 CA GLY A 339 5477 5261 4812 568 -635 -780 C ATOM 886 C GLY A 339 36.255 28.286 -10.601 1.00 53.53 C ANISOU 886 C GLY A 339 7014 6932 6393 555 -593 -857 C ATOM 887 O GLY A 339 36.253 27.135 -11.018 1.00 66.57 O ANISOU 887 O GLY A 339 8724 8573 7997 563 -681 -855 O ATOM 888 N THR A 340 37.115 28.709 -9.683 1.00 62.03 N ANISOU 888 N THR A 340 7978 8076 7513 540 -468 -931 N ATOM 889 CA THR A 340 38.015 27.798 -8.997 1.00 45.07 C ANISOU 889 CA THR A 340 5747 6009 5367 545 -448 -1002 C ATOM 890 C THR A 340 37.205 26.878 -8.088 1.00 54.07 C ANISOU 890 C THR A 340 6799 7197 6549 559 -567 -951 C ATOM 891 O THR A 340 36.307 27.326 -7.373 1.00 52.28 O ANISOU 891 O THR A 340 6490 6993 6382 554 -590 -905 O ATOM 892 CB THR A 340 38.998 28.576 -8.105 1.00 53.16 C ANISOU 892 CB THR A 340 6654 7104 6440 524 -317 -1095 C ATOM 893 OG1 THR A 340 39.873 29.366 -8.917 1.00 70.96 O ANISOU 893 OG1 THR A 340 8978 9312 8674 491 -183 -1145 O ATOM 894 CG2 THR A 340 39.821 27.631 -7.255 1.00 46.26 C ANISOU 894 CG2 THR A 340 5679 6325 5574 548 -333 -1158 C ATOM 895 N VAL A 341 37.512 25.590 -8.112 1.00 48.50 N ANISOU 895 N VAL A 341 6114 6498 5816 578 -632 -957 N ATOM 896 CA VAL A 341 36.899 24.685 -7.159 1.00 55.30 C ANISOU 896 CA VAL A 341 6898 7396 6716 580 -722 -904 C ATOM 897 C VAL A 341 37.760 24.694 -5.908 1.00 46.87 C ANISOU 897 C VAL A 341 5718 6431 5658 601 -657 -963 C ATOM 898 O VAL A 341 38.981 24.632 -6.000 1.00 61.92 O ANISOU 898 O VAL A 341 7621 8365 7542 625 -598 -1049 O ATOM 899 CB VAL A 341 36.723 23.257 -7.739 1.00 51.48 C ANISOU 899 CB VAL A 341 6508 6844 6207 589 -839 -874 C ATOM 900 CG1 VAL A 341 37.864 22.907 -8.660 0.59 41.91 C ANISOU 900 CG1 VAL A 341 5401 5596 4925 625 -794 -957 C ATOM 901 CG2 VAL A 341 36.580 22.232 -6.614 1.00 32.84 C ANISOU 901 CG2 VAL A 341 4076 4521 3880 595 -893 -834 C ATOM 902 N ILE A 342 37.135 24.810 -4.740 1.00 63.04 N ANISOU 902 N ILE A 342 7672 8542 7738 593 -665 -921 N ATOM 903 CA ILE A 342 37.898 24.825 -3.501 1.00 61.20 C ANISOU 903 CA ILE A 342 7353 8413 7488 617 -625 -976 C ATOM 904 C ILE A 342 37.455 23.782 -2.485 1.00 54.25 C ANISOU 904 C ILE A 342 6448 7571 6593 632 -692 -899 C ATOM 905 O ILE A 342 36.315 23.329 -2.472 1.00 51.52 O ANISOU 905 O ILE A 342 6112 7186 6277 602 -740 -798 O ATOM 906 CB ILE A 342 37.878 26.206 -2.806 1.00 66.04 C ANISOU 906 CB ILE A 342 7889 9084 8118 601 -532 -1031 C ATOM 907 CG1 ILE A 342 36.528 26.454 -2.158 1.00 42.69 C ANISOU 907 CG1 ILE A 342 4890 6140 5188 588 -537 -949 C ATOM 908 CG2 ILE A 342 38.239 27.329 -3.768 1.00 56.83 C ANISOU 908 CG2 ILE A 342 6760 7858 6975 575 -453 -1090 C ATOM 909 CD1 ILE A 342 36.563 27.559 -1.124 1.00 60.85 C ANISOU 909 CD1 ILE A 342 7119 8514 7488 590 -449 -1015 C ATOM 910 N GLY A 343 38.393 23.400 -1.634 1.00 61.78 N ANISOU 910 N GLY A 343 7369 8600 7505 676 -696 -946 N ATOM 911 CA GLY A 343 38.088 22.587 -0.480 1.00 46.47 C ANISOU 911 CA GLY A 343 5421 6708 5527 696 -742 -871 C ATOM 912 C GLY A 343 38.045 23.498 0.731 1.00 58.61 C ANISOU 912 C GLY A 343 6886 8359 7024 697 -678 -908 C ATOM 913 O GLY A 343 38.928 24.330 0.932 1.00 58.09 O ANISOU 913 O GLY A 343 6772 8353 6946 710 -638 -1027 O ATOM 914 N LEU A 344 37.008 23.348 1.542 1.00 61.68 N ANISOU 914 N LEU A 344 7266 8775 7394 676 -661 -813 N ATOM 915 CA LEU A 344 36.863 24.167 2.732 1.00 48.97 C ANISOU 915 CA LEU A 344 5610 7272 5726 683 -589 -850 C ATOM 916 C LEU A 344 36.731 23.274 3.967 1.00 67.47 C ANISOU 916 C LEU A 344 7988 9680 7968 710 -613 -765 C ATOM 917 O LEU A 344 35.836 22.432 4.041 1.00 72.16 O ANISOU 917 O LEU A 344 8612 10227 8578 680 -620 -630 O ATOM 918 CB LEU A 344 35.638 25.043 2.577 1.00 49.30 C ANISOU 918 CB LEU A 344 5607 7291 5833 640 -506 -821 C ATOM 919 CG LEU A 344 35.342 25.986 3.727 1.00 57.94 C ANISOU 919 CG LEU A 344 6660 8480 6874 652 -409 -871 C ATOM 920 CD1 LEU A 344 36.271 27.180 3.663 1.00 71.21 C ANISOU 920 CD1 LEU A 344 8322 10182 8553 663 -378 -1033 C ATOM 921 CD2 LEU A 344 33.907 26.404 3.603 1.00 45.03 C ANISOU 921 CD2 LEU A 344 4973 6813 5322 625 -337 -799 C ATOM 922 N LEU A 345 37.634 23.456 4.926 1.00 51.63 N ANISOU 922 N LEU A 345 5984 7776 5857 763 -631 -842 N ATOM 923 CA LEU A 345 37.730 22.573 6.092 1.00 50.46 C ANISOU 923 CA LEU A 345 5901 7691 5582 808 -675 -761 C ATOM 924 C LEU A 345 37.429 23.276 7.416 1.00 62.06 C ANISOU 924 C LEU A 345 7375 9281 6924 818 -600 -789 C ATOM 925 O LEU A 345 38.085 24.259 7.764 1.00 60.13 O ANISOU 925 O LEU A 345 7093 9112 6641 837 -593 -938 O ATOM 926 CB LEU A 345 39.141 21.974 6.181 1.00 55.93 C ANISOU 926 CB LEU A 345 6613 8408 6230 889 -799 -822 C ATOM 927 CG LEU A 345 39.587 20.986 5.105 1.00 55.66 C ANISOU 927 CG LEU A 345 6602 8260 6285 912 -879 -790 C ATOM 928 CD1 LEU A 345 40.158 21.726 3.922 0.80 48.52 C ANISOU 928 CD1 LEU A 345 5627 7320 5488 890 -853 -919 C ATOM 929 CD2 LEU A 345 40.623 20.054 5.678 0.51 62.19 C ANISOU 929 CD2 LEU A 345 7472 9118 7040 1016 -1001 -785 C ATOM 930 N ASN A 346 36.460 22.762 8.167 1.00 58.40 N ANISOU 930 N ASN A 346 6963 8834 6392 801 -537 -652 N ATOM 931 CA ASN A 346 36.253 23.229 9.536 1.00 56.32 C ANISOU 931 CA ASN A 346 6740 8695 5966 827 -463 -669 C ATOM 932 C ASN A 346 36.151 24.743 9.632 1.00 60.87 C ANISOU 932 C ASN A 346 7246 9322 6560 817 -373 -826 C ATOM 933 O ASN A 346 36.798 25.366 10.482 1.00 66.66 O ANISOU 933 O ASN A 346 8006 10155 7167 858 -387 -949 O ATOM 934 CB ASN A 346 37.395 22.755 10.442 1.00 52.81 C ANISOU 934 CB ASN A 346 6380 8336 5349 912 -585 -700 C ATOM 935 CG ASN A 346 37.391 21.256 10.651 1.00 63.45 C ANISOU 935 CG ASN A 346 7832 9632 6644 939 -660 -524 C ATOM 936 OD1 ASN A 346 36.421 20.695 11.157 1.00 71.37 O ANISOU 936 OD1 ASN A 346 8901 10619 7596 902 -571 -366 O ATOM 937 ND2 ASN A 346 38.485 20.599 10.270 1.00 49.31 N ANISOU 937 ND2 ASN A 346 6054 7806 4875 1004 -814 -549 N ATOM 938 N ALA A 347 35.350 25.326 8.746 1.00 46.51 N ANISOU 938 N ALA A 347 5347 7425 4900 765 -294 -826 N ATOM 939 CA ALA A 347 35.079 26.758 8.764 1.00 42.97 C ANISOU 939 CA ALA A 347 4841 6991 4493 760 -196 -955 C ATOM 940 C ALA A 347 34.213 27.112 9.960 1.00 50.59 C ANISOU 940 C ALA A 347 5830 8045 5348 776 -57 -938 C ATOM 941 O ALA A 347 33.622 26.231 10.583 1.00 57.13 O ANISOU 941 O ALA A 347 6702 8907 6096 772 -15 -797 O ATOM 942 CB ALA A 347 34.386 27.178 7.474 1.00 53.50 C ANISOU 942 CB ALA A 347 6097 8209 6024 717 -165 -932 C ATOM 943 N ASN A 348 34.133 28.402 10.273 1.00 61.40 N ANISOU 943 N ASN A 348 7176 9440 6713 794 27 -1081 N ATOM 944 CA ASN A 348 33.355 28.867 11.419 1.00 47.65 C ANISOU 944 CA ASN A 348 5463 7785 4857 823 179 -1096 C ATOM 945 C ASN A 348 32.092 29.582 11.010 1.00 57.88 C ANISOU 945 C ASN A 348 6660 9023 6310 816 325 -1077 C ATOM 946 O ASN A 348 32.138 30.531 10.229 1.00 98.32 O ANISOU 946 O ASN A 348 11725 14061 11572 816 320 -1171 O ATOM 947 CB ASN A 348 34.188 29.817 12.267 1.00 90.85 C ANISOU 947 CB ASN A 348 10998 13333 10187 863 167 -1296 C ATOM 948 CG ASN A 348 35.468 29.189 12.743 1.00 80.46 C ANISOU 948 CG ASN A 348 9761 12089 8720 884 2 -1331 C ATOM 949 OD1 ASN A 348 36.562 29.695 12.484 1.00 86.37 O ANISOU 949 OD1 ASN A 348 10490 12830 9496 880 -108 -1479 O ATOM 950 ND2 ASN A 348 35.343 28.068 13.432 1.00 57.97 N ANISOU 950 ND2 ASN A 348 6998 9307 5723 906 -18 -1189 N ATOM 951 N PRO A 349 30.953 29.138 11.540 1.00 61.18 N ANISOU 951 N PRO A 349 7052 9481 6711 813 458 -952 N ATOM 952 CA PRO A 349 29.713 29.847 11.219 1.00 63.70 C ANISOU 952 CA PRO A 349 7249 9758 7196 823 599 -942 C ATOM 953 C PRO A 349 29.763 31.262 11.763 1.00 66.13 C ANISOU 953 C PRO A 349 7574 10088 7462 888 699 -1130 C ATOM 954 O PRO A 349 30.186 31.478 12.897 1.00 65.80 O ANISOU 954 O PRO A 349 7639 10145 7215 924 747 -1221 O ATOM 955 CB PRO A 349 28.637 29.022 11.935 1.00 46.90 C ANISOU 955 CB PRO A 349 5094 7699 5029 802 740 -782 C ATOM 956 CG PRO A 349 29.242 27.642 12.036 1.00 67.20 C ANISOU 956 CG PRO A 349 7758 10279 7494 754 621 -655 C ATOM 957 CD PRO A 349 30.715 27.866 12.242 1.00 47.04 C ANISOU 957 CD PRO A 349 5327 7754 4794 792 477 -789 C ATOM 958 N MET A 350 29.357 32.216 10.938 1.00 69.93 N ANISOU 958 N MET A 350 7968 10467 8133 908 718 -1189 N ATOM 959 CA MET A 350 29.228 33.593 11.362 1.00 45.90 C ANISOU 959 CA MET A 350 4937 7411 5093 976 827 -1359 C ATOM 960 C MET A 350 27.960 33.704 12.193 1.00 80.84 C ANISOU 960 C MET A 350 9302 11909 9506 1030 1039 -1321 C ATOM 961 O MET A 350 27.102 