Browse entries in the PDBbind-CN Database
HEADER RNA/RNA BINDING PROTEIN 08-OCT-09 3K61 TITLE CRYSTAL STRUCTURE OF FBF-2/FOG-1 FBEA 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*AP*AP*AP*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 3K61 1 JRNL REVDAT 1 03-NOV-09 3K61 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. 2.21 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) : 2.21 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.91 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 27424 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.176 REMARK 3 FREE R VALUE : 0.216 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 1392 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) : 37.60 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 : 0.004 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): 24.7438 2.5823 27.4681 REMARK 3 T TENSOR REMARK 3 T11: 0.6847 T22: 0.6256 REMARK 3 T33: 0.5205 T12: 0.0582 REMARK 3 T13: 0.0171 T23: 0.4904 REMARK 3 L TENSOR REMARK 3 L11: 2.4515 L22: 3.8647 REMARK 3 L33: 3.3091 L12: 2.7855 REMARK 3 L13: 1.8765 L23: 2.9409 REMARK 3 S TENSOR REMARK 3 S11: 0.3827 S12: -0.7383 S13: -1.2502 REMARK 3 S21: 1.2445 S22: 0.7406 S23: 0.0366 REMARK 3 S31: 0.6237 S32: -0.6228 S33: 0.8102 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN A AND RESID 194:229 REMARK 3 ORIGIN FOR THE GROUP (A): 28.6924 8.2473 19.2410 REMARK 3 T TENSOR REMARK 3 T11: 0.4407 T22: 0.3180 REMARK 3 T33: 0.4845 T12: 0.0372 REMARK 3 T13: -0.0688 T23: 0.1064 REMARK 3 L TENSOR REMARK 3 L11: 0.6676 L22: 0.6653 REMARK 3 L33: 1.0984 L12: 0.5413 REMARK 3 L13: 0.4051 L23: -1.0115 REMARK 3 S TENSOR REMARK 3 S11: 0.3083 S12: -0.1791 S13: -0.3829 REMARK 3 S21: 0.1029 S22: 0.1894 S23: 0.1004 REMARK 3 S31: 0.1985 S32: -0.1540 S33: -0.0000 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN A AND RESID 230:276 REMARK 3 ORIGIN FOR THE GROUP (A): 30.6481 9.1749 7.3834 REMARK 3 T TENSOR REMARK 3 T11: 0.3828 T22: 0.2823 REMARK 3 T33: 0.4055 T12: 0.0671 REMARK 3 T13: -0.1079 T23: -0.0624 REMARK 3 L TENSOR REMARK 3 L11: 0.1553 L22: 1.0508 REMARK 3 L33: 2.5570 L12: -0.5931 REMARK 3 L13: 1.3585 L23: -2.2226 REMARK 3 S TENSOR REMARK 3 S11: 0.2799 S12: 0.0726 S13: -0.4908 REMARK 3 S21: -0.2954 S22: 0.0922 S23: 0.2338 REMARK 3 S31: 0.3076 S32: 0.2302 S33: -0.0002 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN A AND RESID 277:313 REMARK 3 ORIGIN FOR THE GROUP (A): 26.8879 15.9227 -1.9183 REMARK 3 T TENSOR REMARK 3 T11: 0.3241 T22: 0.3440 REMARK 3 T33: 0.3360 T12: 0.0776 REMARK 3 T13: -0.0639 T23: -0.0048 REMARK 3 L TENSOR REMARK 3 L11: 0.3702 L22: 0.8623 REMARK 3 L33: 0.3642 L12: -0.9409 REMARK 3 L13: -0.5675 L23: -1.6182 REMARK 3 S TENSOR REMARK 3 S11: 0.4501 S12: -0.2281 S13: -0.4107 REMARK 3 S21: -0.2433 S22: 0.0128 S23: 0.1514 REMARK 3 S31: 0.3191 S32: 0.1150 S33: 0.0002 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN A AND RESID 314:349 REMARK 3 ORIGIN FOR THE GROUP (A): 24.2632 22.6409 -9.0248 REMARK 3 T TENSOR REMARK 3 T11: 0.2838 T22: 0.3590 REMARK 3 T33: 0.3029 T12: 0.0720 REMARK 3 T13: -0.0207 T23: -0.0154 REMARK 3 L TENSOR REMARK 3 L11: 0.7196 L22: 0.7913 REMARK 3 L33: 0.0100 L12: -0.5209 REMARK 3 L13: 0.4781 L23: -0.9497 REMARK 3 S TENSOR REMARK 3 S11: 0.2809 S12: 0.0994 S13: -0.4012 REMARK 3 S21: -0.0948 S22: 0.0554 S23: 0.1687 REMARK 3 S31: 0.2132 S32: 0.2110 S33: -0.0000 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN A AND RESID 350:404 REMARK 3 ORIGIN FOR THE GROUP (A): 25.3428 32.0054 -14.0118 REMARK 3 T TENSOR REMARK 3 T11: 0.2137 T22: 0.4311 REMARK 3 T33: 0.2499 T12: 0.0538 REMARK 3 T13: 0.0281 T23: 0.0113 REMARK 3 L TENSOR REMARK 3 L11: 1.3842 L22: 1.9845 REMARK 3 L33: -0.0203 L12: -0.8591 REMARK 3 L13: 1.0430 L23: -0.8450 REMARK 3 S TENSOR REMARK 3 S11: 0.3010 S12: 0.2926 S13: 0.0051 REMARK 3 S21: -0.0985 S22: -0.0644 S23: 0.1949 REMARK 3 S31: -0.0566 S32: 0.0776 S33: -0.0000 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN A AND RESID 405:441 REMARK 3 ORIGIN FOR THE GROUP (A): 16.9270 41.6473 -17.2392 REMARK 3 T TENSOR REMARK 3 T11: 0.2589 T22: 0.3170 REMARK 3 T33: 0.2936 T12: 0.0886 REMARK 3 T13: 0.0725 T23: 0.0580 REMARK 3 L TENSOR REMARK 3 L11: 0.3055 L22: 2.2311 REMARK 3 L33: -0.8224 L12: -2.1531 REMARK 3 L13: -0.5976 L23: -1.1368 REMARK 3 S TENSOR REMARK 3 S11: 0.3112 S12: -0.1539 S13: -0.4302 REMARK 3 S21: -0.3826 S22: -0.1817 S23: -0.1290 REMARK 3 S31: -0.0407 S32: 0.0231 S33: 0.0018 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN A AND RESID 442:487 REMARK 3 ORIGIN FOR THE GROUP (A): 7.8613 52.3711 -20.7780 REMARK 3 T TENSOR REMARK 3 T11: 0.2971 T22: 0.2622 REMARK 3 T33: 0.2324 T12: 0.0551 REMARK 3 T13: 0.0470 T23: 0.0535 REMARK 3 L TENSOR REMARK 3 L11: 1.9976 L22: 2.5551 REMARK 3 L33: -0.4690 L12: -0.9166 REMARK 3 L13: -1.3983 L23: -0.2724 REMARK 3 S TENSOR REMARK 3 S11: 0.0546 S12: 0.0447 S13: 0.0495 REMARK 3 S21: -0.4565 S22: -0.0800 S23: 0.0671 REMARK 3 S31: 0.0575 S32: -0.0332 S33: -0.0001 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN A AND RESID 488:545 REMARK 3 ORIGIN FOR THE GROUP (A): 10.1567 61.6096 -14.9207 REMARK 3 T TENSOR REMARK 3 T11: 0.2350 T22: 0.2977 REMARK 3 T33: 0.2126 T12: 0.0192 REMARK 3 T13: -0.0074 T23: -0.0260 REMARK 3 L TENSOR REMARK 3 L11: 1.0891 L22: 3.3787 REMARK 3 L33: 1.0350 L12: -1.0323 REMARK 3 L13: -0.9498 L23: -0.7542 REMARK 3 S TENSOR REMARK 3 S11: -0.1587 S12: -0.3195 S13: 0.1253 REMARK 3 S21: -0.0068 S22: 0.0525 S23: -0.1216 REMARK 3 S31: -0.1633 S32: 0.1628 S33: -0.0000 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN A AND RESID 546:567 REMARK 3 ORIGIN FOR THE GROUP (A): 0.0991 64.5969 -6.7868 REMARK 3 T TENSOR REMARK 3 T11: 0.3923 T22: 0.4256 REMARK 3 T33: 0.2310 T12: 0.0550 REMARK 3 T13: -0.0192 T23: -0.0775 REMARK 3 L TENSOR REMARK 3 L11: 0.3403 L22: 0.4556 REMARK 3 L33: 0.1327 L12: 0.6731 REMARK 3 L13: -0.3041 L23: -0.1876 REMARK 3 S TENSOR REMARK 3 S11: 0.0523 S12: -0.6387 S13: 0.3015 REMARK 3 S21: 0.1121 S22: -0.0106 S23: 0.4475 REMARK 3 S31: -0.3975 S32: -0.0164 S33: 0.0001 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN B REMARK 3 ORIGIN FOR THE GROUP (A): 10.2035 33.8376 1.5718 REMARK 3 T TENSOR REMARK 3 T11: 0.4367 T22: 0.5452 REMARK 3 T33: 0.4359 T12: 0.1845 REMARK 3 T13: 0.1233 T23: 0.2307 REMARK 3 L TENSOR REMARK 3 L11: -0.4176 L22: -0.1700 REMARK 3 L33: -0.5599 L12: -0.3250 REMARK 3 L13: 0.7353 L23: 0.2780 REMARK 3 S TENSOR REMARK 3 S11: -0.4007 S12: 0.0498 S13: -0.3548 REMARK 3 S21: 0.6267 S22: 0.1886 S23: 0.2471 REMARK 3 S31: -0.3537 S32: 0.1097 S33: 0.0000 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 3K61 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 RCSB055590. 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 : 27424 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.210 REMARK 200 RESOLUTION RANGE LOW (A) : 27.913 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 11.400 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.11700 REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.21 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.25 REMARK 200 COMPLETENESS FOR SHELL (%) : 96.8 REMARK 200 DATA REDUNDANCY IN SHELL : 9.40 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.89500 REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600 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 (%): 56.07 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80 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 34.10167 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 68.20333 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 51.15250 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 85.25417 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 17.05083 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: 2530 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19460 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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 LEU A 173 REMARK 465 ASP A 174 REMARK 465 SER A 175 REMARK 465 ASN A 176 REMARK 465 GLY A 177 REMARK 465 GLU A 178 REMARK 465 MET A 179 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 C5 G B 2 N7 0.036 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 ARG A 180 N - CA - C ANGL. DEV. = -16.7 DEGREES REMARK 500 G B 2 O4' - C1' - N9 ANGL. DEV. = 6.0 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASP A 312 -154.98 -121.84 REMARK 500 ARG A 441 -6.79 80.93 REMARK 500 ASP A 477 25.72 -155.90 REMARK 500 GLU A 522 135.33 -178.89 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 ARG A 180 45.8 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 610 DISTANCE = 5.47 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: 3K62 RELATED DB: PDB REMARK 900 RELATED ID: 3K64 RELATED DB: PDB DBREF 3K61 A 164 575 UNP Q09312 FBF2_CAEEL 164 575 DBREF 3K61 B 1 9 PDB 3K61 3K61 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 A A A A U C FORMUL 3 HOH *124(H2 O) HELIX 1 1 SER A 184 GLY A 192 1 9 HELIX 2 2 ASP A 193 VAL A 199 1 7 HELIX 3 3 ASP A 200 VAL A 211 1 12 HELIX 4 4 THR A 216 GLY A 229 1 14 HELIX 5 5 ARG A 230 THR A 239 1 10 HELIX 6 6 PHE A 242 THR A 257 1 16 HELIX 7 7 GLY A 261 GLN A 276 1 16 HELIX 8 8 GLN A 276 LEU A 282 1 7 HELIX 9 9 PHE A 285 MET A 297 1 13 HELIX 10 10 ASP A 298 ALA A 308 1 11 HELIX 11 11 ASP A 312 ASP A 321 1 10 HELIX 12 12 ALA A 324 ILE A 335 1 12 HELIX 13 13 PRO A 336 THR A 349 1 14 HELIX 14 14 THR A 349 SER A 358 1 10 HELIX 15 15 ASP A 359 LEU A 373 1 15 HELIX 16 16 ASP A 376 VAL A 380 5 5 HELIX 17 17 THR A 383 ARG A 404 1 22 HELIX 18 18 ARG A 404 THR A 410 1 7 HELIX 19 19 ALA A 414 ASN A 424 1 11 HELIX 20 20 LEU A 427 CYS A 438 1 12 HELIX 21 21 ASN A 442 GLN A 448 1 7 HELIX 22 22 PHE A 451 ALA A 463 1 13 HELIX 23 23 PRO A 464 GLY A 478 1 15 HELIX 24 24 ASP A 488 HIS A 496 1 9 HELIX 25 25 PHE A 498 SER A 515 1 18 HELIX 26 26 HIS A 527 GLU A 545 1 19 HELIX 27 27 GLU A 545 SER A 550 1 6 HELIX 28 28 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 CRYST1 97.173 97.173 102.305 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 0.010291 0.005941 0.000000 0.00000 SCALE2 0.000000 0.011883 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009775 0.00000 ATOM 1 N LEU A 168 14.854 2.107 22.763 1.00 76.62 N ANISOU 1 N LEU A 168 8305 11002 9806 -638 1667 6665 N ATOM 2 CA LEU A 168 16.071 2.030 23.571 1.00 82.00 C ANISOU 2 CA LEU A 168 9329 11542 10285 -524 1542 6560 C ATOM 3 C LEU A 168 16.241 0.682 24.265 1.00 88.10 C ANISOU 3 C LEU A 168 10262 12118 11092 -722 1353 6846 C ATOM 4 O LEU A 168 15.282 0.135 24.810 1.00 88.78 O ANISOU 4 O LEU A 168 10277 12325 11130 -909 1496 7207 O ATOM 5 CB LEU A 168 16.101 3.147 24.619 1.00 86.01 C ANISOU 5 CB LEU A 168 9963 12303 10415 -273 1816 6514 C ATOM 6 CG LEU A 168 16.516 4.539 24.136 1.00 82.25 C ANISOU 6 CG LEU A 168 9501 11906 9842 -18 1888 6143 C ATOM 7 CD1 LEU A 168 16.698 5.483 25.316 1.00 88.28 C ANISOU 7 CD1 LEU A 168 10432 12876 10234 224 2125 6097 C ATOM 8 CD2 LEU A 168 17.790 4.462 23.313 1.00 70.18 C ANISOU 8 CD2 LEU A 168 8126 10112 8427 -25 1597 5793 C ATOM 9 N PRO A 169 17.474 0.149 24.252 1.00 88.63 N ANISOU 9 N PRO A 169 10547 11876 11252 -687 1006 6648 N ATOM 10 CA PRO A 169 17.818 -1.120 24.904 1.00 87.77 C ANISOU 10 CA PRO A 169 10649 11495 11206 -836 709 6871 C ATOM 11 C PRO A 169 17.443 -1.108 26.380 1.00 92.71 C ANISOU 11 C PRO A 169 11514 12275 11438 -870 884 7231 C ATOM 12 O PRO A 169 17.447 -0.048 27.005 1.00 94.10 O ANISOU 12 O PRO A 169 11756 12710 11286 -686 1165 7168 O ATOM 13 CB PRO A 169 19.346 -1.192 24.742 1.00 87.83 C ANISOU 13 CB PRO A 169 10834 11211 11328 -664 349 6455 C ATOM 14 CG PRO A 169 19.766 0.218 24.366 1.00 83.05 C ANISOU 14 CG PRO A 169 10180 10812 10562 -431 565 6072 C ATOM 15 CD PRO A 169 18.632 0.709 23.539 1.00 81.86 C ANISOU 15 CD PRO A 169 9735 10892 10475 -522 843 6156 C ATOM 16 N THR A 170 17.117 -2.277 26.921 1.00 83.38 N ANISOU 16 N THR A 170 10478 10931 10272 -1134 717 7598 N ATOM 17 CA THR A 170 16.725 -2.393 28.318 1.00 92.22 C ANISOU 17 CA THR A 170 11870 12187 10981 -1272 871 7965 C ATOM 18 C THR A 170 17.793 -1.870 29.302 1.00 96.36 C ANISOU 18 C THR A 170 12760 12660 11191 -1046 767 7836 C ATOM 19 O THR A 170 17.461 -1.147 30.240 1.00101.74 O ANISOU 19 O THR A 170 13549 13646 11463 -1022 1104 7944 O ATOM 20 CB THR A 170 16.310 -3.855 28.657 1.00104.26 C ANISOU 20 CB THR A 170 13567 13469 12578 -1655 621 8382 C ATOM 21 OG1 THR A 170 16.259 -4.040 30.078 1.00101.22 O ANISOU 21 OG1 THR A 170 13579 13128 11750 -1820 656 8704 O ATOM 22 CG2 THR A 170 17.293 -4.841 28.056 1.00108.34 C ANISOU 22 CG2 THR A 170 14191 13474 13501 -1624 37 8227 C ATOM 23 N TRP A 171 19.059 -2.211 29.058 1.00 96.97 N ANISOU 23 N TRP A 171 12998 12368 11478 -879 310 7564 N ATOM 24 CA TRP A 171 20.168 -1.968 29.986 1.00 97.12 C ANISOU 24 CA TRP A 171 13384 12255 11261 -686 92 7447 C ATOM 25 C TRP A 171 20.501 -0.480 30.154 1.00 99.19 C ANISOU 25 C TRP A 171 13603 12833 11253 -386 432 7142 C ATOM 26 O TRP A 171 21.153 -0.082 31.126 1.00102.58 O ANISOU 26 O TRP A 171 14333 13273 11369 -253 391 7114 O ATOM 27 CB TRP A 171 21.413 -2.703 29.486 1.00 94.26 C ANISOU 27 CB TRP A 171 13096 11421 11296 -562 -495 7132 C ATOM 28 CG TRP A 171 21.923 -2.168 28.173 1.00 89.83 C ANISOU 28 CG TRP A 171 12195 10872 11064 -374 -474 6601 C ATOM 29 CD1 TRP A 171 21.687 -2.674 26.926 1.00 88.75 C ANISOU 29 CD1 TRP A 171 11751 10623 11346 -490 -559 6458 C ATOM 30 CD2 TRP A 171 22.768 -1.029 27.988 1.00 89.64 C ANISOU 30 CD2 TRP A 171 12137 10983 10939 -88 -360 6137 C ATOM 31 NE1 TRP A 171 22.331 -1.916 25.978 1.00 91.35 N ANISOU 31 NE1 TRP A 171 11874 11016 11820 -321 -501 5934 N ATOM 32 CE2 TRP A 171 23.001 -0.900 26.606 1.00 88.18 C ANISOU 32 CE2 TRP A 171 11639 10764 11102 -77 -378 5729 C ATOM 33 CE3 TRP A 171 23.349 -0.106 28.859 1.00 88.29 C ANISOU 33 CE3 TRP A 171 12187 10963 10398 132 -241 6023 C ATOM 34 CZ2 TRP A 171 23.788 0.117 26.078 1.00 82.43 C ANISOU 34 CZ2 TRP A 171 10834 10146 10341 114 -278 5220 C ATOM 35 CZ3 TRP A 171 24.127 0.897 28.336 1.00 83.67 C ANISOU 35 CZ3 TRP A 171 11504 10479 9806 356 -145 5520 C ATOM 36 CH2 TRP A 171 24.341 1.003 26.959 1.00 80.24 C ANISOU 36 CH2 TRP A 171 10777 10007 9702 332 -164 5125 C ATOM 37 N SER A 172 20.083 0.327 29.183 1.00 90.87 N ANISOU 37 N SER A 172 12198 12004 10324 -288 728 6911 N ATOM 38 CA SER A 172 20.263 1.768 29.243 1.00 90.95 C ANISOU 38 CA SER A 172 12161 12301 10094 -27 1052 6638 C ATOM 39 C SER A 172 19.099 2.396 29.975 1.00 96.53 C ANISOU 39 C SER A 172 12783 13410 10484 -83 1527 6879 C ATOM 40 O SER A 172 18.027 1.830 30.011 1.00102.46 O ANISOU 40 O SER A 172 13389 14261 11280 -331 1662 7189 O ATOM 41 CB SER A 172 20.380 2.343 27.831 1.00 84.76 C ANISOU 41 CB SER A 172 11081 11530 9593 77 1085 6256 C ATOM 42 OG SER A 172 19.187 2.089 27.095 1.00 83.52 O ANISOU 42 OG SER A 172 10618 11482 9635 -109 1246 6449 O ATOM 43 N ARG A 180 19.726 6.346 31.556 1.00126.30 N ANISOU 43 N ARG A 180 16676 17916 13395 692 2338 6156 N ATOM 44 CA ARG A 180 19.274 6.768 32.861 1.00133.99 C ANISOU 44 CA ARG A 180 17764 19162 13983 679 2644 6306 C ATOM 45 C ARG A 180 20.470 7.667 33.109 1.00139.07 C ANISOU 45 C ARG A 180 18614 19753 14471 972 2568 5939 C ATOM 46 O ARG A 180 21.562 7.305 32.692 1.00142.05 O ANISOU 46 O ARG A 180 19143 19852 14978 1025 2219 5773 O ATOM 47 CB ARG A 180 19.341 5.538 33.762 1.00137.63 C ANISOU 47 CB ARG A 180 18516 19491 14285 379 2459 6692 C ATOM 48 CG ARG A 180 19.458 4.279 32.898 1.00135.16 C ANISOU 48 CG ARG A 180 18171 18843 14342 195 2078 6841 C ATOM 49 CD ARG A 180 19.803 3.004 33.656 1.00135.46 C ANISOU 49 CD ARG A 180 18579 18610 14279 -68 1731 7192 C ATOM 50 NE ARG A 180 21.113 2.442 33.315 1.00130.61 N ANISOU 50 NE ARG A 180 18186 17569 13870 52 1200 7044 N ATOM 51 CZ ARG A 180 22.261 2.832 33.860 1.00127.10 C ANISOU 51 CZ ARG A 180 18023 17016 13253 267 1008 6838 C ATOM 52 NH1 ARG A 180 22.266 3.802 34.761 1.00128.42 N ANISOU 52 NH1 ARG A 180 18296 17468 13030 378 1316 6761 N ATOM 53 NH2 ARG A 180 23.405 2.261 33.499 1.00122.98 N ANISOU 53 NH2 ARG A 180 17622 16105 12998 381 498 6629 N ATOM 54 N SER A 181 20.322 8.833 33.728 1.00143.64 N ANISOU 54 N SER A 181 19194 20585 14796 1162 2877 5780 N ATOM 55 CA SER A 181 21.448 9.782 33.690 1.00140.82 C ANISOU 55 CA SER A 181 18985 20160 14361 1449 2797 5373 C ATOM 56 C SER A 181 22.765 9.208 34.236 1.00138.68 C ANISOU 56 C SER A 181 19073 19650 13967 1443 2458 5335 C ATOM 57 O SER A 181 22.777 8.156 34.880 1.00140.20 O ANISOU 57 O SER A 181 19464 19735 14071 1230 2283 5662 O ATOM 58 CB SER A 181 21.106 11.106 34.375 1.00142.71 C ANISOU 58 CB SER A 181 19198 20677 14346 1656 3156 5218 C ATOM 59 OG SER A 181 20.899 10.916 35.760 1.00148.26 O ANISOU 59 OG SER A 181 20090 21546 14694 1535 3321 5444 O ATOM 60 N ARG A 182 23.866 9.906 33.959 1.00131.51 N ANISOU 60 N ARG A 182 18266 18650 13051 1665 2343 4936 N ATOM 61 CA ARG A 182 25.204 9.438 34.322 1.00127.45 C ANISOU 61 CA ARG A 182 18063 17905 12456 1699 1988 4833 C ATOM 62 C ARG A 182 25.548 8.169 33.542 1.00117.59 C ANISOU 62 C ARG A 182 16814 16347 11518 1544 1581 4937 C ATOM 63 O ARG A 182 25.908 7.142 34.115 1.00123.33 O ANISOU 63 O ARG A 182 17779 16858 12222 1436 1250 5188 O ATOM 64 CB ARG A 182 25.321 9.219 35.837 1.00134.58 C ANISOU 64 CB ARG A 182 19282 18861 12989 1646 1987 5082 C ATOM 65 CG ARG A 182 26.755 9.171 36.383 1.00136.84 C ANISOU 65 CG ARG A 182 19912 18961 13120 1776 1655 4898 C ATOM 66 CD ARG A 182 27.265 7.738 36.538 1.00139.98 C ANISOU 66 CD ARG A 182 20553 19010 13623 1628 1126 5165 C ATOM 67 NE ARG A 182 28.554 7.669 37.223 1.00140.32 N ANISOU 67 NE ARG A 182 20945 18869 13501 1772 753 5031 N ATOM 68 CZ ARG A 182 29.177 6.535 37.533 1.00141.85 C ANISOU 68 CZ ARG A 182 21361 18696 13839 1714 191 5154 C ATOM 69 NH1 ARG A 182 28.630 5.368 37.219 1.00142.43 N ANISOU 69 NH1 ARG A 182 21382 18549 14187 1496 -42 5453 N ATOM 70 NH2 ARG A 182 30.346 6.566 38.157 1.00142.56 N ANISOU 70 NH2 ARG A 182 21705 18618 13844 1878 -165 4937 N ATOM 71 N LEU A 183 25.420 8.251 32.224 1.00 98.76 N ANISOU 71 N LEU A 183 14176 13914 9434 1528 1574 4748 N ATOM 72 CA LEU A 183 25.747 7.139 31.346 1.00 87.68 C ANISOU 72 CA LEU A 183 12708 12214 8392 1391 1202 4754 C ATOM 73 C LEU A 183 27.009 7.501 30.577 1.00 77.42 C ANISOU 73 C LEU A 183 11382 10780 7254 1513 1000 4174 C ATOM 74 O LEU A 183 27.225 8.671 30.260 1.00 67.75 O ANISOU 74 O LEU A 183 10149 9731 5863 1629 1236 3884 O ATOM 75 CB LEU A 183 24.601 6.885 30.369 1.00 81.65 C ANISOU 75 CB LEU A 183 11636 11506 7882 1217 1351 4928 C ATOM 76 CG LEU A 183 24.422 5.451 29.873 1.00 76.80 C ANISOU 76 CG LEU A 183 10911 10616 7653 1001 1022 5099 C ATOM 77 CD1 LEU A 183 23.707 4.638 30.926 1.00 73.88 C ANISOU 77 CD1 LEU A 183 10691 10247 7135 837 1018 5625 C ATOM 78 CD2 LEU A 183 23.642 5.426 28.573 1.00 77.28 C ANISOU 78 CD2 LEU A 183 10645 10713 8004 868 1131 5074 C ATOM 79 N SER A 184 27.839 6.506 30.275 1.00 78.29 N ANISOU 79 N SER A 184 11478 10579 7691 1472 560 3979 N ATOM 80 CA SER A 184 29.109 6.759 29.596 1.00 69.73 C ANISOU 80 CA SER A 184 10337 9381 6777 1556 364 3356 C ATOM 81 C SER A 184 29.054 6.454 28.101 1.00 61.16 C ANISOU 81 C SER A 184 8957 8208 6074 1378 309 3074 C ATOM 82 O SER A 184 28.331 5.558 27.651 1.00 54.76 O ANISOU 82 O SER A 184 7994 7281 5532 1208 217 3341 O ATOM 83 CB SER A 184 30.248 5.969 30.248 1.00 72.48 C ANISOU 83 CB SER A 184 10834 9443 7261 1660 -115 3178 C ATOM 84 OG SER A 184 30.400 4.688 29.660 1.00 71.85 O ANISOU 84 OG SER A 184 10596 9045 7659 1540 -515 3123 O ATOM 85 N LEU A 185 29.829 7.214 27.336 1.00 56.73 N ANISOU 85 N LEU A 185 8335 7711 5510 1383 374 2526 N ATOM 86 CA LEU A 185 29.928 7.014 25.902 1.00 48.85 C ANISOU 86 CA LEU A 185 7093 6648 4818 1165 330 2178 C ATOM 87 C LEU A 185 30.500 5.630 25.591 1.00 47.19 C ANISOU 87 C LEU A 185 6724 6123 5082 1086 -108 1983 C ATOM 88 O LEU A 185 30.045 4.950 24.668 1.00 46.73 O ANISOU 88 O LEU A 185 6454 5965 5335 877 -177 2007 O ATOM 89 CB LEU A 185 30.795 8.109 25.276 1.00 44.97 C ANISOU 89 CB LEU A 185 6630 6290 4165 1138 474 1586 C ATOM 90 CG LEU A 185 31.086 7.985 23.786 1.00 47.02 C ANISOU 90 CG LEU A 185 6683 6504 4679 846 436 1127 C ATOM 91 CD1 LEU A 185 29.787 7.998 22.999 1.00 47.78 C ANISOU 91 CD1 LEU A 185 6677 6658 4819 655 608 1508 C ATOM 92 CD2 LEU A 185 32.034 9.098 23.321 1.00 43.71 C ANISOU 92 CD2 LEU A 185 6358 6229 4022 774 583 528 C ATOM 93 N SER A 186 31.494 5.205 26.362 1.00 46.97 N ANISOU 93 N SER A 186 6796 5922 5127 1260 -430 1780 N ATOM 94 CA SER A 186 32.094 3.901 26.107 1.00 52.68 C ANISOU 94 CA SER A 186 7365 6305 6345 1227 -908 1546 C ATOM 95 C SER A 186 31.081 2.763 26.282 1.00 55.84 C ANISOU 95 C SER A 186 7756 6517 6942 1125 -1069 2145 C ATOM 96 O SER A 186 31.108 1.784 25.536 1.00 53.13 O ANISOU 96 O SER A 186 7201 5948 7037 985 -1325 2007 O ATOM 97 CB SER A 186 33.349 3.685 26.953 1.00 55.60 C ANISOU 97 CB SER A 186 7853 6496 6778 1465 -1286 1207 C ATOM 98 OG SER A 186 34.469 4.316 26.350 1.00 52.42 O ANISOU 98 OG SER A 186 7310 6187 6421 1470 -1247 444 O ATOM 99 N GLU A 187 30.173 2.909 27.243 1.00 63.68 N ANISOU 99 N GLU A 187 8972 7621 7603 1164 -895 2782 N ATOM 100 CA GLU A 187 29.102 1.932 27.427 1.00 72.44 C ANISOU 100 CA GLU A 187 10091 8608 8825 1010 -972 3373 C ATOM 101 C GLU A 187 28.301 1.766 26.146 1.00 61.31 C ANISOU 101 C GLU A 187 8386 7264 7647 776 -790 3385 C ATOM 102 O GLU A 187 28.021 0.644 25.712 1.00 57.28 O ANISOU 102 O GLU A 187 7747 6517 7499 624 -1043 3498 O ATOM 103 CB GLU A 187 28.153 2.362 28.545 1.00 79.89 C ANISOU 103 CB GLU A 187 11277 9773 9304 1025 -673 3982 C ATOM 104 CG GLU A 187 28.684 2.157 29.944 1.00 90.55 C ANISOU 104 CG GLU A 187 12980 11000 10425 1165 -921 4159 C ATOM 105 CD GLU A 187 27.621 2.403 30.995 1.00101.23 C ANISOU 105 CD GLU A 187 14554 12578 11331 1083 -608 4774 C ATOM 106 OE1 GLU A 187 26.702 1.563 31.124 1.00109.65 O ANISOU 106 OE1 GLU A 187 15634 13572 12455 862 -639 5238 O ATOM 107 OE2 GLU A 187 27.706 3.434 31.694 1.00100.44 O ANISOU 107 OE2 GLU A 187 14607 12737 10819 1216 -320 4768 O ATOM 108 N VAL A 188 27.927 2.890 25.548 1.00 44.96 N ANISOU 108 N VAL A 188 6228 5496 5361 742 -377 3277 N ATOM 109 CA VAL A 188 27.110 2.865 24.346 1.00 48.30 C ANISOU 109 CA VAL A 188 6405 5995 5952 514 -204 3314 C ATOM 110 C VAL A 188 27.896 2.247 23.197 1.00 53.66 C ANISOU 110 C VAL A 188 6863 6469 7055 365 -469 2770 C ATOM 111 O VAL A 188 27.375 1.409 22.453 1.00 56.49 O ANISOU 111 O VAL A 188 7031 6703 7730 160 -571 2869 O ATOM 112 CB VAL A 188 26.632 4.280 23.957 1.00 48.08 C ANISOU 112 CB VAL A 188 6380 6292 5596 522 224 3279 C ATOM 113 CG1 VAL A 188 25.971 4.269 22.582 1.00 40.70 C ANISOU 113 CG1 VAL A 188 5214 5392 4857 269 319 3230 C ATOM 114 CG2 VAL A 188 25.675 4.819 25.010 1.00 57.07 C ANISOU 114 CG2 VAL A 188 7659 7647 6376 648 511 3802 C ATOM 115 N LEU A 189 29.155 2.654 23.062 1.00 46.06 N ANISOU 115 N LEU A 189 5912 5485 6102 451 -567 2163 N ATOM 116 CA LEU A 189 29.969 2.196 21.948 1.00 46.36 C ANISOU 116 CA LEU A 189 5710 5386 6519 279 -762 1532 C ATOM 117 C LEU A 189 30.249 0.696 22.051 1.00 50.12 C ANISOU 117 C LEU A 189 6067 5493 7482 284 -1231 1513 C ATOM 118 O LEU A 189 30.241 -0.006 21.040 1.00 46.23 O ANISOU 118 O LEU A 189 5326 4874 7365 68 -1353 1270 O ATOM 119 CB LEU A 189 31.272 2.998 21.851 1.00 41.26 C ANISOU 119 CB LEU A 189 5089 4832 5755 350 -738 840 C ATOM 120 CG LEU A 189 31.123 4.477 21.477 1.00 38.81 C ANISOU 120 CG LEU A 189 4898 4845 5002 274 -314 742 C ATOM 121 CD1 LEU A 189 32.427 5.209 21.671 1.00 37.88 C ANISOU 121 CD1 LEU A 189 4857 4810 4727 367 -308 123 C ATOM 122 CD2 LEU A 189 30.647 4.613 20.029 1.00 35.94 C ANISOU 122 CD2 LEU A 189 4375 4561 4719 -90 -152 595 C ATOM 123 N ASP A 190 30.491 0.214 23.270 1.00 53.18 N ANISOU 123 N ASP A 190 6655 5695 7857 516 -1512 1771 N ATOM 124 CA ASP A 190 30.799 -1.201 23.506 1.00 58.84 C ANISOU 124 CA ASP A 190 7330 6000 9027 551 -2042 1782 C ATOM 125 C ASP A 190 29.555 -2.098 23.394 1.00 67.10 C ANISOU 125 C ASP A 190 8364 6935 10198 362 -2065 2408 C ATOM 126 O ASP A 190 29.656 -3.267 23.019 1.00 71.32 O ANISOU 126 O ASP A 190 8764 7147 11187 277 -2437 2328 O ATOM 127 CB ASP A 190 31.447 -1.401 24.887 1.00 63.38 C ANISOU 127 CB ASP A 190 8194 6382 9506 834 -2387 1895 C ATOM 128 CG ASP A 190 32.847 -0.790 24.990 1.00 69.24 C ANISOU 128 CG ASP A 190 8901 7153 10254 1034 -2494 1184 C ATOM 129 OD1 ASP A 190 33.283 -0.498 26.126 1.00 72.03 O ANISOU 129 OD1 ASP A 190 9524 7480 10363 1263 -2622 1298 O ATOM 130 OD2 ASP A 190 33.516 -0.607 23.951 1.00 68.64 O ANISOU 130 OD2 ASP A 190 8532 7135 10413 935 -2446 499 O ATOM 131 N SER A 191 28.389 -1.545 23.724 1.00 68.33 N ANISOU 131 N SER A 191 8643 7358 9963 295 -1670 2996 N ATOM 132 CA SER A 191 27.149 -2.319 23.778 1.00 69.79 C ANISOU 132 CA SER A 191 8831 7485 10202 107 -1648 3618 C ATOM 133 C SER A 191 26.735 -2.877 22.420 1.00 72.14 C ANISOU 133 C SER A 191 8808 7726 10875 -150 -1644 3469 C ATOM 134 O SER A 191 26.153 -3.959 22.336 1.00 76.60 O ANISOU 134 O SER A 191 9334 8079 11693 -300 -1844 3786 O ATOM 135 CB SER A 191 26.013 -1.466 24.340 1.00 60.47 C ANISOU 135 CB SER A 191 7776 6663 8538 90 -1174 4158 C ATOM 136 OG SER A 191 25.643 -0.451 23.417 1.00 53.98 O ANISOU 136 OG SER A 191 6769 6145 7598 23 -777 3973 O ATOM 137 N GLY A 192 27.028 -2.133 21.359 1.00 60.61 N ANISOU 137 N GLY A 192 7148 6457 9425 -232 -1418 2993 N ATOM 138 CA GLY A 192 26.636 -2.535 20.020 1.00 56.18 C ANISOU 138 CA GLY A 192 6303 5881 9160 -515 -1380 2831 C ATOM 139 C GLY A 192 25.250 -2.015 19.694 1.00 58.20 C ANISOU 139 C GLY A 192 6526 6413 9176 -669 -989 3319 C ATOM 140 O GLY A 192 24.670 -2.352 18.662 1.00 54.70 O ANISOU 140 O GLY A 192 5875 5974 8935 -920 -941 3325 O ATOM 141 N ASP A 193 24.719 -1.183 20.584 1.00 56.55 N ANISOU 141 N ASP A 193 6507 6434 8547 -514 -720 3703 N ATOM 142 CA ASP A 193 23.379 -0.644 20.424 1.00 59.59 C ANISOU 142 CA ASP A 193 6837 7083 8721 -607 -366 4147 C ATOM 143 C ASP A 193 23.385 0.816 20.010 1.00 63.41 C ANISOU 143 C ASP A 193 7343 7849 8899 -554 -50 3931 C ATOM 144 O ASP A 193 22.396 1.516 20.224 1.00 63.74 O ANISOU 144 O ASP A 193 7393 8123 8701 -516 236 4276 O ATOM 145 CB ASP A 193 22.605 -0.757 21.731 1.00 64.22 C ANISOU 145 CB ASP A 193 7593 7749 9060 -504 -260 4739 C ATOM 146 CG ASP A 193 22.391 -2.185 22.157 1.00 71.33 C ANISOU 146 CG ASP A 193 8530 8367 10205 -620 -567 5056 C ATOM 147 OD1 ASP A 193 22.419 -2.438 23.375 1.00 70.02 O ANISOU 147 OD1 ASP A 193 8613 8145 9847 -530 -647 5359 O ATOM 148 OD2 ASP A 193 22.202 -3.049 21.275 1.00 80.24 O ANISOU 148 OD2 ASP A 193 9466 9321 11702 -823 -739 5002 O ATOM 149 N LEU A 194 24.487 1.289 19.437 1.00 59.92 N ANISOU 149 N LEU A 194 7809 6239 8720 -62 -1738 1891 N ATOM 150 CA LEU A 194 24.567 2.702 19.072 1.00 51.35 C ANISOU 150 CA LEU A 194 6700 5252 7558 6 -1505 1800 C ATOM 151 C LEU A 194 23.411 3.099 18.159 1.00 50.64 C ANISOU 151 C LEU A 194 6575 5203 7464 -30 -1455 1903 C ATOM 152 O LEU A 194 22.739 4.091 18.407 1.00 50.10 O ANISOU 152 O LEU A 194 6446 5256 7335 -23 -1282 1993 O ATOM 153 CB LEU A 194 25.908 3.046 18.416 1.00 42.48 C ANISOU 153 CB LEU A 194 5631 4075 6436 102 -1459 1542 C ATOM 154 CG LEU A 194 26.043 4.528 18.029 1.00 42.68 C ANISOU 154 CG LEU A 194 5635 4201 6381 166 -1231 1447 C ATOM 155 CD1 LEU A 194 27.465 5.042 18.248 1.00 39.45 C ANISOU 155 CD1 LEU A 194 5257 3795 5935 250 -1156 1250 C ATOM 156 CD2 LEU A 194 25.571 4.789 16.584 1.00 38.37 C ANISOU 156 CD2 LEU A 194 5089 3635 5852 164 -1214 1407 C ATOM 157 N MET A 195 23.174 2.309 17.117 1.00 49.10 N ANISOU 157 N MET A 195 6422 4901 7333 -72 -1608 1897 N ATOM 158 CA MET A 195 22.157 2.638 16.125 1.00 49.90 C ANISOU 158 CA MET A 195 6496 5029 7434 -120 -1578 1989 C ATOM 159 C MET A 195 20.788 2.898 16.748 1.00 54.17 C ANISOU 159 C MET A 195 6944 5688 7948 -190 -1525 2262 C ATOM 160 O MET A 195 19.988 3.649 16.195 1.00 52.32 O ANISOU 160 O MET A 195 6657 5529 7694 -203 -1412 2346 O ATOM 161 CB MET A 195 22.066 1.545 15.056 1.00 46.39 C ANISOU 161 CB MET A 195 6130 4439 7057 -179 -1787 1967 C ATOM 162 CG MET A 195 23.307 1.458 14.157 1.00 47.91 C ANISOU 162 CG MET A 195 6408 4528 7268 -98 -1803 1691 C ATOM 163 SD MET A 195 23.511 2.917 13.103 1.00 51.45 S ANISOU 163 SD MET A 195 6828 5062 7659 -35 -1582 1544 S ATOM 164 CE MET A 195 22.079 2.750 12.030 1.00 50.43 C ANISOU 164 CE MET A 195 6687 4926 7549 -160 -1649 1724 C ATOM 165 N LYS A 196 20.520 2.279 17.895 1.00 61.02 N ANISOU 165 N LYS A 196 7788 6578 8820 -233 -1607 2408 N ATOM 166 CA LYS A 196 19.252 2.487 18.591 1.00 62.58 C ANISOU 166 CA LYS A 196 7889 6902 8986 -293 -1555 2677 C ATOM 167 C LYS A 196 19.218 3.857 19.267 1.00 65.59 C ANISOU 167 C LYS A 196 8211 7427 9283 -213 -1286 2666 C ATOM 168 O LYS A 196 18.207 4.557 19.213 1.00 72.47 O ANISOU 168 O LYS A 196 9005 8405 10125 -220 -1155 2821 O ATOM 169 CB LYS A 196 18.985 1.363 19.600 1.00 66.30 C ANISOU 169 CB LYS A 196 8350 7358 9482 -373 -1737 2839 C ATOM 170 CG LYS A 196 19.218 -0.033 19.037 1.00 73.56 C ANISOU 170 CG LYS A 196 9353 8112 10486 -441 -2013 2818 C ATOM 171 CD LYS A 196 18.393 -1.079 19.762 1.00 86.12 C ANISOU 171 CD LYS A 196 10909 9710 12103 -557 -2206 3072 C ATOM 172 CE LYS A 196 16.916 -0.947 19.417 1.00 96.21 C ANISOU 172 CE LYS A 196 12109 11079 13369 -644 -2203 3336 C ATOM 173 NZ LYS A 196 16.667 -1.059 17.949 1.00 99.34 N ANISOU 173 NZ LYS A 196 12561 11383 13799 -678 -2267 3295 N ATOM 174 N PHE A 197 20.333 4.237 19.888 1.00 56.07 N ANISOU 174 N PHE A 197 7047 6218 8038 -138 -1207 2488 N ATOM 175 CA PHE A 197 20.484 5.566 20.483 1.00 52.27 C ANISOU 175 CA PHE A 197 6542 5851 7468 -59 -957 2440 C ATOM 176 C PHE A 197 20.405 6.686 19.454 1.00 50.03 C ANISOU 176 C PHE A 197 6250 5594 7167 1 -795 2346 C ATOM 177 O PHE A 197 19.776 7.716 19.686 1.00 45.87 O ANISOU 177 O PHE A 197 5670 5174 6585 36 -602 2424 O ATOM 178 CB PHE A 197 21.828 5.680 21.202 1.00 47.27 C ANISOU 178 CB PHE A 197 5973 5189 6799 -5 -935 2253 C ATOM 179 CG PHE A 197 21.862 4.997 22.529 1.00 55.06 C ANISOU 179 CG PHE A 197 6952 6196 7772 -56 -1018 2360 C ATOM 180 CD1 PHE A 197 21.612 5.706 23.691 1.00 58.35 C ANISOU 180 CD1 PHE A 197 7343 6732 8096 -43 -858 2437 C ATOM 181 CD2 PHE A 197 22.148 3.646 22.620 1.00 60.31 C ANISOU 181 CD2 PHE A 197 7641 6760 8516 -119 -1258 2382 C ATOM 182 CE1 PHE A 197 21.643 5.075 24.921 1.00 64.03 C ANISOU 182 CE1 PHE A 197 8053 7479 8798 -102 -938 2539 C ATOM 183 CE2 PHE A 197 22.184 3.011 23.845 1.00 60.21 C ANISOU 183 CE2 PHE A 197 7614 6769 8495 -176 -1344 2488 C ATOM 184 CZ PHE A 197 21.929 3.725 24.997 1.00 61.46 C ANISOU 184 CZ PHE A 197 7739 7057 8557 -172 -1185 2568 C ATOM 185 N ALA A 198 21.071 6.479 18.324 1.00 49.93 N ANISOU 185 N ALA A 198 6290 5482 7199 14 -872 2176 N ATOM 186 CA ALA A 198 21.240 7.524 17.326 1.00 49.45 C ANISOU 186 CA ALA A 198 6228 5441 7121 68 -733 2051 C ATOM 187 C ALA A 198 19.942 7.952 16.633 1.00 52.59 C ANISOU 187 C ALA A 198 6549 5897 7534 26 -671 2223 C ATOM 188 O ALA A 198 19.844 9.084 16.165 1.00 54.77 O ANISOU 188 O ALA A 198 6798 6231 7781 74 -502 2175 O ATOM 189 CB ALA A 198 22.282 7.107 16.301 1.00 49.64 C ANISOU 189 CB ALA A 198 6325 5351 7186 88 -841 1832 C ATOM 190 N VAL A 199 18.957 7.057 16.556 1.00 54.26 N ANISOU 190 N VAL A 199 6725 6095 7795 -68 -812 2432 N ATOM 191 CA VAL A 199 17.672 7.398 15.931 1.00 55.63 C ANISOU 191 CA VAL A 199 6817 6332 7989 -122 -766 2631 C ATOM 192 C VAL A 199 16.604 7.768 16.956 1.00 57.15 C ANISOU 192 C VAL A 199 6913 6655 8147 -124 -650 2876 C ATOM 193 O VAL A 199 15.478 8.115 16.597 1.00 62.71 O ANISOU 193 O VAL A 199 7531 7430 8867 -159 -591 3073 O ATOM 194 CB VAL A 199 17.137 6.267 15.033 1.00 54.46 C ANISOU 194 CB VAL A 199 6686 6094 7911 -239 -992 2733 C ATOM 195 CG1 VAL A 199 18.123 5.969 13.915 1.00 57.33 C ANISOU 195 CG1 VAL A 199 7149 6333 8303 -230 -1086 2489 C ATOM 196 CG2 VAL A 199 16.836 5.019 15.864 1.00 49.79 C ANISOU 196 CG2 VAL A 199 6104 5471 7342 -312 -1182 2885 C ATOM 197 N ASP A 200 16.968 7.682 18.232 1.00 52.37 N ANISOU 197 N ASP A 200 6321 6084 7493 -88 -618 2870 N ATOM 198 CA ASP A 200 16.103 8.100 19.329 1.00 56.17 C ANISOU 198 CA ASP A 200 6722 6697 7923 -72 -484 3073 C ATOM 199 C ASP A 200 16.387 9.568 19.661 1.00 58.82 C ANISOU 199 C ASP A 200 7060 7107 8183 44 -214 2963 C ATOM 200 O ASP A 200 17.540 9.994 19.657 1.00 62.86 O ANISOU 200 O ASP A 200 7652 7569 8661 104 -168 2724 O ATOM 201 CB ASP A 200 16.368 7.216 20.553 1.00 61.00 C ANISOU 201 CB ASP A 200 7355 7307 8514 -107 -598 3121 C ATOM 202 CG ASP A 200 15.402 7.485 21.699 1.00 67.13 C ANISOU 202 CG ASP A 200 8046 8227 9234 -105 -482 3352 C ATOM 203 OD1 ASP A 200 14.216 7.104 21.592 1.00 72.08 O ANISOU 203 OD1 ASP A 200 8582 8914 9891 -172 -535 3608 O ATOM 204 OD2 ASP A 200 15.840 8.061 22.718 1.00 60.61 O ANISOU 204 OD2 ASP A 200 7246 7456 8327 -41 -340 3283 O ATOM 205 N LYS A 201 15.345 10.344 19.938 1.00 58.86 N ANISOU 205 N LYS A 201 6978 7227 8161 75 -39 3141 N ATOM 206 CA LYS A 201 15.520 11.753 20.295 1.00 67.33 C ANISOU 206 CA LYS A 201 8060 8362 9159 188 222 3051 C ATOM 207 C LYS A 201 16.468 11.949 21.481 1.00 62.66 C ANISOU 207 C LYS A 201 7557 7773 8477 240 284 2906 C ATOM 208 O LYS A 201 17.454 12.684 21.396 1.00 61.20 O ANISOU 208 O LYS A 201 7453 7552 8248 303 370 2685 O ATOM 209 CB LYS A 201 14.162 12.397 20.597 1.00 80.78 C ANISOU 209 CB LYS A 201 9652 10192 10849 219 395 3299 C ATOM 210 CG LYS A 201 14.235 13.660 21.450 1.00 93.18 C ANISOU 210 CG LYS A 201 11246 11837 12323 338 662 3246 C ATOM 211 CD LYS A 201 14.960 14.789 20.731 1.00101.86 C ANISOU 211 CD LYS A 201 12407 12889 13409 414 787 3022 C ATOM 212 CE LYS A 201 14.988 16.060 21.573 1.00105.37 C ANISOU 212 CE LYS A 201 12890 13393 13752 529 1048 2976 C ATOM 213 NZ LYS A 201 15.849 17.120 20.967 1.00103.83 N ANISOU 213 NZ LYS A 201 12772 13144 13533 594 1145 2742 N ATOM 214 N THR A 202 16.161 11.284 22.587 1.00 62.33 N ANISOU 214 N THR A 202 7498 7779 8406 201 231 3042 N ATOM 215 CA THR A 202 16.934 11.419 23.813 1.00 63.07 C ANISOU 215 CA THR A 202 7668 7887 8408 229 285 2942 C ATOM 216 C THR A 202 18.303 10.756 23.689 1.00 65.38 C ANISOU 216 C THR A 202 8055 8064 8723 198 114 2730 C ATOM 217 O THR A 202 19.310 11.297 24.151 1.00 60.57 O ANISOU 217 O THR A 202 7532 7436 8046 244 191 2551 O ATOM 218 CB THR A 202 16.172 10.813 25.007 1.00 70.84 C ANISOU 218 CB THR A 202 8596 8963 9357 181 261 3165 C ATOM 219 OG1 THR A 202 14.818 11.284 24.993 1.00 73.81 O ANISOU 219 OG1 THR A 202 8865 9450 9729 208 399 3391 O ATOM 220 CG2 THR A 202 16.833 11.201 26.323 1.00 69.49 C ANISOU 220 CG2 THR A 202 8504 8827 9071 213 367 3076 C ATOM 221 N GLY A 203 18.329 9.580 23.065 1.00 62.57 N ANISOU 221 N GLY A 203 7684 7628 8462 120 -118 2759 N ATOM 222 CA GLY A 203 19.565 8.857 22.830 1.00 58.00 C ANISOU 222 CA GLY A 203 7184 6930 7921 99 -288 2570 C ATOM 223 C GLY A 203 20.546 9.650 21.978 1.00 60.89 C ANISOU 223 C GLY A 203 7615 7242 8280 170 -212 2325 C ATOM 224 O GLY A 203 21.745 9.689 22.261 1.00 55.23 O ANISOU 224 O GLY A 203 6973 6478 7535 196 -229 2147 O ATOM 225 N CYS A 204 20.046 10.293 20.930 1.00 62.31 N ANISOU 225 N CYS A 204 7758 7433 8484 197 -130 2327 N ATOM 226 CA CYS A 204 20.925 11.043 20.048 1.00 60.89 C ANISOU 226 CA CYS A 204 7628 7210 8297 255 -67 2106 C ATOM 227 C CYS A 204 21.367 12.335 20.720 1.00 58.49 C ANISOU 227 C CYS A 204 7367 6969 7889 335 148 2011 C ATOM 228 O CYS A 204 22.479 12.815 20.500 1.00 50.79 O ANISOU 228 O CYS A 204 6459 5959 6881 377 176 1810 O ATOM 229 CB CYS A 204 20.266 11.326 18.700 1.00 60.28 C ANISOU 229 CB CYS A 204 7498 7127 8279 245 -56 2140 C ATOM 230 SG CYS A 204 21.459 11.853 17.430 1.00 62.90 S ANISOU 230 SG CYS A 204 7887 7390 8620 290 -55 1861 S ATOM 231 N GLN A 205 20.497 12.877 21.560 1.00 58.59 N ANISOU 231 N GLN A 205 7344 7073 7844 355 298 2164 N ATOM 232 CA GLN A 205 20.823 14.071 22.321 1.00 66.98 C ANISOU 232 CA GLN A 205 8465 8190 8796 427 505 2089 C ATOM 233 C GLN A 205 22.031 13.791 23.203 1.00 65.31 C ANISOU 233 C GLN A 205 8347 7943 8523 415 447 1957 C ATOM 234 O GLN A 205 22.934 14.617 23.323 1.00 66.59 O ANISOU 234 O GLN A 205 8591 8096 8615 459 537 1793 O ATOM 235 CB GLN A 205 19.627 14.493 23.171 1.00 76.92 C ANISOU 235 CB GLN A 205 9672 9551 10004 449 662 2293 C ATOM 236 CG GLN A 205 19.714 15.904 23.712 1.00 86.13 C ANISOU 236 CG GLN A 205 10899 10765 11060 537 906 2228 C ATOM 237 CD GLN A 205 18.524 16.256 24.584 1.00 98.00 C ANISOU 237 CD GLN A 205 12353 12371 12512 570 1067 2431 C ATOM 238 OE1 GLN A 205 17.456 15.653 24.470 1.00100.59 O ANISOU 238 OE1 GLN A 205 12571 12746 12903 536 1019 2640 O ATOM 239 NE2 GLN A 205 18.705 17.233 25.465 1.00100.23 N ANISOU 239 NE2 GLN A 205 12719 12690 12674 636 1260 2377 N ATOM 240 N PHE A 206 22.048 12.607 23.805 1.00 61.74 N ANISOU 240 N PHE A 206 7882 7472 8103 345 285 2039 N ATOM 241 CA PHE A 206 23.164 12.182 24.642 1.00 63.15 C ANISOU 241 CA PHE A 206 8135 7615 8243 317 203 1940 C ATOM 242 C PHE A 206 24.478 12.073 23.857 1.00 62.94 C ANISOU 242 C PHE A 206 8162 7498 8253 334 107 1725 C ATOM 243 O PHE A 206 25.508 12.620 24.270 1.00 52.14 O ANISOU 243 O PHE A 206 6871 6126 6813 357 161 1588 O ATOM 244 CB PHE A 206 22.833 10.852 25.329 1.00 59.00 C ANISOU 244 CB PHE A 206 7569 7082 7764 233 28 2088 C ATOM 245 CG PHE A 206 24.027 10.168 25.951 1.00 67.74 C ANISOU 245 CG PHE A 206 8737 8131 8872 191 -108 1990 C ATOM 246 CD1 PHE A 206 24.720 10.759 26.995 1.00 70.80 C ANISOU 246 CD1 PHE A 206 9198 8553 9150 195 -10 1926 C ATOM 247 CD2 PHE A 206 24.444 8.925 25.497 1.00 67.51 C ANISOU 247 CD2 PHE A 206 8693 8006 8952 146 -337 1970 C ATOM 248 CE1 PHE A 206 25.811 10.126 27.566 1.00 69.97 C ANISOU 248 CE1 PHE A 206 9138 8396 9050 147 -139 1855 C ATOM 249 CE2 PHE A 206 25.534 8.292 26.065 1.00 69.64 C ANISOU 249 CE2 PHE A 206 9008 8220 9233 113 -460 1892 C ATOM 250 CZ PHE A 206 26.216 8.892 27.101 1.00 67.07 C ANISOU 250 CZ PHE A 206 8742 7938 8804 111 -362 1840 C ATOM 251 N LEU A 207 24.436 11.370 22.728 1.00 54.75 N ANISOU 251 N LEU A 207 7085 6393 7322 320 -34 1702 N ATOM 252 CA LEU A 207 25.629 11.149 21.914 1.00 45.05 C ANISOU 252 CA LEU A 207 5898 5083 6135 342 -131 1508 C ATOM 253 C LEU A 207 26.224 12.463 21.409 1.00 40.55 C ANISOU 253 C LEU A 207 5367 4540 5500 410 24 1352 C ATOM 254 O LEU A 207 27.433 12.688 21.499 1.00 40.25 O ANISOU 254 O LEU A 207 5387 4480 5426 433 14 1200 O ATOM 255 CB LEU A 207 25.306 10.221 20.742 1.00 43.23 C ANISOU 255 CB LEU A 207 5627 4778 6020 315 -292 1521 C ATOM 256 CG LEU A 207 24.788 8.855 21.186 1.00 41.21 C ANISOU 256 CG LEU A 207 5344 4481 5833 240 -474 1672 C ATOM 257 CD1 LEU A 207 24.308 8.027 19.994 1.00 43.02 C ANISOU 257 CD1 LEU A 207 5548 4635 6163 205 -623 1702 C ATOM 258 CD2 LEU A 207 25.855 8.111 21.986 1.00 36.19 C ANISOU 258 CD2 LEU A 207 4755 3792 5205 223 -594 1605 C ATOM 259 N GLU A 208 25.358 13.327 20.892 1.00 36.08 N ANISOU 259 N GLU A 208 4764 4025 4920 439 161 1402 N ATOM 260 CA GLU A 208 25.755 14.640 20.406 1.00 43.65 C ANISOU 260 CA GLU A 208 5754 5013 5818 499 311 1277 C ATOM 261 C GLU A 208 26.524 15.453 21.447 1.00 51.66 C ANISOU 261 C GLU A 208 6856 6059 6712 524 424 1201 C ATOM 262 O GLU A 208 27.427 16.220 21.103 1.00 50.86 O ANISOU 262 O GLU A 208 6806 5955 6562 558 471 1049 O ATOM 263 CB GLU A 208 24.529 15.424 19.911 1.00 54.37 C ANISOU 263 CB GLU A 208 7051 6425 7184 521 450 1386 C ATOM 264 CG GLU A 208 24.211 15.226 18.427 1.00 59.70 C ANISOU 264 CG GLU A 208 7664 7069 7952 507 380 1369 C ATOM 265 CD GLU A 208 25.354 15.673 17.519 1.00 68.75 C ANISOU 265 CD GLU A 208 8847 8185 9090 537 362 1156 C ATOM 266 OE1 GLU A 208 25.328 16.834 17.047 1.00 71.49 O ANISOU 266 OE1 GLU A 208 9192 8571 9401 575 494 1102 O ATOM 267 OE2 GLU A 208 26.284 14.868 17.289 1.00 67.46 O ANISOU 267 OE2 GLU A 208 8712 7962 8957 524 217 1047 O ATOM 268 N LYS A 209 26.171 15.294 22.718 1.00 52.21 N ANISOU 268 N LYS A 209 6948 6163 6727 499 461 1312 N ATOM 269 CA LYS A 209 26.882 16.008 23.774 1.00 54.45 C ANISOU 269 CA LYS A 209 7331 6472 6885 506 560 1249 C ATOM 270 C LYS A 209 28.184 15.283 24.102 1.00 49.91 C ANISOU 270 C LYS A 209 6800 5848 6317 466 408 1152 C ATOM 271 O LYS A 209 29.219 15.909 24.330 1.00 50.18 O ANISOU 271 O LYS A 209 6912 5880 6273 475 444 1032 O ATOM 272 CB LYS A 209 26.011 16.146 25.026 1.00 61.20 C ANISOU 272 CB LYS A 209 8198 7388 7667 492 668 1403 C ATOM 273 CG LYS A 209 26.538 17.148 26.058 1.00 74.44 C ANISOU 273 CG LYS A 209 9997 9096 9193 503 814 1343 C ATOM 274 CD LYS A 209 26.558 18.574 25.502 1.00 82.68 C ANISOU 274 CD LYS A 209 11088 10151 10176 576 983 1249 C ATOM 275 CE LYS A 209 26.840 19.597 26.594 1.00 83.62 C ANISOU 275 CE LYS A 209 11343 10297 10134 587 1142 1215 C ATOM 276 NZ LYS A 209 25.810 19.544 27.671 1.00 81.90 N ANISOU 276 NZ LYS A 209 11126 10134 9860 585 1250 1371 N ATOM 277 N ALA A 210 28.125 13.957 24.107 1.00 47.06 N ANISOU 277 N ALA A 210 6387 5442 6051 420 232 1215 N ATOM 278 CA ALA A 210 29.287 13.147 24.443 1.00 45.59 C ANISOU 278 CA ALA A 210 6228 5203 5891 384 79 1145 C ATOM 279 C ALA A 210 30.411 13.293 23.418 1.00 43.37 C ANISOU 279 C ALA A 210 5960 4878 5642 427 27 968 C ATOM 280 O ALA A 210 31.586 13.355 23.783 1.00 47.34 O ANISOU 280 O ALA A 210 6512 5369 6106 420 -8 879 O ATOM 281 CB ALA A 210 28.888 11.684 24.605 1.00 43.78 C ANISOU 281 CB ALA A 210 5940 4927 5768 330 -102 1257 C ATOM 282 N VAL A 211 30.063 13.352 22.135 1.00 39.79 N ANISOU 282 N VAL A 211 5459 4407 5255 466 19 924 N ATOM 283 CA VAL A 211 31.101 13.418 21.108 1.00 34.58 C ANISOU 283 CA VAL A 211 4802 3712 4624 507 -35 759 C ATOM 284 C VAL A 211 31.743 14.800 21.021 1.00 39.63 C ANISOU 284 C VAL A 211 5494 4406 5158 543 104 651 C ATOM 285 O VAL A 211 32.674 14.995 20.245 1.00 48.55 O ANISOU 285 O VAL A 211 6626 5528 6294 575 72 517 O ATOM 286 CB VAL A 211 30.608 12.951 19.711 1.00 39.17 C ANISOU 286 CB VAL A 211 5322 4252 5307 525 -105 738 C ATOM 287 CG1 VAL A 211 29.847 11.628 19.820 1.00 43.53 C ANISOU 287 CG1 VAL A 211 5835 4748 5956 478 -247 864 C ATOM 288 CG2 VAL A 211 29.745 14.016 19.056 1.00 40.78 C ANISOU 288 CG2 VAL A 211 5501 4511 5482 547 41 758 C ATOM 289 N LYS A 212 31.254 15.753 21.813 1.00 40.95 N ANISOU 289 N LYS A 212 5707 4628 5223 538 257 709 N ATOM 290 CA LYS A 212 31.881 17.078 21.889 1.00 47.72 C ANISOU 290 CA LYS A 212 6636 5528 5966 562 382 615 C ATOM 291 C LYS A 212 33.038 17.101 22.886 1.00 47.91 C ANISOU 291 C LYS A 212 6742 5554 5909 526 349 576 C ATOM 292 O LYS A 212 33.879 18.000 22.845 1.00 46.62 O ANISOU 292 O LYS A 212 6640 5414 5659 535 401 483 O ATOM 293 CB LYS A 212 30.864 18.158 22.280 1.00 54.98 C ANISOU 293 CB LYS A 212 7586 6495 6807 581 569 687 C ATOM 294 CG LYS A 212 29.737 18.367 21.279 1.00 69.81 C ANISOU 294 CG LYS A 212 9383 8384 8757 615 624 736 C ATOM 295 CD LYS A 212 30.262 18.771 19.907 1.00 79.26 C ANISOU 295 CD LYS A 212 10549 9576 9991 645 598 607 C ATOM 296 CE LYS A 212 29.139 18.823 18.869 1.00 84.63 C ANISOU 296 CE LYS A 212 11139 10261 10755 659 627 669 C ATOM 297 NZ LYS A 212 28.540 17.481 18.585 1.00 82.53 N ANISOU 297 NZ LYS A 212 10800 9955 10602 625 491 760 N ATOM 298 N GLY A 213 33.068 16.117 23.784 1.00 43.94 N ANISOU 298 N GLY A 213 6235 5026 5432 475 257 658 N ATOM 299 CA GLY A 213 34.076 16.058 24.830 1.00 43.79 C ANISOU 299 CA GLY A 213 6287 5010 5341 422 218 650 C ATOM 300 C GLY A 213 35.420 15.526 24.362 1.00 43.00 C ANISOU 300 C GLY A 213 6166 4877 5294 428 81 553 C ATOM 301 O GLY A 213 35.688 15.437 23.162 1.00 35.13 O ANISOU 301 O GLY A 213 5116 3865 4366 483 39 463 O ATOM 302 N SER A 214 36.279 15.189 25.316 1.00 39.34 N ANISOU 302 N SER A 214 5744 4409 4796 369 13 576 N ATOM 303 CA SER A 214 37.565 14.589 25.002 1.00 49.66 C ANISOU 303 CA SER A 214 7020 5686 6161 375 -120 509 C ATOM 304 C SER A 214 37.332 13.139 24.621 1.00 50.76 C ANISOU 304 C SER A 214 7073 5756 6459 392 -271 540 C ATOM 305 O SER A 214 36.703 12.389 25.364 1.00 58.04 O ANISOU 305 O SER A 214 7981 6653 7418 342 -323 651 O ATOM 306 CB SER A 214 38.508 14.649 26.206 1.00 53.60 C ANISOU 306 CB SER A 214 7586 6202 6579 294 -151 549 C ATOM 307 OG SER A 214 38.522 15.942 26.779 1.00 51.09 O ANISOU 307 OG SER A 214 7375 5938 6099 260 -10 544 O ATOM 308 N LEU A 215 37.828 12.752 23.457 1.00 44.63 N ANISOU 308 N LEU A 215 6240 4945 5771 460 -343 442 N ATOM 309 CA LEU A 215 37.727 11.372 23.011 1.00 42.27 C ANISOU 309 CA LEU A 215 5877 4565 5620 483 -493 453 C ATOM 310 C LEU A 215 39.117 10.750 22.957 1.00 41.74 C ANISOU 310 C LEU A 215 5789 4463 5608 506 -609 396 C ATOM 311 O LEU A 215 40.071 11.371 22.467 1.00 37.82 O ANISOU 311 O LEU A 215 5296 4007 5067 547 -575 300 O ATOM 312 CB LEU A 215 37.064 11.309 21.632 1.00 39.03 C ANISOU 312 CB LEU A 215 5424 4130 5274 547 -484 390 C ATOM 313 CG LEU A 215 35.698 11.993 21.547 1.00 37.81 C ANISOU 313 CG LEU A 215 5275 4016 5074 532 -363 454 C ATOM 314 CD1 LEU A 215 35.126 11.948 20.137 1.00 33.01 C ANISOU 314 CD1 LEU A 215 4623 3388 4530 581 -363 396 C ATOM 315 CD2 LEU A 215 34.746 11.343 22.522 1.00 37.46 C ANISOU 315 CD2 LEU A 215 5227 3955 5052 468 -396 609 C ATOM 316 N THR A 216 39.234 9.529 23.469 1.00 42.82 N ANISOU 316 N THR A 216 5899 4529 5842 479 -748 464 N ATOM 317 CA THR A 216 40.476 8.785 23.342 1.00 45.13 C ANISOU 317 CA THR A 216 6159 4775 6215 515 -866 419 C ATOM 318 C THR A 216 40.512 8.211 21.943 1.00 41.12 C ANISOU 318 C THR A 216 5609 4205 5809 616 -921 311 C ATOM 319 O THR A 216 39.509 8.247 21.225 1.00 39.14 O ANISOU 319 O THR A 216 5358 3940 5575 633 -891 295 O ATOM 320 CB THR A 216 40.560 7.622 24.342 1.00 46.13 C ANISOU 320 CB THR A 216 6269 4836 6424 452 -1005 532 C ATOM 321 OG1 THR A 216 39.451 6.739 24.134 1.00 45.32 O ANISOU 321 OG1 THR A 216 6146 4662 6411 447 -1079 586 O ATOM 322 CG2 THR A 216 40.544 8.138 25.777 1.00 47.33 C ANISOU 322 CG2 THR A 216 6465 5051 6467 339 -955 643 C ATOM 323 N SER A 217 41.664 7.671 21.561 1.00 35.90 N ANISOU 323 N SER A 217 4916 3509 5216 680 -1001 243 N ATOM 324 CA SER A 217 41.830 7.091 20.238 1.00 34.82 C ANISOU 324 CA SER A 217 4749 3310 5169 783 -1052 128 C ATOM 325 C SER A 217 40.767 6.038 19.930 1.00 41.52 C ANISOU 325 C SER A 217 5603 4052 6121 778 -1146 164 C ATOM 326 O SER A 217 40.204 6.020 18.834 1.00 36.85 O ANISOU 326 O SER A 217 5015 3436 5548 821 -1131 93 O ATOM 327 CB SER A 217 43.214 6.467 20.104 1.00 38.18 C ANISOU 327 CB SER A 217 5137 3702 5667 854 -1136 78 C ATOM 328 OG SER A 217 43.344 5.835 18.845 1.00 40.82 O ANISOU 328 OG SER A 217 5455 3969 6087 960 -1182 -38 O ATOM 329 N TYR A 218 40.495 5.166 20.897 1.00 36.50 N ANISOU 329 N TYR A 218 4967 3353 5546 715 -1252 283 N ATOM 330 CA TYR A 218 39.603 4.036 20.656 1.00 38.95 C ANISOU 330 CA TYR A 218 5284 3554 5962 703 -1372 329 C ATOM 331 C TYR A 218 38.139 4.443 20.578 1.00 41.25 C ANISOU 331 C TYR A 218 5591 3878 6203 642 -1310 401 C ATOM 332 O TYR A 218 37.381 3.881 19.787 1.00 41.06 O ANISOU 332 O TYR A 218 5577 3786 6239 654 -1368 393 O ATOM 333 CB TYR A 218 39.787 2.940 21.707 1.00 37.72 C ANISOU 333 CB TYR A 218 5116 3321 5894 649 -1520 442 C ATOM 334 CG TYR A 218 39.029 1.680 21.367 1.00 39.40 C ANISOU 334 CG TYR A 218 5341 3404 6224 645 -1671 482 C ATOM 335 CD1 TYR A 218 39.255 1.019 20.168 1.00 39.13 C ANISOU 335 CD1 TYR A 218 5324 3269 6273 740 -1738 365 C ATOM 336 CD2 TYR A 218 38.081 1.155 22.241 1.00 38.99 C ANISOU 336 CD2 TYR A 218 5289 3333 6192 540 -1750 639 C ATOM 337 CE1 TYR A 218 38.560 -0.134 19.847 1.00 44.01 C ANISOU 337 CE1 TYR A 218 5973 3758 6991 728 -1885 401 C ATOM 338 CE2 TYR A 218 37.379 0.004 21.930 1.00 39.80 C ANISOU 338 CE2 TYR A 218 5407 3317 6397 524 -1903 687 C ATOM 339 CZ TYR A 218 37.630 -0.638 20.735 1.00 44.45 C ANISOU 339 CZ TYR A 218 6027 3795 7068 617 -1973 567 C ATOM 340 OH TYR A 218 36.946 -1.785 20.413 1.00 47.36 O ANISOU 340 OH TYR A 218 6429 4034 7530 595 -2134 614 O ATOM 341 N GLN A 219 37.735 5.405 21.403 1.00 38.66 N ANISOU 341 N GLN A 219 5270 3654 5765 575 -1192 478 N ATOM 342 CA GLN A 219 36.386 5.953 21.293 1.00 35.40 C ANISOU 342 CA GLN A 219 4864 3289 5298 532 -1104 546 C ATOM 343 C GLN A 219 36.174 6.522 19.897 1.00 35.52 C ANISOU 343 C GLN A 219 4879 3319 5300 598 -1029 431 C ATOM 344 O GLN A 219 35.116 6.339 19.301 1.00 35.42 O ANISOU 344 O GLN A 219 4860 3283 5314 582 -1038 470 O ATOM 345 CB GLN A 219 36.145 7.041 22.342 1.00 34.99 C ANISOU 345 CB GLN A 219 4830 3348 5117 472 -964 621 C ATOM 346 CG GLN A 219 36.173 6.519 23.766 1.00 45.52 C ANISOU 346 CG GLN A 219 6167 4680 6450 387 -1031 751 C ATOM 347 CD GLN A 219 36.015 7.619 24.797 1.00 46.20 C ANISOU 347 CD GLN A 219 6289 4872 6394 329 -885 810 C ATOM 348 OE1 GLN A 219 36.565 8.714 24.648 1.00 43.72 O ANISOU 