Browse entries in the PDBbind-CN Database
HEADER CELL ADHESION 15-FEB-09 3G9W TITLE CRYSTAL STRUCTURE OF TALIN2 F2-F3 IN COMPLEX WITH THE INTEGRIN BETA1D TITLE 2 CYTOPLASMIC TAIL COMPND MOL_ID: 1; COMPND 2 MOLECULE: TALIN-2; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: F2-F3 DOMAIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: INTEGRIN BETA-1D; COMPND 8 CHAIN: C, D; COMPND 9 FRAGMENT: CYTOPLASMIC TAIL; COMPND 10 SYNONYM: FIBRONECTIN RECEPTOR SUBUNIT BETA, INTEGRIN VLA-4 SUBUNIT COMPND 11 BETA; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: TLN2; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET151; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_COMMON: HUMAN; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 GENE: ITGB1; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET16B KEYWDS PROTEIN-PROTEIN COMPLEX, PH DOMAIN SUPERFOLD, PTB DOMAIN, HELICAL KEYWDS 2 BUNDLE, INTRINSICALLY UNSTRUCTURED, CELL ADHESION EXPDTA X-RAY DIFFRACTION AUTHOR N.J.ANTHIS,K.L.WEGENER,F.YE,C.KIM,E.D.LOWE,I.VAKONAKIS,N.BATE, AUTHOR 2 D.R.CRITCHLEY,M.H.GINSBERG,I.D.CAMPBELL REVDAT 3 05-FEB-14 3G9W 1 JRNL REVDAT 2 13-JUL-11 3G9W 1 VERSN REVDAT 1 20-OCT-09 3G9W 0 JRNL AUTH N.J.ANTHIS,K.L.WEGENER,F.YE,C.KIM,B.T.GOULT,E.D.LOWE, JRNL AUTH 2 I.VAKONAKIS,N.BATE,D.R.CRITCHLEY,M.H.GINSBERG,I.D.CAMPBELL JRNL TITL THE STRUCTURE OF AN INTEGRIN/TALIN COMPLEX REVEALS THE BASIS JRNL TITL 2 OF INSIDE-OUT SIGNAL TRANSDUCTION JRNL REF EMBO J. V. 28 3623 2009 JRNL REFN ISSN 0261-4189 JRNL PMID 19798053 JRNL DOI 10.1038/EMBOJ.2009.287 REMARK 2 REMARK 2 RESOLUTION. 2.17 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (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) : 2.17 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.94 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.970 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6 REMARK 3 NUMBER OF REFLECTIONS : 41362 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.215 REMARK 3 R VALUE (WORKING SET) : 0.213 REMARK 3 FREE R VALUE : 0.248 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070 REMARK 3 FREE R VALUE TEST SET COUNT : 2068 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 41.9490 - 6.5660 0.95 2568 127 0.1670 0.1490 REMARK 3 2 6.5660 - 5.2150 0.96 2558 148 0.1630 0.2060 REMARK 3 3 5.2150 - 4.5570 0.97 2601 123 0.1520 0.1680 REMARK 3 4 4.5570 - 4.1400 0.97 2551 169 0.1590 0.2130 REMARK 3 5 4.1400 - 3.8440 0.97 2598 136 0.1690 0.1620 REMARK 3 6 3.8440 - 3.6170 0.97 2596 160 0.1740 0.2150 REMARK 3 7 3.6170 - 3.4360 0.98 2621 137 0.1930 0.2210 REMARK 3 8 3.4360 - 3.2870 0.98 2587 123 0.1960 0.2970 REMARK 3 9 3.2870 - 3.1600 0.98 2618 145 0.2010 0.2240 REMARK 3 10 3.1600 - 3.0510 0.98 2643 145 0.2090 0.2430 REMARK 3 11 3.0510 - 2.9560 0.99 2565 159 0.2220 0.2470 REMARK 3 12 2.9560 - 2.8710 0.99 2701 131 0.2250 0.2490 REMARK 3 13 2.8710 - 2.7960 0.99 2598 145 0.2270 0.2450 REMARK 3 14 2.7960 - 2.7280 0.99 2691 136 0.2330 0.3250 REMARK 3 15 2.7280 - 2.6660 0.99 2648 134 0.2320 0.2840 REMARK 3 16 2.6660 - 2.6090 1.00 2678 142 0.2380 0.2830 REMARK 3 17 2.6090 - 2.5570 1.00 2686 124 0.2400 0.3540 REMARK 3 18 2.5570 - 2.5090 1.00 2650 144 0.2390 0.2830 REMARK 3 19 2.5090 - 2.4640 1.00 2665 148 0.2410 0.2800 REMARK 3 20 2.4640 - 2.4220 1.00 2604 132 0.2400 0.2920 REMARK 3 21 2.4220 - 2.3830 1.00 2712 148 0.2410 0.3410 REMARK 3 22 2.3830 - 2.3460 1.00 2690 174 0.2500 0.2710 REMARK 3 23 2.3460 - 2.3120 1.00 2618 121 0.2400 0.3170 REMARK 3 24 2.3120 - 2.2790 1.00 2709 125 0.2430 0.2550 REMARK 3 25 2.2790 - 2.2480 1.00 2698 140 0.2500 0.2980 REMARK 3 26 2.2480 - 2.2190 1.00 2640 105 0.2430 0.3160 REMARK 3 27 2.2190 - 2.1910 1.00 2722 153 0.2480 0.2760 REMARK 3 28 2.1910 - 2.1650 0.97 2547 168 0.2630 0.2790 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : 0.33 REMARK 3 B_SOL : 36.25 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.320 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 25.31 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.26 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -2.19720 REMARK 3 B22 (A**2) : 2.58870 REMARK 3 B33 (A**2) : -5.18020 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.00000 REMARK 3 B23 (A**2) : -0.00000 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 : 0.005 4277 REMARK 3 ANGLE : 0.874 5729 REMARK 3 CHIRALITY : 0.063 597 REMARK 3 PLANARITY : 0.004 730 REMARK 3 DIHEDRAL : 16.317 1657 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 4 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: chain A REMARK 3 ORIGIN FOR THE GROUP (A): 27.2091 -3.8933 -22.0990 REMARK 3 T TENSOR REMARK 3 T11: 0.1074 T22: 0.1080 REMARK 3 T33: 0.1143 T12: -0.0043 REMARK 3 T13: 0.0031 T23: -0.0238 REMARK 3 L TENSOR REMARK 3 L11: -0.1339 L22: -0.0152 REMARK 3 L33: 1.1358 L12: -0.1017 REMARK 3 L13: 0.2667 L23: 0.3335 REMARK 3 S TENSOR REMARK 3 S11: -0.0491 S12: -0.0112 S13: 0.0303 REMARK 3 S21: 0.0587 S22: 0.0788 S23: 0.0246 REMARK 3 S31: -0.0486 S32: 0.0097 S33: -0.0152 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: chain B REMARK 3 ORIGIN FOR THE GROUP (A): 26.9590 7.5175 7.1256 REMARK 3 T TENSOR REMARK 3 T11: 0.1009 T22: 0.1155 REMARK 3 T33: 0.1440 T12: 0.0302 REMARK 3 T13: -0.0122 T23: 0.0222 REMARK 3 L TENSOR REMARK 3 L11: 0.0123 L22: 0.4876 REMARK 3 L33: 1.0843 L12: -0.0835 REMARK 3 L13: -0.1563 L23: 0.1370 REMARK 3 S TENSOR REMARK 3 S11: 0.1796 S12: 0.0887 S13: 0.0422 REMARK 3 S21: -0.1610 S22: -0.0637 S23: 0.1473 REMARK 3 S31: -0.0020 S32: -0.0902 S33: -0.1011 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: chain C REMARK 3 ORIGIN FOR THE GROUP (A): 41.4702 -1.7207 25.5769 REMARK 3 T TENSOR REMARK 3 T11: 0.1894 T22: 0.0900 REMARK 3 T33: 0.1035 T12: -0.0119 REMARK 3 T13: 0.0087 T23: 0.0069 REMARK 3 L TENSOR REMARK 3 L11: 0.3819 L22: -0.3197 REMARK 3 L33: 0.6451 L12: -0.2377 REMARK 3 L13: 0.4421 L23: -0.2080 REMARK 3 S TENSOR REMARK 3 S11: 0.0627 S12: -0.0448 S13: -0.0238 REMARK 3 S21: -0.1101 S22: -0.0922 S23: -0.0010 REMARK 3 S31: 0.1964 S32: -0.0957 S33: -0.0011 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: chain D REMARK 3 ORIGIN FOR THE GROUP (A): 11.7068 -14.0325 -40.9435 REMARK 3 T TENSOR REMARK 3 T11: 0.1251 T22: 0.1490 REMARK 3 T33: 0.1547 T12: -0.1136 REMARK 3 T13: -0.0318 T23: 0.0092 REMARK 3 L TENSOR REMARK 3 L11: -0.2491 L22: 0.2870 REMARK 3 L33: 0.0190 L12: -0.0979 REMARK 3 L13: -0.1063 L23: -0.1878 REMARK 3 S TENSOR REMARK 3 S11: 0.1198 S12: -0.0053 S13: 0.0500 REMARK 3 S21: 0.1366 S22: -0.1729 S23: 0.1144 REMARK 3 S31: -0.0939 S32: 0.0327 S33: 0.0405 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 3G9W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-FEB-09. REMARK 100 THE RCSB ID CODE IS RCSB051606. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 26-JUN-08 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID23-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.8726 REMARK 200 MONOCHROMATOR : HORIZONTALLY DIFFRACTING REMARK 200 MONOCHROMATOR REMARK 200 OPTICS : MONOCHROMATOR (HORIZONTALLY SIDE REMARK 200 DIFFRACTING SILICON 111 CRYSTAL) REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41362 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.165 REMARK 200 RESOLUTION RANGE LOW (A) : 41.950 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 200 DATA REDUNDANCY : 3.700 REMARK 200 R MERGE (I) : 0.11400 REMARK 200 R SYM (I) : 0.11400 REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.17 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9 REMARK 200 DATA REDUNDANCY IN SHELL : 3.70 REMARK 200 R MERGE FOR SHELL (I) : 0.33800 REMARK 200 R SYM FOR SHELL (I) : 0.33800 REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500 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 ENTRIES 1MIX, 1MK7, 1MK9 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 58.82 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M AMMONIUM ACETATE, 0.02M MAGNESIUM REMARK 280 CHLORIDE, 0.05M HEPES, 5% PEG 8K, PH 7.0, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 26.63000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.92500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.36000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.92500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.63000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.36000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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: 3290 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 15620 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D 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 350 REMARK 350 BIOMOLECULE: 2 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: 3470 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 14430 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C 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 GLY A 186 REMARK 465 ILE A 187 REMARK 465 ASP A 188 REMARK 465 PRO A 189 REMARK 465 PHE A 190 REMARK 465 THR A 191 REMARK 465 GLY B 186 REMARK 465 ILE B 187 REMARK 465 ASP B 188 REMARK 465 PRO B 189 REMARK 465 PHE B 190 REMARK 465 THR B 191 REMARK 465 GLY B 192 REMARK 465 ILE B 193 REMARK 465 ASP B 194 REMARK 465 PRO B 195 REMARK 465 PHE B 196 REMARK 465 THR B 197 REMARK 465 LYS B 198 REMARK 465 PHE B 199 REMARK 465 PHE B 200 REMARK 465 TYR B 201 REMARK 465 SER B 202 REMARK 465 ASP B 203 REMARK 465 GLN B 204 REMARK 465 ASN C 789 REMARK 465 PHE C 790 REMARK 465 LYS C 791 REMARK 465 ASN C 792 REMARK 465 PRO C 793 REMARK 465 ASN C 794 REMARK 465 TYR C 795 REMARK 465 GLY C 796 REMARK 465 ARG C 797 REMARK 465 LYS C 798 REMARK 465 ALA C 799 REMARK 465 GLY C 800 REMARK 465 LEU C 801 REMARK 465 PHE D 790 REMARK 465 LYS D 791 REMARK 465 ASN D 792 REMARK 465 PRO D 793 REMARK 465 ASN D 794 REMARK 465 TYR D 795 REMARK 465 GLY D 796 REMARK 465 ARG D 797 REMARK 465 LYS D 798 REMARK 465 ALA D 799 REMARK 465 GLY D 800 REMARK 465 LEU D 801 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 ILE A 193 160.51 152.05 REMARK 500 THR A 385 146.61 -171.82 REMARK 500 PRO B 259 132.30 -37.92 REMARK 500 THR B 385 146.19 -171.17 REMARK 500 THR C 777 -35.41 -37.17 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 618 DISTANCE = 5.12 ANGSTROMS REMARK 525 HOH A 622 DISTANCE = 5.59 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 409 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 410 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 409 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 410 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 411 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 16158 RELATED DB: BMRB REMARK 900 NMR ASSIGNMENTS OF THE BETA1D INTEGRIN TAIL REMARK 900 RELATED ID: 16159 RELATED DB: BMRB REMARK 900 NMR ASSIGNMENTS OF THE BETA1A INTEGRIN TAIL REMARK 900 RELATED ID: 16162 RELATED DB: BMRB REMARK 900 NMR ASSIGNMENTS OF THE BETA1D INTEGRIN TAIL WITH A C- REMARK 900 TERMINAL POLYHISTIDINE TAG REMARK 900 RELATED ID: 15552 RELATED DB: BMRB REMARK 900 NMR ASSIGNMENTS OF THE BETA3 INTEGRIN TAIL REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE SEQUENCE OF CHAIN C, D IS ISOFORM BETA-1D REMARK 999 AS LISTED IN UNP ENTRY, P05556-5 DBREF 3G9W A 198 408 UNP Q71LX4 TLN2_MOUSE 198 408 DBREF 3G9W B 198 408 UNP Q71LX4 TLN2_MOUSE 198 408 DBREF 3G9W C 752 801 UNP P05556 ITB1_HUMAN 752 801 DBREF 3G9W D 752 801 UNP P05556 ITB1_HUMAN 752 801 SEQADV 3G9W GLY A 186 UNP Q71LX4 EXPRESSION TAG SEQADV 3G9W ILE A 187 UNP Q71LX4 EXPRESSION TAG SEQADV 3G9W ASP A 188 UNP Q71LX4 EXPRESSION TAG SEQADV 3G9W PRO A 189 UNP Q71LX4 EXPRESSION TAG SEQADV 3G9W PHE A 190 UNP Q71LX4 EXPRESSION TAG SEQADV 3G9W THR A 191 UNP Q71LX4 EXPRESSION TAG SEQADV 3G9W GLY A 192 UNP Q71LX4 EXPRESSION TAG SEQADV 3G9W ILE A 193 UNP Q71LX4 EXPRESSION TAG SEQADV 3G9W ASP A 194 UNP Q71LX4 EXPRESSION TAG SEQADV 3G9W PRO A 195 UNP Q71LX4 EXPRESSION TAG SEQADV 3G9W PHE A 196 UNP Q71LX4 EXPRESSION TAG SEQADV 3G9W THR A 197 UNP Q71LX4 EXPRESSION TAG SEQADV 3G9W GLY B 186 UNP Q71LX4 EXPRESSION TAG SEQADV 3G9W ILE B 187 UNP Q71LX4 EXPRESSION TAG SEQADV 3G9W ASP B 188 UNP Q71LX4 EXPRESSION TAG SEQADV 3G9W PRO B 189 UNP Q71LX4 EXPRESSION TAG SEQADV 3G9W PHE B 190 UNP Q71LX4 EXPRESSION TAG SEQADV 3G9W THR B 191 UNP Q71LX4 EXPRESSION TAG SEQADV 3G9W GLY B 192 UNP Q71LX4 EXPRESSION TAG SEQADV 3G9W ILE B 193 UNP Q71LX4 EXPRESSION TAG SEQADV 3G9W ASP B 194 UNP Q71LX4 EXPRESSION TAG SEQADV 3G9W PRO B 195 UNP Q71LX4 EXPRESSION TAG SEQADV 3G9W PHE B 196 UNP Q71LX4 EXPRESSION TAG SEQADV 3G9W THR B 197 UNP Q71LX4 EXPRESSION TAG SEQADV 3G9W GLY C 750 UNP P05556 EXPRESSION TAG SEQADV 3G9W PRO C 751 UNP P05556 EXPRESSION TAG SEQADV 3G9W GLY D 750 UNP P05556 EXPRESSION TAG SEQADV 3G9W PRO D 751 UNP P05556 EXPRESSION TAG SEQRES 1 A 223 GLY ILE ASP PRO PHE THR GLY ILE ASP PRO PHE THR LYS SEQRES 2 A 223 PHE PHE TYR SER ASP GLN ASN VAL ASP SER ARG ASP PRO SEQRES 3 A 223 VAL GLN LEU ASN LEU LEU TYR VAL GLN ALA ARG ASP ASP SEQRES 4 A 223 ILE LEU ASN GLY SER HIS PRO VAL SER PHE GLU LYS ALA SEQRES 5 A 223 CYS GLU PHE GLY GLY PHE GLN ALA GLN ILE GLN PHE GLY SEQRES 6 A 223 PRO HIS VAL GLU HIS LYS HIS LYS PRO GLY PHE LEU ASP SEQRES 7 A 223 LEU LYS GLU PHE LEU PRO LYS GLU TYR ILE LYS GLN ARG SEQRES 8 A 223 GLY ALA GLU LYS ARG ILE PHE GLN GLU HIS LYS ASN CYS SEQRES 9 A 223 GLY GLU MET SER GLU ILE GLU ALA LYS VAL LYS TYR VAL SEQRES 10 A 223 LYS LEU ALA ARG SER LEU ARG THR TYR GLY VAL SER PHE SEQRES 11 A 223 PHE LEU VAL LYS GLU LYS MET LYS GLY LYS ASN LYS LEU SEQRES 12 A 223 VAL PRO ARG LEU LEU GLY ILE THR LYS ASP SER VAL MET SEQRES 13 A 223 ARG VAL ASP GLU LYS THR LYS GLU VAL LEU GLN GLU TRP SEQRES 14 A 223 PRO LEU THR THR VAL LYS ARG TRP ALA ALA SER PRO LYS SEQRES 15 A 223 SER PHE THR LEU ASP PHE GLY GLU TYR GLN GLU SER TYR SEQRES 16 A 223 TYR SER VAL GLN THR THR GLU GLY GLU GLN ILE SER GLN SEQRES 17 A 223 LEU ILE ALA GLY TYR ILE ASP ILE ILE LEU LYS LYS LYS SEQRES 18 A 223 GLN SER SEQRES 1 B 223 GLY ILE ASP PRO PHE THR GLY ILE ASP PRO PHE THR LYS SEQRES 2 B 223 PHE PHE TYR SER ASP GLN ASN VAL ASP SER ARG ASP PRO SEQRES 3 B 223 VAL GLN LEU ASN LEU LEU TYR VAL GLN ALA ARG ASP ASP SEQRES 4 B 223 ILE LEU ASN GLY SER HIS PRO VAL SER PHE GLU LYS ALA SEQRES 5 B 223 CYS GLU PHE GLY GLY PHE GLN ALA GLN ILE GLN PHE GLY SEQRES 6 B 223 PRO HIS VAL GLU HIS LYS HIS LYS PRO GLY PHE LEU ASP SEQRES 7 B 223 LEU LYS GLU PHE LEU PRO LYS GLU TYR ILE LYS GLN ARG SEQRES 8 B 223 GLY ALA GLU LYS ARG ILE PHE GLN GLU HIS LYS ASN CYS SEQRES 9 B 223 GLY GLU MET SER GLU ILE GLU ALA LYS VAL LYS TYR VAL SEQRES 10 B 223 LYS LEU ALA ARG SER LEU ARG THR TYR GLY VAL SER PHE SEQRES 11 B 223 PHE LEU VAL LYS GLU LYS MET LYS GLY LYS ASN LYS LEU SEQRES 12 B 223 VAL PRO ARG LEU LEU GLY ILE THR LYS ASP SER VAL MET SEQRES 13 B 223 ARG VAL ASP GLU LYS THR LYS GLU VAL LEU GLN GLU TRP SEQRES 14 B 223 PRO LEU THR THR VAL LYS ARG TRP ALA ALA SER PRO LYS SEQRES 15 B 223 SER PHE THR LEU ASP PHE GLY GLU TYR GLN GLU SER TYR SEQRES 16 B 223 TYR SER VAL GLN THR THR GLU GLY GLU GLN ILE SER GLN SEQRES 17 B 223 LEU ILE ALA GLY TYR ILE ASP ILE ILE LEU LYS LYS LYS SEQRES 18 B 223 GLN SER SEQRES 1 C 52 GLY PRO LYS LEU LEU MET ILE ILE HIS ASP ARG ARG GLU SEQRES 2 C 52 PHE ALA LYS PHE GLU LYS GLU LYS MET ASN ALA LYS TRP SEQRES 3 C 52 ASP THR GLN GLU ASN PRO ILE TYR LYS SER PRO ILE ASN SEQRES 4 C 52 ASN PHE LYS ASN PRO ASN TYR GLY ARG LYS ALA GLY LEU SEQRES 1 D 52 GLY PRO LYS LEU LEU MET ILE ILE HIS ASP ARG ARG GLU SEQRES 2 D 52 PHE ALA LYS PHE GLU LYS GLU LYS MET ASN ALA LYS TRP SEQRES 3 D 52 ASP THR GLN GLU ASN PRO ILE TYR LYS SER PRO ILE ASN SEQRES 4 D 52 ASN PHE LYS ASN PRO ASN TYR GLY ARG LYS ALA GLY LEU HET GOL A 1 6 HET GOL A 409 6 HET PEG A 410 7 HET GOL B 1 6 HET GOL B 409 6 HET PEG B 410 7 HET GOL B 411 6 HET GOL C 1 6 HETNAM GOL GLYCEROL HETNAM PEG DI(HYDROXYETHYL)ETHER HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 5 GOL 6(C3 H8 O3) FORMUL 7 PEG 2(C4 H10 O3) FORMUL 13 HOH *381(H2 O) HELIX 1 1 ASP A 194 LYS A 198 5 5 HELIX 2 2 ASP A 210 ASN A 227 1 18 HELIX 3 3 SER A 233 GLY A 250 1 18 HELIX 4 4 ASP A 263 PHE A 267 5 5 HELIX 5 5 PRO A 269 ILE A 273 5 5 HELIX 6 6 GLY A 277 CYS A 289 1 13 HELIX 7 7 SER A 293 LEU A 308 1 16 HELIX 8 8 THR A 357 VAL A 359 5 3 HELIX 9 9 PHE A 373 GLN A 377 5 5 HELIX 10 10 GLU A 387 SER A 408 1 22 HELIX 11 11 ASP B 210 ASN B 227 1 18 HELIX 12 12 SER B 233 GLY B 250 1 18 HELIX 13 13 ASP B 263 PHE B 267 5 5 HELIX 14 14 PRO B 269 ILE B 273 5 5 HELIX 15 15 GLY B 277 CYS B 289 1 13 HELIX 16 16 SER B 293 LEU B 308 1 16 HELIX 17 17 THR B 357 VAL B 359 5 3 HELIX 18 18 PHE B 373 GLN B 377 5 5 HELIX 19 19 GLU B 387 GLN B 407 1 21 HELIX 20 20 GLY C 750 LYS C 770 1 21 HELIX 21 21 MET C 771 ALA C 773 5 3 HELIX 22 22 GLY D 750 LYS D 770 1 21 HELIX 23 23 MET D 771 ALA D 773 5 3 HELIX 24 24 SER D 785 ASN D 789 5 5 SHEET 1 A 4 SER A 314 LYS A 321 0 SHEET 2 A 4 LEU A 328 ILE A 335 -1 O LEU A 333 N PHE A 316 SHEET 3 A 4 SER A 339 VAL A 343 -1 O VAL A 343 N LEU A 332 SHEET 4 A 4 VAL A 350 PRO A 355 -1 O TRP A 354 N VAL A 340 SHEET 1 B 4 TYR A 381 GLN A 384 0 SHEET 2 B 4 SER A 368 ASP A 372 -1 N LEU A 371 O TYR A 381 SHEET 3 B 4 ARG A 361 SER A 365 -1 N ARG A 361 O ASP A 372 SHEET 4 B 4 LYS D 774 TRP D 775 -1 O LYS D 774 N ALA A 364 SHEET 1 C 4 SER B 314 LYS B 321 0 SHEET 2 C 4 LEU B 328 ILE B 335 -1 O ARG B 331 N VAL B 318 SHEET 3 C 4 SER B 339 VAL B 343 -1 O VAL B 343 N LEU B 332 SHEET 4 C 4 VAL B 350 PRO B 355 -1 O TRP B 354 N VAL B 340 SHEET 1 D 4 TYR B 381 GLN B 384 0 SHEET 2 D 4 SER B 368 ASP B 372 -1 N LEU B 371 O TYR B 381 SHEET 3 D 4 ARG B 361 ALA B 364 -1 N ARG B 361 O ASP B 372 SHEET 4 D 4 LYS C 774 TRP C 775 -1 O LYS C 774 N ALA B 364 SITE 1 AC1 5 GLY A 228 HOH A 559 HOH A 603 HOH A 605 SITE 2 AC1 5 HOH B 509 SITE 1 AC2 10 ASP A 224 SER A 229 HIS A 230 GLY A 312 SITE 2 AC2 10 VAL A 313 SER A 314 HOH A 657 HOH A 663 SITE 3 AC2 10 HOH A 665 ILE C 757 SITE 1 AC3 6 ARG A 342 GLN A 352 GLN A 377 TYR A 380 SITE 2 AC3 6 HOH A 565 HOH A 695 SITE 1 AC4 8 GLY B 228 SER B 229 PHE B 315 HOH B 491 SITE 2 AC4 8 HOH B 496 HOH B 528 HOH B 578 HOH B 581 SITE 1 AC5 5 GLU A 387 LYS B 321 GLY B 324 LYS B 325 SITE 2 AC5 5 ASN B 326 SITE 1 AC6 8 GLU B 320 LYS B 321 ARG B 342 GLN B 352 SITE 2 AC6 8 GLN B 377 HOH B 681 HOH B 692 HOH B 699 SITE 1 AC7 8 ASP B 224 SER B 229 HIS B 230 GLY B 312 SITE 2 AC7 8 VAL B 313 HOH B 430 HOH B 659 ILE D 757 SITE 1 AC8 4 LYS C 770 MET C 771 ALA C 773 TRP C 775 CRYST1 53.260 108.720 131.850 90.00 90.00 90.00 P 21 21 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.018776 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009198 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007584 0.00000 ATOM 1 N GLY A 192 55.727 -0.467 9.371 1.00104.42 N ANISOU 1 N GLY A 192 13043 13926 12706 1216 -225 -1613 N ATOM 2 CA GLY A 192 56.316 -0.471 8.045 1.00106.07 C ANISOU 2 CA GLY A 192 13189 14244 12869 1156 -210 -1677 C ATOM 3 C GLY A 192 55.290 -0.359 6.931 1.00106.76 C ANISOU 3 C GLY A 192 13310 14274 12979 1081 -180 -1617 C ATOM 4 O GLY A 192 55.660 -0.189 5.774 1.00107.30 O ANISOU 4 O GLY A 192 13333 14425 13011 1012 -162 -1659 O ATOM 5 N ILE A 193 54.015 -0.509 7.297 1.00106.33 N ANISOU 5 N ILE A 193 13333 14088 12981 1096 -177 -1522 N ATOM 6 CA ILE A 193 52.821 -0.176 6.487 1.00103.80 C ANISOU 6 CA ILE A 193 13054 13687 12697 1028 -146 -1451 C ATOM 7 C ILE A 193 51.595 -1.023 6.824 1.00 99.41 C ANISOU 7 C ILE A 193 12571 13023 12178 1074 -158 -1369 C ATOM 8 O ILE A 193 51.706 -2.104 7.405 1.00102.67 O ANISOU 8 O ILE A 193 13007 13430 12572 1153 -192 -1373 O ATOM 9 CB ILE A 193 53.018 -0.143 4.934 1.00131.56 C ANISOU 9 CB ILE A 193 16533 17277 16176 948 -126 -1486 C ATOM 10 CG1 ILE A 193 53.785 -1.369 4.419 1.00131.45 C ANISOU 10 CG1 ILE A 193 16478 17361 16107 997 -158 -1550 C ATOM 11 CG2 ILE A 193 53.623 1.189 4.491 1.00132.10 C ANISOU 11 CG2 ILE A 193 16563 17407 16219 850 -95 -1528 C ATOM 12 CD1 ILE A 193 54.314 -1.190 3.008 1.00131.74 C ANISOU 12 CD1 ILE A 193 16458 17504 16093 916 -143 -1602 C ATOM 13 N ASP A 194 50.430 -0.511 6.436 1.00 89.07 N ANISOU 13 N ASP A 194 11300 11630 10912 1021 -130 -1297 N ATOM 14 CA ASP A 194 49.151 -1.077 6.840 1.00 76.68 C ANISOU 14 CA ASP A 194 9798 9959 9379 1050 -133 -1215 C ATOM 15 C ASP A 194 48.234 -1.286 5.638 1.00 70.21 C ANISOU 15 C ASP A 194 8995 9111 8572 998 -111 -1179 C ATOM 16 O ASP A 194 47.709 -0.324 5.075 1.00 65.58 O ANISOU 16 O ASP A 194 8410 8497 8011 934 -83 -1153 O ATOM 17 CB ASP A 194 48.484 -0.148 7.858 1.00 69.75 C ANISOU 17 CB ASP A 194 8953 9001 8548 1051 -123 -1154 C ATOM 18 CG ASP A 194 47.130 -0.648 8.313 1.00 63.71 C ANISOU 18 CG ASP A 194 8249 8144 7813 1072 -123 -1071 C ATOM 19 OD1 ASP A 194 46.727 -1.758 7.912 1.00 63.11 O ANISOU 19 OD1 ASP A 194 8197 8061 7722 1086 -129 -1061 O ATOM 20 OD2 ASP A 194 46.465 0.077 9.079 1.00 61.93 O ANISOU 20 OD2 ASP A 194 8050 7858 7622 1072 -116 -1017 O ATOM 21 N PRO A 195 48.037 -2.553 5.242 1.00 71.07 N ANISOU 21 N PRO A 195 9122 9224 8657 1028 -128 -1179 N ATOM 22 CA PRO A 195 47.180 -2.898 4.103 1.00 71.42 C ANISOU 22 CA PRO A 195 9183 9243 8710 983 -111 -1147 C ATOM 23 C PRO A 195 45.731 -2.480 4.333 1.00 68.45 C ANISOU 23 C PRO A 195 8853 8768 8388 960 -87 -1062 C ATOM 24 O PRO A 195 44.993 -2.247 3.369 1.00 71.21 O ANISOU 24 O PRO A 195 9207 9097 8755 908 -65 -1036 O ATOM 25 CB PRO A 195 47.261 -4.431 4.050 1.00 71.32 C ANISOU 25 CB PRO A 195 9199 9240 8659 1041 -141 -1160 C ATOM 26 CG PRO A 195 48.508 -4.781 4.786 1.00 72.63 C ANISOU 26 CG PRO A 195 9342 9470 8783 1108 -176 -1224 C ATOM 27 CD PRO A 195 48.646 -3.745 5.856 1.00 71.91 C ANISOU 27 CD PRO A 195 9243 9358 8723 1110 -167 -1212 C ATOM 28 N PHE A 196 45.336 -2.382 5.600 1.00 51.20 N ANISOU 28 N PHE A 196 6701 6528 6224 1001 -94 -1023 N ATOM 29 CA PHE A 196 43.928 -2.211 5.950 1.00 38.73 C ANISOU 29 CA PHE A 196 5165 4866 4686 992 -77 -944 C ATOM 30 C PHE A 196 43.433 -0.772 5.877 1.00 33.77 C ANISOU 30 C PHE A 196 4527 4206 4098 950 -56 -912 C ATOM 31 O PHE A 196 42.272 -0.499 6.174 1.00 31.00 O ANISOU 31 O PHE A 196 4204 3795 3779 947 -45 -850 O ATOM 32 CB PHE A 196 43.639 -2.831 7.317 1.00 34.98 C ANISOU 32 CB PHE A 196 4734 4351 4205 1051 -94 -916 C ATOM 33 CG PHE A 196 43.932 -4.302 7.370 1.00 38.63 C ANISOU 33 CG PHE A 196 5229 4827 4622 1095 -117 -940 C ATOM 34 CD1 PHE A 196 44.957 -4.795 8.165 1.00 33.68 C ANISOU 34 CD1 PHE A 196 4605 4233 3957 1156 -149 -985 C ATOM 35 CD2 PHE A 196 43.208 -5.190 6.582 1.00 36.19 C ANISOU 35 CD2 PHE A 196 4950 4498 4305 1078 -109 -922 C ATOM 36 CE1 PHE A 196 45.234 -6.150 8.199 1.00 38.52 C ANISOU 36 CE1 PHE A 196 5259 4855 4522 1205 -176 -1009 C ATOM 37 CE2 PHE A 196 43.483 -6.546 6.608 1.00 38.23 C ANISOU 37 CE2 PHE A 196 5250 4762 4515 1122 -133 -944 C ATOM 38 CZ PHE A 196 44.498 -7.028 7.416 1.00 39.06 C ANISOU 38 CZ PHE A 196 5365 4897 4579 1188 -168 -988 C ATOM 39 N THR A 197 44.309 0.139 5.466 1.00 27.69 N ANISOU 39 N THR A 197 3720 3480 3320 918 -51 -958 N ATOM 40 CA THR A 197 43.904 1.519 5.238 1.00 26.96 C ANISOU 40 CA THR A 197 3633 3357 3255 875 -33 -935 C ATOM 41 C THR A 197 43.208 1.673 3.881 1.00 28.44 C ANISOU 41 C THR A 197 3825 3533 3448 817 -13 -922 C ATOM 42 O THR A 197 42.693 2.743 3.566 1.00 25.71 O ANISOU 42 O THR A 197 3495 3154 3121 779 -5 -893 O ATOM 43 CB THR A 197 45.108 2.471 5.270 1.00 27.92 C ANISOU 43 CB THR A 197 3726 3529 3355 850 -33 -995 C ATOM 44 OG1 THR A 197 46.067 2.049 4.292 1.00 34.25 O ANISOU 44 OG1 THR A 197 4488 4417 4110 815 -30 -1066 O ATOM 45 CG2 THR A 197 45.757 2.487 6.659 1.00 28.20 C ANISOU 45 CG2 THR A 197 3756 3570 3388 908 -53 -1006 C ATOM 46 N LYS A 198 43.195 0.605 3.085 1.00 29.99 N ANISOU 46 N LYS A 198 4012 3759 3625 810 -12 -938 N ATOM 47 CA LYS A 198 42.705 0.676 1.707 1.00 32.23 C ANISOU 47 CA LYS A 198 4288 4049 3906 744 -2 -922 C ATOM 48 C LYS A 198 41.249 0.256 1.524 1.00 35.49 C ANISOU 48 C LYS A 198 4731 4402 4353 747 5 -852 C ATOM 49 O LYS A 198 40.692 -0.493 2.332 1.00 30.80 O ANISOU 49 O LYS A 198 4164 3768 3770 804 8 -834 O ATOM 50 CB LYS A 198 43.586 -0.162 0.780 1.00 34.52 C ANISOU 50 CB LYS A 198 4546 4420 4151 724 -9 -980 C ATOM 51 CG LYS A 198 44.998 0.365 0.614 1.00 42.94 C ANISOU 51 CG LYS A 198 5569 5571 5175 693 -17 -1048 C ATOM 52 CD LYS A 198 45.802 -0.564 -0.273 1.00 54.23 C ANISOU 52 CD LYS A 198 6963 7087 6553 686 -27 -1109 C ATOM 53 CE LYS A 198 47.290 -0.435 -0.011 1.00 62.67 C ANISOU 53 CE LYS A 198 7992 8252 7569 698 -34 -1201 C ATOM 54 NZ LYS A 198 48.027 -1.635 -0.499 1.00 65.25 N ANISOU 54 NZ LYS A 198 8283 8659 7848 730 -57 -1250 N ATOM 55 N PHE A 199 40.649 0.751 0.443 1.00 35.96 N ANISOU 55 N PHE A 199 4778 4464 4423 673 2 -804 N ATOM 56 CA PHE A 199 39.302 0.362 0.043 1.00 29.48 C ANISOU 56 CA PHE A 199 3973 3603 3627 664 9 -743 C ATOM 57 C PHE A 199 39.218 -1.148 -0.063 1.00 24.31 C ANISOU 57 C PHE A 199 3328 2953 2955 697 14 -764 C ATOM 58 O PHE A 199 40.123 -1.795 -0.593 1.00 26.40 O ANISOU 58 O PHE A 199 3577 3269 3186 693 7 -815 O ATOM 59 CB PHE A 199 38.945 1.001 -1.306 1.00 29.35 C ANISOU 59 CB PHE A 199 3938 3603 3612 580 2 -707 C ATOM 60 CG PHE A 199 37.735 0.392 -1.976 1.00 25.23 C ANISOU 60 CG PHE A 199 3421 3061 3106 565 9 -658 C ATOM 61 CD1 PHE A 199 36.456 0.720 -1.561 1.00 28.51 C ANISOU 61 CD1 PHE A 199 3856 3428 3547 583 15 -603 C ATOM 62 CD2 PHE A 199 37.883 -0.505 -3.024 1.00 24.38 C ANISOU 62 CD2 PHE A 199 3295 2986 2980 534 9 -670 C ATOM 63 CE1 PHE A 199 35.349 0.166 -2.175 1.00 33.18 C ANISOU 63 CE1 PHE A 199 4447 4011 4148 565 22 -563 C ATOM 64 CE2 PHE A 199 36.779 -1.064 -3.645 1.00 28.16 C ANISOU 64 CE2 PHE A 199 3779 3449 3473 517 16 -626 C ATOM 65 CZ PHE A 199 35.511 -0.730 -3.222 1.00 30.39 C ANISOU 65 CZ PHE A 199 4078 3687 3781 530 24 -574 C ATOM 66 N PHE A 200 38.131 -1.714 0.446 1.00 27.64 N ANISOU 66 N PHE A 200 3781 3325 3394 730 25 -726 N ATOM 67 CA PHE A 200 37.931 -3.153 0.346 1.00 31.03 C ANISOU 67 CA PHE A 200 4237 3750 3803 753 29 -739 C ATOM 68 C PHE A 200 36.602 -3.546 -0.296 1.00 27.74 C ANISOU 68 C PHE A 200 3827 3313 3401 714 38 -679 C ATOM 69 O PHE A 200 35.548 -2.988 0.016 1.00 33.73 O ANISOU 69 O PHE A 200 4588 4042 4188 708 47 -628 O ATOM 70 CB PHE A 200 38.043 -3.829 1.711 1.00 28.74 C ANISOU 70 CB PHE A 200 3985 3433 3502 821 25 -750 C ATOM 71 CG PHE A 200 37.573 -5.251 1.703 1.00 26.21 C ANISOU 71 CG PHE A 200 3708 3095 3156 833 24 -742 C ATOM 72 CD1 PHE A 200 38.307 -6.229 1.045 1.00 26.78 C ANISOU 72 CD1 PHE A 200 3788 3202 3186 836 7 -783 C ATOM 73 CD2 PHE A 200 36.382 -5.607 2.319 1.00 29.63 C ANISOU 73 CD2 PHE A 200 4177 3480 3601 841 40 -697 C ATOM 74 CE1 PHE A 200 37.875 -7.543 1.017 1.00 29.07 C ANISOU 74 CE1 PHE A 200 4132 3469 3447 848 3 -777 C ATOM 75 CE2 PHE A 200 35.941 -6.923 2.295 1.00 31.16 C ANISOU 75 CE2 PHE A 200 4422 3653 3765 845 41 -694 C ATOM 76 CZ PHE A 200 36.688 -7.892 1.644 1.00 27.28 C ANISOU 76 CZ PHE A 200 3948 3186 3231 849 22 -732 C ATOM 77 N TYR A 201 36.671 -4.523 -1.190 1.00 24.36 N ANISOU 77 N TYR A 201 3402 2906 2949 691 33 -689 N ATOM 78 CA TYR A 201 35.483 -5.108 -1.796 1.00 28.62 C ANISOU 78 CA TYR A 201 3951 3429 3495 656 42 -639 C ATOM 79 C TYR A 201 35.860 -6.386 -2.523 1.00 25.34 C ANISOU 79 C TYR A 201 3555 3032 3042 651 31 -666 C ATOM 80 O TYR A 201 36.817 -6.420 -3.295 1.00 26.49 O ANISOU 80 O TYR A 201 3675 3224 3168 638 15 -703 O ATOM 81 CB TYR A 201 34.803 -4.146 -2.778 1.00 33.90 C ANISOU 81 CB TYR A 201 4580 4111 4192 592 44 -591 C ATOM 82 CG TYR A 201 33.603 -4.774 -3.453 1.00 36.33 C ANISOU 82 CG TYR A 201 4890 4410 4502 556 53 -545 C ATOM 83 CD1 TYR A 201 32.331 -4.637 -2.914 1.00 38.87 C ANISOU 83 CD1 TYR A 201 5222 4707 4841 559 68 -501 C ATOM 84 CD2 TYR A 201 33.744 -5.531 -4.611 1.00 31.25 C ANISOU 84 CD2 TYR A 201 4241 3790 3842 520 46 -550 C ATOM 85 CE1 TYR A 201 31.232 -5.223 -3.517 1.00 40.74 C ANISOU 85 CE1 TYR A 201 5458 4945 5075 522 79 -464 C ATOM 86 CE2 TYR A 201 32.648 -6.122 -5.224 1.00 30.41 C ANISOU 86 CE2 TYR A 201 4139 3677 3738 485 55 -509 C ATOM 87 CZ TYR A 201 31.395 -5.964 -4.670 1.00 39.86 C ANISOU 87 CZ TYR A 201 5342 4852 4949 483 73 -467 C ATOM 88 OH TYR A 201 30.294 -6.540 -5.260 1.00 38.50 O ANISOU 88 OH TYR A 201 5171 4684 4775 444 83 -431 O ATOM 89 N SER A 202 35.095 -7.437 -2.274 1.00 26.35 N ANISOU 89 N SER A 202 3731 3127 3154 659 38 -648 N ATOM 90 CA SER A 202 35.319 -8.708 -2.933 1.00 25.60 C ANISOU 90 CA SER A 202 3669 3041 3019 656 24 -668 C ATOM 91 C SER A 202 34.010 -9.449 -3.136 1.00 27.77 C ANISOU 91 C SER A 202 3977 3285 3291 620 37 -617 C ATOM 92 O SER A 202 33.256 -9.667 -2.189 1.00 35.15 O ANISOU 92 O SER A 202 4948 4181 4226 633 53 -596 O ATOM 93 CB SER A 202 36.280 -9.568 -2.111 1.00 33.59 C ANISOU 93 CB SER A 202 4737 4042 3982 730 9 -732 C ATOM 94 OG SER A 202 36.351 -10.887 -2.626 1.00 44.97 O ANISOU 94 OG SER A 202 6231 5480 5375 735 -9 -748 O ATOM 95 N ASP A 203 33.738 -9.827 -4.379 1.00 32.59 N ANISOU 95 N ASP A 203 4571 3916 3897 571 31 -597 N ATOM 96 CA ASP A 203 32.670 -10.775 -4.665 1.00 31.75 C ANISOU 96 CA ASP A 203 4503 3786 3774 535 39 -559 C ATOM 97 C ASP A 203 33.191 -11.826 -5.643 1.00 38.12 C ANISOU 97 C ASP A 203 5337 4607 4540 529 13 -581 C ATOM 98 O ASP A 203 34.396 -11.893 -5.902 1.00 37.74 O ANISOU 98 O ASP A 203 5281 4588 4471 565 -10 -632 O ATOM 99 CB ASP A 203 31.393 -10.077 -5.164 1.00 31.39 C ANISOU 99 CB ASP A 203 4409 3749 3770 476 61 -498 C ATOM 100 CG ASP A 203 31.559 -9.424 -6.535 1.00 33.14 C ANISOU 100 CG ASP A 203 4566 4009 4016 434 53 -487 C ATOM 101 OD1 ASP A 203 32.578 -9.666 -7.223 1.00 27.93 O ANISOU 101 OD1 ASP A 203 3899 3374 3340 441 32 -521 O ATOM 102 OD2 ASP A 203 30.650 -8.661 -6.925 1.00 33.06 O ANISOU 102 OD2 ASP A 203 4515 4009 4039 397 67 -445 O ATOM 103 N GLN A 204 32.299 -12.647 -6.180 1.00 43.96 N ANISOU 103 N GLN A 204 6107 5332 5265 486 17 -546 N ATOM 104 CA GLN A 204 32.730 -13.772 -7.005 1.00 52.17 C ANISOU 104 CA GLN A 204 7188 6377 6258 487 -11 -565 C ATOM 105 C GLN A 204 33.327 -13.339 -8.352 1.00 48.26 C ANISOU 105 C GLN A 204 6624 5934 5780 467 -27 -572 C ATOM 106 O GLN A 204 34.003 -14.125 -9.020 1.00 47.50 O ANISOU 106 O GLN A 204 6550 5854 5643 484 -57 -601 O ATOM 107 CB GLN A 204 31.585 -14.766 -7.201 1.00 60.70 C ANISOU 107 CB GLN A 204 8325 7424 7313 439 -4 -523 C ATOM 108 CG GLN A 204 30.436 -14.240 -8.039 1.00 73.16 C ANISOU 108 CG GLN A 204 9839 9023 8936 366 20 -464 C ATOM 109 CD GLN A 204 29.325 -15.260 -8.189 1.00 84.59 C ANISOU 109 CD GLN A 204 11341 10446 10352 314 29 -427 C ATOM 110 OE1 GLN A 204 29.129 -15.828 -9.265 1.00 88.89 O ANISOU 110 OE1 GLN A 204 11889 11000 10886 279 17 -411 O ATOM 111 NE2 GLN A 204 28.602 -15.514 -7.102 1.00 87.05 N ANISOU 111 NE2 GLN A 204 11700 10729 10647 305 50 -414 N ATOM 112 N ASN A 205 33.094 -12.085 -8.734 1.00 42.11 N ANISOU 112 N ASN A 205 5764 5180 5055 433 -10 -547 N ATOM 113 CA ASN A 205 33.586 -11.568 -10.011 1.00 42.22 C ANISOU 113 CA ASN A 205 5713 5240 5086 404 -21 -550 C ATOM 114 C ASN A 205 34.890 -10.786 -9.904 1.00 42.28 C ANISOU 114 C ASN A 205 5681 5290 5094 432 -34 -600 C ATOM 115 O ASN A 205 35.740 -10.871 -10.788 1.00 45.42 O ANISOU 115 O ASN A 205 6048 5734 5473 429 -55 -630 O ATOM 116 CB ASN A 205 32.539 -10.671 -10.667 1.00 42.77 C ANISOU 116 CB ASN A 205 5728 5313 5207 343 2 -495 C ATOM 117 CG ASN A 205 31.229 -11.384 -10.908 1.00 44.02 C ANISOU 117 CG ASN A 205 5914 5448 5365 306 16 -447 C ATOM 118 OD1 ASN A 205 31.204 -12.569 -11.248 1.00 44.20 O ANISOU 118 OD1 ASN A 205 5983 5460 5351 304 1 -450 O ATOM 119 ND2 ASN A 205 30.127 -10.661 -10.743 1.00 40.28 N ANISOU 119 ND2 ASN A 205 5411 4968 4925 277 41 -406 N ATOM 120 N VAL A 206 35.040 -10.020 -8.828 1.00 34.59 N ANISOU 120 N VAL A 206 4703 4303 4136 458 -20 -611 N ATOM 121 CA VAL A 206 36.138 -9.065 -8.733 1.00 32.27 C ANISOU 121 CA VAL A 206 4363 4050 3846 469 -27 -651 C ATOM 122 C VAL A 206 36.581 -8.847 -7.280 1.00 32.56 C ANISOU 122 C VAL A 206 4427 4068 3876 527 -22 -684 C ATOM 123 O VAL A 206 35.803 -9.057 -6.349 1.00 31.36 O ANISOU 123 O VAL A 206 4316 3866 3734 547 -7 -660 O ATOM 124 CB VAL A 206 35.742 -7.725 -9.396 1.00 27.81 C ANISOU 124 CB VAL A 206 3741 3498 3329 409 -14 -613 C ATOM 125 CG1 VAL A 206 34.544 -7.105 -8.684 1.00 30.06 C ANISOU 125 CG1 VAL A 206 4035 3735 3650 402 10 -563 C ATOM 126 CG2 VAL A 206 36.922 -6.768 -9.438 1.00 26.65 C ANISOU 126 CG2 VAL A 206 3553 3396 3177 404 -22 -654 C ATOM 127 N ASP A 207 37.834 -8.435 -7.092 1.00 27.56 N ANISOU 127 N ASP A 207 3768 3478 3224 553 -35 -740 N ATOM 128 CA ASP A 207 38.423 -8.352 -5.755 1.00 30.73 C ANISOU 128 CA ASP A 207 4196 3868 3612 617 -34 -783 C ATOM 129 C ASP A 207 39.492 -7.271 -5.665 1.00 27.68 C ANISOU 129 C ASP A 207 3757 3533 3228 613 -37 -823 C ATOM 130 O ASP A 207 40.495 -7.320 -6.376 1.00 29.74 O ANISOU 130 O ASP A 207 3982 3862 3457 604 -55 -869 O ATOM 131 CB ASP A 207 39.025 -9.703 -5.356 1.00 29.94 C ANISOU 131 CB ASP A 207 4155 3768 3452 687 -56 -837 C ATOM 132 CG ASP A 207 39.529 -9.727 -3.913 1.00 42.35 C ANISOU 132 CG ASP A 207 5765 5318 5009 761 -54 -881 C ATOM 133 OD1 ASP A 207 39.607 -8.656 -3.266 1.00 38.64 O ANISOU 133 OD1 ASP A 207 5264 4843 4573 759 -38 -876 O ATOM 134 OD2 ASP A 207 39.847 -10.833 -3.422 1.00 46.35 O ANISOU 134 OD2 ASP A 207 6331 5812 5468 819 -77 -908 O ATOM 135 N SER A 208 39.278 -6.314 -4.767 1.00 24.54 N ANISOU 135 N SER A 208 3355 3105 2862 619 -21 -807 N ATOM 136 CA SER A 208 40.201 -5.199 -4.570 1.00 28.29 C ANISOU 136 CA SER A 208 3789 3621 3338 607 -23 -839 C ATOM 137 C SER A 208 41.604 -5.624 -4.108 1.00 32.31 C ANISOU 137 C SER A 208 4294 4185 3797 664 -39 -926 C ATOM 138 O SER A 208 42.555 -4.846 -4.208 1.00 32.97 O ANISOU 138 O SER A 208 4334 4327 3867 643 -43 -964 O ATOM 139 CB SER A 208 39.608 -4.188 -3.576 1.00 28.84 C ANISOU 139 CB SER A 208 3869 3638 3449 614 -7 -802 C ATOM 140 OG SER A 208 39.394 -4.775 -2.296 1.00 28.58 O ANISOU 140 OG SER A 208 3885 3560 3415 687 0 -813 O ATOM 141 N ARG A 209 41.736 -6.850 -3.609 1.00 24.37 N ANISOU 141 N ARG A 209 3338 3165 2756 735 -49 -959 N ATOM 142 CA ARG A 209 43.007 -7.285 -3.027 1.00 30.73 C ANISOU 142 CA ARG A 209 4138 4024 3514 798 -76 -1029 C ATOM 143 C ARG A 209 43.954 -7.883 -4.066 1.00 34.28 C ANISOU 143 C ARG A 209 4555 4562 3909 797 -103 -1084 C ATOM 144 O ARG A 209 45.080 -8.274 -3.739 1.00 28.08 O ANISOU 144 O ARG A 209 3750 3840 3081 848 -134 -1138 O ATOM 145 CB ARG A 209 42.766 -8.271 -1.877 1.00 30.60 C ANISOU 145 CB ARG A 209 4184 3956 3488 869 -95 -1010 C ATOM 146 CG ARG A 209 42.136 -7.624 -0.644 1.00 32.69 C ANISOU 146 CG ARG A 209 4468 4156 3796 879 -76 -967 C ATOM 147 CD ARG A 209 41.500 -8.672 0.259 1.00 36.51 C ANISOU 147 CD ARG A 209 5027 4576 4268 925 -85 -935 C ATOM 148 NE ARG A 209 40.554 -9.513 -0.475 1.00 35.93 N ANISOU 148 NE ARG A 209 4998 4466 4188 900 -76 -906 N ATOM 149 CZ ARG A 209 39.949 -10.579 0.041 1.00 34.64 C ANISOU 149 CZ ARG A 209 4912 4250 4001 926 -82 -883 C ATOM 150 NH1 ARG A 209 39.102 -11.287 -0.692 1.00 31.20 N ANISOU 150 NH1 ARG A 209 4514 3784 3556 894 -72 -861 N ATOM 151 NH2 ARG A 209 40.193 -10.942 1.293 1.00 35.75 N ANISOU 151 NH2 ARG A 209 5094 4366 4122 980 -99 -885 N ATOM 152 N ASP A 210 43.495 -7.944 -5.315 1.00 27.79 N ANISOU 152 N ASP A 210 3721 3749 3090 739 -96 -1062 N ATOM 153 CA ASP A 210 44.297 -8.485 -6.410 1.00 30.84 C ANISOU 153 CA ASP A 210 4073 4220 3424 732 -123 -1108 C ATOM 154 C ASP A 210 44.390 -7.470 -7.553 1.00 33.64 C ANISOU 154 C ASP A 210 4354 4625 3802 632 -115 -1081 C ATOM 155 O ASP A 210 43.690 -7.598 -8.563 1.00 28.97 O ANISOU 155 O ASP A 210 3757 4019 3234 580 -114 -1029 O ATOM 156 CB ASP A 210 43.682 -9.800 -6.900 1.00 34.33 C ANISOU 156 CB ASP A 210 4572 4627 3846 757 -140 -1087 C ATOM 157 CG ASP A 210 44.518 -10.481 -7.976 1.00 45.34 C ANISOU 157 CG ASP A 210 5939 6109 5180 766 -174 -1137 C ATOM 158 OD1 ASP A 210 45.581 -9.942 -8.364 1.00 43.49 O ANISOU 158 OD1 ASP A 210 5634 5972 4918 750 -183 -1190 O ATOM 159 OD2 ASP A 210 44.101 -11.566 -8.437 1.00 51.83 O ANISOU 159 OD2 ASP A 210 6809 6906 5980 787 -194 -1120 O ATOM 160 N PRO A 211 45.264 -6.462 -7.392 1.00 37.04 N ANISOU 160 N PRO A 211 4731 5116 4224 603 -110 -1119 N ATOM 161 CA PRO A 211 45.419 -5.317 -8.302 1.00 35.56 C ANISOU 161 CA PRO A 211 4486 4972 4054 501 -101 -1096 C ATOM 162 C PRO A 211 45.685 -5.709 -9.754 1.00 32.97 C ANISOU 162 C PRO A 211 4118 4711 3699 456 -118 -1103 C ATOM 163 O PRO A 211 45.136 -5.078 -10.663 1.00 28.65 O ANISOU 163 O PRO A 211 3552 4148 3185 374 -108 -1048 O ATOM 164 CB PRO A 211 46.645 -4.587 -7.743 1.00 37.60 C ANISOU 164 CB PRO A 211 4704 5306 4277 500 -102 -1165 C ATOM 165 CG PRO A 211 46.711 -4.993 -6.315 1.00 39.90 C ANISOU 165 CG PRO A 211 5040 5554 4565 596 -100 -1194 C ATOM 166 CD PRO A 211 46.221 -6.407 -6.275 1.00 40.31 C ANISOU 166 CD PRO A 211 5147 5565 4604 670 -114 -1192 C ATOM 167 N VAL A 212 46.522 -6.719 -9.967 1.00 28.70 N ANISOU 167 N VAL A 212 3566 4243 3094 514 -145 -1172 N ATOM 168 CA VAL A 212 46.911 -7.106 -11.318 1.00 29.19 C ANISOU 168 CA VAL A 212 3585 4383 3122 479 -165 -1187 C ATOM 169 C VAL A 212 45.755 -7.754 -12.053 1.00 27.72 C ANISOU 169 C VAL A 212 3437 4125 2973 468 -167 -1115 C ATOM 170 O VAL A 212 45.493 -7.431 -13.209 1.00 24.13 O ANISOU 170 O VAL A 212 2948 3685 2536 395 -164 -1079 O ATOM 171 CB VAL A 212 48.094 -8.085 -11.314 1.00 38.79 C ANISOU 171 CB VAL A 212 4786 5703 4252 559 -201 -1284 C ATOM 172 CG1 VAL A 212 48.657 -8.229 -12.729 1.00 31.46 C ANISOU 172 CG1 VAL A 212 3794 4876 3284 512 -221 -1306 C ATOM 173 CG2 VAL A 212 49.165 -7.614 -10.342 1.00 42.74 C ANISOU 173 CG2 VAL A 212 5258 6268 4712 592 -199 -1362 C ATOM 174 N GLN A 213 45.070 -8.677 -11.386 1.00 27.40 N ANISOU 174 N GLN A 213 3468 4005 2939 537 -170 -1097 N ATOM 175 CA GLN A 213 43.888 -9.294 -11.973 1.00 32.38 C ANISOU 175 CA GLN A 213 4138 4562 3602 522 -168 -1027 C ATOM 176 C GLN A 213 42.792 -8.250 -12.223 1.00 29.35 C ANISOU 176 C GLN A 213 3744 4114 3295 440 -135 -943 C ATOM 177 O GLN A 213 42.085 -8.305 -13.237 1.00 21.97 O ANISOU 177 O GLN A 213 2800 3160 2385 390 -132 -892 O ATOM 178 CB GLN A 213 43.359 -10.417 -11.082 1.00 29.46 C ANISOU 178 CB GLN A 213 3855 4119 3218 602 -176 -1024 C ATOM 179 CG GLN A 213 42.174 -11.164 -11.679 1.00 43.96 C ANISOU 179 CG GLN A 213 5737 5889 5078 582 -175 -957 C ATOM 180 CD GLN A 213 42.529 -11.896 -12.964 1.00 60.26 C ANISOU 180 CD GLN A 213 7782 8008 7104 578 -207 -972 C ATOM 181 OE1 GLN A 213 43.689 -12.249 -13.192 1.00 61.80 O ANISOU 181 OE1 GLN A 213 7954 8290 7237 620 -238 -1044 O ATOM 182 NE2 GLN A 213 41.528 -12.130 -13.811 1.00 63.74 N ANISOU 182 NE2 GLN A 213 8232 8407 7580 529 -200 -905 N ATOM 183 N LEU A 214 42.660 -7.301 -11.299 1.00 20.34 N ANISOU 183 N LEU A 214 2605 2939 2183 431 -113 -933 N ATOM 184 CA LEU A 214 41.647 -6.259 -11.418 1.00 23.71 C ANISOU 184 CA LEU A 214 3030 3307 2673 367 -87 -860 C ATOM 185 C LEU A 214 41.864 -5.415 -12.676 1.00 24.31 C ANISOU 185 C LEU A 214 3054 3428 2755 279 -87 -847 C ATOM 186 O LEU A 214 40.917 -5.120 -13.399 1.00 19.90 O ANISOU 186 O LEU A 214 2497 2828 2235 232 -77 -787 O ATOM 187 CB LEU A 214 41.620 -5.370 -10.170 1.00 19.10 C ANISOU 187 CB LEU A 214 2461 2687 2110 382 -70 -859 C ATOM 188 CG LEU A 214 40.789 -4.082 -10.273 1.00 15.97 C ANISOU 188 CG LEU A 214 2061 2242 1764 320 -51 -797 C ATOM 189 CD1 LEU A 214 39.294 -4.363 -10.451 1.00 13.70 C ANISOU 189 CD1 LEU A 214 1805 1882 1518 316 -39 -726 C ATOM 190 CD2 LEU A 214 41.043 -3.147 -9.093 1.00 10.94 C ANISOU 190 CD2 LEU A 214 1435 1586 1137 337 -42 -808 C ATOM 191 N ASN A 215 43.109 -5.035 -12.937 1.00 21.80 N ANISOU 191 N ASN A 215 2689 3198 2395 257 -98 -906 N ATOM 192 CA ASN A 215 43.407 -4.205 -14.095 1.00 23.14 C ANISOU 192 CA ASN A 215 2814 3415 2563 166 -98 -898 C ATOM 193 C ASN A 215 43.057 -4.910 -15.399 1.00 25.07 C ANISOU 193 C ASN A 215 3044 3672 2808 146 -109 -875 C ATOM 194 O ASN A 215 42.590 -4.283 -16.350 1.00 28.63 O ANISOU 194 O ASN A 215 3483 4110 3286 75 -102 -832 O ATOM 195 CB ASN A 215 44.875 -3.768 -14.097 1.00 29.87 C ANISOU 195 CB ASN A 215 3616 4375 3359 143 -107 -973 C ATOM 196 CG ASN A 215 45.192 -2.795 -15.224 1.00 34.54 C ANISOU 196 CG ASN A 215 4167 5012 3943 35 -105 -964 C ATOM 197 OD1 ASN A 215 44.627 -1.700 -15.293 1.00 35.61 O ANISOU 197 OD1 ASN A 215 4325 5093 4114 -27 -90 -915 O ATOM 198 ND2 ASN A 215 46.102 -3.190 -16.112 1.00 28.22 N ANISOU 198 ND2 ASN A 215 3313 4316 3092 13 -122 -1013 N ATOM 199 N LEU A 216 43.279 -6.219 -15.446 1.00 21.19 N ANISOU 199 N LEU A 216 2562 3205 2286 213 -129 -905 N ATOM 200 CA LEU A 216 42.924 -6.982 -16.632 1.00 21.00 C ANISOU 200 CA LEU A 216 2531 3188 2261 202 -144 -882 C ATOM 201 C LEU A 216 41.413 -6.958 -16.820 1.00 25.21 C ANISOU 201 C LEU A 216 3103 3622 2856 182 -124 -799 C ATOM 202 O LEU A 216 40.915 -6.766 -17.936 1.00 21.60 O ANISOU 202 O LEU A 216 2628 3158 2423 129 -122 -759 O ATOM 203 CB LEU A 216 43.417 -8.424 -16.520 1.00 32.11 C ANISOU 203 CB LEU A 216 3957 4631 3614 287 -175 -930 C ATOM 204 CG LEU A 216 44.936 -8.611 -16.491 1.00 40.43 C ANISOU 204 CG LEU A 216 4966 5802 4593 319 -200 -1022 C ATOM 205 CD1 LEU A 216 45.287 -10.058 -16.798 1.00 44.08 C ANISOU 205 CD1 LEU A 216 5450 6301 4998 398 -240 -1061 C ATOM 206 CD2 LEU A 216 45.609 -7.669 -17.483 1.00 37.24 C ANISOU 206 CD2 LEU A 216 4488 5484 4179 230 -197 -1037 C ATOM 207 N LEU A 217 40.684 -7.144 -15.721 1.00 21.60 N ANISOU 207 N LEU A 217 2694 3090 2421 226 -111 -775 N ATOM 208 CA LEU A 217 39.229 -7.135 -15.772 1.00 22.25 C ANISOU 208 CA LEU A 217 2810 3090 2555 210 -92 -703 C ATOM 209 C LEU A 217 38.736 -5.768 -16.224 1.00 18.83 C ANISOU 209 C LEU A 217 2356 2638 2163 139 -73 -661 C ATOM 210 O LEU A 217 37.843 -5.672 -17.064 1.00 13.07 O ANISOU 210 O LEU A 217 1624 1878 1463 103 -66 -613 O ATOM 211 CB LEU A 217 38.633 -7.502 -14.416 1.00 19.52 C ANISOU 211 CB LEU A 217 2518 2682 2218 266 -80 -692 C ATOM 212 CG LEU A 217 38.923 -8.925 -13.924 1.00 25.53 C ANISOU 212 CG LEU A 217 3323 3442 2935 338 -100 -727 C ATOM 213 CD1 LEU A 217 38.420 -9.089 -12.500 1.00 20.05 C ANISOU 213 CD1 LEU A 217 2683 2688 2248 384 -85 -719 C ATOM 214 CD2 LEU A 217 38.308 -9.984 -14.841 1.00 19.92 C ANISOU 214 CD2 LEU A 217 2634 2718 2218 332 -112 -697 C ATOM 215 N TYR A 218 39.335 -4.718 -15.671 1.00 17.46 N ANISOU 215 N TYR A 218 2170 2478 1984 122 -68 -683 N ATOM 216 CA TYR A 218 38.964 -3.353 -16.028 1.00 18.34 C ANISOU 216 CA TYR A 218 2277 2568 2122 57 -56 -649 C ATOM 217 C TYR A 218 39.194 -3.097 -17.512 1.00 18.23 C ANISOU 217 C TYR A 218 2231 2593 2103 -11 -64 -644 C ATOM 218 O TYR A 218 38.299 -2.631 -18.212 1.00 17.16 O ANISOU 218 O TYR A 218 2105 2416 1998 -48 -56 -596 O ATOM 219 CB TYR A 218 39.753 -2.334 -15.199 1.00 12.05 C ANISOU 219 CB TYR A 218 1481 1788 1310 46 -54 -681 C ATOM 220 CG TYR A 218 39.634 -0.910 -15.714 1.00 11.39 C ANISOU 220 CG TYR A 218 1402 1691 1236 -30 -50 -656 C ATOM 221 CD1 TYR A 218 38.420 -0.230 -15.660 1.00 13.28 C ANISOU 221 CD1 TYR A 218 1678 1857 1512 -37 -41 -598 C ATOM 222 CD2 TYR A 218 40.727 -0.245 -16.242 1.00 10.47 C ANISOU 222 CD2 TYR A 218 1257 1638 1082 -95 -58 -693 C ATOM 223 CE1 TYR A 218 38.299 1.064 -16.126 1.00 10.76 C ANISOU 223 CE1 TYR A 218 1377 1518 1192 -99 -44 -578 C ATOM 224 CE2 TYR A 218 40.618 1.067 -16.715 1.00 12.73 C ANISOU 224 CE2 TYR A 218 1564 1905 1369 -171 -57 -670 C ATOM 225 CZ TYR A 218 39.397 1.713 -16.653 1.00 14.39 C ANISOU 225 CZ TYR A 218 1821 2032 1615 -169 -52 -612 C ATOM 226 OH TYR A 218 39.264 3.013 -17.104 1.00 11.95 O ANISOU 226 OH TYR A 218 1547 1695 1297 -236 -56 -590 O ATOM 227 N VAL A 219 40.395 -3.410 -17.991 1.00 15.96 N ANISOU 227 N VAL A 219 1904 2388 1772 -24 -80 -697 N ATOM 228 CA VAL A 219 40.723 -3.165 -19.389 1.00 16.47 C ANISOU 228 CA VAL A 219 1933 2499 1825 -91 -87 -697 C ATOM 229 C VAL A 219 39.736 -3.860 -20.331 1.00 15.71 C ANISOU 229 C VAL A 219 1842 2366 1760 -87 -88 -650 C ATOM 230 O VAL A 219 39.283 -3.273 -21.313 1.00 14.63 O ANISOU 230 O VAL A 219 1702 2213 1644 -144 -84 -616 O ATOM 231 CB VAL A 219 42.182 -3.571 -19.719 1.00 18.50 C ANISOU 231 CB VAL A 219 2139 2867 2022 -95 -107 -769 C ATOM 232 CG1 VAL A 219 42.395 -3.638 -21.210 1.00 21.51 C ANISOU 232 CG1 VAL A 219 2483 3297 2394 -151 -117 -766 C ATOM 233 CG2 VAL A 219 43.167 -2.586 -19.096 1.00 19.38 C ANISOU 233 CG2 VAL A 219 2236 3026 2101 -131 -103 -813 C ATOM 234 N GLN A 220 39.393 -5.105 -20.025 1.00 13.02 N ANISOU 234 N GLN A 220 1517 2011 1420 -22 -95 -649 N ATOM 235 CA GLN A 220 38.498 -5.861 -20.889 1.00 14.34 C ANISOU 235 CA GLN A 220 1691 2148 1610 -19 -97 -607 C ATOM 236 C GLN A 220 37.116 -5.230 -20.921 1.00 13.08 C ANISOU 236 C GLN A 220 1557 1911 1502 -41 -74 -544 C ATOM 237 O GLN A 220 36.537 -5.030 -21.995 1.00 12.28 O ANISOU 237 O GLN A 220 1446 1795 1423 -80 -72 -510 O ATOM 238 CB GLN A 220 38.404 -7.329 -20.463 1.00 13.89 C ANISOU 238 CB GLN A 220 1660 2085 1534 53 -111 -618 C ATOM 239 CG GLN A 220 37.438 -8.147 -21.335 1.00 16.76 C ANISOU 239 CG GLN A 220 2035 2415 1919 51 -113 -572 C ATOM 240 CD GLN A 220 37.980 -8.375 -22.733 1.00 29.29 C ANISOU 240 CD GLN A 220 3581 4058 3491 22 -133 -583 C ATOM 241 OE1 GLN A 220 38.909 -9.160 -22.927 1.00 34.83 O ANISOU 241 OE1 GLN A 220 4269 4819 4145 56 -161 -629 O ATOM 242 NE2 GLN A 220 37.401 -7.694 -23.719 1.00 30.68 N ANISOU 242 NE2 GLN A 220 3737 4217 3704 -36 -121 -544 N ATOM 243 N ALA A 221 36.603 -4.894 -19.743 1.00 14.42 N ANISOU 243 N ALA A 221 1759 2034 1687 -13 -60 -531 N ATOM 244 CA ALA A 221 35.259 -4.327 -19.627 1.00 17.11 C ANISOU 244 CA ALA A 221 2123 2309 2067 -22 -41 -478 C ATOM 245 C ALA A 221 35.135 -2.947 -20.270 1.00 11.66 C ANISOU 245 C ALA A 221 1430 1610 1389 -79 -38 -461 C ATOM 246 O ALA A 221 34.143 -2.658 -20.936 1.00 9.16 O ANISOU 246 O ALA A 221 1121 1261 1099 -97 -32 -421 O ATOM 247 CB ALA A 221 34.834 -4.262 -18.165 1.00 9.18 C ANISOU 247 CB ALA A 221 1151 1267 1069 25 -30 -473 C ATOM 248 N ARG A 222 36.138 -2.104 -20.039 1.00 9.48 N ANISOU 248 N ARG A 222 1150 1362 1090 -108 -44 -493 N ATOM 249 CA ARG A 222 36.177 -0.757 -20.584 1.00 14.72 C ANISOU 249 CA ARG A 222 1826 2015 1752 -169 -45 -483 C ATOM 250 C ARG A 222 36.247 -0.785 -22.116 1.00 15.10 C ANISOU 250 C ARG A 222 1852 2085 1800 -222 -51 -475 C ATOM 251 O ARG A 222 35.477 -0.110 -22.802 1.00 11.52 O ANISOU 251 O ARG A 222 1420 1592 1364 -251 -49 -441 O ATOM 252 CB ARG A 222 37.382 -0.006 -20.003 1.00 9.93 C ANISOU 252 CB ARG A 222 1219 1444 1110 -196 -51 -525 C ATOM 253 CG ARG A 222 37.588 1.401 -20.568 1.00 14.76 C ANISOU 253 CG ARG A 222 1856 2047 1707 -272 -55 -519 C ATOM 254 CD ARG A 222 39.047 1.847 -20.432 1.00 17.36 C ANISOU 254 CD ARG A 222 2164 2442 1988 -322 -62 -571 C ATOM 255 NE ARG A 222 39.922 1.075 -21.312 1.00 17.35 N ANISOU 255 NE ARG A 222 2106 2523 1962 -346 -69 -606 N ATOM 256 CZ ARG A 222 41.248 1.007 -21.209 1.00 17.93 C ANISOU 256 CZ ARG A 222 2141 2683 1989 -372 -76 -664 C ATOM 257 NH1 ARG A 222 41.897 1.670 -20.261 1.00 14.55 N ANISOU 257 NH1 ARG A 222 1724 2270 1535 -381 -74 -693 N ATOM 258 NH2 ARG A 222 41.930 0.267 -22.070 1.00 18.10 N ANISOU 258 NH2 ARG A 222 2110 2783 1986 -385 -85 -695 N ATOM 259 N ASP A 223 37.175 -1.575 -22.649 1.00 11.61 N ANISOU 259 N ASP A 223 1369 1709 1334 -230 -62 -509 N ATOM 260 CA ASP A 223 37.291 -1.728 -24.102 1.00 17.61 C ANISOU 260 CA ASP A 223 2102 2496 2093 -275 -69 -503 C ATOM 261 C ASP A 223 35.978 -2.181 -24.766 1.00 14.01 C ANISOU 261 C ASP A 223 1656 1989 1678 -257 -63 -453 C ATOM 262 O ASP A 223 35.565 -1.617 -25.775 1.00 11.10 O ANISOU 262 O ASP A 223 1293 1601 1323 -299 -62 -430 O ATOM 263 CB ASP A 223 38.439 -2.678 -24.465 1.00 17.59 C ANISOU 263 CB ASP A 223 2050 2578 2054 -268 -86 -550 C ATOM 264 CG ASP A 223 39.816 -2.043 -24.266 1.00 22.72 C ANISOU 264 CG ASP A 223 2675 3301 2654 -311 -93 -604 C ATOM 265 OD1 ASP A 223 39.889 -0.840 -23.916 1.00 21.49 O ANISOU 265 OD1 ASP A 223 2548 3124 2494 -357 -84 -601 O ATOM 266 OD2 ASP A 223 40.827 -2.753 -24.466 1.00 21.28 O ANISOU 266 OD2 ASP A 223 2449 3203 2433 -300 -108 -652 O ATOM 267 N ASP A 224 35.334 -3.195 -24.196 1.00 9.16 N ANISOU 267 N ASP A 224 1047 1354 1081 -196 -58 -440 N ATOM 268 CA ASP A 224 34.066 -3.688 -24.723 1.00 12.34 C ANISOU 268 CA ASP A 224 1457 1714 1517 -181 -50 -395 C ATOM 269 C ASP A 224 33.011 -2.578 -24.765 1.00 12.99 C ANISOU 269 C ASP A 224 1570 1743 1624 -196 -37 -361 C ATOM 270 O ASP A 224 32.200 -2.519 -25.696 1.00 10.89 O ANISOU 270 O ASP A 224 1303 1456 1380 -210 -34 -332 O ATOM 271 CB ASP A 224 33.535 -4.873 -23.901 1.00 11.04 C ANISOU 271 CB ASP A 224 1305 1535 1357 -123 -46 -387 C ATOM 272 CG ASP A 224 34.274 -6.181 -24.187 1.00 18.98 C ANISOU 272 CG ASP A 224 2293 2583 2335 -99 -65 -413 C ATOM 273 OD1 ASP A 224 35.029 -6.244 -25.181 1.00 15.30 O ANISOU 273 OD1 ASP A 224 1797 2163 1856 -126 -81 -431 O ATOM 274 OD2 ASP A 224 34.092 -7.152 -23.412 1.00 17.25 O ANISOU 274 OD2 ASP A 224 2096 2352 2105 -52 -67 -416 O ATOM 275 N ILE A 225 33.017 -1.707 -23.759 1.00 9.07 N ANISOU 275 N ILE A 225 1101 1224 1120 -188 -33 -366 N ATOM 276 CA ILE A 225 32.037 -0.632 -23.697 1.00 13.02 C ANISOU 276 CA ILE A 225 1637 1676 1634 -190 -27 -338 C ATOM 277 C ILE A 225 32.400 0.489 -24.675 1.00 9.68 C ANISOU 277 C ILE A 225 1233 1248 1198 -251 -37 -340 C ATOM 278 O ILE A 225 31.552 0.970 -25.432 1.00 9.29 O ANISOU 278 O ILE A 225 1203 1166 1159 -260 -37 -316 O ATOM 279 CB ILE A 225 31.888 -0.084 -22.259 1.00 15.51 C ANISOU 279 CB ILE A 225 1982 1968 1942 -155 -24 -341 C ATOM 280 CG1 ILE A 225 31.132 -1.081 -21.377 1.00 10.64 C ANISOU 280 CG1 ILE A 225 1359 1344 1341 -98 -11 -328 C ATOM 281 CG2 ILE A 225 31.144 1.247 -22.257 1.00 13.54 C ANISOU 281 CG2 ILE A 225 1779 1675 1692 -159 -28 -321 C ATOM 282 CD1 ILE A 225 31.331 -0.825 -19.883 1.00 9.15 C ANISOU 282 CD1 ILE A 225 1190 1144 1143 -61 -8 -340 C ATOM 283 N LEU A 226 33.667 0.885 -24.673 1.00 9.51 N ANISOU 283 N LEU A 226 1206 1260 1146 -294 -46 -373 N ATOM 284 CA LEU A 226 34.116 1.956 -25.554 1.00 11.12 C ANISOU 284 CA LEU A 226 1435 1462 1327 -365 -56 -378 C ATOM 285 C LEU A 226 33.981 1.593 -27.026 1.00 16.98 C ANISOU 285 C LEU A 226 2154 2216 2081 -396 -58 -368 C ATOM 286 O LEU A 226 33.713 2.464 -27.848 1.00 18.63 O ANISOU 286 O LEU A 226 2399 2395 2283 -437 -63 -355 O ATOM 287 CB LEU A 226 35.565 2.348 -25.256 1.00 10.71 C ANISOU 287 CB LEU A 226 1374 1461 1235 -415 -63 -420 C ATOM 288 CG LEU A 226 35.796 3.060 -23.922 1.00 12.10 C ANISOU 288 CG LEU A 226 1586 1619 1394 -400 -64 -431 C ATOM 289 CD1 LEU A 226 37.272 3.431 -23.757 1.00 10.56 C ANISOU 289 CD1 LEU A 226 1375 1484 1153 -458 -70 -476 C ATOM 290 CD2 LEU A 226 34.893 4.287 -23.824 1.00 12.09 C ANISOU 290 CD2 LEU A 226 1657 1543 1392 -402 -69 -400 C ATOM 291 N ASN A 227 34.168 0.317 -27.367 1.00 12.87 N ANISOU 291 N ASN A 227 1580 1736 1573 -374 -56 -373 N ATOM 292 CA ASN A 227 34.080 -0.072 -28.772 1.00 14.52 C ANISOU 292 CA ASN A 227 1764 1958 1794 -401 -60 -363 C ATOM 293 C ASN A 227 32.740 -0.665 -29.199 1.00 10.76 C ANISOU 293 C ASN A 227 1287 1444 1358 -358 -52 -325 C ATOM 294 O ASN A 227 32.567 -1.034 -30.356 1.00 15.29 O ANISOU 294 O ASN A 227 1840 2023 1945 -373 -55 -314 O ATOM 295 CB ASN A 227 35.275 -0.934 -29.221 1.00 20.40 C ANISOU 295 CB ASN A 227 2453 2781 2516 -417 -71 -396 C ATOM 296 CG ASN A 227 35.269 -2.333 -28.629 1.00 21.78 C ANISOU 296 CG ASN A 227 2599 2980 2699 -351 -73 -402 C ATOM 297 OD1 ASN A 227 34.219 -2.910 -28.349 1.00 24.99 O ANISOU 297 OD1 ASN A 227 3017 3345 3134 -305 -65 -372 O ATOM 298 ND2 ASN A 227 36.459 -2.898 -28.463 1.00 21.84 N ANISOU 298 ND2 ASN A 227 2570 3057 2671 -349 -86 -445 N ATOM 299 N GLY A 228 31.795 -0.734 -28.264 1.00 9.41 N ANISOU 299 N GLY A 228 1136 1237 1203 -307 -42 -307 N ATOM 300 CA GLY A 228 30.436 -1.143 -28.578 1.00 12.04 C ANISOU 300 CA GLY A 228 1469 1539 1566 -273 -31 -274 C ATOM 301 C GLY A 228 30.110 -2.628 -28.489 1.00 10.80 C ANISOU 301 C GLY A 228 1277 1400 1425 -237 -26 -264 C ATOM 302 O GLY A 228 28.960 -3.031 -28.717 1.00 9.48 O ANISOU 302 O GLY A 228 1108 1214 1280 -215 -16 -238 O ATOM 303 N SER A 229 31.105 -3.447 -28.167 1.00 12.01 N ANISOU 303 N SER A 229 1410 1593 1562 -233 -35 -288 N ATOM 304 CA SER A 229 30.878 -4.878 -27.965 1.00 12.16 C ANISOU 304 CA SER A 229 1413 1623 1584 -197 -35 -282 C ATOM 305 C SER A 229 29.921 -5.113 -26.792 1.00 10.88 C ANISOU 305 C SER A 229 1274 1432 1428 -158 -19 -266 C ATOM 306 O SER A 229 29.135 -6.056 -26.799 1.00 9.03 O ANISOU 306 O SER A 229 1040 1191 1202 -140 -13 -245 O ATOM 307 CB SER A 229 32.207 -5.600 -27.726 1.00 9.23 C ANISOU 307 CB SER A 229 1025 1300 1180 -189 -54 -319 C ATOM 308 OG SER A 229 33.042 -5.491 -28.878 1.00 11.86 O ANISOU 308 OG SER A 229 1329 1673 1504 -226 -69 -335 O ATOM 309 N HIS A 230 29.996 -4.243 -25.787 1.00 11.68 N ANISOU 309 N HIS A 230 1397 1521 1522 -150 -14 -275 N ATOM 310 CA HIS A 230 28.997 -4.204 -24.721 1.00 9.13 C ANISOU 310 CA HIS A 230 1093 1171 1203 -116 2 -259 C ATOM 311 C HIS A 230 28.173 -2.922 -24.819 1.00 8.59 C ANISOU 311 C HIS A 230 1043 1077 1145 -119 7 -244 C ATOM 312 O HIS A 230 28.575 -1.884 -24.293 1.00 9.46 O ANISOU 312 O HIS A 230 1177 1176 1243 -121 2 -256 O ATOM 313 CB HIS A 230 29.667 -4.291 -23.346 1.00 8.60 C ANISOU 313 CB HIS A 230 1041 1109 1116 -89 1 -283 C ATOM 314 CG HIS A 230 28.695 -4.384 -22.211 1.00 10.23 C ANISOU 314 CG HIS A 230 1267 1295 1327 -54 16 -267 C ATOM 315 ND1 HIS A 230 29.083 -4.338 -20.888 1.00 12.23 N ANISOU 315 ND1 HIS A 230 1538 1544 1566 -26 18 -284 N ATOM 316 CD2 HIS A 230 27.347 -4.521 -22.203 1.00 11.50 C ANISOU 316 CD2 HIS A 230 1426 1444 1498 -45 31 -239 C ATOM 317 CE1 HIS A 230 28.017 -4.458 -20.115 1.00 11.76 C ANISOU 317 CE1 HIS A 230 1489 1469 1510 -1 33 -264 C ATOM 318 NE2 HIS A 230 26.950 -4.568 -20.888 1.00 8.72 N ANISOU 318 NE2 HIS A 230 1091 1084 1138 -13 42 -238 N ATOM 319 N PRO A 231 27.020 -2.990 -25.500 1.00 10.31 N ANISOU 319 N PRO A 231 1253 1285 1378 -116 16 -220 N ATOM 320 CA PRO A 231 26.168 -1.818 -25.718 1.00 17.40 C ANISOU 320 CA PRO A 231 2172 2162 2278 -109 16 -210 C ATOM 321 C PRO A 231 25.547 -1.332 -24.409 1.00 17.04 C ANISOU 321 C PRO A 231 2146 2108 2220 -69 22 -209 C ATOM 322 O PRO A 231 25.047 -2.142 -23.620 1.00 16.01 O ANISOU 322 O PRO A 231 2003 1991 2090 -46 36 -202 O ATOM 323 CB PRO A 231 25.062 -2.350 -26.648 1.00 19.11 C ANISOU 323 CB PRO A 231 2366 2384 2512 -106 26 -189 C ATOM 324 CG PRO A 231 25.525 -3.695 -27.102 1.00 15.11 C ANISOU 324 CG PRO A 231 1832 1896 2015 -124 27 -186 C ATOM 325 CD PRO A 231 26.404 -4.214 -26.036 1.00 13.67 C ANISOU 325 CD PRO A 231 1655 1723 1816 -115 24 -202 C ATOM 326 N VAL A 232 25.581 -0.023 -24.178 1.00 10.42 N ANISOU 326 N VAL A 232 1345 1248 1367 -62 10 -216 N ATOM 327 CA VAL A 232 25.009 0.539 -22.960 1.00 9.17 C ANISOU 327 CA VAL A 232 1207 1083 1194 -18 10 -215 C ATOM 328 C VAL A 232 24.224 1.796 -23.283 1.00 9.39 C ANISOU 328 C VAL A 232 1272 1090 1204 4 -4 -213 C ATOM 329 O VAL A 232 24.413 2.397 -24.335 1.00 15.71 O ANISOU 329 O VAL A 232 2096 1872 2002 -22 -16 -215 O ATOM 330 CB VAL A 232 26.102 0.889 -21.920 1.00 16.87 C ANISOU 330 CB VAL A 232 2204 2049 2158 -18 3 -232 C ATOM 331 CG1 VAL A 232 26.908 -0.355 -21.538 1.00 9.06 C ANISOU 331 CG1 VAL A 232 1185 1082 1177 -28 13 -242 C ATOM 332 CG2 VAL A 232 27.011 1.999 -22.443 1.00 9.37 C ANISOU 332 CG2 VAL A 232 1291 1078 1192 -56 -17 -245 C ATOM 333 N SER A 233 23.342 2.187 -22.372 1.00 11.02 N ANISOU 333 N SER A 233 1489 1302 1396 55 -4 -210 N ATOM 334 CA SER A 233 22.564 3.412 -22.515 1.00 13.37 C ANISOU 334 CA SER A 233 1830 1584 1666 92 -25 -213 C ATOM 335 C SER A 233 23.454 4.631 -22.355 1.00 13.81 C ANISOU 335 C SER A 233 1953 1597 1698 79 -51 -223 C ATOM 336 O SER A 233 24.571 4.531 -21.851 1.00 10.87 O ANISOU 336 O SER A 233 1583 1217 1331 49 -50 -230 O ATOM 337 CB SER A 233 21.447 3.465 -21.464 1.00 13.14 C ANISOU 337 CB SER A 233 1789 1583 1620 155 -21 -212 C ATOM 338 OG SER A 233 21.988 3.572 -20.156 1.00 12.89 O ANISOU 338 OG SER A 233 1769 1544 1583 170 -22 -214 O ATOM 339 N PHE A 234 22.949 5.783 -22.783 1.00 13.89 N ANISOU 339 N PHE A 234 2021 1580 1677 102 -77 -228 N ATOM 340 CA PHE A 234 23.676 7.036 -22.667 1.00 10.51 C ANISOU 340 CA PHE A 234 1674 1106 1216 87 -106 -236 C ATOM 341 C PHE A 234 24.026 7.309 -21.214 1.00 16.20 C ANISOU 341 C PHE A 234 2407 1823 1926 114 -112 -238 C ATOM 342 O PHE A 234 25.163 7.674 -20.885 1.00 15.73 O ANISOU 342 O PHE A 234 2376 1742 1859 74 -119 -245 O ATOM 343 CB PHE A 234 22.834 8.181 -23.238 1.00 15.70 C ANISOU 343 CB PHE A 234 2402 1733 1829 126 -137 -242 C ATOM 344 CG PHE A 234 23.454 9.545 -23.076 1.00 15.51 C ANISOU 344 CG PHE A 234 2481 1653 1759 113 -174 -250 C ATOM 345 CD1 PHE A 234 24.666 9.848 -23.664 1.00 15.84 C ANISOU 345 CD1 PHE A 234 2557 1665 1796 29 -178 -253 C ATOM 346 CD2 PHE A 234 22.806 10.528 -22.356 1.00 17.15 C ANISOU 346 CD2 PHE A 234 2754 1843 1921 182 -206 -254 C ATOM 347 CE1 PHE A 234 25.231 11.107 -23.519 1.00 17.94 C ANISOU 347 CE1 PHE A 234 2925 1879 2012 6 -212 -260 C ATOM 348 CE2 PHE A 234 23.361 11.787 -22.212 1.00 21.69 C ANISOU 348 CE2 PHE A 234 3435 2360 2446 169 -244 -260 C ATOM 349 CZ PHE A 234 24.576 12.076 -22.796 1.00 18.69 C ANISOU 349 CZ PHE A 234 3093 1947 2062 76 -245 -262 C ATOM 350 N GLU A 235 23.040 7.111 -20.349 1.00 16.53 N ANISOU 350 N GLU A 235 2424 1892 1964 181 -107 -234 N ATOM 351 CA AGLU A 235 23.200 7.370 -18.928 0.67 17.85 C ANISOU 351 CA AGLU A 235 2602 2057 2122 219 -113 -235 C ATOM 352 CA BGLU A 235 23.200 7.360 -18.919 0.33 18.34 C ANISOU 352 CA BGLU A 235 2663 2119 2184 219 -113 -235 C ATOM 353 C GLU A 235 24.331 6.521 -18.338 1.00 19.51 C ANISOU 353 C GLU A 235 2773 2276 2365 177 -90 -237 C ATOM 354 O GLU A 235 25.158 7.016 -17.573 1.00 11.84 O ANISOU 354 O GLU A 235 1832 1282 1383 172 -101 -244 O ATOM 355 CB AGLU A 235 21.870 7.116 -18.204 0.67 20.19 C ANISOU 355 CB AGLU A 235 2865 2396 2411 293 -107 -232 C ATOM 356 CB BGLU A 235 21.897 7.071 -18.162 0.33 19.82 C ANISOU 356 CB BGLU A 235 2816 2350 2365 292 -106 -231 C ATOM 357 CG AGLU A 235 20.722 8.047 -18.645 0.67 22.75 C ANISOU 357 CG AGLU A 235 3230 2723 2691 352 -136 -239 C ATOM 358 CG BGLU A 235 21.975 7.377 -16.670 0.33 22.14 C ANISOU 358 CG BGLU A 235 3121 2643 2648 338 -114 -231 C ATOM 359 CD AGLU A 235 20.188 7.752 -20.055 0.67 26.61 C ANISOU 359 CD AGLU A 235 3701 3224 3185 332 -129 -241 C ATOM 360 CD BGLU A 235 20.764 6.889 -15.892 0.33 26.34 C ANISOU 360 CD BGLU A 235 3603 3230 3174 399 -100 -229 C ATOM 361 OE1AGLU A 235 20.240 6.586 -20.506 0.67 17.39 O ANISOU 361 OE1AGLU A 235 2467 2084 2057 290 -95 -233 O ATOM 362 OE1BGLU A 235 19.959 6.116 -16.454 0.33 27.50 O ANISOU 362 OE1BGLU A 235 3697 3420 3330 393 -79 -227 O ATOM 363 OE2AGLU A 235 19.701 8.696 -20.715 0.67 31.96 O ANISOU 363 OE2AGLU A 235 4439 3881 3824 362 -159 -251 O ATOM 364 OE2BGLU A 235 20.622 7.277 -14.712 0.33 23.00 O ANISOU 364 OE2BGLU A 235 3194 2811 2736 448 -111 -229 O ATOM 365 N LYS A 236 24.368 5.245 -18.700 1.00 13.42 N ANISOU 365 N LYS A 236 1937 1535 1626 151 -60 -233 N ATOM 366 CA LYS A 236 25.408 4.360 -18.183 1.00 12.42 C ANISOU 366 CA LYS A 236 1778 1420 1523 121 -42 -240 C ATOM 367 C LYS A 236 26.794 4.688 -18.767 1.00 12.34 C ANISOU 367 C LYS A 236 1787 1393 1508 58 -52 -255 C ATOM 368 O LYS A 236 27.800 4.658 -18.054 1.00 14.71 O ANISOU 368 O LYS A 236 2089 1693 1806 46 -51 -270 O ATOM 369 CB LYS A 236 25.037 2.891 -18.397 1.00 16.50 C ANISOU 369 CB LYS A 236 2233 1971 2065 114 -14 -234 C ATOM 370 CG LYS A 236 23.923 2.393 -17.478 1.00 13.05 C ANISOU 370 CG LYS A 236 1771 1559 1627 164 1 -223 C ATOM 371 CD LYS A 236 24.413 2.225 -16.053 1.00 20.43 C ANISOU 371 CD LYS A 236 2711 2490 2561 189 5 -230 C ATOM 372 CE LYS A 236 23.252 2.024 -15.071 1.00 24.06 C ANISOU 372 CE LYS A 236 3154 2975 3011 240 15 -221 C ATOM 373 NZ LYS A 236 22.334 3.199 -15.027 1.00 29.12 N ANISOU 373 NZ LYS A 236 3819 3619 3627 285 -6 -218 N ATOM 374 N ALA A 237 26.836 5.020 -20.050 1.00 9.99 N ANISOU 374 N ALA A 237 1505 1087 1206 18 -60 -254 N ATOM 375 CA ALA A 237 28.085 5.413 -20.706 1.00 13.67 C ANISOU 375 CA ALA A 237 1990 1545 1660 -51 -69 -269 C ATOM 376 C ALA A 237 28.793 6.544 -19.955 1.00 14.04 C ANISOU 376 C ALA A 237 2095 1564 1674 -60 -90 -280 C ATOM 377 O ALA A 237 30.013 6.519 -19.765 1.00 10.91 O ANISOU 377 O ALA A 237 1693 1182 1271 -105 -88 -300 O ATOM 378 CB ALA A 237 27.822 5.820 -22.140 1.00 10.14 C ANISOU 378 CB ALA A 237 1565 1083 1205 -86 -79 -264 C ATOM 379 N CYS A 238 28.013 7.530 -19.526 1.00 13.01 N ANISOU 379 N CYS A 238 2023 1400 1520 -15 -110 -271 N ATOM 380 CA CYS A 238 28.556 8.674 -18.813 1.00 15.63 C ANISOU 380 CA CYS A 238 2423 1698 1816 -19 -135 -278 C ATOM 381 C CYS A 238 29.015 8.284 -17.406 1.00 16.40 C ANISOU 381 C CYS A 238 2491 1811 1928 12 -124 -285 C ATOM 382 O CYS A 238 29.988 8.831 -16.890 1.00 11.01 O ANISOU 382 O CYS A 238 1838 1119 1226 -17 -134 -299 O ATOM 383 CB CYS A 238 27.536 9.826 -18.785 1.00 14.01 C ANISOU 383 CB CYS A 238 2297 1452 1575 31 -167 -266 C ATOM 384 SG CYS A 238 27.104 10.487 -20.434 1.00 17.53 S ANISOU 384 SG CYS A 238 2800 1867 1992 -3 -186 -264 S ATOM 385 N GLU A 239 28.319 7.331 -16.794 1.00 14.68 N ANISOU 385 N GLU A 239 2219 1620 1740 67 -103 -277 N ATOM 386 CA GLU A 239 28.725 6.813 -15.493 1.00 14.69 C ANISOU 386 CA GLU A 239 2191 1634 1755 99 -90 -286 C ATOM 387 C GLU A 239 30.067 6.109 -15.613 1.00 13.55 C ANISOU 387 C GLU A 239 2010 1517 1622 47 -76 -310 C ATOM 388 O GLU A 239 30.965 6.328 -14.795 1.00 10.29 O ANISOU 388 O GLU A 239 1605 1105 1200 44 -78 -329 O ATOM 389 CB GLU A 239 27.690 5.832 -14.941 1.00 14.73 C ANISOU 389 CB GLU A 239 2148 1663 1785 156 -69 -273 C ATOM 390 CG GLU A 239 26.523 6.482 -14.220 1.00 30.76 C ANISOU 390 CG GLU A 239 4205 3684 3800 226 -83 -258 C ATOM 391 CD GLU A 239 25.442 5.479 -13.830 1.00 34.23 C ANISOU 391 CD GLU A 239 4591 4158 4256 268 -60 -247 C ATOM 392 OE1 GLU A 239 25.763 4.490 -13.137 1.00 28.30 O ANISOU 392 OE1 GLU A 239 3805 3423 3525 270 -37 -251 O ATOM 393 OE2 GLU A 239 24.271 5.688 -14.213 1.00 40.14 O ANISOU 393 OE2 GLU A 239 5338 4922 4993 297 -65 -236 O ATOM 394 N PHE A 240 30.193 5.251 -16.624 1.00 10.07 N ANISOU 394 N PHE A 240 1528 1103 1196 11 -62 -313 N ATOM 395 CA PHE A 240 31.465 4.592 -16.895 1.00 10.36 C ANISOU 395 CA PHE A 240 1528 1175 1233 -35 -53 -340 C ATOM 396 C PHE A 240 32.539 5.634 -17.170 1.00 10.84 C ANISOU 396 C PHE A 240 1625 1233 1261 -97 -70 -360 C ATOM 397 O PHE A 240 33.625 5.583 -16.592 1.00 11.28 O ANISOU 397 O PHE A 240 1669 1314 1305 -113 -69 -389 O ATOM 398 CB PHE A 240 31.346 3.635 -18.064 1.00 9.83 C ANISOU 398 CB PHE A 240 1418 1135 1182 -61 -42 -337 C ATOM 399 CG PHE A 240 30.574 2.395 -17.743 1.00 11.14 C ANISOU 399 CG PHE A 240 1547 1312 1373 -15 -24 -324 C ATOM 400 CD1 PHE A 240 29.379 2.119 -18.390 1.00 11.82 C ANISOU 400 CD1 PHE A 240 1624 1392 1474 -3 -18 -298 C ATOM 401 CD2 PHE A 240 31.043 1.503 -16.788 1.00 9.48 C ANISOU 401 CD2 PHE A 240 1316 1120 1167 15 -14 -342 C ATOM 402 CE1 PHE A 240 28.655 0.967 -18.091 1.00 9.34 C ANISOU 402 CE1 PHE A 240 1280 1092 1176 29 -1 -286 C ATOM 403 CE2 PHE A 240 30.333 0.349 -16.485 1.00 9.32 C ANISOU 403 CE2 PHE A 240 1274 1105 1161 50 1 -330 C ATOM 404 CZ PHE A 240 29.131 0.084 -17.133 1.00 11.59 C ANISOU 404 CZ PHE A 240 1553 1389 1462 52 9 -301 C ATOM 405 N GLY A 241 32.218 6.590 -18.038 1.00 11.66 N ANISOU 405 N GLY A 241 1777 1308 1346 -133 -86 -346 N ATOM 406 CA GLY A 241 33.139 7.665 -18.370 1.00 12.09 C ANISOU 406 CA GLY A 241 1880 1354 1360 -205 -104 -362 C ATOM 407 C GLY A 241 33.678 8.382 -17.140 1.00 15.61 C ANISOU 407 C GLY A 241 2362 1786 1785 -193 -115 -373 C ATOM 408 O GLY A 241 34.863 8.749 -17.075 1.00 11.24 O ANISOU 408 O GLY A 241 1814 1255 1203 -253 -118 -401 O ATOM 409 N GLY A 242 32.795 8.588 -16.168 1.00 10.95 N ANISOU 409 N GLY A 242 1794 1162 1205 -115 -120 -354 N ATOM 410 CA GLY A 242 33.142 9.272 -14.935 1.00 11.10 C ANISOU 