32.820 12.137 1.00 75.06 O ANISOU 961 O MET A 350 8480 11209 8830 1000 1091 -1153 O ATOM 962 CB MET A 350 29.082 34.486 10.140 1.00 58.04 C ANISOU 962 CB MET A 350 6405 8797 6853 987 781 -1399 C ATOM 963 CG MET A 350 30.051 34.196 9.020 1.00 78.66 C ANISOU 963 CG MET A 350 9043 11323 9521 923 598 -1381 C ATOM 964 SD MET A 350 31.354 35.417 8.988 1.00 72.64 S ANISOU 964 SD MET A 350 8375 10495 8728 917 551 -1600 S ATOM 965 CE MET A 350 30.467 36.839 8.369 1.00 86.04 C ANISOU 965 CE MET A 350 10025 12040 10627 982 647 -1651 C ATOM 966 N LYS A 351 27.841 34.791 12.955 1.00 81.46 N ANISOU 966 N LYS A 351 9424 12007 9519 1105 1169 -1484 N ATOM 967 CA LYS A 351 26.590 35.120 13.627 1.00 66.44 C ANISOU 967 CA LYS A 351 7446 10157 7639 1177 1398 -1476 C ATOM 968 C LYS A 351 25.499 35.363 12.589 1.00 96.72 C ANISOU 968 C LYS A 351 11086 13891 11771 1201 1422 -1387 C ATOM 969 O LYS A 351 25.739 36.010 11.569 1.00 99.63 O ANISOU 969 O LYS A 351 11430 14126 12299 1211 1307 -1430 O ATOM 970 CB LYS A 351 26.757 36.350 14.520 1.00 67.82 C ANISOU 970 CB LYS A 351 7723 10346 7700 1265 1519 -1698 C ATOM 971 CG LYS A 351 27.043 36.008 15.975 1.00118.77 C ANISOU 971 CG LYS A 351 14330 16958 13839 1278 1613 -1749 C ATOM 972 CD LYS A 351 26.073 34.943 16.469 1.00138.60 C ANISOU 972 CD LYS A 351 16778 19582 16303 1260 1767 -1552 C ATOM 973 CE LYS A 351 25.980 34.908 17.984 1.00133.21 C ANISOU 973 CE LYS A 351 16247 19051 15317 1308 1947 -1611 C ATOM 974 NZ LYS A 351 24.771 34.155 18.423 1.00133.09 N ANISOU 974 NZ LYS A 351 16136 19124 15309 1299 2173 -1431 N ATOM 975 N PRO A 352 24.292 34.840 12.845 1.00 92.92 N ANISOU 975 N PRO A 352 10464 13474 11366 1209 1570 -1258 N ATOM 976 CA PRO A 352 23.205 34.945 11.867 1.00 88.04 C ANISOU 976 CA PRO A 352 9634 12776 11042 1229 1566 -1163 C ATOM 977 C PRO A 352 22.618 36.356 11.829 1.00111.20 C ANISOU 977 C PRO A 352 12500 15636 14114 1365 1676 -1300 C ATOM 978 O PRO A 352 22.299 36.931 12.872 1.00 84.91 O ANISOU 978 O PRO A 352 9199 12374 10690 1447 1880 -1409 O ATOM 979 CB PRO A 352 22.155 33.952 12.392 1.00119.81 C ANISOU 979 CB PRO A 352 13524 16911 15088 1185 1718 -1003 C ATOM 980 CG PRO A 352 22.796 33.245 13.582 1.00122.27 C ANISOU 980 CG PRO A 352 14016 17349 15092 1136 1789 -992 C ATOM 981 CD PRO A 352 23.865 34.154 14.077 1.00 81.59 C ANISOU 981 CD PRO A 352 9059 12192 9750 1197 1755 -1195 C ATOM 982 N LYS A 353 22.476 36.909 10.631 1.00125.01 N ANISOU 982 N LYS A 353 14177 17242 16079 1396 1541 -1294 N ATOM 983 CA LYS A 353 21.919 38.245 10.483 1.00124.72 C ANISOU 983 CA LYS A 353 14084 17107 16197 1537 1622 -1408 C ATOM 984 C LYS A 353 20.431 38.192 10.142 1.00126.34 C ANISOU 984 C LYS A 353 14029 17318 16657 1608 1699 -1303 C ATOM 985 O LYS A 353 20.018 37.482 9.222 1.00121.93 O ANISOU 985 O LYS A 353 13342 16737 16247 1546 1557 -1151 O ATOM 986 CB LYS A 353 22.683 39.027 9.412 1.00104.94 C ANISOU 986 CB LYS A 353 11681 14424 13768 1544 1435 -1468 C ATOM 987 CG LYS A 353 22.664 38.384 8.031 1.00 79.64 C ANISOU 987 CG LYS A 353 8413 11148 10699 1473 1219 -1310 C ATOM 988 N GLU A 354 19.630 38.940 10.896 1.00 91.67 N ANISOU 988 N GLU A 354 9555 12958 12318 1739 1921 -1395 N ATOM 989 CA GLU A 354 18.208 39.062 10.609 1.00 79.04 C ANISOU 989 CA GLU A 354 7679 11363 10990 1832 2006 -1322 C ATOM 990 C GLU A 354 18.000 39.321 9.110 1.00108.54 C ANISOU 990 C GLU A 354 11329 14945 14966 1857 1761 -1245 C ATOM 991 O GLU A 354 18.833 39.955 8.456 0.98100.28 O ANISOU 991 O GLU A 354 10453 13758 13890 1868 1607 -1306 O ATOM 992 CB GLU A 354 17.601 40.190 11.448 1.00 84.59 C ANISOU 992 CB GLU A 354 8345 12066 11728 2010 2254 -1481 C ATOM 993 CG GLU A 354 16.143 39.975 11.850 1.00132.76 C ANISOU 993 CG GLU A 354 14153 18275 18016 2084 2469 -1417 C ATOM 994 CD GLU A 354 15.624 41.063 12.783 1.00151.67 C ANISOU 994 CD GLU A 354 16534 20679 20415 2271 2745 -1594 C ATOM 995 OE1 GLU A 354 16.408 41.976 13.119 1.00157.82 O ANISOU 995 OE1 GLU A 354 17548 21371 21046 2335 2753 -1771 O ATOM 996 OE2 GLU A 354 14.436 41.003 13.178 1.00132.25 O ANISOU 996 OE2 GLU A 354 13826 18311 18114 2352 2957 -1564 O ATOM 997 N GLY A 355 16.905 38.804 8.560 1.00101.46 N ANISOU 997 N GLY A 355 10174 14077 14300 1858 1720 -1108 N ATOM 998 CA GLY A 355 16.588 39.042 7.164 1.00 54.89 C ANISOU 998 CA GLY A 355 4191 8045 8621 1898 1478 -1033 C ATOM 999 C GLY A 355 17.144 38.060 6.149 1.00 82.31 C ANISOU 999 C GLY A 355 7730 11487 12055 1740 1216 -905 C ATOM 1000 O GLY A 355 16.834 38.171 4.962 1.00 89.39 O ANISOU 1000 O GLY A 355 8567 12284 13114 1768 1005 -834 O ATOM 1001 N THR A 356 17.961 37.103 6.586 1.00 91.82 N ANISOU 1001 N THR A 356 9071 12774 13043 1586 1220 -876 N ATOM 1002 CA THR A 356 18.511 36.136 5.633 1.00104.59 C ANISOU 1002 CA THR A 356 10761 14355 14623 1445 982 -765 C ATOM 1003 C THR A 356 18.318 34.653 5.918 1.00111.11 C ANISOU 1003 C THR A 356 11514 15293 15410 1289 986 -639 C ATOM 1004 O THR A 356 18.212 34.193 7.065 1.00 60.21 O ANISOU 1004 O THR A 356 5054 8969 8856 1247 1185 -635 O ATOM 1005 CB THR A 356 20.010 36.360 5.299 1.00 84.32 C ANISOU 1005 CB THR A 356 8479 11706 11854 1399 866 -835 C ATOM 1006 OG1 THR A 356 20.670 36.986 6.405 1.00136.29 O ANISOU 1006 OG1 THR A 356 15199 18325 18259 1437 1039 -979 O ATOM 1007 CG2 THR A 356 20.163 37.216 4.050 1.00 85.33 C ANISOU 1007 CG2 THR A 356 8668 11666 12088 1472 690 -847 C ATOM 1008 N ASP A 357 18.319 33.940 4.800 1.00109.88 N ANISOU 1008 N ASP A 357 11341 15077 15333 1204 753 -537 N ATOM 1009 CA ASP A 357 18.139 32.513 4.677 1.00116.82 C ANISOU 1009 CA ASP A 357 12163 16005 16219 1047 682 -408 C ATOM 1010 C ASP A 357 19.544 31.925 4.567 1.00123.52 C ANISOU 1010 C ASP A 357 13277 16827 16829 954 582 -418 C ATOM 1011 O ASP A 357 19.730 30.750 4.244 1.00110.92 O ANISOU 1011 O ASP A 357 11710 15229 15207 828 471 -325 O ATOM 1012 CB ASP A 357 17.396 32.289 3.355 0.95112.66 C ANISOU 1012 CB ASP A 357 11489 15398 15918 1035 448 -327 C ATOM 1013 CG ASP A 357 16.697 30.951 3.278 1.00170.77 C ANISOU 1013 CG ASP A 357 18689 22807 23389 886 401 -199 C ATOM 1014 OD1 ASP A 357 16.873 30.245 2.259 1.00167.64 O ANISOU 1014 OD1 ASP A 357 18342 22338 23016 799 165 -140 O ATOM 1015 OD2 ASP A 357 15.953 30.615 4.221 1.00201.05 O ANISOU 1015 OD2 ASP A 357 22353 26747 27291 851 607 -160 O ATOM 1016 N GLU A 358 20.530 32.764 4.860 1.00 99.68 N ANISOU 1016 N GLU A 358 10443 13783 13650 1020 625 -540 N ATOM 1017 CA GLU A 358 21.869 32.608 4.310 1.00 51.71 C ANISOU 1017 CA GLU A 358 4590 7641 7417 972 479 -574 C ATOM 1018 C GLU A 358 22.881 31.950 5.243 1.00 63.34 C ANISOU 1018 C GLU A 358 6215 9195 8655 901 545 -597 C ATOM 1019 O GLU A 358 22.987 32.319 6.412 1.00 61.89 O ANISOU 1019 O GLU A 358 6062 9096 8358 941 721 -669 O ATOM 1020 CB GLU A 358 22.377 33.987 3.866 1.00 64.82 C ANISOU 1020 CB GLU A 358 6352 9199 9077 1075 455 -692 C ATOM 1021 CG GLU A 358 23.718 33.995 3.118 1.00 75.17 C ANISOU 1021 CG GLU A 358 7869 10427 10264 1028 314 -731 C ATOM 1022 CD GLU A 358 23.991 35.331 2.424 0.36 72.03 C ANISOU 1022 CD GLU A 358 7552 9897 9919 1115 279 -810 C ATOM 1023 OE1 GLU A 358 25.149 35.569 2.032 0.60 75.52 O ANISOU 1023 OE1 GLU A 358 8161 10278 10255 1080 224 -868 O ATOM 1024 OE2 GLU A 358 23.054 36.144 2.264 0.73 77.21 O ANISOU 1024 OE2 GLU A 358 8103 10503 10730 1221 310 -811 O ATOM 1025 N VAL A 359 23.627 30.981 4.707 1.00 44.95 N ANISOU 1025 N VAL A 359 3990 6838 6250 808 395 -541 N ATOM 1026 CA VAL A 359 24.759 30.389 5.418 1.00 54.48 C ANISOU 1026 CA VAL A 359 5357 8102 7240 761 409 -568 C ATOM 1027 C VAL A 359 26.054 31.154 5.127 1.00 53.81 C ANISOU 1027 C VAL A 359 5429 7968 7051 795 347 -699 C ATOM 1028 O VAL A 359 26.463 31.281 3.975 1.00 61.34 O ANISOU 1028 O VAL A 359 6429 8822 8057 785 208 -703 O ATOM 1029 CB VAL A 359 24.952 28.892 5.055 1.00 48.14 C ANISOU 1029 CB VAL A 359 4587 7287 6416 653 287 -445 C ATOM 1030 CG1 VAL A 359 26.167 28.327 5.766 0.36 27.11 C ANISOU 1030 CG1 VAL A 359 2089 4676 3536 630 285 -473 C ATOM 1031 CG2 VAL A 359 23.718 28.092 5.426 0.79 42.45 C ANISOU 1031 CG2 VAL A 359 3713 6610 5806 592 363 -314 C ATOM 1032 N CYS A 360 26.696 31.662 6.176 1.00 58.74 N ANISOU 1032 N CYS A 360 6135 8660 7523 830 453 -810 N ATOM 1033 CA CYS A 360 27.960 32.385 6.031 1.00 49.20 C ANISOU 1033 CA CYS A 360 5056 7413 6226 844 403 -947 C ATOM 1034 C CYS A 360 29.029 31.772 6.913 1.00 64.60 C ANISOU 1034 C CYS A 360 7115 9456 7973 812 391 -988 C