348 OE1 GLN A 219 6008 4620 5984 357 -762 727 O ATOM 349 NE2 GLN A 219 35.270 7.328 25.859 1.00 44.27 N ANISOU 349 NE2 GLN A 219 6044 4648 6129 245 -900 956 N ATOM 350 N LYS A 220 37.185 7.216 19.379 1.00 35.06 N ANISOU 350 N LYS A 220 4821 3305 5197 661 -960 301 N ATOM 351 CA LYS A 220 37.101 7.787 18.041 1.00 36.56 C ANISOU 351 CA LYS A 220 5004 3518 5370 719 -891 185 C ATOM 352 C LYS A 220 37.009 6.655 17.031 1.00 39.69 C ANISOU 352 C LYS A 220 5400 3803 5878 761 -1019 128 C ATOM 353 O LYS A 220 36.184 6.687 16.114 1.00 38.71 O ANISOU 353 O LYS A 220 5278 3664 5765 756 -1008 115 O ATOM 354 CB LYS A 220 38.326 8.652 17.735 1.00 33.04 C ANISOU 354 CB LYS A 220 4553 3145 4856 775 -814 63 C ATOM 355 CG LYS A 220 38.368 10.001 18.454 1.00 38.86 C ANISOU 355 CG LYS A 220 5311 3994 5462 735 -671 96 C ATOM 356 CD LYS A 220 39.543 10.850 17.944 1.00 34.91 C ANISOU 356 CD LYS A 220 4804 3565 4894 787 -611 -24 C ATOM 357 CE LYS A 220 39.769 12.098 18.797 1.00 39.86 C ANISOU 357 CE LYS A 220 5471 4286 5387 739 -495 12 C ATOM 358 NZ LYS A 220 40.654 13.079 18.089 1.00 40.27 N ANISOU 358 NZ LYS A 220 5516 4419 5366 781 -431 -98 N ATOM 359 N PHE A 221 37.855 5.647 17.222 1.00 39.22 N ANISOU 359 N PHE A 221 5343 3661 5899 798 -1142 100 N ATOM 360 CA PHE A 221 37.898 4.480 16.345 1.00 35.76 C ANISOU 360 CA PHE A 221 4923 3097 5568 848 -1272 36 C ATOM 361 C PHE A 221 36.522 3.818 16.226 1.00 36.46 C ANISOU 361 C PHE A 221 5035 3115 5705 777 -1351 142 C ATOM 362 O PHE A 221 36.072 3.495 15.125 1.00 38.01 O ANISOU 362 O PHE A 221 5256 3255 5931 793 -1387 87 O ATOM 363 CB PHE A 221 38.938 3.483 16.864 1.00 37.82 C ANISOU 363 CB PHE A 221 5181 3275 5915 892 -1393 25 C ATOM 364 CG PHE A 221 39.166 2.303 15.959 1.00 43.19 C ANISOU 364 CG PHE A 221 5892 3815 6702 964 -1519 -61 C ATOM 365 CD1 PHE A 221 40.154 2.340 14.984 1.00 42.30 C ANISOU 365 CD1 PHE A 221 5776 3698 6598 1077 -1493 -221 C ATOM 366 CD2 PHE A 221 38.402 1.153 16.090 1.00 49.39 C ANISOU 366 CD2 PHE A 221 6714 4474 7576 919 -1666 20 C ATOM 367 CE1 PHE A 221 40.375 1.252 14.151 1.00 43.01 C ANISOU 367 CE1 PHE A 221 5909 3654 6781 1153 -1600 -309 C ATOM 368 CE2 PHE A 221 38.620 0.050 15.265 1.00 49.08 C ANISOU 368 CE2 PHE A 221 6725 4292 7633 986 -1787 -64 C ATOM 369 CZ PHE A 221 39.608 0.100 14.294 1.00 43.02 C ANISOU 369 CZ PHE A 221 5963 3514 6870 1107 -1748 -235 C ATOM 370 N GLN A 222 35.858 3.627 17.363 1.00 36.40 N ANISOU 370 N GLN A 222 5019 3116 5695 692 -1382 301 N ATOM 371 CA GLN A 222 34.537 3.001 17.400 1.00 36.87 C ANISOU 371 CA GLN A 222 5090 3125 5795 614 -1465 434 C ATOM 372 C GLN A 222 33.469 3.844 16.717 1.00 40.11 C ANISOU 372 C GLN A 222 5490 3606 6144 583 -1353 462 C ATOM 373 O GLN A 222 32.612 3.314 16.007 1.00 40.47 O ANISOU 373 O GLN A 222 5553 3590 6231 549 -1427 502 O ATOM 374 CB GLN A 222 34.117 2.759 18.844 1.00 44.52 C ANISOU 374 CB GLN A 222 6038 4118 6758 530 -1501 604 C ATOM 375 CG GLN A 222 34.894 1.677 19.543 1.00 38.39 C ANISOU 375 CG GLN A 222 5267 3251 6068 532 -1653 621 C ATOM 376 CD GLN A 222 34.530 1.570 21.003 1.00 40.46 C ANISOU 376 CD GLN A 222 5504 3559 6310 438 -1676 788 C ATOM 377 OE1 GLN A 222 34.771 2.492 21.775 1.00 40.22 O ANISOU 377 OE1 GLN A 222 5459 3638 6187 417 -1550 810 O ATOM 378 NE2 GLN A 222 33.953 0.436 21.393 1.00 43.92 N ANISOU 378 NE2 GLN A 222 5944 3914 6829 374 -1842 908 N ATOM 379 N LEU A 223 33.512 5.156 16.953 1.00 36.34 N ANISOU 379 N LEU A 223 4987 3254 5566 588 -1181 450 N ATOM 380 CA LEU A 223 32.570 6.082 16.329 1.00 35.77 C ANISOU 380 CA LEU A 223 4897 3257 5439 566 -1059 476 C ATOM 381 C LEU A 223 32.756 6.065 14.831 1.00 35.31 C ANISOU 381 C LEU A 223 4852 3162 5404 611 -1071 341 C ATOM 382 O LEU A 223 31.787 6.020 14.079 1.00 40.33 O ANISOU 382 O LEU A 223 5485 3784 6055 569 -1080 389 O ATOM 383 CB LEU A 223 32.785 7.506 16.848 1.00 42.04 C ANISOU 383 CB LEU A 223 5673 4178 6122 577 -876 464 C ATOM 384 CG LEU A 223 32.222 7.808 18.232 1.00 45.92 C ANISOU 384 CG LEU A 223 6156 4729 6561 519 -818 617 C ATOM 385 CD1 LEU A 223 32.895 9.036 18.831 1.00 45.37 C ANISOU 385 CD1 LEU A 223 6102 4755 6382 541 -667 564 C ATOM 386 CD2 LEU A 223 30.711 7.993 18.145 1.00 44.78 C ANISOU 386 CD2 LEU A 223 5984 4618 6412 465 -772 764 C ATOM 387 N PHE A 224 34.013 6.096 14.395 1.00 37.93 N ANISOU 387 N PHE A 224 5194 3481 5735 691 -1072 179 N ATOM 388 CA PHE A 224 34.313 6.006 12.973 1.00 43.17 C ANISOU 388 CA PHE A 224 5874 4112 6417 740 -1086 36 C ATOM 389 C PHE A 224 33.690 4.742 12.381 1.00 45.12 C ANISOU 389 C PHE A 224 6167 4225 6751 710 -1243 65 C ATOM 390 O PHE A 224 33.093 4.784 11.308 1.00 36.31 O ANISOU 390 O PHE A 224 5067 3094 5636 685 -1244 42 O ATOM 391 CB PHE A 224 35.818 6.018 12.718 1.00 38.31 C ANISOU 391 CB PHE A 224 5259 3499 5798 839 -1082 -126 C ATOM 392 CG PHE A 224 36.497 7.293 13.152 1.00 42.99 C ANISOU 392 CG PHE A 224 5816 4223 6297 861 -941 -161 C ATOM 393 CD1 PHE A 224 35.781 8.472 13.264 1.00 40.66 C ANISOU 393 CD1 PHE A 224 5499 4028 5921 813 -809 -103 C ATOM 394 CD2 PHE A 224 37.856 7.312 13.427 1.00 44.64 C ANISOU 394 CD2 PHE A 224 6014 4451 6495 929 -943 -245 C ATOM 395 CE1 PHE A 224 36.402 9.647 13.652 1.00 43.87 C ANISOU 395 CE1 PHE A 224 5890 4544 6236 829 -688 -137 C ATOM 396 CE2 PHE A 224 38.488 8.480 13.814 1.00 42.62 C ANISOU 396 CE2 PHE A 224 5735 4313 6145 937 -827 -267 C ATOM 397 CZ PHE A 224 37.757 9.651 13.929 1.00 47.23 C ANISOU 397 CZ PHE A 224 6313 4988 6645 884 -702 -217 C ATOM 398 N GLU A 225 33.817 3.627 13.095 1.00 39.96 N ANISOU 398 N GLU A 225 5541 3474 6170 702 -1380 125 N ATOM 399 CA GLU A 225 33.338 2.346 12.591 1.00 44.63 C ANISOU 399 CA GLU A 225 6192 3920 6843 675 -1549 149 C ATOM 400 C GLU A 225 31.815 2.250 12.571 1.00 43.97 C ANISOU 400 C GLU A 225 6109 3838 6761 561 -1583 322 C ATOM 401 O GLU A 225 31.235 1.777 11.599 1.00 43.91 O ANISOU 401 O GLU A 225 6148 3757 6777 525 -1657 317 O ATOM 402 CB GLU A 225 33.915 1.191 13.418 1.00 53.57 C ANISOU 402 CB GLU A 225 7351 4946 8059 696 -1694 174 C ATOM 403 CG GLU A 225 35.330 0.824 13.041 1.00 77.59 C ANISOU 403 CG GLU A 225 10413 7931 11137 816 -1716 -1 C ATOM 404 CD GLU A 225 35.469 0.540 11.557 1.00 94.79 C ANISOU 404 CD GLU A 225 12650 10039 13326 870 -1737 -151 C ATOM 405 OE1 GLU A 225 34.545 -0.081 10.979 1.00 96.21 O ANISOU 405 OE1 GLU A 225 12891 10131 13534 807 -1833 -104 O ATOM 406 OE2 GLU A 225 36.500 0.939 10.971 1.00100.01 O ANISOU 406 OE2 GLU A 225 13299 10738 13962 970 -1660 -309 O ATOM 407 N GLN A 226 31.177 2.694 13.650 1.00 37.97 N ANISOU 407 N GLN A 226 5296 3162 5968 501 -1527 482 N ATOM 408 CA GLN A 226 29.746 2.490 13.823 1.00 38.15 C ANISOU 408 CA GLN A 226 5304 3192 5998 394 -1570 678 C ATOM 409 C GLN A 226 28.915 3.546 13.092 1.00 39.91 C ANISOU 409 C GLN A 226 5490 3513 6163 362 -1434 711 C ATOM 410 O GLN A 226 27.832 3.252 12.580 1.00 45.23 O ANISOU 410 O GLN A 226 6167 4163 6856 282 -1492 827 O ATOM 411 CB GLN A 226 29.386 2.433 15.317 1.00 40.09 C ANISOU 411 CB GLN A 226 5508 3491 6235 346 -1573 846 C ATOM 412 CG GLN A 226 30.034 1.228 16.057 1.00 45.94 C ANISOU 412 CG GLN A 226 6280 4124 7049 352 -1741 851 C ATOM 413 CD GLN A 226 29.753 1.198 17.558 1.00 49.42 C ANISOU 413 CD GLN A 226 6676 4627 7474 295 -1743 1012 C ATOM 414 OE1 GLN A 226 28.673 1.572 18.014 1.00 65.11 O ANISOU 414 OE1 GLN A 226 8620 6699 9420 225 -1689 1176 O ATOM 415 NE2 GLN A 226 30.733 0.744 18.329 1.00 48.30 N ANISOU 415 NE2 GLN A 226 6540 4447 7364 324 -1803 970 N ATOM 416 N VAL A 227 29.431 4.768 13.025 1.00 40.90 N ANISOU 416 N VAL A 227 5578 3744 6219 419 -1261 615 N ATOM 417 CA VAL A 227 28.669 5.883 12.474 1.00 39.65 C ANISOU 417 CA VAL A 227 5373 3685 6008 392 -1119 656 C ATOM 418 C VAL A 227 28.938 6.132 10.980 1.00 44.04 C ANISOU 418 C VAL A 227 5948 4224 6560 412 -1105 509 C ATOM 419 O VAL A 227 28.008 6.385 10.211 1.00 51.16 O ANISOU 419 O VAL A 227 6832 5144 7461 349 -1088 580 O ATOM 420 CB VAL A 227 28.885 7.189 13.291 1.00 36.39 C ANISOU 420 CB VAL A 227 4912 3403 5513 428 -932 661 C ATOM 421 CG1 VAL A 227 28.115 8.341 12.670 1.00 33.33 C ANISOU 421 CG1 VAL A 227 4475 3107 5081 408 -788 699 C ATOM 422 CG2 VAL A 227 28.465 6.991 14.746 1.00 34.39 C ANISOU 422 CG2 VAL A 227 4641 3177 5250 394 -935 821 C ATOM 423 N ILE A 228 30.198 6.063 10.564 1.00 36.44 N ANISOU 423 N ILE A 228 5017 3234 5595 496 -1112 314 N ATOM 424 CA ILE A 228 30.519 6.328 9.168 1.00 39.55 C ANISOU 424 CA ILE A 228 5426 3626 5975 518 -1091 168 C ATOM 425 C ILE A 228 31.350 5.221 8.534 1.00 40.79 C ANISOU 425 C ILE A 228 5659 3659 6180 571 -1224 23 C ATOM 426 O ILE A 228 32.009 5.441 7.516 1.00 46.84 O ANISOU 426 O ILE A 228 6440 4433 6925 620 -1195 -139 O ATOM 427 CB ILE A 228 31.274 7.661 8.995 1.00 40.96 C ANISOU 427 CB ILE A 228 5557 3928 6079 579 -928 51 C ATOM 428 CG1 ILE A 228 32.666 7.574 9.623 1.00 42.30 C ANISOU 428 CG1 ILE A 228 5736 4099 6236 674 -926 -65 C ATOM 429 CG2 ILE A 228 30.483 8.810 9.590 1.00 38.45 C ANISOU 429 CG2 ILE A 228 5177 3722 5710 539 -787 180 C ATOM 430 CD1 ILE A 228 33.493 8.824 9.414 1.00 49.42 C ANISOU 430 CD1 ILE A 228 6598 5119 7060 728 -787 -178 C ATOM 431 N GLY A 229 31.307 4.034 9.129 1.00 39.48 N ANISOU 431 N GLY A 229 5542 3380 6080 562 -1368 83 N ATOM 432 CA GLY A 229 32.134 2.928 8.679 1.00 42.58 C ANISOU 432 CA GLY A 229 6012 3639 6526 626 -1495 -49 C ATOM 433 C GLY A 229 31.449 1.915 7.777 1.00 48.25 C ANISOU 433 C GLY A 229 6821 4225 7289 564 -1641 -33 C ATOM 434 O GLY A 229 32.098 1.321 6.914 1.00 46.33 O ANISOU 434 O GLY A 229 6651 3889 7062 623 -1700 -188 O ATOM 435 N ARG A 230 30.150 1.696 7.971 1.00 53.81 N ANISOU 435 N ARG A 230 7384 5209 7854 881 -2179 -608 N ATOM 436 CA ARG A 230 29.417 0.763 7.107 1.00 62.03 C ANISOU 436 CA ARG A 230 8614 6011 8943 879 -2479 -603 C ATOM 437 C ARG A 230 28.278 1.435 6.342 1.00 64.66 C ANISOU 437 C ARG A 230 8963 6301 9305 765 -2519 -514 C ATOM 438 O ARG A 230 27.461 2.148 6.927 1.00 63.98 O ANISOU 438 O ARG A 230 8708 6295 9305 627 -2428 -337 O ATOM 439 CB ARG A 230 28.914 -0.449 7.892 1.00 75.24 C ANISOU 439 CB ARG A 230 10286 7523 10780 804 -2727 -469 C ATOM 440 CG ARG A 230 28.554 -0.159 9.340 1.00 87.11 C ANISOU 440 CG ARG A 230 11539 9142 12418 676 -2616 -278 C ATOM 441 CD ARG A 230 28.482 -1.451 10.138 1.00 91.07 C ANISOU 441 CD ARG A 230 12039 9515 13050 645 -2838 -196 C ATOM 442 NE ARG A 230 28.193 -1.225 11.551 1.00 94.45 N ANISOU 442 NE ARG A 230 12226 10060 13600 543 -2728 -14 N ATOM 443 CZ ARG A 230 29.116 -1.171 12.505 1.00 96.72 C ANISOU 443 CZ ARG A 230 12412 10467 13869 594 -2555 -72 C ATOM 444 NH1 ARG A 230 30.399 -1.330 12.200 1.00 97.63 N ANISOU 444 NH1 ARG A 230 12623 10618 13853 742 -2469 -287 N ATOM 445 NH2 ARG A 230 28.757 -0.972 13.767 1.00 98.41 N ANISOU 445 NH2 ARG A 230 12429 10771 14192 506 -2471 103 N ATOM 446 N LYS A 231 28.231 1.184 5.034 1.00 64.15 N ANISOU 446 N LYS A 231 9114 6105 9156 838 -2656 -630 N ATOM 447 CA LYS A 231 27.364 1.925 4.122 1.00 65.00 C ANISOU 447 CA LYS A 231 9252 6188 9256 752 -2662 -588 C ATOM 448 C LYS A 231 25.908 2.018 4.561 1.00 58.80 C ANISOU 448 C LYS A 231 8348 5345 8650 540 -2774 -314 C ATOM 449 O LYS A 231 25.319 3.089 4.507 1.00 48.67 O ANISOU 449 O LYS A 231 6942 4178 7371 455 -2617 -225 O ATOM 450 CB LYS A 231 27.431 1.359 2.702 1.00 65.89 C ANISOU 450 CB LYS A 231 9652 6111 9271 859 -2862 -734 C ATOM 451 CG LYS A 231 26.626 2.184 1.698 1.00 69.42 C ANISOU 451 CG LYS A 231 10133 6541 9703 771 -2851 -708 C ATOM 452 CD LYS A 231 26.480 1.477 0.361 1.00 75.63 C ANISOU 452 CD LYS A 231 11234 7086 10417 851 -3110 -813 C ATOM 453 CE LYS A 231 27.834 1.243 -0.294 1.00 81.74 C ANISOU 453 CE LYS A 231 12175 7902 10979 1128 -3030 -1076 C ATOM 454 NZ LYS A 231 28.505 2.518 -0.676 1.00 84.37 N ANISOU 454 NZ LYS A 231 12376 8501 11180 1199 -2708 -1192 N ATOM 455 N ASP A 232 25.333 0.901 4.985 1.00 59.66 N ANISOU 455 N ASP A 232 8492 5282 8896 460 -3050 -163 N ATOM 456 CA ASP A 232 23.910 0.865 5.321 1.00 64.36 C ANISOU 456 CA ASP A 232 8968 5826 9660 259 -3196 146 C ATOM 457 C ASP A 232 23.552 1.677 6.566 1.00 56.03 C ANISOU 457 C ASP A 232 7618 4995 8676 191 -2954 334 C ATOM 458 O ASP A 232 22.570 2.418 6.570 1.00 57.52 O ANISOU 458 O ASP A 232 7682 5261 8912 90 -2887 528 O ATOM 459 CB ASP A 232 23.414 -0.583 5.448 1.00 73.84 C ANISOU 459 CB ASP A 232 10286 6785 10986 178 -3592 285 C ATOM 460 CG ASP A 232 24.523 -1.553 5.828 1.00 84.84 C ANISOU 460 CG ASP A 232 11795 8109 12329 321 -3660 104 C ATOM 461 OD1 ASP A 232 24.672 -2.576 5.126 1.00 92.79 O ANISOU 461 OD1 ASP A 232 13082 8877 13298 377 -3954 13 O ATOM 462 OD2 ASP A 232 25.248 -1.296 6.816 1.00 83.14 O ANISOU 462 OD2 ASP A 232 11413 8072 12106 384 -3429 55 O ATOM 463 N ASP A 233 24.344 1.529 7.621 1.00 54.74 N ANISOU 463 N ASP A 233 7357 4934 8510 259 -2824 282 N ATOM 464 CA ASP A 233 24.112 2.261 8.860 1.00 51.48 C ANISOU 464 CA ASP A 233 6703 4718 8139 225 -2597 443 C ATOM 465 C ASP A 233 24.384 3.744 8.656 1.00 50.23 C ANISOU 465 C ASP A 233 6503 4742 7841 275 -2282 348 C ATOM 466 O ASP A 233 23.701 4.596 9.222 1.00 45.10 O ANISOU 466 O ASP A 233 5709 4221 7206 232 -2129 524 O ATOM 467 CB ASP A 233 25.002 1.709 9.975 1.00 49.17 C ANISOU 467 CB ASP A 233 6348 4468 7868 286 -2548 387 C ATOM 468 CG ASP A 233 24.527 0.352 10.481 1.00 55.25 C ANISOU 468 CG ASP A 233 7105 5088 8801 207 -2849 550 C ATOM 469 OD1 ASP A 233 23.482 -0.132 9.992 1.00 58.81 O ANISOU 469 OD1 ASP A 233 7592 5405 9347 94 -3107 731 O ATOM 470 OD2 ASP A 233 25.192 -0.223 11.369 1.00 53.31 O ANISOU 470 OD2 ASP A 233 6812 4857 8587 247 -2842 511 O ATOM 471 N PHE A 234 25.395 4.044 7.848 1.00 50.28 N ANISOU 471 N PHE A 234 6642 4762 7699 377 -2194 80 N ATOM 472 CA PHE A 234 25.719 5.422 7.518 1.00 49.82 C ANISOU 472 CA PHE A 234 6566 4864 7498 411 -1935 -18 C ATOM 473 C PHE A 234 24.560 6.077 6.773 1.00 46.91 C ANISOU 473 C PHE A 234 6197 4479 7146 325 -1953 99 C ATOM 474 O PHE A 234 24.187 7.216 7.060 1.00 43.39 O ANISOU 474 O PHE A 234 5663 4173 6652 304 -1757 178 O ATOM 475 CB PHE A 234 26.984 5.495 6.664 1.00 44.95 C ANISOU 475 CB PHE A 234 6082 4272 6725 535 -1876 -295 C ATOM 476 CG PHE A 234 27.153 6.813 5.958 1.00 40.24 C ANISOU 476 CG PHE A 234 5496 3805 5989 545 -1687 -387 C ATOM 477 CD1 PHE A 234 27.614 7.922 6.643 1.00 38.32 C ANISOU 477 CD1 PHE A 234 5160 3746 5656 543 -1449 -384 C ATOM 478 CD2 PHE A 234 26.830 6.944 4.614 1.00 40.77 C ANISOU 478 CD2 PHE A 234 5682 3798 6011 548 -1766 -468 C ATOM 479 CE1 PHE A 234 27.765 9.142 6.002 1.00 43.56 C ANISOU 479 CE1 PHE A 234 5843 4521 6185 539 -1301 -460 C ATOM 480 CE2 PHE A 234 26.974 8.163 3.965 1.00 42.99 C ANISOU 480 CE2 PHE A 234 5963 4203 6168 548 -1599 -550 C ATOM 481 CZ PHE A 234 27.443 9.262 4.660 1.00 45.59 C ANISOU 481 CZ PHE A 234 6194 4720 6408 540 -1371 -544 C ATOM 482 N LEU A 235 24.004 5.352 5.807 1.00 48.19 N ANISOU 482 N LEU A 235 6479 4462 7367 280 -2198 113 N ATOM 483 CA LEU A 235 22.853 5.837 5.052 1.00 55.77 C ANISOU 483 CA LEU A 235 7442 5387 8363 179 -2250 248 C ATOM 484 C LEU A 235 21.621 5.939 5.940 1.00 49.41 C ANISOU 484 C LEU A 235 6449 4635 7691 71 -2262 589 C ATOM 485 O LEU A 235 20.833 6.864 5.807 1.00 46.77 O ANISOU 485 O LEU A 235 6034 4395 7342 27 -2144 723 O ATOM 486 CB LEU A 235 22.563 4.933 3.853 1.00 55.76 C ANISOU 486 CB LEU A 235 7640 5151 8393 147 -2547 201 C ATOM 487 CG LEU A 235 23.581 5.001 2.714 1.00 64.55 C ANISOU 487 CG LEU A 235 8952 6225 9347 279 -2521 -113 C ATOM 488 CD1 LEU A 235 23.112 4.180 1.519 1.00 72.22 C ANISOU 488 CD1 LEU A 235 10155 6944 10341 250 -2827 -133 C ATOM 489 CD2 LEU A 235 23.845 6.446 2.303 1.00 61.12 C ANISOU 489 CD2 LEU A 235 8460 5978 8783 307 -2240 -221 C ATOM 490 N LYS A 236 21.463 4.981 6.845 1.00 43.86 N ANISOU 490 N LYS A 236 5671 3884 7110 40 -2405 741 N ATOM 491 CA LYS A 236 20.332 4.976 7.762 1.00 46.87 C ANISOU 491 CA LYS A 236 5851 4341 7617 -44 -2424 1098 C ATOM 492 C LYS A 236 20.371 6.199 8.687 1.00 44.39 C ANISOU 492 C LYS A 236 5393 4257 7215 36 -2088 1150 C ATOM 493 O LYS A 236 19.359 6.863 8.918 1.00 49.17 O ANISOU 493 O LYS A 236 5877 4972 7835 11 -1998 1396 O ATOM 494 CB LYS A 236 20.347 3.677 8.571 1.00 61.33 C ANISOU 494 CB LYS A 236 7636 6082 9585 -83 -2645 1221 C ATOM 495 CG LYS A 236 19.054 3.354 9.292 1.00 77.39 C ANISOU 495 CG LYS A 236 9468 8162 11776 -195 -2767 1639 C ATOM 496 CD LYS A 236 19.059 3.901 10.709 1.00 88.57 C ANISOU 496 CD LYS A 236 10680 9792 13182 -116 -2515 1773 C ATOM 497 CE LYS A 236 17.945 3.280 11.543 1.00 94.94 C ANISOU 497 CE LYS A 236 11274 10647 14153 -206 -2672 2196 C ATOM 498 NZ LYS A 236 16.595 3.629 11.012 1.00 95.84 N ANISOU 498 NZ LYS A 236 11294 10804 14316 -301 -2742 2516 N ATOM 499 N LEU A 237 21.548 6.504 9.210 1.00 38.89 N ANISOU 499 N LEU A 237 4729 3632 6415 139 -1909 929 N ATOM 500 CA LEU A 237 21.680 7.628 10.122 1.00 41.99 C ANISOU 500 CA LEU A 237 5040 4209 6704 216 -1623 966 C ATOM 501 C LEU A 237 21.598 8.958 9.377 1.00 41.06 C ANISOU 501 C LEU A 237 4991 4173 6439 241 -1444 873 C ATOM 502 O LEU A 237 20.962 9.899 9.847 1.00 38.42 O ANISOU 502 O LEU A 237 4592 3962 6045 276 -1277 1029 O ATOM 503 CB LEU A 237 22.980 7.526 10.924 1.00 39.76 C ANISOU 503 CB LEU A 237 4782 3965 6358 293 -1517 782 C ATOM 504 CG LEU A 237 23.019 6.419 11.979 1.00 43.13 C ANISOU 504 CG LEU A 237 5111 4353 6922 281 -1637 903 C ATOM 505 CD1 LEU A 237 24.210 6.639 12.883 1.00 38.67 C ANISOU 505 CD1 LEU A 237 4557 3862 6275 357 -1473 755 C ATOM 506 CD2 LEU A 237 21.732 6.395 12.797 1.00 42.18 C ANISOU 506 CD2 LEU A 237 4819 4302 6907 251 -1652 1262 C ATOM 507 N SER A 238 22.233 9.023 8.210 1.00 44.99 N ANISOU 507 N SER A 238 5626 4602 6866 236 -1482 624 N ATOM 508 CA SER A 238 22.219 10.237 7.390 1.00 42.18 C ANISOU 508 CA SER A 238 5338 4315 6372 246 -1336 517 C ATOM 509 C SER A 238 20.813 10.691 6.998 1.00 43.38 C ANISOU 509 C SER A 238 5431 4481 6571 183 -1349 746 C ATOM 510 O SER A 238 20.545 11.895 6.913 1.00 39.06 O ANISOU 510 O SER A 238 4890 4044 5909 212 -1167 758 O ATOM 511 CB SER A 238 23.073 10.044 6.132 1.00 39.99 C ANISOU 511 CB SER A 238 5204 3960 6029 256 -1408 238 C ATOM 512 OG SER A 238 24.453 10.022 6.458 1.00 47.58 O ANISOU 512 OG SER A 238 6205 4976 6895 335 -1324 37 O ATOM 513 N THR A 239 19.925 9.729 6.745 1.00 42.84 N ANISOU 513 N THR A 239 5315 4298 6664 93 -1577 939 N ATOM 514 CA THR A 239 18.552 10.029 6.325 1.00 48.10 C ANISOU 514 CA THR A 239 5907 4977 7392 14 -1621 1201 C ATOM 515 C THR A 239 17.608 10.147 7.518 1.00 54.27 C ANISOU 515 C THR A 239 6499 5891 8232 39 -1548 1558 C ATOM 516 O THR A 239 16.394 10.281 7.362 1.00 52.79 O ANISOU 516 O THR A 239 6205 5743 8108 -17 -1588 1853 O ATOM 517 CB THR A 239 17.994 8.956 5.359 1.00 50.06 C ANISOU 517 CB THR A 239 6212 5028 7781 -119 -1941 1274 C ATOM 518 OG1 THR A 239 18.152 7.649 5.937 1.00 47.84 O ANISOU 518 OG1 THR A 239 5913 4641 7624 -149 -2156 1348 O ATOM 519 CG2 THR A 239 18.711 9.016 4.012 1.00 46.27 C ANISOU 519 CG2 THR A 239 5935 4430 7218 -117 -1993 952 C ATOM 520 N ASN A 240 18.173 10.090 8.716 1.00 57.21 N ANISOU 520 N ASN A 240 6823 6339 8575 131 -1439 1548 N ATOM 521 CA ASN A 240 17.366 10.129 9.921 1.00 51.67 C ANISOU 521 CA ASN A 240 5946 5769 7917 185 -1366 1883 C ATOM 522 C ASN A 240 17.299 11.528 10.511 1.00 48.37 C ANISOU 522 C ASN A 240 5541 5523 7315 333 -1062 1904 C ATOM 523 O ASN A 240 18.300 12.254 10.533 1.00 44.65 O ANISOU 523 O ASN A 240 5209 5065 6691 399 -912 1626 O ATOM 524 CB ASN A 240 17.909 9.148 10.958 1.00 48.81 C ANISOU 524 CB ASN A 240 5525 5379 7643 199 -1449 1896 C ATOM 525 CG ASN A 240 17.006 9.025 12.163 1.00 52.24 C ANISOU 525 CG ASN A 240 5758 5949 8141 252 -1408 2275 C ATOM 526 OD1 ASN A 240 17.283 9.593 13.223 1.00 49.72 O ANISOU 526 OD1 ASN A 240 5419 5750 7721 389 -1200 2290 O ATOM 527 ND2 ASN A 240 15.900 8.304 11.999 1.00 51.20 N ANISOU 527 ND2 ASN A 240 5481 5805 8167 146 -1615 2606 N ATOM 528 N ILE A 241 16.113 11.892 10.995 1.00 47.66 N ANISOU 528 N ILE A 241 5313 5567 7230 390 -985 2254 N ATOM 529 CA ILE A 241 15.864 13.210 11.588 1.00 51.33 C ANISOU 529 CA ILE A 241 5811 6191 7499 565 -706 2322 C ATOM 530 C ILE A 241 16.829 13.567 12.723 1.00 46.48 C ANISOU 530 C ILE A 241 5290 5614 6757 699 -549 2173 C ATOM 531 O ILE A 241 17.261 14.715 12.846 1.00 48.17 O ANISOU 531 O ILE A 241 5662 5872 6767 803 -361 2023 O ATOM 532 CB ILE A 241 14.401 13.342 12.089 1.00 46.78 C ANISOU 532 CB ILE A 241 5045 5776 6954 643 -655 2784 C ATOM 533 CG1 ILE A 241 14.212 14.651 12.857 1.00 55.95 C ANISOU 533 CG1 ILE A 241 6280 7096 7882 878 -361 2851 C ATOM 534 CG2 ILE A 241 14.002 12.139 12.945 1.00 40.61 C ANISOU 534 CG2 ILE A 241 4060 5017 6352 611 -809 3070 C ATOM 535 CD1 ILE A 241 12.754 15.046 13.041 1.00 64.69 C ANISOU 535 CD1 ILE A 241 7230 8384 8967 988 -270 3285 C ATOM 536 N PHE A 242 17.160 12.587 13.554 1.00 46.91 N ANISOU 536 N PHE A 242 5256 5640 6926 686 -642 2222 N ATOM 537 CA PHE A 242 18.093 12.823 14.648 1.00 51.92 C ANISOU 537 CA PHE A 242 5976 6295 7458 792 -516 2092 C ATOM 538 C PHE A 242 19.508 12.447 14.234 1.00 48.11 C ANISOU 538 C PHE A 242 5615 5683 6983 695 -595 1723 C ATOM 539 O PHE A 242 20.456 13.191 14.485 1.00 47.02 O ANISOU 539 O PHE A 242 5631 5550 6685 748 -467 1512 O ATOM 540 CB PHE A 242 17.685 12.031 15.891 1.00 52.39 C ANISOU 540 CB PHE A 242 5863 6416 7627 848 -549 2363 C ATOM 541 CG PHE A 242 16.286 12.314 16.354 1.00 60.18 C ANISOU 541 CG PHE A 242 6695 7567 8605 965 -470 2777 C ATOM 542 CD1 PHE A 242 15.900 13.604 16.684 1.00 65.06 C ANISOU 542 CD1 PHE A 242 7413 8305 9002 1161 -230 2854 C ATOM 543 CD2 PHE A 242 15.358 11.292 16.465 1.00 60.71 C ANISOU 543 CD2 PHE A 242 6522 7673 8873 888 -645 3110 C ATOM 544 CE1 PHE A 242 14.613 13.871 17.110 1.00 65.46 C ANISOU 544 CE1 PHE A 242 7317 8530 9024 1305 -139 3257 C ATOM 545 CE2 PHE A 242 14.069 11.550 16.893 1.00 67.61 C ANISOU 545 CE2 PHE A 242 7224 8731 9734 1005 -568 3536 C ATOM 546 CZ PHE A 242 13.695 12.843 17.215 1.00 68.71 C ANISOU 546 CZ PHE A 242 7455 9008 9645 1228 -301 3611 C ATOM 547 N GLY A 243 19.629 11.297 13.578 1.00 47.31 N ANISOU 547 N GLY A 243 5454 5466 7054 559 -818 1669 N ATOM 548 CA GLY A 243 20.916 10.709 13.251 1.00 38.11 C ANISOU 548 CA GLY A 243 4381 4191 5909 497 -909 1365 C ATOM 549 C GLY A 243 21.832 11.551 12.383 1.00 41.72 C ANISOU 549 C GLY A 243 5008 4636 6210 494 -821 1062 C ATOM 550 O GLY A 243 23.055 11.481 12.519 1.00 45.16 O ANISOU 550 O GLY A 243 5521 5051 6588 500 -798 843 O ATOM 551 N ASN A 244 21.253 12.346 11.490 1.00 39.98 N ANISOU 551 N ASN A 244 4833 4439 5919 482 -775 1067 N ATOM 552 CA ASN A 244 22.060 13.113 10.551 1.00 38.67 C ANISOU 552 CA ASN A 244 4811 4267 5613 465 -715 796 C ATOM 553 C ASN A 244 23.003 14.085 11.259 1.00 38.65 C ANISOU 553 C ASN A 244 4918 4342 5424 535 -541 674 C ATOM 554 O ASN A 244 24.056 14.430 10.727 1.00 44.55 O ANISOU 554 O ASN A 244 5762 5090 6075 509 -525 445 O ATOM 555 CB ASN A 244 21.173 13.856 9.549 1.00 35.79 C ANISOU 555 CB ASN A 244 4469 3922 5208 438 -690 845 C ATOM 556 CG ASN A 244 20.572 15.120 10.132 1.00 39.47 C ANISOU 556 CG ASN A 244 4966 4507 5524 537 -491 985 C ATOM 557 OD1 ASN A 244 21.202 16.177 10.130 1.00 40.89 O ANISOU 557 OD1 ASN A 244 5284 4732 5521 577 -364 833 O ATOM 558 ND2 ASN A 244 19.344 15.020 10.629 1.00 40.14 N ANISOU 558 ND2 ASN A 244 4932 4646 5673 584 -475 1293 N ATOM 559 N TYR A 245 22.620 14.521 12.456 1.00 36.12 N ANISOU 559 N TYR A 245 4590 4088 5047 628 -424 848 N ATOM 560 CA TYR A 245 23.463 15.399 13.260 1.00 34.78 C ANISOU 560 CA TYR A 245 4558 3961 4694 691 -290 764 C ATOM 561 C TYR A 245 24.696 14.656 13.761 1.00 40.22 C ANISOU 561 C TYR A 245 5238 4612 5431 652 -347 631 C ATOM 562 O TYR A 245 25.811 15.166 13.683 1.00 35.30 O ANISOU 562 O TYR A 245 4726 4001 4684 624 -313 459 O ATOM 563 CB TYR A 245 22.684 15.982 14.442 1.00 40.14 C ANISOU 563 CB TYR A 245 5259 4706 5287 830 -159 996 C ATOM 564 CG TYR A 245 21.687 17.046 14.043 1.00 41.90 C ANISOU 564 CG TYR A 245 5546 4990 5385 906 -56 1107 C ATOM 565 CD1 TYR A 245 22.069 18.378 13.927 1.00 44.21 C ANISOU 565 CD1 TYR A 245 6052 5301 5444 948 48 993 C ATOM 566 CD2 TYR A 245 20.366 16.717 13.768 1.00 46.14 C ANISOU 566 CD2 TYR A 245 5931 5567 6034 928 -78 1342 C ATOM 567 CE1 TYR A 245 21.153 19.360 13.552 1.00 42.65 C ANISOU 567 CE1 TYR A 245 5927 5157 5122 1029 141 1089 C ATOM 568 CE2 TYR A 245 19.444 17.689 13.397 1.00 43.25 C ANISOU 568 CE2 TYR A 245 5613 5269 5549 1007 27 1459 C ATOM 569 CZ TYR A 245 19.841 19.005 13.292 1.00 43.28 C ANISOU 569 CZ TYR A 245 5841 5286 5316 1066 142 1321 C ATOM 570 OH TYR A 245 18.924 19.966 12.920 1.00 47.04 O ANISOU 570 OH TYR A 245 6377 5828 5666 1154 245 1433 O ATOM 571 N LEU A 246 24.491 13.446 14.273 1.00 40.07 N ANISOU 571 N LEU A 246 5081 4553 5591 643 -444 730 N ATOM 572 CA LEU A 246 25.603 12.628 14.736 1.00 35.44 C ANISOU 572 CA LEU A 246 4473 3927 5064 610 -505 613 C ATOM 573 C LEU A 246 26.546 12.339 13.580 1.00 34.76 C ANISOU 573 C LEU A 246 4427 3808 4971 544 -585 376 C ATOM 574 O LEU A 246 27.761 12.419 13.732 1.00 38.88 O ANISOU 574 O LEU A 246 5001 4352 5419 533 -558 236 O ATOM 575 CB LEU A 246 25.102 11.321 15.350 1.00 35.25 C ANISOU 575 CB LEU A 246 4292 3857 5244 603 -623 766 C ATOM 576 CG LEU A 246 26.183 10.468 16.013 1.00 42.48 C ANISOU 576 CG LEU A 246 5182 4735 6222 583 -674 669 C ATOM 577 CD1 LEU A 246 26.877 11.248 17.137 1.00 38.22 C ANISOU 577 CD1 LEU A 246 4728 4250 5544 631 -523 664 C ATOM 578 CD2 LEU A 246 25.579 9.167 16.537 1.00 38.25 C ANISOU 578 CD2 LEU A 246 4492 4147 5893 564 -819 829 C ATOM 579 N VAL A 247 25.985 12.012 12.418 1.00 32.15 N ANISOU 579 N VAL A 247 4075 3431 4710 509 -685 349 N ATOM 580 CA VAL A 247 26.813 11.751 11.250 1.00 32.71 C ANISOU 580 CA VAL A 247 4200 3474 4755 481 -757 131 C ATOM 581 C VAL A 247 27.732 12.935 10.960 1.00 32.95 C ANISOU 581 C VAL A 247 4332 3600 4587 481 -631 -9 C ATOM 582 O VAL A 247 28.928 12.763 10.723 1.00 34.23 O ANISOU 582 O VAL A 247 4516 3796 4694 482 -638 -154 O ATOM 583 CB VAL A 247 25.972 11.435 10.009 1.00 35.17 C ANISOU 583 CB VAL A 247 4512 3712 5140 446 -877 132 C ATOM 584 CG1 VAL A 247 26.862 11.368 8.780 1.00 35.57 C ANISOU 584 CG1 VAL A 247 4645 3751 5118 451 -920 -99 C ATOM 585 CG2 VAL A 247 25.219 10.117 10.202 1.00 32.73 C ANISOU 585 CG2 VAL A 247 4118 3289 5027 418 -1061 274 C ATOM 586 N GLN A 248 27.169 14.138 11.003 1.00 30.54 N ANISOU 586 N GLN A 248 4089 3347 4167 484 -523 56 N ATOM 587 CA GLN A 248 27.932 15.350 10.759 1.00 29.87 C ANISOU 587 CA GLN A 248 4118 3344 3886 466 -431 -49 C ATOM 588 C GLN A 248 29.027 15.602 11.790 1.00 37.74 C ANISOU 588 C GLN A 248 5164 4384 4791 463 -380 -60 C ATOM 589 O GLN A 248 30.130 16.013 11.438 1.00 41.04 O ANISOU 589 O GLN A 248 5629 4868 5098 422 -375 -170 O ATOM 590 CB GLN A 248 26.996 16.552 10.668 1.00 26.00 C ANISOU 590 CB GLN A 248 3710 2881 3287 482 -342 36 C ATOM 591 CG GLN A 248 26.020 16.461 9.509 1.00 35.55 C ANISOU 591 CG GLN A 248 4877 4061 4570 462 -390 41 C ATOM 592 CD GLN A 248 25.068 17.646 9.457 1.00 41.57 C ANISOU 592 CD GLN A 248 5713 4861 5221 490 -290 141 C ATOM 593 OE1 GLN A 248 25.484 18.789 9.269 1.00 41.06 O ANISOU 593 OE1 GLN A 248 5775 4848 4977 480 -222 62 O ATOM 594 NE2 GLN A 248 23.786 17.375 9.626 1.00 31.35 N ANISOU 594 NE2 GLN A 248 4340 3546 4025 527 -290 333 N ATOM 595 N SER A 249 28.726 15.360 13.062 1.00 37.06 N ANISOU 595 N SER A 249 5065 4269 4749 503 -349 75 N ATOM 596 CA SER A 249 29.727 15.512 14.111 1.00 32.04 C ANISOU 596 CA SER A 249 4483 3652 4040 492 -315 80 C ATOM 597 C SER A 249 30.857 14.510 13.952 1.00 30.99 C ANISOU 597 C SER A 249 4258 3528 3988 458 -386 -25 C ATOM 598 O SER A 249 32.022 14.840 14.175 1.00 32.04 O ANISOU 598 O SER A 249 4436 3718 4020 414 -371 -72 O ATOM 599 CB SER A 249 29.097 15.342 15.490 1.00 39.60 C ANISOU 599 CB SER A 249 5437 4571 5040 560 -269 250 C ATOM 600 OG SER A 249 28.115 16.333 15.710 1.00 43.26 O ANISOU 600 OG SER A 249 6004 5042 5391 631 -185 363 O ATOM 601 N VAL A 250 30.524 13.279 13.574 1.00 31.05 N ANISOU 601 N VAL A 250 4148 3482 4170 480 -475 -44 N ATOM 602 CA VAL A 250 31.558 12.247 13.477 1.00 29.16 C ANISOU 602 CA VAL A 250 3840 3244 3996 482 -543 -139 C ATOM 603 C VAL A 250 32.428 12.475 12.251 1.00 34.71 C ANISOU 603 C VAL A 250 4567 4024 4598 479 -554 -287 C ATOM 604 O VAL A 250 33.627 12.197 12.270 1.00 41.25 O ANISOU 604 O VAL A 250 5369 4921 5382 485 -554 -344 O ATOM 605 CB VAL A 250 30.983 10.805 13.502 1.00 33.71 C ANISOU 605 CB VAL A 250 4318 3717 4773 514 -666 -112 C ATOM 606 CG1 VAL A 250 32.064 9.784 13.152 1.00 31.70 C ANISOU 606 CG1 VAL A 250 4031 3461 4552 546 -741 -236 C ATOM 607 CG2 VAL A 250 30.394 10.499 14.867 1.00 29.04 C ANISOU 607 CG2 VAL A 250 3670 3085 4278 517 -653 52 C ATOM 608 N ILE A 251 31.822 12.991 11.187 1.00 33.73 N ANISOU 608 N ILE A 251 4482 3902 4433 477 -560 -332 N ATOM 609 CA ILE A 251 32.578 13.411 10.016 1.00 34.65 C ANISOU 609 CA ILE A 251 4623 4110 4431 479 -556 -457 C ATOM 610 C ILE A 251 33.581 14.490 10.426 1.00 33.57 C ANISOU 610 C ILE A 251 4532 4099 4123 417 -479 -435 C ATOM 611 O ILE A 251 34.761 14.425 10.077 1.00 32.30 O ANISOU 611 O ILE A 251 4336 4049 3886 421 -481 -483 O ATOM 612 CB ILE A 251 31.645 13.933 8.901 1.00 38.18 C ANISOU 612 CB ILE A 251 5113 4532 4861 471 -568 -494 C ATOM 613 CG1 ILE A 251 30.926 12.755 8.236 1.00 41.68 C ANISOU 613 CG1 ILE A 251 5528 4851 5458 519 -688 -525 C ATOM 614 CG2 ILE A 251 32.426 14.733 7.869 1.00 37.87 C ANISOU 614 CG2 ILE A 251 5105 4618 4665 456 -537 -597 C ATOM 615 CD1 ILE A 251 29.873 13.155 7.217 1.00 40.33 C ANISOU 615 CD1 ILE A 251 5395 4631 5298 495 -717 -534 C ATOM 616 N GLY A 252 33.117 15.460 11.202 1.00 33.61 N ANISOU 616 N GLY A 252 4625 4087 4058 367 -423 -340 N ATOM 617 CA GLY A 252 33.988 16.518 11.681 1.00 38.45 C ANISOU 617 CA GLY A 252 5327 4784 4499 290 -388 -297 C ATOM 618 C GLY A 252 35.150 15.974 12.498 1.00 41.03 C ANISOU 618 C GLY A 252 5601 5151 4837 269 -399 -259 C ATOM 619 O GLY A 252 36.283 16.438 12.371 1.00 38.30 O ANISOU 619 O GLY A 252 5259 4921 4370 204 -409 -245 O ATOM 620 N ILE A 253 34.871 14.979 13.336 1.00 30.19 N ANISOU 620 N ILE A 253 4167 3692 3610 316 -406 -222 N ATOM 621 CA ILE A 253 35.897 14.399 14.199 1.00 26.40 C ANISOU 621 CA ILE A 253 3634 3239 3159 295 -413 -181 C ATOM 622 C ILE A 253 36.884 13.580 13.365 1.00 27.86 C ANISOU 622 C ILE A 253 3700 3523 3364 340 -445 -264 C ATOM 623 O ILE A 253 38.093 13.601 13.607 1.00 35.01 O ANISOU 623 O ILE A 253 4566 4536 4201 303 -440 -223 O ATOM 624 CB ILE A 253 35.264 13.541 15.314 1.00 37.28 C ANISOU 624 CB ILE A 253 4972 4498 4693 336 -415 -118 C ATOM 625 CG1 ILE A 253 34.431 14.430 16.253 1.00 32.37 C ANISOU 625 CG1 ILE A 253 4481 3807 4011 326 -364 -8 C ATOM 626 CG2 ILE A 253 36.338 12.782 16.097 1.00 29.67 C ANISOU 626 CG2 ILE A 253 3934 3559 3779 318 -428 -93 C ATOM 627 CD1 ILE A 253 33.539 13.635 17.236 1.00 26.30 C ANISOU 627 CD1 ILE A 253 3653 2940 3398 388 -360 80 C ATOM 628 N SER A 254 36.361 12.887 12.360 1.00 34.31 N ANISOU 628 N SER A 254 4471 4305 4259 429 -484 -365 N ATOM 629 CA SER A 254 37.192 12.112 11.448 1.00 35.39 C ANISOU 629 CA SER A 254 4533 4525 4387 521 -514 -453 C ATOM 630 C SER A 254 38.198 12.994 10.739 1.00 31.66 C ANISOU 630 C SER A 254 4052 4242 3736 490 -478 -446 C ATOM 631 O SER A 254 39.376 12.656 10.659 1.00 39.84 O ANISOU 631 O SER A 254 5009 5413 4716 529 -467 -422 O ATOM 632 CB SER A 254 36.337 11.393 10.408 1.00 34.58 C ANISOU 632 CB SER A 254 4444 4326 4371 618 -583 -561 C ATOM 633 OG SER A 254 37.159 10.595 9.568 1.00 34.51 O ANISOU 633 OG SER A 254 4401 4383 4328 745 -614 -648 O ATOM 634 N LEU A 255 37.726 14.133 10.237 1.00 39.56 N ANISOU 634 N LEU A 255 5126 5263 4643 422 -463 -449 N ATOM 635 CA LEU A 255 38.574 15.098 9.537 1.00 34.40 C ANISOU 635 CA LEU A 255 4465 4790 3816 368 -449 -424 C ATOM 636 C LEU A 255 39.605 15.760 10.442 1.00 41.95 C ANISOU 636 C LEU A 255 5425 5847 4666 243 -446 -276 C ATOM 637 O LEU A 255 40.677 16.151 9.978 1.00 48.43 O ANISOU 637 O LEU A 255 6181 6858 5363 210 -453 -211 O ATOM 638 CB LEU A 255 37.721 16.173 8.864 1.00 32.49 C ANISOU 638 CB LEU A 255 4317 4523 3506 312 -448 -462 C ATOM 639 CG LEU A 255 36.891 15.674 7.675 1.00 38.04 C ANISOU 639 CG LEU A 255 5011 5162 4280 415 -464 -595 C ATOM 640 CD1 LEU A 255 35.857 16.724 7.248 1.00 43.26 C ANISOU 640 CD1 LEU A 255 5769 5769 4900 346 -455 -614 C ATOM 641 CD2 LEU A 255 37.789 15.273 6.505 1.00 36.85 C ANISOU 641 CD2 LEU A 255 4778 5163 4061 521 -472 -661 C ATOM 642 N ALA A 256 39.285 15.892 11.726 1.00 38.35 N ANISOU 642 N ALA A 256 5049 5270 4253 172 -444 -203 N ATOM 643 CA ALA A 256 40.225 16.499 12.670 1.00 39.02 C ANISOU 643 CA ALA A 256 5174 5413 4237 39 -465 -53 C ATOM 644 C ALA A 256 41.245 15.497 13.221 1.00 41.92 C ANISOU 644 C ALA A 256 5410 5848 4671 68 -459 6 C ATOM 645 O ALA A 256 42.180 15.886 13.916 1.00 44.37 O ANISOU 645 O ALA A 256 5727 6229 4904 -48 -485 150 O ATOM 646 CB ALA A 256 39.483 17.211 13.820 1.00 35.62 C ANISOU 646 CB ALA A 256 4929 4818 3786 -37 -470 8 C ATOM 647 N THR A 257 41.078 14.216 12.903 1.00 43.30 N ANISOU 647 N THR A 257 5478 5995 4979 219 -438 -95 N ATOM 648 CA THR A 257 41.959 13.191 13.460 1.00 37.07 C ANISOU 648 CA THR A 257 4575 5253 4256 266 -429 -51 C ATOM 649 C THR A 257 42.917 12.653 12.419 1.00 43.16 C ANISOU 649 C THR A 257 5213 6220 4965 393 -413 -67 C ATOM 650 O THR A 257 42.619 11.674 11.726 1.00 38.85 O ANISOU 650 O THR A 257 4636 5638 4489 565 -414 -195 O ATOM 651 CB THR A 257 41.170 12.023 14.040 1.00 37.24 C ANISOU 651 CB THR A 257 4588 5094 4466 354 -435 -132 C ATOM 652 OG1 THR A 257 40.183 12.531 14.938 1.00 38.80 O ANISOU 652 OG1 THR A 257 4898 5133 4710 272 -437 -101 O ATOM 653 CG2 THR A 257 42.113 11.059 14.793 1.00 30.08 C ANISOU 653 CG2 THR A 257 3579 4229 3623 382 -429 -75 C ATOM 654 N ASN A 258 44.078 13.291 12.326 1.00 44.90 N ANISOU 654 N ASN A 258 5367 6649 5044 313 -410 84 N ATOM 655 CA ASN A 258 45.033 12.975 11.273 1.00 47.94 C ANISOU 655 CA ASN A 258 5614 7270 5331 447 -382 111 C ATOM 656 C ASN A 258 45.907 11.781 11.645 1.00 44.61 C ANISOU 656 C ASN A 258 5069 6924 4955 575 -347 156 C ATOM 657 O ASN A 258 47.130 11.857 11.583 1.00 48.42 O ANISOU 657 O ASN A 258 5421 7642 5333 576 -323 326 O ATOM 658 CB ASN A 258 45.888 14.207 10.941 1.00 56.36 C ANISOU 658 CB ASN A 258 6636 8559 6217 303 -405 293 C ATOM 659 CG ASN A 258 46.408 14.195 9.505 1.00 77.29 C ANISOU 659 CG ASN A 258 9173 11443 8750 456 -375 288 C ATOM 660 OD1 ASN A 258 45.847 13.529 8.630 1.00 79.60 O ANISOU 660 OD1 ASN A 258 9483 11681 9081 653 -346 108 O ATOM 661 ND2 ASN A 258 47.486 14.936 9.259 1.00 81.59 N ANISOU 661 ND2 ASN A 258 9607 12252 9143 364 -393 504 N ATOM 662 N ASP A 259 45.270 10.684 12.055 1.00 40.44 N ANISOU 662 N ASP A 259 4580 6203 4582 677 -353 23 N ATOM 663 CA ASP A 259 45.980 9.435 12.334 1.00 36.48 C ANISOU 663 CA ASP A 259 3987 5745 4128 826 -329 32 C ATOM 664 C ASP A 259 46.173 8.612 11.058 1.00 42.32 C ANISOU 664 C ASP A 259 4707 6568 4804 1105 -313 -81 C ATOM 665 O ASP A 259 45.909 9.096 9.958 1.00 42.84 O ANISOU 665 O ASP A 259 4805 6692 4780 1164 -313 -140 O ATOM 666 CB ASP A 259 45.264 8.621 13.415 1.00 41.42 C ANISOU 666 CB ASP A 259 4670 6127 4943 799 -365 -43 C ATOM 667 CG ASP A 259 43.914 8.062 12.952 1.00 54.21 C ANISOU 667 CG ASP A 259 6399 7522 6675 891 -425 -236 C ATOM 668 OD1 ASP A 259 43.400 8.462 11.888 1.00 49.55 O ANISOU 668 OD1 ASP A 259 5866 6935 6026 942 -437 -319 O ATOM 669 OD2 ASP A 259 43.359 7.209 13.673 1.00 68.01 O ANISOU 669 OD2 ASP A 259 8173 9093 8576 900 -471 -288 O ATOM 670 N ASP A 260 46.632 7.371 11.199 1.00 46.80 N ANISOU 670 N ASP A 260 5239 7135 5407 1286 -305 -111 N ATOM 671 CA ASP A 260 46.974 6.564 10.029 1.00 50.38 C ANISOU 671 CA ASP A 260 5705 7677 5760 1589 -291 -200 C ATOM 672 C ASP A 260 45.760 6.099 9.213 1.00 51.09 C ANISOU 672 C ASP A 260 5970 7534 5909 1704 -378 -424 C ATOM 673 O ASP A 260 45.872 5.878 8.012 1.00 52.76 O ANISOU 673 O ASP A 260 6232 7813 6000 1919 -375 -500 O ATOM 674 CB ASP A 260 47.838 5.362 10.420 1.00 60.04 C ANISOU 674 CB ASP A 260 6870 8962 6982 1774 -265 -164 C ATOM 675 CG ASP A 260 48.695 4.863 9.266 1.00 73.38 C ANISOU 675 CG ASP A 260 8531 10871 8479 2100 -206 -154 C ATOM 676 OD1 ASP A 260 49.742 5.490 8.986 1.00 79.27 O ANISOU 676 OD1 ASP A 260 9118 11930 9073 2113 -115 45 O ATOM 677 OD2 ASP A 260 48.325 3.843 8.645 1.00 75.84 O ANISOU 677 OD2 ASP A 260 8989 11044 8782 2351 -261 -327 O ATOM 678 N GLY A 261 44.606 5.955 9.858 1.00 53.25 N ANISOU 678 N GLY A 261 6335 7541 6358 1563 -459 -509 N ATOM 679 CA GLY A 261 43.406 5.518 9.163 1.00 55.09 C ANISOU 679 CA GLY A 261 6724 7546 6660 1633 -565 -680 C ATOM 680 C GLY A 261 42.620 6.651 8.516 1.00 52.16 C ANISOU 680 C GLY A 261 6396 7159 6262 1512 -562 -707 C ATOM 681 O GLY A 261 41.511 6.443 8.019 1.00 52.40 O ANISOU 681 O GLY A 261 6546 6996 6365 1521 -652 -820 O ATOM 682 N TYR A 262 43.201 7.848 8.518 1.00 51.13 N ANISOU 682 N TYR A 262 6170 7232 6023 1391 -474 -588 N ATOM 683 CA TYR A 262 42.525 9.053 8.026 1.00 41.42 C ANISOU 683 CA TYR A 262 4979 6001 4757 1253 -469 -597 C ATOM 684 C TYR A 262 42.089 8.898 6.577 1.00 42.74 C ANISOU 684 C TYR A 262 5232 6145 4862 1412 -503 -734 C ATOM 685 O TYR A 262 40.927 9.113 6.247 1.00 49.57 O ANISOU 685 O TYR A 262 6196 6837 5802 1349 -561 -821 O ATOM 686 CB TYR A 262 43.438 10.275 8.197 1.00 38.09 C ANISOU 686 CB TYR A 262 4452 5821 4201 1112 -396 -430 C ATOM 687 CG TYR A 262 42.930 11.581 7.602 1.00 43.24 C ANISOU 687 CG TYR A 262 5146 6504 4780 981 -396 -431 C ATOM 688 CD1 TYR A 262 42.379 12.574 8.409 1.00 44.76 C ANISOU 688 CD1 TYR A 262 5395 6610 5003 755 -408 -370 C ATOM 689 CD2 TYR A 262 43.037 11.834 6.237 1.00 48.37 C ANISOU 689 CD2 TYR A 262 5791 7274 5315 1096 -386 -490 C ATOM 690 CE1 TYR A 262 41.932 13.782 7.869 1.00 42.27 C ANISOU 690 CE1 TYR A 262 5135 6319 4606 644 -414 -372 C ATOM 691 CE2 TYR A 262 42.591 13.027 5.690 1.00 51.38 C ANISOU 691 CE2 TYR A 262 6206 7686 5631 970 -390 -492 C ATOM 692 CZ TYR A 262 42.040 13.995 6.507 1.00 48.46 C ANISOU 692 CZ TYR A 262 5896 7224 5294 742 -407 -435 C ATOM 693 OH TYR A 262 41.605 15.175 5.950 1.00 47.35 O ANISOU 693 OH TYR A 262 5806 7110 5076 628 -418 -441 O ATOM 694 N THR A 263 43.025 8.518 5.716 1.00 48.67 N ANISOU 694 N THR A 263 5948 7075 5470 1629 -466 -738 N ATOM 695 CA THR A 263 42.752 8.405 4.285 1.00 52.33 C ANISOU 695 CA THR A 263 6504 7536 5841 1807 -492 -860 C ATOM 696 C THR A 263 41.639 7.409 3.969 1.00 50.36 C ANISOU 696 C THR A 263 6444 6981 5710 1895 -625 -1027 C ATOM 697 O THR A 263 40.707 7.725 3.234 1.00 56.83 O ANISOU 697 O THR A 263 7363 7677 6554 1857 -682 -1115 O ATOM 698 CB THR A 263 44.017 8.011 3.506 1.00 61.55 C ANISOU 698 CB THR A 263 7609 8960 6817 2081 -423 -817 C ATOM 699 OG1 THR A 263 45.080 8.913 3.833 1.00 63.33 O ANISOU 699 OG1 THR A 263 7638 9487 6938 1976 -322 -614 O ATOM 700 CG2 THR A 263 43.756 8.059 2.001 1.00 63.50 C ANISOU 700 CG2 THR A 263 7958 9220 6946 2265 -441 -934 C ATOM 701 N LYS A 264 41.745 6.206 4.524 1.00 49.90 N ANISOU 701 N LYS A 264 6437 6798 5723 2001 -688 -1055 N ATOM 702 CA LYS A 264 40.741 5.172 4.304 1.00 56.69 C ANISOU 702 CA LYS A 264 7488 7357 6695 2068 -855 -1183 C ATOM 703 C LYS A 264 39.352 5.620 4.747 1.00 54.84 C ANISOU 703 C LYS A 264 7278 6921 6639 1815 -928 -1178 C ATOM 704 O LYS A 264 38.359 5.285 4.103 1.00 58.46 O ANISOU 704 O LYS A 264 7882 7177 7155 1826 -1059 -1261 O ATOM 705 CB LYS A 264 41.134 3.867 5.001 1.00 65.25 C ANISOU 705 CB LYS A 264 8611 8350 7831 2191 -922 -1192 C ATOM 706 CG LYS A 264 42.285 3.131 4.326 1.00 75.61 C ANISOU 706 CG LYS A 264 9972 9804 8953 2521 -886 -1224 C ATOM 707 CD LYS A 264 42.674 1.877 5.090 1.00 85.88 C ANISOU 707 CD LYS A 264 11314 11012 10303 2634 -951 -1229 C ATOM 708 CE LYS A 264 43.551 0.969 4.240 1.00 95.63 C ANISOU 708 CE LYS A 264 12681 12319 11333 3020 -954 -1292 C ATOM 709 NZ LYS A 264 44.706 1.701 3.644 1.00 98.59 N ANISOU 709 NZ LYS A 264 12905 13059 11498 3164 -759 -1193 N ATOM 710 N ARG A 265 39.275 6.377 5.838 1.00 46.40 N ANISOU 710 N ARG A 265 6076 5908 5647 1598 -849 -1065 N ATOM 711 CA ARG A 265 37.982 6.889 6.291 1.00 46.51 C ANISOU 711 CA ARG A 265 6104 5766 5802 1390 -892 -1033 C ATOM 712 C ARG A 265 37.392 7.896 5.312 1.00 43.88 C ANISOU 712 C ARG A 265 5808 5456 5406 1333 -870 -1068 C ATOM 713 O ARG A 265 36.204 7.831 4.970 1.00 41.62 O ANISOU 713 O ARG A 265 5607 4994 5214 1275 -964 -1097 O ATOM 714 CB ARG A 265 38.076 7.512 7.684 1.00 40.10 C ANISOU 714 CB ARG A 265 5175 5008 5052 1206 -807 -902 C ATOM 715 CG ARG A 265 38.345 6.501 8.782 1.00 39.70 C ANISOU 715 CG ARG A 265 5089 4886 5111 1221 -847 -863 C ATOM 716 CD ARG A 265 38.113 7.096 10.153 1.00 36.98 C ANISOU 716 CD ARG A 265 4665 4539 4846 1036 -786 -739 C ATOM 717 NE ARG A 265 38.730 8.412 10.289 1.00 38.22 N ANISOU 717 NE ARG A 265 4771 4876 4873 936 -662 -664 N ATOM 718 CZ ARG A 265 39.965 8.621 10.738 1.00 42.79 C ANISOU 718 CZ ARG A 265 5269 5624 5364 925 -587 -588 C ATOM 719 NH1 ARG A 265 40.731 7.597 11.106 1.00 32.33 N ANISOU 719 NH1 ARG A 265 3894 4323 4068 1024 -599 -585 N ATOM 720 NH2 ARG A 265 40.436 9.859 10.820 1.00 38.76 N ANISOU 720 NH2 ARG A 265 4735 5258 4732 808 -515 -500 N ATOM 721 N GLN A 266 38.211 8.832 4.857 1.00 50.33 N ANISOU 721 N GLN A 266 6556 6499 6068 1338 -754 -1047 N ATOM 722 CA GLN A 266 37.691 9.889 3.999 1.00 53.04 C ANISOU 722 CA GLN A 266 6923 6878 6350 1264 -728 -1075 C ATOM 723 C GLN A 266 37.350 9.323 2.628 1.00 56.38 C ANISOU 723 C GLN A 266 7472 7212 6737 1427 -814 -1206 C ATOM 724 O GLN A 266 36.376 9.739 1.998 1.00 53.48 O ANISOU 724 O GLN A 266 7174 6741 6405 1356 -858 -1249 O ATOM 725 CB GLN A 266 38.680 11.050 3.886 1.00 57.77 C ANISOU 725 CB GLN A 266 7414 7746 6790 1209 -609 -998 C ATOM 726 CG GLN A 266 38.043 12.341 3.400 1.00 62.50 C ANISOU 726 CG GLN A 266 8031 8369 7348 1065 -583 -998 C ATOM 727 CD GLN A 266 39.028 13.498 3.333 1.00 64.16 C ANISOU 727 CD GLN A 266 8145 8837 7398 985 -502 -900 C ATOM 728 OE1 GLN A 266 40.236 13.295 3.184 1.00 72.39 O ANISOU 728 OE1 GLN A 266 9093 10078 8333 1083 -465 -841 O ATOM 729 NE2 GLN A 266 38.514 14.720 3.428 1.00 39.58 N ANISOU 729 NE2 GLN A 266 5056 5725 4257 809 -487 -864 N ATOM 730 N GLU A 267 38.155 8.364 2.176 1.00 51.46 N ANISOU 730 N GLU A 267 6894 6626 6033 1656 -841 -1264 N ATOM 731 CA GLU A 267 37.936 7.731 0.883 1.00 57.31 C ANISOU 731 CA GLU A 267 7799 7266 6708 1851 -935 -1392 C ATOM 732 C GLU A 267 36.619 6.971 0.923 1.00 56.67 C ANISOU 732 C GLU A 267 7875 6863 6794 1790 -1119 -1439 C ATOM 733 O GLU A 267 35.798 7.062 0.007 1.00 58.10 O ANISOU 733 O GLU A 267 8177 6912 6986 1779 -1206 -1504 O ATOM 734 CB GLU A 267 39.084 6.776 0.555 1.00 61.08 C ANISOU 734 CB GLU A 267 8319 7841 7049 2144 -927 -1428 C ATOM 735 CG GLU A 267 38.832 5.892 -0.655 1.00 73.00 C ANISOU 735 CG GLU A 267 10067 9190 8482 2386 -1058 -1568 C ATOM 736 CD GLU A 267 38.908 6.656 -1.967 1.00 78.17 C ANISOU 736 CD GLU A 267 10743 9967 8991 2462 -1002 -1622 C ATOM 737 OE1 GLU A 267 39.334 7.835 -1.950 1.00 79.69 O ANISOU 737 OE1 GLU A 267 10746 10407 9126 2346 -856 -1541 O ATOM 738 OE2 GLU A 267 38.545 6.070 -3.014 1.00 73.04 O ANISOU 738 OE2 GLU A 267 10314 9160 8280 2636 -1118 -1740 O ATOM 739 N LYS A 268 36.427 6.232 2.007 1.00 44.84 N ANISOU 739 N LYS A 268 6363 5245 5428 1736 -1185 -1386 N ATOM 740 CA LYS A 268 35.223 5.456 2.214 1.00 46.27 C ANISOU 740 CA LYS A 268 6661 5140 5779 1656 -1378 -1380 C ATOM 741 C LYS A 268 33.998 6.360 2.242 1.00 54.02 C ANISOU 741 C LYS A 268 7599 6061 6866 1430 -1376 -1310 C ATOM 742 O LYS A 268 32.999 6.085 1.583 1.00 56.82 O ANISOU 742 O LYS A 268 8078 6227 7285 1395 -1525 -1327 O ATOM 743 CB LYS A 268 35.327 4.676 3.520 1.00 47.20 C ANISOU 743 CB LYS A 268 6721 5195 6019 1615 -1422 -1305 C ATOM 744 CG LYS A 268 34.044 4.008 3.938 1.00 57.54 C ANISOU 744 CG LYS A 268 8096 6246 7520 1485 -1619 -1242 C ATOM 745 CD LYS A 268 34.172 3.392 5.320 1.00 64.72 C ANISOU 745 CD LYS A 268 8910 7129 8552 1425 -1638 -1152 C ATOM 746 CE LYS A 268 34.999 2.117 5.306 1.00 57.53 C ANISOU 746 CE LYS A 268 8109 6158 7591 1625 -1738 -1233 C ATOM 747 NZ LYS A 268 34.931 1.437 6.635 1.00 53.70 N ANISOU 747 NZ LYS A 268 7539 5612 7255 1541 -1792 -1143 N ATOM 748 N LEU A 269 34.077 7.442 3.008 1.00 54.13 N ANISOU 748 N LEU A 269 7449 6231 6887 1282 -1215 -1220 N ATOM 749 CA LEU A 269 32.959 8.364 3.115 1.00 51.02 C ANISOU 749 CA LEU A 269 7017 5801 6568 1096 -1191 -1143 C ATOM 750 C LEU A 269 32.607 8.919 1.731 1.00 53.15 C ANISOU 750 C LEU A 269 7369 6069 6758 1114 -1202 -1227 C ATOM 751 O LEU A 269 31.430 9.019 1.371 1.00 48.31 O ANISOU 751 O LEU A 269 6807 5313 6234 1018 -1287 -1193 O ATOM 752 CB LEU A 269 33.287 9.488 4.094 1.00 50.62 C ANISOU 752 CB LEU A 269 6827 5922 6484 976 -1018 -1049 C ATOM 753 CG LEU A 269 32.205 10.530 4.376 1.00 55.12 C ANISOU 753 CG LEU A 269 7369 6474 7100 814 -967 -955 C ATOM 754 CD1 LEU A 269 31.011 9.905 5.068 1.00 49.87 C ANISOU 754 CD1 LEU A 269 6699 5634 6615 743 -1070 -838 C ATOM 755 CD2 LEU A 269 32.786 11.646 5.223 1.00 63.07 C ANISOU 755 CD2 LEU A 269 8299 7649 8017 734 -812 -887 C ATOM 756 N LYS A 270 33.629 9.258 0.950 1.00 45.99 N ANISOU 756 N LYS A 270 6463 5328 5682 1239 -1117 -1319 N ATOM 757 CA LYS A 270 33.409 9.746 -0.411 1.00 48.15 C ANISOU 757 CA LYS A 270 6813 5615 5869 1277 -1125 -1409 C ATOM 758 C LYS A 270 32.714 8.697 -1.279 1.00 50.94 C ANISOU 758 C LYS A 270 7363 5718 6272 1366 -1325 -1484 C ATOM 759 O LYS A 270 31.818 9.025 -2.050 1.00 54.87 O ANISOU 759 O LYS A 270 7934 6113 6802 1292 -1387 -1501 O ATOM 760 CB LYS A 270 34.725 10.194 -1.055 1.00 44.40 C ANISOU 760 CB LYS A 270 6286 5390 5194 1419 -1004 -1468 C ATOM 761 CG LYS A 270 34.597 10.672 -2.503 1.00 46.15 C ANISOU 761 CG LYS A 270 6580 5645 5312 1480 -1006 -1564 C ATOM 762 CD LYS A 270 34.771 9.523 -3.524 1.00 48.66 C ANISOU 762 CD LYS A 270 7090 5836 5563 1728 -1131 -1684 C ATOM 763 CE LYS A 270 36.182 8.941 -3.494 1.00 48.47 C ANISOU 763 CE LYS A 270 7039 5987 5388 1976 -1067 -1697 C ATOM 764 NZ LYS A 270 36.494 8.054 -4.670 1.00 59.08 N ANISOU 764 NZ LYS A 270 8591 7258 6599 2271 -1156 -1819 N ATOM 765 N ASN A 271 33.127 7.439 -1.144 1.00 50.46 N ANISOU 765 N ASN A 271 7407 5552 6213 1522 -1439 -1522 N ATOM 766 CA ASN A 271 32.518 6.338 -1.893 1.00 50.36 C ANISOU 766 CA ASN A 271 7633 5269 6233 1613 -1673 -1585 C ATOM 767 C ASN A 271 31.068 6.074 -1.497 1.00 51.39 C ANISOU 767 C ASN A 271 7791 5166 6567 1401 -1841 -1468 C ATOM 768 O ASN A 271 30.237 5.773 -2.354 1.00 46.06 O ANISOU 768 O ASN A 271 7283 4293 5926 1375 -2014 -1484 O ATOM 769 CB ASN A 271 33.338 5.050 -1.743 1.00 51.48 C ANISOU 769 CB ASN A 271 7899 5348 6312 1839 -1767 -1646 C ATOM 770 CG ASN A 271 34.618 5.078 -2.557 1.00 60.98 C ANISOU 770 CG ASN A 271 9143 6742 7285 2115 -1653 -1758 C ATOM 771 OD1 ASN A 271 34.807 5.957 -3.401 1.00 60.65 O ANISOU 771 OD1 ASN A 271 9064 6847 7134 2139 -1542 -1799 O ATOM 772 ND2 ASN A 271 35.504 4.114 -2.310 1.00 63.54 N ANISOU 772 ND2 ASN A 271 9538 7079 7527 2335 -1677 -1792 N ATOM 773 N PHE A 272 30.771 6.178 -0.202 1.00 47.07 N ANISOU 773 N PHE A 272 7083 4649 6151 1254 -1796 -1332 N ATOM 774 CA PHE A 272 29.412 5.959 0.297 1.00 45.84 C ANISOU 774 CA PHE A 272 6910 4322 6187 1061 -1937 -1171 C ATOM 775 C PHE A 272 28.439 6.970 -0.290 1.00 52.35 C ANISOU 775 C PHE A 272 7700 5154 7038 916 -1895 -1116 C ATOM 776 O PHE A 272 27.408 6.608 -0.861 1.00 56.26 O ANISOU 776 O PHE A 272 8301 5456 7618 835 -2082 -1053 O ATOM 777 CB PHE A 272 29.354 6.063 1.825 1.00 40.50 C ANISOU 777 CB PHE A 272 6043 3727 5617 956 -1848 -1028 C ATOM 778 CG PHE A 272 29.912 4.869 2.547 1.00 48.12 C ANISOU 778 CG PHE A 272 7039 4620 6623 1043 -1951 -1033 C ATOM 779 CD1 PHE A 272 30.251 3.715 1.860 1.00 50.83 C ANISOU 779 CD1 PHE A 272 7594 4801 6918 1198 -2145 -1142 C ATOM 780 CD2 PHE A 272 30.069 4.895 3.929 1.00 46.55 C ANISOU 780 CD2 PHE A 272 6676 4507 6505 975 -1862 -925 C ATOM 781 CE1 PHE A 272 30.758 2.615 2.536 1.00 56.32 C ANISOU 781 CE1 PHE A 272 8329 5426 7644 1283 -2246 -1148 C ATOM 782 CE2 PHE A 272 30.573 3.805 4.609 1.00 47.71 C ANISOU 782 CE2 PHE A 272 6841 4589 6696 1045 -1956 -929 C ATOM 783 CZ PHE A 272 30.914 2.659 3.913 1.00 54.02 C ANISOU 783 CZ PHE A 272 7845 5230 7448 1196 -2150 -1041 C ATOM 784 N ILE A 273 28.765 8.248 -0.127 1.00 54.72 N ANISOU 784 N ILE A 273 7858 5674 7260 875 -1661 -1124 N ATOM 785 CA ILE A 273 27.896 9.319 -0.593 1.00 55.42 C ANISOU 785 CA ILE A 273 7905 5793 7360 743 -1595 -1072 C ATOM 786 C ILE A 273 27.858 9.352 -2.116 1.00 53.23 C ANISOU 786 C ILE A 273 7778 5447 6999 806 -1669 -1206 C ATOM 787 O ILE A 273 26.795 9.480 -2.718 1.00 53.82 O ANISOU 787 O ILE A 273 7908 5397 7146 700 -1766 -1147 O ATOM 788 CB ILE A 273 