410 CA GLY A 242 1850 1160 1207 -90 -132 -361 C ATOM 411 C GLY A 242 34.145 8.484 -14.106 1.00 13.32 C ANISOU 411 C GLY A 242 2073 1484 1502 -84 -113 -391 C ATOM 412 O GLY A 242 35.070 9.061 -13.527 1.00 13.19 O ANISOU 412 O GLY A 242 2079 1472 1462 -111 -121 -413 O ATOM 413 N PHE A 243 33.963 7.167 -14.048 1.00 10.63 N ANISOU 413 N PHE A 243 1666 1177 1196 -50 -90 -396 N ATOM 414 CA PHE A 243 34.923 6.304 -13.362 1.00 11.33 C ANISOU 414 CA PHE A 243 1705 1309 1292 -38 -74 -431 C ATOM 415 C PHE A 243 36.227 6.320 -14.160 1.00 12.20 C ANISOU 415 C PHE A 243 1793 1470 1374 -120 -75 -467 C ATOM 416 O PHE A 243 37.321 6.362 -13.595 1.00 10.84 O ANISOU 416 O PHE A 243 1606 1332 1181 -134 -74 -505 O ATOM 417 CB PHE A 243 34.406 4.863 -13.239 1.00 10.74 C ANISOU 417 CB PHE A 243 1578 1253 1249 13 -54 -427 C ATOM 418 CG PHE A 243 33.369 4.667 -12.161 1.00 13.99 C ANISOU 418 CG PHE A 243 2000 1632 1682 92 -48 -404 C ATOM 419 CD1 PHE A 243 32.202 3.964 -12.420 1.00 19.29 C ANISOU 419 CD1 PHE A 243 2655 2298 2375 122 -37 -376 C ATOM 420 CD2 PHE A 243 33.562 5.177 -10.890 1.00 16.53 C ANISOU 420 CD2 PHE A 243 2346 1934 2000 133 -53 -410 C ATOM 421 CE1 PHE A 243 31.243 3.778 -11.430 1.00 20.86 C ANISOU 421 CE1 PHE A 243 2859 2479 2587 187 -30 -357 C ATOM 422 CE2 PHE A 243 32.612 4.998 -9.896 1.00 14.12 C ANISOU 422 CE2 PHE A 243 2047 1604 1712 204 -48 -389 C ATOM 423 CZ PHE A 243 31.450 4.297 -10.164 1.00 20.28 C ANISOU 423 CZ PHE A 243 2808 2387 2510 229 -36 -363 C ATOM 424 N GLN A 244 36.101 6.300 -15.482 1.00 12.31 N ANISOU 424 N GLN A 244 1802 1495 1383 -173 -77 -458 N ATOM 425 CA GLN A 244 37.277 6.317 -16.345 1.00 20.44 C ANISOU 425 CA GLN A 244 2806 2580 2382 -256 -78 -492 C ATOM 426 C GLN A 244 38.114 7.564 -16.095 1.00 11.38 C ANISOU 426 C GLN A 244 1704 1431 1189 -319 -92 -510 C ATOM 427 O GLN A 244 39.336 7.504 -16.013 1.00 14.97 O ANISOU 427 O GLN A 244 2127 1947 1614 -364 -89 -553 O ATOM 428 CB GLN A 244 36.880 6.227 -17.822 1.00 11.53 C ANISOU 428 CB GLN A 244 1673 1452 1255 -302 -79 -474 C ATOM 429 CG GLN A 244 38.049 5.935 -18.750 1.00 11.12 C ANISOU 429 CG GLN A 244 1576 1473 1175 -378 -78 -510 C ATOM 430 CD GLN A 244 37.663 5.901 -20.228 1.00 15.85 C ANISOU 430 CD GLN A 244 2175 2070 1778 -424 -80 -491 C ATOM 431 OE1 GLN A 244 36.519 5.586 -20.593 1.00 11.02 O ANISOU 431 OE1 GLN A 244 1571 1417 1201 -383 -77 -455 O ATOM 432 NE2 GLN A 244 38.626 6.222 -21.090 1.00 11.39 N ANISOU 432 NE2 GLN A 244 1600 1554 1175 -513 -84 -517 N ATOM 433 N ALA A 245 37.444 8.696 -15.964 1.00 11.54 N ANISOU 433 N ALA A 245 1803 1384 1198 -321 -109 -478 N ATOM 434 CA ALA A 245 38.131 9.948 -15.725 1.00 11.98 C ANISOU 434 CA ALA A 245 1921 1425 1205 -384 -126 -489 C ATOM 435 C ALA A 245 38.870 9.902 -14.383 1.00 22.63 C ANISOU 435 C ALA A 245 3252 2796 2551 -353 -122 -518 C ATOM 436 O ALA A 245 40.024 10.333 -14.288 1.00 14.90 O ANISOU 436 O ALA A 245 2272 1859 1531 -421 -124 -554 O ATOM 437 CB ALA A 245 37.143 11.107 -15.772 1.00 15.40 C ANISOU 437 CB ALA A 245 2454 1773 1624 -373 -152 -448 C ATOM 438 N GLN A 246 38.210 9.371 -13.352 1.00 14.36 N ANISOU 438 N GLN A 246 2189 1724 1543 -252 -115 -505 N ATOM 439 CA GLN A 246 38.829 9.258 -12.032 1.00 13.04 C ANISOU 439 CA GLN A 246 2006 1572 1378 -210 -110 -532 C ATOM 440 C GLN A 246 40.095 8.414 -12.127 1.00 13.09 C ANISOU 440 C GLN A 246 1937 1667 1371 -238 -94 -588 C ATOM 441 O GLN A 246 41.115 8.731 -11.522 1.00 14.52 O ANISOU 441 O GLN A 246 2111 1884 1523 -260 -94 -626 O ATOM 442 CB GLN A 246 37.857 8.645 -11.016 1.00 11.49 C ANISOU 442 CB GLN A 246 1799 1339 1226 -98 -103 -509 C ATOM 443 CG GLN A 246 38.393 8.595 -9.594 1.00 14.05 C ANISOU 443 CG GLN A 246 2117 1668 1556 -45 -99 -533 C ATOM 444 CD GLN A 246 38.322 9.944 -8.896 1.00 13.04 C ANISOU 444 CD GLN A 246 2063 1487 1405 -46 -122 -516 C ATOM 445 OE1 GLN A 246 37.763 10.901 -9.432 1.00 13.33 O ANISOU 445 OE1 GLN A 246 2165 1479 1422 -77 -144 -485 O ATOM 446 NE2 GLN A 246 38.883 10.023 -7.689 1.00 13.72 N ANISOU 446 NE2 GLN A 246 2145 1576 1492 -7 -120 -539 N ATOM 447 N ILE A 247 40.010 7.341 -12.903 1.00 11.94 N ANISOU 447 N ILE A 247 1736 1560 1242 -233 -82 -594 N ATOM 448 CA ILE A 247 41.115 6.418 -13.097 1.00 11.51 C ANISOU 448 CA ILE A 247 1609 1595 1169 -245 -71 -649 C ATOM 449 C ILE A 247 42.300 7.062 -13.828 1.00 19.59 C ANISOU 449 C ILE A 247 2622 2685 2137 -355 -77 -687 C ATOM 450 O ILE A 247 43.458 6.862 -13.449 1.00 15.25 O ANISOU 450 O ILE A 247 2029 2211 1554 -369 -73 -744 O ATOM 451 CB ILE A 247 40.629 5.185 -13.869 1.00 12.24 C ANISOU 451 CB ILE A 247 1658 1705 1288 -216 -63 -641 C ATOM 452 CG1 ILE A 247 39.719 4.329 -12.974 1.00 11.94 C ANISOU 452 CG1 ILE A 247 1621 1622 1294 -112 -54 -619 C ATOM 453 CG2 ILE A 247 41.808 4.396 -14.451 1.00 11.35 C ANISOU 453 CG2 ILE A 247 1478 1691 1142 -245 -61 -698 C ATOM 454 CD1 ILE A 247 38.907 3.282 -13.731 1.00 10.53 C ANISOU 454 CD1 ILE A 247 1420 1438 1143 -88 -48 -594 C ATOM 455 N GLN A 248 42.009 7.842 -14.866 1.00 19.34 N ANISOU 455 N GLN A 248 2631 2629 2089 -433 -86 -659 N ATOM 456 CA GLN A 248 43.060 8.426 -15.696 1.00 20.14 C ANISOU 456 CA GLN A 248 2726 2795 2133 -551 -90 -691 C ATOM 457 C GLN A 248 43.591 9.775 -15.197 1.00 24.02 C ANISOU 457 C GLN A 248 3281 3269 2578 -619 -102 -698 C ATOM 458 O GLN A 248 44.742 10.120 -15.460 1.00 22.63 O ANISOU 458 O GLN A 248 3084 3169 2346 -709 -101 -743 O ATOM 459 CB GLN A 248 42.605 8.538 -17.162 1.00 17.53 C ANISOU 459 CB GLN A 248 2409 2452 1801 -611 -94 -663 C ATOM 460 CG GLN A 248 42.182 7.213 -17.760 1.00 14.49 C ANISOU 460 CG GLN A 248 1960 2090 1455 -556 -84 -659 C ATOM 461 CD GLN A 248 41.981 7.251 -19.266 1.00 18.78 C ANISOU 461 CD GLN A 248 2503 2642 1992 -622 -87 -642 C ATOM 462 OE1 GLN A 248 41.290 6.401 -19.828 1.00 20.26 O ANISOU 462 OE1 GLN A 248 2664 2818 2218 -577 -83 -620 O ATOM 463 NE2 GLN A 248 42.582 8.234 -19.925 1.00 24.80 N ANISOU 463 NE2 GLN A 248 3299 3422 2704 -733 -95 -652 N ATOM 464 N PHE A 249 42.766 10.529 -14.477 1.00 18.41 N ANISOU 464 N PHE A 249 2648 2463 1885 -577 -114 -656 N ATOM 465 CA PHE A 249 43.133 11.893 -14.082 1.00 20.91 C ANISOU 465 CA PHE A 249 3046 2747 2153 -643 -131 -654 C ATOM 466 C PHE A 249 43.234 12.079 -12.568 1.00 17.12 C ANISOU 466 C PHE A 249 2578 2243 1685 -571 -134 -661 C ATOM 467 O PHE A 249 43.791 13.071 -12.085 1.00 17.44 O ANISOU 467 O PHE A 249 2671 2274 1682 -624 -146 -671 O ATOM 468 CB PHE A 249 42.123 12.905 -14.643 1.00 13.63 C ANISOU 468 CB PHE A 249 2231 1726 1222 -666 -155 -598 C ATOM 469 CG PHE A 249 41.881 12.772 -16.122 1.00 15.70 C ANISOU 469 CG PHE A 249 2492 1996 1477 -727 -154 -586 C ATOM 470 CD1 PHE A 249 40.594 12.710 -16.624 1.00 23.55 C ANISOU 470 CD1 PHE A 249 3521 2920 2506 -673 -162 -539 C ATOM 471 CD2 PHE A 249 42.943 12.712 -17.010 1.00 19.13 C ANISOU 471 CD2 PHE A 249 2887 2515 1867 -836 -146 -624 C ATOM 472 CE1 PHE A 249 40.370 12.587 -17.984 1.00 24.31 C ANISOU 472 CE1 PHE A 249 3617 3023 2597 -725 -161 -530 C ATOM 473 CE2 PHE A 249 42.726 12.595 -18.373 1.00 22.85 C ANISOU 473 CE2 PHE A 249 3358 2993 2333 -891 -145 -613 C ATOM 474 CZ PHE A 249 41.440 12.531 -18.861 1.00 24.78 C ANISOU 474 CZ PHE A 249 3640 3158 2616 -834 -153 -565 C ATOM 475 N GLY A 250 42.688 11.131 -11.819 1.00 17.49 N ANISOU 475 N GLY A 250 2580 2278 1788 -454 -122 -655 N ATOM 476 CA GLY A 250 42.570 11.296 -10.382 1.00 16.61 C ANISOU 476 CA GLY A 250 2486 2129 1695 -374 -125 -653 C ATOM 477 C GLY A 250 41.335 12.114 -10.046 1.00 14.14 C ANISOU 477 C GLY A 250 2262 1711 1399 -328 -146 -593 C ATOM 478 O GLY A 250 40.482 12.344 -10.907 1.00 19.16 O ANISOU 478 O GLY A 250 2936 2306 2039 -341 -157 -556 O ATOM 479 N PRO A 251 41.230 12.560 -8.788 1.00 16.04 N ANISOU 479 N PRO A 251 2537 1911 1647 -268 -156 -586 N ATOM 480 CA PRO A 251 40.051 13.298 -8.316 1.00 14.65 C ANISOU 480 CA PRO A 251 2441 1643 1484 -205 -181 -534 C ATOM 481 C PRO A 251 39.720 14.503 -9.193 1.00 15.38 C ANISOU 481 C PRO A 251 2632 1684 1528 -279 -211 -504 C ATOM 482 O PRO A 251 40.605 15.143 -9.768 1.00 19.82 O ANISOU 482 O PRO A 251 3225 2270 2037 -390 -218 -524 O ATOM 483 CB PRO A 251 40.459 13.740 -6.900 1.00 12.63 C ANISOU 483 CB PRO A 251 2205 1370 1225 -160 -188 -545 C ATOM 484 CG PRO A 251 41.407 12.679 -6.456 1.00 16.63 C ANISOU 484 CG PRO A 251 2616 1954 1749 -144 -157 -598 C ATOM 485 CD PRO A 251 42.182 12.280 -7.698 1.00 14.35 C ANISOU 485 CD PRO A 251 2280 1741 1432 -241 -144 -632 C ATOM 486 N HIS A 252 38.433 14.797 -9.301 1.00 14.81 N ANISOU 486 N HIS A 252 2611 1547 1469 -218 -230 -459 N ATOM 487 CA HIS A 252 37.960 15.870 -10.162 1.00 18.03 C ANISOU 487 CA HIS A 252 3122 1899 1830 -270 -263 -431 C ATOM 488 C HIS A 252 38.434 17.246 -9.669 1.00 20.26 C ANISOU 488 C HIS A 252 3514 2134 2051 -314 -299 -428 C ATOM 489 O HIS A 252 38.279 17.579 -8.496 1.00 21.71 O ANISOU 489 O HIS A 252 3721 2286 2240 -244 -313 -420 O ATOM 490 CB HIS A 252 36.431 15.810 -10.250 1.00 15.23 C ANISOU 490 CB HIS A 252 2791 1494 1500 -174 -277 -391 C ATOM 491 CG HIS A 252 35.823 16.882 -11.099 1.00 18.52 C ANISOU 491 CG HIS A 252 3320 1851 1865 -205 -316 -366 C ATOM 492 ND1 HIS A 252 35.756 16.795 -12.472 1.00 18.97 N ANISOU 492 ND1 HIS A 252 3383 1917 1909 -273 -311 -366 N ATOM 493 CD2 HIS A 252 35.236 18.057 -10.767 1.00 19.56 C ANISOU 493 CD2 HIS A 252 3570 1910 1952 -170 -362 -341 C ATOM 494 CE1 HIS A 252 35.165 17.875 -12.953 1.00 18.57 C ANISOU 494 CE1 HIS A 252 3451 1799 1805 -280 -352 -344 C ATOM 495 NE2 HIS A 252 34.840 18.657 -11.940 1.00 27.77 N ANISOU 495 NE2 HIS A 252 4690 2915 2948 -217 -386 -330 N ATOM 496 N VAL A 253 39.023 18.027 -10.572 1.00 18.91 N ANISOU 496 N VAL A 253 3411 1958 1817 -434 -314 -436 N ATOM 497 CA VAL A 253 39.462 19.387 -10.273 1.00 20.85 C ANISOU 497 CA VAL A 253 3778 2153 1991 -494 -352 -431 C ATOM 498 C VAL A 253 38.630 20.345 -11.113 1.00 21.49 C ANISOU 498 C VAL A 253 3991 2154 2021 -512 -394 -397 C ATOM 499 O VAL A 253 38.888 20.519 -12.305 1.00 21.59 O ANISOU 499 O VAL A 253 4031 2175 1998 -610 -393 -403 O ATOM 500 CB VAL A 253 40.959 19.576 -10.587 1.00 27.79 C ANISOU 500 CB VAL A 253 4641 3097 2822 -637 -336 -473 C ATOM 501 CG1 VAL A 253 41.371 21.057 -10.470 1.00 20.09 C ANISOU 501 CG1 VAL A 253 3812 2063 1759 -723 -378 -465 C ATOM 502 CG2 VAL A 253 41.804 18.692 -9.676 1.00 35.35 C ANISOU 502 CG2 VAL A 253 5477 4135 3821 -608 -300 -514 C ATOM 503 N GLU A 254 37.628 20.959 -10.490 1.00 22.17 N ANISOU 503 N GLU A 254 4159 2166 2101 -411 -433 -364 N ATOM 504 CA GLU A 254 36.595 21.685 -11.230 1.00 27.22 C ANISOU 504 CA GLU A 254 4912 2733 2699 -387 -474 -335 C ATOM 505 C GLU A 254 37.087 22.782 -12.178 1.00 24.64 C ANISOU 505 C GLU A 254 4721 2362 2280 -516 -506 -337 C ATOM 506 O GLU A 254 36.455 23.038 -13.193 1.00 30.76 O ANISOU 506 O GLU A 254 5557 3101 3028 -526 -524 -325 O ATOM 507 CB GLU A 254 35.525 22.238 -10.278 1.00 36.50 C ANISOU 507 CB GLU A 254 6156 3845 3869 -251 -517 -307 C ATOM 508 CG GLU A 254 36.032 23.270 -9.295 1.00 43.83 C ANISOU 508 CG GLU A 254 7183 4726 4746 -258 -555 -303 C ATOM 509 CD GLU A 254 34.984 23.638 -8.259 0.50 49.95 C ANISOU 509 CD GLU A 254 8000 5453 5524 -108 -594 -277 C ATOM 510 OE1 GLU A 254 33.791 23.336 -8.490 0.50 50.47 O ANISOU 510 OE1 GLU A 254 8049 5515 5612 -11 -601 -262 O ATOM 511 OE2 GLU A 254 35.353 24.225 -7.216 0.50 48.73 O ANISOU 511 OE2 GLU A 254 7894 5271 5350 -87 -618 -274 O ATOM 512 N HIS A 255 38.204 23.429 -11.864 1.00 28.42 N ANISOU 512 N HIS A 255 5249 2842 2706 -619 -513 -353 N ATOM 513 CA HIS A 255 38.675 24.524 -12.709 1.00 35.18 C ANISOU 513 CA HIS A 255 6250 3653 3465 -752 -545 -353 C ATOM 514 C HIS A 255 39.625 24.041 -13.810 1.00 43.46 C ANISOU 514 C HIS A 255 7229 4777 4506 -896 -504 -383 C ATOM 515 O HIS A 255 40.159 24.836 -14.583 1.00 48.03 O ANISOU 515 O HIS A 255 7911 5334 5003 -1028 -522 -389 O ATOM 516 CB HIS A 255 39.321 25.636 -11.874 1.00 38.34 C ANISOU 516 CB HIS A 255 6766 4007 3793 -801 -582 -352 C ATOM 517 CG HIS A 255 40.449 25.167 -11.015 1.00 42.46 C ANISOU 517 CG HIS A 255 7179 4609 4346 -839 -544 -383 C ATOM 518 ND1 HIS A 255 41.650 24.731 -11.534 1.00 40.18 N ANISOU 518 ND1 HIS A 255 6806 4412 4048 -972 -501 -423 N ATOM 519 CD2 HIS A 255 40.560 25.065 -9.668 1.00 52.30 C ANISOU 519 CD2 HIS A 255 8385 5860 5626 -756 -543 -384 C ATOM 520 CE1 HIS A 255 42.451 24.377 -10.544 1.00 50.57 C ANISOU 520 CE1 HIS A 255 8035 5789 5390 -967 -476 -450 C ATOM 521 NE2 HIS A 255 41.814 24.572 -9.402 1.00 53.79 N ANISOU 521 NE2 HIS A 255 8469 6141 5827 -837 -500 -426 N ATOM 522 N LYS A 256 39.808 22.729 -13.882 1.00 42.58 N ANISOU 522 N LYS A 256 6946 4756 4475 -868 -451 -403 N ATOM 523 CA LYS A 256 40.684 22.109 -14.868 1.00 39.04 C ANISOU 523 CA LYS A 256 6410 4395 4028 -984 -411 -435 C ATOM 524 C LYS A 256 39.879 21.140 -15.736 1.00 33.39 C ANISOU 524 C LYS A 256 5613 3697 3374 -924 -389 -425 C ATOM 525 O LYS A 256 39.993 21.131 -16.966 1.00 30.13 O ANISOU 525 O LYS A 256 5214 3297 2939 -1006 -383 -430 O ATOM 526 CB LYS A 256 41.804 21.366 -14.137 1.00 44.39 C ANISOU 526 CB LYS A 256 6955 5176 4736 -1006 -371 -476 C ATOM 527 CG LYS A 256 42.902 20.776 -15.007 1.00 48.77 C ANISOU 527 CG LYS A 256 7413 5839 5277 -1128 -333 -519 C ATOM 528 CD LYS A 256 43.986 20.170 -14.113 1.00 51.89 C ANISOU 528 CD LYS A 256 7692 6334 5690 -1132 -302 -565 C ATOM 529 CE LYS A 256 45.249 19.831 -14.882 1.00 56.62 C ANISOU 529 CE LYS A 256 8211 7052 6249 -1268 -273 -617 C ATOM 530 NZ LYS A 256 45.149 18.519 -15.569 1.00 55.31 N ANISOU 530 NZ LYS A 256 7914 6960 6143 -1227 -240 -632 N ATOM 531 N HIS A 257 39.053 20.325 -15.088 1.00 26.60 N ANISOU 531 N HIS A 257 4673 2840 2592 -782 -376 -412 N ATOM 532 CA HIS A 257 38.255 19.333 -15.803 1.00 26.62 C ANISOU 532 CA HIS A 257 4594 2864 2656 -721 -354 -403 C ATOM 533 C HIS A 257 36.880 19.885 -16.153 1.00 26.65 C ANISOU 533 C HIS A 257 4696 2781 2649 -643 -390 -367 C ATOM 534 O HIS A 257 35.912 19.655 -15.435 1.00 27.90 O ANISOU 534 O HIS A 257 4838 2916 2845 -516 -398 -348 O ATOM 535 CB HIS A 257 38.128 18.057 -14.967 1.00 18.39 C ANISOU 535 CB HIS A 257 3410 1880 1698 -620 -317 -412 C ATOM 536 CG HIS A 257 39.448 17.473 -14.574 1.00 20.30 C ANISOU 536 CG HIS A 257 3555 2211 1947 -677 -285 -453 C ATOM 537 ND1 HIS A 257 39.752 17.117 -13.277 1.00 21.69 N ANISOU 537 ND1 HIS A 257 3679 2410 2154 -612 -274 -467 N ATOM 538 CD2 HIS A 257 40.559 17.216 -15.304 1.00 15.14 C ANISOU 538 CD2 HIS A 257 2852 1634 1268 -792 -264 -489 C ATOM 539 CE1 HIS A 257 40.987 16.652 -13.230 1.00 22.12 C ANISOU 539 CE1 HIS A 257 3654 2551 2200 -679 -248 -512 C ATOM 540 NE2 HIS A 257 41.500 16.704 -14.448 1.00 17.70 N ANISOU 540 NE2 HIS A 257 3092 2030 1605 -789 -242 -527 N ATOM 541 N LYS A 258 36.809 20.618 -17.258 1.00 29.79 N ANISOU 541 N LYS A 258 5197 3136 2987 -721 -413 -361 N ATOM 542 CA LYS A 258 35.568 21.248 -17.710 1.00 39.37 C ANISOU 542 CA LYS A 258 6519 4267 4174 -652 -454 -335 C ATOM 543 C LYS A 258 35.362 21.015 -19.203 1.00 39.44 C ANISOU 543 C LYS A 258 6528 4279 4178 -707 -444 -336 C ATOM 544 O LYS A 258 36.305 20.659 -19.906 1.00 35.82 O ANISOU 544 O LYS A 258 6016 3876 3718 -819 -415 -356 O ATOM 545 CB LYS A 258 35.600 22.747 -17.406 1.00 41.56 C ANISOU 545 CB LYS A 258 6980 4455 4356 -679 -512 -324 C ATOM 546 CG LYS A 258 36.944 23.396 -17.669 1.00 45.04 C ANISOU 546 CG LYS A 258 7481 4903 4728 -843 -513 -343 C ATOM 547 CD LYS A 258 37.006 24.778 -17.044 1.00 55.05 C ANISOU 547 CD LYS A 258 8924 6086 5908 -857 -570 -331 C ATOM 548 CE LYS A 258 38.403 25.370 -17.138 1.00 63.25 C ANISOU 548 CE LYS A 258 10012 7143 6877 -1028 -567 -352 C ATOM 549 NZ LYS A 258 38.562 26.548 -16.230 1.00 69.04 N ANISOU 549 NZ LYS A 258 10891 7804 7537 -1031 -617 -341 N ATOM 550 N PRO A 259 34.127 21.223 -19.696 1.00 46.94 N ANISOU 550 N PRO A 259 7535 5175 5123 -624 -469 -318 N ATOM 551 CA PRO A 259 33.823 20.948 -21.106 1.00 44.27 C ANISOU 551 CA PRO A 259 7193 4839 4790 -660 -459 -320 C ATOM 552 C PRO A 259 34.921 21.469 -22.022 1.00 40.23 C ANISOU 552 C PRO A 259 6742 4326 4216 -824 -458 -334 C ATOM 553 O PRO A 259 35.309 22.633 -21.912 1.00 38.06 O ANISOU 553 O PRO A 259 6612 3993 3857 -890 -496 -334 O ATOM 554 CB PRO A 259 32.528 21.725 -21.338 1.00 47.36 C ANISOU 554 CB PRO A 259 7710 5147 5139 -565 -508 -304 C ATOM 555 CG PRO A 259 31.867 21.731 -20.005 1.00 47.28 C ANISOU 555 CG PRO A 259 7683 5131 5148 -437 -523 -293 C ATOM 556 CD PRO A 259 32.977 21.814 -18.990 1.00 49.07 C ANISOU 556 CD PRO A 259 7886 5382 5375 -492 -512 -300 C ATOM 557 N GLY A 260 35.424 20.603 -22.896 1.00 35.08 N ANISOU 557 N GLY A 260 5984 3743 3603 -890 -417 -348 N ATOM 558 CA GLY A 260 36.524 20.939 -23.777 1.00 33.63 C ANISOU 558 CA GLY A 260 5831 3582 3366 -1050 -410 -366 C ATOM 559 C GLY A 260 37.815 20.229 -23.411 1.00 38.62 C ANISOU 559 C GLY A 260 6332 4320 4021 -1127 -369 -394 C ATOM 560 O GLY A 260 38.712 20.090 -24.243 1.00 46.97 O ANISOU 560 O GLY A 260 7358 5433 5055 -1248 -350 -414 O ATOM 561 N PHE A 261 37.912 19.773 -22.166 1.00 28.83 N ANISOU 561 N PHE A 261 5016 3114 2825 -1053 -356 -397 N ATOM 562 CA PHE A 261 39.130 19.130 -21.676 1.00 24.05 C ANISOU 562 CA PHE A 261 4292 2610 2236 -1110 -322 -429 C ATOM 563 C PHE A 261 39.301 17.712 -22.214 1.00 23.45 C ANISOU 563 C PHE A 261 4056 2626 2229 -1092 -280 -445 C ATOM 564 O PHE A 261 40.423 17.255 -22.421 1.00 21.80 O ANISOU 564 O PHE A 261 3763 2510 2011 -1174 -255 -479 O ATOM 565 CB PHE A 261 39.139 19.108 -20.141 1.00 28.23 C ANISOU 565 CB PHE A 261 4801 3138 2789 -1027 -325 -429 C ATOM 566 CG PHE A 261 40.296 18.353 -19.547 1.00 32.46 C ANISOU 566 CG PHE A 261 5209 3779 3346 -1059 -290 -467 C ATOM 567 CD1 PHE A 261 41.502 18.987 -19.299 1.00 33.70 C ANISOU 567 CD1 PHE A 261 5396 3973 3437 -1176 -292 -496 C ATOM 568 CD2 PHE A 261 40.177 17.008 -19.233 1.00 34.29 C ANISOU 568 CD2 PHE A 261 5298 4074 3656 -973 -257 -477 C ATOM 569 CE1 PHE A 261 42.566 18.295 -18.752 1.00 33.66 C ANISOU 569 CE1 PHE A 261 5270 4072 3445 -1198 -262 -538 C ATOM 570 CE2 PHE A 261 41.239 16.310 -18.685 1.00 31.36 C ANISOU 570 CE2 PHE A 261 4819 3800 3297 -992 -229 -517 C ATOM 571 CZ PHE A 261 42.432 16.955 -18.444 1.00 34.59 C ANISOU 571 CZ PHE A 261 5250 4251 3640 -1101 -232 -550 C ATOM 572 N LEU A 262 38.188 17.018 -22.430 1.00 28.07 N ANISOU 572 N LEU A 262 4598 3188 2877 -982 -274 -422 N ATOM 573 CA LEU A 262 38.234 15.603 -22.791 1.00 27.82 C ANISOU 573 CA LEU A 262 4421 3235 2915 -947 -238 -433 C ATOM 574 C LEU A 262 38.235 15.379 -24.291 1.00 30.87 C ANISOU 574 C LEU A 262 4797 3637 3296 -1010 -231 -433 C ATOM 575 O LEU A 262 37.574 16.093 -25.044 1.00 30.58 O ANISOU 575 O LEU A 262 4860 3527 3232 -1023 -253 -413 O ATOM 576 CB LEU A 262 37.040 14.842 -22.199 1.00 24.47 C ANISOU 576 CB LEU A 262 3948 2789 2563 -800 -231 -409 C ATOM 577 CG LEU A 262 36.934 14.581 -20.693 1.00 25.42 C ANISOU 577 CG LEU A 262 4034 2912 2712 -711 -227 -409 C ATOM 578 CD1 LEU A 262 35.623 13.882 -20.376 1.00 25.31 C ANISOU 578 CD1 LEU A 262 3982 2876 2760 -582 -222 -383 C ATOM 579 CD2 LEU A 262 38.098 13.753 -20.195 1.00 22.16 C ANISOU 579 CD2 LEU A 262 3514 2592 2315 -738 -199 -445 C ATOM 580 N ASP A 263 38.980 14.370 -24.717 1.00 34.45 N ANISOU 580 N ASP A 263 5129 4185 3774 -1043 -202 -458 N ATOM 581 CA ASP A 263 38.810 13.819 -26.047 1.00 32.92 C ANISOU 581 CA ASP A 263 4896 4013 3599 -1068 -191 -455 C ATOM 582 C ASP A 263 37.660 12.826 -25.920 1.00 27.64 C ANISOU 582 C ASP A 263 4165 3327 3009 -937 -181 -431 C ATOM 583 O ASP A 263 37.874 11.662 -25.579 1.00 31.31 O ANISOU 583 O ASP A 263 4519 3857 3520 -889 -159 -443 O ATOM 584 CB ASP A 263 40.098 13.116 -26.488 1.00 42.49 C ANISOU 584 CB ASP A 263 6002 5343 4800 -1149 -169 -495 C ATOM 585 CG ASP A 263 40.043 12.620 -27.928 1.00 48.91 C ANISOU 585 CG ASP A 263 6777 6183 5624 -1186 -161 -493 C ATOM 586 OD1 ASP A 263 38.987 12.765 -28.586 1.00 50.76 O ANISOU 586 OD1 ASP A 263 7063 6343 5881 -1147 -170 -461 O ATOM 587 OD2 ASP A 263 41.068 12.083 -28.401 1.00 48.75 O ANISOU 587 OD2 ASP A 263 6673 6263 5588 -1252 -147 -527 O ATOM 588 N LEU A 264 36.438 13.293 -26.164 1.00 23.10 N ANISOU 588 N LEU A 264 3668 2667 2442 -879 -198 -399 N ATOM 589 CA LEU A 264 35.242 12.484 -25.914 1.00 22.61 C ANISOU 589 CA LEU A 264 3558 2589 2446 -756 -189 -376 C ATOM 590 C LEU A 264 35.268 11.069 -26.498 1.00 31.56 C ANISOU 590 C LEU A 264 4568 3787 3635 -735 -162 -380 C ATOM 591 O LEU A 264 34.740 10.137 -25.893 1.00 34.94 O ANISOU 591 O LEU A 264 4928 4233 4114 -648 -147 -372 O ATOM 592 CB LEU A 264 33.972 13.206 -26.387 1.00 17.83 C ANISOU 592 CB LEU A 264 3049 1897 1829 -708 -213 -350 C ATOM 593 CG LEU A 264 33.430 14.267 -25.434 1.00 25.57 C ANISOU 593 CG LEU A 264 4134 2808 2772 -658 -244 -339 C ATOM 594 CD1 LEU A 264 32.084 14.773 -25.916 1.00 26.23 C ANISOU 594 CD1 LEU A 264 4297 2823 2847 -588 -268 -320 C ATOM 595 CD2 LEU A 264 33.330 13.715 -24.012 1.00 25.00 C ANISOU 595 CD2 LEU A 264 3997 2763 2738 -578 -232 -338 C ATOM 596 N LYS A 265 35.851 10.902 -27.678 1.00 25.70 N ANISOU 596 N LYS A 265 3803 3080 2881 -814 -156 -391 N ATOM 597 CA LYS A 265 35.834 9.585 -28.303 1.00 24.60 C ANISOU 597 CA LYS A 265 3557 2998 2790 -790 -136 -393 C ATOM 598 C LYS A 265 36.644 8.566 -27.504 1.00 16.68 C ANISOU 598 C LYS A 265 2454 2077 1806 -768 -119 -419 C ATOM 599 O LYS A 265 36.492 7.366 -27.692 1.00 19.36 O ANISOU 599 O LYS A 265 2712 2456 2188 -721 -106 -418 O ATOM 600 CB LYS A 265 36.277 9.645 -29.773 1.00 21.03 C ANISOU 600 CB LYS A 265 3103 2568 2320 -875 -136 -400 C ATOM 601 CG LYS A 265 37.695 10.095 -30.021 1.00 21.02 C ANISOU 601 CG LYS A 265 3101 2627 2259 -994 -137 -434 C ATOM 602 CD LYS A 265 37.875 10.411 -31.504 1.00 29.27 C ANISOU 602 CD LYS A 265 4172 3671 3279 -1079 -141 -433 C ATOM 603 CE LYS A 265 39.312 10.748 -31.854 1.00 32.22 C ANISOU 603 CE LYS A 265 4529 4122 3589 -1207 -140 -470 C ATOM 604 NZ LYS A 265 39.858 11.848 -31.026 1.00 40.65 N ANISOU 604 NZ LYS A 265 5677 5172 4595 -1269 -151 -484 N ATOM 605 N GLU A 266 37.479 9.060 -26.596 1.00 14.62 N ANISOU 605 N GLU A 266 2208 1837 1509 -800 -123 -442 N ATOM 606 CA GLU A 266 38.281 8.211 -25.722 1.00 22.57 C ANISOU 606 CA GLU A 266 3133 2919 2525 -774 -110 -473 C ATOM 607 C GLU A 266 37.472 7.718 -24.534 1.00 18.08 C ANISOU 607 C GLU A 266 2553 2316 2000 -662 -105 -456 C ATOM 608 O GLU A 266 37.877 6.779 -23.847 1.00 14.76 O ANISOU 608 O GLU A 266 2066 1947 1597 -617 -94 -476 O ATOM 609 CB GLU A 266 39.502 8.981 -25.198 1.00 31.18 C ANISOU 609 CB GLU A 266 4242 4049 3556 -853 -115 -508 C ATOM 610 CG GLU A 266 40.599 9.162 -26.219 1.00 44.35 C ANISOU 610 CG GLU A 266 5888 5790 5175 -969 -115 -540 C ATOM 611 CD GLU A 266 41.018 7.845 -26.841 1.00 58.67 C ANISOU 611 CD GLU A 266 7591 7691 7009 -951 -104 -561 C ATOM 612 OE1 GLU A 266 41.696 7.048 -26.156 1.00 67.90 O ANISOU 612 OE1 GLU A 266 8686 8934 8179 -914 -97 -596 O ATOM 613 OE2 GLU A 266 40.666 7.609 -28.016 1.00 59.31 O ANISOU 613 OE2 GLU A 266 7665 7766 7105 -969 -104 -545 O ATOM 614 N PHE A 267 36.330 8.356 -24.300 1.00 16.49 N ANISOU 614 N PHE A 267 2422 2032 1810 -617 -114 -421 N ATOM 615 CA PHE A 267 35.551 8.128 -23.085 1.00 15.68 C ANISOU 615 CA PHE A 267 2322 1898 1738 -520 -112 -405 C ATOM 616 C PHE A 267 34.115 7.633 -23.303 1.00 11.07 C ANISOU 616 C PHE A 267 1733 1277 1198 -442 -107 -371 C ATOM 617 O PHE A 267 33.427 7.285 -22.347 1.00 12.19 O ANISOU 617 O PHE A 267 1864 1403 1365 -364 -102 -359 O ATOM 618 CB PHE A 267 35.551 9.400 -22.234 1.00 11.90 C ANISOU 618 CB PHE A 267 1929 1368 1223 -525 -130 -402 C ATOM 619 CG PHE A 267 36.854 9.649 -21.533 1.00 14.32 C ANISOU 619 CG PHE A 267 2226 1720 1497 -575 -130 -437 C ATOM 620 CD1 PHE A 267 37.030 9.264 -20.214 1.00 17.97 C ANISOU 620 CD1 PHE A 267 2657 2195 1975 -513 -122 -448 C ATOM 621 CD2 PHE A 267 37.907 10.262 -22.195 1.00 17.06 C ANISOU 621 CD2 PHE A 267 2593 2098 1792 -685 -135 -461 C ATOM 622 CE1 PHE A 267 38.232 9.485 -19.565 1.00 21.96 C ANISOU 622 CE1 PHE A 267 3150 2746 2449 -554 -121 -484 C ATOM 623 CE2 PHE A 267 39.113 10.486 -21.553 1.00 21.62 C ANISOU 623 CE2 PHE A 267 3153 2727 2333 -735 -133 -498 C ATOM 624 CZ PHE A 267 39.279 10.094 -20.239 1.00 21.72 C ANISOU 624 CZ PHE A 267 3133 2754 2365 -666 -126 -510 C ATOM 625 N LEU A 268 33.673 7.581 -24.553 1.00 11.03 N ANISOU 625 N LEU A 268 1731 1260 1199 -465 -108 -358 N ATOM 626 CA LEU A 268 32.305 7.170 -24.853 1.00 10.75 C ANISOU 626 CA LEU A 268 1690 1196 1200 -398 -104 -330 C ATOM 627 C LEU A 268 32.217 6.228 -26.045 1.00 13.79 C ANISOU 627 C LEU A 268 2017 1611 1612 -413 -92 -326 C ATOM 628 O LEU A 268 33.051 6.294 -26.952 1.00 12.10 O ANISOU 628 O LEU A 268 1793 1423 1381 -485 -94 -340 O ATOM 629 CB LEU A 268 31.453 8.404 -25.146 1.00 16.63 C ANISOU 629 CB LEU A 268 2530 1873 1917 -389 -126 -313 C ATOM 630 CG LEU A 268 31.209 9.363 -23.979 1.00 17.27 C ANISOU 630 CG LEU A 268 2679 1913 1970 -351 -144 -310 C ATOM 631 CD1 LEU A 268 30.732 10.718 -24.500 1.00 21.06 C ANISOU 631 CD1 LEU A 268 3273 2327 2402 -364 -176 -303 C ATOM 632 CD2 LEU A 268 30.196 8.747 -23.042 1.00 10.99 C ANISOU 632 CD2 LEU A 268 1846 1121 1209 -253 -134 -296 C ATOM 633 N PRO A 269 31.204 5.342 -26.044 1.00 13.57 N ANISOU 633 N PRO A 269 1949 1583 1624 -349 -79 -307 N ATOM 634 CA PRO A 269 30.812 4.612 -27.255 1.00 15.09 C ANISOU 634 CA PRO A 269 2103 1789 1843 -355 -72 -296 C ATOM 635 C PRO A 269 30.514 5.631 -28.361 1.00 16.36 C ANISOU 635 C PRO A 269 2326 1907 1982 -393 -86 -289 C ATOM 636 O PRO A 269 29.957 6.686 -28.063 1.00 16.29 O ANISOU 636 O PRO A 269 2391 1850 1949 -374 -101 -284 O ATOM 637 CB PRO A 269 29.518 3.904 -26.832 1.00 11.88 C ANISOU 637 CB PRO A 269 1672 1374 1469 -277 -59 -274 C ATOM 638 CG PRO A 269 29.618 3.794 -25.345 1.00 11.41 C ANISOU 638 CG PRO A 269 1609 1320 1407 -237 -55 -280 C ATOM 639 CD PRO A 269 30.363 4.996 -24.885 1.00 13.83 C ANISOU 639 CD PRO A 269 1973 1607 1676 -270 -72 -295 C ATOM 640 N LYS A 270 30.884 5.332 -29.603 1.00 18.90 N ANISOU 640 N LYS A 270 2625 2247 2310 -441 -85 -291 N ATOM 641 CA LYS A 270 30.788 6.317 -30.687 1.00 25.14 C ANISOU 641 CA LYS A 270 3482 2998 3074 -488 -99 -289 C ATOM 642 C LYS A 270 29.401 6.939 -30.810 1.00 20.25 C ANISOU 642 C LYS A 270 2922 2319 2454 -429 -108 -272 C ATOM 643 O LYS A 270 29.270 8.123 -31.109 1.00 23.16 O ANISOU 643 O LYS A 270 3382 2636 2781 -449 -129 -275 O ATOM 644 CB LYS A 270 31.233 5.707 -32.028 1.00 32.11 C ANISOU 644 CB LYS A 270 4318 3912 3972 -536 -93 -292 C ATOM 645 CG LYS A 270 30.408 4.511 -32.472 1.00 41.07 C ANISOU 645 CG LYS A 270 5386 5061 5157 -480 -79 -274 C ATOM 646 CD LYS A 270 31.254 3.533 -33.280 1.00 51.45 C ANISOU 646 CD LYS A 270 6629 6433 6486 -518 -74 -282 C ATOM 647 CE LYS A 270 30.586 2.162 -33.376 1.00 52.24 C ANISOU 647 CE LYS A 270 6663 6554 6632 -459 -62 -265 C ATOM 648 NZ LYS A 270 31.484 1.142 -33.997 1.00 47.53 N ANISOU 648 NZ LYS A 270 5999 6017 6042 -484 -63 -275 N ATOM 649 N GLU A 271 28.378 6.126 -30.565 1.00 19.08 N ANISOU 649 N GLU A 271 2726 2181 2344 -356 -95 -258 N ATOM 650 CA GLU A 271 26.973 6.538 -30.568 1.00 25.38 C ANISOU 650 CA GLU A 271 3560 2943 3139 -286 -102 -247 C ATOM 651 C GLU A 271 26.661 7.820 -29.771 1.00 26.54 C ANISOU 651 C GLU A 271 3798 3046 3239 -257 -126 -253 C ATOM 652 O GLU A 271 25.678 8.506 -30.059 1.00 24.26 O ANISOU 652 O GLU A 271 3567 2723 2929 -211 -142 -253 O ATOM 653 CB GLU A 271 26.137 5.394 -29.983 1.00 25.71 C ANISOU 653 CB GLU A 271 3526 3022 3220 -222 -80 -236 C ATOM 654 CG GLU A 271 26.967 4.120 -29.716 1.00 20.50 C ANISOU 654 CG GLU A 271 2787 2412 2591 -247 -61 -236 C ATOM 655 CD GLU A 271 26.149 3.045 -29.049 1.00 29.08 C ANISOU 655 CD GLU A 271 3816 3526 3706 -192 -43 -223 C ATOM 656 OE1 GLU A 271 26.618 1.895 -28.949 1.00 44.52 O ANISOU 656 OE1 GLU A 271 5716 5516 5683 -202 -30 -222 O ATOM 657 OE2 GLU A 271 25.023 3.351 -28.633 1.00 36.72 O ANISOU 657 OE2 GLU A 271 4800 4484 4667 -138 -42 -217 O ATOM 658 N TYR A 272 27.476 8.133 -28.766 1.00 18.80 N ANISOU 658 N TYR A 272 2833 2070 2241 -278 -130 -261 N ATOM 659 CA TYR A 272 27.142 9.219 -27.840 1.00 18.39 C ANISOU 659 CA TYR A 272 2860 1979 2147 -240 -155 -263 C ATOM 660 C TYR A 272 28.118 10.392 -27.858 1.00 18.60 C ANISOU 660 C TYR A 272 2979 1968 2120 -310 -179 -275 C ATOM 661 O TYR A 272 27.958 11.344 -27.095 1.00 21.62 O ANISOU 661 O TYR A 272 3439 2313 2462 -284 -203 -276 O ATOM 662 CB TYR A 272 27.010 8.693 -26.404 1.00 18.64 C ANISOU 662 CB TYR A 272 2843 2040 2198 -187 -142 -260 C ATOM 663 CG TYR A 272 26.069 7.509 -26.252 1.00 20.20 C ANISOU 663 CG TYR A 272 2956 2278 2441 -128 -118 -249 C ATOM 664 CD1 TYR A 272 26.525 6.299 -25.745 1.00 17.61 C ANISOU 664 CD1 TYR A 272 2546 1995 2149 -135 -92 -247 C ATOM 665 CD2 TYR A 272 24.730 7.605 -26.614 1.00 15.75 C ANISOU 665 CD2 TYR A 272 2399 1709 1874 -68 -122 -243 C ATOM 666 CE1 TYR A 272 25.680 5.219 -25.598 1.00 22.34 C ANISOU 666 CE1 TYR A 272 3080 2628 2782 -92 -71 -236 C ATOM 667 CE2 TYR A 272 23.873 6.533 -26.471 1.00 12.22 C ANISOU 667 CE2 TYR A 272 1876 1305 1462 -25 -98 -234 C ATOM 668 CZ TYR A 272 24.355 5.338 -25.965 1.00 18.95 C ANISOU 668 CZ TYR A 272 2655 2196 2350 -42 -72 -229 C ATOM 669 OH TYR A 272 23.515 4.260 -25.816 1.00 13.58 O ANISOU 669 OH TYR A 272 1909 1554 1696 -10 -49 -219 O ATOM 670 N ILE A 273 29.119 10.326 -28.726 1.00 14.63 N ANISOU 670 N ILE A 273 2470 1477 1612 -401 -173 -283 N ATOM 671 CA ILE A 273 30.133 11.371 -28.796 1.00 21.44 C ANISOU 671 CA ILE A 273 3414 2314 2418 -486 -193 -295 C ATOM 672 C ILE A 273 29.535 12.756 -29.051 1.00 27.31 C ANISOU 672 C ILE A 273 4297 2977 3101 -475 -230 -294 C ATOM 673 O ILE A 273 29.918 13.726 -28.406 1.00 25.65 O ANISOU 673 O ILE A 273 4173 2733 2840 -497 -254 -299 O ATOM 674 CB ILE A 273 31.204 11.050 -29.858 1.00 21.65 C ANISOU 674 CB ILE A 273 3406 2376 2444 -589 -180 -307 C ATOM 675 CG1 ILE A 273 31.977 9.797 -29.449 1.00 21.89 C ANISOU 675 CG1 ILE A 273 3314 2488 2517 -597 -152 -316 C ATOM 676 CG2 ILE A 273 32.165 12.233 -30.038 1.00 19.37 C ANISOU 676 CG2 ILE A 273 3213 2060 2085 -690 -201 -321 C ATOM 677 CD1 ILE A 273 32.943 9.298 -30.505 1.00 21.89 C ANISOU 677 CD1 ILE A 273 3260 2540 2517 -680 -141 -330 C ATOM 678 N LYS A 274 28.580 12.833 -29.971 1.00 35.67 N ANISOU 678 N LYS A 274 5383 4007 4162 -436 -237 -288 N ATOM 679 CA LYS A 274 28.000 14.114 -30.369 1.00 42.40 C ANISOU 679 CA LYS A 274 6378 4781 4949 -420 -277 -292 C ATOM 680 C LYS A 274 26.687 14.459 -29.663 1.00 37.12 C ANISOU 680 C LYS A 274 5746 4091 4269 -296 -299 -290 C ATOM 681 O LYS A 274 26.035 15.436 -30.016 1.00 40.07 O ANISOU 681 O LYS A 274 6235 4404 4586 -259 -335 -296 O ATOM 682 CB LYS A 274 27.815 14.171 -31.894 1.00 47.40 C ANISOU 682 CB LYS A 274 7039 5391 5578 -455 -278 -294 C ATOM 683 CG LYS A 274 29.118 14.388 -32.665 1.00 51.83 C ANISOU 683 CG LYS A 274 7622 5956 6116 -589 -273 -301 C ATOM 684 CD LYS A 274 28.893 14.604 -34.163 1.00 57.18 C ANISOU 684 CD LYS A 274 8348 6599 6780 -622 -279 -304 C ATOM 685 CE LYS A 274 28.842 13.285 -34.930 1.00 61.18 C ANISOU 685 CE LYS A 274 8718 7166 7361 -618 -243 -298 C ATOM 686 NZ LYS A 274 28.942 13.493 -36.405 1.00 59.68 N ANISOU 686 NZ LYS A 274 8569 6949 7158 -674 -246 -301 N ATOM 687 N GLN A 275 26.306 13.674 -28.659 1.00 30.02 N ANISOU 687 N GLN A 275 4752 3241 3415 -230 -278 -283 N ATOM 688 CA GLN A 275 25.060 13.935 -27.941 1.00 24.51 C ANISOU 688 CA GLN A 275 4072 2537 2702 -114 -297 -283 C ATOM 689 C GLN A 275 25.186 15.085 -26.934 1.00 36.10 C ANISOU 689 C GLN A 275 5647 3962 4109 -90 -336 -287 C ATOM 690 O GLN A 275 26.170 15.189 -26.199 1.00 30.36 O ANISOU 690 O GLN A 275 4918 3237 3379 -143 -332 -284 O ATOM 691 CB GLN A 275 24.523 12.670 -27.266 1.00 25.81 C ANISOU 691 CB GLN A 275 4102 2774 2933 -56 -261 -275 C ATOM 692 CG GLN A 275 23.197 12.887 -26.542 1.00 33.73 C ANISOU 692 CG GLN A 275 5111 3787 3916 60 -277 -278 C ATOM 693 CD GLN A 275 22.505 11.589 -26.180 1.00 44.07 C ANISOU 693 CD GLN A 275 6292 5169 5285 105 -239 -271 C ATOM 694 OE1 GLN A 275 22.692 10.566 -26.836 1.00 45.28 O ANISOU 694 OE1 GLN A 275 6363 5352 5487 65 -206 -264 O ATOM 695 NE2 GLN A 275 21.693 11.628 -25.133 1.00 51.36 N ANISOU 695 NE2 GLN A 275 7199 6119 6197 188 -245 -272 N ATOM 696 N ARG A 276 24.160 15.934 -26.914 1.00 40.87 N ANISOU 696 N ARG A 276 6343 4528 4658 -4 -376 -295 N ATOM 697 CA AARG A 276 24.151 17.150 -26.105 0.50 42.29 C ANISOU 697 CA AARG A 276 6647 4656 4767 30 -425 -300 C ATOM 698 CA BARG A 276 24.154 17.148 -26.100 0.50 42.30 C ANISOU 698 CA BARG A 276 6648 4656 4767 30 -425 -300 C ATOM 699 C ARG A 276 24.478 16.894 -24.631 1.00 36.35 C ANISOU 699 C ARG A 276 5839 3936 4037 52 -415 -291 C ATOM 700 O ARG A 276 23.895 16.012 -24.001 1.00 31.54 O ANISOU 700 O ARG A 276 5119 3387 3478 114 -388 -286 O ATOM 701 CB AARG A 276 22.789 17.845 -26.235 0.50 44.68 C ANISOU 701 CB AARG A 276 7029 4934 5012 149 -468 -315 C ATOM 702 CB BARG A 276 22.798 17.853 -26.198 0.50 44.73 C ANISOU 702 CB BARG A 276 7036 4941 5019 150 -468 -315 C ATOM 703 CG AARG A 276 22.748 19.269 -25.703 0.50 47.18 C ANISOU 703 CG AARG A 276 7511 5181 5235 186 -532 -323 C ATOM 704 CG BARG A 276 22.698 19.096 -25.325 0.50 47.17 C ANISOU 704 CG BARG A 276 7479 5198 5247 201 -526 -320 C ATOM 705 CD AARG A 276 21.422 19.954 -26.029 0.50 48.34 C ANISOU 705 CD AARG A 276 7745 5307 5315 308 -580 -345 C ATOM 706 CD BARG A 276 21.258 19.428 -24.967 0.50 48.44 C ANISOU 706 CD BARG A 276 7663 5375 5366 350 -561 -337 C ATOM 707 NE AARG A 276 21.301 20.290 -27.446 0.50 47.60 N ANISOU 707 NE AARG A 276 7728 5166 5190 277 -592 -359 N ATOM 708 NE BARG A 276 21.191 20.487 -23.963 0.50 46.48 N ANISOU 708 NE BARG A 276 7527 5087 5046 409 -615 -340 N ATOM 709 CZ AARG A 276 20.452 19.707 -28.287 0.50 48.47 C ANISOU 709 CZ AARG A 276 7776 5313 5328 324 -574 -372 C ATOM 710 CZ BARG A 276 21.379 20.293 -22.661 0.50 46.06 C ANISOU 710 CZ BARG A 276 7419 5065 5016 434 -608 -327 C ATOM 711 NH1AARG A 276 19.632 18.756 -27.861 0.50 45.51 N ANISOU 711 NH1AARG A 276 7258 5026 5009 397 -542 -373 N ATOM 712 NH1BARG A 276 21.644 19.077 -22.201 0.50 42.65 N ANISOU 712 NH1BARG A 276 6828 4704 4674 404 -548 -313 N ATOM 713 NH2AARG A 276 20.418 20.083 -29.559 0.50 50.87 N ANISOU 713 NH2AARG A 276 8161 5566 5601 295 -588 -384 N ATOM 714 NH2BARG A 276 21.301 21.315 -21.818 0.50 46.83 N ANISOU 714 NH2BARG A 276 7629 5122 5044 491 -663 -330 N ATOM 715 N GLY A 277 25.411 17.676 -24.094 1.00 30.25 N ANISOU 715 N GLY A 277 5148 3122 3224 -4 -436 -289 N ATOM 716 CA GLY A 277 25.753 17.616 -22.682 1.00 37.66 C ANISOU 716 CA GLY A 277 6054 4080 4176 20 -433 -282 C ATOM 717 C GLY A 277 26.507 16.387 -22.196 1.00 35.67 C ANISOU 717 C GLY A 277 5658 3894 4002 -25 -379 -276 C ATOM 718 O GLY A 277 26.667 16.196 -20.985 1.00 32.23 O ANISOU 718 O GLY A 277 5184 3479 3584 9 -373 -272 O ATOM 719 N ALA A 278 26.980 15.562 -23.128 1.00 29.71 N ANISOU 719 N ALA A 278 4829 3171 3289 -97 -343 -278 N ATOM 720 CA ALA A 278 27.733 14.356 -22.779 1.00 22.78 C ANISOU 720 CA ALA A 278 3823 2356 2477 -136 -296 -277 C ATOM 721 C ALA A 278 28.831 14.645 -21.757 1.00 16.31 C ANISOU 721 C ALA A 278 3014 1537 1646 -178 -298 -282 C ATOM 722 O ALA A 278 28.899 14.014 -20.694 1.00 16.04 O ANISOU 722 O ALA A 278 2908 1539 1649 -137 -278 -281 O ATOM 723 CB ALA A 278 28.331 13.731 -24.028 1.00 20.80 C ANISOU 723 CB ALA A 278 3524 2129 2252 -222 -270 -282 C ATOM 724 N GLU A 279 29.680 15.610 -22.085 1.00 15.28 N ANISOU 724 N GLU A 279 2978 1367 1460 -263 -321 -290 N ATOM 725 CA GLU A 279 30.830 15.938 -21.261 1.00 19.11 C ANISOU 725 CA GLU A 279 3476 1857 1927 -320 -321 -299 C ATOM 726 C GLU A 279 30.398 16.406 -19.872 1.00 24.47 C ANISOU 726 C GLU A 279 4190 2513 2594 -233 -344 -291 C ATOM 727 O GLU A 279 30.993 16.019 -18.863 1.00 20.99 O ANISOU 727 O GLU A 279 3692 2104 2179 -229 -326 -296 O ATOM 728 CB GLU A 279 31.693 16.999 -21.947 1.00 24.21 C ANISOU 728 CB GLU A 279 4234 2463 2503 -433 -346 -307 C ATOM 729 CG GLU A 279 33.026 17.268 -21.252 1.00 30.93 C ANISOU 729 CG GLU A 279 5085 3334 3331 -515 -341 -322 C ATOM 730 CD GLU A 279 34.136 17.626 -22.232 1.00 36.21 C ANISOU 730 CD GLU A 279 5788 4015 3956 -660 -337 -339 C ATOM 731 OE1 GLU A 279 33.823 18.008 -23.375 1.00 43.15 O ANISOU 731 OE1 GLU A 279 6732 4858 4806 -696 -351 -334 O ATOM 732 OE2 GLU A 279 35.324 17.516 -21.862 1.00 39.84 O ANISOU 732 OE2 GLU A 279 6208 4523 4408 -737 -321 -359 O ATOM 733 N LYS A 280 29.355 17.226 -19.819 1.00 22.90 N ANISOU 733 N LYS A 280 4085 2262 2354 -157 -384 -281 N ATOM 734 CA LYS A 280 28.874 17.732 -18.541 1.00 24.72 C ANISOU 734 CA LYS A 280 4353 2473 2567 -66 -411 -274 C ATOM 735 C LYS A 280 28.402 16.579 -17.656 1.00 18.95 C ANISOU 735 C LYS A 280 3490 1803 1907 13 -375 -270 C ATOM 736 O LYS A 280 28.634 16.568 -16.447 1.00 17.75 O ANISOU 736 O LYS A 280 3319 1658 1765 48 -375 -268 O ATOM 737 CB LYS A 280 27.760 18.758 -18.763 1.00 39.37 C ANISOU 737 CB LYS A 280 6330 4270 4358 13 -465 -270 C ATOM 738 CG LYS A 280 27.173 19.327 -17.483 1.00 54.32 C ANISOU 738 CG LYS A 280 8267 6147 6226 118 -500 -264 C ATOM 739 CD LYS A 280 26.469 20.659 -17.726 1.00 59.07 C ANISOU 739 CD LYS A 280 9030 6677 6735 173 -568 -265 C ATOM 740 CE LYS A 280 25.742 21.132 -16.468 1.00 60.70 C ANISOU 740 CE LYS A 280 9267 6879 6916 296 -605 -261 C ATOM 741 NZ LYS A 280 26.631 21.142 -15.266 1.00 62.07 N ANISOU 741 NZ LYS A 280 9419 7055 7110 272 -596 -253 N ATOM 742 N ARG A 281 27.747 15.599 -18.269 1.00 15.79 N ANISOU 742 N ARG A 281 3002 1446 1553 36 -345 -268 N ATOM 743 CA ARG A 281 27.317 14.416 -17.544 1.00 16.52 C ANISOU 743 CA ARG A 281 2975 1596 1707 95 -309 -264 C ATOM 744 C ARG A 281 28.515 13.626 -17.043 1.00 14.38 C ANISOU 744 C ARG A 281 2627 1360 1477 37 -273 -272 C ATOM 745 O ARG A 281 28.551 13.220 -15.888 1.00 18.61 O ANISOU 745 O ARG A 281 3117 1916 2037 83 -261 -272 O ATOM 746 CB ARG A 281 26.419 13.531 -18.411 1.00 21.87 C ANISOU 746 CB ARG A 281 3582 2310 2419 118 -285 -261 C ATOM 747 CG ARG A 281 24.935 13.795 -18.237 1.00 34.73 C ANISOU 747 CG ARG A 281 5226 3943 4026 223 -306 -257 C ATOM 748 CD ARG A 281 24.109 12.781 -19.008 1.00 48.26 C ANISOU 748 CD ARG A 281 6854 5704 5777 238 -275 -256 C ATOM 749 NE ARG A 281 22.699 12.793 -18.621 1.00 61.51 N ANISOU 749 NE ARG A 281 8518 7414 7441 340 -286 -257 N ATOM 750 CZ ARG A 281 22.192 12.077 -17.622 1.00 71.20 C ANISOU 750 CZ ARG A 281 9668 8691 8695 392 -264 -252 C ATOM 751 NH1 ARG A 281 22.979 11.293 -16.897 1.00 69.56 N ANISOU 751 NH1 ARG A 281 9400 8498 8530 356 -233 -246 N ATOM 752 NH2 ARG A 281 20.896 12.147 -17.342 1.00 79.20 N ANISOU 752 NH2 ARG A 281 10665 9742 9685 479 -275 -257 N ATOM 753 N ILE A 282 29.504 13.420 -17.906 1.00 16.68 N ANISOU 753 N ILE A 282 2904 1662 1770 -61 -258 -284 N ATOM 754 CA ILE A 282 30.697 12.684 -17.509 1.00 16.49 C ANISOU 754 CA ILE A 282 2809 1682 1776 -113 -229 -300 C ATOM 755 C ILE A 282 31.368 13.334 -16.294 1.00 12.22 C ANISOU 755 C ILE A 282 2307 1124 1212 -109 -243 -307 C ATOM 756 O ILE A 282 31.731 12.652 -15.333 1.00 11.97 O ANISOU 756 O ILE A 282 2211 1124 1213 -80 -222 -315 O ATOM 757 CB ILE A 282 31.707 12.573 -18.668 1.00 15.27 C ANISOU 757 CB ILE A 282 2645 1547 1611 -223 -218 -315 C ATOM 758 CG1 ILE A 282 31.177 11.625 -19.744 1.00 14.65 C ANISOU 758 CG1 ILE A 282 2501 1496 1569 -222 -196 -310 C ATOM 759 CG2 ILE A 282 33.070 12.103 -18.153 1.00 15.62 C ANISOU 759 CG2 ILE A 282 2633 1640 1664 -276 -197 -341 C ATOM 760 CD1 ILE A 282 32.001 11.649 -21.027 1.00 14.78 C ANISOU 760 CD1 ILE A 282 2519 1528 1570 -324 -192 -322 C ATOM 761 N PHE A 283 31.522 14.653 -16.337 1.00 12.67 N ANISOU 761 N PHE A 283 2478 1127 1210 -136 -281 -304 N ATOM 762 CA PHE A 283 32.163 15.378 -15.237 1.00 12.90 C ANISOU 762 CA PHE A 283 2556 1134 1211 -138 -300 -309 C ATOM 763 C PHE A 283 31.361 15.377 -13.932 1.00 16.25 C ANISOU 763 C PHE A 283 2974 1547 1652 -22 -309 -296 C ATOM 764 O PHE A 283 31.944 15.413 -12.846 1.00 16.12 O ANISOU 764 O PHE A 283 2946 1536 1643 -9 -306 -303 O ATOM 765 CB PHE A 283 32.547 16.797 -15.652 1.00 16.05 C ANISOU 765 CB PHE A 283 3091 1474 1534 -205 -341 -309 C ATOM 766 CG PHE A 283 33.782 16.854 -16.489 1.00 19.91 C ANISOU 766 CG PHE A 283 3579 1988 2000 -338 -328 -329 C ATOM 767 CD1 PHE A 283 34.882 16.083 -16.159 1.00 18.14 C ANISOU 767 CD1 PHE A 283 3259 1831 1804 -385 -293 -354 C ATOM 768 CD2 PHE A 283 33.849 17.668 -17.601 1.00 27.51 C ANISOU 768 CD2 PHE A 283 4637 2910 2905 -415 -352 -327 C ATOM 769 CE1 PHE A 283 36.030 16.124 -16.928 1.00 20.07 C ANISOU 769 CE1 PHE A 283 3494 2113 2020 -508 -281 -379 C ATOM 770 CE2 PHE A 283 34.991 17.713 -18.377 1.00 26.51 C ANISOU 770 CE2 PHE A 283 4505 2815 2753 -545 -338 -348 C ATOM 771 CZ PHE A 283 36.084 16.947 -18.040 1.00 22.24 C ANISOU 771 CZ PHE A 283 3859 2351 2239 -592 -303 -374 C ATOM 772 N GLN A 284 30.034 15.330 -14.017 1.00 16.69 N ANISOU 772 N GLN A 284 3034 1593 1713 63 -321 -279 N ATOM 773 CA AGLN A 284 29.212 15.177 -12.820 0.33 16.44 C ANISOU 773 CA AGLN A 284 2978 1568 1699 173 -325 -269 C ATOM 774 CA BGLN A 284 29.239 15.193 -12.803 0.67 14.34 C ANISOU 774 CA BGLN A 284 2714 1302 1433 172 -325 -269 C ATOM 775 C GLN A 284 29.504 13.834 -12.160 1.00 16.10 C ANISOU 775 C GLN A 284 2816 1581 1721 186 -277 -276 C ATOM 776 O GLN A 284 29.651 13.738 -10.951 1.00 13.42 O ANISOU 776 O GLN A 284 2459 1245 1395 233 -274 -277 O ATOM 777 CB AGLN A 284 27.725 15.270 -13.164 0.33 19.90 C ANISOU 777 CB AGLN A 284 3430 2006 2126 254 -342 -256 C ATOM 778 CB BGLN A 284 27.745 15.376 -13.081 0.67 20.23 C ANISOU 778 CB BGLN A 284 3480 2044 2164 257 -346 -256 C ATOM 779 CG AGLN A 284 27.198 16.685 -13.307 0.33 21.61 C ANISOU 779 CG AGLN A 284 3779 2164 2269 291 -401 -251 C ATOM 780 CG BGLN A 284 26.883 15.277 -11.830 0.67 25.39 C ANISOU 780 CG BGLN A 284 4108 2713 2826 368 -353 -247 C ATOM 781 CD AGLN A 284 25.707 16.719 -13.572 0.33 26.55 C ANISOU 781 CD AGLN A 284 4405 2805 2879 385 -419 -246 C ATOM 782 CD BGLN A 284 27.271 16.296 -10.774 0.67 27.43 C ANISOU 782 CD BGLN A 284 4446 2928 3048 397 -390 -244 C ATOM 783 OE1AGLN A 284 25.115 15.721 -13.985 0.33 29.34 O ANISOU 783 OE1AGLN A 284 4666 3209 3274 398 -384 -247 O ATOM 784 OE1BGLN A 284 27.209 17.506 -11.009 0.67 24.30 O ANISOU 784 OE1BGLN A 284 4166 2479 2588 400 -439 -241 O ATOM 785 NE2AGLN A 284 25.092 17.871 -13.338 0.33 29.68 N ANISOU 785 NE2AGLN A 284 4909 3160 3208 453 -475 -245 N ATOM 786 NE2BGLN A 284 27.675 15.812 -9.599 0.67 21.04 N ANISOU 786 NE2BGLN A 284 3581 2139 2276 422 -369 -245 N ATOM 787 N GLU A 285 29.575 12.784 -12.972 1.00 11.78 N ANISOU 787 N GLU A 285 2193 1074 1210 148 -243 -282 N ATOM 788 CA GLU A 285 29.899 11.461 -12.454 1.00 11.38 C ANISOU 788 CA GLU A 285 2043 1072 1211 157 -201 -291 C ATOM 789 C GLU A 285 31.334 11.420 -11.930 1.00 14.55 C ANISOU 789 C GLU A 285 2433 1483 1613 106 -192 -315 C ATOM 790 O GLU A 285 31.625 10.778 -10.913 1.00 14.73 O ANISOU 790 O GLU A 285 2409 1526 1663 143 -173 -325 O ATOM 791 CB GLU A 285 29.679 10.399 -13.534 1.00 11.15 C ANISOU 791 CB GLU A 285 1947 1079 1211 125 -173 -292 C ATOM 792 CG GLU A 285 28.254 10.363 -14.106 1.00 39.61 C ANISOU 792 CG GLU A 285 5553 4683 4815 172 -179 -273 C ATOM 793 CD GLU A 285 27.194 9.934 -13.088 1.00 41.78 C ANISOU 793 CD GLU A 285 5792 4977 5106 262 -171 -261 C ATOM 794 OE1 GLU A 285 27.537 9.262 -12.093 1.00 37.19 O ANISOU 794 OE1 GLU A 285 5168 4413 4550 282 -151 -267 O ATOM 795 OE2 GLU A 285 26.007 10.271 -13.288 1.00 49.36 O ANISOU 795 OE2 GLU A 285 6769 5938 6047 314 -186 -250 O ATOM 796 N HIS A 286 32.229 12.116 -12.625 1.00 14.00 N ANISOU 796 N HIS A 286 2409 1403 1509 21 -205 -327 N ATOM 797 CA HIS A 286 33.612 12.235 -12.182 1.00 11.78 C ANISOU 797 CA HIS A 286 2121 1139 1214 -35 -200 -355 C ATOM 798 C HIS A 286 33.658 12.891 -10.797 1.00 11.86 C ANISOU 798 C HIS A 286 2174 1119 1215 20 -218 -352 C ATOM 799 O HIS A 286 34.303 12.385 -9.885 1.00 11.70 O ANISOU 799 O HIS A 286 2106 1124 1215 39 -200 -371 O ATOM 800 CB HIS A 286 34.439 13.027 -13.203 1.00 18.64 C ANISOU 800 CB HIS A 286 3044 2003 2036 -145 -214 -367 C ATOM 801 CG HIS A 286 35.903 13.088 -12.883 1.00 15.67 C ANISOU 801 CG HIS A 286 2649 1664 1640 -215 -205 -402 C ATOM 802 ND1 HIS A 286 36.748 14.017 -13.443 1.00 14.23 N ANISOU 802 ND1 HIS A 286 2527 1477 1402 -319 -221 -415 N ATOM 803 CD2 HIS A 286 36.663 12.336 -12.049 1.00 16.08 C ANISOU 803 CD2 HIS A 286 2630 1764 1716 -196 -182 -430 C ATOM 804 CE1 HIS A 286 37.973 13.830 -12.978 1.00 17.69 C ANISOU 804 CE1 HIS A 286 2924 1968 1831 -363 -207 -451 C ATOM 805 NE2 HIS A 286 37.947 12.818 -12.130 1.00 17.32 N ANISOU 805 NE2 HIS A 286 2797 1952 1831 -285 -184 -463 N ATOM 806 N LYS A 287 32.930 13.989 -10.640 1.00 20.04 N ANISOU 806 N LYS A 287 3299 2100 2217 54 -255 -328 N ATOM 807 CA LYS A 287 32.842 14.680 -9.355 1.00 22.55 C ANISOU 807 CA LYS A 287 3663 2383 2521 116 -279 -321 C ATOM 808 C LYS A 287 32.281 13.779 -8.261 1.00 16.36 C ANISOU 808 C LYS A 287 2806 1622 1787 213 -257 -317 C ATOM 809 O LYS A 287 32.740 13.822 -7.126 1.00 17.37 O ANISOU 809 O LYS A 287 2928 1747 1924 245 -255 -325 O ATOM 810 CB LYS A 287 31.977 15.933 -9.480 1.00 19.68 C ANISOU 810 CB LYS A 287 3411 1959 2107 152 -329 -296 C ATOM 811 CG LYS A 287 31.833 16.744 -8.186 1.00 21.87 C ANISOU 811 CG LYS A 287 3748 2198 2364 222 -362 -286 C ATOM 812 CD LYS A 287 31.136 18.069 -8.498 1.00 28.48 C ANISOU 812 CD LYS A 287 4714 2973 3133 247 -420 -267 C ATOM 813 CE LYS A 287 31.125 19.028 -7.317 1.00 35.40 C ANISOU 813 CE LYS A 287 5670 3806 3977 307 -461 -257 C ATOM 814 NZ LYS A 287 30.479 20.330 -7.685 1.00 40.41 N ANISOU 814 NZ LYS A 287 6444 4376 4533 332 -525 -242 N ATOM 815 N ASN A 288 31.280 12.973 -8.602 1.00 17.25 N ANISOU 815 N ASN A 288 2867 1757 1929 255 -239 -304 N ATOM 816 CA ASN A 288 30.695 12.038 -7.641 1.00 17.64 C ANISOU 816 CA ASN A 288 2850 1832 2021 335 -215 -300 C ATOM 817 C ASN A 288 31.714 11.048 -7.073 1.00 24.73 C ANISOU 817 C ASN A 288 3682 2763 2953 318 -181 -327 C ATOM 818 O ASN A 288 31.490 10.466 -6.018 1.00 24.23 O ANISOU 818 O ASN A 288 3583 2707 2915 381 -166 -328 O ATOM 819 CB ASN A 288 29.529 11.261 -8.265 1.00 14.84 C ANISOU 819 CB ASN A 288 2448 1504 1685 362 -199 -286 C ATOM 820 CG ASN A 288 28.286 12.126 -8.480 1.00 28.74 C ANISOU 820 CG ASN A 288 4263 3244 3411 415 -234 -264 C ATOM 821 OD1 ASN A 288 28.094 13.146 -7.819 1.00 24.17 O ANISOU 821 OD1 ASN A 288 3751 2632 2801 461 -270 -257 O ATOM 822 ND2 ASN A 288 27.436 11.711 -9.413 1.00 31.89 N ANISOU 822 ND2 ASN A 288 4637 3665 3814 414 -225 -257 N ATOM 823 N CYS A 289 32.832 10.853 -7.768 1.00 22.42 N ANISOU 823 N CYS A 289 3373 2491 2653 235 -169 -352 N ATOM 824 CA CYS A 289 33.829 9.890 -7.306 1.00 20.20 C ANISOU 824 CA CYS A 289 3031 2250 2396 226 -140 -386 C ATOM 825 C CYS A 289 34.642 10.385 -6.111 1.00 15.09 C ANISOU 825 C CYS A 289 2404 1591 1740 245 -148 -404 C ATOM 826 O CYS A 289 35.302 9.592 -5.429 1.00 16.43 O ANISOU 826 O CYS A 289 2525 1788 1928 266 -126 -433 O ATOM 827 CB CYS A 289 34.767 9.490 -8.443 1.00 17.07 C ANISOU 827 CB CYS A 289 2603 1895 1989 137 -128 -412 C ATOM 828 SG CYS A 289 33.971 8.489 -9.722 1.00 17.97 S ANISOU 828 SG CYS A 289 2672 2033 2125 123 -110 -397 S ATOM 829 N GLY A 290 34.613 11.693 -5.877 1.00 13.42 N ANISOU 829 N GLY A 290 2266 1336 1495 240 -181 -390 N ATOM 830 CA GLY A 290 35.364 12.287 -4.783 1.00 18.93 C ANISOU 830 CA GLY A 290 2991 2019 2181 255 -192 -405 C ATOM 831 C GLY A 290 36.844 11.962 -4.844 1.00 24.72 C ANISOU 831 C GLY A 290 3686 2799 2905 189 -173 -452 C ATOM 832 O GLY A 290 37.487 12.165 -5.881 1.00 19.76 O ANISOU 832 O GLY A 290 3062 2198 2249 97 -174 -468 O ATOM 833 N GLU A 291 37.377 11.438 -3.739 1.00 19.67 N ANISOU 833 N GLU A 291 3010 2177 2287 239 -157 -479 N ATOM 834 CA GLU A 291 38.798 11.110 -3.634 1.00 15.36 C ANISOU 834 CA GLU A 291 2423 1685 1728 193 -141 -532 C ATOM 835 C GLU A 291 39.078 9.618 -3.715 1.00 15.38 C ANISOU 835 C GLU A 291 2346 1742 1757 218 -110 -565 C ATOM 836 O GLU A 291 40.135 9.165 -3.274 1.00 16.91 O ANISOU 836 O GLU A 291 2501 1981 1943 219 -97 -615 O ATOM 837 CB GLU A 291 39.368 11.635 -2.315 1.00 25.76 C ANISOU 837 CB GLU A 291 3761 2985 3041 232 -149 -549 C ATOM 838 CG GLU A 291 39.061 13.099 -2.039 1.00 34.98 C ANISOU 838 CG GLU A 291 5019 4092 4179 222 -186 -515 C ATOM 839 CD GLU A 291 39.921 14.030 -2.863 1.00 51.68 C ANISOU 839 CD GLU A 291 7178 6221 6238 104 -202 -529 C ATOM 840 OE1 GLU A 291 41.138 13.760 -3.000 1.00 57.42 O ANISOU 840 OE1 GLU A 291 7860 7011 6946 42 -185 -579 O ATOM 841 OE2 GLU A 291 39.379 15.034 -3.370 1.00 57.17 O ANISOU 841 OE2 GLU A 291 7954 6866 6901 72 -234 -493 O ATOM 842 N MET A 292 38.157 8.846 -4.285 1.00 20.68 N ANISOU 842 N MET A 292 2995 2409 2453 239 -99 -540 N ATOM 843 CA MET A 292 38.378 7.407 -4.368 1.00 21.85 C ANISOU 843 CA MET A 292 3081 2601 2619 264 -74 -569 C ATOM 844 C MET A 292 39.657 7.100 -5.144 1.00 24.01 C ANISOU 844 C MET A 292 3316 2946 2862 193 -68 -620 C ATOM 845 O MET A 292 40.034 7.826 -6.067 1.00 22.50 O ANISOU 845 O MET A 292 3138 2771 2641 108 -79 -620 O ATOM 846 CB MET A 292 37.167 6.674 -4.961 1.00 26.37 C ANISOU 846 CB MET A 292 3642 3159 3217 285 -65 -532 C ATOM 847 CG MET A 292 37.039 6.729 -6.467 1.00 18.46 C ANISOU 847 CG MET A 292 2634 2177 2203 211 -68 -520 C ATOM 848 SD MET A 292 35.714 5.651 -7.071 1.00 16.82 S ANISOU 848 SD MET A 292 2402 1963 2026 240 -54 -485 S ATOM 849 CE MET A 292 34.360 6.140 -5.993 1.00 10.06 C ANISOU 849 CE MET A 292 1582 1051 1189 320 -61 -441 C ATOM 850 N SER A 293 40.329 6.028 -4.752 1.00 22.59 N ANISOU 850 N SER A 293 3091 2811 2683 231 -53 -667 N ATOM 851 CA SER A 293 41.579 5.647 -5.381 1.00 16.48 C ANISOU 851 CA SER A 293 2271 2118 1873 179 -50 -725 C ATOM 852 C SER A 293 41.330 5.084 -6.769 1.00 16.39 C ANISOU 852 C SER A 293 2234 2135 1858 131 -47 -714 C ATOM 853 O SER A 293 40.188 4.806 -7.145 1.00 11.73 O ANISOU 853 O SER A 293 1658 1501 1297 148 -45 -666 O ATOM 854 CB SER A 293 42.273 4.582 -4.545 1.00 23.23 C ANISOU 854 CB SER A 293 3092 3011 2725 250 -39 -780 C ATOM 855 OG SER A 293 41.606 3.344 -4.683 1.00 24.29 O ANISOU 855 OG SER A 293 3216 3133 2880 303 -30 -769 O ATOM 856 N GLU A 294 42.419 4.905 -7.510 1.00 11.59 N ANISOU 856 N GLU A 294 1585 1607 1212 72 -48 -763 N ATOM 857 CA GLU A 294 42.390 4.293 -8.825 1.00 22.90 C ANISOU 857 CA GLU A 294 2986 3079 2636 29 -48 -762 C ATOM 858 C GLU A 294 41.803 2.889 -8.729 1.00 24.97 C ANISOU 858 C GLU A 294 3232 3330 2924 106 -40 -757 C ATOM 859 O GLU A 294 40.983 2.489 -9.554 1.00 16.51 O ANISOU 859 O GLU A 294 2161 2238 1872 95 -38 -719 O ATOM 860 CB GLU A 294 43.807 4.244 -9.418 1.00 16.33 C ANISOU 860 CB GLU A 294 2103 2350 1750 -34 -51 -828 C ATOM 861 CG GLU A 294 43.901 3.532 -10.759 1.00 25.08 C ANISOU 861 CG GLU A 294 3172 3511 2845 -72 -52 -835 C ATOM 862 CD GLU A 294 45.288 3.627 -11.383 1.00 39.19 C ANISOU 862 CD GLU A 294 4907 5412 4573 -142 -57 -900 C ATOM 863 OE1 GLU A 294 45.964 4.662 -11.197 1.00 44.97 O ANISOU 863 OE1 GLU A 294 5646 6168 5271 -207 -59 -919 O ATOM 864 OE2 GLU A 294 45.698 2.666 -12.066 1.00 42.19 O ANISOU 864 OE2 GLU A 294 5239 5860 4933 -133 -61 -933 O ATOM 865 N ILE A 295 42.223 2.146 -7.711 1.00 24.06 N ANISOU 865 N ILE A 295 3108 3228 2805 182 -36 -797 N ATOM 866 CA ILE A 295 41.749 0.777 -7.526 1.00 24.41 C ANISOU 866 CA ILE A 295 3152 3259 2863 253 -31 -797 C ATOM 867 C ILE A 295 40.257 0.724 -7.197 1.00 19.08 C ANISOU 867 C ILE A 295 2516 2500 2235 285 -22 -729 C ATOM 868 O ILE A 295 39.533 -0.120 -7.727 1.00 16.53 O ANISOU 868 O ILE A 295 2194 2163 1925 294 -19 -704 O ATOM 869 CB ILE A 295 42.568 0.029 -6.448 1.00 17.29 C ANISOU 869 CB ILE A 295 2245 2385 1938 332 -31 -859 C ATOM 870 CG1 ILE A 295 43.861 -0.500 -7.060 1.00 15.65 C ANISOU 870 CG1 ILE A 295 1990 2280 1678 317 -42 -932 C ATOM 871 CG2 ILE A 295 41.760 -1.119 -5.856 1.00 12.11 C ANISOU 871 CG2 ILE A 295 1620 1677 1303 411 -26 -842 C ATOM 872 CD1 ILE A 295 44.915 -0.844 -6.020 1.00 28.40 C ANISOU 872 CD1 ILE A 295 3595 3938 3257 383 -46 -1007 C ATOM 873 N GLU A 296 39.797 1.636 -6.343 1.00 17.28 N ANISOU 873 N GLU A 296 2318 2219 2027 301 -21 -700 N ATOM 874 CA GLU A 296 38.373 1.703 -6.017 1.00 16.16 C ANISOU 874 CA GLU A 296 2208 2010 1922 332 -15 -640 C ATOM 875 C GLU A 296 37.543 1.999 -7.266 1.00 11.75 C ANISOU 875 C GLU A 296 1649 1442 1374 275 -17 -594 C ATOM 876 O GLU A 296 36.523 1.353 -7.520 1.00 11.89 O ANISOU 876 O GLU A 296 1669 1438 1410 292 -9 -561 O ATOM 877 CB GLU A 296 38.106 2.763 -4.949 1.00 17.26 C ANISOU 877 CB GLU A 296 2380 2105 2075 359 -18 -621 C ATOM 878 CG GLU A 296 36.669 2.773 -4.448 1.00 22.08 C ANISOU 878 CG GLU A 296 3015 2658 2715 404 -13 -567 C ATOM 879 CD GLU A 296 36.461 3.684 -3.240 1.00 32.89 C ANISOU 879 CD GLU A 296 4415 3986 4094 448 -20 -553 C ATOM 880 OE1 GLU A 296 37.460 4.085 -2.596 1.00 27.64 O ANISOU 880 OE1 GLU A 296 3753 3331 3416 457 -25 -589 O ATOM 881 OE2 GLU A 296 35.288 3.988 -2.929 1.00 29.23 O ANISOU 881 OE2 GLU A 296 3972 3487 3648 477 -21 -508 O ATOM 882 N ALA A 297 37.985 2.978 -8.045 1.00 14.70 N ANISOU 882 N ALA A 297 2022 1832 1730 206 -28 -595 N ATOM 883 CA ALA A 297 37.296 3.322 -9.282 1.00 17.11 C ANISOU 883 CA ALA A 297 2333 2128 2041 151 -33 -557 C ATOM 884 C ALA A 297 37.225 2.132 -10.253 1.00 11.70 C ANISOU 884 C ALA A 297 1612 1476 1357 140 -26 -562 C ATOM 885 O ALA A 297 36.185 1.887 -10.856 1.00 11.10 O ANISOU 885 O ALA A 297 1540 1377 1301 138 -22 -523 O ATOM 886 CB ALA A 297 37.952 4.534 -9.943 1.00 13.81 C ANISOU 886 CB ALA A 297 1929 1723 1594 72 -47 -564 C ATOM 887 N LYS A 298 38.321 1.385 -10.378 1.00 10.04 N ANISOU 887 N LYS A 298 1368 1323 1122 138 -26 -613 N ATOM 888 CA LYS A 298 38.354 0.219 -11.266 1.00 13.71 C ANISOU 888 CA LYS A 298 1805 1822 1583 134 -26 -622 C ATOM 889 C LYS A 298 37.418 -0.889 -10.788 1.00 16.19 C ANISOU 889 C LYS A 298 2133 2100 1918 197 -16 -599 C ATOM 890 O LYS A 298 36.711 -1.508 -11.582 1.00 10.50 O ANISOU 890 O LYS A 298 1408 1372 1208 185 -14 -572 O ATOM 891 CB LYS A 298 39.776 -0.320 -11.400 1.00 15.64 C ANISOU 891 CB LYS A 298 2014 2144 1786 131 -34 -689 C ATOM 892 CG LYS A 298 40.676 0.486 -12.325 1.00 11.71 C ANISOU 892 CG LYS A 298 1488 1703 1258 48 -42 -712 C ATOM 893 CD LYS A 298 42.064 -0.137 -12.401 1.00 18.30 C ANISOU 893 CD LYS A 298 2278 2630 2044 54 -51 -786 C ATOM 894 CE LYS A 298 43.010 0.700 -13.251 1.00 24.69 C ANISOU 894 CE LYS A 298 3057 3509 2817 -39 -58 -814 C ATOM 895 NZ LYS A 298 44.398 0.145 -13.231 1.00 27.18 N ANISOU 895 NZ LYS A 298 3320 3930 3076 -29 -67 -894 N ATOM 896 N VAL A 299 37.401 -1.127 -9.482 1.00 14.38 N ANISOU 896 N VAL A 299 1925 1846 1691 259 -11 -611 N ATOM 897 CA VAL A 299 36.476 -2.099 -8.923 1.00 14.91 C ANISOU 897 CA VAL A 299 2015 1876 1773 309 -1 -588 C ATOM 898 C VAL A 299 35.036 -1.712 -9.259 1.00 17.09 C ANISOU 898 C VAL A 299 2301 2113 2080 291 8 -526 C ATOM 899 O VAL A 299 34.247 -2.541 -9.734 1.00 14.63 O ANISOU 899 O VAL A 299 1990 1794 1774 288 15 -502 O ATOM 900 CB VAL A 299 36.643 -2.231 -7.397 1.00 15.22 C ANISOU 900 CB VAL A 299 2081 1891 1811 376 5 -608 C ATOM 901 CG1 VAL A 299 35.426 -2.908 -6.790 1.00 18.77 C ANISOU 901 CG1 VAL A 299 2560 2295 2278 412 18 -571 C ATOM 902 CG2 VAL A 299 37.926 -3.004 -7.070 1.00 10.75 C ANISOU 902 CG2 VAL A 299 1510 1366 1208 412 -5 -675 C ATOM 903 N LYS A 300 34.700 -0.445 -9.029 1.00 9.44 N ANISOU 903 N LYS A 300 1342 1122 1123 279 6 -503 N ATOM 904 CA LYS A 300 33.328 0.010 -9.229 1.00 9.43 C ANISOU 904 CA LYS A 300 1352 1090 1143 276 11 -452 C ATOM 905 C LYS A 300 32.928 0.029 -10.719 1.00 14.11 C ANISOU 905 C LYS A 300 1927 1695 1738 221 8 -431 C ATOM 906 O LYS A 300 31.763 -0.199 -11.066 1.00 9.63 O ANISOU 906 O LYS A 300 1359 1116 1183 223 15 -396 O ATOM 907 CB LYS A 300 33.097 1.355 -8.534 1.00 15.67 C ANISOU 907 CB LYS A 300 2166 1851 1937 291 2 -437 C ATOM 908 CG LYS A 300 32.985 1.183 -7.018 1.00 18.42 C ANISOU 908 CG LYS A 300 2530 2177 2290 356 9 -443 C ATOM 909 CD LYS A 300 32.833 2.489 -6.264 1.00 20.31 C ANISOU 909 CD LYS A 300 2796 2389 2532 379 -4 -430 C ATOM 910 CE LYS A 300 32.782 2.204 -4.763 1.00 22.51 C ANISOU 910 CE LYS A 300 3086 2648 2818 446 4 -438 C ATOM 911 NZ LYS A 300 32.457 3.408 -3.960 1.00 30.48 N ANISOU 911 NZ LYS A 300 4123 3628 3829 479 -10 -420 N ATOM 912 N TYR A 301 33.903 0.263 -11.593 1.00 12.46 N ANISOU 912 N TYR A 301 1703 1517 1515 173 -2 -455 N ATOM 913 CA TYR A 301 33.659 0.213 -13.025 1.00 14.06 C ANISOU 913 CA TYR A 301 1889 1733 1719 122 -5 -439 C ATOM 914 C TYR A 301 33.277 -1.225 -13.409 1.00 10.83 C ANISOU 914 C TYR A 301 1463 1337 1316 135 3 -435 C ATOM 915 O TYR A 301 32.239 -1.454 -14.029 1.00 11.06 O ANISOU 915 O TYR A 301 1489 1354 1359 126 10 -401 O ATOM 916 CB TYR A 301 34.901 0.687 -13.789 1.00 9.63 C ANISOU 916 CB TYR A 301 1314 1211 1136 65 -17 -472 C ATOM 917 CG TYR A 301 34.701 0.894 -15.287 1.00 10.96 C ANISOU 917 CG TYR A 301 1471 1389 1304 6 -22 -455 C ATOM 918 CD1 TYR A 301 34.639 2.174 -15.828 1.00 13.57 C ANISOU 918 CD1 TYR A 301 1827 1702 1626 -41 -32 -442 C ATOM 919 CD2 TYR A 301 34.606 -0.189 -16.156 1.00 9.52 C ANISOU 919 CD2 TYR A 301 1260 1232 1127 0 -20 -454 C ATOM 920 CE1 TYR A 301 34.474 2.376 -17.193 1.00 9.87 C ANISOU 920 CE1 TYR A 301 1353 1239 1156 -94 -37 -429 C ATOM 921 CE2 TYR A 301 34.445 -0.003 -17.532 1.00 9.53 C ANISOU 921 CE2 TYR A 301 1249 1241 1131 -51 -24 -440 C ATOM 922 CZ TYR A 301 34.375 1.283 -18.042 1.00 11.96 C ANISOU 922 CZ TYR A 301 1581 1530 1432 -98 -32 -427 C ATOM 923 OH TYR A 301 34.214 1.485 -19.396 1.00 9.71 O ANISOU 923 OH TYR A 301 1291 1250 1149 -148 -36 -414 O ATOM 924 N VAL A 302 34.106 -2.185 -13.010 1.00 9.31 N ANISOU 924 N VAL A 302 1264 1168 1105 160 2 -472 N ATOM 925 CA VAL A 302 33.844 -3.597 -13.281 1.00 11.94 C ANISOU 925 CA VAL A 302 1597 1508 1433 176 4 -471 C ATOM 926 C VAL A 302 32.526 -4.072 -12.680 1.00 16.32 C ANISOU 926 C VAL A 302 2173 2025 2003 203 20 -434 C ATOM 927 O VAL A 302 31.795 -4.839 -13.310 1.00 9.08 O ANISOU 927 O VAL A 302 1255 1106 1089 189 25 -410 O ATOM 928 CB VAL A 302 34.989 -4.498 -12.776 1.00 17.24 C ANISOU 928 CB VAL A 302 2272 2207 2072 213 -6 -523 C ATOM 929 CG1 VAL A 302 34.590 -5.971 -12.852 1.00 12.92 C ANISOU 929 CG1 VAL A 302 1746 1651 1511 238 -7 -519 C ATOM 930 CG2 VAL A 302 36.241 -4.247 -13.589 1.00 10.16 C ANISOU 930 CG2 VAL A 302 1342 1367 1152 181 -22 -563 C ATOM 931 N LYS A 303 32.216 -3.605 -11.471 1.00 13.84 N ANISOU 931 N LYS A 303 1878 1685 1695 238 28 -429 N ATOM 932 CA LYS A 303 30.949 -3.956 -10.825 1.00 16.36 C ANISOU 932 CA LYS A 303 2214 1979 2024 260 44 -396 C ATOM 933 C LYS A 303 29.755 -3.449 -11.622 1.00 14.92 C ANISOU 933 C LYS A 303 2015 1796 1858 230 50 -354 C ATOM 934 O LYS A 303 28.739 -4.134 -11.750 1.00 13.51 O ANISOU 934 O LYS A 303 1836 1618 1680 224 62 -330 O ATOM 935 CB LYS A 303 30.860 -3.348 -9.418 1.00 24.89 C ANISOU 935 CB LYS A 303 3313 3037 3108 304 48 -398 C ATOM 936 CG LYS A 303 31.623 -4.090 -8.336 1.00 38.62 C ANISOU 936 CG LYS A 303 5077 4767 4828 349 49 -434 C ATOM 937 CD LYS A 303 31.508 -3.360 -7.001 1.00 45.49 C ANISOU 937 CD LYS A 303 5962 5614 5707 392 53 -434 C ATOM 938 CE LYS A 303 30.050 -3.194 -6.580 1.00 47.41 C ANISOU 938 CE LYS A 303 6207 5843 5961 400 67 -391 C ATOM 939 NZ LYS A 303 29.901 -2.284 -5.410 1.00 47.38 N ANISOU 939 NZ LYS A 303 6214 5822 5967 443 66 -387 N ATOM 940 N LEU A 304 29.851 -2.215 -12.103 1.00 11.01 N ANISOU 940 N LEU A 304 1511 1301 1371 211 40 -349 N ATOM 941 CA LEU A 304 28.738 -1.620 -12.832 1.00 11.35 C ANISOU 941 CA LEU A 304 1545 1342 1425 194 41 -316 C ATOM 942 C LEU A 304 28.507 -2.401 -14.122 1.00 11.52 C ANISOU 942 C LEU A 304 1546 1381 1450 155 44 -306 C ATOM 943 O LEU A 304 27.368 -2.683 -14.490 1.00 14.18 O ANISOU 943 O LEU A 304 1873 1723 1792 150 54 -280 O ATOM 944 CB LEU A 304 29.027 -0.156 -13.140 1.00 9.31 C ANISOU 944 CB LEU A 304 1298 1073 1165 181 24 -316 C ATOM 945 CG LEU A 304 27.916 0.662 -13.796 1.00 10.31 C ANISOU 945 CG LEU A 304 1429 1195 1294 176 19 -288 C ATOM 946 CD1 LEU A 304 26.695 0.745 -12.896 1.00 15.85 C ANISOU 946 CD1 LEU A 304 2133 1896 1994 224 27 -269 C ATOM 947 CD2 LEU A 304 28.424 2.052 -14.127 1.00 9.54 C ANISOU 947 CD2 LEU A 304 1361 1079 1185 158 -3 -294 C ATOM 948 N ALA A 305 29.600 -2.757 -14.794 1.00 12.10 N ANISOU 948 N ALA A 305 1611 1469 1518 130 34 -329 N ATOM 949 CA ALA A 305 29.526 -3.502 -16.043 1.00 15.77 C ANISOU 949 CA ALA A 305 2057 1951 1986 97 33 -322 C ATOM 950 C ALA A 305 28.824 -4.845 -15.845 1.00 14.61 C ANISOU 950 C ALA A 305 1916 1803 1833 108 45 -309 C ATOM 951 O ALA A 305 27.900 -5.199 -16.582 1.00 11.03 O ANISOU 951 O ALA A 305 1451 1353 1388 87 52 -283 O ATOM 952 CB ALA A 305 30.931 -3.708 -16.617 1.00 8.99 C ANISOU 952 CB ALA A 305 1186 1116 1112 76 17 -357 C ATOM 953 N ARG A 306 29.271 -5.591 -14.843 1.00 12.00 N ANISOU 953 N ARG A 306 1608 1465 1485 138 46 -329 N ATOM 954 CA ARG A 306 28.671 -6.878 -14.515 1.00 17.91 C ANISOU 954 CA ARG A 306 2380 2207 2219 145 55 -318 C ATOM 955 C ARG A 306 27.213 -6.778 -14.052 1.00 21.11 C ANISOU 955 C ARG A 306 2785 2607 2630 143 76 -284 C ATOM 956 O ARG A 306 26.468 -7.754 -14.145 1.00 18.30 O ANISOU 956 O ARG A 306 2440 2251 2261 127 86 -267 O ATOM 957 CB ARG A 306 29.513 -7.594 -13.456 1.00 19.67 C ANISOU 957 CB ARG A 306 2639 2419 2414 184 48 -351 C ATOM 958 CG ARG A 306 30.984 -7.612 -13.802 1.00 29.14 C ANISOU 958 CG ARG A 306 3832 3639 3600 194 26 -394 C ATOM 959 CD ARG A 306 31.578 -8.980 -13.599 1.00 39.00 C ANISOU 959 CD ARG A 306 5121 4889 4811 221 12 -422 C ATOM 960 NE ARG A 306 30.632 -10.028 -13.979 1.00 39.46 N ANISOU 960 NE ARG A 306 5204 4931 4859 201 17 -391 N ATOM 961 CZ ARG A 306 30.980 -11.274 -14.283 1.00 42.11 C ANISOU 961 CZ ARG A 306 5577 5265 5157 211 -2 -406 C ATOM 962 NH1 ARG A 306 30.048 -12.162 -14.602 1.00 43.55 N ANISOU 962 NH1 ARG A 306 5788 5430 5329 185 3 -374 N ATOM 963 NH2 ARG A 306 32.262 -11.630 -14.278 1.00 40.12 N ANISOU 963 NH2 ARG A 306 5337 5033 4874 247 -28 -454 N ATOM 964 N SER A 307 26.800 -5.607 -13.569 1.00 15.83 N ANISOU 964 N SER A 307 2104 1936 1975 159 81 -276 N ATOM 965 CA SER A 307 25.437 -5.451 -13.056 1.00 14.69 C ANISOU 965 CA SER A 307 1953 1800 1829 165 98 -251 C ATOM 966 C SER A 307 24.378 -5.362 -14.156 1.00 20.70 C ANISOU 966 C SER A 307 2685 2584 2597 134 104 -226 C ATOM 967 O SER A 307 23.191 -5.532 -13.892 1.00 19.68 O ANISOU 967 O SER A 307 2544 2477 2458 131 120 -208 O ATOM 968 CB SER A 307 25.331 -4.219 -12.157 1.00 18.85 C ANISOU 968 CB SER A 307 2480 2320 2361 203 95 -253 C ATOM 969 OG SER A 307 25.242 -3.028 -12.928 1.00 17.80 O ANISOU 969 OG SER A 307 2332 2190 2240 197 82 -247 O ATOM 970 N LEU A 308 24.803 -5.083 -15.385 1.00 14.11 N ANISOU 970 N LEU A 308 1835 1750 1776 111 92 -227 N ATOM 971 CA LEU A 308 23.870 -4.964 -16.507 1.00 15.19 C ANISOU 971 CA LEU A 308 1945 1907 1921 86 97 -207 C ATOM 972 C LEU A 308 23.490 -6.324 -17.107 1.00 13.84 C ANISOU 972 C LEU A 308 1770 1746 1743 52 106 -195 C ATOM 973 O LEU A 308 24.320 -7.227 -17.198 1.00 13.58 O ANISOU 973 O LEU A 308 1757 1700 1702 43 98 -205 O ATOM 974 CB LEU A 308 24.456 -4.054 -17.593 1.00 16.30 C ANISOU 974 CB LEU A 308 2077 2039 2077 73 80 -213 C ATOM 975 CG LEU A 308 24.825 -2.634 -17.154 1.00 18.15 C ANISOU 975 CG LEU A 308 2326 2258 2311 97 66 -223 C ATOM 976 CD1 LEU A 308 25.702 -1.938 -18.181 1.00 15.84 C ANISOU 976 CD1 LEU A 308 2038 1955 2026 70 48 -234 C ATOM 977 CD2 LEU A 308 23.562 -1.816 -16.887 1.00 25.56 C ANISOU 977 CD2 LEU A 308 3262 3208 3243 125 69 -210 C ATOM 978 N ARG A 309 22.229 -6.464 -17.514 1.00 13.94 N ANISOU 978 N ARG A 309 1760 1785 1752 36 121 -175 N ATOM 979 CA ARG A 309 21.756 -7.694 -18.145 1.00 14.24 C ANISOU 979 CA ARG A 309 1796 1834 1781 -3 130 -161 C ATOM 980 C ARG A 309 22.497 -7.970 -19.456 1.00 14.32 C ANISOU 980 C ARG A 309 1802 1832 1808 -22 114 -162 C ATOM 981 O ARG A 309 22.562 -9.108 -19.921 1.00 19.12 O ANISOU 981 O ARG A 309 2422 2437 2405 -48 