Browse entries in the PDBbind-CN Database
HEADER RNA/RNA BINDING PROTEIN 08-OCT-09 3K62 TITLE CRYSTAL STRUCTURE OF FBF-2/GLD-1 FBEB COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: FEM-3 MRNA-BINDING FACTOR 2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: UNP RESIDUES 164-575, RNA-BINDING DOMAIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: 5'-R(*UP*GP*UP*GP*UP*UP*AP*UP*C)-3'; COMPND 8 CHAIN: B; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CAENORHABDITIS ELEGANS; SOURCE 3 ORGANISM_COMMON: NEMATODE; SOURCE 4 ORGANISM_TAXID: 6239; SOURCE 5 GENE: F21H12.5, FBF-2; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 STAR (DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P1; SOURCE 11 MOL_ID: 2; SOURCE 12 SYNTHETIC: YES KEYWDS FBF, FEM-3 BINDING FACTOR, PUF, RNA-BINDING SPECIFICITY, KEYWDS 2 BASE FLIPPING, BASE STACKING EXPDTA X-RAY DIFFRACTION AUTHOR Y.WANG,L.OPPERMAN,M.WICKENS,T.M.T.HALL REVDAT 2 22-DEC-09 3K62 1 JRNL REVDAT 1 03-NOV-09 3K62 0 JRNL AUTH Y.WANG,L.OPPERMAN,M.WICKENS,T.M.HALL JRNL TITL STRUCTURAL BASIS FOR SPECIFIC RECOGNITION OF JRNL TITL 2 MULTIPLE MRNA TARGETS BY A PUF REGULATORY PROTEIN. JRNL REF PROC.NATL.ACAD.SCI.USA V. 106 20186 2009 JRNL REFN ISSN 0027-8424 JRNL PMID 19901328 JRNL DOI 10.1073/PNAS.0812076106 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX.REFINE REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.89 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 3 NUMBER OF REFLECTIONS : 42208 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.158 REMARK 3 FREE R VALUE : 0.197 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 2120 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : NULL REMARK 3 SHRINKAGE RADIUS : NULL REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 24.69 REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.006 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 : 11 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN A AND RESID 168:193 REMARK 3 ORIGIN FOR THE GROUP (A): 21.9558 2.5143 29.5966 REMARK 3 T TENSOR REMARK 3 T11: 0.4619 T22: 0.2572 REMARK 3 T33: 0.2636 T12: -0.0555 REMARK 3 T13: 0.1181 T23: 0.2432 REMARK 3 L TENSOR REMARK 3 L11: -0.2182 L22: 1.0303 REMARK 3 L33: 3.8041 L12: 0.9676 REMARK 3 L13: 0.0203 L23: 1.3748 REMARK 3 S TENSOR REMARK 3 S11: 0.2303 S12: -0.7429 S13: -0.6149 REMARK 3 S21: 1.1649 S22: 0.2310 S23: 0.0813 REMARK 3 S31: 0.8015 S32: 0.3522 S33: 1.0945 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN A AND RESID 194:229 REMARK 3 ORIGIN FOR THE GROUP (A): 28.5819 7.7967 20.1323 REMARK 3 T TENSOR REMARK 3 T11: 0.2037 T22: 0.1835 REMARK 3 T33: 0.2507 T12: 0.0322 REMARK 3 T13: -0.0177 T23: 0.0274 REMARK 3 L TENSOR REMARK 3 L11: 0.3239 L22: 0.5864 REMARK 3 L33: 0.7544 L12: 0.2240 REMARK 3 L13: 0.0242 L23: -0.5063 REMARK 3 S TENSOR REMARK 3 S11: 0.1760 S12: -0.1885 S13: -0.1123 REMARK 3 S21: 0.2070 S22: 0.1408 S23: 0.1029 REMARK 3 S31: 0.0354 S32: -0.0719 S33: 0.0002 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN A AND RESID 230:276 REMARK 3 ORIGIN FOR THE GROUP (A): 30.5450 8.8713 8.1718 REMARK 3 T TENSOR REMARK 3 T11: 0.1884 T22: 0.1699 REMARK 3 T33: 0.2128 T12: 0.0159 REMARK 3 T13: -0.0335 T23: -0.0227 REMARK 3 L TENSOR REMARK 3 L11: 0.2632 L22: 0.8501 REMARK 3 L33: 1.9578 L12: -0.1115 REMARK 3 L13: 1.2748 L23: -0.7348 REMARK 3 S TENSOR REMARK 3 S11: 0.1007 S12: 0.0427 S13: -0.2946 REMARK 3 S21: -0.1126 S22: 0.0505 S23: 0.0521 REMARK 3 S31: 0.0820 S32: 0.1845 S33: -0.0000 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN A AND RESID 277:313 REMARK 3 ORIGIN FOR THE GROUP (A): 26.7466 15.7336 -1.0278 REMARK 3 T TENSOR REMARK 3 T11: 0.1708 T22: 0.1860 REMARK 3 T33: 0.1827 T12: 0.0436 REMARK 3 T13: -0.0373 T23: -0.0210 REMARK 3 L TENSOR REMARK 3 L11: 0.3801 L22: 0.5784 REMARK 3 L33: 0.4129 L12: -0.6144 REMARK 3 L13: 0.2567 L23: -1.1545 REMARK 3 S TENSOR REMARK 3 S11: 0.1445 S12: -0.1141 S13: -0.1960 REMARK 3 S21: -0.0898 S22: 0.0116 S23: 0.1102 REMARK 3 S31: 0.1671 S32: 0.1257 S33: 0.0000 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN A AND RESID 314:349 REMARK 3 ORIGIN FOR THE GROUP (A): 23.9427 22.4756 -8.2138 REMARK 3 T TENSOR REMARK 3 T11: 0.1219 T22: 0.1796 REMARK 3 T33: 0.1589 T12: 0.0277 REMARK 3 T13: -0.0287 T23: 0.0089 REMARK 3 L TENSOR REMARK 3 L11: 0.9535 L22: 0.7077 REMARK 3 L33: 0.5481 L12: -0.7223 REMARK 3 L13: 0.8403 L23: -0.6245 REMARK 3 S TENSOR REMARK 3 S11: 0.2387 S12: 0.0803 S13: -0.2671 REMARK 3 S21: -0.0992 S22: 0.0089 S23: 0.1729 REMARK 3 S31: 0.0859 S32: 0.1161 S33: 0.0029 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN A AND RESID 350:404 REMARK 3 ORIGIN FOR THE GROUP (A): 25.0126 32.0339 -13.0817 REMARK 3 T TENSOR REMARK 3 T11: 0.1235 T22: 0.2402 REMARK 3 T33: 0.1304 T12: 0.0384 REMARK 3 T13: 0.0025 T23: 0.0298 REMARK 3 L TENSOR REMARK 3 L11: 1.3250 L22: 1.5273 REMARK 3 L33: -0.1248 L12: -0.7686 REMARK 3 L13: 0.3290 L23: -0.9444 REMARK 3 S TENSOR REMARK 3 S11: 0.1835 S12: 0.3086 S13: 0.1101 REMARK 3 S21: -0.0947 S22: -0.0346 S23: 0.1957 REMARK 3 S31: -0.0208 S32: 0.0447 S33: 0.0059 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN A AND RESID 405:441 REMARK 3 ORIGIN FOR THE GROUP (A): 16.5454 41.2171 -16.4495 REMARK 3 T TENSOR REMARK 3 T11: 0.1614 T22: 0.2264 REMARK 3 T33: 0.2060 T12: 0.0506 REMARK 3 T13: 0.0292 T23: 0.0619 REMARK 3 L TENSOR REMARK 3 L11: 0.5984 L22: 1.4039 REMARK 3 L33: -0.5590 L12: -1.4044 REMARK 3 L13: -0.3767 L23: -0.5725 REMARK 3 S TENSOR REMARK 3 S11: 0.2061 S12: 0.0862 S13: -0.1394 REMARK 3 S21: -0.2732 S22: -0.1279 S23: -0.0206 REMARK 3 S31: -0.0243 S32: 0.0906 S33: 0.0011 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN A AND RESID 442:487 REMARK 3 ORIGIN FOR THE GROUP (A): 7.5494 52.1106 -19.8223 REMARK 3 T TENSOR REMARK 3 T11: 0.2260 T22: 0.1831 REMARK 3 T33: 0.1591 T12: 0.0376 REMARK 3 T13: 0.0333 T23: 0.0472 REMARK 3 L TENSOR REMARK 3 L11: 0.8818 L22: 1.8106 REMARK 3 L33: 0.1327 L12: -0.7753 REMARK 3 L13: -0.5430 L23: -0.4012 REMARK 3 S TENSOR REMARK 3 S11: 0.0717 S12: 0.0835 S13: 0.0355 REMARK 3 S21: -0.4559 S22: -0.0866 S23: 0.0031 REMARK 3 S31: 0.1595 S32: 0.0537 S33: -0.0000 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN A AND RESID 488:545 REMARK 3 ORIGIN FOR THE GROUP (A): 9.9142 61.2483 -13.8073 REMARK 3 T TENSOR REMARK 3 T11: 0.1525 T22: 0.1726 REMARK 3 T33: 0.1099 T12: 0.0012 REMARK 3 T13: 0.0098 T23: 0.0245 REMARK 3 L TENSOR REMARK 3 L11: 1.1450 L22: 2.0867 REMARK 3 L33: 1.2419 L12: -0.6035 REMARK 3 L13: -0.1278 L23: -0.7875 REMARK 3 S TENSOR REMARK 3 S11: -0.0283 S12: -0.1208 S13: 0.1930 REMARK 3 S21: -0.0347 S22: -0.0837 S23: -0.0716 REMARK 3 S31: -0.0767 S32: 0.2049 S33: -0.0000 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN A AND RESID 546:567 REMARK 3 ORIGIN FOR THE GROUP (A): -0.0190 64.0343 -5.4857 REMARK 3 T TENSOR REMARK 3 T11: 0.2756 T22: 0.2961 REMARK 3 T33: 0.1430 T12: -0.0033 REMARK 3 T13: -0.0153 T23: -0.0039 REMARK 3 L TENSOR REMARK 3 L11: 0.2583 L22: 0.2567 REMARK 3 L33: 0.3733 L12: 0.2044 REMARK 3 L13: -0.4178 L23: -0.2597 REMARK 3 S TENSOR REMARK 3 S11: 0.0026 S12: -0.5304 S13: 0.1707 REMARK 3 S21: 0.1839 S22: -0.0436 S23: 0.1851 REMARK 3 S31: -0.4534 S32: 0.0600 S33: -0.0000 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN B REMARK 3 ORIGIN FOR THE GROUP (A): 10.1234 33.3198 2.3739 REMARK 3 T TENSOR REMARK 3 T11: 0.3734 T22: 0.3268 REMARK 3 T33: 0.2823 T12: 0.1552 REMARK 3 T13: 0.0720 T23: 0.1422 REMARK 3 L TENSOR REMARK 3 L11: -0.3139 L22: -0.3049 REMARK 3 L33: -0.8152 L12: -0.6281 REMARK 3 L13: 0.4489 L23: -0.4539 REMARK 3 S TENSOR REMARK 3 S11: -0.2126 S12: -0.1630 S13: -0.0941 REMARK 3 S21: 0.2766 S22: 0.1282 S23: 0.1066 REMARK 3 S31: -0.0641 S32: 0.0817 S33: -0.0035 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 3K62 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-OCT-09. REMARK 100 THE RCSB ID CODE IS RCSB055591. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-OCT-07 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 22-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42208 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 27.892 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 200 DATA REDUNDANCY : 11.200 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.08300 REMARK 200
FOR THE DATA SET : 28.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93 REMARK 200 COMPLETENESS FOR SHELL (%) : 93.5 REMARK 200 DATA REDUNDANCY IN SHELL : 8.10 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.80700 REMARK 200
FOR SHELL : 2.900 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 3K5Q REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 55.32 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS PH 7.5, 10% REMARK 280 POLYETHYLENE GLYCOL 8000, AND 8% ETHYLENE GLYCOL, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 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 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+5/6 REMARK 290 6555 X-Y,X,Z+1/6 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 33.89267 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 67.78533 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 50.83900 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 84.73167 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 16.94633 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: 2490 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19730 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 164 REMARK 465 ASN A 165 REMARK 465 ASN A 166 REMARK 465 VAL A 167 REMARK 465 THR A 568 REMARK 465 HIS A 569 REMARK 465 PRO A 570 REMARK 465 ILE A 571 REMARK 465 TYR A 572 REMARK 465 GLU A 573 REMARK 465 LEU A 574 REMARK 465 GLN A 575 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 G B 2 P G B 2 OP1 0.284 REMARK 500 G B 2 P G B 2 OP2 -0.105 REMARK 500 U B 1 O3' G B 2 P -0.112 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 G B 2 O3' - P - OP2 ANGL. DEV. = 6.9 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 ARG A 182 11.96 80.26 REMARK 500 ASN A 258 49.04 -88.17 REMARK 500 ASP A 312 -154.30 -113.39 REMARK 500 ARG A 441 -5.31 74.70 REMARK 500 GLU A 522 146.08 -178.21 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 636 DISTANCE = 5.08 ANGSTROMS REMARK 525 HOH A 753 DISTANCE = 7.05 ANGSTROMS REMARK 525 HOH A 767 DISTANCE = 5.05 ANGSTROMS REMARK 525 HOH A 798 DISTANCE = 6.20 ANGSTROMS REMARK 525 HOH A 810 DISTANCE = 6.69 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3K5Q RELATED DB: PDB REMARK 900 RELATED ID: 3K5Y RELATED DB: PDB REMARK 900 RELATED ID: 3K5Z RELATED DB: PDB REMARK 900 RELATED ID: 3K61 RELATED DB: PDB REMARK 900 RELATED ID: 3K64 RELATED DB: PDB DBREF 3K62 A 164 575 UNP Q09312 FBF2_CAEEL 164 575 DBREF 3K62 B 1 9 PDB 3K62 3K62 1 9 SEQRES 1 A 412 SER ASN ASN VAL LEU PRO THR TRP SER LEU ASP SER ASN SEQRES 2 A 412 GLY GLU MET ARG SER ARG LEU SER LEU SER GLU VAL LEU SEQRES 3 A 412 ASP SER GLY ASP LEU MET LYS PHE ALA VAL ASP LYS THR SEQRES 4 A 412 GLY CYS GLN PHE LEU GLU LYS ALA VAL LYS GLY SER LEU SEQRES 5 A 412 THR SER TYR GLN LYS PHE GLN LEU PHE GLU GLN VAL ILE SEQRES 6 A 412 GLY ARG LYS ASP ASP PHE LEU LYS LEU SER THR ASN ILE SEQRES 7 A 412 PHE GLY ASN TYR LEU VAL GLN SER VAL ILE GLY ILE SER SEQRES 8 A 412 LEU ALA THR ASN ASP ASP GLY TYR THR LYS ARG GLN GLU SEQRES 9 A 412 LYS LEU LYS ASN PHE ILE SER SER GLN MET THR ASP MET SEQRES 10 A 412 CYS LEU ASP LYS PHE ALA CYS ARG VAL ILE GLN SER SER SEQRES 11 A 412 LEU GLN ASN MET ASP LEU SER LEU ALA CYS LYS LEU VAL SEQRES 12 A 412 GLN ALA LEU PRO ARG ASP ALA ARG LEU ILE ALA ILE CYS SEQRES 13 A 412 VAL ASP GLN ASN ALA ASN HIS VAL ILE GLN LYS VAL VAL SEQRES 14 A 412 ALA VAL ILE PRO LEU LYS ASN TRP GLU PHE ILE VAL ASP SEQRES 15 A 412 PHE VAL ALA THR PRO GLU HIS LEU ARG GLN ILE CYS SER SEQRES 16 A 412 ASP LYS TYR GLY CYS ARG VAL VAL GLN THR ILE ILE GLU SEQRES 17 A 412 LYS LEU THR ALA ASP SER MET ASN VAL ASP LEU THR SER SEQRES 18 A 412 ALA ALA GLN ASN LEU ARG GLU ARG ALA LEU GLN ARG LEU SEQRES 19 A 412 MET THR SER VAL THR ASN ARG CYS GLN GLU LEU ALA THR SEQRES 20 A 412 ASN GLU TYR ALA ASN TYR ILE ILE GLN HIS ILE VAL SER SEQRES 21 A 412 ASN ASP ASP LEU ALA VAL TYR ARG GLU CYS ILE ILE GLU SEQRES 22 A 412 LYS CYS LEU MET ARG ASN LEU LEU SER LEU SER GLN GLU SEQRES 23 A 412 LYS PHE ALA SER HIS VAL VAL GLU LYS ALA PHE LEU HIS SEQRES 24 A 412 ALA PRO LEU GLU LEU LEU ALA GLU MET MET ASP GLU ILE SEQRES 25 A 412 PHE ASP GLY TYR ILE PRO HIS PRO ASP THR GLY LYS ASP SEQRES 26 A 412 ALA LEU ASP ILE MET MET PHE HIS GLN PHE GLY ASN TYR SEQRES 27 A 412 VAL VAL GLN CYS MET LEU THR ILE CYS CYS ASP ALA VAL SEQRES 28 A 412 SER GLY ARG ARG GLN THR LYS GLU GLY GLY TYR ASP HIS SEQRES 29 A 412 ALA ILE SER PHE GLN ASP TRP LEU LYS LYS LEU HIS SER SEQRES 30 A 412 ARG VAL THR LYS GLU ARG HIS ARG LEU SER ARG PHE SER SEQRES 31 A 412 SER GLY LYS LYS MET ILE GLU THR LEU ALA ASN LEU ARG SEQRES 32 A 412 SER THR HIS PRO ILE TYR GLU LEU GLN SEQRES 1 B 9 U G U G U U A U C FORMUL 3 HOH *417(H2 O) HELIX 1 1 PRO A 169 LEU A 173 5 5 HELIX 2 2 SER A 184 GLY A 192 1 9 HELIX 3 3 ASP A 193 VAL A 199 1 7 HELIX 4 4 ASP A 200 VAL A 211 1 12 HELIX 5 5 THR A 216 ILE A 228 1 13 HELIX 6 6 ARG A 230 THR A 239 1 10 HELIX 7 7 PHE A 242 THR A 257 1 16 HELIX 8 8 GLY A 261 GLN A 276 1 16 HELIX 9 9 GLN A 276 ASP A 283 1 8 HELIX 10 10 PHE A 285 MET A 297 1 13 HELIX 11 11 ASP A 298 ALA A 308 1 11 HELIX 12 12 ASP A 312 ASP A 321 1 10 HELIX 13 13 ALA A 324 ILE A 335 1 12 HELIX 14 14 PRO A 336 THR A 349 1 14 HELIX 15 15 THR A 349 SER A 358 1 10 HELIX 16 16 ASP A 359 LEU A 373 1 15 HELIX 17 17 ASP A 376 VAL A 380 5 5 HELIX 18 18 THR A 383 ARG A 404 1 22 HELIX 19 19 ARG A 404 ASN A 411 1 8 HELIX 20 20 ALA A 414 ASN A 424 1 11 HELIX 21 21 LEU A 427 LEU A 439 1 13 HELIX 22 22 ASN A 442 GLN A 448 1 7 HELIX 23 23 PHE A 451 ALA A 463 1 13 HELIX 24 24 PRO A 464 GLY A 478 1 15 HELIX 25 25 ASP A 488 HIS A 496 1 9 HELIX 26 26 PHE A 498 SER A 515 1 18 HELIX 27 27 HIS A 527 GLU A 545 1 19 HELIX 28 28 GLU A 545 SER A 550 1 6 HELIX 29 29 PHE A 552 SER A 567 1 16 SHEET 1 A 2 LYS A 521 GLU A 522 0 SHEET 2 A 2 TYR A 525 ASP A 526 -1 O TYR A 525 N GLU A 522 SSBOND 1 CYS A 405 CYS A 438 1555 1555 2.04 CRYST1 96.620 96.620 101.678 90.00 90.00 120.00 P 61 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 0.010350 0.005975 0.000000 0.00000 SCALE2 0.000000 0.011951 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009835 0.00000 ATOM 1 N LEU A 168 15.025 1.618 23.746 1.00 49.24 N ANISOU 1 N LEU A 168 6387 5185 7135 -714 1727 1801 N ATOM 2 CA LEU A 168 16.295 1.484 24.457 1.00 49.83 C ANISOU 2 CA LEU A 168 6609 5263 7059 -705 1616 1881 C ATOM 3 C LEU A 168 16.419 0.116 25.126 1.00 49.60 C ANISOU 3 C LEU A 168 6824 5089 6934 -781 1574 2142 C ATOM 4 O LEU A 168 15.450 -0.395 25.687 1.00 50.83 O ANISOU 4 O LEU A 168 7113 5188 7014 -898 1704 2282 O ATOM 5 CB LEU A 168 16.455 2.582 25.511 1.00 46.30 C ANISOU 5 CB LEU A 168 6255 4939 6396 -722 1705 1857 C ATOM 6 CG LEU A 168 16.619 4.028 25.034 1.00 46.85 C ANISOU 6 CG LEU A 168 6184 5128 6491 -647 1714 1601 C ATOM 7 CD1 LEU A 168 16.800 4.964 26.223 1.00 51.87 C ANISOU 7 CD1 LEU A 168 6954 5874 6880 -685 1806 1607 C ATOM 8 CD2 LEU A 168 17.788 4.156 24.072 1.00 41.19 C ANISOU 8 CD2 LEU A 168 5353 4426 5870 -567 1531 1443 C ATOM 9 N PRO A 169 17.621 -0.477 25.068 1.00 46.92 N ANISOU 9 N PRO A 169 6577 4671 6580 -713 1381 2205 N ATOM 10 CA PRO A 169 17.907 -1.772 25.693 1.00 53.68 C ANISOU 10 CA PRO A 169 7743 5334 7317 -733 1282 2455 C ATOM 11 C PRO A 169 17.588 -1.729 27.177 1.00 52.87 C ANISOU 11 C PRO A 169 7936 5228 6924 -818 1383 2638 C ATOM 12 O PRO A 169 17.827 -0.718 27.839 1.00 52.11 O ANISOU 12 O PRO A 169 7830 5283 6685 -809 1444 2586 O ATOM 13 CB PRO A 169 19.422 -1.929 25.487 1.00 56.76 C ANISOU 13 CB PRO A 169 8171 5686 7710 -582 1036 2443 C ATOM 14 CG PRO A 169 19.908 -0.551 25.213 1.00 48.52 C ANISOU 14 CG PRO A 169 6893 4857 6687 -551 1064 2221 C ATOM 15 CD PRO A 169 18.814 0.055 24.397 1.00 46.00 C ANISOU 15 CD PRO A 169 6306 4627 6544 -605 1228 2037 C ATOM 16 N THR A 170 17.038 -2.819 27.690 1.00 50.45 N ANISOU 16 N THR A 170 7908 4749 6513 -915 1405 2841 N ATOM 17 CA THR A 170 16.605 -2.854 29.074 1.00 61.11 C ANISOU 17 CA THR A 170 9558 6084 7577 -1032 1516 3010 C ATOM 18 C THR A 170 17.743 -2.559 30.056 1.00 63.34 C ANISOU 18 C THR A 170 10060 6389 7616 -916 1372 3101 C ATOM 19 O THR A 170 17.532 -1.881 31.061 1.00 55.54 O ANISOU 19 O THR A 170 9160 5518 6424 -986 1495 3128 O ATOM 20 CB THR A 170 15.948 -4.199 29.410 1.00 60.62 C ANISOU 20 CB THR A 170 9822 5799 7413 -1170 1534 3214 C ATOM 21 OG1 THR A 170 15.681 -4.255 30.816 1.00 69.77 O ANISOU 21 OG1 THR A 170 11319 6930 8259 -1290 1615 3380 O ATOM 22 CG2 THR A 170 16.863 -5.343 29.014 1.00 63.17 C ANISOU 22 CG2 THR A 170 10350 5889 7763 -1027 1266 3319 C ATOM 23 N TRP A 171 18.945 -3.052 29.757 1.00 63.21 N ANISOU 23 N TRP A 171 10129 6274 7616 -724 1103 3139 N ATOM 24 CA TRP A 171 20.096 -2.837 30.634 1.00 57.01 C ANISOU 24 CA TRP A 171 9557 5523 6580 -565 917 3229 C ATOM 25 C TRP A 171 20.348 -1.361 30.926 1.00 52.58 C ANISOU 25 C TRP A 171 8784 5249 5944 -582 1035 3074 C ATOM 26 O TRP A 171 20.953 -1.019 31.938 1.00 55.12 O ANISOU 26 O TRP A 171 9297 5660 5986 -525 970 3155 O ATOM 27 CB TRP A 171 21.368 -3.493 30.072 1.00 52.96 C ANISOU 27 CB TRP A 171 9098 4893 6132 -299 578 3241 C ATOM 28 CG TRP A 171 21.939 -2.851 28.819 1.00 46.35 C ANISOU 28 CG TRP A 171 7860 4185 5564 -223 532 2999 C ATOM 29 CD1 TRP A 171 21.824 -3.317 27.538 1.00 41.28 C ANISOU 29 CD1 TRP A 171 7006 3450 5230 -219 499 2883 C ATOM 30 CD2 TRP A 171 22.729 -1.653 28.738 1.00 48.69 C ANISOU 30 CD2 TRP A 171 7917 4758 5825 -158 507 2784 C ATOM 31 NE1 TRP A 171 22.480 -2.476 26.667 1.00 40.65 N ANISOU 31 NE1 TRP A 171 6604 3528 5314 -169 461 2656 N ATOM 32 CE2 TRP A 171 23.043 -1.450 27.378 1.00 45.42 C ANISOU 32 CE2 TRP A 171 7180 4371 5705 -133 465 2570 C ATOM 33 CE3 TRP A 171 23.195 -0.732 29.680 1.00 53.23 C ANISOU 33 CE3 TRP A 171 8504 5583 6138 -135 520 2705 C ATOM 34 CZ2 TRP A 171 23.798 -0.363 26.939 1.00 44.12 C ANISOU 34 CZ2 TRP A 171 6726 4473 5566 -100 437 2273 C ATOM 35 CZ3 TRP A 171 23.942 0.347 29.240 1.00 52.24 C ANISOU 35 CZ3 TRP A 171 8086 5727 6037 -97 497 2416 C ATOM 36 CH2 TRP A 171 24.235 0.522 27.883 1.00 45.70 C ANISOU 36 CH2 TRP A 171 6956 4916 5489 -86 456 2199 C ATOM 37 N SER A 172 19.877 -0.488 30.041 1.00 56.90 N ANISOU 37 N SER A 172 8958 5941 6718 -653 1196 2843 N ATOM 38 CA SER A 172 20.160 0.938 30.156 1.00 53.71 C ANISOU 38 CA SER A 172 8363 5790 6253 -659 1292 2657 C ATOM 39 C SER A 172 19.020 1.714 30.811 1.00 54.82 C ANISOU 39 C SER A 172 8476 6035 6319 -805 1559 2611 C ATOM 40 O SER A 172 19.069 2.944 30.891 1.00 47.98 O ANISOU 40 O SER A 172 7464 5352 5412 -811 1655 2437 O ATOM 41 CB SER A 172 20.426 1.534 28.777 1.00 49.84 C ANISOU 41 CB SER A 172 7521 5381 6034 -618 1270 2400 C ATOM 42 OG SER A 172 19.201 1.847 28.135 1.00 46.47 O ANISOU 42 OG SER A 172 6884 4960 5812 -701 1448 2268 O ATOM 43 N LEU A 173 17.995 0.998 31.263 1.00 58.29 N ANISOU 43 N LEU A 173 9069 6348 6729 -925 1671 2758 N ATOM 44 CA LEU A 173 16.809 1.623 31.848 1.00 63.60 C ANISOU 44 CA LEU A 173 9717 7107 7343 -1067 1924 2721 C ATOM 45 C LEU A 173 16.743 1.425 33.358 1.00 65.38 C ANISOU 45 C LEU A 173 10281 7317 7244 -1167 1980 2912 C ATOM 46 O LEU A 173 17.204 0.407 33.885 1.00 63.43 O ANISOU 46 O LEU A 173 10345 6914 6841 -1160 1837 3123 O ATOM 47 CB LEU A 173 15.540 1.051 31.214 1.00 61.13 C ANISOU 47 CB LEU A 173 9302 6704 7221 -1170 2047 2718 C ATOM 48 CG LEU A 173 15.370 1.278 29.714 1.00 60.30 C ANISOU 48 CG LEU A 173 8861 6617 7433 -1082 2012 2521 C ATOM 49 CD1 LEU A 173 14.086 0.632 29.224 1.00 63.99 C ANISOU 49 CD1 LEU A 173 9266 7011 8038 -1193 2132 2546 C ATOM 50 CD2 LEU A 173 15.389 2.765 29.393 1.00 52.65 C ANISOU 50 CD2 LEU A 173 7661 5821 6521 -1004 2073 2282 C ATOM 51 N ASP A 174 16.160 2.400 34.049 1.00 64.00 N ANISOU 51 N ASP A 174 10071 7287 6961 -1251 2174 2835 N ATOM 52 CA ASP A 174 15.942 2.284 35.489 1.00 76.44 C ANISOU 52 CA ASP A 174 11954 8857 8234 -1381 2261 2994 C ATOM 53 C ASP A 174 14.601 1.616 35.787 1.00 85.71 C ANISOU 53 C ASP A 174 13234 9933 9397 -1589 2445 3092 C ATOM 54 O ASP A 174 13.939 1.110 34.879 1.00 79.93 O ANISOU 54 O ASP A 174 12359 9132 8881 -1618 2476 3060 O ATOM 55 CB ASP A 174 16.033 3.653 36.173 1.00 76.72 C ANISOU 55 CB ASP A 174 11924 9094 8133 -1382 2380 2862 C ATOM 56 CG ASP A 174 15.023 4.653 35.630 1.00 83.94 C ANISOU 56 CG ASP A 174 12548 10113 9232 -1401 2576 2649 C ATOM 57 OD1 ASP A 174 15.199 5.866 35.879 1.00 89.11 O ANISOU 57 OD1 ASP A 174 13120 10910 9829 -1357 2637 2498 O ATOM 58 OD2 ASP A 174 14.057 4.236 34.955 1.00 84.96 O ANISOU 58 OD2 ASP A 174 12551 10178 9552 -1452 2659 2633 O ATOM 59 N SER A 175 14.204 1.624 37.057 1.00100.40 N ANISOU 59 N SER A 175 15350 11803 10994 -1750 2570 3202 N ATOM 60 CA SER A 175 12.953 0.999 37.482 1.00114.71 C ANISOU 60 CA SER A 175 17301 13543 12738 -1996 2761 3292 C ATOM 61 C SER A 175 11.737 1.830 37.086 1.00120.20 C ANISOU 61 C SER A 175 17677 14397 13596 -2064 3006 3106 C ATOM 62 O SER A 175 10.597 1.433 37.327 1.00122.37 O ANISOU 62 O SER A 175 17999 14663 13832 -2276 3192 3141 O ATOM 63 CB SER A 175 12.953 0.772 38.995 1.00120.28 C ANISOU 63 CB SER A 175 18404 14209 13089 -2166 2815 3458 C ATOM 64 OG SER A 175 13.973 -0.132 39.379 1.00122.74 O ANISOU 64 OG SER A 175 19069 14340 13227 -2095 2566 3655 O ATOM 65 N ASN A 176 11.989 2.986 36.483 1.00121.83 N ANISOU 65 N ASN A 176 17580 14744 13964 -1885 2999 2904 N ATOM 66 CA ASN A 176 10.924 3.885 36.058 1.00123.38 C ANISOU 66 CA ASN A 176 17494 15073 14311 -1891 3191 2722 C ATOM 67 C ASN A 176 10.604 3.718 34.577 1.00116.00 C ANISOU 67 C ASN A 176 16277 14107 13690 -1785 3132 2613 C ATOM 68 O ASN A 176 9.728 4.397 34.043 1.00112.13 O ANISOU 68 O ASN A 176 15552 13708 13346 -1759 3255 2466 O ATOM 69 CB ASN A 176 11.313 5.338 36.340 1.00129.14 C ANISOU 69 CB ASN A 176 18122 15948 14996 -1766 3221 2562 C ATOM 70 CG ASN A 176 11.855 5.537 37.744 1.00136.01 C ANISOU 70 CG ASN A 176 19268 16852 15557 -1845 3241 2662 C ATOM 71 OD1 ASN A 176 11.337 4.974 38.708 1.00142.12 O ANISOU 71 OD1 ASN A 176 20271 17591 16137 -2046 3357 2804 O ATOM 72 ND2 ASN A 176 12.902 6.345 37.865 1.00134.80 N ANISOU 72 ND2 ASN A 176 19106 16769 15340 -1705 3128 2580 N ATOM 73 N GLY A 177 11.319 2.810 33.918 1.00113.70 N ANISOU 73 N GLY A 177 16025 13683 13494 -1719 2934 2687 N ATOM 74 CA GLY A 177 11.169 2.612 32.488 1.00111.04 C ANISOU 74 CA GLY A 177 15435 13306 13451 -1613 2852 2581 C ATOM 75 C GLY A 177 11.773 3.769 31.715 1.00105.79 C ANISOU 75 C GLY A 177 14532 12728 12936 -1401 2760 2369 C ATOM 76 O GLY A 177 11.272 4.169 30.664 1.00105.95 O ANISOU 76 O GLY A 177 14312 12767 13177 -1321 2769 2218 O ATOM 77 N GLU A 178 12.865 4.306 32.243 1.00 98.79 N ANISOU 77 N GLU A 178 13740 11888 11908 -1322 2666 2355 N ATOM 78 CA GLU A 178 13.474 5.501 31.686 1.00 95.95 C ANISOU 78 CA GLU A 178 13212 11619 11624 -1167 2598 2145 C ATOM 79 C GLU A 178 14.993 5.371 31.676 1.00 85.51 C ANISOU 79 C GLU A 178 11964 10298 10228 -1079 2390 2159 C ATOM 80 O GLU A 178 15.575 4.775 32.581 1.00 85.64 O ANISOU 80 O GLU A 178 12210 10287 10040 -1126 2336 2336 O ATOM 81 CB GLU A 178 13.048 6.717 32.507 1.00103.40 C ANISOU 81 CB GLU A 178 14184 12685 12418 -1192 2762 2060 C ATOM 82 CG GLU A 178 13.258 8.047 31.820 1.00107.53 C ANISOU 82 CG GLU A 178 14552 13271 13034 -1058 2733 1821 C ATOM 83 CD GLU A 178 12.422 9.147 32.442 1.00111.74 C ANISOU 83 CD GLU A 178 15098 13885 13473 -1085 2928 1744 C ATOM 84 OE1 GLU A 178 11.341 8.834 32.984 1.00112.50 O ANISOU 84 OE1 GLU A 178 15218 13997 13532 -1197 3104 1837 O ATOM 85 OE2 GLU A 178 12.841 10.322 32.387 1.00112.94 O ANISOU 85 OE2 GLU A 178 15247 14087 13579 -1008 2908 1586 O ATOM 86 N MET A 179 15.631 5.927 30.649 1.00 76.13 N ANISOU 86 N MET A 179 10596 9140 9189 -956 2269 1973 N ATOM 87 CA MET A 179 17.082 5.830 30.511 1.00 62.97 C ANISOU 87 CA MET A 179 8962 7503 7460 -885 2077 1961 C ATOM 88 C MET A 179 17.806 6.267 31.780 1.00 60.17 C ANISOU 88 C MET A 179 8805 7262 6796 -912 2081 2027 C ATOM 89 O MET A 179 17.589 7.370 32.278 1.00 57.89 O ANISOU 89 O MET A 179 8521 7077 6397 -933 2193 1915 O ATOM 90 CB MET A 179 17.589 6.659 29.325 1.00 53.39 C ANISOU 90 CB MET A 179 7541 6339 6407 -792 1983 1703 C ATOM 91 CG MET A 179 19.029 6.337 28.966 1.00 44.09 C ANISOU 91 CG MET A 179 6356 5194 5200 -740 1785 1689 C ATOM 92 SD MET A 179 19.710 7.383 27.668 1.00 44.60 S ANISOU 92 SD MET A 179 6220 5331 5395 -685 1683 1359 S ATOM 93 CE MET A 179 20.315 8.776 28.616 1.00 40.82 C ANISOU 93 CE MET A 179 5855 5041 4616 -728 1734 1235 C ATOM 94 N ARG A 180 18.668 5.395 32.290 1.00 57.93 N ANISOU 94 N ARG A 180 8705 6944 6363 -898 1944 2214 N ATOM 95 CA ARG A 180 19.441 5.680 33.490 1.00 65.02 C ANISOU 95 CA ARG A 180 9813 7954 6939 -905 1912 2296 C ATOM 96 C ARG A 180 20.316 6.904 33.285 1.00 72.75 C ANISOU 96 C ARG A 180 10669 9129 7842 -857 1874 2067 C ATOM 97 O ARG A 180 20.915 7.072 32.223 1.00 72.49 O ANISOU 97 O ARG A 180 10460 9129 7954 -794 1767 1914 O ATOM 98 CB ARG A 180 20.329 4.483 33.837 1.00 66.16 C ANISOU 98 CB ARG A 180 10187 8009 6944 -838 1702 2529 C ATOM 99 CG ARG A 180 19.572 3.224 34.236 1.00 71.99 C ANISOU 99 CG ARG A 180 11147 8523 7683 -906 1715 2771 C ATOM 100 CD ARG A 180 20.468 1.997 34.113 1.00 75.69 C ANISOU 100 CD ARG A 180 11818 8835 8106 -773 1439 2958 C ATOM 101 NE ARG A 180 21.829 2.276 34.565 1.00 78.47 N ANISOU 101 NE ARG A 180 12273 9333 8210 -624 1237 2974 N ATOM 102 CZ ARG A 180 22.903 1.592 34.180 1.00 83.30 C ANISOU 102 CZ ARG A 180 12889 9910 8851 -399 913 2935 C ATOM 103 NH1 ARG A 180 22.780 0.584 33.327 1.00 83.45 N ANISOU 103 NH1 ARG A 180 12892 9708 9105 -330 796 2984 N ATOM 104 NH2 ARG A 180 24.102 1.919 34.643 1.00 86.33 N ANISOU 104 NH2 ARG A 180 13263 10496 9041 -232 697 2801 N ATOM 105 N SER A 181 20.380 7.769 34.291 1.00 77.94 N ANISOU 105 N SER A 181 11430 9914 8269 -907 1966 2029 N ATOM 106 CA SER A 181 21.388 8.819 34.292 1.00 84.31 C ANISOU 106 CA SER A 181 12183 10917 8932 -884 1906 1831 C ATOM 107 C SER A 181 22.651 8.190 34.863 1.00 85.89 C ANISOU 107 C SER A 181 12537 11228 8868 -822 1721 1970 C ATOM 108 O SER A 181 22.575 7.146 35.514 1.00 91.33 O ANISOU 108 O SER A 181 13437 11812 9453 -803 1662 2230 O ATOM 109 CB SER A 181 20.941 10.023 35.125 1.00 89.65 C ANISOU 109 CB SER A 181 12921 11671 9471 -963 2068 1727 C ATOM 110 OG SER A 181 20.746 9.672 36.484 1.00 93.21 O ANISOU 110 OG SER A 181 13602 12123 9689 -1026 2134 1930 O ATOM 111 N ARG A 182 23.804 8.800 34.601 1.00 81.16 N ANISOU 111 N ARG A 182 11856 10842 8140 -782 1610 1789 N ATOM 112 CA ARG A 182 25.086 8.243 35.034 1.00 77.09 C ANISOU 112 CA ARG A 182 11465 10495 7332 -676 1395 1880 C ATOM 113 C ARG A 182 25.571 7.127 34.090 1.00 59.61 C ANISOU 113 C ARG A 182 9147 8173 5328 -515 1146 1887 C ATOM 114 O ARG A 182 26.513 6.395 34.398 1.00 49.85 O ANISOU 114 O ARG A 182 7955 6979 4004 -335 851 1884 O ATOM 115 CB ARG A 182 24.997 7.742 36.481 1.00 89.43 C ANISOU 115 CB ARG A 182 13331 12026 8621 -674 1378 2139 C ATOM 116 CG ARG A 182 26.330 7.432 37.138 1.00105.12 C ANISOU 116 CG ARG A 182 15412 14200 10329 -521 1087 2118 C ATOM 117 CD ARG A 182 26.139 6.577 38.387 1.00117.11 C ANISOU 117 CD ARG A 182 17259 15581 11657 -487 1006 2403 C ATOM 118 NE ARG A 182 27.412 6.196 38.990 1.00125.19 N ANISOU 118 NE ARG A 182 18352 16758 12456 -293 674 2354 N ATOM 119 CZ ARG A 182 28.242 5.294 38.475 1.00129.98 C ANISOU 119 CZ ARG A 182 18876 17340 13171 -45 335 2281 C ATOM 120 NH1 ARG A 182 27.937 4.682 37.338 1.00130.19 N ANISOU 120 NH1 ARG A 182 18757 17179 13529 18 295 2257 N ATOM 121 NH2 ARG A 182 29.380 5.007 39.092 1.00132.95 N ANISOU 121 NH2 ARG A 182 19309 17887 13320 148 33 2224 N ATOM 122 N LEU A 183 24.922 7.009 32.936 1.00 51.74 N ANISOU 122 N LEU A 183 7989 7022 4649 -561 1236 1852 N ATOM 123 CA LEU A 183 25.354 6.082 31.895 1.00 49.24 C ANISOU 123 CA LEU A 183 7521 6586 4601 -421 1003 1786 C ATOM 124 C LEU A 183 26.660 6.605 31.298 1.00 39.67 C ANISOU 124 C LEU A 183 6093 5627 3352 -346 818 1452 C ATOM 125 O LEU A 183 26.823 7.813 31.160 1.00 37.83 O ANISOU 125 O LEU A 183 5777 5589 3006 -473 960 1255 O ATOM 126 CB LEU A 183 24.288 6.014 30.803 1.00 54.23 C ANISOU 126 CB LEU A 183 8025 7017 5563 -530 1184 1814 C ATOM 127 CG LEU A 183 23.996 4.640 30.211 1.00 66.91 C ANISOU 127 CG LEU A 183 9639 8353 7429 -446 1050 1963 C ATOM 128 CD1 LEU A 183 25.265 4.029 29.654 1.00 73.13 C ANISOU 128 CD1 LEU A 183 10311 9187 8288 -242 713 1797 C ATOM 129 CD2 LEU A 183 23.383 3.740 31.270 1.00 69.98 C ANISOU 129 CD2 LEU A 183 10329 8567 7692 -449 1069 2280 C ATOM 130 N SER A 184 27.586 5.715 30.941 1.00 40.06 N ANISOU 130 N SER A 184 6062 5681 3479 -146 506 1374 N ATOM 131 CA SER A 184 28.848 6.148 30.318 1.00 35.77 C ANISOU 131 CA SER A 184 5279 5407 2905 -85 325 1024 C ATOM 132 C SER A 184 28.863 5.919 28.802 1.00 36.52 C ANISOU 132 C SER A 184 5133 5399 3343 -95 284 854 C ATOM 133 O SER A 184 28.177 5.039 28.292 1.00 37.21 O ANISOU 133 O SER A 184 5242 5200 3695 -61 284 1025 O ATOM 134 CB SER A 184 30.060 5.474 30.986 1.00 39.03 C ANISOU 134 CB SER A 184 5724 5982 3125 161 -13 980 C ATOM 135 OG SER A 184 30.250 4.134 30.548 1.00 40.16 O ANISOU 135 OG SER A 184 5861 5922 3476 381 -260 1059 O ATOM 136 N LEU A 185 29.639 6.721 28.081 1.00 33.10 N ANISOU 136 N LEU A 185 4484 5200 2891 -169 258 511 N ATOM 137 CA LEU A 185 29.755 6.530 26.647 1.00 25.00 C ANISOU 137 CA LEU A 185 3234 4092 2173 -196 206 324 C ATOM 138 C LEU A 185 30.324 5.146 26.356 1.00 24.78 C ANISOU 138 C LEU A 185 3143 3962 2313 54 -96 354 C ATOM 139 O LEU A 185 29.855 4.454 25.450 1.00 25.23 O ANISOU 139 O LEU A 185 3138 3767 2682 65 -106 418 O ATOM 140 CB LEU A 185 30.629 7.611 26.005 1.00 25.20 C ANISOU 140 CB LEU A 185 3067 4413 2094 -337 210 -79 C ATOM 141 CG LEU A 185 30.908 7.408 24.509 1.00 23.28 C ANISOU 141 CG LEU A 185 2588 4110 2149 -380 131 -314 C ATOM 142 CD1 LEU A 185 29.616 7.462 23.665 1.00 25.29 C ANISOU 142 CD1 LEU A 185 2865 4040 2704 -523 350 -169 C ATOM 143 CD2 LEU A 185 31.925 8.432 23.999 1.00 27.55 C ANISOU 143 CD2 LEU A 185 2966 4981 2521 -536 112 -740 C ATOM 144 N SER A 186 31.329 4.737 27.123 1.00 26.89 N ANISOU 144 N SER A 186 3434 4419 2362 263 -347 307 N ATOM 145 CA SER A 186 31.969 3.442 26.861 1.00 29.02 C ANISOU 145 CA SER A 186 3654 4607 2765 544 -664 306 C ATOM 146 C SER A 186 31.015 2.252 27.062 1.00 31.26 C ANISOU 146 C SER A 186 4182 4483 3212 641 -664 688 C ATOM 147 O SER A 186 31.060 1.291 26.302 1.00 29.89 O ANISOU 147 O SER A 186 3959 4114 3285 765 -805 703 O ATOM 148 CB SER A 186 33.250 3.279 27.669 1.00 32.06 C ANISOU 148 CB SER A 186 4015 5302 2863 776 -950 162 C ATOM 149 OG SER A 186 34.295 4.034 27.075 1.00 31.84 O ANISOU 149 OG SER A 186 3689 5640 2767 711 -1015 -258 O ATOM 150 N GLU A 187 30.140 2.329 28.057 1.00 30.60 N ANISOU 150 N GLU A 187 4370 4275 2983 559 -493 984 N ATOM 151 CA GLU A 187 29.110 1.293 28.235 1.00 38.48 C ANISOU 151 CA GLU A 187 5619 4894 4109 576 -441 1337 C ATOM 152 C GLU A 187 28.261 1.135 26.965 1.00 29.60 C ANISOU 152 C GLU A 187 4365 3539 3344 423 -278 1353 C ATOM 153 O GLU A 187 28.005 0.025 26.503 1.00 29.75 O ANISOU 153 O GLU A 187 4453 3292 3557 513 -375 1487 O ATOM 154 CB GLU A 187 28.163 1.670 29.372 1.00 41.13 C ANISOU 154 CB GLU A 187 6218 5170 4239 420 -203 1601 C ATOM 155 CG GLU A 187 28.618 1.322 30.762 1.00 50.85 C ANISOU 155 CG GLU A 187 7715 6462 5144 571 -362 1742 C ATOM 156 CD GLU A 187 27.570 1.702 31.794 1.00 63.26 C ANISOU 156 CD GLU A 187 9540 7955 6539 371 -90 1997 C ATOM 157 OE1 GLU A 187 27.391 2.917 32.044 1.00 59.90 O ANISOU 157 OE1 GLU A 187 9033 7731 5995 194 130 1902 O ATOM 158 OE2 GLU A 187 26.913 0.789 32.342 1.00 67.78 O ANISOU 158 OE2 GLU A 187 10407 8263 7083 379 -88 2284 O ATOM 159 N VAL A 188 27.809 2.255 26.416 1.00 27.82 N ANISOU 159 N VAL A 188 3972 3408 3191 189 -30 1219 N ATOM 160 CA VAL A 188 27.015 2.222 25.191 1.00 25.06 C ANISOU 160 CA VAL A 188 3486 2864 3170 37 123 1213 C ATOM 161 C VAL A 188 27.831 1.689 24.012 1.00 26.39 C ANISOU 161 C VAL A 188 3435 3018 3572 144 -96 991 C ATOM 162 O VAL A 188 27.365 0.824 23.271 1.00 29.34 O ANISOU 162 O VAL A 188 3808 3132 4208 150 -112 1102 O ATOM 163 CB VAL A 188 26.413 3.600 24.850 1.00 32.22 C ANISOU 163 CB VAL A 188 4283 3877 4080 -210 410 1094 C ATOM 164 CG1 VAL A 188 25.683 3.547 23.516 1.00 31.75 C ANISOU 164 CG1 VAL A 188 4073 3627 4364 -346 531 1066 C ATOM 165 CG2 VAL A 188 25.475 4.053 25.956 1.00 33.41 C ANISOU 165 CG2 VAL A 188 4645 4018 4032 -313 646 1323 C ATOM 166 N LEU A 189 29.053 2.186 23.852 1.00 23.30 N ANISOU 166 N LEU A 189 2860 2918 3073 217 -259 670 N ATOM 167 CA LEU A 189 29.911 1.729 22.768 1.00 25.44 C ANISOU 167 CA LEU A 189 2901 3219 3545 313 -467 417 C ATOM 168 C LEU A 189 30.210 0.225 22.866 1.00 28.84 C ANISOU 168 C LEU A 189 3443 3454 4061 594 -728 569 C ATOM 169 O LEU A 189 30.213 -0.482 21.863 1.00 26.82 O ANISOU 169 O LEU A 189 3091 3021 4080 628 -804 533 O ATOM 170 CB LEU A 189 31.218 2.528 22.741 1.00 23.72 C ANISOU 170 CB LEU A 189 2473 3401 3136 334 -598 29 C ATOM 171 CG LEU A 189 31.047 4.002 22.356 1.00 22.67 C ANISOU 171 CG LEU A 189 2237 3441 2935 37 -359 -183 C ATOM 172 CD1 LEU A 189 32.373 4.689 22.472 1.00 20.50 C ANISOU 172 CD1 LEU A 189 1796 3577 2416 44 -493 -556 C ATOM 173 CD2 LEU A 189 30.514 4.091 20.928 1.00 23.98 C ANISOU 173 CD2 LEU A 189 2263 3415 3435 -145 -242 -271 C ATOM 174 N ASP A 190 30.463 -0.253 24.080 1.00 28.66 N ANISOU 174 N ASP A 190 3647 3452 3790 792 -867 738 N ATOM 175 CA ASP A 190 30.800 -1.659 24.299 1.00 35.23 C ANISOU 175 CA ASP A 190 4649 4091 4644 1089 -1139 882 C ATOM 176 C ASP A 190 29.609 -2.603 24.078 1.00 37.13 C ANISOU 176 C ASP A 190 5128 3904 5074 1019 -1020 1225 C ATOM 177 O ASP A 190 29.779 -3.775 23.732 1.00 38.34 O ANISOU 177 O ASP A 190 5382 3835 5350 1204 -1207 1303 O ATOM 178 CB ASP A 190 31.339 -1.857 25.723 1.00 39.95 C ANISOU 178 CB ASP A 190 5473 4815 4893 1306 -1318 982 C ATOM 179 CG ASP A 190 32.766 -1.348 25.894 1.00 43.75 C ANISOU 179 CG ASP A 190 5717 5717 5188 1471 -1543 629 C ATOM 180 OD1 ASP A 190 33.251 -1.322 27.047 1.00 42.28 O ANISOU 180 OD1 ASP A 190 5677 5689 4697 1624 -1677 675 O ATOM 181 OD2 ASP A 190 33.406 -0.984 24.885 1.00 39.51 O ANISOU 181 OD2 ASP A 190 4850 5364 4796 1435 -1586 297 O ATOM 182 N SER A 191 28.408 -2.087 24.300 1.00 31.07 N ANISOU 182 N SER A 191 4459 3037 4310 750 -707 1420 N ATOM 183 CA SER A 191 27.205 -2.920 24.382 1.00 39.79 C ANISOU 183 CA SER A 191 5825 3786 5505 651 -568 1763 C ATOM 184 C SER A 191 26.735 -3.468 23.040 1.00 40.59 C ANISOU 184 C SER A 191 5806 3657 5959 557 -513 1763 C ATOM 185 O SER A 191 26.009 -4.458 22.992 1.00 42.18 O ANISOU 185 O SER A 191 6233 3557 6238 530 -480 2018 O ATOM 186 CB SER A 191 26.064 -2.104 24.952 1.00 30.98 C ANISOU 186 CB SER A 191 4790 2688 4294 381 -235 1922 C ATOM 187 OG SER A 191 25.632 -1.172 23.967 1.00 32.65 O ANISOU 187 OG SER A 191 4718 2976 4711 164 -22 1757 O ATOM 188 N GLY A 192 27.120 -2.802 21.960 1.00 38.04 N ANISOU 188 N GLY A 192 5146 3476 5832 477 -492 1475 N ATOM 189 CA GLY A 192 26.622 -3.139 20.641 1.00 34.37 C ANISOU 189 CA GLY A 192 4542 2812 5704 342 -409 1457 C ATOM 190 C GLY A 192 25.247 -2.551 20.370 1.00 38.45 C ANISOU 190 C GLY A 192 5034 3251 6325 33 -68 1588 C ATOM 191 O GLY A 192 24.648 -2.825 19.332 1.00 39.50 O ANISOU 191 O GLY A 192 4954 3397 6656 -92 24 1494 O ATOM 192 N ASP A 193 24.746 -1.733 21.294 1.00 35.54 N ANISOU 192 N ASP A 193 4755 3003 5744 -65 110 1676 N ATOM 193 CA ASP A 193 23.400 -1.174 21.173 1.00 33.87 C ANISOU 193 CA ASP A 193 4408 2915 5545 -261 399 1649 C ATOM 194 C ASP A 193 23.358 0.278 20.701 1.00 31.57 C ANISOU 194 C ASP A 193 3879 2857 5257 -345 523 1381 C ATOM 195 O ASP A 193 22.310 0.911 20.772 1.00 33.63 O ANISOU 195 O ASP A 193 4088 3212 5478 -386 705 1339 O ATOM 196 CB ASP A 193 22.664 -1.264 22.506 1.00 31.97 C ANISOU 196 CB ASP A 193 4431 2651 5066 -294 526 1889 C ATOM 197 CG ASP A 193 22.290 -2.687 22.866 1.00 42.42 C ANISOU 197 CG ASP A 193 6008 3745 6366 -251 458 2129 C ATOM 198 OD1 ASP A 193 22.483 -3.081 24.034 1.00 49.65 O ANISOU 198 OD1 ASP A 193 7250 4570 7044 -178 390 2345 O ATOM 199 OD2 ASP A 193 21.811 -3.412 21.974 1.00 48.37 O ANISOU 199 OD2 ASP A 193 6653 4415 7312 -287 466 2098 O ATOM 200 N LEU A 194 24.485 0.820 20.258 1.00 25.24 N ANISOU 200 N LEU A 194 3040 2784 3766 144 -675 862 N ATOM 201 CA LEU A 194 24.499 2.241 19.867 1.00 29.88 C ANISOU 201 CA LEU A 194 3606 3403 4345 175 -551 804 C ATOM 202 C LEU A 194 23.355 2.624 18.915 1.00 28.24 C ANISOU 202 C LEU A 194 3346 3199 4185 160 -506 880 C ATOM 203 O LEU A 194 22.761 3.692 19.048 1.00 26.31 O ANISOU 203 O LEU A 194 3072 2996 3930 176 -386 907 O ATOM 204 CB LEU A 194 25.852 2.639 19.268 1.00 22.12 C ANISOU 204 CB LEU A 194 2647 2397 3360 210 -563 654 C ATOM 205 CG LEU A 194 25.974 4.108 18.812 1.00 24.07 C ANISOU 205 CG LEU A 194 2877 2671 3598 240 -443 586 C ATOM 206 CD1 LEU A 194 27.417 4.613 18.971 1.00 23.06 C ANISOU 206 CD1 LEU A 194 2782 2545 3434 271 -436 449 C ATOM 207 CD2 LEU A 194 25.508 4.264 17.370 1.00 27.22 C ANISOU 207 CD2 LEU A 194 3241 3046 4058 233 -446 593 C ATOM 208 N MET A 195 23.047 1.769 17.950 1.00 25.78 N ANISOU 208 N MET A 195 3026 2844 3927 128 -602 916 N ATOM 209 CA MET A 195 22.037 2.126 16.952 1.00 23.66 C ANISOU 209 CA MET A 195 2707 2578 3705 107 -570 986 C ATOM 210 C MET A 195 20.662 2.343 17.591 1.00 32.83 C ANISOU 210 C MET A 195 3819 3791 4864 87 -501 1136 C ATOM 211 O MET A 195 19.863 3.114 17.080 1.00 28.04 O ANISOU 211 O MET A 195 3161 3209 4281 88 -423 1189 O ATOM 212 CB MET A 195 21.963 1.080 15.836 1.00 25.87 C ANISOU 212 CB MET A 195 2998 2797 4033 67 -696 1001 C ATOM 213 CG MET A 195 23.207 1.063 14.935 1.00 27.92 C ANISOU 213 CG MET A 195 3297 3009 4303 94 -741 855 C ATOM 214 SD MET A 195 23.342 2.607 13.990 1.00 27.26 S ANISOU 214 SD MET A 195 3177 2950 4229 127 -625 778 S ATOM 215 CE MET A 195 21.846 2.511 13.004 1.00 25.49 C ANISOU 215 CE MET A 195 2901 2725 4059 70 -634 914 C ATOM 216 N LYS A 196 20.392 1.685 18.718 1.00 30.13 N ANISOU 216 N LYS A 196 3489 3465 4492 70 -527 1208 N ATOM 217 CA LYS A 196 19.142 1.943 19.438 1.00 31.73 C ANISOU 217 CA LYS A 196 3645 3724 4687 58 -449 1349 C ATOM 218 C LYS A 196 19.135 3.298 20.146 1.00 29.24 C ANISOU 218 C LYS A 196 3322 3461 4326 110 -290 1317 C ATOM 219 O LYS A 196 18.112 3.971 20.202 1.00 30.12 O ANISOU 219 O LYS A 196 3382 3615 4449 118 -189 1409 O ATOM 220 CB LYS A 196 18.857 0.825 20.443 1.00 34.49 C ANISOU 220 CB LYS A 196 4011 4078 5014 21 -525 1437 C ATOM 221 CG LYS A 196 18.620 -0.531 19.794 1.00 42.38 C ANISOU 221 CG LYS A 196 5018 5025 6058 -37 -677 1496 C ATOM 222 CD LYS A 196 18.249 -1.589 20.834 1.00 47.29 C ANISOU 222 CD LYS A 196 5654 5655 6659 -76 -747 1595 C ATOM 223 CE LYS A 196 18.190 -2.977 20.215 1.00 56.07 C ANISOU 223 CE LYS A 196 6793 6702 7810 -134 -908 1635 C ATOM 224 NZ LYS A 196 17.882 -4.021 21.233 1.00 64.36 N ANISOU 224 NZ LYS A 196 7860 7756 8838 -173 -981 1730 N ATOM 225 N PHE A 197 20.273 3.693 20.710 1.00 24.88 N ANISOU 225 N PHE A 197 2825 2905 3723 144 -267 1192 N ATOM 226 CA PHE A 197 20.377 5.012 21.334 1.00 25.61 C ANISOU 226 CA PHE A 197 2927 3036 3766 191 -119 1146 C ATOM 227 C PHE A 197 20.331 6.158 20.306 1.00 25.26 C ANISOU 227 C PHE A 197 2855 2990 3753 221 -36 1096 C ATOM 228 O PHE A 197 19.733 7.212 20.544 1.00 24.10 O ANISOU 228 O PHE A 197 2686 2877 3593 251 98 1127 O ATOM 229 CB PHE A 197 21.698 5.113 22.100 1.00 23.76 C ANISOU 229 CB PHE A 197 2762 2795 3469 209 -133 1021 C ATOM 230 CG PHE A 197 21.708 4.358 23.405 1.00 31.62 C ANISOU 230 CG PHE A 197 3790 3809 4416 189 -171 1071 C ATOM 231 CD1 PHE A 197 21.468 5.016 24.605 1.00 38.10 C ANISOU 231 CD1 PHE A 197 4635 4674 5168 205 -62 1091 C ATOM 232 CD2 PHE A 197 21.979 3.005 23.436 1.00 36.69 C ANISOU 232 CD2 PHE A 197 4445 4419 5076 153 -314 1094 C ATOM 233 CE1 PHE A 197 21.494 4.322 25.815 1.00 36.44 C ANISOU 233 CE1 PHE A 197 4456 4481 4907 182 -99 1137 C ATOM 234 CE2 PHE A 197 22.002 2.308 24.638 1.00 37.85 C ANISOU 234 CE2 PHE A 197 4621 4582 5177 132 -353 1142 C ATOM 235 CZ PHE A 197 21.756 2.969 25.823 1.00 35.34 C ANISOU 235 CZ PHE A 197 4322 4314 4791 145 -246 1164 C ATOM 236 N ALA A 198 21.004 5.960 19.178 1.00 23.93 N ANISOU 236 N ALA A 198 2690 2779 3623 215 -112 1014 N ATOM 237 CA ALA A 198 21.185 7.038 18.198 1.00 22.32 C ANISOU 237 CA ALA A 198 2468 2570 3442 241 -43 945 C ATOM 238 C ALA A 198 19.888 7.448 17.496 1.00 25.87 C ANISOU 238 C ALA A 198 2847 3038 3944 233 14 1060 C ATOM 239 O ALA A 198 19.782 8.570 16.985 1.00 28.08 O ANISOU 239 O ALA A 198 3107 3328 4236 263 110 1030 O ATOM 240 CB ALA A 198 22.266 6.654 17.171 1.00 21.60 C ANISOU 240 CB ALA A 198 2400 2431 3376 236 -143 829 C ATOM 241 N VAL A 199 18.902 6.550 17.457 1.00 25.68 N ANISOU 241 N VAL A 199 2784 3019 3954 191 -46 1195 N ATOM 242 CA VAL A 199 17.608 6.902 16.851 1.00 30.14 C ANISOU 242 CA VAL A 199 3273 3609 4571 178 6 1324 C ATOM 243 C VAL A 199 16.514 7.247 17.872 1.00 34.65 C ANISOU 243 C VAL A 199 3805 4236 5124 194 112 1454 C ATOM 244 O VAL A 199 15.344 7.405 17.515 1.00 32.87 O ANISOU 244 O VAL A 199 3507 4038 4943 182 151 1586 O ATOM 245 CB VAL A 199 17.093 5.809 15.891 1.00 25.56 C ANISOU 245 CB VAL A 199 2664 3000 4048 113 -126 1404 C ATOM 246 CG1 VAL A 199 18.136 5.525 14.805 1.00 24.38 C ANISOU 246 CG1 VAL A 199 2556 2793 3915 103 -219 1275 C ATOM 247 CG2 VAL A 199 16.699 4.534 16.659 1.00 30.17 C ANISOU 247 CG2 VAL A 199 3257 3585 4621 69 -218 1500 C ATOM 248 N ASP A 200 16.909 7.390 19.129 1.00 29.28 N ANISOU 248 N ASP A 200 3173 3575 4379 221 163 1418 N ATOM 249 CA ASP A 200 15.993 7.732 20.214 1.00 29.51 C ANISOU 249 CA ASP A 200 3178 3656 4379 243 274 1527 C ATOM 250 C ASP A 200 16.297 9.162 20.646 1.00 32.97 C ANISOU 250 C ASP A 200 3647 4108 4772 308 431 1447 C ATOM 251 O ASP A 200 17.457 9.546 20.732 1.00 27.91 O ANISOU 251 O ASP A 200 3072 3443 4092 327 428 1301 O ATOM 252 CB ASP A 200 16.201 6.757 21.375 1.00 33.61 C ANISOU 252 CB ASP A 200 3739 4182 4848 218 209 1549 C ATOM 253 CG ASP A 200 15.310 7.061 22.581 1.00 45.02 C ANISOU 253 CG ASP A 200 5169 5684 6254 239 324 1658 C ATOM 254 OD1 ASP A 200 14.085 6.808 22.518 1.00 42.00 O ANISOU 254 OD1 ASP A 200 4712 5336 5909 222 342 1815 O ATOM 255 OD2 ASP A 200 15.850 7.522 23.610 1.00 41.36 O ANISOU 255 OD2 ASP A 200 4767 5232 5717 271 394 1589 O ATOM 256 N LYS A 201 15.272 9.972 20.903 1.00 32.17 N ANISOU 256 N LYS A 201 3500 4046 4677 345 568 1543 N ATOM 257 CA LYS A 201 15.527 11.369 21.257 1.00 35.75 C ANISOU 257 CA LYS A 201 3990 4505 5089 409 722 1467 C ATOM 258 C LYS A 201 16.479 11.490 22.456 1.00 33.96 C ANISOU 258 C LYS A 201 3862 4273 4768 423 743 1360 C ATOM 259 O LYS A 201 17.506 12.151 22.376 1.00 34.75 O ANISOU 259 O LYS A 201 4023 4347 4833 441 762 1218 O ATOM 260 CB LYS A 201 14.217 12.109 21.544 1.00 39.66 C ANISOU 260 CB LYS A 201 4426 5043 5601 452 872 1601 C ATOM 261 CG LYS A 201 14.414 13.577 21.873 1.00 48.20 C ANISOU 261 CG LYS A 201 5552 6121 6640 521 1038 1526 C ATOM 262 CD LYS A 201 13.092 14.325 21.900 1.00 57.66 C ANISOU 262 CD LYS A 201 6680 7356 7873 571 1185 1664 C ATOM 263 CE LYS A 201 13.262 15.713 22.503 1.00 61.64 C ANISOU 263 CE LYS A 201 7249 7853 8320 645 1360 1593 C ATOM 264 NZ LYS A 201 14.457 16.424 21.956 1.00 54.08 N ANISOU 264 NZ LYS A 201 6359 6847 7344 651 1347 1420 N ATOM 265 N THR A 202 16.128 10.844 23.562 1.00 30.17 N ANISOU 265 N THR A 202 3395 3822 4247 408 737 1433 N ATOM 266 CA THR A 202 16.916 10.905 24.794 1.00 31.70 C ANISOU 266 CA THR A 202 3682 4018 4347 414 757 1351 C ATOM 267 C THR A 202 18.279 10.247 24.647 1.00 30.18 C ANISOU 267 C THR A 202 3543 3788 4137 378 616 1224 C ATOM 268 O THR A 202 19.283 10.751 25.154 1.00 34.39 O ANISOU 268 O THR A 202 4154 4309 4605 390 638 1103 O ATOM 269 CB THR A 202 16.173 10.204 25.967 1.00 42.52 C ANISOU 269 CB THR A 202 5046 5429 5680 398 767 1472 C ATOM 270 OG1 THR A 202 14.905 10.837 26.186 1.00 41.38 O ANISOU 270 OG1 THR A 202 4849 5324 5548 438 911 1596 O ATOM 271 CG2 THR A 202 16.994 10.276 27.245 1.00 48.13 C ANISOU 271 CG2 THR A 202 5857 6142 6289 398 785 1389 C ATOM 272 N GLY A 203 18.312 9.108 23.967 1.00 29.27 N ANISOU 272 N GLY A 203 3388 3653 4078 334 470 1256 N ATOM 273 CA GLY A 203 19.560 8.388 23.772 1.00 30.43 C ANISOU 273 CA GLY A 203 3581 3764 4218 306 333 1147 C ATOM 274 C GLY A 203 20.529 9.182 22.912 1.00 33.67 C ANISOU 274 C GLY A 203 4013 4143 4638 328 342 1006 C ATOM 275 O GLY A 203 21.728 9.244 23.192 1.00 28.61 O ANISOU 275 O GLY A 203 3432 3485 3952 328 305 887 O ATOM 276 N CYS A 204 20.015 9.806 21.860 1.00 29.53 N ANISOU 276 N CYS A 204 3437 3613 4170 344 391 1024 N ATOM 277 CA CYS A 204 20.895 10.544 20.952 1.00 25.01 C ANISOU 277 CA CYS A 204 2880 3012 3610 362 396 897 C ATOM 278 C CYS A 204 21.396 11.832 21.594 1.00 27.06 C ANISOU 278 C CYS A 204 3199 3282 3802 401 522 808 C ATOM 279 O CYS A 204 22.530 12.262 21.367 1.00 24.58 O ANISOU 279 O CYS A 204 2929 2948 3464 406 505 679 O ATOM 280 CB CYS A 204 20.191 10.848 19.639 1.00 26.66 C ANISOU 280 CB CYS A 204 3019 3213 3897 364 410 945 C ATOM 281 SG CYS A 204 21.369 11.254 18.306 1.00 34.35 S ANISOU 281 SG CYS A 204 4005 4146 4898 366 357 794 S ATOM 282 N GLN A 205 20.541 12.444 22.401 1.00 30.70 N ANISOU 282 N GLN A 205 3663 3771 4230 428 649 882 N ATOM 283 CA GLN A 205 20.917 13.617 23.169 1.00 34.46 C ANISOU 283 CA GLN A 205 4210 4252 4630 463 775 808 C ATOM 284 C GLN A 205 22.120 13.297 24.053 1.00 34.68 C ANISOU 284 C GLN A 205 4321 4276 4582 439 712 709 C ATOM 285 O GLN A 205 23.079 14.073 24.126 1.00 31.12 O ANISOU 285 O GLN A 205 3930 3811 4085 447 740 590 O ATOM 286 CB GLN A 205 19.732 14.053 24.036 1.00 45.44 C ANISOU 286 CB GLN A 205 5595 5675 5994 494 911 921 C ATOM 287 CG GLN A 205 19.903 15.384 24.730 1.00 54.97 C ANISOU 287 CG GLN A 205 6878 6881 7128 537 1064 857 C ATOM 288 CD GLN A 205 18.648 15.791 25.493 1.00 66.00 C ANISOU 288 CD GLN A 205 8263 8308 8506 576 1208 977 C ATOM 289 OE1 GLN A 205 18.309 15.198 26.522 1.00 62.44 O ANISOU 289 OE1 GLN A 205 7829 7884 8010 564 1208 1042 O ATOM 290 NE2 GLN A 205 17.949 16.802 24.984 1.00 65.08 N ANISOU 290 NE2 GLN A 205 8114 8187 8424 626 1332 1011 N ATOM 291 N PHE A 206 22.070 12.145 24.713 1.00 32.10 N ANISOU 291 N PHE A 206 3995 3961 4242 407 623 764 N ATOM 292 CA PHE A 206 23.181 11.681 25.532 1.00 31.38 C ANISOU 292 CA PHE A 206 3970 3866 4084 379 546 686 C ATOM 293 C PHE A 206 24.456 11.474 24.702 1.00 29.64 C ANISOU 293 C PHE A 206 3756 3616 3889 366 438 568 C ATOM 294 O PHE A 206 25.508 12.006 25.048 1.00 27.74 O ANISOU 294 O PHE A 206 3576 3372 3593 364 444 460 O ATOM 295 CB PHE A 206 22.812 10.400 26.289 1.00 31.99 C ANISOU 295 CB PHE A 206 4039 3961 4156 346 463 780 C ATOM 296 CG PHE A 206 24.003 9.648 26.816 1.00 31.23 C ANISOU 296 CG PHE A 206 3991 3855 4020 313 343 708 C ATOM 297 CD1 PHE A 206 24.708 10.123 27.913 1.00 32.81 C ANISOU 297 CD1 PHE A 206 4272 4069 4125 307 382 643 C ATOM 298 CD2 PHE A 206 24.427 8.475 26.207 1.00 34.27 C ANISOU 298 CD2 PHE A 206 4344 4216 4462 288 192 708 C ATOM 299 CE1 PHE A 206 25.811 9.436 28.399 1.00 40.23 C ANISOU 299 CE1 PHE A 206 5250 5003 5031 275 269 586 C ATOM 300 CE2 PHE A 206 25.535 7.779 26.689 1.00 37.22 C ANISOU 300 CE2 PHE A 206 4758 4581 4805 264 84 647 C ATOM 301 CZ PHE A 206 26.225 8.267 27.787 1.00 36.15 C ANISOU 301 CZ PHE A 206 4694 4465 4578 257 122 589 C ATOM 302 N LEU A 207 24.359 10.718 23.607 1.00 30.20 N ANISOU 302 N LEU A 207 3765 3666 4042 355 340 590 N ATOM 303 CA LEU A 207 25.518 10.503 22.733 1.00 23.12 C ANISOU 303 CA LEU A 207 2870 2741 3175 349 244 482 C ATOM 304 C LEU A 207 26.103 11.824 22.226 1.00 20.85 C ANISOU 304 C LEU A 207 2602 2447 2872 373 325 377 C ATOM 305 O LEU A 207 27.317 12.018 22.247 1.00 27.32 O ANISOU 305 O LEU A 207 3460 3261 3661 368 287 269 O ATOM 306 CB LEU A 207 25.158 9.590 21.554 1.00 23.17 C ANISOU 306 CB LEU A 207 2813 2722 3269 335 146 528 C ATOM 307 CG LEU A 207 24.880 8.151 21.993 1.00 27.60 C ANISOU 307 CG LEU A 207 3366 3278 3843 304 35 610 C ATOM 308 CD1 LEU A 207 24.418 7.288 20.825 1.00 30.43 C ANISOU 308 CD1 LEU A 207 3673 3605 4284 285 -57 662 C ATOM 309 CD2 LEU A 207 26.109 7.539 22.666 1.00 26.93 C ANISOU 309 CD2 LEU A 207 3332 3185 3715 292 -55 535 C ATOM 310 N GLU A 208 25.231 12.741 21.807 1.00 21.82 N ANISOU 310 N GLU A 208 2700 2575 3016 399 438 416 N ATOM 311 CA GLU A 208 25.668 14.032 21.264 1.00 27.20 C ANISOU 311 CA GLU A 208 3398 3248 3689 422 520 326 C ATOM 312 C GLU A 208 26.486 14.831 22.270 1.00 30.56 C ANISOU 312 C GLU A 208 3910 3682 4021 423 579 240 C ATOM 313 O GLU A 208 27.484 15.438 21.910 1.00 33.34 O ANISOU 313 O GLU A 208 4290 4023 4355 422 573 132 O ATOM 314 CB GLU A 208 24.478 14.866 20.766 1.00 32.65 C ANISOU 314 CB GLU A 208 4046 3941 4418 452 639 399 C ATOM 315 CG GLU A 208 24.170 14.684 19.283 1.00 32.91 C ANISOU 315 CG GLU A 208 4005 3958 4541 450 592 419 C ATOM 316 CD GLU A 208 25.257 15.279 18.402 1.00 46.15 C ANISOU 316 CD GLU A 208 5695 5615 6224 451 570 291 C ATOM 317 OE1 GLU A 208 25.291 16.521 18.223 1.00 49.74 O ANISOU 317 OE1 GLU A 208 6169 6067 6664 476 674 248 O ATOM 318 OE2 GLU A 208 26.090 14.503 17.895 1.00 43.46 O ANISOU 318 OE2 GLU A 208 5349 5260 5903 430 452 235 O ATOM 319 N LYS A 209 26.065 14.824 23.530 1.00 26.41 N ANISOU 319 N LYS A 209 3428 3175 3431 422 634 289 N ATOM 320 CA LYS A 209 26.795 15.538 24.575 1.00 31.00 C ANISOU 320 CA LYS A 209 4103 3762 3913 414 687 214 C ATOM 321 C LYS A 209 28.079 14.793 24.894 1.00 31.28 C ANISOU 321 C LYS A 209 4165 3800 3920 376 557 143 C ATOM 322 O LYS A 209 29.142 15.394 25.058 1.00 28.06 O ANISOU 322 O LYS A 209 3811 3391 3462 363 554 41 O ATOM 323 CB LYS A 209 25.944 15.654 25.845 1.00 39.36 C ANISOU 323 CB LYS A 209 5205 4842 4910 421 781 293 C ATOM 324 CG LYS A 209 26.401 16.745 26.798 1.00 50.28 C ANISOU 324 CG LYS A 209 6694 6224 6187 421 882 221 C ATOM 325 CD LYS A 209 26.440 18.094 26.087 1.00 62.25 C ANISOU 325 CD LYS A 209 8225 7717 7712 452 983 159 C ATOM 326 CE LYS A 209 26.204 19.253 27.044 1.00 68.01 C ANISOU 326 CE LYS A 209 9053 8440 8347 470 1134 140 C ATOM 327 NZ LYS A 209 27.112 19.208 28.222 1.00 73.34 N ANISOU 327 NZ LYS A 209 9828 9123 8915 426 1103 77 N ATOM 328 N ALA A 210 27.972 13.471 24.985 1.00 26.97 N ANISOU 328 N ALA A 210 3582 3258 3407 358 447 202 N ATOM 329 CA ALA A 210 29.129 12.653 25.308 1.00 28.39 C ANISOU 329 CA ALA A 210 3780 3439 3567 328 320 150 C ATOM 330 C ALA A 210 30.260 12.820 24.287 1.00 26.92 C ANISOU 330 C ALA A 210 3576 3237 3416 330 256 45 C ATOM 331 O ALA A 210 31.427 12.877 24.666 1.00 29.17 O ANISOU 331 O ALA A 210 3899 3530 3656 310 207 -32 O ATOM 332 CB ALA A 210 28.721 11.180 25.459 1.00 23.07 C ANISOU 332 CB ALA A 210 3067 2765 2934 313 214 239 C ATOM 333 N VAL A 211 29.934 12.934 23.003 1.00 22.65 N ANISOU 333 N VAL A 211 2977 2678 2953 351 258 45 N ATOM 334 CA VAL A 211 31.003 12.990 21.989 1.00 22.32 C ANISOU 334 CA VAL A 211 2914 2622 2945 353 192 -50 C ATOM 335 C VAL A 211 31.641 14.373 21.830 1.00 26.12 C ANISOU 335 C VAL A 211 3431 3108 3385 358 272 -145 C ATOM 336 O VAL A 211 32.582 14.535 21.068 1.00 25.32 O ANISOU 336 O VAL A 211 3315 3002 3304 358 227 -226 O ATOM 337 CB VAL A 211 30.560 12.436 20.596 1.00 25.34 C ANISOU 337 CB VAL A 211 3224 2980 3424 367 143 -23 C ATOM 338 CG1 VAL A 211 30.106 10.983 20.724 1.00 29.34 C ANISOU 338 CG1 VAL A 211 3704 3475 3968 355 44 62 C ATOM 339 CG2 VAL A 211 29.452 13.291 19.976 1.00 29.63 C ANISOU 339 CG2 VAL A 211 3739 3520 