HEADER SIGNALING PROTEIN/PROTEIN BINDING 25-SEP-18 6IGK TITLE CRYSTAL STRUCTURE OF HUMAN ETB RECEPTOR IN COMPLEX WITH ENDOTHELIN-3 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENDOTHELIN RECEPTOR TYPE B,ENDOLYSIN,ENDOTHELIN RECEPTOR COMPND 3 TYPE B; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: ET-BR,ENDOTHELIN RECEPTOR NON-SELECTIVE TYPE,LYSIS PROTEIN, COMPND 6 LYSOZYME,MURAMIDASE; COMPND 7 EC: 3.2.1.17; COMPND 8 ENGINEERED: YES; COMPND 9 MUTATION: YES; COMPND 10 OTHER_DETAILS: CHIMERA PROTEIN OF ENDOTHELIN RECEPTOR TYPE B INSERTED COMPND 11 WITH ENDOLYSIN BETWEEN RESIDUES 303 AND 311.; COMPND 12 MOL_ID: 2; COMPND 13 MOLECULE: ENDOTHELIN-3; COMPND 14 CHAIN: B; COMPND 15 SYNONYM: ET-3,PREPROENDOTHELIN-3,PPET3; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE RB59; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 697290; SOURCE 5 GENE: EDNRB, ETRB, E, RB59_126; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF9; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: MODIFIED PFASTBAC; SOURCE 11 MOL_ID: 2; SOURCE 12 SYNTHETIC: YES; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_COMMON: HUMAN; SOURCE 15 ORGANISM_TAXID: 9606 KEYWDS ALPHA HELICAL, SIGNALING PROTEIN-PROTEIN BINDING COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR W.SHIHOYA,T.IZUME,A.INOUE,K.YAMASHITA,F.M.N.KADJI,K.HIRATA,J.AOKI, AUTHOR 2 T.NISHIZAWA,O.NUREKI REVDAT 1 21-NOV-18 6IGK 0 JRNL AUTH W.SHIHOYA,T.IZUME,A.INOUE,K.YAMASHITA,F.M.N.KADJI,K.HIRATA, JRNL AUTH 2 J.AOKI,T.NISHIZAWA,O.NUREKI JRNL TITL CRYSTAL STRUCTURES OF HUMAN ETBRECEPTOR PROVIDE MECHANISTIC JRNL TITL 2 INSIGHT INTO RECEPTOR ACTIVATION AND PARTIAL ACTIVATION. JRNL REF NAT COMMUN V. 9 4711 2018 JRNL REFN ESSN 2041-1723 JRNL PMID 30413709 JRNL DOI 10.1038/S41467-018-07094-0 REMARK 2 REMARK 2 RESOLUTION. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.13_2998 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.60 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 46782 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.185 REMARK 3 R VALUE (WORKING SET) : 0.183 REMARK 3 FREE R VALUE : 0.227 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.270 REMARK 3 FREE R VALUE TEST SET COUNT : 1998 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 49.6145 - 4.8191 1.00 3375 150 0.1865 0.2275 REMARK 3 2 4.8191 - 3.8255 1.00 3251 146 0.1696 0.2094 REMARK 3 3 3.8255 - 3.3421 1.00 3242 144 0.1624 0.2467 REMARK 3 4 3.3421 - 3.0366 1.00 3204 144 0.1768 0.2023 REMARK 3 5 3.0366 - 2.8189 1.00 3183 142 0.1661 0.1801 REMARK 3 6 2.8189 - 2.6527 1.00 3201 142 0.1649 0.2208 REMARK 3 7 2.6527 - 2.5199 1.00 3171 142 0.1667 0.2234 REMARK 3 8 2.5199 - 2.4102 1.00 3186 143 0.1798 0.2180 REMARK 3 9 2.4102 - 2.3174 1.00 3169 141 0.1834 0.2428 REMARK 3 10 2.3174 - 2.2375 1.00 3164 141 0.1993 0.2253 REMARK 3 11 2.2375 - 2.1675 1.00 3174 142 0.2074 0.2745 REMARK 3 12 2.1675 - 2.1055 1.00 3152 141 0.2456 0.2874 REMARK 3 13 2.1055 - 2.0501 1.00 3147 140 0.2770 0.2885 REMARK 3 14 2.0501 - 2.0001 1.00 3165 140 0.3583 0.3702 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.250 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.030 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 35.54 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.02 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : NULL NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 6 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ( CHAIN A AND RESID 86:164 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.967 42.034 137.416 REMARK 3 T TENSOR REMARK 3 T11: 0.2994 T22: 0.3197 REMARK 3 T33: 0.2150 T12: -0.0033 REMARK 3 T13: -0.0204 T23: 0.0032 REMARK 3 L TENSOR REMARK 3 L11: 2.0430 L22: 3.6691 REMARK 3 L33: 2.0854 L12: -0.5877 REMARK 3 L13: 0.3923 L23: 0.2668 REMARK 3 S TENSOR REMARK 3 S11: -0.1555 S12: -0.1941 S13: 0.2099 REMARK 3 S21: 0.4677 S22: 0.1318 S23: -0.3781 REMARK 3 S31: -0.3085 S32: -0.0426 S33: 0.0149 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: ( CHAIN A AND RESID 165:303 ) OR ( CHAIN A AND RESID REMARK 3 1000:1009 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.127 44.532 129.735 REMARK 3 T TENSOR REMARK 3 T11: 0.1748 T22: 0.3118 REMARK 3 T33: 0.2936 T12: 0.0021 REMARK 3 T13: 0.0303 T23: 0.0403 REMARK 3 L TENSOR REMARK 3 L11: 0.3646 L22: 4.3559 REMARK 3 L33: 1.1495 L12: -0.8803 REMARK 3 L13: 0.3714 L23: -1.5420 REMARK 3 S TENSOR REMARK 3 S11: -0.0249 S12: -0.1846 S13: -0.1758 REMARK 3 S21: 0.2988 S22: 0.1577 S23: 0.4153 REMARK 3 S31: -0.0102 S32: -0.0986 S33: -0.1465 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: ( CHAIN A AND RESID 1010:1159 ) OR ( CHAIN A AND REMARK 3 RESID 311:312 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.815 80.865 103.410 REMARK 3 T TENSOR REMARK 3 T11: 0.4148 T22: 0.2706 REMARK 3 T33: 0.2589 T12: -0.0488 REMARK 3 T13: 0.0670 T23: 0.0046 REMARK 3 L TENSOR REMARK 3 L11: 3.0008 L22: 2.0454 REMARK 3 L33: 2.5333 L12: -0.6271 REMARK 3 L13: -1.3194 L23: 0.3618 REMARK 3 S TENSOR REMARK 3 S11: 0.0179 S12: 0.2694 S13: 0.0680 REMARK 3 S21: -0.5946 S22: -0.0291 S23: -0.3174 REMARK 3 S31: -0.2673 S32: 0.1923 S33: 0.0190 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: ( CHAIN A AND RESID 313:403 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.177 44.992 126.920 REMARK 3 T TENSOR REMARK 3 T11: 0.1718 T22: 0.2623 REMARK 3 T33: 0.2633 T12: -0.0035 REMARK 3 T13: 0.0029 T23: 0.0229 REMARK 3 L TENSOR REMARK 3 L11: 0.7313 L22: 3.0778 REMARK 3 L33: 1.4084 L12: -1.0416 REMARK 3 L13: 0.2706 L23: -1.4617 REMARK 3 S TENSOR REMARK 3 S11: -0.0787 S12: -0.0168 S13: 0.1673 REMARK 3 S21: 0.0028 S22: -0.0045 S23: -0.4246 REMARK 3 S31: -0.1816 S32: 0.0360 S33: 0.0602 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: ( CHAIN B AND RESID 1:8 ) REMARK 3 ORIGIN FOR THE GROUP (A): 11.101 17.119 129.353 REMARK 3 T TENSOR REMARK 3 T11: 0.3234 T22: 0.5014 REMARK 3 T33: 0.5867 T12: -0.0075 REMARK 3 T13: 0.0108 T23: -0.0060 REMARK 3 L TENSOR REMARK 3 L11: 9.0435 L22: 3.8520 REMARK 3 L33: 5.9642 L12: 2.8909 REMARK 3 L13: 2.7445 L23: 4.7532 REMARK 3 S TENSOR REMARK 3 S11: -0.2036 S12: -0.3711 S13: -0.1624 REMARK 3 S21: 0.3021 S22: -0.3415 S23: 1.2130 REMARK 3 S31: 0.0029 S32: -1.0708 S33: 0.4689 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: ( CHAIN B AND RESID 9:21 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.699 22.590 132.731 REMARK 3 T TENSOR REMARK 3 T11: 0.2615 T22: 0.3205 REMARK 3 T33: 0.2989 T12: 0.0325 REMARK 3 T13: 0.0449 T23: 0.0529 REMARK 3 L TENSOR REMARK 3 L11: 2.1237 L22: 7.4919 REMARK 3 L33: 2.5604 L12: 0.1316 REMARK 3 L13: 0.3986 L23: 0.2153 REMARK 3 S TENSOR REMARK 3 S11: 0.0257 S12: -0.2180 S13: -0.4263 REMARK 3 S21: 0.1090 S22: -0.0203 S23: -0.1141 REMARK 3 S31: 0.2128 S32: -0.0515 S33: -0.0141 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 6IGK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-OCT-18. REMARK 100 THE DEPOSITION ID IS D_1300009132. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 27-JUL-16 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SPRING-8 REMARK 200 BEAMLINE : BL32XU REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46829 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 REMARK 200 RESOLUTION RANGE LOW (A) : 49.599 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 204.6 REMARK 200 R MERGE (I) : 0.85800 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 199.2 REMARK 200 R MERGE FOR SHELL (I) : 18.01100 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.950 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: 5GLH REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.91 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 500DME, AMMONIUM CITRATE TRIBASIC, REMARK 280 PH 6.0, LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.66500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.66500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 32.77500 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 86.14000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 32.77500 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 86.14000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 60.66500 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 32.77500 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 86.14000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 60.66500 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 32.77500 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 86.14000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 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: 3630 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 24230 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A 63 REMARK 465 GLY A 64 REMARK 465 GLY A 65 REMARK 465 LEU A 66 REMARK 465 ALA A 67 REMARK 465 PRO A 68 REMARK 465 ALA A 69 REMARK 465 GLU A 70 REMARK 465 VAL A 71 REMARK 465 PRO A 72 REMARK 465 LYS A 73 REMARK 465 GLY A 74 REMARK 465 ASP A 75 REMARK 465 ARG A 76 REMARK 465 THR A 77 REMARK 465 ALA A 78 REMARK 465 GLY A 79 REMARK 465 SER A 80 REMARK 465 PRO A 81 REMARK 465 PRO A 82 REMARK 465 ARG A 83 REMARK 465 THR A 84 REMARK 465 ILE A 85 REMARK 465 TRP A 404 REMARK 465 ALA A 405 REMARK 465 GLN A 406 REMARK 465 SER A 407 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 128 CG CD CE NZ REMARK 470 LYS A 130 CG CD CE NZ REMARK 470 ARG A 201 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 391 CG CD CE NZ 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 VAL A 260 79.60 60.03 REMARK 500 PHE A 282 -64.80 -131.66 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLC A 1209 REMARK 610 OLC A 1211 REMARK 610 OLC A 1212 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1202 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1203 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1204 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1205 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1206 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1207 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1208 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1209 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1210 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1211 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1212 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CIT A 1213 DBREF 6IGK A 66 303 UNP P24530 EDNRB_HUMAN 66 303 DBREF1 6IGK A 1000 1159 UNP A0A097J809_BPT4 DBREF2 6IGK A A0A097J809 2 161 DBREF 6IGK A 311 407 UNP P24530 EDNRB_HUMAN 311 407 DBREF 6IGK B 1 21 UNP P14138 EDN3_HUMAN 97 117 SEQADV 6IGK GLY A 63 UNP P24530 EXPRESSION TAG SEQADV 6IGK GLY A 64 UNP P24530 EXPRESSION TAG SEQADV 6IGK GLY A 65 UNP P24530 EXPRESSION TAG SEQADV 6IGK TYR A 124 UNP P24530 ARG 124 ENGINEERED MUTATION SEQADV 6IGK ALA A 154 UNP P24530 ASP 154 ENGINEERED MUTATION SEQADV 6IGK ALA A 270 UNP P24530 LYS 270 ENGINEERED MUTATION SEQADV 6IGK THR A 1052 UNP A0A097J80 CYS 54 ENGINEERED MUTATION SEQADV 6IGK ALA A 1095 UNP A0A097J80 CYS 97 ENGINEERED MUTATION SEQADV 6IGK ALA A 342 UNP P24530 SER 342 ENGINEERED MUTATION SEQADV 6IGK ALA A 381 UNP P24530 ILE 381 ENGINEERED MUTATION SEQADV 6IGK ALA A 396 UNP P24530 CYS 396 ENGINEERED MUTATION SEQADV 6IGK ALA A 400 UNP P24530 CYS 400 ENGINEERED MUTATION SEQADV 6IGK ALA A 405 UNP P24530 CYS 405 ENGINEERED MUTATION SEQRES 1 A 498 GLY GLY GLY LEU ALA PRO ALA GLU VAL PRO LYS GLY ASP SEQRES 2 A 498 ARG THR ALA GLY SER PRO PRO ARG THR ILE SER PRO PRO SEQRES 3 A 498 PRO CYS GLN GLY PRO ILE GLU ILE LYS GLU THR PHE LYS SEQRES 4 A 498 TYR ILE ASN THR VAL VAL SER CYS LEU VAL PHE VAL LEU SEQRES 5 A 498 GLY ILE ILE GLY ASN SER THR LEU LEU TYR ILE ILE TYR SEQRES 6 A 498 LYS ASN LYS CYS MET ARG ASN GLY PRO ASN ILE LEU ILE SEQRES 7 A 498 ALA SER LEU ALA LEU GLY ASP LEU LEU HIS ILE VAL ILE SEQRES 8 A 498 ALA ILE PRO ILE ASN VAL TYR LYS LEU LEU ALA GLU ASP SEQRES 9 A 498 TRP PRO PHE GLY ALA GLU MET CYS LYS LEU VAL PRO PHE SEQRES 10 A 498 ILE GLN LYS ALA SER VAL GLY ILE THR VAL LEU SER LEU SEQRES 11 A 498 CYS ALA LEU SER ILE ASP ARG TYR ARG ALA VAL ALA SER SEQRES 12 A 498 TRP SER ARG ILE LYS GLY ILE GLY VAL PRO LYS TRP THR SEQRES 13 A 498 ALA VAL GLU ILE VAL LEU ILE TRP VAL VAL SER VAL VAL SEQRES 14 A 498 LEU ALA VAL PRO GLU ALA ILE GLY PHE ASP ILE ILE THR SEQRES 15 A 498 MET ASP TYR LYS GLY SER TYR LEU ARG ILE CYS LEU LEU SEQRES 16 A 498 HIS PRO VAL GLN LYS THR ALA PHE MET GLN PHE TYR ALA SEQRES 17 A 498 THR ALA LYS ASP TRP TRP LEU PHE SER PHE TYR PHE CYS SEQRES 18 A 498 LEU PRO LEU ALA ILE THR ALA PHE PHE TYR THR LEU MET SEQRES 19 A 498 THR CYS GLU MET LEU ARG LYS ASN ILE PHE GLU MET LEU SEQRES 20 A 498 ARG ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP SEQRES 21 A 498 THR GLU GLY TYR TYR THR ILE GLY ILE GLY HIS LEU LEU SEQRES 22 A 498 THR LYS SER PRO SER LEU ASN ALA ALA LYS SER GLU LEU SEQRES 23 A 498 ASP LYS ALA ILE GLY ARG ASN THR ASN GLY VAL ILE THR SEQRES 24 A 498 LYS ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP SEQRES 25 A 498 ALA ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS SEQRES 26 A 498 PRO VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA SEQRES 27 A 498 LEU ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL SEQRES 28 A 498 ALA GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS SEQRES 29 A 498 ARG TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG SEQRES 30 A 498 TRP TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE SEQRES 31 A 498 THR THR PHE ARG THR GLY THR TRP ASP ALA TYR LEU ASN SEQRES 32 A 498 ASP HIS LEU LYS GLN ARG ARG GLU VAL ALA LYS THR VAL SEQRES 33 A 498 PHE CYS LEU VAL LEU VAL PHE ALA LEU CYS TRP LEU PRO SEQRES 34 A 498 LEU HIS LEU ALA ARG ILE LEU LYS LEU THR LEU TYR ASN SEQRES 35 A 498 GLN ASN ASP PRO ASN ARG CYS GLU LEU LEU SER PHE LEU SEQRES 36 A 498 LEU VAL LEU ASP TYR ILE GLY ILE ASN MET ALA SER LEU SEQRES 37 A 498 ASN SER CYS ALA ASN PRO ILE ALA LEU TYR LEU VAL SER SEQRES 38 A 498 LYS ARG PHE LYS ASN ALA PHE LYS SER ALA LEU CYS CYS SEQRES 39 A 498 TRP ALA GLN SER SEQRES 1 B 21 CYS THR CYS PHE THR TYR LYS ASP LYS GLU CYS VAL TYR SEQRES 2 B 21 TYR CYS HIS LEU ASP ILE ILE TRP HET OLC A1201 25 HET OLC A1202 25 HET OLC A1203 25 HET OLC A1204 25 HET OLC A1205 25 HET OLC A1206 25 HET OLC A1207 25 HET OLC A1208 25 HET OLC A1209 20 HET OLC A1210 25 HET OLC A1211 19 HET OLC A1212 19 HET CIT A1213 13 HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM CIT CITRIC ACID HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 3 OLC 12(C21 H40 O4) FORMUL 15 CIT C6 H8 O7 FORMUL 16 HOH *175(H2 O) HELIX 1 AA1 LYS A 97 ASN A 129 1 33 HELIX 2 AA2 LYS A 130 ARG A 133 5 4 HELIX 3 AA3 ASN A 134 GLU A 165 1 32 HELIX 4 AA4 PHE A 169 SER A 205 1 37 HELIX 5 AA5 PRO A 215 ALA A 233 1 19 HELIX 6 AA6 ALA A 233 GLY A 239 1 7 HELIX 7 AA7 THR A 263 PHE A 282 1 20 HELIX 8 AA8 PHE A 282 GLY A 1010 1 33 HELIX 9 AA9 SER A 1036 GLY A 1049 1 14 HELIX 10 AB1 THR A 1057 ARG A 1078 1 22 HELIX 11 AB2 LEU A 1082 LEU A 1089 1 8 HELIX 12 AB3 ASP A 1090 GLY A 1111 1 22 HELIX 13 AB4 PHE A 1112 GLN A 1121 1 10 HELIX 14 AB5 ARG A 1123 ALA A 1132 1 10 HELIX 15 AB6 SER A 1134 THR A 1140 1 7 HELIX 16 AB7 THR A 1140 GLY A 1154 1 15 HELIX 17 AB8 TRP A 1156 LEU A 311 5 5 HELIX 18 AB9 ASN A 312 TYR A 350 1 39 HELIX 19 AC1 ARG A 357 SER A 390 1 34 HELIX 20 AC2 SER A 390 CYS A 402 1 13 HELIX 21 AC3 ASP B 8 ASP B 18 1 11 SHEET 1 AA1 2 PHE A 240 TYR A 247 0 SHEET 2 AA1 2 SER A 250 LEU A 257 -1 O ILE A 254 N ILE A 243 SHEET 1 AA2 3 ARG A1012 LYS A1017 0 SHEET 2 AA2 3 TYR A1023 GLY A1026 -1 O GLY A1026 N ARG A1012 SHEET 3 AA2 3 HIS A1029 THR A1032 -1 O LEU A1031 N TYR A1023 SSBOND 1 CYS A 90 CYS A 358 1555 1555 2.06 SSBOND 2 CYS A 174 CYS A 255 1555 1555 2.06 SSBOND 3 CYS B 1 CYS B 15 1555 1555 2.06 SSBOND 4 CYS B 3 CYS B 11 1555 1555 2.05 SITE 1 AC1 6 LYS A 101 TYR A 102 THR A 105 VAL A 106 SITE 2 AC1 6 LEU A 110 LEU A 114 SITE 1 AC2 2 PRO A 156 LEU A 163 SITE 1 AC3 3 LEU A 145 ILE A 222 OLC A1204 SITE 1 AC4 5 LEU A 149 LYS A 175 PHE A 179 ALA A 183 SITE 2 AC4 5 OLC A1203 SITE 1 AC5 3 LEU A 341 LEU A 349 OLC A1210 SITE 1 AC6 5 TRP A 275 CYS A 283 LEU A 337 LEU A 341 SITE 2 AC6 5 ILE A 344 SITE 1 AC7 3 LEU A 284 ILE A 288 OLC A1208 SITE 1 AC8 7 TYR A 200 ALA A 287 PHE A 291 LEU A 295 SITE 2 AC8 7 VAL A 366 OLC A1207 HOH A1367 SITE 1 AC9 5 VAL A 231 ILE A 238 THR A 263 PHE A 265 SITE 2 AC9 5 TRP A 276 SITE 1 AD1 7 CYS A 327 LEU A 334 MET A 374 ALA A 385 SITE 2 AD1 7 LEU A 388 VAL A 389 OLC A1205 SITE 1 AD2 3 TRP A 275 SER A 279 OLC A1212 SITE 1 AD3 5 TRP A 275 TRP A 276 SER A 279 PHE A 280 SITE 2 AD3 5 OLC A1211 SITE 1 AD4 5 GLY A1111 ASN A1114 SER A1115 ASN A1130 SITE 2 AD4 5 HOH A1303 CRYST1 65.550 172.280 121.330 90.00 90.00 90.00 C 2 2 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 0.015256 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005805 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008242 0.00000 ATOM 1 N SER A 86 11.071 7.081 123.833 1.00 69.08 N ANISOU 1 N SER A 86 8649 6571 11028 -1789 -979 -942 N ATOM 2 CA SER A 86 11.983 7.518 124.890 1.00 72.18 C ANISOU 2 CA SER A 86 9085 7041 11299 -1670 -798 -735 C ATOM 3 C SER A 86 13.352 7.878 124.317 1.00 59.10 C ANISOU 3 C SER A 86 7551 5478 9425 -1416 -785 -864 C ATOM 4 O SER A 86 13.948 7.087 123.581 1.00 66.38 O ANISOU 4 O SER A 86 8607 6236 10376 -1324 -881 -1051 O ATOM 5 CB SER A 86 12.127 6.432 125.957 1.00 81.35 C ANISOU 5 CB SER A 86 10335 7919 12656 -1754 -752 -557 C ATOM 6 OG SER A 86 12.831 6.927 127.083 1.00 84.55 O ANISOU 6 OG SER A 86 10774 8415 12936 -1656 -595 -339 O ATOM 7 N PRO A 87 13.840 9.073 124.641 1.00 53.87 N ANISOU 7 N PRO A 87 6836 5075 8556 -1303 -661 -770 N ATOM 8 CA PRO A 87 15.083 9.566 124.025 1.00 49.46 C ANISOU 8 CA PRO A 87 6355 4638 7802 -1080 -630 -890 C ATOM 9 C PRO A 87 16.290 8.805 124.540 1.00 58.70 C ANISOU 9 C PRO A 87 7644 5629 9031 -951 -601 -858 C ATOM 10 O PRO A 87 16.384 8.507 125.739 1.00 59.51 O ANISOU 10 O PRO A 87 7758 5632 9222 -991 -550 -654 O ATOM 11 CB PRO A 87 15.131 11.040 124.454 1.00 47.50 C ANISOU 11 CB PRO A 87 5999 4682 7367 -1038 -506 -758 C ATOM 12 CG PRO A 87 13.739 11.365 124.902 1.00 49.34 C ANISOU 12 CG PRO A 87 6096 4976 7676 -1226 -504 -642 C ATOM 13 CD PRO A 87 13.197 10.100 125.476 1.00 46.96 C ANISOU 13 CD PRO A 87 5818 4403 7620 -1380 -545 -572 C ATOM 14 N PRO A 88 17.247 8.490 123.673 1.00 60.81 N ANISOU 14 N PRO A 88 8005 5855 9244 -781 -629 -1053 N ATOM 15 CA PRO A 88 18.438 7.771 124.121 1.00 58.91 C ANISOU 15 CA PRO A 88 7857 5445 9081 -634 -611 -1038 C ATOM 16 C PRO A 88 19.295 8.655 125.008 1.00 45.96 C ANISOU 16 C PRO A 88 6153 3973 7337 -529 -494 -868 C ATOM 17 O PRO A 88 19.192 9.895 124.968 1.00 39.15 O ANISOU 17 O PRO A 88 5192 3373 6310 -530 -415 -822 O ATOM 18 CB PRO A 88 19.159 7.432 122.808 1.00 54.54 C ANISOU 18 CB PRO A 88 7390 4865 8468 -469 -644 -1317 C ATOM 19 CG PRO A 88 18.792 8.563 121.910 1.00 55.53 C ANISOU 19 CG PRO A 88 7452 5269 8377 -473 -606 -1405 C ATOM 20 CD PRO A 88 17.372 8.940 122.273 1.00 53.65 C ANISOU 20 CD PRO A 88 7122 5091 8172 -691 -654 -1284 C ATOM 21 N PRO A 89 20.150 8.063 125.835 1.00 46.37 N ANISOU 21 N PRO A 89 6261 3870 7486 -433 -497 -774 N ATOM 22 CA PRO A 89 21.141 8.873 126.546 1.00 43.79 C ANISOU 22 CA PRO A 89 5876 3697 7067 -305 -419 -658 C ATOM 23 C PRO A 89 22.138 9.454 125.552 1.00 40.21 C ANISOU 23 C PRO A 89 5370 3404 6504 -132 -358 -842 C ATOM 24 O PRO A 89 22.255 8.999 124.412 1.00 40.88 O ANISOU 24 O PRO A 89 5504 3439 6591 -73 -375 -1056 O ATOM 25 CB PRO A 89 21.807 7.876 127.500 1.00 43.21 C ANISOU 25 CB PRO A 89 5897 3375 7146 -228 -482 -549 C ATOM 26 CG PRO A 89 21.647 6.544 126.818 1.00 43.82 C ANISOU 26 CG PRO A 89 6088 3175 7387 -230 -576 -705 C ATOM 27 CD PRO A 89 20.350 6.611 126.041 1.00 43.94 C ANISOU 27 CD PRO A 89 6085 3228 7384 -415 -593 -795 C ATOM 28 N CYS A 90 22.852 10.480 125.996 1.00 37.48 N ANISOU 28 N CYS A 90 4929 3251 6059 -55 -280 -756 N ATOM 29 CA CYS A 90 23.885 11.081 125.168 1.00 37.07 C ANISOU 29 CA CYS A 90 4808 3351 5926 99 -193 -898 C ATOM 30 C CYS A 90 25.149 10.262 125.177 1.00 38.73 C ANISOU 30 C CYS A 90 5030 3410 6275 289 -212 -983 C ATOM 31 O CYS A 90 25.452 9.582 126.153 1.00 39.57 O ANISOU 31 O CYS A 90 5175 3342 6517 324 -296 -871 O ATOM 32 CB CYS A 90 24.266 12.460 125.680 1.00 41.84 C ANISOU 32 CB CYS A 90 5293 4190 6413 106 -112 -777 C ATOM 33 SG CYS A 90 23.060 13.714 125.217 1.00 44.44 S ANISOU 33 SG CYS A 90 5585 4754 6548 -49 -55 -747 S ATOM 34 N GLN A 91 25.918 10.391 124.101 1.00 39.33 N ANISOU 34 N GLN A 91 5070 3564 6311 424 -122 -1173 N ATOM 35 CA GLN A 91 27.257 9.823 124.091 1.00 40.90 C ANISOU 35 CA GLN A 91 5228 3666 6647 630 -108 -1260 C ATOM 36 C GLN A 91 28.257 10.725 124.810 1.00 39.82 C ANISOU 36 C GLN A 91 4927 3679 6523 706 -58 -1146 C ATOM 37 O GLN A 91 29.248 10.226 125.349 1.00 52.46 O ANISOU 37 O GLN A 91 6477 5170 8286 853 -110 -1137 O ATOM 38 CB GLN A 91 27.688 9.551 122.652 1.00 42.41 C ANISOU 38 CB GLN A 91 5446 3877 6792 752 -7 -1517 C ATOM 39 CG GLN A 91 27.008 8.316 122.075 1.00 44.37 C ANISOU 39 CG GLN A 91 5871 3893 7095 732 -107 -1663 C ATOM 40 CD GLN A 91 27.407 7.050 122.845 1.00 46.23 C ANISOU 40 CD GLN A 91 6167 3827 7570 817 -236 -1634 C ATOM 41 OE1 GLN A 91 28.566 6.646 122.837 1.00 47.66 O ANISOU 41 OE1 GLN A 91 6296 3940 7872 1020 -208 -1713 O ATOM 42 NE2 GLN A 91 26.447 6.456 123.539 1.00 46.37 N ANISOU 42 NE2 GLN A 91 6289 3664 7665 662 -372 -1507 N ATOM 43 N GLY A 92 28.001 12.036 124.861 1.00 37.73 N ANISOU 43 N GLY A 92 4580 3649 6107 610 20 -1060 N ATOM 44 CA GLY A 92 28.882 12.978 125.527 1.00 36.78 C ANISOU 44 CA GLY A 92 4306 3668 6002 658 53 -960 C ATOM 45 C GLY A 92 28.282 13.644 126.756 1.00 38.01 C ANISOU 45 C GLY A 92 4470 3877 6097 531 -26 -745 C ATOM 46 O GLY A 92 27.091 13.519 127.047 1.00 34.39 O ANISOU 46 O GLY A 92 4117 3381 5567 390 -72 -660 O ATOM 47 N PRO A 93 29.102 14.382 127.500 1.00 36.10 N ANISOU 47 N PRO A 93 4108 3723 5886 580 -41 -660 N ATOM 48 CA PRO A 93 28.630 14.976 128.751 1.00 36.14 C ANISOU 48 CA PRO A 93 4144 3767 5822 486 -126 -467 C ATOM 49 C PRO A 93 27.936 16.311 128.527 1.00 33.56 C ANISOU 49 C PRO A 93 3786 3649 5317 356 -32 -424 C ATOM 50 O PRO A 93 28.107 16.977 127.503 1.00 35.77 O ANISOU 50 O PRO A 93 3993 4063 5534 354 93 -523 O ATOM 51 CB PRO A 93 29.926 15.171 129.549 1.00 44.79 C ANISOU 51 CB PRO A 93 5123 4856 7039 615 -209 -430 C ATOM 52 CG PRO A 93 30.940 15.506 128.482 1.00 42.18 C ANISOU 52 CG PRO A 93 4622 4623 6783 712 -80 -593 C ATOM 53 CD PRO A 93 30.524 14.693 127.249 1.00 39.87 C ANISOU 53 CD PRO A 93 4410 4264 6476 726 15 -744 C ATOM 54 N ILE A 94 27.122 16.682 129.510 1.00 30.56 N ANISOU 54 N ILE A 94 3477 3287 4849 253 -88 -269 N ATOM 55 CA ILE A 94 26.642 18.057 129.667 1.00 31.80 C ANISOU 55 CA ILE A 94 3596 3629 4858 161 -30 -203 C ATOM 56 C ILE A 94 27.490 18.702 130.750 1.00 38.06 C ANISOU 56 C ILE A 94 4332 4457 5673 216 -107 -119 C ATOM 57 O ILE A 94 27.498 18.228 131.894 1.00 34.89 O ANISOU 57 O ILE A 94 4014 3955 5290 239 -225 -9 O ATOM 58 CB ILE A 94 25.160 18.107 130.060 1.00 30.93 C ANISOU 58 CB ILE A 94 3588 3525 4637 22 -30 -101 C ATOM 59 CG1 ILE A 94 24.286 17.445 129.008 1.00 31.37 C ANISOU 59 CG1 ILE A 94 3690 3535 4694 -42 10 -195 C ATOM 60 CG2 ILE A 94 24.742 19.569 130.314 1.00 27.25 C ANISOU 60 CG2 ILE A 94 3083 3241 4030 -45 22 -38 C ATOM 61 CD1 ILE A 94 22.857 17.171 129.473 1.00 36.31 C ANISOU 61 CD1 ILE A 94 4393 4121 5283 -180 -6 -95 C ATOM 62 N GLU A 95 28.208 19.774 130.410 1.00 30.38 N ANISOU 62 N GLU A 95 3228 3618 4696 235 -50 -165 N ATOM 63 CA GLU A 95 29.117 20.349 131.384 1.00 30.21 C ANISOU 63 CA GLU A 95 3136 3616 4728 290 -151 -111 C ATOM 64 C GLU A 95 29.370 21.811 131.050 1.00 31.37 C ANISOU 64 C GLU A 95 3174 3923 4821 238 -70 -130 C ATOM 65 O GLU A 95 29.190 22.257 129.911 1.00 29.89 O ANISOU 65 O GLU A 95 2944 3824 4591 196 77 -199 O ATOM 66 CB GLU A 95 30.440 19.568 131.450 1.00 35.52 C ANISOU 66 CB GLU A 95 3707 4185 5604 437 -232 -178 C ATOM 67 CG GLU A 95 31.110 19.360 130.110 1.00 44.96 C ANISOU 67 CG GLU A 95 4772 5407 6905 496 -92 -332 C ATOM 68 CD GLU A 95 32.325 18.431 130.188 1.00 55.52 C ANISOU 68 CD GLU A 95 6005 6625 8465 661 -167 -406 C ATOM 69 OE1 GLU A 95 33.288 18.667 129.427 1.00 67.55 O ANISOU 69 OE1 GLU A 95 7347 8210 10110 728 -61 -518 O ATOM 70 OE2 GLU A 95 32.321 17.476 131.004 1.00 49.56 O ANISOU 70 OE2 GLU A 95 5349 5715 7769 729 -325 -349 O ATOM 71 N ILE A 96 29.791 22.545 132.071 1.00 28.93 N ANISOU 71 N ILE A 96 2841 3640 4512 243 -177 -65 N ATOM 72 CA ILE A 96 30.207 23.937 131.944 1.00 29.12 C ANISOU 72 CA ILE A 96 2758 3781 4526 197 -135 -79 C ATOM 73 C ILE A 96 31.654 23.995 132.397 1.00 32.44 C ANISOU 73 C ILE A 96 3018 4166 5139 284 -249 -118 C ATOM 74 O ILE A 96 31.985 23.516 133.488 1.00 31.79 O ANISOU 74 O ILE A 96 2982 4000 5097 354 -434 -71 O ATOM 75 CB ILE A 96 29.307 24.880 132.768 1.00 31.76 C ANISOU 75 CB ILE A 96 3210 4172 4685 117 -175 15 C ATOM 76 CG1 ILE A 96 27.828 24.687 132.375 1.00 26.85 C ANISOU 76 CG1 ILE A 96 2718 3577 3906 42 -76 53 C ATOM 77 CG2 ILE A 96 29.741 26.329 132.580 1.00 26.84 C ANISOU 77 CG2 ILE A 96 2487 3642 4067 67 -138 -6 C ATOM 78 CD1 ILE A 96 26.800 25.519 133.196 1.00 26.22 C ANISOU 78 CD1 ILE A 96 2752 3554 3657 -22 -91 143 C ATOM 79 N LYS A 97 32.522 24.524 131.544 1.00 32.99 N ANISOU 79 N LYS A 97 2901 4298 5336 282 -138 -199 N ATOM 80 CA LYS A 97 33.945 24.513 131.844 1.00 31.86 C ANISOU 80 CA LYS A 97 2555 4124 5428 364 -232 -252 C ATOM 81 C LYS A 97 34.285 25.584 132.874 1.00 38.51 C ANISOU 81 C LYS A 97 3364 4987 6279 322 -392 -207 C ATOM 82 O LYS A 97 33.702 26.667 132.891 1.00 34.24 O ANISOU 82 O LYS A 97 2887 4515 5606 216 -342 -168 O ATOM 83 CB LYS A 97 34.752 24.729 130.565 1.00 40.05 C ANISOU 83 CB LYS A 97 3387 5223 6608 366 -25 -351 C ATOM 84 CG LYS A 97 34.452 23.729 129.461 1.00 47.36 C ANISOU 84 CG LYS A 97 4361 6131 7503 418 138 -421 C ATOM 85 CD LYS A 97 34.894 22.328 129.863 1.00 54.57 C ANISOU 85 CD LYS A 97 5270 6911 8553 565 10 -460 C ATOM 86 CE LYS A 97 34.784 21.357 128.691 1.00 65.13 C ANISOU 86 CE LYS A 97 6636 8218 9893 630 173 -563 C ATOM 87 NZ LYS A 97 35.552 21.828 127.495 1.00 70.26 N ANISOU 87 NZ LYS A 97 7106 8969 10622 638 411 -661 N ATOM 88 N GLU A 98 35.264 25.280 133.722 1.00 31.90 N ANISOU 88 N GLU A 98 2429 4082 5610 415 -600 -223 N ATOM 89 CA GLU A 98 35.588 26.184 134.819 1.00 36.08 C ANISOU 89 CA GLU A 98 2957 4613 6139 390 -803 -195 C ATOM 90 C GLU A 98 36.109 27.535 134.322 1.00 39.21 C ANISOU 90 C GLU A 98 3173 5087 6639 280 -710 -239 C ATOM 91 O GLU A 98 35.842 28.566 134.948 1.00 37.92 O ANISOU 91 O GLU A 98 3083 4942 6382 206 -798 -209 O ATOM 92 CB GLU A 98 36.616 25.531 135.749 1.00 51.57 C ANISOU 92 CB GLU A 98 4836 6480 8277 526 -1072 -215 C ATOM 93 CG GLU A 98 36.724 26.221 137.100 1.00 75.52 C ANISOU 93 CG GLU A 98 7964 9494 11236 524 -1338 -178 C ATOM 94 CD GLU A 98 36.588 25.256 138.267 1.00 94.79 C ANISOU 94 CD GLU A 98 10609 11833 13576 650 -1578 -107 C ATOM 95 OE1 GLU A 98 37.436 24.345 138.389 1.00100.40 O ANISOU 95 OE1 GLU A 98 11211 12460 14474 783 -1711 -138 O ATOM 96 OE2 GLU A 98 35.625 25.405 139.055 1.00 99.17 O ANISOU 96 OE2 GLU A 98 11435 12386 13859 623 -1623 -16 O ATOM 97 N THR A 99 36.880 27.554 133.227 1.00 36.19 N ANISOU 97 N THR A 99 2558 4740 6452 271 -528 -310 N ATOM 98 CA THR A 99 37.352 28.836 132.694 1.00 38.33 C ANISOU 98 CA THR A 99 2665 5073 6824 149 -408 -331 C ATOM 99 C THR A 99 36.185 29.758 132.351 1.00 36.26 C ANISOU 99 C THR A 99 2599 4869 6310 27 -275 -266 C ATOM 100 O THR A 99 36.242 30.967 132.606 1.00 36.65 O ANISOU 100 O THR A 99 2633 4927 6363 -72 -308 -249 O ATOM 101 CB THR A 99 38.214 28.633 131.450 1.00 39.21 C ANISOU 101 CB THR A 99 2529 5224 7144 157 -168 -401 C ATOM 102 OG1 THR A 99 39.297 27.747 131.742 1.00 40.10 O ANISOU 102 OG1 THR A 99 2439 5282 7515 291 -288 -472 O ATOM 103 CG2 THR A 99 38.779 29.990 130.974 1.00 37.79 C ANISOU 103 CG2 THR A 99 2174 5092 7092 15 -41 -402 C ATOM 104 N PHE A 100 35.119 29.209 131.766 1.00 31.00 N ANISOU 104 N PHE A 100 2112 4230 5436 35 -136 -235 N ATOM 105 CA PHE A 100 33.943 30.028 131.517 1.00 35.39 C ANISOU 105 CA PHE A 100 2850 4838 5758 -60 -43 -174 C ATOM 106 C PHE A 100 33.312 30.501 132.821 1.00 39.82 C ANISOU 106 C PHE A 100 3577 5371 6180 -70 -243 -121 C ATOM 107 O PHE A 100 32.849 31.642 132.913 1.00 37.21 O ANISOU 107 O PHE A 100 3316 5065 5755 -151 -227 -91 O ATOM 108 CB PHE A 100 32.910 29.275 130.687 1.00 28.86 C ANISOU 108 CB PHE A 100 2167 4042 4756 -44 107 -163 C ATOM 109 CG PHE A 100 31.604 30.022 130.579 1.00 33.89 C ANISOU 109 CG PHE A 100 2988 4727 5161 -120 159 -100 C ATOM 110 CD1 PHE A 100 31.521 31.190 129.809 1.00 34.87 C ANISOU 110 CD1 PHE A 100 3096 4905 5249 -208 297 -84 C ATOM 111 CD2 PHE A 100 30.486 29.615 131.297 1.00 29.93 C ANISOU 111 CD2 PHE A 100 2669 4211 4493 -103 69 -49 C ATOM 112 CE1 PHE A 100 30.337 31.900 129.716 1.00 29.22 C ANISOU 112 CE1 PHE A 100 2540 4225 4337 -259 327 -29 C ATOM 113 CE2 PHE A 100 29.295 30.344 131.225 1.00 33.48 C ANISOU 113 CE2 PHE A 100 3256 4709 4757 -162 117 1 C ATOM 114 CZ PHE A 100 29.224 31.489 130.416 1.00 25.15 C ANISOU 114 CZ PHE A 100 2179 3705 3671 -232 236 6 C ATOM 115 N LYS A 101 33.273 29.636 133.836 1.00 37.99 N ANISOU 115 N LYS A 101 3429 5081 5923 20 -427 -106 N ATOM 116 CA LYS A 101 32.694 30.037 135.116 1.00 37.82 C ANISOU 116 CA LYS A 101 3590 5039 5742 25 -603 -55 C ATOM 117 C LYS A 101 33.442 31.212 135.716 1.00 39.61 C ANISOU 117 C LYS A 101 3735 5249 6064 -16 -746 -91 C ATOM 118 O LYS A 101 32.826 32.100 136.320 1.00 38.26 O ANISOU 118 O LYS A 101 3709 5087 5742 -56 -799 -68 O ATOM 119 CB LYS A 101 32.694 28.874 136.105 1.00 31.16 C ANISOU 119 CB LYS A 101 2855 4125 4861 135 -777 -21 C ATOM 120 CG LYS A 101 31.695 27.777 135.767 1.00 33.23 C ANISOU 120 CG LYS A 101 3254 4378 4996 156 -662 31 C ATOM 121 CD LYS A 101 31.750 26.663 136.803 1.00 32.60 C ANISOU 121 CD LYS A 101 3298 4204 4886 258 -836 85 C ATOM 122 CE LYS A 101 30.776 25.539 136.413 1.00 38.50 C ANISOU 122 CE LYS A 101 4166 4917 5543 257 -715 137 C ATOM 123 NZ LYS A 101 30.505 24.628 137.559 1.00 41.44 N ANISOU 123 NZ LYS A 101 4726 5194 5824 327 -858 232 N ATOM 124 N TYR A 102 34.776 31.223 135.595 1.00 38.55 N ANISOU 124 N TYR A 102 3364 5085 6197 -4 -818 -157 N ATOM 125 CA TYR A 102 35.544 32.344 136.130 1.00 38.89 C ANISOU 125 CA TYR A 102 3304 5099 6373 -61 -970 -202 C ATOM 126 C TYR A 102 35.189 33.640 135.422 1.00 35.92 C ANISOU 126 C TYR A 102 2922 4756 5968 -197 -799 -192 C ATOM 127 O TYR A 102 34.939 34.663 136.072 1.00 38.78 O ANISOU 127 O TYR A 102 3387 5092 6255 -245 -909 -196 O ATOM 128 CB TYR A 102 37.042 32.088 136.007 1.00 42.56 C ANISOU 128 CB TYR A 102 3467 5530 7175 -34 -1058 -277 C ATOM 129 CG TYR A 102 37.668 31.543 137.260 1.00 57.32 C ANISOU 129 CG TYR A 102 5340 7330 9108 82 -1388 -306 C ATOM 130 CD1 TYR A 102 38.178 32.390 138.230 1.00 62.94 C ANISOU 130 CD1 TYR A 102 6040 7994 9880 59 -1651 -352 C ATOM 131 CD2 TYR A 102 37.753 30.173 137.471 1.00 68.44 C ANISOU 131 CD2 TYR A 102 6781 8707 10515 221 -1454 -290 C ATOM 132 CE1 TYR A 102 38.761 31.885 139.382 1.00 74.27 C ANISOU 132 CE1 TYR A 102 7500 9365 11353 179 -1982 -381 C ATOM 133 CE2 TYR A 102 38.330 29.658 138.616 1.00 75.44 C ANISOU 133 CE2 TYR A 102 7695 9522 11448 341 -1772 -304 C ATOM 134 CZ TYR A 102 38.833 30.516 139.567 1.00 79.23 C ANISOU 134 CZ TYR A 102 8167 9968 11968 323 -2040 -349 C ATOM 135 OH TYR A 102 39.407 29.996 140.705 1.00 85.10 O ANISOU 135 OH TYR A 102 8958 10640 12737 456 -2382 -364 O ATOM 136 N ILE A 103 35.216 33.626 134.086 1.00 36.47 N ANISOU 136 N ILE A 103 2884 4875 6097 -251 -535 -183 N ATOM 137 CA ILE A 103 34.981 34.849 133.318 1.00 41.11 C ANISOU 137 CA ILE A 103 3468 5482 6669 -377 -365 -158 C ATOM 138 C ILE A 103 33.564 35.349 133.555 1.00 39.61 C ANISOU 138 C ILE A 103 3548 5312 6189 -387 -349 -102 C ATOM 139 O ILE A 103 33.340 36.539 133.802 1.00 40.44 O ANISOU 139 O ILE A 103 3720 5387 6260 -457 -385 -94 O ATOM 140 CB ILE A 103 35.242 34.616 131.816 1.00 44.42 C ANISOU 140 CB ILE A 103 3759 5958 7163 -413 -75 -149 C ATOM 141 CG1 ILE A 103 36.600 33.961 131.567 1.00 40.00 C ANISOU 141 CG1 ILE A 103 2917 5388 6893 -376 -62 -213 C ATOM 142 CG2 ILE A 103 35.155 35.936 131.047 1.00 51.10 C ANISOU 142 CG2 ILE A 103 4602 6805 8008 -546 90 -106 C ATOM 143 CD1 ILE A 103 37.760 34.678 132.156 1.00 47.14 C ANISOU 143 CD1 ILE A 103 3605 6232 8075 -435 -216 -258 C ATOM 144 N ASN A 104 32.584 34.434 133.507 1.00 28.75 N ANISOU 144 N ASN A 104 2323 3980 4620 -315 -299 -67 N ATOM 145 CA ASN A 104 31.186 34.829 133.643 1.00 30.89 C ANISOU 145 CA ASN A 104 2814 4283 4641 -320 -258 -15 C ATOM 146 C ASN A 104 30.885 35.381 135.035 1.00 33.85 C ANISOU 146 C ASN A 104 3331 4617 4914 -293 -459 -20 C ATOM 147 O ASN A 104 30.078 36.312 135.172 1.00 35.18 O ANISOU 147 O ASN A 104 3629 4791 4948 -320 -435 -2 O ATOM 148 CB ASN A 104 30.286 33.639 133.310 1.00 27.90 C ANISOU 148 CB ASN A 104 2529 3950 4123 -262 -170 16 C ATOM 149 CG ASN A 104 28.844 34.043 133.073 1.00 32.18 C ANISOU 149 CG ASN A 104 3235 4540 4451 -280 -78 65 C ATOM 150 OD1 ASN A 104 28.483 34.475 131.975 1.00 32.72 O ANISOU 150 OD1 ASN A 104 3297 4648 4487 -327 74 78 O ATOM 151 ND2 ASN A 104 28.009 33.901 134.100 1.00 27.69 N ANISOU 151 ND2 ASN A 104 2816 3970 3734 -237 -167 94 N ATOM 152 N THR A 105 31.543 34.857 136.069 1.00 33.24 N ANISOU 152 N THR A 105 3241 4496 4895 -228 -663 -50 N ATOM 153 CA THR A 105 31.293 35.336 137.427 1.00 33.84 C ANISOU 153 CA THR A 105 3483 4535 4841 -188 -862 -63 C ATOM 154 C THR A 105 31.922 36.709 137.666 1.00 38.36 C ANISOU 154 C THR A 105 4003 5048 5526 -259 -969 -125 C ATOM 155 O THR A 105 31.344 37.546 138.375 1.00 34.90 O ANISOU 155 O THR A 105 3735 4588 4938 -252 -1043 -139 O ATOM 156 CB THR A 105 31.797 34.312 138.447 1.00 34.02 C ANISOU 156 CB THR A 105 3539 4522 4866 -85 -1065 -68 C ATOM 157 OG1 THR A 105 31.052 33.095 138.299 1.00 41.49 O ANISOU 157 OG1 THR A 105 4573 5500 5691 -30 -961 1 O ATOM 158 CG2 THR A 105 31.620 34.818 139.861 1.00 32.27 C ANISOU 158 CG2 THR A 105 3514 4264 4483 -32 -1278 -87 C ATOM 159 N VAL A 106 33.101 36.965 137.087 1.00 33.43 N ANISOU 159 N VAL A 106 3140 4389 5175 -329 -971 -167 N ATOM 160 CA VAL A 106 33.673 38.311 137.158 1.00 35.23 C ANISOU 160 CA VAL A 106 3298 4544 5544 -428 -1046 -218 C ATOM 161 C VAL A 106 32.727 39.313 136.511 1.00 40.78 C ANISOU 161 C VAL A 106 4120 5254 6120 -495 -865 -173 C ATOM 162 O VAL A 106 32.438 40.379 137.076 1.00 40.40 O ANISOU 162 O VAL A 106 4197 5143 6009 -518 -963 -204 O ATOM 163 CB VAL A 106 35.065 38.349 136.503 1.00 40.55 C ANISOU 163 CB VAL A 106 3660 5186 6559 -509 -1025 -254 C ATOM 164 CG1 VAL A 106 35.581 39.810 136.415 1.00 45.91 C ANISOU 164 CG1 VAL A 106 4261 5774 7408 -647 -1062 -290 C ATOM 165 CG2 VAL A 106 36.043 37.494 137.299 1.00 39.60 C ANISOU 165 CG2 VAL A 106 3416 5042 6589 -425 -1262 -314 C ATOM 166 N VAL A 107 32.199 38.971 135.331 1.00 35.33 N ANISOU 166 N VAL A 107 3409 4634 5379 -514 -615 -105 N ATOM 167 CA VAL A 107 31.250 39.860 134.667 1.00 35.03 C ANISOU 167 CA VAL A 107 3492 4604 5212 -559 -460 -55 C ATOM 168 C VAL A 107 30.013 40.074 135.540 1.00 39.43 C ANISOU 168 C VAL A 107 4291 5176 5515 -476 -531 -52 C ATOM 169 O VAL A 107 29.576 41.214 135.755 1.00 32.34 O ANISOU 169 O VAL A 107 3505 4224 4560 -496 -557 -64 O ATOM 170 CB VAL A 107 30.896 39.315 133.274 1.00 35.91 C ANISOU 170 CB VAL A 107 3557 4796 5290 -573 -209 9 C ATOM 171 CG1 VAL A 107 29.739 40.089 132.678 1.00 35.21 C ANISOU 171 CG1 VAL A 107 3624 4724 5030 -586 -86 66 C ATOM 172 CG2 VAL A 107 32.130 39.398 132.360 1.00 34.92 C ANISOU 172 CG2 VAL A 107 3205 4653 5411 -663 -97 8 C ATOM 173 N SER A 108 29.446 38.981 136.073 1.00 30.66 N ANISOU 173 N SER A 108 3262 4129 4258 -381 -555 -37 N ATOM 174 CA SER A 108 28.278 39.072 136.951 1.00 31.00 C ANISOU 174 CA SER A 108 3519 4197 4062 -300 -591 -28 C ATOM 175 C SER A 108 28.524 40.010 138.127 1.00 34.93 C ANISOU 175 C SER A 108 4129 4615 4528 -278 -788 -100 C ATOM 176 O SER A 108 27.653 40.816 138.477 1.00 39.44 O ANISOU 176 O SER A 108 4856 5178 4952 -246 -772 -111 O ATOM 177 CB SER A 108 27.888 37.684 137.478 1.00 30.62 C ANISOU 177 CB SER A 108 3527 4206 3900 -217 -602 7 C ATOM 178 OG SER A 108 27.485 36.828 136.431 1.00 28.65 O ANISOU 178 OG SER A 108 3206 4020 3662 -232 -430 59 O ATOM 179 N CYS A 109 29.691 39.909 138.768 1.00 33.92 N ANISOU 179 N CYS A 109 3926 4426 4536 -284 -987 -161 N ATOM 180 CA CYS A 109 29.950 40.754 139.931 1.00 37.00 C ANISOU 180 CA CYS A 109 4442 4733 4884 -257 -1210 -248 C ATOM 181 C CYS A 109 30.076 42.226 139.538 1.00 38.70 C ANISOU 181 C CYS A 109 4642 4856 5206 -349 -1203 -291 C ATOM 182 O CYS A 109 29.616 43.108 140.270 1.00 37.56 O ANISOU 182 O CYS A 109 4678 4655 4937 -310 -1294 -350 O ATOM 183 CB CYS A 109 31.211 40.283 140.651 1.00 48.70 C ANISOU 183 CB CYS A 109 5829 6165 6507 -242 -1458 -309 C ATOM 184 SG CYS A 109 31.037 38.637 141.390 1.00 56.42 S ANISOU 184 SG CYS A 109 6897 7214 7327 -110 -1518 -254 S ATOM 185 N LEU A 110 30.696 42.507 138.389 1.00 39.69 N ANISOU 185 N LEU A 110 4568 4955 5556 -468 -1088 -260 N ATOM 186 CA LEU A 110 30.827 43.884 137.921 1.00 43.08 C ANISOU 186 CA LEU A 110 4988 5278 6101 -570 -1060 -275 C ATOM 187 C LEU A 110 29.467 44.479 137.579 1.00 43.18 C ANISOU 187 C LEU A 110 5183 5313 5912 -525 -910 -227 C ATOM 188 O LEU A 110 29.140 45.591 138.008 1.00 42.20 O ANISOU 188 O LEU A 110 5197 5092 5744 -518 -985 -278 O ATOM 189 CB LEU A 110 31.753 43.936 136.707 1.00 36.98 C ANISOU 189 CB LEU A 110 3969 4487 5595 -706 -924 -226 C ATOM 190 CG LEU A 110 33.227 43.657 136.972 1.00 49.82 C ANISOU 190 CG LEU A 110 5363 6065 7500 -770 -1075 -287 C ATOM 191 CD1 LEU A 110 33.945 43.368 135.660 1.00 56.94 C ANISOU 191 CD1 LEU A 110 6019 6999 8618 -872 -857 -221 C ATOM 192 CD2 LEU A 110 33.863 44.835 137.695 1.00 54.21 C ANISOU 192 CD2 LEU A 110 5924 6464 8208 -847 -1301 -384 C ATOM 193 N VAL A 111 28.665 43.753 136.796 1.00 35.06 N ANISOU 193 N VAL A 111 4152 4401 4769 -489 -709 -139 N ATOM 194 CA VAL A 111 27.321 44.215 136.459 1.00 32.30 C ANISOU 194 CA VAL A 111 3948 4084 4239 -432 -581 -95 C ATOM 195 C VAL A 111 26.507 44.445 137.723 1.00 41.60 C ANISOU 195 C VAL A 111 5327 5264 5217 -311 -685 -158 C ATOM 196 O VAL A 111 25.796 45.452 137.845 1.00 35.35 O ANISOU 196 O VAL A 111 4665 4418 4348 -272 -676 -180 O ATOM 197 CB VAL A 111 26.624 43.208 135.519 1.00 38.14 C ANISOU 197 CB VAL A 111 4639 4956 4896 -408 -390 -8 C ATOM 198 CG1 VAL A 111 25.148 43.567 135.340 1.00 38.07 C ANISOU 198 CG1 VAL A 111 4767 4994 4705 -329 -294 25 C ATOM 199 CG2 VAL A 111 27.318 43.174 134.165 1.00 30.27 C ANISOU 199 CG2 VAL A 111 3487 3955 4058 -514 -257 49 C ATOM 200 N PHE A 112 26.625 43.531 138.696 1.00 37.02 N ANISOU 200 N PHE A 112 4783 4738 4545 -243 -782 -186 N ATOM 201 CA PHE A 112 25.862 43.640 139.939 1.00 39.41 C ANISOU 201 CA PHE A 112 5294 5056 4623 -120 -853 -236 C ATOM 202 C PHE A 112 26.248 44.887 140.733 1.00 43.64 C ANISOU 202 C PHE A 112 5951 5458 5172 -111 -1037 -352 C ATOM 203 O PHE A 112 25.380 45.665 141.148 1.00 44.39 O ANISOU 203 O PHE A 112 6212 5530 5123 -30 -1014 -394 O ATOM 204 CB PHE A 112 26.074 42.385 140.786 1.00 36.23 C ANISOU 204 CB PHE A 112 4921 4722 4125 -59 -928 -225 C ATOM 205 CG PHE A 112 25.271 42.358 142.055 1.00 40.31 C ANISOU 205 CG PHE A 112 5667 5270 4377 70 -963 -256 C ATOM 206 CD1 PHE A 112 23.965 41.887 142.053 1.00 35.15 C ANISOU 206 CD1 PHE A 112 5081 4723 3550 138 -771 -187 C ATOM 207 CD2 PHE A 112 25.822 42.791 143.250 1.00 38.66 C ANISOU 207 CD2 PHE A 112 5606 4988 4095 124 -1185 -357 C ATOM 208 CE1 PHE A 112 23.220 41.854 143.218 1.00 34.22 C ANISOU 208 CE1 PHE A 112 5170 4644 3189 256 -763 -206 C ATOM 209 CE2 PHE A 112 25.085 42.757 144.419 1.00 44.66 C ANISOU 209 CE2 PHE A 112 6604 5786 4580 253 -1195 -384 C ATOM 210 CZ PHE A 112 23.781 42.283 144.404 1.00 40.50 C ANISOU 210 CZ PHE A 112 6138 5371 3879 319 -965 -303 C ATOM 211 N VAL A 113 27.549 45.071 140.990 1.00 39.68 N ANISOU 211 N VAL A 113 5365 4862 4851 -187 -1230 -416 N ATOM 212 CA VAL A 113 27.995 46.194 141.809 1.00 34.60 C ANISOU 212 CA VAL A 113 4837 4074 4235 -188 -1445 -545 C ATOM 213 C VAL A 113 27.704 47.509 141.099 1.00 43.28 C ANISOU 213 C VAL A 113 5952 5062 5432 -250 -1369 -550 C ATOM 214 O VAL A 113 27.140 48.446 141.675 1.00 43.99 O ANISOU 214 O VAL A 113 6233 5072 5409 -178 -1425 -631 O ATOM 215 CB VAL A 113 29.495 46.067 142.135 1.00 38.92 C ANISOU 215 CB VAL A 113 5242 4540 5004 -273 -1681 -612 C ATOM 216 CG1 VAL A 113 30.012 47.374 142.781 1.00 43.09 C ANISOU 216 CG1 VAL A 113 5863 4890 5619 -309 -1914 -754 C ATOM 217 CG2 VAL A 113 29.769 44.876 143.047 1.00 38.01 C ANISOU 217 CG2 VAL A 113 5167 4510 4766 -179 -1812 -619 C ATOM 218 N LEU A 114 28.093 47.596 139.832 1.00 40.04 N ANISOU 218 N LEU A 114 5354 4635 5226 -378 -1236 -461 N ATOM 219 CA LEU A 114 27.875 48.814 139.075 1.00 42.58 C ANISOU 219 CA LEU A 114 5699 4836 5645 -446 -1159 -438 C ATOM 220 C LEU A 114 26.390 49.100 138.885 1.00 43.05 C ANISOU 220 C LEU A 114 5917 4951 5490 -322 -1008 -400 C ATOM 221 O LEU A 114 25.971 50.262 138.920 1.00 37.90 O ANISOU 221 O LEU A 114 5394 4174 4833 -298 -1031 -439 O ATOM 222 CB LEU A 114 28.600 48.714 137.736 1.00 45.10 C ANISOU 222 CB LEU A 114 5798 5146 6193 -601 -1020 -331 C ATOM 223 CG LEU A 114 30.122 48.701 137.906 1.00 55.83 C ANISOU 223 CG LEU A 114 6968 6419 7825 -736 -1170 -383 C ATOM 224 CD1 LEU A 114 30.798 48.775 136.552 1.00 61.86 C ANISOU 224 CD1 LEU A 114 7525 7165 8816 -892 -988 -274 C ATOM 225 CD2 LEU A 114 30.581 49.845 138.800 1.00 59.73 C ANISOU 225 CD2 LEU A 114 7558 6723 8414 -771 -1413 -515 C ATOM 226 N GLY A 115 25.573 48.064 138.699 1.00 37.90 N ANISOU 226 N GLY A 115 5251 4473 4678 -240 -863 -329 N ATOM 227 CA GLY A 115 24.157 48.301 138.463 1.00 34.28 C ANISOU 227 CA GLY A 115 4898 4074 4052 -127 -721 -293 C ATOM 228 C GLY A 115 23.429 48.777 139.707 1.00 41.06 C ANISOU 228 C GLY A 115 5962 4914 4724 21 -796 -400 C ATOM 229 O GLY A 115 22.533 49.625 139.632 1.00 35.67 O ANISOU 229 O GLY A 115 5387 4188 3978 107 -743 -419 O ATOM 230 N ILE A 116 23.810 48.251 140.872 1.00 38.55 N ANISOU 230 N ILE A 116 5713 4625 4308 67 -923 -475 N ATOM 231 CA ILE A 116 23.174 48.702 142.106 1.00 42.01 C ANISOU 231 CA ILE A 116 6375 5049 4539 217 -986 -585 C ATOM 232 C ILE A 116 23.582 50.134 142.445 1.00 44.18 C ANISOU 232 C ILE A 116 6773 5121 4893 210 -1152 -712 C ATOM 233 O ILE A 116 22.746 50.945 142.860 1.00 43.69 O ANISOU 233 O ILE A 116 6878 5012 4710 335 -1129 -786 O ATOM 234 CB ILE A 116 23.490 47.721 143.245 1.00 45.54 C ANISOU 234 CB ILE A 116 6894 5579 4830 272 -1081 -617 C ATOM 235 CG1 ILE A 116 22.722 46.424 143.005 1.00 46.19 C ANISOU 235 CG1 ILE A 116 6904 5846 4802 307 -883 -493 C ATOM 236 CG2 ILE A 116 23.117 48.314 144.587 1.00 44.83 C ANISOU 236 CG2 ILE A 116 7066 5447 4520 418 -1181 -753 C ATOM 237 CD1 ILE A 116 22.805 45.462 144.140 1.00 48.93 C ANISOU 237 CD1 ILE A 116 7361 6270 4960 379 -939 -497 C ATOM 238 N ILE A 117 24.859 50.476 142.263 1.00 42.43 N ANISOU 238 N ILE A 117 6462 4766 4893 64 -1319 -744 N ATOM 239 CA ILE A 117 25.301 51.840 142.547 1.00 47.48 C ANISOU 239 CA ILE A 117 7209 5187 5646 31 -1491 -865 C ATOM 240 C ILE A 117 24.652 52.826 141.579 1.00 44.51 C ANISOU 240 C ILE A 117 6845 4714 5352 21 -1356 -808 C ATOM 241 O ILE A 117 24.086 53.843 141.994 1.00 43.28 O ANISOU 241 O ILE A 117 6874 4440 5130 121 -1399 -904 O ATOM 242 CB ILE A 117 26.834 51.935 142.496 1.00 46.46 C ANISOU 242 CB ILE A 117 6935 4937 5781 -146 -1690 -901 C ATOM 243 CG1 ILE A 117 27.460 51.098 143.614 1.00 51.06 C ANISOU 243 CG1 ILE A 117 7545 5587 6268 -103 -1883 -982 C ATOM 244 CG2 ILE A 117 27.277 53.397 142.600 1.00 44.04 C ANISOU 244 CG2 ILE A 117 6715 4376 5643 -217 -1853 -1010 C ATOM 245 CD1 ILE A 117 28.956 50.935 143.490 1.00 48.74 C ANISOU 245 CD1 ILE A 117 7044 5216 6258 -269 -2069 -1002 C ATOM 246 N GLY A 118 24.717 52.533 140.277 1.00 42.37 N ANISOU 246 N GLY A 118 6394 4489 5215 -86 -1195 -653 N ATOM 247 CA GLY A 118 24.177 53.459 139.297 1.00 42.72 C ANISOU 247 CA GLY A 118 6464 4434 5335 -98 -1086 -581 C ATOM 248 C GLY A 118 22.688 53.698 139.466 1.00 42.43 C ANISOU 248 C GLY A 118 6568 4461 5092 102 -978 -594 C ATOM 249 O GLY A 118 22.232 54.838 139.479 1.00 41.02 O ANISOU 249 O GLY A 118 6528 4131 4928 170 -1008 -644 O ATOM 250 N ASN A 119 21.906 52.623 139.585 1.00 43.62 N ANISOU 250 N ASN A 119 6673 4832 5070 198 -847 -549 N ATOM 251 CA ASN A 119 20.462 52.804 139.690 1.00 41.14 C ANISOU 251 CA ASN A 119 6445 4594 4594 381 -725 -556 C ATOM 252 C ASN A 119 20.047 53.372 141.044 1.00 44.90 C ANISOU 252 C ASN A 119 7128 5017 4914 542 -808 -722 C ATOM 253 O ASN A 119 19.056 54.107 141.123 1.00 38.56 O ANISOU 253 O ASN A 119 6427 4177 4047 692 -750 -766 O ATOM 254 CB ASN A 119 19.751 51.483 139.416 1.00 36.44 C ANISOU 254 CB ASN A 119 5722 4235 3888 416 -558 -459 C ATOM 255 CG ASN A 119 19.780 51.115 137.947 1.00 36.48 C ANISOU 255 CG ASN A 119 5564 4287 4008 310 -454 -310 C ATOM 256 OD1 ASN A 119 19.008 51.651 137.151 1.00 35.49 O ANISOU 256 OD1 ASN A 119 5443 4141 3899 363 -383 -255 O ATOM 257 ND2 ASN A 119 20.683 50.211 137.575 1.00 35.39 N ANISOU 257 ND2 ASN A 119 5293 4208 3946 173 -453 -249 N ATOM 258 N SER A 120 20.776 53.044 142.116 1.00 39.28 N ANISOU 258 N SER A 120 6489 4302 4132 529 -946 -820 N ATOM 259 CA SER A 120 20.490 53.674 143.398 1.00 38.67 C ANISOU 259 CA SER A 120 6647 4157 3888 682 -1044 -994 C ATOM 260 C SER A 120 20.795 55.167 143.346 1.00 47.26 C ANISOU 260 C SER A 120 7861 4983 5113 673 -1190 -1100 C ATOM 261 O SER A 120 20.019 55.975 143.857 1.00 49.36 O ANISOU 261 O SER A 120 8304 5179 5273 842 -1180 -1212 O ATOM 262 CB SER A 120 21.280 53.007 144.524 1.00 39.89 C ANISOU 262 CB SER A 120 6875 4354 3926 670 -1195 -1074 C ATOM 263 OG SER A 120 20.953 51.631 144.624 1.00 42.00 O ANISOU 263 OG SER A 120 7053 4843 4064 686 -1057 -968 O ATOM 264 N THR A 121 21.912 55.552 142.720 1.00 43.17 N ANISOU 264 N THR A 121 7251 4309 4844 477 -1316 -1066 N ATOM 265 CA THR A 121 22.252 56.969 142.640 1.00 47.00 C ANISOU 265 CA THR A 121 7854 4517 5489 441 -1458 -1154 C ATOM 266 C THR A 121 21.256 57.719 141.765 1.00 47.53 C ANISOU 266 C THR A 121 7947 4521 5592 524 -1314 -1078 C ATOM 267 O THR A 121 20.878 58.856 142.073 1.00 52.12 O ANISOU 267 O THR A 121 8710 4915 6179 629 -1385 -1190 O ATOM 268 CB THR A 121 23.670 57.143 142.099 1.00 50.47 C ANISOU 268 CB THR A 121 8153 4811 6213 189 -1592 -1110 C ATOM 269 OG1 THR A 121 24.594 56.408 142.910 1.00 49.42 O ANISOU 269 OG1 THR A 121 7974 4741 6061 128 -1749 -1184 O ATOM 270 CG2 THR A 121 24.059 58.608 