112 -155 O ATOM 982 CB ARG A 309 20.253 -7.610 -18.433 1.00 16.14 C ANISOU 982 CB ARG A 309 2003 2116 2013 -18 149 -144 C ATOM 983 CG ARG A 309 19.350 -7.810 -17.224 1.00 30.67 C ANISOU 983 CG ARG A 309 3844 3985 3824 -14 169 -141 C ATOM 984 CD ARG A 309 18.107 -8.623 -17.624 1.00 41.09 C ANISOU 984 CD ARG A 309 5142 5348 5121 -59 190 -125 C ATOM 985 NE ARG A 309 16.931 -7.807 -17.902 1.00 39.64 N ANISOU 985 NE ARG A 309 4909 5220 4933 -46 199 -126 N ATOM 986 CZ ARG A 309 15.877 -8.219 -18.605 1.00 35.47 C ANISOU 986 CZ ARG A 309 4348 4739 4391 -80 215 -118 C ATOM 987 NH1 ARG A 309 15.851 -9.435 -19.137 1.00 33.14 N ANISOU 987 NH1 ARG A 309 4066 4437 4088 -133 222 -104 N ATOM 988 NH2 ARG A 309 14.849 -7.404 -18.793 1.00 36.97 N ANISOU 988 NH2 ARG A 309 4492 4985 4570 -56 220 -127 N ATOM 989 N THR A 310 23.026 -6.911 -20.058 1.00 11.68 N ANISOU 989 N THR A 310 1453 1491 1494 -13 100 -171 N ATOM 990 CA THR A 310 23.745 -7.001 -21.320 1.00 12.31 C ANISOU 990 CA THR A 310 1524 1565 1590 -32 84 -174 C ATOM 991 C THR A 310 25.172 -7.511 -21.165 1.00 14.27 C ANISOU 991 C THR A 310 1792 1802 1829 -28 66 -196 C ATOM 992 O THR A 310 25.846 -7.794 -22.163 1.00 12.93 O ANISOU 992 O THR A 310 1612 1635 1664 -44 51 -201 O ATOM 993 CB THR A 310 23.810 -5.638 -21.979 1.00 11.25 C ANISOU 993 CB THR A 310 1375 1427 1472 -29 76 -178 C ATOM 994 OG1 THR A 310 24.265 -4.682 -21.011 1.00 13.39 O ANISOU 994 OG1 THR A 310 1664 1686 1737 -4 71 -193 O ATOM 995 CG2 THR A 310 22.430 -5.232 -22.491 1.00 12.38 C ANISOU 995 CG2 THR A 310 1497 1587 1620 -28 88 -161 C ATOM 996 N TYR A 311 25.647 -7.620 -19.926 1.00 11.10 N ANISOU 996 N TYR A 311 1416 1391 1411 -3 66 -212 N ATOM 997 CA TYR A 311 27.010 -8.081 -19.717 1.00 8.72 C ANISOU 997 CA TYR A 311 1133 1087 1093 10 48 -242 C ATOM 998 C TYR A 311 27.180 -9.490 -20.268 1.00 10.50 C ANISOU 998 C TYR A 311 1375 1315 1300 0 36 -240 C ATOM 999 O TYR A 311 26.330 -10.354 -20.061 1.00 18.30 O ANISOU 999 O TYR A 311 2383 2295 2274 -10 47 -220 O ATOM 1000 CB TYR A 311 27.414 -8.052 -18.236 1.00 11.04 C ANISOU 1000 CB TYR A 311 1455 1369 1370 44 50 -261 C ATOM 1001 CG TYR A 311 28.833 -8.521 -18.040 1.00 13.95 C ANISOU 1001 CG TYR A 311 1841 1744 1717 65 29 -299 C ATOM 1002 CD1 TYR A 311 29.901 -7.642 -18.197 1.00 15.32 C ANISOU 1002 CD1 TYR A 311 1994 1932 1893 66 17 -327 C ATOM 1003 CD2 TYR A 311 29.114 -9.856 -17.757 1.00 17.30 C ANISOU 1003 CD2 TYR A 311 2303 2161 2108 81 19 -311 C ATOM 1004 CE1 TYR A 311 31.204 -8.073 -18.045 1.00 21.47 C ANISOU 1004 CE1 TYR A 311 2781 2732 2646 87 -3 -368 C ATOM 1005 CE2 TYR A 311 30.413 -10.295 -17.613 1.00 15.44 C ANISOU 1005 CE2 TYR A 311 2083 1938 1844 110 -5 -353 C ATOM 1006 CZ TYR A 311 31.455 -9.401 -17.757 1.00 23.29 C ANISOU 1006 CZ TYR A 311 3046 2959 2844 114 -15 -383 C ATOM 1007 OH TYR A 311 32.756 -9.831 -17.613 1.00 21.69 O ANISOU 1007 OH TYR A 311 2851 2785 2606 144 -39 -431 O ATOM 1008 N GLY A 312 28.278 -9.708 -20.983 1.00 11.87 N ANISOU 1008 N GLY A 312 1541 1502 1467 1 13 -262 N ATOM 1009 CA GLY A 312 28.625 -11.033 -21.466 1.00 14.59 C ANISOU 1009 CA GLY A 312 1909 1850 1786 4 -6 -266 C ATOM 1010 C GLY A 312 27.773 -11.523 -22.620 1.00 18.54 C ANISOU 1010 C GLY A 312 2396 2350 2299 -28 -4 -233 C ATOM 1011 O GLY A 312 27.810 -12.705 -22.964 1.00 23.07 O ANISOU 1011 O GLY A 312 2999 2919 2848 -28 -19 -229 O ATOM 1012 N VAL A 313 27.016 -10.618 -23.233 1.00 14.01 N ANISOU 1012 N VAL A 313 1783 1779 1761 -53 14 -211 N ATOM 1013 CA VAL A 313 26.147 -10.983 -24.347 1.00 12.77 C ANISOU 1013 CA VAL A 313 1609 1625 1620 -81 19 -181 C ATOM 1014 C VAL A 313 26.770 -10.590 -25.698 1.00 17.69 C ANISOU 1014 C VAL A 313 2196 2261 2263 -93 2 -186 C ATOM 1015 O VAL A 313 27.300 -9.487 -25.859 1.00 12.11 O ANISOU 1015 O VAL A 313 1468 1562 1571 -95 1 -200 O ATOM 1016 CB VAL A 313 24.747 -10.340 -24.178 1.00 10.44 C ANISOU 1016 CB VAL A 313 1294 1329 1343 -95 48 -157 C ATOM 1017 CG1 VAL A 313 23.796 -10.742 -25.326 1.00 9.33 C ANISOU 1017 CG1 VAL A 313 1131 1196 1217 -123 55 -130 C ATOM 1018 CG2 VAL A 313 24.162 -10.728 -22.831 1.00 9.37 C ANISOU 1018 CG2 VAL A 313 1188 1189 1183 -87 64 -154 C ATOM 1019 N SER A 314 26.718 -11.501 -26.667 1.00 12.00 N ANISOU 1019 N SER A 314 1475 1544 1540 -104 -11 -173 N ATOM 1020 CA SER A 314 27.199 -11.194 -28.014 1.00 14.65 C ANISOU 1020 CA SER A 314 1777 1895 1896 -117 -26 -174 C ATOM 1021 C SER A 314 26.062 -10.641 -28.863 1.00 7.83 C ANISOU 1021 C SER A 314 884 1023 1067 -140 -6 -146 C ATOM 1022 O SER A 314 25.108 -11.360 -29.184 1.00 14.57 O ANISOU 1022 O SER A 314 1741 1871 1924 -151 3 -121 O ATOM 1023 CB SER A 314 27.781 -12.443 -28.686 1.00 10.84 C ANISOU 1023 CB SER A 314 1306 1422 1390 -108 -56 -177 C ATOM 1024 OG SER A 314 28.971 -12.856 -28.053 1.00 17.10 O ANISOU 1024 OG SER A 314 2122 2230 2144 -77 -80 -213 O ATOM 1025 N PHE A 315 26.163 -9.372 -29.235 1.00 9.38 N ANISOU 1025 N PHE A 315 1058 1221 1286 -149 0 -152 N ATOM 1026 CA PHE A 315 25.072 -8.717 -29.950 1.00 7.75 C ANISOU 1026 CA PHE A 315 832 1006 1107 -160 17 -132 C ATOM 1027 C PHE A 315 25.317 -8.597 -31.444 1.00 15.39 C ANISOU 1027 C PHE A 315 1776 1976 2096 -177 5 -127 C ATOM 1028 O PHE A 315 26.445 -8.395 -31.890 1.00 16.53 O ANISOU 1028 O PHE A 315 1914 2131 2236 -186 -14 -145 O ATOM 1029 CB PHE A 315 24.776 -7.339 -29.357 1.00 12.75 C ANISOU 1029 CB PHE A 315 1471 1630 1743 -153 29 -141 C ATOM 1030 CG PHE A 315 24.051 -7.392 -28.042 1.00 8.92 C ANISOU 1030 CG PHE A 315 1000 1145 1243 -134 46 -138 C ATOM 1031 CD1 PHE A 315 24.745 -7.294 -26.848 1.00 9.93 C ANISOU 1031 CD1 PHE A 315 1150 1271 1353 -119 42 -156 C ATOM 1032 CD2 PHE A 315 22.678 -7.546 -28.004 1.00 10.83 C ANISOU 1032 CD2 PHE A 315 1232 1395 1487 -132 65 -121 C ATOM 1033 CE1 PHE A 315 24.081 -7.341 -25.632 1.00 12.23 C ANISOU 1033 CE1 PHE A 315 1455 1562 1630 -101 58 -153 C ATOM 1034 CE2 PHE A 315 22.007 -7.603 -26.795 1.00 15.01 C ANISOU 1034 CE2 PHE A 315 1771 1933 1998 -118 81 -119 C ATOM 1035 CZ PHE A 315 22.705 -7.493 -25.609 1.00 15.78 C ANISOU 1035 CZ PHE A 315 1892 2023 2079 -103 77 -134 C ATOM 1036 N PHE A 316 24.233 -8.721 -32.202 1.00 12.82 N ANISOU 1036 N PHE A 316 1437 1645 1791 -183 17 -105 N ATOM 1037 CA PHE A 316 24.238 -8.525 -33.643 1.00 12.74 C ANISOU 1037 CA PHE A 316 1405 1632 1805 -195 10 -98 C ATOM 1038 C PHE A 316 23.218 -7.457 -33.999 1.00 13.12 C ANISOU 1038 C PHE A 316 1449 1668 1870 -191 26 -94 C ATOM 1039 O PHE A 316 22.102 -7.458 -33.478 1.00 9.88 O ANISOU 1039 O PHE A 316 1037 1262 1455 -178 45 -87 O ATOM 1040 CB PHE A 316 23.870 -9.833 -34.353 1.00 9.45 C ANISOU 1040 CB PHE A 316 977 1219 1393 -199 4 -76 C ATOM 1041 CG PHE A 316 24.876 -10.925 -34.158 1.00 12.57 C ANISOU 1041 CG PHE A 316 1386 1625 1764 -194 -21 -82 C ATOM 1042 CD1 PHE A 316 24.858 -11.705 -33.018 1.00 13.19 C ANISOU 1042 CD1 PHE A 316 1495 1703 1811 -185 -21 -84 C ATOM 1043 CD2 PHE A 316 25.856 -11.161 -35.111 1.00 14.87 C ANISOU 1043 CD2 PHE A 316 1663 1929 2058 -196 -47 -90 C ATOM 1044 CE1 PHE A 316 25.792 -12.706 -32.838 1.00 14.33 C ANISOU 1044 CE1 PHE A 316 1664 1857 1926 -171 -49 -95 C ATOM 1045 CE2 PHE A 316 26.786 -12.159 -34.935 1.00 13.22 C ANISOU 1045 CE2 PHE A 316 1469 1738 1818 -181 -76 -101 C ATOM 1046 CZ PHE A 316 26.755 -12.935 -33.798 1.00 13.80 C ANISOU 1046 CZ PHE A 316 1580 1806 1857 -165 -78 -105 C ATOM 1047 N LEU A 317 23.599 -6.546 -34.885 1.00 13.16 N ANISOU 1047 N LEU A 317 1454 1660 1887 -201 18 -102 N ATOM 1048 CA LEU A 317 22.672 -5.545 -35.375 1.00 13.94 C ANISOU 1048 CA LEU A 317 1559 1742 1995 -190 28 -103 C ATOM 1049 C LEU A 317 21.862 -6.108 -36.544 1.00 14.81 C ANISOU 1049 C LEU A 317 1643 1854 2129 -188 33 -86 C ATOM 1050 O LEU A 317 22.409 -6.433 -37.593 1.00 15.38 O ANISOU 1050 O LEU A 317 1703 1922 2219 -204 21 -80 O ATOM 1051 CB LEU A 317 23.430 -4.290 -35.815 1.00 12.66 C ANISOU 1051 CB LEU A 317 1424 1559 1828 -206 15 -120 C ATOM 1052 CG LEU A 317 22.567 -3.164 -36.403 1.00 24.25 C ANISOU 1052 CG LEU A 317 2916 3001 3296 -190 17 -125 C ATOM 1053 CD1 LEU A 317 21.561 -2.662 -35.373 1.00 20.92 C ANISOU 1053 CD1 LEU A 317 2510 2583 2855 -152 28 -131 C ATOM 1054 CD2 LEU A 317 23.443 -2.016 -36.918 1.00 28.09 C ANISOU 1054 CD2 LEU A 317 3443 3461 3771 -218 1 -140 C ATOM 1055 N VAL A 318 20.555 -6.214 -36.365 1.00 15.47 N ANISOU 1055 N VAL A 318 1716 1949 2212 -168 52 -80 N ATOM 1056 CA VAL A 318 19.714 -6.819 -37.388 1.00 17.90 C ANISOU 1056 CA VAL A 318 1997 2265 2541 -166 59 -66 C ATOM 1057 C VAL A 318 18.515 -5.927 -37.686 1.00 17.26 C ANISOU 1057 C VAL A 318 1915 2188 2457 -136 71 -78 C ATOM 1058 O VAL A 318 18.376 -4.848 -37.107 1.00 16.41 O ANISOU 1058 O VAL A 318 1833 2073 2328 -114 70 -97 O ATOM 1059 CB VAL A 318 19.221 -8.211 -36.936 1.00 15.93 C ANISOU 1059 CB VAL A 318 1729 2041 2284 -178 70 -47 C ATOM 1060 CG1 VAL A 318 20.396 -9.043 -36.426 1.00 12.40 C ANISOU 1060 CG1 VAL A 318 1296 1590 1826 -195 53 -42 C ATOM 1061 CG2 VAL A 318 18.180 -8.079 -35.849 1.00 15.02 C ANISOU 1061 CG2 VAL A 318 1611 1954 2143 -165 91 -53 C ATOM 1062 N LYS A 319 17.663 -6.367 -38.609 1.00 14.30 N ANISOU 1062 N LYS A 319 1512 1824 2099 -130 80 -70 N ATOM 1063 CA LYS A 319 16.394 -5.690 -38.850 1.00 7.46 C ANISOU 1063 CA LYS A 319 637 974 1222 -94 93 -88 C ATOM 1064 C LYS A 319 15.229 -6.643 -38.637 1.00 14.05 C ANISOU 1064 C LYS A 319 1431 1859 2048 -97 115 -80 C ATOM 1065 O LYS A 319 15.275 -7.796 -39.072 1.00 21.47 O ANISOU 1065 O LYS A 319 2349 2804 3004 -126 118 -57 O ATOM 1066 CB LYS A 319 16.344 -5.104 -40.260 1.00 12.20 C ANISOU 1066 CB LYS A 319 1246 1545 1844 -79 83 -95 C ATOM 1067 CG LYS A 319 17.293 -3.943 -40.479 1.00 18.19 C ANISOU 1067 CG LYS A 319 2056 2257 2600 -80 63 -108 C ATOM 1068 CD LYS A 319 16.941 -3.193 -41.757 1.00 31.17 C ANISOU 1068 CD LYS A 319 3719 3872 4253 -57 56 -122 C ATOM 1069 CE LYS A 319 17.945 -2.086 -42.062 1.00 39.23 C ANISOU 1069 CE LYS A 319 4800 4843 5264 -73 34 -133 C ATOM 1070 NZ LYS A 319 17.512 -1.248 -43.224 1.00 42.91 N ANISOU 1070 NZ LYS A 319 5301 5273 5728 -47 26 -150 N ATOM 1071 N GLU A 320 14.189 -6.160 -37.963 1.00 16.96 N ANISOU 1071 N GLU A 320 1790 2269 2385 -68 129 -101 N ATOM 1072 CA GLU A 320 12.975 -6.946 -37.764 1.00 19.46 C ANISOU 1072 CA GLU A 320 2063 2647 2684 -75 152 -100 C ATOM 1073 C GLU A 320 11.767 -6.184 -38.306 1.00 20.23 C ANISOU 1073 C GLU A 320 2140 2782 2766 -26 160 -131 C ATOM 1074 O GLU A 320 11.855 -4.990 -38.611 1.00 18.26 O ANISOU 1074 O GLU A 320 1921 2505 2511 19 144 -155 O ATOM 1075 CB GLU A 320 12.778 -7.285 -36.276 1.00 17.15 C ANISOU 1075 CB GLU A 320 1769 2392 2357 -91 165 -99 C ATOM 1076 CG GLU A 320 12.734 -6.082 -35.357 1.00 21.68 C ANISOU 1076 CG GLU A 320 2364 2970 2901 -49 158 -124 C ATOM 1077 CD GLU A 320 12.625 -6.444 -33.874 1.00 17.45 C ANISOU 1077 CD GLU A 320 1827 2468 2334 -64 170 -121 C ATOM 1078 OE1 GLU A 320 13.113 -7.521 -33.459 1.00 18.98 O ANISOU 1078 OE1 GLU A 320 2027 2654 2533 -111 175 -97 O ATOM 1079 OE2 GLU A 320 12.059 -5.630 -33.117 1.00 21.09 O ANISOU 1079 OE2 GLU A 320 2288 2962 2762 -26 171 -145 O ATOM 1080 N LYS A 321 10.639 -6.873 -38.431 1.00 12.60 N ANISOU 1080 N LYS A 321 1125 1878 1784 -35 182 -135 N ATOM 1081 CA LYS A 321 9.404 -6.213 -38.839 1.00 20.38 C ANISOU 1081 CA LYS A 321 2083 2917 2744 17 189 -173 C ATOM 1082 C LYS A 321 8.956 -5.206 -37.780 1.00 22.69 C ANISOU 1082 C LYS A 321 2386 3247 2987 65 185 -206 C ATOM 1083 O LYS A 321 8.928 -5.517 -36.593 1.00 27.53 O ANISOU 1083 O LYS A 321 2992 3893 3575 42 195 -200 O ATOM 1084 CB LYS A 321 8.296 -7.238 -39.074 1.00 19.75 C ANISOU 1084 CB LYS A 321 1943 2912 2651 -13 216 -172 C ATOM 1085 CG LYS A 321 6.971 -6.620 -39.501 1.00 24.91 C ANISOU 1085 CG LYS A 321 2558 3636 3271 44 225 -218 C ATOM 1086 CD LYS A 321 5.869 -7.672 -39.603 1.00 25.06 C ANISOU 1086 CD LYS A 321 2511 3742 3268 3 255 -220 C ATOM 1087 CE LYS A 321 4.586 -7.091 -40.216 1.00 26.74 C ANISOU 1087 CE LYS A 321 2680 4032 3448 65 262 -272 C ATOM 1088 NZ LYS A 321 4.124 -5.852 -39.513 1.00 21.88 N ANISOU 1088 NZ LYS A 321 2073 3459 2780 141 251 -320 N ATOM 1089 N MET A 322 8.613 -3.999 -38.216 1.00 21.92 N ANISOU 1089 N MET A 322 2313 3144 2872 135 168 -242 N ATOM 1090 CA MET A 322 8.040 -2.996 -37.326 1.00 25.33 C ANISOU 1090 CA MET A 322 2757 3618 3249 195 159 -279 C ATOM 1091 C MET A 322 6.588 -3.362 -37.001 1.00 26.69 C ANISOU 1091 C MET A 322 2860 3909 3374 211 182 -309 C ATOM 1092 O MET A 322 5.831 -3.793 -37.874 1.00 16.28 O ANISOU 1092 O MET A 322 1497 2631 2057 212 196 -321 O ATOM 1093 CB MET A 322 8.123 -1.609 -37.968 1.00 26.10 C ANISOU 1093 CB MET A 322 2917 3668 3334 268 128 -311 C ATOM 1094 CG MET A 322 7.571 -0.457 -37.134 1.00 32.70 C ANISOU 1094 CG MET A 322 3781 4538 4104 344 108 -352 C ATOM 1095 SD MET A 322 7.697 1.121 -38.016 1.00 52.97 S ANISOU 1095 SD MET A 322 6444 7034 6648 427 65 -389 S ATOM 1096 CE MET A 322 6.822 2.227 -36.906 1.00 32.94 C ANISOU 1096 CE MET A 322 3929 4563 4022 522 41 -440 C ATOM 1097 N LYS A 323 6.214 -3.206 -35.736 1.00 24.97 N ANISOU 1097 N LYS A 323 2628 3749 3110 221 187 -322 N ATOM 1098 CA LYS A 323 4.859 -3.514 -35.284 1.00 34.09 C ANISOU 1098 CA LYS A 323 3713 5031 4210 230 209 -354 C ATOM 1099 C LYS A 323 3.780 -2.853 -36.144 1.00 35.55 C ANISOU 1099 C LYS A 323 3874 5275 4359 309 202 -408 C ATOM 1100 O LYS A 323 3.685 -1.626 -36.204 1.00 34.06 O ANISOU 1100 O LYS A 323 3729 5071 4140 395 171 -444 O ATOM 1101 CB LYS A 323 4.689 -3.069 -33.831 1.00 42.56 C ANISOU 1101 CB LYS A 323 4787 6151 5233 252 205 -367 C ATOM 1102 CG LYS A 323 3.255 -3.085 -33.331 1.00 53.99 C ANISOU 1102 CG LYS A 323 6163 7742 6608 280 221 -412 C ATOM 1103 CD LYS A 323 2.921 -4.394 -32.636 1.00 62.37 C ANISOU 1103 CD LYS A 323 7168 8870 7659 186 259 -388 C ATOM 1104 CE LYS A 323 1.818 -4.194 -31.599 1.00 64.38 C ANISOU 1104 CE LYS A 323 7367 9261 7835 210 270 -429 C ATOM 1105 NZ LYS A 323 1.757 -5.316 -30.621 1.00 64.88 N ANISOU 1105 NZ LYS A 323 7401 9366 7884 113 302 -399 N ATOM 1106 N GLY A 324 2.963 -3.671 -36.802 1.00 31.57 N ANISOU 1106 N GLY A 324 3304 4838 3853 279 228 -415 N ATOM 1107 CA GLY A 324 1.845 -3.161 -37.574 1.00 34.48 C ANISOU 1107 CA GLY A 324 3638 5279 4182 354 225 -472 C ATOM 1108 C GLY A 324 2.196 -2.559 -38.926 1.00 36.81 C ANISOU 1108 C GLY A 324 3984 5488 4515 404 202 -480 C ATOM 1109 O GLY A 324 1.313 -2.070 -39.634 1.00 35.17 O ANISOU 1109 O GLY A 324 3759 5332 4273 476 195 -532 O ATOM 1110 N LYS A 325 3.476 -2.591 -39.292 1.00 26.77 N ANISOU 1110 N LYS A 325 2774 4091 3307 367 189 -433 N ATOM 1111 CA LYS A 325 3.919 -1.996 -40.557 1.00 30.61 C ANISOU 1111 CA LYS A 325 3315 4488 3828 406 167 -437 C ATOM 1112 C LYS A 325 4.699 -2.983 -41.434 1.00 29.36 C ANISOU 1112 C LYS A 325 3152 4259 3746 330 180 -385 C ATOM 1113 O LYS A 325 5.505 -3.772 -40.934 1.00 26.18 O ANISOU 1113 O LYS A 325 2748 3823 3376 253 189 -336 O ATOM 1114 CB LYS A 325 4.800 -0.769 -40.295 1.00 35.16 C ANISOU 1114 CB LYS A 325 3988 4973 4397 449 130 -440 C ATOM 1115 CG LYS A 325 4.192 0.277 -39.383 1.00 35.00 C ANISOU 1115 CG LYS A 325 3991 5007 4301 530 108 -488 C ATOM 1116 CD LYS A 325 3.500 1.362 -40.172 1.00 41.66 C ANISOU 1116 CD LYS A 325 4877 5855 5098 636 79 -548 C ATOM 1117 CE LYS A 325 2.726 2.285 -39.251 1.00 47.72 C ANISOU 1117 CE LYS A 325 5657 6698 5777 727 55 -601 C ATOM 1118 NZ LYS A 325 1.646 1.553 -38.538 1.00 50.00 N ANISOU 1118 NZ LYS A 325 5838 7133 6027 718 86 -621 N ATOM 1119 N ASN A 326 4.459 -2.933 -42.742 1.00 26.89 N ANISOU 1119 N ASN A 326 2838 3923 3457 356 177 -397 N ATOM 1120 CA ASN A 326 5.294 -3.662 -43.691 1.00 31.09 C ANISOU 1120 CA ASN A 326 3377 4376 4060 299 181 -350 C ATOM 1121 C ASN A 326 6.607 -2.911 -43.900 1.00 26.32 C ANISOU 1121 C ASN A 326 2857 3658 3485 300 152 -330 C ATOM 1122 O ASN A 326 6.813 -2.265 -44.921 1.00 26.14 O ANISOU 1122 O ASN A 326 2879 3577 3478 337 134 -343 O ATOM 1123 CB ASN A 326 4.562 -3.865 -45.020 1.00 32.53 C ANISOU 1123 CB ASN A 326 3526 4575 4257 329 188 -371 C ATOM 1124 CG ASN A 326 3.598 -5.042 -44.983 1.00 33.56 C ANISOU 1124 CG ASN A 326 3568 4803 4379 287 222 -369 C ATOM 1125 OD1 ASN A 326 3.209 -5.509 -43.911 1.00 34.34 O ANISOU 1125 OD1 ASN A 326 3629 4976 4442 250 240 -366 O ATOM 1126 ND2 ASN A 326 3.216 -5.534 -46.158 1.00 31.32 N ANISOU 1126 ND2 ASN A 326 3253 4520 4125 288 232 -369 N ATOM 1127 N LYS A 327 7.485 -2.989 -42.908 1.00 26.28 N ANISOU 1127 N LYS A 327 2875 3626 3483 256 147 -301 N ATOM 1128 CA LYS A 327 8.707 -2.196 -42.894 1.00 19.76 C ANISOU 1128 CA LYS A 327 2128 2708 2672 252 120 -288 C ATOM 1129 C LYS A 327 9.728 -2.865 -41.974 1.00 23.56 C ANISOU 1129 C LYS A 327 2607 3170 3174 181 125 -245 C ATOM 1130 O LYS A 327 9.374 -3.347 -40.897 1.00 23.39 O ANISOU 1130 O LYS A 327 2551 3206 3128 163 140 -241 O ATOM 1131 CB LYS A 327 8.401 -0.775 -42.391 1.00 20.05 C ANISOU 1131 CB LYS A 327 2225 2743 2651 325 96 -332 C ATOM 1132 CG LYS A 327 9.519 0.239 -42.624 1.00 29.86 C ANISOU 1132 CG LYS A 327 3561 3886 3897 326 65 -327 C ATOM 1133 CD LYS A 327 9.270 1.523 -41.854 1.00 37.48 C ANISOU 1133 CD LYS A 327 4592 4851 4797 389 39 -364 C ATOM 1134 CE LYS A 327 10.263 2.607 -42.247 1.00 45.78 C ANISOU 1134 CE LYS A 327 5750 5802 5843 388 6 -364 C ATOM 1135 NZ LYS A 327 11.670 2.107 -42.241 1.00 46.69 N ANISOU 1135 NZ LYS A 327 5868 5864 6010 297 12 -316 N ATOM 1136 N LEU A 328 10.989 -2.893 -42.397 1.00 23.43 N ANISOU 1136 N LEU A 328 2627 3079 3196 142 111 -216 N ATOM 1137 CA LEU A 328 12.068 -3.409 -41.555 1.00 22.28 C ANISOU 1137 CA LEU A 328 2488 2915 3064 85 110 -183 C ATOM 1138 C LEU A 328 12.762 -2.279 -40.794 1.00 25.89 C ANISOU 1138 C LEU A 328 3009 3335 3495 99 90 -196 C ATOM 1139 O LEU A 328 13.112 -1.254 -41.383 1.00 26.46 O ANISOU 1139 O LEU A 328 3137 3355 3560 121 69 -211 O ATOM 1140 CB LEU A 328 13.092 -4.160 -42.406 1.00 25.39 C ANISOU 1140 CB LEU A 328 2878 3263 3508 34 105 -149 C ATOM 1141 CG LEU A 328 12.604 -5.420 -43.115 1.00 24.93 C ANISOU 1141 CG LEU A 328 2764 3231 3478 12 121 -128 C ATOM 1142 CD1 LEU A 328 13.646 -5.892 -44.123 1.00 22.24 C ANISOU 1142 CD1 LEU A 328 2428 2839 3182 -20 107 -100 C ATOM 1143 CD2 LEU A 328 12.299 -6.503 -42.092 1.00 24.42 C ANISOU 1143 CD2 LEU A 328 2663 3217 3398 -24 139 -110 C ATOM 1144 N VAL A 329 12.952 -2.470 -39.488 1.00 28.28 N ANISOU 1144 N VAL A 329 3305 3661 3777 83 95 -189 N ATOM 1145 CA VAL A 329 13.674 -1.508 -38.656 1.00 22.37 C ANISOU 1145 CA VAL A 329 2615 2880 3006 91 76 -197 C ATOM 1146 C VAL A 329 14.783 -2.199 -37.862 1.00 24.20 C ANISOU 1146 C VAL A 329 2841 3099 3254 35 79 -168 C ATOM 1147 O VAL A 329 14.734 -3.407 -37.663 1.00 23.30 O ANISOU 1147 O VAL A 329 2682 3015 3157 2 96 -147 O ATOM 1148 CB VAL A 329 12.734 -0.772 -37.682 1.00 21.09 C ANISOU 1148 CB VAL A 329 2461 2762 2791 148 74 -227 C ATOM 1149 CG1 VAL A 329 11.597 -0.096 -38.446 1.00 24.85 C ANISOU 1149 CG1 VAL A 329 2944 3259 3239 215 67 -263 C ATOM 1150 CG2 VAL A 329 12.196 -1.729 -36.613 1.00 16.57 C ANISOU 1150 CG2 VAL A 329 1830 2259 2208 130 98 -217 C ATOM 1151 N PRO A 330 15.785 -1.426 -37.402 1.00 26.29 N ANISOU 1151 N PRO A 330 3158 3322 3509 25 60 -170 N ATOM 1152 CA PRO A 330 16.960 -1.967 -36.701 1.00 26.74 C ANISOU 1152 CA PRO A 330 3213 3367 3578 -21 60 -151 C ATOM 1153 C PRO A 330 16.662 -2.471 -35.285 1.00 23.13 C ANISOU 1153 C PRO A 330 2734 2950 3102 -18 73 -147 C ATOM 1154 O PRO A 330 15.756 -1.977 -34.619 1.00 17.00 O ANISOU 1154 O PRO A 330 1960 2205 2295 22 77 -164 O ATOM 1155 CB PRO A 330 17.914 -0.760 -36.625 1.00 23.45 C ANISOU 1155 CB PRO A 330 2862 2901 3146 -27 36 -163 C ATOM 1156 CG PRO A 330 17.398 0.221 -37.625 1.00 29.84 C ANISOU 1156 CG PRO A 330 3712 3683 3943 4 23 -182 C ATOM 1157 CD PRO A 330 15.914 0.020 -37.638 1.00 22.24 C ANISOU 1157 CD PRO A 330 2715 2767 2969 56 37 -194 C ATOM 1158 N ARG A 331 17.446 -3.438 -34.825 1.00 17.65 N ANISOU 1158 N ARG A 331 2025 2258 2423 -58 78 -128 N ATOM 1159 CA ARG A 331 17.313 -3.938 -33.465 1.00 13.60 C ANISOU 1159 CA ARG A 331 1502 1774 1891 -59 90 -124 C ATOM 1160 C ARG A 331 18.570 -4.702 -33.089 1.00 15.08 C ANISOU 1160 C ARG A 331 1695 1944 2090 -96 84 -110 C ATOM 1161 O ARG A 331 19.277 -5.204 -33.959 1.00 13.20 O ANISOU 1161 O ARG A 331 1452 1689 1874 -122 75 -101 O ATOM 1162 CB ARG A 331 16.106 -4.868 -33.347 1.00 15.40 C ANISOU 1162 CB ARG A 331 1686 2054 2112 -60 113 -117 C ATOM 1163 CG ARG A 331 15.639 -5.092 -31.916 1.00 13.83 C ANISOU 1163 CG ARG A 331 1480 1892 1881 -55 126 -120 C ATOM 1164 CD ARG A 331 14.957 -3.839 -31.375 1.00 13.33 C ANISOU 1164 CD ARG A 331 1429 1849 1788 -2 122 -145 C ATOM 1165 NE ARG A 331 13.650 -3.629 -31.991 1.00 25.53 N ANISOU 1165 NE ARG A 331 2943 3439 3317 28 130 -162 N ATOM 1166 CZ ARG A 331 13.045 -2.446 -32.092 1.00 38.59 C ANISOU 1166 CZ ARG A 331 4614 5105 4945 86 117 -190 C ATOM 1167 NH1 ARG A 331 11.852 -2.357 -32.667 1.00 45.79 N ANISOU 1167 NH1 ARG A 331 5493 6067 5838 117 125 -210 N ATOM 1168 NH2 ARG A 331 13.632 -1.347 -31.631 1.00 33.40 N ANISOU 1168 NH2 ARG A 331 4010 4408 4274 115 94 -201 N ATOM 1169 N LEU A 332 18.840 -4.806 -31.792 1.00 12.47 N ANISOU 1169 N LEU A 332 1376 1621 1741 -94 87 -113 N ATOM 1170 CA LEU A 332 19.973 -5.597 -31.330 1.00 12.56 C ANISOU 1170 CA LEU A 332 1395 1623 1756 -120 80 -106 C ATOM 1171 C LEU A 332 19.517 -6.998 -30.902 1.00 16.93 C ANISOU 1171 C LEU A 332 1933 2200 2301 -136 94 -90 C ATOM 1172 O LEU A 332 18.652 -7.154 -30.039 1.00 18.70 O ANISOU 1172 O LEU A 332 2151 2451 2505 -129 111 -90 O ATOM 1173 CB LEU A 332 20.703 -4.893 -30.184 1.00 10.85 C ANISOU 1173 CB LEU A 332 1208 1393 1522 -109 72 -121 C ATOM 1174 CG LEU A 332 21.393 -3.561 -30.486 1.00 19.18 C ANISOU 1174 CG LEU A 332 2293 2419 2576 -105 55 -136 C ATOM 1175 CD1 LEU A 332 21.985 -2.956 -29.210 1.00 20.38 C ANISOU 1175 CD1 LEU A 332 2473 2562 2707 -94 49 -149 C ATOM 1176 CD2 LEU A 332 22.473 -3.741 -31.538 1.00 20.82 C ANISOU 1176 CD2 LEU A 332 2499 2613 2800 -139 41 -136 C ATOM 1177 N LEU A 333 20.099 -8.011 -31.530 1.00 13.91 N ANISOU 1177 N LEU A 333 1547 1809 1929 -160 85 -78 N ATOM 1178 CA LEU A 333 19.813 -9.394 -31.189 1.00 8.77 C ANISOU 1178 CA LEU A 333 898 1170 1263 -180 91 -62 C ATOM 1179 C LEU A 333 21.007 -9.970 -30.441 1.00 16.00 C ANISOU 1179 C LEU A 333 1846 2071 2162 -181 75 -68 C ATOM 1180 O LEU A 333 22.112 -10.041 -30.979 1.00 14.18 O ANISOU 1180 O LEU A 333 1619 1827 1939 -181 53 -75 O ATOM 1181 CB LEU A 333 19.542 -10.212 -32.452 1.00 8.54 C ANISOU 1181 CB LEU A 333 853 1142 1250 -199 87 -44 C ATOM 1182 CG LEU A 333 19.282 -11.700 -32.184 1.00 12.90 C ANISOU 1182 CG LEU A 333 1421 1700 1779 -225 89 -25 C ATOM 1183 CD1 LEU A 333 18.011 -11.878 -31.341 1.00 13.46 C ANISOU 1183 CD1 LEU A 333 1487 1803 1823 -239 117 -22 C ATOM 1184 CD2 LEU A 333 19.178 -12.475 -33.487 1.00 18.88 C ANISOU 1184 CD2 LEU A 333 2169 2453 2554 -240 78 -7 C ATOM 1185 N GLY A 334 20.782 -10.371 -29.195 1.00 13.92 N ANISOU 1185 N GLY A 334 1604 1815 1872 -180 85 -69 N ATOM 1186 CA GLY A 334 21.860 -10.853 -28.354 1.00 10.58 C ANISOU 1186 CA GLY A 334 1216 1377 1428 -172 70 -81 C ATOM 1187 C GLY A 334 21.795 -12.332 -28.006 1.00 16.48 C ANISOU 1187 C GLY A 334 1999 2119 2143 -189 65 -70 C ATOM 1188 O GLY A 334 20.727 -12.890 -27.728 1.00 12.95 O ANISOU 1188 O GLY A 334 1557 1684 1679 -212 84 -54 O ATOM 1189 N ILE A 335 22.958 -12.971 -28.029 1.00 13.64 N ANISOU 1189 N ILE A 335 1669 1746 1769 -177 37 -81 N ATOM 1190 CA ILE A 335 23.061 -14.370 -27.659 1.00 14.41 C ANISOU 1190 CA ILE A 335 1819 1831 1826 -184 24 -75 C ATOM 1191 C ILE A 335 23.872 -14.492 -26.377 1.00 18.86 C ANISOU 1191 C ILE A 335 2426 2383 2358 -157 15 -100 C ATOM 1192 O ILE A 335 24.979 -13.961 -26.276 1.00 21.07 O ANISOU 1192 O ILE A 335 2697 2666 2642 -129 -2 -126 O ATOM 1193 CB ILE A 335 23.752 -15.193 -28.761 1.00 10.07 C ANISOU 1193 CB ILE A 335 1280 1275 1271 -180 -10 -72 C ATOM 1194 CG1 ILE A 335 23.161 -14.850 -30.128 1.00 13.17 C ANISOU 1194 CG1 ILE A 335 1623 1678 1704 -198 -3 -52 C ATOM 1195 CG2 ILE A 335 23.617 -16.673 -28.454 1.00 11.03 C ANISOU 1195 CG2 ILE A 335 1469 1378 1343 -190 -26 -61 C ATOM 1196 CD1 ILE A 335 21.652 -15.079 -30.216 1.00 13.19 C ANISOU 1196 CD1 ILE A 335 1614 1687 1709 -233 27 -26 C ATOM 1197 N THR A 336 23.315 -15.183 -25.393 1.00 20.65 N ANISOU 1197 N THR A 336 2698 2599 2549 -170 26 -93 N ATOM 1198 CA THR A 336 24.020 -15.387 -24.137 1.00 26.81 C ANISOU 1198 CA THR A 336 3527 3364 3297 -142 17 -117 C ATOM 1199 C THR A 336 24.267 -16.868 -23.915 1.00 24.15 C ANISOU 1199 C THR A 336 3270 3001 2903 -143 -7 -117 C ATOM 1200 O THR A 336 23.837 -17.713 -24.708 1.00 24.77 O ANISOU 1200 O THR A 336 3367 3075 2970 -170 -17 -95 O ATOM 1201 CB THR A 336 23.232 -14.830 -22.937 1.00 29.72 C ANISOU 1201 CB THR A 336 3891 3737 3663 -149 50 -115 C ATOM 1202 OG1 THR A 336 22.308 -15.818 -22.459 1.00 28.21 O ANISOU 1202 OG1 THR A 336 3745 3540 3433 -186 63 -96 O ATOM 1203 CG2 THR A 336 22.478 -13.584 -23.332 1.00 26.05 C ANISOU 1203 CG2 THR A 336 3358 3299 3242 -156 74 -105 C ATOM 1204 N LYS A 337 24.953 -17.182 -22.827 1.00 30.03 N ANISOU 1204 N LYS A 337 4069 3728 3612 -111 -19 -143 N ATOM 1205 CA LYS A 337 25.259 -18.565 -22.503 1.00 36.83 C ANISOU 1205 CA LYS A 337 5025 4559 4409 -104 -48 -149 C ATOM 1206 C LYS A 337 23.996 -19.408 -22.300 1.00 33.60 C ANISOU 1206 C LYS A 337 4664 4134 3969 -163 -30 -115 C ATOM 1207 O LYS A 337 24.027 -20.624 -22.476 1.00 34.58 O ANISOU 1207 O LYS A 337 4868 4230 4040 -174 -56 -108 O ATOM 1208 CB LYS A 337 26.154 -18.625 -21.266 1.00 42.76 C ANISOU 1208 CB LYS A 337 5827 5295 5127 -55 -61 -187 C ATOM 1209 CG LYS A 337 25.648 -17.805 -20.100 1.00 44.51 C ANISOU 1209 CG LYS A 337 6029 5518 5367 -61 -23 -187 C ATOM 1210 CD LYS A 337 26.624 -17.860 -18.938 1.00 50.06 C ANISOU 1210 CD LYS A 337 6779 6203 6038 -6 -38 -227 C ATOM 1211 CE LYS A 337 25.995 -17.317 -17.668 1.00 55.52 C ANISOU 1211 CE LYS A 337 7470 6888 6737 -15 -3 -223 C ATOM 1212 NZ LYS A 337 26.915 -17.428 -16.503 1.00 58.84 N ANISOU 1212 NZ LYS A 337 7942 7288 7127 40 -17 -263 N ATOM 1213 N ASP A 338 22.883 -18.766 -21.950 1.00 30.89 N ANISOU 1213 N ASP A 338 4274 3811 3651 -203 13 -95 N ATOM 1214 CA ASP A 338 21.650 -19.507 -21.675 1.00 27.25 C ANISOU 1214 CA ASP A 338 3851 3349 3154 -268 35 -67 C ATOM 1215 C ASP A 338 20.367 -18.912 -22.274 1.00 23.00 C ANISOU 1215 C ASP A 338 3231 2856 2652 -315 72 -41 C ATOM 1216 O ASP A 338 19.266 -19.374 -21.968 1.00 20.50 O ANISOU 1216 O ASP A 338 2929 2555 2304 -374 97 -23 O ATOM 1217 CB ASP A 338 21.478 -19.721 -20.164 1.00 29.21 C ANISOU 1217 CB ASP A 338 4157 3581 3360 -273 50 -77 C ATOM 1218 CG ASP A 338 21.307 -18.418 -19.400 1.00 41.71 C ANISOU 1218 CG ASP A 338 5671 5193 4984 -250 80 -89 C ATOM 1219 OD1 ASP A 338 20.759 -17.451 -19.970 1.00 38.32 O ANISOU 1219 OD1 ASP A 338 5153 4802 4603 -256 101 -79 O ATOM 1220 OD2 ASP A 338 21.719 -18.365 -18.219 1.00 52.22 O ANISOU 1220 OD2 ASP A 338 7042 6505 6295 -222 81 -109 O ATOM 1221 N SER A 339 20.498 -17.905 -23.134 1.00 25.69 N ANISOU 1221 N SER A 339 3488 3221 3051 -291 75 -44 N ATOM 1222 CA SER A 339 19.307 -17.270 -23.694 1.00 20.29 C ANISOU 1222 CA SER A 339 2730 2581 2398 -323 107 -26 C ATOM 1223 C SER A 339 19.549 -16.482 -24.981 1.00 17.18 C ANISOU 1223 C SER A 339 2269 2200 2061 -300 99 -26 C ATOM 1224 O SER A 339 20.684 -16.356 -25.459 1.00 13.28 O ANISOU 1224 O SER A 339 1778 1684 1584 -263 71 -39 O ATOM 1225 CB SER A 339 18.674 -16.342 -22.649 1.00 24.36 C ANISOU 1225 CB SER A 339 3209 3129 2919 -319 139 -35 C ATOM 1226 OG SER A 339 19.466 -15.170 -22.469 1.00 19.20 O ANISOU 1226 OG SER A 339 2522 2470 2304 -262 132 -56 O ATOM 1227 N VAL A 340 18.449 -15.966 -25.524 1.00 14.94 N ANISOU 1227 N VAL A 340 1925 1955 1798 -323 125 -15 N ATOM 1228 CA VAL A 340 18.438 -15.031 -26.638 1.00 12.58 C ANISOU 1228 CA VAL A 340 1561 1668 1549 -301 124 -17 C ATOM 1229 C VAL A 340 17.574 -13.829 -26.246 1.00 15.84 C ANISOU 1229 C VAL A 340 1920 2123 1977 -289 152 -26 C ATOM 1230 O VAL A 340 16.493 -14.009 -25.681 1.00 16.18 O ANISOU 1230 O VAL A 340 1953 2203 1991 -317 178 -22 O ATOM 1231 CB VAL A 340 17.829 -15.685 -27.882 1.00 14.96 C ANISOU 1231 CB VAL A 340 1848 1979 1857 -334 124 5 C ATOM 1232 CG1 VAL A 340 17.664 -14.669 -28.988 1.00 14.90 C ANISOU 1232 CG1 VAL A 340 1776 1986 1899 -311 126 1 C ATOM 1233 CG2 VAL A 340 18.696 -16.862 -28.338 1.00 15.96 C ANISOU 1233 CG2 VAL A 340 2032 2066 1965 -338 89 14 C ATOM 1234 N MET A 341 18.041 -12.613 -26.534 1.00 16.43 N ANISOU 1234 N MET A 341 1963 2193 2088 -247 145 -41 N ATOM 1235 CA MET A 341 17.297 -11.398 -26.164 1.00 17.48 C ANISOU 1235 CA MET A 341 2056 2359 2228 -223 163 -53 C ATOM 1236 C MET A 341 17.196 -10.354 -27.287 1.00 15.36 C ANISOU 1236 C MET A 341 1749 2093 1994 -198 157 -60 C ATOM 1237 O MET A 341 18.111 -10.219 -28.091 1.00 16.99 O ANISOU 1237 O MET A 341 1962 2267 2227 -190 137 -60 O ATOM 1238 CB MET A 341 17.903 -10.754 -24.910 1.00 16.18 C ANISOU 1238 CB MET A 341 1913 2181 2056 -191 160 -70 C ATOM 1239 CG MET A 341 19.381 -10.377 -25.022 1.00 16.53 C ANISOU 1239 CG MET A 341 1979 2182 2121 -165 134 -82 C ATOM 1240 SD MET A 341 20.030 -9.415 -23.606 1.00 21.97 S ANISOU 1240 SD MET A 341 2686 2858 2804 -125 131 -103 S ATOM 1241 CE MET A 341 20.007 -10.603 -22.280 1.00 11.01 C ANISOU 1241 CE MET A 341 1343 1465 1376 -139 139 -101 C ATOM 1242 N ARG A 342 16.072 -9.636 -27.337 1.00 12.27 N ANISOU 1242 N ARG A 342 1320 1744 1597 -184 174 -68 N ATOM 1243 CA ARG A 342 15.908 -8.495 -28.237 1.00 15.62 C ANISOU 1243 CA ARG A 342 1721 2168 2045 -151 167 -80 C ATOM 1244 C ARG A 342 16.172 -7.231 -27.446 1.00 17.41 C ANISOU 1244 C ARG A 342 1961 2388 2267 -107 158 -99 C ATOM 1245 O ARG A 342 15.602 -7.050 -26.372 1.00 14.07 O ANISOU 1245 O ARG A 342 1533 1996 1815 -94 170 -106 O ATOM 1246 CB ARG A 342 14.478 -8.426 -28.792 1.00 14.42 C ANISOU 1246 CB ARG A 342 1525 2072 1881 -151 185 -84 C ATOM 1247 CG ARG A 342 14.148 -9.449 -29.865 1.00 19.05 C ANISOU 1247 CG ARG A 342 2095 2664 2478 -190 191 -67 C ATOM 1248 CD ARG A 342 12.871 -9.080 -30.621 1.00 23.23 C ANISOU 1248 CD ARG A 342 2577 3247 3002 -177 205 -79 C ATOM 1249 NE ARG A 342 11.810 -8.663 -29.717 1.00 31.71 N ANISOU 1249 NE ARG A 342 3624 4389 4035 -161 223 -100 N ATOM 1250 CZ ARG A 342 11.182 -7.492 -29.767 1.00 24.65 C ANISOU 1250 CZ ARG A 342 2709 3528 3128 -106 220 -128 C ATOM 1251 NH1 ARG A 342 11.475 -6.597 -30.703 1.00 18.54 N ANISOU 1251 NH1 ARG A 342 1946 2719 2380 -65 201 -139 N ATOM 1252 NH2 ARG A 342 10.241 -7.225 -28.880 1.00 32.56 N ANISOU 1252 NH2 ARG A 342 3684 4601 4085 -91 234 -147 N ATOM 1253 N VAL A 343 17.014 -6.349 -27.972 1.00 16.28 N ANISOU 1253 N VAL A 343 1835 2204 2145 -87 138 -107 N ATOM 1254 CA VAL A 343 17.366 -5.130 -27.249 1.00 14.46 C ANISOU 1254 CA VAL A 343 1629 1959 1907 -49 126 -123 C ATOM 1255 C VAL A 343 17.223 -3.904 -28.134 1.00 11.19 C ANISOU 1255 C VAL A 343 1223 1530 1498 -20 111 -137 C ATOM 1256 O VAL A 343 17.601 -3.930 -29.296 1.00 13.21 O ANISOU 1256 O VAL A 343 1480 1762 1777 -36 102 -133 O ATOM 1257 CB VAL A 343 18.820 -5.197 -26.694 1.00 14.20 C ANISOU 1257 CB VAL A 343 1629 1885 1883 -59 112 -124 C ATOM 1258 CG1 VAL A 343 19.246 -3.856 -26.125 1.00 16.14 C ANISOU 1258 CG1 VAL A 343 1903 2109 2120 -27 97 -140 C ATOM 1259 CG2 VAL A 343 18.939 -6.290 -25.634 1.00 12.04 C ANISOU 1259 CG2 VAL A 343 1361 1620 1593 -75 123 -117 C ATOM 1260 N ASP A 344 16.675 -2.833 -27.571 1.00 14.62 N ANISOU 1260 N ASP A 344 1670 1977 1907 25 104 -154 N ATOM 1261 CA ASP A 344 16.526 -1.565 -28.278 1.00 13.42 C ANISOU 1261 CA ASP A 344 1546 1805 1749 59 84 -170 C ATOM 1262 C ASP A 344 17.891 -0.953 -28.599 1.00 14.42 C ANISOU 1262 C ASP A 344 1719 1870 1891 40 63 -170 C ATOM 1263 O ASP A 344 18.710 -0.732 -27.703 1.00 15.44 O ANISOU 1263 O ASP A 344 1873 1980 2016 36 56 -171 O ATOM 1264 CB ASP A 344 15.690 -0.609 -27.410 1.00 24.07 C ANISOU 1264 CB ASP A 344 2907 3183 3057 119 76 -190 C ATOM 1265 CG ASP A 344 15.339 0.680 -28.123 1.00 29.62 C ANISOU 1265 CG ASP A 344 3649 3867 3738 165 51 -211 C ATOM 1266 OD1 ASP A 344 16.259 1.436 -28.486 1.00 22.94 O ANISOU 1266 OD1 ASP A 344 2857 2960 2897 157 29 -212 O ATOM 1267 OD2 ASP A 344 14.137 0.939 -28.311 1.00 38.86 O ANISOU 1267 OD2 ASP A 344 4800 5086 4880 210 52 -229 O ATOM 1268 N GLU A 345 18.139 -0.673 -29.874 1.00 12.49 N ANISOU 1268 N GLU A 345 1487 1598 1662 26 53 -171 N ATOM 1269 CA GLU A 345 19.469 -0.248 -30.309 1.00 17.08 C ANISOU 1269 CA GLU A 345 2104 2131 2255 -8 36 -171 C ATOM 1270 C GLU A 345 19.822 1.158 -29.832 1.00 17.14 C ANISOU 1270 C GLU A 345 2175 2105 2232 13 13 -186 C ATOM 1271 O GLU A 345 20.988 1.531 -29.790 1.00 15.53 O ANISOU 1271 O GLU A 345 2002 1870 2028 -21 1 -188 O ATOM 1272 CB GLU A 345 19.600 -0.334 -31.838 1.00 23.21 C ANISOU 1272 CB GLU A 345 2877 2889 3053 -31 32 -167 C ATOM 1273 CG GLU A 345 18.821 0.725 -32.599 1.00 36.54 C ANISOU 1273 CG GLU A 345 4600 4562 4723 5 19 -182 C ATOM 1274 CD GLU A 345 17.309 0.493 -32.572 1.00 53.31 C ANISOU 1274 CD GLU A 345 6689 6731 6835 52 32 -189 C ATOM 1275 OE1 GLU A 345 16.871 -0.639 -32.252 1.00 53.73 O ANISOU 1275 OE1 GLU A 345 6685 6827 6901 41 55 -177 O ATOM 1276 OE2 GLU A 345 16.556 1.448 -32.877 1.00 57.06 O ANISOU 1276 OE2 GLU A 345 7196 7203 7281 101 18 -210 O ATOM 1277 N LYS A 346 18.808 1.935 -29.480 1.00 17.81 N ANISOU 1277 N LYS A 346 2281 2201 2286 68 5 -199 N ATOM 1278 CA LYS A 346 19.037 3.308 -29.042 1.00 27.42 C ANISOU 1278 CA LYS A 346 3570 3382 3466 95 -23 -214 C ATOM 1279 C LYS A 346 19.170 3.405 -27.531 1.00 22.64 C ANISOU 1279 C LYS A 346 2967 2789 2845 116 -23 -214 C ATOM 1280 O LYS A 346 20.112 4.011 -27.020 1.00 24.79 O ANISOU 1280 O LYS A 346 3285 3028 3108 100 -38 -216 O ATOM 1281 CB LYS A 346 17.910 4.225 -29.514 1.00 30.49 C ANISOU 1281 CB LYS A 346 3995 3771 3818 156 -41 -233 C ATOM 1282 CG LYS A 346 17.821 4.369 -31.023 1.00 45.26 C ANISOU 1282 CG LYS A 346 5882 5618 5699 142 -47 -238 C ATOM 1283 CD LYS A 346 16.533 5.087 -31.424 1.00 57.83 C ANISOU 1283 CD LYS A 346 7499 7223 7250 216 -62 -263 C ATOM 1284 CE LYS A 346 16.342 5.108 -32.936 1.00 60.48 C ANISOU 1284 CE LYS A 346 7845 7537 7599 208 -64 -268 C ATOM 1285 NZ LYS A 346 14.935 5.448 -33.305 1.00 61.53 N ANISOU 1285 NZ LYS A 346 7976 7705 7698 286 -71 -296 N ATOM 1286 N THR A 347 18.224 2.805 -26.820 1.00 19.73 N ANISOU 1286 N THR A 347 2550 2473 2472 149 -6 -213 N ATOM 1287 CA THR A 347 18.172 2.928 -25.372 1.00 16.58 C ANISOU 1287 CA THR A 347 2153 2091 2056 178 -6 -214 C ATOM 1288 C THR A 347 18.836 1.758 -24.660 1.00 20.18 C ANISOU 1288 C THR A 347 2568 2558 2540 137 18 -199 C ATOM 1289 O THR A 347 19.138 1.851 -23.469 1.00 21.83 O ANISOU 1289 O THR A 347 2786 2767 2740 151 18 -199 O ATOM 1290 CB THR A 347 16.735 3.011 -24.878 1.00 23.67 C ANISOU 1290 CB THR A 347 3024 3049 2922 239 -2 -225 C ATOM 1291 OG1 THR A 347 16.122 1.722 -24.996 1.00 25.68 O ANISOU 1291 OG1 THR A 347 3206 3356 3195 215 31 -216 O ATOM 1292 CG2 THR A 347 15.954 4.043 -25.680 1.00 30.68 C ANISOU 1292 CG2 THR A 347 3949 3934 3775 290 -27 -247 C ATOM 1293 N LYS A 348 19.038 0.659 -25.388 1.00 13.88 N ANISOU 1293 N LYS A 348 1732 1769 1773 93 37 -187 N ATOM 1294 CA LYS A 348 19.632 -0.558 -24.836 1.00 14.14 C ANISOU 1294 CA LYS A 348 1736 1810 1825 58 55 -175 C ATOM 1295 C LYS A 348 18.735 -1.273 -23.826 1.00 16.61 C ANISOU 1295 C LYS A 348 2017 2169 2125 75 76 -171 C ATOM 1296 O LYS A 348 19.175 -2.191 -23.128 1.00 13.62 O ANISOU 1296 O LYS A 348 1631 1793 1752 54 88 -164 O ATOM 1297 CB LYS A 348 21.016 -0.290 -24.237 1.00 12.90 C ANISOU 1297 CB LYS A 348 1610 1618 1671 42 43 -181 C ATOM 1298 CG LYS A 348 22.115 -0.168 -25.268 1.00 12.07 C ANISOU 1298 CG LYS A 348 1519 1485 1582 -1 31 -183 C ATOM 1299 CD LYS A 348 21.938 1.071 -26.134 1.00 11.16 C ANISOU 1299 CD LYS A 348 1443 1343 1455 5 12 -191 C ATOM 1300 CE LYS A 348 23.125 1.257 -27.074 1.00 13.22 C ANISOU 1300 CE LYS A 348 1720 1579 1725 -48 0 -195 C ATOM 1301 NZ LYS A 348 22.960 2.465 -27.920 1.00 13.24 N ANISOU 1301 NZ LYS A 348 1773 1549 1710 -48 -19 -202 N ATOM 1302 N GLU A 349 17.474 -0.865 -23.760 1.00 18.54 N ANISOU 1302 N GLU A 349 2246 2453 2344 113 79 -178 N ATOM 1303 CA GLU A 349 16.484 -1.603 -22.976 1.00 22.61 C ANISOU 1303 CA GLU A 349 2722 3027 2841 118 101 -175 C ATOM 1304 C GLU A 349 16.308 -3.024 -23.509 1.00 18.96 C ANISOU 1304 C GLU A 349 2226 2584 2395 65 125 -159 C ATOM 1305 O GLU A 349 16.181 -3.232 -24.719 1.00 21.37 O ANISOU 1305 O GLU A 349 2518 2885 2716 47 125 -156 O ATOM 1306 CB GLU A 349 15.132 -0.880 -23.007 1.00 30.80 C ANISOU 1306 CB GLU A 349 3741 4120 3843 170 98 -193 C ATOM 1307 CG GLU A 349 14.070 -1.509 -22.105 1.00 40.74 C ANISOU 1307 CG GLU A 349 4954 5453 5071 173 121 -195 C ATOM 1308 CD GLU A 349 12.662 -0.981 -22.378 1.00 52.11 C ANISOU 1308 CD GLU A 349 6361 6967 6471 220 120 -218 C ATOM 1309 OE1 GLU A 349 12.524 0.102 -22.990 1.00 49.66 O ANISOU 1309 OE1 GLU A 349 6077 6643 6150 269 93 -235 O ATOM 1310 OE2 GLU A 349 11.689 -1.656 -21.978 1.00 62.01 O ANISOU 1310 OE2 GLU A 349 7565 8298 7699 206 144 -221 O ATOM 1311 N VAL A 350 16.311 -3.996 -22.605 1.00 14.38 N ANISOU 1311 N VAL A 350 1638 2019 1806 41 143 -150 N ATOM 1312 CA VAL A 350 16.013 -5.367 -22.969 1.00 18.66 C ANISOU 1312 CA VAL A 350 2159 2579 2350 -11 162 -135 C ATOM 1313 C VAL A 350 14.508 -5.513 -23.167 1.00 20.31 C ANISOU 1313 C VAL A 350 2323 2861 2532 -12 181 -139 C ATOM 1314 O VAL A 350 13.739 -5.382 -22.227 1.00 18.07 O ANISOU 1314 O VAL A 350 2022 2628 2215 4 192 -148 O ATOM 1315 CB VAL A 350 16.490 -6.359 -21.894 1.00 19.61 C ANISOU 1315 CB VAL A 350 2302 2689 2461 -37 172 -126 C ATOM 1316 CG1 VAL A 350 16.210 -7.779 -22.339 1.00 17.58 C ANISOU 1316 CG1 VAL A 350 2040 2442 2197 -93 187 -109 C ATOM 1317 CG2 VAL A 350 17.978 -6.174 -21.628 1.00 22.72 C ANISOU 1317 CG2 VAL A 350 2735 3022 2875 -28 153 -130 C ATOM 1318 N LEU A 351 14.095 -5.781 -24.398 1.00 18.53 N ANISOU 1318 N LEU A 351 2075 2647 2318 -29 185 -136 N ATOM 1319 CA LEU A 351 12.679 -5.794 -24.740 1.00 12.59 C ANISOU 1319 CA LEU A 351 1274 1970 1538 -25 201 -147 C ATOM 1320 C LEU A 351 12.062 -7.163 -24.524 1.00 15.72 C ANISOU 1320 C LEU A 351 1649 2410 1913 -89 228 -133 C ATOM 1321 O LEU A 351 10.891 -7.272 -24.187 1.00 18.71 O ANISOU 1321 O LEU A 351 1988 2870 2253 -94 247 -145 O ATOM 1322 CB LEU A 351 12.485 -5.346 -26.190 1.00 15.55 C ANISOU 1322 CB LEU A 351 1638 2338 1934 -9 191 -154 C ATOM 1323 CG LEU A 351 13.005 -3.936 -26.469 1.00 22.38 C ANISOU 1323 CG LEU A 351 2536 3157 2808 47 162 -169 C ATOM 1324 CD1 LEU A 351 12.968 -3.576 -27.953 1.00 16.91 C ANISOU 1324 CD1 LEU A 351 1845 2444 2138 56 151 -174 C ATOM 1325 CD2 LEU A 351 12.197 -2.948 -25.655 1.00 23.43 C ANISOU 1325 CD2 LEU A 351 2664 3340 2899 108 155 -195 C ATOM 1326 N GLN A 352 12.865 -8.206 -24.707 1.00 17.04 N ANISOU 1326 N GLN A 352 1848 2528 2100 -137 228 -110 N ATOM 1327 CA GLN A 352 12.368 -9.574 -24.681 1.00 20.41 C ANISOU 1327 CA GLN A 352 2271 2981 2503 -204 248 -93 C ATOM 1328 C GLN A 352 13.532 -10.537 -24.454 1.00 18.46 C ANISOU 1328 C GLN A 352 2082 2665 2268 -235 237 -73 C ATOM 1329 O GLN A 352 14.645 -10.295 -24.919 1.00 19.06 O ANISOU 1329 O GLN A 352 2183 2682 2379 -213 214 -71 O ATOM 1330 CB GLN A 352 11.658 -9.888 -26.006 1.00 21.64 C ANISOU 1330 CB GLN A 352 2391 3166 2667 -225 255 -90 C ATOM 1331 CG GLN A 352 10.685 -11.049 -25.948 1.00 28.20 C ANISOU 1331 CG GLN A 352 3204 4054 3458 -294 281 -81 C ATOM 1332 CD GLN A 352 9.805 -11.157 -27.189 1.00 40.36 C ANISOU 1332 CD GLN A 352 4696 5638 5001 -306 291 -85 C ATOM 1333 OE1 GLN A 352 10.130 -10.626 -28.252 1.00 44.63 O ANISOU 1333 OE1 GLN A 352 5229 6145 5581 -269 275 -87 O ATOM 1334 NE2 GLN A 352 8.684 -11.853 -27.056 1.00 41.83 N ANISOU 1334 NE2 GLN A 352 4851 5901 5142 -360 317 -87 N ATOM 1335 N GLU A 353 13.284 -11.619 -23.725 1.00 22.88 N ANISOU 1335 N GLU A 353 2668 3237 2791 -286 251 -62 N ATOM 1336 CA GLU A 353 14.317 -12.621 -23.491 1.00 22.78 C ANISOU 1336 CA GLU A 353 2720 3160 2776 -310 237 -47 C ATOM 1337 C GLU A 353 13.718 -14.025 -23.519 1.00 25.29 C ANISOU 1337 C GLU A 353 3065 3493 3052 -384 250 -29 C ATOM 1338 O GLU A 353 12.753 -14.308 -22.818 1.00 29.30 O ANISOU 1338 O GLU A 353 3563 4055 3516 -423 275 -30 O ATOM 1339 CB GLU A 353 15.042 -12.366 -22.154 1.00 26.51 C ANISOU 1339 CB GLU A 353 3230 3603 3239 -282 231 -57 C ATOM 1340 CG GLU A 353 16.318 -13.190 -21.975 1.00 28.17 C ANISOU 1340 CG GLU A 353 3509 3745 3449 -284 208 -52 C ATOM 1341 CD GLU A 353 17.102 -12.848 -20.713 1.00 36.33 C ANISOU 1341 CD GLU A 353 4577 4750 4477 -248 201 -67 C ATOM 1342 OE1 GLU A 353 16.549 -12.161 -19.829 1.00 44.49 O ANISOU 1342 OE1 GLU A 353 5588 5816 5501 -231 217 -76 O ATOM 1343 OE2 GLU A 353 18.273 -13.276 -20.600 1.00 32.39 O ANISOU 1343 OE2 GLU A 353 4126 4200 3979 -232 179 -73 O ATOM 1344 N TRP A 354 14.293 -14.897 -24.340 1.00 24.47 N ANISOU 1344 N TRP A 354 2998 3344 2956 -405 231 -13 N ATOM 1345 CA TRP A 354 13.885 -16.292 -24.397 1.00 21.36 C ANISOU 1345 CA TRP A 354 2650 2948 2517 -476 236 7 C ATOM 1346 C TRP A 354 15.008 -17.204 -23.889 1.00 26.55 C ANISOU 1346 C TRP A 354 3400 3534 3152 -476 209 12 C ATOM 1347 O TRP A 354 16.131 -17.137 -24.378 1.00 27.67 O ANISOU 1347 O TRP A 354 3562 3629 3325 -433 179 9 O ATOM 1348 CB TRP A 354 13.585 -16.707 -25.831 1.00 22.95 C ANISOU 1348 CB TRP A 354 2830 3153 2736 -498 230 22 C ATOM 1349 CG TRP A 354 12.530 -15.937 -26.561 1.00 26.69 C ANISOU 1349 CG TRP A 354 3219 3692 3230 -493 252 13 C ATOM 1350 CD1 TRP A 354 11.180 -16.092 -26.451 1.00 32.38 C ANISOU 1350 CD1 TRP A 354 3899 4491 3914 -540 283 10 C ATOM 1351 CD2 TRP A 354 12.738 -14.947 -27.572 1.00 30.50 C ANISOU 1351 CD2 TRP A 354 3651 4171 3767 -438 242 4 C ATOM 1352 NE1 TRP A 354 10.534 -15.242 -27.310 1.00 34.44 N ANISOU 1352 NE1 TRP A 354 4085 4799 4203 -508 292 -4 N ATOM 1353 CE2 TRP A 354 11.468 -14.529 -28.014 1.00 31.55 C ANISOU 1353 CE2 TRP A 354 3717 4377 3893 -446 266 -7 C ATOM 1354 CE3 TRP A 354 13.877 -14.364 -28.140 1.00 25.81 C ANISOU 1354 CE3 TRP A 354 3063 3522 3221 -385 215 1 C ATOM 1355 CZ2 TRP A 354 11.301 -13.553 -28.995 1.00 29.17 C ANISOU 1355 CZ2 TRP A 354 3364 4087 3632 -397 262 -20 C ATOM 1356 CZ3 TRP A 354 13.710 -13.394 -29.111 1.00 21.77 C ANISOU 1356 CZ3 TRP A 354 2501 3020 2749 -347 213 -10 C ATOM 1357 CH2 TRP A 354 12.430 -13.002 -29.533 1.00 21.96 C ANISOU 1357 CH2 TRP A 354 2468 3110 2767 -350 235 -20 C ATOM 1358 N PRO A 355 14.707 -18.068 -22.909 1.00 25.67 N ANISOU 1358 N PRO A 355 3350 3420 2982 -524 218 17 N ATOM 1359 CA PRO A 355 15.680 -19.085 -22.493 1.00 25.86 C ANISOU 1359 CA PRO A 355 3478 3375 2972 -524 188 20 C ATOM 1360 C PRO A 355 16.047 -20.028 -23.636 1.00 20.21 C ANISOU 1360 C PRO A 355 2803 2623 2252 -540 159 38 C ATOM 1361 O PRO A 355 15.182 -20.441 -24.406 1.00 19.01 O ANISOU 1361 O PRO A 355 2631 2499 2091 -592 170 56 O ATOM 1362 CB PRO A 355 14.934 -19.854 -21.395 1.00 29.08 C ANISOU 1362 CB PRO A 355 3943 3797 3310 -591 210 26 C ATOM 1363 CG PRO A 355 13.996 -18.835 -20.807 1.00 28.32 C ANISOU 1363 CG PRO A 355 3762 3775 3224 -592 248 15 C ATOM 1364 CD PRO A 355 13.568 -17.967 -21.977 1.00 24.87 C ANISOU 1364 CD PRO A 355 3227 3381 2841 -568 254 14 C ATOM 1365 N LEU A 356 17.323 -20.369 -23.749 1.00 21.86 N ANISOU 1365 N LEU A 356 3069 2774 2462 -492 119 29 N ATOM 1366 CA LEU A 356 17.744 -21.338 -24.753 1.00 19.16 C ANISOU 1366 CA LEU A 356 2775 2397 2106 -498 84 44 C ATOM 1367 C LEU A 356 16.971 -22.656 -24.641 1.00 28.93 C ANISOU 1367 C LEU A 356 4095 3624 3273 -578 85 67 C ATOM 1368 O LEU A 356 16.875 -23.392 -25.616 1.00 30.99 O ANISOU 1368 O LEU A 356 4381 3870 3523 -601 65 86 O ATOM 1369 CB LEU A 356 19.243 -21.602 -24.661 1.00 23.14 C ANISOU 1369 CB LEU A 356 3337 2850 2604 -431 38 23 C ATOM 1370 CG LEU A 356 20.132 -20.615 -25.415 1.00 34.58 C ANISOU 1370 CG LEU A 356 4711 4308 4118 -366 24 7 C ATOM 1371 CD1 LEU A 356 21.569 -21.079 -25.395 1.00 36.54 C ANISOU 1371 CD1 LEU A 356 5019 4521 4345 -306 -25 -16 C ATOM 1372 CD2 LEU A 356 19.651 -20.460 -26.847 1.00 33.69 C ANISOU 1372 CD2 LEU A 356 4536 4218 4047 -382 26 27 C ATOM 1373 N THR A 357 16.418 -22.949 -23.462 1.00 36.08 N ANISOU 1373 N THR A 357 5046 4536 4127 -624 107 66 N ATOM 1374 CA THR A 357 15.650 -24.183 -23.276 1.00 36.61 C ANISOU 1374 CA THR A 357 5200 4594 4116 -714 111 87 C ATOM 1375 C THR A 357 14.250 -24.106 -23.892 1.00 40.85 C ANISOU 1375 C THR A 357 5663 5200 4657 -791 149 106 C ATOM 1376 O THR A 357 13.506 -25.090 -23.876 1.00 44.74 O ANISOU 1376 O THR A 357 6217 5697 5085 -879 156 125 O ATOM 1377 CB THR A 357 15.515 -24.594 -21.788 1.00 30.28 C ANISOU 1377 CB THR A 357 4481 3777 3249 -748 123 78 C ATOM 1378 OG1 THR A 357 14.768 -23.603 -21.070 1.00 33.20 O ANISOU 1378 OG1 THR A 357 4761 4213 3642 -758 170 68 O ATOM 1379 CG2 THR A 357 16.879 -24.781 -21.139 1.00 33.59 C ANISOU 1379 CG2 THR A 357 4983 4127 3654 -671 83 55 C ATOM 1380 N THR A 358 13.889 -22.942 -24.424 1.00 36.22 N ANISOU 1380 N THR A 358 4952 4671 4140 -758 173 98 N ATOM 1381 CA THR A 358 12.595 -22.780 -25.089 1.00 31.91 C ANISOU 1381 CA THR A 358 4327 4198 3599 -815 208 108 C ATOM 1382 C THR A 358 12.744 -22.745 -26.606 1.00 31.25 C ANISOU 1382 C THR A 358 4202 4107 3566 -791 189 120 C ATOM 1383 O THR A 358 11.757 -22.618 -27.335 1.00 32.15 O ANISOU 1383 O THR A 358 4248 4277 3689 -828 213 126 O ATOM 1384 CB THR A 358 11.866 -21.495 -24.641 1.00 33.69 C ANISOU 1384 CB THR A 358 4442 4504 3855 -796 248 87 C ATOM 1385 OG1 THR A 358 12.588 -20.343 -25.101 1.00 32.31 O ANISOU 1385 OG1 THR A 358 4202 4317 3756 -702 236 72 O ATOM 1386 CG2 THR A 358 11.738 -21.449 -23.132 1.00 28.09 C ANISOU 1386 CG2 THR A 358 3765 3806 3101 -813 266 75 C ATOM 1387 N VAL A 359 13.977 -22.859 -27.085 1.00 33.03 N ANISOU 1387 N VAL A 359 4464 4267 3819 -726 147 120 N ATOM 1388 CA VAL A 359 14.225 -22.814 -28.517 1.00 28.88 C ANISOU 1388 CA VAL A 359 3901 3731 3341 -698 126 131 C ATOM 1389 C VAL A 359 14.211 -24.211 -29.113 1.00 31.77 C ANISOU 1389 C VAL A 359 4354 4057 3659 -745 97 158 C ATOM 1390 O VAL A 359 15.047 -25.044 -28.779 1.00 32.12 O ANISOU 1390 O VAL A 359 4504 4041 3660 -732 57 160 O ATOM 1391 CB VAL A 359 15.561 -22.135 -28.854 1.00 29.18 C ANISOU 1391 CB VAL A 359 3920 3732 3434 -605 95 115 C ATOM 1392 CG1 VAL A 359 15.884 -22.327 -30.323 1.00 26.07 C ANISOU 1392 CG1 VAL A 359 3505 3322 3077 -583 68 128 C ATOM 1393 CG2 VAL A 359 15.507 -20.658 -28.508 1.00 31.67 C ANISOU 1393 CG2 VAL A 359 4146 4086 3801 -561 122 91 C ATOM 1394 N LYS A 360 13.255 -24.454 -30.002 1.00 30.52 N ANISOU 1394 N LYS A 360 4157 3935 3505 -795 113 176 N ATOM 1395 CA LYS A 360 13.067 -25.767 -30.593 1.00 34.66 C ANISOU 1395 CA LYS A 360 4764 4426 3980 -850 88 204 C ATOM 1396 C LYS A 360 14.057 -25.996 -31.725 1.00 35.11 C ANISOU 1396 C LYS A 360 4835 4432 4074 -784 38 213 C ATOM 1397 O LYS A 360 14.662 -27.066 -31.825 1.00 34.42 O ANISOU 1397 O LYS A 360 4855 4285 3937 -784 -8 227 O ATOM 1398 CB LYS A 360 11.635 -25.907 -31.110 1.00 39.34 C ANISOU 1398 CB LYS A 360 5300 5085 4561 -932 127 217 C ATOM 1399 CG LYS A 360 11.247 -27.312 -31.543 1.00 48.19 C ANISOU 1399 CG LYS A 360 6516 6178 5617 -1011 107 248 C ATOM 1400 CD LYS A 360 9.774 -27.360 -31.907 1.00 58.28 C ANISOU 1400 CD LYS A 360 7729 7538 6879 -1099 153 254 C ATOM 1401 CE LYS A 360 9.384 -28.683 -32.536 1.00 65.17 C ANISOU 1401 CE LYS A 360 8686 8383 7693 -1178 132 287 C ATOM 1402 NZ LYS A 360 7.953 -28.680 -32.954 1.00 67.37 N ANISOU 1402 NZ LYS A 360 8888 8751 7957 -1264 179 289 N ATOM 1403 N ARG A 361 14.210 -24.988 -32.581 1.00 31.53 N ANISOU 1403 N ARG A 361 4276 4003 3701 -727 46 204 N ATOM 1404 CA ARG A 361 15.165 -25.044 -33.684 1.00 25.87 C ANISOU 1404 CA ARG A 361 3555 3248 3024 -662 3 209 C ATOM 1405 C ARG A 361 15.411 -23.651 -34.272 1.00 27.09 C ANISOU 1405 C ARG A 361 3597 3432 3265 -600 19 190 C ATOM 1406 O ARG A 361 14.718 -22.686 -33.939 1.00 26.82 O ANISOU 1406 O ARG A 361 3487 3445 3256 -607 62 175 O ATOM 1407 CB ARG A 361 14.657 -25.981 -34.774 1.00 31.95 C ANISOU 1407 CB ARG A 361 4351 4009 3782 -702 -13 240 C ATOM 1408 CG ARG A 361 13.266 -25.625 -35.263 1.00 39.16 C ANISOU 1408 CG ARG A 361 5179 4984 4717 -757 36 247 C ATOM 1409 CD ARG A 361 12.749 -26.599 -36.311 1.00 41.27 C ANISOU 1409 CD ARG A 361 5474 5240 4967 -801 20 278 C ATOM 1410 NE ARG A 361 11.479 -26.144 -36.866 1.00 40.77 N ANISOU 1410 NE ARG A 361 5315 5245 4931 -842 67 277 N ATOM 1411 CZ ARG A 361 10.934 -26.615 -37.981 1.00 38.84 C ANISOU 1411 CZ ARG A 361 5054 5006 4697 -866 64 297 C ATOM 1412 NH1 ARG A 361 11.555 -27.560 -38.671 1.00 34.39 N ANISOU 1412 NH1 ARG A 361 4565 4380 4120 -854 13 324 N ATOM 1413 NH2 ARG A 361 9.771 -26.137 -38.411 1.00 36.43 N ANISOU 1413 NH2 ARG A 361 4658 4772 4414 -897 109 288 N ATOM 1414 N TRP A 362 16.405 -23.547 -35.144 1.00 23.01 N ANISOU 1414 N TRP A 362 3071 2888 2786 -540 -18 189 N ATOM 1415 CA TRP A 362 16.692 -22.278 -35.795 1.00 24.59 C ANISOU 1415 CA TRP A 362 3176 3108 3060 -488 -7 172 C ATOM 1416 C TRP A 362 17.185 -22.540 -37.197 1.00 21.97 C ANISOU 1416 C TRP A 362 2829 2756 2761 -457 -40 186 C ATOM 1417 O TRP A 362 17.607 -23.649 -37.517 1.00 23.06 O ANISOU 1417 O TRP A 362 3037 2862 2863 -457 -81 203 O ATOM 1418 CB TRP A 362 17.748 -21.491 -35.017 1.00 25.96 C ANISOU 1418 CB TRP A 362 3347 3275 3244 -437 -14 143 C ATOM 1419 CG TRP A 362 19.018 -22.259 -34.843 1.00 28.66 C ANISOU 1419 CG TRP A 362 3763 3577 3549 -401 -66 138 C ATOM 1420 CD1 TRP A 362 20.106 -22.244 -35.666 1.00 27.86 C ANISOU 1420 CD1 TRP A 362 3654 3464 3468 -348 -105 131 C ATOM 1421 CD2 TRP A 362 19.321 -23.181 -33.792 1.00 28.84 C ANISOU 1421 CD2 TRP A 362 3885 3572 3501 -411 -86 135 C ATOM 1422 NE1 TRP A 362 21.076 -23.092 -35.183 1.00 34.84 N ANISOU 1422 NE1 TRP A 362 4620 4321 4296 -319 -151 120 N ATOM 1423 CE2 TRP A 362 20.618 -23.680 -34.034 1.00 34.68 C ANISOU 1423 CE2 TRP A 362 4673 4286 4219 -355 -140 123 C ATOM 1424 CE3 TRP A 362 18.626 -23.628 -32.664 1.00 28.09 C ANISOU 1424 CE3 TRP A 362 3845 3475 3353 -462 -64 139 C ATOM 1425 CZ2 TRP A 362 21.234 -24.603 -33.187 1.00 33.12 C ANISOU 1425 CZ2 TRP A 362 4580 4055 3947 -341 -175 112 C ATOM 1426 CZ3 TRP A 362 19.239 -24.544 -31.824 1.00 32.36 C ANISOU 1426 CZ3 TRP A 362 4494 3977 3824 -456 -96 132 C ATOM 1427 CH2 TRP A 362 20.530 -25.022 -32.091 1.00 31.88 C ANISOU 1427 CH2 TRP A 362 4485 3886 3742 -391 -153 118 C ATOM 1428 N ALA A 363 17.130 -21.508 -38.030 1.00 19.89 N ANISOU 1428 N ALA A 363 2482 2512 2562 -428 -25 177 N ATOM 1429 CA ALA A 363 17.551 -21.614 -39.411 1.00 17.23 C ANISOU 1429 CA ALA A 363 2121 2161 2264 -397 -52 189 C ATOM 1430 C ALA A 363 18.189 -20.309 -39.866 1.00 18.83 C ANISOU 1430 C ALA A 363 2257 2372 2524 -350 -48 166 C ATOM 1431 O ALA A 363 17.908 -19.237 -39.328 1.00 26.45 O ANISOU 1431 O ALA A 363 3184 3359 3508 -347 -16 146 O ATOM 1432 CB ALA A 363 16.364 -21.955 -40.294 1.00 29.05 C ANISOU 1432 CB ALA A 363 3589 3672 3776 -434 -33 212 C ATOM 1433 N ALA A 364 19.064 -20.407 -40.855 1.00 16.70 N ANISOU 1433 N ALA A 364 1979 2089 2278 -314 -83 169 N ATOM 1434 CA ALA A 364 19.685 -19.226 -41.425 1.00 17.72 C ANISOU 1434 CA ALA A 364 2051 2225 2456 -279 -81 149 C ATOM 1435 C ALA A 364 19.772 -19.369 -42.930 1.00 21.55 C ANISOU 1435 C ALA A 364 2505 2703 2981 -263 -99 164 C ATOM 1436 O ALA A 364 19.892 -20.476 -43.453 1.00 25.91 O ANISOU 1436 O ALA A 364 3090 3241 3514 -261 -131 186 O ATOM 1437 CB ALA A 364 21.071 -19.022 -40.841 1.00 11.11 C ANISOU 1437 CB ALA A 364 1235 1388 1599 -249 -109 124 C ATOM 1438 N SER A 365 19.686 -18.235 -43.611 1.00 26.35 N ANISOU 1438 N SER A 365 3056 3317 3638 -250 -81 152 N ATOM 1439 CA SER A 365 19.924 -18.147 -45.039 1.00 29.35 C ANISOU 1439 CA SER A 365 3402 3689 4059 -230 -97 161 C ATOM 1440 C SER A 365 20.956 -17.045 -45.160 1.00 32.49 C ANISOU 1440 C SER A 365 3776 4092 4475 -209 -103 135 C ATOM 1441 O SER A 365 21.265 -16.391 -44.172 1.00 29.21 O ANISOU 1441 O SER A 365 3369 3686 4044 -213 -91 112 O ATOM 1442 CB SER A 365 18.649 -17.738 -45.762 1.00 29.17 C ANISOU 1442 CB SER A 365 3340 3669 4075 -240 -63 169 C ATOM 1443 OG SER A 365 18.367 -16.369 -45.523 1.00 26.93 O ANISOU 1443 OG SER A 365 3026 3393 3812 -233 -31 143 O ATOM 1444 N PRO A 366 21.502 -16.823 -46.360 1.00 33.72 N ANISOU 1444 N PRO A 366 3904 4246 4663 -192 -122 136 N ATOM 1445 CA PRO A 366 22.525 -15.775 -46.408 1.00 26.80 C ANISOU 1445 CA PRO A 366 3009 3380 3793 -185 -127 108 C ATOM 1446 C PRO A 366 21.971 -14.389 -46.101 1.00 20.29 C ANISOU 1446 C PRO A 366 2171 2548 2988 -196 -88 90 C ATOM 1447 O PRO A 366 22.743 -13.443 -46.097 1.00 19.51 O ANISOU 1447 O PRO A 366 2067 2455 2892 -199 -90 67 O ATOM 1448 CB PRO A 366 23.027 -15.834 -47.855 1.00 30.83 C ANISOU 1448 CB PRO A 366 3490 3889 4333 -170 -151 116 C ATOM 1449 CG PRO A 366 22.693 -17.221 -48.315 1.00 36.19 C ANISOU 1449 CG PRO A 366 4184 4561 5005 -158 -175 147 C ATOM 1450 CD PRO A 366 21.396 -17.562 -47.629 1.00 32.98 C ANISOU 1450 CD PRO A 366 3798 4143 4591 -179 -144 161 C ATOM 1451 N LYS A 367 20.671 -14.260 -45.842 1.00 19.39 N ANISOU 1451 N LYS A 367 2055 2429 2883 -202 -56 96 N ATOM 1452 CA LYS A 367 20.092 -12.927 -45.654 1.00 17.57 C ANISOU 1452 CA LYS A 367 1816 2194 2666 -200 -25 75 C ATOM 1453 C LYS A 367 19.114 -12.816 -44.483 1.00 15.87 C ANISOU 1453 C LYS A 367 1611 1993 2427 -207 4 69 C ATOM 1454 O LYS A 367 18.551 -11.747 -44.219 1.00 16.39 O ANISOU 1454 O LYS A 367 1672 2060 2494 -198 26 49 O ATOM 1455 CB LYS A 367 19.403 -12.471 -46.933 1.00 21.06 C ANISOU 1455 CB LYS A 367 2234 2621 3148 -187 -15 78 C ATOM 1456 CG LYS A 367 20.318 -12.372 -48.138 1.00 32.44 C ANISOU 1456 CG LYS A 367 3662 4048 4614 -182 -40 81 C ATOM 1457 CD LYS A 367 19.561 -11.772 -49.311 1.00 42.79 C ANISOU 1457 CD LYS A 367 4956 5339 5963 -166 -26 79 C ATOM 1458 CE LYS A 367 20.431 -11.654 -50.548 1.00 47.07 C ANISOU 1458 CE LYS A 367 5487 5867 6530 -163 -50 83 C ATOM 1459 NZ LYS A 367 19.739 -10.849 -51.600 1.00 48.72 N ANISOU 1459 NZ LYS A 367 5691 6049 6772 -146 -35 74 N ATOM 1460 N SER A 368 18.913 -13.915 -43.773 1.00 15.91 N ANISOU 1460 N SER A 368 1632 2009 2403 -222 1 84 N ATOM 1461 CA SER A 368 17.958 -13.910 -42.683 1.00 22.62 C ANISOU 1461 CA SER A 368 2489 2880 3226 -235 29 79 C ATOM 1462 C SER A 368 18.355 -14.908 -41.623 1.00 18.33 C ANISOU 1462 C SER A 368 1984 2340 2641 -254 18 88 C ATOM 1463 O SER A 368 19.189 -15.780 -41.854 1.00 16.78 O ANISOU 1463 O SER A 368 1811 2132 2434 -253 -14 101 O ATOM 1464 CB SER A 368 16.559 -14.248 -43.209 1.00 25.96 C ANISOU 1464 CB SER A 368 2885 3320 3657 -244 53 90 C ATOM 1465 OG SER A 368 16.529 -15.563 -43.740 1.00 26.09 O ANISOU 1465 OG SER A 368 2912 3330 3670 -262 36 118 O ATOM 1466 N PHE A 369 17.739 -14.771 -40.459 1.00 14.40 N ANISOU 1466 N PHE A 369 1495 1860 2114 -267 41 80 N ATOM 1467 CA PHE A 369 17.901 -15.726 -39.386 1.00 15.46 C ANISOU 1467 CA PHE A 369 1673 1997 2203 -288 35 88 C ATOM 1468 C PHE A 369 16.550 -15.887 -38.697 1.00 13.07 C ANISOU 1468 C PHE A 369 1364 1726 1876 -318 70 90 C ATOM 1469 O PHE A 369 15.837 -14.902 -38.496 1.00 15.15 O ANISOU 1469 O PHE A 369 1594 2014 2148 -307 96 72 O ATOM 1470 CB PHE A 369 18.967 -15.245 -38.385 1.00 8.91 C ANISOU 1470 CB PHE A 369 868 1160 1358 -272 24 67 C ATOM 1471 CG PHE A 369 19.072 -16.113 -37.179 1.00 12.50 C ANISOU 1471 CG PHE A 369 1372 1613 1763 -289 20 71 C ATOM 1472 CD1 PHE A 369 19.818 -17.281 -37.216 1.00 14.78 C ANISOU 1472 CD1 PHE A 369 1709 1884 2023 -288 -15 81 C ATOM 1473 CD2 PHE A 369 18.383 -15.795 -36.023 1.00 13.78 C ANISOU 1473 CD2 PHE A 369 1539 1794 1904 -302 49 62 C ATOM 1474 CE1 PHE A 369 19.890 -18.100 -36.118 1.00 13.88 C ANISOU 1474 CE1 PHE A 369 1653 1762 1858 -302 -21 82 C ATOM 1475 CE2 PHE A 369 18.451 -16.611 -34.919 1.00 15.72 C ANISOU 1475 CE2 PHE A 369 1836 2035 2102 -321 46 65 C ATOM 1476 CZ PHE A 369 19.207 -17.768 -34.965 1.00 18.84 C ANISOU 1476 CZ PHE A 369 2286 2405 2467 -322 11 75 C ATOM 1477 N THR A 370 16.209 -17.117 -38.321 1.00 10.97 N ANISOU 1477 N THR A 370 1135 1461 1570 -355 67 110 N ATOM 1478 CA THR A 370 14.878 -17.416 -37.799 1.00 12.52 C ANISOU 1478 CA THR A 370 1323 1698 1737 -397 100 113 C ATOM 1479 C THR A 370 14.931 -18.343 -36.595 1.00 18.82 C ANISOU 1479 C THR A 370 2183 2492 2476 -435 98 121 C ATOM 1480 O THR A 370 15.670 -19.328 -36.592 1.00 15.06 O ANISOU 1480 O THR A 370 1767 1979 1977 -442 66 136 O ATOM 1481 CB THR A 370 13.979 -18.056 -38.894 1.00 20.64 C ANISOU 1481 CB THR A 370 2329 2741 2774 -423 107 132 C ATOM 1482 OG1 THR A 370 13.809 -17.128 -39.963 1.00 19.74 O ANISOU 1482 OG1 THR A 370 2158 2631 2711 -385 113 120 O ATOM 1483 CG2 THR A 370 12.618 -18.412 -38.349 1.00 21.76 C ANISOU 1483 CG2 THR A 370 2457 2935 2874 -476 142 131 C ATOM 1484 N LEU A 371 14.151 -18.010 -35.570 1.00 16.87 N ANISOU 1484 N LEU A 371 1924 2284 2201 -457 130 108 N ATOM 1485 CA LEU A 371 14.037 -18.851 -34.388 1.00 17.77 C ANISOU 1485 CA LEU A 371 2098 2399 2256 -501 133 114 C ATOM 1486 C LEU A 371 12.633 -19.426 -34.286 1.00 16.03 C ANISOU 1486 C LEU A 371 1865 2230 1996 -568 165 123 C ATOM 1487 O LEU A 371 11.657 -18.706 -34.454 1.00 15.42 O ANISOU 1487 O LEU A 371 1719 2210 1930 -567 196 107 O ATOM 1488 CB LEU A 371 14.347 -18.057 -33.122 1.00 17.63 C ANISOU 1488 CB LEU A 371 2082 2388 2229 -477 144 91 C ATOM 1489 CG LEU A 371 15.810 -17.741 -32.839 1.00 17.67 C ANISOU 1489 CG LEU A 371 2118 2346 2250 -428 113 81 C ATOM 1490 CD1 LEU A 371 15.906 -16.654 -31.790 1.00 18.43 C ANISOU 1490 CD1 LEU A 371 2195 2458 2350 -400 130 56 C ATOM 1491 CD2 LEU A 371 16.557 -18.982 -32.396 1.00 11.90 C ANISOU 1491 CD2 LEU A 371 1473 1573 1474 -442 83 92 C ATOM 1492 N ASP A 372 12.558 -20.728 -34.020 1.00 18.42 N ANISOU 1492 N ASP A 372 2239 2513 2246 -625 154 146 N ATOM 1493 CA ASP A 372 11.302 -21.445 -33.763 1.00 28.41 C ANISOU 1493 CA ASP A 372 3510 3828 3458 -707 183 155 C ATOM 1494 C ASP A 372 11.269 -21.865 -32.291 1.00 24.24 C ANISOU 1494 C ASP A 372 3043 3301 2865 -750 192 152 C ATOM 1495 O ASP A 372 12.094 -22.664 -31.851 1.00 29.91 O ANISOU 1495 O ASP A 372 3854 3959 3551 -754 160 164 O ATOM 1496 CB ASP A 372 11.209 -22.675 -34.686 1.00 33.50 C ANISOU 1496 CB ASP A 372 4203 4443 4084 -750 160 186 C ATOM 1497 CG ASP A 372 10.051 -23.625 -34.334 1.00 36.45 C ANISOU 1497 CG ASP A 372 4606 4858 4386 -852 184 200 C ATOM 1498 OD1 ASP A 372 9.207 -23.306 -33.467 1.00 29.79 O ANISOU 1498 OD1 ASP A 372 3730 4080 3508 -893 223 182 O ATOM 1499 OD2 ASP A 372 9.990 -24.714 -34.948 1.00 34.40 O ANISOU 1499 OD2 ASP A 372 4403 4568 4099 -895 163 227 O ATOM 1500 N PHE A 373 10.326 -21.311 -31.534 1.00 23.96 N ANISOU 1500 N PHE A 373 2957 3337 2809 -775 232 133 N ATOM 1501 CA PHE A 373 10.213 -21.589 -30.102 1.00 24.98 C ANISOU 1501 CA PHE A 373 3135 3476 2879 -815 245 127 C ATOM 1502 C PHE A 373 9.196 -22.690 -29.786 1.00 33.26 C ANISOU 1502 C PHE A 373 4225 4563 3850 -925 266 142 C ATOM 1503 O PHE A 373 8.707 -22.793 -28.655 1.00 28.52 O ANISOU 1503 O PHE A 373 3641 4001 3196 -973 289 133 O ATOM 1504 CB PHE A 373 9.816 -20.324 -29.350 1.00 26.40 C ANISOU 1504 CB PHE A 373 3240 3717 3074 -777 274 96 C ATOM 1505 CG PHE A 373 10.708 -19.152 -29.616 1.00 31.96 C ANISOU 1505 CG PHE A 373 3907 4388 3847 -679 257 80 C ATOM 1506 CD1 PHE A 373 11.966 -19.079 -29.045 1.00 28.36 C ANISOU 1506 CD1 PHE A 373 3508 3866 3403 -635 229 79 C ATOM 1507 CD2 PHE A 373 10.279 -18.107 -30.421 1.00 35.99 C ANISOU 1507 CD2 PHE A 373 4332 4939 4405 -633 268 63 C ATOM 1508 CE1 PHE A 373 12.789 -17.987 -29.277 1.00 30.14 C ANISOU 1508 CE1 PHE A 373 3700 4066 3685 -557 215 64 C ATOM 1509 CE2 PHE A 373 11.098 -17.014 -30.657 1.00 32.18 C ANISOU 1509 CE2 PHE A 373 3826 4422 3977 -552 251 49 C ATOM 1510 CZ PHE A 373 12.355 -16.957 -30.083 1.00 28.83 C ANISOU 1510 CZ PHE A 373 3456 3935 3564 -519 225 50 C ATOM 1511 N GLY A 374 8.870 -23.498 -30.789 1.00 39.13 N ANISOU 1511 N GLY A 374 4984 5298 4583 -968 256 164 N ATOM 1512 CA GLY A 374 7.941 -24.599 -30.615 1.00 44.07 C ANISOU 1512 CA GLY A 374 5657 5957 5131 -1082 273 180 C ATOM 1513 C GLY A 374 6.635 -24.237 -29.925 1.00 47.96 C ANISOU 1513 C GLY A 374 6079 6563 5580 -1145 325 158 C ATOM 1514 O GLY A 374 5.841 -23.449 -30.440 1.00 45.70 O ANISOU 1514 O GLY A 374 5682 6359 5323 -1125 353 136 O ATOM 1515 N GLU A 375 6.419 -24.816 -28.748 1.00 50.25 N ANISOU 1515 N GLU A 375 6437 6860 5794 -1217 337 160 N ATOM 1516 CA GLU A 375 5.136 -24.712 -28.056 1.00 50.96 C ANISOU 1516 CA GLU A 375 6471 7066 5823 -1298 385 140 C ATOM 1517 C GLU A 375 5.004 -23.464 -27.186 1.00 48.96 C ANISOU 1517 C GLU A 375 6136 6873 5592 -1235 408 105 C ATOM 1518 O GLU A 375 3.948 -23.218 -26.604 1.00 48.86 O ANISOU 1518 O GLU A 375 6062 6971 5532 -1285 447 82 O ATOM 1519 CB GLU A 375 4.895 -25.962 -27.204 1.00 53.61 C ANISOU 1519 CB GLU A 375 6925 7386 6058 -1418 388 159 C ATOM 1520 CG GLU A 375 5.055 -27.268 -27.965 1.00 59.44 C ANISOU 1520 CG GLU A 375 7768 8055 6761 -1484 359 196 C ATOM 1521 CD GLU A 375 4.895 -28.484 -27.075 1.00 64.28 C ANISOU 1521 CD GLU A 375 8519 8639 7265 -1601 356 214 C ATOM 1522 OE1 GLU A 375 3.795 -28.668 -26.511 1.00 59.19 O ANISOU 1522 OE1 GLU A 375 7849 8090 6550 -1708 398 204 O ATOM 1523 OE2 GLU A 375 5.868 -29.258 -26.946 1.00 69.99 O ANISOU 1523 OE2 GLU A 375 9378 9246 7968 -1588 310 236 O ATOM 1524 N TYR A 376 6.070 -22.675 -27.101 1.00 43.69 N ANISOU 1524 N TYR A 376 5467 6139 4992 -1125 383 99 N ATOM 1525 CA TYR A 376 6.073 -21.503 -26.230 1.00 38.12 C ANISOU 1525 CA TYR A 376 4702 5476 4308 -1060 398 70 C ATOM 1526 C TYR A 376 5.401 -20.282 -26.856 1.00 39.45 C ANISOU 1526 C TYR A 376 4742 5729 4520 -997 416 39 C ATOM 1527 O TYR A 376 4.954 -19.383 -26.147 1.00 38.63 O ANISOU 1527 O TYR A 376 4576 5695 4407 -963 435 10 O ATOM 1528 CB TYR A 376 7.495 -21.173 -25.770 1.00 33.75 C ANISOU 1528 CB TYR A 376 4207 4818 3797 -978 364 74 C ATOM 1529 CG TYR A 376 8.010 -22.123 -24.715 1.00 31.52 C ANISOU 1529 CG TYR A 376 4043 4475 3458 -1026 352 89 C ATOM 1530 CD1 TYR A 376 8.624 -23.321 -25.065 1.00 25.52 C ANISOU 1530 CD1 TYR A 376 3394 3629 2672 -1062 320 116 C ATOM 1531 CD2 TYR A 376 7.874 -21.825 -23.364 1.00 36.26 C ANISOU 1531 CD2 TYR A 376 4650 5103 4025 -1032 370 73 C ATOM 1532 CE1 TYR A 376 9.095 -24.197 -24.091 1.00 27.18 C ANISOU 1532 CE1 TYR A 376 3726 3780 2821 -1101 305 126 C ATOM 1533 CE2 TYR A 376 8.344 -22.690 -22.384 1.00 34.56 C ANISOU 1533 CE2 TYR A 376 4550 4827 3754 -1074 359 84 C ATOM 1534 CZ TYR A 376 8.949 -23.873 -22.750 1.00 31.83 C ANISOU 1534 CZ TYR A 376 4321 4394 3380 -1108 327 109 C ATOM 1535 OH TYR A 376 9.406 -24.727 -21.767 1.00 33.07 O ANISOU 1535 OH TYR A 376 4604 4488 3473 -1144 312 116 O ATOM 1536 N GLN A 377 5.332 -20.254 -28.181 1.00 40.67 N ANISOU 1536 N GLN A 377 4862 5875 4716 -976 407 44 N ATOM 1537 CA GLN A 377 4.593 -19.210 -28.883 1.00 44.97 C ANISOU 1537 CA GLN A 377 5295 6500 5291 -920 422 13 C ATOM 1538 C GLN A 377 4.268 -19.650 -30.312 1.00 47.85 C ANISOU 1538 C GLN A 377 5639 6865 5678 -938 419 24 C ATOM 1539 O GLN A 377 4.933 -20.528 -30.867 1.00 42.48 O ANISOU 1539 O GLN A 377 5030 6098 5011 -963 394 59 O ATOM 1540 CB GLN A 377 5.343 -17.868 -28.855 1.00 49.05 C ANISOU 1540 CB GLN A 377 5784 6979 5873 -801 403 -6 C ATOM 1541 CG GLN A 377 6.608 -17.810 -29.702 1.00 56.33 C ANISOU 1541 CG GLN A 377 6750 7787 6867 -743 366 16 C ATOM 1542 CD GLN A 377 7.150 -16.389 -29.858 1.00 58.00 C ANISOU 1542 CD GLN A 377 6924 7977 7136 -636 351 -7 C ATOM 1543 OE1 GLN A 377 7.689 -15.805 -28.914 1.00 53.16 O ANISOU 1543 OE1 GLN A 377 6329 7343 6525 -598 345 -15 O ATOM 1544 NE2 GLN A 377 7.013 -15.833 -31.060 1.00 53.19 N ANISOU 1544 NE2 GLN A 377 6270 7371 6571 -590 345 -16 N ATOM 1545 N GLU A 378 3.240 -19.042 -30.897 1.00 55.64 N ANISOU 1545 N GLU A 378 6528 7950 6664 -920 442 -8 N ATOM 1546 CA GLU A 378 2.697 -19.491 -32.180 1.00 62.87 C ANISOU 1546 CA GLU A 378 7412 8885 7589 -946 446 -2 C ATOM 1547 C GLU A 378 3.582 -19.177 -33.385 1.00 58.83 C ANISOU 1547 C GLU A 