ATOM 1035 O CYS A 360 28.780 31.479 8.079 1.00 62.38 O ANISOU 1035 O CYS A 360 6844 9284 7576 824 494 -978 O ATOM 1036 CB CYS A 360 27.800 33.854 6.435 1.00 59.71 C ANISOU 1036 CB CYS A 360 6387 8717 7584 926 519 -1086 C ATOM 1037 SG CYS A 360 26.502 34.736 5.578 1.00 69.41 S ANISOU 1037 SG CYS A 360 7487 9835 9053 1004 541 -1049 S ATOM 1038 N LEU A 361 30.230 31.606 6.371 1.00 62.64 N ANISOU 1038 N LEU A 361 6951 9171 7678 779 268 -1034 N ATOM 1039 CA LEU A 361 31.320 31.033 7.153 1.00 65.17 C ANISOU 1039 CA LEU A 361 7361 9579 7821 763 226 -1078 C ATOM 1040 C LEU A 361 32.642 31.748 6.919 1.00 61.38 C ANISOU 1040 C LEU A 361 6942 9070 7310 758 164 -1232 C ATOM 1041 O LEU A 361 32.866 32.325 5.860 1.00 64.10 O ANISOU 1041 O LEU A 361 7280 9307 7769 743 128 -1263 O ATOM 1042 CB LEU A 361 31.474 29.542 6.855 1.00 54.79 C ANISOU 1042 CB LEU A 361 6064 8271 6483 718 123 -939 C ATOM 1043 CG LEU A 361 30.186 28.766 6.601 1.00 40.07 C ANISOU 1043 CG LEU A 361 4120 6385 4719 687 148 -774 C ATOM 1044 CD1 LEU A 361 29.934 28.683 5.108 0.03 48.56 C ANISOU 1044 CD1 LEU A 361 5156 7338 5956 658 43 -727 C ATOM 1045 CD2 LEU A 361 30.290 27.385 7.182 1.00 56.91 C ANISOU 1045 CD2 LEU A 361 6304 8568 6750 652 119 -658 C ATOM 1046 N SER A 362 33.514 31.698 7.921 1.00 53.44 N ANISOU 1046 N SER A 362 5997 8161 6146 767 149 -1326 N ATOM 1047 CA SER A 362 34.843 32.287 7.823 1.00 54.95 C ANISOU 1047 CA SER A 362 6222 8342 6316 749 81 -1481 C ATOM 1048 C SER A 362 35.874 31.240 8.199 1.00 68.01 C ANISOU 1048 C SER A 362 7911 10081 7850 744 -40 -1470 C ATOM 1049 O SER A 362 35.513 30.159 8.667 1.00 61.47 O ANISOU 1049 O SER A 362 7107 9313 6935 762 -58 -1344 O ATOM 1050 CB SER A 362 34.953 33.466 8.781 1.00 58.00 C ANISOU 1050 CB SER A 362 6639 8763 6634 774 162 -1651 C ATOM 1051 OG SER A 362 34.438 33.100 10.051 1.00 61.60 O ANISOU 1051 OG SER A 362 7135 9341 6930 818 225 -1628 O ATOM 1052 N VAL A 363 37.153 31.550 8.004 1.00 53.89 N ANISOU 1052 N VAL A 363 6119 8292 6065 722 -121 -1597 N ATOM 1053 CA VAL A 363 38.196 30.633 8.453 1.00 45.12 C ANISOU 1053 CA VAL A 363 5025 7271 4848 740 -248 -1605 C ATOM 1054 C VAL A 363 39.331 31.324 9.183 1.00 77.45 C ANISOU 1054 C VAL A 363 9116 11439 8873 737 -307 -1800 C ATOM 1055 O VAL A 363 39.827 32.367 8.754 1.00 97.86 O ANISOU 1055 O VAL A 363 11661 13963 11559 688 -282 -1937 O ATOM 1056 CB VAL A 363 38.768 29.787 7.316 1.00 58.70 C ANISOU 1056 CB VAL A 363 6714 8928 6660 724 -334 -1533 C ATOM 1057 CG1 VAL A 363 37.737 28.752 6.871 1.00 53.27 C ANISOU 1057 CG1 VAL A 363 6049 8193 5998 730 -323 -1337 C ATOM 1058 CG2 VAL A 363 39.205 30.683 6.174 1.00 63.05 C ANISOU 1058 CG2 VAL A 363 7220 9374 7363 669 -301 -1618 C ATOM 1059 N ASP A 364 39.739 30.704 10.285 1.00 66.78 N ANISOU 1059 N ASP A 364 7814 10214 7347 787 -393 -1807 N ATOM 1060 CA ASP A 364 40.739 31.247 11.193 1.00 41.55 C ANISOU 1060 CA ASP A 364 4624 7114 4051 794 -480 -1993 C ATOM 1061 C ASP A 364 42.139 30.972 10.684 1.00 61.05 C ANISOU 1061 C ASP A 364 7002 9592 6603 778 -621 -2070 C ATOM 1062 O ASP A 364 43.111 31.112 11.422 1.00 62.25 O ANISOU 1062 O ASP A 364 7135 9841 6677 793 -744 -2207 O ATOM 1063 CB ASP A 364 40.597 30.556 12.546 1.00 79.04 C ANISOU 1063 CB ASP A 364 9478 11997 8555 869 -535 -1944 C ATOM 1064 CG ASP A 364 40.909 29.065 12.470 1.00 90.69 C ANISOU 1064 CG ASP A 364 10973 13503 9982 921 -651 -1783 C ATOM 1065 OD1 ASP A 364 41.186 28.443 13.517 0.86 79.53 O ANISOU 1065 OD1 ASP A 364 9649 12199 8371 989 -746 -1754 O ATOM 1066 OD2 ASP A 364 40.887 28.515 11.348 0.53 67.28 O ANISOU 1066 OD2 ASP A 364 7949 10443 7171 900 -651 -1685 O ATOM 1067 N ASN A 365 42.250 30.553 9.432 1.00 56.86 N ANISOU 1067 N ASN A 365 6411 8967 6227 753 -608 -1987 N ATOM 1068 CA ASN A 365 43.532 30.100 8.945 1.00 50.41 C ANISOU 1068 CA ASN A 365 5502 8166 5486 755 -722 -2041 C ATOM 1069 C ASN A 365 43.531 29.798 7.455 1.00 61.95 C ANISOU 1069 C ASN A 365 6920 9508 7112 721 -665 -1960 C ATOM 1070 O ASN A 365 42.704 29.033 6.975 1.00 49.93 O ANISOU 1070 O ASN A 365 5454 7928 5588 745 -634 -1796 O ATOM 1071 CB ASN A 365 43.949 28.858 9.722 1.00 57.60 C ANISOU 1071 CB ASN A 365 6447 9184 6255 853 -873 -1970 C ATOM 1072 CG ASN A 365 45.390 28.527 9.530 1.00 73.56 C ANISOU 1072 CG ASN A 365 8351 11254 8343 878 -1013 -2069 C ATOM 1073 OD1 ASN A 365 45.832 28.246 8.416 1.00 85.84 O ANISOU 1073 OD1 ASN A 365 9827 12737 10050 860 -991 -2053 O ATOM 1074 ND2 ASN A 365 46.151 28.567 10.615 1.00101.78 N ANISOU 1074 ND2 ASN A 365 11910 14956 11805 924 -1159 -2179 N ATOM 1075 N PRO A 366 44.488 30.382 6.727 1.00 66.42 N ANISOU 1075 N PRO A 366 7385 10035 7815 661 -652 -2081 N ATOM 1076 CA PRO A 366 44.669 30.264 5.277 1.00 74.28 C ANISOU 1076 CA PRO A 366 8349 10922 8954 622 -582 -2035 C ATOM 1077 C PRO A 366 44.646 28.825 4.788 1.00 61.57 C ANISOU 1077 C PRO A 366 6764 9303 7325 697 -643 -1895 C ATOM 1078 O PRO A 366 44.246 28.567 3.651 1.00 69.23 O ANISOU 1078 O PRO A 366 7771 10170 8362 680 -578 -1807 O ATOM 1079 CB PRO A 366 46.071 30.842 5.059 1.00 55.81 C ANISOU 1079 CB PRO A 366 5874 8607 6726 566 -596 -2209 C ATOM 1080 CG PRO A 366 46.234 31.810 6.159 1.00 65.77 C ANISOU 1080 CG PRO A 366 7118 9930 7941 529 -625 -2358 C ATOM 1081 CD PRO A 366 45.546 31.197 7.343 1.00 55.42 C ANISOU 1081 CD PRO A 366 5903 8713 6441 620 -709 -2285 C ATOM 1082 N GLN A 367 45.077 27.895 5.630 1.00 74.58 N ANISOU 1082 N GLN A 367 8408 11050 8880 783 -776 -1878 N ATOM 1083 CA GLN A 367 45.227 26.517 5.184 1.00 52.22 C ANISOU 1083 CA GLN A 367 5601 8194 6047 861 -845 -1764 C ATOM 1084 C GLN A 367 43.907 25.757 5.144 1.00 57.65 C ANISOU 1084 C GLN A 367 6420 8818 6668 879 -823 -1575 C ATOM 1085 O GLN A 367 43.843 24.651 4.598 1.00 72.66 O ANISOU 1085 O GLN A 367 8364 10659 8586 924 -862 -1473 O ATOM 1086 CB GLN A 367 46.275 25.779 6.019 1.00 81.59 C ANISOU 1086 CB GLN A 367 9265 12025 9709 960 -1007 -1811 C ATOM 1087 CG GLN A 367 47.709 25.971 5.510 1.00121.36 C ANISOU 1087 CG GLN A 367 14137 17095 14881 962 -1037 -1962 C ATOM 1088 CD GLN A 367 48.130 27.432 5.450 1.00112.19 C ANISOU 1088 CD GLN A 367 12873 15948 13805 845 -957 -2131 C ATOM 1089 OE1 GLN A 367 48.348 28.077 6.481 0.59 77.25 O ANISOU 1089 OE1 GLN A 367 8420 11612 9320 828 -1022 -2237 O ATOM 1090 NE2 GLN A 367 48.258 27.958 4.236 0.55 91.90 N ANISOU 1090 NE2 GLN A 367 10264 13282 11371 763 -815 -2158 N ATOM 1091 N LYS A 368 42.861 26.362 5.709 1.00 61.64 N ANISOU 1091 N LYS A 368 6979 9329 7111 840 -754 -1539 N ATOM 1092 CA LYS A 368 41.500 25.814 5.666 1.00 49.97 C ANISOU 1092 CA LYS A 368 5592 7793 5600 835 -709 -1369 C ATOM 1093 C LYS A 368 40.837 25.953 4.290 1.00 60.36 C ANISOU 1093 C LYS A 368 6917 8978 7038 779 -634 -1311 C ATOM 1094 O LYS A 368 39.749 25.419 4.059 1.00 70.86 O ANISOU 1094 O LYS A 368 8300 10249 8373 766 -616 -1175 O ATOM 1095 CB LYS A 368 40.628 26.499 6.711 1.00 63.63 C ANISOU 1095 CB LYS A 368 7357 9583 7238 819 -640 -1366 C ATOM 1096 CG LYS A 368 41.216 26.495 8.104 1.00 56.48 C ANISOU 1096 CG LYS A 368 6472 8812 6178 873 -715 -1434 C ATOM 1097 CD LYS A 368 40.846 25.230 8.839 1.00 65.91 C ANISOU 1097 CD LYS A 368 7762 10040 7242 934 -774 -1276 C ATOM 1098 CE LYS A 368 40.946 25.430 10.343 1.00 68.43 C ANISOU 1098 CE LYS A 368 8147 10492 7363 980 -805 -1315 C ATOM 1099 NZ LYS A 368 39.860 26.303 10.840 1.00 60.17 N ANISOU 1099 NZ LYS A 368 7130 9463 6269 937 -654 -1323 N ATOM 1100 N VAL A 369 41.483 26.677 3.382 1.00 44.18 N ANISOU 1100 N VAL A 369 4818 6884 5084 741 -591 -1412 N ATOM 1101 CA VAL A 369 40.962 26.814 2.032 1.00 57.63 C ANISOU 1101 CA VAL A 369 6554 8466 6876 698 -533 -1360 C ATOM 1102 C VAL A 369 41.892 26.171 1.021 1.00 38.70 C ANISOU 1102 C VAL A 369 4154 6024 4527 717 -562 -1383 C ATOM 1103 O VAL A 369 42.976 26.663 0.771 1.00 78.29 O ANISOU 1103 O VAL A 369 9100 11061 9586 705 -533 -1503 O ATOM 1104 CB VAL A 369 40.792 28.269 1.643 1.00 59.66 C ANISOU 1104 CB VAL A 369 6792 8678 7197 636 -429 -1435 C ATOM 1105 CG1 VAL A 369 40.206 28.344 0.255 1.00 49.36 C ANISOU 1105 CG1 VAL A 369 5547 7249 5958 606 -390 -1362 C ATOM 1106 CG2 VAL A 369 39.909 28.984 2.660 1.00 51.05 C ANISOU 1106 CG2 VAL A 369 5702 7629 6066 632 -386 -1435 C ATOM 1107 N LEU A 370 41.445 25.072 0.433 1.00 74.09 N ANISOU 1107 N LEU A 370 8707 10437 9005 743 -611 -1275 N ATOM 1108 CA LEU A 370 42.259 24.307 -0.496 1.00 55.57 C ANISOU 1108 CA LEU A 370 6380 8044 6692 779 -636 -1297 C