142.117 1.00 44.10 C ANISOU 270 CG2 THR A 121 7477 3691 5587 134 -1752 -1206 C ATOM 271 N LEU A 122 20.825 57.093 140.667 1.00 46.57 N ANISOU 271 N LEU A 122 7654 4546 5495 487 -1127 -896 N ATOM 272 CA LEU A 122 19.798 57.677 139.812 1.00 45.57 C ANISOU 272 CA LEU A 122 7545 4387 5381 587 -1003 -813 C ATOM 273 C LEU A 122 18.532 57.980 140.607 1.00 47.78 C ANISOU 273 C LEU A 122 7967 4717 5471 849 -949 -933 C ATOM 274 O LEU A 122 17.991 59.091 140.542 1.00 44.06 O ANISOU 274 O LEU A 122 7629 4075 5036 967 -978 -989 O ATOM 275 CB LEU A 122 19.504 56.724 138.642 1.00 37.89 C ANISOU 275 CB LEU A 122 6371 3608 4418 522 -829 -619 C ATOM 276 CG LEU A 122 18.459 57.173 137.613 1.00 40.42 C ANISOU 276 CG LEU A 122 6688 3922 4749 619 -718 -513 C ATOM 277 CD1 LEU A 122 18.728 58.599 137.177 1.00 44.33 C ANISOU 277 CD1 LEU A 122 7320 4125 5400 589 -814 -509 C ATOM 278 CD2 LEU A 122 18.450 56.236 136.401 1.00 34.28 C ANISOU 278 CD2 LEU A 122 5725 3308 3991 516 -589 -332 C ATOM 279 N LEU A 123 18.045 56.999 141.370 1.00 48.45 N ANISOU 279 N LEU A 123 8025 5028 5356 947 -860 -969 N ATOM 280 CA LEU A 123 16.860 57.215 142.196 1.00 47.71 C ANISOU 280 CA LEU A 123 8051 5003 5076 1195 -772 -1083 C ATOM 281 C LEU A 123 17.084 58.330 143.209 1.00 53.88 C ANISOU 281 C LEU A 123 9086 5572 5815 1297 -932 -1292 C ATOM 282 O LEU A 123 16.226 59.203 143.387 1.00 56.25 O ANISOU 282 O LEU A 123 9506 5783 6083 1488 -899 -1382 O ATOM 283 CB LEU A 123 16.468 55.916 142.901 1.00 48.03 C ANISOU 283 CB LEU A 123 8029 5309 4913 1247 -642 -1072 C ATOM 284 CG LEU A 123 15.769 54.880 142.024 1.00 48.75 C ANISOU 284 CG LEU A 123 7890 5617 5015 1219 -452 -899 C ATOM 285 CD1 LEU A 123 15.832 53.494 142.678 1.00 46.91 C ANISOU 285 CD1 LEU A 123 7596 5597 4629 1188 -370 -866 C ATOM 286 CD2 LEU A 123 14.325 55.282 141.762 1.00 40.61 C ANISOU 286 CD2 LEU A 123 6830 4640 3961 1414 -305 -899 C ATOM 287 N TYR A 124 18.235 58.322 143.888 1.00 52.68 N ANISOU 287 N TYR A 124 9018 5329 5670 1181 -1121 -1384 N ATOM 288 CA TYR A 124 18.494 59.359 144.886 1.00 54.26 C ANISOU 288 CA TYR A 124 9475 5317 5824 1273 -1304 -1604 C ATOM 289 C TYR A 124 18.532 60.745 144.246 1.00 55.27 C ANISOU 289 C TYR A 124 9681 5151 6167 1259 -1396 -1627 C ATOM 290 O TYR A 124 18.061 61.728 144.836 1.00 63.27 O ANISOU 290 O TYR A 124 10907 6006 7125 1434 -1454 -1796 O ATOM 291 CB TYR A 124 19.801 59.065 145.627 1.00 51.21 C ANISOU 291 CB TYR A 124 9140 4879 5439 1130 -1529 -1692 C ATOM 292 CG TYR A 124 20.240 60.204 146.516 1.00 59.55 C ANISOU 292 CG TYR A 124 10456 5676 6494 1184 -1772 -1925 C ATOM 293 CD1 TYR A 124 19.740 60.343 147.803 1.00 64.64 C ANISOU 293 CD1 TYR A 124 11351 6355 6856 1404 -1795 -2122 C ATOM 294 CD2 TYR A 124 21.145 61.155 146.060 1.00 65.57 C ANISOU 294 CD2 TYR A 124 11223 6151 7539 1012 -1971 -1952 C ATOM 295 CE1 TYR A 124 20.137 61.402 148.616 1.00 73.13 C ANISOU 295 CE1 TYR A 124 12600 7234 7951 1434 -1992 -2286 C ATOM 296 CE2 TYR A 124 21.546 62.211 146.861 1.00 75.19 C ANISOU 296 CE2 TYR A 124 12683 7109 8778 1051 -2214 -2179 C ATOM 297 CZ TYR A 124 21.041 62.332 148.134 1.00 77.87 C ANISOU 297 CZ TYR A 124 13185 7553 8851 1255 -2203 -2310 C ATOM 298 OH TYR A 124 21.450 63.388 148.922 1.00 86.61 O ANISOU 298 OH TYR A 124 14428 8481 9998 1268 -2390 -2451 O ATOM 299 N ILE A 125 19.093 60.843 143.040 1.00 53.51 N ANISOU 299 N ILE A 125 9303 4845 6185 1057 -1404 -1458 N ATOM 300 CA ILE A 125 19.095 62.107 142.312 1.00 57.97 C ANISOU 300 CA ILE A 125 9943 5127 6955 1032 -1467 -1436 C ATOM 301 C ILE A 125 17.672 62.601 142.096 1.00 61.11 C ANISOU 301 C ILE A 125 10408 5539 7271 1285 -1330 -1439 C ATOM 302 O ILE A 125 17.379 63.792 142.262 1.00 60.59 O ANISOU 302 O ILE A 125 10528 5228 7264 1403 -1416 -1549 O ATOM 303 CB ILE A 125 19.828 61.942 140.970 1.00 64.12 C ANISOU 303 CB ILE A 125 10533 5866 7962 780 -1436 -1214 C ATOM 304 CG1 ILE A 125 21.341 61.903 141.178 1.00 61.33 C ANISOU 304 CG1 ILE A 125 10130 5395 7777 529 -1611 -1244 C ATOM 305 CG2 ILE A 125 19.430 63.056 140.014 1.00 71.02 C ANISOU 305 CG2 ILE A 125 11480 6513 8990 801 -1421 -1125 C ATOM 306 CD1 ILE A 125 22.074 61.297 139.996 1.00 51.97 C ANISOU 306 CD1 ILE A 125 8708 4278 6759 292 -1519 -1025 C ATOM 307 N ILE A 126 16.771 61.697 141.705 1.00 59.93 N ANISOU 307 N ILE A 126 10098 5665 7008 1373 -1124 -1323 N ATOM 308 CA ILE A 126 15.415 62.101 141.350 1.00 59.41 C ANISOU 308 CA ILE A 126 10037 5629 6907 1603 -997 -1306 C ATOM 309 C ILE A 126 14.618 62.455 142.598 1.00 59.64 C ANISOU 309 C ILE A 126 10232 5674 6753 1871 -968 -1525 C ATOM 310 O ILE A 126 13.820 63.401 142.595 1.00 62.10 O ANISOU 310 O ILE A 126 10653 5851 7092 2076 -962 -1603 O ATOM 311 CB ILE A 126 14.734 60.994 140.519 1.00 54.27 C ANISOU 311 CB ILE A 126 9140 5262 6217 1593 -806 -1120 C ATOM 312 CG1 ILE A 126 15.413 60.853 139.152 1.00 48.85 C ANISOU 312 CG1 ILE A 126 8331 4528 5703 1366 -826 -911 C ATOM 313 CG2 ILE A 126 13.245 61.275 140.341 1.00 53.71 C ANISOU 313 CG2 ILE A 126 9041 5264 6103 1854 -681 -1130 C ATOM 314 CD1 ILE A 126 15.060 59.533 138.399 1.00 39.96 C ANISOU 314 CD1 ILE A 126 6967 3691 4526 1303 -671 -745 C ATOM 315 N TYR A 127 14.828 61.722 143.691 1.00 55.99 N ANISOU 315 N TYR A 127 9807 5371 6095 1887 -948 -1628 N ATOM 316 CA TYR A 127 14.092 62.031 144.911 1.00 65.81 C ANISOU 316 CA TYR A 127 11233 6643 7130 2148 -895 -1837 C ATOM 317 C TYR A 127 14.621 63.290 145.598 1.00 69.49 C ANISOU 317 C TYR A 127 11985 6794 7624 2202 -1115 -2055 C ATOM 318 O TYR A 127 13.835 64.081 146.134 1.00 68.68 O ANISOU 318 O TYR A 127 12005 6633 7458 2423 -1073 -2184 O ATOM 319 CB TYR A 127 14.135 60.841 145.871 1.00 69.35 C ANISOU 319 CB TYR A 127 11664 7356 7330 2152 -797 -1864 C ATOM 320 CG TYR A 127 13.779 61.215 147.295 1.00 81.91 C ANISOU 320 CG TYR A 127 13504 8941 8677 2372 -788 -2094 C ATOM 321 CD1 TYR A 127 12.455 61.410 147.675 1.00 86.29 C ANISOU 321 CD1 TYR A 127 14020 9628 9139 2598 -568 -2117 C ATOM 322 CD2 TYR A 127 14.769 61.383 148.258 1.00 84.56 C ANISOU 322 CD2 TYR A 127 13992 9197 8940 2275 -985 -2194 C ATOM 323 CE1 TYR A 127 12.128 61.762 148.978 1.00 91.85 C ANISOU 323 CE1 TYR A 127 14857 10375 9666 2722 -527 -2239 C ATOM 324 CE2 TYR A 127 14.451 61.735 149.562 1.00 87.72 C ANISOU 324 CE2 TYR A 127 14536 9642 9153 2410 -962 -2315 C ATOM 325 CZ TYR A 127 13.131 61.920 149.916 1.00 92.95 C ANISOU 325 CZ TYR A 127 15179 10429 9710 2632 -724 -2337 C ATOM 326 OH TYR A 127 12.818 62.266 151.212 1.00100.80 O ANISOU 326 OH TYR A 127 16327 11460 10511 2764 -688 -2460 O ATOM 327 N LYS A 128 15.941 63.504 145.586 1.00 70.84 N ANISOU 327 N LYS A 128 12211 6786 7921 1972 -1342 -2069 N ATOM 328 CA LYS A 128 16.508 64.613 146.351 1.00 72.68 C ANISOU 328 CA LYS A 128 12659 6764 8193 1973 -1558 -2251 C ATOM 329 C LYS A 128 16.206 65.969 145.723 1.00 74.94 C ANISOU 329 C LYS A 128 13013 6771 8691 2020 -1614 -2248 C ATOM 330 O LYS A 128 16.111 66.970 146.440 1.00 72.67 O ANISOU 330 O LYS A 128 12869 6350 8392 2109 -1700 -2385 O ATOM 331 CB LYS A 128 18.020 64.441 146.502 1.00 77.01 C ANISOU 331 CB LYS A 128 13202 7205 8852 1700 -1793 -2261 C ATOM 332 N ASN A 129 16.055 66.036 144.404 1.00 72.05 N ANISOU 332 N ASN A 129 12560 6305 8511 1966 -1572 -2088 N ATOM 333 CA ASN A 129 15.951 67.313 143.702 1.00 76.98 C ANISOU 333 CA ASN A 129 13253 6637 9359 1965 -1649 -2043 C ATOM 334 C ASN A 129 14.514 67.530 143.236 1.00 71.02 C ANISOU 334 C ASN A 129 12459 5958 8567 2232 -1474 -1994 C ATOM 335 O ASN A 129 14.035 66.837 142.330 1.00 69.84 O ANISOU 335 O ASN A 129 12130 5974 8430 2232 -1333 -1814 O ATOM 336 CB ASN A 129 16.926 67.362 142.527 1.00 78.18 C ANISOU 336 CB ASN A 129 13322 6613 9768 1675 -1735 -1851 C ATOM 337 CG ASN A 129 18.370 67.144 142.954 1.00 80.00 C ANISOU 337 CG ASN A 129 13546 6768 10081 1404 -1914 -1902 C ATOM 338 OD1 ASN A 129 18.873 66.018 142.942 1.00 80.01 O ANISOU 338 OD1 ASN A 129 13363 7013 10023 1260 -1859 -1816 O ATOM 339 ND2 ASN A 129 19.044 68.226 143.334 1.00 78.43 N ANISOU 339 ND2 ASN A 129 13451 6319 10028 1305 -2094 -1992 N ATOM 340 N LYS A 130 13.830 68.500 143.853 1.00 72.25 N ANISOU 340 N LYS A 130 12721 6043 8689 2427 -1474 -2124 N ATOM 341 CA LYS A 130 12.497 68.881 143.389 1.00 73.63 C ANISOU 341 CA LYS A 130 12841 6258 8878 2675 -1337 -2082 C ATOM 342 C LYS A 130 12.510 69.314 141.926 1.00 78.98 C ANISOU 342 C LYS A 130 13483 6742 9783 2603 -1386 -1879 C ATOM 343 O LYS A 130 11.493 69.194 141.234 1.00 80.84 O ANISOU 343 O LYS A 130 13609 7074 10033 2770 -1272 -1779 O ATOM 344 CB LYS A 130 11.931 69.998 144.271 1.00 74.32 C ANISOU 344 CB LYS A 130 13066 6243 8929 2869 -1361 -2262 C ATOM 345 N CYS A 131 13.651 69.806 141.437 1.00 76.27 N ANISOU 345 N CYS A 131 13221 6137 9622 2348 -1551 -1803 N ATOM 346 CA CYS A 131 13.806 70.144 140.028 1.00 75.98 C ANISOU 346 CA CYS A 131 13164 5921 9783 2236 -1581 -1572 C ATOM 347 C CYS A 131 13.882 68.920 139.121 1.00 70.06 C ANISOU 347 C CYS A 131 12218 5399 9003 2118 -1465 -1363 C ATOM 348 O CYS A 131 13.798 69.079 137.900 1.00 67.11 O ANISOU 348 O CYS A 131 11794 4966 8740 2048 -1447 -1141 O ATOM 349 CB CYS A 131 15.064 70.991 139.828 1.00 88.82 C ANISOU 349 CB CYS A 131 14900 7231 11617 1957 -1753 -1534 C ATOM 350 SG CYS A 131 16.278 70.804 141.161 1.00106.30 S ANISOU 350 SG CYS A 131 17158 9446 13787 1774 -1888 -1745 S ATOM 351 N MET A 132 14.062 67.720 139.672 1.00 71.02 N ANISOU 351 N MET A 132 12182 5838 8965 2051 -1368 -1394 N ATOM 352 CA MET A 132 14.140 66.507 138.867 1.00 75.27 C ANISOU 352 CA MET A 132 12466 6670 9464 1897 -1234 -1182 C ATOM 353 C MET A 132 12.859 65.689 138.906 1.00 77.24 C ANISOU 353 C MET A 132 12545 7245 9557 2112 -1053 -1172 C ATOM 354 O MET A 132 12.853 64.558 138.421 1.00 83.12 O ANISOU 354 O MET A 132 13080 8255 10246 2001 -941 -1034 O ATOM 355 CB MET A 132 15.310 65.626 139.319 1.00 74.83 C ANISOU 355 CB MET A 132 12325 6735 9372 1644 -1255 -1192 C ATOM 356 CG MET A 132 16.677 66.282 139.248 1.00 87.11 C ANISOU 356 CG MET A 132 13982 7998 11117 1390 -1429 -1192 C ATOM 357 SD MET A 132 17.377 66.382 137.594 1.00 92.97 S ANISOU 357 SD MET A 132 14623 8632 12071 1119 -1400 -889 S ATOM 358 CE MET A 132 17.450 64.659 137.193 1.00 90.24 C ANISOU 358 CE MET A 132 13987 8709 11591 1011 -1225 -751 C ATOM 359 N ARG A 133 11.782 66.216 139.476 1.00 81.18 N ANISOU 359 N ARG A 133 13120 7728 9998 2413 -1018 -1322 N ATOM 360 CA ARG A 133 10.551 65.450 139.650 1.00 86.92 C ANISOU 360 CA ARG A 133 13662 8766 10598 2617 -832 -1333 C ATOM 361 C ARG A 133 9.515 65.958 138.651 1.00 87.31 C ANISOU 361 C ARG A 133 13648 8768 10758 2795 -824 -1227 C ATOM 362 O ARG A 133 8.683 66.808 138.969 1.00 91.55 O ANISOU 362 O ARG A 133 14277 9184 11324 3068 -836 -1353 O ATOM 363 CB ARG A 133 10.044 65.544 141.082 1.00 95.50 C ANISOU 363 CB ARG A 133 14846 9914 11524 2840 -761 -1583 C ATOM 364 CG ARG A 133 9.454 64.241 141.603 1.00 98.35 C ANISOU 364 CG ARG A 133 15005 10654 11708 2881 -549 -1582 C ATOM 365 CD ARG A 133 10.124 63.845 142.898 1.00 96.65 C ANISOU 365 CD ARG A 133 14920 10496 11306 2827 -547 -1735 C ATOM 366 NE ARG A 133 10.508 65.030 143.656 1.00 97.39 N ANISOU 366 NE ARG A 133 15310 10297 11397 2925 -703 -1946 N ATOM 367 CZ ARG A 133 10.936 65.010 144.912 1.00103.20 C ANISOU 367 CZ ARG A 133 16172 11072 11969 2901 -729 -2091 C ATOM 368 NH1 ARG A 133 11.264 66.146 145.517 1.00110.06 N ANISOU 368 NH1 ARG A 133 17231 11718 12870 2919 -878 -2226 N ATOM 369 NH2 ARG A 133 11.029 63.860 145.567 1.00 98.83 N ANISOU 369 NH2 ARG A 133 15556 10777 11216 2859 -612 -2092 N ATOM 370 N ASN A 134 9.574 65.420 137.436 1.00 82.62 N ANISOU 370 N ASN A 134 12901 8270 10221 2651 -812 -1001 N ATOM 371 CA ASN A 134 8.600 65.731 136.399 1.00 75.55 C ANISOU 371 CA ASN A 134 11929 7367 9410 2808 -823 -880 C ATOM 372 C ASN A 134 8.049 64.433 135.814 1.00 65.09 C ANISOU 372 C ASN A 134 10319 6389 8025 2763 -700 -752 C ATOM 373 O ASN A 134 8.336 63.349 136.332 1.00 56.01 O ANISOU 373 O ASN A 134 9042 5471 6769 2637 -589 -774 O ATOM 374 CB ASN A 134 9.234 66.612 135.314 1.00 71.94 C ANISOU 374 CB ASN A 134 11638 6607 9090 2686 -977 -716 C ATOM 375 CG ASN A 134 10.521 66.014 134.741 1.00 73.65 C ANISOU 375 CG ASN A 134 11830 6843 9309 2332 -980 -557 C ATOM 376 OD1 ASN A 134 10.718 64.801 134.753 1.00 68.85 O ANISOU 376 OD1 ASN A 134 11035 6514 8609 2200 -875 -515 O ATOM 377 ND2 ASN A 134 11.399 66.873 134.235 1.00 76.78 N ANISOU 377 ND2 ASN A 134 12413 6933 9825 2180 -1093 -467 N ATOM 378 N GLY A 135 7.265 64.539 134.741 1.00 64.66 N ANISOU 378 N GLY A 135 10174 6355 8039 2867 -737 -622 N ATOM 379 CA GLY A 135 6.725 63.398 134.039 1.00 59.21 C ANISOU 379 CA GLY A 135 9227 5958 7313 2822 -661 -502 C ATOM 380 C GLY A 135 7.761 62.358 133.653 1.00 61.15 C ANISOU 380 C GLY A 135 9411 6332 7492 2506 -620 -380 C ATOM 381 O GLY A 135 7.729 61.218 134.128 1.00 55.02 O ANISOU 381 O GLY A 135 8463 5808 6633 2429 -496 -412 O ATOM 382 N PRO A 136 8.711 62.729 132.787 1.00 62.93 N ANISOU 382 N PRO A 136 9776 6377 7757 2319 -712 -234 N ATOM 383 CA PRO A 136 9.676 61.722 132.301 1.00 57.21 C ANISOU 383 CA PRO A 136 8974 5782 6981 2034 -661 -114 C ATOM 384 C PRO A 136 10.591 61.166 133.379 1.00 49.09 C ANISOU 384 C PRO A 136 7936 4815 5903 1876 -596 -221 C ATOM 385 O PRO A 136 10.931 59.980 133.330 1.00 47.48 O ANISOU 385 O PRO A 136 7581 4824 5634 1727 -513 -178 O ATOM 386 CB PRO A 136 10.468 62.490 131.233 1.00 54.39 C ANISOU 386 CB PRO A 136 8799 5177 6691 1898 -756 53 C ATOM 387 CG PRO A 136 10.352 63.907 131.650 1.00 53.45 C ANISOU 387 CG PRO A 136 8893 4752 6664 2043 -860 -27 C ATOM 388 CD PRO A 136 8.945 64.045 132.171 1.00 54.28 C ANISOU 388 CD PRO A 136 8912 4951 6759 2357 -851 -160 C ATOM 389 N ASN A 137 11.010 61.980 134.355 1.00 45.61 N ANISOU 389 N ASN A 137 7662 4181 5488 1911 -649 -364 N ATOM 390 CA ASN A 137 11.978 61.481 135.326 1.00 47.68 C ANISOU 390 CA ASN A 137 7933 4484 5698 1755 -629 -460 C ATOM 391 C ASN A 137 11.330 60.541 136.331 1.00 41.59 C ANISOU 391 C ASN A 137 7031 3980 4793 1861 -505 -578 C ATOM 392 O ASN A 137 12.013 59.703 136.925 1.00 40.26 O ANISOU 392 O ASN A 137 6816 3931 4551 1721 -466 -606 O ATOM 393 CB ASN A 137 12.663 62.645 136.045 1.00 51.22 C ANISOU 393 CB ASN A 137 8613 4632 6214 1751 -754 -587 C ATOM 394 CG ASN A 137 13.690 63.354 135.172 1.00 61.94 C ANISOU 394 CG ASN A 137 10084 5729 7721 1547 -855 -454 C ATOM 395 OD1 ASN A 137 13.937 62.961 134.032 1.00 61.65 O ANISOU 395 OD1 ASN A 137 9965 5747 7712 1411 -816 -263 O ATOM 396 ND2 ASN A 137 14.282 64.421 135.705 1.00 67.44 N ANISOU 396 ND2 ASN A 137 10978 6132 8513 1525 -980 -558 N ATOM 397 N ILE A 138 10.022 60.667 136.544 1.00 43.86 N ANISOU 397 N ILE A 138 7255 4358 5053 2109 -437 -642 N ATOM 398 CA ILE A 138 9.315 59.693 137.365 1.00 42.03 C ANISOU 398 CA ILE A 138 6870 4397 4703 2196 -279 -719 C ATOM 399 C ILE A 138 9.195 58.372 136.618 1.00 43.72 C ANISOU 399 C ILE A 138 6853 4855 4904 2056 -198 -571 C ATOM 400 O ILE A 138 9.293 57.293 137.216 1.00 46.04 O ANISOU 400 O ILE A 138 7046 5344 5104 1980 -91 -586 O ATOM 401 CB ILE A 138 7.941 60.248 137.785 1.00 53.27 C ANISOU 401 CB ILE A 138 8265 5845 6133 2503 -211 -832 C ATOM 402 CG1 ILE A 138 8.126 61.365 138.813 1.00 69.52 C ANISOU 402 CG1 ILE A 138 10569 7686 8161 2646 -267 -1022 C ATOM 403 CG2 ILE A 138 7.080 59.162 138.369 1.00 50.35 C ANISOU 403 CG2 ILE A 138 7684 5773 5672 2573 -15 -864 C ATOM 404 CD1 ILE A 138 8.939 60.922 140.027 1.00 75.77 C ANISOU 404 CD1 ILE A 138 11468 8521 8801 2546 -237 -1136 C ATOM 405 N LEU A 139 8.996 58.434 135.296 1.00 41.63 N ANISOU 405 N LEU A 139 6522 4570 4725 2021 -257 -425 N ATOM 406 CA LEU A 139 9.056 57.226 134.481 1.00 40.83 C ANISOU 406 CA LEU A 139 6240 4666 4609 1867 -210 -292 C ATOM 407 C LEU A 139 10.453 56.619 134.507 1.00 40.96 C ANISOU 407 C LEU A 139 6294 4675 4592 1608 -217 -243 C ATOM 408 O LEU A 139 10.602 55.388 134.530 1.00 35.44 O ANISOU 408 O LEU A 139 5454 4169 3843 1493 -137 -206 O ATOM 409 CB LEU A 139 8.631 57.535 133.046 1.00 37.57 C ANISOU 409 CB LEU A 139 5800 4208 4268 1895 -297 -156 C ATOM 410 CG LEU A 139 7.174 57.936 132.815 1.00 47.78 C ANISOU 410 CG LEU A 139 6995 5542 5617 2151 -313 -185 C ATOM 411 CD1 LEU A 139 6.960 58.286 131.353 1.00 39.75 C ANISOU 411 CD1 LEU A 139 6003 4451 4647 2163 -441 -38 C ATOM 412 CD2 LEU A 139 6.229 56.824 133.234 1.00 44.65 C ANISOU 412 CD2 LEU A 139 6340 5423 5203 2204 -181 -232 C ATOM 413 N ILE A 140 11.487 57.465 134.493 1.00 36.11 N ANISOU 413 N ILE A 140 5860 3832 4027 1513 -315 -243 N ATOM 414 CA ILE A 140 12.858 56.969 134.618 1.00 41.08 C ANISOU 414 CA ILE A 140 6506 4446 4658 1277 -330 -215 C ATOM 415 C ILE A 140 13.073 56.346 135.991 1.00 39.97 C ANISOU 415 C ILE A 140 6354 4412 4422 1279 -284 -345 C ATOM 416 O ILE A 140 13.780 55.341 136.130 1.00 41.15 O ANISOU 416 O ILE A 140 6421 4675 4538 1125 -254 -314 O ATOM 417 CB ILE A 140 13.863 58.105 134.339 1.00 42.76 C ANISOU 417 CB ILE A 140 6895 4372 4979 1174 -446 -193 C ATOM 418 CG1 ILE A 140 13.971 58.362 132.838 1.00 41.72 C ANISOU 418 CG1 ILE A 140 6770 4170 4912 1097 -459 -11 C ATOM 419 CG2 ILE A 140 15.241 57.802 134.927 1.00 38.93 C ANISOU 419 CG2 ILE A 140 6428 3844 4520 973 -484 -234 C ATOM 420 CD1 ILE A 140 14.465 59.749 132.512 1.00 40.09 C ANISOU 420 CD1 ILE A 140 6761 3652 4820 1070 -560 23 C ATOM 421 N ALA A 141 12.464 56.933 137.027 1.00 39.48 N ANISOU 421 N ALA A 141 6388 4310 4303 1466 -279 -493 N ATOM 422 CA ALA A 141 12.503 56.329 138.354 1.00 36.07 C ANISOU 422 CA ALA A 141 5973 3997 3736 1500 -219 -610 C ATOM 423 C ALA A 141 11.886 54.936 138.346 1.00 39.16 C ANISOU 423 C ALA A 141 6164 4664 4051 1487 -67 -545 C ATOM 424 O ALA A 141 12.392 54.023 139.008 1.00 38.46 O ANISOU 424 O ALA A 141 6056 4683 3873 1396 -31 -555 O ATOM 425 CB ALA A 141 11.777 57.217 139.367 1.00 38.36 C ANISOU 425 CB ALA A 141 6406 4211 3958 1735 -207 -780 C ATOM 426 N SER A 142 10.774 54.758 137.628 1.00 35.95 N ANISOU 426 N SER A 142 5608 4364 3687 1581 11 -480 N ATOM 427 CA SER A 142 10.179 53.429 137.527 1.00 37.94 C ANISOU 427 CA SER A 142 5655 4858 3902 1546 143 -415 C ATOM 428 C SER A 142 11.129 52.457 136.823 1.00 35.12 C ANISOU 428 C SER A 142 5225 4552 3568 1314 112 -299 C ATOM 429 O SER A 142 11.308 51.323 137.267 1.00 35.60 O ANISOU 429 O SER A 142 5209 4752 3564 1231 187 -281 O ATOM 430 CB SER A 142 8.834 53.512 136.799 1.00 33.89 C ANISOU 430 CB SER A 142 4982 4429 3465 1685 192 -378 C ATOM 431 OG SER A 142 8.327 52.207 136.525 1.00 40.45 O ANISOU 431 OG SER A 142 5601 5473 4297 1614 294 -305 O ATOM 432 N LEU A 143 11.757 52.899 135.734 1.00 34.47 N ANISOU 432 N LEU A 143 5175 4347 3575 1215 11 -216 N ATOM 433 CA LEU A 143 12.771 52.102 135.052 1.00 33.57 C ANISOU 433 CA LEU A 143 5006 4262 3487 1006 -9 -119 C ATOM 434 C LEU A 143 13.923 51.736 135.982 1.00 38.79 C ANISOU 434 C LEU A 143 5730 4898 4110 893 -36 -173 C ATOM 435 O LEU A 143 14.387 50.589 135.984 1.00 33.26 O ANISOU 435 O LEU A 143 4937 4312 3389 777 3 -130 O ATOM 436 CB LEU A 143 13.288 52.874 133.835 1.00 31.21 C ANISOU 436 CB LEU A 143 4772 3810 3277 935 -93 -28 C ATOM 437 CG LEU A 143 14.360 52.217 132.955 1.00 33.45 C ANISOU 437 CG LEU A 143 5006 4107 3595 730 -92 76 C ATOM 438 CD1 LEU A 143 13.880 50.894 132.335 1.00 33.71 C ANISOU 438 CD1 LEU A 143 4873 4345 3588 695 -16 138 C ATOM 439 CD2 LEU A 143 14.782 53.174 131.870 1.00 30.52 C ANISOU 439 CD2 LEU A 143 4735 3566 3294 681 -148 169 C ATOM 440 N ALA A 144 14.409 52.702 136.770 1.00 33.46 N ANISOU 440 N ALA A 144 5218 4062 3434 930 -121 -272 N ATOM 441 CA ALA A 144 15.539 52.444 137.662 1.00 35.84 C ANISOU 441 CA ALA A 144 5587 4323 3708 830 -191 -335 C ATOM 442 C ALA A 144 15.176 51.432 138.746 1.00 39.47 C ANISOU 442 C ALA A 144 6024 4954 4018 885 -110 -383 C ATOM 443 O ALA A 144 16.001 50.589 139.118 1.00 41.70 O ANISOU 443 O ALA A 144 6283 5285 4276 776 -138 -370 O ATOM 444 CB ALA A 144 16.020 53.756 138.294 1.00 35.47 C ANISOU 444 CB ALA A 144 5732 4054 3692 871 -323 -452 C ATOM 445 N LEU A 145 13.958 51.520 139.285 1.00 40.85 N ANISOU 445 N LEU A 145 6208 5213 4098 1060 -4 -434 N ATOM 446 CA LEU A 145 13.507 50.537 140.261 1.00 41.63 C ANISOU 446 CA LEU A 145 6287 5480 4050 1109 114 -453 C ATOM 447 C LEU A 145 13.403 49.158 139.634 1.00 42.33 C ANISOU 447 C LEU A 145 6186 5727 4169 992 200 -326 C ATOM 448 O LEU A 145 13.781 48.159 140.254 1.00 37.65 O ANISOU 448 O LEU A 145 5592 5217 3496 930 229 -306 O ATOM 449 CB LEU A 145 12.165 50.958 140.847 1.00 40.93 C ANISOU 449 CB LEU A 145 6218 5454 3881 1319 246 -524 C ATOM 450 CG LEU A 145 12.257 51.971 141.971 1.00 52.68 C ANISOU 450 CG LEU A 145 7934 6824 5259 1460 195 -683 C ATOM 451 CD1 LEU A 145 10.889 52.553 142.249 1.00 56.41 C ANISOU 451 CD1 LEU A 145 8394 7339 5698 1683 333 -752 C ATOM 452 CD2 LEU A 145 12.819 51.296 143.213 1.00 53.85 C ANISOU 452 CD2 LEU A 145 8208 7030 5223 1439 196 -730 C ATOM 453 N GLY A 146 12.896 49.090 138.397 1.00 35.68 N ANISOU 453 N GLY A 146 5200 4918 3440 966 227 -243 N ATOM 454 CA GLY A 146 12.879 47.827 137.681 1.00 37.71 C ANISOU 454 CA GLY A 146 5291 5299 3736 847 281 -138 C ATOM 455 C GLY A 146 14.270 47.266 137.458 1.00 36.11 C ANISOU 455 C GLY A 146 5100 5053 3567 678 196 -99 C ATOM 456 O GLY A 146 14.486 46.062 137.606 1.00 35.16 O ANISOU 456 O GLY A 146 4908 5027 3423 601 239 -54 O ATOM 457 N ASP A 147 15.230 48.136 137.102 1.00 33.56 N ANISOU 457 N ASP A 147 4857 4577 3316 620 78 -114 N ATOM 458 CA ASP A 147 16.634 47.739 136.967 1.00 36.57 C ANISOU 458 CA ASP A 147 5232 4906 3759 467 -3 -92 C ATOM 459 C ASP A 147 17.148 47.089 138.247 1.00 38.18 C ANISOU 459 C ASP A 147 5493 5142 3871 464 -36 -146 C ATOM 460 O ASP A 147 17.806 46.044 138.208 1.00 35.81 O ANISOU 460 O ASP A 147 5121 4896 3590 369 -43 -103 O ATOM 461 CB ASP A 147 17.521 48.956 136.658 1.00 37.20 C ANISOU 461 CB ASP A 147 5398 4796 3942 413 -118 -117 C ATOM 462 CG ASP A 147 17.310 49.556 135.260 1.00 42.38 C ANISOU 462 CG ASP A 147 6022 5395 4687 385 -96 -33 C ATOM 463 OD1 ASP A 147 16.652 48.945 134.386 1.00 35.82 O ANISOU 463 OD1 ASP A 147 5091 4676 3843 390 -15 43 O ATOM 464 OD2 ASP A 147 17.839 50.679 135.038 1.00 41.53 O ANISOU 464 OD2 ASP A 147 6004 5113 4662 355 -171 -42 O ATOM 465 N LEU A 148 16.906 47.739 139.389 1.00 35.19 N ANISOU 465 N LEU A 148 5264 4718 3387 577 -70 -246 N ATOM 466 CA LEU A 148 17.385 47.228 140.669 1.00 38.00 C ANISOU 466 CA LEU A 148 5723 5097 3619 594 -122 -301 C ATOM 467 C LEU A 148 16.716 45.910 141.018 1.00 40.20 C ANISOU 467 C LEU A 148 5940 5543 3792 613 18 -232 C ATOM 468 O LEU A 148 17.378 44.978 141.488 1.00 36.12 O ANISOU 468 O LEU A 148 5432 5058 3236 555 -24 -205 O ATOM 469 CB LEU A 148 17.137 48.251 141.780 1.00 39.22 C ANISOU 469 CB LEU A 148 6080 5172 3651 732 -175 -434 C ATOM 470 CG LEU A 148 18.116 49.411 141.921 1.00 47.61 C ANISOU 470 CG LEU A 148 7256 6035 4798 697 -371 -532 C ATOM 471 CD1 LEU A 148 17.597 50.424 142.932 1.00 47.00 C ANISOU 471 CD1 LEU A 148 7389 5883 4587 864 -401 -676 C ATOM 472 CD2 LEU A 148 19.486 48.894 142.338 1.00 41.07 C ANISOU 472 CD2 LEU A 148 6432 5167 4006 580 -534 -548 C ATOM 473 N LEU A 149 15.400 45.825 140.812 1.00 37.82 N ANISOU 473 N LEU A 149 5571 5339 3458 695 179 -202 N ATOM 474 CA LEU A 149 14.683 44.582 141.064 1.00 35.66 C ANISOU 474 CA LEU A 149 5216 5213 3119 692 328 -126 C ATOM 475 C LEU A 149 15.252 43.459 140.213 1.00 32.58 C ANISOU 475 C LEU A 149 4686 4854 2838 544 308 -32 C ATOM 476 O LEU A 149 15.533 42.362 140.707 1.00 33.08 O ANISOU 476 O LEU A 149 4755 4965 2848 498 327 17 O ATOM 477 CB LEU A 149 13.199 44.772 140.755 1.00 41.82 C ANISOU 477 CB LEU A 149 5893 6083 3914 787 488 -114 C ATOM 478 CG LEU A 149 12.246 43.758 141.375 1.00 55.01 C ANISOU 478 CG LEU A 149 7504 7894 5502 813 675 -59 C ATOM 479 CD1 LEU A 149 12.338 43.842 142.898 1.00 56.88 C ANISOU 479 CD1 LEU A 149 7947 8137 5528 907 718 -112 C ATOM 480 CD2 LEU A 149 10.821 44.008 140.897 1.00 58.29 C ANISOU 480 CD2 LEU A 149 7760 8392 5994 895 814 -53 C ATOM 481 N HIS A 150 15.453 43.737 138.929 1.00 27.32 N ANISOU 481 N HIS A 150 3912 4152 2315 476 268 -5 N ATOM 482 CA HIS A 150 15.951 42.730 138.011 1.00 28.15 C ANISOU 482 CA HIS A 150 3891 4286 2518 351 262 69 C ATOM 483 C HIS A 150 17.344 42.261 138.402 1.00 34.05 C ANISOU 483 C HIS A 150 4680 4975 3281 272 151 63 C ATOM 484 O HIS A 150 17.630 41.059 138.389 1.00 34.03 O ANISOU 484 O HIS A 150 4620 5017 3291 212 168 114 O ATOM 485 CB HIS A 150 15.959 43.285 136.587 1.00 30.00 C ANISOU 485 CB HIS A 150 4046 4485 2867 310 241 92 C ATOM 486 CG HIS A 150 16.412 42.289 135.565 1.00 34.10 C ANISOU 486 CG HIS A 150 4451 5039 3468 198 249 153 C ATOM 487 ND1 HIS A 150 17.449 42.535 134.693 1.00 34.68 N ANISOU 487 ND1 HIS A 150 4507 5043 3628 113 192 167 N ATOM 488 CD2 HIS A 150 15.987 41.028 135.299 1.00 31.87 C ANISOU 488 CD2 HIS A 150 4072 4846 3193 158 314 198 C ATOM 489 CE1 HIS A 150 17.633 41.477 133.918 1.00 33.73 C ANISOU 489 CE1 HIS A 150 4290 4975 3549 42 227 209 C ATOM 490 NE2 HIS A 150 16.759 40.548 134.266 1.00 30.92 N ANISOU 490 NE2 HIS A 150 3889 4708 3150 66 288 224 N ATOM 491 N ILE A 151 18.234 43.198 138.719 1.00 34.72 N ANISOU 491 N ILE A 151 4854 4949 3388 271 25 -2 N ATOM 492 CA ILE A 151 19.611 42.835 139.028 1.00 33.37 C ANISOU 492 CA ILE A 151 4690 4717 3272 196 -105 -18 C ATOM 493 C ILE A 151 19.659 41.965 140.273 1.00 33.97 C ANISOU 493 C ILE A 151 4857 4838 3213 242 -128 -18 C ATOM 494 O ILE A 151 20.380 40.967 140.319 1.00 30.84 O ANISOU 494 O ILE A 151 4413 4450 2856 187 -175 19 O ATOM 495 CB ILE A 151 20.466 44.108 139.186 1.00 36.48 C ANISOU 495 CB ILE A 151 5155 4971 3736 180 -247 -99 C ATOM 496 CG1 ILE A 151 20.840 44.656 137.815 1.00 37.37 C ANISOU 496 CG1 ILE A 151 5159 5025 4013 87 -227 -61 C ATOM 497 CG2 ILE A 151 21.718 43.831 140.027 1.00 40.38 C ANISOU 497 CG2 ILE A 151 5686 5405 4251 145 -417 -149 C ATOM 498 CD1 ILE A 151 21.375 46.088 137.888 1.00 45.67 C ANISOU 498 CD1 ILE A 151 6289 5920 5144 70 -335 -126 C ATOM 499 N VAL A 152 18.884 42.329 141.296 1.00 30.03 N ANISOU 499 N VAL A 152 4503 4365 2544 354 -86 -57 N ATOM 500 CA VAL A 152 18.889 41.618 142.566 1.00 32.59 C ANISOU 500 CA VAL A 152 4962 4726 2696 412 -97 -49 C ATOM 501 C VAL A 152 18.255 40.233 142.431 1.00 39.10 C ANISOU 501 C VAL A 152 5707 5652 3497 382 50 65 C ATOM 502 O VAL A 152 18.666 39.287 143.113 1.00 36.36 O ANISOU 502 O VAL A 152 5428 5311 3077 376 12 111 O ATOM 503 CB VAL A 152 18.170 42.472 143.630 1.00 42.83 C ANISOU 503 CB VAL A 152 6447 6026 3800 550 -60 -128 C ATOM 504 CG1 VAL A 152 17.897 41.655 144.885 1.00 44.99 C ANISOU 504 CG1 VAL A 152 6878 6365 3853 620 -6 -92 C ATOM 505 CG2 VAL A 152 18.988 43.725 143.969 1.00 41.61 C ANISOU 505 CG2 VAL A 152 6409 5738 3662 575 -255 -257 C ATOM 506 N ILE A 153 17.251 40.083 141.569 1.00 37.14 N ANISOU 506 N ILE A 153 5322 5473 3319 362 205 113 N ATOM 507 CA ILE A 153 16.579 38.794 141.456 1.00 38.31 C ANISOU 507 CA ILE A 153 5388 5702 3466 321 339 213 C ATOM 508 C ILE A 153 17.282 37.875 140.458 1.00 37.05 C ANISOU 508 C ILE A 153 5092 5519 3465 207 285 259 C ATOM 509 O ILE A 153 17.226 36.653 140.610 1.00 38.62 O ANISOU 509 O ILE A 153 5273 5738 3664 166 327 333 O ATOM 510 CB ILE A 153 15.085 38.963 141.093 1.00 36.83 C ANISOU 510 CB ILE A 153 5101 5602 3288 355 520 233 C ATOM 511 CG1 ILE A 153 14.321 37.647 141.333 1.00 35.99 C ANISOU 511 CG1 ILE A 153 4938 5569 3167 312 669 334 C ATOM 512 CG2 ILE A 153 14.892 39.384 139.644 1.00 31.81 C ANISOU 512 CG2 ILE A 153 4307 4964 2816 310 503 220 C ATOM 513 CD1 ILE A 153 14.035 37.376 142.788 1.00 41.33 C ANISOU 513 CD1 ILE A 153 5784 6274 3645 381 760 367 C ATOM 514 N ALA A 154 17.971 38.429 139.458 1.00 32.33 N ANISOU 514 N ALA A 154 4412 4873 3000 158 201 219 N ATOM 515 CA ALA A 154 18.524 37.632 138.375 1.00 31.60 C ANISOU 515 CA ALA A 154 4186 4771 3049 65 185 251 C ATOM 516 C ALA A 154 19.989 37.267 138.554 1.00 39.20 C ANISOU 516 C ALA A 154 5155 5662 4079 29 47 235 C ATOM 517 O ALA A 154 20.387 36.174 138.135 1.00 36.86 O ANISOU 517 O ALA A 154 4783 5363 3858 -19 48 271 O ATOM 518 CB ALA A 154 18.374 38.354 137.037 1.00 27.88 C ANISOU 518 CB ALA A 154 3617 4300 2677 33 207 232 C ATOM 519 N ILE A 155 20.814 38.139 139.130 1.00 33.45 N ANISOU 519 N ILE A 155 4500 4867 3343 53 -81 172 N ATOM 520 CA ILE A 155 22.251 37.860 139.125 1.00 31.52 C ANISOU 520 CA ILE A 155 4206 4554 3214 11 -224 147 C ATOM 521 C ILE A 155 22.637 36.930 140.274 1.00 31.56 C ANISOU 521 C ILE A 155 4308 4546 3135 57 -317 170 C ATOM 522 O ILE A 155 23.278 35.901 140.021 1.00 34.84 O ANISOU 522 O ILE A 155 4646 4945 3644 28 -352 202 O ATOM 523 CB ILE A 155 23.090 39.149 139.139 1.00 35.56 C ANISOU 523 CB ILE A 155 4723 4982 3804 -7 -344 68 C ATOM 524 CG1 ILE A 155 23.000 39.850 137.789 1.00 35.76 C ANISOU 524 CG1 ILE A 155 4640 5001 3946 -72 -255 73 C ATOM 525 CG2 ILE A 155 24.543 38.822 139.444 1.00 33.79 C ANISOU 525 CG2 ILE A 155 4443 4693 3704 -37 -513 34 C ATOM 526 CD1 ILE A 155 23.390 38.953 136.627 1.00 46.29 C ANISOU 526 CD1 ILE A 155 5821 6365 5401 -141 -178 118 C ATOM 527 N PRO A 156 22.290 37.220 141.534 1.00 34.23 N ANISOU 527 N PRO A 156 4828 4886 3291 138 -360 157 N ATOM 528 CA PRO A 156 22.794 36.356 142.613 1.00 33.81 C ANISOU 528 CA PRO A 156 4895 4808 3143 187 -474 188 C ATOM 529 C PRO A 156 22.385 34.897 142.466 1.00 43.30 C ANISOU 529 C PRO A 156 6070 6041 4343 168 -370 297 C ATOM 530 O PRO A 156 23.237 34.008 142.620 1.00 34.36 O ANISOU 530 O PRO A 156 4923 4857 3275 169 -484 324 O ATOM 531 CB PRO A 156 22.204 37.003 143.874 1.00 38.22 C ANISOU 531 CB PRO A 156 5680 5381 3460 285 -482 159 C ATOM 532 CG PRO A 156 22.072 38.473 143.495 1.00 37.03 C ANISOU 532 CG PRO A 156 5506 5210 3355 283 -486 61 C ATOM 533 CD PRO A 156 21.640 38.440 142.069 1.00 37.33 C ANISOU 533 CD PRO A 156 5345 5283 3556 201 -339 97 C ATOM 534 N ILE A 157 21.114 34.628 142.144 1.00 33.10 N ANISOU 534 N ILE A 157 4758 4817 3000 150 -167 358 N ATOM 535 CA ILE A 157 20.649 33.255 142.023 1.00 29.50 C ANISOU 535 CA ILE A 157 4278 4371 2558 115 -68 460 C ATOM 536 C ILE A 157 21.319 32.546 140.840 1.00 30.59 C ANISOU 536 C ILE A 157 4240 4473 2909 44 -100 453 C ATOM 537 O ILE A 157 21.574 31.336 140.895 1.00 34.13 O ANISOU 537 O ILE A 157 4691 4876 3401 32 -118 513 O ATOM 538 CB ILE A 157 19.110 33.219 141.910 1.00 33.36 C ANISOU 538 CB ILE A 157 4752 4942 2981 99 151 513 C ATOM 539 CG1 ILE A 157 18.593 31.785 142.079 1.00 34.12 C ANISOU 539 CG1 ILE A 157 4859 5027 3077 56 249 629 C ATOM 540 CG2 ILE A 157 18.643 33.727 140.561 1.00 29.41 C ANISOU 540 CG2 ILE A 157 4071 4482 2620 45 223 466 C ATOM 541 CD1 ILE A 157 18.886 31.195 143.424 1.00 43.99 C ANISOU 541 CD1 ILE A 157 6319 6235 4161 113 200 708 C ATOM 542 N ASN A 158 21.610 33.266 139.754 1.00 27.55 N ANISOU 542 N ASN A 158 3716 4099 2653 3 -98 383 N ATOM 543 CA ASN A 158 22.254 32.606 138.625 1.00 29.94 C ANISOU 543 CA ASN A 158 3868 4376 3133 -51 -104 368 C ATOM 544 C ASN A 158 23.759 32.447 138.825 1.00 35.92 C ANISOU 544 C ASN A 158 4588 5061 3999 -31 -271 327 C ATOM 545 O ASN A 158 24.343 31.502 138.280 1.00 33.64 O ANISOU 545 O ASN A 158 4210 4737 3836 -45 -285 331 O ATOM 546 CB ASN A 158 21.938 33.350 137.330 1.00 25.96 C ANISOU 546 CB ASN A 158 3246 3914 2702 -101 -15 325 C ATOM 547 CG ASN A 158 20.550 33.030 136.826 1.00 34.79 C ANISOU 547 CG ASN A 158 4343 5095 3780 -127 127 364 C ATOM 548 OD1 ASN A 158 20.228 31.869 136.624 1.00 32.71 O ANISOU 548 OD1 ASN A 158 4055 4823 3550 -155 169 404 O ATOM 549 ND2 ASN A 158 19.704 34.045 136.680 1.00 28.48 N ANISOU 549 ND2 ASN A 158 3552 4349 2921 -113 189 350 N ATOM 550 N VAL A 159 24.406 33.337 139.591 1.00 26.31 N ANISOU 550 N VAL A 159 3431 3817 2750 5 -407 279 N ATOM 551 CA VAL A 159 25.783 33.075 140.010 1.00 28.15 C ANISOU 551 CA VAL A 159 3628 3979 3089 35 -599 242 C ATOM 552 C VAL A 159 25.830 31.813 140.864 1.00 34.25 C ANISOU 552 C VAL A 159 4512 4712 3788 97 -670 315 C ATOM 553 O VAL A 159 26.697 30.950 140.683 1.00 33.78 O ANISOU 553 O VAL A 159 4370 4597 3866 115 -756 315 O ATOM 554 CB VAL A 159 26.371 34.279 140.769 1.00 35.45 C ANISOU 554 CB VAL A 159 4612 4872 3986 58 -760 167 C ATOM 555 CG1 VAL A 159 27.753 33.930 141.324 1.00 39.41 C ANISOU 555 CG1 VAL A 159 5069 5299 4604 97 -993 127 C ATOM 556 CG2 VAL A 159 26.444 35.516 139.869 1.00 26.81 C ANISOU 556 CG2 VAL A 159 3405 3784 2996 -14 -696 107 C ATOM 557 N TYR A 160 24.889 31.684 141.799 1.00 33.13 N ANISOU 557 N TYR A 160 4564 4593 3431 135 -622 383 N ATOM 558 CA TYR A 160 24.840 30.506 142.653 1.00 36.76 C ANISOU 558 CA TYR A 160 5166 5006 3795 189 -669 479 C ATOM 559 C TYR A 160 24.624 29.236 141.838 1.00 34.26 C ANISOU 559 C TYR A 160 4754 4661 3604 143 -566 538 C ATOM 560 O TYR A 160 25.264 28.212 142.094 1.00 40.73 O ANISOU 560 O TYR A 160 5596 5397 4483 185 -671 578 O ATOM 561 CB TYR A 160 23.741 30.655 143.707 1.00 35.41 C ANISOU 561 CB TYR A 160 5218 4877 3360 225 -576 552 C ATOM 562 CG TYR A 160 23.683 29.456 144.624 1.00 42.51 C ANISOU 562 CG TYR A 160 6294 5717 4140 274 -609 675 C ATOM 563 CD1 TYR A 160 24.450 29.406 145.786 1.00 47.15 C ANISOU 563 CD1 TYR A 160 7066 6250 4599 374 -823 684 C ATOM 564 CD2 TYR A 160 22.898 28.353 144.309 1.00 42.17 C ANISOU 564 CD2 TYR A 160 6242 5659 4122 219 -444 785 C ATOM 565 CE1 TYR A 160 24.421 28.300 146.614 1.00 48.47 C ANISOU 565 CE1 TYR A 160 7421 6350 4643 427 -860 814 C ATOM 566 CE2 TYR A 160 22.866 27.241 145.135 1.00 37.63 C ANISOU 566 CE2 TYR A 160 5844 5007 3448 256 -469 915 C ATOM 567 CZ TYR A 160 23.624 27.224 146.285 1.00 42.87 C ANISOU 567 CZ TYR A 160 6706 5618 3964 364 -672 937 C ATOM 568 OH TYR A 160 23.588 26.126 147.106 1.00 57.30 O ANISOU 568 OH TYR A 160 8737 7359 5676 408 -701 1083 O ATOM 569 N LYS A 161 23.691 29.263 140.884 1.00 36.73 N ANISOU 569 N LYS A 161 4972 5030 3955 66 -374 541 N ATOM 570 CA LYS A 161 23.443 28.063 140.084 1.00 40.38 C ANISOU 570 CA LYS A 161 5354 5453 4535 20 -291 578 C ATOM 571 C LYS A 161 24.683 27.672 139.294 1.00 38.60 C ANISOU 571 C LYS A 161 4980 5172 4514 34 -387 504 C ATOM 572 O LYS A 161 24.978 26.485 139.119 1.00 38.37 O ANISOU 572 O LYS A 161 4940 5062 4577 50 -413 532 O ATOM 573 CB LYS A 161 22.276 28.282 139.127 1.00 38.84 C ANISOU 573 CB LYS A 161 5072 5332 4352 -61 -105 569 C ATOM 574 CG LYS A 161 20.910 28.267 139.770 1.00 45.79 C ANISOU 574 CG LYS A 161 6054 6259 5085 -84 29 654 C ATOM 575 CD LYS A 161 19.910 27.712 138.793 1.00 46.86 C ANISOU 575 CD LYS A 161 6082 6415 5307 -169 167 665 C ATOM 576 CE LYS A 161 20.144 26.218 138.599 1.00 43.47 C ANISOU 576 CE LYS A 161 5656 5876 4984 -198 144 711 C ATOM 577 NZ LYS A 161 19.326 25.638 137.504 1.00 48.75 N ANISOU 577 NZ LYS A 161 6212 6546 5764 -285 238 689 N ATOM 578 N LEU A 162 25.419 28.662 138.801 1.00 29.70 N ANISOU 578 N LEU A 162 3733 4081 3471 30 -430 411 N ATOM 579 CA LEU A 162 26.587 28.365 137.989 1.00 31.60 C ANISOU 579 CA LEU A 162 3805 4284 3919 40 -481 338 C ATOM 580 C LEU A 162 27.672 27.699 138.819 1.00 34.54 C ANISOU 580 C LEU A 162 4198 4566 4361 129 -679 345 C ATOM 581 O LEU A 162 28.324 26.759 138.357 1.00 36.52 O ANISOU 581 O LEU A 162 4358 4754 4765 165 -706 325 O ATOM 582 CB LEU A 162 27.107 29.648 137.351 1.00 34.58 C ANISOU 582 CB LEU A 162 4053 4715 4373 0 -464 255 C ATOM 583 CG LEU A 162 28.286 29.532 136.400 1.00 32.37 C ANISOU 583 CG LEU A 162 3572 4416 4310 -3 -463 179 C ATOM 584 CD1 LEU A 162 27.883 28.704 135.193 1.00 25.04 C ANISOU 584 CD1 LEU A 162 2589 3500 3425 -28 -306 170 C ATOM 585 CD2 LEU A 162 28.715 30.954 135.982 1.00 26.44 C ANISOU 585 CD2 LEU A 162 2725 3706 3615 -61 -441 124 C ATOM 586 N LEU A 163 27.870 28.160 140.053 1.00 35.07 N ANISOU 586 N LEU A 163 4394 4619 4310 180 -831 367 N ATOM 587 CA LEU A 163 28.991 27.682 140.854 1.00 37.89 C ANISOU 587 CA LEU A 163 4769 4893 4736 277 -1065 363 C ATOM 588 C LEU A 163 28.638 26.481 141.727 1.00 42.46 C ANISOU 588 C LEU A 163 5548 5391 5194 344 -1121 480 C ATOM 589 O LEU A 163 29.495 25.624 141.957 1.00 39.34 O ANISOU 589 O LEU A 163 5133 4902 4911 428 -1276 488 O ATOM 590 CB LEU A 163 29.517 28.816 141.731 1.00 34.75 C ANISOU 590 CB LEU A 163 4418 4509 4276 304 -1243 310 C ATOM 591 CG LEU A 163 29.948 30.068 140.949 1.00 38.39 C ANISOU 591 CG LEU A 163 4689 5021 4876 227 -1202 204 C ATOM 592 CD1 LEU A 163 30.463 31.160 141.887 1.00 40.26 C ANISOU 592 CD1 LEU A 163 4986 5245 5066 248 -1406 142 C ATOM 593 CD2 LEU A 163 30.997 29.701 139.890 1.00 35.75 C ANISOU 593 CD2 LEU A 163 4087 4666 4830 213 -1186 139 C ATOM 594 N ALA A 164 27.405 26.406 142.230 1.00 34.51 N ANISOU 594 N ALA A 164 4730 4412 3969 312 -995 578 N ATOM 595 CA ALA A 164 27.001 25.342 143.132 1.00 43.16 C ANISOU 595 CA ALA A 164 6043 5428 4930 360 -1022 714 C ATOM 596 C ALA A 164 26.269 24.210 142.424 1.00 47.33 C ANISOU 596 C ALA A 164 6546 5905 5531 297 -851 781 C ATOM 597 O ALA A 164 26.216 23.098 142.962 1.00 43.82 O ANISOU 597 O ALA A 164 6243 5349 5058 335 -894 890 O ATOM 598 CB ALA A 164 26.120 25.905 144.253 1.00 38.11 C ANISOU 598 CB ALA A 164 5639 4842 3999 367 -975 791 C ATOM 599 N GLU A 165 25.707 24.474 141.242 1.00 54.48 N ANISOU 599 N GLU A 165 6716 6868 7117 390 -1021 1278 N ATOM 600 CA GLU A 165 25.060 23.458 140.410 1.00 65.27 C ANISOU 600 CA GLU A 165 8058 8263 8477 421 -824 1259 C ATOM 601 C GLU A 165 23.980 22.725 141.195 1.00 69.36 C ANISOU 601 C GLU A 165 8765 8765 8825 410 -758 1233 C ATOM 602 O GLU A 165 23.878 21.497 141.170 1.00 71.90 O ANISOU 602 O GLU A 165 9117 9059 9142 439 -702 1262 O ATOM 603 CB GLU A 165 26.090 22.478 139.841 1.00 60.38 C ANISOU 603 CB GLU A 165 7317 7613 8012 488 -816 1341 C ATOM 604 CG GLU A 165 27.224 23.162 139.098 1.00 70.17 C ANISOU 604 CG GLU A 165 8351 8854 9457 516 -852 1405 C ATOM 605 CD GLU A 165 28.025 22.205 138.237 1.00 73.50 C ANISOU 605 CD GLU A 165 8656 9244 10026 613 -751 1489 C ATOM 606 OE1 GLU A 165 27.997 20.983 138.524 1.00 62.69 O ANISOU 606 OE1 GLU A 165 7369 7839 8612 652 -731 1511 O ATOM 607 OE2 GLU A 165 28.668 22.680 137.266 1.00 74.77 O ANISOU 607 OE2 GLU A 165 8657 9410 10344 660 -676 1539 O ATOM 608 N ASP A 166 23.156 23.501 141.891 1.00 64.80 N ANISOU 608 N ASP A 166 8318 8195 8110 376 -749 1189 N ATOM 609 CA ASP A 166 22.295 22.946 142.922 1.00 64.96 C ANISOU 609 CA ASP A 166 8534 8176 7971 383 -692 1197 C ATOM 610 C ASP A 166 21.128 23.894 143.170 1.00 59.83 C ANISOU 610 C ASP A 166 7973 7549 7211 361 -585 1151 C ATOM 611 O ASP A 166 21.150 25.059 142.759 1.00 49.30 O ANISOU 611 O ASP A 166 6578 6253 5900 338 -606 1106 O ATOM 612 CB ASP A 166 23.093 22.712 144.205 1.00 69.39 C ANISOU 612 CB ASP A 166 9255 8659 8452 411 -870 1244 C ATOM 613 CG ASP A 166 22.318 21.956 145.233 1.00 84.51 C ANISOU 613 CG ASP A 166 11386 10520 10202 439 -790 1269 C ATOM 614 OD1 ASP A 166 21.317 21.318 144.847 1.00 92.51 O ANISOU 614 OD1 ASP A 166 12371 11557 11221 432 -601 1272 O ATOM 615 OD2 ASP A 166 22.694 22.009 146.422 1.00 89.71 O ANISOU 615 OD2 ASP A 166 12254 11100 10732 468 -921 1293 O ATOM 616 N TRP A 167 20.100 23.371 143.838 1.00 55.62 N ANISOU 616 N TRP A 167 7577 6985 6570 375 -454 1176 N ATOM 617 CA TRP A 167 18.970 24.176 144.299 1.00 53.29 C ANISOU 617 CA TRP A 167 7392 6690 6167 381 -322 1164 C ATOM 618 C TRP A 167 18.633 23.813 145.739 1.00 57.21 C ANISOU 618 C TRP A 167 8154 7102 6482 440 -279 1218 C ATOM 619 O TRP A 167 17.906 22.834 145.989 1.00 67.44 O ANISOU 619 O TRP A 167 9479 8369 7776 455 -136 1279 O ATOM 620 CB TRP A 167 17.745 24.005 143.413 1.00 43.12 C ANISOU 620 CB TRP A 167 5963 5443 4979 345 -135 1167 C ATOM 621 CG TRP A 167 16.683 24.982 143.785 1.00 38.43 C ANISOU 621 CG TRP A 167 5439 4850 4312 357 3 1167 C ATOM 622 CD1 TRP A 167 15.658 24.787 144.668 1.00 44.27 C ANISOU 622 CD1 TRP A 167 6314 5537 4969 401 177 1239 C ATOM 623 CD2 TRP A 167 16.561 26.330 143.318 1.00 39.35 C ANISOU 623 CD2 TRP A 167 5502 5014 4436 341 -5 1106 C ATOM 624 NE1 TRP A 167 14.895 25.926 144.761 1.00 50.67 N ANISOU 624 NE1 TRP A 167 7155 6358 5738 421 290 1231 N ATOM 625 CE2 TRP A 167 15.430 26.888 143.942 1.00 45.62 C ANISOU 625 CE2 TRP A 167 6405 5783 5147 379 169 1142 C ATOM 626 CE3 TRP A 167 17.286 27.112 142.416 1.00 39.04 C ANISOU 626 CE3 TRP A 167 5331 5030 4473 304 -125 1036 C ATOM 627 CZ2 TRP A 167 15.017 28.194 143.703 1.00 44.72 C ANISOU 627 CZ2 TRP A 167 6278 5698 5014 380 211 1100 C ATOM 628 CZ3 TRP A 167 16.875 28.417 142.180 1.00 43.27 C ANISOU 628 CZ3 TRP A 167 5854 5597 4990 296 -92 991 C ATOM 629 CH2 TRP A 167 15.753 28.942 142.822 1.00 43.67 C ANISOU 629 CH2 TRP A 167 6022 5624 4949 333 67 1018 C ATOM 630 N PRO A 168 19.120 24.580 146.710 1.00 58.26 N ANISOU 630 N PRO A 168 8503 7175 6457 481 -403 1205 N ATOM 631 CA PRO A 168 18.806 24.310 148.118 1.00 66.44 C ANISOU 631 CA PRO A 168 9859 8107 7280 560 -358 1255 C ATOM 632 C PRO A 168 17.587 25.039 148.668 1.00 66.80 C ANISOU 632 C PRO A 168 10076 8122 7185 621 -135 1274 C ATOM 633 O PRO A 168 17.228 24.792 149.824 1.00 71.15 O ANISOU 633 O PRO A 168 10916 8572 7545 710 -46 1330 O ATOM 634 CB PRO A 168 20.079 24.804 148.820 1.00 64.97 C ANISOU 634 CB PRO A 168 9846 7844 6996 574 -658 1229 C ATOM 635 CG PRO A 168 20.494 25.989 147.977 1.00 61.14 C ANISOU 635 CG PRO A 168 9187 7422 6623 515 -767 1163 C ATOM 636 CD PRO A 168 20.128 25.642 146.554 1.00 57.71 C ANISOU 636 CD PRO A 168 8412 7109 6406 456 -624 1151 C ATOM 637 N PHE A 169 16.929 25.909 147.897 1.00 50.44 N ANISOU 637 N PHE A 169 7849 6121 5197 589 -26 1239 N ATOM 638 CA PHE A 169 16.034 26.897 148.488 1.00 54.04 C ANISOU 638 CA PHE A 169 8495 6533 5504 662 141 1251 C ATOM 639 C PHE A 169 14.574 26.460 148.583 1.00 53.25 C ANISOU 639 C PHE A 169 8357 6426 5450 704 472 1352 C ATOM 640 O PHE A 169 13.756 27.223 149.104 1.00 58.90 O ANISOU 640 O PHE A 169 9226 7095 6055 787 659 1388 O ATOM 641 CB PHE A 169 16.135 28.208 147.704 1.00 53.61 C ANISOU 641 CB PHE A 169 8313 6545 5510 615 71 1167 C ATOM 642 CG PHE A 169 17.548 28.635 147.457 1.00 59.98 C ANISOU 642 CG PHE A 169 9087 7359 6343 560 -245 1094 C ATOM 643 CD1 PHE A 169 18.120 28.496 146.201 1.00 61.71 C ANISOU 643 CD1 PHE A 169 8987 7675 6784 469 -340 1058 C ATOM 644 CD2 PHE A 169 18.324 29.130 148.494 1.00 63.06 C ANISOU 644 CD2 PHE A 169 9777 7639 6545 604 -453 1076 C ATOM 645 CE1 PHE A 169 19.435 28.871 145.977 1.00 63.84 C ANISOU 645 CE1 PHE A 169 9197 7941 7118 427 -604 1023 C ATOM 646 CE2 PHE A 169 19.636 29.509 148.275 1.00 68.12 C ANISOU 646 CE2 PHE A 169 10352 8268 7260 543 -763 1036 C ATOM 647 CZ PHE A 169 20.193 29.377 147.013 1.00 67.07 C ANISOU 647 CZ PHE A 169 9859 8243 7381 455 -824 1018 C ATOM 648 N GLY A 170 14.216 25.270 148.118 1.00 51.00 N ANISOU 648 N GLY A 170 7877 6168 5334 656 551 1413 N ATOM 649 CA GLY A 170 12.848 24.807 148.235 1.00 47.85 C ANISOU 649 CA GLY A 170 7417 5742 5024 684 844 1537 C ATOM 650 C GLY A 170 11.939 25.298 147.115 1.00 51.01 C ANISOU 650 C GLY A 170 7525 6212 5644 615 946 1541 C ATOM 651 O GLY A 170 12.304 26.121 146.268 1.00 45.02 O ANISOU 651 O GLY A 170 6641 5528 4936 558 815 1439 O ATOM 652 N ALA A 171 10.713 24.766 147.124 1.00 49.05 N ANISOU 652 N ALA A 171 7165 5929 5545 621 1180 1677 N ATOM 653 CA ALA A 171 9.801 24.977 146.004 1.00 50.73 C ANISOU 653 CA ALA A 171 7074 6187 6016 537 1240 1703 C ATOM 654 C ALA A 171 9.263 26.403 145.970 1.00 46.67 C ANISOU 654 C ALA A 171 6571 5692 5467 584 1349 1688 C ATOM 655 O ALA A 171 9.057 26.963 144.887 1.00 47.30 O ANISOU 655 O ALA A 171 6441 5837 5695 506 1277 1630 O ATOM 656 CB ALA A 171 8.655 23.968 146.067 1.00 54.77 C ANISOU 656 CB ALA A 171 7444 6630 6737 520 1432 1879 C ATOM 657 N GLU A 172 9.027 27.007 147.136 1.00 41.13 N ANISOU 657 N GLU A 172 6141 4924 4561 721 1525 1738 N ATOM 658 CA GLU A 172 8.455 28.351 147.158 1.00 49.61 C ANISOU 658 CA GLU A 172 7253 6002 5594 784 1654 1734 C ATOM 659 C GLU A 172 9.378 29.349 146.464 1.00 46.88 C ANISOU 659 C GLU A 172 6892 5740 5180 722 1397 1554 C ATOM 660 O GLU A 172 8.930 30.182 145.667 1.00 41.47 O ANISOU 660 O GLU A 172 6036 5108 4612 683 1411 1523 O ATOM 661 CB GLU A 172 8.169 28.788 148.599 1.00 58.47 C ANISOU 661 CB GLU A 172 8747 7014 6456 968 1881 1814 C ATOM 662 CG GLU A 172 7.119 27.946 149.333 1.00 74.09 C ANISOU 662 CG GLU A 172 10744 8895 8513 1059 2209 2027 C ATOM 663 CD GLU A 172 7.662 26.610 149.828 1.00 82.94 C ANISOU 663 CD GLU A 172 11955 9975 9584 1044 2134 2056 C ATOM 664 OE1 GLU A 172 6.878 25.638 149.913 1.00 86.39 O ANISOU 664 OE1 GLU A 172 12247 10366 10211 1038 2318 2219 O ATOM 665 OE2 GLU A 172 8.872 26.529 150.128 1.00 83.06 O ANISOU 665 OE2 GLU A 172 12176 9996 9388 1036 1883 1925 O ATOM 666 N MET A 173 10.677 29.280 146.760 1.00 41.15 N ANISOU 666 N MET A 173 6335 5018 4283 713 1157 1446 N ATOM 667 CA MET A 173 11.636 30.130 146.069 1.00 42.32 C ANISOU 667 CA MET A 173 6434 5236 4411 645 906 1298 C ATOM 668 C MET A 173 11.783 29.724 144.606 1.00 38.68 C ANISOU 668 C MET A 173 5630 4870 4196 512 787 1251 C ATOM 669 O MET A 173 12.000 30.584 143.749 1.00 39.11 O ANISOU 669 O MET A 173 5564 4988 4309 461 692 1167 O ATOM 670 CB MET A 173 12.979 30.083 146.788 1.00 40.71 C ANISOU 670 CB MET A 173 6471 4988 4008 666 671 1229 C ATOM 671 CG MET A 173 12.957 30.766 148.148 1.00 47.69 C ANISOU 671 CG MET A 173 7760 5755 4604 800 725 1244 C ATOM 672 SD MET A 173 12.649 32.534 147.929 1.00 56.67 S ANISOU 672 SD MET A 173 8962 6901 5670 831 746 1175 S ATOM 673 CE MET A 173 14.158 33.031 147.099 1.00 55.30 C ANISOU 673 CE MET A 173 8648 6797 5568 700 353 1034 C ATOM 674 N CYS A 174 11.647 28.428 144.304 1.00 42.62 N ANISOU 674 N CYS A 174 5998 5366 4830 464 794 1307 N ATOM 675 CA CYS A 174 11.644 27.977 142.914 1.00 38.32 C ANISOU 675 CA CYS A 174 5180 4879 4500 355 697 1272 C ATOM 676 C CYS A 174 10.570 28.702 142.106 1.00 37.74 C ANISOU 676 C CYS A 174 4928 4831 4581 321 797 1289 C ATOM 677 O CYS A 174 10.777 29.023 140.932 1.00 37.35 O ANISOU 677 O CYS A 174 4724 4834 4633 251 678 1211 O ATOM 678 CB CYS A 174 11.434 26.453 142.861 1.00 34.86 C ANISOU 678 CB CYS A 174 4673 4400 4173 322 714 1351 C ATOM 679 SG CYS A 174 11.426 25.794 141.174 1.00 44.44 S ANISOU 679 SG CYS A 174 5629 5642 5613 205 575 1308 S ATOM 680 N LYS A 175 9.426 28.998 142.728 1.00 36.53 N ANISOU 680 N LYS A 175 4802 4631 4448 382 1024 1400 N ATOM 681 CA LYS A 175 8.351 29.691 142.018 1.00 38.46 C ANISOU 681 CA LYS A 175 4861 4887 4866 354 1122 1438 C ATOM 682 C LYS A 175 8.512 31.212 142.082 1.00 38.21 C ANISOU 682 C LYS A 175 4922 4894 4704 403 1129 1356 C ATOM 683 O LYS A 175 8.228 31.912 141.106 1.00 32.98 O ANISOU 683 O LYS A 175 4101 4275 4153 350 1080 1308 O ATOM 684 CB LYS A 175 6.990 29.282 142.603 1.00 37.69 C ANISOU 684 CB LYS A 175 4705 4708 4906 401 1384 1629 C ATOM 685 CG LYS A 175 6.652 27.783 142.484 1.00 34.27 C ANISOU 685 CG LYS A 175 4151 4221 4651 338 1378 1734 C ATOM 686 CD LYS A 175 5.352 27.436 