378 6911 8278 7162 -867 413 13 C ATOM 1548 O GLU A 378 3.713 -19.993 -34.296 1.00 59.30 O ANISOU 1548 O GLU A 378 7001 8296 7236 -900 401 41 O ATOM 1549 CB GLU A 378 1.302 -18.896 -32.400 1.00 74.20 C ANISOU 1549 CB GLU A 378 8736 10465 8992 -943 480 -49 C ATOM 1550 CG GLU A 378 1.268 -17.373 -32.388 1.00 80.86 C ANISOU 1550 CG GLU A 378 9513 11340 9870 -823 476 -92 C ATOM 1551 CD GLU A 378 -0.143 -16.819 -32.455 0.50 88.38 C ANISOU 1551 CD GLU A 378 10359 12447 10772 -813 506 -146 C ATOM 1552 OE1 GLU A 378 -1.000 -17.444 -33.115 0.50 90.12 O ANISOU 1552 OE1 GLU A 378 10541 12737 10962 -874 527 -153 O ATOM 1553 OE2 GLU A 378 -0.395 -15.755 -31.848 0.50 90.82 O ANISOU 1553 OE2 GLU A 378 10626 12814 11069 -742 508 -185 O ATOM 1554 N SER A 379 4.183 -17.993 -33.390 1.00 51.35 N ANISOU 1554 N SER A 379 5944 7300 6268 -766 398 -5 N ATOM 1555 CA SER A 379 4.902 -17.513 -34.565 1.00 48.36 C ANISOU 1555 CA SER A 379 5562 6847 5964 -691 371 1 C ATOM 1556 C SER A 379 6.416 -17.627 -34.420 1.00 36.87 C ANISOU 1556 C SER A 379 4185 5274 4550 -661 335 30 C ATOM 1557 O SER A 379 6.943 -17.560 -33.313 1.00 33.87 O ANISOU 1557 O SER A 379 3846 4872 4152 -662 330 32 O ATOM 1558 CB SER A 379 4.524 -16.059 -34.837 1.00 54.34 C ANISOU 1558 CB SER A 379 6249 7651 6748 -599 376 -42 C ATOM 1559 OG SER A 379 4.621 -15.290 -33.647 1.00 60.00 O ANISOU 1559 OG SER A 379 6965 8390 7444 -567 379 -63 O ATOM 1560 N TYR A 380 7.103 -17.799 -35.548 1.00 29.21 N ANISOU 1560 N TYR A 380 3232 4234 3632 -634 309 50 N ATOM 1561 CA TYR A 380 8.561 -17.746 -35.584 1.00 31.36 C ANISOU 1561 CA TYR A 380 3563 4408 3945 -592 272 68 C ATOM 1562 C TYR A 380 9.051 -16.314 -35.374 1.00 26.41 C ANISOU 1562 C TYR A 380 2908 3770 3355 -511 267 41 C ATOM 1563 O TYR A 380 8.296 -15.361 -35.538 1.00 25.71 O ANISOU 1563 O TYR A 380 2760 3737 3270 -474 284 11 O ATOM 1564 CB TYR A 380 9.097 -18.245 -36.931 1.00 31.92 C ANISOU 1564 CB TYR A 380 3648 4421 4059 -581 245 93 C ATOM 1565 CG TYR A 380 8.797 -19.693 -37.262 1.00 31.19 C ANISOU 1565 CG TYR A 380 3598 4321 3933 -655 240 125 C ATOM 1566 CD1 TYR A 380 8.645 -20.638 -36.262 1.00 28.53 C ANISOU 1566 CD1 TYR A 380 3322 3988 3530 -727 245 139 C ATOM 1567 CD2 TYR A 380 8.702 -20.118 -38.585 1.00 32.63 C ANISOU 1567 CD2 TYR A 380 3769 4485 4146 -654 228 142 C ATOM 1568 CE1 TYR A 380 8.377 -21.961 -36.561 1.00 32.03 C ANISOU 1568 CE1 TYR A 380 3819 4418 3933 -799 236 169 C ATOM 1569 CE2 TYR A 380 8.440 -21.443 -38.897 1.00 34.78 C ANISOU 1569 CE2 TYR A 380 4088 4745 4383 -721 219 173 C ATOM 1570 CZ TYR A 380 8.276 -22.360 -37.877 1.00 36.32 C ANISOU 1570 CZ TYR A 380 4350 4944 4507 -795 222 186 C ATOM 1571 OH TYR A 380 8.016 -23.682 -38.164 1.00 38.31 O ANISOU 1571 OH TYR A 380 4664 5179 4714 -868 210 218 O ATOM 1572 N TYR A 381 10.323 -16.170 -35.019 1.00 23.14 N ANISOU 1572 N TYR A 381 2544 3287 2962 -482 240 50 N ATOM 1573 CA TYR A 381 10.967 -14.863 -34.968 1.00 16.46 C ANISOU 1573 CA TYR A 381 1684 2418 2153 -412 229 29 C ATOM 1574 C TYR A 381 12.025 -14.787 -36.055 1.00 19.54 C ANISOU 1574 C TYR A 381 2089 2741 2594 -380 198 41 C ATOM 1575 O TYR A 381 13.038 -15.485 -35.990 1.00 20.01 O ANISOU 1575 O TYR A 381 2198 2750 2655 -391 173 61 O ATOM 1576 CB TYR A 381 11.615 -14.636 -33.603 1.00 13.81 C ANISOU 1576 CB TYR A 381 1386 2066 1796 -405 225 23 C ATOM 1577 CG TYR A 381 12.358 -13.321 -33.494 1.00 20.24 C ANISOU 1577 CG TYR A 381 2195 2852 2642 -340 211 3 C ATOM 1578 CD1 TYR A 381 11.682 -12.106 -33.563 1.00 22.33 C ANISOU 1578 CD1 TYR A 381 2417 3155 2910 -296 223 -25 C ATOM 1579 CD2 TYR A 381 13.733 -13.294 -33.324 1.00 15.78 C ANISOU 1579 CD2 TYR A 381 1674 2225 2096 -323 184 10 C ATOM 1580 CE1 TYR A 381 12.359 -10.902 -33.471 1.00 20.70 C ANISOU 1580 CE1 TYR A 381 2221 2918 2727 -242 207 -42 C ATOM 1581 CE2 TYR A 381 14.416 -12.097 -33.222 1.00 18.67 C ANISOU 1581 CE2 TYR A 381 2040 2569 2486 -275 173 -9 C ATOM 1582 CZ TYR A 381 13.728 -10.907 -33.294 1.00 16.20 C ANISOU 1582 CZ TYR A 381 1693 2285 2176 -238 184 -32 C ATOM 1583 OH TYR A 381 14.427 -9.727 -33.193 1.00 18.71 O ANISOU 1583 OH TYR A 381 2024 2574 2511 -195 169 -49 O ATOM 1584 N SER A 382 11.801 -13.954 -37.065 1.00 15.74 N ANISOU 1584 N SER A 382 1569 2263 2150 -339 199 27 N ATOM 1585 CA SER A 382 12.764 -13.850 -38.153 1.00 14.37 C ANISOU 1585 CA SER A 382 1405 2031 2023 -314 171 38 C ATOM 1586 C SER A 382 13.291 -12.438 -38.289 1.00 10.70 C ANISOU 1586 C SER A 382 936 1546 1585 -261 163 14 C ATOM 1587 O SER A 382 12.574 -11.474 -38.056 1.00 13.70 O ANISOU 1587 O SER A 382 1292 1958 1955 -231 178 -12 O ATOM 1588 CB SER A 382 12.142 -14.296 -39.478 1.00 16.56 C ANISOU 1588 CB SER A 382 1653 2317 2323 -321 174 49 C ATOM 1589 OG SER A 382 11.679 -15.627 -39.376 1.00 26.19 O ANISOU 1589 OG SER A 382 2886 3551 3512 -378 179 73 O ATOM 1590 N VAL A 383 14.553 -12.324 -38.675 1.00 7.99 N ANISOU 1590 N VAL A 383 617 1150 1268 -249 136 22 N ATOM 1591 CA VAL A 383 15.165 -11.021 -38.845 1.00 11.41 C ANISOU 1591 CA VAL A 383 1056 1559 1721 -211 125 1 C ATOM 1592 C VAL A 383 16.041 -11.029 -40.079 1.00 13.35 C ANISOU 1592 C VAL A 383 1303 1764 2004 -205 102 11 C ATOM 1593 O VAL A 383 16.511 -12.082 -40.516 1.00 12.22 O ANISOU 1593 O VAL A 383 1167 1608 1868 -225 87 34 O ATOM 1594 CB VAL A 383 16.031 -10.621 -37.630 1.00 13.64 C ANISOU 1594 CB VAL A 383 1370 1829 1985 -207 117 -8 C ATOM 1595 CG1 VAL A 383 15.177 -10.458 -36.385 1.00 16.71 C ANISOU 1595 CG1 VAL A 383 1755 2258 2337 -208 140 -20 C ATOM 1596 CG2 VAL A 383 17.139 -11.635 -37.395 1.00 16.88 C ANISOU 1596 CG2 VAL A 383 1809 2215 2390 -230 96 10 C ATOM 1597 N GLN A 384 16.259 -9.848 -40.638 1.00 13.16 N ANISOU 1597 N GLN A 384 1281 1721 1999 -177 97 -7 N ATOM 1598 CA GLN A 384 17.167 -9.697 -41.759 1.00 14.84 C ANISOU 1598 CA GLN A 384 1497 1897 2243 -175 75 -2 C ATOM 1599 C GLN A 384 18.582 -9.440 -41.241 1.00 12.72 C ANISOU 1599 C GLN A 384 1257 1611 1967 -186 55 -7 C ATOM 1600 O GLN A 384 18.788 -8.582 -40.382 1.00 13.21 O ANISOU 1600 O GLN A 384 1339 1671 2010 -179 58 -25 O ATOM 1601 CB GLN A 384 16.711 -8.537 -42.635 1.00 13.56 C ANISOU 1601 CB GLN A 384 1334 1721 2097 -146 79 -22 C ATOM 1602 CG GLN A 384 17.513 -8.371 -43.921 1.00 17.56 C ANISOU 1602 CG GLN A 384 1843 2192 2636 -148 60 -16 C ATOM 1603 CD GLN A 384 16.982 -7.224 -44.767 1.00 24.96 C ANISOU 1603 CD GLN A 384 2791 3110 3584 -118 63 -37 C ATOM 1604 OE1 GLN A 384 16.448 -7.433 -45.857 1.00 28.73 O ANISOU 1604 OE1 GLN A 384 3249 3581 4086 -105 66 -33 O ATOM 1605 NE2 GLN A 384 17.098 -6.006 -44.249 1.00 22.71 N ANISOU 1605 NE2 GLN A 384 2543 2810 3275 -104 61 -62 N ATOM 1606 N THR A 385 19.547 -10.188 -41.765 1.00 15.77 N ANISOU 1606 N THR A 385 1642 1988 2363 -200 32 7 N ATOM 1607 CA THR A 385 20.941 -10.084 -41.342 1.00 15.20 C ANISOU 1607 CA THR A 385 1587 1911 2276 -209 11 -2 C ATOM 1608 C THR A 385 21.814 -10.921 -42.268 1.00 19.03 C ANISOU 1608 C THR A 385 2062 2397 2772 -215 -16 10 C ATOM 1609 O THR A 385 21.383 -11.973 -42.749 1.00 15.42 O ANISOU 1609 O THR A 385 1595 1942 2322 -214 -21 32 O ATOM 1610 CB THR A 385 21.137 -10.603 -39.888 1.00 16.72 C ANISOU 1610 CB THR A 385 1800 2118 2434 -213 13 -5 C ATOM 1611 OG1 THR A 385 22.535 -10.669 -39.577 1.00 14.58 O ANISOU 1611 OG1 THR A 385 1541 1850 2147 -218 -11 -17 O ATOM 1612 CG2 THR A 385 20.548 -12.000 -39.734 1.00 13.95 C ANISOU 1612 CG2 THR A 385 1451 1778 2072 -221 14 18 C ATOM 1613 N THR A 386 23.042 -10.467 -42.508 1.00 21.33 N ANISOU 1613 N THR A 386 2355 2691 3060 -222 -36 -5 N ATOM 1614 CA THR A 386 23.992 -11.258 -43.290 1.00 25.40 C ANISOU 1614 CA THR A 386 2856 3219 3576 -223 -67 1 C ATOM 1615 C THR A 386 24.881 -12.116 -42.394 1.00 24.41 C ANISOU 1615 C THR A 386 2746 3118 3411 -217 -89 -7 C ATOM 1616 O THR A 386 25.773 -12.833 -42.873 1.00 16.44 O ANISOU 1616 O THR A 386 1729 2130 2389 -209 -121 -8 O ATOM 1617 CB THR A 386 24.861 -10.377 -44.210 1.00 26.77 C ANISOU 1617 CB THR A 386 3016 3394 3759 -237 -78 -14 C ATOM 1618 OG1 THR A 386 25.386 -9.272 -43.467 1.00 23.62 O ANISOU 1618 OG1 THR A 386 2635 2997 3340 -255 -71 -40 O ATOM 1619 CG2 THR A 386 24.017 -9.843 -45.371 1.00 23.09 C ANISOU 1619 CG2 THR A 386 2541 2900 3332 -235 -65 -4 C ATOM 1620 N GLU A 387 24.612 -12.070 -41.093 1.00 17.40 N ANISOU 1620 N GLU A 387 1881 2229 2500 -216 -74 -14 N ATOM 1621 CA GLU A 387 25.446 -12.786 -40.134 1.00 17.89 C ANISOU 1621 CA GLU A 387 1967 2310 2521 -206 -94 -26 C ATOM 1622 C GLU A 387 24.725 -13.974 -39.506 1.00 17.02 C ANISOU 1622 C GLU A 387 1887 2190 2390 -199 -93 -7 C ATOM 1623 O GLU A 387 25.106 -14.448 -38.435 1.00 14.24 O ANISOU 1623 O GLU A 387 1566 1843 2000 -191 -101 -18 O ATOM 1624 CB GLU A 387 25.949 -11.823 -39.060 1.00 13.10 C ANISOU 1624 CB GLU A 387 1371 1711 1898 -212 -83 -54 C ATOM 1625 CG GLU A 387 26.698 -10.632 -39.648 1.00 18.01 C ANISOU 1625 CG GLU A 387 1973 2341 2529 -230 -85 -74 C ATOM 1626 CD GLU A 387 27.243 -9.699 -38.582 1.00 24.91 C ANISOU 1626 CD GLU A 387 2862 3220 3381 -239 -77 -101 C ATOM 1627 OE1 GLU A 387 26.441 -8.954 -37.979 1.00 22.92 O ANISOU 1627 OE1 GLU A 387 2626 2944 3137 -240 -53 -98 O ATOM 1628 OE2 GLU A 387 28.471 -9.710 -38.354 1.00 25.21 O ANISOU 1628 OE2 GLU A 387 2895 3291 3391 -243 -97 -127 O ATOM 1629 N GLY A 388 23.691 -14.461 -40.184 1.00 12.68 N ANISOU 1629 N GLY A 388 1331 1627 1861 -206 -83 21 N ATOM 1630 CA GLY A 388 22.936 -15.604 -39.694 1.00 14.14 C ANISOU 1630 CA GLY A 388 1548 1803 2021 -213 -81 42 C ATOM 1631 C GLY A 388 23.758 -16.823 -39.318 1.00 18.68 C ANISOU 1631 C GLY A 388 2169 2380 2549 -197 -120 41 C ATOM 1632 O GLY A 388 23.451 -17.504 -38.336 1.00 22.09 O ANISOU 1632 O GLY A 388 2648 2803 2944 -204 -118 44 O ATOM 1633 N GLU A 389 24.807 -17.101 -40.088 1.00 21.95 N ANISOU 1633 N GLU A 389 2574 2807 2959 -174 -157 32 N ATOM 1634 CA GLU A 389 25.694 -18.236 -39.811 1.00 21.66 C ANISOU 1634 CA GLU A 389 2584 2778 2869 -145 -203 23 C ATOM 1635 C GLU A 389 26.457 -18.102 -38.487 1.00 20.70 C ANISOU 1635 C GLU A 389 2492 2668 2705 -130 -208 -10 C ATOM 1636 O GLU A 389 26.564 -19.068 -37.722 1.00 18.19 O ANISOU 1636 O GLU A 389 2236 2338 2336 -116 -228 -12 O ATOM 1637 CB GLU A 389 26.675 -18.445 -40.970 1.00 32.05 C ANISOU 1637 CB GLU A 389 3873 4119 4186 -118 -243 16 C ATOM 1638 CG GLU A 389 27.836 -19.383 -40.653 1.00 42.44 C ANISOU 1638 CG GLU A 389 5229 5457 5437 -74 -296 -9 C ATOM 1639 CD GLU A 389 27.388 -20.811 -40.389 0.50 48.39 C ANISOU 1639 CD GLU A 389 6060 6180 6145 -62 -323 13 C ATOM 1640 OE1 GLU A 389 26.177 -21.098 -40.513 0.50 50.36 O ANISOU 1640 OE1 GLU A 389 6325 6394 6414 -96 -298 50 O ATOM 1641 OE2 GLU A 389 28.252 -21.649 -40.059 0.50 49.19 O ANISOU 1641 OE2 GLU A 389 6211 6294 6184 -18 -371 -8 O ATOM 1642 N GLN A 390 26.985 -16.909 -38.220 1.00 19.84 N ANISOU 1642 N GLN A 390 2345 2578 2613 -134 -191 -36 N ATOM 1643 CA GLN A 390 27.668 -16.647 -36.956 1.00 22.49 C ANISOU 1643 CA GLN A 390 2703 2927 2915 -121 -191 -68 C ATOM 1644 C GLN A 390 26.704 -16.872 -35.806 1.00 19.94 C ANISOU 1644 C GLN A 390 2421 2573 2580 -135 -163 -55 C ATOM 1645 O GLN A 390 27.042 -17.502 -34.799 1.00 22.31 O ANISOU 1645 O GLN A 390 2774 2869 2834 -117 -177 -69 O ATOM 1646 CB GLN A 390 28.165 -15.201 -36.886 1.00 20.39 C ANISOU 1646 CB GLN A 390 2391 2682 2675 -135 -171 -93 C ATOM 1647 CG GLN A 390 29.350 -14.868 -37.769 1.00 28.84 C ANISOU 1647 CG GLN A 390 3421 3794 3742 -129 -197 -117 C ATOM 1648 CD GLN A 390 29.573 -13.360 -37.878 1.00 34.74 C ANISOU 1648 CD GLN A 390 4132 4551 4518 -161 -172 -132 C ATOM 1649 OE1 GLN A 390 30.071 -12.716 -36.946 1.00 32.26 O ANISOU 1649 OE1 GLN A 390 3823 4249 4186 -165 -163 -158 O ATOM 1650 NE2 GLN A 390 29.202 -12.792 -39.025 1.00 31.05 N ANISOU 1650 NE2 GLN A 390 3633 4074 4090 -184 -162 -115 N ATOM 1651 N ILE A 391 25.501 -16.328 -35.960 1.00 14.09 N ANISOU 1651 N ILE A 391 1658 1816 1878 -166 -125 -30 N ATOM 1652 CA ILE A 391 24.482 -16.399 -34.924 1.00 10.48 C ANISOU 1652 CA ILE A 391 1227 1343 1411 -186 -94 -19 C ATOM 1653 C ILE A 391 24.146 -17.856 -34.603 1.00 12.67 C ANISOU 1653 C ILE A 391 1569 1603 1643 -191 -111 -2 C ATOM 1654 O ILE A 391 24.124 -18.245 -33.437 1.00 16.13 O ANISOU 1654 O ILE A 391 2056 2031 2042 -191 -108 -9 O ATOM 1655 CB ILE A 391 23.233 -15.594 -35.328 1.00 12.66 C ANISOU 1655 CB ILE A 391 1462 1619 1731 -212 -54 -1 C ATOM 1656 CG1 ILE A 391 23.607 -14.111 -35.467 1.00 13.45 C ANISOU 1656 CG1 ILE A 391 1521 1728 1864 -205 -42 -21 C ATOM 1657 CG2 ILE A 391 22.092 -15.798 -34.327 1.00 11.03 C ANISOU 1657 CG2 ILE A 391 1276 1409 1505 -235 -24 10 C ATOM 1658 CD1 ILE A 391 22.518 -13.247 -36.094 1.00 11.21 C ANISOU 1658 CD1 ILE A 391 1200 1443 1618 -218 -13 -10 C ATOM 1659 N SER A 392 23.928 -18.660 -35.642 1.00 16.61 N ANISOU 1659 N SER A 392 2074 2094 2143 -195 -131 21 N ATOM 1660 CA SER A 392 23.650 -20.090 -35.471 1.00 26.50 C ANISOU 1660 CA SER A 392 3399 3324 3344 -203 -154 40 C ATOM 1661 C SER A 392 24.748 -20.814 -34.704 1.00 22.28 C ANISOU 1661 C SER A 392 2934 2783 2749 -165 -195 14 C ATOM 1662 O SER A 392 24.462 -21.658 -33.853 1.00 25.07 O ANISOU 1662 O SER A 392 3364 3112 3050 -175 -200 18 O ATOM 1663 CB SER A 392 23.479 -20.781 -36.824 1.00 24.23 C ANISOU 1663 CB SER A 392 3108 3031 3069 -204 -178 65 C ATOM 1664 OG SER A 392 22.557 -20.087 -37.633 1.00 34.86 O ANISOU 1664 OG SER A 392 4388 4385 4472 -231 -144 84 O ATOM 1665 N GLN A 393 26.003 -20.501 -35.021 1.00 21.68 N ANISOU 1665 N GLN A 393 2833 2732 2672 -120 -225 -17 N ATOM 1666 CA GLN A 393 27.136 -21.165 -34.373 1.00 18.89 C ANISOU 1666 CA GLN A 393 2539 2383 2254 -71 -268 -50 C ATOM 1667 C GLN A 393 27.267 -20.810 -32.898 1.00 24.94 C ANISOU 1667 C GLN A 393 3333 3145 2999 -68 -248 -75 C ATOM 1668 O GLN A 393 27.576 -21.668 -32.073 1.00 25.95 O ANISOU 1668 O GLN A 393 3542 3253 3064 -45 -273 -89 O ATOM 1669 CB GLN A 393 28.438 -20.878 -35.123 1.00 34.19 C ANISOU 1669 CB GLN A 393 4432 4367 4193 -27 -304 -82 C ATOM 1670 CG GLN A 393 28.660 -21.802 -36.316 1.00 51.25 C ANISOU 1670 CG GLN A 393 6605 6531 6336 -4 -350 -68 C ATOM 1671 CD GLN A 393 29.818 -21.364 -37.193 1.00 66.38 C ANISOU 1671 CD GLN A 393 8456 8503 8260 30 -378 -97 C ATOM 1672 OE1 GLN A 393 30.420 -20.316 -36.967 1.00 70.79 O ANISOU 1672 OE1 GLN A 393 8959 9097 8840 27 -360 -127 O ATOM 1673 NE2 GLN A 393 30.133 -22.167 -38.203 1.00 70.00 N ANISOU 1673 NE2 GLN A 393 8925 8973 8700 60 -424 -90 N ATOM 1674 N LEU A 394 27.033 -19.547 -32.560 1.00 24.75 N ANISOU 1674 N LEU A 394 3247 3134 3023 -89 -205 -80 N ATOM 1675 CA LEU A 394 27.060 -19.137 -31.165 1.00 20.83 C ANISOU 1675 CA LEU A 394 2772 2631 2512 -87 -183 -99 C ATOM 1676 C LEU A 394 25.988 -19.889 -30.380 1.00 28.19 C ANISOU 1676 C LEU A 394 3769 3528 3415 -119 -166 -74 C ATOM 1677 O LEU A 394 26.225 -20.350 -29.258 1.00 24.62 O ANISOU 1677 O LEU A 394 3382 3058 2915 -104 -173 -91 O ATOM 1678 CB LEU A 394 26.842 -17.632 -31.039 1.00 19.07 C ANISOU 1678 CB LEU A 394 2476 2424 2344 -105 -143 -104 C ATOM 1679 CG LEU A 394 28.039 -16.785 -30.628 1.00 25.81 C ANISOU 1679 CG LEU A 394 3302 3306 3197 -77 -150 -145 C ATOM 1680 CD1 LEU A 394 29.346 -17.317 -31.209 1.00 19.73 C ANISOU 1680 CD1 LEU A 394 2534 2568 2393 -37 -198 -176 C ATOM 1681 CD2 LEU A 394 27.810 -15.316 -30.985 1.00 24.99 C ANISOU 1681 CD2 LEU A 394 3131 3216 3150 -102 -119 -143 C ATOM 1682 N ILE A 395 24.807 -20.010 -30.978 1.00 24.25 N ANISOU 1682 N ILE A 395 3253 3020 2940 -165 -142 -36 N ATOM 1683 CA ILE A 395 23.690 -20.680 -30.322 1.00 24.53 C ANISOU 1683 CA ILE A 395 3341 3033 2945 -210 -121 -12 C ATOM 1684 C ILE A 395 24.007 -22.157 -30.075 1.00 27.94 C ANISOU 1684 C ILE A 395 3882 3432 3303 -201 -163 -11 C ATOM 1685 O ILE A 395 23.845 -22.656 -28.962 1.00 33.58 O ANISOU 1685 O ILE A 395 4669 4124 3968 -211 -160 -16 O ATOM 1686 CB ILE A 395 22.390 -20.527 -31.139 1.00 30.41 C ANISOU 1686 CB ILE A 395 4039 3789 3728 -261 -89 23 C ATOM 1687 CG1 ILE A 395 21.823 -19.113 -30.964 1.00 26.51 C ANISOU 1687 CG1 ILE A 395 3462 3322 3287 -270 -44 18 C ATOM 1688 CG2 ILE A 395 21.362 -21.567 -30.723 1.00 28.16 C ANISOU 1688 CG2 ILE A 395 3819 3486 3394 -315 -79 49 C ATOM 1689 CD1 ILE A 395 20.754 -18.764 -31.973 1.00 25.75 C ANISOU 1689 CD1 ILE A 395 3306 3244 3232 -301 -19 42 C ATOM 1690 N ALA A 396 24.476 -22.843 -31.111 1.00 26.55 N ANISOU 1690 N ALA A 396 3723 3252 3114 -179 -206 -5 N ATOM 1691 CA ALA A 396 24.932 -24.226 -30.982 1.00 31.15 C ANISOU 1691 CA ALA A 396 4418 3801 3617 -156 -258 -8 C ATOM 1692 C ALA A 396 26.055 -24.371 -29.952 1.00 34.22 C ANISOU 1692 C ALA A 396 4862 4185 3954 -96 -287 -54 C ATOM 1693 O ALA A 396 26.031 -25.263 -29.102 1.00 36.37 O ANISOU 1693 O ALA A 396 5243 4421 4157 -95 -305 -59 O ATOM 1694 CB ALA A 396 25.392 -24.749 -32.331 1.00 32.03 C ANISOU 1694 CB ALA A 396 4523 3918 3729 -127 -303 0 C ATOM 1695 N GLY A 397 27.041 -23.490 -30.036 1.00 27.78 N ANISOU 1695 N GLY A 397 3977 3409 3170 -49 -291 -89 N ATOM 1696 CA GLY A 397 28.173 -23.546 -29.135 1.00 30.44 C ANISOU 1696 CA GLY A 397 4353 3754 3461 12 -318 -138 C ATOM 1697 C GLY A 397 27.755 -23.435 -27.686 1.00 38.42 C ANISOU 1697 C GLY A 397 5410 4737 4452 -7 -287 -144 C ATOM 1698 O GLY A 397 28.259 -24.163 -26.824 1.00 32.96 O ANISOU 1698 O GLY A 397 4812 4021 3691 31 -316 -171 O ATOM 1699 N TYR A 398 26.832 -22.518 -27.413 1.00 37.72 N ANISOU 1699 N TYR A 398 5257 4654 4422 -60 -229 -121 N ATOM 1700 CA TYR A 398 26.390 -22.279 -26.047 1.00 36.43 C ANISOU 1700 CA TYR A 398 5122 4472 4246 -78 -196 -125 C ATOM 1701 C TYR A 398 25.510 -23.418 -25.533 1.00 38.51 C ANISOU 1701 C TYR A 398 5490 4692 4450 -123 -196 -100 C ATOM 1702 O TYR A 398 25.610 -23.804 -24.365 1.00 35.22 O ANISOU 1702 O TYR A 398 5150 4247 3984 -114 -198 -116 O ATOM 1703 CB TYR A 398 25.669 -20.936 -25.933 1.00 33.59 C ANISOU 1703 CB TYR A 398 4665 4139 3959 -114 -141 -111 C ATOM 1704 CG TYR A 398 26.609 -19.762 -25.748 1.00 37.98 C ANISOU 1704 CG TYR A 398 5153 4726 4553 -72 -137 -146 C ATOM 1705 CD1 TYR A 398 26.567 -18.665 -26.601 1.00 34.51 C ANISOU 1705 CD1 TYR A 398 4618 4317 4177 -82 -119 -139 C ATOM 1706 CD2 TYR A 398 27.543 -19.756 -24.720 1.00 36.53 C ANISOU 1706 CD2 TYR A 398 5006 4538 4334 -24 -152 -186 C ATOM 1707 CE1 TYR A 398 27.431 -17.594 -26.429 1.00 32.48 C ANISOU 1707 CE1 TYR A 398 4309 4086 3946 -55 -117 -170 C ATOM 1708 CE2 TYR A 398 28.406 -18.691 -24.541 1.00 35.71 C ANISOU 1708 CE2 TYR A 398 4842 4467 4260 7 -148 -219 C ATOM 1709 CZ TYR A 398 28.348 -17.613 -25.401 1.00 35.66 C ANISOU 1709 CZ TYR A 398 4746 4490 4314 -12 -131 -209 C ATOM 1710 OH TYR A 398 29.208 -16.550 -25.218 1.00 29.95 O ANISOU 1710 OH TYR A 398 3971 3796 3612 8 -128 -241 O ATOM 1711 N ILE A 399 24.664 -23.961 -26.405 1.00 30.65 N ANISOU 1711 N ILE A 399 4500 3689 3456 -173 -194 -61 N ATOM 1712 CA ILE A 399 23.825 -25.084 -26.027 1.00 31.52 C ANISOU 1712 CA ILE A 399 4713 3759 3502 -228 -196 -35 C ATOM 1713 C ILE A 399 24.707 -26.252 -25.644 1.00 35.19 C ANISOU 1713 C ILE A 399 5312 4181 3879 -179 -256 -59 C ATOM 1714 O ILE A 399 24.410 -26.991 -24.706 1.00 38.88 O ANISOU 1714 O ILE A 399 5887 4608 4279 -203 -259 -59 O ATOM 1715 CB ILE A 399 22.884 -25.516 -27.166 1.00 31.50 C ANISOU 1715 CB ILE A 399 4694 3761 3514 -287 -190 8 C ATOM 1716 CG1 ILE A 399 21.637 -24.635 -27.186 1.00 30.13 C ANISOU 1716 CG1 ILE A 399 4425 3626 3399 -351 -126 32 C ATOM 1717 CG2 ILE A 399 22.481 -26.994 -27.008 1.00 22.88 C ANISOU 1717 CG2 ILE A 399 3741 2619 2332 -328 -219 28 C ATOM 1718 CD1 ILE A 399 20.785 -24.823 -28.421 1.00 29.56 C ANISOU 1718 CD1 ILE A 399 4309 3569 3354 -398 -117 67 C ATOM 1719 N ASP A 400 25.808 -26.405 -26.369 1.00 33.53 N ANISOU 1719 N ASP A 400 5095 3981 3662 -107 -305 -84 N ATOM 1720 CA ASP A 400 26.695 -27.535 -26.159 1.00 43.18 C ANISOU 1720 CA ASP A 400 6444 5169 4792 -46 -372 -112 C ATOM 1721 C ASP A 400 27.369 -27.443 -24.799 1.00 41.89 C ANISOU 1721 C ASP A 400 6334 4993 4589 2 -376 -158 C ATOM 1722 O ASP A 400 27.439 -28.426 -24.068 1.00 43.68 O ANISOU 1722 O ASP A 400 6699 5170 4729 12 -406 -169 O ATOM 1723 CB ASP A 400 27.742 -27.618 -27.269 1.00 58.55 C ANISOU 1723 CB ASP A 400 8355 7149 6742 26 -424 -134 C ATOM 1724 CG ASP A 400 28.152 -29.045 -27.568 1.00 73.98 C ANISOU 1724 CG ASP A 400 10446 9064 8598 68 -497 -140 C ATOM 1725 OD1 ASP A 400 27.272 -29.843 -27.963 1.00 75.92 O ANISOU 1725 OD1 ASP A 400 10759 9270 8818 9 -502 -96 O ATOM 1726 OD2 ASP A 400 29.348 -29.369 -27.407 1.00 81.03 O ANISOU 1726 OD2 ASP A 400 11383 9970 9436 159 -552 -191 O ATOM 1727 N ILE A 401 27.861 -26.256 -24.462 1.00 36.98 N ANISOU 1727 N ILE A 401 5609 4415 4027 30 -347 -184 N ATOM 1728 CA ILE A 401 28.431 -26.028 -23.144 1.00 38.72 C ANISOU 1728 CA ILE A 401 5865 4626 4220 73 -343 -226 C ATOM 1729 C ILE A 401 27.439 -26.420 -22.045 1.00 46.35 C ANISOU 1729 C ILE A 401 6914 5544 5154 12 -311 -203 C ATOM 1730 O ILE A 401 27.822 -27.000 -21.028 1.00 52.42 O ANISOU 1730 O ILE A 401 7790 6274 5854 45 -332 -232 O ATOM 1731 CB ILE A 401 28.904 -24.572 -22.977 1.00 37.61 C ANISOU 1731 CB ILE A 401 5592 4539 4157 93 -308 -248 C ATOM 1732 CG1 ILE A 401 30.259 -24.383 -23.664 1.00 36.75 C ANISOU 1732 CG1 ILE A 401 5438 4480 4046 169 -352 -293 C ATOM 1733 CG2 ILE A 401 29.007 -24.198 -21.510 1.00 39.57 C ANISOU 1733 CG2 ILE A 401 5867 4772 4395 107 -284 -273 C ATOM 1734 CD1 ILE A 401 30.725 -22.942 -23.727 1.00 34.25 C ANISOU 1734 CD1 ILE A 401 4992 4218 3802 175 -319 -311 C ATOM 1735 N ILE A 402 26.161 -26.125 -22.262 1.00 45.92 N ANISOU 1735 N ILE A 402 6811 5494 5144 -77 -262 -154 N ATOM 1736 CA ILE A 402 25.123 -26.489 -21.298 1.00 44.57 C ANISOU 1736 CA ILE A 402 6706 5289 4938 -148 -228 -131 C ATOM 1737 C ILE A 402 24.851 -27.994 -21.297 1.00 48.67 C ANISOU 1737 C ILE A 402 7384 5750 5359 -178 -267 -117 C ATOM 1738 O ILE A 402 24.626 -28.594 -20.246 1.00 50.88 O ANISOU 1738 O ILE A 402 7775 5986 5572 -199 -267 -123 O ATOM 1739 CB ILE A 402 23.800 -25.744 -21.566 1.00 39.26 C ANISOU 1739 CB ILE A 402 5931 4654 4332 -234 -166 -89 C ATOM 1740 CG1 ILE A 402 23.964 -24.243 -21.313 1.00 38.02 C ANISOU 1740 CG1 ILE A 402 5642 4544 4258 -207 -127 -104 C ATOM 1741 CG2 ILE A 402 22.675 -26.315 -20.701 1.00 35.38 C ANISOU 1741 CG2 ILE A 402 5514 4140 3790 -318 -136 -65 C ATOM 1742 CD1 ILE A 402 22.743 -23.427 -21.694 1.00 30.86 C ANISOU 1742 CD1 ILE A 402 4629 3680 3414 -273 -74 -69 C ATOM 1743 N LEU A 403 24.867 -28.607 -22.475 1.00 51.38 N ANISOU 1743 N LEU A 403 7743 6089 5689 -181 -302 -98 N ATOM 1744 CA LEU A 403 24.581 -30.033 -22.561 1.00 57.45 C ANISOU 1744 CA LEU A 403 8669 6800 6360 -213 -344 -81 C ATOM 1745 C LEU A 403 25.694 -30.850 -21.921 1.00 65.96 C ANISOU 1745 C LEU A 403 9890 7829 7344 -126 -408 -128 C ATOM 1746 O LEU A 403 25.489 -32.004 -21.548 1.00 70.19 O ANISOU 1746 O LEU A 403 10587 8301 7780 -149 -441 -123 O ATOM 1747 CB LEU A 403 24.356 -30.477 -24.005 1.00 54.10 C ANISOU 1747 CB LEU A 403 8228 6382 5946 -231 -370 -49 C ATOM 1748 CG LEU A 403 23.771 -31.886 -24.098 1.00 59.57 C ANISOU 1748 CG LEU A 403 9080 7013 6539 -290 -403 -21 C ATOM 1749 CD1 LEU A 403 22.584 -32.021 -23.153 1.00 58.90 C ANISOU 1749 CD1 LEU A 403 9039 6913 6428 -400 -350 5 C ATOM 1750 CD2 LEU A 403 23.374 -32.240 -25.525 1.00 60.70 C ANISOU 1750 CD2 LEU A 403 9194 7167 6703 -319 -419 17 C ATOM 1751 N LYS A 404 26.869 -30.241 -21.788 1.00 67.44 N ANISOU 1751 N LYS A 404 10019 8048 7556 -26 -426 -178 N ATOM 1752 CA LYS A 404 28.015 -30.922 -21.197 1.00 70.36 C ANISOU 1752 CA LYS A 404 10511 8386 7837 73 -489 -234 C ATOM 1753 C LYS A 404 28.163 -30.627 -19.706 1.00 74.65 C ANISOU 1753 C LYS A 404 11092 8909 8364 88 -464 -265 C ATOM 1754 O LYS A 404 28.975 -31.247 -19.021 1.00 69.95 O ANISOU 1754 O LYS A 404 10615 8278 7684 164 -511 -313 O ATOM 1755 CB LYS A 404 29.297 -30.593 -21.967 1.00 69.42 C ANISOU 1755 CB LYS A 404 10318 8322 7737 178 -533 -277 C ATOM 1756 CG LYS A 404 29.395 -31.341 -23.291 1.00 72.46 C ANISOU 1756 CG LYS A 404 10729 8708 8093 191 -586 -259 C ATOM 1757 CD LYS A 404 30.536 -30.845 -24.161 1.00 74.43 C ANISOU 1757 CD LYS A 404 10875 9031 8376 278 -619 -296 C ATOM 1758 CE LYS A 404 30.650 -31.687 -25.428 1.00 76.38 C ANISOU 1758 CE LYS A 404 11160 9275 8585 299 -677 -279 C ATOM 1759 NZ LYS A 404 31.728 -31.205 -26.338 1.00 76.58 N ANISOU 1759 NZ LYS A 404 11076 9381 8641 378 -708 -315 N ATOM 1760 N LYS A 405 27.371 -29.682 -19.211 1.00 84.62 N ANISOU 1760 N LYS A 405 12256 10195 9702 21 -392 -240 N ATOM 1761 CA LYS A 405 27.282 -29.444 -17.776 1.00 97.49 C ANISOU 1761 CA LYS A 405 13924 11801 11316 19 -362 -259 C ATOM 1762 C LYS A 405 26.441 -30.546 -17.140 1.00105.58 C ANISOU 1762 C LYS A 405 15109 12755 12250 -55 -364 -234 C ATOM 1763 O LYS A 405 26.807 -31.099 -16.103 1.00107.60 O ANISOU 1763 O LYS A 405 15493 12959 12430 -21 -386 -266 O ATOM 1764 CB LYS A 405 26.659 -28.077 -17.484 1.00102.83 C ANISOU 1764 CB LYS A 405 14444 12529 12097 -27 -288 -239 C ATOM 1765 CG LYS A 405 27.577 -26.892 -17.741 1.00107.88 C ANISOU 1765 CG LYS A 405 14947 13229 12815 46 -283 -271 C ATOM 1766 CD LYS A 405 26.807 -25.580 -17.656 1.00112.23 C ANISOU 1766 CD LYS A 405 15353 13825 13464 -8 -215 -243 C ATOM 1767 CE LYS A 405 27.679 -24.389 -18.032 1.00114.26 C ANISOU 1767 CE LYS A 405 15481 14138 13794 51 -211 -271 C ATOM 1768 NZ LYS A 405 26.865 -23.174 -18.332 1.00115.10 N ANISOU 1768 NZ LYS A 405 15455 14287 13991 -2 -156 -238 N ATOM 1769 N LYS A 406 25.313 -30.859 -17.773 1.00111.16 N ANISOU 1769 N LYS A 406 15811 13462 12962 -159 -342 -179 N ATOM 1770 CA LYS A 406 24.438 -31.931 -17.311 1.00116.67 C ANISOU 1770 CA LYS A 406 16661 14101 13569 -249 -343 -151 C ATOM 1771 C LYS A 406 25.228 -33.212 -17.068 1.00122.58 C ANISOU 1771 C LYS A 406 17611 14771 14193 -187 -421 -184 C ATOM 1772 O LYS A 406 25.018 -33.905 -16.072 1.00125.70 O ANISOU 1772 O LYS A 406 18155 15104 14501 -215 -428 -191 O ATOM 1773 CB LYS A 406 23.327 -32.199 -18.332 1.00116.55 C ANISOU 1773 CB LYS A 406 16611 14103 13568 -355 -323 -94 C ATOM 1774 CG LYS A 406 22.211 -31.163 -18.355 1.00115.53 C ANISOU 1774 CG LYS A 406 16322 14043 13531 -440 -243 -60 C ATOM 1775 CD LYS A 406 21.137 -31.543 -19.367 1.00114.31 C ANISOU 1775 CD LYS A 406 16145 13908 13378 -540 -228 -10 C ATOM 1776 CE LYS A 406 19.922 -30.632 -19.268 1.00112.35 C ANISOU 1776 CE LYS A 406 15756 13731 13199 -627 -151 17 C ATOM 1777 NZ LYS A 406 18.870 -31.005 -20.258 1.00110.79 N ANISOU 1777 NZ LYS A 406 15533 13560 13001 -722 -136 61 N ATOM 1778 N GLN A 407 26.141 -33.515 -17.986 1.00124.23 N ANISOU 1778 N GLN A 407 17827 14985 14388 -99 -482 -205 N ATOM 1779 CA GLN A 407 26.942 -34.732 -17.914 1.00126.38 C ANISOU 1779 CA GLN A 407 18290 15191 14536 -24 -567 -240 C ATOM 1780 C GLN A 407 27.837 -34.766 -16.675 1.00128.37 C ANISOU 1780 C GLN A 407 18625 15414 14736 69 -589 -304 C ATOM 1781 O GLN A 407 27.959 -35.800 -16.015 1.00131.06 O ANISOU 1781 O GLN A 407 19163 15676 14958 82 -633 -322 O ATOM 1782 CB GLN A 407 27.780 -34.887 -19.186 1.00126.01 C ANISOU 1782 CB GLN A 407 18204 15177 14496 62 -627 -256 C ATOM 1783 CG GLN A 407 26.950 -34.939 -20.461 1.00126.19 C ANISOU 1783 CG GLN A 407 18157 15223 14565 -20 -612 -195 C ATOM 1784 CD GLN A 407 27.795 -34.854 -21.718 1.00126.25 C ANISOU 1784 CD GLN A 407 18091 15278 14601 67 -661 -210 C ATOM 1785 OE1 GLN A 407 29.008 -34.654 -21.653 1.00126.48 O ANISOU 1785 OE1 GLN A 407 18101 15336 14619 185 -701 -268 O ATOM 1786 NE2 GLN A 407 27.154 -35.002 -22.872 1.00125.38 N ANISOU 1786 NE2 GLN A 407 17934 15180 14524 7 -657 -161 N ATOM 1787 N SER A 408 28.459 -33.634 -16.362 1.00124.80 N ANISOU 1787 N SER A 408 18028 15022 14369 133 -559 -337 N ATOM 1788 CA SER A 408 29.319 -33.535 -15.187 1.00120.81 C ANISOU 1788 CA SER A 408 17579 14498 13825 223 -573 -400 C ATOM 1789 C SER A 408 28.817 -32.466 -14.220 1.00117.72 C ANISOU 1789 C SER A 408 17082 14131 13517 176 -494 -390 C ATOM 1790 O SER A 408 27.737 -32.595 -13.641 1.00115.51 O ANISOU 1790 O SER A 408 16840 13819 13228 72 -449 -350 O ATOM 1791 CB SER A 408 30.764 -33.242 -15.597 1.00118.56 C ANISOU 1791 CB SER A 408 17236 14267 13545 364 -623 -465 C ATOM 1792 OG SER A 408 30.874 -31.974 -16.219 1.00116.55 O ANISOU 1792 OG SER A 408 16768 14101 13416 360 -578 -455 O TER 1793 SER A 408 ATOM 1794 N ASN B 205 18.068 -0.642 -9.239 1.00 98.84 N ANISOU 1794 N ASN B 205 12710 12632 12214 697 -1401 188 N ATOM 1795 CA ASN B 205 16.864 -0.947 -8.471 1.00 99.30 C ANISOU 1795 CA ASN B 205 12660 12745 12324 617 -1441 170 C ATOM 1796 C ASN B 205 16.245 0.297 -7.840 1.00 96.31 C ANISOU 1796 C ASN B 205 12174 12410 12010 645 -1388 189 C ATOM 1797 O ASN B 205 15.220 0.221 -7.160 1.00 93.66 O ANISOU 1797 O ASN B 205 11736 12127 11724 587 -1410 177 O ATOM 1798 CB ASN B 205 17.151 -2.009 -7.406 1.00 99.61 C ANISOU 1798 CB ASN B 205 12703 12761 12383 511 -1427 145 C ATOM 1799 CG ASN B 205 17.568 -3.339 -8.008 1.00 98.83 C ANISOU 1799 CG ASN B 205 12711 12622 12217 480 -1489 124 C ATOM 1800 OD1 ASN B 205 18.621 -3.446 -8.637 1.00 97.96 O ANISOU 1800 OD1 ASN B 205 12703 12463 12054 536 -1471 132 O ATOM 1801 ND2 ASN B 205 16.743 -4.363 -7.814 1.00 98.25 N ANISOU 1801 ND2 ASN B 205 12621 12569 12142 388 -1560 95 N ATOM 1802 N VAL B 206 16.881 1.442 -8.065 1.00 95.77 N ANISOU 1802 N VAL B 206 12132 12319 11938 732 -1317 218 N ATOM 1803 CA VAL B 206 16.305 2.722 -7.678 1.00 98.20 C ANISOU 1803 CA VAL B 206 12359 12661 12291 778 -1269 240 C ATOM 1804 C VAL B 206 15.520 3.267 -8.869 1.00100.69 C ANISOU 1804 C VAL B 206 12675 13013 12572 867 -1334 252 C ATOM 1805 O VAL B 206 16.025 4.068 -9.657 1.00 98.41 O ANISOU 1805 O VAL B 206 12454 12695 12243 960 -1304 276 O ATOM 1806 CB VAL B 206 17.386 3.721 -7.213 1.00 98.18 C ANISOU 1806 CB VAL B 206 12391 12613 12302 818 -1151 264 C ATOM 1807 CG1 VAL B 206 18.560 3.743 -8.187 1.00100.50 C ANISOU 1807 CG1 VAL B 206 12806 12850 12530 877 -1132 274 C ATOM 1808 CG2 VAL B 206 16.790 5.108 -7.025 1.00 98.18 C ANISOU 1808 CG2 VAL B 206 12331 12640 12333 883 -1105 289 C ATOM 1809 N ASP B 207 14.281 2.805 -8.998 1.00105.48 N ANISOU 1809 N ASP B 207 13204 13685 13188 835 -1423 233 N ATOM 1810 CA ASP B 207 13.476 3.073 -10.183 1.00108.79 C ANISOU 1810 CA ASP B 207 13622 14147 13566 911 -1507 237 C ATOM 1811 C ASP B 207 12.658 4.352 -10.052 1.00107.33 C ANISOU 1811 C ASP B 207 13354 14014 13412 989 -1483 259 C ATOM 1812 O ASP B 207 11.999 4.577 -9.037 1.00109.78 O ANISOU 1812 O ASP B 207 13557 14370 13785 947 -1458 255 O ATOM 1813 CB ASP B 207 12.550 1.887 -10.465 1.00112.07 C ANISOU 1813 CB ASP B 207 13997 14614 13970 835 -1622 203 C ATOM 1814 CG ASP B 207 11.887 1.977 -11.822 1.00116.76 C ANISOU 1814 CG ASP B 207 14610 15245 14507 909 -1720 202 C ATOM 1815 OD1 ASP B 207 12.482 2.590 -12.732 1.00118.71 O ANISOU 1815 OD1 ASP B 207 14950 15451 14704 1011 -1704 226 O ATOM 1816 OD2 ASP B 207 10.774 1.431 -11.981 1.00118.21 O ANISOU 1816 OD2 ASP B 207 14719 15502 14695 864 -1812 177 O ATOM 1817 N SER B 208 12.704 5.185 -11.087 1.00102.59 N ANISOU 1817 N SER B 208 12812 13404 12763 1107 -1491 282 N ATOM 1818 CA SER B 208 11.917 6.411 -11.120 1.00 99.93 C ANISOU 1818 CA SER B 208 12414 13114 12440 1199 -1476 304 C ATOM 1819 C SER B 208 10.564 6.162 -11.777 1.00 99.73 C ANISOU 1819 C SER B 208 12312 13179 12400 1224 -1595 288 C ATOM 1820 O SER B 208 9.758 7.080 -11.930 1.00 97.96 O ANISOU 1820 O SER B 208 12031 13009 12180 1311 -1603 302 O ATOM 1821 CB SER B 208 12.663 7.513 -11.873 1.00 99.57 C ANISOU 1821 CB SER B 208 12480 13008 12345 1319 -1415 338 C ATOM 1822 OG SER B 208 12.673 7.260 -13.267 1.00100.84 O ANISOU 1822 OG SER B 208 12724 13159 12431 1382 -1493 338 O ATOM 1823 N ARG B 209 10.322 4.914 -12.168 1.00101.31 N ANISOU 1823 N ARG B 209 12514 13399 12579 1148 -1688 256 N ATOM 1824 CA ARG B 209 9.056 4.546 -12.790 1.00103.46 C ANISOU 1824 CA ARG B 209 12710 13764 12835 1153 -1808 234 C ATOM 1825 C ARG B 209 8.088 3.927 -11.786 1.00100.06 C ANISOU 1825 C ARG B 209 12135 13413 12470 1039 -1836 204 C ATOM 1826 O ARG B 209 7.077 3.338 -12.167 1.00102.94 O ANISOU 1826 O ARG B 209 12428 13858 12825 1004 -1939 176 O ATOM 1827 CB ARG B 209 9.278 3.615 -13.983 1.00109.12 C ANISOU 1827 CB ARG B 209 13524 14458 13479 1145 -1902 217 C ATOM 1828 CG ARG B 209 9.777 4.333 -15.228 1.00114.59 C ANISOU 1828 CG ARG B 209 14336 15105 14100 1280 -1904 245 C ATOM 1829 CD ARG B 209 9.737 3.428 -16.448 1.00119.57 C ANISOU 1829 CD ARG B 209 15045 15729 14656 1277 -2013 226 C ATOM 1830 NE ARG B 209 10.497 2.200 -16.238 1.00122.01 N ANISOU 1830 NE ARG B 209 15420 15980 14957 1167 -2012 205 N ATOM 1831 CZ ARG B 209 11.812 2.101 -16.397 1.00122.04 C ANISOU 1831 CZ ARG B 209 15549 15888 14932 1179 -1945 220 C ATOM 1832 NH1 ARG B 209 12.519 3.160 -16.766 1.00121.80 N ANISOU 1832 NH1 ARG B 209 15592 15808 14880 1285 -1870 254 N ATOM 1833 NH2 ARG B 209 12.421 0.942 -16.184 1.00121.46 N ANISOU 1833 NH2 ARG B 209 15530 15770 14848 1084 -1950 199 N ATOM 1834 N ASP B 210 8.416 4.058 -10.504 1.00 91.32 N ANISOU 1834 N ASP B 210 10988 12284 11426 977 -1743 208 N ATOM 1835 CA ASP B 210 7.474 3.761 -9.430 1.00 83.19 C ANISOU 1835 CA ASP B 210 9815 11329 10464 886 -1746 186 C ATOM 1836 C ASP B 210 7.609 4.813 -8.338 1.00 72.24 C ANISOU 1836 C ASP B 210 8380 9933 9137 916 -1632 212 C ATOM 1837 O ASP B 210 8.245 4.571 -7.313 1.00 68.83 O ANISOU 1837 O ASP B 210 7959 9451 8744 839 -1556 211 O ATOM 1838 CB ASP B 210 7.705 2.366 -8.847 1.00 84.97 C ANISOU 1838 CB ASP B 210 10049 11531 10704 733 -1763 153 C ATOM 1839 CG ASP B 210 6.694 2.014 -7.765 1.00 86.03 C ANISOU 1839 CG ASP B 210 10040 11743 10905 630 -1766 127 C ATOM 1840 OD1 ASP B 210 5.720 2.781 -7.589 1.00 86.73 O ANISOU 1840 OD1 ASP B 210 10012 11917 11026 680 -1770 133 O ATOM 1841 OD2 ASP B 210 6.870 0.975 -7.093 1.00 84.28 O ANISOU 1841 OD2 ASP B 210 9824 11497 10700 502 -1762 102 O ATOM 1842 N PRO B 211 7.010 5.991 -8.562 1.00 66.91 N ANISOU 1842 N PRO B 211 7656 9304 8462 1032 -1621 235 N ATOM 1843 CA PRO B 211 7.111 7.146 -7.663 1.00 62.32 C ANISOU 1843 CA PRO B 211 7043 8709 7926 1082 -1513 264 C ATOM 1844 C PRO B 211 6.832 6.821 -6.198 1.00 54.77 C ANISOU 1844 C PRO B 211 5988 7775 7046 970 -1460 249 C ATOM 1845 O PRO B 211 7.389 7.483 -5.322 1.00 54.27 O ANISOU 1845 O PRO B 211 5941 7662 7017 976 -1355 270 O ATOM 1846 CB PRO B 211 6.046 8.099 -8.210 1.00 62.61 C ANISOU 1846 CB PRO B 211 7011 8829 7949 1208 -1553 277 C ATOM 1847 CG PRO B 211 6.000 7.789 -9.660 1.00 64.57 C ANISOU 1847 CG PRO B 211 7327 9084 8123 1266 -1652 271 C ATOM 1848 CD PRO B 211 6.217 6.301 -9.764 1.00 65.75 C ANISOU 1848 CD PRO B 211 7494 9222 8266 1133 -1716 236 C ATOM 1849 N VAL B 212 5.991 5.827 -5.930 1.00 49.13 N ANISOU 1849 N VAL B 212 5179 7132 6357 867 -1530 213 N ATOM 1850 CA VAL B 212 5.655 5.488 -4.551 1.00 45.28 C ANISOU 1850 CA VAL B 212 4599 6667 5940 758 -1481 197 C ATOM 1851 C VAL B 212 6.783 4.721 -3.873 1.00 45.49 C ANISOU 1851 C VAL B 212 4711 6598 5976 655 -1426 190 C ATOM 1852 O VAL B 212 7.194 5.061 -2.767 1.00 41.18 O ANISOU 1852 O VAL B 212 4158 6014 5474 625 -1331 201 O ATOM 1853 CB VAL B 212 4.359 4.675 -4.456 1.00 48.02 C ANISOU 1853 CB VAL B 212 4814 7124 6309 673 -1567 158 C ATOM 1854 CG1 VAL B 212 4.137 4.205 -3.019 1.00 43.20 C ANISOU 1854 CG1 VAL B 212 4126 6521 5765 546 -1510 140 C ATOM 1855 CG2 VAL B 212 3.179 5.504 -4.955 1.00 51.15 C ANISOU 1855 CG2 VAL B 212 5102 7630 6702 779 -1615 164 C ATOM 1856 N GLN B 213 7.275 3.681 -4.538 1.00 44.79 N ANISOU 1856 N GLN B 213 4706 6471 5841 604 -1486 171 N ATOM 1857 CA GLN B 213 8.431 2.948 -4.044 1.00 40.93 C ANISOU 1857 CA GLN B 213 4314 5889 5348 525 -1440 165 C ATOM 1858 C GLN B 213 9.656 3.871 -3.945 1.00 39.53 C ANISOU 1858 C GLN B 213 4230 5628 5162 604 -1343 200 C ATOM 1859 O GLN B 213 10.426 3.795 -2.980 1.00 35.71 O ANISOU 1859 O GLN B 213 3775 5088 4707 553 -1263 203 O ATOM 1860 CB GLN B 213 8.723 1.741 -4.943 1.00 38.22 C ANISOU 1860 CB GLN B 213 4056 5521 4946 478 -1527 141 C ATOM 1861 CG GLN B 213 10.023 1.020 -4.631 1.00 42.42 C ANISOU 1861 CG GLN B 213 4706 5955 5458 423 -1484 137 C ATOM 1862 CD GLN B 213 9.990 0.298 -3.301 0.50 43.71 C ANISOU 1862 CD GLN B 213 4832 6108 5669 298 -1445 116 C ATOM 1863 OE1 GLN B 213 8.992 -0.331 -2.948 0.50 49.48 O ANISOU 1863 OE1 GLN B 213 5480 6897 6423 211 -1491 88 O ATOM 1864 NE2 GLN B 213 11.087 0.378 -2.557 0.50 36.29 N ANISOU 1864 NE2 GLN B 213 3955 5094 4741 287 -1359 127 N ATOM 1865 N LEU B 214 9.828 4.748 -4.935 1.00 34.71 N ANISOU 1865 N LEU B 214 3668 5009 4509 727 -1348 226 N ATOM 1866 CA LEU B 214 10.957 5.679 -4.934 1.00 34.82 C ANISOU 1866 CA LEU B 214 3773 4946 4510 801 -1255 258 C ATOM 1867 C LEU B 214 10.918 6.599 -3.714 1.00 32.19 C ANISOU 1867 C LEU B 214 3382 4612 4236 803 -1153 275 C ATOM 1868 O LEU B 214 11.950 6.859 -3.098 1.00 26.41 O ANISOU 1868 O LEU B 214 2707 3812 3514 786 -1065 286 O ATOM 1869 CB LEU B 214 11.010 6.510 -6.223 1.00 24.93 C ANISOU 1869 CB LEU B 214 2584 3689 3200 933 -1277 282 C ATOM 1870 CG LEU B 214 12.030 7.662 -6.222 1.00 24.24 C ANISOU 1870 CG LEU B 214 2584 3530 3098 1013 -1173 316 C ATOM 1871 CD1 LEU B 214 13.466 7.146 -6.190 1.00 23.50 C ANISOU 1871 CD1 LEU B 214 2596 3351 2980 968 -1128 313 C ATOM 1872 CD2 LEU B 214 11.816 8.633 -7.394 1.00 20.48 C ANISOU 1872 CD2 LEU B 214 2157 3057 2567 1151 -1192 342 C ATOM 1873 N ASN B 215 9.726 7.083 -3.372 1.00 27.73 N ANISOU 1873 N ASN B 215 2703 4124 3708 824 -1165 276 N ATOM 1874 CA ASN B 215 9.557 7.951 -2.212 1.00 29.44 C ANISOU 1874 CA ASN B 215 2861 4344 3980 828 -1072 292 C ATOM 1875 C ASN B 215 9.949 7.265 -0.903 1.00 35.27 C ANISOU 1875 C ASN B 215 3579 5053 4767 703 -1021 275 C ATOM 1876 O ASN B 215 10.564 7.882 -0.029 1.00 31.44 O ANISOU 1876 O ASN B 215 3116 4520 4310 700 -923 291 O ATOM 1877 CB ASN B 215 8.127 8.475 -2.122 1.00 30.98 C ANISOU 1877 CB ASN B 215 2930 4638 4202 875 -1103 294 C ATOM 1878 CG ASN B 215 7.955 9.495 -1.014 1.00 37.19 C ANISOU 1878 CG ASN B 215 3669 5424 5039 899 -1002 315 C ATOM 1879 OD1 ASN B 215 8.462 10.615 -1.101 1.00 42.10 O ANISOU 1879 OD1 ASN B 215 4355 5997 5643 989 -932 346 O ATOM 1880 ND2 ASN B 215 7.237 9.114 0.038 1.00 32.54 N ANISOU 1880 ND2 ASN B 215 2971 4885 4509 816 -992 297 N ATOM 1881 N LEU B 216 9.599 5.988 -0.773 1.00 32.86 N ANISOU 1881 N LEU B 216 3241 4773 4469 599 -1086 241 N ATOM 1882 CA LEU B 216 9.974 5.226 0.410 1.00 31.19 C ANISOU 1882 CA LEU B 216 3025 4529 4296 480 -1044 223 C ATOM 1883 C LEU B 216 11.490 5.163 0.571 1.00 27.07 C ANISOU 1883 C LEU B 216 2622 3911 3751 474 -983 232 C ATOM 1884 O LEU B 216 12.011 5.392 1.659 1.00 21.12 O ANISOU 1884 O LEU B 216 1872 3120 3033 437 -901 236 O ATOM 1885 CB LEU B 216 9.403 3.809 0.358 1.00 36.97 C ANISOU 1885 CB LEU B 216 3726 5297 5025 372 -1129 184 C ATOM 1886 CG LEU B 216 7.883 3.656 0.358 1.00 48.71 C ANISOU 1886 CG LEU B 216 5080 6889 6539 345 -1191 166 C ATOM 1887 CD1 LEU B 216 7.518 2.178 0.449 1.00 52.99 C ANISOU 1887 CD1 LEU B 216 5611 7448 7076 214 -1260 125 C ATOM 1888 CD2 LEU B 216 7.247 4.447 1.498 1.00 43.80 C ANISOU 1888 CD2 LEU B 216 4354 6307 5983 346 -1118 176 C ATOM 1889 N LEU B 217 12.193 4.837 -0.512 1.00 27.72 N ANISOU 1889 N LEU B 217 2801 3958 3775 511 -1024 232 N ATOM 1890 CA LEU B 217 13.653 4.774 -0.482 1.00 23.00 C ANISOU 1890 CA LEU B 217 2313 3278 3150 513 -969 239 C ATOM 1891 C LEU B 217 14.231 6.127 -0.083 1.00 20.46 C ANISOU 1891 C LEU B 217 2008 2923 2843 579 -867 270 C ATOM 1892 O LEU B 217 15.142 6.203 0.740 1.00 25.03 O ANISOU 1892 O LEU B 217 2619 3453 3436 543 -793 271 O ATOM 1893 CB LEU B 217 14.220 4.377 -1.848 1.00 26.08 C ANISOU 1893 CB LEU B 217 2799 3641 3469 561 -1028 239 C ATOM 1894 CG LEU B 217 13.831 3.041 -2.488 1.00 30.07 C ANISOU 1894 CG LEU B 217 3319 4165 3941 506 -1133 210 C ATOM 1895 CD1 LEU B 217 14.661 2.828 -3.743 1.00 30.14 C ANISOU 1895 CD1 LEU B 217 3443 4131 3878 565 -1165 215 C ATOM 1896 CD2 LEU B 217 14.028 1.886 -1.525 1.00 22.72 C ANISOU 1896 CD2 LEU B 217 2388 3214 3030 387 -1131 182 C ATOM 1897 N TYR B 218 13.700 7.190 -0.678 1.00 20.84 N ANISOU 1897 N TYR B 218 2038 2998 2882 676 -864 294 N ATOM 1898 CA TYR B 218 14.172 8.537 -0.390 1.00 20.32 C ANISOU 1898 CA TYR B 218 2000 2898 2823 743 -767 324 C ATOM 1899 C TYR B 218 13.987 8.858 1.075 1.00 20.58 C ANISOU 1899 C TYR B 218 1968 2934 2919 688 -693 324 C ATOM 1900 O TYR B 218 14.917 9.314 1.732 1.00 19.76 O ANISOU 1900 O TYR B 218 1908 2776 2822 674 -607 333 O ATOM 1901 CB TYR B 218 13.433 9.575 -1.231 1.00 17.35 C ANISOU 1901 CB TYR B 218 1612 2555 2423 859 -784 348 C ATOM 1902 CG TYR B 218 13.624 10.996 -0.743 1.00 19.86 C ANISOU 1902 CG TYR B 218 1945 2845 2754 922 -682 378 C ATOM 1903 CD1 TYR B 218 14.884 11.592 -0.748 1.00 20.35 C ANISOU 1903 CD1 TYR B 218 2107 2832 2791 938 -599 393 C ATOM 1904 CD2 TYR B 218 12.551 11.740 -0.276 1.00 20.18 C ANISOU 1904 CD2 TYR B 218 1903 2936 2829 962 -666 390 C ATOM 1905 CE1 TYR B 218 15.061 12.885 -0.296 1.00 16.90 C ANISOU 1905 CE1 TYR B 218 1693 2367 2362 987 -504 419 C ATOM 1906 CE2 TYR B 218 12.719 13.039 0.172 1.00 17.66 C ANISOU 1906 CE2 TYR B 218 1608 2585 2516 1021 -571 418 C ATOM 1907 CZ TYR B 218 13.971 13.605 0.159 1.00 17.03 C ANISOU 1907 CZ TYR B 218 1635 2425 2409 1030 -491 432 C ATOM 1908 OH TYR B 218 14.138 14.896 0.602 1.00 16.99 O ANISOU 1908 OH TYR B 218 1664 2385 2406 1081 -394 458 O ATOM 1909 N VAL B 219 12.784 8.615 1.586 1.00 20.00 N ANISOU 1909 N VAL B 219 1787 2924 2887 655 -727 313 N ATOM 1910 CA VAL B 219 12.494 8.905 2.985 1.00 20.75 C ANISOU 1910 CA VAL B 219 1817 3025 3042 603 -658 313 C ATOM 1911 C VAL B 219 13.434 8.168 3.937 1.00 20.33 C ANISOU 1911 C VAL B 219 1801 2919 3006 503 -617 296 C ATOM 1912 O VAL B 219 13.912 8.751 4.906 1.00 17.94 O ANISOU 1912 O VAL B 219 1506 2581 2730 488 -530 306 O ATOM 1913 CB VAL B 219 11.023 8.629 3.348 1.00 23.41 C ANISOU 1913 CB VAL B 219 2027 3447 3420 575 -704 300 C ATOM 1914 CG1 VAL B 219 10.804 8.766 4.853 1.00 21.71 C ANISOU 1914 CG1 VAL B 219 1752 3231 3265 509 -631 297 C ATOM 1915 CG2 VAL B 219 10.114 9.591 2.596 1.00 20.66 C ANISOU 1915 CG2 VAL B 219 1636 3155 3059 690 -728 320 C ATOM 1916 N GLN B 220 13.711 6.900 3.651 1.00 15.54 N ANISOU 1916 N GLN B 220 1222 2304 2377 439 -680 270 N ATOM 1917 CA GLN B 220 14.584 6.103 4.515 1.00 20.48 C ANISOU 1917 CA GLN B 220 1889 2883 3012 351 -650 252 C ATOM 1918 C GLN B 220 16.023 6.638 4.524 1.00 16.10 C ANISOU 1918 C GLN B 220 1425 2262 2431 383 -580 266 C ATOM 1919 O GLN B 220 16.630 6.804 5.586 1.00 13.47 O ANISOU 1919 O GLN B 220 1100 1896 2123 342 -509 265 O ATOM 1920 CB GLN B 220 14.561 4.622 4.102 1.00 24.68 C ANISOU 1920 CB GLN B 220 2445 3417 3515 285 -736 222 C ATOM 1921 CG GLN B 220 15.483 3.719 4.931 1.00 28.94 C ANISOU 1921 CG GLN B 220 3038 3904 4052 203 -711 202 C ATOM 1922 CD GLN B 220 15.028 3.590 6.377 1.00 36.10 C ANISOU 1922 CD GLN B 220 3883 4818 5016 124 -666 192 C ATOM 1923 OE1 GLN B 220 14.015 2.954 6.666 1.00 44.41 O ANISOU 1923 OE1 GLN B 220 4873 5910 6092 61 -707 173 O ATOM 1924 NE2 GLN B 220 15.777 4.195 7.292 1.00 32.02 N ANISOU 1924 NE2 GLN B 220 3384 4263 4520 124 -579 202 N ATOM 1925 N ALA B 221 16.562 6.914 3.339 1.00 16.72 N ANISOU 1925 N ALA B 221 1572 2324 2459 455 -598 277 N ATOM 1926 CA ALA B 221 17.938 7.399 3.225 1.00 16.67 C ANISOU 1926 CA ALA B 221 1649 2261 2422 484 -533 288 C ATOM 1927 C ALA B 221 18.106 8.773 3.855 1.00 13.33 C ANISOU 1927 C ALA B 221 1219 1822 2024 517 -436 312 C ATOM 1928 O ALA B 221 19.080 9.017 4.572 1.00 12.72 O ANISOU 1928 O ALA B 221 1174 1707 1953 488 -364 311 O ATOM 1929 CB ALA B 221 18.378 7.430 1.769 1.00 16.14 C ANISOU 1929 CB ALA B 221 1656 2183 2293 555 -573 296 C ATOM 1930 N ARG B 222 17.154 9.658 3.567 1.00 13.91 N ANISOU 1930 N ARG B 222 1251 1926 2108 581 -435 332 N ATOM 1931 CA ARG B 222 17.139 11.008 4.115 1.00 15.89 C ANISOU 1931 CA ARG B 222 1499 2160 2378 621 -345 357 C ATOM 1932 C ARG B 222 17.122 10.992 5.639 1.00 18.78 C ANISOU 1932 C ARG B 222 1817 2519 2798 545 -286 349 C ATOM 1933 O ARG B 222 17.934 11.665 6.279 1.00 12.98 O ANISOU 1933 O ARG B 222 1121 1742 2068 535 -201 357 O ATOM 1934 CB ARG B 222 15.926 11.788 3.591 1.00 16.71 C ANISOU 1934 CB ARG B 222 1558 2308 2484 706 -367 377 C ATOM 1935 CG ARG B 222 15.871 13.260 4.036 1.00 15.50 C ANISOU 1935 CG ARG B 222 1418 2132 2339 763 -274 406 C ATOM 1936 CD ARG B 222 14.444 13.811 3.977 1.00 21.42 C ANISOU 1936 CD ARG B 222 2091 2940 3108 828 -297 420 C ATOM 1937 NE ARG B 222 13.550 13.094 4.885 1.00 19.41 N ANISOU 1937 NE ARG B 222 1728 2738 2910 757 -326 401 N ATOM 1938 CZ ARG B 222 12.219 13.159 4.845 1.00 24.55 C ANISOU 1938 CZ ARG B 222 2285 3460 3582 789 -370 402 C ATOM 1939 NH1 ARG B 222 11.603 13.920 3.942 1.00 20.64 N ANISOU 1939 NH1 ARG B 222 1792 2995 3057 901 -394 422 N ATOM 1940 NH2 ARG B 222 11.501 12.461 5.716 1.00 21.79 N ANISOU 1940 NH2 ARG B 222 1841 3156 3284 711 -388 381 N ATOM 1941 N ASP B 223 16.193 10.233 6.222 1.00 18.37 N ANISOU 1941 N ASP B 223 1684 2509 2785 489 -330 332 N ATOM 1942 CA ASP B 223 16.091 10.173 7.677 1.00 18.80 C ANISOU 1942 CA ASP B 223 1695 2557 2891 417 -276 324 C ATOM 1943 C ASP B 223 17.388 9.635 8.296 1.00 15.95 C ANISOU 1943 C ASP B 223 1393 2146 2522 351 -242 308 C ATOM 1944 O ASP B 223 17.850 10.160 9.299 1.00 12.12 O ANISOU 1944 O ASP B 223 914 1630 2058 324 -164 312 O ATOM 1945 CB ASP B 223 14.883 9.335 8.128 1.00 20.57 C ANISOU 1945 CB ASP B 223 1826 2835 3153 359 -331 306 C ATOM 1946 CG ASP B 223 13.539 10.018 7.846 1.00 24.56 C ANISOU 1946 CG ASP B 223 2251 3402 3678 422 -348 321 C ATOM 1947 OD1 ASP B 223 13.517 11.179 7.374 1.00 23.80 O ANISOU 1947 OD1 ASP B 223 2178 3301 3565 515 -313 348 O ATOM 1948 OD2 ASP B 223 12.493 9.381 8.099 1.00 27.24 O ANISOU 1948 OD2 ASP B 223 2506 3798 4047 378 -396 305 O ATOM 1949 N ASP B 224 17.978 8.603 7.688 1.00 12.36 N ANISOU 1949 N ASP B 224 982 1682 2033 328 -300 289 N ATOM 1950 CA ASP B 224 19.233 8.043 8.194 1.00 11.68 C ANISOU 1950 CA ASP B 224 952 1555 1931 278 -274 272 C ATOM 1951 C ASP B 224 20.336 9.106 8.224 1.00 15.08 C ANISOU 1951 C ASP B 224 1438 1948 2344 314 -190 288 C ATOM 1952 O ASP B 224 21.136 9.154 9.162 1.00 14.14 O ANISOU 1952 O ASP B 224 1335 1803 2235 270 -134 279 O ATOM 1953 CB ASP B 224 19.692 6.842 7.366 1.00 11.66 C ANISOU 1953 CB ASP B 224 997 1550 1884 267 -350 252 C ATOM 1954 CG ASP B 224 18.967 5.553 7.739 1.00 20.70 C ANISOU 1954 CG ASP B 224 2108 2714 3044 195 -416 227 C ATOM 1955 OD1 ASP B 224 18.245 5.528 8.759 1.00 18.17 O ANISOU 1955 OD1 ASP B 224 1726 2406 2770 144 -396 223 O ATOM 1956 OD2 ASP B 224 19.126 4.554 7.007 1.00 19.48 O ANISOU 1956 OD2 ASP B 224 1992 2559 2852 187 -485 212 O ATOM 1957 N ILE B 225 20.374 9.961 7.204 1.00 11.74 N ANISOU 1957 N ILE B 225 1047 1524 1891 393 -182 309 N ATOM 1958 CA ILE B 225 21.369 11.028 7.151 1.00 16.76 C ANISOU 1958 CA ILE B 225 1740 2123 2505 423 -99 324 C ATOM 1959 C ILE B 225 21.044 12.142 8.145 1.00 11.30 C ANISOU 1959 C ILE B 225 1024 1420 1851 420 -17 340 C ATOM 1960 O ILE B 225 21.911 12.594 8.881 1.00 10.88 O ANISOU 1960 O ILE B 225 997 1336 1800 387 56 337 O ATOM 1961 CB ILE B 225 21.506 11.598 5.725 1.00 20.71 C ANISOU 1961 CB ILE B 225 2295 2618 2955 508 -112 342 C ATOM 1962 CG1 ILE B 225 22.237 10.600 4.827 1.00 17.30 C ANISOU 1962 CG1 ILE B 225 1910 2184 2479 507 -170 325 C ATOM 1963 CG2 ILE B 225 22.277 12.906 5.733 1.00 20.61 C ANISOU 1963 CG2 ILE B 225 2340 2568 2924 538 -15 360 C ATOM 1964 CD1 ILE B 225 21.910 10.772 3.364 1.00 12.11 C ANISOU 1964 CD1 ILE B 225 1289 1534 1777 587 -219 339 C ATOM 1965 N LEU B 226 19.784 12.561 8.179 1.00 11.81 N ANISOU 1965 N LEU B 226 1035 1512 1942 454 -29 355 N ATOM 1966 CA LEU B 226 19.375 13.637 9.069 1.00 16.08 C ANISOU 1966 CA LEU B 226 1555 2041 2514 461 48 373 C ATOM 1967 C LEU B 226 19.540 13.295 10.550 1.00 17.90 C ANISOU 1967 C LEU B 226 1752 2261 2787 375 87 357 C ATOM 1968 O LEU B 226 19.950 14.147 11.332 1.00 19.81 O ANISOU 1968 O LEU B 226 2016 2471 3039 363 170 366 O ATOM 1969 CB LEU B 226 17.939 14.066 8.780 1.00 12.61 C ANISOU 1969 CB LEU B 226 1058 1643 2093 523 21 391 C ATOM 1970 CG LEU B 226 17.756 14.829 7.473 1.00 13.15 C ANISOU 1970 CG LEU B 226 1170 1711 2114 626 7 414 C ATOM 1971 CD1 LEU B 226 16.282 15.159 7.254 1.00 13.93 C ANISOU 1971 CD1 LEU B 226 1200 1863 2232 689 -29 428 C ATOM 1972 CD2 LEU B 226 18.607 16.092 7.498 1.00 13.76 C ANISOU 1972 CD2 LEU B 226 1332 1732 2163 658 105 434 C ATOM 1973 N ASN B 227 19.227 12.061 10.938 1.00 13.92 N ANISOU 1973 N ASN B 227 1203 1780 2306 314 28 334 N ATOM 1974 CA ASN B 227 19.346 11.689 12.347 1.00 18.28 C ANISOU 1974 CA ASN B 227 1730 2320 2895 234 62 318 C ATOM 1975 C ASN B 227 20.680 11.041 12.706 1.00 14.88 C ANISOU 1975 C ASN B 227 1350 1860 2444 180 71 295 C ATOM 1976 O ASN B 227 20.868 10.608 13.835 1.00 18.06 O ANISOU 1976 O ASN B 227 1741 2251 2870 115 91 279 O ATOM 1977 CB ASN B 227 18.160 10.835 12.819 1.00 22.89 C ANISOU 1977 CB ASN B 227 2237 2942 3518 191 11 305 C ATOM 1978 CG ASN B 227 18.120 9.459 12.172 1.00 24.12 C ANISOU 1978 CG ASN B 227 2393 3118 3654 161 -82 282 C ATOM 1979 OD1 ASN B 227 19.148 8.897 11.804 1.00 22.58 O ANISOU 1979 OD1 ASN B 227 2257 2900 3423 151 -101 269 O ATOM 1980 ND2 ASN B 227 16.920 8.901 12.053 1.00 24.82 N ANISOU 1980 ND2 ASN B 227 2415 3251 3764 146 -139 276 N ATOM 1981 N GLY B 228 21.594 10.980 11.738 1.00 11.84 N ANISOU 1981 N GLY B 228 1022 1466 2012 212 56 293 N ATOM 1982 CA GLY B 228 22.947 10.507 11.982 1.00 9.97 C ANISOU 1982 CA GLY B 228 831 1207 1748 175 69 273 C ATOM 1983 C GLY B 228 23.209 9.005 11.990 1.00 11.61 C ANISOU 1983 C GLY B 228 1045 1424 1944 134 -1 245 C ATOM 1984 O GLY B 228 24.333 8.580 12.262 1.00 12.42 O ANISOU 1984 O GLY B 228 1183 1513 2023 109 10 226 O ATOM 1985 N SER B 229 22.192 8.197 11.713 1.00 9.81 N ANISOU 1985 N SER B 229 782 1219 1727 125 -72 240 N ATOM 1986 CA SER B 229 22.400 6.758 11.543 1.00 9.74 C ANISOU 1986 CA SER B 229 794 1212 1696 91 -143 214 C ATOM 1987 C SER B 229 23.370 6.498 10.384 1.00 14.44 C ANISOU 1987 C SER B 229 1451 1803 2234 136 -171 211 C ATOM 1988 O SER B 229 24.126 5.524 10.396 1.00 13.12 O ANISOU 1988 O SER B 229 1323 1626 2036 116 -200 190 O ATOM 1989 CB SER B 229 21.072 6.044 11.271 1.00 10.38 C ANISOU 1989 CB SER B 229 830 1321 1794 73 -214 210 C ATOM 1990 OG SER B 229 20.173 6.212 12.356 1.00 15.24 O ANISOU 1990 OG SER B 229 1384 1944 2460 28 -186 211 O ATOM 1991 N HIS B 230 23.336 7.367 9.377 1.00 11.28 N ANISOU 1991 N HIS B 230 1063 1408 1816 202 -161 233 N ATOM 1992 CA HIS B 230 24.316 7.308 8.292 1.00 9.88 C ANISOU 1992 CA HIS B 230 946 1223 1583 248 -172 232 C ATOM 1993 C HIS B 230 25.216 8.546 8.338 1.00 9.67 C ANISOU 1993 C HIS B 230 947 1181 1548 272 -84 245 C ATOM 1994 O HIS B 230 24.870 9.592 7.797 1.00 9.96 O ANISOU 1994 O HIS B 230 987 1214 1582 320 -54 269 O ATOM 1995 CB HIS B 230 23.621 7.179 6.932 1.00 10.39 C ANISOU 1995 CB HIS B 230 1020 1304 1624 303 -238 243 C ATOM 1996 CG HIS B 230 24.569 7.051 5.779 1.00 13.98 C ANISOU 1996 CG HIS B 230 1543 1750 2020 351 -252 243 C ATOM 1997 ND1 HIS B 230 24.152 7.090 4.467 1.00 14.21 N ANISOU 1997 ND1 HIS B 230 1596 1787 2017 410 -302 255 N ATOM 1998 CD2 HIS B 230 25.914 6.895 5.741 1.00 10.03 C ANISOU 1998 CD2 HIS B 230 1090 1236 1486 350 -221 231 C ATOM 1999 CE1 HIS B 230 25.197 6.945 3.671 1.00 13.19 C ANISOU 1999 CE1 HIS B 230 1530 1644 1837 442 -298 251 C ATOM 2000 NE2 HIS B 230 26.279 6.830 4.418 1.00 12.64 N ANISOU 2000 NE2 HIS B 230 1472 1565 1766 407 -249 237 N ATOM 2001 N PRO B 231 26.371 8.431 9.011 1.00 17.12 N ANISOU 2001 N PRO B 231 1909 2114 2482 238 -41 228 N ATOM 2002 CA PRO B 231 27.280 9.575 9.147 1.00 20.21 C ANISOU 2002 CA PRO B 231 2323 2493 2863 246 46 235 C ATOM 2003 C PRO B 231 27.869 9.983 7.795 1.00 15.29 C ANISOU 2003 C PRO B 231 1751 1868 2190 304 51 245 C ATOM 2004 O PRO B 231 28.286 9.123 7.020 1.00 11.82 O ANISOU 2004 O PRO B 231 1340 1437 1714 325 -2 234 O ATOM 2005 CB PRO B 231 28.389 9.050 10.075 1.00 16.43 C ANISOU 2005 CB PRO B 231 1847 2016 2378 195 68 208 C ATOM 2006 CG PRO B 231 27.866 7.775 10.651 1.00 16.37 C ANISOU 2006 CG PRO B 231 1819 2013 2388 160 3 191 C ATOM 2007 CD PRO B 231 26.899 7.222 9.660 1.00 12.82 C ANISOU 2007 CD PRO B 231 1369 1571 1930 192 -73 199 C ATOM 2008 N VAL B 232 27.887 11.283 7.519 1.00 9.49 N ANISOU 2008 N VAL B 232 1036 1117 1451 332 116 267 N ATOM 2009 CA VAL B 232 28.451 11.794 6.277 1.00 15.29 C ANISOU 2009 CA VAL B 232 1828 1845 2137 385 133 277 C ATOM 2010 C VAL B 232 29.270 13.041 6.574 1.00 11.28 C ANISOU 2010 C VAL B 232 1349 1317 1619 371 237 283 C ATOM 2011 O VAL B 232 29.161 13.615 7.660 1.00 12.78 O ANISOU 2011 O VAL B 232 1514 1497 1842 329 289 284 O ATOM 2012 CB VAL B 232 27.355 12.141 5.248 1.00 13.44 C ANISOU 2012 CB VAL B 232 1606 1606 1894 453 94 303 C ATOM 2013 CG1 VAL B 232 26.579 10.885 4.826 1.00 10.37 C ANISOU 2013 CG1 VAL B 232 1193 1240 1509 463 -12 295 C ATOM 2014 CG2 VAL B 232 26.415 13.193 5.815 1.00 10.44 C ANISOU 2014 CG2 VAL B 232 1202 1215 1552 462 137 326 C ATOM 2015 N SER B 233 30.089 13.453 5.613 1.00 9.87 N ANISOU 2015 N SER B 233 1226 1132 1392 400 267 285 N ATOM 2016 CA SER B 233 30.934 14.638 5.775 1.00 10.08 C ANISOU 2016 CA SER B 233 1290 1141 1401 380 369 288 C ATOM 2017 C SER B 233 30.096 15.896 5.660 1.00 10.86 C ANISOU 2017 C SER B 233 1417 1204 1507 413 415 319 C ATOM 2018 O SER B 233 28.960 15.853 5.194 1.00 10.56 O ANISOU 2018 O SER B 233 1372 1162 1477 467 365 339 O ATOM 2019 CB SER B 233 32.056 14.663 4.729 1.00 12.39 C ANISOU 2019 CB SER B 233 1635 1438 1636 399 391 279 C ATOM 2020 OG SER B 233 31.534 14.781 3.409 1.00 17.35 O ANISOU 2020 OG SER B 233 2311 2050 2232 472 357 301 O ATOM 2021 N PHE B 234 30.660 17.016 6.096 1.00 15.93 N ANISOU 2021 N PHE B 234 2090 1821 2140 381 512 322 N ATOM 2022 CA PHE B 234 30.003 18.309 5.969 1.00 12.04 C ANISOU 2022 CA PHE B 234 1645 1288 1643 417 568 352 C ATOM 2023 C PHE B 234 29.604 18.574 4.524 1.00 16.09 C ANISOU 2023 C PHE B 234 2217 1785 2113 502 544 374 C ATOM 2024 O PHE B 234 28.462 18.948 4.232 1.00 17.88 O ANISOU 2024 O PHE B 234 2450 1999 2346 564 520 400 O ATOM 2025 CB PHE B 234 30.936 19.416 6.450 1.00 15.14 C ANISOU 2025 CB PHE B 234 2083 1653 2016 363 680 347 C ATOM 2026 CG PHE B 234 30.390 20.805 6.249 1.00 18.70 C ANISOU 2026 CG PHE B 234 2604 2053 2449 401 748 378 C ATOM 2027 CD1 PHE B 234 29.210 21.191 6.849 1.00 17.12 C ANISOU 2027 CD1 PHE B 234 2384 1838 2285 428 744 399 C ATOM 2028 CD2 PHE B 234 31.077 21.729 5.480 1.00 22.13 C ANISOU 2028 CD2 PHE B 234 3129 2454 2827 410 822 384 C ATOM 2029 CE1 PHE B 234 28.716 22.470 6.680 1.00 20.95 C ANISOU 2029 CE1 PHE B 234 2940 2274 2747 472 808 427 C ATOM 2030 CE2 PHE B 234 30.589 23.007 5.301 1.00 24.59 C ANISOU 2030 CE2 PHE B 234 3519 2711 3114 448 887 413 C ATOM 2031 CZ PHE B 234 29.405 23.377 5.905 1.00 20.07 C ANISOU 2031 CZ PHE B 234 2927 2122 2575 483 879 435 C ATOM 2032 N GLU B 235 30.555 18.373 3.622 1.00 14.54 N ANISOU 2032 N GLU B 235 2063 1592 1869 508 550 364 N ATOM 2033 CA GLU B 235 30.329 18.630 2.213 1.00 15.45 C ANISOU 2033 CA GLU B 235 2247 1689 1936 586 533 383 C ATOM 2034 C GLU B 235 29.200 17.766 1.636 1.00 13.85 C ANISOU 2034 C GLU B 235 2010 1507 1745 649 421 393 C ATOM 2035 O GLU B 235 28.350 18.256 0.892 1.00 14.27 O ANISOU 2035 O GLU B 235 2100 1543 1780 724 402 418 O ATOM 2036 CB GLU B 235 31.636 18.452 1.431 1.00 24.01 C ANISOU 2036 CB GLU B 235 3377 2777 2968 572 561 366 C ATOM 2037 CG GLU B 235 32.712 19.480 1.796 1.00 31.78 C ANISOU 2037 CG GLU B 235 4406 3741 3930 512 679 358 C ATOM 2038 CD GLU B 235 33.467 19.141 3.082 1.00 42.03 C ANISOU 2038 CD GLU B 235 5634 5071 5263 420 704 327 C ATOM 2039 OE1 GLU B 235 33.296 18.019 3.616 1.00 41.26 O ANISOU 2039 OE1 GLU B 235 5463 5012 5202 406 631 311 O ATOM 2040 OE2 GLU B 235 34.244 20.003 3.557 1.00 44.30 O ANISOU 2040 OE2 GLU B 235 5948 5346 5538 361 798 318 O ATOM 2041 N LYS B 236 29.184 16.484 1.975 1.00 12.98 N ANISOU 2041 N LYS B 236 1833 1435 1662 619 346 372 N ATOM 2042 CA LYS B 236 28.098 15.619 1.525 1.00 13.75 C ANISOU 2042 CA LYS B 236 1895 1556 1774 664 240 377 C ATOM 2043 C LYS B 236 26.754 16.047 2.127 1.00 11.86 C ANISOU 2043 C LYS B 236 1609 1319 1578 682 227 395 C ATOM 2044 O LYS B 236 25.742 16.081 1.435 1.00 13.43 O ANISOU 2044 O LYS B 236 1808 1524 1770 748 172 412 O ATOM 2045 CB LYS B 236 28.389 14.152 1.849 1.00 14.12 C ANISOU 2045 CB LYS B 236 1890 1638 1837 620 170 349 C ATOM 2046 CG LYS B 236 29.449 13.525 0.969 1.00 15.84 C ANISOU 2046 CG LYS B 236 2152 1861 2004 629 156 333 C ATOM 2047 CD LYS B 236 29.065 13.593 -0.497 1.00 22.98 C ANISOU 2047 CD LYS B 236 3116 2754 2862 709 114 351 C ATOM 2048 CE LYS B 236 30.261 13.265 -1.380 1.00 28.91 C ANISOU 2048 CE LYS B 236 3924 3502 3557 720 127 339 C ATOM 2049 NZ LYS B 236 29.890 13.211 -2.817 1.00 34.61 N ANISOU 2049 NZ LYS B 236 4708 4211 4231 798 79 355 N ATOM 2050 N ALA B 237 26.754 16.378 3.413 1.00 11.56 N ANISOU 2050 N ALA B 237 1531 1278 1583 625 278 390 N ATOM 2051 CA ALA B 237 25.535 16.804 4.091 1.00 11.75 C ANISOU 2051 CA ALA B 237 1508 1305 1649 639 276 407 C ATOM 2052 C ALA B 237 24.869 17.948 3.345 1.00 12.38 C ANISOU 2052 C ALA B 237 1643 1361 1701 725 302 439 C ATOM 2053 O ALA B 237 23.640 17.987 3.201 1.00 12.78 O ANISOU 2053 O ALA B 237 1656 1431 1768 779 253 454 O ATOM 2054 CB ALA B 237 25.830 17.208 5.535 1.00 11.37 C ANISOU 2054 CB ALA B 237 1432 1246 1641 568 347 399 C ATOM 2055 N CYS B 238 25.687 18.876 2.864 1.00 13.33 N ANISOU 2055 N CYS B 238 1851 1440 1774 740 379 448 N ATOM 2056 CA CYS B 238 25.172 20.056 2.186 1.00 13.17 C ANISOU 2056 CA CYS B 238 1903 1385 1716 823 416 478 C ATOM 2057 C CYS B 238 24.675 19.720 0.790 1.00 13.64 C ANISOU 2057 C CYS B 238 1990 1456 1736 909 338 489 C ATOM 2058 O CYS B 238 23.774 20.382 0.276 1.00 14.24 O ANISOU 2058 O CYS B 238 2093 1524 1794 995 328 514 O ATOM 2059 CB CYS B 238 26.249 21.142 2.120 1.00 14.97 C ANISOU 2059 CB CYS B 238 2228 1559 1900 802 529 482 C ATOM 2060 SG CYS B 238 26.603 21.888 3.729 1.00 20.16 S ANISOU 2060 SG CYS B 238 2870 2194 2595 716 629 477 S ATOM 2061 N GLU B 239 25.281 18.702 0.177 1.00 18.17 N ANISOU 2061 N GLU B 239 2561 2049 2294 890 284 469 N ATOM 2062 CA GLU B 239 24.847 18.214 -1.127 1.00 16.59 C ANISOU 2062 CA GLU B 239 2385 1863 2057 963 200 476 C ATOM 2063 C GLU B 239 23.488 17.549 -1.013 1.00 16.10 C ANISOU 2063 C GLU B 239 2236 1849 2034 989 101 476 C ATOM 2064 O GLU B 239 22.620 17.765 -1.854 1.00 14.63 O ANISOU 2064 O GLU B 239 2065 1672 1823 1074 51 493 O ATOM 2065 CB GLU B 239 25.840 17.206 -1.710 1.00 13.94 C ANISOU 2065 CB GLU B 239 2066 1536 1696 931 167 453 C ATOM 2066 CG GLU B 239 27.038 17.816 -2.407 1.00 35.16 C ANISOU 2066 CG GLU B 239 4851 4183 4324 936 244 455 C ATOM 2067 CD GLU B 239 28.042 16.762 -2.850 1.00 40.08 C ANISOU 2067 CD GLU B 239 5479 4823 4926 903 214 430 C ATOM 2068 OE1 GLU B 239 27.610 15.726 -3.398 1.00 31.52 O ANISOU 2068 OE1 GLU B 239 4372 3766 3839 927 116 423 O ATOM 2069 OE2 GLU B 239 29.259 16.971 -2.648 1.00 45.88 O ANISOU 2069 OE2 GLU B 239 6241 5547 5645 852 288 416 O ATOM 2070 N PHE B 240 23.326 16.712 0.014 1.00 13.56 N ANISOU 2070 N PHE B 240 1824 1560 1768 915 72 456 N ATOM 2071 CA PHE B 240 22.030 16.101 0.311 1.00 18.24 C ANISOU 2071 CA PHE B 240 2325 2201 2403 922 -10 454 C ATOM 2072 C PHE B 240 20.980 17.179 0.583 1.00 14.85 C ANISOU 2072 C PHE B 240 1879 1774 1988 982 19 479 C ATOM 2073 O PHE B 240 19.903 17.173 -0.009 1.00 16.31 O ANISOU 2073 O PHE B 240 2038 1993 2168 1051 -46 490 O ATOM 2074 CB PHE B 240 22.128 15.136 1.494 1.00 13.19 C ANISOU 2074 CB PHE B 240 1606 1586 1819 824 -26 428 C ATOM 2075 CG PHE B 240 22.819 13.835 1.165 1.00 12.83 C ANISOU 2075 CG PHE B 240 1565 1552 1759 780 -84 402 C ATOM 2076 CD1 PHE B 240 24.041 13.511 1.745 1.00 12.23 C ANISOU 2076 CD1 PHE B 240 1504 1458 1683 713 -38 383 C ATOM 2077 CD2 PHE B 240 22.237 12.925 0.298 1.00 13.16 C ANISOU 2077 CD2 PHE B 240 1593 1622 1784 806 -186 395 C ATOM 2078 CE1 PHE B 240 24.673 12.312 1.456 1.00 11.96 C ANISOU 2078 CE1 PHE B 240 1478 1434 1631 682 -90 360 C ATOM 2079 CE2 PHE B 240 22.865 11.723 0.000 1.00 12.87 C ANISOU 2079 CE2 PHE B 240 1572 1590 1729 769 -237 372 C ATOM 2080 CZ PHE B 240 24.086 11.418 0.571 1.00 12.97 C ANISOU 2080 CZ PHE B 240 1604 1584 1741 711 -189 355 C ATOM 2081 N GLY B 241 21.307 18.118 1.464 1.00 17.07 N ANISOU 2081 N GLY B 241 2179 2022 2284 959 117 489 N ATOM 2082 CA GLY B 241 20.412 19.237 1.732 1.00 16.08 C ANISOU 2082 CA GLY B 241 2055 1890 2164 1024 157 515 C ATOM 2083 C GLY B 241 19.983 19.984 0.476 1.00 15.38 C ANISOU 2083 C GLY B 241 2040 1788 2016 1141 144 540 C ATOM 2084 O GLY B 241 18.830 20.403 0.350 1.00 16.00 O ANISOU 2084 O GLY B 241 2089 1894 2099 1218 116 557 O ATOM 2085 N GLY B 242 20.919 20.167 -0.450 1.00 15.38 N ANISOU 2085 N GLY B 242 2138 1746 1958 1157 167 542 N ATOM 2086 CA GLY B 242 20.627 20.797 -1.732 1.00 16.10 C ANISOU 2086 CA GLY B 242 2313 1818 1985 1267 153 564 C ATOM 2087 C GLY B 242 19.528 20.084 -2.514 1.00 16.61 C ANISOU 2087 C GLY B 242 2321 1942 2048 1332 31 563 C ATOM 2088 O GLY B 242 18.595 20.722 -3.026 1.00 17.36 O ANISOU 2088 O GLY B 242 2430 2049 2119 1434 8 584 O ATOM 2089 N PHE B 243 19.635 18.759 -2.603 1.00 18.70 N ANISOU 2089 N PHE B 243 2524 2247 2335 1273 -50 537 N ATOM 2090 CA PHE B 243 18.611 17.952 -3.265 1.00 16.72 C ANISOU 2090 CA PHE B 243 2211 2057 2086 1314 -171 531 C ATOM 2091 C PHE B 243 17.322 18.030 -2.455 1.00 17.04 C ANISOU 2091 C PHE B 243 2141 2154 2181 1322 -198 533 C ATOM 2092 O PHE B 243 16.235 18.131 -3.011 1.00 17.79 O ANISOU 2092 O PHE B 243 2201 2294 2265 1402 -264 542 O ATOM 2093 CB PHE B 243 19.049 16.486 -3.401 1.00 16.25 C ANISOU 2093 CB PHE B 243 2116 2021 2039 1235 -243 501 C ATOM 2094 CG PHE B 243 20.102 16.250 -4.454 1.00 16.14 C ANISOU 2094 CG PHE B 243 2201 1966 1963 1247 -242 498 C ATOM 2095 CD1 PHE B 243 21.262 15.557 -4.147 1.00 16.35 C ANISOU 2095 CD1 PHE B 243 2243 1974 1995 1163 -217 477 C ATOM 2096 CD2 PHE B 243 19.933 16.717 -5.742 1.00 24.81 C ANISOU 2096 CD2 PHE B 243 3380 3048 2998 1346 -266 515 C ATOM 2097 CE1 PHE B 243 22.235 15.337 -5.109 1.00 18.32 C ANISOU 2097 CE1 PHE B 243 2581 2192 2189 1176 -213 474 C ATOM 2098 CE2 PHE B 243 20.903 16.501 -6.712 1.00 25.06 C ANISOU 2098 CE2 PHE B 243 3507 3042 2973 1356 -261 512 C ATOM 2099 CZ PHE B 243 22.056 15.813 -6.396 1.00 23.24 C ANISOU 2099 CZ PHE B 243 3285 2795 2749 1271 -233 492 C ATOM 2100 N GLN B 244 17.457 17.985 -1.134 1.00 17.10 N ANISOU 2100 N GLN B 244 2091 2161 2245 1241 -145 525 N ATOM 2101 CA GLN B 244 16.296 18.057 -0.258 1.00 19.93 C ANISOU 2101 CA GLN B 244 2343 2571 2658 1240 -159 526 C ATOM 2102 C GLN B 244 15.525 19.343 -0.519 1.00 20.53 C ANISOU 2102 C GLN B 244 2447 2645 2708 1358 -126 557 C ATOM 2103 O GLN B 244 14.295 19.346 -0.588 1.00 18.23 O ANISOU 2103 O GLN B 244 2078 2418 2433 1414 -183 561 O ATOM 2104 CB GLN B 244 16.716 17.965 1.214 1.00 16.07 C ANISOU 2104 CB GLN B 244 1813 2067 2226 1138 -89 515 C ATOM 2105 CG GLN B 244 15.545 17.705 2.165 1.00 16.28 C ANISOU 2105 CG GLN B 244 1717 2154 2315 1115 -115 509 C ATOM 2106 CD GLN B 244 15.955 17.696 3.628 1.00 18.10 C ANISOU 2106 CD GLN B 244 1918 2362 2597 1021 -41 500 C ATOM 2107 OE1 GLN B 244 17.073 17.315 3.970 1.00 15.40 O ANISOU 2107 OE1 GLN B 244 1615 1981 2256 944 -8 486 O ATOM 2108 NE2 GLN B 244 15.044 18.118 4.502 1.00 17.20 N ANISOU 2108 NE2 GLN B 244 1734 2276 2525 1030 -16 508 N ATOM 2109 N ALA B 245 16.262 20.435 -0.691 1.00 18.42 N ANISOU 2109 N ALA B 245 2295 2305 2397 1396 -33 578 N ATOM 2110 CA ALA B 245 15.660 21.726 -0.983 1.00 21.30 C ANISOU 2110 CA ALA B 245 2714 2653 2725 1514 8 609 C ATOM 2111 C ALA B 245 14.909 21.690 -2.316 1.00 24.94 C ANISOU 2111 C ALA B 245 3189 3150 3137 1628 -82 618 C ATOM 2112 O ALA B 245 13.768 22.140 -2.403 1.00 24.28 O ANISOU 2112 O ALA B 245 3062 3113 3051 1721 -113 632 O ATOM 2113 CB ALA B 245 16.722 22.823 -0.978 1.00 18.12 C ANISOU 2113 CB ALA B 245 2450 2156 2277 1519 126 627 C ATOM 2114 N GLN B 246 15.544 