ATOM 1109 C LEU A 370 41.856 24.583 -1.950 1.00 77.14 C ANISOU 1109 C LEU A 370 9183 10661 9465 732 -574 -1275 C ATOM 1110 O LEU A 370 40.767 24.202 -2.385 1.00 53.57 O ANISOU 1110 O LEU A 370 6280 7601 6474 714 -606 -1170 O ATOM 1111 CB LEU A 370 42.114 22.818 -0.175 1.00 45.77 C ANISOU 1111 CB LEU A 370 5196 6785 5411 847 -744 -1203 C ATOM 1112 CG LEU A 370 42.900 21.822 -1.024 1.00 58.60 C ANISOU 1112 CG LEU A 370 6854 8347 7064 911 -782 -1224 C ATOM 1113 CD1 LEU A 370 44.402 21.958 -0.767 0.69 21.54 C ANISOU 1113 CD1 LEU A 370 2045 3742 2399 972 -782 -1358 C ATOM 1114 CD2 LEU A 370 42.414 20.413 -0.729 0.45 36.28 C ANISOU 1114 CD2 LEU A 370 4119 5461 4206 960 -886 -1105 C ATOM 1115 N LEU A 371 42.724 25.258 -2.699 1.00 59.01 N ANISOU 1115 N LEU A 371 6858 8353 7208 709 -488 -1373 N ATOM 1116 CA LEU A 371 42.470 25.466 -4.120 1.00 68.67 C ANISOU 1116 CA LEU A 371 8180 9471 8441 675 -427 -1350 C ATOM 1117 C LEU A 371 42.742 24.180 -4.908 1.00 50.45 C ANISOU 1117 C LEU A 371 5952 7107 6110 733 -477 -1328 C ATOM 1118 O LEU A 371 43.850 23.657 -4.883 1.00 64.77 O ANISOU 1118 O LEU A 371 7710 8958 7940 789 -469 -1404 O ATOM 1119 CB LEU A 371 43.340 26.595 -4.670 1.00 40.74 C ANISOU 1119 CB LEU A 371 4603 5930 4946 623 -292 -1451 C ATOM 1120 CG LEU A 371 43.428 27.925 -3.928 1.00 53.51 C ANISOU 1120 CG LEU A 371 6136 7589 6604 563 -229 -1516 C ATOM 1121 CD1 LEU A 371 44.119 28.933 -4.822 0.88 61.75 C ANISOU 1121 CD1 LEU A 371 7187 8579 7697 493 -84 -1584 C ATOM 1122 CD2 LEU A 371 42.076 28.444 -3.509 1.00 46.17 C ANISOU 1122 CD2 LEU A 371 5252 6630 5658 545 -257 -1432 C ATOM 1123 N MET A 372 41.744 23.692 -5.633 1.00 61.00 N ANISOU 1123 N MET A 372 7227 5787 10164 -192 -2056 -1220 N ATOM 1124 CA MET A 372 41.885 22.430 -6.360 1.00 67.82 C ANISOU 1124 CA MET A 372 7866 6669 11232 -218 -1948 -1335 C ATOM 1125 C MET A 372 41.981 22.548 -7.893 1.00 78.22 C ANISOU 1125 C MET A 372 9144 8091 12484 -216 -1765 -1466 C ATOM 1126 O MET A 372 42.362 21.593 -8.570 1.00 84.92 O ANISOU 1126 O MET A 372 9796 8939 13531 -260 -1657 -1586 O ATOM 1127 CB MET A 372 40.745 21.490 -5.969 1.00 72.81 C ANISOU 1127 CB MET A 372 8440 7378 11848 -157 -1975 -1372 C ATOM 1128 CG MET A 372 40.657 21.265 -4.466 1.00 48.29 C ANISOU 1128 CG MET A 372 5349 4195 8805 -164 -2146 -1232 C ATOM 1129 SD MET A 372 39.157 20.415 -3.981 1.00 90.70 S ANISOU 1129 SD MET A 372 10692 9670 14100 -73 -2174 -1246 S ATOM 1130 CE MET A 372 39.346 18.858 -4.852 1.00 71.27 C ANISOU 1130 CE MET A 372 7923 7184 11971 -106 -2042 -1394 C ATOM 1131 N GLY A 373 41.644 23.711 -8.441 1.00 55.37 N ANISOU 1131 N GLY A 373 6425 5291 9320 -168 -1725 -1441 N ATOM 1132 CA GLY A 373 41.690 23.889 -9.880 1.00 69.78 C ANISOU 1132 CA GLY A 373 8219 7253 11041 -166 -1558 -1537 C ATOM 1133 C GLY A 373 40.430 24.519 -10.444 1.00 54.85 C ANISOU 1133 C GLY A 373 6471 5560 8811 -67 -1524 -1543 C ATOM 1134 O GLY A 373 39.601 25.025 -9.693 1.00 76.86 O ANISOU 1134 O GLY A 373 9404 8349 11449 1 -1627 -1461 O ATOM 1135 N ASP A 374 40.290 24.482 -11.768 1.00 55.69 N ANISOU 1135 N ASP A 374 6525 5841 8793 -64 -1379 -1639 N ATOM 1136 CA ASP A 374 39.167 25.109 -12.458 1.00 41.25 C ANISOU 1136 CA ASP A 374 4810 4223 6639 21 -1342 -1627 C ATOM 1137 C ASP A 374 37.997 24.160 -12.649 1.00 57.85 C ANISOU 1137 C ASP A 374 6841 6474 8665 71 -1334 -1762 C ATOM 1138 O ASP A 374 38.186 22.995 -13.010 1.00 63.64 O ANISOU 1138 O ASP A 374 7390 7232 9559 24 -1267 -1928 O ATOM 1139 CB ASP A 374 39.598 25.637 -13.829 1.00 49.77 C ANISOU 1139 CB ASP A 374 5870 5453 7587 -4 -1194 -1638 C ATOM 1140 CG ASP A 374 40.505 26.847 -13.734 0.09 52.47 C ANISOU 1140 CG ASP A 374 6313 5670 7954 -28 -1199 -1470 C ATOM 1141 OD1 ASP A 374 40.585 27.448 -12.641 0.58 54.98 O ANISOU 1141 OD1 ASP A 374 6746 5812 8333 -11 -1324 -1352 O ATOM 1142 OD2 ASP A 374 41.132 27.201 -14.756 0.34 44.11 O ANISOU 1142 OD2 ASP A 374 5211 4696 6852 -67 -1072 -1462 O ATOM 1143 N ALA A 375 36.787 24.677 -12.427 1.00 52.03 N ANISOU 1143 N ALA A 375 6239 5828 7701 166 -1396 -1695 N ATOM 1144 CA ALA A 375 35.556 23.922 -12.658 1.00 66.12 C ANISOU 1144 CA ALA A 375 7970 7766 9386 224 -1393 -1809 C ATOM 1145 C ALA A 375 35.215 23.936 -14.139 1.00 72.06 C ANISOU 1145 C ALA A 375 8668 8780 9931 224 -1269 -1909 C ATOM 1146 O ALA A 375 34.600 24.881 -14.631 1.00 94.62 O ANISOU 1146 O ALA A 375 11644 11778 12528 283 -1263 -1807 O ATOM 1147 CB ALA A 375 34.401 24.504 -11.843 0.84 51.06 C ANISOU 1147 CB ALA A 375 6225 5852 7325 324 -1502 -1691 C ATOM 1148 N VAL A 376 35.614 22.881 -14.841 1.00 64.41 N ANISOU 1148 N VAL A 376 7508 7882 9085 156 -1168 -2109 N ATOM 1149 CA VAL A 376 35.504 22.840 -16.293 1.00 61.05 C ANISOU 1149 CA VAL A 376 7009 7723 8463 131 -1037 -2231 C ATOM 1150 C VAL A 376 34.052 22.832 -16.754 1.00 69.73 C ANISOU 1150 C VAL A 376 8141 9058 9296 209 -1059 -2269 C ATOM 1151 O VAL A 376 33.772 23.164 -17.903 1.00 76.91 O ANISOU 1151 O VAL A 376 9043 10228 9952 206 -982 -2298 O ATOM 1152 CB VAL A 376 36.270 21.628 -16.896 1.00 66.58 C ANISOU 1152 CB VAL A 376 7480 8436 9383 30 -913 -2478 C ATOM 1153 CG1 VAL A 376 35.598 20.333 -16.519 0.42 69.41 C ANISOU 1153 CG1 VAL A 376 7693 8762 9917 40 -940 -2656 C ATOM 1154 CG2 VAL A 376 36.351 21.741 -18.399 0.83 70.59 C ANISOU 1154 CG2 VAL A 376 7925 9234 9660 -12 -766 -2597 C ATOM 1155 N ASP A 377 33.133 22.489 -15.849 1.00 95.86 N ANISOU 1155 N ASP A 377 11482 12284 12657 277 -1167 -2252 N ATOM 1156 CA ASP A 377 31.713 22.343 -16.196 1.00 54.14 C ANISOU 1156 CA ASP A 377 6206 7198 7166 351 -1196 -2300 C ATOM 1157 C ASP A 377 30.761 23.432 -15.686 1.00 69.93 C ANISOU 1157 C ASP A 377 8404 9198 8969 458 -1295 -2080 C ATOM 1158 O ASP A 377 29.546 23.302 -15.862 1.00 65.12 O ANISOU 1158 O ASP A 377 7797 8728 8215 525 -1329 -2104 O ATOM 1159 CB ASP A 377 31.193 20.987 -15.731 1.00 70.76 C ANISOU 1159 CB ASP A 377 8160 9243 9484 353 -1221 -2477 C ATOM 1160 CG ASP A 377 31.822 19.832 -16.479 1.00 91.27 C ANISOU 1160 CG ASP A 377 10529 11892 12257 256 -1102 -2742 C ATOM 1161 OD1 ASP A 377 32.410 18.949 -15.815 1.00 74.60 O ANISOU 1161 OD1 ASP A 377 8292 9570 10482 212 -1103 -2812 O ATOM 1162 OD2 ASP A 377 31.729 19.808 -17.725 1.00 84.15 O ANISOU 1162 OD2 ASP A 377 9563 11246 11163 221 -1006 -2878 O ATOM 1163 N LEU A 378 31.283 24.491 -15.061 1.00 49.06 N ANISOU 1163 N LEU A 378 5912 6394 6335 473 -1338 -1879 N ATOM 1164 CA LEU A 378 30.416 25.581 -14.607 1.00 64.14 C ANISOU 1164 CA LEU A 378 7999 8289 8083 570 -1415 -1685 C ATOM 1165 C LEU A 378 29.776 26.294 -15.807 1.00 72.27 C ANISOU 1165 C LEU A 378 9054 9583 8820 608 -1366 -1616 C ATOM 1166 O LEU A 378 30.465 26.947 -16.583 1.00 67.72 O ANISOU 1166 O LEU A 378 8487 9088 8156 568 -1296 -1542 O ATOM 1167 CB LEU A 378 31.184 26.580 -13.728 1.00 58.43 C ANISOU 1167 CB LEU A 378 7417 7334 7451 566 -1461 -1511 C ATOM 1168 CG LEU A 378 30.470 27.909 -13.401 1.00 65.89 C ANISOU 1168 CG LEU A 378 8538 8251 8246 655 -1510 -1312 C ATOM 1169 CD1 LEU A 378 29.215 27.710 -12.546 1.00 50.80 C ANISOU 1169 CD1 LEU A 378 6684 6307 6312 743 -1593 -1307 C ATOM 1170 CD2 LEU A 378 31.406 28.894 -12.719 1.00 39.59 C ANISOU 1170 CD2 LEU A 378 5319 4703 5022 630 -1535 -1179 C ATOM 1171 N GLY A 379 28.460 26.173 -15.965 1.00 83.87 N ANISOU 1171 N GLY A 379 10527 11195 10145 682 -1406 -1624 N ATOM 1172 CA GLY A 379 27.817 26.678 -17.168 1.00 68.88 C ANISOU 1172 CA GLY A 379 8619 9584 7969 708 -1369 -1567 C ATOM 1173 C GLY A 379 26.426 27.258 -17.012 1.00 64.28 C ANISOU 1173 C GLY A 379 8120 9065 7238 818 -1441 -1432 C ATOM 1174 O GLY A 379 25.890 27.369 -15.910 1.00 77.61 O ANISOU 1174 O GLY A 379 9894 10565 9031 883 -1514 -1378 O ATOM 1175 N THR A 380 25.839 27.633 -18.142 1.00 84.18 N ANISOU 1175 N THR A 380 10607 11866 9509 835 -1416 -1373 N ATOM 1176 CA THR A 380 24.514 28.240 -18.166 1.00 70.51 C ANISOU 1176 CA THR A 380 8936 10221 7633 936 -1480 -1223 C ATOM 1177 C THR A 380 23.533 27.425 -18.998 1.00 89.24 C ANISOU 1177 C THR A 380 11178 12884 9843 939 -1492 -1369 C ATOM 1178 O THR A 380 23.913 26.843 -20.017 1.00 83.19 O ANISOU 1178 O THR A 380 10288 12353 8967 859 -1431 -1523 O ATOM 1179 CB THR A 380 24.578 29.663 -18.744 1.00 79.01 C ANISOU 1179 CB THR A 380 10090 11372 8557 966 -1458 -946 C ATOM 1180 OG1 THR A 380 24.854 30.591 -17.690 1.00 78.71 O ANISOU 1180 OG1 THR A 380 10196 11030 8681 1012 -1483 -783 O ATOM 1181 CG2 THR A 380 23.258 30.041 -19.407 1.00 96.31 