143.222 1.00 47.18 C ANISOU 686 CD LYS A 175 5730 5761 6434 399 1666 1954 C ATOM 687 CE LYS A 175 4.789 26.068 142.789 1.00 42.18 C ANISOU 687 CE LYS A 175 4895 5061 6071 299 1626 2074 C ATOM 688 NZ LYS A 175 4.395 26.093 141.338 1.00 42.26 N ANISOU 688 NZ LYS A 175 4649 5079 6329 162 1433 2039 N ATOM 689 N LEU A 176 8.968 31.736 143.221 1.00 37.81 N ANISOU 689 N LEU A 176 5148 4811 4407 506 1174 1339 N ATOM 690 CA LEU A 176 8.976 33.181 143.439 1.00 33.26 C ANISOU 690 CA LEU A 176 4703 4241 3695 568 1201 1280 C ATOM 691 C LEU A 176 10.056 33.875 142.624 1.00 35.39 C ANISOU 691 C LEU A 176 4926 4584 3936 491 943 1124 C ATOM 692 O LEU A 176 9.841 34.979 142.110 1.00 33.88 O ANISOU 692 O LEU A 176 4683 4425 3763 483 941 1073 O ATOM 693 CB LEU A 176 9.157 33.457 144.930 1.00 46.53 C ANISOU 693 CB LEU A 176 6750 5831 5100 708 1301 1311 C ATOM 694 CG LEU A 176 9.182 34.907 145.398 1.00 65.67 C ANISOU 694 CG LEU A 176 9402 8221 7328 798 1331 1257 C ATOM 695 CD1 LEU A 176 7.813 35.544 145.203 1.00 71.84 C ANISOU 695 CD1 LEU A 176 10072 8994 8231 857 1604 1354 C ATOM 696 CD2 LEU A 176 9.627 34.988 146.854 1.00 69.10 C ANISOU 696 CD2 LEU A 176 10266 8538 7452 931 1348 1266 C ATOM 697 N VAL A 177 11.226 33.246 142.486 1.00 34.87 N ANISOU 697 N VAL A 177 4870 4539 3842 438 735 1060 N ATOM 698 CA VAL A 177 12.345 33.905 141.800 1.00 34.57 C ANISOU 698 CA VAL A 177 4787 4554 3793 379 509 940 C ATOM 699 C VAL A 177 12.024 34.186 140.335 1.00 32.44 C ANISOU 699 C VAL A 177 4256 4355 3714 299 488 900 C ATOM 700 O VAL A 177 12.111 35.355 139.920 1.00 33.85 O ANISOU 700 O VAL A 177 4419 4564 3878 291 450 837 O ATOM 701 CB VAL A 177 13.640 33.097 141.985 1.00 33.30 C ANISOU 701 CB VAL A 177 4667 4387 3598 353 316 914 C ATOM 702 CG1 VAL A 177 14.743 33.643 141.067 1.00 33.37 C ANISOU 702 CG1 VAL A 177 4554 4450 3675 288 115 826 C ATOM 703 CG2 VAL A 177 14.078 33.145 143.441 1.00 32.20 C ANISOU 703 CG2 VAL A 177 4834 4161 3239 433 280 933 C ATOM 704 N PRO A 178 11.630 33.201 139.512 1.00 32.61 N ANISOU 704 N PRO A 178 4095 4389 3906 241 500 934 N ATOM 705 CA PRO A 178 11.270 33.542 138.124 1.00 30.11 C ANISOU 705 CA PRO A 178 3584 4113 3744 176 464 894 C ATOM 706 C PRO A 178 10.035 34.422 138.028 1.00 35.92 C ANISOU 706 C PRO A 178 4264 4844 4542 191 605 932 C ATOM 707 O PRO A 178 9.928 35.206 137.076 1.00 34.27 O ANISOU 707 O PRO A 178 3956 4669 4396 155 555 874 O ATOM 708 CB PRO A 178 11.060 32.177 137.468 1.00 30.92 C ANISOU 708 CB PRO A 178 3570 4190 3988 123 431 934 C ATOM 709 CG PRO A 178 10.589 31.297 138.610 1.00 33.94 C ANISOU 709 CG PRO A 178 4034 4517 4344 162 549 1040 C ATOM 710 CD PRO A 178 11.405 31.770 139.797 1.00 28.24 C ANISOU 710 CD PRO A 178 3526 3795 3409 234 541 1014 C ATOM 711 N PHE A 179 9.113 34.340 138.992 1.00 32.86 N ANISOU 711 N PHE A 179 3939 4406 4140 255 793 1039 N ATOM 712 CA PHE A 179 7.971 35.255 139.014 1.00 31.65 C ANISOU 712 CA PHE A 179 3737 4239 4050 293 955 1095 C ATOM 713 C PHE A 179 8.439 36.702 139.144 1.00 32.73 C ANISOU 713 C PHE A 179 4000 4407 4029 335 923 999 C ATOM 714 O PHE A 179 8.124 37.552 138.303 1.00 32.84 O ANISOU 714 O PHE A 179 3902 4454 4122 304 899 957 O ATOM 715 CB PHE A 179 7.028 34.866 140.162 1.00 35.26 C ANISOU 715 CB PHE A 179 4267 4621 4508 384 1201 1250 C ATOM 716 CG PHE A 179 5.974 35.896 140.481 1.00 46.99 C ANISOU 716 CG PHE A 179 5757 6078 6020 467 1416 1328 C ATOM 717 CD1 PHE A 179 4.911 36.117 139.617 1.00 45.21 C ANISOU 717 CD1 PHE A 179 5279 5850 6048 420 1467 1397 C ATOM 718 CD2 PHE A 179 6.035 36.628 141.660 1.00 49.05 C ANISOU 718 CD2 PHE A 179 6292 6296 6048 603 1564 1340 C ATOM 719 CE1 PHE A 179 3.933 37.061 139.916 1.00 42.38 C ANISOU 719 CE1 PHE A 179 4908 5460 5735 507 1680 1485 C ATOM 720 CE2 PHE A 179 5.062 37.567 141.961 1.00 53.53 C ANISOU 720 CE2 PHE A 179 6882 6825 6631 702 1789 1421 C ATOM 721 CZ PHE A 179 4.010 37.782 141.086 1.00 48.14 C ANISOU 721 CZ PHE A 179 5912 6154 6226 655 1857 1499 C ATOM 722 N ILE A 180 9.216 36.997 140.187 1.00 32.89 N ANISOU 722 N ILE A 180 4269 4403 3825 402 897 964 N ATOM 723 CA ILE A 180 9.720 38.357 140.372 1.00 34.51 C ANISOU 723 CA ILE A 180 4623 4614 3877 435 829 876 C ATOM 724 C ILE A 180 10.602 38.773 139.202 1.00 33.09 C ANISOU 724 C ILE A 180 4301 4504 3766 338 617 764 C ATOM 725 O ILE A 180 10.574 39.931 138.758 1.00 31.62 O ANISOU 725 O ILE A 180 4102 4342 3571 332 590 706 O ATOM 726 CB ILE A 180 10.466 38.466 141.713 1.00 36.23 C ANISOU 726 CB ILE A 180 5162 4761 3843 515 784 862 C ATOM 727 CG1 ILE A 180 9.477 38.286 142.867 1.00 37.93 C ANISOU 727 CG1 ILE A 180 5563 4888 3959 646 1048 981 C ATOM 728 CG2 ILE A 180 11.200 39.825 141.798 1.00 32.16 C ANISOU 728 CG2 ILE A 180 4799 4234 3186 522 632 760 C ATOM 729 CD1 ILE A 180 10.131 38.052 144.219 1.00 43.08 C ANISOU 729 CD1 ILE A 180 6567 5445 4355 733 1007 985 C ATOM 730 N GLN A 181 11.389 37.837 138.677 1.00 32.92 N ANISOU 730 N GLN A 181 4182 4511 3817 272 481 741 N ATOM 731 CA GLN A 181 12.247 38.144 137.539 1.00 28.14 C ANISOU 731 CA GLN A 181 3448 3959 3286 201 319 658 C ATOM 732 C GLN A 181 11.432 38.648 136.352 1.00 30.04 C ANISOU 732 C GLN A 181 3519 4233 3662 164 366 642 C ATOM 733 O GLN A 181 11.757 39.687 135.768 1.00 30.90 O ANISOU 733 O GLN A 181 3603 4371 3766 147 304 576 O ATOM 734 CB GLN A 181 13.073 36.908 137.169 1.00 26.69 C ANISOU 734 CB GLN A 181 3192 3782 3165 162 216 662 C ATOM 735 CG GLN A 181 13.965 37.053 135.957 1.00 31.33 C ANISOU 735 CG GLN A 181 3654 4409 3840 114 94 604 C ATOM 736 CD GLN A 181 14.548 35.699 135.547 1.00 36.50 C ANISOU 736 CD GLN A 181 4249 5056 4564 99 44 627 C ATOM 737 OE1 GLN A 181 13.827 34.715 135.503 1.00 30.87 O ANISOU 737 OE1 GLN A 181 3510 4318 3899 93 109 671 O ATOM 738 NE2 GLN A 181 15.845 35.655 135.240 1.00 30.55 N ANISOU 738 NE2 GLN A 181 3466 4310 3829 97 -67 609 N ATOM 739 N LYS A 182 10.347 37.947 135.994 1.00 28.79 N ANISOU 739 N LYS A 182 3245 4057 3637 148 463 709 N ATOM 740 CA LYS A 182 9.567 38.401 134.839 1.00 29.16 C ANISOU 740 CA LYS A 182 3140 4115 3823 107 468 699 C ATOM 741 C LYS A 182 8.765 39.660 135.153 1.00 31.44 C ANISOU 741 C LYS A 182 3453 4404 4090 153 584 712 C ATOM 742 O LYS A 182 8.491 40.455 134.251 1.00 29.09 O ANISOU 742 O LYS A 182 3070 4126 3856 126 551 669 O ATOM 743 CB LYS A 182 8.622 37.306 134.336 1.00 27.91 C ANISOU 743 CB LYS A 182 2849 3912 3845 64 492 779 C ATOM 744 CG LYS A 182 9.344 36.038 133.834 1.00 25.51 C ANISOU 744 CG LYS A 182 2534 3593 3566 22 371 761 C ATOM 745 CD LYS A 182 10.511 36.357 132.903 1.00 31.02 C ANISOU 745 CD LYS A 182 3248 4328 4212 8 240 656 C ATOM 746 CE LYS A 182 11.106 35.058 132.335 1.00 34.76 C ANISOU 746 CE LYS A 182 3722 4768 4716 -11 153 653 C ATOM 747 NZ LYS A 182 11.519 34.137 133.453 1.00 28.44 N ANISOU 747 NZ LYS A 182 2988 3959 3857 13 180 703 N ATOM 748 N ALA A 183 8.339 39.832 136.403 1.00 28.60 N ANISOU 748 N ALA A 183 3222 4009 3636 233 732 778 N ATOM 749 CA ALA A 183 7.698 41.081 136.782 1.00 30.18 C ANISOU 749 CA ALA A 183 3490 4196 3780 302 857 789 C ATOM 750 C ALA A 183 8.636 42.251 136.525 1.00 32.11 C ANISOU 750 C ALA A 183 3826 4475 3899 292 721 667 C ATOM 751 O ALA A 183 8.241 43.254 135.910 1.00 31.43 O ANISOU 751 O ALA A 183 3680 4408 3854 287 732 634 O ATOM 752 CB ALA A 183 7.273 41.025 138.249 1.00 28.82 C ANISOU 752 CB ALA A 183 3513 3960 3479 418 1048 880 C ATOM 753 N SER A 184 9.909 42.104 136.909 1.00 33.40 N ANISOU 753 N SER A 184 4112 4643 3937 278 575 606 N ATOM 754 CA SER A 184 10.848 43.214 136.774 1.00 34.03 C ANISOU 754 CA SER A 184 4273 4735 3923 263 432 513 C ATOM 755 C SER A 184 11.184 43.492 135.315 1.00 38.57 C ANISOU 755 C SER A 184 4656 5368 4632 184 332 453 C ATOM 756 O SER A 184 11.424 44.654 134.951 1.00 30.61 O ANISOU 756 O SER A 184 3660 4371 3598 175 280 396 O ATOM 757 CB SER A 184 12.118 42.937 137.582 1.00 36.33 C ANISOU 757 CB SER A 184 4722 4993 4088 263 279 490 C ATOM 758 OG SER A 184 12.941 41.970 136.948 1.00 34.62 O ANISOU 758 OG SER A 184 4365 4812 3978 197 166 485 O ATOM 759 N VAL A 185 11.187 42.452 134.469 1.00 34.17 N ANISOU 759 N VAL A 185 3944 4832 4205 134 307 469 N ATOM 760 CA VAL A 185 11.350 42.654 133.030 1.00 27.71 C ANISOU 760 CA VAL A 185 2986 4047 3496 82 239 421 C ATOM 761 C VAL A 185 10.148 43.410 132.468 1.00 27.51 C ANISOU 761 C VAL A 185 2890 4021 3542 84 319 425 C ATOM 762 O VAL A 185 10.295 44.337 131.659 1.00 28.94 O ANISOU 762 O VAL A 185 3037 4221 3737 67 274 369 O ATOM 763 CB VAL A 185 11.563 41.300 132.317 1.00 28.99 C ANISOU 763 CB VAL A 185 3060 4203 3753 48 196 440 C ATOM 764 CG1 VAL A 185 11.857 41.499 130.830 1.00 26.70 C ANISOU 764 CG1 VAL A 185 2688 3921 3535 17 129 390 C ATOM 765 CG2 VAL A 185 12.713 40.547 132.959 1.00 28.67 C ANISOU 765 CG2 VAL A 185 3082 4159 3654 55 129 450 C ATOM 766 N GLY A 186 8.942 43.043 132.901 1.00 30.27 N ANISOU 766 N GLY A 186 3208 4340 3953 109 444 506 N ATOM 767 CA GLY A 186 7.769 43.785 132.469 1.00 28.45 C ANISOU 767 CA GLY A 186 2893 4098 3818 118 523 535 C ATOM 768 C GLY A 186 7.864 45.262 132.814 1.00 31.30 C ANISOU 768 C GLY A 186 3355 4472 4064 165 559 487 C ATOM 769 O GLY A 186 7.619 46.125 131.966 1.00 27.47 O ANISOU 769 O GLY A 186 2808 4002 3628 146 528 445 O ATOM 770 N ILE A 187 8.238 45.570 134.062 1.00 30.63 N ANISOU 770 N ILE A 187 3454 4369 3815 230 611 490 N ATOM 771 CA ILE A 187 8.368 46.968 134.487 1.00 32.85 C ANISOU 771 CA ILE A 187 3881 4638 3962 281 625 443 C ATOM 772 C ILE A 187 9.380 47.698 133.609 1.00 31.60 C ANISOU 772 C ILE A 187 3694 4517 3795 215 451 341 C ATOM 773 O ILE A 187 9.151 48.829 133.178 1.00 33.19 O ANISOU 773 O ILE A 187 3893 4723 3992 220 452 302 O ATOM 774 CB ILE A 187 8.765 47.032 135.976 1.00 33.86 C ANISOU 774 CB ILE A 187 4268 4709 3886 360 660 457 C ATOM 775 CG1 ILE A 187 7.621 46.529 136.860 1.00 32.55 C ANISOU 775 CG1 ILE A 187 4152 4493 3722 456 894 577 C ATOM 776 CG2 ILE A 187 9.173 48.480 136.385 1.00 34.85 C ANISOU 776 CG2 ILE A 187 4595 4799 3847 401 605 388 C ATOM 777 CD1 ILE A 187 8.066 46.097 138.246 1.00 33.77 C ANISOU 777 CD1 ILE A 187 4568 4582 3683 532 922 603 C ATOM 778 N THR A 188 10.516 47.056 133.338 1.00 36.91 N ANISOU 778 N THR A 188 4339 5209 4476 159 313 311 N ATOM 779 CA THR A 188 11.555 47.636 132.491 1.00 28.53 C ANISOU 779 CA THR A 188 3228 4172 3439 105 174 246 C ATOM 780 C THR A 188 11.018 47.991 131.107 1.00 30.60 C ANISOU 780 C THR A 188 3349 4463 3816 76 191 221 C ATOM 781 O THR A 188 11.165 49.130 130.644 1.00 27.72 O ANISOU 781 O THR A 188 2989 4104 3440 69 160 176 O ATOM 782 CB THR A 188 12.717 46.638 132.378 1.00 31.46 C ANISOU 782 CB THR A 188 3558 4551 3845 68 69 254 C ATOM 783 OG1 THR A 188 13.331 46.488 133.662 1.00 36.04 O ANISOU 783 OG1 THR A 188 4289 5092 4314 89 9 272 O ATOM 784 CG2 THR A 188 13.760 47.108 131.365 1.00 28.01 C ANISOU 784 CG2 THR A 188 3034 4131 3476 26 -33 220 C ATOM 785 N VAL A 189 10.404 47.022 130.415 1.00 23.74 N ANISOU 785 N VAL A 189 2369 3596 3057 58 222 253 N ATOM 786 CA VAL A 189 10.040 47.262 129.017 1.00 29.75 C ANISOU 786 CA VAL A 189 3033 4358 3912 29 193 225 C ATOM 787 C VAL A 189 8.836 48.199 128.932 1.00 32.58 C ANISOU 787 C VAL A 189 3366 4707 4305 50 265 234 C ATOM 788 O VAL A 189 8.781 49.075 128.062 1.00 34.60 O ANISOU 788 O VAL A 189 3600 4968 4580 39 231 188 O ATOM 789 CB VAL A 189 9.804 45.937 128.248 1.00 31.87 C ANISOU 789 CB VAL A 189 3233 4601 4277 2 160 252 C ATOM 790 CG1 VAL A 189 11.011 45.018 128.397 1.00 30.21 C ANISOU 790 CG1 VAL A 189 3052 4395 4030 -1 111 251 C ATOM 791 CG2 VAL A 189 8.534 45.241 128.672 1.00 36.39 C ANISOU 791 CG2 VAL A 189 3749 5138 4938 2 224 330 C ATOM 792 N LEU A 190 7.874 48.062 129.850 1.00 25.40 N ANISOU 792 N LEU A 190 2464 3778 3410 90 381 304 N ATOM 793 CA LEU A 190 6.736 48.981 129.831 1.00 29.02 C ANISOU 793 CA LEU A 190 2887 4219 3919 126 474 335 C ATOM 794 C LEU A 190 7.144 50.398 130.249 1.00 30.58 C ANISOU 794 C LEU A 190 3213 4428 3977 167 489 275 C ATOM 795 O LEU A 190 6.558 51.372 129.769 1.00 33.54 O ANISOU 795 O LEU A 190 3558 4799 4386 181 514 262 O ATOM 796 CB LEU A 190 5.621 48.446 130.725 1.00 32.80 C ANISOU 796 CB LEU A 190 3332 4661 4471 178 631 455 C ATOM 797 CG LEU A 190 4.914 47.190 130.202 1.00 39.50 C ANISOU 797 CG LEU A 190 4021 5474 5514 127 603 536 C ATOM 798 CD1 LEU A 190 3.810 46.751 131.156 1.00 36.16 C ANISOU 798 CD1 LEU A 190 3543 5004 5192 184 786 683 C ATOM 799 CD2 LEU A 190 4.338 47.453 128.821 1.00 43.19 C ANISOU 799 CD2 LEU A 190 4362 5916 6130 71 493 521 C ATOM 800 N SER A 191 8.133 50.535 131.140 1.00 32.12 N ANISOU 800 N SER A 191 3560 4623 4020 184 454 243 N ATOM 801 CA SER A 191 8.614 51.870 131.496 1.00 29.95 C ANISOU 801 CA SER A 191 3427 4336 3616 209 420 184 C ATOM 802 C SER A 191 9.335 52.521 130.320 1.00 35.62 C ANISOU 802 C SER A 191 4075 5083 4378 144 294 113 C ATOM 803 O SER A 191 9.171 53.724 130.069 1.00 33.04 O ANISOU 803 O SER A 191 3783 4748 4022 157 293 75 O ATOM 804 CB SER A 191 9.532 51.808 132.717 1.00 23.48 C ANISOU 804 CB SER A 191 2804 3480 2637 232 361 174 C ATOM 805 OG SER A 191 8.795 51.469 133.878 1.00 26.53 O ANISOU 805 OG SER A 191 3316 3821 2942 321 509 240 O ATOM 806 N LEU A 192 10.144 51.744 129.594 1.00 27.10 N ANISOU 806 N LEU A 192 2906 4028 3365 87 203 101 N ATOM 807 CA LEU A 192 10.785 52.250 128.385 1.00 26.12 C ANISOU 807 CA LEU A 192 2714 3919 3291 45 124 55 C ATOM 808 C LEU A 192 9.748 52.705 127.370 1.00 31.16 C ANISOU 808 C LEU A 192 3280 4557 4003 48 166 44 C ATOM 809 O LEU A 192 9.862 53.793 126.794 1.00 28.73 O ANISOU 809 O LEU A 192 2982 4249 3686 44 142 2 O ATOM 810 CB LEU A 192 11.674 51.169 127.767 1.00 30.57 C ANISOU 810 CB LEU A 192 3208 4492 3915 12 68 68 C ATOM 811 CG LEU A 192 13.164 51.172 128.028 1.00 45.32 C ANISOU 811 CG LEU A 192 5090 6356 5773 -9 -21 74 C ATOM 812 CD1 LEU A 192 13.787 49.949 127.333 1.00 48.47 C ANISOU 812 CD1 LEU A 192 5414 6758 6246 -15 -26 104 C ATOM 813 CD2 LEU A 192 13.757 52.473 127.515 1.00 37.53 C ANISOU 813 CD2 LEU A 192 4100 5361 4798 -27 -70 46 C ATOM 814 N CYS A 193 8.751 51.854 127.108 1.00 26.24 N ANISOU 814 N CYS A 193 2580 3922 3467 51 209 87 N ATOM 815 CA CYS A 193 7.641 52.223 126.237 1.00 30.94 C ANISOU 815 CA CYS A 193 3102 4495 4158 51 220 94 C ATOM 816 C CYS A 193 6.986 53.516 126.695 1.00 35.57 C ANISOU 816 C CYS A 193 3723 5080 4713 95 296 93 C ATOM 817 O CYS A 193 6.790 54.440 125.895 1.00 31.57 O ANISOU 817 O CYS A 193 3204 4567 4223 91 266 55 O ATOM 818 CB CYS A 193 6.608 51.097 126.207 1.00 30.83 C ANISOU 818 CB CYS A 193 2995 4446 4272 41 239 171 C ATOM 819 SG CYS A 193 7.163 49.673 125.237 1.00 32.02 S ANISOU 819 SG CYS A 193 3132 4569 4467 -7 122 161 S ATOM 820 N ALA A 194 6.650 53.601 127.990 1.00 30.17 N ANISOU 820 N ALA A 194 3106 4389 3970 149 403 137 N ATOM 821 CA ALA A 194 6.003 54.806 128.505 1.00 32.56 C ANISOU 821 CA ALA A 194 3476 4673 4223 217 501 145 C ATOM 822 C ALA A 194 6.877 56.040 128.300 1.00 27.45 C ANISOU 822 C ALA A 194 2935 4032 3462 205 419 56 C ATOM 823 O ALA A 194 6.368 57.120 127.992 1.00 28.89 O ANISOU 823 O ALA A 194 3129 4203 3646 232 448 38 O ATOM 824 CB ALA A 194 5.649 54.646 129.984 1.00 26.73 C ANISOU 824 CB ALA A 194 2855 3904 3397 301 644 209 C ATOM 825 N LEU A 195 8.195 55.901 128.440 1.00 22.12 N ANISOU 825 N LEU A 195 2324 3369 2711 161 311 11 N ATOM 826 CA LEU A 195 9.064 57.064 128.274 1.00 28.44 C ANISOU 826 CA LEU A 195 3206 4159 3439 139 219 -52 C ATOM 827 C LEU A 195 9.090 57.545 126.824 1.00 36.78 C ANISOU 827 C LEU A 195 4158 5234 4583 100 175 -87 C ATOM 828 O LEU A 195 9.112 58.758 126.565 1.00 33.78 O ANISOU 828 O LEU A 195 3825 4840 4171 105 157 -124 O ATOM 829 CB LEU A 195 10.474 56.738 128.756 1.00 33.26 C ANISOU 829 CB LEU A 195 3874 4762 4001 95 99 -62 C ATOM 830 CG LEU A 195 11.455 57.915 128.715 1.00 37.68 C ANISOU 830 CG LEU A 195 4506 5290 4521 60 -23 -102 C ATOM 831 CD1 LEU A 195 11.016 59.054 129.667 1.00 41.64 C ANISOU 831 CD1 LEU A 195 5208 5730 4882 117 -9 -125 C ATOM 832 CD2 LEU A 195 12.867 57.454 129.031 1.00 37.12 C ANISOU 832 CD2 LEU A 195 4431 5201 4473 5 -160 -82 C ATOM 833 N SER A 196 9.085 56.613 125.866 1.00 30.03 N ANISOU 833 N SER A 196 3190 4396 3824 68 155 -75 N ATOM 834 CA SER A 196 9.126 57.003 124.459 1.00 26.56 C ANISOU 834 CA SER A 196 2700 3952 3441 47 115 -106 C ATOM 835 C SER A 196 7.844 57.724 124.052 1.00 30.75 C ANISOU 835 C SER A 196 3206 4464 4012 75 155 -107 C ATOM 836 O SER A 196 7.882 58.661 123.241 1.00 31.13 O ANISOU 836 O SER A 196 3268 4502 4059 72 127 -146 O ATOM 837 CB SER A 196 9.363 55.775 123.572 1.00 27.49 C ANISOU 837 CB SER A 196 2760 4062 3621 27 82 -91 C ATOM 838 OG SER A 196 8.195 54.964 123.477 1.00 30.12 O ANISOU 838 OG SER A 196 3039 4376 4030 32 97 -55 O ATOM 839 N ILE A 197 6.703 57.291 124.596 1.00 26.52 N ANISOU 839 N ILE A 197 2625 3919 3533 106 225 -52 N ATOM 840 CA ILE A 197 5.429 57.962 124.344 1.00 27.81 C ANISOU 840 CA ILE A 197 2738 4056 3773 140 273 -24 C ATOM 841 C ILE A 197 5.398 59.333 125.009 1.00 29.86 C ANISOU 841 C ILE A 197 3098 4314 3933 192 340 -49 C ATOM 842 O ILE A 197 4.874 60.303 124.445 1.00 30.61 O ANISOU 842 O ILE A 197 3184 4391 4054 209 341 -65 O ATOM 843 CB ILE A 197 4.269 57.089 124.846 1.00 31.68 C ANISOU 843 CB ILE A 197 3126 4523 4388 164 350 76 C ATOM 844 CG1 ILE A 197 4.163 55.811 124.009 1.00 31.00 C ANISOU 844 CG1 ILE A 197 2951 4412 4415 105 245 98 C ATOM 845 CG2 ILE A 197 2.967 57.884 124.876 1.00 29.03 C ANISOU 845 CG2 ILE A 197 2724 4152 4153 219 435 137 C ATOM 846 CD1 ILE A 197 3.256 54.772 124.616 1.00 36.86 C ANISOU 846 CD1 ILE A 197 3587 5126 5292 112 304 209 C ATOM 847 N ASP A 198 5.908 59.421 126.237 1.00 30.04 N ANISOU 847 N ASP A 198 3241 4338 3834 223 387 -49 N ATOM 848 CA ASP A 198 5.910 60.687 126.958 1.00 36.78 C ANISOU 848 CA ASP A 198 4246 5163 4565 281 433 -75 C ATOM 849 C ASP A 198 6.785 61.725 126.261 1.00 38.39 C ANISOU 849 C ASP A 198 4499 5367 4722 232 317 -154 C ATOM 850 O ASP A 198 6.440 62.918 126.215 1.00 31.36 O ANISOU 850 O ASP A 198 3676 4449 3789 269 340 -178 O ATOM 851 CB ASP A 198 6.387 60.449 128.389 1.00 35.78 C ANISOU 851 CB ASP A 198 4287 5011 4298 322 466 -63 C ATOM 852 CG ASP A 198 6.510 61.730 129.176 1.00 41.47 C ANISOU 852 CG ASP A 198 5228 5672 4856 385 480 -98 C ATOM 853 OD1 ASP A 198 5.494 62.154 129.768 1.00 41.42 O ANISOU 853 OD1 ASP A 198 5298 5626 4815 494 641 -51 O ATOM 854 OD2 ASP A 198 7.622 62.306 129.204 1.00 37.17 O ANISOU 854 OD2 ASP A 198 4783 5108 4231 331 332 -160 O ATOM 855 N ARG A 199 7.932 61.296 125.729 1.00 29.65 N ANISOU 855 N ARG A 199 3355 4282 3629 157 206 -182 N ATOM 856 CA ARG A 199 8.816 62.227 125.039 1.00 30.49 C ANISOU 856 CA ARG A 199 3483 4379 3723 113 114 -230 C ATOM 857 C ARG A 199 8.206 62.685 123.717 1.00 31.01 C ANISOU 857 C ARG A 199 3472 4448 3864 112 124 -247 C ATOM 858 O ARG A 199 8.333 63.856 123.341 1.00 29.97 O ANISOU 858 O ARG A 199 3388 4296 3705 112 100 -281 O ATOM 859 CB ARG A 199 10.195 61.579 124.844 1.00 23.78 C ANISOU 859 CB ARG A 199 2593 3539 2902 49 25 -222 C ATOM 860 CG ARG A 199 10.955 61.384 126.182 1.00 30.05 C ANISOU 860 CG ARG A 199 3488 4308 3620 39 -36 -208 C ATOM 861 CD ARG A 199 11.257 62.715 126.915 1.00 39.45 C ANISOU 861 CD ARG A 199 4843 5435 4712 44 -109 -237 C ATOM 862 NE ARG A 199 10.144 63.202 127.731 1.00 47.56 N ANISOU 862 NE ARG A 199 6013 6433 5626 131 -13 -249 N ATOM 863 CZ ARG A 199 10.037 64.456 128.175 1.00 50.59 C ANISOU 863 CZ ARG A 199 6563 6751 5906 163 -40 -281 C ATOM 864 NH1 ARG A 199 8.992 64.822 128.903 1.00 43.65 N ANISOU 864 NH1 ARG A 199 5823 5837 4924 267 86 -276 N ATOM 865 NH2 ARG A 199 10.969 65.351 127.877 1.00 41.15 N ANISOU 865 NH2 ARG A 199 5399 5515 4723 98 -182 -307 N ATOM 866 N TYR A 200 7.503 61.789 123.020 1.00 27.85 N ANISOU 866 N TYR A 200 2970 4057 3554 113 143 -221 N ATOM 867 CA TYR A 200 6.756 62.188 121.832 1.00 31.30 C ANISOU 867 CA TYR A 200 3362 4473 4059 119 126 -232 C ATOM 868 C TYR A 200 5.677 63.210 122.175 1.00 33.50 C ANISOU 868 C TYR A 200 3655 4733 4342 173 188 -223 C ATOM 869 O TYR A 200 5.536 64.243 121.500 1.00 28.16 O ANISOU 869 O TYR A 200 3004 4036 3658 179 165 -257 O ATOM 870 CB TYR A 200 6.112 60.968 121.169 1.00 28.15 C ANISOU 870 CB TYR A 200 2876 4059 3762 107 95 -196 C ATOM 871 CG TYR A 200 5.079 61.417 120.162 1.00 31.55 C ANISOU 871 CG TYR A 200 3272 4441 4273 118 51 -194 C ATOM 872 CD1 TYR A 200 3.719 61.245 120.391 1.00 33.61 C ANISOU 872 CD1 TYR A 200 3438 4675 4658 141 73 -128 C ATOM 873 CD2 TYR A 200 5.473 62.073 119.002 1.00 28.58 C ANISOU 873 CD2 TYR A 200 2960 4038 3862 111 -9 -244 C ATOM 874 CE1 TYR A 200 2.786 61.687 119.465 1.00 31.86 C ANISOU 874 CE1 TYR A 200 3176 4396 4535 145 2 -116 C ATOM 875 CE2 TYR A 200 4.552 62.520 118.085 1.00 26.36 C ANISOU 875 CE2 TYR A 200 2672 3701 3644 122 -71 -245 C ATOM 876 CZ TYR A 200 3.219 62.324 118.315 1.00 31.05 C ANISOU 876 CZ TYR A 200 3161 4265 4370 135 -81 -183 C ATOM 877 OH TYR A 200 2.323 62.777 117.375 1.00 42.63 O ANISOU 877 OH TYR A 200 4613 5662 5922 140 -173 -174 O ATOM 878 N ARG A 201 4.879 62.921 123.205 1.00 29.43 N ANISOU 878 N ARG A 201 3124 4216 3844 223 284 -167 N ATOM 879 CA ARG A 201 3.832 63.858 123.606 1.00 37.27 C ANISOU 879 CA ARG A 201 4132 5179 4848 300 382 -137 C ATOM 880 C ARG A 201 4.417 65.219 123.981 1.00 34.50 C ANISOU 880 C ARG A 201 3942 4813 4352 323 381 -200 C ATOM 881 O ARG A 201 3.820 66.265 123.693 1.00 37.05 O ANISOU 881 O ARG A 201 4286 5110 4682 365 411 -207 O ATOM 882 CB ARG A 201 3.035 63.273 124.775 1.00 35.83 C ANISOU 882 CB ARG A 201 3932 4986 4698 371 527 -46 C ATOM 883 N ALA A 202 5.597 65.224 124.598 1.00 29.63 N ANISOU 883 N ALA A 202 3440 4200 3616 291 326 -239 N ATOM 884 CA ALA A 202 6.217 66.475 125.020 1.00 32.10 C ANISOU 884 CA ALA A 202 3921 4475 3802 299 284 -292 C ATOM 885 C ALA A 202 6.565 67.363 123.822 1.00 37.11 C ANISOU 885 C ALA A 202 4522 5106 4470 251 203 -339 C ATOM 886 O ALA A 202 6.475 68.594 123.904 1.00 34.84 O ANISOU 886 O ALA A 202 4340 4779 4119 279 199 -370 O ATOM 887 CB ALA A 202 7.464 66.171 125.852 1.00 31.70 C ANISOU 887 CB ALA A 202 3976 4409 3659 255 192 -308 C ATOM 888 N VAL A 203 6.959 66.757 122.702 1.00 32.21 N ANISOU 888 N VAL A 203 3782 4517 3940 190 146 -342 N ATOM 889 CA VAL A 203 7.250 67.508 121.484 1.00 34.18 C ANISOU 889 CA VAL A 203 4016 4754 4217 160 93 -375 C ATOM 890 C VAL A 203 5.968 67.864 120.738 1.00 35.63 C ANISOU 890 C VAL A 203 4150 4924 4463 205 129 -370 C ATOM 891 O VAL A 203 5.840 68.967 120.194 1.00 35.88 O ANISOU 891 O VAL A 203 4225 4929 4478 215 113 -400 O ATOM 892 CB VAL A 203 8.212 66.706 120.580 1.00 38.51 C ANISOU 892 CB VAL A 203 4496 5318 4817 103 42 -367 C ATOM 893 CG1 VAL A 203 8.453 67.457 119.276 1.00 39.69 C ANISOU 893 CG1 VAL A 203 4655 5440 4984 94 18 -389 C ATOM 894 CG2 VAL A 203 9.531 66.420 121.306 1.00 33.01 C ANISOU 894 CG2 VAL A 203 3819 4625 4098 57 -4 -352 C ATOM 895 N ALA A 204 5.005 66.941 120.670 1.00 32.18 N ANISOU 895 N ALA A 204 3614 4494 4117 226 160 -323 N ATOM 896 CA ALA A 204 3.873 67.133 119.768 1.00 30.48 C ANISOU 896 CA ALA A 204 3327 4248 4005 249 143 -303 C ATOM 897 C ALA A 204 2.734 67.950 120.368 1.00 33.52 C ANISOU 897 C ALA A 204 3703 4610 4423 327 237 -264 C ATOM 898 O ALA A 204 1.997 68.602 119.620 1.00 33.51 O ANISOU 898 O ALA A 204 3669 4574 4490 348 210 -259 O ATOM 899 CB ALA A 204 3.316 65.781 119.304 1.00 30.32 C ANISOU 899 CB ALA A 204 3196 4218 4107 226 96 -254 C ATOM 900 N SER A 205 2.538 67.916 121.685 1.00 26.38 N ANISOU 900 N SER A 205 2838 3712 3473 384 354 -227 N ATOM 901 CA SER A 205 1.369 68.565 122.271 1.00 26.38 C ANISOU 901 CA SER A 205 2830 3676 3516 487 488 -164 C ATOM 902 C SER A 205 1.628 70.059 122.410 1.00 28.78 C ANISOU 902 C SER A 205 3295 3953 3689 528 503 -225 C ATOM 903 O SER A 205 2.645 70.463 122.976 1.00 36.70 O ANISOU 903 O SER A 205 4459 4953 4532 510 472 -287 O ATOM 904 CB SER A 205 1.047 67.970 123.642 1.00 31.16 C ANISOU 904 CB SER A 205 3461 4279 4100 559 640 -90 C ATOM 905 OG SER A 205 -0.037 68.667 124.222 1.00 32.97 O ANISOU 905 OG SER A 205 3704 4461 4364 685 810 -13 O ATOM 906 N TRP A 206 0.713 70.881 121.901 1.00 31.33 N ANISOU 906 N TRP A 206 3574 4241 4090 580 533 -200 N ATOM 907 CA TRP A 206 0.834 72.316 122.119 1.00 34.52 C ANISOU 907 CA TRP A 206 4141 4607 4368 634 563 -250 C ATOM 908 C TRP A 206 0.093 72.780 123.364 1.00 40.17 C ANISOU 908 C TRP A 206 4961 5275 5028 778 758 -187 C ATOM 909 O TRP A 206 0.357 73.885 123.850 1.00 38.01 O ANISOU 909 O TRP A 206 4893 4953 4596 834 787 -235 O ATOM 910 CB TRP A 206 0.324 73.106 120.901 1.00 33.02 C ANISOU 910 CB TRP A 206 3886 4395 4267 626 493 -265 C ATOM 911 CG TRP A 206 1.060 72.835 119.607 1.00 36.46 C ANISOU 911 CG TRP A 206 4282 4852 4719 513 322 -327 C ATOM 912 CD1 TRP A 206 2.156 72.056 119.444 1.00 36.19 C ANISOU 912 CD1 TRP A 206 4261 4855 4637 428 246 -366 C ATOM 913 CD2 TRP A 206 0.727 73.340 118.298 1.00 31.61 C ANISOU 913 CD2 TRP A 206 3631 4208 4172 492 225 -347 C ATOM 914 NE1 TRP A 206 2.523 72.020 118.120 1.00 39.60 N ANISOU 914 NE1 TRP A 206 4674 5278 5094 368 132 -402 N ATOM 915 CE2 TRP A 206 1.672 72.811 117.396 1.00 36.45 C ANISOU 915 CE2 TRP A 206 4260 4836 4755 405 109 -397 C ATOM 916 CE3 TRP A 206 -0.270 74.198 117.808 1.00 29.53 C ANISOU 916 CE3 TRP A 206 3334 3896 3989 549 229 -320 C ATOM 917 CZ2 TRP A 206 1.653 73.102 116.023 1.00 31.95 C ANISOU 917 CZ2 TRP A 206 3706 4226 4206 379 2 -426 C ATOM 918 CZ3 TRP A 206 -0.290 74.490 116.440 1.00 26.61 C ANISOU 918 CZ3 TRP A 206 2965 3493 3653 509 94 -354 C ATOM 919 CH2 TRP A 206 0.673 73.948 115.567 1.00 27.53 C ANISOU 919 CH2 TRP A 206 3131 3618 3712 428 -14 -410 C ATOM 920 N SER A 207 -0.832 71.979 123.888 1.00 34.14 N ANISOU 920 N SER A 207 4076 4507 4390 848 901 -71 N ATOM 921 CA SER A 207 -1.575 72.379 125.076 1.00 35.97 C ANISOU 921 CA SER A 207 4420 4677 4569 1014 1135 13 C ATOM 922 C SER A 207 -0.923 71.897 126.370 1.00 35.62 C ANISOU 922 C SER A 207 4578 4620 4335 1051 1205 1 C ATOM 923 O SER A 207 -1.280 72.382 127.450 1.00 39.93 O ANISOU 923 O SER A 207 5327 5092 4752 1203 1391 44 O ATOM 924 CB SER A 207 -3.009 71.849 125.000 1.00 37.00 C ANISOU 924 CB SER A 207 4300 4789 4970 1092 1287 182 C ATOM 925 OG SER A 207 -2.966 70.425 124.941 1.00 40.87 O ANISOU 925 OG SER A 207 4620 5321 5586 1011 1239 232 O ATOM 926 N ARG A 208 0.000 70.953 126.293 1.00 35.08 N ANISOU 926 N ARG A 208 4480 4607 4243 930 1066 -49 N ATOM 927 CA ARG A 208 0.728 70.522 127.480 1.00 39.60 C ANISOU 927 CA ARG A 208 5258 5158 4630 952 1089 -69 C ATOM 928 C ARG A 208 1.324 71.723 128.208 1.00 44.23 C ANISOU 928 C ARG A 208 6181 5661 4962 1011 1065 -149 C ATOM 929 O ARG A 208 2.067 72.517 127.623 1.00 45.62 O ANISOU 929 O ARG A 208 6413 5835 5084 925 892 -245 O ATOM 930 CB ARG A 208 1.825 69.545 127.072 1.00 38.07 C ANISOU 930 CB ARG A 208 4980 5034 4452 795 898 -128 C ATOM 931 CG ARG A 208 2.661 68.995 128.211 1.00 49.10 C ANISOU 931 CG ARG A 208 6564 6409 5683 796 879 -147 C ATOM 932 CD ARG A 208 3.586 67.903 127.672 1.00 57.80 C ANISOU 932 CD ARG A 208 7520 7585 6859 650 716 -178 C ATOM 933 NE ARG A 208 4.640 67.508 128.602 1.00 65.56 N ANISOU 933 NE ARG A 208 8675 8543 7692 623 632 -211 N ATOM 934 CZ ARG A 208 5.767 68.192 128.784 1.00 74.31 C ANISOU 934 CZ ARG A 208 9949 9608 8677 564 462 -287 C ATOM 935 NH1 ARG A 208 6.682 67.746 129.640 1.00 75.48 N ANISOU 935 NH1 ARG A 208 10240 9721 8720 535 360 -301 N ATOM 936 NH2 ARG A 208 5.975 69.323 128.115 1.00 72.03 N ANISOU 936 NH2 ARG A 208 9680 9302 8387 532 381 -340 N ATOM 937 N ILE A 209 0.984 71.871 129.481 1.00 39.32 N ANISOU 937 N ILE A 209 5802 4953 4184 1164 1238 -102 N ATOM 938 CA ILE A 209 1.511 72.978 130.269 1.00 47.74 C ANISOU 938 CA ILE A 209 7249 5906 4983 1233 1197 -177 C ATOM 939 C ILE A 209 2.949 72.674 130.661 1.00 56.58 C ANISOU 939 C ILE A 209 8524 7011 5963 1109 952 -268 C ATOM 940 O ILE A 209 3.237 71.652 131.297 1.00 50.91 O ANISOU 940 O ILE A 209 7826 6303 5216 1101 960 -240 O ATOM 941 CB ILE A 209 0.643 73.257 131.500 1.00 45.23 C ANISOU 941 CB ILE A 209 7195 5473 4518 1466 1477 -90 C ATOM 942 CG1 ILE A 209 -0.557 74.104 131.080 1.00 48.53 C ANISOU 942 CG1 ILE A 209 7524 5867 5046 1592 1675 -18 C ATOM 943 CG2 ILE A 209 1.456 73.986 132.562 1.00 49.57 C ANISOU 943 CG2 ILE A 209 8216 5879 4738 1522 1378 -177 C ATOM 944 CD1 ILE A 209 -1.192 74.824 132.210 1.00 55.44 C ANISOU 944 CD1 ILE A 209 8690 6598 5777 1764 1843 64 C ATOM 945 N LYS A 210 3.855 73.567 130.270 1.00 70.16 N ANISOU 945 N LYS A 210 10340 8700 7618 1009 728 -366 N ATOM 946 CA LYS A 210 5.268 73.431 130.586 1.00 74.00 C ANISOU 946 CA LYS A 210 10950 9152 8015 881 467 -433 C ATOM 947 C LYS A 210 5.497 73.819 132.043 1.00 66.56 C ANISOU 947 C LYS A 210 10446 8046 6796 992 449 -450 C ATOM 948 O LYS A 210 5.009 74.858 132.500 1.00 48.02 O ANISOU 948 O LYS A 210 8373 5584 4289 1124 530 -463 O ATOM 949 CB LYS A 210 6.099 74.307 129.646 1.00 73.22 C ANISOU 949 CB LYS A 210 10785 9057 7979 742 248 -503 C ATOM 950 CG LYS A 210 5.432 74.591 128.294 1.00 70.22 C ANISOU 950 CG LYS A 210 10125 8773 7784 719 328 -493 C ATOM 951 CD LYS A 210 6.113 73.871 127.133 1.00 69.60 C ANISOU 951 CD LYS A 210 9743 8805 7896 561 210 -498 C ATOM 952 CE LYS A 210 5.411 72.559 126.769 1.00 74.24 C ANISOU 952 CE LYS A 210 10083 9496 8630 572 342 -435 C ATOM 953 NZ LYS A 210 4.449 72.659 125.613 1.00 70.87 N ANISOU 953 NZ LYS A 210 9440 9126 8361 586 426 -409 N ATOM 954 N GLY A 211 6.215 72.972 132.771 1.00 70.49 N ANISOU 954 N GLY A 211 11037 8521 7228 951 344 -448 N ATOM 955 CA GLY A 211 6.410 73.191 134.190 1.00 80.72 C ANISOU 955 CA GLY A 211 12782 9643 8243 1065 316 -460 C ATOM 956 C GLY A 211 6.929 71.942 134.866 1.00 86.41 C ANISOU 956 C GLY A 211 13517 10373 8940 1032 262 -432 C ATOM 957 O GLY A 211 7.167 70.913 134.228 1.00 84.70 O ANISOU 957 O GLY A 211 12953 10300 8929 917 246 -405 O ATOM 958 N ILE A 212 7.078 72.050 136.193 1.00 92.80 N ANISOU 958 N ILE A 212 14769 11013 9479 1148 236 -439 N ATOM 959 CA ILE A 212 7.751 71.017 136.977 1.00101.84 C ANISOU 959 CA ILE A 212 16008 12125 10561 1112 120 -424 C ATOM 960 C ILE A 212 6.818 69.904 137.436 1.00111.39 C ANISOU 960 C ILE A 212 17152 13395 11777 1247 443 -330 C ATOM 961 O ILE A 212 7.283 68.949 138.075 1.00119.93 O ANISOU 961 O ILE A 212 18302 14460 12807 1229 380 -311 O ATOM 962 CB ILE A 212 8.451 71.632 138.211 1.00102.05 C ANISOU 962 CB ILE A 212 16426 11913 10433 1125 -114 -430 C ATOM 963 CG1 ILE A 212 7.508 71.663 139.418 1.00 99.70 C ANISOU 963 CG1 ILE A 212 16416 11475 9992 1346 141 -348 C ATOM 964 CG2 ILE A 212 8.949 73.040 137.897 1.00102.34 C ANISOU 964 CG2 ILE A 212 16557 11850 10478 1050 -338 -483 C ATOM 965 CD1 ILE A 212 8.191 71.994 140.729 1.00 98.60 C ANISOU 965 CD1 ILE A 212 16698 11081 9684 1380 -77 -349 C ATOM 966 N GLY A 213 5.528 69.979 137.120 1.00110.27 N ANISOU 966 N GLY A 213 16853 13316 11728 1372 775 -254 N ATOM 967 CA GLY A 213 4.566 69.083 137.734 1.00108.42 C ANISOU 967 CA GLY A 213 16569 13089 11535 1510 1080 -128 C ATOM 968 C GLY A 213 4.721 67.633 137.307 1.00 98.22 C ANISOU 968 C GLY A 213 14961 11954 10405 1414 1103 -96 C ATOM 969 O GLY A 213 5.291 67.305 136.266 1.00 98.52 O ANISOU 969 O GLY A 213 14658 12122 10654 1222 916 -138 O ATOM 970 N VAL A 214 4.203 66.748 138.155 1.00 88.91 N ANISOU 970 N VAL A 214 13857 10742 9182 1533 1315 1 N ATOM 971 CA VAL A 214 4.056 65.331 137.838 1.00 85.70 C ANISOU 971 CA VAL A 214 13118 10467 8977 1463 1388 71 C ATOM 972 C VAL A 214 2.576 65.080 137.551 1.00 82.70 C ANISOU 972 C VAL A 214 12486 10139 8798 1583 1749 215 C ATOM 973 O VAL A 214 1.761 65.114 138.489 1.00 80.92 O ANISOU 973 O VAL A 214 12402 9794 8550 1733 1952 331 O ATOM 974 CB VAL A 214 4.574 64.440 138.976 1.00 84.92 C ANISOU 974 CB VAL A 214 13274 10291 8700 1504 1359 88 C ATOM 975 CG1 VAL A 214 4.169 64.995 140.339 1.00 87.23 C ANISOU 975 CG1 VAL A 214 13966 10370 8809 1682 1460 140 C ATOM 976 CG2 VAL A 214 4.087 63.005 138.807 1.00 83.35 C ANISOU 976 CG2 VAL A 214 12752 10204 8714 1479 1520 195 C ATOM 977 N PRO A 215 2.183 64.850 136.294 1.00 76.36 N ANISOU 977 N PRO A 215 11241 9473 8299 1463 1731 236 N ATOM 978 CA PRO A 215 0.754 64.797 135.959 1.00 77.62 C ANISOU 978 CA PRO A 215 11153 9656 8684 1567 2028 384 C ATOM 979 C PRO A 215 0.007 63.745 136.765 1.00 86.67 C ANISOU 979 C PRO A 215 12245 10759 9926 1649 2236 546 C ATOM 980 O PRO A 215 0.561 62.714 137.154 1.00 93.55 O ANISOU 980 O PRO A 215 13144 11655 10744 1609 2196 541 O ATOM 981 CB PRO A 215 0.751 64.450 134.464 1.00 70.99 C ANISOU 981 CB PRO A 215 9870 8958 8145 1373 1857 358 C ATOM 982 CG PRO A 215 2.057 64.927 133.965 1.00 66.01 C ANISOU 982 CG PRO A 215 9318 8358 7403 1218 1530 189 C ATOM 983 CD PRO A 215 3.035 64.751 135.096 1.00 69.84 C ANISOU 983 CD PRO A 215 10151 8764 7620 1238 1430 132 C ATOM 984 N LYS A 216 -1.270 64.038 137.025 1.00 85.76 N ANISOU 984 N LYS A 216 12057 10565 9962 1762 2448 700 N ATOM 985 CA LYS A 216 -2.140 63.086 137.710 1.00 87.89 C ANISOU 985 CA LYS A 216 12239 10777 10379 1838 2649 882 C ATOM 986 C LYS A 216 -2.108 61.725 137.031 1.00 81.73 C ANISOU 986 C LYS A 216 11096 10122 9837 1696 2592 918 C ATOM 987 O LYS A 216 -2.033 60.687 137.699 1.00 90.53 O ANISOU 987 O LYS A 216 12240 11214 10943 1711 2649 980 O ATOM 988 CB LYS A 216 -3.572 63.625 137.742 1.00 93.74 C ANISOU 988 CB LYS A 216 12865 11432 11319 1951 2861 1059 C ATOM 989 CG LYS A 216 -4.027 64.193 136.397 1.00 92.05 C ANISOU 989 CG LYS A 216 12331 11309 11336 1856 2784 1045 C ATOM 990 CD LYS A 216 -5.504 64.548 136.374 1.00 97.53 C ANISOU 990 CD LYS A 216 12864 11919 12275 1949 2980 1246 C ATOM 991 CE LYS A 216 -5.851 65.309 135.097 1.00 98.45 C ANISOU 991 CE LYS A 216 12734 12106 12567 1864 2874 1209 C ATOM 992 NZ LYS A 216 -7.285 65.713 135.039 1.00102.15 N ANISOU 992 NZ LYS A 216 13046 12485 13280 1949 3048 1412 N ATOM 993 N TRP A 217 -2.133 61.716 135.697 1.00 69.67 N ANISOU 993 N TRP A 217 9239 8712 8519 1559 2464 876 N ATOM 994 CA TRP A 217 -2.258 60.463 134.966 1.00 67.79 C ANISOU 994 CA TRP A 217 8646 8566 8546 1424 2390 927 C ATOM 995 C TRP A 217 -0.987 59.628 135.041 1.00 66.68 C ANISOU 995 C TRP A 217 8580 8506 8250 1340 2260 816 C ATOM 996 O TRP A 217 -1.056 58.403 134.926 1.00 63.69 O ANISOU 996 O TRP A 217 8009 8164 8028 1265 2240 880 O ATOM 997 CB TRP A 217 -2.627 60.739 133.508 1.00 62.31 C ANISOU 997 CB TRP A 217 7622 7946 8107 1307 2257 911 C ATOM 998 CG TRP A 217 -4.011 61.277 133.349 1.00 72.96 C ANISOU 998 CG TRP A 217 8831 9215 9676 1366 2368 1056 C ATOM 999 CD1 TRP A 217 -4.364 62.549 132.990 1.00 78.56 C ANISOU 999 CD1 TRP A 217 9579 9899 10370 1417 2385 1032 C ATOM 1000 CD2 TRP A 217 -5.238 60.566 133.565 1.00 72.01 C ANISOU 1000 CD2 TRP A 217 8515 9016 9828 1386 2482 1262 C ATOM 1001 NE1 TRP A 217 -5.734 62.669 132.961 1.00 79.94 N ANISOU 1001 NE1 TRP A 217 9589 9990 10794 1467 2505 1215 N ATOM 1002 CE2 TRP A 217 -6.293 61.467 133.310 1.00 75.08 C ANISOU 1002 CE2 TRP A 217 8827 9336 10363 1449 2564 1362 C ATOM 1003 CE3 TRP A 217 -5.546 59.256 133.944 1.00 74.51 C ANISOU 1003 CE3 TRP A 217 8716 9307 10287 1358 2519 1379 C ATOM 1004 CZ2 TRP A 217 -7.632 61.099 133.422 1.00 73.18 C ANISOU 1004 CZ2 TRP A 217 8394 8996 10413 1483 2683 1584 C ATOM 1005 CZ3 TRP A 217 -6.881 58.891 134.057 1.00 73.98 C ANISOU 1005 CZ3 TRP A 217 8464 9138 10507 1392 2632 1594 C ATOM 1006 CH2 TRP A 217 -7.905 59.810 133.796 1.00 74.76 C ANISOU 1006 CH2 TRP A 217 8486 9165 10756 1454 2713 1699 C ATOM 1007 N THR A 218 0.175 60.259 135.220 1.00 66.62 N ANISOU 1007 N THR A 218 8850 8497 7965 1302 2066 644 N ATOM 1008 CA THR A 218 1.419 59.495 135.264 1.00 67.09 C ANISOU 1008 CA THR A 218 8968 8604 7921 1168 1824 536 C ATOM 1009 C THR A 218 1.470 58.604 136.499 1.00 63.19 C ANISOU 1009 C THR A 218 8657 8049 7302 1261 1964 611 C ATOM 1010 O THR A 218 1.998 57.487 136.445 1.00 63.38 O ANISOU 1010 O THR A 218 8583 8123 7375 1159 1849 602 O ATOM 1011 CB THR A 218 2.625 60.436 135.223 1.00 71.34 C ANISOU 1011 CB THR A 218 9744 9130 8233 1107 1579 365 C ATOM 1012 OG1 THR A 218 2.588 61.319 136.351 1.00 82.08 O ANISOU 1012 OG1 THR A 218 11500 10365 9321 1272 1694 359 O ATOM 1013 CG2 THR A 218 2.630 61.258 133.923 1.00 56.12 C ANISOU 1013 CG2 THR A 218 7625 7265 6435 1009 1441 293 C ATOM 1014 N ALA A 219 0.905 59.072 137.612 1.00 59.75 N ANISOU 1014 N ALA A 219 8504 7498 6698 1466 2226 693 N ATOM 1015 CA ALA A 219 0.847 58.256 138.820 1.00 64.40 C ANISOU 1015 CA ALA A 219 9287 8003 7181 1561 2354 777 C ATOM 1016 C ALA A 219 0.077 56.959 138.578 1.00 63.85 C ANISOU 1016 C ALA A 219 8865 7976 7418 1515 2463 927 C ATOM 1017 O ALA A 219 0.538 55.869 138.945 1.00 62.11 O ANISOU 1017 O ALA A 219 8658 7777 7165 1479 2439 940 O ATOM 1018 CB ALA A 219 0.217 59.062 139.956 1.00 65.05 C ANISOU 1018 CB ALA A 219 9689 7903 7122 1750 2514 842 C ATOM 1019 N VAL A 220 -1.103 57.054 137.960 1.00 54.63 N ANISOU 1019 N VAL A 220 7390 6807 6558 1508 2556 1046 N ATOM 1020 CA VAL A 220 -1.875 55.850 137.679 1.00 62.03 C ANISOU 1020 CA VAL A 220 7998 7758 7811 1445 2604 1192 C ATOM 1021 C VAL A 220 -1.231 55.067 136.541 1.00 57.79 C ANISOU 1021 C VAL A 220 7187 7362 7407 1255 2392 1115 C ATOM 1022 O VAL A 220 -1.316 53.835 136.495 1.00 52.42 O ANISOU 1022 O VAL A 220 6342 6700 6876 1185 2370 1184 O ATOM 1023 CB VAL A 220 -3.350 56.203 137.388 1.00 65.08 C ANISOU 1023 CB VAL A 220 8165 8072 8489 1491 2728 1356 C ATOM 1024 CG1 VAL A 220 -3.463 57.239 136.304 1.00 69.45 C ANISOU 1024 CG1 VAL A 220 8589 8681 9118 1430 2617 1281 C ATOM 1025 CG2 VAL A 220 -4.147 54.966 137.005 1.00 63.20 C ANISOU 1025 CG2 VAL A 220 7591 7829 8595 1406 2721 1507 C ATOM 1026 N GLU A 221 -0.553 55.762 135.628 1.00 53.59 N ANISOU 1026 N GLU A 221 6626 6914 6821 1167 2211 969 N ATOM 1027 CA GLU A 221 0.168 55.097 134.554 1.00 48.61 C ANISOU 1027 CA GLU A 221 5803 6374 6292 965 1907 862 C ATOM 1028 C GLU A 221 1.196 54.113 135.105 1.00 50.05 C ANISOU 1028 C GLU A 221 6118 6575 6324 913 1798 803 C ATOM 1029 O GLU A 221 1.311 52.980 134.621 1.00 46.06 O ANISOU 1029 O GLU A 221 5421 6110 5971 803 1693 822 O ATOM 1030 CB GLU A 221 0.835 56.153 133.680 1.00 49.32 C ANISOU 1030 CB GLU A 221 5930 6511 6300 885 1692 699 C ATOM 1031 CG GLU A 221 1.770 55.637 132.617 1.00 53.86 C ANISOU 1031 CG GLU A 221 6381 7164 6921 707 1402 579 C ATOM 1032 CD GLU A 221 2.410 56.766 131.820 1.00 66.62 C ANISOU 1032 CD GLU A 221 8047 8812 8455 650 1232 440 C ATOM 1033 OE1 GLU A 221 2.505 57.899 132.346 1.00 74.47 O ANISOU 1033 OE1 GLU A 221 9247 9767 9281 734 1289 401 O ATOM 1034 OE2 GLU A 221 2.814 56.523 130.663 1.00 69.98 O ANISOU 1034 OE2 GLU A 221 8323 9288 8979 528 1045 375 O ATOM 1035 N ILE A 222 1.926 54.519 136.144 1.00 44.65 N ANISOU 1035 N ILE A 222 5779 5846 5342 995 1813 738 N ATOM 1036 CA ILE A 222 2.980 53.680 136.695 1.00 46.13 C ANISOU 1036 CA ILE A 222 6108 6038 5380 945 1679 679 C ATOM 1037 C ILE A 222 2.390 52.540 137.515 1.00 45.78 C ANISOU 1037 C ILE A 222 6053 5952 5389 1021 1885 827 C ATOM 1038 O ILE A 222 2.866 51.402 137.443 1.00 45.09 O ANISOU 1038 O ILE A 222 5877 5900 5353 931 1778 823 O ATOM 1039 CB ILE A 222 3.960 54.543 137.514 1.00 54.20 C ANISOU 1039 CB ILE A 222 7516 6999 6079 998 1577 565 C ATOM 1040 CG1 ILE A 222 4.640 55.563 136.587 1.00 48.01 C ANISOU 1040 CG1 ILE A 222 6693 6260 5287 894 1347 428 C ATOM 1041 CG2 ILE A 222 4.986 53.671 138.218 1.00 54.74 C ANISOU 1041 CG2 ILE A 222 7744 7051 6004 961 1440 527 C ATOM 1042 CD1 ILE A 222 5.991 56.030 137.049 1.00 51.06 C ANISOU 1042 CD1 ILE A 222 7347 6606 5449 854 1109 307 C ATOM 1043 N VAL A 223 1.339 52.813 138.288 1.00 42.34 N ANISOU 1043 N VAL A 223 5701 5432 4953 1194 2200 972 N ATOM 1044 CA VAL A 223 0.672 51.742 139.023 1.00 45.79 C ANISOU 1044 CA VAL A 223 6098 5820 5481 1275 2434 1145 C ATOM 1045 C VAL A 223 0.199 50.656 138.065 1.00 47.75 C ANISOU 1045 C VAL A 223 5927 6132 6082 1130 2361 1223 C ATOM 1046 O VAL A 223 0.358 49.460 138.333 1.00 48.27 O ANISOU 1046 O VAL A 223 5942 6199 6198 1088 2350 1274 O ATOM 1047 CB VAL A 223 -0.489 52.308 139.861 1.00 47.50 C ANISOU 1047 CB VAL A 223 6428 5888 5729 1445 2659 1269 C ATOM 1048 CG1 VAL A 223 -1.319 51.173 140.448 1.00 49.46 C ANISOU 1048 CG1 VAL A 223 6564 6060 6167 1491 2812 1445 C ATOM 1049 CG2 VAL A 223 0.053 53.185 140.966 1.00 53.31 C ANISOU 1049 CG2 VAL A 223 7637 6523 6095 1592 2696 1189 C ATOM 1050 N LEU A 224 -0.348 51.054 136.914 1.00 46.59 N ANISOU 1050 N LEU A 224 5500 6025 6175 1047 2279 1227 N ATOM 1051 CA LEU A 224 -0.842 50.077 135.948 1.00 49.04 C ANISOU 1051 CA LEU A 224 5457 6361 6816 903 2151 1293 C ATOM 1052 C LEU A 224 0.301 49.277 135.334 1.00 48.20 C ANISOU 1052 C LEU A 224 5329 6332 6654 745 1866 1152 C ATOM 1053 O LEU A 224 0.175 48.066 135.112 1.00 47.10 O ANISOU 1053 O LEU A 224 5030 6191 6677 666 1809 1216 O ATOM 1054 CB LEU A 224 -1.646 50.786 134.859 1.00 50.39 C ANISOU 1054 CB LEU A 224 5408 6525 7214 848 2061 1305 C ATOM 1055 CG LEU A 224 -2.961 51.385 135.374 1.00 57.26 C ANISOU 1055 CG LEU A 224 6281 7277 8199 971 2249 1450 C ATOM 1056 CD1 LEU A 224 -3.718 52.089 134.259 1.00 54.28 C ANISOU 1056 CD1 LEU A 224 5694 6890 8039 910 2141 1463 C ATOM 1057 CD2 LEU A 224 -3.812 50.294 136.017 1.00 61.10 C ANISOU 1057 CD2 LEU A 224 6681 7665 8870 1005 2367 1634 C ATOM 1058 N ILE A 225 1.411 49.948 135.032 1.00 40.79 N ANISOU 1058 N ILE A 225 4551 5446 5500 697 1672 965 N ATOM 1059 CA ILE A 225 2.606 49.269 134.548 1.00 40.13 C ANISOU 1059 CA ILE A 225 4479 5423 5347 570 1418 837 C ATOM 1060 C ILE A 225 3.019 48.170 135.515 1.00 35.33 C ANISOU 1060 C ILE A 225 3984 4794 4647 594 1465 879 C ATOM 1061 O ILE A 225 3.314 47.042 135.109 1.00 35.19 O ANISOU 1061 O ILE A 225 3846 4798 4726 501 1348 880 O ATOM 1062 CB ILE A 225 3.741 50.290 134.346 1.00 40.81 C ANISOU 1062 CB ILE A 225 4741 5547 5219 546 1253 667 C ATOM 1063 CG1 ILE A 225 3.460 51.193 133.150 1.00 35.70 C ANISOU 1063 CG1 ILE A 225 3956 4928 4680 494 1166 614 C ATOM 1064 CG2 ILE A 225 5.090 49.579 134.185 1.00 37.96 C ANISOU 1064 CG2 ILE A 225 4426 5227 4768 451 1042 568 C ATOM 1065 CD1 ILE A 225 4.541 52.230 132.951 1.00 33.75 C ANISOU 1065 CD1 ILE A 225 3866 4709 4250 469 1018 468 C ATOM 1066 N TRP A 226 3.045 48.481 136.809 1.00 38.14 N ANISOU 1066 N TRP A 226 4598 5094 4800 729 1634 914 N ATOM 1067 CA TRP A 226 3.492 47.501 137.794 1.00 40.54 C ANISOU 1067 CA TRP A 226 5054 5366 4984 762 1671 948 C ATOM 1068 C TRP A 226 2.462 46.396 137.985 1.00 41.18 C ANISOU 1068 C TRP A 226 4947 5411 5289 783 1856 1130 C ATOM 1069 O TRP A 226 2.826 45.223 138.099 1.00 40.53 O ANISOU 1069 O TRP A 226 4828 5336 5236 724 1789 1146 O ATOM 1070 CB TRP A 226 3.805 48.208 139.116 1.00 41.75 C ANISOU 1070 CB TRP A 226 5593 5441 4830 912 1783 931 C ATOM 1071 CG TRP A 226 5.117 48.922 139.065 1.00 42.94 C ANISOU 1071 CG TRP A 226 5938 5609 4768 857 1522 757 C ATOM 1072 CD1 TRP A 226 5.474 49.935 138.210 1.00 39.81 C ANISOU 1072 CD1 TRP A 226 5484 5258 4385 789 1368 649 C ATOM 1073 CD2 TRP A 226 6.270 48.653 139.872 1.00 42.05 C ANISOU 1073 CD2 TRP A 226 6090 5458 4431 857 1367 687 C ATOM 1074 NE1 TRP A 226 6.774 50.319 138.447 1.00 36.41 N ANISOU 1074 NE1 TRP A 226 5249 4817 3770 744 1134 527 N ATOM 1075 CE2 TRP A 226 7.287 49.549 139.460 1.00 42.18 C ANISOU 1075 CE2 TRP A 226 6175 5493 4358 781 1115 548 C ATOM 1076 CE3 TRP A 226 6.540 47.747 140.907 1.00 41.31 C ANISOU 1076 CE3 TRP A 226 6179 5305 4211 912 1408 736 C ATOM 1077 CZ2 TRP A 226 8.547 49.567 140.052 1.00 45.44 C ANISOU 1077 CZ2 TRP A 226 6814 5860 4591 752 889 470 C ATOM 1078 CZ3 TRP A 226 7.795 47.761 141.490 1.00 42.50 C ANISOU 1078 CZ3 TRP A 226 6576 5414 4157 888 1177 644 C ATOM 1079 CH2 TRP A 226 8.783 48.662 141.063 1.00 41.88 C ANISOU 1079 CH2 TRP A 226 6541 5348 4022 805 912 517 C ATOM 1080 N VAL A 227 1.169 46.740 138.014 1.00 40.70 N ANISOU 1080 N VAL A 227 4753 5302 5410 864 2090 1282 N ATOM 1081 CA VAL A 227 0.152 45.706 138.199 1.00 40.38 C ANISOU 1081 CA VAL A 227 4501 5210 5632 879 2266 1487 C ATOM 1082 C VAL A 227 0.145 44.747 137.016 1.00 42.81 C ANISOU 1082 C VAL A 227 4510 5558 6199 694 2026 1475 C ATOM 1083 O VAL A 227 0.129 43.525 137.192 1.00 45.12 O ANISOU 1083 O VAL A 227 4728 5829 6585 649 2015 1547 O ATOM 1084 CB VAL A 227 -1.231 46.340 138.429 1.00 45.81 C ANISOU 1084 CB VAL A 227 5127 5790 6488 980 2425 1611 C ATOM 1085 CG1 VAL A 227 -2.332 45.262 138.458 1.00 39.23 C ANISOU 1085 CG1 VAL A 227 4063 4866 5975 958 2470 1792 C ATOM 1086 CG2 VAL A 227 -1.242 47.124 139.731 1.00 42.54 C ANISOU 1086 CG2 VAL A 227 5065 5293 5804 1178 2638 1619 C ATOM 1087 N VAL A 228 0.181 45.289 135.796 1.00 39.22 N ANISOU 1087 N VAL A 228 3910 5148 5842 593 1826 1381 N ATOM 1088 CA VAL A 228 0.210 44.463 134.591 1.00 39.52 C ANISOU 1088 CA VAL A 228 3729 5201 6088 431 1575 1354 C ATOM 1089 C VAL A 228 1.460 43.583 134.562 1.00 35.52 C ANISOU 1089 C VAL A 228 3344 4739 5412 357 1392 1226 C ATOM 1090 O VAL A 228 1.384 42.388 134.264 1.00 39.34 O ANISOU 1090 O VAL A 228 3715 5198 6036 278 1301 1275 O ATOM 1091 CB VAL A 228 0.115 45.357 133.338 1.00 44.07 C ANISOU 1091 CB VAL A 228 4203 5804 6737 362 1403 1261 C ATOM 1092 CG1 VAL A 228 0.691 44.648 132.117 1.00 40.22 C ANISOU 1092 CG1 VAL A 228 3643 5335 6304 214 1104 1155 C ATOM 1093 CG2 VAL A 228 -1.336 45.751 133.091 1.00 48.99 C ANISOU 1093 CG2 VAL A 228 4624 6348 7640 388 1500 1417 C ATOM 1094 N SER A 229 2.631 44.165 134.849 1.00 40.26 N ANISOU 1094 N SER A 229 4171 5396 5729 381 1322 1071 N ATOM 1095 CA SER A 229 3.865 43.376 134.858 1.00 35.23 C ANISOU 1095 CA SER A 229 3635 4796 4953 321 1156 969 C ATOM 1096 C SER A 229 3.760 42.210 135.833 1.00 36.06 C ANISOU 1096 C SER A 229 3785 4860 5056 357 1267 1074 C ATOM 1097 O SER A 229 4.179 41.086 135.523 1.00 36.62 O ANISOU 1097 O SER A 229 3802 4934 5177 281 1143 1063 O ATOM 1098 CB SER A 229 5.065 44.255 135.226 1.00 31.93 C ANISOU 1098 CB SER A 229 3445 4421 4265 352 1079 827 C ATOM 1099 OG SER A 229 5.246 45.329 134.311 1.00 33.67 O ANISOU 1099 OG SER A 229 3627 4678 4488 316 976 731 O ATOM 1100 N VAL A 230 3.178 42.458 137.010 1.00 34.90 N ANISOU 1100 N VAL A 230 3755 4662 4845 484 1515 1184 N ATOM 1101 CA VAL A 230 3.007 41.409 138.004 1.00 39.53 C ANISOU 1101 CA VAL A 230 4404 5196 5420 537 1656 1300 C ATOM 1102 C VAL A 230 2.039 40.343 137.500 1.00 43.05 C ANISOU 1102 C VAL A 230 4566 5599 6191 465 1680 1450 C ATOM 1103 O VAL A 230 2.329 39.144 137.577 1.00 37.96 O ANISOU 1103 O VAL A 230 3898 4942 5583 410 1610 1473 O ATOM 1104 CB VAL A 230 2.556 42.019 139.345 1.00 40.31 C ANISOU 1104 CB VAL A 230 4729 5229 5359 717 1945 1393 C ATOM 1105 CG1 VAL A 230 2.045 40.939 140.285 1.00 35.84 C ANISOU 1105 CG1 VAL A 230 4185 4589 4844 787 2153 1563 C ATOM 1106 CG2 VAL A 230 3.715 42.776 139.981 1.00 39.09 C ANISOU 1106 CG2 VAL A 230 4913 5085 4854 772 1851 1239 C ATOM 1107 N VAL