3999 387 251 23 C ATOM 340 N LYS A 212 31.122 15.368 22.543 1.00 22.19 N ANISOU 340 N LYS A 212 2983 2618 2828 362 393 -133 N ATOM 341 CA LYS A 212 31.726 16.695 22.551 1.00 25.69 C ANISOU 341 CA LYS A 212 3479 3061 3221 360 470 -221 C ATOM 342 C LYS A 212 32.815 16.825 23.617 1.00 34.73 C ANISOU 342 C LYS A 212 4696 4223 4275 324 439 -284 C ATOM 343 O LYS A 212 33.512 17.842 23.680 1.00 29.86 O ANISOU 343 O LYS A 212 4130 3608 3609 310 482 -363 O ATOM 344 CB LYS A 212 30.656 17.771 22.783 1.00 33.21 C ANISOU 344 CB LYS A 212 4460 4006 4151 385 622 -182 C ATOM 345 CG LYS A 212 29.752 17.992 21.569 1.00 40.55 C ANISOU 345 CG LYS A 212 5318 4921 5169 418 664 -137 C ATOM 346 CD LYS A 212 28.686 19.045 21.830 1.00 56.60 C ANISOU 346 CD LYS A 212 7374 6946 7185 450 819 -90 C ATOM 347 CE LYS A 212 27.695 19.113 20.672 1.00 68.22 C ANISOU 347 CE LYS A 212 8763 8408 8750 479 849 -23 C ATOM 348 NZ LYS A 212 26.521 19.983 20.978 1.00 76.37 N ANISOU 348 NZ LYS A 212 9805 9437 9775 518 998 47 N ATOM 349 N GLY A 213 32.944 15.811 24.467 1.00 29.73 N ANISOU 349 N GLY A 213 4073 3604 3619 303 364 -243 N ATOM 350 CA GLY A 213 33.900 15.873 25.565 1.00 25.88 C ANISOU 350 CA GLY A 213 3655 3137 3043 263 330 -287 C ATOM 351 C GLY A 213 35.228 15.235 25.202 1.00 28.96 C ANISOU 351 C GLY A 213 4013 3537 3455 245 199 -345 C ATOM 352 O GLY A 213 35.508 14.984 24.034 1.00 24.05 O ANISOU 352 O GLY A 213 3326 2903 2908 267 151 -371 O ATOM 353 N SER A 214 36.062 14.978 26.201 1.00 23.03 N ANISOU 353 N SER A 214 3307 2807 2636 206 141 -363 N ATOM 354 CA SER A 214 37.318 14.283 25.956 1.00 23.25 C ANISOU 354 CA SER A 214 3299 2849 2687 193 14 -404 C ATOM 355 C SER A 214 37.001 12.864 25.509 1.00 30.25 C ANISOU 355 C SER A 214 4116 3721 3658 219 -79 -344 C ATOM 356 O SER A 214 36.174 12.189 26.111 1.00 34.79 O ANISOU 356 O SER A 214 4696 4292 4231 218 -82 -264 O ATOM 357 CB SER A 214 38.166 14.254 27.234 1.00 32.45 C ANISOU 357 CB SER A 214 4527 4043 3760 141 -29 -418 C ATOM 358 OG SER A 214 38.396 15.572 27.699 1.00 32.01 O ANISOU 358 OG SER A 214 4550 3994 3617 109 58 -471 O ATOM 359 N LEU A 215 37.636 12.420 24.433 1.00 22.25 N ANISOU 359 N LEU A 215 3040 2698 2717 242 -152 -381 N ATOM 360 CA LEU A 215 37.498 11.037 24.011 1.00 20.46 C ANISOU 360 CA LEU A 215 2759 2452 2565 265 -250 -333 C ATOM 361 C LEU A 215 38.872 10.379 23.962 1.00 22.33 C ANISOU 361 C LEU A 215 2971 2699 2813 264 -363 -376 C ATOM 362 O LEU A 215 39.819 10.984 23.471 1.00 21.66 O ANISOU 362 O LEU A 215 2875 2629 2725 264 -365 -451 O ATOM 363 CB LEU A 215 36.867 10.979 22.619 1.00 20.08 C ANISOU 363 CB LEU A 215 2656 2372 2601 302 -231 -330 C ATOM 364 CG LEU A 215 35.496 11.656 22.490 1.00 19.19 C ANISOU 364 CG LEU A 215 2551 2249 2490 309 -118 -281 C ATOM 365 CD1 LEU A 215 35.069 11.641 21.023 1.00 20.41 C ANISOU 365 CD1 LEU A 215 2650 2378 2729 339 -113 -286 C ATOM 366 CD2 LEU A 215 34.489 10.882 23.317 1.00 27.07 C ANISOU 366 CD2 LEU A 215 3560 3245 3481 301 -124 -179 C ATOM 367 N THR A 216 38.964 9.143 24.458 1.00 20.32 N ANISOU 367 N THR A 216 2707 2438 2576 263 -457 -323 N ATOM 368 CA THR A 216 40.169 8.344 24.295 1.00 21.38 C ANISOU 368 CA THR A 216 2808 2576 2740 275 -568 -350 C ATOM 369 C THR A 216 40.207 7.817 22.880 1.00 22.35 C ANISOU 369 C THR A 216 2874 2663 2955 323 -604 -371 C ATOM 370 O THR A 216 39.180 7.792 22.188 1.00 20.66 O ANISOU 370 O THR A 216 2649 2420 2783 339 -563 -344 O ATOM 371 CB THR A 216 40.177 7.137 25.238 1.00 26.49 C ANISOU 371 CB THR A 216 3464 3220 3380 263 -658 -280 C ATOM 372 OG1 THR A 216 39.118 6.239 24.869 1.00 24.89 O ANISOU 372 OG1 THR A 216 3245 2977 3237 284 -676 -212 O ATOM 373 CG2 THR A 216 39.992 7.584 26.683 1.00 32.81 C ANISOU 373 CG2 THR A 216 4328 4054 4084 211 -621 -249 C ATOM 374 N SER A 217 41.402 7.431 22.443 1.00 19.95 N ANISOU 374 N SER A 217 2535 2364 2680 344 -677 -419 N ATOM 375 CA SER A 217 41.590 6.827 21.135 1.00 19.58 C ANISOU 375 CA SER A 217 2441 2282 2717 392 -717 -444 C ATOM 376 C SER A 217 40.584 5.710 20.859 1.00 22.97 C ANISOU 376 C SER A 217 2868 2659 3200 409 -756 -374 C ATOM 377 O SER A 217 39.974 5.660 19.787 1.00 21.03 O ANISOU 377 O SER A 217 2606 2380 3005 430 -734 -378 O ATOM 378 CB SER A 217 43.011 6.269 21.017 1.00 21.10 C ANISOU 378 CB SER A 217 2599 2486 2930 417 -804 -482 C ATOM 379 OG SER A 217 43.203 5.709 19.732 1.00 26.11 O ANISOU 379 OG SER A 217 3196 3084 3641 468 -835 -511 O ATOM 380 N TYR A 218 40.402 4.802 21.812 1.00 23.49 N ANISOU 380 N TYR A 218 2953 2718 3254 396 -817 -307 N ATOM 381 CA TYR A 218 39.520 3.671 21.542 1.00 22.75 C ANISOU 381 CA TYR A 218 2859 2573 3212 408 -865 -239 C ATOM 382 C TYR A 218 38.058 4.097 21.439 1.00 20.56 C ANISOU 382 C TYR A 218 2593 2287 2930 386 -787 -187 C ATOM 383 O TYR A 218 37.336 3.573 20.610 1.00 19.87 O ANISOU 383 O TYR A 218 2494 2158 2898 399 -802 -157 O ATOM 384 CB TYR A 218 39.670 2.561 22.576 1.00 24.78 C ANISOU 384 CB TYR A 218 3133 2823 3460 397 -954 -175 C ATOM 385 CG TYR A 218 38.937 1.310 22.161 1.00 23.33 C ANISOU 385 CG TYR A 218 2949 2578 3336 411 -1019 -112 C ATOM 386 CD1 TYR A 218 39.216 0.696 20.945 1.00 27.23 C ANISOU 386 CD1 TYR A 218 3423 3022 3899 453 -1064 -146 C ATOM 387 CD2 TYR A 218 37.981 0.736 22.985 1.00 24.83 C ANISOU 387 CD2 TYR A 218 3163 2761 3510 378 -1036 -19 C ATOM 388 CE1 TYR A 218 38.563 -0.469 20.563 1.00 34.17 C ANISOU 388 CE1 TYR A 218 4314 3839 4828 460 -1129 -89 C ATOM 389 CE2 TYR A 218 37.315 -0.423 22.612 1.00 27.96 C ANISOU 389 CE2 TYR A 218 3564 3101 3960 384 -1102 43 C ATOM 390 CZ TYR A 218 37.610 -1.019 21.403 1.00 35.93 C ANISOU 390 CZ TYR A 218 4560 4055 5035 423 -1150 6 C ATOM 391 OH TYR A 218 36.949 -2.165 21.027 1.00 36.86 O ANISOU 391 OH TYR A 218 4693 4111 5200 422 -1219 67 O ATOM 392 N GLN A 219 37.629 5.065 22.247 1.00 20.30 N ANISOU 392 N GLN A 219 2587 2294 2833 355 -702 -174 N ATOM 393 CA GLN A 219 36.265 5.595 22.106 1.00 19.82 C ANISOU 393 CA GLN A 219 2531 2229 2770 343 -613 -124 C ATOM 394 C GLN A 219 36.032 6.162 20.711 1.00 19.73 C ANISOU 394 C GLN A 219 2488 2199 2807 365 -567 -168 C ATOM 395 O GLN A 219 34.999 5.909 20.092 1.00 19.04 O ANISOU 395 O GLN A 219 2385 2086 2763 367 -553 -115 O ATOM 396 CB GLN A 219 35.963 6.650 23.173 1.00 20.54 C ANISOU 396 CB GLN A 219 2661 2363 2779 313 -518 -116 C ATOM 397 CG GLN A 219 35.897 6.065 24.585 1.00 26.91 C ANISOU 397 CG GLN A 219 3503 3187 3533 283 -555 -55 C ATOM 398 CD GLN A 219 35.738 7.133 25.633 1.00 22.94 C ANISOU 398 CD GLN A 219 3052 2725 2940 254 -460 -59 C ATOM 399 OE1 GLN A 219 36.329 8.195 25.524 1.00 21.34 O ANISOU 399 OE1 GLN A 219 2866 2541 2701 251 -404 -133 O ATOM 400 NE2 GLN A 219 34.918 6.869 26.640 1.00 25.55 N ANISOU 400 NE2 GLN A 219 3411 3067 3230 230 -438 21 N ATOM 401 N LYS A 220 36.996 6.921 20.210 1.00 19.73 N ANISOU 401 N LYS A 220 2480 2217 2801 379 -545 -259 N ATOM 402 CA LYS A 220 36.900 7.421 18.842 1.00 20.16 C ANISOU 402 CA LYS A 220 2504 2255 2902 399 -509 -305 C ATOM 403 C LYS A 220 36.829 6.259 17.845 1.00 19.23 C ANISOU 403 C LYS A 220 2361 2087 2857 423 -593 -292 C ATOM 404 O LYS A 220 36.006 6.265 16.917 1.00 18.73 O ANISOU 404 O LYS A 220 2283 1998 2837 425 -572 -269 O ATOM 405 CB LYS A 220 38.102 8.310 18.507 1.00 18.10 C ANISOU 405 CB LYS A 220 2235 2022 2620 408 -487 -405 C ATOM 406 CG LYS A 220 38.235 9.605 19.354 1.00 19.08 C ANISOU 406 CG LYS A 220 2394 2189 2667 380 -399 -431 C ATOM 407 CD LYS A 220 39.380 10.491 18.792 1.00 25.54 C ANISOU 407 CD LYS A 220 3199 3032 3473 385 -382 -528 C ATOM 408 CE LYS A 220 39.692 11.694 19.686 1.00 36.89 C ANISOU 408 CE LYS A 220 4681 4507 4827 350 -312 -559 C ATOM 409 NZ LYS A 220 40.649 12.638 19.012 1.00 39.14 N ANISOU 409 NZ LYS A 220 4953 4814 5104 350 -288 -646 N ATOM 410 N PHE A 221 37.707 5.276 18.032 1.00 19.59 N ANISOU 410 N PHE A 221 2408 2120 2917 440 -689 -305 N ATOM 411 CA PHE A 221 37.761 4.111 17.147 1.00 23.00 C ANISOU 411 CA PHE A 221 2829 2497 3413 466 -772 -299 C ATOM 412 C PHE A 221 36.392 3.437 17.022 1.00 22.01 C ANISOU 412 C PHE A 221 2714 2333 3316 445 -787 -206 C ATOM 413 O PHE A 221 35.941 3.098 15.915 1.00 22.69 O ANISOU 413 O PHE A 221 2792 2378 3450 451 -803 -202 O ATOM 414 CB PHE A 221 38.777 3.108 17.677 1.00 22.04 C ANISOU 414 CB PHE A 221 2713 2365 3295 487 -868 -306 C ATOM 415 CG PHE A 221 39.055 1.963 16.736 1.00 24.41 C ANISOU 415 CG PHE A 221 3011 2605 3659 524 -950 -317 C ATOM 416 CD1 PHE A 221 39.992 2.094 15.721 1.00 25.67 C ANISOU 416 CD1 PHE A 221 3149 2758 3848 564 -954 -400 C ATOM 417 CD2 PHE A 221 38.390 0.753 16.878 1.00 24.62 C ANISOU 417 CD2 PHE A 221 3061 2580 3714 517 -1021 -243 C ATOM 418 CE1 PHE A 221 40.278 1.037 14.869 1.00 33.15 C ANISOU 418 CE1 PHE A 221 4103 3645 4848 602 -1023 -413 C ATOM 419 CE2 PHE A 221 38.656 -0.316 16.014 1.00 30.69 C ANISOU 419 CE2 PHE A 221 3840 3283 4537 551 -1095 -255 C ATOM 420 CZ PHE A 221 39.607 -0.170 15.011 1.00 32.32 C ANISOU 420 CZ PHE A 221 4030 3481 4769 596 -1093 -343 C ATOM 421 N GLN A 222 35.739 3.240 18.167 1.00 19.02 N ANISOU 421 N GLN A 222 2353 1969 2904 416 -783 -128 N ATOM 422 CA GLN A 222 34.426 2.613 18.220 1.00 21.54 C ANISOU 422 CA GLN A 222 2677 2262 3244 390 -797 -27 C ATOM 423 C GLN A 222 33.375 3.460 17.537 1.00 22.19 C ANISOU 423 C GLN A 222 2739 2352 3339 377 -710 -3 C ATOM 424 O GLN A 222 32.541 2.938 16.793 1.00 20.78 O ANISOU 424 O GLN A 222 2553 2138 3206 364 -736 50 O ATOM 425 CB GLN A 222 34.000 2.367 19.673 1.00 19.99 C ANISOU 425 CB GLN A 222 2501 2092 3001 362 -799 50 C ATOM 426 CG GLN A 222 34.867 1.341 20.403 1.00 21.00 C ANISOU 426 CG GLN A 222 2648 2207 3123 369 -900 50 C ATOM 427 CD GLN A 222 34.460 1.208 21.850 1.00 26.68 C ANISOU 427 CD GLN A 222 3389 2958 3788 336 -895 123 C ATOM 428 OE1 GLN A 222 34.591 2.151 22.625 1.00 22.85 O ANISOU 428 OE1 GLN A 222 2916 2524 3243 323 -822 106 O ATOM 429 NE2 GLN A 222 33.954 0.037 22.222 1.00 24.79 N ANISOU 429 NE2 GLN A 222 3162 2689 3568 320 -973 206 N ATOM 430 N LEU A 223 33.393 4.761 17.810 1.00 21.23 N ANISOU 430 N LEU A 223 2613 2276 3177 376 -607 -36 N ATOM 431 CA LEU A 223 32.469 5.685 17.141 1.00 19.00 C ANISOU 431 CA LEU A 223 2308 2002 2909 369 -516 -17 C ATOM 432 C LEU A 223 32.683 5.661 15.619 1.00 20.16 C ANISOU 432 C LEU A 223 2434 2117 3110 384 -538 -69 C ATOM 433 O LEU A 223 31.719 5.658 14.849 1.00 19.49 O ANISOU 433 O LEU A 223 2329 2014 3062 370 -522 -18 O ATOM 434 CB LEU A 223 32.673 7.114 17.663 1.00 18.75 C ANISOU 434 CB LEU A 223 2285 2017 2822 372 -405 -62 C ATOM 435 CG LEU A 223 32.110 7.410 19.052 1.00 22.09 C ANISOU 435 CG LEU A 223 2735 2473 3187 354 -348 0 C ATOM 436 CD1 LEU A 223 32.803 8.648 19.666 1.00 21.32 C ANISOU 436 CD1 LEU A 223 2666 2413 3022 356 -267 -74 C ATOM 437 CD2 LEU A 223 30.598 7.603 18.944 1.00 19.61 C ANISOU 437 CD2 LEU A 223 2398 2159 2892 343 -283 100 C ATOM 438 N PHE A 224 33.942 5.660 15.186 1.00 19.41 N ANISOU 438 N PHE A 224 2340 2017 3017 410 -572 -166 N ATOM 439 CA PHE A 224 34.238 5.603 13.753 1.00 21.27 C ANISOU 439 CA PHE A 224 2560 2223 3299 426 -592 -221 C ATOM 440 C PHE A 224 33.630 4.339 13.113 1.00 21.32 C ANISOU 440 C PHE A 224 2575 2171 3354 416 -677 -163 C ATOM 441 O PHE A 224 33.041 4.384 12.017 1.00 22.85 O ANISOU 441 O PHE A 224 2758 2341 3584 405 -672 -152 O ATOM 442 CB PHE A 224 35.742 5.650 13.474 1.00 18.61 C ANISOU 442 CB PHE A 224 2221 1892 2956 460 -622 -327 C ATOM 443 CG PHE A 224 36.435 6.908 13.947 1.00 20.08 C ANISOU 443 CG PHE A 224 2402 2132 3094 463 -547 -389 C ATOM 444 CD1 PHE A 224 35.735 8.098 14.113 1.00 24.00 C ANISOU 444 CD1 PHE A 224 2896 2658 3565 444 -446 -374 C ATOM 445 CD2 PHE A 224 37.807 6.894 14.195 1.00 23.75 C ANISOU 445 CD2 PHE A 224 2866 2618 3541 484 -581 -462 C ATOM 446 CE1 PHE A 224 36.380 9.245 14.542 1.00 22.02 C ANISOU 446 CE1 PHE A 224 2651 2450 3266 442 -380 -433 C ATOM 447 CE2 PHE A 224 38.472 8.041 14.622 1.00 18.08 C ANISOU 447 CE2 PHE A 224 2146 1948 2774 478 -520 -517 C ATOM 448 CZ PHE A 224 37.758 9.215 14.800 1.00 20.77 C ANISOU 448 CZ PHE A 224 2495 2312 3085 455 -421 -505 C ATOM 449 N GLU A 225 33.778 3.213 13.804 1.00 21.77 N ANISOU 449 N GLU A 225 2656 2205 3412 416 -759 -126 N ATOM 450 CA GLU A 225 33.307 1.925 13.296 1.00 21.82 C ANISOU 450 CA GLU A 225 2682 2149 3459 404 -851 -74 C ATOM 451 C GLU A 225 31.787 1.868 13.277 1.00 25.15 C ANISOU 451 C GLU A 225 3095 2567 3893 358 -833 38 C ATOM 452 O GLU A 225 31.173 1.375 12.321 1.00 25.04 O ANISOU 452 O GLU A 225 3086 2511 3917 337 -871 71 O ATOM 453 CB GLU A 225 33.801 0.789 14.192 1.00 33.74 C ANISOU 453 CB GLU A 225 4220 3637 4963 414 -939 -52 C ATOM 454 CG GLU A 225 35.186 0.273 13.905 1.00 56.03 C ANISOU 454 CG GLU A 225 7055 6436 7797 462 -997 -139 C ATOM 455 CD GLU A 225 35.506 -0.970 14.734 1.00 80.90 C ANISOU 455 CD GLU A 225 10234 9555 10950 469 -1092 -99 C ATOM 456 OE1 GLU A 225 35.411 -0.902 15.983 1.00 84.33 O ANISOU 456 OE1 GLU A 225 10667 10026 11348 452 -1086 -54 O ATOM 457 OE2 GLU A 225 35.842 -2.019 14.137 1.00 88.59 O ANISOU 457 OE2 GLU A 225 11235 10464 11960 492 -1171 -112 O ATOM 458 N GLN A 226 31.177 2.350 14.351 1.00 21.51 N ANISOU 458 N GLN A 226 2622 2151 3399 341 -776 100 N ATOM 459 CA GLN A 226 29.741 2.148 14.558 1.00 20.90 C ANISOU 459 CA GLN A 226 2533 2077 3332 299 -765 224 C ATOM 460 C GLN A 226 28.851 3.211 13.903 1.00 20.05 C ANISOU 460 C GLN A 226 2387 1995 3237 286 -671 252 C ATOM 461 O GLN A 226 27.705 2.935 13.568 1.00 22.35 O ANISOU 461 O GLN A 226 2660 2276 3555 250 -679 349 O ATOM 462 CB GLN A 226 29.434 2.058 16.056 1.00 23.04 C ANISOU 462 CB GLN A 226 2810 2384 3561 288 -748 290 C ATOM 463 CG GLN A 226 30.088 0.819 16.706 1.00 24.88 C ANISOU 463 CG GLN A 226 3079 2586 3789 291 -855 292 C ATOM 464 CD GLN A 226 29.727 0.655 18.171 1.00 26.34 C ANISOU 464 CD GLN A 226 3272 2806 3931 272 -846 365 C ATOM 465 OE1 GLN A 226 28.588 0.874 18.563 1.00 29.76 O ANISOU 465 OE1 GLN A 226 3688 3265 4356 244 -797 460 O ATOM 466 NE2 GLN A 226 30.700 0.256 18.984 1.00 28.82 N ANISOU 466 NE2 GLN A 226 3611 3123 4217 288 -893 326 N ATOM 467 N VAL A 227 29.379 4.416 13.727 1.00 19.63 N ANISOU 467 N VAL A 227 2320 1975 3165 312 -585 172 N ATOM 468 CA VAL A 227 28.571 5.528 13.214 1.00 21.65 C ANISOU 468 CA VAL A 227 2540 2257 3430 305 -486 198 C ATOM 469 C VAL A 227 28.863 5.803 11.738 1.00 22.19 C ANISOU 469 C VAL A 227 2596 2300 3534 309 -494 134 C ATOM 470 O VAL A 227 27.943 6.050 10.947 1.00 24.05 O ANISOU 470 O VAL A 227 2803 2531 3802 285 -471 191 O ATOM 471 CB VAL A 227 28.756 6.835 14.061 1.00 17.67 C ANISOU 471 CB VAL A 227 2032 1805 2876 326 -369 166 C ATOM 472 CG1 VAL A 227 27.990 8.023 13.420 1.00 17.78 C ANISOU 472 CG1 VAL A 227 2010 1838 2905 326 -265 187 C ATOM 473 CG2 VAL A 227 28.264 6.616 15.485 1.00 21.17 C ANISOU 473 CG2 VAL A 227 2490 2274 3281 317 -351 243 C ATOM 474 N ILE A 228 30.135 5.756 11.353 1.00 20.40 N ANISOU 474 N ILE A 228 2388 2060 3302 337 -526 21 N ATOM 475 CA ILE A 228 30.484 6.060 9.973 1.00 21.20 C ANISOU 475 CA ILE A 228 2480 2142 3431 343 -527 -45 C ATOM 476 C ILE A 228 31.281 4.947 9.294 1.00 23.63 C ANISOU 476 C ILE A 228 2820 2399 3761 355 -630 -100 C ATOM 477 O ILE A 228 31.900 5.169 8.258 1.00 29.88 O ANISOU 477 O ILE A 228 3611 3176 4565 370 -632 -179 O ATOM 478 CB ILE A 228 31.236 7.404 9.861 1.00 23.00 C ANISOU 478 CB ILE A 228 2695 2411 3635 370 -439 -138 C ATOM 479 CG1 ILE A 228 32.566 7.363 10.644 1.00 22.20 C ANISOU 479 CG1 ILE A 228 2614 2325 3495 401 -456 -222 C ATOM 480 CG2 ILE A 228 30.320 8.524 10.332 1.00 18.31 C ANISOU 480 CG2 ILE A 228 2076 1856 3026 360 -330 -81 C ATOM 481 CD1 ILE A 228 33.490 8.558 10.321 1.00 22.11 C ANISOU 481 CD1 ILE A 228 2592 2347 3463 422 -390 -324 C ATOM 482 N GLY A 229 31.224 3.749 9.868 1.00 19.11 N ANISOU 482 N GLY A 229 2276 1795 3191 348 -713 -55 N ATOM 483 CA GLY A 229 32.086 2.650 9.457 1.00 22.42 C ANISOU 483 CA GLY A 229 2732 2160 3625 370 -808 -108 C ATOM 484 C GLY A 229 31.429 1.640 8.532 1.00 27.10 C ANISOU 484 C GLY A 229 3355 2689 4254 339 -886 -60 C ATOM 485 O GLY A 229 32.099 0.978 7.732 1.00 27.66 O ANISOU 485 O GLY A 229 3460 2710 4341 358 -945 -122 O ATOM 486 N ARG A 230 30.121 1.487 8.656 1.00 21.05 N ANISOU 486 N ARG A 230 2721 2002 3276 354 -881 -226 N ATOM 487 CA ARG A 230 29.419 0.547 7.785 1.00 26.98 C ANISOU 487 CA ARG A 230 3559 2630 4063 370 -1019 -233 C ATOM 488 C ARG A 230 28.303 1.264 7.053 1.00 27.57 C ANISOU 488 C ARG A 230 3645 2696 4135 308 -996 -192 C ATOM 489 O ARG A 230 27.584 2.078 7.637 1.00 23.71 O ANISOU 489 O ARG A 230 3094 2259 3657 231 -926 -106 O ATOM 490 CB ARG A 230 28.896 -0.654 8.571 1.00 36.76 C ANISOU 490 CB ARG A 230 4820 3763 5383 331 -1167 -149 C ATOM 491 CG ARG A 230 27.683 -0.353 9.431 1.00 49.27 C ANISOU 491 CG ARG A 230 6343 5359 7021 210 -1162 1 C ATOM 492 CD ARG A 230 27.292 -1.547 10.296 1.00 57.48 C ANISOU 492 CD ARG A 230 7394 6313 8132 158 -1310 95 C ATOM 493 NE ARG A 230 27.839 -1.450 11.641 1.00 53.27 N ANISOU 493 NE ARG A 230 6792 5843 7606 142 -1250 127 N ATOM 494 CZ ARG A 230 29.108 -1.688 11.941 1.00 60.63 C ANISOU 494 CZ ARG A 230 7732 6787 8516 217 -1233 36 C ATOM 495 NH1 ARG A 230 29.956 -2.044 10.984 1.00 61.69 N ANISOU 495 NH1 ARG A 230 7931 6893 8614 326 -1263 -92 N ATOM 496 NH2 ARG A 230 29.523 -1.584 13.197 1.00 62.92 N ANISOU 496 NH2 ARG A 230 7966 7123 8818 189 -1186 77 N ATOM 497 N LYS A 231 28.173 0.955 5.769 1.00 26.05 N ANISOU 497 N LYS A 231 3538 2435 3923 352 -1058 -258 N ATOM 498 CA LYS A 231 27.271 1.667 4.878 1.00 26.96 C ANISOU 498 CA LYS A 231 3677 2539 4027 304 -1037 -242 C ATOM 499 C LYS A 231 25.821 1.693 5.354 1.00 26.42 C ANISOU 499 C LYS A 231 3576 2430 4032 196 -1087 -98 C ATOM 500 O LYS A 231 25.206 2.751 5.345 1.00 24.04 O ANISOU 500 O LYS A 231 3227 2192 3716 145 -998 -58 O ATOM 501 CB LYS A 231 27.340 1.059 3.482 1.00 31.84 C ANISOU 501 CB LYS A 231 4414 3062 4620 372 -1129 -328 C ATOM 502 CG LYS A 231 26.681 1.869 2.384 1.00 40.57 C ANISOU 502 CG LYS A 231 5555 4161 5698 337 -1094 -342 C ATOM 503 CD LYS A 231 27.044 1.235 1.048 1.00 44.40 C ANISOU 503 CD LYS A 231 6168 4563 6137 430 -1174 -448 C ATOM 504 CE LYS A 231 26.645 2.096 -0.113 1.00 48.89 C ANISOU 504 CE LYS A 231 6777 5137 6661 405 -1125 -485 C ATOM 505 NZ LYS A 231 25.170 2.181 -0.231 1.00 57.78 N ANISOU 505 NZ LYS A 231 7921 6171 7864 298 -1202 -376 N ATOM 506 N ASP A 232 25.261 0.543 5.727 1.00 27.31 N ANISOU 506 N ASP A 232 3716 2444 4216 162 -1236 -16 N ATOM 507 CA ASP A 232 23.831 0.515 6.090 1.00 31.15 C ANISOU 507 CA ASP A 232 4159 2909 4769 53 -1292 140 C ATOM 508 C ASP A 232 23.546 1.362 7.310 1.00 25.94 C ANISOU 508 C ASP A 232 3371 2378 4107 6 -1165 226 C ATOM 509 O ASP A 232 22.605 2.156 7.306 1.00 25.36 O ANISOU 509 O ASP A 232 3242 2359 4034 -42 -1109 299 O ATOM 510 CB ASP A 232 23.305 -0.894 6.366 1.00 44.09 C ANISOU 510 CB ASP A 232 5846 4428 6480 4 -1492 236 C ATOM 511 CG ASP A 232 23.588 -1.856 5.250 1.00 64.21 C ANISOU 511 CG ASP A 232 8549 6826 9021 64 -1647 154 C ATOM 512 OD1 ASP A 232 23.393 -1.480 4.074 1.00 65.31 O ANISOU 512 OD1 ASP A 232 8753 6930 9131 89 -1640 95 O ATOM 513 OD2 ASP A 232 23.992 -2.999 5.564 1.00 71.20 O ANISOU 513 OD2 ASP A 232 9502 7624 9925 90 -1786 149 O ATOM 514 N ASP A 233 24.341 1.187 8.363 1.00 22.15 N ANISOU 514 N ASP A 233 2851 1945 3620 28 -1126 217 N ATOM 515 CA ASP A 233 24.127 1.972 9.586 1.00 26.26 C ANISOU 515 CA ASP A 233 3270 2581 4128 -4 -1009 295 C ATOM 516 C ASP A 233 24.400 3.467 9.368 1.00 27.74 C ANISOU 516 C ASP A 233 3437 2866 4236 28 -849 232 C ATOM 517 O ASP A 233 23.691 4.319 9.910 1.00 22.22 O ANISOU 517 O ASP A 233 2680 2245 3519 3 -771 307 O ATOM 518 CB ASP A 233 24.955 1.425 10.751 1.00 21.01 C ANISOU 518 CB ASP A 233 2581 1927 3473 8 -1014 299 C ATOM 519 CG ASP A 233 24.373 0.122 11.328 1.00 33.38 C ANISOU 519 CG ASP A 233 4147 3419 5116 -58 -1171 411 C ATOM 520 OD1 ASP A 233 23.293 -0.305 10.880 1.00 33.68 O ANISOU 520 OD1 ASP A 233 4194 3407 5196 -120 -1273 502 O ATOM 521 OD2 ASP A 233 24.995 -0.473 12.233 1.00 31.32 O ANISOU 521 OD2 ASP A 233 3881 3149 4871 -56 -1202 416 O ATOM 522 N PHE A 234 25.426 3.783 8.580 1.00 24.59 N ANISOU 522 N PHE A 234 3091 2468 3783 87 -808 99 N ATOM 523 CA PHE A 234 25.707 5.175 8.224 1.00 20.71 C ANISOU 523 CA PHE A 234 2599 2059 3211 101 -685 41 C ATOM 524 C PHE A 234 24.493 5.826 7.559 1.00 23.43 C ANISOU 524 C PHE A 234 2950 2398 3556 65 -681 83 C ATOM 525 O PHE A 234 24.115 6.952 7.898 1.00 19.65 O ANISOU 525 O PHE A 234 2444 1991 3030 55 -595 111 O ATOM 526 CB PHE A 234 26.903 5.261 7.288 1.00 19.02 C ANISOU 526 CB PHE A 234 2436 1852 2939 158 -663 -94 C ATOM 527 CG PHE A 234 27.106 6.618 6.693 1.00 19.20 C ANISOU 527 CG PHE A 234 2471 1946 2876 151 -567 -146 C ATOM 528 CD1 PHE A 234 27.602 7.665 7.466 1.00 17.91 C ANISOU 528 CD1 PHE A 234 2280 1876 2652 139 -472 -137 C ATOM 529 CD2 PHE A 234 26.774 6.858 5.365 1.00 25.14 C ANISOU 529 CD2 PHE A 234 3280 2665 3608 150 -585 -200 C ATOM 530 CE1 PHE A 234 27.806 8.943 6.906 1.00 21.29 C ANISOU 530 CE1 PHE A 234 2737 2362 2991 122 -406 -180 C ATOM 531 CE2 PHE A 234 26.953 8.117 4.801 1.00 20.26 C ANISOU 531 CE2 PHE A 234 2682 2109 2906 132 -510 -246 C ATOM 532 CZ PHE A 234 27.469 9.166 5.569 1.00 24.84 C ANISOU 532 CZ PHE A 234 3235 2782 3421 115 -425 -235 C ATOM 533 N LEU A 235 23.890 5.120 6.607 1.00 21.56 N ANISOU 533 N LEU A 235 2758 2068 3367 49 -785 87 N ATOM 534 CA LEU A 235 22.710 5.637 5.904 1.00 19.98 C ANISOU 534 CA LEU A 235 2563 1850 3177 10 -798 132 C ATOM 535 C LEU A 235 21.499 5.735 6.821 1.00 25.11 C ANISOU 535 C LEU A 235 3124 2546 3869 -37 -798 285 C ATOM 536 O LEU A 235 20.726 6.698 6.748 1.00 24.75 O ANISOU 536 O LEU A 235 3050 2556 3798 -45 -740 321 O ATOM 537 CB LEU A 235 22.358 4.747 4.697 1.00 21.15 C ANISOU 537 CB LEU A 235 2795 1872 3371 0 -929 112 C ATOM 538 CG LEU A 235 23.394 4.783 3.567 1.00 34.55 C ANISOU 538 CG LEU A 235 4584 3536 5008 61 -919 -41 C ATOM 539 CD1 LEU A 235 22.984 3.863 2.406 1.00 41.81 C ANISOU 539 CD1 LEU A 235 5608 4316 5964 62 -1061 -57 C ATOM 540 CD2 LEU A 235 23.608 6.209 3.076 1.00 37.83 C ANISOU 540 CD2 LEU A 235 5001 4031 5341 62 -800 -108 C ATOM 541 N LYS A 236 21.329 4.734 7.675 1.00 23.20 N ANISOU 541 N LYS A 236 2839 2289 3686 -65 -867 376 N ATOM 542 CA LYS A 236 20.207 4.729 8.601 1.00 26.32 C ANISOU 542 CA LYS A 236 3134 2752 4115 -112 -867 537 C ATOM 543 C LYS A 236 20.274 5.919 9.563 1.00 22.46 C ANISOU 543 C LYS A 236 2587 2393 3554 -69 -717 546 C ATOM 544 O LYS A 236 19.265 6.560 9.841 1.00 23.25 O ANISOU 544 O LYS A 236 2623 2571 3639 -70 -672 634 O ATOM 545 CB LYS A 236 20.188 3.432 9.391 1.00 26.22 C ANISOU 545 CB LYS A 236 3092 2703 4166 -158 -973 628 C ATOM 546 CG LYS A 236 18.967 3.256 10.269 1.00 40.85 C ANISOU 546 CG LYS A 236 4831 4636 6055 -222 -992 817 C ATOM 547 CD LYS A 236 18.884 1.817 10.784 1.00 58.42 C ANISOU 547 CD LYS A 236 7050 6797 8349 -295 -1143 915 C ATOM 548 CE LYS A 236 17.672 1.601 11.681 1.00 72.27 C ANISOU 548 CE LYS A 236 8674 8654 10132 -374 -1165 1123 C ATOM 549 NZ LYS A 236 17.778 2.361 12.961 1.00 77.49 N ANISOU 549 NZ LYS A 236 9246 9462 10734 -328 -1010 1154 N ATOM 550 N LEU A 237 21.461 6.222 10.072 1.00 19.73 N ANISOU 550 N LEU A 237 2269 2070 3157 -26 -648 459 N ATOM 551 CA LEU A 237 21.587 7.371 10.978 1.00 19.71 C ANISOU 551 CA LEU A 237 2243 2172 3075 17 -524 465 C ATOM 552 C LEU A 237 21.531 8.692 10.203 1.00 24.60 C ANISOU 552 C LEU A 237 2914 2814 3618 49 -458 388 C ATOM 553 O LEU A 237 20.957 9.680 10.674 1.00 21.24 O ANISOU 553 O LEU A 237 2472 2465 3134 84 -389 428 O ATOM 554 CB LEU A 237 22.878 7.277 11.804 1.00 19.16 C ANISOU 554 CB LEU A 237 2192 2110 2976 40 -486 411 C ATOM 555 CG LEU A 237 22.988 6.067 12.761 1.00 21.85 C ANISOU 555 CG LEU A 237 2488 2431 3383 9 -549 487 C ATOM 556 CD1 LEU A 237 24.186 6.246 13.697 1.00 26.92 C ANISOU 556 CD1 LEU A 237 3148 3096 3986 37 -494 441 C ATOM 557 CD2 LEU A 237 21.707 5.897 13.573 1.00 22.51 C ANISOU 557 CD2 LEU A 237 2483 2579 3491 -22 -555 646 C ATOM 558 N SER A 238 22.131 8.715 9.016 1.00 19.96 N ANISOU 558 N SER A 238 2398 2164 3023 44 -484 278 N ATOM 559 CA SER A 238 22.169 9.952 8.234 1.00 21.44 C ANISOU 559 CA SER A 238 2645 2369 3133 59 -435 201 C ATOM 560 C SER A 238 20.761 10.433 7.863 1.00 21.47 C ANISOU 560 C SER A 238 2627 2384 3148 54 -445 268 C ATOM 561 O SER A 238 20.517 11.640 7.768 1.00 20.08 O ANISOU 561 O SER A 238 2484 2249 2895 82 -392 243 O ATOM 562 CB SER A 238 23.027 9.785 6.985 1.00 22.13 C ANISOU 562 CB SER A 238 2804 2397 3209 49 -464 81 C ATOM 563 OG SER A 238 24.413 9.693 7.333 1.00 21.84 O ANISOU 563 OG SER A 238 2780 2385 3134 68 -432 15 O ATOM 564 N THR A 239 19.849 9.482 7.657 1.00 22.73 N ANISOU 564 N THR A 239 2734 2503 3398 16 -524 357 N ATOM 565 CA THR A 239 18.477 9.787 7.255 1.00 26.26 C ANISOU 565 CA THR A 239 3144 2965 3870 3 -547 438 C ATOM 566 C THR A 239 17.535 9.839 8.458 1.00 30.83 C ANISOU 566 C THR A 239 3609 3652 4453 23 -512 584 C ATOM 567 O THR A 239 16.309 9.850 8.304 1.00 27.65 O ANISOU 567 O THR A 239 3138 3284 4083 10 -538 689 O ATOM 568 CB THR A 239 17.925 8.752 6.231 1.00 23.79 C ANISOU 568 CB THR A 239 2842 2546 3651 -63 -673 471 C ATOM 569 OG1 THR A 239 18.012 7.435 6.783 1.00 26.85 O ANISOU 569 OG1 THR A 239 3192 2901 4110 -100 -751 546 O ATOM 570 CG2 THR A 239 18.728 8.799 4.924 1.00 28.87 C ANISOU 570 CG2 THR A 239 3604 3091 4275 -66 -702 324 C ATOM 571 N ASN A 240 18.107 9.863 9.655 1.00 28.86 N ANISOU 571 N ASN A 240 3335 3463 4165 57 -451 598 N ATOM 572 CA ASN A 240 17.300 9.859 10.869 1.00 25.60 C ANISOU 572 CA ASN A 240 2817 3166 3744 85 -410 737 C ATOM 573 C ASN A 240 17.230 11.239 11.503 1.00 24.00 C ANISOU 573 C ASN A 240 2638 3057 3424 185 -302 714 C ATOM 574 O ASN A 240 18.223 11.974 11.525 1.00 23.52 O ANISOU 574 O ASN A 240 2676 2971 3288 218 -259 600 O ATOM 575 CB ASN A 240 17.868 8.892 11.897 1.00 21.77 C ANISOU 575 CB ASN A 240 2294 2684 3293 56 -427 786 C ATOM 576 CG ASN A 240 16.995 8.804 13.135 1.00 28.40 C ANISOU 576 CG ASN A 240 3017 3653 4121 76 -387 943 C ATOM 577 OD1 ASN A 240 17.303 9.390 14.174 1.00 25.52 O ANISOU 577 OD1 ASN A 240 2655 3362 3679 143 -299 942 O ATOM 578 ND2 ASN A 240 15.878 8.099 13.015 1.00 24.09 N ANISOU 578 ND2 ASN A 240 2368 3140 3645 16 -456 1086 N ATOM 579 N ILE A 241 16.056 11.573 12.031 1.00 21.78 N ANISOU 579 N ILE A 241 2267 2890 3120 235 -266 830 N ATOM 580 CA ILE A 241 15.786 12.895 12.607 1.00 21.64 C ANISOU 580 CA ILE A 241 2280 2964 2978 356 -175 816 C ATOM 581 C ILE A 241 16.767 13.268 13.724 1.00 22.03 C ANISOU 581 C ILE A 241 2395 3031 2943 409 -112 773 C ATOM 582 O ILE A 241 17.171 14.433 13.851 1.00 26.47 O ANISOU 582 O ILE A 241 3069 3593 3394 486 -70 690 O ATOM 583 CB ILE A 241 14.309 12.980 13.111 1.00 31.38 C ANISOU 583 CB ILE A 241 3377 4344 4202 415 -144 971 C ATOM 584 CG1 ILE A 241 14.052 14.298 13.832 1.00 34.90 C ANISOU 584 CG1 ILE A 241 3867 4890 4502 571 -52 954 C ATOM 585 CG2 ILE A 241 13.982 11.796 14.023 1.00 31.19 C ANISOU 585 CG2 ILE A 241 3217 4392 4244 360 -159 1124 C ATOM 586 CD1 ILE A 241 12.571 14.560 14.106 1.00 41.89 C ANISOU 586 CD1 ILE A 241 4621 5934 5361 658 -16 1089 C ATOM 587 N PHE A 242 17.167 12.283 14.524 1.00 22.04 N ANISOU 587 N PHE A 242 2342 3036 2996 362 -121 831 N ATOM 588 CA PHE A 242 18.133 12.525 15.591 1.00 23.31 C ANISOU 588 CA PHE A 242 2566 3201 3091 399 -72 797 C ATOM 589 C PHE A 242 19.536 12.135 15.150 1.00 22.09 C ANISOU 589 C PHE A 242 2491 2927 2974 326 -114 684 C ATOM 590 O PHE A 242 20.493 12.883 15.371 1.00 27.02 O ANISOU 590 O PHE A 242 3220 3525 3520 355 -86 598 O ATOM 591 CB PHE A 242 17.772 11.728 16.846 1.00 27.18 C ANISOU 591 CB PHE A 242 2949 3774 3604 396 -53 931 C ATOM 592 CG PHE A 242 16.360 11.943 17.294 1.00 29.79 C ANISOU 592 CG PHE A 242 3166 4252 3900 464 -10 1067 C ATOM 593 CD1 PHE A 242 15.900 13.222 17.556 1.00 31.70 C ANISOU 593 CD1 PHE A 242 3455 4574 4015 603 65 1050 C ATOM 594 CD2 PHE A 242 15.492 10.876 17.430 1.00 32.88 C ANISOU 594 CD2 PHE A 242 3406 4708 4380 391 -52 1217 C ATOM 595 CE1 PHE A 242 14.587 13.434 17.959 1.00 36.28 C ANISOU 595 CE1 PHE A 242 3919 5312 4554 688 112 1177 C ATOM 596 CE2 PHE A 242 14.181 11.078 17.830 1.00 42.67 C ANISOU 596 CE2 PHE A 242 4519 6112 5583 453 -8 1358 C ATOM 597 CZ PHE A 242 13.732 12.359 18.094 1.00 40.52 C ANISOU 597 CZ PHE A 242 4281 5933 5181 610 82 1335 C ATOM 598 N GLY A 243 19.642 10.959 14.531 1.00 22.06 N ANISOU 598 N GLY A 243 2440 2857 3083 236 -191 690 N ATOM 599 CA GLY A 243 20.934 10.379 14.198 1.00 19.29 C ANISOU 599 CA GLY A 243 2145 2413 2772 184 -233 596 C ATOM 600 C GLY A 243 21.810 11.234 13.300 1.00 20.68 C ANISOU 600 C GLY A 243 2427 2541 2889 192 -220 458 C ATOM 601 O GLY A 243 23.047 11.152 13.362 1.00 19.03 O ANISOU 601 O GLY A 243 2267 2296 2667 177 -220 384 O ATOM 602 N ASN A 244 21.196 12.067 12.459 1.00 18.50 N ANISOU 602 N ASN A 244 2184 2271 2574 212 -213 429 N ATOM 603 CA ASN A 244 22.004 12.832 11.499 1.00 17.37 C ANISOU 603 CA ASN A 244 2141 2084 2374 200 -215 306 C ATOM 604 C ASN A 244 22.966 13.774 12.215 1.00 19.21 C ANISOU 604 C ASN A 244 2456 2341 2501 230 -169 263 C ATOM 605 O ASN A 244 24.049 14.067 11.710 1.00 19.60 O ANISOU 605 O ASN A 244 2568 2364 2516 196 -178 179 O ATOM 606 CB ASN A 244 21.131 13.592 10.489 1.00 18.95 C ANISOU 606 CB ASN A 244 2372 2278 2549 210 -226 283 C ATOM 607 CG ASN A 244 20.530 14.873 11.060 1.00 23.38 C ANISOU 607 CG ASN A 244 2976 2904 3005 290 -178 306 C ATOM 608 OD1 ASN A 244 21.169 15.940 11.047 1.00 22.82 O ANISOU 608 OD1 ASN A 244 3013 2827 2829 309 -165 236 O ATOM 609 ND2 ASN A 244 19.279 14.787 11.531 1.00 24.79 N ANISOU 609 ND2 ASN A 244 3072 3146 3199 341 -162 409 N ATOM 610 N TYR A 245 22.561 14.250 13.391 1.00 18.35 N ANISOU 610 N TYR A 245 2350 2289 2335 293 -126 330 N ATOM 611 CA TYR A 245 23.416 15.099 14.208 1.00 20.84 C ANISOU 611 CA TYR A 245 2758 2612 2546 323 -99 307 C ATOM 612 C TYR A 245 24.637 14.346 14.716 1.00 23.24 C ANISOU 612 C TYR A 245 3047 2891 2892 274 -107 295 C ATOM 613 O TYR A 245 25.750 14.885 14.726 1.00 19.66 O ANISOU 613 O TYR A 245 2671 2421 2379 249 -113 242 O ATOM 614 CB TYR A 245 22.639 15.670 15.406 1.00 20.93 C ANISOU 614 CB TYR A 245 2783 2687 2481 421 -54 385 C ATOM 615 CG TYR A 245 21.628 16.732 15.020 1.00 22.05 C ANISOU 615 CG TYR A 245 2974 2861 2542 498 -46 381 C ATOM 616 CD1 TYR A 245 22.004 18.061 14.893 1.00 28.06 C ANISOU 616 CD1 TYR A 245 3887 3599 3175 534 -63 316 C ATOM 617 CD2 TYR A 245 20.300 16.400 14.784 1.00 24.19 C ANISOU 617 CD2 TYR A 245 3141 3186 2863 532 -34 449 C ATOM 618 CE1 TYR A 245 21.086 19.041 14.538 1.00 25.95 C ANISOU 618 CE1 TYR A 245 3679 3353 2828 614 -69 305 C ATOM 619 CE2 TYR A 245 19.373 17.370 14.427 1.00 25.02 C ANISOU 619 CE2 TYR A 245 3286 3325 2895 613 -29 443 C ATOM 620 CZ TYR A 245 19.779 18.688 14.302 1.00 28.06 C ANISOU 620 CZ TYR A 245 3834 3678 3150 659 -47 364 C ATOM 621 OH TYR A 245 18.866 19.659 13.951 1.00 29.85 O ANISOU 621 OH TYR A 245 4114 3931 3298 750 -54 351 O ATOM 622 N LEU A 246 24.419 13.122 15.179 1.00 20.81 N ANISOU 622 N LEU A 246 2641 2582 2682 257 -116 354 N ATOM 623 CA LEU A 246 25.518 12.283 15.653 1.00 17.49 C ANISOU 623 CA LEU A 246 2202 2132 2313 216 -134 343 C ATOM 624 C LEU A 246 26.468 11.959 14.499 1.00 18.49 C ANISOU 624 C LEU A 246 2339 2217 2471 168 -171 247 C ATOM 625 O LEU A 246 27.683 11.939 14.674 1.00 18.39 O ANISOU 625 O LEU A 246 2349 2198 2441 148 -173 206 O ATOM 626 CB LEU A 246 24.971 10.972 16.242 1.00 18.05 C ANISOU 626 CB LEU A 246 2173 2202 2485 199 -159 426 C ATOM 627 CG LEU A 246 26.027 10.054 16.859 1.00 24.33 C ANISOU 627 CG LEU A 246 2953 2960 3333 165 -188 418 C ATOM 628 CD1 LEU A 246 26.842 10.769 17.936 1.00 19.77 C ANISOU 628 CD1 LEU A 246 2440 2396 2676 186 -147 421 C ATOM 629 CD2 LEU A 246 25.404 8.772 17.403 1.00 24.29 C ANISOU 629 CD2 LEU A 246 2861 2945 3421 136 -235 506 C ATOM 630 N VAL A 247 25.914 11.689 13.319 1.00 17.12 N ANISOU 630 N VAL A 247 2145 2021 2339 153 -200 216 N ATOM 631 CA VAL A 247 26.762 11.419 12.159 1.00 17.12 C ANISOU 631 CA VAL A 247 2161 1992 2352 124 -229 122 C ATOM 632 C VAL A 247 27.666 12.618 11.871 1.00 20.16 C ANISOU 632 C VAL A 247 2621 2410 2629 111 -201 62 C ATOM 633 O VAL A 247 28.876 12.466 11.657 1.00 16.92 O ANISOU 633 O VAL A 247 2211 2013 2204 90 -204 13 O ATOM 634 CB VAL A 247 25.938 11.084 10.914 1.00 18.65 C ANISOU 634 CB VAL A 247 2346 2149 2593 113 -269 100 C ATOM 635 CG1 VAL A 247 26.821 11.105 9.671 1.00 21.96 C ANISOU 635 CG1 VAL A 247 2801 2554 2990 96 -284 -4 C ATOM 636 CG2 VAL A 247 25.250 9.711 11.080 1.00 19.98 C ANISOU 636 CG2 VAL A 247 2446 2272 2872 104 -330 164 C ATOM 637 N GLN A 248 27.085 13.814 11.882 1.00 16.65 N ANISOU 637 N GLN A 248 2240 1983 2102 124 -182 73 N ATOM 638 CA GLN A 248 27.876 15.012 11.626 1.00 18.49 C ANISOU 638 CA GLN A 248 2563 2239 2222 97 -179 29 C ATOM 639 C GLN A 248 28.980 15.209 12.673 1.00 17.55 C ANISOU 639 C GLN A 248 2468 2140 2060 85 -172 53 C ATOM 640 O GLN A 248 30.112 15.592 12.335 1.00 17.75 O ANISOU 640 O GLN A 248 2520 2191 2032 36 -184 20 O ATOM 641 CB GLN A 248 26.959 16.241 11.560 1.00 16.63 C ANISOU 641 CB GLN A 248 2412 2004 1901 126 -180 39 C ATOM 642 CG GLN A 248 25.995 16.187 10.370 1.00 19.22 C ANISOU 642 CG GLN A 248 2725 2311 2265 124 -196 9 C ATOM 643 CD GLN A 248 25.052 17.372 10.362 1.00 26.27 C ANISOU 643 CD GLN A 248 3699 3207 3076 167 -201 18 C ATOM 644 OE1 GLN A 248 25.472 18.509 10.143 1.00 22.69 O ANISOU 644 OE1 GLN A 248 3355 2752 2512 148 -225 -19 O ATOM 645 NE2 GLN A 248 23.774 17.113 10.618 1.00 19.31 N ANISOU 645 NE2 GLN A 248 2763 2334 2239 225 -187 74 N ATOM 646 N SER A 249 28.652 14.975 13.945 1.00 16.32 N ANISOU 646 N SER A 249 2303 1978 1920 126 -154 121 N ATOM 647 CA SER A 249 29.643 15.096 15.018 1.00 18.93 C ANISOU 647 CA SER A 249 2664 2313 2217 114 -154 151 C ATOM 648 C SER A 249 30.784 14.119 14.828 1.00 17.60 C ANISOU 648 C SER A 249 2419 2150 2119 75 -165 123 C ATOM 649 O SER A 249 31.958 14.478 15.008 1.00 18.83 O ANISOU 649 O SER A 249 2600 2327 2226 34 -177 118 O ATOM 650 CB SER A 249 29.010 14.869 16.404 1.00 21.42 C ANISOU 650 CB SER A 249 2975 2619 2543 170 -130 229 C ATOM 651 OG SER A 249 28.126 15.923 16.713 1.00 28.97 O ANISOU 651 OG SER A 249 4017 3585 3406 229 -117 256 O ATOM 652 N VAL A 250 30.449 12.880 14.476 1.00 16.65 N ANISOU 652 N VAL A 250 2210 2012 2106 88 -172 109 N ATOM 653 CA VAL A 250 31.477 11.851 14.311 1.00 17.83 C ANISOU 653 CA VAL A 250 2293 2162 2319 77 -192 74 C ATOM 654 C VAL A 250 32.326 12.102 13.056 1.00 16.45 C ANISOU 654 C VAL A 250 2114 2031 2104 53 -195 0 C ATOM 655 O VAL A 250 33.539 11.899 13.057 1.00 18.35 O ANISOU 655 O VAL A 250 2323 2313 2334 40 -198 -20 O ATOM 656 CB VAL A 250 30.893 10.422 14.346 1.00 16.64 C ANISOU 656 CB VAL A 250 2073 1964 2285 102 -223 84 C ATOM 657 CG1 VAL A 250 31.997 9.396 14.011 1.00 17.34 C ANISOU 657 CG1 VAL A 250 2114 2050 2424 111 -256 29 C ATOM 658 CG2 VAL A 250 30.283 10.141 15.726 1.00 17.38 C ANISOU 658 CG2 VAL A 250 2157 2037 2410 111 -220 172 C ATOM 659 N ILE A 251 31.723 12.611 11.995 1.00 18.82 N ANISOU 659 N ILE A 251 2443 2334 2371 46 -194 -37 N ATOM 660 CA ILE A 251 32.549 13.028 10.852 1.00 16.62 C ANISOU 660 CA ILE A 251 2169 2114 2032 14 -192 -98 C ATOM 661 C ILE A 251 33.586 14.090 11.285 1.00 19.13 C ANISOU 661 C ILE A 251 2528 2493 2248 -43 -189 -69 C ATOM 662 O ILE A 251 34.751 14.038 10.889 1.00 19.20 O ANISOU 662 O ILE A 251 2494 2576 2226 -69 -187 -88 O ATOM 663 CB ILE A 251 31.680 13.549 9.692 1.00 19.99 C ANISOU 663 CB ILE A 251 2638 2525 2431 4 -197 -137 C ATOM 664 CG1 ILE A 251 30.948 12.366 9.020 1.00 17.75 C ANISOU 664 CG1 ILE A 251 2312 2185 2246 47 -219 -168 C ATOM 665 CG2 ILE A 251 32.536 14.329 8.705 1.00 19.75 C ANISOU 665 CG2 ILE A 251 2631 2568 2305 -49 -195 -180 C ATOM 666 CD1 ILE A 251 29.807 12.789 8.056 1.00 16.40 C ANISOU 666 CD1 ILE A 251 2186 1975 2070 38 -232 -187 C ATOM 667 N GLY A 252 33.164 15.047 12.102 1.00 18.15 N ANISOU 667 N GLY A 252 2489 2342 2065 -57 -196 -16 N ATOM 668 CA GLY A 252 34.064 16.086 12.589 1.00 18.61 C ANISOU 668 CA GLY A 252 2615 2436 2020 -118 -219 26 C ATOM 669 C GLY A 252 35.218 15.524 13.403 1.00 22.32 C ANISOU 669 C GLY A 252 3027 2933 2520 -130 -220 61 C ATOM 670 O GLY A 252 36.378 15.930 13.244 1.00 20.60 O ANISOU 670 O GLY A 252 2798 2784 2243 -194 -239 79 O ATOM 671 N ILE A 253 34.906 14.596 14.295 1.00 16.63 N ANISOU 671 N ILE A 253 2266 2162 1890 -77 -206 80 N ATOM 672 CA ILE A 253 35.941 13.943 15.094 1.00 16.92 C ANISOU 672 CA ILE A 253 2248 2212 1969 -82 -213 108 C ATOM 673 C ILE A 253 36.883 13.132 14.196 1.00 18.44 C ANISOU 673 C ILE A 253 2330 2477 2199 -75 -207 53 C ATOM 674 O ILE A 253 38.098 13.183 14.351 1.00 18.29 O ANISOU 674 O ILE A 253 2270 2525 2155 -108 -216 74 O ATOM 675 CB ILE A 253 35.307 13.051 16.166 1.00 18.60 C ANISOU 675 CB ILE A 253 2444 2352 2272 -30 -208 136 C ATOM 676 CG1 ILE A 253 34.467 13.926 17.112 1.00 19.21 C ANISOU 676 CG1 ILE A 253 2628 2381 2289 -20 -204 196 C ATOM 677 CG2 ILE A 253 36.385 12.308 16.944 1.00 18.81 C ANISOU 677 CG2 ILE A 253 2415 2381 2350 -36 -223 157 C ATOM 678 CD1 ILE A 253 33.484 13.125 18.004 1.00 20.47 C ANISOU 678 CD1 ILE A 253 2763 2488 2525 34 -188 232 C ATOM 679 N SER A 254 36.321 12.431 13.219 1.00 17.16 N ANISOU 679 N SER A 254 2125 2308 2087 -27 -196 -14 N ATOM 680 CA SER A 254 37.143 11.685 12.264 1.00 19.65 C ANISOU 680 CA SER A 254 2353 2694 2419 6 -191 -77 C ATOM 681 C SER A 254 38.152 12.596 11.549 1.00 19.75 C ANISOU 681 C SER A 254 2350 2831 2324 -56 -179 -72 C ATOM 682 O SER A 254 39.328 12.259 11.422 1.00 20.94 O ANISOU 682 O SER A 254 2418 3076 2462 -48 -173 -74 O ATOM 683 CB SER A 254 36.273 10.982 11.221 1.00 18.37 C ANISOU 683 CB SER A 254 2185 2491 2305 63 -194 -147 C ATOM 684 OG SER A 254 37.092 10.233 10.331 1.00 19.62 O ANISOU 684 OG SER A 254 2275 2716 2466 118 -192 -213 O ATOM 685 N LEU A 255 37.682 13.747 11.073 1.00 17.77 N ANISOU 685 N LEU A 255 2177 2585 1991 -118 -183 -62 N ATOM 686 CA LEU A 255 38.547 14.693 10.374 1.00 18.16 C ANISOU 686 CA LEU A 255 2223 2750 1928 -199 -188 -44 C ATOM 687 C LEU A 255 39.595 15.303 11.296 1.00 22.41 C ANISOU 687 C LEU A 255 2765 3337 2412 -275 -217 47 C ATOM 688 O LEU A 255 40.639 15.736 10.834 1.00 21.95 O ANISOU 688 O LEU A 255 2655 3405 2278 -341 -225 79 O ATOM 689 CB LEU A 255 37.721 15.815 9.740 1.00 19.16 C ANISOU 689 CB LEU A 255 2455 2848 1978 -255 -206 -51 C ATOM 690 CG LEU A 255 36.817 15.414 8.580 1.00 21.15 C ANISOU 690 CG LEU A 255 2706 3069 2262 -206 -186 -133 C ATOM 691 CD1 LEU A 255 35.777 16.518 8.318 1.00 25.22 C ANISOU 691 CD1 LEU A 255 3342 3520 2720 -250 -214 -131 C ATOM 692 CD2 LEU A 255 37.638 15.143 7.351 1.00 20.36 C ANISOU 692 CD2 LEU A 255 2525 3089 2121 -207 -163 -181 C ATOM 693 N ALA A 256 39.307 15.363 12.592 1.00 20.68 N ANISOU 693 N ALA A 256 2608 3023 2226 -271 -239 97 N ATOM 694 CA ALA A 256 40.257 15.925 13.564 1.00 19.39 C ANISOU 694 CA ALA A 256 2471 2882 2015 -345 -280 190 C ATOM 695 C ALA A 256 41.288 14.910 14.072 1.00 21.95 C ANISOU 695 C ALA A 256 2674 3255 2411 -312 -268 204 C ATOM 696 O ALA A 256 42.240 15.283 14.752 1.00 31.10 O ANISOU 696 O ALA A 256 3831 4450 3537 -379 -305 285 O ATOM 697 CB ALA A 256 39.501 16.535 14.746 1.00 26.08 C ANISOU 697 CB ALA A 256 3462 3601 2846 -348 -314 239 C ATOM 698 N THR A 257 41.106 13.635 13.734 1.00 22.03 N ANISOU 698 N THR A 257 2594 3260 2518 -210 -230 127 N ATOM 699 CA THR A 257 41.945 12.579 14.279 1.00 21.29 C ANISOU 699 CA THR A 257 2401 3189 2499 -158 -229 127 C ATOM 700 C THR A 257 42.904 12.014 13.233 1.00 23.09 C ANISOU 700 C THR A 257 2494 3568 2712 -111 -201 80 C ATOM 701 O THR A 257 42.556 11.117 12.465 1.00 24.63 O ANISOU 701 O THR A 257 2648 3759 2951 -12 -178 -10 O ATOM 702 CB THR A 257 41.090 11.457 14.892 1.00 25.56 C ANISOU 702 CB THR A 257 2954 3601 3156 -71 -230 84 C ATOM 703 OG1 THR A 257 40.150 12.038 15.805 1.00 24.35 O ANISOU 703 OG1 THR A 257 2917 3336 3000 -104 -243 131 O ATOM 704 CG2 THR A 257 41.967 10.441 15.617 1.00 23.24 C ANISOU 704 CG2 THR A 257 2583 3311 2937 -27 -248 89 C ATOM 705 N ASN A 258 44.130 12.530 13.249 1.00 22.76 N ANISOU 705 N ASN A 258 2385 3659 2603 -179 -210 151 N ATOM 706 CA ASN A 258 45.139 12.200 12.241 1.00 25.97 C ANISOU 706 CA ASN A 258 2650 4252 2965 -140 -175 128 C ATOM 707 C ASN A 258 45.994 10.981 12.539 1.00 27.38 C ANISOU 707 C ASN A 258 2708 4483 3213 -30 -167 100 C ATOM 708 O ASN A 258 47.229 11.041 12.456 1.00 30.63 O ANISOU 708 O ASN A 258 3000 5059 3580 -43 -161 154 O ATOM 709 CB ASN A 258 46.050 13.396 12.049 1.00 31.98 C ANISOU 709 CB ASN A 258 3382 5159 3608 -279 -195 236 C ATOM 710 CG ASN A 258 45.318 14.565 11.462 1.00 38.51 C ANISOU 710 CG ASN A 258 4323 5960 4348 -376 -211 248 C ATOM 711 OD1 ASN A 258 45.059 15.563 12.140 1.00 41.90 O ANISOU 711 OD1 ASN A 258 4876 6309 4736 -484 -269 324 O ATOM 712 ND2 ASN A 258 44.951 14.440 10.194 1.00 39.22 N ANISOU 712 ND2 ASN A 258 4388 6108 4407 -331 -168 169 N ATOM 713 N ASP A 259 45.348 9.884 12.898 1.00 22.14 N ANISOU 713 N ASP A 259 2074 3683 2653 77 -177 24 N ATOM 714 CA ASP A 259 46.059 8.626 13.053 1.00 23.24 C ANISOU 714 CA ASP A 259 2119 3855 2855 202 -184 -25 C ATOM 715 C ASP A 259 46.151 7.904 11.722 1.00 28.77 C ANISOU 715 C ASP A 259 2758 4647 3528 339 -151 -130 C ATOM 716 O ASP A 259 45.740 8.441 10.697 1.00 28.46 O ANISOU 716 O ASP A 259 2740 4654 3420 319 -118 -156 O ATOM 717 CB ASP A 259 45.412 7.746 14.126 1.00 25.44 C ANISOU 717 CB ASP A 259 2469 3944 3253 243 -233 -47 C ATOM 718 CG ASP A 259 43.967 7.393 13.820 1.00 37.45 C ANISOU 718 CG ASP A 259 4091 5319 4820 276 -243 -113 C ATOM 719 OD1 ASP A 259 43.512 7.539 12.664 1.00 38.42 O ANISOU 719 OD1 ASP A 259 4224 5476 4897 304 -215 -168 O ATOM 720 OD2 ASP A 259 43.280 6.958 14.764 1.00 46.37 O ANISOU 720 OD2 ASP A 259 5287 6301 6029 268 -282 -100 O ATOM 721 N ASP A 260 46.698 6.690 11.747 1.00 25.98 N ANISOU 721 N ASP A 260 2339 4310 3220 484 -168 -194 N ATOM 722 CA ASP A 260 46.936 5.919 10.537 1.00 31.16 C ANISOU 722 CA ASP A 260 2945 5059 3837 644 -145 -298 C ATOM 723 C ASP A 260 45.656 5.548 9.792 1.00 29.30 C ANISOU 723 C ASP A 260 2826 4684 3623 692 -162 -388 C ATOM 724 O ASP A 260 45.701 5.234 8.607 1.00 37.90 O ANISOU 724 O ASP A 260 3901 5845 4653 797 -138 -466 O ATOM 725 CB ASP A 260 47.726 4.648 10.860 1.00 31.41 C ANISOU 725 CB ASP A 260 2909 5109 3915 805 -181 -353 C ATOM 726 CG ASP A 260 48.341 4.030 9.630 1.00 43.81 C ANISOU 726 CG ASP A 260 4403 6836 5407 986 -148 -443 C ATOM 727 OD1 ASP A 260 49.203 4.690 9.007 1.00 49.80 O ANISOU 727 OD1 ASP A 260 5039 7822 6059 970 -77 -398 O ATOM 728 OD2 ASP A 260 47.958 2.891 9.281 1.00 42.96 O ANISOU 728 OD2 ASP A 260 4362 6627 5333 1143 -200 -554 O ATOM 729 N GLY A 261 44.522 5.589 10.482 1.00 24.10 N ANISOU 729 N GLY A 261 2281 3833 3044 618 -204 -370 N ATOM 730 CA GLY A 261 43.247 5.229 9.875 1.00 26.08 C ANISOU 730 CA GLY A 261 2637 3945 3326 647 -232 -434 C ATOM 731 C GLY A 261 42.550 6.371 9.140 1.00 26.71 C ANISOU 731 C GLY A 261 2763 4044 3341 546 -187 -414 C ATOM 732 O GLY A 261 41.512 6.173 8.502 1.00 23.82 O ANISOU 732 O GLY A 261 2478 3579 2993 565 -207 -462 O ATOM 733 N TYR A 262 43.125 7.567 9.226 1.00 23.85 N ANISOU 733 N TYR A 262 2356 3804 2903 435 -140 -338 N ATOM 734 CA TYR A 262 42.471 8.775 8.718 1.00 22.03 C ANISOU 734 CA TYR A 262 2186 3576 2608 320 -115 -308 C ATOM 735 C TYR A 262 42.050 8.604 7.266 1.00 22.38 C ANISOU 735 C TYR A 262 2251 3644 2607 383 -96 -393 C ATOM 736 O TYR A 262 40.885 8.764 6.922 1.00 26.52 O ANISOU 736 O TYR A 262 2870 4052 3156 358 -112 -417 O ATOM 737 CB TYR A 262 43.416 9.976 8.866 1.00 22.65 C ANISOU 737 CB TYR A 262 2207 3807 2590 200 -87 -214 C ATOM 738 CG TYR A 262 42.889 11.291 8.305 1.00 21.76 C ANISOU 738 CG TYR A 262 2166 3708 2394 76 -79 -180 C ATOM 739 CD1 TYR A 262 42.220 12.212 9.114 1.00 24.91 C ANISOU 739 CD1 TYR A 262 2669 3999 2795 -35 -111 -114 C ATOM 740 CD2 TYR A 262 43.077 11.615 6.965 1.00 26.62 C ANISOU 740 CD2 TYR A 262 2752 4444 2919 77 -45 -217 C ATOM 741 CE1 TYR A 262 41.757 13.429 8.596 1.00 26.94 C ANISOU 741 CE1 TYR A 262 3005 4263 2968 -139 -119 -89 C ATOM 742 CE2 TYR A 262 42.623 12.812 6.438 1.00 27.02 C ANISOU 742 CE2 TYR A 262 2874 4503 2890 -43 -51 -188 C ATOM 743 CZ TYR A 262 41.955 13.713 7.250 1.00 35.82 C ANISOU 743 CZ TYR A 262 4098 5501 4010 -149 -93 -127 C ATOM 744 OH TYR A 262 41.506 14.899 6.698 1.00 29.31 O ANISOU 744 OH TYR A 262 3359 4677 3101 -257 -112 -106 O ATOM 745 N THR A 263 43.012 8.296 6.411 1.00 28.20 N ANISOU 745 N THR A 263 2899 4543 3274 468 -60 -434 N ATOM 746 CA THR A 263 42.742 8.225 4.974 1.00 32.35 C ANISOU 746 CA THR A 263 3447 5111 3734 528 -37 -512 C ATOM 747 C THR A 263 41.621 7.255 4.634 1.00 30.05 C ANISOU 747 C THR A 263 3264 4632 3522 621 -91 -597 C ATOM 748 O THR A 263 40.712 7.588 3.878 1.00 30.16 O ANISOU 748 O THR A 263 3360 4576 3524 586 -97 -624 O ATOM 749 CB THR A 263 44.011 7.840 4.207 1.00 34.04 C ANISOU 749 CB THR A 263 3540 5539 3855 643 12 -546 C ATOM 750 OG1 THR A 263 45.014 8.834 4.449 1.00 36.10 O ANISOU 750 OG1 THR A 263 3692 5989 4035 528 54 -443 O ATOM 751 CG2 THR A 263 43.732 7.748 2.705 1.00 36.98 C ANISOU 751 CG2 THR A 263 3947 5955 4149 715 38 -629 C ATOM 752 N LYS A 264 41.693 6.048 5.190 1.00 26.45 N ANISOU 752 N LYS A 264 2813 4090 3145 733 -145 -633 N ATOM 753 CA LYS A 264 40.695 5.028 4.905 1.00 28.74 C ANISOU 753 CA LYS A 264 3212 4199 3508 815 -223 -700 C ATOM 754 C LYS A 264 39.305 5.426 5.393 1.00 29.01 C ANISOU 754 C LYS A 264 3335 4067 3620 694 -259 -649 C ATOM 755 O LYS A 264 38.316 5.189 4.698 1.00 26.09 O ANISOU 755 O LYS A 264 3053 3588 3271 704 -299 -683 O ATOM 756 CB LYS A 264 41.113 3.676 5.483 1.00 40.87 C ANISOU 756 CB LYS A 264 4744 5676 5107 949 -294 -741 C ATOM 757 CG LYS A 264 42.216 2.992 4.686 1.00 53.44 C ANISOU 757 CG LYS A 264 6283 7405 6619 1130 -278 -825 C ATOM 758 CD LYS A 264 42.589 1.641 5.281 1.00 66.04 C ANISOU 758 CD LYS A 264 7895 8923 8275 1270 -368 -872 C ATOM 759 CE LYS A 264 43.785 1.036 4.559 1.00 74.76 C ANISOU 759 CE LYS A 264 8934 10190 9283 1472 -344 -954 C ATOM 760 NZ LYS A 264 44.961 1.952 4.577 1.00 80.98 N ANISOU 760 NZ LYS A 264 9552 11231 9984 1431 -226 -895 N ATOM 761 N ARG A 265 39.219 6.049 6.567 1.00 22.41 N ANISOU 761 N ARG A 265 2478 3216 2821 583 -245 -561 N ATOM 762 CA ARG A 265 37.917 6.533 7.051 1.00 21.66 C ANISOU 762 CA ARG A 265 2456 2993 2781 481 -266 -506 C ATOM 763 C ARG A 265 37.290 7.577 6.112 1.00 22.32 C ANISOU 763 C ARG A 265 2584 3096 2801 410 -230 -509 C ATOM 764 O ARG A 265 36.086 7.557 5.851 1.00 24.19 O ANISOU 764 O ARG A 265 2892 3219 3080 386 -263 -509 O ATOM 765 CB ARG A 265 38.042 7.148 8.457 1.00 23.23 C ANISOU 765 CB ARG A 265 2632 3190 3002 389 -249 -414 C ATOM 766 CG ARG A 265 38.325 6.151 9.571 1.00 27.00 C ANISOU 766 CG ARG A 265 3088 3606 3564 433 -298 -396 C ATOM 767 CD ARG A 265 38.100 6.787 10.946 1.00 20.47 C ANISOU 767 CD ARG A 265 2271 2744 2762 337 -287 -302 C ATOM 768 NE ARG A 265 38.764 8.089 11.061 1.00 21.01 N ANISOU 768 NE ARG A 265 2320 2922 2742 255 -231 -253 N ATOM 769 CZ ARG A 265 40.006 8.253 11.509 1.00 19.89 C ANISOU 769 CZ ARG A 265 2112 2876 2567 245 -216 -224 C ATOM 770 NH1 ARG A 265 40.721 7.198 11.879 1.00 21.06 N ANISOU 770 NH1 ARG A 265 2205 3029 2768 323 -243 -249 N ATOM 771 NH2 ARG A 265 40.535 9.475 11.588 1.00 20.70 N ANISOU 771 NH2 ARG A 265 2212 3069 2585 152 -185 -165 N ATOM 772 N GLN A 266 38.098 8.500 5.608 1.00 24.97 N ANISOU 772 N GLN A 266 2876 3578 3033 367 -171 -505 N ATOM 773 CA GLN A 266 37.527 9.571 4.783 1.00 22.07 C ANISOU 773 CA GLN A 266 2560 3224 2600 284 -149 -504 C ATOM 774 C GLN A 266 37.161 9.053 3.395 1.00 25.75 C ANISOU 774 C GLN A 266 3067 3667 3049 357 -161 -590 C ATOM 775 O GLN A 266 36.196 9.517 2.779 1.00 24.86 O ANISOU 775 O GLN A 266 3028 3482 2933 309 -175 -599 O ATOM 776 CB GLN A 266 38.484 10.760 4.662 1.00 25.64 C ANISOU 776 CB GLN A 266 2964 3838 2939 194 -101 -459 C ATOM 777 CG GLN A 266 37.772 12.039 4.208 1.00 35.91 C ANISOU 777 CG GLN A 266 4343 5120 4180 79 -102 -436 C ATOM 778 CD GLN A 266 38.699 13.243 4.040 1.00 43.96 C ANISOU 778 CD GLN A 266 5333 6292 5077 -31 -81 -381 C ATOM 779 OE1 GLN A 266 38.265 14.398 4.160 1.00 23.19 O ANISOU 779 OE1 GLN A 266 2779 3636 2398 -139 -104 -336 O ATOM 780 NE2 GLN A 266 39.978 12.980 3.756 1.00 48.91 N ANISOU 780 NE2 GLN A 266 5852 7084 5646 -2 -48 -377 N ATOM 781 N GLU A 267 37.942 8.100 2.905 1.00 26.16 N ANISOU 781 N GLU A 267 3079 3778 3084 482 -162 -653 N ATOM 782 CA GLU A 267 37.661 7.492 1.612 1.00 34.20 C ANISOU 782 CA GLU A 267 4154 4763 4076 575 -183 -741 C ATOM 783 C GLU A 267 36.354 6.714 1.692 1.00 34.03 C ANISOU 783 C GLU A 267 4235 4533 4163 595 -272 -752 C ATOM 784 O GLU A 267 35.525 6.776 0.782 1.00 30.32 O ANISOU 784 O GLU A 267 3847 3984 3690 585 -300 -783 O ATOM 785 CB GLU A 267 38.808 6.574 1.183 1.00 30.42 C ANISOU 785 CB GLU A 267 3618 4394 3546 733 -171 -808 C ATOM 786 CG GLU A 267 38.537 5.803 -0.105 1.00 40.06 C ANISOU 786 CG GLU A 267 4922 5565 4733 860 -207 -907 C ATOM 787 CD GLU A 267 38.690 6.664 -1.352 1.00 46.73 C ANISOU 787 CD GLU A 267 5769 6526 5460 823 -144 -932 C ATOM 788 OE1 GLU A 267 39.074 7.850 -1.226 1.00 57.16 O ANISOU 788 OE1 GLU A 267 7020 7976 6721 694 -78 -869 O ATOM 789 OE2 GLU A 267 38.436 6.150 -2.461 1.00 49.11 O ANISOU 789 OE2 GLU A 267 6152 6785 5723 919 -170 -1010 O ATOM 790 N LYS A 268 36.181 5.983 2.791 1.00 26.62 N ANISOU 790 N LYS A 268 3290 3508 3318 615 -323 -718 N ATOM 791 CA LYS A 268 34.953 5.243 3.066 1.00 29.26 C ANISOU 791 CA LYS A 268 3704 3657 3758 610 -418 -697 C ATOM 792 C LYS A 268 33.753 6.181 3.057 1.00 30.63 C ANISOU 792 C LYS A 268 3914 3771 3952 486 -408 -639 C ATOM 793 O LYS A 268 32.729 5.908 2.432 1.00 25.97 O ANISOU 793 O LYS A 268 3399 3068 3399 480 -468 -645 O ATOM 794 CB LYS A 268 35.055 4.625 4.450 1.00 35.60 C ANISOU 794 CB LYS A 268 4471 4413 4643 610 -456 -644 C ATOM 795 CG LYS A 268 34.632 3.194 4.575 1.00 45.59 C ANISOU 795 CG LYS A 268 5800 5535 5986 686 -579 -662 C ATOM 796 CD LYS A 268 35.135 2.680 5.914 1.00 40.34 C ANISOU 796 CD LYS A 268 5083 4867 5376 692 -601 -622 C ATOM 797 CE LYS A 268 34.645 1.302 6.218 1.00 42.04 C ANISOU 797 CE LYS A 268 5368 4931 5674 740 -743 -620 C ATOM 798 NZ LYS A 268 34.986 0.953 7.617 1.00 36.44 N ANISOU 798 NZ LYS A 268 4610 4214 5023 715 -761 -566 N ATOM 799 N LEU A 269 33.877 7.287 3.779 1.00 27.74 N ANISOU 799 N LEU A 269 3501 3478 3561 394 -342 -578 N ATOM 800 CA LEU A 269 32.788 8.248 3.893 1.00 27.38 C ANISOU 800 CA LEU A 269 3491 3386 3524 295 -332 -523 C ATOM 801 C LEU A 269 32.439 8.783 2.498 1.00 27.46 C ANISOU 801 C LEU A 269 3558 3399 3475 276 -326 -575 C ATOM 802 O LEU A 269 31.274 8.858 2.121 1.00 26.50 O ANISOU 802 O LEU A 269 3494 3180 3395 245 -365 -561 O ATOM 803 CB LEU A 269 33.212 9.379 4.832 1.00 26.20 C ANISOU 803 CB LEU A 269 3305 3323 3329 219 -271 -463 C ATOM 804 CG LEU A 269 32.195 10.421 5.288 1.00 40.84 C ANISOU 804 CG LEU A 269 5199 5138 5180 139 -262 -400 C ATOM 805 CD1 LEU A 269 30.978 9.775 5.939 1.00 33.38 C ANISOU 805 CD1 LEU A 269 4263 4081 4337 149 -308 -346 C ATOM 806 CD2 LEU A 269 32.893 11.371 6.261 1.00 45.61 C ANISOU 806 CD2 LEU A 269 5785 5822 5724 86 -221 -349 C ATOM 807 N LYS A 270 33.464 9.132 1.731 1.00 25.02 N ANISOU 807 N LYS A 270 3228 3211 3069 294 -278 -629 N ATOM 808 CA LYS A 270 33.277 9.577 0.352 1.00 26.06 C ANISOU 808 CA LYS A 270 3413 3356 3132 279 -271 -684 C ATOM 809 C LYS A 270 32.546 8.525 -0.498 1.00 25.97 C ANISOU 809 C LYS A 270 3481 3213 3175 355 -345 -736 C ATOM 810 O LYS A 270 31.636 8.858 -1.261 1.00 29.38 O ANISOU 810 O LYS A 270 3985 3567 3611 311 -374 -744 O ATOM 811 CB LYS A 270 34.626 9.950 -0.273 1.00 29.23 C ANISOU 811 CB LYS A 270 