21.137 -3.346 1.00 23.84 N ANISOU 2114 N GLN B 246 3108 2994 2955 1624 -127 609 N ATOM 2115 CA GLN B 246 14.902 21.000 -4.649 1.00 19.84 C ANISOU 2115 CA GLN B 246 2619 2520 2399 1726 -219 614 C ATOM 2116 C GLN B 246 13.611 20.193 -4.537 1.00 20.28 C ANISOU 2116 C GLN B 246 2530 2679 2498 1730 -330 598 C ATOM 2117 O GLN B 246 12.619 20.483 -5.190 1.00 21.19 O ANISOU 2117 O GLN B 246 2624 2841 2586 1837 -392 608 O ATOM 2118 CB GLN B 246 15.845 20.309 -5.633 1.00 26.74 C ANISOU 2118 CB GLN B 246 3567 3363 3230 1697 -253 602 C ATOM 2119 CG GLN B 246 15.325 20.256 -7.062 1.00 25.01 C ANISOU 2119 CG GLN B 246 3392 3163 2948 1805 -340 609 C ATOM 2120 CD GLN B 246 15.491 21.580 -7.786 1.00 28.13 C ANISOU 2120 CD GLN B 246 3926 3495 3268 1921 -276 641 C ATOM 2121 OE1 GLN B 246 16.185 22.479 -7.307 1.00 26.44 O ANISOU 2121 OE1 GLN B 246 3790 3211 3043 1908 -160 655 O ATOM 2122 NE2 GLN B 246 14.855 21.706 -8.945 1.00 31.89 N ANISOU 2122 NE2 GLN B 246 4439 3991 3688 2035 -350 650 N ATOM 2123 N ILE B 247 13.642 19.165 -3.704 1.00 23.52 N ANISOU 2123 N ILE B 247 2840 3124 2972 1612 -356 572 N ATOM 2124 CA ILE B 247 12.493 18.297 -3.517 1.00 21.21 C ANISOU 2124 CA ILE B 247 2408 2928 2724 1592 -455 551 C ATOM 2125 C ILE B 247 11.348 19.029 -2.822 1.00 22.23 C ANISOU 2125 C ILE B 247 2454 3109 2885 1649 -436 565 C ATOM 2126 O ILE B 247 10.208 19.005 -3.295 1.00 23.09 O ANISOU 2126 O ILE B 247 2493 3295 2987 1724 -514 564 O ATOM 2127 CB ILE B 247 12.905 17.043 -2.733 1.00 21.67 C ANISOU 2127 CB ILE B 247 2399 2998 2838 1445 -473 520 C ATOM 2128 CG1 ILE B 247 13.771 16.149 -3.628 1.00 18.90 C ANISOU 2128 CG1 ILE B 247 2115 2618 2448 1408 -523 504 C ATOM 2129 CG2 ILE B 247 11.686 16.295 -2.217 1.00 22.47 C ANISOU 2129 CG2 ILE B 247 2351 3193 2994 1406 -548 499 C ATOM 2130 CD1 ILE B 247 14.531 15.090 -2.891 1.00 18.01 C ANISOU 2130 CD1 ILE B 247 1979 2489 2374 1276 -515 478 C ATOM 2131 N GLN B 248 11.657 19.708 -1.722 1.00 22.33 N ANISOU 2131 N GLN B 248 2476 3080 2929 1619 -331 576 N ATOM 2132 CA GLN B 248 10.626 20.354 -0.906 1.00 23.72 C ANISOU 2132 CA GLN B 248 2570 3302 3139 1664 -302 588 C ATOM 2133 C GLN B 248 10.137 21.696 -1.455 1.00 24.71 C ANISOU 2133 C GLN B 248 2765 3414 3209 1820 -271 622 C ATOM 2134 O GLN B 248 8.977 22.053 -1.267 1.00 28.19 O ANISOU 2134 O GLN B 248 3124 3924 3662 1896 -294 629 O ATOM 2135 CB GLN B 248 11.083 20.509 0.562 1.00 21.10 C ANISOU 2135 CB GLN B 248 2220 2933 2864 1567 -205 586 C ATOM 2136 CG GLN B 248 11.361 19.177 1.275 1.00 19.24 C ANISOU 2136 CG GLN B 248 1903 2720 2688 1420 -238 552 C ATOM 2137 CD GLN B 248 11.764 19.329 2.747 1.00 23.10 C ANISOU 2137 CD GLN B 248 2374 3174 3230 1329 -146 550 C ATOM 2138 OE1 GLN B 248 12.381 18.434 3.326 1.00 18.53 O ANISOU 2138 OE1 GLN B 248 1775 2582 2684 1213 -147 527 O ATOM 2139 NE2 GLN B 248 11.404 20.455 3.355 1.00 25.01 N ANISOU 2139 NE2 GLN B 248 2627 3399 3476 1387 -67 574 N ATOM 2140 N PHE B 249 11.006 22.437 -2.134 1.00 26.06 N ANISOU 2140 N PHE B 249 3087 3498 3315 1871 -216 642 N ATOM 2141 CA PHE B 249 10.652 23.792 -2.563 1.00 27.20 C ANISOU 2141 CA PHE B 249 3323 3613 3400 2017 -169 675 C ATOM 2142 C PHE B 249 10.538 23.939 -4.068 1.00 29.63 C ANISOU 2142 C PHE B 249 3709 3918 3629 2129 -234 685 C ATOM 2143 O PHE B 249 9.960 24.910 -4.559 1.00 29.52 O ANISOU 2143 O PHE B 249 3751 3902 3562 2269 -225 710 O ATOM 2144 CB PHE B 249 11.668 24.804 -2.033 1.00 25.25 C ANISOU 2144 CB PHE B 249 3206 3256 3132 1997 -31 695 C ATOM 2145 CG PHE B 249 11.936 24.674 -0.568 1.00 22.26 C ANISOU 2145 CG PHE B 249 2767 2867 2823 1882 38 686 C ATOM 2146 CD1 PHE B 249 13.228 24.539 -0.094 1.00 23.59 C ANISOU 2146 CD1 PHE B 249 2997 2963 3002 1767 110 676 C ATOM 2147 CD2 PHE B 249 10.892 24.674 0.338 1.00 29.67 C ANISOU 2147 CD2 PHE B 249 3583 3873 3816 1889 30 684 C ATOM 2148 CE1 PHE B 249 13.476 24.414 1.262 1.00 21.01 C ANISOU 2148 CE1 PHE B 249 2617 2628 2736 1663 169 666 C ATOM 2149 CE2 PHE B 249 11.133 24.550 1.695 1.00 34.05 C ANISOU 2149 CE2 PHE B 249 4089 4416 4434 1784 94 676 C ATOM 2150 CZ PHE B 249 12.426 24.421 2.157 1.00 24.98 C ANISOU 2150 CZ PHE B 249 3007 3191 3292 1672 162 667 C ATOM 2151 N GLY B 250 11.088 22.976 -4.801 1.00 31.09 N ANISOU 2151 N GLY B 250 3906 4103 3803 2071 -300 665 N ATOM 2152 CA GLY B 250 11.194 23.104 -6.241 1.00 31.69 C ANISOU 2152 CA GLY B 250 4079 4160 3800 2165 -351 673 C ATOM 2153 C GLY B 250 12.444 23.889 -6.582 1.00 22.90 C ANISOU 2153 C GLY B 250 3143 2929 2630 2170 -247 692 C ATOM 2154 O GLY B 250 13.272 24.135 -5.711 1.00 32.22 O ANISOU 2154 O GLY B 250 4353 4052 3838 2082 -149 692 O ATOM 2155 N PRO B 251 12.583 24.295 -7.849 1.00 29.89 N ANISOU 2155 N PRO B 251 4146 3779 3432 2270 -268 707 N ATOM 2156 CA PRO B 251 13.780 25.002 -8.321 1.00 31.57 C ANISOU 2156 CA PRO B 251 4534 3880 3582 2273 -171 722 C ATOM 2157 C PRO B 251 14.160 26.191 -7.440 1.00 29.32 C ANISOU 2157 C PRO B 251 4322 3523 3295 2270 -34 744 C ATOM 2158 O PRO B 251 13.298 26.822 -6.838 1.00 29.62 O ANISOU 2158 O PRO B 251 4318 3589 3349 2333 -16 758 O ATOM 2159 CB PRO B 251 13.367 25.485 -9.715 1.00 30.62 C ANISOU 2159 CB PRO B 251 4513 3749 3371 2423 -221 741 C ATOM 2160 CG PRO B 251 12.352 24.485 -10.159 1.00 30.45 C ANISOU 2160 CG PRO B 251 4361 3837 3372 2448 -368 721 C ATOM 2161 CD PRO B 251 11.584 24.124 -8.920 1.00 32.44 C ANISOU 2161 CD PRO B 251 4444 4168 3713 2389 -383 708 C ATOM 2162 N HIS B 252 15.452 26.491 -7.387 1.00 30.38 N ANISOU 2162 N HIS B 252 4567 3569 3408 2197 63 744 N ATOM 2163 CA HIS B 252 15.978 27.565 -6.552 1.00 28.56 C ANISOU 2163 CA HIS B 252 4416 3263 3172 2170 199 760 C ATOM 2164 C HIS B 252 15.511 28.965 -6.981 1.00 25.83 C ANISOU 2164 C HIS B 252 4202 2864 2749 2316 254 795 C ATOM 2165 O HIS B 252 15.586 29.332 -8.154 1.00 29.00 O ANISOU 2165 O HIS B 252 4719 3228 3070 2409 241 809 O ATOM 2166 CB HIS B 252 17.508 27.485 -6.542 1.00 30.00 C ANISOU 2166 CB HIS B 252 4684 3372 3343 2055 280 748 C ATOM 2167 CG HIS B 252 18.167 28.498 -5.657 1.00 38.41 C ANISOU 2167 CG HIS B 252 5829 4362 4405 2004 419 758 C ATOM 2168 ND1 HIS B 252 18.113 28.433 -4.281 1.00 33.60 N ANISOU 2168 ND1 HIS B 252 5127 3772 3867 1919 457 749 N ATOM 2169 CD2 HIS B 252 18.915 29.588 -5.954 1.00 36.73 C ANISOU 2169 CD2 HIS B 252 5782 4053 4122 2019 530 775 C ATOM 2170 CE1 HIS B 252 18.792 29.444 -3.768 1.00 33.77 C ANISOU 2170 CE1 HIS B 252 5255 3714 3864 1885 583 760 C ATOM 2171 NE2 HIS B 252 19.289 30.159 -4.761 1.00 42.24 N ANISOU 2171 NE2 HIS B 252 6485 4715 4850 1942 630 775 N ATOM 2172 N VAL B 253 15.026 29.744 -6.022 1.00 31.00 N ANISOU 2172 N VAL B 253 4843 3512 3424 2339 318 810 N ATOM 2173 CA VAL B 253 14.607 31.118 -6.291 1.00 37.81 C ANISOU 2173 CA VAL B 253 5839 4316 4210 2476 382 844 C ATOM 2174 C VAL B 253 15.499 32.082 -5.520 1.00 42.38 C ANISOU 2174 C VAL B 253 6534 4793 4773 2409 532 854 C ATOM 2175 O VAL B 253 15.379 32.220 -4.303 1.00 40.82 O ANISOU 2175 O VAL B 253 6272 4606 4634 2348 580 852 O ATOM 2176 CB VAL B 253 13.134 31.352 -5.911 1.00 41.57 C ANISOU 2176 CB VAL B 253 6215 4872 4708 2591 329 856 C ATOM 2177 CG1 VAL B 253 12.775 32.832 -6.043 1.00 42.20 C ANISOU 2177 CG1 VAL B 253 6444 4884 4707 2732 410 892 C ATOM 2178 CG2 VAL B 253 12.224 30.497 -6.779 1.00 45.97 C ANISOU 2178 CG2 VAL B 253 6666 5531 5268 2665 179 845 C ATOM 2179 N GLU B 254 16.390 32.746 -6.246 1.00 49.61 N ANISOU 2179 N GLU B 254 7628 5613 5609 2417 607 865 N ATOM 2180 CA GLU B 254 17.472 33.528 -5.652 1.00 49.15 C ANISOU 2180 CA GLU B 254 7688 5456 5532 2323 749 867 C ATOM 2181 C GLU B 254 17.026 34.569 -4.621 1.00 48.89 C ANISOU 2181 C GLU B 254 7689 5387 5500 2353 837 887 C ATOM 2182 O GLU B 254 17.600 34.655 -3.536 1.00 49.55 O ANISOU 2182 O GLU B 254 7749 5448 5629 2233 911 876 O ATOM 2183 CB GLU B 254 18.303 34.189 -6.757 1.00 51.42 C ANISOU 2183 CB GLU B 254 8173 5647 5718 2353 812 878 C ATOM 2184 CG GLU B 254 19.649 34.717 -6.301 1.00 49.45 C ANISOU 2184 CG GLU B 254 8029 5308 5452 2221 947 870 C ATOM 2185 CD GLU B 254 20.592 34.967 -7.464 0.50 48.39 C ANISOU 2185 CD GLU B 254 8051 5101 5235 2217 990 870 C ATOM 2186 OE1 GLU B 254 21.016 33.984 -8.109 0.50 43.15 O ANISOU 2186 OE1 GLU B 254 7331 4478 4587 2176 921 851 O ATOM 2187 OE2 GLU B 254 20.910 36.145 -7.732 0.50 50.49 O ANISOU 2187 OE2 GLU B 254 8501 5267 5417 2254 1096 890 O ATOM 2188 N HIS B 255 16.009 35.357 -4.948 1.00 55.00 N ANISOU 2188 N HIS B 255 8519 6157 6221 2516 827 916 N ATOM 2189 CA HIS B 255 15.613 36.455 -4.064 1.00 58.63 C ANISOU 2189 CA HIS B 255 9040 6570 6666 2560 920 939 C ATOM 2190 C HIS B 255 14.816 35.990 -2.840 1.00 54.09 C ANISOU 2190 C HIS B 255 8281 6082 6187 2531 884 930 C ATOM 2191 O HIS B 255 14.510 36.784 -1.953 1.00 57.07 O ANISOU 2191 O HIS B 255 8690 6428 6566 2551 961 946 O ATOM 2192 CB HIS B 255 14.878 37.564 -4.838 1.00 64.37 C ANISOU 2192 CB HIS B 255 9917 7251 7290 2754 937 974 C ATOM 2193 CG HIS B 255 13.488 37.202 -5.264 1.00 74.87 C ANISOU 2193 CG HIS B 255 11131 8687 8629 2905 811 982 C ATOM 2194 ND1 HIS B 255 12.370 37.845 -4.775 1.00 82.67 N ANISOU 2194 ND1 HIS B 255 12096 9704 9610 3032 814 1004 N ATOM 2195 CD2 HIS B 255 13.033 36.276 -6.141 1.00 78.79 C ANISOU 2195 CD2 HIS B 255 11528 9270 9137 2950 679 969 C ATOM 2196 CE1 HIS B 255 11.288 37.326 -5.327 1.00 84.29 C ANISOU 2196 CE1 HIS B 255 12184 10017 9825 3146 688 1003 C ATOM 2197 NE2 HIS B 255 11.662 36.371 -6.159 1.00 82.07 N ANISOU 2197 NE2 HIS B 255 11857 9770 9555 3096 603 981 N ATOM 2198 N LYS B 256 14.514 34.697 -2.786 1.00 49.11 N ANISOU 2198 N LYS B 256 7466 5557 5636 2477 772 905 N ATOM 2199 CA LYS B 256 13.714 34.132 -1.703 1.00 41.99 C ANISOU 2199 CA LYS B 256 6382 4746 4827 2446 729 894 C ATOM 2200 C LYS B 256 14.517 33.143 -0.860 1.00 44.50 C ANISOU 2200 C LYS B 256 6592 5085 5232 2257 730 861 C ATOM 2201 O LYS B 256 14.466 33.172 0.370 1.00 50.17 O ANISOU 2201 O LYS B 256 7246 5809 6007 2185 776 856 O ATOM 2202 CB LYS B 256 12.485 33.437 -2.288 1.00 49.58 C ANISOU 2202 CB LYS B 256 7207 5824 5808 2550 590 891 C ATOM 2203 CG LYS B 256 11.541 32.803 -1.280 1.00 58.71 C ANISOU 2203 CG LYS B 256 8166 7085 7057 2524 537 878 C ATOM 2204 CD LYS B 256 10.516 31.943 -2.010 1.00 66.24 C ANISOU 2204 CD LYS B 256 8983 8158 8028 2597 392 866 C ATOM 2205 CE LYS B 256 9.183 31.890 -1.283 1.00 66.98 C ANISOU 2205 CE LYS B 256 8925 8352 8172 2658 352 868 C ATOM 2206 NZ LYS B 256 8.091 31.522 -2.230 1.00 64.56 N ANISOU 2206 NZ LYS B 256 8535 8149 7846 2783 226 865 N ATOM 2207 N HIS B 257 15.255 32.262 -1.525 1.00 39.94 N ANISOU 2207 N HIS B 257 5998 4517 4659 2183 678 839 N ATOM 2208 CA HIS B 257 16.030 31.241 -0.823 1.00 38.56 C ANISOU 2208 CA HIS B 257 5724 4367 4560 2015 670 806 C ATOM 2209 C HIS B 257 17.431 31.739 -0.500 1.00 35.66 C ANISOU 2209 C HIS B 257 5476 3905 4169 1906 786 801 C ATOM 2210 O HIS B 257 18.381 31.461 -1.227 1.00 27.70 O ANISOU 2210 O HIS B 257 4529 2868 3130 1858 789 789 O ATOM 2211 CB HIS B 257 16.115 29.948 -1.642 1.00 31.69 C ANISOU 2211 CB HIS B 257 4770 3562 3710 1988 552 783 C ATOM 2212 CG HIS B 257 14.782 29.390 -2.033 1.00 34.14 C ANISOU 2212 CG HIS B 257 4960 3971 4040 2083 431 783 C ATOM 2213 ND1 HIS B 257 14.476 29.035 -3.329 1.00 32.29 N ANISOU 2213 ND1 HIS B 257 4741 3765 3761 2166 341 784 N ATOM 2214 CD2 HIS B 257 13.668 29.142 -1.302 1.00 31.97 C ANISOU 2214 CD2 HIS B 257 4548 3775 3823 2106 387 782 C ATOM 2215 CE1 HIS B 257 13.235 28.581 -3.378 1.00 33.61 C ANISOU 2215 CE1 HIS B 257 4782 4030 3959 2233 242 781 C ATOM 2216 NE2 HIS B 257 12.722 28.636 -2.161 1.00 30.80 N ANISOU 2216 NE2 HIS B 257 4328 3707 3666 2198 269 780 N ATOM 2217 N LYS B 258 17.548 32.483 0.591 1.00 46.14 N ANISOU 2217 N LYS B 258 6833 5188 5508 1866 883 808 N ATOM 2218 CA LYS B 258 18.842 32.961 1.059 1.00 50.95 C ANISOU 2218 CA LYS B 258 7542 5717 6101 1749 995 799 C ATOM 2219 C LYS B 258 18.943 32.734 2.562 1.00 48.46 C ANISOU 2219 C LYS B 258 7133 5419 5862 1639 1030 784 C ATOM 2220 O LYS B 258 17.943 32.411 3.204 1.00 40.35 O ANISOU 2220 O LYS B 258 5987 4453 4890 1670 982 786 O ATOM 2221 CB LYS B 258 19.019 34.440 0.715 1.00 48.55 C ANISOU 2221 CB LYS B 258 7434 5309 5704 1821 1104 828 C ATOM 2222 CG LYS B 258 17.831 35.304 1.064 1.00 43.57 C ANISOU 2222 CG LYS B 258 6827 4672 5055 1951 1122 858 C ATOM 2223 CD LYS B 258 17.909 36.629 0.330 1.00 47.79 C ANISOU 2223 CD LYS B 258 7571 5108 5480 2054 1204 888 C ATOM 2224 CE LYS B 258 16.634 37.434 0.508 1.00 52.23 C ANISOU 2224 CE LYS B 258 8157 5673 6015 2212 1208 921 C ATOM 2225 NZ LYS B 258 16.531 38.512 -0.515 1.00 57.74 N ANISOU 2225 NZ LYS B 258 9051 6290 6599 2347 1252 951 N ATOM 2226 N PRO B 259 20.156 32.877 3.123 1.00 51.72 N ANISOU 2226 N PRO B 259 7593 5781 6277 1507 1112 766 N ATOM 2227 CA PRO B 259 20.391 32.688 4.557 1.00 51.45 C ANISOU 2227 CA PRO B 259 7483 5756 6308 1395 1150 749 C ATOM 2228 C PRO B 259 19.251 33.216 5.427 1.00 37.21 C ANISOU 2228 C PRO B 259 5646 3961 4529 1463 1167 771 C ATOM 2229 O PRO B 259 18.771 34.329 5.236 1.00 39.05 O ANISOU 2229 O PRO B 259 5990 4142 4705 1564 1223 800 O ATOM 2230 CB PRO B 259 21.671 33.484 4.792 1.00 55.51 C ANISOU 2230 CB PRO B 259 8130 6184 6777 1301 1270 742 C ATOM 2231 CG PRO B 259 22.431 33.289 3.519 1.00 54.58 C ANISOU 2231 CG PRO B 259 8079 6052 6607 1303 1255 735 C ATOM 2232 CD PRO B 259 21.407 33.186 2.406 1.00 50.97 C ANISOU 2232 CD PRO B 259 7622 5623 6121 1454 1171 758 C ATOM 2233 N GLY B 260 18.826 32.391 6.374 1.00 27.57 N ANISOU 2233 N GLY B 260 4277 2808 3392 1408 1120 755 N ATOM 2234 CA GLY B 260 17.699 32.705 7.221 1.00 24.75 C ANISOU 2234 CA GLY B 260 3862 2474 3067 1467 1126 771 C ATOM 2235 C GLY B 260 16.492 31.889 6.817 1.00 32.26 C ANISOU 2235 C GLY B 260 4677 3525 4058 1550 1007 772 C ATOM 2236 O GLY B 260 15.661 31.551 7.653 1.00 41.20 O ANISOU 2236 O GLY B 260 5694 4711 5248 1551 982 770 O ATOM 2237 N PHE B 261 16.405 31.558 5.532 1.00 33.74 N ANISOU 2237 N PHE B 261 4875 3736 4209 1616 935 774 N ATOM 2238 CA PHE B 261 15.225 30.889 4.986 1.00 32.18 C ANISOU 2238 CA PHE B 261 4560 3631 4034 1706 820 775 C ATOM 2239 C PHE B 261 14.976 29.513 5.586 1.00 33.86 C ANISOU 2239 C PHE B 261 4599 3930 4336 1613 738 745 C ATOM 2240 O PHE B 261 13.844 29.180 5.959 1.00 25.16 O ANISOU 2240 O PHE B 261 3379 2903 3278 1655 686 746 O ATOM 2241 CB PHE B 261 15.323 30.775 3.459 1.00 36.17 C ANISOU 2241 CB PHE B 261 5125 4139 4480 1784 760 780 C ATOM 2242 CG PHE B 261 14.115 30.147 2.825 1.00 39.65 C ANISOU 2242 CG PHE B 261 5452 4676 4935 1880 640 780 C ATOM 2243 CD1 PHE B 261 12.958 30.883 2.632 1.00 39.74 C ANISOU 2243 CD1 PHE B 261 5467 4712 4918 2028 632 807 C ATOM 2244 CD2 PHE B 261 14.130 28.817 2.437 1.00 38.77 C ANISOU 2244 CD2 PHE B 261 5232 4636 4865 1822 534 753 C ATOM 2245 CE1 PHE B 261 11.841 30.307 2.059 1.00 44.70 C ANISOU 2245 CE1 PHE B 261 5983 5441 5560 2113 518 804 C ATOM 2246 CE2 PHE B 261 13.018 28.235 1.860 1.00 37.87 C ANISOU 2246 CE2 PHE B 261 5012 4613 4763 1900 423 751 C ATOM 2247 CZ PHE B 261 11.872 28.979 1.670 1.00 44.19 C ANISOU 2247 CZ PHE B 261 5809 5445 5537 2044 413 775 C ATOM 2248 N LEU B 262 16.033 28.711 5.669 1.00 31.55 N ANISOU 2248 N LEU B 262 4293 3629 4065 1488 729 718 N ATOM 2249 CA LEU B 262 15.898 27.331 6.107 1.00 28.27 C ANISOU 2249 CA LEU B 262 3732 3287 3723 1400 647 688 C ATOM 2250 C LEU B 262 15.953 27.196 7.618 1.00 32.23 C ANISOU 2250 C LEU B 262 4173 3788 4286 1304 697 677 C ATOM 2251 O LEU B 262 16.729 27.878 8.296 1.00 30.24 O ANISOU 2251 O LEU B 262 4001 3467 4022 1249 794 680 O ATOM 2252 CB LEU B 262 17.004 26.458 5.506 1.00 23.93 C ANISOU 2252 CB LEU B 262 3197 2731 3165 1317 610 664 C ATOM 2253 CG LEU B 262 17.074 26.226 3.999 1.00 26.13 C ANISOU 2253 CG LEU B 262 3520 3018 3390 1387 544 667 C ATOM 2254 CD1 LEU B 262 18.290 25.354 3.673 1.00 24.81 C ANISOU 2254 CD1 LEU B 262 3364 2840 3221 1288 524 640 C ATOM 2255 CD2 LEU B 262 15.789 25.589 3.490 1.00 26.85 C ANISOU 2255 CD2 LEU B 262 3505 3197 3501 1463 431 667 C ATOM 2256 N ASP B 263 15.130 26.296 8.139 1.00 29.98 N ANISOU 2256 N ASP B 263 3748 3579 4065 1279 629 663 N ATOM 2257 CA ASP B 263 15.346 25.787 9.480 1.00 34.36 C ANISOU 2257 CA ASP B 263 4235 4139 4682 1164 655 644 C ATOM 2258 C ASP B 263 16.394 24.671 9.369 1.00 29.97 C ANISOU 2258 C ASP B 263 3662 3585 4140 1052 614 612 C ATOM 2259 O ASP B 263 16.059 23.508 9.127 1.00 27.56 O ANISOU 2259 O ASP B 263 3264 3341 3866 1025 522 592 O ATOM 2260 CB ASP B 263 14.037 25.268 10.073 1.00 37.19 C ANISOU 2260 CB ASP B 263 4456 4577 5099 1180 604 640 C ATOM 2261 CG ASP B 263 14.150 24.963 11.555 1.00 51.07 C ANISOU 2261 CG ASP B 263 6161 6329 6916 1076 649 626 C ATOM 2262 OD1 ASP B 263 15.265 25.086 12.113 1.00 51.02 O ANISOU 2262 OD1 ASP B 263 6219 6261 6905 990 710 616 O ATOM 2263 OD2 ASP B 263 13.122 24.599 12.163 1.00 57.06 O ANISOU 2263 OD2 ASP B 263 6812 7146 7722 1079 622 623 O ATOM 2264 N LEU B 264 17.663 25.041 9.533 1.00 23.29 N ANISOU 2264 N LEU B 264 2908 2672 3268 989 684 606 N ATOM 2265 CA LEU B 264 18.786 24.150 9.252 1.00 27.48 C ANISOU 2265 CA LEU B 264 3443 3201 3796 903 653 578 C ATOM 2266 C LEU B 264 18.707 22.752 9.871 1.00 29.81 C ANISOU 2266 C LEU B 264 3625 3550 4151 816 584 549 C ATOM 2267 O LEU B 264 19.250 21.786 9.316 1.00 22.35 O ANISOU 2267 O LEU B 264 2665 2626 3202 779 522 528 O ATOM 2268 CB LEU B 264 20.109 24.816 9.638 1.00 27.16 C ANISOU 2268 CB LEU B 264 3501 3092 3727 835 750 573 C ATOM 2269 CG LEU B 264 20.575 25.937 8.708 1.00 31.66 C ANISOU 2269 CG LEU B 264 4203 3602 4223 898 810 594 C ATOM 2270 CD1 LEU B 264 21.873 26.551 9.209 1.00 30.19 C ANISOU 2270 CD1 LEU B 264 4104 3355 4013 813 909 584 C ATOM 2271 CD2 LEU B 264 20.726 25.427 7.283 1.00 26.61 C ANISOU 2271 CD2 LEU B 264 3579 2984 3547 947 738 592 C ATOM 2272 N LYS B 265 18.048 22.630 11.016 1.00 25.96 N ANISOU 2272 N LYS B 265 3066 3083 3716 784 597 546 N ATOM 2273 CA LYS B 265 17.963 21.326 11.665 1.00 26.76 C ANISOU 2273 CA LYS B 265 3071 3227 3870 699 538 518 C ATOM 2274 C LYS B 265 17.041 20.350 10.920 1.00 25.36 C ANISOU 2274 C LYS B 265 2810 3120 3707 732 428 511 C ATOM 2275 O LYS B 265 17.080 19.143 11.165 1.00 24.75 O ANISOU 2275 O LYS B 265 2670 3075 3659 662 368 485 O ATOM 2276 CB LYS B 265 17.567 21.466 13.137 1.00 34.67 C ANISOU 2276 CB LYS B 265 4028 4224 4920 648 589 516 C ATOM 2277 CG LYS B 265 16.134 21.879 13.381 1.00 35.69 C ANISOU 2277 CG LYS B 265 4095 4390 5074 719 587 536 C ATOM 2278 CD LYS B 265 15.951 22.245 14.842 1.00 36.37 C ANISOU 2278 CD LYS B 265 4165 4454 5198 671 660 538 C ATOM 2279 CE LYS B 265 14.495 22.158 15.276 1.00 37.97 C ANISOU 2279 CE LYS B 265 4269 4715 5443 711 640 546 C ATOM 2280 NZ LYS B 265 13.582 22.991 14.443 1.00 38.18 N ANISOU 2280 NZ LYS B 265 4301 4766 5441 842 633 574 N ATOM 2281 N GLU B 266 16.230 20.875 10.003 1.00 21.61 N ANISOU 2281 N GLU B 266 2339 2668 3205 838 401 532 N ATOM 2282 CA GLU B 266 15.422 20.040 9.110 1.00 27.36 C ANISOU 2282 CA GLU B 266 2997 3463 3935 876 293 525 C ATOM 2283 C GLU B 266 16.237 19.531 7.920 1.00 20.00 C ANISOU 2283 C GLU B 266 2122 2520 2959 879 242 515 C ATOM 2284 O GLU B 266 15.810 18.626 7.200 1.00 16.71 O ANISOU 2284 O GLU B 266 1657 2151 2540 886 148 503 O ATOM 2285 CB GLU B 266 14.212 20.822 8.579 1.00 29.01 C ANISOU 2285 CB GLU B 266 3185 3708 4130 998 280 551 C ATOM 2286 CG GLU B 266 13.173 21.163 9.628 1.00 41.34 C ANISOU 2286 CG GLU B 266 4669 5302 5738 1008 312 558 C ATOM 2287 CD GLU B 266 12.764 19.951 10.443 1.00 50.34 C ANISOU 2287 CD GLU B 266 5696 6493 6940 909 266 530 C ATOM 2288 OE1 GLU B 266 12.627 18.860 9.855 1.00 54.22 O ANISOU 2288 OE1 GLU B 266 6138 7028 7435 878 175 509 O ATOM 2289 OE2 GLU B 266 12.582 20.088 11.671 1.00 51.69 O ANISOU 2289 OE2 GLU B 266 5833 6655 7151 860 322 529 O ATOM 2290 N PHE B 267 17.409 20.119 7.713 1.00 17.85 N ANISOU 2290 N PHE B 267 1953 2183 2646 871 307 520 N ATOM 2291 CA PHE B 267 18.173 19.864 6.498 1.00 14.60 C ANISOU 2291 CA PHE B 267 1608 1756 2183 891 273 516 C ATOM 2292 C PHE B 267 19.587 19.326 6.715 1.00 13.48 C ANISOU 2292 C PHE B 267 1506 1583 2035 799 297 493 C ATOM 2293 O PHE B 267 20.261 18.992 5.752 1.00 13.42 O ANISOU 2293 O PHE B 267 1545 1566 1986 809 268 487 O ATOM 2294 CB PHE B 267 18.212 21.128 5.633 1.00 16.48 C ANISOU 2294 CB PHE B 267 1946 1953 2361 992 321 546 C ATOM 2295 CG PHE B 267 16.900 21.439 4.956 1.00 17.06 C ANISOU 2295 CG PHE B 267 1989 2070 2424 1104 267 565 C ATOM 2296 CD1 PHE B 267 16.673 21.044 3.643 1.00 16.28 C ANISOU 2296 CD1 PHE B 267 1901 1996 2287 1167 185 566 C ATOM 2297 CD2 PHE B 267 15.897 22.121 5.629 1.00 18.77 C ANISOU 2297 CD2 PHE B 267 2162 2303 2664 1151 298 583 C ATOM 2298 CE1 PHE B 267 15.471 21.323 3.013 1.00 16.94 C ANISOU 2298 CE1 PHE B 267 1952 2126 2357 1273 131 582 C ATOM 2299 CE2 PHE B 267 14.686 22.406 5.006 1.00 20.86 C ANISOU 2299 CE2 PHE B 267 2391 2617 2917 1262 246 599 C ATOM 2300 CZ PHE B 267 14.469 22.000 3.699 1.00 20.31 C ANISOU 2300 CZ PHE B 267 2330 2578 2809 1322 160 598 C ATOM 2301 N LEU B 268 20.029 19.234 7.966 1.00 12.95 N ANISOU 2301 N LEU B 268 1417 1501 2004 715 347 480 N ATOM 2302 CA LEU B 268 21.391 18.802 8.264 1.00 12.29 C ANISOU 2302 CA LEU B 268 1365 1392 1911 633 374 457 C ATOM 2303 C LEU B 268 21.461 17.892 9.481 1.00 16.90 C ANISOU 2303 C LEU B 268 1879 1995 2547 540 360 432 C ATOM 2304 O LEU B 268 20.653 18.005 10.405 1.00 13.63 O ANISOU 2304 O LEU B 268 1410 1592 2176 526 373 437 O ATOM 2305 CB LEU B 268 22.303 20.010 8.494 1.00 12.22 C ANISOU 2305 CB LEU B 268 1445 1325 1872 624 482 468 C ATOM 2306 CG LEU B 268 22.600 20.895 7.287 1.00 16.85 C ANISOU 2306 CG LEU B 268 2128 1879 2395 699 512 488 C ATOM 2307 CD1 LEU B 268 23.233 22.218 7.718 1.00 18.67 C ANISOU 2307 CD1 LEU B 268 2444 2049 2600 686 628 500 C ATOM 2308 CD2 LEU B 268 23.481 20.164 6.267 1.00 12.81 C ANISOU 2308 CD2 LEU B 268 1646 1375 1847 691 467 471 C ATOM 2309 N PRO B 269 22.448 16.990 9.493 1.00 14.98 N ANISOU 2309 N PRO B 269 1642 1755 2296 480 336 406 N ATOM 2310 CA PRO B 269 22.777 16.235 10.708 1.00 14.63 C ANISOU 2310 CA PRO B 269 1553 1715 2289 391 338 382 C ATOM 2311 C PRO B 269 23.165 17.209 11.831 1.00 17.19 C ANISOU 2311 C PRO B 269 1900 2004 2627 354 437 386 C ATOM 2312 O PRO B 269 23.739 18.265 11.562 1.00 18.37 O ANISOU 2312 O PRO B 269 2117 2119 2744 375 506 399 O ATOM 2313 CB PRO B 269 23.992 15.405 10.290 1.00 10.32 C ANISOU 2313 CB PRO B 269 1037 1171 1712 357 311 357 C ATOM 2314 CG PRO B 269 24.005 15.445 8.776 1.00 10.68 C ANISOU 2314 CG PRO B 269 1123 1222 1712 428 271 368 C ATOM 2315 CD PRO B 269 23.397 16.742 8.398 1.00 11.18 C ANISOU 2315 CD PRO B 269 1218 1266 1764 496 317 399 C ATOM 2316 N LYS B 270 22.844 16.845 13.065 1.00 22.81 N ANISOU 2316 N LYS B 270 2562 2722 3384 297 444 376 N ATOM 2317 CA LYS B 270 23.063 17.684 14.245 1.00 27.28 C ANISOU 2317 CA LYS B 270 3143 3254 3967 259 532 379 C ATOM 2318 C LYS B 270 24.401 18.416 14.243 1.00 20.63 C ANISOU 2318 C LYS B 270 2374 2376 3087 233 604 374 C ATOM 2319 O LYS B 270 24.469 19.616 14.518 1.00 19.18 O ANISOU 2319 O LYS B 270 2239 2157 2892 243 684 391 O ATOM 2320 CB LYS B 270 22.959 16.811 15.499 1.00 36.63 C ANISOU 2320 CB LYS B 270 4274 4450 5195 184 516 357 C ATOM 2321 CG LYS B 270 23.158 17.534 16.814 1.00 52.34 C ANISOU 2321 CG LYS B 270 6277 6407 7204 138 599 358 C ATOM 2322 CD LYS B 270 23.407 16.530 17.937 1.00 60.21 C ANISOU 2322 CD LYS B 270 7238 7411 8230 59 579 330 C ATOM 2323 CE LYS B 270 23.452 17.200 19.311 1.00 67.12 C ANISOU 2323 CE LYS B 270 8122 8253 9126 14 657 332 C ATOM 2324 NZ LYS B 270 22.095 17.538 19.846 1.00 67.82 N ANISOU 2324 NZ LYS B 270 8171 8344 9255 37 673 352 N ATOM 2325 N GLU B 271 25.458 17.676 13.926 1.00 16.77 N ANISOU 2325 N GLU B 271 1896 1901 2576 199 576 349 N ATOM 2326 CA GLU B 271 26.838 18.165 13.973 1.00 24.29 C ANISOU 2326 CA GLU B 271 2901 2834 3493 160 636 336 C ATOM 2327 C GLU B 271 27.173 19.338 13.059 1.00 24.27 C ANISOU 2327 C GLU B 271 2975 2803 3445 204 695 355 C ATOM 2328 O GLU B 271 28.220 19.965 13.230 1.00 24.18 O ANISOU 2328 O GLU B 271 3010 2772 3406 163 763 345 O ATOM 2329 CB GLU B 271 27.794 17.008 13.651 1.00 24.13 C ANISOU 2329 CB GLU B 271 2868 2846 3455 132 582 306 C ATOM 2330 CG GLU B 271 27.140 15.940 12.770 1.00 24.94 C ANISOU 2330 CG GLU B 271 2940 2977 3558 176 484 306 C ATOM 2331 CD GLU B 271 27.981 14.693 12.620 1.00 31.89 C ANISOU 2331 CD GLU B 271 3810 3885 4422 149 428 277 C ATOM 2332 OE1 GLU B 271 28.831 14.407 13.492 1.00 50.58 O ANISOU 2332 OE1 GLU B 271 6170 6257 6792 92 449 252 O ATOM 2333 OE2 GLU B 271 27.783 13.984 11.626 1.00 28.76 O ANISOU 2333 OE2 GLU B 271 3414 3505 4007 188 360 277 O ATOM 2334 N TYR B 272 26.318 19.633 12.082 1.00 21.74 N ANISOU 2334 N TYR B 272 2668 2479 3111 285 669 381 N ATOM 2335 CA TYR B 272 26.685 20.629 11.071 1.00 13.81 C ANISOU 2335 CA TYR B 272 1747 1444 2054 332 717 399 C ATOM 2336 C TYR B 272 25.824 21.882 11.077 1.00 14.77 C ANISOU 2336 C TYR B 272 1914 1529 2171 390 773 432 C ATOM 2337 O TYR B 272 26.108 22.838 10.353 1.00 21.23 O ANISOU 2337 O TYR B 272 2816 2311 2941 428 826 448 O ATOM 2338 CB TYR B 272 26.690 20.012 9.661 1.00 19.31 C ANISOU 2338 CB TYR B 272 2453 2164 2721 389 646 400 C ATOM 2339 CG TYR B 272 27.644 18.842 9.502 1.00 15.08 C ANISOU 2339 CG TYR B 272 1891 1661 2178 343 598 368 C ATOM 2340 CD1 TYR B 272 27.216 17.637 8.950 1.00 11.99 C ANISOU 2340 CD1 TYR B 272 1455 1306 1795 368 499 361 C ATOM 2341 CD2 TYR B 272 28.968 18.944 9.911 1.00 11.48 C ANISOU 2341 CD2 TYR B 272 1455 1203 1705 277 651 345 C ATOM 2342 CE1 TYR B 272 28.079 16.564 8.814 1.00 12.73 C ANISOU 2342 CE1 TYR B 272 1534 1426 1878 333 456 333 C ATOM 2343 CE2 TYR B 272 29.839 17.883 9.779 1.00 16.30 C ANISOU 2343 CE2 TYR B 272 2040 1848 2306 245 608 316 C ATOM 2344 CZ TYR B 272 29.392 16.693 9.231 1.00 17.31 C ANISOU 2344 CZ TYR B 272 2133 2005 2440 277 511 311 C ATOM 2345 OH TYR B 272 30.268 15.639 9.098 1.00 12.93 O ANISOU 2345 OH TYR B 272 1563 1481 1870 253 470 283 O ATOM 2346 N ILE B 273 24.768 21.865 11.881 1.00 16.40 N ANISOU 2346 N ILE B 273 2067 1743 2421 400 762 442 N ATOM 2347 CA ILE B 273 23.837 22.976 11.957 1.00 28.28 C ANISOU 2347 CA ILE B 273 3606 3218 3923 465 809 474 C ATOM 2348 C ILE B 273 24.533 24.317 12.208 1.00 36.30 C ANISOU 2348 C ILE B 273 4723 4171 4899 447 922 484 C ATOM 2349 O ILE B 273 24.151 25.335 11.631 1.00 35.82 O ANISOU 2349 O ILE B 273 4735 4074 4800 519 963 511 O ATOM 2350 CB ILE B 273 22.775 22.722 13.044 1.00 26.02 C ANISOU 2350 CB ILE B 273 3240 2952 3693 458 795 478 C ATOM 2351 CG1 ILE B 273 21.902 21.524 12.651 1.00 27.05 C ANISOU 2351 CG1 ILE B 273 3278 3143 3856 483 687 472 C ATOM 2352 CG2 ILE B 273 21.923 23.953 13.255 1.00 31.54 C ANISOU 2352 CG2 ILE B 273 3980 3619 4386 525 857 510 C ATOM 2353 CD1 ILE B 273 20.943 21.068 13.743 1.00 26.24 C ANISOU 2353 CD1 ILE B 273 3089 3068 3813 458 668 468 C ATOM 2354 N LYS B 274 25.564 24.308 13.051 1.00 40.39 N ANISOU 2354 N LYS B 274 5249 4676 5421 351 969 460 N ATOM 2355 CA LYS B 274 26.258 25.537 13.439 1.00 44.73 C ANISOU 2355 CA LYS B 274 5892 5169 5936 314 1078 464 C ATOM 2356 C LYS B 274 27.571 25.779 12.702 1.00 43.27 C ANISOU 2356 C LYS B 274 5772 4970 5697 277 1114 448 C ATOM 2357 O LYS B 274 28.331 26.673 13.074 1.00 44.17 O ANISOU 2357 O LYS B 274 5958 5044 5782 222 1203 443 O ATOM 2358 CB LYS B 274 26.513 25.556 14.952 1.00 52.97 C ANISOU 2358 CB LYS B 274 6908 6205 7015 228 1119 447 C ATOM 2359 CG LYS B 274 25.404 26.215 15.762 1.00 59.74 C ANISOU 2359 CG LYS B 274 7767 7034 7896 263 1155 472 C ATOM 2360 CD LYS B 274 25.503 25.869 17.239 1.00 63.90 C ANISOU 2360 CD LYS B 274 8244 7566 8468 182 1168 454 C ATOM 2361 CE LYS B 274 25.219 24.391 17.471 1.00 68.82 C ANISOU 2361 CE LYS B 274 8757 8251 9142 163 1072 434 C ATOM 2362 NZ LYS B 274 24.899 24.103 18.897 1.00 70.00 N ANISOU 2362 NZ LYS B 274 8859 8400 9338 109 1082 424 N ATOM 2363 N GLN B 275 27.842 24.994 11.664 1.00 37.75 N ANISOU 2363 N GLN B 275 5052 4306 4984 303 1047 439 N ATOM 2364 CA GLN B 275 29.117 25.104 10.960 1.00 33.06 C ANISOU 2364 CA GLN B 275 4510 3709 4343 265 1079 422 C ATOM 2365 C GLN B 275 29.127 26.243 9.945 1.00 40.20 C ANISOU 2365 C GLN B 275 5529 4561 5184 322 1139 447 C ATOM 2366 O GLN B 275 28.126 26.500 9.279 1.00 35.83 O ANISOU 2366 O GLN B 275 4999 3994 4621 419 1113 476 O ATOM 2367 CB GLN B 275 29.491 23.785 10.289 1.00 29.26 C ANISOU 2367 CB GLN B 275 3966 3284 3867 268 988 401 C ATOM 2368 CG GLN B 275 30.849 23.814 9.586 1.00 33.37 C ANISOU 2368 CG GLN B 275 4530 3811 4340 230 1020 380 C ATOM 2369 CD GLN B 275 31.477 22.436 9.481 1.00 38.33 C ANISOU 2369 CD GLN B 275 5082 4499 4981 202 945 350 C ATOM 2370 OE1 GLN B 275 31.183 21.548 10.280 1.00 40.58 O ANISOU 2370 OE1 GLN B 275 5290 4817 5313 179 889 337 O ATOM 2371 NE2 GLN B 275 32.351 22.253 8.498 1.00 43.74 N ANISOU 2371 NE2 GLN B 275 5797 5198 5623 206 946 338 N ATOM 2372 N ARG B 276 30.274 26.913 9.835 1.00 47.38 N ANISOU 2372 N ARG B 276 6510 5443 6049 260 1221 433 N ATOM 2373 CA ARG B 276 30.421 28.092 8.982 1.00 55.47 C ANISOU 2373 CA ARG B 276 7662 6406 7006 296 1297 453 C ATOM 2374 C ARG B 276 30.011 27.861 7.531 1.00 50.88 C ANISOU 2374 C ARG B 276 7110 5828 6393 396 1243 472 C ATOM 2375 O ARG B 276 30.533 26.975 6.856 1.00 51.20 O ANISOU 2375 O ARG B 276 7112 5912 6431 391 1188 455 O ATOM 2376 CB ARG B 276 31.860 28.618 9.017 1.00 65.91 C ANISOU 2376 CB ARG B 276 9043 7713 8286 197 1385 427 C ATOM 2377 CG ARG B 276 32.126 29.727 7.997 1.00 77.39 C ANISOU 2377 CG ARG B 276 10637 9105 9665 227 1463 445 C ATOM 2378 CD ARG B 276 33.591 30.155 7.958 1.00 84.82 C ANISOU 2378 CD ARG B 276 11625 10041 10562 119 1548 414 C ATOM 2379 NE ARG B 276 34.050 30.692 9.238 1.00 89.08 N ANISOU 2379 NE ARG B 276 12165 10566 11114 16 1617 396 N ATOM 2380 CZ ARG B 276 35.036 31.576 9.368 1.00 91.05 C ANISOU 2380 CZ ARG B 276 12494 10784 11316 -76 1720 378 C ATOM 2381 NH1 ARG B 276 35.661 32.037 8.293 1.00 92.99 N ANISOU 2381 NH1 ARG B 276 12826 11007 11499 -78 1771 377 N ATOM 2382 NH2 ARG B 276 35.389 32.008 10.571 1.00 88.97 N ANISOU 2382 NH2 ARG B 276 12226 10512 11066 -168 1774 360 N ATOM 2383 N GLY B 277 29.081 28.682 7.059 1.00 50.15 N ANISOU 2383 N GLY B 277 7093 5690 6273 490 1261 508 N ATOM 2384 CA GLY B 277 28.700 28.684 5.659 1.00 45.54 C ANISOU 2384 CA GLY B 277 6559 5098 5646 590 1222 528 C ATOM 2385 C GLY B 277 27.864 27.498 5.223 1.00 37.00 C ANISOU 2385 C GLY B 277 5376 4078 4604 656 1096 530 C ATOM 2386 O GLY B 277 27.822 27.176 4.036 1.00 35.39 O ANISOU 2386 O GLY B 277 5196 3882 4367 717 1048 536 O ATOM 2387 N ALA B 278 27.190 26.857 6.176 1.00 34.77 N ANISOU 2387 N ALA B 278 4986 3836 4387 641 1043 525 N ATOM 2388 CA ALA B 278 26.369 25.685 5.880 1.00 29.78 C ANISOU 2388 CA ALA B 278 4254 3265 3796 688 924 524 C ATOM 2389 C ALA B 278 25.219 26.036 4.937 1.00 23.30 C ANISOU 2389 C ALA B 278 3465 2438 2950 816 883 555 C ATOM 2390 O ALA B 278 25.036 25.402 3.902 1.00 22.38 O ANISOU 2390 O ALA B 278 3338 2349 2817 868 807 556 O ATOM 2391 CB ALA B 278 25.836 25.066 7.168 1.00 26.34 C ANISOU 2391 CB ALA B 278 3708 2866 3432 642 892 513 C ATOM 2392 N GLU B 279 24.449 27.053 5.299 1.00 22.52 N ANISOU 2392 N GLU B 279 3408 2304 2843 870 932 582 N ATOM 2393 CA GLU B 279 23.287 27.425 4.510 1.00 28.01 C ANISOU 2393 CA GLU B 279 4128 3001 3515 1000 892 612 C ATOM 2394 C GLU B 279 23.701 27.906 3.119 1.00 26.88 C ANISOU 2394 C GLU B 279 4101 2818 3293 1062 907 624 C ATOM 2395 O GLU B 279 23.055 27.575 2.124 1.00 29.94 O ANISOU 2395 O GLU B 279 4482 3231 3662 1153 830 635 O ATOM 2396 CB GLU B 279 22.433 28.473 5.241 1.00 23.83 C ANISOU 2396 CB GLU B 279 3626 2440 2988 1050 951 638 C ATOM 2397 CG GLU B 279 21.087 28.753 4.573 1.00 37.10 C ANISOU 2397 CG GLU B 279 5304 4140 4652 1193 897 666 C ATOM 2398 CD GLU B 279 20.055 29.347 5.528 1.00 46.67 C ANISOU 2398 CD GLU B 279 6485 5354 5893 1236 926 685 C ATOM 2399 OE1 GLU B 279 20.438 29.772 6.638 1.00 54.13 O ANISOU 2399 OE1 GLU B 279 7444 6265 6857 1162 1004 681 O ATOM 2400 OE2 GLU B 279 18.857 29.384 5.168 1.00 43.09 O ANISOU 2400 OE2 GLU B 279 5991 4939 5440 1346 870 703 O ATOM 2401 N LYS B 280 24.784 28.671 3.044 1.00 26.40 N ANISOU 2401 N LYS B 280 4150 2696 3185 1010 1006 620 N ATOM 2402 CA LYS B 280 25.279 29.139 1.754 1.00 31.77 C ANISOU 2402 CA LYS B 280 4950 3333 3788 1058 1032 630 C ATOM 2403 C LYS B 280 25.653 27.955 0.859 1.00 30.76 C ANISOU 2403 C LYS B 280 4769 3254 3662 1053 943 611 C ATOM 2404 O LYS B 280 25.357 27.947 -0.340 1.00 26.86 O ANISOU 2404 O LYS B 280 4328 2755 3122 1141 901 625 O ATOM 2405 CB LYS B 280 26.472 30.082 1.937 1.00 40.70 C ANISOU 2405 CB LYS B 280 6196 4396 4872 978 1159 623 C ATOM 2406 CG LYS B 280 27.144 30.482 0.628 1.00 55.10 C ANISOU 2406 CG LYS B 280 8145 6177 6616 1007 1194 628 C ATOM 2407 CD LYS B 280 28.237 31.525 0.841 1.00 64.58 C ANISOU 2407 CD LYS B 280 9466 7307 7766 924 1329 621 C ATOM 2408 CE LYS B 280 29.040 31.770 -0.439 1.00 69.62 C ANISOU 2408 CE LYS B 280 10216 7909 8328 933 1365 619 C ATOM 2409 NZ LYS B 280 28.207 32.299 -1.562 1.00 68.15 N ANISOU 2409 NZ LYS B 280 10132 7680 8079 1076 1345 654 N ATOM 2410 N ARG B 281 26.295 26.951 1.450 1.00 27.37 N ANISOU 2410 N ARG B 281 4244 2873 3283 954 913 580 N ATOM 2411 CA ARG B 281 26.649 25.738 0.723 1.00 25.93 C ANISOU 2411 CA ARG B 281 4008 2739 3106 947 827 561 C ATOM 2412 C ARG B 281 25.418 24.980 0.236 1.00 15.27 C ANISOU 2412 C ARG B 281 2587 1437 1778 1033 708 571 C ATOM 2413 O ARG B 281 25.378 24.513 -0.895 1.00 21.29 O ANISOU 2413 O ARG B 281 3370 2211 2507 1086 647 572 O ATOM 2414 CB ARG B 281 27.490 24.819 1.599 1.00 27.21 C ANISOU 2414 CB ARG B 281 4078 2942 3317 831 819 526 C ATOM 2415 CG ARG B 281 28.937 24.708 1.195 1.00 37.45 C ANISOU 2415 CG ARG B 281 5420 4232 4577 764 867 503 C ATOM 2416 CD ARG B 281 29.526 23.413 1.745 1.00 41.89 C ANISOU 2416 CD ARG B 281 5875 4854 5185 688 812 469 C ATOM 2417 NE ARG B 281 30.942 23.284 1.441 1.00 47.55 N ANISOU 2417 NE ARG B 281 6621 5576 5870 624 858 444 N ATOM 2418 CZ ARG B 281 31.412 22.799 0.300 1.00 58.55 C ANISOU 2418 CZ ARG B 281 8045 6979 7223 655 828 439 C ATOM 2419 NH1 ARG B 281 30.573 22.397 -0.642 1.00 62.02 N ANISOU 2419 NH1 ARG B 281 8495 7422 7650 746 747 457 N ATOM 2420 NH2 ARG B 281 32.719 22.716 0.098 1.00 67.69 N ANISOU 2420 NH2 ARG B 281 9222 8146 8351 595 877 415 N ATOM 2421 N ILE B 282 24.424 24.834 1.104 1.00 17.86 N ANISOU 2421 N ILE B 282 2829 1796 2161 1042 674 576 N ATOM 2422 CA ILE B 282 23.197 24.141 0.726 1.00 21.74 C ANISOU 2422 CA ILE B 282 3241 2342 2676 1115 562 583 C ATOM 2423 C ILE B 282 22.527 24.831 -0.470 1.00 22.55 C ANISOU 2423 C ILE B 282 3427 2422 2717 1244 546 611 C ATOM 2424 O ILE B 282 22.104 24.173 -1.426 1.00 21.00 O ANISOU 2424 O ILE B 282 3212 2261 2507 1300 454 611 O ATOM 2425 CB ILE B 282 22.218 24.016 1.923 1.00 16.89 C ANISOU 2425 CB ILE B 282 2524 1764 2130 1101 545 584 C ATOM 2426 CG1 ILE B 282 22.779 23.047 2.967 1.00 17.94 C ANISOU 2426 CG1 ILE B 282 2567 1928 2322 982 534 553 C ATOM 2427 CG2 ILE B 282 20.840 23.553 1.463 1.00 16.09 C ANISOU 2427 CG2 ILE B 282 2349 1719 2044 1187 441 594 C ATOM 2428 CD1 ILE B 282 21.962 22.993 4.245 1.00 14.46 C ANISOU 2428 CD1 ILE B 282 2036 1512 1945 955 534 553 C ATOM 2429 N PHE B 283 22.458 26.157 -0.430 1.00 16.78 N ANISOU 2429 N PHE B 283 2797 1633 1947 1291 635 636 N ATOM 2430 CA PHE B 283 21.816 26.909 -1.510 1.00 17.66 C ANISOU 2430 CA PHE B 283 3001 1717 1993 1423 626 664 C ATOM 2431 C PHE B 283 22.599 26.887 -2.820 1.00 25.09 C ANISOU 2431 C PHE B 283 4044 2624 2864 1445 627 664 C ATOM 2432 O PHE B 283 22.006 26.969 -3.903 1.00 20.60 O ANISOU 2432 O PHE B 283 3519 2057 2249 1553 573 680 O ATOM 2433 CB PHE B 283 21.497 28.342 -1.088 1.00 21.52 C ANISOU 2433 CB PHE B 283 3581 2146 2450 1474 724 692 C ATOM 2434 CG PHE B 283 20.317 28.448 -0.166 1.00 25.62 C ANISOU 2434 CG PHE B 283 4008 2705 3022 1509 702 702 C ATOM 2435 CD1 PHE B 283 19.159 27.733 -0.422 1.00 30.76 C ANISOU 2435 CD1 PHE B 283 4549 3433 3704 1576 588 702 C ATOM 2436 CD2 PHE B 283 20.359 29.269 0.946 1.00 27.45 C ANISOU 2436 CD2 PHE B 283 4263 2899 3269 1474 795 709 C ATOM 2437 CE1 PHE B 283 18.065 27.829 0.423 1.00 33.99 C ANISOU 2437 CE1 PHE B 283 4867 3887 4162 1608 571 710 C ATOM 2438 CE2 PHE B 283 19.270 29.369 1.796 1.00 28.27 C ANISOU 2438 CE2 PHE B 283 4282 3039 3419 1510 779 719 C ATOM 2439 CZ PHE B 283 18.121 28.648 1.535 1.00 26.97 C ANISOU 2439 CZ PHE B 283 4003 2958 3288 1577 668 719 C ATOM 2440 N GLN B 284 23.922 26.787 -2.737 1.00 23.55 N ANISOU 2440 N GLN B 284 3889 2401 2660 1347 690 644 N ATOM 2441 CA AGLN B 284 24.733 26.624 -3.936 0.67 27.60 C ANISOU 2441 CA AGLN B 284 4485 2889 3112 1356 690 640 C ATOM 2442 CA BGLN B 284 24.714 26.637 -3.947 0.33 26.90 C ANISOU 2442 CA BGLN B 284 4397 2800 3022 1358 690 640 C ATOM 2443 C GLN B 284 24.377 25.303 -4.600 1.00 26.10 C ANISOU 2443 C GLN B 284 4212 2764 2941 1380 561 627 C ATOM 2444 O GLN B 284 24.251 25.222 -5.818 1.00 21.81 O ANISOU 2444 O GLN B 284 3730 2211 2344 1456 518 636 O ATOM 2445 CB AGLN B 284 26.228 26.661 -3.605 0.67 30.03 C ANISOU 2445 CB AGLN B 284 4825 3170 3413 1236 779 616 C ATOM 2446 CB BGLN B 284 26.212 26.732 -3.652 0.33 29.24 C ANISOU 2446 CB BGLN B 284 4733 3067 3309 1242 782 618 C ATOM 2447 CG AGLN B 284 26.805 28.062 -3.460 0.67 36.17 C ANISOU 2447 CG AGLN B 284 5735 3868 4139 1218 914 629 C ATOM 2448 CG BGLN B 284 27.090 26.626 -4.894 0.33 27.96 C ANISOU 2448 CG BGLN B 284 4662 2879 3081 1251 794 613 C ATOM 2449 CD AGLN B 284 28.317 28.064 -3.285 0.67 46.45 C ANISOU 2449 CD AGLN B 284 7066 5155 5429 1099 997 602 C ATOM 2450 CD BGLN B 284 26.807 27.718 -5.916 0.33 27.37 C ANISOU 2450 CD BGLN B 284 4740 2736 2923 1354 838 643 C ATOM 2451 OE1AGLN B 284 28.973 27.030 -3.427 0.67 48.37 O ANISOU 2451 OE1AGLN B 284 7240 5445 5693 1045 952 576 O ATOM 2452 OE1BGLN B 284 26.807 28.906 -5.591 0.33 27.94 O ANISOU 2452 OE1BGLN B 284 4903 2748 2964 1361 933 660 O ATOM 2453 NE2AGLN B 284 28.875 29.231 -2.976 0.67 49.16 N ANISOU 2453 NE2AGLN B 284 7512 5434 5734 1057 1119 607 N ATOM 2454 NE2BGLN B 284 26.571 27.316 -7.161 0.33 24.11 N ANISOU 2454 NE2BGLN B 284 4365 2328 2467 1435 769 650 N ATOM 2455 N GLU B 285 24.220 24.265 -3.781 1.00 19.71 N ANISOU 2455 N GLU B 285 3269 2016 2205 1311 501 605 N ATOM 2456 CA GLU B 285 23.864 22.944 -4.292 1.00 19.88 C ANISOU 2456 CA GLU B 285 3210 2098 2247 1321 379 590 C ATOM 2457 C GLU B 285 22.429 22.945 -4.827 1.00 17.48 C ANISOU 2457 C GLU B 285 2878 1827 1938 1432 290 608 C ATOM 2458 O GLU B 285 22.131 22.319 -5.842 1.00 17.49 O ANISOU 2458 O GLU B 285 2882 1852 1913 1484 203 606 O ATOM 2459 CB GLU B 285 24.027 21.874 -3.203 1.00 20.23 C ANISOU 2459 CB GLU B 285 3128 2194 2366 1217 344 562 C ATOM 2460 CG GLU B 285 25.446 21.741 -2.635 1.00 33.07 C ANISOU 2460 CG GLU B 285 4765 3802 3999 1109 419 539 C ATOM 2461 CD GLU B 285 26.457 21.148 -3.628 1.00 42.24 C ANISOU 2461 CD GLU B 285 5975 4959 5114 1098 406 524 C ATOM 2462 OE1 GLU B 285 26.068 20.751 -4.752 1.00 42.86 O ANISOU 2462 OE1 GLU B 285 6082 5046 5159 1169 333 531 O ATOM 2463 OE2 GLU B 285 27.653 21.084 -3.274 1.00 43.74 O ANISOU 2463 OE2 GLU B 285 6176 5141 5303 1018 469 505 O ATOM 2464 N HIS B 286 21.546 23.655 -4.135 1.00 17.51 N ANISOU 2464 N HIS B 286 2854 1834 1965 1469 313 625 N ATOM 2465 CA HIS B 286 20.160 23.793 -4.566 1.00 18.24 C ANISOU 2465 CA HIS B 286 2914 1965 2052 1581 237 643 C ATOM 2466 C HIS B 286 20.101 24.410 -5.965 1.00 24.13 C ANISOU 2466 C HIS B 286 3786 2672 2711 1695 231 664 C ATOM 2467 O HIS B 286 19.423 23.900 -6.859 1.00 19.47 O ANISOU 2467 O HIS B 286 3175 2121 2100 1767 130 664 O ATOM 2468 CB HIS B 286 19.393 24.655 -3.562 1.00 25.73 C ANISOU 2468 CB HIS B 286 3833 2913 3030 1607 287 659 C ATOM 2469 CG HIS B 286 17.929 24.776 -3.852 1.00 21.21 C ANISOU 2469 CG HIS B 286 3206 2395 2459 1720 210 675 C ATOM 2470 ND1 HIS B 286 17.129 25.715 -3.240 1.00 23.30 N ANISOU 2470 ND1 HIS B 286 3467 2657 2730 1783 254 696 N ATOM 2471 CD2 HIS B 286 17.123 24.076 -4.685 1.00 19.71 C ANISOU 2471 CD2 HIS B 286 2961 2266 2261 1783 92 670 C ATOM 2472 CE1 HIS B 286 15.889 25.589 -3.682 1.00 26.96 C ANISOU 2472 CE1 HIS B 286 3867 3184 3191 1883 166 704 C ATOM 2473 NE2 HIS B 286 15.858 24.603 -4.560 1.00 21.13 N ANISOU 2473 NE2 HIS B 286 3096 2487 2445 1882 65 687 N ATOM 2474 N LYS B 287 20.835 25.502 -6.146 1.00 21.82 N ANISOU 2474 N LYS B 287 3628 2298 2363 1707 341 679 N ATOM 2475 CA LYS B 287 20.907 26.187 -7.433 1.00 29.95 C ANISOU 2475 CA LYS B 287 4801 3277 3304 1810 354 700 C ATOM 2476 C LYS B 287 21.418 25.270 -8.549 1.00 29.36 C ANISOU 2476 C LYS B 287 4744 3212 3198 1805 286 685 C ATOM 2477 O LYS B 287 20.904 25.297 -9.667 1.00 32.23 O ANISOU 2477 O LYS B 287 5160 3578 3508 1909 224 698 O ATOM 2478 CB LYS B 287 21.783 27.441 -7.318 1.00 31.54 C ANISOU 2478 CB LYS B 287 5146 3384 3452 1793 498 714 C ATOM 2479 CG LYS B 287 21.783 28.331 -8.556 1.00 39.63 C ANISOU 2479 CG LYS B 287 6337 4342 4377 1905 527 739 C ATOM 2480 CD LYS B 287 22.558 29.619 -8.302 1.00 47.31 C ANISOU 2480 CD LYS B 287 7455 5221 5301 1879 676 752 C ATOM 2481 CE LYS B 287 22.467 30.575 -9.482 1.00 51.12 C ANISOU 2481 CE LYS B 287 8115 5630 5679 1998 711 779 C ATOM 2482 NZ LYS B 287 23.178 31.845 -9.187 1.00 51.16 N ANISOU 2482 NZ LYS B 287 8267 5539 5633 1965 860 790 N ATOM 2483 N ASN B 288 22.422 24.454 -8.241 1.00 26.06 N ANISOU 2483 N ASN B 288 4286 2804 2811 1690 297 659 N ATOM 2484 CA ASN B 288 22.986 23.526 -9.219 1.00 29.12 C ANISOU 2484 CA ASN B 288 4691 3201 3171 1679 238 644 C ATOM 2485 C ASN B 288 21.962 22.574 -9.832 1.00 36.06 C ANISOU 2485 C ASN B 288 5496 4146 4060 1740 94 639 C ATOM 2486 O ASN B 288 22.169 22.052 -10.929 1.00 39.66 O ANISOU 2486 O ASN B 288 5998 4599 4470 1773 39 635 O ATOM 2487 CB ASN B 288 24.123 22.710 -8.596 1.00 30.26 C ANISOU 2487 CB ASN B 288 4781 3359 3358 1548 265 614 C ATOM 2488 CG ASN B 288 25.431 23.476 -8.536 1.00 40.40 C ANISOU 2488 CG ASN B 288 6165 4579 4605 1491 395 612 C ATOM 2489 OD1 ASN B 288 25.456 24.710 -8.619 1.00 37.10 O ANISOU 2489 OD1 ASN B 288 5849 4103 4145 1529 482 634 O ATOM 2490 ND2 ASN B 288 26.531 22.744 -8.394 1.00 46.70 N ANISOU 2490 ND2 ASN B 288 6937 5389 5416 1399 411 586 N ATOM 2491 N CYS B 289 20.866 22.344 -9.118 1.00 31.35 N ANISOU 2491 N CYS B 289 4783 3608 3520 1749 36 638 N ATOM 2492 CA CYS B 289 19.838 21.416 -9.575 1.00 28.98 C ANISOU 2492 CA CYS B 289 4396 3380 3235 1791 -101 630 C ATOM 2493 C CYS B 289 19.003 21.978 -10.724 1.00 26.14 C ANISOU 2493 C CYS B 289 4104 3018 2808 1934 -152 652 C ATOM 2494 O CYS B 289 18.275 21.237 -11.387 1.00 30.90 O ANISOU 2494 O CYS B 289 4660 3675 3405 1976 -268 644 O ATOM 2495 CB CYS B 289 18.923 21.015 -8.413 1.00 28.34 C ANISOU 2495 CB CYS B 289 4164 3368 3237 1749 -141 620 C ATOM 2496 SG CYS B 289 19.731 20.029 -7.132 1.00 23.26 S ANISOU 2496 SG CYS B 289 3425 2741 2671 1585 -117 589 S ATOM 2497 N GLY B 290 19.104 23.286 -10.948 1.00 22.00 N ANISOU 2497 N GLY B 290 3697 2430 2231 2008 -65 679 N ATOM 2498 CA GLY B 290 18.352 23.946 -12.007 1.00 25.35 C ANISOU 2498 CA GLY B 290 4204 2844 2583 2155 -103 702 C ATOM 2499 C GLY B 290 16.862 23.655 -11.951 1.00 34.78 C ANISOU 2499 C GLY B 290 5280 4128 3805 2228 -215 702 C ATOM 2500 O GLY B 290 16.211 23.941 -10.947 1.00 39.93 O ANISOU 2500 O GLY B 290 5844 4816 4511 2220 -199 705 O ATOM 2501 N GLU B 291 16.323 23.074 -13.022 1.00 37.71 N ANISOU 2501 N GLU B 291 5648 4539 4141 2295 -328 697 N ATOM 2502 CA GLU B 291 14.890 22.773 -13.098 1.00 36.32 C ANISOU 2502 CA GLU B 291 5357 4458 3984 2366 -444 694 C ATOM 2503 C GLU B 291 14.595 21.288 -12.880 1.00 32.79 C ANISOU 2503 C GLU B 291 4767 4092 3599 2271 -551 660 C ATOM 2504 O GLU B 291 13.514 20.804 -13.209 1.00 38.53 O ANISOU 2504 O GLU B 291 5405 4902 4332 2317 -665 651 O ATOM 2505 CB GLU B 291 14.312 23.232 -14.440 1.00 38.63 C ANISOU 2505 CB GLU B 291 5743 4748 4189 2520 -505 711 C ATOM 2506 CG GLU B 291 14.680 24.657 -14.817 1.00 41.55 C ANISOU 2506 CG GLU B 291 6283 5024 4482 2617 -399 744 C ATOM 2507 CD GLU B 291 14.109 25.678 -13.855 1.00 50.79 C ANISOU 2507 CD GLU B 291 7429 6195 5674 2660 -329 763 C ATOM 2508 OE1 GLU B 291 12.877 25.673 -13.641 1.00 53.22 O ANISOU 2508 OE1 GLU B 291 7629 6588 6005 2731 -403 763 O ATOM 2509 OE2 GLU B 291 14.891 26.491 -13.317 1.00 56.63 O ANISOU 2509 OE2 GLU B 291 8258 6853 6407 2623 -199 777 O ATOM 2510 N MET B 292 15.567 20.576 -12.323 1.00 27.96 N ANISOU 2510 N MET B 292 4136 3458 3030 2139 -513 641 N ATOM 2511 CA MET B 292 15.417 19.170 -11.982 1.00 29.93 C ANISOU 2511 CA MET B 292 4264 3770 3336 2036 -598 609 C ATOM 2512 C MET B 292 14.063 18.893 -11.323 1.00 36.04 C ANISOU 2512 C MET B 292 4883 4642 4169 2040 -671 600 C ATOM 2513 O MET B 292 13.612 19.648 -10.457 1.00 30.86 O ANISOU 2513 O MET B 292 4183 3997 3546 2057 -615 612 O ATOM 2514 CB MET B 292 16.558 18.765 -11.044 1.00 27.91 C ANISOU 2514 CB MET B 292 3999 3477 3128 1901 -518 595 C ATOM 2515 CG MET B 292 16.619 17.296 -10.680 1.00 21.64 C ANISOU 2515 CG MET B 292 3107 2731 2385 1790 -591 562 C ATOM 2516 SD MET B 292 17.941 17.035 -9.475 1.00 27.64 S ANISOU 2516 SD MET B 292 3860 3446 3195 1651 -486 549 S ATOM 2517 CE MET B 292 19.370 17.442 -10.475 1.00 26.83 C ANISOU 2517 CE MET B 292 3924 3256 3015 1675 -414 559 C ATOM 2518 N SER B 293 13.416 17.809 -11.733 1.00 37.15 N ANISOU 2518 N SER B 293 4942 4854 4319 2020 -794 576 N ATOM 2519 CA SER B 293 12.118 17.447 -11.173 1.00 32.79 C ANISOU 2519 CA SER B 293 4234 4403 3820 2013 -869 562 C ATOM 2520 C SER B 293 12.242 16.864 -9.767 1.00 26.06 C ANISOU 2520 C SER B 293 3275 3570 3055 1878 -832 543 C ATOM 2521 O SER B 293 13.314 16.414 -9.357 1.00 24.15 O ANISOU 2521 O SER B 293 3070 3276 2831 1781 -780 534 O ATOM 2522 CB SER B 293 11.413 16.439 -12.083 1.00 35.67 C ANISOU 2522 CB SER B 293 4550 4837 4163 2022 -1012 539 C ATOM 2523 OG SER B 293 12.126 15.213 -12.124 1.00 31.35 O ANISOU 2523 OG SER B 293 4008 4273 3629 1907 -1042 514 O ATOM 2524 N GLU B 294 11.130 16.865 -9.040 1.00 25.11 N ANISOU 2524 N GLU B 294 3023 3531 2987 1875 -862 537 N ATOM 2525 CA GLU B 294 11.070 16.253 -7.723 1.00 32.84 C ANISOU 2525 CA GLU B 294 3892 4537 4048 1751 -838 517 C ATOM 2526 C GLU B 294 11.580 14.816 -7.788 1.00 30.78 C ANISOU 2526 C GLU B 294 3617 4277 3802 1631 -895 486 C ATOM 2527 O GLU B 294 12.367 14.378 -6.941 1.00 28.32 O ANISOU 2527 O GLU B 294 3305 3927 3529 1525 -839 475 O ATOM 2528 CB GLU B 294 9.631 16.292 -7.192 1.00 35.06 C ANISOU 2528 CB GLU B 294 4025 4922 4373 1772 -887 510 C ATOM 2529 CG GLU B 294 9.419 15.592 -5.858 1.00 36.55 C ANISOU 2529 CG GLU B 294 4096 5147 4646 1642 -871 488 C ATOM 2530 CD GLU B 294 8.073 15.927 -5.240 1.00 45.90 C ANISOU 2530 CD GLU B 294 5143 6425 5872 1677 -889 487 C ATOM 2531 OE1 GLU B 294 7.401 16.843 -5.754 1.00 47.96 O ANISOU 2531 OE1 GLU B 294 5410 6716 6098 1810 -900 508 O ATOM 2532 OE2 GLU B 294 7.688 15.282 -4.240 1.00 51.63 O ANISOU 2532 OE2 GLU B 294 5759 7195 6664 1574 -891 466 O ATOM 2533 N ILE B 295 11.134 14.096 -8.810 1.00 28.24 N ANISOU 2533 N ILE B 295 3289 3996 3443 1652 -1007 471 N ATOM 2534 CA ILE B 295 11.509 12.704 -9.001 1.00 26.16 C ANISOU 2534 CA ILE B 295 3022 3734 3183 1549 -1072 441 C ATOM 2535 C ILE B 295 13.009 12.542 -9.254 1.00 25.91 C ANISOU 2535 C ILE B 295 3118 3606 3119 1516 -1011 445 C ATOM 2536 O ILE B 295 13.660 11.711 -8.622 1.00 24.27 O ANISOU 2536 O ILE B 295 2901 3377 2942 1408 -993 426 O ATOM 2537 CB ILE B 295 10.720 12.075 -10.171 1.00 32.45 C ANISOU 2537 CB ILE B 295 3802 4591 3935 1589 -1206 425 C ATOM 2538 CG1 ILE B 295 9.248 11.919 -9.795 1.00 33.17 C ANISOU 2538 CG1 ILE B 295 3740 4795 4068 1587 -1277 409 C ATOM 2539 CG2 ILE B 295 11.307 10.729 -10.551 1.00 30.74 C ANISOU 2539 CG2 ILE B 295 3623 4353 3704 1497 -1263 398 C ATOM 2540 CD1 ILE B 295 9.006 10.844 -8.781 1.00 36.80 C ANISOU 2540 CD1 ILE B 295 4095 5293 4594 1442 -1294 378 C ATOM 2541 N GLU B 296 13.565 13.327 -10.173 1.00 31.45 N ANISOU 2541 N GLU B 296 3940 4252 3757 1611 -978 469 N ATOM 2542 CA GLU B 296 14.983 13.175 -10.495 1.00 35.64 C ANISOU 2542 CA GLU B 296 4589 4700 4254 1582 -920 471 C ATOM 2543 C GLU B 296 15.860 13.518 -9.290 1.00 24.74 C ANISOU 2543 C GLU B 296 3208 3274 2920 1509 -802 475 C ATOM 2544 O GLU B 296 16.908 12.906 -9.076 1.00 27.40 O ANISOU 2544 O GLU B 296 3581 3571 3258 1434 -771 462 O ATOM 2545 CB GLU B 296 15.388 14.021 -11.709 1.00 42.37 C ANISOU 2545 CB GLU B 296 5575 5499 5026 1696 -899 496 C ATOM 2546 CG GLU B 296 16.685 13.531 -12.373 1.00 49.53 C ANISOU 2546 CG GLU B 296 6594 6339 5886 1669 -878 491 C ATOM 2547 CD GLU B 296 17.391 14.608 -13.183 0.50 53.97 C ANISOU 2547 CD GLU B 296 7296 6830 6381 1758 -803 519 C ATOM 2548 OE1 GLU B 296 16.767 15.651 -13.471 0.50 53.68 O ANISOU 2548 OE1 GLU B 296 7281 6794 6319 1858 -790 542 O ATOM 2549 OE2 GLU B 296 18.575 14.410 -13.531 0.50 54.11 O ANISOU 2549 OE2 GLU B 296 7402 6789 6367 1730 -755 517 O ATOM 2550 N ALA B 297 15.425 14.505 -8.515 1.00 21.01 N ANISOU 2550 N ALA B 297 2694 2808 2480 1536 -738 492 N ATOM 2551 CA ALA B 297 16.143 14.903 -7.312 1.00 20.35 C ANISOU 2551 CA ALA B 297 2605 2687 2441 1468 -628 495 C ATOM 2552 C ALA B 297 16.153 13.747 -6.320 1.00 18.18 C ANISOU 2552 C ALA B 297 2236 2443 2228 1344 -654 466 C ATOM 2553 O ALA B 297 17.177 13.473 -5.691 1.00 19.22 O ANISOU 2553 O ALA B 297 2391 2534 2377 1266 -593 457 O ATOM 2554 CB ALA B 297 15.502 16.149 -6.689 1.00 19.11 C ANISOU 2554 CB ALA B 297 2421 2535 2304 1527 -564 519 C ATOM 2555 N LYS B 298 15.016 13.060 -6.203 1.00 18.63 N ANISOU 2555 N LYS B 298 2189 2574 2315 1325 -745 449 N ATOM 2556 CA LYS B 298 14.905 11.908 -5.302 1.00 19.67 C ANISOU 2556 CA LYS B 298 2237 2736 2502 1206 -775 420 C ATOM 2557 C LYS B 298 15.819 10.765 -5.736 1.00 17.72 C ANISOU 2557 C LYS B 298 2050 2457 2227 1145 -810 399 C ATOM 2558 O LYS B 298 16.492 10.145 -4.913 1.00 19.00 O ANISOU 2558 O LYS B 298 2204 2597 2418 1054 -777 384 O ATOM 2559 CB LYS B 298 13.457 11.430 -5.207 1.00 22.00 C ANISOU 2559 CB LYS B 298 2412 3119 2827 1198 -866 405 C ATOM 2560 CG LYS B 298 12.606 12.219 -4.231 1.00 19.56 C ANISOU 2560 CG LYS B 298 2011 2851 2571 1213 -820 416 C ATOM 2561 CD LYS B 298 11.133 11.850 -4.345 1.00 24.91 C ANISOU 2561 CD LYS B 298 2569 3627 3268 1222 -914 402 C ATOM 2562 CE LYS B 298 10.335 12.475 -3.203 1.00 27.80 C ANISOU 2562 CE LYS B 298 2832 4036 3694 1220 -863 409 C ATOM 2563 NZ LYS B 298 8.865 12.337 -3.359 1.00 28.30 N ANISOU 2563 NZ LYS B 298 2773 4205 3773 1249 -945 398 N ATOM 2564 N VAL B 299 15.853 10.494 -7.036 1.00 21.52 N ANISOU 2564 N VAL B 299 2595 2934 2647 1200 -877 400 N ATOM 2565 CA VAL B 299 16.751 9.476 -7.560 1.00 26.10 C ANISOU 2565 CA VAL B 299 3246 3480 3192 1157 -907 383 C ATOM 2566 C VAL B 299 18.206 9.821 -7.228 1.00 16.98 C ANISOU 2566 C VAL B 299 2169 2256 2028 1138 -802 390 C ATOM 2567 O VAL B 299 18.977 8.960 -6.796 1.00 16.39 O ANISOU 2567 O VAL B 299 2104 2161 1960 1062 -793 371 O ATOM 2568 CB VAL B 299 16.591 9.305 -9.084 1.00 26.15 C ANISOU 2568 CB VAL B 299 3323 3486 3127 1234 -986 386 C ATOM 2569 CG1 VAL B 299 17.704 8.443 -9.636 1.00 25.06 C ANISOU 2569 CG1 VAL B 299 3278 3300 2945 1204 -995 374 C ATOM 2570 CG2 VAL B 299 15.225 8.707 -9.415 1.00 25.57 C ANISOU 2570 CG2 VAL B 299 3168 3487 3059 1233 -1104 370 C ATOM 2571 N LYS B 300 18.577 11.082 -7.431 1.00 22.07 N ANISOU 2571 N LYS B 300 2869 2865 2652 1208 -722 417 N ATOM 2572 CA LYS B 300 19.957 11.509 -7.195 1.00 16.38 C ANISOU 2572 CA LYS B 300 2222 2084 1918 1189 -619 423 C ATOM 2573 C LYS B 300 20.340 11.479 -5.708 1.00 18.29 C ANISOU 2573 C LYS B 300 2404 2324 2222 1100 -550 413 C ATOM 2574 O LYS B 300 21.479 11.144 -5.361 1.00 15.06 O ANISOU 2574 O LYS B 300 2026 1885 1810 1047 -502 402 O ATOM 2575 CB LYS B 300 20.220 12.876 -7.833 1.00 22.04 C ANISOU 2575 CB LYS B 300 3022 2760 2590 1281 -550 452 C ATOM 2576 CG LYS B 300 20.504 12.758 -9.331 1.00 21.74 C ANISOU 2576 CG LYS B 300 3085 2699 2477 1352 -593 458 C ATOM 2577 CD LYS B 300 20.823 14.080 -9.985 1.00 32.11 C ANISOU 2577 CD LYS B 300 4497 3964 3740 1439 -519 487 C ATOM 2578 CE LYS B 300 21.622 13.844 -11.257 1.00 41.67 C ANISOU 2578 CE LYS B 300 5821 5136 4877 1478 -529 488 C ATOM 2579 NZ LYS B 300 21.177 14.721 -12.372 1.00 42.70 N ANISOU 2579 NZ LYS B 300 6035 5245 4945 1594 -538 513 N ATOM 2580 N TYR B 301 19.382 11.806 -4.842 1.00 15.82 N ANISOU 2580 N TYR B 301 2001 2046 1962 1087 -547 416 N ATOM 2581 CA TYR B 301 19.603 11.754 -3.403 1.00 20.73 C ANISOU 2581 CA TYR B 301 2564 2669 2645 1003 -489 407 C ATOM 2582 C TYR B 301 19.895 10.309 -3.009 1.00 16.66 C ANISOU 2582 C TYR B 301 2019 2165 2145 914 -540 376 C ATOM 2583 O TYR B 301 20.896 10.027 -2.345 1.00 14.14 O ANISOU 2583 O TYR B 301 1717 1819 1836 854 -489 364 O ATOM 2584 CB TYR B 301 18.385 12.297 -2.642 1.00 17.41 C ANISOU 2584 CB TYR B 301 2052 2288 2275 1012 -486 416 C ATOM 2585 CG TYR B 301 18.612 12.551 -1.160 1.00 16.16 C ANISOU 2585 CG TYR B 301 1846 2121 2174 941 -407 412 C ATOM 2586 CD1 TYR B 301 18.706 13.850 -0.656 1.00 21.53 C ANISOU 2586 CD1 TYR B 301 2544 2774 2863 974 -312 435 C ATOM 2587 CD2 TYR B 301 18.723 11.494 -0.262 1.00 14.53 C ANISOU 2587 CD2 TYR B 301 1585 1928 2007 843 -427 386 C ATOM 2588 CE1 TYR B 301 18.908 14.087 0.705 1.00 14.50 C ANISOU 2588 CE1 TYR B 301 1614 1873 2022 908 -242 431 C ATOM 2589 CE2 TYR B 301 18.920 11.717 1.085 1.00 14.05 C ANISOU 2589 CE2 TYR B 301 1485 1857 1995 781 -358 383 C ATOM 2590 CZ TYR B 301 19.016 13.013 1.570 1.00 14.61 C ANISOU 2590 CZ TYR B 301 1571 1904 2076 812 -266 405 C ATOM 2591 OH TYR B 301 19.217 13.222 2.925 1.00 14.12 O ANISOU 2591 OH TYR B 301 1474 1830 2061 748 -198 401 O ATOM 2592 N VAL B 302 19.033 9.394 -3.444 1.00 15.22 N ANISOU 2592 N VAL B 302 1799 2024 1961 905 -643 362 N ATOM 2593 CA VAL B 302 19.231 7.980 -3.138 1.00 14.93 C ANISOU 2593 CA VAL B 302 1748 1993 1931 822 -697 332 C ATOM 2594 C VAL B 302 20.519 7.429 -3.751 1.00 19.18 C ANISOU 2594 C VAL B 302 2381 2488 2417 822 -691 324 C ATOM 2595 O VAL B 302 21.245 6.676 -3.098 1.00 16.26 O ANISOU 2595 O VAL B 302 2018 2104 2057 756 -675 305 O ATOM 2596 CB VAL B 302 18.031 7.118 -3.564 1.00 15.57 C ANISOU 2596 CB VAL B 302 1776 2126 2013 808 -809 317 C ATOM 2597 CG1 VAL B 302 18.354 5.632 -3.408 1.00 15.32 C ANISOU 2597 CG1 VAL B 302 1760 2088 1973 726 -863 287 C ATOM 2598 CG2 VAL B 302 16.796 7.490 -2.752 1.00 15.91 C ANISOU 2598 CG2 VAL B 302 1709 2222 2116 790 -812 318 C ATOM 2599 N LYS B 303 20.818 7.805 -4.992 1.00 16.99 N ANISOU 2599 N LYS B 303 2179 2193 2083 899 -701 338 N ATOM 2600 CA LYS B 303 22.039 7.303 -5.626 1.00 20.92 C ANISOU 2600 CA LYS B 303 2767 2653 2528 905 -692 331 C ATOM 2601 C LYS B 303 23.275 7.841 -4.917 1.00 19.33 C ANISOU 2601 C LYS B 303 2588 2420 2337 881 -583 333 C ATOM 2602 O LYS B 303 24.257 7.121 -4.722 1.00 22.19 O ANISOU 2602 O LYS B 303 2980 2767 2684 843 -571 316 O ATOM 2603 CB LYS B 303 22.088 7.629 -7.124 1.00 22.45 C ANISOU 2603 CB LYS B 303 3042 2831 2656 994 -722 346 C ATOM 2604 CG LYS B 303 21.206 6.733 -7.999 1.00 28.64 C ANISOU 2604 CG LYS B 303 3827 3642 3412 1008 -843 335 C ATOM 2605 CD LYS B 303 21.555 6.888 -9.479 1.00 35.24 C ANISOU 2605 CD LYS B 303 4764 4452 4173 1091 -867 347 C ATOM 2606 CE LYS B 303 20.467 6.329 -10.384 0.50 34.81 C ANISOU 2606 CE LYS B 303 4705 4431 4092 1119 -986 341 C ATOM 2607 NZ LYS B 303 20.790 6.539 -11.826 0.50 33.58 N ANISOU 2607 NZ LYS B 303 4653 4245 3860 1205 -1008 354 N ATOM 2608 N LEU B 304 23.222 9.106 -4.516 1.00 15.51 N ANISOU 2608 N LEU B 304 2090 1927 1874 904 -505 353 N ATOM 2609 CA LEU B 304 24.340 9.695 -3.792 1.00 13.37 C ANISOU 2609 CA LEU B 304 1837 1630 1614 873 -400 354 C ATOM 2610 C LEU B 304 24.552 8.952 -2.469 1.00 12.81 C ANISOU 2610 C LEU B 304 1705 1573 1592 784 -393 331 C ATOM 2611 O LEU B 304 25.679 8.598 -2.119 1.00 12.35 O ANISOU 2611 O LEU B 304 1669 1502 1523 748 -355 316 O ATOM 2612 CB LEU B 304 24.121 11.197 -3.563 1.00 13.53 C ANISOU 2612 CB LEU B 304 1860 1636 1647 910 -319 379 C ATOM 2613 CG LEU B 304 25.274 11.929 -2.864 1.00 13.56 C ANISOU 2613 CG LEU B 304 1886 1610 1656 874 -206 379 C ATOM 2614 CD1 LEU B 304 26.528 11.819 -3.697 1.00 20.85 C ANISOU 2614 CD1 LEU B 304 2890 2509 2521 890 -177 374 C ATOM 2615 CD2 LEU B 304 24.924 13.389 -2.612 1.00 13.50 C ANISOU 2615 CD2 LEU B 304 1888 1582 1658 908 -130 404 C ATOM 2616 N ALA B 305 23.464 8.681 -1.754 1.00 12.91 N ANISOU 2616 N ALA B 305 1639 1613 1653 750 -433 327 N ATOM 2617 CA ALA B 305 23.565 7.948 -0.494 1.00 13.87 C ANISOU 2617 CA ALA B 305 1708 1744 1818 666 -429 305 C ATOM 2618 C ALA B 305 24.184 6.558 -0.672 1.00 13.57 C ANISOU 2618 C ALA B 305 1704 1702 1751 631 -482 280 C ATOM 2619 O ALA B 305 25.056 6.148 0.100 1.00 13.29 O ANISOU 2619 O ALA B 305 1672 1656 1721 585 -447 264 O ATOM 2620 CB ALA B 305 22.198 7.850 0.185 1.00 12.70 C ANISOU 2620 CB ALA B 305 1473 1628 1722 636 -466 305 C ATOM 2621 N ARG B 306 23.726 5.828 -1.682 1.00 15.62 N ANISOU 2621 N ARG B 306 1990 1970 1975 657 -569 276 N ATOM 2622 CA ARG B 306 24.242 4.484 -1.942 1.00 23.16 C ANISOU 2622 CA ARG B 306 2990 2916 2894 631 -623 252 C ATOM 2623 C ARG B 306 25.704 4.487 -2.393 1.00 23.63 C ANISOU 2623 C ARG B 306 3124 2951 2905 661 -577 250 C ATOM 2624 O ARG B 306 26.414 3.501 -2.195 1.00 20.54 O ANISOU 2624 O ARG B 306 2762 2550 2491 634 -592 230 O ATOM 2625 CB ARG B 306 23.373 3.756 -2.974 1.00 24.05 C ANISOU 2625 CB ARG B 306 3120 3041 2975 652 -727 249 C ATOM 2626 CG ARG B 306 22.000 3.384 -2.443 1.00 23.84 C ANISOU 2626 CG ARG B 306 3016 3050 2993 602 -784 240 C ATOM 2627 CD ARG B 306 21.107 2.774 -3.508 1.00 20.48 C ANISOU 2627 CD ARG B 306 2603 2645 2536 620 -887 235 C ATOM 2628 NE ARG B 306 19.871 2.260 -2.924 1.00 33.39 N ANISOU 2628 NE ARG B 306 4158 4318 4212 556 -941 221 N ATOM 2629 CZ ARG B 306 18.876 1.716 -3.620 1.00 43.40 C ANISOU 2629 CZ ARG B 306 5411 5617 5463 551 -1034 211 C ATOM 2630 NH1 ARG B 306 18.966 1.606 -4.940 1.00 44.68 N ANISOU 2630 NH1 ARG B 306 5638 5771 5566 612 -1086 216 N ATOM 2631 NH2 ARG B 306 17.790 1.280 -2.992 1.00 44.91 N ANISOU 2631 NH2 ARG B 306 5522 5847 5695 483 -1073 196 N ATOM 2632 N SER B 307 26.153 5.592 -2.984 1.00 17.79 N ANISOU 2632 N SER B 307 2415 2199 2146 716 -518 270 N ATOM 2633 CA SER B 307 27.524 5.670 -3.499 1.00 19.29 C ANISOU 2633 CA SER B 307 2672 2370 2288 744 -469 268 C ATOM 2634 C SER B 307 28.589 5.750 -2.397 1.00 22.97 C ANISOU 2634 C SER B 307 3115 2837 2773 696 -393 254 C ATOM 2635 O SER B 307 29.763 5.466 -2.638 1.00 21.27 O ANISOU 2635 O SER B 307 2941 2619 2520 706 -365 242 O ATOM 2636 CB SER B 307 27.677 6.862 -4.443 1.00 20.28 C ANISOU 2636 CB SER B 307 2843 2480 2384 811 -422 293 C ATOM 2637 OG SER B 307 27.801 8.073 -3.714 1.00 22.05 O ANISOU 2637 OG SER B 307 3037 2700 2643 798 -333 305 O ATOM 2638 N LEU B 308 28.190 6.142 -1.192 1.00 21.60 N ANISOU 2638 N LEU B 308 2876 2673 2658 647 -359 253 N ATOM 2639 CA LEU B 308 29.144 6.278 -0.089 1.00 17.86 C ANISOU 2639 CA LEU B 308 2379 2203 2205 600 -289 239 C ATOM 2640 C LEU B 308 29.492 4.929 0.542 1.00 14.52 C ANISOU 2640 C LEU B 308 1951 1787 1779 558 -332 211 C ATOM 2641 O LEU B 308 28.624 4.082 0.724 1.00 14.60 O ANISOU 2641 O LEU B 308 1945 1799 1802 534 -403 204 O ATOM 2642 CB LEU B 308 28.593 7.228 0.972 1.00 15.31 C ANISOU 2642 CB LEU B 308 1996 1881 1941 565 -235 250 C ATOM 2643 CG LEU B 308 28.137 8.608 0.481 1.00 23.05 C ANISOU 2643 CG LEU B 308 2985 2849 2924 608 -189 278 C ATOM 2644 CD1 LEU B 308 27.440 9.376 1.595 1.00 18.08 C ANISOU 2644 CD1 LEU B 308 2296 2220 2353 575 -146 288 C ATOM 2645 CD2 LEU B 308 29.311 9.411 -0.071 1.00 23.61 C ANISOU 2645 CD2 LEU B 308 3112 2905 2954 635 -111 283 C ATOM 2646 N ARG B 309 30.767 4.739 0.877 1.00 12.72 N ANISOU 2646 N ARG B 309 1737 1566 1529 549 -288 195 N ATOM 2647 CA ARG B 309 31.233 3.513 1.541 1.00 19.63 C ANISOU 2647 CA ARG B 309 2616 2447 2395 519 -321 168 C ATOM 2648 C ARG B 309 30.567 3.269 2.901 1.00 14.49 C ANISOU 2648 C ARG B 309 1909 1796 1798 454 -328 160 C ATOM 2649 O ARG B 309 30.557 2.150 3.416 1.00 18.39 O ANISOU 2649 O ARG B 309 2414 2288 2287 426 -372 140 O ATOM 2650 CB ARG B 309 32.753 3.563 1.737 1.00 13.92 C ANISOU 2650 CB ARG B 309 1906 1742 1642 527 -263 152 C ATOM 2651 CG ARG B 309 33.546 3.317 0.476 1.00 27.41 C ANISOU 2651 CG ARG B 309 3676 3453 3286 587 -269 151 C ATOM 2652 CD ARG B 309 34.795 2.517 0.813 1.00 40.59 C ANISOU 2652 CD ARG B 309 5359 5144 4918 593 -261 124 C ATOM 2653 NE ARG B 309 35.946 3.367 1.066 1.00 39.42 N ANISOU 2653 NE ARG B 309 5186 5025 4767 589 -172 117 N ATOM 2654 CZ ARG B 309 36.992 3.009 1.803 1.00 33.45 C ANISOU 2654 CZ ARG B 309 4409 4302 3999 577 -145 92 C ATOM 2655 NH1 ARG B 309 37.033 1.817 2.390 1.00 34.53 N ANISOU 2655 NH1 ARG B 309 4555 4440 4125 573 -199 73 N ATOM 2656 NH2 ARG B 309 37.993 3.856 1.960 1.00 30.05 N ANISOU 2656 NH2 ARG B 309 3950 3902 3564 568 -64 85 N ATOM 2657 N THR B 310 30.036 4.334 3.478 1.00 12.89 N ANISOU 2657 N THR B 310 1658 1595 1646 431 -279 175 N ATOM 2658 CA THR B 310 29.385 4.288 4.777 1.00 12.40 C ANISOU 2658 CA THR B 310 1541 1531 1638 372 -272 170 C ATOM 2659 C THR B 310 27.942 3.821 4.681 1.00 10.27 C ANISOU 2659 C THR B 310 1248 1259 1393 356 -341 176 C ATOM 2660 O THR B 310 27.299 3.570 5.699 1.00 12.97 O ANISOU 2660 O THR B 310 1550 1602 1777 303 -346 169 O ATOM 2661 CB THR B 310 29.361 5.672 5.374 1.00 10.62 C ANISOU 2661 CB THR B 310 1276 1306 1452 359 -189 185 C ATOM 2662 OG1 THR B 310 28.990 6.601 4.342 1.00 10.78 O ANISOU 2662 OG1 THR B 310 1312 1321 1462 410 -176 210 O ATOM 2663 CG2 THR B 310 30.737 6.031 5.921 1.00 9.06 C ANISOU 2663 CG2 THR B 310 1084 1117 1242 345 -118 171 C ATOM 2664 N TYR B 311 27.419 3.729 3.464 1.00 10.22 N ANISOU 2664 N TYR B 311 1268 1254 1360 400 -393 187 N ATOM 2665 CA TYR B 311 26.044 3.273 3.286 1.00 11.62 C ANISOU 2665 CA TYR B 311 1419 1438 1557 383 -464 189 C ATOM 2666 C TYR B 311 25.860 1.849 3.808 1.00 11.61 C ANISOU 2666 C TYR B 311 1430 1432 1550 329 -523 164 C ATOM 2667 O TYR B 311 26.698 0.982 3.576 1.00 14.87 O ANISOU 2667 O TYR B 311 1901 1832 1916 337 -544 148 O ATOM 2668 CB TYR B 311 25.632 3.353 1.816 1.00 11.09 C ANISOU 2668 CB TYR B 311 1386 1375 1453 444 -516 203 C ATOM 2669 CG TYR B 311 24.192 2.959 1.583 1.00 11.91 C ANISOU 2669 CG TYR B 311 1452 1497 1575 427 -591 204 C ATOM 2670 CD1 TYR B 311 23.164 3.877 1.752 1.00 12.94 C ANISOU 2670 CD1 TYR B 311 1519 1649 1750 435 -577 221 C ATOM 2671 CD2 TYR B 311 23.861 1.661 1.208 1.00 12.82 C ANISOU 2671 CD2 TYR B 311 1598 1610 1661 403 -675 185 C ATOM 2672 CE1 TYR B 311 21.843 3.512 1.546 1.00 16.84 C ANISOU 2672 CE1 TYR B 311 1968 2171 2261 419 -647 219 C ATOM 2673 CE2 TYR B 311 22.548 1.285 1.002 1.00 13.49 C ANISOU 2673 CE2 TYR B 311 1645 1719 1763 377 -744 181 C ATOM 2674 CZ TYR B 311 21.545 2.212 1.169 1.00 20.20 C ANISOU 2674 CZ TYR B 311 2419 2599 2659 386 -731 198 C ATOM 2675 OH TYR B 311 20.243 1.836 0.964 1.00 22.09 O ANISOU 2675 OH TYR B 311 2610 2872 2913 361 -801 192 O ATOM 2676 N GLY B 312 24.762 1.611 4.520 1.00 19.54 N ANISOU 2676 N GLY B 312 2381 2444 2598 275 -545 160 N ATOM 2677 CA GLY B 312 24.434 0.273 4.992 1.00 14.93 C ANISOU 2677 CA GLY B 312 1815 1851 2007 215 -600 135 C ATOM 2678 C GLY B 312 25.250 -0.197 6.186 1.00 19.47 C ANISOU 2678 C GLY B 312 2406 2407 2585 175 -562 117 C ATOM 2679 O GLY B 312 25.159 -1.350 6.594 1.00 21.73 O ANISOU 2679 O GLY B 312 2726 2677 2854 131 -602 96 O ATOM 2680 N VAL B 313 26.037 0.700 6.763 1.00 16.11 N ANISOU 2680 N VAL B 313 1961 1983 2177 189 -485 124 N ATOM 2681 CA VAL B 313 26.894 0.354 7.891 1.00 12.17 C ANISOU 2681 CA VAL B 313 1474 1471 1677 158 -447 106 C ATOM 2682 C VAL B 313 26.326 0.804 9.239 1.00 15.10 C ANISOU 2682 C VAL B 313 1786 1843 2110 100 -403 107 C ATOM 2683 O VAL B 313 25.820 1.921 9.372 1.00 10.37 O ANISOU 2683 O VAL B 313 1132 1255 1554 104 -360 127 O ATOM 2684 CB VAL B 313 28.276 0.986 7.704 1.00 15.35 C ANISOU 2684 CB VAL B 313 