A 231 0.887 40.753 136.954 1.00 40.89 N ANISOU 1107 N VAL A 231 4071 5290 6174 458 1755 1560 N ATOM 1108 CA VAL A 231 -0.109 39.767 136.528 1.00 39.71 C ANISOU 1108 CA VAL A 231 3643 5070 6374 383 1755 1731 C ATOM 1109 C VAL A 231 0.446 38.879 135.414 1.00 41.91 C ANISOU 1109 C VAL A 231 3834 5365 6723 222 1434 1627 C ATOM 1110 O VAL A 231 0.244 37.661 135.418 1.00 40.31 O ANISOU 1110 O VAL A 231 3541 5108 6666 161 1389 1715 O ATOM 1111 CB VAL A 231 -1.414 40.460 136.090 1.00 46.65 C ANISOU 1111 CB VAL A 231 4361 5875 7491 402 1776 1816 C ATOM 1112 CG1 VAL A 231 -2.364 39.446 135.481 1.00 44.86 C ANISOU 1112 CG1 VAL A 231 3903 5542 7599 304 1635 1938 C ATOM 1113 CG2 VAL A 231 -2.075 41.140 137.270 1.00 49.86 C ANISOU 1113 CG2 VAL A 231 4905 6219 7822 583 2061 1912 C ATOM 1114 N LEU A 232 1.157 39.475 134.447 1.00 37.10 N ANISOU 1114 N LEU A 232 3270 4818 6007 160 1218 1446 N ATOM 1115 CA LEU A 232 1.691 38.722 133.318 1.00 38.10 C ANISOU 1115 CA LEU A 232 3356 4944 6175 35 937 1348 C ATOM 1116 C LEU A 232 2.748 37.712 133.734 1.00 41.65 C ANISOU 1116 C LEU A 232 3950 5418 6457 26 879 1283 C ATOM 1117 O LEU A 232 3.012 36.769 132.983 1.00 38.30 O ANISOU 1117 O LEU A 232 3492 4962 6099 -61 693 1252 O ATOM 1118 CB LEU A 232 2.300 39.671 132.281 1.00 37.77 C ANISOU 1118 CB LEU A 232 3366 4959 6025 3 771 1178 C ATOM 1119 CG LEU A 232 1.342 40.568 131.496 1.00 38.93 C ANISOU 1119 CG LEU A 232 3366 5074 6353 -16 743 1215 C ATOM 1120 CD1 LEU A 232 2.094 41.375 130.481 1.00 37.85 C ANISOU 1120 CD1 LEU A 232 3312 4989 6078 -45 578 1040 C ATOM 1121 CD2 LEU A 232 0.276 39.707 130.816 1.00 39.68 C ANISOU 1121 CD2 LEU A 232 3249 5052 6775 -109 623 1350 C ATOM 1122 N ALA A 233 3.362 37.892 134.902 1.00 40.30 N ANISOU 1122 N ALA A 233 3959 5289 6063 118 1022 1263 N ATOM 1123 CA ALA A 233 4.372 36.970 135.396 1.00 37.26 C ANISOU 1123 CA ALA A 233 3712 4922 5525 116 966 1213 C ATOM 1124 C ALA A 233 3.788 35.804 136.191 1.00 39.33 C ANISOU 1124 C ALA A 233 3937 5115 5894 132 1092 1371 C ATOM 1125 O ALA A 233 4.535 34.877 136.528 1.00 35.99 O ANISOU 1125 O ALA A 233 3608 4694 5373 121 1033 1342 O ATOM 1126 CB ALA A 233 5.391 37.734 136.254 1.00 30.95 C ANISOU 1126 CB ALA A 233 3147 4180 4434 200 1007 1114 C ATOM 1127 N VAL A 234 2.475 35.824 136.484 1.00 32.91 N ANISOU 1127 N VAL A 234 2974 4232 5298 159 1270 1550 N ATOM 1128 CA VAL A 234 1.887 34.763 137.310 1.00 40.90 C ANISOU 1128 CA VAL A 234 3943 5167 6429 185 1426 1727 C ATOM 1129 C VAL A 234 2.135 33.369 136.760 1.00 41.62 C ANISOU 1129 C VAL A 234 3963 5220 6631 71 1229 1726 C ATOM 1130 O VAL A 234 2.380 32.452 137.565 1.00 41.30 O ANISOU 1130 O VAL A 234 4007 5155 6532 99 1303 1783 O ATOM 1131 CB VAL A 234 0.396 35.054 137.559 1.00 47.19 C ANISOU 1131 CB VAL A 234 4541 5883 7505 229 1651 1948 C ATOM 1132 CG1 VAL A 234 -0.300 33.821 138.128 1.00 46.61 C ANISOU 1132 CG1 VAL A 234 4370 5708 7630 228 1753 2137 C ATOM 1133 CG2 VAL A 234 0.244 36.231 138.520 1.00 48.17 C ANISOU 1133 CG2 VAL A 234 4826 6026 7451 393 1924 1972 C ATOM 1134 N PRO A 235 2.077 33.108 135.441 1.00 38.40 N ANISOU 1134 N PRO A 235 3433 4790 6369 -49 978 1668 N ATOM 1135 CA PRO A 235 2.328 31.730 134.976 1.00 38.56 C ANISOU 1135 CA PRO A 235 3435 4750 6467 -141 794 1668 C ATOM 1136 C PRO A 235 3.665 31.160 135.423 1.00 34.58 C ANISOU 1136 C PRO A 235 3140 4306 5692 -108 755 1548 C ATOM 1137 O PRO A 235 3.771 29.936 135.560 1.00 39.50 O ANISOU 1137 O PRO A 235 3771 4874 6362 -145 703 1596 O ATOM 1138 CB PRO A 235 2.248 31.856 133.448 1.00 41.98 C ANISOU 1138 CB PRO A 235 3796 5148 7005 -243 525 1580 C ATOM 1139 CG PRO A 235 1.293 32.975 133.234 1.00 39.22 C ANISOU 1139 CG PRO A 235 3302 4790 6808 -231 600 1646 C ATOM 1140 CD PRO A 235 1.588 33.958 134.336 1.00 39.85 C ANISOU 1140 CD PRO A 235 3492 4967 6682 -101 857 1630 C ATOM 1141 N GLU A 236 4.683 31.999 135.660 1.00 36.96 N ANISOU 1141 N GLU A 236 3604 4709 5732 -44 766 1404 N ATOM 1142 CA GLU A 236 5.961 31.491 136.163 1.00 35.76 C ANISOU 1142 CA GLU A 236 3630 4602 5355 -12 721 1314 C ATOM 1143 C GLU A 236 5.800 30.870 137.545 1.00 35.57 C ANISOU 1143 C GLU A 236 3691 4546 5278 56 901 1429 C ATOM 1144 O GLU A 236 6.377 29.818 137.833 1.00 33.20 O ANISOU 1144 O GLU A 236 3461 4228 4924 47 846 1428 O ATOM 1145 CB GLU A 236 7.003 32.614 136.207 1.00 31.09 C ANISOU 1145 CB GLU A 236 3171 4103 4539 37 687 1168 C ATOM 1146 CG GLU A 236 7.410 33.133 134.831 1.00 31.65 C ANISOU 1146 CG GLU A 236 3189 4206 4631 -19 515 1049 C ATOM 1147 CD GLU A 236 8.369 32.194 134.107 1.00 37.15 C ANISOU 1147 CD GLU A 236 3924 4895 5296 -56 348 976 C ATOM 1148 OE1 GLU A 236 9.595 32.427 134.168 1.00 36.21 O ANISOU 1148 OE1 GLU A 236 3901 4831 5026 -25 296 886 O ATOM 1149 OE2 GLU A 236 7.902 31.203 133.494 1.00 39.01 O ANISOU 1149 OE2 GLU A 236 4100 5054 5669 -113 267 1020 O ATOM 1150 N ALA A 237 5.014 31.513 138.416 1.00 40.47 N ANISOU 1150 N ALA A 237 4324 5148 5905 139 1130 1536 N ATOM 1151 CA ALA A 237 4.824 31.005 139.770 1.00 39.33 C ANISOU 1151 CA ALA A 237 4301 4956 5686 230 1335 1655 C ATOM 1152 C ALA A 237 3.970 29.741 139.787 1.00 41.56 C ANISOU 1152 C ALA A 237 4425 5147 6219 178 1387 1826 C ATOM 1153 O ALA A 237 4.093 28.929 140.709 1.00 47.35 O ANISOU 1153 O ALA A 237 5264 5840 6888 227 1491 1903 O ATOM 1154 CB ALA A 237 4.190 32.091 140.648 1.00 38.21 C ANISOU 1154 CB ALA A 237 4248 4799 5469 358 1595 1732 C ATOM 1155 N ILE A 238 3.085 29.570 138.802 1.00 41.59 N ANISOU 1155 N ILE A 238 4183 5102 6518 79 1305 1896 N ATOM 1156 CA ILE A 238 2.290 28.350 138.734 1.00 46.29 C ANISOU 1156 CA ILE A 238 4614 5589 7387 9 1303 2065 C ATOM 1157 C ILE A 238 3.098 27.221 138.120 1.00 43.90 C ANISOU 1157 C ILE A 238 4361 5274 7044 -83 1049 1964 C ATOM 1158 O ILE A 238 2.992 26.069 138.551 1.00 43.66 O ANISOU 1158 O ILE A 238 4330 5176 7083 -101 1069 2061 O ATOM 1159 CB ILE A 238 0.993 28.584 137.944 1.00 47.82 C ANISOU 1159 CB ILE A 238 4527 5702 7941 -69 1276 2200 C ATOM 1160 CG1 ILE A 238 0.201 29.747 138.545 1.00 53.70 C ANISOU 1160 CG1 ILE A 238 5218 6455 8730 40 1555 2311 C ATOM 1161 CG2 ILE A 238 0.164 27.272 137.890 1.00 43.28 C ANISOU 1161 CG2 ILE A 238 3769 4988 7687 -159 1242 2396 C ATOM 1162 CD1 ILE A 238 -0.962 30.195 137.697 1.00 53.16 C ANISOU 1162 CD1 ILE A 238 4920 6320 8959 -6 1456 2366 C ATOM 1163 N GLY A 239 3.921 27.534 137.114 1.00 38.49 N ANISOU 1163 N GLY A 239 3730 4648 6245 -129 823 1776 N ATOM 1164 CA GLY A 239 4.536 26.484 136.322 1.00 41.16 C ANISOU 1164 CA GLY A 239 4107 4950 6582 -207 588 1698 C ATOM 1165 C GLY A 239 5.825 25.925 136.879 1.00 38.28 C ANISOU 1165 C GLY A 239 3938 4640 5966 -153 573 1603 C ATOM 1166 O GLY A 239 6.109 24.745 136.686 1.00 35.50 O ANISOU 1166 O GLY A 239 3618 4230 5642 -194 465 1610 O ATOM 1167 N PHE A 240 6.639 26.752 137.536 1.00 37.89 N ANISOU 1167 N PHE A 240 4025 4689 5681 -65 656 1516 N ATOM 1168 CA PHE A 240 7.885 26.264 138.109 1.00 33.66 C ANISOU 1168 CA PHE A 240 3663 4193 4932 -17 618 1441 C ATOM 1169 C PHE A 240 7.603 25.387 139.325 1.00 40.48 C ANISOU 1169 C PHE A 240 4593 5002 5786 26 763 1570 C ATOM 1170 O PHE A 240 6.656 25.618 140.083 1.00 38.92 O ANISOU 1170 O PHE A 240 4366 4767 5656 68 966 1704 O ATOM 1171 CB PHE A 240 8.794 27.426 138.515 1.00 35.06 C ANISOU 1171 CB PHE A 240 3969 4464 4889 55 631 1330 C ATOM 1172 CG PHE A 240 9.718 27.898 137.424 1.00 32.80 C ANISOU 1172 CG PHE A 240 3673 4236 4556 27 457 1185 C ATOM 1173 CD1 PHE A 240 9.260 28.747 136.424 1.00 31.65 C ANISOU 1173 CD1 PHE A 240 3422 4105 4497 -11 417 1142 C ATOM 1174 CD2 PHE A 240 11.055 27.508 137.415 1.00 37.83 C ANISOU 1174 CD2 PHE A 240 4403 4902 5070 47 346 1107 C ATOM 1175 CE1 PHE A 240 10.119 29.203 135.426 1.00 29.34 C ANISOU 1175 CE1 PHE A 240 3136 3856 4154 -23 285 1021 C ATOM 1176 CE2 PHE A 240 11.920 27.947 136.433 1.00 29.32 C ANISOU 1176 CE2 PHE A 240 3307 3866 3968 38 224 1002 C ATOM 1177 CZ PHE A 240 11.450 28.808 135.428 1.00 27.61 C ANISOU 1177 CZ PHE A 240 3003 3664 3822 6 202 957 C ATOM 1178 N ASP A 241 8.437 24.368 139.502 1.00 34.02 N ANISOU 1178 N ASP A 241 3870 4172 4884 26 673 1540 N ATOM 1179 CA ASP A 241 8.327 23.487 140.655 1.00 38.47 C ANISOU 1179 CA ASP A 241 4526 4682 5408 71 794 1650 C ATOM 1180 C ASP A 241 9.609 22.668 140.742 1.00 36.64 C ANISOU 1180 C ASP A 241 4424 4466 5034 83 653 1567 C ATOM 1181 O ASP A 241 10.425 22.651 139.820 1.00 31.99 O ANISOU 1181 O ASP A 241 3819 3912 4422 53 482 1451 O ATOM 1182 CB ASP A 241 7.097 22.575 140.550 1.00 47.95 C ANISOU 1182 CB ASP A 241 5574 5776 6871 8 861 1818 C ATOM 1183 CG ASP A 241 6.488 22.255 141.904 1.00 59.84 C ANISOU 1183 CG ASP A 241 7141 7225 8371 85 1110 1985 C ATOM 1184 OD1 ASP A 241 7.206 22.341 142.918 1.00 56.05 O ANISOU 1184 OD1 ASP A 241 6875 6771 7648 182 1182 1953 O ATOM 1185 OD2 ASP A 241 5.285 21.917 141.954 1.00 67.14 O ANISOU 1185 OD2 ASP A 241 7905 8063 9543 53 1233 2161 O ATOM 1186 N ILE A 242 9.770 21.986 141.855 1.00 40.05 N ANISOU 1186 N ILE A 242 4984 4860 5374 138 739 1639 N ATOM 1187 CA ILE A 242 10.880 21.063 142.036 1.00 45.41 C ANISOU 1187 CA ILE A 242 5773 5535 5944 151 615 1589 C ATOM 1188 C ILE A 242 10.421 19.679 141.610 1.00 46.50 C ANISOU 1188 C ILE A 242 5831 5589 6250 84 576 1666 C ATOM 1189 O ILE A 242 9.385 19.189 142.071 1.00 42.55 O ANISOU 1189 O ILE A 242 5279 5012 5876 69 711 1811 O ATOM 1190 CB ILE A 242 11.364 21.062 143.494 1.00 44.08 C ANISOU 1190 CB ILE A 242 5823 5356 5567 249 699 1619 C ATOM 1191 CG1 ILE A 242 11.859 22.463 143.882 1.00 47.82 C ANISOU 1191 CG1 ILE A 242 6410 5889 5870 310 692 1536 C ATOM 1192 CG2 ILE A 242 12.437 19.992 143.702 1.00 43.55 C ANISOU 1192 CG2 ILE A 242 5853 5273 5423 260 565 1590 C ATOM 1193 CD1 ILE A 242 12.382 22.544 145.302 1.00 51.41 C ANISOU 1193 CD1 ILE A 242 7135 6306 6093 411 728 1555 C ATOM 1194 N ILE A 243 11.169 19.063 140.703 1.00 41.84 N ANISOU 1194 N ILE A 243 5230 4995 5671 49 397 1582 N ATOM 1195 CA ILE A 243 10.968 17.665 140.356 1.00 49.74 C ANISOU 1195 CA ILE A 243 6215 5901 6784 -2 326 1638 C ATOM 1196 C ILE A 243 12.213 16.896 140.770 1.00 43.51 C ANISOU 1196 C ILE A 243 5567 5121 5845 56 256 1593 C ATOM 1197 O ILE A 243 13.287 17.463 140.993 1.00 44.36 O ANISOU 1197 O ILE A 243 5746 5304 5803 117 215 1508 O ATOM 1198 CB ILE A 243 10.691 17.452 138.856 1.00 50.18 C ANISOU 1198 CB ILE A 243 6179 5905 6981 -81 170 1589 C ATOM 1199 CG1 ILE A 243 11.949 17.800 138.063 1.00 43.58 C ANISOU 1199 CG1 ILE A 243 5407 5133 6017 -37 51 1441 C ATOM 1200 CG2 ILE A 243 9.472 18.259 138.407 1.00 51.92 C ANISOU 1200 CG2 ILE A 243 6249 6109 7370 -144 209 1637 C ATOM 1201 CD1 ILE A 243 11.936 17.330 136.655 1.00 55.05 C ANISOU 1201 CD1 ILE A 243 6864 6510 7545 -78 -101 1388 C ATOM 1202 N THR A 244 12.067 15.585 140.861 1.00 38.43 N ANISOU 1202 N THR A 244 4953 4388 5262 32 229 1661 N ATOM 1203 CA THR A 244 13.182 14.702 141.162 1.00 46.24 C ANISOU 1203 CA THR A 244 6065 5369 6137 85 156 1631 C ATOM 1204 C THR A 244 13.383 13.731 140.011 1.00 42.81 C ANISOU 1204 C THR A 244 5626 4857 5782 48 14 1597 C ATOM 1205 O THR A 244 12.418 13.289 139.379 1.00 47.27 O ANISOU 1205 O THR A 244 6128 5329 6505 -33 -25 1646 O ATOM 1206 CB THR A 244 12.949 13.906 142.455 1.00 48.11 C ANISOU 1206 CB THR A 244 6395 5551 6332 113 261 1746 C ATOM 1207 OG1 THR A 244 11.817 13.053 142.277 1.00 55.55 O ANISOU 1207 OG1 THR A 244 7261 6386 7460 38 297 1862 O ATOM 1208 CG2 THR A 244 12.695 14.837 143.628 1.00 52.97 C ANISOU 1208 CG2 THR A 244 7077 6212 6838 173 417 1787 C ATOM 1209 N MET A 245 14.635 13.380 139.756 1.00 43.09 N ANISOU 1209 N MET A 245 5741 4913 5718 113 -70 1525 N ATOM 1210 CA MET A 245 14.917 12.293 138.837 1.00 46.11 C ANISOU 1210 CA MET A 245 6181 5200 6139 111 -178 1506 C ATOM 1211 C MET A 245 16.174 11.579 139.296 1.00 43.26 C ANISOU 1211 C MET A 245 5919 4846 5670 201 -202 1498 C ATOM 1212 O MET A 245 17.015 12.138 140.007 1.00 39.96 O ANISOU 1212 O MET A 245 5507 4515 5159 262 -179 1481 O ATOM 1213 CB MET A 245 15.076 12.783 137.385 1.00 48.41 C ANISOU 1213 CB MET A 245 6456 5484 6453 112 -260 1413 C ATOM 1214 CG MET A 245 16.489 13.182 136.986 1.00 46.16 C ANISOU 1214 CG MET A 245 6202 5269 6067 215 -272 1333 C ATOM 1215 SD MET A 245 16.667 13.417 135.190 1.00 48.69 S ANISOU 1215 SD MET A 245 6570 5532 6399 244 -342 1245 S ATOM 1216 CE MET A 245 14.941 13.338 134.652 1.00 44.46 C ANISOU 1216 CE MET A 245 6011 4887 5993 108 -418 1271 C ATOM 1217 N ASP A 246 16.280 10.321 138.891 1.00 44.76 N ANISOU 1217 N ASP A 246 6194 4929 5885 207 -266 1517 N ATOM 1218 CA ASP A 246 17.545 9.611 138.939 1.00 46.12 C ANISOU 1218 CA ASP A 246 6455 5092 5978 305 -301 1502 C ATOM 1219 C ASP A 246 18.220 9.789 137.587 1.00 45.32 C ANISOU 1219 C ASP A 246 6377 4974 5869 368 -346 1424 C ATOM 1220 O ASP A 246 17.615 9.531 136.542 1.00 47.30 O ANISOU 1220 O ASP A 246 6680 5130 6163 334 -401 1397 O ATOM 1221 CB ASP A 246 17.356 8.136 139.263 1.00 60.20 C ANISOU 1221 CB ASP A 246 8341 6758 7775 297 -330 1569 C ATOM 1222 CG ASP A 246 18.673 7.419 139.388 1.00 73.63 C ANISOU 1222 CG ASP A 246 10126 8449 9401 409 -355 1565 C ATOM 1223 OD1 ASP A 246 19.201 6.971 138.347 1.00 73.19 O ANISOU 1223 OD1 ASP A 246 10139 8329 9341 471 -397 1525 O ATOM 1224 OD2 ASP A 246 19.203 7.352 140.522 1.00 80.66 O ANISOU 1224 OD2 ASP A 246 11026 9388 10235 445 -331 1606 O ATOM 1225 N TYR A 247 19.439 10.291 137.603 1.00 40.61 N ANISOU 1225 N TYR A 247 5749 4457 5226 462 -326 1397 N ATOM 1226 CA TYR A 247 20.174 10.580 136.382 1.00 39.12 C ANISOU 1226 CA TYR A 247 5572 4256 5034 547 -322 1345 C ATOM 1227 C TYR A 247 21.437 9.739 136.479 1.00 42.11 C ANISOU 1227 C TYR A 247 6006 4602 5394 671 -313 1384 C ATOM 1228 O TYR A 247 22.357 10.078 137.229 1.00 45.19 O ANISOU 1228 O TYR A 247 6311 5069 5791 717 -306 1419 O ATOM 1229 CB TYR A 247 20.449 12.089 136.229 1.00 33.74 C ANISOU 1229 CB TYR A 247 4760 3694 4365 547 -289 1303 C ATOM 1230 CG TYR A 247 21.249 12.419 134.987 1.00 36.25 C ANISOU 1230 CG TYR A 247 5088 3996 4688 648 -254 1268 C ATOM 1231 CD1 TYR A 247 20.639 12.473 133.739 1.00 35.64 C ANISOU 1231 CD1 TYR A 247 5100 3841 4600 642 -261 1214 C ATOM 1232 CD2 TYR A 247 22.621 12.638 135.055 1.00 42.36 C ANISOU 1232 CD2 TYR A 247 5792 4813 5489 757 -215 1304 C ATOM 1233 CE1 TYR A 247 21.366 12.748 132.596 1.00 36.08 C ANISOU 1233 CE1 TYR A 247 5205 3864 4638 757 -203 1190 C ATOM 1234 CE2 TYR A 247 23.358 12.924 133.917 1.00 43.97 C ANISOU 1234 CE2 TYR A 247 6000 4991 5714 868 -142 1298 C ATOM 1235 CZ TYR A 247 22.728 12.969 132.692 1.00 41.51 C ANISOU 1235 CZ TYR A 247 5810 4603 5359 875 -123 1238 C ATOM 1236 OH TYR A 247 23.449 13.253 131.560 1.00 40.03 O ANISOU 1236 OH TYR A 247 5665 4374 5170 1005 -26 1239 O ATOM 1237 N LYS A 248 21.429 8.596 135.784 1.00 50.41 N ANISOU 1237 N LYS A 248 7209 5521 6424 720 -328 1388 N ATOM 1238 CA LYS A 248 22.569 7.680 135.707 1.00 35.55 C ANISOU 1238 CA LYS A 248 5401 3580 4526 857 -301 1432 C ATOM 1239 C LYS A 248 23.152 7.387 137.084 1.00 40.33 C ANISOU 1239 C LYS A 248 5937 4246 5143 862 -319 1500 C ATOM 1240 O LYS A 248 24.363 7.449 137.307 1.00 47.61 O ANISOU 1240 O LYS A 248 6789 5201 6099 963 -298 1546 O ATOM 1241 CB LYS A 248 23.626 8.226 134.751 1.00 40.55 C ANISOU 1241 CB LYS A 248 6006 4226 5176 996 -216 1426 C ATOM 1242 CG LYS A 248 22.973 8.673 133.436 1.00 44.65 C ANISOU 1242 CG LYS A 248 6621 4685 5659 989 -205 1352 C ATOM 1243 CD LYS A 248 23.932 9.107 132.355 1.00 36.48 C ANISOU 1243 CD LYS A 248 5608 3630 4623 1147 -88 1355 C ATOM 1244 CE LYS A 248 23.124 9.656 131.168 1.00 35.42 C ANISOU 1244 CE LYS A 248 5590 3435 4433 1120 -101 1273 C ATOM 1245 NZ LYS A 248 23.975 10.129 130.044 1.00 49.12 N ANISOU 1245 NZ LYS A 248 7379 5137 6149 1286 37 1279 N ATOM 1246 N GLY A 249 22.274 7.053 138.021 1.00 42.69 N ANISOU 1246 N GLY A 249 6257 4542 5423 754 -360 1518 N ATOM 1247 CA GLY A 249 22.736 6.690 139.341 1.00 48.33 C ANISOU 1247 CA GLY A 249 6959 5286 6118 763 -385 1581 C ATOM 1248 C GLY A 249 22.482 7.726 140.416 1.00 59.45 C ANISOU 1248 C GLY A 249 8282 6800 7506 694 -395 1584 C ATOM 1249 O GLY A 249 22.187 7.358 141.555 1.00 69.61 O ANISOU 1249 O GLY A 249 9625 8078 8745 661 -408 1630 O ATOM 1250 N SER A 250 22.577 9.014 140.085 1.00 56.11 N ANISOU 1250 N SER A 250 7751 6463 7105 681 -383 1540 N ATOM 1251 CA SER A 250 22.558 10.060 141.097 1.00 53.63 C ANISOU 1251 CA SER A 250 7386 6236 6756 640 -407 1541 C ATOM 1252 C SER A 250 21.195 10.738 141.159 1.00 45.38 C ANISOU 1252 C SER A 250 6333 5219 5691 539 -349 1511 C ATOM 1253 O SER A 250 20.575 11.021 140.134 1.00 43.75 O ANISOU 1253 O SER A 250 6084 5007 5532 503 -317 1466 O ATOM 1254 CB SER A 250 23.659 11.095 140.843 1.00 64.44 C ANISOU 1254 CB SER A 250 8634 7674 8178 691 -449 1529 C ATOM 1255 OG SER A 250 23.703 11.510 139.492 1.00 72.56 O ANISOU 1255 OG SER A 250 9592 8711 9266 715 -393 1485 O ATOM 1256 N TYR A 251 20.744 10.998 142.378 1.00 47.34 N ANISOU 1256 N TYR A 251 6634 5483 5868 506 -334 1544 N ATOM 1257 CA TYR A 251 19.450 11.612 142.634 1.00 41.87 C ANISOU 1257 CA TYR A 251 5935 4808 5166 431 -246 1546 C ATOM 1258 C TYR A 251 19.569 13.126 142.542 1.00 36.74 C ANISOU 1258 C TYR A 251 5212 4247 4499 424 -250 1490 C ATOM 1259 O TYR A 251 20.458 13.722 143.154 1.00 46.87 O ANISOU 1259 O TYR A 251 6517 5566 5724 465 -323 1482 O ATOM 1260 CB TYR A 251 18.976 11.188 144.018 1.00 43.09 C ANISOU 1260 CB TYR A 251 6214 4922 5235 431 -192 1622 C ATOM 1261 CG TYR A 251 17.619 11.662 144.457 1.00 45.83 C ANISOU 1261 CG TYR A 251 6564 5264 5584 378 -56 1665 C ATOM 1262 CD1 TYR A 251 17.469 12.843 145.171 1.00 47.50 C ANISOU 1262 CD1 TYR A 251 6818 5525 5703 396 -8 1655 C ATOM 1263 CD2 TYR A 251 16.493 10.887 144.228 1.00 54.76 C ANISOU 1263 CD2 TYR A 251 7665 6323 6820 317 25 1734 C ATOM 1264 CE1 TYR A 251 16.222 13.257 145.611 1.00 54.96 C ANISOU 1264 CE1 TYR A 251 7772 6455 6655 372 152 1715 C ATOM 1265 CE2 TYR A 251 15.252 11.289 144.662 1.00 58.70 C ANISOU 1265 CE2 TYR A 251 8137 6805 7360 278 170 1807 C ATOM 1266 CZ TYR A 251 15.118 12.468 145.355 1.00 61.35 C ANISOU 1266 CZ TYR A 251 8515 7198 7598 315 252 1800 C ATOM 1267 OH TYR A 251 13.869 12.849 145.785 1.00 69.05 O ANISOU 1267 OH TYR A 251 9465 8147 8624 297 431 1892 O ATOM 1268 N LEU A 252 18.685 13.747 141.765 1.00 41.80 N ANISOU 1268 N LEU A 252 5770 4910 5200 367 -192 1455 N ATOM 1269 CA LEU A 252 18.723 15.185 141.534 1.00 42.29 C ANISOU 1269 CA LEU A 252 5760 5054 5256 357 -190 1398 C ATOM 1270 C LEU A 252 17.376 15.809 141.855 1.00 39.55 C ANISOU 1270 C LEU A 252 5402 4714 4910 301 -80 1419 C ATOM 1271 O LEU A 252 16.327 15.246 141.531 1.00 40.08 O ANISOU 1271 O LEU A 252 5439 4727 5062 248 -20 1461 O ATOM 1272 CB LEU A 252 19.091 15.526 140.077 1.00 39.20 C ANISOU 1272 CB LEU A 252 5265 4685 4945 361 -223 1333 C ATOM 1273 CG LEU A 252 20.464 15.067 139.603 1.00 48.39 C ANISOU 1273 CG LEU A 252 6416 5837 6133 440 -290 1330 C ATOM 1274 CD1 LEU A 252 20.687 15.531 138.185 1.00 48.49 C ANISOU 1274 CD1 LEU A 252 6355 5861 6208 461 -276 1276 C ATOM 1275 CD2 LEU A 252 21.542 15.605 140.534 1.00 51.96 C ANISOU 1275 CD2 LEU A 252 6862 6331 6550 482 -366 1351 C ATOM 1276 N ARG A 253 17.425 16.983 142.471 1.00 36.52 N ANISOU 1276 N ARG A 253 5044 4385 4447 316 -63 1398 N ATOM 1277 CA ARG A 253 16.268 17.841 142.693 1.00 39.49 C ANISOU 1277 CA ARG A 253 5403 4778 4825 285 58 1414 C ATOM 1278 C ARG A 253 16.445 19.064 141.812 1.00 40.09 C ANISOU 1278 C ARG A 253 5373 4926 4935 266 19 1330 C ATOM 1279 O ARG A 253 17.445 19.778 141.941 1.00 41.74 O ANISOU 1279 O ARG A 253 5600 5178 5083 299 -72 1280 O ATOM 1280 CB ARG A 253 16.152 18.254 144.163 1.00 47.48 C ANISOU 1280 CB ARG A 253 6585 5773 5683 339 126 1460 C ATOM 1281 CG ARG A 253 15.325 17.311 145.013 1.00 62.28 C ANISOU 1281 CG ARG A 253 8551 7568 7544 352 261 1572 C ATOM 1282 CD ARG A 253 15.574 17.549 146.501 1.00 66.87 C ANISOU 1282 CD ARG A 253 9374 8110 7923 437 299 1610 C ATOM 1283 NE ARG A 253 15.748 18.967 146.828 1.00 62.60 N ANISOU 1283 NE ARG A 253 8915 7605 7267 472 283 1553 N ATOM 1284 CZ ARG A 253 14.792 19.745 147.327 1.00 64.88 C ANISOU 1284 CZ ARG A 253 9277 7877 7498 508 459 1595 C ATOM 1285 NH1 ARG A 253 15.048 21.022 147.600 1.00 66.22 N ANISOU 1285 NH1 ARG A 253 9546 8067 7546 544 420 1533 N ATOM 1286 NH2 ARG A 253 13.582 19.246 147.552 1.00 65.71 N ANISOU 1286 NH2 ARG A 253 9353 7933 7680 513 678 1711 N ATOM 1287 N ILE A 254 15.489 19.297 140.915 1.00 34.27 N ANISOU 1287 N ILE A 254 4524 4189 4309 210 72 1323 N ATOM 1288 CA ILE A 254 15.655 20.256 139.834 1.00 33.41 C ANISOU 1288 CA ILE A 254 4314 4134 4246 191 26 1241 C ATOM 1289 C ILE A 254 14.510 21.260 139.875 1.00 37.33 C ANISOU 1289 C ILE A 254 4757 4652 4774 158 127 1252 C ATOM 1290 O ILE A 254 13.335 20.877 139.795 1.00 37.54 O ANISOU 1290 O ILE A 254 4732 4628 4906 113 205 1321 O ATOM 1291 CB ILE A 254 15.705 19.564 138.465 1.00 36.64 C ANISOU 1291 CB ILE A 254 4663 4502 4756 166 -39 1211 C ATOM 1292 CG1 ILE A 254 16.848 18.552 138.420 1.00 37.13 C ANISOU 1292 CG1 ILE A 254 4784 4534 4788 220 -110 1213 C ATOM 1293 CG2 ILE A 254 15.852 20.610 137.350 1.00 32.62 C ANISOU 1293 CG2 ILE A 254 4076 4040 4278 159 -69 1131 C ATOM 1294 CD1 ILE A 254 16.390 17.173 138.089 1.00 46.96 C ANISOU 1294 CD1 ILE A 254 6070 5681 6091 198 -125 1255 C ATOM 1295 N CYS A 255 14.852 22.539 139.964 1.00 38.37 N ANISOU 1295 N CYS A 255 4890 4849 4839 178 118 1195 N ATOM 1296 CA CYS A 255 13.873 23.608 139.829 1.00 34.16 C ANISOU 1296 CA CYS A 255 4300 4341 4340 156 208 1193 C ATOM 1297 C CYS A 255 13.746 23.977 138.352 1.00 37.03 C ANISOU 1297 C CYS A 255 4535 4723 4812 108 145 1129 C ATOM 1298 O CYS A 255 14.729 24.370 137.716 1.00 32.05 O ANISOU 1298 O CYS A 255 3890 4133 4156 125 56 1054 O ATOM 1299 CB CYS A 255 14.295 24.816 140.660 1.00 44.12 C ANISOU 1299 CB CYS A 255 5661 5645 5458 205 218 1160 C ATOM 1300 SG CYS A 255 13.263 26.277 140.379 1.00 38.13 S ANISOU 1300 SG CYS A 255 4838 4921 4729 193 323 1144 S ATOM 1301 N LEU A 256 12.542 23.858 137.806 1.00 32.17 N ANISOU 1301 N LEU A 256 3829 4065 4328 53 189 1171 N ATOM 1302 CA LEU A 256 12.355 24.190 136.404 1.00 27.35 C ANISOU 1302 CA LEU A 256 3136 3450 3807 11 109 1110 C ATOM 1303 C LEU A 256 10.872 24.378 136.129 1.00 33.38 C ANISOU 1303 C LEU A 256 3794 4164 4726 -51 158 1178 C ATOM 1304 O LEU A 256 10.019 24.155 136.989 1.00 37.50 O ANISOU 1304 O LEU A 256 4289 4653 5307 -57 273 1286 O ATOM 1305 CB LEU A 256 12.950 23.120 135.481 1.00 27.24 C ANISOU 1305 CB LEU A 256 3159 3377 3815 8 -6 1079 C ATOM 1306 CG LEU A 256 12.181 21.833 135.152 1.00 39.08 C ANISOU 1306 CG LEU A 256 4661 4758 5429 -45 -55 1146 C ATOM 1307 CD1 LEU A 256 12.966 20.966 134.146 1.00 34.23 C ANISOU 1307 CD1 LEU A 256 4139 4080 4786 -18 -170 1091 C ATOM 1308 CD2 LEU A 256 11.830 21.019 136.404 1.00 39.78 C ANISOU 1308 CD2 LEU A 256 4769 4818 5528 -46 28 1251 C ATOM 1309 N LEU A 257 10.589 24.832 134.919 1.00 35.08 N ANISOU 1309 N LEU A 257 3950 4364 5015 -90 73 1124 N ATOM 1310 CA LEU A 257 9.239 24.907 134.375 1.00 38.52 C ANISOU 1310 CA LEU A 257 4271 4726 5637 -163 55 1189 C ATOM 1311 C LEU A 257 8.884 23.492 133.946 1.00 40.75 C ANISOU 1311 C LEU A 257 4569 4881 6035 -220 -57 1246 C ATOM 1312 O LEU A 257 9.214 23.049 132.843 1.00 44.29 O ANISOU 1312 O LEU A 257 5089 5264 6476 -235 -210 1179 O ATOM 1313 CB LEU A 257 9.195 25.899 133.216 1.00 32.13 C ANISOU 1313 CB LEU A 257 3433 3936 4840 -179 -25 1101 C ATOM 1314 CG LEU A 257 7.811 26.123 132.597 1.00 41.63 C ANISOU 1314 CG LEU A 257 4511 5054 6250 -257 -76 1168 C ATOM 1315 CD1 LEU A 257 6.852 26.710 133.616 1.00 32.48 C ANISOU 1315 CD1 LEU A 257 3229 3923 5188 -253 101 1284 C ATOM 1316 CD2 LEU A 257 7.910 27.011 131.366 1.00 35.05 C ANISOU 1316 CD2 LEU A 257 3692 4228 5399 -264 -181 1065 C ATOM 1317 N HIS A 258 8.235 22.752 134.832 1.00 43.19 N ANISOU 1317 N HIS A 258 4832 5137 6439 -241 22 1375 N ATOM 1318 CA HIS A 258 8.264 21.301 134.691 1.00 43.84 C ANISOU 1318 CA HIS A 258 4969 5111 6577 -277 -77 1419 C ATOM 1319 C HIS A 258 7.440 20.855 133.485 1.00 37.65 C ANISOU 1319 C HIS A 258 4145 4181 5980 -373 -273 1442 C ATOM 1320 O HIS A 258 6.408 21.453 133.173 1.00 39.76 O ANISOU 1320 O HIS A 258 4276 4410 6420 -432 -290 1502 O ATOM 1321 CB HIS A 258 7.787 20.603 135.970 1.00 52.57 C ANISOU 1321 CB HIS A 258 6042 6189 7745 -274 65 1563 C ATOM 1322 CG HIS A 258 6.382 20.929 136.374 1.00 64.51 C ANISOU 1322 CG HIS A 258 7380 7652 9478 -319 182 1721 C ATOM 1323 ND1 HIS A 258 5.304 20.142 136.026 1.00 69.82 N ANISOU 1323 ND1 HIS A 258 7929 8177 10423 -418 99 1858 N ATOM 1324 CD2 HIS A 258 5.884 21.930 137.136 1.00 67.92 C ANISOU 1324 CD2 HIS A 258 7744 8148 9915 -269 384 1783 C ATOM 1325 CE1 HIS A 258 4.200 20.656 136.541 1.00 69.40 C ANISOU 1325 CE1 HIS A 258 7705 8105 10559 -428 257 2010 C ATOM 1326 NE2 HIS A 258 4.524 21.745 137.216 1.00 72.05 N ANISOU 1326 NE2 HIS A 258 8083 8569 10723 -330 446 1964 N ATOM 1327 N PRO A 259 7.900 19.849 132.751 1.00 45.49 N ANISOU 1327 N PRO A 259 5273 5075 6935 -383 -437 1393 N ATOM 1328 CA PRO A 259 7.035 19.229 131.749 1.00 56.05 C ANISOU 1328 CA PRO A 259 6616 6229 8453 -481 -658 1434 C ATOM 1329 C PRO A 259 5.809 18.658 132.441 1.00 54.21 C ANISOU 1329 C PRO A 259 6211 5902 8485 -573 -634 1624 C ATOM 1330 O PRO A 259 5.799 18.435 133.655 1.00 57.80 O ANISOU 1330 O PRO A 259 6602 6418 8940 -543 -443 1714 O ATOM 1331 CB PRO A 259 7.910 18.119 131.149 1.00 65.23 C ANISOU 1331 CB PRO A 259 8003 7302 9478 -443 -792 1357 C ATOM 1332 CG PRO A 259 9.315 18.407 131.632 1.00 63.22 C ANISOU 1332 CG PRO A 259 7830 7208 8982 -318 -636 1263 C ATOM 1333 CD PRO A 259 9.153 19.101 132.939 1.00 57.64 C ANISOU 1333 CD PRO A 259 6972 6642 8286 -304 -430 1325 C ATOM 1334 N VAL A 260 4.773 18.407 131.652 1.00 57.41 N ANISOU 1334 N VAL A 260 6547 6138 9127 -684 -838 1698 N ATOM 1335 CA VAL A 260 3.485 17.992 132.201 1.00 58.10 C ANISOU 1335 CA VAL A 260 6416 6118 9540 -784 -823 1913 C ATOM 1336 C VAL A 260 2.989 19.092 133.127 1.00 52.92 C ANISOU 1336 C VAL A 260 5559 5597 8952 -742 -545 2001 C ATOM 1337 O VAL A 260 3.142 19.015 134.350 1.00 55.54 O ANISOU 1337 O VAL A 260 5861 6016 9226 -675 -295 2072 O ATOM 1338 CB VAL A 260 3.556 16.648 132.950 1.00 60.21 C ANISOU 1338 CB VAL A 260 6715 6313 9848 -799 -793 2013 C ATOM 1339 CG1 VAL A 260 2.146 16.181 133.305 1.00 57.27 C ANISOU 1339 CG1 VAL A 260 6101 5790 9869 -916 -810 2258 C ATOM 1340 CG2 VAL A 260 4.309 15.602 132.129 1.00 61.25 C ANISOU 1340 CG2 VAL A 260 7104 6335 9834 -800 -1027 1896 C ATOM 1341 N GLN A 261 2.429 20.137 132.548 1.00 47.09 N ANISOU 1341 N GLN A 261 4713 4868 8311 -766 -584 1993 N ATOM 1342 CA GLN A 261 1.684 21.078 133.352 1.00 48.91 C ANISOU 1342 CA GLN A 261 4736 5176 8673 -736 -335 2118 C ATOM 1343 C GLN A 261 0.277 20.529 133.571 1.00 53.76 C ANISOU 1343 C GLN A 261 5099 5623 9703 -838 -351 2377 C ATOM 1344 O GLN A 261 -0.192 19.657 132.836 1.00 53.41 O ANISOU 1344 O GLN A 261 5034 5396 9865 -958 -629 2435 O ATOM 1345 CB GLN A 261 1.674 22.445 132.670 1.00 41.05 C ANISOU 1345 CB GLN A 261 3720 4258 7617 -714 -359 2011 C ATOM 1346 CG GLN A 261 3.074 23.067 132.573 1.00 44.80 C ANISOU 1346 CG GLN A 261 4410 4900 7713 -608 -308 1786 C ATOM 1347 CD GLN A 261 3.554 23.604 133.915 1.00 44.95 C ANISOU 1347 CD GLN A 261 4448 5075 7555 -495 -6 1792 C ATOM 1348 OE1 GLN A 261 2.792 24.230 134.642 1.00 48.01 O ANISOU 1348 OE1 GLN A 261 4699 5487 8056 -466 195 1915 O ATOM 1349 NE2 GLN A 261 4.811 23.350 134.251 1.00 41.52 N ANISOU 1349 NE2 GLN A 261 4197 4728 6848 -422 23 1669 N ATOM 1350 N LYS A 262 -0.393 21.040 134.605 1.00 60.49 N ANISOU 1350 N LYS A 262 5770 6524 10688 -784 -48 2546 N ATOM 1351 CA LYS A 262 -1.647 20.435 135.045 1.00 62.36 C ANISOU 1351 CA LYS A 262 5814 6672 11209 -774 -12 2724 C ATOM 1352 C LYS A 262 -2.864 20.879 134.233 1.00 68.61 C ANISOU 1352 C LYS A 262 6414 7379 12276 -806 -193 2781 C ATOM 1353 O LYS A 262 -3.811 20.100 134.092 1.00 84.21 O ANISOU 1353 O LYS A 262 8250 9225 14520 -845 -332 2910 O ATOM 1354 CB LYS A 262 -1.871 20.727 136.530 1.00 60.03 C ANISOU 1354 CB LYS A 262 5479 6470 10859 -626 392 2832 C ATOM 1355 CG LYS A 262 -1.059 19.821 137.443 1.00 67.30 C ANISOU 1355 CG LYS A 262 6560 7412 11600 -595 529 2845 C ATOM 1356 CD LYS A 262 -1.261 18.364 137.040 1.00 75.88 C ANISOU 1356 CD LYS A 262 7627 8353 12852 -705 285 2895 C ATOM 1357 CE LYS A 262 -0.484 17.418 137.934 1.00 79.46 C ANISOU 1357 CE LYS A 262 8244 8815 13133 -671 412 2913 C ATOM 1358 NZ LYS A 262 -0.679 16.000 137.529 1.00 82.83 N ANISOU 1358 NZ LYS A 262 8664 9095 13712 -777 168 2955 N ATOM 1359 N THR A 263 -2.885 22.095 133.693 1.00 60.77 N ANISOU 1359 N THR A 263 5409 6446 11234 -788 -205 2699 N ATOM 1360 CA THR A 263 -4.059 22.559 132.966 1.00 60.64 C ANISOU 1360 CA THR A 263 5225 6341 11475 -803 -370 2769 C ATOM 1361 C THR A 263 -3.708 22.860 131.513 1.00 65.18 C ANISOU 1361 C THR A 263 5917 6861 11987 -901 -716 2612 C ATOM 1362 O THR A 263 -2.535 22.972 131.139 1.00 60.39 O ANISOU 1362 O THR A 263 5508 6310 11127 -936 -767 2446 O ATOM 1363 CB THR A 263 -4.663 23.812 133.609 1.00 53.04 C ANISOU 1363 CB THR A 263 4142 5467 10543 -673 -74 2837 C ATOM 1364 OG1 THR A 263 -3.695 24.866 133.574 1.00 57.21 O ANISOU 1364 OG1 THR A 263 4813 6144 10780 -639 41 2671 O ATOM 1365 CG2 THR A 263 -5.067 23.543 135.044 1.00 56.17 C ANISOU 1365 CG2 THR A 263 4464 5891 10988 -550 275 2993 C ATOM 1366 N ALA A 264 -4.754 22.998 130.691 1.00 61.74 N ANISOU 1366 N ALA A 264 5368 6300 11788 -934 -954 2679 N ATOM 1367 CA ALA A 264 -4.549 23.225 129.265 1.00 62.10 C ANISOU 1367 CA ALA A 264 5557 6262 11775 -1014 -1307 2541 C ATOM 1368 C ALA A 264 -3.813 24.532 129.024 1.00 61.50 C ANISOU 1368 C ALA A 264 5575 6326 11466 -977 -1189 2383 C ATOM 1369 O ALA A 264 -2.914 24.601 128.177 1.00 67.68 O ANISOU 1369 O ALA A 264 6568 7099 12048 -1028 -1368 2210 O ATOM 1370 CB ALA A 264 -5.888 23.222 128.528 1.00 61.40 C ANISOU 1370 CB ALA A 264 5330 6009 11992 -1037 -1568 2669 C ATOM 1371 N PHE A 265 -4.178 25.577 129.770 1.00 56.75 N ANISOU 1371 N PHE A 265 4834 5844 10883 -878 -885 2442 N ATOM 1372 CA PHE A 265 -3.514 26.865 129.630 1.00 51.93 C ANISOU 1372 CA PHE A 265 4298 5379 10055 -836 -759 2300 C ATOM 1373 C PHE A 265 -2.033 26.747 129.962 1.00 49.82 C ANISOU 1373 C PHE A 265 4199 5237 9493 -841 -648 2160 C ATOM 1374 O PHE A 265 -1.174 27.232 129.217 1.00 45.74 O ANISOU 1374 O PHE A 265 3843 4771 8764 -851 -757 1981 O ATOM 1375 CB PHE A 265 -4.179 27.906 130.532 1.00 50.44 C ANISOU 1375 CB PHE A 265 3961 5284 9922 -712 -432 2399 C ATOM 1376 CG PHE A 265 -3.466 29.231 130.546 1.00 50.30 C ANISOU 1376 CG PHE A 265 4021 5426 9663 -656 -278 2256 C ATOM 1377 CD1 PHE A 265 -3.667 30.148 129.535 1.00 55.91 C ANISOU 1377 CD1 PHE A 265 4745 6121 10378 -679 -439 2173 C ATOM 1378 CD2 PHE A 265 -2.577 29.548 131.563 1.00 52.68 C ANISOU 1378 CD2 PHE A 265 4400 5888 9728 -577 16 2206 C ATOM 1379 CE1 PHE A 265 -2.999 31.367 129.536 1.00 59.56 C ANISOU 1379 CE1 PHE A 265 5273 6733 10623 -626 -304 2040 C ATOM 1380 CE2 PHE A 265 -1.902 30.765 131.570 1.00 50.22 C ANISOU 1380 CE2 PHE A 265 4162 5722 9197 -523 137 2078 C ATOM 1381 CZ PHE A 265 -2.115 31.675 130.559 1.00 50.52 C ANISOU 1381 CZ PHE A 265 4190 5751 9254 -548 -20 1994 C ATOM 1382 N MET A 266 -1.717 26.102 131.086 1.00 41.65 N ANISOU 1382 N MET A 266 3161 4253 8411 -802 -427 2233 N ATOM 1383 CA MET A 266 -0.328 26.014 131.511 1.00 41.89 C ANISOU 1383 CA MET A 266 3414 4423 8080 -732 -311 2072 C ATOM 1384 C MET A 266 0.484 25.113 130.592 1.00 43.15 C ANISOU 1384 C MET A 266 3800 4514 8083 -778 -593 1920 C ATOM 1385 O MET A 266 1.678 25.363 130.390 1.00 41.40 O ANISOU 1385 O MET A 266 3789 4404 7537 -702 -580 1728 O ATOM 1386 CB MET A 266 -0.258 25.555 132.966 1.00 40.07 C ANISOU 1386 CB MET A 266 3157 4249 7818 -659 -13 2189 C ATOM 1387 CG MET A 266 -0.693 26.655 133.944 1.00 41.19 C ANISOU 1387 CG MET A 266 3193 4490 7966 -552 324 2282 C ATOM 1388 SD MET A 266 0.285 28.171 133.723 1.00 44.42 S ANISOU 1388 SD MET A 266 3778 5086 8015 -453 378 2040 S ATOM 1389 CE MET A 266 1.947 27.583 134.023 1.00 34.90 C ANISOU 1389 CE MET A 266 2861 3979 6418 -398 347 1843 C ATOM 1390 N GLN A 267 -0.137 24.078 130.016 1.00 45.90 N ANISOU 1390 N GLN A 267 4114 4662 8664 -894 -851 2014 N ATOM 1391 CA GLN A 267 0.551 23.276 129.004 1.00 53.66 C ANISOU 1391 CA GLN A 267 5355 5544 9489 -925 -1137 1869 C ATOM 1392 C GLN A 267 0.970 24.145 127.832 1.00 44.15 C ANISOU 1392 C GLN A 267 4307 4357 8111 -898 -1285 1690 C ATOM 1393 O GLN A 267 2.127 24.111 127.394 1.00 47.03 O ANISOU 1393 O GLN A 267 4921 4782 8165 -820 -1299 1510 O ATOM 1394 CB GLN A 267 -0.347 22.131 128.508 1.00 54.09 C ANISOU 1394 CB GLN A 267 5359 5343 9851 -1066 -1436 2010 C ATOM 1395 CG GLN A 267 -0.591 21.031 129.497 1.00 60.89 C ANISOU 1395 CG GLN A 267 6120 6158 10857 -1096 -1331 2171 C ATOM 1396 CD GLN A 267 -1.672 20.061 129.033 1.00 70.64 C ANISOU 1396 CD GLN A 267 7279 7207 12355 -1169 -1612 2281 C ATOM 1397 OE1 GLN A 267 -1.904 19.890 127.834 1.00 71.46 O ANISOU 1397 OE1 GLN A 267 7509 7171 12472 -1220 -1955 2210 O ATOM 1398 NE2 GLN A 267 -2.341 19.426 129.988 1.00 75.00 N ANISOU 1398 NE2 GLN A 267 7640 7762 13093 -1153 -1466 2451 N ATOM 1399 N PHE A 268 0.030 24.941 127.324 1.00 45.42 N ANISOU 1399 N PHE A 268 4316 4458 8484 -956 -1383 1753 N ATOM 1400 CA PHE A 268 0.303 25.858 126.223 1.00 51.75 C ANISOU 1400 CA PHE A 268 5257 5267 9140 -931 -1516 1599 C ATOM 1401 C PHE A 268 1.400 26.855 126.581 1.00 47.96 C ANISOU 1401 C PHE A 268 4862 5023 8337 -798 -1250 1445 C ATOM 1402 O PHE A 268 2.300 27.117 125.776 1.00 46.96 O ANISOU 1402 O PHE A 268 4965 4922 7956 -738 -1318 1273 O ATOM 1403 CB PHE A 268 -0.985 26.584 125.842 1.00 51.96 C ANISOU 1403 CB PHE A 268 5056 5200 9487 -1015 -1632 1725 C ATOM 1404 CG PHE A 268 -0.782 27.711 124.889 1.00 56.27 C ANISOU 1404 CG PHE A 268 5711 5779 9892 -979 -1715 1583 C ATOM 1405 CD1 PHE A 268 -0.606 27.467 123.536 1.00 58.55 C ANISOU 1405 CD1 PHE A 268 6262 5904 10082 -1008 -2043 1469 C ATOM 1406 CD2 PHE A 268 -0.769 29.024 125.341 1.00 57.28 C ANISOU 1406 CD2 PHE A 268 5709 6087 9970 -907 -1464 1566 C ATOM 1407 CE1 PHE A 268 -0.420 28.520 122.648 1.00 50.30 C ANISOU 1407 CE1 PHE A 268 5334 4881 8898 -965 -2107 1344 C ATOM 1408 CE2 PHE A 268 -0.581 30.077 124.461 1.00 54.09 C ANISOU 1408 CE2 PHE A 268 5403 5709 9438 -876 -1538 1439 C ATOM 1409 CZ PHE A 268 -0.403 29.824 123.117 1.00 50.47 C ANISOU 1409 CZ PHE A 268 5193 5095 8888 -904 -1852 1330 C ATOM 1410 N TYR A 269 1.327 27.440 127.781 1.00 51.41 N ANISOU 1410 N TYR A 269 5127 5618 8788 -744 -947 1514 N ATOM 1411 CA TYR A 269 2.382 28.338 128.247 1.00 45.45 C ANISOU 1411 CA TYR A 269 4460 5069 7741 -627 -721 1380 C ATOM 1412 C TYR A 269 3.743 27.653 128.205 1.00 46.26 C ANISOU 1412 C TYR A 269 4792 5217 7568 -565 -724 1249 C ATOM 1413 O TYR A 269 4.726 28.233 127.732 1.00 42.36 O ANISOU 1413 O TYR A 269 4442 4806 6846 -495 -710 1101 O ATOM 1414 CB TYR A 269 2.075 28.821 129.666 1.00 44.45 C ANISOU 1414 CB TYR A 269 4170 5059 7658 -574 -416 1491 C ATOM 1415 CG TYR A 269 3.148 29.728 130.249 1.00 44.33 C ANISOU 1415 CG TYR A 269 4264 5231 7349 -462 -218 1363 C ATOM 1416 CD1 TYR A 269 3.240 31.070 129.860 1.00 38.32 C ANISOU 1416 CD1 TYR A 269 3502 4549 6511 -427 -187 1278 C ATOM 1417 CD2 TYR A 269 4.049 29.256 131.204 1.00 34.77 C ANISOU 1417 CD2 TYR A 269 3156 4101 5953 -397 -82 1336 C ATOM 1418 CE1 TYR A 269 4.210 31.906 130.386 1.00 34.86 C ANISOU 1418 CE1 TYR A 269 3160 4257 5827 -337 -39 1172 C ATOM 1419 CE2 TYR A 269 5.021 30.093 131.739 1.00 36.45 C ANISOU 1419 CE2 TYR A 269 3469 4458 5924 -307 53 1232 C ATOM 1420 CZ TYR A 269 5.099 31.408 131.323 1.00 35.50 C ANISOU 1420 CZ TYR A 269 3342 4405 5741 -282 68 1152 C ATOM 1421 OH TYR A 269 6.063 32.235 131.841 1.00 36.29 O ANISOU 1421 OH TYR A 269 3541 4626 5623 -205 169 1057 O ATOM 1422 N ALA A 270 3.813 26.406 128.682 1.00 43.36 N ANISOU 1422 N ALA A 270 4451 4787 7238 -587 -739 1315 N ATOM 1423 CA ALA A 270 5.087 25.697 128.697 1.00 46.07 C ANISOU 1423 CA ALA A 270 4997 5166 7340 -521 -732 1210 C ATOM 1424 C ALA A 270 5.665 25.562 127.293 1.00 45.13 C ANISOU 1424 C ALA A 270 5100 4959 7088 -502 -932 1077 C ATOM 1425 O ALA A 270 6.880 25.688 127.107 1.00 45.87 O ANISOU 1425 O ALA A 270 5344 5134 6951 -407 -865 962 O ATOM 1426 CB ALA A 270 4.928 24.322 129.354 1.00 43.04 C ANISOU 1426 CB ALA A 270 4607 4703 7043 -556 -740 1314 C ATOM 1427 N THR A 271 4.814 25.338 126.285 1.00 44.04 N ANISOU 1427 N THR A 271 4996 4642 7097 -582 -1180 1102 N ATOM 1428 CA THR A 271 5.344 25.188 124.933 1.00 46.17 C ANISOU 1428 CA THR A 271 5539 4798 7205 -544 -1366 978 C ATOM 1429 C THR A 271 5.594 26.533 124.245 1.00 41.39 C ANISOU 1429 C THR A 271 4966 4268 6490 -491 -1331 877 C ATOM 1430 O THR A 271 6.474 26.624 123.383 1.00 47.75 O ANISOU 1430 O THR A 271 6006 5053 7083 -402 -1354 760 O ATOM 1431 CB THR A 271 4.407 24.318 124.082 1.00 44.21 C ANISOU 1431 CB THR A 271 5385 4288 7127 -647 -1693 1036 C ATOM 1432 OG1 THR A 271 3.244 25.067 123.715 1.00 56.38 O ANISOU 1432 OG1 THR A 271 6767 5763 8893 -738 -1824 1103 O ATOM 1433 CG2 THR A 271 3.977 23.095 124.854 1.00 39.69 C ANISOU 1433 CG2 THR A 271 4722 3638 6720 -720 -1724 1165 C ATOM 1434 N ALA A 272 4.870 27.588 124.610 1.00 41.84 N ANISOU 1434 N ALA A 272 4804 4409 6685 -531 -1255 927 N ATOM 1435 CA ALA A 272 4.970 28.858 123.895 1.00 38.94 C ANISOU 1435 CA ALA A 272 4467 4093 6237 -494 -1250 840 C ATOM 1436 C ALA A 272 5.762 29.937 124.628 1.00 35.87 C ANISOU 1436 C ALA A 272 3993 3929 5708 -412 -981 786 C ATOM 1437 O ALA A 272 5.990 30.999 124.052 1.00 35.42 O ANISOU 1437 O ALA A 272 3970 3920 5567 -373 -962 709 O ATOM 1438 CB ALA A 272 3.570 29.395 123.582 1.00 38.12 C ANISOU 1438 CB ALA A 272 4197 3895 6391 -593 -1395 929 C ATOM 1439 N LYS A 273 6.199 29.684 125.864 1.00 32.55 N ANISOU 1439 N LYS A 273 3484 3629 5256 -384 -793 826 N ATOM 1440 CA LYS A 273 6.727 30.738 126.731 1.00 32.18 C ANISOU 1440 CA LYS A 273 3348 3767 5113 -325 -574 800 C ATOM 1441 C LYS A 273 7.802 31.570 126.047 1.00 35.00 C ANISOU 1441 C LYS A 273 3825 4194 5279 -248 -545 673 C ATOM 1442 O LYS A 273 7.800 32.803 126.144 1.00 37.45 O ANISOU 1442 O LYS A 273 4067 4596 5565 -231 -463 642 O ATOM 1443 CB LYS A 273 7.284 30.124 128.020 1.00 27.73 C ANISOU 1443 CB LYS A 273 2761 3284 4492 -293 -425 843 C ATOM 1444 CG LYS A 273 8.091 31.088 128.871 1.00 32.05 C ANISOU 1444 CG LYS A 273 3289 3991 4897 -224 -249 799 C ATOM 1445 CD LYS A 273 8.623 30.387 130.104 1.00 37.14 C ANISOU 1445 CD LYS A 273 3949 4684 5479 -193 -144 843 C ATOM 1446 CE LYS A 273 9.763 31.165 130.738 1.00 36.89 C ANISOU 1446 CE LYS A 273 3961 4776 5279 -123 -46 779 C ATOM 1447 NZ LYS A 273 10.075 30.606 132.069 1.00 33.37 N ANISOU 1447 NZ LYS A 273 3539 4361 4779 -96 44 835 N ATOM 1448 N ASP A 274 8.730 30.922 125.350 1.00 35.96 N ANISOU 1448 N ASP A 274 4127 4264 5271 -193 -598 609 N ATOM 1449 CA ASP A 274 9.860 31.667 124.819 1.00 37.67 C ANISOU 1449 CA ASP A 274 4434 4548 5329 -105 -524 520 C ATOM 1450 C ASP A 274 9.496 32.455 123.566 1.00 40.53 C ANISOU 1450 C ASP A 274 4879 4843 5679 -101 -617 463 C ATOM 1451 O ASP A 274 10.105 33.500 123.312 1.00 34.77 O ANISOU 1451 O ASP A 274 4148 4194 4867 -50 -529 410 O ATOM 1452 CB ASP A 274 11.028 30.725 124.573 1.00 35.50 C ANISOU 1452 CB ASP A 274 4313 4241 4934 -23 -502 497 C ATOM 1453 CG ASP A 274 11.597 30.171 125.878 1.00 41.35 C ANISOU 1453 CG ASP A 274 4968 5072 5670 -15 -397 546 C ATOM 1454 OD1 ASP A 274 11.677 30.915 126.879 1.00 44.56 O ANISOU 1454 OD1 ASP A 274 5241 5604 6087 -27 -297 562 O ATOM 1455 OD2 ASP A 274 11.935 28.989 125.917 1.00 44.76 O ANISOU 1455 OD2 ASP A 274 5489 5439 6080 7 -426 567 O ATOM 1456 N TRP A 275 8.509 32.000 122.786 1.00 31.94 N ANISOU 1456 N TRP A 275 3864 3594 4677 -159 -809 479 N ATOM 1457 CA TRP A 275 7.975 32.873 121.740 1.00 33.92 C ANISOU 1457 CA TRP A 275 4175 3778 4937 -169 -916 436 C ATOM 1458 C TRP A 275 7.160 34.014 122.340 1.00 37.91 C ANISOU 1458 C TRP A 275 4445 4384 5573 -228 -856 474 C ATOM 1459 O TRP A 275 7.176 35.137 121.816 1.00 32.71 O ANISOU 1459 O TRP A 275 3793 3761 4873 -205 -839 422 O ATOM 1460 CB TRP A 275 7.128 32.073 120.743 1.00 39.61 C ANISOU 1460 CB TRP A 275 5058 4270 5722 -220 -1184 449 C ATOM 1461 CG TRP A 275 7.913 31.048 119.959 1.00 44.10 C ANISOU 1461 CG TRP A 275 5930 4704 6120 -136 -1248 399 C ATOM 1462 CD1 TRP A 275 7.759 29.689 119.994 1.00 45.89 C ANISOU 1462 CD1 TRP A 275 6265 4797 6373 -162 -1373 437 C ATOM 1463 CD2 TRP A 275 8.977 31.307 119.028 1.00 42.86 C ANISOU 1463 CD2 TRP A 275 6021 4522 5741 1 -1170 315 C ATOM 1464 NE1 TRP A 275 8.656 29.089 119.137 1.00 46.52 N ANISOU 1464 NE1 TRP A 275 6663 4768 6245 -42 -1379 373 N ATOM 1465 CE2 TRP A 275 9.418 30.059 118.538 1.00 48.39 C ANISOU 1465 CE2 TRP A 275 6986 5068 6330 66 -1240 305 C ATOM 1466 CE3 TRP A 275 9.602 32.474 118.569 1.00 48.94 C ANISOU 1466 CE3 TRP A 275 6815 5378 6404 82 -1033 258 C ATOM 1467 CZ2 TRP A 275 10.451 29.943 117.609 1.00 48.40 C ANISOU 1467 CZ2 TRP A 275 7282 4995 6113 225 -1153 249 C ATOM 1468 CZ3 TRP A 275 10.628 32.359 117.647 1.00 50.53 C ANISOU 1468 CZ3 TRP A 275 7285 5506 6406 229 -950 210 C ATOM 1469 CH2 TRP A 275 11.039 31.104 117.174 1.00 47.44 C ANISOU 1469 CH2 TRP A 275 7162 4959 5904 308 -999 209 C ATOM 1470 N TRP A 276 6.461 33.747 123.445 1.00 37.71 N ANISOU 1470 N TRP A 276 4224 4401 5703 -291 -805 571 N ATOM 1471 CA TRP A 276 5.741 34.796 124.159 1.00 32.55 C ANISOU 1471 CA TRP A 276 3363 3842 5162 -319 -698 623 C ATOM 1472 C TRP A 276 6.701 35.858 124.680 1.00 35.05 C ANISOU 1472 C TRP A 276 3672 4328 5320 -245 -508 555 C ATOM 1473 O TRP A 276 6.454 37.064 124.522 1.00 29.79 O ANISOU 1473 O TRP A 276 2951 3712 4655 -238 -470 529 O ATOM 1474 CB TRP A 276 4.923 34.163 125.296 1.00 33.50 C ANISOU 1474 CB TRP A 276 3309 3959 5462 -371 -636 759 C ATOM 1475 CG TRP A 276 4.572 35.063 126.465 1.00 37.81 C ANISOU 1475 CG TRP A 276 3689 4629 6050 -348 -423 819 C ATOM 1476 CD1 TRP A 276 5.076 34.987 127.738 1.00 36.81 C ANISOU 1476 CD1 TRP A 276 3545 4606 5834 -299 -234 843 C ATOM 1477 CD2 TRP A 276 3.614 36.132 126.480 1.00 35.83 C ANISOU 1477 CD2 TRP A 276 3296 4386 5931 -361 -381 871 C ATOM 1478 NE1 TRP A 276 4.498 35.949 128.536 1.00 34.81 N ANISOU 1478 NE1 TRP A 276 3181 4418 5627 -272 -71 900 N ATOM 1479 CE2 TRP A 276 3.599 36.664 127.789 1.00 37.84 C ANISOU 1479 CE2 TRP A 276 3474 4750 6153 -307 -145 922 C ATOM 1480 CE3 TRP A 276 2.783 36.706 125.506 1.00 33.82 C ANISOU 1480 CE3 TRP A 276 2991 4048 5812 -406 -526 880 C ATOM 1481 CZ2 TRP A 276 2.794 37.754 128.148 1.00 39.22 C ANISOU 1481 CZ2 TRP A 276 3526 4955 6420 -284 -24 982 C ATOM 1482 CZ3 TRP A 276 1.980 37.787 125.869 1.00 37.65 C ANISOU 1482 CZ3 TRP A 276 3320 4572 6412 -394 -415 945 C ATOM 1483 CH2 TRP A 276 1.994 38.296 127.176 1.00 37.35 C ANISOU 1483 CH2 TRP A 276 3210 4646 6334 -329 -154 996 C ATOM 1484 N LEU A 277 7.821 35.434 125.284 1.00 28.70 N ANISOU 1484 N LEU A 277 2922 3598 4385 -194 -408 530 N ATOM 1485 CA LEU A 277 8.782 36.413 125.803 1.00 31.84 C ANISOU 1485 CA LEU A 277 3310 4132 4655 -136 -270 478 C ATOM 1486 C LEU A 277 9.460 37.183 124.671 1.00 37.64 C ANISOU 1486 C LEU A 277 4142 4865 5294 -92 -297 390 C ATOM 1487 O LEU A 277 9.701 38.396 124.783 1.00 33.60 O ANISOU 1487 O LEU A 277 3589 4435 4744 -74 -228 356 O ATOM 1488 CB LEU A 277 9.816 35.713 126.683 1.00 32.67 C ANISOU 1488 CB LEU A 277 3445 4293 4675 -99 -194 488 C ATOM 1489 CG LEU A 277 9.275 35.138 128.000 1.00 32.26 C ANISOU 1489 CG LEU A 277 3315 4258 4683 -124 -125 575 C ATOM 1490 CD1 LEU A 277 10.260 34.118 128.576 1.00 33.30 C ANISOU 1490 CD1 LEU A 277 3511 4403 4738 -92 -106 584 C ATOM 1491 CD2 LEU A 277 9.038 36.277 128.985 1.00 34.98 C ANISOU 1491 CD2 LEU A 277 3593 4691 5005 -108 -3 590 C ATOM 1492 N PHE A 278 9.786 36.493 123.576 1.00 31.93 N ANISOU 1492 N PHE A 278 3570 4037 4524 -64 -388 359 N ATOM 1493 CA PHE A 278 10.403 37.160 122.436 1.00 33.12 C ANISOU 1493 CA PHE A 278 3843 4164 4578 -2 -390 291 C ATOM 1494 C PHE A 278 9.453 38.180 121.812 1.00 34.99 C ANISOU 1494 C PHE A 278 4056 4371 4867 -39 -461 268 C ATOM 1495 O PHE A 278 9.869 39.283 121.432 1.00 33.56 O ANISOU 1495 O PHE A 278 3883 4242 4627 -2 -401 223 O ATOM 1496 CB PHE A 278 10.836 36.102 121.417 1.00 35.05 C ANISOU 1496 CB PHE A 278 4304 4270 4742 57 -462 273 C ATOM 1497 CG PHE A 278 11.455 36.667 120.175 1.00 36.93 C ANISOU 1497 CG PHE A 278 4712 4454 4866 147 -437 218 C ATOM 1498 CD1 PHE A 278 12.627 37.402 120.246 1.00 32.65 C ANISOU 1498 CD1 PHE A 278 4131 4009 4264 219 -275 211 C ATOM 1499 CD2 PHE A 278 10.869 36.457 118.938 1.00 35.03 C ANISOU 1499 CD2 PHE A 278 4681 4045 4582 161 -585 185 C ATOM 1500 CE1 PHE A 278 13.205 37.929 119.098 1.00 39.63 C ANISOU 1500 CE1 PHE A 278 5168 4835 5055 314 -220 182 C ATOM 1501 CE2 PHE A 278 11.442 36.974 117.792 1.00 41.79 C ANISOU 1501 CE2 PHE A 278 5731 4836 5310 263 -541 141 C ATOM 1502 CZ PHE A 278 12.616 37.703 117.870 1.00 39.06 C ANISOU 1502 CZ PHE A 278 5331 4599 4912 345 -338 144 C ATOM 1503 N SER A 279 8.170 37.831 121.715 1.00 33.94 N ANISOU 1503 N SER A 279 3880 4149 4867 -114 -595 311 N ATOM 1504 CA SER A 279 7.174 38.698 121.094 1.00 33.48 C ANISOU 1504 CA SER A 279 3789 4041 4892 -154 -692 306 C ATOM 1505 C SER A 279 6.830 39.879 121.985 1.00 39.01 C ANISOU 1505 C SER A 279 4296 4875 5650 -170 -561 328 C ATOM 1506 O SER A 279 6.909 41.040 121.561 1.00 35.22 O ANISOU 1506 O SER A 279 3824 4433 5126 -147 -534 279 O ATOM 1507 CB SER A 279 5.896 37.903 120.795 1.00 36.97 C ANISOU 1507 CB SER A 279 4211 4328 5509 -238 -896 376 C ATOM 1508 OG SER A 279 6.143 36.887 119.860 1.00 45.42 O ANISOU 1508 OG SER A 279 5512 5241 6504 -220 -1052 346 O ATOM 1509 N PHE A 280 6.389 39.596 123.213 1.00 34.32 N ANISOU 1509 N PHE A 280 3550 4338 5152 -201 -476 407 N ATOM 1510 CA PHE A 280 5.808 40.641 124.044 1.00 34.49 C ANISOU 1510 CA PHE A 280 3422 4446 5238 -204 -355 446 C ATOM 1511 C PHE A 280 6.862 41.430 124.791 1.00 34.45 C ANISOU 1511 C PHE A 280 3437 4575 5076 -147 -201 393 C ATOM 1512 O PHE A 280 6.641 42.613 125.082 1.00 35.72 O ANISOU 1512 O PHE A 280 3549 4795 5228 -132 -126 382 O ATOM 1513 CB PHE A 280 4.797 40.057 125.053 1.00 44.42 C ANISOU 1513 CB PHE A 280 4527 5684 6668 -242 -302 576 C ATOM 1514 CG PHE A 280 4.099 41.119 125.883 1.00 51.18 C ANISOU 1514 CG PHE A 280 5253 6604 7589 -219 -149 634 C ATOM 1515 CD1 PHE A 280 2.893 41.670 125.459 1.00 52.46 C ANISOU 1515 CD1 PHE A 280 5292 6702 7938 -250 -197 701 C ATOM 1516 CD2 PHE A 280 4.675 41.606 127.061 1.00 51.43 C ANISOU 1516 CD2 PHE A 280 5308 6744 7489 -159 34 624 C ATOM 1517 CE1 PHE A 280 2.264 42.671 126.201 1.00 55.25 C ANISOU 1517 CE1 PHE A 280 5540 7107 8347 -207 -30 762 C ATOM 1518 CE2 PHE A 280 4.059 42.612 127.802 1.00 54.57 C ANISOU 