C ANISOU 1181 CG2 THR A 380 12260 13800 10532 1040 -1499 -823 C ATOM 1182 N CYS A 381 22.273 27.387 -18.567 1.00 74.48 N ANISOU 1182 N CYS A 381 9332 11003 7964 1029 -1569 -1333 N ATOM 1183 CA CYS A 381 21.231 26.737 -19.351 1.00 70.21 C ANISOU 1183 CA CYS A 381 8670 10740 7267 1039 -1596 -1449 C ATOM 1184 C CYS A 381 21.318 27.174 -20.810 1.00 88.87 C ANISOU 1184 C CYS A 381 10971 13456 9341 993 -1556 -1386 C ATOM 1185 O CYS A 381 21.389 28.367 -21.109 1.00100.62 O ANISOU 1185 O CYS A 381 12539 14981 10712 1024 -1550 -1121 O ATOM 1186 CB CYS A 381 19.845 27.050 -18.789 1.00 73.46 C ANISOU 1186 CB CYS A 381 9137 11096 7677 1155 -1681 -1328 C ATOM 1187 SG CYS A 381 18.512 26.156 -19.609 1.00 87.92 S ANISOU 1187 SG CYS A 381 10808 13236 9360 1168 -1732 -1487 S ATOM 1188 N LYS A 382 21.314 26.195 -21.711 1.00104.99 N ANISOU 1188 N LYS A 382 12856 15761 11275 916 -1523 -1631 N ATOM 1189 CA LYS A 382 21.473 26.435 -23.145 1.00106.25 C ANISOU 1189 CA LYS A 382 12935 16303 11132 851 -1476 -1616 C ATOM 1190 C LYS A 382 20.174 26.927 -23.792 0.35111.37 C ANISOU 1190 C LYS A 382 13563 17225 11529 914 -1557 -1457 C ATOM 1191 O LYS A 382 20.175 27.400 -24.929 1.00106.49 O ANISOU 1191 O LYS A 382 12896 16938 10627 877 -1537 -1351 O ATOM 1192 CB LYS A 382 21.959 25.154 -23.833 1.00 63.86 C ANISOU 1192 CB LYS A 382 7396 11115 5750 735 -1403 -1979 C ATOM 1193 CG LYS A 382 22.183 25.271 -25.323 1.00103.65 C ANISOU 1193 CG LYS A 382 12340 16584 10459 651 -1341 -2013 C ATOM 1194 CD LYS A 382 22.531 23.917 -25.931 1.00128.48 C ANISOU 1194 CD LYS A 382 15304 19896 13616 537 -1264 -2424 C ATOM 1195 CE LYS A 382 23.020 24.055 -27.370 1.00131.46 C ANISOU 1195 CE LYS A 382 15594 20693 13664 434 -1173 -2477 C ATOM 1196 NZ LYS A 382 21.986 24.631 -28.275 1.00124.74 N ANISOU 1196 NZ LYS A 382 14722 20234 12440 461 -1249 -2311 N ATOM 1197 N ALA A 383 19.069 26.820 -23.061 1.00100.89 N ANISOU 1197 N ALA A 383 12265 15764 10306 1007 -1647 -1427 N ATOM 1198 CA ALA A 383 17.765 27.227 -23.580 1.00 96.46 C ANISOU 1198 CA ALA A 383 11672 15431 9547 1072 -1733 -1276 C ATOM 1199 C ALA A 383 17.596 28.742 -23.672 1.00 97.33 C ANISOU 1199 C ALA A 383 11890 15529 9564 1143 -1752 -876 C ATOM 1200 O ALA A 383 18.499 29.506 -23.322 1.00 78.59 O ANISOU 1200 O ALA A 383 9618 12959 7282 1142 -1695 -723 O ATOM 1201 CB ALA A 383 16.650 26.625 -22.741 1.00 94.35 C ANISOU 1201 CB ALA A 383 11394 15004 9450 1151 -1813 -1368 C ATOM 1202 N ARG A 384 16.427 29.158 -24.156 1.00102.57 N ANISOU 1202 N ARG A 384 12513 16395 10065 1203 -1832 -708 N ATOM 1203 CA ARG A 384 16.075 30.572 -24.273 1.00107.81 C ANISOU 1203 CA ARG A 384 13246 17048 10670 1280 -1856 -310 C ATOM 1204 C ARG A 384 14.787 30.909 -23.523 1.00110.54 C ANISOU 1204 C ARG A 384 13633 17217 11149 1404 -1940 -173 C ATOM 1205 O ARG A 384 13.779 30.211 -23.669 1.00 83.78 O ANISOU 1205 O ARG A 384 10156 13964 7711 1423 -2013 -298 O ATOM 1206 CB ARG A 384 15.937 30.962 -25.743 1.00 93.47 C ANISOU 1206 CB ARG A 384 11321 15687 8507 1230 -1867 -157 C ATOM 1207 CG ARG A 384 17.040 31.865 -26.240 1.00115.87 C ANISOU 1207 CG ARG A 384 14195 18566 11264 1187 -1779 57 C ATOM 1208 CD ARG A 384 17.328 31.623 -27.708 1.00120.54 C ANISOU 1208 CD ARG A 384 14653 19649 11496 1081 -1752 21 C ATOM 1209 NE ARG A 384 17.841 32.821 -28.364 0.24146.33 N ANISOU 1209 NE ARG A 384 17930 23037 14633 1077 -1705 383 N ATOM 1210 CZ ARG A 384 18.940 33.468 -27.988 1.00157.20 C ANISOU 1210 CZ ARG A 384 19396 24161 16170 1071 -1612 501 C ATOM 1211 NH1 ARG A 384 19.329 34.548 -28.651 1.00169.85 N ANISOU 1211 NH1 ARG A 384 20986 25890 17661 1070 -1570 847 N ATOM 1212 NH2 ARG A 384 19.642 33.044 -26.945 1.00138.15 N ANISOU 1212 NH2 ARG A 384 17078 21371 14042 1066 -1567 288 N ATOM 1213 N LYS A 385 14.829 31.975 -22.724 1.00111.16 N ANISOU 1213 N LYS A 385 13839 16988 11409 1485 -1924 72 N ATOM 1214 CA LYS A 385 13.678 32.409 -21.934 1.00105.31 C ANISOU 1214 CA LYS A 385 13146 16043 10823 1605 -1981 210 C ATOM 1215 C LYS A 385 12.454 32.618 -22.808 1.00135.53 C ANISOU 1215 C LYS A 385 16858 20171 14464 1645 -2066 375 C ATOM 1216 O LYS A 385 12.358 33.636 -23.486 1.00119.76 O ANISOU 1216 O LYS A 385 14837 18310 12357 1664 -2071 684 O ATOM 1217 CB LYS A 385 13.977 33.723 -21.214 1.00 85.06 C ANISOU 1217 CB LYS A 385 10711 13160 8446 1672 -1936 475 C ATOM 1218 CG LYS A 385 14.682 33.611 -19.872 1.00 74.61 C ANISOU 1218 CG LYS A 385 9523 11446 7381 1676 -1885 332 C ATOM 1219 CD LYS A 385 14.380 34.849 -19.021 1.00 91.12 C ANISOU 1219 CD LYS A 385 11724 13224 9675 1771 -1866 567 C ATOM 1220 CE LYS A 385 15.644 35.457 -18.421 1.00121.68 C ANISOU 1220 CE LYS A 385 15706 16833 13695 1735 -1792 585 C ATOM 1221 NZ LYS A 385 16.509 36.075 -19.472 1.00109.07 N ANISOU 1221 NZ LYS A 385 14063 15407 11970 1674 -1748 753 N ATOM 1222 N LYS A 386 11.523 31.663 -22.760 1.00166.76 N ANISOU 1222 N LYS A 386 20734 24219 18407 1660 -2135 182 N ATOM 1223 CA LYS A 386 10.296 31.651 -23.571 1.00165.23 C ANISOU 1223 CA LYS A 386 20413 24329 18040 1689 -2234 287 C ATOM 1224 C LYS A 386 9.690 33.039 -23.779 1.00142.94 C ANISOU 1224 C LYS A 386 17599 21497 15215 1775 -2262 711 C ATOM 1225 O LYS A 386 8.592 33.327 -23.302 1.00133.72 O ANISOU 1225 O LYS A 386 16428 20197 14181 1874 -2312 833 O ATOM 1226 CB LYS A 386 9.248 30.748 -22.909 1.00176.26 C ANISOU 1226 CB LYS A 386 21773 25619 19579 1742 -2294 87 C ATOM 1227 CG LYS A 386 9.828 29.702 -21.969 1.00160.32 C ANISOU 1227 CG LYS A 386 19803 23354 17756 1712 -2241 -244 C ATOM 1228 CD LYS A 386 8.731 28.950 -21.227 1.00149.39 C ANISOU 1228 CD LYS A 386 18384 21833 16545 1781 -2292 -381 C ATOM 1229 CE LYS A 386 7.760 29.902 -20.533 1.00132.07 C ANISOU 1229 CE LYS A 386 16262 19421 14496 1912 -2314 -107 C ATOM 1230 NZ LYS A 386 6.683 30.395 -21.442 1.00118.15 N ANISOU 1230 NZ LYS A 386 14390 17925 12575 1951 -2403 110 N ATOM 1231 N ASN A 387 10.397 33.876 -24.524 1.00134.21 N ANISOU 1231 N ASN A 387 16488 20536 13969 1735 -2224 940 N ATOM 1232 CA ASN A 387 10.117 35.300 -24.573 1.00112.80 C ANISOU 1232 CA ASN A 387 13796 17730 11334 1814 -2219 1359 C ATOM 1233 C ASN A 387 11.087 35.960 -25.533 1.00 95.36 C ANISOU 1233 C ASN A 387 11557 15738 8939 1743 -2168 1558 C ATOM 1234 O ASN A 387 10.716 36.356 -26.627 1.00126.47 O ANISOU 1234 O ASN A 387 15376 20030 12646 1726 -2219 1797 O ATOM 1235 CB ASN A 387 10.269 35.923 -23.188 1.00119.95 C ANISOU 1235 CB ASN A 387 14853 18129 12593 1898 -2151 1402 C ATOM 1236 N GLY A 388 12.336 36.087 -25.112 1.00 99.63 N ANISOU 1236 N GLY A 388 12201 16071 9585 1700 -2067 1473 N ATOM 1237 CA GLY A 388 13.404 36.458 -26.020 1.00116.47 C ANISOU 1237 CA GLY A 388 14300 18418 11534 1614 -2003 1587 C ATOM 1238 C GLY A 388 14.716 35.891 -25.511 1.00133.29 C ANISOU 1238 C GLY A 388 16524 20364 13755 1539 -1910 1297 C ATOM 1239 O GLY A 388 14.962 34.690 -25.580 1.00137.19 O ANISOU 1239 O GLY A 388 16992 20971 14163 1466 -1911 947 O ATOM 1240 N ASP A 389 15.568 36.786 -25.035 1.00121.93 N ANISOU 1240 N ASP A 389 15179 18640 12509 1554 -1830 1454 N ATOM 1241 CA ASP A 389 16.712 36.485 -24.180 1.00109.78 C ANISOU 1241 CA ASP A 389 13755 16796 11163 1512 -1753 1229 C ATOM 1242 C ASP A 389 17.056 35.026 -23.837 1.00126.04 C ANISOU 1242 C ASP A 389 15819 18858 13211 1442 -1753 798 C ATOM 1243 O ASP A 389 16.183 34.172 -23.715 1.00118.56 O ANISOU 1243 O ASP A 389 14827 17993 12227 1459 -1820 615 O ATOM 1244 CB ASP A 389 16.482 37.224 -22.868 1.00131.15 C ANISOU 1244 CB ASP A 389 16585 19042 14203 1609 -1745 1319 C ATOM 1245 CG ASP A 389 15.744 38.543 -23.064 1.00151.36 C ANISOU 1245 CG ASP A 389 19115 21559 16834 1701 -1759 1718 C ATOM 1246 OD1 ASP A 389 16.278 39.429 -23.756 0.76149.78 O ANISOU 1246 OD1 ASP A 389 18873 21445 16592 1684 -1712 1991 O ATOM 1247 OD2 ASP A 389 14.627 38.696 -22.526 1.00143.01 O ANISOU 1247 OD2 ASP A 389 18067 20377 15894 1792 -1811 1768 O ATOM 1248 N PRO A 390 18.347 34.761 -23.605 1.00128.67 N ANISOU 1248 N PRO A 390 16200 19066 13620 1367 -1673 643 N ATOM 1249 CA PRO A 390 18.810 33.403 -23.329 1.00101.16 C ANISOU 1249 CA PRO A 390 12701 15575 10161 1293 -1660 256 C ATOM 1250 C PRO A 390 18.628 33.108 -21.849 1.00105.43 C ANISOU 1250 C PRO A 390 13348 15720 10991 1349 -1685 120 C ATOM 1251 O PRO A 390 18.732 34.029 -21.035 1.00 94.56 O ANISOU 1251 O PRO A 390 12081 14044 9803 1410 -1674 289 O ATOM 1252 CB PRO A 390 20.305 33.472 -23.672 1.00 95.11 C ANISOU 1252 CB