28.357 10.690 -0.065 1.00 50.64 C ANISOU 788 CB ILE A 273 7150 5427 6662 696 -1349 -1062 C ATOM 789 CG1 ILE A 273 28.408 10.682 1.461 1.00 41.48 C ANISOU 789 CG1 ILE A 273 5869 4322 5568 647 -1277 -930 C ATOM 790 CG2 ILE A 273 27.424 11.790 -0.556 1.00 54.48 C ANISOU 790 CG2 ILE A 273 7613 5937 7150 573 -1287 -1011 C ATOM 791 CD1 ILE A 273 28.911 11.972 2.046 1.00 44.46 C ANISOU 791 CD1 ILE A 273 6152 4903 5838 605 -1070 -914 C ATOM 792 N SER A 274 29.031 9.243 -2.728 1.00 49.19 N ANISOU 792 N SER A 274 7329 5031 6331 985 -1617 -1370 N ATOM 793 CA SER A 274 29.142 9.218 -4.178 1.00 56.17 C ANISOU 793 CA SER A 274 8368 5864 7110 1089 -1678 -1508 C ATOM 794 C SER A 274 28.113 8.255 -4.761 1.00 59.29 C ANISOU 794 C SER A 274 8968 5951 7608 1056 -1948 -1478 C ATOM 795 O SER A 274 27.414 8.585 -5.723 1.00 61.37 O ANISOU 795 O SER A 274 9317 6124 7878 991 -2012 -1494 O ATOM 796 CB SER A 274 30.554 8.785 -4.587 1.00 65.76 C ANISOU 796 CB SER A 274 9645 7195 8148 1344 -1629 -1651 C ATOM 797 OG SER A 274 31.115 9.656 -5.553 1.00 70.86 O ANISOU 797 OG SER A 274 10266 8021 8638 1416 -1500 -1748 O ATOM 798 N SER A 275 28.002 7.076 -4.153 1.00 64.23 N ANISOU 798 N SER A 275 9675 6412 8319 1082 -2122 -1421 N ATOM 799 CA SER A 275 27.199 5.987 -4.711 1.00 61.08 C ANISOU 799 CA SER A 275 9516 5698 7995 1066 -2433 -1388 C ATOM 800 C SER A 275 25.692 6.165 -4.521 1.00 62.52 C ANISOU 800 C SER A 275 9641 5749 8365 804 -2555 -1176 C ATOM 801 O SER A 275 24.895 5.478 -5.165 1.00 66.33 O ANISOU 801 O SER A 275 10319 5975 8909 744 -2824 -1120 O ATOM 802 CB SER A 275 27.640 4.639 -4.127 1.00 61.65 C ANISOU 802 CB SER A 275 9709 5635 8081 1184 -2602 -1393 C ATOM 803 OG SER A 275 27.132 4.453 -2.817 1.00 56.80 O ANISOU 803 OG SER A 275 8921 5023 7637 1021 -2620 -1208 O ATOM 804 N GLN A 276 25.301 7.076 -3.637 1.00 51.07 N ANISOU 804 N GLN A 276 7935 4474 6994 658 -2368 -1039 N ATOM 805 CA GLN A 276 23.885 7.309 -3.373 1.00 55.93 C ANISOU 805 CA GLN A 276 8461 5015 7775 437 -2448 -800 C ATOM 806 C GLN A 276 23.561 8.791 -3.503 1.00 51.80 C ANISOU 806 C GLN A 276 7776 4686 7218 350 -2206 -777 C ATOM 807 O GLN A 276 22.622 9.299 -2.887 1.00 46.74 O ANISOU 807 O GLN A 276 6982 4096 6680 207 -2152 -568 O ATOM 808 CB GLN A 276 23.514 6.799 -1.978 1.00 57.31 C ANISOU 808 CB GLN A 276 8493 5191 8091 356 -2491 -594 C ATOM 809 CG GLN A 276 23.695 5.295 -1.801 1.00 67.53 C ANISOU 809 CG GLN A 276 9949 6273 9435 412 -2767 -590 C ATOM 810 CD GLN A 276 22.606 4.480 -2.484 1.00 76.67 C ANISOU 810 CD GLN A 276 11288 7147 10697 287 -3115 -448 C ATOM 811 OE1 GLN A 276 22.726 3.260 -2.626 1.00 85.25 O ANISOU 811 OE1 GLN A 276 12583 8013 11795 335 -3391 -467 O ATOM 812 NE2 GLN A 276 21.536 5.148 -2.905 1.00 72.28 N ANISOU 812 NE2 GLN A 276 10664 6589 10211 123 -3117 -293 N ATOM 813 N MET A 277 24.356 9.476 -4.313 1.00 54.87 N ANISOU 813 N MET A 277 7281 6087 7480 889 -1906 216 N ATOM 814 CA MET A 277 24.296 10.928 -4.418 1.00 51.53 C ANISOU 814 CA MET A 277 6809 5806 6965 873 -1685 165 C ATOM 815 C MET A 277 22.873 11.488 -4.522 1.00 53.75 C ANISOU 815 C MET A 277 7045 6068 7309 768 -1700 281 C ATOM 816 O MET A 277 22.414 12.212 -3.636 1.00 51.52 O ANISOU 816 O MET A 277 6627 5916 7032 674 -1563 389 O ATOM 817 CB MET A 277 25.128 11.395 -5.608 1.00 45.74 C ANISOU 817 CB MET A 277 6216 5051 6113 1020 -1602 -22 C ATOM 818 CG MET A 277 25.443 12.875 -5.580 1.00 50.72 C ANISOU 818 CG MET A 277 6775 5854 6642 1024 -1335 -94 C ATOM 819 SD MET A 277 26.046 13.372 -3.958 1.00 55.84 S ANISOU 819 SD MET A 277 7236 6723 7259 928 -1154 -34 S ATOM 820 CE MET A 277 27.047 14.784 -4.394 1.00 41.78 C ANISOU 820 CE MET A 277 5451 5082 5343 1012 -883 -195 C ATOM 821 N THR A 278 22.180 11.147 -5.603 1.00 52.63 N ANISOU 821 N THR A 278 7025 5762 7210 789 -1865 270 N ATOM 822 CA THR A 278 20.872 11.742 -5.890 1.00 50.77 C ANISOU 822 CA THR A 278 6756 5510 7023 699 -1870 381 C ATOM 823 C THR A 278 19.900 11.525 -4.740 1.00 49.26 C ANISOU 823 C THR A 278 6412 5343 6962 561 -1917 622 C ATOM 824 O THR A 278 19.196 12.447 -4.315 1.00 50.08 O ANISOU 824 O THR A 278 6416 5550 7061 482 -1766 740 O ATOM 825 CB THR A 278 20.268 11.171 -7.191 1.00 51.98 C ANISOU 825 CB THR A 278 7070 5462 7218 735 -2096 346 C ATOM 826 OG1 THR A 278 21.145 11.452 -8.289 1.00 52.04 O ANISOU 826 OG1 THR A 278 7227 5448 7097 890 -2034 131 O ATOM 827 CG2 THR A 278 18.905 11.783 -7.471 1.00 51.71 C ANISOU 827 CG2 THR A 278 6987 5423 7238 632 -2100 486 C ATOM 828 N ASP A 279 19.879 10.301 -4.228 1.00 47.49 N ANISOU 828 N ASP A 279 6169 5019 6855 544 -2113 705 N ATOM 829 CA ASP A 279 18.963 9.943 -3.156 1.00 49.09 C ANISOU 829 CA ASP A 279 6224 5223 7207 440 -2180 950 C ATOM 830 C ASP A 279 19.270 10.707 -1.875 1.00 45.38 C ANISOU 830 C ASP A 279 5605 4959 6679 411 -1940 1014 C ATOM 831 O ASP A 279 18.365 11.039 -1.122 1.00 46.57 O ANISOU 831 O ASP A 279 5641 5153 6900 334 -1893 1221 O ATOM 832 CB ASP A 279 19.003 8.434 -2.896 1.00 62.66 C ANISOU 832 CB ASP A 279 7947 6794 9067 448 -2429 1009 C ATOM 833 CG ASP A 279 18.425 7.629 -4.047 1.00 73.81 C ANISOU 833 CG ASP A 279 9506 7975 10561 449 -2702 992 C ATOM 834 OD1 ASP A 279 18.886 6.486 -4.251 1.00 84.75 O ANISOU 834 OD1 ASP A 279 10977 9231 11993 500 -2875 932 O ATOM 835 OD2 ASP A 279 17.521 8.140 -4.749 1.00 69.42 O ANISOU 835 OD2 ASP A 279 8987 7369 10020 400 -2740 1042 O ATOM 836 N MET A 280 20.545 10.987 -1.622 1.00 44.92 N ANISOU 836 N MET A 280 5554 5023 6491 477 -1790 848 N ATOM 837 CA MET A 280 20.892 11.740 -0.428 1.00 42.78 C ANISOU 837 CA MET A 280 5159 4944 6149 446 -1573 890 C ATOM 838 C MET A 280 20.584 13.223 -0.601 1.00 39.63 C ANISOU 838 C MET A 280 4758 4660 5640 412 -1342 872 C ATOM 839 O MET A 280 20.179 13.890 0.347 1.00 42.06 O ANISOU 839 O MET A 280 4972 5078 5931 353 -1195 999 O ATOM 840 CB MET A 280 22.344 11.508 -0.024 1.00 43.61 C ANISOU 840 CB MET A 280 5260 5145 6164 512 -1504 742 C ATOM 841 CG MET A 280 22.586 10.127 0.590 1.00 44.23 C ANISOU 841 CG MET A 280 5290 5163 6352 530 -1674 815 C ATOM 842 SD MET A 280 24.273 9.905 1.205 1.00 49.04 S ANISOU 842 SD MET A 280 5867 5914 6850 596 -1566 684 S ATOM 843 CE MET A 280 24.246 10.855 2.724 1.00 48.65 C ANISOU 843 CE MET A 280 5657 6086 6743 524 -1358 779 C ATOM 844 N CYS A 281 20.761 13.733 -1.815 1.00 40.51 N ANISOU 844 N CYS A 281 4977 4740 5676 460 -1301 719 N ATOM 845 CA CYS A 281 20.454 15.134 -2.093 1.00 42.92 C ANISOU 845 CA CYS A 281 5277 5148 5882 436 -1070 697 C ATOM 846 C CYS A 281 18.974 15.415 -1.874 1.00 40.56 C ANISOU 846 C CYS A 281 4922 4822 5667 339 -1074 935 C ATOM 847 O CYS A 281 18.614 16.417 -1.259 1.00 43.92 O ANISOU 847 O CYS A 281 5285 5369 6033 287 -861 1026 O ATOM 848 CB CYS A 281 20.873 15.530 -3.517 1.00 36.28 C ANISOU 848 CB CYS A 281 4555 4268 4963 527 -1038 498 C ATOM 849 SG CYS A 281 22.679 15.617 -3.783 1.00 48.21 S ANISOU 849 SG CYS A 281 6121 5846 6352 659 -945 242 S ATOM 850 N LEU A 282 18.122 14.522 -2.376 1.00 43.10 N ANISOU 850 N LEU A 282 5272 4978 6125 317 -1316 1048 N ATOM 851 CA LEU A 282 16.671 14.699 -2.297 1.00 46.22 C ANISOU 851 CA LEU A 282 5614 5327 6620 227 -1349 1303 C ATOM 852 C LEU A 282 16.093 14.409 -0.903 1.00 50.86 C ANISOU 852 C LEU A 282 6074 5940 7309 169 -1356 1561 C ATOM 853 O LEU A 282 14.924 14.698 -0.631 1.00 52.53 O ANISOU 853 O LEU A 282 6226 6137 7596 103 -1333 1812 O ATOM 854 CB LEU A 282 15.968 13.853 -3.370 1.00 48.72 C ANISOU 854 CB LEU A 282 6008 5449 7054 218 -1625 1337 C ATOM 855 CG LEU A 282 16.267 14.256 -4.821 1.00 50.55 C ANISOU 855 CG LEU A 282 6372 5649 7186 284 -1610 1124 C ATOM 856 CD1 LEU A 282 15.692 13.254 -5.812 1.00 47.62 C ANISOU 856 CD1 LEU A 282 6101 5069 6924 281 -1922 1138 C ATOM 857 CD2 LEU A 282 15.768 15.664 -5.141 1.00 44.16 C ANISOU 857 CD2 LEU A 282 5534 4965 6281 256 -1349 1155 C ATOM 858 N ASP A 283 16.909 13.845 -0.019 1.00 47.84 N ANISOU 858 N ASP A 283 5647 5600 6931 205 -1378 1513 N ATOM 859 CA ASP A 283 16.473 13.622 1.354 1.00 47.86 C ANISOU 859 CA ASP A 283 5527 5644 7015 178 -1360 1742 C ATOM 860 C ASP A 283 16.633 14.886 2.192 1.00 52.04 C ANISOU 860 C ASP A 283 6021 6355 7398 164 -1059 1765 C ATOM 861 O ASP A 283 17.665 15.554 2.140 1.00 57.50 O ANISOU 861 O ASP A 283 6754 7164 7930 191 -896 1546 O ATOM 862 CB ASP A 283 17.234 12.463 2.003 1.00 45.16 C ANISOU 862 CB ASP A 283 5139 5280 6741 226 -1503 1698 C ATOM 863 CG ASP A 283 16.705 12.131 3.387 1.00 51.54 C ANISOU 863 CG ASP A 283 5809 6118 7656 219 -1502 1950 C ATOM 864 OD1 ASP A 283 17.337 12.540 4.386 1.00 50.52 O ANISOU 864 OD1 ASP A 283 5630 6137 7427 243 -1338 1922 O ATOM 865 OD2 ASP A 283 15.637 11.488 3.477 1.00 56.65 O ANISOU 865 OD2 ASP A 283 6398 6640 8489 195 -1665 2188 O ATOM 866 N LYS A 284 15.604 15.201 2.970 1.00 52.85 N ANISOU 866 N LYS A 284 6052 6470 7558 127 -989 2043 N ATOM 867 CA LYS A 284 15.590 16.402 3.795 1.00 49.00 C ANISOU 867 CA LYS A 284 5553 6134 6930 114 -703 2101 C ATOM 868 C LYS A 284 16.767 16.430 4.772 1.00 48.92 C ANISOU 868 C LYS A 284 5521 6250 6815 154 -618 1956 C ATOM 869 O LYS A 284 17.307 17.490 5.085 1.00 50.25 O ANISOU 869 O LYS A 284 5726 6553 6814 146 -388 1845 O ATOM 870 CB LYS A 284 14.270 16.481 4.561 1.00 49.61 C ANISOU 870 CB LYS A 284 5561 6177 7111 93 -675 2469 C ATOM 871 CG LYS A 284 14.049 17.771 5.344 1.00 58.96 C ANISOU 871 CG LYS A 284 6764 7494 8144 84 -369 2570 C ATOM 872 CD LYS A 284 12.816 17.657 6.244 1.00 66.46 C ANISOU 872 CD LYS A 284 7645 8395 9211 94 -358 2968 C ATOM 873 CE LYS A 284 12.450 18.994 6.880 1.00 76.04 C ANISOU 873 CE LYS A 284 8909 9718 10264 89 -40 3097 C ATOM 874 NZ LYS A 284 13.635 19.707 7.444 1.00 80.46 N ANISOU 874 NZ LYS A 284 9529 10427 10616 105 144 2841 N ATOM 875 N PHE A 285 17.171 15.262 5.248 1.00 38.56 N ANISOU 875 N PHE A 285 4148 4896 5606 193 -802 1958 N ATOM 876 CA PHE A 285 18.197 15.211 6.280 1.00 41.99 C ANISOU 876 CA PHE A 285 4543 5457 5955 228 -731 1862 C ATOM 877 C PHE A 285 19.570 14.899 5.720 1.00 39.87 C ANISOU 877 C PHE A 285 4317 5220 5611 254 -777 1568 C ATOM 878 O PHE A 285 20.559 15.477 6.159 1.00 43.34 O ANISOU 878 O PHE A 285 4766 5796 5905 258 -635 1417 O ATOM 879 CB PHE A 285 17.788 14.232 7.382 1.00 46.03 C ANISOU 879 CB PHE A 285 4938 5935 6615 269 -853 2083 C ATOM 880 CG PHE A 285 16.408 14.488 7.903 1.00 52.72 C ANISOU 880 CG PHE A 285 5742 6735 7555 263 -813 2409 C ATOM 881 CD1 PHE A 285 16.119 15.676 8.563 1.00 50.09 C ANISOU 881 CD1 PHE A 285 5442 6505 7084 254 -568 2501 C ATOM 882 CD2 PHE A 285 15.387 13.575 7.690 1.00 53.45 C ANISOU 882 CD2 PHE A 285 5770 6670 7870 268 -1017 2636 C ATOM 883 CE1 PHE A 285 14.839 15.940 9.028 1.00 45.27 C ANISOU 883 CE1 PHE A 285 4804 5845 6551 263 -512 2830 C ATOM 884 CE2 PHE A 285 14.109 13.831 8.151 1.00 54.10 C ANISOU 884 CE2 PHE A 285 5807 6703 8046 270 -975 2969 C ATOM 885 CZ PHE A 285 13.835 15.014 8.823 1.00 49.05 C ANISOU 885 CZ PHE A 285 5204 6172 7262 273 -716 3074 C ATOM 886 N ALA A 286 19.623 14.010 4.734 1.00 44.73 N ANISOU 886 N ALA A 286 4968 5703 6324 274 -976 1497 N ATOM 887 CA ALA A 286 20.894 13.590 4.147 1.00 43.25 C ANISOU 887 CA ALA A 286 4834 5523 6077 320 -1029 1250 C ATOM 888 C ALA A 286 21.560 14.715 3.356 1.00 42.41 C ANISOU 888 C ALA A 286 4817 5490 5805 323 -856 1037 C ATOM 889 O ALA A 286 22.787 14.787 3.290 1.00 37.95 O ANISOU 889 O ALA A 286 4273 4999 5145 361 -805 854 O ATOM 890 CB ALA A 286 20.698 12.361 3.272 1.00 47.53 C ANISOU 890 CB ALA A 286 5418 5884 6756 350 -1282 1243 C ATOM 891 N CYS A 287 20.750 15.595 2.763 1.00 34.67 N ANISOU 891 N CYS A 287 3881 4492 4800 288 -758 1076 N ATOM 892 CA CYS A 287 21.282 16.720 2.001 1.00 34.21 C ANISOU 892 CA CYS A 287 3893 4505 4601 301 -575 889 C ATOM 893 C CYS A 287 22.116 17.617 2.909 1.00 29.34 C ANISOU 893 C CYS A 287 3244 4061 3842 283 -363 810 C ATOM 894 O CYS A 287 23.060 18.270 2.460 1.00 34.32 O ANISOU 894 O CYS A 287 3912 4761 4365 311 -244 614 O ATOM 895 CB CYS A 287 20.150 17.517 1.319 1.00 43.43 C ANISOU 895 CB CYS A 287 5093 5637 5771 262 -486 979 C ATOM 896 SG CYS A 287 19.221 18.648 2.396 1.00 39.42 S ANISOU 896 SG CYS A 287 4534 5237 5206 184 -248 1197 S ATOM 897 N ARG A 288 21.777 17.629 4.193 1.00 33.70 N ANISOU 897 N ARG A 288 3729 4677 4400 243 -323 968 N ATOM 898 CA ARG A 288 22.570 18.347 5.188 1.00 39.74 C ANISOU 898 CA ARG A 288 4471 5599 5031 222 -156 902 C ATOM 899 C ARG A 288 23.937 17.684 5.408 1.00 39.68 C ANISOU 899 C ARG A 288 4435 5641 5001 261 -240 751 C ATOM 900 O ARG A 288 24.943 18.371 5.585 1.00 35.06 O ANISOU 900 O ARG A 288 3859 5169 4293 253 -114 602 O ATOM 901 CB ARG A 288 21.800 18.453 6.503 1.00 35.31 C ANISOU 901 CB ARG A 288 3859 5078 4479 191 -104 1126 C ATOM 902 CG ARG A 288 20.443 19.125 6.364 1.00 35.14 C ANISOU 902 CG ARG A 288 3866 5011 4475 158 -1 1317 C ATOM 903 CD ARG A 288 20.562 20.646 6.187 1.00 35.08 C ANISOU 903 CD ARG A 288 3928 5099 4302 118 269 1223 C ATOM 904 NE ARG A 288 19.252 21.288 6.276 1.00 46.76 N ANISOU 904 NE ARG A 288 5430 6551 5785 88 398 1448 N ATOM 905 CZ ARG A 288 19.047 22.541 6.673 1.00 44.58 C ANISOU 905 CZ ARG A 288 5209 6360 5371 54 654 1477 C ATOM 906 NH1 ARG A 288 20.075 23.299 7.029 1.00 37.50 N ANISOU 906 NH1 ARG A 288 4347 5576 4324 37 796 1281 N ATOM 907 NH2 ARG A 288 17.808 23.032 6.721 1.00 39.89 N ANISOU 907 NH2 ARG A 288 4637 5732 4788 34 772 1716 N ATOM 908 N VAL A 289 23.967 16.350 5.398 1.00 41.57 N ANISOU 908 N VAL A 289 4638 5795 5362 301 -448 804 N ATOM 909 CA VAL A 289 25.226 15.602 5.478 1.00 36.91 C ANISOU 909 CA VAL A 289 4025 5240 4760 346 -529 684 C ATOM 910 C VAL A 289 26.098 15.882 4.254 1.00 35.30 C ANISOU 910 C VAL A 289 3905 5013 4495 396 -503 479 C ATOM 911 O VAL A 289 27.302 16.110 4.368 1.00 40.24 O ANISOU 911 O VAL A 289 4523 5732 5033 414 -436 353 O ATOM 912 CB VAL A 289 24.982 14.079 5.627 1.00 37.21 C ANISOU 912 CB VAL A 289 4014 5175 4950 385 -749 793 C ATOM 913 CG1 VAL A 289 26.299 13.304 5.546 1.00 33.76 C ANISOU 913 CG1 VAL A 289 3568 4766 4491 440 -813 674 C ATOM 914 CG2 VAL A 289 24.279 13.779 6.950 1.00 30.13 C ANISOU 914 CG2 VAL A 289 3011 4317 4120 363 -762 1001 C ATOM 915 N ILE A 290 25.477 15.887 3.081 1.00 37.22 N ANISOU 915 N ILE A 290 4226 5128 4786 423 -554 459 N ATOM 916 CA ILE A 290 26.174 16.247 1.852 1.00 37.98 C ANISOU 916 CA ILE A 290 4410 5194 4826 494 -514 278 C ATOM 917 C ILE A 290 26.791 17.645 1.957 1.00 39.77 C ANISOU 917 C ILE A 290 4629 5561 4921 474 -279 163 C ATOM 918 O ILE A 290 27.957 17.858 1.604 1.00 37.77 O ANISOU 918 O ILE A 290 4392 5353 4606 531 -226 22 O ATOM 919 CB ILE A 290 25.214 16.179 0.656 1.00 35.05 C ANISOU 919 CB ILE A 290 4121 4676 4519 521 -590 291 C ATOM 920 CG1 ILE A 290 24.813 14.730 0.413 1.00 38.97 C ANISOU 920 CG1 ILE A 290 4643 5015 5146 548 -845 373 C ATOM 921 CG2 ILE A 290 25.845 16.753 -0.598 1.00 28.21 C ANISOU 921 CG2 ILE A 290 3342 3791 3584 611 -511 110 C ATOM 922 CD1 ILE A 290 24.027 14.547 -0.850 1.00 49.24 C ANISOU 922 CD1 ILE A 290 6044 6160 6504 579 -956 365 C ATOM 923 N GLN A 291 26.015 18.593 2.471 1.00 32.19 N ANISOU 923 N GLN A 291 3646 4665 3921 395 -135 238 N ATOM 924 CA GLN A 291 26.469 19.974 2.531 1.00 32.53 C ANISOU 924 CA GLN A 291 3692 4825 3842 369 96 133 C ATOM 925 C GLN A 291 27.676 20.167 3.459 1.00 36.00 C ANISOU 925 C GLN A 291 4082 5397 4200 343 150 62 C ATOM 926 O GLN A 291 28.620 20.851 3.098 1.00 32.32 O ANISOU 926 O GLN A 291 3623 4990 3666 368 258 -81 O ATOM 927 CB GLN A 291 25.321 20.921 2.904 1.00 30.27 C ANISOU 927 CB GLN A 291 3409 4571 3523 291 250 249 C ATOM 928 CG GLN A 291 24.261 21.073 1.798 1.00 34.15 C ANISOU 928 CG GLN A 291 3945 4959 4070 313 251 295 C ATOM 929 CD GLN A 291 23.098 21.954 2.230 1.00 36.70 C ANISOU 929 CD GLN A 291 4267 5317 4361 236 415 451 C ATOM 930 OE1 GLN A 291 23.258 23.153 2.433 1.00 34.83 O ANISOU 930 OE1 GLN A 291 4040 5178 4014 204 644 398 O ATOM 931 NE2 GLN A 291 21.926 21.351 2.390 1.00 33.63 N ANISOU 931 NE2 GLN A 291 3865 4841 4070 210 302 659 N ATOM 932 N SER A 292 27.668 19.577 4.645 1.00 35.64 N ANISOU 932 N SER A 292 3978 5398 4165 299 76 169 N ATOM 933 CA SER A 292 28.828 19.771 5.514 1.00 45.61 C ANISOU 933 CA SER A 292 5193 6794 5343 269 121 103 C ATOM 934 C SER A 292 30.063 19.006 5.007 1.00 37.83 C ANISOU 934 C SER A 292 4194 5798 4381 344 19 8 C ATOM 935 O SER A 292 31.191 19.429 5.233 1.00 37.44 O ANISOU 935 O SER A 292 4119 5847 4259 335 85 -84 O ATOM 936 CB SER A 292 28.508 19.440 6.973 1.00 51.77 C ANISOU 936 CB SER A 292 5913 7644 6113 212 91 241 C ATOM 937 OG SER A 292 27.950 18.154 7.088 1.00 52.66 O ANISOU 937 OG SER A 292 5989 7670 6350 251 -87 372 O ATOM 938 N SER A 293 29.840 17.901 4.298 1.00 33.19 N ANISOU 938 N SER A 293 3633 5083 3894 419 -140 40 N ATOM 939 CA SER A 293 30.939 17.159 3.685 1.00 34.54 C ANISOU 939 CA SER A 293 3820 5221 4082 510 -224 -32 C ATOM 940 C SER A 293 31.626 17.990 2.614 1.00 37.31 C ANISOU 940 C SER A 293 4228 5565 4384 579 -113 -177 C ATOM 941 O SER A 293 32.855 18.078 2.576 1.00 42.60 O ANISOU 941 O SER A 293 4878 6297 5012 617 -77 -242 O ATOM 942 CB SER A 293 30.442 15.846 3.078 1.00 41.12 C ANISOU 942 CB SER A 293 4700 5897 5028 579 -413 30 C ATOM 943 OG SER A 293 29.854 15.022 4.066 1.00 41.17 O ANISOU 943 OG SER A 293 4636 5908 5101 530 -515 174 O ATOM 944 N LEU A 294 30.827 18.594 1.738 1.00 34.58 N ANISOU 944 N LEU A 294 3945 5143 4050 602 -55 -213 N ATOM 945 CA LEU A 294 31.355 19.495 0.717 1.00 36.67 C ANISOU 945 CA LEU A 294 4251 5406 4277 680 75 -346 C ATOM 946 C LEU A 294 32.264 20.590 1.284 1.00 37.44 C ANISOU 946 C LEU A 294 4286 5652 4289 628 243 -418 C ATOM 947 O LEU A 294 33.327 20.862 0.732 1.00 40.45 O ANISOU 947 O LEU A 294 4665 6047 4655 712 294 -503 O ATOM 948 CB LEU A 294 30.218 20.130 -0.095 1.00 27.52 C ANISOU 948 CB LEU A 294 3144 4178 3132 689 144 -357 C ATOM 949 CG LEU A 294 29.486 19.182 -1.045 1.00 32.08 C ANISOU 949 CG LEU A 294 3805 4590 3793 766 -24 -322 C ATOM 950 CD1 LEU A 294 28.154 19.780 -1.560 1.00 26.11 C ANISOU 950 CD1 LEU A 294 3077 3788 3054 732 35 -284 C ATOM 951 CD2 LEU A 294 30.414 18.798 -2.190 1.00 31.23 C ANISOU 951 CD2 LEU A 294 3775 4399 3690 931 -70 -427 C ATOM 952 N GLN A 295 31.866 21.233 2.376 1.00 40.18 N ANISOU 952 N GLN A 295 4586 6100 4580 498 329 -375 N ATOM 953 CA GLN A 295 32.688 22.345 2.846 1.00 44.61 C ANISOU 953 CA GLN A 295 5105 6788 5058 441 483 -456 C ATOM 954 C GLN A 295 33.834 21.936 3.777 1.00 43.01 C ANISOU 954 C GLN A 295 4835 6684 4822 400 419 -442 C ATOM 955 O GLN A 295 34.813 22.669 3.904 1.00 43.81 O ANISOU 955 O GLN A 295 4901 6868 4876 380 507 -517 O ATOM 956 CB GLN A 295 31.843 23.472 3.449 1.00 44.22 C ANISOU 956 CB GLN A 295 5064 6799 4940 331 644 -441 C ATOM 957 CG GLN A 295 31.354 23.239 4.853 1.00 43.29 C ANISOU 957 CG GLN A 295 4925 6742 4781 222 605 -325 C ATOM 958 CD GLN A 295 30.420 24.342 5.308 1.00 50.54 C ANISOU 958 CD GLN A 295 5883 7695 5627 138 777 -290 C ATOM 959 OE1 GLN A 295 29.980 24.369 6.456 1.00 54.98 O ANISOU 959 OE1 GLN A 295 6447 8307 6138 62 783 -193 O ATOM 960 NE2 GLN A 295 30.108 25.258 4.400 1.00 46.48 N ANISOU 960 NE2 GLN A 295 5402 7154 5104 165 932 -360 N ATOM 961 N ASN A 296 33.722 20.759 4.390 1.00 40.00 N ANISOU 961 N ASN A 296 4430 6294 4476 390 265 -341 N ATOM 962 CA ASN A 296 34.688 20.317 5.398 1.00 42.02 C ANISOU 962 CA ASN A 296 4609 6661 4696 343 208 -305 C ATOM 963 C ASN A 296 35.735 19.304 4.911 1.00 46.59 C ANISOU 963 C ASN A 296 5171 7211 5321 443 103 -293 C ATOM 964 O ASN A 296 36.879 19.331 5.370 1.00 49.07 O ANISOU 964 O ASN A 296 5423 7627 5597 421 110 -294 O ATOM 965 CB ASN A 296 33.957 19.781 6.640 1.00 42.47 C ANISOU 965 CB ASN A 296 4628 6762 4747 264 139 -186 C ATOM 966 CG ASN A 296 33.239 20.884 7.419 1.00 51.56 C ANISOU 966 CG ASN A 296 5798 7976 5817 160 266 -181 C ATOM 967 OD1 ASN A 296 33.728 22.014 7.511 1.00 49.35 O ANISOU 967 OD1 ASN A 296 5529 7767 5455 107 395 -274 O ATOM 968 ND2 ASN A 296 32.074 20.558 7.984 1.00 47.26 N ANISOU 968 ND2 ASN A 296 5261 7398 5297 138 233 -61 N ATOM 969 N MET A 297 35.351 18.413 3.996 1.00 32.50 N ANISOU 969 N MET A 297 3449 5286 3615 551 6 -269 N ATOM 970 CA MET A 297 36.288 17.424 3.479 1.00 39.38 C ANISOU 970 CA MET A 297 4331 6110 4520 661 -81 -245 C ATOM 971 C MET A 297 37.432 18.129 2.771 1.00 44.62 C ANISOU 971 C MET A 297 5001 6795 5156 737 18 -321 C ATOM 972 O MET A 297 37.269 19.261 2.318 1.00 35.07 O ANISOU 972 O MET A 297 3810 5587 3928 736 138 -410 O ATOM 973 CB MET A 297 35.607 16.495 2.480 1.00 33.22 C ANISOU 973 CB MET A 297 3653 5152 3819 771 -194 -226 C ATOM 974 CG MET A 297 34.635 15.506 3.087 1.00 45.89 C ANISOU 974 CG MET A 297 5241 6711 5483 722 -324 -123 C ATOM 975 SD MET A 297 34.008 14.415 1.795 1.00 55.67 S ANISOU 975 SD MET A 297 6616 7723 6812 850 -476 -114 S ATOM 976 CE MET A 297 35.502 13.526 1.378 1.00 68.57 C ANISOU 976 CE MET A 297 8284 9339 8430 980 -509 -102 C ATOM 977 N ASP A 298 38.584 17.465 2.672 1.00 38.29 N ANISOU 977 N ASP A 298 4180 6009 4359 810 -22 -270 N ATOM 978 CA ASP A 298 39.658 17.975 1.836 1.00 39.73 C ANISOU 978 CA ASP A 298 4377 6180 4540 921 59 -308 C ATOM 979 C ASP A 298 39.055 18.313 0.478 1.00 41.70 C ANISOU 979 C ASP A 298 4738 6279 4825 1054 95 -392 C ATOM 980 O ASP A 298 38.193 17.592 -0.014 1.00 38.32 O ANISOU 980 O ASP A 298 4399 5727 4432 1105 3 -384 O ATOM 981 CB ASP A 298 40.763 16.930 1.676 1.00 44.42 C ANISOU 981 CB ASP A 298 4971 6760 5145 1024 -3 -204 C ATOM 982 CG ASP A 298 41.493 16.658 2.971 1.00 45.50 C ANISOU 982 CG ASP A 298 4981 7064 5243 900 -23 -115 C ATOM 983 OD1 ASP A 298 41.641 17.597 3.785 1.00 39.79 O ANISOU 983 OD1 ASP A 298 4171 6473 4475 764 39 -152 O ATOM 984 OD2 ASP A 298 41.903 15.502 3.179 1.00 45.52 O ANISOU 984 OD2 ASP A 298 4975 7065 5255 940 -98 -7 O ATOM 985 N LEU A 299 39.509 19.405 -0.125 1.00 47.86 N ANISOU 985 N LEU A 299 5509 7073 5602 1110 226 -468 N ATOM 986 CA LEU A 299 38.922 19.891 -1.370 1.00 49.72 C ANISOU 986 CA LEU A 299 5833 7191 5867 1237 287 -556 C ATOM 987 C LEU A 299 38.944 18.849 -2.484 1.00 43.55 C ANISOU 987 C LEU A 299 5183 6243 5123 1430 187 -529 C ATOM 988 O LEU A 299 37.980 18.720 -3.232 1.00 45.80 O ANISOU 988 O LEU A 299 5563 6413 5427 1487 152 -576 O ATOM 989 CB LEU A 299 39.624 21.170 -1.832 1.00 47.47 C ANISOU 989 CB LEU A 299 5496 6953 5586 1293 454 -628 C ATOM 990 CG LEU A 299 39.001 21.867 -3.042 1.00 43.77 C ANISOU 990 CG LEU A 299 5092 6394 5146 1420 553 -725 C ATOM 991 CD1 LEU A 299 37.508 22.090 -2.809 1.00 39.95 C ANISOU 991 CD1 LEU A 299 4634 5903 4643 1298 554 -763 C ATOM 992 CD2 LEU A 299 39.707 23.183 -3.296 1.00 37.96 C ANISOU 992 CD2 LEU A 299 4273 5727 4425 1456 733 -789 C ATOM 993 N SER A 300 40.047 18.114 -2.591 1.00 41.71 N ANISOU 993 N SER A 300 4962 5992 4892 1532 144 -445 N ATOM 994 CA SER A 300 40.202 17.105 -3.637 1.00 44.67 C ANISOU 994 CA SER A 300 5487 6200 5286 1733 60 -409 C ATOM 995 C SER A 300 39.171 15.977 -3.544 1.00 43.33 C ANISOU 995 C SER A 300 5404 5930 5128 1689 -103 -386 C ATOM 996 O SER A 300 38.761 15.426 -4.564 1.00 44.45 O ANISOU 996 O SER A 300 5698 5907 5286 1829 -176 -410 O ATOM 997 CB SER A 300 41.624 16.523 -3.630 1.00 53.67 C ANISOU 997 CB SER A 300 6620 7354 6419 1840 63 -289 C ATOM 998 OG SER A 300 41.888 15.812 -2.426 1.00 65.83 O ANISOU 998 OG SER A 300 8073 9000 7939 1693 -5 -191 O ATOM 999 N LEU A 301 38.769 15.626 -2.323 1.00 40.66 N ANISOU 999 N LEU A 301 4973 5687 4788 1503 -163 -336 N ATOM 1000 CA LEU A 301 37.738 14.603 -2.123 1.00 41.33 C ANISOU 1000 CA LEU A 301 5113 5685 4907 1449 -316 -300 C ATOM 1001 C LEU A 301 36.330 15.193 -2.294 1.00 42.00 C ANISOU 1001 C LEU A 301 5213 5730 5015 1370 -321 -368 C ATOM 1002 O LEU A 301 35.430 14.540 -2.836 1.00 37.44 O ANISOU 1002 O LEU A 301 4737 5011 4479 1402 -443 -367 O ATOM 1003 CB LEU A 301 37.870 13.949 -0.741 1.00 48.98 C ANISOU 1003 CB LEU A 301 5963 6771 5876 1306 -370 -199 C ATOM 1004 CG LEU A 301 38.841 12.784 -0.494 1.00 57.82 C ANISOU 1004 CG LEU A 301 7084 7894 6991 1367 -424 -88 C ATOM 1005 CD1 LEU A 301 38.453 11.549 -1.298 1.00 61.19 C ANISOU 1005 CD1 LEU A 301 7669 8125 7457 1487 -557 -60 C ATOM 1006 CD2 LEU A 301 40.285 13.187 -0.779 1.00 62.72 C ANISOU 1006 CD2 LEU A 301 7686 8577 7569 1465 -314 -62 C ATOM 1007 N ALA A 302 36.137 16.422 -1.821 1.00 33.39 N ANISOU 1007 N ALA A 302 4025 4763 3897 1264 -189 -418 N ATOM 1008 CA ALA A 302 34.877 17.133 -2.050 1.00 39.32 C ANISOU 1008 CA ALA A 302 4790 5489 4661 1202 -153 -468 C ATOM 1009 C ALA A 302 34.588 17.299 -3.549 1.00 44.66 C ANISOU 1009 C ALA A 302 5592 6023 5353 1363 -146 -546 C ATOM 1010 O ALA A 302 33.442 17.176 -3.981 1.00 46.28 O ANISOU 1010 O ALA A 302 5858 6138 5589 1348 -211 -551 O ATOM 1011 CB ALA A 302 34.886 18.476 -1.356 1.00 34.32 C ANISOU 1011 CB ALA A 302 4048 5010 3981 1081 17 -508 C ATOM 1012 N CYS A 303 35.628 17.566 -4.339 1.00 43.34 N ANISOU 1012 N CYS A 303 5463 5837 5169 1527 -69 -596 N ATOM 1013 CA CYS A 303 35.480 17.648 -5.795 1.00 40.40 C ANISOU 1013 CA CYS A 303 5220 5324 4805 1718 -63 -666 C ATOM 1014 C CYS A 303 34.933 16.349 -6.390 1.00 42.48 C ANISOU 1014 C CYS A 303 5639 5408 5095 1791 -265 -635 C ATOM 1015 O CYS A 303 34.122 16.373 -7.311 1.00 42.68 O ANISOU 1015 O CYS A 303 5764 5320 5132 1858 -309 -686 O ATOM 1016 CB CYS A 303 36.803 18.026 -6.464 1.00 40.84 C ANISOU 1016 CB CYS A 303 5288 5383 4847 1908 47 -692 C ATOM 1017 SG CYS A 303 37.261 19.765 -6.231 1.00 47.30 S ANISOU 1017 SG CYS A 303 5949 6367 5657 1864 293 -763 S ATOM 1018 N LYS A 304 35.366 15.215 -5.853 1.00 43.13 N ANISOU 1018 N LYS A 304 5739 5465 5185 1774 -386 -548 N ATOM 1019 CA LYS A 304 34.867 13.925 -6.321 1.00 47.08 C ANISOU 1019 CA LYS A 304 6387 5788 5713 1828 -583 -514 C ATOM 1020 C LYS A 304 33.383 13.709 -5.999 1.00 50.66 C ANISOU 1020 C LYS A 304 6825 6202 6220 1672 -701 -493 C ATOM 1021 O LYS A 304 32.671 13.051 -6.756 1.00 55.64 O ANISOU 1021 O LYS A 304 7592 6666 6880 1725 -849 -502 O ATOM 1022 CB LYS A 304 35.733 12.778 -5.784 1.00 44.61 C ANISOU 1022 CB LYS A 304 6085 5468 5395 1848 -658 -416 C ATOM 1023 CG LYS A 304 37.152 12.776 -6.350 1.00 52.70 C ANISOU 1023 CG LYS A 304 7169 6481 6372 2042 -566 -403 C ATOM 1024 CD LYS A 304 37.904 11.501 -5.987 1.00 71.81 C ANISOU 1024 CD LYS A 304 9633 8868 8784 2080 -643 -287 C ATOM 1025 CE LYS A 304 39.288 11.446 -6.638 1.00 79.80 C ANISOU 1025 CE LYS A 304 10724 9849 9749 2294 -549 -240 C ATOM 1026 NZ LYS A 304 39.220 11.267 -8.121 1.00 85.30 N ANISOU 1026 NZ LYS A 304 11648 10340 10422 2531 -583 -295 N ATOM 1027 N LEU A 305 32.918 14.267 -4.885 1.00 50.49 N ANISOU 1027 N LEU A 305 6645 6327 6213 1488 -639 -453 N ATOM 1028 CA LEU A 305 31.493 14.230 -4.555 1.00 50.37 C ANISOU 1028 CA LEU A 305 6599 6284 6253 1349 -721 -404 C ATOM 1029 C LEU A 305 30.674 14.972 -5.596 1.00 46.07 C ANISOU 1029 C LEU A 305 6123 5675 5707 1392 -681 -475 C ATOM 1030 O LEU A 305 29.565 14.565 -5.938 1.00 46.08 O ANISOU 1030 O LEU A 305 6181 5565 5762 1353 -814 -438 O ATOM 1031 CB LEU A 305 31.229 14.851 -3.185 1.00 49.89 C ANISOU 1031 CB LEU A 305 6369 6399 6190 1171 -624 -341 C ATOM 1032 CG LEU A 305 31.429 13.948 -1.976 1.00 61.11 C ANISOU 1032 CG LEU A 305 7704 7872 7643 1084 -711 -233 C ATOM 1033 CD1 LEU A 305 30.901 14.642 -0.731 1.00 61.74 C ANISOU 1033 CD1 LEU A 305 7643 8101 7716 924 -622 -169 C ATOM 1034 CD2 LEU A 305 30.730 12.614 -2.202 1.00 59.72 C ANISOU 1034 CD2 LEU A 305 7603 7531 7556 1096 -929 -159 C ATOM 1035 N VAL A 306 31.224 16.078 -6.081 1.00 35.92 N ANISOU 1035 N VAL A 306 4820 4464 4365 1471 -495 -569 N ATOM 1036 CA VAL A 306 30.560 16.892 -7.088 1.00 37.63 C ANISOU 1036 CA VAL A 306 5082 4643 4572 1531 -417 -642 C ATOM 1037 C VAL A 306 30.420 16.146 -8.427 1.00 47.08 C ANISOU 1037 C VAL A 306 6466 5645 5778 1702 -565 -689 C ATOM 1038 O VAL A 306 29.423 16.306 -9.138 1.00 47.20 O ANISOU 1038 O VAL A 306 6538 5586 5810 1704 -610 -706 O ATOM 1039 CB VAL A 306 31.292 18.241 -7.275 1.00 34.55 C ANISOU 1039 CB VAL A 306 4616 4381 4129 1592 -168 -730 C ATOM 1040 CG1 VAL A 306 30.738 18.990 -8.461 1.00 35.66 C ANISOU 1040 CG1 VAL A 306 4808 4479 4262 1697 -78 -811 C ATOM 1041 CG2 VAL A 306 31.177 19.086 -6.000 1.00 30.13 C ANISOU 1041 CG2 VAL A 306 3897 4000 3551 1404 -28 -691 C ATOM 1042 N GLN A 307 31.406 15.316 -8.757 1.00 53.59 N ANISOU 1042 N GLN A 307 7393 6384 6585 1844 -641 -700 N ATOM 1043 CA GLN A 307 31.365 14.545 -10.001 1.00 58.88 C ANISOU 1043 CA GLN A 307 8271 6853 7246 2023 -785 -743 C ATOM 1044 C GLN A 307 30.247 13.507 -9.977 1.00 58.08 C ANISOU 1044 C GLN A 307 8250 6612 7205 1922 -1029 -683 C ATOM 1045 O GLN A 307 29.777 13.070 -11.028 1.00 57.19 O ANISOU 1045 O GLN A 307 8306 6333 7090 2021 -1163 -726 O ATOM 1046 CB GLN A 307 32.712 13.862 -10.277 1.00 59.71 C ANISOU 1046 CB GLN A 307 8479 6896 7313 2204 -796 -741 C ATOM 1047 CG GLN A 307 33.908 14.803 -10.246 1.00 70.33 C ANISOU 1047 CG GLN A 307 9731 8372 8618 2305 -572 -769 C ATOM 1048 CD GLN A 307 33.591 16.195 -10.786 1.00 81.05 C ANISOU 1048 CD GLN A 307 11019 9808 9967 2341 -392 -859 C ATOM 1049 OE1 GLN A 307 32.917 16.350 -11.809 1.00 81.21 O ANISOU 1049 OE1 GLN A 307 11141 9731 9983 2437 -420 -924 O ATOM 1050 NE2 GLN A 307 34.084 17.215 -10.095 1.00 83.15 N ANISOU 1050 NE2 GLN A 307 11111 10253 10231 2265 -202 -863 N ATOM 1051 N ALA A 308 29.828 13.119 -8.774 1.00 48.17 N ANISOU 1051 N ALA A 308 6874 5421 6007 1729 -1090 -579 N ATOM 1052 CA ALA A 308 28.750 12.149 -8.603 1.00 44.02 C ANISOU 1052 CA ALA A 308 6389 4772 5565 1619 -1319 -495 C ATOM 1053 C ALA A 308 27.339 12.729 -8.815 1.00 48.15 C ANISOU 1053 C ALA A 308 6872 5288 6133 1507 -1341 -465 C ATOM 1054 O ALA A 308 26.357 11.986 -8.831 1.00 52.23 O ANISOU 1054 O ALA A 308 7427 5685 6732 1423 -1543 -386 O ATOM 1055 CB ALA A 308 28.846 11.489 -7.238 1.00 40.60 C ANISOU 1055 CB ALA A 308 5829 4408 5187 1481 -1367 -378 C ATOM 1056 N LEU A 309 27.223 14.044 -8.962 1.00 45.08 N ANISOU 1056 N LEU A 309 6401 5028 5700 1502 -1133 -512 N ATOM 1057 CA LEU A 309 25.920 14.624 -9.284 1.00 49.41 C ANISOU 1057 CA LEU A 309 6921 5572 6279 1413 -1131 -473 C ATOM 1058 C LEU A 309 25.415 14.066 -10.621 1.00 50.72 C ANISOU 1058 C LEU A 309 7274 5545 6454 1518 -1315 -525 C ATOM 1059 O LEU A 309 26.200 13.880 -11.553 1.00 48.41 O ANISOU 1059 O LEU A 309 7126 5169 6099 1712 -1322 -641 O ATOM 1060 CB LEU A 309 25.989 16.155 -9.323 1.00 36.75 C ANISOU 1060 CB LEU A 309 5211 4139 4614 1414 -848 -526 C ATOM 1061 CG LEU A 309 26.125 16.806 -7.944 1.00 40.29 C ANISOU 1061 CG LEU A 309 5481 4770 5055 1267 -682 -455 C ATOM 1062 CD1 LEU A 309 26.539 18.261 -8.060 1.00 38.22 C ANISOU 1062 CD1 LEU A 309 5141 4662 4720 1302 -395 -540 C ATOM 1063 CD2 LEU A 309 24.831 16.658 -7.135 1.00 36.51 C ANISOU 1063 CD2 LEU A 309 4922 4300 4652 1078 -756 -283 C ATOM 1064 N PRO A 310 24.104 13.780 -10.707 1.00 46.34 N ANISOU 1064 N PRO A 310 6722 4910 5975 1396 -1471 -425 N ATOM 1065 CA PRO A 310 23.455 13.306 -11.936 1.00 43.99 C ANISOU 1065 CA PRO A 310 6594 4431 5688 1465 -1665 -462 C ATOM 1066 C PRO A 310 23.454 14.389 -13.012 1.00 50.46 C ANISOU 1066 C PRO A 310 7447 5301 6424 1592 -1493 -576 C ATOM 1067 O PRO A 310 23.504 15.583 -12.696 1.00 49.21 O ANISOU 1067 O PRO A 310 7143 5323 6231 1563 -1234 -580 O ATOM 1068 CB PRO A 310 22.017 13.038 -11.478 1.00 50.31 C ANISOU 1068 CB PRO A 310 7317 5195 6605 1261 -1815 -286 C ATOM 1069 CG PRO A 310 21.830 13.981 -10.330 1.00 48.93 C ANISOU 1069 CG PRO A 310 6928 5227 6438 1129 -1586 -185 C ATOM 1070 CD PRO A 310 23.141 13.854 -9.596 1.00 44.78 C ANISOU 1070 CD PRO A 310 6364 4784 5865 1186 -1483 -249 C ATOM 1071 N ARG A 311 23.392 13.970 -14.271 1.00 55.60 N ANISOU 1071 N ARG A 311 8292 5793 7042 1739 -1635 -668 N ATOM 1072 CA ARG A 311 23.460 14.896 -15.395 1.00 59.98 C ANISOU 1072 CA ARG A 311 8891 6383 7516 1899 -1481 -785 C ATOM 1073 C ARG A 311 22.189 14.840 -16.236 1.00 61.23 C ANISOU 1073 C ARG A 311 9118 6447 7700 1852 -1634 -751 C ATOM 1074 O ARG A 311 22.179 15.278 -17.384 1.00 59.25 O ANISOU 1074 O ARG A 311 8959 6171 7383 2013 -1585 -856 O ATOM 1075 CB ARG A 311 24.658 14.555 -16.282 1.00 62.79 C ANISOU 1075 CB ARG A 311 9433 6638 7788 2172 -1484 -933 C ATOM 1076 CG ARG A 311 25.889 14.121 -15.519 1.00 66.99 C ANISOU 1076 CG ARG A 311 9949 7195 8309 2213 -1437 -933 C ATOM 1077 CD ARG A 311 26.382 15.238 -14.627 1.00 68.01 C ANISOU 1077 CD ARG A 311 9852 7557 8432 2147 -1148 -917 C ATOM 1078 NE ARG A 311 27.572 14.856 -13.874 1.00 69.94 N ANISOU 1078 NE ARG A 311 10069 7840 8666 2177 -1106 -907 N ATOM 1079 CZ ARG A 311 28.814 15.033 -14.308 1.00 64.65 C ANISOU 1079 CZ ARG A 311 9454 7174 7935 2387 -986 -983 C ATOM 1080 NH1 ARG A 311 29.030 15.582 -15.498 1.00 58.27 N ANISOU 1080 NH1 ARG A 311 8735 6329 7076 2603 -895 -1084 N ATOM 1081 NH2 ARG A 311 29.837 14.661 -13.554 1.00 60.49 N ANISOU 1081 NH2 ARG A 311 8888 6691 7404 2390 -953 -945 N ATOM 1082 N ASP A 312 21.122 14.289 -15.671 1.00 61.19 N ANISOU 1082 N ASP A 312 9064 6390 7795 1639 -1822 -595 N ATOM 1083 CA ASP A 312 19.881 14.120 -16.417 1.00 61.02 C ANISOU 1083 CA ASP A 312 9105 6266 7812 1571 -2006 -534 C ATOM 1084 C ASP A 312 18.715 14.832 -15.738 1.00 63.63 C ANISOU 1084 C ASP A 312 9229 6732 8217 1352 -1907 -343 C ATOM 1085 O ASP A 312 18.915 15.796 -14.998 1.00 59.04 O ANISOU 1085 O ASP A 312 8474 6345 7614 1305 -1627 -308 O ATOM 1086 CB ASP A 312 19.570 12.632 -16.629 1.00 60.72 C ANISOU 1086 CB ASP A 312 9247 5983 7841 1537 -2384 -505 C ATOM 1087 CG ASP A 312 19.551 11.835 -15.329 1.00 67.17 C ANISOU 1087 CG ASP A 312 9970 6783 8768 1375 -2491 -368 C ATOM 1088 OD1 ASP A 312 19.533 12.447 -14.241 1.00 68.13 O ANISOU 1088 OD1 ASP A 312 9883 7082 8922 1263 -2297 -268 O ATOM 1089 OD2 ASP A 312 19.551 10.583 -15.398 1.00 69.84 O ANISOU 1089 OD2 ASP A 312 10448 6928 9160 1369 -2768 -360 O ATOM 1090 N ALA A 313 17.501 14.354 -15.998 1.00 61.54 N ANISOU 1090 N ALA A 313 8990 6357 8036 1222 -2139 -210 N ATOM 1091 CA ALA A 313 16.299 14.894 -15.370 1.00 56.43 C ANISOU 1091 CA ALA A 313 8157 5811 7471 1014 -2074 18 C ATOM 1092 C ALA A 313 16.444 15.013 -13.851 1.00 54.60 C ANISOU 1092 C ALA A 313 7751 5697 7297 888 -1947 152 C ATOM 1093 O ALA A 313 15.893 15.926 -13.237 1.00 50.38 O ANISOU 1093 O ALA A 313 7051 5319 6771 781 -1731 293 O ATOM 1094 CB ALA A 313 15.097 14.031 -15.716 1.00 60.63 C ANISOU 1094 CB ALA A 313 8752 6167 8118 884 -2412 168 C ATOM 1095 N ARG A 314 17.188 14.084 -13.254 1.00 56.42 N ANISOU 1095 N ARG A 314 6962 6263 8210 931 -1782 -9 N ATOM 1096 CA ARG A 314 17.430 14.078 -11.812 1.00 49.82 C ANISOU 1096 CA ARG A 314 6048 5469 7411 881 -1685 107 C ATOM 1097 C ARG A 314 18.111 15.349 -11.291 1.00 44.84 C ANISOU 1097 C ARG A 314 5405 5028 6603 840 -1429 98 C ATOM 1098 O ARG A 314 17.903 15.735 -10.143 1.00 48.27 O ANISOU 1098 O ARG A 314 5786 5493 7061 773 -1315 235 O ATOM 1099 CB ARG A 314 18.256 12.853 -11.417 1.00 49.49 C ANISOU 1099 CB ARG A 314 5987 5392 7426 951 -1813 35 C ATOM 1100 CG ARG A 314 17.524 11.533 -11.579 1.00 56.30 C ANISOU 1100 CG ARG A 314 6836 6052 8503 979 -2074 86 C ATOM 1101 CD ARG A 314 18.469 10.358 -11.389 1.00 59.37 C ANISOU 1101 CD ARG A 314 7214 6417 8926 1059 -2201 -21 C ATOM 1102 NE ARG A 314 19.524 10.342 -12.401 1.00 63.36 N ANISOU 1102 NE ARG A 314 7803 7004 9267 1160 -2204 -247 N ATOM 1103 CZ ARG A 314 20.642 9.623 -12.312 1.00 64.07 C ANISOU 1103 CZ ARG A 314 7895 7129 9319 1238 -2246 -369 C ATOM 1104 NH1 ARG A 314 20.865 8.859 -11.248 1.00 62.87 N ANISOU 1104 NH1 ARG A 314 7664 6939 9284 1218 -2293 -294 N ATOM 1105 NH2 ARG A 314 21.544 9.677 -13.284 1.00 62.26 N ANISOU 1105 NH2 ARG A 314 7745 6977 8936 1339 -2237 -558 N ATOM 1106 N LEU A 315 18.928 15.991 -12.120 1.00 42.12 N ANISOU 1106 N LEU A 315 5110 4810 6084 885 -1343 -59 N ATOM 1107 CA LEU A 315 19.574 17.235 -11.704 1.00 43.02 C ANISOU 1107 CA LEU A 315 5210 5097 6039 846 -1115 -66 C ATOM 1108 C LEU A 315 18.547 18.363 -11.600 1.00 44.60 C ANISOU 1108 C LEU A 315 5399 5309 6238 750 -989 65 C ATOM 1109 O LEU A 315 18.610 19.198 -10.692 1.00 45.58 O ANISOU 1109 O LEU A 315 5493 5515 6312 687 -826 149 O ATOM 1110 CB LEU A 315 20.727 17.616 -12.640 1.00 42.42 C ANISOU 1110 CB LEU A 315 5175 5153 5789 926 -1061 -251 C ATOM 1111 CG LEU A 315 21.615 18.790 -12.192 1.00 41.48 C ANISOU 1111 CG LEU A 315 5034 5213 5515 897 -850 -267 C ATOM 1112 CD1 LEU A 315 22.243 18.540 -10.820 1.00 33.30 C ANISOU 1112 CD1 LEU A 315 3954 4201 4496 872 -804 -211 C ATOM 1113 CD2 LEU A 315 22.703 19.075 -13.217 1.00 36.46 C ANISOU 1113 CD2 LEU A 315 4427 4697 4728 989 -815 -431 C ATOM 1114 N ILE A 316 17.588 18.380 -12.516 1.00 41.76 N ANISOU 1114 N ILE A 316 5068 4862 5938 739 -1068 84 N ATOM 1115 CA ILE A 316 16.502 19.353 -12.424 1.00 39.69 C ANISOU 1115 CA ILE A 316 4791 4590 5699 644 -961 226 C ATOM 1116 C ILE A 316 15.699 19.093 -11.154 1.00 40.25 C ANISOU 1116 C ILE A 316 4808 4573 5911 581 -956 432 C ATOM 1117 O ILE A 316 15.332 20.023 -10.436 1.00 41.76 O ANISOU 1117 O ILE A 316 4975 4821 6072 511 -793 549 O ATOM 1118 CB ILE A 316 15.573 19.304 -13.652 1.00 49.35 C ANISOU 1118 CB ILE A 316 6054 5717 6980 641 -1068 221 C ATOM 1119 CG1 ILE A 316 16.308 19.809 -14.893 1.00 53.21 C ANISOU 1119 CG1 ILE A 316 6592 6320 7306 703 -1032 35 C ATOM 1120 CG2 ILE A 316 14.331 20.143 -13.408 1.00 52.00 C ANISOU 1120 CG2 ILE A 316 6363 6014 7379 535 -973 403 C ATOM 1121 CD1 ILE A 316 15.453 19.874 -16.124 1.00 53.45 C ANISOU 1121 CD1 ILE A 316 6667 6272 7370 701 -1124 21 C ATOM 1122 N ALA A 317 15.446 17.818 -10.870 1.00 45.60 N ANISOU 1122 N ALA A 317 5466 5115 6744 612 -1137 477 N ATOM 1123 CA ALA A 317 14.719 17.435 -9.665 1.00 46.36 C ANISOU 1123 CA ALA A 317 5499 5127 6988 568 -1148 682 C ATOM 1124 C ALA A 317 15.392 18.015 -8.424 1.00 44.00 C ANISOU 1124 C ALA A 317 5171 4959 6590 548 -967 716 C ATOM 1125 O ALA A 317 14.728 18.463 -7.488 1.00 48.11 O ANISOU 1125 O ALA A 317 5656 5474 7148 494 -865 891 O ATOM 1126 CB ALA A 317 14.629 15.914 -9.560 1.00 45.18 C ANISOU 1126 CB ALA A 317 5323 4832 7011 619 -1379 697 C ATOM 1127 N ILE A 318 16.720 18.011 -8.429 1.00 40.99 N ANISOU 1127 N ILE A 318 4809 4690 6077 595 -930 551 N ATOM 1128 CA ILE A 318 17.485 18.501 -7.290 1.00 39.17 C ANISOU 1128 CA ILE A 318 4558 4577 5748 580 -781 567 C ATOM 1129 C ILE A 318 17.400 20.021 -7.181 1.00 34.20 C ANISOU 1129 C ILE A 318 3949 4064 4983 523 -573 592 C ATOM 1130 O ILE A 318 17.217 20.557 -6.097 1.00 36.62 O ANISOU 1130 O ILE A 318 4239 4407 5269 484 -452 707 O ATOM 1131 CB ILE A 318 18.946 18.050 -7.374 1.00 37.06 C ANISOU 1131 CB ILE A 318 4302 4388 5390 644 -809 393 C ATOM 1132 CG1 ILE A 318 19.061 16.595 -6.907 1.00 40.23 C ANISOU 1132 CG1 ILE A 318 4664 4685 5935 685 -980 414 C ATOM 1133 CG2 ILE A 318 19.843 18.962 -6.542 1.00 43.47 C ANISOU 1133 CG2 ILE A 318 5114 5348 6055 621 -629 376 C ATOM 1134 CD1 ILE A 318 20.280 15.890 -7.435 1.00 38.89 C ANISOU 1134 CD1 ILE A 318 4515 4549 5714 764 -1065 231 C ATOM 1135 N CYS A 319 17.529 20.700 -8.312 1.00 31.45 N ANISOU 1135 N CYS A 319 3637 3771 4541 525 -536 483 N ATOM 1136 CA CYS A 319 17.433 22.160 -8.353 1.00 43.35 C ANISOU 1136 CA CYS A 319 5157 5387 5929 471 -350 499 C ATOM 1137 C CYS A 319 16.070 22.706 -7.900 1.00 45.75 C ANISOU 1137 C CYS A 319 5447 5627 6310 397 -279 694 C ATOM 1138 O CYS A 319 16.003 23.797 -7.338 1.00 44.02 O ANISOU 1138 O CYS A 319 5231 5489 6007 352 -113 750 O ATOM 1139 CB CYS A 319 17.752 22.683 -9.757 1.00 32.46 C ANISOU 1139 CB CYS A 319 3807 4072 4454 492 -343 355 C ATOM 1140 SG CYS A 319 19.456 22.402 -10.315 1.00 46.78 S ANISOU 1140 SG CYS A 319 5637 6000 6138 586 -369 138 S ATOM 1141 N VAL A 320 14.990 21.960 -8.143 1.00 41.06 N ANISOU 1141 N VAL A 320 4838 4885 5879 389 -406 802 N ATOM 1142 CA VAL A 320 13.654 22.462 -7.814 1.00 37.09 C ANISOU 1142 CA VAL A 320 4318 4315 5460 324 -341 1002 C ATOM 1143 C VAL A 320 13.144 21.982 -6.462 1.00 37.70 C ANISOU 1143 C VAL A 320 4353 4329 5643 320 -337 1191 C ATOM 1144 O VAL A 320 12.077 22.402 -6.013 1.00 42.66 O ANISOU 1144 O VAL A 320 4963 4909 6336 277 -265 1379 O ATOM 1145 CB VAL A 320 12.610 22.142 -8.914 1.00 48.23 C ANISOU 1145 CB VAL A 320 5734 5599 6994 304 -465 1045 C ATOM 1146 CG1 VAL A 320 13.113 22.605 -10.273 1.00 46.61 C ANISOU 1146 CG1 VAL A 320 5570 5463 6676 318 -467 858 C ATOM 1147 CG2 VAL A 320 12.276 20.652 -8.934 1.00 48.46 C ANISOU 1147 CG2 VAL A 320 5740 5470 7203 346 -689 1090 C ATOM 1148 N ASP A 321 13.903 21.111 -5.805 1.00 38.13 N ANISOU 1148 N ASP A 321 4388 4385 5713 370 -410 1150 N ATOM 1149 CA ASP A 321 13.514 20.664 -4.471 1.00 35.70 C ANISOU 1149 CA ASP A 321 4035 4035 5496 375 -399 1328 C ATOM 1150 C ASP A 321 13.886 21.720 -3.434 1.00 33.79 C ANISOU 1150 C ASP A 321 3813 3919 5107 358 -194 1359 C ATOM 1151 O ASP A 321 14.971 22.300 -3.491 1.00 37.89 O ANISOU 1151 O ASP A 321 4369 4560 5468 364 -117 1203 O ATOM 1152 CB ASP A 321 14.152 19.317 -4.126 1.00 41.81 C ANISOU 1152 CB ASP A 321 4773 4762 6353 430 -556 1281 C ATOM 1153 CG ASP A 321 13.686 18.781 -2.783 1.00 48.71 C ANISOU 1153 CG ASP A 321 5585 5588 7336 440 -557 1480 C ATOM 1154 OD1 ASP A 321 12.486 18.452 -2.653 1.00 56.10 O ANISOU 1154 OD1 ASP A 321 6476 6407 8432 427 -611 1675 O ATOM 1155 OD2 ASP A 321 14.515 18.692 -1.854 1.00 50.41 O ANISOU 1155 OD2 ASP A 321 5793 5881 7479 462 -503 1450 O ATOM 1156 N GLN A 322 12.986 21.962 -2.487 1.00 35.50 N ANISOU 1156 N GLN A 322 4007 4103 5378 343 -112 1569 N ATOM 1157 CA GLN A 322 13.208 22.980 -1.464 1.00 38.12 C ANISOU 1157 CA GLN A 322 4371 4542 5571 335 77 1612 C ATOM 1158 C GLN A 322 14.437 22.688 -0.603 1.00 39.56 C ANISOU 1158 C GLN A 322 4561 4806 5664 374 83 1517 C ATOM 1159 O GLN A 322 15.068 23.608 -0.092 1.00 34.48 O ANISOU 1159 O GLN A 322 3965 4272 4865 368 217 1460 O ATOM 1160 CB GLN A 322 11.982 23.141 -0.567 1.00 38.90 C ANISOU 1160 CB GLN A 322 4444 4582 5753 332 154 1869 C ATOM 1161 CG GLN A 322 12.122 24.279 0.433 1.00 50.15 C ANISOU 1161 CG GLN A 322 5918 6113 7022 333 353 1912 C ATOM 1162 CD GLN A 322 10.897 24.450 1.316 1.00 57.36 C ANISOU 1162 CD GLN A 322 6811 6974 8008 347 440 2175 C ATOM 1163 OE1 GLN A 322 10.622 25.547 1.802 1.00 57.45 O ANISOU 1163 OE1 GLN A 322 6872 7047 7910 340 608 2233 O ATOM 1164 NE2 GLN A 322 10.155 23.363 1.526 1.00 48.93 N ANISOU 1164 NE2 GLN A 322 5670 5791 7129 372 323 2342 N ATOM 1165 N ASN A 323 14.766 21.409 -0.438 1.00 38.10 N ANISOU 1165 N ASN A 323 4328 4562 5585 411 -67 1505 N ATOM 1166 CA ASN A 323 15.948 21.023 0.337 1.00 39.48 C ANISOU 1166 CA ASN A 323 4504 4806 5692 444 -74 1418 C ATOM 1167 C ASN A 323 17.166 20.744 -0.533 1.00 39.49 C ANISOU 1167 C ASN A 323 4523 4853 5629 457 -152 1189 C ATOM 1168 O ASN A 323 18.262 21.229 -0.251 1.00 39.13 O ANISOU 1168 O ASN A 323 4512 4913 5444 460 -81 1073 O ATOM 1169 CB ASN A 323 15.657 19.786 1.193 1.00 43.47 C ANISOU 1169 CB ASN A 323 4936 5230 6350 480 -181 1554 C ATOM 1170 CG ASN A 323 14.461 19.972 2.091 1.00 47.83 C ANISOU 1170 CG ASN A 323 5459 5738 6974 484 -106 1802 C ATOM 1171 OD1 ASN A 323 14.506 20.738 3.057 1.00 44.48 O ANISOU 1171 OD1 ASN A 323 5071 5392 6439 490 44 1866 O ATOM 1172 ND2 ASN A 323 13.375 19.273 1.777 1.00 47.80 N ANISOU 1172 ND2 ASN A 323 5394 5607 7160 485 -213 1951 N ATOM 1173 N ALA A 324 16.980 19.948 -1.583 1.00 38.29 N ANISOU 1173 N ALA A 324 4350 4618 5582 470 -304 1130 N ATOM 1174 CA ALA A 324 18.107 19.524 -2.418 1.00 39.98 C ANISOU 1174 CA ALA A 324 4581 4866 5745 502 -389 922 C ATOM 1175 C ALA A 324 18.802 20.682 -3.126 1.00 41.24 C ANISOU 1175 C ALA A 324 4796 5145 5729 488 -275 776 C ATOM 1176 O ALA A 324 20.001 20.620 -3.379 1.00 36.79 O ANISOU 1176 O ALA A 324 4247 4656 5077 517 -284 626 O ATOM 1177 CB ALA A 324 17.661 18.474 -3.435 1.00 40.31 C ANISOU 1177 CB ALA A 324 4602 4786 5930 530 -580 892 C ATOM 1178 N ASN A 325 18.058 21.733 -3.465 1.00 35.25 N ANISOU 1178 N ASN A 325 4061 4405 4929 445 -170 829 N ATOM 1179 CA ASN A 325 18.667 22.836 -4.198 1.00 36.52 C ANISOU 1179 CA ASN A 325 4261 4677 4938 431 -70 699 C ATOM 1180 C ASN A 325 19.863 23.417 -3.430 1.00 35.31 C ANISOU 1180 C ASN A 325 4126 4643 4647 435 30 632 C ATOM 1181 O ASN A 325 20.813 23.906 -4.026 1.00 32.90 O ANISOU 1181 O ASN A 325 3837 4430 4235 447 61 495 O ATOM 1182 CB ASN A 325 17.634 23.920 -4.548 1.00 35.71 C ANISOU 1182 CB ASN A 325 4173 4576 4820 377 37 784 C ATOM 1183 CG ASN A 325 17.386 24.884 -3.408 1.00 39.26 C ANISOU 1183 CG ASN A 325 4639 5077 5200 341 196 896 C ATOM 1184 OD1 ASN A 325 16.439 24.727 -2.636 1.00 42.96 O ANISOU 1184 OD1 ASN A 325 5095 5478 5751 330 216 1068 O ATOM 1185 ND2 ASN A 325 18.240 25.889 -3.295 1.00 34.69 N ANISOU 1185 ND2 ASN A 325 4090 4618 4473 331 307 805 N ATOM 1186 N HIS A 326 19.823 23.325 -2.106 1.00 32.35 N ANISOU 1186 N HIS A 326 3747 4265 4279 429 71 736 N ATOM 1187 CA HIS A 326 20.908 23.845 -1.278 1.00 36.38 C ANISOU 1187 CA HIS A 326 4283 4874 4667 430 153 686 C ATOM 1188 C HIS A 326 22.233 23.082 -1.415 1.00 37.15 C ANISOU 1188 C HIS A 326 4365 5002 4747 470 65 553 C ATOM 1189 O HIS A 326 23.291 23.601 -1.058 1.00 30.64 O ANISOU 1189 O HIS A 326 3561 4265 3814 469 123 484 O ATOM 1190 CB HIS A 326 20.481 23.908 0.186 1.00 37.11 C ANISOU 1190 CB HIS A 326 4382 4952 4768 423 215 835 C ATOM 1191 CG HIS A 326 19.390 24.899 0.444 1.00 40.98 C ANISOU 1191 CG HIS A 326 4899 5437 5236 390 336 960 C ATOM 1192 ND1 HIS A 326 19.630 26.247 0.584 1.00 36.12 N ANISOU 1192 ND1 HIS A 326 4334 4908 4483 363 469 930 N ATOM 1193 CD2 HIS A 326 18.053 24.737 0.583 1.00 43.87 C ANISOU 1193 CD2 HIS A 326 5245 5719 5704 383 342 1123 C ATOM 1194 CE1 HIS A 326 18.488 26.875 0.800 1.00 42.71 C ANISOU 1194 CE1 HIS A 326 5183 5714 5330 341 558 1062 C ATOM 1195 NE2 HIS A 326 17.515 25.982 0.801 1.00 44.22 N ANISOU 1195 NE2 HIS A 326 5332 5804 5666 353 487 1185 N ATOM 1196 N VAL A 327 22.182 21.851 -1.911 1.00 29.19 N ANISOU 1196 N VAL A 327 3322 3916 3851 507 -78 523 N ATOM 1197 CA VAL A 327 23.415 21.137 -2.214 1.00 31.51 C ANISOU 1197 CA VAL A 327 3605 4239 4128 551 -160 390 C ATOM 1198 C VAL A 327 24.126 21.848 -3.368 1.00 39.27 C ANISOU 1198 C VAL A 327 4612 5308 5001 568 -121 249 C ATOM 1199 O VAL A 327 25.333 22.103 -3.311 1.00 36.31 O ANISOU 1199 O VAL A 327 4242 5018 4535 585 -88 163 O ATOM 1200 CB VAL A 327 23.153 19.661 -2.563 1.00 34.34 C ANISOU 1200 CB VAL A 327 3926 4488 4635 593 -331 384 C ATOM 1201 CG1 VAL A 327 24.412 19.024 -3.124 1.00 35.64 C ANISOU 1201 CG1 VAL A 327 4087 4685 4768 648 -406 231 C ATOM 1202 CG2 VAL A 327 22.682 18.901 -1.325 1.00 30.88 C ANISOU 1202 CG2 VAL A 327 3445 3979 4308 583 -372 526 C ATOM 1203 N ILE A 328 23.360 22.193 -4.403 1.00 28.87 N ANISOU 1203 N ILE A 328 3305 3970 3695 564 -122 237 N ATOM 1204 CA ILE A 328 23.915 22.883 -5.557 1.00 27.98 C ANISOU 1204 CA ILE A 328 3207 3942 3483 586 -83 117 C ATOM 1205 C ILE A 328 24.458 24.249 -5.165 1.00 31.18 C ANISOU 1205 C ILE A 328 3623 4463 3760 547 67 116 C ATOM 1206 O ILE A 328 25.528 24.645 -5.624 1.00 33.11 O ANISOU 1206 O ILE A 328 3864 4799 3915 575 95 19 O ATOM 1207 CB ILE A 328 22.890 23.033 -6.689 1.00 33.08 C ANISOU 1207 CB ILE A 328 3861 4541 4169 582 -111 118 C ATOM 1208 CG1 ILE A 328 22.292 21.671 -7.052 1.00 35.05 C ANISOU 1208 CG1 ILE A 328 4102 4656 4557 619 -281 126 C ATOM 1209 CG2 ILE A 328 23.542 23.634 -7.911 1.00 29.13 C ANISOU 1209 CG2 ILE A 328 3368 4136 3565 619 -79 -11 C ATOM 1210 CD1 ILE A 328 23.331 20.635 -7.413 1.00 37.00 C ANISOU 1210 CD1 ILE A 328 4348 4903 4808 700 -394 2 C ATOM 1211 N GLN A 329 23.734 24.961 -4.304 1.00 30.65 N ANISOU 1211 N GLN A 329 3570 4387 3687 488 157 232 N ATOM 1212 CA GLN A 329 24.224 26.236 -3.785 1.00 32.23 C ANISOU 1212 CA GLN A 329 3789 4683 3772 452 286 236 C ATOM 1213 C GLN A 329 25.520 26.077 -2.975 1.00 28.76 C ANISOU 1213 C GLN A 329 3354 4295 3280 469 281 196 C ATOM 1214 O GLN A 329 26.389 26.936 -3.019 1.00 28.63 O ANISOU 1214 O GLN A 329 3343 4367 3169 462 343 145 O ATOM 1215 CB GLN A 329 23.150 26.946 -2.939 1.00 26.31 C ANISOU 1215 CB GLN A 329 3065 3906 3027 397 379 372 C ATOM 1216 CG GLN A 329 21.862 27.291 -3.723 1.00 25.67 C ANISOU 1216 CG GLN A 329 2979 3780 2996 369 403 428 C ATOM 1217 CD GLN A 329 21.038 28.361 -3.031 1.00 35.82 C ANISOU 1217 CD GLN A 329 4291 5072 4247 317 530 544 C ATOM 1218 OE1 GLN A 329 21.559 29.396 -2.618 1.00 38.43 O ANISOU 1218 OE1 GLN A 329 4646 5482 4474 297 624 523 O ATOM 1219 NE2 GLN A 329 19.750 28.113 -2.894 1.00 36.58 N ANISOU 1219 NE2 GLN A 329 4384 5079 4435 299 530 672 N ATOM 1220 N LYS A 330 25.634 25.001 -2.211 1.00 25.68 N ANISOU 1220 N LYS A 330 2955 3843 2958 486 205 230 N ATOM 1221 CA LYS A 330 26.855 24.755 -1.456 1.00 33.70 C ANISOU 1221 CA LYS A 330 3972 4898 3934 498 191 196 C ATOM 1222 C LYS A 330 28.027 24.449 -2.391 1.00 33.90 C ANISOU 1222 C LYS A 330 3974 4977 3932 547 142 69 C ATOM 1223 O LYS A 330 29.145 24.916 -2.176 1.00 29.14 O ANISOU 1223 O LYS A 330 3373 