1518 CE2 PHE A 280 5640 7181 7913 -116 184 673 C ATOM 1519 CZ PHE A 280 2.848 43.141 127.373 1.00 55.03 C ANISOU 1519 CZ PHE A 280 5568 7183 8158 -134 170 745 C ATOM 1520 N TYR A 281 7.996 40.813 125.130 1.00 30.17 N ANISOU 1520 N TYR A 281 2968 4071 4424 -117 -165 368 N ATOM 1521 CA TYR A 281 9.008 41.490 125.932 1.00 30.21 C ANISOU 1521 CA TYR A 281 2985 4181 4313 -77 -60 336 C ATOM 1522 C TYR A 281 10.215 41.947 125.134 1.00 29.24 C ANISOU 1522 C TYR A 281 2940 4075 4093 -39 -74 266 C ATOM 1523 O TYR A 281 11.112 42.575 125.712 1.00 25.65 O ANISOU 1523 O TYR A 281 2482 3691 3573 -17 -19 250 O ATOM 1524 CB TYR A 281 9.478 40.595 127.088 1.00 28.98 C ANISOU 1524 CB TYR A 281 2833 4053 4125 -67 -6 380 C ATOM 1525 CG TYR A 281 8.419 40.340 128.144 1.00 32.22 C ANISOU 1525 CG TYR A 281 3173 4458 4613 -81 68 467 C ATOM 1526 CD1 TYR A 281 7.449 39.368 127.946 1.00 38.41 C ANISOU 1526 CD1 TYR A 281 3897 5160 5537 -122 24 541 C ATOM 1527 CD2 TYR A 281 8.392 41.065 129.341 1.00 31.55 C ANISOU 1527 CD2 TYR A 281 3095 4428 4463 -46 184 487 C ATOM 1528 CE1 TYR A 281 6.478 39.106 128.904 1.00 41.15 C ANISOU 1528 CE1 TYR A 281 4158 5490 5986 -126 121 650 C ATOM 1529 CE2 TYR A 281 7.416 40.803 130.321 1.00 34.78 C ANISOU 1529 CE2 TYR A 281 3461 4816 4937 -32 296 586 C ATOM 1530 CZ TYR A 281 6.468 39.816 130.083 1.00 35.96 C ANISOU 1530 CZ TYR A 281 3516 4893 5253 -72 277 674 C ATOM 1531 OH TYR A 281 5.486 39.527 131.001 1.00 34.18 O ANISOU 1531 OH TYR A 281 3223 4635 5129 -53 410 800 O ATOM 1532 N PHE A 282 10.259 41.680 123.826 1.00 28.50 N ANISOU 1532 N PHE A 282 2929 3904 3996 -27 -148 235 N ATOM 1533 CA PHE A 282 11.369 42.157 123.011 1.00 27.51 C ANISOU 1533 CA PHE A 282 2881 3783 3790 29 -121 190 C ATOM 1534 C PHE A 282 10.872 42.834 121.737 1.00 32.66 C ANISOU 1534 C PHE A 282 3608 4369 4434 39 -178 147 C ATOM 1535 O PHE A 282 11.068 44.040 121.557 1.00 30.01 O ANISOU 1535 O PHE A 282 3248 4078 4076 49 -137 117 O ATOM 1536 CB PHE A 282 12.319 41.016 122.665 1.00 32.08 C ANISOU 1536 CB PHE A 282 3550 4314 4324 81 -112 204 C ATOM 1537 CG PHE A 282 13.579 41.463 121.974 1.00 31.45 C ANISOU 1537 CG PHE A 282 3523 4237 4189 157 -36 195 C ATOM 1538 CD1 PHE A 282 14.601 42.062 122.695 1.00 34.69 C ANISOU 1538 CD1 PHE A 282 3834 4733 4613 166 35 220 C ATOM 1539 CD2 PHE A 282 13.745 41.275 120.609 1.00 31.62 C ANISOU 1539 CD2 PHE A 282 3705 4155 4153 226 -38 175 C ATOM 1540 CE1 PHE A 282 15.775 42.493 122.065 1.00 34.88 C ANISOU 1540 CE1 PHE A 282 3868 4749 4635 234 115 242 C ATOM 1541 CE2 PHE A 282 14.920 41.678 119.971 1.00 35.67 C ANISOU 1541 CE2 PHE A 282 4262 4660 4631 316 75 192 C ATOM 1542 CZ PHE A 282 15.939 42.301 120.707 1.00 28.83 C ANISOU 1542 CZ PHE A 282 3245 3890 3821 315 158 235 C ATOM 1543 N CYS A 283 10.224 42.070 120.853 1.00 28.16 N ANISOU 1543 N CYS A 283 3145 3677 3879 34 -290 144 N ATOM 1544 CA CYS A 283 9.780 42.621 119.575 1.00 28.43 C ANISOU 1544 CA CYS A 283 3296 3618 3887 51 -374 101 C ATOM 1545 C CYS A 283 8.754 43.734 119.762 1.00 32.99 C ANISOU 1545 C CYS A 283 3754 4232 4550 -4 -404 100 C ATOM 1546 O CYS A 283 8.854 44.790 119.120 1.00 31.14 O ANISOU 1546 O CYS A 283 3559 4001 4271 21 -390 58 O ATOM 1547 CB CYS A 283 9.202 41.511 118.702 1.00 31.22 C ANISOU 1547 CB CYS A 283 3815 3805 4243 47 -536 103 C ATOM 1548 SG CYS A 283 10.470 40.351 118.130 1.00 37.51 S ANISOU 1548 SG CYS A 283 4831 4524 4898 153 -482 96 S ATOM 1549 N LEU A 284 7.763 43.519 120.642 1.00 27.87 N ANISOU 1549 N LEU A 284 2957 3603 4030 -70 -427 157 N ATOM 1550 CA LEU A 284 6.698 44.507 120.793 1.00 31.99 C ANISOU 1550 CA LEU A 284 3361 4141 4655 -107 -441 177 C ATOM 1551 C LEU A 284 7.208 45.821 121.385 1.00 33.64 C ANISOU 1551 C LEU A 284 3511 4475 4797 -78 -299 145 C ATOM 1552 O LEU A 284 6.896 46.884 120.821 1.00 33.10 O ANISOU 1552 O LEU A 284 3450 4401 4727 -72 -316 113 O ATOM 1553 CB LEU A 284 5.543 43.909 121.598 1.00 36.92 C ANISOU 1553 CB LEU A 284 3833 4740 5455 -165 -464 275 C ATOM 1554 CG LEU A 284 4.403 44.870 121.941 1.00 49.97 C ANISOU 1554 CG LEU A 284 5332 6409 7247 -187 -433 330 C ATOM 1555 CD1 LEU A 284 3.785 45.456 120.674 1.00 48.70 C ANISOU 1555 CD1 LEU A 284 5218 6149 7136 -204 -591 303 C ATOM 1556 CD2 LEU A 284 3.353 44.162 122.788 1.00 54.82 C ANISOU 1556 CD2 LEU A 284 5783 6989 8059 -228 -413 461 C ATOM 1557 N PRO A 285 7.988 45.843 122.475 1.00 32.87 N ANISOU 1557 N PRO A 285 3375 4475 4641 -61 -180 152 N ATOM 1558 CA PRO A 285 8.525 47.137 122.935 1.00 30.71 C ANISOU 1558 CA PRO A 285 3083 4289 4298 -38 -90 119 C ATOM 1559 C PRO A 285 9.516 47.766 121.961 1.00 33.28 C ANISOU 1559 C PRO A 285 3494 4611 4541 -5 -94 60 C ATOM 1560 O PRO A 285 9.609 49.001 121.898 1.00 30.88 O ANISOU 1560 O PRO A 285 3180 4342 4211 2 -64 31 O ATOM 1561 CB PRO A 285 9.193 46.792 124.275 1.00 34.55 C ANISOU 1561 CB PRO A 285 3547 4842 4739 -31 -12 146 C ATOM 1562 CG PRO A 285 9.426 45.272 124.218 1.00 34.03 C ANISOU 1562 CG PRO A 285 3504 4735 4692 -37 -49 176 C ATOM 1563 CD PRO A 285 8.294 44.749 123.422 1.00 30.12 C ANISOU 1563 CD PRO A 285 3002 4148 4295 -66 -141 198 C ATOM 1564 N LEU A 286 10.274 46.964 121.207 1.00 28.09 N ANISOU 1564 N LEU A 286 2928 3903 3842 27 -114 53 N ATOM 1565 CA LEU A 286 11.126 47.537 120.171 1.00 31.12 C ANISOU 1565 CA LEU A 286 3402 4262 4161 79 -85 22 C ATOM 1566 C LEU A 286 10.291 48.219 119.097 1.00 31.43 C ANISOU 1566 C LEU A 286 3512 4232 4196 81 -153 -16 C ATOM 1567 O LEU A 286 10.590 49.351 118.698 1.00 31.33 O ANISOU 1567 O LEU A 286 3512 4240 4153 101 -113 -42 O ATOM 1568 CB LEU A 286 12.019 46.472 119.545 1.00 32.75 C ANISOU 1568 CB LEU A 286 3717 4406 4319 139 -62 38 C ATOM 1569 CG LEU A 286 13.216 46.056 120.389 1.00 46.51 C ANISOU 1569 CG LEU A 286 5389 6213 6070 155 19 83 C ATOM 1570 CD1 LEU A 286 14.122 45.116 119.585 1.00 40.21 C ANISOU 1570 CD1 LEU A 286 4707 5339 5231 240 73 111 C ATOM 1571 CD2 LEU A 286 13.976 47.286 120.853 1.00 54.36 C ANISOU 1571 CD2 LEU A 286 6289 7283 7082 147 77 90 C ATOM 1572 N ALA A 287 9.208 47.571 118.657 1.00 24.40 N ANISOU 1572 N ALA A 287 2665 3252 3354 54 -275 -11 N ATOM 1573 CA ALA A 287 8.348 48.196 117.657 1.00 31.05 C ANISOU 1573 CA ALA A 287 3577 4010 4209 50 -380 -40 C ATOM 1574 C ALA A 287 7.691 49.464 118.208 1.00 34.08 C ANISOU 1574 C ALA A 287 3820 4470 4658 16 -348 -40 C ATOM 1575 O ALA A 287 7.606 50.482 117.513 1.00 34.16 O ANISOU 1575 O ALA A 287 3880 4464 4636 34 -358 -76 O ATOM 1576 CB ALA A 287 7.291 47.203 117.173 1.00 27.50 C ANISOU 1576 CB ALA A 287 3187 3427 3834 12 -560 -17 C ATOM 1577 N ILE A 288 7.226 49.424 119.458 1.00 31.76 N ANISOU 1577 N ILE A 288 3371 4251 4445 -22 -297 5 N ATOM 1578 CA ILE A 288 6.506 50.562 120.014 1.00 31.00 C ANISOU 1578 CA ILE A 288 3167 4207 4405 -35 -250 16 C ATOM 1579 C ILE A 288 7.440 51.764 120.176 1.00 35.20 C ANISOU 1579 C ILE A 288 3726 4817 4833 -4 -155 -33 C ATOM 1580 O ILE A 288 7.089 52.887 119.801 1.00 31.61 O ANISOU 1580 O ILE A 288 3273 4361 4377 3 -158 -59 O ATOM 1581 CB ILE A 288 5.844 50.187 121.349 1.00 31.02 C ANISOU 1581 CB ILE A 288 3036 4252 4498 -54 -181 90 C ATOM 1582 CG1 ILE A 288 4.645 49.280 121.113 1.00 33.96 C ANISOU 1582 CG1 ILE A 288 3337 4530 5037 -96 -287 165 C ATOM 1583 CG2 ILE A 288 5.400 51.466 122.104 1.00 27.93 C ANISOU 1583 CG2 ILE A 288 2578 3921 4114 -33 -77 100 C ATOM 1584 CD1 ILE A 288 3.994 48.821 122.415 1.00 43.55 C ANISOU 1584 CD1 ILE A 288 4415 5774 6359 -103 -186 263 C ATOM 1585 N THR A 289 8.638 51.550 120.745 1.00 31.47 N ANISOU 1585 N THR A 289 3267 4402 4289 9 -85 -38 N ATOM 1586 CA THR A 289 9.552 52.666 120.970 1.00 33.00 C ANISOU 1586 CA THR A 289 3469 4650 4418 23 -26 -65 C ATOM 1587 C THR A 289 10.117 53.193 119.656 1.00 37.01 C ANISOU 1587 C THR A 289 4060 5114 4886 53 -34 -98 C ATOM 1588 O THR A 289 10.298 54.405 119.503 1.00 29.55 O ANISOU 1588 O THR A 289 3118 4188 3922 57 -11 -121 O ATOM 1589 CB THR A 289 10.688 52.273 121.926 1.00 31.90 C ANISOU 1589 CB THR A 289 3310 4561 4248 21 16 -42 C ATOM 1590 OG1 THR A 289 11.405 51.135 121.409 1.00 29.39 O ANISOU 1590 OG1 THR A 289 3026 4212 3930 40 12 -23 O ATOM 1591 CG2 THR A 289 10.146 51.970 123.302 1.00 23.45 C ANISOU 1591 CG2 THR A 289 2199 3526 3185 6 39 -13 C ATOM 1592 N ALA A 290 10.395 52.304 118.694 1.00 29.15 N ANISOU 1592 N ALA A 290 3157 4049 3871 85 -58 -95 N ATOM 1593 CA ALA A 290 10.859 52.759 117.384 1.00 29.93 C ANISOU 1593 CA ALA A 290 3377 4082 3912 138 -42 -116 C ATOM 1594 C ALA A 290 9.788 53.578 116.680 1.00 29.10 C ANISOU 1594 C ALA A 290 3318 3929 3809 131 -118 -154 C ATOM 1595 O ALA A 290 10.095 54.564 115.995 1.00 31.60 O ANISOU 1595 O ALA A 290 3693 4230 4085 161 -85 -176 O ATOM 1596 CB ALA A 290 11.266 51.566 116.513 1.00 27.22 C ANISOU 1596 CB ALA A 290 3178 3646 3519 197 -46 -103 C ATOM 1597 N PHE A 291 8.524 53.174 116.824 1.00 22.68 N ANISOU 1597 N PHE A 291 2471 3083 3065 91 -224 -150 N ATOM 1598 CA PHE A 291 7.425 53.928 116.235 1.00 24.99 C ANISOU 1598 CA PHE A 291 2775 3321 3397 78 -316 -169 C ATOM 1599 C PHE A 291 7.311 55.316 116.852 1.00 30.08 C ANISOU 1599 C PHE A 291 3321 4053 4057 67 -242 -180 C ATOM 1600 O PHE A 291 7.191 56.313 116.135 1.00 26.33 O ANISOU 1600 O PHE A 291 2903 3550 3552 86 -256 -211 O ATOM 1601 CB PHE A 291 6.116 53.167 116.412 1.00 26.99 C ANISOU 1601 CB PHE A 291 2961 3516 3778 30 -445 -127 C ATOM 1602 CG PHE A 291 4.927 53.893 115.892 1.00 29.50 C ANISOU 1602 CG PHE A 291 3255 3769 4183 11 -556 -122 C ATOM 1603 CD1 PHE A 291 4.642 53.901 114.528 1.00 36.08 C ANISOU 1603 CD1 PHE A 291 4263 4468 4980 28 -708 -153 C ATOM 1604 CD2 PHE A 291 4.082 54.556 116.756 1.00 31.25 C ANISOU 1604 CD2 PHE A 291 3299 4051 4523 -13 -509 -79 C ATOM 1605 CE1 PHE A 291 3.525 54.572 114.036 1.00 39.77 C ANISOU 1605 CE1 PHE A 291 4702 4863 5546 7 -839 -141 C ATOM 1606 CE2 PHE A 291 2.966 55.235 116.278 1.00 35.39 C ANISOU 1606 CE2 PHE A 291 3779 4511 5157 -24 -607 -57 C ATOM 1607 CZ PHE A 291 2.684 55.242 114.914 1.00 36.19 C ANISOU 1607 CZ PHE A 291 4030 4480 5240 -22 -786 -88 C ATOM 1608 N PHE A 292 7.298 55.401 118.184 1.00 27.64 N ANISOU 1608 N PHE A 292 2887 3832 3782 44 -168 -153 N ATOM 1609 CA PHE A 292 7.126 56.709 118.805 1.00 31.66 C ANISOU 1609 CA PHE A 292 3344 4399 4286 45 -106 -165 C ATOM 1610 C PHE A 292 8.373 57.559 118.661 1.00 35.22 C ANISOU 1610 C PHE A 292 3849 4883 4651 59 -51 -198 C ATOM 1611 O PHE A 292 8.266 58.788 118.538 1.00 29.05 O ANISOU 1611 O PHE A 292 3079 4107 3850 65 -38 -224 O ATOM 1612 CB PHE A 292 6.706 56.571 120.270 1.00 24.69 C ANISOU 1612 CB PHE A 292 2368 3572 3439 37 -39 -123 C ATOM 1613 CG PHE A 292 5.222 56.373 120.420 1.00 30.48 C ANISOU 1613 CG PHE A 292 3012 4270 4301 35 -58 -67 C ATOM 1614 CD1 PHE A 292 4.359 57.449 120.293 1.00 25.67 C ANISOU 1614 CD1 PHE A 292 2368 3645 3739 54 -47 -61 C ATOM 1615 CD2 PHE A 292 4.690 55.106 120.600 1.00 28.85 C ANISOU 1615 CD2 PHE A 292 2743 4029 4190 13 -94 -7 C ATOM 1616 CE1 PHE A 292 2.989 57.272 120.381 1.00 29.84 C ANISOU 1616 CE1 PHE A 292 2780 4126 4431 55 -61 19 C ATOM 1617 CE2 PHE A 292 3.324 54.924 120.705 1.00 29.63 C ANISOU 1617 CE2 PHE A 292 2725 4078 4456 4 -117 74 C ATOM 1618 CZ PHE A 292 2.474 55.997 120.594 1.00 36.71 C ANISOU 1618 CZ PHE A 292 3567 4959 5422 27 -98 94 C ATOM 1619 N TYR A 293 9.552 56.928 118.643 1.00 27.99 N ANISOU 1619 N TYR A 293 2956 3976 3703 65 -20 -185 N ATOM 1620 CA TYR A 293 10.775 57.666 118.348 1.00 31.60 C ANISOU 1620 CA TYR A 293 3438 4441 4129 78 30 -185 C ATOM 1621 C TYR A 293 10.709 58.273 116.955 1.00 33.01 C ANISOU 1621 C TYR A 293 3712 4555 4277 116 29 -208 C ATOM 1622 O TYR A 293 11.084 59.433 116.761 1.00 29.76 O ANISOU 1622 O TYR A 293 3305 4147 3855 118 58 -217 O ATOM 1623 CB TYR A 293 12.002 56.759 118.478 1.00 26.36 C ANISOU 1623 CB TYR A 293 2759 3781 3473 89 72 -139 C ATOM 1624 CG TYR A 293 13.302 57.434 118.086 1.00 29.27 C ANISOU 1624 CG TYR A 293 3120 4140 3862 106 133 -103 C ATOM 1625 CD1 TYR A 293 13.825 57.280 116.807 1.00 28.98 C ANISOU 1625 CD1 TYR A 293 3165 4037 3811 172 203 -78 C ATOM 1626 CD2 TYR A 293 14.006 58.233 118.993 1.00 30.70 C ANISOU 1626 CD2 TYR A 293 3224 4358 4084 62 118 -80 C ATOM 1627 CE1 TYR A 293 15.023 57.915 116.427 1.00 27.75 C ANISOU 1627 CE1 TYR A 293 2978 3860 3706 197 290 -15 C ATOM 1628 CE2 TYR A 293 15.209 58.875 118.622 1.00 28.82 C ANISOU 1628 CE2 TYR A 293 2945 4093 3911 66 160 -21 C ATOM 1629 CZ TYR A 293 15.707 58.694 117.340 1.00 31.92 C ANISOU 1629 CZ TYR A 293 3384 4430 4316 135 262 20 C ATOM 1630 OH TYR A 293 16.887 59.303 116.957 1.00 34.98 O ANISOU 1630 OH TYR A 293 3710 4781 4799 150 335 107 O ATOM 1631 N THR A 294 10.218 57.509 115.975 1.00 26.86 N ANISOU 1631 N THR A 294 3032 3698 3475 148 -16 -217 N ATOM 1632 CA THR A 294 10.121 58.031 114.616 1.00 29.03 C ANISOU 1632 CA THR A 294 3449 3887 3694 198 -28 -241 C ATOM 1633 C THR A 294 9.103 59.165 114.535 1.00 30.92 C ANISOU 1633 C THR A 294 3670 4127 3953 175 -90 -277 C ATOM 1634 O THR A 294 9.374 60.196 113.908 1.00 28.95 O ANISOU 1634 O THR A 294 3479 3856 3665 200 -57 -293 O ATOM 1635 CB THR A 294 9.772 56.915 113.626 1.00 29.80 C ANISOU 1635 CB THR A 294 3708 3871 3743 241 -100 -246 C ATOM 1636 OG1 THR A 294 10.767 55.888 113.687 1.00 29.96 O ANISOU 1636 OG1 THR A 294 3758 3886 3740 279 -20 -207 O ATOM 1637 CG2 THR A 294 9.705 57.452 112.183 1.00 26.80 C ANISOU 1637 CG2 THR A 294 3534 3376 3271 310 -117 -271 C ATOM 1638 N LEU A 295 7.920 58.996 115.153 1.00 26.38 N ANISOU 1638 N LEU A 295 3005 3569 3449 134 -168 -277 N ATOM 1639 CA LEU A 295 6.949 60.098 115.188 1.00 28.20 C ANISOU 1639 CA LEU A 295 3194 3801 3719 123 -205 -294 C ATOM 1640 C LEU A 295 7.567 61.336 115.813 1.00 32.23 C ANISOU 1640 C LEU A 295 3664 4385 4199 119 -112 -308 C ATOM 1641 O LEU A 295 7.366 62.461 115.331 1.00 26.23 O ANISOU 1641 O LEU A 295 2942 3604 3418 133 -116 -334 O ATOM 1642 CB LEU A 295 5.698 59.710 115.978 1.00 29.60 C ANISOU 1642 CB LEU A 295 3243 3990 4013 92 -253 -257 C ATOM 1643 CG LEU A 295 4.536 58.895 115.398 1.00 34.67 C ANISOU 1643 CG LEU A 295 3879 4535 4759 75 -400 -225 C ATOM 1644 CD1 LEU A 295 3.376 58.896 116.391 1.00 36.45 C ANISOU 1644 CD1 LEU A 295 3924 4787 5139 53 -386 -157 C ATOM 1645 CD2 LEU A 295 4.056 59.409 114.061 1.00 29.78 C ANISOU 1645 CD2 LEU A 295 3383 3807 4127 92 -528 -254 C ATOM 1646 N MET A 296 8.338 61.139 116.883 1.00 27.10 N ANISOU 1646 N MET A 296 2950 3804 3543 99 -47 -289 N ATOM 1647 CA MET A 296 8.924 62.249 117.623 1.00 25.59 C ANISOU 1647 CA MET A 296 2738 3658 3327 85 -1 -297 C ATOM 1648 C MET A 296 9.972 62.987 116.790 1.00 32.45 C ANISOU 1648 C MET A 296 3662 4499 4169 95 28 -299 C ATOM 1649 O MET A 296 9.997 64.228 116.759 1.00 27.26 O ANISOU 1649 O MET A 296 3022 3838 3497 91 31 -318 O ATOM 1650 CB MET A 296 9.545 61.727 118.924 1.00 22.90 C ANISOU 1650 CB MET A 296 2346 3369 2986 60 22 -270 C ATOM 1651 CG MET A 296 10.125 62.814 119.793 1.00 27.57 C ANISOU 1651 CG MET A 296 2951 3978 3545 40 24 -278 C ATOM 1652 SD MET A 296 11.109 62.246 121.197 1.00 32.00 S ANISOU 1652 SD MET A 296 3496 4566 4097 8 2 -244 S ATOM 1653 CE MET A 296 12.488 61.447 120.392 1.00 28.77 C ANISOU 1653 CE MET A 296 3031 4144 3754 -5 11 -193 C ATOM 1654 N THR A 297 10.863 62.245 116.119 1.00 27.27 N ANISOU 1654 N THR A 297 3035 3814 3512 117 65 -267 N ATOM 1655 CA THR A 297 11.903 62.914 115.342 1.00 33.75 C ANISOU 1655 CA THR A 297 3893 4598 4332 141 131 -238 C ATOM 1656 C THR A 297 11.330 63.580 114.094 1.00 29.78 C ANISOU 1656 C THR A 297 3510 4029 3777 185 127 -271 C ATOM 1657 O THR A 297 11.790 64.660 113.716 1.00 28.07 O ANISOU 1657 O THR A 297 3311 3792 3561 191 168 -261 O ATOM 1658 CB THR A 297 13.036 61.948 114.975 1.00 33.28 C ANISOU 1658 CB THR A 297 3834 4514 4296 176 211 -171 C ATOM 1659 OG1 THR A 297 12.522 60.865 114.204 1.00 37.75 O ANISOU 1659 OG1 THR A 297 4509 5028 4806 229 203 -186 O ATOM 1660 CG2 THR A 297 13.715 61.410 116.229 1.00 32.98 C ANISOU 1660 CG2 THR A 297 3672 4535 4323 127 198 -130 C ATOM 1661 N CYS A 298 10.322 62.978 113.460 1.00 23.19 N ANISOU 1661 N CYS A 298 2762 3146 2905 213 60 -305 N ATOM 1662 CA ACYS A 298 9.586 63.683 112.409 0.70 26.14 C ANISOU 1662 CA ACYS A 298 3256 3446 3231 246 11 -342 C ATOM 1663 CA BCYS A 298 9.584 63.681 112.413 0.30 27.61 C ANISOU 1663 CA BCYS A 298 3442 3633 3418 246 10 -342 C ATOM 1664 C CYS A 298 9.015 65.002 112.932 1.00 31.87 C ANISOU 1664 C CYS A 298 3910 4214 3984 211 -15 -371 C ATOM 1665 O CYS A 298 9.128 66.050 112.279 1.00 29.18 O ANISOU 1665 O CYS A 298 3638 3838 3612 232 5 -384 O ATOM 1666 CB ACYS A 298 8.465 62.795 111.868 0.70 32.02 C ANISOU 1666 CB ACYS A 298 4082 4118 3966 259 -117 -365 C ATOM 1667 CB BCYS A 298 8.466 62.782 111.889 0.30 31.57 C ANISOU 1667 CB BCYS A 298 4022 4062 3910 258 -117 -365 C ATOM 1668 SG ACYS A 298 9.050 61.414 110.850 0.70 34.76 S ANISOU 1668 SG ACYS A 298 4623 4357 4227 331 -106 -345 S ATOM 1669 SG BCYS A 298 7.301 63.643 110.804 0.30 35.97 S ANISOU 1669 SG BCYS A 298 4705 4520 4441 282 -243 -407 S ATOM 1670 N GLU A 299 8.418 64.981 114.123 1.00 29.98 N ANISOU 1670 N GLU A 299 3552 4044 3797 168 -43 -376 N ATOM 1671 CA GLU A 299 7.855 66.213 114.669 1.00 33.48 C ANISOU 1671 CA GLU A 299 3957 4514 4251 155 -49 -399 C ATOM 1672 C GLU A 299 8.956 67.201 115.022 1.00 33.13 C ANISOU 1672 C GLU A 299 3912 4492 4185 136 7 -394 C ATOM 1673 O GLU A 299 8.815 68.408 114.789 1.00 32.76 O ANISOU 1673 O GLU A 299 3903 4426 4120 141 4 -416 O ATOM 1674 CB GLU A 299 6.987 65.901 115.890 1.00 35.40 C ANISOU 1674 CB GLU A 299 4103 4806 4543 140 -57 -388 C ATOM 1675 CG GLU A 299 6.195 67.096 116.442 1.00 36.39 C ANISOU 1675 CG GLU A 299 4213 4941 4674 156 -43 -402 C ATOM 1676 CD GLU A 299 5.088 67.595 115.508 1.00 46.22 C ANISOU 1676 CD GLU A 299 5473 6127 5960 184 -102 -411 C ATOM 1677 OE1 GLU A 299 4.702 68.771 115.635 1.00 50.45 O ANISOU 1677 OE1 GLU A 299 6026 6658 6486 205 -83 -426 O ATOM 1678 OE2 GLU A 299 4.597 66.831 114.654 1.00 46.26 O ANISOU 1678 OE2 GLU A 299 5489 6078 6009 186 -184 -400 O ATOM 1679 N MET A 300 10.076 66.710 115.563 1.00 27.92 N ANISOU 1679 N MET A 300 3206 3860 3544 109 41 -356 N ATOM 1680 CA MET A 300 11.179 67.611 115.871 1.00 27.97 C ANISOU 1680 CA MET A 300 3195 3863 3571 77 59 -329 C ATOM 1681 C MET A 300 11.705 68.314 114.619 1.00 31.84 C ANISOU 1681 C MET A 300 3741 4292 4062 104 110 -308 C ATOM 1682 O MET A 300 12.134 69.471 114.700 1.00 29.34 O ANISOU 1682 O MET A 300 3424 3956 3766 79 105 -299 O ATOM 1683 CB MET A 300 12.311 66.859 116.561 1.00 27.87 C ANISOU 1683 CB MET A 300 3105 3871 3613 43 68 -271 C ATOM 1684 CG MET A 300 12.057 66.539 118.049 1.00 29.83 C ANISOU 1684 CG MET A 300 3324 4164 3847 9 10 -285 C ATOM 1685 SD MET A 300 13.375 65.437 118.661 1.00 31.87 S ANISOU 1685 SD MET A 300 3497 4435 4178 -26 2 -210 S ATOM 1686 CE MET A 300 12.989 65.370 120.408 1.00 30.37 C ANISOU 1686 CE MET A 300 3338 4271 3931 -54 -79 -238 C ATOM 1687 N LEU A 301 11.709 67.634 113.465 1.00 27.00 N ANISOU 1687 N LEU A 301 3201 3635 3424 162 160 -295 N ATOM 1688 CA LEU A 301 12.129 68.292 112.231 1.00 28.27 C ANISOU 1688 CA LEU A 301 3456 3722 3562 212 232 -270 C ATOM 1689 C LEU A 301 11.247 69.507 111.916 1.00 30.55 C ANISOU 1689 C LEU A 301 3810 3991 3806 214 178 -330 C ATOM 1690 O LEU A 301 11.758 70.570 111.555 1.00 26.24 O ANISOU 1690 O LEU A 301 3284 3412 3274 213 220 -307 O ATOM 1691 CB LEU A 301 12.113 67.299 111.075 1.00 30.34 C ANISOU 1691 CB LEU A 301 3853 3915 3760 296 285 -257 C ATOM 1692 CG LEU A 301 12.324 67.903 109.680 1.00 35.65 C ANISOU 1692 CG LEU A 301 4691 4486 4366 377 365 -239 C ATOM 1693 CD1 LEU A 301 13.687 68.582 109.590 1.00 40.57 C ANISOU 1693 CD1 LEU A 301 5244 5094 5077 381 508 -137 C ATOM 1694 CD2 LEU A 301 12.162 66.864 108.566 1.00 38.80 C ANISOU 1694 CD2 LEU A 301 5296 4788 4659 476 392 -239 C ATOM 1695 N ARG A 302 9.922 69.368 112.052 1.00 25.21 N ANISOU 1695 N ARG A 302 3155 3327 3098 216 87 -393 N ATOM 1696 CA ARG A 302 9.018 70.492 111.819 1.00 32.89 C ANISOU 1696 CA ARG A 302 4171 4278 4047 224 34 -440 C ATOM 1697 C ARG A 302 9.243 71.608 112.822 1.00 31.51 C ANISOU 1697 C ARG A 302 3931 4145 3896 178 36 -446 C ATOM 1698 O ARG A 302 9.176 72.786 112.462 1.00 31.88 O ANISOU 1698 O ARG A 302 4030 4159 3924 184 35 -462 O ATOM 1699 CB ARG A 302 7.556 70.043 111.894 1.00 31.92 C ANISOU 1699 CB ARG A 302 4039 4154 3936 234 -63 -475 C ATOM 1700 CG ARG A 302 7.156 68.985 110.890 1.00 42.12 C ANISOU 1700 CG ARG A 302 5426 5373 5205 271 -124 -474 C ATOM 1701 CD ARG A 302 5.706 68.582 111.142 1.00 53.50 C ANISOU 1701 CD ARG A 302 6805 6805 6718 260 -245 -483 C ATOM 1702 NE ARG A 302 4.768 69.288 110.273 1.00 58.24 N ANISOU 1702 NE ARG A 302 7484 7324 7321 288 -345 -503 N ATOM 1703 CZ ARG A 302 3.503 69.546 110.587 1.00 59.29 C ANISOU 1703 CZ ARG A 302 7522 7451 7556 280 -428 -493 C ATOM 1704 NH1 ARG A 302 2.725 70.184 109.724 1.00 56.70 N ANISOU 1704 NH1 ARG A 302 7267 7037 7240 305 -534 -504 N ATOM 1705 NH2 ARG A 302 3.022 69.187 111.769 1.00 69.15 N ANISOU 1705 NH2 ARG A 302 8603 8770 8900 256 -395 -458 N ATOM 1706 N LYS A 303 9.460 71.259 114.100 1.00 27.18 N ANISOU 1706 N LYS A 303 3297 3655 3376 136 25 -437 N ATOM 1707 CA LYS A 303 9.779 72.270 115.099 1.00 26.13 C ANISOU 1707 CA LYS A 303 3154 3531 3242 97 2 -444 C ATOM 1708 C LYS A 303 11.056 73.017 114.733 1.00 31.79 C ANISOU 1708 C LYS A 303 3873 4206 4001 62 18 -397 C ATOM 1709 O LYS A 303 11.153 74.234 114.941 1.00 31.98 O ANISOU 1709 O LYS A 303 3936 4197 4018 41 -16 -409 O ATOM 1710 CB LYS A 303 9.934 71.638 116.489 1.00 27.00 C ANISOU 1710 CB LYS A 303 3215 3687 3357 67 -22 -435 C ATOM 1711 CG LYS A 303 8.715 70.915 117.009 1.00 33.64 C ANISOU 1711 CG LYS A 303 4035 4565 4181 104 -14 -456 C ATOM 1712 CD LYS A 303 7.533 71.864 117.252 1.00 32.44 C ANISOU 1712 CD LYS A 303 3928 4398 3998 149 -9 -489 C ATOM 1713 CE LYS A 303 6.247 71.052 117.400 1.00 34.99 C ANISOU 1713 CE LYS A 303 4188 4740 4365 191 14 -474 C ATOM 1714 NZ LYS A 303 5.068 71.940 117.613 1.00 33.23 N ANISOU 1714 NZ LYS A 303 3982 4496 4148 249 43 -479 N ATOM 1715 N ASN A1000 12.061 72.298 114.222 1.00 29.81 N ANISOU 1715 N ASN A1000 3575 3943 3809 60 75 -329 N ATOM 1716 CA ASN A1000 13.332 72.940 113.898 1.00 28.21 C ANISOU 1716 CA ASN A1000 3335 3689 3697 29 111 -247 C ATOM 1717 C ASN A1000 13.182 73.922 112.741 1.00 24.98 C ANISOU 1717 C ASN A1000 3011 3220 3261 69 165 -249 C ATOM 1718 O ASN A1000 13.792 74.993 112.756 1.00 28.39 O ANISOU 1718 O ASN A1000 3427 3606 3754 30 153 -209 O ATOM 1719 CB ASN A1000 14.392 71.886 113.568 1.00 27.17 C ANISOU 1719 CB ASN A1000 3124 3549 3651 42 198 -151 C ATOM 1720 CG ASN A1000 14.991 71.253 114.817 1.00 39.17 C ANISOU 1720 CG ASN A1000 4535 5104 5242 -22 125 -118 C ATOM 1721 OD1 ASN A1000 14.907 71.810 115.902 1.00 38.91 O ANISOU 1721 OD1 ASN A1000 4500 5078 5206 -83 6 -149 O ATOM 1722 ND2 ASN A1000 15.585 70.079 114.663 1.00 33.49 N ANISOU 1722 ND2 ASN A1000 3753 4396 4576 2 193 -55 N ATOM 1723 N ILE A1001 12.399 73.560 111.718 1.00 21.59 N ANISOU 1723 N ILE A1001 2683 2775 2744 145 208 -289 N ATOM 1724 CA ILE A1001 12.166 74.476 110.604 1.00 27.86 C ANISOU 1724 CA ILE A1001 3592 3503 3492 192 248 -297 C ATOM 1725 C ILE A1001 11.451 75.730 111.099 1.00 27.11 C ANISOU 1725 C ILE A1001 3517 3415 3370 159 159 -362 C ATOM 1726 O ILE A1001 11.786 76.851 110.706 1.00 28.69 O ANISOU 1726 O ILE A1001 3754 3564 3585 152 177 -342 O ATOM 1727 CB ILE A1001 11.388 73.760 109.481 1.00 24.60 C ANISOU 1727 CB ILE A1001 3319 3050 2977 280 265 -334 C ATOM 1728 CG1 ILE A1001 12.150 72.494 109.075 1.00 35.37 C ANISOU 1728 CG1 ILE A1001 4694 4394 4350 324 361 -268 C ATOM 1729 CG2 ILE A1001 11.293 74.658 108.240 1.00 37.13 C ANISOU 1729 CG2 ILE A1001 5059 4547 4501 341 311 -332 C ATOM 1730 CD1 ILE A1001 11.456 71.635 108.003 1.00 35.56 C ANISOU 1730 CD1 ILE A1001 4904 4351 4257 413 349 -304 C ATOM 1731 N PHE A1002 10.466 75.557 111.982 1.00 24.17 N ANISOU 1731 N PHE A1002 3124 3096 2963 148 76 -430 N ATOM 1732 CA PHE A1002 9.808 76.695 112.610 1.00 25.63 C ANISOU 1732 CA PHE A1002 3339 3282 3119 135 14 -481 C ATOM 1733 C PHE A1002 10.808 77.572 113.353 1.00 28.05 C ANISOU 1733 C PHE A1002 3624 3561 3471 66 -20 -448 C ATOM 1734 O PHE A1002 10.779 78.801 113.226 1.00 28.24 O ANISOU 1734 O PHE A1002 3711 3539 3482 58 -45 -461 O ATOM 1735 CB PHE A1002 8.708 76.183 113.550 1.00 23.66 C ANISOU 1735 CB PHE A1002 3061 3086 2843 152 -26 -527 C ATOM 1736 CG PHE A1002 8.018 77.256 114.328 1.00 28.17 C ANISOU 1736 CG PHE A1002 3681 3649 3374 164 -57 -568 C ATOM 1737 CD1 PHE A1002 6.982 77.981 113.760 1.00 31.89 C ANISOU 1737 CD1 PHE A1002 4203 4093 3822 218 -62 -600 C ATOM 1738 CD2 PHE A1002 8.386 77.531 115.631 1.00 33.42 C ANISOU 1738 CD2 PHE A1002 4362 4318 4017 133 -88 -570 C ATOM 1739 CE1 PHE A1002 6.331 78.978 114.481 1.00 36.78 C ANISOU 1739 CE1 PHE A1002 4877 4696 4403 248 -67 -629 C ATOM 1740 CE2 PHE A1002 7.750 78.521 116.346 1.00 39.70 C ANISOU 1740 CE2 PHE A1002 5250 5085 4750 167 -102 -606 C ATOM 1741 CZ PHE A1002 6.718 79.242 115.772 1.00 35.43 C ANISOU 1741 CZ PHE A1002 4747 4525 4191 229 -77 -633 C ATOM 1742 N GLU A1003 11.689 76.965 114.159 1.00 30.96 N ANISOU 1742 N GLU A1003 3913 3949 3903 12 -43 -401 N ATOM 1743 CA GLU A1003 12.631 77.764 114.937 1.00 32.74 C ANISOU 1743 CA GLU A1003 4125 4124 4192 -67 -129 -361 C ATOM 1744 C GLU A1003 13.629 78.465 114.034 1.00 34.27 C ANISOU 1744 C GLU A1003 4283 4247 4492 -95 -88 -275 C ATOM 1745 O GLU A1003 14.047 79.591 114.321 1.00 28.26 O ANISOU 1745 O GLU A1003 3548 3418 3773 -150 -169 -256 O ATOM 1746 CB GLU A1003 13.386 76.895 115.945 1.00 30.32 C ANISOU 1746 CB GLU A1003 3738 3836 3946 -121 -187 -317 C ATOM 1747 CG GLU A1003 12.502 76.228 116.970 1.00 43.33 C ANISOU 1747 CG GLU A1003 5430 5541 5491 -92 -216 -386 C ATOM 1748 CD GLU A1003 12.446 76.985 118.283 1.00 53.29 C ANISOU 1748 CD GLU A1003 6806 6755 6688 -120 -339 -422 C ATOM 1749 OE1 GLU A1003 12.893 78.161 118.335 1.00 42.58 O ANISOU 1749 OE1 GLU A1003 5512 5317 5349 -163 -422 -413 O ATOM 1750 OE2 GLU A1003 11.960 76.382 119.268 1.00 58.18 O ANISOU 1750 OE2 GLU A1003 7471 7403 7230 -94 -351 -454 O ATOM 1751 N MET A1004 14.033 77.800 112.952 1.00 27.60 N ANISOU 1751 N MET A1004 3393 3402 3693 -51 42 -212 N ATOM 1752 CA MET A1004 14.950 78.401 111.993 1.00 30.29 C ANISOU 1752 CA MET A1004 3706 3666 4139 -50 133 -107 C ATOM 1753 C MET A1004 14.346 79.654 111.363 1.00 29.74 C ANISOU 1753 C MET A1004 3755 3551 3995 -24 133 -156 C ATOM 1754 O MET A1004 14.985 80.714 111.320 1.00 29.30 O ANISOU 1754 O MET A1004 3680 3422 4029 -76 107 -96 O ATOM 1755 CB MET A1004 15.301 77.370 110.920 1.00 26.53 C ANISOU 1755 CB MET A1004 3221 3187 3674 33 304 -40 C ATOM 1756 CG MET A1004 16.209 77.875 109.823 1.00 28.62 C ANISOU 1756 CG MET A1004 3477 3361 4035 70 458 88 C ATOM 1757 SD MET A1004 16.089 76.824 108.368 1.00 30.47 S ANISOU 1757 SD MET A1004 3846 3566 4163 224 667 114 S ATOM 1758 CE MET A1004 17.792 76.702 107.850 1.00 35.27 C ANISOU 1758 CE MET A1004 4320 4089 4993 253 881 344 C ATOM 1759 N LEU A1005 13.117 79.551 110.854 1.00 27.61 N ANISOU 1759 N LEU A1005 3601 3311 3578 52 148 -256 N ATOM 1760 CA LEU A1005 12.515 80.707 110.196 1.00 28.79 C ANISOU 1760 CA LEU A1005 3867 3414 3660 84 145 -300 C ATOM 1761 C LEU A1005 12.083 81.758 111.202 1.00 33.34 C ANISOU 1761 C LEU A1005 4472 3986 4211 33 17 -363 C ATOM 1762 O LEU A1005 12.075 82.958 110.881 1.00 32.51 O ANISOU 1762 O LEU A1005 4433 3819 4100 26 1 -365 O ATOM 1763 CB LEU A1005 11.339 80.278 109.316 1.00 27.17 C ANISOU 1763 CB LEU A1005 3775 3220 3329 178 171 -374 C ATOM 1764 CG LEU A1005 11.723 79.858 107.886 1.00 30.40 C ANISOU 1764 CG LEU A1005 4274 3566 3712 257 300 -316 C ATOM 1765 CD1 LEU A1005 12.367 81.047 107.146 1.00 27.57 C ANISOU 1765 CD1 LEU A1005 3968 3119 3386 265 379 -250 C ATOM 1766 CD2 LEU A1005 12.652 78.671 107.873 1.00 32.20 C ANISOU 1766 CD2 LEU A1005 4425 3805 4004 265 395 -233 C ATOM 1767 N ARG A1006 11.760 81.346 112.430 1.00 28.57 N ANISOU 1767 N ARG A1006 3842 3433 3581 6 -67 -409 N ATOM 1768 CA ARG A1006 11.515 82.341 113.470 1.00 32.80 C ANISOU 1768 CA ARG A1006 4449 3936 4075 -29 -180 -457 C ATOM 1769 C ARG A1006 12.762 83.185 113.736 1.00 28.99 C ANISOU 1769 C ARG A1006 3945 3365 3707 -124 -261 -379 C ATOM 1770 O ARG A1006 12.672 84.409 113.903 1.00 29.19 O ANISOU 1770 O ARG A1006 4065 3319 3706 -144 -334 -402 O ATOM 1771 CB ARG A1006 11.037 81.658 114.749 1.00 31.43 C ANISOU 1771 CB ARG A1006 4282 3815 3844 -24 -233 -504 C ATOM 1772 CG ARG A1006 10.790 82.670 115.869 1.00 36.93 C ANISOU 1772 CG ARG A1006 5114 4455 4464 -34 -338 -552 C ATOM 1773 CD ARG A1006 10.338 82.019 117.171 1.00 33.13 C ANISOU 1773 CD ARG A1006 4680 4006 3903 -8 -365 -589 C ATOM 1774 NE ARG A1006 9.890 83.052 118.101 1.00 42.30 N ANISOU 1774 NE ARG A1006 6031 5093 4947 25 -431 -641 N ATOM 1775 CZ ARG A1006 9.320 82.808 119.278 1.00 47.29 C ANISOU 1775 CZ ARG A1006 6778 5721 5468 83 -430 -676 C ATOM 1776 NH1 ARG A1006 9.129 81.558 119.670 1.00 39.92 N ANISOU 1776 NH1 ARG A1006 5763 4863 4542 103 -374 -662 N ATOM 1777 NH2 ARG A1006 8.925 83.815 120.051 1.00 47.21 N ANISOU 1777 NH2 ARG A1006 6983 5622 5331 135 -472 -719 N ATOM 1778 N ILE A1007 13.936 82.547 113.797 1.00 27.76 N ANISOU 1778 N ILE A1007 3656 3197 3694 -186 -259 -276 N ATOM 1779 CA ILE A1007 15.187 83.287 113.985 1.00 31.27 C ANISOU 1779 CA ILE A1007 4035 3538 4307 -288 -350 -167 C ATOM 1780 C ILE A1007 15.454 84.205 112.795 1.00 34.54 C ANISOU 1780 C ILE A1007 4453 3888 4784 -275 -258 -107 C ATOM 1781 O ILE A1007 15.878 85.359 112.960 1.00 35.74 O ANISOU 1781 O ILE A1007 4633 3941 5006 -342 -360 -71 O ATOM 1782 CB ILE A1007 16.360 82.304 114.214 1.00 34.17 C ANISOU 1782 CB ILE A1007 4225 3906 4853 -344 -348 -44 C ATOM 1783 CG1 ILE A1007 16.334 81.755 115.643 1.00 37.00 C ANISOU 1783 CG1 ILE A1007 4607 4283 5170 -389 -507 -90 C ATOM 1784 CG2 ILE A1007 17.738 82.994 113.930 1.00 34.60 C ANISOU 1784 CG2 ILE A1007 4147 3840 5160 -437 -385 126 C ATOM 1785 CD1 ILE A1007 17.066 80.392 115.831 1.00 37.18 C ANISOU 1785 CD1 ILE A1007 4470 4351 5308 -405 -471 -7 C ATOM 1786 N ASP A1008 15.212 83.717 111.575 1.00 31.37 N ANISOU 1786 N ASP A1008 4046 3523 4350 -185 -71 -91 N ATOM 1787 CA ASP A1008 15.570 84.514 110.398 1.00 35.25 C ANISOU 1787 CA ASP A1008 4558 3939 4898 -158 42 -15 C ATOM 1788 C ASP A1008 14.516 85.555 110.009 1.00 40.18 C ANISOU 1788 C ASP A1008 5350 4547 5368 -111 19 -123 C ATOM 1789 O ASP A1008 14.882 86.624 109.506 1.00 38.83 O ANISOU 1789 O ASP A1008 5207 4290 5256 -131 33 -69 O ATOM 1790 CB ASP A1008 15.853 83.594 109.217 1.00 33.51 C ANISOU 1790 CB ASP A1008 4311 3731 4689 -64 257 60 C ATOM 1791 CG ASP A1008 17.189 82.891 109.345 1.00 36.26 C ANISOU 1791 CG ASP A1008 4473 4054 5250 -104 326 225 C ATOM 1792 OD1 ASP A1008 18.007 83.298 110.199 1.00 40.23 O ANISOU 1792 OD1 ASP A1008 4847 4509 5930 -220 194 304 O ATOM 1793 OD2 ASP A1008 17.424 81.934 108.597 1.00 37.77 O ANISOU 1793 OD2 ASP A1008 4655 4259 5437 -16 501 282 O ATOM 1794 N GLU A1009 13.220 85.284 110.211 1.00 34.15 N ANISOU 1794 N GLU A1009 4688 3857 4431 -47 -12 -261 N ATOM 1795 CA GLU A1009 12.172 86.210 109.782 1.00 34.90 C ANISOU 1795 CA GLU A1009 4926 3934 4401 11 -26 -350 C ATOM 1796 C GLU A1009 11.320 86.753 110.914 1.00 41.35 C ANISOU 1796 C GLU A1009 5818 4767 5126 3 -155 -453 C ATOM 1797 O GLU A1009 10.449 87.600 110.654 1.00 41.65 O ANISOU 1797 O GLU A1009 5968 4783 5075 54 -168 -518 O ATOM 1798 CB GLU A1009 11.242 85.547 108.748 1.00 31.24 C ANISOU 1798 CB GLU A1009 4532 3509 3828 119 63 -399 C ATOM 1799 CG GLU A1009 11.974 84.982 107.558 1.00 40.33 C ANISOU 1799 CG GLU A1009 5681 4623 5019 163 211 -306 C ATOM 1800 CD GLU A1009 11.097 84.851 106.330 1.00 43.38 C ANISOU 1800 CD GLU A1009 6225 4983 5275 272 261 -354 C ATOM 1801 OE1 GLU A1009 9.869 85.060 106.434 1.00 43.75 O ANISOU 1801 OE1 GLU A1009 6338 5054 5231 304 167 -455 O ATOM 1802 OE2 GLU A1009 11.646 84.545 105.255 1.00 36.85 O ANISOU 1802 OE2 GLU A1009 5465 4096 4440 333 395 -280 O ATOM 1803 N GLY A1010 11.538 86.300 112.149 1.00 35.19 N ANISOU 1803 N GLY A1010 4919 4023 4430 -765 205 -228 N ATOM 1804 CA GLY A1010 10.769 86.773 113.284 1.00 30.73 C ANISOU 1804 CA GLY A1010 4344 3469 3861 -730 108 -291 C ATOM 1805 C GLY A1010 9.414 86.103 113.362 1.00 32.33 C ANISOU 1805 C GLY A1010 4600 3681 4001 -583 21 -230 C ATOM 1806 O GLY A1010 8.870 85.663 112.345 1.00 34.09 O ANISOU 1806 O GLY A1010 4919 3850 4184 -525 34 -150 O ATOM 1807 N LEU A1011 8.862 86.005 114.560 1.00 33.50 N ANISOU 1807 N LEU A1011 4681 3913 4137 -526 -63 -275 N ATOM 1808 CA LEU A1011 7.474 85.601 114.768 1.00 33.49 C ANISOU 1808 CA LEU A1011 4723 3906 4096 -403 -132 -233 C ATOM 1809 C LEU A1011 6.676 86.851 115.149 1.00 37.59 C ANISOU 1809 C LEU A1011 5337 4322 4623 -394 -155 -281 C ATOM 1810 O LEU A1011 6.821 87.361 116.261 1.00 40.26 O ANISOU 1810 O LEU A1011 5619 4709 4968 -419 -178 -374 O ATOM 1811 CB LEU A1011 7.391 84.554 115.865 1.00 29.57 C ANISOU 1811 CB LEU A1011 4085 3571 3578 -331 -183 -231 C ATOM 1812 CG LEU A1011 5.967 84.193 116.254 1.00 34.11 C ANISOU 1812 CG LEU A1011 4684 4145 4132 -221 -235 -198 C ATOM 1813 CD1 LEU A1011 5.297 83.542 115.066 1.00 31.09 C ANISOU 1813 CD1 LEU A1011 4370 3689 3752 -184 -226 -129 C ATOM 1814 CD2 LEU A1011 6.012 83.285 117.458 1.00 38.41 C ANISOU 1814 CD2 LEU A1011 5098 4843 4653 -155 -257 -184 C ATOM 1815 N ARG A1012 5.843 87.350 114.237 1.00 30.97 N ANISOU 1815 N ARG A1012 4642 3349 3776 -347 -147 -222 N ATOM 1816 CA ARG A1012 5.096 88.590 114.465 1.00 31.32 C ANISOU 1816 CA ARG A1012 4793 3268 3841 -316 -148 -250 C ATOM 1817 C ARG A1012 3.623 88.247 114.626 1.00 29.58 C ANISOU 1817 C ARG A1012 4577 3076 3588 -173 -226 -210 C ATOM 1818 O ARG A1012 2.971 87.836 113.659 1.00 33.06 O ANISOU 1818 O ARG A1012 5065 3505 3992 -104 -252 -129 O ATOM 1819 CB ARG A1012 5.304 89.558 113.308 1.00 34.57 C ANISOU 1819 CB ARG A1012 5366 3500 4270 -350 -65 -192 C ATOM 1820 CG ARG A1012 6.765 89.731 112.946 1.00 43.14 C ANISOU 1820 CG ARG A1012 6433 4561 5397 -502 33 -215 C ATOM 1821 CD ARG A1012 7.437 90.591 113.975 1.00 33.38 C ANISOU 1821 CD ARG A1012 5145 3298 4240 -619 67 -354 C ATOM 1822 NE ARG A1012 6.920 91.938 113.882 1.00 43.50 N ANISOU 1822 NE ARG A1012 6584 4369 5574 -612 126 -363 N ATOM 1823 CZ ARG A1012 7.501 92.907 113.187 1.00 53.79 C ANISOU 1823 CZ ARG A1012 8006 5484 6949 -707 258 -342 C ATOM 1824 NH1 ARG A1012 8.628 92.660 112.537 1.00 56.26 N ANISOU 1824 NH1 ARG A1012 8283 5813 7281 -826 341 -319 N ATOM 1825 NH2 ARG A1012 6.960 94.119 113.152 1.00 53.37 N ANISOU 1825 NH2 ARG A1012 8108 5215 6955 -680 325 -338 N ATOM 1826 N LEU A1013 3.103 88.413 115.845 1.00 27.00 N ANISOU 1826 N LEU A1013 4190 2802 3267 -131 -262 -279 N ATOM 1827 CA LEU A1013 1.722 88.051 116.148 1.00 27.32 C ANISOU 1827 CA LEU A1013 4203 2887 3292 -3 -321 -251 C ATOM 1828 C LEU A1013 0.735 89.154 115.768 1.00 28.36 C ANISOU 1828 C LEU A1013 4453 2882 3440 87 -322 -230 C ATOM 1829 O LEU A1013 -0.477 88.904 115.747 1.00 29.35 O ANISOU 1829 O LEU A1013 4551 3043 3557 202 -373 -196 O ATOM 1830 CB LEU A1013 1.599 87.692 117.641 1.00 27.87 C ANISOU 1830 CB LEU A1013 4156 3087 3346 17 -340 -319 C ATOM 1831 CG LEU A1013 2.525 86.522 118.047 1.00 29.92 C ANISOU 1831 CG LEU A1013 4295 3494 3581 -32 -339 -308 C ATOM 1832 CD1 LEU A1013 2.295 86.050 119.499 1.00 26.84 C ANISOU 1832 CD1 LEU A1013 3796 3255 3146 21 -355 -340 C ATOM 1833 CD2 LEU A1013 2.378 85.335 117.085 1.00 22.59 C ANISOU 1833 CD2 LEU A1013 3345 2579 2659 -15 -341 -214 C ATOM 1834 N LYS A1014 1.227 90.348 115.436 1.00 29.42 N ANISOU 1834 N LYS A1014 4711 2858 3608 41 -258 -245 N ATOM 1835 CA LYS A1014 0.409 91.460 114.959 1.00 27.83 C ANISOU 1835 CA LYS A1014 4646 2497 3431 144 -236 -198 C ATOM 1836 C LYS A1014 0.718 91.745 113.494 1.00 34.20 C ANISOU 1836 C LYS A1014 5583 3200 4213 143 -197 -80 C ATOM 1837 O LYS A1014 1.875 91.650 113.068 1.00 30.92 O ANISOU 1837 O LYS A1014 5186 2760 3800 15 -135 -79 O ATOM 1838 CB LYS A1014 0.664 92.722 115.788 1.00 28.04 C ANISOU 1838 CB LYS A1014 4741 2383 3529 104 -160 -306 C ATOM 1839 CG LYS A1014 0.259 92.589 117.248 1.00 38.35 C ANISOU 1839 CG LYS A1014 5940 3798 4832 127 -193 -429 C ATOM 1840 CD LYS A1014 0.808 93.719 118.109 1.00 44.70 C ANISOU 1840 CD LYS A1014 6798 4490 5696 40 -116 -585 C ATOM 1841 CE LYS A1014 -0.102 94.916 118.114 1.00 51.39 C ANISOU 1841 CE LYS A1014 7777 5141 6607 157 -59 -589 C ATOM 1842 NZ LYS A1014 0.233 95.813 119.252 1.00 54.00 N ANISOU 1842 NZ LYS A1014 8129 5401 6986 82 6 -787 N ATOM 1843 N ILE A1015 -0.315 92.107 112.729 1.00 32.37 N ANISOU 1843 N ILE A1015 5432 2919 3947 297 -230 23 N ATOM 1844 CA ILE A1015 -0.109 92.535 111.346 1.00 30.91 C ANISOU 1844 CA ILE A1015 5396 2638 3711 329 -187 153 C ATOM 1845 C ILE A1015 0.960 93.625 111.299 1.00 32.17 C ANISOU 1845 C ILE A1015 5688 2589 3946 214 -36 146 C ATOM 1846 O ILE A1015 0.932 94.576 112.089 1.00 36.07 O ANISOU 1846 O ILE A1015 6225 2943 4536 201 28 73 O ATOM 1847 CB ILE A1015 -1.437 93.039 110.739 1.00 33.95 C ANISOU 1847 CB ILE A1015 5851 2999 4049 543 -244 263 C ATOM 1848 CG1 ILE A1015 -2.437 91.887 110.565 1.00 33.70 C ANISOU 1848 CG1 ILE A1015 5671 3189 3945 629 -393 260 C ATOM 1849 CG2 ILE A1015 -1.201 93.706 109.396 1.00 32.52 C ANISOU 1849 CG2 ILE A1015 5854 2701 3800 603 -180 418 C ATOM 1850 CD1 ILE A1015 -3.737 92.341 109.914 1.00 31.06 C ANISOU 1850 CD1 ILE A1015 5371 2877 3554 846 -471 360 C ATOM 1851 N TYR A1016 1.905 93.488 110.363 1.00 31.17 N ANISOU 1851 N TYR A1016 5623 2435 3784 123 35 211 N ATOM 1852 CA TYR A1016 2.965 94.468 110.146 1.00 36.64 C ANISOU 1852 CA TYR A1016 6437 2927 4560 -5 202 217 C ATOM 1853 C TYR A1016 3.181 94.597 108.644 1.00 35.79 C ANISOU 1853 C TYR A1016 6477 2763 4360 40 272 392 C ATOM 1854 O TYR A1016 2.581 93.872 107.853 1.00 39.64 O ANISOU 1854 O TYR A1016 6958 3394 4711 157 174 478 O ATOM 1855 CB TYR A1016 4.255 94.065 110.875 1.00 35.29 C ANISOU 1855 CB TYR A1016 6131 2818 4458 -221 241 70 C ATOM 1856 CG TYR A1016 4.945 92.862 110.278 1.00 39.15 C ANISOU 1856 CG TYR A1016 6528 3477 4870 -284 215 96 C ATOM 1857 CD1 TYR A1016 6.030 93.010 109.412 1.00 45.26 C ANISOU 1857 CD1 TYR A1016 7362 4185 5649 -395 344 150 C ATOM 1858 CD2 TYR A1016 4.520 91.570 110.581 1.00 36.03 C ANISOU 1858 CD2 TYR A1016 5987 3294 4408 -231 82 66 C ATOM 1859 CE1 TYR A1016 6.666 91.884 108.862 1.00 36.94 C ANISOU 1859 CE1 TYR A1016 6222 3285 4526 -440 332 166 C ATOM 1860 CE2 TYR A1016 5.147 90.466 110.050 1.00 38.10 C ANISOU 1860 CE2 TYR A1016 6174 3687 4616 -280 75 81 C ATOM 1861 CZ TYR A1016 6.218 90.621 109.197 1.00 43.63 C ANISOU 1861 CZ TYR A1016 6933 4330 5314 -379 196 127 C ATOM 1862 OH TYR A1016 6.823 89.492 108.678 1.00 46.56 O ANISOU 1862 OH TYR A1016 7227 4830 5632 -414 199 134 O ATOM 1863 N LYS A1017 4.027 95.536 108.238 1.00 43.74 N ANISOU 1863 N LYS A1017 7620 3562 5438 -57 450 440 N ATOM 1864 CA LYS A1017 4.339 95.730 106.824 1.00 50.45 C ANISOU 1864 CA LYS A1017 8628 4350 6192 -18 550 621 C ATOM 1865 C LYS A1017 5.732 95.190 106.535 1.00 49.40 C ANISOU 1865 C LYS A1017 8427 4270 6074 -220 644 576 C ATOM 1866 O LYS A1017 6.697 95.549 107.221 1.00 50.49 O ANISOU 1866 O LYS A1017 8501 4324 6360 -412 743 454 O ATOM 1867 CB LYS A1017 4.247 97.205 106.428 1.00 50.61 C ANISOU 1867 CB LYS A1017 8874 4074 6283 40 721 752 C ATOM 1868 CG LYS A1017 2.839 97.753 106.353 1.00 43.86 C ANISOU 1868 CG LYS A1017 8113 3170 5381 297 644 858 C ATOM 1869 CD LYS A1017 2.866 99.253 106.090 1.00 49.28 C ANISOU 1869 CD LYS A1017 9017 3536 6173 348 843 979 C ATOM 1870 CE LYS A1017 1.528 99.909 106.379 1.00 57.98 C ANISOU 1870 CE LYS A1017 10145 4597 7288 585 770 1027 C ATOM 1871 NZ LYS A1017 1.596 101.428 106.315 1.00 63.34 N ANISOU 1871 NZ LYS A1017 10923 5033 8111 602 951 1079 N ATOM 1872 N ASP A1018 5.838 94.332 105.523 1.00 44.66 N ANISOU 1872 N ASP A1018 7830 3820 5319 -177 613 660 N ATOM 1873 CA ASP A1018 7.138 93.794 105.161 1.00 47.05 C ANISOU 1873 CA ASP A1018 8069 4177 5630 -346 716 628 C ATOM 1874 C ASP A1018 7.984 94.891 104.505 1.00 48.11 C ANISOU 1874 C ASP A1018 8369 4083 5829 -439 956 733 C ATOM 1875 O ASP A1018 7.561 96.039 104.363 1.00 50.33 O ANISOU 1875 O ASP A1018 8821 4150 6153 -369 1045 833 O ATOM 1876 CB ASP A1018 6.966 92.558 104.272 1.00 47.02 C ANISOU 1876 CB ASP A1018 8033 4389 5445 -268 626 669 C ATOM 1877 CG ASP A1018 6.370 92.872 102.891 1.00 55.27 C ANISOU 1877 CG ASP A1018 9280 5419 6300 -100 649 860 C ATOM 1878 OD1 ASP A1018 6.026 91.901 102.188 1.00 56.67 O ANISOU 1878 OD1 ASP A1018 9435 5786 6313 -20 551 868 O ATOM 1879 OD2 ASP A1018 6.254 94.055 102.490 1.00 55.41 O ANISOU 1879 OD2 ASP A1018 9483 5245 6327 -42 769 1000 O ATOM 1880 N THR A1019 9.200 94.529 104.083 1.00 50.52 N ANISOU 1880 N THR A1019 8621 4424 6151 -592 1082 717 N ATOM 1881 CA THR A1019 10.104 95.518 103.498 1.00 55.49 C ANISOU 1881 CA THR A1019 9383 4836 6865 -713 1338 808 C ATOM 1882 C THR A1019 9.535 96.163 102.241 1.00 59.45 C ANISOU 1882 C THR A1019 10152 5217 7218 -539 1436 1056 C ATOM 1883 O THR A1019 9.934 97.282 101.904 1.00 62.92 O ANISOU 1883 O THR A1019 10655 5498 7755 -570 1600 1116 O ATOM 1884 CB THR A1019 11.459 94.887 103.178 1.00 60.43 C ANISOU 1884 CB THR A1019 9885 5561 7517 -888 1453 755 C ATOM 1885 OG1 THR A1019 11.274 93.788 102.279 1.00 69.67 O ANISOU 1885 OG1 THR A1019 11058 6935 8478 -772 1379 823 O ATOM 1886 CG2 THR A1019 12.137 94.381 104.448 1.00 57.38 C ANISOU 1886 CG2 THR A1019 9229 5292 7282 -1053 1372 525 C ATOM 1887 N GLU A1020 8.610 95.504 101.546 1.00 56.63 N ANISOU 1887 N GLU A1020 9847 5035 6636 -330 1282 1149 N ATOM 1888 CA GLU A1020 7.985 96.099 100.367 1.00 58.89 C ANISOU 1888 CA GLU A1020 10328 5292 6754 -125 1321 1364 C ATOM 1889 C GLU A1020 6.698 96.847 100.691 1.00 58.44 C ANISOU 1889 C GLU A1020 10338 5162 6704 71 1210 1421 C ATOM 1890 O GLU A1020 6.088 97.421 99.783 1.00 65.70 O ANISOU 1890 O GLU A1020 11373 6089 7500 263 1215 1587 O ATOM 1891 CB GLU A1020 7.709 95.019 99.315 1.00 65.73 C ANISOU 1891 CB GLU A1020 11232 6399 7344 -5 1227 1433 C ATOM 1892 CG GLU A1020 8.936 94.190 98.976 1.00 81.06 C ANISOU 1892 CG GLU A1020 13092 8433 9272 -179 1337 1365 C ATOM 1893 CD GLU A1020 8.674 93.162 97.894 1.00100.83 C ANISOU 1893 CD GLU A1020 15622 11182 11505 -61 1251 1399 C ATOM 1894 OE1 GLU A1020 7.518 93.064 97.432 1.00106.95 O ANISOU 1894 OE1 GLU A1020 16474 12070 12093 146 1089 1468 O ATOM 1895 OE2 GLU A1020 9.628 92.452 97.506 1.00107.43 O ANISOU 1895 OE2 GLU A1020 16393 12108 12317 -175 1346 1342 O ATOM 1896 N GLY A1021 6.272 96.860 101.953 1.00 58.63 N ANISOU 1896 N GLY A1021 10283 5126 6869 37 1112 1287 N ATOM 1897 CA GLY A1021 5.095 97.603 102.364 1.00 50.32 C ANISOU 1897 CA GLY A1021 9273 3996 5849 217 1025 1322 C ATOM 1898 C GLY A1021 3.819 96.800 102.478 1.00 48.85 C ANISOU 1898 C GLY A1021 9026 4018 5515 411 772 1313 C ATOM 1899 O GLY A1021 2.761 97.390 102.707 1.00 53.06 O ANISOU 1899 O GLY A1021 9603 4499 6056 593 702 1368 O ATOM 1900 N TYR A1022 3.887 95.477 102.352 1.00 42.83 N ANISOU 1900 N TYR A1022 8107 3523 4646 368 631 1211 N ATOM 1901 CA TYR A1022 2.704 94.631 102.284 1.00 51.89 C ANISOU 1901 CA TYR A1022 9149 4913 5655 528 392 1177 C ATOM 1902 C TYR A1022 2.350 94.058 103.655 1.00 43.32 C ANISOU 1902 C TYR A1022 7848 3904 4709 457 260 975 C ATOM 1903 O TYR A1022 3.233 93.689 104.434 1.00 44.04 O ANISOU 1903 O TYR A1022 7822 3984 4928 262 307 834 O ATOM 1904 CB TYR A1022 2.940 93.496 101.283 1.00 51.47 C ANISOU 1904 CB TYR A1022 9064 5088 5404 522 333 1176 C ATOM 1905 CG TYR A1022 3.164 93.977 99.859 1.00 55.78 C ANISOU 1905 CG TYR A1022 9828 5610 5758 625 448 1384 C ATOM 1906 CD1 TYR A1022 2.362 94.966 99.304 1.00 56.70 C ANISOU 1906 CD1 TYR A1022 10108 5654 5782 847 452 1577 C ATOM 1907 CD2 TYR A1022 4.179 93.445 99.074 1.00 61.59 C ANISOU 1907 CD2 TYR A1022 10596 6404 6401 514 561 1392 C ATOM 1908 CE1 TYR A1022 2.561 95.408 98.000 1.00 61.81 C ANISOU 1908 CE1 TYR A1022 10859 6343 6284 931 547 1727 C ATOM 1909 CE2 TYR A1022 4.388 93.885 97.765 1.00 62.18 C ANISOU 1909 CE2 TYR A1022 10867 6474 6283 614 678 1585 C ATOM 1910 CZ TYR A1022 3.576 94.865 97.239 1.00 64.97 C ANISOU 1910 CZ TYR A1022 11295 6806 6585 813 658 1729 C ATOM 1911 OH TYR A1022 3.778 95.307 95.944 1.00 73.52 O ANISOU 1911 OH TYR A1022 12485 7934 7514 902 756 1879 O ATOM 1912 N TYR A1023 1.048 93.976 103.938 1.00 40.07 N ANISOU 1912 N TYR A1023 7376 3585 4263 626 96 967 N ATOM 1913 CA TYR A1023 0.580 93.484 105.231 1.00 35.23 C ANISOU 1913 CA TYR A1023 6572 3045 3769 583 -15 798 C ATOM 1914 C TYR A1023 0.915 92.006 105.395 1.00 42.58 C ANISOU 1914 C TYR A1023 7325 4181 4672 462 -101 666 C ATOM 1915 O TYR A1023 0.593 91.182 104.533 1.00 42.05 O ANISOU 1915 O TYR A1023 7235 4282 4460 515 -188 683 O ATOM 1916 CB TYR A1023 -0.923 93.710 105.374 1.00 37.38 C ANISOU 1916 CB TYR A1023 6812 3383 4008 800 -155 833 C ATOM 1917 CG TYR A1023 -1.310 95.176 105.489 1.00 37.99 C ANISOU 1917 CG TYR A1023 7047 3232 4156 935 -61 947 C ATOM 1918 CD1 TYR A1023 -0.873 95.944 106.559 1.00 39.30 C ANISOU 1918 CD1 TYR A1023 7233 3189 4512 832 58 862 C ATOM 1919 CD2 TYR A1023 -2.116 95.784 104.537 1.00 39.70 C ANISOU 1919 CD2 TYR A1023 7392 3445 4247 1173 -89 1134 C ATOM 1920 CE1 TYR A1023 -1.221 97.289 106.674 1.00 46.19 C ANISOU 1920 CE1 TYR A1023 8262 3819 5470 952 166 952 C ATOM 1921 CE2 TYR A1023 -2.469 97.125 104.642 1.00 43.83 C ANISOU 1921 CE2 TYR A1023 8070 3733 4849 1318 16 1254 C ATOM 1922 CZ TYR A1023 -2.023 97.868 105.716 1.00 50.85 C ANISOU 1922 CZ TYR A1023 8987 4383 5950 1201 153 1158 C ATOM 1923 OH TYR A1023 -2.370 99.201 105.832 1.00 54.43 O ANISOU 1923 OH TYR A1023 9568 4604 6508 1322 275 1245 O ATOM 1924 N THR A1024 1.540 91.674 106.522 1.00 40.17 N ANISOU 1924 N THR A1024 6894 3865 4505 308 -74 528 N ATOM 1925 CA THR A1024 2.107 90.357 106.760 1.00 35.04 C ANISOU 1925 CA THR A1024 6092 3366 3856 188 -110 422 C ATOM 1926 C THR A1024 1.874 90.014 108.224 1.00 33.52 C ANISOU 1926 C THR A1024 5738 3217 3780 146 -167 294 C ATOM 1927 O THR A1024 1.675 90.901 109.061 1.00 32.39 O ANISOU 1927 O THR A1024 5613 2968 3726 157 -142 266 O ATOM 1928 CB THR A1024 3.612 90.355 106.433 1.00 40.65 C ANISOU 1928 CB THR A1024 6836 4016 4592 27 38 422 C ATOM 1929 OG1 THR A1024 3.826 90.920 105.132 1.00 44.39 O ANISOU 1929 OG1 THR A1024 7490 4417 4958 74 128 562 O ATOM 1930 CG2 THR A1024 4.223 88.948 106.509 1.00 38.11 C ANISOU 1930 CG2 THR A1024 6369 3849 4263 -65 14 335 C ATOM 1931 N ILE A1025 1.914 88.723 108.546 1.00 30.89 N ANISOU 1931 N ILE A1025 5256 3035 3445 101 -231 217 N ATOM 1932 CA ILE A1025 1.755 88.290 109.928 1.00 34.26 C ANISOU 1932 CA ILE A1025 5534 3521 3962 69 -271 118 C ATOM 1933 C ILE A1025 2.492 86.970 110.126 1.00 33.92 C ANISOU 1933 C ILE A1025 5367 3592 3930 -22 -264 65 C ATOM 1934 O ILE A1025 2.919 86.318 109.168 1.00 38.42 O