PRO A 390 11940 14808 9388 1196 -1559 218 C ATOM 1253 CG PRO A 390 20.573 34.926 -24.092 1.00119.96 C ANISOU 1253 CG PRO A 390 15113 17955 12512 1228 -1523 604 C ATOM 1254 CD PRO A 390 19.453 35.723 -23.534 1.00125.43 C ANISOU 1254 CD PRO A 390 15854 18486 13318 1348 -1591 828 C ATOM 1255 N CYS A 391 18.343 31.859 -21.497 1.00 79.12 N ANISOU 1255 N CYS A 391 9975 12389 7698 1328 -1715 -178 N ATOM 1256 CA CYS A 391 18.207 31.520 -20.089 1.00 92.92 C ANISOU 1256 CA CYS A 391 11814 13787 9706 1375 -1735 -296 C ATOM 1257 C CYS A 391 19.505 31.786 -19.338 1.00 79.82 C ANISOU 1257 C CYS A 391 10254 11844 8232 1333 -1676 -318 C ATOM 1258 O CYS A 391 20.595 31.630 -19.884 1.00125.27 O ANISOU 1258 O CYS A 391 15975 17681 13941 1244 -1615 -379 O ATOM 1259 CB CYS A 391 17.774 30.072 -19.879 1.00 94.79 C ANISOU 1259 CB CYS A 391 11966 14075 9976 1353 -1769 -603 C ATOM 1260 SG CYS A 391 17.711 29.657 -18.120 1.00 77.69 S ANISOU 1260 SG CYS A 391 9904 11494 8121 1404 -1788 -714 S ATOM 1261 N THR A 392 19.370 32.168 -18.075 1.00 78.61 N ANISOU 1261 N THR A 392 10217 11364 8286 1395 -1694 -278 N ATOM 1262 CA THR A 392 20.500 32.589 -17.257 1.00 89.10 C ANISOU 1262 CA THR A 392 11649 12411 9795 1363 -1655 -271 C ATOM 1263 C THR A 392 20.746 31.641 -16.068 1.00 83.31 C ANISOU 1263 C THR A 392 10948 11462 9242 1344 -1677 -495 C ATOM 1264 O THR A 392 21.565 31.916 -15.195 1.00 78.63 O ANISOU 1264 O THR A 392 10443 10624 8808 1321 -1665 -502 O ATOM 1265 CB THR A 392 20.261 34.027 -16.733 1.00 99.51 C ANISOU 1265 CB THR A 392 13079 13519 11211 1440 -1650 -17 C ATOM 1266 OG1 THR A 392 21.514 34.658 -16.441 1.00103.05 O ANISOU 1266 OG1 THR A 392 13594 13782 11778 1389 -1600 32 O ATOM 1267 CG2 THR A 392 19.363 34.018 -15.482 1.00 90.56 C ANISOU 1267 CG2 THR A 392 12027 12162 10220 1524 -1693 -52 C ATOM 1268 N GLN A 393 20.034 30.522 -16.038 1.00 92.19 N ANISOU 1268 N GLN A 393 11992 12686 10351 1353 -1714 -669 N ATOM 1269 CA GLN A 393 20.086 29.628 -14.889 1.00 55.43 C ANISOU 1269 CA GLN A 393 7350 7835 5875 1349 -1740 -841 C ATOM 1270 C GLN A 393 21.401 28.863 -14.855 1.00 63.89 C ANISOU 1270 C GLN A 393 8370 8860 7044 1241 -1704 -1008 C ATOM 1271 O GLN A 393 21.895 28.421 -15.894 1.00 76.47 O ANISOU 1271 O GLN A 393 9858 10653 8545 1169 -1662 -1099 O ATOM 1272 CB GLN A 393 18.903 28.658 -14.918 1.00 49.87 C ANISOU 1272 CB GLN A 393 6552 7245 5151 1393 -1783 -964 C ATOM 1273 CG GLN A 393 18.657 27.963 -13.595 1.00 81.55 C ANISOU 1273 CG GLN A 393 10591 11040 9354 1420 -1813 -1065 C ATOM 1274 CD GLN A 393 17.701 28.732 -12.703 1.00 80.42 C ANISOU 1274 CD GLN A 393 10564 10745 9246 1527 -1840 -917 C ATOM 1275 OE1 GLN A 393 16.907 29.549 -13.179 1.00 60.49 O ANISOU 1275 OE1 GLN A 393 8062 8304 6617 1592 -1846 -765 O ATOM 1276 NE2 GLN A 393 17.763 28.464 -11.402 1.00 73.27 N ANISOU 1276 NE2 GLN A 393 9723 9624 8492 1542 -1854 -959 N ATOM 1277 N MET A 394 21.969 28.702 -13.662 1.00 70.02 N ANISOU 1277 N MET A 394 9214 9383 8007 1226 -1720 -1047 N ATOM 1278 CA MET A 394 23.261 28.027 -13.535 1.00 51.02 C ANISOU 1278 CA MET A 394 6754 6903 5729 1125 -1692 -1179 C ATOM 1279 C MET A 394 23.118 26.535 -13.712 1.00 63.99 C ANISOU 1279 C MET A 394 8238 8632 7442 1086 -1691 -1401 C ATOM 1280 O MET A 394 22.118 25.945 -13.308 1.00 90.14 O ANISOU 1280 O MET A 394 11516 11948 10786 1142 -1731 -1455 O ATOM 1281 CB MET A 394 23.912 28.310 -12.189 1.00 44.27 C ANISOU 1281 CB MET A 394 6007 5766 5047 1115 -1723 -1140 C ATOM 1282 CG MET A 394 25.319 27.766 -12.095 0.89 53.68 C ANISOU 1282 CG MET A 394 7142 6874 6381 1008 -1699 -1237 C ATOM 1283 SD MET A 394 26.066 28.139 -10.521 0.76 58.50 S ANISOU 1283 SD MET A 394 7872 7186 7170 988 -1755 -1180 S ATOM 1284 CE MET A 394 25.918 29.926 -10.491 0.39 37.50 C ANISOU 1284 CE MET A 394 5381 4455 4411 1044 -1746 -976 C ATOM 1285 N VAL A 395 24.140 25.922 -14.292 1.00 86.48 N ANISOU 1285 N VAL A 395 10982 11534 10343 988 -1637 -1532 N ATOM 1286 CA VAL A 395 24.026 24.548 -14.752 1.00 83.29 C ANISOU 1286 CA VAL A 395 10397 11245 10006 941 -1613 -1764 C ATOM 1287 C VAL A 395 25.341 23.790 -14.673 1.00 62.40 C ANISOU 1287 C VAL A 395 7653 8496 7559 836 -1563 -1902 C ATOM 1288 O VAL A 395 26.417 24.386 -14.743 1.00 90.53 O ANISOU 1288 O VAL A 395 11270 11988 11137 785 -1529 -1829 O ATOM 1289 CB VAL A 395 23.504 24.527 -16.203 1.00 60.84 C ANISOU 1289 CB VAL A 395 7465 8724 6926 931 -1575 -1826 C ATOM 1290 CG1 VAL A 395 24.232 23.501 -17.027 0.85 42.16 C ANISOU 1290 CG1 VAL A 395 4925 6485 4610 825 -1497 -2069 C ATOM 1291 CG2 VAL A 395 21.997 24.305 -16.217 1.00 57.48 C ANISOU 1291 CG2 VAL A 395 7015 8406 6416 1017 -1634 -1832 C ATOM 1292 N ASN A 396 25.249 22.475 -14.502 1.00 69.65 N ANISOU 1292 N ASN A 396 8416 9390 8660 806 -1558 -2095 N ATOM 1293 CA ASN A 396 26.418 21.606 -14.606 1.00 60.42 C ANISOU 1293 CA ASN A 396 7107 8143 7707 703 -1496 -2251 C ATOM 1294 C ASN A 396 26.500 21.010 -16.011 1.00 71.87 C ANISOU 1294 C ASN A 396 8395 9844 9067 636 -1403 -2467 C ATOM 1295 O ASN A 396 25.791 20.058 -16.332 1.00 68.71 O ANISOU 1295 O ASN A 396 7852 9545 8710 638 -1395 -2651 O ATOM 1296 CB ASN A 396 26.369 20.497 -13.548 1.00 73.85 C ANISOU 1296 CB ASN A 396 8706 9644 9708 702 -1535 -2324 C ATOM 1297 CG ASN A 396 27.631 19.640 -13.533 1.00 91.17 C ANISOU 1297 CG ASN A 396 10747 11717 12176 597 -1476 -2453 C ATOM 1298 OD1 ASN A 396 28.208 19.374 -12.475 1.00 65.72 O ANISOU 1298 OD1 ASN A 396 7520 8271 9180 580 -1519 -2380 O ATOM 1299 ND2 ASN A 396 28.064 19.206 -14.708 1.00 66.83 N ANISOU 1299 ND2 ASN A 396 7528 8790 9074 523 -1374 -2643 N ATOM 1300 N LEU A 397 27.363 21.576 -16.848 1.00 64.14 N ANISOU 1300 N LEU A 397 7434 8970 7964 574 -1328 -2450 N ATOM 1301 CA LEU A 397 27.485 21.144 -18.244 1.00 79.07 C ANISOU 1301 CA LEU A 397 9185 11140 9718 503 -1229 -2649 C ATOM 1302 C LEU A 397 27.774 19.640 -18.431 1.00 90.07 C ANISOU 1302 C LEU A 397 10348 12513 11361 425 -1161 -2959 C ATOM 1303 O LEU A 397 27.519 19.080 -19.499 1.00 93.14 O ANISOU 1303 O LEU A 397 10599 13149 11643 376 -1092 -3180 O ATOM 1304 CB LEU A 397 28.564 21.964 -18.954 1.00 72.96 C ANISOU 1304 CB LEU A 397 8462 10441 8817 442 -1147 -2563 C ATOM 1305 CG LEU A 397 28.201 23.311 -19.575 1.00 60.70 C ANISOU 1305 CG LEU A 397 7052 9077 6936 489 -1159 -2334 C ATOM 1306 CD1 LEU A 397 26.950 23.912 -18.960 0.19 70.26 C ANISOU 1306 CD1 LEU A 397 8390 10255 8052 608 -1275 -2154 C ATOM 1307 CD2 LEU A 397 29.391 24.252 -19.440 0.65 57.54 C ANISOU 1307 CD2 LEU A 397 6752 8539 6573 458 -1121 -2153 C ATOM 1308 N ASN A 398 28.317 18.990 -17.407 1.00 83.37 N ANISOU 1308 N ASN A 398 9446 11377 10855 409 -1180 -2975 N ATOM 1309 CA ASN A 398 28.614 17.567 -17.500 1.00 72.34 C ANISOU 1309 CA ASN A 398 7811 9918 9758 339 -1112 -3246 C ATOM 1310 C ASN A 398 27.448 16.681 -17.061 1.00 73.37 C ANISOU 1310 C ASN A 398 7842 10022 10014 397 -1172 -3343 C ATOM 1311 O ASN A 398 27.344 15.532 -17.486 1.00 80.09 O ANISOU 1311 O ASN A 398 8476 10909 11046 346 -1107 -3610 O ATOM 1312 CB ASN A 398 29.870 17.223 -16.698 1.00104.32 C ANISOU 1312 CB ASN A 398 11812 13674 14152 282 -1094 -3208 C ATOM 1313 CG ASN A 398 30.329 15.793 -16.919 1.00 96.21 C ANISOU 1313 CG ASN A 398 10514 12572 13471 199 -1000 -3485 C ATOM 1314 OD1 ASN A 398 30.494 15.351 -18.055 1.00 86.33 O ANISOU 1314 OD1 ASN A 398 9125 11509 12169 129 -883 -3733 O ATOM 1315 ND2 ASN A 398 30.537 15.062 -15.829 1.00 91.50 N ANISOU 1315 ND2 ASN A 398 9828 11704 13234 203 -1048 -3444 N ATOM 1316 N ASP A 399 26.578 17.214 -16.209 1.00 85.73 N ANISOU 1316 N ASP A 399 9558 11517 11500 500 -1287 -3134 N ATOM 1317 CA ASP A 399 25.408 16.471 -15.747 1.00 70.58 C ANISOU 1317 CA ASP A 399 7558 9571 9690 566 -1345 -3192 C ATOM 1318 C ASP A 399 24.181 16.764 -16.624 1.00 86.02 C ANISOU 1318 C ASP A 399 9535 11812 11337 615 -1365 -3246 C ATOM 1319 O ASP A 399 23.512 15.849 -17.105 1.00 93.30 O ANISOU 1319 O ASP A 399 10284 12843 12324 603 -1345 -3468 O ATOM 1320 CB ASP A 399 25.107 16.780 -14.272 1.00 68.55 C ANISOU 1320 CB ASP A 399 7432 9078 9536 649 -1450 -2947 C ATOM 1321 CG ASP A 399 26.177 16.243 -13.320 1.00 85.51 C ANISOU 1321 CG ASP A 399 9513 10954 12023 597 -1449 -2904 C ATOM 1322 OD1 ASP A 399 27.015 15.422 -13.749 1.00 81.88 O ANISOU 1322 OD1 ASP A 399 8867 10455 11787 506 -1364 -3083 O ATOM 1323 OD2 ASP A 399 26.176 16.644 -12.134 1.00 90.15 O ANISOU 1323 OD2 ASP A 399 10226 11373 12655 645 -1532 -2691 O ATOM 1324 