3759 3935 3413 296 -207 -723 C ATOM 812 CG LYS A 270 34.542 10.496 -1.700 1.00 31.30 C ANISOU 812 CG LYS A 270 4072 4233 3586 270 -192 -776 C ATOM 813 CD LYS A 270 34.672 9.391 -2.739 1.00 29.73 C ANISOU 813 CD LYS A 270 3914 4006 3377 403 -218 -863 C ATOM 814 CE LYS A 270 36.112 8.943 -2.893 1.00 40.93 C ANISOU 814 CE LYS A 270 5242 5596 4712 507 -165 -899 C ATOM 815 NZ LYS A 270 36.251 7.810 -3.871 1.00 43.46 N ANISOU 815 NZ LYS A 270 5621 5884 5009 669 -197 -992 N ATOM 816 N ASN A 271 32.932 7.261 -0.360 1.00 27.63 N ANISOU 816 N ASN A 271 3689 3388 3422 466 -390 -768 N ATOM 817 CA ASN A 271 32.286 6.178 -1.117 1.00 25.44 C ANISOU 817 CA ASN A 271 3509 2967 3189 542 -488 -812 C ATOM 818 C ASN A 271 30.836 5.943 -0.712 1.00 29.87 C ANISOU 818 C ASN A 271 4121 3366 3863 474 -573 -739 C ATOM 819 O ASN A 271 29.971 5.742 -1.567 1.00 25.64 O ANISOU 819 O ASN A 271 3674 2719 3348 464 -640 -749 O ATOM 820 CB ASN A 271 33.090 4.878 -0.998 1.00 27.47 C ANISOU 820 CB ASN A 271 3768 3220 3448 688 -535 -864 C ATOM 821 CG ASN A 271 34.401 4.947 -1.754 1.00 37.39 C ANISOU 821 CG ASN A 271 4986 4638 4580 788 -462 -946 C ATOM 822 OD1 ASN A 271 34.542 5.736 -2.690 1.00 36.19 O ANISOU 822 OD1 ASN A 271 4840 4568 4341 756 -403 -975 O ATOM 823 ND2 ASN A 271 35.371 4.136 -1.345 1.00 39.51 N ANISOU 823 ND2 ASN A 271 5210 4967 4837 908 -468 -979 N ATOM 824 N PHE A 272 30.564 5.993 0.590 1.00 24.35 N ANISOU 824 N PHE A 272 3360 2660 3230 423 -570 -656 N ATOM 825 CA PHE A 272 29.204 5.798 1.087 1.00 24.99 C ANISOU 825 CA PHE A 272 3461 2622 3411 356 -639 -567 C ATOM 826 C PHE A 272 28.258 6.864 0.532 1.00 29.40 C ANISOU 826 C PHE A 272 4046 3168 3956 270 -614 -543 C ATOM 827 O PHE A 272 27.177 6.562 0.014 1.00 28.31 O ANISOU 827 O PHE A 272 3966 2918 3873 244 -693 -514 O ATOM 828 CB PHE A 272 29.163 5.869 2.620 1.00 26.50 C ANISOU 828 CB PHE A 272 3572 2845 3652 317 -615 -482 C ATOM 829 CG PHE A 272 29.805 4.690 3.313 1.00 27.98 C ANISOU 829 CG PHE A 272 3742 3009 3880 386 -669 -486 C ATOM 830 CD1 PHE A 272 30.171 3.564 2.596 1.00 28.40 C ANISOU 830 CD1 PHE A 272 3863 2994 3932 482 -756 -556 C ATOM 831 CD2 PHE A 272 29.998 4.704 4.695 1.00 28.89 C ANISOU 831 CD2 PHE A 272 3787 3160 4031 358 -643 -420 C ATOM 832 CE1 PHE A 272 30.749 2.471 3.232 1.00 32.44 C ANISOU 832 CE1 PHE A 272 4372 3475 4477 552 -822 -566 C ATOM 833 CE2 PHE A 272 30.578 3.620 5.338 1.00 26.05 C ANISOU 833 CE2 PHE A 272 3418 2771 3710 415 -703 -425 C ATOM 834 CZ PHE A 272 30.938 2.497 4.605 1.00 27.06 C ANISOU 834 CZ PHE A 272 3613 2829 3838 511 -796 -499 C ATOM 835 N ILE A 273 28.673 8.114 0.660 1.00 23.72 N ANISOU 835 N ILE A 273 3289 2561 3164 223 -517 -549 N ATOM 836 CA ILE A 273 27.853 9.246 0.207 1.00 23.93 C ANISOU 836 CA ILE A 273 3346 2580 3165 146 -497 -531 C ATOM 837 C ILE A 273 27.691 9.235 -1.315 1.00 27.71 C ANISOU 837 C ILE A 273 3909 3011 3607 152 -529 -604 C ATOM 838 O ILE A 273 26.580 9.367 -1.828 1.00 30.06 O ANISOU 838 O ILE A 273 4259 3217 3947 111 -580 -580 O ATOM 839 CB ILE A 273 28.459 10.577 0.688 1.00 26.05 C ANISOU 839 CB ILE A 273 3579 2970 3346 95 -409 -525 C ATOM 840 CG1 ILE A 273 28.322 10.687 2.217 1.00 22.58 C ANISOU 840 CG1 ILE A 273 3081 2551 2946 85 -388 -442 C ATOM 841 CG2 ILE A 273 27.798 11.772 -0.017 1.00 23.27 C ANISOU 841 CG2 ILE A 273 3284 2612 2945 25 -401 -532 C ATOM 842 CD1 ILE A 273 29.001 11.940 2.823 1.00 23.72 C ANISOU 842 CD1 ILE A 273 3212 2801 3000 40 -321 -427 C ATOM 843 N SER A 274 28.795 9.052 -2.034 1.00 23.52 N ANISOU 843 N SER A 274 3389 2549 2997 207 -500 -688 N ATOM 844 CA SER A 274 28.750 9.115 -3.495 1.00 31.32 C ANISOU 844 CA SER A 274 4461 3509 3930 218 -519 -761 C ATOM 845 C SER A 274 27.785 8.093 -4.044 1.00 31.87 C ANISOU 845 C SER A 274 4620 3407 4081 250 -633 -757 C ATOM 846 O SER A 274 27.004 8.382 -4.951 1.00 27.54 O ANISOU 846 O SER A 274 4149 2778 3536 208 -673 -767 O ATOM 847 CB SER A 274 30.135 8.863 -4.099 1.00 30.40 C ANISOU 847 CB SER A 274 4330 3511 3710 301 -468 -845 C ATOM 848 OG SER A 274 31.002 9.943 -3.827 1.00 33.32 O ANISOU 848 OG SER A 274 4625 4045 3990 244 -375 -837 O ATOM 849 N SER A 275 27.855 6.890 -3.487 1.00 27.44 N ANISOU 849 N SER A 275 4056 2786 3585 320 -698 -739 N ATOM 850 CA SER A 275 27.074 5.761 -3.976 1.00 31.11 C ANISOU 850 CA SER A 275 4621 3081 4120 354 -834 -728 C ATOM 851 C SER A 275 25.569 5.982 -3.805 1.00 30.06 C ANISOU 851 C SER A 275 4498 2841 4081 249 -900 -626 C ATOM 852 O SER A 275 24.764 5.312 -4.452 1.00 31.56 O ANISOU 852 O SER A 275 4783 2887 4322 244 -1020 -605 O ATOM 853 CB SER A 275 27.485 4.482 -3.241 1.00 30.41 C ANISOU 853 CB SER A 275 4526 2953 4076 437 -904 -718 C ATOM 854 OG SER A 275 26.877 4.439 -1.960 1.00 28.20 O ANISOU 854 OG SER A 275 4167 2662 3886 367 -918 -607 O ATOM 855 N GLN A 276 25.197 6.910 -2.925 1.00 28.91 N ANISOU 855 N GLN A 276 4258 2771 3954 173 -827 -557 N ATOM 856 CA GLN A 276 23.789 7.187 -2.642 1.00 27.06 C ANISOU 856 CA GLN A 276 4007 2473 3802 90 -872 -451 C ATOM 857 C GLN A 276 23.500 8.688 -2.743 1.00 27.17 C ANISOU 857 C GLN A 276 3997 2563 3766 28 -784 -453 C ATOM 858 O GLN A 276 22.603 9.205 -2.073 1.00 26.14 O ANISOU 858 O GLN A 276 3810 2444 3676 -20 -774 -365 O ATOM 859 CB GLN A 276 23.434 6.691 -1.235 1.00 31.44 C ANISOU 859 CB GLN A 276 4472 3041 4434 77 -890 -342 C ATOM 860 CG GLN A 276 23.549 5.175 -1.044 1.00 45.00 C ANISOU 860 CG GLN A 276 6225 4664 6210 121 -1009 -321 C ATOM 861 CD GLN A 276 22.418 4.392 -1.713 1.00 60.97 C ANISOU 861 CD GLN A 276 8330 6529 8307 81 -1164 -256 C ATOM 862 OE1 GLN A 276 21.822 4.840 -2.694 1.00 65.46 O ANISOU 862 OE1 GLN A 276 8958 7045 8869 47 -1185 -269 O ATOM 863 NE2 GLN A 276 22.125 3.210 -1.179 1.00 65.87 N ANISOU 863 NE2 GLN A 276 8960 7069 8997 77 -1288 -179 N ATOM 864 N MET A 277 24.262 9.386 -3.576 1.00 30.27 N ANISOU 864 N MET A 277 4014 3335 4154 545 -923 -94 N ATOM 865 CA MET A 277 24.218 10.855 -3.591 1.00 27.30 C ANISOU 865 CA MET A 277 3593 3044 3735 513 -815 -121 C ATOM 866 C MET A 277 22.810 11.453 -3.759 1.00 25.97 C ANISOU 866 C MET A 277 3405 2834 3627 443 -827 -69 C ATOM 867 O MET A 277 22.387 12.311 -2.969 1.00 24.50 O ANISOU 867 O MET A 277 3147 2718 3443 393 -748 -26 O ATOM 868 CB MET A 277 25.177 11.418 -4.653 1.00 23.96 C ANISOU 868 CB MET A 277 3224 2651 3229 578 -772 -217 C ATOM 869 CG MET A 277 25.330 12.944 -4.618 1.00 23.84 C ANISOU 869 CG MET A 277 3155 2734 3170 548 -659 -247 C ATOM 870 SD MET A 277 26.069 13.508 -3.062 1.00 32.46 S ANISOU 870 SD MET A 277 4151 3958 4223 517 -560 -220 S ATOM 871 CE MET A 277 26.317 15.256 -3.401 1.00 33.88 C ANISOU 871 CE MET A 277 4299 4223 4349 497 -456 -271 C ATOM 872 N THR A 278 22.076 11.010 -4.775 1.00 27.41 N ANISOU 872 N THR A 278 3656 2901 3856 441 -925 -67 N ATOM 873 CA THR A 278 20.768 11.612 -5.057 1.00 27.07 C ANISOU 873 CA THR A 278 3597 2819 3870 373 -934 -10 C ATOM 874 C THR A 278 19.790 11.378 -3.908 1.00 25.16 C ANISOU 874 C THR A 278 3274 2575 3709 312 -946 124 C ATOM 875 O THR A 278 19.129 12.308 -3.445 1.00 27.40 O ANISOU 875 O THR A 278 3498 2913 4000 265 -868 179 O ATOM 876 CB THR A 278 20.158 11.059 -6.358 1.00 29.55 C ANISOU 876 CB THR A 278 4006 2997 4223 381 -1058 -24 C ATOM 877 OG1 THR A 278 21.041 11.339 -7.451 1.00 31.49 O ANISOU 877 OG1 THR A 278 4326 3251 4387 454 -1038 -142 O ATOM 878 CG2 THR A 278 18.814 11.693 -6.620 1.00 27.76 C ANISOU 878 CG2 THR A 278 3753 2735 4058 303 -1063 49 C ATOM 879 N ASP A 279 19.720 10.132 -3.444 1.00 25.49 N ANISOU 879 N ASP A 279 3315 2558 3812 323 -1042 182 N ATOM 880 CA ASP A 279 18.849 9.767 -2.331 1.00 29.99 C ANISOU 880 CA ASP A 279 3800 3127 4468 281 -1061 323 C ATOM 881 C ASP A 279 19.163 10.592 -1.085 1.00 26.85 C ANISOU 881 C ASP A 279 3315 2868 4020 279 -922 344 C ATOM 882 O ASP A 279 18.256 11.082 -0.410 1.00 27.51 O ANISOU 882 O ASP A 279 3334 2978 4139 244 -880 450 O ATOM 883 CB ASP A 279 18.991 8.278 -1.986 1.00 42.09 C ANISOU 883 CB ASP A 279 5337 4589 6065 304 -1178 367 C ATOM 884 CG ASP A 279 18.368 7.355 -3.032 1.00 57.08 C ANISOU 884 CG ASP A 279 7321 6328 8039 295 -1345 385 C ATOM 885 OD1 ASP A 279 18.815 6.188 -3.116 1.00 64.91 O ANISOU 885 OD1 ASP A 279 8359 7254 9052 333 -1443 367 O ATOM 886 OD2 ASP A 279 17.441 7.780 -3.756 1.00 53.24 O ANISOU 886 OD2 ASP A 279 6860 5779 7590 251 -1384 417 O ATOM 887 N MET A 280 20.445 10.731 -0.760 1.00 23.46 N ANISOU 887 N MET A 280 2888 2522 3504 321 -854 252 N ATOM 888 CA MET A 280 20.816 11.536 0.400 1.00 20.01 C ANISOU 888 CA MET A 280 2383 2208 3010 320 -734 262 C ATOM 889 C MET A 280 20.493 13.035 0.222 1.00 23.74 C ANISOU 889 C MET A 280 2852 2737 3432 291 -634 239 C ATOM 890 O MET A 280 20.025 13.699 1.152 1.00 22.10 O ANISOU 890 O MET A 280 2593 2590 3214 274 -561 304 O ATOM 891 CB MET A 280 22.290 11.319 0.744 1.00 20.46 C ANISOU 891 CB MET A 280 2445 2337 2993 365 -697 178 C ATOM 892 CG MET A 280 22.575 9.896 1.258 1.00 25.23 C ANISOU 892 CG MET A 280 3032 2908 3646 392 -772 220 C ATOM 893 SD MET A 280 24.279 9.749 1.829 1.00 27.66 S ANISOU 893 SD MET A 280 3330 3317 3863 437 -707 145 S ATOM 894 CE MET A 280 24.193 10.570 3.429 1.00 24.83 C ANISOU 894 CE MET A 280 2880 3078 3474 414 -603 201 C ATOM 895 N CYS A 281 20.734 13.578 -0.966 1.00 21.81 N ANISOU 895 N CYS A 281 2664 2472 3151 292 -628 149 N ATOM 896 CA CYS A 281 20.426 14.996 -1.186 1.00 22.13 C ANISOU 896 CA CYS A 281 2696 2564 3148 262 -533 127 C ATOM 897 C CYS A 281 18.939 15.281 -1.007 1.00 24.88 C ANISOU 897 C CYS A 281 3015 2876 3561 214 -531 246 C ATOM 898 O CYS A 281 18.554 16.311 -0.451 1.00 24.00 O ANISOU 898 O CYS A 281 2873 2830 3418 195 -436 279 O ATOM 899 CB CYS A 281 20.892 15.470 -2.571 1.00 20.62 C ANISOU 899 CB CYS A 281 2561 2356 2919 278 -531 18 C ATOM 900 SG CYS A 281 22.680 15.531 -2.793 1.00 27.48 S ANISOU 900 SG CYS A 281 3451 3293 3698 343 -498 -102 S ATOM 901 N LEU A 282 18.095 14.367 -1.473 1.00 21.95 N ANISOU 901 N LEU A 282 2657 2400 3281 197 -640 320 N ATOM 902 CA LEU A 282 16.648 14.594 -1.418 1.00 22.97 C ANISOU 902 CA LEU A 282 2756 2489 3483 148 -648 455 C ATOM 903 C LEU A 282 16.074 14.404 -0.007 1.00 29.23 C ANISOU 903 C LEU A 282 3474 3321 4312 152 -620 598 C ATOM 904 O LEU A 282 14.956 14.814 0.272 1.00 30.23 O ANISOU 904 O LEU A 282 3564 3443 4478 125 -591 725 O ATOM 905 CB LEU A 282 15.929 13.678 -2.420 1.00 28.05 C ANISOU 905 CB LEU A 282 3442 2998 4220 123 -791 498 C ATOM 906 CG LEU A 282 16.231 14.020 -3.881 1.00 26.66 C ANISOU 906 CG LEU A 282 3342 2779 4007 124 -811 376 C ATOM 907 CD1 LEU A 282 15.660 12.973 -4.838 1.00 29.61 C ANISOU 907 CD1 LEU A 282 3778 3008 4463 110 -973 404 C ATOM 908 CD2 LEU A 282 15.686 15.406 -4.204 1.00 27.66 C ANISOU 908 CD2 LEU A 282 3450 2957 4103 86 -702 378 C ATOM 909 N ASP A 283 16.842 13.770 0.877 1.00 28.53 N ANISOU 909 N ASP A 283 3362 3273 4207 192 -626 584 N ATOM 910 CA ASP A 283 16.359 13.475 2.224 1.00 25.90 C ANISOU 910 CA ASP A 283 2954 2978 3908 211 -605 720 C ATOM 911 C ASP A 283 16.499 14.691 3.132 1.00 27.96 C ANISOU 911 C ASP A 283 3196 3351 4075 229 -464 716 C ATOM 912 O ASP A 283 17.545 15.325 3.154 1.00 23.93 O ANISOU 912 O ASP A 283 2717 2907 3470 242 -401 585 O ATOM 913 CB ASP A 283 17.141 12.303 2.836 1.00 25.36 C ANISOU 913 CB ASP A 283 2863 2913 3860 248 -664 707 C ATOM 914 CG ASP A 283 16.552 11.852 4.161 1.00 26.96 C ANISOU 914 CG ASP A 283 2979 3147 4117 275 -657 862 C ATOM 915 OD1 ASP A 283 17.088 12.224 5.222 1.00 25.16 O ANISOU 915 OD1 ASP A 283 2722 3018 3820 312 -570 850 O ATOM 916 OD2 ASP A 283 15.522 11.158 4.137 1.00 31.25 O ANISOU 916 OD2 ASP A 283 3483 3616 4774 260 -741 1006 O ATOM 917 N LYS A 284 15.460 14.990 3.909 1.00 22.72 N ANISOU 917 N LYS A 284 2485 2708 3440 237 -419 867 N ATOM 918 CA LYS A 284 15.460 16.167 4.789 1.00 24.69 C ANISOU 918 CA LYS A 284 2733 3054 3594 265 -288 875 C ATOM 919 C LYS A 284 16.632 16.188 5.773 1.00 22.55 C ANISOU 919 C LYS A 284 2462 2867 3239 310 -246 791 C ATOM 920 O LYS A 284 17.196 17.247 6.075 1.00 24.24 O ANISOU 920 O LYS A 284 2711 3150 3347 319 -159 707 O ATOM 921 CB LYS A 284 14.140 16.238 5.567 1.00 32.86 C ANISOU 921 CB LYS A 284 3715 4093 4678 289 -255 1080 C ATOM 922 CG LYS A 284 14.014 17.437 6.505 1.00 37.81 C ANISOU 922 CG LYS A 284 4356 4811 5198 333 -120 1104 C ATOM 923 CD LYS A 284 12.722 17.336 7.328 1.00 41.65 C ANISOU 923 CD LYS A 284 4787 5303 5737 380 -90 1333 C ATOM 924 CE LYS A 284 12.274 18.686 7.883 1.00 57.87 C ANISOU 924 CE LYS A 284 6878 7423 7688 419 48 1374 C ATOM 925 NZ LYS A 284 13.198 19.250 8.902 1.00 65.93 N ANISOU 925 NZ LYS A 284 7940 8530 8581 478 119 1276 N ATOM 926 N PHE A 285 17.004 15.014 6.265 1.00 23.04 N ANISOU 926 N PHE A 285 2484 2921 3351 335 -314 817 N ATOM 927 CA PHE A 285 18.088 14.905 7.244 1.00 23.54 C ANISOU 927 CA PHE A 285 2537 3062 3344 375 -280 754 C ATOM 928 C PHE A 285 19.450 14.590 6.634 1.00 23.56 C ANISOU 928 C PHE A 285 2576 3066 3311 360 -316 597 C ATOM 929 O PHE A 285 20.460 15.178 7.031 1.00 21.82 O ANISOU 929 O PHE A 285 2377 2916 2997 370 -261 503 O ATOM 930 CB PHE A 285 17.709 13.882 8.328 1.00 24.17 C ANISOU 930 CB PHE A 285 2538 3152 3492 423 -312 890 C ATOM 931 CG PHE A 285 16.341 14.141 8.908 1.00 23.68 C ANISOU 931 CG PHE A 285 2435 3091 3472 452 -277 1072 C ATOM 932 CD1 PHE A 285 16.094 15.319 9.600 1.00 28.24 C ANISOU 932 CD1 PHE A 285 3038 3738 3954 489 -166 1093 C ATOM 933 CD2 PHE A 285 15.296 13.249 8.706 1.00 28.84 C ANISOU 933 CD2 PHE A 285 3028 3670 4258 446 -359 1228 C ATOM 934 CE1 PHE A 285 14.815 15.597 10.111 1.00 31.39 C ANISOU 934 CE1 PHE A 285 3404 4140 4382 529 -122 1276 C ATOM 935 CE2 PHE A 285 14.022 13.510 9.217 1.00 32.70 C ANISOU 935 CE2 PHE A 285 3471 4163 4790 478 -323 1419 C ATOM 936 CZ PHE A 285 13.786 14.691 9.917 1.00 28.58 C ANISOU 936 CZ PHE A 285 2977 3719 4165 524 -198 1445 C ATOM 937 N ALA A 286 19.496 13.669 5.676 1.00 19.42 N ANISOU 937 N ALA A 286 2062 2460 2858 340 -411 576 N ATOM 938 CA ALA A 286 20.800 13.308 5.101 1.00 21.06 C ANISOU 938 CA ALA A 286 2306 2669 3026 343 -439 443 C ATOM 939 C ALA A 286 21.387 14.467 4.282 1.00 19.54 C ANISOU 939 C ALA A 286 2171 2502 2750 324 -384 321 C ATOM 940 O ALA A 286 22.596 14.553 4.108 1.00 18.84 O ANISOU 940 O ALA A 286 2105 2452 2602 335 -371 222 O ATOM 941 CB ALA A 286 20.700 12.036 4.255 1.00 19.90 C ANISOU 941 CB ALA A 286 2175 2422 2965 340 -557 450 C ATOM 942 N CYS A 287 20.542 15.381 3.800 1.00 18.73 N ANISOU 942 N CYS A 287 2087 2383 2647 296 -348 339 N ATOM 943 CA CYS A 287 21.078 16.507 3.035 1.00 18.09 C ANISOU 943 CA CYS A 287 2048 2330 2494 279 -294 229 C ATOM 944 C CYS A 287 21.928 17.393 3.954 1.00 18.29 C ANISOU 944 C CYS A 287 2071 2454 2424 291 -213 179 C ATOM 945 O CYS A 287 22.831 18.087 3.505 1.00 17.76 O ANISOU 945 O CYS A 287 2029 2422 2298 286 -185 81 O ATOM 946 CB CYS A 287 19.953 17.325 2.366 1.00 19.80 C ANISOU 946 CB CYS A 287 2278 2513 2732 245 -264 264 C ATOM 947 SG CYS A 287 19.065 18.470 3.464 1.00 22.82 S ANISOU 947 SG CYS A 287 2642 2957 3073 243 -158 356 S ATOM 948 N ARG A 288 21.652 17.338 5.251 1.00 19.67 N ANISOU 948 N ARG A 288 2217 2671 2588 311 -184 255 N ATOM 949 CA ARG A 288 22.467 18.072 6.222 1.00 19.04 C ANISOU 949 CA ARG A 288 2144 2675 2415 325 -124 212 C ATOM 950 C ARG A 288 23.855 17.446 6.385 1.00 17.91 C ANISOU 950 C ARG A 288 1992 2563 2248 337 -157 145 C ATOM 951 O ARG A 288 24.868 18.156 6.521 1.00 17.32 O ANISOU 951 O ARG A 288 1937 2542 2101 330 -128 69 O ATOM 952 CB ARG A 288 21.738 18.101 7.564 1.00 19.15 C ANISOU 952 CB ARG A 288 2135 2722 2419 359 -87 319 C ATOM 953 CG ARG A 288 20.369 18.779 7.471 1.00 21.68 C ANISOU 953 CG ARG A 288 2464 3018 2754 357 -42 406 C ATOM 954 CD ARG A 288 20.498 20.310 7.339 1.00 24.96 C ANISOU 954 CD ARG A 288 2936 3469 3079 340 34 337 C ATOM 955 NE ARG A 288 19.199 20.954 7.576 1.00 26.02 N ANISOU 955 NE ARG A 288 3080 3596 3211 353 95 440 N ATOM 956 CZ ARG A 288 19.013 22.241 7.855 1.00 26.38 C ANISOU 956 CZ ARG A 288 3175 3675 3173 360 174 423 C ATOM 957 NH1 ARG A 288 20.041 23.081 7.929 1.00 24.20 N ANISOU 957 NH1 ARG A 288 2943 3438 2813 346 193 302 N ATOM 958 NH2 ARG A 288 17.780 22.687 8.062 1.00 26.39 N ANISOU 958 NH2 ARG A 288 3182 3667 3175 380 233 538 N ATOM 959 N VAL A 289 23.890 16.114 6.390 1.00 20.69 N ANISOU 959 N VAL A 289 2313 2881 2665 354 -220 184 N ATOM 960 CA VAL A 289 25.149 15.370 6.384 1.00 22.11 C ANISOU 960 CA VAL A 289 2486 3082 2832 367 -251 132 C ATOM 961 C VAL A 289 25.975 15.724 5.142 1.00 21.26 C ANISOU 961 C VAL A 289 2419 2962 2696 359 -259 35 C ATOM 962 O VAL A 289 27.183 15.947 5.226 1.00 18.85 O ANISOU 962 O VAL A 289 2117 2709 2336 364 -243 -19 O ATOM 963 CB VAL A 289 24.911 13.842 6.470 1.00 22.37 C ANISOU 963 CB VAL A 289 2484 3066 2948 388 -321 195 C ATOM 964 CG1 VAL A 289 26.242 13.066 6.317 1.00 21.54 C ANISOU 964 CG1 VAL A 289 2380 2980 2824 407 -347 141 C ATOM 965 CG2 VAL A 289 24.254 13.493 7.790 1.00 18.56 C ANISOU 965 CG2 VAL A 289 1945 2613 2493 408 -308 300 C ATOM 966 N ILE A 290 25.316 15.809 3.991 1.00 20.25 N ANISOU 966 N ILE A 290 2319 2767 2607 349 -283 22 N ATOM 967 CA ILE A 290 26.015 16.168 2.758 1.00 18.47 C ANISOU 967 CA ILE A 290 2131 2531 2356 356 -286 -63 C ATOM 968 C ILE A 290 26.619 17.576 2.847 1.00 16.56 C ANISOU 968 C ILE A 290 1892 2359 2042 338 -218 -118 C ATOM 969 O ILE A 290 27.789 17.773 2.538 1.00 18.46 O ANISOU 969 O ILE A 290 2135 2637 2242 353 -212 -169 O ATOM 970 CB ILE A 290 25.080 16.070 1.535 1.00 18.84 C ANISOU 970 CB ILE A 290 2210 2492 2456 349 -325 -64 C ATOM 971 CG1 ILE A 290 24.615 14.621 1.350 1.00 24.47 C ANISOU 971 CG1 ILE A 290 2931 3122 3244 367 -415 -14 C ATOM 972 CG2 ILE A 290 25.780 16.579 0.265 1.00 18.58 C ANISOU 972 CG2 ILE A 290 2212 2458 2389 369 -317 -150 C ATOM 973 CD1 ILE A 290 23.609 14.454 0.251 1.00 33.30 C ANISOU 973 CD1 ILE A 290 4086 4145 4421 354 -470 -2 C ATOM 974 N GLN A 291 25.833 18.543 3.297 1.00 16.29 N ANISOU 974 N GLN A 291 1856 2341 1991 309 -170 -97 N ATOM 975 CA GLN A 291 26.315 19.917 3.362 1.00 16.01 C ANISOU 975 CA GLN A 291 1831 2361 1891 289 -115 -149 C ATOM 976 C GLN A 291 27.498 20.060 4.317 1.00 18.00 C ANISOU 976 C GLN A 291 2073 2682 2086 293 -108 -165 C ATOM 977 O GLN A 291 28.480 20.753 4.014 1.00 17.86 O ANISOU 977 O GLN A 291 2056 2702 2029 285 -99 -216 O ATOM 978 CB GLN A 291 25.190 20.860 3.775 1.00 15.87 C ANISOU 978 CB GLN A 291 1824 2344 1861 266 -62 -114 C ATOM 979 CG GLN A 291 24.114 21.029 2.691 1.00 16.12 C ANISOU 979 CG GLN A 291 1865 2318 1944 250 -58 -102 C ATOM 980 CD GLN A 291 22.916 21.807 3.206 1.00 21.60 C ANISOU 980 CD GLN A 291 2566 3012 2627 233 0 -40 C ATOM 981 OE1 GLN A 291 23.021 23.001 3.513 1.00 19.87 O ANISOU 981 OE1 GLN A 291 2367 2836 2348 221 59 -69 O ATOM 982 NE2 GLN A 291 21.775 21.138 3.310 1.00 19.22 N ANISOU 982 NE2 GLN A 291 2253 2663 2387 235 -18 56 N ATOM 983 N SER A 292 27.423 19.423 5.473 1.00 17.96 N ANISOU 983 N SER A 292 2052 2694 2078 303 -116 -113 N ATOM 984 CA SER A 292 28.536 19.608 6.403 1.00 19.80 C ANISOU 984 CA SER A 292 2277 2992 2253 301 -113 -127 C ATOM 985 C SER A 292 29.782 18.897 5.879 1.00 20.77 C ANISOU 985 C SER A 292 2381 3127 2383 316 -146 -150 C ATOM 986 O SER A 292 30.900 19.383 6.081 1.00 21.54 O ANISOU 986 O SER A 292 2475 3274 2435 304 -144 -174 O ATOM 987 CB SER A 292 28.197 19.160 7.827 1.00 31.07 C ANISOU 987 CB SER A 292 3691 4445 3668 317 -107 -66 C ATOM 988 OG SER A 292 27.647 17.872 7.831 1.00 32.15 O ANISOU 988 OG SER A 292 3796 4546 3874 341 -137 -8 O ATOM 989 N SER A 293 29.598 17.771 5.188 1.00 19.28 N ANISOU 989 N SER A 293 2186 2890 2249 343 -181 -136 N ATOM 990 CA SER A 293 30.735 17.086 4.577 1.00 17.17 C ANISOU 990 CA SER A 293 1914 2630 1982 372 -206 -152 C ATOM 991 C SER A 293 31.414 17.935 3.496 1.00 22.61 C ANISOU 991 C SER A 293 2615 3329 2646 378 -193 -202 C ATOM 992 O SER A 293 32.635 17.960 3.406 1.00 21.53 O ANISOU 992 O SER A 293 2465 3237 2480 392 -193 -203 O ATOM 993 CB SER A 293 30.325 15.726 3.987 1.00 24.07 C ANISOU 993 CB SER A 293 2797 3436 2914 408 -253 -131 C ATOM 994 OG SER A 293 29.841 14.857 4.996 1.00 23.68 O ANISOU 994 OG SER A 293 2718 3381 2897 408 -269 -74 O ATOM 995 N LEU A 294 30.612 18.587 2.654 1.00 17.55 N ANISOU 995 N LEU A 294 1995 2650 2022 371 -182 -232 N ATOM 996 CA LEU A 294 31.137 19.447 1.589 1.00 17.84 C ANISOU 996 CA LEU A 294 2036 2700 2044 382 -166 -275 C ATOM 997 C LEU A 294 32.037 20.555 2.124 1.00 20.11 C ANISOU 997 C LEU A 294 2299 3057 2284 351 -143 -283 C ATOM 998 O LEU A 294 33.041 20.906 1.504 1.00 20.06 O ANISOU 998 O LEU A 294 2275 3081 2265 373 -143 -291 O ATOM 999 CB LEU A 294 29.981 20.079 0.806 1.00 16.78 C ANISOU 999 CB LEU A 294 1920 2520 1936 367 -149 -301 C ATOM 1000 CG LEU A 294 29.248 19.125 -0.139 1.00 18.57 C ANISOU 1000 CG LEU A 294 2175 2667 2212 399 -187 -299 C ATOM 1001 CD1 LEU A 294 27.919 19.742 -0.611 1.00 15.82 C ANISOU 1001 CD1 LEU A 294 1841 2277 1894 367 -170 -304 C ATOM 1002 CD2 LEU A 294 30.156 18.760 -1.334 1.00 17.35 C ANISOU 1002 CD2 LEU A 294 2037 2505 2050 466 -207 -328 C ATOM 1003 N GLN A 295 31.682 21.122 3.268 1.00 17.68 N ANISOU 1003 N GLN A 295 1996 2772 1951 307 -128 -275 N ATOM 1004 CA GLN A 295 32.458 22.257 3.760 1.00 20.27 C ANISOU 1004 CA GLN A 295 2316 3152 2233 273 -120 -287 C ATOM 1005 C GLN A 295 33.580 21.867 4.718 1.00 21.33 C ANISOU 1005 C GLN A 295 2432 3334 2337 266 -146 -253 C ATOM 1006 O GLN A 295 34.519 22.628 4.907 1.00 24.48 O ANISOU 1006 O GLN A 295 2819 3773 2709 242 -159 -251 O ATOM 1007 CB GLN A 295 31.556 23.333 4.380 1.00 23.08 C ANISOU 1007 CB GLN A 295 2703 3504 2562 234 -92 -303 C ATOM 1008 CG GLN A 295 30.959 22.987 5.720 1.00 27.91 C ANISOU 1008 CG GLN A 295 3337 4118 3149 228 -87 -270 C ATOM 1009 CD GLN A 295 29.964 24.046 6.193 1.00 39.87 C ANISOU 1009 CD GLN A 295 4895 5624 4631 209 -49 -278 C ATOM 1010 OE1 GLN A 295 29.479 23.997 7.322 1.00 35.24 O ANISOU 1010 OE1 GLN A 295 4335 5044 4011 217 -38 -247 O ATOM 1011 NE2 GLN A 295 29.652 25.000 5.322 1.00 27.15 N ANISOU 1011 NE2 GLN A 295 3290 3998 3026 193 -24 -314 N ATOM 1012 N ASN A 296 33.494 20.677 5.293 1.00 19.50 N ANISOU 1012 N ASN A 296 2195 3097 2116 285 -157 -219 N ATOM 1013 CA ASN A 296 34.476 20.252 6.292 1.00 24.20 C ANISOU 1013 CA ASN A 296 2769 3742 2683 276 -175 -182 C ATOM 1014 C ASN A 296 35.527 19.246 5.808 1.00 24.92 C ANISOU 1014 C ASN A 296 2830 3850 2790 313 -189 -148 C ATOM 1015 O ASN A 296 36.657 19.245 6.303 1.00 23.50 O ANISOU 1015 O ASN A 296 2625 3720 2584 300 -201 -112 O ATOM 1016 CB ASN A 296 33.762 19.686 7.531 1.00 25.95 C ANISOU 1016 CB ASN A 296 2998 3964 2898 273 -170 -158 C ATOM 1017 CG ASN A 296 32.953 20.744 8.276 1.00 33.01 C ANISOU 1017 CG ASN A 296 3931 4857 3755 248 -152 -175 C ATOM 1018 OD1 ASN A 296 33.340 21.903 8.327 1.00 37.71 O ANISOU 1018 OD1 ASN A 296 4549 5468 4311 217 -156 -203 O ATOM 1019 ND2 ASN A 296 31.824 20.339 8.860 1.00 28.84 N ANISOU 1019 ND2 ASN A 296 3412 4308 3238 266 -134 -150 N ATOM 1020 N MET A 297 35.160 18.370 4.872 1.00 20.44 N ANISOU 1020 N MET A 297 2269 3237 2260 362 -190 -151 N ATOM 1021 CA MET A 297 36.094 17.339 4.417 1.00 20.40 C ANISOU 1021 CA MET A 297 2249 3241 2260 412 -199 -116 C ATOM 1022 C MET A 297 37.247 18.000 3.692 1.00 24.56 C ANISOU 1022 C MET A 297 2758 3805 2767 429 -194 -100 C ATOM 1023 O MET A 297 37.111 19.128 3.232 1.00 21.90 O ANISOU 1023 O MET A 297 2422 3470 2429 411 -188 -129 O ATOM 1024 CB MET A 297 35.421 16.366 3.440 1.00 17.91 C ANISOU 1024 CB MET A 297 1965 2855 1983 468 -211 -130 C ATOM 1025 CG MET A 297 34.488 15.331 4.035 1.00 30.66 C ANISOU 1025 CG MET A 297 3586 4428 3634 466 -230 -118 C ATOM 1026 SD MET A 297 33.876 14.366 2.613 1.00 40.41 S ANISOU 1026 SD MET A 297 4874 5567 4912 532 -267 -138 S ATOM 1027 CE MET A 297 33.097 12.989 3.443 1.00 61.02 C ANISOU 1027 CE MET A 297 7475 8136 7575 528 -303 -99 C ATOM 1028 N ASP A 298 38.370 17.291 3.572 1.00 18.35 N ANISOU 1028 N ASP A 298 1950 3051 1969 469 -194 -43 N ATOM 1029 CA ASP A 298 39.474 17.771 2.746 1.00 20.82 C ANISOU 1029 CA ASP A 298 2240 3400 2271 506 -188 -3 C ATOM 1030 C ASP A 298 38.892 18.124 1.377 1.00 19.48 C ANISOU 1030 C ASP A 298 2098 3183 2119 558 -180 -51 C ATOM 1031 O ASP A 298 38.028 17.413 0.863 1.00 19.22 O ANISOU 1031 O ASP A 298 2109 3088 2104 595 -184 -90 O ATOM 1032 CB ASP A 298 40.539 16.691 2.597 1.00 24.24 C ANISOU 1032 CB ASP A 298 2660 3859 2690 568 -179 73 C ATOM 1033 CG ASP A 298 41.281 16.424 3.905 1.00 25.63 C ANISOU 1033 CG ASP A 298 2797 4093 2848 514 -183 132 C ATOM 1034 OD1 ASP A 298 41.293 17.306 4.787 1.00 21.61 O ANISOU 1034 OD1 ASP A 298 2269 3612 2330 435 -200 125 O ATOM 1035 OD2 ASP A 298 41.848 15.331 4.036 1.00 24.29 O ANISOU 1035 OD2 ASP A 298 2621 3939 2671 553 -170 186 O ATOM 1036 N LEU A 299 39.351 19.221 0.790 1.00 18.80 N ANISOU 1036 N LEU A 299 1984 3125 2034 560 -174 -43 N ATOM 1037 CA LEU A 299 38.717 19.714 -0.436 1.00 19.12 C ANISOU 1037 CA LEU A 299 2044 3129 2094 602 -162 -94 C ATOM 1038 C LEU A 299 38.739 18.681 -1.557 1.00 22.91 C ANISOU 1038 C LEU A 299 2564 3568 2571 711 -158 -91 C ATOM 1039 O LEU A 299 37.748 18.501 -2.274 1.00 19.75 O ANISOU 1039 O LEU A 299 2211 3106 2188 735 -162 -151 O ATOM 1040 CB LEU A 299 39.367 21.026 -0.893 1.00 26.23 C ANISOU 1040 CB LEU A 299 2891 4074 3000 596 -156 -72 C ATOM 1041 CG LEU A 299 38.773 21.696 -2.140 1.00 24.09 C ANISOU 1041 CG LEU A 299 2625 3778 2751 636 -137 -121 C ATOM 1042 CD1 LEU A 299 37.262 21.899 -2.022 1.00 18.61 C ANISOU 1042 CD1 LEU A 299 1973 3026 2070 583 -132 -208 C ATOM 1043 CD2 LEU A 299 39.475 23.040 -2.392 1.00 25.25 C ANISOU 1043 CD2 LEU A 299 2704 3977 2913 619 -136 -88 C ATOM 1044 N SER A 300 39.872 18.003 -1.717 1.00 21.94 N ANISOU 1044 N SER A 300 2432 3479 2427 779 -152 -15 N ATOM 1045 CA SER A 300 39.986 17.025 -2.791 1.00 23.45 C ANISOU 1045 CA SER A 300 2677 3630 2603 900 -148 -7 C ATOM 1046 C SER A 300 38.923 15.938 -2.673 1.00 24.57 C ANISOU 1046 C SER A 300 2889 3690 2755 897 -176 -65 C ATOM 1047 O SER A 300 38.405 15.459 -3.684 1.00 25.54 O ANISOU 1047 O SER A 300 3079 3748 2879 971 -192 -104 O ATOM 1048 CB SER A 300 41.395 16.413 -2.833 1.00 34.10 C ANISOU 1048 CB SER A 300 4008 5032 3919 976 -129 99 C ATOM 1049 OG SER A 300 42.334 17.387 -3.258 1.00 41.79 O ANISOU 1049 OG SER A 300 4916 6071 4892 1003 -110 169 O ATOM 1050 N LEU A 301 38.582 15.549 -1.449 1.00 22.06 N ANISOU 1050 N LEU A 301 2559 3373 2450 816 -189 -67 N ATOM 1051 CA LEU A 301 37.505 14.570 -1.273 1.00 18.93 C ANISOU 1051 CA LEU A 301 2214 2899 2079 807 -223 -108 C ATOM 1052 C LEU A 301 36.112 15.180 -1.430 1.00 23.59 C ANISOU 1052 C LEU A 301 2820 3437 2706 751 -239 -176 C ATOM 1053 O LEU A 301 35.214 14.538 -1.991 1.00 21.01 O ANISOU 1053 O LEU A 301 2549 3028 2404 776 -275 -209 O ATOM 1054 CB LEU A 301 37.630 13.821 0.065 1.00 26.31 C ANISOU 1054 CB LEU A 301 3120 3857 3018 755 -229 -73 C ATOM 1055 CG LEU A 301 38.633 12.649 0.048 1.00 39.87 C ANISOU 1055 CG LEU A 301 4850 5589 4709 826 -223 -11 C ATOM 1056 CD1 LEU A 301 38.302 11.660 1.126 1.00 46.53 C ANISOU 1056 CD1 LEU A 301 5680 6423 5575 786 -239 3 C ATOM 1057 CD2 LEU A 301 38.647 11.928 -1.294 1.00 45.34 C ANISOU 1057 CD2 LEU A 301 5624 6215 5387 942 -240 -24 C ATOM 1058 N ALA A 302 35.924 16.405 -0.941 1.00 20.89 N ANISOU 1058 N ALA A 302 2433 3138 2367 677 -216 -189 N ATOM 1059 CA ALA A 302 34.658 17.106 -1.167 1.00 20.65 C ANISOU 1059 CA ALA A 302 2415 3065 2365 630 -217 -243 C ATOM 1060 C ALA A 302 34.363 17.260 -2.662 1.00 24.89 C ANISOU 1060 C ALA A 302 2992 3557 2910 695 -221 -280 C ATOM 1061 O ALA A 302 33.215 17.118 -3.090 1.00 21.99 O ANISOU 1061 O ALA A 302 2661 3120 2573 684 -243 -315 O ATOM 1062 CB ALA A 302 34.648 18.479 -0.482 1.00 17.23 C ANISOU 1062 CB ALA A 302 1937 2687 1922 553 -188 -250 C ATOM 1063 N CYS A 303 35.391 17.550 -3.458 1.00 23.12 N ANISOU 1063 N CYS A 303 2755 3370 2659 767 -202 -263 N ATOM 1064 CA CYS A 303 35.199 17.655 -4.907 1.00 25.07 C ANISOU 1064 CA CYS A 303 3039 3579 2905 848 -203 -294 C ATOM 1065 C CYS A 303 34.651 16.352 -5.503 1.00 27.87 C ANISOU 1065 C CYS A 303 3483 3841 3265 911 -253 -314 C ATOM 1066 O CYS A 303 33.863 16.372 -6.446 1.00 25.14 O ANISOU 1066 O CYS A 303 3185 3432 2934 938 -274 -358 O ATOM 1067 CB CYS A 303 36.501 18.055 -5.605 1.00 21.78 C ANISOU 1067 CB CYS A 303 2591 3226 2458 935 -172 -250 C ATOM 1068 SG CYS A 303 37.003 19.750 -5.228 1.00 26.58 S ANISOU 1068 SG CYS A 303 3098 3924 3077 864 -133 -231 S ATOM 1069 N LYS A 304 35.067 15.219 -4.948 1.00 26.52 N ANISOU 1069 N LYS A 304 3336 3659 3082 932 -277 -278 N ATOM 1070 CA LYS A 304 34.577 13.917 -5.413 1.00 23.81 C ANISOU 1070 CA LYS A 304 3082 3219 2746 987 -337 -293 C ATOM 1071 C LYS A 304 33.086 13.724 -5.132 1.00 30.17 C ANISOU 1071 C LYS A 304 3907 3946 3609 906 -386 -325 C ATOM 1072 O LYS A 304 32.376 13.111 -5.931 1.00 24.98 O ANISOU 1072 O LYS A 304 3327 3194 2970 942 -446 -353 O ATOM 1073 CB LYS A 304 35.400 12.773 -4.802 1.00 30.19 C ANISOU 1073 CB LYS A 304 3901 4039 3531 1024 -346 -242 C ATOM 1074 CG LYS A 304 36.823 12.682 -5.349 1.00 35.22 C ANISOU 1074 CG LYS A 304 4542 4732 4107 1134 -306 -193 C ATOM 1075 CD LYS A 304 37.519 11.440 -4.818 1.00 54.13 C ANISOU 1075 CD LYS A 304 6960 7128 6479 1174 -313 -140 C ATOM 1076 CE LYS A 304 39.024 11.450 -5.070 1.00 58.34 C ANISOU 1076 CE LYS A 304 7474 7740 6954 1267 -258 -60 C ATOM 1077 NZ LYS A 304 39.684 10.318 -4.343 1.00 62.59 N ANISOU 1077 NZ LYS A 304 8016 8292 7473 1283 -253 -1 N ATOM 1078 N LEU A 305 32.596 14.266 -4.020 1.00 23.06 N ANISOU 1078 N LEU A 305 2940 3083 2738 801 -365 -313 N ATOM 1079 CA LEU A 305 31.152 14.220 -3.752 1.00 23.91 C ANISOU 1079 CA LEU A 305 3056 3127 2903 729 -401 -321 C ATOM 1080 C LEU A 305 30.373 14.951 -4.827 1.00 22.44 C ANISOU 1080 C LEU A 305 2895 2899 2731 729 -402 -364 C ATOM 1081 O LEU A 305 29.312 14.507 -5.269 1.00 25.16 O ANISOU 1081 O LEU A 305 3287 3155 3119 716 -460 -371 O ATOM 1082 CB LEU A 305 30.803 14.864 -2.403 1.00 22.82 C ANISOU 1082 CB LEU A 305 2846 3047 2779 634 -362 -294 C ATOM 1083 CG LEU A 305 31.465 14.306 -1.156 1.00 30.70 C ANISOU 1083 CG LEU A 305 3803 4096 3764 619 -354 -250 C ATOM 1084 CD1 LEU A 305 30.820 14.945 0.077 1.00 30.52 C ANISOU 1084 CD1 LEU A 305 3728 4111 3755 537 -325 -227 C ATOM 1085 CD2 LEU A 305 31.320 12.796 -1.112 1.00 28.72 C ANISOU 1085 CD2 LEU A 305 3589 3779 3544 654 -417 -225 C ATOM 1086 N VAL A 306 30.889 16.100 -5.229 1.00 24.22 N ANISOU 1086 N VAL A 306 3085 3191 2926 738 -342 -386 N ATOM 1087 CA VAL A 306 30.229 16.900 -6.259 1.00 21.96 C ANISOU 1087 CA VAL A 306 2811 2881 2652 739 -330 -427 C ATOM 1088 C VAL A 306 30.141 16.109 -7.563 1.00 26.66 C ANISOU 1088 C VAL A 306 3494 3393 3242 833 -387 -454 C ATOM 1089 O VAL A 306 29.144 16.165 -8.287 1.00 23.86 O ANISOU 1089 O VAL A 306 3179 2970 2918 821 -420 -480 O ATOM 1090 CB VAL A 306 31.001 18.204 -6.511 1.00 23.41 C ANISOU 1090 CB VAL A 306 2933 3156 2806 748 -258 -440 C ATOM 1091 CG1 VAL A 306 30.377 18.975 -7.666 1.00 23.47 C ANISOU 1091 CG1 VAL A 306 2948 3142 2827 761 -241 -482 C ATOM 1092 CG2 VAL A 306 31.032 19.050 -5.226 1.00 23.35 C ANISOU 1092 CG2 VAL A 306 2857 3218 2799 653 -214 -419 C ATOM 1093 N GLN A 307 31.204 15.378 -7.858 1.00 26.55 N ANISOU 1093 N GLN A 307 3517 3386 3185 931 -399 -444 N ATOM 1094 CA GLN A 307 31.260 14.554 -9.050 1.00 30.92 C ANISOU 1094 CA GLN A 307 4173 3859 3716 1042 -455 -469 C ATOM 1095 C GLN A 307 30.143 13.496 -9.047 1.00 33.33 C ANISOU 1095 C GLN A 307 4555 4041 4067 1010 -555 -474 C ATOM 1096 O GLN A 307 29.704 13.045 -10.105 1.00 34.16 O ANISOU 1096 O GLN A 307 4753 4055 4170 1070 -619 -507 O ATOM 1097 CB GLN A 307 32.654 13.914 -9.148 1.00 31.83 C ANISOU 1097 CB GLN A 307 4312 4011 3769 1154 -440 -437 C ATOM 1098 CG GLN A 307 32.868 12.982 -10.320 1.00 50.52 C ANISOU 1098 CG GLN A 307 6803 6298 6095 1293 -495 -457 C ATOM 1099 CD GLN A 307 34.257 12.347 -10.307 1.00 65.06 C ANISOU 1099 CD GLN A 307 8666 8183 7871 1408 -467 -407 C ATOM 1100 OE1 GLN A 307 35.225 12.945 -9.827 1.00 61.97 O ANISOU 1100 OE1 GLN A 307 8185 7899 7460 1405 -393 -358 O ATOM 1101 NE2 GLN A 307 34.357 11.129 -10.834 1.00 67.82 N ANISOU 1101 NE2 GLN A 307 9138 8445 8186 1509 -531 -413 N ATOM 1102 N ALA A 308 29.677 13.114 -7.859 1.00 27.88 N ANISOU 1102 N ALA A 308 3824 3346 3421 919 -573 -436 N ATOM 1103 CA ALA A 308 28.631 12.094 -7.717 1.00 25.17 C ANISOU 1103 CA ALA A 308 3534 2890 3138 882 -673 -419 C ATOM 1104 C ALA A 308 27.208 12.631 -7.948 1.00 25.96 C ANISOU 1104 C ALA A 308 3626 2939 3301 798 -699 -418 C ATOM 1105 O ALA A 308 26.241 11.868 -7.963 1.00 26.25 O ANISOU 1105 O ALA A 308 3703 2873 3397 763 -792 -391 O ATOM 1106 CB ALA A 308 28.710 11.444 -6.341 1.00 26.54 C ANISOU 1106 CB ALA A 308 3656 3087 3341 829 -679 -364 C ATOM 1107 N LEU A 309 27.064 13.941 -8.078 1.00 21.41 N ANISOU 1107 N LEU A 309 2989 2430 2715 760 -618 -435 N ATOM 1108 CA LEU A 309 25.750 14.488 -8.404 1.00 22.89 C ANISOU 1108 CA LEU A 309 3170 2571 2955 687 -632 -428 C ATOM 1109 C LEU A 309 25.305 13.932 -9.755 1.00 27.43 C ANISOU 1109 C LEU A 309 3849 3035 3537 743 -722 -463 C ATOM 1110 O LEU A 309 26.132 13.732 -10.657 1.00 25.97 O ANISOU 1110 O LEU A 309 3727 2846 3295 852 -727 -513 O ATOM 1111 CB LEU A 309 25.780 16.013 -8.460 1.00 20.47 C ANISOU 1111 CB LEU A 309 2790 2359 2629 651 -525 -449 C ATOM 1112 CG LEU A 309 25.864 16.708 -7.100 1.00 24.31 C ANISOU 1112 CG LEU A 309 3186 2935 3114 577 -449 -412 C ATOM 1113 CD1 LEU A 309 26.219 18.179 -7.294 1.00 21.67 C ANISOU 1113 CD1 LEU A 309 2795 2693 2747 564 -351 -446 C ATOM 1114 CD2 LEU A 309 24.551 16.561 -6.335 1.00 20.71 C ANISOU 1114 CD2 LEU A 309 2709 2437 2722 488 -473 -345 C ATOM 1115 N PRO A 310 23.999 13.681 -9.895 1.00 26.71 N ANISOU 1115 N PRO A 310 3780 2852 3516 675 -795 -428 N ATOM 1116 CA PRO A 310 23.442 13.135 -11.136 1.00 29.60 C ANISOU 1116 CA PRO A 310 4254 3097 3896 715 -899 -455 C ATOM 1117 C PRO A 310 23.459 14.198 -12.227 1.00 33.10 C ANISOU 1117 C PRO A 310 4698 3576 4304 746 -837 -513 C ATOM 1118 O PRO A 310 23.507 15.394 -11.923 1.00 27.07 O ANISOU 1118 O PRO A 310 3839 2914 3533 701 -724 -514 O ATOM 1119 CB PRO A 310 21.998 12.810 -10.746 1.00 25.72 C ANISOU 1119 CB PRO A 310 3749 2520 3501 606 -978 -374 C ATOM 1120 CG PRO A 310 21.680 13.868 -9.701 1.00 29.05 C ANISOU 1120 CG PRO A 310 4046 3050 3942 518 -861 -324 C ATOM 1121 CD PRO A 310 22.958 13.875 -8.868 1.00 25.26 C ANISOU 1121 CD PRO A 310 3524 2672 3403 561 -788 -347 C ATOM 1122 N ARG A 311 23.401 13.768 -13.482 1.00 33.21 N ANISOU 1122 N ARG A 311 4819 3503 4296 825 -914 -561 N ATOM 1123 CA ARG A 311 23.496 14.685 -14.614 1.00 36.29 C ANISOU 1123 CA ARG A 311 5214 3927 4649 877 -858 -618 C ATOM 1124 C ARG A 311 22.232 14.667 -15.454 1.00 38.69 C ANISOU 1124 C ARG A 311 5572 4126 5003 829 -939 -614 C ATOM 1125 O ARG A 311 22.179 15.287 -16.509 1.00 41.34 O ANISOU 1125 O ARG A 311 5924 4470 5312 875 -911 -662 O ATOM 1126 CB ARG A 311 24.676 14.290 -15.503 1.00 39.05 C ANISOU 1126 CB ARG A 311 5648 4278 4911 1043 -864 -679 C ATOM 1127 CG ARG A 311 25.922 13.968 -14.728 1.00 45.09 C ANISOU 1127 CG ARG A 311 6384 5119 5630 1097 -815 -665 C ATOM 1128 CD ARG A 311 26.292 15.134 -13.848 1.00 42.32 C ANISOU 1128 CD ARG A 311 5886 4909 5286 1026 -684 -642 C ATOM 1129 NE ARG A 311 27.451 14.856 -13.004 1.00 40.18 N ANISOU 1129 NE ARG A 311 5579 4711 4977 1061 -642 -618 N ATOM 1130 CZ ARG A 311 28.705 15.145 -13.333 1.00 43.85 C ANISOU 1130 CZ ARG A 311 6028 5257 5378 1167 -577 -627 C ATOM 1131 NH1 ARG A 311 28.982 15.694 -14.510 1.00 33.30 N ANISOU 1131 NH1 ARG A 311 4709 3938 4005 1262 -547 -662 N ATOM 1132 NH2 ARG A 311 29.687 14.871 -12.487 1.00 40.33 N ANISOU 1132 NH2 ARG A 311 5544 4874 4905 1182 -544 -591 N ATOM 1133 N ASP A 312 21.217 13.954 -14.992 1.00 40.71 N ANISOU 1133 N ASP A 312 5849 4283 5334 738 -1042 -548 N ATOM 1134 CA ASP A 312 19.998 13.797 -15.768 1.00 44.76 C ANISOU 1134 CA ASP A 312 6422 4682 5904 686 -1142 -527 C ATOM 1135 C ASP A 312 18.833 14.489 -15.083 1.00 46.01 C ANISOU 1135 C ASP A 312 6473 4866 6145 539 -1098 -435 C ATOM 1136 O ASP A 312 19.029 15.431 -14.316 1.00 38.24 O ANISOU 1136 O ASP A 312 5373 4004 5151 496 -962 -418 O ATOM 1137 CB ASP A 312 19.697 12.316 -15.981 1.00 48.68 C ANISOU 1137 CB ASP A 312 7049 5018 6429 710 -1326 -510 C ATOM 1138 CG ASP A 312 19.666 11.533 -14.681 1.00 48.51 C ANISOU 1138 CG ASP A 312 6987 4986 6460 655 -1363 -434 C ATOM 1139 OD1 ASP A 312 19.445 12.142 -13.612 1.00 38.37 O ANISOU 1139 OD1 ASP A 312 5574 3795 5211 570 -1267 -371 O ATOM 1140 OD2 ASP A 312 19.856 10.303 -14.730 1.00 47.64 O ANISOU 1140 OD2 ASP A 312 6976 4773 6353 703 -1490 -435 O ATOM 1141 N ALA A 313 17.623 14.011 -15.358 1.00 38.74 N ANISOU 1141 N ALA A 313 5594 3825 5303 464 -1216 -367 N ATOM 1142 CA ALA A 313 16.415 14.585 -14.774 1.00 41.49 C ANISOU 1142 CA ALA A 313 5846 4185 5732 330 -1182 -254 C ATOM 1143 C ALA A 313 16.473 14.676 -13.246 1.00 32.82 C ANISOU 1143 C ALA A 313 4643 3168 4658 278 -1109 -176 C ATOM 1144 O ALA A 313 15.841 15.536 -12.648 1.00 32.77 O ANISOU 1144 O ALA A 313 4540 3229 4681 198 -1013 -104 O ATOM 1145 CB ALA A 313 15.187 13.796 -15.215 1.00 43.76 C ANISOU 1145 CB ALA A 313 6201 4316 6111 264 -1351 -170 C ATOM 1146 N ARG A 314 17.238 13.800 -12.608 1.00 36.15 N ANISOU 1146 N ARG A 314 4208 3891 5638 515 -1723 122 N ATOM 1147 CA ARG A 314 17.378 13.860 -11.155 1.00 36.81 C ANISOU 1147 CA ARG A 314 4223 4015 5750 424 -1616 236 C ATOM 1148 C ARG A 314 18.015 15.180 -10.686 1.00 32.37 C ANISOU 1148 C ARG A 314 3671 3604 5025 394 -1374 230 C ATOM 1149 O ARG A 314 17.782 15.621 -9.563 1.00 35.24 O ANISOU 1149 O ARG A 314 3984 4005 5399 319 -1255 341 O ATOM 1150 CB ARG A 314 18.184 12.661 -10.641 1.00 33.11 C ANISOU 1150 CB ARG A 314 3740 3509 5329 440 -1730 204 C ATOM 1151 CG ARG A 314 17.494 11.317 -10.878 1.00 39.33 C ANISOU 1151 CG ARG A 314 4503 4132 6307 452 -1985 236 C ATOM 1152 CD ARG A 314 18.423 10.148 -10.593 1.00 40.13 C ANISOU 1152 CD ARG A 314 4609 4199 6438 488 -2112 171 C ATOM 1153 NE ARG A 314 19.555 10.090 -11.517 1.00 38.69 N ANISOU 1153 NE ARG A 314 4515 4076 6110 605 -2131 -17 N ATOM 1154 CZ ARG A 314 20.638 9.343 -11.318 1.00 43.74 C ANISOU 1154 CZ ARG A 314 5172 4731 6716 651 -2189 -101 C ATOM 1155 NH1 ARG A 314 20.740 8.603 -10.222 1.00 40.52 N ANISOU 1155 NH1 ARG A 314 4703 4280 6414 584 -2233 -17 N ATOM 1156 NH2 ARG A 314 21.627 9.347 -12.205 1.00 41.16 N ANISOU 1156 NH2 ARG A 314 4921 4470 6247 769 -2196 -262 N ATOM 1157 N LEU A 315 18.817 15.809 -11.536 1.00 31.99 N ANISOU 1157 N LEU A 315 3687 3640 4826 460 -1306 106 N ATOM 1158 CA LEU A 315 19.464 17.060 -11.138 1.00 27.96 C ANISOU 1158 CA LEU A 315 3186 3263 4174 431 -1097 103 C ATOM 1159 C LEU A 315 18.441 18.189 -11.069 1.00 25.23 C ANISOU 1159 C LEU A 315 2827 2932 3828 376 -985 190 C ATOM 1160 O LEU A 315 18.523 19.063 -10.203 1.00 26.75 O ANISOU 1160 O LEU A 315 3000 3194 3969 319 -834 251 O ATOM 1161 CB LEU A 315 20.618 17.426 -12.069 1.00 28.65 C ANISOU 1161 CB LEU A 315 3332 3444 4111 514 -1057 -33 C ATOM 1162 CG LEU A 315 21.443 18.647 -11.613 1.00 25.98 C ANISOU 1162 CG LEU A 315 2996 3236 3640 480 -861 -31 C ATOM 1163 CD1 LEU A 315 21.951 18.427 -10.190 1.00 24.92 C ANISOU 1163 CD1 LEU A 315 2824 3117 3527 416 -808 26 C ATOM 1164 CD2 LEU A 315 22.603 18.899 -12.563 1.00 24.60 C ANISOU 1164 CD2 LEU A 315 2862 3156 3329 566 -834 -146 C ATOM 1165 N ILE A 316 17.472 18.177 -11.984 1.00 24.30 N ANISOU 1165 N ILE A 316 2721 2745 3766 398 -1066 193 N ATOM 1166 CA ILE A 316 16.363 19.116 -11.893 1.00 23.16 C ANISOU 1166 CA ILE A 316 2557 2599 3643 344 -979 287 C ATOM 1167 C ILE A 316 15.627 18.884 -10.576 1.00 28.03 C ANISOU 1167 C ILE A 316 3099 3181 4368 266 -958 441 C ATOM 1168 O ILE A 316 15.331 19.830 -9.847 1.00 28.66 O ANISOU 1168 O ILE A 316 3160 3323 4406 219 -811 517 O ATOM 1169 CB ILE A 316 15.351 18.933 -13.057 1.00 28.48 C ANISOU 1169 CB ILE A 316 3251 3183 4388 379 -1100 275 C ATOM 1170 CG1 ILE A 316 16.035 19.107 -14.411 1.00 32.97 C ANISOU 1170 CG1 ILE A 316 3893 3791 4842 475 -1129 126 C ATOM 1171 CG2 ILE A 316 14.185 19.919 -12.917 1.00 30.44 C ANISOU 1171 CG2 ILE A 316 3474 3432 4661 321 -1005 380 C ATOM 1172 CD1 ILE A 316 15.090 18.943 -15.606 1.00 43.03 C ANISOU 1172 CD1 ILE A 316 5198 4978 6175 522 -1254 101 C ATOM 1173 N ALA A 317 15.347 17.619 -10.268 1.00 30.12 N ANISOU 1173 N ALA A 317 3322 3350 4772 260 -1110 490 N ATOM 1174 CA ALA A 317 14.636 17.268 -9.036 1.00 33.25 C ANISOU 1174 CA ALA A 317 3635 3717 5283 193 -1103 654 C ATOM 1175 C ALA A 317 15.370 17.802 -7.802 1.00 30.36 C ANISOU 1175 C ALA A 317 3255 3459 4821 162 -940 682 C ATOM 1176 O ALA A 317 14.760 18.309 -6.862 1.00 26.16 O ANISOU 1176 O ALA A 317 2677 2964 4300 119 -837 807 O ATOM 1177 CB ALA A 317 14.460 15.765 -8.934 1.00 34.15 C ANISOU 1177 CB ALA A 317 3705 3713 5556 194 -1304 691 C ATOM 1178 N ILE A 318 16.686 17.689 -7.815 1.00 28.09 N ANISOU 1178 N ILE A 318 3012 3225 4437 192 -922 566 N ATOM 1179 CA ILE A 318 17.485 18.193 -6.701 1.00 26.53 C ANISOU 1179 CA ILE A 318 2811 3123 4148 167 -781 579 C ATOM 1180 C ILE A 318 17.368 19.715 -6.605 1.00 23.83 C ANISOU 1180 C ILE A 318 2498 2868 3688 154 -608 585 C ATOM 1181 O ILE A 318 17.145 20.251 -5.526 1.00 26.71 O ANISOU 1181 O ILE A 318 2837 3280 4030 122 -502 672 O ATOM 1182 CB ILE A 318 18.938 17.754 -6.824 1.00 23.61 C ANISOU 1182 CB ILE A 318 2480 2788 3705 203 -805 454 C ATOM 1183 CG1 ILE A 318 19.066 16.291 -6.369 1.00 24.96 C ANISOU 1183 CG1 ILE A 318 2607 2881 3994 200 -952 482 C ATOM 1184 CG2 ILE A 318 19.861 18.660 -5.986 1.00 24.24 C ANISOU 1184 CG2 ILE A 318 2578 2975 3656 184 -643 438 C ATOM 1185 CD1 ILE A 318 20.385 15.671 -6.700 1.00 27.56 C ANISOU 1185 CD1 ILE A 318 2976 3227 4269 249 -1011 351 C ATOM 1186 N CYS A 319 17.508 20.392 -7.744 1.00 24.53 N ANISOU 1186 N CYS A 319 2640 2978 3703 185 -589 493 N ATOM 1187 CA CYS A 319 17.449 21.857 -7.787 1.00 28.12 C ANISOU 1187 CA CYS A 319 3125 3508 4050 173 -441 489 C ATOM 1188 C CYS A 319 16.128 22.454 -7.307 1.00 28.65 C ANISOU 1188 C CYS A 319 3159 3564 4164 139 -382 613 C ATOM 1189 O CYS A 319 16.130 23.550 -6.742 1.00 29.34 O ANISOU 1189 O CYS A 319 3261 3717 4170 123 -253 638 O ATOM 1190 CB CYS A 319 17.778 22.383 -9.188 1.00 26.26 C ANISOU 1190 CB CYS A 319 2944 3295 3740 215 -446 379 C ATOM 1191 SG CYS A 319 19.521 22.241 -9.653 1.00 31.83 S ANISOU 1191 SG CYS A 319 3690 4072 4333 264 -444 242 S ATOM 1192 N VAL A 320 15.008 21.746 -7.501 1.00 26.74 N ANISOU 1192 N VAL A 320 2871 3236 4053 130 -481 696 N ATOM 1193 CA VAL A 320 13.719 22.297 -7.092 1.00 24.79 C ANISOU 1193 CA VAL A 320 2584 2983 3852 103 -424 826 C ATOM 1194 C VAL A 320 13.191 21.728 -5.778 1.00 26.43 C ANISOU 1194 C VAL A 320 2714 3186 4143 78 -420 977 C ATOM 1195 O VAL A 320 12.096 22.077 -5.339 1.00 28.94 O ANISOU 1195 O VAL A 320 2985 3508 4505 64 -373 1105 O ATOM 1196 CB VAL A 320 12.648 22.147 -8.196 1.00 26.72 C ANISOU 1196 CB VAL A 320 2822 3145 4186 107 -517 844 C ATOM 1197 CG1 VAL A 320 13.168 22.739 -9.497 1.00 26.26 C ANISOU 1197 CG1 VAL A 320 2839 3104 4034 142 -514 700 C ATOM 1198 CG2 VAL A 320 12.274 20.664 -8.370 1.00 28.30 C ANISOU 1198 CG2 VAL A 320 2973 3233 4546 107 -701 887 C ATOM 1199 N ASP A 321 13.985 20.879 -5.133 1.00 26.46 N ANISOU 1199 N ASP A 321 2700 3190 4163 76 -462 967 N ATOM 1200 CA ASP A 321 13.572 20.262 -3.878 1.00 27.15 C ANISOU 1200 CA ASP A 321 2708 3278 4328 56 -462 1115 C ATOM 1201 C ASP A 321 13.745 21.211 -2.687 1.00 29.82 C ANISOU 1201 C ASP A 321 3053 3723 4553 63 -296 1161 C ATOM 1202 O ASP A 321 14.755 21.907 -2.591 1.00 25.60 O ANISOU 1202 O ASP A 321 2586 3251 3890 76 -217 1052 O ATOM 1203 CB ASP A 321 14.396 18.995 -3.643 1.00 30.71 C ANISOU 1203 CB ASP A 321 3141 3688 4838 54 -575 1082 C ATOM 1204 CG ASP A 321 13.872 18.181 -2.500 1.00 31.99 C ANISOU 1204 CG ASP A 321 3208 3836 5110 30 -605 1248 C ATOM 1205 OD1 ASP A 321 12.748 17.656 -2.632 1.00 33.07 O ANISOU 1205 OD1 ASP A 321 3273 3904 5388 11 -690 1375 O ATOM 1206 OD2 ASP A 321 14.566 18.078 -1.462 1.00 28.09 O ANISOU 1206 OD2 ASP A 321 2707 3402 4564 30 -545 1260 O ATOM 1207 N GLN A 322 12.775 21.224 -1.772 1.00 23.54 N ANISOU 1207 N GLN A 322 2187 2951 3806 60 -250 1327 N ATOM 1208 CA GLN A 322 12.830 22.099 -0.595 1.00 26.36 C ANISOU 1208 CA GLN A 322 2553 3412 4052 87 -101 1377 C ATOM 1209 C GLN A 322 14.079 21.848 0.279 1.00 23.23 C ANISOU 1209 C GLN A 322 2182 3061 3583 95 -76 1319 C ATOM 1210 O GLN A 322 14.590 22.778 0.906 1.00 28.58 O ANISOU 1210 O GLN A 322 2914 3815 4131 122 35 1276 O ATOM 1211 CB GLN A 322 11.573 21.932 0.264 1.00 29.59 C ANISOU 1211 CB GLN A 322 2866 3844 4533 97 -69 1583 C ATOM 1212 CG GLN A 322 11.339 20.486 0.672 1.00 39.21 C ANISOU 1212 CG GLN A 322 3986 5009 5904 71 -184 1704 C ATOM 1213 CD GLN A 322 10.014 20.273 1.397 1.00 53.75 C ANISOU 1213 CD GLN A 322 5713 6874 7837 80 -161 1934 C ATOM 1214 OE1 GLN A 322 9.571 21.120 2.179 1.00 50.51 O ANISOU 1214 OE1 GLN A 322 5297 6560 7334 125 -26 2011 O ATOM 1215 NE2 GLN A 322 9.384 19.131 1.145 1.00 53.63 N ANISOU 1215 NE2 GLN A 322 5604 6770 8004 41 -300 2049 N ATOM 1216 N ASN A 323 14.548 20.605 0.321 1.00 26.12 N ANISOU 1216 N ASN A 323 2512 3375 4038 74 -186 1317 N ATOM 1217 CA ASN A 323 15.774 20.255 1.053 1.00 23.33 C ANISOU 1217 CA ASN A 323 2181 3055 3628 78 -176 1256 C ATOM 1218 C ASN A 323 17.002 20.330 0.182 1.00 24.90 C ANISOU 1218 C ASN A 323 2459 3237 3765 74 -211 1072 C ATOM 1219 O ASN A 323 17.997 20.982 0.532 1.00 22.81 O ANISOU 1219 O ASN A 323 2254 3031 3383 86 -135 985 O ATOM 1220 CB ASN A 323 15.687 18.827 1.587 1.00 25.39 C ANISOU 1220 CB ASN A 323 2357 3268 4020 57 -282 1353 C ATOM 1221 CG ASN A 323 14.449 18.600 2.403 1.00 35.58 C ANISOU 1221 CG ASN A 323 3550 4578 5393 60 -261 1562 C ATOM 1222 OD1 ASN A 323 14.067 19.456 3.194 1.00 33.49 O ANISOU 1222 OD1 ASN A 323 3286 4400 5041 95 -132 1631 O ATOM 1223 ND2 ASN A 323 13.798 17.451 2.207 1.00 43.78 N ANISOU 1223 ND2 ASN A 323 4499 5534 6602 29 -393 1670 N ATOM 1224 N ALA A 324 16.941 19.626 -0.944 1.00 21.22 N ANISOU 1224 N ALA A 324 1989 2692 3381 65 -334 1018 N ATOM 1225 CA ALA A 324 18.132 19.378 -1.750 1.00 26.10 C ANISOU 1225 CA ALA A 324 2665 3296 3955 75 -390 858 C ATOM 1226 C ALA A 324 18.691 20.627 -2.414 1.00 26.01 C ANISOU 1226 C ALA A 324 2731 3340 3810 91 -298 744 C ATOM 1227 O ALA A 324 19.877 20.671 -2.750 1.00 22.58 O ANISOU 1227 O ALA A 324 2342 2932 3306 104 -299 628 O ATOM 1228 CB ALA A 324 17.850 18.297 -2.799 1.00 21.71 C ANISOU 1228 CB ALA A 324 2091 2640 3516 80 -556 830 C ATOM 1229 N ASN A 325 17.855 21.647 -2.619 1.00 21.10 N ANISOU 1229 N ASN A 325 2120 2739 3157 91 -222 783 N ATOM 1230 CA ASN A 325 18.367 22.839 -3.274 1.00 19.36 C ANISOU 1230 CA ASN A 325 1968 2566 2821 102 -145 684 C ATOM 1231 C ASN A 325 19.523 23.396 -2.433 1.00 19.37 C ANISOU 1231 C ASN A 325 2006 2636 2717 102 -62 637 C ATOM 1232 O ASN A 325 20.439 23.993 -2.967 1.00 18.41 O ANISOU 1232 O ASN A 325 1932 2548 2515 108 -35 539 O ATOM 1233 CB ASN A 325 17.285 23.913 -3.521 1.00 18.31 C ANISOU 1233 CB ASN A 325 1842 2445 2668 101 -74 735 C ATOM 1234 CG ASN A 325 16.858 24.642 -2.239 1.00 23.66 C ANISOU 1234 CG ASN A 325 2513 3177 3300 105 34 827 C ATOM 1235 OD1 ASN A 325 15.909 24.241 -1.553 1.00 25.60 O ANISOU 1235 OD1 ASN A 325 2700 3413 3614 107 33 954 O ATOM 1236 ND2 ASN A 325 17.574 25.699 -1.903 1.00 16.56 N ANISOU 1236 ND2 ASN A 325 1671 2336 2286 113 121 768 N ATOM 1237 N HIS A 326 19.469 23.194 -1.119 1.00 17.84 N ANISOU 1237 N HIS A 326 1787 2464 2528 100 -28 715 N ATOM 1238 CA HIS A 326 20.521 23.720 -0.239 1.00 21.96 C ANISOU 1238 CA HIS A 326 2348 3042 2955 105 41 674 C ATOM 1239 C HIS A 326 21.855 22.994 -0.424 1.00 20.73 C ANISOU 1239 C HIS A 326 2202 2881 2793 99 -17 583 C ATOM 1240 O HIS A 326 22.926 23.532 -0.114 1.00 18.13 O ANISOU 1240 O HIS A 326 1914 2593 2383 99 27 520 O ATOM 1241 CB HIS A 326 20.075 23.649 1.224 1.00 18.32 C ANISOU 1241 CB HIS A 326 1858 2609 2493 118 90 784 C ATOM 1242 CG HIS A 326 18.901 24.526 1.523 1.00 19.01 C ANISOU 1242 CG HIS A 326 1942 2722 2558 139 164 870 C ATOM 1243 ND1 HIS A 326 19.004 25.898 1.641 1.00 21.25 N ANISOU 1243 ND1 HIS A 326 2289 3048 2736 159 248 830 N ATOM 1244 CD2 HIS A 326 17.591 24.228 1.697 1.00 21.67 C ANISOU 1244 CD2 HIS A 326 2218 3047 2967 147 161 997 C ATOM 1245 CE1 HIS A 326 17.806 26.404 1.882 1.00 21.01 C ANISOU 1245 CE1 HIS A 326 2242 3034 2707 184 297 921 C ATOM 1246 NE2 HIS A 326 16.932 25.412 1.921 1.00 21.40 N ANISOU 1246 NE2 HIS A 326 2213 3055 2862 177 251 1027 N ATOM 1247 N VAL A 327 21.800 21.767 -0.920 1.00 16.95 N ANISOU 1247 N VAL A 327 1686 2349 2404 97 -124 577 N ATOM 1248 CA VAL A 327 23.049 21.080 -1.258 1.00 15.25 C ANISOU 1248 CA VAL A 327 1484 2132 2179 104 -184 480 C ATOM 1249 C VAL A 327 23.708 21.791 -2.426 1.00 17.43 C ANISOU 1249 C VAL A 327 1807 2438 2379 121 -165 375 C ATOM 1250 O VAL A 327 24.917 22.012 -2.420 1.00 16.65 O ANISOU 1250 O VAL A 327 1733 2382 2212 125 -141 305 O ATOM 1251 CB VAL A 327 22.825 19.585 -1.612 1.00 18.48 C ANISOU 1251 CB VAL A 327 1849 2469 2704 109 -322 489 C ATOM 1252 CG1 VAL A 327 24.137 18.941 -2.145 1.00 17.37 C ANISOU 1252 CG1 VAL A 327 1731 2332 2538 133 -387 372 C ATOM 1253 CG2 VAL A 327 22.305 18.815 -0.388 1.00 18.30 C ANISOU 1253 CG2 VAL A 327 1767 2422 2764 88 -345 608 C ATOM 1254 N ILE A 328 22.928 22.130 -3.450 1.00 15.45 N ANISOU 1254 N ILE A 328 1561 2168 2140 132 -177 370 N ATOM 1255 CA ILE A 328 23.533 22.816 -4.598 1.00 18.27 C ANISOU 1255 CA ILE A 328 1957 2564 2421 154 -156 280 C ATOM 1256 C ILE A 328 24.081 24.183 -4.186 1.00 16.49 C ANISOU 1256 C ILE A 328 1764 2402 2100 134 -43 274 C ATOM 1257 O ILE A 328 25.161 24.571 -4.607 1.00 15.95 O ANISOU 1257 O ILE A 328 1715 2381 1966 143 -22 210 O ATOM 1258 CB ILE A 328 22.551 22.970 -5.774 1.00 20.17 C ANISOU 1258 CB ILE A 328 2201 2772 2692 172 -190 278 C ATOM 1259 CG1 ILE A 328 22.038 21.589 -6.216 1.00 20.03 C ANISOU 1259 CG1 ILE A 328 2156 2676 2780 195 -328 280 C ATOM 1260 CG2 ILE A 328 23.219 23.716 -6.940 1.00 15.89 C ANISOU 1260 CG2 ILE A 328 1692 2283 2061 200 -160 194 C ATOM 1261 CD1 ILE A 328 23.156 20.576 -6.500 1.00 21.14 C ANISOU 1261 CD1 ILE A 328 2300 2816 2915 233 -412 195 C ATOM 1262 N GLN A 329 23.335 24.912 -3.355 1.00 15.65 N ANISOU 1262 N GLN A 329 1661 2297 1987 114 24 346 N ATOM 1263 CA GLN A 329 23.829 26.199 -2.860 1.00 15.17 C ANISOU 1263 CA GLN A 329 1638 2283 1842 101 111 338 C ATOM 1264 C GLN A 329 25.101 26.053 -2.034 1.00 17.68 C ANISOU 1264 C GLN A 329 1966 2627 2124 94 118 309 C ATOM 1265 O GLN A 329 25.972 26.919 -2.086 1.00 16.08 O ANISOU 1265 O GLN A 329 1792 2460 1859 85 156 271 O ATOM 1266 CB GLN A 329 22.766 26.917 -2.022 1.00 16.30 C ANISOU 1266 CB GLN A 329 1789 2423 1980 98 171 418 C ATOM 1267 CG GLN A 329 21.484 27.227 -2.798 1.00 16.74 C ANISOU 1267 CG GLN A 329 1836 2455 2069 102 173 454 C ATOM 1268 CD GLN A 329 20.630 28.226 -2.064 1.00 26.40 C ANISOU 1268 CD GLN A 329 3076 3693 3260 108 247 519 C ATOM 1269 OE1 GLN A 329 20.982 29.398 -1.979 1.00 24.97 O ANISOU 1269 OE1 GLN A 329 2941 3540 3007 107 298 489 O ATOM 1270 NE2 GLN A 329 19.501 27.772 -1.520 1.00 21.74 N ANISOU 1270 NE2 GLN A 329 2449 3085 2725 119 246 614 N ATOM 1271 N LYS A 330 25.213 24.976 -1.259 1.00 16.49 N ANISOU 1271 N LYS A 330 1789 2456 2020 95 77 333 N ATOM 1272 CA LYS A 330 26.468 24.728 -0.523 1.00 15.37 C ANISOU 1272 CA LYS A 330 1656 2334 1848 89 76 300 C ATOM 1273 C LYS A 330 27.645 24.431 -1.466 1.00 16.13 C ANISOU 1273 C LYS A 330 1751 2453 1924 96 40 217 C ATOM 1274 O LYS A 330 28.770 24.927 -1.282 1.00 17.40 O ANISOU 1274 O LYS A 330 1929 2650 2034 87 66 182 O ATOM 1275 CB LYS A 330 26.291 23.579 0.477 1.00 14.84 C ANISOU 1275 CB LYS A 330 1557 2242 1841 89 36 349 C ATOM 1276 CG LYS A 330 27.559 23.242 