ANISOU 1934 O ILE A1025 5957 4198 4441 -48 -241 90 O ATOM 1935 CB ILE A1025 0.260 88.172 110.326 1.00 33.91 C ANISOU 1935 CB ILE A1025 5429 3540 3915 201 -381 109 C ATOM 1936 CG1 ILE A1025 0.122 88.250 111.857 1.00 30.50 C ANISOU 1936 CG1 ILE A1025 4894 3122 3572 183 -383 25 C ATOM 1937 CG2 ILE A1025 -0.357 86.911 109.736 1.00 35.53 C ANISOU 1937 CG2 ILE A1025 5549 3887 4063 231 -464 99 C ATOM 1938 CD1 ILE A1025 -1.249 88.597 112.329 1.00 29.66 C ANISOU 1938 CD1 ILE A1025 4756 3030 3482 315 -448 22 C ATOM 1939 N GLY A1026 2.670 86.591 111.390 1.00 27.83 N ANISOU 1939 N GLY A1026 4471 2877 3228 -57 -273 -4 N ATOM 1940 CA GLY A1026 3.268 85.298 111.688 1.00 28.24 C ANISOU 1940 CA GLY A1026 4400 3034 3296 -108 -262 -33 C ATOM 1941 C GLY A1026 4.722 85.279 111.257 1.00 33.39 C ANISOU 1941 C GLY A1026 5063 3670 3954 -211 -171 -30 C ATOM 1942 O GLY A1026 5.472 86.240 111.467 1.00 32.98 O ANISOU 1942 O GLY A1026 5046 3551 3935 -282 -114 -47 O ATOM 1943 N ILE A1027 5.120 84.185 110.619 1.00 31.53 N ANISOU 1943 N ILE A1027 4795 3488 3698 -225 -146 -18 N ATOM 1944 CA ILE A1027 6.477 84.039 110.105 1.00 28.36 C ANISOU 1944 CA ILE A1027 4389 3084 3302 -309 -47 -11 C ATOM 1945 C ILE A1027 6.380 84.316 108.610 1.00 30.05 C ANISOU 1945 C ILE A1027 4750 3238 3429 -300 -9 41 C ATOM 1946 O ILE A1027 6.227 83.404 107.796 1.00 38.37 O ANISOU 1946 O ILE A1027 5817 4335 4426 -274 -8 41 O ATOM 1947 CB ILE A1027 7.064 82.657 110.411 1.00 33.23 C ANISOU 1947 CB ILE A1027 4877 3795 3955 -312 -22 -28 C ATOM 1948 CG1 ILE A1027 7.185 82.466 111.918 1.00 35.14 C ANISOU 1948 CG1 ILE A1027 4982 4115 4253 -298 -59 -56 C ATOM 1949 CG2 ILE A1027 8.434 82.525 109.791 1.00 32.82 C ANISOU 1949 CG2 ILE A1027 4812 3747 3911 -384 87 -21 C ATOM 1950 CD1 ILE A1027 7.813 81.146 112.306 1.00 43.23 C ANISOU 1950 CD1 ILE A1027 5882 5227 5315 -273 -22 -43 C ATOM 1951 N GLY A1028 6.445 85.598 108.253 1.00 36.08 N ANISOU 1951 N GLY A1028 5635 3899 4175 -316 30 83 N ATOM 1952 CA GLY A1028 6.468 86.028 106.866 1.00 37.61 C ANISOU 1952 CA GLY A1028 5986 4036 4269 -296 87 161 C ATOM 1953 C GLY A1028 5.265 85.628 106.042 1.00 41.26 C ANISOU 1953 C GLY A1028 6515 4552 4610 -179 -10 189 C ATOM 1954 O GLY A1028 5.403 85.417 104.834 1.00 41.99 O ANISOU 1954 O GLY A1028 6701 4669 4586 -160 27 228 O ATOM 1955 N HIS A1029 4.082 85.518 106.647 1.00 36.39 N ANISOU 1955 N HIS A1029 5844 3972 4010 -100 -132 161 N ATOM 1956 CA HIS A1029 2.885 85.132 105.901 1.00 32.35 C ANISOU 1956 CA HIS A1029 5359 3539 3393 4 -240 165 C ATOM 1957 C HIS A1029 2.229 86.377 105.308 1.00 43.69 C ANISOU 1957 C HIS A1029 6939 4916 4743 111 -266 265 C ATOM 1958 O HIS A1029 1.597 87.158 106.024 1.00 39.34 O ANISOU 1958 O HIS A1029 6385 4308 4254 170 -305 283 O ATOM 1959 CB HIS A1029 1.892 84.378 106.781 1.00 26.25 C ANISOU 1959 CB HIS A1029 4441 2842 2691 36 -345 88 C ATOM 1960 CG HIS A1029 0.677 83.933 106.031 1.00 34.62 C ANISOU 1960 CG HIS A1029 5493 4001 3661 119 -461 63 C ATOM 1961 ND1 HIS A1029 0.609 82.719 105.376 1.00 35.88 N ANISOU 1961 ND1 HIS A1029 5607 4247 3777 85 -479 -15 N ATOM 1962 CD2 HIS A1029 -0.499 84.557 105.792 1.00 39.16 C ANISOU 1962 CD2 HIS A1029 6090 4611 4178 237 -565 96 C ATOM 1963 CE1 HIS A1029 -0.569 82.605 104.789 1.00 36.34 C ANISOU 1963 CE1 HIS A1029 5650 4404 3755 161 -599 -48 C ATOM 1964 NE2 HIS A1029 -1.257 83.709 105.018 1.00 39.64 N ANISOU 1964 NE2 HIS A1029 6101 4803 4158 263 -659 28 N ATOM 1965 N LEU A1030 2.368 86.552 103.998 1.00 44.48 N ANISOU 1965 N LEU A1030 7172 5034 4695 153 -237 337 N ATOM 1966 CA LEU A1030 1.758 87.685 103.315 1.00 40.87 C ANISOU 1966 CA LEU A1030 6867 4530 4132 286 -254 465 C ATOM 1967 C LEU A1030 0.241 87.556 103.320 1.00 34.59 C ANISOU 1967 C LEU A1030 6009 3850 3284 429 -429 447 C ATOM 1968 O LEU A1030 -0.303 86.520 102.935 1.00 39.94 O ANISOU 1968 O LEU A1030 6596 4686 3894 438 -532 359 O ATOM 1969 CB LEU A1030 2.271 87.768 101.880 1.00 41.95 C ANISOU 1969 CB LEU A1030 7157 4692 4088 310 -180 554 C ATOM 1970 CG LEU A1030 1.460 88.678 100.957 1.00 46.84 C ANISOU 1970 CG LEU A1030 7933 5324 4541 494 -225 703 C ATOM 1971 CD1 LEU A1030 1.692 90.116 101.315 1.00 50.98 C ANISOU 1971 CD1 LEU A1030 8583 5631 5156 523 -108 834 C ATOM 1972 CD2 LEU A1030 1.817 88.423 99.500 1.00 55.33 C ANISOU 1972 CD2 LEU A1030 9137 6499 5389 531 -183 766 C ATOM 1973 N LEU A1031 -0.445 88.611 103.750 1.00 36.15 N ANISOU 1973 N LEU A1031 6245 3965 3524 539 -455 520 N ATOM 1974 CA LEU A1031 -1.903 88.572 103.800 1.00 43.19 C ANISOU 1974 CA LEU A1031 7056 4975 4380 688 -616 507 C ATOM 1975 C LEU A1031 -2.552 89.106 102.526 1.00 46.33 C ANISOU 1975 C LEU A1031 7573 5454 4575 871 -685 633 C ATOM 1976 O LEU A1031 -3.537 88.530 102.050 1.00 43.38 O ANISOU 1976 O LEU A1031 7105 5278 4098 959 -843 583 O ATOM 1977 CB LEU A1031 -2.407 89.367 105.009 1.00 40.35 C ANISOU 1977 CB LEU A1031 6655 4503 4176 735 -612 509 C ATOM 1978 CG LEU A1031 -2.187 88.651 106.347 1.00 38.46 C ANISOU 1978 CG LEU A1031 6251 4265 4096 600 -601 370 C ATOM 1979 CD1 LEU A1031 -2.491 89.606 107.520 1.00 35.61 C ANISOU 1979 CD1 LEU A1031 5886 3779 3867 640 -565 368 C ATOM 1980 CD2 LEU A1031 -3.057 87.395 106.403 1.00 32.20 C ANISOU 1980 CD2 LEU A1031 5280 3658 3295 601 -727 266 C ATOM 1981 N THR A1032 -2.027 90.202 101.981 1.00 46.48 N ANISOU 1981 N THR A1032 7794 5330 4538 933 -566 797 N ATOM 1982 CA THR A1032 -2.553 90.851 100.785 1.00 50.44 C ANISOU 1982 CA THR A1032 8441 5894 4830 1136 -606 962 C ATOM 1983 C THR A1032 -1.570 91.935 100.367 1.00 55.64 C ANISOU 1983 C THR A1032 9331 6329 5480 1131 -398 1136 C ATOM 1984 O THR A1032 -0.796 92.433 101.188 1.00 56.32 O ANISOU 1984 O THR A1032 9442 6199 5757 1000 -251 1120 O ATOM 1985 CB THR A1032 -3.954 91.448 101.015 1.00 47.12 C ANISOU 1985 CB THR A1032 7968 5526 4408 1354 -742 1017 C ATOM 1986 OG1 THR A1032 -4.432 92.061 99.810 1.00 47.56 O ANISOU 1986 OG1 THR A1032 8165 5667 4239 1579 -788 1198 O ATOM 1987 CG2 THR A1032 -3.940 92.482 102.115 1.00 49.45 C ANISOU 1987 CG2 THR A1032 8299 5577 4913 1366 -637 1057 C ATOM 1988 N LYS A1033 -1.587 92.277 99.082 1.00 60.92 N ANISOU 1988 N LYS A1033 10164 7058 5923 1268 -380 1297 N ATOM 1989 CA LYS A1033 -0.831 93.427 98.606 1.00 62.61 C ANISOU 1989 CA LYS A1033 10614 7048 6126 1298 -165 1500 C ATOM 1990 C LYS A1033 -1.673 94.695 98.565 1.00 62.34 C ANISOU 1990 C LYS A1033 10610 6927 6149 1489 -155 1635 C ATOM 1991 O LYS A1033 -1.155 95.757 98.206 1.00 62.37 O ANISOU 1991 O LYS A1033 10752 6742 6206 1497 35 1775 O ATOM 1992 CB LYS A1033 -0.240 93.146 97.223 1.00 65.37 C ANISOU 1992 CB LYS A1033 11048 7524 6266 1289 -98 1565 C ATOM 1993 CG LYS A1033 0.925 92.171 97.237 1.00 64.84 C ANISOU 1993 CG LYS A1033 10970 7467 6197 1069 -12 1448 C ATOM 1994 CD LYS A1033 1.549 92.064 95.855 1.00 72.79 C ANISOU 1994 CD LYS A1033 12093 8569 6993 1080 90 1534 C ATOM 1995 CE LYS A1033 2.655 91.018 95.796 1.00 76.56 C ANISOU 1995 CE LYS A1033 12542 9084 7465 877 178 1404 C ATOM 1996 NZ LYS A1033 3.192 90.871 94.405 1.00 83.69 N ANISOU 1996 NZ LYS A1033 13552 10101 8144 904 276 1476 N ATOM 1997 N SER A1034 -2.947 94.604 98.934 1.00 60.20 N ANISOU 1997 N SER A1034 10205 6789 5880 1638 -344 1591 N ATOM 1998 CA SER A1034 -3.807 95.776 98.992 1.00 60.41 C ANISOU 1998 CA SER A1034 10246 6735 5974 1827 -334 1710 C ATOM 1999 C SER A1034 -3.334 96.734 100.085 1.00 54.31 C ANISOU 1999 C SER A1034 9550 5626 5459 1748 -155 1716 C ATOM 2000 O SER A1034 -2.902 96.296 101.156 1.00 55.24 O ANISOU 2000 O SER A1034 9623 5649 5716 1592 -143 1577 O ATOM 2001 CB SER A1034 -5.248 95.355 99.266 1.00 65.33 C ANISOU 2001 CB SER A1034 10670 7586 6566 1978 -570 1632 C ATOM 2002 OG SER A1034 -6.017 96.450 99.732 1.00 71.47 O ANISOU 2002 OG SER A1034 11445 8238 7472 2134 -541 1712 O ATOM 2003 N PRO A1035 -3.408 98.045 99.849 1.00 55.48 N ANISOU 2003 N PRO A1035 9813 5590 5676 1848 -13 1862 N ATOM 2004 CA PRO A1035 -3.044 99.011 100.898 1.00 57.15 C ANISOU 2004 CA PRO A1035 10087 5485 6144 1767 155 1834 C ATOM 2005 C PRO A1035 -4.064 99.125 102.028 1.00 64.05 C ANISOU 2005 C PRO A1035 10838 6350 7147 1859 48 1737 C ATOM 2006 O PRO A1035 -3.846 99.921 102.952 1.00 70.35 O ANISOU 2006 O PRO A1035 11678 6897 8153 1797 179 1687 O ATOM 2007 CB PRO A1035 -2.926 100.333 100.122 1.00 61.41 C ANISOU 2007 CB PRO A1035 10785 5856 6692 1869 330 2029 C ATOM 2008 CG PRO A1035 -3.828 100.156 98.934 1.00 61.91 C ANISOU 2008 CG PRO A1035 10825 6186 6512 2099 182 2160 C ATOM 2009 CD PRO A1035 -3.729 98.695 98.566 1.00 54.32 C ANISOU 2009 CD PRO A1035 9757 5511 5371 2025 13 2054 C ATOM 2010 N SER A1036 -5.156 98.361 101.994 1.00 58.11 N ANISOU 2010 N SER A1036 9924 5869 6286 1994 -178 1691 N ATOM 2011 CA SER A1036 -6.214 98.463 102.992 1.00 54.10 C ANISOU 2011 CA SER A1036 9279 5382 5895 2100 -276 1607 C ATOM 2012 C SER A1036 -5.909 97.535 104.162 1.00 51.19 C ANISOU 2012 C SER A1036 8811 5016 5622 1935 -332 1409 C ATOM 2013 O SER A1036 -5.821 96.313 103.989 1.00 48.81 O ANISOU 2013 O SER A1036 8416 4918 5210 1864 -468 1328 O ATOM 2014 CB SER A1036 -7.576 98.123 102.385 1.00 56.68 C ANISOU 2014 CB SER A1036 9448 6012 6076 2315 -486 1644 C ATOM 2015 OG SER A1036 -8.597 98.138 103.376 1.00 61.59 O ANISOU 2015 OG SER A1036 9911 6672 6819 2406 -574 1551 O ATOM 2016 N LEU A1037 -5.742 98.119 105.349 1.00 44.99 N ANISOU 2016 N LEU A1037 8048 4005 5040 1874 -224 1323 N ATOM 2017 CA LEU A1037 -5.574 97.310 106.546 1.00 41.54 C ANISOU 2017 CA LEU A1037 7457 3619 4708 1704 -276 1108 C ATOM 2018 C LEU A1037 -6.809 96.455 106.803 1.00 43.45 C ANISOU 2018 C LEU A1037 7463 4143 4903 1810 -483 1029 C ATOM 2019 O LEU A1037 -6.692 95.306 107.240 1.00 46.19 O ANISOU 2019 O LEU A1037 7633 4664 5254 1649 -566 876 O ATOM 2020 CB LEU A1037 -5.281 98.210 107.751 1.00 45.79 C ANISOU 2020 CB LEU A1037 8050 3892 5456 1632 -123 1013 C ATOM 2021 CG LEU A1037 -5.272 97.559 109.143 1.00 42.39 C ANISOU 2021 CG LEU A1037 7424 3549 5133 1473 -168 779 C ATOM 2022 CD1 LEU A1037 -4.269 96.416 109.206 1.00 38.33 C ANISOU 2022 CD1 LEU A1037 6810 3172 4581 1222 -197 669 C ATOM 2023 CD2 LEU A1037 -4.998 98.610 110.230 1.00 47.49 C ANISOU 2023 CD2 LEU A1037 8153 3932 5960 1423 -12 681 C ATOM 2024 N ASN A1038 -8.002 96.998 106.538 1.00 46.08 N ANISOU 2024 N ASN A1038 7783 4523 5202 2084 -557 1137 N ATOM 2025 CA ASN A1038 -9.219 96.211 106.710 1.00 47.30 C ANISOU 2025 CA ASN A1038 7690 4961 5321 2183 -751 1060 C ATOM 2026 C ASN A1038 -9.245 95.007 105.776 1.00 48.86 C ANISOU 2026 C ASN A1038 7779 5441 5343 2120 -908 1032 C ATOM 2027 O ASN A1038 -9.737 93.936 106.153 1.00 51.84 O ANISOU 2027 O ASN A1038 7933 6027 5739 2035 -1027 882 O ATOM 2028 CB ASN A1038 -10.447 97.088 106.496 1.00 47.04 C ANISOU 2028 CB ASN A1038 7605 4968 5302 2432 -777 1160 C ATOM 2029 CG ASN A1038 -10.789 97.891 107.726 1.00 56.09 C ANISOU 2029 CG ASN A1038 8750 5920 6642 2483 -667 1102 C ATOM 2030 OD1 ASN A1038 -10.291 97.610 108.822 1.00 62.99 O ANISOU 2030 OD1 ASN A1038 9626 6682 7624 2353 -613 963 O ATOM 2031 ND2 ASN A1038 -11.640 98.883 107.565 1.00 59.39 N ANISOU 2031 ND2 ASN A1038 9165 6301 7100 2675 -632 1199 N ATOM 2032 N ALA A1039 -8.722 95.157 104.554 1.00 46.71 N ANISOU 2032 N ALA A1039 7664 5177 4908 2149 -892 1166 N ATOM 2033 CA ALA A1039 -8.644 94.013 103.651 1.00 50.79 C ANISOU 2033 CA ALA A1039 8103 5951 5246 2081 -1028 1117 C ATOM 2034 C ALA A1039 -7.686 92.959 104.184 1.00 50.94 C ANISOU 2034 C ALA A1039 8048 5963 5342 1776 -978 940 C ATOM 2035 O ALA A1039 -7.943 91.758 104.048 1.00 53.56 O ANISOU 2035 O ALA A1039 8210 6509 5629 1683 -1098 807 O ATOM 2036 CB ALA A1039 -8.223 94.459 102.253 1.00 51.26 C ANISOU 2036 CB ALA A1039 8319 6027 5129 2131 -973 1273 C ATOM 2037 N ALA A1040 -6.575 93.384 104.798 1.00 43.15 N ANISOU 2037 N ALA A1040 7182 4733 4480 1621 -799 931 N ATOM 2038 CA ALA A1040 -5.660 92.414 105.386 1.00 43.15 C ANISOU 2038 CA ALA A1040 7098 4740 4557 1359 -754 774 C ATOM 2039 C ALA A1040 -6.310 91.711 106.565 1.00 36.41 C ANISOU 2039 C ALA A1040 6021 3980 3831 1303 -826 615 C ATOM 2040 O ALA A1040 -6.131 90.503 106.752 1.00 34.48 O ANISOU 2040 O ALA A1040 5641 3864 3597 1159 -871 493 O ATOM 2041 CB ALA A1040 -4.362 93.096 105.813 1.00 42.20 C ANISOU 2041 CB ALA A1040 7128 4365 4541 1213 -558 791 C ATOM 2042 N LYS A1041 -7.085 92.451 107.356 1.00 35.97 N ANISOU 2042 N LYS A1041 5934 3857 3878 1426 -821 622 N ATOM 2043 CA LYS A1041 -7.756 91.861 108.505 1.00 39.41 C ANISOU 2043 CA LYS A1041 6165 4381 4429 1389 -867 486 C ATOM 2044 C LYS A1041 -8.802 90.834 108.080 1.00 35.29 C ANISOU 2044 C LYS A1041 5442 4121 3846 1436 -1033 430 C ATOM 2045 O LYS A1041 -8.988 89.817 108.753 1.00 37.79 O ANISOU 2045 O LYS A1041 5587 4535 4236 1315 -1056 304 O ATOM 2046 CB LYS A1041 -8.388 92.972 109.349 1.00 35.27 C ANISOU 2046 CB LYS A1041 5664 3725 4013 1533 -812 508 C ATOM 2047 CG LYS A1041 -7.391 93.665 110.286 1.00 38.06 C ANISOU 2047 CG LYS A1041 6138 3844 4479 1410 -647 460 C ATOM 2048 CD LYS A1041 -8.010 94.887 110.953 1.00 43.05 C ANISOU 2048 CD LYS A1041 6830 4317 5210 1568 -575 479 C ATOM 2049 CE LYS A1041 -7.022 95.514 111.926 1.00 41.35 C ANISOU 2049 CE LYS A1041 6717 3888 5105 1419 -420 385 C ATOM 2050 NZ LYS A1041 -7.687 96.544 112.769 1.00 45.29 N ANISOU 2050 NZ LYS A1041 7250 4247 5711 1555 -346 352 N ATOM 2051 N SER A1042 -9.513 91.090 106.980 1.00 46.93 N ANISOU 2051 N SER A1042 6929 5715 5188 1611 -1145 521 N ATOM 2052 CA SER A1042 -10.552 90.156 106.561 1.00 47.29 C ANISOU 2052 CA SER A1042 6760 6028 5179 1645 -1314 439 C ATOM 2053 C SER A1042 -9.943 88.877 106.000 1.00 47.49 C ANISOU 2053 C SER A1042 6747 6161 5137 1449 -1345 336 C ATOM 2054 O SER A1042 -10.482 87.786 106.215 1.00 45.17 O ANISOU 2054 O SER A1042 6253 6016 4894 1356 -1416 195 O ATOM 2055 CB SER A1042 -11.478 90.815 105.545 1.00 50.94 C ANISOU 2055 CB SER A1042 7232 6623 5498 1904 -1442 559 C ATOM 2056 OG SER A1042 -10.764 91.099 104.367 1.00 63.97 O ANISOU 2056 OG SER A1042 9083 8255 6968 1936 -1432 675 O ATOM 2057 N GLU A1043 -8.825 88.989 105.274 1.00 44.02 N ANISOU 2057 N GLU A1043 6498 5635 4593 1384 -1274 400 N ATOM 2058 CA GLU A1043 -8.075 87.801 104.879 1.00 40.92 C ANISOU 2058 CA GLU A1043 6085 5302 4160 1191 -1263 296 C ATOM 2059 C GLU A1043 -7.609 87.028 106.102 1.00 47.35 C ANISOU 2059 C GLU A1043 6798 6038 5156 1003 -1173 181 C ATOM 2060 O GLU A1043 -7.763 85.805 106.172 1.00 38.44 O ANISOU 2060 O GLU A1043 5528 5011 4066 883 -1207 52 O ATOM 2061 CB GLU A1043 -6.872 88.187 104.018 1.00 35.71 C ANISOU 2061 CB GLU A1043 5651 4540 3375 1159 -1168 398 C ATOM 2062 CG GLU A1043 -7.247 88.657 102.627 1.00 49.48 C ANISOU 2062 CG GLU A1043 7502 6407 4892 1334 -1257 511 C ATOM 2063 CD GLU A1043 -7.739 87.512 101.747 1.00 60.72 C ANISOU 2063 CD GLU A1043 8802 8092 6176 1303 -1407 380 C ATOM 2064 OE1 GLU A1043 -7.155 86.406 101.819 1.00 64.77 O ANISOU 2064 OE1 GLU A1043 9260 8617 6733 1109 -1368 241 O ATOM 2065 OE2 GLU A1043 -8.711 87.720 100.991 1.00 65.00 O ANISOU 2065 OE2 GLU A1043 9298 8831 6567 1478 -1562 410 O ATOM 2066 N LEU A1044 -7.028 87.734 107.078 1.00 40.04 N ANISOU 2066 N LEU A1044 5946 4929 4340 977 -1051 223 N ATOM 2067 CA LEU A1044 -6.538 87.079 108.285 1.00 32.17 C ANISOU 2067 CA LEU A1044 4861 3878 3485 825 -968 132 C ATOM 2068 C LEU A1044 -7.660 86.327 108.989 1.00 36.17 C ANISOU 2068 C LEU A1044 5152 4506 4085 830 -1032 38 C ATOM 2069 O LEU A1044 -7.498 85.162 109.373 1.00 37.15 O ANISOU 2069 O LEU A1044 5166 4673 4274 698 -1008 -51 O ATOM 2070 CB LEU A1044 -5.909 88.118 109.222 1.00 30.61 C ANISOU 2070 CB LEU A1044 4765 3497 3368 821 -852 175 C ATOM 2071 CG LEU A1044 -5.293 87.536 110.503 1.00 32.31 C ANISOU 2071 CG LEU A1044 4900 3682 3695 681 -772 90 C ATOM 2072 CD1 LEU A1044 -4.253 86.459 110.191 1.00 30.03 C ANISOU 2072 CD1 LEU A1044 4602 3421 3388 527 -733 53 C ATOM 2073 CD2 LEU A1044 -4.691 88.665 111.368 1.00 28.84 C ANISOU 2073 CD2 LEU A1044 4559 3082 3315 675 -672 103 C ATOM 2074 N ASP A1045 -8.812 86.983 109.164 1.00 31.62 N ANISOU 2074 N ASP A1045 4509 3978 3527 986 -1099 63 N ATOM 2075 CA ASP A1045 -9.951 86.333 109.806 1.00 40.12 C ANISOU 2075 CA ASP A1045 5364 5178 4702 994 -1147 -24 C ATOM 2076 C ASP A1045 -10.395 85.095 109.031 1.00 42.77 C ANISOU 2076 C ASP A1045 5561 5680 5009 912 -1241 -123 C ATOM 2077 O ASP A1045 -10.792 84.091 109.633 1.00 32.88 O ANISOU 2077 O ASP A1045 4144 4479 3871 808 -1217 -220 O ATOM 2078 CB ASP A1045 -11.118 87.313 109.941 1.00 41.19 C ANISOU 2078 CB ASP A1045 5446 5354 4851 1200 -1207 26 C ATOM 2079 CG ASP A1045 -10.843 88.438 110.941 1.00 45.17 C ANISOU 2079 CG ASP A1045 6059 5681 5423 1268 -1094 82 C ATOM 2080 OD1 ASP A1045 -9.837 88.382 111.680 1.00 42.95 O ANISOU 2080 OD1 ASP A1045 5858 5277 5184 1141 -982 60 O ATOM 2081 OD2 ASP A1045 -11.656 89.381 110.993 1.00 49.61 O ANISOU 2081 OD2 ASP A1045 6618 6236 5996 1456 -1119 137 O ATOM 2082 N LYS A1046 -10.353 85.156 107.695 1.00 39.01 N ANISOU 2082 N LYS A1046 5153 5289 4380 958 -1337 -105 N ATOM 2083 CA LYS A1046 -10.693 83.992 106.882 1.00 44.54 C ANISOU 2083 CA LYS A1046 5736 6149 5037 865 -1427 -232 C ATOM 2084 C LYS A1046 -9.729 82.838 107.134 1.00 44.06 C ANISOU 2084 C LYS A1046 5691 6004 5046 657 -1315 -312 C ATOM 2085 O LYS A1046 -10.152 81.681 107.254 1.00 43.14 O ANISOU 2085 O LYS A1046 5419 5952 5021 539 -1319 -443 O ATOM 2086 CB LYS A1046 -10.682 84.362 105.401 1.00 46.25 C ANISOU 2086 CB LYS A1046 6056 6481 5035 965 -1543 -191 C ATOM 2087 CG LYS A1046 -11.047 83.198 104.468 1.00 61.38 C ANISOU 2087 CG LYS A1046 7855 8586 6879 869 -1649 -356 C ATOM 2088 CD LYS A1046 -10.913 83.572 102.987 1.00 68.43 C ANISOU 2088 CD LYS A1046 8876 9612 7513 975 -1758 -312 C ATOM 2089 CE LYS A1046 -11.393 82.440 102.086 1.00 76.66 C ANISOU 2089 CE LYS A1046 9783 10870 8473 880 -1881 -514 C ATOM 2090 NZ LYS A1046 -10.994 82.631 100.661 1.00 83.83 N ANISOU 2090 NZ LYS A1046 10846 11902 9101 953 -1956 -486 N ATOM 2091 N ALA A1047 -8.427 83.135 107.215 1.00 39.52 N ANISOU 2091 N ALA A1047 5296 5279 4440 612 -1205 -234 N ATOM 2092 CA ALA A1047 -7.427 82.083 107.362 1.00 38.88 C ANISOU 2092 CA ALA A1047 5235 5126 4413 444 -1100 -292 C ATOM 2093 C ALA A1047 -7.422 81.490 108.764 1.00 38.75 C ANISOU 2093 C ALA A1047 5109 5040 4576 365 -999 -317 C ATOM 2094 O ALA A1047 -6.961 80.364 108.947 1.00 37.94 O ANISOU 2094 O ALA A1047 4966 4904 4546 242 -921 -378 O ATOM 2095 CB ALA A1047 -6.036 82.620 107.033 1.00 40.43 C ANISOU 2095 CB ALA A1047 5631 5205 4527 426 -1013 -200 C ATOM 2096 N ILE A1048 -7.901 82.227 109.765 1.00 38.76 N ANISOU 2096 N ILE A1048 5071 5014 4642 445 -985 -265 N ATOM 2097 CA ILE A1048 -7.822 81.753 111.144 1.00 35.30 C ANISOU 2097 CA ILE A1048 4550 4522 4338 389 -878 -270 C ATOM 2098 C ILE A1048 -9.165 81.150 111.536 1.00 41.27 C ANISOU 2098 C ILE A1048 5106 5374 5203 390 -906 -341 C ATOM 2099 O ILE A1048 -9.225 80.204 112.329 1.00 41.47 O ANISOU 2099 O ILE A1048 5035 5377 5346 304 -811 -371 O ATOM 2100 CB ILE A1048 -7.423 82.888 112.112 1.00 35.95 C ANISOU 2100 CB ILE A1048 4717 4520 4422 460 -823 -190 C ATOM 2101 CG1 ILE A1048 -6.098 83.532 111.683 1.00 33.20 C ANISOU 2101 CG1 ILE A1048 4551 4074 3988 438 -787 -133 C ATOM 2102 CG2 ILE A1048 -7.278 82.348 113.524 1.00 32.36 C ANISOU 2102 CG2 ILE A1048 4184 4044 4068 411 -718 -195 C ATOM 2103 CD1 ILE A1048 -4.920 82.551 111.611 1.00 30.44 C ANISOU 2103 CD1 ILE A1048 4224 3694 3648 308 -710 -150 C ATOM 2104 N GLY A1049 -10.250 81.693 110.978 1.00 36.43 N ANISOU 2104 N GLY A1049 4421 4869 4552 493 -1027 -362 N ATOM 2105 CA GLY A1049 -11.584 81.265 111.334 1.00 33.88 C ANISOU 2105 CA GLY A1049 3881 4653 4338 500 -1057 -435 C ATOM 2106 C GLY A1049 -12.147 81.930 112.563 1.00 42.36 C ANISOU 2106 C GLY A1049 4896 5709 5489 595 -998 -382 C ATOM 2107 O GLY A1049 -13.049 81.373 113.196 1.00 43.86 O ANISOU 2107 O GLY A1049 4903 5957 5803 567 -958 -433 O ATOM 2108 N ARG A1050 -11.640 83.104 112.934 1.00 32.40 N ANISOU 2108 N ARG A1050 3785 4362 4165 700 -976 -290 N ATOM 2109 CA ARG A1050 -12.248 83.893 113.993 1.00 35.45 C ANISOU 2109 CA ARG A1050 4128 4736 4604 813 -928 -258 C ATOM 2110 C ARG A1050 -11.973 85.367 113.712 1.00 35.35 C ANISOU 2110 C ARG A1050 4285 4646 4502 959 -962 -181 C ATOM 2111 O ARG A1050 -11.269 85.719 112.763 1.00 37.79 O ANISOU 2111 O ARG A1050 4741 4907 4709 961 -1008 -139 O ATOM 2112 CB ARG A1050 -11.727 83.490 115.378 1.00 35.90 C ANISOU 2112 CB ARG A1050 4189 4725 4727 738 -778 -250 C ATOM 2113 CG ARG A1050 -10.256 83.789 115.600 1.00 32.55 C ANISOU 2113 CG ARG A1050 3955 4183 4231 686 -721 -206 C ATOM 2114 CD ARG A1050 -9.745 83.237 116.953 1.00 30.48 C ANISOU 2114 CD ARG A1050 3673 3900 4008 621 -591 -198 C ATOM 2115 NE ARG A1050 -8.327 83.528 117.103 1.00 30.73 N ANISOU 2115 NE ARG A1050 3856 3852 3967 572 -558 -171 N ATOM 2116 CZ ARG A1050 -7.861 84.724 117.458 1.00 33.33 C ANISOU 2116 CZ ARG A1050 4303 4119 4244 626 -551 -167 C ATOM 2117 NH1 ARG A1050 -8.705 85.704 117.724 1.00 32.78 N ANISOU 2117 NH1 ARG A1050 4230 4040 4186 745 -564 -178 N ATOM 2118 NH2 ARG A1050 -6.560 84.940 117.551 1.00 33.34 N ANISOU 2118 NH2 ARG A1050 4414 4060 4193 558 -522 -161 N ATOM 2119 N ASN A1051 -12.545 86.222 114.553 1.00 38.70 N ANISOU 2119 N ASN A1051 4689 5045 4969 1082 -920 -163 N ATOM 2120 CA ASN A1051 -12.343 87.672 114.492 1.00 39.34 C ANISOU 2120 CA ASN A1051 4935 5011 5001 1225 -914 -96 C ATOM 2121 C ASN A1051 -11.063 87.987 115.256 1.00 33.29 C ANISOU 2121 C ASN A1051 4331 4096 4223 1131 -800 -96 C ATOM 2122 O ASN A1051 -11.056 88.011 116.486 1.00 42.38 O ANISOU 2122 O ASN A1051 5450 5232 5422 1115 -710 -137 O ATOM 2123 CB ASN A1051 -13.551 88.396 115.085 1.00 46.09 C ANISOU 2123 CB ASN A1051 5688 5903 5922 1402 -906 -96 C ATOM 2124 CG ASN A1051 -13.469 89.926 114.957 1.00 62.45 C ANISOU 2124 CG ASN A1051 7933 7830 7964 1573 -886 -26 C ATOM 2125 OD1 ASN A1051 -12.511 90.485 114.406 1.00 63.33 O ANISOU 2125 OD1 ASN A1051 8246 7808 8009 1551 -874 29 O ATOM 2126 ND2 ASN A1051 -14.497 90.604 115.460 1.00 65.90 N ANISOU 2126 ND2 ASN A1051 8290 8284 8463 1748 -867 -25 N ATOM 2127 N THR A1052 -9.963 88.216 114.531 1.00 40.68 N ANISOU 2127 N THR A1052 5431 4939 5086 1066 -804 -58 N ATOM 2128 CA THR A1052 -8.666 88.433 115.173 1.00 38.37 C ANISOU 2128 CA THR A1052 5262 4531 4786 954 -708 -75 C ATOM 2129 C THR A1052 -8.344 89.901 115.441 1.00 36.52 C ANISOU 2129 C THR A1052 5188 4132 4554 1028 -647 -60 C ATOM 2130 O THR A1052 -7.468 90.176 116.266 1.00 33.20 O ANISOU 2130 O THR A1052 4832 3638 4145 941 -566 -114 O ATOM 2131 CB THR A1052 -7.526 87.858 114.318 1.00 38.41 C ANISOU 2131 CB THR A1052 5345 4517 4731 822 -717 -54 C ATOM 2132 OG1 THR A1052 -7.338 88.686 113.166 1.00 38.55 O ANISOU 2132 OG1 THR A1052 5507 4458 4682 888 -750 20 O ATOM 2133 CG2 THR A1052 -7.826 86.400 113.858 1.00 32.88 C ANISOU 2133 CG2 THR A1052 4507 3952 4035 746 -769 -81 C ATOM 2134 N ASN A1053 -9.011 90.837 114.760 1.00 36.61 N ANISOU 2134 N ASN A1053 5265 4086 4558 1189 -681 7 N ATOM 2135 CA ASN A1053 -8.601 92.244 114.701 1.00 36.66 C ANISOU 2135 CA ASN A1053 5463 3888 4577 1256 -606 43 C ATOM 2136 C ASN A1053 -7.090 92.370 114.513 1.00 40.31 C ANISOU 2136 C ASN A1053 6068 4233 5016 1086 -537 35 C ATOM 2137 O ASN A1053 -6.448 93.198 115.163 1.00 39.54 O ANISOU 2137 O ASN A1053 6073 3984 4965 1037 -438 -20 O ATOM 2138 CB ASN A1053 -9.032 93.015 115.957 1.00 36.95 C ANISOU 2138 CB ASN A1053 5496 3850 4692 1328 -522 -33 C ATOM 2139 CG ASN A1053 -8.983 94.547 115.752 1.00 48.97 C ANISOU 2139 CG ASN A1053 7211 5142 6255 1447 -440 10 C ATOM 2140 OD1 ASN A1053 -9.438 95.066 114.730 1.00 45.45 O ANISOU 2140 OD1 ASN A1053 6834 4647 5786 1597 -476 135 O ATOM 2141 ND2 ASN A1053 -8.400 95.256 116.711 1.00 57.22 N ANISOU 2141 ND2 ASN A1053 8345 6043 7355 1380 -326 -95 N ATOM 2142 N GLY A1054 -6.507 91.511 113.675 1.00 38.51 N ANISOU 2142 N GLY A1054 5829 4080 4722 985 -584 70 N ATOM 2143 CA GLY A1054 -5.113 91.618 113.310 1.00 33.08 C ANISOU 2143 CA GLY A1054 5262 3295 4013 839 -518 78 C ATOM 2144 C GLY A1054 -4.111 91.051 114.291 1.00 30.85 C ANISOU 2144 C GLY A1054 4918 3043 3759 665 -467 -26 C ATOM 2145 O GLY A1054 -2.909 91.310 114.137 1.00 29.17 O ANISOU 2145 O GLY A1054 4790 2745 3548 543 -401 -37 O ATOM 2146 N VAL A1055 -4.548 90.283 115.291 1.00 32.08 N ANISOU 2146 N VAL A1055 4924 3329 3936 657 -491 -95 N ATOM 2147 CA VAL A1055 -3.650 89.692 116.276 1.00 26.50 C ANISOU 2147 CA VAL A1055 4152 2685 3234 526 -452 -174 C ATOM 2148 C VAL A1055 -3.943 88.194 116.379 1.00 25.44 C ANISOU 2148 C VAL A1055 3866 2712 3087 500 -495 -162 C ATOM 2149 O VAL A1055 -5.095 87.803 116.599 1.00 27.28 O ANISOU 2149 O VAL A1055 4000 3022 3342 584 -528 -158 O ATOM 2150 CB VAL A1055 -3.799 90.368 117.656 1.00 27.44 C ANISOU 2150 CB VAL A1055 4260 2785 3381 548 -402 -271 C ATOM 2151 CG1 VAL A1055 -2.751 89.827 118.608 1.00 33.60 C ANISOU 2151 CG1 VAL A1055 4977 3656 4134 423 -375 -347 C ATOM 2152 CG2 VAL A1055 -3.627 91.853 117.541 1.00 36.82 C ANISOU 2152 CG2 VAL A1055 5602 3779 4608 574 -341 -297 C ATOM 2153 N ILE A1056 -2.908 87.358 116.250 1.00 27.42 N ANISOU 2153 N ILE A1056 4094 3006 3319 385 -479 -161 N ATOM 2154 CA ILE A1056 -3.067 85.905 116.348 1.00 23.63 C ANISOU 2154 CA ILE A1056 3490 2643 2847 355 -491 -146 C ATOM 2155 C ILE A1056 -2.186 85.363 117.470 1.00 22.47 C ANISOU 2155 C ILE A1056 3281 2564 2693 291 -439 -173 C ATOM 2156 O ILE A1056 -1.292 86.042 117.981 1.00 24.12 O ANISOU 2156 O ILE A1056 3534 2750 2879 246 -413 -217 O ATOM 2157 CB ILE A1056 -2.737 85.175 115.032 1.00 23.40 C ANISOU 2157 CB ILE A1056 3481 2614 2797 305 -515 -108 C ATOM 2158 CG1 ILE A1056 -1.279 85.437 114.608 1.00 25.93 C ANISOU 2158 CG1 ILE A1056 3890 2874 3087 212 -470 -101 C ATOM 2159 CG2 ILE A1056 -3.719 85.579 113.948 1.00 23.57 C ANISOU 2159 CG2 ILE A1056 3542 2621 2794 389 -587 -80 C ATOM 2160 CD1 ILE A1056 -0.887 84.671 113.316 1.00 24.52 C ANISOU 2160 CD1 ILE A1056 3738 2703 2876 166 -476 -70 C ATOM 2161 N THR A1057 -2.455 84.113 117.846 1.00 24.51 N ANISOU 2161 N THR A1057 3430 2909 2972 291 -422 -147 N ATOM 2162 CA THR A1057 -1.620 83.439 118.821 1.00 24.20 C ANISOU 2162 CA THR A1057 3331 2952 2913 259 -372 -138 C ATOM 2163 C THR A1057 -0.424 82.786 118.134 1.00 25.15 C ANISOU 2163 C THR A1057 3463 3063 3030 181 -356 -110 C ATOM 2164 O THR A1057 -0.394 82.600 116.913 1.00 24.38 O ANISOU 2164 O THR A1057 3411 2903 2948 148 -372 -97 O ATOM 2165 CB THR A1057 -2.420 82.370 119.562 1.00 27.84 C ANISOU 2165 CB THR A1057 3683 3489 3407 306 -329 -96 C ATOM 2166 OG1 THR A1057 -2.744 81.325 118.641 1.00 23.76 O ANISOU 2166 OG1 THR A1057 3133 2941 2955 273 -322 -63 O ATOM 2167 CG2 THR A1057 -3.717 82.978 120.106 1.00 23.26 C ANISOU 2167 CG2 THR A1057 3076 2921 2839 387 -334 -124 C ATOM 2168 N LYS A1058 0.568 82.425 118.946 1.00 22.18 N ANISOU 2168 N LYS A1058 3038 2767 2622 163 -323 -101 N ATOM 2169 CA LYS A1058 1.708 81.689 118.426 1.00 23.05 C ANISOU 2169 CA LYS A1058 3133 2886 2741 111 -294 -67 C ATOM 2170 C LYS A1058 1.281 80.335 117.834 1.00 25.21 C ANISOU 2170 C LYS A1058 3372 3130 3076 121 -254 -9 C ATOM 2171 O LYS A1058 1.777 79.945 116.773 1.00 25.35 O ANISOU 2171 O LYS A1058 3424 3095 3114 73 -240 -6 O ATOM 2172 CB LYS A1058 2.751 81.511 119.526 1.00 27.14 C ANISOU 2172 CB LYS A1058 3575 3529 3207 119 -277 -62 C ATOM 2173 CG LYS A1058 3.787 80.435 119.209 1.00 41.45 C ANISOU 2173 CG LYS A1058 5335 5375 5041 109 -231 1 C ATOM 2174 CD LYS A1058 4.927 80.459 120.206 1.00 47.82 C ANISOU 2174 CD LYS A1058 6055 6335 5781 126 -238 -2 C ATOM 2175 CE LYS A1058 5.916 79.342 119.924 1.00 52.71 C ANISOU 2175 CE LYS A1058 6608 6992 6428 148 -185 78 C ATOM 2176 NZ LYS A1058 5.305 78.028 120.221 1.00 44.62 N ANISOU 2176 NZ LYS A1058 5557 5953 5443 241 -115 191 N ATOM 2177 N ASP A1059 0.366 79.605 118.496 1.00 23.73 N ANISOU 2177 N ASP A1059 3120 2971 2926 174 -221 28 N ATOM 2178 CA ASP A1059 -0.156 78.363 117.901 1.00 29.27 C ANISOU 2178 CA ASP A1059 3790 3616 3714 160 -170 56 C ATOM 2179 C ASP A1059 -0.789 78.619 116.529 1.00 28.82 C ANISOU 2179 C ASP A1059 3785 3489 3677 114 -229 -8 C ATOM 2180 O ASP A1059 -0.576 77.853 115.580 1.00 27.03 O ANISOU 2180 O ASP A1059 3572 3213 3484 67 -206 -24 O ATOM 2181 CB ASP A1059 -1.187 77.691 118.830 1.00 25.08 C ANISOU 2181 CB ASP A1059 3180 3110 3237 210 -109 100 C ATOM 2182 CG ASP A1059 -0.559 77.085 120.081 1.00 29.32 C ANISOU 2182 CG ASP A1059 3670 3725 3745 275 -27 196 C ATOM 2183 OD1 ASP A1059 0.665 76.885 120.113 1.00 28.81 O ANISOU 2183 OD1 ASP A1059 3611 3692 3642 281 -17 230 O ATOM 2184 OD2 ASP A1059 -1.300 76.809 121.043 1.00 32.12 O ANISOU 2184 OD2 ASP A1059 3975 4121 4109 331 30 246 O ATOM 2185 N GLU A1060 -1.570 79.696 116.400 1.00 27.79 N ANISOU 2185 N GLU A1060 3686 3360 3514 140 -305 -47 N ATOM 2186 CA GLU A1060 -2.139 80.037 115.096 1.00 32.14 C ANISOU 2186 CA GLU A1060 4287 3874 4051 126 -377 -91 C ATOM 2187 C GLU A1060 -1.044 80.345 114.074 1.00 30.99 C ANISOU 2187 C GLU A1060 4243 3687 3844 79 -382 -92 C ATOM 2188 O GLU A1060 -1.116 79.896 112.923 1.00 27.95 O ANISOU 2188 O GLU A1060 3889 3286 3446 47 -398 -119 O ATOM 2189 CB GLU A1060 -3.124 81.210 115.237 1.00 25.27 C ANISOU 2189 CB GLU A1060 3432 3014 3157 196 -447 -109 C ATOM 2190 CG GLU A1060 -4.470 80.744 115.852 1.00 26.22 C ANISOU 2190 CG GLU A1060 3430 3183 3350 237 -442 -122 C ATOM 2191 CD GLU A1060 -5.320 81.855 116.441 1.00 35.83 C ANISOU 2191 CD GLU A1060 4640 4420 4555 329 -477 -130 C ATOM 2192 OE1 GLU A1060 -6.444 81.546 116.887 1.00 31.57 O ANISOU 2192 OE1 GLU A1060 3990 3928 4077 365 -467 -142 O ATOM 2193 OE2 GLU A1060 -4.883 83.032 116.463 1.00 27.89 O ANISOU 2193 OE2 GLU A1060 3735 3372 3491 362 -500 -129 O ATOM 2194 N ALA A1061 -0.016 81.099 114.475 1.00 24.76 N ANISOU 2194 N ALA A1061 3502 2889 3017 66 -363 -75 N ATOM 2195 CA ALA A1061 1.080 81.389 113.555 1.00 22.62 C ANISOU 2195 CA ALA A1061 3314 2577 2702 11 -342 -71 C ATOM 2196 C ALA A1061 1.827 80.111 113.172 1.00 26.04 C ANISOU 2196 C ALA A1061 3710 3018 3164 -31 -276 -63 C ATOM 2197 O ALA A1061 2.318 79.985 112.043 1.00 26.70 O ANISOU 2197 O ALA A1061 3859 3072 3215 -68 -257 -72 O ATOM 2198 CB ALA A1061 2.046 82.406 114.170 1.00 21.33 C ANISOU 2198 CB ALA A1061 3179 2405 2519 -17 -322 -74 C ATOM 2199 N GLU A1062 1.943 79.161 114.099 1.00 23.78 N ANISOU 2199 N GLU A1062 3329 2770 2937 -13 -226 -38 N ATOM 2200 CA GLU A1062 2.668 77.929 113.766 1.00 28.72 C ANISOU 2200 CA GLU A1062 3925 3381 3607 -32 -144 -21 C ATOM 2201 C GLU A1062 1.893 77.082 112.755 1.00 29.46 C ANISOU 2201 C GLU A1062 4036 3421 3735 -58 -138 -72 C ATOM 2202 O GLU A1062 2.488 76.532 111.824 1.00 31.51 O ANISOU 2202 O GLU A1062 4335 3647 3992 -93 -91 -99 O ATOM 2203 CB GLU A1062 2.979 77.113 115.028 1.00 26.04 C ANISOU 2203 CB GLU A1062 3488 3087 3318 19 -79 44 C ATOM 2204 CG GLU A1062 3.847 75.848 114.736 1.00 27.67 C ANISOU 2204 CG GLU A1062 3667 3262 3585 25 26 80 C ATOM 2205 CD GLU A1062 4.352 75.164 115.998 1.00 35.44 C ANISOU 2205 CD GLU A1062 4563 4307 4597 108 91 179 C ATOM 2206 OE1 GLU A1062 4.067 75.657 117.108 1.00 33.66 O ANISOU 2206 OE1 GLU A1062 4298 4166 4327 153 52 210 O ATOM 2207 OE2 GLU A1062 5.028 74.118 115.884 1.00 36.21 O ANISOU 2207 OE2 GLU A1062 4633 4371 4752 142 188 229 O ATOM 2208 N LYS A1063 0.562 76.989 112.899 1.00 31.87 N ANISOU 2208 N LYS A1063 4305 3730 4073 -45 -184 -103 N ATOM 2209 CA LYS A1063 -0.243 76.282 111.898 1.00 34.58 C ANISOU 2209 CA LYS A1063 4647 4047 4445 -87 -200 -187 C ATOM 2210 C LYS A1063 -0.166 76.964 110.535 1.00 29.98 C ANISOU 2210 C LYS A1063 4165 3481 3745 -103 -275 -235 C ATOM 2211 O LYS A1063 -0.061 76.300 109.497 1.00 28.90 O ANISOU 2211 O LYS A1063 4060 3330 3589 -146 -258 -306 O ATOM 2212 CB LYS A1063 -1.706 76.199 112.343 1.00 37.51 C ANISOU 2212 CB LYS A1063 4932 4443 4876 -74 -244 -218 C ATOM 2213 CG LYS A1063 -1.939 75.298 113.538 1.00 47.63 C ANISOU 2213 CG LYS A1063 6120 5698 6278 -64 -140 -168 C ATOM 2214 CD LYS A1063 -3.423 74.996 113.730 1.00 48.55 C ANISOU 2214 CD LYS A1063 6138 5830 6481 -81 -158 -221 C ATOM 2215 CE LYS A1063 -4.210 76.259 114.034 1.00 56.63 C ANISOU 2215 CE LYS A1063 7146 6933 7438 -18 -266 -217 C ATOM 2216 NZ LYS A1063 -5.650 75.927 114.184 1.00 64.43 N ANISOU 2216 NZ LYS A1063 8010 7952 8519 -33 -278 -274 N ATOM 2217 N LEU A1064 -0.280 78.291 110.515 1.00 21.85 N ANISOU 2217 N LEU A1064 3192 2478 2631 -61 -351 -200 N ATOM 2218 CA LEU A1064 -0.094 79.046 109.285 1.00 30.63 C ANISOU 2218 CA LEU A1064 4420 3598 3620 -55 -400 -205 C ATOM 2219 C LEU A1064 1.262 78.745 108.658 1.00 28.43 C ANISOU 2219 C LEU A1064 4209 3287 3307 -104 -309 -196 C ATOM 2220 O LEU A1064 1.365 78.528 107.452 1.00 29.92 O ANISOU 2220 O LEU A1064 4469 3489 3412 -121 -311 -237 O ATOM 2221 CB LEU A1064 -0.207 80.536 109.604 1.00 27.90 C ANISOU 2221 CB LEU A1064 4134 3242 3224 2 -449 -142 C ATOM 2222 CG LEU A1064 -0.991 81.515 108.754 1.00 40.95 C ANISOU 2222 CG LEU A1064 5868 4915 4774 73 -542 -126 C ATOM 2223 CD1 LEU A1064 -2.379 80.965 108.490 1.00 49.23 C ANISOU 2223 CD1 LEU A1064 6825 6048 5831 108 -638 -193 C ATOM 2224 CD2 LEU A1064 -1.048 82.841 109.528 1.00 35.54 C ANISOU 2224 CD2 LEU A1064 5223 4177 4104 128 -547 -65 C ATOM 2225 N PHE A1065 2.324 78.779 109.470 1.00 25.37 N ANISOU 2225 N PHE A1065 3793 2874 2971 -120 -231 -145 N ATOM 2226 CA PHE A1065 3.670 78.515 108.969 1.00 25.90 C ANISOU 2226 CA PHE A1065 3894 2922 3023 -161 -136 -132 C ATOM 2227 C PHE A1065 3.792 77.112 108.394 1.00 27.94 C ANISOU 2227 C PHE A1065 4132 3164 3319 -182 -69 -191 C ATOM 2228 O PHE A1065 4.427 76.916 107.349 1.00 31.61 O ANISOU 2228 O PHE A1065 4666 3621 3723 -208 -14 -218 O ATOM 2229 CB PHE A1065 4.698 78.712 110.086 1.00 24.06 C ANISOU 2229 CB PHE A1065 3591 2700 2850 -166 -82 -80 C ATOM 2230 CG PHE A1065 6.097 78.296 109.695 1.00 28.56 C ANISOU 2230 CG PHE A1065 4151 3270 3429 -199 23 -69 C ATOM 2231 CD1 PHE A1065 6.891 79.145 108.925 1.00 27.78 C ANISOU 2231 CD1 PHE A1065 4131 3158 3268 -245 60 -57 C ATOM 2232 CD2 PHE A1065 6.597 77.053 110.066 1.00 29.81 C ANISOU 2232 CD2 PHE A1065 4224 3434 3667 -176 100 -61 C ATOM 2233 CE1 PHE A1065 8.177 78.768 108.550 1.00 31.01 C ANISOU 2233 CE1 PHE A1065 4513 3577 3693 -276 168 -51 C ATOM 2234 CE2 PHE A1065 7.877 76.659 109.697 1.00 29.86 C ANISOU 2234 CE2 PHE A1065 4207 3448 3690 -188 202 -49 C ATOM 2235 CZ PHE A1065 8.675 77.522 108.946 1.00 27.36 C ANISOU 2235 CZ PHE A1065 3950 3136 3311 -242 234 -50 C ATOM 2236 N ASN A1066 3.202 76.111 109.062 1.00 24.72 N ANISOU 2236 N ASN A1066 3635 2740 3018 -174 -52 -213 N ATOM 2237 CA ASN A1066 3.317 74.747 108.545 1.00 26.81 C ANISOU 2237 CA ASN A1066 3888 2954 3347 -201 36 -281 C ATOM 2238 C ASN A1066 2.638 74.614 107.186 1.00 27.85 C ANISOU 2238 C ASN A1066 4089 3102 3391 -240 -18 -399 C ATOM 2239 O ASN A1066 3.125 73.887 106.312 1.00 31.17 O ANISOU 2239 O ASN A1066 4555 3493 3795 -270 58 -472 O ATOM 2240 CB ASN A1066 2.738 73.732 109.541 1.00 31.06 C ANISOU 2240 CB ASN A1066 4325 3444 4032 -189 86 -271 C ATOM 2241 CG ASN A1066 3.672 73.483 110.725 1.00 36.56 C ANISOU 2241 CG ASN A1066 4959 4137 4797 -131 171 -153 C ATOM 2242 OD1 ASN A1066 4.878 73.687 110.627 1.00 38.27 O ANISOU 2242 OD1 ASN A1066 5185 4375 4979 -114 215 -110 O ATOM 2243 ND2 ASN A1066 3.111 73.040 111.848 1.00 34.86 N ANISOU 2243 ND2 ASN A1066 4666 3910 4668 -94 195 -97 N ATOM 2244 N GLN A1067 1.505 75.296 106.992 1.00 30.88 N ANISOU 2244 N GLN A1067 4478 3547 3709 -229 -149 -426 N ATOM 2245 CA GLN A1067 0.867 75.312 105.671 1.00 35.22 C ANISOU 2245 CA GLN A1067 5087 4160 4134 -246 -229 -534 C ATOM 2246 C GLN A1067 1.739 76.025 104.649 1.00 31.62 C ANISOU 2246 C GLN A1067 4766 3733 3514 -229 -213 -497 C ATOM 2247 O GLN A1067 1.822 75.597 103.492 1.00 34.18 O ANISOU 2247 O GLN A1067 5157 4094 3736 -251 -202 -589 O ATOM 2248 CB GLN A1067 -0.496 76.012 105.726 1.00 39.61 C ANISOU 2248 CB GLN A1067 5603 4799 4646 -207 -382 -546 C ATOM 2249 CG GLN A1067 -1.508 75.385 106.656 1.00 52.89 C ANISOU 2249 CG GLN A1067 7142 6467 6485 -229 -394 -588 C ATOM 2250 CD GLN A1067 -2.748 76.248 106.814 1.00 67.74 C ANISOU 2250 CD GLN A1067 8970 8440 8327 -170 -537 -580 C ATOM 2251 OE1 GLN A1067 -3.016 77.126 105.990 1.00 72.37 O ANISOU 2251 OE1 GLN A1067 9627 9110 8760 -110 -642 -569 O ATOM 2252 NE2 GLN A1067 -3.503 76.013 107.883 1.00 71.79 N ANISOU 2252 NE2 GLN A1067 9361 8939 8977 -171 -528 -571 N ATOM 2253 N ASP A1068 2.350 77.148 105.042 1.00 30.12 N ANISOU 2253 N ASP A1068 4621 3530 3293 -194 -205 -370 N ATOM 2254 CA ASP A1068 3.257 77.850 104.137 1.00 31.98 C ANISOU 2254 CA ASP A1068 4983 3772 3396 -190 -154 -317 C ATOM 2255 C ASP A1068 4.428 76.958 103.732 1.00 28.13 C ANISOU 2255 C ASP A1068 4505 3249 2935 -235 -9 -354 C ATOM 2256 O ASP A1068 4.850 76.961 102.570 1.00 34.54 O ANISOU 2256 O ASP A1068 5419 4091 3616 -240 38 -381 O ATOM 2257 CB ASP A1068 3.742 79.160 104.782 1.00 25.25 C ANISOU 2257 CB ASP A1068 4159 2881 2554 -171 -146 -192 C ATOM 2258 CG ASP A1068 2.638 80.234 104.816 1.00 35.29 C ANISOU 2258 CG ASP A1068 5469 4176 3762 -102 -271 -149 C ATOM 2259 OD1 ASP A1068 1.618 80.038 104.118 1.00 32.52 O ANISOU 2259 OD1 ASP A1068 5131 3901 3324 -60 -370 -203 O ATOM 2260 OD2 ASP A1068 2.768 81.250 105.553 1.00 36.94 O ANISOU 2260 OD2 ASP A1068 5687 4334 4014 -85 -271 -72 O ATOM 2261 N VAL A1069 4.951 76.164 104.664 1.00 31.65 N ANISOU 2261 N VAL A1069 4846 3639 3540 -252 72 -350 N ATOM 2262 CA VAL A1069 6.037 75.251 104.308 1.00 28.78 C ANISOU 2262 CA VAL A1069 4480 3239 3218 -272 218 -381 C ATOM 2263 C VAL A1069 5.548 74.199 103.311 1.00 32.15 C ANISOU 2263 C VAL A1069 4948 3662 3607 -295 237 -529 C ATOM 2264 O VAL A1069 6.188 73.962 102.275 1.00 31.45 O ANISOU 2264 O VAL A1069 4941 3585 3425 -306 320 -580 O ATOM 2265 CB VAL A1069 6.638 74.616 105.573 1.00 31.29 C ANISOU 2265 CB VAL A1069 4671 3509 3709 -253 294 -325 C ATOM 2266 CG1 VAL A1069 7.458 73.345 105.233 1.00 30.63 C ANISOU 2266 CG1 VAL A1069 4568 3368 3701 -247 447 -372 C ATOM 2267 CG2 VAL A1069 7.493 75.643 106.308 1.00 27.97 C ANISOU 2267 CG2 VAL A1069 4212 3120 3295 -246 296 -214 C ATOM 2268 N ASP A1070 4.402 73.560 103.598 1.00 31.35 N ANISOU 2268 N ASP A1070 4787 3548 3576 -312 167 -615 N ATOM 2269 CA ASP A1070 3.824 72.609 102.643 1.00 30.89 C ANISOU 2269 CA ASP A1070 4758 3494 3486 -358 170 -795 C ATOM 2270 C ASP A1070 3.642 73.237 101.268 1.00 39.98 C ANISOU 2270 C ASP A1070 6031 4765 4397 -352 94 -852 C ATOM 2271 O ASP A1070 3.894 72.591 100.247 1.00 34.83 O ANISOU 2271 O ASP A1070 5445 4128 3662 -379 155 -981 O ATOM 2272 CB ASP A1070 2.464 72.102 103.127 1.00 34.45 C ANISOU 2272 CB ASP A1070 5113 3937 4040 -395 83 -882 C ATOM 2273 CG ASP A1070 2.566 71.232 104.350 1.00 44.90 C ANISOU 2273 CG ASP A1070 6333 5132 5595 -400 189 -836 C ATOM 2274 OD1 ASP A1070 3.675 70.739 104.631 1.00 45.28 O ANISOU 2274 OD1 ASP A1070 6387 5098 5721 -373 334 -774 O ATOM 2275 OD2 ASP A1070 1.534 71.053 105.033 1.00 46.57 O ANISOU 2275 OD2 ASP A1070 6455 5334 5906 -420 134 -852 O ATOM 2276 N ALA A1071 3.158 74.484 101.218 1.00 33.83 N ANISOU 2276 N ALA A1071 5287 4072 3495 -304 -35 -758 N ATOM 2277 CA ALA A1071 2.977 75.143 99.924 1.00 35.06 C ANISOU 2277 CA ALA A1071 5570 4350 3401 -268 -104 -775 C ATOM 2278 C ALA A1071 4.318 75.403 99.250 1.00 31.47 C ANISOU 2278 C ALA A1071 5231 3877 2849 -261 43 -708 C ATOM 2279 O ALA A1071 4.465 75.188 98.044 1.00 37.74 O ANISOU 2279 O ALA A1071 6127 4748 3464 -257 69 -790 O ATOM 2280 CB ALA A1071 2.206 76.461 100.097 1.00 35.92 C ANISOU 2280 CB ALA A1071 5698 4528 3421 -194 -251 -656 C ATOM 2281 N ALA A1072 5.306 75.875 100.007 1.00 33.19 N ANISOU 2281 N ALA A1072 5426 4009 3175 -261 142 -569 N ATOM 2282 CA ALA A1072 6.626 76.106 99.423 1.00 31.90 C ANISOU 2282 CA ALA A1072 5342 3830 2949 -267 300 -509 C ATOM 2283 C ALA A1072 7.209 74.816 98.862 1.00 31.14 C ANISOU 2283 C ALA A1072 5245 3712 2875 -296 431 -644 C ATOM 2284 O ALA A1072 7.795 74.810 97.770 1.00 34.75 O ANISOU 2284 O ALA A1072 5810 4214 3179 -290 526 -671 O ATOM 2285 CB ALA A1072 7.570 76.695 100.469 1.00 30.35 C ANISOU 2285 CB ALA A1072 5072 3557 2900 -281 376 -372 C ATOM 2286 N VAL A1073 7.037 73.707 99.589 1.00 29.15 N ANISOU 2286 N VAL A1073 4881 3382 2813 -319 455 -727 N ATOM 2287 CA VAL A1073 7.507 72.407 99.107 1.00 35.31 C ANISOU 2287 CA VAL A1073 5665 4108 3645 -339 594 -866 C ATOM 2288 C VAL A1073 6.779 72.005 97.829 1.00 36.36 C ANISOU 2288 C VAL A1073 5897 4325 3593 -362 541 -1053 C ATOM 2289 O VAL A1073 7.396 71.532 96.865 1.00 40.63 O ANISOU 2289 O VAL A1073 6522 4881 4035 -365 662 -1147 O ATOM 2290 CB VAL A1073 7.344 71.338 100.203 1.00 34.59 C ANISOU 2290 CB VAL A1073 5444 3892 3806 -349 636 -895 C ATOM 2291 CG1 VAL A1073 7.552 69.943 99.618 1.00 39.38 C ANISOU 2291 CG1 VAL A1073 6072 4415 4476 -372 776 -1069 C ATOM 2292 CG2 VAL A1073 8.310 71.595 101.330 1.00 34.85 C ANISOU 2292 CG2 VAL A1073 5381 3877 3985 -308 709 -724 C ATOM 2293 N ARG A1074 5.450 72.162 97.800 1.00 39.34 N ANISOU 2293 N ARG A1074 6256 4775 3916 -377 360 -1123 N ATOM 2294 CA ARG A1074 4.722 71.816 96.576 1.00 45.34 C ANISOU 2294 CA ARG A1074 7090 5658 4477 -399 282 -1320 C ATOM 2295 C ARG A1074 5.213 72.644 95.397 1.00 43.11 C ANISOU 2295 C ARG A1074 6966 5510 3905 -341 295 -1262 C ATOM 2296 O ARG A1074 5.358 72.128 94.283 1.00 44.28 O ANISOU 2296 O ARG A1074 7205 5733 3885 -350 345 -1416 O ATOM 2297 CB ARG A1074 3.218 72.013 96.760 1.00 50.69 C ANISOU 2297 CB ARG A1074 7694 6429 5135 -412 66 -1387 C ATOM 2298 CG ARG A1074 2.528 70.929 97.563 1.00 58.52 C ANISOU 2298 CG ARG A1074 8545 7310 6380 -494 68 -1518 C ATOM 2299 CD ARG A1074 1.009 71.026 97.426 1.00 58.75 C ANISOU 2299 CD ARG A1074 8493 7472 6357 -522 -141 -1640 C ATOM 2300 NE ARG A1074 0.507 72.371 97.694 1.00 63.44 N ANISOU 2300 NE ARG A1074 9083 8176 6845 -431 -297 -1460 N ATOM 2301 CZ ARG A1074 0.224 72.837 98.906 1.00 56.50 C ANISOU 2301 CZ ARG A1074 8112 7227 6130 -408 -326 -1312 C ATOM 2302 NH1 ARG A1074 0.404 72.069 99.970 1.00 57.13 N ANISOU 2302 NH1 ARG A1074 8096 7142 6468 -462 -215 -1306 N ATOM 2303 NH2 ARG A1074 -0.236 74.070 99.054 1.00 55.91 N ANISOU 2303 NH2 ARG A1074 8048 7243 5953 -319 -455 -1167 N ATOM 2304 N GLY A1075 5.471 73.935 95.625 1.00 41.92 N ANISOU 2304 N GLY A1075 6856 5383 3689 -281 265 -1041 N ATOM 2305 CA GLY A1075 6.009 74.776 94.567 1.00 44.42 C ANISOU 2305 CA GLY A1075 7333 5798 3748 -224 315 -946 C ATOM 2306 C GLY A1075 7.401 74.354 94.134 1.00 48.35 C ANISOU 2306 C GLY A1075 7884 6235 4252 -243 550 -949 C ATOM 2307 O GLY A1075 7.705 74.318 92.937 1.00 46.46 O ANISOU 2307 O GLY A1075 7776 6096 3780 -217 619 -1002 O ATOM 2308 N ILE A1076 8.262 74.024 95.103 1.00 40.54 N ANISOU 2308 N ILE A1076 6786 5100 3518 -276 676 -890 N ATOM 2309 CA ILE A1076 9.600 73.528 94.787 1.00 38.58 C ANISOU 2309 CA ILE A1076 6550 4796 3312 -284 904 -898 C ATOM 2310 C ILE A1076 9.523 72.295 93.894 1.00 43.80 C ANISOU 2310 C ILE A1076 7264 5479 3900 -298 974 -1132 C ATOM 2311 O ILE A1076 10.302 72.148 92.945 1.00 47.94 O ANISOU 2311 O ILE A1076 7885 6045 4285 -281 1129 -1170 O ATOM 2312 CB ILE A1076 10.382 73.224 96.078 1.00 32.50 C ANISOU 2312 CB ILE A1076 5619 3891 2837 -300 993 -815 C ATOM 2313 CG1 ILE A1076 10.878 74.509 96.741 1.00 37.59 C ANISOU 2313 CG1 ILE A1076 6229 4528 3526 -301 984 -605 C ATOM 2314 CG2 ILE A1076 11.567 72.278 95.768 1.00 35.73 C ANISOU 2314 CG2 ILE A1076 6007 4243 3326 -292 1219 -881 C ATOM 2315 CD1 ILE A1076 11.372 74.284 98.183 1.00 41.16 C ANISOU 2315 CD1 ILE A1076 6501 4891 4245 -310 1003 -536 C ATOM 2316 N LEU A1077 8.585 71.392 94.178 1.00 43.43 N ANISOU 2316 N LEU A1077 7153 5398 3950 -336 877 -1304 N ATOM 2317 CA LEU A1077 8.506 70.155 93.413 1.00 49.36 C ANISOU 2317 CA LEU A1077 7946 6138 4671 -369 957 -1559 C ATOM 2318 C LEU A1077 7.851 70.342 92.051 1.00 56.76 C ANISOU 2318 C LEU A1077 9021 7273 5272 -363 858 -1706 C ATOM 2319 O LEU A1077 8.007 69.475 91.184 1.00 61.94 O ANISOU 2319 O LEU A1077 9747 7950 5836 -385 952 -1924 O ATOM 2320 CB LEU A1077 7.758 69.081 94.207 1.00 49.97 C ANISOU 2320 CB LEU A1077 7904 6085 4999 -430 916 -1700 C ATOM 2321 CG LEU A1077 8.405 68.648 95.526 1.00 49.77 C ANISOU 2321 CG LEU A1077 7747 5868 5293 -414 1033 -1571 C ATOM 2322 CD1 LEU A1077 7.477 67.742 96.316 1.00 45.74 C ANISOU 2322 CD1 LEU A1077 7135 5236 5008 -470 983 -1677 C ATOM 2323 CD2 LEU A1077 9.748 67.971 95.281 1.00 50.49 C ANISOU 2323 CD2 LEU A1077 7857 5865 5463 -374 1283 -1581 C ATOM 2324 N ARG A1078 7.118 71.430 91.846 1.00 54.64 N ANISOU 2324 N ARG A1078 8795 7154 4812 -323 672 -1597 N ATOM 2325 CA ARG A1078 6.589 71.771 90.533 1.00 56.96 C ANISOU 2325 CA ARG A1078 9226 7674 4743 -280 572 -1686 C ATOM 2326 C ARG A1078 7.576 72.583 89.701 1.00 56.42 C ANISOU 2326 C ARG A1078 9316 7679 4442 -204 715 -1520 C ATOM 2327 O ARG A1078 7.280 72.904 88.547 1.00 55.54 O ANISOU 2327 O ARG A1078 9344 7768 3992 -145 662 -1562 O ATOM 2328 CB ARG A1078 5.265 72.539 90.686 1.00 54.28 C ANISOU 2328 CB ARG A1078 8850 7471 4303 -244 302 -1635 C ATOM 2329 CG ARG A1078 4.072 71.641 91.004 1.00 54.14 C ANISOU 2329 CG ARG A1078 8697 7465 4407 -327 146 -1878 C ATOM 2330 CD ARG A1078 2.893 72.419 91.578 1.00 63.58 C ANISOU 2330 CD ARG A1078 9799 8742 5616 -291 -89 -1779 C ATOM 2331 NE ARG A1078 1.856 71.526 92.096 1.00 74.39 N ANISOU 2331 NE ARG A1078 11004 10084 7176 -391 -199 -1993 N ATOM 2332 CZ ARG A1078 0.814 71.919 92.826 1.00 78.45 C ANISOU 2332 CZ ARG A1078 11388 10627 7791 -385 -372 -1943 C ATOM 2333 NH1 ARG A1078 0.656 73.201 93.137 1.00 73.25 N ANISOU 2333 NH1 ARG A1078 10752 10019 7059 -274 -462 -1691 N ATOM 2334 NH2 ARG A1078 -0.073 71.025 93.248 1.00 82.22 N ANISOU 2334 NH2 ARG A1078 11713 11072 8454 -494 -438 -2151 N ATOM 2335 N ASN A1079 8.735 72.923 90.263 1.00 53.80 N ANISOU 2335 N ASN A1079 8960 7204 4279 -204 898 -1334 N ATOM 2336 CA ASN A1079 9.741 73.743 89.596 1.00 49.34 C ANISOU 2336 CA ASN A1079 8522 6680 3544 -152 1065 -1158 C ATOM 2337 C ASN A1079 10.837 72.814 89.092 1.00 46.81 C ANISOU 2337 C ASN A1079 8223 6311 3249 -172 1314 -1283 C ATOM 2338 O ASN A1079 11.558 72.210 89.893 1.00 43.48 O ANISOU 2338 O ASN A1079 7674 5728 3118 -209 1440 -1287 O ATOM 2339 CB ASN A1079 10.306 74.794 90.551 1.00 48.25 C ANISOU 2339 CB ASN A1079 8318 6424 3589 -156 1107 -888 C ATOM 2340 CG ASN A1079 11.153 75.836 89.838 1.00 50.71 C ANISOU 2340 CG ASN A1079 8768 6777 3723 -115 1266 -689 C ATOM 2341 OD1 ASN A1079 12.198 75.520 89.274 1.00 52.34 O ANISOU 2341 OD1 ASN A1079 9016 6978 3892 -123 1488 -707 O ATOM 2342 ND2 ASN A1079 10.705 77.085 89.864 1.00 49.20 N ANISOU 2342 ND2 ASN A1079 8648 6613 3431 -69 1171 -494 N ATOM 2343 N ALA A1080 10.962 72.702 87.766 1.00 46.85 N ANISOU 2343 N ALA A1080 8390 6470 2943 -130 1386 -1379 N ATOM 2344 CA ALA A1080 11.899 71.754 87.176 1.00 48.42 C ANISOU 2344 CA ALA A1080 8570 6639 3189 -130 1593 -1511 C ATOM 2345 C ALA A1080 13.352 72.093 87.484 1.00 52.01 C ANISOU 2345 C ALA A1080 8998 6981 3784 -129 1856 -1330 C ATOM 2346 