4446 3254 549 175 29 O ATOM 1224 CB LYS A 330 26.668 23.608 -0.462 1.00 28.37 C ANISOU 1224 CB LYS A 330 3282 4147 3350 506 118 267 C ATOM 1225 CG LYS A 330 27.910 23.308 0.343 1.00 27.84 C ANISOU 1225 CG LYS A 330 3214 4116 3250 512 101 238 C ATOM 1226 CD LYS A 330 28.244 24.467 1.252 1.00 32.58 C ANISOU 1226 CD LYS A 330 3861 4776 3743 473 204 275 C ATOM 1227 CE LYS A 330 27.145 24.674 2.283 1.00 34.30 C ANISOU 1227 CE LYS A 330 4108 4950 3976 449 255 406 C ATOM 1228 NZ LYS A 330 27.616 25.609 3.345 1.00 39.54 N ANISOU 1228 NZ LYS A 330 4829 5663 4533 425 332 435 N ATOM 1229 N VAL A 331 27.769 23.665 -3.431 1.00 30.86 N ANISOU 1229 N VAL A 331 3569 4550 3606 594 58 12 N ATOM 1230 CA VAL A 331 28.805 23.380 -4.413 1.00 28.12 C ANISOU 1230 CA VAL A 331 3206 4256 3224 658 17 -105 C ATOM 1231 C VAL A 331 29.355 24.687 -4.971 1.00 33.41 C ANISOU 1231 C VAL A 331 3874 5037 3782 653 118 -144 C ATOM 1232 O VAL A 331 30.568 24.906 -5.010 1.00 30.88 O ANISOU 1232 O VAL A 331 3540 4790 3404 679 135 -189 O ATOM 1233 CB VAL A 331 28.264 22.525 -5.557 1.00 35.66 C ANISOU 1233 CB VAL A 331 4156 5149 4244 715 -83 -163 C ATOM 1234 CG1 VAL A 331 29.231 22.554 -6.743 1.00 33.47 C ANISOU 1234 CG1 VAL A 331 3871 4947 3897 794 -93 -283 C ATOM 1235 CG2 VAL A 331 28.004 21.099 -5.076 1.00 27.03 C ANISOU 1235 CG2 VAL A 331 3051 3947 3271 734 -208 -139 C ATOM 1236 N VAL A 332 28.442 25.558 -5.390 1.00 29.29 N ANISOU 1236 N VAL A 332 3362 4526 3242 617 182 -114 N ATOM 1237 CA VAL A 332 28.795 26.841 -5.980 1.00 30.06 C ANISOU 1237 CA VAL A 332 3447 4726 3248 607 276 -141 C ATOM 1238 C VAL A 332 29.602 27.683 -5.000 1.00 33.08 C ANISOU 1238 C VAL A 332 3836 5167 3567 567 344 -107 C ATOM 1239 O VAL A 332 30.535 28.378 -5.391 1.00 29.39 O ANISOU 1239 O VAL A 332 3342 4788 3035 584 382 -145 O ATOM 1240 CB VAL A 332 27.518 27.601 -6.419 1.00 32.39 C ANISOU 1240 CB VAL A 332 3751 5007 3550 561 334 -96 C ATOM 1241 CG1 VAL A 332 27.825 29.044 -6.764 1.00 31.37 C ANISOU 1241 CG1 VAL A 332 3603 4981 3334 533 440 -103 C ATOM 1242 CG2 VAL A 332 26.884 26.892 -7.597 1.00 30.67 C ANISOU 1242 CG2 VAL A 332 3529 4742 3384 606 259 -143 C ATOM 1243 N ALA A 333 29.267 27.589 -3.717 1.00 27.76 N ANISOU 1243 N ALA A 333 3194 4440 2913 521 352 -30 N ATOM 1244 CA ALA A 333 29.952 28.380 -2.710 1.00 26.92 C ANISOU 1244 CA ALA A 333 3109 4375 2745 483 405 3 C ATOM 1245 C ALA A 333 31.369 27.895 -2.413 1.00 28.54 C ANISOU 1245 C ALA A 333 3298 4608 2938 514 355 -36 C ATOM 1246 O ALA A 333 32.272 28.713 -2.242 1.00 32.96 O ANISOU 1246 O ALA A 333 3854 5232 3438 502 389 -42 O ATOM 1247 CB ALA A 333 29.125 28.444 -1.415 1.00 27.16 C ANISOU 1247 CB ALA A 333 3188 4343 2788 436 433 101 C ATOM 1248 N VAL A 334 31.584 26.583 -2.345 1.00 31.92 N ANISOU 1248 N VAL A 334 3714 4985 3430 551 270 -57 N ATOM 1249 CA VAL A 334 32.875 26.095 -1.829 1.00 35.90 C ANISOU 1249 CA VAL A 334 4205 5504 3930 568 227 -74 C ATOM 1250 C VAL A 334 33.746 25.236 -2.747 1.00 35.57 C ANISOU 1250 C VAL A 334 4121 5482 3911 644 164 -152 C ATOM 1251 O VAL A 334 34.817 24.800 -2.326 1.00 28.49 O ANISOU 1251 O VAL A 334 3211 4594 3019 657 131 -158 O ATOM 1252 CB VAL A 334 32.702 25.326 -0.513 1.00 34.89 C ANISOU 1252 CB VAL A 334 4101 5306 3852 540 187 -14 C ATOM 1253 CG1 VAL A 334 32.011 26.214 0.535 1.00 31.95 C ANISOU 1253 CG1 VAL A 334 3780 4922 3438 480 256 69 C ATOM 1254 CG2 VAL A 334 31.932 24.037 -0.758 1.00 33.07 C ANISOU 1254 CG2 VAL A 334 3851 4994 3720 570 109 -16 C ATOM 1255 N ILE A 335 33.292 24.973 -3.972 1.00 34.60 N ANISOU 1255 N ILE A 335 3983 5362 3802 696 145 -209 N ATOM 1256 CA ILE A 335 34.087 24.211 -4.941 1.00 28.80 C ANISOU 1256 CA ILE A 335 3219 4651 3073 786 90 -289 C ATOM 1257 C ILE A 335 34.518 25.111 -6.099 1.00 30.79 C ANISOU 1257 C ILE A 335 3445 5004 3251 832 149 -330 C ATOM 1258 O ILE A 335 33.741 25.941 -6.550 1.00 33.67 O ANISOU 1258 O ILE A 335 3813 5391 3588 807 202 -322 O ATOM 1259 CB ILE A 335 33.307 23.014 -5.519 1.00 29.56 C ANISOU 1259 CB ILE A 335 3323 4664 3244 835 -3 -333 C ATOM 1260 CG1 ILE A 335 32.711 22.155 -4.399 1.00 30.00 C ANISOU 1260 CG1 ILE A 335 3391 4619 3390 788 -63 -273 C ATOM 1261 CG2 ILE A 335 34.211 22.165 -6.411 1.00 28.83 C ANISOU 1261 CG2 ILE A 335 3212 4591 3150 939 -64 -419 C ATOM 1262 CD1 ILE A 335 33.748 21.514 -3.498 1.00 27.07 C ANISOU 1262 CD1 ILE A 335 3003 4241 3040 785 -96 -260 C ATOM 1263 N PRO A 336 35.763 24.949 -6.587 1.00 35.29 N ANISOU 1263 N PRO A 336 3981 5637 3791 903 142 -366 N ATOM 1264 CA PRO A 336 36.234 25.756 -7.718 1.00 33.42 C ANISOU 1264 CA PRO A 336 3706 5505 3488 962 199 -392 C ATOM 1265 C PRO A 336 35.444 25.468 -8.996 1.00 40.31 C ANISOU 1265 C PRO A 336 4587 6376 4353 1029 179 -461 C ATOM 1266 O PRO A 336 35.076 24.322 -9.254 1.00 32.45 O ANISOU 1266 O PRO A 336 3619 5307 3403 1076 96 -511 O ATOM 1267 CB PRO A 336 37.693 25.318 -7.877 1.00 34.28 C ANISOU 1267 CB PRO A 336 3780 5661 3585 1037 181 -403 C ATOM 1268 CG PRO A 336 38.080 24.784 -6.529 1.00 37.18 C ANISOU 1268 CG PRO A 336 4164 5963 4001 974 142 -358 C ATOM 1269 CD PRO A 336 36.835 24.104 -6.033 1.00 37.81 C ANISOU 1269 CD PRO A 336 4288 5939 4139 928 93 -365 C ATOM 1270 N LEU A 337 35.206 26.509 -9.787 1.00 36.45 N ANISOU 1270 N LEU A 337 4073 5966 3812 1034 249 -461 N ATOM 1271 CA LEU A 337 34.309 26.427 -10.932 1.00 36.75 C ANISOU 1271 CA LEU A 337 4124 6001 3840 1079 237 -516 C ATOM 1272 C LEU A 337 34.576 25.244 -11.885 1.00 38.19 C ANISOU 1272 C LEU A 337 4324 6165 4022 1207 155 -605 C ATOM 1273 O LEU A 337 33.636 24.621 -12.384 1.00 37.35 O ANISOU 1273 O LEU A 337 4259 5985 3948 1227 89 -651 O ATOM 1274 CB LEU A 337 34.299 27.764 -11.691 1.00 33.09 C ANISOU 1274 CB LEU A 337 3613 5648 3312 1077 331 -500 C ATOM 1275 CG LEU A 337 33.624 27.774 -13.071 1.00 38.47 C ANISOU 1275 CG LEU A 337 4296 6356 3966 1143 328 -560 C ATOM 1276 CD1 LEU A 337 32.140 27.380 -12.962 1.00 30.69 C ANISOU 1276 CD1 LEU A 337 3367 5254 3039 1080 281 -563 C ATOM 1277 CD2 LEU A 337 33.777 29.141 -13.731 1.00 31.27 C ANISOU 1277 CD2 LEU A 337 3318 5567 2996 1138 428 -532 C ATOM 1278 N LYS A 338 35.843 24.924 -12.128 1.00 36.82 N ANISOU 1278 N LYS A 338 4123 6051 3816 1297 153 -625 N ATOM 1279 CA LYS A 338 36.179 23.858 -13.078 1.00 41.15 C ANISOU 1279 CA LYS A 338 4694 6591 4349 1436 82 -713 C ATOM 1280 C LYS A 338 35.438 22.548 -12.770 1.00 44.93 C ANISOU 1280 C LYS A 338 5233 6928 4909 1431 -39 -757 C ATOM 1281 O LYS A 338 35.055 21.802 -13.672 1.00 38.55 O ANISOU 1281 O LYS A 338 4465 6080 4101 1521 -116 -838 O ATOM 1282 CB LYS A 338 37.696 23.630 -13.130 1.00 33.97 C ANISOU 1282 CB LYS A 338 3746 5754 3407 1525 100 -706 C ATOM 1283 CG LYS A 338 38.157 22.613 -14.178 1.00 37.67 C ANISOU 1283 CG LYS A 338 4240 6230 3843 1690 41 -795 C ATOM 1284 CD LYS A 338 37.605 22.921 -15.575 1.00 35.15 C ANISOU 1284 CD LYS A 338 3937 5965 3455 1782 53 -858 C ATOM 1285 CE LYS A 338 38.004 21.846 -16.590 1.00 40.11 C ANISOU 1285 CE LYS A 338 4609 6588 4042 1959 -17 -956 C ATOM 1286 NZ LYS A 338 37.256 22.001 -17.886 1.00 41.24 N ANISOU 1286 NZ LYS A 338 4790 6757 4124 2042 -30 -1028 N ATOM 1287 N ASN A 339 35.218 22.287 -11.489 1.00 41.12 N ANISOU 1287 N ASN A 339 4755 6368 4500 1327 -62 -700 N ATOM 1288 CA ASN A 339 34.576 21.051 -11.058 1.00 38.97 C ANISOU 1288 CA ASN A 339 4521 5963 4323 1315 -179 -720 C ATOM 1289 C ASN A 339 33.061 20.996 -11.288 1.00 44.46 C ANISOU 1289 C ASN A 339 5252 6572 5070 1269 -226 -717 C ATOM 1290 O ASN A 339 32.495 19.913 -11.422 1.00 45.00 O ANISOU 1290 O ASN A 339 5352 6533 5215 1298 -344 -752 O ATOM 1291 CB ASN A 339 34.914 20.794 -9.595 1.00 33.58 C ANISOU 1291 CB ASN A 339 3822 5237 3699 1227 -182 -648 C ATOM 1292 CG ASN A 339 36.402 20.620 -9.382 1.00 36.87 C ANISOU 1292 CG ASN A 339 4207 5717 4085 1275 -160 -649 C ATOM 1293 OD1 ASN A 339 36.959 19.572 -9.692 1.00 40.32 O ANISOU 1293 OD1 ASN A 339 4649 6127 4544 1361 -231 -704 O ATOM 1294 ND2 ASN A 339 37.057 21.657 -8.878 1.00 34.01 N ANISOU 1294 ND2 ASN A 339 3812 5434 3676 1221 -67 -584 N ATOM 1295 N TRP A 340 32.410 22.157 -11.338 1.00 42.89 N ANISOU 1295 N TRP A 340 5044 6414 4839 1197 -138 -668 N ATOM 1296 CA TRP A 340 30.965 22.200 -11.553 1.00 36.32 C ANISOU 1296 CA TRP A 340 4240 5501 4059 1146 -171 -647 C ATOM 1297 C TRP A 340 30.554 22.979 -12.802 1.00 38.04 C ANISOU 1297 C TRP A 340 4461 5783 4210 1180 -125 -685 C ATOM 1298 O TRP A 340 29.424 23.466 -12.902 1.00 36.96 O ANISOU 1298 O TRP A 340 4334 5609 4100 1111 -107 -643 O ATOM 1299 CB TRP A 340 30.222 22.726 -10.310 1.00 32.50 C ANISOU 1299 CB TRP A 340 3749 4973 3625 1014 -120 -535 C ATOM 1300 CG TRP A 340 30.699 24.058 -9.770 1.00 32.30 C ANISOU 1300 CG TRP A 340 3696 5050 3528 950 14 -479 C ATOM 1301 CD1 TRP A 340 31.705 24.267 -8.863 1.00 31.55 C ANISOU 1301 CD1 TRP A 340 3581 4999 3408 927 54 -448 C ATOM 1302 CD2 TRP A 340 30.162 25.357 -10.079 1.00 35.88 C ANISOU 1302 CD2 TRP A 340 4137 5563 3932 896 114 -444 C ATOM 1303 NE1 TRP A 340 31.834 25.617 -8.597 1.00 31.72 N ANISOU 1303 NE1 TRP A 340 3584 5100 3369 868 163 -400 N ATOM 1304 CE2 TRP A 340 30.902 26.305 -9.334 1.00 27.72 C ANISOU 1304 CE2 TRP A 340 3078 4607 2846 848 205 -398 C ATOM 1305 CE3 TRP A 340 29.128 25.810 -10.914 1.00 35.76 C ANISOU 1305 CE3 TRP A 340 4130 5541 3918 882 132 -446 C ATOM 1306 CZ2 TRP A 340 30.639 27.679 -9.398 1.00 25.29 C ANISOU 1306 CZ2 TRP A 340 2752 4368 2489 790 309 -357 C ATOM 1307 CZ3 TRP A 340 28.872 27.180 -10.979 1.00 27.98 C ANISOU 1307 CZ3 TRP A 340 3120 4629 2881 820 246 -402 C ATOM 1308 CH2 TRP A 340 29.629 28.095 -10.229 1.00 32.70 C ANISOU 1308 CH2 TRP A 340 3692 5304 3430 777 332 -361 C ATOM 1309 N GLU A 341 31.467 23.085 -13.756 1.00 43.42 N ANISOU 1309 N GLU A 341 5130 6562 4804 1289 -104 -757 N ATOM 1310 CA GLU A 341 31.176 23.762 -15.010 1.00 41.73 C ANISOU 1310 CA GLU A 341 4913 6421 4521 1338 -62 -797 C ATOM 1311 C GLU A 341 30.064 23.025 -15.756 1.00 45.05 C ANISOU 1311 C GLU A 341 5394 6733 4990 1368 -177 -848 C ATOM 1312 O GLU A 341 29.272 23.636 -16.476 1.00 36.68 O ANISOU 1312 O GLU A 341 4339 5687 3911 1348 -151 -846 O ATOM 1313 CB GLU A 341 32.427 23.832 -15.872 1.00 43.09 C ANISOU 1313 CB GLU A 341 5060 6716 4595 1474 -28 -858 C ATOM 1314 CG GLU A 341 32.585 25.119 -16.629 1.00 53.28 C ANISOU 1314 CG GLU A 341 6299 8144 5801 1485 87 -841 C ATOM 1315 CD GLU A 341 33.785 25.094 -17.558 1.00 64.27 C ANISOU 1315 CD GLU A 341 7663 9658 7101 1639 116 -889 C ATOM 1316 OE1 GLU A 341 34.009 26.109 -18.255 1.00 68.92 O ANISOU 1316 OE1 GLU A 341 8195 10370 7621 1666 208 -870 O ATOM 1317 OE2 GLU A 341 34.497 24.059 -17.587 1.00 58.16 O ANISOU 1317 OE2 GLU A 341 6917 8856 6325 1737 48 -939 O ATOM 1318 N PHE A 342 29.993 21.712 -15.570 1.00 38.44 N ANISOU 1318 N PHE A 342 4600 5782 4223 1411 -310 -887 N ATOM 1319 CA PHE A 342 28.933 20.933 -16.193 1.00 37.27 C ANISOU 1319 CA PHE A 342 4511 5508 4141 1435 -445 -928 C ATOM 1320 C PHE A 342 27.544 21.351 -15.698 1.00 35.59 C ANISOU 1320 C PHE A 342 4296 5210 4017 1299 -440 -828 C ATOM 1321 O PHE A 342 26.547 21.143 -16.385 1.00 35.07 O ANISOU 1321 O PHE A 342 4269 5064 3992 1301 -518 -839 O ATOM 1322 CB PHE A 342 29.154 19.430 -15.981 1.00 36.43 C ANISOU 1322 CB PHE A 342 4443 5288 4111 1502 -600 -980 C ATOM 1323 CG PHE A 342 28.853 18.954 -14.583 1.00 46.67 C ANISOU 1323 CG PHE A 342 5715 6490 5527 1399 -634 -890 C ATOM 1324 CD1 PHE A 342 27.576 18.527 -14.240 1.00 36.46 C ANISOU 1324 CD1 PHE A 342 4437 5056 4361 1325 -727 -825 C ATOM 1325 CD2 PHE A 342 29.857 18.900 -13.621 1.00 47.68 C ANISOU 1325 CD2 PHE A 342 5803 6668 5647 1381 -578 -860 C ATOM 1326 CE1 PHE A 342 27.296 18.081 -12.964 1.00 40.05 C ANISOU 1326 CE1 PHE A 342 4861 5431 4924 1242 -754 -731 C ATOM 1327 CE2 PHE A 342 29.586 18.452 -12.340 1.00 47.26 C ANISOU 1327 CE2 PHE A 342 5726 6533 5697 1292 -609 -776 C ATOM 1328 CZ PHE A 342 28.304 18.043 -12.009 1.00 46.44 C ANISOU 1328 CZ PHE A 342 5632 6299 5713 1227 -693 -710 C ATOM 1329 N ILE A 343 27.476 21.932 -14.506 1.00 39.33 N ANISOU 1329 N ILE A 343 4728 5696 4519 1186 -350 -724 N ATOM 1330 CA ILE A 343 26.193 22.377 -13.968 1.00 39.85 C ANISOU 1330 CA ILE A 343 4790 5688 4662 1065 -327 -615 C ATOM 1331 C ILE A 343 25.753 23.655 -14.671 1.00 46.84 C ANISOU 1331 C ILE A 343 5660 6658 5479 1027 -216 -600 C ATOM 1332 O ILE A 343 24.577 23.823 -14.992 1.00 47.70 O ANISOU 1332 O ILE A 343 5785 6696 5641 975 -238 -554 O ATOM 1333 CB ILE A 343 26.260 22.613 -12.462 1.00 32.78 C ANISOU 1333 CB ILE A 343 3865 4785 3807 970 -262 -510 C ATOM 1334 CG1 ILE A 343 26.692 21.334 -11.745 1.00 32.84 C ANISOU 1334 CG1 ILE A 343 3877 4713 3890 1002 -371 -519 C ATOM 1335 CG2 ILE A 343 24.916 23.089 -11.936 1.00 33.51 C ANISOU 1335 CG2 ILE A 343 3956 4806 3972 860 -228 -388 C ATOM 1336 CD1 ILE A 343 26.632 21.458 -10.236 1.00 31.83 C ANISOU 1336 CD1 ILE A 343 3723 4564 3808 912 -321 -408 C ATOM 1337 N VAL A 344 26.711 24.543 -14.923 1.00 36.43 N ANISOU 1337 N VAL A 344 4305 5488 4049 1054 -102 -630 N ATOM 1338 CA VAL A 344 26.439 25.766 -15.677 1.00 39.33 C ANISOU 1338 CA VAL A 344 4643 5952 4349 1030 4 -623 C ATOM 1339 C VAL A 344 25.885 25.441 -17.065 1.00 47.75 C ANISOU 1339 C VAL A 344 5746 6994 5404 1101 -73 -695 C ATOM 1340 O VAL A 344 24.865 25.992 -17.478 1.00 47.68 O ANISOU 1340 O VAL A 344 5739 6961 5418 1039 -50 -655 O ATOM 1341 CB VAL A 344 27.703 26.625 -15.844 1.00 39.04 C ANISOU 1341 CB VAL A 344 4551 6080 4204 1072 115 -647 C ATOM 1342 CG1 VAL A 344 27.459 27.748 -16.842 1.00 40.50 C ANISOU 1342 CG1 VAL A 344 4698 6368 4323 1069 204 -651 C ATOM 1343 CG2 VAL A 344 28.174 27.175 -14.489 1.00 34.96 C ANISOU 1343 CG2 VAL A 344 4002 5587 3693 986 195 -568 C ATOM 1344 N ASP A 345 26.563 24.545 -17.777 1.00 52.01 N ANISOU 1344 N ASP A 345 6319 7535 5906 1235 -165 -801 N ATOM 1345 CA ASP A 345 26.173 24.175 -19.133 1.00 56.15 C ANISOU 1345 CA ASP A 345 6892 8040 6402 1328 -249 -887 C ATOM 1346 C ASP A 345 24.850 23.420 -19.137 1.00 48.77 C ANISOU 1346 C ASP A 345 6015 6926 5588 1279 -387 -861 C ATOM 1347 O ASP A 345 24.050 23.566 -20.056 1.00 48.00 O ANISOU 1347 O ASP A 345 5948 6797 5493 1284 -426 -878 O ATOM 1348 CB ASP A 345 27.268 23.332 -19.801 1.00 70.14 C ANISOU 1348 CB ASP A 345 8696 9851 8101 1498 -317 -1006 C ATOM 1349 CG ASP A 345 28.556 24.119 -20.038 1.00 82.74 C ANISOU 1349 CG ASP A 345 10230 11632 9577 1564 -183 -1020 C ATOM 1350 OD1 ASP A 345 28.474 25.337 -20.313 1.00 82.33 O ANISOU 1350 OD1 ASP A 345 10119 11687 9475 1517 -60 -976 O ATOM 1351 OD2 ASP A 345 29.651 23.518 -19.954 1.00 87.71 O ANISOU 1351 OD2 ASP A 345 10861 12295 10169 1664 -203 -1068 O ATOM 1352 N PHE A 346 24.622 22.612 -18.107 1.00 43.39 N ANISOU 1352 N PHE A 346 5344 6126 5015 1233 -464 -810 N ATOM 1353 CA PHE A 346 23.358 21.900 -17.992 1.00 43.07 C ANISOU 1353 CA PHE A 346 5343 5909 5112 1181 -599 -757 C ATOM 1354 C PHE A 346 22.208 22.900 -17.873 1.00 42.00 C ANISOU 1354 C PHE A 346 5181 5759 5017 1051 -513 -641 C ATOM 1355 O PHE A 346 21.210 22.807 -18.588 1.00 43.13 O ANISOU 1355 O PHE A 346 5358 5818 5211 1035 -588 -629 O ATOM 1356 CB PHE A 346 23.373 20.952 -16.795 1.00 35.62 C ANISOU 1356 CB PHE A 346 4393 4858 4282 1150 -679 -702 C ATOM 1357 CG PHE A 346 22.085 20.194 -16.609 1.00 46.35 C ANISOU 1357 CG PHE A 346 5778 6032 5802 1098 -824 -624 C ATOM 1358 CD1 PHE A 346 21.937 18.911 -17.114 1.00 41.14 C ANISOU 1358 CD1 PHE A 346 5172 5245 5216 1182 -1024 -694 C ATOM 1359 CD2 PHE A 346 21.015 20.770 -15.935 1.00 45.17 C ANISOU 1359 CD2 PHE A 346 5597 5832 5735 970 -763 -473 C ATOM 1360 CE1 PHE A 346 20.749 18.212 -16.945 1.00 48.10 C ANISOU 1360 CE1 PHE A 346 6067 5947 6261 1134 -1172 -608 C ATOM 1361 CE2 PHE A 346 19.831 20.075 -15.762 1.00 48.46 C ANISOU 1361 CE2 PHE A 346 6026 6075 6312 925 -897 -379 C ATOM 1362 CZ PHE A 346 19.697 18.793 -16.266 1.00 46.33 C ANISOU 1362 CZ PHE A 346 5803 5676 6126 1005 -1107 -444 C ATOM 1363 N VAL A 347 22.374 23.867 -16.978 1.00 42.19 N ANISOU 1363 N VAL A 347 5149 5865 5016 961 -357 -556 N ATOM 1364 CA VAL A 347 21.357 24.880 -16.702 1.00 33.00 C ANISOU 1364 CA VAL A 347 3956 4696 3885 836 -255 -437 C ATOM 1365 C VAL A 347 21.145 25.848 -17.872 1.00 38.08 C ANISOU 1365 C VAL A 347 4589 5431 4450 838 -181 -473 C ATOM 1366 O VAL A 347 20.033 26.285 -18.120 1.00 38.88 O ANISOU 1366 O VAL A 347 4689 5478 4605 759 -167 -398 O ATOM 1367 CB VAL A 347 21.706 25.661 -15.417 1.00 36.16 C ANISOU 1367 CB VAL A 347 4310 5164 4266 755 -112 -351 C ATOM 1368 CG1 VAL A 347 20.812 26.879 -15.255 1.00 35.33 C ANISOU 1368 CG1 VAL A 347 4177 5082 4167 642 15 -244 C ATOM 1369 CG2 VAL A 347 21.600 24.740 -14.200 1.00 32.66 C ANISOU 1369 CG2 VAL A 347 3875 4613 3921 734 -184 -284 C ATOM 1370 N ALA A 348 22.210 26.172 -18.597 1.00 38.35 N ANISOU 1370 N ALA A 348 4607 5604 4359 930 -134 -579 N ATOM 1371 CA ALA A 348 22.087 27.015 -19.779 1.00 41.43 C ANISOU 1371 CA ALA A 348 4978 6092 4670 949 -71 -617 C ATOM 1372 C ALA A 348 21.411 26.302 -20.954 1.00 47.70 C ANISOU 1372 C ALA A 348 5840 6796 5489 1013 -213 -681 C ATOM 1373 O ALA A 348 21.041 26.944 -21.928 1.00 46.91 O ANISOU 1373 O ALA A 348 5731 6751 5343 1013 -176 -697 O ATOM 1374 CB ALA A 348 23.447 27.547 -20.207 1.00 38.45 C ANISOU 1374 CB ALA A 348 4556 5894 4160 1042 20 -695 C ATOM 1375 N THR A 349 21.271 24.981 -20.896 1.00 47.37 N ANISOU 1375 N THR A 349 5865 6617 5518 1071 -383 -720 N ATOM 1376 CA THR A 349 20.545 24.295 -21.961 1.00 47.09 C ANISOU 1376 CA THR A 349 5903 6474 5517 1126 -540 -776 C ATOM 1377 C THR A 349 19.114 24.822 -21.958 1.00 48.16 C ANISOU 1377 C THR A 349 6029 6518 5750 989 -529 -654 C ATOM 1378 O THR A 349 18.424 24.737 -20.940 1.00 46.95 O ANISOU 1378 O THR A 349 5857 6267 5716 883 -528 -528 O ATOM 1379 CB THR A 349 20.541 22.777 -21.776 1.00 52.08 C ANISOU 1379 CB THR A 349 6605 6951 6234 1197 -740 -823 C ATOM 1380 OG1 THR A 349 21.867 22.269 -21.968 1.00 55.31 O ANISOU 1380 OG1 THR A 349 7029 7444 6543 1337 -753 -945 O ATOM 1381 CG2 THR A 349 19.609 22.126 -22.782 1.00 48.04 C ANISOU 1381 CG2 THR A 349 6174 6300 5781 1233 -918 -859 C ATOM 1382 N PRO A 350 18.672 25.388 -23.095 1.00 52.01 N ANISOU 1382 N PRO A 350 5788 7682 6289 1526 -1540 -174 N ATOM 1383 CA PRO A 350 17.400 26.120 -23.184 1.00 47.57 C ANISOU 1383 CA PRO A 350 5197 6998 5878 1488 -1532 -48 C ATOM 1384 C PRO A 350 16.228 25.474 -22.437 1.00 49.50 C ANISOU 1384 C PRO A 350 5330 7053 6423 1420 -1672 31 C ATOM 1385 O PRO A 350 15.554 26.163 -21.668 1.00 51.63 O ANISOU 1385 O PRO A 350 5528 7253 6837 1308 -1521 159 O ATOM 1386 CB PRO A 350 17.136 26.164 -24.692 1.00 45.66 C ANISOU 1386 CB PRO A 350 5066 6768 5517 1653 -1696 -96 C ATOM 1387 CG PRO A 350 18.505 26.212 -25.287 1.00 49.62 C ANISOU 1387 CG PRO A 350 5658 7466 5730 1747 -1609 -199 C ATOM 1388 CD PRO A 350 19.391 25.383 -24.384 1.00 46.65 C ANISOU 1388 CD PRO A 350 5229 7133 5362 1691 -1589 -272 C ATOM 1389 N GLU A 351 15.985 24.185 -22.658 1.00 54.35 N ANISOU 1389 N GLU A 351 5925 7585 7140 1494 -1956 -37 N ATOM 1390 CA GLU A 351 14.815 23.538 -22.068 1.00 56.81 C ANISOU 1390 CA GLU A 351 6114 7705 7767 1444 -2117 63 C ATOM 1391 C GLU A 351 14.978 23.322 -20.569 1.00 52.17 C ANISOU 1391 C GLU A 351 5410 7114 7297 1300 -1966 131 C ATOM 1392 O GLU A 351 13.994 23.317 -19.823 1.00 50.81 O ANISOU 1392 O GLU A 351 5124 6812 7368 1224 -1951 275 O ATOM 1393 CB GLU A 351 14.496 22.216 -22.768 1.00 60.48 C ANISOU 1393 CB GLU A 351 6585 8065 8331 1571 -2498 -23 C ATOM 1394 CG GLU A 351 13.331 21.449 -22.142 1.00 68.66 C ANISOU 1394 CG GLU A 351 7468 8891 9728 1520 -2688 99 C ATOM 1395 CD GLU A 351 12.039 22.261 -22.059 1.00 72.28 C ANISOU 1395 CD GLU A 351 7865 9209 10390 1466 -2623 279 C ATOM 1396 OE1 GLU A 351 11.894 23.259 -22.801 1.00 68.94 O ANISOU 1396 OE1 GLU A 351 7535 8819 9840 1499 -2531 284 O ATOM 1397 OE2 GLU A 351 11.160 21.886 -21.251 1.00 72.27 O ANISOU 1397 OE2 GLU A 351 7714 9063 10685 1391 -2665 425 O ATOM 1398 N HIS A 352 16.222 23.149 -20.133 1.00 47.50 N ANISOU 1398 N HIS A 352 4849 6664 6536 1270 -1851 36 N ATOM 1399 CA HIS A 352 16.523 23.051 -18.709 1.00 46.55 C ANISOU 1399 CA HIS A 352 4646 6556 6484 1136 -1689 90 C ATOM 1400 C HIS A 352 16.345 24.404 -18.036 1.00 45.85 C ANISOU 1400 C HIS A 352 4558 6493 6369 1037 -1382 200 C ATOM 1401 O HIS A 352 15.738 24.497 -16.971 1.00 45.10 O ANISOU 1401 O HIS A 352 4376 6325 6433 948 -1284 319 O ATOM 1402 CB HIS A 352 17.943 22.525 -18.478 1.00 46.62 C ANISOU 1402 CB HIS A 352 4696 6697 6322 1130 -1664 -46 C ATOM 1403 CG HIS A 352 18.183 21.168 -19.061 1.00 56.71 C ANISOU 1403 CG HIS A 352 5971 7953 7623 1230 -1965 -168 C ATOM 1404 ND1 HIS A 352 19.439 20.714 -19.405 1.00 58.04 N ANISOU 1404 ND1 HIS A 352 6206 8245 7602 1285 -1991 -320 N ATOM 1405 CD2 HIS A 352 17.322 20.170 -19.376 1.00 58.75 C ANISOU 1405 CD2 HIS A 352 6165 8071 8085 1292 -2265 -159 C ATOM 1406 CE1 HIS A 352 19.344 19.491 -19.894 1.00 59.35 C ANISOU 1406 CE1 HIS A 352 6356 8354 7840 1380 -2293 -412 C ATOM 1407 NE2 HIS A 352 18.071 19.138 -19.889 1.00 66.98 N ANISOU 1407 NE2 HIS A 352 7244 9157 9050 1385 -2474 -318 N ATOM 1408 N LEU A 353 16.867 25.454 -18.664 1.00 42.23 N ANISOU 1408 N LEU A 353 4196 6136 5713 1063 -1235 167 N ATOM 1409 CA LEU A 353 16.739 26.794 -18.103 1.00 38.11 C ANISOU 1409 CA LEU A 353 3680 5634 5167 978 -965 260 C ATOM 1410 C LEU A 353 15.259 27.150 -17.929 1.00 44.37 C ANISOU 1410 C LEU A 353 4400 6280 6181 955 -970 405 C ATOM 1411 O LEU A 353 14.859 27.693 -16.894 1.00 37.16 O ANISOU 1411 O LEU A 353 3435 5329 5354 870 -792 505 O ATOM 1412 CB LEU A 353 17.444 27.829 -18.981 1.00 38.02 C ANISOU 1412 CB LEU A 353 3767 5742 4938 1021 -847 216 C ATOM 1413 CG LEU A 353 17.455 29.265 -18.441 1.00 43.53 C ANISOU 1413 CG LEU A 353 4472 6462 5607 937 -585 300 C ATOM 1414 CD1 LEU A 353 18.434 29.389 -17.286 1.00 39.72 C ANISOU 1414 CD1 LEU A 353 3990 6041 5060 849 -422 275 C ATOM 1415 CD2 LEU A 353 17.785 30.277 -19.526 1.00 40.39 C ANISOU 1415 CD2 LEU A 353 4144 6148 5055 991 -519 296 C ATOM 1416 N ARG A 354 14.447 26.823 -18.935 1.00 41.27 N ANISOU 1416 N ARG A 354 4004 5796 5880 1040 -1181 417 N ATOM 1417 CA ARG A 354 13.008 27.087 -18.879 1.00 40.34 C ANISOU 1417 CA ARG A 354 3806 5517 6003 1024 -1217 563 C ATOM 1418 C ARG A 354 12.338 26.388 -17.689 1.00 42.27 C ANISOU 1418 C ARG A 354 3916 5655 6489 960 -1226 675 C ATOM 1419 O ARG A 354 11.507 26.979 -16.996 1.00 49.68 O ANISOU 1419 O ARG A 354 4784 6519 7573 902 -1078 817 O ATOM 1420 CB ARG A 354 12.323 26.667 -20.188 1.00 42.27 C ANISOU 1420 CB ARG A 354 4077 5664 6318 1135 -1495 544 C ATOM 1421 CG ARG A 354 10.854 27.085 -20.284 1.00 47.30 C ANISOU 1421 CG ARG A 354 4640 6124 7209 1119 -1533 701 C ATOM 1422 CD ARG A 354 10.118 26.315 -21.374 1.00 56.53 C ANISOU 1422 CD ARG A 354 5817 7150 8513 1227 -1878 688 C ATOM 1423 NE ARG A 354 10.059 24.889 -21.067 1.00 63.73 N ANISOU 1423 NE ARG A 354 6653 7985 9578 1254 -2113 668 N ATOM 1424 CZ ARG A 354 9.083 24.313 -20.372 1.00 67.75 C ANISOU 1424 CZ ARG A 354 7009 8329 10405 1211 -2199 815 C ATOM 1425 NH1 ARG A 354 8.069 25.040 -19.920 1.00 72.23 N ANISOU 1425 NH1 ARG A 354 7487 8792 11164 1147 -2059 991 N ATOM 1426 NH2 ARG A 354 9.118 23.009 -20.131 1.00 62.97 N ANISOU 1426 NH2 ARG A 354 6328 7661 9936 1237 -2427 796 N ATOM 1427 N GLN A 355 12.702 25.133 -17.449 1.00 38.57 N ANISOU 1427 N GLN A 355 3408 5182 6064 975 -1396 619 N ATOM 1428 CA GLN A 355 12.101 24.381 -16.351 1.00 47.68 C ANISOU 1428 CA GLN A 355 4423 6241 7454 919 -1420 739 C ATOM 1429 C GLN A 355 12.577 24.896 -15.002 1.00 44.11 C ANISOU 1429 C GLN A 355 3964 5875 6922 822 -1128 779 C ATOM 1430 O GLN A 355 11.802 25.019 -14.059 1.00 47.38 O ANISOU 1430 O GLN A 355 4284 6218 7501 775 -1012 932 O ATOM 1431 CB GLN A 355 12.433 22.893 -16.459 1.00 52.46 C ANISOU 1431 CB GLN A 355 4982 6821 8129 957 -1695 664 C ATOM 1432 CG GLN A 355 11.697 22.153 -17.564 1.00 55.73 C ANISOU 1432 CG GLN A 355 5374 7097 8707 1061 -2038 655 C ATOM 1433 CD GLN A 355 11.965 20.655 -17.517 1.00 58.15 C ANISOU 1433 CD GLN A 355 5615 7361 9119 1095 -2321 591 C ATOM 1434 OE1 GLN A 355 12.468 20.067 -18.478 1.00 61.55 O ANISOU 1434 OE1 GLN A 355 6127 7814 9447 1195 -2548 434 O ATOM 1435 NE2 GLN A 355 11.639 20.033 -16.388 1.00 51.04 N ANISOU 1435 NE2 GLN A 355 4569 6403 8422 1019 -2307 715 N ATOM 1436 N ILE A 356 13.863 25.198 -14.916 1.00 35.88 N ANISOU 1436 N ILE A 356 3025 4980 5627 801 -1013 645 N ATOM 1437 CA ILE A 356 14.459 25.554 -13.640 1.00 39.18 C ANISOU 1437 CA ILE A 356 3455 5470 5959 717 -781 659 C ATOM 1438 C ILE A 356 14.063 26.965 -13.239 1.00 38.72 C ANISOU 1438 C ILE A 356 3429 5413 5867 684 -524 741 C ATOM 1439 O ILE A 356 13.708 27.220 -12.086 1.00 45.01 O ANISOU 1439 O ILE A 356 4188 6187 6726 637 -359 839 O ATOM 1440 CB ILE A 356 15.987 25.400 -13.694 1.00 32.08 C ANISOU 1440 CB ILE A 356 2652 4709 4829 705 -763 495 C ATOM 1441 CG1 ILE A 356 16.349 23.908 -13.744 1.00 37.75 C ANISOU 1441 CG1 ILE A 356 3319 5417 5608 723 -1000 424 C ATOM 1442 CG2 ILE A 356 16.645 26.112 -12.516 1.00 30.28 C ANISOU 1442 CG2 ILE A 356 2471 4546 4488 623 -511 501 C ATOM 1443 CD1 ILE A 356 17.765 23.630 -14.228 1.00 32.99 C ANISOU 1443 CD1 ILE A 356 2805 4935 4795 746 -1043 250 C ATOM 1444 N CYS A 357 14.108 27.874 -14.202 1.00 42.24 N ANISOU 1444 N CYS A 357 3947 5887 6216 717 -495 703 N ATOM 1445 CA CYS A 357 13.732 29.265 -13.960 1.00 46.05 C ANISOU 1445 CA CYS A 357 4458 6365 6675 690 -275 772 C ATOM 1446 C CYS A 357 12.240 29.504 -13.815 1.00 43.96 C ANISOU 1446 C CYS A 357 4099 5962 6642 696 -259 933 C ATOM 1447 O CYS A 357 11.827 30.588 -13.419 1.00 39.78 O ANISOU 1447 O CYS A 357 3578 5417 6120 673 -69 1002 O ATOM 1448 CB CYS A 357 14.288 30.165 -15.052 1.00 42.84 C ANISOU 1448 CB CYS A 357 4145 6034 6099 719 -255 693 C ATOM 1449 SG CYS A 357 16.035 30.470 -14.812 1.00 42.89 S ANISOU 1449 SG CYS A 357 4252 6198 5845 689 -143 558 S ATOM 1450 N SER A 358 11.425 28.504 -14.135 1.00 46.75 N ANISOU 1450 N SER A 358 4357 6207 7200 731 -467 999 N ATOM 1451 CA SER A 358 10.000 28.640 -13.887 1.00 44.14 C ANISOU 1451 CA SER A 358 3913 5730 7127 734 -450 1178 C ATOM 1452 C SER A 358 9.693 28.141 -12.480 1.00 39.72 C ANISOU 1452 C SER A 358 3260 5147 6686 700 -341 1294 C ATOM 1453 O SER A 358 8.541 28.158 -12.046 1.00 41.97 O ANISOU 1453 O SER A 358 3432 5319 7197 706 -296 1470 O ATOM 1454 CB SER A 358 9.174 27.873 -14.925 1.00 51.04 C ANISOU 1454 CB SER A 358 4721 6470 8204 792 -741 1219 C ATOM 1455 OG SER A 358 9.115 26.493 -14.604 1.00 57.93 O ANISOU 1455 OG SER A 358 5502 7293 9217 803 -929 1242 O ATOM 1456 N ASP A 359 10.729 27.703 -11.771 1.00 43.78 N ANISOU 1456 N ASP A 359 3820 5768 7048 668 -295 1206 N ATOM 1457 CA ASP A 359 10.568 27.159 -10.420 1.00 37.24 C ANISOU 1457 CA ASP A 359 2916 4933 6299 640 -198 1308 C ATOM 1458 C ASP A 359 11.064 28.101 -9.326 1.00 38.67 C ANISOU 1458 C ASP A 359 3188 5203 6304 608 89 1292 C ATOM 1459 O ASP A 359 12.069 28.800 -9.471 1.00 42.98 O ANISOU 1459 O ASP A 359 3863 5844 6624 588 167 1152 O ATOM 1460 CB ASP A 359 11.279 25.808 -10.280 1.00 31.73 C ANISOU 1460 CB ASP A 359 2188 4268 5597 626 -384 1236 C ATOM 1461 CG ASP A 359 10.975 25.129 -8.949 1.00 38.42 C ANISOU 1461 CG ASP A 359 2935 5098 6563 600 -312 1371 C ATOM 1462 OD1 ASP A 359 9.857 24.590 -8.784 1.00 43.56 O ANISOU 1462 OD1 ASP A 359 3434 5634 7482 622 -382 1552 O ATOM 1463 OD2 ASP A 359 11.857 25.133 -8.067 1.00 42.07 O ANISOU 1463 OD2 ASP A 359 3469 5657 6859 560 -190 1306 O ATOM 1464 N LYS A 360 10.334 28.085 -8.225 1.00 41.71 N ANISOU 1464 N LYS A 360 3500 5547 6801 613 236 1448 N ATOM 1465 CA LYS A 360 10.613 28.895 -7.054 1.00 44.09 C ANISOU 1465 CA LYS A 360 3885 5912 6956 607 500 1454 C ATOM 1466 C LYS A 360 12.020 28.674 -6.499 1.00 40.63 C ANISOU 1466 C LYS A 360 3563 5585 6290 564 516 1302 C ATOM 1467 O LYS A 360 12.749 29.628 -6.229 1.00 44.41 O ANISOU 1467 O LYS A 360 4175 6126 6573 552 652 1201 O ATOM 1468 CB LYS A 360 9.557 28.566 -5.995 1.00 51.95 C ANISOU 1468 CB LYS A 360 4761 6847 8129 639 620 1665 C ATOM 1469 CG LYS A 360 9.861 29.031 -4.600 1.00 53.34 C ANISOU 1469 CG LYS A 360 5023 7093 8151 652 863 1680 C ATOM 1470 CD LYS A 360 8.612 28.909 -3.754 1.00 50.81 C ANISOU 1470 CD LYS A 360 4578 6710 8018 710 1009 1916 C ATOM 1471 CE LYS A 360 7.500 29.794 -4.308 1.00 49.27 C ANISOU 1471 CE LYS A 360 4327 6423 7969 752 1083 2016 C ATOM 1472 NZ LYS A 360 6.374 29.887 -3.338 1.00 50.97 N ANISOU 1472 NZ LYS A 360 4442 6594 8331 823 1285 2244 N ATOM 1473 N TYR A 361 12.407 27.414 -6.331 1.00 32.97 N ANISOU 1473 N TYR A 361 2537 4627 5362 540 362 1288 N ATOM 1474 CA TYR A 361 13.717 27.110 -5.769 1.00 35.23 C ANISOU 1474 CA TYR A 361 2922 5005 5460 493 365 1154 C ATOM 1475 C TYR A 361 14.772 27.032 -6.860 1.00 36.04 C ANISOU 1475 C TYR A 361 3094 5160 5440 472 212 972 C ATOM 1476 O TYR A 361 15.941 27.371 -6.642 1.00 31.76 O ANISOU 1476 O TYR A 361 2668 4692 4707 438 263 843 O ATOM 1477 CB TYR A 361 13.654 25.837 -4.915 1.00 39.21 C ANISOU 1477 CB TYR A 361 3332 5502 6067 473 294 1236 C ATOM 1478 CG TYR A 361 12.598 25.960 -3.841 1.00 37.28 C ANISOU 1478 CG TYR A 361 3014 5216 5933 511 471 1439 C ATOM 1479 CD1 TYR A 361 12.785 26.807 -2.750 1.00 37.91 C ANISOU 1479 CD1 TYR A 361 3209 5343 5851 528 715 1445 C ATOM 1480 CD2 TYR A 361 11.392 25.274 -3.942 1.00 41.14 C ANISOU 1480 CD2 TYR A 361 3320 5614 6696 542 393 1632 C ATOM 1481 CE1 TYR A 361 11.803 26.948 -1.774 1.00 42.03 C ANISOU 1481 CE1 TYR A 361 3673 5839 6457 586 896 1634 C ATOM 1482 CE2 TYR A 361 10.408 25.409 -2.979 1.00 45.31 C ANISOU 1482 CE2 TYR A 361 3771 6111 7335 589 576 1840 C ATOM 1483 CZ TYR A 361 10.618 26.245 -1.897 1.00 50.60 C ANISOU 1483 CZ TYR A 361 4564 6845 7816 616 837 1839 C ATOM 1484 OH TYR A 361 9.636 26.374 -0.943 1.00 56.60 O ANISOU 1484 OH TYR A 361 5252 7584 8669 683 1032 2049 O ATOM 1485 N GLY A 362 14.352 26.606 -8.044 1.00 30.00 N ANISOU 1485 N GLY A 362 2260 4351 4788 502 24 969 N ATOM 1486 CA GLY A 362 15.254 26.553 -9.178 1.00 29.08 C ANISOU 1486 CA GLY A 362 2211 4290 4547 510 -112 809 C ATOM 1487 C GLY A 362 15.859 27.917 -9.465 1.00 34.90 C ANISOU 1487 C GLY A 362 3073 5090 5098 506 46 731 C ATOM 1488 O GLY A 362 17.040 28.018 -9.799 1.00 36.43 O ANISOU 1488 O GLY A 362 3349 5365 5129 491 27 600 O ATOM 1489 N CYS A 363 15.049 28.966 -9.327 1.00 30.44 N ANISOU 1489 N CYS A 363 2510 4482 4572 520 197 821 N ATOM 1490 CA CYS A 363 15.520 30.339 -9.519 1.00 31.33 C ANISOU 1490 CA CYS A 363 2726 4639 4538 515 344 766 C ATOM 1491 C CYS A 363 16.627 30.707 -8.538 1.00 33.24 C ANISOU 1491 C CYS A 363 3070 4944 4618 472 468 690 C ATOM 1492 O CYS A 363 17.605 31.361 -8.911 1.00 33.68 O ANISOU 1492 O CYS A 363 3209 5057 4533 457 494 595 O ATOM 1493 CB CYS A 363 14.355 31.340 -9.415 1.00 30.49 C ANISOU 1493 CB CYS A 363 2592 4461 4530 539 479 884 C ATOM 1494 SG CYS A 363 13.368 31.411 -10.930 1.00 40.38 S ANISOU 1494 SG CYS A 363 3774 5644 5924 582 333 935 S ATOM 1495 N ARG A 364 16.478 30.285 -7.287 1.00 32.15 N ANISOU 1495 N ARG A 364 2924 4787 4505 456 538 741 N ATOM 1496 CA ARG A 364 17.511 30.533 -6.277 1.00 28.00 C ANISOU 1496 CA ARG A 364 2506 4303 3830 419 631 667 C ATOM 1497 C ARG A 364 18.847 29.935 -6.699 1.00 28.94 C ANISOU 1497 C ARG A 364 2661 4484 3852 379 502 535 C ATOM 1498 O ARG A 364 19.910 30.521 -6.471 1.00 32.19 O ANISOU 1498 O ARG A 364 3170 4928 4131 350 554 449 O ATOM 1499 CB ARG A 364 17.070 29.986 -4.922 1.00 29.87 C ANISOU 1499 CB ARG A 364 2724 4515 4111 420 705 754 C ATOM 1500 CG ARG A 364 15.706 30.524 -4.488 1.00 37.76 C ANISOU 1500 CG ARG A 364 3674 5456 5215 476 848 902 C ATOM 1501 CD ARG A 364 15.705 32.043 -4.527 1.00 40.66 C ANISOU 1501 CD ARG A 364 4138 5817 5495 500 994 871 C ATOM 1502 NE ARG A 364 16.694 32.609 -3.608 1.00 42.19 N ANISOU 1502 NE ARG A 364 4477 6037 5514 486 1083 779 N ATOM 1503 CZ ARG A 364 17.293 33.783 -3.784 1.00 44.16 C ANISOU 1503 CZ ARG A 364 4828 6290 5661 484 1134 696 C ATOM 1504 NH1 ARG A 364 17.021 34.512 -4.860 1.00 40.28 N ANISOU 1504 NH1 ARG A 364 4303 5791 5212 489 1119 697 N ATOM 1505 NH2 ARG A 364 18.175 34.228 -2.893 1.00 40.65 N ANISOU 1505 NH2 ARG A 364 4515 5848 5080 476 1187 618 N ATOM 1506 N VAL A 365 18.793 28.770 -7.336 1.00 32.57 N ANISOU 1506 N VAL A 365 3037 4951 4389 383 325 522 N ATOM 1507 CA VAL A 365 20.013 28.120 -7.791 1.00 32.05 C ANISOU 1507 CA VAL A 365 2996 4944 4239 358 199 397 C ATOM 1508 C VAL A 365 20.669 28.949 -8.903 1.00 34.94 C ANISOU 1508 C VAL A 365 3417 5362 4497 381 207 323 C ATOM 1509 O VAL A 365 21.873 29.190 -8.889 1.00 31.73 O ANISOU 1509 O VAL A 365 3076 5004 3974 353 226 238 O ATOM 1510 CB VAL A 365 19.764 26.656 -8.247 1.00 33.20 C ANISOU 1510 CB VAL A 365 3038 5079 4498 372 -13 391 C ATOM 1511 CG1 VAL A 365 20.975 26.111 -9.002 1.00 27.94 C ANISOU 1511 CG1 VAL A 365 2401 4480 3737 371 -144 251 C ATOM 1512 CG2 VAL A 365 19.437 25.764 -7.053 1.00 36.35 C ANISOU 1512 CG2 VAL A 365 3377 5440 4994 334 -26 463 C ATOM 1513 N VAL A 366 19.870 29.410 -9.851 1.00 35.72 N ANISOU 1513 N VAL A 366 3483 5446 4642 432 193 368 N ATOM 1514 CA VAL A 366 20.409 30.209 -10.938 1.00 33.10 C ANISOU 1514 CA VAL A 366 3196 5170 4210 462 205 320 C ATOM 1515 C VAL A 366 20.937 31.540 -10.431 1.00 34.81 C ANISOU 1515 C VAL A 366 3489 5394 4342 429 377 323 C ATOM 1516 O VAL A 366 22.010 31.984 -10.839 1.00 30.22 O ANISOU 1516 O VAL A 366 2953 4871 3658 422 394 266 O ATOM 1517 CB VAL A 366 19.376 30.428 -12.035 1.00 34.35 C ANISOU 1517 CB VAL A 366 3310 5302 4441 524 145 375 C ATOM 1518 CG1 VAL A 366 19.898 31.426 -13.061 1.00 31.44 C ANISOU 1518 CG1 VAL A 366 2990 4996 3960 553 189 348 C ATOM 1519 CG2 VAL A 366 19.053 29.096 -12.700 1.00 30.14 C ANISOU 1519 CG2 VAL A 366 2715 4755 3983 571 -69 350 C ATOM 1520 N GLN A 367 20.196 32.163 -9.519 1.00 30.89 N ANISOU 1520 N GLN A 367 3003 4835 3897 415 500 395 N ATOM 1521 CA GLN A 367 20.657 33.398 -8.891 1.00 33.35 C ANISOU 1521 CA GLN A 367 3397 5136 4140 392 642 389 C ATOM 1522 C GLN A 367 22.043 33.250 -8.248 1.00 33.50 C ANISOU 1522 C GLN A 367 3487 5179 4062 345 639 305 C ATOM 1523 O GLN A 367 22.921 34.087 -8.452 1.00 33.28 O ANISOU 1523 O GLN A 367 3508 5168 3970 331 674 272 O ATOM 1524 CB GLN A 367 19.651 33.882 -7.844 1.00 36.48 C ANISOU 1524 CB GLN A 367 3803 5461 4596 402 767 467 C ATOM 1525 CG GLN A 367 20.119 35.116 -7.073 1.00 32.53 C ANISOU 1525 CG GLN A 367 3404 4935 4022 392 893 445 C ATOM 1526 CD GLN A 367 20.219 36.336 -7.959 1.00 40.02 C ANISOU 1526 CD GLN A 367 4354 5889 4961 402 922 450 C ATOM 1527 OE1 GLN A 367 21.012 37.244 -7.710 1.00 55.82 O ANISOU 1527 OE1 GLN A 367 6424 7881 6905 386 962 413 O ATOM 1528 NE2 GLN A 367 19.416 36.362 -9.005 1.00 28.74 N ANISOU 1528 NE2 GLN A 367 2849 4467 3603 428 887 503 N ATOM 1529 N THR A 368 22.244 32.195 -7.465 1.00 35.50 N ANISOU 1529 N THR A 368 3739 5426 4323 317 589 280 N ATOM 1530 CA THR A 368 23.512 32.051 -6.749 1.00 24.63 C ANISOU 1530 CA THR A 368 2436 4053 2870 266 581 205 C ATOM 1531 C THR A 368 24.671 31.782 -7.717 1.00 28.54 C ANISOU 1531 C THR A 368 2917 4612 3316 256 491 135 C ATOM 1532 O THR A 368 25.788 32.287 -7.532 1.00 30.90 O ANISOU 1532 O THR A 368 3271 4908 3560 225 513 94 O ATOM 1533 CB THR A 368 23.450 30.975 -5.632 1.00 42.38 C ANISOU 1533 CB THR A 368 4685 6277 5139 234 547 203 C ATOM 1534 OG1 THR A 368 24.751 30.811 -5.059 1.00 42.42 O ANISOU 1534 OG1 THR A 368 4763 6280 5076 179 517 124 O ATOM 1535 CG2 THR A 368 23.012 29.646 -6.185 1.00 46.63 C ANISOU 1535 CG2 THR A 368 5117 6843 5759 243 413 212 C ATOM 1536 N ILE A 369 24.399 30.994 -8.754 1.00 29.97 N ANISOU 1536 N ILE A 369 3022 4843 3522 294 387 126 N ATOM 1537 CA ILE A 369 25.366 30.767 -9.821 1.00 29.98 C ANISOU 1537 CA ILE A 369 3009 4918 3462 317 316 67 C ATOM 1538 C ILE A 369 25.754 32.077 -10.496 1.00 32.40 C ANISOU 1538 C ILE A 369 3340 5252 3718 338 405 97 C ATOM 1539 O ILE A 369 26.936 32.352 -10.700 1.00 30.43 O ANISOU 1539 O ILE A 369 3109 5035 3417 325 417 69 O ATOM 1540 CB ILE A 369 24.808 29.800 -10.885 1.00 32.95 C ANISOU 1540 CB ILE A 369 3316 5336 3867 382 181 51 C ATOM 1541 CG1 ILE A 369 24.770 28.372 -10.332 1.00 31.90 C ANISOU 1541 CG1 ILE A 369 3144 5183 3793 357 56 11 C ATOM 1542 CG2 ILE A 369 25.663 29.840 -12.152 1.00 29.81 C ANISOU 1542 CG2 ILE A 369 2919 5029 3378 440 141 4 C ATOM 1543 CD1 ILE A 369 24.008 27.412 -11.209 1.00 29.95 C ANISOU 1543 CD1 ILE A 369 2826 4942 3610 424 -104 4 C ATOM 1544 N ILE A 370 24.761 32.897 -10.835 1.00 35.95 N ANISOU 1544 N ILE A 370 3778 5682 4200 369 465 165 N ATOM 1545 CA ILE A 370 25.046 34.177 -11.489 1.00 30.91 C ANISOU 1545 CA ILE A 370 3149 5067 3530 387 542 207 C ATOM 1546 C ILE A 370 26.011 35.017 -10.650 1.00 33.78 C ANISOU 1546 C ILE A 370 3569 5387 3878 332 615 203 C ATOM 1547 O ILE A 370 26.977 35.568 -11.176 1.00 30.80 O ANISOU 1547 O ILE A 370 3186 5047 3471 334 630 214 O ATOM 1548 CB ILE A 370 23.761 34.966 -11.793 1.00 32.34 C ANISOU 1548 CB ILE A 370 3309 5212 3766 415 595 283 C ATOM 1549 CG1 ILE A 370 23.056 34.347 -13.001 1.00 31.91 C ANISOU 1549 CG1 ILE A 370 3202 5200 3721 480 500 293 C ATOM 1550 CG2 ILE A 370 24.084 36.424 -12.095 1.00 33.77 C ANISOU 1550 CG2 ILE A 370 3503 5392 3935 411 684 332 C ATOM 1551 CD1 ILE A 370 21.611 34.777 -13.153 1.00 31.09 C ANISOU 1551 CD1 ILE A 370 3069 5035 3710 500 522 367 C ATOM 1552 N GLU A 371 25.768 35.072 -9.342 1.00 27.51 N ANISOU 1552 N GLU A 371 2829 4513 3110 292 652 192 N ATOM 1553 CA GLU A 371 26.580 35.891 -8.453 1.00 32.16 C ANISOU 1553 CA GLU A 371 3491 5035 3691 251 698 179 C ATOM 1554 C GLU A 371 27.992 35.352 -8.339 1.00 36.48 C ANISOU 1554 C GLU A 371 4052 5595 4213 211 635 126 C ATOM 1555 O GLU A 371 28.942 36.120 -8.299 1.00 36.60 O ANISOU 1555 O GLU A 371 4088 5580 4237 191 646 137 O ATOM 1556 CB GLU A 371 25.946 35.977 -7.067 1.00 25.60 C ANISOU 1556 CB GLU A 371 2735 4121 2872 239 747 173 C ATOM 1557 CG GLU A 371 24.571 36.579 -7.073 1.00 32.41 C ANISOU 1557 CG GLU A 371 3582 4958 3773 282 825 234 C ATOM 1558 CD GLU A 371 23.933 36.570 -5.697 1.00 43.47 C ANISOU 1558 CD GLU A 371 5055 6291 5170 291 890 236 C ATOM 1559 OE1 GLU A 371 22.759 36.963 -5.595 1.00 48.55 O ANISOU 1559 OE1 GLU A 371 5681 6912 5854 333 965 294 O ATOM 1560 OE2 GLU A 371 24.598 36.166 -4.723 1.00 53.27 O ANISOU 1560 OE2 GLU A 371 6371 7501 6368 263 868 186 O ATOM 1561 N LYS A 372 28.124 34.030 -8.275 1.00 35.58 N ANISOU 1561 N LYS A 372 3918 5517 4086 200 560 75 N ATOM 1562 CA LYS A 372 29.438 33.407 -8.233 1.00 33.21 C ANISOU 1562 CA LYS A 372 3617 5229 3770 163 494 22 C ATOM 1563 C LYS A 372 30.205 33.706 -9.524 1.00 34.29 C ANISOU 1563 C LYS A 372 3694 5446 3887 202 495 47 C ATOM 1564 O LYS A 372 31.414 33.895 -9.496 1.00 35.17 O ANISOU 1564 O LYS A 372 3808 5545 4009 175 487 46 O ATOM 1565 CB LYS A 372 29.327 31.891 -8.019 1.00 33.20 C ANISOU 1565 CB LYS A 372 3591 5254 3770 148 401 -38 C ATOM 1566 CG LYS A 372 30.677 31.157 -7.969 1.00 37.44 C ANISOU 1566 CG LYS A 372 4123 5802 4302 108 327 -100 C ATOM 1567 CD LYS A 372 31.615 31.746 -6.906 1.00 36.47 C ANISOU 1567 CD LYS A 372 4080 5579 4198 38 346 -108 C ATOM 1568 CE LYS A 372 30.946 31.791 -5.529 1.00 41.25 C ANISOU 1568 CE LYS A 372 4770 6099 4804 5 366 -114 C ATOM 1569 NZ LYS A 372 31.894 32.217 -4.463 1.00 38.54 N ANISOU 1569 NZ LYS A 372 4525 5648 4471 -54 351 -139 N ATOM 1570 N LEU A 373 29.493 33.766 -10.645 1.00 36.25 N ANISOU 1570 N LEU A 373 3890 5773 4110 272 504 81 N ATOM 1571 CA LEU A 373 30.122 33.987 -11.950 1.00 34.99 C ANISOU 1571 CA LEU A 373 3678 5710 3908 332 512 115 C ATOM 1572 C LEU A 373 30.376 35.459 -12.279 1.00 34.37 C ANISOU 1572 C LEU A 373 3588 5620 3851 337 600 209 C ATOM 1573 O LEU A 373 30.843 35.776 -13.369 1.00 36.04 O ANISOU 1573 O LEU A 373 3749 5917 4028 393 625 264 O ATOM 1574 CB LEU A 373 29.298 33.345 -13.071 1.00 30.48 C ANISOU 1574 CB LEU A 373 3068 5226 3287 418 462 104 C ATOM 1575 CG LEU A 373 29.200 31.817 -13.063 1.00 34.20 C ANISOU 1575 CG LEU A 373 3528 5721 3745 434 342 14 C ATOM 1576 CD1 LEU A 373 28.419 31.326 -14.282 1.00 32.30 C ANISOU 1576 CD1 LEU A 373 3259 5551 3461 537 270 5 C ATOM 1577 CD2 LEU A 373 30.579 31.176 -13.020 1.00 32.22 C ANISOU 1577 CD2 LEU A 373 3271 5503 3469 421 307 -41 C ATOM 1578 N THR A 374 30.074 36.350 -11.340 1.00 34.00 N ANISOU 1578 N THR A 374 3588 5470 3862 286 641 231 N ATOM 1579 CA THR A 374 30.242 37.782 -11.563 1.00 28.15 C ANISOU 1579 CA THR A 374 2831 4698 3166 287 702 319 C ATOM 1580 C THR A 374 31.632 38.230 -11.122 1.00 37.29 C ANISOU 1580 C THR A 374 3993 5795 4381 242 691 342 C ATOM 1581 O THR A 374 32.109 37.836 -10.062 1.00 34.55 O ANISOU 1581 O THR A 374 3707 5364 4055 188 647 280 O ATOM 1582 CB THR A 374 29.173 38.599 -10.791 1.00 31.43 C ANISOU 1582 CB THR A 374 3297 5021 3625 270 742 328 C ATOM 1583 OG1 THR A 374 27.869 38.168 -11.189 1.00 33.00 O ANISOU 1583 OG1 THR A 374 3478 5260 3799 308 749 323 O ATOM 1584 CG2 THR A 374 29.305 40.086 -11.076 1.00 30.92 C ANISOU 1584 CG2 THR A 374 3207 4921 3622 272 785 416 C ATOM 1585 N ALA A 375 32.278 39.056 -11.936 1.00 39.33 N ANISOU 1585 N ALA A 375 4181 6088 4673 265 723 442 N ATOM 1586 CA ALA A 375 33.594 39.574 -11.590 1.00 35.13 C ANISOU 1586 CA ALA A 375 3632 5483 4233 226 704 493 C ATOM 1587 C ALA A 375 33.445 40.744 -10.630 1.00 36.66 C ANISOU 1587 C ALA A 375 3881 5526 4523 182 687 510 C ATOM 1588 O ALA A 375 33.677 41.905 -10.992 1.00 39.07 O ANISOU 1588 O ALA A 375 4131 5802 4914 188 702 614 O ATOM 1589 CB ALA A 375 34.352 39.993 -12.847 1.00 31.41 C ANISOU 1589 CB ALA A 375 3048 5111 3777 277 749 620 C ATOM 1590 N ASP A 376 33.039 40.439 -9.404 1.00 31.00 N ANISOU 1590 N ASP A 376 3274 4714 3792 146 652 410 N ATOM 1591 CA ASP A 376 32.878 41.478 -8.406 1.00 33.35 C ANISOU 1591 CA ASP A 376 3650 4864 4159 125 627 404 C ATOM 1592 C ASP A 376 34.017 41.469 -7.405 1.00 37.13 C ANISOU 1592 C ASP A 376 4195 5205 4706 73 537 371 C ATOM 1593 O ASP A 376 34.974 40.703 -7.542 1.00 39.63 O ANISOU 1593 O ASP A 376 4481 5542 5033 46 503 367 O ATOM 1594 CB ASP A 376 31.514 41.380 -7.709 1.00 46.26 C ANISOU 1594 CB ASP A 376 5371 6479 5726 143 663 331 C ATOM 1595 CG ASP A 376 31.225 39.994 -7.144 1.00 45.25 C ANISOU 1595 CG ASP A 376 5297 6384 5512 130 654 239 C ATOM 1596 OD1 ASP A 376 32.167 39.259 -6.768 1.00 45.12 O ANISOU 1596 OD1 ASP A 376 5302 6347 5496 91 594 198 O ATOM 1597 OD2 ASP A 376 30.029 39.652 -7.058 1.00 48.55 O ANISOU 1597 OD2 ASP A 376 5728 6840 5877 159 701 217 O ATOM 1598 N SER A 377 33.914 42.332 -6.402 1.00 41.30 N ANISOU 1598 N SER A 377 4822 5585 5285 67 490 344 N ATOM 1599 CA SER A 377 34.977 42.498 -5.428 1.00 47.10 C ANISOU 1599 CA SER A 377 5636 6160 6101 26 377 316 C ATOM 1600 C SER A 377 35.228 41.184 -4.693 1.00 45.47 C ANISOU 1600 C SER A 377 5509 5953 5815 -11 347 214 C ATOM 1601 O SER A 377 36.294 40.972 -4.110 1.00 46.32 O ANISOU 1601 O SER A 377 5658 5953 5987 -57 251 195 O ATOM 1602 CB SER A 377 34.622 43.612 -4.440 1.00 44.31 C ANISOU 1602 CB SER A 377 5402 5648 5787 50 322 281 C ATOM 1603 OG SER A 377 33.561 43.203 -3.603 1.00 60.99 O ANISOU 1603 OG SER A 377 7637 7769 7767 81 370 179 O ATOM 1604 N MET A 378 34.244 40.295 -4.748 1.00 40.41 N ANISOU 1604 N MET A 378 4878 5425 5049 8 419 159 N ATOM 1605 CA MET A 378 34.342 39.002 -4.087 1.00 43.29 C ANISOU 1605 CA MET A 378 5302 5802 5343 -26 391 73 C ATOM 1606 C MET A 378 35.184 37.971 -4.854 1.00 41.53 C ANISOU 1606 C MET A 378 4977 5669 5134 -59 369 83 C ATOM 1607 O MET A 378 35.493 36.910 -4.317 1.00 38.63 O ANISOU 1607 O MET A 378 4647 5295 4737 -100 322 15 O ATOM 1608 CB MET A 378 32.942 38.442 -3.808 1.00 52.69 C ANISOU 1608 CB MET A 378 6529 7068 6423 10 465 28 C ATOM 1609 CG MET A 378 32.916 37.454 -2.663 1.00 65.05 C ANISOU 1609 CG MET A 378 8195 8596 7926 -19 427 -53 C ATOM 1610 SD MET A 378 33.764 38.116 -1.209 1.00103.48 S ANISOU 1610 SD MET A 378 13237 13261 12820 -41 327 -105 S ATOM 1611 CE MET A 378 34.606 36.648 -0.617 1.00 57.86 C ANISOU 1611 CE MET A 378 7486 7471 7026 -120 240 -170 C ATOM 1612 N ASN A 379 35.556 38.282 -6.096 1.00 34.76 N ANISOU 1612 N ASN A 379 3993 4895 4319 -35 406 171 N ATOM 1613 CA ASN A 379 36.319 37.342 -6.925 1.00 32.16 C ANISOU 1613 CA ASN A 379 3566 4665 3987 -40 401 182 C ATOM 1614 C ASN A 379 37.731 37.822 -7.265 1.00 38.12 C ANISOU 1614 C ASN A 379 4251 5364 4869 -60 368 272 C ATOM 1615 O ASN A 379 38.406 37.242 -8.116 1.00 39.07 O ANISOU 1615 O ASN A 379 4274 5578 4994 -43 388 307 O ATOM 1616 CB ASN A 379 35.550 36.999 -8.210 1.00 31.93 C ANISOU 1616 CB ASN A 379 3446 4813 3874 30 478 209 C ATOM 1617 CG ASN A 379 34.540 35.875 -7.999 1.00 39.13 C ANISOU 1617 CG ASN A 379 4391 5789 4688 40 472 117 C ATOM 1618 OD1 ASN A 379 33.464 35.869 -8.597 1.00 36.75 O ANISOU 1618 OD1 ASN A 379 4063 5570 4331 92 519 127 O ATOM 1619 ND2 ASN A 379 34.885 34.924 -7.135 1.00 28.96 N ANISOU 1619 ND2 ASN A 379 3155 4453 3395 -14 405 36 N ATOM 1620 N VAL A 380 38.180 38.873 -6.588 1.00 36.39 N ANISOU 1620 N VAL A 380 4078 4985 4762 -89 312 311 N ATOM 1621 CA VAL A 380 39.477 39.466 -6.895 1.00 37.33 C ANISOU 1621 CA VAL A 380 4114 5027 5043 -108 271 425 C ATOM 1622 C VAL A 380 40.628 38.541 -6.509 1.00 37.60 C ANISOU 1622 C VAL A 380 4148 5002 5135 -166 198 393 C ATOM 1623 O VAL A 380 41.777 38.772 -6.891 1.00 36.82 O ANISOU 1623 O VAL A 380 3954 4859 5177 -179 175 497 O ATOM 1624 CB VAL A 380 39.674 40.823 -6.186 1.00 36.72 C ANISOU 1624 CB VAL A 380 4092 4762 5099 -123 190 471 C ATOM 1625 CG1 VAL A 380 38.785 41.883 -6.802 1.00 30.69 C ANISOU 1625 CG1 VAL A 380 3282 4054 4324 -67 260 540 C ATOM 1626 CG2 VAL A 380 39.421 40.677 -4.687 1.00 33.45 C ANISOU 1626 CG2 VAL A 380 3862 4198 4648 -159 95 338 C ATOM 1627 N ASP A 381 40.324 37.504 -5.740 1.00 31.91 N ANISOU 1627 N ASP A 381 3525 4277 4322 -202 160 260 N ATOM 1628 CA ASP A 381 41.348 36.547 -5.345 1.00 36.57 C ANISOU 1628 CA ASP A 381 4117 4812 4967 -265 83 218 C ATOM 1629 C ASP A 381 41.639 35.518 -6.450 1.00 40.11 C ANISOU 1629 C ASP A 381 4440 5434 5365 -232 147 227 C ATOM 1630 O ASP A 381 42.576 34.732 -6.331 1.00 33.84 O ANISOU 1630 O ASP A 381 3617 4609 4631 -276 95 207 O ATOM 1631 CB ASP A 381 40.945 35.828 -4.054 1.00 29.97 C ANISOU 1631 CB ASP A 381 3432 3900 4057 -319 8 80 C ATOM 1632 CG ASP A 381 39.690 35.011 -4.219 1.00 38.36 C ANISOU 1632 CG ASP A 381 4507 5115 4953 -283 77 2 C ATOM 1633 OD1 ASP A 381 38.630 35.604 -4.494 1.00 40.27 O ANISOU 1633 OD1 ASP A 381 4756 5418 5126 -226 153 20 O ATOM 1634 OD2 ASP A 381 39.762 33.780 -4.077 1.00 37.56 O ANISOU 1634 OD2 ASP A 381 4401 5063 4808 -315 45 -71 O ATOM 1635 N LEU A 382 40.849 35.530 -7.523 1.00 30.78 N ANISOU 1635 N LEU A 382 3190 4427 4078 -149 251 254 N ATOM 1636 CA LEU A 382 41.034 34.563 -8.608 1.00 31.79 C ANISOU 1636 CA LEU A 382 3221 4725 4134 -92 302 248 C ATOM 1637 C LEU A 382 42.274 34.854 -9.453 1.00 33.50 C ANISOU 1637 C LEU A 382 3310 4965 4453 -59 344 380 C ATOM 1638 O LEU A 382 42.582 36.009 -9.723 1.00 28.51 O ANISOU 1638 O LEU A 382 2626 4288 3917 -43 379 514 O ATOM 1639 CB LEU A 382 39.812 34.537 -9.531 1.00 31.62 C ANISOU 1639 CB LEU A 382 3176 4869 3967 -1 384 241 C ATOM 1640 CG LEU A 382 38.460 34.083 -8.975 1.00 34.20 C ANISOU 1640 CG LEU A 382 3593 5209 4192 -10 362 133 C ATOM 1641 CD1 LEU A 382 37.427 34.073 -10.100 1.00 33.58 C ANISOU 1641 CD1 LEU A 382 3469 5285 4003 87 431 149 C ATOM 1642 CD2 LEU A 382 38.551 32.708 -8.303 1.00 29.36 C ANISOU 1642 CD2 LEU A 382 3019 4580 3554 -61 277 11 C ATOM 1643 N THR A 383 42.972 33.801 -9.881 1.00 32.71 N ANISOU 1643 N THR A 383 3152 4937 4341 -41 342 350 N ATOM 1644 CA THR A 383 43.992 33.938 -10.914 1.00 35.29 C ANISOU 1644 CA THR A 383 3344 5338 4727 28 419 482 C ATOM 1645 C THR A 383 43.324 34.341 -12.220 1.00 38.90 C ANISOU 1645 C THR A 383 3742 5983 5057 156 539 554 C ATOM 1646 O THR A 383 42.110 34.176 -12.379 1.00 38.39 O ANISOU 1646 O THR A 383 3737 5998 4851 189 545 471 O ATOM 1647 CB THR A 383 44.759 32.623 -11.167 1.00 41.88 C ANISOU 1647 CB THR A 383 4134 6231 5547 42 399 415 C ATOM 1648 OG1 THR A 383 43.834 31.590 -11.522 1.00 39.37 O ANISOU 1648 OG1 THR A 383 3857 6051 5049 96 388 273 O ATOM 1649 CG2 THR A 383 45.554 32.202 -9.933 1.00 38.90 C ANISOU 1649 CG2 THR A 383 3804 5662 5314 -90 275 357 C ATOM 1650 N SER A 384 44.117 34.857 -13.158 1.00 41.81 N ANISOU 1650 N SER A 384 3988 6420 5480 231 634 719 N ATOM 1651 CA SER A 384 43.575 35.352 -14.422 1.00 42.13 C ANISOU 1651 CA SER A 384 3971 6635 5401 358 751 811 C ATOM 1652 C SER A 384 43.011 34.197 -15.246 1.00 40.26 C ANISOU 1652 C SER A 384 3761 6584 4954 467 773 690 C ATOM 1653 O SER A 384 41.961 34.326 -15.880 1.00 37.88 O ANISOU 1653 O SER A 384 3490 6391 4510 539 804 667 O ATOM 1654 CB SER A 384 44.634 36.146 -15.201 1.00 46.06 C ANISOU 1654 CB SER A 384 4322 7164 6014 419 852 1038 C ATOM 1655 OG SER A 384 45.800 35.375 -15.406 1.00 57.85 O ANISOU 1655 OG SER A 384 5744 8677 7557 447 873 1062 O ATOM 1656 N ALA A 385 43.694 33.057 -15.200 1.00 30.82 N ANISOU 1656 N ALA A 385 2555 5407 3748 475 737 607 N ATOM 1657 CA ALA A 385 43.182 31.837 -15.814 1.00 39.61 C ANISOU 1657 CA ALA A 385 3705 6664 4681 571 712 462 C ATOM 1658 C ALA A 385 41.818 31.473 -15.239 1.00 44.44 C ANISOU 1658 C ALA A 385 4425 7245 5217 518 615 313 C ATOM 1659 O ALA A 385 40.913 31.068 -15.975 1.00 39.02 O ANISOU 1659 O ALA A 385 3768 6678 4380 616 609 249 O ATOM 1660 CB ALA A 385 44.150 30.696 -15.614 1.00 45.10 C ANISOU 1660 CB ALA A 385 4375 7347 5416 562 662 385 C ATOM 1661 N ALA A 386 41.668 31.618 -13.924 1.00 37.31 N ANISOU 1661 N ALA A 386 3581 6174 4421 372 536 265 N ATOM 1662 CA ALA A 386 40.395 31.313 -13.287 1.00 36.01 C ANISOU 1662 CA ALA A 386 3509 5973 4201 324 460 148 C ATOM 1663 C ALA A 386 39.333 32.348 -13.668 1.00 35.86 C ANISOU 1663 C ALA A 386 3508 5987 4131 362 523 216 C ATOM 1664 O ALA A 386 38.165 32.006 -13.810 1.00 30.45 O ANISOU 1664 O ALA A 386 2867 5348 3357 392 493 144 O ATOM 1665 CB ALA A 386 40.553 31.224 -11.767 1.00 27.35 C ANISOU 1665 CB ALA A 386 2479 4697 3215 174 373 90 C ATOM 1666 N GLN A 387 39.747 33.605 -13.834 1.00 34.59 N ANISOU 1666 N GLN A 387 3303 5793 4046 359 601 361 N ATOM 1667 CA GLN A 387 38.846 34.663 -14.288 1.00 34.31 C ANISOU 1667 CA GLN A 387 3269 5791 3978 396 663 439 C ATOM 1668 C GLN A 387 38.367 34.358 -15.706 1.00 36.54 C ANISOU 1668 C GLN A 387 3518 6258 4106 539 716 452 C ATOM 1669 O GLN A 387 37.208 34.541 -16.030 1.00 34.49 O ANISOU 1669 O GLN A 387 3294 6039 3771 573 715 430 O ATOM 1670 CB GLN A 387 39.543 36.036 -14.251 1.00 29.81 C ANISOU 1670 CB GLN A 387 2636 5146 3544 368 719 606 C ATOM 1671 CG GLN A 387 39.760 36.625 -12.852 1.00 35.69 C ANISOU 1671 CG GLN A 387 3438 5685 4437 241 648 595 C ATOM 1672 CD GLN A 387 38.500 37.255 -12.261 1.00 39.59 C ANISOU 1672 CD GLN A 387 4017 6116 4909 208 631 550 C ATOM 1673 OE1 GLN A 387 37.405 37.095 -12.796 1.00 44.66 O ANISOU 1673 OE1 GLN A 387 4675 6858 5437 262 662 514 O ATOM 1674 NE2 GLN A 387 38.657 37.982 -11.154 1.00 35.27 N ANISOU 1674 NE2 GLN A 387 3527 5397 4478 126 575 553 N ATOM 1675 N ASN A 388 39.278 33.896 -16.552 1.00 38.50 N ANISOU 1675 N ASN A 388 3703 6616 4309 631 759 489 N ATOM 1676 CA ASN A 388 38.928 33.503 -17.908 1.00 41.73 C ANISOU 1676 CA ASN A 388 4102 7206 4549 791 798 487 C ATOM 1677 C ASN A 388 37.890 32.383 -17.909 1.00 43.01 C ANISOU 1677 C ASN A 388 4343 7394 4603 819 687 313 C ATOM 1678 O ASN A 388 36.906 32.437 -18.642 1.00 43.85 O ANISOU 1678 O ASN A 388 4481 7576 4605 901 678 300 O ATOM 1679 CB ASN A 388 40.184 33.069 -18.674 1.00 48.47 C ANISOU 1679 CB ASN A 388 4882 8165 5368 895 865 545 C ATOM 1680 CG ASN A 388 39.897 32.737 -20.123 1.00 64.61 C ANISOU 1680 CG ASN A 388 6930 10404 7214 1087 913 549 C ATOM 1681 OD1 ASN A 388 39.594 33.624 -20.925 1.00 71.49 O ANISOU 1681 OD1 ASN A 388 7776 11356 8030 1161 1000 675 O ATOM 1682 ND2 ASN A 388 39.992 31.454 -20.470 1.00 63.24 N ANISOU 1682 ND2 ASN A 388 6792 10305 6931 1176 844 410 N ATOM 1683 N LEU A 389 38.108 31.362 -17.086 1.00 34.63 N ANISOU 1683 N LEU A 389 3310 6262 3586 748 588 187 N ATOM 1684 CA LEU A 389 37.119 30.304 -16.952 1.00 36.49 C ANISOU 1684 CA LEU A 389 3604 6500 3762 759 463 38 C ATOM 1685 C LEU A 389 35.769 30.870 -16.510 1.00 37.66 C ANISOU 1685 C LEU A 389 3797 6578 3933 701 445 42 C ATOM 1686 O LEU A 389 34.730 30.519 -17.066 1.00 41.22 O ANISOU 1686 O LEU A 389 4275 7076 4309 772 390 -4 O ATOM 1687 CB LEU A 389 37.586 29.265 -15.940 1.00 39.33 C ANISOU 1687 CB LEU A 389 3974 6771 4199 662 360 -74 C ATOM 1688 CG LEU A 389 36.772 27.986 -15.984 1.00 43.92 C ANISOU 1688 CG LEU A 389 4586 7371 4729 696 216 -218 C ATOM 1689 CD1 LEU A 389 36.986 27.341 -17.337 1.00 39.17 C ANISOU 1689 CD1 LEU A 389 3972 6918 3993 873 195 -260 C ATOM 1690 CD2 LEU A 389 37.192 27.059 -14.853 1.00 50.75 C ANISOU 1690 CD2 LEU A 389 5455 8138 5691 579 115 -311 C ATOM 1691 N ARG A 390 35.793 31.729 -15.494 1.00 35.60 N ANISOU 1691 N ARG A 390 3548 6197 3783 580 484 97 N ATOM 1692 CA ARG A 390 34.576 32.353 -14.969 1.00 32.35 C ANISOU 1692 CA ARG A 390 3178 5711 3402 527 486 108 C ATOM 1693 C ARG A 390 33.809 33.091 -16.064 1.00 37.58 C ANISOU 1693 C ARG A 390 3826 6457 3994 620 542 184 C ATOM 1694 O ARG A 390 32.588 32.990 -16.153 1.00 37.85 O ANISOU 1694 O ARG A 390 3890 6483 4009 635 503 155 O ATOM 1695 CB ARG A 390 34.910 33.321 -13.823 1.00 27.32 C ANISOU 1695 CB ARG A 390 2562 4938 2881 411 526 162 C ATOM 1696 CG ARG A 390 33.673 33.901 -13.097 1.00 33.36 C ANISOU 1696 CG ARG A 390 3381 5618 3677 361 531 160 C ATOM 1697 CD ARG A 390 34.006 35.219 -12.405 1.00 40.79 C ANISOU 1697 CD ARG A 390 4339 6451 4710 296 584 239 C ATOM 1698 NE ARG A 390 34.886 36.009 -13.256 1.00 38.41 N ANISOU 1698 NE ARG A 390 3964 6199 4430 336 646 354 N ATOM 1699 CZ ARG A 390 34.490 36.614 -14.371 1.00 41.05 C ANISOU 1699 CZ ARG A 390 4249 6629 4718 414 707 439 C ATOM 1700 NH1 ARG A 390 33.215 36.540 -14.753 1.00 32.84 N ANISOU 1700 NH1 ARG A 390 3232 5631 3615 454 704 411 N ATOM 1701 NH2 ARG A 390 35.364 37.289 -15.104 1.00 36.04 N ANISOU 1701 NH2 ARG A 390 3538 6046 4112 453 768 562 N ATOM 1702 N GLU A 391 34.540 33.823 -16.900 1.00 37.10 N ANISOU 1702 N GLU A 391 3714 6473 3908 681 632 294 N ATOM 1703 CA GLU A 391 33.947 34.610 -17.969 1.00 39.68 C ANISOU 1703 CA GLU A 391 4023 6883 4169 767 692 385 C ATOM 1704 C GLU A 391 33.229 33.746 -19.004 1.00 46.47 C ANISOU 1704 C GLU A 391 4914 7851 4891 895 626 313 C ATOM 1705 O GLU A 391 32.099 34.043 -19.396 1.00 40.36 O ANISOU 1705 O GLU A 391 4165 7078 4092 923 605 321 O ATOM 1706 CB GLU A 391 35.020 35.455 -18.641 1.00 35.22 C ANISOU 1706 CB GLU A 391 3384 6388 3611 814 803 534 C ATOM 1707 CG GLU A 391 34.460 36.621 -19.427 1.00 49.92 C ANISOU 1707 CG GLU A 391 5216 8298 5454 858 875 662 C ATOM 1708 CD GLU A 391 33.437 37.413 -18.640 1.00 60.69 C ANISOU 1708 CD GLU A 391 6610 9535 6914 756 857 661 C ATOM 1709 OE1 GLU A 391 33.670 37.652 -17.432 1.00 62.56 O ANISOU 1709 OE1 GLU A 391 6862 9639 7269 643 838 638 O ATOM 1710 OE2 GLU A 391 32.402 37.799 -19.232 1.00 64.02 O ANISOU 1710 OE2 GLU A 391 7045 9988 7292 795 858 683 O ATOM 1711 N ARG A 392 33.879 32.675 -19.445 1.00 46.56 N ANISOU 1711 N ARG A 392 4926 7942 4821 977 580 238 N ATOM 1712 CA ARG A 392 33.248 31.773 -20.406 1.00 54.46 C ANISOU 1712 CA ARG A 392 5970 9031 5692 1113 484 150 C ATOM 1713 C ARG A 392 31.935 31.205 -19.880 1.00 45.16 C ANISOU 1713 C ARG A 392 4835 7757 4566 1062 353 56 C ATOM 1714 O ARG A 392 30.934 31.164 -20.594 1.00 44.84 O ANISOU 1714 O ARG A 392 4826 7738 4473 1139 292 46 O ATOM 1715 CB ARG A 392 34.190 30.635 -20.793 1.00 59.53 C ANISOU 1715 CB ARG A 392 6610 9755 6253 1205 438 64 C ATOM 1716 CG ARG A 392 35.184 31.013 -21.877 1.00 78.06 C ANISOU 1716 CG ARG A 392 8923 12248 8487 1341 559 161 C ATOM 1717 CD ARG A 392 36.239 29.935 -22.035 1.00 90.67 C ANISOU 1717 CD ARG A 392 10509 13907 10034 1415 531 80 C ATOM 1718 NE ARG A 392 36.984 30.071 -23.282 1.00103.84 N ANISOU 1718 NE ARG A 392 12160 15743 11551 1599 636 157 N ATOM 1719 CZ ARG A 392 36.538 29.656 -24.465 1.00110.33 C ANISOU 1719 CZ ARG A 392 13046 16688 12186 1789 591 108 C ATOM 1720 NH1 ARG A 392 35.345 29.083 -24.559 1.00112.12 N ANISOU 1720 NH1 ARG A 392 13350 16870 12379 1810 425 -17 N ATOM 1721 NH2 ARG A 392 37.282 29.816 -25.553 1.00109.56 N ANISOU 1721 NH2 ARG A 392 12937 16753 11939 1968 707 191 N ATOM 1722 N ALA A 393 31.950 30.756 -18.631 1.00 33.67 N ANISOU 1722 N ALA A 393 3378 6192 3223 937 306 -4 N ATOM 1723 CA ALA A 393 30.755 30.203 -18.025 1.00 41.56 C ANISOU 1723 CA ALA A 393 4400 7098 4293 885 196 -67 C ATOM 1724 C ALA A 393 29.675 31.283 -17.929 1.00 42.14 C ANISOU 1724 C ALA A 393 4480 7115 4417 848 256 20 C ATOM 1725 O ALA A 393 28.502 31.016 -18.196 1.00 41.60 O ANISOU 1725 O ALA A 393 4424 7016 4365 880 174 4 O ATOM 1726 CB ALA A 393 31.069 29.612 -16.655 1.00 32.46 C ANISOU 1726 CB ALA A 393 3242 5847 3243 759 157 -125 C ATOM 1727 N LEU A 394 30.079 32.499 -17.566 1.00 33.11 N ANISOU 1727 N LEU A 394 3321 5946 3311 782 388 116 N ATOM 1728 CA LEU A 394 29.132 33.608 -17.474 1.00 41.18 C ANISOU 1728 CA LEU A 394 4346 6914 4387 748 449 198 C ATOM 1729 C LEU A 394 28.478 33.881 -18.825 1.00 43.43 C ANISOU 1729 C LEU A 394 4631 7279 4592 860 436 240 C ATOM 1730 O LEU A 394 27.259 34.033 -18.915 1.00 43.46 O ANISOU 1730 O LEU A 394 4645 7230 4638 860 397 251 O ATOM 1731 CB LEU A 394 29.797 34.886 -16.945 1.00 29.41 C ANISOU 1731 CB LEU A 394 2836 5383 2957 672 570 290 C ATOM 1732 CG LEU A 394 28.865 36.109 -16.865 1.00 29.58 C ANISOU 1732 CG LEU A 394 2854 5346 3038 641 630 373 C ATOM 1733 CD1 LEU A 394 27.782 35.903 -15.826 1.00 29.54 C ANISOU 1733 CD1 LEU A 394 2883 5228 3113 575 600 327 C ATOM 1734 CD2 LEU A 394 29.647 37.371 -16.543 1.00 33.10 C ANISOU 1734 CD2 LEU A 394 3273 5757 3546 587 723 467 C ATOM 1735 N GLN A 395 29.290 33.952 -19.875 1.00 43.03 N ANISOU 1735 N GLN A 395 4570 7352 4428 960 470 272 N ATOM 1736 CA GLN A 395 28.761 34.242 -21.200 1.00 39.36 C ANISOU 1736 CA GLN A 395 4120 6973 3864 1080 460 317 C ATOM 1737 C GLN A 395 27.781 33.178 -21.665 1.00 45.64 C ANISOU 1737 C GLN A 395 4963 7755 4623 1159 297 217 C ATOM 1738 O GLN A 395 26.734 33.499 -22.218 1.00 49.56 O ANISOU 1738 O GLN A 395 5478 8228 5124 1194 255 248 O ATOM 1739 CB GLN A 395 29.887 34.382 -22.218 1.00 42.77 C ANISOU 1739 CB GLN A 395 4535 7554 4161 1195 534 372 C ATOM 1740 CG GLN A 395 30.611 35.690 -22.136 1.00 42.96 C ANISOU 1740 CG GLN A 395 4495 7594 4235 1143 685 521 C ATOM 1741 CD GLN A 395 31.853 35.701 -22.995 1.00 61.65 C ANISOU 1741 CD GLN A 395 6827 10106 6494 1254 769 593 C ATOM 1742 OE1 GLN A 395 31.939 34.983 -23.990 1.00 69.31 O ANISOU 1742 OE1 GLN A 395 7836 11193 7307 1406 731 548 O ATOM 1743 NE2 GLN A 395 32.826 36.517 -22.616 1.00 65.28 N ANISOU 1743 NE2 GLN A 395 7210 10552 7041 1190 880 710 N ATOM 1744 N ARG A 396 28.122 31.913 -21.443 1.00 38.15 N ANISOU 1744 N ARG A 396 4029 6809 3655 1186 191 101 N ATOM 1745 CA ARG A 396 27.262 30.824 -21.883 1.00 47.46 C ANISOU 1745 CA ARG A 396 5247 7964 4823 1267 4 4 C ATOM 1746 C ARG A 396 25.912 30.871 -21.163 1.00 49.79 C ANISOU 1746 C ARG A 396 5527 8113 5277 1174 -58 19 C ATOM 1747 O ARG A 396 24.861 30.701 -21.786 1.00 49.21 O ANISOU 1747 O ARG A 396 5475 8002 5220 1237 -170 18 O ATOM 1748 CB ARG A 396 27.963 29.470 -21.711 1.00 58.65 C ANISOU 1748 CB ARG A 396 6669 9405 6209 1306 -106 -121 C ATOM 1749 CG ARG A 396 29.351 29.430 -22.383 1.00 69.22 C ANISOU 1749 CG ARG A 396 8014 10888 7398 1405 -24 -126 C ATOM 1750 CD ARG A 396 29.918 28.019 -22.568 1.00 70.28 C ANISOU 1750 CD ARG A 396 8166 11061 7475 1492 -161 -266 C ATOM 1751 NE ARG A 396 29.938 27.241 -21.330 1.00 71.69 N ANISOU 1751 NE ARG A 396 8308 11133 7798 1360 -239 -336 N ATOM 1752 CZ ARG A 396 30.889 27.318 -20.400 1.00 67.83 C ANISOU 1752 CZ ARG A 396 7778 10623 7370 1246 -147 -324 C ATOM 1753 NH1 ARG A 396 31.912 28.150 -20.550 1.00 65.77 N ANISOU 1753 NH1 ARG A 396 7498 10432 7061 1243 22 -239 N ATOM 1754 NH2 ARG A 396 30.811 26.565 -19.311 1.00 63.51 N ANISOU 1754 NH2 ARG A 396 7207 9980 6946 1133 -233 -388 N ATOM 1755 N LEU A 397 25.938 31.130 -19.860 1.00 38.42 N ANISOU 1755 N LEU A 397 4052 6589 3957 1032 17 42 N ATOM 1756 CA LEU A 397 24.699 31.227 -19.091 1.00 40.54 C ANISOU 1756 CA LEU A 397 4300 6727 4376 951 -9 74 C ATOM 1757 C LEU A 397 23.881 32.457 -19.475 1.00 41.57 C ANISOU 1757 C LEU A 397 4428 6831 4536 944 72 178 C ATOM 1758 O LEU A 397 22.659 32.388 -19.554 1.00 44.79 O ANISOU 1758 O LEU A 397 4826 7155 5037 948 0 203 O ATOM 1759 CB LEU A 397 24.972 31.238 -17.587 1.00 31.13 C ANISOU 1759 CB LEU A 397 3088 5463 3279 819 63 74 C ATOM 1760 CG LEU A 397 23.722 31.403 -16.716 1.00 39.96 C ANISOU 1760 CG LEU A 397 4183 6458 4543 748 70 125 C ATOM 1761 CD1 LEU A 397 22.705 30.295 -16.999 1.00 35.94 C ANISOU 1761 CD1 LEU A 397 3648 5894 4115 797 -108 97 C ATOM 1762 CD2 LEU A 397 24.085 31.436 -15.231 1.00 33.90 C ANISOU 1762 CD2 LEU A 397 3415 5633 3833 638 151 122 C ATOM 1763 N MET A 398 24.558 33.576 -19.715 1.00 41.90 N ANISOU 1763 N MET A 398 4469 6935 4517 933 213 245 N ATOM 1764 CA MET A 398 23.870 34.826 -20.031 1.00 42.00 C ANISOU 1764 CA MET A 398 4469 6921 4567 916 292 347 C ATOM 1765 C MET A 398 23.279 34.834 -21.433 1.00 46.59 C ANISOU 1765 C MET A 398 5076 7551 5076 1031 211 367 C ATOM 1766 O MET A 398 22.279 35.507 -21.688 1.00 45.30 O ANISOU 1766 O MET A 398 4903 7327 4982 1018 213 432 O ATOM 1767 CB MET A 398 24.801 36.025 -19.860 1.00 40.18 C ANISOU 1767 CB MET A 398 4218 6733 4317 868 447 424 C ATOM 1768 CG MET A 398 25.074 36.382 -18.414 1.00 43.66 C ANISOU 1768 CG MET A 398 4648 7084 4856 749 523 423 C ATOM 1769 SD MET A 398 23.604 37.036 -17.580 1.00 45.65 S ANISOU 1769 SD MET A 398 4893 7194 5256 674 553 465 S ATOM 1770 CE MET A 398 23.760 36.265 -15.984 1.00 27.29 C ANISOU 1770 CE MET A 398 2589 4787 2991 597 549 392 C ATOM 1771 N THR A 399 23.901 34.108 -22.351 1.00 37.98 N ANISOU 1771 N THR A 399 4021 6566 3842 1151 137 309 N ATOM 1772 CA THR A 399 23.332 34.006 -23.681 1.00 42.71 C ANISOU 1772 CA THR A 399 4667 7207 4352 1280 36 312 C ATOM 1773 C THR A 399 21.976 33.333 -23.553 1.00 42.61 C ANISOU 1773 C THR A 399 4663 7060 4469 1277 -132 275 C ATOM 1774 O THR A 399 21.005 33.769 -24.156 1.00 42.20 O ANISOU 1774 O THR A 399 4623 6955 4456 1303 -182 327 O ATOM 1775 CB THR A 399 24.219 33.202 -24.650 1.00 43.92 C ANISOU 1775 CB THR A 399 4875 7498 4314 1436 -28 238 C ATOM 1776 OG1 THR A 399 25.564 33.681 -24.583 1.00 48.54 O ANISOU 1776 OG1 THR A 399 5431 8196 4814 1429 133 283 O ATOM 1777 CG2 THR A 399 23.718 33.367 -26.075 1.00 44.50 C ANISOU 1777 CG2 THR A 399 5015 7629 4265 1583 -105 260 C ATOM 1778 N SER A 400 21.907 32.278 -22.747 1.00 39.55 N ANISOU 1778 N SER A 400 4257 6606 4165 1240 -222 197 N ATOM 1779 CA SER A 400 20.646 31.567 -22.561 1.00 44.34 C ANISOU 1779 CA SER A 400 4847 7073 4926 1236 -390 182 C ATOM 1780 C SER A 400 19.595 32.406 -21.839 1.00 43.10 C ANISOU 1780 C SER A 400 4637 6793 4947 1123 -305 286 C ATOM 1781 O SER A 400 18.411 32.349 -22.174 1.00 41.99 O ANISOU 1781 O SER A 400 4486 6548 4922 1142 -412 326 O ATOM 1782 CB SER A 400 20.865 30.246 -21.825 1.00 43.84 C ANISOU 1782 CB SER A 400 4760 6972 4926 1218 -504 92 C ATOM 1783 OG SER A 400 21.517 29.317 -22.670 1.00 52.51 O ANISOU 1783 OG SER A 400 5913 8155 5885 1350 -642 -16 O ATOM 1784 N VAL A 401 20.032 33.169 -20.843 1.00 37.24 N ANISOU 1784 N VAL A 401 3862 6056 4232 1014 -120 329 N ATOM 1785 CA VAL A 401 19.137 34.041 -20.095 1.00 32.96 C ANISOU 1785 CA VAL A 401 3276 5408 3838 919 -18 421 C ATOM 1786 C VAL A 401 18.575 35.150 -20.979 1.00 34.07 C ANISOU 1786 C VAL A 401 3423 5546 3976 941 18 502 C ATOM 1787 O VAL A 401 17.367 35.402 -20.990 1.00 38.52 O ANISOU 1787 O VAL A 401 3957 5997 4680 923 -16 564 O ATOM 1788 CB VAL A 401 19.844 34.672 -18.881 1.00 33.45 C ANISOU 1788 CB VAL A 401 3325 5480 3906 818 158 434 C ATOM 1789 CG1 VAL A 401 19.008 35.808 -18.304 1.00 29.00 C ANISOU 1789 CG1 VAL A 401 2732 4826 3460 748 277 526 C ATOM 1790 CG2 VAL A 401 20.118 33.618 -17.832 1.00 32.89 C ANISOU 1790 CG2 VAL A 401 3242 5379 3875 778 122 373 C ATOM 1791 N THR A 402 19.449 35.812 -21.724 1.00 30.49 N ANISOU 1791 N THR A 402 2999 5213 3374 981 88 514 N ATOM 1792 CA THR A 402 19.015 36.927 -22.558 1.00 41.34 C ANISOU 1792 CA THR A 402 4372 6595 4740 995 130 602 C ATOM 1793 C THR A 402 18.137 36.450 -23.723 1.00 48.97 C ANISOU 1793 C THR A 402 5378 7530 5699 1096 -46 596 C ATOM 1794 O THR A 402 17.212 37.151 -24.135 1.00 46.56 O ANISOU 1794 O THR A 402 5061 7154 5477 1083 -58 670 O ATOM 1795 CB THR A 402 20.207 37.747 -23.086 1.00 40.54 C ANISOU 1795 CB THR A 402 4278 6636 4490 1018 249 640 C ATOM 1796 OG1 THR A 402 21.118 36.882 -23.772 1.00 43.61 O ANISOU 1796 OG1 THR A 402 4713 7146 4709 1127 187 571 O ATOM 1797 CG2 THR A 402 20.933 38.428 -21.937 1.00 38.39 C ANISOU 1797 CG2 THR A 402 3965 6356 4267 911 402 664 C ATOM 1798 N ASN A 403 18.423 35.258 -24.247 1.00 38.98 N ANISOU 1798 N ASN A 403 4163 6307 4340 1200 -197 503 N ATOM 1799 CA ASN A 403 17.583 34.677 -25.295 1.00 43.67 C ANISOU 1799 CA ASN A 403 4809 6848 4934 1309 -405 479 C ATOM 1800 C ASN A 403 16.151 34.365 -24.842 1.00 41.62 C ANISOU 1800 C ASN A 403 4502 6393 4917 1256 -521 515 C ATOM 1801 O ASN A 403 15.242 34.303 -25.668 1.00 47.49 O ANISOU 1801 O ASN A 403 5274 7054 5715 1316 -672 538 O ATOM 1802 CB ASN A 403 18.223 33.419 -25.880 1.00 44.92 C ANISOU 1802 CB ASN A 403 5038 7084 4947 1443 -560 358 C ATOM 1803 CG ASN A 403 19.446 33.722 -26.714 1.00 50.87 C ANISOU 1803 CG ASN A 403 5848 8028 5450 1543 -470 342 C ATOM 1804 OD1 ASN A 403 19.684 34.867 -27.097 1.00 55.31 O ANISOU 1804 OD1 ASN A 403 6403 8661 5950 1527 -327 436 O ATOM 1805 ND2 ASN A 403 20.235 32.695 -26.996 1.00 47.06 N ANISOU 1805 ND2 ASN A 403 5415 7632 4834 1649 -554 233 N ATOM 1806 N ARG A 404 15.952 34.158 -23.541 1.00 42.55 N ANISOU 1806 N ARG A 404 4547 6436 5185 1150 -452 528 N ATOM 1807 CA ARG A 404 14.608 33.914 -23.010 1.00 45.55 C ANISOU 1807 CA ARG A 404 4860 6635 5812 1100 -528 592 C ATOM 1808 C ARG A 404 14.165 35.058 -22.115 1.00 40.02 C ANISOU 1808 C ARG A 404 4095 5879 5230 982 -325 692 C ATOM 1809 O ARG A 404 13.303 34.883 -21.256 1.00 41.63 O ANISOU 1809 O ARG A 404 4229 5959 5629 924 -312 751 O ATOM 1810 CB ARG A 404 14.555 32.612 -22.208 1.00 45.48 C ANISOU 1810 CB ARG A 404 4810 6569 5903 1091 -632 543 C ATOM 1811 CG ARG A 404 14.981 31.378 -22.973 1.00 54.30 C ANISOU 1811 CG ARG A 404 5984 7724 6924 1210 -855 430 C ATOM 1812 CD ARG A 404 14.753 30.112 -22.149 1.00 65.30 C ANISOU 1812 CD ARG A 404 7311 9033 8466 1189 -979 403 C ATOM 1813 NE ARG A 404 13.349 29.704 -22.132 1.00 75.04 N ANISOU 1813 NE ARG A 404 8477 10078 9958 1188 -1143 487 N ATOM 1814 CZ ARG A 404 12.786 28.920 -23.050 1.00 77.65 C ANISOU 1814 CZ ARG A 404 8833 10317 10352 1293 -1421 455 C ATOM 1815 NH1 ARG A 404 13.509 28.456 -24.064 1.00 74.03 N ANISOU 1815 NH1 ARG A 404 8482 9954 9692 1418 -1558 328 N ATOM 1816 NH2 ARG A 404 11.501 28.598 -22.955 1.00 76.81 N ANISOU 1816 NH2 ARG A 404 8647 10019 10518 1282 -1567 553 N ATOM 1817 N CYS A 405 14.759 36.228 -22.323 1.00 33.41 N ANISOU 1817 N CYS A 405 4288 3736 4669 1471 35 221 N ATOM 1818 CA CYS A 405 14.539 37.361 -21.434 1.00 38.46 C ANISOU 1818 CA CYS A 405 4854 4531 5229 1355 142 277 C ATOM 1819 C CYS A 405 13.055 37.686 -21.264 1.00 43.79 C ANISOU 1819 C CYS A 405 5504 5209 5926 1338 17 256 C ATOM 1820 O CYS A 405 12.594 37.967 -20.156 1.00 44.35 O ANISOU 1820 O CYS A 405 5424 5385 6042 1215 31 363 O ATOM 1821 CB CYS A 405 15.291 38.598 -21.938 1.00 36.78 C ANISOU 1821 CB CYS A 405 4805 4352 4818 1419 340 230 C ATOM 1822 SG CYS A 405 15.285 39.952 -20.724 1.00 69.93 S ANISOU 1822 SG CYS A 405 8899 8747 8926 1261 481 310 S ATOM 1823 N GLN A 406 12.316 37.651 -22.369 1.00 48.66 N ANISOU 1823 N GLN A 406 6281 5697 6511 1476 -105 126 N ATOM 1824 CA GLN A 406 10.892 37.974 -22.356 1.00 54.22 C ANISOU 1824 CA GLN A 406 6977 6375 7249 1470 -231 105 C ATOM 1825 C GLN A 406 10.150 37.048 -21.391 1.00 48.32 C ANISOU 1825 C GLN A 406 5983 5605 6771 1369 -374 230 C ATOM 1826 O GLN A 406 9.429 37.497 -20.503 1.00 40.32 O ANISOU 1826 O GLN A 406 4859 4662 5797 1275 -353 343 O ATOM 1827 CB GLN A 406 10.315 37.846 -23.769 1.00 66.23 C ANISOU 1827 CB GLN A 406 8709 7730 8726 1658 -379 -69 C ATOM 1828 CG GLN A 406 8.816 38.078 -23.861 1.00 83.22 C ANISOU 1828 CG GLN A 406 10854 9821 10946 1659 -539 -95 C ATOM 1829 CD GLN A 406 8.436 39.542 -23.728 1.00 93.47 C ANISOU 1829 CD GLN A 406 12232 11249 12034 1618 -376 -85 C ATOM 1830 OE1 GLN A 406 9.232 40.436 -24.030 1.00 96.09 O ANISOU 1830 OE1 GLN A 406 12692 11674 12143 1660 -168 -130 O ATOM 1831 NE2 GLN A 406 7.210 39.794 -23.281 1.00 95.56 N ANISOU 1831 NE2 GLN A 406 12415 11507 12386 1543 -459 -14 N ATOM 1832 N GLU A 407 10.353 35.749 -21.568 1.00 48.60 N ANISOU 1832 N GLU A 407 5936 5533 6996 1404 -502 222 N ATOM 1833 CA GLU A 407 9.760 34.750 -20.697 1.00 48.27 C ANISOU 1833 CA GLU A 407 5637 5456 7247 1335 -616 343 C ATOM 1834 C GLU A 407 10.165 34.945 -19.230 1.00 41.44 C ANISOU 1834 C GLU A 407 4582 4762 6400 1201 -452 524 C ATOM 1835 O GLU A 407 9.324 34.905 -18.338 1.00 39.21 O ANISOU 1835 O GLU A 407 4140 4491 6268 1156 -477 654 O ATOM 1836 CB GLU A 407 10.146 33.355 -21.184 1.00 45.00 C ANISOU 1836 CB GLU A 407 5174 4916 7006 1398 -743 296 C ATOM 1837 CG GLU A 407 9.729 32.235 -20.245 1.00 53.61 C ANISOU 1837 CG GLU A 407 5967 5982 8422 1336 -818 429 C ATOM 1838 CD GLU A 407 10.291 30.895 -20.672 1.00 63.20 C ANISOU 1838 CD GLU A 407 7128 7103 9781 1382 -902 389 C ATOM 1839 OE1 GLU A 407 11.034 30.282 -19.873 1.00 65.07 O ANISOU 1839 OE1 GLU A 407 7191 7438 10093 1305 -782 502 O ATOM 1840 OE2 GLU A 407 10.004 30.467 -21.814 1.00 66.10 O ANISOU 1840 OE2 GLU A 407 7641 7299 10176 1502 -1086 243 O ATOM 1841 N LEU A 408 11.451 35.181 -18.988 1.00 37.34 N ANISOU 1841 N LEU A 408 4092 4362 5734 1157 -285 538 N ATOM 1842 CA LEU A 408 11.961 35.330 -17.621 1.00 34.54 C ANISOU 1842 CA LEU A 408 3577 4163 5386 1048 -149 689 C ATOM 1843 C LEU A 408 11.490 36.617 -16.927 1.00 37.07 C ANISOU 1843 C LEU A 408 3933 4594 5560 996 -59 754 C ATOM 1844 O LEU A 408 11.077 36.591 -15.765 1.00 32.69 O ANISOU 1844 O LEU A 408 3232 4099 5088 953 -36 901 O ATOM 1845 CB LEU A 408 13.485 35.252 -17.622 1.00 38.98 C ANISOU 1845 CB LEU A 408 4165 4797 5848 1016 -15 682 C ATOM 1846 CG LEU A 408 14.021 33.993 -18.307 1.00 42.62 C ANISOU 1846 CG LEU A 408 4612 5152 6429 1067 -79 639 C ATOM 1847 CD1 LEU A 408 15.535 33.956 -18.259 1.00 43.69 C ANISOU 1847 CD1 LEU A 408 4772 5348 6479 1029 73 668 C ATOM 1848 CD2 LEU A 408 13.431 32.764 -17.656 1.00 42.53 C ANISOU 1848 CD2 LEU A 408 4362 5108 6690 1050 -181 728 C ATOM 1849 N ALA A 409 11.550 37.737 -17.644 1.00 30.82 N ANISOU 1849 N ALA A 409 3341 3820 4547 1018 4 652 N ATOM 1850 CA ALA A 409 11.145 39.027 -17.085 1.00 31.27 C ANISOU 1850 CA ALA A 409 3453 3986 4443 966 102 703 C ATOM 1851 C ALA A 409 9.683 39.046 -16.652 1.00 34.02 C ANISOU 1851 C ALA A 409 3738 4286 4900 965 14 805 C ATOM 1852 O ALA A 409 9.331 39.709 -15.683 1.00 35.10 O ANISOU 1852 O ALA A 409 3845 4513 4979 913 90 933 O ATOM 1853 CB ALA A 409 11.415 40.150 -18.086 1.00 28.48 C ANISOU 1853 CB ALA A 409 3317 3649 3857 1011 196 565 C ATOM 1854 N THR A 410 8.834 38.318 -17.375 1.00 39.73 N ANISOU 1854 N THR A 410 4450 4852 5794 1032 -152 755 N ATOM 1855 CA THR A 410 7.405 38.298 -17.080 1.00 34.62 C ANISOU 1855 CA THR A 410 3736 4116 5302 1040 -248 861 C ATOM 1856 C THR A 410 6.997 37.186 -16.119 1.00 39.20 C ANISOU 1856 C THR A 410 4068 4631 6196 1045 -315 1032 C ATOM 1857 O THR A 410 5.830 37.094 -15.738 1.00 39.90 O ANISOU 1857 O THR A 410 4069 4623 6467 1066 -379 1164 O ATOM 1858 CB THR A 410 6.546 38.181 -18.361 1.00 35.22 C ANISOU 1858 CB THR A 410 3922 4027 5432 1121 -417 722 C ATOM 1859 OG1 THR A 410 6.917 37.005 -19.089 1.00 42.53 O ANISOU 1859 OG1 THR A 410 4818 4829 6512 1194 -563 607 O ATOM 1860 CG2 THR A 410 6.731 39.408 -19.252 1.00 30.96 C ANISOU 1860 CG2 THR A 410 3628 3554 4580 1145 -322 575 C ATOM 1861 N ASN A 411 7.947 36.344 -15.728 1.00 37.64 N ANISOU 1861 N ASN A 411 3750 4478 6075 1037 -286 1043 N ATOM 1862 CA ASN A 411 7.626 35.190 -14.900 1.00 40.76 C ANISOU 1862 CA ASN A 411 3894 4811 6782 1066 -331 1191 C ATOM 1863 C ASN A 411 7.605 35.528 -13.416 1.00 43.50 C ANISOU 1863 C ASN A 411 4141 5272 7114 1053 -188 1399 C ATOM 1864 O ASN A 411 8.396 36.350 -12.942 1.00 36.12 O ANISOU 1864 O ASN A 411 3302 4498 5925 1001 -56 1398 O ATOM 1865 CB ASN A 411 8.598 34.029 -15.158 1.00 28.17 C ANISOU 1865 CB ASN A 411 2204 3209 5289 1073 -356 1118 C ATOM 1866 CG ASN A 411 8.327 32.835 -14.245 1.00 36.34 C ANISOU 1866 CG ASN A 411 2958 4201 6651 1111 -368 1275 C ATOM 1867 OD1 ASN A 411 7.409 32.048 -14.484 1.00 45.99 O ANISOU 1867 OD1 ASN A 411 4048 5252 8174 1173 -508 1302 O ATOM 1868 ND2 ASN A 411 9.116 32.707 -13.186 1.00 29.13 N ANISOU 1868 ND2 ASN A 411 1943 3433 5693 1087 -219 1379 N ATOM 1869 N GLU A 412 6.707 34.868 -12.691 1.00 43.40 N ANISOU 1869 N GLU A 412 3936 5159 7394 1121 -220 1580 N ATOM 1870 CA GLU A 412 6.492 35.123 -11.267 1.00 40.64 C ANISOU 1870 CA GLU A 412 3503 4879 7057 1164 -87 1807 C ATOM 1871 C GLU A 412 7.738 34.952 -10.396 1.00 36.35 C ANISOU 1871 C GLU A 412 2911 4509 6392 1152 39 1825 C ATOM 1872 O GLU A 412 7.865 35.613 -9.368 1.00 37.69 O ANISOU 1872 O GLU A 412 3124 4783 6414 1174 152 1947 O ATOM 1873 CB GLU A 412 5.378 34.219 -10.736 1.00 36.00 C ANISOU 1873 CB GLU A 412 2689 4117 6874 1279 -134 2006 C ATOM 1874 CG GLU A 412 5.723 32.742 -10.782 1.00 40.96 C ANISOU 1874 CG GLU A 412 3081 4682 7799 1325 -186 1983 C ATOM 1875 CD GLU A 412 4.548 31.848 -10.391 1.00 53.29 C ANISOU 1875 CD GLU A 412 4395 6035 9818 1452 -239 2173 C ATOM 1876 OE1 GLU A 412 3.727 32.271 -9.545 1.00 41.47 O ANISOU 1876 OE1 GLU A 412 2907 4490 8358 1470 -130 2380 O ATOM 1877 OE2 GLU A 412 4.456 30.722 -10.926 1.00 56.49 O ANISOU 1877 OE2 GLU A 412 4651 6315 10496 1446 -346 2097 O ATOM 1878 N TYR A 413 8.639 34.054 -10.791 1.00 34.89 N ANISOU 1878 N TYR A 413 2641 4344 6271 1125 14 1712 N ATOM 1879 CA TYR A 413 9.864 33.818 -10.033 1.00 38.03 C ANISOU 1879 CA TYR A 413 2982 4896 6572 1106 125 1725 C ATOM 1880 C TYR A 413 11.102 34.419 -10.692 1.00 37.60 C ANISOU 1880 C TYR A 413 3098 4944 6244 998 151 1548 C ATOM 1881 O TYR A 413 11.943 35.015 -10.019 1.00 34.14 O ANISOU 1881 O TYR A 413 2711 4641 5619 964 244 1561 O ATOM 1882 CB TYR A 413 10.083 32.319 -9.769 1.00 41.43 C ANISOU 1882 CB TYR A 413 3163 5290 7290 1160 124 1775 C ATOM 1883 CG TYR A 413 8.899 31.656 -9.106 1.00 44.33 C ANISOU 1883 CG TYR A 413 3326 5533 7986 1293 118 1967 C ATOM 1884 CD1 TYR A 413 8.349 32.188 -7.946 1.00 46.04 C ANISOU 1884 CD1 TYR A 413 3535 5774 8185 1392 215 2165 C ATOM 1885 CD2 TYR A 413 8.323 30.507 -9.641 1.00 46.84 C ANISOU 1885 CD2 TYR A 413 3461 5689 8647 1338 16 1961 C ATOM 1886 CE1 TYR A 413 7.255 31.596 -7.333 1.00 56.73 C ANISOU 1886 CE1 TYR A 413 4730 6981 9843 1507 246 2366 C ATOM 1887 CE2 TYR A 413 7.223 29.907 -9.036 1.00 50.13 C ANISOU 1887 CE2 TYR A 413 3705 5956 9388 1431 32 2145 C ATOM 1888 CZ TYR A 413 6.694 30.458 -7.879 1.00 58.96 C ANISOU 1888 CZ TYR A 413 4859 7088 10457 1484 171 2350 C ATOM 1889 OH TYR A 413 5.598 29.882 -7.267 1.00 64.84 O ANISOU 1889 OH TYR A 413 5485 7657 11492 1522 237 2547 O ATOM 1890 N ALA A 414 11.222 34.269 -12.005 1.00 33.84 N ANISOU 1890 N ALA A 414 2714 4387 5757 965 68 1387 N ATOM 1891 CA ALA A 414 12.469 34.652 -12.663 1.00 32.67 C ANISOU 1891 CA ALA A 414 2706 4305 5404 897 116 1246 C ATOM 1892 C ALA A 414 12.595 36.159 -12.903 1.00 32.51 C ANISOU 1892 C ALA A 414 2896 4347 5109 857 172 1180 C ATOM 1893 O ALA A 414 13.670 36.648 -13.244 1.00 32.37 O ANISOU 1893 O ALA A 414 2979 4386 4935 813 241 1095 O ATOM 1894 CB ALA A 414 12.682 33.855 -13.954 1.00 29.88 C ANISOU 1894 CB ALA A 414 2389 3832 5133 914 27 1115 C ATOM 1895 N ASN A 415 11.509 36.904 -12.707 1.00 32.92 N ANISOU 1895 N ASN A 415 3008 4383 5118 877 156 1234 N ATOM 1896 CA ASN A 415 11.615 38.359 -12.789 1.00 31.84 C ANISOU 1896 CA ASN A 415 3052 4326 4719 836 233 1189 C ATOM 1897 C ASN A 415 12.660 38.918 -11.809 1.00 31.71 C ANISOU 1897 C ASN A 415 3031 4452 4564 790 336 1230 C ATOM 1898 O ASN A 415 13.291 39.928 -12.087 1.00 31.99 O ANISOU 1898 O ASN A 415 3195 4548 4411 746 403 1145 O ATOM 1899 CB ASN A 415 10.252 39.044 -12.607 1.00 26.95 C ANISOU 1899 CB ASN A 415 2491 3673 4075 859 216 1274 C ATOM 1900 CG ASN A 415 9.824 39.130 -11.147 1.00 33.43 C ANISOU 1900 CG ASN A 415 3224 4545 4932 889 264 1480 C ATOM 1901 OD1 ASN A 415 10.163 40.080 -10.446 1.00 35.73 O ANISOU 1901 OD1 ASN A 415 3601 4949 5026 864 350 1521 O ATOM 1902 ND2 ASN A 415 9.054 38.141 -10.691 1.00 28.75 N ANISOU 1902 ND2 ASN A 415 2466 3855 4602 964 210 1618 N ATOM 1903 N TYR A 416 12.848 38.247 -10.672 1.00 29.24 N ANISOU 1903 N TYR A 416 2566 4184 4361 815 345 1356 N ATOM 1904 CA TYR A 416 13.851 38.664 -9.694 1.00 28.64 C ANISOU 1904 CA TYR A 416 2481 4229 4172 789 410 1388 C ATOM 1905 C TYR A 416 15.279 38.528 -10.229 1.00 36.35 C ANISOU 1905 C TYR A 416 3464 5227 5122 722 439 1271 C ATOM 1906 O TYR A 416 16.169 39.317 -9.889 1.00 30.58 O ANISOU 1906 O TYR A 416 2788 4567 4263 678 484 1239 O ATOM 1907 CB TYR A 416 13.709 37.858 -8.402 1.00 31.34 C ANISOU 1907 CB TYR A 416 2659 4604 4645 866 416 1547 C ATOM 1908 CG TYR A 416 12.453 38.171 -7.612 1.00 30.66 C ANISOU 1908 CG TYR A 416 2585 4493 4570 961 422 1710 C ATOM 1909 CD1 TYR A 416 12.458 39.142 -6.624 1.00 40.30 C ANISOU 1909 CD1 TYR A 416 3910 5795 5607 995 464 1788 C ATOM 1910 CD2 TYR A 416 11.268 37.494 -7.856 1.00 34.10 C ANISOU 1910 CD2 TYR A 416 2932 4807 5217 1027 383 1797 C ATOM 1911 CE1 TYR A 416 11.315 39.434 -5.890 1.00 38.94 C ANISOU 1911 CE1 TYR A 416 3772 5585 5438 1101 488 1968 C ATOM 1912 CE2 TYR A 416 10.107 37.786 -7.135 1.00 40.62 C ANISOU 1912 CE2 TYR A 416 3768 5583 6081 1126 405 1982 C ATOM 1913 CZ TYR A 416 10.143 38.754 -6.153 1.00 38.35 C ANISOU 1913 CZ TYR A 416 3604 5380 5587 1166 469 2075 C ATOM 1914 OH TYR A 416 9.018 39.044 -5.424 1.00 41.14 O ANISOU 1914 OH TYR A 416 3990 5671 5969 1283 508 2286 O ATOM 1915 N ILE A 417 15.497 37.521 -11.066 1.00 33.47 N ANISOU 1915 N ILE A 417 3041 4784 4893 724 411 1219 N ATOM 1916 CA ILE A 417 16.809 37.322 -11.669 1.00 31.48 C ANISOU 1916 CA ILE A 417 2808 4522 4631 676 454 1139 C ATOM 1917 C ILE A 417 17.096 38.439 -12.663 1.00 33.87 C ANISOU 1917 C ILE A 417 3298 4791 4779 664 498 1021 C ATOM 1918 O ILE A 417 18.169 39.044 -12.643 1.00 28.59 O ANISOU 1918 O ILE A 417 2669 4151 4044 625 567 991 O ATOM 1919 CB ILE A 417 16.914 35.940 -12.343 1.00 34.18 C ANISOU 1919 CB ILE A 417 3064 4777 5145 697 418 1127 C ATOM 1920 CG1 ILE A 417 16.845 34.848 -11.275 1.00 35.95 C ANISOU 1920 CG1 ILE A 417 3073 5053 5535 711 414 1249 C ATOM 1921 CG2 ILE A 417 18.211 35.817 -13.129 1.00 29.90 C ANISOU 1921 CG2 ILE A 417 2586 4197 4578 664 479 1064 C ATOM 1922 CD1 ILE A 417 16.686 33.462 -11.823 1.00 37.92 C ANISOU 1922 CD1 ILE A 417 3210 5218 5979 738 372 1251 C ATOM 1923 N ILE A 418 16.117 38.727 -13.512 1.00 32.38 N ANISOU 1923 N ILE A 418 3218 4535 4551 710 462 959 N ATOM 1924 CA ILE A 418 16.271 39.780 -14.501 1.00 29.73 C ANISOU 1924 CA ILE A 418 3060 4168 4066 731 524 845 C ATOM 1925 C ILE A 418 16.510 41.124 -13.811 1.00 33.01 C ANISOU 1925 C ILE A 418 3522 4688 4331 682 601 859 C ATOM 1926 O ILE A 418 17.346 41.913 -14.245 1.00 33.40 O ANISOU 1926 O ILE A 418 3648 4736 4306 678 692 793 O ATOM 1927 CB ILE A 418 15.046 39.858 -15.435 1.00 28.27 C ANISOU 1927 CB ILE A 418 2982 3902 3859 799 459 778 C ATOM 1928 CG1 ILE A 418 14.843 38.521 -16.163 1.00 25.45 C ANISOU 1928 CG1 ILE A 418 2588 3420 3662 859 354 747 C ATOM 1929 CG2 ILE A 418 15.199 41.016 -16.425 1.00 24.55 C ANISOU 1929 CG2 ILE A 418 2698 3415 3214 844 553 660 C ATOM 1930 CD1 ILE A 418 16.095 38.046 -16.938 1.00 30.53 C ANISOU 1930 CD1 ILE A 418 3281 4000 4318 892 408 691 C ATOM 1931 N GLN A 419 15.770 41.378 -12.733 1.00 32.07 N ANISOU 1931 N GLN A 419 3358 4644 4182 662 568 954 N ATOM 1932 CA GLN A 419 15.983 42.577 -11.929 1.00 32.40 C ANISOU 1932 CA GLN A 419 3447 4783 4079 623 620 978 C ATOM 1933 C GLN A 419 17.393 42.615 -11.367 1.00 29.00 C ANISOU 1933 C GLN A 419 2949 4390 3679 581 643 976 C ATOM 1934 O GLN A 419 18.029 43.653 -11.396 1.00 27.65 O ANISOU 1934 O GLN A 419 2839 4244 3424 553 700 922 O ATOM 1935 CB GLN A 419 15.012 42.639 -10.758 1.00 28.25 C ANISOU 1935 CB GLN A 419 2892 4314 3528 640 578 1114 C ATOM 1936 CG GLN A 419 13.575 42.987 -11.108 1.00 27.21 C ANISOU 1936 CG GLN A 419 2842 4150 3348 669 571 1148 C ATOM 1937 CD GLN A 419 12.771 43.138 -9.845 1.00 34.32 C ANISOU 1937 CD GLN A 419 3726 5091 4224 703 558 1319 C ATOM 1938 OE1 GLN A 419 12.963 44.097 -9.094 1.00 37.00 O ANISOU 1938 OE1 GLN A 419 4142 5512 4406 690 598 1355 O ATOM 1939 NE2 GLN A 419 11.911 42.159 -9.565 1.00 27.29 N ANISOU 1939 NE2 GLN A 419 2734 4129 3506 765 502 1437 N ATOM 1940 N HIS A 420 17.875 41.496 -10.828 1.00 25.47 N ANISOU 1940 N HIS A 420 2366 3943 3368 578 598 1038 N ATOM 1941 CA HIS A 420 19.250 41.481 -10.337 1.00 29.90 C ANISOU 1941 CA HIS A 420 2859 4527 3975 535 612 1039 C ATOM 1942 C HIS A 420 20.256 41.859 -11.434 1.00 32.41 C ANISOU 1942 C HIS A 420 3234 4762 4318 516 691 950 C ATOM 1943 O HIS A 420 21.149 42.678 -11.218 1.00 31.89 O ANISOU 1943 O HIS A 420 3176 4699 4240 483 724 924 O ATOM 1944 CB HIS A 420 19.648 40.130 -9.745 1.00 28.99 C ANISOU 1944 CB HIS A 420 2586 4425 4006 536 576 1118 C ATOM 1945 CG HIS A 420 21.085 40.078 -9.331 1.00 30.19 C ANISOU 1945 CG HIS A 420 2667 4587 4216 485 589 1121 C ATOM 1946 ND1 HIS A 420 22.088 39.627 -10.166 1.00 36.47 N ANISOU 1946 ND1 HIS A 420 3442 5300 5115 451 644 1097 N ATOM 1947 CD2 HIS A 420 21.696 40.474 -8.191 1.00 26.20 C ANISOU 1947 CD2 HIS A 420 2121 4148 3686 471 548 1150 C ATOM 1948 CE1 HIS A 420 23.248 39.711 -9.541 1.00 33.48 C ANISOU 1948 CE1 HIS A 420 2992 4935 4794 404 641 1123 C ATOM 1949 NE2 HIS A 420 23.039 40.228 -8.342 1.00 38.35 N ANISOU 1949 NE2 HIS A 420 3594 5643 5333 415 571 1142 N ATOM 1950 N ILE A 421 20.113 41.265 -12.610 1.00 33.62 N ANISOU 1950 N ILE A 421 3430 4825 4521 557 720 909 N ATOM 1951 CA ILE A 421 21.054 41.545 -13.690 1.00 30.56 C ANISOU 1951 CA ILE A 421 3114 4334 4164 583 817 851 C ATOM 1952 C ILE A 421 21.036 43.027 -14.090 1.00 35.01 C ANISOU 1952 C ILE A 421 3790 4896 4614 607 902 776 C ATOM 1953 O ILE A 421 22.083 43.645 -14.248 1.00 34.26 O ANISOU 1953 O ILE A 421 3693 4753 4570 604 983 764 O ATOM 1954 CB ILE A 421 20.799 40.649 -14.905 1.00 29.04 C ANISOU 1954 CB ILE A 421 2986 4031 4016 661 823 819 C ATOM 1955 CG1 ILE A 421 21.038 39.184 -14.534 1.00 34.07 C ANISOU 1955 CG1 ILE A 421 3492 4664 4789 630 763 897 C ATOM 1956 CG2 ILE A 421 21.709 41.049 -16.056 1.00 25.98 C ANISOU 1956 CG2 ILE A 421 2709 3520 3642 737 948 776 C ATOM 1957 CD1 ILE A 421 20.488 38.188 -15.548 1.00 32.65 C ANISOU 1957 CD1 ILE A 421 3365 4385 4654 707 720 864 C ATOM 1958 N VAL A 422 19.841 43.598 -14.228 1.00 38.83 N ANISOU 1958 N VAL A 422 4361 5428 4963 631 891 736 N ATOM 1959 CA VAL A 422 19.703 45.013 -14.582 1.00 34.39 C ANISOU 1959 CA VAL A 422 3901 4887 4278 652 989 667 C ATOM 1960 C VAL A 422 20.253 45.946 -13.494 1.00 34.76 C ANISOU 1960 C VAL A 422 3894 5012 4303 578 987 691 C ATOM 1961 O VAL A 422 20.810 46.994 -13.791 1.00 32.85 O ANISOU 1961 O VAL A 422 3682 4749 4049 590 1086 640 O ATOM 1962 CB VAL A 422 18.229 45.370 -14.888 1.00 36.44 C ANISOU 1962 CB VAL A 422 4262 5190 4394 681 976 637 C ATOM 1963 CG1 VAL A 422 18.062 46.875 -15.074 1.00 31.79 C ANISOU 1963 CG1 VAL A 422 3763 4653 3661 687 1092 579 C ATOM 1964 CG2 VAL A 422 17.741 44.610 -16.119 1.00 31.36 C ANISOU 1964 CG2 VAL A 422 3696 4445 3776 777 962 581 C ATOM 1965 N SER A 423 20.099 45.548 -12.236 1.00 27.98 N ANISOU 1965 N SER A 423 2953 4230 3447 522 873 770 N ATOM 1966 CA SER A 423 20.518 46.356 -11.085 1.00 31.91 C ANISOU 1966 CA SER A 423 3422 4798 3905 474 830 790 C ATOM 1967 C SER A 423 22.030 46.367 -10.816 1.00 38.15 C ANISOU 1967 C SER A 423 4114 5530 4851 441 820 785 C ATOM 1968 O SER A 423 22.544 47.261 -10.140 1.00 42.97 O ANISOU 1968 O SER A 423 4711 6161 5454 412 788 766 O ATOM 1969 CB SER A 423 19.831 45.825 -9.832 1.00 32.70 C ANISOU 1969 CB SER A 423 3486 4983 3955 471 714 887 C ATOM 1970 OG SER A 423 18.427 45.837 -10.015 1.00 52.98 O ANISOU 1970 OG SER A 423 6133 7581 6417 503 723 920 O ATOM 1971 N ASN A 424 22.731 45.360 -11.315 1.00 33.30 N ANISOU 1971 N ASN A 424 3431 4833 4388 445 837 809 N ATOM 1972 CA ASN A 424 24.117 45.139 -10.916 1.00 36.96 C ANISOU 1972 CA ASN A 424 3784 5237 5023 405 813 841 C ATOM 1973 C ASN A 424 25.113 45.782 -11.879 1.00 34.86 C ANISOU 1973 C ASN A 424 3527 4832 4887 431 939 808 C ATOM 1974 O ASN A 424 25.212 45.379 -13.033 1.00 36.35 O ANISOU 1974 O ASN A 424 3764 4924 5123 495 1049 809 O ATOM 1975 CB ASN A 424 24.389 43.639 -10.774 1.00 36.29 C ANISOU 1975 CB ASN A 424 3607 5143 5039 390 774 917 C ATOM 1976 CG ASN A 424 25.674 43.348 -10.032 1.00 41.30 C ANISOU 1976 CG ASN A 424 4116 5749 5827 335 723 968 C ATOM 1977 OD1 ASN A 424 26.568 44.183 -9.964 1.00 45.36 O ANISOU 1977 OD1 ASN A 424 4609 6195 6432 314 729 946 O ATOM 1978 ND2 ASN A 424 25.769 42.160 -9.466 1.00 47.46 N ANISOU 1978 ND2 ASN A 424 4803 6577 6655 315 671 1038 N ATOM 1979 N ASP A 425 25.835 46.791 -11.398 1.00 38.47 N ANISOU 1979 N ASP A 425 3940 5263 5414 403 923 783 N ATOM 1980 CA ASP A 425 26.830 47.477 -12.213 1.00 35.55 C ANISOU 1980 CA ASP A 425 3549 4738 5220 445 1053 772 C ATOM 1981 C ASP A 425 27.861 46.515 -12.778 1.00 37.01 C ANISOU 1981 C ASP A 425 3671 4778 5612 461 1114 861 C ATOM 1982 O ASP A 425 28.366 46.723 -13.879 1.00 35.03 O ANISOU 1982 O ASP A 425 3455 4378 5475 551 1276 879 O ATOM 1983 CB ASP A 425 27.523 48.577 -11.413 1.00 40.30 C ANISOU 1983 CB ASP A 425 4075 5319 5918 401 983 740 C ATOM 1984 CG ASP A 425 26.616 49.770 -11.152 1.00 42.15 C ANISOU 1984 CG ASP A 425 4394 5663 5958 407 982 656 C ATOM 1985 OD1 ASP A 425 25.664 49.993 -11.944 1.00 32.67 O ANISOU 1985 OD1 ASP A 425 3305 4511 4598 461 1101 620 O ATOM 1986 OD2 ASP A 425 26.863 50.487 -10.161 1.00 42.95 O ANISOU 1986 OD2 ASP A 425 4458 5797 6062 362 859 627 O ATOM 1987 N ASP A 426 28.155 45.451 -12.035 1.00 32.20 N ANISOU 1987 N ASP A 426 2979 4209 5047 390 1002 928 N ATOM 1988 CA ASP A 426 29.169 44.489 -12.465 1.00 37.30 C ANISOU 1988 CA ASP A 426 3563 4726 5885 387 1062 1033 C ATOM 1989 C ASP A 426 28.664 43.583 -13.583 1.00 39.00 C ANISOU 1989 C ASP A 426 3880 4906 6032 464 1165 1057 C ATOM 1990 O ASP A 426 29.435 42.816 -14.170 1.00 36.35 O ANISOU 1990 O ASP A 426 3533 4445 5832 488 1249 1153 O ATOM 1991 CB ASP A 426 29.684 43.671 -11.278 1.00 36.35 C ANISOU 1991 CB ASP A 426 3311 4671 5829 287 920 1096 C ATOM 1992 CG ASP A 426 30.572 44.492 -10.355 1.00 46.43 C ANISOU 1992 CG ASP A 426 4488 5910 7245 233 814 1084 C ATOM 1993 OD1 ASP A 426 30.512 44.280 -9.126 1.00 45.60 O ANISOU 1993 OD1 ASP A 426 4323 5918 7084 182 652 1073 O ATOM 1994 OD2 ASP A 426 31.332 45.352 -10.865 1.00 45.07 O ANISOU 1994 OD2 ASP A 426 4294 5580 7250 260 890 1087 O ATOM 1995 N LEU A 427 27.371 43.692 -13.889 1.00 30.58 N ANISOU 1995 N LEU A 427 2921 3936 4761 509 1155 975 N ATOM 1996 CA LEU A 427 26.791 42.984 -15.028 1.00 32.23 C ANISOU 1996 CA LEU A 427 3248 4095 4901 605 1227 967 C ATOM 1997 C LEU A 427 26.307 43.991 -16.083 1.00 35.70 C ANISOU 1997 C LEU A 427 3834 4480 5249 732 1348 880 C ATOM 1998 O LEU A 427 25.373 43.718 -16.843 1.00 34.76 O ANISOU 1998 O LEU A 427 3838 4369 4999 816 1359 823 O ATOM 1999 CB LEU A 427 25.654 42.054 -14.560 1.00 30.14 C ANISOU 1999 CB LEU A 427 2974 3967 4513 565 1101 952 C ATOM 2000 CG LEU A 427 26.095 40.914 -13.614 1.00 33.17 C ANISOU 2000 CG LEU A 427 3209 4407 4987 471 1015 1043 C ATOM 2001 CD1 LEU A 427 24.914 40.180 -12.984 1.00 30.68 C ANISOU 2001 CD1 LEU A 427 2854 4224 4578 452 904 1037 C ATOM 2002 CD2 LEU A 427 27.014 39.919 -14.322 1.00 30.28 C ANISOU 2002 CD2 LEU A 427 2834 3912 4758 490 1099 1133 C ATOM 2003 N ALA A 428 26.953 45.156 -16.124 1.00 41.11 N ANISOU 2003 N ALA A 428 4497 5104 6019 755 1438 868 N ATOM 2004 CA ALA A 428 26.485 46.280 -16.947 1.00 42.36 C ANISOU 2004 CA ALA A 428 4767 5240 6087 874 1571 781 C ATOM 2005 C ALA A 428 26.181 45.925 -18.407 1.00 46.11 C ANISOU 2005 C ALA A 428 5411 5606 6504 1058 1701 761 C ATOM 2006 O ALA A 428 25.161 46.351 -18.955 1.00 45.13 O ANISOU 2006 O ALA A 428 5407 5539 6203 1136 1730 664 O ATOM 2007 CB ALA A 428 27.464 47.445 -16.878 1.00 43.67 C ANISOU 2007 CB ALA A 428 4854 5311 6427 894 1677 794 C ATOM 2008 N VAL A 429 27.054 45.141 -19.030 1.00 39.28 N ANISOU 2008 N VAL A 429 4568 4578 5781 1138 1774 859 N ATOM 2009 CA VAL A 429 26.897 44.812 -20.446 1.00 42.96 C ANISOU 2009 CA VAL A 429 5222 4907 6193 1354 1899 851 C ATOM 2010 C VAL A 429 25.649 43.955 -20.676 1.00 45.21 C ANISOU 2010 C VAL A 429 5609 5283 6284 1357 1758 770 C ATOM 2011 O VAL A 429 24.995 44.046 -21.716 1.00 46.66 O ANISOU 2011 O VAL A 429 5969 5420 6341 1529 1808 690 O ATOM 2012 CB VAL A 429 28.176 44.137 -21.025 1.00 47.99 C ANISOU 2012 CB VAL A 429 5876 5328 7030 1451 2019 1006 C ATOM 2013 CG1 VAL A 429 28.447 42.808 -20.339 1.00 40.84 C ANISOU 2013 CG1 VAL A 429 4877 4463 6179 1293 1876 1094 C ATOM 2014 CG2 VAL A 429 28.064 43.956 -22.534 1.00 54.38 C ANISOU 2014 CG2 VAL A 429 6918 5972 7772 1728 2167 1002 C ATOM 2015 N TYR A 430 25.304 43.144 -19.687 1.00 42.54 N ANISOU 2015 N TYR A 430 5154 5069 5939 1180 1579 790 N ATOM 2016 CA TYR A 430 24.118 42.308 -19.781 1.00 44.90 C ANISOU 2016 CA TYR A 430 5507 5439 6112 1172 1433 729 C ATOM 2017 C TYR A 430 22.855 43.094 -19.455 1.00 36.30 C ANISOU 2017 C TYR A 430 4437 4493 4863 1134 1366 624 C ATOM 2018 O TYR A 430 21.796 42.855 -20.030 1.00 36.83 O ANISOU 2018 O TYR A 430 4611 4564 4819 1206 1303 546 O ATOM 2019 CB TYR A 430 24.278 41.067 -18.900 1.00 48.61 C ANISOU 2019 CB TYR A 430 5831 5967 6669 1027 1301 812 C ATOM 2020 CG TYR A 430 25.428 40.231 -19.386 1.00 52.26 C ANISOU 2020 CG TYR A 430 6306 6283 7269 1074 1381 923 C ATOM 2021 CD1 TYR A 430 25.296 39.437 -20.521 1.00 57.54 C ANISOU 2021 CD1 TYR A 430 7134 6822 7908 1224 1400 918 C ATOM 2022 CD2 TYR A 430 26.664 40.276 -18.756 1.00 49.74 C ANISOU 2022 CD2 TYR A 430 5855 5935 7108 982 1440 1039 C ATOM 2023 CE1 TYR A 430 26.355 38.686 -21.001 1.00 51.13 C ANISOU 2023 CE1 TYR A 430 6357 5862 7207 1280 1492 1044 C ATOM 2024 CE2 TYR A 430 27.728 39.530 -19.227 1.00 48.53 C ANISOU 2024 CE2 TYR A 430 5719 5633 7086 1024 1534 1168 C ATOM 2025 CZ TYR A 430 27.568 38.733 -20.349 1.00 51.20 C ANISOU 2025 CZ TYR A 430 6226 5850 7379 1174 1570 1179 C ATOM 2026 OH TYR A 430 28.624 37.985 -20.826 1.00 56.44 O ANISOU 2026 OH TYR A 430 6928 6356 8160 1225 1677 1330 O ATOM 2027 N ARG A 431 22.980 44.047 -18.545 1.00 29.00 N ANISOU 2027 N ARG A 431 3414 3671 3933 1027 1378 628 N ATOM 2028 CA ARG A 431 21.902 44.991 -18.293 1.00 37.70 C ANISOU 2028 CA ARG A 431 4553 4895 4875 1002 1360 549 C ATOM 2029 C ARG A 431 21.503 45.690 -19.596 1.00 40.46 C ANISOU 2029 C ARG A 431 5076 5178 5118 1178 1496 454 C ATOM 2030 O ARG A 431 20.320 45.839 -19.891 1.00 36.89 O ANISOU 2030 O ARG A 431 4712 4782 4522 1206 1450 382 O ATOM 2031 CB ARG A 431 22.344 46.018 -17.251 1.00 36.19 C ANISOU 2031 CB ARG A 431 4256 4791 4703 891 1377 570 C ATOM 2032 CG ARG A 431 21.764 47.410 -17.450 1.00 37.35 C ANISOU 2032 CG ARG A 431 4476 5004 4712 923 1475 491 C ATOM 2033 CD ARG A 431 21.877 48.184 -16.156 1.00 36.31 C ANISOU 2033 CD ARG A 431 4245 4986 4566 789 1417 515 C ATOM 2034 NE ARG A 431 23.172 48.827 -15.985 1.00 43.04 N ANISOU 2034 NE ARG A 431 5009 5762 5582 784 1492 532 N ATOM 2035 CZ ARG A 431 23.780 49.007 -14.816 1.00 39.76 C ANISOU 2035 CZ ARG A 431 4476 5382 5248 674 1388 572 C ATOM 2036 NH1 ARG A 431 23.233 48.565 -13.693 1.00 32.49 N ANISOU 2036 NH1 ARG A 431 3524 4580 4242 578 1222 606 N ATOM 2037 NH2 ARG A 431 24.949 49.630 -14.770 1.00 39.25 N ANISOU 2037 NH2 ARG A 431 4325 5218 5369 680 1449 582 N ATOM 2038 N GLU A 432 22.495 46.093 -20.385 1.00 39.91 N ANISOU 2038 N GLU A 432 5055 4976 5134 1312 1671 465 N ATOM 2039 CA GLU A 432 22.227 46.802 -21.636 1.00 44.15 C ANISOU 2039 CA GLU A 432 5758 5441 5575 1523 1835 381 C ATOM 2040 C GLU A 432 21.630 45.892 -22.708 1.00 44.19 C ANISOU 2040 C GLU A 432 5937 5353 5499 1684 1779 328 C ATOM 2041 O GLU A 432 20.715 46.287 -23.430 1.00 41.78 O ANISOU 2041 O GLU A 432 5771 5064 5039 1802 1800 223 O ATOM 2042 CB GLU A 432 23.486 47.505 -22.131 1.00 41.76 C ANISOU 2042 CB GLU A 432 5446 5000 5422 1653 2059 431 C ATOM 2043 CG GLU A 432 24.006 48.502 -21.106 1.00 48.80 C ANISOU 2043 CG GLU A 432 6165 5970 6407 1504 2089 459 C ATOM 2044 CD GLU A 432 25.164 49.346 -21.611 1.00 57.05 C ANISOU 2044 CD GLU A 432 7174 6862 7641 1643 2319 507 C ATOM 2045 OE1 GLU A 432 25.618 49.133 -22.758 1.00 58.87 O ANISOU 2045 OE1 GLU A 432 7522 6917 7930 1873 2479 540 O ATOM 2046 OE2 GLU A 432 25.619 50.226 -20.850 1.00 54.89 O ANISOU 2046 OE2 GLU A 432 6755 6628 7471 1538 2339 518 O ATOM 2047 N CYS A 433 22.122 44.663 -22.787 1.00 39.78 N ANISOU 2047 N CYS A 433 5372 4699 5042 1686 1697 399 N ATOM 2048 CA CYS A 433 21.568 43.694 -23.722 1.00 41.20 C ANISOU 2048 CA CYS A 433 5714 4782 5159 1831 1605 347 C ATOM 2049 C CYS A 433 20.075 43.519 -23.441 1.00 49.28 C ANISOU 2049 C CYS A 433 6737 5923 6064 1746 1414 255 C ATOM 2050 O CYS A 433 19.240 43.612 -24.349 1.00 42.17 O ANISOU 2050 O CYS A 433 6001 4978 5042 1899 1385 145 O ATOM 2051 CB CYS A 433 22.321 42.361 -23.617 1.00 37.46 C ANISOU 2051 CB CYS A 433 5197 4213 4822 1798 1535 454 C ATOM 2052 SG CYS A 433 21.550 40.955 -24.453 1.00 61.00 S ANISOU 2052 SG CYS A 433 8331 7095 7753 1916 1349 393 S ATOM 2053 N ILE A 434 19.745 43.297 -22.172 1.00 43.06 N ANISOU 2053 N ILE A 434 5766 5272 5324 1518 1288 308 N ATOM 2054 CA ILE A 434 18.362 43.116 -21.757 1.00 38.81 C ANISOU 2054 CA ILE A 434 5198 4827 4721 1432 1120 266 C ATOM 2055 C ILE A 434 17.480 44.304 -22.123 1.00 40.65 C ANISOU 2055 C ILE A 434 5533 5123 4789 1485 1187 175 C ATOM 2056 O ILE A 434 16.395 44.144 -22.672 1.00 44.44 O ANISOU 2056 O ILE A 434 6109 5580 5195 1552 1089 97 O ATOM 2057 CB ILE A 434 18.278 42.869 -20.246 1.00 39.69 C ANISOU 2057 CB ILE A 434 5101 5070 4909 1215 1026 367 C ATOM 2058 CG1 ILE A 434 18.721 41.431 -19.944 1.00 43.28 C ANISOU 2058 CG1 ILE A 434 5453 5473 5518 1170 920 442 C ATOM 2059 CG2 ILE A 434 16.863 43.142 -19.740 1.00 33.36 C ANISOU 2059 CG2 ILE A 434 4278 4365 4032 1143 920 354 C ATOM 2060 CD1 ILE A 434 18.974 41.151 -18.489 1.00 41.66 C ANISOU 2060 CD1 ILE A 434 5045 5383 5400 997 869 550 C ATOM 2061 N ILE A 435 17.958 45.499 -21.815 1.00 37.49 N ANISOU 2061 N ILE A 435 5104 4798 4343 1453 1354 186 N ATOM 2062 CA ILE A 435 17.190 46.700 -22.072 1.00 42.42 C ANISOU 2062 CA ILE A 435 5807 5505 4805 1485 1451 112 C ATOM 2063 C ILE A 435 16.924 46.864 -23.567 1.00 44.23 C ANISOU 2063 C ILE A 435 6243 5627 4936 1732 1534 -5 C ATOM 2064 O ILE A 435 15.783 47.070 -23.985 1.00 42.40 O ANISOU 2064 O ILE A 435 6106 5423 4581 1775 1480 -84 O ATOM 2065 CB ILE A 435 17.916 47.935 -21.540 1.00 41.28 C ANISOU 2065 CB ILE A 435 5588 5442 4656 1425 1628 142 C ATOM 2066 CG1 ILE A 435 17.901 47.937 -20.013 1.00 41.94 C ANISOU 2066 CG1 ILE A 435 5506 5648 4783 1199 1520 237 C ATOM 2067 CG2 ILE A 435 17.271 49.195 -22.081 1.00 48.51 C ANISOU 2067 CG2 ILE A 435 6604 6426 5403 1502 1783 57 C ATOM 2068 CD1 ILE A 435 18.682 49.079 -19.398 1.00 42.84 C ANISOU 2068 CD1 ILE A 435 5538 5824 4915 1135 1649 261 C ATOM 2069 N GLU A 436 17.983 46.753 -24.364 1.00 45.35 N ANISOU 2069 N GLU A 436 6461 5633 5139 1910 1667 -6 N ATOM 2070 CA GLU A 436 17.893 46.900 -25.818 1.00 49.80 C ANISOU 2070 CA GLU A 436 7246 6070 5606 2202 1771 -106 C ATOM 2071 C GLU A 436 17.019 45.839 -26.484 1.00 52.65 C ANISOU 2071 C GLU A 436 7742 6341 5922 2299 1552 -185 C ATOM 2072 O GLU A 436 16.096 46.165 -27.230 1.00 63.44 O ANISOU 2072 O GLU A 436 9255 7701 7147 2432 1532 -303 O ATOM 2073 CB GLU A 436 19.294 46.868 -26.450 1.00 55.02 C ANISOU 2073 CB GLU A 436 7960 6572 6375 2391 1962 -46 C ATOM 2074 CG GLU A 436 20.188 48.042 -26.063 1.00 64.06 C ANISOU 2074 CG GLU A 436 8989 7754 7596 2347 2186 28 C ATOM 2075 CD GLU A 436 21.618 47.900 -26.582 1.00 78.17 C ANISOU 2075 CD GLU A 436 10804 9350 9545 2486 2337 156 C ATOM 2076 OE1 GLU A 436 21.897 46.945 -27.344 1.00 86.50 O ANISOU 2076 OE1 GLU A 436 12000 10250 10615 2660 2310 174 O ATOM 2077 OE2 GLU A 436 22.467 48.746 -26.223 1.00 75.06 O ANISOU 2077 OE2 GLU A 436 10297 8948 9276 2424 2480 250 O ATOM 2078 N LYS A 437 17.306 44.571 -26.209 1.00 48.71 N ANISOU 2078 N LYS A 437 7187 5768 5552 2233 1384 -124 N ATOM 2079 CA LYS A 437 16.702 43.480 -26.966 1.00 54.52 C ANISOU 2079 CA LYS A 437 8058 6375 6281 2361 1179 -199 C ATOM 2080 C LYS A 437 15.456 42.892 -26.313 1.00 58.53 C ANISOU 2080 C LYS A 437 8456 6950 6834 2182 919 -215 C ATOM 2081 O LYS A 437 14.728 42.111 -26.931 1.00 58.17 O ANISOU 2081 O LYS A 437 8509 6796 6798 2282 720 -297 O ATOM 2082 CB LYS A 437 17.730 42.377 -27.222 1.00 58.36 C ANISOU 2082 CB LYS A 437 8572 6716 6888 2433 1161 -122 C ATOM 2083 CG LYS A 437 19.099 42.879 -27.667 1.00 61.38 C ANISOU 2083 CG LYS A 437 9020 7009 7291 2584 1431 -45 C ATOM 2084 CD LYS A 437 20.025 41.709 -27.965 1.00 71.32 C ANISOU 2084 CD LYS A 437 10328 8109 8661 2658 1408 52 C ATOM 2085 CE LYS A 437 21.462 42.156 -28.222 