1.287 1.00 17.75 C ANISOU 1276 CG LYS A 330 1933 2627 2184 82 30 316 C ATOM 1277 CD LYS A 330 27.867 24.393 2.254 1.00 23.68 C ANISOU 1277 CD LYS A 330 2730 3407 2862 79 103 328 C ATOM 1278 CE LYS A 330 26.822 24.492 3.361 1.00 28.10 C ANISOU 1278 CE LYS A 330 3287 3965 3427 96 138 418 C ATOM 1279 NZ LYS A 330 27.180 25.603 4.315 1.00 26.60 N ANISOU 1279 NZ LYS A 330 3153 3799 3155 111 194 415 N ATOM 1280 N VAL A 331 27.401 23.606 -2.476 1.00 14.32 N ANISOU 1280 N VAL A 331 1500 2205 1737 120 -26 188 N ATOM 1281 CA VAL A 331 28.447 23.306 -3.447 1.00 13.66 C ANISOU 1281 CA VAL A 331 1414 2154 1621 149 -59 111 C ATOM 1282 C VAL A 331 28.974 24.605 -4.036 1.00 14.76 C ANISOU 1282 C VAL A 331 1572 2351 1684 145 10 92 C ATOM 1283 O VAL A 331 30.186 24.846 -4.100 1.00 17.07 O ANISOU 1283 O VAL A 331 1863 2691 1931 146 27 62 O ATOM 1284 CB VAL A 331 27.907 22.434 -4.588 1.00 15.53 C ANISOU 1284 CB VAL A 331 1638 2361 1902 193 -143 78 C ATOM 1285 CG1 VAL A 331 28.913 22.358 -5.757 1.00 19.33 C ANISOU 1285 CG1 VAL A 331 2123 2899 2324 245 -162 -1 C ATOM 1286 CG2 VAL A 331 27.566 21.031 -4.079 1.00 16.71 C ANISOU 1286 CG2 VAL A 331 1761 2446 2141 197 -237 95 C ATOM 1287 N VAL A 332 28.052 25.448 -4.472 1.00 13.50 N ANISOU 1287 N VAL A 332 1426 2186 1518 138 46 119 N ATOM 1288 CA VAL A 332 28.422 26.740 -5.057 1.00 14.14 C ANISOU 1288 CA VAL A 332 1521 2315 1537 128 104 112 C ATOM 1289 C VAL A 332 29.281 27.581 -4.096 1.00 13.48 C ANISOU 1289 C VAL A 332 1453 2251 1417 92 150 128 C ATOM 1290 O VAL A 332 30.211 28.284 -4.517 1.00 16.00 O ANISOU 1290 O VAL A 332 1768 2617 1695 85 173 117 O ATOM 1291 CB VAL A 332 27.134 27.501 -5.492 1.00 17.14 C ANISOU 1291 CB VAL A 332 1915 2673 1923 122 133 145 C ATOM 1292 CG1 VAL A 332 27.428 28.935 -5.853 1.00 22.00 C ANISOU 1292 CG1 VAL A 332 2546 3328 2485 101 192 152 C ATOM 1293 CG2 VAL A 332 26.498 26.761 -6.672 1.00 20.62 C ANISOU 1293 CG2 VAL A 332 2342 3098 2394 163 76 119 C ATOM 1294 N ALA A 333 28.973 27.503 -2.814 1.00 18.49 N ANISOU 1294 N ALA A 333 2104 2851 2070 73 158 160 N ATOM 1295 CA ALA A 333 29.652 28.324 -1.811 1.00 18.58 C ANISOU 1295 CA ALA A 333 2143 2868 2049 48 189 172 C ATOM 1296 C ALA A 333 31.063 27.842 -1.487 1.00 19.82 C ANISOU 1296 C ALA A 333 2288 3046 2199 42 165 143 C ATOM 1297 O ALA A 333 31.975 28.654 -1.308 1.00 21.89 O ANISOU 1297 O ALA A 333 2560 3326 2432 21 179 142 O ATOM 1298 CB ALA A 333 28.824 28.388 -0.536 1.00 20.12 C ANISOU 1298 CB ALA A 333 2364 3028 2253 49 206 216 C ATOM 1299 N VAL A 334 31.254 26.529 -1.391 1.00 16.24 N ANISOU 1299 N VAL A 334 1808 2584 1777 59 122 124 N ATOM 1300 CA VAL A 334 32.512 26.024 -0.820 1.00 19.83 C ANISOU 1300 CA VAL A 334 2254 3052 2228 53 101 102 C ATOM 1301 C VAL A 334 33.407 25.173 -1.740 1.00 20.41 C ANISOU 1301 C VAL A 334 2291 3164 2300 82 63 55 C ATOM 1302 O VAL A 334 34.436 24.658 -1.292 1.00 18.69 O ANISOU 1302 O VAL A 334 2062 2957 2083 80 43 37 O ATOM 1303 CB VAL A 334 32.249 25.263 0.495 1.00 20.67 C ANISOU 1303 CB VAL A 334 2368 3119 2366 48 83 123 C ATOM 1304 CG1 VAL A 334 31.341 26.122 1.435 1.00 18.56 C ANISOU 1304 CG1 VAL A 334 2139 2828 2084 41 125 173 C ATOM 1305 CG2 VAL A 334 31.605 23.911 0.216 1.00 15.85 C ANISOU 1305 CG2 VAL A 334 1726 2483 1812 71 30 122 C ATOM 1306 N ILE A 335 33.033 25.044 -3.012 1.00 16.20 N ANISOU 1306 N ILE A 335 1742 2653 1761 117 52 35 N ATOM 1307 CA ILE A 335 33.782 24.201 -3.966 1.00 18.62 C ANISOU 1307 CA ILE A 335 2019 3003 2053 170 12 -15 C ATOM 1308 C ILE A 335 34.216 25.033 -5.169 1.00 18.91 C ANISOU 1308 C ILE A 335 2039 3111 2034 194 48 -16 C ATOM 1309 O ILE A 335 33.424 25.820 -5.677 1.00 18.42 O ANISOU 1309 O ILE A 335 1989 3048 1963 187 78 4 O ATOM 1310 CB ILE A 335 32.905 23.039 -4.483 1.00 17.23 C ANISOU 1310 CB ILE A 335 1840 2787 1920 214 -59 -44 C ATOM 1311 CG1 ILE A 335 32.371 22.198 -3.312 1.00 19.23 C ANISOU 1311 CG1 ILE A 335 2097 2970 2241 187 -99 -21 C ATOM 1312 CG2 ILE A 335 33.692 22.154 -5.492 1.00 20.33 C ANISOU 1312 CG2 ILE A 335 2213 3224 2287 289 -113 -108 C ATOM 1313 CD1 ILE A 335 33.478 21.464 -2.509 1.00 14.88 C ANISOU 1313 CD1 ILE A 335 1535 2423 1697 181 -125 -41 C ATOM 1314 N PRO A 336 35.461 24.849 -5.657 1.00 19.55 N ANISOU 1314 N PRO A 336 2088 3263 2077 227 47 -34 N ATOM 1315 CA PRO A 336 35.821 25.696 -6.804 1.00 17.01 C ANISOU 1315 CA PRO A 336 1740 3021 1701 253 89 -16 C ATOM 1316 C PRO A 336 34.982 25.402 -8.051 1.00 21.79 C ANISOU 1316 C PRO A 336 2350 3641 2287 320 69 -47 C ATOM 1317 O PRO A 336 34.564 24.270 -8.274 1.00 19.71 O ANISOU 1317 O PRO A 336 2099 3346 2043 371 4 -99 O ATOM 1318 CB PRO A 336 37.298 25.343 -7.069 1.00 19.46 C ANISOU 1318 CB PRO A 336 2006 3412 1975 291 88 -21 C ATOM 1319 CG PRO A 336 37.808 24.783 -5.747 1.00 20.19 C ANISOU 1319 CG PRO A 336 2109 3454 2108 248 62 -28 C ATOM 1320 CD PRO A 336 36.609 24.050 -5.161 1.00 16.21 C ANISOU 1320 CD PRO A 336 1646 2858 1655 238 20 -56 C ATOM 1321 N LEU A 337 34.786 26.428 -8.870 1.00 18.41 N ANISOU 1321 N LEU A 337 1912 3260 1825 322 116 -15 N ATOM 1322 CA LEU A 337 33.858 26.378 -9.996 1.00 15.93 C ANISOU 1322 CA LEU A 337 1610 2952 1492 376 103 -38 C ATOM 1323 C LEU A 337 34.127 25.223 -10.964 1.00 17.35 C ANISOU 1323 C LEU A 337 1782 3174 1636 488 44 -104 C ATOM 1324 O LEU A 337 33.195 24.648 -11.533 1.00 21.89 O ANISOU 1324 O LEU A 337 2384 3707 2225 535 -11 -147 O ATOM 1325 CB LEU A 337 33.901 27.702 -10.761 1.00 20.02 C ANISOU 1325 CB LEU A 337 2106 3532 1969 364 167 14 C ATOM 1326 CG LEU A 337 33.238 27.729 -12.149 1.00 21.10 C ANISOU 1326 CG LEU A 337 2245 3706 2065 437 162 -7 C ATOM 1327 CD1 LEU A 337 31.736 27.391 -12.101 1.00 17.49 C ANISOU 1327 CD1 LEU A 337 1836 3151 1659 428 120 -36 C ATOM 1328 CD2 LEU A 337 33.453 29.103 -12.777 1.00 22.87 C ANISOU 1328 CD2 LEU A 337 2437 3999 2252 414 230 60 C ATOM 1329 N LYS A 338 35.392 24.888 -11.176 1.00 16.92 N ANISOU 1329 N LYS A 338 1692 3202 1535 538 48 -112 N ATOM 1330 CA LYS A 338 35.702 23.885 -12.205 1.00 20.40 C ANISOU 1330 CA LYS A 338 2129 3700 1922 667 -8 -179 C ATOM 1331 C LYS A 338 34.941 22.587 -11.912 1.00 24.09 C ANISOU 1331 C LYS A 338 2640 4064 2449 692 -113 -250 C ATOM 1332 O LYS A 338 34.438 21.927 -12.820 1.00 26.20 O ANISOU 1332 O LYS A 338 2931 4323 2699 785 -182 -309 O ATOM 1333 CB LYS A 338 37.215 23.621 -12.301 1.00 21.16 C ANISOU 1333 CB LYS A 338 2178 3900 1962 719 11 -173 C ATOM 1334 CG LYS A 338 37.601 22.534 -13.331 1.00 26.10 C ANISOU 1334 CG LYS A 338 2805 4593 2519 874 -51 -249 C ATOM 1335 CD LYS A 338 37.102 22.878 -14.737 1.00 26.22 C ANISOU 1335 CD LYS A 338 2824 4674 2463 969 -42 -259 C ATOM 1336 CE LYS A 338 37.383 21.746 -15.748 1.00 27.87 C ANISOU 1336 CE LYS A 338 3050 4941 2597 1143 -120 -349 C ATOM 1337 NZ LYS A 338 36.682 21.987 -17.041 1.00 22.54 N ANISOU 1337 NZ LYS A 338 2397 4305 1861 1238 -131 -372 N ATOM 1338 N ASN A 339 34.820 22.255 -10.632 1.00 19.85 N ANISOU 1338 N ASN A 339 2113 3443 1986 609 -131 -238 N ATOM 1339 CA ASN A 339 34.086 21.060 -10.204 1.00 21.55 C ANISOU 1339 CA ASN A 339 2357 3553 2276 616 -232 -282 C ATOM 1340 C ASN A 339 32.574 21.069 -10.458 1.00 24.77 C ANISOU 1340 C ASN A 339 2794 3876 2740 601 -272 -278 C ATOM 1341 O ASN A 339 31.969 20.013 -10.640 1.00 24.97 O ANISOU 1341 O ASN A 339 2839 3830 2819 643 -380 -320 O ATOM 1342 CB ASN A 339 34.334 20.811 -8.716 1.00 23.13 C ANISOU 1342 CB ASN A 339 2552 3697 2539 528 -229 -253 C ATOM 1343 CG ASN A 339 35.797 20.643 -8.402 1.00 23.81 C ANISOU 1343 CG ASN A 339 2611 3851 2584 541 -207 -260 C ATOM 1344 OD1 ASN A 339 36.371 19.581 -8.622 1.00 22.23 O ANISOU 1344 OD1 ASN A 339 2407 3664 2375 611 -275 -317 O ATOM 1345 ND2 ASN A 339 36.419 21.702 -7.892 1.00 24.56 N ANISOU 1345 ND2 ASN A 339 2687 3988 2658 475 -119 -202 N ATOM 1346 N TRP A 340 31.954 22.243 -10.444 1.00 19.58 N ANISOU 1346 N TRP A 340 2139 3219 2080 540 -195 -222 N ATOM 1347 CA TRP A 340 30.513 22.308 -10.637 1.00 19.86 C ANISOU 1347 CA TRP A 340 2198 3176 2171 522 -226 -207 C ATOM 1348 C TRP A 340 30.110 23.073 -11.887 1.00 20.73 C ANISOU 1348 C TRP A 340 2317 3334 2227 565 -195 -212 C ATOM 1349 O TRP A 340 28.940 23.407 -12.075 1.00 18.94 O ANISOU 1349 O TRP A 340 2107 3052 2039 540 -200 -189 O ATOM 1350 CB TRP A 340 29.787 22.841 -9.388 1.00 18.49 C ANISOU 1350 CB TRP A 340 2026 2937 2061 415 -179 -135 C ATOM 1351 CG TRP A 340 30.282 24.148 -8.831 1.00 18.10 C ANISOU 1351 CG TRP A 340 1971 2937 1970 351 -71 -85 C ATOM 1352 CD1 TRP A 340 31.269 24.322 -7.890 1.00 17.35 C ANISOU 1352 CD1 TRP A 340 1864 2865 1862 311 -35 -68 C ATOM 1353 CD2 TRP A 340 29.784 25.455 -9.136 1.00 19.21 C ANISOU 1353 CD2 TRP A 340 2119 3096 2085 317 1 -44 C ATOM 1354 NE1 TRP A 340 31.423 25.661 -7.613 1.00 18.76 N ANISOU 1354 NE1 TRP A 340 2046 3072 2013 258 45 -21 N ATOM 1355 CE2 TRP A 340 30.520 26.375 -8.361 1.00 20.30 C ANISOU 1355 CE2 TRP A 340 2250 3264 2198 260 69 -6 C ATOM 1356 CE3 TRP A 340 28.785 25.938 -9.994 1.00 20.71 C ANISOU 1356 CE3 TRP A 340 2321 3275 2273 330 6 -38 C ATOM 1357 CZ2 TRP A 340 30.290 27.750 -8.416 1.00 19.76 C ANISOU 1357 CZ2 TRP A 340 2189 3212 2108 217 134 38 C ATOM 1358 CZ3 TRP A 340 28.563 27.308 -10.047 1.00 21.33 C ANISOU 1358 CZ3 TRP A 340 2403 3376 2324 285 83 7 C ATOM 1359 CH2 TRP A 340 29.311 28.195 -9.263 1.00 23.61 C ANISOU 1359 CH2 TRP A 340 2687 3692 2593 230 143 43 C ATOM 1360 N GLU A 341 31.075 23.321 -12.768 1.00 23.03 N ANISOU 1360 N GLU A 341 2591 3733 2426 637 -164 -236 N ATOM 1361 CA GLU A 341 30.777 24.011 -14.005 1.00 26.92 C ANISOU 1361 CA GLU A 341 3087 4284 2857 689 -135 -237 C ATOM 1362 C GLU A 341 29.684 23.268 -14.775 1.00 20.48 C ANISOU 1362 C GLU A 341 2309 3398 2074 755 -236 -290 C ATOM 1363 O GLU A 341 28.861 23.889 -15.448 1.00 25.87 O ANISOU 1363 O GLU A 341 3006 4074 2750 757 -220 -277 O ATOM 1364 CB GLU A 341 32.051 24.156 -14.870 1.00 25.39 C ANISOU 1364 CB GLU A 341 2861 4230 2557 780 -97 -249 C ATOM 1365 CG GLU A 341 31.892 25.206 -15.956 1.00 34.35 C ANISOU 1365 CG GLU A 341 3982 5446 3623 810 -33 -217 C ATOM 1366 CD GLU A 341 33.145 25.387 -16.797 1.00 43.92 C ANISOU 1366 CD GLU A 341 5149 6811 4728 904 13 -206 C ATOM 1367 OE1 GLU A 341 34.035 24.517 -16.720 1.00 40.05 O ANISOU 1367 OE1 GLU A 341 4647 6361 4209 971 -23 -245 O ATOM 1368 OE2 GLU A 341 33.224 26.399 -17.530 1.00 49.72 O ANISOU 1368 OE2 GLU A 341 5854 7629 5410 911 83 -152 O ATOM 1369 N PHE A 342 29.673 21.942 -14.675 1.00 20.62 N ANISOU 1369 N PHE A 342 2345 3358 2133 809 -351 -350 N ATOM 1370 CA PHE A 342 28.638 21.143 -15.323 1.00 23.65 C ANISOU 1370 CA PHE A 342 2766 3653 2567 869 -475 -399 C ATOM 1371 C PHE A 342 27.221 21.534 -14.893 1.00 27.39 C ANISOU 1371 C PHE A 342 3248 4023 3138 774 -475 -340 C ATOM 1372 O PHE A 342 26.276 21.396 -15.652 1.00 22.67 O ANISOU 1372 O PHE A 342 2675 3372 2567 811 -541 -358 O ATOM 1373 CB PHE A 342 28.871 19.639 -15.123 1.00 25.10 C ANISOU 1373 CB PHE A 342 2965 3774 2800 928 -615 -465 C ATOM 1374 CG PHE A 342 28.477 19.120 -13.763 1.00 26.98 C ANISOU 1374 CG PHE A 342 3187 3907 3157 824 -648 -418 C ATOM 1375 CD1 PHE A 342 27.202 18.618 -13.537 1.00 25.29 C ANISOU 1375 CD1 PHE A 342 2982 3565 3061 786 -741 -393 C ATOM 1376 CD2 PHE A 342 29.393 19.095 -12.726 1.00 29.12 C ANISOU 1376 CD2 PHE A 342 3430 4210 3423 769 -591 -394 C ATOM 1377 CE1 PHE A 342 26.844 18.122 -12.293 1.00 25.34 C ANISOU 1377 CE1 PHE A 342 2964 3489 3175 698 -768 -334 C ATOM 1378 CE2 PHE A 342 29.051 18.597 -11.476 1.00 29.64 C ANISOU 1378 CE2 PHE A 342 3480 4190 3590 683 -619 -347 C ATOM 1379 CZ PHE A 342 27.774 18.114 -11.254 1.00 26.57 C ANISOU 1379 CZ PHE A 342 3095 3685 3315 649 -704 -313 C ATOM 1380 N ILE A 343 27.067 22.010 -13.671 1.00 21.77 N ANISOU 1380 N ILE A 343 2513 3283 2475 659 -404 -267 N ATOM 1381 CA ILE A 343 25.744 22.446 -13.219 1.00 16.85 C ANISOU 1381 CA ILE A 343 1891 2577 1933 578 -391 -200 C ATOM 1382 C ILE A 343 25.334 23.721 -13.939 1.00 19.83 C ANISOU 1382 C ILE A 343 2277 3003 2256 568 -305 -176 C ATOM 1383 O ILE A 343 24.180 23.886 -14.323 1.00 24.09 O ANISOU 1383 O ILE A 343 2829 3482 2840 559 -332 -157 O ATOM 1384 CB ILE A 343 25.706 22.659 -11.697 1.00 18.91 C ANISOU 1384 CB ILE A 343 2131 2810 2246 475 -332 -128 C ATOM 1385 CG1 ILE A 343 26.045 21.351 -10.985 1.00 22.96 C ANISOU 1385 CG1 ILE A 343 2631 3270 2821 482 -423 -144 C ATOM 1386 CG2 ILE A 343 24.308 23.152 -11.260 1.00 19.41 C ANISOU 1386 CG2 ILE A 343 2191 2803 2380 407 -310 -50 C ATOM 1387 CD1 ILE A 343 26.127 21.467 -9.458 1.00 24.40 C ANISOU 1387 CD1 ILE A 343 2792 3435 3044 395 -368 -75 C ATOM 1388 N VAL A 344 26.283 24.629 -14.122 1.00 21.65 N ANISOU 1388 N VAL A 344 2493 3337 2393 567 -206 -170 N ATOM 1389 CA VAL A 344 26.009 25.853 -14.867 1.00 22.26 C ANISOU 1389 CA VAL A 344 2573 3468 2418 560 -129 -145 C ATOM 1390 C VAL A 344 25.499 25.541 -16.276 1.00 26.44 C ANISOU 1390 C VAL A 344 3126 4000 2920 657 -195 -197 C ATOM 1391 O VAL A 344 24.488 26.097 -16.732 1.00 24.38 O ANISOU 1391 O VAL A 344 2880 3705 2679 639 -187 -176 O ATOM 1392 CB VAL A 344 27.257 26.732 -14.957 1.00 26.21 C ANISOU 1392 CB VAL A 344 3045 4085 2831 556 -34 -124 C ATOM 1393 CG1 VAL A 344 26.959 27.998 -15.770 1.00 31.35 C ANISOU 1393 CG1 VAL A 344 3690 4788 3433 547 37 -90 C ATOM 1394 CG2 VAL A 344 27.751 27.085 -13.545 1.00 23.93 C ANISOU 1394 CG2 VAL A 344 2740 3782 2571 463 19 -77 C ATOM 1395 N ASP A 345 26.203 24.661 -16.973 1.00 27.91 N ANISOU 1395 N ASP A 345 3320 4228 3057 767 -264 -268 N ATOM 1396 CA ASP A 345 25.803 24.293 -18.329 1.00 31.37 C ANISOU 1396 CA ASP A 345 3789 4672 3457 882 -340 -330 C ATOM 1397 C ASP A 345 24.483 23.510 -18.334 1.00 29.52 C ANISOU 1397 C ASP A 345 3589 4295 3333 878 -465 -348 C ATOM 1398 O ASP A 345 23.645 23.704 -19.210 1.00 31.09 O ANISOU 1398 O ASP A 345 3813 4465 3533 914 -501 -362 O ATOM 1399 CB ASP A 345 26.929 23.528 -19.024 1.00 35.82 C ANISOU 1399 CB ASP A 345 4356 5323 3930 1018 -387 -405 C ATOM 1400 CG ASP A 345 28.162 24.406 -19.261 1.00 47.66 C ANISOU 1400 CG ASP A 345 5811 6979 5318 1033 -261 -369 C ATOM 1401 OD1 ASP A 345 27.989 25.582 -19.656 1.00 50.34 O ANISOU 1401 OD1 ASP A 345 6133 7374 5621 997 -170 -314 O ATOM 1402 OD2 ASP A 345 29.295 23.926 -19.056 1.00 50.57 O ANISOU 1402 OD2 ASP A 345 6159 7414 5643 1078 -259 -388 O ATOM 1403 N PHE A 346 24.294 22.645 -17.347 1.00 24.45 N ANISOU 1403 N PHE A 346 2941 3562 2789 830 -532 -338 N ATOM 1404 CA PHE A 346 23.013 21.951 -17.189 1.00 28.71 C ANISOU 1404 CA PHE A 346 3494 3959 3455 806 -649 -324 C ATOM 1405 C PHE A 346 21.839 22.925 -17.048 1.00 30.91 C ANISOU 1405 C PHE A 346 3766 4198 3780 718 -582 -246 C ATOM 1406 O PHE A 346 20.820 22.807 -17.740 1.00 25.35 O ANISOU 1406 O PHE A 346 3083 3425 3124 742 -656 -251 O ATOM 1407 CB PHE A 346 23.060 21.021 -15.977 1.00 28.28 C ANISOU 1407 CB PHE A 346 3417 3828 3500 751 -708 -297 C ATOM 1408 CG PHE A 346 21.803 20.215 -15.779 1.00 28.29 C ANISOU 1408 CG PHE A 346 3418 3684 3646 725 -839 -264 C ATOM 1409 CD1 PHE A 346 21.711 18.918 -16.271 1.00 25.85 C ANISOU 1409 CD1 PHE A 346 3133 3294 3396 807 -1021 -330 C ATOM 1410 CD2 PHE A 346 20.714 20.750 -15.095 1.00 26.90 C ANISOU 1410 CD2 PHE A 346 3214 3452 3553 622 -790 -161 C ATOM 1411 CE1 PHE A 346 20.550 18.160 -16.086 1.00 25.48 C ANISOU 1411 CE1 PHE A 346 3077 3103 3501 777 -1158 -285 C ATOM 1412 CE2 PHE A 346 19.551 20.003 -14.913 1.00 27.08 C ANISOU 1412 CE2 PHE A 346 3223 3346 3719 597 -912 -110 C ATOM 1413 CZ PHE A 346 19.477 18.700 -15.403 1.00 32.44 C ANISOU 1413 CZ PHE A 346 3920 3936 4469 669 -1100 -167 C ATOM 1414 N VAL A 347 21.982 23.873 -16.130 1.00 22.80 N ANISOU 1414 N VAL A 347 2711 3211 2742 621 -450 -174 N ATOM 1415 CA VAL A 347 20.937 24.858 -15.856 1.00 21.96 C ANISOU 1415 CA VAL A 347 2598 3075 2672 540 -378 -98 C ATOM 1416 C VAL A 347 20.720 25.759 -17.064 1.00 26.12 C ANISOU 1416 C VAL A 347 3146 3654 3126 578 -337 -119 C ATOM 1417 O VAL A 347 19.610 26.204 -17.318 1.00 26.93 O ANISOU 1417 O VAL A 347 3255 3706 3272 549 -336 -83 O ATOM 1418 CB VAL A 347 21.293 25.722 -14.619 1.00 28.86 C ANISOU 1418 CB VAL A 347 3447 3989 3530 447 -253 -31 C ATOM 1419 CG1 VAL A 347 20.422 26.955 -14.550 1.00 39.91 C ANISOU 1419 CG1 VAL A 347 4848 5385 4930 387 -166 31 C ATOM 1420 CG2 VAL A 347 21.156 24.896 -13.346 1.00 26.63 C ANISOU 1420 CG2 VAL A 347 3143 3642 3335 402 -291 11 C ATOM 1421 N ALA A 348 21.776 26.007 -17.829 1.00 22.31 N ANISOU 1421 N ALA A 348 2666 3277 2532 648 -303 -170 N ATOM 1422 CA ALA A 348 21.651 26.904 -18.975 1.00 23.34 C ANISOU 1422 CA ALA A 348 2809 3473 2587 687 -255 -180 C ATOM 1423 C ALA A 348 20.950 26.269 -20.182 1.00 29.23 C ANISOU 1423 C ALA A 348 3594 4172 3341 785 -371 -241 C ATOM 1424 O ALA A 348 20.626 26.959 -21.137 1.00 31.42 O ANISOU 1424 O ALA A 348 3884 4487 3566 817 -342 -245 O ATOM 1425 CB ALA A 348 23.013 27.461 -19.384 1.00 28.71 C ANISOU 1425 CB ALA A 348 3467 4294 3146 730 -172 -191 C ATOM 1426 N THR A 349 20.736 24.963 -20.155 1.00 28.00 N ANISOU 1426 N THR A 349 3457 3931 3250 835 -510 -288 N ATOM 1427 CA THR A 349 20.002 24.329 -21.250 1.00 33.22 C ANISOU 1427 CA THR A 349 4163 4526 3933 929 -644 -348 C ATOM 1428 C THR A 349 18.583 24.894 -21.229 1.00 36.51 C ANISOU 1428 C THR A 349 4581 4855 4437 850 -639 -284 C ATOM 1429 O THR A 349 17.943 24.908 -20.181 1.00 35.27 O ANISOU 1429 O THR A 349 4396 4624 4382 746 -624 -208 O ATOM 1430 CB THR A 349 19.967 22.809 -21.073 1.00 40.01 C ANISOU 1430 CB THR A 349 5042 5287 4873 984 -815 -401 C ATOM 1431 OG1 THR A 349 21.304 22.294 -21.153 1.00 37.58 O ANISOU 1431 OG1 THR A 349 4735 5068 4475 1068 -819 -466 O ATOM 1432 CG2 THR A 349 19.114 22.162 -22.145 1.00 48.54 C ANISOU 1432 CG2 THR A 349 6174 6277 5994 1077 -976 -461 C ATOM 1433 N PRO A 350 18.091 25.369 -22.387 1.00 39.49 N ANISOU 1433 N PRO A 350 4613 5875 4515 913 -1416 39 N ATOM 1434 CA PRO A 350 16.820 26.102 -22.467 1.00 36.58 C ANISOU 1434 CA PRO A 350 4186 5429 4285 877 -1438 160 C ATOM 1435 C PRO A 350 15.678 25.465 -21.676 1.00 36.43 C ANISOU 1435 C PRO A 350 4082 5246 4515 818 -1529 192 C ATOM 1436 O PRO A 350 14.987 26.171 -20.933 1.00 37.55 O ANISOU 1436 O PRO A 350 4152 5306 4807 751 -1426 311 O ATOM 1437 CB PRO A 350 16.505 26.086 -23.964 1.00 45.14 C ANISOU 1437 CB PRO A 350 5332 6577 5244 971 -1596 138 C ATOM 1438 CG PRO A 350 17.848 26.032 -24.619 1.00 45.31 C ANISOU 1438 CG PRO A 350 5445 6754 5017 1056 -1542 57 C ATOM 1439 CD PRO A 350 18.727 25.214 -23.710 1.00 40.51 C ANISOU 1439 CD PRO A 350 4838 6133 4420 1026 -1488 -32 C ATOM 1440 N GLU A 351 15.474 24.161 -21.839 1.00 37.56 N ANISOU 1440 N GLU A 351 4227 5335 4708 850 -1717 96 N ATOM 1441 CA GLU A 351 14.363 23.488 -21.172 1.00 46.02 C ANISOU 1441 CA GLU A 351 5202 6243 6039 807 -1821 143 C ATOM 1442 C GLU A 351 14.602 23.386 -19.668 1.00 37.81 C ANISOU 1442 C GLU A 351 4097 5152 5117 736 -1660 178 C ATOM 1443 O GLU A 351 13.668 23.503 -18.874 1.00 35.70 O ANISOU 1443 O GLU A 351 3739 4766 5059 688 -1628 290 O ATOM 1444 CB GLU A 351 14.118 22.105 -21.769 1.00 58.72 C ANISOU 1444 CB GLU A 351 6823 7801 7686 864 -2080 28 C ATOM 1445 CG GLU A 351 12.862 21.428 -21.235 1.00 80.18 C ANISOU 1445 CG GLU A 351 9424 10338 10704 828 -2217 99 C ATOM 1446 CD GLU A 351 12.343 20.330 -22.152 1.00 96.49 C ANISOU 1446 CD GLU A 351 11503 12334 12825 892 -2520 8 C ATOM 1447 OE1 GLU A 351 13.056 19.320 -22.353 1.00100.58 O ANISOU 1447 OE1 GLU A 351 12067 12886 13263 938 -2618 -141 O ATOM 1448 OE2 GLU A 351 11.212 20.476 -22.664 1.00101.79 O ANISOU 1448 OE2 GLU A 351 12137 12908 13630 895 -2668 87 O ATOM 1449 N HIS A 352 15.854 23.179 -19.277 1.00 28.55 N ANISOU 1449 N HIS A 352 2971 4068 3808 735 -1556 91 N ATOM 1450 CA HIS A 352 16.193 23.140 -17.856 1.00 30.23 C ANISOU 1450 CA HIS A 352 3137 4246 4102 672 -1400 119 C ATOM 1451 C HIS A 352 16.048 24.511 -17.203 1.00 33.36 C ANISOU 1451 C HIS A 352 3521 4639 4514 622 -1196 238 C ATOM 1452 O HIS A 352 15.532 24.630 -16.096 1.00 31.21 O ANISOU 1452 O HIS A 352 3186 4280 4391 579 -1106 319 O ATOM 1453 CB HIS A 352 17.608 22.614 -17.644 1.00 30.63 C ANISOU 1453 CB HIS A 352 3244 4391 4005 679 -1347 1 C ATOM 1454 CG HIS A 352 17.808 21.215 -18.137 1.00 33.08 C ANISOU 1454 CG HIS A 352 3563 4696 4310 727 -1534 -122 C ATOM 1455 ND1 HIS A 352 19.046 20.708 -18.463 1.00 36.23 N ANISOU 1455 ND1 HIS A 352 4032 5193 4541 761 -1529 -240 N ATOM 1456 CD2 HIS A 352 16.919 20.223 -18.381 1.00 38.04 C ANISOU 1456 CD2 HIS A 352 4137 5225 5093 749 -1736 -143 C ATOM 1457 CE1 HIS A 352 18.915 19.459 -18.872 1.00 38.98 C ANISOU 1457 CE1 HIS A 352 4373 5505 4931 804 -1717 -339 C ATOM 1458 NE2 HIS A 352 17.634 19.142 -18.834 1.00 41.46 N ANISOU 1458 NE2 HIS A 352 4611 5697 5444 796 -1853 -285 N ATOM 1459 N LEU A 353 16.514 25.541 -17.895 1.00 31.08 N ANISOU 1459 N LEU A 353 3291 4445 4072 638 -1121 252 N ATOM 1460 CA LEU A 353 16.412 26.901 -17.387 1.00 29.24 C ANISOU 1460 CA LEU A 353 3047 4208 3855 595 -939 357 C ATOM 1461 C LEU A 353 14.961 27.256 -17.109 1.00 27.50 C ANISOU 1461 C LEU A 353 2750 3865 3834 570 -950 485 C ATOM 1462 O LEU A 353 14.636 27.832 -16.068 1.00 29.33 O ANISOU 1462 O LEU A 353 2947 4032 4165 529 -809 567 O ATOM 1463 CB LEU A 353 17.007 27.893 -18.387 1.00 28.18 C ANISOU 1463 CB LEU A 353 2968 4190 3551 626 -890 366 C ATOM 1464 CG LEU A 353 17.148 29.320 -17.859 1.00 31.77 C ANISOU 1464 CG LEU A 353 3411 4647 4014 582 -699 460 C ATOM 1465 CD1 LEU A 353 18.156 29.347 -16.724 1.00 36.58 C ANISOU 1465 CD1 LEU A 353 4041 5263 4593 545 -568 416 C ATOM 1466 CD2 LEU A 353 17.568 30.266 -18.960 1.00 33.67 C ANISOU 1466 CD2 LEU A 353 3679 4994 4120 619 -670 493 C ATOM 1467 N ARG A 354 14.086 26.916 -18.051 1.00 31.37 N ANISOU 1467 N ARG A 354 3219 4318 4383 601 -1121 506 N ATOM 1468 CA ARG A 354 12.666 27.215 -17.917 1.00 32.30 C ANISOU 1468 CA ARG A 354 3256 4310 4706 580 -1151 642 C ATOM 1469 C ARG A 354 12.082 26.561 -16.662 1.00 30.90 C ANISOU 1469 C ARG A 354 3001 4008 4734 553 -1123 695 C ATOM 1470 O ARG A 354 11.441 27.225 -15.846 1.00 35.57 O ANISOU 1470 O ARG A 354 3543 4523 5451 524 -989 817 O ATOM 1471 CB ARG A 354 11.897 26.752 -19.163 1.00 32.39 C ANISOU 1471 CB ARG A 354 3261 4294 4752 620 -1379 640 C ATOM 1472 CG ARG A 354 10.388 26.981 -19.074 1.00 40.12 C ANISOU 1472 CG ARG A 354 4146 5126 5971 595 -1431 795 C ATOM 1473 CD ARG A 354 9.642 26.344 -20.245 1.00 50.92 C ANISOU 1473 CD ARG A 354 5508 6447 7391 635 -1696 781 C ATOM 1474 NE ARG A 354 9.851 24.897 -20.319 1.00 64.74 N ANISOU 1474 NE ARG A 354 7262 8168 9166 670 -1881 660 N ATOM 1475 CZ ARG A 354 9.242 24.004 -19.539 1.00 73.17 C ANISOU 1475 CZ ARG A 354 8237 9101 10462 655 -1946 699 C ATOM 1476 NH1 ARG A 354 8.384 24.402 -18.608 1.00 73.08 N ANISOU 1476 NH1 ARG A 354 8127 8975 10665 612 -1831 863 N ATOM 1477 NH2 ARG A 354 9.499 22.709 -19.686 1.00 76.88 N ANISOU 1477 NH2 ARG A 354 8709 9551 10953 689 -2122 582 N ATOM 1478 N GLN A 355 12.323 25.266 -16.502 1.00 29.77 N ANISOU 1478 N GLN A 355 2843 3846 4621 572 -1243 607 N ATOM 1479 CA GLN A 355 11.777 24.516 -15.371 1.00 31.56 C ANISOU 1479 CA GLN A 355 2981 3960 5052 558 -1232 665 C ATOM 1480 C GLN A 355 12.323 25.016 -14.043 1.00 31.43 C ANISOU 1480 C GLN A 355 2977 3963 5003 529 -1003 689 C ATOM 1481 O GLN A 355 11.580 25.243 -13.092 1.00 31.77 O ANISOU 1481 O GLN A 355 2957 3913 5201 521 -901 811 O ATOM 1482 CB GLN A 355 12.137 23.034 -15.486 1.00 34.15 C ANISOU 1482 CB GLN A 355 3293 4282 5402 583 -1401 550 C ATOM 1483 CG GLN A 355 11.406 22.265 -16.566 1.00 42.04 C ANISOU 1483 CG GLN A 355 4262 5216 6494 619 -1664 528 C ATOM 1484 CD GLN A 355 11.777 20.794 -16.548 1.00 53.34 C ANISOU 1484 CD GLN A 355 5669 6629 7967 644 -1824 412 C ATOM 1485 OE1 GLN A 355 11.576 20.102 -15.544 1.00 50.33 O ANISOU 1485 OE1 GLN A 355 5198 6173 7754 629 -1800 455 O ATOM 1486 NE2 GLN A 355 12.333 20.310 -17.654 1.00 54.41 N ANISOU 1486 NE2 GLN A 355 5886 6836 7950 688 -1982 267 N ATOM 1487 N ILE A 356 13.639 25.151 -13.972 1.00 23.23 N ANISOU 1487 N ILE A 356 2022 3041 3763 522 -927 574 N ATOM 1488 CA ILE A 356 14.292 25.481 -12.712 1.00 23.97 C ANISOU 1488 CA ILE A 356 2139 3154 3815 496 -741 572 C ATOM 1489 C ILE A 356 13.981 26.919 -12.274 1.00 31.21 C ANISOU 1489 C ILE A 356 3074 4051 4731 478 -564 672 C ATOM 1490 O ILE A 356 13.693 27.162 -11.102 1.00 30.95 O ANISOU 1490 O ILE A 356 3023 3960 4775 473 -433 739 O ATOM 1491 CB ILE A 356 15.817 25.233 -12.808 1.00 23.21 C ANISOU 1491 CB ILE A 356 2123 3177 3518 489 -722 430 C ATOM 1492 CG1 ILE A 356 16.066 23.741 -13.061 1.00 24.40 C ANISOU 1492 CG1 ILE A 356 2247 3331 3694 509 -884 336 C ATOM 1493 CG2 ILE A 356 16.545 25.694 -11.533 1.00 20.71 C ANISOU 1493 CG2 ILE A 356 1841 2877 3151 459 -541 426 C ATOM 1494 CD1 ILE A 356 17.497 23.390 -13.402 1.00 23.76 C ANISOU 1494 CD1 ILE A 356 2240 3363 3423 512 -891 200 C ATOM 1495 N CYS A 357 14.018 27.864 -13.213 1.00 27.27 N ANISOU 1495 N CYS A 357 2611 3602 4148 475 -560 684 N ATOM 1496 CA CYS A 357 13.801 29.277 -12.875 1.00 29.57 C ANISOU 1496 CA CYS A 357 2918 3878 4440 456 -398 770 C ATOM 1497 C CYS A 357 12.372 29.588 -12.489 1.00 31.57 C ANISOU 1497 C CYS A 357 3096 4004 4893 459 -362 922 C ATOM 1498 O CYS A 357 12.126 30.544 -11.761 1.00 34.67 O ANISOU 1498 O CYS A 357 3497 4357 5319 451 -203 995 O ATOM 1499 CB CYS A 357 14.234 30.211 -14.017 1.00 30.89 C ANISOU 1499 CB CYS A 357 3126 4135 4477 455 -401 757 C ATOM 1500 SG CYS A 357 16.022 30.333 -14.212 1.00 29.78 S ANISOU 1500 SG CYS A 357 3072 4134 4108 455 -359 624 S ATOM 1501 N SER A 358 11.443 28.769 -12.980 1.00 25.95 N ANISOU 1501 N SER A 358 2312 3223 4323 475 -516 970 N ATOM 1502 CA SER A 358 10.019 28.929 -12.732 1.00 31.33 C ANISOU 1502 CA SER A 358 2906 3771 5227 481 -508 1134 C ATOM 1503 C SER A 358 9.566 28.201 -11.475 1.00 28.47 C ANISOU 1503 C SER A 358 2483 3316 5017 503 -453 1198 C ATOM 1504 O SER A 358 8.378 28.007 -11.257 1.00 33.94 O ANISOU 1504 O SER A 358 3084 3887 5924 520 -472 1342 O ATOM 1505 CB SER A 358 9.236 28.422 -13.939 1.00 33.34 C ANISOU 1505 CB SER A 358 3108 3985 5576 490 -722 1164 C ATOM 1506 OG SER A 358 9.588 29.195 -15.074 1.00 43.57 O ANISOU 1506 OG SER A 358 4459 5371 6724 481 -753 1125 O ATOM 1507 N ASP A 359 10.530 27.811 -10.652 1.00 29.00 N ANISOU 1507 N ASP A 359 2598 3442 4978 505 -382 1102 N ATOM 1508 CA ASP A 359 10.258 27.106 -9.407 1.00 26.73 C ANISOU 1508 CA ASP A 359 2260 3090 4807 533 -318 1156 C ATOM 1509 C ASP A 359 10.730 27.936 -8.223 1.00 28.80 C ANISOU 1509 C ASP A 359 2594 3374 4974 540 -99 1158 C ATOM 1510 O ASP A 359 11.757 28.597 -8.291 1.00 25.81 O ANISOU 1510 O ASP A 359 2312 3085 4409 514 -39 1052 O ATOM 1511 CB ASP A 359 11.001 25.772 -9.386 1.00 27.16 C ANISOU 1511 CB ASP A 359 2304 3191 4825 534 -440 1037 C ATOM 1512 CG ASP A 359 10.788 25.022 -8.096 1.00 29.22 C ANISOU 1512 CG ASP A 359 2504 3398 5202 566 -371 1098 C ATOM 1513 OD1 ASP A 359 9.740 24.358 -7.970 1.00 30.88 O ANISOU 1513 OD1 ASP A 359 2596 3499 5637 596 -439 1221 O ATOM 1514 OD2 ASP A 359 11.668 25.088 -7.210 1.00 25.91 O ANISOU 1514 OD2 ASP A 359 2148 3040 4656 564 -253 1031 O ATOM 1515 N LYS A 360 9.973 27.887 -7.137 1.00 27.71 N ANISOU 1515 N LYS A 360 2409 3148 4971 584 16 1283 N ATOM 1516 CA LYS A 360 10.266 28.632 -5.916 1.00 26.50 C ANISOU 1516 CA LYS A 360 2331 3000 4738 610 222 1293 C ATOM 1517 C LYS A 360 11.712 28.417 -5.426 1.00 27.47 C ANISOU 1517 C LYS A 360 2549 3229 4660 590 244 1129 C ATOM 1518 O LYS A 360 12.450 29.375 -5.137 1.00 28.13 O ANISOU 1518 O LYS A 360 2736 3359 4593 574 345 1059 O ATOM 1519 CB LYS A 360 9.284 28.160 -4.837 1.00 41.51 C ANISOU 1519 CB LYS A 360 4152 4800 6818 681 310 1450 C ATOM 1520 CG LYS A 360 9.343 28.923 -3.542 1.00 53.89 C ANISOU 1520 CG LYS A 360 5799 6357 8318 734 526 1485 C ATOM 1521 CD LYS A 360 8.824 28.066 -2.390 1.00 61.83 C ANISOU 1521 CD LYS A 360 6738 7310 9445 814 596 1597 C ATOM 1522 CE LYS A 360 7.549 27.329 -2.757 1.00 67.56 C ANISOU 1522 CE LYS A 360 7300 7926 10442 842 510 1773 C ATOM 1523 NZ LYS A 360 7.006 26.564 -1.596 1.00 69.93 N ANISOU 1523 NZ LYS A 360 7520 8171 10878 933 598 1912 N ATOM 1524 N TYR A 361 12.125 27.154 -5.340 1.00 21.99 N ANISOU 1524 N TYR A 361 1814 2564 3978 588 141 1071 N ATOM 1525 CA TYR A 361 13.471 26.851 -4.869 1.00 20.01 C ANISOU 1525 CA TYR A 361 1640 2405 3557 564 156 928 C ATOM 1526 C TYR A 361 14.493 26.918 -5.986 1.00 26.61 C ANISOU 1526 C TYR A 361 2527 3334 4248 509 48 790 C ATOM 1527 O TYR A 361 15.606 27.377 -5.774 1.00 23.54 O ANISOU 1527 O TYR A 361 2230 3014 3698 482 101 691 O ATOM 1528 CB TYR A 361 13.505 25.479 -4.195 1.00 23.04 C ANISOU 1528 CB TYR A 361 1951 2780 4022 588 110 935 C ATOM 1529 CG TYR A 361 12.521 25.395 -3.047 1.00 31.32 C ANISOU 1529 CG TYR A 361 2943 3744 5214 660 232 1091 C ATOM 1530 CD1 TYR A 361 12.718 26.134 -1.883 1.00 27.47 C ANISOU 1530 CD1 TYR A 361 2543 3260 4632 700 414 1107 C ATOM 1531 CD2 TYR A 361 11.387 24.594 -3.136 1.00 35.54 C ANISOU 1531 CD2 TYR A 361 3334 4188 5980 699 164 1230 C ATOM 1532 CE1 TYR A 361 11.804 26.069 -0.832 1.00 33.57 C ANISOU 1532 CE1 TYR A 361 3272 3962 5523 786 541 1260 C ATOM 1533 CE2 TYR A 361 10.477 24.520 -2.101 1.00 37.60 C ANISOU 1533 CE2 TYR A 361 3534 4371 6383 778 289 1397 C ATOM 1534 CZ TYR A 361 10.687 25.256 -0.951 1.00 44.19 C ANISOU 1534 CZ TYR A 361 4464 5222 7103 826 485 1412 C ATOM 1535 OH TYR A 361 9.772 25.175 0.078 1.00 46.99 O ANISOU 1535 OH TYR A 361 4764 5505 7587 924 621 1587 O ATOM 1536 N GLY A 362 14.117 26.456 -7.175 1.00 22.30 N ANISOU 1536 N GLY A 362 1926 2787 3762 499 -106 788 N ATOM 1537 CA GLY A 362 15.041 26.477 -8.291 1.00 22.42 C ANISOU 1537 CA GLY A 362 1991 2895 3632 467 -204 667 C ATOM 1538 C GLY A 362 15.491 27.898 -8.572 1.00 20.11 C ANISOU 1538 C GLY A 362 1781 2646 3215 447 -105 655 C ATOM 1539 O GLY A 362 16.649 28.137 -8.895 1.00 22.11 O ANISOU 1539 O GLY A 362 2100 2985 3315 423 -104 556 O ATOM 1540 N CYS A 363 14.575 28.858 -8.464 1.00 21.12 N ANISOU 1540 N CYS A 363 1894 2708 3422 457 -21 765 N ATOM 1541 CA CYS A 363 14.951 30.252 -8.738 1.00 17.03 C ANISOU 1541 CA CYS A 363 1440 2222 2810 438 71 762 C ATOM 1542 C CYS A 363 16.026 30.753 -7.760 1.00 25.64 C ANISOU 1542 C CYS A 363 2618 3344 3781 426 188 690 C ATOM 1543 O CYS A 363 16.957 31.470 -8.146 1.00 23.05 O ANISOU 1543 O CYS A 363 2344 3078 3337 400 206 629 O ATOM 1544 CB CYS A 363 13.721 31.150 -8.708 1.00 25.10 C ANISOU 1544 CB CYS A 363 2423 3156 3958 452 146 900 C ATOM 1545 SG CYS A 363 14.157 32.865 -8.787 1.00 48.31 S ANISOU 1545 SG CYS A 363 5428 6117 6810 431 275 902 S ATOM 1546 N ARG A 364 15.920 30.349 -6.503 1.00 20.92 N ANISOU 1546 N ARG A 364 2030 2703 3217 448 259 701 N ATOM 1547 CA ARG A 364 16.954 30.673 -5.501 1.00 21.60 C ANISOU 1547 CA ARG A 364 2206 2814 3187 439 347 623 C ATOM 1548 C ARG A 364 18.306 30.041 -5.843 1.00 23.16 C ANISOU 1548 C ARG A 364 2433 3102 3266 401 263 500 C ATOM 1549 O ARG A 364 19.376 30.645 -5.622 1.00 21.48 O ANISOU 1549 O ARG A 364 2292 2923 2944 375 302 432 O ATOM 1550 CB ARG A 364 16.491 30.231 -4.104 1.00 24.33 C ANISOU 1550 CB ARG A 364 2554 3102 3588 486 433 667 C ATOM 1551 CG ARG A 364 17.445 30.569 -2.963 1.00 28.68 C ANISOU 1551 CG ARG A 364 3209 3668 4021 487 518 591 C ATOM 1552 CD ARG A 364 17.694 32.070 -2.841 1.00 32.08 C ANISOU 1552 CD ARG A 364 3724 4076 4391 482 605 577 C ATOM 1553 NE ARG A 364 18.988 32.466 -3.400 1.00 27.41 N ANISOU 1553 NE ARG A 364 3178 3547 3690 424 550 477 N ATOM 1554 CZ ARG A 364 19.519 33.678 -3.269 1.00 36.91 C ANISOU 1554 CZ ARG A 364 4450 4733 4840 411 601 447 C ATOM 1555 NH1 ARG A 364 18.858 34.628 -2.606 1.00 38.34 N ANISOU 1555 NH1 ARG A 364 4674 4838 5056 451 707 494 N ATOM 1556 NH2 ARG A 364 20.718 33.942 -3.792 1.00 30.04 N ANISOU 1556 NH2 ARG A 364 3604 3916 3893 363 546 375 N ATOM 1557 N VAL A 365 18.282 28.819 -6.367 1.00 18.18 N ANISOU 1557 N VAL A 365 1741 2500 2665 400 145 475 N ATOM 1558 CA VAL A 365 19.534 28.173 -6.775 1.00 15.92 C ANISOU 1558 CA VAL A 365 1479 2298 2271 370 68 365 C ATOM 1559 C VAL A 365 20.209 28.970 -7.898 1.00 17.91 C ANISOU 1559 C VAL A 365 1766 2614 2424 352 46 333 C ATOM 1560 O VAL A 365 21.433 29.208 -7.875 1.00 16.85 O ANISOU 1560 O VAL A 365 1686 2533 2185 327 64 267 O ATOM 1561 CB VAL A 365 19.310 26.716 -7.239 1.00 18.99 C ANISOU 1561 CB VAL A 365 1796 2700 2720 380 -66 341 C ATOM 1562 CG1 VAL A 365 20.589 26.133 -7.843 1.00 17.51 C ANISOU 1562 CG1 VAL A 365 1638 2601 2416 357 -141 229 C ATOM 1563 CG2 VAL A 365 18.839 25.854 -6.066 1.00 20.57 C ANISOU 1563 CG2 VAL A 365 1947 2845 3023 399 -41 378 C ATOM 1564 N VAL A 366 19.425 29.364 -8.891 1.00 15.85 N ANISOU 1564 N VAL A 366 1470 2348 2205 369 6 390 N ATOM 1565 CA VAL A 366 20.003 30.093 -10.026 1.00 15.50 C ANISOU 1565 CA VAL A 366 1447 2373 2069 365 -12 377 C ATOM 1566 C VAL A 366 20.544 31.452 -9.574 1.00 15.89 C ANISOU 1566 C VAL A 366 1545 2414 2079 344 107 394 C ATOM 1567 O VAL A 366 21.608 31.883 -10.024 1.00 18.25 O ANISOU 1567 O VAL A 366 1873 2774 2287 333 113 359 O ATOM 1568 CB VAL A 366 19.011 30.247 -11.179 1.00 22.93 C ANISOU 1568 CB VAL A 366 2340 3313 3061 389 -86 440 C ATOM 1569 CG1 VAL A 366 19.625 31.096 -12.285 1.00 22.35 C ANISOU 1569 CG1 VAL A 366 2287 3320 2885 396 -85 442 C ATOM 1570 CG2 VAL A 366 18.639 28.865 -11.734 1.00 24.86 C ANISOU 1570 CG2 VAL A 366 2543 3563 3338 413 -236 403 C ATOM 1571 N GLN A 367 19.842 32.130 -8.670 1.00 17.15 N ANISOU 1571 N GLN A 367 1712 2490 2313 346 203 450 N ATOM 1572 CA GLN A 367 20.374 33.417 -8.194 1.00 16.80 C ANISOU 1572 CA GLN A 367 1720 2425 2240 329 302 453 C ATOM 1573 C GLN A 367 21.689 33.250 -7.443 1.00 20.94 C ANISOU 1573 C GLN A 367 2308 2969 2680 306 315 366 C ATOM 1574 O GLN A 367 22.623 34.036 -7.604 1.00 18.95 O ANISOU 1574 O GLN A 367 2084 2735 2380 286 334 346 O ATOM 1575 CB GLN A 367 19.363 34.180 -7.312 1.00 20.38 C ANISOU 1575 CB GLN A 367 2182 2779 2781 348 406 522 C ATOM 1576 CG GLN A 367 19.814 35.635 -7.073 1.00 24.39 C ANISOU 1576 CG GLN A 367 2735 3257 3273 335 489 525 C ATOM 1577 CD GLN A 367 18.876 36.404 -6.177 1.00 36.30 C ANISOU 1577 CD GLN A 367 4266 4666 4858 363 598 582 C ATOM 1578 OE1 GLN A 367 17.673 36.158 -6.164 1.00 34.96 O ANISOU 1578 OE1 GLN A 367 4053 4454 4778 390 619 662 O ATOM 1579 NE2 GLN A 367 19.425 37.345 -5.416 1.00 38.43 N ANISOU 1579 NE2 GLN A 367 4608 4892 5102 361 664 545 N ATOM 1580 N THR A 368 21.770 32.226 -6.610 1.00 15.89 N ANISOU 1580 N THR A 368 1681 2319 2036 307 300 323 N ATOM 1581 CA THR A 368 23.034 31.915 -5.919 1.00 15.25 C ANISOU 1581 CA THR A 368 1656 2259 1880 280 297 242 C ATOM 1582 C THR A 368 24.184 31.615 -6.884 1.00 16.53 C ANISOU 1582 C THR A 368 1809 2505 1968 257 228 198 C ATOM 1583 O THR A 368 25.322 32.064 -6.684 1.00 17.22 O ANISOU 1583 O THR A 368 1936 2600 2005 229 241 166 O ATOM 1584 CB THR A 368 22.831 30.742 -4.941 1.00 18.67 C ANISOU 1584 CB THR A 368 2088 2677 2330 289 290 216 C ATOM 1585 OG1 THR A 368 21.930 31.170 -3.908 1.00 23.63 O ANISOU 1585 OG1 THR A 368 2739 3227 3010 324 379 265 O ATOM 1586 CG2 THR A 368 24.188 30.277 -4.328 1.00 17.56 C ANISOU 1586 CG2 THR A 368 1996 2566 2112 253 271 134 C ATOM 1587 N ILE A 369 23.895 30.867 -7.942 1.00 15.59 N ANISOU 1587 N ILE A 369 1636 2441 1845 274 150 201 N ATOM 1588 CA ILE A 369 24.906 30.610 -8.967 1.00 14.17 C ANISOU 1588 CA ILE A 369 1452 2346 1585 274 95 169 C ATOM 1589 C ILE A 369 25.371 31.919 -9.627 1.00 15.55 C ANISOU 1589 C ILE A 369 1633 2542 1736 276 138 217 C ATOM 1590 O ILE A 369 26.561 32.153 -9.811 1.00 15.30 O ANISOU 1590 O ILE A 369 1617 2544 1653 264 144 204 O ATOM 1591 CB ILE A 369 24.369 29.638 -10.036 1.00 14.39 C ANISOU 1591 CB ILE A 369 1435 2425 1608 310 -4 160 C ATOM 1592 CG1 ILE A 369 24.268 28.215 -9.464 1.00 15.79 C ANISOU 1592 CG1 ILE A 369 1594 2590 1814 304 -63 104 C ATOM 1593 CG2 ILE A 369 25.296 29.620 -11.310 1.00 15.29 C ANISOU 1593 CG2 ILE A 369 1554 2636 1621 336 -46 144 C ATOM 1594 CD1 ILE A 369 23.483 27.227 -10.386 1.00 18.89 C ANISOU 1594 CD1 ILE A 369 1937 3001 2239 343 -182 94 C ATOM 1595 N ILE A 370 24.426 32.766 -10.000 1.00 17.24 N ANISOU 1595 N ILE A 370 1822 2730 2001 293 167 286 N ATOM 1596 CA ILE A 370 24.783 34.041 -10.622 1.00 21.55 C ANISOU 1596 CA ILE A 370 2354 3290 2542 296 210 345 C ATOM 1597 C ILE A 370 25.659 34.878 -9.689 1.00 18.37 C ANISOU 1597 C ILE A 370 1992 2832 2156 261 271 332 C ATOM 1598 O ILE A 370 26.667 35.458 -10.119 1.00 16.97 O ANISOU 1598 O ILE A 370 1805 2683 1958 257 278 354 O ATOM 1599 CB ILE A 370 23.532 34.831 -11.002 1.00 19.38 C ANISOU 1599 CB ILE A 370 2041 2982 2339 312 239 424 C ATOM 1600 CG1 ILE A 370 22.825 34.156 -12.173 1.00 20.71 C ANISOU 1600 CG1 ILE A 370 2169 3212 2490 349 157 445 C ATOM 1601 CG2 ILE A 370 23.874 36.279 -11.358 1.00 19.60 C ANISOU 1601 CG2 ILE A 370 2049 3006 2393 307 299 490 C ATOM 1602 CD1 ILE A 370 21.401 34.644 -12.367 1.00 19.42 C ANISOU 1602 CD1 ILE A 370 1965 2995 2419 356 169 524 C ATOM 1603 N GLU A 371 25.280 34.935 -8.414 1.00 18.92 N ANISOU 1603 N GLU A 371 2106 2818 2264 244 309 303 N ATOM 1604 CA GLU A 371 26.063 35.677 -7.417 1.00 18.06 C ANISOU 1604 CA GLU A 371 2054 2643 2166 216 347 274 C ATOM 1605 C GLU A 371 27.505 35.189 -7.323 1.00 24.69 C ANISOU 1605 C GLU A 371 2913 3515 2952 189 304 227 C ATOM 1606 O GLU A 371 28.451 35.994 -7.263 1.00 21.25 O ANISOU 1606 O GLU A 371 2487 3053 2535 169 309 239 O ATOM 1607 CB GLU A 371 25.366 35.627 -6.054 1.00 18.42 C ANISOU 1607 CB GLU A 371 2158 2605 2237 221 392 243 C ATOM 1608 CG GLU A 371 24.076 36.472 -6.045 1.00 18.87 C ANISOU 1608 CG GLU A 371 2199 2605 2365 249 457 308 C ATOM 1609 CD GLU A 371 23.227 36.273 -4.792 1.00 32.68 C ANISOU 1609 CD GLU A 371 4001 4282 4135 278 515 297 C ATOM 1610 OE1 GLU A 371 22.249 37.027 -4.600 1.00 31.15 O ANISOU 1610 OE1 GLU A 371 3806 4026 4003 305 584 351 O ATOM 1611 OE2 GLU A 371 23.519 35.352 -4.011 1.00 36.18 O ANISOU 1611 OE2 GLU A 371 4481 4730 4535 278 499 244 O ATOM 1612 N LYS A 372 27.678 33.874 -7.349 1.00 18.57 N ANISOU 1612 N LYS A 372 2136 2791 2128 187 259 181 N ATOM 1613 CA LYS A 372 29.009 33.286 -7.258 1.00 17.29 C ANISOU 1613 CA LYS A 372 1989 2660 1922 160 222 141 C ATOM 1614 C LYS A 372 29.817 33.547 -8.531 1.00 19.80 C ANISOU 1614 C LYS A 372 2261 3049 2215 177 207 191 C ATOM 1615 O LYS A 372 31.033 33.646 -8.469 1.00 21.66 O ANISOU 1615 O LYS A 372 2501 3282 2446 155 199 195 O ATOM 1616 CB LYS A 372 28.910 31.778 -6.993 1.00 16.72 C ANISOU 1616 CB LYS A 372 1915 2624 1815 157 179 83 C ATOM 1617 CG LYS A 372 30.247 31.053 -6.864 1.00 21.23 C ANISOU 1617 CG LYS A 372 2496 3225 2346 125 144 43 C ATOM 1618 CD LYS A 372 31.149 31.703 -5.806 1.00 29.73 C ANISOU 1618 CD LYS A 372 3627 4227 3441 80 160 29 C ATOM 1619 CE LYS A 372 30.516 31.649 -4.403 1.00 27.39 C ANISOU 1619 CE LYS A 372 3388 3862 3157 71 182 -13 C ATOM 1620 NZ LYS A 372 31.478 32.140 -3.342 1.00 31.06 N ANISOU 1620 NZ LYS A 372 3921 4255 3624 31 174 -43 N ATOM 1621 N LEU A 373 29.141 33.641 -9.676 1.00 14.99 N ANISOU 1621 N LEU A 373 1605 2498 1591 221 203 238 N ATOM 1622 CA LEU A 373 29.805 33.910 -10.965 1.00 15.87 C ANISOU 1622 CA LEU A 373 1674 2691 1665 260 200 298 C ATOM 1623 C LEU A 373 30.034 35.405 -11.239 1.00 15.51 C ANISOU 1623 C LEU A 373 1595 2617 1683 263 249 387 C ATOM 1624 O LEU A 373 30.538 35.781 -12.296 1.00 21.24 O ANISOU 1624 O LEU A 373 2273 3408 2388 304 260 461 O ATOM 1625 CB LEU A 373 28.999 33.310 -12.132 1.00 15.74 C ANISOU 1625 CB LEU A 373 1630 2759 1592 318 161 306 C ATOM 1626 CG LEU A 373 28.853 31.781 -12.104 1.00 21.10 C ANISOU 1626 CG LEU A 373 2327 3472 2220 326 93 223 C ATOM 1627 CD1 LEU A 373 27.974 31.297 -13.267 1.00 21.58 C ANISOU 1627 CD1 LEU A 373 2367 3597 2237 387 33 227 C ATOM 1628 CD2 LEU A 373 30.224 31.112 -12.139 1.00 23.16 C ANISOU 1628 CD2 LEU A 373 2602 3772 2427 322 82 192 C ATOM 1629 N THR A 374 29.687 36.251 -10.281 1.00 16.00 N ANISOU 1629 N THR A 374 1679 2579 1821 227 280 382 N ATOM 1630 CA THR A 374 29.838 37.687 -10.462 1.00 18.75 C ANISOU 1630 CA THR A 374 1989 2884 2252 227 319 461 C ATOM 1631 C THR A 374 31.226 38.152 -10.008 1.00 22.11 C ANISOU 1631 C THR A 374 2418 3256 2726 197 308 473 C ATOM 1632 O THR A 374 31.703 37.763 -8.931 1.00 22.84 O ANISOU 1632 O THR A 374 2574 3287 2818 156 282 400 O ATOM 1633 CB THR A 374 28.755 38.450 -9.679 1.00 18.68 C ANISOU 1633 CB THR A 374 2004 2782 2310 212 355 450 C ATOM 1634 OG1 THR A 374 27.469 38.133 -10.225 1.00 20.58 O ANISOU 1634 OG1 THR A 374 2223 3064 2534 241 364 468 O ATOM 1635 CG2 THR A 374 28.979 39.956 -9.766 1.00 22.13 C ANISOU 1635 CG2 THR A 374 2400 3158 2850 208 388 522 C ATOM 1636 N ALA A 375 31.868 38.997 -10.813 1.00 21.68 N ANISOU 1636 N ALA A 375 2290 3220 2725 220 325 576 N ATOM 1637 CA ALA A 375 33.189 39.516 -10.443 1.00 24.62 C ANISOU 1637 CA ALA A 375 2648 3527 3178 193 306 611 C ATOM 1638 C ALA A 375 33.062 40.663 -9.445 1.00 28.67 C ANISOU 1638 C ALA A 375 3185 3900 3807 153 299 593 C ATOM 1639 O ALA A 375 33.311 41.831 -9.776 1.00 27.92 O ANISOU 1639 O ALA A 375 3021 3762 3826 161 310 681 O ATOM 1640 CB ALA A 375 33.959 39.968 -11.694 1.00 29.02 C ANISOU 1640 CB ALA A 375 3105 4155 3767 243 330 748 C ATOM 1641 N ASP A 376 32.667 40.346 -8.217 1.00 23.24 N ANISOU 1641 N ASP A 376 2595 3140 3094 119 280 482 N ATOM 1642 CA ASP A 376 32.465 41.413 -7.238 1.00 19.50 C ANISOU 1642 CA ASP A 376 2165 2534 2711 97 272 449 C ATOM 1643 C ASP A 376 33.541 41.367 -6.158 1.00 22.51 C ANISOU 1643 C ASP A 376 2614 2816 3122 54 202 388 C ATOM 1644 O ASP A 376 34.503 40.612 -6.268 1.00 21.47 O ANISOU 1644 O ASP A 376 2475 2719 2962 35 167 393 O ATOM 1645 CB ASP A 376 31.060 41.347 -6.630 1.00 28.52 C ANISOU 1645 CB ASP A 376 3372 3654 3810 110 315 383 C ATOM 1646 CG ASP A 376 30.765 40.016 -5.968 1.00 34.36 C ANISOU 1646 CG ASP A 376 4189 4429 4438 105 307 293 C ATOM 1647 OD1 ASP A 376 31.710 39.250 -5.670 1.00 29.80 O ANISOU 1647 OD1 ASP A 376 3637 3865 3821 79 261 256 O ATOM 1648 OD2 ASP A 376 29.573 39.738 -5.751 1.00 44.71 O ANISOU 1648 OD2 ASP A 376 5525 5750 5714 128 350 270 O ATOM 1649 N SER A 377 33.368 42.155 -5.105 1.00 23.10 N ANISOU 1649 N SER A 377 2760 2764 3251 41 178 327 N ATOM 1650 CA SER A 377 34.413 42.276 -4.095 1.00 28.62 C ANISOU 1650 CA SER A 377 3528 3355 3992 3 91 271 C ATOM 1651 C SER A 377 34.662 40.948 -3.376 1.00 28.79 C ANISOU 1651 C SER A 377 3633 3413 3893 -20 68 185 C ATOM 1652 O SER A 377 35.738 40.728 -2.826 1.00 31.31 O ANISOU 1652 O SER A 377 3984 3677 4234 -59 -7 162 O ATOM 1653 CB SER A 377 34.105 43.414 -3.105 1.00 37.18 C ANISOU 1653 CB SER A 377 4688 4292 5146 7 61 209 C ATOM 1654 OG SER A 377 32.912 43.152 -2.386 1.00 41.39 O ANISOU 1654 OG SER A 377 5318 4829 5579 39 118 124 O ATOM 1655 N MET A 378 33.682 40.048 -3.412 1.00 23.70 N ANISOU 1655 N MET A 378 3011 2858 3135 4 128 148 N ATOM 1656 CA MET A 378 33.836 38.738 -2.785 1.00 23.92 C ANISOU 1656 CA MET A 378 3098 2929 3061 -14 112 77 C ATOM 1657 C MET A 378 34.705 37.758 -3.584 1.00 25.47 C ANISOU 1657 C MET A 378 3225 3217 3234 -36 94 121 C ATOM 1658 O MET A 378 35.131 36.732 -3.049 1.00 29.23 O ANISOU 1658 O MET A 378 3739 3714 3652 -63 66 71 O ATOM 1659 CB MET A 378 32.457 38.100 -2.514 1.00 29.52 C ANISOU 1659 CB MET A 378 3841 3689 3684 24 178 35 C ATOM 1660 CG MET A 378 31.524 38.953 -1.664 1.00 44.41 C ANISOU 1660 CG MET A 378 5804 5489 5581 59 216 -4 C ATOM 1661 SD MET A 378 32.104 39.263 0.012 1.00130.77 S ANISOU 1661 SD MET A 378 16889 16302 16495 52 156 -109 S ATOM 1662 CE MET A 378 32.964 40.819 -0.200 1.00 89.97 C ANISOU 1662 CE MET A 378 11702 11015 11467 30 87 -80 C ATOM 1663 N ASN A 379 34.967 38.058 -4.857 1.00 20.21 N ANISOU 1663 N ASN A 379 2460 2610 2611 -17 115 219 N ATOM 1664 CA ASN A 379 35.778 37.159 -5.690 1.00 16.61 C ANISOU 1664 CA ASN A 379 1944 2245 2123 -19 109 267 C ATOM 1665 C ASN A 379 37.179 37.688 -5.982 1.00 18.78 C ANISOU 1665 C ASN A 379 2164 2471 2500 -39 71 354 C ATOM 1666 O ASN A 379 37.864 37.153 -6.834 1.00 22.61 O ANISOU 1666 O ASN A 379 2588 3031 2972 -23 84 421 O ATOM 1667 CB ASN A 379 35.071 36.849 -7.021 1.00 22.21 C ANISOU 1667 CB ASN A 379 2583 3078 2777 37 163 319 C ATOM 1668 CG ASN A 379 34.076 35.688 -6.902 1.00 29.03 C ANISOU 1668 CG ASN A 379 3482 4011 3539 51 176 242 C ATOM 1669 OD1 ASN A 379 33.010 35.686 -7.529 1.00 28.77 O ANISOU 1669 OD1 ASN A 379 3424 4031 3477 91 208 256 O ATOM 1670 ND2 ASN A 379 34.424 34.703 -6.092 1.00 19.81 N ANISOU 1670 ND2 ASN A 379 2362 2835 2330 16 145 170 N ATOM 1671 N VAL A 380 37.627 38.723 -5.276 1.00 18.91 N ANISOU 1671 N VAL A 380 2202 2357 2626 -67 21 358 N ATOM 1672 CA VAL A 380 38.957 39.270 -5.602 1.00 17.92 C ANISOU 1672 CA VAL A 380 2006 2171 2632 -84 -24 464 C ATOM 1673 C VAL A 380 40.117 38.317 -5.304 1.00 17.10 C ANISOU 1673 C VAL A 380 1912 2064 2520 -127 -68 465 C ATOM 1674 O VAL A 380 41.239 38.528 -5.792 1.00 22.61 O ANISOU 1674 O VAL A 380 2532 2736 3322 -132 -87 579 O ATOM 1675 CB VAL A 380 39.229 40.628 -4.914 1.00 24.63 C ANISOU 1675 CB VAL A 380 2869 2859 3629 -107 -92 469 C ATOM 1676 CG1 VAL A 380 38.187 41.650 -5.363 1.00 28.55 C ANISOU 1676 CG1 VAL A 380 3329 3358 4159 -63 -39 493 C ATOM 1677 CG2 VAL A 380 39.252 40.460 -3.394 1.00 26.32 C ANISOU 1677 CG2 VAL A 380 3219 2970 3811 -152 -169 333 C ATOM 1678 N ASP A 381 39.852 37.273 -4.520 1.00 20.49 N ANISOU 1678 N ASP A 381 2427 2518 2840 -156 -80 352 N ATOM 1679 CA ASP A 381 40.869 36.269 -4.206 1.00 22.92 C ANISOU 1679 CA ASP A 381 2743 2829 3135 -202 -118 348 C ATOM 1680 C ASP A 381 41.088 35.230 -5.313 1.00 25.20 C ANISOU 1680 C ASP A 381 2963 3254 3356 -169 -55 402 C ATOM 1681 O ASP A 381 41.998 34.404 -5.215 1.00 20.96 O ANISOU 1681 O ASP A 381 2418 2725 2821 -201 -74 418 O ATOM 1682 CB ASP A 381 40.528 35.536 -2.908 1.00 19.81 C ANISOU 1682 CB ASP A 381 2459 2412 2656 -243 -154 215 C ATOM 1683 CG ASP A 381 39.241 34.760 -3.012 1.00 28.28 C ANISOU 1683 CG ASP A 381 3556 3592 3598 -205 -87 142 C ATOM 1684 OD1 ASP A 381 38.197 35.387 -3.303 1.00 22.80 O ANISOU 1684 OD1 ASP A 381 2861 2912 2889 -160 -43 138 O ATOM 1685 OD2 ASP A 381 39.267 33.528 -2.814 1.00 24.70 O ANISOU 1685 OD2 ASP A 381 3112 3202 3070 -221 -82 98 O ATOM 1686 N LEU A 382 40.256 35.242 -6.354 1.00 24.70 N ANISOU 1686 N LEU A 382 2859 3297 3230 -102 15 428 N ATOM 1687 CA LEU A 382 40.441 34.289 -7.462 1.00 19.85 C ANISOU 1687 CA LEU A 382 2193 2811 2537 -53 65 469 C ATOM 1688 C LEU A 382 41.717 34.613 -8.239 1.00 23.52 C ANISOU 1688 C LEU A 382 2574 3270 3091 -30 80 617 C ATOM 1689 O LEU A 382 42.056 35.789 -8.431 1.00 23.44 O ANISOU 1689 O LEU A 382 2512 3193 3200 -20 76 714 O ATOM 1690 CB LEU A 382 39.248 34.359 -8.440 1.00 18.80 C ANISOU 1690 CB LEU A 382 2039 2782 2321 21 121 468 C ATOM 1691 CG LEU A 382 37.922 33.826 -7.896 1.00 21.64 C ANISOU 1691 CG LEU A 382 2461 3164 2595 14 117 346 C ATOM 1692 CD1 LEU A 382 36.840 33.945 -8.978 1.00 23.30 C ANISOU 1692 CD1 LEU A 382 2640 3467 2746 86 159 366 C ATOM 1693 CD2 LEU A 382 38.072 32.382 -7.438 1.00 27.49 C ANISOU 1693 CD2 LEU A 382 3237 3941 3268 -15 93 262 C ATOM 1694 N THR A 383 42.417 33.583 -8.713 1.00 21.32 N ANISOU 1694 N THR A 383 2275 3060 2766 -15 103 643 N ATOM 1695 CA THR A 383 43.507 33.793 -9.661 1.00 20.35 C ANISOU 1695 CA THR A 383 2066 2957 2708 37 145 802 C ATOM 1696 C THR A 383 42.927 34.319 -10.967 1.00 21.86 C ANISOU 1696 C THR A 383 2204 3251 2850 142 216 879 C ATOM 1697 O THR A 383 41.738 34.168 -11.224 1.00 18.52 O ANISOU 1697 O THR A 383 1816 2899 2321 172 228 795 O ATOM 1698 CB THR A 383 44.262 32.491 -10.015 1.00 24.63 C ANISOU 1698 CB THR A 383 2604 3567 3188 51 171 810 C ATOM 1699 OG1 THR A 383 43.336 31.509 -10.512 1.00 22.39 O ANISOU 1699 OG1 THR A 383 2359 3407 2741 99 197 706 O ATOM 1700 CG2 THR A 383 45.027 31.941 -8.808 1.00 22.74 C ANISOU 1700 CG2 THR A 383 2399 3228 3012 -55 105 763 C ATOM 1701 N SER A 384 43.761 34.906 -11.820 1.00 22.88 N ANISOU 1701 N SER A 384 2244 3390 3060 205 263 1049 N ATOM 1702 CA SER A 384 43.251 35.405 -13.095 1.00 26.84 C ANISOU 1702 CA SER A 384 2692 4000 3506 316 335 1135 C ATOM 1703 C SER A 384 42.745 34.262 -13.978 1.00 27.53 C ANISOU 1703 C SER A 384 2821 4242 3397 397 377 1071 C ATOM 1704 O SER A 384 41.792 34.436 -14.739 1.00 23.89 O ANISOU 1704 O SER A 384 2364 3872 2841 465 402 1056 O ATOM 1705 CB SER A 384 44.281 36.285 -13.826 1.00 33.59 C ANISOU 1705 CB SER A 384 3430 4836 4498 380 385 1353 C ATOM 1706 OG SER A 384 45.413 35.540 -14.210 1.00 45.54 O ANISOU 1706 OG SER A 384 4918 6378 6008 418 426 1440 O ATOM 1707 N ALA A 385 43.362 33.088 -13.864 1.00 26.07 N ANISOU 1707 N ALA A 385 2669 4080 3156 388 375 1029 N ATOM 1708 CA ALA A 385 42.877 31.928 -14.605 1.00 28.16 C ANISOU 1708 CA ALA A 385 2983 4475 3243 461 394 944 C ATOM 1709 C ALA A 385 41.472 31.543 -14.134 1.00 25.62 C ANISOU 1709 C ALA A 385 2730 4165 2840 418 335 773 C ATOM 1710 O ALA A 385 40.595 31.222 -14.947 1.00 22.36 O ANISOU 1710 O ALA A 385 2339 3851 2306 493 339 727 O ATOM 1711 CB ALA A 385 43.828 30.753 -14.445 1.00 25.99 C ANISOU 1711 CB ALA A 385 2725 4204 2947 448 398 927 C ATOM 1712 N ALA A 386 41.257 31.586 -12.822 1.00 19.46 N ANISOU 1712 N ALA A 386 1983 3280 2132 304 278 687 N ATOM 1713 CA ALA A 386 39.946 31.272 -12.269 1.00 21.27 C ANISOU 1713 CA ALA A 386 2268 3508 2307 266 233 548 C ATOM 1714 C ALA A 386 38.910 32.334 -12.651 1.00 21.78 C ANISOU 1714 C ALA A 386 2317 3581 2377 300 247 574 C ATOM 1715 O ALA A 386 37.724 32.024 -12.831 1.00 18.09 O ANISOU 1715 O ALA A 386 1878 3158 1838 319 229 496 O ATOM 1716 CB ALA A 386 40.031 31.084 -10.730 1.00 22.83 C ANISOU 1716 CB ALA A 386 2507 3594 2573 151 180 463 C ATOM 1717 N GLN A 387 39.352 33.587 -12.782 1.00 20.22 N ANISOU 1717 N GLN A 387 2065 3335 2282 305 275 692 N ATOM 1718 CA GLN A 387 38.444 34.663 -13.190 1.00 19.88 C ANISOU 1718 CA GLN A 387 1994 3299 2261 336 295 733 C ATOM 1719 C GLN A 387 38.001 34.416 -14.627 1.00 24.96 C ANISOU 1719 C GLN A 387 2616 4083 2786 448 333 775 C ATOM 1720 O GLN A 387 36.864 34.698 -14.997 1.00 19.47 O ANISOU 1720 O GLN A 387 1925 3423 2049 474 330 751 O ATOM 1721 CB GLN A 387 39.128 36.036 -13.077 1.00 26.50 C ANISOU 1721 CB GLN A 387 2762 4051 3255 323 312 861 C ATOM 1722 CG GLN A 387 39.353 36.526 -11.646 1.00 26.42 C ANISOU 1722 CG GLN A 387 2786 3888 3364 219 256 808 C ATOM 1723 CD GLN A 387 38.095 37.108 -11.009 1.00 25.87 C ANISOU 1723 CD GLN A 387 2760 3768 3303 186 239 723 C ATOM 1724 OE1 GLN A 387 37.004 36.981 -11.550 1.00 26.65 O ANISOU 1724 OE1 GLN A 387 2864 3942 3320 226 265 695 O ATOM 1725 NE2 GLN A 387 38.254 37.770 -9.863 1.00 24.61 N ANISOU 1725 NE2 GLN A 387 2632 3472 3244 117 194 687 N ATOM 1726 N ASN A 388 38.906 33.883 -15.443 1.00 25.82 N ANISOU 1726 N ASN A 388 2705 4268 2837 522 367 841 N ATOM 1727 CA ASN A 388 38.574 33.629 -16.837 1.00 28.07 C ANISOU 1727 CA ASN A 388 2984 4691 2989 647 400 880 C ATOM 1728 C ASN A 388 37.548 32.518 -16.944 1.00 24.04 C ANISOU 1728 C ASN A 388 2549 4236 2351 656 341 727 C ATOM 1729 O ASN A 388 36.587 32.592 -17.731 1.00 24.99 O ANISOU 1729 O ASN A 388 2678 4428 2389 720 328 715 O ATOM 1730 CB ASN A 388 39.814 33.278 -17.655 1.00 29.42 C ANISOU 1730 CB ASN A 388 3127 4931 3121 739 460 988 C ATOM 1731 CG ASN A 388 39.686 33.723 -19.096 1.00 52.73 C ANISOU 1731 CG ASN A 388 6042 8008 5984 884 521 1104 C ATOM 1732 OD1 ASN A 388 39.661 34.922 -19.383 1.00 62.37 O ANISOU 1732 OD1 ASN A 388 7187 9220 7291 904 562 1232 O ATOM 1733 ND2 ASN A 388 39.572 32.766 -20.007 1.00 57.80 N ANISOU 1733 ND2 ASN A 388 6740 8768 6453 990 522 1057 N ATOM 1734 N LEU A 389 37.749 31.482 -16.146 1.00 21.82 N ANISOU 1734 N LEU A 389 2313 3914 2064 592 297 617 N ATOM 1735 CA LEU A 389 36.788 30.392 -16.081 1.00 20.74 C ANISOU 1735 CA LEU A 389 2232 3805 1843 588 228 475 C ATOM 1736 C LEU A 389 35.432 30.918 -15.660 1.00 22.33 C ANISOU 1736 C LEU A 389 2438 3961 2084 544 195 431 C ATOM 1737 O