N CYS A 400 23.885 18.043 -16.825 1.00 93.88 N ANISOU 1324 N CYS A 400 10729 12924 12016 668 -1408 -3037 N ATOM 1325 CA CYS A 400 22.807 18.438 -17.724 1.00 78.85 C ANISOU 1325 CA CYS A 400 8845 11310 9805 709 -1432 -3049 C ATOM 1326 C CYS A 400 23.048 19.828 -18.303 1.00 80.18 C ANISOU 1326 C CYS A 400 9184 11628 9652 719 -1430 -2842 C ATOM 1327 O CYS A 400 23.588 20.710 -17.637 0.65 72.91 O ANISOU 1327 O CYS A 400 8424 10537 8742 745 -1451 -2620 O ATOM 1328 CB CYS A 400 21.451 18.382 -17.023 1.00100.18 C ANISOU 1328 CB CYS A 400 11583 13956 12524 818 -1529 -2960 C ATOM 1329 SG CYS A 400 20.064 18.217 -18.159 1.00102.46 S ANISOU 1329 SG CYS A 400 11779 14590 12561 845 -1558 -3088 S ATOM 1330 N GLU A 401 22.632 20.009 -19.549 1.00 94.78 N ANISOU 1330 N GLU A 401 10985 13806 11222 695 -1407 -2914 N ATOM 1331 CA GLU A 401 22.982 21.189 -20.323 1.00 80.40 C ANISOU 1331 CA GLU A 401 9275 12170 9103 684 -1382 -2736 C ATOM 1332 C GLU A 401 21.864 22.211 -20.217 1.00 85.28 C ANISOU 1332 C GLU A 401 10030 12859 9514 793 -1476 -2478 C ATOM 1333 O GLU A 401 22.057 23.402 -20.451 1.00 84.30 O ANISOU 1333 O GLU A 401 10033 12783 9213 818 -1478 -2236 O ATOM 1334 CB GLU A 401 23.189 20.785 -21.782 1.00 91.73 C ANISOU 1334 CB GLU A 401 10563 13957 10333 586 -1299 -2954 C ATOM 1335 CG GLU A 401 24.272 21.555 -22.514 1.00131.98 C ANISOU 1335 CG GLU A 401 15712 19174 15261 520 -1211 -2858 C ATOM 1336 CD GLU A 401 24.615 20.933 -23.858 1.00155.34 C ANISOU 1336 CD GLU A 401 18502 22466 18056 405 -1106 -3130 C ATOM 1337 OE1 GLU A 401 23.822 20.102 -24.355 1.00147.98 O ANISOU 1337 OE1 GLU A 401 17427 21728 17070 385 -1119 -3368 O ATOM 1338 OE2 GLU A 401 25.679 21.275 -24.417 1.00161.11 O ANISOU 1338 OE2 GLU A 401 19235 23267 18713 332 -1005 -3116 O ATOM 1339 N TYR A 402 20.681 21.727 -19.871 1.00 89.50 N ANISOU 1339 N TYR A 402 10521 13389 10096 859 -1549 -2527 N ATOM 1340 CA TYR A 402 19.538 22.593 -19.682 1.00 73.37 C ANISOU 1340 CA TYR A 402 8590 11384 7905 968 -1636 -2295 C ATOM 1341 C TYR A 402 19.334 22.687 -18.190 1.00 71.97 C ANISOU 1341 C TYR A 402 8521 10859 7965 1049 -1684 -2177 C ATOM 1342 O TYR A 402 19.839 21.850 -17.444 1.00 92.81 O ANISOU 1342 O TYR A 402 11108 13292 10864 1020 -1665 -2306 O ATOM 1343 CB TYR A 402 18.289 21.994 -20.340 1.00 79.12 C ANISOU 1343 CB TYR A 402 9187 12359 8517 987 -1686 -2431 C ATOM 1344 CG TYR A 402 18.493 21.520 -21.765 1.00107.69 C ANISOU 1344 CG TYR A 402 12651 16339 11927 883 -1635 -2647 C ATOM 1345 CD1 TYR A 402 18.718 20.178 -22.045 1.00144.54 C ANISOU 1345 CD1 TYR A 402 17129 21047 16742 800 -1584 -2999 C ATOM 1346 CD2 TYR A 402 18.454 22.412 -22.829 1.00 99.77 C ANISOU 1346 CD2 TYR A 402 11680 15643 10585 866 -1634 -2499 C ATOM 1347 CE1 TYR A 402 18.899 19.739 -23.342 1.00170.24 C ANISOU 1347 CE1 TYR A 402 20239 24645 19799 697 -1528 -3229 C ATOM 1348 CE2 TYR A 402 18.635 21.983 -24.129 1.00105.06 C ANISOU 1348 CE2 TYR A 402 12209 16678 11032 764 -1585 -2701 C ATOM 1349 CZ TYR A 402 18.856 20.646 -24.380 1.00159.09 C ANISOU 1349 CZ TYR A 402 18872 23561 18012 678 -1530 -3081 C ATOM 1350 OH TYR A 402 19.036 20.215 -25.674 1.00175.99 O ANISOU 1350 OH TYR A 402 20868 26078 19922 568 -1472 -3313 O ATOM 1351 N CYS A 403 18.595 23.699 -17.752 1.00 92.12 N ANISOU 1351 N CYS A 403 11213 13351 10436 1148 -1741 -1929 N ATOM 1352 CA CYS A 403 18.310 23.864 -16.335 1.00 79.07 C ANISOU 1352 CA CYS A 403 9671 11397 8975 1226 -1781 -1820 C ATOM 1353 C CYS A 403 17.051 23.106 -15.941 1.00 78.88 C ANISOU 1353 C CYS A 403 9568 11364 9039 1293 -1834 -1900 C ATOM 1354 O CYS A 403 16.415 22.457 -16.765 1.00 92.92 O ANISOU 1354 O CYS A 403 11204 13359 10743 1278 -1846 -2047 O ATOM 1355 CB CYS A 403 18.134 25.339 -15.991 1.00 69.98 C ANISOU 1355 CB CYS A 403 8702 10161 7727 1299 -1801 -1533 C ATOM 1356 SG CYS A 403 16.517 25.993 -16.449 1.00 75.92 S ANISOU 1356 SG CYS A 403 9464 11083 8299 1406 -1862 -1372 S ATOM 1357 N GLN A 404 16.699 23.208 -14.667 1.00 85.07 N ANISOU 1357 N GLN A 404 10443 11902 9979 1365 -1863 -1803 N ATOM 1358 CA GLN A 404 15.555 22.499 -14.103 1.00 63.43 C ANISOU 1358 CA GLN A 404 7635 9109 7358 1435 -1904 -1855 C ATOM 1359 C GLN A 404 14.254 22.867 -14.793 1.00 83.25 C ANISOU 1359 C GLN A 404 10120 11815 9696 1504 -1949 -1791 C ATOM 1360 O GLN A 404 13.363 22.036 -14.964 1.00 89.40 O ANISOU 1360 O GLN A 404 10767 12672 10530 1526 -1977 -1915 O ATOM 1361 CB GLN A 404 15.452 22.826 -12.615 1.00 84.06 C ANISOU 1361 CB GLN A 404 10380 11445 10113 1502 -1919 -1717 C ATOM 1362 CG GLN A 404 14.060 22.740 -12.033 1.00 85.36 C ANISOU 1362 CG GLN A 404 10547 11565 10321 1609 -1956 -1656 C ATOM 1363 CD GLN A 404 13.989 23.433 -10.694 1.00108.84 C ANISOU 1363 CD GLN A 404 13689 14308 13358 1672 -1957 -1491 C ATOM 1364 OE1 GLN A 404 15.013 23.865 -10.165 1.00 76.46 O ANISOU 1364 OE1 GLN A 404 9690 10080 9283 1629 -1939 -1442 O ATOM 1365 NE2 GLN A 404 12.786 23.552 -10.140 1.00125.07 N ANISOU 1365 NE2 GLN A 404 15769 16314 15438 1771 -1975 -1414 N ATOM 1366 N TYR A 405 14.157 24.126 -15.193 1.00107.62 N ANISOU 1366 N TYR A 405 13322 14975 12593 1537 -1956 -1586 N ATOM 1367 CA TYR A 405 12.914 24.672 -15.707 1.00 88.93 C ANISOU 1367 CA TYR A 405 10947 12761 10080 1613 -2005 -1460 C ATOM 1368 C TYR A 405 12.773 24.527 -17.222 1.00 87.55 C ANISOU 1368 C TYR A 405 10645 12940 9680 1555 -2022 -1533 C ATOM 1369 O TYR A 405 11.909 25.157 -17.821 1.00 89.28 O ANISOU 1369 O TYR A 405 10857 13326 9737 1604 -2068 -1387 O ATOM 1370 CB TYR A 405 12.815 26.147 -15.320 1.00 85.79 C ANISOU 1370 CB TYR A 405 10723 12247 9626 1684 -2002 -1178 C ATOM 1371 CG TYR A 405 12.885 26.409 -13.829 1.00 91.63 C ANISOU 1371 CG TYR A 405 11596 12666 10553 1739 -1985 -1112 C ATOM 1372 CD1 TYR A 405 14.006 26.992 -13.257 1.00 88.96 C ANISOU 1372 CD1 TYR A 405 11382 12154 10264 1702 -1945 -1054 C ATOM 1373 CD2 TYR A 405 11.824 26.081 -12.996 1.00 88.24 C ANISOU 1373 CD2 TYR A 405 11164 12120 10243 1824 -2007 -1109 C ATOM 1374 CE1 TYR A 405 14.066 27.241 -11.893 1.00 96.35 C ANISOU 1374 CE1 TYR A 405 12438 12828 11345 1742 -1934 -1006 C ATOM 1375 CE2 TYR A 405 11.878 26.320 -11.633 1.00 83.22 C ANISOU 1375 CE2 TYR A 405 10648 11222 9749 1868 -1985 -1054 C ATOM 1376 CZ TYR A 405 12.998 26.901 -11.086 1.00 74.48 C ANISOU 1376 CZ TYR A 405 9665 9966 8669 1824 -1952 -1008 C ATOM 1377 OH TYR A 405 13.045 27.143 -9.730 1.00 81.32 O ANISOU 1377 OH TYR A 405 10647 10600 9650 1858 -1936 -966 O ATOM 1378 N HIS A 406 13.624 23.710 -17.836 1.00 83.23 N ANISOU 1378 N HIS A 406 9989 12512 9121 1446 -1982 -1757 N ATOM 1379 CA HIS A 406 13.580 23.481 -19.280 1.00 89.51 C ANISOU 1379 CA HIS A 406 10654 13671 9684 1373 -1986 -1868 C ATOM 1380 C HIS A 406 13.974 22.033 -19.588 1.00107.41 C ANISOU 1380 C HIS A 406 12743 16002 12065 1278 -1950 -2221 C ATOM 1381 O HIS A 406 15.159 21.717 -19.681 1.00111.85 O ANISOU 1381 O HIS A 406 13288 16523 12686 1192 -1877 -2341 O ATOM 1382 CB HIS A 406 14.530 24.434 -20.035 1.00 83.65 C ANISOU 1382 CB HIS A 406 9983 13065 8735 1317 -1941 -1727 C ATOM 1383 CG HIS A 406 14.177 25.893 -19.933 1.00 98.31 C ANISOU 1383 CG HIS A 406 11982 14885 10487 1401 -1968 -1379 C ATOM 1384 ND1 HIS A 406 15.121 26.890 -20.017 1.00127.27 N ANISOU 1384 ND1 HIS A 406 15758 18498 14099 1380 -1917 -1197 N ATOM 1385 CD2 HIS A 406 12.987 26.518 -19.759 1.00107.92 C ANISOU 1385 CD2 HIS A 406 13232 16096 11675 1504 -2033 -1181 C ATOM 1386 CE1 HIS A 406 14.532 28.071 -19.900 1.00 82.42 C ANISOU 1386 CE1 HIS A 406 10170 12776 8371 1467 -1948 -904 C ATOM 1387 NE2 HIS A 406 13.240 27.871 -19.741 1.00 99.02 N ANISOU 1387 NE2 HIS A 406 12229 14906 10488 1543 -2017 -888 N ATOM 1388 N VAL A 407 12.994 21.149 -19.747 1.00129.28 N ANISOU 1388 N VAL A 407 15368 18860 14892 1293 -1996 -2391 N ATOM 1389 CA VAL A 407 13.305 19.735 -19.954 1.00117.72 C ANISOU 1389 CA VAL A 407 13715 17416 13596 1208 -1955 -2738 C ATOM 1390 C VAL A 407 12.389 19.039 -20.968 1.00126.29 C ANISOU 1390 C VAL A 407 14611 18809 14566 1174 -2000 -2954 C ATOM 1391 O VAL A 407 11.256 19.465 -21.208 1.00121.63 O ANISOU 1391 O VAL A 407 14026 18352 13837 1242 -2085 -2827 O ATOM 1392 CB VAL A 407 13.294 18.962 -18.617 1.00116.45 C ANISOU 1392 CB VAL A 407 13539 16900 13805 1251 -1943 -2790 C ATOM 1393 CG1 VAL A 407 14.432 19.442 -17.706 1.00 70.04 C ANISOU 1393 CG1 VAL A 407 7815 10754 8044 1248 -1893 -2646 C ATOM 1394 CG2 VAL A 407 11.942 19.116 -17.926 1.00110.31 C ANISOU 