1896 1882 2054 205 -390 108 C ATOM 2685 CG1 VAL B 313 29.209 0.628 8.874 1.00 8.82 C ANISOU 2685 CG1 VAL B 313 1078 1051 1224 178 -356 87 C ATOM 2686 CG2 VAL B 313 28.850 0.556 6.357 1.00 9.41 C ANISOU 2686 CG2 VAL B 313 1204 1130 1240 265 -429 108 C ATOM 2687 N SER B 314 26.397 -0.075 10.235 1.00 9.57 N ANISOU 2687 N SER B 314 1102 1124 1409 50 -411 86 N ATOM 2688 CA SER B 314 25.984 0.285 11.591 1.00 15.21 C ANISOU 2688 CA SER B 314 1769 1834 2176 -6 -365 85 C ATOM 2689 C SER B 314 27.168 0.849 12.384 1.00 12.20 C ANISOU 2689 C SER B 314 1390 1452 1795 3 -297 80 C ATOM 2690 O SER B 314 28.155 0.148 12.624 1.00 14.13 O ANISOU 2690 O SER B 314 1683 1689 1998 11 -304 60 O ATOM 2691 CB SER B 314 25.395 -0.930 12.318 1.00 14.22 C ANISOU 2691 CB SER B 314 1665 1686 2050 -70 -405 64 C ATOM 2692 OG SER B 314 24.190 -1.350 11.702 1.00 16.88 O ANISOU 2692 OG SER B 314 1987 2031 2394 -92 -462 66 O ATOM 2693 N PHE B 315 27.059 2.112 12.790 1.00 11.17 N ANISOU 2693 N PHE B 315 1207 1329 1706 1 -231 97 N ATOM 2694 CA PHE B 315 28.152 2.795 13.462 1.00 8.03 C ANISOU 2694 CA PHE B 315 808 935 1309 5 -164 93 C ATOM 2695 C PHE B 315 27.931 2.959 14.952 1.00 15.72 C ANISOU 2695 C PHE B 315 1755 1895 2322 -52 -122 86 C ATOM 2696 O PHE B 315 26.817 3.222 15.412 1.00 10.98 O ANISOU 2696 O PHE B 315 1117 1288 1768 -85 -114 97 O ATOM 2697 CB PHE B 315 28.444 4.153 12.809 1.00 14.87 C ANISOU 2697 CB PHE B 315 1655 1815 2181 45 -112 115 C ATOM 2698 CG PHE B 315 29.226 4.045 11.522 1.00 10.12 C ANISOU 2698 CG PHE B 315 1092 1226 1527 102 -133 115 C ATOM 2699 CD1 PHE B 315 28.594 4.177 10.297 1.00 10.76 C ANISOU 2699 CD1 PHE B 315 1179 1310 1598 142 -168 133 C ATOM 2700 CD2 PHE B 315 30.582 3.781 11.546 1.00 8.52 C ANISOU 2700 CD2 PHE B 315 919 1036 1283 119 -118 96 C ATOM 2701 CE1 PHE B 315 29.307 4.063 9.106 1.00 14.13 C ANISOU 2701 CE1 PHE B 315 1649 1745 1974 196 -186 133 C ATOM 2702 CE2 PHE B 315 31.309 3.651 10.361 1.00 11.99 C ANISOU 2702 CE2 PHE B 315 1395 1489 1674 173 -133 96 C ATOM 2703 CZ PHE B 315 30.670 3.801 9.145 1.00 17.38 C ANISOU 2703 CZ PHE B 315 2090 2168 2347 210 -166 115 C ATOM 2704 N PHE B 316 29.021 2.791 15.694 1.00 11.12 N ANISOU 2704 N PHE B 316 1194 1312 1719 -59 -97 67 N ATOM 2705 CA PHE B 316 29.045 3.009 17.129 1.00 11.31 C ANISOU 2705 CA PHE B 316 1202 1322 1772 -108 -52 59 C ATOM 2706 C PHE B 316 30.084 4.053 17.441 1.00 13.16 C ANISOU 2706 C PHE B 316 1423 1573 2006 -98 15 58 C ATOM 2707 O PHE B 316 31.187 4.034 16.882 1.00 9.92 O ANISOU 2707 O PHE B 316 1031 1185 1553 -62 15 48 O ATOM 2708 CB PHE B 316 29.387 1.717 17.865 1.00 8.78 C ANISOU 2708 CB PHE B 316 927 986 1423 -130 -89 31 C ATOM 2709 CG PHE B 316 28.365 0.627 17.676 1.00 10.12 C ANISOU 2709 CG PHE B 316 1120 1135 1591 -154 -151 28 C ATOM 2710 CD1 PHE B 316 28.392 -0.181 16.555 1.00 11.22 C ANISOU 2710 CD1 PHE B 316 1298 1277 1687 -121 -214 24 C ATOM 2711 CD2 PHE B 316 27.375 0.415 18.622 1.00 11.30 C ANISOU 2711 CD2 PHE B 316 1254 1261 1779 -214 -144 27 C ATOM 2712 CE1 PHE B 316 27.459 -1.189 16.386 1.00 13.06 C ANISOU 2712 CE1 PHE B 316 1556 1490 1915 -152 -271 18 C ATOM 2713 CE2 PHE B 316 26.438 -0.592 18.453 1.00 9.99 C ANISOU 2713 CE2 PHE B 316 1108 1078 1609 -246 -198 21 C ATOM 2714 CZ PHE B 316 26.481 -1.390 17.338 1.00 12.83 C ANISOU 2714 CZ PHE B 316 1509 1441 1925 -218 -262 16 C ATOM 2715 N LEU B 317 29.721 4.975 18.324 1.00 11.80 N ANISOU 2715 N LEU B 317 1217 1389 1876 -133 74 68 N ATOM 2716 CA LEU B 317 30.640 5.995 18.778 1.00 12.04 C ANISOU 2716 CA LEU B 317 1238 1430 1906 -138 142 66 C ATOM 2717 C LEU B 317 31.421 5.427 19.961 1.00 13.12 C ANISOU 2717 C LEU B 317 1391 1567 2027 -168 146 37 C ATOM 2718 O LEU B 317 30.840 5.034 20.971 1.00 14.27 O ANISOU 2718 O LEU B 317 1538 1688 2196 -207 143 32 O ATOM 2719 CB LEU B 317 29.862 7.241 19.191 1.00 19.17 C ANISOU 2719 CB LEU B 317 2110 2317 2858 -160 204 90 C ATOM 2720 CG LEU B 317 30.670 8.416 19.744 1.00 23.98 C ANISOU 2720 CG LEU B 317 2715 2928 3468 -177 283 89 C ATOM 2721 CD1 LEU B 317 31.696 8.888 18.731 1.00 18.48 C ANISOU 2721 CD1 LEU B 317 2031 2258 2733 -142 298 88 C ATOM 2722 CD2 LEU B 317 29.721 9.549 20.149 1.00 29.26 C ANISOU 2722 CD2 LEU B 317 3363 3571 4182 -193 340 116 C ATOM 2723 N VAL B 318 32.735 5.358 19.825 1.00 11.08 N ANISOU 2723 N VAL B 318 1144 1339 1727 -147 151 17 N ATOM 2724 CA VAL B 318 33.562 4.765 20.870 1.00 17.39 C ANISOU 2724 CA VAL B 318 1960 2147 2503 -163 146 -13 C ATOM 2725 C VAL B 318 34.753 5.655 21.178 1.00 11.89 C ANISOU 2725 C VAL B 318 1242 1484 1791 -170 202 -27 C ATOM 2726 O VAL B 318 34.912 6.717 20.583 1.00 18.07 O ANISOU 2726 O VAL B 318 2005 2278 2582 -168 248 -12 O ATOM 2727 CB VAL B 318 34.084 3.375 20.443 1.00 16.28 C ANISOU 2727 CB VAL B 318 1859 2018 2308 -122 76 -34 C ATOM 2728 CG1 VAL B 318 32.932 2.491 19.964 1.00 13.06 C ANISOU 2728 CG1 VAL B 318 1478 1578 1908 -120 19 -23 C ATOM 2729 CG2 VAL B 318 35.131 3.518 19.345 1.00 19.87 C ANISOU 2729 CG2 VAL B 318 2312 2517 2720 -72 74 -40 C ATOM 2730 N LYS B 319 35.586 5.220 22.116 1.00 9.16 N ANISOU 2730 N LYS B 319 904 1156 1421 -180 199 -56 N ATOM 2731 CA LYS B 319 36.874 5.866 22.336 1.00 7.55 C ANISOU 2731 CA LYS B 319 677 999 1193 -185 240 -77 C ATOM 2732 C LYS B 319 38.023 4.893 22.153 1.00 10.94 C ANISOU 2732 C LYS B 319 1118 1476 1563 -139 194 -108 C ATOM 2733 O LYS B 319 37.928 3.722 22.529 1.00 14.35 O ANISOU 2733 O LYS B 319 1585 1896 1973 -119 140 -121 O ATOM 2734 CB LYS B 319 36.932 6.485 23.729 1.00 11.41 C ANISOU 2734 CB LYS B 319 1154 1475 1706 -241 287 -85 C ATOM 2735 CG LYS B 319 35.968 7.643 23.911 1.00 19.71 C ANISOU 2735 CG LYS B 319 2193 2485 2809 -282 345 -55 C ATOM 2736 CD LYS B 319 36.229 8.363 25.231 1.00 29.23 C ANISOU 2736 CD LYS B 319 3392 3682 4031 -336 398 -66 C ATOM 2737 CE LYS B 319 35.218 9.472 25.482 1.00 36.70 C ANISOU 2737 CE LYS B 319 4336 4583 5027 -371 458 -34 C ATOM 2738 NZ LYS B 319 35.610 10.333 26.647 1.00 37.16 N ANISOU 2738 NZ LYS B 319 4394 4633 5092 -423 517 -45 N ATOM 2739 N GLU B 320 39.111 5.383 21.575 1.00 12.72 N ANISOU 2739 N GLU B 320 1316 1757 1759 -122 220 -121 N ATOM 2740 CA GLU B 320 40.319 4.579 21.402 1.00 19.94 C ANISOU 2740 CA GLU B 320 2231 2731 2614 -74 184 -153 C ATOM 2741 C GLU B 320 41.526 5.356 21.925 1.00 15.05 C ANISOU 2741 C GLU B 320 1565 2175 1980 -100 234 -181 C ATOM 2742 O GLU B 320 41.423 6.541 22.229 1.00 19.69 O ANISOU 2742 O GLU B 320 2128 2754 2599 -157 297 -172 O ATOM 2743 CB GLU B 320 40.530 4.229 19.922 1.00 17.10 C ANISOU 2743 CB GLU B 320 1881 2391 2224 -16 158 -145 C ATOM 2744 CG GLU B 320 40.841 5.440 19.056 1.00 21.53 C ANISOU 2744 CG GLU B 320 2411 2976 2794 -29 218 -133 C ATOM 2745 CD GLU B 320 40.888 5.141 17.557 1.00 20.31 C ANISOU 2745 CD GLU B 320 2276 2830 2613 27 195 -120 C ATOM 2746 OE1 GLU B 320 40.361 4.095 17.112 1.00 18.85 O ANISOU 2746 OE1 GLU B 320 2130 2618 2413 69 131 -113 O ATOM 2747 OE2 GLU B 320 41.448 5.980 16.826 1.00 21.99 O ANISOU 2747 OE2 GLU B 320 2467 3073 2816 24 242 -118 O ATOM 2748 N LYS B 321 42.669 4.688 22.025 1.00 14.92 N ANISOU 2748 N LYS B 321 1538 2222 1910 -59 205 -215 N ATOM 2749 CA LYS B 321 43.900 5.360 22.418 1.00 20.06 C ANISOU 2749 CA LYS B 321 2134 2947 2540 -83 247 -246 C ATOM 2750 C LYS B 321 44.335 6.407 21.384 1.00 23.39 C ANISOU 2750 C LYS B 321 2521 3402 2963 -100 305 -238 C ATOM 2751 O LYS B 321 44.351 6.142 20.183 1.00 28.01 O ANISOU 2751 O LYS B 321 3118 3994 3531 -54 290 -226 O ATOM 2752 CB LYS B 321 45.018 4.345 22.628 1.00 19.60 C ANISOU 2752 CB LYS B 321 2067 2959 2420 -22 198 -284 C ATOM 2753 CG LYS B 321 46.303 4.953 23.179 1.00 22.83 C ANISOU 2753 CG LYS B 321 2411 3457 2804 -48 234 -322 C ATOM 2754 CD LYS B 321 47.426 3.924 23.242 1.00 18.17 C ANISOU 2754 CD LYS B 321 1807 2948 2148 28 183 -361 C ATOM 2755 CE LYS B 321 48.683 4.518 23.886 1.00 18.09 C ANISOU 2755 CE LYS B 321 1722 3036 2114 -2 214 -403 C ATOM 2756 NZ LYS B 321 49.142 5.732 23.143 1.00 18.14 N ANISOU 2756 NZ LYS B 321 1673 3084 2133 -56 286 -402 N ATOM 2757 N MET B 322 44.677 7.599 21.859 1.00 17.96 N ANISOU 2757 N MET B 322 1800 2732 2293 -169 372 -245 N ATOM 2758 CA MET B 322 45.228 8.635 20.995 1.00 24.96 C ANISOU 2758 CA MET B 322 2658 3652 3173 -196 435 -244 C ATOM 2759 C MET B 322 46.650 8.242 20.597 1.00 28.58 C ANISOU 2759 C MET B 322 3071 4213 3576 -160 425 -282 C ATOM 2760 O MET B 322 47.428 7.760 21.423 1.00 18.34 O ANISOU 2760 O MET B 322 1743 2975 2252 -152 400 -318 O ATOM 2761 CB MET B 322 45.215 9.996 21.705 1.00 24.91 C ANISOU 2761 CB MET B 322 2638 3632 3196 -286 511 -243 C ATOM 2762 CG MET B 322 45.763 11.163 20.880 1.00 27.63 C ANISOU 2762 CG MET B 322 2966 4003 3531 -325 586 -242 C ATOM 2763 SD MET B 322 45.579 12.775 21.694 1.00 43.03 S ANISOU 2763 SD MET B 322 4922 5915 5511 -433 679 -237 S ATOM 2764 CE MET B 322 46.622 13.799 20.654 1.00 44.41 C ANISOU 2764 CE MET B 322 5076 6146 5651 -471 756 -251 C ATOM 2765 N LYS B 323 46.979 8.424 19.325 1.00 29.20 N ANISOU 2765 N LYS B 323 3145 4315 3634 -134 444 -275 N ATOM 2766 CA LYS B 323 48.318 8.111 18.838 1.00 33.15 C ANISOU 2766 CA LYS B 323 3597 4917 4081 -99 442 -310 C ATOM 2767 C LYS B 323 49.373 8.840 19.668 1.00 30.87 C ANISOU 2767 C LYS B 323 3243 4706 3779 -166 490 -350 C ATOM 2768 O LYS B 323 49.351 10.068 19.763 1.00 30.55 O ANISOU 2768 O LYS B 323 3194 4652 3761 -247 562 -346 O ATOM 2769 CB LYS B 323 48.443 8.510 17.367 1.00 43.13 C ANISOU 2769 CB LYS B 323 4871 6186 5332 -81 477 -293 C ATOM 2770 CG LYS B 323 49.815 8.281 16.759 1.00 55.19 C ANISOU 2770 CG LYS B 323 6346 7820 6804 -48 486 -328 C ATOM 2771 CD LYS B 323 49.987 6.844 16.280 1.00 67.16 C ANISOU 2771 CD LYS B 323 7880 9357 8280 58 408 -333 C ATOM 2772 CE LYS B 323 51.182 6.719 15.333 1.00 73.89 C ANISOU 2772 CE LYS B 323 8691 10304 9079 100 427 -358 C ATOM 2773 NZ LYS B 323 51.453 5.309 14.925 1.00 75.68 N ANISOU 2773 NZ LYS B 323 8938 10557 9259 210 354 -366 N ATOM 2774 N GLY B 324 50.281 8.079 20.275 1.00 28.02 N ANISOU 2774 N GLY B 324 2839 4426 3380 -130 449 -390 N ATOM 2775 CA GLY B 324 51.397 8.648 21.012 1.00 30.45 C ANISOU 2775 CA GLY B 324 3075 4826 3668 -186 485 -435 C ATOM 2776 C GLY B 324 51.093 9.236 22.387 1.00 32.08 C ANISOU 2776 C GLY B 324 3282 5001 3905 -264 503 -441 C ATOM 2777 O GLY B 324 51.986 9.768 23.046 1.00 27.36 O ANISOU 2777 O GLY B 324 2626 4479 3292 -319 532 -480 O ATOM 2778 N LYS B 325 49.846 9.150 22.838 1.00 27.02 N ANISOU 2778 N LYS B 325 2705 4253 3307 -270 486 -406 N ATOM 2779 CA LYS B 325 49.511 9.706 24.149 1.00 30.07 C ANISOU 2779 CA LYS B 325 3099 4604 3722 -341 506 -410 C ATOM 2780 C LYS B 325 48.636 8.778 24.990 1.00 25.64 C ANISOU 2780 C LYS B 325 2589 3975 3177 -302 443 -396 C ATOM 2781 O LYS B 325 47.785 8.066 24.455 1.00 25.24 O ANISOU 2781 O LYS B 325 2587 3863 3139 -247 404 -366 O ATOM 2782 CB LYS B 325 48.838 11.074 23.996 1.00 29.43 C ANISOU 2782 CB LYS B 325 3044 4453 3684 -425 585 -380 C ATOM 2783 CG LYS B 325 49.355 11.859 22.818 1.00 29.98 C ANISOU 2783 CG LYS B 325 3094 4557 3739 -448 645 -378 C ATOM 2784 CD LYS B 325 49.840 13.235 23.224 1.00 38.77 C ANISOU 2784 CD LYS B 325 4187 5689 4855 -556 730 -395 C ATOM 2785 CE LYS B 325 50.855 13.750 22.208 1.00 44.75 C ANISOU 2785 CE LYS B 325 4902 6523 5577 -577 781 -415 C ATOM 2786 NZ LYS B 325 51.802 14.741 22.788 1.00 52.03 N ANISOU 2786 NZ LYS B 325 5793 7498 6478 -675 830 -457 N ATOM 2787 N ASN B 326 48.862 8.786 26.305 1.00 21.52 N ANISOU 2787 N ASN B 326 2058 3465 2653 -334 435 -421 N ATOM 2788 CA ASN B 326 47.991 8.078 27.246 1.00 27.27 C ANISOU 2788 CA ASN B 326 2842 4120 3400 -315 389 -408 C ATOM 2789 C ASN B 326 46.677 8.835 27.452 1.00 26.65 C ANISOU 2789 C ASN B 326 2811 3932 3382 -373 433 -365 C ATOM 2790 O ASN B 326 46.477 9.505 28.469 1.00 22.75 O ANISOU 2790 O ASN B 326 2324 3410 2909 -438 467 -368 O ATOM 2791 CB ASN B 326 48.699 7.835 28.586 1.00 20.09 C ANISOU 2791 CB ASN B 326 1912 3259 2462 -326 366 -449 C ATOM 2792 CG ASN B 326 49.621 6.619 28.552 1.00 27.30 C ANISOU 2792 CG ASN B 326 2805 4254 3313 -234 295 -484 C ATOM 2793 OD1 ASN B 326 50.005 6.140 27.480 1.00 27.78 O ANISOU 2793 OD1 ASN B 326 2851 4357 3348 -172 276 -484 O ATOM 2794 ND2 ASN B 326 49.975 6.111 29.730 1.00 26.29 N ANISOU 2794 ND2 ASN B 326 2682 4147 3158 -219 257 -513 N ATOM 2795 N LYS B 327 45.785 8.719 26.473 1.00 22.02 N ANISOU 2795 N LYS B 327 2257 3288 2820 -345 430 -326 N ATOM 2796 CA LYS B 327 44.556 9.504 26.450 1.00 22.87 C ANISOU 2796 CA LYS B 327 2401 3304 2983 -390 474 -284 C ATOM 2797 C LYS B 327 43.543 8.835 25.527 1.00 24.64 C ANISOU 2797 C LYS B 327 2663 3474 3225 -334 436 -248 C ATOM 2798 O LYS B 327 43.907 8.316 24.470 1.00 18.53 O ANISOU 2798 O LYS B 327 1882 2735 2423 -280 408 -250 O ATOM 2799 CB LYS B 327 44.860 10.922 25.954 1.00 25.85 C ANISOU 2799 CB LYS B 327 2758 3694 3370 -451 555 -278 C ATOM 2800 CG LYS B 327 43.698 11.908 26.061 1.00 32.30 C ANISOU 2800 CG LYS B 327 3614 4422 4237 -497 610 -238 C ATOM 2801 CD LYS B 327 43.908 13.084 25.112 1.00 36.87 C ANISOU 2801 CD LYS B 327 4198 4998 4811 -525 671 -228 C ATOM 2802 CE LYS B 327 43.121 14.314 25.537 1.00 37.77 C ANISOU 2802 CE LYS B 327 4375 5023 4953 -567 715 -210 C ATOM 2803 NZ LYS B 327 41.690 14.012 25.792 1.00 42.92 N ANISOU 2803 NZ LYS B 327 5064 5595 5648 -538 694 -174 N ATOM 2804 N LEU B 328 42.276 8.837 25.928 1.00 22.86 N ANISOU 2804 N LEU B 328 2477 3166 3043 -349 435 -218 N ATOM 2805 CA LEU B 328 41.217 8.268 25.099 1.00 26.33 C ANISOU 2805 CA LEU B 328 2948 3555 3502 -307 401 -184 C ATOM 2806 C LEU B 328 40.531 9.355 24.264 1.00 25.85 C ANISOU 2806 C LEU B 328 2889 3459 3476 -327 454 -149 C ATOM 2807 O LEU B 328 40.183 10.409 24.790 1.00 22.41 O ANISOU 2807 O LEU B 328 2454 2991 3069 -381 513 -137 O ATOM 2808 CB LEU B 328 40.183 7.543 25.973 1.00 22.26 C ANISOU 2808 CB LEU B 328 2470 2976 3012 -309 366 -174 C ATOM 2809 CG LEU B 328 40.617 6.234 26.642 1.00 23.89 C ANISOU 2809 CG LEU B 328 2697 3199 3180 -273 302 -203 C ATOM 2810 CD1 LEU B 328 39.595 5.802 27.702 1.00 24.38 C ANISOU 2810 CD1 LEU B 328 2800 3191 3271 -298 289 -193 C ATOM 2811 CD2 LEU B 328 40.823 5.134 25.598 1.00 24.61 C ANISOU 2811 CD2 LEU B 328 2806 3312 3234 -201 240 -205 C ATOM 2812 N VAL B 329 40.344 9.094 22.970 1.00 22.78 N ANISOU 2812 N VAL B 329 2505 3072 3077 -280 432 -132 N ATOM 2813 CA VAL B 329 39.644 10.019 22.080 1.00 15.19 C ANISOU 2813 CA VAL B 329 1555 2076 2142 -284 473 -97 C ATOM 2814 C VAL B 329 38.561 9.310 21.259 1.00 20.79 C ANISOU 2814 C VAL B 329 2287 2746 2865 -235 420 -69 C ATOM 2815 O VAL B 329 38.630 8.093 21.060 1.00 21.99 O ANISOU 2815 O VAL B 329 2450 2909 2994 -193 354 -80 O ATOM 2816 CB VAL B 329 40.619 10.736 21.130 1.00 25.36 C ANISOU 2816 CB VAL B 329 2827 3412 3399 -283 516 -105 C ATOM 2817 CG1 VAL B 329 41.739 11.385 21.923 1.00 27.04 C ANISOU 2817 CG1 VAL B 329 3009 3672 3593 -339 565 -138 C ATOM 2818 CG2 VAL B 329 41.179 9.761 20.102 1.00 20.50 C ANISOU 2818 CG2 VAL B 329 2208 2840 2742 -218 462 -116 C ATOM 2819 N PRO B 330 37.559 10.078 20.780 1.00 26.06 N ANISOU 2819 N PRO B 330 2966 3368 3567 -239 450 -34 N ATOM 2820 CA PRO B 330 36.386 9.573 20.045 1.00 21.10 C ANISOU 2820 CA PRO B 330 2354 2704 2957 -201 404 -6 C ATOM 2821 C PRO B 330 36.718 9.007 18.668 1.00 17.10 C ANISOU 2821 C PRO B 330 1859 2224 2415 -143 362 -5 C ATOM 2822 O PRO B 330 37.684 9.427 18.035 1.00 15.56 O ANISOU 2822 O PRO B 330 1658 2065 2187 -133 390 -15 O ATOM 2823 CB PRO B 330 35.508 10.825 19.873 1.00 17.60 C ANISOU 2823 CB PRO B 330 1916 2221 2550 -217 461 28 C ATOM 2824 CG PRO B 330 35.984 11.786 20.903 1.00 25.91 C ANISOU 2824 CG PRO B 330 2962 3271 3611 -274 532 18 C ATOM 2825 CD PRO B 330 37.457 11.527 21.030 1.00 22.71 C ANISOU 2825 CD PRO B 330 2543 2924 3164 -284 532 -19 C ATOM 2826 N ARG B 331 35.905 8.060 18.217 1.00 16.25 N ANISOU 2826 N ARG B 331 1767 2096 2311 -109 296 6 N ATOM 2827 CA ARG B 331 36.036 7.484 16.885 1.00 15.63 C ANISOU 2827 CA ARG B 331 1708 2033 2200 -53 251 10 C ATOM 2828 C ARG B 331 34.754 6.720 16.556 1.00 12.32 C ANISOU 2828 C ARG B 331 1305 1577 1799 -36 189 28 C ATOM 2829 O ARG B 331 34.005 6.343 17.458 1.00 15.92 O ANISOU 2829 O ARG B 331 1757 2007 2285 -67 174 29 O ATOM 2830 CB ARG B 331 37.244 6.547 16.820 1.00 13.00 C ANISOU 2830 CB ARG B 331 1380 1744 1814 -25 217 -23 C ATOM 2831 CG ARG B 331 37.745 6.298 15.415 1.00 19.02 C ANISOU 2831 CG ARG B 331 2160 2533 2535 30 197 -21 C ATOM 2832 CD ARG B 331 38.404 7.543 14.849 1.00 23.32 C ANISOU 2832 CD ARG B 331 2689 3101 3072 22 269 -16 C ATOM 2833 NE ARG B 331 39.641 7.874 15.549 1.00 31.93 N ANISOU 2833 NE ARG B 331 3748 4240 4143 -8 312 -47 N ATOM 2834 CZ ARG B 331 40.194 9.084 15.558 1.00 43.82 C ANISOU 2834 CZ ARG B 331 5236 5762 5650 -46 389 -48 C ATOM 2835 NH1 ARG B 331 41.323 9.298 16.224 1.00 48.94 N ANISOU 2835 NH1 ARG B 331 5852 6463 6280 -78 422 -81 N ATOM 2836 NH2 ARG B 331 39.613 10.085 14.912 1.00 44.47 N ANISOU 2836 NH2 ARG B 331 5337 5809 5750 -53 432 -19 N ATOM 2837 N LEU B 332 34.502 6.498 15.269 1.00 11.44 N ANISOU 2837 N LEU B 332 1212 1467 1670 10 155 42 N ATOM 2838 CA LEU B 332 33.368 5.689 14.838 1.00 14.31 C ANISOU 2838 CA LEU B 332 1590 1804 2043 25 89 55 C ATOM 2839 C LEU B 332 33.819 4.284 14.434 1.00 16.99 C ANISOU 2839 C LEU B 332 1967 2155 2335 58 20 35 C ATOM 2840 O LEU B 332 34.731 4.120 13.625 1.00 15.79 O ANISOU 2840 O LEU B 332 1832 2030 2138 100 14 26 O ATOM 2841 CB LEU B 332 32.622 6.359 13.673 1.00 11.45 C ANISOU 2841 CB LEU B 332 1230 1432 1690 56 91 85 C ATOM 2842 CG LEU B 332 31.889 7.671 13.965 1.00 11.59 C ANISOU 2842 CG LEU B 332 1221 1430 1753 36 151 110 C ATOM 2843 CD1 LEU B 332 31.361 8.303 12.683 1.00 13.27 C ANISOU 2843 CD1 LEU B 332 1445 1637 1959 82 150 137 C ATOM 2844 CD2 LEU B 332 30.756 7.457 14.948 1.00 13.12 C ANISOU 2844 CD2 LEU B 332 1391 1602 1995 -3 139 115 C ATOM 2845 N LEU B 333 33.181 3.277 15.018 1.00 14.87 N ANISOU 2845 N LEU B 333 1713 1863 2073 38 -29 27 N ATOM 2846 CA LEU B 333 33.410 1.889 14.644 1.00 7.32 C ANISOU 2846 CA LEU B 333 807 905 1070 67 -99 10 C ATOM 2847 C LEU B 333 32.202 1.398 13.853 1.00 12.63 C ANISOU 2847 C LEU B 333 1496 1552 1750 70 -154 26 C ATOM 2848 O LEU B 333 31.070 1.445 14.341 1.00 13.53 O ANISOU 2848 O LEU B 333 1591 1644 1908 28 -160 36 O ATOM 2849 CB LEU B 333 33.587 1.027 15.893 1.00 11.02 C ANISOU 2849 CB LEU B 333 1296 1361 1531 38 -115 -14 C ATOM 2850 CG LEU B 333 33.822 -0.464 15.641 1.00 9.36 C ANISOU 2850 CG LEU B 333 1151 1140 1264 69 -184 -33 C ATOM 2851 CD1 LEU B 333 35.106 -0.648 14.875 1.00 8.34 C ANISOU 2851 CD1 LEU B 333 1041 1051 1078 133 -188 -45 C ATOM 2852 CD2 LEU B 333 33.876 -1.229 16.968 1.00 14.19 C ANISOU 2852 CD2 LEU B 333 1790 1731 1870 38 -193 -54 C ATOM 2853 N GLY B 334 32.442 0.943 12.629 1.00 12.43 N ANISOU 2853 N GLY B 334 1506 1534 1681 120 -195 28 N ATOM 2854 CA GLY B 334 31.371 0.482 11.767 1.00 11.67 C ANISOU 2854 CA GLY B 334 1428 1419 1586 125 -253 41 C ATOM 2855 C GLY B 334 31.394 -1.020 11.534 1.00 12.90 C ANISOU 2855 C GLY B 334 1651 1558 1693 135 -325 23 C ATOM 2856 O GLY B 334 32.452 -1.616 11.312 1.00 13.49 O ANISOU 2856 O GLY B 334 1769 1643 1713 177 -336 7 O ATOM 2857 N ILE B 335 30.217 -1.631 11.609 1.00 11.78 N ANISOU 2857 N ILE B 335 1518 1391 1568 96 -371 25 N ATOM 2858 CA ILE B 335 30.055 -3.037 11.284 1.00 14.58 C ANISOU 2858 CA ILE B 335 1946 1721 1874 97 -441 10 C ATOM 2859 C ILE B 335 29.228 -3.160 10.002 1.00 17.86 C ANISOU 2859 C ILE B 335 2370 2134 2280 111 -492 24 C ATOM 2860 O ILE B 335 28.098 -2.679 9.940 1.00 17.07 O ANISOU 2860 O ILE B 335 2221 2038 2229 77 -496 38 O ATOM 2861 CB ILE B 335 29.350 -3.789 12.414 1.00 17.84 C ANISOU 2861 CB ILE B 335 2373 2103 2304 29 -456 -4 C ATOM 2862 CG1 ILE B 335 29.901 -3.351 13.776 1.00 17.71 C ANISOU 2862 CG1 ILE B 335 2328 2089 2313 7 -396 -13 C ATOM 2863 CG2 ILE B 335 29.472 -5.298 12.206 1.00 17.75 C ANISOU 2863 CG2 ILE B 335 2456 2059 2227 33 -519 -25 C ATOM 2864 CD1 ILE B 335 31.360 -3.719 14.011 1.00 12.56 C ANISOU 2864 CD1 ILE B 335 1717 1449 1607 56 -386 -32 C ATOM 2865 N THR B 336 29.809 -3.774 8.975 1.00 17.63 N ANISOU 2865 N THR B 336 2404 2103 2190 164 -532 19 N ATOM 2866 CA THR B 336 29.127 -3.931 7.694 1.00 23.26 C ANISOU 2866 CA THR B 336 3137 2815 2887 183 -585 31 C ATOM 2867 C THR B 336 28.809 -5.396 7.468 1.00 29.34 C ANISOU 2867 C THR B 336 3990 3552 3607 165 -657 13 C ATOM 2868 O THR B 336 29.149 -6.256 8.290 1.00 24.66 O ANISOU 2868 O THR B 336 3444 2936 2990 144 -663 -7 O ATOM 2869 CB THR B 336 29.984 -3.443 6.491 1.00 25.13 C ANISOU 2869 CB THR B 336 3391 3071 3086 261 -574 42 C ATOM 2870 OG1 THR B 336 30.755 -4.533 5.966 1.00 25.51 O ANISOU 2870 OG1 THR B 336 3527 3106 3061 303 -613 26 O ATOM 2871 CG2 THR B 336 30.908 -2.309 6.891 1.00 23.68 C ANISOU 2871 CG2 THR B 336 3159 2915 2925 283 -493 48 C ATOM 2872 N LYS B 337 28.175 -5.685 6.339 1.00 29.47 N ANISOU 2872 N LYS B 337 4032 3565 3602 175 -714 19 N ATOM 2873 CA LYS B 337 27.820 -7.060 6.016 1.00 35.14 C ANISOU 2873 CA LYS B 337 4835 4248 4267 153 -785 2 C ATOM 2874 C LYS B 337 29.049 -7.962 5.865 1.00 30.90 C ANISOU 2874 C LYS B 337 4397 3691 3653 208 -794 -14 C ATOM 2875 O LYS B 337 28.969 -9.163 6.105 1.00 31.21 O ANISOU 2875 O LYS B 337 4519 3693 3648 184 -835 -33 O ATOM 2876 CB LYS B 337 26.947 -7.111 4.753 1.00 37.74 C ANISOU 2876 CB LYS B 337 5172 4583 4586 157 -844 12 C ATOM 2877 CG LYS B 337 27.524 -6.382 3.549 1.00 42.14 C ANISOU 2877 CG LYS B 337 5729 5161 5122 240 -836 30 C ATOM 2878 CD LYS B 337 26.489 -6.294 2.436 1.00 50.48 C ANISOU 2878 CD LYS B 337 6778 6225 6177 238 -894 41 C ATOM 2879 CE LYS B 337 27.075 -5.699 1.167 1.00 57.34 C ANISOU 2879 CE LYS B 337 7667 7105 7013 323 -890 58 C ATOM 2880 NZ LYS B 337 26.054 -5.598 0.085 1.00 60.49 N ANISOU 2880 NZ LYS B 337 8062 7514 7408 327 -951 68 N ATOM 2881 N ASP B 338 30.187 -7.379 5.490 1.00 27.96 N ANISOU 2881 N ASP B 338 4017 3343 3262 282 -754 -7 N ATOM 2882 CA ASP B 338 31.390 -8.168 5.227 1.00 29.27 C ANISOU 2882 CA ASP B 338 4267 3500 3352 347 -762 -21 C ATOM 2883 C ASP B 338 32.673 -7.640 5.886 1.00 22.28 C ANISOU 2883 C ASP B 338 3347 2649 2469 389 -696 -27 C ATOM 2884 O ASP B 338 33.757 -8.176 5.662 1.00 17.67 O ANISOU 2884 O ASP B 338 2819 2071 1823 453 -696 -39 O ATOM 2885 CB ASP B 338 31.600 -8.292 3.717 1.00 34.42 C ANISOU 2885 CB ASP B 338 4970 4154 3954 410 -796 -12 C ATOM 2886 CG ASP B 338 31.535 -6.954 3.013 1.00 46.20 C ANISOU 2886 CG ASP B 338 6388 5681 5486 434 -760 12 C ATOM 2887 OD1 ASP B 338 32.272 -6.031 3.423 1.00 40.81 O ANISOU 2887 OD1 ASP B 338 5645 5030 4831 454 -693 17 O ATOM 2888 OD2 ASP B 338 30.744 -6.826 2.052 1.00 61.56 O ANISOU 2888 OD2 ASP B 338 8339 7620 7432 434 -800 25 O ATOM 2889 N SER B 339 32.561 -6.598 6.701 1.00 21.69 N ANISOU 2889 N SER B 339 3182 2598 2462 354 -639 -19 N ATOM 2890 CA SER B 339 33.765 -5.994 7.256 1.00 15.42 C ANISOU 2890 CA SER B 339 2348 1841 1670 387 -576 -26 C ATOM 2891 C SER B 339 33.533 -5.188 8.522 1.00 11.29 C ANISOU 2891 C SER B 339 1746 1330 1215 329 -524 -25 C ATOM 2892 O SER B 339 32.395 -4.962 8.945 1.00 10.80 O ANISOU 2892 O SER B 339 1650 1249 1205 267 -529 -16 O ATOM 2893 CB SER B 339 34.423 -5.092 6.206 1.00 24.34 C ANISOU 2893 CB SER B 339 3450 3007 2791 443 -542 -12 C ATOM 2894 OG SER B 339 33.620 -3.944 5.942 1.00 17.02 O ANISOU 2894 OG SER B 339 2457 2086 1925 413 -517 12 O ATOM 2895 N VAL B 340 34.643 -4.761 9.114 1.00 10.85 N ANISOU 2895 N VAL B 340 1660 1308 1156 353 -472 -35 N ATOM 2896 CA VAL B 340 34.646 -3.808 10.206 1.00 13.98 C ANISOU 2896 CA VAL B 340 1980 1721 1611 307 -412 -34 C ATOM 2897 C VAL B 340 35.483 -2.595 9.791 1.00 15.58 C ANISOU 2897 C VAL B 340 2126 1969 1823 336 -349 -26 C ATOM 2898 O VAL B 340 36.563 -2.750 9.223 1.00 16.07 O ANISOU 2898 O VAL B 340 2207 2062 1836 394 -343 -36 O ATOM 2899 CB VAL B 340 35.257 -4.424 11.454 1.00 12.82 C ANISOU 2899 CB VAL B 340 1851 1574 1446 299 -407 -59 C ATOM 2900 CG1 VAL B 340 35.353 -3.383 12.559 1.00 14.19 C ANISOU 2900 CG1 VAL B 340 1949 1767 1677 254 -343 -59 C ATOM 2901 CG2 VAL B 340 34.438 -5.634 11.899 1.00 15.08 C ANISOU 2901 CG2 VAL B 340 2205 1807 1716 265 -463 -68 C ATOM 2902 N MET B 341 35.000 -1.389 10.068 1.00 8.26 N ANISOU 2902 N MET B 341 1135 1048 958 295 -300 -9 N ATOM 2903 CA MET B 341 35.765 -0.196 9.689 1.00 20.58 C ANISOU 2903 CA MET B 341 2651 2645 2524 314 -235 -2 C ATOM 2904 C MET B 341 35.944 0.833 10.807 1.00 15.66 C ANISOU 2904 C MET B 341 1965 2036 1949 265 -166 -3 C ATOM 2905 O MET B 341 35.075 1.007 11.654 1.00 17.98 O ANISOU 2905 O MET B 341 2236 2304 2290 214 -162 3 O ATOM 2906 CB MET B 341 35.205 0.455 8.407 1.00 22.36 C ANISOU 2906 CB MET B 341 2879 2862 2756 335 -235 25 C ATOM 2907 CG MET B 341 33.754 0.886 8.465 1.00 14.54 C ANISOU 2907 CG MET B 341 1865 1841 1820 296 -247 48 C ATOM 2908 SD MET B 341 33.094 1.622 6.922 1.00 18.11 S ANISOU 2908 SD MET B 341 2324 2285 2270 334 -256 78 S ATOM 2909 CE MET B 341 33.289 0.279 5.763 1.00 20.71 C ANISOU 2909 CE MET B 341 2733 2607 2530 387 -336 69 C ATOM 2910 N ARG B 342 37.099 1.492 10.798 1.00 10.46 N ANISOU 2910 N ARG B 342 1280 1421 1275 279 -111 -13 N ATOM 2911 CA ARG B 342 37.410 2.574 11.720 1.00 9.75 C ANISOU 2911 CA ARG B 342 1135 1347 1222 233 -40 -16 C ATOM 2912 C ARG B 342 37.219 3.885 10.959 1.00 13.11 C ANISOU 2912 C ARG B 342 1541 1772 1669 229 14 8 C ATOM 2913 O ARG B 342 37.805 4.082 9.895 1.00 12.08 O ANISOU 2913 O ARG B 342 1426 1662 1504 269 25 11 O ATOM 2914 CB ARG B 342 38.862 2.430 12.210 1.00 9.86 C ANISOU 2914 CB ARG B 342 1131 1415 1199 246 -15 -47 C ATOM 2915 CG ARG B 342 39.192 3.151 13.505 1.00 22.62 C ANISOU 2915 CG ARG B 342 2700 3048 2847 191 39 -60 C ATOM 2916 CD ARG B 342 40.566 2.736 14.072 1.00 22.28 C ANISOU 2916 CD ARG B 342 2640 3065 2761 210 44 -96 C ATOM 2917 NE ARG B 342 41.651 3.187 13.216 1.00 33.48 N ANISOU 2917 NE ARG B 342 4038 4539 4144 240 81 -105 N ATOM 2918 CZ ARG B 342 42.348 4.303 13.401 1.00 34.68 C ANISOU 2918 CZ ARG B 342 4141 4729 4305 203 152 -113 C ATOM 2919 NH1 ARG B 342 42.097 5.095 14.433 1.00 25.89 N ANISOU 2919 NH1 ARG B 342 2997 3604 3234 138 194 -113 N ATOM 2920 NH2 ARG B 342 43.309 4.619 12.545 1.00 47.67 N ANISOU 2920 NH2 ARG B 342 5772 6426 5914 229 184 -123 N ATOM 2921 N VAL B 343 36.387 4.775 11.484 1.00 14.68 N ANISOU 2921 N VAL B 343 1712 1944 1920 184 49 27 N ATOM 2922 CA VAL B 343 36.012 5.975 10.737 1.00 15.44 C ANISOU 2922 CA VAL B 343 1805 2029 2034 187 94 53 C ATOM 2923 C VAL B 343 36.209 7.244 11.562 1.00 10.99 C ANISOU 2923 C VAL B 343 1207 1466 1502 137 177 56 C ATOM 2924 O VAL B 343 35.874 7.277 12.743 1.00 11.36 O ANISOU 2924 O VAL B 343 1231 1501 1584 94 186 51 O ATOM 2925 CB VAL B 343 34.543 5.885 10.240 1.00 11.61 C ANISOU 2925 CB VAL B 343 1332 1504 1576 197 50 81 C ATOM 2926 CG1 VAL B 343 34.041 7.231 9.761 1.00 12.39 C ANISOU 2926 CG1 VAL B 343 1424 1586 1696 200 102 109 C ATOM 2927 CG2 VAL B 343 34.415 4.845 9.128 1.00 10.92 C ANISOU 2927 CG2 VAL B 343 1287 1414 1447 248 -24 81 C ATOM 2928 N ASP B 344 36.765 8.281 10.941 1.00 11.81 N ANISOU 2928 N ASP B 344 1315 1581 1592 142 238 63 N ATOM 2929 CA ASP B 344 36.946 9.571 11.609 1.00 13.12 C ANISOU 2929 CA ASP B 344 1461 1741 1781 92 322 67 C ATOM 2930 C ASP B 344 35.595 10.215 11.898 1.00 15.38 C ANISOU 2930 C ASP B 344 1747 1980 2116 79 332 97 C ATOM 2931 O ASP B 344 34.793 10.434 10.978 1.00 14.02 O ANISOU 2931 O ASP B 344 1598 1784 1945 117 314 123 O ATOM 2932 CB ASP B 344 37.797 10.498 10.741 1.00 20.37 C ANISOU 2932 CB ASP B 344 2396 2677 2666 100 386 68 C ATOM 2933 CG ASP B 344 38.160 11.792 11.444 1.00 26.23 C ANISOU 2933 CG ASP B 344 3128 3416 3424 40 477 66 C ATOM 2934 OD1 ASP B 344 37.253 12.585 11.770 1.00 21.50 O ANISOU 2934 OD1 ASP B 344 2538 2773 2859 23 505 90 O ATOM 2935 OD2 ASP B 344 39.365 12.026 11.655 1.00 37.62 O ANISOU 2935 OD2 ASP B 344 4553 4902 4840 11 520 39 O ATOM 2936 N GLU B 345 35.348 10.529 13.169 1.00 12.15 N ANISOU 2936 N GLU B 345 1314 1560 1744 28 360 93 N ATOM 2937 CA GLU B 345 34.030 10.991 13.608 1.00 13.66 C ANISOU 2937 CA GLU B 345 1499 1710 1982 17 365 119 C ATOM 2938 C GLU B 345 33.702 12.412 13.147 1.00 15.16 C ANISOU 2938 C GLU B 345 1709 1873 2177 24 433 146 C ATOM 2939 O GLU B 345 32.538 12.817 13.155 1.00 11.99 O ANISOU 2939 O GLU B 345 1307 1442 1806 38 431 172 O ATOM 2940 CB GLU B 345 33.859 10.850 15.131 1.00 19.02 C ANISOU 2940 CB GLU B 345 2150 2381 2695 -37 376 106 C ATOM 2941 CG GLU B 345 34.472 11.960 15.974 1.00 27.78 C ANISOU 2941 CG GLU B 345 3255 3489 3812 -87 461 99 C ATOM 2942 CD GLU B 345 35.999 11.927 15.997 1.00 45.78 C ANISOU 2942 CD GLU B 345 5530 5813 6050 -105 485 68 C ATOM 2943 OE1 GLU B 345 36.600 11.011 15.389 1.00 46.89 O ANISOU 2943 OE1 GLU B 345 5671 5988 6157 -71 436 51 O ATOM 2944 OE2 GLU B 345 36.601 12.821 16.632 1.00 51.22 O ANISOU 2944 OE2 GLU B 345 6215 6507 6739 -153 553 58 O ATOM 2945 N LYS B 346 34.724 13.154 12.730 1.00 18.71 N ANISOU 2945 N LYS B 346 2180 2336 2593 17 492 139 N ATOM 2946 CA LYS B 346 34.528 14.507 12.202 1.00 25.19 C ANISOU 2946 CA LYS B 346 3038 3126 3407 25 561 164 C ATOM 2947 C LYS B 346 34.381 14.541 10.679 1.00 21.22 C ANISOU 2947 C LYS B 346 2574 2618 2870 89 540 181 C ATOM 2948 O LYS B 346 33.438 15.123 10.143 1.00 25.41 O ANISOU 2948 O LYS B 346 3131 3116 3408 128 544 212 O ATOM 2949 CB LYS B 346 35.677 15.430 12.621 1.00 27.25 C ANISOU 2949 CB LYS B 346 3310 3397 3647 -30 649 146 C ATOM 2950 CG LYS B 346 35.779 15.646 14.125 1.00 43.86 C ANISOU 2950 CG LYS B 346 5385 5499 5781 -96 681 131 C ATOM 2951 CD LYS B 346 36.969 16.527 14.487 1.00 52.21 C ANISOU 2951 CD LYS B 346 6452 6572 6812 -157 764 110 C ATOM 2952 CE LYS B 346 37.194 16.560 15.998 1.00 56.12 C ANISOU 2952 CE LYS B 346 6917 7073 7332 -222 783 89 C ATOM 2953 NZ LYS B 346 38.401 17.358 16.374 1.00 58.00 N ANISOU 2953 NZ LYS B 346 7158 7336 7543 -289 858 63 N ATOM 2954 N THR B 347 35.323 13.926 9.981 1.00 12.64 N ANISOU 2954 N THR B 347 1494 1566 1745 105 519 162 N ATOM 2955 CA THR B 347 35.357 14.034 8.533 1.00 13.77 C ANISOU 2955 CA THR B 347 1681 1702 1849 162 510 177 C ATOM 2956 C THR B 347 34.639 12.873 7.868 1.00 20.95 C ANISOU 2956 C THR B 347 2588 2615 2758 217 411 184 C ATOM 2957 O THR B 347 34.270 12.963 6.697 1.00 14.58 O ANISOU 2957 O THR B 347 1820 1794 1927 272 390 202 O ATOM 2958 CB THR B 347 36.791 14.032 8.024 1.00 19.07 C ANISOU 2958 CB THR B 347 2363 2409 2471 153 546 153 C ATOM 2959 OG1 THR B 347 37.373 12.750 8.294 1.00 17.28 O ANISOU 2959 OG1 THR B 347 2101 2228 2237 154 487 125 O ATOM 2960 CG2 THR B 347 37.604 15.139 8.707 1.00 21.57 C ANISOU 2960 CG2 THR B 347 2680 2731 2785 85 645 141 C ATOM 2961 N LYS B 348 34.468 11.787 8.623 1.00 17.57 N ANISOU 2961 N LYS B 348 2120 2203 2351 200 352 167 N ATOM 2962 CA LYS B 348 33.845 10.551 8.144 1.00 15.99 C ANISOU 2962 CA LYS B 348 1920 2007 2148 237 256 167 C ATOM 2963 C LYS B 348 34.714 9.797 7.137 1.00 17.46 C ANISOU 2963 C LYS B 348 2136 2218 2282 277 224 153 C ATOM 2964 O LYS B 348 34.245 8.907 6.429 1.00 13.55 O ANISOU 2964 O LYS B 348 1658 1719 1770 316 150 157 O ATOM 2965 CB LYS B 348 32.432 10.803 7.605 1.00 15.35 C ANISOU 2965 CB LYS B 348 1847 1897 2088 273 222 198 C ATOM 2966 CG LYS B 348 31.372 10.979 8.697 1.00 8.69 C ANISOU 2966 CG LYS B 348 962 1039 1301 239 222 206 C ATOM 2967 CD LYS B 348 31.566 12.267 9.488 1.00 10.13 C ANISOU 2967 CD LYS B 348 1140 1204 1503 203 314 214 C ATOM 2968 CE LYS B 348 30.399 12.472 10.462 1.00 14.83 C ANISOU 2968 CE LYS B 348 1699 1784 2153 181 314 226 C ATOM 2969 NZ LYS B 348 30.499 13.740 11.242 1.00 14.14 N ANISOU 2969 NZ LYS B 348 1616 1674 2082 150 404 235 N ATOM 2970 N GLU B 349 35.992 10.149 7.082 1.00 17.75 N ANISOU 2970 N GLU B 349 2177 2282 2288 264 281 135 N ATOM 2971 CA GLU B 349 36.940 9.394 6.271 1.00 17.03 C ANISOU 2971 CA GLU B 349 2105 2221 2144 300 256 118 C ATOM 2972 C GLU B 349 37.088 7.979 6.832 1.00 18.17 C ANISOU 2972 C GLU B 349 2232 2387 2286 302 186 95 C ATOM 2973 O GLU B 349 37.221 7.798 8.045 1.00 16.94 O ANISOU 2973 O GLU B 349 2040 2242 2155 259 192 78 O ATOM 2974 CB GLU B 349 38.306 10.097 6.254 1.00 22.58 C ANISOU 2974 CB GLU B 349 2803 2959 2819 276 338 100 C ATOM 2975 CG GLU B 349 39.389 9.335 5.496 1.00 31.74 C ANISOU 2975 CG GLU B 349 3974 4161 3923 315 321 79 C ATOM 2976 CD GLU B 349 40.787 9.931 5.673 1.00 39.11 C ANISOU 2976 CD GLU B 349 4885 5144 4832 281 401 54 C ATOM 2977 OE1 GLU B 349 40.910 11.059 6.208 1.00 34.90 O ANISOU 2977 OE1 GLU B 349 4338 4604 4318 225 476 55 O ATOM 2978 OE2 GLU B 349 41.768 9.261 5.271 1.00 40.00 O ANISOU 2978 OE2 GLU B 349 4992 5304 4902 309 391 31 O ATOM 2979 N VAL B 350 37.052 6.980 5.956 1.00 15.44 N ANISOU 2979 N VAL B 350 1920 2042 1905 353 119 93 N ATOM 2980 CA VAL B 350 37.284 5.606 6.371 1.00 16.35 C ANISOU 2980 CA VAL B 350 2036 2173 2003 362 55 71 C ATOM 2981 C VAL B 350 38.786 5.416 6.572 1.00 21.35 C ANISOU 2981 C VAL B 350 2655 2858 2598 367 89 41 C ATOM 2982 O VAL B 350 39.550 5.475 5.621 1.00 18.06 O ANISOU 2982 O VAL B 350 2261 2465 2138 406 107 37 O ATOM 2983 CB VAL B 350 36.777 4.599 5.316 1.00 16.56 C ANISOU 2983 CB VAL B 350 2114 2181 1997 415 -26 78 C ATOM 2984 CG1 VAL B 350 37.095 3.180 5.745 1.00 14.82 C ANISOU 2984 CG1 VAL B 350 1910 1971 1751 426 -86 54 C ATOM 2985 CG2 VAL B 350 35.287 4.764 5.102 1.00 18.57 C ANISOU 2985 CG2 VAL B 350 2374 2395 2288 409 -64 104 C ATOM 2986 N LEU B 351 39.205 5.207 7.816 1.00 17.77 N ANISOU 2986 N LEU B 351 2164 2428 2160 330 100 18 N ATOM 2987 CA LEU B 351 40.630 5.139 8.146 1.00 15.19 C ANISOU 2987 CA LEU B 351 1809 2161 1800 331 135 -13 C ATOM 2988 C LEU B 351 41.198 3.731 7.975 1.00 16.04 C ANISOU 2988 C LEU B 351 1942 2294 1858 387 72 -35 C ATOM 2989 O LEU B 351 42.316 3.555 7.491 1.00 17.19 O ANISOU 2989 O LEU B 351 2085 2491 1957 423 89 -53 O ATOM 2990 CB LEU B 351 40.867 5.645 9.575 1.00 16.88 C ANISOU 2990 CB LEU B 351 1972 2391 2049 268 177 -29 C ATOM 2991 CG LEU B 351 40.359 7.075 9.791 1.00 16.03 C ANISOU 2991 CG LEU B 351 1850 2257 1986 214 245 -8 C ATOM 2992 CD1 LEU B 351 40.370 7.458 11.267 1.00 19.58 C ANISOU 2992 CD1 LEU B 351 2258 2708 2472 151 276 -20 C ATOM 2993 CD2 LEU B 351 41.180 8.053 8.955 1.00 19.50 C ANISOU 2993 CD2 LEU B 351 2289 2721 2398 214 317 -8 C ATOM 2994 N GLN B 352 40.423 2.730 8.374 1.00 10.25 N ANISOU 2994 N GLN B 352 1237 1526 1132 392 2 -33 N ATOM 2995 CA GLN B 352 40.809 1.342 8.174 1.00 15.61 C ANISOU 2995 CA GLN B 352 1959 2214 1759 448 -62 -50 C ATOM 2996 C GLN B 352 39.584 0.494 7.911 1.00 14.06 C ANISOU 2996 C GLN B 352 1817 1958 1569 454 -136 -34 C ATOM 2997 O GLN B 352 38.484 0.831 8.344 1.00 15.38 O ANISOU 2997 O GLN B 352 1971 2085 1787 406 -141 -18 O ATOM 2998 CB GLN B 352 41.526 0.788 9.405 1.00 16.26 C ANISOU 2998 CB GLN B 352 2018 2330 1829 441 -66 -82 C ATOM 2999 CG GLN B 352 42.956 1.246 9.593 1.00 26.67 C ANISOU 2999 CG GLN B 352 3285 3726 3122 450 -10 -108 C ATOM 3000 CD GLN B 352 43.535 0.719 10.891 1.00 46.11 C ANISOU 3000 CD GLN B 352 5725 6221 5576 444 -21 -138 C ATOM 3001 OE1 GLN B 352 43.119 1.132 11.974 1.00 53.14 O ANISOU 3001 OE1 GLN B 352 6587 7093 6510 385 -4 -139 O ATOM 3002 NE2 GLN B 352 44.483 -0.211 10.792 1.00 47.31 N ANISOU 3002 NE2 GLN B 352 5891 6418 5666 510 -50 -163 N ATOM 3003 N GLU B 353 39.787 -0.622 7.222 1.00 13.26 N ANISOU 3003 N GLU B 353 1776 1851 1412 511 -192 -41 N ATOM 3004 CA GLU B 353 38.709 -1.548 6.931 1.00 16.66 C ANISOU 3004 CA GLU B 353 2266 2227 1837 514 -267 -30 C ATOM 3005 C GLU B 353 39.239 -2.977 6.942 1.00 20.90 C ANISOU 3005 C GLU B 353 2868 2763 2309 564 -321 -52 C ATOM 3006 O GLU B 353 40.158 -3.309 6.204 1.00 24.79 O ANISOU 3006 O GLU B 353 3387 3285 2745 629 -321 -61 O ATOM 3007 CB GLU B 353 38.047 -1.213 5.581 1.00 17.46 C ANISOU 3007 CB GLU B 353 2394 2304 1937 533 -282 -4 C ATOM 3008 CG GLU B 353 36.879 -2.129 5.239 1.00 19.49 C ANISOU 3008 CG GLU B 353 2706 2509 2188 528 -362 5 C ATOM 3009 CD GLU B 353 36.007 -1.621 4.095 1.00 31.19 C ANISOU 3009 CD GLU B 353 4200 3969 3682 535 -378 32 C ATOM 3010 OE1 GLU B 353 36.416 -0.674 3.383 1.00 31.20 O ANISOU 3010 OE1 GLU B 353 4184 3988 3681 559 -330 44 O ATOM 3011 OE2 GLU B 353 34.903 -2.186 3.907 1.00 32.21 O ANISOU 3011 OE2 GLU B 353 4357 4062 3819 515 -439 39 O ATOM 3012 N TRP B 354 38.668 -3.808 7.805 1.00 14.95 N ANISOU 3012 N TRP B 354 2144 1976 1561 536 -364 -61 N ATOM 3013 CA TRP B 354 39.071 -5.204 7.933 1.00 21.59 C ANISOU 3013 CA TRP B 354 3062 2805 2337 582 -416 -81 C ATOM 3014 C TRP B 354 37.954 -6.121 7.458 1.00 18.65 C ANISOU 3014 C TRP B 354 2767 2369 1950 569 -486 -72 C ATOM 3015 O TRP B 354 36.838 -6.038 7.959 1.00 17.98 O ANISOU 3015 O TRP B 354 2669 2248 1914 501 -500 -63 O ATOM 3016 CB TRP B 354 39.354 -5.550 9.398 1.00 18.56 C ANISOU 3016 CB TRP B 354 2667 2427 1959 558 -410 -103 C ATOM 3017 CG TRP B 354 40.454 -4.775 10.050 1.00 22.45 C ANISOU 3017 CG TRP B 354 3083 2984 2461 564 -348 -119 C ATOM 3018 CD1 TRP B 354 41.792 -5.010 9.943 1.00 28.82 C ANISOU 3018 CD1 TRP B 354 3885 3851 3214 630 -335 -141 C ATOM 3019 CD2 TRP B 354 40.313 -3.659 10.939 1.00 26.69 C ANISOU 3019 CD2 TRP B 354 3540 3538 3065 498 -293 -116 C ATOM 3020 NE1 TRP B 354 42.495 -4.102 10.698 1.00 29.51 N ANISOU 3020 NE1 TRP B 354 3888 3995 3330 605 -276 -153 N ATOM 3021 CE2 TRP B 354 41.610 -3.262 11.322 1.00 26.36 C ANISOU 3021 CE2 TRP B 354 3446 3565 3003 523 -249 -138 C ATOM 3022 CE3 TRP B 354 39.214 -2.954 11.449 1.00 20.86 C ANISOU 3022 CE3 TRP B 354 2767 2763 2397 422 -275 -97 C ATOM 3023 CZ2 TRP B 354 41.842 -2.195 12.186 1.00 26.70 C ANISOU 3023 CZ2 TRP B 354 3413 3639 3094 468 -189 -142 C ATOM 3024 CZ3 TRP B 354 39.444 -1.894 12.304 1.00 20.32 C ANISOU 3024 CZ3 TRP B 354 2625 2720 2374 375 -214 -99 C ATOM 3025 CH2 TRP B 354 40.750 -1.524 12.664 1.00 24.24 C ANISOU 3025 CH2 TRP B 354 3080 3282 2850 395 -172 -122 C ATOM 3026 N PRO B 355 38.254 -7.016 6.508 1.00 17.38 N ANISOU 3026 N PRO B 355 2687 2196 1721 631 -530 -75 N ATOM 3027 CA PRO B 355 37.263 -8.029 6.133 1.00 19.94 C ANISOU 3027 CA PRO B 355 3096 2458 2021 614 -600 -71 C ATOM 3028 C PRO B 355 36.898 -8.891 7.329 1.00 19.21 C ANISOU 3028 C PRO B 355 3044 2329 1926 573 -626 -88 C ATOM 3029 O PRO B 355 37.769 -9.256 8.119 1.00 13.99 O ANISOU 3029 O PRO B 355 2393 1687 1235 604 -611 -108 O ATOM 3030 CB PRO B 355 38.003 -8.885 5.091 1.00 19.81 C ANISOU 3030 CB PRO B 355 3168 2441 1918 701 -632 -78 C ATOM 3031 CG PRO B 355 39.061 -7.980 4.531 1.00 21.41 C ANISOU 3031 CG PRO B 355 3312 2707 2118 753 -575 -74 C ATOM 3032 CD PRO B 355 39.475 -7.091 5.686 1.00 23.77 C ANISOU 3032 CD PRO B 355 3513 3049 2471 716 -514 -82 C ATOM 3033 N LEU B 356 35.622 -9.224 7.465 1.00 17.27 N ANISOU 3033 N LEU B 356 2821 2034 1707 504 -663 -81 N ATOM 3034 CA LEU B 356 35.225 -10.122 8.538 1.00 18.28 C ANISOU 3034 CA LEU B 356 3000 2119 1825 461 -687 -98 C ATOM 3035 C LEU B 356 36.044 -11.417 8.538 1.00 23.47 C ANISOU 3035 C LEU B 356 3772 2756 2388 528 -720 -119 C ATOM 3036 O LEU B 356 36.222 -12.037 9.584 1.00 29.32 O ANISOU 3036 O LEU B 356 4554 3477 3109 519 -722 -137 O ATOM 3037 CB LEU B 356 33.736 -10.438 8.456 1.00 17.97 C ANISOU 3037 CB LEU B 356 2980 2032 1815 378 -728 -90 C ATOM 3038 CG LEU B 356 32.837 -9.379 9.079 1.00 26.22 C ANISOU 3038 CG LEU B 356 3919 3090 2955 301 -692 -76 C ATOM 3039 CD1 LEU B 356 31.383 -9.754 8.891 1.00 31.07 C ANISOU 3039 CD1 LEU B 356 4546 3666 3591 225 -737 -71 C ATOM 3040 CD2 LEU B 356 33.170 -9.221 10.561 1.00 22.15 C ANISOU 3040 CD2 LEU B 356 3373 2579 2465 273 -649 -89 C ATOM 3041 N THR B 357 36.547 -11.823 7.377 1.00 27.08 N ANISOU 3041 N THR B 357 4288 3218 2784 600 -745 -117 N ATOM 3042 CA THR B 357 37.299 -13.076 7.289 1.00 32.23 C ANISOU 3042 CA THR B 357 5058 3848 3339 673 -778 -136 C ATOM 3043 C THR B 357 38.707 -12.951 7.876 1.00 34.12 C ANISOU 3043 C THR B 357 5269 4145 3550 749 -738 -152 C ATOM 3044 O THR B 357 39.418 -13.949 8.014 1.00 38.97 O ANISOU 3044 O THR B 357 5974 4749 4085 820 -760 -170 O ATOM 3045 CB THR B 357 37.372 -13.635 5.839 1.00 24.26 C ANISOU 3045 CB THR B 357 4132 2821 2266 730 -819 -129 C ATOM 3046 OG1 THR B 357 38.100 -12.731 4.998 1.00 26.48 O ANISOU 3046 OG1 THR B 357 4343 3161 2556 786 -783 -117 O ATOM 3047 CG2 THR B 357 35.977 -13.841 5.266 1.00 28.39 C ANISOU 3047 CG2 THR B 357 4686 3290 2809 653 -866 -117 C ATOM 3048 N THR B 358 39.112 -11.731 8.218 1.00 26.20 N ANISOU 3048 N THR B 358 4142 3203 2609 737 -681 -148 N ATOM 3049 CA THR B 358 40.390 -11.533 8.901 1.00 24.25 C ANISOU 3049 CA THR B 358 3852 3020 2343 794 -642 -167 C ATOM 3050 C THR B 358 40.205 -11.434 10.419 1.00 27.63 C ANISOU 3050 C THR B 358 4249 3441 2809 739 -625 -179 C ATOM 3051 O THR B 358 41.177 -11.311 11.165 1.00 27.38 O ANISOU 3051 O THR B 358 4181 3459 2761 778 -598 -198 O ATOM 3052 CB THR B 358 41.155 -10.294 8.381 1.00 29.93 C ANISOU 3052 CB THR B 358 4460 3817 3094 817 -585 -160 C ATOM 3053 OG1 THR B 358 40.503 -9.092 8.822 1.00 25.73 O ANISOU 3053 OG1 THR B 358 3829 3292 2654 731 -544 -145 O ATOM 3054 CG2 THR B 358 41.242 -10.313 6.848 1.00 28.97 C ANISOU 3054 CG2 THR B 358 4371 3697 2940 866 -598 -145 C ATOM 3055 N VAL B 359 38.956 -11.488 10.874 1.00 25.36 N ANISOU 3055 N VAL B 359 3974 3095 2568 649 -640 -169 N ATOM 3056 CA VAL B 359 38.674 -11.429 12.301 1.00 27.43 C ANISOU 3056 CA VAL B 359 4216 3341 2865 592 -624 -180 C ATOM 3057 C VAL B 359 38.694 -12.825 12.901 1.00 27.25 C ANISOU 3057 C VAL B 359 4320 3263 2770 614 -666 -199 C ATOM 3058 O VAL B 359 37.859 -13.662 12.561 1.00 30.31 O ANISOU 3058 O VAL B 359 4800 3583 3132 584 -710 -196 O ATOM 3059 CB VAL B 359 37.308 -10.788 12.596 1.00 28.89 C ANISOU 3059 CB VAL B 359 4348 3493 3137 483 -613 -161 C ATOM 3060 CG1 VAL B 359 36.961 -10.958 14.065 1.00 21.10 C ANISOU 3060 CG1 VAL B 359 3366 2478 2174 426 -600 -173 C ATOM 3061 CG2 VAL B 359 37.313 -9.310 12.204 1.00 29.57 C ANISOU 3061 CG2 VAL B 359 4310 3630 3293 463 -562 -142 C ATOM 3062 N LYS B 360 39.651 -13.072 13.793 1.00 20.41 N ANISOU 3062 N LYS B 360 3463 2425 1867 666 -654 -221 N ATOM 3063 CA LYS B 360 39.796 -14.378 14.426 1.00 26.68 C ANISOU 3063 CA LYS B 360 4387 3168 2583 700 -690 -241 C ATOM 3064 C LYS B 360 38.852 -14.561 15.608 1.00 28.79 C ANISOU 3064 C LYS B 360 4680 3374 2887 607 -688 -243 C ATOM 3065 O LYS B 360 38.340 -15.662 15.825 1.00 36.86 O ANISOU 3065 O LYS B 360 5827 4320 3858 592 -724 -251 O ATOM 3066 CB LYS B 360 41.239 -14.605 14.875 1.00 41.94 C ANISOU 3066 CB LYS B 360 6321 5161 4453 807 -682 -264 C ATOM 3067 CG LYS B 360 41.527 -16.026 15.352 1.00 50.35 C ANISOU 3067 CG LYS B 360 7538 6174 5419 870 -723 -284 C ATOM 3068 CD LYS B 360 42.966 -16.159 15.827 1.00 55.17 C ANISOU 3068 CD LYS B 360 8134 6858 5970 982 -715 -309 C ATOM 3069 CE LYS B 360 43.268 -17.570 16.292 1.00 60.03 C ANISOU 3069 CE LYS B 360 8910 7420 6479 1057 -756 -328 C ATOM 3070 NZ LYS B 360 44.664 -17.690 16.795 1.00 63.79 N ANISOU 3070 NZ LYS B 360 9366 7976 6896 1174 -752 -354 N ATOM 3071 N ARG B 361 38.637 -13.489 16.374 1.00 20.32 N ANISOU 3071 N ARG B 361 3494 2330 1896 544 -643 -238 N ATOM 3072 CA ARG B 361 37.682 -13.501 17.486 1.00 23.69 C ANISOU 3072 CA ARG B 361 3929 2703 2367 450 -632 -238 C ATOM 3073 C ARG B 361 37.468 -12.099 18.055 1.00 23.04 C ANISOU 3073 C ARG B 361 3708 2664 2383 387 -576 -227 C ATOM 3074 O ARG B 361 38.123 -11.144 17.641 1.00 25.64 O ANISOU 3074 O ARG B 361 3941 3063 2739 417 -546 -222 O ATOM 3075 CB ARG B 361 38.152 -14.444 18.596 1.00 29.06 C ANISOU 3075 CB ARG B 361 4710 3350 2981 485 -645 -263 C ATOM 3076 CG ARG B 361 39.541 -14.119 19.094 1.00 32.54 C ANISOU 3076 CG ARG B 361 5103 3867 3394 571 -625 -281 C ATOM 3077 CD ARG B 361 40.032 -15.096 20.150 1.00 34.08 C ANISOU 3077 CD ARG B 361 5406 4031 3514 620 -644 -306 C ATOM 3078 NE ARG B 361 41.327 -14.667 20.667 1.00 32.79 N ANISOU 3078 NE ARG B 361 5176 3952 3331 697 -625 -325 N ATOM 3079 CZ ARG B 361 41.913 -15.158 21.752 1.00 35.05 C ANISOU 3079 CZ ARG B 361 5514 4236 3565 743 -632 -348 C ATOM 3080 NH1 ARG B 361 41.324 -16.114 22.457 1.00 35.40 N ANISOU 3080 NH1 ARG B 361 5690 4191 3570 720 -654 -355 N ATOM 3081 NH2 ARG B 361 43.092 -14.682 22.134 1.00 37.14 N ANISOU 3081 NH2 ARG B 361 5702 4593 3817 810 -617 -367 N ATOM 3082 N TRP B 362 36.543 -11.982 19.002 1.00 20.64 N ANISOU 3082 N TRP B 362 3400 2315 2127 299 -560 -224 N ATOM 3083 CA TRP B 362 36.263 -10.701 19.644 1.00 23.44 C ANISOU 3083 CA TRP B 362 3636 2701 2571 238 -506 -214 C ATOM 3084 C TRP B 362 35.839 -10.914 21.085 1.00 23.31 C ANISOU 3084 C TRP B 362 3649 2640 2568 181 -489 -224 C ATOM 3085 O TRP B 362 35.378 -11.994 21.448 1.00 26.94 O ANISOU 3085 O TRP B 362 4217 3034 2986 162 -519 -234 O ATOM 3086 CB TRP B 362 35.171 -9.933 18.890 1.00 24.14 C ANISOU 3086 CB TRP B 362 3653 2786 2733 172 -495 -187 C ATOM 3087 CG TRP B 362 33.928 -10.738 18.692 1.00 29.24 C ANISOU 3087 CG TRP B 362 4367 3365 3377 110 -531 -182 C ATOM 3088 CD1 TRP B 362 32.848 -10.797 19.522 1.00 25.12 C ANISOU 3088 CD1 TRP B 362 3848 2798 2898 19 -518 -180 C ATOM 3089 CD2 TRP B 362 33.647 -11.624 17.603 1.00 29.47 C ANISOU 3089 CD2 TRP B 362 4475 3366 3356 129 -584 -181 C ATOM 3090 NE1 TRP B 362 31.907 -11.663 19.014 1.00 29.03 N ANISOU 3090 NE1 TRP B 362 4413 3243 3374 -24 -560 -179 N ATOM 3091 CE2 TRP B 362 32.374 -12.183 17.836 1.00 32.25 C ANISOU 3091 CE2 TRP B 362 4871 3659 3724 42 -603 -180 C ATOM 3092 CE3 TRP B 362 34.346 -11.994 16.448 1.00 30.58 C ANISOU 3092 CE3 TRP B 362 4654 3527 3438 210 -616 -181 C ATOM 3093 CZ2 TRP B 362 31.782 -13.089 16.955 1.00 36.41 C ANISOU 3093 CZ2 TRP B 362 5479 4146 4209 28 -655 -180 C ATOM 3094 CZ3 TRP B 362 33.759 -12.895 15.574 1.00 32.98 C ANISOU 3094 CZ3 TRP B 362 5044 3787 3700 202 -667 -180 C ATOM 3095 CH2 TRP B 362 32.488 -13.432 15.833 1.00 33.00 C ANISOU 3095 CH2 TRP B 362 5089 3730 3718 110 -688 -180 C ATOM 3096 N ALA B 363 36.004 -9.874 21.899 1.00 16.53 N ANISOU 3096 N ALA B 363 2701 1815 1767 151 -440 -222 N ATOM 3097 CA ALA B 363 35.587 -9.908 23.292 1.00 20.40 C ANISOU 3097 CA ALA B 363 3208 2265 2277 94 -416 -230 C ATOM 3098 C ALA B 363 34.883 -8.615 23.709 1.00 17.35 C ANISOU 3098 C ALA B 363 2713 1891 1988 16 -361 -211 C ATOM 3099 O ALA B 363 35.148 -7.534 23.183 1.00 19.06 O ANISOU 3099 O ALA B 363 2833 2161 2246 23 -333 -198 O ATOM 3100 CB ALA B 363 36.781 -10.166 24.191 1.00 21.82 C ANISOU 3100 CB ALA B 363 3418 2470 2403 157 -415 -256 C ATOM 3101 N ALA B 364 33.980 -8.733 24.667 1.00 22.88 N ANISOU 3101 N ALA B 364 3435 2539 2720 -59 -344 -210 N ATOM 3102 CA ALA B 364 33.332 -7.565 25.224 1.00 20.97 C ANISOU 3102 CA ALA B 364 3101 2304 2563 -127 -289 -193 C ATOM 3103 C ALA B 364 33.297 -7.645 26.741 1.00 25.10 C ANISOU 3103 C ALA B 364 3655 2794 3089 -163 -261 -207 C ATOM 3104 O ALA B 364 33.167 -8.725 27.318 1.00 27.92 O ANISOU 3104 O ALA B 364 4115 3098 3398 -168 -285 -223 O ATOM 3105 CB ALA B 364 31.926 -7.428 24.674 1.00 18.84 C ANISOU 3105 CB ALA B 364 2803 2008 2347 -195 -289 -171 C ATOM 3106 N SER B 365 33.429 -6.486 27.371 1.00 20.03 N ANISOU 3106 N SER B 365 2931 2179 2500 -187 -209 -200 N ATOM 3107 CA SER B 365 33.221 -6.337 28.797 1.00 26.17 C ANISOU 3107 CA SER B 365 3724 2924 3295 -233 -173 -208 C ATOM 3108 C SER B 365 32.166 -5.261 28.867 1.00 30.39 C ANISOU 3108 C SER B 365 4174 3455 3918 -304 -123 -182 C ATOM 3109 O SER B 365 31.768 -4.734 27.836 1.00 26.85 O ANISOU 3109 O SER B 365 3664 3032 3504 -306 -122 -162 O ATOM 3110 CB SER B 365 34.502 -5.863 29.482 1.00 22.45 C ANISOU 3110 CB SER B 365 3232 2498 2799 -187 -156 -226 C ATOM 3111 OG SER B 365 34.840 -4.549 29.060 1.00 25.41 O ANISOU 3111 OG SER B 365 3500 2931 3221 -187 -118 -213 O ATOM 3112 N PRO B 366 31.695 -4.930 30.071 1.00 30.98 N ANISOU 3112 N PRO B 366 4248 3498 4026 -360 -80 -181 N ATOM 3113 CA PRO B 366 30.678 -3.875 30.128 1.00 24.23 C ANISOU 3113 CA PRO B 366 3312 2643 3254 -420 -30 -155 C ATOM 3114 C PRO B 366 31.218 -2.504 29.725 1.00 19.51 C ANISOU 3114 C PRO B 366 2621 2101 2691 -398 7 -142 C ATOM 3115 O PRO B 366 30.450 -1.551 29.627 1.00 17.98 O ANISOU 3115 O PRO B 366 2360 1911 2559 -434 48 -118 O ATOM 3116 CB PRO B 366 30.268 -3.869 31.605 1.00 30.62 C ANISOU 3116 CB PRO B 366 4151 3404 4078 -474 10 -162 C ATOM 3117 CG PRO B 366 30.590 -5.261 32.090 1.00 33.57 C ANISOU 3117 CG PRO B 366 4641 3734 4379 -459 -32 -187 C ATOM 3118 CD PRO B 366 31.843 -5.642 31.352 1.00 34.14 C ANISOU 3118 CD PRO B 366 4734 3850 4389 -373 -79 -202 C ATOM 3119 N LYS B 367 32.521 -2.395 29.500 1.00 20.47 N ANISOU 3119 N LYS B 367 2740 2268 2770 -339 -6 -157 N ATOM 3120 CA LYS B 367 33.097 -1.087 29.229 1.00 15.99 C ANISOU 3120 CA LYS B 367 2093 1753 2232 -328 35 -148 C ATOM 3121 C LYS B 367 34.063 -1.073 28.045 1.00 10.86 C ANISOU 3121 C LYS B 367 1422 1159 1545 -263 7 -153 C ATOM 3122 O LYS B 367 34.621 -0.032 27.700 1.00 16.68 O ANISOU 3122 O LYS B 367 2098 1941 2298 -254 42 -148 O ATOM 3123 CB LYS B 367 33.785 -0.536 30.480 1.00 26.49 C ANISOU 3123 CB LYS B 367 3418 3089 3559 -342 74 -164 C ATOM 3124 CG LYS B 367 32.859 -0.348 31.670 1.00 36.60 C ANISOU 3124 CG LYS B 367 4714 4314 4879 -407 114 -156 C ATOM 3125 CD LYS B 367 33.549 0.438 32.766 1.00 43.51 C ANISOU 3125 CD LYS B 367 5575 5201 5757 -422 157 -169 C ATOM 3126 CE LYS B 367 32.549 0.944 33.790 1.00 50.16 C ANISOU 3126 CE LYS B 367 6417 5991 6650 -488 210 -154 C ATOM 3127 NZ LYS B 367 33.139 2.020 34.631 1.00 53.59 N ANISOU 3127 NZ LYS B 367 6824 6440 7096 -507 262 -160 N ATOM 3128 N SER B 368 34.258 -2.215 27.406 1.00 13.41 N ANISOU 3128 N SER B 368 1801 1479 1817 -220 -51 -163 N ATOM 3129 CA SER B 368 35.205 -2.244 26.308 1.00 17.52 C ANISOU 3129 CA SER B 368 2305 2053 2298 -154 -76 -169 C ATOM 3130 C SER B 368 34.825 -3.282 25.279 1.00 18.95 C ANISOU 3130 C SER B 368 2538 2216 2446 -124 -133 -165 C ATOM 3131 O SER B 368 34.018 -4.172 25.548 1.00 18.61 O ANISOU 3131 O SER B 368 2556 2119 2396 -151 -160 -166 O ATOM 3132 CB SER B 368 36.617 -2.528 26.830 1.00 17.40 C ANISOU 3132 CB SER B 368 2306 2081 2224 -103 -87 -201 C ATOM 3133 OG SER B 368 36.720 -3.868 27.287 1.00 19.20 O ANISOU 3133 OG SER B 368 2626 2275 2394 -75 -135 -220 O ATOM 3134 N PHE B 369 35.426 -3.154 24.102 1.00 15.17 N ANISOU 3134 N PHE B 369 2037 1781 1945 -72 -149 -162 N ATOM 3135 CA PHE B 369 35.267 -4.117 23.030 1.00 14.05 C ANISOU 3135 CA PHE B 369 1949 1629 1763 -32 -204 -161 C ATOM 3136 C PHE B 369 36.594 -4.319 22.314 1.00 11.33 C ANISOU 3136 C PHE B 369 1606 1340 1358 50 -223 -176 C ATOM 3137 O PHE B 369 37.295 -3.352 22.025 1.00 12.34 O ANISOU 3137 O PHE B 369 1666 1522 1500 64 -187 -175 O ATOM 3138 CB PHE B 369 34.212 -3.655 22.018 1.00 11.90 C ANISOU 3138 CB PHE B 369 1639 1344 1537 -60 -204 -131 C ATOM 3139 CG PHE B 369 34.034 -4.608 20.884 1.00 12.05 C ANISOU 3139 CG PHE B 369 1714 1352 1513 -24 -263 -130 C ATOM 3140 CD1 PHE B 369 33.270 -5.753 21.043 1.00 17.86 C ANISOU 3140 CD1 PHE B 369 2526 2033 2227 -49 -306 -136 C ATOM 3141 CD2 PHE B 369 34.657 -4.385 19.664 1.00 13.85 C ANISOU 3141 CD2 PHE B 369 1925 1621 1717 34 -273 -125 C ATOM 3142 CE1 PHE B 369 33.115 -6.649 20.002 1.00 18.81 C ANISOU 3142 CE1 PHE B 369 2706 2138 2302 -20 -361 -136 C ATOM 3143 CE2 PHE B 369 34.509 -5.287 18.621 1.00 13.32 C ANISOU 3143 CE2 PHE B 369 1917 1539 1606 69 -328 -124 C ATOM 3144 CZ PHE B 369 33.739 -6.421 18.794 1.00 14.66 C ANISOU 3144 CZ PHE B 369 2164 1654 1754 42 -373 -130 C ATOM 3145 N THR B 370 36.920 -5.569 21.999 1.00 13.70 N ANISOU 3145 N THR B 370 1989 1627 1590 103 -278 -191 N ATOM 3146 CA THR B 370 38.224 -5.889 21.428 1.00 13.13 C ANISOU 3146 CA THR B 370 1926 1610 1453 189 -297 -209 C ATOM 3147 C THR B 370 38.125 -6.871 20.285 1.00 16.46 C ANISOU 3147 C THR B 370 2418 2014 1824 239 -350 -205 C ATOM 3148 O THR B 370 37.365 -7.836 20.354 1.00 13.21 O ANISOU 3148 O THR B 370 2088 1539 1392 222 -388 -205 O ATOM 3149 CB THR B 370 39.150 -6.496 22.489 1.00 17.70 C ANISOU 3149 CB THR B 370 2545 2204 1977 230 -308 -240 C ATOM 3150 OG1 THR B 370 39.270 -5.583 23.579 1.00 17.93 O ANISOU 3150 OG1 THR B 370 2512 2250 2050 182 -260 -244 O ATOM 3151 CG2 THR B 370 40.526 -6.771 21.907 1.00 16.53 C ANISOU 3151 CG2 THR B 370 2392 2126 1762 325 -325 -259 C ATOM 3152 N LEU B 371 38.905 -6.612 19.237 1.00 16.02 N ANISOU 3152 N LEU B 371 2332 2012 1744 298 -350 -205 N ATOM 3153 CA LEU B 371 38.980 -7.482 18.075 1.00 15.63 C ANISOU 3153 CA LEU B 371 2349 1952 1639 356 -398 -202 C ATOM 3154 C LEU B 371 40.363 -8.113 17.954 1.00 14.51 C ANISOU 3154 C LEU B 371 2239 1860 1416 455 -417 -228 C ATOM 3155 O LEU B 371 41.371 -7.446 18.161 1.00 19.09 O ANISOU 3155 O LEU B 371 2746 2511 1994 481 -382 -241 O ATOM 3156 CB LEU B 371 38.675 -6.695 16.798 1.00 18.07 C ANISOU 3156 CB LEU B 371 2604 2279 1982 350 -384 -178 C ATOM 3157 CG LEU B 371 37.213 -6.359 16.487 1.00 18.90 C ANISOU 3157 CG LEU B 371 2698 2334 2148 277 -386 -151 C ATOM 3158 CD1 LEU B 371 37.139 -5.226 15.486 1.00 23.87 C ANISOU 3158 CD1 LEU B 371 3255 2997 2817 276 -354 -129 C ATOM 3159 CD2 LEU B 371 36.471 -7.571 15.967 1.00 13.43 C ANISOU 3159 CD2 LEU B 371 2102 1584 1418 279 -448 -149 C ATOM 3160 N ASP B 372 40.390 -9.397 17.604 1.00 17.69 N ANISOU 3160 N ASP B 372 2748 2225 1746 508 -470 -236 N ATOM 3161 CA ASP B 372 41.627 -10.137 17.357 1.00 22.62 C ANISOU 3161 CA ASP B 372 3417 2893 2283 615 -494 -258 C ATOM 3162 C ASP B 372 41.703 -10.532 15.881 1.00 21.62 C ANISOU 3162 C ASP B 372 3330 2767 2118 669 -521 -247 C ATOM 3163 O ASP B 372 40.873 -11.306 15.400 1.00 21.08 O ANISOU 3163 O ASP B 372 3350 2630 2031 654 -561 -237 O ATOM 3164 CB ASP B 372 41.651 -11.388 18.239 1.00 30.14 C ANISOU 3164 CB ASP B 372 4485 3796 3172 645 -533 -278 C ATOM 3165 CG ASP B 372 42.902 -12.242 18.047 1.00 30.71 C ANISOU 3165 CG ASP B 372 4613 3909 3145 768 -561 -302 C ATOM 3166 OD1 ASP B 372 43.693 -12.004 17.105 1.00 28.06 O ANISOU 3166 OD1 ASP B 372 4235 3638 2786 832 -555 -303 O ATOM 3167 OD2 ASP B 372 43.085 -13.177 18.857 1.00 31.88 O ANISOU 3167 OD2 ASP B 372 4854 4025 3234 805 -589 -321 O ATOM 3168 N PHE B 373 42.697 -10.003 15.166 1.00 22.06 N ANISOU 3168 N PHE B 373 3322 2901 2160 727 -498 -251 N ATOM 3169 CA PHE B 373 42.839 -10.261 13.729 1.00 24.60 C ANISOU 3169 CA PHE B 373 3674 3227 2445 780 -516 -240 C ATOM 3170 C PHE B 373 43.831 -11.377 13.399 1.00 28.43 C ANISOU 3170 C PHE B 373 4241 3733 2828 896 -551 -260 C ATOM 3171 O PHE B 373 44.351 -11.441 12.280 1.00 25.45 O ANISOU 3171 O PHE B 373 3868 3387 2414 959 -553 -256 O ATOM 3172 CB PHE B 373 43.252 -8.989 12.989 1.00 22.07 C ANISOU 3172 CB PHE B 373 3243 2973 2169 771 -464 -229 C ATOM 3173 CG PHE B 373 42.311 -7.839 13.186 1.00 28.22 C ANISOU 3173 CG PHE B 373 3949 3733 3042 669 -427 -207 C ATOM 3174 CD1 PHE B 373 41.070 -7.832 12.579 1.00 28.86 C ANISOU 3174 CD1 PHE B 373 4059 3749 3157 619 -448 -181 C ATOM 3175 CD2 PHE B 373 42.673 -6.758 13.978 1.00 28.39 C ANISOU 3175 CD2 PHE B 373 3872 3801 3114 626 -372 -213 C ATOM 3176 CE1 PHE B 373 40.204 -6.771 12.757 1.00 30.40 C ANISOU 3176 CE1 PHE B 373 4186 3930 3434 536 -414 -161 C ATOM 3177 CE2 PHE B 373 41.818 -5.697 14.156 1.00 25.37 C ANISOU 3177 CE2 PHE B 373 3429 3397 2812 540 -335 -192 C ATOM 3178 CZ PHE B 373 40.575 -5.703 13.544 1.00 26.30 C ANISOU 3178 CZ PHE B 373 3576 3453 2962 499 -356 -165 C ATOM 3179 N GLY B 374 44.089 -12.255 14.364 1.00 32.63 N ANISOU 3179 N GLY B 374 4842 4246 3310 930 -577 -281 N ATOM 3180 CA GLY B 374 44.972 -13.389 14.148 1.00 31.37 C ANISOU 3180 CA GLY B 374 4774 4099 3046 1048 -613 -300 C ATOM 3181 C GLY B 374 46.303 -13.005 13.526 1.00 33.47 C ANISOU 3181 C GLY B 374 4966 4472 3280 1137 -588 -313 C ATOM 3182 O GLY B 374 46.991 -12.109 14.012 1.00 30.08 O ANISOU 3182 O GLY B 374 4418 4124 2885 1127 -545 -326 O ATOM 3183 N GLU B 375 46.658 -13.678 12.437 1.00 33.41 N ANISOU 3183 N GLU B 375 5026 4463 3204 1220 -612 -310 N ATOM 3184 CA GLU B 375 47.955 -13.482 11.791 1.00 38.09 C ANISOU 3184 CA GLU B 375 5561 5157 3755 1316 -590 -324 C ATOM 3185 C GLU B 375 48.035 -12.233 10.908 1.00 39.44 C ANISOU 3185 C GLU B 375 5617 5380 3989 1271 -538 -308 C ATOM 3186 O GLU B 375 49.093 -11.929 10.357 1.00 35.63 O ANISOU 3186 O GLU B 375 5072 4986 3478 1335 -510 -320 O ATOM 3187 CB GLU B 375 48.310 -14.712 10.953 1.00 41.07 C ANISOU 3187 CB GLU B 375 6065 5510 4029 1428 -633 -327 C ATOM 3188 CG GLU B 375 48.605 -15.962 11.765 1.00 53.39 C ANISOU 3188 CG GLU B 375 7742 7040 5504 1506 -676 -348 C ATOM 3189 CD GLU B 375 48.129 -17.224 11.072 1.00 62.49 C ANISOU 3189 CD GLU B 375 9068 8098 6579 1553 -728 -338 C ATOM 3190 OE1 GLU B 375 48.937 -17.851 10.353 1.00 69.13 O ANISOU 3190 OE1 GLU B 375 9962 8969 7335 1671 -741 -346 O ATOM 3191 OE2 GLU B 375 46.939 -17.579 11.234 1.00 62.10 O ANISOU 3191 OE2 GLU B 375 9100 7944 6551 1470 -754 -324 O ATOM 3192 N TYR B 376 46.927 -11.511 10.777 1.00 35.32 N ANISOU 3192 N TYR B 376 5068 4804 3548 1163 -525 -283 N ATOM 3193 CA TYR B 376 46.861 -10.389 9.848 1.00 30.18 C ANISOU 3193 CA TYR B 376 4334 4183 2950 1123 -480 -264 C ATOM 3194 C TYR B 376 47.495 -9.100 10.367 1.00 30.62 C ANISOU 3194 C TYR B 376 4248 4325 3062 1079 -415 -275 C ATOM 3195 O TYR B 376 47.893 -8.239 9.581 1.00 37.67 O ANISOU 3195 O TYR B 376 5072 5268 3974 1074 -369 -268 O ATOM 3196 CB TYR B 376 45.414 -10.140 9.409 1.00 31.64 C ANISOU 3196 CB TYR B 376 4550 4279 3192 1035 -495 -233 C ATOM 3197 CG TYR B 376 44.884 -11.188 8.462 1.00 35.61 C ANISOU 3197 CG TYR B 376 5179 4712 3640 1075 -551 -220 C ATOM 3198 CD1 TYR B 376 44.123 -12.253 8.926 1.00 37.23 C ANISOU 3198 CD1 TYR B 376 5492 4834 3817 1060 -605 -222 C ATOM 3199 CD2 TYR B 376 45.154 -11.120 7.100 1.00 38.82 C ANISOU 3199 CD2 TYR B 376 5600 5132 4017 1123 -548 -209 C ATOM 3200 CE1 TYR B 376 43.638 -13.219 8.054 1.00 34.63 C ANISOU 3200 CE1 TYR B 376 5285 4440 3434 1089 -657 -213 C ATOM 3201 CE2 TYR B 376 44.676 -12.081 6.225 1.00 40.36 C ANISOU 3201 CE2 TYR B 376 5916 5262 4158 1158 -601 -199 C ATOM 3202 CZ TYR B 376 43.919 -13.130 6.705 1.00 36.01 C ANISOU 3202 CZ TYR B 376 5472 4630 3580 1139 -656 -201 C ATOM 3203 OH TYR B 376 43.439 -14.083 5.827 1.00 31.43 O ANISOU 3203 OH TYR B 376 5017 3983 2943 1166 -708 -193 O ATOM 3204 N GLN B 377 47.574 -8.954 11.682 1.00 32.28 N ANISOU 3204 N GLN B 377 4421 4548 3294 1044 -408 -291 N ATOM 3205 CA GLN B 377 48.318 -7.841 12.262 1.00 36.03 C ANISOU 3205 CA GLN B 377 4770 5112 3810 1009 -349 -308 C ATOM 3206 C GLN B 377 48.839 -8.176 13.667 1.00 36.37 C ANISOU 3206 C GLN B 377 4798 5188 3833 1024 -361 -338 C ATOM 3207 O GLN B 377 48.383 -9.129 14.300 1.00 31.40 O ANISOU 3207 O GLN B 377 4258 4495 3175 1040 -409 -340 O ATOM 3208 CB GLN B 377 47.511 -6.531 12.231 1.00 36.02 C ANISOU 3208 CB GLN B 377 4700 5083 3901 895 -302 -283 C ATOM 3209 CG GLN B 377 46.469 -6.354 13.322 1.00 41.73 C ANISOU 3209 CG GLN B 377 5433 5740 4684 809 -309 -274 C ATOM 3210 CD GLN B 377 45.785 -4.982 13.266 1.00 45.43 C ANISOU 3210 CD GLN B 377 5831 6193 5238 710 -256 -251 C ATOM 3211 OE1 GLN B 377 45.484 -4.466 12.186 1.00 39.81 O ANISOU 3211 OE1 GLN B 377 5111 5470 4544 700 -237 -229 O ATOM 3212 NE2 GLN B 377 45.542 -4.392 14.435 1.00 42.04 N ANISOU 3212 NE2 GLN B 377 5355 5760 4858 641 -230 -256 N ATOM 3213 N GLU B 378 49.808 -7.396 14.135 1.00 34.25 N ANISOU 3213 N GLU B 378 4420 5018 3575 1017 -316 -361 N ATOM 3214 CA GLU B 378 50.520 -7.715 15.367 1.00 46.57 C ANISOU 3214 CA GLU B 378 5958 6630 5105 1048 -329 -395 C ATOM 3215 C GLU B 378 49.653 -7.623 16.622 1.00 47.06 C ANISOU 3215 C GLU B 378 6042 6623 5214 969 -339 -390 C ATOM 3216 O GLU B 378 49.654 -8.537 17.450 1.00 51.73 O ANISOU 3216 O GLU B 378 6704 7187 5763 1011 -382 -404 O ATOM 3217 CB GLU B 378 51.763 -6.829 15.511 1.00 55.24 C ANISOU 3217 CB GLU B 378 6924 7859 6204 1049 -278 -424 C ATOM 3218 CG GLU B 378 52.752 -6.966 14.357 1.00 63.41 C ANISOU 3218 CG GLU B 378 7931 8976 7185 1133 -265 -434 C ATOM 3219 CD GLU B 378 53.992 -6.106 14.536 0.50 66.24 C ANISOU 3219 CD GLU B 378 8153 9472 7544 1126 -211 -467 C ATOM 3220 OE1 GLU B 378 54.147 -5.498 15.617 0.50 69.19 O ANISOU 3220 OE1 GLU B 378 8460 9879 7952 1064 -193 -485 O ATOM 3221 OE2 GLU B 378 54.813 -6.040 13.596 0.50 63.04 O ANISOU 3221 OE2 GLU B 378 7708 9143 7103 1179 -187 -476 O ATOM 3222 N SER B 379 48.911 -6.530 16.759 1.00 38.87 N ANISOU 3222 N SER B 379 4953 5555 4262 859 -296 -370 N ATOM 3223 CA SER B 379 48.196 -6.254 18.004 1.00 42.40 C ANISOU 3223 CA SER B 379 5401 5950 4758 780 -292 -367 C ATOM 3224 C SER B 379 46.674 -6.330 17.880 1.00 28.69 C ANISOU 3224 C SER B 379 3731 4098 3073 711 -305 -332 C ATOM 3225 O SER B 379 46.140 -6.390 16.781 1.00 29.16 O ANISOU 3225 O SER B 379 3820 4121 3139 713 -312 -308 O ATOM 3226 CB SER B 379 48.607 -4.880 18.536 1.00 50.62 C ANISOU 3226 CB SER B 379 6324 7054 5854 705 -229 -377 C ATOM 3227 OG SER B 379 48.798 -3.975 17.463 1.00 56.87 O ANISOU 3227 OG SER B 379 7053 7881 6672 682 -182 -364 O ATOM 3228 N TYR B 380 45.990 -6.335 19.022 1.00 28.28 N ANISOU 3228 N TYR B 380 3700 3992 3054 652 -309 -331 N ATOM 3229 CA TYR B 380 44.532 -6.279 19.057 1.00 25.53 C ANISOU 3229 CA TYR B 380 3393 3544 2761 575 -313 -300 C ATOM 3230 C TYR B 380 44.059 -4.846 18.811 1.00 24.48 C ANISOU 3230 C TYR B 380 3173 3417 2711 491 -254 -278 C ATOM 3231 O TYR B 380 44.827 -3.896 18.946 1.00 21.30 O ANISOU 3231 O TYR B 380 2684 3084 2324 476 -207 -290 O ATOM 3232 CB TYR B 380 43.994 -6.731 20.420 1.00 28.05 C ANISOU 3232 CB TYR B 380 3763 3808 3088 539 -329 -308 C ATOM 3233 CG TYR B 380 44.264 -8.174 20.823 1.00 27.90 C ANISOU 3233 CG TYR B 380 3853 3762 2988 614 -386 -328 C ATOM 3234 CD1 TYR B 380 44.565 -9.148 19.879 1.00 32.09 C ANISOU 3234 CD1 TYR B 380 4456 4289 3449 698 -428 -329 C ATOM 3235 CD2 TYR B 380 44.182 -8.564 22.161 1.00 30.00 C ANISOU 3235 CD2 TYR B 380 4160 3998 3241 600 -396 -344 C ATOM 3236 CE1 TYR B 380 44.799 -10.464 20.253 1.00 35.54 C ANISOU 3236 CE1 TYR B 380 5006 4693 3804 769 -478 -347 C ATOM 3237 CE2 TYR B 380 44.406 -9.877 22.545 1.00 31.71 C ANISOU 3237 CE2 TYR B 380 4490 4182 3377 671 -446 -361 C ATOM 3238 CZ TYR B 380 44.715 -10.821 21.588 1.00 40.44 C ANISOU 3238 CZ TYR B 380 5669 5284 4413 756 -487 -362 C ATOM 3239 OH TYR B 380 44.943 -12.125 21.963 1.00 47.36 O ANISOU 3239 OH TYR B 380 6669 6123 5203 830 -534 -379 O ATOM 3240 N TYR B 381 42.793 -4.691 18.447 1.00 19.72 N ANISOU 3240 N TYR B 381 2595 2742 2157 436 -256 -248 N ATOM 3241 CA TYR B 381 42.170 -3.371 18.438 1.00 18.75 C ANISOU 3241 CA TYR B 381 2402 2611 2112 355 -202 -225 C ATOM 3242 C TYR B 381 41.139 -3.323 19.561 1.00 16.17 C ANISOU 3242 C TYR B 381 2091 2220 1833 283 -198 -217 C ATOM 3243 O TYR B 381 40.151 -4.053 19.532 1.00 16.58 O ANISOU 3243 O TYR B 381 2207 2204 1888 269 -235 -205 O ATOM 3244 CB TYR B 381 41.522 -3.077 17.079 1.00 20.64 C ANISOU 3244 CB TYR B 381 2644 2826 2371 353 -202 -196 C ATOM 3245 CG TYR B 381 40.874 -1.708 16.970 1.00 22.20 C ANISOU 3245 CG TYR B 381 2779 3014 2642 283 -147 -171 C ATOM 3246 CD1 TYR B 381 41.553 -0.557 17.357 1.00 22.34 C ANISOU 3246 CD1 TYR B 381 2723 3083 2683 253 -84 -179 C ATOM 3247 CD2 TYR B 381 39.584 -1.567 16.461 1.00 20.88 C ANISOU 3247 CD2 TYR B 381 2629 2788 2516 249 -158 -141 C ATOM 3248 CE1 TYR B 381 40.959 0.696 17.254 1.00 23.38 C ANISOU 3248 CE1 TYR B 381 2810 3198 2874 194 -30 -156 C ATOM 3249 CE2 TYR B 381 38.984 -0.317 16.348 1.00 17.63 C ANISOU 3249 CE2 TYR B 381 2165 2368 2165 197 -107 -118 C ATOM 3250 CZ TYR B 381 39.674 0.807 16.746 1.00 21.98 C ANISOU 3250 CZ TYR B 381 2654 2961 2735 171 -43 -124 C ATOM 3251 OH TYR B 381 39.076 2.046 16.639 1.00 25.10 O ANISOU 3251 OH TYR B 381 3011 3341 3185 123 10 -100 O ATOM 3252 N SER B 382 41.391 -2.491 20.565 1.00 14.39 N ANISOU 3252 N SER B 382 1810 2016 1641 237 -153 -226 N ATOM 3253 CA SER B 382 40.483 -2.362 21.700 1.00 11.42 C ANISOU 3253 CA SER B 382 1447 1583 1311 169 -142 -219 C ATOM 3254 C SER B 382 39.977 -0.934 21.827 1.00 14.20 C ANISOU 3254 C SER B 382 1728 1931 1734 98 -78 -198 C ATOM 3255 O SER B 382 40.738 0.021 21.657 1.00 14.47 O ANISOU 3255 O SER B 382 1702 2021 1776 93 -34 -204 O ATOM 3256 CB