1.00 76.66 C ANISOU 2085 CE LYS A 437 11028 8680 9418 2776 1682 182 C ATOM 2086 NZ LYS A 437 22.387 41.860 -27.090 1.00 72.47 N ANISOU 2086 NZ LYS A 437 10256 8208 9070 2523 1703 340 N ATOM 2087 N CYS A 438 15.198 43.262 -25.066 1.00 50.24 N ANISOU 2087 N CYS A 438 7204 6058 5825 1936 915 -129 N ATOM 2088 CA CYS A 438 14.003 42.766 -24.405 1.00 38.42 C ANISOU 2088 CA CYS A 438 5596 4607 4395 1789 701 -109 C ATOM 2089 C CYS A 438 13.004 43.866 -24.024 1.00 40.49 C ANISOU 2089 C CYS A 438 5845 4997 4543 1704 743 -116 C ATOM 2090 O CYS A 438 11.814 43.752 -24.323 1.00 47.50 O ANISOU 2090 O CYS A 438 6781 5850 5419 1727 602 -169 O ATOM 2091 CB CYS A 438 14.371 41.930 -23.174 1.00 45.73 C ANISOU 2091 CB CYS A 438 6296 5585 5495 1593 620 29 C ATOM 2092 SG CYS A 438 12.932 41.249 -22.312 1.00 61.08 S ANISOU 2092 SG CYS A 438 8080 7554 7575 1451 385 91 S ATOM 2093 N LEU A 439 13.477 44.920 -23.362 1.00 33.42 N ANISOU 2093 N LEU A 439 4885 4238 3574 1605 931 -57 N ATOM 2094 CA LEU A 439 12.564 45.911 -22.781 1.00 36.72 C ANISOU 2094 CA LEU A 439 5275 4792 3887 1491 974 -27 C ATOM 2095 C LEU A 439 12.159 47.005 -23.766 1.00 42.16 C ANISOU 2095 C LEU A 439 6135 5500 4385 1631 1124 -144 C ATOM 2096 O LEU A 439 11.009 47.447 -23.778 1.00 42.91 O ANISOU 2096 O LEU A 439 6267 5642 4395 1597 1089 -156 O ATOM 2097 CB LEU A 439 13.172 46.545 -21.523 1.00 32.05 C ANISOU 2097 CB LEU A 439 4540 4340 3297 1318 1083 89 C ATOM 2098 CG LEU A 439 13.723 45.580 -20.468 1.00 36.66 C ANISOU 2098 CG LEU A 439 4953 4925 4052 1195 971 205 C ATOM 2099 CD1 LEU A 439 14.260 46.326 -19.270 1.00 37.28 C ANISOU 2099 CD1 LEU A 439 4923 5134 4106 1055 1061 298 C ATOM 2100 CD2 LEU A 439 12.665 44.585 -20.044 1.00 32.86 C ANISOU 2100 CD2 LEU A 439 4395 4405 3684 1140 761 266 C ATOM 2101 N MET A 440 13.107 47.443 -24.587 1.00 44.10 N ANISOU 2101 N MET A 440 6481 5701 4574 1801 1307 -216 N ATOM 2102 CA MET A 440 12.865 48.558 -25.491 1.00 41.54 C ANISOU 2102 CA MET A 440 6305 5406 4071 1961 1501 -321 C ATOM 2103 C MET A 440 11.758 48.208 -26.479 1.00 41.46 C ANISOU 2103 C MET A 440 6459 5309 3985 2111 1361 -440 C ATOM 2104 O MET A 440 11.747 47.114 -27.048 1.00 38.80 O ANISOU 2104 O MET A 440 6194 4818 3729 2227 1179 -490 O ATOM 2105 CB MET A 440 14.152 48.959 -26.223 1.00 41.82 C ANISOU 2105 CB MET A 440 6409 5358 4125 2123 1681 -309 C ATOM 2106 CG MET A 440 14.207 50.435 -26.613 1.00 48.30 C ANISOU 2106 CG MET A 440 7268 6211 4872 2109 1798 -224 C ATOM 2107 SD MET A 440 14.180 51.559 -25.194 1.00 55.11 S ANISOU 2107 SD MET A 440 7939 7233 5769 1822 1847 -117 S ATOM 2108 CE MET A 440 15.906 51.519 -24.707 1.00 55.60 C ANISOU 2108 CE MET A 440 7881 7248 5996 1812 1981 -56 C ATOM 2109 N ARG A 441 10.825 49.141 -26.652 1.00 32.29 N ANISOU 2109 N ARG A 441 5347 4233 2690 2079 1400 -446 N ATOM 2110 CA ARG A 441 9.682 48.969 -27.547 1.00 40.24 C ANISOU 2110 CA ARG A 441 6502 5167 3619 2206 1263 -553 C ATOM 2111 C ARG A 441 8.559 48.155 -26.916 1.00 43.64 C ANISOU 2111 C ARG A 441 6848 5570 4163 2064 1013 -529 C ATOM 2112 O ARG A 441 7.481 48.039 -27.493 1.00 45.40 O ANISOU 2112 O ARG A 441 7164 5726 4359 2132 872 -603 O ATOM 2113 CB ARG A 441 10.106 48.363 -28.893 1.00 40.00 C ANISOU 2113 CB ARG A 441 6664 4963 3573 2494 1194 -661 C ATOM 2114 CG ARG A 441 10.920 49.325 -29.753 1.00 53.97 C ANISOU 2114 CG ARG A 441 8529 6732 5244 2616 1364 -569 C ATOM 2115 CD ARG A 441 11.507 48.645 -30.989 1.00 59.46 C ANISOU 2115 CD ARG A 441 9430 7261 5901 2914 1323 -635 C ATOM 2116 NE ARG A 441 12.314 47.482 -30.640 1.00 69.11 N ANISOU 2116 NE ARG A 441 10612 8378 7270 2938 1279 -663 N ATOM 2117 CZ ARG A 441 13.588 47.542 -30.265 1.00 76.30 C ANISOU 2117 CZ ARG A 441 11439 9282 8270 2901 1443 -552 C ATOM 2118 NH1 ARG A 441 14.202 48.718 -30.190 1.00 75.56 N ANISOU 2118 NH1 ARG A 441 11294 9264 8150 2844 1650 -419 N ATOM 2119 NH2 ARG A 441 14.244 46.425 -29.961 1.00 73.35 N ANISOU 2119 NH2 ARG A 441 11023 8801 8046 2924 1389 -568 N ATOM 2120 N ASN A 442 8.807 47.601 -25.729 1.00 39.78 N ANISOU 2120 N ASN A 442 6029 4771 4315 614 535 447 N ATOM 2121 CA ASN A 442 7.774 46.851 -25.010 1.00 36.47 C ANISOU 2121 CA ASN A 442 5473 4383 4001 568 447 382 C ATOM 2122 C ASN A 442 7.408 47.474 -23.659 1.00 38.37 C ANISOU 2122 C ASN A 442 5534 4684 4362 551 426 415 C ATOM 2123 O ASN A 442 6.697 46.859 -22.861 1.00 36.49 O ANISOU 2123 O ASN A 442 5170 4459 4234 527 398 386 O ATOM 2124 CB ASN A 442 8.216 45.405 -24.790 1.00 41.30 C ANISOU 2124 CB ASN A 442 6051 4964 4677 532 558 367 C ATOM 2125 CG ASN A 442 8.481 44.671 -26.086 1.00 46.12 C ANISOU 2125 CG ASN A 442 6840 5506 5180 538 586 313 C ATOM 2126 OD1 ASN A 442 9.601 44.235 -26.344 1.00 46.22 O ANISOU 2126 OD1 ASN A 442 6922 5469 5170 533 745 366 O ATOM 2127 ND2 ASN A 442 7.452 44.535 -26.911 1.00 40.30 N ANISOU 2127 ND2 ASN A 442 6177 4758 4378 548 431 206 N ATOM 2128 N LEU A 443 7.890 48.691 -23.411 1.00 33.42 N ANISOU 2128 N LEU A 443 4894 4083 3721 570 454 471 N ATOM 2129 CA LEU A 443 7.756 49.324 -22.097 1.00 29.21 C ANISOU 2129 CA LEU A 443 4204 3609 3287 551 458 495 C ATOM 2130 C LEU A 443 6.310 49.523 -21.665 1.00 35.20 C ANISOU 2130 C LEU A 443 4880 4378 4116 536 335 456 C ATOM 2131 O LEU A 443 5.957 49.250 -20.515 1.00 37.80 O ANISOU 2131 O LEU A 443 5084 4737 4543 520 349 458 O ATOM 2132 CB LEU A 443 8.479 50.664 -22.083 1.00 31.19 C ANISOU 2132 CB LEU A 443 4456 3868 3525 572 509 538 C ATOM 2133 CG LEU A 443 9.975 50.548 -22.310 1.00 30.29 C ANISOU 2133 CG LEU A 443 4390 3721 3397 589 646 585 C ATOM 2134 CD1 LEU A 443 10.639 51.900 -22.134 1.00 31.86 C ANISOU 2134 CD1 LEU A 443 4549 3916 3642 612 703 613 C ATOM 2135 CD2 LEU A 443 10.571 49.500 -21.350 1.00 31.56 C ANISOU 2135 CD2 LEU A 443 4455 3919 3617 559 714 601 C ATOM 2136 N LEU A 444 5.477 50.006 -22.583 1.00 28.12 N ANISOU 2136 N LEU A 444 4057 3451 3175 551 221 431 N ATOM 2137 CA LEU A 444 4.063 50.202 -22.285 1.00 32.91 C ANISOU 2137 CA LEU A 444 4584 4044 3876 535 99 403 C ATOM 2138 C LEU A 444 3.416 48.903 -21.828 1.00 32.49 C ANISOU 2138 C LEU A 444 4456 3958 3932 517 78 351 C ATOM 2139 O LEU A 444 2.777 48.874 -20.779 1.00 33.37 O ANISOU 2139 O LEU A 444 4442 4061 4176 505 85 360 O ATOM 2140 CB LEU A 444 3.292 50.783 -23.480 1.00 32.84 C ANISOU 2140 CB LEU A 444 4669 4011 3797 562 -37 388 C ATOM 2141 CG LEU A 444 1.785 50.998 -23.254 1.00 35.97 C ANISOU 2141 CG LEU A 444 4975 4374 4319 542 -175 367 C ATOM 2142 CD1 LEU A 444 1.510 51.791 -21.969 1.00 30.45 C ANISOU 2142 CD1 LEU A 444 4137 3681 3752 512 -115 417 C ATOM 2143 CD2 LEU A 444 1.106 51.670 -24.448 1.00 28.82 C ANISOU 2143 CD2 LEU A 444 4156 3462 3332 578 -316 370 C ATOM 2144 N SER A 445 3.585 47.828 -22.595 1.00 32.12 N ANISOU 2144 N SER A 445 4482 3879 3842 520 74 297 N ATOM 2145 CA SER A 445 2.934 46.571 -22.232 1.00 37.88 C ANISOU 2145 CA SER A 445 5120 4559 4712 507 72 239 C ATOM 2146 C SER A 445 3.533 45.941 -20.971 1.00 32.56 C ANISOU 2146 C SER A 445 4332 3913 4125 509 234 294 C ATOM 2147 O SER A 445 2.801 45.442 -20.121 1.00 39.02 O ANISOU 2147 O SER A 445 5025 4700 5103 518 254 291 O ATOM 2148 CB SER A 445 2.916 45.569 -23.401 1.00 36.42 C ANISOU 2148 CB SER A 445 5034 4329 4474 504 29 146 C ATOM 2149 OG SER A 445 4.220 45.179 -23.771 1.00 45.66 O ANISOU 2149 OG SER A 445 6303 5517 5528 505 162 176 O ATOM 2150 N LEU A 446 4.858 45.970 -20.855 1.00 32.11 N ANISOU 2150 N LEU A 446 4317 3909 3974 511 353 353 N ATOM 2151 CA LEU A 446 5.547 45.352 -19.719 1.00 28.30 C ANISOU 2151 CA LEU A 446 3730 3471 3550 522 499 416 C ATOM 2152 C LEU A 446 5.197 46.075 -18.409 1.00 31.55 C ANISOU 2152 C LEU A 446 4033 3936 4018 541 500 460 C ATOM 2153 O LEU A 446 5.058 45.457 -17.345 1.00 32.89 O ANISOU 2153 O LEU A 446 4094 4126 4278 572 581 495 O ATOM 2154 CB LEU A 446 7.062 45.342 -19.962 1.00 27.74 C ANISOU 2154 CB LEU A 446 3727 3435 3378 518 607 472 C ATOM 2155 CG LEU A 446 7.596 44.374 -21.031 1.00 34.10 C ANISOU 2155 CG LEU A 446 4634 4179 4143 502 670 449 C ATOM 2156 CD1 LEU A 446 9.109 44.453 -21.140 1.00 31.82 C ANISOU 2156 CD1 LEU A 446 4398 3901 3791 501 796 527 C ATOM 2157 CD2 LEU A 446 7.163 42.946 -20.724 1.00 38.72 C ANISOU 2157 CD2 LEU A 446 5125 4728 4859 500 742 424 C ATOM 2158 N SER A 447 5.040 47.390 -18.503 1.00 31.02 N ANISOU 2158 N SER A 447 3999 3888 3900 528 423 458 N ATOM 2159 CA SER A 447 4.671 48.211 -17.356 1.00 30.13 C ANISOU 2159 CA SER A 447 3799 3816 3833 536 423 484 C ATOM 2160 C SER A 447 3.301 47.819 -16.819 1.00 32.24 C ANISOU 2160 C SER A 447 3986 4016 4248 551 392 471 C ATOM 2161 O SER A 447 2.991 48.092 -15.663 1.00 32.63 O ANISOU 2161 O SER A 447 3958 4086 4352 574 436 502 O ATOM 2162 CB SER A 447 4.669 49.700 -17.741 1.00 34.70 C ANISOU 2162 CB SER A 447 4423 4404 4358 513 359 478 C ATOM 2163 OG SER A 447 5.973 50.140 -18.091 1.00 34.80 O ANISOU 2163 OG SER A 447 4489 4459 4273 512 414 496 O ATOM 2164 N GLN A 448 2.484 47.182 -17.658 1.00 29.13 N ANISOU 2164 N GLN A 448 3610 3531 3927 544 319 419 N ATOM 2165 CA GLN A 448 1.163 46.719 -17.233 1.00 35.03 C ANISOU 2165 CA GLN A 448 4264 4180 4864 562 295 402 C ATOM 2166 C GLN A 448 1.133 45.254 -16.779 1.00 35.59 C ANISOU 2166 C GLN A 448 4253 4211 5058 605 410 403 C ATOM 2167 O GLN A 448 0.060 44.695 -16.534 1.00 37.92 O ANISOU 2167 O GLN A 448 4461 4396 5551 631 409 381 O ATOM 2168 CB GLN A 448 0.130 46.940 -18.343 1.00 30.75 C ANISOU 2168 CB GLN A 448 3759 3548 4376 533 130 334 C ATOM 2169 CG GLN A 448 0.009 48.391 -18.779 1.00 36.73 C ANISOU 2169 CG GLN A 448 4579 4335 5042 505 34 353 C ATOM 2170 CD GLN A 448 -0.871 48.546 -19.999 1.00 38.42 C ANISOU 2170 CD GLN A 448 4841 4485 5270 491 -140 296 C ATOM 2171 OE1 GLN A 448 -2.100 48.480 -19.911 1.00 40.17 O ANISOU 2171 OE1 GLN A 448 4986 4609 5668 487 -224 276 O ATOM 2172 NE2 GLN A 448 -0.246 48.739 -21.149 1.00 32.90 N ANISOU 2172 NE2 GLN A 448 4272 3838 4392 491 -194 274 N ATOM 2173 N GLU A 449 2.303 44.634 -16.668 1.00 37.28 N ANISOU 2173 N GLU A 449 4480 4501 5181 617 522 437 N ATOM 2174 CA GLU A 449 2.395 43.253 -16.196 1.00 36.38 C ANISOU 2174 CA GLU A 449 4275 4361 5188 664 666 461 C ATOM 2175 C GLU A 449 2.681 43.243 -14.709 1.00 37.92 C ANISOU 2175 C GLU A 449 4387 4628 5391 736 797 562 C ATOM 2176 O GLU A 449 3.465 44.057 -14.223 1.00 36.24 O ANISOU 2176 O GLU A 449 4210 4530 5030 733 795 605 O ATOM 2177 CB GLU A 449 3.549 42.543 -16.897 1.00 36.55 C ANISOU 2177 CB GLU A 449 4353 4421 5112 639 735 459 C ATOM 2178 CG GLU A 449 3.455 42.556 -18.395 1.00 46.88 C ANISOU 2178 CG GLU A 449 5778 5675 6359 580 619 361 C ATOM 2179 CD GLU A 449 3.024 41.231 -18.948 1.00 54.23 C ANISOU 2179 CD GLU A 449 6666 6508 7431 575 659 282 C ATOM 2180 OE1 GLU A 449 3.078 40.237 -18.198 1.00 57.36 O ANISOU 2180 OE1 GLU A 449 6939 6885 7971 617 820 327 O ATOM 2181 OE2 GLU A 449 2.646 41.181 -20.135 1.00 63.65 O ANISOU 2181 OE2 GLU A 449 7946 7647 8592 537 536 174 O ATOM 2182 N LYS A 450 2.078 42.306 -13.989 1.00 34.86 N ANISOU 2182 N LYS A 450 3887 4176 5183 811 917 597 N ATOM 2183 CA LYS A 450 2.316 42.196 -12.558 1.00 35.08 C ANISOU 2183 CA LYS A 450 3846 4278 5204 907 1055 704 C ATOM 2184 C LYS A 450 3.805 41.983 -12.250 1.00 37.53 C ANISOU 2184 C LYS A 450 4171 4745 5345 919 1135 776 C ATOM 2185 O LYS A 450 4.361 42.608 -11.354 1.00 31.45 O ANISOU 2185 O LYS A 450 3408 4097 4444 954 1143 830 O ATOM 2186 CB LYS A 450 1.495 41.051 -11.962 1.00 35.16 C ANISOU 2186 CB LYS A 450 3730 4174 5455 1006 1210 744 C ATOM 2187 CG LYS A 450 1.689 40.875 -10.461 1.00 37.18 C ANISOU 2187 CG LYS A 450 3927 4508 5693 1137 1372 872 C ATOM 2188 CD LYS A 450 0.774 39.795 -9.896 1.00 45.36 C ANISOU 2188 CD LYS A 450 4834 5401 7000 1256 1551 923 C ATOM 2189 CE LYS A 450 1.047 39.553 -8.421 1.00 42.63 C ANISOU 2189 CE LYS A 450 4445 5147 6606 1414 1732 1069 C ATOM 2190 NZ LYS A 450 0.540 40.663 -7.574 1.00 53.42 N ANISOU 2190 NZ LYS A 450 5876 6530 7893 1448 1679 1085 N ATOM 2191 N PHE A 451 4.453 41.097 -12.993 1.00 29.33 N ANISOU 2191 N PHE A 451 3132 3696 4318 889 1194 772 N ATOM 2192 CA PHE A 451 5.823 40.761 -12.669 1.00 32.32 C ANISOU 2192 CA PHE A 451 3501 4198 4582 905 1290 859 C ATOM 2193 C PHE A 451 6.820 41.664 -13.398 1.00 35.45 C ANISOU 2193 C PHE A 451 4011 4655 4804 816 1179 825 C ATOM 2194 O PHE A 451 7.750 42.183 -12.782 1.00 32.53 O ANISOU 2194 O PHE A 451 3641 4404 4314 831 1179 878 O ATOM 2195 CB PHE A 451 6.072 39.259 -12.881 1.00 35.17 C ANISOU 2195 CB PHE A 451 3778 4508 5076 932 1465 904 C ATOM 2196 CG PHE A 451 5.074 38.385 -12.146 1.00 37.35 C ANISOU 2196 CG PHE A 451 3924 4704 5564 1037 1603 943 C ATOM 2197 CD1 PHE A 451 4.996 38.422 -10.762 1.00 33.63 C ANISOU 2197 CD1 PHE A 451 3386 4312 5081 1162 1697 1054 C ATOM 2198 CD2 PHE A 451 4.197 37.558 -12.839 1.00 38.25 C ANISOU 2198 CD2 PHE A 451 3984 4655 5896 1021 1640 861 C ATOM 2199 CE1 PHE A 451 4.076 37.643 -10.078 1.00 41.95 C ANISOU 2199 CE1 PHE A 451 4324 5272 6344 1281 1852 1105 C ATOM 2200 CE2 PHE A 451 3.276 36.774 -12.164 1.00 42.73 C ANISOU 2200 CE2 PHE A 451 4414 5121 6701 1127 1786 896 C ATOM 2201 CZ PHE A 451 3.215 36.817 -10.778 1.00 45.61 C ANISOU 2201 CZ PHE A 451 4717 5553 7061 1263 1904 1028 C ATOM 2202 N ALA A 452 6.602 41.891 -14.691 1.00 26.63 N ANISOU 2202 N ALA A 452 2988 3450 3678 735 1083 732 N ATOM 2203 CA ALA A 452 7.574 42.639 -15.494 1.00 24.14 C ANISOU 2203 CA ALA A 452 2786 3164 3220 670 1016 714 C ATOM 2204 C ALA A 452 7.650 44.115 -15.115 1.00 27.62 C ANISOU 2204 C ALA A 452 3261 3672 3563 660 907 699 C ATOM 2205 O ALA A 452 8.653 44.771 -15.387 1.00 29.71 O ANISOU 2205 O ALA A 452 3577 3977 3733 632 890 707 O ATOM 2206 CB ALA A 452 7.290 42.482 -16.977 1.00 22.60 C ANISOU 2206 CB ALA A 452 2701 2865 3023 609 953 626 C ATOM 2207 N SER A 453 6.600 44.637 -14.478 1.00 29.94 N ANISOU 2207 N SER A 453 3515 3959 3901 684 849 676 N ATOM 2208 CA SER A 453 6.591 46.053 -14.099 1.00 28.37 C ANISOU 2208 CA SER A 453 3337 3812 3629 668 762 653 C ATOM 2209 C SER A 453 7.756 46.376 -13.167 1.00 26.66 C ANISOU 2209 C SER A 453 3080 3727 3323 694 807 698 C ATOM 2210 O SER A 453 8.307 47.469 -13.216 1.00 30.52 O ANISOU 2210 O SER A 453 3595 4256 3746 661 751 666 O ATOM 2211 CB SER A 453 5.243 46.496 -13.488 1.00 21.64 C ANISOU 2211 CB SER A 453 2448 2916 2860 688 720 632 C ATOM 2212 OG SER A 453 4.861 45.662 -12.409 1.00 34.16 O ANISOU 2212 OG SER A 453 3947 4512 4522 770 822 689 O ATOM 2213 N HIS A 454 8.144 45.416 -12.335 1.00 23.72 N ANISOU 2213 N HIS A 454 2632 3419 2960 760 909 772 N ATOM 2214 CA HIS A 454 9.295 45.604 -11.454 1.00 28.13 C ANISOU 2214 CA HIS A 454 3143 4115 3430 794 935 818 C ATOM 2215 C HIS A 454 10.599 45.656 -12.238 1.00 32.28 C ANISOU 2215 C HIS A 454 3703 4638 3924 741 940 828 C ATOM 2216 O HIS A 454 11.521 46.395 -11.888 1.00 33.62 O ANISOU 2216 O HIS A 454 3854 4883 4038 733 901 816 O ATOM 2217 CB HIS A 454 9.345 44.504 -10.395 1.00 32.14 C ANISOU 2217 CB HIS A 454 3561 4697 3953 896 1052 917 C ATOM 2218 CG HIS A 454 8.148 44.493 -9.499 1.00 32.24 C ANISOU 2218 CG HIS A 454 3544 4701 4005 971 1074 923 C ATOM 2219 ND1 HIS A 454 8.043 45.300 -8.386 1.00 31.41 N ANISOU 2219 ND1 HIS A 454 3431 4693 3809 1019 1035 909 N ATOM 2220 CD2 HIS A 454 6.990 43.793 -9.565 1.00 32.63 C ANISOU 2220 CD2 HIS A 454 3570 4636 4191 1009 1140 937 C ATOM 2221 CE1 HIS A 454 6.877 45.090 -7.799 1.00 28.97 C ANISOU 2221 CE1 HIS A 454 3109 4326 3573 1088 1090 929 C ATOM 2222 NE2 HIS A 454 6.221 44.176 -8.495 1.00 25.70 N ANISOU 2222 NE2 HIS A 454 2676 3778 3312 1085 1155 949 N ATOM 2223 N VAL A 455 10.670 44.878 -13.311 1.00 29.77 N ANISOU 2223 N VAL A 455 3434 4221 3656 707 993 842 N ATOM 2224 CA VAL A 455 11.854 44.871 -14.153 1.00 33.10 C ANISOU 2224 CA VAL A 455 3909 4605 4064 661 1025 862 C ATOM 2225 C VAL A 455 12.003 46.215 -14.856 1.00 33.41 C ANISOU 2225 C VAL A 455 4031 4600 4064 614 932 788 C ATOM 2226 O VAL A 455 13.108 46.755 -14.944 1.00 32.93 O ANISOU 2226 O VAL A 455 3969 4547 3995 601 940 800 O ATOM 2227 CB VAL A 455 11.819 43.717 -15.165 1.00 32.67 C ANISOU 2227 CB VAL A 455 3904 4443 4065 636 1117 884 C ATOM 2228 CG1 VAL A 455 13.029 43.781 -16.094 1.00 30.08 C ANISOU 2228 CG1 VAL A 455 3655 4049 3723 592 1168 911 C ATOM 2229 CG2 VAL A 455 11.770 42.384 -14.426 1.00 24.30 C ANISOU 2229 CG2 VAL A 455 2735 3421 3077 690 1246 970 C ATOM 2230 N VAL A 456 10.883 46.760 -15.329 1.00 32.34 N ANISOU 2230 N VAL A 456 3952 4411 3926 596 852 720 N ATOM 2231 CA VAL A 456 10.873 48.058 -16.001 1.00 32.24 C ANISOU 2231 CA VAL A 456 4009 4356 3886 565 780 664 C ATOM 2232 C VAL A 456 11.374 49.165 -15.065 1.00 31.74 C ANISOU 2232 C VAL A 456 3867 4377 3815 570 749 639 C ATOM 2233 O VAL A 456 12.167 50.021 -15.465 1.00 27.43 O ANISOU 2233 O VAL A 456 3338 3804 3279 554 752 621 O ATOM 2234 CB VAL A 456 9.464 48.417 -16.546 1.00 32.18 C ANISOU 2234 CB VAL A 456 4053 4288 3886 551 693 609 C ATOM 2235 CG1 VAL A 456 9.441 49.847 -17.091 1.00 26.26 C ANISOU 2235 CG1 VAL A 456 3351 3510 3115 533 638 572 C ATOM 2236 CG2 VAL A 456 9.024 47.423 -17.621 1.00 29.35 C ANISOU 2236 CG2 VAL A 456 3778 3842 3533 543 699 601 C ATOM 2237 N GLU A 457 10.916 49.144 -13.818 1.00 21.59 N ANISOU 2237 N GLU A 457 2496 3185 2522 599 729 633 N ATOM 2238 CA GLU A 457 11.407 50.095 -12.827 1.00 26.52 C ANISOU 2238 CA GLU A 457 3045 3904 3127 605 694 590 C ATOM 2239 C GLU A 457 12.932 50.062 -12.695 1.00 30.90 C ANISOU 2239 C GLU A 457 3553 4500 3686 610 723 611 C ATOM 2240 O GLU A 457 13.593 51.108 -12.752 1.00 28.23 O ANISOU 2240 O GLU A 457 3188 4155 3382 587 698 553 O ATOM 2241 CB GLU A 457 10.761 49.835 -11.468 1.00 27.01 C ANISOU 2241 CB GLU A 457 3043 4067 3155 656 687 595 C ATOM 2242 CG GLU A 457 9.295 50.230 -11.424 1.00 39.41 C ANISOU 2242 CG GLU A 457 4641 5578 4756 647 657 563 C ATOM 2243 CD GLU A 457 8.700 50.047 -10.045 1.00 40.87 C ANISOU 2243 CD GLU A 457 4775 5841 4912 711 675 575 C ATOM 2244 OE1 GLU A 457 9.177 50.720 -9.118 1.00 36.05 O ANISOU 2244 OE1 GLU A 457 4124 5335 4238 727 651 531 O ATOM 2245 OE2 GLU A 457 7.765 49.232 -9.892 1.00 35.65 O ANISOU 2245 OE2 GLU A 457 4117 5130 4300 754 720 625 O ATOM 2246 N LYS A 458 13.474 48.857 -12.521 1.00 27.65 N ANISOU 2246 N LYS A 458 3118 4119 3269 640 786 697 N ATOM 2247 CA LYS A 458 14.915 48.643 -12.419 1.00 30.77 C ANISOU 2247 CA LYS A 458 3460 4539 3693 645 820 742 C ATOM 2248 C LYS A 458 15.663 49.198 -13.618 1.00 32.87 C ANISOU 2248 C LYS A 458 3789 4668 4031 601 852 730 C ATOM 2249 O LYS A 458 16.709 49.839 -13.473 1.00 34.28 O ANISOU 2249 O LYS A 458 3909 4844 4272 596 842 708 O ATOM 2250 CB LYS A 458 15.232 47.146 -12.296 1.00 32.86 C ANISOU 2250 CB LYS A 458 3699 4823 3962 678 916 861 C ATOM 2251 CG LYS A 458 14.765 46.505 -11.009 1.00 38.61 C ANISOU 2251 CG LYS A 458 4347 5692 4631 754 920 904 C ATOM 2252 CD LYS A 458 15.196 47.308 -9.798 1.00 40.59 C ANISOU 2252 CD LYS A 458 4516 6091 4815 791 826 852 C ATOM 2253 CE LYS A 458 14.957 46.508 -8.521 1.00 51.57 C ANISOU 2253 CE LYS A 458 5837 7631 6125 894 854 928 C ATOM 2254 NZ LYS A 458 15.331 47.300 -7.329 1.00 59.12 N ANISOU 2254 NZ LYS A 458 6732 8746 6985 939 747 859 N ATOM 2255 N ALA A 459 15.133 48.923 -14.803 1.00 30.54 N ANISOU 2255 N ALA A 459 3613 4254 3736 579 893 745 N ATOM 2256 CA ALA A 459 15.715 49.432 -16.037 1.00 30.69 C ANISOU 2256 CA ALA A 459 3725 4133 3804 560 942 746 C ATOM 2257 C ALA A 459 15.787 50.962 -16.029 1.00 31.55 C ANISOU 2257 C ALA A 459 3807 4226 3955 555 894 664 C ATOM 2258 O ALA A 459 16.807 51.539 -16.390 1.00 29.62 O ANISOU 2258 O ALA A 459 3548 3903 3803 559 944 666 O ATOM 2259 CB ALA A 459 14.928 48.933 -17.243 1.00 25.30 C ANISOU 2259 CB ALA A 459 3187 3352 3074 550 967 757 C ATOM 2260 N PHE A 460 14.704 51.622 -15.631 1.00 28.81 N ANISOU 2260 N PHE A 460 3443 3934 3568 548 815 597 N ATOM 2261 CA PHE A 460 14.732 53.084 -15.525 1.00 31.73 C ANISOU 2261 CA PHE A 460 3764 4292 3998 539 790 516 C ATOM 2262 C PHE A 460 15.804 53.541 -14.527 1.00 34.08 C ANISOU 2262 C PHE A 460 3923 4660 4367 541 774 466 C ATOM 2263 O PHE A 460 16.533 54.488 -14.790 1.00 31.20 O ANISOU 2263 O PHE A 460 3512 4225 4117 539 807 422 O ATOM 2264 CB PHE A 460 13.361 53.642 -15.108 1.00 29.11 C ANISOU 2264 CB PHE A 460 3425 4011 3625 524 720 462 C ATOM 2265 CG PHE A 460 12.450 53.960 -16.262 1.00 33.00 C ANISOU 2265 CG PHE A 460 4027 4408 4104 520 720 478 C ATOM 2266 CD1 PHE A 460 11.313 53.194 -16.501 1.00 30.94 C ANISOU 2266 CD1 PHE A 460 3831 4146 3781 518 676 503 C ATOM 2267 CD2 PHE A 460 12.726 55.024 -17.106 1.00 26.27 C ANISOU 2267 CD2 PHE A 460 3202 3467 3314 529 768 469 C ATOM 2268 CE1 PHE A 460 10.466 53.483 -17.572 1.00 27.62 C ANISOU 2268 CE1 PHE A 460 3505 3648 3342 519 649 512 C ATOM 2269 CE2 PHE A 460 11.885 55.322 -18.176 1.00 29.52 C ANISOU 2269 CE2 PHE A 460 3716 3808 3693 542 761 497 C ATOM 2270 CZ PHE A 460 10.750 54.551 -18.405 1.00 27.03 C ANISOU 2270 CZ PHE A 460 3469 3505 3297 534 687 514 C ATOM 2271 N LEU A 461 15.889 52.855 -13.387 1.00 31.10 N ANISOU 2271 N LEU A 461 3473 4418 3928 554 725 472 N ATOM 2272 CA LEU A 461 16.758 53.268 -12.290 1.00 31.32 C ANISOU 2272 CA LEU A 461 3365 4546 3989 564 671 407 C ATOM 2273 C LEU A 461 18.226 53.094 -12.630 1.00 38.07 C ANISOU 2273 C LEU A 461 4172 5332 4963 569 718 447 C ATOM 2274 O LEU A 461 19.068 53.852 -12.148 1.00 39.77 O ANISOU 2274 O LEU A 461 4271 5562 5278 566 679 364 O ATOM 2275 CB LEU A 461 16.427 52.493 -11.001 1.00 35.68 C ANISOU 2275 CB LEU A 461 3870 5273 4416 602 612 425 C ATOM 2276 CG LEU A 461 15.147 52.886 -10.242 1.00 39.07 C ANISOU 2276 CG LEU A 461 4309 5781 4753 608 562 363 C ATOM 2277 CD1 LEU A 461 14.666 51.764 -9.296 1.00 33.62 C ANISOU 2277 CD1 LEU A 461 3617 5214 3943 673 560 437 C ATOM 2278 CD2 LEU A 461 15.347 54.191 -9.470 1.00 32.25 C ANISOU 2278 CD2 LEU A 461 3359 4979 3915 590 495 216 C ATOM 2279 N HIS A 462 18.529 52.105 -13.470 1.00 32.81 N ANISOU 2279 N HIS A 462 3589 4575 4304 574 806 567 N ATOM 2280 CA HIS A 462 19.915 51.729 -13.721 1.00 30.86 C ANISOU 2280 CA HIS A 462 3297 4250 4179 579 869 634 C ATOM 2281 C HIS A 462 20.412 51.878 -15.161 1.00 37.28 C ANISOU 2281 C HIS A 462 4216 4845 5104 575 999 691 C ATOM 2282 O HIS A 462 21.588 51.673 -15.421 1.00 40.91 O ANISOU 2282 O HIS A 462 4640 5203 5699 580 1071 750 O ATOM 2283 CB HIS A 462 20.164 50.297 -13.238 1.00 34.35 C ANISOU 2283 CB HIS A 462 3717 4777 4557 597 889 751 C ATOM 2284 CG HIS A 462 19.918 50.112 -11.774 1.00 34.95 C ANISOU 2284 CG HIS A 462 3686 5066 4527 631 781 719 C ATOM 2285 ND1 HIS A 462 20.875 50.381 -10.818 1.00 34.19 N ANISOU 2285 ND1 HIS A 462 3447 5070 4472 653 699 682 N ATOM 2286 CD2 HIS A 462 18.813 49.710 -11.101 1.00 29.73 C ANISOU 2286 CD2 HIS A 462 3044 4530 3721 660 744 717 C ATOM 2287 CE1 HIS A 462 20.375 50.137 -9.619 1.00 34.46 C ANISOU 2287 CE1 HIS A 462 3433 5301 4360 700 614 662 C ATOM 2288 NE2 HIS A 462 19.125 49.733 -9.765 1.00 32.59 N ANISOU 2288 NE2 HIS A 462 3293 5071 4017 707 653 689 N ATOM 2289 N ALA A 463 19.535 52.214 -16.097 1.00 36.96 N ANISOU 2289 N ALA A 463 4307 4727 5008 574 1033 681 N ATOM 2290 CA ALA A 463 19.966 52.401 -17.481 1.00 35.66 C ANISOU 2290 CA ALA A 463 4266 4363 4920 593 1162 737 C ATOM 2291 C ALA A 463 21.030 53.497 -17.598 1.00 40.90 C ANISOU 2291 C ALA A 463 4842 4907 5793 614 1220 701 C ATOM 2292 O ALA A 463 20.942 54.534 -16.932 1.00 41.19 O ANISOU 2292 O ALA A 463 4755 5002 5891 609 1150 590 O ATOM 2293 CB ALA A 463 18.770 52.739 -18.373 1.00 29.12 C ANISOU 2293 CB ALA A 463 3583 3502 3980 602 1160 721 C ATOM 2294 N PRO A 464 22.045 53.267 -18.448 1.00 34.00 N ANISOU 2294 N PRO A 464 4024 3846 5047 641 1362 791 N ATOM 2295 CA PRO A 464 22.956 54.342 -18.867 1.00 43.05 C ANISOU 2295 CA PRO A 464 5113 4817 6425 682 1462 770 C ATOM 2296 C PRO A 464 22.161 55.445 -19.557 1.00 42.25 C ANISOU 2296 C PRO A 464 5084 4667 6302 720 1497 722 C ATOM 2297 O PRO A 464 21.154 55.164 -20.211 1.00 46.18 O ANISOU 2297 O PRO A 464 5741 5194 6613 728 1490 754 O ATOM 2298 CB PRO A 464 23.877 53.668 -19.902 1.00 37.28 C ANISOU 2298 CB PRO A 464 4504 3874 5788 714 1641 910 C ATOM 2299 CG PRO A 464 23.681 52.230 -19.742 1.00 38.85 C ANISOU 2299 CG PRO A 464 4766 4160 5836 671 1617 988 C ATOM 2300 CD PRO A 464 22.331 51.994 -19.123 1.00 33.14 C ANISOU 2300 CD PRO A 464 4045 3659 4888 638 1461 918 C ATOM 2301 N LEU A 465 22.626 56.678 -19.415 1.00 43.30 N ANISOU 2301 N LEU A 465 5088 4724 6641 746 1538 647 N ATOM 2302 CA LEU A 465 21.945 57.861 -19.929 1.00 47.03 C ANISOU 2302 CA LEU A 465 5581 5153 7133 787 1589 603 C ATOM 2303 C LEU A 465 21.345 57.732 -21.332 1.00 48.26 C ANISOU 2303 C LEU A 465 5968 5213 7155 853 1694 712 C ATOM 2304 O LEU A 465 20.206 58.147 -21.562 1.00 42.39 O ANISOU 2304 O LEU A 465 5283 4548 6276 858 1645 691 O ATOM 2305 CB LEU A 465 22.883 59.066 -19.865 1.00 56.39 C ANISOU 2305 CB LEU A 465 6601 6190 8635 828 1696 539 C ATOM 2306 CG LEU A 465 22.717 59.959 -18.633 1.00 63.95 C ANISOU 2306 CG LEU A 465 7336 7279 9684 772 1576 364 C ATOM 2307 CD1 LEU A 465 21.434 60.752 -18.760 1.00 69.43 C ANISOU 2307 CD1 LEU A 465 8062 8049 10269 767 1563 322 C ATOM 2308 CD2 LEU A 465 22.723 59.158 -17.332 1.00 59.58 C ANISOU 2308 CD2 LEU A 465 6698 6936 9003 694 1378 300 C ATOM 2309 N GLU A 466 22.099 57.167 -22.267 1.00 44.72 N ANISOU 2309 N GLU A 466 5655 4593 6743 908 1838 827 N ATOM 2310 CA GLU A 466 21.628 57.102 -23.647 1.00 47.12 C ANISOU 2310 CA GLU A 466 6194 4801 6910 990 1944 923 C ATOM 2311 C GLU A 466 20.407 56.202 -23.778 1.00 43.19 C ANISOU 2311 C GLU A 466 5834 4464 6111 944 1802 923 C ATOM 2312 O GLU A 466 19.447 56.549 -24.468 1.00 51.48 O ANISOU 2312 O GLU A 466 7001 5542 7016 986 1782 931 O ATOM 2313 CB GLU A 466 22.739 56.661 -24.607 1.00 53.38 C ANISOU 2313 CB GLU A 466 7119 5360 7805 1064 2147 1046 C ATOM 2314 CG GLU A 466 23.840 57.707 -24.816 1.00 69.63 C ANISOU 2314 CG GLU A 466 9069 7195 10190 1150 2336 1065 C ATOM 2315 CD GLU A 466 23.317 59.051 -25.325 1.00 83.22 C ANISOU 2315 CD GLU A 466 10783 8875 11960 1244 2419 1050 C ATOM 2316 OE1 GLU A 466 22.207 59.093 -25.906 1.00 92.93 O ANISOU 2316 OE1 GLU A 466 12162 10201 12945 1273 2369 1071 O ATOM 2317 OE2 GLU A 466 24.023 60.069 -25.146 1.00 78.88 O ANISOU 2317 OE2 GLU A 466 10067 8191 11714 1293 2539 1019 O ATOM 2318 N LEU A 467 20.443 55.048 -23.118 1.00 38.08 N ANISOU 2318 N LEU A 467 5161 3918 5389 862 1708 916 N ATOM 2319 CA LEU A 467 19.286 54.164 -23.101 1.00 35.50 C ANISOU 2319 CA LEU A 467 4926 3736 4827 815 1577 900 C ATOM 2320 C LEU A 467 18.142 54.790 -22.316 1.00 37.19 C ANISOU 2320 C LEU A 467 5032 4116 4983 775 1422 805 C ATOM 2321 O LEU A 467 16.983 54.689 -22.710 1.00 43.54 O ANISOU 2321 O LEU A 467 5930 4983 5632 776 1341 793 O ATOM 2322 CB LEU A 467 19.647 52.808 -22.504 1.00 38.72 C ANISOU 2322 CB LEU A 467 5302 4202 5210 748 1548 925 C ATOM 2323 CG LEU A 467 20.640 52.022 -23.352 1.00 50.38 C ANISOU 2323 CG LEU A 467 6906 5505 6730 773 1714 1030 C ATOM 2324 CD1 LEU A 467 20.972 50.695 -22.686 1.00 50.77 C ANISOU 2324 CD1 LEU A 467 6894 5619 6777 704 1700 1066 C ATOM 2325 CD2 LEU A 467 20.058 51.816 -24.746 1.00 47.61 C ANISOU 2325 CD2 LEU A 467 6802 5075 6213 828 1770 1063 C ATOM 2326 N LEU A 468 18.473 55.441 -21.204 1.00 34.61 N ANISOU 2326 N LEU A 468 4509 3853 4790 742 1379 733 N ATOM 2327 CA LEU A 468 17.459 56.070 -20.375 1.00 32.59 C ANISOU 2327 CA LEU A 468 4149 3739 4494 701 1253 642 C ATOM 2328 C LEU A 468 16.656 57.070 -21.212 1.00 37.02 C ANISOU 2328 C LEU A 468 4780 4252 5034 748 1285 649 C ATOM 2329 O LEU A 468 15.425 57.144 -21.109 1.00 32.59 O ANISOU 2329 O LEU A 468 4239 3782 4361 723 1184 625 O ATOM 2330 CB LEU A 468 18.085 56.752 -19.154 1.00 29.26 C ANISOU 2330 CB LEU A 468 3516 3373 4228 668 1222 550 C ATOM 2331 CG LEU A 468 17.097 57.561 -18.302 1.00 32.67 C ANISOU 2331 CG LEU A 468 3847 3930 4637 627 1123 449 C ATOM 2332 CD1 LEU A 468 15.969 56.671 -17.791 1.00 32.98 C ANISOU 2332 CD1 LEU A 468 3934 4109 4488 587 999 452 C ATOM 2333 CD2 LEU A 468 17.788 58.272 -17.141 1.00 39.62 C ANISOU 2333 CD2 LEU A 468 4527 4862 5665 599 1093 333 C ATOM 2334 N ALA A 469 17.363 57.813 -22.058 1.00 33.42 N ANISOU 2334 N ALA A 469 4357 3641 4699 826 1438 694 N ATOM 2335 CA ALA A 469 16.747 58.808 -22.918 1.00 37.63 C ANISOU 2335 CA ALA A 469 4951 4120 5228 897 1502 726 C ATOM 2336 C ALA A 469 15.807 58.143 -23.913 1.00 39.05 C ANISOU 2336 C ALA A 469 5341 4323 5175 928 1444 790 C ATOM 2337 O ALA A 469 14.724 58.657 -24.192 1.00 35.78 O ANISOU 2337 O ALA A 469 4950 3962 4683 941 1384 791 O ATOM 2338 CB ALA A 469 17.819 59.617 -23.651 1.00 33.44 C ANISOU 2338 CB ALA A 469 4418 3396 4890 999 1712 781 C ATOM 2339 N GLU A 470 16.216 56.994 -24.441 1.00 38.92 N ANISOU 2339 N GLU A 470 5468 4264 5058 938 1461 838 N ATOM 2340 CA GLU A 470 15.356 56.232 -25.342 1.00 33.91 C ANISOU 2340 CA GLU A 470 5028 3656 4200 959 1389 869 C ATOM 2341 C GLU A 470 14.119 55.714 -24.618 1.00 35.14 C ANISOU 2341 C GLU A 470 5125 3970 4257 869 1194 798 C ATOM 2342 O GLU A 470 13.019 55.719 -25.171 1.00 37.21 O ANISOU 2342 O GLU A 470 5472 4276 4392 885 1098 795 O ATOM 2343 CB GLU A 470 16.110 55.053 -25.957 1.00 35.23 C ANISOU 2343 CB GLU A 470 5346 3737 4302 972 1464 918 C ATOM 2344 CG GLU A 470 17.250 55.436 -26.867 1.00 48.83 C ANISOU 2344 CG GLU A 470 7173 5270 6111 1077 1676 1008 C ATOM 2345 CD GLU A 470 17.919 54.210 -27.484 1.00 58.88 C ANISOU 2345 CD GLU A 470 8611 6448 7315 1081 1761 1061 C ATOM 2346 OE1 GLU A 470 19.150 54.249 -27.692 1.00 61.56 O ANISOU 2346 OE1 GLU A 470 8962 6624 7805 1121 1940 1129 O ATOM 2347 OE2 GLU A 470 17.213 53.209 -27.749 1.00 54.29 O ANISOU 2347 OE2 GLU A 470 8136 5941 6551 1039 1658 1031 O ATOM 2348 N MET A 471 14.311 55.249 -23.387 1.00 26.25 N ANISOU 2348 N MET A 471 3854 2922 3197 785 1140 747 N ATOM 2349 CA MET A 471 13.203 54.780 -22.554 1.00 30.19 C ANISOU 2349 CA MET A 471 4282 3552 3637 714 987 689 C ATOM 2350 C MET A 471 12.190 55.882 -22.314 1.00 29.22 C ANISOU 2350 C MET A 471 4087 3476 3539 708 922 658 C ATOM 2351 O MET A 471 10.989 55.679 -22.478 1.00 34.57 O ANISOU 2351 O MET A 471 4801 4198 4137 693 812 646 O ATOM 2352 CB MET A 471 13.720 54.246 -21.217 1.00 29.91 C ANISOU 2352 CB MET A 471 4101 3593 3672 653 970 655 C ATOM 2353 CG MET A 471 14.562 52.979 -21.376 1.00 38.87 C ANISOU 2353 CG MET A 471 5291 4692 4787 647 1031 702 C ATOM 2354 SD MET A 471 15.112 52.251 -19.822 1.00 37.25 S ANISOU 2354 SD MET A 471 4913 4597 4642 597 1006 688 S ATOM 2355 CE MET A 471 13.549 51.778 -19.065 1.00 26.47 C ANISOU 2355 CE MET A 471 3506 3359 3191 564 872 641 C ATOM 2356 N MET A 472 12.684 57.051 -21.930 1.00 29.89 N ANISOU 2356 N MET A 472 4059 3539 3760 717 998 642 N ATOM 2357 CA MET A 472 11.821 58.193 -21.641 1.00 32.03 C ANISOU 2357 CA MET A 472 4240 3841 4088 704 971 616 C ATOM 2358 C MET A 472 11.075 58.604 -22.901 1.00 32.22 C ANISOU 2358 C MET A 472 4389 3820 4033 772 972 684 C ATOM 2359 O MET A 472 9.858 58.827 -22.874 1.00 29.99 O ANISOU 2359 O MET A 472 4096 3584 3713 749 875 683 O ATOM 2360 CB MET A 472 12.650 59.365 -21.114 1.00 32.28 C ANISOU 2360 CB MET A 472 4122 3836 4306 707 1083 576 C ATOM 2361 CG MET A 472 13.224 59.136 -19.713 1.00 30.64 C ANISOU 2361 CG MET A 472 3768 3705 4168 638 1045 487 C ATOM 2362 SD MET A 472 11.974 59.365 -18.430 1.00 36.44 S ANISOU 2362 SD MET A 472 4397 4569 4879 556 925 410 S ATOM 2363 CE MET A 472 12.928 59.098 -16.932 1.00 36.82 C ANISOU 2363 CE MET A 472 4305 4711 4976 514 894 312 C ATOM 2364 N ASP A 473 11.823 58.707 -23.996 1.00 32.39 N ANISOU 2364 N ASP A 473 4531 3742 4032 865 1087 751 N ATOM 2365 CA ASP A 473 11.274 59.113 -25.279 1.00 37.30 C ANISOU 2365 CA ASP A 473 5293 4326 4554 961 1103 829 C ATOM 2366 C ASP A 473 10.196 58.128 -25.710 1.00 36.12 C ANISOU 2366 C ASP A 473 5265 4242 4217 941 927 818 C ATOM 2367 O ASP A 473 9.195 58.515 -26.311 1.00 34.74 O ANISOU 2367 O ASP A 473 5137 4093 3968 978 850 849 O ATOM 2368 CB ASP A 473 12.377 59.190 -26.353 1.00 47.54 C ANISOU 2368 CB ASP A 473 6727 5493 5841 1080 1274 907 C ATOM 2369 CG ASP A 473 13.338 60.375 -26.150 1.00 63.05 C ANISOU 2369 CG ASP A 473 8562 7358 8037 1129 1470 927 C ATOM 2370 OD1 ASP A 473 14.223 60.572 -27.015 1.00 69.42 O ANISOU 2370 OD1 ASP A 473 9467 8032 8878 1243 1641 1003 O ATOM 2371 OD2 ASP A 473 13.229 61.106 -25.139 1.00 60.91 O ANISOU 2371 OD2 ASP A 473 8091 7127 7924 1060 1466 861 O ATOM 2372 N GLU A 474 10.402 56.855 -25.395 1.00 31.64 N ANISOU 2372 N GLU A 474 4733 3698 3591 885 867 772 N ATOM 2373 CA GLU A 474 9.416 55.838 -25.732 1.00 35.73 C ANISOU 2373 CA GLU A 474 5339 4264 3973 859 709 739 C ATOM 2374 C GLU A 474 8.106 56.046 -24.971 1.00 34.42 C ANISOU 2374 C GLU A 474 5047 4171 3859 790 567 697 C ATOM 2375 O GLU A 474 7.023 55.914 -25.539 1.00 31.88 O ANISOU 2375 O GLU A 474 4781 3869 3463 802 438 693 O ATOM 2376 CB GLU A 474 9.954 54.426 -25.481 1.00 29.93 C ANISOU 2376 CB GLU A 474 4641 3527 3206 811 711 702 C ATOM 2377 CG GLU A 474 8.868 53.362 -25.629 1.00 31.49 C ANISOU 2377 CG GLU A 474 4880 3767 3319 772 554 643 C ATOM 2378 CD GLU A 474 9.406 51.945 -25.662 1.00 41.71 C ANISOU 2378 CD GLU A 474 6229 5040 4579 742 588 616 C ATOM 2379 OE1 GLU A 474 10.633 51.765 -25.844 1.00 39.61 O ANISOU 2379 OE1 GLU A 474 6014 4713 4321 762 733 659 O ATOM 2380 OE2 GLU A 474 8.593 51.011 -25.494 1.00 37.87 O ANISOU 2380 OE2 GLU A 474 5722 4583 4084 697 484 554 O ATOM 2381 N ILE A 475 8.198 56.368 -23.687 1.00 33.83 N ANISOU 2381 N ILE A 475 4805 4133 3918 722 591 666 N ATOM 2382 CA ILE A 475 6.989 56.669 -22.921 1.00 33.02 C ANISOU 2382 CA ILE A 475 4587 4074 3883 663 491 639 C ATOM 2383 C ILE A 475 6.315 57.968 -23.391 1.00 35.68 C ANISOU 2383 C ILE A 475 4901 4395 4260 695 495 690 C ATOM 2384 O ILE A 475 5.103 58.007 -23.581 1.00 36.68 O ANISOU 2384 O ILE A 475 5025 4531 4383 682 379 700 O ATOM 2385 CB ILE A 475 7.261 56.722 -21.407 1.00 32.19 C ANISOU 2385 CB ILE A 475 4327 4015 3889 594 525 591 C ATOM 2386 CG1 ILE A 475 7.835 55.384 -20.918 1.00 30.51 C ANISOU 2386 CG1 ILE A 475 4125 3830 3637 573 522 562 C ATOM 2387 CG2 ILE A 475 5.983 57.094 -20.641 1.00 26.70 C ANISOU 2387 CG2 ILE A 475 3532 3342 3272 541 449 574 C ATOM 2388 CD1 ILE A 475 6.997 54.160 -21.278 1.00 27.35 C ANISOU 2388 CD1 ILE A 475 3793 3425 3174 566 419 549 C ATOM 2389 N PHE A 476 7.096 59.020 -23.608 1.00 30.51 N ANISOU 2389 N PHE A 476 4221 3705 3667 742 638 728 N ATOM 2390 CA PHE A 476 6.509 60.314 -23.959 1.00 34.56 C ANISOU 2390 CA PHE A 476 4682 4199 4248 775 681 789 C ATOM 2391 C PHE A 476 6.010 60.409 -25.405 1.00 39.54 C ANISOU 2391 C PHE A 476 5462 4816 4746 877 634 872 C ATOM 2392 O PHE A 476 5.091 61.175 -25.688 1.00 35.01 O ANISOU 2392 O PHE A 476 4850 4249 4204 895 602 931 O ATOM 2393 CB PHE A 476 7.479 61.462 -23.657 1.00 30.92 C ANISOU 2393 CB PHE A 476 4114 3695 3939 796 872 795 C ATOM 2394 CG PHE A 476 7.807 61.596 -22.194 1.00 34.40 C ANISOU 2394 CG PHE A 476 4393 4167 4509 697 895 700 C ATOM 2395 CD1 PHE A 476 6.797 61.776 -21.262 1.00 28.83 C ANISOU 2395 CD1 PHE A 476 3587 3505 3863 611 822 663 C ATOM 2396 CD2 PHE A 476 9.121 61.544 -21.754 1.00 32.50 C ANISOU 2396 CD2 PHE A 476 4107 3907 4334 698 990 648 C ATOM 2397 CE1 PHE A 476 7.090 61.902 -19.910 1.00 32.88 C ANISOU 2397 CE1 PHE A 476 3973 4056 4465 535 843 571 C ATOM 2398 CE2 PHE A 476 9.425 61.671 -20.411 1.00 35.56 C ANISOU 2398 CE2 PHE A 476 4352 4343 4817 618 989 551 C ATOM 2399 CZ PHE A 476 8.403 61.847 -19.483 1.00 35.97 C ANISOU 2399 CZ PHE A 476 4322 4453 4895 540 916 510 C ATOM 2400 N ASP A 477 6.605 59.623 -26.303 1.00 34.93 N ANISOU 2400 N ASP A 477 5050 4213 4009 947 632 881 N ATOM 2401 CA ASP A 477 6.324 59.738 -27.736 1.00 41.40 C ANISOU 2401 CA ASP A 477 6040 5024 4667 1070 605 957 C ATOM 2402 C ASP A 477 6.597 58.465 -28.558 1.00 40.48 C ANISOU 2402 C ASP A 477 6124 4904 4351 1108 530 922 C ATOM 2403 O ASP A 477 6.850 58.544 -29.757 1.00 45.03 O ANISOU 2403 O ASP A 477 6876 5456 4776 1232 568 982 O ATOM 2404 CB ASP A 477 7.136 60.889 -28.328 1.00 49.60 C ANISOU 2404 CB ASP A 477 7093 5997 5756 1190 819 1056 C ATOM 2405 CG ASP A 477 6.629 61.318 -29.683 1.00 54.01 C ANISOU 2405 CG ASP A 477 7797 6564 6161 1335 801 1162 C ATOM 2406 OD1 ASP A 477 5.410 61.202 -29.931 1.00 50.38 O ANISOU 2406 OD1 ASP A 477 7347 6173 5622 1321 614 1164 O ATOM 2407 OD2 ASP A 477 7.454 61.773 -30.500 1.00 68.15 O ANISOU 2407 OD2 ASP A 477 9691 8288 7916 1474 976 1247 O ATOM 2408 N GLY A 478 6.539 57.298 -27.925 1.00 40.87 N ANISOU 2408 N GLY A 478 6152 4974 4402 1009 440 828 N ATOM 2409 CA GLY A 478 6.798 56.055 -28.636 1.00 40.53 C ANISOU 2409 CA GLY A 478 6280 4919 4200 1029 389 783 C ATOM 2410 C GLY A 478 5.543 55.384 -29.175 1.00 47.53 C ANISOU 2410 C GLY A 478 7229 5853 4975 1021 166 722 C ATOM 2411 O GLY A 478 5.623 54.486 -30.010 1.00 55.22 O ANISOU 2411 O GLY A 478 8366 6821 5795 1055 111 676 O ATOM 2412 N TYR A 479 4.381 55.822 -28.702 1.00 43.20 N ANISOU 2412 N TYR A 479 6548 5343 4523 974 40 717 N ATOM 2413 CA TYR A 479 3.121 55.144 -29.011 1.00 42.70 C ANISOU 2413 CA TYR A 479 6496 5307 4421 948 -186 645 C ATOM 2414 C TYR A 479 2.080 56.111 -29.550 1.00 47.98 C ANISOU 2414 C TYR A 479 7146 6006 5077 1002 -299 712 C ATOM 2415 O TYR A 479 2.004 57.273 -29.132 1.00 46.12 O ANISOU 2415 O TYR A 479 6800 5768 4955 1004 -209 801 O ATOM 2416 CB TYR A 479 2.560 54.433 -27.768 1.00 36.91 C ANISOU 2416 CB TYR A 479 5593 4564 3867 825 -244 568 C ATOM 2417 CG TYR A 479 3.484 53.393 -27.187 1.00 39.29 C ANISOU 2417 CG TYR A 479 5892 4847 4188 776 -140 515 C ATOM 2418 CD1 TYR A 479 3.474 52.083 -27.660 1.00 42.53 C ANISOU 2418 CD1 TYR A 479 6391 5243 4525 767 -202 426 C ATOM 2419 CD2 TYR A 479 4.381 53.721 -26.171 1.00 37.69 C ANISOU 2419 CD2 TYR A 479 5592 4643 4086 740 23 550 C ATOM 2420 CE1 TYR A 479 4.330 51.124 -27.133 1.00 40.49 C ANISOU 2420 CE1 TYR A 479 6118 4965 4301 724 -86 396 C ATOM 2421 CE2 TYR A 479 5.243 52.770 -25.637 1.00 36.18 C ANISOU 2421 CE2 TYR A 479 5390 4442 3914 703 115 519 C ATOM 2422 CZ TYR A 479 5.213 51.474 -26.121 1.00 34.95 C ANISOU 2422 CZ TYR A 479 5318 4268 3692 696 70 453 C ATOM 2423 OH TYR A 479 6.064 50.527 -25.597 1.00 42.31 O ANISOU 2423 OH TYR A 479 6228 5189 4660 660 181 440 O ATOM 2424 N ILE A 480 1.270 55.623 -30.478 1.00 51.60 N ANISOU 2424 N ILE A 480 7705 6493 5407 1045 -498 664 N ATOM 2425 CA ILE A 480 0.200 56.431 -31.041 1.00 49.51 C ANISOU 2425 CA ILE A 480 7420 6266 5126 1100 -639 730 C ATOM 2426 C ILE A 480 -1.013 56.444 -30.102 1.00 51.33 C ANISOU 2426 C ILE A 480 7443 6469 5592 989 -762 704 C ATOM 2427 O ILE A 480 -1.481 55.389 -29.672 1.00 55.49 O ANISOU 2427 O ILE A 480 7916 6963 6203 909 -872 588 O ATOM 2428 CB ILE A 480 -0.166 55.925 -32.447 1.00 54.40 C ANISOU 2428 CB ILE A 480 8236 6935 5497 1203 -823 682 C ATOM 2429 CG1 ILE A 480 1.076 55.996 -33.343 1.00 62.49 C ANISOU 2429 CG1 ILE A 480 9483 7966 6295 1328 -659 729 C ATOM 2430 CG2 ILE A 480 -1.324 56.732 -33.033 1.00 55.09 C ANISOU 2430 CG2 ILE A 480 8292 7074 5566 1268 -995 758 C ATOM 2431 CD1 ILE A 480 0.878 55.439 -34.735 1.00 73.78 C ANISOU 2431 CD1 ILE A 480 11147 9448 7440 1441 -815 671 C ATOM 2432 N PRO A 481 -1.500 57.648 -29.757 1.00 49.56 N ANISOU 2432 N PRO A 481 7093 6239 5498 985 -716 819 N ATOM 2433 CA PRO A 481 -2.652 57.841 -28.862 1.00 49.53 C ANISOU 2433 CA PRO A 481 6894 6186 5739 885 -797 823 C ATOM 2434 C PRO A 481 -3.923 57.175 -29.397 1.00 50.68 C ANISOU 2434 C PRO A 481 7035 6322 5899 881 -1075 755 C ATOM 2435 O PRO A 481 -4.035 56.973 -30.599 1.00 45.19 O ANISOU 2435 O PRO A 481 6482 5686 5000 975 -1216 737 O ATOM 2436 CB PRO A 481 -2.829 59.367 -28.830 1.00 48.98 C ANISOU 2436 CB PRO A 481 6740 6121 5751 916 -682 979 C ATOM 2437 CG PRO A 481 -1.503 59.918 -29.230 1.00 53.57 C ANISOU 2437 CG PRO A 481 7423 6734 6197 1004 -473 1036 C ATOM 2438 CD PRO A 481 -0.917 58.928 -30.198 1.00 55.23 C ANISOU 2438 CD PRO A 481 7844 6982 6160 1082 -546 960 C ATOM 2439 N HIS A 482 -4.856 56.829 -28.513 1.00 54.04 N ANISOU 2439 N HIS A 482 7300 6666 6568 782 -1148 714 N ATOM 2440 CA HIS A 482 -6.110 56.212 -28.929 1.00 51.53 C ANISOU 2440 CA HIS A 482 6940 6309 6330 772 -1410 642 C ATOM 2441 C HIS A 482 -6.850 57.112 -29.916 1.00 55.89 C ANISOU 2441 C HIS A 482 7510 6911 6815 852 -1556 746 C ATOM 2442 O HIS A 482 -7.037 58.298 -29.652 1.00 46.87 O ANISOU 2442 O HIS A 482 6282 5761 5764 852 -1449 895 O ATOM 2443 CB HIS A 482 -7.010 55.924 -27.725 1.00 44.54 C ANISOU 2443 CB HIS A 482 5858 5294 5771 664 -1415 620 C ATOM 2444 CG HIS A 482 -8.305 55.269 -28.091 1.00 55.74 C ANISOU 2444 CG HIS A 482 7205 6639 7334 652 -1675 539 C ATOM 2445 ND1 HIS A 482 -8.549 53.928 -27.876 1.00 65.49 N ANISOU 2445 ND1 HIS A 482 8408 7803 8671 616 -1756 381 N ATOM 2446 CD2 HIS A 482 -9.420 55.764 -28.679 1.00 62.23 C ANISOU 2446 CD2 HIS A 482 7968 7442 8236 674 -1872 592 C ATOM 2447 CE1 HIS A 482 -9.761 53.628 -28.309 1.00 69.74 C ANISOU 2447 CE1 HIS A 482 8867 8273 9359 615 -1997 325 C ATOM 2448 NE2 HIS A 482 -10.310 54.724 -28.802 1.00 71.07 N ANISOU 2448 NE2 HIS A 482 9019 8474 9510 649 -2082 453 N ATOM 2449 N PRO A 483 -7.281 56.540 -31.053 1.00 58.22 N ANISOU 2449 N PRO A 483 7912 7259 6951 922 -1800 663 N ATOM 2450 CA PRO A 483 -7.913 57.284 -32.153 1.00 56.47 C ANISOU 2450 CA PRO A 483 7738 7116 6603 1028 -1968 757 C ATOM 2451 C PRO A 483 -9.163 58.075 -31.746 1.00 59.16 C ANISOU 2451 C PRO A 483 7876 7384 7218 979 -2045 875 C ATOM 2452 O PRO A 483 -9.434 59.128 -32.330 1.00 55.48 O ANISOU 2452 O PRO A 483 7411 6979 6690 1060 -2054 1033 O ATOM 2453 CB PRO A 483 -8.279 56.173 -33.157 1.00 51.06 C ANISOU 2453 CB PRO A 483 7172 6475 5752 1077 -2252 581 C ATOM 2454 CG PRO A 483 -8.235 54.894 -32.355 1.00 53.29 C ANISOU 2454 CG PRO A 483 7385 6655 6207 962 -2243 404 C ATOM 2455 CD PRO A 483 -7.102 55.119 -31.403 1.00 50.53 C ANISOU 2455 CD PRO A 483 7030 6284 5883 915 -1922 468 C ATOM 2456 N ASP A 484 -9.908 57.584 -30.759 1.00 53.25 N ANISOU 2456 N ASP A 484 6953 6495 6782 857 -2078 813 N ATOM 2457 CA ASP A 484 -11.161 58.227 -30.366 1.00 56.87 C ANISOU 2457 CA ASP A 484 7218 6851 7537 804 -2152 921 C ATOM 2458 C ASP A 484 -11.025 59.134 -29.138 1.00 40.47 C ANISOU 2458 C ASP A 484 5009 4688 5681 719 -1868 1056 C ATOM 2459 O ASP A 484 -11.534 60.249 -29.130 1.00 48.64 O ANISOU 2459 O ASP A 484 5949 5704 6827 720 -1818 1223 O ATOM 2460 CB ASP A 484 -12.256 57.178 -30.114 1.00 64.05 C ANISOU 2460 CB ASP A 484 8008 7627 8703 737 -2375 780 C ATOM 2461 CG ASP A 484 -12.485 56.266 -31.311 1.00 68.72 C ANISOU 2461 CG ASP A 484 8710 8296 9105 810 -2677 615 C ATOM 2462 OD1 ASP A 484 -12.666 56.779 -32.439 1.00 66.70 O ANISOU 2462 OD1 ASP A 484 8545 8165 8633 915 -2841 672 O ATOM 2463 OD2 ASP A 484 -12.488 55.031 -31.114 1.00 70.61 O ANISOU 2463 OD2 ASP A 484 8943 8472 9414 768 -2743 425 O ATOM 2464 N THR A 485 -10.341 58.653 -28.106 1.00 43.50 N ANISOU 2464 N THR A 485 5383 5021 6125 649 -1680 982 N ATOM 2465 CA THR A 485 -10.282 59.361 -26.826 1.00 50.16 C ANISOU 2465 CA THR A 485 6101 5774 7183 561 -1433 1073 C ATOM 2466 C THR A 485 -9.096 60.320 -26.699 1.00 56.24 C ANISOU 2466 C THR A 485 6930 6639 7799 588 -1178 1155 C ATOM 2467 O THR A 485 -9.148 61.281 -25.932 1.00 50.24 O ANISOU 2467 O THR A 485 6064 5828 7199 533 -990 1257 O ATOM 2468 CB THR A 485 -10.172 58.372 -25.661 1.00 42.44 C ANISOU 2468 CB THR A 485 5074 4697 6356 483 -1353 956 C ATOM 2469 OG1 THR A 485 -8.986 57.584 -25.835 1.00 43.17 O ANISOU 2469 OG1 THR A 485 5305 4888 6210 518 -1305 842 O ATOM 2470 CG2 THR A 485 -11.401 57.464 -25.604 1.00 46.36 C ANISOU 2470 CG2 THR A 485 5471 5053 7091 453 -1558 878 C ATOM 2471 N GLY A 486 -8.019 60.036 -27.425 1.00 56.13 N ANISOU 2471 N GLY A 486 7082 6747 7499 671 -1162 1104 N ATOM 2472 CA GLY A 486 -6.799 60.809 -27.299 1.00 51.01 C ANISOU 2472 CA GLY A 486 6484 6164 6734 703 -915 1161 C ATOM 2473 C GLY A 486 -5.913 60.365 -26.142 1.00 48.20 C ANISOU 2473 C GLY A 486 6111 5782 6420 629 -741 1072 C ATOM 2474 O GLY A 486 -4.937 61.036 -25.814 1.00 44.71 O ANISOU 2474 O GLY A 486 5673 5373 5942 636 -532 1105 O ATOM 2475 N LYS A 487 -6.242 59.235 -25.522 1.00 47.73 N ANISOU 2475 N LYS A 487 6024 5662 6448 568 -823 959 N ATOM 2476 CA LYS A 487 -5.399 58.682 -24.454 1.00 52.33 C ANISOU 2476 CA LYS A 487 6599 6237 7046 517 -672 880 C ATOM 2477 C LYS A 487 -4.037 58.209 -24.951 1.00 44.62 C ANISOU 2477 C LYS A 487 5770 5355 5829 575 -612 821 C ATOM 2478 O LYS A 487 -3.946 57.457 -25.919 1.00 45.15 O ANISOU 2478 O LYS A 487 5956 5459 5738 632 -744 763 O ATOM 2479 CB LYS A 487 -6.098 57.521 -23.739 1.00 62.45 C ANISOU 2479 CB LYS A 487 7815 7427 8487 463 -757 790 C ATOM 2480 CG LYS A 487 -7.105 57.961 -22.693 1.00 72.90 C ANISOU 2480 CG LYS A 487 8983 8624 10091 391 -706 848 C ATOM 2481 CD LYS A 487 -7.581 56.787 -21.851 1.00 72.19 C ANISOU 2481 CD LYS A 487 8834 8432 10163 359 -726 766 C ATOM 2482 CE LYS A 487 -8.639 57.231 -20.856 1.00 67.69 C ANISOU 2482 CE LYS A 487 8126 7710 9884 301 -662 837 C ATOM 2483 NZ LYS A 487 -9.516 56.105 -20.438 1.00 67.32 N ANISOU 2483 NZ LYS A 487 8008 7519 10051 297 -735 778 N ATOM 2484 N ASP A 488 -2.978 58.630 -24.266 1.00 36.56 N ANISOU 2484 N ASP A 488 4728 4203 4960 95 -1168 -208 N ATOM 2485 CA ASP A 488 -1.631 58.202 -24.629 1.00 34.74 C ANISOU 2485 CA ASP A 488 4680 3980 4541 78 -1064 -234 C ATOM 2486 C ASP A 488 -1.032 57.192 -23.639 1.00 35.52 C ANISOU 2486 C ASP A 488 4691 4132 4674 63 -880 -217 C ATOM 2487 O ASP A 488 -1.698 56.742 -22.700 1.00 34.31 O ANISOU 2487 O ASP A 488 4350 4001 4686 69 -830 -189 O ATOM 2488 CB ASP A 488 -0.696 59.408 -24.843 1.00 32.25 C ANISOU 2488 CB ASP A 488 4494 3692 4066 122 -992 -231 C ATOM 2489 CG ASP A 488 -0.623 60.336 -23.633 1.00 39.80 C ANISOU 2489 CG ASP A 488 5312 4732 5078 162 -871 -204 C ATOM 2490 OD1 ASP A 488 -0.890 59.886 -22.496 1.00 36.60 O ANISOU 2490 OD1 ASP A 488 4744 4378 4782 167 -784 -183 O ATOM 2491 OD2 ASP A 488 -0.279 61.526 -23.824 1.00 41.49 O ANISOU 2491 OD2 ASP A 488 5598 4948 5219 195 -854 -205 O ATOM 2492 N ALA A 489 0.230 56.851 -23.859 1.00 34.55 N ANISOU 2492 N ALA A 489 4705 4022 4400 56 -766 -222 N ATOM 2493 CA ALA A 489 0.916 55.849 -23.061 1.00 38.37 C ANISOU 2493 CA ALA A 489 5130 4556 4893 51 -593 -197 C ATOM 2494 C ALA A 489 1.000 56.289 -21.610 1.00 38.14 C ANISOU 2494 C ALA A 489 4932 4634 4925 101 -469 -162 C ATOM 2495 O ALA A 489 0.820 55.495 -20.694 1.00 45.62 O ANISOU 2495 O ALA A 489 5755 5617 5960 118 -368 -132 O ATOM 2496 CB ALA A 489 2.315 55.599 -23.615 1.00 28.94 C ANISOU 2496 CB ALA A 489 4111 3353 3531 47 -490 -191 C ATOM 2497 N LEU A 490 1.280 57.566 -21.413 1.00 32.47 N ANISOU 2497 N LEU A 490 4228 3957 4151 132 -470 -167 N ATOM 2498 CA LEU A 490 1.403 58.129 -20.076 1.00 30.40 C ANISOU 2498 CA LEU A 490 3850 3787 3915 183 -370 -149 C ATOM 2499 C LEU A 490 0.057 58.166 -19.329 1.00 35.26 C ANISOU 2499 C LEU A 490 4310 4394 4694 221 -384 -123 C ATOM 2500 O LEU A 490 0.011 57.910 -18.128 1.00 36.17 O ANISOU 2500 O LEU A 490 4327 4566 4851 273 -265 -92 O ATOM 2501 CB LEU A 490 2.024 59.517 -20.191 1.00 27.89 C ANISOU 2501 CB LEU A 490 3605 3488 3504 193 -377 -173 C ATOM 2502 CG LEU A 490 2.666 60.213 -19.005 1.00 33.45 C ANISOU 2502 CG LEU A 490 4258 4279 4171 228 -283 -179 C ATOM 2503 CD1 LEU A 490 3.715 59.329 -18.346 1.00 27.95 C ANISOU 2503 CD1 LEU A 490 3535 3660 3424 232 -174 -161 C ATOM 2504 CD2 LEU A 490 3.284 61.524 -19.494 1.00 31.58 C ANISOU 2504 CD2 LEU A 490 4116 4020 3864 213 -307 -213 C ATOM 2505 N ASP A 491 -1.034 58.478 -20.034 1.00 31.32 N ANISOU 2505 N ASP A 491 3792 3818 4291 206 -525 -125 N ATOM 2506 CA ASP A 491 -2.362 58.397 -19.435 1.00 32.14 C ANISOU 2506 CA ASP A 491 3726 3890 4594 239 -534 -81 C ATOM 2507 C ASP A 491 -2.606 56.971 -18.939 1.00 41.36 C ANISOU 2507 C ASP A 491 4792 5045 5879 232 -449 -53 C ATOM 2508 O ASP A 491 -2.998 56.758 -17.788 1.00 44.40 O ANISOU 2508 O ASP A 491 5053 5451 6366 297 -315 -2 O ATOM 2509 CB ASP A 491 -3.480 58.770 -20.426 1.00 36.72 C ANISOU 2509 CB ASP A 491 4286 4385 5283 214 -729 -81 C ATOM 2510 CG ASP A 491 -3.693 60.276 -20.555 1.00 59.64 C ANISOU 2510 CG ASP A 491 7224 7293 8146 258 -773 -75 C ATOM 2511 OD1 ASP A 491 -3.541 61.013 -19.547 1.00 57.57 O ANISOU 2511 OD1 ASP A 491 6927 7078 7868 317 -643 -55 O ATOM 2512 OD2 ASP A 491 -4.041 60.717 -21.680 1.00 63.75 O ANISOU 2512 OD2 ASP A 491 7817 7760 8643 239 -939 -90 O ATOM 2513 N ILE A 492 -2.392 55.996 -19.815 1.00 33.48 N ANISOU 2513 N ILE A 492 3860 3996 4863 162 -514 -84 N ATOM 2514 CA ILE A 492 -2.666 54.609 -19.463 1.00 35.52 C ANISOU 2514 CA ILE A 492 4028 4219 5248 145 -433 -61 C ATOM 2515 C ILE A 492 -1.870 54.222 -18.231 1.00 35.20 C ANISOU 2515 C ILE A 492 3957 4271 5145 215 -209 -19 C ATOM 2516 O ILE A 492 -2.407 53.669 -17.274 1.00 36.96 O ANISOU 2516 O ILE A 492 4045 4489 5508 270 -81 36 O ATOM 2517 CB ILE A 492 -2.300 53.638 -20.598 1.00 33.87 C ANISOU 2517 CB ILE A 492 3948 3940 4980 59 -514 -111 C ATOM 2518 CG1 ILE A 492 -3.225 53.855 -21.803 1.00 43.05 C ANISOU 2518 CG1 ILE A 492 5144 5001 6212 -4 -765 -158 C ATOM 2519 CG2 ILE A 492 -2.400 52.187 -20.101 1.00 29.83 C ANISOU 2519 CG2 ILE A 492 3351 3394 4588 48 -381 -85 C ATOM 2520 CD1 ILE A 492 -2.868 52.987 -23.008 1.00 44.94 C ANISOU 2520 CD1 ILE A 492 5565 5156 6355 -82 -865 -222 C ATOM 2521 N MET A 493 -0.584 54.532 -18.255 1.00 30.28 N ANISOU 2521 N MET A 493 3460 3727 4317 221 -161 -39 N ATOM 2522 CA MET A 493 0.320 54.086 -17.200 1.00 32.59 C ANISOU 2522 CA MET A 493 3737 4116 4529 284 20 -2 C ATOM 2523 C MET A 493 0.045 54.727 -15.843 1.00 36.20 C ANISOU 2523 C MET A 493 4108 4640 5005 386 113 33 C ATOM 2524 O MET A 493 0.093 54.044 -14.826 1.00 34.79 O ANISOU 2524 O MET A 493 3867 4501 4851 462 265 83 O ATOM 2525 CB MET A 493 1.783 54.294 -17.611 1.00 26.86 C ANISOU 2525 CB MET A 493 3147 3451 3609 261 32 -24 C ATOM 2526 CG MET A 493 2.264 53.319 -18.685 1.00 22.97 C ANISOU 2526 CG MET A 493 2760 2892 3077 194 25 -32 C ATOM 2527 SD MET A 493 3.811 53.864 -19.422 1.00 37.20 S ANISOU 2527 SD MET A 493 4724 4722 4688 170 29 -44 S ATOM 2528 CE MET A 493 4.988 53.549 -18.106 1.00 26.39 C ANISOU 2528 CE MET A 493 3276 3492 3258 240 202 15 C ATOM 2529 N MET A 494 -0.245 56.027 -15.830 1.00 35.90 N ANISOU 2529 N MET A 494 4087 4607 4947 397 35 8 N ATOM 2530 CA MET A 494 -0.518 56.735 -14.578 1.00 35.72 C ANISOU 2530 CA MET A 494 4022 4629 4921 497 124 33 C ATOM 2531 C MET A 494 -1.670 56.118 -13.799 1.00 39.33 C ANISOU 2531 C MET A 494 4347 5031 5565 574 236 107 C ATOM 2532 O MET A 494 -1.691 56.150 -12.568 1.00 37.31 O ANISOU 2532 O MET A 494 4075 4816 5285 686 380 148 O ATOM 2533 CB MET A 494 -0.857 58.200 -14.842 1.00 31.55 C ANISOU 2533 CB MET A 494 3532 4079 4375 490 26 -1 C ATOM 2534 CG MET A 494 0.326 59.091 -15.119 1.00 31.73 C ANISOU 2534 CG MET A 494 3677 4160 4218 453 -25 -65 C ATOM 2535 SD MET A 494 -0.202 60.816 -15.244 1.00 40.28 S ANISOU 2535 SD MET A 494 4801 5202 5302 464 -95 -94 S ATOM 2536 CE MET A 494 1.408 61.596 -15.375 1.00 47.92 C ANISOU 2536 CE MET A 494 5892 6234 6082 416 -115 -168 C ATOM 2537 N PHE A 495 -2.646 55.576 -14.513 1.00 32.96 N ANISOU 2537 N PHE A 495 3450 4121 4952 520 171 125 N ATOM 2538 CA PHE A 495 -3.854 55.099 -13.850 1.00 30.93 C ANISOU 2538 CA PHE A 495 3038 3785 4930 587 277 206 C ATOM 2539 C PHE A 495 -3.969 53.581 -13.829 1.00 28.18 C ANISOU 2539 C PHE A 495 2613 3388 4705 570 370 240 C ATOM 2540 O PHE A 495 -4.965 53.029 -13.363 1.00 35.04 O ANISOU 2540 O PHE A 495 3337 4168 5807 616 471 311 O ATOM 2541 CB PHE A 495 -5.093 55.745 -14.472 1.00 40.30 C ANISOU 2541 CB PHE A 495 4130 4872 6310 552 143 220 C ATOM 2542 CG PHE A 495 -5.170 57.226 -14.242 1.00 34.79 C ANISOU 2542 CG PHE A 495 3489 4203 5527 601 114 214 C ATOM 2543 CD1 PHE A 495 -5.653 57.727 -13.044 1.00 29.91 C ANISOU 2543 CD1 PHE A 495 2835 3576 4955 729 278 282 C ATOM 2544 CD2 PHE A 495 -4.733 58.119 -15.214 1.00 35.32 C ANISOU 2544 CD2 PHE A 495 3666 4293 5461 528 -56 144 C ATOM 2545 CE1 PHE A 495 -5.724 59.097 -12.826 1.00 37.47 C ANISOU 2545 CE1 PHE A 495 3862 4545 5830 773 265 272 C ATOM 2546 CE2 PHE A 495 -4.796 59.487 -15.003 1.00 35.79 C ANISOU 2546 CE2 PHE A 495 3780 4366 5451 572 -65 138 C ATOM 2547 CZ PHE A 495 -5.295 59.975 -13.807 1.00 37.71 C ANISOU 2547 CZ PHE A 495 3986 4600 5743 689 93 198 C ATOM 2548 N HIS A 496 -2.938 52.908 -14.323 1.00 28.08 N ANISOU 2548 N HIS A 496 2697 3422 4549 510 355 196 N ATOM 2549 CA HIS A 496 -2.943 51.460 -14.342 1.00 29.39 C ANISOU 2549 CA HIS A 496 2815 3539 4814 492 457 224 C ATOM 2550 C HIS A 496 -2.490 50.891 -12.989 1.00 35.31 C ANISOU 2550 C HIS A 496 3549 4358 5510 629 703 298 C ATOM 2551 O HIS A 496 -1.630 51.469 -12.319 1.00 27.71 O ANISOU 2551 O HIS A 496 2673 3515 4340 703 747 296 O ATOM 2552 CB HIS A 496 -2.048 50.962 -15.455 1.00 27.47 C ANISOU 2552 CB HIS A 496 2699 3300 4437 383 360 158 C ATOM 2553 CG HIS A 496 -2.169 49.497 -15.701 1.00 34.07 C ANISOU 2553 CG HIS A 496 3501 4054 5390 341 441 173 C ATOM 2554 ND1 HIS A 496 -1.340 48.576 -15.102 1.00 31.17 N ANISOU 2554 ND1 HIS A 496 3161 3740 4942 400 637 219 N ATOM 2555 CD2 HIS A 496 -3.041 48.791 -16.460 1.00 34.22 C ANISOU 2555 CD2 HIS A 496 3459 3933 5610 246 351 146 C ATOM 2556 CE1 HIS A 496 -1.686 47.361 -15.497 1.00 40.25 C ANISOU 2556 CE1 HIS A 496 4277 4779 6236 343 687 222 C ATOM 2557 NE2 HIS A 496 -2.713 47.466 -16.320 1.00 33.15 N ANISOU 2557 NE2 HIS A 496 3326 3759 5511 243 507 170 N ATOM 2558 N GLN A 497 -3.074 49.763 -12.594 1.00 31.63 N ANISOU 2558 N GLN A 497 2975 3810 5234 665 858 363 N ATOM 2559 CA GLN A 497 -2.801 49.157 -11.284 1.00 36.27 C ANISOU 2559 CA GLN A 497 3547 4445 5787 822 1115 451 C ATOM 2560 C GLN A 497 -1.319 48.855 -11.036 1.00 32.86 C ANISOU 2560 C GLN A 497 3244 4155 5087 857 1169 443 C ATOM 2561 O GLN A 497 -0.850 48.946 -9.902 1.00 36.24 O ANISOU 2561 O GLN A 497 3710 4678 5382 1001 1304 493 O ATOM 2562 CB GLN A 497 -3.627 47.886 -11.097 1.00 33.39 C ANISOU 2562 CB GLN A 497 3046 3947 5695 839 1281 522 C ATOM 2563 CG GLN A 497 -3.307 46.838 -12.131 1.00 41.51 C ANISOU 2563 CG GLN A 497 4093 4916 6763 702 1225 473 C ATOM 2564 CD GLN A 497 -4.227 45.631 -12.045 1.00 52.20 C ANISOU 2564 CD GLN A 497 5298 6108 8426 692 1368 526 C ATOM 2565 OE1 GLN A 497 -4.618 45.209 -10.955 1.00 43.89 O ANISOU 2565 OE1 GLN A 497 4161 5025 7489 834 1612 630 O ATOM 2566 NE2 GLN A 497 -4.558 45.057 -13.198 1.00 50.64 N ANISOU 2566 NE2 GLN A 497 5082 5795 8364 528 1221 455 N ATOM 2567 N PHE A 498 -0.586 48.489 -12.089 1.00 24.97 N ANISOU 2567 N PHE A 498 2317 3164 4009 734 1064 385 N ATOM 2568 CA PHE A 498 0.851 48.273 -11.980 1.00 26.33 C ANISOU 2568 CA PHE A 498 2593 3460 3950 757 1104 388 C ATOM 2569 C PHE A 498 1.642 49.421 -12.632 1.00 35.74 C ANISOU 2569 C PHE A 498 3887 4725 4967 680 911 310 C ATOM 2570 O PHE A 498 2.698 49.814 -12.141 1.00 39.36 O ANISOU 2570 O PHE A 498 4402 5307 5245 732 921 314 O ATOM 2571 CB PHE A 498 1.270 46.915 -12.595 1.00 25.63 C ANISOU 2571 CB PHE A 498 2525 3318 3896 700 1190 407 C ATOM 2572 CG PHE A 498 0.454 45.746 -12.103 1.00 32.16 C ANISOU 2572 CG PHE A 498 3247 4043 4930 755 1385 477 C ATOM 2573 CD1 PHE A 498 0.242 45.554 -10.747 1.00 35.46 C ANISOU 2573 CD1 PHE A 498 3605 4503 5367 927 1585 569 C ATOM 2574 CD2 PHE A 498 -0.100 44.843 -12.996 1.00 32.12 C ANISOU 2574 CD2 PHE A 498 3214 3887 5103 640 1371 450 C ATOM 2575 CE1 PHE A 498 -0.522 44.494 -10.285 1.00 41.53 C ANISOU 2575 CE1 PHE A 498 4271 5159 6347 988 1793 645 C ATOM 2576 CE2 PHE A 498 -0.862 43.769 -12.541 1.00 29.23 C ANISOU 2576 CE2 PHE A 498 2736 3408 4962 682 1560 513 C ATOM 2577 CZ PHE A 498 -1.069 43.594 -11.185 1.00 32.76 C ANISOU 2577 CZ PHE A 498 3109 3894 5445 859 1784 617 C ATOM 2578 N GLY A 499 1.131 49.959 -13.736 1.00 36.12 N ANISOU 2578 N GLY A 499 3956 4690 5078 562 733 242 N ATOM 2579 CA GLY A 499 1.859 50.973 -14.487 1.00 26.91 C ANISOU 2579 CA GLY A 499 2895 3566 3763 491 575 175 C ATOM 2580 C GLY A 499 2.101 52.253 -13.706 1.00 26.54 C ANISOU 2580 C GLY A 499 2858 3612 3613 555 540 159 C ATOM 2581 O GLY A 499 3.075 52.966 -13.942 1.00 25.13 O ANISOU 2581 O GLY A 499 2757 3500 3292 526 470 122 O ATOM 2582 N ASN A 500 1.203 52.559 -12.775 1.00 23.14 N ANISOU 2582 N ASN A 500 2354 3173 3266 643 598 189 N ATOM 2583 CA ASN A 500 1.358 53.761 -11.977 1.00 27.50 C ANISOU 2583 CA ASN A 500 2940 3796 3712 710 575 167 C ATOM 2584 C ASN A 500 2.681 53.788 -11.209 1.00 30.00 C ANISOU 2584 C ASN A 500 3318 4248 3834 771 620 168 C ATOM 2585 O ASN A 500 3.203 54.865 -10.922 1.00 29.50 O ANISOU 2585 O ASN A 500 3312 4244 3652 774 540 116 O ATOM 2586 CB ASN A 500 0.176 53.932 -11.020 1.00 30.20 C ANISOU 2586 CB ASN A 500 3212 4088 4173 821 676 218 C ATOM 2587 CG ASN A 500 0.278 53.031 -9.804 1.00 34.27 C ANISOU 2587 CG ASN A 500 3706 4646 4671 964 879 298 C ATOM 2588 OD1 ASN A 500 0.897 53.395 -8.806 1.00 32.61 O ANISOU 2588 OD1 ASN A 500 3567 4532 4291 1068 926 299 O ATOM 2589 ND2 ASN A 500 -0.343 51.851 -9.876 1.00 30.05 N ANISOU 2589 ND2 ASN A 500 3079 4030 4310 976 998 362 N ATOM 2590 N TYR A 501 3.222 52.610 -10.882 1.00 28.27 N ANISOU 2590 N TYR A 501 3079 4072 3590 819 742 227 N ATOM 2591 CA TYR A 501 4.468 52.528 -10.111 1.00 22.18 C ANISOU 2591 CA TYR A 501 2345 3437 2646 889 776 244 C ATOM 2592 C TYR A 501 5.666 52.882 -10.990 1.00 30.93 C ANISOU 2592 C TYR A 501 3496 4585 3673 778 661 201 C ATOM 2593 O TYR A 501 6.680 53.393 -10.510 1.00 28.23 O ANISOU 2593 O TYR A 501 3176 4344 3206 799 610 183 O ATOM 2594 CB TYR A 501 4.660 51.126 -9.497 1.00 25.55 C ANISOU 2594 CB TYR A 501 2733 3895 3078 991 961 340 C ATOM 2595 CG TYR A 501 3.661 50.794 -8.398 1.00 30.06 C ANISOU 2595 CG TYR A 501 3272 4436 3714 1139 1115 401 C ATOM 2596 CD1 TYR A 501 3.779 51.354 -7.121 1.00 34.37 C ANISOU 2596 CD1 TYR A 501 3873 5063 4122 1284 1145 408 C ATOM 2597 CD2 TYR A 501 2.597 49.929 -8.638 1.00 32.62 C ANISOU 2597 CD2 TYR A 501 3519 4635 4241 1138 1235 452 C ATOM 2598 CE1 TYR A 501 2.855 51.062 -6.105 1.00 30.77 C ANISOU 2598 CE1 TYR A 501 3412 4560 3718 1443 1318 478 C ATOM 2599 CE2 TYR A 501 1.664 49.629 -7.629 1.00 31.62 C ANISOU 2599 CE2 TYR A 501 3352 4457 4205 1285 1409 525 C ATOM 2600 CZ TYR A 501 1.807 50.196 -6.373 1.00 32.20 C ANISOU 2600 CZ TYR A 501 3498 4609 4126 1445 1462 544 C ATOM 2601 OH TYR A 501 0.896 49.884 -5.397 1.00 37.76 O ANISOU 2601 OH TYR A 501 4185 5246 4915 1609 1662 630 O ATOM 2602 N VAL A 502 5.549 52.594 -12.281 1.00 30.65 N ANISOU 2602 N VAL A 502 3475 4456 3713 665 621 188 N ATOM 2603 CA VAL A 502 6.599 52.951 -13.222 1.00 31.82 C ANISOU 2603 CA VAL A 502 3682 4610 3800 571 541 160 C ATOM 2604 C VAL A 502 6.666 54.479 -13.412 1.00 29.02 C ANISOU 2604 C VAL A 502 3365 4253 3407 522 398 80 C ATOM 2605 O VAL A 502 7.739 55.066 -13.391 1.00 28.66 O ANISOU 2605 O VAL A 502 3335 4264 3288 498 350 61 O ATOM 2606 CB VAL A 502 6.418 52.219 -14.559 1.00 31.37 C ANISOU 2606 CB VAL A 502 3672 4437 3809 482 547 167 C ATOM 2607 CG1 VAL A 502 7.443 52.691 -15.569 1.00 29.87 C ANISOU 2607 CG1 VAL A 502 3567 4227 3555 403 487 148 C ATOM 2608 CG2 VAL A 502 6.535 50.721 -14.342 1.00 31.36 C ANISOU 2608 CG2 VAL A 502 3643 4433 3840 526 707 244 C ATOM 2609 N VAL A 503 5.515 55.120 -13.569 1.00 25.84 N ANISOU 2609 N VAL A 503 2966 3779 3074 509 337 40 N ATOM 2610 CA VAL A 503 5.502 56.570 -13.719 1.00 33.46 C ANISOU 2610 CA VAL A 503 3973 4733 4009 473 224 -29 C ATOM 2611 C VAL A 503 6.061 57.244 -12.456 1.00 32.87 C ANISOU 2611 C VAL A 503 3894 4759 3835 541 223 -54 C ATOM 2612 O VAL A 503 6.839 58.189 -12.547 1.00 30.17 O ANISOU 2612 O VAL A 503 3585 4439 3438 495 144 -108 O ATOM 2613 CB VAL A 503 4.096 57.110 -14.064 1.00 29.46 C ANISOU 2613 CB VAL A 503 3459 4131 3604 464 170 -50 C ATOM 2614 CG1 VAL A 503 4.146 58.624 -14.323 1.00 24.93 C ANISOU 2614 CG1 VAL A 503 2942 3537 2995 428 72 -114 C ATOM 2615 CG2 VAL A 503 3.534 56.383 -15.273 1.00 29.73 C ANISOU 2615 CG2 VAL A 503 3501 4066 3729 397 137 -36 C ATOM 2616 N GLN A 504 5.686 56.742 -11.282 1.00 26.81 N ANISOU 2616 N GLN A 504 3096 4044 3047 654 311 -17 N ATOM 2617 CA GLN A 504 6.244 57.265 -10.041 1.00 33.69 C ANISOU 2617 CA GLN A 504 3994 5012 3794 734 298 -45 C ATOM 2618 C GLN A 504 7.758 57.121 -10.052 1.00 34.85 C ANISOU 2618 C GLN A 504 4128 5251 3860 698 250 -47 C ATOM 2619 O GLN A 504 8.477 58.019 -9.624 1.00 31.75 O ANISOU 2619 O GLN A 504 3761 4909 3394 682 153 -111 O ATOM 2620 CB GLN A 504 5.677 56.534 -8.821 1.00 35.28 C ANISOU 2620 CB GLN A 504 4187 5250 3968 887 427 17 C ATOM 2621 CG GLN A 504 4.170 56.641 -8.678 1.00 46.62 C ANISOU 2621 CG GLN A 504 5612 6583 5517 939 502 41 C ATOM 2622 CD GLN A 504 3.682 56.044 -7.382 1.00 45.71 C ANISOU 2622 CD GLN A 504 5507 6490 5371 1111 657 110 C ATOM 2623 OE1 GLN A 504 3.874 56.624 -6.318 1.00 47.72 O ANISOU 2623 OE1 GLN A 504 5848 6796 5487 1212 658 83 O ATOM 2624 NE2 GLN A 504 3.051 54.874 -7.462 1.00 36.91 N ANISOU 2624 NE2 GLN A 504 4315 5324 4384 1152 796 197 N ATOM 2625 N CYS A 505 8.236 55.980 -10.535 1.00 30.05 N ANISOU 2625 N CYS A 505 3476 4657 3283 686 322 26 N ATOM 2626 CA CYS A 505 9.671 55.755 -10.651 1.00 30.30 C ANISOU 2626 CA CYS A 505 3476 4764 3273 655 298 50 C ATOM 2627 C CYS A 505 10.328 56.777 -11.594 1.00 30.89 C ANISOU 2627 C CYS A 505 3568 4786 3383 530 193 -8 C ATOM 2628 O CYS A 505 11.365 57.352 -11.268 1.00 28.87 O ANISOU 2628 O CYS A 505 3283 4589 3096 506 115 -35 O ATOM 2629 CB CYS A 505 9.952 54.319 -11.105 1.00 31.21 C ANISOU 2629 CB CYS A 505 3556 4876 3426 669 428 152 C ATOM 2630 SG CYS A 505 11.693 53.918 -11.322 1.00 35.79 S ANISOU 2630 SG CYS A 505 4079 5532 3985 645 436 219 S ATOM 2631 N MET A 506 9.726 57.007 -12.758 1.00 32.07 N ANISOU 2631 N MET A 506 3765 4817 3604 454 190 -24 N ATOM 2632 CA MET A 506 10.237 58.015 -13.701 1.00 30.47 C ANISOU 2632 CA MET A 506 3599 4544 3435 355 117 -70 C ATOM 2633 C MET A 506 10.353 59.394 -13.073 1.00 27.20 C ANISOU 2633 C MET A 506 3192 4149 2993 341 14 -161 C ATOM 2634 O MET A 506 11.338 60.109 -13.268 1.00 30.33 O ANISOU 2634 O MET A 506 3573 4542 3410 279 -40 -191 O ATOM 2635 CB MET A 506 9.306 58.119 -14.906 1.00 26.50 C ANISOU 2635 CB MET A 506 3170 3914 2985 307 115 -80 C ATOM 2636 CG MET A 506 9.318 56.867 -15.759 1.00 33.74 C ANISOU 2636 CG MET A 506 4113 4780 3925 297 198 -10 C ATOM 2637 SD MET A 506 7.982 56.862 -16.952 1.00 31.81 S ANISOU 2637 SD MET A 506 3958 4397 3731 257 152 -36 S ATOM 2638 CE MET A 506 8.502 58.175 -18.057 1.00 34.27 C ANISOU 2638 CE MET A 506 4369 4624 4028 191 83 -77 C ATOM 2639 N LEU A 507 9.315 59.770 -12.341 1.00 24.93 N ANISOU 2639 N LEU A 507 2932 3865 2675 398 -1 -202 N ATOM 2640 CA LEU A 507 9.232 61.086 -11.729 1.00 31.30 C ANISOU 2640 CA LEU A 507 3778 4668 3445 393 -83 -294 C ATOM 2641 C LEU A 507 10.305 61.244 -10.657 1.00 34.14 C ANISOU 2641 C LEU A 507 4109 5135 3727 416 -148 -328 C ATOM 2642 O LEU A 507 10.943 62.294 -10.547 1.00 32.96 O ANISOU 2642 O LEU A 507 3969 4973 3579 353 -242 -407 O ATOM 2643 CB LEU A 507 7.849 61.278 -11.109 1.00 33.41 C ANISOU 2643 CB LEU A 507 4089 4908 3697 475 -49 -304 C ATOM 2644 CG LEU A 507 7.598 62.605 -10.389 1.00 40.42 C ANISOU 2644 CG LEU A 507 5049 5776 4534 490 -105 -395 C ATOM 2645 CD1 LEU A 507 7.828 63.791 -11.340 1.00 33.39 C ANISOU 2645 CD1 LEU A 507 4188 4795 3702 381 -167 -454 C ATOM 2646 CD2 LEU A 507 6.191 62.627 -9.811 1.00 33.68 C ANISOU 2646 CD2 LEU A 507 4232 4881 3683 591 -29 -371 C ATOM 2647 N THR A 508 10.495 60.192 -9.868 1.00 30.96 N ANISOU 2647 N THR A 508 3670 4832 3261 508 -103 -268 N ATOM 2648 CA THR A 508 11.450 60.220 -8.765 1.00 36.75 C ANISOU 2648 CA THR A 508 4381 5683 3901 553 -184 -293 C ATOM 2649 C THR A 508 12.878 60.327 -9.286 1.00 33.60 C ANISOU 2649 C THR A 508 3889 5304 3572 455 -253 -283 C ATOM 2650 O THR A 508 13.714 61.014 -8.703 1.00 37.17 O ANISOU 2650 O THR A 508 4317 5802 4003 425 -384 -351 O ATOM 2651 CB THR A 508 11.284 58.982 -7.846 1.00 42.41 C ANISOU 2651 CB THR A 508 5087 6498 4529 698 -98 -210 C ATOM 2652 OG1 THR A 508 10.036 59.083 -7.148 1.00 47.43 O ANISOU 2652 OG1 THR A 508 5811 7104 5106 802 -33 -223 O ATOM 2653 CG2 THR A 508 12.425 58.885 -6.827 1.00 40.28 C ANISOU 2653 CG2 THR A 508 4786 6363 4156 750 -201 -219 C ATOM 2654 N ILE A 509 13.152 59.660 -10.400 1.00 38.61 N ANISOU 2654 N ILE A 509 4475 5891 4302 406 -163 -198 N ATOM 2655 CA ILE A 509 14.458 59.767 -11.033 1.00 37.16 C ANISOU 2655 CA ILE A 509 4205 5696 4216 320 -188 -165 C ATOM 2656 C ILE A 509 14.721 61.219 -11.436 1.00 34.42 C ANISOU 2656 C ILE A 509 3875 5259 3943 213 -279 -264 C ATOM 2657 O ILE A 509 15.769 61.789 -11.125 1.00 38.93 O ANISOU 2657 O ILE A 509 4368 5855 4568 158 -379 -300 O ATOM 2658 CB ILE A 509 14.537 58.857 -12.262 1.00 38.31 C ANISOU 2658 CB ILE A 509 4347 5772 4436 298 -45 -57 C ATOM 2659 CG1 ILE A 509 14.538 57.392 -11.814 1.00 38.34 C ANISOU 2659 CG1 ILE A 509 4317 5863 4388 397 55 47 C ATOM 2660 CG2 ILE A 509 15.767 59.185 -13.092 1.00 33.00 C ANISOU 2660 CG2 ILE A 509 3611 5041 3888 211 -37 -18 C ATOM 2661 CD1 ILE A 509 14.352 56.405 -12.950 1.00 33.31 C ANISOU 2661 CD1 ILE A 509 3716 5141 3800 385 206 138 C ATOM 2662 N CYS A 510 13.750 61.821 -12.110 1.00 31.93 N ANISOU 2662 N CYS A 510 3655 4836 3642 185 -246 -306 N ATOM 2663 CA CYS A 510 13.891 63.192 -12.586 1.00 38.36 C ANISOU 2663 CA CYS A 510 4500 5547 4528 95 -300 -389 C ATOM 2664 C CYS A 510 14.063 64.206 -11.460 1.00 42.73 C ANISOU 2664 C CYS A 510 5062 6138 5035 83 -434 -510 C ATOM 2665 O CYS A 510 14.916 65.094 -11.551 1.00 42.09 O ANISOU 2665 O CYS A 510 4936 6012 5045 -6 -506 -569 O ATOM 2666 CB CYS A 510 12.713 63.571 -13.484 1.00 31.86 C ANISOU 2666 CB CYS A 510 3784 4611 3712 91 -239 -397 C ATOM 2667 SG CYS A 510 12.713 62.643 -15.037 1.00 33.45 S ANISOU 2667 SG CYS A 510 4012 4728 3968 78 -115 -282 S ATOM 2668 N CYS A 511 13.262 64.075 -10.403 1.00 36.61 N ANISOU 2668 N CYS A 511 4353 5429 4126 176 -459 -548 N ATOM 2669 CA CYS A 511 13.391 64.964 -9.246 1.00 40.57 C ANISOU 2669 CA CYS A 511 4906 5963 4547 184 -586 -669 C ATOM 2670 C CYS A 511 14.720 64.753 -8.501 1.00 40.03 C ANISOU 2670 C CYS A 511 4738 6000 4470 168 -719 -686 C ATOM 2671 O CYS A 511 15.302 65.707 -8.002 1.00 47.76 O ANISOU 2671 O CYS A 511 5719 6966 5461 104 -859 -798 O ATOM 2672 CB CYS A 511 12.198 64.819 -8.287 1.00 37.27 C ANISOU 2672 CB CYS A 511 4607 5577 3978 312 -552 -687 C ATOM 2673 SG CYS A 511 10.601 65.328 -8.977 1.00 46.46 S ANISOU 2673 SG CYS A 511 5868 6609 5177 329 -432 -679 S ATOM 2674 N ASP A 512 15.194 63.511 -8.423 1.00 38.87 N ANISOU 2674 N ASP A 512 4502 5954 4313 226 -681 -574 N ATOM 2675 CA ASP A 512 16.499 63.236 -7.818 1.00 38.78 C ANISOU 2675 CA ASP A 512 4369 6048 4317 216 -808 -564 C ATOM 2676 C ASP A 512 17.642 63.850 -8.628 1.00 41.98 C ANISOU 2676 C ASP A 512 4643 6377 4933 70 -855 -567 C ATOM 2677 O ASP A 512 18.612 64.348 -8.064 1.00 44.47 O ANISOU 2677 O ASP A 512 4872 6727 5299 13 -1023 -631 O ATOM 2678 CB ASP A 512 16.751 61.731 -7.674 1.00 37.85 C ANISOU 2678 CB ASP A 512 4179 6042 4159 318 -722 -419 C ATOM 2679 CG ASP A 512 15.950 61.111 -6.554 1.00 48.43 C ANISOU 2679 CG ASP A 512 5625 7479 5299 480 -700 -414 C ATOM 2680 OD1 ASP A 512 15.205 61.853 -5.869 1.00 44.66 O ANISOU 2680 OD1 ASP A 512 5283 6977 4709 517 -751 -520 O ATOM 2681 OD2 ASP A 512 16.062 59.881 -6.363 1.00 48.80 O ANISOU 2681 OD2 ASP A 512 5626 7612 5305 578 -610 -296 O ATOM 2682 N ALA A 513 17.531 63.799 -9.949 1.00 38.36 N ANISOU 2682 N ALA A 513 4171 5805 4601 14 -706 -495 N ATOM 2683 CA ALA A 513 18.565 64.350 -10.818 1.00 44.93 C ANISOU 2683 CA ALA A 513 4890 6536 5646 -106 -699 -474 C ATOM 2684 C ALA A 513 18.624 65.869 -10.694 1.00 47.80 C ANISOU 2684 C ALA A 513 5285 6801 6075 -206 -806 -623 C ATOM 2685 O ALA A 513 19.681 66.444 -10.438 1.00 47.15 O ANISOU 2685 O ALA A 513 5082 6705 6130 -294 -927 -669 O ATOM 2686 CB ALA A 513 18.317 63.943 -12.256 1.00 40.86 C ANISOU 2686 CB ALA A 513 4407 5909 5210 -114 -500 -363 C ATOM 2687 N VAL A 514 17.475 66.512 -10.860 1.00 50.00 N ANISOU 2687 N VAL A 514 5720 7005 6271 -193 -759 -694 N ATOM 2688 CA VAL A 514 17.390 67.963 -10.802 1.00 52.60 C ANISOU 2688 CA VAL A 514 6107 7224 6656 -278 -824 -830 C ATOM 2689 C VAL A 514 17.748 68.528 -9.421 1.00 58.03 C ANISOU 2689 C VAL A 514 6802 7980 7268 -295 -1033 -972 C ATOM 2690 O VAL A 514 18.179 69.678 -9.304 1.00 62.70 O ANISOU 2690 O VAL A 514 7386 8479 7957 -398 -1123 -1089 O ATOM 2691 CB VAL A 514 15.991 68.451 -11.236 1.00 49.86 C ANISOU 2691 CB VAL A 514 5928 6791 6224 -238 -718 -856 C ATOM 2692 CG1 VAL A 514 15.852 69.943 -11.018 1.00 55.40 C ANISOU 2692 CG1 VAL A 514 6706 7383 6960 -310 -774 -997 C ATOM 2693 CG2 VAL A 514 15.749 68.105 -12.699 1.00 47.49 C ANISOU 2693 CG2 VAL A 514 5636 6400 6009 -239 -549 -738 C ATOM 2694 N SER A 515 17.587 67.719 -8.378 1.00 52.35 N ANISOU 2694 N SER A 515 6109 7411 6371 -188 -1108 -964 N ATOM 2695 CA SER A 515 17.853 68.195 -7.023 1.00 55.98 C ANISOU 2695 CA SER A 515 6621 7938 6710 -177 -1317 -1102 C ATOM 2696 C SER A 515 19.247 67.812 -6.521 1.00 63.18 C ANISOU 2696 C SER A 515 7355 8951 7700 -216 -1496 -1091 C ATOM 2697 O SER A 515 19.613 68.129 -5.386 1.00 64.47 O ANISOU 2697 O SER A 515 7553 9182 7761 -207 -1708 -1206 O ATOM 2698 CB SER A 515 16.792 67.684 -6.050 1.00 57.43 C ANISOU 2698 CB SER A 515 6978 8212 6631 -13 -1296 -1110 C ATOM 2699 OG SER A 515 17.070 66.353 -5.659 1.00 61.15 O ANISOU 2699 OG SER A 515 7378 8833 7024 94 -1289 -994 O ATOM 2700 N GLY A 516 20.015 67.124 -7.361 1.00 58.19 N ANISOU 2700 N GLY A 516 6538 8324 7246 -250 -1412 -947 N ATOM 2701 CA GLY A 516 21.379 66.764 -7.016 1.00 61.52 C ANISOU 2701 CA GLY A 516 6754 8829 7791 -290 -1564 -907 C ATOM 2702 C GLY A 516 21.536 65.417 -6.331 1.00 63.37 C ANISOU 2702 C GLY A 516 6951 9250 7878 -148 -1585 -797 C ATOM 2703 O GLY A 516 22.657 64.939 -6.143 1.00 54.05 O ANISOU 2703 O GLY A 516 5581 8149 6809 -161 -1684 -724 O ATOM 2704 N ARG A 517 20.419 64.797 -5.957 1.00 66.98 N ANISOU 2704 N ARG A 517 7579 9769 8103 -5 -1481 -774 N ATOM 2705 CA ARG A 517 20.453 63.480 -5.320 1.00 64.03 C ANISOU 2705 CA ARG A 517 7189 9558 7582 150 -1460 -660 C ATOM 2706 C ARG A 517 20.958 62.380 -6.258 1.00 67.60 C ANISOU 2706 C ARG A 517 7484 10021 8180 157 -1282 -464 C ATOM 2707 O ARG A 517 21.218 61.258 -5.822 1.00 70.48 O ANISOU 2707 O ARG A 517 7797 10514 8467 273 -1254 -349 O ATOM 2708 CB ARG A 517 19.072 63.108 -4.771 1.00 61.26 C ANISOU 2708 CB ARG A 517 7054 9237 6985 300 -1351 -673 C ATOM 2709 CG ARG A 517 18.606 63.988 -3.618 1.00 65.96 C ANISOU 2709 CG ARG A 517 7835 9839 7389 342 -1511 -844 C ATOM 2710 CD ARG A 517 17.338 63.446 -2.979 1.00 65.91 C ANISOU 2710 CD ARG A 517 8023 9866 7154 522 -1376 -818 C ATOM 2711 NE ARG A 517 16.168 63.638 -3.832 1.00 70.43 N ANISOU 2711 NE ARG A 517 8669 10310 7780 502 -1169 -796 N ATOM 2712 CZ ARG A 517 15.295 64.631 -3.690 1.00 71.03 C ANISOU 2712 CZ ARG A 517 8904 10282 7802 491 -1156 -904 C ATOM 2713 NH1 ARG A 517 15.457 65.525 -2.722 1.00 72.82 N ANISOU 2713 NH1 ARG A 517 9256 10507 7905 495 -1326 -1053 N ATOM 2714 NH2 ARG A 517 14.257 64.728 -4.513 1.00 64.80 N ANISOU 2714 NH2 ARG A 517 8154 9387 7079 479 -976 -863 N ATOM 2715 N ARG A 518 21.110 62.710 -7.539 1.00 62.43 N ANISOU 2715 N ARG A 518 6771 9224 7728 45 -1150 -421 N ATOM 2716 CA ARG A 518 21.511 61.734 -8.549 1.00 59.84 C ANISOU 2716 CA ARG A 518 6340 8869 7526 55 -952 -238 C ATOM 2717 C ARG A 518 22.456 62.357 -9.573 1.00 55.68 C ANISOU 2717 C ARG A 518 5674 8205 7278 -84 -916 -203 C ATOM 2718 O ARG A 518 22.198 63.446 -10.080 1.00 57.10 O ANISOU 2718 O ARG A 518 5911 8249 7536 -180 -916 -299 O ATOM 2719 CB ARG A 518 20.267 61.184 -9.253 1.00 63.29 C ANISOU 2719 CB ARG A 518 6935 9247 7865 115 -734 -190 C ATOM 2720 CG ARG A 518 20.539 60.175 -10.357 1.00 64.79 C ANISOU 2720 CG ARG A 518 7075 9387 8154 128 -519 -19 C ATOM 2721 CD ARG A 518 19.349 60.106 -11.297 1.00 62.57 C ANISOU 2721 CD ARG A 518 6957 8990 7825 131 -358 -22 C ATOM 2722 NE ARG A 518 19.332 58.897 -12.118 1.00 61.79 N ANISOU 2722 NE ARG A 518 6869 8863 7743 177 -159 126 N ATOM 2723 CZ ARG A 518 20.223 58.609 -13.064 1.00 66.96 C ANISOU 2723 CZ ARG A 518 7456 9439 8549 138 -42 241 C ATOM 2724 NH1 ARG A 518 21.241 59.428 -13.310 1.00 72.76 N ANISOU 2724 NH1 ARG A 518 8074 10113 9457 51 -97 238 N ATOM 2725 NH2 ARG A 518 20.098 57.486 -13.759 1.00 58.29 N ANISOU 2725 NH2 ARG A 518 6408 8306 7435 190 144 363 N ATOM 2726 N GLN A 519 23.551 61.661 -9.865 1.00 64.25 N ANISOU 2726 N GLN A 519 6577 9316 8520 -83 -867 -52 N ATOM 2727 CA GLN A 519 24.519 62.107 -10.864 1.00 68.74 C ANISOU 2727 CA GLN A 519 7000 9740 9379 -192 -787 21 C ATOM 2728 C GLN A 519 23.843 62.395 -12.195 1.00 70.69 C ANISOU 2728 C GLN A 519 7394 9807 9656 -222 -565 40 C ATOM 2729 O GLN A 519 23.045 61.592 -12.675 1.00 73.96 O ANISOU 2729 O GLN A 519 7948 10220 9933 -142 -403 104 O ATOM 2730 CB GLN A 519 25.592 61.035 -11.079 1.00 74.46 C ANISOU 2730 CB GLN A 519 7537 10513 10240 -145 -692 226 C ATOM 2731 CG GLN A 519 26.912 61.297 -10.377 1.00 80.33 C ANISOU 2731 CG GLN A 519 8022 11325 11175 -198 -903 240 C ATOM 2732 CD GLN A 519 27.674 62.456 -10.992 1.00 82.82 C ANISOU 2732 CD GLN A 519 8204 11466 11799 -352 -926 205 C ATOM 2733 OE1 GLN A 519 27.119 63.238 -11.765 1.00 83.79 O ANISOU 2733 OE1 GLN A 519 8458 11431 11949 -415 -819 135 O ATOM 2734 NE2 GLN A 519 28.950 62.573 -10.648 1.00 82.03 N ANISOU 2734 NE2 GLN A 519 7832 11388 11946 -409 -1065 262 N ATOM 2735 N THR A 520 24.166 63.534 -12.800 1.00 65.36 N ANISOU 2735 N THR A 520 6691 8975 9166 -335 -561 -17 N ATOM 2736 CA THR A 520 23.632 63.842 -14.124 1.00 61.46 C ANISOU 2736 CA THR A 520 6342 8305 8707 -349 -349 15 C ATOM 2737 C THR A 520 24.704 63.754 -15.203 1.00 62.76 C ANISOU 2737 C THR A 520 6391 8322 9133 -381 -164 174 C ATOM 2738 O THR A 520 24.389 63.667 -16.389 1.00 63.75 O ANISOU 2738 O THR A 520 6652 8307 9264 -355 49 247 O ATOM 2739 CB THR A 520 22.932 65.219 -14.182 1.00 63.19 C ANISOU 2739 CB THR A 520 6680 8424 8907 -420 -415 -155 C ATOM 2740 OG1 THR A 520 23.849 66.248 -13.793 1.00 68.99 O ANISOU 2740 OG1 THR A 520 7257 9106 9851 -535 -555 -234 O ATOM 2741 CG2 THR A 520 21.714 65.246 -13.260 1.00 59.88 C ANISOU 2741 CG2 THR A 520 6411 8121 8219 -365 -538 -286 C ATOM 2742 N LYS A 521 25.971 63.776 -14.801 1.00 61.80 N ANISOU 2742 N LYS A 521 6024 8224 9232 -429 -243 233 N ATOM 2743 CA LYS A 521 27.045 63.582 -15.772 1.00 67.97 C ANISOU 2743 CA LYS A 521 6677 8861 10288 -441 -39 416 C ATOM 2744 C LYS A 521 27.373 62.103 -15.984 1.00 71.88 C ANISOU 2744 C LYS A 521 7146 9425 10739 -331 118 613 C ATOM 2745 O LYS A 521 27.296 61.290 -15.062 1.00 69.77 O ANISOU 2745 O LYS A 521 6832 9347 10328 -270 2 619 O ATOM 2746 CB LYS A 521 28.295 64.404 -15.433 1.00 69.69 C ANISOU 2746 CB LYS A 521 6619 9024 10838 -557 -164 408 C ATOM 2747 CG LYS A 521 28.639 64.482 -13.965 1.00 74.71 C ANISOU 2747 CG LYS A 521 7092 9849 11446 -594 -493 298 C ATOM 2748 CD LYS A 521 29.627 65.608 -13.713 1.00 84.17 C ANISOU 2748 CD LYS A 521 8060 10952 12970 -741 -651 229 C ATOM 2749 CE LYS A 521 30.782 65.554 -14.702 1.00 89.90 C ANISOU 2749 CE LYS A 521 8585 11499 14074 -769 -427 433 C ATOM 2750 NZ LYS A 521 31.872 66.503 -14.338 1.00 94.79 N ANISOU 2750 NZ LYS A 521 8918 12036 15062 -916 -601 384 N ATOM 2751 N GLU A 522 27.718 61.768 -17.221 1.00 80.63 N ANISOU 2751 N GLU A 522 8308 10366 11961 -296 399 775 N ATOM 2752 CA GLU A 522 27.991 60.396 -17.619 1.00 81.17 C ANISOU 2752 CA GLU A 522 8397 10454 11988 -189 600 967 C ATOM 2753 C GLU A 522 28.378 60.406 -19.090 1.00 79.75 C ANISOU 2753 C GLU A 522 8317 10032 11951 -163 913 1117 C ATOM 2754 O GLU A 522 27.739 61.075 -19.902 1.00 71.88 O ANISOU 2754 O GLU A 522 7522 8893 10895 -176 993 1047 O ATOM 2755 CB GLU A 522 26.757 59.517 -17.399 1.00 76.03 C ANISOU 2755 CB GLU A 522 7965 9924 11000 -104 595 912 C ATOM 2756 CG GLU A 522 26.896 58.094 -17.925 1.00 76.88 C ANISOU 2756 CG GLU A 522 8144 10023 11045 3 828 1096 C ATOM 2757 CD GLU A 522 25.642 57.256 -17.704 1.00 77.74 C ANISOU 2757 CD GLU A 522 8455 10230 10851 73 820 1030 C ATOM 2758 OE1 GLU A 522 25.101 57.262 -16.576 1.00 74.37 O ANISOU 2758 OE1 GLU A 522 7992 9977 10288 78 616 914 O ATOM 2759 OE2 GLU A 522 25.205 56.583 -18.661 1.00 74.23 O ANISOU 2759 OE2 GLU A 522 8211 9679 10313 126 1023 1097 O ATOM 2760 N GLY A 523 29.427 59.671 -19.437 1.00 88.89 N ANISOU 2760 N GLY A 523 9345 11136 13292 -112 1099 1333 N ATOM 2761 CA GLY A 523 29.917 59.691 -20.800 1.00 93.80 C ANISOU 2761 CA GLY A 523 10065 11510 14066 -71 1421 1495 C ATOM 2762 C GLY A 523 30.525 61.042 -21.132 1.00 97.45 C ANISOU 2762 C GLY A 523 10403 11802 14821 -163 1427 1471 C ATOM 2763 O GLY A 523 30.360 61.558 -22.240 1.00 92.76 O ANISOU 2763 O GLY A 523 9995 10995 14253 -142 1631 1497 O ATOM 2764 N GLY A 524 31.225 61.618 -20.158 1.00 98.83 N ANISOU 2764 N GLY A 524 10270 12067 15215 -262 1197 1418 N ATOM 2765 CA GLY A 524 31.924 62.874 -20.350 1.00 96.43 C ANISOU 2765 CA GLY A 524 9795 11600 15244 -367 1188 1395 C ATOM 2766 C GLY A 524 31.017 64.087 -20.404 1.00 96.32 C ANISOU 2766 C GLY A 524 9944 11535 15118 -441 1072 1172 C ATOM 2767 O GLY A 524 31.497 65.218 -20.451 1.00 96.99 O ANISOU 2767 O GLY A 524 9895 11490 15467 -540 1040 1120 O ATOM 2768 N TYR A 525 29.705 63.858 -20.389 1.00 89.21 N ANISOU 2768 N TYR A 525 9322 10728 13845 -394 1014 1045 N ATOM 2769 CA TYR A 525 28.745 64.951 -20.525 1.00 87.80 C ANISOU 2769 CA TYR A 525 9323 10497 13542 -443 933 854 C ATOM 2770 C TYR A 525 27.743 65.033 -19.368 1.00 73.86 C ANISOU 2770 C TYR A 525 7607 8950 11505 -474 632 644 C ATOM 2771 O TYR A 525 27.372 64.018 -18.773 1.00 66.27 O ANISOU 2771 O TYR A 525 6671 8172 10339 -414 550 651 O ATOM 2772 CB TYR A 525 27.997 64.850 -21.862 1.00 98.79 C ANISOU 2772 CB TYR A 525 11042 11729 14764 -345 1188 906 C ATOM 2773 CG TYR A 525 27.287 66.130 -22.265 1.00110.15 C ANISOU 2773 CG TYR A 525 12634 13050 16168 -385 1174 765 C ATOM 2774 CD1 TYR A 525 27.973 67.154 -22.909 1.00115.20 C ANISOU 2774 CD1 TYR A 525 13212 13465 17093 -423 1327 810 C ATOM 2775 CD2 TYR A 525 25.933 66.315 -21.999 1.00110.18 C ANISOU 2775 CD2 TYR A 525 12834 13156 15871 -376 1025 599 C ATOM 2776 CE1 TYR A 525 27.333 68.326 -23.277 1.00116.59 C ANISOU 2776 CE1 TYR A 525 13532 13530 17238 -448 1333 691 C ATOM 2777 CE2 TYR A 525 25.284 67.485 -22.363 1.00111.08 C ANISOU 2777 CE2 TYR A 525 13083 13164 15957 -401 1023 484 C ATOM 2778 CZ TYR A 525 25.990 68.487 -23.001 1.00114.70 C ANISOU 2778 CZ TYR A 525 13490 13406 16684 -436 1177 529 C ATOM 2779 OH TYR A 525 25.351 69.652 -23.368 1.00112.25 O ANISOU 2779 OH TYR A 525 13319 12985 16347 -450 1193 424 O ATOM 2780 N ASP A 526 27.318 66.257 -19.061 1.00 60.54 N ANISOU 2780 N ASP A 526 5945 7230 9827 -560 491 465 N ATOM 2781 CA ASP A 526 26.276 66.511 -18.071 1.00 62.20 C ANISOU 2781 CA ASP A 526 6248 7605 9780 -579 245 266 C ATOM 2782 C ASP A 526 24.902 66.537 -18.750 1.00 57.51 C ANISOU 2782 C ASP A 526 5958 6973 8920 -508 341 217 C ATOM 2783 O ASP A 526 24.592 67.456 -19.507 1.00 62.59 O ANISOU 2783 O ASP A 526 6720 7455 9609 -525 441 181 O ATOM 2784 CB ASP A 526 26.543 67.834 -17.336 1.00 64.33 C ANISOU 2784 CB ASP A 526 6395 7848 10200 -710 42 95 C ATOM 2785 CG ASP A 526 25.628 68.036 -16.139 1.00 68.14 C ANISOU 2785 CG ASP A 526 6962 8505 10423 -719 -217 -99 C ATOM 2786 OD1 ASP A 526 24.500 67.508 -16.163 1.00 66.94 O ANISOU 2786 OD1 ASP A 526 7011 8434 9988 -630 -190 -119 O ATOM 2787 OD2 ASP A 526 26.031 68.718 -15.172 1.00 70.34 O ANISOU 2787 OD2 ASP A 526 7112 8828 10787 -813 -444 -231 O ATOM 2788 N HIS A 527 24.088 65.523 -18.465 1.00 52.20 N ANISOU 2788 N HIS A 527 5401 6447 7986 -426 308 219 N ATOM 2789 CA HIS A 527 22.771 65.365 -19.079 1.00 50.74 C ANISOU 2789 CA HIS A 527 5478 6239 7562 -357 377 185 C ATOM 2790 C HIS A 527 21.643 66.070 -18.328 1.00 50.50 C ANISOU 2790 C HIS A 527 5535 6289 7366 -379 196 2 C ATOM 2791 O HIS A 527 20.472 65.740 -18.520 1.00 49.81 O ANISOU 2791 O HIS A 527 5620 6233 7072 -317 204 -28 O ATOM 2792 CB HIS A 527 22.414 63.885 -19.152 1.00 55.92 C ANISOU 2792 CB HIS A 527 6206 6995 8046 -262 440 280 C ATOM 2793 CG HIS A 527 23.141 63.136 -20.219 1.00 66.19 C ANISOU 2793 CG HIS A 527 7534 8176 9437 -209 678 466 C ATOM 2794 ND1 HIS A 527 24.465 62.773 -20.104 1.00 67.27 N ANISOU 2794 ND1 HIS A 527 7468 8305 9788 -220 747 598 N ATOM 2795 CD2 HIS A 527 22.722 62.663 -21.417 1.00 72.15 C ANISOU 2795 CD2 HIS A 527 8509 8810 10095 -137 865 545 C ATOM 2796 CE1 HIS A 527 24.834 62.116 -21.188 1.00 71.72 C ANISOU 2796 CE1 HIS A 527 8130 8736 10383 -151 994 759 C ATOM 2797 NE2 HIS A 527 23.795 62.036 -22.002 1.00 74.39 N ANISOU 2797 NE2 HIS A 527 8740 9004 10522 -100 1064 723 N ATOM 2798 N ALA A 528 21.993 67.019 -17.468 1.00 45.98 N ANISOU 2798 N ALA A 528 4843 5738 6890 -465 36 -118 N ATOM 2799 CA ALA A 528 21.018 67.691 -16.617 1.00 44.78 C ANISOU 2799 CA ALA A 528 4776 5657 6582 -480 -129 -288 C ATOM 2800 C ALA A 528 19.864 68.257 -17.429 1.00 44.02 C ANISOU 2800 C ALA A 528 4890 5454 6379 -445 -34 -323 C ATOM 2801 O ALA A 528 18.715 68.236 -16.993 1.00 42.15 O ANISOU 2801 O ALA A 528 4769 5292 5953 -401 -103 -399 O ATOM 2802 CB ALA A 528 21.694 68.806 -15.804 1.00 44.69 C ANISOU 2802 CB ALA A 528 4632 5625 6722 -591 -290 -415 C ATOM 2803 N ILE A 529 20.178 68.757 -18.615 1.00 49.64 N ANISOU 2803 N ILE A 529 5652 5988 7223 -454 134 -256 N ATOM 2804 CA ILE A 529 19.177 69.378 -19.470 1.00 46.89 C ANISOU 2804 CA ILE A 529 5502 5528 6785 -413 222 -279 C ATOM 2805 C ILE A 529 18.092 68.376 -19.901 1.00 40.95 C ANISOU 2805 C ILE A 529 4907 4840 5812 -313 250 -229 C ATOM 2806 O ILE A 529 16.932 68.741 -20.086 1.00 42.99 O ANISOU 2806 O ILE A 529 5305 5088 5942 -275 227 -283 O ATOM 2807 CB ILE A 529 19.842 70.011 -20.705 1.00 52.07 C ANISOU 2807 CB ILE A 529 6192 5971 7622 -418 419 -194 C ATOM 2808 CG1 ILE A 529 18.810 70.741 -21.559 1.00 57.05 C ANISOU 2808 CG1 ILE A 529 7036 6491 8150 -362 497 -218 C ATOM 2809 CG2 ILE A 529 20.587 68.953 -21.517 1.00 52.62 C ANISOU 2809 CG2 ILE A 529 6252 5996 7743 -363 580 -22 C ATOM 2810 CD1 ILE A 529 19.400 71.321 -22.819 1.00 60.76 C ANISOU 2810 CD1 ILE A 529 7576 6742 8767 -336 715 -122 C ATOM 2811 N SER A 530 18.471 67.112 -20.039 1.00 35.23 N ANISOU 2811 N SER A 530 4150 4176 5058 -272 300 -123 N ATOM 2812 CA SER A 530 17.527 66.076 -20.426 1.00 36.72 C ANISOU 2812 CA SER A 530 4474 4414 5062 -192 322 -81 C ATOM 2813 C SER A 530 16.582 65.746 -19.274 1.00 35.95 C ANISOU 2813 C SER A 530 4355 4481 4822 -177 168 -170 C ATOM 2814 O SER A 530 15.377 65.585 -19.466 1.00 38.53 O ANISOU 2814 O SER A 530 4802 4819 5020 -131 144 -196 O ATOM 2815 CB SER A 530 18.274 64.830 -20.897 1.00 35.11 C ANISOU 2815 CB SER A 530 4250 4209 4880 -154 444 59 C ATOM 2816 OG SER A 530 19.016 65.132 -22.058 1.00 44.53 O ANISOU 2816 OG SER A 530 5505 5225 6191 -144 620 155 O ATOM 2817 N PHE A 531 17.131 65.661 -18.073 1.00 31.38 N ANISOU 2817 N PHE A 531 3626 4023 4275 -208 63 -210 N ATOM 2818 CA PHE A 531 16.312 65.423 -16.895 1.00 35.42 C ANISOU 2818 CA PHE A 531 4132 4677 4649 -176 -64 -289 C ATOM 2819 C PHE A 531 15.291 66.542 -16.677 1.00 33.66 C ANISOU 2819 C PHE A 531 4003 4414 4371 -183 -126 -404 C ATOM 2820 O PHE A 531 14.141 66.282 -16.315 1.00 39.79 O ANISOU 2820 O PHE A 531 4851 5245 5025 -127 -157 -431 O ATOM 2821 CB PHE A 531 17.197 65.235 -15.666 1.00 41.00 C ANISOU 2821 CB PHE A 531 4681 5510 5386 -198 -175 -314 C ATOM 2822 CG PHE A 531 17.899 63.915 -15.636 1.00 40.79 C ANISOU 2822 CG PHE A 531 4565 5563 5370 -158 -119 -191 C ATOM 2823 CD1 PHE A 531 17.233 62.776 -15.209 1.00 38.07 C ANISOU 2823 CD1 PHE A 531 4254 5327 4883 -73 -106 -154 C ATOM 2824 CD2 PHE A 531 19.219 63.803 -16.053 1.00 41.15 C ANISOU 2824 CD2 PHE A 531 4488 5563 5586 -198 -59 -101 C ATOM 2825 CE1 PHE A 531 17.874 61.551 -15.188 1.00 41.82 C ANISOU 2825 CE1 PHE A 531 4655 5869 5368 -30 -34 -34 C ATOM 2826 CE2 PHE A 531 19.861 62.579 -16.040 1.00 37.85 C ANISOU 2826 CE2 PHE A 531 3988 5212 5182 -151 13 28 C ATOM 2827 CZ PHE A 531 19.191 61.452 -15.599 1.00 40.34 C ANISOU 2827 CZ PHE A 531 4350 5640 5336 -66 25 59 C ATOM 2828 N GLN A 532 15.709 67.780 -16.924 1.00 36.34 N ANISOU 2828 N GLN A 532 4341 4646 4821 -249 -125 -461 N ATOM 2829 CA GLN A 532 14.826 68.936 -16.792 1.00 37.35 C ANISOU 2829 CA GLN A 532 4565 4714 4913 -255 -157 -560 C ATOM 2830 C GLN A 532 13.708 68.863 -17.827 1.00 35.54 C ANISOU 2830 C GLN A 532 4477 4414 4612 -192 -77 -511 C ATOM 2831 O GLN A 532 12.545 69.118 -17.526 1.00 35.63 O ANISOU 2831 O GLN A 532 4560 4445 4533 -150 -115 -554 O ATOM 2832 CB GLN A 532 15.622 70.238 -16.938 1.00 47.89 C ANISOU 2832 CB GLN A 532 5863 5927 6407 -343 -148 -621 C ATOM 2833 CG GLN A 532 16.594 70.492 -15.788 1.00 62.68 C ANISOU 2833 CG GLN A 532 7597 7865 8354 -418 -280 -703 C ATOM 2834 CD GLN A 532 17.579 71.619 -16.074 1.00 76.74 C ANISOU 2834 CD GLN A 532 9304 9503 10350 -523 -259 -747 C ATOM 2835 OE1 GLN A 532 17.522 72.261 -17.128 1.00 84.32 O ANISOU 2835 OE1 GLN A 532 10329 10310 11400 -528 -121 -710 O ATOM 2836 NE2 GLN A 532 18.492 71.860 -15.134 1.00 71.15 N ANISOU 2836 NE2 GLN A 532 8461 8840 9734 -603 -400 -824 N ATOM 2837 N ASP A 533 14.084 68.492 -19.042 1.00 33.97 N ANISOU 2837 N ASP A 533 4322 4128 4456 -180 31 -415 N ATOM 2838 CA ASP A 533 13.152 68.236 -20.124 1.00 38.40 C ANISOU 2838 CA ASP A 533 5029 4625 4937 -115 84 -361 C ATOM 2839 C ASP A 533 12.078 67.232 -19.681 1.00 39.89 C ANISOU 2839 C ASP A 533 5228 4926 5001 -62 15 -356 C ATOM 2840 O ASP A 533 10.883 67.504 -19.774 1.00 42.03 O ANISOU 2840 O ASP A 533 5569 5187 5213 -23 -25 -381 O ATOM 2841 CB ASP A 533 13.938 67.674 -21.314 1.00 49.67 C ANISOU 2841 CB ASP A 533 6508 5959 6405 -100 211 -252 C ATOM 2842 CG ASP A 533 13.328 68.036 -22.654 1.00 63.31 C ANISOU 2842 CG ASP A 533 8422 7553 8081 -42 279 -213 C ATOM 2843 OD1 ASP A 533 12.216 67.564 -22.956 1.00 59.03 O ANISOU 2843 OD1 ASP A 533 7971 7037 7419 9 219 -212 O ATOM 2844 OD2 ASP A 533 13.980 68.781 -23.417 1.00 74.02 O ANISOU 2844 OD2 ASP A 533 9830 8771 9522 -42 391 -180 O ATOM 2845 N TRP A 534 12.509 66.072 -19.193 1.00 33.70 N ANISOU 2845 N TRP A 534 4365 4242 4199 -57 10 -316 N ATOM 2846 CA TRP A 534 11.568 65.014 -18.822 1.00 33.99 C ANISOU 2846 CA TRP A 534 4405 4367 4144 -5 -26 -299 C ATOM 2847 C TRP A 534 10.700 65.414 -17.628 1.00 31.95 C ANISOU 2847 C TRP A 534 4110 4187 3844 19 -107 -374 C ATOM 2848 O TRP A 534 9.534 65.040 -17.545 1.00 26.64 O ANISOU 2848 O TRP A 534 3465 3529 3126 66 -127 -368 O ATOM 2849 CB TRP A 534 12.308 63.708 -18.528 1.00 31.98 C ANISOU 2849 CB TRP A 534 4075 4194 3884 5 14 -231 C ATOM 2850 CG TRP A 534 13.172 63.225 -19.671 1.00 31.09 C ANISOU 2850 CG TRP A 534 4011 3992 3811 -4 124 -141 C ATOM 2851 CD1 TRP A 534 12.876 63.275 -21.005 1.00 30.90 C ANISOU 2851 CD1 TRP A 534 4138 3839 3764 13 181 -105 C ATOM 2852 CD2 TRP A 534 14.447 62.589 -19.568 1.00 31.79 C ANISOU 2852 CD2 TRP A 534 4012 4108 3961 -16 197 -65 C ATOM 2853 NE1 TRP A 534 13.899 62.723 -21.738 1.00 35.89 N ANISOU 2853 NE1 TRP A 534 4801 4405 4433 16 304 -12 N ATOM 2854 CE2 TRP A 534 14.879 62.300 -20.879 1.00 37.66 C ANISOU 2854 CE2 TRP A 534 4865 4720 4723 -4 323 20 C ATOM 2855 CE3 TRP A 534 15.275 62.248 -18.494 1.00 30.36 C ANISOU 2855 CE3 TRP A 534 3672 4044 3818 -25 168 -54 C ATOM 2856 CZ2 TRP A 534 16.103 61.679 -21.144 1.00 37.49 C ANISOU 2856 CZ2 TRP A 534 4793 4675 4777 -2 443 126 C ATOM 2857 CZ3 TRP A 534 16.487 61.633 -18.759 1.00 33.09 C ANISOU 2857 CZ3 TRP A 534 3948 4380 4246 -28 264 50 C ATOM 2858 CH2 TRP A 534 16.889 61.354 -20.073 1.00 34.85 C ANISOU 2858 CH2 TRP A 534 4275 4463 4505 -18 412 144 C ATOM 2859 N LEU A 535 11.276 66.178 -16.708 1.00 26.27 N ANISOU 2859 N LEU A 535 3334 3502 3146 -13 -151 -444 N ATOM 2860 CA LEU A 535 10.547 66.650 -15.538 1.00 31.10 C ANISOU 2860 CA LEU A 535 3948 4170 3701 20 -212 -518 C ATOM 2861 C LEU A 535 9.430 67.625 -15.905 1.00 37.99 C ANISOU 2861 C LEU A 535 4909 4952 4574 38 -206 -549 C ATOM 2862 O LEU A 535 8.323 67.557 -15.368 1.00 39.19 O ANISOU 2862 O LEU A 535 5081 5128 4682 100 -214 -553 O ATOM 2863 CB LEU A 535 11.507 67.332 -14.570 1.00 29.50 C ANISOU 2863 CB LEU A 535 3692 4005 3513 -27 -278 -600 C ATOM 2864 CG LEU A 535 10.906 67.812 -13.257 1.00 34.53 C ANISOU 2864 CG LEU A 535 4366 4693 4061 17 -339 -685 C ATOM 2865 CD1 LEU A 535 10.113 66.690 -12.599 1.00 35.77 C ANISOU 2865 CD1 LEU A 535 4519 4945 4125 118 -319 -633 C ATOM 2866 CD2 LEU A 535 12.018 68.292 -12.354 1.00 40.58 C ANISOU 2866 CD2 LEU A 535 5085 5502 4832 -35 -437 -771 C ATOM 2867 N LYS A 536 9.741 68.539 -16.813 1.00 32.53 N ANISOU 2867 N LYS A 536 4266 4149 3944 -6 -176 -559 N ATOM 2868 CA LYS A 536 8.781 69.519 -17.287 1.00 31.49 C ANISOU 2868 CA LYS A 536 4221 3924 3818 18 -159 -574 C ATOM 2869 C LYS A 536 7.583 68.821 -17.928 1.00 33.39 C ANISOU 2869 C LYS A 536 4497 4162 4028 82 -165 -504 C ATOM 2870 O LYS A 536 6.436 69.205 -17.699 1.00 36.02 O ANISOU 2870 O LYS A 536 4850 4482 4354 131 -178 -506 O ATOM 2871 CB LYS A 536 9.457 70.455 -18.285 1.00 40.28 C ANISOU 2871 CB LYS A 536 5386 4912 5007 -27 -102 -576 C ATOM 2872 CG LYS A 536 8.552 71.486 -18.942 1.00 54.91 C ANISOU 2872 CG LYS A 536 7338 6661 6865 10 -70 -574 C ATOM 2873 CD LYS A 536 9.350 72.311 -19.959 1.00 63.69 C ANISOU 2873 CD LYS A 536 8507 7640 8053 -21 17 -561 C ATOM 2874 CE LYS A 536 8.610 73.566 -20.400 1.00 68.05 C ANISOU 2874 CE LYS A 536 9154 8085 8617 17 63 -571 C ATOM 2875 NZ LYS A 536 9.423 74.374 -21.364 1.00 69.26 N ANISOU 2875 NZ LYS A 536 9368 8096 8853 0 175 -551 N ATOM 2876 N LYS A 537 7.851 67.795 -18.731 1.00 27.52 N ANISOU 2876 N LYS A 537 3758 3422 3276 80 -154 -439 N ATOM 2877 CA LYS A 537 6.777 67.022 -19.340 1.00 31.85 C ANISOU 2877 CA LYS A 537 4335 3962 3802 126 -186 -385 C ATOM 2878 C LYS A 537 5.882 66.411 -18.260 1.00 34.22 C ANISOU 2878 C LYS A 537 4554 4348 4099 168 -212 -385 C ATOM 2879 O LYS A 537 4.664 66.544 -18.313 1.00 33.55 O ANISOU 2879 O LYS A 537 4468 4239 4041 211 -243 -368 O ATOM 2880 CB LYS A 537 7.345 65.923 -20.242 1.00 35.08 C ANISOU 2880 CB LYS A 537 4781 4357 4190 113 -164 -328 C ATOM 2881 CG LYS A 537 7.819 66.389 -21.622 1.00 35.65 C ANISOU 2881 CG LYS A 537 4981 4310 4254 109 -124 -300 C ATOM 2882 CD LYS A 537 8.775 65.366 -22.238 1.00 42.36 C ANISOU 2882 CD LYS A 537 5868 5142 5084 96 -59 -243 C ATOM 2883 CE LYS A 537 8.384 64.992 -23.655 1.00 44.44 C ANISOU 2883 CE LYS A 537 6299 5305 5282 133 -66 -200 C ATOM 2884 NZ LYS A 537 8.359 66.150 -24.575 1.00 51.20 N ANISOU 2884 NZ LYS A 537 7282 6046 6127 164 -43 -197 N ATOM 2885 N LEU A 538 6.498 65.753 -17.279 1.00 30.79 N ANISOU 2885 N LEU A 538 4049 4007 3642 166 -193 -394 N ATOM 2886 CA LEU A 538 5.760 65.097 -16.208 1.00 38.02 C ANISOU 2886 CA LEU A 538 4901 4997 4550 224 -186 -381 C ATOM 2887 C LEU A 538 4.986 66.104 -15.361 1.00 37.41 C ANISOU 2887 C LEU A 538 4837 4905 4472 270 -184 -421 C ATOM 2888 O LEU A 538 3.858 65.841 -14.941 1.00 32.78 O ANISOU 2888 O LEU A 538 4221 4317 3918 335 -164 -386 O ATOM 2889 CB LEU A 538 6.707 64.265 -15.330 1.00 35.76 C ANISOU 2889 CB LEU A 538 4555 4815 4218 229 -161 -378 C ATOM 2890 CG LEU A 538 7.297 63.009 -15.980 1.00 35.03 C ANISOU 2890 CG LEU A 538 4440 4740 4129 208 -131 -316 C ATOM 2891 CD1 LEU A 538 8.481 62.437 -15.191 1.00 30.75 C ANISOU 2891 CD1 LEU A 538 3835 4299 3550 211 -107 -306 C ATOM 2892 CD2 LEU A 538 6.220 61.956 -16.162 1.00 31.05 C ANISOU 2892 CD2 LEU A 538 3916 4226 3655 248 -113 -263 C ATOM 2893 N HIS A 539 5.594 67.259 -15.119 1.00 37.03 N ANISOU 2893 N HIS A 539 4834 4833 4404 237 -190 -490 N ATOM 2894 CA HIS A 539 4.958 68.302 -14.325 1.00 35.28 C ANISOU 2894 CA HIS A 539 4656 4579 4169 279 -173 -535 C ATOM 2895 C HIS A 539 3.757 68.890 -15.059 1.00 39.30 C ANISOU 2895 C HIS A 539 5193 4998 4743 310 -160 -493 C ATOM 2896 O HIS A 539 2.702 69.131 -14.469 1.00 33.11 O ANISOU 2896 O HIS A 539 4408 4194 3980 383 -123 -470 O ATOM 2897 CB HIS A 539 5.958 69.410 -14.002 1.00 41.67 C ANISOU 2897 CB HIS A 539 5513 5364 4954 218 -190 -631 C ATOM 2898 CG HIS A 539 5.369 70.544 -13.224 1.00 47.07 C ANISOU 2898 CG HIS A 539 6274 5997 5614 256 -163 -688 C ATOM 2899 ND1 HIS A 539 4.833 71.661 -13.830 1.00 58.57 N ANISOU 2899 ND1 HIS A 539 7790 7344 7119 253 -127 -692 N ATOM 2900 CD2 HIS A 539 5.232 70.735 -11.890 1.00 43.52 C ANISOU 2900 CD2 HIS A 539 5872 5580 5085 310 -155 -740 C ATOM 2901 CE1 HIS A 539 4.391 72.492 -12.901 1.00 62.60 C ANISOU 2901 CE1 HIS A 539 8376 7819 7592 295 -89 -743 C ATOM 2902 NE2 HIS A 539 4.623 71.954 -11.716 1.00 53.04 N ANISOU 2902 NE2 HIS A 539 7168 6689 6295 332 -107 -777 N ATOM 2903 N SER A 540 3.923 69.127 -16.353 1.00 32.90 N ANISOU 2903 N SER A 540 4412 4125 3964 268 -185 -474 N ATOM 2904 CA SER A 540 2.827 69.631 -17.159 1.00 37.19 C ANISOU 2904 CA SER A 540 4982 4589 4560 306 -197 -425 C ATOM 2905 C SER A 540 1.655 68.630 -17.153 1.00 38.41 C ANISOU 2905 C SER A 540 5057 4766 4772 358 -227 -351 C ATOM 2906 O SER A 540 0.503 69.020 -16.972 1.00 32.90 O ANISOU 2906 O SER A 540 4331 4029 4139 418 -217 -309 O ATOM 2907 CB SER A 540 3.311 69.934 -18.579 1.00 38.65 C ANISOU 2907 CB SER A 540 5238 4706 4743 268 -219 -413 C ATOM 2908 OG SER A 540 2.234 70.324 -19.410 1.00 53.87 O ANISOU 2908 OG SER A 540 7195 6567 6705 317 -255 -360 O ATOM 2909 N ARG A 541 1.953 67.343 -17.320 1.00 34.29 N ANISOU 2909 N ARG A 541 4489 4296 4242 336 -254 -329 N ATOM 2910 CA ARG A 541 0.901 66.318 -17.296 1.00 30.03 C ANISOU 2910 CA ARG A 541 3863 3765 3783 372 -279 -266 C ATOM 2911 C ARG A 541 0.209 66.241 -15.932 1.00 29.44 C ANISOU 2911 C ARG A 541 3718 3717 3752 446 -199 -245 C ATOM 2912 O ARG A 541 -1.017 66.222 -15.853 1.00 28.84 O ANISOU 2912 O ARG A 541 3574 3597 3788 499 -194 -184 O ATOM 2913 CB ARG A 541 1.447 64.936 -17.683 1.00 22.61 C ANISOU 2913 CB ARG A 541 2904 2864 2824 331 -299 -254 C ATOM 2914 CG ARG A 541 0.381 63.805 -17.626 1.00 26.17 C ANISOU 2914 CG ARG A 541 3254 3308 3381 356 -320 -196 C ATOM 2915 CD ARG A 541 -0.733 64.040 -18.659 1.00 32.03 C ANISOU 2915 CD ARG A 541 3989 3968 4215 356 -432 -164 C ATOM 2916 NE ARG A 541 -0.175 64.149 -20.003 1.00 35.63 N ANISOU 2916 NE ARG A 541 4567 4383 4588 308 -516 -188 N ATOM 2917 CZ ARG A 541 -0.211 63.181 -20.913 1.00 35.05 C ANISOU 2917 CZ ARG A 541 4529 4279 4509 271 -597 -183 C ATOM 2918 NH1 ARG A 541 -0.801 62.023 -20.637 1.00 32.01 N ANISOU 2918 NH1 ARG A 541 4044 3898 4219 262 -611 -161 N ATOM 2919 NH2 ARG A 541 0.339 63.374 -22.106 1.00 36.58 N ANISOU 2919 NH2 ARG A 541 4873 4423 4602 249 -652 -201 N ATOM 2920 N VAL A 542 0.995 66.199 -14.861 1.00 35.37 N ANISOU 2920 N VAL A 542 4489 4534 4417 458 -136 -288 N ATOM 2921 CA VAL A 542 0.434 66.109 -13.513 1.00 34.37 C ANISOU 2921 CA VAL A 542 4337 4427 4296 551 -43 -267 C ATOM 2922 C VAL A 542 -0.399 67.344 -13.148 1.00 43.72 C ANISOU 2922 C VAL A 542 5563 5536 5512 610 6 -261 C ATOM 2923 O VAL A 542 -1.447 67.224 -12.505 1.00 41.55 O ANISOU 2923 O VAL A 542 5243 5226 5317 701 89 -193 O ATOM 2924 CB VAL A 542 1.535 65.840 -12.465 1.00 35.88 C ANISOU 2924 CB VAL A 542 4567 4708 4356 561 -11 -322 C ATOM 2925 CG1 VAL A 542 1.013 66.057 -11.033 1.00 31.13 C ANISOU 2925 CG1 VAL A 542 4004 4111 3715 677 90 -314 C ATOM 2926 CG2 VAL A 542 2.078 64.429 -12.646 1.00 30.52 C ANISOU 2926 CG2 VAL A 542 3824 4099 3673 538 -17 -290 C ATOM 2927 N THR A 543 0.057 68.517 -13.581 1.00 35.05 N ANISOU 2927 N THR A 543 4550 4399 4367 563 -25 -321 N ATOM 2928 CA THR A 543 -0.699 69.754 -13.407 1.00 36.37 C ANISOU 2928 CA THR A 543 4769 4482 4568 614 30 -311 C ATOM 2929 C THR A 543 -2.053 69.670 -14.108 1.00 37.85 C ANISOU 2929 C THR A 543 4866 4606 4909 657 18 -205 C ATOM 2930 O THR A 543 -3.087 69.944 -13.504 1.00 36.88 O ANISOU 2930 O THR A 543 4713 4431 4868 748 106 -137 O ATOM 2931 CB THR A 543 0.076 70.973 -13.952 1.00 39.41 C ANISOU 2931 CB THR A 543 5254 4824 4896 546 4 -390 C ATOM 2932 OG1 THR A 543 1.273 71.162 -13.188 1.00 38.76 O ANISOU 2932 OG1 THR A 543 5237 4788 4701 502 3 -493 O ATOM 2933 CG2 THR A 543 -0.768 72.240 -13.872 1.00 39.30 C ANISOU 2933 CG2 THR A 543 5296 4710 4924 604 77 -369 C ATOM 2934 N LYS A 544 -2.059 69.276 -15.377 1.00 33.89 N ANISOU 2934 N LYS A 544 4325 4100 4450 599 -94 -184 N ATOM 2935 CA LYS A 544 -3.313 69.244 -16.123 1.00 34.39 C ANISOU 2935 CA LYS A 544 4301 4105 4660 633 -150 -91 C ATOM 2936 C LYS A 544 -4.303 68.205 -15.589 1.00 33.81 C ANISOU 2936 C LYS A 544 4084 4032 4732 685 -122 -8 C ATOM 2937 O LYS A 544 -5.506 68.427 -15.636 1.00 36.57 O ANISOU 2937 O LYS A 544 4340 4317 5237 745 -112 83 O ATOM 2938 CB LYS A 544 -3.061 69.053 -17.620 1.00 30.49 C ANISOU 2938 CB LYS A 544 3833 3601 4149 567 -294 -99 C ATOM 2939 CG LYS A 544 -2.212 70.184 -18.209 1.00 38.84 C ANISOU 2939 CG LYS A 544 5029 4630 5097 536 -288 -158 C ATOM 2940 CD LYS A 544 -2.203 70.192 -19.731 1.00 38.95 C ANISOU 2940 CD LYS A 544 5098 4607 5094 513 -408 -141 C ATOM 2941 CE LYS A 544 -1.180 69.238 -20.309 1.00 41.86 C ANISOU 2941 CE LYS A 544 5516 5012 5376 442 -458 -184 C ATOM 2942 NZ LYS A 544 -0.877 69.598 -21.736 1.00 37.30 N ANISOU 2942 NZ LYS A 544 5064 4376 4731 437 -527 -181 N ATOM 2943 N GLU A 545 -3.789 67.095 -15.056 1.00 31.96 N ANISOU 2943 N GLU A 545 3821 3860 4461 668 -95 -29 N ATOM 2944 CA GLU A 545 -4.632 65.996 -14.591 1.00 38.08 C ANISOU 2944 CA GLU A 545 4457 4624 5387 713 -50 51 C ATOM 2945 C GLU A 545 -4.717 65.920 -13.068 1.00 37.07 C ANISOU 2945 C GLU A 545 4341 4507 5238 815 130 74 C ATOM 2946 O GLU A 545 -5.055 64.872 -12.515 1.00 32.86 O ANISOU 2946 O GLU A 545 3720 3978 4788 858 203 127 O ATOM 2947 CB GLU A 545 -4.118 64.660 -15.152 1.00 39.35 C ANISOU 