1394 CG2 VAL A 407 12795 16023 13093 1374 -2019 -2647 C TER 1395 VAL A 407 ATOM 1396 O5' DC B 9 39.887 39.221 11.034 1.00114.75 O ANISOU 1396 O5' DC B 9 12264 18265 13069 4129 5588 -4616 O ATOM 1397 C5' DC B 9 39.043 40.374 11.028 1.00130.24 C ANISOU 1397 C5' DC B 9 14676 19416 15396 3917 5994 -4862 C ATOM 1398 C4' DC B 9 37.628 40.002 11.447 1.00113.55 C ANISOU 1398 C4' DC B 9 12734 16956 13456 4430 5985 -4404 C ATOM 1399 O4' DC B 9 37.671 39.043 12.529 1.00155.99 O ANISOU 1399 O4' DC B 9 17726 23194 18351 4735 5715 -4269 O ATOM 1400 C3' DC B 9 36.747 41.154 11.925 1.00169.01 C ANISOU 1400 C3' DC B 9 20119 23402 20696 4281 6428 -4720 C ATOM 1401 O3' DC B 9 35.692 41.327 10.982 1.00206.06 O ANISOU 1401 O3' DC B 9 25200 27162 25932 4591 6546 -4231 O ATOM 1402 C2' DC B 9 36.228 40.708 13.300 1.00157.57 C ANISOU 1402 C2' DC B 9 18451 22539 18880 4518 6339 -4735 C ATOM 1403 C1' DC B 9 36.513 39.206 13.315 1.00170.42 C ANISOU 1403 C1' DC B 9 19711 24809 20231 4951 5858 -4206 C ATOM 1404 N1 DC B 9 36.779 38.566 14.658 1.00178.30 N ANISOU 1404 N1 DC B 9 20301 26814 20630 5092 5678 -4296 N ATOM 1405 C2 DC B 9 35.713 38.110 15.444 1.00154.85 C ANISOU 1405 C2 DC B 9 17371 23856 17608 5487 5659 -4007 C ATOM 1406 O2 DC B 9 34.555 38.249 15.039 1.00130.24 O ANISOU 1406 O2 DC B 9 14597 19960 14929 5702 5786 -3708 O ATOM 1407 N3 DC B 9 35.975 37.527 16.641 1.00176.67 N ANISOU 1407 N3 DC B 9 19773 27546 19808 5635 5510 -4053 N ATOM 1408 C4 DC B 9 37.236 37.385 17.060 1.00180.09 C ANISOU 1408 C4 DC B 9 19773 28940 19714 5436 5368 -4349 C ATOM 1409 N4 DC B 9 37.441 36.805 18.249 1.00189.86 N ANISOU 1409 N4 DC B 9 20632 31149 20358 5645 5228 -4332 N ATOM 1410 C5 DC B 9 38.340 37.832 16.275 1.00153.67 C ANISOU 1410 C5 DC B 9 16337 25656 16394 5023 5373 -4665 C ATOM 1411 C6 DC B 9 38.065 38.406 15.097 1.00162.19 C ANISOU 1411 C6 DC B 9 17822 25740 18063 4853 5534 -4633 C ATOM 1412 P DC B 10 35.504 42.682 10.140 1.00220.96 P ANISOU 1412 P DC B 10 27581 28088 28287 4327 7037 -4420 P ATOM 1413 OP1 DC B 10 36.441 42.660 8.991 1.00199.99 O ANISOU 1413 OP1 DC B 10 24927 25317 25743 4084 6943 -4398 O ATOM 1414 OP2 DC B 10 35.548 43.813 11.093 1.00196.37 O ANISOU 1414 OP2 DC B 10 24638 24909 25066 3928 7519 -5105 O ATOM 1415 O5' DC B 10 34.008 42.508 9.576 1.00226.59 O ANISOU 1415 O5' DC B 10 28537 28144 29411 4912 7054 -3728 O ATOM 1416 C5' DC B 10 33.354 43.450 8.700 1.00206.01 C ANISOU 1416 C5' DC B 10 26364 24640 27270 5008 7441 -3541 C ATOM 1417 C4' DC B 10 32.096 42.825 8.106 1.00177.19 C ANISOU 1417 C4' DC B 10 22714 20765 23847 5599 7253 -2788 C ATOM 1418 O4' DC B 10 31.925 41.535 8.744 1.00122.94 O ANISOU 1418 O4' DC B 10 15472 14573 16667 5815 6815 -2583 O ATOM 1419 C3' DC B 10 30.791 43.572 8.391 1.00187.18 C ANISOU 1419 C3' DC B 10 24248 21526 25346 5945 7638 -2632 C ATOM 1420 O3' DC B 10 29.599 43.104 7.672 1.00202.29 O ANISOU 1420 O3' DC B 10 26127 23278 27455 6472 7496 -1925 O ATOM 1421 C2' DC B 10 30.644 43.174 9.846 1.00171.71 C ANISOU 1421 C2' DC B 10 22070 20130 23043 5934 7539 -2924 C ATOM 1422 C1' DC B 10 30.929 41.674 9.732 1.00145.13 C ANISOU 1422 C1' DC B 10 18310 17411 19424 6060 6958 -2593 C ATOM 1423 N1 DC B 10 31.397 41.095 11.015 1.00172.09 N ANISOU 1423 N1 DC B 10 21433 21566 22388 5944 6768 -2915 N ATOM 1424 C2 DC B 10 31.028 39.789 11.339 1.00169.46 C ANISOU 1424 C2 DC B 10 20833 21716 21839 6265 6399 -2523 C ATOM 1425 O2 DC B 10 30.341 39.147 10.534 1.00149.85 O ANISOU 1425 O2 DC B 10 18360 19033 19544 6563 6249 -1979 O ATOM 1426 N3 DC B 10 31.440 39.271 12.520 1.00173.29 N ANISOU 1426 N3 DC B 10 21058 22896 21888 6224 6253 -2756 N ATOM 1427 C4 DC B 10 32.177 40.015 13.345 1.00181.36 C ANISOU 1427 C4 DC B 10 22030 24212 22666 5841 6431 -3384 C ATOM 1428 N4 DC B 10 32.553 39.458 14.496 1.00188.47 N ANISOU 1428 N4 DC B 10 22623 25906 23083 5839 6265 -3562 N ATOM 1429 C5 DC B 10 32.558 41.356 13.037 1.00164.12 C ANISOU 1429 C5 DC B 10 20115 21548 20693 5428 6829 -3862 C ATOM 1430 C6 DC B 10 32.145 41.854 11.868 1.00168.36 C ANISOU 1430 C6 DC B 10 20963 21310 21694 5517 7003 -3589 C ATOM 1431 P DC B 11 29.435 43.078 6.078 1.00170.67 P ANISOU 1431 P DC B 11 22199 18923 23725 6636 7435 -1390 P ATOM 1432 OP1 DC B 11 29.000 41.732 5.708 1.00151.49 O ANISOU 1432 OP1 DC B 11 19434 16955 21169 6853 6960 -918 O ATOM 1433 OP2 DC B 11 30.650 43.659 5.507 1.00199.82 O ANISOU 1433 OP2 DC B 11 26067 22361 27494 6198 7575 -1723 O ATOM 1434 O5' DC B 11 28.209 44.021 5.676 1.00172.44 O ANISOU 1434 O5' DC B 11 22695 18570 24253 7089 7861 -1017 O ATOM 1435 C5' DC B 11 27.707 43.929 4.335 1.00162.48 C ANISOU 1435 C5' DC B 11 21417 17147 23171 7377 7790 -410 C ATOM 1436 C4' DC B 11 26.759 45.063 4.022 1.00142.57 C ANISOU 1436 C4' DC B 11 19191 14066 20913 7820 8303 -106 C ATOM 1437 O4' DC B 11 26.285 45.015 2.662 1.00135.76 O ANISOU 1437 O4' DC B 11 18268 13144 20171 8126 8236 524 O ATOM 1438 C3' DC B 11 25.481 44.998 4.812 1.00145.11 C ANISOU 1438 C3' DC B 11 19396 14561 21179 8265 8377 80 C ATOM 1439 O3' DC B 11 25.775 45.480 6.111 1.00183.05 O ANISOU 1439 O3' DC B 11 24376 19247 25928 8043 8647 -517 O ATOM 1440 C2' DC B 11 24.570 45.927 3.996 1.00183.25 C ANISOU 1440 C2' DC B 11 24429 18939 26260 8811 8798 615 C ATOM 1441 C1' DC B 11 25.148 45.852 2.573 1.00164.72 C ANISOU 1441 C1' DC B 11 22090 16499 23997 8698 8658 913 C ATOM 1442 N1 DC B 11 24.233 45.365 1.448 1.00199.36 N ANISOU 1442 N1 DC B 11 26157 21256 28334 9121 8415 1654 N ATOM 1443 C2 DC B 11 23.217 44.415 1.657 1.00209.51 C ANISOU 1443 C2 DC B 11 26999 23207 29397 9355 8065 1947 C ATOM 1444 O2 DC B 11 23.041 43.951 2.788 1.00252.00 O ANISOU 1444 O2 DC B 11 32275 28829 34644 9263 7949 1636 O ATOM 1445 N3 DC B 11 22.434 44.020 0.613 1.00155.02 N ANISOU 1445 N3 DC B 11 19779 16722 22401 9651 7881 2553 N ATOM 1446 C4 DC B 11 22.628 44.520 -0.607 1.00153.27 C ANISOU 1446 C4 DC B 11 19653 16293 22291 9764 8003 2912 C ATOM 1447 N4 DC B 11 21.836 44.094 -1.601 1.00114.16 N ANISOU 1447 N4 DC B 11 14318 11882 17174 10027 7805 3492 N ATOM 1448 C5 DC B 11 23.654 45.483 -0.847 1.00186.36 C ANISOU 1448 C5 DC B 11 24329 19747 26733 9573 8359 2665 C ATOM 1449 C6 DC B 11 24.418 45.865 0.189 1.00202.82 C ANISOU 1449 C6 DC B 11 26731 21418 28913 9235 8561 2025 C TER 1450 DC B 11 HETATM 1451 ZN ZN A 500 16.857 27.434 -18.374 1.00 77.21 ZN ANISOU 1451 ZN ZN A 500 9630 11633 8074 1365 -1833 -1133 ZN HETATM 1452 O HOH A 502 23.467 30.818 1.784 1.00 68.05 O HETATM 1453 O HOH A 504 17.082 28.636 4.911 1.00 73.47 O HETATM 1454 O HOH A 505 31.066 14.702 -20.863 1.00 96.25 O HETATM 1455 O HOH A 507 39.833 12.877 12.704 1.00 57.31 O HETATM 1456 O HOH A 508 38.461 37.642 -3.178 1.00 51.07 O HETATM 1457 O HOH A 510 -4.201 21.532 -35.527 1.00 80.18 O HETATM 1458 O HOH A 511 35.135 12.166 11.120 1.00 69.53 O HETATM 1459 O HOH A 512 27.648 23.331 15.972 1.00 63.27 O HETATM 1460 O HOH A 513 32.590 33.286 12.321 1.00 77.54 O HETATM 1461 O HOH A 514 38.236 28.313 10.942 1.00 61.30 O HETATM 1462 O HOH A 515 33.820 21.339 -13.300 1.00 62.53 O HETATM 1463 O HOH A 516 20.142 26.000 -11.663 1.00 64.66 O HETATM 1464 O HOH B 517 27.262 40.789 7.891 1.00 59.53 O HETATM 1465 O HOH B 518 19.831 43.219 -0.458 1.00 73.29 O HETATM 1466 O HOH B 519 41.317 37.664 14.599 1.00 81.88 O CONECT 1187 1451 CONECT 1260 1451 CONECT 1356 1451 CONECT 1384 1451 CONECT 1451 1187 1260 1356 1384 MASTER 459 0 1 5 15 0 1 6 1450 2 5 17 END
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PDB Code
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Ligand Name
1si2
RCSB PDB
PDBbind
9-mer
1si3
RCSB PDB
PDBbind
9-mer
3gib
RCSB PDB
PDBbind
9-mer
3k5q
RCSB PDB
PDBbind
9-mer
3k5y
RCSB PDB
PDBbind
9-mer
3k5z
RCSB PDB
PDBbind
9-mer
3k61
RCSB PDB
PDBbind
9-mer
3k62
RCSB PDB
PDBbind
9-mer
3k64
RCSB PDB
PDBbind
9-mer
5yki
RCSB PDB
PDBbind
9-mer
5zvb
RCSB PDB
PDBbind
9-mer
Entry Information
PDB ID
3h15
Complex Type
Protein-Nucleic Acid
PDBbind Subset
general set
Protein Name
Protein MCM10 homolog internal domain
Ligand Name
9-mer
EC.Number
E.C.-.-.-.-
Resolution
2.72(Å)
Affinity (Kd/Ki/IC50)
Kd=3.4uM
Release Year
2009
Protein/NA Sequence
Check fasta file
Primary Reference
(2009) J.Biol.Chem. Vol. 284: pp. 24662-24672
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):
Q5EAW4
Entrez Gene ID
NCBI Entrez Gene ID:
398196
ASD
Information of known allosteric effects of PDB entries
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