SER B 382 41.182 -2.761 23.007 1.00 11.98 C ANISOU 3256 CB SER B 382 1532 1672 1350 180 -149 -250 C ATOM 3257 OG SER B 382 41.534 -4.128 23.008 1.00 22.12 O ANISOU 3257 OG SER B 382 2896 2947 2563 249 -207 -268 O ATOM 3258 N VAL B 383 38.697 -0.794 22.153 1.00 10.38 N ANISOU 3258 N VAL B 383 1258 1383 1302 42 -72 -176 N ATOM 3259 CA VAL B 383 38.088 0.521 22.297 1.00 15.94 C ANISOU 3259 CA VAL B 383 1906 2076 2073 -19 -13 -153 C ATOM 3260 C VAL B 383 37.196 0.560 23.522 1.00 10.70 C ANISOU 3260 C VAL B 383 1256 1359 1450 -79 2 -148 C ATOM 3261 O VAL B 383 36.753 -0.477 24.005 1.00 8.15 O ANISOU 3261 O VAL B 383 990 997 1111 -79 -38 -155 O ATOM 3262 CB VAL B 383 37.234 0.892 21.063 1.00 17.81 C ANISOU 3262 CB VAL B 383 2134 2295 2340 -19 -13 -122 C ATOM 3263 CG1 VAL B 383 38.091 0.883 19.798 1.00 10.61 C ANISOU 3263 CG1 VAL B 383 1215 1430 1385 40 -23 -125 C ATOM 3264 CG2 VAL B 383 36.054 -0.059 20.926 1.00 15.49 C ANISOU 3264 CG2 VAL B 383 1890 1944 2052 -28 -63 -110 C ATOM 3265 N GLN B 384 36.937 1.764 24.016 1.00 13.12 N ANISOU 3265 N GLN B 384 1516 1664 1807 -130 62 -136 N ATOM 3266 CA GLN B 384 36.062 1.948 25.159 1.00 13.42 C ANISOU 3266 CA GLN B 384 1560 1651 1887 -188 86 -129 C ATOM 3267 C GLN B 384 34.636 2.241 24.689 1.00 11.24 C ANISOU 3267 C GLN B 384 1274 1333 1663 -217 93 -95 C ATOM 3268 O GLN B 384 34.422 3.087 23.831 1.00 14.72 O ANISOU 3268 O GLN B 384 1679 1787 2128 -212 118 -74 O ATOM 3269 CB GLN B 384 36.580 3.076 26.051 1.00 9.91 C ANISOU 3269 CB GLN B 384 1077 1226 1463 -226 149 -135 C ATOM 3270 CG GLN B 384 35.732 3.260 27.312 1.00 16.83 C ANISOU 3270 CG GLN B 384 1967 2050 2380 -283 176 -129 C ATOM 3271 CD GLN B 384 36.274 4.344 28.218 1.00 21.92 C ANISOU 3271 CD GLN B 384 2582 2710 3038 -322 236 -137 C ATOM 3272 OE1 GLN B 384 36.813 4.066 29.291 1.00 28.62 O ANISOU 3272 OE1 GLN B 384 3449 3561 3864 -332 234 -162 O ATOM 3273 NE2 GLN B 384 36.150 5.591 27.782 1.00 21.70 N ANISOU 3273 NE2 GLN B 384 2513 2689 3042 -343 291 -118 N ATOM 3274 N THR B 385 33.673 1.519 25.248 1.00 11.55 N ANISOU 3274 N THR B 385 1348 1324 1718 -245 71 -92 N ATOM 3275 CA THR B 385 32.277 1.605 24.835 1.00 18.15 C ANISOU 3275 CA THR B 385 2171 2127 2599 -272 68 -65 C ATOM 3276 C THR B 385 31.426 0.818 25.819 1.00 18.12 C ANISOU 3276 C THR B 385 2205 2074 2607 -316 56 -71 C ATOM 3277 O THR B 385 31.856 -0.218 26.331 1.00 19.75 O ANISOU 3277 O THR B 385 2471 2266 2769 -308 22 -94 O ATOM 3278 CB THR B 385 32.048 0.978 23.427 1.00 14.09 C ANISOU 3278 CB THR B 385 1671 1622 2062 -232 14 -58 C ATOM 3279 OG1 THR B 385 30.645 0.840 23.173 1.00 13.22 O ANISOU 3279 OG1 THR B 385 1551 1482 1990 -263 0 -38 O ATOM 3280 CG2 THR B 385 32.657 -0.398 23.354 1.00 11.67 C ANISOU 3280 CG2 THR B 385 1430 1312 1691 -198 -46 -83 C ATOM 3281 N THR B 386 30.210 1.290 26.058 1.00 15.29 N ANISOU 3281 N THR B 386 1815 1689 2303 -361 84 -50 N ATOM 3282 CA THR B 386 29.247 0.530 26.848 1.00 21.51 C ANISOU 3282 CA THR B 386 2635 2432 3105 -410 74 -53 C ATOM 3283 C THR B 386 28.380 -0.352 25.952 1.00 20.57 C ANISOU 3283 C THR B 386 2532 2304 2981 -413 19 -48 C ATOM 3284 O THR B 386 27.470 -1.031 26.423 1.00 18.76 O ANISOU 3284 O THR B 386 2325 2040 2762 -460 8 -52 O ATOM 3285 CB THR B 386 28.356 1.463 27.680 1.00 26.99 C ANISOU 3285 CB THR B 386 3285 3108 3861 -460 137 -35 C ATOM 3286 OG1 THR B 386 27.914 2.553 26.860 1.00 23.14 O ANISOU 3286 OG1 THR B 386 2734 2646 3413 -445 163 -8 O ATOM 3287 CG2 THR B 386 29.150 2.032 28.851 1.00 31.42 C ANISOU 3287 CG2 THR B 386 3855 3663 4419 -471 184 -47 C ATOM 3288 N GLU B 387 28.672 -0.360 24.657 1.00 18.50 N ANISOU 3288 N GLU B 387 2258 2071 2698 -366 -15 -42 N ATOM 3289 CA GLU B 387 27.803 -1.071 23.718 1.00 19.70 C ANISOU 3289 CA GLU B 387 2420 2218 2847 -370 -67 -36 C ATOM 3290 C GLU B 387 28.465 -2.310 23.126 1.00 18.21 C ANISOU 3290 C GLU B 387 2306 2025 2589 -333 -131 -56 C ATOM 3291 O GLU B 387 28.053 -2.817 22.080 1.00 12.34 O ANISOU 3291 O GLU B 387 1575 1285 1830 -321 -178 -52 O ATOM 3292 CB GLU B 387 27.307 -0.117 22.619 1.00 18.11 C ANISOU 3292 CB GLU B 387 2151 2049 2680 -348 -59 -9 C ATOM 3293 CG GLU B 387 26.559 1.099 23.175 1.00 21.30 C ANISOU 3293 CG GLU B 387 2488 2456 3149 -377 5 12 C ATOM 3294 CD GLU B 387 26.068 2.050 22.097 1.00 25.59 C ANISOU 3294 CD GLU B 387 2974 3028 3720 -345 13 39 C ATOM 3295 OE1 GLU B 387 26.898 2.769 21.511 1.00 25.21 O ANISOU 3295 OE1 GLU B 387 2919 3002 3656 -299 31 46 O ATOM 3296 OE2 GLU B 387 24.847 2.095 21.848 1.00 30.07 O ANISOU 3296 OE2 GLU B 387 3504 3600 4322 -365 3 52 O ATOM 3297 N GLY B 388 29.487 -2.804 23.814 1.00 17.66 N ANISOU 3297 N GLY B 388 2290 1947 2474 -313 -133 -78 N ATOM 3298 CA GLY B 388 30.218 -3.970 23.351 1.00 15.63 C ANISOU 3298 CA GLY B 388 2111 1685 2143 -267 -189 -98 C ATOM 3299 C GLY B 388 29.342 -5.153 23.005 1.00 16.16 C ANISOU 3299 C GLY B 388 2240 1712 2188 -297 -241 -103 C ATOM 3300 O GLY B 388 29.597 -5.862 22.029 1.00 14.46 O ANISOU 3300 O GLY B 388 2069 1499 1925 -258 -292 -108 O ATOM 3301 N GLU B 389 28.308 -5.387 23.807 1.00 23.48 N ANISOU 3301 N GLU B 389 3173 2601 3147 -370 -227 -103 N ATOM 3302 CA GLU B 389 27.408 -6.513 23.552 1.00 22.01 C ANISOU 3302 CA GLU B 389 3045 2376 2940 -414 -272 -111 C ATOM 3303 C GLU B 389 26.657 -6.378 22.224 1.00 22.13 C ANISOU 3303 C GLU B 389 3017 2416 2974 -415 -305 -95 C ATOM 3304 O GLU B 389 26.581 -7.338 21.446 1.00 19.78 O ANISOU 3304 O GLU B 389 2783 2104 2629 -407 -361 -103 O ATOM 3305 CB GLU B 389 26.427 -6.711 24.716 1.00 32.97 C ANISOU 3305 CB GLU B 389 4441 3724 4362 -500 -241 -115 C ATOM 3306 CG GLU B 389 25.217 -7.582 24.390 1.00 43.00 C ANISOU 3306 CG GLU B 389 5740 4966 5631 -567 -275 -119 C ATOM 3307 CD GLU B 389 25.563 -9.050 24.199 0.75 55.08 C ANISOU 3307 CD GLU B 389 7400 6451 7078 -561 -329 -143 C ATOM 3308 OE1 GLU B 389 26.765 -9.389 24.130 0.75 58.81 O ANISOU 3308 OE1 GLU B 389 7933 6920 7490 -488 -347 -153 O ATOM 3309 OE2 GLU B 389 24.624 -9.869 24.116 0.75 60.41 O ANISOU 3309 OE2 GLU B 389 8116 7093 7743 -629 -352 -151 O ATOM 3310 N GLN B 390 26.098 -5.199 21.959 1.00 23.24 N ANISOU 3310 N GLN B 390 3057 2593 3181 -423 -272 -71 N ATOM 3311 CA GLN B 390 25.425 -4.981 20.679 1.00 23.59 C ANISOU 3311 CA GLN B 390 3056 2666 3240 -414 -305 -56 C ATOM 3312 C GLN B 390 26.404 -5.216 19.535 1.00 20.20 C ANISOU 3312 C GLN B 390 2664 2254 2755 -337 -344 -57 C ATOM 3313 O GLN B 390 26.062 -5.827 18.519 1.00 18.41 O ANISOU 3313 O GLN B 390 2466 2027 2501 -330 -399 -58 O ATOM 3314 CB GLN B 390 24.888 -3.556 20.564 1.00 23.64 C ANISOU 3314 CB GLN B 390 2956 2711 3317 -413 -258 -30 C ATOM 3315 CG GLN B 390 23.739 -3.204 21.483 1.00 30.29 C ANISOU 3315 CG GLN B 390 3744 3545 4219 -483 -219 -24 C ATOM 3316 CD GLN B 390 23.535 -1.696 21.554 1.00 38.17 C ANISOU 3316 CD GLN B 390 4652 4575 5275 -463 -161 2 C ATOM 3317 OE1 GLN B 390 23.069 -1.066 20.595 1.00 34.84 O ANISOU 3317 OE1 GLN B 390 4175 4187 4875 -434 -171 21 O ATOM 3318 NE2 GLN B 390 23.907 -1.106 22.690 1.00 36.55 N ANISOU 3318 NE2 GLN B 390 4438 4356 5092 -475 -101 2 N ATOM 3319 N ILE B 391 27.619 -4.699 19.690 1.00 14.06 N ANISOU 3319 N ILE B 391 1884 1495 1962 -280 -316 -58 N ATOM 3320 CA ILE B 391 28.613 -4.814 18.634 1.00 14.99 C ANISOU 3320 CA ILE B 391 2029 1636 2029 -205 -344 -60 C ATOM 3321 C ILE B 391 28.906 -6.284 18.336 1.00 16.72 C ANISOU 3321 C ILE B 391 2354 1824 2174 -188 -404 -81 C ATOM 3322 O ILE B 391 28.930 -6.696 17.177 1.00 18.76 O ANISOU 3322 O ILE B 391 2642 2088 2399 -154 -450 -78 O ATOM 3323 CB ILE B 391 29.915 -4.076 19.003 1.00 14.40 C ANISOU 3323 CB ILE B 391 1932 1592 1947 -156 -299 -63 C ATOM 3324 CG1 ILE B 391 29.644 -2.585 19.190 1.00 11.64 C ANISOU 3324 CG1 ILE B 391 1491 1269 1665 -172 -237 -42 C ATOM 3325 CG2 ILE B 391 30.972 -4.299 17.933 1.00 11.22 C ANISOU 3325 CG2 ILE B 391 1559 1217 1488 -79 -326 -68 C ATOM 3326 CD1 ILE B 391 30.791 -1.845 19.853 1.00 8.99 C ANISOU 3326 CD1 ILE B 391 1133 957 1327 -150 -185 -49 C ATOM 3327 N SER B 392 29.096 -7.071 19.392 1.00 19.44 N ANISOU 3327 N SER B 392 2764 2132 2491 -212 -404 -101 N ATOM 3328 CA SER B 392 29.321 -8.514 19.258 1.00 27.45 C ANISOU 3328 CA SER B 392 3895 3105 3429 -199 -457 -121 C ATOM 3329 C SER B 392 28.207 -9.219 18.511 1.00 22.87 C ANISOU 3329 C SER B 392 3347 2500 2844 -246 -505 -120 C ATOM 3330 O SER B 392 28.467 -10.061 17.650 1.00 21.52 O ANISOU 3330 O SER B 392 3251 2314 2610 -211 -556 -127 O ATOM 3331 CB SER B 392 29.461 -9.170 20.629 1.00 23.37 C ANISOU 3331 CB SER B 392 3444 2544 2890 -229 -443 -142 C ATOM 3332 OG SER B 392 30.484 -8.547 21.366 1.00 27.11 O ANISOU 3332 OG SER B 392 3888 3045 3366 -188 -402 -146 O ATOM 3333 N GLN B 393 26.964 -8.893 18.855 1.00 23.42 N ANISOU 3333 N GLN B 393 3360 2564 2974 -327 -489 -111 N ATOM 3334 CA GLN B 393 25.813 -9.527 18.212 1.00 24.63 C ANISOU 3334 CA GLN B 393 3531 2701 3126 -385 -535 -113 C ATOM 3335 C GLN B 393 25.719 -9.196 16.726 1.00 31.30 C ANISOU 3335 C GLN B 393 4340 3583 3969 -342 -572 -98 C ATOM 3336 O GLN B 393 25.353 -10.047 15.915 1.00 30.01 O ANISOU 3336 O GLN B 393 4236 3402 3763 -353 -628 -105 O ATOM 3337 CB GLN B 393 24.517 -9.152 18.933 1.00 35.60 C ANISOU 3337 CB GLN B 393 4850 4091 4586 -478 -504 -108 C ATOM 3338 CG GLN B 393 24.189 -10.062 20.111 1.00 47.54 C ANISOU 3338 CG GLN B 393 6437 5546 6079 -549 -493 -129 C ATOM 3339 CD GLN B 393 23.304 -9.386 21.139 1.00 65.33 C ANISOU 3339 CD GLN B 393 8609 7805 8406 -620 -438 -123 C ATOM 3340 OE1 GLN B 393 23.041 -8.185 21.055 1.00 67.38 O ANISOU 3340 OE1 GLN B 393 8759 8112 8731 -608 -404 -102 O ATOM 3341 NE2 GLN B 393 22.843 -10.155 22.122 1.00 72.87 N ANISOU 3341 NE2 GLN B 393 9627 8712 9350 -694 -425 -141 N ATOM 3342 N LEU B 394 26.044 -7.956 16.370 1.00 30.74 N ANISOU 3342 N LEU B 394 4180 3560 3940 -294 -539 -77 N ATOM 3343 CA LEU B 394 26.033 -7.546 14.974 1.00 26.74 C ANISOU 3343 CA LEU B 394 3644 3086 3428 -245 -568 -61 C ATOM 3344 C LEU B 394 27.062 -8.333 14.181 1.00 24.33 C ANISOU 3344 C LEU B 394 3432 2770 3043 -175 -609 -71 C ATOM 3345 O LEU B 394 26.763 -8.877 13.119 1.00 26.69 O ANISOU 3345 O LEU B 394 3771 3063 3306 -165 -663 -72 O ATOM 3346 CB LEU B 394 26.301 -6.051 14.850 1.00 24.07 C ANISOU 3346 CB LEU B 394 3208 2794 3143 -206 -516 -38 C ATOM 3347 CG LEU B 394 25.134 -5.225 14.333 1.00 30.34 C ANISOU 3347 CG LEU B 394 3914 3619 3997 -229 -515 -17 C ATOM 3348 CD1 LEU B 394 23.834 -5.696 14.948 1.00 28.74 C ANISOU 3348 CD1 LEU B 394 3692 3401 3825 -319 -527 -25 C ATOM 3349 CD2 LEU B 394 25.359 -3.748 14.613 1.00 37.59 C ANISOU 3349 CD2 LEU B 394 4748 4567 4968 -203 -448 4 C ATOM 3350 N ILE B 395 28.279 -8.384 14.707 1.00 20.53 N ANISOU 3350 N ILE B 395 2984 2287 2529 -125 -582 -81 N ATOM 3351 CA ILE B 395 29.360 -9.126 14.073 1.00 23.65 C ANISOU 3351 CA ILE B 395 3465 2676 2844 -49 -614 -92 C ATOM 3352 C ILE B 395 28.992 -10.596 13.848 1.00 22.12 C ANISOU 3352 C ILE B 395 3389 2429 2585 -72 -675 -110 C ATOM 3353 O ILE B 395 29.133 -11.107 12.740 1.00 24.44 O ANISOU 3353 O ILE B 395 3737 2718 2829 -33 -720 -109 O ATOM 3354 CB ILE B 395 30.654 -9.016 14.886 1.00 25.47 C ANISOU 3354 CB ILE B 395 3706 2919 3051 1 -576 -104 C ATOM 3355 CG1 ILE B 395 31.248 -7.613 14.724 1.00 20.82 C ANISOU 3355 CG1 ILE B 395 3017 2387 2506 37 -524 -88 C ATOM 3356 CG2 ILE B 395 31.653 -10.069 14.449 1.00 26.65 C ANISOU 3356 CG2 ILE B 395 3962 3056 3109 75 -614 -121 C ATOM 3357 CD1 ILE B 395 32.310 -7.294 15.740 1.00 20.42 C ANISOU 3357 CD1 ILE B 395 2951 2356 2451 62 -478 -101 C ATOM 3358 N ALA B 396 28.513 -11.267 14.891 1.00 20.74 N ANISOU 3358 N ALA B 396 3261 2212 2408 -137 -672 -125 N ATOM 3359 CA ALA B 396 28.000 -12.632 14.752 1.00 26.78 C ANISOU 3359 CA ALA B 396 4141 2919 3114 -179 -724 -142 C ATOM 3360 C ALA B 396 26.919 -12.737 13.672 1.00 33.10 C ANISOU 3360 C ALA B 396 4926 3724 3928 -223 -769 -135 C ATOM 3361 O ALA B 396 27.000 -13.572 12.772 1.00 35.74 O ANISOU 3361 O ALA B 396 5348 4035 4198 -202 -822 -142 O ATOM 3362 CB ALA B 396 27.450 -13.129 16.081 1.00 25.22 C ANISOU 3362 CB ALA B 396 3980 2677 2928 -259 -703 -158 C ATOM 3363 N GLY B 397 25.899 -11.895 13.782 1.00 30.87 N ANISOU 3363 N GLY B 397 4531 3472 3725 -284 -750 -121 N ATOM 3364 CA GLY B 397 24.771 -11.941 12.873 1.00 35.53 C ANISOU 3364 CA GLY B 397 5091 4077 4333 -332 -794 -116 C ATOM 3365 C GLY B 397 25.185 -11.882 11.418 1.00 38.02 C ANISOU 3365 C GLY B 397 5423 4411 4610 -257 -836 -106 C ATOM 3366 O GLY B 397 24.662 -12.622 10.588 1.00 38.35 O ANISOU 3366 O GLY B 397 5522 4436 4612 -281 -894 -114 O ATOM 3367 N TYR B 398 26.125 -11.000 11.100 1.00 33.77 N ANISOU 3367 N TYR B 398 4841 3908 4081 -171 -805 -90 N ATOM 3368 CA TYR B 398 26.573 -10.861 9.722 1.00 32.90 C ANISOU 3368 CA TYR B 398 4747 3818 3936 -97 -836 -79 C ATOM 3369 C TYR B 398 27.423 -12.047 9.266 1.00 35.94 C ANISOU 3369 C TYR B 398 5269 4163 4224 -45 -875 -95 C ATOM 3370 O TYR B 398 27.344 -12.472 8.111 1.00 35.91 O ANISOU 3370 O TYR B 398 5317 4152 4175 -19 -925 -94 O ATOM 3371 CB TYR B 398 27.323 -9.551 9.529 1.00 26.49 C ANISOU 3371 CB TYR B 398 3850 3054 3160 -27 -785 -59 C ATOM 3372 CG TYR B 398 26.403 -8.365 9.390 1.00 22.05 C ANISOU 3372 CG TYR B 398 3170 2531 2677 -55 -764 -38 C ATOM 3373 CD1 TYR B 398 26.590 -7.217 10.153 1.00 23.25 C ANISOU 3373 CD1 TYR B 398 3234 2710 2889 -53 -696 -26 C ATOM 3374 CD2 TYR B 398 25.338 -8.402 8.505 1.00 20.46 C ANISOU 3374 CD2 TYR B 398 2949 2340 2485 -82 -813 -32 C ATOM 3375 CE1 TYR B 398 25.749 -6.134 10.022 1.00 25.93 C ANISOU 3375 CE1 TYR B 398 3474 3082 3294 -70 -674 -6 C ATOM 3376 CE2 TYR B 398 24.491 -7.326 8.365 1.00 26.85 C ANISOU 3376 CE2 TYR B 398 3652 3189 3361 -96 -795 -13 C ATOM 3377 CZ TYR B 398 24.696 -6.194 9.126 1.00 31.48 C ANISOU 3377 CZ TYR B 398 4158 3798 4005 -88 -725 1 C ATOM 3378 OH TYR B 398 23.846 -5.120 8.980 1.00 26.60 O ANISOU 3378 OH TYR B 398 3443 3217 3448 -95 -706 21 O ATOM 3379 N ILE B 399 28.228 -12.583 10.177 1.00 31.11 N ANISOU 3379 N ILE B 399 4719 3526 3578 -27 -853 -110 N ATOM 3380 CA ILE B 399 29.029 -13.752 9.867 1.00 36.93 C ANISOU 3380 CA ILE B 399 5592 4222 4218 28 -887 -126 C ATOM 3381 C ILE B 399 28.116 -14.924 9.537 1.00 39.58 C ANISOU 3381 C ILE B 399 6028 4504 4509 -40 -946 -141 C ATOM 3382 O ILE B 399 28.361 -15.672 8.586 1.00 39.48 O ANISOU 3382 O ILE B 399 6110 4466 4423 0 -993 -145 O ATOM 3383 CB ILE B 399 29.959 -14.130 11.035 1.00 40.96 C ANISOU 3383 CB ILE B 399 6150 4715 4698 58 -853 -142 C ATOM 3384 CG1 ILE B 399 31.243 -13.301 10.973 1.00 39.95 C ANISOU 3384 CG1 ILE B 399 5962 4642 4574 153 -811 -134 C ATOM 3385 CG2 ILE B 399 30.285 -15.624 10.999 1.00 41.61 C ANISOU 3385 CG2 ILE B 399 6396 4734 4679 78 -896 -163 C ATOM 3386 CD1 ILE B 399 32.188 -13.554 12.125 1.00 39.58 C ANISOU 3386 CD1 ILE B 399 5945 4592 4501 188 -780 -150 C ATOM 3387 N ASP B 400 27.053 -15.068 10.322 1.00 38.46 N ANISOU 3387 N ASP B 400 5863 4343 4409 -145 -942 -148 N ATOM 3388 CA ASP B 400 26.116 -16.167 10.137 1.00 44.84 C ANISOU 3388 CA ASP B 400 6760 5099 5176 -229 -992 -166 C ATOM 3389 C ASP B 400 25.536 -16.127 8.731 1.00 42.92 C ANISOU 3389 C ASP B 400 6505 4875 4926 -231 -1047 -158 C ATOM 3390 O ASP B 400 25.458 -17.151 8.049 1.00 45.11 O ANISOU 3390 O ASP B 400 6900 5110 5128 -237 -1100 -170 O ATOM 3391 CB ASP B 400 24.986 -16.108 11.167 1.00 50.51 C ANISOU 3391 CB ASP B 400 7426 5811 5955 -348 -971 -174 C ATOM 3392 CG ASP B 400 24.052 -17.301 11.071 1.00 66.83 C ANISOU 3392 CG ASP B 400 9592 7824 7977 -448 -1017 -196 C ATOM 3393 OD1 ASP B 400 24.464 -18.413 11.472 1.00 71.66 O ANISOU 3393 OD1 ASP B 400 10348 8368 8511 -449 -1026 -215 O ATOM 3394 OD2 ASP B 400 22.907 -17.129 10.592 1.00 70.14 O ANISOU 3394 OD2 ASP B 400 9946 8270 8435 -524 -1044 -196 O ATOM 3395 N ILE B 401 25.133 -14.937 8.299 1.00 32.44 N ANISOU 3395 N ILE B 401 5042 3611 3672 -224 -1034 -137 N ATOM 3396 CA ILE B 401 24.577 -14.778 6.960 1.00 37.62 C ANISOU 3396 CA ILE B 401 5678 4291 4324 -218 -1086 -128 C ATOM 3397 C ILE B 401 25.580 -15.204 5.886 1.00 39.91 C ANISOU 3397 C ILE B 401 6067 4565 4533 -118 -1115 -125 C ATOM 3398 O ILE B 401 25.234 -15.935 4.960 1.00 47.19 O ANISOU 3398 O ILE B 401 7068 5462 5400 -129 -1175 -133 O ATOM 3399 CB ILE B 401 24.083 -13.343 6.723 1.00 38.38 C ANISOU 3399 CB ILE B 401 5618 4456 4509 -210 -1061 -104 C ATOM 3400 CG1 ILE B 401 22.863 -13.066 7.607 1.00 33.75 C ANISOU 3400 CG1 ILE B 401 4941 3888 3995 -315 -1044 -109 C ATOM 3401 CG2 ILE B 401 23.743 -13.127 5.254 1.00 38.91 C ANISOU 3401 CG2 ILE B 401 5676 4549 4561 -176 -1113 -93 C ATOM 3402 CD1 ILE B 401 22.476 -11.604 7.691 1.00 30.78 C ANISOU 3402 CD1 ILE B 401 4413 3575 3707 -300 -1003 -85 C ATOM 3403 N ILE B 402 26.825 -14.767 6.025 1.00 41.42 N ANISOU 3403 N ILE B 402 6254 4770 4714 -23 -1072 -116 N ATOM 3404 CA ILE B 402 27.877 -15.182 5.107 1.00 43.49 C ANISOU 3404 CA ILE B 402 6607 5020 4898 78 -1091 -114 C ATOM 3405 C ILE B 402 27.986 -16.703 5.041 1.00 51.97 C ANISOU 3405 C ILE B 402 7847 6024 5876 67 -1137 -137 C ATOM 3406 O ILE B 402 28.187 -17.271 3.969 1.00 56.12 O ANISOU 3406 O ILE B 402 8461 6528 6333 110 -1181 -138 O ATOM 3407 CB ILE B 402 29.238 -14.596 5.502 1.00 42.33 C ANISOU 3407 CB ILE B 402 6429 4902 4751 171 -1032 -108 C ATOM 3408 CG1 ILE B 402 29.224 -13.075 5.337 1.00 46.59 C ANISOU 3408 CG1 ILE B 402 6823 5506 5372 189 -987 -84 C ATOM 3409 CG2 ILE B 402 30.343 -15.213 4.658 1.00 37.83 C ANISOU 3409 CG2 ILE B 402 5964 4319 4091 273 -1051 -111 C ATOM 3410 CD1 ILE B 402 30.452 -12.383 5.894 1.00 46.17 C ANISOU 3410 CD1 ILE B 402 6723 5488 5332 257 -922 -81 C ATOM 3411 N LEU B 403 27.849 -17.360 6.189 1.00 56.82 N ANISOU 3411 N LEU B 403 8510 6598 6480 12 -1123 -155 N ATOM 3412 CA LEU B 403 27.928 -18.818 6.243 1.00 58.17 C ANISOU 3412 CA LEU B 403 8853 6694 6555 -2 -1161 -177 C ATOM 3413 C LEU B 403 26.738 -19.497 5.571 1.00 64.74 C ANISOU 3413 C LEU B 403 9740 7494 7366 -96 -1223 -187 C ATOM 3414 O LEU B 403 26.893 -20.537 4.936 1.00 67.90 O ANISOU 3414 O LEU B 403 10284 7841 7675 -81 -1267 -199 O ATOM 3415 CB LEU B 403 28.061 -19.311 7.685 1.00 53.89 C ANISOU 3415 CB LEU B 403 8355 6113 6006 -39 -1127 -193 C ATOM 3416 CG LEU B 403 29.482 -19.520 8.203 1.00 54.54 C ANISOU 3416 CG LEU B 403 8495 6190 6037 71 -1095 -197 C ATOM 3417 CD1 LEU B 403 29.447 -20.197 9.563 1.00 55.26 C ANISOU 3417 CD1 LEU B 403 8657 6230 6108 26 -1074 -216 C ATOM 3418 CD2 LEU B 403 30.295 -20.345 7.215 1.00 54.56 C ANISOU 3418 CD2 LEU B 403 8631 6164 5935 167 -1132 -201 C ATOM 3419 N LYS B 404 25.554 -18.911 5.717 1.00 66.93 N ANISOU 3419 N LYS B 404 9903 7805 7724 -193 -1225 -184 N ATOM 3420 CA LYS B 404 24.352 -19.474 5.114 1.00 71.67 C ANISOU 3420 CA LYS B 404 10532 8389 8310 -291 -1284 -197 C ATOM 3421 C LYS B 404 24.274 -19.176 3.613 1.00 76.58 C ANISOU 3421 C LYS B 404 11140 9040 8916 -242 -1333 -184 C ATOM 3422 O LYS B 404 23.356 -19.625 2.924 1.00 70.72 O ANISOU 3422 O LYS B 404 10424 8290 8155 -312 -1391 -194 O ATOM 3423 CB LYS B 404 23.099 -18.984 5.847 1.00 73.70 C ANISOU 3423 CB LYS B 404 10665 8679 8656 -411 -1269 -201 C ATOM 3424 CG LYS B 404 22.945 -19.572 7.248 1.00 78.40 C ANISOU 3424 CG LYS B 404 11309 9229 9252 -486 -1232 -220 C ATOM 3425 CD LYS B 404 21.710 -19.033 7.969 1.00 81.79 C ANISOU 3425 CD LYS B 404 11607 9697 9771 -601 -1211 -223 C ATOM 3426 CE LYS B 404 21.507 -19.726 9.317 1.00 82.26 C ANISOU 3426 CE LYS B 404 11731 9702 9821 -684 -1176 -244 C ATOM 3427 NZ LYS B 404 20.343 -19.183 10.080 1.00 79.93 N ANISOU 3427 NZ LYS B 404 11307 9447 9616 -793 -1147 -247 N ATOM 3428 N LYS B 405 25.247 -18.417 3.116 1.00 86.24 N ANISOU 3428 N LYS B 405 12324 10298 10146 -124 -1309 -162 N ATOM 3429 CA LYS B 405 25.396 -18.189 1.683 1.00 98.36 C ANISOU 3429 CA LYS B 405 13869 11852 11651 -59 -1348 -149 C ATOM 3430 C LYS B 405 26.346 -19.228 1.103 1.00108.18 C ANISOU 3430 C LYS B 405 15283 13039 12784 17 -1372 -157 C ATOM 3431 O LYS B 405 26.182 -19.664 -0.035 1.00110.86 O ANISOU 3431 O LYS B 405 15696 13360 13067 32 -1427 -158 O ATOM 3432 CB LYS B 405 25.940 -16.788 1.405 1.00101.84 C ANISOU 3432 CB LYS B 405 14182 12359 12154 26 -1304 -122 C ATOM 3433 CG LYS B 405 24.954 -15.661 1.651 1.00105.73 C ANISOU 3433 CG LYS B 405 14512 12911 12749 -31 -1288 -109 C ATOM 3434 CD LYS B 405 25.673 -14.321 1.670 1.00108.34 C ANISOU 3434 CD LYS B 405 14737 13294 13135 52 -1227 -84 C ATOM 3435 CE LYS B 405 24.716 -13.175 1.950 1.00111.10 C ANISOU 3435 CE LYS B 405 14934 13699 13581 4 -1206 -71 C ATOM 3436 NZ LYS B 405 25.443 -11.945 2.380 1.00112.89 N ANISOU 3436 NZ LYS B 405 15068 13963 13861 65 -1132 -51 N ATOM 3437 N LYS B 406 27.349 -19.609 1.893 1.00114.44 N ANISOU 3437 N LYS B 406 16137 13804 13541 71 -1332 -163 N ATOM 3438 CA LYS B 406 28.275 -20.671 1.508 1.00120.07 C ANISOU 3438 CA LYS B 406 17018 14461 14143 149 -1350 -172 C ATOM 3439 C LYS B 406 27.533 -21.998 1.448 1.00128.86 C ANISOU 3439 C LYS B 406 18278 15497 15184 62 -1404 -196 C ATOM 3440 O LYS B 406 28.004 -22.960 0.838 1.00130.06 O ANISOU 3440 O LYS B 406 18587 15595 15236 110 -1436 -204 O ATOM 3441 CB LYS B 406 29.441 -20.768 2.496 1.00116.89 C ANISOU 3441 CB LYS B 406 16638 14053 13721 223 -1295 -175 C ATOM 3442 CG LYS B 406 30.533 -19.728 2.293 1.00113.48 C ANISOU 3442 CG LYS B 406 16108 13688 13320 335 -1246 -156 C ATOM 3443 CD LYS B 406 31.675 -19.941 3.275 1.00110.20 C ANISOU 3443 CD LYS B 406 15721 13273 12878 405 -1200 -165 C ATOM 3444 CE LYS B 406 32.819 -18.974 3.018 1.00107.08 C ANISOU 3444 CE LYS B 406 15233 12948 12504 513 -1152 -150 C ATOM 3445 NZ LYS B 406 33.929 -19.177 3.988 1.00105.85 N ANISOU 3445 NZ LYS B 406 15094 12802 12320 581 -1111 -161 N ATOM 3446 N GLN B 407 26.373 -22.042 2.095 1.00135.24 N ANISOU 3446 N GLN B 407 19039 16302 16044 -70 -1411 -208 N ATOM 3447 CA GLN B 407 25.491 -23.199 2.022 1.00140.47 C ANISOU 3447 CA GLN B 407 19824 16899 16648 -178 -1462 -233 C ATOM 3448 C GLN B 407 24.629 -23.085 0.767 1.00141.77 C ANISOU 3448 C GLN B 407 19964 17086 16815 -220 -1525 -231 C ATOM 3449 O GLN B 407 23.706 -23.872 0.558 1.00143.43 O ANISOU 3449 O GLN B 407 20246 17261 16991 -328 -1574 -252 O ATOM 3450 CB GLN B 407 24.615 -23.282 3.276 1.00143.41 C ANISOU 3450 CB GLN B 407 20150 17265 17076 -306 -1437 -248 C ATOM 3451 CG GLN B 407 25.403 -23.259 4.582 1.00145.22 C ANISOU 3451 CG GLN B 407 20386 17478 17312 -266 -1373 -249 C ATOM 3452 CD GLN B 407 24.513 -23.270 5.814 1.00146.14 C ANISOU 3452 CD GLN B 407 20452 17587 17485 -392 -1345 -263 C ATOM 3453 OE1 GLN B 407 23.350 -23.667 5.752 1.00147.64 O ANISOU 3453 OE1 GLN B 407 20649 17765 17684 -519 -1375 -279 O ATOM 3454 NE2 GLN B 407 25.061 -22.835 6.944 1.00144.59 N ANISOU 3454 NE2 GLN B 407 20206 17402 17328 -360 -1285 -258 N ATOM 3455 N SER B 408 24.953 -22.095 -0.063 1.00139.79 N ANISOU 3455 N SER B 408 19615 16896 16602 -136 -1524 -207 N ATOM 3456 CA SER B 408 24.236 -21.833 -1.308 1.00136.84 C ANISOU 3456 CA SER B 408 19209 16553 16232 -155 -1583 -201 C ATOM 3457 C SER B 408 22.721 -21.849 -1.120 1.00136.17 C ANISOU 3457 C SER B 408 19051 16491 16198 -303 -1619 -218 C ATOM 3458 O SER B 408 22.093 -20.797 -0.996 1.00134.48 O ANISOU 3458 O SER B 408 18671 16349 16078 -328 -1606 -206 O ATOM 3459 CB SER B 408 24.658 -22.821 -2.401 1.00134.77 C ANISOU 3459 CB SER B 408 19123 16230 15854 -106 -1635 -208 C ATOM 3460 OG SER B 408 25.952 -22.516 -2.893 1.00131.74 O ANISOU 3460 OG SER B 408 18767 15852 15437 42 -1606 -188 O TER 3461 SER B 408 ATOM 3462 N GLY C 750 46.303 23.714 39.007 1.00 71.11 N ANISOU 3462 N GLY C 750 8861 8728 9432 416 -809 -235 N ATOM 3463 CA GLY C 750 46.217 24.215 37.646 1.00 70.08 C ANISOU 3463 CA GLY C 750 8778 8539 9310 399 -829 -208 C ATOM 3464 C GLY C 750 45.276 23.394 36.784 1.00 66.86 C ANISOU 3464 C GLY C 750 8380 8172 8850 382 -769 -220 C ATOM 3465 O GLY C 750 45.327 22.162 36.806 1.00 62.71 O ANISOU 3465 O GLY C 750 7842 7686 8300 352 -681 -198 O ATOM 3466 N PRO C 751 44.405 24.076 36.020 1.00 65.07 N ANISOU 3466 N PRO C 751 8178 7937 8608 403 -819 -254 N ATOM 3467 CA PRO C 751 43.427 23.449 35.122 1.00 59.99 C ANISOU 3467 CA PRO C 751 7546 7331 7915 391 -772 -270 C ATOM 3468 C PRO C 751 44.026 22.360 34.228 1.00 49.76 C ANISOU 3468 C PRO C 751 6268 6018 6621 336 -675 -200 C ATOM 3469 O PRO C 751 43.550 21.229 34.253 1.00 43.72 O ANISOU 3469 O PRO C 751 5492 5305 5814 318 -608 -207 O ATOM 3470 CB PRO C 751 42.939 24.624 34.275 1.00 62.84 C ANISOU 3470 CB PRO C 751 7940 7651 8284 415 -847 -291 C ATOM 3471 CG PRO C 751 43.059 25.793 35.185 1.00 64.54 C ANISOU 3471 CG PRO C 751 8149 7847 8527 462 -949 -330 C ATOM 3472 CD PRO C 751 44.281 25.545 36.028 1.00 63.86 C ANISOU 3472 CD PRO C 751 8043 7738 8483 443 -930 -285 C ATOM 3473 N LYS C 752 45.049 22.694 33.448 1.00 47.34 N ANISOU 3473 N LYS C 752 5988 5641 6357 312 -674 -131 N ATOM 3474 CA LYS C 752 45.674 21.711 32.568 1.00 44.64 C ANISOU 3474 CA LYS C 752 5663 5287 6012 271 -590 -63 C ATOM 3475 C LYS C 752 46.299 20.562 33.373 1.00 33.53 C ANISOU 3475 C LYS C 752 4236 3909 4595 250 -519 -39 C ATOM 3476 O LYS C 752 46.165 19.393 33.015 1.00 28.69 O ANISOU 3476 O LYS C 752 3629 3321 3950 228 -445 -25 O ATOM 3477 CB LYS C 752 46.723 22.383 31.684 1.00 52.23 C ANISOU 3477 CB LYS C 752 6647 6180 7018 254 -612 12 C ATOM 3478 CG LYS C 752 47.037 21.630 30.403 1.00 65.64 C ANISOU 3478 CG LYS C 752 8366 7872 8702 227 -544 70 C ATOM 3479 CD LYS C 752 45.820 21.558 29.490 1.00 73.62 C ANISOU 3479 CD LYS C 752 9390 8902 9679 237 -539 26 C ATOM 3480 CE LYS C 752 46.180 21.018 28.111 1.00 76.90 C ANISOU 3480 CE LYS C 752 9826 9307 10088 217 -486 85 C ATOM 3481 NZ LYS C 752 44.993 20.974 27.209 1.00 78.96 N ANISOU 3481 NZ LYS C 752 10098 9586 10317 227 -480 42 N ATOM 3482 N LEU C 753 46.976 20.916 34.463 1.00 27.80 N ANISOU 3482 N LEU C 753 3488 3177 3898 259 -545 -36 N ATOM 3483 CA LEU C 753 47.612 19.951 35.358 1.00 28.74 C ANISOU 3483 CA LEU C 753 3583 3324 4013 244 -483 -16 C ATOM 3484 C LEU C 753 46.614 18.872 35.779 1.00 27.54 C ANISOU 3484 C LEU C 753 3412 3243 3811 242 -436 -63 C ATOM 3485 O LEU C 753 46.906 17.681 35.691 1.00 27.08 O ANISOU 3485 O LEU C 753 3357 3199 3731 214 -360 -32 O ATOM 3486 CB LEU C 753 48.170 20.692 36.587 1.00 35.83 C ANISOU 3486 CB LEU C 753 4452 4215 4945 265 -535 -27 C ATOM 3487 CG LEU C 753 48.870 20.052 37.804 1.00 33.72 C ANISOU 3487 CG LEU C 753 4150 3978 4684 260 -492 -16 C ATOM 3488 CD1 LEU C 753 48.057 18.921 38.429 1.00 32.24 C ANISOU 3488 CD1 LEU C 753 3932 3866 4452 260 -439 -58 C ATOM 3489 CD2 LEU C 753 50.296 19.608 37.506 1.00 36.38 C ANISOU 3489 CD2 LEU C 753 4503 4279 5039 226 -436 71 C ATOM 3490 N LEU C 754 45.434 19.295 36.227 1.00 27.69 N ANISOU 3490 N LEU C 754 3409 3307 3805 272 -486 -135 N ATOM 3491 CA LEU C 754 44.439 18.364 36.745 1.00 30.04 C ANISOU 3491 CA LEU C 754 3679 3684 4052 270 -453 -177 C ATOM 3492 C LEU C 754 43.787 17.545 35.632 1.00 29.35 C ANISOU 3492 C LEU C 754 3622 3604 3926 241 -404 -169 C ATOM 3493 O LEU C 754 43.459 16.374 35.825 1.00 25.70 O ANISOU 3493 O LEU C 754 3151 3184 3430 216 -350 -167 O ATOM 3494 CB LEU C 754 43.375 19.105 37.555 1.00 36.57 C ANISOU 3494 CB LEU C 754 4469 4571 4856 317 -526 -254 C ATOM 3495 CG LEU C 754 43.788 19.636 38.930 1.00 39.64 C ANISOU 3495 CG LEU C 754 4814 4979 5269 352 -569 -277 C ATOM 3496 CD1 LEU C 754 42.663 20.463 39.534 1.00 40.08 C ANISOU 3496 CD1 LEU C 754 4839 5096 5294 410 -652 -356 C ATOM 3497 CD2 LEU C 754 44.188 18.508 39.871 1.00 36.76 C ANISOU 3497 CD2 LEU C 754 4409 4660 4897 330 -504 -257 C ATOM 3498 N MET C 755 43.589 18.166 34.473 1.00 25.29 N ANISOU 3498 N MET C 755 3142 3048 3417 245 -428 -164 N ATOM 3499 CA AMET C 755 43.021 17.476 33.318 0.50 27.60 C ANISOU 3499 CA AMET C 755 3466 3343 3677 222 -384 -155 C ATOM 3500 CA BMET C 755 43.011 17.468 33.335 0.50 27.53 C ANISOU 3500 CA BMET C 755 3457 3336 3669 222 -384 -156 C ATOM 3501 C MET C 755 43.953 16.355 32.879 1.00 27.25 C ANISOU 3501 C MET C 755 3445 3271 3639 187 -308 -91 C ATOM 3502 O MET C 755 43.516 15.241 32.588 1.00 29.88 O ANISOU 3502 O MET C 755 3789 3628 3936 163 -258 -90 O ATOM 3503 CB AMET C 755 42.799 18.452 32.156 0.50 28.84 C ANISOU 3503 CB AMET C 755 3653 3458 3848 237 -424 -156 C ATOM 3504 CB BMET C 755 42.716 18.444 32.190 0.50 28.51 C ANISOU 3504 CB BMET C 755 3609 3420 3803 238 -426 -160 C ATOM 3505 CG AMET C 755 42.372 17.788 30.848 0.50 29.74 C ANISOU 3505 CG AMET C 755 3799 3567 3935 216 -377 -141 C ATOM 3506 CG BMET C 755 41.671 19.506 32.535 0.50 27.89 C ANISOU 3506 CG BMET C 755 3516 3374 3708 278 -503 -230 C ATOM 3507 SD AMET C 755 42.386 18.907 29.426 0.50 56.80 S ANISOU 3507 SD AMET C 755 7255 6940 7387 231 -416 -125 S ATOM 3508 SD BMET C 755 41.198 20.565 31.149 0.50 66.03 S ANISOU 3508 SD BMET C 755 8381 8162 8545 295 -547 -239 S ATOM 3509 CE AMET C 755 41.754 17.832 28.139 0.50 39.74 C ANISOU 3509 CE AMET C 755 5121 4794 5183 208 -349 -118 C ATOM 3510 CE BMET C 755 42.641 21.615 30.983 0.50 16.04 C ANISOU 3510 CE BMET C 755 2064 1742 2290 297 -592 -179 C ATOM 3511 N ILE C 756 45.246 16.658 32.836 1.00 28.55 N ANISOU 3511 N ILE C 756 3618 3384 3845 185 -304 -36 N ATOM 3512 CA ILE C 756 46.246 15.663 32.457 1.00 26.78 C ANISOU 3512 CA ILE C 756 3416 3138 3621 160 -236 27 C ATOM 3513 C ILE C 756 46.204 14.451 33.389 1.00 21.09 C ANISOU 3513 C ILE C 756 2679 2459 2875 142 -186 20 C ATOM 3514 O ILE C 756 46.100 13.316 32.934 1.00 15.44 O ANISOU 3514 O ILE C 756 1988 1749 2131 121 -134 35 O ATOM 3515 CB ILE C 756 47.666 16.264 32.448 1.00 27.84 C ANISOU 3515 CB ILE C 756 3553 3226 3798 162 -245 89 C ATOM 3516 CG1 ILE C 756 47.761 17.367 31.389 1.00 33.77 C ANISOU 3516 CG1 ILE C 756 4322 3936 4574 172 -294 109 C ATOM 3517 CG2 ILE C 756 48.718 15.176 32.190 1.00 20.77 C ANISOU 3517 CG2 ILE C 756 2677 2322 2891 143 -173 153 C ATOM 3518 CD1 ILE C 756 49.038 18.168 31.457 1.00 40.17 C ANISOU 3518 CD1 ILE C 756 5130 4706 5429 172 -323 170 C ATOM 3519 N ILE C 757 46.277 14.697 34.693 1.00 19.91 N ANISOU 3519 N ILE C 757 2488 2338 2738 152 -206 -4 N ATOM 3520 CA ILE C 757 46.254 13.608 35.662 1.00 29.20 C ANISOU 3520 CA ILE C 757 3641 3559 3894 135 -162 -8 C ATOM 3521 C ILE C 757 45.001 12.752 35.477 1.00 25.58 C ANISOU 3521 C ILE C 757 3185 3147 3388 117 -147 -43 C ATOM 3522 O ILE C 757 45.068 11.520 35.506 1.00 20.76 O ANISOU 3522 O ILE C 757 2587 2547 2755 89 -96 -23 O ATOM 3523 CB ILE C 757 46.357 14.134 37.121 1.00 29.60 C ANISOU 3523 CB ILE C 757 3637 3646 3965 156 -195 -37 C ATOM 3524 CG1 ILE C 757 47.749 14.717 37.364 1.00 34.19 C ANISOU 3524 CG1 ILE C 757 4220 4180 4591 163 -197 9 C ATOM 3525 CG2 ILE C 757 46.067 13.020 38.123 1.00 30.85 C ANISOU 3525 CG2 ILE C 757 3761 3864 4097 138 -155 -48 C ATOM 3526 CD1 ILE C 757 47.945 15.320 38.739 1.00 36.53 C ANISOU 3526 CD1 ILE C 757 4464 4502 4911 188 -233 -19 C ATOM 3527 N HIS C 758 43.868 13.417 35.263 1.00 24.82 N ANISOU 3527 N HIS C 758 3078 3078 3273 133 -196 -92 N ATOM 3528 CA HIS C 758 42.594 12.744 35.028 1.00 28.11 C ANISOU 3528 CA HIS C 758 3494 3546 3639 115 -190 -124 C ATOM 3529 C HIS C 758 42.597 11.891 33.750 1.00 25.11 C ANISOU 3529 C HIS C 758 3169 3128 3242 88 -145 -94 C ATOM 3530 O HIS C 758 42.157 10.742 33.768 1.00 22.59 O ANISOU 3530 O HIS C 758 2859 2834 2890 56 -112 -90 O ATOM 3531 CB HIS C 758 41.463 13.773 34.960 1.00 31.36 C ANISOU 3531 CB HIS C 758 3887 3995 4032 145 -254 -182 C ATOM 3532 CG HIS C 758 40.134 13.185 34.600 1.00 37.98 C ANISOU 3532 CG HIS C 758 4727 4891 4813 126 -250 -211 C ATOM 3533 ND1 HIS C 758 39.206 12.807 35.546 1.00 45.55 N ANISOU 3533 ND1 HIS C 758 5638 5940 5728 122 -264 -244 N ATOM 3534 CD2 HIS C 758 39.576 12.912 33.396 1.00 40.88 C ANISOU 3534 CD2 HIS C 758 5135 5242 5157 111 -234 -210 C ATOM 3535 CE1 HIS C 758 38.133 12.327 34.942 1.00 42.84 C ANISOU 3535 CE1 HIS C 758 5307 5633 5336 100 -259 -259 C ATOM 3536 NE2 HIS C 758 38.331 12.380 33.637 1.00 41.77 N ANISOU 3536 NE2 HIS C 758 5227 5432 5213 94 -240 -241 N ATOM 3537 N ASP C 759 43.084 12.454 32.646 1.00 18.71 N ANISOU 3537 N ASP C 759 2395 2261 2454 100 -148 -70 N ATOM 3538 CA ASP C 759 43.149 11.714 31.381 1.00 22.26 C ANISOU 3538 CA ASP C 759 2893 2676 2887 84 -108 -41 C ATOM 3539 C ASP C 759 44.025 10.457 31.463 1.00 21.47 C ANISOU 3539 C ASP C 759 2818 2557 2783 63 -51 5 C ATOM 3540 O ASP C 759 43.663 9.412 30.921 1.00 23.65 O ANISOU 3540 O ASP C 759 3126 2831 3028 42 -21 9 O ATOM 3541 CB ASP C 759 43.630 12.610 30.234 1.00 25.11 C ANISOU 3541 CB ASP C 759 3278 2987 3275 106 -124 -18 C ATOM 3542 CG ASP C 759 42.612 13.677 29.852 1.00 34.11 C ANISOU 3542 CG ASP C 759 4408 4142 4410 125 -176 -64 C ATOM 3543 OD1 ASP C 759 41.422 13.528 30.208 1.00 38.43 O ANISOU 3543 OD1 ASP C 759 4939 4742 4921 120 -190 -114 O ATOM 3544 OD2 ASP C 759 43.006 14.666 29.192 1.00 31.41 O ANISOU 3544 OD2 ASP C 759 4074 3763 4099 145 -204 -48 O ATOM 3545 N ARG C 760 45.170 10.559 32.140 1.00 22.18 N ANISOU 3545 N ARG C 760 2896 2631 2902 70 -39 38 N ATOM 3546 CA ARG C 760 46.076 9.411 32.304 1.00 21.56 C ANISOU 3546 CA ARG C 760 2840 2536 2816 56 15 81 C ATOM 3547 C ARG C 760 45.479 8.314 33.181 1.00 17.42 C ANISOU 3547 C ARG C 760 2302 2052 2263 26 34 61 C ATOM 3548 O ARG C 760 45.634 7.121 32.894 1.00 18.94 O ANISOU 3548 O ARG C 760 2533 2232 2433 7 71 83 O ATOM 3549 CB ARG C 760 47.443 9.853 32.851 1.00 17.34 C ANISOU 3549 CB ARG C 760 2292 1982 2315 70 25 123 C ATOM 3550 CG ARG C 760 48.202 10.783 31.898 1.00 21.07 C ANISOU 3550 CG ARG C 760 2781 2414 2812 92 8 160 C ATOM 3551 CD ARG C 760 49.582 11.134 32.426 1.00 20.71 C ANISOU 3551 CD ARG C 760 2723 2354 2794 100 18 209 C ATOM 3552 NE ARG C 760 50.507 9.999 32.408 1.00 17.00 N ANISOU 3552 NE ARG C 760 2280 1880 2301 96 77 255 N ATOM 3553 CZ ARG C 760 51.098 9.521 31.312 1.00 17.30 C ANISOU 3553 CZ ARG C 760 2358 1898 2316 106 104 300 C ATOM 3554 NH1 ARG C 760 50.842 10.054 30.118 1.00 12.73 N ANISOU 3554 NH1 ARG C 760 1795 1303 1739 119 81 307 N ATOM 3555 NH2 ARG C 760 51.938 8.496 31.408 1.00 16.46 N ANISOU 3555 NH2 ARG C 760 2277 1792 2184 108 154 336 N ATOM 3556 N ARG C 761 44.802 8.715 34.255 1.00 16.24 N ANISOU 3556 N ARG C 761 2100 1956 2116 24 4 22 N ATOM 3557 CA ARG C 761 44.095 7.750 35.089 1.00 21.29 C ANISOU 3557 CA ARG C 761 2716 2647 2726 -6 13 6 C ATOM 3558 C ARG C 761 43.013 7.036 34.284 1.00 18.83 C ANISOU 3558 C ARG C 761 2435 2344 2373 -33 12 -9 C ATOM 3559 O ARG C 761 42.886 5.816 34.346 1.00 23.71 O ANISOU 3559 O ARG C 761 3075 2964 2968 -66 37 7 O ATOM 3560 CB ARG C 761 43.477 8.429 36.320 1.00 22.55 C ANISOU 3560 CB ARG C 761 2805 2876 2889 5 -27 -35 C ATOM 3561 CG ARG C 761 44.373 8.418 37.552 1.00 24.54 C ANISOU 3561 CG ARG C 761 3016 3141 3167 13 -12 -20 C ATOM 3562 CD ARG C 761 43.773 9.256 38.668 1.00 30.03 C ANISOU 3562 CD ARG C 761 3639 3905 3866 38 -60 -64 C ATOM 3563 NE ARG C 761 44.435 9.022 39.947 1.00 30.03 N ANISOU 3563 NE ARG C 761 3592 3934 3884 41 -42 -54 N ATOM 3564 CZ ARG C 761 44.559 9.946 40.894 1.00 32.02 C ANISOU 3564 CZ ARG C 761 3789 4219 4159 77 -78 -80 C ATOM 3565 NH1 ARG C 761 44.076 11.164 40.682 1.00 30.87 N ANISOU 3565 NH1 ARG C 761 3635 4076 4019 113 -138 -118 N ATOM 3566 NH2 ARG C 761 45.169 9.661 42.043 1.00 22.98 N ANISOU 3566 NH2 ARG C 761 2599 3102 3031 80 -56 -69 N ATOM 3567 N GLU C 762 42.233 7.802 33.529 1.00 23.65 N ANISOU 3567 N GLU C 762 3051 2960 2975 -20 -20 -38 N ATOM 3568 CA GLU C 762 41.140 7.226 32.748 1.00 25.09 C ANISOU 3568 CA GLU C 762 3260 3156 3116 -44 -23 -54 C ATOM 3569 C GLU C 762 41.659 6.245 31.701 1.00 21.52 C ANISOU 3569 C GLU C 762 2875 2643 2658 -56 15 -19 C ATOM 3570 O GLU C 762 41.083 5.177 31.506 1.00 25.53 O ANISOU 3570 O GLU C 762 3408 3157 3134 -91 24 -17 O ATOM 3571 CB GLU C 762 40.294 8.320 32.094 1.00 27.62 C ANISOU 3571 CB GLU C 762 3573 3492 3428 -21 -62 -92 C ATOM 3572 CG GLU C 762 39.492 9.149 33.091 1.00 33.31 C ANISOU 3572 CG GLU C 762 4231 4287 4137 -6 -108 -137 C ATOM 3573 CD GLU C 762 38.470 8.321 33.865 1.00 44.98 C ANISOU 3573 CD GLU C 762 5675 5846 5568 -42 -115 -152 C ATOM 3574 OE1 GLU C 762 37.759 7.501 33.240 1.00 44.08 O ANISOU 3574 OE1 GLU C 762 5591 5740 5418 -77 -104 -149 O ATOM 3575 OE2 GLU C 762 38.375 8.500 35.101 1.00 47.13 O ANISOU 3575 OE2 GLU C 762 5891 6179 5839 -35 -135 -165 O ATOM 3576 N PHE C 763 42.754 6.593 31.036 1.00 20.84 N ANISOU 3576 N PHE C 763 2817 2500 2600 -27 33 12 N ATOM 3577 CA PHE C 763 43.346 5.665 30.079 1.00 21.77 C ANISOU 3577 CA PHE C 763 2997 2569 2708 -27 67 46 C ATOM 3578 C PHE C 763 43.767 4.388 30.806 1.00 16.60 C ANISOU 3578 C PHE C 763 2357 1910 2040 -52 95 69 C ATOM 3579 O PHE C 763 43.463 3.273 30.361 1.00 12.84 O ANISOU 3579 O PHE C 763 1926 1418 1536 -74 106 74 O ATOM 3580 CB PHE C 763 44.542 6.292 29.351 1.00 17.26 C ANISOU 3580 CB PHE C 763 2443 1953 2164 13 79 83 C ATOM 3581 CG PHE C 763 45.264 5.335 28.441 1.00 20.26 C ANISOU 3581 CG PHE C 763 2881 2292 2526 25 112 121 C ATOM 3582 CD1 PHE C 763 46.533 4.870 28.762 1.00 20.80 C ANISOU 3582 CD1 PHE C 763 2963 2341 2598 38 143 164 C ATOM 3583 CD2 PHE C 763 44.665 4.881 27.272 1.00 24.08 C ANISOU 3583 CD2 PHE C 763 3404 2760 2984 27 111 111 C ATOM 3584 CE1 PHE C 763 47.203 3.980 27.923 1.00 23.90 C ANISOU 3584 CE1 PHE C 763 3412 2703 2967 58 169 196 C ATOM 3585 CE2 PHE C 763 45.327 3.990 26.429 1.00 25.27 C ANISOU 3585 CE2 PHE C 763 3610 2877 3116 47 136 141 C ATOM 3586 CZ PHE C 763 46.599 3.540 26.757 1.00 26.18 C ANISOU 3586 CZ PHE C 763 3741 2976 3231 65 163 184 C ATOM 3587 N ALA C 764 44.448 4.558 31.936 1.00 21.38 N ANISOU 3587 N ALA C 764 2925 2531 2666 -50 104 81 N ATOM 3588 CA ALA C 764 44.900 3.420 32.735 1.00 22.09 C ANISOU 3588 CA ALA C 764 3023 2622 2747 -73 132 103 C ATOM 3589 C ALA C 764 43.738 2.535 33.198 1.00 20.99 C ANISOU 3589 C ALA C 764 2877 2522 2578 -121 117 82 C ATOM 3590 O ALA C 764 43.853 1.309 33.187 1.00 21.19 O ANISOU 3590 O ALA C 764 2941 2525 2583 -146 133 101 O ATOM 3591 CB ALA C 764 45.714 3.899 33.932 1.00 14.40 C ANISOU 3591 CB ALA C 764 2000 1669 1803 -62 143 114 C ATOM 3592 N LYS C 765 42.627 3.149 33.606 1.00 15.62 N ANISOU 3592 N LYS C 765 2145 1900 1890 -133 81 46 N ATOM 3593 CA LYS C 765 41.432 2.375 33.964 1.00 20.00 C ANISOU 3593 CA LYS C 765 2686 2503 2408 -181 61 32 C ATOM 3594 C LYS C 765 41.016 1.488 32.796 1.00 23.12 C ANISOU 3594 C LYS C 765 3153 2856 2776 -203 63 38 C ATOM 3595 O LYS C 765 40.668 0.311 32.974 1.00 21.73 O ANISOU 3595 O LYS C 765 3000 2679 2576 -246 61 52 O ATOM 3596 CB LYS C 765 40.251 3.287 34.325 1.00 16.07 C ANISOU 3596 CB LYS C 765 2128 2081 1895 -181 19 -10 C ATOM 3597 CG LYS C 765 40.305 3.930 35.705 1.00 28.49 C ANISOU 3597 CG LYS C 765 3621 3720 3483 -167 4 -23 C ATOM 3598 CD LYS C 765 39.008 4.695 35.971 1.00 36.87 C ANISOU 3598 CD LYS C 765 4628 4865 4514 -163 -44 -66 C ATOM 3599 CE LYS C 765 39.167 5.700 37.093 1.00 45.35 C ANISOU 3599 CE LYS C 765 5630 5993 5607 -124 -67 -89 C ATOM 3600 NZ LYS C 765 37.931 6.513 37.285 1.00 49.64 N ANISOU 3600 NZ LYS C 765 6126 6621 6115 -107 -118 -135 N ATOM 3601 N PHE C 766 41.046 2.066 31.600 1.00 19.69 N ANISOU 3601 N PHE C 766 2752 2385 2346 -172 63 29 N ATOM 3602 CA PHE C 766 40.603 1.362 30.396 1.00 21.08 C ANISOU 3602 CA PHE C 766 2991 2523 2495 -183 62 30 C ATOM 3603 C PHE C 766 41.521 0.178 30.101 1.00 19.58 C ANISOU 3603 C PHE C 766 2866 2271 2303 -182 87 64 C ATOM 3604 O PHE C 766 41.053 -0.938 29.851 1.00 20.43 O ANISOU 3604 O PHE C 766 3017 2361 2383 -217 78 69 O ATOM 3605 CB PHE C 766 40.543 2.328 29.202 1.00 18.28 C ANISOU 3605 CB PHE C 766 2649 2148 2149 -143 58 14 C ATOM 3606 CG PHE C 766 40.518 1.643 27.865 1.00 18.66 C ANISOU 3606 CG PHE C 766 2766 2145 2179 -136 67 21 C ATOM 3607 CD1 PHE C 766 41.644 1.634 27.056 1.00 22.07 C ANISOU 3607 CD1 PHE C 766 3237 2523 2625 -91 91 48 C ATOM 3608 CD2 PHE C 766 39.376 0.998 27.424 1.00 20.96 C ANISOU 3608 CD2 PHE C 766 3080 2448 2435 -173 48 3 C ATOM 3609 CE1 PHE C 766 41.626 0.999 25.818 1.00 24.35 C ANISOU 3609 CE1 PHE C 766 3586 2771 2895 -75 95 52 C ATOM 3610 CE2 PHE C 766 39.349 0.352 26.194 1.00 25.05 C ANISOU 3610 CE2 PHE C 766 3663 2919 2937 -163 53 7 C ATOM 3611 CZ PHE C 766 40.476 0.355 25.391 1.00 27.14 C ANISOU 3611 CZ PHE C 766 3964 3130 3217 -110 76 29 C ATOM 3612 N GLU C 767 42.828 0.425 30.155 1.00 18.60 N ANISOU 3612 N GLU C 767 2750 2115 2204 -142 116 90 N ATOM 3613 CA GLU C 767 43.825 -0.608 29.867 1.00 21.24 C ANISOU 3613 CA GLU C 767 3146 2396 2529 -128 141 123 C ATOM 3614 C GLU C 767 43.658 -1.825 30.774 1.00 24.03 C ANISOU 3614 C GLU C 767 3509 2753 2867 -175 139 133 C ATOM 3615 O GLU C 767 43.865 -2.966 30.351 1.00 22.71 O ANISOU 3615 O GLU C 767 3408 2541 2678 -180 140 148 O ATOM 3616 CB GLU C 767 45.245 -0.047 30.014 1.00 19.20 C ANISOU 3616 CB GLU C 767 2877 2122 2294 -81 172 152 C ATOM 3617 CG GLU C 767 45.673 0.881 28.888 1.00 32.66 C ANISOU 3617 CG GLU C 767 4590 3810 4010 -32 174 158 C ATOM 3618 CD GLU C 767 45.871 0.148 27.568 1.00 43.61 C ANISOU 3618 CD GLU C 767 6047 5154 5369 -5 178 169 C ATOM 3619 OE1 GLU C 767 44.865 -0.098 26.868 1.00 45.01 O ANISOU 3619 OE1 GLU C 767 6246 5327 5530 -20 157 143 O ATOM 3620 OE2 GLU C 767 47.033 -0.173 27.227 1.00 46.79 O ANISOU 3620 OE2 GLU C 767 6483 5533 5763 35 201 204 O ATOM 3621 N LYS C 768 43.289 -1.568 32.024 1.00 23.37 N ANISOU 3621 N LYS C 768 3359 2726 2795 -205 132 127 N ATOM 3622 CA LYS C 768 43.095 -2.629 33.006 1.00 26.54 C ANISOU 3622 CA LYS C 768 3754 3143 3184 -254 128 141 C ATOM 3623 C LYS C 768 41.758 -3.332 32.793 1.00 25.82 C ANISOU 3623 C LYS C 768 3679 3070 3063 -310 89 130 C ATOM 3624 O LYS C 768 41.696 -4.558 32.732 1.00 29.39 O ANISOU 3624 O LYS C 768 4182 3488 3496 -343 80 148 O ATOM 3625 CB LYS C 768 43.151 -2.046 34.422 1.00 28.32 C ANISOU 3625 CB LYS C 768 3893 3435 3432 -262 133 138 C ATOM 3626 CG LYS C 768 42.978 -3.069 35.537 1.00 28.75 C ANISOU 3626 CG LYS C 768 3927 3518 3477 -311 130 157 C ATOM 3627 CD LYS C 768 44.167 -4.014 35.620 1.00 30.21 C ANISOU 3627 CD LYS C 768 4167 3645 3665 -300 164 190 C ATOM 3628 CE LYS C 768 44.115 -4.806 36.920 1.00 34.89 C ANISOU 3628 CE LYS C 768 4723 4276 4259 -344 165 209 C ATOM 3629 NZ LYS C 768 45.299 -5.675 37.056 1.00 37.94 N ANISOU 3629 NZ LYS C 768 5162 4608 4645 -328 200 239 N ATOM 3630 N GLU C 769 40.695 -2.539 32.682 1.00 21.19 N ANISOU 3630 N GLU C 769 3047 2537 2469 -321 64 101 N ATOM 3631 CA GLU C 769 39.340 -3.062 32.528 1.00 26.75 C ANISOU 3631 CA GLU C 769 3752 3274 3137 -377 25 92 C ATOM 3632 C GLU C 769 39.200 -3.982 31.318 1.00 21.71 C ANISOU 3632 C GLU C 769 3205 2565 2477 -386 16 97 C ATOM 3633 O GLU C 769 38.519 -5.002 31.387 1.00 29.39 O ANISOU 3633 O GLU C 769 4205 3537 3425 -442 -13 110 O ATOM 3634 CB GLU C 769 38.331 -1.909 32.433 1.00 29.90 C ANISOU 3634 CB GLU C 769 4094 3742 3525 -371 4 57 C ATOM 3635 CG GLU C 769 36.884 -2.305 32.738 1.00 35.85 C ANISOU 3635 CG GLU C 769 4817 4568 4236 -433 -37 52 C ATOM 3636 CD GLU C 769 36.241 -3.104 31.617 1.00 42.67 C ANISOU 3636 CD GLU C 769 5753 5389 5070 -464 -54 54 C ATOM 3637 OE1 GLU C 769 35.302 -3.877 31.898 1.00 41.87 O ANISOU 3637 OE1 GLU C 769 5647 5326 4934 -529 -88 68 O ATOM 3638 OE2 GLU C 769 36.678 -2.963 30.454 1.00 45.72 O ANISOU 3638 OE2 GLU C 769 6199 5707 5467 -424 -37 44 O ATOM 3639 N LYS C 770 39.844 -3.620 30.213 1.00 22.40 N ANISOU 3639 N LYS C 770 3339 2595 2575 -330 36 91 N ATOM 3640 CA LYS C 770 39.702 -4.378 28.971 1.00 26.34 C ANISOU 3640 CA LYS C 770 3922 3033 3054 -325 25 90 C ATOM 3641 C LYS C 770 40.193 -5.819 29.129 1.00 26.26 C ANISOU 3641 C LYS C 770 3979 2967 3033 -346 18 117 C ATOM 3642 O LYS C 770 39.793 -6.708 28.369 1.00 25.94 O ANISOU 3642 O LYS C 770 4006 2881 2969 -362 -8 117 O ATOM 3643 CB LYS C 770 40.418 -3.675 27.807 1.00 28.25 C ANISOU 3643 CB LYS C 770 4190 3235 3308 -253 50 82 C ATOM 3644 CG LYS C 770 41.943 -3.771 27.832 1.00 28.70 C ANISOU 3644 CG LYS C 770 4273 3250 3383 -200 83 108 C ATOM 3645 CD LYS C 770 42.559 -3.086 26.608 1.00 27.98 C ANISOU 3645 CD LYS C 770 4200 3132 3298 -132 101 107 C ATOM 3646 CE LYS C 770 44.045 -3.397 26.494 1.00 25.07 C ANISOU 3646 CE LYS C 770 3867 2727 2932 -78 129 140 C ATOM 3647 NZ LYS C 770 44.715 -2.635 25.405 1.00 32.57 N ANISOU 3647 NZ LYS C 770 4821 3668 3887 -12 144 148 N ATOM 3648 N MET C 771 41.056 -6.045 30.116 1.00 24.58 N ANISOU 3648 N MET C 771 3748 2754 2836 -342 39 140 N ATOM 3649 CA AMET C 771 41.567 -7.392 30.331 0.75 27.52 C ANISOU 3649 CA AMET C 771 4185 3074 3197 -359 32 166 C ATOM 3650 CA BMET C 771 41.584 -7.370 30.440 0.25 27.17 C ANISOU 3650 CA BMET C 771 4134 3034 3154 -360 34 167 C ATOM 3651 C MET C 771 40.477 -8.313 30.896 1.00 31.03 C ANISOU 3651 C MET C 771 4629 3539 3623 -444 -13 176 C ATOM 3652 O MET C 771 40.667 -9.529 30.964 1.00 27.64 O ANISOU 3652 O MET C 771 4262 3060 3182 -468 -34 197 O ATOM 3653 CB AMET C 771 42.821 -7.379 31.216 0.75 25.65 C ANISOU 3653 CB AMET C 771 3930 2836 2981 -330 72 188 C ATOM 3654 CB BMET C 771 42.619 -7.266 31.567 0.25 25.60 C ANISOU 3654 CB BMET C 771 3897 2851 2978 -345 69 188 C ATOM 3655 CG AMET C 771 43.994 -6.580 30.630 0.75 21.44 C ANISOU 3655 CG AMET C 771 3403 2282 2460 -249 113 189 C ATOM 3656 CG BMET C 771 44.056 -7.038 31.127 0.25 24.52 C ANISOU 3656 CG BMET C 771 3795 2673 2849 -269 111 199 C ATOM 3657 SD AMET C 771 44.300 -6.929 28.872 0.75 44.04 S ANISOU 3657 SD AMET C 771 6361 5076 5298 -191 105 182 S ATOM 3658 SD BMET C 771 45.200 -7.187 32.519 0.25 31.94 S ANISOU 3658 SD BMET C 771 4699 3631 3807 -263 151 227 S ATOM 3659 CE AMET C 771 44.794 -8.650 28.937 0.75 43.64 C ANISOU 3659 CE AMET C 771 6405 4958 5218 -197 88 203 C ATOM 3660 CE BMET C 771 46.674 -7.753 31.676 0.25 33.61 C ANISOU 3660 CE BMET C 771 5001 3772 3997 -188 180 247 C ATOM 3661 N ASN C 772 39.330 -7.737 31.254 1.00 28.05 N ANISOU 3661 N ASN C 772 4182 3237 3239 -487 -34 163 N ATOM 3662 CA ASN C 772 38.213 -8.511 31.791 1.00 28.18 C ANISOU 3662 CA ASN C 772 4186 3292 3232 -572 -81 179 C ATOM 3663 C ASN C 772 37.259 -9.047 30.727 1.00 30.24 C ANISOU 3663 C ASN C 772 4507 3522 3462 -604 -123 171 C ATOM 3664 O ASN C 772 36.371 -9.844 31.032 1.00 29.19 O ANISOU 3664 O ASN C 772 4378 3409 3305 -679 -169 191 O ATOM 3665 CB ASN C 772 37.425 -7.683 32.812 1.00 37.79 C ANISOU 3665 CB ASN C 772 5291 4622 4446 -602 -87 174 C ATOM 3666 CG ASN C 772 38.221 -7.396 34.079 1.00 43.16 C ANISOU 3666 CG ASN C 772 5906 5339 5154 -587 -57 188 C ATOM 3667 OD1 ASN C 772 39.220 -8.056 34.361 1.00 44.05 O ANISOU 3667 OD1 ASN C 772 6056 5398 5282 -574 -36 209 O ATOM 3668 ND2 ASN C 772 37.778 -6.406 34.848 1.00 40.97 N ANISOU 3668 ND2 ASN C 772 5532 5156 4879 -584 -55 173 N ATOM 3669 N ALA C 773 37.434 -8.606 29.485 1.00 27.53 N ANISOU 3669 N ALA C 773 4207 3135 3118 -548 -108 144 N ATOM 3670 CA ALA C 773 36.531 -8.994 28.405 1.00 27.39 C ANISOU 3670 CA ALA C 773 4242 3092 3072 -570 -143 131 C ATOM 3671 C ALA C 773 36.548 -10.499 28.172 1.00 34.72 C ANISOU 3671 C ALA C 773 5262 3945 3986 -608 -186 153 C ATOM 3672 O ALA C 773 37.596 -11.140 28.267 1.00 35.43 O ANISOU 3672 O ALA C 773 5405 3971 4087 -576 -177 168 O ATOM 3673 CB ALA C 773 36.876 -8.254 27.119 1.00 15.83 C ANISOU 3673 CB ALA C 773 2806 1595 1615 -494 -115 100 C ATOM 3674 N LYS C 774 35.383 -11.058 27.865 1.00 34.66 N ANISOU 3674 N LYS C 774 5276 3946 3949 -674 -236 157 N ATOM 3675 CA LYS C 774 35.267 -12.490 27.604 1.00 41.57 C ANISOU 3675 CA LYS C 774 6242 4745 4809 -716 -290 179 C ATOM 3676 C LYS C 774 35.204 -12.791 26.107 1.00 41.29 C ANISOU 3676 C LYS C 774 6296 4634 4760 -675 -305 152 C ATOM 3677 O LYS C 774 34.322 -12.296 25.396 1.00 41.27 O ANISOU 3677 O LYS C 774 6278 4663 4741 -683 -310 130 O ATOM 3678 CB LYS C 774 34.031 -13.056 28.307 1.00 47.39 C ANISOU 3678 CB LYS C 774 6948 5539 5521 -827 -346 211 C ATOM 3679 CG LYS C 774 33.847 -12.515 29.711 1.00 58.01 C ANISOU 3679 CG LYS C 774 8181 6988 6871 -862 -330 231 C ATOM 3680 CD LYS C 774 33.153 -13.516 30.621 1.00 65.78 C ANISOU 3680 CD LYS C 774 9152 8005 7837 -966 -389 281 C ATOM 3681 CE LYS C 774 33.271 -13.090 32.079 1.00 68.05 C ANISOU 3681 CE LYS C 774 9331 8389 8136 -985 -369 304 C ATOM 3682 NZ LYS C 774 32.649 -14.070 33.011 1.00 71.68 N ANISOU 3682 NZ LYS C 774 9769 8889 8579 -1085 -427 360 N ATOM 3683 N TRP C 775 36.147 -13.602 25.636 1.00 36.67 N ANISOU 3683 N TRP C 775 5801 3954 4179 -627 -314 154 N ATOM 3684 CA TRP C 775 36.168 -14.016 24.239 1.00 42.09 C ANISOU 3684 CA TRP C 775 6576 4566 4850 -579 -336 129 C ATOM 3685 C TRP C 775 34.868 -14.699 23.853 1.00 47.64 C ANISOU 3685 C TRP C 775 7314 5260 5526 -659 -401 132 C ATOM 3686 O TRP C 775 34.506 -15.729 24.429 1.00 53.38 O ANISOU 3686 O TRP C 775 8075 5962 6244 -735 -457 164 O ATOM 3687 CB TRP C 775 37.347 -14.947 23.979 1.00 42.54 C ANISOU 3687 CB TRP C 775 6727 4528 4907 -519 -347 133 C ATOM 3688 CG TRP C 775 38.646 -14.240 24.078 1.00 44.12 C ANISOU 3688 CG TRP C 775 6900 4738 5125 -430 -282 129 C ATOM 3689 CD1 TRP C 775 39.598 -14.405 25.036 1.00 40.97 C ANISOU 3689 CD1 TRP C 775 6489 4339 4739 -419 -258 152 C ATOM 3690 CD2 TRP C 775 39.134 -13.223 23.196 1.00 42.65 C ANISOU 3690 CD2 TRP C 775 6690 4570 4945 -343 -234 103 C ATOM 3691 NE1 TRP C 775 40.656 -13.564 24.801 1.00 41.92 N ANISOU 3691 NE1 TRP C 775 6582 4475 4869 -331 -198 144 N ATOM 3692 CE2 TRP C 775 40.398 -12.827 23.676 1.00 40.96 C ANISOU 3692 CE2 TRP C 775 6452 4365 4745 -284 -184 116 C ATOM 3693 CE3 TRP C 775 38.627 -12.614 22.042 1.00 33.01 C ANISOU 3693 CE3 TRP C 775 5464 3361 3718 -310 -227 74 C ATOM 3694 CZ2 TRP C 775 41.165 -11.849 23.044 1.00 39.15 C ANISOU 3694 CZ2 TRP C 775 6194 4157 4524 -198 -135 105 C ATOM 3695 CZ3 TRP C 775 39.389 -11.642 21.415 1.00 32.61 C ANISOU 3695 CZ3 TRP C 775 5383 3330 3678 -222 -177 62 C ATOM 3696 CH2 TRP C 775 40.645 -11.269 21.917 1.00 37.53 C ANISOU 3696 CH2 TRP C 775 5983 3962 4314 -169 -133 79 C ATOM 3697 N ASP C 776 34.168 -14.123 22.880 0.50 38.71 N ANISOU 3697 N ASP C 776 6175 4151 4383 -644 -394 103 N ATOM 3698 CA ASP C 776 32.863 -14.638 22.497 0.50 34.74 C ANISOU 3698 CA ASP C 776 5695 3652 3851 -722 -451 106 C ATOM 3699 C ASP C 776 32.896 -16.154 22.404 0.50 39.60 C ANISOU 3699 C ASP C 776 6417 4173 4456 -760 -526 127 C ATOM 3700 O ASP C 776 33.860 -16.742 21.912 0.50 31.16 O ANISOU 3700 O ASP C 776 5430 3016 3394 -691 -534 116 O ATOM 3701 CB ASP C 776 32.374 -14.027 21.186 0.50 34.31 C ANISOU 3701 CB ASP C 776 5647 3605 3785 -677 -433 65 C ATOM 3702 CG ASP C 776 30.969 -14.473 20.831 0.50 33.07 C ANISOU 3702 CG ASP C 776 5505 3465 3594 -761 -487 70 C ATOM 3703 OD1 ASP C 776 30.765 -15.689 20.644 0.50 27.42 O ANISOU 3703 OD1 ASP C 776 4874 2678 2866 -803 -555 86 O ATOM 3704 OD2 ASP C 776 30.069 -13.611 20.742 0.50 33.03 O ANISOU 3704 OD2 ASP C 776 5430 3546 3572 -785 -464 58 O ATOM 3705 N THR C 777 31.826 -16.767 22.897 1.00 56.54 N ANISOU 3705 N THR C 777 8558 6342 6581 -871 -586 160 N ATOM 3706 CA THR C 777 31.696 -18.218 23.002 1.00 71.67 C ANISOU 3706 CA THR C 777 10568 8176 8488 -931 -671 190 C ATOM 3707 C THR C 777 32.306 -19.013 21.841 1.00 72.81 C ANISOU 3707 C THR C 777 10839 8196 8631 -857 -705 161 C ATOM 3708 O THR C 777 32.842 -20.103 22.048 1.00 68.20 O ANISOU 3708 O THR C 777 10338 7525 8049 -861 -757 178 O ATOM 3709 CB THR C 777 30.213 -18.622 23.175 1.00 81.54 C ANISOU 3709 CB THR C 777 11802 9471 9707 -1055 -735 222 C ATOM 3710 OG1 THR C 777 30.109 -20.045 23.310 1.00 88.27 O ANISOU 3710 OG1 THR C 777 12748 10237 10554 -1119 -826 257 O ATOM 3711 CG2 THR C 777 29.387 -18.161 21.981 1.00 82.26 C ANISOU 3711 CG2 THR C 777 11901 9580 9776 -1040 -730 186 C ATOM 3712 N GLN C 778 32.226 -18.477 20.627 1.00 75.47 N ANISOU 3712 N GLN C 778 11188 8526 8961 -786 -678 116 N ATOM 3713 CA GLN C 778 32.725 -19.205 19.463 1.00 78.98 C ANISOU 3713 CA GLN C 778 11746 8864 9398 -709 -715 86 C ATOM 3714 C GLN C 778 33.633 -18.371 18.555 1.00 74.44 C ANISOU 3714 C GLN C 778 11160 8291 8832 -574 -646 43 C ATOM 3715 O GLN C 778 33.377 -17.188 18.320 1.00 67.12 O ANISOU 3715 O GLN C 778 10149 7443 7911 -553 -582 25 O ATOM 3716 CB GLN C 778 31.565 -19.795 18.655 1.00 84.14 C ANISOU 3716 CB GLN C 778 12454 9488 10027 -766 -784 79 C ATOM 3717 CG GLN C 778 32.017 -20.681 17.509 1.00 89.88 C ANISOU 3717 CG GLN C 778 13305 10099 10745 -689 -837 48 C ATOM 3718 CD GLN C 778 30.878 -21.117 16.615 1.00 96.14 C ANISOU 3718 CD GLN C 778 14147 10868 11516 -736 -897 35 C ATOM 3719 OE1 GLN C 778 29.715 -21.103 17.018 1.00 99.09 O ANISOU 3719 OE1 GLN C 778 14480 11295 11876 -850 -922 64 O ATOM 3720 NE2 GLN C 778 31.207 -21.511 15.388 1.00 96.56 N ANISOU 3720 NE2 GLN C 778 14282 10845 11559 -645 -923 -6 N ATOM 3721 N GLU C 779 34.687 -19.008 18.045 1.00 73.84 N ANISOU 3721 N GLU C 779 11170 8132 8754 -483 -663 28 N ATOM 3722 CA GLU C 779 35.657 -18.358 17.164 1.00 69.06 C ANISOU 3722 CA GLU C 779 10560 7529 8150 -350 -607 -6 C ATOM 3723 C GLU C 779 35.192 -18.313 15.712 1.00 63.57 C ANISOU 3723 C GLU C 779 9900 6815 7439 -298 -623 -45 C ATOM 3724 O GLU C 779 34.591 -19.262 15.211 1.00 63.16 O ANISOU 3724 O GLU C 779 9930 6698 7370 -328 -698 -53 O ATOM 3725 CB GLU C 779 37.009 -19.063 17.243 1.00 68.94 C ANISOU 3725 CB GLU C 779 10619 7447 8130 -267 -620 -3 C ATOM 3726 CG GLU C 779 37.642 -19.026 18.614 1.00 76.44 C ANISOU 3726 CG GLU C 779 11529 8419 9095 -301 -592 33 C ATOM 3727 CD GLU C 779 38.980 -19.721 18.635 1.00 88.48 C ANISOU 3727 CD GLU C 779 13130 9883 10606 -213 -602 35 C ATOM 3728 OE1 GLU C 779 39.421 -20.183 17.560 1.00 94.73 O ANISOU 3728 OE1 GLU C 779 14000 10619 11373 -120 -632 6 O ATOM 3729 OE2 GLU C 779 39.590 -19.807 19.721 1.00 91.59 O ANISOU 3729 OE2 GLU C 779 13502 10288 11011 -234 -581 63 O ATOM 3730 N ASN C 780 35.501 -17.208 15.041 1.00 52.64 N ANISOU 3730 N ASN C 780 8453 5486 6062 -219 -554 -69 N ATOM 3731 CA ASN C 780 35.001 -16.934 13.701 1.00 39.74 C ANISOU 3731 CA ASN C 780 6826 3855 4417 -171 -553 -105 C ATOM 3732 C ASN C 780 35.137 -18.085 12.707 1.00 36.76 C ANISOU 3732 C ASN C 780 6566 3385 4015 -114 -626 -130 C ATOM 3733 O ASN C 780 36.246 -18.440 12.307 1.00 31.79 O ANISOU 3733 O ASN C 780 5988 2717 3376 -8 -633 -140 O ATOM 3734 CB ASN C 780 35.679 -15.696 13.133 1.00 36.50 C ANISOU 3734 CB ASN C 780 6342 3508 4019 -73 -473 -120 C ATOM 3735 CG ASN C 780 35.030 -15.226 11.862 1.00 29.98 C ANISOU 3735 CG ASN C 780 5499 2705 3185 -36 -461 -155 C ATOM 3736 OD1 ASN C 780 34.067 -15.830 11.391 1.00 30.53 O ANISOU 3736 OD1 ASN C 780 5615 2744 3240 -82 -511 -170 O ATOM 3737 ND2 ASN C 780 35.542 -14.136 11.299 1.00 23.66 N ANISOU 3737 ND2 ASN C 780 4631 1961 2396 44 -396 -165 N ATOM 3738 N PRO C 781 33.996 -18.650 12.286 1.00 37.52 N ANISOU 3738 N PRO C 781 6704 3452 4098 -180 -684 -140 N ATOM 3739 CA PRO C 781 33.948 -19.791 11.364 1.00 38.47 C ANISOU 3739 CA PRO C 781 6942 3479 4197 -138 -767 -166 C ATOM 3740 C PRO C 781 34.431 -19.425 9.962 1.00 34.69 C ANISOU 3740 C PRO C 781 6468 3006 3708 0 -742 -209 C ATOM 3741 O PRO C 781 34.779 -20.316 9.194 1.00 34.22 O ANISOU 3741 O PRO C 781 6503 2872 3626 74 -805 -233 O ATOM 3742 CB PRO C 781 32.455 -20.149 11.318 1.00 37.10 C ANISOU 3742 CB PRO C 781 6781 3301 4015 -258 -818 -161 C ATOM 3743 CG PRO C 781 31.828 -19.425 12.466 1.00 38.05 C ANISOU 3743 CG PRO C 781 6802 3506 4148 -370 -774 -124 C ATOM 3744 CD PRO C 781 32.651 -18.210 12.687 1.00 35.24 C ANISOU 3744 CD PRO C 781 6354 3225 3813 -300 -677 -127 C ATOM 3745 N ILE C 782 34.451 -18.139 9.629 1.00 33.30 N ANISOU 3745 N ILE C 782 6190 2919 3545 36 -657 -217 N ATOM 3746 CA ILE C 782 34.891 -17.731 8.298 1.00 29.84 C ANISOU 3746 CA ILE C 782 5742 2498 3097 165 -630 -252 C ATOM 3747 C ILE C 782 36.279 -17.100 8.304 1.00 34.28 C ANISOU 3747 C ILE C 782 6261 3099 3664 273 -573 -242 C ATOM 3748 O ILE C 782 36.736 -16.588 7.274 1.00 31.72 O ANISOU 3748 O ILE C 782 5909 2811 3334 381 -542 -261 O ATOM 3749 CB ILE C 782 33.892 -16.771 7.609 1.00 28.58 C ANISOU 3749 CB ILE C 782 5505 2408 2945 143 -583 -272 C ATOM 3750 CG1 ILE C 782 33.946 -15.375 8.248 1.00 26.20 C ANISOU 3750 CG1 ILE C 782 5083 2203 2670 115 -494 -251 C ATOM 3751 CG2 ILE C 782 32.484 -17.358 7.634 1.00 29.83 C ANISOU 3751 CG2 ILE C 782 5701 2540 3094 29 -637 -277 C ATOM 3752 CD1 ILE C 782 33.023 -14.370 7.591 1.00 28.15 C ANISOU 3752 CD1 ILE C 782 5253 2521 2922 100 -445 -272 C ATOM 3753 N TYR C 783 36.947 -17.130 9.456 1.00 32.77 N ANISOU 3753 N TYR C 783 6061 2908 3482 244 -559 -208 N ATOM 3754 CA TYR C 783 38.333 -16.671 9.514 1.00 37.20 C ANISOU 3754 CA TYR C 783 6592 3501 4040 344 -512 -194 C ATOM 3755 C TYR C 783 39.186 -17.492 8.546 1.00 40.39 C ANISOU 3755 C TYR C 783 7081 3858 4407 476 -559 -216 C ATOM 3756 O TYR C 783 39.085 -18.718 8.507 1.00 43.10 O ANISOU 3756 O TYR C 783 7531 4117 4729 473 -639 -228 O ATOM 3757 CB TYR C 783 38.901 -16.777 10.933 1.00 35.20 C ANISOU 3757 CB TYR C 783 6332 3244 3800 289 -500 -156 C ATOM 3758 CG TYR C 783 40.378 -16.436 11.012 1.00 38.64 C ANISOU 3758 CG TYR C 783 6748 3709 4226 392 -458 -138 C ATOM 3759 CD1 TYR C 783 40.809 -15.113 11.077 1.00 31.86 C ANISOU 3759 CD1 TYR C 783 5784 2935 3388 417 -379 -121 C ATOM 3760 CD2 TYR C 783 41.345 -17.438 11.006 1.00 40.32 C ANISOU 3760 CD2 TYR C 783 7048 3866 4404 465 -502 -136 C ATOM 3761 CE1 TYR C 783 42.164 -14.801 11.146 1.00 35.62 C ANISOU 3761 CE1 TYR C 783 6240 3443 3852 505 -344 -98 C ATOM 3762 CE2 TYR C 783 42.699 -17.135 11.071 1.00 37.24 C ANISOU 3762 CE2 TYR C 783 6639 3513 3997 559 -463 -116 C ATOM 3763 CZ TYR C 783 43.104 -15.821 11.143 1.00 39.54 C ANISOU 3763 CZ TYR C 783 6822 3891 4309 577 -384 -95 C ATOM 3764 OH TYR C 783 44.451 -15.528 11.213 1.00 40.16 O ANISOU 3764 OH TYR C 783 6881 4011 4368 665 -349 -69 O ATOM 3765 N LYS C 784 40.013 -16.812 7.758 1.00 40.41 N ANISOU 3765 N LYS C 784 7037 3918 4400 593 -515 -218 N ATOM 3766 CA LYS C 784 40.928 -17.488 6.842 1.00 46.50 C ANISOU 3766 CA LYS C 784 7875 4665 5126 734 -555 -236 C ATOM 3767 C LYS C 784 42.359 -17.157 7.216 1.00 44.84 C ANISOU 3767 C LYS C 784 7636 4500 4900 813 -515 -203 C ATOM 3768 O LYS C 784 42.732 -15.985 7.278 1.00 40.86 O ANISOU 3768 O LYS C 784 7032 4078 4415 824 -442 -179 O ATOM 3769 CB LYS C 784 40.700 -17.040 5.396 1.00 53.59 C ANISOU 3769 CB LYS C 784 8739 5606 6015 822 -545 -266 C ATOM 3770 CG LYS C 784 39.279 -17.174 4.879 1.00 64.76 C ANISOU 3770 CG LYS C 784 10166 6995 7445 753 -571 -299 C ATOM 3771 CD LYS C 784 39.152 -16.486 3.520 1.00 72.02 C ANISOU 3771 CD LYS C 784 11028 7977 8361 842 -540 -323 C ATOM 3772 CE LYS C 784 37.702 -16.329 3.086 1.00 74.08 C ANISOU 3772 CE LYS C 784 11274 8233 8640 762 -544 -351 C ATOM 3773 NZ LYS C 784 37.588 -15.413 1.916 1.00 74.24 N ANISOU 3773 NZ LYS C 784 11213 8330 8665 838 -494 -367 N ATOM 3774 N SER C 785 43.164 -18.183 7.461 1.00 43.91 N ANISOU 3774 N SER C 785 7610 4330 4745 867 -565 -202 N ATOM 3775 CA SER C 785 44.582 -17.973 7.694 1.00 47.21 C ANISOU 3775 CA SER C 785 8009 4795 5134 957 -532 -172 C ATOM 3776 C SER C 785 45.172 -17.261 6.473 1.00 52.88 C ANISOU 3776 C SER C 785 8666 5597 5827 1086 -501 -173 C ATOM 3777 O SER C 785 44.700 -17.450 5.350 1.00 54.76 O ANISOU 3777 O SER C 785 8923 5830 6054 1141 -533 -208 O ATOM 3778 CB SER C 785 45.284 -19.308 7.945 1.00 50.59 C ANISOU 3778 CB SER C 785 8557 5150 5513 1011 -602 -179 C ATOM 3779 OG SER C 785 46.513 -19.117 8.624 1.00 56.00 O ANISOU 3779 OG SER C 785 9222 5876 6177 1053 -562 -141 O ATOM 3780 N PRO C 786 46.185 -16.440 6.713 1.00 52.38 N ANISOU 3780 N PRO C 786 8526 5616 5758 1133 -439 -132 N ATOM 3781 CA PRO C 786 46.807 -15.636 5.665 1.00 57.91 C ANISOU 3781 CA PRO C 786 9156 6410 6437 1248 -407 -120 C ATOM 3782 C PRO C 786 47.671 -16.467 4.727 1.00 68.65 C ANISOU 3782 C PRO C 786 10584 7777 7722 1406 -461 -135 C ATOM 3783 O PRO C 786 47.846 -17.668 4.920 1.00 65.96 O ANISOU 3783 O PRO C 786 10353 7364 7346 1431 -525 -155 O ATOM 3784 CB PRO C 786 47.718 -14.714 6.477 1.00 51.20 C ANISOU 3784 CB PRO C 786 8218 5636 5601 1235 -335 -63 C ATOM 3785 CG PRO C 786 46.953 -14.513 7.708 1.00 49.36 C ANISOU 3785 CG PRO C 786 7989 5353 5414 1093 -318 -55 C ATOM 3786 CD PRO C 786 46.559 -15.922 8.035 1.00 49.90 C ANISOU 3786 CD PRO C 786 8176 5319 5466 1063 -391 -90 C ATOM 3787 N ILE C 787 48.219 -15.805 3.718 1.00 77.79 N ANISOU 3787 N ILE C 787 11675 9028 8856 1515 -440 -123 N ATOM 3788 CA ILE C 787 49.172 -16.429 2.818 1.00 87.64 C ANISOU 3788 CA ILE C 787 12967 10310 10024 1682 -486 -131 C ATOM 3789 C ILE C 787 50.441 -15.591 2.761 1.00 93.22 C ANISOU 3789 C ILE C 787 13579 11143 10697 1770 -435 -72 C ATOM 3790 O ILE C 787 50.793 -15.045 1.716 1.00 96.82 O ANISOU 3790 O ILE C 787 13961 11686 11140 1852 -420 -62 O ATOM 3791 CB ILE C 787 48.601 -16.586 1.409 1.00 89.07 C ANISOU 3791 CB ILE C 787 13171 10482 10192 1756 -535 -181 C ATOM 3792 CG1 ILE C 787 49.643 -17.237 0.506 1.00 89.91 C ANISOU 3792 CG1 ILE C 787 13316 10637 10209 1941 -587 -189 C ATOM 3793 CG2 ILE C 787 48.169 -15.237 0.861 1.00 87.90 C ANISOU 3793 CG2 ILE C 787 12903 10402 10093 1723 -477 -173 C ATOM 3794 CD1 ILE C 787 50.351 -18.400 1.158 1.00 88.98 C ANISOU 3794 CD1 ILE C 787 13307 10470 10031 1988 -637 -190 C ATOM 3795 N ASN C 788 51.119 -15.487 3.899 1.00110.02 N ANISOU 3795 N ASN C 788 15735 13257 12812 1682 -384 3 N ATOM 3796 CA ASN C 788 52.328 -14.684 4.001 1.00109.77 C ANISOU 3796 CA ASN C 788 15595 13355 12759 1758 -336 55 C ATOM 3797 C ASN C 788 53.607 -15.468 3.760 1.00108.82 C ANISOU 3797 C ASN C 788 15502 13305 12538 1912 -361 81 C ATOM 3798 O ASN C 788 54.474 -15.027 3.009 1.00108.33 O ANISOU 3798 O ASN C 788 15419 13317 12424 2040 -385 80 O ATOM 3799 CB ASN C 788 52.384 -13.970 5.349 1.00109.12 C ANISOU 3799 CB ASN C 788 15418 13308 12735 1649 -261 107 C ATOM 3800 CG ASN C 788 51.292 -12.938 5.500 1.00107.16 C ANISOU 3800 CG ASN C 788 15122 13017 12576 1516 -233 86 C ATOM 3801 OD1 ASN C 788 50.633 -12.576 4.529 1.00105.41 O ANISOU 3801 OD1 ASN C 788 14877 12802 12374 1528 -244 58 O ATOM 3802 ND2 ASN C 788 51.094 -12.456 6.720 1.00106.34 N ANISOU 3802 ND2 ASN C 788 15001 12878 12525 1393 -198 100 N TER 3803 ASN C 788 ATOM 3804 N GLY D 750 6.763 12.380 -54.313 1.00 69.49 N ANISOU 3804 N GLY D 750 8669 8715 9018 -386 188 -242 N ATOM 3805 CA GLY D 750 7.628 13.057 -53.362 1.00 71.11 C ANISOU 3805 CA GLY D 750 8928 8926 9164 -457 203 -211 C ATOM 3806 C GLY D 750 8.637 12.117 -52.731 1.00 70.65 C ANISOU 3806 C GLY D 750 8877 8875 9091 -508 152 -164 C ATOM 3807 O GLY D 750 8.753 10.962 -53.146 1.00 68.77 O ANISOU 3807 O GLY D 750 8601 8640 8887 -480 104 -155 O ATOM 3808 N PRO D 751 9.370 12.605 -51.717 1.00 68.27 N ANISOU 3808 N PRO D 751 8627 8575 8738 -583 161 -133 N ATOM 3809 CA PRO D 751 10.397 11.799 -51.047 1.00 63.43 C ANISOU 3809 CA PRO D 751 8026 7969 8107 -637 114 -86 C ATOM 3810 C PRO D 751 9.771 10.680 -50.219 1.00 53.54 C ANISOU 3810 C PRO D 751 6771 6702 6871 -679 108 -88 C ATOM 3811 O PRO D 751 10.304 9.569 -50.155 1.00 47.41 O ANISOU 3811 O PRO D 751 5974 5933 6106 -687 59 -62 O ATOM 3812 CB PRO D 751 11.092 12.808 -50.131 1.00 65.37 C ANISOU 3812 CB PRO D 751 8333 8213 8292 -707 137 -60 C ATOM 3813 CG PRO D 751 10.078 13.870 -49.883 1.00 66.14 C ANISOU 3813 CG PRO D 751 8460 8296 8376 -713 207 -98 C ATOM 3814 CD PRO D 751 9.189 13.927 -51.090 1.00 67.02 C ANISOU 3814 CD PRO D 751 8522 8409 8534 -624 220 -141 C ATOM 3815 N LYS D 752 8.638 10.980 -49.597 1.00 47.88 N ANISOU 3815 N LYS D 752 6074 5962 6156 -705 161 -119 N ATOM 3816 CA LYS D 752 7.967 10.025 -48.731 1.00 44.24 C ANISOU 3816 CA LYS D 752 5616 5482 5712 -747 165 -124 C ATOM 3817 C LYS D 752 7.308 8.902 -49.537 1.00 37.40 C ANISOU 3817 C LYS D 752 4687 4618 4905 -686 136 -145 C ATOM 3818 O LYS D 752 7.326 7.736 -49.126 1.00 28.31 O ANISOU 3818 O LYS D 752 3523 3465 3769 -708 106 -134 O ATOM 3819 CB LYS D 752 6.945 10.749 -47.859 1.00 48.98 C ANISOU 3819 CB LYS D 752 6259 6053 6298 -789 234 -147 C ATOM 3820 CG LYS D 752 6.348 9.898 -46.763 1.00 59.45 C ANISOU 3820 CG LYS D 752 7601 7354 7633 -843 245 -148 C ATOM 3821 CD LYS D 752 6.057 10.736 -45.528 1.00 67.92 C ANISOU 3821 CD LYS D 752 8747 8398 8663 -914 303 -144 C ATOM 3822 CE LYS D 752 7.286 10.849 -44.641 1.00 71.85 C ANISOU 3822 CE LYS