LEU A 389 34.403 30.568 -16.243 1.00 22.23 O ANISOU 1737 O LEU A 389 2444 3999 2004 590 152 383 O ATOM 1738 CB LEU A 389 37.258 29.356 -15.070 1.00 20.75 C ANISOU 1738 CB LEU A 389 2262 3751 1873 508 192 382 C ATOM 1739 CG LEU A 389 36.501 28.034 -15.044 1.00 26.42 C ANISOU 1739 CG LEU A 389 3020 4496 2521 512 119 246 C ATOM 1740 CD1 LEU A 389 36.840 27.232 -16.293 1.00 28.99 C ANISOU 1740 CD1 LEU A 389 3366 4930 2721 628 113 237 C ATOM 1741 CD2 LEU A 389 36.891 27.257 -13.799 1.00 30.15 C ANISOU 1741 CD2 LEU A 389 3503 4896 3057 413 92 173 C ATOM 1742 N ARG A 390 35.432 31.737 -14.617 1.00 17.19 N ANISOU 1742 N ARG A 390 1774 3208 1549 458 210 448 N ATOM 1743 CA ARG A 390 34.192 32.331 -14.116 1.00 16.93 C ANISOU 1743 CA ARG A 390 1747 3121 1566 418 196 419 C ATOM 1744 C ARG A 390 33.516 33.197 -15.194 1.00 23.25 C ANISOU 1744 C ARG A 390 2510 3980 2346 488 221 502 C ATOM 1745 O ARG A 390 32.305 33.123 -15.402 1.00 26.76 O ANISOU 1745 O ARG A 390 2962 4435 2770 499 190 467 O ATOM 1746 CB ARG A 390 34.496 33.236 -12.923 1.00 15.91 C ANISOU 1746 CB ARG A 390 1616 2874 1557 334 216 436 C ATOM 1747 CG ARG A 390 33.229 33.821 -12.266 1.00 16.03 C ANISOU 1747 CG ARG A 390 1646 2822 1623 298 213 402 C ATOM 1748 CD ARG A 390 33.529 35.102 -11.440 1.00 21.86 C ANISOU 1748 CD ARG A 390 2379 3452 2476 248 239 444 C ATOM 1749 NE ARG A 390 34.415 35.995 -12.188 1.00 21.41 N ANISOU 1749 NE ARG A 390 2257 3411 2468 280 271 564 N ATOM 1750 CZ ARG A 390 34.039 36.720 -13.237 1.00 26.82 C ANISOU 1750 CZ ARG A 390 2882 4153 3154 340 306 656 C ATOM 1751 NH1 ARG A 390 32.770 36.707 -13.641 1.00 24.56 N ANISOU 1751 NH1 ARG A 390 2600 3905 2826 365 306 636 N ATOM 1752 NH2 ARG A 390 34.933 37.476 -13.874 1.00 29.43 N ANISOU 1752 NH2 ARG A 390 3142 4498 3541 376 340 782 N ATOM 1753 N GLU A 391 34.296 34.045 -15.854 1.00 26.16 N ANISOU 1753 N GLU A 391 2826 4379 2735 534 276 624 N ATOM 1754 CA GLU A 391 33.715 34.979 -16.822 1.00 25.41 C ANISOU 1754 CA GLU A 391 2682 4338 2634 597 307 719 C ATOM 1755 C GLU A 391 33.028 34.230 -17.948 1.00 32.04 C ANISOU 1755 C GLU A 391 3550 5292 3333 687 270 687 C ATOM 1756 O GLU A 391 31.960 34.634 -18.406 1.00 27.64 O ANISOU 1756 O GLU A 391 2980 4756 2767 707 255 701 O ATOM 1757 CB GLU A 391 34.758 35.941 -17.406 1.00 27.36 C ANISOU 1757 CB GLU A 391 2854 4608 2934 645 376 875 C ATOM 1758 CG GLU A 391 34.097 37.033 -18.292 1.00 40.02 C ANISOU 1758 CG GLU A 391 4392 6260 4554 701 413 985 C ATOM 1759 CD GLU A 391 32.791 37.582 -17.676 1.00 48.58 C ANISOU 1759 CD GLU A 391 5482 7268 5709 630 390 934 C ATOM 1760 OE1 GLU A 391 32.860 38.075 -16.531 1.00 37.61 O ANISOU 1760 OE1 GLU A 391 4096 5758 4438 542 390 905 O ATOM 1761 OE2 GLU A 391 31.696 37.525 -18.315 1.00 42.41 O ANISOU 1761 OE2 GLU A 391 4706 6542 4867 666 370 924 O ATOM 1762 N ARG A 392 33.642 33.135 -18.389 1.00 30.78 N ANISOU 1762 N ARG A 392 3429 5200 3066 742 249 642 N ATOM 1763 CA ARG A 392 33.068 32.328 -19.464 1.00 38.34 C ANISOU 1763 CA ARG A 392 4428 6260 3880 838 194 593 C ATOM 1764 C ARG A 392 31.789 31.616 -19.035 1.00 31.13 C ANISOU 1764 C ARG A 392 3554 5302 2972 790 100 468 C ATOM 1765 O ARG A 392 30.816 31.565 -19.785 1.00 28.84 O ANISOU 1765 O ARG A 392 3274 5056 2628 841 46 458 O ATOM 1766 CB ARG A 392 34.086 31.314 -19.988 1.00 42.32 C ANISOU 1766 CB ARG A 392 4970 6836 4273 914 196 568 C ATOM 1767 CG ARG A 392 35.340 31.936 -20.570 1.00 62.13 C ANISOU 1767 CG ARG A 392 7434 9398 6773 986 295 715 C ATOM 1768 CD ARG A 392 35.010 32.859 -21.732 1.00 78.22 C ANISOU 1768 CD ARG A 392 9434 11528 8759 1090 338 836 C ATOM 1769 NE ARG A 392 36.211 33.301 -22.435 1.00 88.80 N ANISOU 1769 NE ARG A 392 10725 12935 10078 1189 437 991 N ATOM 1770 CZ ARG A 392 36.202 34.092 -23.502 1.00 95.58 C ANISOU 1770 CZ ARG A 392 11538 13888 10890 1301 496 1129 C ATOM 1771 NH1 ARG A 392 35.051 34.532 -23.993 1.00 98.11 N ANISOU 1771 NH1 ARG A 392 11857 14246 11175 1319 459 1124 N ATOM 1772 NH2 ARG A 392 37.344 34.445 -24.081 1.00 99.04 N ANISOU 1772 NH2 ARG A 392 11924 14382 11324 1397 595 1285 N ATOM 1773 N ALA A 393 31.797 31.046 -17.839 1.00 24.14 N ANISOU 1773 N ALA A 393 2685 4328 2158 696 75 383 N ATOM 1774 CA ALA A 393 30.592 30.425 -17.306 1.00 24.01 C ANISOU 1774 CA ALA A 393 2688 4256 2178 650 -3 290 C ATOM 1775 C ALA A 393 29.464 31.448 -17.140 1.00 24.89 C ANISOU 1775 C ALA A 393 2768 4318 2372 619 12 343 C ATOM 1776 O ALA A 393 28.305 31.165 -17.445 1.00 23.16 O ANISOU 1776 O ALA A 393 2552 4094 2155 633 -54 316 O ATOM 1777 CB ALA A 393 30.885 29.736 -15.971 1.00 21.98 C ANISOU 1777 CB ALA A 393 2445 3916 1989 560 -13 211 C ATOM 1778 N LEU A 394 29.798 32.635 -16.646 1.00 18.93 N ANISOU 1778 N LEU A 394 1980 3514 1698 575 93 421 N ATOM 1779 CA LEU A 394 28.781 33.677 -16.490 1.00 21.90 C ANISOU 1779 CA LEU A 394 2323 3838 2158 548 119 477 C ATOM 1780 C LEU A 394 28.208 34.043 -17.850 1.00 21.42 C ANISOU 1780 C LEU A 394 2236 3865 2037 628 103 544 C ATOM 1781 O LEU A 394 27.001 34.174 -18.011 1.00 21.58 O ANISOU 1781 O LEU A 394 2246 3863 2090 624 67 550 O ATOM 1782 CB LEU A 394 29.380 34.923 -15.831 1.00 21.28 C ANISOU 1782 CB LEU A 394 2213 3695 2179 499 201 547 C ATOM 1783 CG LEU A 394 28.446 36.131 -15.730 1.00 22.53 C ANISOU 1783 CG LEU A 394 2332 3799 2431 477 240 614 C ATOM 1784 CD1 LEU A 394 27.241 35.825 -14.823 1.00 20.10 C ANISOU 1784 CD1 LEU A 394 2052 3404 2180 427 217 550 C ATOM 1785 CD2 LEU A 394 29.203 37.354 -15.211 1.00 21.34 C ANISOU 1785 CD2 LEU A 394 2145 3583 2379 442 306 682 C ATOM 1786 N GLN A 395 29.087 34.213 -18.832 1.00 20.21 N ANISOU 1786 N GLN A 395 2071 3810 1798 707 131 607 N ATOM 1787 CA GLN A 395 28.659 34.630 -20.167 1.00 23.76 C ANISOU 1787 CA GLN A 395 2497 4356 2173 797 123 684 C ATOM 1788 C GLN A 395 27.736 33.590 -20.800 1.00 28.64 C ANISOU 1788 C GLN A 395 3167 5015 2700 845 8 599 C ATOM 1789 O GLN A 395 26.766 33.946 -21.478 1.00 31.37 O ANISOU 1789 O GLN A 395 3496 5383 3038 875 -29 639 O ATOM 1790 CB GLN A 395 29.888 34.892 -21.062 1.00 23.99 C ANISOU 1790 CB GLN A 395 2508 4491 2116 891 185 774 C ATOM 1791 CG GLN A 395 29.591 34.828 -22.558 1.00 44.81 C ANISOU 1791 CG GLN A 395 5154 7260 4611 1020 159 821 C ATOM 1792 CD GLN A 395 29.172 36.161 -23.137 1.00 63.25 C ANISOU 1792 CD GLN A 395 7411 9625 6997 1041 215 963 C ATOM 1793 OE1 GLN A 395 28.487 36.951 -22.484 1.00 67.18 O ANISOU 1793 OE1 GLN A 395 7861 10031 7633 952 234 989 O ATOM 1794 NE2 GLN A 395 29.578 36.418 -24.377 1.00 71.39 N ANISOU 1794 NE2 GLN A 395 8425 10785 7913 1168 248 1061 N ATOM 1795 N ARG A 396 28.017 32.309 -20.567 1.00 27.88 N ANISOU 1795 N ARG A 396 3127 4918 2550 850 -58 485 N ATOM 1796 CA ARG A 396 27.159 31.250 -21.096 1.00 33.05 C ANISOU 1796 CA ARG A 396 3826 5589 3141 893 -189 394 C ATOM 1797 C ARG A 396 25.790 31.236 -20.418 1.00 31.81 C ANISOU 1797 C ARG A 396 3647 5325 3115 815 -245 372 C ATOM 1798 O ARG A 396 24.765 31.044 -21.070 1.00 30.94 O ANISOU 1798 O ARG A 396 3541 5220 2996 848 -339 367 O ATOM 1799 CB ARG A 396 27.827 29.881 -20.975 1.00 30.53 C ANISOU 1799 CB ARG A 396 3562 5286 2752 916 -246 278 C ATOM 1800 CG ARG A 396 29.142 29.789 -21.769 1.00 40.81 C ANISOU 1800 CG ARG A 396 4891 6697 3916 1013 -191 307 C ATOM 1801 CD ARG A 396 29.654 28.357 -21.894 1.00 39.57 C ANISOU 1801 CD ARG A 396 4796 6566 3674 1057 -262 187 C ATOM 1802 NE ARG A 396 29.756 27.685 -20.606 1.00 40.05 N ANISOU 1802 NE ARG A 396 4845 6527 3846 947 -276 109 N ATOM 1803 CZ ARG A 396 30.837 27.702 -19.830 1.00 42.33 C ANISOU 1803 CZ ARG A 396 5119 6790 4175 893 -192 125 C ATOM 1804 NH1 ARG A 396 31.924 28.372 -20.204 1.00 43.10 N ANISOU 1804 NH1 ARG A 396 5205 6943 4229 936 -89 222 N ATOM 1805 NH2 ARG A 396 30.829 27.054 -18.673 1.00 32.74 N ANISOU 1805 NH2 ARG A 396 3896 5491 3054 798 -214 53 N ATOM 1806 N LEU A 397 25.773 31.433 -19.107 1.00 25.13 N ANISOU 1806 N LEU A 397 2779 4379 2391 717 -189 364 N ATOM 1807 CA LEU A 397 24.503 31.447 -18.379 1.00 23.98 C ANISOU 1807 CA LEU A 397 2609 4128 2375 653 -219 361 C ATOM 1808 C LEU A 397 23.693 32.676 -18.759 1.00 27.54 C ANISOU 1808 C LEU A 397 3014 4566 2883 650 -178 470 C ATOM 1809 O LEU A 397 22.481 32.591 -18.950 1.00 26.75 O ANISOU 1809 O LEU A 397 2896 4424 2845 646 -242 487 O ATOM 1810 CB LEU A 397 24.739 31.409 -16.867 1.00 21.50 C ANISOU 1810 CB LEU A 397 2292 3718 2158 567 -156 331 C ATOM 1811 CG LEU A 397 23.478 31.445 -15.993 1.00 25.53 C ANISOU 1811 CG LEU A 397 2778 4119 2805 514 -162 343 C ATOM 1812 CD1 LEU A 397 22.547 30.282 -16.360 1.00 28.84 C ANISOU 1812 CD1 LEU A 397 3191 4521 3245 541 -296 296 C ATOM 1813 CD2 LEU A 397 23.844 31.389 -14.494 1.00 23.60 C ANISOU 1813 CD2 LEU A 397 2546 3795 2626 448 -92 311 C ATOM 1814 N MET A 398 24.358 33.822 -18.868 1.00 25.85 N ANISOU 1814 N MET A 398 2773 4382 2666 649 -73 552 N ATOM 1815 CA MET A 398 23.656 35.055 -19.223 1.00 27.35 C ANISOU 1815 CA MET A 398 2908 4560 2922 643 -24 663 C ATOM 1816 C MET A 398 23.082 34.980 -20.636 1.00 31.08 C ANISOU 1816 C MET A 398 3377 5123 3312 723 -102 701 C ATOM 1817 O MET A 398 22.016 35.534 -20.913 1.00 25.15 O ANISOU 1817 O MET A 398 2586 4341 2630 710 -116 768 O ATOM 1818 CB MET A 398 24.564 36.271 -19.083 1.00 26.59 C ANISOU 1818 CB MET A 398 2772 4476 2856 631 93 746 C ATOM 1819 CG MET A 398 24.934 36.620 -17.642 1.00 21.76 C ANISOU 1819 CG MET A 398 2165 3754 2347 549 162 718 C ATOM 1820 SD MET A 398 23.527 37.153 -16.629 1.00 28.13 S ANISOU 1820 SD MET A 398 2957 4424 3306 478 190 731 S ATOM 1821 CE MET A 398 23.249 35.720 -15.578 1.00 22.46 C ANISOU 1821 CE MET A 398 2299 3643 2590 447 131 609 C ATOM 1822 N THR A 399 23.783 34.301 -21.535 1.00 27.58 N ANISOU 1822 N THR A 399 2977 4787 2716 810 -153 662 N ATOM 1823 CA THR A 399 23.241 34.140 -22.881 1.00 32.44 C ANISOU 1823 CA THR A 399 3608 5489 3228 900 -243 683 C ATOM 1824 C THR A 399 21.888 33.420 -22.823 1.00 32.59 C ANISOU 1824 C THR A 399 3639 5431 3313 875 -378 629 C ATOM 1825 O THR A 399 20.928 33.840 -23.474 1.00 30.11 O ANISOU 1825 O THR A 399 3300 5118 3024 889 -428 694 O ATOM 1826 CB THR A 399 24.217 33.406 -23.824 1.00 30.75 C ANISOU 1826 CB THR A 399 3458 5402 2823 1015 -279 635 C ATOM 1827 OG1 THR A 399 25.438 34.150 -23.908 1.00 36.95 O ANISOU 1827 OG1 THR A 399 4214 6251 3573 1043 -147 716 O ATOM 1828 CG2 THR A 399 23.617 33.276 -25.225 1.00 32.17 C ANISOU 1828 CG2 THR A 399 3669 5675 2880 1122 -381 651 C ATOM 1829 N SER A 400 21.804 32.345 -22.038 1.00 27.76 N ANISOU 1829 N SER A 400 3056 4745 2745 836 -440 524 N ATOM 1830 CA SER A 400 20.551 31.591 -21.914 1.00 32.73 C ANISOU 1830 CA SER A 400 3683 5286 3468 814 -574 484 C ATOM 1831 C SER A 400 19.450 32.393 -21.222 1.00 32.00 C ANISOU 1831 C SER A 400 3522 5081 3557 732 -522 578 C ATOM 1832 O SER A 400 18.273 32.331 -21.611 1.00 25.53 O ANISOU 1832 O SER A 400 2676 4211 2812 733 -616 617 O ATOM 1833 CB SER A 400 20.768 30.277 -21.159 1.00 37.69 C ANISOU 1833 CB SER A 400 4338 5859 4123 792 -640 365 C ATOM 1834 OG SER A 400 21.572 29.392 -21.912 1.00 55.39 O ANISOU 1834 OG SER A 400 6645 8193 6206 875 -716 272 O ATOM 1835 N VAL A 401 19.823 33.130 -20.180 1.00 21.64 N ANISOU 1835 N VAL A 401 2181 3720 2319 667 -377 614 N ATOM 1836 CA VAL A 401 18.838 33.982 -19.496 1.00 22.11 C ANISOU 1836 CA VAL A 401 2185 3675 2543 601 -307 705 C ATOM 1837 C VAL A 401 18.323 35.047 -20.450 1.00 25.09 C ANISOU 1837 C VAL A 401 2519 4092 2924 621 -291 818 C ATOM 1838 O VAL A 401 17.113 35.272 -20.561 1.00 28.61 O ANISOU 1838 O VAL A 401 2921 4467 3480 599 -328 887 O ATOM 1839 CB VAL A 401 19.431 34.643 -18.230 1.00 24.72 C ANISOU 1839 CB VAL A 401 2510 3950 2933 540 -159 711 C ATOM 1840 CG1 VAL A 401 18.466 35.705 -17.676 1.00 24.61 C ANISOU 1840 CG1 VAL A 401 2444 3839 3069 491 -72 812 C ATOM 1841 CG2 VAL A 401 19.737 33.579 -17.176 1.00 23.42 C ANISOU 1841 CG2 VAL A 401 2381 3734 2784 515 -177 612 C ATOM 1842 N THR A 402 19.237 35.673 -21.184 1.00 25.36 N ANISOU 1842 N THR A 402 2554 4238 2843 667 -237 850 N ATOM 1843 CA THR A 402 18.837 36.734 -22.113 1.00 26.68 C ANISOU 1843 CA THR A 402 2669 4457 3012 691 -211 970 C ATOM 1844 C THR A 402 17.931 36.200 -23.231 1.00 27.91 C ANISOU 1844 C THR A 402 2838 4646 3121 744 -365 976 C ATOM 1845 O THR A 402 16.982 36.867 -23.647 1.00 32.18 O ANISOU 1845 O THR A 402 3325 5161 3740 729 -375 1076 O ATOM 1846 CB THR A 402 20.057 37.463 -22.710 1.00 34.01 C ANISOU 1846 CB THR A 402 3585 5505 3832 743 -122 1018 C ATOM 1847 OG1 THR A 402 20.794 38.089 -21.651 1.00 35.01 O ANISOU 1847 OG1 THR A 402 3691 5577 4036 684 4 1024 O ATOM 1848 CG2 THR A 402 19.604 38.536 -23.685 1.00 43.07 C ANISOU 1848 CG2 THR A 402 4666 6711 4989 772 -96 1153 C ATOM 1849 N ASN A 403 18.206 34.985 -23.696 1.00 31.15 N ANISOU 1849 N ASN A 403 3320 5104 3411 807 -492 868 N ATOM 1850 CA ASN A 403 17.375 34.339 -24.717 1.00 36.92 C ANISOU 1850 CA ASN A 403 4079 5853 4094 864 -670 849 C ATOM 1851 C ASN A 403 15.933 34.066 -24.268 1.00 36.64 C ANISOU 1851 C ASN A 403 4003 5669 4250 798 -759 877 C ATOM 1852 O ASN A 403 15.019 33.946 -25.089 1.00 38.63 O ANISOU 1852 O ASN A 403 4250 5911 4517 825 -892 911 O ATOM 1853 CB ASN A 403 18.032 33.038 -25.177 1.00 36.73 C ANISOU 1853 CB ASN A 403 4148 5895 3914 947 -790 709 C ATOM 1854 CG ASN A 403 19.238 33.280 -26.056 1.00 42.47 C ANISOU 1854 CG ASN A 403 4920 6785 4432 1049 -733 709 C ATOM 1855 OD1 ASN A 403 19.443 34.386 -26.552 1.00 46.71 O ANISOU 1855 OD1 ASN A 403 5415 7395 4938 1071 -633 823 O ATOM 1856 ND2 ASN A 403 20.045 32.247 -26.251 1.00 40.96 N ANISOU 1856 ND2 ASN A 403 4808 6649 4107 1116 -789 590 N ATOM 1857 N ARG A 404 15.732 33.965 -22.962 1.00 27.60 N ANISOU 1857 N ARG A 404 2826 4407 3252 718 -688 870 N ATOM 1858 CA ARG A 404 14.405 33.701 -22.415 1.00 33.79 C ANISOU 1858 CA ARG A 404 3560 5043 4235 662 -748 916 C ATOM 1859 C ARG A 404 13.909 34.847 -21.542 1.00 30.99 C ANISOU 1859 C ARG A 404 3136 4602 4038 586 -583 1034 C ATOM 1860 O ARG A 404 13.001 34.665 -20.736 1.00 31.23 O ANISOU 1860 O ARG A 404 3124 4500 4240 539 -579 1076 O ATOM 1861 CB ARG A 404 14.408 32.402 -21.606 1.00 37.12 C ANISOU 1861 CB ARG A 404 4003 5389 4712 650 -822 814 C ATOM 1862 CG ARG A 404 14.408 31.143 -22.460 1.00 58.33 C ANISOU 1862 CG ARG A 404 6743 8108 7313 718 -1032 709 C ATOM 1863 CD ARG A 404 13.550 30.057 -21.826 1.00 72.01 C ANISOU 1863 CD ARG A 404 8439 9699 9220 691 -1154 685 C ATOM 1864 NE ARG A 404 13.229 28.990 -22.772 1.00 80.57 N ANISOU 1864 NE ARG A 404 9561 10784 10268 754 -1390 605 N ATOM 1865 CZ ARG A 404 12.224 28.133 -22.619 1.00 81.79 C ANISOU 1865 CZ ARG A 404 9669 10807 10600 742 -1552 612 C ATOM 1866 NH1 ARG A 404 11.435 28.222 -21.560 1.00 82.94 N ANISOU 1866 NH1 ARG A 404 9727 10817 10968 675 -1485 709 N ATOM 1867 NH2 ARG A 404 12.007 27.192 -23.527 1.00 85.38 N ANISOU 1867 NH2 ARG A 404 10166 11260 11014 806 -1783 525 N ATOM 1868 N CYS A 405 14.504 36.024 -21.724 1.00 26.67 N ANISOU 1868 N CYS A 405 3245 3430 3460 992 -195 294 N ATOM 1869 CA CYS A 405 14.258 37.181 -20.870 1.00 26.31 C ANISOU 1869 CA CYS A 405 3162 3418 3415 899 -119 354 C ATOM 1870 C CYS A 405 12.772 37.495 -20.661 1.00 29.40 C ANISOU 1870 C CYS A 405 3539 3764 3869 881 -201 340 C ATOM 1871 O CYS A 405 12.327 37.713 -19.526 1.00 26.62 O ANISOU 1871 O CYS A 405 3107 3412 3597 790 -185 394 O ATOM 1872 CB CYS A 405 14.997 38.420 -21.437 1.00 35.91 C ANISOU 1872 CB CYS A 405 4463 4680 4502 932 6 383 C ATOM 1873 SG CYS A 405 14.569 39.989 -20.645 1.00119.28 S ANISOU 1873 SG CYS A 405 14997 15275 15049 838 92 441 S ATOM 1874 N GLN A 406 12.006 37.545 -21.751 1.00 26.66 N ANISOU 1874 N GLN A 406 3274 3372 3482 977 -288 274 N ATOM 1875 CA GLN A 406 10.583 37.878 -21.658 1.00 31.48 C ANISOU 1875 CA GLN A 406 3875 3928 4158 964 -369 265 C ATOM 1876 C GLN A 406 9.826 36.877 -20.775 1.00 28.10 C ANISOU 1876 C GLN A 406 3325 3428 3923 913 -462 277 C ATOM 1877 O GLN A 406 9.068 37.259 -19.898 1.00 26.93 O ANISOU 1877 O GLN A 406 3119 3256 3858 842 -451 339 O ATOM 1878 CB GLN A 406 9.948 37.918 -23.047 1.00 40.12 C ANISOU 1878 CB GLN A 406 5079 4980 5186 1094 -467 177 C ATOM 1879 CG GLN A 406 8.515 38.408 -23.037 1.00 60.45 C ANISOU 1879 CG GLN A 406 7652 7496 7819 1079 -542 173 C ATOM 1880 CD GLN A 406 8.127 39.063 -24.347 1.00 79.13 C ANISOU 1880 CD GLN A 406 10149 9864 10054 1199 -572 109 C ATOM 1881 OE1 GLN A 406 7.957 38.389 -25.366 1.00 85.11 O ANISOU 1881 OE1 GLN A 406 10973 10574 10792 1326 -695 12 O ATOM 1882 NE2 GLN A 406 7.988 40.386 -24.328 1.00 83.33 N ANISOU 1882 NE2 GLN A 406 10721 10450 10490 1168 -457 160 N ATOM 1883 N GLU A 407 10.061 35.596 -21.007 1.00 28.97 N ANISOU 1883 N GLU A 407 3397 3502 4108 958 -543 226 N ATOM 1884 CA GLU A 407 9.410 34.551 -20.234 1.00 30.65 C ANISOU 1884 CA GLU A 407 3479 3641 4526 929 -621 238 C ATOM 1885 C GLU A 407 9.798 34.641 -18.757 1.00 26.96 C ANISOU 1885 C GLU A 407 2910 3219 4115 827 -507 340 C ATOM 1886 O GLU A 407 8.964 34.487 -17.874 1.00 29.38 O ANISOU 1886 O GLU A 407 3127 3467 4568 794 -523 395 O ATOM 1887 CB GLU A 407 9.795 33.178 -20.789 1.00 32.80 C ANISOU 1887 CB GLU A 407 3726 3880 4855 997 -708 162 C ATOM 1888 CG GLU A 407 9.277 32.023 -19.950 1.00 48.00 C ANISOU 1888 CG GLU A 407 5494 5734 7011 972 -764 180 C ATOM 1889 CD GLU A 407 9.892 30.691 -20.344 1.00 64.60 C ANISOU 1889 CD GLU A 407 7559 7827 9159 1020 -815 119 C ATOM 1890 OE1 GLU A 407 9.856 30.346 -21.548 1.00 60.32 O ANISOU 1890 OE1 GLU A 407 7106 7250 8565 1116 -922 21 O ATOM 1891 OE2 GLU A 407 10.416 29.995 -19.446 1.00 71.97 O ANISOU 1891 OE2 GLU A 407 8380 8790 10176 969 -744 171 O ATOM 1892 N LEU A 408 11.069 34.898 -18.489 1.00 22.98 N ANISOU 1892 N LEU A 408 2423 2808 3499 791 -393 368 N ATOM 1893 CA LEU A 408 11.545 34.938 -17.105 1.00 25.42 C ANISOU 1893 CA LEU A 408 2644 3164 3849 710 -297 451 C ATOM 1894 C LEU A 408 11.068 36.185 -16.366 1.00 27.12 C ANISOU 1894 C LEU A 408 2877 3394 4034 653 -235 521 C ATOM 1895 O LEU A 408 10.659 36.124 -15.205 1.00 22.48 O ANISOU 1895 O LEU A 408 2213 2788 3539 617 -210 591 O ATOM 1896 CB LEU A 408 13.068 34.869 -17.079 1.00 19.87 C ANISOU 1896 CB LEU A 408 1955 2547 3047 689 -206 457 C ATOM 1897 CG LEU A 408 13.646 33.571 -17.646 1.00 21.88 C ANISOU 1897 CG LEU A 408 2189 2793 3332 737 -247 407 C ATOM 1898 CD1 LEU A 408 15.159 33.640 -17.729 1.00 26.89 C ANISOU 1898 CD1 LEU A 408 2854 3502 3861 717 -147 428 C ATOM 1899 CD2 LEU A 408 13.212 32.387 -16.789 1.00 24.46 C ANISOU 1899 CD2 LEU A 408 2377 3081 3835 725 -284 424 C ATOM 1900 N ALA A 409 11.135 37.325 -17.037 1.00 22.34 N ANISOU 1900 N ALA A 409 2372 2821 3295 654 -200 508 N ATOM 1901 CA ALA A 409 10.705 38.594 -16.440 1.00 23.35 C ANISOU 1901 CA ALA A 409 2525 2967 3381 598 -135 571 C ATOM 1902 C ALA A 409 9.248 38.594 -16.000 1.00 23.60 C ANISOU 1902 C ALA A 409 2525 2913 3530 593 -194 614 C ATOM 1903 O ALA A 409 8.896 39.241 -15.021 1.00 20.65 O ANISOU 1903 O ALA A 409 2135 2541 3170 544 -139 694 O ATOM 1904 CB ALA A 409 10.936 39.737 -17.423 1.00 22.76 C ANISOU 1904 CB ALA A 409 2556 2933 3158 617 -87 544 C ATOM 1905 N THR A 410 8.394 37.874 -16.727 1.00 21.39 N ANISOU 1905 N THR A 410 2237 2548 3343 652 -310 565 N ATOM 1906 CA THR A 410 6.966 37.885 -16.434 1.00 19.62 C ANISOU 1906 CA THR A 410 1980 2219 3255 653 -372 610 C ATOM 1907 C THR A 410 6.539 36.782 -15.464 1.00 20.48 C ANISOU 1907 C THR A 410 1961 2250 3572 663 -403 663 C ATOM 1908 O THR A 410 5.392 36.762 -15.014 1.00 26.16 O ANISOU 1908 O THR A 410 2637 2868 4435 669 -434 730 O ATOM 1909 CB THR A 410 6.132 37.765 -17.730 1.00 20.76 C ANISOU 1909 CB THR A 410 2179 2292 3416 720 -496 528 C ATOM 1910 OG1 THR A 410 6.599 36.636 -18.481 1.00 28.40 O ANISOU 1910 OG1 THR A 410 3133 3246 4413 789 -584 431 O ATOM 1911 CG2 THR A 410 6.288 39.019 -18.576 1.00 23.03 C ANISOU 1911 CG2 THR A 410 2591 2649 3511 723 -446 501 C ATOM 1912 N ASN A 411 7.466 35.887 -15.137 1.00 23.84 N ANISOU 1912 N ASN A 411 2322 2717 4017 671 -381 644 N ATOM 1913 CA ASN A 411 7.177 34.746 -14.268 1.00 25.81 C ANISOU 1913 CA ASN A 411 2439 2902 4466 697 -394 690 C ATOM 1914 C ASN A 411 7.144 35.089 -12.785 1.00 27.75 C ANISOU 1914 C ASN A 411 2640 3164 4742 671 -288 811 C ATOM 1915 O ASN A 411 7.937 35.893 -12.308 1.00 23.20 O ANISOU 1915 O ASN A 411 2117 2685 4013 625 -198 834 O ATOM 1916 CB ASN A 411 8.212 33.638 -14.492 1.00 21.87 C ANISOU 1916 CB ASN A 411 1888 2452 3970 717 -400 626 C ATOM 1917 CG ASN A 411 7.914 32.405 -13.676 1.00 28.09 C ANISOU 1917 CG ASN A 411 2525 3175 4973 753 -404 669 C ATOM 1918 OD1 ASN A 411 6.996 31.631 -13.989 1.00 30.07 O ANISOU 1918 OD1 ASN A 411 2703 3308 5417 805 -501 649 O ATOM 1919 ND2 ASN A 411 8.664 32.222 -12.609 1.00 19.38 N ANISOU 1919 ND2 ASN A 411 1367 2142 3852 734 -298 728 N ATOM 1920 N GLU A 412 6.249 34.428 -12.058 1.00 24.53 N ANISOU 1920 N GLU A 412 2128 2648 4543 716 -300 887 N ATOM 1921 CA GLU A 412 6.070 34.631 -10.627 1.00 26.68 C ANISOU 1921 CA GLU A 412 2360 2913 4864 728 -201 1014 C ATOM 1922 C GLU A 412 7.342 34.486 -9.779 1.00 19.88 C ANISOU 1922 C GLU A 412 1481 2172 3900 717 -106 1021 C ATOM 1923 O GLU A 412 7.460 35.148 -8.746 1.00 23.93 O ANISOU 1923 O GLU A 412 2023 2719 4349 715 -25 1102 O ATOM 1924 CB GLU A 412 5.002 33.670 -10.089 1.00 26.63 C ANISOU 1924 CB GLU A 412 2225 2759 5136 808 -223 1094 C ATOM 1925 CG GLU A 412 5.326 32.228 -10.357 1.00 28.39 C ANISOU 1925 CG GLU A 412 2324 2960 5503 854 -268 1031 C ATOM 1926 CD GLU A 412 4.217 31.280 -9.890 1.00 35.95 C ANISOU 1926 CD GLU A 412 3173 3762 6723 860 -262 1089 C ATOM 1927 OE1 GLU A 412 3.400 31.706 -9.055 1.00 33.29 O ANISOU 1927 OE1 GLU A 412 2843 3359 6446 845 -188 1205 O ATOM 1928 OE2 GLU A 412 4.183 30.120 -10.356 1.00 36.73 O ANISOU 1928 OE2 GLU A 412 3181 3806 6969 875 -324 1021 O ATOM 1929 N TYR A 413 8.287 33.640 -10.196 1.00 20.27 N ANISOU 1929 N TYR A 413 1488 2282 3932 715 -120 940 N ATOM 1930 CA TYR A 413 9.540 33.491 -9.442 1.00 21.13 C ANISOU 1930 CA TYR A 413 1578 2503 3946 700 -35 945 C ATOM 1931 C TYR A 413 10.761 34.035 -10.168 1.00 24.27 C ANISOU 1931 C TYR A 413 2064 3010 4147 633 -28 862 C ATOM 1932 O TYR A 413 11.620 34.653 -9.550 1.00 24.94 O ANISOU 1932 O TYR A 413 2183 3179 4114 599 39 879 O ATOM 1933 CB TYR A 413 9.822 32.028 -9.059 1.00 25.11 C ANISOU 1933 CB TYR A 413 1946 2999 4597 753 -19 947 C ATOM 1934 CG TYR A 413 8.707 31.419 -8.258 1.00 28.28 C ANISOU 1934 CG TYR A 413 2239 3286 5221 839 -3 1043 C ATOM 1935 CD1 TYR A 413 8.375 31.928 -7.007 1.00 34.49 C ANISOU 1935 CD1 TYR A 413 3040 4060 6004 870 83 1155 C ATOM 1936 CD2 TYR A 413 7.971 30.348 -8.755 1.00 31.88 C ANISOU 1936 CD2 TYR A 413 2605 3630 5878 866 -64 1020 C ATOM 1937 CE1 TYR A 413 7.330 31.385 -6.268 1.00 37.49 C ANISOU 1937 CE1 TYR A 413 3376 4320 6548 888 137 1247 C ATOM 1938 CE2 TYR A 413 6.923 29.797 -8.021 1.00 38.59 C ANISOU 1938 CE2 TYR A 413 3397 4351 6913 874 -19 1107 C ATOM 1939 CZ TYR A 413 6.615 30.321 -6.780 1.00 38.32 C ANISOU 1939 CZ TYR A 413 3392 4311 6856 885 91 1227 C ATOM 1940 OH TYR A 413 5.586 29.783 -6.047 1.00 40.88 O ANISOU 1940 OH TYR A 413 3654 4511 7367 901 154 1328 O ATOM 1941 N ALA A 414 10.846 33.788 -11.470 1.00 23.65 N ANISOU 1941 N ALA A 414 2020 2920 4044 628 -97 776 N ATOM 1942 CA ALA A 414 12.060 34.150 -12.196 1.00 22.43 C ANISOU 1942 CA ALA A 414 1942 2855 3726 588 -76 712 C ATOM 1943 C ALA A 414 12.200 35.672 -12.331 1.00 21.13 C ANISOU 1943 C ALA A 414 1885 2731 3412 543 -38 722 C ATOM 1944 O ALA A 414 13.290 36.181 -12.633 1.00 20.92 O ANISOU 1944 O ALA A 414 1909 2776 3264 511 9 696 O ATOM 1945 CB ALA A 414 12.124 33.438 -13.550 1.00 19.81 C ANISOU 1945 CB ALA A 414 1630 2495 3400 622 -155 625 C ATOM 1946 N ASN A 415 11.136 36.421 -12.052 1.00 20.44 N ANISOU 1946 N ASN A 415 1826 2593 3346 541 -47 768 N ATOM 1947 CA ASN A 415 11.288 37.873 -12.116 1.00 17.91 C ANISOU 1947 CA ASN A 415 1598 2317 2889 496 1 781 C ATOM 1948 C ASN A 415 12.348 38.365 -11.123 1.00 20.13 C ANISOU 1948 C ASN A 415 1873 2678 3098 457 80 810 C ATOM 1949 O ASN A 415 12.966 39.394 -11.340 1.00 18.86 O ANISOU 1949 O ASN A 415 1772 2568 2827 418 123 795 O ATOM 1950 CB ASN A 415 9.957 38.611 -11.923 1.00 21.57 C ANISOU 1950 CB ASN A 415 2095 2714 3385 494 -12 838 C ATOM 1951 CG ASN A 415 9.498 38.623 -10.483 1.00 26.87 C ANISOU 1951 CG ASN A 415 2722 3358 4130 504 27 938 C ATOM 1952 OD1 ASN A 415 9.908 39.481 -9.706 1.00 23.29 O ANISOU 1952 OD1 ASN A 415 2304 2956 3589 474 90 976 O ATOM 1953 ND2 ASN A 415 8.632 37.667 -10.117 1.00 23.64 N ANISOU 1953 ND2 ASN A 415 2234 2858 3890 559 -8 983 N ATOM 1954 N TYR A 416 12.550 37.625 -10.036 1.00 17.73 N ANISOU 1954 N TYR A 416 1491 2380 2867 478 98 849 N ATOM 1955 CA TYR A 416 13.579 37.988 -9.060 1.00 17.21 C ANISOU 1955 CA TYR A 416 1416 2384 2737 455 155 866 C ATOM 1956 C TYR A 416 14.981 37.852 -9.640 1.00 19.48 C ANISOU 1956 C TYR A 416 1705 2736 2959 421 173 806 C ATOM 1957 O TYR A 416 15.890 38.619 -9.289 1.00 20.00 O ANISOU 1957 O TYR A 416 1794 2852 2952 385 210 801 O ATOM 1958 CB TYR A 416 13.451 37.130 -7.798 1.00 17.54 C ANISOU 1958 CB TYR A 416 1375 2418 2869 509 173 922 C ATOM 1959 CG TYR A 416 12.218 37.491 -6.989 1.00 20.32 C ANISOU 1959 CG TYR A 416 1739 2703 3277 554 180 1009 C ATOM 1960 CD1 TYR A 416 12.223 38.596 -6.159 1.00 21.82 C ANISOU 1960 CD1 TYR A 416 1994 2914 3383 547 212 1052 C ATOM 1961 CD2 TYR A 416 11.064 36.729 -7.066 1.00 22.09 C ANISOU 1961 CD2 TYR A 416 1911 2834 3649 610 154 1053 C ATOM 1962 CE1 TYR A 416 11.120 38.943 -5.419 1.00 25.67 C ANISOU 1962 CE1 TYR A 416 2506 3335 3912 597 228 1145 C ATOM 1963 CE2 TYR A 416 9.934 37.078 -6.334 1.00 26.09 C ANISOU 1963 CE2 TYR A 416 2430 3263 4220 659 172 1153 C ATOM 1964 CZ TYR A 416 9.979 38.182 -5.506 1.00 26.77 C ANISOU 1964 CZ TYR A 416 2594 3376 4201 654 214 1203 C ATOM 1965 OH TYR A 416 8.879 38.534 -4.770 1.00 29.01 O ANISOU 1965 OH TYR A 416 2904 3578 4541 711 240 1315 O ATOM 1966 N ILE A 417 15.165 36.869 -10.516 1.00 17.65 N ANISOU 1966 N ILE A 417 1448 2493 2765 440 145 765 N ATOM 1967 CA ILE A 417 16.464 36.692 -11.155 1.00 18.13 C ANISOU 1967 CA ILE A 417 1520 2600 2768 418 172 724 C ATOM 1968 C ILE A 417 16.738 37.885 -12.066 1.00 21.29 C ANISOU 1968 C ILE A 417 2012 3008 3071 399 193 701 C ATOM 1969 O ILE A 417 17.830 38.468 -12.060 1.00 19.92 O ANISOU 1969 O ILE A 417 1852 2871 2847 369 243 701 O ATOM 1970 CB ILE A 417 16.522 35.423 -12.038 1.00 21.78 C ANISOU 1970 CB ILE A 417 1955 3040 3279 454 135 686 C ATOM 1971 CG1 ILE A 417 16.198 34.156 -11.236 1.00 27.20 C ANISOU 1971 CG1 ILE A 417 2533 3714 4087 481 124 709 C ATOM 1972 CG2 ILE A 417 17.900 35.312 -12.716 1.00 20.21 C ANISOU 1972 CG2 ILE A 417 1784 2882 3014 439 177 664 C ATOM 1973 CD1 ILE A 417 17.093 33.952 -10.078 1.00 42.38 C ANISOU 1973 CD1 ILE A 417 4394 5698 6008 461 185 744 C ATOM 1974 N ILE A 418 15.749 38.220 -12.882 1.00 19.00 N ANISOU 1974 N ILE A 418 1777 2674 2767 425 156 684 N ATOM 1975 CA ILE A 418 15.932 39.305 -13.833 1.00 18.51 C ANISOU 1975 CA ILE A 418 1800 2620 2613 426 189 664 C ATOM 1976 C ILE A 418 16.176 40.603 -13.052 1.00 21.60 C ANISOU 1976 C ILE A 418 2201 3043 2965 374 246 699 C ATOM 1977 O ILE A 418 17.031 41.410 -13.410 1.00 19.20 O ANISOU 1977 O ILE A 418 1922 2762 2611 360 305 693 O ATOM 1978 CB ILE A 418 14.711 39.450 -14.757 1.00 19.95 C ANISOU 1978 CB ILE A 418 2040 2754 2787 470 135 639 C ATOM 1979 CG1 ILE A 418 14.515 38.162 -15.574 1.00 20.60 C ANISOU 1979 CG1 ILE A 418 2115 2797 2915 532 59 589 C ATOM 1980 CG2 ILE A 418 14.881 40.692 -15.670 1.00 17.82 C ANISOU 1980 CG2 ILE A 418 1855 2501 2413 483 190 626 C ATOM 1981 CD1 ILE A 418 15.794 37.723 -16.360 1.00 20.26 C ANISOU 1981 CD1 ILE A 418 2099 2782 2817 565 93 561 C ATOM 1982 N GLN A 419 15.424 40.805 -11.975 1.00 17.72 N ANISOU 1982 N GLN A 419 1686 2540 2505 354 231 739 N ATOM 1983 CA GLN A 419 15.667 41.973 -11.138 1.00 18.02 C ANISOU 1983 CA GLN A 419 1736 2605 2505 312 273 767 C ATOM 1984 C GLN A 419 17.065 41.991 -10.557 1.00 16.81 C ANISOU 1984 C GLN A 419 1541 2493 2351 287 301 757 C ATOM 1985 O GLN A 419 17.686 43.051 -10.476 1.00 21.56 O ANISOU 1985 O GLN A 419 2158 3112 2922 256 340 753 O ATOM 1986 CB GLN A 419 14.674 42.050 -9.982 1.00 16.54 C ANISOU 1986 CB GLN A 419 1542 2394 2350 315 253 823 C ATOM 1987 CG GLN A 419 13.301 42.544 -10.375 1.00 16.58 C ANISOU 1987 CG GLN A 419 1597 2351 2352 321 240 852 C ATOM 1988 CD GLN A 419 12.416 42.635 -9.157 1.00 23.45 C ANISOU 1988 CD GLN A 419 2463 3185 3261 334 236 928 C ATOM 1989 OE1 GLN A 419 12.577 43.531 -8.329 1.00 21.57 O ANISOU 1989 OE1 GLN A 419 2253 2969 2973 314 268 959 O ATOM 1990 NE2 GLN A 419 11.507 41.690 -9.019 1.00 18.59 N ANISOU 1990 NE2 GLN A 419 1812 2507 2744 380 198 964 N ATOM 1991 N HIS A 420 17.541 40.830 -10.110 1.00 17.39 N ANISOU 1991 N HIS A 420 1556 2578 2475 302 282 756 N ATOM 1992 CA HIS A 420 18.886 40.772 -9.548 1.00 20.75 C ANISOU 1992 CA HIS A 420 1939 3039 2908 278 303 748 C ATOM 1993 C HIS A 420 19.923 41.236 -10.578 1.00 23.97 C ANISOU 1993 C HIS A 420 2365 3446 3296 262 347 726 C ATOM 1994 O HIS A 420 20.824 42.015 -10.270 1.00 19.71 O ANISOU 1994 O HIS A 420 1812 2914 2762 233 374 725 O ATOM 1995 CB HIS A 420 19.239 39.362 -9.091 1.00 21.61 C ANISOU 1995 CB HIS A 420 1979 3164 3069 299 288 752 C ATOM 1996 CG HIS A 420 20.615 39.269 -8.514 1.00 21.26 C ANISOU 1996 CG HIS A 420 1889 3154 3034 275 307 746 C ATOM 1997 ND1 HIS A 420 21.712 38.862 -9.248 1.00 26.33 N ANISOU 1997 ND1 HIS A 420 2516 3801 3688 258 336 736 N ATOM 1998 CD2 HIS A 420 21.086 39.619 -7.296 1.00 22.23 C ANISOU 1998 CD2 HIS A 420 1987 3302 3158 269 297 750 C ATOM 1999 CE1 HIS A 420 22.794 38.928 -8.490 1.00 23.21 C ANISOU 1999 CE1 HIS A 420 2077 3428 3314 233 344 738 C ATOM 2000 NE2 HIS A 420 22.440 39.377 -7.299 1.00 34.08 N ANISOU 2000 NE2 HIS A 420 3447 4820 4682 242 313 738 N ATOM 2001 N ILE A 421 19.805 40.737 -11.802 1.00 18.01 N ANISOU 2001 N ILE A 421 1640 2673 2529 295 354 713 N ATOM 2002 CA ILE A 421 20.772 41.097 -12.845 1.00 18.95 C ANISOU 2002 CA ILE A 421 1786 2781 2632 309 412 709 C ATOM 2003 C ILE A 421 20.711 42.591 -13.164 1.00 20.33 C ANISOU 2003 C ILE A 421 1999 2946 2778 302 461 713 C ATOM 2004 O ILE A 421 21.738 43.267 -13.188 1.00 20.93 O ANISOU 2004 O ILE A 421 2053 3014 2883 288 515 725 O ATOM 2005 CB ILE A 421 20.565 40.252 -14.122 1.00 19.23 C ANISOU 2005 CB ILE A 421 1868 2796 2644 372 405 693 C ATOM 2006 CG1 ILE A 421 20.785 38.765 -13.807 1.00 20.44 C ANISOU 2006 CG1 ILE A 421 1968 2957 2839 373 368 690 C ATOM 2007 CG2 ILE A 421 21.500 40.741 -15.249 1.00 20.85 C ANISOU 2007 CG2 ILE A 421 2119 2979 2824 415 481 705 C ATOM 2008 CD1 ILE A 421 20.210 37.799 -14.885 1.00 21.84 C ANISOU 2008 CD1 ILE A 421 2187 3108 3004 439 325 661 C ATOM 2009 N VAL A 422 19.501 43.108 -13.386 1.00 21.99 N ANISOU 2009 N VAL A 422 2256 3153 2945 312 446 707 N ATOM 2010 CA VAL A 422 19.320 44.522 -13.717 1.00 21.91 C ANISOU 2010 CA VAL A 422 2279 3141 2904 307 504 713 C ATOM 2011 C VAL A 422 19.844 45.445 -12.604 1.00 21.20 C ANISOU 2011 C VAL A 422 2144 3062 2848 248 517 724 C ATOM 2012 O VAL A 422 20.422 46.483 -12.880 1.00 21.12 O ANISOU 2012 O VAL A 422 2126 3043 2856 242 582 728 O ATOM 2013 CB VAL A 422 17.839 44.831 -14.068 1.00 21.91 C ANISOU 2013 CB VAL A 422 2337 3136 2853 322 481 711 C ATOM 2014 CG1 VAL A 422 17.570 46.341 -14.176 1.00 19.40 C ANISOU 2014 CG1 VAL A 422 2043 2826 2500 302 548 725 C ATOM 2015 CG2 VAL A 422 17.473 44.123 -15.378 1.00 23.65 C ANISOU 2015 CG2 VAL A 422 2610 3337 3040 398 464 685 C ATOM 2016 N SER A 423 19.674 45.036 -11.352 1.00 17.74 N ANISOU 2016 N SER A 423 1674 2637 2428 217 457 727 N ATOM 2017 CA SER A 423 20.020 45.870 -10.208 1.00 18.83 C ANISOU 2017 CA SER A 423 1786 2783 2585 177 446 728 C ATOM 2018 C SER A 423 21.505 45.883 -9.863 1.00 22.62 C ANISOU 2018 C SER A 423 2203 3257 3134 160 450 713 C ATOM 2019 O SER A 423 21.983 46.779 -9.168 1.00 26.95 O ANISOU 2019 O SER A 423 2726 3798 3714 134 441 701 O ATOM 2020 CB SER A 423 19.226 45.386 -8.981 1.00 25.46 C ANISOU 2020 CB SER A 423 2629 3634 3409 181 381 744 C ATOM 2021 OG SER A 423 17.844 45.609 -9.202 1.00 33.83 O ANISOU 2021 OG SER A 423 3744 4682 4428 190 381 771 O ATOM 2022 N ASN A 424 22.244 44.888 -10.336 1.00 19.90 N ANISOU 2022 N ASN A 424 1833 2909 2821 177 458 715 N ATOM 2023 CA ASN A 424 23.633 44.754 -9.908 1.00 19.69 C ANISOU 2023 CA ASN A 424 1742 2869 2870 157 455 711 C ATOM 2024 C ASN A 424 24.624 45.425 -10.870 1.00 22.58 C ANISOU 2024 C ASN A 424 2089 3187 3302 166 534 728 C ATOM 2025 O ASN A 424 24.770 45.003 -12.016 1.00 21.93 O ANISOU 2025 O ASN A 424 2034 3088 3210 207 590 751 O ATOM 2026 CB ASN A 424 23.996 43.278 -9.722 1.00 25.35 C ANISOU 2026 CB ASN A 424 2430 3606 3596 166 430 718 C ATOM 2027 CG ASN A 424 25.342 43.094 -9.026 1.00 34.36 C ANISOU 2027 CG ASN A 424 3503 4740 4813 140 414 716 C ATOM 2028 OD1 ASN A 424 26.126 44.034 -8.896 1.00 35.90 O ANISOU 2028 OD1 ASN A 424 3667 4898 5075 120 423 709 O ATOM 2029 ND2 ASN A 424 25.599 41.891 -8.566 1.00 34.21 N ANISOU 2029 ND2 ASN A 424 3452 4751 4797 143 391 721 N ATOM 2030 N ASP A 425 25.295 46.472 -10.396 1.00 21.20 N ANISOU 2030 N ASP A 425 1867 2982 3204 139 537 718 N ATOM 2031 CA ASP A 425 26.276 47.192 -11.208 1.00 25.56 C ANISOU 2031 CA ASP A 425 2382 3472 3858 157 621 744 C ATOM 2032 C ASP A 425 27.381 46.273 -11.719 1.00 23.91 C ANISOU 2032 C ASP A 425 2144 3226 3713 177 655 783 C ATOM 2033 O ASP A 425 27.918 46.490 -12.807 1.00 22.11 O ANISOU 2033 O ASP A 425 1920 2946 3535 227 751 830 O ATOM 2034 CB ASP A 425 26.895 48.342 -10.408 1.00 24.62 C ANISOU 2034 CB ASP A 425 2194 3314 3846 121 595 719 C ATOM 2035 CG ASP A 425 25.940 49.523 -10.242 1.00 31.08 C ANISOU 2035 CG ASP A 425 3041 4150 4616 110 603 698 C ATOM 2036 OD1 ASP A 425 24.954 49.636 -11.015 1.00 25.82 O ANISOU 2036 OD1 ASP A 425 2440 3513 3856 135 658 714 O ATOM 2037 OD2 ASP A 425 26.189 50.347 -9.344 1.00 29.20 O ANISOU 2037 OD2 ASP A 425 2763 3895 4437 79 551 663 O ATOM 2038 N ASP A 426 27.719 45.246 -10.942 1.00 20.25 N ANISOU 2038 N ASP A 426 1656 2790 3247 148 587 773 N ATOM 2039 CA ASP A 426 28.729 44.291 -11.385 1.00 23.64 C ANISOU 2039 CA ASP A 426 2063 3191 3729 159 622 818 C ATOM 2040 C ASP A 426 28.245 43.392 -12.532 1.00 23.93 C ANISOU 2040 C ASP A 426 2173 3244 3677 213 672 847 C ATOM 2041 O ASP A 426 29.021 42.615 -13.091 1.00 24.16 O ANISOU 2041 O ASP A 426 2201 3244 3734 235 717 894 O ATOM 2042 CB ASP A 426 29.278 43.465 -10.211 1.00 24.00 C ANISOU 2042 CB ASP A 426 2054 3265 3799 114 544 800 C ATOM 2043 CG ASP A 426 30.122 44.305 -9.253 1.00 28.64 C ANISOU 2043 CG ASP A 426 2568 3813 4503 77 491 773 C ATOM 2044 OD1 ASP A 426 29.937 44.200 -8.029 1.00 27.75 O ANISOU 2044 OD1 ASP A 426 2438 3743 4363 57 399 724 O ATOM 2045 OD2 ASP A 426 30.955 45.101 -9.722 1.00 24.42 O ANISOU 2045 OD2 ASP A 426 1990 3195 4095 81 541 802 O ATOM 2046 N LEU A 427 26.969 43.519 -12.897 1.00 19.58 N ANISOU 2046 N LEU A 427 1688 2729 3022 239 661 819 N ATOM 2047 CA LEU A 427 26.440 42.813 -14.052 1.00 19.91 C ANISOU 2047 CA LEU A 427 1804 2775 2984 305 692 832 C ATOM 2048 C LEU A 427 25.968 43.791 -15.131 1.00 24.09 C ANISOU 2048 C LEU A 427 2394 3279 3478 372 762 839 C ATOM 2049 O LEU A 427 25.092 43.459 -15.930 1.00 23.50 O ANISOU 2049 O LEU A 427 2395 3220 3313 429 757 824 O ATOM 2050 CB LEU A 427 25.280 41.894 -13.618 1.00 19.39 C ANISOU 2050 CB LEU A 427 1761 2768 2839 293 608 791 C ATOM 2051 CG LEU A 427 25.710 40.742 -12.695 1.00 18.79 C ANISOU 2051 CG LEU A 427 1625 2722 2791 251 560 790 C ATOM 2052 CD1 LEU A 427 24.486 39.949 -12.185 1.00 18.34 C ANISOU 2052 CD1 LEU A 427 1573 2710 2685 252 490 759 C ATOM 2053 CD2 LEU A 427 26.683 39.807 -13.408 1.00 19.01 C ANISOU 2053 CD2 LEU A 427 1654 2727 2843 275 608 831 C ATOM 2054 N ALA A 428 26.572 44.979 -15.158 1.00 26.98 N ANISOU 2054 N ALA A 428 2721 3603 3926 372 826 862 N ATOM 2055 CA ALA A 428 26.087 46.085 -15.990 1.00 26.34 C ANISOU 2055 CA ALA A 428 2680 3508 3822 432 905 869 C ATOM 2056 C ALA A 428 25.918 45.720 -17.463 1.00 25.54 C ANISOU 2056 C ALA A 428 2668 3387 3647 552 976 897 C ATOM 2057 O ALA A 428 24.906 46.065 -18.071 1.00 24.55 O ANISOU 2057 O ALA A 428 2609 3288 3429 602 985 873 O ATOM 2058 CB ALA A 428 26.991 47.296 -15.844 1.00 28.75 C ANISOU 2058 CB ALA A 428 2906 3752 4263 425 978 900 C ATOM 2059 N VAL A 429 26.900 45.027 -18.041 1.00 24.70 N ANISOU 2059 N VAL A 429 2571 3232 3580 609 1025 951 N ATOM 2060 CA VAL A 429 26.787 44.640 -19.445 1.00 27.28 C ANISOU 2060 CA VAL A 429 3002 3537 3828 747 1088 979 C ATOM 2061 C VAL A 429 25.555 43.753 -19.705 1.00 28.28 C ANISOU 2061 C VAL A 429 3210 3720 3815 763 987 912 C ATOM 2062 O VAL A 429 24.884 43.879 -20.737 1.00 26.90 O ANISOU 2062 O VAL A 429 3129 3547 3547 871 1008 897 O ATOM 2063 CB VAL A 429 28.084 43.977 -19.978 1.00 32.32 C ANISOU 2063 CB VAL A 429 3645 4103 4530 809 1161 1062 C ATOM 2064 CG1 VAL A 429 28.180 42.534 -19.505 1.00 28.84 C ANISOU 2064 CG1 VAL A 429 3204 3694 4058 747 1067 1043 C ATOM 2065 CG2 VAL A 429 28.121 44.044 -21.476 1.00 41.39 C ANISOU 2065 CG2 VAL A 429 4903 5207 5615 987 1264 1111 C ATOM 2066 N TYR A 430 25.227 42.891 -18.751 1.00 23.75 N ANISOU 2066 N TYR A 430 2597 3188 3238 664 877 871 N ATOM 2067 CA TYR A 430 24.053 42.017 -18.876 1.00 23.44 C ANISOU 2067 CA TYR A 430 2609 3188 3109 673 775 810 C ATOM 2068 C TYR A 430 22.735 42.747 -18.584 1.00 28.81 C ANISOU 2068 C TYR A 430 3299 3902 3744 643 727 762 C ATOM 2069 O TYR A 430 21.698 42.486 -19.203 1.00 27.23 O ANISOU 2069 O TYR A 430 3168 3709 3471 697 676 722 O ATOM 2070 CB TYR A 430 24.249 40.746 -18.025 1.00 24.50 C ANISOU 2070 CB TYR A 430 2688 3346 3277 598 697 799 C ATOM 2071 CG TYR A 430 25.526 40.055 -18.462 1.00 27.11 C ANISOU 2071 CG TYR A 430 3021 3639 3641 632 757 856 C ATOM 2072 CD1 TYR A 430 25.603 39.437 -19.710 1.00 26.74 C ANISOU 2072 CD1 TYR A 430 3069 3560 3530 749 780 869 C ATOM 2073 CD2 TYR A 430 26.669 40.087 -17.674 1.00 26.57 C ANISOU 2073 CD2 TYR A 430 2868 3559 3669 560 791 903 C ATOM 2074 CE1 TYR A 430 26.781 38.817 -20.143 1.00 25.14 C ANISOU 2074 CE1 TYR A 430 2882 3316 3356 788 847 938 C ATOM 2075 CE2 TYR A 430 27.866 39.478 -18.104 1.00 30.69 C ANISOU 2075 CE2 TYR A 430 3393 4036 4231 590 857 972 C ATOM 2076 CZ TYR A 430 27.909 38.853 -19.340 1.00 31.44 C ANISOU 2076 CZ TYR A 430 3588 4099 4258 703 891 996 C ATOM 2077 OH TYR A 430 29.081 38.270 -19.780 1.00 32.19 O ANISOU 2077 OH TYR A 430 3698 4143 4391 740 966 1080 O ATOM 2078 N ARG A 431 22.783 43.676 -17.648 1.00 21.96 N ANISOU 2078 N ARG A 431 2367 3049 2926 560 740 769 N ATOM 2079 CA ARG A 431 21.661 44.575 -17.444 1.00 23.23 C ANISOU 2079 CA ARG A 431 2544 3235 3046 536 725 744 C ATOM 2080 C ARG A 431 21.267 45.251 -18.767 1.00 22.96 C ANISOU 2080 C ARG A 431 2590 3188 2944 643 798 745 C ATOM 2081 O ARG A 431 20.088 45.368 -19.105 1.00 22.04 O ANISOU 2081 O ARG A 431 2527 3089 2757 665 758 713 O ATOM 2082 CB ARG A 431 22.066 45.630 -16.436 1.00 23.91 C ANISOU 2082 CB ARG A 431 2558 3328 3200 454 753 759 C ATOM 2083 CG ARG A 431 21.234 46.880 -16.504 1.00 24.41 C ANISOU 2083 CG ARG A 431 2641 3405 3227 446 789 753 C ATOM 2084 CD ARG A 431 21.336 47.587 -15.183 1.00 37.28 C ANISOU 2084 CD ARG A 431 4207 5049 4911 350 765 752 C ATOM 2085 NE ARG A 431 22.580 48.305 -15.090 1.00 34.36 N ANISOU 2085 NE ARG A 431 3770 4644 4642 345 833 773 N ATOM 2086 CZ ARG A 431 23.273 48.515 -13.975 1.00 26.29 C ANISOU 2086 CZ ARG A 431 2676 3613 3702 278 793 766 C ATOM 2087 NH1 ARG A 431 22.885 48.051 -12.792 1.00 22.65 N ANISOU 2087 NH1 ARG A 431 2205 3181 3218 220 692 742 N ATOM 2088 NH2 ARG A 431 24.381 49.216 -14.065 1.00 21.27 N ANISOU 2088 NH2 ARG A 431 1974 2926 3180 284 856 786 N ATOM 2089 N GLU A 432 22.261 45.707 -19.519 1.00 25.06 N ANISOU 2089 N GLU A 432 2863 3419 3239 720 910 789 N ATOM 2090 CA GLU A 432 21.964 46.421 -20.756 1.00 26.51 C ANISOU 2090 CA GLU A 432 3121 3593 3359 846 1001 799 C ATOM 2091 C GLU A 432 21.353 45.515 -21.825 1.00 28.24 C ANISOU 2091 C GLU A 432 3450 3808 3471 962 948 764 C ATOM 2092 O GLU A 432 20.414 45.919 -22.522 1.00 28.18 O ANISOU 2092 O GLU A 432 3512 3816 3378 1032 948 733 O ATOM 2093 CB GLU A 432 23.211 47.141 -21.257 1.00 32.88 C ANISOU 2093 CB GLU A 432 3898 4348 4247 919 1151 870 C ATOM 2094 CG GLU A 432 23.633 48.227 -20.281 1.00 34.83 C ANISOU 2094 CG GLU A 432 4034 4592 4609 814 1192 889 C ATOM 2095 CD GLU A 432 24.806 49.047 -20.764 1.00 41.19 C ANISOU 2095 CD GLU A 432 4787 5330 5534 890 1344 963 C ATOM 2096 OE1 GLU A 432 25.228 48.867 -21.927 1.00 38.21 O ANISOU 2096 OE1 GLU A 432 4472 4909 5136 1040 1439 1011 O ATOM 2097 OE2 GLU A 432 25.296 49.872 -19.967 1.00 38.54 O ANISOU 2097 OE2 GLU A 432 4349 4975 5321 808 1367 974 O ATOM 2098 N CYS A 433 21.863 44.289 -21.919 1.00 28.34 N ANISOU 2098 N CYS A 433 3478 3800 3490 980 896 764 N ATOM 2099 CA CYS A 433 21.329 43.292 -22.837 1.00 27.75 C ANISOU 2099 CA CYS A 433 3503 3714 3326 1086 821 720 C ATOM 2100 C CYS A 433 19.854 43.049 -22.542 1.00 32.79 C ANISOU 2100 C CYS A 433 4151 4382 3926 1036 690 646 C ATOM 2101 O CYS A 433 19.012 43.027 -23.446 1.00 27.07 O ANISOU 2101 O CYS A 433 3515 3651 3119 1137 648 600 O ATOM 2102 CB CYS A 433 22.093 41.965 -22.703 1.00 27.09 C ANISOU 2102 CB CYS A 433 3409 3610 3274 1076 778 732 C ATOM 2103 SG CYS A 433 23.838 42.026 -23.219 1.00 47.50 S ANISOU 2103 SG CYS A 433 6001 6137 5911 1156 929 837 S ATOM 2104 N ILE A 434 19.547 42.865 -21.265 1.00 26.00 N ANISOU 2104 N ILE A 434 3201 3545 3134 890 624 639 N ATOM 2105 CA ILE A 434 18.186 42.556 -20.861 1.00 26.59 C ANISOU 2105 CA ILE A 434 3270 3628 3205 842 507 590 C ATOM 2106 C ILE A 434 17.240 43.688 -21.213 1.00 29.16 C ANISOU 2106 C ILE A 434 3638 3966 3476 861 533 581 C ATOM 2107 O ILE A 434 16.168 43.466 -21.779 1.00 27.86 O ANISOU 2107 O ILE A 434 3530 3787 3268 913 455 534 O ATOM 2108 CB ILE A 434 18.104 42.268 -19.362 1.00 25.40 C ANISOU 2108 CB ILE A 434 3017 3495 3140 703 460 605 C ATOM 2109 CG1 ILE A 434 18.640 40.865 -19.089 1.00 26.47 C ANISOU 2109 CG1 ILE A 434 3113 3621 3323 694 405 598 C ATOM 2110 CG2 ILE A 434 16.653 42.417 -18.869 1.00 28.56 C ANISOU 2110 CG2 ILE A 434 3410 3893 3549 657 380 586 C ATOM 2111 CD1 ILE A 434 18.940 40.592 -17.631 1.00 34.69 C ANISOU 2111 CD1 ILE A 434 4052 4685 4443 582 391 624 C ATOM 2112 N ILE A 435 17.636 44.908 -20.880 1.00 21.44 N ANISOU 2112 N ILE A 435 2627 3011 2509 820 642 624 N ATOM 2113 CA ILE A 435 16.805 46.060 -21.191 1.00 28.56 C ANISOU 2113 CA ILE A 435 3561 3931 3358 832 690 625 C ATOM 2114 C ILE A 435 16.558 46.174 -22.703 1.00 32.17 C ANISOU 2114 C ILE A 435 4125 4379 3720 996 722 598 C ATOM 2115 O ILE A 435 15.428 46.372 -23.138 1.00 32.58 O ANISOU 2115 O ILE A 435 4230 4435 3714 1028 674 564 O ATOM 2116 CB ILE A 435 17.434 47.352 -20.657 1.00 25.14 C ANISOU 2116 CB ILE A 435 3068 3520 2966 772 814 675 C ATOM 2117 CG1 ILE A 435 17.444 47.335 -19.123 1.00 28.91 C ANISOU 2117 CG1 ILE A 435 3459 4008 3516 625 761 689 C ATOM 2118 CG2 ILE A 435 16.672 48.563 -21.159 1.00 36.83 C ANISOU 2118 CG2 ILE A 435 4583 5025 4386 801 890 681 C ATOM 2119 CD1 ILE A 435 18.274 48.434 -18.520 1.00 26.38 C ANISOU 2119 CD1 ILE A 435 3071 3697 3257 568 857 726 C ATOM 2120 N GLU A 436 17.613 46.043 -23.501 1.00 34.03 N ANISOU 2120 N GLU A 436 4396 4596 3939 1110 803 620 N ATOM 2121 CA GLU A 436 17.468 46.099 -24.960 1.00 34.24 C ANISOU 2121 CA GLU A 436 4539 4610 3863 1300 840 599 C ATOM 2122 C GLU A 436 16.630 44.929 -25.513 1.00 36.96 C ANISOU 2122 C GLU A 436 4962 4930 4150 1368 675 519 C ATOM 2123 O GLU A 436 15.806 45.113 -26.413 1.00 46.80 O ANISOU 2123 O GLU A 436 6298 6176 5309 1480 643 472 O ATOM 2124 CB GLU A 436 18.850 46.153 -25.636 1.00 38.47 C ANISOU 2124 CB GLU A 436 5098 5115 4406 1423 972 659 C ATOM 2125 CG GLU A 436 19.686 47.381 -25.240 1.00 47.49 C ANISOU 2125 CG GLU A 436 6153 6261 5632 1382 1139 737 C ATOM 2126 CD GLU A 436 21.100 47.374 -25.827 1.00 68.41 C ANISOU 2126 CD GLU A 436 8809 8856 8330 1501 1272 815 C ATOM 2127 OE1 GLU A 436 21.776 48.427 -25.764 1.00 66.48 O ANISOU 2127 OE1 GLU A 436 8497 8595 8167 1511 1422 882 O ATOM 2128 OE2 GLU A 436 21.540 46.320 -26.347 1.00 75.74 O ANISOU 2128 OE2 GLU A 436 9804 9748 9225 1588 1232 816 O ATOM 2129 N LYS A 437 16.816 43.746 -24.938 1.00 37.29 N ANISOU 2129 N LYS A 437 4963 4950 4253 1298 568 501 N ATOM 2130 CA LYS A 437 16.271 42.498 -25.473 1.00 42.16 C ANISOU 2130 CA LYS A 437 5641 5532 4847 1370 416 427 C ATOM 2131 C LYS A 437 14.784 42.310 -25.246 1.00 41.17 C ANISOU 2131 C LYS A 437 5507 5394 4743 1321 273 365 C ATOM 2132 O LYS A 437 14.069 41.844 -26.132 1.00 39.15 O ANISOU 2132 O LYS A 437 5333 5105 4437 1435 166 292 O ATOM 2133 CB LYS A 437 16.998 41.300 -24.863 1.00 43.99 C ANISOU 2133 CB LYS A 437 5812 5746 5155 1304 367 437 C ATOM 2134 CG LYS A 437 16.292 39.969 -25.073 1.00 46.81 C ANISOU 2134 CG LYS A 437 6187 6065 5534 1332 195 359 C ATOM 2135 CD LYS A 437 16.569 39.424 -26.464 1.00 56.14 C ANISOU 2135 CD LYS A 437 7503 7212 6616 1527 168 317 C ATOM 2136 CE LYS A 437 15.965 38.049 -26.642 1.00 60.65 C ANISOU 2136 CE LYS A 437 8080 7737 7227 1553 -12 233 C ATOM 2137 NZ LYS A 437 16.115 37.578 -28.040 1.00 59.66 N ANISOU 2137 NZ LYS A 437 8105 7573 6990 1762 -57 179 N ATOM 2138 N CYS A 438 14.303 42.632 -24.053 1.00 30.78 N ANISOU 2138 N CYS A 438 4093 4094 3509 1161 263 395 N ATOM 2139 CA CYS A 438 12.896 42.380 -23.791 1.00 36.24 C ANISOU 2139 CA CYS A 438 4769 4753 4247 1118 133 355 C ATOM 2140 C CYS A 438 12.130 43.541 -23.165 1.00 28.22 C ANISOU 2140 C CYS A 438 3721 3761 3238 1022 185 400 C ATOM 2141 O CYS A 438 10.903 43.534 -23.200 1.00 35.55 O ANISOU 2141 O CYS A 438 4659 4656 4192 1011 95 377 O ATOM 2142 CB CYS A 438 12.694 41.087 -22.985 1.00 41.52 C ANISOU 2142 CB CYS A 438 5354 5382 5039 1045 13 341 C ATOM 2143 SG CYS A 438 13.056 41.224 -21.233 1.00 42.41 S ANISOU 2143 SG CYS A 438 5335 5524 5254 869 72 422 S ATOM 2144 N LEU A 439 12.818 44.541 -22.615 1.00 22.32 N ANISOU 2144 N LEU A 439 2936 3064 2479 954 325 464 N ATOM 2145 CA LEU A 439 12.061 45.631 -21.975 1.00 24.40 C ANISOU 2145 CA LEU A 439 3173 3350 2748 859 372 508 C ATOM 2146 C LEU A 439 11.738 46.761 -22.949 1.00 19.75 C ANISOU 2146 C LEU A 439 2658 2791 2057 940 463 506 C ATOM 2147 O LEU A 439 10.595 47.224 -23.009 1.00 24.93 O ANISOU 2147 O LEU A 439 3335 3441 2696 919 435 506 O ATOM 2148 CB LEU A 439 12.784 46.185 -20.742 1.00 21.78 C ANISOU 2148 CB LEU A 439 2758 3051 2467 737 457 573 C ATOM 2149 CG LEU A 439 13.184 45.116 -19.716 1.00 27.43 C ANISOU 2149 CG LEU A 439 3399 3747 3275 668 385 580 C ATOM 2150 CD1 LEU A 439 13.840 45.780 -18.518 1.00 26.88 C ANISOU 2150 CD1 LEU A 439 3261 3710 3243 565 459 634 C ATOM 2151 CD2 LEU A 439 11.958 44.329 -19.292 1.00 26.85 C ANISOU 2151 CD2 LEU A 439 3308 3623 3271 640 256 570 C ATOM 2152 N MET A 440 12.734 47.192 -23.719 1.00 21.57 N ANISOU 2152 N MET A 440 2922 3048 2225 1041 581 511 N ATOM 2153 CA MET A 440 12.526 48.326 -24.632 1.00 20.54 C ANISOU 2153 CA MET A 440 2851 2953 2001 1135 698 518 C ATOM 2154 C MET A 440 11.426 47.993 -25.619 1.00 22.92 C ANISOU 2154 C MET A 440 3247 3232 2230 1246 595 452 C ATOM 2155 O MET A 440 11.394 46.876 -26.144 1.00 25.75 O ANISOU 2155 O MET A 440 3655 3547 2583 1332 470 390 O ATOM 2156 CB MET A 440 13.802 48.654 -25.409 1.00 28.52 C ANISOU 2156 CB MET A 440 3886 3975 2974 1265 841 542 C ATOM 2157 CG MET A 440 14.970 49.089 -24.555 1.00 43.97 C ANISOU 2157 CG MET A 440 5745 5942 5022 1172 948 607 C ATOM 2158 SD MET A 440 14.503 50.347 -23.352 1.00 48.27 S ANISOU 2158 SD MET A 440 6198 6526 5618 993 1010 654 S ATOM 2159 CE MET A 440 13.883 51.639 -24.383 1.00 19.23 C ANISOU 2159 CE MET A 440 2574 2889 1844 1095 1147 664 C ATOM 2160 N ARG A 441 10.561 48.972 -25.885 1.00 20.57 N ANISOU 2160 N ARG A 441 2975 2962 1878 1246 647 462 N ATOM 2161 CA ARG A 441 9.398 48.824 -26.772 1.00 25.76 C ANISOU 2161 CA ARG A 441 3719 3598 2470 1343 547 399 C ATOM 2162 C ARG A 441 8.245 48.021 -26.137 1.00 32.14 C ANISOU 2162 C ARG A 441 4497 4341 3374 1239 358 375 C ATOM 2163 O ARG A 441 7.154 47.915 -26.704 1.00 23.54 O ANISOU 2163 O ARG A 441 3461 3217 2266 1292 256 328 O ATOM 2164 CB ARG A 441 9.819 48.240 -28.133 1.00 31.45 C ANISOU 2164 CB ARG A 441 4549 4303 3097 1566 515 329 C ATOM 2165 CG ARG A 441 10.658 49.200 -28.979 1.00 36.31 C ANISOU 2165 CG ARG A 441 5212 4973 3613 1713 720 364 C ATOM 2166 CD ARG A 441 11.221 48.520 -30.239 1.00 44.15 C ANISOU 2166 CD ARG A 441 6323 5938 4513 1952 696 311 C ATOM 2167 NE ARG A 441 11.868 47.253 -29.912 1.00 53.09 N ANISOU 2167 NE ARG A 441 7440 7020 5712 1926 586 291 N ATOM 2168 CZ ARG A 441 13.113 47.145 -29.458 1.00 54.48 C ANISOU 2168 CZ ARG A 441 7558 7197 5946 1885 684 355 C ATOM 2169 NH1 ARG A 441 13.852 48.235 -29.285 1.00 48.59 N ANISOU 2169 NH1 ARG A 441 6760 6489 5214 1871 885 440 N ATOM 2170 NH2 ARG A 441 13.618 45.948 -29.174 1.00 58.20 N ANISOU 2170 NH2 ARG A 441 8016 7625 6472 1859 581 337 N ATOM 2171 N ASN A 442 8.476 47.480 -24.944 1.00 24.75 N ANISOU 2171 N ASN A 442 4289 2797 2319 617 369 409 N ATOM 2172 CA ASN A 442 7.442 46.724 -24.247 1.00 21.10 C ANISOU 2172 CA ASN A 442 3762 2331 1925 552 257 353 C ATOM 2173 C ASN A 442 7.121 47.315 -22.880 1.00 20.32 C ANISOU 2173 C ASN A 442 3465 2296 1959 489 243 368 C ATOM 2174 O ASN A 442 6.492 46.650 -22.057 1.00 21.05 O ANISOU 2174 O ASN A 442 3480 2388 2129 446 194 341 O ATOM 2175 CB ASN A 442 7.879 45.268 -24.057 1.00 24.18 C ANISOU 2175 CB ASN A 442 4190 2690 2308 563 309 334 C ATOM 2176 CG ASN A 442 8.123 44.571 -25.368 1.00 33.00 C ANISOU 2176 CG ASN A 442 5516 3734 3290 625 319 310 C ATOM 2177 OD1 ASN A 442 9.214 44.081 -25.631 1.00 38.87 O ANISOU 2177 OD1 ASN A 442 6326 4459 3984 678 449 344 O ATOM 2178 ND2 ASN A 442 7.108 44.552 -26.216 1.00 28.44 N ANISOU 2178 ND2 ASN A 442 5047 3110 2650 623 180 252 N ATOM 2179 N LEU A 443 7.548 48.551 -22.638 1.00 19.62 N ANISOU 2179 N LEU A 443 3299 2254 1901 489 293 411 N ATOM 2180 CA LEU A 443 7.459 49.105 -21.278 1.00 19.57 C ANISOU 2180 CA LEU A 443 3117 2309 2011 440 299 423 C ATOM 2181 C LEU A 443 6.009 49.294 -20.835 1.00 18.58 C ANISOU 2181 C LEU A 443 2932 2178 1951 382 174 395 C ATOM 2182 O LEU A 443 5.666 48.993 -19.692 1.00 18.12 O ANISOU 2182 O LEU A 443 2766 2142 1977 348 164 389 O ATOM 2183 CB LEU A 443 8.240 50.425 -21.161 1.00 18.43 C ANISOU 2183 CB LEU A 443 2903 2204 1894 450 376 467 C ATOM 2184 CG LEU A 443 9.758 50.348 -21.386 1.00 20.47 C ANISOU 2184 CG LEU A 443 3179 2465 2134 504 513 509 C ATOM 2185 CD1 LEU A 443 10.385 51.718 -21.214 1.00 19.22 C ANISOU 2185 CD1 LEU A 443 2931 2335 2038 506 576 545 C ATOM 2186 CD2 LEU A 443 10.426 49.355 -20.424 1.00 18.88 C ANISOU 2186 CD2 LEU A 443 2909 2291 1973 502 562 510 C ATOM 2187 N LEU A 444 5.154 49.786 -21.732 1.00 19.39 N ANISOU 2187 N LEU A 444 3105 2246 2015 377 85 383 N ATOM 2188 CA LEU A 444 3.754 50.000 -21.376 1.00 19.94 C ANISOU 2188 CA LEU A 444 3112 2301 2162 323 -33 366 C ATOM 2189 C LEU A 444 3.106 48.680 -20.996 1.00 19.29 C ANISOU 2189 C LEU A 444 3024 2175 2130 301 -93 327 C ATOM 2190 O LEU A 444 2.413 48.580 -19.990 1.00 19.26 O ANISOU 2190 O LEU A 444 2909 2172 2237 262 -118 330 O ATOM 2191 CB LEU A 444 2.963 50.674 -22.513 1.00 19.66 C ANISOU 2191 CB LEU A 444 3162 2235 2074 329 -129 362 C ATOM 2192 CG LEU A 444 1.457 50.854 -22.240 1.00 19.92 C ANISOU 2192 CG LEU A 444 3128 2239 2200 273 -261 351 C ATOM 2193 CD1 LEU A 444 1.184 51.579 -20.902 1.00 19.93 C ANISOU 2193 CD1 LEU A 444 2965 2281 2327 226 -222 385 C ATOM 2194 CD2 LEU A 444 0.762 51.608 -23.418 1.00 20.27 C ANISOU 2194 CD2 LEU A 444 3256 2262 2183 288 -357 355 C ATOM 2195 N SER A 445 3.335 47.657 -21.810 1.00 20.21 N ANISOU 2195 N SER A 445 3265 2245 2170 332 -105 292 N ATOM 2196 CA SER A 445 2.739 46.371 -21.565 1.00 19.95 C ANISOU 2196 CA SER A 445 