O ALA A1080 14.215 71.224 87.351 1.00 50.24 O ANISOU 2346 O ALA A1080 8716 6684 3691 -129 2040 -1426 O ATOM 2347 CB ALA A1080 11.704 71.680 85.659 1.00 51.66 C ANISOU 2347 CB ALA A1080 9077 7272 3280 -61 1560 -1609 C ATOM 2348 N LYS A1081 13.654 73.330 87.871 1.00 49.61 N ANISOU 2348 N LYS A1081 8719 6660 3469 -127 1879 -1074 N ATOM 2349 CA LYS A1081 15.027 73.642 88.252 1.00 57.39 C ANISOU 2349 CA LYS A1081 9624 7546 4637 -147 2113 -917 C ATOM 2350 C LYS A1081 15.296 73.307 89.715 1.00 48.29 C ANISOU 2350 C LYS A1081 8246 6231 3872 -192 2081 -885 C ATOM 2351 O LYS A1081 16.413 72.912 90.067 1.00 52.11 O ANISOU 2351 O LYS A1081 8610 6638 4551 -198 2270 -867 O ATOM 2352 CB LYS A1081 15.330 75.122 87.991 1.00 51.28 C ANISOU 2352 CB LYS A1081 8933 6812 3738 -138 2155 -653 C ATOM 2353 CG LYS A1081 16.786 75.396 87.671 1.00 54.46 C ANISOU 2353 CG LYS A1081 9282 7187 4222 -152 2419 -535 C ATOM 2354 CD LYS A1081 16.970 76.816 87.140 1.00 62.40 C ANISOU 2354 CD LYS A1081 10386 8232 5092 -143 2455 -293 C ATOM 2355 CE LYS A1081 18.432 77.110 86.830 1.00 67.93 C ANISOU 2355 CE LYS A1081 11013 8900 5899 -178 2721 -186 C ATOM 2356 NZ LYS A1081 18.658 78.540 86.480 1.00 71.36 N ANISOU 2356 NZ LYS A1081 11523 9322 6267 -192 2777 57 N ATOM 2357 N LEU A1082 14.288 73.432 90.570 1.00 45.00 N ANISOU 2357 N LEU A1082 7762 5777 3558 -210 1846 -879 N ATOM 2358 CA LEU A1082 14.471 73.215 91.995 1.00 41.81 C ANISOU 2358 CA LEU A1082 7158 5243 3487 -240 1804 -826 C ATOM 2359 C LEU A1082 14.238 71.762 92.409 1.00 48.40 C ANISOU 2359 C LEU A1082 7903 5988 4499 -236 1804 -1017 C ATOM 2360 O LEU A1082 14.932 71.259 93.305 1.00 39.09 O ANISOU 2360 O LEU A1082 6567 4704 3580 -227 1891 -982 O ATOM 2361 CB LEU A1082 13.538 74.143 92.774 1.00 42.36 C ANISOU 2361 CB LEU A1082 7202 5308 3585 -258 1577 -707 C ATOM 2362 CG LEU A1082 13.855 75.637 92.596 1.00 43.51 C ANISOU 2362 CG LEU A1082 7420 5484 3626 -265 1602 -494 C ATOM 2363 CD1 LEU A1082 12.926 76.486 93.438 1.00 36.32 C ANISOU 2363 CD1 LEU A1082 6481 4547 2773 -271 1390 -394 C ATOM 2364 CD2 LEU A1082 15.307 75.924 92.958 1.00 45.36 C ANISOU 2364 CD2 LEU A1082 7548 5658 4028 -305 1813 -384 C ATOM 2365 N LYS A1083 13.275 71.080 91.782 1.00 42.36 N ANISOU 2365 N LYS A1083 7229 5263 3602 -240 1712 -1219 N ATOM 2366 CA LYS A1083 12.932 69.718 92.199 1.00 43.12 C ANISOU 2366 CA LYS A1083 7250 5241 3892 -254 1719 -1407 C ATOM 2367 C LYS A1083 14.132 68.776 92.241 1.00 46.14 C ANISOU 2367 C LYS A1083 7572 5511 4447 -215 1975 -1452 C ATOM 2368 O LYS A1083 14.322 68.114 93.274 1.00 47.32 O ANISOU 2368 O LYS A1083 7582 5520 4877 -198 2006 -1427 O ATOM 2369 CB LYS A1083 11.828 69.135 91.301 1.00 44.65 C ANISOU 2369 CB LYS A1083 7556 5511 3896 -285 1611 -1659 C ATOM 2370 CG LYS A1083 11.479 67.666 91.630 1.00 43.89 C ANISOU 2370 CG LYS A1083 7398 5262 4018 -322 1655 -1884 C ATOM 2371 CD LYS A1083 10.527 67.067 90.603 1.00 53.07 C ANISOU 2371 CD LYS A1083 8667 6515 4984 -376 1574 -2180 C ATOM 2372 CE LYS A1083 10.491 65.528 90.675 1.00 65.03 C ANISOU 2372 CE LYS A1083 10105 7855 6748 -403 1663 -2378 C ATOM 2373 NZ LYS A1083 10.178 65.023 92.043 1.00 66.61 N ANISOU 2373 NZ LYS A1083 10181 7848 7278 -436 1669 -2340 N ATOM 2374 N PRO A1084 14.972 68.665 91.201 1.00 50.82 N ANISOU 2374 N PRO A1084 8258 6161 4890 -185 2171 -1505 N ATOM 2375 CA PRO A1084 16.115 67.736 91.304 1.00 49.29 C ANISOU 2375 CA PRO A1084 7987 5855 4887 -129 2423 -1545 C ATOM 2376 C PRO A1084 17.018 68.023 92.492 1.00 49.50 C ANISOU 2376 C PRO A1084 7815 5817 5174 -93 2475 -1326 C ATOM 2377 O PRO A1084 17.512 67.090 93.136 1.00 43.92 O ANISOU 2377 O PRO A1084 6989 4983 4714 -33 2585 -1342 O ATOM 2378 CB PRO A1084 16.854 67.940 89.974 1.00 51.26 C ANISOU 2378 CB PRO A1084 8357 6221 4898 -103 2591 -1579 C ATOM 2379 CG PRO A1084 15.823 68.471 89.041 1.00 48.31 C ANISOU 2379 CG PRO A1084 8143 6003 4207 -138 2409 -1649 C ATOM 2380 CD PRO A1084 14.938 69.339 89.889 1.00 45.94 C ANISOU 2380 CD PRO A1084 7821 5715 3920 -182 2189 -1524 C ATOM 2381 N VAL A1085 17.247 69.298 92.800 1.00 44.36 N ANISOU 2381 N VAL A1085 7127 5254 4475 -123 2401 -1126 N ATOM 2382 CA VAL A1085 18.096 69.649 93.932 1.00 50.17 C ANISOU 2382 CA VAL A1085 7660 5961 5440 -104 2429 -943 C ATOM 2383 C VAL A1085 17.428 69.245 95.238 1.00 45.07 C ANISOU 2383 C VAL A1085 6896 5223 5004 -94 2267 -917 C ATOM 2384 O VAL A1085 18.019 68.537 96.059 1.00 41.89 O ANISOU 2384 O VAL A1085 6342 4746 4829 -24 2344 -879 O ATOM 2385 CB VAL A1085 18.427 71.156 93.908 1.00 50.93 C ANISOU 2385 CB VAL A1085 7757 6157 5436 -165 2394 -765 C ATOM 2386 CG1 VAL A1085 19.423 71.504 95.003 1.00 45.90 C ANISOU 2386 CG1 VAL A1085 6894 5517 5031 -162 2436 -616 C ATOM 2387 CG2 VAL A1085 18.973 71.550 92.537 1.00 54.86 C ANISOU 2387 CG2 VAL A1085 8401 6742 5701 -173 2571 -779 C ATOM 2388 N TYR A1086 16.187 69.696 95.448 1.00 40.71 N ANISOU 2388 N TYR A1086 6411 4686 4371 -150 2046 -925 N ATOM 2389 CA TYR A1086 15.463 69.395 96.678 1.00 39.30 C ANISOU 2389 CA TYR A1086 6129 4430 4373 -146 1896 -893 C ATOM 2390 C TYR A1086 15.416 67.894 96.942 1.00 42.57 C ANISOU 2390 C TYR A1086 6504 4701 4970 -90 1996 -1011 C ATOM 2391 O TYR A1086 15.644 67.447 98.072 1.00 43.28 O ANISOU 2391 O TYR A1086 6453 4714 5276 -32 2005 -920 O ATOM 2392 CB TYR A1086 14.044 69.974 96.601 1.00 35.45 C ANISOU 2392 CB TYR A1086 5736 3986 3750 -209 1668 -927 C ATOM 2393 CG TYR A1086 13.234 69.842 97.878 1.00 38.25 C ANISOU 2393 CG TYR A1086 5985 4277 4271 -213 1514 -879 C ATOM 2394 CD1 TYR A1086 13.322 70.805 98.877 1.00 44.11 C ANISOU 2394 CD1 TYR A1086 6632 5057 5072 -218 1411 -708 C ATOM 2395 CD2 TYR A1086 12.373 68.763 98.083 1.00 49.85 C ANISOU 2395 CD2 TYR A1086 7454 5646 5842 -220 1485 -1013 C ATOM 2396 CE1 TYR A1086 12.589 70.703 100.043 1.00 41.49 C ANISOU 2396 CE1 TYR A1086 6211 4682 4872 -213 1282 -664 C ATOM 2397 CE2 TYR A1086 11.630 68.650 99.265 1.00 46.82 C ANISOU 2397 CE2 TYR A1086 6975 5206 5610 -223 1367 -954 C ATOM 2398 CZ TYR A1086 11.753 69.630 100.235 1.00 45.59 C ANISOU 2398 CZ TYR A1086 6730 5107 5485 -211 1265 -775 C ATOM 2399 OH TYR A1086 11.042 69.559 101.404 1.00 53.80 O ANISOU 2399 OH TYR A1086 7682 6107 6651 -205 1158 -714 O ATOM 2400 N ASP A1087 15.107 67.103 95.906 1.00 40.72 N ANISOU 2400 N ASP A1087 6400 4425 4646 -103 2079 -1216 N ATOM 2401 CA ASP A1087 15.054 65.643 96.040 1.00 47.92 C ANISOU 2401 CA ASP A1087 7299 5164 5744 -61 2208 -1353 C ATOM 2402 C ASP A1087 16.355 65.074 96.591 1.00 46.91 C ANISOU 2402 C ASP A1087 7040 4960 5824 61 2411 -1244 C ATOM 2403 O ASP A1087 16.342 64.221 97.483 1.00 54.07 O ANISOU 2403 O ASP A1087 7858 5724 6961 131 2458 -1205 O ATOM 2404 CB ASP A1087 14.748 64.989 94.689 1.00 50.99 C ANISOU 2404 CB ASP A1087 7853 5541 5979 -100 2295 -1616 C ATOM 2405 CG ASP A1087 13.282 65.043 94.328 1.00 56.67 C ANISOU 2405 CG ASP A1087 8664 6300 6567 -206 2096 -1777 C ATOM 2406 OD1 ASP A1087 12.473 65.458 95.180 1.00 59.94 O ANISOU 2406 OD1 ASP A1087 9010 6719 7046 -242 1910 -1685 O ATOM 2407 OD2 ASP A1087 12.942 64.673 93.184 1.00 64.81 O ANISOU 2407 OD2 ASP A1087 9829 7375 7423 -251 2124 -2006 O ATOM 2408 N SER A1088 17.492 65.530 96.062 1.00 41.57 N ANISOU 2408 N SER A1088 6342 4382 5069 98 2542 -1184 N ATOM 2409 CA SER A1088 18.779 64.956 96.441 1.00 49.81 C ANISOU 2409 CA SER A1088 7246 5381 6299 227 2746 -1099 C ATOM 2410 C SER A1088 19.216 65.337 97.854 1.00 45.80 C ANISOU 2410 C SER A1088 6529 4913 5961 287 2661 -875 C ATOM 2411 O SER A1088 20.107 64.680 98.404 1.00 44.00 O ANISOU 2411 O SER A1088 6159 4642 5916 422 2798 -795 O ATOM 2412 CB SER A1088 19.859 65.397 95.455 1.00 51.59 C ANISOU 2412 CB SER A1088 7490 5721 6392 237 2915 -1104 C ATOM 2413 OG SER A1088 20.250 66.738 95.720 1.00 49.19 O ANISOU 2413 OG SER A1088 7105 5574 6011 180 2822 -937 O ATOM 2414 N LEU A1089 18.636 66.380 98.446 1.00 39.88 N ANISOU 2414 N LEU A1089 5754 4255 5144 204 2444 -775 N ATOM 2415 CA LEU A1089 19.126 66.888 99.722 1.00 41.46 C ANISOU 2415 CA LEU A1089 5756 4532 5464 248 2359 -584 C ATOM 2416 C LEU A1089 18.528 66.119 100.889 1.00 45.38 C ANISOU 2416 C LEU A1089 6190 4922 6132 323 2288 -530 C ATOM 2417 O LEU A1089 17.390 65.638 100.829 1.00 36.12 O ANISOU 2417 O LEU A1089 5132 3633 4959 278 2226 -625 O ATOM 2418 CB LEU A1089 18.791 68.371 99.894 1.00 38.27 C ANISOU 2418 CB LEU A1089 5359 4258 4924 127 2174 -509 C ATOM 2419 CG LEU A1089 19.473 69.385 98.975 1.00 40.87 C ANISOU 2419 CG LEU A1089 5728 4699 5102 50 2244 -499 C ATOM 2420 CD1 LEU A1089 18.929 70.776 99.281 1.00 36.39 C ANISOU 2420 CD1 LEU A1089 5188 4206 4434 -61 2059 -422 C ATOM 2421 CD2 LEU A1089 20.985 69.354 99.137 1.00 38.22 C ANISOU 2421 CD2 LEU A1089 5204 4438 4878 114 2411 -424 C ATOM 2422 N ASP A1090 19.307 66.031 101.967 1.00 43.63 N ANISOU 2422 N ASP A1090 5773 4755 6049 436 2298 -372 N ATOM 2423 CA ASP A1090 18.815 65.540 103.248 1.00 46.20 C ANISOU 2423 CA ASP A1090 6023 5024 6507 518 2215 -267 C ATOM 2424 C ASP A1090 17.840 66.546 103.870 1.00 45.07 C ANISOU 2424 C ASP A1090 5899 4955 6271 404 1977 -229 C ATOM 2425 O ASP A1090 17.712 67.694 103.428 1.00 40.70 O ANISOU 2425 O ASP A1090 5389 4503 5570 279 1877 -257 O ATOM 2426 CB ASP A1090 19.981 65.300 104.202 1.00 42.65 C ANISOU 2426 CB ASP A1090 5350 4669 6186 686 2272 -101 C ATOM 2427 CG ASP A1090 20.884 66.526 104.318 1.00 46.35 C ANISOU 2427 CG ASP A1090 5670 5365 6576 629 2200 -40 C ATOM 2428 OD1 ASP A1090 21.688 66.756 103.385 1.00 44.12 O ANISOU 2428 OD1 ASP A1090 5381 5130 6251 599 2327 -98 O ATOM 2429 OD2 ASP A1090 20.760 67.273 105.316 1.00 44.00 O ANISOU 2429 OD2 ASP A1090 5267 5192 6257 603 2028 52 O ATOM 2430 N ALA A1091 17.180 66.109 104.948 1.00 37.26 N ANISOU 2430 N ALA A1091 4873 3907 5376 460 1904 -151 N ATOM 2431 CA ALA A1091 16.082 66.885 105.529 1.00 33.29 C ANISOU 2431 CA ALA A1091 4403 3445 4800 363 1699 -134 C ATOM 2432 C ALA A1091 16.546 68.252 106.036 1.00 38.02 C ANISOU 2432 C ALA A1091 4898 4240 5307 314 1560 -51 C ATOM 2433 O ALA A1091 15.828 69.253 105.902 1.00 35.65 O ANISOU 2433 O ALA A1091 4671 3982 4893 193 1418 -87 O ATOM 2434 CB ALA A1091 15.424 66.073 106.651 1.00 30.48 C ANISOU 2434 CB ALA A1091 4014 2992 4573 451 1687 -47 C ATOM 2435 N VAL A1092 17.735 68.319 106.631 1.00 35.56 N ANISOU 2435 N VAL A1092 4409 4051 5052 407 1600 52 N ATOM 2436 CA VAL A1092 18.237 69.594 107.133 1.00 32.99 C ANISOU 2436 CA VAL A1092 3967 3908 4659 340 1479 100 C ATOM 2437 C VAL A1092 18.527 70.545 105.973 1.00 35.19 C ANISOU 2437 C VAL A1092 4327 4214 4830 197 1507 15 C ATOM 2438 O VAL A1092 18.109 71.711 105.974 1.00 33.94 O ANISOU 2438 O VAL A1092 4218 4100 4579 74 1388 1 O ATOM 2439 CB VAL A1092 19.490 69.364 108.002 1.00 35.60 C ANISOU 2439 CB VAL A1092 4061 4390 5076 475 1514 210 C ATOM 2440 CG1 VAL A1092 20.063 70.687 108.493 1.00 35.05 C ANISOU 2440 CG1 VAL A1092 3854 4516 4948 379 1394 220 C ATOM 2441 CG2 VAL A1092 19.171 68.439 109.183 1.00 36.93 C ANISOU 2441 CG2 VAL A1092 4166 4539 5327 643 1491 327 C ATOM 2442 N ARG A1093 19.266 70.071 104.973 1.00 31.56 N ANISOU 2442 N ARG A1093 3888 3723 4381 220 1683 -34 N ATOM 2443 CA ARG A1093 19.599 70.936 103.857 1.00 34.50 C ANISOU 2443 CA ARG A1093 4343 4126 4641 97 1739 -94 C ATOM 2444 C ARG A1093 18.355 71.330 103.068 1.00 38.02 C ANISOU 2444 C ARG A1093 5020 4485 4941 -4 1661 -175 C ATOM 2445 O ARG A1093 18.300 72.435 102.510 1.00 37.70 O ANISOU 2445 O ARG A1093 5058 4484 4783 -114 1630 -179 O ATOM 2446 CB ARG A1093 20.646 70.247 102.975 1.00 38.11 C ANISOU 2446 CB ARG A1093 4771 4574 5136 161 1963 -130 C ATOM 2447 CG ARG A1093 21.980 70.076 103.693 1.00 34.00 C ANISOU 2447 CG ARG A1093 3989 4183 4748 260 2031 -44 C ATOM 2448 CD ARG A1093 23.058 69.636 102.747 1.00 38.47 C ANISOU 2448 CD ARG A1093 4514 4759 5343 307 2260 -81 C ATOM 2449 NE ARG A1093 24.412 69.691 103.307 1.00 44.43 N ANISOU 2449 NE ARG A1093 4990 5678 6214 380 2322 -7 N ATOM 2450 CZ ARG A1093 24.985 68.698 103.985 1.00 45.81 C ANISOU 2450 CZ ARG A1093 4998 5883 6526 575 2375 62 C ATOM 2451 NH1 ARG A1093 24.314 67.581 104.208 1.00 42.68 N ANISOU 2451 NH1 ARG A1093 4703 5332 6181 704 2392 72 N ATOM 2452 NH2 ARG A1093 26.225 68.819 104.445 1.00 46.30 N ANISOU 2452 NH2 ARG A1093 4784 6129 6677 644 2417 123 N ATOM 2453 N ARG A1094 17.344 70.455 103.032 1.00 34.48 N ANISOU 2453 N ARG A1094 4673 3922 4505 33 1630 -235 N ATOM 2454 CA ARG A1094 16.045 70.836 102.478 1.00 33.16 C ANISOU 2454 CA ARG A1094 4685 3709 4206 -54 1513 -312 C ATOM 2455 C ARG A1094 15.474 72.058 103.189 1.00 32.54 C ANISOU 2455 C ARG A1094 4591 3694 4079 -121 1329 -242 C ATOM 2456 O ARG A1094 14.869 72.929 102.552 1.00 34.31 O ANISOU 2456 O ARG A1094 4944 3932 4163 -199 1255 -266 O ATOM 2457 CB ARG A1094 15.060 69.667 102.577 1.00 32.50 C ANISOU 2457 CB ARG A1094 4660 3500 4188 -15 1503 -394 C ATOM 2458 CG ARG A1094 15.201 68.662 101.454 1.00 32.07 C ANISOU 2458 CG ARG A1094 4707 3358 4120 3 1664 -533 C ATOM 2459 CD ARG A1094 14.213 67.518 101.576 1.00 33.25 C ANISOU 2459 CD ARG A1094 4908 3362 4363 13 1666 -636 C ATOM 2460 NE ARG A1094 14.483 66.510 100.532 1.00 35.13 N ANISOU 2460 NE ARG A1094 5238 3505 4606 30 1844 -793 N ATOM 2461 CZ ARG A1094 13.722 65.441 100.327 1.00 40.84 C ANISOU 2461 CZ ARG A1094 6029 4081 5409 14 1890 -939 C ATOM 2462 NH1 ARG A1094 12.653 65.232 101.094 1.00 34.48 N ANISOU 2462 NH1 ARG A1094 5201 3210 4690 -20 1777 -931 N ATOM 2463 NH2 ARG A1094 14.037 64.580 99.371 1.00 38.82 N ANISOU 2463 NH2 ARG A1094 5858 3738 5153 24 2061 -1101 N ATOM 2464 N ALA A1095 15.624 72.123 104.511 1.00 26.85 N ANISOU 2464 N ALA A1095 3723 3015 3465 -79 1257 -154 N ATOM 2465 CA ALA A1095 15.097 73.268 105.252 1.00 28.85 C ANISOU 2465 CA ALA A1095 3961 3322 3679 -139 1093 -106 C ATOM 2466 C ALA A1095 15.810 74.557 104.856 1.00 36.88 C ANISOU 2466 C ALA A1095 4979 4406 4628 -233 1110 -84 C ATOM 2467 O ALA A1095 15.183 75.625 104.764 1.00 31.71 O ANISOU 2467 O ALA A1095 4415 3743 3890 -307 1014 -79 O ATOM 2468 CB ALA A1095 15.230 73.014 106.750 1.00 28.04 C ANISOU 2468 CB ALA A1095 3695 3275 3685 -65 1027 -26 C ATOM 2469 N ALA A1096 17.123 74.482 104.621 1.00 32.76 N ANISOU 2469 N ALA A1096 4352 3941 4154 -229 1247 -68 N ATOM 2470 CA ALA A1096 17.844 75.668 104.175 1.00 33.14 C ANISOU 2470 CA ALA A1096 4398 4034 4160 -337 1300 -52 C ATOM 2471 C ALA A1096 17.312 76.156 102.829 1.00 40.75 C ANISOU 2471 C ALA A1096 5586 4929 4968 -396 1342 -78 C ATOM 2472 O ALA A1096 17.176 77.371 102.606 1.00 35.95 O ANISOU 2472 O ALA A1096 5056 4309 4294 -484 1317 -45 O ATOM 2473 CB ALA A1096 19.338 75.359 104.104 1.00 40.58 C ANISOU 2473 CB ALA A1096 5166 5059 5194 -318 1457 -40 C ATOM 2474 N LEU A1097 16.969 75.218 101.929 1.00 33.13 N ANISOU 2474 N LEU A1097 4734 3918 3935 -340 1408 -140 N ATOM 2475 CA LEU A1097 16.407 75.593 100.632 1.00 34.49 C ANISOU 2475 CA LEU A1097 5119 4062 3922 -374 1431 -172 C ATOM 2476 C LEU A1097 15.040 76.242 100.799 1.00 38.44 C ANISOU 2476 C LEU A1097 5734 4537 4335 -392 1243 -164 C ATOM 2477 O LEU A1097 14.742 77.257 100.156 1.00 33.66 O ANISOU 2477 O LEU A1097 5264 3930 3596 -433 1227 -121 O ATOM 2478 CB LEU A1097 16.304 74.375 99.712 1.00 30.27 C ANISOU 2478 CB LEU A1097 4668 3502 3332 -313 1528 -277 C ATOM 2479 CG LEU A1097 16.155 74.673 98.211 1.00 36.42 C ANISOU 2479 CG LEU A1097 5646 4300 3891 -335 1605 -317 C ATOM 2480 CD1 LEU A1097 17.416 75.335 97.678 1.00 38.05 C ANISOU 2480 CD1 LEU A1097 5835 4547 4077 -378 1790 -245 C ATOM 2481 CD2 LEU A1097 15.823 73.425 97.389 1.00 41.87 C ANISOU 2481 CD2 LEU A1097 6424 4968 4515 -283 1665 -466 C ATOM 2482 N ILE A1098 14.195 75.663 101.652 1.00 31.32 N ANISOU 2482 N ILE A1098 4779 3613 3508 -350 1112 -193 N ATOM 2483 CA ILE A1098 12.904 76.273 101.965 1.00 31.98 C ANISOU 2483 CA ILE A1098 4934 3683 3535 -359 934 -184 C ATOM 2484 C ILE A1098 13.109 77.654 102.573 1.00 36.25 C ANISOU 2484 C ILE A1098 5449 4231 4094 -412 885 -94 C ATOM 2485 O ILE A1098 12.332 78.587 102.321 1.00 36.56 O ANISOU 2485 O ILE A1098 5603 4251 4037 -426 800 -62 O ATOM 2486 CB ILE A1098 12.104 75.357 102.910 1.00 31.53 C ANISOU 2486 CB ILE A1098 4793 3599 3588 -311 837 -224 C ATOM 2487 CG1 ILE A1098 11.738 74.036 102.198 1.00 28.68 C ANISOU 2487 CG1 ILE A1098 4483 3199 3217 -280 893 -340 C ATOM 2488 CG2 ILE A1098 10.891 76.088 103.455 1.00 28.21 C ANISOU 2488 CG2 ILE A1098 4403 3179 3137 -318 663 -203 C ATOM 2489 CD1 ILE A1098 11.355 72.926 103.167 1.00 31.51 C ANISOU 2489 CD1 ILE A1098 4737 3498 3738 -234 879 -361 C ATOM 2490 N ASN A1099 14.156 77.800 103.386 1.00 32.35 N ANISOU 2490 N ASN A1099 4799 3766 3728 -439 941 -59 N ATOM 2491 CA ASN A1099 14.466 79.086 103.992 1.00 36.29 C ANISOU 2491 CA ASN A1099 5258 4267 4263 -514 911 -9 C ATOM 2492 C ASN A1099 14.701 80.141 102.914 1.00 35.53 C ANISOU 2492 C ASN A1099 5311 4124 4063 -581 1004 36 C ATOM 2493 O ASN A1099 14.112 81.229 102.958 1.00 37.41 O ANISOU 2493 O ASN A1099 5648 4306 4259 -610 942 79 O ATOM 2494 CB ASN A1099 15.680 78.935 104.914 1.00 25.75 C ANISOU 2494 CB ASN A1099 3705 3007 3070 -536 961 -7 C ATOM 2495 CG ASN A1099 15.967 80.185 105.753 1.00 34.34 C ANISOU 2495 CG ASN A1099 4722 4108 4216 -629 911 3 C ATOM 2496 OD1 ASN A1099 16.063 81.309 105.238 1.00 33.72 O ANISOU 2496 OD1 ASN A1099 4744 3964 4105 -719 963 25 O ATOM 2497 ND2 ASN A1099 16.145 79.977 107.058 1.00 32.06 N ANISOU 2497 ND2 ASN A1099 4262 3905 4015 -605 823 -15 N ATOM 2498 N MET A1100 15.538 79.824 101.919 1.00 32.02 N ANISOU 2498 N MET A1100 4896 3695 3575 -593 1169 37 N ATOM 2499 CA MET A1100 15.800 80.773 100.839 1.00 35.64 C ANISOU 2499 CA MET A1100 5509 4111 3921 -647 1289 101 C ATOM 2500 C MET A1100 14.533 81.067 100.044 1.00 42.07 C ANISOU 2500 C MET A1100 6542 4895 4547 -584 1198 128 C ATOM 2501 O MET A1100 14.324 82.204 99.605 1.00 37.94 O ANISOU 2501 O MET A1100 6156 4314 3945 -607 1223 216 O ATOM 2502 CB MET A1100 16.895 80.251 99.905 1.00 39.35 C ANISOU 2502 CB MET A1100 5968 4619 4364 -656 1495 93 C ATOM 2503 CG MET A1100 18.210 79.896 100.588 1.00 38.76 C ANISOU 2503 CG MET A1100 5653 4602 4473 -699 1593 68 C ATOM 2504 SD MET A1100 19.476 79.388 99.408 1.00 41.30 S ANISOU 2504 SD MET A1100 5962 4967 4763 -703 1861 63 S ATOM 2505 CE MET A1100 19.724 80.895 98.445 1.00 41.35 C ANISOU 2505 CE MET A1100 6144 4904 4665 -815 2011 168 C ATOM 2506 N VAL A1101 13.679 80.056 99.838 1.00 32.62 N ANISOU 2506 N VAL A1101 5375 3739 3281 -501 1097 52 N ATOM 2507 CA VAL A1101 12.440 80.287 99.096 1.00 33.97 C ANISOU 2507 CA VAL A1101 5719 3921 3265 -437 986 58 C ATOM 2508 C VAL A1101 11.508 81.218 99.869 1.00 36.61 C ANISOU 2508 C VAL A1101 6067 4211 3634 -425 831 112 C ATOM 2509 O VAL A1101 10.844 82.074 99.273 1.00 41.29 O ANISOU 2509 O VAL A1101 6812 4789 4088 -383 789 187 O ATOM 2510 CB VAL A1101 11.757 78.951 98.743 1.00 34.30 C ANISOU 2510 CB VAL A1101 5761 4021 3250 -378 916 -72 C ATOM 2511 CG1 VAL A1101 10.312 79.177 98.310 1.00 35.87 C ANISOU 2511 CG1 VAL A1101 6075 4262 3293 -315 745 -90 C ATOM 2512 CG2 VAL A1101 12.532 78.249 97.635 1.00 33.89 C ANISOU 2512 CG2 VAL A1101 5766 4008 3101 -373 1084 -127 C ATOM 2513 N PHE A1102 11.442 81.077 101.201 1.00 32.22 N ANISOU 2513 N PHE A1102 5355 3637 3250 -447 750 82 N ATOM 2514 CA PHE A1102 10.694 82.040 102.007 1.00 32.03 C ANISOU 2514 CA PHE A1102 5337 3564 3270 -441 630 126 C ATOM 2515 C PHE A1102 11.231 83.460 101.814 1.00 37.28 C ANISOU 2515 C PHE A1102 6090 4141 3935 -501 728 224 C ATOM 2516 O PHE A1102 10.455 84.415 101.705 1.00 38.12 O ANISOU 2516 O PHE A1102 6314 4186 3983 -460 670 292 O ATOM 2517 CB PHE A1102 10.754 81.666 103.494 1.00 31.40 C ANISOU 2517 CB PHE A1102 5072 3496 3362 -460 558 77 C ATOM 2518 CG PHE A1102 9.580 80.845 103.994 1.00 33.87 C ANISOU 2518 CG PHE A1102 5340 3844 3685 -389 414 19 C ATOM 2519 CD1 PHE A1102 9.451 79.499 103.654 1.00 30.68 C ANISOU 2519 CD1 PHE A1102 4902 3479 3275 -358 425 -53 C ATOM 2520 CD2 PHE A1102 8.651 81.402 104.872 1.00 38.40 C ANISOU 2520 CD2 PHE A1102 5895 4401 4296 -361 288 29 C ATOM 2521 CE1 PHE A1102 8.383 78.727 104.133 1.00 29.35 C ANISOU 2521 CE1 PHE A1102 4683 3325 3144 -314 316 -111 C ATOM 2522 CE2 PHE A1102 7.589 80.639 105.365 1.00 36.76 C ANISOU 2522 CE2 PHE A1102 5628 4226 4112 -307 176 -22 C ATOM 2523 CZ PHE A1102 7.461 79.290 104.995 1.00 36.98 C ANISOU 2523 CZ PHE A1102 5621 4287 4145 -291 194 -90 C ATOM 2524 N GLN A1103 12.556 83.626 101.780 1.00 36.72 N ANISOU 2524 N GLN A1103 5956 4054 3944 -596 889 235 N ATOM 2525 CA GLN A1103 13.098 84.981 101.723 1.00 40.59 C ANISOU 2525 CA GLN A1103 6510 4436 4478 -682 1002 313 C ATOM 2526 C GLN A1103 12.954 85.596 100.334 1.00 46.27 C ANISOU 2526 C GLN A1103 7454 5102 5023 -644 1110 429 C ATOM 2527 O GLN A1103 12.566 86.761 100.212 1.00 39.49 O ANISOU 2527 O GLN A1103 6730 4130 4145 -636 1127 525 O ATOM 2528 CB GLN A1103 14.566 85.008 102.162 1.00 41.32 C ANISOU 2528 CB GLN A1103 6434 4539 4726 -813 1142 274 C ATOM 2529 CG GLN A1103 15.172 86.445 102.287 1.00 38.79 C ANISOU 2529 CG GLN A1103 6147 4088 4503 -944 1268 322 C ATOM 2530 CD GLN A1103 16.688 86.419 102.495 1.00 45.95 C ANISOU 2530 CD GLN A1103 6870 5033 5554 -1086 1424 272 C ATOM 2531 OE1 GLN A1103 17.281 85.354 102.716 1.00 43.77 O ANISOU 2531 OE1 GLN A1103 6426 4892 5315 -1068 1418 208 O ATOM 2532 NE2 GLN A1103 17.322 87.586 102.409 1.00 43.76 N ANISOU 2532 NE2 GLN A1103 6620 4636 5370 -1225 1574 302 N ATOM 2533 N MET A1104 13.244 84.851 99.266 1.00 42.80 N ANISOU 2533 N MET A1104 7072 4742 4447 -606 1191 429 N ATOM 2534 CA MET A1104 13.305 85.496 97.957 1.00 46.21 C ANISOU 2534 CA MET A1104 7718 5141 4700 -572 1325 555 C ATOM 2535 C MET A1104 12.406 84.850 96.910 1.00 48.76 C ANISOU 2535 C MET A1104 8176 5579 4770 -434 1236 549 C ATOM 2536 O MET A1104 12.485 85.218 95.736 1.00 47.54 O ANISOU 2536 O MET A1104 8201 5440 4421 -384 1345 649 O ATOM 2537 CB MET A1104 14.749 85.538 97.444 1.00 40.62 C ANISOU 2537 CB MET A1104 6978 4419 4035 -678 1575 581 C ATOM 2538 CG MET A1104 15.302 84.181 97.083 1.00 51.80 C ANISOU 2538 CG MET A1104 8297 5963 5421 -663 1621 475 C ATOM 2539 SD MET A1104 17.092 84.223 96.938 1.00 63.38 S ANISOU 2539 SD MET A1104 9631 7422 7028 -801 1899 479 S ATOM 2540 CE MET A1104 17.498 85.097 98.433 1.00 59.01 C ANISOU 2540 CE MET A1104 8890 6779 6751 -939 1855 458 C ATOM 2541 N GLY A1105 11.559 83.909 97.290 1.00 46.30 N ANISOU 2541 N GLY A1105 7785 5356 4451 -374 1048 430 N ATOM 2542 CA GLY A1105 10.640 83.325 96.344 1.00 44.18 C ANISOU 2542 CA GLY A1105 7624 5208 3954 -261 945 390 C ATOM 2543 C GLY A1105 11.294 82.288 95.449 1.00 47.16 C ANISOU 2543 C GLY A1105 8013 5679 4227 -269 1062 302 C ATOM 2544 O GLY A1105 12.513 82.233 95.279 1.00 50.52 O ANISOU 2544 O GLY A1105 8407 6072 4716 -342 1259 320 O ATOM 2545 N GLU A1106 10.432 81.466 94.848 1.00 45.61 N ANISOU 2545 N GLU A1106 7859 5604 3869 -193 938 191 N ATOM 2546 CA GLU A1106 10.856 80.365 93.986 1.00 50.68 C ANISOU 2546 CA GLU A1106 8521 6338 4399 -192 1028 64 C ATOM 2547 C GLU A1106 11.750 80.830 92.838 1.00 51.10 C ANISOU 2547 C GLU A1106 8727 6415 4274 -184 1244 164 C ATOM 2548 O GLU A1106 12.758 80.185 92.522 1.00 51.82 O ANISOU 2548 O GLU A1106 8782 6512 4396 -230 1421 103 O ATOM 2549 CB GLU A1106 9.613 79.680 93.436 1.00 53.79 C ANISOU 2549 CB GLU A1106 8958 6864 4615 -117 842 -73 C ATOM 2550 CG GLU A1106 9.716 78.210 93.254 1.00 56.03 C ANISOU 2550 CG GLU A1106 9169 7191 4929 -149 862 -288 C ATOM 2551 CD GLU A1106 8.442 77.647 92.677 1.00 66.31 C ANISOU 2551 CD GLU A1106 10507 8630 6056 -97 673 -443 C ATOM 2552 OE1 GLU A1106 8.322 77.580 91.429 1.00 65.05 O ANISOU 2552 OE1 GLU A1106 10491 8612 5614 -43 687 -490 O ATOM 2553 OE2 GLU A1106 7.550 77.300 93.478 1.00 70.53 O ANISOU 2553 OE2 GLU A1106 10923 9147 6731 -112 510 -520 O ATOM 2554 N THR A1107 11.389 81.937 92.189 1.00 48.71 N ANISOU 2554 N THR A1107 8600 6126 3780 -114 1246 329 N ATOM 2555 CA THR A1107 12.131 82.381 91.012 1.00 55.68 C ANISOU 2555 CA THR A1107 9655 7042 4458 -91 1461 444 C ATOM 2556 C THR A1107 13.522 82.879 91.383 1.00 47.23 C ANISOU 2556 C THR A1107 8519 5832 3595 -212 1710 539 C ATOM 2557 O THR A1107 14.490 82.612 90.663 1.00 48.85 O ANISOU 2557 O THR A1107 8759 6067 3734 -241 1928 540 O ATOM 2558 CB THR A1107 11.349 83.472 90.278 1.00 61.51 C ANISOU 2558 CB THR A1107 10604 7821 4943 37 1405 627 C ATOM 2559 OG1 THR A1107 10.080 82.945 89.868 1.00 68.18 O ANISOU 2559 OG1 THR A1107 11482 8842 5582 151 1163 516 O ATOM 2560 CG2 THR A1107 12.115 83.951 89.048 1.00 58.81 C ANISOU 2560 CG2 THR A1107 10386 7517 4444 70 1612 756 C ATOM 2561 N GLY A1108 13.643 83.602 92.498 1.00 50.53 N ANISOU 2561 N GLY A1108 8831 6106 4262 -289 1684 604 N ATOM 2562 CA GLY A1108 14.956 84.066 92.920 1.00 52.02 C ANISOU 2562 CA GLY A1108 8922 6179 4666 -425 1902 661 C ATOM 2563 C GLY A1108 15.902 82.919 93.226 1.00 43.59 C ANISOU 2563 C GLY A1108 7658 5160 3745 -493 1986 510 C ATOM 2564 O GLY A1108 17.042 82.887 92.754 1.00 44.71 O ANISOU 2564 O GLY A1108 7778 5303 3907 -552 2221 535 O ATOM 2565 N VAL A1109 15.433 81.954 94.013 1.00 40.29 N ANISOU 2565 N VAL A1109 7094 4779 3435 -474 1808 362 N ATOM 2566 CA VAL A1109 16.272 80.814 94.373 1.00 44.86 C ANISOU 2566 CA VAL A1109 7487 5391 4165 -509 1883 234 C ATOM 2567 C VAL A1109 16.732 80.068 93.122 1.00 51.63 C ANISOU 2567 C VAL A1109 8440 6335 4841 -463 2047 176 C ATOM 2568 O VAL A1109 17.896 79.658 93.019 1.00 49.06 O ANISOU 2568 O VAL A1109 8011 6018 4612 -503 2243 150 O ATOM 2569 CB VAL A1109 15.516 79.905 95.359 1.00 42.71 C ANISOU 2569 CB VAL A1109 7083 5129 4016 -475 1670 108 C ATOM 2570 CG1 VAL A1109 16.342 78.673 95.715 1.00 40.76 C ANISOU 2570 CG1 VAL A1109 6660 4903 3923 -479 1757 -5 C ATOM 2571 CG2 VAL A1109 15.187 80.711 96.612 1.00 43.01 C ANISOU 2571 CG2 VAL A1109 7027 5093 4224 -522 1536 167 C ATOM 2572 N ALA A1110 15.848 79.929 92.129 1.00 48.96 N ANISOU 2572 N ALA A1110 8296 6078 4226 -373 1975 152 N ATOM 2573 CA ALA A1110 16.242 79.262 90.892 1.00 51.51 C ANISOU 2573 CA ALA A1110 8730 6500 4342 -326 2130 79 C ATOM 2574 C ALA A1110 17.399 79.967 90.195 1.00 51.95 C ANISOU 2574 C ALA A1110 8852 6543 4345 -367 2415 218 C ATOM 2575 O ALA A1110 18.089 79.341 89.383 1.00 56.31 O ANISOU 2575 O ALA A1110 9416 7162 4818 -345 2581 151 O ATOM 2576 CB ALA A1110 15.050 79.155 89.940 1.00 51.55 C ANISOU 2576 CB ALA A1110 8934 6626 4025 -222 1983 31 C ATOM 2577 N GLY A1111 17.631 81.247 90.490 1.00 47.78 N ANISOU 2577 N GLY A1111 8344 5921 3890 -427 2470 400 N ATOM 2578 CA GLY A1111 18.712 81.978 89.844 1.00 51.58 C ANISOU 2578 CA GLY A1111 8822 6373 4404 -473 2689 526 C ATOM 2579 C GLY A1111 20.108 81.557 90.263 1.00 55.71 C ANISOU 2579 C GLY A1111 9119 6874 5174 -571 2879 470 C ATOM 2580 O GLY A1111 21.070 81.940 89.591 1.00 55.92 O ANISOU 2580 O GLY A1111 9124 6905 5220 -601 3064 540 O ATOM 2581 N PHE A1112 20.244 80.787 91.347 1.00 51.15 N ANISOU 2581 N PHE A1112 8363 6286 4785 -611 2836 353 N ATOM 2582 CA PHE A1112 21.555 80.346 91.831 1.00 52.72 C ANISOU 2582 CA PHE A1112 8309 6491 5230 -679 2990 301 C ATOM 2583 C PHE A1112 21.995 79.077 91.094 1.00 55.40 C ANISOU 2583 C PHE A1112 8628 6920 5499 -589 3089 173 C ATOM 2584 O PHE A1112 22.194 78.019 91.689 1.00 51.36 O ANISOU 2584 O PHE A1112 7972 6426 5117 -558 3085 51 O ATOM 2585 CB PHE A1112 21.514 80.117 93.342 1.00 49.00 C ANISOU 2585 CB PHE A1112 7604 5988 5027 -721 2821 241 C ATOM 2586 CG PHE A1112 21.293 81.379 94.160 1.00 47.03 C ANISOU 2586 CG PHE A1112 7326 5647 4897 -823 2728 339 C ATOM 2587 CD1 PHE A1112 22.365 82.151 94.580 1.00 52.39 C ANISOU 2587 CD1 PHE A1112 7846 6289 5771 -964 2879 390 C ATOM 2588 CD2 PHE A1112 20.019 81.778 94.511 1.00 43.61 C ANISOU 2588 CD2 PHE A1112 7013 5165 4391 -783 2497 361 C ATOM 2589 CE1 PHE A1112 22.163 83.301 95.333 1.00 51.06 C ANISOU 2589 CE1 PHE A1112 7658 6021 5722 -1069 2804 449 C ATOM 2590 CE2 PHE A1112 19.810 82.925 95.265 1.00 49.64 C ANISOU 2590 CE2 PHE A1112 7760 5830 5270 -868 2426 437 C ATOM 2591 CZ PHE A1112 20.881 83.685 95.676 1.00 46.38 C ANISOU 2591 CZ PHE A1112 7206 5367 5051 -1015 2581 474 C ATOM 2592 N THR A1113 22.171 79.211 89.776 1.00 54.87 N ANISOU 2592 N THR A1113 8709 6908 5233 -539 3188 208 N ATOM 2593 CA THR A1113 22.316 78.033 88.918 1.00 53.76 C ANISOU 2593 CA THR A1113 8608 6854 4964 -442 3253 69 C ATOM 2594 C THR A1113 23.527 77.189 89.307 1.00 53.52 C ANISOU 2594 C THR A1113 8335 6830 5169 -448 3404 -13 C ATOM 2595 O THR A1113 23.410 75.978 89.517 1.00 55.93 O ANISOU 2595 O THR A1113 8588 7143 5520 -377 3382 -163 O ATOM 2596 CB THR A1113 22.408 78.456 87.448 1.00 57.40 C ANISOU 2596 CB THR A1113 9251 7391 5168 -394 3347 137 C ATOM 2597 OG1 THR A1113 21.254 79.230 87.098 1.00 57.68 O ANISOU 2597 OG1 THR A1113 9495 7438 4984 -359 3189 226 O ATOM 2598 CG2 THR A1113 22.471 77.231 86.548 1.00 53.82 C ANISOU 2598 CG2 THR A1113 8848 7036 4566 -298 3399 -32 C ATOM 2599 N ASN A1114 24.708 77.805 89.390 1.00 51.08 N ANISOU 2599 N ASN A1114 7871 6516 5021 -525 3558 82 N ATOM 2600 CA ASN A1114 25.903 77.036 89.731 1.00 53.14 C ANISOU 2600 CA ASN A1114 7880 6810 5500 -512 3690 14 C ATOM 2601 C ASN A1114 25.854 76.531 91.166 1.00 50.88 C ANISOU 2601 C ASN A1114 7384 6497 5452 -516 3582 -41 C ATOM 2602 O ASN A1114 26.288 75.409 91.447 1.00 51.18 O ANISOU 2602 O ASN A1114 7280 6557 5608 -429 3622 -139 O ATOM 2603 CB ASN A1114 27.155 77.881 89.500 1.00 55.50 C ANISOU 2603 CB ASN A1114 8045 7129 5915 -606 3865 121 C ATOM 2604 CG ASN A1114 27.466 78.054 88.033 1.00 70.24 C ANISOU 2604 CG ASN A1114 10076 9043 7570 -571 4024 161 C ATOM 2605 OD1 ASN A1114 26.844 78.865 87.349 1.00 78.54 O ANISOU 2605 OD1 ASN A1114 11347 10076 8418 -582 4001 257 O ATOM 2606 ND2 ASN A1114 28.428 77.287 87.537 1.00 72.52 N ANISOU 2606 ND2 ASN A1114 10256 9399 7898 -516 4188 94 N ATOM 2607 N SER A1115 25.328 77.341 92.089 1.00 47.57 N ANISOU 2607 N SER A1115 6944 6028 5105 -603 3449 26 N ATOM 2608 CA SER A1115 25.247 76.900 93.478 1.00 48.97 C ANISOU 2608 CA SER A1115 6919 6199 5490 -601 3341 -18 C ATOM 2609 C SER A1115 24.294 75.717 93.637 1.00 51.81 C ANISOU 2609 C SER A1115 7361 6533 5793 -476 3200 -133 C ATOM 2610 O SER A1115 24.583 74.777 94.386 1.00 47.88 O ANISOU 2610 O SER A1115 6679 6041 5470 -398 3164 -193 O ATOM 2611 CB SER A1115 24.831 78.067 94.370 1.00 44.13 C ANISOU 2611 CB SER A1115 6277 5538 4953 -721 3194 66 C ATOM 2612 OG SER A1115 25.912 78.973 94.486 1.00 58.85 O ANISOU 2612 OG SER A1115 7981 7419 6959 -846 3318 134 O ATOM 2613 N LEU A1116 23.156 75.741 92.940 1.00 56.39 N ANISOU 2613 N LEU A1116 8204 7085 6137 -448 3100 -163 N ATOM 2614 CA LEU A1116 22.246 74.600 92.982 1.00 55.35 C ANISOU 2614 CA LEU A1116 8143 6924 5962 -349 2961 -298 C ATOM 2615 C LEU A1116 22.903 73.351 92.398 1.00 57.58 C ANISOU 2615 C LEU A1116 8398 7218 6260 -255 3160 -423 C ATOM 2616 O LEU A1116 22.711 72.241 92.906 1.00 53.51 O ANISOU 2616 O LEU A1116 7807 6651 5874 -175 3108 -521 O ATOM 2617 CB LEU A1116 20.951 74.926 92.233 1.00 50.06 C ANISOU 2617 CB LEU A1116 7743 6260 5020 -345 2822 -322 C ATOM 2618 CG LEU A1116 20.041 76.001 92.846 1.00 51.08 C ANISOU 2618 CG LEU A1116 7915 6359 5134 -402 2597 -217 C ATOM 2619 CD1 LEU A1116 18.980 76.443 91.837 1.00 57.32 C ANISOU 2619 CD1 LEU A1116 8972 7190 5617 -376 2512 -213 C ATOM 2620 CD2 LEU A1116 19.397 75.521 94.143 1.00 38.78 C ANISOU 2620 CD2 LEU A1116 6219 4750 3767 -386 2377 -261 C ATOM 2621 N ARG A1117 23.679 73.505 91.327 1.00 50.28 N ANISOU 2621 N ARG A1117 7526 6350 5230 -254 3351 -410 N ATOM 2622 CA ARG A1117 24.374 72.342 90.786 1.00 55.84 C ANISOU 2622 CA ARG A1117 8175 7060 5982 -156 3490 -522 C ATOM 2623 C ARG A1117 25.370 71.786 91.800 1.00 55.54 C ANISOU 2623 C ARG A1117 7844 7010 6250 -107 3558 -501 C ATOM 2624 O ARG A1117 25.457 70.567 91.991 1.00 54.50 O ANISOU 2624 O ARG A1117 7655 6826 6229 3 3586 -602 O ATOM 2625 CB ARG A1117 25.073 72.696 89.472 1.00 56.36 C ANISOU 2625 CB ARG A1117 8323 7202 5888 -161 3647 -493 C ATOM 2626 CG ARG A1117 25.704 71.487 88.786 1.00 65.86 C ANISOU 2626 CG ARG A1117 9502 8415 7108 -56 3793 -624 C ATOM 2627 CD ARG A1117 26.702 71.896 87.707 1.00 76.00 C ANISOU 2627 CD ARG A1117 10795 9787 8294 -64 3984 -569 C ATOM 2628 NE ARG A1117 27.800 72.684 88.261 1.00 80.34 N ANISOU 2628 NE ARG A1117 11122 10366 9037 -133 4073 -423 N ATOM 2629 CZ ARG A1117 27.954 73.988 88.064 1.00 78.48 C ANISOU 2629 CZ ARG A1117 10918 10159 8740 -242 4092 -279 C ATOM 2630 NH1 ARG A1117 28.983 74.625 88.611 1.00 84.30 N ANISOU 2630 NH1 ARG A1117 11429 10920 9681 -320 4171 -179 N ATOM 2631 NH2 ARG A1117 27.088 74.650 87.306 1.00 67.60 N ANISOU 2631 NH2 ARG A1117 9793 8789 7101 -269 4030 -237 N ATOM 2632 N MET A1118 26.118 72.669 92.472 1.00 55.18 N ANISOU 2632 N MET A1118 7605 7014 6348 -184 3574 -372 N ATOM 2633 CA MET A1118 27.076 72.229 93.482 1.00 54.80 C ANISOU 2633 CA MET A1118 7249 7000 6572 -130 3605 -345 C ATOM 2634 C MET A1118 26.380 71.494 94.621 1.00 53.72 C ANISOU 2634 C MET A1118 7049 6800 6561 -52 3471 -379 C ATOM 2635 O MET A1118 26.892 70.484 95.120 1.00 55.02 O ANISOU 2635 O MET A1118 7050 6956 6898 79 3506 -402 O ATOM 2636 CB MET A1118 27.863 73.428 94.021 1.00 51.03 C ANISOU 2636 CB MET A1118 6576 6603 6209 -257 3610 -226 C ATOM 2637 CG MET A1118 28.820 74.055 93.006 1.00 55.92 C ANISOU 2637 CG MET A1118 7195 7282 6770 -324 3779 -181 C ATOM 2638 SD MET A1118 29.604 75.555 93.638 1.00 61.83 S ANISOU 2638 SD MET A1118 7736 8092 7665 -511 3776 -66 S ATOM 2639 CE MET A1118 30.549 76.084 92.215 1.00 60.56 C ANISOU 2639 CE MET A1118 7639 7968 7405 -565 4005 -21 C ATOM 2640 N LEU A1119 25.217 71.995 95.056 1.00 48.97 N ANISOU 2640 N LEU A1119 6570 6151 5884 -118 3254 -362 N ATOM 2641 CA LEU A1119 24.453 71.314 96.096 1.00 45.35 C ANISOU 2641 CA LEU A1119 6066 5628 5538 -46 3052 -381 C ATOM 2642 C LEU A1119 24.008 69.935 95.622 1.00 50.58 C ANISOU 2642 C LEU A1119 6849 6187 6182 71 3116 -515 C ATOM 2643 O LEU A1119 24.119 68.946 96.354 1.00 46.14 O ANISOU 2643 O LEU A1119 6168 5567 5797 189 3113 -525 O ATOM 2644 CB LEU A1119 23.242 72.160 96.508 1.00 40.07 C ANISOU 2644 CB LEU A1119 5518 4931 4775 -142 2799 -344 C ATOM 2645 CG LEU A1119 23.529 73.472 97.250 1.00 44.71 C ANISOU 2645 CG LEU A1119 5982 5584 5422 -258 2705 -228 C ATOM 2646 CD1 LEU A1119 22.250 74.215 97.580 1.00 45.02 C ANISOU 2646 CD1 LEU A1119 6165 5576 5365 -326 2474 -204 C ATOM 2647 CD2 LEU A1119 24.315 73.200 98.510 1.00 44.77 C ANISOU 2647 CD2 LEU A1119 5691 5660 5658 -207 2670 -182 C ATOM 2648 N GLN A1120 23.505 69.854 94.389 1.00 52.93 N ANISOU 2648 N GLN A1120 7388 6461 6262 44 3183 -623 N ATOM 2649 CA GLN A1120 23.038 68.579 93.858 1.00 51.56 C ANISOU 2649 CA GLN A1120 7342 6185 6062 128 3248 -792 C ATOM 2650 C GLN A1120 24.166 67.563 93.753 1.00 54.03 C ANISOU 2650 C GLN A1120 7519 6470 6541 255 3447 -819 C ATOM 2651 O GLN A1120 23.926 66.352 93.860 1.00 51.55 O ANISOU 2651 O GLN A1120 7222 6031 6333 348 3466 -916 O ATOM 2652 CB GLN A1120 22.394 68.797 92.493 1.00 60.72 C ANISOU 2652 CB GLN A1120 8772 7375 6924 69 3270 -911 C ATOM 2653 CG GLN A1120 21.723 67.572 91.926 1.00 73.13 C ANISOU 2653 CG GLN A1120 10475 8853 8457 117 3256 -1114 C ATOM 2654 CD GLN A1120 20.934 67.885 90.680 1.00 84.79 C ANISOU 2654 CD GLN A1120 12187 10407 9621 55 3184 -1224 C ATOM 2655 OE1 GLN A1120 20.123 67.081 90.231 1.00 92.36 O ANISOU 2655 OE1 GLN A1120 13258 11318 10516 57 3115 -1407 O ATOM 2656 NE2 GLN A1120 21.166 69.063 90.111 1.00 88.74 N ANISOU 2656 NE2 GLN A1120 12753 11034 9931 2 3192 -1106 N ATOM 2657 N GLN A1121 25.396 68.023 93.534 1.00 52.26 N ANISOU 2657 N GLN A1121 7151 6352 6354 256 3564 -727 N ATOM 2658 CA GLN A1121 26.545 67.130 93.494 1.00 54.34 C ANISOU 2658 CA GLN A1121 7252 6613 6783 385 3710 -729 C ATOM 2659 C GLN A1121 27.197 66.961 94.862 1.00 53.80 C ANISOU 2659 C GLN A1121 6896 6575 6969 474 3673 -604 C ATOM 2660 O GLN A1121 28.236 66.305 94.959 1.00 50.91 O ANISOU 2660 O GLN A1121 6360 6234 6747 595 3776 -578 O ATOM 2661 CB GLN A1121 27.572 67.634 92.470 1.00 51.98 C ANISOU 2661 CB GLN A1121 6935 6428 6388 349 3864 -709 C ATOM 2662 CG GLN A1121 27.000 67.829 91.068 1.00 56.11 C ANISOU 2662 CG GLN A1121 7736 6954 6629 283 3898 -814 C ATOM 2663 CD GLN A1121 28.015 68.398 90.077 1.00 66.51 C ANISOU 2663 CD GLN A1121 9037 8387 7846 251 4061 -769 C ATOM 2664 OE1 GLN A1121 29.185 68.580 90.403 1.00 71.93 O ANISOU 2664 OE1 GLN A1121 9495 9144 8689 271 4158 -680 O ATOM 2665 NE2 GLN A1121 27.563 68.679 88.860 1.00 67.85 N ANISOU 2665 NE2 GLN A1121 9441 8591 7749 205 4087 -832 N ATOM 2666 N LYS A1122 26.612 67.545 95.913 1.00 51.59 N ANISOU 2666 N LYS A1122 6554 6312 6735 425 3521 -525 N ATOM 2667 CA LYS A1122 27.085 67.389 97.293 1.00 53.40 C ANISOU 2667 CA LYS A1122 6515 6596 7178 519 3450 -406 C ATOM 2668 C LYS A1122 28.480 67.981 97.498 1.00 54.72 C ANISOU 2668 C LYS A1122 6411 6947 7433 509 3504 -315 C ATOM 2669 O LYS A1122 29.252 67.505 98.336 1.00 52.04 O ANISOU 2669 O LYS A1122 5826 6683 7266 641 3489 -241 O ATOM 2670 CB LYS A1122 27.058 65.920 97.735 1.00 60.50 C ANISOU 2670 CB LYS A1122 7385 7368 8234 711 3473 -420 C ATOM 2671 CG LYS A1122 25.731 65.215 97.482 1.00 60.49 C ANISOU 2671 CG LYS A1122 7638 7168 8177 705 3436 -538 C ATOM 2672 CD LYS A1122 25.515 64.070 98.448 1.00 60.55 C ANISOU 2672 CD LYS A1122 7581 7046 8380 866 3405 -488 C ATOM 2673 CE LYS A1122 24.480 63.083 97.914 1.00 65.60 C ANISOU 2673 CE LYS A1122 8462 7463 9001 857 3428 -642 C ATOM 2674 NZ LYS A1122 23.137 63.693 97.717 1.00 67.37 N ANISOU 2674 NZ LYS A1122 8873 7656 9069 700 3308 -740 N ATOM 2675 N ARG A1123 28.815 69.030 96.744 1.00 51.61 N ANISOU 2675 N ARG A1123 6057 6633 6920 355 3560 -316 N ATOM 2676 CA ARG A1123 30.063 69.760 96.962 1.00 54.69 C ANISOU 2676 CA ARG A1123 6185 7196 7399 299 3603 -244 C ATOM 2677 C ARG A1123 29.753 70.883 97.947 1.00 55.31 C ANISOU 2677 C ARG A1123 6158 7348 7511 163 3450 -175 C ATOM 2678 O ARG A1123 29.575 72.047 97.584 1.00 56.72 O ANISOU 2678 O ARG A1123 6422 7536 7592 -19 3445 -162 O ATOM 2679 CB ARG A1123 30.632 70.282 95.646 1.00 51.41 C ANISOU 2679 CB ARG A1123 5865 6810 6857 202 3763 -272 C ATOM 2680 CG ARG A1123 30.594 69.269 94.507 1.00 52.94 C ANISOU 2680 CG ARG A1123 6247 6910 6956 307 3902 -369 C ATOM 2681 CD ARG A1123 31.637 69.585 93.451 1.00 61.68 C ANISOU 2681 CD ARG A1123 7326 8103 8008 268 4086 -372 C ATOM 2682 NE ARG A1123 31.054 69.720 92.120 1.00 78.23 N ANISOU 2682 NE ARG A1123 9728 10133 9863 214 4161 -440 N ATOM 2683 CZ ARG A1123 31.028 70.853 91.421 1.00 89.58 C ANISOU 2683 CZ ARG A1123 11277 11613 11147 69 4199 -391 C ATOM 2684 NH1 ARG A1123 30.474 70.880 90.214 1.00 86.32 N ANISOU 2684 NH1 ARG A1123 11141 11163 10493 52 4253 -448 N ATOM 2685 NH2 ARG A1123 31.564 71.961 91.921 1.00 96.21 N ANISOU 2685 NH2 ARG A1123 11949 12533 12072 -57 4180 -286 N ATOM 2686 N TRP A1124 29.683 70.507 99.227 1.00 52.16 N ANISOU 2686 N TRP A1124 5573 6995 7251 263 3322 -127 N ATOM 2687 CA TRP A1124 29.161 71.411 100.245 1.00 52.49 C ANISOU 2687 CA TRP A1124 5557 7088 7299 150 3098 -80 C ATOM 2688 C TRP A1124 30.045 72.641 100.408 1.00 52.50 C ANISOU 2688 C TRP A1124 5351 7243 7353 -23 3119 -62 C ATOM 2689 O TRP A1124 29.559 73.777 100.360 1.00 48.53 O ANISOU 2689 O TRP A1124 4961 6706 6770 -211 3031 -62 O ATOM 2690 CB TRP A1124 29.023 70.679 101.576 1.00 53.79 C ANISOU 2690 CB TRP A1124 5561 7298 7580 315 2930 -23 C ATOM 2691 CG TRP A1124 28.283 69.370 101.499 1.00 49.70 C ANISOU 2691 CG TRP A1124 5212 6610 7061 490 2948 -35 C ATOM 2692 CD1 TRP A1124 28.733 68.154 101.928 1.00 51.12 C ANISOU 2692 CD1 TRP A1124 5265 6784 7376 722 3025 9 C ATOM 2693 CD2 TRP A1124 26.967 69.148 100.970 1.00 44.50 C ANISOU 2693 CD2 TRP A1124 4873 5760 6275 444 2896 -100 C ATOM 2694 NE1 TRP A1124 27.780 67.189 101.704 1.00 53.26 N ANISOU 2694 NE1 TRP A1124 5767 6843 7628 807 3041 -29 N ATOM 2695 CE2 TRP A1124 26.687 67.770 101.113 1.00 48.84 C ANISOU 2695 CE2 TRP A1124 5472 6180 6907 631 2955 -109 C ATOM 2696 CE3 TRP A1124 26.001 69.975 100.381 1.00 40.92 C ANISOU 2696 CE3 TRP A1124 4661 5235 5651 270 2808 -151 C ATOM 2697 CZ2 TRP A1124 25.481 67.201 100.696 1.00 43.24 C ANISOU 2697 CZ2 TRP A1124 5030 5277 6124 621 2927 -192 C ATOM 2698 CZ3 TRP A1124 24.804 69.404 99.960 1.00 43.21 C ANISOU 2698 CZ3 TRP A1124 5206 5363 5850 282 2763 -224 C ATOM 2699 CH2 TRP A1124 24.555 68.032 100.125 1.00 46.34 C ANISOU 2699 CH2 TRP A1124 5629 5636 6340 442 2821 -256 C ATOM 2700 N ASP A1125 31.350 72.434 100.611 1.00 48.75 N ANISOU 2700 N ASP A1125 4576 6933 7014 37 3208 -50 N ATOM 2701 CA ASP A1125 32.234 73.568 100.849 1.00 60.48 C ANISOU 2701 CA ASP A1125 5837 8575 8568 -142 3199 -52 C ATOM 2702 C ASP A1125 32.305 74.473 99.629 1.00 59.56 C ANISOU 2702 C ASP A1125 5917 8370 8342 -331 3338 -68 C ATOM 2703 O ASP A1125 32.335 75.701 99.764 1.00 54.95 O ANISOU 2703 O ASP A1125 5315 7797 7766 -538 3304 -67 O ATOM 2704 CB ASP A1125 33.621 73.078 101.254 1.00 69.37 C ANISOU 2704 CB ASP A1125 6608 9917 9831 -24 3225 -43 C ATOM 2705 CG ASP A1125 33.559 72.039 102.351 1.00 81.31 C ANISOU 2705 CG ASP A1125 7962 11509 11425 215 3096 1 C ATOM 2706 OD1 ASP A1125 33.877 70.865 102.069 1.00 83.62 O ANISOU 2706 OD1 ASP A1125 8263 11772 11738 426 3176 17 O ATOM 2707 OD2 ASP A1125 33.154 72.387 103.484 1.00 82.75 O ANISOU 2707 OD2 ASP A1125 8029 11767 11643 198 2916 22 O ATOM 2708 N GLU A1126 32.299 73.886 98.430 1.00 58.15 N ANISOU 2708 N GLU A1126 5942 8096 8057 -256 3493 -81 N ATOM 2709 CA GLU A1126 32.313 74.681 97.205 1.00 59.08 C ANISOU 2709 CA GLU A1126 6270 8136 8040 -401 3627 -76 C ATOM 2710 C GLU A1126 31.029 75.484 97.059 1.00 57.01 C ANISOU 2710 C GLU A1126 6298 7730 7633 -523 3541 -59 C ATOM 2711 O GLU A1126 31.062 76.677 96.741 1.00 58.41 O ANISOU 2711 O GLU A1126 6546 7876 7771 -699 3567 -23 O ATOM 2712 CB GLU A1126 32.501 73.774 95.992 1.00 58.38 C ANISOU 2712 CB GLU A1126 6339 7995 7849 -272 3794 -109 C ATOM 2713 CG GLU A1126 33.876 73.797 95.396 1.00 66.55 C ANISOU 2713 CG GLU A1126 7197 9143 8946 -276 3969 -104 C ATOM 2714 CD GLU A1126 33.922 73.064 94.072 1.00 75.73 C ANISOU 2714 CD GLU A1126 8566 10239 9971 -176 4140 -146 C ATOM 2715 OE1 GLU A1126 33.884 73.733 93.012 1.00 79.14 O ANISOU 2715 OE1 GLU A1126 9185 10629 10255 -279 4253 -127 O ATOM 2716 OE2 GLU A1126 33.974 71.815 94.099 1.00 76.23 O ANISOU 2716 OE2 GLU A1126 8611 10284 10068 10 4161 -197 O ATOM 2717 N ALA A1127 29.883 74.835 97.267 1.00 54.93 N ANISOU 2717 N ALA A1127 6212 7371 7290 -426 3444 -83 N ATOM 2718 CA ALA A1127 28.612 75.549 97.216 1.00 50.79 C ANISOU 2718 CA ALA A1127 5946 6730 6621 -526 3343 -67 C ATOM 2719 C ALA A1127 28.563 76.660 98.257 1.00 50.27 C ANISOU 2719 C ALA A1127 5749 6697 6654 -674 3178 -32 C ATOM 2720 O ALA A1127 28.022 77.741 97.997 1.00 47.50 O ANISOU 2720 O ALA A1127 5571 6263 6213 -813 3146 4 O ATOM 2721 CB ALA A1127 27.453 74.573 97.420 1.00 46.01 C ANISOU 2721 CB ALA A1127 5506 6037 5938 -384 3179 -109 C ATOM 2722 N ALA A1128 29.132 76.419 99.438 1.00 51.64 N ANISOU 2722 N ALA A1128 5618 6996 7006 -637 3071 -46 N ATOM 2723 CA ALA A1128 29.101 77.433 100.484 1.00 50.04 C ANISOU 2723 CA ALA A1128 5281 6843 6889 -777 2900 -45 C ATOM 2724 C ALA A1128 29.932 78.654 100.105 1.00 57.99 C ANISOU 2724 C ALA A1128 6202 7868 7965 -997 3065 -45 C ATOM 2725 O ALA A1128 29.523 79.791 100.369 1.00 52.98 O ANISOU 2725 O ALA A1128 5645 7159 7324 -1161 2988 -40 O ATOM 2726 CB ALA A1128 29.582 76.841 101.805 1.00 48.30 C ANISOU 2726 CB ALA A1128 4744 6791 6815 -669 2749 -65 C ATOM 2727 N VAL A1129 31.103 78.449 99.489 1.00 58.38 N ANISOU 2727 N VAL A1129 6110 8000 8071 -983 3234 -44 N ATOM 2728 CA VAL A1129 31.908 79.613 99.126 1.00 59.13 C ANISOU 2728 CA VAL A1129 6142 8098 8226 -1176 3327 -33 C ATOM 2729 C VAL A1129 31.260 80.357 97.969 1.00 59.75 C ANISOU 2729 C VAL A1129 6581 7984 8135 -1254 3427 34 C ATOM 2730 O VAL A1129 31.360 81.588 97.878 1.00 59.11 O ANISOU 2730 O VAL A1129 6549 7825 8087 -1430 3453 59 O ATOM 2731 CB VAL A1129 33.372 79.235 98.794 1.00 67.06 C ANISOU 2731 CB VAL A1129 6886 9257 9337 -1140 3468 -45 C ATOM 2732 CG1 VAL A1129 33.953 78.299 99.843 1.00 64.45 C ANISOU 2732 CG1 VAL A1129 6217 9132 9138 -995 3363 -88 C ATOM 2733 CG2 VAL A1129 33.504 78.651 97.397 1.00 73.53 C ANISOU 2733 CG2 VAL A1129 7904 10013 10021 -1036 3661 -6 C ATOM 2734 N ASN A1130 30.567 79.638 97.085 1.00 58.86 N ANISOU 2734 N ASN A1130 6731 7796 7837 -1117 3478 61 N ATOM 2735 CA ASN A1130 29.944 80.290 95.940 1.00 61.24 C ANISOU 2735 CA ASN A1130 7369 7953 7944 -1158 3557 133 C ATOM 2736 C ASN A1130 28.730 81.110 96.365 1.00 56.44 C ANISOU 2736 C ASN A1130 6959 7219 7268 -1233 3410 167 C ATOM 2737 O ASN A1130 28.532 82.234 95.882 1.00 61.10 O ANISOU 2737 O ASN A1130 7715 7697 7803 -1338 3452 241 O ATOM 2738 CB ASN A1130 29.569 79.244 94.894 1.00 57.29 C ANISOU 2738 CB ASN A1130 7073 7442 7252 -988 3632 124 C ATOM 2739 CG ASN A1130 29.541 79.812 93.501 1.00 66.99 C ANISOU 2739 CG ASN A1130 8550 8605 8296 -1012 3776 196 C ATOM 2740 OD1 ASN A1130 30.584 80.151 92.934 1.00 71.04 O ANISOU 2740 OD1 ASN A1130 8973 9158 8862 -1066 3943 226 O ATOM 2741 ND2 ASN A1130 28.347 79.925 92.937 1.00 69.21 N ANISOU 2741 ND2 ASN A1130 9142 8800 8354 -965 3710 229 N ATOM 2742 N LEU A1131 27.924 80.578 97.288 1.00 47.60 N ANISOU 2742 N LEU A1131 5817 6109 6158 -1172 3242 122 N ATOM 2743 CA LEU A1131 26.756 81.309 97.770 1.00 45.67 C ANISOU 2743 CA LEU A1131 5745 5755 5853 -1227 3071 150 C ATOM 2744 C LEU A1131 27.136 82.606 98.484 1.00 50.53 C ANISOU 2744 C LEU A1131 6236 6334 6629 -1427 3059 150 C ATOM 2745 O LEU A1131 26.350 83.560 98.495 1.00 48.67 O ANISOU 2745 O LEU A1131 6196 5961 6337 -1498 2996 200 O ATOM 2746 CB LEU A1131 25.933 80.417 98.691 1.00 43.45 C ANISOU 2746 CB LEU A1131 5428 5510 5569 -1084 2801 94 C ATOM 2747 CG LEU A1131 25.060 79.396 97.967 1.00 46.53 C ANISOU 2747 CG LEU A1131 6039 5866 5774 -917 2765 84 C ATOM 2748 CD1 LEU A1131 24.418 78.453 98.964 1.00 38.88 C ANISOU 2748 CD1 LEU A1131 4991 4926 4855 -791 2540 30 C ATOM 2749 CD2 LEU A1131 24.009 80.123 97.157 1.00 50.28 C ANISOU 2749 CD2 LEU A1131 6836 6226 6041 -939 2739 146 C ATOM 2750 N ALA A1132 28.323 82.663 99.087 1.00 54.75 N ANISOU 2750 N ALA A1132 6447 6992 7365 -1503 3086 86 N ATOM 2751 CA ALA A1132 28.764 83.868 99.779 1.00 54.02 C ANISOU 2751 CA ALA A1132 6217 6876 7434 -1697 3049 47 C ATOM 2752 C ALA A1132 29.229 84.972 98.835 1.00 55.55 C ANISOU 2752 C ALA A1132 6540 6940 7626 -1815 3217 117 C ATOM 2753 O ALA A1132 29.494 86.083 99.301 1.00 65.38 O ANISOU 2753 O ALA A1132 7723 8116 9002 -1982 3204 84 O ATOM 2754 CB ALA A1132 29.889 83.531 100.764 1.00 51.99 C ANISOU 2754 CB ALA A1132 5548 6829 7376 -1731 2998 -60 C ATOM 2755 N LYS A1133 29.340 84.702 97.536 1.00 57.91 N ANISOU 2755 N LYS A1133 7015 7204 7783 -1731 3377 204 N ATOM 2756 CA LYS A1133 29.721 85.708 96.551 1.00 63.06 C ANISOU 2756 CA LYS A1133 7812 7735 8412 -1819 3552 294 C ATOM 2757 C LYS A1133 28.517 86.393 95.910 1.00 62.56 C ANISOU 2757 C LYS