2947 CB GLU A 545 4581 4832 5538 636 -131 28 C ATOM 2948 CG GLU A 545 -4.607 64.371 -16.561 1.00 48.85 C ANISOU 2948 CG GLU A 545 5740 5989 6831 569 -303 41 C ATOM 2949 CD GLU A 545 -6.123 64.286 -16.628 1.00 59.45 C ANISOU 2949 CD GLU A 545 6922 7251 8414 613 -331 139 C ATOM 2950 OE1 GLU A 545 -6.677 63.205 -16.331 1.00 54.80 O ANISOU 2950 OE1 GLU A 545 6202 6640 7978 618 -306 186 O ATOM 2951 OE2 GLU A 545 -6.765 65.304 -16.974 1.00 71.34 O ANISOU 2951 OE2 GLU A 545 8422 8709 9974 646 -371 175 O ATOM 2952 N ARG A 546 -4.422 67.024 -12.389 1.00 29.54 N ANISOU 2952 N ARG A 546 4298 3348 3578 870 -552 -639 N ATOM 2953 CA ARG A 546 -4.304 66.990 -10.931 1.00 39.63 C ANISOU 2953 CA ARG A 546 5510 4819 4728 875 -424 -732 C ATOM 2954 C ARG A 546 -5.580 66.498 -10.232 1.00 39.49 C ANISOU 2954 C ARG A 546 5352 4872 4779 962 -350 -700 C ATOM 2955 O ARG A 546 -5.508 65.769 -9.245 1.00 35.17 O ANISOU 2955 O ARG A 546 4729 4519 4115 954 -275 -691 O ATOM 2956 CB ARG A 546 -3.862 68.348 -10.374 1.00 40.28 C ANISOU 2956 CB ARG A 546 5660 4874 4770 859 -359 -918 C ATOM 2957 CG ARG A 546 -4.909 69.436 -10.462 1.00 56.61 C ANISOU 2957 CG ARG A 546 7714 6779 7015 939 -328 -1001 C ATOM 2958 CD ARG A 546 -4.364 70.766 -9.955 1.00 66.49 C ANISOU 2958 CD ARG A 546 9044 8002 8218 912 -259 -1186 C ATOM 2959 NE ARG A 546 -5.243 71.883 -10.301 1.00 74.03 N ANISOU 2959 NE ARG A 546 10003 8760 9363 983 -249 -1256 N ATOM 2960 CZ ARG A 546 -5.172 72.567 -11.441 1.00 74.26 C ANISOU 2960 CZ ARG A 546 10120 8588 9509 982 -349 -1247 C ATOM 2961 NH1 ARG A 546 -4.259 72.253 -12.356 1.00 67.34 N ANISOU 2961 NH1 ARG A 546 9337 7676 8572 911 -464 -1177 N ATOM 2962 NH2 ARG A 546 -6.015 73.567 -11.670 1.00 71.95 N ANISOU 2962 NH2 ARG A 546 9819 8124 9396 1050 -332 -1307 N ATOM 2963 N HIS A 547 -6.738 66.886 -10.759 1.00 32.08 N ANISOU 2963 N HIS A 547 4379 3776 4033 1041 -373 -678 N ATOM 2964 CA HIS A 547 -8.023 66.490 -10.182 1.00 43.48 C ANISOU 2964 CA HIS A 547 5692 5264 5565 1129 -306 -649 C ATOM 2965 C HIS A 547 -8.280 64.987 -10.228 1.00 40.94 C ANISOU 2965 C HIS A 547 5290 5064 5203 1132 -331 -489 C ATOM 2966 O HIS A 547 -8.625 64.388 -9.212 1.00 40.17 O ANISOU 2966 O HIS A 547 5097 5130 5038 1156 -243 -493 O ATOM 2967 CB HIS A 547 -9.171 67.261 -10.839 1.00 43.32 C ANISOU 2967 CB HIS A 547 5653 5033 5772 1210 -337 -649 C ATOM 2968 CG HIS A 547 -9.141 68.727 -10.536 1.00 58.15 C ANISOU 2968 CG HIS A 547 7581 6809 7703 1225 -278 -817 C ATOM 2969 ND1 HIS A 547 -8.784 69.677 -11.469 1.00 62.62 N ANISOU 2969 ND1 HIS A 547 8254 7190 8349 1204 -357 -850 N ATOM 2970 CD2 HIS A 547 -9.387 69.402 -9.387 1.00 62.84 C ANISOU 2970 CD2 HIS A 547 8136 7463 8276 1252 -143 -966 C ATOM 2971 CE1 HIS A 547 -8.835 70.877 -10.915 1.00 67.44 C ANISOU 2971 CE1 HIS A 547 8885 7747 8990 1224 -272 -1010 C ATOM 2972 NE2 HIS A 547 -9.199 70.737 -9.652 1.00 65.45 N ANISOU 2972 NE2 HIS A 547 8548 7642 8680 1251 -138 -1084 N ATOM 2973 N ARG A 548 -8.108 64.373 -11.393 1.00 37.42 N ANISOU 2973 N ARG A 548 4884 4537 4796 1102 -446 -350 N ATOM 2974 CA ARG A 548 -8.259 62.925 -11.480 1.00 35.73 C ANISOU 2974 CA ARG A 548 4602 4436 4536 1096 -466 -197 C ATOM 2975 C ARG A 548 -7.162 62.212 -10.684 1.00 41.27 C ANISOU 2975 C ARG A 548 5303 5347 5030 1027 -418 -203 C ATOM 2976 O ARG A 548 -7.415 61.187 -10.046 1.00 34.74 O ANISOU 2976 O ARG A 548 4383 4680 4138 1041 -370 -136 O ATOM 2977 CB ARG A 548 -8.319 62.444 -12.940 1.00 37.60 C ANISOU 2977 CB ARG A 548 4890 4533 4864 1068 -594 -50 C ATOM 2978 CG ARG A 548 -9.756 62.314 -13.478 1.00 48.16 C ANISOU 2978 CG ARG A 548 6155 5757 6385 1148 -627 39 C ATOM 2979 CD ARG A 548 -9.822 61.927 -14.967 1.00 49.86 C ANISOU 2979 CD ARG A 548 6429 5825 6690 1106 -757 182 C ATOM 2980 NE ARG A 548 -9.583 63.075 -15.844 1.00 46.55 N ANISOU 2980 NE ARG A 548 6117 5206 6363 1080 -835 129 N ATOM 2981 CZ ARG A 548 -10.528 63.880 -16.336 1.00 43.05 C ANISOU 2981 CZ ARG A 548 5663 4595 6099 1136 -872 123 C ATOM 2982 NH1 ARG A 548 -11.823 63.683 -16.063 1.00 41.62 N ANISOU 2982 NH1 ARG A 548 5367 4413 6034 1224 -840 168 N ATOM 2983 NH2 ARG A 548 -10.174 64.895 -17.113 1.00 38.33 N ANISOU 2983 NH2 ARG A 548 5169 3826 5569 1102 -944 74 N ATOM 2984 N LEU A 549 -5.957 62.782 -10.687 1.00 37.74 N ANISOU 2984 N LEU A 549 4956 4902 4481 952 -429 -283 N ATOM 2985 CA LEU A 549 -4.826 62.159 -10.012 1.00 35.50 C ANISOU 2985 CA LEU A 549 4676 4807 4005 877 -395 -280 C ATOM 2986 C LEU A 549 -4.990 62.169 -8.496 1.00 41.72 C ANISOU 2986 C LEU A 549 5379 5782 4689 895 -271 -370 C ATOM 2987 O LEU A 549 -4.554 61.244 -7.818 1.00 32.55 O ANISOU 2987 O LEU A 549 4163 4808 3397 860 -234 -318 O ATOM 2988 CB LEU A 549 -3.508 62.824 -10.416 1.00 40.49 C ANISOU 2988 CB LEU A 549 5439 5388 4559 792 -439 -346 C ATOM 2989 CG LEU A 549 -2.969 62.492 -11.814 1.00 42.02 C ANISOU 2989 CG LEU A 549 5721 5449 4796 739 -558 -240 C ATOM 2990 CD1 LEU A 549 -1.805 63.422 -12.175 1.00 32.18 C ANISOU 2990 CD1 LEU A 549 4608 4127 3492 666 -596 -336 C ATOM 2991 CD2 LEU A 549 -2.540 61.030 -11.887 1.00 35.00 C ANISOU 2991 CD2 LEU A 549 4786 4685 3827 697 -572 -91 C ATOM 2992 N SER A 550 -5.628 63.209 -7.965 1.00 30.26 N ANISOU 2992 N SER A 550 3916 4280 3300 945 -203 -504 N ATOM 2993 CA SER A 550 -5.812 63.312 -6.518 1.00 39.98 C ANISOU 2993 CA SER A 550 5074 5680 4436 951 -78 -604 C ATOM 2994 C SER A 550 -6.812 62.292 -5.935 1.00 35.68 C ANISOU 2994 C SER A 550 4394 5252 3910 1011 -28 -523 C ATOM 2995 O SER A 550 -6.857 62.096 -4.726 1.00 39.88 O ANISOU 2995 O SER A 550 4861 5955 4338 1000 69 -580 O ATOM 2996 CB SER A 550 -6.173 64.751 -6.110 1.00 40.86 C ANISOU 2996 CB SER A 550 5218 5698 4610 980 -7 -780 C ATOM 2997 OG SER A 550 -7.376 65.182 -6.726 1.00 46.47 O ANISOU 2997 OG SER A 550 5901 6228 5529 1071 -28 -768 O ATOM 2998 N ARG A 551 -7.590 61.638 -6.795 1.00 35.69 N ANISOU 2998 N ARG A 551 4358 5165 4040 1066 -96 -391 N ATOM 2999 CA ARG A 551 -8.463 60.533 -6.376 1.00 42.37 C ANISOU 2999 CA ARG A 551 5081 6121 4897 1117 -62 -293 C ATOM 3000 C ARG A 551 -7.681 59.294 -5.924 1.00 44.83 C ANISOU 3000 C ARG A 551 5358 6636 5041 1055 -57 -200 C ATOM 3001 O ARG A 551 -8.214 58.449 -5.204 1.00 46.64 O ANISOU 3001 O ARG A 551 5483 7006 5230 1082 -2 -153 O ATOM 3002 CB ARG A 551 -9.409 60.123 -7.516 1.00 36.87 C ANISOU 3002 CB ARG A 551 4363 5275 4373 1179 -145 -164 C ATOM 3003 CG ARG A 551 -10.443 61.173 -7.893 1.00 39.26 C ANISOU 3003 CG ARG A 551 4665 5387 4864 1256 -146 -228 C ATOM 3004 CD ARG A 551 -11.207 60.782 -9.157 1.00 40.79 C ANISOU 3004 CD ARG A 551 4853 5428 5218 1297 -248 -85 C ATOM 3005 NE ARG A 551 -11.742 59.427 -9.067 1.00 45.60 N ANISOU 3005 NE ARG A 551 5369 6149 5808 1320 -247 52 N ATOM 3006 CZ ARG A 551 -12.215 58.734 -10.098 1.00 49.24 C ANISOU 3006 CZ ARG A 551 5822 6528 6357 1331 -332 202 C ATOM 3007 NH1 ARG A 551 -12.237 59.275 -11.315 1.00 35.28 N ANISOU 3007 NH1 ARG A 551 4134 4563 4708 1317 -431 239 N ATOM 3008 NH2 ARG A 551 -12.674 57.497 -9.906 1.00 48.50 N ANISOU 3008 NH2 ARG A 551 5644 6552 6234 1350 -317 317 N ATOM 3009 N PHE A 552 -6.426 59.190 -6.358 1.00 39.43 N ANISOU 3009 N PHE A 552 4757 5960 4263 971 -113 -172 N ATOM 3010 CA PHE A 552 -5.615 57.984 -6.153 1.00 34.56 C ANISOU 3010 CA PHE A 552 4113 5507 3512 910 -124 -60 C ATOM 3011 C PHE A 552 -4.403 58.236 -5.270 1.00 35.84 C ANISOU 3011 C PHE A 552 4307 5817 3495 824 -79 -141 C ATOM 3012 O PHE A 552 -3.821 59.320 -5.306 1.00 35.19 O ANISOU 3012 O PHE A 552 4313 5665 3391 788 -80 -258 O ATOM 3013 CB PHE A 552 -5.164 57.424 -7.506 1.00 32.69 C ANISOU 3013 CB PHE A 552 3939 5156 3326 879 -231 74 C ATOM 3014 CG PHE A 552 -6.310 57.139 -8.437 1.00 35.46 C ANISOU 3014 CG PHE A 552 4264 5364 3845 949 -283 166 C ATOM 3015 CD1 PHE A 552 -6.951 55.909 -8.410 1.00 38.67 C ANISOU 3015 CD1 PHE A 552 4577 5851 4266 982 -275 297 C ATOM 3016 CD2 PHE A 552 -6.773 58.114 -9.310 1.00 31.96 C ANISOU 3016 CD2 PHE A 552 3887 4709 3545 980 -338 122 C ATOM 3017 CE1 PHE A 552 -8.026 55.649 -9.250 1.00 45.54 C ANISOU 3017 CE1 PHE A 552 5422 6595 5285 1041 -322 384 C ATOM 3018 CE2 PHE A 552 -7.845 57.865 -10.153 1.00 38.86 C ANISOU 3018 CE2 PHE A 552 4734 5455 4575 1038 -389 213 C ATOM 3019 CZ PHE A 552 -8.476 56.627 -10.122 1.00 41.28 C ANISOU 3019 CZ PHE A 552 4948 5846 4889 1067 -381 345 C ATOM 3020 N SER A 553 -4.040 57.229 -4.474 1.00 34.00 N ANISOU 3020 N SER A 553 3998 5787 3133 788 -40 -74 N ATOM 3021 CA SER A 553 -2.806 57.250 -3.694 1.00 37.21 C ANISOU 3021 CA SER A 553 4426 6351 3363 694 -10 -113 C ATOM 3022 C SER A 553 -1.576 57.570 -4.558 1.00 34.00 C ANISOU 3022 C SER A 553 4135 5853 2930 623 -88 -101 C ATOM 3023 O SER A 553 -0.740 58.374 -4.164 1.00 36.00 O ANISOU 3023 O SER A 553 4454 6134 3091 562 -70 -207 O ATOM 3024 CB SER A 553 -2.595 55.915 -2.966 1.00 36.60 C ANISOU 3024 CB SER A 553 4245 6486 3173 667 19 2 C ATOM 3025 OG SER A 553 -3.589 55.686 -1.974 1.00 38.51 O ANISOU 3025 OG SER A 553 4384 6840 3408 716 101 -30 O ATOM 3026 N SER A 554 -1.462 56.935 -5.723 1.00 29.35 N ANISOU 3026 N SER A 554 3574 5158 2419 626 -171 26 N ATOM 3027 CA SER A 554 -0.318 57.184 -6.599 1.00 33.58 C ANISOU 3027 CA SER A 554 4221 5599 2938 555 -244 42 C ATOM 3028 C SER A 554 -0.296 58.619 -7.092 1.00 34.29 C ANISOU 3028 C SER A 554 4421 5513 3093 561 -271 -95 C ATOM 3029 O SER A 554 0.757 59.248 -7.138 1.00 35.35 O ANISOU 3029 O SER A 554 4644 5637 3151 492 -287 -163 O ATOM 3030 CB SER A 554 -0.334 56.239 -7.795 1.00 31.35 C ANISOU 3030 CB SER A 554 3949 5221 2741 555 -320 201 C ATOM 3031 OG SER A 554 -1.540 56.362 -8.525 1.00 33.01 O ANISOU 3031 OG SER A 554 4152 5279 3110 633 -350 223 O ATOM 3032 N GLY A 555 -1.469 59.118 -7.477 1.00 33.09 N ANISOU 3032 N GLY A 555 4262 5224 3087 642 -276 -128 N ATOM 3033 CA GLY A 555 -1.625 60.495 -7.904 1.00 29.92 C ANISOU 3033 CA GLY A 555 3951 4650 2767 659 -294 -256 C ATOM 3034 C GLY A 555 -1.171 61.477 -6.838 1.00 40.44 C ANISOU 3034 C GLY A 555 5307 6067 3991 628 -215 -421 C ATOM 3035 O GLY A 555 -0.397 62.396 -7.130 1.00 37.03 O ANISOU 3035 O GLY A 555 4981 5557 3531 580 -240 -511 O ATOM 3036 N LYS A 556 -1.650 61.282 -5.608 1.00 32.72 N ANISOU 3036 N LYS A 556 4234 5251 2949 648 -118 -462 N ATOM 3037 CA LYS A 556 -1.271 62.136 -4.477 1.00 41.27 C ANISOU 3037 CA LYS A 556 5331 6435 3915 607 -29 -618 C ATOM 3038 C LYS A 556 0.221 62.050 -4.193 1.00 41.99 C ANISOU 3038 C LYS A 556 5478 6644 3833 498 -41 -621 C ATOM 3039 O LYS A 556 0.830 63.036 -3.790 1.00 38.66 O ANISOU 3039 O LYS A 556 5127 6229 3334 447 -7 -752 O ATOM 3040 CB LYS A 556 -2.030 61.746 -3.201 1.00 39.59 C ANISOU 3040 CB LYS A 556 4998 6390 3653 635 77 -643 C ATOM 3041 CG LYS A 556 -3.472 62.212 -3.128 1.00 52.47 C ANISOU 3041 CG LYS A 556 6579 7920 5438 735 125 -701 C ATOM 3042 CD LYS A 556 -4.186 61.487 -1.992 1.00 59.04 C ANISOU 3042 CD LYS A 556 7284 8929 6219 759 215 -686 C ATOM 3043 CE LYS A 556 -5.625 61.930 -1.845 1.00 72.26 C ANISOU 3043 CE LYS A 556 8900 10509 8045 857 272 -747 C ATOM 3044 NZ LYS A 556 -6.370 61.015 -0.932 1.00 81.99 N ANISOU 3044 NZ LYS A 556 10006 11903 9242 885 341 -703 N ATOM 3045 N LYS A 557 0.801 60.864 -4.378 1.00 31.20 N ANISOU 3045 N LYS A 557 4076 5373 2407 460 -85 -474 N ATOM 3046 CA LYS A 557 2.236 60.697 -4.194 1.00 40.13 C ANISOU 3046 CA LYS A 557 5253 6606 3387 358 -105 -457 C ATOM 3047 C LYS A 557 3.026 61.547 -5.192 1.00 34.89 C ANISOU 3047 C LYS A 557 4728 5774 2754 321 -177 -508 C ATOM 3048 O LYS A 557 3.977 62.219 -4.818 1.00 36.86 O ANISOU 3048 O LYS A 557 5045 6070 2891 248 -163 -597 O ATOM 3049 CB LYS A 557 2.632 59.218 -4.277 1.00 44.74 C ANISOU 3049 CB LYS A 557 5764 7306 3927 333 -136 -278 C ATOM 3050 CG LYS A 557 2.274 58.433 -3.010 1.00 58.00 C ANISOU 3050 CG LYS A 557 7315 9208 5513 333 -57 -243 C ATOM 3051 CD LYS A 557 2.169 56.924 -3.252 1.00 59.59 C ANISOU 3051 CD LYS A 557 7428 9482 5732 347 -84 -57 C ATOM 3052 CE LYS A 557 3.535 56.275 -3.392 1.00 63.06 C ANISOU 3052 CE LYS A 557 7884 10003 6074 258 -124 41 C ATOM 3053 NZ LYS A 557 3.448 54.790 -3.414 1.00 67.98 N ANISOU 3053 NZ LYS A 557 8407 10723 6701 267 -131 216 N ATOM 3054 N MET A 558 2.615 61.529 -6.456 1.00 30.13 N ANISOU 3054 N MET A 558 4170 4977 2302 366 -256 -451 N ATOM 3055 CA MET A 558 3.303 62.300 -7.492 1.00 34.73 C ANISOU 3055 CA MET A 558 4887 5387 2923 330 -332 -493 C ATOM 3056 C MET A 558 3.163 63.808 -7.289 1.00 38.67 C ANISOU 3056 C MET A 558 5461 5794 3438 341 -299 -674 C ATOM 3057 O MET A 558 4.114 64.561 -7.480 1.00 36.58 O ANISOU 3057 O MET A 558 5300 5489 3110 279 -321 -753 O ATOM 3058 CB MET A 558 2.781 61.913 -8.869 1.00 28.93 C ANISOU 3058 CB MET A 558 4177 4466 2348 371 -421 -388 C ATOM 3059 CG MET A 558 3.174 60.496 -9.283 1.00 27.28 C ANISOU 3059 CG MET A 558 3925 4319 2122 339 -460 -213 C ATOM 3060 SD MET A 558 2.967 60.252 -11.050 1.00 35.13 S ANISOU 3060 SD MET A 558 4995 5077 3275 343 -573 -110 S ATOM 3061 CE MET A 558 1.197 60.486 -11.192 1.00 27.74 C ANISOU 3061 CE MET A 558 3995 4040 2504 458 -563 -115 C ATOM 3062 N ILE A 559 1.961 64.237 -6.923 1.00 32.46 N ANISOU 3062 N ILE A 559 4621 4970 2742 421 -244 -736 N ATOM 3063 CA ILE A 559 1.694 65.642 -6.647 1.00 39.12 C ANISOU 3063 CA ILE A 559 5522 5727 3616 440 -195 -908 C ATOM 3064 C ILE A 559 2.616 66.120 -5.531 1.00 49.94 C ANISOU 3064 C ILE A 559 6916 7259 4800 357 -119 -1020 C ATOM 3065 O ILE A 559 3.249 67.176 -5.633 1.00 50.07 O ANISOU 3065 O ILE A 559 7036 7209 4778 315 -118 -1138 O ATOM 3066 CB ILE A 559 0.229 65.833 -6.243 1.00 37.99 C ANISOU 3066 CB ILE A 559 5290 5550 3593 537 -129 -943 C ATOM 3067 CG1 ILE A 559 -0.659 65.685 -7.480 1.00 31.84 C ANISOU 3067 CG1 ILE A 559 4513 4573 3014 613 -214 -853 C ATOM 3068 CG2 ILE A 559 0.021 67.185 -5.529 1.00 37.84 C ANISOU 3068 CG2 ILE A 559 5306 5504 3568 543 -36 -1133 C ATOM 3069 CD1 ILE A 559 -2.138 65.587 -7.172 1.00 39.57 C ANISOU 3069 CD1 ILE A 559 5386 5528 4122 713 -162 -846 C ATOM 3070 N GLU A 560 2.704 65.308 -4.482 1.00 49.47 N ANISOU 3070 N GLU A 560 6762 7415 4620 329 -57 -977 N ATOM 3071 CA GLU A 560 3.520 65.612 -3.315 1.00 48.75 C ANISOU 3071 CA GLU A 560 6677 7506 4341 241 19 -1066 C ATOM 3072 C GLU A 560 5.007 65.601 -3.660 1.00 49.57 C ANISOU 3072 C GLU A 560 6867 7638 4328 144 -44 -1041 C ATOM 3073 O GLU A 560 5.765 66.435 -3.176 1.00 46.15 O ANISOU 3073 O GLU A 560 6504 7250 3781 73 -8 -1157 O ATOM 3074 CB GLU A 560 3.213 64.609 -2.198 1.00 48.49 C ANISOU 3074 CB GLU A 560 6514 7694 4218 232 86 -1000 C ATOM 3075 CG GLU A 560 4.175 64.630 -1.027 1.00 66.13 C ANISOU 3075 CG GLU A 560 8741 10144 6241 122 146 -1047 C ATOM 3076 CD GLU A 560 3.855 63.555 0.006 1.00 90.96 C ANISOU 3076 CD GLU A 560 11754 13503 9304 111 201 -966 C ATOM 3077 OE1 GLU A 560 2.757 62.956 -0.073 1.00 97.67 O ANISOU 3077 OE1 GLU A 560 12519 14330 10262 196 211 -904 O ATOM 3078 OE2 GLU A 560 4.699 63.312 0.897 1.00 98.96 O ANISOU 3078 OE2 GLU A 560 12748 14710 10143 13 233 -961 O ATOM 3079 N THR A 561 5.415 64.650 -4.498 1.00 51.04 N ANISOU 3079 N THR A 561 7050 7798 4546 138 -133 -890 N ATOM 3080 CA THR A 561 6.798 64.574 -4.957 1.00 50.92 C ANISOU 3080 CA THR A 561 7115 7789 4443 51 -197 -855 C ATOM 3081 C THR A 561 7.203 65.890 -5.610 1.00 50.83 C ANISOU 3081 C THR A 561 7244 7606 4461 35 -230 -984 C ATOM 3082 O THR A 561 8.254 66.449 -5.306 1.00 52.62 O ANISOU 3082 O THR A 561 7543 7889 4563 -47 -222 -1058 O ATOM 3083 CB THR A 561 7.007 63.408 -5.953 1.00 47.88 C ANISOU 3083 CB THR A 561 6711 7354 4127 57 -285 -677 C ATOM 3084 OG1 THR A 561 6.951 62.158 -5.251 1.00 48.96 O ANISOU 3084 OG1 THR A 561 6724 7678 4201 50 -253 -554 O ATOM 3085 CG2 THR A 561 8.360 63.521 -6.644 1.00 42.50 C ANISOU 3085 CG2 THR A 561 6133 6624 3392 -25 -356 -658 C ATOM 3086 N LEU A 562 6.348 66.384 -6.497 1.00 47.07 N ANISOU 3086 N LEU A 562 6805 6925 4154 112 -267 -1009 N ATOM 3087 CA LEU A 562 6.602 67.631 -7.209 1.00 46.95 C ANISOU 3087 CA LEU A 562 6920 6727 4191 106 -304 -1125 C ATOM 3088 C LEU A 562 6.545 68.843 -6.288 1.00 53.41 C ANISOU 3088 C LEU A 562 7770 7582 4942 94 -208 -1307 C ATOM 3089 O LEU A 562 7.287 69.809 -6.480 1.00 50.05 O ANISOU 3089 O LEU A 562 7457 7094 4467 45 -219 -1414 O ATOM 3090 CB LEU A 562 5.589 67.798 -8.336 1.00 35.93 C ANISOU 3090 CB LEU A 562 5540 5110 3001 193 -367 -1092 C ATOM 3091 CG LEU A 562 5.879 66.996 -9.600 1.00 33.07 C ANISOU 3091 CG LEU A 562 5209 4645 2712 180 -479 -946 C ATOM 3092 CD1 LEU A 562 4.634 66.924 -10.458 1.00 31.54 C ANISOU 3092 CD1 LEU A 562 4991 4280 2714 268 -525 -890 C ATOM 3093 CD2 LEU A 562 7.026 67.629 -10.368 1.00 34.47 C ANISOU 3093 CD2 LEU A 562 5527 4719 2851 107 -549 -994 C ATOM 3094 N ALA A 563 5.661 68.788 -5.295 1.00 51.93 N ANISOU 3094 N ALA A 563 7485 7492 4752 135 -111 -1345 N ATOM 3095 CA ALA A 563 5.518 69.884 -4.344 1.00 54.15 C ANISOU 3095 CA ALA A 563 7788 7814 4974 119 -3 -1519 C ATOM 3096 C ALA A 563 6.757 70.008 -3.461 1.00 55.64 C ANISOU 3096 C ALA A 563 8010 8189 4942 0 39 -1571 C ATOM 3097 O ALA A 563 7.198 71.113 -3.154 1.00 52.67 O ANISOU 3097 O ALA A 563 7719 7794 4498 -46 86 -1717 O ATOM 3098 CB ALA A 563 4.268 69.698 -3.493 1.00 54.64 C ANISOU 3098 CB ALA A 563 7733 7940 5088 185 95 -1539 C ATOM 3099 N ASN A 564 7.314 68.868 -3.060 1.00 58.50 N ANISOU 3099 N ASN A 564 8304 8729 5195 -51 23 -1447 N ATOM 3100 CA ASN A 564 8.503 68.847 -2.212 1.00 69.92 C ANISOU 3100 CA ASN A 564 9767 10367 6432 -169 54 -1470 C ATOM 3101 C ASN A 564 9.752 69.312 -2.954 1.00 73.52 C ANISOU 3101 C ASN A 564 10349 10749 6835 -235 -24 -1487 C ATOM 3102 O ASN A 564 10.760 69.661 -2.340 1.00 74.46 O ANISOU 3102 O ASN A 564 10513 10990 6790 -335 3 -1543 O ATOM 3103 CB ASN A 564 8.738 67.448 -1.634 1.00 72.84 C ANISOU 3103 CB ASN A 564 10020 10939 6715 -201 50 -1315 C ATOM 3104 CG ASN A 564 7.745 67.091 -0.536 1.00 81.22 C ANISOU 3104 CG ASN A 564 10963 12134 7762 -172 148 -1326 C ATOM 3105 OD1 ASN A 564 6.922 67.919 -0.126 1.00 82.60 O ANISOU 3105 OD1 ASN A 564 11142 12258 7983 -134 229 -1457 O ATOM 3106 ND2 ASN A 564 7.819 65.850 -0.052 1.00 76.38 N ANISOU 3106 ND2 ASN A 564 10242 11689 7089 -191 145 -1189 N ATOM 3107 N LEU A 565 9.680 69.309 -4.279 1.00 68.03 N ANISOU 3107 N LEU A 565 9712 9855 6281 -185 -120 -1437 N ATOM 3108 CA LEU A 565 10.815 69.715 -5.093 1.00 65.95 C ANISOU 3108 CA LEU A 565 9571 9503 5984 -244 -200 -1450 C ATOM 3109 C LEU A 565 10.920 71.236 -5.205 1.00 73.00 C ANISOU 3109 C LEU A 565 10585 10274 6877 -253 -174 -1633 C ATOM 3110 O LEU A 565 12.014 71.790 -5.115 1.00 65.49 O ANISOU 3110 O LEU A 565 9723 9356 5803 -338 -180 -1700 O ATOM 3111 CB LEU A 565 10.733 69.085 -6.480 1.00 57.17 C ANISOU 3111 CB LEU A 565 8479 8227 5015 -201 -313 -1324 C ATOM 3112 CG LEU A 565 11.887 69.482 -7.397 1.00 53.13 C ANISOU 3112 CG LEU A 565 8099 7611 4479 -265 -397 -1337 C ATOM 3113 CD1 LEU A 565 13.184 68.875 -6.903 1.00 56.08 C ANISOU 3113 CD1 LEU A 565 8460 8163 4684 -366 -401 -1274 C ATOM 3114 CD2 LEU A 565 11.602 69.054 -8.815 1.00 41.34 C ANISOU 3114 CD2 LEU A 565 6637 5924 3148 -221 -499 -1238 C ATOM 3115 N ARG A 566 9.780 71.899 -5.397 1.00 94.39 N ANISOU 3115 N ARG A 566 13293 12843 9728 -166 -142 -1710 N ATOM 3116 CA ARG A 566 9.737 73.354 -5.554 1.00109.71 C ANISOU 3116 CA ARG A 566 15342 14647 11698 -161 -112 -1881 C ATOM 3117 C ARG A 566 10.631 74.044 -4.532 1.00112.86 C ANISOU 3117 C ARG A 566 15790 15194 11898 -263 -30 -2007 C ATOM 3118 O ARG A 566 11.398 74.949 -4.867 1.00117.90 O ANISOU 3118 O ARG A 566 16550 15759 12487 -311 -50 -2103 O ATOM 3119 CB ARG A 566 8.301 73.870 -5.428 1.00118.71 C ANISOU 3119 CB ARG A 566 16433 15680 12993 -60 -47 -1947 C ATOM 3120 CG ARG A 566 7.298 73.091 -6.260 1.00125.24 C ANISOU 3120 CG ARG A 566 17188 16392 14006 37 -116 -1813 C ATOM 3121 CD ARG A 566 5.883 73.613 -6.077 1.00130.17 C ANISOU 3121 CD ARG A 566 17756 16917 14786 136 -49 -1877 C ATOM 3122 NE ARG A 566 4.891 72.593 -6.405 1.00132.34 N ANISOU 3122 NE ARG A 566 17922 17172 15189 216 -83 -1735 N ATOM 3123 CZ ARG A 566 4.569 72.230 -7.642 1.00131.53 C ANISOU 3123 CZ ARG A 566 17834 16910 15231 264 -194 -1627 C ATOM 3124 NH1 ARG A 566 5.164 72.802 -8.679 1.00131.27 N ANISOU 3124 NH1 ARG A 566 17921 16721 15236 238 -284 -1645 N ATOM 3125 NH2 ARG A 566 3.653 71.291 -7.841 1.00130.49 N ANISOU 3125 NH2 ARG A 566 17599 16777 15203 331 -215 -1501 N ATOM 3126 N SER A 567 10.528 73.600 -3.284 1.00 97.89 N ANISOU 3126 N SER A 567 13802 13509 9885 -300 61 -2003 N ATOM 3127 CA SER A 567 11.414 74.059 -2.225 1.00 90.99 C ANISOU 3127 CA SER A 567 12961 12810 8802 -414 137 -2097 C ATOM 3128 C SER A 567 12.791 73.395 -2.326 1.00 87.86 C ANISOU 3128 C SER A 567 12587 12533 8264 -509 62 -1996 C ATOM 3129 O SER A 567 13.189 72.626 -1.449 1.00 83.40 O ANISOU 3129 O SER A 567 11943 12182 7566 -575 91 -1923 O ATOM 3130 CB SER A 567 10.782 73.787 -0.860 1.00 88.41 C ANISOU 3130 CB SER A 567 12524 12665 8401 -429 259 -2122 C ATOM 3131 OG SER A 567 9.902 72.679 -0.922 1.00 80.72 O ANISOU 3131 OG SER A 567 11427 11714 7530 -351 240 -1988 O TER 3132 SER A 567 ATOM 3133 O5' U B 1 -2.761 50.787 -0.964 1.00 59.95 O ANISOU 3133 O5' U B 1 8900 7973 5906 1623 -41 1522 O ATOM 3134 C5' U B 1 -3.819 50.008 -1.444 1.00 48.73 C ANISOU 3134 C5' U B 1 7358 6453 4705 1640 200 1425 C ATOM 3135 C4' U B 1 -3.612 49.670 -2.917 1.00 39.86 C ANISOU 3135 C4' U B 1 6027 5376 3743 1473 214 1307 C ATOM 3136 O4' U B 1 -3.586 50.923 -3.680 1.00 40.44 O ANISOU 3136 O4' U B 1 6157 5521 3686 1315 -39 1199 O ATOM 3137 C3' U B 1 -2.285 48.997 -3.273 1.00 42.78 C ANISOU 3137 C3' U B 1 6250 5842 4162 1414 198 1378 C ATOM 3138 O3' U B 1 -2.387 47.628 -2.993 1.00 41.28 O ANISOU 3138 O3' U B 1 5936 5588 4162 1521 458 1432 O ATOM 3139 C2' U B 1 -2.274 49.256 -4.783 1.00 39.56 C ANISOU 3139 C2' U B 1 5699 5491 3840 1226 118 1230 C ATOM 3140 O2' U B 1 -3.152 48.376 -5.482 1.00 34.23 O ANISOU 3140 O2' U B 1 4860 4727 3418 1234 348 1132 O ATOM 3141 C1' U B 1 -2.814 50.696 -4.865 1.00 40.03 C ANISOU 3141 C1' U B 1 5930 5560 3722 1158 -95 1146 C ATOM 3142 N1 U B 1 -1.686 51.669 -4.917 1.00 39.99 N ANISOU 3142 N1 U B 1 6004 5691 3501 1056 -390 1193 N ATOM 3143 C2 U B 1 -1.198 51.942 -6.166 1.00 33.63 C ANISOU 3143 C2 U B 1 5076 4975 2726 874 -514 1101 C ATOM 3144 O2 U B 1 -1.645 51.443 -7.204 1.00 37.26 O ANISOU 3144 O2 U B 1 5372 5405 3378 799 -396 982 O ATOM 3145 N3 U B 1 -0.159 52.845 -6.175 1.00 34.27 N ANISOU 3145 N3 U B 1 5233 5182 2605 786 -789 1151 N ATOM 3146 C4 U B 1 0.431 53.446 -5.082 1.00 40.06 C ANISOU 3146 C4 U B 1 6144 5952 3125 868 -942 1285 C ATOM 3147 O4 U B 1 1.368 54.204 -5.267 1.00 45.49 O ANISOU 3147 O4 U B 1 6874 6753 3658 776 -1185 1318 O ATOM 3148 C5 U B 1 -0.133 53.105 -3.801 1.00 34.77 C ANISOU 3148 C5 U B 1 5594 5178 2438 1066 -797 1376 C ATOM 3149 C6 U B 1 -1.143 52.230 -3.765 1.00 38.90 C ANISOU 3149 C6 U B 1 6046 5584 3150 1148 -529 1329 C ATOM 3150 P G B 2 -1.088 46.750 -2.582 1.00 43.28 P ANISOU 3150 P G B 2 6113 5904 4429 1556 489 1567 P ATOM 3151 OP1 G B 2 -1.596 45.540 -1.898 1.00 44.67 O ANISOU 3151 OP1 G B 2 6235 5977 4760 1713 761 1626 O ATOM 3152 OP2 G B 2 -0.137 47.657 -1.901 1.00 45.06 O ANISOU 3152 OP2 G B 2 6511 6205 4406 1553 254 1662 O ATOM 3153 O5' G B 2 -0.440 46.364 -3.986 1.00 42.70 O ANISOU 3153 O5' G B 2 5814 5925 4485 1388 453 1486 O ATOM 3154 C5' G B 2 -1.171 45.594 -4.926 1.00 36.16 C ANISOU 3154 C5' G B 2 4793 5047 3900 1359 631 1381 C ATOM 3155 C4' G B 2 -0.242 44.989 -5.971 1.00 35.19 C ANISOU 3155 C4' G B 2 4452 5028 3890 1236 605 1356 C ATOM 3156 O4' G B 2 0.348 46.033 -6.790 1.00 40.59 O ANISOU 3156 O4' G B 2 5152 5822 4447 1065 355 1292 O ATOM 3157 C3' G B 2 0.924 44.200 -5.404 1.00 38.83 C ANISOU 3157 C3' G B 2 4866 5550 4336 1279 623 1483 C ATOM 3158 O3' G B 2 0.511 42.864 -5.097 1.00 43.93 O ANISOU 3158 O3' G B 2 5392 6120 5181 1399 877 1517 O ATOM 3159 C2' G B 2 1.905 44.266 -6.555 1.00 34.82 C ANISOU 3159 C2' G B 2 4208 5178 3845 1107 477 1434 C ATOM 3160 O2' G B 2 1.618 43.379 -7.620 1.00 35.08 O ANISOU 3160 O2' G B 2 4000 5212 4117 1061 610 1350 O ATOM 3161 C1' G B 2 1.702 45.677 -7.086 1.00 34.84 C ANISOU 3161 C1' G B 2 4319 5217 3700 988 264 1349 C ATOM 3162 N9 G B 2 2.709 46.592 -6.529 1.00 36.15 N ANISOU 3162 N9 G B 2 4650 5471 3617 952 28 1432 N ATOM 3163 C8 G B 2 2.842 46.998 -5.202 1.00 33.84 C ANISOU 3163 C8 G B 2 4569 5140 3150 1073 -17 1546 C ATOM 3164 N7 G B 2 3.858 47.824 -5.006 1.00 41.91 N ANISOU 3164 N7 G B 2 5697 6255 3971 1013 -253 1604 N ATOM 3165 C5 G B 2 4.426 47.942 -6.307 1.00 36.48 C ANISOU 3165 C5 G B 2 4852 5678 3329 833 -364 1521 C ATOM 3166 C6 G B 2 5.558 48.702 -6.799 1.00 35.50 C ANISOU 3166 C6 G B 2 4739 5689 3060 692 -619 1529 C ATOM 3167 O6 G B 2 6.304 49.450 -6.121 1.00 35.89 O ANISOU 3167 O6 G B 2 4950 5782 2904 707 -805 1619 O ATOM 3168 N1 G B 2 5.777 48.560 -8.204 1.00 32.00 N ANISOU 3168 N1 G B 2 4098 5330 2729 529 -654 1423 N ATOM 3169 C2 G B 2 4.979 47.757 -9.009 1.00 32.23 C ANISOU 3169 C2 G B 2 3943 5310 2992 516 -461 1323 C ATOM 3170 N2 G B 2 5.314 47.730 -10.309 1.00 30.96 N ANISOU 3170 N2 G B 2 3609 5239 2916 362 -526 1232 N ATOM 3171 N3 G B 2 3.926 47.036 -8.612 1.00 37.45 N ANISOU 3171 N3 G B 2 4586 5843 3800 647 -225 1312 N ATOM 3172 C4 G B 2 3.727 47.182 -7.253 1.00 36.98 C ANISOU 3172 C4 G B 2 4718 5709 3624 796 -192 1415 C ATOM 3173 P U B 3 1.181 41.958 -3.978 1.00 47.06 P ANISOU 3173 P U B 3 5808 6505 5565 1523 973 1657 P ATOM 3174 OP1 U B 3 0.391 40.719 -3.863 1.00 58.31 O ANISOU 3174 OP1 U B 3 7102 7837 7216 1635 1238 1657 O ATOM 3175 OP2 U B 3 1.469 42.758 -2.768 1.00 46.17 O ANISOU 3175 OP2 U B 3 5947 6376 5220 1598 861 1754 O ATOM 3176 O5' U B 3 2.564 41.609 -4.707 1.00 47.69 O ANISOU 3176 O5' U B 3 5737 6729 5655 1391 855 1663 O ATOM 3177 C5' U B 3 3.558 40.865 -4.020 1.00 42.06 C ANISOU 3177 C5' U B 3 5013 6048 4919 1440 876 1766 C ATOM 3178 C4' U B 3 4.035 39.804 -4.986 1.00 43.69 C ANISOU 3178 C4' U B 3 4953 6330 5315 1363 936 1723 C ATOM 3179 O4' U B 3 4.558 40.461 -6.149 1.00 41.21 O ANISOU 3179 O4' U B 3 4562 6130 4965 1190 753 1644 O ATOM 3180 C3' U B 3 5.190 38.963 -4.526 1.00 45.14 C ANISOU 3180 C3' U B 3 5088 6572 5493 1378 937 1805 C ATOM 3181 O3' U B 3 4.648 37.911 -3.768 1.00 46.95 O ANISOU 3181 O3' U B 3 5290 6704 5846 1527 1156 1855 O ATOM 3182 C2' U B 3 5.721 38.477 -5.872 1.00 46.60 C ANISOU 3182 C2' U B 3 5023 6873 5810 1238 892 1728 C ATOM 3183 O2' U B 3 4.930 37.442 -6.427 1.00 41.57 O ANISOU 3183 O2' U B 3 4179 6195 5422 1281 1085 1677 O ATOM 3184 C1' U B 3 5.569 39.708 -6.751 1.00 45.12 C ANISOU 3184 C1' U B 3 4873 6735 5536 1108 722 1644 C ATOM 3185 N1 U B 3 6.798 40.560 -6.889 1.00 47.51 N ANISOU 3185 N1 U B 3 5256 7156 5639 985 473 1666 N ATOM 3186 C2 U B 3 7.666 40.195 -7.896 1.00 45.48 C ANISOU 3186 C2 U B 3 4809 7028 5445 853 391 1624 C ATOM 3187 O2 U B 3 7.425 39.243 -8.624 1.00 43.31 O ANISOU 3187 O2 U B 3 4311 6768 5376 842 511 1573 O ATOM 3188 N3 U B 3 8.783 40.986 -8.021 1.00 42.21 N ANISOU 3188 N3 U B 3 4469 6720 4847 741 163 1644 N ATOM 3189 C4 U B 3 9.092 42.069 -7.228 1.00 43.17 C ANISOU 3189 C4 U B 3 4835 6827 4740 758 13 1706 C ATOM 3190 O4 U B 3 10.123 42.694 -7.444 1.00 36.16 O ANISOU 3190 O4 U B 3 3990 6041 3710 654 -191 1722 O ATOM 3191 C5 U B 3 8.137 42.382 -6.189 1.00 43.37 C ANISOU 3191 C5 U B 3 5047 6718 4715 905 107 1749 C ATOM 3192 C6 U B 3 7.039 41.640 -6.057 1.00 39.46 C ANISOU 3192 C6 U B 3 4484 6120 4390 1009 330 1726 C ATOM 3193 P A B 4 5.461 37.420 -2.477 1.00 55.66 P ANISOU 3193 P A B 4 6509 7787 6854 1624 1176 1973 P ATOM 3194 OP1 A B 4 4.505 36.651 -1.656 1.00 53.43 O ANISOU 3194 OP1 A B 4 6243 7377 6682 1789 1404 2015 O ATOM 3195 OP2 A B 4 6.198 38.584 -1.916 1.00 54.59 O ANISOU 3195 OP2 A B 4 6598 7678 6467 1597 971 2025 O ATOM 3196 O5' A B 4 6.606 36.450 -3.049 1.00 48.57 O ANISOU 3196 O5' A B 4 5408 7002 6043 1534 1146 1965 O ATOM 3197 C5' A B 4 6.333 35.186 -3.623 1.00 51.61 C ANISOU 3197 C5' A B 4 5548 7400 6661 1543 1297 1928 C ATOM 3198 C4' A B 4 7.601 34.535 -4.160 1.00 46.63 C ANISOU 3198 C4' A B 4 4758 6901 6059 1436 1205 1918 C ATOM 3199 O4' A B 4 8.404 35.505 -4.883 1.00 52.65 O ANISOU 3199 O4' A B 4 5544 7775 6687 1282 982 1880 O ATOM 3200 C3' A B 4 8.580 33.999 -3.130 1.00 46.83 C ANISOU 3200 C3' A B 4 4870 6926 5999 1485 1195 1999 C ATOM 3201 O3' A B 4 8.172 32.731 -2.652 1.00 42.15 O ANISOU 3201 O3' A B 4 4180 6272 5565 1596 1391 2027 O ATOM 3202 C2' A B 4 9.824 33.843 -3.989 1.00 47.63 C ANISOU 3202 C2' A B 4 4830 7180 6086 1329 1036 1959 C ATOM 3203 O2' A B 4 9.731 32.739 -4.851 1.00 44.11 O ANISOU 3203 O2' A B 4 4109 6797 5853 1295 1118 1905 O ATOM 3204 C1' A B 4 9.771 35.123 -4.807 1.00 52.41 C ANISOU 3204 C1' A B 4 5479 7841 6593 1214 874 1907 C ATOM 3205 N9 A B 4 10.566 36.171 -4.178 1.00 52.53 N ANISOU 3205 N9 A B 4 5727 7866 6367 1189 697 1960 N ATOM 3206 C8 A B 4 10.139 37.058 -3.234 1.00 48.65 C ANISOU 3206 C8 A B 4 5484 7276 5726 1281 681 2017 C ATOM 3207 N7 A B 4 11.073 37.880 -2.834 1.00 46.66 N ANISOU 3207 N7 A B 4 5399 7057 5273 1243 498 2061 N ATOM 3208 C5 A B 4 12.185 37.511 -3.563 1.00 47.78 C ANISOU 3208 C5 A B 4 5396 7326 5432 1112 392 2028 C ATOM 3209 C6 A B 4 13.502 38.005 -3.595 1.00 47.55 C ANISOU 3209 C6 A B 4 5436 7383 5249 1017 189 2048 C ATOM 3210 N6 A B 4 13.897 39.039 -2.843 1.00 44.91 N ANISOU 3210 N6 A B 4 5342 7011 4709 1050 53 2113 N ATOM 3211 N1 A B 4 14.381 37.402 -4.433 1.00 49.01 N ANISOU 3211 N1 A B 4 5429 7693 5501 893 129 2000 N ATOM 3212 C2 A B 4 13.972 36.372 -5.189 1.00 41.20 C ANISOU 3212 C2 A B 4 4192 6742 4720 870 256 1939 C ATOM 3213 N3 A B 4 12.759 35.827 -5.235 1.00 51.14 N ANISOU 3213 N3 A B 4 5364 7924 6142 958 448 1919 N ATOM 3214 C4 A B 4 11.901 36.446 -4.392 1.00 52.62 C ANISOU 3214 C4 A B 4 5750 7985 6257 1076 510 1965 C ATOM 3215 P A B 5 8.517 32.274 -1.156 1.00 48.09 P ANISOU 3215 P A B 5 5099 6937 6236 1724 1462 2122 P ATOM 3216 OP1 A B 5 7.834 30.963 -0.974 1.00 44.90 O ANISOU 3216 OP1 A B 5 4544 6479 6038 1824 1673 2129 O ATOM 3217 OP2 A B 5 8.230 33.407 -0.226 1.00 51.88 O ANISOU 3217 OP2 A B 5 5861 7325 6526 1799 1419 2180 O ATOM 3218 O5' A B 5 10.079 32.073 -1.089 1.00 47.92 O ANISOU 3218 O5' A B 5 5079 7012 6114 1631 1310 2133 O ATOM 3219 C5' A B 5 10.755 31.230 -2.033 1.00 46.23 C ANISOU 3219 C5' A B 5 4620 6925 6021 1520 1270 2074 C ATOM 3220 C4' A B 5 12.263 31.259 -1.809 1.00 46.85 C ANISOU 3220 C4' A B 5 4758 7080 5961 1435 1107 2086 C ATOM 3221 O4' A B 5 12.769 32.536 -2.297 1.00 41.41 O ANISOU 3221 O4' A B 5 4166 6457 5112 1326 909 2070 O ATOM 3222 C3' A B 5 12.719 31.146 -0.351 1.00 46.03 C ANISOU 3222 C3' A B 5 4878 6875 5736 1543 1134 2166 C ATOM 3223 O3' A B 5 12.962 29.777 0.038 1.00 46.29 O ANISOU 3223 O3' A B 5 4801 6898 5888 1588 1245 2169 O ATOM 3224 C2' A B 5 14.024 31.940 -0.375 1.00 46.65 C ANISOU 3224 C2' A B 5 5079 7022 5624 1439 913 2169 C ATOM 3225 O2' A B 5 15.107 31.185 -0.867 1.00 45.37 O ANISOU 3225 O2' A B 5 4765 6972 5503 1330 836 2124 O ATOM 3226 C1' A B 5 13.748 33.027 -1.402 1.00 52.63 C ANISOU 3226 C1' A B 5 5805 7853 6340 1336 793 2127 C ATOM 3227 N9 A B 5 13.298 34.303 -0.857 1.00 60.78 N ANISOU 3227 N9 A B 5 7074 8805 7215 1395 738 2175 N ATOM 3228 C8 A B 5 12.011 34.723 -0.673 1.00 61.39 C ANISOU 3228 C8 A B 5 7212 8793 7321 1485 844 2186 C ATOM 3229 N7 A B 5 11.926 35.935 -0.175 1.00 60.95 N ANISOU 3229 N7 A B 5 7378 8690 7088 1517 741 2228 N ATOM 3230 C5 A B 5 13.244 36.336 -0.020 1.00 63.55 C ANISOU 3230 C5 A B 5 7801 9077 7268 1448 559 2252 C ATOM 3231 C6 A B 5 13.835 37.522 0.466 1.00 71.13 C ANISOU 3231 C6 A B 5 8985 10026 8014 1448 377 2303 C ATOM 3232 N6 A B 5 13.144 38.584 0.902 1.00 71.86 N ANISOU 3232 N6 A B 5 9256 10052 7995 1519 339 2341 N ATOM 3233 N1 A B 5 15.180 37.584 0.481 1.00 74.88 N ANISOU 3233 N1 A B 5 9495 10563 8393 1373 227 2314 N ATOM 3234 C2 A B 5 15.880 36.532 0.043 1.00 74.09 C ANISOU 3234 C2 A B 5 9217 10535 8398 1297 255 2270 C ATOM 3235 N3 A B 5 15.440 35.368 -0.430 1.00 67.22 N ANISOU 3235 N3 A B 5 8126 9691 7725 1288 410 2219 N ATOM 3236 C4 A B 5 14.101 35.336 -0.437 1.00 61.73 C ANISOU 3236 C4 A B 5 7400 8929 7127 1370 559 2216 C ATOM 3237 P A B 6 12.526 29.223 1.484 1.00 43.22 P ANISOU 3237 P A B 6 4563 6356 5501 1763 1412 2243 P ATOM 3238 OP1 A B 6 12.664 27.746 1.467 1.00 54.66 O ANISOU 3238 OP1 A B 6 5821 7832 7114 1775 1515 2220 O ATOM 3239 OP2 A B 6 11.206 29.867 1.776 1.00 47.36 O ANISOU 3239 OP2 A B 6 5189 6778 6029 1872 1520 2278 O ATOM 3240 O5' A B 6 13.624 29.782 2.505 1.00 45.49 O ANISOU 3240 O5' A B 6 5113 6596 5577 1779 1290 2295 O ATOM 3241 C5' A B 6 15.012 29.508 2.258 1.00 51.03 C ANISOU 3241 C5' A B 6 5775 7389 6223 1663 1145 2258 C ATOM 3242 C4' A B 6 15.887 30.423 3.084 1.00 52.34 C ANISOU 3242 C4' A B 6 6215 7498 6173 1680 1009 2309 C ATOM 3243 O4' A B 6 15.948 31.752 2.492 1.00 58.08 O ANISOU 3243 O4' A B 6 7010 8278 6779 1605 853 2307 O ATOM 3244 C3' A B 6 15.346 30.608 4.493 1.00 55.29 C ANISOU 3244 C3' A B 6 6827 7700 6481 1861 1122 2395 C ATOM 3245 O3' A B 6 15.836 29.570 5.349 1.00 54.10 O ANISOU 3245 O3' A B 6 6706 7485 6365 1922 1203 2405 O ATOM 3246 C2' A B 6 15.858 32.010 4.849 1.00 59.71 C ANISOU 3246 C2' A B 6 7628 8231 6828 1863 951 2441 C ATOM 3247 O2' A B 6 17.159 32.003 5.410 1.00 60.73 O ANISOU 3247 O2' A B 6 7890 8342 6843 1845 837 2453 O ATOM 3248 C1' A B 6 15.823 32.743 3.497 1.00 60.40 C ANISOU 3248 C1' A B 6 7582 8456 6910 1715 819 2386 C ATOM 3249 N9 A B 6 14.578 33.503 3.340 1.00 62.96 N ANISOU 3249 N9 A B 6 7940 8746 7238 1769 870 2404 N ATOM 3250 C8 A B 6 13.347 33.008 3.001 1.00 64.15 C ANISOU 3250 C8 A B 6 7947 8878 7549 1812 1040 2381 C ATOM 3251 N7 A B 6 12.392 33.907 2.955 1.00 62.59 N ANISOU 3251 N7 A B 6 7830 8640 7312 1856 1048 2396 N ATOM 3252 C5 A B 6 13.038 35.084 3.301 1.00 68.69 C ANISOU 3252 C5 A B 6 8810 9409 7879 1842 865 2436 C ATOM 3253 C6 A B 6 12.574 36.414 3.434 1.00 74.21 C ANISOU 3253 C6 A B 6 9676 10081 8440 1869 767 2465 C ATOM 3254 N6 A B 6 11.299 36.763 3.226 1.00 73.22 N ANISOU 3254 N6 A B 6 9534 9919 8365 1912 852 2450 N ATOM 3255 N1 A B 6 13.470 37.365 3.786 1.00 73.43 N ANISOU 3255 N1 A B 6 9759 9991 8151 1851 572 2508 N ATOM 3256 C2 A B 6 14.746 36.999 3.991 1.00 71.43 C ANISOU 3256 C2 A B 6 9525 9763 7852 1809 491 2517 C ATOM 3257 N3 A B 6 15.296 35.784 3.894 1.00 69.42 N ANISOU 3257 N3 A B 6 9130 9534 7712 1774 570 2483 N ATOM 3258 C4 A B 6 14.382 34.857 3.543 1.00 66.73 C ANISOU 3258 C4 A B 6 8604 9193 7557 1793 756 2444 C ATOM 3259 P A B 7 14.962 29.056 6.596 1.00 56.76 P ANISOU 3259 P A B 7 7157 7661 6747 2112 1407 2472 P ATOM 3260 OP1 A B 7 13.760 29.912 6.698 1.00 62.53 O ANISOU 3260 OP1 A B 7 7969 8333 7456 2200 1468 2519 O ATOM 3261 OP2 A B 7 15.884 28.923 7.740 1.00 62.57 O ANISOU 3261 OP2 A B 7 8099 8301 7374 2174 1374 2507 O ATOM 3262 O5' A B 7 14.504 27.587 6.164 1.00 66.80 O ANISOU 3262 O5' A B 7 8160 8980 8239 2099 1558 2423 O ATOM 3263 C5' A B 7 13.261 27.308 5.521 1.00 63.12 C ANISOU 3263 C5' A B 7 7514 8537 7932 2121 1687 2410 C ATOM 3264 C4' A B 7 13.388 25.935 4.885 1.00 63.13 C ANISOU 3264 C4' A B 7 7239 8628 8119 2059 1743 2348 C ATOM 3265 O4' A B 7 14.306 26.050 3.763 1.00 56.65 O ANISOU 3265 O4' A B 7 6274 7962 7287 1886 1571 2276 O ATOM 3266 C3' A B 7 14.034 24.862 5.766 1.00 57.16 C ANISOU 3266 C3' A B 7 6512 7825 7381 2100 1791 2351 C ATOM 3267 O3' A B 7 13.101 24.200 6.586 1.00 59.64 O ANISOU 3267 O3' A B 7 6847 8027 7787 2248 1987 2400 O ATOM 3268 C2' A B 7 14.572 23.891 4.724 1.00 57.21 C ANISOU 3268 C2' A B 7 6234 7984 7519 1967 1735 2267 C ATOM 3269 O2' A B 7 13.564 23.057 4.193 1.00 55.61 O ANISOU 3269 O2' A B 7 5798 7810 7522 2003 1873 2254 O ATOM 3270 C1' A B 7 15.067 24.857 3.654 1.00 54.72 C ANISOU 3270 C1' A B 7 5880 7786 7125 1827 1558 2226 C ATOM 3271 N9 A B 7 16.481 25.145 3.822 1.00 48.63 N ANISOU 3271 N9 A B 7 5222 7051 6204 1735 1385 2202 N ATOM 3272 C8 A B 7 17.068 26.299 4.244 1.00 44.04 C ANISOU 3272 C8 A B 7 4881 6424 5428 1729 1263 2236 C ATOM 3273 N7 A B 7 18.369 26.237 4.303 1.00 47.72 N ANISOU 3273 N7 A B 7 5396 6932 5803 1641 1121 2200 N ATOM 3274 C5 A B 7 18.659 24.947 3.895 1.00 47.62 C ANISOU 3274 C5 A B 7 5160 7004 5930 1580 1150 2134 C ATOM 3275 C6 A B 7 19.868 24.246 3.720 1.00 46.59 C ANISOU 3275 C6 A B 7 4956 6954 5792 1471 1041 2063 C ATOM 3276 N6 A B 7 21.074 24.780 3.958 1.00 44.07 N ANISOU 3276 N6 A B 7 4796 6633 5314 1404 884 2047 N ATOM 3277 N1 A B 7 19.781 22.970 3.298 1.00 38.83 N ANISOU 3277 N1 A B 7 3730 6053 4973 1437 1097 2008 N ATOM 3278 C2 A B 7 18.587 22.435 3.058 1.00 45.93 C ANISOU 3278 C2 A B 7 4468 6947 6035 1510 1251 2027 C ATOM 3279 N3 A B 7 17.393 22.999 3.172 1.00 41.60 N ANISOU 3279 N3 A B 7 3970 6320 5514 1614 1369 2090 N ATOM 3280 C4 A B 7 17.503 24.261 3.600 1.00 46.42 C ANISOU 3280 C4 A B 7 4826 6857 5956 1640 1309 2138 C ATOM 3281 P U B 8 13.343 24.062 8.161 1.00 56.21 P ANISOU 3281 P U B 8 6667 7435 7254 2380 2054 2464 P ATOM 3282 OP1 U B 8 12.259 23.206 8.709 1.00 62.79 O ANISOU 3282 OP1 U B 8 7443 8187 8228 2511 2265 2502 O ATOM 3283 OP2 U B 8 13.568 25.404 8.742 1.00 60.06 O ANISOU 3283 OP2 U B 8 7431 7846 7543 2424 1966 2518 O ATOM 3284 O5' U B 8 14.751 23.355 8.283 1.00 56.92 O ANISOU 3284 O5' U B 8 6742 7573 7313 2287 1946 2406 O ATOM 3285 C5' U B 8 15.288 23.183 9.586 1.00 52.02 C ANISOU 3285 C5' U B 8 6345 6821 6597 2374 1968 2439 C ATOM 3286 C4' U B 8 15.164 21.727 9.997 1.00 53.57 C ANISOU 3286 C4' U B 8 6422 6997 6934 2412 2093 2417 C ATOM 3287 O4' U B 8 16.016 20.929 9.133 1.00 53.36 O ANISOU 3287 O4' U B 8 6178 7116 6978 2258 1987 2323 O ATOM 3288 C3' U B 8 15.624 21.387 11.406 1.00 58.90 C ANISOU 3288 C3' U B 8 7321 7524 7535 2512 2141 2446 C ATOM 3289 O3' U B 8 14.538 21.580 12.313 1.00 72.80 O ANISOU 3289 O3' U B 8 9214 9147 9301 2685 2306 2535 O ATOM 3290 C2' U B 8 15.920 19.903 11.263 1.00 54.74 C ANISOU 3290 C2' U B 8 6594 7058 7149 2457 2176 2377 C ATOM 3291 O2' U B 8 14.752 19.101 11.299 1.00 65.24 O ANISOU 3291 O2' U B 8 7770 8375 8644 2542 2353 2406 O ATOM 3292 C1' U B 8 16.530 19.843 9.873 1.00 48.29 C ANISOU 3292 C1' U B 8 5551 6427 6370 2277 2025 2294 C ATOM 3293 N1 U B 8 18.023 19.886 9.903 1.00 46.46 N ANISOU 3293 N1 U B 8 5401 6228 6023 2164 1850 2225 N ATOM 3294 C2 U B 8 18.663 18.687 10.109 1.00 41.20 C ANISOU 3294 C2 U B 8 4650 5586 5419 2116 1840 2155 C ATOM 3295 O2 U B 8 18.054 17.640 10.273 1.00 50.26 O ANISOU 3295 O2 U B 8 5659 6730 6707 2165 1962 2153 O ATOM 3296 N3 U B 8 20.033 18.756 10.126 1.00 38.53 N ANISOU 3296 N3 U B 8 4395 5272 4973 2008 1677 2085 N ATOM 3297 C4 U B 8 20.804 19.894 9.964 1.00 41.25 C ANISOU 3297 C4 U B 8 4896 5618 5159 1951 1529 2086 C ATOM 3298 O4 U B 8 22.024 19.807 10.008 1.00 37.92 O ANISOU 3298 O4 U B 8 4538 5213 4656 1858 1392 2017 O ATOM 3299 C5 U B 8 20.065 21.113 9.763 1.00 45.49 C ANISOU 3299 C5 U B 8 5512 6133 5638 2009 1545 2168 C ATOM 3300 C6 U B 8 18.722 21.065 9.740 1.00 50.36 C ANISOU 3300 C6 U B 8 6052 6727 6357 2109 1702 2230 C ATOM 3301 P C B 9 14.754 22.298 13.727 1.00105.17 P ANISOU 3301 P C B 9 13658 13067 13235 2824 2319 2610 P ATOM 3302 OP1 C B 9 13.538 23.083 14.018 1.00106.53 O ANISOU 3302 OP1 C B 9 13919 13170 13388 2952 2420 2697 O ATOM 3303 OP2 C B 9 16.076 22.964 13.733 1.00109.23 O ANISOU 3303 OP2 C B 9 14320 13589 13595 2743 2128 2579 O ATOM 3304 O5' C B 9 14.836 21.051 14.723 1.00195.52 O ANISOU 3304 O5' C B 9 25124 24414 24749 2901 2443 2604 O ATOM 3305 C5' C B 9 13.893 19.990 14.613 1.00195.17 C ANISOU 3305 C5' C B 9 24880 24391 24883 2941 2604 2606 C ATOM 3306 C4' C B 9 14.025 19.045 15.793 1.00193.84 C ANISOU 3306 C4' C B 9 24807 24103 24741 3033 2709 2614 C ATOM 3307 O4' C B 9 15.271 18.312 15.693 1.00193.12 O ANISOU 3307 O4' C B 9 24672 24059 24646 2914 2596 2520 O ATOM 3308 C3' C B 9 14.078 19.742 17.145 1.00192.77 C ANISOU 3308 C3' C B 9 24999 23784 24460 3184 2746 2691 C ATOM 3309 O3' C B 9 12.759 19.958 17.640 1.00191.53 O ANISOU 3309 O3' C B 9 24885 23548 24340 3336 2912 2783 O ATOM 3310 C2' C B 9 14.853 18.740 17.996 1.00193.54 C ANISOU 3310 C2' C B 9 25167 23803 24568 3193 2763 2645 C ATOM 3311 O2' C B 9 14.016 17.749 18.562 1.00193.76 O ANISOU 3311 O2' C B 9 25124 23776 24720 3289 2942 2673 O ATOM 3312 C1' C B 9 15.820 18.116 16.986 1.00193.39 C ANISOU 3312 C1' C B 9 24944 23936 24597 3000 2622 2530 C ATOM 3313 N1 C B 9 17.206 18.695 17.030 1.00191.60 N ANISOU 3313 N1 C B 9 24880 23698 24223 2915 2438 2478 N ATOM 3314 C2 C B 9 18.271 17.925 17.524 1.00188.12 C ANISOU 3314 C2 C B 9 24499 23214 23765 2865 2383 2397 C ATOM 3315 O2 C B 9 18.057 16.770 17.917 1.00186.84 O ANISOU 3315 O2 C B 9 24253 23030 23709 2888 2481 2369 O ATOM 3316 N3 C B 9 19.515 18.469 17.557 1.00185.06 N ANISOU 3316 N3 C B 9 24263 22807 23247 2793 2218 2348 N ATOM 3317 C4 C B 9 19.715 19.717 17.125 1.00183.21 C ANISOU 3317 C4 C B 9 24111 22600 22900 2771 2108 2383 C ATOM 3318 N4 C B 9 20.959 20.207 17.178 1.00179.21 N ANISOU 3318 N4 C B 9 23751 22070 22269 2704 1945 2336 N ATOM 3319 C5 C B 9 18.646 20.517 16.621 1.00186.24 C ANISOU 3319 C5 C B 9 24433 23034 23295 2817 2155 2465 C ATOM 3320 C6 C B 9 17.423 19.972 16.592 1.00189.73 C ANISOU 3320 C6 C B 9 24732 23490 23868 2887 2321 2506 C TER 3321 C B 9 HETATM 3322 O HOH A 1 26.007 39.368 -9.292 1.00 29.47 O HETATM 3323 O HOH A 2 33.093 28.413 -6.354 1.00 33.72 O HETATM 3324 O HOH A 3 -2.989 54.033 -9.256 1.00 34.20 O HETATM 3325 O HOH A 4 22.350 27.605 1.105 1.00 37.34 O HETATM 3326 O HOH A 5 -0.617 63.106 -26.212 1.00 34.72 O HETATM 3327 O HOH A 8 35.182 15.794 20.600 1.00 31.73 O HETATM 3328 O HOH A 9 7.306 53.437 -7.689 1.00 37.87 O HETATM 3329 O HOH A 10 36.555 39.836 -9.800 1.00 32.54 O HETATM 3330 O HOH A 12 2.597 59.257 -23.680 1.00 34.07 O HETATM 3331 O HOH A 13 27.215 32.844 -5.255 1.00 32.81 O HETATM 3332 O HOH A 14 37.889 3.170 12.526 1.00 46.12 O HETATM 3333 O HOH A 15 4.604 48.170 -25.378 1.00 38.14 O HETATM 3334 O HOH A 16 9.270 40.972 -3.282 1.00 46.46 O HETATM 3335 O HOH A 17 28.228 42.874 -7.897 1.00 40.54 O HETATM 3336 O HOH A 18 34.055 30.352 -4.527 1.00 38.82 O HETATM 3337 O HOH A 20 3.817 57.515 -26.405 1.00 30.34 O HETATM 3338 O HOH A 21 -0.790 57.985 -10.779 1.00 32.75 O HETATM 3339 O HOH A 22 6.615 34.279 -18.479 1.00 38.95 O HETATM 3340 O HOH A 23 -10.932 56.716 -18.016 1.00 39.27 O HETATM 3341 O HOH A 24 30.963 36.872 -6.571 1.00 39.06 O HETATM 3342 O HOH A 28 -1.428 54.675 -26.452 1.00 47.96 O HETATM 3343 O HOH A 29 17.817 49.014 -7.457 1.00 39.76 O HETATM 3344 O HOH A 30 8.204 51.198 -6.828 1.00 38.89 O HETATM 3345 O HOH A 32 1.922 57.280 -11.259 1.00 47.41 O HETATM 3346 O HOH A 33 9.791 47.210 -7.361 1.00 49.08 O HETATM 3347 O HOH A 35 16.975 36.497 -7.974 1.00 37.73 O HETATM 3348 O HOH A 36 45.252 14.475 15.419 1.00 47.98 O HETATM 3349 O HOH A 37 11.958 32.397 -6.039 1.00 40.04 O HETATM 3350 O HOH A 39 -7.406 68.061 -13.362 1.00 39.04 O HETATM 3351 O HOH A 42 4.667 39.689 -15.626 1.00 37.23 O HETATM 3352 O HOH A 47 17.991 29.968 -1.312 1.00 41.81 O HETATM 3353 O HOH A 49 3.232 62.004 -23.833 1.00 34.58 O HETATM 3354 O HOH A 50 -5.039 52.955 -17.255 1.00 42.35 O HETATM 3355 O HOH A 51 19.191 55.507 -15.173 1.00 30.79 O HETATM 3356 O HOH A 53 -5.535 53.810 -4.873 1.00 46.92 O HETATM 3357 O HOH A 57 0.952 57.351 -26.727 1.00 47.09 O HETATM 3358 O HOH A 59 12.910 34.316 -7.566 1.00 33.80 O HETATM 3359 O HOH A 61 -5.731 61.017 -17.659 1.00 45.67 O HETATM 3360 O HOH A 63 37.089 19.004 11.520 1.00 46.13 O HETATM 3361 O HOH A 64 -4.705 53.155 -2.061 1.00 43.44 O HETATM 3362 O HOH A 65 -3.076 54.339 -6.255 1.00 31.50 O HETATM 3363 O HOH A 68 35.484 2.926 24.203 1.00 46.78 O HETATM 3364 O HOH A 69 35.625 25.431 2.976 1.00 40.77 O HETATM 3365 O HOH A 76 41.416 5.564 14.503 1.00 48.24 O HETATM 3366 O HOH A 81 32.471 17.406 15.338 1.00 46.34 O HETATM 3367 O HOH A 82 24.895 20.929 6.685 1.00 40.67 O HETATM 3368 O HOH A 83 11.343 62.696 -24.298 1.00 38.19 O HETATM 3369 O HOH A 84 37.230 26.268 -3.183 1.00 41.58 O HETATM 3370 O HOH A 87 31.005 40.329 -14.271 1.00 38.87 O HETATM 3371 O HOH A 90 29.510 44.287 -17.873 1.00 45.02 O HETATM 3372 O HOH A 104 16.253 40.731 -7.604 1.00 44.99 O HETATM 3373 O HOH A 108 43.045 11.671 19.080 1.00 42.16 O HETATM 3374 O HOH A 109 40.112 4.710 11.426 1.00 47.37 O HETATM 3375 O HOH A 113 13.702 10.410 9.892 1.00 46.08 O HETATM 3376 O HOH A 114 32.344 40.108 -16.873 1.00 43.52 O HETATM 3377 O HOH A 115 31.222 17.743 9.424 1.00 44.98 O HETATM 3378 O HOH A 119 38.923 11.555 7.349 1.00 45.06 O HETATM 3379 O HOH A 123 25.696 47.529 -8.356 1.00 42.49 O HETATM 3380 O HOH A 126 6.395 29.665 -12.920 1.00 39.11 O HETATM 3381 O HOH A 130 4.359 33.563 -14.058 1.00 44.63 O HETATM 3382 O HOH A 134 38.070 28.872 -9.913 1.00 47.33 O HETATM 3383 O HOH A 138 41.313 38.355 -10.257 1.00 43.46 O HETATM 3384 O HOH A 142 36.847 30.204 -12.133 1.00 35.88 O HETATM 3385 O HOH A 147 42.410 3.086 18.193 1.00 45.12 O HETATM 3386 O HOH A 149 3.503 44.241 -9.396 1.00 46.40 O HETATM 3387 O HOH A 152 31.848 44.554 -6.697 1.00 45.61 O HETATM 3388 O HOH A 153 15.738 34.205 -7.265 1.00 34.97 O HETATM 3389 O HOH A 155 -0.186 40.589 -15.281 1.00 39.82 O HETATM 3390 O HOH A 156 32.589 34.883 -5.242 1.00 39.35 O HETATM 3391 O HOH A 157 17.556 25.490 7.621 1.00 44.05 O HETATM 3392 O HOH A 158 36.292 25.296 -19.837 1.00 40.66 O HETATM 3393 O HOH A 159 38.130 26.598 -11.420 1.00 43.11 O HETATM 3394 O HOH A 160 11.429 34.726 -24.063 1.00 47.36 O HETATM 3395 O HOH A 162 37.455 27.420 -21.283 1.00 47.13 O HETATM 3396 O HOH A 576 -5.459 48.936 -13.828 1.00 40.67 O HETATM 3397 O HOH A 577 46.766 32.505 -14.285 1.00 46.87 O HETATM 3398 O HOH A 578 25.241 50.540 -17.792 1.00 43.84 O HETATM 3399 O HOH A 579 0.486 44.100 -21.018 1.00 51.80 O HETATM 3400 O HOH A 580 -4.478 62.858 -29.857 1.00 44.60 O HETATM 3401 O HOH A 581 37.487 14.789 19.538 1.00 40.17 O HETATM 3402 O HOH A 582 11.596 52.868 -28.158 1.00 47.52 O HETATM 3403 O HOH A 583 7.716 26.580 -7.977 1.00 45.64 O HETATM 3404 O HOH A 584 44.585 5.372 5.774 1.00 44.60 O HETATM 3405 O HOH A 585 26.379 19.027 -18.337 1.00 45.35 O HETATM 3406 O HOH A 586 -7.568 58.652 -18.108 1.00 46.02 O HETATM 3407 O HOH A 587 23.901 53.006 -14.723 1.00 44.45 O HETATM 3408 O HOH A 588 -6.251 60.999 -30.724 1.00 48.62 O HETATM 3409 O HOH A 589 26.837 35.971 -23.603 1.00 48.89 O HETATM 3410 O HOH A 590 26.102 18.234 14.317 1.00 47.98 O HETATM 3411 O HOH A 591 38.544 15.829 17.193 1.00 48.08 O HETATM 3412 O HOH A 592 41.721 14.210 20.888 1.00 47.19 O HETATM 3413 O HOH A 593 29.955 -0.897 3.415 1.00 47.57 O HETATM 3414 O HOH A 594 14.866 26.158 0.286 1.00 40.26 O HETATM 3415 O HOH A 595 18.589 56.668 -11.696 1.00 46.29 O HETATM 3416 O HOH A 596 27.991 31.383 -3.246 1.00 40.25 O HETATM 3417 O HOH A 597 39.825 18.937 10.615 1.00 41.05 O HETATM 3418 O HOH A 598 17.983 57.499 -9.179 1.00 50.06 O HETATM 3419 O HOH A 599 9.234 55.278 -7.144 1.00 49.77 O HETATM 3420 O HOH A 600 12.374 65.216 -24.493 1.00 49.76 O HETATM 3421 O HOH A 601 16.881 22.588 -24.929 1.00 48.88 O HETATM 3422 O HOH A 602 -3.313 62.861 -26.690 1.00 49.45 O HETATM 3423 O HOH A 603 12.615 55.395 -27.910 1.00 53.05 O HETATM 3424 O HOH A 604 32.615 20.048 -15.257 1.00 47.74 O HETATM 3425 O HOH A 605 19.888 13.048 26.325 1.00 48.85 O HETATM 3426 O HOH A 606 25.876 29.531 -2.681 1.00 49.90 O HETATM 3427 O HOH A 607 36.544 17.683 16.387 1.00 47.82 O HETATM 3428 O HOH A 608 -6.564 55.983 -17.979 1.00 47.39 O HETATM 3429 O HOH A 609 41.577 40.972 -9.536 1.00 50.30 O HETATM 3430 O HOH A 610 38.682 20.989 14.238 1.00 47.53 O HETATM 3431 O HOH A 611 11.119 20.165 4.066 1.00 51.83 O HETATM 3432 O HOH A 612 34.700 6.615 6.837 1.00 50.14 O HETATM 3433 O HOH A 613 -2.008 49.046 -23.824 1.00 51.91 O HETATM 3434 O HOH A 614 -2.084 47.727 -7.798 1.00 36.88 O HETATM 3435 O HOH B 11 -3.848 51.539 -8.939 1.00 40.07 O HETATM 3436 O HOH B 26 1.354 49.610 -2.740 1.00 39.89 O HETATM 3437 O HOH B 44 3.364 44.580 -2.638 1.00 43.44 O HETATM 3438 O HOH B 58 17.132 33.026 -0.142 1.00 44.26 O HETATM 3439 O HOH B 125 4.108 49.014 -2.745 1.00 38.30 O HETATM 3440 O HOH B 127 6.273 35.269 -7.167 1.00 44.86 O HETATM 3441 O HOH B 150 9.096 28.876 0.250 1.00 46.68 O HETATM 3442 O HOH B 161 15.845 28.297 -1.436 1.00 41.53 O HETATM 3443 O HOH B 215 2.132 36.415 -5.989 1.00 49.80 O HETATM 3444 O HOH B 275 5.393 44.446 -4.779 1.00 47.19 O HETATM 3445 O HOH B 327 17.021 38.653 -5.676 1.00 50.80 O MASTER 491 0 0 28 2 0 0 6 3443 2 0 33 END
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Ligand Name
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PDBbind
9-mer
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Entry Information
PDB ID
3k61
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
2.21(Å)
Affinity (Kd/Ki/IC50)
Kd=96.9nM
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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times since Nov 2007.
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