3231 2156 2191 313 -157 250 C ATOM 2197 C SER A 445 3.263 45.750 -20.256 1.00 23.99 C ANISOU 2197 C SER A 445 3632 2702 2780 311 -54 272 C ATOM 2198 O SER A 445 2.485 45.248 -19.434 1.00 21.39 O ANISOU 2198 O SER A 445 3214 2349 2564 282 -85 266 O ATOM 2199 CB SER A 445 3.054 45.427 -22.741 1.00 25.24 C ANISOU 2199 CB SER A 445 4072 2769 2749 354 -174 205 C ATOM 2200 OG SER A 445 2.411 44.182 -22.542 1.00 37.09 O ANISOU 2200 OG SER A 445 5567 4204 4319 331 -230 157 O ATOM 2201 N LEU A 446 4.579 45.783 -20.069 1.00 21.29 N ANISOU 2201 N LEU A 446 3295 2412 2384 349 69 303 N ATOM 2202 CA LEU A 446 5.201 45.102 -18.923 1.00 20.30 C ANISOU 2202 CA LEU A 446 3081 2322 2311 360 165 324 C ATOM 2203 C LEU A 446 4.882 45.822 -17.623 1.00 19.43 C ANISOU 2203 C LEU A 446 2823 2266 2294 335 170 352 C ATOM 2204 O LEU A 446 4.856 45.212 -16.549 1.00 18.39 O ANISOU 2204 O LEU A 446 2610 2150 2227 341 210 363 O ATOM 2205 CB LEU A 446 6.717 44.999 -19.111 1.00 18.37 C ANISOU 2205 CB LEU A 446 2873 2114 1991 408 288 356 C ATOM 2206 CG LEU A 446 7.146 44.027 -20.218 1.00 21.48 C ANISOU 2206 CG LEU A 446 3419 2447 2294 445 316 336 C ATOM 2207 CD1 LEU A 446 8.612 44.236 -20.538 1.00 25.61 C ANISOU 2207 CD1 LEU A 446 3981 2997 2752 496 443 383 C ATOM 2208 CD2 LEU A 446 6.878 42.580 -19.819 1.00 24.61 C ANISOU 2208 CD2 LEU A 446 3811 2803 2735 444 328 312 C ATOM 2209 N SER A 447 4.638 47.122 -17.721 1.00 19.04 N ANISOU 2209 N SER A 447 2745 2242 2247 313 135 364 N ATOM 2210 CA SER A 447 4.324 47.909 -16.534 1.00 17.09 C ANISOU 2210 CA SER A 447 2373 2041 2080 291 140 386 C ATOM 2211 C SER A 447 2.952 47.550 -15.998 1.00 19.20 C ANISOU 2211 C SER A 447 2589 2260 2448 262 71 380 C ATOM 2212 O SER A 447 2.631 47.862 -14.857 1.00 19.22 O ANISOU 2212 O SER A 447 2496 2286 2522 256 91 402 O ATOM 2213 CB SER A 447 4.348 49.412 -16.851 1.00 18.79 C ANISOU 2213 CB SER A 447 2574 2285 2282 272 126 400 C ATOM 2214 OG SER A 447 5.661 49.847 -17.142 1.00 22.11 O ANISOU 2214 OG SER A 447 3011 2746 2643 302 207 415 O ATOM 2215 N GLN A 448 2.133 46.914 -16.835 1.00 17.51 N ANISOU 2215 N GLN A 448 2441 1969 2244 247 -12 351 N ATOM 2216 CA GLN A 448 0.800 46.493 -16.426 1.00 18.76 C ANISOU 2216 CA GLN A 448 2543 2059 2524 219 -81 348 C ATOM 2217 C GLN A 448 0.761 45.038 -15.953 1.00 18.50 C ANISOU 2217 C GLN A 448 2496 1984 2548 240 -42 337 C ATOM 2218 O GLN A 448 -0.314 44.502 -15.705 1.00 19.78 O ANISOU 2218 O GLN A 448 2615 2072 2830 222 -91 334 O ATOM 2219 CB GLN A 448 -0.185 46.680 -17.583 1.00 18.36 C ANISOU 2219 CB GLN A 448 2556 1940 2479 186 -213 319 C ATOM 2220 CG GLN A 448 -0.408 48.146 -17.920 1.00 18.02 C ANISOU 2220 CG GLN A 448 2506 1931 2411 166 -250 343 C ATOM 2221 CD GLN A 448 -1.246 48.310 -19.166 1.00 27.32 C ANISOU 2221 CD GLN A 448 3760 3051 3568 147 -383 317 C ATOM 2222 OE1 GLN A 448 -2.460 48.148 -19.126 1.00 27.75 O ANISOU 2222 OE1 GLN A 448 3771 3040 3734 114 -480 314 O ATOM 2223 NE2 GLN A 448 -0.599 48.602 -20.283 1.00 23.79 N ANISOU 2223 NE2 GLN A 448 3431 2623 2983 177 -389 300 N ATOM 2224 N GLU A 449 1.924 44.412 -15.828 1.00 19.10 N ANISOU 2224 N GLU A 449 2603 2103 2553 280 53 338 N ATOM 2225 CA GLU A 449 2.010 43.022 -15.359 1.00 18.64 C ANISOU 2225 CA GLU A 449 2530 2010 2543 308 112 336 C ATOM 2226 C GLU A 449 2.382 42.944 -13.891 1.00 21.36 C ANISOU 2226 C GLU A 449 2771 2414 2929 346 213 383 C ATOM 2227 O GLU A 449 3.226 43.694 -13.421 1.00 19.14 O ANISOU 2227 O GLU A 449 2465 2221 2588 363 262 406 O ATOM 2228 CB GLU A 449 3.055 42.231 -16.154 1.00 23.37 C ANISOU 2228 CB GLU A 449 3232 2610 3037 336 163 313 C ATOM 2229 CG GLU A 449 2.803 42.230 -17.637 1.00 27.21 C ANISOU 2229 CG GLU A 449 3848 3038 3454 317 71 263 C ATOM 2230 CD GLU A 449 2.829 40.850 -18.239 1.00 45.45 C ANISOU 2230 CD GLU A 449 6241 5271 5755 330 75 220 C ATOM 2231 OE1 GLU A 449 2.747 40.761 -19.485 1.00 50.97 O ANISOU 2231 OE1 GLU A 449 7069 5923 6374 326 3 172 O ATOM 2232 OE2 GLU A 449 2.926 39.860 -17.473 1.00 40.34 O ANISOU 2232 OE2 GLU A 449 5536 4610 5180 348 152 233 O ATOM 2233 N LYS A 450 1.764 42.013 -13.177 1.00 18.70 N ANISOU 2233 N LYS A 450 2378 2026 2699 365 244 397 N ATOM 2234 CA LYS A 450 1.985 41.890 -11.749 1.00 20.36 C ANISOU 2234 CA LYS A 450 2502 2287 2948 416 339 446 C ATOM 2235 C LYS A 450 3.470 41.674 -11.436 1.00 20.87 C ANISOU 2235 C LYS A 450 2578 2446 2905 464 433 462 C ATOM 2236 O LYS A 450 4.016 42.331 -10.570 1.00 21.07 O ANISOU 2236 O LYS A 450 2555 2554 2895 492 470 488 O ATOM 2237 CB LYS A 450 1.171 40.729 -11.187 1.00 20.67 C ANISOU 2237 CB LYS A 450 2492 2242 3121 443 379 464 C ATOM 2238 CG LYS A 450 1.335 40.553 -9.682 1.00 24.78 C ANISOU 2238 CG LYS A 450 2933 2810 3674 516 487 523 C ATOM 2239 CD LYS A 450 0.548 39.345 -9.184 1.00 29.24 C ANISOU 2239 CD LYS A 450 3449 3279 4383 554 547 549 C ATOM 2240 CE LYS A 450 0.726 39.160 -7.688 1.00 31.08 C ANISOU 2240 CE LYS A 450 3617 3560 4633 645 666 616 C ATOM 2241 NZ LYS A 450 0.129 40.303 -6.929 1.00 33.76 N ANISOU 2241 NZ LYS A 450 3916 3917 4994 650 643 646 N ATOM 2242 N PHE A 451 4.113 40.744 -12.135 1.00 17.48 N ANISOU 2242 N PHE A 451 2214 1997 2430 475 469 445 N ATOM 2243 CA PHE A 451 5.510 40.421 -11.836 1.00 19.09 C ANISOU 2243 CA PHE A 451 2421 2280 2552 524 566 471 C ATOM 2244 C PHE A 451 6.488 41.311 -12.596 1.00 24.07 C ANISOU 2244 C PHE A 451 3103 2962 3079 505 551 462 C ATOM 2245 O PHE A 451 7.415 41.874 -12.003 1.00 20.57 O ANISOU 2245 O PHE A 451 2614 2605 2596 530 592 488 O ATOM 2246 CB PHE A 451 5.779 38.922 -12.072 1.00 18.97 C ANISOU 2246 CB PHE A 451 2440 2216 2552 555 642 473 C ATOM 2247 CG PHE A 451 4.805 38.045 -11.345 1.00 22.76 C ANISOU 2247 CG PHE A 451 2859 2631 3155 577 670 487 C ATOM 2248 CD1 PHE A 451 4.765 38.049 -9.956 1.00 24.33 C ANISOU 2248 CD1 PHE A 451 2967 2881 3395 635 736 539 C ATOM 2249 CD2 PHE A 451 3.882 37.271 -12.038 1.00 22.03 C ANISOU 2249 CD2 PHE A 451 2802 2422 3147 545 626 447 C ATOM 2250 CE1 PHE A 451 3.835 37.270 -9.266 1.00 26.06 C ANISOU 2250 CE1 PHE A 451 3129 3030 3741 668 779 564 C ATOM 2251 CE2 PHE A 451 2.951 36.484 -11.350 1.00 26.30 C ANISOU 2251 CE2 PHE A 451 3271 2888 3832 568 660 465 C ATOM 2252 CZ PHE A 451 2.930 36.491 -9.970 1.00 26.82 C ANISOU 2252 CZ PHE A 451 3246 3002 3942 632 746 529 C ATOM 2253 N ALA A 452 6.271 41.481 -13.896 1.00 17.13 N ANISOU 2253 N ALA A 452 2319 2028 2162 467 490 425 N ATOM 2254 CA ALA A 452 7.235 42.255 -14.683 1.00 17.10 C ANISOU 2254 CA ALA A 452 2372 2060 2065 465 498 426 C ATOM 2255 C ALA A 452 7.287 43.736 -14.307 1.00 18.58 C ANISOU 2255 C ALA A 452 2498 2308 2253 444 462 435 C ATOM 2256 O ALA A 452 8.267 44.413 -14.603 1.00 17.29 O ANISOU 2256 O ALA A 452 2343 2186 2039 452 496 449 O ATOM 2257 CB ALA A 452 6.988 42.083 -16.180 1.00 19.27 C ANISOU 2257 CB ALA A 452 2780 2260 2283 446 448 388 C ATOM 2258 N SER A 453 6.239 44.262 -13.669 1.00 19.25 N ANISOU 2258 N SER A 453 2520 2388 2405 418 402 430 N ATOM 2259 CA SER A 453 6.251 45.683 -13.324 1.00 16.53 C ANISOU 2259 CA SER A 453 2122 2094 2063 396 373 436 C ATOM 2260 C SER A 453 7.416 45.987 -12.386 1.00 16.43 C ANISOU 2260 C SER A 453 2040 2170 2033 431 440 458 C ATOM 2261 O SER A 453 7.995 47.068 -12.449 1.00 16.80 O ANISOU 2261 O SER A 453 2063 2257 2063 419 437 457 O ATOM 2262 CB SER A 453 4.917 46.158 -12.713 1.00 16.31 C ANISOU 2262 CB SER A 453 2040 2040 2117 368 311 435 C ATOM 2263 OG SER A 453 4.531 45.332 -11.627 1.00 17.75 O ANISOU 2263 OG SER A 453 2166 2217 2360 402 349 454 O ATOM 2264 N HIS A 454 7.751 45.041 -11.512 1.00 16.11 N ANISOU 2264 N HIS A 454 1962 2156 2004 477 497 478 N ATOM 2265 CA HIS A 454 8.914 45.206 -10.642 1.00 16.71 C ANISOU 2265 CA HIS A 454 1973 2318 2058 518 549 498 C ATOM 2266 C HIS A 454 10.227 45.241 -11.432 1.00 20.44 C ANISOU 2266 C HIS A 454 2476 2805 2484 525 595 509 C ATOM 2267 O HIS A 454 11.165 45.937 -11.052 1.00 17.32 O ANISOU 2267 O HIS A 454 2024 2468 2088 534 608 515 O ATOM 2268 CB HIS A 454 8.986 44.059 -9.628 1.00 15.67 C ANISOU 2268 CB HIS A 454 1805 2208 1940 578 607 525 C ATOM 2269 CG HIS A 454 7.796 43.986 -8.731 1.00 18.24 C ANISOU 2269 CG HIS A 454 2095 2514 2321 590 587 529 C ATOM 2270 ND1 HIS A 454 7.664 44.780 -7.614 1.00 17.79 N ANISOU 2270 ND1 HIS A 454 1979 2510 2269 609 570 530 N ATOM 2271 CD2 HIS A 454 6.679 43.221 -8.789 1.00 20.44 C ANISOU 2271 CD2 HIS A 454 2390 2715 2661 589 587 533 C ATOM 2272 CE1 HIS A 454 6.507 44.518 -7.028 1.00 20.87 C ANISOU 2272 CE1 HIS A 454 2357 2856 2718 625 570 545 C ATOM 2273 NE2 HIS A 454 5.893 43.576 -7.721 1.00 19.29 N ANISOU 2273 NE2 HIS A 454 2193 2574 2563 611 581 548 N ATOM 2274 N VAL A 455 10.296 44.464 -12.510 1.00 16.15 N ANISOU 2274 N VAL A 455 2024 2202 1912 525 623 511 N ATOM 2275 CA VAL A 455 11.470 44.475 -13.380 1.00 16.48 C ANISOU 2275 CA VAL A 455 2112 2237 1912 539 683 531 C ATOM 2276 C VAL A 455 11.594 45.814 -14.076 1.00 16.92 C ANISOU 2276 C VAL A 455 2182 2287 1961 509 649 521 C ATOM 2277 O VAL A 455 12.698 46.355 -14.216 1.00 16.78 O ANISOU 2277 O VAL A 455 2135 2293 1948 523 697 545 O ATOM 2278 CB VAL A 455 11.386 43.347 -14.436 1.00 17.88 C ANISOU 2278 CB VAL A 455 2408 2339 2048 551 720 531 C ATOM 2279 CG1 VAL A 455 12.514 43.474 -15.450 1.00 17.81 C ANISOU 2279 CG1 VAL A 455 2468 2309 1992 573 790 558 C ATOM 2280 CG2 VAL A 455 11.394 41.985 -13.746 1.00 18.05 C ANISOU 2280 CG2 VAL A 455 2407 2363 2089 586 775 548 C ATOM 2281 N VAL A 456 10.464 46.349 -14.538 1.00 17.29 N ANISOU 2281 N VAL A 456 2267 2295 2007 470 573 491 N ATOM 2282 CA VAL A 456 10.471 47.675 -15.150 1.00 18.31 C ANISOU 2282 CA VAL A 456 2404 2419 2134 444 546 486 C ATOM 2283 C VAL A 456 10.991 48.747 -14.172 1.00 17.85 C ANISOU 2283 C VAL A 456 2225 2428 2129 435 547 488 C ATOM 2284 O VAL A 456 11.789 49.608 -14.550 1.00 16.68 O ANISOU 2284 O VAL A 456 2058 2286 1995 436 580 500 O ATOM 2285 CB VAL A 456 9.074 48.054 -15.711 1.00 20.14 C ANISOU 2285 CB VAL A 456 2686 2602 2362 405 456 458 C ATOM 2286 CG1 VAL A 456 9.063 49.515 -16.194 1.00 16.93 C ANISOU 2286 CG1 VAL A 456 2272 2200 1962 384 438 460 C ATOM 2287 CG2 VAL A 456 8.715 47.116 -16.853 1.00 17.10 C ANISOU 2287 CG2 VAL A 456 2432 2145 1918 417 442 445 C ATOM 2288 N GLU A 457 10.545 48.703 -12.917 1.00 15.75 N ANISOU 2288 N GLU A 457 1881 2205 1898 431 514 475 N ATOM 2289 CA GLU A 457 11.061 49.656 -11.938 1.00 16.16 C ANISOU 2289 CA GLU A 457 1830 2320 1990 427 506 466 C ATOM 2290 C GLU A 457 12.579 49.538 -11.794 1.00 17.00 C ANISOU 2290 C GLU A 457 1890 2464 2106 461 565 487 C ATOM 2291 O GLU A 457 13.286 50.556 -11.831 1.00 20.37 O ANISOU 2291 O GLU A 457 2260 2904 2574 449 570 482 O ATOM 2292 CB GLU A 457 10.407 49.456 -10.576 1.00 15.89 C ANISOU 2292 CB GLU A 457 1740 2324 1972 438 472 453 C ATOM 2293 CG GLU A 457 8.916 49.770 -10.559 1.00 19.46 C ANISOU 2293 CG GLU A 457 2213 2734 2445 404 418 441 C ATOM 2294 CD GLU A 457 8.362 49.634 -9.143 1.00 30.65 C ANISOU 2294 CD GLU A 457 3578 4183 3883 430 406 439 C ATOM 2295 OE1 GLU A 457 8.898 50.311 -8.232 1.00 28.33 O ANISOU 2295 OE1 GLU A 457 3224 3948 3591 444 400 424 O ATOM 2296 OE2 GLU A 457 7.413 48.852 -8.948 1.00 21.69 O ANISOU 2296 OE2 GLU A 457 2466 3009 2766 442 405 453 O ATOM 2297 N LYS A 458 13.082 48.312 -11.633 1.00 17.08 N ANISOU 2297 N LYS A 458 1913 2483 2091 502 613 513 N ATOM 2298 CA LYS A 458 14.538 48.115 -11.523 1.00 20.13 C ANISOU 2298 CA LYS A 458 2251 2900 2498 537 673 544 C ATOM 2299 C LYS A 458 15.268 48.687 -12.738 1.00 22.63 C ANISOU 2299 C LYS A 458 2602 3165 2832 530 724 568 C ATOM 2300 O LYS A 458 16.323 49.296 -12.592 1.00 19.75 O ANISOU 2300 O LYS A 458 2160 2818 2528 537 749 582 O ATOM 2301 CB LYS A 458 14.918 46.643 -11.327 1.00 18.73 C ANISOU 2301 CB LYS A 458 2096 2730 2291 585 733 580 C ATOM 2302 CG LYS A 458 14.540 46.046 -9.966 1.00 20.40 C ANISOU 2302 CG LYS A 458 2254 3003 2496 616 708 574 C ATOM 2303 CD LYS A 458 14.904 46.985 -8.808 1.00 28.09 C ANISOU 2303 CD LYS A 458 3123 4051 3499 621 649 548 C ATOM 2304 CE LYS A 458 14.870 46.255 -7.462 1.00 39.01 C ANISOU 2304 CE LYS A 458 4461 5502 4858 681 645 557 C ATOM 2305 NZ LYS A 458 13.478 45.968 -7.030 1.00 44.85 N ANISOU 2305 NZ LYS A 458 5240 6221 5579 684 625 544 N ATOM 2306 N ALA A 459 14.705 48.508 -13.931 1.00 18.09 N ANISOU 2306 N ALA A 459 2143 2522 2209 522 740 573 N ATOM 2307 CA ALA A 459 15.338 49.040 -15.144 1.00 19.55 C ANISOU 2307 CA ALA A 459 2381 2649 2396 533 803 603 C ATOM 2308 C ALA A 459 15.435 50.586 -15.111 1.00 17.28 C ANISOU 2308 C ALA A 459 2021 2368 2176 504 778 588 C ATOM 2309 O ALA A 459 16.486 51.175 -15.416 1.00 20.25 O ANISOU 2309 O ALA A 459 2351 2727 2615 520 841 619 O ATOM 2310 CB ALA A 459 14.576 48.566 -16.390 1.00 20.46 C ANISOU 2310 CB ALA A 459 2652 2694 2429 539 806 601 C ATOM 2311 N PHE A 460 14.349 51.244 -14.722 1.00 17.52 N ANISOU 2311 N PHE A 460 2034 2417 2207 461 696 545 N ATOM 2312 CA PHE A 460 14.375 52.695 -14.579 1.00 20.52 C ANISOU 2312 CA PHE A 460 2340 2804 2655 430 676 527 C ATOM 2313 C PHE A 460 15.433 53.115 -13.566 1.00 23.02 C ANISOU 2313 C PHE A 460 2520 3169 3057 432 679 517 C ATOM 2314 O PHE A 460 16.201 54.030 -13.820 1.00 20.08 O ANISOU 2314 O PHE A 460 2086 2776 2766 429 716 527 O ATOM 2315 CB PHE A 460 13.007 53.259 -14.174 1.00 18.12 C ANISOU 2315 CB PHE A 460 2033 2511 2340 386 591 487 C ATOM 2316 CG PHE A 460 12.111 53.546 -15.341 1.00 18.80 C ANISOU 2316 CG PHE A 460 2221 2542 2382 375 580 495 C ATOM 2317 CD1 PHE A 460 11.033 52.717 -15.636 1.00 18.17 C ANISOU 2317 CD1 PHE A 460 2228 2439 2237 370 530 487 C ATOM 2318 CD2 PHE A 460 12.374 54.624 -16.172 1.00 17.24 C ANISOU 2318 CD2 PHE A 460 2029 2309 2211 376 621 514 C ATOM 2319 CE1 PHE A 460 10.209 52.988 -16.726 1.00 23.61 C ANISOU 2319 CE1 PHE A 460 3010 3077 2882 364 502 491 C ATOM 2320 CE2 PHE A 460 11.553 54.900 -17.266 1.00 23.58 C ANISOU 2320 CE2 PHE A 460 2932 3067 2961 377 607 526 C ATOM 2321 CZ PHE A 460 10.478 54.079 -17.542 1.00 19.40 C ANISOU 2321 CZ PHE A 460 2492 2521 2360 371 539 512 C ATOM 2322 N LEU A 461 15.473 52.426 -12.429 1.00 20.32 N ANISOU 2322 N LEU A 461 2132 2888 2703 442 639 499 N ATOM 2323 CA LEU A 461 16.369 52.791 -11.342 1.00 22.69 C ANISOU 2323 CA LEU A 461 2306 3243 3071 447 613 479 C ATOM 2324 C LEU A 461 17.836 52.627 -11.706 1.00 24.67 C ANISOU 2324 C LEU A 461 2507 3476 3389 478 685 524 C ATOM 2325 O LEU A 461 18.680 53.363 -11.205 1.00 24.68 O ANISOU 2325 O LEU A 461 2395 3495 3487 471 667 507 O ATOM 2326 CB LEU A 461 16.058 51.954 -10.103 1.00 23.82 C ANISOU 2326 CB LEU A 461 2431 3455 3165 471 563 460 C ATOM 2327 CG LEU A 461 14.730 52.312 -9.415 1.00 24.03 C ANISOU 2327 CG LEU A 461 2474 3500 3156 447 493 416 C ATOM 2328 CD1 LEU A 461 14.310 51.217 -8.443 1.00 25.22 C ANISOU 2328 CD1 LEU A 461 2639 3697 3248 489 477 420 C ATOM 2329 CD2 LEU A 461 14.873 53.676 -8.699 1.00 25.01 C ANISOU 2329 CD2 LEU A 461 2512 3650 3342 417 437 363 C ATOM 2330 N HIS A 462 18.144 51.654 -12.559 1.00 20.79 N ANISOU 2330 N HIS A 462 2098 2945 2856 513 765 581 N ATOM 2331 CA HIS A 462 19.541 51.280 -12.776 1.00 23.00 C ANISOU 2331 CA HIS A 462 2331 3207 3202 551 844 637 C ATOM 2332 C HIS A 462 20.055 51.425 -14.202 1.00 27.87 C ANISOU 2332 C HIS A 462 3018 3731 3841 574 957 699 C ATOM 2333 O HIS A 462 21.240 51.206 -14.453 1.00 25.07 O ANISOU 2333 O HIS A 462 2621 3345 3560 609 1039 757 O ATOM 2334 CB HIS A 462 19.788 49.843 -12.297 1.00 20.02 C ANISOU 2334 CB HIS A 462 1971 2867 2767 591 863 667 C ATOM 2335 CG HIS A 462 19.540 49.655 -10.831 1.00 23.39 C ANISOU 2335 CG HIS A 462 2321 3386 3179 592 771 622 C ATOM 2336 ND1 HIS A 462 20.470 49.988 -9.868 1.00 25.74 N ANISOU 2336 ND1 HIS A 462 2489 3739 3551 604 727 611 N ATOM 2337 CD2 HIS A 462 18.464 49.170 -10.166 1.00 21.43 C ANISOU 2337 CD2 HIS A 462 2114 3179 2849 592 717 589 C ATOM 2338 CE1 HIS A 462 19.972 49.726 -8.672 1.00 27.57 C ANISOU 2338 CE1 HIS A 462 2697 4048 3729 617 648 570 C ATOM 2339 NE2 HIS A 462 18.755 49.235 -8.825 1.00 24.74 N ANISOU 2339 NE2 HIS A 462 2439 3679 3281 612 650 561 N ATOM 2340 N ALA A 463 19.183 51.767 -15.142 1.00 19.82 N ANISOU 2340 N ALA A 463 2109 2663 2759 563 966 692 N ATOM 2341 CA ALA A 463 19.631 51.915 -16.523 1.00 23.46 C ANISOU 2341 CA ALA A 463 2657 3034 3222 602 1079 753 C ATOM 2342 C ALA A 463 20.684 53.010 -16.642 1.00 26.32 C ANISOU 2342 C ALA A 463 2905 3358 3736 609 1138 783 C ATOM 2343 O ALA A 463 20.557 54.078 -16.028 1.00 23.85 O ANISOU 2343 O ALA A 463 2485 3073 3504 566 1075 736 O ATOM 2344 CB ALA A 463 18.459 52.248 -17.442 1.00 23.64 C ANISOU 2344 CB ALA A 463 2811 3021 3150 593 1058 734 C ATOM 2345 N PRO A 464 21.711 52.767 -17.467 1.00 25.85 N ANISOU 2345 N PRO A 464 2873 3223 3725 665 1269 865 N ATOM 2346 CA PRO A 464 22.648 53.852 -17.780 1.00 29.19 C ANISOU 2346 CA PRO A 464 3196 3584 4310 679 1347 905 C ATOM 2347 C PRO A 464 21.893 54.992 -18.453 1.00 32.34 C ANISOU 2347 C PRO A 464 3640 3948 4699 668 1349 886 C ATOM 2348 O PRO A 464 20.858 54.764 -19.094 1.00 29.42 O ANISOU 2348 O PRO A 464 3419 3576 4184 674 1329 872 O ATOM 2349 CB PRO A 464 23.619 53.206 -18.780 1.00 30.70 C ANISOU 2349 CB PRO A 464 3462 3684 4517 758 1508 1010 C ATOM 2350 CG PRO A 464 22.823 52.104 -19.409 1.00 31.45 C ANISOU 2350 CG PRO A 464 3753 3778 4418 783 1514 1011 C ATOM 2351 CD PRO A 464 22.005 51.549 -18.234 1.00 24.41 C ANISOU 2351 CD PRO A 464 2823 2995 3456 723 1364 927 C ATOM 2352 N LEU A 465 22.411 56.203 -18.311 1.00 28.67 N ANISOU 2352 N LEU A 465 3045 3454 4395 653 1372 885 N ATOM 2353 CA LEU A 465 21.741 57.410 -18.817 1.00 36.68 C ANISOU 2353 CA LEU A 465 4075 4439 5422 640 1378 868 C ATOM 2354 C LEU A 465 21.170 57.348 -20.239 1.00 31.74 C ANISOU 2354 C LEU A 465 3637 3751 4671 700 1463 920 C ATOM 2355 O LEU A 465 20.046 57.791 -20.468 1.00 29.96 O ANISOU 2355 O LEU A 465 3479 3548 4357 677 1403 883 O ATOM 2356 CB LEU A 465 22.656 58.631 -18.686 1.00 46.61 C ANISOU 2356 CB LEU A 465 5167 5642 6902 634 1438 883 C ATOM 2357 CG LEU A 465 22.449 59.536 -17.470 1.00 58.39 C ANISOU 2357 CG LEU A 465 6499 7194 8493 553 1315 788 C ATOM 2358 CD1 LEU A 465 21.121 60.273 -17.571 1.00 64.39 C ANISOU 2358 CD1 LEU A 465 7318 7980 9166 515 1258 738 C ATOM 2359 CD2 LEU A 465 22.538 58.750 -16.168 1.00 63.11 C ANISOU 2359 CD2 LEU A 465 7034 7887 9058 514 1185 727 C ATOM 2360 N GLU A 466 21.932 56.838 -21.203 1.00 33.15 N ANISOU 2360 N GLU A 466 3905 3849 4841 782 1602 1009 N ATOM 2361 CA GLU A 466 21.448 56.836 -22.584 1.00 34.72 C ANISOU 2361 CA GLU A 466 4297 3984 4911 855 1683 1058 C ATOM 2362 C GLU A 466 20.233 55.921 -22.756 1.00 33.11 C ANISOU 2362 C GLU A 466 4254 3832 4492 839 1575 1005 C ATOM 2363 O GLU A 466 19.296 56.242 -23.488 1.00 31.11 O ANISOU 2363 O GLU A 466 4121 3571 4129 856 1549 994 O ATOM 2364 CB GLU A 466 22.558 56.468 -23.577 1.00 37.55 C ANISOU 2364 CB GLU A 466 4731 4234 5301 960 1869 1169 C ATOM 2365 CG GLU A 466 23.695 57.487 -23.641 1.00 49.74 C ANISOU 2365 CG GLU A 466 6123 5698 7078 989 1999 1236 C ATOM 2366 CD GLU A 466 23.238 58.877 -24.100 1.00 65.55 C ANISOU 2366 CD GLU A 466 8105 7668 9132 998 2031 1237 C ATOM 2367 OE1 GLU A 466 22.242 58.975 -24.853 1.00 64.83 O ANISOU 2367 OE1 GLU A 466 8173 7584 8874 1026 2011 1228 O ATOM 2368 OE2 GLU A 466 23.886 59.874 -23.711 1.00 68.59 O ANISOU 2368 OE2 GLU A 466 8311 8019 9732 978 2074 1246 O ATOM 2369 N LEU A 467 20.233 54.795 -22.057 1.00 26.49 N ANISOU 2369 N LEU A 467 3411 3048 3607 808 1508 973 N ATOM 2370 CA LEU A 467 19.079 53.902 -22.094 1.00 26.25 C ANISOU 2370 CA LEU A 467 3508 3060 3406 786 1401 918 C ATOM 2371 C LEU A 467 17.917 54.447 -21.268 1.00 26.74 C ANISOU 2371 C LEU A 467 3498 3199 3463 702 1250 835 C ATOM 2372 O LEU A 467 16.749 54.277 -21.631 1.00 27.92 O ANISOU 2372 O LEU A 467 3753 3359 3497 688 1170 798 O ATOM 2373 CB LEU A 467 19.456 52.499 -21.602 1.00 22.11 C ANISOU 2373 CB LEU A 467 2996 2560 2846 786 1396 917 C ATOM 2374 CG LEU A 467 20.285 51.636 -22.546 1.00 41.19 C ANISOU 2374 CG LEU A 467 5541 4896 5214 871 1536 994 C ATOM 2375 CD1 LEU A 467 20.581 50.290 -21.877 1.00 42.76 C ANISOU 2375 CD1 LEU A 467 5725 5129 5391 859 1524 989 C ATOM 2376 CD2 LEU A 467 19.566 51.434 -23.871 1.00 35.32 C ANISOU 2376 CD2 LEU A 467 5018 4094 4308 926 1553 998 C ATOM 2377 N LEU A 468 18.223 55.076 -20.140 1.00 24.16 N ANISOU 2377 N LEU A 468 2994 2922 3264 647 1208 804 N ATOM 2378 CA LEU A 468 17.168 55.690 -19.339 1.00 23.77 C ANISOU 2378 CA LEU A 468 2880 2936 3217 575 1083 732 C ATOM 2379 C LEU A 468 16.434 56.732 -20.178 1.00 24.67 C ANISOU 2379 C LEU A 468 3050 3014 3310 580 1092 740 C ATOM 2380 O LEU A 468 15.220 56.827 -20.121 1.00 22.07 O ANISOU 2380 O LEU A 468 2764 2712 2909 544 999 700 O ATOM 2381 CB LEU A 468 17.726 56.315 -18.058 1.00 25.51 C ANISOU 2381 CB LEU A 468 2911 3203 3576 527 1046 696 C ATOM 2382 CG LEU A 468 16.730 57.112 -17.208 1.00 27.73 C ANISOU 2382 CG LEU A 468 3126 3539 3873 459 936 627 C ATOM 2383 CD1 LEU A 468 15.653 56.200 -16.630 1.00 20.03 C ANISOU 2383 CD1 LEU A 468 2208 2617 2785 433 834 585 C ATOM 2384 CD2 LEU A 468 17.450 57.851 -16.077 1.00 29.61 C ANISOU 2384 CD2 LEU A 468 3190 3810 4252 424 910 589 C ATOM 2385 N ALA A 469 17.172 57.501 -20.976 1.00 23.84 N ANISOU 2385 N ALA A 469 2941 2843 3275 631 1212 799 N ATOM 2386 CA ALA A 469 16.543 58.507 -21.823 1.00 22.48 C ANISOU 2386 CA ALA A 469 2824 2636 3082 651 1238 818 C ATOM 2387 C ALA A 469 15.604 57.871 -22.842 1.00 21.76 C ANISOU 2387 C ALA A 469 2930 2529 2809 691 1203 824 C ATOM 2388 O ALA A 469 14.529 58.412 -23.120 1.00 24.09 O ANISOU 2388 O ALA A 469 3265 2836 3051 673 1137 805 O ATOM 2389 CB ALA A 469 17.598 59.373 -22.523 1.00 29.39 C ANISOU 2389 CB ALA A 469 3661 3430 4075 716 1397 892 C ATOM 2390 N GLU A 470 16.016 56.734 -23.402 1.00 25.00 N ANISOU 2390 N GLU A 470 3462 2908 3128 746 1244 851 N ATOM 2391 CA GLU A 470 15.183 55.989 -24.345 1.00 28.48 C ANISOU 2391 CA GLU A 470 4100 3330 3393 785 1197 843 C ATOM 2392 C GLU A 470 13.926 55.479 -23.654 1.00 24.99 C ANISOU 2392 C GLU A 470 3650 2950 2895 705 1029 765 C ATOM 2393 O GLU A 470 12.833 55.547 -24.219 1.00 26.18 O ANISOU 2393 O GLU A 470 3896 3097 2952 704 946 743 O ATOM 2394 CB GLU A 470 15.957 54.813 -24.965 1.00 29.10 C ANISOU 2394 CB GLU A 470 4306 3357 3395 856 1282 881 C ATOM 2395 CG GLU A 470 17.052 55.254 -25.931 1.00 35.71 C ANISOU 2395 CG GLU A 470 5198 4109 4263 959 1462 974 C ATOM 2396 CD GLU A 470 17.767 54.084 -26.591 1.00 47.95 C ANISOU 2396 CD GLU A 470 6892 5599 5729 1036 1557 1017 C ATOM 2397 OE1 GLU A 470 18.947 54.254 -26.969 1.00 49.68 O ANISOU 2397 OE1 GLU A 470 7101 5750 6026 1106 1720 1102 O ATOM 2398 OE2 GLU A 470 17.154 53.000 -26.727 1.00 42.11 O ANISOU 2398 OE2 GLU A 470 6271 4871 4856 1026 1473 970 O ATOM 2399 N MET A 471 14.085 54.959 -22.439 1.00 21.57 N ANISOU 2399 N MET A 471 3101 2569 2525 646 982 728 N ATOM 2400 CA MET A 471 12.941 54.503 -21.647 1.00 20.63 C ANISOU 2400 CA MET A 471 2956 2502 2380 576 843 663 C ATOM 2401 C MET A 471 11.963 55.635 -21.344 1.00 23.55 C ANISOU 2401 C MET A 471 3258 2897 2792 524 770 640 C ATOM 2402 O MET A 471 10.754 55.475 -21.487 1.00 19.90 O ANISOU 2402 O MET A 471 2850 2439 2273 498 669 611 O ATOM 2403 CB MET A 471 13.411 53.889 -20.326 1.00 18.46 C ANISOU 2403 CB MET A 471 2561 2280 2173 538 828 639 C ATOM 2404 CG MET A 471 14.222 52.613 -20.506 1.00 26.20 C ANISOU 2404 CG MET A 471 3603 3240 3113 582 891 663 C ATOM 2405 SD MET A 471 14.799 51.963 -18.921 1.00 25.21 S ANISOU 2405 SD MET A 471 3329 3185 3066 549 874 644 S ATOM 2406 CE MET A 471 13.264 51.451 -18.159 1.00 22.88 C ANISOU 2406 CE MET A 471 3034 2931 2729 494 738 580 C ATOM 2407 N MET A 472 12.483 56.780 -20.908 1.00 20.96 N ANISOU 2407 N MET A 472 2807 2581 2576 508 821 652 N ATOM 2408 CA MET A 472 11.608 57.911 -20.597 1.00 21.27 C ANISOU 2408 CA MET A 472 2778 2639 2663 459 768 634 C ATOM 2409 C MET A 472 10.865 58.347 -21.863 1.00 21.59 C ANISOU 2409 C MET A 472 2940 2641 2622 497 764 664 C ATOM 2410 O MET A 472 9.661 58.573 -21.829 1.00 22.19 O ANISOU 2410 O MET A 472 3029 2729 2672 460 671 644 O ATOM 2411 CB MET A 472 12.406 59.082 -20.017 1.00 22.29 C ANISOU 2411 CB MET A 472 2761 2775 2934 441 836 640 C ATOM 2412 CG MET A 472 12.975 58.791 -18.624 1.00 22.44 C ANISOU 2412 CG MET A 472 2652 2844 3030 399 806 598 C ATOM 2413 SD MET A 472 11.732 59.083 -17.347 1.00 25.99 S ANISOU 2413 SD MET A 472 3030 3351 3494 320 683 535 S ATOM 2414 CE MET A 472 12.660 58.678 -15.859 1.00 21.85 C ANISOU 2414 CE MET A 472 2383 2882 3036 303 664 493 C ATOM 2415 N ASP A 473 11.597 58.438 -22.968 1.00 24.28 N ANISOU 2415 N ASP A 473 3372 2930 2925 578 868 717 N ATOM 2416 CA ASP A 473 11.030 58.855 -24.251 1.00 26.29 C ANISOU 2416 CA ASP A 473 3758 3147 3086 637 877 752 C ATOM 2417 C ASP A 473 9.932 57.903 -24.698 1.00 24.53 C ANISOU 2417 C ASP A 473 3669 2925 2726 634 747 717 C ATOM 2418 O ASP A 473 8.958 58.322 -25.323 1.00 22.47 O ANISOU 2418 O ASP A 473 3473 2658 2407 643 680 720 O ATOM 2419 CB ASP A 473 12.118 58.893 -25.329 1.00 23.98 C ANISOU 2419 CB ASP A 473 3560 2790 2762 743 1026 820 C ATOM 2420 CG ASP A 473 13.069 60.083 -25.172 1.00 43.71 C ANISOU 2420 CG ASP A 473 5930 5265 5414 759 1163 868 C ATOM 2421 OD1 ASP A 473 14.085 60.120 -25.899 1.00 45.40 O ANISOU 2421 OD1 ASP A 473 6193 5417 5640 846 1305 933 O ATOM 2422 OD2 ASP A 473 12.809 60.973 -24.327 1.00 43.37 O ANISOU 2422 OD2 ASP A 473 5737 5255 5486 688 1135 842 O ATOM 2423 N GLU A 474 10.096 56.616 -24.390 1.00 23.96 N ANISOU 2423 N GLU A 474 3634 2857 2614 624 710 683 N ATOM 2424 CA GLU A 474 9.089 55.626 -24.754 1.00 24.76 C ANISOU 2424 CA GLU A 474 3850 2948 2609 616 584 640 C ATOM 2425 C GLU A 474 7.785 55.868 -23.997 1.00 22.39 C ANISOU 2425 C GLU A 474 3461 2683 2362 531 451 600 C ATOM 2426 O GLU A 474 6.697 55.780 -24.563 1.00 21.17 O ANISOU 2426 O GLU A 474 3383 2512 2148 527 344 583 O ATOM 2427 CB GLU A 474 9.592 54.186 -24.492 1.00 23.19 C ANISOU 2427 CB GLU A 474 3694 2742 2377 620 591 614 C ATOM 2428 CG GLU A 474 8.524 53.118 -24.753 1.00 23.66 C ANISOU 2428 CG GLU A 474 3851 2783 2355 601 457 559 C ATOM 2429 CD GLU A 474 9.068 51.690 -24.730 1.00 26.63 C ANISOU 2429 CD GLU A 474 4295 3136 2687 621 484 539 C ATOM 2430 OE1 GLU A 474 10.281 51.495 -24.960 1.00 23.75 O ANISOU 2430 OE1 GLU A 474 3960 2754 2310 675 614 580 O ATOM 2431 OE2 GLU A 474 8.271 50.757 -24.496 1.00 21.54 O ANISOU 2431 OE2 GLU A 474 3670 2482 2031 584 382 488 O ATOM 2432 N ILE A 475 7.878 56.156 -22.704 1.00 19.23 N ANISOU 2432 N ILE A 475 2903 2326 2077 467 456 586 N ATOM 2433 CA ILE A 475 6.658 56.408 -21.929 1.00 21.51 C ANISOU 2433 CA ILE A 475 3111 2638 2426 394 350 559 C ATOM 2434 C ILE A 475 6.003 57.722 -22.383 1.00 21.04 C ANISOU 2434 C ILE A 475 3035 2574 2385 389 339 589 C ATOM 2435 O ILE A 475 4.801 57.769 -22.645 1.00 20.81 O ANISOU 2435 O ILE A 475 3034 2533 2340 367 236 583 O ATOM 2436 CB ILE A 475 6.941 56.422 -20.418 1.00 18.86 C ANISOU 2436 CB ILE A 475 2626 2347 2193 341 365 539 C ATOM 2437 CG1 ILE A 475 7.515 55.062 -19.985 1.00 21.04 C ANISOU 2437 CG1 ILE A 475 2919 2630 2445 353 375 517 C ATOM 2438 CG2 ILE A 475 5.661 56.775 -19.624 1.00 21.00 C ANISOU 2438 CG2 ILE A 475 2821 2631 2528 277 276 523 C ATOM 2439 CD1 ILE A 475 6.662 53.851 -20.453 1.00 19.51 C ANISOU 2439 CD1 ILE A 475 2829 2400 2184 355 286 491 C ATOM 2440 N PHE A 476 6.798 58.779 -22.529 1.00 18.73 N ANISOU 2440 N PHE A 476 2696 2284 2135 414 449 626 N ATOM 2441 CA PHE A 476 6.229 60.087 -22.866 1.00 19.48 C ANISOU 2441 CA PHE A 476 2761 2376 2265 410 459 659 C ATOM 2442 C PHE A 476 5.740 60.201 -24.327 1.00 23.25 C ANISOU 2442 C PHE A 476 3385 2820 2627 479 434 693 C ATOM 2443 O PHE A 476 4.786 60.928 -24.613 1.00 21.25 O ANISOU 2443 O PHE A 476 3127 2568 2380 467 383 713 O ATOM 2444 CB PHE A 476 7.242 61.216 -22.561 1.00 21.91 C ANISOU 2444 CB PHE A 476 2964 2688 2675 417 592 686 C ATOM 2445 CG PHE A 476 7.564 61.373 -21.085 1.00 18.98 C ANISOU 2445 CG PHE A 476 2441 2353 2418 348 595 647 C ATOM 2446 CD1 PHE A 476 6.555 61.629 -20.164 1.00 21.85 C ANISOU 2446 CD1 PHE A 476 2731 2741 2831 278 515 620 C ATOM 2447 CD2 PHE A 476 8.872 61.290 -20.631 1.00 24.21 C ANISOU 2447 CD2 PHE A 476 3040 3020 3139 359 677 639 C ATOM 2448 CE1 PHE A 476 6.842 61.779 -18.802 1.00 20.05 C ANISOU 2448 CE1 PHE A 476 2384 2545 2690 227 517 581 C ATOM 2449 CE2 PHE A 476 9.173 61.443 -19.271 1.00 23.28 C ANISOU 2449 CE2 PHE A 476 2791 2939 3114 304 663 596 C ATOM 2450 CZ PHE A 476 8.159 61.683 -18.358 1.00 22.83 C ANISOU 2450 CZ PHE A 476 2679 2910 3086 241 584 565 C ATOM 2451 N ASP A 477 6.389 59.480 -25.240 1.00 23.67 N ANISOU 2451 N ASP A 477 3575 2844 2573 556 471 701 N ATOM 2452 CA ASP A 477 6.158 59.698 -26.664 1.00 26.23 C ANISOU 2452 CA ASP A 477 4055 3136 2776 644 472 737 C ATOM 2453 C ASP A 477 6.167 58.424 -27.526 1.00 29.01 C ANISOU 2453 C ASP A 477 4590 3455 2978 702 414 710 C ATOM 2454 O ASP A 477 6.053 58.494 -28.750 1.00 37.34 O ANISOU 2454 O ASP A 477 5800 4480 3907 791 413 734 O ATOM 2455 CB ASP A 477 7.202 60.681 -27.200 1.00 28.99 C ANISOU 2455 CB ASP A 477 4401 3463 3150 721 647 806 C ATOM 2456 CG ASP A 477 6.772 61.329 -28.491 1.00 53.08 C ANISOU 2456 CG ASP A 477 7577 6490 6101 812 659 858 C ATOM 2457 OD1 ASP A 477 5.605 61.118 -28.894 1.00 51.20 O ANISOU 2457 OD1 ASP A 477 7411 6261 5782 803 514 837 O ATOM 2458 OD2 ASP A 477 7.599 62.045 -29.100 1.00 58.62 O ANISOU 2458 OD2 ASP A 477 8302 7161 6811 897 813 923 O ATOM 2459 N GLY A 478 6.290 57.265 -26.894 1.00 26.87 N ANISOU 2459 N GLY A 478 4306 3187 2715 658 369 658 N ATOM 2460 CA GLY A 478 6.440 56.018 -27.630 1.00 27.86 C ANISOU 2460 CA GLY A 478 4597 3275 2713 710 334 628 C ATOM 2461 C GLY A 478 5.152 55.390 -28.138 1.00 37.33 C ANISOU 2461 C GLY A 478 5894 4457 3832 696 152 575 C ATOM 2462 O GLY A 478 5.189 54.464 -28.947 1.00 34.81 O ANISOU 2462 O GLY A 478 5739 4098 3391 749 112 544 O ATOM 2463 N TYR A 479 4.007 55.884 -27.675 1.00 26.01 N ANISOU 2463 N TYR A 479 4362 3045 2475 625 41 565 N ATOM 2464 CA TYR A 479 2.743 55.219 -27.974 1.00 31.88 C ANISOU 2464 CA TYR A 479 5162 3765 3187 595 -145 511 C ATOM 2465 C TYR A 479 1.704 56.197 -28.508 1.00 29.92 C ANISOU 2465 C TYR A 479 4915 3522 2932 600 -236 539 C ATOM 2466 O TYR A 479 1.651 57.357 -28.091 1.00 27.29 O ANISOU 2466 O TYR A 479 4466 3220 2682 577 -172 590 O ATOM 2467 CB TYR A 479 2.195 54.497 -26.733 1.00 24.24 C ANISOU 2467 CB TYR A 479 4060 2802 2347 496 -213 468 C ATOM 2468 CG TYR A 479 3.128 53.445 -26.171 1.00 21.57 C ANISOU 2468 CG TYR A 479 3718 2461 2017 493 -134 443 C ATOM 2469 CD1 TYR A 479 3.059 52.119 -26.600 1.00 23.66 C ANISOU 2469 CD1 TYR A 479 4097 2681 2212 510 -196 388 C ATOM 2470 CD2 TYR A 479 4.078 53.775 -25.209 1.00 21.32 C ANISOU 2470 CD2 TYR A 479 3567 2470 2065 476 0 473 C ATOM 2471 CE1 TYR A 479 3.917 51.150 -26.088 1.00 25.50 C ANISOU 2471 CE1 TYR A 479 4322 2911 2454 511 -111 373 C ATOM 2472 CE2 TYR A 479 4.942 52.803 -24.681 1.00 22.52 C ANISOU 2472 CE2 TYR A 479 3708 2623 2224 478 71 457 C ATOM 2473 CZ TYR A 479 4.857 51.504 -25.134 1.00 24.19 C ANISOU 2473 CZ TYR A 479 4034 2792 2366 497 22 412 C ATOM 2474 OH TYR A 479 5.691 50.545 -24.620 1.00 21.98 O ANISOU 2474 OH TYR A 479 3741 2512 2097 501 101 404 O ATOM 2475 N ILE A 480 0.879 55.721 -29.430 1.00 28.79 N ANISOU 2475 N ILE A 480 4900 3346 2693 629 -388 502 N ATOM 2476 CA ILE A 480 -0.208 56.543 -29.973 1.00 29.59 C ANISOU 2476 CA ILE A 480 5004 3452 2786 634 -499 528 C ATOM 2477 C ILE A 480 -1.379 56.527 -28.987 1.00 27.49 C ANISOU 2477 C ILE A 480 4571 3186 2688 521 -614 513 C ATOM 2478 O ILE A 480 -1.816 55.458 -28.556 1.00 29.15 O ANISOU 2478 O ILE A 480 4761 3364 2952 467 -709 454 O ATOM 2479 CB ILE A 480 -0.683 56.014 -31.353 1.00 44.93 C ANISOU 2479 CB ILE A 480 7155 5359 4559 714 -642 487 C ATOM 2480 CG1 ILE A 480 0.346 56.328 -32.442 1.00 53.75 C ANISOU 2480 CG1 ILE A 480 8449 6473 5501 850 -514 526 C ATOM 2481 CG2 ILE A 480 -2.020 56.638 -31.735 1.00 43.70 C ANISOU 2481 CG2 ILE A 480 6974 5205 4424 699 -804 502 C ATOM 2482 CD1 ILE A 480 1.582 55.486 -32.404 1.00 58.28 C ANISOU 2482 CD1 ILE A 480 9099 7024 6022 887 -385 507 C ATOM 2483 N PRO A 481 -1.863 57.711 -28.591 1.00 28.87 N ANISOU 2483 N PRO A 481 4624 3389 2958 487 -588 574 N ATOM 2484 CA PRO A 481 -2.994 57.798 -27.655 1.00 25.26 C ANISOU 2484 CA PRO A 481 4009 2921 2667 388 -677 577 C ATOM 2485 C PRO A 481 -4.261 57.167 -28.235 1.00 28.96 C ANISOU 2485 C PRO A 481 4526 3342 3135 373 -893 538 C ATOM 2486 O PRO A 481 -4.378 57.025 -29.454 1.00 27.04 O ANISOU 2486 O PRO A 481 4438 3087 2750 445 -983 519 O ATOM 2487 CB PRO A 481 -3.180 59.316 -27.459 1.00 24.79 C ANISOU 2487 CB PRO A 481 3853 2897 2671 381 -595 657 C ATOM 2488 CG PRO A 481 -2.425 59.947 -28.595 1.00 41.96 C ANISOU 2488 CG PRO A 481 6156 5090 4698 488 -511 693 C ATOM 2489 CD PRO A 481 -1.279 59.034 -28.868 1.00 32.40 C ANISOU 2489 CD PRO A 481 5058 3870 3382 539 -444 649 C ATOM 2490 N HIS A 482 -5.187 56.771 -27.369 1.00 28.22 N ANISOU 2490 N HIS A 482 4305 3215 3202 286 -977 525 N ATOM 2491 CA HIS A 482 -6.460 56.195 -27.820 1.00 29.31 C ANISOU 2491 CA HIS A 482 4457 3295 3386 260 -1189 491 C ATOM 2492 C HIS A 482 -7.167 57.099 -28.835 1.00 29.86 C ANISOU 2492 C HIS A 482 4577 3374 3396 302 -1288 534 C ATOM 2493 O HIS A 482 -7.319 58.300 -28.605 1.00 29.25 O ANISOU 2493 O HIS A 482 4416 3332 3367 296 -1209 614 O ATOM 2494 CB HIS A 482 -7.386 55.939 -26.624 1.00 35.12 C ANISOU 2494 CB HIS A 482 5015 3987 4342 164 -1226 503 C ATOM 2495 CG HIS A 482 -8.606 55.141 -26.968 1.00 36.51 C ANISOU 2495 CG HIS A 482 5184 4084 4602 130 -1437 460 C ATOM 2496 ND1 HIS A 482 -8.679 53.777 -26.775 1.00 45.53 N ANISOU 2496 ND1 HIS A 482 6342 5167 5790 107 -1503 383 N ATOM 2497 CD2 HIS A 482 -9.794 55.511 -27.504 1.00 38.93 C ANISOU 2497 CD2 HIS A 482 5466 4357 4970 117 -1599 483 C ATOM 2498 CE1 HIS A 482 -9.861 53.341 -27.177 1.00 47.53 C ANISOU 2498 CE1 HIS A 482 6575 5346 6136 78 -1700 355 C ATOM 2499 NE2 HIS A 482 -10.558 54.373 -27.620 1.00 48.68 N ANISOU 2499 NE2 HIS A 482 6695 5507 6293 83 -1768 415 N ATOM 2500 N PRO A 483 -7.615 56.520 -29.962 1.00 28.49 N ANISOU 2500 N PRO A 483 4542 3167 3115 349 -1464 479 N ATOM 2501 CA PRO A 483 -8.195 57.307 -31.060 1.00 28.68 C ANISOU 2501 CA PRO A 483 4643 3207 3045 411 -1567 516 C ATOM 2502 C PRO A 483 -9.478 58.034 -30.687 1.00 34.47 C ANISOU 2502 C PRO A 483 5219 3926 3951 347 -1656 581 C ATOM 2503 O PRO A 483 -9.816 59.021 -31.342 1.00 36.30 O ANISOU 2503 O PRO A 483 5473 4189 4129 395 -1676 645 O ATOM 2504 CB PRO A 483 -8.503 56.244 -32.130 1.00 30.71 C ANISOU 2504 CB PRO A 483 5072 3418 3178 458 -1770 419 C ATOM 2505 CG PRO A 483 -8.540 54.934 -31.371 1.00 36.14 C ANISOU 2505 CG PRO A 483 5703 4046 3981 381 -1805 340 C ATOM 2506 CD PRO A 483 -7.468 55.100 -30.332 1.00 35.74 C ANISOU 2506 CD PRO A 483 5573 4036 3971 359 -1564 376 C ATOM 2507 N ASP A 484 -10.187 57.553 -29.670 1.00 34.05 N ANISOU 2507 N ASP A 484 5011 3821 4107 247 -1699 574 N ATOM 2508 CA ASP A 484 -11.443 58.187 -29.274 1.00 34.65 C ANISOU 2508 CA ASP A 484 4931 3867 4368 185 -1775 645 C ATOM 2509 C ASP A 484 -11.244 59.126 -28.088 1.00 26.95 C ANISOU 2509 C ASP A 484 3802 2921 3517 136 -1574 731 C ATOM 2510 O ASP A 484 -11.671 60.277 -28.132 1.00 34.52 O ANISOU 2510 O ASP A 484 4697 3903 4516 138 -1538 818 O ATOM 2511 CB ASP A 484 -12.501 57.141 -28.914 1.00 41.30 C ANISOU 2511 CB ASP A 484 5688 4614 5391 111 -1950 597 C ATOM 2512 CG ASP A 484 -12.886 56.260 -30.093 1.00 51.55 C ANISOU 2512 CG ASP A 484 7126 5871 6591 149 -2182 504 C ATOM 2513 OD1 ASP A 484 -12.837 56.737 -31.251 1.00 53.25 O ANISOU 2513 OD1 ASP A 484 7477 6127 6630 230 -2259 505 O ATOM 2514 OD2 ASP A 484 -13.252 55.088 -29.848 1.00 50.16 O ANISOU 2514 OD2 ASP A 484 6924 5617 6518 103 -2287 428 O ATOM 2515 N THR A 485 -10.599 58.626 -27.037 1.00 29.01 N ANISOU 2515 N THR A 485 4007 3179 3836 98 -1447 706 N ATOM 2516 CA THR A 485 -10.500 59.377 -25.776 1.00 31.03 C ANISOU 2516 CA THR A 485 4117 3451 4223 47 -1277 773 C ATOM 2517 C THR A 485 -9.257 60.264 -25.655 1.00 31.71 C ANISOU 2517 C THR A 485 4232 3615 4199 88 -1077 798 C ATOM 2518 O THR A 485 -9.230 61.176 -24.841 1.00 26.39 O ANISOU 2518 O THR A 485 3452 2960 3614 56 -950 857 O ATOM 2519 CB THR A 485 -10.517 58.439 -24.550 1.00 24.73 C ANISOU 2519 CB THR A 485 3229 2607 3560 -11 -1239 740 C ATOM 2520 OG1 THR A 485 -9.345 57.622 -24.567 1.00 27.79 O ANISOU 2520 OG1 THR A 485 3711 3024 3824 21 -1175 666 O ATOM 2521 CG2 THR A 485 -11.754 57.526 -24.565 1.00 38.91 C ANISOU 2521 CG2 THR A 485 4973 4307 5505 -55 -1420 720 C ATOM 2522 N GLY A 486 -8.224 59.994 -26.448 1.00 28.80 N ANISOU 2522 N GLY A 486 4008 3285 3650 159 -1046 752 N ATOM 2523 CA GLY A 486 -6.967 60.710 -26.302 1.00 22.73 C ANISOU 2523 CA GLY A 486 3257 2576 2804 197 -852 772 C ATOM 2524 C GLY A 486 -6.170 60.281 -25.061 1.00 24.89 C ANISOU 2524 C GLY A 486 3457 2858 3140 155 -728 741 C ATOM 2525 O GLY A 486 -5.159 60.896 -24.711 1.00 25.84 O ANISOU 2525 O GLY A 486 3559 3022 3237 172 -571 756 O ATOM 2526 N LYS A 487 -6.612 59.229 -24.376 1.00 23.71 N ANISOU 2526 N LYS A 487 3262 2666 3079 105 -798 700 N ATOM 2527 CA LYS A 487 -5.806 58.707 -23.260 1.00 24.50 C ANISOU 2527 CA LYS A 487 3311 2780 3216 82 -686 669 C ATOM 2528 C LYS A 487 -4.442 58.224 -23.749 1.00 31.46 C ANISOU 2528 C LYS A 487 4308 3698 3949 142 -614 624 C ATOM 2529 O LYS A 487 -4.359 57.505 -24.740 1.00 27.63 O ANISOU 2529 O LYS A 487 3950 3194 3355 185 -697 583 O ATOM 2530 CB LYS A 487 -6.508 57.541 -22.575 1.00 35.54 C ANISOU 2530 CB LYS A 487 4657 4120 4726 36 -769 636 C ATOM 2531 CG LYS A 487 -7.375 57.910 -21.400 1.00 47.45 C ANISOU 2531 CG LYS A 487 6019 5597 6415 -23 -745 687 C ATOM 2532 CD LYS A 487 -7.636 56.660 -20.577 1.00 46.57 C ANISOU 2532 CD LYS A 487 5864 5434 6398 -48 -767 652 C ATOM 2533 CE LYS A 487 -8.811 56.834 -19.649 1.00 41.21 C ANISOU 2533 CE LYS A 487 5054 4691 5911 -95 -777 710 C ATOM 2534 NZ LYS A 487 -9.245 55.486 -19.188 1.00 36.18 N ANISOU 2534 NZ LYS A 487 4389 3983 5375 -107 -828 678 N ATOM 2535 N ASP A 488 -3.368 58.607 -23.063 1.00 19.62 N ANISOU 2535 N ASP A 488 2885 2078 2494 94 -710 257 N ATOM 2536 CA ASP A 488 -2.050 58.162 -23.499 1.00 19.97 C ANISOU 2536 CA ASP A 488 3056 2140 2390 119 -655 240 C ATOM 2537 C ASP A 488 -1.426 57.151 -22.523 1.00 25.97 C ANISOU 2537 C ASP A 488 3794 2932 3142 107 -560 222 C ATOM 2538 O ASP A 488 -2.066 56.742 -21.536 1.00 21.24 O ANISOU 2538 O ASP A 488 3089 2335 2645 78 -542 223 O ATOM 2539 CB ASP A 488 -1.119 59.360 -23.797 1.00 19.59 C ANISOU 2539 CB ASP A 488 3048 2124 2273 157 -582 260 C ATOM 2540 CG ASP A 488 -0.873 60.236 -22.587 1.00 25.65 C ANISOU 2540 CG ASP A 488 3706 2932 3109 147 -477 264 C ATOM 2541 OD1 ASP A 488 -1.023 59.743 -21.438 1.00 22.37 O ANISOU 2541 OD1 ASP A 488 3209 2541 2751 126 -426 247 O ATOM 2542 OD2 ASP A 488 -0.521 61.428 -22.784 1.00 24.84 O ANISOU 2542 OD2 ASP A 488 3607 2831 3000 163 -445 283 O ATOM 2543 N ALA A 489 -0.195 56.732 -22.801 1.00 20.57 N ANISOU 2543 N ALA A 489 3207 2271 2338 138 -494 217 N ATOM 2544 CA ALA A 489 0.458 55.724 -21.955 1.00 25.84 C ANISOU 2544 CA ALA A 489 3861 2967 2989 137 -408 209 C ATOM 2545 C ALA A 489 0.596 56.188 -20.505 1.00 24.96 C ANISOU 2545 C ALA A 489 3621 2917 2946 124 -313 216 C ATOM 2546 O ALA A 489 0.407 55.414 -19.565 1.00 18.97 O ANISOU 2546 O ALA A 489 2805 2170 2231 110 -274 215 O ATOM 2547 CB ALA A 489 1.810 55.348 -22.509 1.00 22.23 C ANISOU 2547 CB ALA A 489 3516 2531 2398 185 -342 216 C ATOM 2548 N LEU A 490 0.953 57.446 -20.323 1.00 23.95 N ANISOU 2548 N LEU A 490 3460 2822 2819 130 -274 224 N ATOM 2549 CA LEU A 490 1.084 57.992 -18.978 1.00 23.45 C ANISOU 2549 CA LEU A 490 3298 2807 2804 121 -197 220 C ATOM 2550 C LEU A 490 -0.262 57.953 -18.236 1.00 27.09 C ANISOU 2550 C LEU A 490 3665 3246 3381 104 -217 218 C ATOM 2551 O LEU A 490 -0.323 57.555 -17.067 1.00 26.18 O ANISOU 2551 O LEU A 490 3490 3164 3294 104 -152 216 O ATOM 2552 CB LEU A 490 1.664 59.405 -19.067 1.00 22.54 C ANISOU 2552 CB LEU A 490 3181 2708 2675 125 -170 223 C ATOM 2553 CG LEU A 490 2.227 60.091 -17.841 1.00 27.47 C ANISOU 2553 CG LEU A 490 3744 3381 3312 115 -96 208 C ATOM 2554 CD1 LEU A 490 3.216 59.182 -17.114 1.00 24.62 C ANISOU 2554 CD1 LEU A 490 3378 3083 2893 119 -35 209 C ATOM 2555 CD2 LEU A 490 2.887 61.426 -18.253 1.00 23.73 C ANISOU 2555 CD2 LEU A 490 3289 2900 2828 109 -87 215 C ATOM 2556 N ASP A 491 -1.344 58.308 -18.929 1.00 19.27 N ANISOU 2556 N ASP A 491 2661 2202 2458 96 -304 228 N ATOM 2557 CA ASP A 491 -2.684 58.231 -18.352 1.00 19.17 C ANISOU 2557 CA ASP A 491 2544 2164 2575 84 -324 244 C ATOM 2558 C ASP A 491 -2.973 56.800 -17.906 1.00 26.91 C ANISOU 2558 C ASP A 491 3501 3136 3589 63 -319 252 C ATOM 2559 O ASP A 491 -3.475 56.564 -16.801 1.00 27.22 O ANISOU 2559 O ASP A 491 3450 3190 3703 65 -253 270 O ATOM 2560 CB ASP A 491 -3.766 58.642 -19.365 1.00 21.90 C ANISOU 2560 CB ASP A 491 2878 2452 2990 76 -444 265 C ATOM 2561 CG ASP A 491 -3.802 60.148 -19.653 1.00 36.01 C ANISOU 2561 CG ASP A 491 4663 4236 4782 102 -442 272 C ATOM 2562 OD1 ASP A 491 -3.798 60.987 -18.710 1.00 27.36 O ANISOU 2562 OD1 ASP A 491 3512 3161 3722 121 -356 269 O ATOM 2563 OD2 ASP A 491 -3.880 60.490 -20.855 1.00 31.06 O ANISOU 2563 OD2 ASP A 491 4101 3578 4120 108 -531 282 O ATOM 2564 N ILE A 492 -2.683 55.838 -18.773 1.00 21.99 N ANISOU 2564 N ILE A 492 2965 2479 2909 49 -383 242 N ATOM 2565 CA ILE A 492 -2.983 54.446 -18.454 1.00 18.62 C ANISOU 2565 CA ILE A 492 2527 2023 2523 25 -387 249 C ATOM 2566 C ILE A 492 -2.168 54.019 -17.237 1.00 20.72 C ANISOU 2566 C ILE A 492 2772 2351 2749 48 -253 254 C ATOM 2567 O ILE A 492 -2.690 53.423 -16.297 1.00 19.43 O ANISOU 2567 O ILE A 492 2531 2188 2664 40 -204 281 O ATOM 2568 CB ILE A 492 -2.629 53.506 -19.624 1.00 16.29 C ANISOU 2568 CB ILE A 492 2365 1673 2149 15 -472 224 C ATOM 2569 CG1 ILE A 492 -3.618 53.714 -20.782 1.00 24.18 C ANISOU 2569 CG1 ILE A 492 3388 2605 3195 -13 -631 220 C ATOM 2570 CG2 ILE A 492 -2.652 52.043 -19.167 1.00 20.44 C ANISOU 2570 CG2 ILE A 492 2897 2165 2703 -4 -449 228 C ATOM 2571 CD1 ILE A 492 -3.165 53.068 -22.070 1.00 31.44 C ANISOU 2571 CD1 ILE A 492 4477 3472 3995 -5 -719 183 C ATOM 2572 N MET A 493 -0.883 54.335 -17.245 1.00 17.70 N ANISOU 2572 N MET A 493 2454 2023 2248 78 -195 237 N ATOM 2573 CA MET A 493 0.000 53.827 -16.197 1.00 23.79 C ANISOU 2573 CA MET A 493 3215 2856 2968 102 -89 245 C ATOM 2574 C MET A 493 -0.294 54.447 -14.825 1.00 21.72 C ANISOU 2574 C MET A 493 2857 2646 2751 113 -12 254 C ATOM 2575 O MET A 493 -0.286 53.747 -13.805 1.00 18.05 O ANISOU 2575 O MET A 493 2355 2209 2296 127 58 275 O ATOM 2576 CB MET A 493 1.460 54.015 -16.583 1.00 19.28 C ANISOU 2576 CB MET A 493 2720 2332 2274 129 -54 237 C ATOM 2577 CG MET A 493 1.939 53.047 -17.682 1.00 24.50 C ANISOU 2577 CG MET A 493 3494 2949 2866 143 -86 236 C ATOM 2578 SD MET A 493 3.473 53.615 -18.427 1.00 25.57 S ANISOU 2578 SD MET A 493 3708 3131 2877 184 -45 244 S ATOM 2579 CE MET A 493 4.666 53.286 -17.113 1.00 15.71 C ANISOU 2579 CE MET A 493 2398 1978 1592 209 68 271 C ATOM 2580 N MET A 494 -0.573 55.747 -14.810 1.00 18.51 N ANISOU 2580 N MET A 494 2421 2246 2367 115 -22 239 N ATOM 2581 CA MET A 494 -0.837 56.462 -13.559 1.00 20.89 C ANISOU 2581 CA MET A 494 2658 2586 2694 137 52 237 C ATOM 2582 C MET A 494 -1.992 55.876 -12.786 1.00 22.32 C ANISOU 2582 C MET A 494 2758 2748 2976 145 90 274 C ATOM 2583 O MET A 494 -2.011 55.910 -11.551 1.00 24.34 O ANISOU 2583 O MET A 494 2980 3046 3221 178 180 282 O ATOM 2584 CB MET A 494 -1.156 57.938 -13.827 1.00 19.84 C ANISOU 2584 CB MET A 494 2516 2435 2588 140 27 217 C ATOM 2585 CG MET A 494 0.045 58.766 -14.113 1.00 26.13 C ANISOU 2585 CG MET A 494 3371 3260 3297 136 26 187 C ATOM 2586 SD MET A 494 -0.419 60.500 -14.121 1.00 25.43 S ANISOU 2586 SD MET A 494 3269 3137 3256 143 18 165 S ATOM 2587 CE MET A 494 -1.825 60.552 -15.234 1.00 26.02 C ANISOU 2587 CE MET A 494 3313 3138 3436 140 -66 200 C ATOM 2588 N PHE A 495 -2.980 55.366 -13.504 1.00 18.44 N ANISOU 2588 N PHE A 495 2234 2190 2584 115 20 301 N ATOM 2589 CA PHE A 495 -4.161 54.832 -12.838 1.00 21.12 C ANISOU 2589 CA PHE A 495 2473 2502 3049 116 55 354 C ATOM 2590 C PHE A 495 -4.238 53.304 -12.859 1.00 22.01 C ANISOU 2590 C PHE A 495 2587 2582 3194 88 49 385 C ATOM 2591 O PHE A 495 -5.213 52.717 -12.394 1.00 21.32 O ANISOU 2591 O PHE A 495 2410 2461 3230 77 75 441 O ATOM 2592 CB PHE A 495 -5.428 55.473 -13.424 1.00 23.11 C ANISOU 2592 CB PHE A 495 2650 2699 3432 100 -16 379 C ATOM 2593 CG PHE A 495 -5.516 56.948 -13.161 1.00 21.91 C ANISOU 2593 CG PHE A 495 2486 2569 3270 141 18 360 C ATOM 2594 CD1 PHE A 495 -5.989 57.420 -11.944 1.00 26.20 C ANISOU 2594 CD1 PHE A 495 2967 3137 3850 194 133 382 C ATOM 2595 CD2 PHE A 495 -5.102 57.872 -14.123 1.00 20.54 C ANISOU 2595 CD2 PHE A 495 2375 2384 3044 133 -56 323 C ATOM 2596 CE1 PHE A 495 -6.068 58.796 -11.697 1.00 19.00 C ANISOU 2596 CE1 PHE A 495 2062 2230 2925 236 167 357 C ATOM 2597 CE2 PHE A 495 -5.181 59.240 -13.877 1.00 23.51 C ANISOU 2597 CE2 PHE A 495 2747 2766 3419 169 -21 307 C ATOM 2598 CZ PHE A 495 -5.657 59.697 -12.657 1.00 21.81 C ANISOU 2598 CZ PHE A 495 2477 2568 3242 219 88 319 C ATOM 2599 N HIS A 496 -3.192 52.648 -13.350 1.00 16.98 N ANISOU 2599 N HIS A 496 2048 1950 2452 80 27 356 N ATOM 2600 CA HIS A 496 -3.203 51.178 -13.385 1.00 16.73 C ANISOU 2600 CA HIS A 496 2036 1874 2447 59 26 382 C ATOM 2601 C HIS A 496 -2.785 50.568 -12.046 1.00 16.63 C ANISOU 2601 C HIS A 496 1999 1916 2404 100 157 418 C ATOM 2602 O HIS A 496 -1.905 51.105 -11.366 1.00 17.95 O ANISOU 2602 O HIS A 496 2189 2168 2465 146 226 401 O ATOM 2603 CB HIS A 496 -2.249 50.661 -14.464 1.00 15.66 C ANISOU 2603 CB HIS A 496 2029 1715 2206 51 -37 341 C ATOM 2604 CG HIS A 496 -2.422 49.203 -14.760 1.00 18.48 C ANISOU 2604 CG HIS A 496 2426 1994 2601 24 -66 355 C ATOM 2605 ND1 HIS A 496 -1.644 48.227 -14.174 1.00 18.94 N ANISOU 2605 ND1 HIS A 496 2523 2070 2604 55 21 375 N ATOM 2606 CD2 HIS A 496 -3.298 48.554 -15.566 1.00 19.76 C ANISOU 2606 CD2 HIS A 496 2598 2052 2857 -34 -177 354 C ATOM 2607 CE1 HIS A 496 -2.024 47.043 -14.614 1.00 20.50 C ANISOU 2607 CE1 HIS A 496 2759 2169 2859 20 -27 382 C ATOM 2608 NE2 HIS A 496 -3.018 47.215 -15.469 1.00 17.50 N ANISOU 2608 NE2 HIS A 496 2366 1712 2570 -39 -154 365 N ATOM 2609 N GLN A 497 -3.360 49.416 -11.700 1.00 16.48 N ANISOU 2609 N GLN A 497 1940 1845 2475 83 182 470 N ATOM 2610 CA GLN A 497 -3.084 48.776 -10.413 1.00 20.08 C ANISOU 2610 CA GLN A 497 2372 2348 2910 129 312 521 C ATOM 2611 C GLN A 497 -1.601 48.438 -10.196 1.00 19.69 C ANISOU 2611 C GLN A 497 2416 2365 2701 173 356 499 C ATOM 2612 O GLN A 497 -1.135 48.390 -9.059 1.00 17.79 O ANISOU 2612 O GLN A 497 2163 2200 2395 227 456 526 O ATOM 2613 CB GLN A 497 -3.938 47.515 -10.224 1.00 22.36 C ANISOU 2613 CB GLN A 497 2606 2552 3337 96 329 590 C ATOM 2614 CG GLN A 497 -3.592 46.398 -11.175 1.00 24.04 C ANISOU 2614 CG GLN A 497 2908 2679 3548 53 250 569 C ATOM 2615 CD GLN A 497 -4.488 45.182 -11.003 1.00 34.94 C ANISOU 2615 CD GLN A 497 4232 3956 5087 6 254 636 C ATOM 2616 OE1 GLN A 497 -4.832 44.802 -9.882 1.00 29.13 O ANISOU 2616 OE1 GLN A 497 3419 3239 4410 34 373 715 O ATOM 2617 NE2 GLN A 497 -4.851 44.553 -12.114 1.00 36.20 N ANISOU 2617 NE2 GLN A 497 4439 4001 5313 -66 124 607 N ATOM 2618 N PHE A 498 -0.869 48.191 -11.285 1.00 15.74 N ANISOU 2618 N PHE A 498 2007 1837 2136 156 283 456 N ATOM 2619 CA PHE A 498 0.569 47.956 -11.189 1.00 15.59 C ANISOU 2619 CA PHE A 498 2063 1884 1978 202 325 446 C ATOM 2620 C PHE A 498 1.389 49.090 -11.813 1.00 16.87 C ANISOU 2620 C PHE A 498 2265 2098 2047 207 281 393 C ATOM 2621 O PHE A 498 2.473 49.446 -11.324 1.00 16.67 O ANISOU 2621 O PHE A 498 2250 2161 1924 244 326 391 O ATOM 2622 CB PHE A 498 0.956 46.620 -11.846 1.00 17.94 C ANISOU 2622 CB PHE A 498 2443 2109 2265 201 311 455 C ATOM 2623 CG PHE A 498 0.165 45.446 -11.336 1.00 17.36 C ANISOU 2623 CG PHE A 498 2335 1962 2299 185 348 511 C ATOM 2624 CD1 PHE A 498 0.001 45.244 -9.971 1.00 23.10 C ANISOU 2624 CD1 PHE A 498 2989 2743 3045 222 456 573 C ATOM 2625 CD2 PHE A 498 -0.426 44.554 -12.215 1.00 16.89 C ANISOU 2625 CD2 PHE A 498 2321 1774 2321 133 272 503 C ATOM 2626 CE1 PHE A 498 -0.752 44.166 -9.488 1.00 24.43 C ANISOU 2626 CE1 PHE A 498 3117 2839 3326 208 503 640 C ATOM 2627 CE2 PHE A 498 -1.167 43.464 -11.744 1.00 18.03 C ANISOU 2627 CE2 PHE A 498 2426 1837 2587 108 304 560 C ATOM 2628 CZ PHE A 498 -1.337 43.277 -10.376 1.00 23.70 C ANISOU 2628 CZ PHE A 498 3058 2611 3336 145 427 635 C ATOM 2629 N GLY A 499 0.893 49.625 -12.920 1.00 15.26 N ANISOU 2629 N GLY A 499 2084 1837 1879 168 188 357 N ATOM 2630 CA GLY A 499 1.596 50.683 -13.617 1.00 14.61 C ANISOU 2630 CA GLY A 499 2042 1789 1721 171 150 319 C ATOM 2631 C GLY A 499 1.827 51.915 -12.758 1.00 18.12 C ANISOU 2631 C GLY A 499 2429 2314 2142 184 189 308 C ATOM 2632 O GLY A 499 2.805 52.631 -12.960 1.00 16.85 O ANISOU 2632 O GLY A 499 2294 2202 1905 194 189 289 O ATOM 2633 N ASN A 500 0.940 52.171 -11.797 1.00 14.58 N ANISOU 2633 N ASN A 500 1906 1872 1760 187 226 321 N ATOM 2634 CA ASN A 500 1.087 53.371 -10.972 1.00 14.20 C ANISOU 2634 CA ASN A 500 1827 1886 1683 205 260 298 C ATOM 2635 C ASN A 500 2.426 53.409 -10.214 1.00 16.27 C ANISOU 2635 C ASN A 500 2111 2239 1831 235 306 293 C ATOM 2636 O ASN A 500 2.999 54.495 -9.971 1.00 14.92 O ANISOU 2636 O ASN A 500 1945 2111 1612 233 296 258 O ATOM 2637 CB ASN A 500 -0.099 53.505 -10.004 1.00 15.45 C ANISOU 2637 CB ASN A 500 1914 2035 1923 222 313 321 C ATOM 2638 CG ASN A 500 0.040 52.608 -8.772 1.00 18.13 C ANISOU 2638 CG ASN A 500 2236 2419 2232 264 407 364 C ATOM 2639 OD1 ASN A 500 0.643 53.000 -7.780 1.00 17.02 O ANISOU 2639 OD1 ASN A 500 2109 2354 2005 304 458 352 O ATOM 2640 ND2 ASN A 500 -0.534 51.408 -8.831 1.00 18.46 N ANISOU 2640 ND2 ASN A 500 2254 2411 2348 256 425 416 N ATOM 2641 N TYR A 501 2.928 52.228 -9.841 1.00 15.25 N ANISOU 2641 N TYR A 501 1994 2134 1665 261 349 331 N ATOM 2642 CA TYR A 501 4.202 52.140 -9.126 1.00 15.45 C ANISOU 2642 CA TYR A 501 2030 2251 1587 293 384 340 C ATOM 2643 C TYR A 501 5.379 52.480 -10.039 1.00 16.45 C ANISOU 2643 C TYR A 501 2190 2398 1663 279 342 329 C ATOM 2644 O TYR A 501 6.412 53.000 -9.587 1.00 17.37 O ANISOU 2644 O TYR A 501 2295 2589 1715 285 341 324 O ATOM 2645 CB TYR A 501 4.405 50.739 -8.549 1.00 13.83 C ANISOU 2645 CB TYR A 501 1828 2062 1363 333 446 398 C ATOM 2646 CG TYR A 501 3.427 50.405 -7.448 1.00 14.28 C ANISOU 2646 CG TYR A 501 1848 2118 1462 359 511 428 C ATOM 2647 CD1 TYR A 501 3.620 50.895 -6.161 1.00 16.63 C ANISOU 2647 CD1 TYR A 501 2133 2496 1690 400 555 425 C ATOM 2648 CD2 TYR A 501 2.313 49.613 -7.702 1.00 16.34 C ANISOU 2648 CD2 TYR A 501 2087 2292 1829 344 527 462 C ATOM 2649 CE1 TYR A 501 2.719 50.600 -5.117 1.00 16.26 C ANISOU 2649 CE1 TYR A 501 2060 2449 1668 440 635 463 C ATOM 2650 CE2 TYR A 501 1.402 49.300 -6.664 1.00 16.45 C ANISOU 2650 CE2 TYR A 501 2054 2304 1894 372 605 509 C ATOM 2651 CZ TYR A 501 1.630 49.800 -5.387 1.00 16.45 C ANISOU 2651 CZ TYR A 501 2049 2390 1811 427 667 512 C ATOM 2652 OH TYR A 501 0.754 49.497 -4.388 1.00 18.25 O ANISOU 2652 OH TYR A 501 2240 2616 2077 470 760 567 O ATOM 2653 N VAL A 502 5.235 52.161 -11.319 1.00 15.90 N ANISOU 2653 N VAL A 502 2162 2259 1621 263 307 329 N ATOM 2654 CA VAL A 502 6.283 52.481 -12.285 1.00 13.83 C ANISOU 2654 CA VAL A 502 1937 2008 1310 262 285 331 C ATOM 2655 C VAL A 502 6.375 53.998 -12.474 1.00 19.11 C ANISOU 2655 C VAL A 502 2587 2687 1988 227 244 295 C ATOM 2656 O VAL A 502 7.469 54.564 -12.495 1.00 17.61 O ANISOU 2656 O VAL A 502 2384 2549 1757 223 245 303 O ATOM 2657 CB VAL A 502 6.036 51.799 -13.642 1.00 15.23 C ANISOU 2657 CB VAL A 502 2189 2101 1496 264 258 335 C ATOM 2658 CG1 VAL