D 752 9297 8898 9104 -986 280 -101 C ATOM 3823 NZ LYS D 752 7.832 9.507 -44.279 1.00 72.94 N ANISOU 3823 NZ LYS D 752 9418 9043 9254 -1010 225 -79 N ATOM 3824 N LEU D 753 6.749 9.256 -50.693 1.00 29.42 N ANISOU 3824 N LEU D 753 3639 3611 3928 -609 144 -176 N ATOM 3825 CA LEU D 753 6.061 8.285 -51.541 1.00 32.14 C ANISOU 3825 CA LEU D 753 3927 3955 4330 -547 116 -197 C ATOM 3826 C LEU D 753 6.997 7.195 -52.045 1.00 27.22 C ANISOU 3826 C LEU D 753 3275 3351 3717 -524 47 -166 C ATOM 3827 O LEU D 753 6.669 6.009 -52.006 1.00 25.69 O ANISOU 3827 O LEU D 753 3054 3154 3553 -521 20 -167 O ATOM 3828 CB LEU D 753 5.380 8.979 -52.722 1.00 33.29 C ANISOU 3828 CB LEU D 753 4043 4099 4506 -467 136 -234 C ATOM 3829 CG LEU D 753 4.814 8.052 -53.805 1.00 36.03 C ANISOU 3829 CG LEU D 753 4333 4446 4912 -393 99 -254 C ATOM 3830 CD1 LEU D 753 3.476 8.557 -54.323 1.00 41.45 C ANISOU 3830 CD1 LEU D 753 4998 5115 5636 -348 139 -300 C ATOM 3831 CD2 LEU D 753 5.808 7.870 -54.947 1.00 33.07 C ANISOU 3831 CD2 LEU D 753 3935 4089 4540 -331 46 -235 C ATOM 3832 N LEU D 754 8.162 7.603 -52.530 1.00 30.09 N ANISOU 3832 N LEU D 754 3645 3733 4056 -508 21 -137 N ATOM 3833 CA LEU D 754 9.120 6.656 -53.077 1.00 31.27 C ANISOU 3833 CA LEU D 754 3769 3899 4213 -482 -41 -102 C ATOM 3834 C LEU D 754 9.717 5.794 -51.975 1.00 26.46 C ANISOU 3834 C LEU D 754 3179 3295 3580 -556 -64 -66 C ATOM 3835 O LEU D 754 9.934 4.598 -52.162 1.00 23.89 O ANISOU 3835 O LEU D 754 2828 2977 3273 -545 -107 -50 O ATOM 3836 CB LEU D 754 10.215 7.393 -53.847 1.00 37.28 C ANISOU 3836 CB LEU D 754 4534 4676 4956 -445 -58 -78 C ATOM 3837 CG LEU D 754 9.710 7.997 -55.159 1.00 45.27 C ANISOU 3837 CG LEU D 754 5519 5684 5998 -355 -47 -113 C ATOM 3838 CD1 LEU D 754 10.714 8.980 -55.735 1.00 45.87 C ANISOU 3838 CD1 LEU D 754 5608 5771 6050 -327 -49 -94 C ATOM 3839 CD2 LEU D 754 9.384 6.894 -56.163 1.00 42.37 C ANISOU 3839 CD2 LEU D 754 5106 5314 5680 -285 -89 -120 C ATOM 3840 N MET D 755 9.972 6.411 -50.825 1.00 24.53 N ANISOU 3840 N MET D 755 2983 3044 3293 -633 -35 -55 N ATOM 3841 CA MET D 755 10.468 5.699 -49.657 1.00 30.02 C ANISOU 3841 CA MET D 755 3705 3739 3963 -710 -51 -24 C ATOM 3842 C MET D 755 9.492 4.599 -49.226 1.00 31.19 C ANISOU 3842 C MET D 755 3834 3874 4142 -721 -48 -47 C ATOM 3843 O MET D 755 9.894 3.465 -48.962 1.00 34.53 O ANISOU 3843 O MET D 755 4246 4306 4567 -739 -85 -25 O ATOM 3844 CB MET D 755 10.725 6.687 -48.507 1.00 39.77 C ANISOU 3844 CB MET D 755 5000 4962 5147 -787 -14 -14 C ATOM 3845 CG MET D 755 10.784 6.053 -47.125 1.00 46.11 C ANISOU 3845 CG MET D 755 5838 5752 5928 -870 -12 1 C ATOM 3846 SD MET D 755 11.022 7.258 -45.799 0.50 48.57 S ANISOU 3846 SD MET D 755 6231 6043 6180 -959 32 13 S ATOM 3847 CE MET D 755 10.434 6.328 -44.383 1.00 47.83 C ANISOU 3847 CE MET D 755 6168 5923 6084 -1031 47 8 C ATOM 3848 N ILE D 756 8.208 4.935 -49.158 1.00 26.01 N ANISOU 3848 N ILE D 756 3176 3197 3510 -709 -2 -90 N ATOM 3849 CA ILE D 756 7.196 3.958 -48.776 1.00 22.86 C ANISOU 3849 CA ILE D 756 2759 2782 3146 -716 5 -114 C ATOM 3850 C ILE D 756 7.219 2.768 -49.728 1.00 24.09 C ANISOU 3850 C ILE D 756 2859 2952 3340 -657 -47 -112 C ATOM 3851 O ILE D 756 7.289 1.617 -49.301 1.00 22.29 O ANISOU 3851 O ILE D 756 2623 2728 3119 -680 -72 -101 O ATOM 3852 CB ILE D 756 5.783 4.582 -48.763 1.00 24.28 C ANISOU 3852 CB ILE D 756 2937 2935 3353 -701 62 -159 C ATOM 3853 CG1 ILE D 756 5.655 5.582 -47.609 1.00 32.51 C ANISOU 3853 CG1 ILE D 756 4041 3956 4354 -769 118 -159 C ATOM 3854 CG2 ILE D 756 4.728 3.497 -48.626 1.00 24.68 C ANISOU 3854 CG2 ILE D 756 2956 2970 3450 -692 62 -183 C ATOM 3855 CD1 ILE D 756 4.241 6.055 -47.368 1.00 35.32 C ANISOU 3855 CD1 ILE D 756 4401 4282 4736 -765 178 -197 C ATOM 3856 N ILE D 757 7.167 3.059 -51.022 1.00 23.40 N ANISOU 3856 N ILE D 757 2739 2873 3277 -580 -62 -123 N ATOM 3857 CA ILE D 757 7.218 2.022 -52.043 1.00 27.55 C ANISOU 3857 CA ILE D 757 3219 3411 3838 -517 -112 -119 C ATOM 3858 C ILE D 757 8.449 1.137 -51.871 1.00 19.82 C ANISOU 3858 C ILE D 757 2242 2453 2835 -539 -161 -70 C ATOM 3859 O ILE D 757 8.350 -0.090 -51.844 1.00 22.07 O ANISOU 3859 O ILE D 757 2506 2743 3136 -537 -190 -63 O ATOM 3860 CB ILE D 757 7.180 2.634 -53.457 1.00 28.77 C ANISOU 3860 CB ILE D 757 3349 3568 4015 -432 -120 -132 C ATOM 3861 CG1 ILE D 757 5.751 3.083 -53.777 1.00 25.64 C ANISOU 3861 CG1 ILE D 757 2934 3150 3657 -398 -81 -183 C ATOM 3862 CG2 ILE D 757 7.668 1.628 -54.497 1.00 27.41 C ANISOU 3862 CG2 ILE D 757 3142 3408 3864 -371 -179 -111 C ATOM 3863 CD1 ILE D 757 5.614 3.863 -55.073 1.00 22.95 C ANISOU 3863 CD1 ILE D 757 2575 2809 3335 -318 -80 -203 C ATOM 3864 N HIS D 758 9.606 1.769 -51.735 1.00 17.28 N ANISOU 3864 N HIS D 758 1947 2145 2473 -562 -169 -34 N ATOM 3865 CA HIS D 758 10.852 1.050 -51.508 1.00 19.23 C ANISOU 3865 CA HIS D 758 2200 2412 2695 -588 -212 17 C ATOM 3866 C HIS D 758 10.790 0.150 -50.258 1.00 25.90 C ANISOU 3866 C HIS D 758 3061 3255 3525 -662 -213 26 C ATOM 3867 O HIS D 758 11.119 -1.038 -50.324 1.00 23.36 O ANISOU 3867 O HIS D 758 2721 2947 3209 -658 -250 47 O ATOM 3868 CB HIS D 758 12.010 2.049 -51.404 1.00 25.87 C ANISOU 3868 CB HIS D 758 3071 3263 3496 -610 -213 52 C ATOM 3869 CG HIS D 758 13.303 1.435 -50.969 1.00 28.53 C ANISOU 3869 CG HIS D 758 3418 3617 3803 -651 -253 109 C ATOM 3870 ND1 HIS D 758 14.190 0.863 -51.855 1.00 32.93 N ANISOU 3870 ND1 HIS D 758 3952 4193 4369 -603 -299 147 N ATOM 3871 CD2 HIS D 758 13.862 1.308 -49.742 1.00 33.32 C ANISOU 3871 CD2 HIS D 758 4060 4227 4373 -734 -252 135 C ATOM 3872 CE1 HIS D 758 15.238 0.408 -51.192 1.00 38.55 C ANISOU 3872 CE1 HIS D 758 4679 4918 5051 -656 -325 196 C ATOM 3873 NE2 HIS D 758 15.064 0.665 -49.908 1.00 37.86 N ANISOU 3873 NE2 HIS D 758 4627 4822 4935 -736 -299 188 N ATOM 3874 N ASP D 759 10.358 0.718 -49.131 1.00 18.06 N ANISOU 3874 N ASP D 759 2105 2244 2511 -726 -170 9 N ATOM 3875 CA ASP D 759 10.273 -0.029 -47.878 1.00 19.89 C ANISOU 3875 CA ASP D 759 2359 2469 2728 -797 -164 14 C ATOM 3876 C ASP D 759 9.392 -1.267 -47.988 1.00 21.05 C ANISOU 3876 C ASP D 759 2472 2613 2915 -775 -173 -10 C ATOM 3877 O ASP D 759 9.719 -2.328 -47.442 1.00 21.15 O ANISOU 3877 O ASP D 759 2484 2633 2918 -807 -195 7 O ATOM 3878 CB ASP D 759 9.755 0.856 -46.737 1.00 21.80 C ANISOU 3878 CB ASP D 759 2651 2684 2948 -860 -110 -6 C ATOM 3879 CG ASP D 759 10.778 1.889 -46.274 1.00 33.40 C ANISOU 3879 CG ASP D 759 4167 4157 4368 -906 -106 26 C ATOM 3880 OD1 ASP D 759 11.979 1.734 -46.588 1.00 32.72 O ANISOU 3880 OD1 ASP D 759 4075 4094 4262 -903 -148 69 O ATOM 3881 OD2 ASP D 759 10.372 2.854 -45.583 1.00 33.28 O ANISOU 3881 OD2 ASP D 759 4194 4120 4333 -944 -59 11 O ATOM 3882 N ARG D 760 8.262 -1.132 -48.672 1.00 22.87 N ANISOU 3882 N ARG D 760 2674 2830 3188 -721 -154 -51 N ATOM 3883 CA ARG D 760 7.319 -2.243 -48.770 1.00 18.93 C ANISOU 3883 CA ARG D 760 2140 2322 2729 -700 -160 -76 C ATOM 3884 C ARG D 760 7.887 -3.350 -49.636 1.00 23.24 C ANISOU 3884 C ARG D 760 2651 2894 3286 -654 -217 -52 C ATOM 3885 O ARG D 760 7.728 -4.531 -49.327 1.00 24.09 O ANISOU 3885 O ARG D 760 2745 3005 3402 -667 -234 -50 O ATOM 3886 CB ARG D 760 5.948 -1.768 -49.268 1.00 17.57 C ANISOU 3886 CB ARG D 760 1947 2128 2603 -656 -127 -124 C ATOM 3887 CG ARG D 760 5.242 -0.881 -48.233 1.00 15.75 C ANISOU 3887 CG ARG D 760 1753 1868 2362 -708 -64 -147 C ATOM 3888 CD ARG D 760 3.889 -0.390 -48.715 1.00 20.63 C ANISOU 3888 CD ARG D 760 2349 2463 3026 -665 -28 -191 C ATOM 3889 NE ARG D 760 2.925 -1.478 -48.856 1.00 21.83 N ANISOU 3889 NE ARG D 760 2462 2604 3226 -642 -38 -214 N ATOM 3890 CZ ARG D 760 2.257 -2.023 -47.842 1.00 20.28 C ANISOU 3890 CZ ARG D 760 2277 2387 3041 -687 -11 -226 C ATOM 3891 NH1 ARG D 760 2.446 -1.582 -46.596 1.00 19.58 N ANISOU 3891 NH1 ARG D 760 2240 2283 2917 -758 26 -218 N ATOM 3892 NH2 ARG D 760 1.397 -3.007 -48.073 1.00 21.91 N ANISOU 3892 NH2 ARG D 760 2444 2585 3295 -661 -23 -247 N ATOM 3893 N ARG D 761 8.571 -2.963 -50.709 1.00 23.69 N ANISOU 3893 N ARG D 761 2695 2965 3341 -601 -244 -31 N ATOM 3894 CA ARG D 761 9.295 -3.930 -51.522 1.00 27.52 C ANISOU 3894 CA ARG D 761 3156 3472 3830 -559 -298 2 C ATOM 3895 C ARG D 761 10.383 -4.626 -50.709 1.00 24.80 C ANISOU 3895 C ARG D 761 2831 3147 3445 -618 -320 48 C ATOM 3896 O ARG D 761 10.530 -5.849 -50.776 1.00 25.70 O ANISOU 3896 O ARG D 761 2928 3275 3564 -612 -350 63 O ATOM 3897 CB ARG D 761 9.898 -3.270 -52.767 1.00 25.83 C ANISOU 3897 CB ARG D 761 2932 3264 3619 -492 -318 19 C ATOM 3898 CG ARG D 761 8.980 -3.296 -53.980 1.00 28.53 C ANISOU 3898 CG ARG D 761 3240 3593 4009 -409 -324 -15 C ATOM 3899 CD ARG D 761 9.641 -2.623 -55.160 1.00 33.95 C ANISOU 3899 CD ARG D 761 3921 4282 4696 -344 -341 2 C ATOM 3900 NE ARG D 761 8.894 -2.811 -56.398 1.00 38.05 N ANISOU 3900 NE ARG D 761 4410 4788 5259 -260 -356 -25 N ATOM 3901 CZ ARG D 761 8.811 -1.884 -57.346 1.00 37.53 C ANISOU 3901 CZ ARG D 761 4341 4712 5208 -200 -349 -40 C ATOM 3902 NH1 ARG D 761 9.412 -0.712 -57.167 1.00 32.22 N ANISOU 3902 NH1 ARG D 761 3691 4043 4507 -217 -325 -32 N ATOM 3903 NH2 ARG D 761 8.123 -2.115 -58.459 1.00 35.11 N ANISOU 3903 NH2 ARG D 761 4008 4390 4941 -125 -366 -64 N ATOM 3904 N GLU D 762 11.153 -3.853 -49.949 1.00 24.06 N ANISOU 3904 N GLU D 762 2774 3056 3312 -674 -306 70 N ATOM 3905 CA GLU D 762 12.193 -4.450 -49.118 1.00 27.12 C ANISOU 3905 CA GLU D 762 3183 3460 3662 -734 -327 114 C ATOM 3906 C GLU D 762 11.587 -5.446 -48.129 1.00 23.80 C ANISOU 3906 C GLU D 762 2765 3034 3242 -781 -317 95 C ATOM 3907 O GLU D 762 12.108 -6.548 -47.952 1.00 20.06 O ANISOU 3907 O GLU D 762 2285 2579 2758 -794 -346 122 O ATOM 3908 CB GLU D 762 13.026 -3.382 -48.398 1.00 31.89 C ANISOU 3908 CB GLU D 762 3828 4063 4224 -791 -313 138 C ATOM 3909 CG GLU D 762 13.936 -2.585 -49.335 1.00 36.89 C ANISOU 3909 CG GLU D 762 4458 4707 4851 -748 -333 170 C ATOM 3910 CD GLU D 762 14.848 -3.477 -50.183 1.00 45.30 C ANISOU 3910 CD GLU D 762 5496 5796 5920 -704 -383 216 C ATOM 3911 OE1 GLU D 762 15.712 -4.184 -49.614 1.00 42.96 O ANISOU 3911 OE1 GLU D 762 5209 5516 5598 -747 -407 258 O ATOM 3912 OE2 GLU D 762 14.701 -3.465 -51.425 1.00 47.18 O ANISOU 3912 OE2 GLU D 762 5706 6034 6187 -625 -397 212 O ATOM 3913 N PHE D 763 10.475 -5.078 -47.498 1.00 20.43 N ANISOU 3913 N PHE D 763 2351 2581 2831 -804 -273 50 N ATOM 3914 CA PHE D 763 9.808 -6.024 -46.611 1.00 17.37 C ANISOU 3914 CA PHE D 763 1966 2183 2451 -842 -259 28 C ATOM 3915 C PHE D 763 9.379 -7.291 -47.361 1.00 18.82 C ANISOU 3915 C PHE D 763 2104 2379 2667 -790 -289 21 C ATOM 3916 O PHE D 763 9.614 -8.414 -46.892 1.00 18.57 O ANISOU 3916 O PHE D 763 2069 2360 2625 -815 -305 33 O ATOM 3917 CB PHE D 763 8.613 -5.396 -45.895 1.00 22.21 C ANISOU 3917 CB PHE D 763 2598 2760 3080 -868 -204 -18 C ATOM 3918 CG PHE D 763 7.877 -6.359 -44.998 1.00 25.64 C ANISOU 3918 CG PHE D 763 3034 3180 3527 -902 -187 -41 C ATOM 3919 CD1 PHE D 763 8.468 -6.832 -43.837 1.00 26.79 C ANISOU 3919 CD1 PHE D 763 3214 3327 3637 -971 -187 -23 C ATOM 3920 CD2 PHE D 763 6.600 -6.793 -45.319 1.00 25.55 C ANISOU 3920 CD2 PHE D 763 2990 3152 3566 -865 -171 -82 C ATOM 3921 CE1 PHE D 763 7.796 -7.720 -43.008 1.00 30.31 C ANISOU 3921 CE1 PHE D 763 3664 3758 4096 -1000 -169 -46 C ATOM 3922 CE2 PHE D 763 5.920 -7.683 -44.497 1.00 31.28 C ANISOU 3922 CE2 PHE D 763 3716 3862 4305 -895 -154 -104 C ATOM 3923 CZ PHE D 763 6.519 -8.150 -43.341 1.00 34.08 C ANISOU 3923 CZ PHE D 763 4107 4218 4623 -961 -152 -87 C ATOM 3924 N ALA D 764 8.758 -7.113 -48.523 1.00 19.71 N ANISOU 3924 N ALA D 764 2183 2487 2819 -718 -295 0 N ATOM 3925 CA ALA D 764 8.252 -8.258 -49.285 1.00 23.39 C ANISOU 3925 CA ALA D 764 2609 2961 3318 -665 -324 -9 C ATOM 3926 C ALA D 764 9.389 -9.191 -49.712 1.00 19.74 C ANISOU 3926 C ALA D 764 2139 2530 2832 -652 -373 41 C ATOM 3927 O ALA D 764 9.248 -10.411 -49.661 1.00 19.41 O ANISOU 3927 O ALA D 764 2082 2499 2795 -650 -391 43 O ATOM 3928 CB ALA D 764 7.452 -7.794 -50.493 1.00 23.30 C ANISOU 3928 CB ALA D 764 2567 2936 3350 -589 -325 -37 C ATOM 3929 N LYS D 765 10.519 -8.614 -50.112 1.00 17.67 N ANISOU 3929 N LYS D 765 1889 2282 2544 -644 -391 82 N ATOM 3930 CA LYS D 765 11.676 -9.421 -50.484 1.00 25.75 C ANISOU 3930 CA LYS D 765 2907 3333 3543 -633 -434 136 C ATOM 3931 C LYS D 765 12.100 -10.318 -49.330 1.00 28.32 C ANISOU 3931 C LYS D 765 3250 3674 3837 -702 -436 154 C ATOM 3932 O LYS D 765 12.384 -11.506 -49.520 1.00 23.18 O ANISOU 3932 O LYS D 765 2585 3043 3181 -691 -463 176 O ATOM 3933 CB LYS D 765 12.861 -8.545 -50.882 1.00 22.63 C ANISOU 3933 CB LYS D 765 2527 2947 3124 -625 -448 180 C ATOM 3934 CG LYS D 765 12.817 -8.004 -52.299 1.00 39.83 C ANISOU 3934 CG LYS D 765 4687 5119 5329 -541 -462 179 C ATOM 3935 CD LYS D 765 14.101 -7.234 -52.613 1.00 48.22 C ANISOU 3935 CD LYS D 765 5764 6191 6366 -537 -475 228 C ATOM 3936 CE LYS D 765 13.928 -6.326 -53.819 1.00 55.86 C ANISOU 3936 CE LYS D 765 6722 7145 7360 -462 -474 215 C ATOM 3937 NZ LYS D 765 15.117 -5.453 -54.030 1.00 61.52 N ANISOU 3937 NZ LYS D 765 7454 7867 8053 -461 -481 258 N ATOM 3938 N PHE D 766 12.160 -9.735 -48.136 1.00 26.63 N ANISOU 3938 N PHE D 766 3068 3449 3600 -773 -405 145 N ATOM 3939 CA PHE D 766 12.615 -10.461 -46.952 1.00 24.47 C ANISOU 3939 CA PHE D 766 2817 3186 3294 -844 -405 161 C ATOM 3940 C PHE D 766 11.659 -11.604 -46.587 1.00 24.17 C ANISOU 3940 C PHE D 766 2763 3144 3276 -847 -395 126 C ATOM 3941 O PHE D 766 12.092 -12.721 -46.287 1.00 26.29 O ANISOU 3941 O PHE D 766 3028 3434 3526 -865 -414 148 O ATOM 3942 CB PHE D 766 12.804 -9.486 -45.783 1.00 23.65 C ANISOU 3942 CB PHE D 766 2758 3064 3163 -916 -373 157 C ATOM 3943 CG PHE D 766 12.678 -10.120 -44.430 1.00 22.98 C ANISOU 3943 CG PHE D 766 2699 2973 3058 -986 -355 147 C ATOM 3944 CD1 PHE D 766 11.469 -10.096 -43.752 1.00 24.42 C ANISOU 3944 CD1 PHE D 766 2891 3126 3263 -1006 -314 95 C ATOM 3945 CD2 PHE D 766 13.770 -10.733 -43.829 1.00 22.80 C ANISOU 3945 CD2 PHE D 766 2693 2972 2996 -1033 -379 190 C ATOM 3946 CE1 PHE D 766 11.345 -10.680 -42.493 1.00 26.82 C ANISOU 3946 CE1 PHE D 766 3221 3419 3549 -1068 -296 84 C ATOM 3947 CE2 PHE D 766 13.654 -11.320 -42.571 1.00 22.91 C ANISOU 3947 CE2 PHE D 766 2734 2979 2991 -1097 -362 178 C ATOM 3948 CZ PHE D 766 12.439 -11.288 -41.904 1.00 24.11 C ANISOU 3948 CZ PHE D 766 2897 3099 3166 -1113 -320 124 C ATOM 3949 N GLU D 767 10.360 -11.322 -46.627 1.00 20.65 N ANISOU 3949 N GLU D 767 2306 2671 2868 -829 -365 74 N ATOM 3950 CA GLU D 767 9.345 -12.326 -46.323 1.00 23.30 C ANISOU 3950 CA GLU D 767 2623 2998 3230 -828 -354 38 C ATOM 3951 C GLU D 767 9.466 -13.544 -47.237 1.00 25.18 C ANISOU 3951 C GLU D 767 2828 3262 3479 -776 -395 54 C ATOM 3952 O GLU D 767 9.193 -14.672 -46.829 1.00 24.30 O ANISOU 3952 O GLU D 767 2708 3159 3367 -790 -398 46 O ATOM 3953 CB GLU D 767 7.937 -11.721 -46.436 1.00 26.63 C ANISOU 3953 CB GLU D 767 3035 3386 3699 -805 -318 -16 C ATOM 3954 CG GLU D 767 7.565 -10.798 -45.280 1.00 32.03 C ANISOU 3954 CG GLU D 767 3757 4039 4374 -864 -269 -39 C ATOM 3955 CD GLU D 767 7.466 -11.534 -43.942 1.00 37.99 C ANISOU 3955 CD GLU D 767 4537 4786 5112 -929 -248 -47 C ATOM 3956 OE1 GLU D 767 8.454 -11.518 -43.181 1.00 36.52 O ANISOU 3956 OE1 GLU D 767 4385 4611 4881 -983 -254 -17 O ATOM 3957 OE2 GLU D 767 6.406 -12.134 -43.657 1.00 40.87 O ANISOU 3957 OE2 GLU D 767 4886 5132 5510 -925 -228 -84 O ATOM 3958 N LYS D 768 9.873 -13.310 -48.479 1.00 27.46 N ANISOU 3958 N LYS D 768 3098 3561 3774 -714 -426 79 N ATOM 3959 CA LYS D 768 10.033 -14.394 -49.440 1.00 29.03 C ANISOU 3959 CA LYS D 768 3270 3779 3980 -660 -466 100 C ATOM 3960 C LYS D 768 11.367 -15.112 -49.211 1.00 26.48 C ANISOU 3960 C LYS D 768 2960 3490 3610 -686 -492 157 C ATOM 3961 O LYS D 768 11.422 -16.338 -49.126 1.00 31.86 O ANISOU 3961 O LYS D 768 3634 4190 4283 -688 -508 167 O ATOM 3962 CB LYS D 768 9.954 -13.845 -50.867 1.00 26.13 C ANISOU 3962 CB LYS D 768 2884 3405 3639 -581 -487 104 C ATOM 3963 CG LYS D 768 10.137 -14.892 -51.958 1.00 30.89 C ANISOU 3963 CG LYS D 768 3466 4022 4249 -520 -529 130 C ATOM 3964 CD LYS D 768 8.876 -15.726 -52.136 1.00 40.38 C ANISOU 3964 CD LYS D 768 4643 5213 5488 -495 -529 87 C ATOM 3965 CE LYS D 768 8.948 -16.562 -53.402 1.00 46.22 C ANISOU 3965 CE LYS D 768 5365 5959 6238 -424 -572 110 C ATOM 3966 NZ LYS D 768 7.723 -17.369 -53.626 1.00 43.62 N ANISOU 3966 NZ LYS D 768 5011 5617 5946 -399 -576 70 N ATOM 3967 N GLU D 769 12.442 -14.344 -49.095 1.00 24.30 N ANISOU 3967 N GLU D 769 2706 3222 3305 -707 -497 196 N ATOM 3968 CA GLU D 769 13.771 -14.936 -48.950 1.00 26.41 C ANISOU 3968 CA GLU D 769 2984 3520 3531 -729 -524 257 C ATOM 3969 C GLU D 769 13.911 -15.799 -47.694 1.00 28.55 C ANISOU 3969 C GLU D 769 3270 3804 3773 -799 -513 257 C ATOM 3970 O GLU D 769 14.573 -16.836 -47.729 1.00 33.04 O ANISOU 3970 O GLU D 769 3836 4401 4318 -801 -536 294 O ATOM 3971 CB GLU D 769 14.856 -13.857 -48.992 1.00 30.09 C ANISOU 3971 CB GLU D 769 3469 3988 3975 -743 -529 298 C ATOM 3972 CG GLU D 769 16.261 -14.392 -49.273 1.00 38.32 C ANISOU 3972 CG GLU D 769 4515 5060 4985 -742 -564 370 C ATOM 3973 CD GLU D 769 16.873 -15.112 -48.074 1.00 44.76 C ANISOU 3973 CD GLU D 769 5349 5896 5762 -816 -563 393 C ATOM 3974 OE1 GLU D 769 16.445 -14.842 -46.930 1.00 47.69 O ANISOU 3974 OE1 GLU D 769 5741 6254 6126 -878 -534 358 O ATOM 3975 OE2 GLU D 769 17.780 -15.949 -48.277 1.00 42.94 O ANISOU 3975 OE2 GLU D 769 5115 5692 5507 -812 -589 446 O ATOM 3976 N LYS D 770 13.280 -15.385 -46.595 1.00 24.32 N ANISOU 3976 N LYS D 770 2753 3247 3240 -853 -477 215 N ATOM 3977 CA LYS D 770 13.434 -16.082 -45.317 1.00 26.94 C ANISOU 3977 CA LYS D 770 3106 3586 3543 -922 -463 212 C ATOM 3978 C LYS D 770 12.926 -17.529 -45.378 1.00 33.24 C ANISOU 3978 C LYS D 770 3882 4398 4348 -905 -470 197 C ATOM 3979 O LYS D 770 13.304 -18.366 -44.556 1.00 35.82 O ANISOU 3979 O LYS D 770 4221 4742 4646 -950 -468 208 O ATOM 3980 CB LYS D 770 12.726 -15.326 -44.184 1.00 30.05 C ANISOU 3980 CB LYS D 770 3529 3946 3944 -976 -419 167 C ATOM 3981 CG LYS D 770 11.243 -15.675 -44.051 1.00 36.01 C ANISOU 3981 CG LYS D 770 4267 4676 4739 -960 -390 105 C ATOM 3982 CD LYS D 770 10.527 -14.805 -43.025 1.00 37.96 C ANISOU 3982 CD LYS D 770 4545 4884 4995 -1007 -343 65 C ATOM 3983 CE LYS D 770 9.017 -15.030 -43.092 1.00 40.80 C ANISOU 3983 CE LYS D 770 4882 5216 5404 -979 -315 8 C ATOM 3984 NZ LYS D 770 8.266 -14.158 -42.142 1.00 41.52 N ANISOU 3984 NZ LYS D 770 5005 5265 5507 -1020 -265 -28 N ATOM 3985 N MET D 771 12.066 -17.821 -46.349 1.00 33.47 N ANISOU 3985 N MET D 771 3880 4422 4417 -841 -477 173 N ATOM 3986 CA MET D 771 11.543 -19.174 -46.508 1.00 33.30 C ANISOU 3986 CA MET D 771 3836 4413 4402 -820 -486 160 C ATOM 3987 C MET D 771 12.607 -20.110 -47.083 1.00 33.19 C ANISOU 3987 C MET D 771 3818 4438 4355 -800 -524 219 C ATOM 3988 O MET D 771 12.434 -21.329 -47.082 1.00 33.30 O ANISOU 3988 O MET D 771 3820 4469 4362 -793 -532 218 O ATOM 3989 CB MET D 771 10.287 -19.176 -47.389 1.00 33.45 C ANISOU 3989 CB MET D 771 3824 4410 4474 -758 -486 118 C ATOM 3990 CG MET D 771 9.162 -18.269 -46.886 1.00 34.95 C ANISOU 3990 CG MET D 771 4017 4561 4701 -773 -446 62 C ATOM 3991 SD MET D 771 8.732 -18.510 -45.138 1.00 49.95 S ANISOU 3991 SD MET D 771 5944 6445 6590 -856 -400 26 S ATOM 3992 CE MET D 771 8.350 -20.261 -45.116 1.00 35.89 C ANISOU 3992 CE MET D 771 4140 4685 4810 -845 -413 17 C ATOM 3993 N ASN D 772 13.706 -19.531 -47.564 1.00 31.08 N ANISOU 3993 N ASN D 772 3559 4181 4068 -790 -545 271 N ATOM 3994 CA ASN D 772 14.830 -20.303 -48.093 1.00 34.82 C ANISOU 3994 CA ASN D 772 4032 4689 4509 -772 -578 336 C ATOM 3995 C ASN D 772 15.775 -20.811 -47.006 1.00 36.09 C ANISOU 3995 C ASN D 772 4214 4875 4622 -841 -575 368 C ATOM 3996 O ASN D 772 16.700 -21.575 -47.281 1.00 34.48 O ANISOU 3996 O ASN D 772 4010 4701 4388 -834 -598 423 O ATOM 3997 CB ASN D 772 15.628 -19.469 -49.101 1.00 39.09 C ANISOU 3997 CB ASN D 772 4573 5228 5052 -728 -601 382 C ATOM 3998 CG ASN D 772 14.844 -19.171 -50.365 1.00 39.07 C ANISOU 3998 CG ASN D 772 4549 5203 5092 -648 -611 359 C ATOM 3999 OD1 ASN D 772 13.777 -19.737 -50.588 1.00 35.89 O ANISOU 3999 OD1 ASN D 772 4129 4791 4715 -623 -608 317 O ATOM 4000 ND2 ASN D 772 15.373 -18.279 -51.200 1.00 38.10 N ANISOU 4000 ND2 ASN D 772 4427 5071 4977 -608 -625 387 N ATOM 4001 N ALA D 773 15.543 -20.383 -45.771 1.00 34.47 N ANISOU 4001 N ALA D 773 4031 4656 4411 -907 -546 336 N ATOM 4002 CA ALA D 773 16.435 -20.728 -44.674 1.00 36.34 C ANISOU 4002 CA ALA D 773 4293 4912 4604 -977 -542 364 C ATOM 4003 C ALA D 773 16.484 -22.241 -44.432 1.00 38.20 C ANISOU 4003 C ALA D 773 4521 5177 4816 -983 -547 371 C ATOM 4004 O ALA D 773 15.471 -22.927 -44.548 1.00 39.33 O ANISOU 4004 O ALA D 773 4647 5315 4981 -960 -536 327 O ATOM 4005 CB ALA D 773 16.024 -19.994 -43.415 1.00 32.36 C ANISOU 4005 CB ALA D 773 3816 4378 4099 -1042 -508 322 C ATOM 4006 N LYS D 774 17.671 -22.747 -44.102 1.00 37.46 N ANISOU 4006 N LYS D 774 4439 5114 4679 -1015 -562 426 N ATOM 4007 CA LYS D 774 17.861 -24.164 -43.789 1.00 42.34 C ANISOU 4007 CA LYS D 774 5055 5765 5268 -1027 -564 438 C ATOM 4008 C LYS D 774 17.947 -24.366 -42.281 1.00 39.64 C ANISOU 4008 C LYS D 774 4740 5422 4900 -1106 -539 415 C ATOM 4009 O LYS D 774 18.702 -23.670 -41.598 1.00 44.23 O ANISOU 4009 O LYS D 774 5346 5997 5461 -1158 -539 438 O ATOM 4010 CB LYS D 774 19.144 -24.694 -44.435 1.00 49.65 C ANISOU 4010 CB LYS D 774 5977 6728 6161 -1008 -595 519 C ATOM 4011 CG LYS D 774 19.303 -24.360 -45.911 1.00 63.44 C ANISOU 4011 CG LYS D 774 7705 8470 7929 -931 -621 553 C ATOM 4012 CD LYS D 774 20.613 -24.916 -46.461 1.00 69.83 C ANISOU 4012 CD LYS D 774 8515 9313 8705 -915 -648 638 C ATOM 4013 CE LYS D 774 20.882 -24.442 -47.888 1.00 71.43 C ANISOU 4013 CE LYS D 774 8706 9505 8930 -839 -673 677 C ATOM 4014 NZ LYS D 774 19.888 -24.969 -48.867 1.00 69.48 N ANISOU 4014 NZ LYS D 774 8441 9248 8709 -770 -678 646 N ATOM 4015 N TRP D 775 17.184 -25.320 -41.760 1.00 42.01 N ANISOU 4015 N TRP D 775 5039 5725 5198 -1113 -517 372 N ATOM 4016 CA TRP D 775 17.215 -25.615 -40.330 1.00 48.29 C ANISOU 4016 CA TRP D 775 5873 6517 5960 -1170 -487 350 C ATOM 4017 C TRP D 775 18.524 -26.303 -39.923 1.00 59.54 C ANISOU 4017 C TRP D 775 7320 7980 7323 -1194 -499 412 C ATOM 4018 O TRP D 775 18.907 -27.323 -40.500 1.00 60.93 O ANISOU 4018 O TRP D 775 7482 8191 7477 -1162 -512 447 O ATOM 4019 CB TRP D 775 16.010 -26.465 -39.930 1.00 39.66 C ANISOU 4019 CB TRP D 775 4774 5414 4881 -1159 -456 287 C ATOM 4020 CG TRP D 775 14.687 -25.792 -40.175 1.00 38.74 C ANISOU 4020 CG TRP D 775 4638 5256 4826 -1141 -441 225 C ATOM 4021 CD1 TRP D 775 13.836 -26.018 -41.215 1.00 41.90 C ANISOU 4021 CD1 TRP D 775 4998 5653 5270 -1085 -452 203 C ATOM 4022 CD2 TRP D 775 14.063 -24.791 -39.357 1.00 39.11 C ANISOU 4022 CD2 TRP D 775 4705 5256 4897 -1180 -411 180 C ATOM 4023 NE1 TRP D 775 12.724 -25.219 -41.101 1.00 43.54 N ANISOU 4023 NE1 TRP D 775 5201 5816 5525 -1081 -429 149 N ATOM 4024 CE2 TRP D 775 12.836 -24.458 -39.968 1.00 40.68 C ANISOU 4024 CE2 TRP D 775 4875 5428 5155 -1141 -403 134 C ATOM 4025 CE3 TRP D 775 14.424 -24.143 -38.170 1.00 33.37 C ANISOU 4025 CE3 TRP D 775 4024 4509 4147 -1240 -390 177 C ATOM 4026 CZ2 TRP D 775 11.967 -23.506 -39.435 1.00 40.67 C ANISOU 4026 CZ2 TRP D 775 4888 5379 5187 -1158 -370 87 C ATOM 4027 CZ3 TRP D 775 13.560 -23.200 -37.640 1.00 37.17 C ANISOU 4027 CZ3 TRP D 775 4520 4941 4663 -1263 -360 129 C ATOM 4028 CH2 TRP D 775 12.343 -22.891 -38.272 1.00 38.80 C ANISOU 4028 CH2 TRP D 775 4695 5121 4928 -1223 -349 85 C ATOM 4029 N ASP D 776 19.198 -25.738 -38.923 1.00 65.38 N ANISOU 4029 N ASP D 776 8096 8712 8033 -1252 -494 426 N ATOM 4030 CA ASP D 776 20.532 -26.187 -38.516 1.00 71.03 C ANISOU 4030 CA ASP D 776 8834 9462 8693 -1280 -510 489 C ATOM 4031 C ASP D 776 20.493 -27.374 -37.556 1.00 68.11 C ANISOU 4031 C ASP D 776 8488 9113 8279 -1301 -487 472 C ATOM 4032 O ASP D 776 21.518 -27.787 -37.012 1.00 63.27 O ANISOU 4032 O ASP D 776 7898 8527 7616 -1330 -496 515 O ATOM 4033 CB ASP D 776 21.305 -25.030 -37.876 1.00 76.30 C ANISOU 4033 CB ASP D 776 9531 10111 9348 -1332 -520 514 C ATOM 4034 CG ASP D 776 22.723 -25.415 -37.486 1.00 80.80 C ANISOU 4034 CG ASP D 776 10121 10715 9863 -1361 -542 583 C ATOM 4035 OD1 ASP D 776 23.388 -26.127 -38.269 1.00 81.55 O ANISOU 4035 OD1 ASP D 776 10195 10847 9944 -1328 -563 638 O ATOM 4036 OD2 ASP D 776 23.172 -25.002 -36.395 1.00 81.25 O ANISOU 4036 OD2 ASP D 776 10219 10762 9893 -1416 -539 584 O ATOM 4037 N THR D 777 19.302 -27.916 -37.353 1.00 70.38 N ANISOU 4037 N THR D 777 8768 9386 8587 -1284 -457 407 N ATOM 4038 CA THR D 777 19.109 -29.037 -36.450 1.00 73.86 C ANISOU 4038 CA THR D 777 9230 9842 8991 -1300 -430 380 C ATOM 4039 C THR D 777 17.651 -29.424 -36.528 1.00 76.50 C ANISOU 4039 C THR D 777 9545 10155 9366 -1270 -401 309 C ATOM 4040 O THR D 777 16.801 -28.587 -36.830 1.00 70.80 O ANISOU 4040 O THR D 777 8808 9395 8696 -1259 -396 272 O ATOM 4041 CB THR D 777 19.445 -28.666 -34.987 1.00 73.14 C ANISOU 4041 CB THR D 777 9189 9734 8868 -1364 -413 366 C ATOM 4042 OG1 THR D 777 19.023 -29.722 -34.112 1.00 66.90 O ANISOU 4042 OG1 THR D 777 8417 8952 8051 -1373 -381 325 O ATOM 4043 CG2 THR D 777 18.741 -27.371 -34.586 1.00 73.41 C ANISOU 4043 CG2 THR D 777 9236 9713 8943 -1388 -398 322 C ATOM 4044 N GLN D 778 17.354 -30.691 -36.269 1.00 83.99 N ANISOU 4044 N GLN D 778 10494 11126 10291 -1257 -382 291 N ATOM 4045 CA GLN D 778 15.963 -31.106 -36.236 1.00 89.54 C ANISOU 4045 CA GLN D 778 11181 11808 11033 -1232 -353 222 C ATOM 4046 C GLN D 778 15.360 -30.727 -34.887 1.00 88.50 C ANISOU 4046 C GLN D 778 11082 11635 10908 -1276 -315 164 C ATOM 4047 O GLN D 778 14.164 -30.449 -34.800 1.00 89.96 O ANISOU 4047 O GLN D 778 11256 11782 11143 -1266 -292 106 O ATOM 4048 CB GLN D 778 15.811 -32.600 -36.535 1.00 93.75 C ANISOU 4048 CB GLN D 778 11701 12379 11542 -1198 -346 223 C ATOM 4049 CG GLN D 778 14.435 -32.977 -37.079 1.00 95.53 C ANISOU 4049 CG GLN D 778 11893 12586 11819 -1154 -334 169 C ATOM 4050 CD GLN D 778 14.465 -34.216 -37.959 1.00 93.83 C ANISOU 4050 CD GLN D 778 11656 12410 11584 -1107 -345 193 C ATOM 4051 OE1 GLN D 778 13.796 -35.210 -37.675 1.00 92.55 O ANISOU 4051 OE1 GLN D 778 11491 12255 11417 -1094 -320 156 O ATOM 4052 NE2 GLN D 778 15.246 -34.162 -39.031 1.00 91.63 N ANISOU 4052 NE2 GLN D 778 11364 12157 11296 -1080 -381 257 N ATOM 4053 N GLU D 779 16.197 -30.696 -33.847 1.00 81.43 N ANISOU 4053 N GLU D 779 10229 10746 9964 -1325 -309 181 N ATOM 4054 CA GLU D 779 15.773 -30.201 -32.534 1.00 76.97 C ANISOU 4054 CA GLU D 779 9705 10138 9401 -1370 -275 133 C ATOM 4055 C GLU D 779 16.894 -29.915 -31.529 1.00 65.98 C ANISOU 4055 C GLU D 779 8363 8751 7955 -1426 -282 165 C ATOM 4056 O GLU D 779 17.910 -30.610 -31.477 1.00 65.77 O ANISOU 4056 O GLU D 779 8344 8769 7876 -1432 -299 211 O ATOM 4057 CB GLU D 779 14.718 -31.116 -31.900 1.00 85.25 C ANISOU 4057 CB GLU D 779 10756 11174 10460 -1360 -232 69 C ATOM 4058 CG GLU D 779 13.291 -30.695 -32.214 1.00 94.02 C ANISOU 4058 CG GLU D 779 11841 12240 11642 -1334 -211 13 C ATOM 4059 CD GLU D 779 12.292 -31.191 -31.194 1.00101.64 C ANISOU 4059 CD GLU D 779 12823 13173 12621 -1343 -161 -54 C ATOM 4060 OE1 GLU D 779 12.723 -31.734 -30.153 1.00103.16 O ANISOU 4060 OE1 GLU D 779 13055 13374 12768 -1372 -142 -60 O ATOM 4061 OE2 GLU D 779 11.075 -31.029 -31.432 1.00104.54 O ANISOU 4061 OE2 GLU D 779 13167 13506 13048 -1319 -142 -100 O ATOM 4062 N ASN D 780 16.674 -28.872 -30.733 1.00 54.34 N ANISOU 4062 N ASN D 780 6923 7228 6494 -1466 -267 141 N ATOM 4063 CA ASN D 780 17.572 -28.476 -29.658 1.00 45.16 C ANISOU 4063 CA ASN D 780 5814 6058 5285 -1522 -271 162 C ATOM 4064 C ASN D 780 17.559 -29.498 -28.522 1.00 42.71 C ANISOU 4064 C ASN D 780 5538 5755 4934 -1541 -241 133 C ATOM 4065 O ASN D 780 16.500 -29.818 -27.978 1.00 37.23 O ANISOU 4065 O ASN D 780 4851 5031 4263 -1535 -199 71 O ATOM 4066 CB ASN D 780 17.162 -27.094 -29.143 1.00 35.40 C ANISOU 4066 CB ASN D 780 4610 4762 4078 -1555 -259 139 C ATOM 4067 CG ASN D 780 17.946 -26.658 -27.922 1.00 32.82 C ANISOU 4067 CG ASN D 780 4347 4419 3706 -1616 -260 153 C ATOM 4068 OD1 ASN D 780 18.938 -27.280 -27.544 1.00 32.46 O ANISOU 4068 OD1 ASN D 780 4317 4409 3607 -1635 -278 188 O ATOM 4069 ND2 ASN D 780 17.506 -25.567 -27.301 1.00 33.44 N ANISOU 4069 ND2 ASN D 780 4463 4441 3803 -1647 -242 127 N ATOM 4070 N PRO D 781 18.744 -30.019 -28.169 1.00 43.81 N ANISOU 4070 N PRO D 781 5698 5935 5014 -1564 -262 179 N ATOM 4071 CA PRO D 781 18.916 -31.035 -27.123 1.00 45.14 C ANISOU 4071 CA PRO D 781 5899 6118 5135 -1582 -237 158 C ATOM 4072 C PRO D 781 18.369 -30.599 -25.770 1.00 42.01 C ANISOU 4072 C PRO D 781 5557 5664 4742 -1622 -200 105 C ATOM 4073 O PRO D 781 17.846 -31.434 -25.040 1.00 42.03 O ANISOU 4073 O PRO D 781 5575 5661 4733 -1619 -161 59 O ATOM 4074 CB PRO D 781 20.436 -31.190 -27.030 1.00 47.13 C ANISOU 4074 CB PRO D 781 6166 6412 5327 -1609 -277 228 C ATOM 4075 CG PRO D 781 20.947 -30.744 -28.344 1.00 47.54 C ANISOU 4075 CG PRO D 781 6175 6489 5397 -1583 -319 286 C ATOM 4076 CD PRO D 781 20.020 -29.668 -28.814 1.00 43.72 C ANISOU 4076 CD PRO D 781 5676 5959 4978 -1571 -312 256 C ATOM 4077 N ILE D 782 18.491 -29.316 -25.437 1.00 41.47 N ANISOU 4077 N ILE D 782 5518 5552 4685 -1658 -209 111 N ATOM 4078 CA ILE D 782 18.067 -28.836 -24.123 1.00 36.38 C ANISOU 4078 CA ILE D 782 4935 4850 4039 -1698 -175 68 C ATOM 4079 C ILE D 782 16.692 -28.165 -24.132 1.00 38.76 C ANISOU 4079 C ILE D 782 5233 5090 4402 -1684 -138 13 C ATOM 4080 O ILE D 782 16.310 -27.510 -23.162 1.00 40.62 O ANISOU 4080 O ILE D 782 5522 5269 4642 -1716 -111 -17 O ATOM 4081 CB ILE D 782 19.100 -27.882 -23.502 1.00 34.89 C ANISOU 4081 CB ILE D 782 4798 4645 3815 -1754 -205 110 C ATOM 4082 CG1 ILE D 782 19.160 -26.565 -24.280 1.00 30.51 C ANISOU 4082 CG1 ILE D 782 4227 4071 3294 -1755 -232 138 C ATOM 4083 CG2 ILE D 782 20.473 -28.535 -23.467 1.00 38.57 C ANISOU 4083 CG2 ILE D 782 5265 5168 4221 -1770 -243 167 C ATOM 4084 CD1 ILE D 782 20.074 -25.536 -23.638 1.00 24.25 C ANISOU 4084 CD1 ILE D 782 3487 3256 2471 -1812 -259 175 C ATOM 4085 N TYR D 783 15.950 -28.333 -25.218 1.00 43.46 N ANISOU 4085 N TYR D 783 5770 5697 5045 -1634 -137 0 N ATOM 4086 CA TYR D 783 14.590 -27.818 -25.278 1.00 43.35 C ANISOU 4086 CA TYR D 783 5747 5630 5094 -1616 -100 -54 C ATOM 4087 C TYR D 783 13.683 -28.597 -24.328 1.00 43.04 C ANISOU 4087 C TYR D 783 5727 5564 5061 -1610 -47 -116 C ATOM 4088 O TYR D 783 13.673 -29.822 -24.340 1.00 40.46 O ANISOU 4088 O TYR D 783 5380 5276 4715 -1587 -40 -124 O ATOM 4089 CB TYR D 783 14.041 -27.894 -26.702 1.00 38.80 C ANISOU 4089 CB TYR D 783 5100 5074 4567 -1563 -116 -50 C ATOM 4090 CG TYR D 783 12.579 -27.530 -26.809 1.00 38.61 C ANISOU 4090 CG TYR D 783 5059 4999 4611 -1539 -79 -107 C ATOM 4091 CD1 TYR D 783 12.178 -26.209 -26.924 1.00 32.24 C ANISOU 4091 CD1 TYR D 783 4266 4144 3841 -1553 -73 -113 C ATOM 4092 CD2 TYR D 783 11.599 -28.511 -26.793 1.00 40.08 C ANISOU 4092 CD2 TYR D 783 5216 5188 4826 -1503 -49 -152 C ATOM 4093 CE1 TYR D 783 10.851 -25.878 -27.019 1.00 36.22 C ANISOU 4093 CE1 TYR D 783 4754 4599 4407 -1531 -37 -162 C ATOM 4094 CE2 TYR D 783 10.269 -28.189 -26.888 1.00 38.67 C ANISOU 4094 CE2 TYR D 783 5020 4961 4713 -1481 -17 -201 C ATOM 4095 CZ TYR D 783 9.898 -26.873 -27.002 1.00 41.06 C ANISOU 4095 CZ TYR D 783 5336 5214 5051 -1496 -10 -205 C ATOM 4096 OH TYR D 783 8.570 -26.552 -27.097 1.00 42.40 O ANISOU 4096 OH TYR D 783 5487 5335 5286 -1474 24 -250 O ATOM 4097 N LYS D 784 12.929 -27.876 -23.506 1.00 39.75 N ANISOU 4097 N LYS D 784 5352 5080 4671 -1631 -8 -156 N ATOM 4098 CA LYS D 784 11.969 -28.491 -22.600 1.00 42.07 C ANISOU 4098 CA LYS D 784 5664 5338 4982 -1621 48 -217 C ATOM 4099 C LYS D 784 10.580 -27.991 -22.932 1.00 41.81 C ANISOU 4099 C LYS D 784 5612 5251 5023 -1598 79 -257 C ATOM 4100 O LYS D 784 10.350 -26.787 -23.022 1.00 39.37 O ANISOU 4100 O LYS D 784 5327 4898 4733 -1618 80 -251 O ATOM 4101 CB LYS D 784 12.266 -28.136 -21.142 1.00 43.52 C ANISOU 4101 CB LYS D 784 5929 5481 5126 -1669 74 -229 C ATOM 4102 CG LYS D 784 13.651 -28.473 -20.652 1.00 47.52 C ANISOU 4102 CG LYS D 784 6467 6029 5559 -1706 37 -182 C ATOM 4103 CD LYS D 784 13.877 -27.871 -19.274 0.50 45.30 C ANISOU 4103 CD LYS D 784 6272 5694 5246 -1757 57 -190 C ATOM 4104 CE LYS D 784 15.340 -27.897 -18.876 0.50 42.11 C ANISOU 4104 CE LYS D 784 5900 5326 4775 -1799 11 -136 C ATOM 4105 NZ LYS D 784 15.580 -27.128 -17.631 0.50 37.91 N ANISOU 4105 NZ LYS D 784 5451 4734 4217 -1851 19 -135 N ATOM 4106 N SER D 785 9.653 -28.922 -23.098 1.00 42.43 N ANISOU 4106 N SER D 785 5647 5332 5143 -1555 105 -297 N ATOM 4107 CA SER D 785 8.261 -28.578 -23.314 1.00 47.76 C ANISOU 4107 CA SER D 785 6301 5953 5892 -1532 137 -337 C ATOM 4108 C SER D 785 7.763 -27.817 -22.089 1.00 47.97 C ANISOU 4108 C SER D 785 6396 5902 5927 -1563 188 -370 C ATOM 4109 O SER D 785 8.241 -28.037 -20.984 1.00 37.95 O ANISOU 4109 O SER D 785 5183 4624 4610 -1593 205 -374 O ATOM 4110 CB SER D 785 7.444 -29.852 -23.514 1.00 50.68 C ANISOU 4110 CB SER D 785 6613 6341 6302 -1482 152 -372 C ATOM 4111 OG SER D 785 6.197 -29.563 -24.106 1.00 58.18 O ANISOU 4111 OG SER D 785 7585 7297 7225 -1483 185 -401 O ATOM 4112 N PRO D 786 6.814 -26.911 -22.285 1.00 52.09 N ANISOU 4112 N PRO D 786 6917 6366 6509 -1555 215 -391 N ATOM 4113 CA PRO D 786 6.303 -26.114 -21.170 1.00 59.99 C ANISOU 4113 CA PRO D 786 7987 7287 7519 -1583 266 -416 C ATOM 4114 C PRO D 786 5.895 -26.989 -19.984 1.00 69.29 C ANISOU 4114 C PRO D 786 9200 8436 8690 -1581 317 -459 C ATOM 4115 O PRO D 786 6.060 -26.577 -18.839 1.00 70.41 O ANISOU 4115 O PRO D 786 9417 8525 8811 -1613 350 -468 O ATOM 4116 CB PRO D 786 5.083 -25.438 -21.792 1.00 55.65 C ANISOU 4116 CB PRO D 786 7408 6692 7046 -1559 287 -434 C ATOM 4117 CG PRO D 786 5.550 -25.185 -23.169 1.00 54.27 C ANISOU 4117 CG PRO D 786 7166 6572 6881 -1538 232 -401 C ATOM 4118 CD PRO D 786 6.137 -26.527 -23.532 1.00 50.97 C ANISOU 4118 CD PRO D 786 6711 6229 6425 -1521 197 -388 C ATOM 4119 N ILE D 787 5.379 -28.183 -20.256 1.00 74.88 N ANISOU 4119 N ILE D 787 9859 9177 9416 -1545 326 -485 N ATOM 4120 CA ILE D 787 4.979 -29.093 -19.188 1.00 84.86 C ANISOU 4120 CA ILE D 787 11154 10418 10673 -1541 376 -527 C ATOM 4121 C ILE D 787 6.159 -29.764 -18.495 1.00 93.15 C ANISOU 4121 C ILE D 787 12237 11514 11641 -1566 359 -509 C ATOM 4122 O ILE D 787 5.987 -30.432 -17.479 1.00 97.14 O ANISOU 4122 O ILE D 787 12768 12011 12131 -1563 397 -540 O ATOM 4123 CB ILE D 787 4.000 -30.174 -19.676 1.00 82.16 C ANISOU 4123 CB ILE D 787 10747 10086 10385 -1490 398 -566 C ATOM 4124 CG1 ILE D 787 4.682 -31.100 -20.682 1.00 78.40 C ANISOU 4124 CG1 ILE D 787 10209 9698 9880 -1467 351 -546 C ATOM 4125 CG2 ILE D 787 2.747 -29.541 -20.246 1.00 83.08 C ANISOU 4125 CG2 ILE D 787 10827 10155 10584 -1465 414 -583 C ATOM 4126 CD1 ILE D 787 3.744 -32.071 -21.342 1.00 76.97 C ANISOU 4126 CD1 ILE D 787 9974 9531 9738 -1421 372 -585 C ATOM 4127 N ASN D 788 7.354 -29.585 -19.045 1.00 93.94 N ANISOU 4127 N ASN D 788 12339 11662 11693 -1590 303 -458 N ATOM 4128 CA ASN D 788 8.564 -30.123 -18.437 1.00 91.66 C ANISOU 4128 CA ASN D 788 12082 11418 11327 -1617 281 -432 C ATOM 4129 C ASN D 788 9.533 -29.018 -18.021 1.00 92.62 C ANISOU 4129 C ASN D 788 12263 11525 11405 -1669 252 -390 C ATOM 4130 O ASN D 788 10.705 -29.280 -17.768 1.00 94.97 O ANISOU 4130 O ASN D 788 12584 11862 11639 -1696 221 -357 O ATOM 4131 CB ASN D 788 9.269 -31.080 -19.403 1.00 89.02 C ANISOU 4131 CB ASN D 788 11684 11171 10968 -1593 236 -404 C ATOM 4132 CG ASN D 788 8.523 -32.388 -19.586 1.00 85.85 C ANISOU 4132 CG ASN D 788 11242 10793 10583 -1551 265 -443 C ATOM 4133 OD1 ASN D 788 7.859 -32.874 -18.672 1.00 85.22 O ANISOU 4133 OD1 ASN D 788 11189 10672 10516 -1547 319 -490 O ATOM 4134 ND2 ASN D 788 8.641 -32.970 -20.770 1.00 80.42 N ANISOU 4134 ND2 ASN D 788 10491 10171 9892 -1519 232 -423 N ATOM 4135 N ASN D 789 9.044 -27.784 -17.954 1.00 90.18 N ANISOU 4135 N ASN D 789 11979 11157 11128 -1682 262 -390 N ATOM 4136 CA ASN D 789 9.905 -26.637 -17.683 1.00 87.38 C ANISOU 4136 CA ASN D 789 11678 10785 10736 -1730 233 -349 C ATOM 4137 C ASN D 789 9.133 -25.322 -17.650 1.00 87.45 C ANISOU 4137 C ASN D 789 11715 10723 10788 -1737 258 -358 C ATOM 4138 O ASN D 789 8.168 -25.175 -16.904 1.00 87.28 O ANISOU 4138 O ASN D 789 11743 10633 10785 -1740 312 -394 O ATOM 4139 CB ASN D 789 11.011 -26.555 -18.740 1.00 84.23 C ANISOU 4139 CB ASN D 789 11235 10458 10310 -1733 165 -292 C ATOM 4140 CG ASN D 789 11.771 -25.241 -18.699 1.00 81.92 C ANISOU 4140 CG ASN D 789 10991 10149 9985 -1780 132 -248 C ATOM 4141 OD1 ASN D 789 11.929 -24.569 -19.722 1.00 78.70 O ANISOU 4141 OD1 ASN D 789 10659 9708 9536 -1822 140 -245 O ATOM 4142 ND2 ASN D 789 12.246 -24.867 -17.517 1.00 78.97 N ANISOU 4142 ND2 ASN D 789 10576 9800 9630 -1773 93 -213 N TER 4143 ASN D 789 HETATM 4144 C1 GOL A 1 28.831 -5.275 -32.419 1.00 31.35 C HETATM 4145 O1 GOL A 1 30.099 -5.294 -31.786 1.00 26.98 O HETATM 4146 C2 GOL A 1 27.829 -4.497 -31.564 1.00 29.16 C HETATM 4147 O2 GOL A 1 27.701 -5.098 -30.298 1.00 21.21 O HETATM 4148 C3 GOL A 1 26.466 -4.458 -32.242 1.00 26.23 C HETATM 4149 O3 GOL A 1 26.554 -3.709 -33.436 1.00 27.52 O HETATM 4150 O HOH A 4 33.149 -9.964 0.642 1.00 33.68 O HETATM 4151 O HOH A 13 20.788 -2.250 -21.041 1.00 23.34 O HETATM 4152 O HOH A 22 23.466 -7.927 -41.692 1.00 25.58 O HETATM 4153 O HOH A 25 22.585 -14.534 -42.866 1.00 20.41 O HETATM 4154 O HOH A 32 31.851 5.424 -21.379 1.00 14.99 O HETATM 4155 O HOH A 34 34.191 4.065 -19.980 1.00 19.83 O HETATM 4156 O HOH A 38 30.300 -7.802 -9.608 1.00 41.00 O HETATM 4157 O HOH A 41 36.252 13.287 -8.055 1.00 28.90 O HETATM 4158 O HOH A 43 10.605 -11.332 -22.221 1.00 41.14 O HETATM 4159 O HOH A 44 20.411 -4.247 -16.699 1.00 33.14 O HETATM 4160 O HOH A 45 29.405 17.200 -24.586 1.00 29.64 O HETATM 4161 O HOH A 46 23.731 -8.587 -38.575 1.00 34.97 O HETATM 4162 O HOH A 48 10.500 -9.716 -37.900 1.00 25.59 O HETATM 4163 O HOH A 49 29.533 18.808 -14.949 1.00 38.48 O HETATM 4164 O HOH A 50 44.989 2.853 -6.225 1.00 22.10 O HETATM 4165 O HOH A 51 31.217 2.293 -1.755 1.00 20.52 O HETATM 4166 O HOH A 53 28.573 18.793 -22.204 1.00 30.82 O HETATM 4167 O HOH A 72 12.561 -8.543 -20.572 1.00 46.56 O HETATM 4168 O HOH A 78 21.911 15.505 -28.778 1.00 32.91 O HETATM 4169 O HOH A 80 8.386 -13.282 -24.089 1.00 47.59 O HETATM 4170 O HOH A 81 20.653 5.797 -24.634 1.00 32.62 O HETATM 4171 O HOH A 87 26.424 -14.582 -21.866 1.00 25.49 O HETATM 4172 O HOH A 91 5.585 -18.248 -37.815 1.00 40.76 O HETATM 4173 O HOH A 92 44.685 10.193 -19.924 1.00 36.34 O HETATM 4174 O HOH A 93 32.886 -12.129 -37.196 1.00 22.66 O HETATM 4175 O HOH A 96 21.283 -7.452 -43.777 1.00 33.50 O HETATM 4176 O HOH A 102 23.153 0.313 -20.156 1.00 16.11 O HETATM 4177 O HOH A 104 19.992 8.188 -25.748 1.00 39.72 O HETATM 4178 O HOH A 105 36.097 15.836 -27.920 1.00 43.50 O HETATM 4179 O HOH A 107 15.936 -3.278 -45.732 1.00 50.46 O HETATM 4180 O HOH A 108 24.850 9.623 -16.364 1.00 46.93 O HETATM 4181 O HOH A 112 6.325 0.441 -45.073 1.00 28.21 O HETATM 4182 O HOH A 117 28.333 15.882 -27.035 1.00 30.00 O HETATM 4183 O HOH A 120 39.820 4.747 -2.190 1.00 18.56 O HETATM 4184 O HOH A 121 16.708 -3.157 -19.774 1.00 26.03 O HETATM 4185 O HOH A 122 33.438 20.760 -14.755 1.00 37.00 O HETATM 4186 O HOH A 123 28.911 -13.949 -25.611 1.00 29.09 O HETATM 4187 O HOH A 128 29.317 -23.653 -32.618 1.00 38.88 O HETATM 4188 O HOH A 130 44.973 5.697 -6.566 1.00 30.69 O HETATM 4189 O HOH A 135 42.257 -7.467 -20.083 1.00 32.73 O HETATM 4190 O HOH A 137 18.262 -21.900 -20.892 1.00 31.24 O HETATM 4191 O HOH A 140 43.346 15.023 -10.332 1.00 31.04 O HETATM 4192 O HOH A 143 39.909 -8.414 -8.966 1.00 33.16 O HETATM 4193 O HOH A 146 42.385 8.404 -7.423 1.00 38.33 O HETATM 4194 O HOH A 151 19.441 -5.805 -42.592 1.00 43.54 O HETATM 4195 O HOH A 156 40.552 13.377 -22.597 1.00 37.16 O HETATM 4196 O HOH A 158 25.422 -15.844 -42.441 1.00 39.86 O HETATM 4197 O HOH A 159 36.137 13.204 -29.690 1.00 41.85 O HETATM 4198 O HOH A 166 37.553 6.124 -0.377 1.00 42.08 O HETATM 4199 O HOH A 169 21.934 4.745 -29.233 1.00 48.35 O HETATM 4200 O HOH A 174 20.346 -9.722 -45.097 1.00 36.80 O HETATM 4201 O HOH A 177 32.687 20.439 -11.960 1.00 39.29 O HETATM 4202 O HOH A 178 9.164 -12.485 -37.287 1.00 25.15 O HETATM 4203 O HOH A 181 31.502 -1.042 -2.855 1.00 29.01 O HETATM 4204 O HOH A 411 25.798 -13.831 -45.648 1.00 39.33 O HETATM 4205 O HOH A 412 42.934 7.472 -9.924 1.00 26.85 O HETATM 4206 O HOH A 413 13.683 3.471 -28.903 1.00 46.39 O HETATM 4207 O HOH A 414 14.636 0.528 -34.708 1.00 31.89 O HETATM 4208 O HOH A 415 18.741 0.974 -20.969 1.00 41.95 O HETATM 4209 O HOH A 416 20.008 2.926 -18.364 1.00 31.04 O HETATM 4210 O HOH A 417 26.345 -21.828 -22.331 1.00 32.49 O HETATM 4211 O HOH A 418 27.772 10.644 -31.511 1.00 34.79 O HETATM 4212 O HOH A 419 31.222 20.319 -16.459 1.00 44.77 O HETATM 4213 O HOH A 420 3.386 -6.742 -36.769 1.00 28.80 O HETATM 4214 O HOH A 421 41.376 -4.327 -0.446 1.00 27.03 O HETATM 4215 O HOH A 422 9.903 -14.457 -21.659 1.00 54.85 O HETATM 4216 O HOH A 423 31.703 18.674 -24.912 1.00 32.55 O HETATM 4217 O HOH A 424 8.656 -15.854 -39.608 1.00 44.55 O HETATM 4218 O HOH A 425 23.539 -2.145 -21.481 1.00 20.53 O HETATM 4219 O HOH A 426 34.210 6.181 -2.070 1.00 30.90 O HETATM 4220 O HOH A 427 14.411 1.855 -31.337 1.00 44.26 O HETATM 4221 O HOH A 428 35.978 18.043 -25.040 1.00 48.58 O HETATM 4222 O HOH A 429 15.013 -17.243 -42.132 1.00 27.55 O HETATM 4223 O HOH A 430 31.228 -18.821 -38.722 1.00 36.19 O HETATM 4224 O HOH A 431 42.296 -10.246 3.173 1.00 34.59 O HETATM 4225 O HOH A 432 8.788 -6.177 -27.073 1.00 45.90 O HETATM 4226 O HOH A 433 18.459 5.310 -22.638 1.00 42.86 O HETATM 4227 O HOH A 434 46.174 -11.308 -12.801 1.00 42.13 O HETATM 4228 O HOH A 435 40.476 -11.039 -9.143 1.00 41.18 O HETATM 4229 O HOH A 436 47.810 -8.758 -7.414 1.00 48.59 O HETATM 4230 O HOH A 437 40.356 5.214 -24.574 1.00 46.76 O HETATM 4231 O HOH A 438 8.102 -2.431 -33.379 1.00 43.47 O HETATM 4232 O HOH A 439 18.532 2.586 -35.049 1.00 39.32 O HETATM 4233 O HOH A 440 7.927 -20.261 -32.097 1.00 56.13 O HETATM 4234 O HOH A 441 41.823 3.944 -22.681 1.00 36.77 O HETATM 4235 O HOH A 442 33.072 -6.897 -0.193 1.00 39.62 O HETATM 4236 O HOH A 443 9.337 -4.724 -23.772 1.00 58.57 O HETATM 4237 O HOH A 444 41.498 3.794 -18.351 1.00 19.54 O HETATM 4238 O HOH A 445 43.875 3.401 -17.617 1.00 29.51 O HETATM 4239 O HOH A 446 35.932 11.082 -1.105 1.00 50.23 O HETATM 4240 O HOH A 447 18.860 -11.147 -18.391 1.00 32.40 O HETATM 4241 O HOH A 448 37.708 -10.425 -19.007 1.00 39.76 O HETATM 4242 O HOH A 449 22.461 -22.707 -39.161 1.00 39.42 O HETATM 4243 O HOH A 462 38.997 -6.896 -26.461 1.00 28.70 O HETATM 4244 O HOH A 463 36.489 -5.330 -27.049 1.00 38.73 O HETATM 4245 O HOH A 469 26.804 1.532 -26.412 1.00 31.03 O HETATM 4246 O HOH A 470 29.015 0.524 -25.875 1.00 18.86 O HETATM 4247 O HOH A 471 47.443 -6.472 -15.087 1.00 47.00 O HETATM 4248 O HOH A 473 31.891 2.736 -29.909 1.00 23.39 O HETATM 4249 O HOH A 474 38.074 4.114 -27.424 1.00 23.75 O HETATM 4250 O HOH A 476 27.507 4.643 -11.229 1.00 23.03 O HETATM 4251 O HOH A 477 28.009 2.660 -9.470 1.00 28.52 O HETATM 4252 O HOH A 478 29.443 0.446 -9.320 1.00 23.22 O HETATM 4253 O HOH A 479 27.262 -1.394 -9.526 1.00 30.79 O HETATM 4254 O HOH A 480 29.649 0.208 -6.559 1.00 29.32 O HETATM 4255 O HOH A 481 29.178 1.715 -30.093 1.00 31.54 O HETATM 4256 O HOH A 482 29.102 14.597 -5.989 1.00 42.28 O HETATM 4257 O HOH A 520 30.625 -27.256 -19.551 1.00 45.04 O HETATM 4258 O HOH A 523 42.808 -7.573 3.462 1.00 48.87 O HETATM 4259 O HOH A 540 30.547 18.558 -12.611 1.00 48.44 O HETATM 4260 O HOH A 544 23.757 3.605 -11.309 1.00 43.37 O HETATM 4261 O HOH A 551 9.931 -4.337 -34.021 1.00 34.11 O HETATM 4262 O HOH A 552 1.872 -4.974 -41.437 1.00 33.10 O HETATM 4263 O HOH A 557 32.288 -7.436 -30.548 1.00 23.35 O HETATM 4264 O HOH A 559 28.375 -7.368 -29.122 1.00 18.96 O HETATM 4265 O HOH A 565 6.647 -12.503 -28.919 1.00 44.86 O HETATM 4266 O HOH A 566 6.459 -9.753 -36.043 1.00 33.66 O HETATM 4267 O HOH A 567 7.153 -8.419 -27.465 1.00 46.78 O HETATM 4268 O HOH A 568 16.665 -0.543 -19.525 1.00 33.17 O HETATM 4269 O HOH A 569 20.822 0.209 -19.127 1.00 49.32 O HETATM 4270 O HOH A 570 28.180 -6.164 -10.043 1.00 33.39 O HETATM 4271 O HOH A 571 21.377 -14.257 -18.834 1.00 47.81 O HETATM 4272 O HOH A 573 27.306 -10.277 -14.612 1.00 41.63 O HETATM 4273 O HOH A 574 29.352 -12.580 -5.687 1.00 47.72 O HETATM 4274 O HOH A 583 23.815 18.733 -8.617 1.00 48.39 O HETATM 4275 O HOH A 585 25.219 13.751 -6.974 1.00 33.72 O HETATM 4276 O HOH A 586 26.046 10.000 -7.000 1.00 37.00 O HETATM 4277 O HOH A 587 44.692 -6.653 -20.993 1.00 38.60 O HETATM 4278 O HOH A 588 47.918 -3.451 9.787 1.00 57.40 O HETATM 4279 O HOH A 589 45.037 0.794 -19.251 1.00 44.65 O HETATM 4280 O HOH A 590 45.442 2.183 -14.963 1.00 46.19 O HETATM 4281 O HOH A 591 43.401 -2.030 -24.501 1.00 33.73 O HETATM 4282 O HOH A 592 40.812 -5.462 -24.963 1.00 34.13 O HETATM 4283 O HOH A 593 41.248 -6.984 -23.063 1.00 38.13 O HETATM 4284 O HOH A 594 40.543 -12.764 -16.951 1.00 46.45 O HETATM 4285 O HOH A 595 32.335 -11.240 -21.713 1.00 31.81 O HETATM 4286 O HOH A 596 34.840 -10.771 -21.150 1.00 30.12 O HETATM 4287 O HOH A 597 34.376 -8.461 -19.547 1.00 24.75 O HETATM 4288 O HOH A 598 32.801 -6.923 -21.016 1.00 23.06 O HETATM 4289 O HOH A 599 31.856 -4.344 -20.207 1.00 17.24 O HETATM 4290 O HOH A 602 38.582 -0.961 -28.148 1.00 40.84 O HETATM 4291 O HOH A 603 30.663 -2.435 -31.924 1.00 25.28 O HETATM 4292 O HOH A 604 31.615 -3.304 -34.260 1.00 29.19 O HETATM 4293 O HOH A 605 27.512 -4.590 -35.990 1.00 20.37 O HETATM 4294 O HOH A 606 26.375 -7.036 -36.221 1.00 20.32 O HETATM 4295 O HOH A 607 42.416 7.833 -22.918 1.00 40.37 O HETATM 4296 O HOH A 608 44.141 15.856 -15.114 1.00 30.22 O HETATM 4297 O HOH A 609 32.076 9.745 -2.994 1.00 43.59 O HETATM 4298 O HOH A 611 44.741 17.655 -12.411 1.00 50.29 O HETATM 4299 O HOH A 612 30.057 22.853 -16.620 1.00 48.60 O HETATM 4300 O HOH A 613 42.940 15.049 -21.732 1.00 48.04 O HETATM 4301 O HOH A 614 24.014 2.586 -31.711 1.00 63.02 O HETATM 4302 O HOH A 615 24.947 17.325 -16.113 1.00 50.35 O HETATM 4303 O HOH A 616 45.940 7.813 -11.306 1.00 44.68 O HETATM 4304 O HOH A 617 23.130 -1.074 -12.298 1.00 40.65 O HETATM 4305 O HOH A 618 5.930 3.625 -40.426 1.00 57.06 O HETATM 4306 O HOH A 619 6.356 -22.745 -32.980 1.00 44.42 O HETATM 4307 O HOH A 620 1.555 -21.084 -27.987 1.00 47.97 O HETATM 4308 O HOH A 621 25.112 -27.955 -29.526 1.00 42.06 O HETATM 4309 O HOH A 622 32.911 -20.024 -22.876 1.00 45.71 O HETATM 4310 O HOH A 657 27.610 -7.253 -24.206 1.00 17.71 O HETATM 4311 O HOH A 661 45.705 -9.038 0.936 1.00 49.09 O HETATM 4312 O HOH A 662 27.502 -0.877 -30.030 1.00 38.17 O HETATM 4313 O HOH A 663 32.504 -10.012 -29.474 1.00 32.08 O HETATM 4314 O HOH A 664 29.674 -9.640 -30.714 1.00 28.96 O HETATM 4315 O HOH A 665 30.486 -8.048 -21.655 1.00 45.34 O HETATM 4316 O HOH A 667 41.923 10.544 -23.744 1.00 63.43 O HETATM 4317 O HOH A 668 21.905 -9.215 -14.464 1.00 39.26 O HETATM 4318 O HOH A 669 11.937 0.677 -33.704 1.00 50.59 O HETATM 4319 O HOH A 683 32.896 -1.663 -0.279 1.00 41.38 O HETATM 4320 O HOH A 693 15.670 -4.774 -17.659 1.00 51.59 O HETATM 4321 O HOH A 695 9.345 -8.781 -34.969 1.00 50.52 O HETATM 4322 O HOH A 696 42.320 -1.037 -2.474 1.00 27.17 O HETATM 4323 O HOH A 697 42.888 1.586 -2.728 1.00 26.39 O HETATM 4324 O HOH A 698 41.657 3.160 -1.000 1.00 29.52 O HETATM 4325 C1 GOL A 409 31.648 -10.444 -26.109 1.00 38.95 C HETATM 4326 O1 GOL A 409 30.997 -10.709 -27.327 1.00 35.57 O HETATM 4327 C2 GOL A 409 30.703 -9.616 -25.255 1.00 38.80 C HETATM 4328 O2 GOL A 409 30.481 -10.296 -24.045 1.00 37.87 O HETATM 4329 C3 GOL A 409 31.314 -8.245 -24.992 1.00 35.67 C HETATM 4330 O3 GOL A 409 30.378 -7.442 -24.307 1.00 30.83 O HETATM 4331 O HOH B 27 41.718 9.409 28.575 1.00 23.23 O HETATM 4332 O HOH B 31 29.433 2.961 21.831 1.00 23.58 O HETATM 4333 O HOH B 33 34.196 -0.115 1.541 1.00 32.18 O HETATM 4334 O HOH B 36 19.331 15.867 3.378 1.00 22.43 O HETATM 4335 O HOH B 37 14.916 10.712 11.848 1.00 34.57 O HETATM 4336 O HOH B 40 38.213 4.784 31.560 1.00 23.12 O HETATM 4337 O HOH B 42 38.902 11.915 18.012 1.00 15.91 O HETATM 4338 O HOH B 60 21.653 16.954 4.793 1.00 20.19 O HETATM 4339 O HOH B 65 38.842 13.285 14.665 1.00 35.97 O HETATM 4340 O HOH B 68 25.114 0.600 -2.393 1.00 40.11 O HETATM 4341 O HOH B 70 30.339 11.473 3.570 1.00 20.50 O HETATM 4342 O HOH B 74 49.921 5.337 20.404 1.00 30.58 O HETATM 4343 O HOH B 76 36.831 7.786 2.924 1.00 29.99 O HETATM 4344 O HOH B 79 10.614 4.967 3.918 1.00 42.19 O HETATM 4345 O HOH B 82 34.816 -10.518 4.745 1.00 38.21 O HETATM 4346 O HOH B 88 33.400 14.345 1.637 1.00 38.01 O HETATM 4347 O HOH B 89 17.587 25.040 -8.804 1.00 27.22 O HETATM 4348 O HOH B 90 12.178 15.981 2.120 1.00 27.10 O HETATM 4349 O HOH B 98 31.195 5.726 -4.886 1.00 29.33 O HETATM 4350 O HOH B 114 32.526 8.646 4.566 1.00 17.37 O HETATM 4351 O HOH B 119 40.892 -12.708 4.470 1.00 32.17 O HETATM 4352 O HOH B 125 24.849 30.171 -1.580 1.00 46.13 O HETATM 4353 O HOH B 126 9.825 28.313 -1.756 1.00 40.13 O HETATM 4354 O HOH B 127 40.083 3.780 3.555 1.00 34.06 O HETATM 4355 O HOH B 132 41.302 -2.954 3.770 1.00 33.30 O HETATM 4356 O HOH B 133 26.521 22.210 14.617 1.00 37.82 O HETATM 4357 O HOH B 136 32.864 25.463 6.894 1.00 38.31 O HETATM 4358 O HOH B 139 21.980 13.567 -14.591 1.00 54.65 O HETATM 4359 O HOH B 142 18.466 27.500 10.977 1.00 43.00 O HETATM 4360 O HOH B 144 47.533 -6.834 21.423 1.00 38.87 O HETATM 4361 O HOH B 154 25.868 27.521 10.079 1.00 39.49 O HETATM 4362 O HOH B 155 32.439 26.030 12.113 1.00 44.66 O HETATM 4363 O HOH B 171 39.319 10.641 29.518 1.00 44.70 O HETATM 4364 O HOH B 172 32.679 6.754 0.136 1.00 23.68 O HETATM 4365 O HOH B 175 50.590 3.616 26.982 1.00 39.72 O HETATM 4366 O HOH B 185 28.700 20.633 -0.668 1.00 39.45 O HETATM 4367 O HOH B 412 10.460 26.786 -6.328 1.00 58.82 O HETATM 4368 O HOH B 413 9.010 15.125 -10.497 1.00 45.10 O HETATM 4369 O HOH B 414 26.636 -10.662 6.122 1.00 20.71 O HETATM 4370 O HOH B 415 36.761 8.182 29.224 1.00 44.74 O HETATM 4371 O HOH B 416 34.966 14.118 18.336 1.00 42.46 O HETATM 4372 O HOH B 417 12.049 4.961 7.106 1.00 49.79 O HETATM 4373 O HOH B 418 44.916 -8.740 15.932 1.00 36.04 O HETATM 4374 O HOH B 419 28.851 -9.248 25.970 1.00 48.36 O HETATM 4375 O HOH B 420 17.890 27.439 -10.852 1.00 47.92 O HETATM 4376 O HOH B 421 25.826 29.890 5.458 1.00 38.36 O HETATM 4377 O HOH B 422 9.818 10.237 8.586 1.00 41.43 O HETATM 4378 O HOH B 423 44.790 9.827 17.574 1.00 22.08 O HETATM 4379 O HOH B 424 9.781 15.712 0.983 1.00 41.94 O HETATM 4380 O HOH B 425 26.722 29.714 12.261 1.00 52.52 O HETATM 4381 O HOH B 426 22.586 30.249 8.991 1.00 50.67 O HETATM 4382 O HOH B 427 41.359 -5.305 2.335 1.00 35.48 O HETATM 4383 O HOH B 428 15.415 15.971 10.863 1.00 39.13 O HETATM 4384 O HOH B 429 29.908 9.016 4.740 1.00 22.32 O HETATM 4385 O HOH B 430 25.559 4.304 7.932 1.00 19.24 O HETATM 4386 O HOH B 432 23.199 31.880 -0.336 1.00 38.68 O HETATM 4387 O HOH B 437 24.781 28.634 7.467 1.00 35.40 O HETATM 4388 O HOH B 438 14.302 16.175 -14.003 1.00 34.23 O HETATM 4389 O HOH B 448 37.738 -5.808 25.576 1.00 31.85 O HETATM 4390 O HOH B 449 30.710 -2.871 26.348 1.00 26.30 O HETATM 4391 O HOH B 450 24.946 -3.257 24.277 1.00 14.75 O HETATM 4392 O HOH B 451 35.041 17.039 5.705 1.00 34.90 O HETATM 4393 O HOH B 452 33.118 16.875 7.765 1.00 29.39 O HETATM 4394 O HOH B 453 33.781 19.131 9.092 1.00 35.16 O HETATM 4395 O HOH B 454 31.565 19.278 12.784 1.00 38.30 O HETATM 4396 O HOH B 455 31.860 16.569 12.191 1.00 34.90 O HETATM 4397 O HOH B 457 16.565 3.871 1.114 1.00 29.04 O HETATM 4398 O HOH B 458 21.265 7.281 3.831 1.00 19.41 O HETATM 4399 O HOH B 460 18.550 3.111 2.987 1.00 30.31 O HETATM 4400 O HOH B 483 32.224 13.155 -4.247 1.00 39.79 O HETATM 4401 O HOH B 486 24.444 11.800 9.274 1.00 22.90 O HETATM 4402 O HOH B 487 21.925 14.349 13.514 1.00 22.77 O HETATM 4403 O HOH B 488 24.597 13.388 13.602 1.00 36.17 O HETATM 4404 O HOH B 489 26.808 12.836 9.596 1.00 32.50 O HETATM 4405 O HOH B 490 19.803 11.864 16.073 1.00 22.41 O HETATM 4406 O HOH B 491 22.687 9.244 15.288 1.00 19.23 O HETATM 4407 O HOH B 492 21.552 8.435 17.808 1.00 32.19 O HETATM 4408 O HOH B 493 14.269 4.880 9.863 1.00 28.51 O HETATM 4409 O HOH B 495 21.028 4.239 14.092 1.00 30.43 O HETATM 4410 O HOH B 496 21.645 5.317 17.635 1.00 25.90 O HETATM 4411 O HOH B 497 11.251 20.403 6.293 1.00 49.43 O HETATM 4412 O HOH B 498 12.928 25.023 6.423 1.00 31.22 O HETATM 4413 O HOH B 500 18.261 19.215 15.739 1.00 42.76 O HETATM 4414 O HOH B 501 32.096 25.615 2.946 1.00 49.83 O HETATM 4415 O HOH B 503 8.277 17.929 -9.775 1.00 38.81 O HETATM 4416 O HOH B 508 49.969 16.893 25.603 1.00 33.09 O HETATM 4417 O HOH B 509 48.207 6.077 31.826 1.00 18.92 O HETATM 4418 O HOH B 510 32.796 2.152 28.681 1.00 34.13 O HETATM 4419 O HOH B 511 29.758 3.818 24.971 1.00 26.40 O HETATM 4420 O HOH B 513 21.376 -7.059 22.525 1.00 39.38 O HETATM 4421 O HOH B 514 23.560 -12.113 16.472 1.00 31.61 O HETATM 4422 O HOH B 522 23.447 -6.640 26.411 1.00 43.91 O HETATM 4423 O HOH B 525 50.946 -16.220 9.119 1.00 50.72 O HETATM 4424 O HOH B 528 24.808 4.074 12.695 1.00 24.02 O HETATM 4425 O HOH B 529 23.590 2.314 14.345 1.00 21.56 O HETATM 4426 O HOH B 530 26.069 10.602 13.334 1.00 35.67 O HETATM 4427 O HOH B 538 12.326 6.779 9.192 1.00 46.15 O HETATM 4428 O HOH B 539 14.675 12.961 9.951 1.00 42.14 O HETATM 4429 O HOH B 542 51.777 14.879 25.454 1.00 17.24 O HETATM 4430 O HOH B 543 44.435 15.597 22.950 1.00 47.13 O HETATM 4431 O HOH B 545 33.555 6.218 26.300 1.00 37.60 O HETATM 4432 O HOH B 546 27.566 -1.993 29.066 1.00 34.24 O HETATM 4433 O HOH B 547 27.486 -3.990 26.252 1.00 30.06 O HETATM 4434 O HOH B 553 20.182 4.712 4.590 1.00 25.26 O HETATM 4435 O HOH B 554 18.022 1.045 4.827 1.00 41.53 O HETATM 4436 O HOH B 555 20.520 0.713 4.993 1.00 36.59 O HETATM 4437 O HOH B 556 20.555 1.541 13.108 1.00 31.96 O HETATM 4438 O HOH B 577 33.792 12.808 23.975 1.00 37.65 O HETATM 4439 O HOH B 578 27.284 10.142 16.259 1.00 38.16 O HETATM 4440 O HOH B 579 23.441 9.910 19.648 1.00 40.06 O HETATM 4441 O HOH B 580 26.922 4.585 19.705 1.00 21.94 O HETATM 4442 O HOH B 581 25.847 7.118 19.455 1.00 24.01 O HETATM 4443 O HOH B 582 23.494 11.264 -7.280 1.00 23.48 O HETATM 4444 O HOH B 584 26.072 15.752 -5.344 1.00 42.84 O HETATM 4445 O HOH B 600 36.889 1.200 30.162 1.00 27.40 O HETATM 4446 O HOH B 601 36.815 2.669 32.979 1.00 37.53 O HETATM 4447 O HOH B 610 29.629 10.161 -3.934 1.00 39.24 O HETATM 4448 O HOH B 625 16.353 -0.803 0.152 1.00 47.91 O HETATM 4449 O HOH B 626 5.732 10.989 -2.848 1.00 38.76 O HETATM 4450 O HOH B 627 15.111 1.483 2.267 1.00 46.10 O HETATM 4451 O HOH B 628 32.812 11.751 1.703 1.00 47.52 O HETATM 4452 O HOH B 629 35.765 14.703 4.188 1.00 41.06 O HETATM 4453 O HOH B 630 39.255 13.907 5.406 1.00 50.15 O HETATM 4454 O HOH B 631 32.023 15.971 -0.842 1.00 42.56 O HETATM 4455 O HOH B 632 23.334 18.794 -4.997 1.00 48.20 O HETATM 4456 O HOH B 633 10.666 19.226 -6.786 1.00 43.86 O HETATM 4457 O HOH B 634 11.184 20.360 -9.262 1.00 38.72 O HETATM 4458 O HOH B 636 8.944 22.257 3.030 1.00 47.12 O HETATM 4459 O HOH B 637 23.866 29.578 -4.650 1.00 42.28 O HETATM 4460 O HOH B 638 29.339 23.657 -6.807 1.00 48.03 O HETATM 4461 O HOH B 639 11.741 22.984 7.546 1.00 45.62 O HETATM 4462 O HOH B 640 31.702 15.606 14.682 1.00 47.94 O HETATM 4463 O HOH B 641 20.752 9.687 -12.101 1.00 46.19 O HETATM 4464 O HOH B 642 27.112 5.737 23.964 1.00 44.69 O HETATM 4465 O HOH B 643 42.598 1.846 21.762 1.00 21.04 O HETATM 4466 O HOH B 644 44.063 -0.970 20.486 1.00 27.44 O HETATM 4467 O HOH B 645 48.424 12.202 17.650 1.00 40.25 O HETATM 4468 O HOH B 647 46.940 -10.982 16.452 1.00 46.63 O HETATM 4469 O HOH B 658 24.327 -2.330 9.155 1.00 28.27 O HETATM 4470 O HOH B 659 22.395 3.336 5.124 1.00 32.21 O HETATM 4471 O HOH B 660 51.347 -9.049 10.993 1.00 50.75 O HETATM 4472 O HOH B 666 11.401 27.182 5.509 1.00 46.79 O HETATM 4473 O HOH B 671 11.281 27.470 -11.897 1.00 48.37 O HETATM 4474 O HOH B 672 13.822 16.997 8.762 1.00 49.07 O HETATM 4475 O HOH B 673 20.586 -1.019 -1.577 1.00 36.64 O HETATM 4476 O HOH B 674 29.792 11.775 14.650 1.00 49.66 O HETATM 4477 O HOH B 675 33.174 9.285 22.310 1.00 30.82 O HETATM 4478 O HOH B 676 32.350 11.671 21.970 1.00 32.30 O HETATM 4479 O HOH B 677 32.510 12.910 19.188 1.00 46.83 O HETATM 4480 O HOH B 678 39.182 14.394 19.045 1.00 47.31 O HETATM 4481 O HOH B 679 43.838 12.238 18.135 1.00 49.18 O HETATM 4482 O HOH B 680 41.808 11.351 10.948 1.00 46.76 O HETATM 4483 O HOH B 681 47.433 4.430 18.909 1.00 47.42 O HETATM 4484 O HOH B 682 35.078 12.126 4.259 1.00 35.49 O HETATM 4485 O HOH B 684 47.515 -14.737 16.321 1.00 47.51 O HETATM 4486 O HOH B 685 27.863 -16.778 14.135 1.00 53.79 O HETATM 4487 O HOH B 686 34.775 -1.101 35.743 1.00 41.75 O HETATM 4488 O HOH B 687 33.778 3.611 31.178 1.00 40.00 O HETATM 4489 O HOH B 688 29.170 -0.337 31.974 1.00 44.99 O HETATM 4490 O HOH B 692 44.291 1.510 19.598 1.00 50.11 O HETATM 4491 O HOH B 694 6.474 0.180 -2.364 1.00 50.59 O HETATM 4492 O HOH B 699 45.631 -1.812 17.318 1.00 53.14 O HETATM 4493 O HOH B 700 48.976 -9.339 21.297 1.00 48.27 O HETATM 4494 C1 PEG A 410 8.997 -8.723 -32.042 1.00 61.04 C HETATM 4495 O1 PEG A 410 8.328 -7.648 -32.714 1.00 57.10 O HETATM 4496 C2 PEG A 410 7.973 -9.694 -31.458 1.00 63.48 C HETATM 4497 O2 PEG A 410 8.570 -10.982 -31.309 1.00 63.76 O HETATM 4498 C3 PEG A 410 7.615 -12.033 -31.475 1.00 64.36 C HETATM 4499 C4 PEG A 410 8.199 -13.167 -32.317 1.00 58.24 C HETATM 4500 O4 PEG A 410 7.842 -12.993 -33.698 1.00 52.79 O HETATM 4501 O HOH C 271 33.836 -9.182 31.008 1.00 52.23 O HETATM 4502 O HOH C 285 41.441 -6.684 34.750 1.00 44.05 O HETATM 4503 O HOH C 398 47.386 -3.427 25.448 1.00 52.93 O HETATM 4504 O HOH C 413 48.062 23.589 35.075 1.00 42.64 O HETATM 4505 O HOH C 414 46.112 25.518 33.680 1.00 37.93 O HETATM 4506 O HOH C 415 42.959 15.067 38.285 1.00 37.93 O HETATM 4507 O HOH C 416 42.372 12.509 38.662 1.00 25.91 O HETATM 4508 O HOH C 417 39.771 16.848 32.054 1.00 53.58 O HETATM 4509 O HOH C 440 33.440 -8.131 33.670 1.00 40.15 O HETATM 4510 O HOH C 441 34.932 -5.753 34.044 1.00 39.84 O HETATM 4511 O HOH C 517 39.297 -2.888 35.923 1.00 43.52 O HETATM 4512 O HOH C 518 49.365 25.393 39.187 1.00 38.85 O HETATM 4513 O HOH C 521 31.042 -11.565 22.956 1.00 47.39 O HETATM 4514 O HOH C 531 34.458 -14.704 18.876 1.00 56.39 O HETATM 4515 O HOH C 548 27.074 -12.894 20.414 1.00 48.67 O HETATM 4516 O HOH C 550 43.243 -11.305 30.689 1.00 48.32 O HETATM 4517 O HOH C 561 46.523 13.508 41.788 1.00 42.73 O HETATM 4518 O HOH C 562 44.409 15.226 40.890 1.00 49.66 O HETATM 4519 O HOH C 563 39.964 11.973 38.048 1.00 45.09 O HETATM 4520 O HOH C 564 39.912 10.425 40.235 1.00 34.40 O HETATM 4521 O HOH C 648 45.938 14.465 28.533 1.00 32.60 O HETATM 4522 O HOH C 649 46.307 -0.168 33.316 1.00 24.46 O HETATM 4523 O HOH C 651 42.809 -20.925 10.718 1.00 45.56 O HETATM 4524 O HOH C 701 50.061 -10.074 6.960 1.00 30.00 O HETATM 4525 C1 GOL B 1 24.415 6.382 15.850 1.00 32.21 C HETATM 4526 O1 GOL B 1 23.184 6.324 15.150 1.00 29.60 O HETATM 4527 C2 GOL B 1 25.484 7.005 14.954 1.00 30.33 C HETATM 4528 O2 GOL B 1 25.486 6.346 13.706 1.00 23.85 O HETATM 4529 C3 GOL B 1 26.862 6.901 15.606 1.00 27.64 C HETATM 4530 O3 GOL B 1 26.877 7.580 16.847 1.00 29.60 O HETATM 4531 O HOH D 67 11.537 -2.404 -45.259 1.00 28.98 O HETATM 4532 O HOH D 95 7.646 2.991 -45.167 1.00 32.59 O HETATM 4533 O HOH D 106 15.015 -6.836 -48.420 1.00 33.70 O HETATM 4534 O HOH D 173 21.351 -23.628 -41.445 1.00 38.15 O HETATM 4535 O HOH D 217 19.371 -21.131 -47.409 1.00 36.45 O HETATM 4536 O HOH D 355 12.490 -21.764 -43.161 1.00 40.79 O HETATM 4537 O HOH D 410 25.698 -24.262 -35.969 1.00 45.56 O HETATM 4538 O HOH D 418 7.578 10.812 -56.554 1.00 39.96 O HETATM 4539 O HOH D 419 7.141 13.617 -48.869 1.00 56.86 O HETATM 4540 O HOH D 515 13.398 -12.202 -52.077 1.00 34.12 O HETATM 4541 O HOH D 516 13.956 -15.226 -52.677 1.00 42.75 O HETATM 4542 O HOH D 532 10.577 3.185 -54.766 1.00 30.72 O HETATM 4543 O HOH D 533 11.370 0.550 -54.953 1.00 35.45 O HETATM 4544 O HOH D 534 10.405 -31.599 -22.850 1.00 43.25 O HETATM 4545 O HOH D 653 5.675 12.453 -50.990 1.00 52.18 O HETATM 4546 O HOH D 670 19.536 -19.907 -49.593 1.00 34.33 O HETATM 4547 O HOH D 689 16.122 -4.511 -56.276 1.00 45.38 O HETATM 4548 O HOH D 690 12.078 -19.583 -41.964 1.00 45.15 O HETATM 4549 O HOH D 691 9.467 -19.772 -41.711 1.00 49.95 O HETATM 4550 C1 GOL B 409 52.637 5.475 22.833 1.00 63.62 C HETATM 4551 O1 GOL B 409 52.463 4.085 22.993 1.00 66.56 O HETATM 4552 C2 GOL B 409 52.784 6.141 24.199 1.00 62.29 C HETATM 4553 O2 GOL B 409 53.633 5.381 25.031 1.00 62.94 O HETATM 4554 C3 GOL B 409 51.411 6.247 24.847 1.00 55.71 C HETATM 4555 O3 GOL B 409 51.313 7.449 25.568 1.00 54.21 O HETATM 4556 C1 PEG B 410 45.236 3.637 16.925 1.00 71.67 C HETATM 4557 O1 PEG B 410 44.332 4.061 17.951 1.00 71.11 O HETATM 4558 C2 PEG B 410 44.483 2.799 15.898 1.00 69.94 C HETATM 4559 O2 PEG B 410 45.388 1.884 15.278 1.00 69.42 O HETATM 4560 C3 PEG B 410 44.771 1.170 14.211 1.00 58.86 C HETATM 4561 C4 PEG B 410 45.291 -0.262 14.175 1.00 55.11 C HETATM 4562 O4 PEG B 410 44.499 -1.078 15.048 1.00 48.65 O HETATM 4563 C1 GOL B 411 21.850 3.271 8.772 1.00 40.29 C HETATM 4564 O1 GOL B 411 22.632 4.102 7.939 1.00 35.46 O HETATM 4565 C2 GOL B 411 22.616 1.972 8.957 1.00 43.85 C HETATM 4566 O2 GOL B 411 22.635 1.293 7.726 1.00 38.64 O HETATM 4567 C3 GOL B 411 21.937 1.082 9.985 1.00 47.90 C HETATM 4568 O3 GOL B 411 21.512 -0.082 9.308 1.00 48.17 O HETATM 4569 C1 GOL C 1 41.025 -10.494 28.057 1.00 56.26 C HETATM 4570 O1 GOL C 1 39.827 -9.754 27.988 1.00 55.64 O HETATM 4571 C2 GOL C 1 41.579 -10.699 26.654 1.00 56.27 C HETATM 4572 O2 GOL C 1 42.933 -10.299 26.632 1.00 56.69 O HETATM 4573 C3 GOL C 1 40.767 -9.877 25.655 1.00 50.80 C HETATM 4574 O3 GOL C 1 41.029 -8.502 25.829 1.00 49.44 O CONECT 4144 4145 4146 CONECT 4145 4144 CONECT 4146 4144 4147 4148 CONECT 4147 4146 CONECT 4148 4146 4149 CONECT 4149 4148 CONECT 4325 4326 4327 CONECT 4326 4325 CONECT 4327 4325 4328 4329 CONECT 4328 4327 CONECT 4329 4327 4330 CONECT 4330 4329 CONECT 4494 4495 4496 CONECT 4495 4494 CONECT 4496 4494 4497 CONECT 4497 4496 4498 CONECT 4498 4497 4499 CONECT 4499 4498 4500 CONECT 4500 4499 CONECT 4525 4526 4527 CONECT 4526 4525 CONECT 4527 4525 4528 4529 CONECT 4528 4527 CONECT 4529 4527 4530 CONECT 4530 4529 CONECT 4550 4551 4552 CONECT 4551 4550 CONECT 4552 4550 4553 4554 CONECT 4553 4552 CONECT 4554 4552 4555 CONECT 4555 4554 CONECT 4556 4557 4558 CONECT 4557 4556 CONECT 4558 4556 4559 CONECT 4559 4558 4560 CONECT 4560 4559 4561 CONECT 4561 4560 4562 CONECT 4562 4561 CONECT 4563 4564 4565 CONECT 4564 4563 CONECT 4565 4563 4566 4567 CONECT 4566 4565 CONECT 4567 4565 4568 CONECT 4568 4567 CONECT 4569 4570 4571 CONECT 4570 4569 CONECT 4571 4569 4572 4573 CONECT 4572 4571 CONECT 4573 4571 4574 CONECT 4574 4573 MASTER 436 0 8 24 16 0 16 6 4534 4 50 44 END
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Related entries of code: 3g9w
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
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Protein Sequence Similarity
No similar entries are found!
Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
3lk2
RCSB PDB
PDBbind
52-mer
Entry Information
PDB ID
3g9w
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
Talin2 F2-F3 domain
Ligand Name
52-mer
EC.Number
E.C.-.-.-.-
Resolution
2.17(Å)
Affinity (Kd/Ki/IC50)
Kd=36uM
Release Year
2009
Protein/NA Sequence
Check fasta file
Primary Reference
(2009) Embo J.
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):
P05556
Q71LX4
Entrez Gene ID
NCBI Entrez Gene ID:
3688
70549
ASD
Information of known allosteric effects of PDB entries
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