A 502 7.032 52.349 -14.709 1.00 17.29 C ANISOU 2658 CG1 VAL A 502 2494 2371 1704 273 248 342 C ATOM 2659 CG2 VAL A 502 6.180 50.263 -13.499 1.00 18.08 C ANISOU 2659 CG2 VAL A 502 2585 2442 1843 301 303 370 C ATOM 2660 N VAL A 503 5.230 54.660 -12.610 1.00 15.50 N ANISOU 2660 N VAL A 503 2120 2176 1593 201 209 262 N ATOM 2661 CA VAL A 503 5.247 56.121 -12.737 1.00 17.04 C ANISOU 2661 CA VAL A 503 2303 2368 1803 173 177 229 C ATOM 2662 C VAL A 503 5.807 56.780 -11.462 1.00 17.93 C ANISOU 2662 C VAL A 503 2380 2550 1883 172 198 208 C ATOM 2663 O VAL A 503 6.525 57.771 -11.536 1.00 17.53 O ANISOU 2663 O VAL A 503 2326 2516 1819 146 174 191 O ATOM 2664 CB VAL A 503 3.856 56.711 -13.054 1.00 15.10 C ANISOU 2664 CB VAL A 503 2049 2051 1637 157 140 206 C ATOM 2665 CG1 VAL A 503 3.971 58.236 -13.277 1.00 18.74 C ANISOU 2665 CG1 VAL A 503 2509 2498 2112 135 113 177 C ATOM 2666 CG2 VAL A 503 3.248 56.050 -14.296 1.00 16.68 C ANISOU 2666 CG2 VAL A 503 2289 2182 1868 152 93 222 C ATOM 2667 N GLN A 504 5.471 56.241 -10.291 1.00 15.37 N ANISOU 2667 N GLN A 504 2036 2261 1544 199 238 209 N ATOM 2668 CA GLN A 504 6.026 56.779 -9.039 1.00 13.82 C ANISOU 2668 CA GLN A 504 1827 2133 1292 206 247 184 C ATOM 2669 C GLN A 504 7.549 56.684 -9.056 1.00 19.28 C ANISOU 2669 C GLN A 504 2508 2893 1924 197 230 206 C ATOM 2670 O GLN A 504 8.242 57.589 -8.595 1.00 19.58 O ANISOU 2670 O GLN A 504 2536 2965 1938 170 193 177 O ATOM 2671 CB GLN A 504 5.473 56.023 -7.807 1.00 15.03 C ANISOU 2671 CB GLN A 504 1972 2319 1420 255 306 198 C ATOM 2672 CG GLN A 504 3.992 56.302 -7.517 1.00 27.92 C ANISOU 2672 CG GLN A 504 3596 3895 3119 271 338 185 C ATOM 2673 CD GLN A 504 3.463 55.519 -6.310 1.00 27.65 C ANISOU 2673 CD GLN A 504 3551 3892 3062 327 416 217 C ATOM 2674 OE1 GLN A 504 3.807 55.814 -5.174 1.00 32.66 O ANISOU 2674 OE1 GLN A 504 4208 4586 3615 361 440 197 O ATOM 2675 NE2 GLN A 504 2.612 54.532 -6.563 1.00 16.80 N ANISOU 2675 NE2 GLN A 504 2149 2474 1761 337 453 269 N ATOM 2676 N CYS A 505 8.052 55.557 -9.556 1.00 19.94 N ANISOU 2676 N CYS A 505 2593 2992 1993 221 255 262 N ATOM 2677 CA CYS A 505 9.484 55.310 -9.655 1.00 17.61 C ANISOU 2677 CA CYS A 505 2273 2763 1654 226 253 305 C ATOM 2678 C CYS A 505 10.125 56.349 -10.589 1.00 17.44 C ANISOU 2678 C CYS A 505 2243 2721 1661 181 216 302 C ATOM 2679 O CYS A 505 11.166 56.931 -10.268 1.00 19.68 O ANISOU 2679 O CYS A 505 2484 3059 1935 154 187 311 O ATOM 2680 CB CYS A 505 9.726 53.894 -10.185 1.00 24.66 C ANISOU 2680 CB CYS A 505 3185 3652 2534 273 303 366 C ATOM 2681 SG CYS A 505 11.448 53.449 -10.432 1.00 25.18 S ANISOU 2681 SG CYS A 505 3214 3794 2558 302 324 441 S ATOM 2682 N MET A 506 9.503 56.588 -11.740 1.00 13.53 N ANISOU 2682 N MET A 506 1787 2148 1207 170 211 295 N ATOM 2683 CA MET A 506 10.000 57.622 -12.664 1.00 15.35 C ANISOU 2683 CA MET A 506 2017 2350 1466 134 186 301 C ATOM 2684 C MET A 506 10.114 58.983 -11.993 1.00 16.10 C ANISOU 2684 C MET A 506 2082 2448 1587 81 140 253 C ATOM 2685 O MET A 506 11.117 59.700 -12.133 1.00 17.32 O ANISOU 2685 O MET A 506 2200 2622 1758 43 120 272 O ATOM 2686 CB MET A 506 9.063 57.738 -13.869 1.00 15.21 C ANISOU 2686 CB MET A 506 2058 2244 1478 138 176 292 C ATOM 2687 CG MET A 506 9.088 56.522 -14.797 1.00 17.34 C ANISOU 2687 CG MET A 506 2383 2491 1715 185 207 332 C ATOM 2688 SD MET A 506 7.742 56.558 -16.014 1.00 21.49 S ANISOU 2688 SD MET A 506 2986 2912 2269 185 162 307 S ATOM 2689 CE MET A 506 8.128 58.061 -16.921 1.00 21.11 C ANISOU 2689 CE MET A 506 2945 2838 2236 159 141 317 C ATOM 2690 N LEU A 507 9.065 59.358 -11.273 1.00 15.15 N ANISOU 2690 N LEU A 507 1979 2299 1477 79 128 192 N ATOM 2691 CA LEU A 507 9.020 60.663 -10.619 1.00 17.49 C ANISOU 2691 CA LEU A 507 2274 2579 1792 38 87 133 C ATOM 2692 C LEU A 507 10.089 60.785 -9.532 1.00 19.37 C ANISOU 2692 C LEU A 507 2481 2896 1985 18 56 123 C ATOM 2693 O LEU A 507 10.761 61.820 -9.409 1.00 21.25 O ANISOU 2693 O LEU A 507 2703 3125 2246 -39 5 100 O ATOM 2694 CB LEU A 507 7.630 60.886 -10.013 1.00 16.78 C ANISOU 2694 CB LEU A 507 2215 2447 1715 63 101 80 C ATOM 2695 CG LEU A 507 7.463 62.191 -9.228 1.00 20.75 C ANISOU 2695 CG LEU A 507 2741 2920 2223 39 72 8 C ATOM 2696 CD1 LEU A 507 7.669 63.391 -10.151 1.00 21.19 C ANISOU 2696 CD1 LEU A 507 2804 2905 2343 -11 37 2 C ATOM 2697 CD2 LEU A 507 6.063 62.211 -8.592 1.00 21.09 C ANISOU 2697 CD2 LEU A 507 2810 2928 2274 89 114 -26 C ATOM 2698 N THR A 508 10.236 59.734 -8.736 1.00 18.80 N ANISOU 2698 N THR A 508 2398 2894 1851 61 79 142 N ATOM 2699 CA THR A 508 11.211 59.745 -7.643 1.00 23.81 C ANISOU 2699 CA THR A 508 3004 3612 2430 50 37 136 C ATOM 2700 C THR A 508 12.640 59.863 -8.185 1.00 22.26 C ANISOU 2700 C THR A 508 2739 3456 2262 9 5 196 C ATOM 2701 O THR A 508 13.480 60.569 -7.614 1.00 22.96 O ANISOU 2701 O THR A 508 2794 3578 2353 -43 -68 178 O ATOM 2702 CB THR A 508 11.053 58.495 -6.741 1.00 29.81 C ANISOU 2702 CB THR A 508 3769 4442 3116 119 79 162 C ATOM 2703 OG1 THR A 508 9.767 58.551 -6.096 1.00 25.04 O ANISOU 2703 OG1 THR A 508 3218 3801 2494 154 114 112 O ATOM 2704 CG2 THR A 508 12.152 58.456 -5.675 1.00 30.43 C ANISOU 2704 CG2 THR A 508 3817 4617 3127 114 22 167 C ATOM 2705 N ILE A 509 12.905 59.166 -9.284 1.00 20.80 N ANISOU 2705 N ILE A 509 2535 3266 2102 35 59 271 N ATOM 2706 CA ILE A 509 14.204 59.260 -9.950 1.00 19.94 C ANISOU 2706 CA ILE A 509 2356 3188 2030 11 55 348 C ATOM 2707 C ILE A 509 14.486 60.711 -10.363 1.00 23.16 C ANISOU 2707 C ILE A 509 2747 3542 2512 -69 5 325 C ATOM 2708 O ILE A 509 15.571 61.256 -10.093 1.00 20.88 O ANISOU 2708 O ILE A 509 2384 3289 2260 -125 -48 351 O ATOM 2709 CB ILE A 509 14.252 58.369 -11.197 1.00 18.69 C ANISOU 2709 CB ILE A 509 2215 3010 1876 67 137 422 C ATOM 2710 CG1 ILE A 509 14.376 56.895 -10.783 1.00 22.90 C ANISOU 2710 CG1 ILE A 509 2750 3602 2350 142 186 464 C ATOM 2711 CG2 ILE A 509 15.401 58.811 -12.127 1.00 21.01 C ANISOU 2711 CG2 ILE A 509 2449 3309 2224 45 153 502 C ATOM 2712 CD1 ILE A 509 14.036 55.925 -11.915 1.00 23.82 C ANISOU 2712 CD1 ILE A 509 2927 3670 2455 204 262 505 C ATOM 2713 N CYS A 510 13.515 61.341 -11.018 1.00 17.49 N ANISOU 2713 N CYS A 510 2090 2731 1824 -78 18 284 N ATOM 2714 CA CYS A 510 13.699 62.731 -11.461 1.00 19.10 C ANISOU 2714 CA CYS A 510 2287 2867 2103 -148 -20 268 C ATOM 2715 C CYS A 510 13.864 63.701 -10.296 1.00 21.89 C ANISOU 2715 C CYS A 510 2637 3216 2465 -213 -107 188 C ATOM 2716 O CYS A 510 14.692 64.609 -10.357 1.00 24.35 O ANISOU 2716 O CYS A 510 2901 3508 2842 -288 -159 199 O ATOM 2717 CB CYS A 510 12.557 63.189 -12.377 1.00 20.38 C ANISOU 2717 CB CYS A 510 2520 2932 2292 -132 9 245 C ATOM 2718 SG CYS A 510 12.496 62.245 -13.932 1.00 23.07 S ANISOU 2718 SG CYS A 510 2887 3261 2617 -66 87 333 S ATOM 2719 N CYS A 511 13.077 63.522 -9.238 1.00 21.27 N ANISOU 2719 N CYS A 511 2613 3148 2320 -183 -122 110 N ATOM 2720 CA CYS A 511 13.208 64.391 -8.072 1.00 22.74 C ANISOU 2720 CA CYS A 511 2826 3327 2488 -231 -205 23 C ATOM 2721 C CYS A 511 14.567 64.168 -7.393 1.00 24.63 C ANISOU 2721 C CYS A 511 2990 3659 2710 -271 -279 53 C ATOM 2722 O CYS A 511 15.203 65.126 -6.937 1.00 29.86 O ANISOU 2722 O CYS A 511 3638 4301 3406 -352 -374 12 O ATOM 2723 CB CYS A 511 12.039 64.199 -7.094 1.00 24.53 C ANISOU 2723 CB CYS A 511 3139 3548 2635 -170 -184 -58 C ATOM 2724 SG CYS A 511 10.466 64.784 -7.780 1.00 26.43 S ANISOU 2724 SG CYS A 511 3448 3671 2924 -137 -121 -94 S ATOM 2725 N ASP A 512 15.020 62.915 -7.329 1.00 24.89 N ANISOU 2725 N ASP A 512 2973 3787 2698 -217 -242 127 N ATOM 2726 CA ASP A 512 16.317 62.625 -6.712 1.00 28.02 C ANISOU 2726 CA ASP A 512 3282 4282 3084 -245 -313 173 C ATOM 2727 C ASP A 512 17.424 63.305 -7.520 1.00 28.80 C ANISOU 2727 C ASP A 512 3279 4363 3302 -327 -345 244 C ATOM 2728 O ASP A 512 18.364 63.872 -6.962 1.00 29.28 O ANISOU 2728 O ASP A 512 3275 4451 3399 -405 -452 242 O ATOM 2729 CB ASP A 512 16.599 61.119 -6.660 1.00 21.15 C ANISOU 2729 CB ASP A 512 2373 3507 2155 -159 -248 258 C ATOM 2730 CG ASP A 512 15.818 60.397 -5.564 1.00 33.48 C ANISOU 2730 CG ASP A 512 4010 5109 3601 -87 -233 208 C ATOM 2731 OD1 ASP A 512 15.174 61.061 -4.726 1.00 30.31 O ANISOU 2731 OD1 ASP A 512 3688 4676 3151 -98 -277 108 O ATOM 2732 OD2 ASP A 512 15.864 59.150 -5.551 1.00 35.20 O ANISOU 2732 OD2 ASP A 512 4212 5386 3777 -11 -167 275 O ATOM 2733 N ALA A 513 17.320 63.236 -8.841 1.00 26.41 N ANISOU 2733 N ALA A 513 2962 4012 3059 -309 -254 313 N ATOM 2734 CA ALA A 513 18.335 63.843 -9.699 1.00 29.75 C ANISOU 2734 CA ALA A 513 3289 4416 3599 -372 -255 401 C ATOM 2735 C ALA A 513 18.399 65.363 -9.545 1.00 28.85 C ANISOU 2735 C ALA A 513 3182 4212 3568 -482 -344 336 C ATOM 2736 O ALA A 513 19.483 65.923 -9.397 1.00 26.89 O ANISOU 2736 O ALA A 513 2833 3975 3407 -569 -419 378 O ATOM 2737 CB ALA A 513 18.127 63.450 -11.165 1.00 27.05 C ANISOU 2737 CB ALA A 513 2959 4038 3281 -312 -129 485 C ATOM 2738 N VAL A 514 17.252 66.034 -9.559 1.00 27.37 N ANISOU 2738 N VAL A 514 3108 3928 3363 -481 -339 239 N ATOM 2739 CA VAL A 514 17.254 67.500 -9.495 1.00 29.28 C ANISOU 2739 CA VAL A 514 3374 4064 3689 -577 -410 178 C ATOM 2740 C VAL A 514 17.591 68.043 -8.106 1.00 36.36 C ANISOU 2740 C VAL A 514 4287 4968 4558 -647 -550 78 C ATOM 2741 O VAL A 514 18.040 69.181 -7.969 1.00 36.00 O ANISOU 2741 O VAL A 514 4231 4846 4600 -750 -637 43 O ATOM 2742 CB VAL A 514 15.933 68.126 -9.989 1.00 35.89 C ANISOU 2742 CB VAL A 514 4325 4788 4525 -547 -357 114 C ATOM 2743 CG1 VAL A 514 15.690 67.785 -11.459 1.00 31.06 C ANISOU 2743 CG1 VAL A 514 3702 4155 3944 -493 -245 212 C ATOM 2744 CG2 VAL A 514 14.777 67.697 -9.104 1.00 43.66 C ANISOU 2744 CG2 VAL A 514 5412 5784 5393 -474 -350 14 C ATOM 2745 N SER A 515 17.382 67.229 -7.080 1.00 33.04 N ANISOU 2745 N SER A 515 3903 4636 4016 -589 -574 31 N ATOM 2746 CA SER A 515 17.682 67.640 -5.712 1.00 39.63 C ANISOU 2746 CA SER A 515 4777 5488 4792 -637 -711 -68 C ATOM 2747 C SER A 515 19.104 67.245 -5.315 1.00 49.54 C ANISOU 2747 C SER A 515 5899 6851 6075 -691 -807 7 C ATOM 2748 O SER A 515 19.552 67.544 -4.208 1.00 50.47 O ANISOU 2748 O SER A 515 6034 6996 6147 -741 -947 -63 O ATOM 2749 CB SER A 515 16.696 67.001 -4.741 1.00 40.90 C ANISOU 2749 CB SER A 515 5054 5689 4794 -537 -683 -150 C ATOM 2750 OG SER A 515 16.991 65.626 -4.584 1.00 44.06 O ANISOU 2750 OG SER A 515 5396 6217 5128 -462 -638 -69 O ATOM 2751 N GLY A 516 19.802 66.552 -6.208 1.00 47.03 N ANISOU 2751 N GLY A 516 5451 6593 5825 -672 -734 151 N ATOM 2752 CA GLY A 516 21.176 66.155 -5.955 1.00 48.57 C ANISOU 2752 CA GLY A 516 5494 6892 6069 -713 -808 248 C ATOM 2753 C GLY A 516 21.375 64.887 -5.137 1.00 49.89 C ANISOU 2753 C GLY A 516 5645 7196 6113 -626 -815 274 C ATOM 2754 O GLY A 516 22.486 64.604 -4.698 1.00 47.81 O ANISOU 2754 O GLY A 516 5261 7026 5878 -658 -903 343 O ATOM 2755 N ARG A 517 20.315 64.113 -4.928 1.00 39.34 N ANISOU 2755 N ARG A 517 4422 5874 4651 -515 -722 230 N ATOM 2756 CA ARG A 517 20.453 62.841 -4.226 1.00 43.55 C ANISOU 2756 CA ARG A 517 4945 6530 5073 -422 -706 270 C ATOM 2757 C ARG A 517 20.960 61.769 -5.190 1.00 48.08 C ANISOU 2757 C ARG A 517 5415 7160 5694 -353 -583 421 C ATOM 2758 O ARG A 517 21.401 60.700 -4.774 1.00 50.85 O ANISOU 2758 O ARG A 517 5719 7615 5988 -283 -567 490 O ATOM 2759 CB ARG A 517 19.123 62.404 -3.613 1.00 40.41 C ANISOU 2759 CB ARG A 517 4701 6117 4536 -330 -645 178 C ATOM 2760 CG ARG A 517 18.401 63.476 -2.811 1.00 49.54 C ANISOU 2760 CG ARG A 517 5989 7196 5638 -370 -724 26 C ATOM 2761 CD ARG A 517 17.099 62.927 -2.225 1.00 55.49 C ANISOU 2761 CD ARG A 517 6875 7945 6263 -262 -637 -37 C ATOM 2762 NE ARG A 517 16.117 63.975 -1.958 1.00 63.75 N ANISOU 2762 NE ARG A 517 8050 8881 7290 -278 -644 -162 N ATOM 2763 CZ ARG A 517 15.075 64.240 -2.740 1.00 70.69 C ANISOU 2763 CZ ARG A 517 8974 9667 8219 -254 -540 -177 C ATOM 2764 NH1 ARG A 517 14.875 63.534 -3.842 1.00 68.56 N ANISOU 2764 NH1 ARG A 517 8643 9396 8010 -220 -434 -85 N ATOM 2765 NH2 ARG A 517 14.231 65.214 -2.423 1.00 79.31 N ANISOU 2765 NH2 ARG A 517 10178 10661 9295 -260 -546 -284 N ATOM 2766 N ARG A 518 20.894 62.073 -6.482 1.00 39.38 N ANISOU 2766 N ARG A 518 4289 5984 4689 -366 -491 473 N ATOM 2767 CA ARG A 518 21.308 61.150 -7.530 1.00 34.09 C ANISOU 2767 CA ARG A 518 3550 5346 4055 -292 -360 608 C ATOM 2768 C ARG A 518 22.265 61.840 -8.507 1.00 35.11 C ANISOU 2768 C ARG A 518 3560 5447 4333 -360 -347 708 C ATOM 2769 O ARG A 518 21.982 62.933 -8.987 1.00 40.88 O ANISOU 2769 O ARG A 518 4318 6079 5134 -433 -363 666 O ATOM 2770 CB ARG A 518 20.067 60.640 -8.280 1.00 39.71 C ANISOU 2770 CB ARG A 518 4386 5990 4710 -209 -230 577 C ATOM 2771 CG ARG A 518 20.376 59.857 -9.539 1.00 44.13 C ANISOU 2771 CG ARG A 518 4915 6551 5300 -136 -95 695 C ATOM 2772 CD ARG A 518 19.103 59.329 -10.196 1.00 48.04 C ANISOU 2772 CD ARG A 518 5543 6976 5733 -64 1 651 C ATOM 2773 NE ARG A 518 19.433 58.674 -11.456 1.00 48.84 N ANISOU 2773 NE ARG A 518 5638 7065 5852 5 119 752 N ATOM 2774 CZ ARG A 518 19.191 57.400 -11.737 1.00 41.59 C ANISOU 2774 CZ ARG A 518 4772 6162 4869 105 207 786 C ATOM 2775 NH1 ARG A 518 18.579 56.600 -10.856 1.00 32.92 N ANISOU 2775 NH1 ARG A 518 3723 5092 3694 146 195 736 N ATOM 2776 NH2 ARG A 518 19.562 56.931 -12.919 1.00 44.88 N ANISOU 2776 NH2 ARG A 518 5198 6558 5295 169 311 873 N ATOM 2777 N GLN A 519 23.387 61.186 -8.800 1.00 37.48 N ANISOU 2777 N GLN A 519 3724 5831 4686 -327 -308 851 N ATOM 2778 CA GLN A 519 24.431 61.735 -9.671 1.00 37.50 C ANISOU 2778 CA GLN A 519 3586 5821 4840 -380 -280 977 C ATOM 2779 C GLN A 519 23.928 61.861 -11.105 1.00 40.81 C ANISOU 2779 C GLN A 519 4074 6150 5282 -334 -130 1012 C ATOM 2780 O GLN A 519 23.394 60.904 -11.662 1.00 43.96 O ANISOU 2780 O GLN A 519 4560 6550 5595 -220 -10 1028 O ATOM 2781 CB GLN A 519 25.664 60.830 -9.631 1.00 48.39 C ANISOU 2781 CB GLN A 519 4807 7320 6259 -324 -248 1134 C ATOM 2782 CG GLN A 519 26.737 61.190 -10.641 1.00 51.34 C ANISOU 2782 CG GLN A 519 5027 7689 6790 -347 -174 1296 C ATOM 2783 CD GLN A 519 27.319 62.560 -10.380 1.00 53.24 C ANISOU 2783 CD GLN A 519 5162 7889 7178 -511 -313 1289 C ATOM 2784 OE1 GLN A 519 26.992 63.526 -11.073 1.00 52.05 O ANISOU 2784 OE1 GLN A 519 5051 7630 7095 -572 -288 1265 O ATOM 2785 NE2 GLN A 519 28.176 62.658 -9.363 1.00 48.09 N ANISOU 2785 NE2 GLN A 519 4377 7319 6577 -584 -470 1309 N ATOM 2786 N THR A 520 24.095 63.037 -11.703 1.00 36.33 N ANISOU 2786 N THR A 520 3477 5500 4828 -423 -142 1026 N ATOM 2787 CA THR A 520 23.582 63.274 -13.056 1.00 33.28 C ANISOU 2787 CA THR A 520 3168 5023 4452 -380 -11 1057 C ATOM 2788 C THR A 520 24.662 63.212 -14.133 1.00 40.20 C ANISOU 2788 C THR A 520 3924 5917 5432 -350 107 1240 C ATOM 2789 O THR A 520 24.354 63.220 -15.324 1.00 41.07 O ANISOU 2789 O THR A 520 4105 5969 5531 -287 234 1288 O ATOM 2790 CB THR A 520 22.887 64.641 -13.157 1.00 33.44 C ANISOU 2790 CB THR A 520 3261 4923 4520 -476 -74 958 C ATOM 2791 OG1 THR A 520 23.751 65.649 -12.625 1.00 34.19 O ANISOU 2791 OG1 THR A 520 3235 5007 4750 -611 -193 973 O ATOM 2792 CG2 THR A 520 21.586 64.635 -12.368 1.00 38.23 C ANISOU 2792 CG2 THR A 520 4018 5497 5010 -467 -138 788 C ATOM 2793 N LYS A 521 25.923 63.183 -13.713 1.00 43.08 N ANISOU 2793 N LYS A 521 4107 6362 5901 -393 64 1347 N ATOM 2794 CA LYS A 521 27.037 63.066 -14.647 1.00 46.76 C ANISOU 2794 CA LYS A 521 4432 6855 6478 -356 188 1543 C ATOM 2795 C LYS A 521 27.298 61.612 -15.019 1.00 46.16 C ANISOU 2795 C LYS A 521 4367 6860 6313 -193 329 1635 C ATOM 2796 O LYS A 521 27.315 60.733 -14.167 1.00 53.43 O ANISOU 2796 O LYS A 521 5283 7861 7157 -150 282 1603 O ATOM 2797 CB LYS A 521 28.308 63.672 -14.056 1.00 51.74 C ANISOU 2797 CB LYS A 521 4840 7535 7285 -476 79 1636 C ATOM 2798 CG LYS A 521 28.297 65.180 -13.938 1.00 57.47 C ANISOU 2798 CG LYS A 521 5536 8160 8139 -641 -37 1583 C ATOM 2799 CD LYS A 521 29.669 65.673 -13.512 1.00 71.47 C ANISOU 2799 CD LYS A 521 7068 9980 10108 -759 -136 1704 C ATOM 2800 CE LYS A 521 29.625 67.109 -13.039 1.00 81.38 C ANISOU 2800 CE LYS A 521 8308 11132 11480 -943 -304 1613 C ATOM 2801 NZ LYS A 521 30.899 67.484 -12.365 1.00 87.06 N ANISOU 2801 NZ LYS A 521 8798 11904 12379 -1073 -453 1700 N ATOM 2802 N GLU A 522 27.507 61.374 -16.305 1.00 52.75 N ANISOU 2802 N GLU A 522 5225 7666 7151 -95 507 1751 N ATOM 2803 CA GLU A 522 27.764 60.037 -16.820 1.00 51.58 C ANISOU 2803 CA GLU A 522 5111 7572 6916 71 661 1841 C ATOM 2804 C GLU A 522 27.992 60.198 -18.313 1.00 47.32 C ANISOU 2804 C GLU A 522 4610 6976 6395 154 844 1961 C ATOM 2805 O GLU A 522 27.399 61.075 -18.941 1.00 43.83 O ANISOU 2805 O GLU A 522 4255 6440 5958 109 848 1916 O ATOM 2806 CB GLU A 522 26.568 59.112 -16.551 1.00 53.36 C ANISOU 2806 CB GLU A 522 5534 7781 6959 148 652 1694 C ATOM 2807 CG GLU A 522 26.714 57.689 -17.089 1.00 60.32 C ANISOU 2807 CG GLU A 522 6485 8695 7741 320 805 1766 C ATOM 2808 CD GLU A 522 25.543 56.782 -16.705 1.00 70.23 C ANISOU 2808 CD GLU A 522 7918 9926 8841 374 777 1622 C ATOM 2809 OE1 GLU A 522 25.095 56.828 -15.538 1.00 78.34 O ANISOU 2809 OE1 GLU A 522 8937 10981 9847 303 641 1516 O ATOM 2810 OE2 GLU A 522 25.076 56.010 -17.568 1.00 64.52 O ANISOU 2810 OE2 GLU A 522 7345 9153 8016 488 892 1619 O ATOM 2811 N GLY A 523 28.866 59.375 -18.875 1.00 45.37 N ANISOU 2811 N GLY A 523 4301 6784 6154 282 1001 2122 N ATOM 2812 CA GLY A 523 29.162 59.428 -20.298 1.00 55.13 C ANISOU 2812 CA GLY A 523 5585 7973 7388 387 1198 2251 C ATOM 2813 C GLY A 523 29.803 60.717 -20.789 1.00 59.38 C ANISOU 2813 C GLY A 523 5987 8475 8100 293 1220 2366 C ATOM 2814 O GLY A 523 29.627 61.096 -21.952 1.00 61.87 O ANISOU 2814 O GLY A 523 6398 8720 8391 350 1348 2421 O ATOM 2815 N GLY A 524 30.553 61.390 -19.916 1.00 52.78 N ANISOU 2815 N GLY A 524 4931 7683 7438 150 1092 2409 N ATOM 2816 CA GLY A 524 31.258 62.608 -20.292 1.00 48.41 C ANISOU 2816 CA GLY A 524 4221 7090 7082 43 1102 2531 C ATOM 2817 C GLY A 524 30.351 63.823 -20.334 1.00 53.64 C ANISOU 2817 C GLY A 524 4989 7638 7755 -85 995 2394 C ATOM 2818 O GLY A 524 30.700 64.846 -20.933 1.00 53.42 O ANISOU 2818 O GLY A 524 4892 7544 7863 -150 1039 2488 O ATOM 2819 N TYR A 525 29.185 63.722 -19.693 1.00 42.41 N ANISOU 2819 N TYR A 525 3730 6187 6198 -117 863 2181 N ATOM 2820 CA TYR A 525 28.241 64.828 -19.687 1.00 51.80 C ANISOU 2820 CA TYR A 525 5029 7266 7388 -223 766 2045 C ATOM 2821 C TYR A 525 27.391 64.843 -18.411 1.00 44.72 C ANISOU 2821 C TYR A 525 4203 6371 6418 -305 569 1835 C ATOM 2822 O TYR A 525 27.148 63.798 -17.805 1.00 42.10 O ANISOU 2822 O TYR A 525 3915 6112 5970 -239 544 1772 O ATOM 2823 CB TYR A 525 27.345 64.765 -20.932 1.00 63.17 C ANISOU 2823 CB TYR A 525 6679 8627 8696 -109 900 2027 C ATOM 2824 CG TYR A 525 26.664 66.074 -21.269 1.00 73.54 C ANISOU 2824 CG TYR A 525 8066 9820 10057 -202 850 1964 C ATOM 2825 CD1 TYR A 525 27.363 67.106 -21.886 1.00 77.57 C ANISOU 2825 CD1 TYR A 525 8467 10273 10731 -263 912 2105 C ATOM 2826 CD2 TYR A 525 25.320 66.278 -20.971 1.00 78.28 C ANISOU 2826 CD2 TYR A 525 8837 10358 10546 -225 749 1775 C ATOM 2827 CE1 TYR A 525 26.743 68.309 -22.194 1.00 78.57 C ANISOU 2827 CE1 TYR A 525 8666 10281 10904 -343 872 2053 C ATOM 2828 CE2 TYR A 525 24.691 67.475 -21.276 1.00 79.02 C ANISOU 2828 CE2 TYR A 525 8997 10339 10686 -299 710 1723 C ATOM 2829 CZ TYR A 525 25.407 68.487 -21.887 1.00 76.93 C ANISOU 2829 CZ TYR A 525 8634 10016 10579 -357 770 1860 C ATOM 2830 OH TYR A 525 24.784 69.676 -22.192 1.00 69.46 O ANISOU 2830 OH TYR A 525 7759 8951 9683 -426 736 1815 O ATOM 2831 N ASP A 526 26.980 66.042 -17.996 1.00 33.83 N ANISOU 2831 N ASP A 526 2836 4907 5110 -445 440 1736 N ATOM 2832 CA ASP A 526 26.029 66.207 -16.900 1.00 37.65 C ANISOU 2832 CA ASP A 526 3421 5371 5512 -510 276 1532 C ATOM 2833 C ASP A 526 24.632 66.259 -17.515 1.00 36.35 C ANISOU 2833 C ASP A 526 3473 5123 5215 -444 325 1423 C ATOM 2834 O ASP A 526 24.285 67.214 -18.208 1.00 39.36 O ANISOU 2834 O ASP A 526 3904 5402 5647 -478 352 1428 O ATOM 2835 CB ASP A 526 26.325 67.493 -16.120 1.00 43.35 C ANISOU 2835 CB ASP A 526 4057 6035 6380 -690 110 1478 C ATOM 2836 CG ASP A 526 25.449 67.652 -14.886 1.00 45.39 C ANISOU 2836 CG ASP A 526 4422 6279 6545 -746 -55 1272 C ATOM 2837 OD1 ASP A 526 25.860 68.369 -13.950 1.00 51.29 O ANISOU 2837 OD1 ASP A 526 5095 7012 7379 -879 -214 1218 O ATOM 2838 OD2 ASP A 526 24.348 67.065 -14.846 1.00 40.12 O ANISOU 2838 OD2 ASP A 526 3915 5610 5718 -657 -26 1166 O ATOM 2839 N HIS A 527 23.841 65.224 -17.263 1.00 33.33 N ANISOU 2839 N HIS A 527 3210 4781 4673 -350 333 1334 N ATOM 2840 CA HIS A 527 22.530 65.082 -17.878 1.00 29.18 C ANISOU 2840 CA HIS A 527 2875 4189 4025 -278 376 1244 C ATOM 2841 C HIS A 527 21.422 65.747 -17.077 1.00 29.10 C ANISOU 2841 C HIS A 527 2954 4115 3987 -352 248 1072 C ATOM 2842 O HIS A 527 20.251 65.433 -17.277 1.00 29.66 O ANISOU 2842 O HIS A 527 3166 4151 3952 -292 259 983 O ATOM 2843 CB HIS A 527 22.187 63.600 -18.032 1.00 37.87 C ANISOU 2843 CB HIS A 527 4059 5351 4980 -144 448 1237 C ATOM 2844 CG HIS A 527 23.091 62.864 -18.967 1.00 46.13 C ANISOU 2844 CG HIS A 527 5063 6441 6021 -38 600 1397 C ATOM 2845 ND1 HIS A 527 24.389 62.535 -18.641 1.00 53.02 N ANISOU 2845 ND1 HIS A 527 5766 7401 6977 -38 627 1521 N ATOM 2846 CD2 HIS A 527 22.882 62.388 -20.217 1.00 51.24 C ANISOU 2846 CD2 HIS A 527 5823 7057 6587 81 735 1456 C ATOM 2847 CE1 HIS A 527 24.943 61.891 -19.653 1.00 50.46 C ANISOU 2847 CE1 HIS A 527 5450 7096 6627 83 789 1655 C ATOM 2848 NE2 HIS A 527 24.051 61.789 -20.621 1.00 60.81 N ANISOU 2848 NE2 HIS A 527 6942 8334 7830 158 856 1613 N ATOM 2849 N ALA A 528 21.778 66.654 -16.174 1.00 29.49 N ANISOU 2849 N ALA A 528 2924 4146 4133 -477 127 1025 N ATOM 2850 CA ALA A 528 20.769 67.297 -15.326 1.00 35.53 C ANISOU 2850 CA ALA A 528 3784 4849 4866 -536 13 859 C ATOM 2851 C ALA A 528 19.614 67.852 -16.161 1.00 30.71 C ANISOU 2851 C ALA A 528 3309 4132 4226 -503 61 814 C ATOM 2852 O ALA A 528 18.455 67.755 -15.780 1.00 25.48 O ANISOU 2852 O ALA A 528 2759 3443 3479 -474 29 695 O ATOM 2853 CB ALA A 528 21.397 68.402 -14.486 1.00 33.25 C ANISOU 2853 CB ALA A 528 3410 4525 4698 -680 -118 825 C ATOM 2854 N ILE A 529 19.954 68.431 -17.304 1.00 28.33 N ANISOU 2854 N ILE A 529 2992 3773 3999 -502 143 920 N ATOM 2855 CA ILE A 529 18.974 69.005 -18.211 1.00 27.53 C ANISOU 2855 CA ILE A 529 3011 3573 3876 -465 189 902 C ATOM 2856 C ILE A 529 17.914 67.987 -18.651 1.00 24.12 C ANISOU 2856 C ILE A 529 2706 3165 3294 -344 237 857 C ATOM 2857 O ILE A 529 16.734 68.330 -18.799 1.00 26.45 O ANISOU 2857 O ILE A 529 3107 3393 3548 -326 213 776 O ATOM 2858 CB ILE A 529 19.687 69.619 -19.448 1.00 36.87 C ANISOU 2858 CB ILE A 529 4150 4709 5152 -464 291 1056 C ATOM 2859 CG1 ILE A 529 18.697 70.287 -20.389 1.00 39.81 C ANISOU 2859 CG1 ILE A 529 4650 4979 5499 -424 330 1044 C ATOM 2860 CG2 ILE A 529 20.467 68.563 -20.210 1.00 35.27 C ANISOU 2860 CG2 ILE A 529 3906 4591 4903 -365 414 1192 C ATOM 2861 CD1 ILE A 529 19.396 70.965 -21.569 1.00 40.58 C ANISOU 2861 CD1 ILE A 529 4711 5023 5684 -419 437 1204 C ATOM 2862 N SER A 530 18.315 66.733 -18.831 1.00 25.89 N ANISOU 2862 N SER A 530 2916 3479 3443 -264 297 911 N ATOM 2863 CA SER A 530 17.358 65.695 -19.209 1.00 24.27 C ANISOU 2863 CA SER A 530 2831 3288 3104 -160 330 865 C ATOM 2864 C SER A 530 16.385 65.401 -18.076 1.00 26.39 C ANISOU 2864 C SER A 530 3141 3566 3322 -177 239 725 C ATOM 2865 O SER A 530 15.181 65.294 -18.300 1.00 23.45 O ANISOU 2865 O SER A 530 2869 3148 2893 -139 226 656 O ATOM 2866 CB SER A 530 18.078 64.416 -19.652 1.00 24.71 C ANISOU 2866 CB SER A 530 2871 3422 3095 -67 422 956 C ATOM 2867 OG SER A 530 18.827 64.682 -20.825 1.00 27.03 O ANISOU 2867 OG SER A 530 3151 3698 3419 -28 529 1091 O ATOM 2868 N PHE A 531 16.904 65.269 -16.862 1.00 24.20 N ANISOU 2868 N PHE A 531 2781 3348 3065 -229 177 690 N ATOM 2869 CA PHE A 531 16.050 65.019 -15.704 1.00 24.48 C ANISOU 2869 CA PHE A 531 2858 3397 3047 -237 104 567 C ATOM 2870 C PHE A 531 15.073 66.168 -15.437 1.00 20.31 C ANISOU 2870 C PHE A 531 2392 2775 2551 -285 46 470 C ATOM 2871 O PHE A 531 13.925 65.951 -15.042 1.00 23.38 O ANISOU 2871 O PHE A 531 2853 3145 2886 -252 28 385 O ATOM 2872 CB PHE A 531 16.895 64.750 -14.458 1.00 21.20 C ANISOU 2872 CB PHE A 531 2350 3066 2637 -280 42 555 C ATOM 2873 CG PHE A 531 17.601 63.422 -14.485 1.00 23.64 C ANISOU 2873 CG PHE A 531 2610 3474 2896 -211 97 635 C ATOM 2874 CD1 PHE A 531 16.946 62.267 -14.100 1.00 24.79 C ANISOU 2874 CD1 PHE A 531 2816 3659 2944 -138 116 594 C ATOM 2875 CD2 PHE A 531 18.920 63.334 -14.899 1.00 26.21 C ANISOU 2875 CD2 PHE A 531 2827 3847 3284 -217 138 759 C ATOM 2876 CE1 PHE A 531 17.584 61.041 -14.127 1.00 23.91 C ANISOU 2876 CE1 PHE A 531 2669 3627 2790 -68 173 668 C ATOM 2877 CE2 PHE A 531 19.582 62.108 -14.922 1.00 30.46 C ANISOU 2877 CE2 PHE A 531 3321 4473 3779 -140 200 839 C ATOM 2878 CZ PHE A 531 18.915 60.961 -14.531 1.00 32.40 C ANISOU 2878 CZ PHE A 531 3640 4752 3920 -65 216 790 C ATOM 2879 N GLN A 532 15.537 67.390 -15.631 1.00 24.18 N ANISOU 2879 N GLN A 532 2847 3200 3138 -361 22 490 N ATOM 2880 CA GLN A 532 14.667 68.550 -15.472 1.00 21.17 C ANISOU 2880 CA GLN A 532 2532 2715 2797 -399 -21 407 C ATOM 2881 C GLN A 532 13.523 68.528 -16.492 1.00 20.30 C ANISOU 2881 C GLN A 532 2513 2546 2652 -326 30 412 C ATOM 2882 O GLN A 532 12.381 68.898 -16.188 1.00 21.91 O ANISOU 2882 O GLN A 532 2785 2696 2844 -311 4 330 O ATOM 2883 CB GLN A 532 15.493 69.829 -15.601 1.00 26.35 C ANISOU 2883 CB GLN A 532 3133 3302 3578 -497 -50 443 C ATOM 2884 CG GLN A 532 16.472 69.998 -14.443 1.00 39.40 C ANISOU 2884 CG GLN A 532 4701 4998 5272 -587 -140 414 C ATOM 2885 CD GLN A 532 17.452 71.134 -14.659 1.00 58.15 C ANISOU 2885 CD GLN A 532 6997 7305 7792 -696 -172 471 C ATOM 2886 OE1 GLN A 532 18.314 71.398 -13.814 1.00 64.12 O ANISOU 2886 OE1 GLN A 532 7676 8083 8604 -786 -264 455 O ATOM 2887 NE2 GLN A 532 17.334 71.806 -15.798 1.00 61.10 N ANISOU 2887 NE2 GLN A 532 7388 7594 8233 -691 -103 545 N ATOM 2888 N ASP A 533 13.837 68.081 -17.695 1.00 21.36 N ANISOU 2888 N ASP A 533 2653 2694 2769 -274 103 513 N ATOM 2889 CA ASP A 533 12.852 67.989 -18.778 1.00 21.01 C ANISOU 2889 CA ASP A 533 2701 2601 2680 -202 137 528 C ATOM 2890 C ASP A 533 11.789 66.941 -18.406 1.00 23.76 C ANISOU 2890 C ASP A 533 3102 2984 2941 -143 117 456 C ATOM 2891 O ASP A 533 10.584 67.210 -18.436 1.00 21.67 O ANISOU 2891 O ASP A 533 2894 2667 2673 -123 89 400 O ATOM 2892 CB ASP A 533 13.590 67.591 -20.063 1.00 25.87 C ANISOU 2892 CB ASP A 533 3322 3236 3271 -149 222 652 C ATOM 2893 CG ASP A 533 12.713 67.644 -21.304 1.00 40.93 C ANISOU 2893 CG ASP A 533 5337 5088 5127 -77 246 676 C ATOM 2894 OD1 ASP A 533 13.242 67.427 -22.411 1.00 53.23 O ANISOU 2894 OD1 ASP A 533 6926 6650 6649 -23 320 775 O ATOM 2895 OD2 ASP A 533 11.504 67.897 -21.183 1.00 43.76 O ANISOU 2895 OD2 ASP A 533 5751 5400 5477 -69 193 602 O ATOM 2896 N TRP A 534 12.231 65.751 -18.016 1.00 17.12 N ANISOU 2896 N TRP A 534 2234 2228 2042 -116 134 464 N ATOM 2897 CA TRP A 534 11.274 64.714 -17.636 1.00 15.78 C ANISOU 2897 CA TRP A 534 2106 2083 1805 -66 120 406 C ATOM 2898 C TRP A 534 10.443 65.118 -16.425 1.00 16.42 C ANISOU 2898 C TRP A 534 2183 2149 1906 -96 67 308 C ATOM 2899 O TRP A 534 9.246 64.810 -16.345 1.00 19.47 O ANISOU 2899 O TRP A 534 2611 2511 2275 -62 55 263 O ATOM 2900 CB TRP A 534 11.983 63.376 -17.373 1.00 17.99 C ANISOU 2900 CB TRP A 534 2359 2451 2025 -30 155 440 C ATOM 2901 CG TRP A 534 12.847 62.938 -18.521 1.00 19.95 C ANISOU 2901 CG TRP A 534 2619 2714 2247 16 225 540 C ATOM 2902 CD1 TRP A 534 12.579 63.076 -19.864 1.00 19.08 C ANISOU 2902 CD1 TRP A 534 2587 2551 2111 62 258 585 C ATOM 2903 CD2 TRP A 534 14.109 62.266 -18.429 1.00 17.44 C ANISOU 2903 CD2 TRP A 534 2239 2471 1918 35 278 615 C ATOM 2904 NE1 TRP A 534 13.620 62.543 -20.606 1.00 23.41 N ANISOU 2904 NE1 TRP A 534 3135 3133 2625 112 339 682 N ATOM 2905 CE2 TRP A 534 14.567 62.045 -19.745 1.00 21.17 C ANISOU 2905 CE2 TRP A 534 2758 2928 2358 97 357 705 C ATOM 2906 CE3 TRP A 534 14.905 61.849 -17.354 1.00 22.44 C ANISOU 2906 CE3 TRP A 534 2781 3183 2560 13 267 621 C ATOM 2907 CZ2 TRP A 534 15.788 61.422 -20.017 1.00 24.16 C ANISOU 2907 CZ2 TRP A 534 3090 3366 2725 142 438 805 C ATOM 2908 CZ3 TRP A 534 16.115 61.232 -17.622 1.00 23.41 C ANISOU 2908 CZ3 TRP A 534 2847 3370 2680 50 334 722 C ATOM 2909 CH2 TRP A 534 16.544 61.021 -18.945 1.00 24.72 C ANISOU 2909 CH2 TRP A 534 3055 3515 2823 116 426 814 C ATOM 2910 N LEU A 535 11.078 65.784 -15.470 1.00 16.28 N ANISOU 2910 N LEU A 535 2117 2143 1924 -157 36 276 N ATOM 2911 CA LEU A 535 10.367 66.231 -14.277 1.00 17.96 C ANISOU 2911 CA LEU A 535 2346 2338 2140 -174 -6 180 C ATOM 2912 C LEU A 535 9.258 67.207 -14.647 1.00 19.58 C ANISOU 2912 C LEU A 535 2604 2443 2391 -168 -13 144 C ATOM 2913 O LEU A 535 8.132 67.110 -14.147 1.00 21.13 O ANISOU 2913 O LEU A 535 2831 2621 2575 -132 -14 90 O ATOM 2914 CB LEU A 535 11.342 66.896 -13.304 1.00 19.04 C ANISOU 2914 CB LEU A 535 2440 2492 2303 -247 -55 148 C ATOM 2915 CG LEU A 535 10.722 67.448 -12.024 1.00 25.04 C ANISOU 2915 CG LEU A 535 3241 3227 3046 -259 -98 40 C ATOM 2916 CD1 LEU A 535 9.947 66.379 -11.293 1.00 28.28 C ANISOU 2916 CD1 LEU A 535 3672 3696 3377 -191 -73 8 C ATOM 2917 CD2 LEU A 535 11.830 68.027 -11.148 1.00 29.16 C ANISOU 2917 CD2 LEU A 535 3728 3766 3583 -337 -168 10 C ATOM 2918 N LYS A 536 9.579 68.156 -15.517 1.00 19.13 N ANISOU 2918 N LYS A 536 2553 2321 2395 -197 -10 187 N ATOM 2919 CA LYS A 536 8.582 69.139 -15.949 1.00 19.09 C ANISOU 2919 CA LYS A 536 2597 2217 2438 -184 -14 167 C ATOM 2920 C LYS A 536 7.393 68.482 -16.628 1.00 19.95 C ANISOU 2920 C LYS A 536 2742 2322 2517 -111 -3 182 C ATOM 2921 O LYS A 536 6.255 68.932 -16.478 1.00 18.53 O ANISOU 2921 O LYS A 536 2587 2088 2366 -84 -13 145 O ATOM 2922 CB LYS A 536 9.195 70.185 -16.886 1.00 28.17 C ANISOU 2922 CB LYS A 536 3748 3298 3657 -221 -4 231 C ATOM 2923 CG LYS A 536 10.150 71.153 -16.197 1.00 48.14 C ANISOU 2923 CG LYS A 536 6245 5793 6255 -310 -34 208 C ATOM 2924 CD LYS A 536 10.506 72.316 -17.117 1.00 59.94 C ANISOU 2924 CD LYS A 536 7744 7192 7838 -345 -16 273 C ATOM 2925 CE LYS A 536 11.834 72.949 -16.722 1.00 70.27 C ANISOU 2925 CE LYS A 536 8989 8487 9226 -447 -43 292 C ATOM 2926 NZ LYS A 536 11.858 73.336 -15.285 1.00 73.22 N ANISOU 2926 NZ LYS A 536 9370 8845 9605 -503 -116 174 N ATOM 2927 N LYS A 537 7.641 67.421 -17.387 1.00 18.13 N ANISOU 2927 N LYS A 537 2514 2144 2233 -78 15 238 N ATOM 2928 CA LYS A 537 6.532 66.728 -18.038 1.00 18.67 C ANISOU 2928 CA LYS A 537 2619 2203 2273 -20 4 246 C ATOM 2929 C LYS A 537 5.649 66.050 -17.003 1.00 21.46 C ANISOU 2929 C LYS A 537 2952 2583 2618 -2 -6 186 C ATOM 2930 O LYS A 537 4.426 66.119 -17.068 1.00 19.29 O ANISOU 2930 O LYS A 537 2685 2270 2375 27 -25 170 O ATOM 2931 CB LYS A 537 7.048 65.677 -19.014 1.00 19.96 C ANISOU 2931 CB LYS A 537 2810 2406 2367 13 23 307 C ATOM 2932 CG LYS A 537 7.754 66.226 -20.260 1.00 23.03 C ANISOU 2932 CG LYS A 537 3234 2767 2750 22 50 386 C ATOM 2933 CD LYS A 537 8.150 65.002 -21.118 1.00 25.31 C ANISOU 2933 CD LYS A 537 3572 3096 2949 75 77 434 C ATOM 2934 CE LYS A 537 8.924 65.373 -22.350 1.00 29.21 C ANISOU 2934 CE LYS A 537 4111 3573 3416 103 125 523 C ATOM 2935 NZ LYS A 537 8.028 65.836 -23.425 1.00 31.57 N ANISOU 2935 NZ LYS A 537 4492 3808 3697 143 89 540 N ATOM 2936 N LEU A 538 6.279 65.373 -16.050 1.00 17.52 N ANISOU 2936 N LEU A 538 2422 2153 2082 -15 11 164 N ATOM 2937 CA LEU A 538 5.527 64.726 -14.986 1.00 20.11 C ANISOU 2937 CA LEU A 538 2733 2510 2398 7 17 119 C ATOM 2938 C LEU A 538 4.784 65.760 -14.132 1.00 22.70 C ANISOU 2938 C LEU A 538 3064 2790 2771 7 16 60 C ATOM 2939 O LEU A 538 3.632 65.559 -13.763 1.00 21.17 O ANISOU 2939 O LEU A 538 2864 2580 2601 45 27 43 O ATOM 2940 CB LEU A 538 6.455 63.870 -14.122 1.00 15.68 C ANISOU 2940 CB LEU A 538 2144 2034 1778 0 36 115 C ATOM 2941 CG LEU A 538 7.056 62.661 -14.848 1.00 20.76 C ANISOU 2941 CG LEU A 538 2791 2723 2375 20 53 174 C ATOM 2942 CD1 LEU A 538 8.173 62.016 -14.004 1.00 22.02 C ANISOU 2942 CD1 LEU A 538 2913 2968 2487 14 73 184 C ATOM 2943 CD2 LEU A 538 5.976 61.648 -15.192 1.00 20.22 C ANISOU 2943 CD2 LEU A 538 2744 2637 2302 60 52 179 C ATOM 2944 N HIS A 539 5.436 66.877 -13.843 1.00 19.18 N ANISOU 2944 N HIS A 539 2628 2314 2345 -34 6 33 N ATOM 2945 CA HIS A 539 4.814 67.896 -12.993 1.00 20.84 C ANISOU 2945 CA HIS A 539 2864 2467 2588 -28 9 -32 C ATOM 2946 C HIS A 539 3.593 68.488 -13.699 1.00 24.64 C ANISOU 2946 C HIS A 539 3358 2867 3135 11 14 -15 C ATOM 2947 O HIS A 539 2.547 68.736 -13.093 1.00 23.03 O ANISOU 2947 O HIS A 539 3159 2633 2958 56 39 -46 O ATOM 2948 CB HIS A 539 5.810 69.007 -12.695 1.00 25.19 C ANISOU 2948 CB HIS A 539 3433 2981 3156 -91 -18 -65 C ATOM 2949 CG HIS A 539 5.220 70.160 -11.944 1.00 34.66 C ANISOU 2949 CG HIS A 539 4685 4099 4387 -83 -16 -139 C ATOM 2950 ND1 HIS A 539 4.671 71.257 -12.575 1.00 41.14 N ANISOU 2950 ND1 HIS A 539 5534 4816 5282 -76 -11 -131 N ATOM 2951 CD2 HIS A 539 5.101 70.391 -10.615 1.00 39.90 C ANISOU 2951 CD2 HIS A 539 5388 4763 5007 -71 -13 -220 C ATOM 2952 CE1 HIS A 539 4.236 72.113 -11.665 1.00 44.97 C ANISOU 2952 CE1 HIS A 539 6075 5236 5776 -59 -1 -208 C ATOM 2953 NE2 HIS A 539 4.486 71.611 -10.468 1.00 43.85 N ANISOU 2953 NE2 HIS A 539 5947 5157 5558 -55 -2 -266 N ATOM 2954 N SER A 540 3.733 68.714 -14.994 1.00 20.86 N ANISOU 2954 N SER A 540 2885 2358 2684 2 -5 44 N ATOM 2955 CA SER A 540 2.637 69.262 -15.774 1.00 25.20 C ANISOU 2955 CA SER A 540 3444 2837 3292 41 -15 72 C ATOM 2956 C SER A 540 1.437 68.302 -15.835 1.00 22.38 C ANISOU 2956 C SER A 540 3056 2505 2944 91 -21 89 C ATOM 2957 O SER A 540 0.290 68.736 -15.733 1.00 23.27 O ANISOU 2957 O SER A 540 3152 2571 3119 132 -16 90 O ATOM 2958 CB SER A 540 3.120 69.619 -17.178 1.00 29.27 C ANISOU 2958 CB SER A 540 3984 3322 3814 28 -36 139 C ATOM 2959 OG SER A 540 2.020 69.938 -17.998 1.00 39.79 O ANISOU 2959 OG SER A 540 5326 4603 5190 74 -60 176 O ATOM 2960 N ARG A 541 1.698 67.010 -16.008 1.00 19.15 N ANISOU 2960 N ARG A 541 2632 2163 2483 87 -31 108 N ATOM 2961 CA ARG A 541 0.618 66.009 -16.016 1.00 20.32 C ANISOU 2961 CA ARG A 541 2743 2326 2651 119 -43 125 C ATOM 2962 C ARG A 541 -0.047 65.954 -14.655 1.00 16.76 C ANISOU 2962 C ARG A 541 2255 1887 2227 145 8 89 C ATOM 2963 O ARG A 541 -1.273 65.950 -14.552 1.00 19.27 O ANISOU 2963 O ARG A 541 2530 2176 2615 182 13 106 O ATOM 2964 CB ARG A 541 1.131 64.602 -16.373 1.00 15.72 C ANISOU 2964 CB ARG A 541 2167 1800 2004 107 -58 146 C ATOM 2965 CG ARG A 541 -0.007 63.544 -16.486 1.00 14.50 C ANISOU 2965 CG ARG A 541 1977 1643 1888 127 -86 166 C ATOM 2966 CD ARG A 541 -1.075 63.945 -17.556 1.00 21.34 C ANISOU 2966 CD ARG A 541 2840 2449 2819 142 -157 200 C ATOM 2967 NE ARG A 541 -0.429 63.987 -18.867 1.00 23.45 N ANISOU 2967 NE ARG A 541 3181 2705 3024 135 -205 224 N ATOM 2968 CZ ARG A 541 -0.444 62.984 -19.743 1.00 27.98 C ANISOU 2968 CZ ARG A 541 3798 3281 3553 135 -261 242 C ATOM 2969 NH1 ARG A 541 -1.130 61.876 -19.483 1.00 24.85 N ANISOU 2969 NH1 ARG A 541 3368 2888 3185 129 -288 238 N ATOM 2970 NH2 ARG A 541 0.212 63.092 -20.889 1.00 23.61 N ANISOU 2970 NH2 ARG A 541 3329 2718 2925 145 -286 265 N ATOM 2971 N VAL A 542 0.762 65.904 -13.597 1.00 17.75 N ANISOU 2971 N VAL A 542 2393 2055 2294 131 47 45 N ATOM 2972 CA VAL A 542 0.199 65.739 -12.261 1.00 18.13 C ANISOU 2972 CA VAL A 542 2424 2123 2341 169 105 13 C ATOM 2973 C VAL A 542 -0.641 66.957 -11.895 1.00 19.76 C ANISOU 2973 C VAL A 542 2641 2258 2607 209 136 -10 C ATOM 2974 O VAL A 542 -1.701 66.823 -11.283 1.00 20.54 O ANISOU 2974 O VAL A 542 2706 2348 2749 265 187 -1 O ATOM 2975 CB VAL A 542 1.284 65.488 -11.205 1.00 20.38 C ANISOU 2975 CB VAL A 542 2737 2472 2536 151 127 -31 C ATOM 2976 CG1 VAL A 542 0.724 65.708 -9.813 1.00 25.57 C ANISOU 2976 CG1 VAL A 542 3408 3133 3175 202 190 -73 C ATOM 2977 CG2 VAL A 542 1.847 64.059 -11.363 1.00 21.67 C ANISOU 2977 CG2 VAL A 542 2876 2708 2649 137 120 5 C ATOM 2978 N THR A 543 -0.176 68.136 -12.303 1.00 16.73 N ANISOU 2978 N THR A 543 2303 1817 2236 186 112 -32 N ATOM 2979 CA THR A 543 -0.915 69.377 -12.099 1.00 23.78 C ANISOU 2979 CA THR A 543 3220 2626 3191 227 141 -53 C ATOM 2980 C THR A 543 -2.263 69.341 -12.806 1.00 23.34 C ANISOU 2980 C THR A 543 3104 2534 3230 277 138 13 C ATOM 2981 O THR A 543 -3.311 69.614 -12.203 1.00 22.65 O ANISOU 2981 O THR A 543 2991 2418 3197 343 196 18 O ATOM 2982 CB THR A 543 -0.112 70.593 -12.638 1.00 25.52 C ANISOU 2982 CB THR A 543 3497 2778 3421 182 107 -73 C ATOM 2983 OG1 THR A 543 1.079 70.747 -11.863 1.00 28.19 O ANISOU 2983 OG1 THR A 543 3880 3142 3691 130 99 -135 O ATOM 2984 CG2 THR A 543 -0.926 71.880 -12.552 1.00 29.11 C ANISOU 2984 CG2 THR A 543 3983 3130 3949 231 139 -86 C ATOM 2985 N LYS A 544 -2.239 68.997 -14.086 1.00 20.37 N ANISOU 2985 N LYS A 544 2707 2160 2873 249 70 68 N ATOM 2986 CA LYS A 544 -3.470 68.939 -14.879 1.00 22.29 C ANISOU 2986 CA LYS A 544 2891 2372 3205 287 36 134 C ATOM 2987 C LYS A 544 -4.478 67.924 -14.348 1.00 20.58 C ANISOU 2987 C LYS A 544 2592 2193 3036 318 59 163 C ATOM 2988 O LYS A 544 -5.684 68.174 -14.372 1.00 23.52 O ANISOU 2988 O LYS A 544 2898 2531 3508 368 70 208 O ATOM 2989 CB LYS A 544 -3.157 68.601 -16.337 1.00 22.80 C ANISOU 2989 CB LYS A 544 2971 2442 3251 252 -54 180 C ATOM 2990 CG LYS A 544 -2.553 69.766 -17.151 1.00 23.72 C ANISOU 2990 CG LYS A 544 3150 2501 3360 240 -74 189 C ATOM 2991 CD LYS A 544 -2.169 69.207 -18.514 1.00 26.49 C ANISOU 2991 CD LYS A 544 3530 2871 3663 217 -149 237 C ATOM 2992 CE LYS A 544 -1.371 70.154 -19.356 1.00 38.86 C ANISOU 2992 CE LYS A 544 5162 4396 5206 204 -154 261 C ATOM 2993 NZ LYS A 544 -1.005 69.475 -20.627 1.00 32.22 N ANISOU 2993 NZ LYS A 544 4363 3582 4297 198 -213 308 N ATOM 2994 N GLU A 545 -3.981 66.779 -13.890 1.00 18.32 N ANISOU 2994 N GLU A 545 2300 1973 2688 289 69 149 N ATOM 2995 CA GLU A 545 -4.843 65.679 -13.461 1.00 17.77 C ANISOU 2995 CA GLU A 545 2150 1934 2669 307 90 188 C ATOM 2996 C GLU A 545 -4.948 65.562 -11.938 1.00 17.85 C ANISOU 2996 C GLU A 545 2154 1973 2656 351 202 161 C ATOM 2997 O GLU A 545 -5.304 64.508 -11.395 1.00 17.89 O ANISOU 2997 O GLU A 545 2107 2016 2674 359 238 190 O ATOM 2998 CB GLU A 545 -4.335 64.371 -14.083 1.00 17.46 C ANISOU 2998 CB GLU A 545 2115 1937 2584 253 26 202 C ATOM 2999 CG GLU A 545 -4.914 64.188 -15.496 1.00 22.85 C ANISOU 2999 CG GLU A 545 2778 2583 3321 234 -85 249 C ATOM 3000 CD GLU A 545 -6.430 63.977 -15.458 1.00 29.28 C ANISOU 3000 CD GLU A 545 3482 3369 4275 260 -101 309 C ATOM 3001 OE1 GLU A 545 -7.209 64.962 -15.352 1.00 30.25 O ANISOU 3001 OE1 GLU A 545 3562 3453 4478 307 -77 333 O ATOM 3002 OE2 GLU A 545 -6.859 62.809 -15.516 1.00 30.04 O ANISOU 3002 OE2 GLU A 545 3527 3476 4410 234 -134 338 O ATOM 3003 N ARG A 546 -4.656 66.655 -11.254 1.00 20.02 N ANISOU 3003 N ARG A 546 3130 2234 2243 345 -220 -117 N ATOM 3004 CA ARG A 546 -4.596 66.639 -9.797 1.00 21.11 C ANISOU 3004 CA ARG A 546 3246 2506 2268 338 -168 -166 C ATOM 3005 C ARG A 546 -5.877 66.120 -9.142 1.00 21.20 C ANISOU 3005 C ARG A 546 3174 2585 2298 437 -104 -147 C ATOM 3006 O ARG A 546 -5.821 65.387 -8.153 1.00 21.35 O ANISOU 3006 O ARG A 546 3120 2748 2243 431 -68 -121 O ATOM 3007 CB ARG A 546 -4.281 68.042 -9.276 1.00 26.54 C ANISOU 3007 CB ARG A 546 4051 3141 2891 310 -154 -302 C ATOM 3008 CG ARG A 546 -3.884 68.076 -7.818 1.00 46.07 C ANISOU 3008 CG ARG A 546 6519 5757 5230 269 -112 -356 C ATOM 3009 CD ARG A 546 -4.014 69.481 -7.252 1.00 59.77 C ANISOU 3009 CD ARG A 546 8365 7429 6916 270 -75 -497 C ATOM 3010 NE ARG A 546 -3.408 69.612 -5.928 1.00 70.37 N ANISOU 3010 NE ARG A 546 9720 8903 8117 204 -44 -556 N ATOM 3011 CZ ARG A 546 -2.186 70.092 -5.712 1.00 75.73 C ANISOU 3011 CZ ARG A 546 10464 9605 8705 94 -76 -603 C ATOM 3012 NH1 ARG A 546 -1.437 70.484 -6.735 1.00 76.34 N ANISOU 3012 NH1 ARG A 546 10604 9580 8824 40 -138 -599 N ATOM 3013 NH2 ARG A 546 -1.711 70.183 -4.476 1.00 78.72 N ANISOU 3013 NH2 ARG A 546 10847 10111 8950 33 -46 -654 N ATOM 3014 N HIS A 547 -7.032 66.497 -9.686 1.00 21.36 N ANISOU 3014 N HIS A 547 3200 2500 2414 529 -89 -158 N ATOM 3015 CA HIS A 547 -8.303 66.080 -9.088 1.00 21.74 C ANISOU 3015 CA HIS A 547 3171 2604 2485 628 -27 -143 C ATOM 3016 C HIS A 547 -8.530 64.586 -9.136 1.00 21.20 C ANISOU 3016 C HIS A 547 2978 2640 2437 640 -23 -23 C ATOM 3017 O HIS A 547 -8.819 63.957 -8.109 1.00 21.50 O ANISOU 3017 O HIS A 547 2945 2807 2418 662 26 -9 O ATOM 3018 CB HIS A 547 -9.483 66.863 -9.680 1.00 23.00 C ANISOU 3018 CB HIS A 547 3364 2628 2746 724 -11 -177 C ATOM 3019 CG HIS A 547 -9.526 68.282 -9.201 1.00 26.86 C ANISOU 3019 CG HIS A 547 3962 3044 3199 735 21 -304 C ATOM 3020 ND1 HIS A 547 -9.172 69.351 -9.998 1.00 34.03 N ANISOU 3020 ND1 HIS A 547 4977 3809 4146 713 -14 -359 N ATOM 3021 CD2 HIS A 547 -9.812 68.800 -7.981 1.00 30.58 C ANISOU 3021 CD2 HIS A 547 4458 3566 3594 758 88 -390 C ATOM 3022 CE1 HIS A 547 -9.277 70.471 -9.301 1.00 34.42 C ANISOU 3022 CE1 HIS A 547 5110 3820 4146 725 34 -473 C ATOM 3023 NE2 HIS A 547 -9.663 70.164 -8.075 1.00 38.25 N ANISOU 3023 NE2 HIS A 547 5550 4422 4563 751 97 -495 N ATOM 3024 N ARG A 548 -8.377 63.994 -10.310 1.00 20.10 N ANISOU 3024 N ARG A 548 2812 2447 2376 621 -72 65 N ATOM 3025 CA ARG A 548 -8.478 62.542 -10.376 1.00 20.07 C ANISOU 3025 CA ARG A 548 2696 2542 2388 621 -65 181 C ATOM 3026 C ARG A 548 -7.389 61.829 -9.560 1.00 22.86 C ANISOU 3026 C ARG A 548 3012 3037 2635 543 -58 212 C ATOM 3027 O ARG A 548 -7.658 60.838 -8.882 1.00 19.23 O ANISOU 3027 O ARG A 548 2459 2702 2145 563 -16 268 O ATOM 3028 CB ARG A 548 -8.480 62.071 -11.828 1.00 19.39 C ANISOU 3028 CB ARG A 548 2599 2364 2403 606 -116 266 C ATOM 3029 CG ARG A 548 -9.914 61.980 -12.409 1.00 21.50 C ANISOU 3029 CG ARG A 548 2824 2568 2775 703 -101 295 C ATOM 3030 CD ARG A 548 -9.890 61.543 -13.882 1.00 25.18 C ANISOU 3030 CD ARG A 548 3286 2944 3338 678 -154 377 C ATOM 3031 NE ARG A 548 -9.628 62.692 -14.746 1.00 23.51 N ANISOU 3031 NE ARG A 548 3178 2585 3169 662 -205 322 N ATOM 3032 CZ ARG A 548 -10.565 63.495 -15.246 1.00 27.15 C ANISOU 3032 CZ ARG A 548 3672 2941 3704 732 -208 287 C ATOM 3033 NH1 ARG A 548 -11.876 63.283 -15.006 1.00 21.56 N ANISOU 3033 NH1 ARG A 548 2897 2256 3039 825 -165 304 N ATOM 3034 NH2 ARG A 548 -10.185 64.524 -15.997 1.00 21.19 N ANISOU 3034 NH2 ARG A 548 3015 2056 2981 710 -252 238 N ATOM 3035 N LEU A 549 -6.158 62.320 -9.633 1.00 19.44 N ANISOU 3035 N LEU A 549 2649 2589 2147 453 -99 179 N ATOM 3036 CA LEU A 549 -5.061 61.648 -8.942 1.00 18.59 C ANISOU 3036 CA LEU A 549 2505 2617 1943 374 -98 220 C ATOM 3037 C LEU A 549 -5.269 61.660 -7.427 1.00 19.53 C ANISOU 3037 C LEU A 549 2592 2871 1958 393 -39 170 C ATOM 3038 O LEU A 549 -4.866 60.733 -6.729 1.00 19.37 O ANISOU 3038 O LEU A 549 2493 2992 1873 366 -17 231 O ATOM 3039 CB LEU A 549 -3.722 62.309 -9.299 1.00 19.18 C ANISOU 3039 CB LEU A 549 2667 2644 1976 273 -154 186 C ATOM 3040 CG LEU A 549 -3.193 62.015 -10.714 1.00 20.93 C ANISOU 3040 CG LEU A 549 2906 2764 2281 231 -213 259 C ATOM 3041 CD1 LEU A 549 -2.064 62.985 -11.082 1.00 22.58 C ANISOU 3041 CD1 LEU A 549 3223 2897 2459 147 -267 198 C ATOM 3042 CD2 LEU A 549 -2.731 60.564 -10.810 1.00 18.07 C ANISOU 3042 CD2 LEU A 549 2447 2502 1919 198 -207 389 C ATOM 3043 N SER A 550 -5.879 62.723 -6.917 1.00 20.54 N ANISOU 3043 N SER A 550 2782 2955 2069 437 -12 60 N ATOM 3044 CA SER A 550 -6.036 62.881 -5.473 1.00 21.54 C ANISOU 3044 CA SER A 550 2895 3198 2091 448 44 -2 C ATOM 3045 C SER A 550 -7.041 61.872 -4.900 1.00 22.25 C ANISOU 3045 C SER A 550 2872 3385 2196 528 102 58 C ATOM 3046 O SER A 550 -7.133 61.707 -3.688 1.00 22.13 O ANISOU 3046 O SER A 550 2825 3492 2094 535 150 32 O ATOM 3047 CB SER A 550 -6.402 64.335 -5.117 1.00 23.11 C ANISOU 3047 CB SER A 550 3201 3309 2269 470 65 -139 C ATOM 3048 OG SER A 550 -7.709 64.669 -5.574 1.00 29.33 O ANISOU 3048 OG SER A 550 3992 3993 3158 575 90 -155 O ATOM 3049 N ARG A 551 -7.764 61.177 -5.782 1.00 20.68 N ANISOU 3049 N ARG A 551 2615 3137 2106 584 96 140 N ATOM 3050 CA ARG A 551 -8.661 60.083 -5.372 1.00 21.63 C ANISOU 3050 CA ARG A 551 2622 3350 2248 654 147 211 C ATOM 3051 C ARG A 551 -7.901 58.829 -4.925 1.00 22.53 C ANISOU 3051 C ARG A 551 2647 3611 2300 601 156 306 C ATOM 3052 O ARG A 551 -8.463 57.958 -4.264 1.00 20.83 O ANISOU 3052 O ARG A 551 2341 3503 2072 648 208 353 O ATOM 3053 CB ARG A 551 -9.587 59.686 -6.545 1.00 22.61 C ANISOU 3053 CB ARG A 551 2710 3376 2505 717 135 276 C ATOM 3054 CG ARG A 551 -10.550 60.763 -6.959 1.00 21.17 C ANISOU 3054 CG ARG A 551 2591 3061 2394 788 136 202 C ATOM 3055 CD ARG A 551 -11.387 60.337 -8.178 1.00 21.48 C ANISOU 3055 CD ARG A 551 2591 3011 2560 838 116 276 C ATOM 3056 NE ARG A 551 -11.940 58.998 -8.028 1.00 26.18 N ANISOU 3056 NE ARG A 551 3069 3703 3176 871 150 372 N ATOM 3057 CZ ARG A 551 -12.340 58.252 -9.053 1.00 31.77 C ANISOU 3057 CZ ARG A 551 3728 4372 3973 882 130 461 C ATOM 3058 NH1 ARG A 551 -12.250 58.735 -10.295 1.00 21.81 N ANISOU 3058 NH1 ARG A 551 2523 2976 2787 862 74 467 N ATOM 3059 NH2 ARG A 551 -12.833 57.035 -8.838 1.00 26.75 N ANISOU 3059 NH2 ARG A 551 2987 3829 3349 909 169 544 N ATOM 3060 N PHE A 552 -6.632 58.728 -5.299 1.00 19.85 N ANISOU 3060 N PHE A 552 2333 3278 1929 507 109 339 N ATOM 3061 CA PHE A 552 -5.854 57.499 -5.095 1.00 19.94 C ANISOU 3061 CA PHE A 552 2262 3414 1901 456 115 447 C ATOM 3062 C PHE A 552 -4.628 57.717 -4.221 1.00 20.66 C ANISOU 3062 C PHE A 552 2373 3610 1865 369 105 423 C ATOM 3063 O PHE A 552 -3.992 58.763 -4.312 1.00 19.64 O ANISOU 3063 O PHE A 552 2339 3422 1701 314 66 343 O ATOM 3064 CB PHE A 552 -5.407 56.965 -6.458 1.00 19.96 C ANISOU 3064 CB PHE A 552 2261 3333 1990 419 69 537 C ATOM 3065 CG PHE A 552 -6.558 56.633 -7.357 1.00 17.90 C ANISOU 3065 CG PHE A 552 1972 2981 1849 493 76 575 C ATOM 3066 CD1 PHE A 552 -7.188 55.400 -7.262 1.00 29.28 C ANISOU 3066 CD1 PHE A 552 3308 4496 3321 537 123 665 C ATOM 3067 CD2 PHE A 552 -7.043 57.566 -8.257 1.00 17.51 C ANISOU 3067 CD2 PHE A 552 2000 2776 1878 519 39 518 C ATOM 3068 CE1 PHE A 552 -8.285 55.097 -8.071 1.00 29.28 C ANISOU 3068 CE1 PHE A 552 3279 4417 3427 601 129 699 C ATOM 3069 CE2 PHE A 552 -8.142 57.283 -9.058 1.00 17.00 C ANISOU 3069 CE2 PHE A 552 1905 2636 1919 586 44 554 C ATOM 3070 CZ PHE A 552 -8.757 56.036 -8.970 1.00 21.44 C ANISOU 3070 CZ PHE A 552 2361 3275 2510 624 88 645 C ATOM 3071 N SER A 553 -4.277 56.721 -3.407 1.00 19.15 N ANISOU 3071 N SER A 553 2092 3577 1607 352 140 495 N ATOM 3072 CA SER A 553 -3.053 56.793 -2.621 1.00 19.54 C ANISOU 3072 CA SER A 553 2146 3742 1536 263 128 492 C ATOM 3073 C SER A 553 -1.826 57.115 -3.486 1.00 19.04 C ANISOU 3073 C SER A 553 2144 3610 1479 171 61 511 C ATOM 3074 O SER A 553 -0.971 57.906 -3.080 1.00 19.63 O ANISOU 3074 O SER A 553 2284 3705 1469 98 32 446 O ATOM 3075 CB SER A 553 -2.799 55.484 -1.859 1.00 21.79 C ANISOU 3075 CB SER A 553 2312 4200 1767 260 173 598 C ATOM 3076 OG SER A 553 -3.862 55.191 -0.960 1.00 22.44 O ANISOU 3076 OG SER A 553 2338 4356 1832 341 237 577 O ATOM 3077 N SER A 554 -1.727 56.465 -4.643 1.00 17.97 N ANISOU 3077 N SER A 554 1987 3401 1440 169 39 602 N ATOM 3078 CA SER A 554 -0.585 56.673 -5.536 1.00 18.12 C ANISOU 3078 CA SER A 554 2059 3349 1475 84 -22 630 C ATOM 3079 C SER A 554 -0.510 58.118 -6.020 1.00 18.85 C ANISOU 3079 C SER A 554 2279 3301 1582 65 -71 512 C ATOM 3080 O SER A 554 0.575 58.706 -6.120 1.00 18.19 O ANISOU 3080 O SER A 554 2258 3204 1450 -19 -116 484 O ATOM 3081 CB SER A 554 -0.668 55.725 -6.741 1.00 17.06 C ANISOU 3081 CB SER A 554 1884 3146 1453 95 -28 744 C ATOM 3082 OG SER A 554 -1.824 55.994 -7.521 1.00 17.04 O ANISOU 3082 OG SER A 554 1906 3013 1554 168 -29 713 O ATOM 3083 N GLY A 555 -1.667 58.684 -6.338 1.00 20.33 N ANISOU 3083 N GLY A 555 2503 3384 1840 143 -61 446 N ATOM 3084 CA GLY A 555 -1.731 60.064 -6.787 1.00 20.15 C ANISOU 3084 CA GLY A 555 2598 3220 1837 138 -98 333 C ATOM 3085 C GLY A 555 -1.395 61.053 -5.688 1.00 22.01 C ANISOU 3085 C GLY A 555 2895 3511 1958 103 -88 219 C ATOM 3086 O GLY A 555 -0.673 62.015 -5.925 1.00 19.99 O ANISOU 3086 O GLY A 555 2734 3187 1674 41 -129 150 O ATOM 3087 N LYS A 556 -1.923 60.833 -4.485 1.00 20.40 N ANISOU 3087 N LYS A 556 2640 3426 1686 142 -31 196 N ATOM 3088 CA LYS A 556 -1.542 61.678 -3.354 1.00 24.39 C ANISOU 3088 CA LYS A 556 3199 3999 2067 98 -16 93 C ATOM 3089 C LYS A 556 -0.039 61.605 -3.126 1.00 26.89 C ANISOU 3089 C LYS A 556 3524 4401 2291 -21 -56 120 C ATOM 3090 O LYS A 556 0.600 62.599 -2.788 1.00 23.15 O ANISOU 3090 O LYS A 556 3137 3917 1741 -88 -77 28 O ATOM 3091 CB LYS A 556 -2.268 61.259 -2.075 1.00 22.24 C ANISOU 3091 CB LYS A 556 2858 3860 1732 151 52 82 C ATOM 3092 CG LYS A 556 -3.768 61.568 -2.084 1.00 30.35 C ANISOU 3092 CG LYS A 556 3891 4809 2834 266 98 31 C ATOM 3093 CD LYS A 556 -4.405 61.008 -0.807 1.00 39.38 C ANISOU 3093 CD LYS A 556 4955 6095 3912 314 167 34 C ATOM 3094 CE LYS A 556 -5.900 60.840 -0.944 1.00 58.59 C ANISOU 3094 CE LYS A 556 7352 8472 6437 435 213 33 C ATOM 3095 NZ LYS A 556 -6.401 59.782 -0.024 1.00 63.32 N ANISOU 3095 NZ LYS A 556 7839 9218 7000 481 271 92 N ATOM 3096 N LYS A 557 0.528 60.420 -3.311 1.00 20.69 N ANISOU 3096 N LYS A 557 2649 3701 1512 -47 -64 249 N ATOM 3097 CA LYS A 557 1.963 60.255 -3.104 1.00 24.02 C ANISOU 3097 CA LYS A 557 3066 4213 1850 -156 -100 292 C ATOM 3098 C LYS A 557 2.793 61.093 -4.089 1.00 21.19 C ANISOU 3098 C LYS A 557 2808 3722 1520 -225 -167 256 C ATOM 3099 O LYS A 557 3.814 61.679 -3.705 1.00 25.30 O ANISOU 3099 O LYS A 557 3379 4286 1949 -317 -197 213 O ATOM 3100 CB LYS A 557 2.352 58.783 -3.214 1.00 28.06 C ANISOU 3100 CB LYS A 557 3458 4826 2377 -162 -88 448 C ATOM 3101 CG LYS A 557 3.681 58.448 -2.579 1.00 45.10 C ANISOU 3101 CG LYS A 557 5580 7131 4425 -260 -103 503 C ATOM 3102 CD LYS A 557 3.909 56.931 -2.533 1.00 53.86 C ANISOU 3102 CD LYS A 557 6562 8354 5550 -249 -72 660 C ATOM 3103 CE LYS A 557 2.656 56.158 -2.143 1.00 50.25 C ANISOU 3103 CE LYS A 557 6024 7938 5131 -145 -6 689 C ATOM 3104 NZ LYS A 557 2.912 54.684 -2.210 1.00 51.47 N ANISOU 3104 NZ LYS A 557 6061 8186 5308 -137 27 844 N ATOM 3105 N MET A 558 2.378 61.135 -5.353 1.00 20.78 N ANISOU 3105 N MET A 558 2786 3514 1594 -185 -191 275 N ATOM 3106 CA MET A 558 3.110 61.904 -6.372 1.00 19.26 C ANISOU 3106 CA MET A 558 2690 3186 1440 -244 -254 244 C ATOM 3107 C MET A 558 2.968 63.400 -6.125 1.00 25.64 C ANISOU 3107 C MET A 558 3617 3912 2211 -254 -262 91 C ATOM 3108 O MET A 558 3.907 64.186 -6.314 1.00 22.66 O ANISOU 3108 O MET A 558 3322 3494 1792 -337 -305 39 O ATOM 3109 CB MET A 558 2.585 61.578 -7.790 1.00 18.20 C ANISOU 3109 CB MET A 558 2559 2905 1453 -193 -274 301 C ATOM 3110 CG MET A 558 2.868 60.137 -8.203 1.00 21.32 C ANISOU 3110 CG MET A 558 2851 3360 1891 -197 -267 453 C ATOM 3111 SD MET A 558 2.770 59.945 -9.988 1.00 23.95 S ANISOU 3111 SD MET A 558 3217 3511 2373 -187 -309 513 S ATOM 3112 CE MET A 558 1.026 60.214 -10.245 1.00 20.38 C ANISOU 3112 CE MET A 558 2767 2966 2011 -66 -278 461 C ATOM 3113 N ILE A 559 1.771 63.798 -5.722 1.00 22.28 N ANISOU 3113 N ILE A 559 3203 3457 1804 -169 -216 19 N ATOM 3114 CA ILE A 559 1.515 65.196 -5.412 1.00 24.68 C ANISOU 3114 CA ILE A 559 3619 3683 2074 -169 -208 -126 C ATOM 3115 C ILE A 559 2.405 65.627 -4.255 1.00 29.48 C ANISOU 3115 C ILE A 559 4254 4415 2531 -261 -203 -187 C ATOM 3116 O ILE A 559 2.997 66.707 -4.290 1.00 27.02 O ANISOU 3116 O ILE A 559 4048 4044 2175 -326 -228 -281 O ATOM 3117 CB ILE A 559 0.036 65.415 -5.052 1.00 24.69 C ANISOU 3117 CB ILE A 559 3613 3650 2118 -56 -148 -179 C ATOM 3118 CG1 ILE A 559 -0.820 65.294 -6.317 1.00 24.00 C ANISOU 3118 CG1 ILE A 559 3524 3414 2182 26 -161 -139 C ATOM 3119 CG2 ILE A 559 -0.156 66.768 -4.359 1.00 30.27 C ANISOU 3119 CG2 ILE A 559 4425 4317 2759 -64 -119 -330 C ATOM 3120 CD1 ILE A 559 -2.312 65.070 -6.050 1.00 27.14 C ANISOU 3120 CD1 ILE A 559 3871 3805 2635 145 -103 -143 C ATOM 3121 N GLU A 560 2.510 64.764 -3.242 1.00 29.67 N ANISOU 3121 N GLU A 560 4184 4616 2475 -270 -171 -131 N ATOM 3122 CA GLU A 560 3.359 65.033 -2.078 1.00 32.06 C ANISOU 3122 CA GLU A 560 4496 5061 2625 -362 -167 -174 C ATOM 3123 C GLU A 560 4.841 65.053 -2.458 1.00 29.13 C ANISOU 3123 C GLU A 560 4144 4714 2210 -479 -231 -133 C ATOM 3124 O GLU A 560 5.617 65.866 -1.950 1.00 30.17 O ANISOU 3124 O GLU A 560 4345 4879 2239 -570 -248 -211 O ATOM 3125 CB GLU A 560 3.138 63.966 -1.006 1.00 31.68 C ANISOU 3125 CB GLU A 560 4328 5199 2511 -341 -121 -102 C ATOM 3126 CG GLU A 560 4.084 64.070 0.187 1.00 46.51 C ANISOU 3126 CG GLU A 560 6198 7247 4227 -442 -120 -123 C ATOM 3127 CD GLU A 560 4.046 62.830 1.081 1.00 64.73 C ANISOU 3127 CD GLU A 560 8372 9745 6479 -427 -84 -21 C ATOM 3128 OE1 GLU A 560 3.541 61.774 0.633 1.00 64.64 O ANISOU 3128 OE1 GLU A 560 8271 9734 6556 -354 -68 85 O ATOM 3129 OE2 GLU A 560 4.532 62.912 2.232 1.00 75.34 O ANISOU 3129 OE2 GLU A 560 9702 11239 7687 -491 -70 -46 O ATOM 3130 N THR A 561 5.237 64.129 -3.324 1.00 25.17 N ANISOU 3130 N THR A 561 3579 4201 1783 -480 -262 -6 N ATOM 3131 CA THR A 561 6.616 64.079 -3.800 1.00 25.36 C ANISOU 3131 CA THR A 561 3617 4236 1782 -583 -321 46 C ATOM 3132 C THR A 561 6.995 65.407 -4.464 1.00 31.74 C ANISOU 3132 C THR A 561 4562 4890 2606 -629 -365 -63 C ATOM 3133 O THR A 561 8.055 65.971 -4.181 1.00 30.06 O ANISOU 3133 O THR A 561 4400 4718 2303 -733 -398 -102 O ATOM 3134 CB THR A 561 6.849 62.882 -4.754 1.00 28.94 C ANISOU 3134 CB THR A 561 3988 4674 2333 -564 -339 199 C ATOM 3135 OG1 THR A 561 6.729 61.660 -4.009 1.00 29.23 O ANISOU 3135 OG1 THR A 561 3898 4875 2334 -540 -297 302 O ATOM 3136 CG2 THR A 561 8.242 62.947 -5.380 1.00 31.06 C ANISOU 3136 CG2 THR A 561 4284 4926 2590 -666 -400 247 C ATOM 3137 N LEU A 562 6.124 65.919 -5.329 1.00 25.19 N ANISOU 3137 N LEU A 562 3794 3889 1889 -554 -363 -112 N ATOM 3138 CA LEU A 562 6.403 67.187 -6.002 1.00 27.45 C ANISOU 3138 CA LEU A 562 4211 4019 2199 -588 -399 -214 C ATOM 3139 C LEU A 562 6.371 68.359 -5.025 1.00 36.59 C ANISOU 3139 C LEU A 562 5456 5196 3249 -624 -372 -361 C ATOM 3140 O LEU A 562 7.163 69.294 -5.145 1.00 36.66 O ANISOU 3140 O LEU A 562 5561 5156 3212 -706 -404 -437 O ATOM 3141 CB LEU A 562 5.428 67.425 -7.158 1.00 22.01 C ANISOU 3141 CB LEU A 562 3559 3146 1658 -494 -401 -224 C ATOM 3142 CG LEU A 562 5.653 66.531 -8.384 1.00 23.72 C ANISOU 3142 CG LEU A 562 3725 3302 1983 -483 -441 -97 C ATOM 3143 CD1 LEU A 562 4.415 66.466 -9.289 1.00 24.27 C ANISOU 3143 CD1 LEU A 562 3795 3235 2191 -374 -428 -87 C ATOM 3144 CD2 LEU A 562 6.842 67.054 -9.160 1.00 24.70 C ANISOU 3144 CD2 LEU A 562 3925 3348 2110 -575 -505 -104 C ATOM 3145 N ALA A 563 5.454 68.309 -4.060 1.00 33.57 N ANISOU 3145 N ALA A 563 5044 4883 2829 -564 -309 -402 N ATOM 3146 CA ALA A 563 5.382 69.345 -3.027 1.00 37.41 C ANISOU 3146 CA ALA A 563 5609 5398 3205 -599 -272 -539 C ATOM 3147 C ALA A 563 6.659 69.404 -2.190 1.00 40.01 C ANISOU 3147 C ALA A 563 5939 5878 3384 -731 -295 -546 C ATOM 3148 O ALA A 563 7.175 70.486 -1.916 1.00 43.07 O ANISOU 3148 O ALA A 563 6430 6237 3696 -808 -302 -656 O ATOM 3149 CB ALA A 563 4.168 69.133 -2.134 1.00 44.08 C ANISOU 3149 CB ALA A 563 6410 6300 4038 -508 -198 -567 C ATOM 3150 N ASN A 564 7.169 68.242 -1.789 1.00 33.02 N ANISOU 3150 N ASN A 564 4936 5154 2455 -759 -305 -426 N ATOM 3151 CA ASN A 564 8.389 68.170 -0.987 1.00 41.43 C ANISOU 3151 CA ASN A 564 5983 6381 3378 -883 -329 -411 C ATOM 3152 C ASN A 564 9.609 68.709 -1.736 1.00 47.16 C ANISOU 3152 C ASN A 564 6778 7043 4099 -984 -398 -416 C ATOM 3153 O ASN A 564 10.552 69.213 -1.128 1.00 46.93 O ANISOU 3153 O ASN A 564 6786 7098 3946 -1098 -418 -462 O ATOM 3154 CB ASN A 564 8.676 66.732 -0.543 1.00 45.57 C ANISOU 3154 CB ASN A 564 6358 7082 3874 -881 -326 -261 C ATOM 3155 CG ASN A 564 7.688 66.228 0.499 1.00 55.36 C ANISOU 3155 CG ASN A 564 7527 8429 5078 -808 -257 -263 C ATOM 3156 OD1 ASN A 564 7.688 65.043 0.846 1.00 58.00 O ANISOU 3156 OD1 ASN A 564 7739 8892 5405 -785 -242 -145 O ATOM 3157 ND2 ASN A 564 6.838 67.123 0.997 1.00 52.04 N ANISOU 3157 ND2 ASN A 564 7184 7952 4637 -771 -212 -395 N ATOM 3158 N LEU A 565 9.591 68.585 -3.056 1.00 45.59 N ANISOU 3158 N LEU A 565 6593 6697 4031 -946 -434 -367 N ATOM 3159 CA LEU A 565 10.700 69.069 -3.868 1.00 49.72 C ANISOU 3159 CA LEU A 565 7183 7144 4563 -1034 -498 -368 C ATOM 3160 C LEU A 565 10.766 70.594 -3.838 1.00 57.67 C ANISOU 3160 C LEU A 565 8338 8042 5532 -1078 -499 -531 C ATOM 3161 O LEU A 565 11.839 71.171 -3.643 1.00 51.33 O ANISOU 3161 O LEU A 565 7590 7274 4639 -1193 -533 -573 O ATOM 3162 CB LEU A 565 10.582 68.564 -5.303 1.00 38.31 C ANISOU 3162 CB LEU A 565 5722 5562 3273 -978 -531 -279 C ATOM 3163 CG LEU A 565 11.783 68.893 -6.193 1.00 38.37 C ANISOU 3163 CG LEU A 565 5784 5498 3297 -1066 -599 -259 C ATOM 3164 CD1 LEU A 565 13.053 68.337 -5.594 1.00 40.66 C ANISOU 3164 CD1 LEU A 565 6008 5963 3479 -1173 -625 -178 C ATOM 3165 CD2 LEU A 565 11.578 68.357 -7.590 1.00 37.89 C ANISOU 3165 CD2 LEU A 565 5707 5300 3388 -1007 -625 -171 C ATOM 3166 N ARG A 566 9.616 71.240 -4.026 1.00 69.46 N ANISOU 3166 N ARG A 566 9896 9404 7093 -987 -457 -622 N ATOM 3167 CA ARG A 566 9.530 72.697 -3.953 1.00 82.76 C ANISOU 3167 CA ARG A 566 11723 10977 8746 -1015 -442 -780 C ATOM 3168 C ARG A 566 10.115 73.204 -2.642 1.00 83.35 C ANISOU 3168 C ARG A 566 11828 11191 8648 -1120 -421 -862 C ATOM 3169 O ARG A 566 10.757 74.251 -2.605 1.00 86.10 O ANISOU 3169 O ARG A 566 12285 11493 8935 -1208 -435 -964 O ATOM 3170 CB ARG A 566 8.081 73.167 -4.075 1.00 91.10 C ANISOU 3170 CB ARG A 566 12819 11908 9887 -891 -382 -852 C ATOM 3171 CG ARG A 566 7.426 72.860 -5.405 1.00 98.87 C ANISOU 3171 CG ARG A 566 13789 12738 11040 -791 -402 -788 C ATOM 3172 CD ARG A 566 5.974 73.312 -5.404 1.00105.82 C ANISOU 3172 CD ARG A 566 14699 13514 11993 -669 -340 -854 C ATOM 3173 NE ARG A 566 5.230 72.780 -6.542 1.00109.84 N ANISOU 3173 NE ARG A 566 15164 13912 12656 -568 -355 -772 N ATOM 3174 CZ ARG A 566 4.640 71.588 -6.558 1.00111.07 C ANISOU 3174 CZ ARG A 566 15201 14139 12863 -498 -345 -662 C ATOM 3175 NH1 ARG A 566 4.711 70.796 -5.496 1.00112.01 N ANISOU 3175 NH1 ARG A 566 15229 14436 12894 -514 -318 -618 N ATOM 3176 NH2 ARG A 566 3.982 71.184 -7.637 1.00110.27 N ANISOU 3176 NH2 ARG A 566 15070 13929 12898 -416 -360 -595 N ATOM 3177 N SER A 567 9.890 72.452 -1.570 1.00 82.05 N ANISOU 3177 N SER A 567 11569 11201 8406 -1113 -387 -819 N ATOM 3178 CA SER A 567 10.413 72.807 -0.254 1.00 81.47 C ANISOU 3178 CA SER A 567 11512 11283 8162 -1215 -367 -885 C ATOM 3179 C SER A 567 11.925 72.581 -0.162 1.00 81.74 C ANISOU 3179 C SER A 567 11520 11435 8102 -1352 -431 -826 C ATOM 3180 O SER A 567 12.594 72.238 -1.138 1.00 75.65 O ANISOU 3180 O SER A 567 10730 10614 7402 -1370 -490 -741 O ATOM 3181 CB SER A 567 9.688 72.012 0.837 1.00 83.81 C ANISOU 3181 CB SER A 567 11707 11729 8406 -1161 -311 -848 C ATOM 3182 OG SER A 567 9.932 72.556 2.124 1.00 89.26 O ANISOU 3182 OG SER A 567 12436 12542 8937 -1245 -278 -941 O TER 3183 SER A 567 ATOM 3184 O5' U B 1 -2.953 50.286 -0.018 1.00 41.04 O ANISOU 3184 O5' U B 1 5993 5186 4412 675 447 834 O ATOM 3185 C5' U B 1 -4.094 49.644 -0.534 1.00 31.13 C ANISOU 3185 C5' U B 1 4768 3824 3235 623 591 856 C ATOM 3186 C4' U B 1 -3.885 49.196 -1.967 1.00 22.50 C ANISOU 3186 C4' U B 1 3574 2688 2286 529 643 791 C ATOM 3187 O4' U B 1 -3.862 50.409 -2.772 1.00 21.78 O ANISOU 3187 O4' U B 1 3418 2660 2198 396 579 680 O ATOM 3188 C3' U B 1 -2.540 48.513 -2.297 1.00 22.28 C ANISOU 3188 C3' U B 1 3461 2688 2316 584 597 787 C ATOM 3189 O3' U B 1 -2.629 47.057 -2.098 1.00 22.56 O ANISOU 3189 O3' U B 1 3520 2639 2412 673 694 873 O ATOM 3190 C2' U B 1 -2.466 48.806 -3.832 1.00 23.71 C ANISOU 3190 C2' U B 1 3535 2863 2611 453 607 687 C ATOM 3191 O2' U B 1 -3.351 47.886 -4.530 1.00 22.18 O ANISOU 3191 O2' U B 1 3350 2546 2529 422 747 706 O ATOM 3192 C1' U B 1 -3.062 50.200 -3.946 1.00 22.39 C ANISOU 3192 C1' U B 1 3374 2747 2385 345 563 613 C ATOM 3193 N1 U B 1 -1.964 51.169 -3.971 1.00 20.23 N ANISOU 3193 N1 U B 1 3024 2597 2066 335 410 554 N ATOM 3194 C2 U B 1 -1.431 51.448 -5.201 1.00 19.31 C ANISOU 3194 C2 U B 1 2785 2508 2044 253 381 469 C ATOM 3195 O2 U B 1 -1.873 50.916 -6.202 1.00 18.35 O ANISOU 3195 O2 U B 1 2627 2311 2036 193 480 441 O ATOM 3196 N3 U B 1 -0.392 52.348 -5.207 1.00 17.99 N ANISOU 3196 N3 U B 1 2542 2455 1840 253 231 425 N ATOM 3197 C4 U B 1 0.138 52.984 -4.090 1.00 22.93 C ANISOU 3197 C4 U B 1 3208 3161 2344 328 108 457 C ATOM 3198 O4 U B 1 1.077 53.771 -4.227 1.00 22.58 O ANISOU 3198 O4 U B 1 3085 3209 2287 325 -29 418 O ATOM 3199 C5 U B 1 -0.467 52.635 -2.828 1.00 19.91 C ANISOU 3199 C5 U B 1 2961 2741 1865 416 149 542 C ATOM 3200 C6 U B 1 -1.481 51.758 -2.821 1.00 21.74 C ANISOU 3200 C6 U B 1 3262 2867 2131 416 297 587 C ATOM 3201 P G B 2 -1.337 46.378 -1.773 1.00 25.11 P ANISOU 3201 P G B 2 3807 3003 2733 768 640 904 P ATOM 3202 OP1 G B 2 -1.859 44.867 -1.016 1.00 24.45 O ANISOU 3202 OP1 G B 2 3789 2829 2673 888 758 1023 O ATOM 3203 OP2 G B 2 -0.426 47.077 -1.007 1.00 26.72 O ANISOU 3203 OP2 G B 2 4017 3301 2835 821 517 898 O ATOM 3204 O5' G B 2 -0.713 45.951 -3.119 1.00 26.54 O ANISOU 3204 O5' G B 2 3879 3172 3034 707 645 850 O ATOM 3205 C5' G B 2 -1.434 45.159 -4.089 1.00 25.15 C ANISOU 3205 C5' G B 2 3677 2895 2983 660 757 849 C ATOM 3206 C4' G B 2 -0.498 44.594 -5.147 1.00 21.83 C ANISOU 3206 C4' G B 2 3154 2481 2659 647 736 817 C ATOM 3207 O4' G B 2 0.118 45.685 -5.845 1.00 20.73 O ANISOU 3207 O4' G B 2 2937 2420 2519 568 641 726 O ATOM 3208 C3' G B 2 0.638 43.747 -4.625 1.00 21.79 C ANISOU 3208 C3' G B 2 3137 2511 2630 749 696 875 C ATOM 3209 O3' G B 2 0.186 42.419 -4.438 1.00 22.76 O ANISOU 3209 O3' G B 2 3289 2552 2806 814 794 951 O ATOM 3210 C2' G B 2 1.572 43.844 -5.809 1.00 22.44 C ANISOU 3210 C2' G B 2 3112 2629 2785 701 637 815 C ATOM 3211 O2' G B 2 1.189 42.927 -6.804 1.00 24.60 O ANISOU 3211 O2' G B 2 3344 2821 3181 683 719 818 O ATOM 3212 C1' G B 2 1.395 45.298 -6.252 1.00 21.96 C ANISOU 3212 C1' G B 2 3017 2622 2705 603 575 726 C ATOM 3213 N9 G B 2 2.445 46.163 -5.660 1.00 24.83 N ANISOU 3213 N9 G B 2 3369 3093 2974 629 440 713 N ATOM 3214 C8 G B 2 2.589 46.571 -4.342 1.00 24.63 C ANISOU 3214 C8 G B 2 3420 3111 2827 694 387 752 C ATOM 3215 N7 G B 2 3.651 47.307 -4.150 1.00 23.49 N ANISOU 3215 N7 G B 2 3240 3053 2632 710 257 732 N ATOM 3216 C5 G B 2 4.256 47.382 -5.414 1.00 21.00 C ANISOU 3216 C5 G B 2 2813 2756 2409 652 225 682 C ATOM 3217 C6 G B 2 5.447 48.034 -5.839 1.00 22.85 C ANISOU 3217 C6 G B 2 2962 3070 2649 645 96 651 C ATOM 3218 O6 G B 2 6.214 48.702 -5.131 1.00 22.14 O ANISOU 3218 O6 G B 2 2884 3047 2481 690 -21 663 O ATOM 3219 N1 G B 2 5.723 47.845 -7.204 1.00 19.72 N ANISOU 3219 N1 G B 2 2460 2666 2365 592 106 611 N ATOM 3220 C2 G B 2 4.898 47.116 -8.041 1.00 19.51 C ANISOU 3220 C2 G B 2 2420 2560 2434 551 228 596 C ATOM 3221 N2 G B 2 5.262 47.041 -9.335 1.00 19.64 N ANISOU 3221 N2 G B 2 2330 2577 2555 512 220 555 N ATOM 3222 N3 G B 2 3.783 46.514 -7.649 1.00 20.10 N ANISOU 3222 N3 G B 2 2577 2554 2508 554 345 624 N ATOM 3223 C4 G B 2 3.534 46.683 -6.339 1.00 24.39 C ANISOU 3223 C4 G B 2 3217 3108 2942 605 336 668 C ATOM 3224 P U B 3 0.875 41.455 -3.321 1.00 29.30 P ANISOU 3224 P U B 3 4153 3403 3578 939 789 1038 P ATOM 3225 OP1 U B 3 0.110 40.216 -3.271 1.00 31.85 O ANISOU 3225 OP1 U B 3 4495 3634 3973 988 898 1108 O ATOM 3226 OP2 U B 3 1.104 42.253 -2.080 1.00 26.63 O ANISOU 3226 OP2 U B 3 3880 3130 3107 988 725 1051 O ATOM 3227 O5' U B 3 2.252 41.205 -4.043 1.00 23.94 O ANISOU 3227 O5' U B 3 3387 2776 2931 931 716 1008 O ATOM 3228 C5' U B 3 3.347 40.578 -3.359 1.00 23.89 C ANISOU 3228 C5' U B 3 3386 2817 2875 1013 675 1055 C ATOM 3229 C4' U B 3 3.820 39.395 -4.212 1.00 24.62 C ANISOU 3229 C4' U B 3 3413 2882 3060 1020 704 1074 C ATOM 3230 O4' U B 3 4.259 39.899 -5.499 1.00 24.65 O ANISOU 3230 O4' U B 3 3335 2904 3126 943 651 1007 O ATOM 3231 C3' U B 3 5.003 38.609 -3.690 1.00 27.15 C ANISOU 3231 C3' U B 3 3730 3247 3340 1089 669 1120 C ATOM 3232 O3' U B 3 4.498 37.606 -2.816 1.00 33.56 O ANISOU 3232 O3' U B 3 4589 4020 4144 1166 750 1191 O ATOM 3233 C2' U B 3 5.505 37.984 -4.987 1.00 31.89 C ANISOU 3233 C2' U B 3 4245 3837 4035 1055 661 1106 C ATOM 3234 O2' U B 3 4.696 36.898 -5.392 1.00 32.82 O ANISOU 3234 O2' U B 3 4351 3877 4244 1070 753 1141 O ATOM 3235 C1' U B 3 5.308 39.110 -5.999 1.00 26.17 C ANISOU 3235 C1' U B 3 3473 3120 3352 968 619 1027 C ATOM 3236 N1 U B 3 6.527 39.947 -6.169 1.00 26.06 N ANISOU 3236 N1 U B 3 3421 3191 3291 950 500 993 N ATOM 3237 C2 U B 3 7.412 39.549 -7.133 1.00 31.45 C ANISOU 3237 C2 U B 3 4030 3893 4029 942 458 991 C ATOM 3238 O2 U B 3 7.191 38.552 -7.805 1.00 27.20 O ANISOU 3238 O2 U B 3 3459 3306 3570 950 514 1011 O ATOM 3239 N3 U B 3 8.521 40.353 -7.275 1.00 23.67 N ANISOU 3239 N3 U B 3 3008 2981 3004 931 345 969 N ATOM 3240 C4 U B 3 8.817 41.474 -6.525 1.00 25.96 C ANISOU 3240 C4 U B 3 3329 3324 3209 930 268 950 C ATOM 3241 O4 U B 3 9.859 42.096 -6.743 1.00 24.50 O ANISOU 3241 O4 U B 3 3104 3200 3005 928 161 941 O ATOM 3242 C5 U B 3 7.830 41.826 -5.529 1.00 26.49 C ANISOU 3242 C5 U B 3 3477 3370 3219 940 316 949 C ATOM 3243 C6 U B 3 6.742 41.062 -5.386 1.00 30.05 C ANISOU 3243 C6 U B 3 3964 3749 3703 949 431 973 C ATOM 3244 P G B 4 5.319 37.207 -1.493 1.00 42.27 P ANISOU 3244 P G B 4 5738 5172 5149 1256 729 1241 P ATOM 3245 OP1 G B 4 4.333 36.597 -0.566 1.00 38.05 O ANISOU 3245 OP1 G B 4 5256 4592 4610 1328 820 1303 O ATOM 3246 OP2 G B 4 6.147 38.349 -1.044 1.00 39.31 O ANISOU 3246 OP2 G B 4 5388 4866 4683 1252 626 1205 O ATOM 3247 O5' G B 4 6.344 36.112 -2.044 1.00 39.48 O ANISOU 3247 O5' G B 4 5325 4836 4837 1263 718 1260 O ATOM 3248 C5' G B 4 5.882 34.882 -2.564 1.00 49.08 C ANISOU 3248 C5' G B 4 6503 6002 6145 1274 792 1297 C ATOM 3249 C4' G B 4 7.063 34.053 -3.034 1.00 47.93 C ANISOU 3249 C4' G B 4 6306 5894 6011 1276 754 1310 C ATOM 3250 O4' G B 4 7.869 34.883 -3.895 1.00 45.01 O ANISOU 3250 O4' G B 4 5899 5563 5639 1215 664 1258 O ATOM 3251 C3' G B 4 8.065 33.585 -1.976 1.00 49.50 C ANISOU 3251 C3' G B 4 6538 6148 6123 1333 736 1346 C ATOM 3252 O3' G B 4 7.650 32.398 -1.347 1.00 50.13 O ANISOU 3252 O3' G B 4 6622 6205 6220 1395 815 1403 O ATOM 3253 C2' G B 4 9.247 33.261 -2.863 1.00 47.83 C ANISOU 3253 C2' G B 4 6273 5975 5927 1297 671 1337 C ATOM 3254 O2' G B 4 9.014 32.083 -3.595 1.00 47.21 O ANISOU 3254 O2' G B 4 6139 5867 5932 1299 714 1366 O ATOM 3255 C1' G B 4 9.208 34.444 -3.816 1.00 48.57 C ANISOU 3255 C1' G B 4 6338 6070 6048 1231 609 1278 C ATOM 3256 N9 G B 4 10.065 35.522 -3.361 1.00 45.09 N ANISOU 3256 N9 G B 4 5927 5683 5522 1225 520 1253 N ATOM 3257 C8 G B 4 9.762 36.611 -2.578 1.00 45.76 C ANISOU 3257 C8 G B 4 6065 5778 5543 1233 494 1229 C ATOM 3258 N7 G B 4 10.803 37.376 -2.361 1.00 46.98 N ANISOU 3258 N7 G B 4 6231 5983 5637 1233 396 1216 N ATOM 3259 C5 G B 4 11.843 36.747 -3.033 1.00 37.49 C ANISOU 3259 C5 G B 4 4984 4803 4457 1220 361 1235 C ATOM 3260 C6 G B 4 13.204 37.099 -3.175 1.00 42.43 C ANISOU 3260 C6 G B 4 5601 5474 5046 1216 260 1242 C ATOM 3261 O6 G B 4 13.798 38.080 -2.710 1.00 50.63 O ANISOU 3261 O6 G B 4 6668 6542 6028 1226 175 1230 O ATOM 3262 N1 G B 4 13.893 36.170 -3.951 1.00 40.12 N ANISOU 3262 N1 G B 4 5263 5190 4792 1204 259 1271 N ATOM 3263 C2 G B 4 13.335 35.050 -4.519 1.00 38.35 C ANISOU 3263 C2 G B 4 5002 4936 4634 1200 337 1288 C ATOM 3264 N2 G B 4 14.138 34.256 -5.231 1.00 40.38 N ANISOU 3264 N2 G B 4 5218 5211 4913 1194 315 1319 N ATOM 3265 N3 G B 4 12.070 34.711 -4.397 1.00 40.31 N ANISOU 3265 N3 G B 4 5254 5137 4925 1207 427 1282 N ATOM 3266 C4 G B 4 11.395 35.607 -3.648 1.00 37.85 C ANISOU 3266 C4 G B 4 4990 4815 4576 1215 436 1256 C ATOM 3267 P U B 5 8.379 31.890 -0.006 1.00 50.99 P ANISOU 3267 P U B 5 6773 6361 6241 1466 825 1440 P ATOM 3268 OP1 U B 5 7.825 30.538 0.248 1.00 62.95 O ANISOU 3268 OP1 U B 5 8259 7850 7811 1516 909 1496 O ATOM 3269 OP2 U B 5 8.243 32.946 1.027 1.00 45.29 O ANISOU 3269 OP2 U B 5 6124 5650 5433 1500 805 1426 O ATOM 3270 O5' U B 5 9.936 31.766 -0.360 1.00 47.18 O ANISOU 3270 O5' U B 5 6272 5937 5717 1433 747 1426 O ATOM 3271 C5' U B 5 10.446 30.607 -1.029 1.00 47.42 C ANISOU 3271 C5' U B 5 6246 5980 5794 1418 754 1451 C ATOM 3272 C4' U B 5 11.962 30.597 -1.120 1.00 39.13 C ANISOU 3272 C4' U B 5 5200 4987 4681 1395 680 1447 C ATOM 3273 O4' U B 5 12.429 31.799 -1.793 1.00 45.61 O ANISOU 3273 O4' U B 5 6019 5819 5492 1346 590 1406 O ATOM 3274 C3' U B 5 12.689 30.574 0.220 1.00 39.75 C ANISOU 3274 C3' U B 5 5344 5099 4662 1441 681 1461 C ATOM 3275 O3' U B 5 12.810 29.232 0.708 1.00 40.51 O ANISOU 3275 O3' U B 5 5423 5208 4759 1474 746 1501 O ATOM 3276 C2' U B 5 14.038 31.204 -0.141 1.00 49.60 C ANISOU 3276 C2' U B 5 6605 6382 5859 1401 580 1445 C ATOM 3277 O2' U B 5 14.975 30.280 -0.661 1.00 52.94 O ANISOU 3277 O2' U B 5 6996 6836 6283 1374 563 1471 O ATOM 3278 C1' U B 5 13.672 32.199 -1.243 1.00 37.85 C ANISOU 3278 C1' U B 5 5079 4879 4423 1351 523 1408 C ATOM 3279 N1 U B 5 13.530 33.599 -0.786 1.00 51.29 N ANISOU 3279 N1 U B 5 6826 6579 6082 1357 472 1373 N ATOM 3280 C2 U B 5 14.639 34.419 -0.712 1.00 58.61 C ANISOU 3280 C2 U B 5 7776 7537 6954 1347 372 1364 C ATOM 3281 O2 U B 5 15.763 34.051 -0.999 1.00 61.51 O ANISOU 3281 O2 U B 5 8136 7929 7304 1332 327 1386 O ATOM 3282 N3 U B 5 14.387 35.703 -0.283 1.00 61.48 N ANISOU 3282 N3 U B 5 8175 7900 7285 1358 321 1333 N ATOM 3283 C4 U B 5 13.161 36.233 0.067 1.00 57.30 C ANISOU 3283 C4 U B 5 7663 7346 6762 1372 362 1310 C ATOM 3284 O4 U B 5 13.077 37.402 0.434 1.00 66.79 O ANISOU 3284 O4 U B 5 8895 8556 7925 1379 300 1283 O ATOM 3285 C5 U B 5 12.057 35.314 -0.041 1.00 59.41 C ANISOU 3285 C5 U B 5 7910 7577 7085 1379 472 1326 C ATOM 3286 C6 U B 5 12.274 34.062 -0.454 1.00 55.71 C ANISOU 3286 C6 U B 5 7403 7106 6659 1374 520 1356 C ATOM 3287 P U B 6 12.309 28.808 2.189 1.00 44.10 P ANISOU 3287 P U B 6 5917 5659 5178 1558 828 1525 P ATOM 3288 OP1 U B 6 12.483 27.346 2.312 1.00 37.50 O ANISOU 3288 OP1 U B 6 5036 4847 4366 1572 884 1562 O ATOM 3289 OP2 U B 6 11.002 29.413 2.506 1.00 41.05 O ANISOU 3289 OP2 U B 6 5549 5228 4819 1596 867 1524 O ATOM 3290 O5' U B 6 13.428 29.457 3.113 1.00 36.95 O ANISOU 3290 O5' U B 6 5088 4784 4167 1576 779 1509 O ATOM 3291 C5' U B 6 14.713 28.833 3.069 1.00 46.21 C ANISOU 3291 C5' U B 6 6260 5996 5300 1547 754 1518 C ATOM 3292 C4' U B 6 15.760 29.721 3.692 1.00 47.20 C ANISOU 3292 C4' U B 6 6463 6132 5340 1555 685 1500 C ATOM 3293 O4' U B 6 15.956 30.896 2.870 1.00 48.00 O ANISOU 3293 O4' U B 6 6565 6225 5449 1510 589 1476 O ATOM 3294 C3' U B 6 15.370 30.269 5.055 1.00 45.68 C ANISOU 3294 C3' U B 6 6337 5922 5097 1639 713 1494 C ATOM 3295 O3' U B 6 15.631 29.278 6.042 1.00 34.71 O ANISOU 3295 O3' U B 6 4961 4548 3678 1688 787 1514 O ATOM 3296 C2' U B 6 16.324 31.456 5.148 1.00 58.27 C ANISOU 3296 C2' U B 6 7993 7516 6632 1629 606 1473 C ATOM 3297 O2' U B 6 17.633 31.075 5.525 1.00 70.78 O ANISOU 3297 O2' U B 6 9615 9116 8163 1622 584 1483 O ATOM 3298 C1' U B 6 16.325 31.976 3.708 1.00 55.69 C ANISOU 3298 C1' U B 6 7611 7191 6356 1550 535 1459 C ATOM 3299 N1 U B 6 15.370 33.101 3.521 1.00 60.73 N ANISOU 3299 N1 U B 6 8250 7809 7017 1555 507 1432 N ATOM 3300 C2 U B 6 15.837 34.394 3.649 1.00 65.02 C ANISOU 3300 C2 U B 6 8833 8353 7519 1558 406 1410 C ATOM 3301 O2 U B 6 17.000 34.655 3.896 1.00 66.58 O ANISOU 3301 O2 U B 6 9067 8560 7669 1562 337 1416 O ATOM 3302 N3 U B 6 14.891 35.377 3.471 1.00 64.07 N ANISOU 3302 N3 U B 6 8706 8220 7416 1557 384 1382 N ATOM 3303 C4 U B 6 13.551 35.187 3.189 1.00 65.69 C ANISOU 3303 C4 U B 6 8880 8405 7674 1551 459 1377 C ATOM 3304 O4 U B 6 12.817 36.160 3.058 1.00 69.72 O ANISOU 3304 O4 U B 6 9395 8906 8190 1542 431 1351 O ATOM 3305 C5 U B 6 13.139 33.812 3.075 1.00 61.47 C ANISOU 3305 C5 U B 6 8309 7861 7187 1555 560 1407 C ATOM 3306 C6 U B 6 14.043 32.839 3.245 1.00 58.10 C ANISOU 3306 C6 U B 6 7878 7454 6744 1558 578 1432 C ATOM 3307 P A B 7 14.862 29.257 7.444 1.00 43.18 P ANISOU 3307 P A B 7 6071 5605 4729 1798 862 1524 P ATOM 3308 OP1 A B 7 13.708 30.193 7.369 1.00 43.28 O ANISOU 3308 OP1 A B 7 6094 5587 4765 1827 850 1519 O ATOM 3309 OP2 A B 7 15.873 29.408 8.517 1.00 53.49 O ANISOU 3309 OP2 A B 7 7451 6917 5956 1843 848 1515 O ATOM 3310 O5' A B 7 14.306 27.766 7.511 1.00 40.29 O ANISOU 3310 O5' A B 7 5631 5258 4420 1814 966 1556 O ATOM 3311 C5' A B 7 13.188 27.365 6.741 1.00 39.81 C ANISOU 3311 C5' A B 7 5500 5180 4446 1799 1001 1577 C ATOM 3312 C4' A B 7 13.316 25.899 6.383 1.00 36.40 C ANISOU 3312 C4' A B 7 4989 4780 4063 1774 1051 1603 C ATOM 3313 O4' A B 7 14.115 25.781 5.179 1.00 30.93 O ANISOU 3313 O4' A B 7 4270 4104 3377 1677 985 1591 O ATOM 3314 C3' A B 7 14.039 25.036 7.417 1.00 36.86 C ANISOU 3314 C3' A B 7 5054 4878 4072 1810 1103 1610 C ATOM 3315 O3' A B 7 13.121 24.566 8.397 1.00 40.53 O ANISOU 3315 O3' A B 7 5497 5337 4563 1908 1190 1639 O ATOM 3316 C2' A B 7 14.447 23.876 6.531 1.00 34.35 C ANISOU 3316 C2' A B 7 4660 4597 3794 1738 1104 1624 C ATOM 3317 O2' A B 7 13.333 23.057 6.262 1.00 38.50 O ANISOU 3317 O2' A B 7 5102 5114 4411 1769 1159 1661 O ATOM 3318 C1' A B 7 14.858 24.580 5.246 1.00 30.23 C ANISOU 3318 C1' A B 7 4145 4062 3277 1654 1011 1606 C ATOM 3319 N9 A B 7 16.283 24.889 5.196 1.00 30.85 N ANISOU 3319 N9 A B 7 4278 4165 3278 1601 948 1587 N ATOM 3320 C8 A B 7 16.888 26.097 5.425 1.00 33.44 C ANISOU 3320 C8 A B 7 4686 4474 3547 1598 882 1562 C ATOM 3321 N7 A B 7 18.197 26.046 5.293 1.00 30.91 N ANISOU 3321 N7 A B 7 4400 4174 3169 1548 833 1560 N ATOM 3322 C5 A B 7 18.463 24.731 4.953 1.00 32.67 C ANISOU 3322 C5 A B 7 4565 4439 3409 1509 871 1581 C ATOM 3323 C6 A B 7 19.655 24.028 4.673 1.00 30.57 C ANISOU 3323 C6 A B 7 4302 4213 3100 1445 850 1594 C ATOM 3324 N6 A B 7 20.869 24.593 4.696 1.00 27.42 N ANISOU 3324 N6 A B 7 3976 3810 2633 1409 784 1591 N ATOM 3325 N1 A B 7 19.552 22.714 4.372 1.00 26.13 N ANISOU 3325 N1 A B 7 3668 3694 2567 1421 894 1614 N ATOM 3326 C2 A B 7 18.345 22.150 4.349 1.00 30.25 C ANISOU 3326 C2 A B 7 4115 4214 3164 1463 952 1625 C ATOM 3327 N3 A B 7 17.155 22.703 4.603 1.00 27.94 N ANISOU 3327 N3 A B 7 3814 3877 2922 1527 981 1621 N ATOM 3328 C4 A B 7 17.288 24.006 4.894 1.00 29.34 C ANISOU 3328 C4 A B 7 4068 4018 3061 1544 939 1596 C ATOM 3329 P U B 8 13.529 24.393 9.932 1.00 47.75 P ANISOU 3329 P U B 8 6456 6271 5415 1996 1245 1635 P ATOM 3330 OP1 U B 8 12.426 23.707 10.644 1.00 54.17 O ANISOU 3330 OP1 U B 8 7215 7084 6284 2096 1335 1678 O ATOM 3331 OP2 U B 8 14.093 25.664 10.430 1.00 48.73 O ANISOU 3331 OP2 U B 8 6685 6371 5460 2016 1184 1602 O ATOM 3332 O5' U B 8 14.748 23.368 9.872 1.00 34.78 O ANISOU 3332 O5' U B 8 4789 4683 3745 1931 1255 1622 O ATOM 3333 C5' U B 8 15.266 22.957 11.126 1.00 33.20 C ANISOU 3333 C5' U B 8 4614 4506 3496 1990 1314 1612 C ATOM 3334 C4' U B 8 15.204 21.453 11.238 1.00 34.09 C ANISOU 3334 C4' U B 8 4628 4672 3651 1986 1389 1633 C ATOM 3335 O4' U B 8 16.194 20.877 10.350 1.00 31.97 O ANISOU 3335 O4' U B 8 4340 4442 3365 1867 1348 1621 O ATOM 3336 C3' U B 8 15.577 20.922 12.606 1.00 33.22 C ANISOU 3336 C3' U B 8 4526 4590 3504 2058 1467 1622 C ATOM 3337 O3' U B 8 14.438 20.963 13.469 1.00 38.72 O ANISOU 3337 O3' U B 8 5199 5270 4243 2189 1530 1653 O ATOM 3338 C2' U B 8 15.963 19.488 12.271 1.00 40.80 C ANISOU 3338 C2' U B 8 5393 5618 4492 1992 1505 1629 C ATOM 3339 O2' U B 8 14.838 18.646 12.119 1.00 42.24 O ANISOU 3339 O2' U B 8 5461 5818 4770 2039 1552 1675 O ATOM 3340 C1' U B 8 16.637 19.648 10.910 1.00 27.48 C ANISOU 3340 C1' U B 8 3718 3932 2790 1863 1415 1620 C ATOM 3341 N1 U B 8 18.130 19.638 10.957 1.00 28.77 N ANISOU 3341 N1 U B 8 3948 4117 2865 1781 1386 1586 N ATOM 3342 C2 U B 8 18.758 18.418 11.107 1.00 29.91 C ANISOU 3342 C2 U B 8 4042 4327 2996 1731 1431 1582 C ATOM 3343 O2 U B 8 18.124 17.379 11.223 1.00 34.44 O ANISOU 3343 O2 U B 8 4510 4944 3630 1758 1489 1604 O ATOM 3344 N3 U B 8 20.134 18.469 11.143 1.00 26.45 N ANISOU 3344 N3 U B 8 3678 3898 2473 1652 1404 1555 N ATOM 3345 C4 U B 8 20.918 19.609 11.019 1.00 27.92 C ANISOU 3345 C4 U B 8 3979 4033 2597 1625 1331 1539 C ATOM 3346 O4 U B 8 22.144 19.519 11.051 1.00 26.42 O ANISOU 3346 O4 U B 8 3851 3850 2339 1554 1311 1524 O ATOM 3347 C5 U B 8 20.187 20.844 10.870 1.00 31.59 C ANISOU 3347 C5 U B 8 4480 4436 3086 1686 1282 1543 C ATOM 3348 C6 U B 8 18.843 20.816 10.838 1.00 29.72 C ANISOU 3348 C6 U B 8 4177 4192 2924 1755 1313 1564 C ATOM 3349 P C B 9 14.621 21.410 14.992 1.00 61.28 P ANISOU 3349 P C B 9 8128 8114 7044 2309 1575 1636 P ATOM 3350 OP1 C B 9 13.277 21.662 15.548 1.00 58.46 O ANISOU 3350 OP1 C B 9 7748 7729 6734 2440 1614 1683 O ATOM 3351 OP2 C B 9 15.670 22.453 15.051 1.00 70.98 O ANISOU 3351 OP2 C B 9 9476 9309 8185 2271 1502 1591 O ATOM 3352 O5' C B 9 15.161 20.082 15.694 1.00116.70 O ANISOU 3352 O5' C B 9 15080 15196 14066 2316 1663 1626 O ATOM 3353 C5' C B 9 14.280 18.965 15.752 1.00119.17 C ANISOU 3353 C5' C B 9 15264 15550 14466 2360 1732 1671 C ATOM 3354 C4' C B 9 14.735 17.941 16.773 1.00121.09 C ANISOU 3354 C4' C B 9 15454 15852 14704 2402 1822 1654 C ATOM 3355 O4' C B 9 16.094 17.527 16.481 1.00121.72 O ANISOU 3355 O4' C B 9 15558 15967 14722 2275 1807 1604 O ATOM 3356 C3' C B 9 14.782 18.449 18.205 1.00121.55 C ANISOU 3356 C3' C B 9 15577 15886 14721 2537 1873 1639 C ATOM 3357 O3' C B 9 13.498 18.340 18.802 1.00119.21 O ANISOU 3357 O3' C B 9 15219 15583 14492 2682 1925 1697 O ATOM 3358 C2' C B 9 15.778 17.475 18.824 1.00124.40 C ANISOU 3358 C2' C B 9 15906 16306 15053 2503 1940 1594 C ATOM 3359 O2' C B 9 15.189 16.239 19.174 1.00126.80 O ANISOU 3359 O2' C B 9 16067 16675 15434 2553 2022 1625 O ATOM 3360 C1' C B 9 16.781 17.270 17.690 1.00123.08 C ANISOU 3360 C1' C B 9 15759 16158 14847 2323 1876 1564 C ATOM 3361 N1 C B 9 17.977 18.163 17.785 1.00122.61 N ANISOU 3361 N1 C B 9 15842 16053 14691 2269 1823 1514 N ATOM 3362 C2 C B 9 19.216 17.608 18.123 1.00117.83 C ANISOU 3362 C2 C B 9 15264 15477 14029 2194 1855 1467 C ATOM 3363 O2 C B 9 19.286 16.391 18.327 1.00114.87 O ANISOU 3363 O2 C B 9 14790 15175 13681 2170 1927 1462 O ATOM 3364 N3 C B 9 20.301 18.417 18.210 1.00116.54 N ANISOU 3364 N3 C B 9 15233 15262 13784 2150 1803 1430 N ATOM 3365 C4 C B 9 20.176 19.726 17.978 1.00118.76 C ANISOU 3365 C4 C B 9 15608 15473 14044 2181 1717 1438 C ATOM 3366 N4 C B 9 21.272 20.485 18.077 1.00117.87 N ANISOU 3366 N4 C B 9 15619 15307 13859 2143 1660 1408 N ATOM 3367 C5 C B 9 18.920 20.313 17.634 1.00122.47 C ANISOU 3367 C5 C B 9 16046 15920 14566 2251 1685 1479 C ATOM 3368 C6 C B 9 17.858 19.504 17.550 1.00123.93 C ANISOU 3368 C6 C B 9 16109 16149 14828 2291 1742 1517 C TER 3369 C B 9 HETATM 3370 O HOH A 1 25.528 39.006 -8.527 1.00 21.13 O HETATM 3371 O HOH A 2 4.251 48.035 -24.567 1.00 20.40 O HETATM 3372 O HOH A 3 -0.792 62.837 -25.078 1.00 23.71 O HETATM 3373 O HOH A 4 3.227 61.712 -22.474 1.00 23.01 O HETATM 3374 O HOH A 5 -1.035 57.483 -9.567 1.00 22.16 O HETATM 3375 O HOH A 6 41.525 20.882 1.910 1.00 28.41 O HETATM 3376 O HOH A 7 4.263 39.441 -15.001 1.00 24.47 O HETATM 3377 O HOH A 8 32.643 28.365 -5.439 1.00 23.25 O HETATM 3378 O HOH A 9 36.094 39.665 -8.574 1.00 24.25 O HETATM 3379 O HOH A 10 7.804 50.663 -5.949 1.00 27.53 O HETATM 3380 O HOH A 11 35.075 15.347 21.344 1.00 21.73 O HETATM 3381 O HOH A 12 -5.193 52.848 -1.117 1.00 23.31 O HETATM 3382 O HOH A 13 -3.310 53.994 -5.133 1.00 19.39 O HETATM 3383 O HOH A 14 7.012 52.977 -6.852 1.00 22.66 O HETATM 3384 O HOH A 15 21.398 27.494 1.824 1.00 35.90 O HETATM 3385 O HOH A 16 27.175 -0.048 20.625 1.00 23.47 O HETATM 3386 O HOH A 17 33.627 30.174 -3.403 1.00 31.47 O HETATM 3387 O HOH A 18 -3.096 53.659 -7.978 1.00 24.54 O HETATM 3388 O HOH A 19 -3.767 44.967 -7.372 1.00 29.37 O HETATM 3389 O HOH A 20 30.897 17.272 10.279 1.00 25.18 O HETATM 3390 O HOH A 21 -11.076 56.284 -17.203 1.00 24.43 O HETATM 3391 O HOH A 22 25.452 29.503 -1.122 1.00 27.64 O HETATM 3392 O HOH A 23 -7.726 67.887 -12.169 1.00 26.88 O HETATM 3393 O HOH A 24 -5.823 60.748 -16.757 1.00 25.84 O HETATM 3394 O HOH A 25 24.579 20.711 7.703 1.00 30.29 O HETATM 3395 O HOH A 26 35.514 25.109 3.985 1.00 27.37 O HETATM 3396 O HOH A 27 -2.173 47.276 -6.874 1.00 25.01 O HETATM 3397 O HOH A 28 1.651 56.940 -10.040 1.00 24.46 O HETATM 3398 O HOH A 29 32.532 16.934 16.026 1.00 29.38 O HETATM 3399 O HOH A 30 2.282 59.062 -22.537 1.00 22.03 O HETATM 3400 O HOH A 31 34.568 6.121 7.660 1.00 34.66 O HETATM 3401 O HOH A 32 42.779 17.397 10.874 1.00 34.08 O HETATM 3402 O HOH A 33 36.926 18.453 12.562 1.00 22.67 O HETATM 3403 O HOH A 34 37.754 26.357 -10.359 1.00 27.65 O HETATM 3404 O HOH A 35 -12.611 58.563 -5.337 1.00 26.63 O HETATM 3405 O HOH A 36 22.781 51.231 -9.920 1.00 37.84 O HETATM 3406 O HOH A 37 -3.975 51.004 -7.967 1.00 26.90 O HETATM 3407 O HOH A 38 30.699 40.043 -13.113 1.00 21.83 O HETATM 3408 O HOH A 39 27.521 30.908 -2.460 1.00 30.76 O HETATM 3409 O HOH A 40 32.410 20.702 -14.115 1.00 30.24 O HETATM 3410 O HOH A 41 -0.378 40.428 -14.323 1.00 24.27 O HETATM 3411 O HOH A 42 26.619 0.384 14.094 1.00 24.78 O HETATM 3412 O HOH A 43 26.725 32.712 -4.423 1.00 26.17 O HETATM 3413 O HOH A 44 18.009 29.713 0.361 1.00 26.10 O HETATM 3414 O HOH A 45 24.014 -0.853 17.423 1.00 32.31 O HETATM 3415 O HOH A 46 17.344 48.533 -6.634 1.00 32.23 O HETATM 3416 O HOH A 47 11.455 52.517 -27.060 1.00 29.98 O HETATM 3417 O HOH A 48 6.118 29.379 -12.171 1.00 27.48 O HETATM 3418 O HOH A 49 38.331 31.213 -3.947 1.00 29.98 O HETATM 3419 O HOH A 50 4.009 33.222 -13.376 1.00 28.92 O HETATM 3420 O HOH A 51 37.935 28.776 -9.177 1.00 35.00 O HETATM 3421 O HOH A 52 37.364 14.299 20.286 1.00 28.34 O HETATM 3422 O HOH A 53 33.144 -1.072 17.932 1.00 30.03 O HETATM 3423 O HOH A 54 -7.398 58.301 -16.930 1.00 28.62 O HETATM 3424 O HOH A 55 18.859 54.961 -14.152 1.00 27.19 O HETATM 3425 O HOH A 56 23.382 25.719 1.874 1.00 32.16 O HETATM 3426 O HOH A 57 10.258 19.960 -2.594 1.00 32.82 O HETATM 3427 O HOH A 58 7.507 26.369 -7.189 1.00 29.91 O HETATM 3428 O HOH A 59 -1.441 54.965 -25.588 1.00 38.05 O HETATM 3429 O HOH A 60 43.895 16.923 6.059 1.00 34.64 O HETATM 3430 O HOH A 62 40.268 4.308 12.460 1.00 29.71 O HETATM 3431 O HOH A 63 6.158 64.078 -24.536 1.00 29.79 O HETATM 3432 O HOH A 64 12.374 55.215 -26.943 1.00 33.21 O HETATM 3433 O HOH A 65 30.373 36.669 -5.430 1.00 31.43 O HETATM 3434 O HOH A 66 29.332 32.204 -0.821 1.00 39.92 O HETATM 3435 O HOH A 67 1.250 49.354 -1.805 1.00 29.66 O HETATM 3436 O HOH A 68 -5.328 52.613 -16.212 1.00 31.14 O HETATM 3437 O HOH A 69 14.447 10.390 6.466 1.00 28.02 O HETATM 3438 O HOH A 70 27.200 11.133 -11.424 1.00 46.42 O HETATM 3439 O HOH A 71 3.644 57.417 -25.323 1.00 26.50 O HETATM 3440 O HOH A 72 41.310 5.249 14.988 1.00 37.58 O HETATM 3441 O HOH A 73 6.560 59.542 -6.290 1.00 42.16 O HETATM 3442 O HOH A 74 35.296 19.737 10.843 1.00 29.64 O HETATM 3443 O HOH A 75 13.668 10.116 10.969 1.00 29.97 O HETATM 3444 O HOH A 76 -3.420 68.438 -21.800 1.00 38.89 O HETATM 3445 O HOH A 77 40.860 6.397 17.345 1.00 46.24 O HETATM 3446 O HOH A 78 33.913 29.653 -7.233 1.00 42.63 O HETATM 3447 O HOH A 79 15.571 10.536 -0.283 1.00 32.46 O HETATM 3448 O HOH A 80 45.972 8.084 7.104 1.00 28.48 O HETATM 3449 O HOH A 81 36.517 30.195 -11.098 1.00 25.47 O HETATM 3450 O HOH A 82 35.511 2.468 25.184 1.00 31.17 O HETATM 3451 O HOH A 83 -5.886 54.133 -3.729 1.00 37.20 O HETATM 3452 O HOH A 84 30.463 57.379 -17.869 1.00 40.33 O HETATM 3453 O HOH A 85 40.836 38.140 -8.837 1.00 31.71 O HETATM 3454 O HOH A 86 32.684 17.117 -10.617 1.00 42.98 O HETATM 3455 O HOH A 87 37.632 2.927 13.338 1.00 37.27 O HETATM 3456 O HOH A 88 44.327 5.077 6.306 1.00 29.23 O HETATM 3457 O HOH A 90 -4.482 62.637 -28.811 1.00 28.46 O HETATM 3458 O HOH A 91 20.836 31.871 -0.479 1.00 44.18 O HETATM 3459 O HOH A 92 12.126 65.004 -23.403 1.00 37.33 O HETATM 3460 O HOH A 93 32.943 6.326 28.918 1.00 30.33 O HETATM 3461 O HOH A 94 9.168 40.341 -2.792 1.00 37.59 O HETATM 3462 O HOH A 95 29.892 -1.115 4.526 1.00 34.45 O HETATM 3463 O HOH A 96 27.933 42.510 -6.852 1.00 34.20 O HETATM 3464 O HOH A 97 36.973 25.828 -2.248 1.00 33.12 O HETATM 3465 O HOH A 98 25.092 47.087 -7.401 1.00 34.06 O HETATM 3466 O HOH A 100 29.402 44.497 -16.964 1.00 32.26 O HETATM 3467 O HOH A 101 35.061 4.948 10.030 1.00 31.55 O HETATM 3468 O HOH A 103 -5.731 48.609 -13.059 1.00 29.46 O HETATM 3469 O HOH A 105 3.677 33.076 -6.627 1.00 39.88 O HETATM 3470 O HOH A 106 3.516 61.883 4.569 1.00 41.81 O HETATM 3471 O HOH A 107 16.644 47.521 -28.032 1.00 47.64 O HETATM 3472 O HOH A 108 22.941 39.646 -3.760 1.00 45.94 O HETATM 3473 O HOH A 109 36.691 17.154 17.374 1.00 34.82 O HETATM 3474 O HOH A 110 42.134 3.038 19.180 1.00 28.18 O HETATM 3475 O HOH A 111 15.034 21.157 4.840 1.00 32.46 O HETATM 3476 O HOH A 112 6.384 49.914 -28.667 1.00 37.63 O HETATM 3477 O HOH A 114 43.208 10.325 19.527 1.00 44.66 O HETATM 3478 O HOH A 115 9.054 55.009 -6.177 1.00 40.20 O HETATM 3479 O HOH A 116 30.388 -3.192 20.830 1.00 53.34 O HETATM 3480 O HOH A 117 24.608 49.997 -16.905 1.00 35.09 O HETATM 3481 O HOH A 119 24.544 29.185 -23.117 1.00 40.68 O HETATM 3482 O HOH A 120 15.407 2.882 19.571 1.00 47.27 O HETATM 3483 O HOH A 122 38.707 14.304 22.590 1.00 34.98 O HETATM 3484 O HOH A 123 -10.936 57.950 -3.038 1.00 33.79 O HETATM 3485 O HOH A 124 35.559 17.918 20.131 1.00 46.82 O HETATM 3486 O HOH A 126 28.219 50.519 -7.554 1.00 43.86 O HETATM 3487 O HOH A 127 -4.378 62.458 -22.370 1.00 35.86 O HETATM 3488 O HOH A 128 0.891 52.806 -30.049 1.00 38.85 O HETATM 3489 O HOH A 129 -6.423 70.608 -15.729 1.00 33.71 O HETATM 3490 O HOH A 130 31.829 40.228 -15.620 1.00 37.34 O HETATM 3491 O HOH A 131 39.216 11.019 8.463 1.00 31.11 O HETATM 3492 O HOH A 132 9.494 22.611 -6.093 1.00 31.52 O HETATM 3493 O HOH A 133 31.571 46.963 -7.776 1.00 45.69 O HETATM 3494 O HOH A 134 15.862 40.114 -6.854 1.00 30.78 O HETATM 3495 O HOH A 135 26.055 17.780 15.228 1.00 37.25 O HETATM 3496 O HOH A 136 20.330 1.580 5.943 1.00 38.18 O HETATM 3497 O HOH A 137 25.575 27.394 1.474 1.00 48.31 O HETATM 3498 O HOH A 139 17.554 25.384 9.105 1.00 30.47 O HETATM 3499 O HOH A 141 41.930 12.422 24.706 1.00 34.73 O HETATM 3500 O HOH A 142 -0.561 47.785 -23.395 1.00 48.00 O HETATM 3501 O HOH A 143 10.648 17.249 -8.629 1.00 42.12 O HETATM 3502 O HOH A 145 12.581 15.360 -1.229 1.00 33.14 O HETATM 3503 O HOH A 146 12.971 44.530 -26.331 1.00 37.28 O HETATM 3504 O HOH A 147 15.868 70.747 -3.725 1.00 51.75 O HETATM 3505 O HOH A 149 2.938 43.992 -8.763 1.00 29.41 O HETATM 3506 O HOH A 150 -9.435 55.030 -23.525 1.00 49.02 O HETATM 3507 O HOH A 152 19.586 22.292 14.356 1.00 38.08 O HETATM 3508 O HOH A 153 -6.333 60.699 -29.788 1.00 32.98 O HETATM 3509 O HOH A 154 17.682 56.873 -8.155 1.00 49.29 O HETATM 3510 O HOH A 155 8.438 19.964 -7.217 1.00 49.05 O HETATM 3511 O HOH A 156 0.095 43.909 -20.131 1.00 35.94 O HETATM 3512 O HOH A 157 40.281 30.751 -21.727 1.00 42.40 O HETATM 3513 O HOH A 158 -3.448 62.606 -26.061 1.00 32.18 O HETATM 3514 O HOH A 161 12.975 37.240 -24.543 1.00 52.44 O HETATM 3515 O HOH A 162 9.108 71.316 -11.898 1.00 53.14 O HETATM 3516 O HOH A 163 22.962 9.156 -6.863 1.00 37.69 O HETATM 3517 O HOH A 576 19.021 -1.119 16.107 1.00 52.89 O HETATM 3518 O HOH A 577 9.468 46.853 -6.519 1.00 42.21 O HETATM 3519 O HOH A 578 6.286 33.885 -17.951 1.00 41.03 O HETATM 3520 O HOH A 579 26.689 -2.177 5.335 1.00 40.81 O HETATM 3521 O HOH A 580 28.386 2.417 10.758 1.00 38.62 O HETATM 3522 O HOH A 581 45.207 1.971 9.114 1.00 53.08 O HETATM 3523 O HOH A 582 18.918 5.412 -9.636 1.00 55.88 O HETATM 3524 O HOH A 583 6.137 71.433 -15.402 1.00 40.75 O HETATM 3525 O HOH A 584 38.584 15.333 18.150 1.00 33.68 O HETATM 3526 O HOH A 585 3.016 59.788 -29.788 1.00 29.16 O HETATM 3527 O HOH A 586 2.382 69.067 -5.512 1.00 37.83 O HETATM 3528 O HOH A 587 -6.330 55.744 -17.055 1.00 35.24 O HETATM 3529 O HOH A 588 11.542 53.804 -6.584 1.00 46.51 O HETATM 3530 O HOH A 589 29.710 -1.465 1.421 1.00 56.13 O HETATM 3531 O HOH A 590 36.302 2.611 9.542 1.00 47.52 O HETATM 3532 O HOH A 591 39.459 15.498 -6.113 1.00 38.65 O HETATM 3533 O HOH A 592 32.093 34.852 -4.120 1.00 33.37 O HETATM 3534 O HOH A 593 26.862 -0.397 16.795 1.00 36.21 O HETATM 3535 O HOH A 594 38.365 3.062 2.799 1.00 39.91 O HETATM 3536 O HOH A 595 32.045 20.829 -17.007 1.00 49.79 O HETATM 3537 O HOH A 596 30.723 15.911 27.757 1.00 47.22 O HETATM 3538 O HOH A 597 35.092 18.073 15.394 1.00 46.11 O HETATM 3539 O HOH A 598 8.002 29.689 -17.359 1.00 41.83 O HETATM 3540 O HOH A 599 23.617 52.691 -14.490 1.00 45.45 O HETATM 3541 O HOH A 600 30.797 8.877 29.471 1.00 39.14 O HETATM 3542 O HOH A 601 -6.169 46.253 -14.864 1.00 48.07 O HETATM 3543 O HOH A 602 23.989 24.623 -21.826 1.00 40.49 O HETATM 3544 O HOH A 603 7.905 21.376 -1.962 1.00 49.47 O HETATM 3545 O HOH A 604 7.513 68.451 -25.004 1.00 40.11 O HETATM 3546 O HOH A 605 22.870 48.760 -7.223 1.00 49.48 O HETATM 3547 O HOH A 606 34.066 24.196 -20.794 1.00 53.45 O HETATM 3548 O HOH A 607 43.129 17.830 15.069 1.00 33.95 O HETATM 3549 O HOH A 608 22.433 55.254 -14.175 1.00 47.70 O HETATM 3550 O HOH A 609 15.681 70.861 -19.136 1.00 33.95 O HETATM 3551 O HOH A 610 47.256 10.087 8.792 1.00 47.71 O HETATM 3552 O HOH A 611 44.540 11.576 3.322 1.00 44.66 O HETATM 3553 O HOH A 612 1.520 48.157 -25.451 1.00 34.35 O HETATM 3554 O HOH A 613 28.132 16.249 19.392 1.00 47.70 O HETATM 3555 O HOH A 614 16.523 6.199 9.275 1.00 44.05 O HETATM 3556 O HOH A 615 21.182 -3.855 19.276 1.00 55.14 O HETATM 3557 O HOH A 616 13.478 51.422 -28.733 1.00 41.89 O HETATM 3558 O HOH A 617 23.047 16.911 23.607 1.00 41.99 O HETATM 3559 O HOH A 618 46.254 12.724 8.412 1.00 37.22 O HETATM 3560 O HOH A 619 -14.047 61.370 -29.489 1.00 42.23 O HETATM 3561 O HOH A 620 -6.414 68.584 -5.345 1.00 53.49 O HETATM 3562 O HOH A 621 35.686 25.416 -18.884 1.00 29.58 O HETATM 3563 O HOH A 622 42.016 13.821 21.447 1.00 44.40 O HETATM 3564 O HOH A 623 26.272 19.467 -17.695 1.00 42.34 O HETATM 3565 O HOH A 624 12.838 13.610 3.373 1.00 33.47 O HETATM 3566 O HOH A 625 38.124 37.160 -18.695 1.00 38.34 O HETATM 3567 O HOH A 626 35.548 17.281 -9.656 1.00 47.69 O HETATM 3568 O HOH A 627 -5.623 71.578 -8.986 1.00 53.13 O HETATM 3569 O HOH A 628 20.902 7.686 -4.717 1.00 34.05 O HETATM 3570 O HOH A 629 0.510 57.332 -25.626 1.00 30.51 O HETATM 3571 O HOH A 630 25.730 45.165 -23.068 1.00 56.95 O HETATM 3572 O HOH A 631 15.765 69.830 -22.222 1.00 44.27 O HETATM 3573 O HOH A 632 6.712 57.964 -1.959 1.00 47.75 O HETATM 3574 O HOH A 633 25.655 -4.912 17.461 1.00 49.23 O HETATM 3575 O HOH A 634 36.081 27.569 -4.081 1.00 41.25 O HETATM 3576 O HOH A 635 35.373 28.912 -1.826 1.00 36.14 O HETATM 3577 O HOH A 636 28.667 28.441 -25.508 1.00 47.21 O HETATM 3578 O HOH A 637 17.763 29.683 -23.097 1.00 38.86 O HETATM 3579 O HOH A 638 33.997 31.361 -9.516 1.00 45.30 O HETATM 3580 O HOH A 639 22.944 22.736 7.033 1.00 37.11 O HETATM 3581 O HOH A 640 33.343 12.003 26.792 1.00 51.39 O HETATM 3582 O HOH A 641 4.523 45.422 -25.890 1.00 41.05 O HETATM 3583 O HOH A 642 -4.843 71.858 -11.576 1.00 43.94 O HETATM 3584 O HOH A 643 11.788 13.495 -3.213 1.00 50.63 O HETATM 3585 O HOH A 644 28.378 -2.606 27.604 1.00 45.41 O HETATM 3586 O HOH A 645 17.032 42.985 -7.090 1.00 51.92 O HETATM 3587 O HOH A 646 9.684 50.815 -3.868 1.00 45.50 O HETATM 3588 O HOH A 647 14.275 7.184 10.586 1.00 53.31 O HETATM 3589 O HOH A 648 -10.810 64.384 -6.187 1.00 39.11 O HETATM 3590 O HOH A 649 18.650 71.475 -9.523 1.00 47.56 O HETATM 3591 O HOH A 650 31.391 44.521 -5.653 1.00 32.58 O HETATM 3592 O HOH A 651 34.221 28.882 -18.329 1.00 38.18 O HETATM 3593 O HOH A 652 -0.768 64.625 -1.382 1.00 32.46 O HETATM 3594 O HOH A 653 13.864 7.923 15.282 1.00 32.74 O HETATM 3595 O HOH A 654 12.468 9.027 20.441 1.00 36.50 O HETATM 3596 O HOH A 655 11.004 62.495 -22.796 1.00 42.59 O HETATM 3597 O HOH A 656 44.312 16.606 8.673 1.00 34.78 O HETATM 3598 O HOH A 657 22.727 69.347 -17.981 1.00 37.02 O HETATM 3599 O HOH A 658 43.131 7.798 17.580 1.00 48.12 O HETATM 3600 O HOH A 659 27.728 -3.057 16.435 1.00 53.08 O HETATM 3601 O HOH A 660 16.615 22.472 -24.088 1.00 46.97 O HETATM 3602 O HOH A 661 29.218 42.070 -15.833 1.00 40.95 O HETATM 3603 O HOH A 662 11.412 31.836 -5.252 1.00 45.90 O HETATM 3604 O HOH A 663 16.751 19.819 7.154 1.00 40.67 O HETATM 3605 O HOH A 664 11.188 46.553 -8.505 1.00 57.44 O HETATM 3606 O HOH A 665 6.044 57.333 -4.649 1.00 40.29 O HETATM 3607 O HOH A 666 35.053 39.026 -16.065 1.00 42.57 O HETATM 3608 O HOH A 667 9.504 53.064 -28.938 1.00 41.13 O HETATM 3609 O HOH A 668 12.174 17.382 -6.035 1.00 38.67 O HETATM 3610 O HOH A 669 0.610 69.410 -8.047 1.00 49.65 O HETATM 3611 O HOH A 670 -7.034 60.654 -32.397 1.00 43.27 O HETATM 3612 O HOH A 671 26.007 52.210 -15.597 1.00 44.02 O HETATM 3613 O HOH A 672 3.062 34.970 -15.326 1.00 42.38 O HETATM 3614 O HOH A 673 18.622 7.946 -7.874 1.00 41.37 O HETATM 3615 O HOH A 674 -10.147 63.337 -3.638 1.00 47.84 O HETATM 3616 O HOH A 675 26.474 22.690 6.713 1.00 38.61 O HETATM 3617 O HOH A 676 7.450 24.457 -14.629 1.00 46.76 O HETATM 3618 O HOH A 677 -3.774 65.670 -2.487 1.00 48.03 O HETATM 3619 O HOH A 678 26.211 26.408 -21.869 1.00 48.19 O HETATM 3620 O HOH A 679 41.152 10.202 2.328 1.00 43.57 O HETATM 3621 O HOH A 680 26.045 -4.517 27.816 1.00 56.89 O HETATM 3622 O HOH A 681 13.517 73.955 -3.841 1.00 57.08 O HETATM 3623 O HOH A 682 28.163 19.890 10.958 1.00 39.23 O HETATM 3624 O HOH A 683 -6.872 67.124 -16.640 1.00 38.12 O HETATM 3625 O HOH A 684 22.413 25.704 -23.926 1.00 50.52 O HETATM 3626 O HOH A 685 11.279 16.007 2.821 1.00 42.35 O HETATM 3627 O HOH A 686 33.576 -2.383 20.460 1.00 44.70 O HETATM 3628 O HOH A 687 10.795 64.797 -3.374 1.00 44.87 O HETATM 3629 O HOH A 688 20.942 0.785 3.202 1.00 49.88 O HETATM 3630 O HOH A 689 40.383 3.063 0.756 1.00 45.15 O HETATM 3631 O HOH A 690 19.460 58.229 -25.575 1.00 48.89 O HETATM 3632 O HOH A 691 37.829 29.789 -1.557 1.00 38.30 O HETATM 3633 O HOH A 692 5.546 31.646 -16.520 1.00 45.89 O HETATM 3634 O HOH A 693 12.990 1.144 21.706 1.00 55.95 O HETATM 3635 O HOH A 694 39.246 27.593 -2.257 1.00 44.69 O HETATM 3636 O HOH A 695 -0.532 63.283 1.123 1.00 50.19 O HETATM 3637 O HOH A 696 32.477 10.299 -6.271 1.00 48.87 O HETATM 3638 O HOH A 697 9.980 56.729 -28.032 1.00 44.25 O HETATM 3639 O HOH A 698 38.231 -2.863 13.231 1.00 42.21 O HETATM 3640 O HOH A 699 23.586 11.038 -14.132 1.00 42.96 O HETATM 3641 O HOH A 700 13.684 18.562 -19.449 1.00 54.80 O HETATM 3642 O HOH A 701 28.587 34.952 -3.687 1.00 43.62 O HETATM 3643 O HOH A 702 7.589 60.529 -31.439 1.00 47.93 O HETATM 3644 O HOH A 703 11.941 48.860 -7.128 1.00 42.78 O HETATM 3645 O HOH A 704 28.570 18.658 13.803 1.00 51.25 O HETATM 3646 O HOH A 705 19.888 12.587 27.316 1.00 50.15 O HETATM 3647 O HOH A 706 -3.263 61.798 -31.191 1.00 40.85 O HETATM 3648 O HOH A 707 40.899 3.445 8.670 1.00 41.85 O HETATM 3649 O HOH A 708 22.640 8.946 31.209 1.00 51.63 O HETATM 3650 O HOH A 709 11.234 34.514 -23.614 1.00 39.94 O HETATM 3651 O HOH A 710 10.892 71.486 -20.305 1.00 47.51 O HETATM 3652 O HOH A 711 44.252 19.173 12.505 1.00 47.14 O HETATM 3653 O HOH A 712 27.275 38.524 -6.179 1.00 52.41 O HETATM 3654 O HOH A 713 18.389 3.755 6.064 1.00 46.93 O HETATM 3655 O HOH A 714 37.230 29.084 -5.914 1.00 47.98 O HETATM 3656 O HOH A 715 -6.454 71.943 -6.424 1.00 55.94 O HETATM 3657 O HOH A 716 24.877 56.131 -20.675 1.00 51.49 O HETATM 3658 O HOH A 717 21.868 19.319 -20.068 1.00 57.80 O HETATM 3659 O HOH A 718 11.150 42.815 -27.912 1.00 55.30 O HETATM 3660 O HOH A 719 -2.517 64.221 -22.965 1.00 50.21 O HETATM 3661 O HOH A 720 18.713 23.854 11.852 1.00 39.55 O HETATM 3662 O HOH A 721 41.437 9.363 -0.383 1.00 45.18 O HETATM 3663 O HOH A 722 44.920 18.767 4.791 1.00 46.00 O HETATM 3664 O HOH A 723 -12.358 53.821 -17.030 1.00 45.23 O HETATM 3665 O HOH A 724 5.549 60.710 -1.256 1.00 53.90 O HETATM 3666 O HOH A 725 -7.669 56.488 -1.134 1.00 58.33 O HETATM 3667 O HOH A 726 25.716 53.086 -9.468 1.00 50.42 O HETATM 3668 O HOH A 727 21.646 42.977 -7.427 1.00 49.65 O HETATM 3669 O HOH A 728 5.064 28.020 -14.573 1.00 52.70 O HETATM 3670 O HOH A 729 28.344 68.873 -19.091 1.00 54.06 O HETATM 3671 O HOH A 730 43.143 38.259 -10.761 1.00 45.87 O HETATM 3672 O HOH A 731 23.987 37.998 -23.213 1.00 51.33 O HETATM 3673 O HOH A 732 19.019 40.551 -5.447 1.00 50.18 O HETATM 3674 O HOH A 733 -9.772 53.176 -15.072 1.00 52.27 O HETATM 3675 O HOH A 734 -4.433 57.213 1.046 1.00 51.97 O HETATM 3676 O HOH A 735 25.173 53.280 -22.527 1.00 54.30 O HETATM 3677 O HOH A 736 34.951 -3.301 23.754 1.00 52.39 O HETATM 3678 O HOH A 737 10.385 20.149 -12.557 1.00 49.87 O HETATM 3679 O HOH A 738 -4.322 45.890 -17.883 1.00 51.51 O HETATM 3680 O HOH A 739 24.732 65.478 -9.591 1.00 50.98 O HETATM 3681 O HOH A 740 24.552 20.316 -20.044 1.00 54.80 O HETATM 3682 O HOH A 741 -2.365 43.792 -18.671 1.00 54.14 O HETATM 3683 O HOH A 742 32.811 6.622 -5.226 1.00 49.02 O HETATM 3684 O HOH A 743 14.287 7.513 28.414 1.00 51.96 O HETATM 3685 O HOH A 744 0.972 60.854 0.691 1.00 51.05 O HETATM 3686 O HOH A 745 1.079 60.703 3.673 1.00 44.31 O HETATM 3687 O HOH A 746 29.916 22.317 9.719 1.00 49.31 O HETATM 3688 O HOH A 747 27.931 32.269 -24.789 1.00 55.17 O HETATM 3689 O HOH A 748 11.959 14.415 -6.092 1.00 54.25 O HETATM 3690 O HOH A 749 -5.549 48.868 -7.125 1.00 36.74 O HETATM 3691 O HOH A 750 13.117 15.949 -12.829 1.00 40.96 O HETATM 3692 O HOH A 751 15.837 29.381 -25.128 1.00 55.72 O HETATM 3693 O HOH A 752 9.496 69.136 -20.106 1.00 50.62 O HETATM 3694 O HOH A 753 29.133 39.251 2.102 1.00 54.50 O HETATM 3695 O HOH A 754 38.455 2.856 7.452 1.00 40.62 O HETATM 3696 O HOH A 755 27.327 16.032 -16.943 1.00 55.14 O HETATM 3697 O HOH A 756 14.516 12.175 -8.508 1.00 44.12 O HETATM 3698 O HOH A 757 5.417 53.619 -3.964 1.00 55.50 O HETATM 3699 O HOH A 758 42.593 6.727 -0.514 1.00 49.87 O HETATM 3700 O HOH A 759 11.595 17.709 -11.225 1.00 49.80 O HETATM 3701 O HOH A 760 32.556 19.369 11.892 1.00 57.91 O HETATM 3702 O HOH A 761 37.543 6.749 29.640 1.00 56.61 O HETATM 3703 O HOH A 762 23.550 71.480 -15.588 1.00 55.60 O HETATM 3704 O HOH A 763 20.009 42.529 -26.280 1.00 48.87 O HETATM 3705 O HOH A 764 27.915 46.359 -7.206 1.00 56.01 O HETATM 3706 O HOH A 765 22.450 32.044 -28.154 1.00 52.87 O HETATM 3707 O HOH A 766 35.810 -0.150 26.540 1.00 50.44 O HETATM 3708 O HOH A 767 33.758 -0.558 2.956 1.00 54.12 O HETATM 3709 O HOH A 768 13.030 5.929 18.293 1.00 57.07 O HETATM 3710 O HOH A 769 14.656 9.402 -2.746 1.00 55.32 O HETATM 3711 O HOH A 770 32.325 17.773 -14.682 1.00 50.16 O HETATM 3712 O HOH A 771 22.150 23.309 13.567 1.00 53.29 O HETATM 3713 O HOH A 772 38.010 20.225 14.617 1.00 53.46 O HETATM 3714 O HOH A 773 31.183 9.648 -8.652 1.00 50.80 O HETATM 3715 O HOH A 774 23.796 70.379 -12.788 1.00 60.67 O HETATM 3716 O HOH A 775 14.276 16.085 -18.275 1.00 59.20 O HETATM 3717 O HOH A 776 21.282 -1.468 12.554 1.00 53.30 O HETATM 3718 O HOH A 777 -4.658 59.031 -31.473 1.00 55.06 O HETATM 3719 O HOH A 778 32.379 -1.489 11.737 1.00 44.32 O HETATM 3720 O HOH A 779 23.112 17.976 18.956 1.00 51.67 O HETATM 3721 O HOH A 780 43.306 19.771 3.055 1.00 46.20 O HETATM 3722 O HOH A 781 7.119 52.551 -27.885 1.00 41.97 O HETATM 3723 O HOH A 782 25.526 -1.462 7.819 1.00 51.90 O HETATM 3724 O HOH A 783 29.459 15.982 8.156 1.00 40.10 O HETATM 3725 O HOH A 784 -2.299 41.278 -7.383 1.00 53.62 O HETATM 3726 O HOH A 785 25.076 33.999 -2.522 1.00 55.81 O HETATM 3727 O HOH A 786 29.716 -3.074 18.160 1.00 50.77 O HETATM 3728 O HOH A 787 6.230 30.195 -3.238 1.00 51.69 O HETATM 3729 O HOH A 788 12.324 12.568 5.997 1.00 57.87 O HETATM 3730 O HOH A 789 16.819 11.979 -17.392 1.00 51.45 O HETATM 3731 O HOH A 790 23.603 16.417 -18.521 1.00 52.05 O HETATM 3732 O HOH A 791 27.643 25.969 8.425 1.00 52.78 O HETATM 3733 O HOH A 792 -3.849 53.688 -29.767 1.00 53.82 O HETATM 3734 O HOH A 793 9.639 62.275 -25.279 1.00 53.64 O HETATM 3735 O HOH A 794 31.664 32.318 -22.903 1.00 58.50 O HETATM 3736 O HOH A 795 11.686 19.771 4.754 1.00 46.53 O HETATM 3737 O HOH A 796 13.555 45.273 -4.165 1.00 57.73 O HETATM 3738 O HOH A 797 32.051 16.729 18.786 1.00 47.39 O HETATM 3739 O HOH A 798 -0.793 36.545 -11.776 1.00 54.27 O HETATM 3740 O HOH A 799 0.614 72.100 -16.465 1.00 47.29 O HETATM 3741 O HOH A 800 11.524 17.363 -15.520 1.00 55.42 O HETATM 3742 O HOH A 801 35.908 1.032 29.202 1.00 56.91 O HETATM 3743 O HOH A 802 13.287 5.394 14.300 1.00 52.73 O HETATM 3744 O HOH A 803 17.236 16.236 -17.661 1.00 55.11 O HETATM 3745 O HOH A 804 15.100 73.422 -15.203 1.00 56.46 O HETATM 3746 O HOH A 805 13.635 7.735 5.409 1.00 56.72 O HETATM 3747 O HOH A 806 13.278 9.564 24.180 1.00 55.38 O HETATM 3748 O HOH A 807 38.974 15.397 -8.834 1.00 57.18 O HETATM 3749 O HOH A 808 -6.960 53.411 -23.709 1.00 58.30 O HETATM 3750 O HOH A 809 23.888 58.548 -7.694 1.00 48.58 O HETATM 3751 O HOH A 810 17.341 75.414 2.349 1.00 58.03 O HETATM 3752 O HOH A 811 37.910 8.123 32.456 1.00 57.74 O HETATM 3753 O HOH A 812 19.722 29.623 3.007 1.00 57.38 O HETATM 3754 O HOH A 813 33.072 19.307 19.564 1.00 51.88 O HETATM 3755 O HOH A 814 18.568 66.330 -0.786 1.00 64.09 O HETATM 3756 O HOH A 815 29.773 61.960 -25.181 1.00 53.04 O HETATM 3757 O HOH B 61 6.251 35.056 -6.247 1.00 27.24 O HETATM 3758 O HOH B 89 -5.388 45.674 -3.444 1.00 39.03 O HETATM 3759 O HOH B 102 3.173 43.955 -1.904 1.00 33.87 O HETATM 3760 O HOH B 104 3.836 48.560 -1.752 1.00 32.04 O HETATM 3761 O HOH B 113 23.970 21.322 10.340 1.00 47.96 O HETATM 3762 O HOH B 118 15.802 27.770 -0.473 1.00 30.58 O HETATM 3763 O HOH B 138 2.287 46.219 -0.348 1.00 38.80 O HETATM 3764 O HOH B 148 11.104 27.144 10.594 1.00 47.42 O HETATM 3765 O HOH B 170 13.258 25.529 13.483 1.00 43.85 O HETATM 3766 O HOH B 208 5.082 43.878 -4.117 1.00 31.28 O HETATM 3767 O HOH B 216 3.806 41.720 -7.288 1.00 43.60 O HETATM 3768 O HOH B 217 16.105 34.147 -6.781 1.00 43.18 O HETATM 3769 O HOH B 230 10.027 39.232 -0.460 1.00 50.14 O HETATM 3770 O HOH B 254 2.067 36.030 -5.234 1.00 51.34 O HETATM 3771 O HOH B 255 9.083 35.618 1.273 1.00 48.51 O HETATM 3772 O HOH B 294 16.026 16.944 14.006 1.00 39.81 O HETATM 3773 O HOH B 299 14.241 25.396 1.685 1.00 41.92 O HETATM 3774 O HOH B 318 11.259 25.156 2.744 1.00 44.60 O HETATM 3775 O HOH B 379 17.490 32.515 0.553 1.00 52.31 O HETATM 3776 O HOH B 386 0.125 51.373 0.037 1.00 39.39 O HETATM 3777 O HOH B 388 20.559 14.459 19.662 1.00 52.06 O HETATM 3778 O HOH B 395 6.217 47.615 -0.438 1.00 52.35 O HETATM 3779 O HOH B 409 12.572 27.215 15.897 1.00 47.75 O HETATM 3780 O HOH B 435 9.269 26.940 5.433 1.00 49.91 O HETATM 3781 O HOH B 448 21.796 27.578 5.722 1.00 55.20 O HETATM 3782 O HOH B 491 -0.053 37.833 -4.779 1.00 39.72 O HETATM 3783 O HOH B 497 12.228 40.086 -1.859 1.00 57.99 O HETATM 3784 O HOH B 501 18.159 29.315 7.611 1.00 56.02 O HETATM 3785 O HOH B 521 16.835 37.421 -0.077 1.00 55.91 O HETATM 3786 O HOH B 749 8.001 49.596 0.843 1.00 53.65 O CONECT 1873 2143 CONECT 2143 1873 MASTER 472 0 0 29 2 0 0 6 3784 2 2 33 END
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Entry Information
PDB ID
3k62
Complex Type
Protein-Nucleic Acid
PDBbind Subset
general set
Protein Name
Fem-3 mRNA-binding factor 2
Ligand Name
9-mer
EC.Number
E.C.-.-.-.-
Resolution
1.9(Å)
Affinity (Kd/Ki/IC50)
Kd=127nM
Release Year
2009
Protein/NA Sequence
Check fasta file
Primary Reference
(2009) Proc.Natl.Acad.Sci.USA Vol. 106: pp. 20186-20191
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):
Q09312
Entrez Gene ID
No matched NCBI Entrez Gene ID found!
ASD
Information of known allosteric effects of PDB entries
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