A1133 8121 7486 8161 -1780 3535 410 C ATOM 2758 O LYS A1133 28.689 87.181 94.976 1.00 68.67 O ANISOU 2758 O LYS A1133 9058 8155 8879 -1813 3684 513 O ATOM 2759 CB LYS A1133 30.587 85.077 95.452 1.00 59.49 C ANISOU 2759 CB LYS A1133 7334 7370 7899 -1744 3747 327 C ATOM 2760 CG LYS A1133 31.895 84.454 95.927 1.00 58.23 C ANISOU 2760 CG LYS A1133 6802 7400 7924 -1763 3791 233 C ATOM 2761 CD LYS A1133 32.601 83.737 94.781 1.00 66.19 C ANISOU 2761 CD LYS A1133 7820 8483 8846 -1660 3983 268 C ATOM 2762 CE LYS A1133 33.944 83.172 95.219 1.00 74.70 C ANISOU 2762 CE LYS A1133 8519 9754 10111 -1666 4034 189 C ATOM 2763 NZ LYS A1133 34.611 82.381 94.138 1.00 78.21 N ANISOU 2763 NZ LYS A1133 8971 10275 10472 -1548 4221 213 N ATOM 2764 N SER A1134 27.314 86.118 96.395 1.00 54.89 N ANISOU 2764 N SER A1134 7281 6483 7092 -1702 3357 405 N ATOM 2765 CA SER A1134 26.085 86.557 95.757 1.00 57.56 C ANISOU 2765 CA SER A1134 7963 6687 7220 -1618 3313 517 C ATOM 2766 C SER A1134 25.633 87.912 96.286 1.00 60.67 C ANISOU 2766 C SER A1134 8438 6908 7704 -1728 3257 552 C ATOM 2767 O SER A1134 26.090 88.394 97.326 1.00 60.89 O ANISOU 2767 O SER A1134 8260 6927 7948 -1872 3211 457 O ATOM 2768 CB SER A1134 24.979 85.531 95.994 1.00 54.30 C ANISOU 2768 CB SER A1134 7648 6331 6651 -1472 3148 487 C ATOM 2769 OG SER A1134 24.665 85.466 97.378 1.00 52.14 O ANISOU 2769 OG SER A1134 7218 6073 6518 -1530 2984 399 O ATOM 2770 N ARG A1135 24.687 88.517 95.561 1.00 61.98 N ANISOU 2770 N ARG A1135 8909 6947 7694 -1645 3252 683 N ATOM 2771 CA ARG A1135 24.030 89.719 96.060 1.00 61.19 C ANISOU 2771 CA ARG A1135 8922 6668 7659 -1702 3182 724 C ATOM 2772 C ARG A1135 23.181 89.415 97.284 1.00 59.04 C ANISOU 2772 C ARG A1135 8596 6409 7426 -1696 2960 633 C ATOM 2773 O ARG A1135 22.949 90.300 98.116 1.00 56.91 O ANISOU 2773 O ARG A1135 8304 6023 7295 -1790 2893 595 O ATOM 2774 CB ARG A1135 23.169 90.346 94.961 1.00 71.69 C ANISOU 2774 CB ARG A1135 10581 7885 8774 -1571 3217 901 C ATOM 2775 CG ARG A1135 22.793 91.801 95.216 1.00 84.43 C ANISOU 2775 CG ARG A1135 12311 9284 10485 -1627 3228 970 C ATOM 2776 CD ARG A1135 22.020 92.405 94.045 1.00 94.31 C ANISOU 2776 CD ARG A1135 13869 10446 11517 -1470 3276 1167 C ATOM 2777 NE ARG A1135 20.708 91.787 93.876 1.00100.47 N ANISOU 2777 NE ARG A1135 14814 11302 12058 -1280 3085 1208 N ATOM 2778 CZ ARG A1135 19.621 92.137 94.559 1.00101.23 C ANISOU 2778 CZ ARG A1135 14989 11320 12152 -1225 2911 1212 C ATOM 2779 NH1 ARG A1135 19.685 93.104 95.465 1.00100.63 N ANISOU 2779 NH1 ARG A1135 14855 11082 12300 -1342 2908 1172 N ATOM 2780 NH2 ARG A1135 18.468 91.517 94.341 1.00100.66 N ANISOU 2780 NH2 ARG A1135 15050 11339 11856 -1052 2738 1243 N ATOM 2781 N TRP A1136 22.699 88.176 97.400 1.00 49.90 N ANISOU 2781 N TRP A1136 7426 5388 6148 -1585 2852 592 N ATOM 2782 CA TRP A1136 21.896 87.781 98.547 1.00 46.24 C ANISOU 2782 CA TRP A1136 6901 4953 5714 -1562 2632 508 C ATOM 2783 C TRP A1136 22.702 87.876 99.833 1.00 44.74 C ANISOU 2783 C TRP A1136 6395 4828 5777 -1709 2578 360 C ATOM 2784 O TRP A1136 22.200 88.332 100.864 1.00 44.67 O ANISOU 2784 O TRP A1136 6343 4779 5852 -1741 2408 294 O ATOM 2785 CB TRP A1136 21.379 86.349 98.333 1.00 43.39 C ANISOU 2785 CB TRP A1136 6541 4749 5197 -1374 2484 467 C ATOM 2786 CG TRP A1136 20.894 85.634 99.557 1.00 38.07 C ANISOU 2786 CG TRP A1136 5702 4168 4595 -1311 2223 349 C ATOM 2787 CD1 TRP A1136 19.910 86.039 100.412 1.00 36.57 C ANISOU 2787 CD1 TRP A1136 5550 3924 4422 -1285 2017 329 C ATOM 2788 CD2 TRP A1136 21.334 84.343 100.034 1.00 38.91 C ANISOU 2788 CD2 TRP A1136 5592 4435 4756 -1243 2157 252 C ATOM 2789 NE1 TRP A1136 19.714 85.082 101.400 1.00 39.26 N ANISOU 2789 NE1 TRP A1136 5712 4388 4816 -1214 1829 228 N ATOM 2790 CE2 TRP A1136 20.580 84.041 101.190 1.00 41.91 C ANISOU 2790 CE2 TRP A1136 5895 4850 5178 -1184 1912 188 C ATOM 2791 CE3 TRP A1136 22.300 83.426 99.601 1.00 40.12 C ANISOU 2791 CE3 TRP A1136 5612 4699 4931 -1216 2295 221 C ATOM 2792 CZ2 TRP A1136 20.763 82.856 101.920 1.00 40.65 C ANISOU 2792 CZ2 TRP A1136 5542 4825 5079 -1096 1808 113 C ATOM 2793 CZ3 TRP A1136 22.484 82.257 100.332 1.00 40.43 C ANISOU 2793 CZ3 TRP A1136 5454 4866 5041 -1123 2186 139 C ATOM 2794 CH2 TRP A1136 21.717 81.984 101.479 1.00 34.89 C ANISOU 2794 CH2 TRP A1136 4691 4189 4378 -1063 1946 95 C ATOM 2795 N TYR A1137 23.944 87.398 99.800 1.00 46.80 N ANISOU 2795 N TYR A1137 6421 5213 6149 -1784 2713 300 N ATOM 2796 CA TYR A1137 24.810 87.472 100.968 1.00 46.67 C ANISOU 2796 CA TYR A1137 6073 5302 6357 -1917 2660 154 C ATOM 2797 C TYR A1137 25.162 88.923 101.287 1.00 52.96 C ANISOU 2797 C TYR A1137 6856 5958 7309 -2094 2703 120 C ATOM 2798 O TYR A1137 25.228 89.310 102.457 1.00 54.75 O ANISOU 2798 O TYR A1137 6916 6210 7674 -2201 2582 -9 O ATOM 2799 CB TYR A1137 26.070 86.636 100.716 1.00 48.16 C ANISOU 2799 CB TYR A1137 6011 5672 6615 -1913 2780 109 C ATOM 2800 CG TYR A1137 27.042 86.537 101.875 1.00 56.27 C ANISOU 2800 CG TYR A1137 6656 6872 7850 -2015 2710 -40 C ATOM 2801 CD1 TYR A1137 27.038 85.431 102.724 1.00 57.75 C ANISOU 2801 CD1 TYR A1137 6644 7258 8041 -1880 2524 -111 C ATOM 2802 CD2 TYR A1137 27.983 87.538 102.108 1.00 57.69 C ANISOU 2802 CD2 TYR A1137 6684 7035 8200 -2190 2768 -108 C ATOM 2803 CE1 TYR A1137 27.936 85.340 103.779 1.00 60.35 C ANISOU 2803 CE1 TYR A1137 6615 7782 8533 -1950 2447 -238 C ATOM 2804 CE2 TYR A1137 28.877 87.455 103.151 1.00 52.97 C ANISOU 2804 CE2 TYR A1137 5730 6628 7768 -2275 2679 -256 C ATOM 2805 CZ TYR A1137 28.854 86.361 103.979 1.00 63.45 C ANISOU 2805 CZ TYR A1137 6844 8174 9092 -2165 2535 -320 C ATOM 2806 OH TYR A1137 29.756 86.292 105.010 1.00 71.82 O ANISOU 2806 OH TYR A1137 7542 9456 10290 -2222 2426 -458 O ATOM 2807 N ASN A1138 25.384 89.736 100.254 1.00 49.58 N ANISOU 2807 N ASN A1138 6602 5384 6851 -2115 2871 228 N ATOM 2808 CA ASN A1138 25.713 91.143 100.464 1.00 56.06 C ANISOU 2808 CA ASN A1138 7433 6043 7826 -2269 2935 203 C ATOM 2809 C ASN A1138 24.564 91.887 101.134 1.00 54.20 C ANISOU 2809 C ASN A1138 7360 5649 7584 -2263 2795 196 C ATOM 2810 O ASN A1138 24.790 92.731 102.007 1.00 58.30 O ANISOU 2810 O ASN A1138 7775 6106 8272 -2403 2754 75 O ATOM 2811 CB ASN A1138 26.079 91.786 99.124 1.00 60.52 C ANISOU 2811 CB ASN A1138 8178 6478 8338 -2262 3159 350 C ATOM 2812 CG ASN A1138 26.391 93.269 99.247 1.00 70.68 C ANISOU 2812 CG ASN A1138 9501 7566 9787 -2414 3259 338 C ATOM 2813 OD1 ASN A1138 25.532 94.118 98.994 1.00 75.51 O ANISOU 2813 OD1 ASN A1138 10367 7982 10343 -2363 3264 438 O ATOM 2814 ND2 ASN A1138 27.629 93.588 99.620 1.00 64.27 N ANISOU 2814 ND2 ASN A1138 8432 6808 9180 -2592 3343 215 N ATOM 2815 N GLN A1139 23.323 91.559 100.769 1.00 51.54 N ANISOU 2815 N GLN A1139 7270 5260 7052 -2097 2712 310 N ATOM 2816 CA GLN A1139 22.179 92.289 101.299 1.00 52.57 C ANISOU 2816 CA GLN A1139 7572 5234 7168 -2064 2588 324 C ATOM 2817 C GLN A1139 21.780 91.819 102.699 1.00 58.80 C ANISOU 2817 C GLN A1139 8198 6122 8021 -2097 2380 170 C ATOM 2818 O GLN A1139 21.441 92.651 103.550 1.00 52.01 O ANISOU 2818 O GLN A1139 7337 5159 7264 -2166 2299 85 O ATOM 2819 CB GLN A1139 21.001 92.186 100.326 1.00 58.55 C ANISOU 2819 CB GLN A1139 8648 5914 7685 -1862 2571 511 C ATOM 2820 CG GLN A1139 21.245 92.894 98.976 1.00 72.15 C ANISOU 2820 CG GLN A1139 10561 7524 9329 -1815 2765 675 C ATOM 2821 CD GLN A1139 21.557 94.378 99.122 1.00 82.88 C ANISOU 2821 CD GLN A1139 11955 8676 10862 -1931 2876 679 C ATOM 2822 OE1 GLN A1139 21.135 95.028 100.082 1.00 86.11 O ANISOU 2822 OE1 GLN A1139 12347 8983 11390 -1986 2781 594 O ATOM 2823 NE2 GLN A1139 22.303 94.923 98.161 1.00 90.31 N ANISOU 2823 NE2 GLN A1139 12947 9549 11817 -1967 3088 772 N ATOM 2824 N THR A1140 21.786 90.501 102.964 1.00 50.24 N ANISOU 2824 N THR A1140 6971 5255 6862 -2002 2256 126 N ATOM 2825 CA THR A1140 21.471 89.956 104.292 1.00 39.61 C ANISOU 2825 CA THR A1140 5439 4066 5547 -1950 1994 -15 C ATOM 2826 C THR A1140 22.556 88.971 104.714 1.00 45.05 C ANISOU 2826 C THR A1140 5809 5003 6304 -1968 1974 -114 C ATOM 2827 O THR A1140 22.354 87.746 104.678 1.00 44.96 O ANISOU 2827 O THR A1140 5751 5141 6190 -1798 1872 -91 O ATOM 2828 CB THR A1140 20.098 89.280 104.322 1.00 46.57 C ANISOU 2828 CB THR A1140 6477 4972 6246 -1723 1788 48 C ATOM 2829 OG1 THR A1140 20.037 88.227 103.338 1.00 47.77 O ANISOU 2829 OG1 THR A1140 6695 5207 6248 -1584 1825 139 O ATOM 2830 CG2 THR A1140 18.990 90.304 104.075 1.00 43.73 C ANISOU 2830 CG2 THR A1140 6394 4391 5829 -1687 1780 137 C ATOM 2831 N PRO A1141 23.712 89.474 105.151 1.00 45.88 N ANISOU 2831 N PRO A1141 5679 5159 6594 -2168 2071 -231 N ATOM 2832 CA PRO A1141 24.834 88.566 105.444 1.00 45.09 C ANISOU 2832 CA PRO A1141 5258 5312 6560 -2170 2071 -308 C ATOM 2833 C PRO A1141 24.621 87.701 106.673 1.00 50.19 C ANISOU 2833 C PRO A1141 5710 6181 7177 -2040 1807 -398 C ATOM 2834 O PRO A1141 25.037 86.538 106.668 1.00 55.57 O ANISOU 2834 O PRO A1141 6242 7047 7826 -1907 1776 -379 O ATOM 2835 CB PRO A1141 26.020 89.528 105.628 1.00 48.01 C ANISOU 2835 CB PRO A1141 5430 5671 7140 -2431 2226 -425 C ATOM 2836 CG PRO A1141 25.392 90.847 106.006 1.00 49.72 C ANISOU 2836 CG PRO A1141 5821 5669 7402 -2527 2186 -465 C ATOM 2837 CD PRO A1141 24.082 90.897 105.287 1.00 51.05 C ANISOU 2837 CD PRO A1141 6353 5634 7411 -2398 2204 -295 C ATOM 2838 N ASN A1142 24.020 88.243 107.738 1.00 47.85 N ANISOU 2838 N ASN A1142 5413 5872 6895 -2070 1633 -492 N ATOM 2839 CA ASN A1142 23.787 87.449 108.942 1.00 46.19 C ANISOU 2839 CA ASN A1142 5032 5881 6636 -1936 1392 -561 C ATOM 2840 C ASN A1142 22.933 86.230 108.635 1.00 48.35 C ANISOU 2840 C ASN A1142 5440 6176 6754 -1686 1306 -429 C ATOM 2841 O ASN A1142 23.271 85.105 109.023 1.00 48.00 O ANISOU 2841 O ASN A1142 5224 6327 6689 -1550 1232 -421 O ATOM 2842 CB ASN A1142 23.117 88.297 110.022 1.00 44.83 C ANISOU 2842 CB ASN A1142 4894 5663 6474 -1999 1240 -674 C ATOM 2843 CG ASN A1142 24.010 89.414 110.523 1.00 56.99 C ANISOU 2843 CG ASN A1142 6261 7209 8183 -2259 1303 -856 C ATOM 2844 OD1 ASN A1142 25.231 89.352 110.399 1.00 57.04 O ANISOU 2844 OD1 ASN A1142 6026 7346 8299 -2377 1402 -921 O ATOM 2845 ND2 ASN A1142 23.402 90.438 111.105 1.00 62.29 N ANISOU 2845 ND2 ASN A1142 7043 7739 8883 -2354 1252 -952 N ATOM 2846 N ARG A1143 21.813 86.441 107.943 1.00 41.85 N ANISOU 2846 N ARG A1143 4919 5153 5828 -1621 1319 -328 N ATOM 2847 CA ARG A1143 20.932 85.334 107.597 1.00 43.71 C ANISOU 2847 CA ARG A1143 5284 5398 5927 -1412 1241 -229 C ATOM 2848 C ARG A1143 21.606 84.370 106.630 1.00 36.33 C ANISOU 2848 C ARG A1143 4314 4521 4970 -1345 1381 -166 C ATOM 2849 O ARG A1143 21.541 83.149 106.813 1.00 36.67 O ANISOU 2849 O ARG A1143 4284 4674 4976 -1190 1318 -147 O ATOM 2850 CB ARG A1143 19.636 85.866 106.995 1.00 38.34 C ANISOU 2850 CB ARG A1143 4912 4516 5141 -1369 1223 -149 C ATOM 2851 CG ARG A1143 18.674 84.742 106.600 1.00 35.32 C ANISOU 2851 CG ARG A1143 4650 4148 4623 -1176 1139 -75 C ATOM 2852 CD ARG A1143 17.342 85.311 106.195 1.00 34.45 C ANISOU 2852 CD ARG A1143 4797 3884 4410 -1126 1081 -15 C ATOM 2853 NE ARG A1143 16.378 84.273 105.849 1.00 32.93 N ANISOU 2853 NE ARG A1143 4697 3715 4099 -965 991 26 N ATOM 2854 CZ ARG A1143 15.098 84.530 105.610 1.00 37.13 C ANISOU 2854 CZ ARG A1143 5409 4164 4535 -890 900 67 C ATOM 2855 NH1 ARG A1143 14.662 85.784 105.691 1.00 32.80 N ANISOU 2855 NH1 ARG A1143 4976 3492 3994 -941 896 90 N ATOM 2856 NH2 ARG A1143 14.257 83.550 105.307 1.00 31.95 N ANISOU 2856 NH2 ARG A1143 4808 3544 3788 -767 819 78 N ATOM 2857 N ALA A1144 22.253 84.905 105.592 1.00 38.54 N ANISOU 2857 N ALA A1144 4654 4714 5276 -1455 1590 -131 N ATOM 2858 CA ALA A1144 22.880 84.055 104.584 1.00 41.51 C ANISOU 2858 CA ALA A1144 5017 5136 5618 -1391 1749 -76 C ATOM 2859 C ALA A1144 23.977 83.195 105.191 1.00 45.64 C ANISOU 2859 C ALA A1144 5223 5874 6246 -1354 1746 -137 C ATOM 2860 O ALA A1144 24.133 82.028 104.817 1.00 47.42 O ANISOU 2860 O ALA A1144 5421 6166 6431 -1207 1782 -103 O ATOM 2861 CB ALA A1144 23.449 84.906 103.447 1.00 39.18 C ANISOU 2861 CB ALA A1144 4832 4720 5335 -1530 1994 -23 C ATOM 2862 N LYS A1145 24.775 83.766 106.101 1.00 47.25 N ANISOU 2862 N LYS A1145 5177 6190 6585 -1481 1712 -233 N ATOM 2863 CA LYS A1145 25.777 82.978 106.815 1.00 46.26 C ANISOU 2863 CA LYS A1145 4722 6308 6547 -1420 1673 -287 C ATOM 2864 C LYS A1145 25.145 81.769 107.501 1.00 44.06 C ANISOU 2864 C LYS A1145 4429 6122 6191 -1190 1497 -249 C ATOM 2865 O LYS A1145 25.691 80.659 107.447 1.00 43.92 O ANISOU 2865 O LYS A1145 4275 6223 6191 -1043 1535 -215 O ATOM 2866 CB LYS A1145 26.498 83.854 107.842 1.00 41.28 C ANISOU 2866 CB LYS A1145 3834 5806 6045 -1592 1605 -423 C ATOM 2867 CG LYS A1145 27.637 84.695 107.313 1.00 53.10 C ANISOU 2867 CG LYS A1145 5197 7294 7684 -1817 1812 -483 C ATOM 2868 CD LYS A1145 27.900 85.874 108.254 1.00 60.63 C ANISOU 2868 CD LYS A1145 6008 8279 8750 -2035 1734 -643 C ATOM 2869 CE LYS A1145 29.286 86.446 108.072 1.00 67.71 C ANISOU 2869 CE LYS A1145 6634 9264 9831 -2254 1907 -746 C ATOM 2870 NZ LYS A1145 29.549 87.588 108.987 1.00 72.27 N ANISOU 2870 NZ LYS A1145 7103 9853 10504 -2443 1799 -917 N ATOM 2871 N ARG A1146 23.989 81.961 108.148 1.00 35.78 N ANISOU 2871 N ARG A1146 3522 5007 5066 -1149 1322 -248 N ATOM 2872 CA ARG A1146 23.359 80.855 108.868 1.00 37.81 C ANISOU 2872 CA ARG A1146 3765 5339 5262 -944 1173 -205 C ATOM 2873 C ARG A1146 22.814 79.805 107.906 1.00 40.10 C ANISOU 2873 C ARG A1146 4239 5515 5480 -800 1254 -118 C ATOM 2874 O ARG A1146 22.915 78.597 108.173 1.00 37.36 O ANISOU 2874 O ARG A1146 3811 5244 5141 -629 1239 -76 O ATOM 2875 CB ARG A1146 22.236 81.375 109.774 1.00 33.20 C ANISOU 2875 CB ARG A1146 3285 4711 4618 -947 987 -230 C ATOM 2876 CG ARG A1146 22.703 82.289 110.925 1.00 37.70 C ANISOU 2876 CG ARG A1146 3663 5416 5243 -1070 880 -347 C ATOM 2877 CD ARG A1146 21.558 82.507 111.933 1.00 38.58 C ANISOU 2877 CD ARG A1146 3867 5515 5277 -1017 695 -365 C ATOM 2878 NE ARG A1146 20.538 83.433 111.432 1.00 37.69 N ANISOU 2878 NE ARG A1146 4023 5169 5130 -1103 710 -363 N ATOM 2879 CZ ARG A1146 20.603 84.759 111.580 1.00 41.30 C ANISOU 2879 CZ ARG A1146 4512 5543 5639 -1281 724 -457 C ATOM 2880 NH1 ARG A1146 19.638 85.541 111.106 1.00 34.25 N ANISOU 2880 NH1 ARG A1146 3871 4430 4713 -1320 745 -429 N ATOM 2881 NH2 ARG A1146 21.635 85.313 112.205 1.00 33.43 N ANISOU 2881 NH2 ARG A1146 3287 4683 4731 -1419 722 -585 N ATOM 2882 N VAL A1147 22.207 80.246 106.801 1.00 35.24 N ANISOU 2882 N VAL A1147 3880 4720 4791 -861 1339 -92 N ATOM 2883 CA VAL A1147 21.700 79.311 105.799 1.00 39.45 C ANISOU 2883 CA VAL A1147 4589 5160 5239 -746 1414 -43 C ATOM 2884 C VAL A1147 22.857 78.556 105.143 1.00 38.81 C ANISOU 2884 C VAL A1147 4385 5149 5211 -700 1599 -38 C ATOM 2885 O VAL A1147 22.765 77.348 104.874 1.00 36.92 O ANISOU 2885 O VAL A1147 4164 4905 4959 -553 1638 -21 O ATOM 2886 CB VAL A1147 20.835 80.071 104.770 1.00 35.74 C ANISOU 2886 CB VAL A1147 4407 4523 4651 -817 1450 -19 C ATOM 2887 CG1 VAL A1147 20.444 79.178 103.596 1.00 32.15 C ANISOU 2887 CG1 VAL A1147 4124 4004 4088 -720 1539 1 C ATOM 2888 CG2 VAL A1147 19.580 80.636 105.446 1.00 31.85 C ANISOU 2888 CG2 VAL A1147 4029 3963 4111 -818 1263 -20 C ATOM 2889 N ILE A1148 23.970 79.251 104.900 1.00 34.70 N ANISOU 2889 N ILE A1148 3728 4688 4767 -828 1727 -59 N ATOM 2890 CA ILE A1148 25.123 78.651 104.235 1.00 39.65 C ANISOU 2890 CA ILE A1148 4223 5390 5454 -793 1925 -56 C ATOM 2891 C ILE A1148 25.791 77.624 105.140 1.00 46.94 C ANISOU 2891 C ILE A1148 4873 6485 6475 -641 1873 -57 C ATOM 2892 O ILE A1148 26.198 76.549 104.684 1.00 46.45 O ANISOU 2892 O ILE A1148 4777 6440 6432 -500 1990 -35 O ATOM 2893 CB ILE A1148 26.104 79.755 103.799 1.00 41.11 C ANISOU 2893 CB ILE A1148 4317 5592 5711 -990 2083 -79 C ATOM 2894 CG1 ILE A1148 25.551 80.499 102.581 1.00 41.59 C ANISOU 2894 CG1 ILE A1148 4683 5469 5652 -1083 2206 -34 C ATOM 2895 CG2 ILE A1148 27.492 79.184 103.506 1.00 40.79 C ANISOU 2895 CG2 ILE A1148 4028 5692 5777 -958 2263 -91 C ATOM 2896 CD1 ILE A1148 26.339 81.766 102.207 1.00 40.49 C ANISOU 2896 CD1 ILE A1148 4500 5295 5592 -1299 2373 -37 C ATOM 2897 N THR A1149 25.924 77.943 106.430 1.00 48.34 N ANISOU 2897 N THR A1149 4858 6798 6711 -655 1704 -83 N ATOM 2898 CA THR A1149 26.391 76.964 107.409 1.00 50.89 C ANISOU 2898 CA THR A1149 4942 7299 7093 -474 1621 -57 C ATOM 2899 C THR A1149 25.532 75.708 107.393 1.00 47.11 C ANISOU 2899 C THR A1149 4620 6718 6562 -269 1594 13 C ATOM 2900 O THR A1149 26.050 74.589 107.480 1.00 53.62 O ANISOU 2900 O THR A1149 5326 7604 7443 -87 1662 61 O ATOM 2901 CB THR A1149 26.389 77.587 108.805 1.00 44.75 C ANISOU 2901 CB THR A1149 3992 6680 6331 -520 1414 -101 C ATOM 2902 OG1 THR A1149 27.419 78.570 108.871 1.00 43.45 O ANISOU 2902 OG1 THR A1149 3617 6639 6254 -706 1459 -190 O ATOM 2903 CG2 THR A1149 26.616 76.534 109.886 1.00 39.81 C ANISOU 2903 CG2 THR A1149 3170 6237 5720 -293 1303 -41 C ATOM 2904 N THR A1150 24.215 75.876 107.291 1.00 40.15 N ANISOU 2904 N THR A1150 3997 5675 5585 -294 1505 16 N ATOM 2905 CA THR A1150 23.325 74.725 107.224 1.00 33.75 C ANISOU 2905 CA THR A1150 3337 4748 4738 -135 1491 61 C ATOM 2906 C THR A1150 23.586 73.898 105.962 1.00 38.35 C ANISOU 2906 C THR A1150 4023 5226 5321 -74 1693 53 C ATOM 2907 O THR A1150 23.651 72.664 106.030 1.00 39.72 O ANISOU 2907 O THR A1150 4173 5371 5547 96 1755 85 O ATOM 2908 CB THR A1150 21.870 75.203 107.306 1.00 38.85 C ANISOU 2908 CB THR A1150 4214 5261 5287 -199 1355 48 C ATOM 2909 OG1 THR A1150 21.710 76.067 108.448 1.00 36.00 O ANISOU 2909 OG1 THR A1150 3757 4997 4923 -263 1188 38 O ATOM 2910 CG2 THR A1150 20.922 74.029 107.450 1.00 36.33 C ANISOU 2910 CG2 THR A1150 4010 4838 4957 -53 1326 81 C ATOM 2911 N PHE A1151 23.759 74.558 104.806 1.00 35.26 N ANISOU 2911 N PHE A1151 3753 4773 4872 -206 1814 11 N ATOM 2912 CA PHE A1151 24.144 73.845 103.585 1.00 41.37 C ANISOU 2912 CA PHE A1151 4612 5480 5627 -154 2023 -12 C ATOM 2913 C PHE A1151 25.511 73.189 103.726 1.00 43.72 C ANISOU 2913 C PHE A1151 4652 5904 6055 -46 2163 7 C ATOM 2914 O PHE A1151 25.715 72.060 103.266 1.00 42.56 O ANISOU 2914 O PHE A1151 4527 5703 5940 98 2297 2 O ATOM 2915 CB PHE A1151 24.170 74.790 102.381 1.00 37.30 C ANISOU 2915 CB PHE A1151 4261 4906 5004 -310 2135 -40 C ATOM 2916 CG PHE A1151 22.824 75.044 101.771 1.00 41.06 C ANISOU 2916 CG PHE A1151 5034 5245 5322 -351 2056 -60 C ATOM 2917 CD1 PHE A1151 21.948 74.000 101.526 1.00 39.20 C ANISOU 2917 CD1 PHE A1151 4939 4918 5037 -244 2025 -99 C ATOM 2918 CD2 PHE A1151 22.436 76.335 101.436 1.00 38.88 C ANISOU 2918 CD2 PHE A1151 4888 4932 4955 -496 2019 -42 C ATOM 2919 CE1 PHE A1151 20.701 74.239 100.955 1.00 39.55 C ANISOU 2919 CE1 PHE A1151 5227 4869 4932 -284 1937 -132 C ATOM 2920 CE2 PHE A1151 21.188 76.581 100.871 1.00 38.03 C ANISOU 2920 CE2 PHE A1151 5037 4723 4691 -508 1935 -49 C ATOM 2921 CZ PHE A1151 20.324 75.540 100.631 1.00 40.27 C ANISOU 2921 CZ PHE A1151 5435 4950 4915 -405 1884 -100 C ATOM 2922 N ARG A1152 26.475 73.897 104.325 1.00 41.38 N ANISOU 2922 N ARG A1152 4103 5779 5842 -115 2144 17 N ATOM 2923 CA ARG A1152 27.831 73.360 104.402 1.00 43.29 C ANISOU 2923 CA ARG A1152 4068 6172 6208 -15 2277 32 C ATOM 2924 C ARG A1152 27.893 72.129 105.298 1.00 51.25 C ANISOU 2924 C ARG A1152 4946 7236 7292 230 2218 98 C ATOM 2925 O ARG A1152 28.563 71.146 104.963 1.00 51.78 O ANISOU 2925 O ARG A1152 4927 7311 7434 394 2378 121 O ATOM 2926 CB ARG A1152 28.799 74.420 104.915 1.00 41.65 C ANISOU 2926 CB ARG A1152 3591 6157 6077 -160 2247 6 C ATOM 2927 CG ARG A1152 30.261 74.027 104.801 1.00 46.17 C ANISOU 2927 CG ARG A1152 3859 6906 6779 -87 2406 7 C ATOM 2928 CD ARG A1152 31.203 75.089 105.344 1.00 52.47 C ANISOU 2928 CD ARG A1152 4361 7909 7667 -257 2366 -46 C ATOM 2929 NE ARG A1152 31.150 75.163 106.800 1.00 59.81 N ANISOU 2929 NE ARG A1152 5093 9017 8616 -204 2120 -44 N ATOM 2930 CZ ARG A1152 30.552 76.138 107.474 1.00 70.04 C ANISOU 2930 CZ ARG A1152 6438 10310 9862 -361 1938 -94 C ATOM 2931 NH1 ARG A1152 29.964 77.137 106.818 1.00 71.13 N ANISOU 2931 NH1 ARG A1152 6816 10264 9947 -574 1980 -136 N ATOM 2932 NH2 ARG A1152 30.548 76.121 108.802 1.00 73.02 N ANISOU 2932 NH2 ARG A1152 6630 10875 10237 -292 1722 -98 N ATOM 2933 N THR A1153 27.203 72.162 106.438 1.00 46.29 N ANISOU 2933 N THR A1153 4306 6638 6642 270 2006 138 N ATOM 2934 CA THR A1153 27.373 71.136 107.458 1.00 47.79 C ANISOU 2934 CA THR A1153 4342 6916 6900 507 1945 231 C ATOM 2935 C THR A1153 26.231 70.132 107.512 1.00 50.71 C ANISOU 2935 C THR A1153 4944 7079 7246 635 1934 276 C ATOM 2936 O THR A1153 26.433 69.024 108.019 1.00 50.80 O ANISOU 2936 O THR A1153 4875 7092 7333 860 1975 367 O ATOM 2937 CB THR A1153 27.515 71.783 108.843 1.00 45.16 C ANISOU 2937 CB THR A1153 3800 6804 6556 489 1725 254 C ATOM 2938 OG1 THR A1153 26.243 72.315 109.258 1.00 41.12 O ANISOU 2938 OG1 THR A1153 3491 6188 5945 389 1561 238 O ATOM 2939 CG2 THR A1153 28.552 72.904 108.802 1.00 48.57 C ANISOU 2939 CG2 THR A1153 4004 7428 7023 310 1726 172 C ATOM 2940 N GLY A1154 25.046 70.487 107.022 1.00 44.11 N ANISOU 2940 N GLY A1154 4381 6065 6315 501 1886 218 N ATOM 2941 CA GLY A1154 23.892 69.635 107.215 1.00 40.87 C ANISOU 2941 CA GLY A1154 4158 5476 5894 591 1852 245 C ATOM 2942 C GLY A1154 23.430 69.522 108.649 1.00 44.02 C ANISOU 2942 C GLY A1154 4475 5952 6298 683 1678 340 C ATOM 2943 O GLY A1154 22.728 68.566 108.996 1.00 40.58 O ANISOU 2943 O GLY A1154 4134 5387 5898 809 1690 398 O ATOM 2944 N THR A1155 23.802 70.474 109.497 1.00 38.56 N ANISOU 2944 N THR A1155 3613 5467 5571 618 1527 350 N ATOM 2945 CA THR A1155 23.397 70.503 110.893 1.00 35.94 C ANISOU 2945 CA THR A1155 3201 5247 5209 698 1352 429 C ATOM 2946 C THR A1155 22.613 71.778 111.178 1.00 38.65 C ANISOU 2946 C THR A1155 3632 5601 5451 498 1185 353 C ATOM 2947 O THR A1155 22.561 72.712 110.362 1.00 39.02 O ANISOU 2947 O THR A1155 3769 5592 5464 306 1204 256 O ATOM 2948 CB THR A1155 24.613 70.419 111.827 1.00 43.03 C ANISOU 2948 CB THR A1155 3781 6428 6143 836 1307 499 C ATOM 2949 OG1 THR A1155 25.290 71.684 111.844 1.00 45.46 O ANISOU 2949 OG1 THR A1155 3937 6913 6424 649 1232 396 O ATOM 2950 CG2 THR A1155 25.591 69.346 111.344 1.00 41.58 C ANISOU 2950 CG2 THR A1155 3484 6243 6071 1023 1498 562 C ATOM 2951 N TRP A1156 21.999 71.814 112.362 1.00 33.80 N ANISOU 2951 N TRP A1156 2998 5055 4787 558 1035 408 N ATOM 2952 CA TRP A1156 21.277 72.994 112.822 1.00 33.44 C ANISOU 2952 CA TRP A1156 3017 5036 4654 397 875 338 C ATOM 2953 C TRP A1156 22.160 73.953 113.625 1.00 31.66 C ANISOU 2953 C TRP A1156 2558 5069 4402 329 759 285 C ATOM 2954 O TRP A1156 21.630 74.850 114.293 1.00 35.08 O ANISOU 2954 O TRP A1156 3014 5551 4764 229 618 228 O ATOM 2955 CB TRP A1156 20.071 72.579 113.672 1.00 33.73 C ANISOU 2955 CB TRP A1156 3164 5010 4643 485 784 407 C ATOM 2956 CG TRP A1156 19.023 71.779 112.954 1.00 41.08 C ANISOU 2956 CG TRP A1156 4320 5683 5604 506 875 423 C ATOM 2957 CD1 TRP A1156 18.775 70.436 113.085 1.00 40.29 C ANISOU 2957 CD1 TRP A1156 4255 5477 5575 677 974 521 C ATOM 2958 CD2 TRP A1156 18.065 72.273 112.009 1.00 36.88 C ANISOU 2958 CD2 TRP A1156 4002 4973 5037 350 876 329 C ATOM 2959 NE1 TRP A1156 17.727 70.072 112.276 1.00 38.24 N ANISOU 2959 NE1 TRP A1156 4209 4987 5335 611 1034 467 N ATOM 2960 CE2 TRP A1156 17.278 71.179 111.603 1.00 40.70 C ANISOU 2960 CE2 TRP A1156 4625 5269 5570 420 963 351 C ATOM 2961 CE3 TRP A1156 17.804 73.536 111.458 1.00 34.39 C ANISOU 2961 CE3 TRP A1156 3772 4638 4656 165 817 232 C ATOM 2962 CZ2 TRP A1156 16.248 71.307 110.670 1.00 47.91 C ANISOU 2962 CZ2 TRP A1156 5738 6015 6451 308 969 263 C ATOM 2963 CZ3 TRP A1156 16.774 73.660 110.534 1.00 32.91 C ANISOU 2963 CZ3 TRP A1156 3798 4277 4429 82 829 175 C ATOM 2964 CH2 TRP A1156 16.011 72.557 110.154 1.00 38.26 C ANISOU 2964 CH2 TRP A1156 4588 4808 5140 152 892 183 C ATOM 2965 N ASP A1157 23.487 73.787 113.557 1.00 34.92 N ANISOU 2965 N ASP A1157 2739 5651 4876 375 820 287 N ATOM 2966 CA ASP A1157 24.397 74.488 114.464 1.00 44.97 C ANISOU 2966 CA ASP A1157 3738 7216 6132 338 699 230 C ATOM 2967 C ASP A1157 24.234 76.008 114.403 1.00 46.18 C ANISOU 2967 C ASP A1157 3928 7360 6258 67 624 74 C ATOM 2968 O ASP A1157 24.371 76.690 115.423 1.00 42.73 O ANISOU 2968 O ASP A1157 3355 7112 5768 16 471 2 O ATOM 2969 CB ASP A1157 25.845 74.110 114.154 1.00 51.14 C ANISOU 2969 CB ASP A1157 4261 8165 7006 406 801 239 C ATOM 2970 CG ASP A1157 26.154 72.649 114.460 1.00 63.02 C ANISOU 2970 CG ASP A1157 5682 9718 8543 710 864 403 C ATOM 2971 OD1 ASP A1157 25.397 72.013 115.231 1.00 60.88 O ANISOU 2971 OD1 ASP A1157 5498 9420 8213 871 796 514 O ATOM 2972 OD2 ASP A1157 27.161 72.138 113.926 1.00 66.60 O ANISOU 2972 OD2 ASP A1157 5987 10229 9090 794 998 428 O ATOM 2973 N ALA A1158 23.957 76.564 113.222 1.00 37.09 N ANISOU 2973 N ALA A1158 2964 5992 5138 -103 736 18 N ATOM 2974 CA ALA A1158 23.810 78.014 113.131 1.00 39.29 C ANISOU 2974 CA ALA A1158 3295 6226 5408 -347 694 -110 C ATOM 2975 C ALA A1158 22.528 78.512 113.778 1.00 42.59 C ANISOU 2975 C ALA A1158 3890 6558 5736 -374 553 -127 C ATOM 2976 O ALA A1158 22.346 79.727 113.909 1.00 42.99 O ANISOU 2976 O ALA A1158 3982 6573 5781 -554 506 -235 O ATOM 2977 CB ALA A1158 23.854 78.459 111.675 1.00 34.03 C ANISOU 2977 CB ALA A1158 2794 5351 4783 -493 868 -133 C ATOM 2978 N TYR A1159 21.643 77.608 114.187 1.00 38.81 N ANISOU 2978 N TYR A1159 3513 6033 5199 -199 503 -26 N ATOM 2979 CA TYR A1159 20.387 77.971 114.828 1.00 38.90 C ANISOU 2979 CA TYR A1159 3678 5973 5130 -203 383 -32 C ATOM 2980 C TYR A1159 20.298 77.428 116.250 1.00 37.20 C ANISOU 2980 C TYR A1159 3331 5959 4845 -36 256 24 C ATOM 2981 O TYR A1159 19.200 77.271 116.784 1.00 40.83 O ANISOU 2981 O TYR A1159 3919 6356 5240 27 190 67 O ATOM 2982 CB TYR A1159 19.215 77.483 113.972 1.00 33.29 C ANISOU 2982 CB TYR A1159 3232 5009 4408 -170 448 31 C ATOM 2983 CG TYR A1159 19.198 78.177 112.623 1.00 34.44 C ANISOU 2983 CG TYR A1159 3528 4982 4577 -328 553 -22 C ATOM 2984 CD1 TYR A1159 18.607 79.432 112.481 1.00 30.12 C ANISOU 2984 CD1 TYR A1159 3111 4334 3999 -479 509 -92 C ATOM 2985 CD2 TYR A1159 19.811 77.601 111.506 1.00 34.79 C ANISOU 2985 CD2 TYR A1159 3585 4967 4666 -314 709 5 C ATOM 2986 CE1 TYR A1159 18.603 80.090 111.261 1.00 30.99 C ANISOU 2986 CE1 TYR A1159 3369 4291 4116 -601 615 -112 C ATOM 2987 CE2 TYR A1159 19.814 78.251 110.277 1.00 38.10 C ANISOU 2987 CE2 TYR A1159 4149 5248 5079 -446 813 -30 C ATOM 2988 CZ TYR A1159 19.206 79.493 110.162 1.00 38.82 C ANISOU 2988 CZ TYR A1159 4375 5243 5131 -585 764 -77 C ATOM 2989 OH TYR A1159 19.188 80.142 108.957 1.00 35.33 O ANISOU 2989 OH TYR A1159 4090 4665 4668 -692 876 -82 O ATOM 2990 N LEU A 311 21.437 77.143 116.872 1.00 36.36 N ANISOU 2990 N LEU A 311 2963 6108 4743 44 223 31 N ATOM 2991 CA LEU A 311 21.442 76.561 118.207 1.00 50.38 C ANISOU 2991 CA LEU A 311 4608 8107 6427 237 107 110 C ATOM 2992 C LEU A 311 20.844 77.531 119.215 1.00 56.00 C ANISOU 2992 C LEU A 311 5339 8909 7029 152 -50 5 C ATOM 2993 O LEU A 311 21.329 78.659 119.374 1.00 67.30 O ANISOU 2993 O LEU A 311 6675 10435 8462 -31 -112 -164 O ATOM 2994 CB LEU A 311 22.870 76.191 118.604 1.00 59.01 C ANISOU 2994 CB LEU A 311 5392 9493 7537 339 90 124 C ATOM 2995 CG LEU A 311 23.029 75.195 119.753 1.00 68.74 C ANISOU 2995 CG LEU A 311 6489 10952 8677 620 16 278 C ATOM 2996 CD1 LEU A 311 22.571 73.815 119.325 1.00 66.64 C ANISOU 2996 CD1 LEU A 311 6366 10485 8468 825 160 477 C ATOM 2997 CD2 LEU A 311 24.478 75.156 120.225 1.00 77.67 C ANISOU 2997 CD2 LEU A 311 7276 12433 9802 693 -46 251 C ATOM 2998 N ASN A 312 19.765 77.107 119.864 1.00 41.82 N ANISOU 2998 N ASN A 312 3675 7066 5149 273 -94 95 N ATOM 2999 CA ASN A 312 19.217 77.798 121.023 1.00 42.99 C ANISOU 2999 CA ASN A 312 3822 7344 5168 254 -238 20 C ATOM 3000 C ASN A 312 18.791 76.739 122.036 1.00 48.86 C ANISOU 3000 C ASN A 312 4553 8207 5806 509 -269 196 C ATOM 3001 O ASN A 312 19.052 75.546 121.850 1.00 42.24 O ANISOU 3001 O ASN A 312 3686 7351 5011 690 -180 366 O ATOM 3002 CB ASN A 312 18.073 78.747 120.643 1.00 33.13 C ANISOU 3002 CB ASN A 312 2804 5853 3931 85 -237 -77 C ATOM 3003 CG ASN A 312 16.908 78.052 119.964 1.00 40.57 C ANISOU 3003 CG ASN A 312 3972 6525 4917 147 -142 46 C ATOM 3004 OD1 ASN A 312 16.723 76.831 120.059 1.00 38.25 O ANISOU 3004 OD1 ASN A 312 3687 6216 4631 324 -85 204 O ATOM 3005 ND2 ASN A 312 16.088 78.847 119.281 1.00 44.66 N ANISOU 3005 ND2 ASN A 312 4674 6825 5469 1 -123 -30 N ATOM 3006 N ASP A 313 18.150 77.182 123.124 1.00 51.31 N ANISOU 3006 N ASP A 313 8512 3879 7105 122 -738 396 N ATOM 3007 CA ASP A 313 17.818 76.263 124.210 1.00 51.28 C ANISOU 3007 CA ASP A 313 8569 3976 6941 204 -806 289 C ATOM 3008 C ASP A 313 16.866 75.165 123.745 1.00 38.26 C ANISOU 3008 C ASP A 313 6775 2630 5134 321 -581 313 C ATOM 3009 O ASP A 313 17.019 74.005 124.137 1.00 38.66 O ANISOU 3009 O ASP A 313 6706 2813 5169 303 -591 282 O ATOM 3010 CB ASP A 313 17.209 77.025 125.389 1.00 57.81 C ANISOU 3010 CB ASP A 313 9755 4647 7564 355 -942 175 C ATOM 3011 CG ASP A 313 18.252 77.714 126.255 1.00 71.35 C ANISOU 3011 CG ASP A 313 11639 6060 9412 229 -1250 109 C ATOM 3012 OD1 ASP A 313 19.460 77.464 126.074 1.00 76.64 O ANISOU 3012 OD1 ASP A 313 12113 6659 10349 17 -1372 156 O ATOM 3013 OD2 ASP A 313 17.850 78.513 127.127 1.00 79.29 O ANISOU 3013 OD2 ASP A 313 12984 6889 10255 350 -1377 18 O ATOM 3014 N HIS A 314 15.876 75.507 122.908 1.00 37.64 N ANISOU 3014 N HIS A 314 6705 2654 4941 439 -391 373 N ATOM 3015 CA HIS A 314 14.922 74.501 122.430 1.00 44.61 C ANISOU 3015 CA HIS A 314 7453 3808 5689 542 -207 406 C ATOM 3016 C HIS A 314 15.605 73.429 121.584 1.00 34.54 C ANISOU 3016 C HIS A 314 5901 2669 4555 407 -134 468 C ATOM 3017 O HIS A 314 15.248 72.245 121.660 1.00 36.18 O ANISOU 3017 O HIS A 314 5994 3062 4689 438 -78 456 O ATOM 3018 CB HIS A 314 13.810 75.166 121.616 1.00 43.03 C ANISOU 3018 CB HIS A 314 7310 3670 5370 678 -46 474 C ATOM 3019 CG HIS A 314 12.878 76.006 122.430 1.00 55.66 C ANISOU 3019 CG HIS A 314 9172 5188 6787 863 -64 429 C ATOM 3020 ND1 HIS A 314 11.943 76.843 121.858 1.00 61.62 N ANISOU 3020 ND1 HIS A 314 10017 5951 7446 994 56 490 N ATOM 3021 CD2 HIS A 314 12.737 76.145 123.770 1.00 60.39 C ANISOU 3021 CD2 HIS A 314 9981 5691 7272 957 -180 335 C ATOM 3022 CE1 HIS A 314 11.268 77.461 122.810 1.00 64.47 C ANISOU 3022 CE1 HIS A 314 10624 6225 7647 1165 27 442 C ATOM 3023 NE2 HIS A 314 11.728 77.053 123.979 1.00 63.14 N ANISOU 3023 NE2 HIS A 314 10544 5989 7455 1151 -114 346 N ATOM 3024 N LEU A 315 16.577 73.826 120.758 1.00 35.22 N ANISOU 3024 N LEU A 315 5881 2658 4844 267 -123 545 N ATOM 3025 CA LEU A 315 17.296 72.861 119.932 1.00 39.95 C ANISOU 3025 CA LEU A 315 6237 3366 5575 160 -33 618 C ATOM 3026 C LEU A 315 18.209 71.978 120.773 1.00 39.53 C ANISOU 3026 C LEU A 315 6087 3304 5629 56 -165 569 C ATOM 3027 O LEU A 315 18.276 70.762 120.557 1.00 38.80 O ANISOU 3027 O LEU A 315 5844 3375 5522 45 -93 578 O ATOM 3028 CB LEU A 315 18.095 73.587 118.851 1.00 44.68 C ANISOU 3028 CB LEU A 315 6757 3852 6368 63 38 738 C ATOM 3029 CG LEU A 315 19.000 72.718 117.969 1.00 50.32 C ANISOU 3029 CG LEU A 315 7239 4643 7237 -34 150 838 C ATOM 3030 CD1 LEU A 315 18.185 71.743 117.142 1.00 46.19 C ANISOU 3030 CD1 LEU A 315 6659 4349 6540 66 322 854 C ATOM 3031 CD2 LEU A 315 19.864 73.580 117.068 1.00 60.01 C ANISOU 3031 CD2 LEU A 315 8400 5722 8678 -121 218 976 C ATOM 3032 N LYS A 316 18.926 72.566 121.732 1.00 35.76 N ANISOU 3032 N LYS A 316 5701 2627 5258 -22 -370 518 N ATOM 3033 CA LYS A 316 19.744 71.749 122.626 1.00 37.97 C ANISOU 3033 CA LYS A 316 5905 2893 5628 -112 -520 468 C ATOM 3034 C LYS A 316 18.887 70.738 123.380 1.00 34.36 C ANISOU 3034 C LYS A 316 5497 2610 4949 12 -505 374 C ATOM 3035 O LYS A 316 19.293 69.590 123.579 1.00 37.77 O ANISOU 3035 O LYS A 316 5783 3150 5418 -34 -508 367 O ATOM 3036 CB LYS A 316 20.488 72.633 123.625 1.00 39.56 C ANISOU 3036 CB LYS A 316 6251 2833 5947 -198 -785 416 C ATOM 3037 CG LYS A 316 21.520 73.579 123.042 1.00 47.49 C ANISOU 3037 CG LYS A 316 7180 3634 7231 -355 -844 524 C ATOM 3038 CD LYS A 316 22.291 74.221 124.184 1.00 53.74 C ANISOU 3038 CD LYS A 316 8109 4166 8145 -457 -1161 461 C ATOM 3039 CE LYS A 316 23.349 75.183 123.683 1.00 65.47 C ANISOU 3039 CE LYS A 316 9505 5423 9947 -633 -1252 584 C ATOM 3040 NZ LYS A 316 24.225 75.635 124.804 1.00 71.29 N ANISOU 3040 NZ LYS A 316 10346 5903 10840 -762 -1605 531 N ATOM 3041 N GLN A 317 17.704 71.159 123.832 1.00 40.64 N ANISOU 3041 N GLN A 317 6493 3428 5520 177 -483 314 N ATOM 3042 CA GLN A 317 16.813 70.241 124.535 1.00 43.36 C ANISOU 3042 CA GLN A 317 6873 3936 5665 309 -447 253 C ATOM 3043 C GLN A 317 16.329 69.128 123.615 1.00 37.89 C ANISOU 3043 C GLN A 317 5976 3481 4940 324 -262 316 C ATOM 3044 O GLN A 317 16.269 67.955 124.020 1.00 37.34 O ANISOU 3044 O GLN A 317 5817 3541 4831 331 -257 289 O ATOM 3045 CB GLN A 317 15.631 71.013 125.129 1.00 56.22 C ANISOU 3045 CB GLN A 317 8752 5532 7078 501 -431 211 C ATOM 3046 CG GLN A 317 14.607 70.121 125.824 1.00 74.10 C ANISOU 3046 CG GLN A 317 11041 7966 9147 659 -362 182 C ATOM 3047 CD GLN A 317 13.578 70.902 126.614 1.00 95.02 C ANISOU 3047 CD GLN A 317 13956 10555 11593 868 -350 151 C ATOM 3048 OE1 GLN A 317 12.846 70.335 127.426 1.00105.06 O ANISOU 3048 OE1 GLN A 317 15288 11917 12711 1013 -311 132 O ATOM 3049 NE2 GLN A 317 13.510 72.211 126.376 1.00103.41 N ANISOU 3049 NE2 GLN A 317 15181 11458 12652 896 -369 157 N ATOM 3050 N ARG A 318 15.985 69.467 122.369 1.00 36.18 N ANISOU 3050 N ARG A 318 5697 3314 4734 331 -118 399 N ATOM 3051 CA ARG A 318 15.478 68.448 121.449 1.00 40.66 C ANISOU 3051 CA ARG A 318 6110 4086 5253 352 31 454 C ATOM 3052 C ARG A 318 16.548 67.432 121.105 1.00 31.67 C ANISOU 3052 C ARG A 318 4787 2990 4257 221 38 477 C ATOM 3053 O ARG A 318 16.263 66.228 121.018 1.00 33.67 O ANISOU 3053 O ARG A 318 4942 3399 4453 237 88 473 O ATOM 3054 CB ARG A 318 14.959 69.089 120.166 1.00 41.56 C ANISOU 3054 CB ARG A 318 6227 4222 5343 390 163 539 C ATOM 3055 CG ARG A 318 13.566 69.607 120.268 1.00 49.85 C ANISOU 3055 CG ARG A 318 7399 5323 6218 549 210 542 C ATOM 3056 CD ARG A 318 13.194 70.336 118.995 1.00 50.48 C ANISOU 3056 CD ARG A 318 7489 5401 6291 577 320 628 C ATOM 3057 NE ARG A 318 12.100 71.229 119.290 1.00 55.28 N ANISOU 3057 NE ARG A 318 8246 5989 6771 722 337 633 N ATOM 3058 CZ ARG A 318 12.094 72.525 119.024 1.00 50.54 C ANISOU 3058 CZ ARG A 318 7770 5250 6184 750 347 658 C ATOM 3059 NH1 ARG A 318 13.118 73.094 118.395 1.00 47.32 N ANISOU 3059 NH1 ARG A 318 7342 4713 5926 633 344 691 N ATOM 3060 NH2 ARG A 318 11.034 73.232 119.359 1.00 52.85 N ANISOU 3060 NH2 ARG A 318 8200 5536 6346 904 373 666 N ATOM 3061 N ARG A 319 17.778 67.899 120.866 1.00 36.72 N ANISOU 3061 N ARG A 319 5370 3487 5096 95 -6 518 N ATOM 3062 CA ARG A 319 18.870 66.970 120.587 1.00 34.22 C ANISOU 3062 CA ARG A 319 4869 3200 4934 -17 11 560 C ATOM 3063 C ARG A 319 19.035 65.979 121.725 1.00 34.47 C ANISOU 3063 C ARG A 319 4873 3285 4938 -27 -99 478 C ATOM 3064 O ARG A 319 19.160 64.768 121.498 1.00 38.54 O ANISOU 3064 O ARG A 319 5266 3932 5447 -38 -34 488 O ATOM 3065 CB ARG A 319 20.172 67.736 120.355 1.00 37.80 C ANISOU 3065 CB ARG A 319 5255 3469 5637 -148 -39 636 C ATOM 3066 CG ARG A 319 20.329 68.272 118.953 1.00 42.24 C ANISOU 3066 CG ARG A 319 5768 4013 6270 -154 129 759 C ATOM 3067 CD ARG A 319 21.559 69.175 118.877 1.00 50.49 C ANISOU 3067 CD ARG A 319 6747 4850 7585 -284 65 850 C ATOM 3068 NE ARG A 319 21.742 69.755 117.550 1.00 50.04 N ANISOU 3068 NE ARG A 319 6648 4762 7602 -279 242 986 N ATOM 3069 CZ ARG A 319 22.748 70.556 117.220 1.00 60.07 C ANISOU 3069 CZ ARG A 319 7838 5862 9124 -381 237 1106 C ATOM 3070 NH1 ARG A 319 23.662 70.876 118.125 1.00 63.04 N ANISOU 3070 NH1 ARG A 319 8163 6077 9712 -511 37 1105 N ATOM 3071 NH2 ARG A 319 22.840 71.039 115.989 1.00 61.31 N ANISOU 3071 NH2 ARG A 319 7967 6000 9326 -353 424 1237 N ATOM 3072 N GLU A 320 18.993 66.472 122.962 1.00 36.69 N ANISOU 3072 N GLU A 320 5293 3461 5186 -9 -266 393 N ATOM 3073 CA GLU A 320 19.215 65.604 124.113 1.00 42.51 C ANISOU 3073 CA GLU A 320 6026 4230 5895 -12 -382 316 C ATOM 3074 C GLU A 320 18.076 64.601 124.285 1.00 37.16 C ANISOU 3074 C GLU A 320 5351 3750 5018 110 -287 283 C ATOM 3075 O GLU A 320 18.324 63.421 124.556 1.00 36.42 O ANISOU 3075 O GLU A 320 5152 3755 4932 87 -286 269 O ATOM 3076 CB GLU A 320 19.411 66.466 125.361 1.00 37.13 C ANISOU 3076 CB GLU A 320 5540 3365 5201 -3 -592 233 C ATOM 3077 CG GLU A 320 19.479 65.709 126.656 1.00 48.05 C ANISOU 3077 CG GLU A 320 6981 4768 6508 30 -720 145 C ATOM 3078 CD GLU A 320 20.000 66.580 127.788 1.00 65.81 C ANISOU 3078 CD GLU A 320 9432 6794 8781 10 -965 69 C ATOM 3079 OE1 GLU A 320 20.951 67.367 127.556 1.00 57.27 O ANISOU 3079 OE1 GLU A 320 8326 5535 7900 -125 -1084 106 O ATOM 3080 OE2 GLU A 320 19.449 66.478 128.905 1.00 77.37 O ANISOU 3080 OE2 GLU A 320 11088 8249 10062 133 -1042 -20 O ATOM 3081 N VAL A 321 16.821 65.041 124.114 1.00 32.33 N ANISOU 3081 N VAL A 321 4848 3195 4242 240 -206 285 N ATOM 3082 CA VAL A 321 15.689 64.116 124.213 1.00 32.11 C ANISOU 3082 CA VAL A 321 4794 3348 4057 349 -117 284 C ATOM 3083 C VAL A 321 15.799 63.020 123.150 1.00 32.13 C ANISOU 3083 C VAL A 321 4614 3490 4104 288 -9 340 C ATOM 3084 O VAL A 321 15.619 61.832 123.435 1.00 34.01 O ANISOU 3084 O VAL A 321 4774 3844 4304 296 2 326 O ATOM 3085 CB VAL A 321 14.355 64.880 124.102 1.00 34.29 C ANISOU 3085 CB VAL A 321 5193 3651 4185 496 -45 308 C ATOM 3086 CG1 VAL A 321 13.198 63.903 123.965 1.00 33.79 C ANISOU 3086 CG1 VAL A 321 5051 3777 4009 585 51 347 C ATOM 3087 CG2 VAL A 321 14.132 65.777 125.325 1.00 35.27 C ANISOU 3087 CG2 VAL A 321 5535 3644 4221 596 -140 245 C ATOM 3088 N ALA A 322 16.106 63.407 121.907 1.00 29.55 N ANISOU 3088 N ALA A 322 4237 3143 3850 236 74 406 N ATOM 3089 CA ALA A 322 16.268 62.424 120.844 1.00 28.52 C ANISOU 3089 CA ALA A 322 3980 3118 3740 197 176 458 C ATOM 3090 C ALA A 322 17.360 61.416 121.188 1.00 34.12 C ANISOU 3090 C ALA A 322 4572 3832 4558 107 142 444 C ATOM 3091 O ALA A 322 17.151 60.204 121.096 1.00 37.61 O ANISOU 3091 O ALA A 322 4947 4393 4952 115 176 438 O ATOM 3092 CB ALA A 322 16.570 63.128 119.520 1.00 29.43 C ANISOU 3092 CB ALA A 322 4090 3179 3912 171 275 538 C ATOM 3093 N LYS A 323 18.531 61.900 121.609 1.00 36.38 N ANISOU 3093 N LYS A 323 4833 3985 5004 19 63 444 N ATOM 3094 CA LYS A 323 19.641 60.997 121.910 1.00 33.94 C ANISOU 3094 CA LYS A 323 4396 3675 4825 -67 30 450 C ATOM 3095 C LYS A 323 19.320 60.097 123.097 1.00 39.30 C ANISOU 3095 C LYS A 323 5088 4427 5418 -33 -60 367 C ATOM 3096 O LYS A 323 19.756 58.940 123.143 1.00 38.27 O ANISOU 3096 O LYS A 323 4853 4369 5319 -63 -39 370 O ATOM 3097 CB LYS A 323 20.917 61.795 122.178 1.00 33.77 C ANISOU 3097 CB LYS A 323 4332 3481 5019 -175 -66 485 C ATOM 3098 CG LYS A 323 21.511 62.433 120.943 1.00 48.94 C ANISOU 3098 CG LYS A 323 6187 5332 7074 -221 52 602 C ATOM 3099 CD LYS A 323 22.513 63.531 121.310 1.00 63.13 C ANISOU 3099 CD LYS A 323 7967 6932 9089 -325 -73 643 C ATOM 3100 CE LYS A 323 23.001 64.278 120.070 1.00 65.28 C ANISOU 3100 CE LYS A 323 8178 7130 9498 -358 64 778 C ATOM 3101 NZ LYS A 323 23.782 65.508 120.403 1.00 68.70 N ANISOU 3101 NZ LYS A 323 8609 7353 10142 -460 -70 825 N ATOM 3102 N THR A 324 18.573 60.615 124.074 1.00 37.41 N ANISOU 3102 N THR A 324 4988 4163 5064 43 -148 299 N ATOM 3103 CA THR A 324 18.219 59.807 125.234 1.00 37.13 C ANISOU 3103 CA THR A 324 4982 4192 4934 98 -216 232 C ATOM 3104 C THR A 324 17.373 58.612 124.820 1.00 40.15 C ANISOU 3104 C THR A 324 5291 4750 5214 150 -104 252 C ATOM 3105 O THR A 324 17.649 57.475 125.219 1.00 37.76 O ANISOU 3105 O THR A 324 4912 4516 4921 130 -117 236 O ATOM 3106 CB THR A 324 17.469 60.651 126.270 1.00 40.44 C ANISOU 3106 CB THR A 324 5595 4548 5224 207 -297 174 C ATOM 3107 OG1 THR A 324 18.246 61.800 126.626 1.00 46.59 O ANISOU 3107 OG1 THR A 324 6470 5137 6095 152 -428 150 O ATOM 3108 CG2 THR A 324 17.173 59.838 127.534 1.00 38.27 C ANISOU 3108 CG2 THR A 324 5367 4327 4848 281 -356 116 C ATOM 3109 N VAL A 325 16.334 58.856 124.014 1.00 33.34 N ANISOU 3109 N VAL A 325 4453 3955 4261 213 -8 294 N ATOM 3110 CA VAL A 325 15.428 57.788 123.612 1.00 33.55 C ANISOU 3110 CA VAL A 325 4418 4130 4200 255 64 321 C ATOM 3111 C VAL A 325 16.150 56.808 122.707 1.00 34.34 C ANISOU 3111 C VAL A 325 4407 4270 4371 172 119 348 C ATOM 3112 O VAL A 325 16.019 55.586 122.861 1.00 32.21 O ANISOU 3112 O VAL A 325 4076 4087 4077 168 124 341 O ATOM 3113 CB VAL A 325 14.174 58.359 122.923 1.00 31.48 C ANISOU 3113 CB VAL A 325 4205 3914 3843 335 128 371 C ATOM 3114 CG1 VAL A 325 13.220 57.211 122.555 1.00 31.30 C ANISOU 3114 CG1 VAL A 325 4109 4031 3754 363 165 409 C ATOM 3115 CG2 VAL A 325 13.472 59.350 123.824 1.00 28.34 C ANISOU 3115 CG2 VAL A 325 3929 3469 3369 441 97 356 C ATOM 3116 N PHE A 326 16.926 57.326 121.753 1.00 27.51 N ANISOU 3116 N PHE A 326 3525 3334 3594 115 170 388 N ATOM 3117 CA PHE A 326 17.627 56.441 120.842 1.00 31.12 C ANISOU 3117 CA PHE A 326 3903 3819 4104 65 249 428 C ATOM 3118 C PHE A 326 18.577 55.527 121.611 1.00 34.85 C ANISOU 3118 C PHE A 326 4287 4292 4664 12 205 402 C ATOM 3119 O PHE A 326 18.609 54.314 121.378 1.00 34.46 O ANISOU 3119 O PHE A 326 4190 4317 4586 10 243 404 O ATOM 3120 CB PHE A 326 18.386 57.253 119.789 1.00 31.60 C ANISOU 3120 CB PHE A 326 3961 3790 4256 32 332 497 C ATOM 3121 CG PHE A 326 19.125 56.397 118.816 1.00 37.40 C ANISOU 3121 CG PHE A 326 4638 4541 5030 12 443 554 C ATOM 3122 CD1 PHE A 326 18.486 55.892 117.698 1.00 42.03 C ANISOU 3122 CD1 PHE A 326 5287 5190 5493 65 525 579 C ATOM 3123 CD2 PHE A 326 20.443 56.041 119.051 1.00 33.52 C ANISOU 3123 CD2 PHE A 326 4042 3999 4696 -49 458 587 C ATOM 3124 CE1 PHE A 326 19.163 55.064 116.815 1.00 44.91 C ANISOU 3124 CE1 PHE A 326 5641 5557 5866 71 633 628 C ATOM 3125 CE2 PHE A 326 21.123 55.219 118.173 1.00 38.52 C ANISOU 3125 CE2 PHE A 326 4633 4646 5357 -41 584 651 C ATOM 3126 CZ PHE A 326 20.487 54.735 117.054 1.00 43.00 C ANISOU 3126 CZ PHE A 326 5294 5268 5777 26 678 667 C ATOM 3127 N CYS A 327 19.337 56.095 122.556 1.00 32.38 N ANISOU 3127 N CYS A 327 3963 3887 4455 -30 108 377 N ATOM 3128 CA CYS A 327 20.350 55.324 123.264 1.00 32.31 C ANISOU 3128 CA CYS A 327 3862 3864 4550 -86 50 364 C ATOM 3129 C CYS A 327 19.722 54.288 124.184 1.00 28.79 C ANISOU 3129 C CYS A 327 3427 3516 3995 -39 3 302 C ATOM 3130 O CYS A 327 20.174 53.139 124.220 1.00 31.43 O ANISOU 3130 O CYS A 327 3682 3903 4358 -61 26 307 O ATOM 3131 CB CYS A 327 21.261 56.260 124.052 1.00 38.75 C ANISOU 3131 CB CYS A 327 4677 4539 5506 -149 -81 355 C ATOM 3132 SG CYS A 327 22.410 57.155 122.979 1.00 50.98 S ANISOU 3132 SG CYS A 327 6139 5965 7266 -234 -14 469 S ATOM 3133 N LEU A 328 18.678 54.666 124.925 1.00 26.13 N ANISOU 3133 N LEU A 328 3190 3201 3535 36 -50 256 N ATOM 3134 CA LEU A 328 18.005 53.693 125.785 1.00 33.08 C ANISOU 3134 CA LEU A 328 4076 4174 4317 95 -73 221 C ATOM 3135 C LEU A 328 17.432 52.537 124.977 1.00 35.74 C ANISOU 3135 C LEU A 328 4350 4627 4604 100 19 255 C ATOM 3136 O LEU A 328 17.492 51.382 125.407 1.00 31.67 O ANISOU 3136 O LEU A 328 3782 4172 4079 98 12 243 O ATOM 3137 CB LEU A 328 16.895 54.362 126.594 1.00 30.12 C ANISOU 3137 CB LEU A 328 3822 3804 3819 201 -106 197 C ATOM 3138 CG LEU A 328 17.413 55.349 127.638 1.00 34.81 C ANISOU 3138 CG LEU A 328 4529 4269 4427 216 -228 143 C ATOM 3139 CD1 LEU A 328 16.260 56.088 128.322 1.00 33.08 C ANISOU 3139 CD1 LEU A 328 4463 4044 4062 353 -229 130 C ATOM 3140 CD2 LEU A 328 18.282 54.626 128.652 1.00 37.31 C ANISOU 3140 CD2 LEU A 328 4821 4563 4791 184 -328 99 C ATOM 3141 N VAL A 329 16.862 52.825 123.808 1.00 32.52 N ANISOU 3141 N VAL A 329 3958 4239 4157 108 92 298 N ATOM 3142 CA VAL A 329 16.239 51.763 123.036 1.00 30.06 C ANISOU 3142 CA VAL A 329 3619 4016 3787 113 143 326 C ATOM 3143 C VAL A 329 17.304 50.872 122.414 1.00 35.49 C ANISOU 3143 C VAL A 329 4253 4692 4539 55 192 336 C ATOM 3144 O VAL A 329 17.198 49.639 122.442 1.00 31.11 O ANISOU 3144 O VAL A 329 3668 4194 3958 50 195 331 O ATOM 3145 CB VAL A 329 15.284 52.371 121.999 1.00 34.80 C ANISOU 3145 CB VAL A 329 4274 4631 4318 146 181 369 C ATOM 3146 CG1 VAL A 329 14.833 51.336 120.981 1.00 31.93 C ANISOU 3146 CG1 VAL A 329 3908 4323 3901 135 206 397 C ATOM 3147 CG2 VAL A 329 14.093 52.953 122.740 1.00 28.98 C ANISOU 3147 CG2 VAL A 329 3569 3926 3514 224 145 377 C ATOM 3148 N LEU A 330 18.375 51.477 121.902 1.00 30.77 N ANISOU 3148 N LEU A 330 3639 4013 4037 17 237 362 N ATOM 3149 CA LEU A 330 19.418 50.691 121.262 1.00 31.94 C ANISOU 3149 CA LEU A 330 3736 4145 4253 -15 315 397 C ATOM 3150 C LEU A 330 20.105 49.762 122.260 1.00 32.48 C ANISOU 3150 C LEU A 330 3723 4231 4386 -41 268 370 C ATOM 3151 O LEU A 330 20.324 48.582 121.954 1.00 30.44 O ANISOU 3151 O LEU A 330 3446 4011 4110 -37 316 378 O ATOM 3152 CB LEU A 330 20.426 51.615 120.591 1.00 31.96 C ANISOU 3152 CB LEU A 330 3716 4054 4374 -42 386 460 C ATOM 3153 CG LEU A 330 21.687 50.972 120.028 1.00 38.22 C ANISOU 3153 CG LEU A 330 4435 4815 5273 -59 492 527 C ATOM 3154 CD1 LEU A 330 21.331 50.009 118.918 1.00 35.37 C ANISOU 3154 CD1 LEU A 330 4154 4498 4786 -3 595 545 C ATOM 3155 CD2 LEU A 330 22.640 52.053 119.523 1.00 37.69 C ANISOU 3155 CD2 LEU A 330 4319 4645 5358 -87 557 616 C ATOM 3156 N VAL A 331 20.418 50.262 123.467 1.00 29.81 N ANISOU 3156 N VAL A 331 3358 3858 4111 -60 165 335 N ATOM 3157 CA VAL A 331 21.081 49.412 124.447 1.00 34.32 C ANISOU 3157 CA VAL A 331 3860 4440 4738 -80 106 310 C ATOM 3158 C VAL A 331 20.143 48.309 124.925 1.00 32.55 C ANISOU 3158 C VAL A 331 3659 4315 4393 -36 92 272 C ATOM 3159 O VAL A 331 20.599 47.201 125.213 1.00 30.47 O ANISOU 3159 O VAL A 331 3342 4082 4153 -45 98 270 O ATOM 3160 CB VAL A 331 21.634 50.222 125.635 1.00 37.43 C ANISOU 3160 CB VAL A 331 4252 4757 5215 -107 -30 278 C ATOM 3161 CG1 VAL A 331 22.623 51.284 125.153 1.00 37.02 C ANISOU 3161 CG1 VAL A 331 4155 4591 5320 -170 -32 334 C ATOM 3162 CG2 VAL A 331 20.515 50.840 126.449 1.00 51.39 C ANISOU 3162 CG2 VAL A 331 6135 6536 6855 -43 -106 220 C ATOM 3163 N PHE A 332 18.836 48.589 125.031 1.00 28.18 N ANISOU 3163 N PHE A 332 3174 3808 3724 14 76 257 N ATOM 3164 CA PHE A 332 17.871 47.536 125.339 1.00 30.96 C ANISOU 3164 CA PHE A 332 3527 4249 3989 51 72 252 C ATOM 3165 C PHE A 332 17.929 46.421 124.302 1.00 32.71 C ANISOU 3165 C PHE A 332 3733 4500 4197 26 136 276 C ATOM 3166 O PHE A 332 18.011 45.231 124.646 1.00 29.49 O ANISOU 3166 O PHE A 332 3291 4129 3784 22 130 269 O ATOM 3167 CB PHE A 332 16.456 48.119 125.416 1.00 27.88 C ANISOU 3167 CB PHE A 332 3189 3897 3506 111 61 267 C ATOM 3168 CG PHE A 332 15.376 47.066 125.431 1.00 32.84 C ANISOU 3168 CG PHE A 332 3792 4608 4076 134 63 297 C ATOM 3169 CD1 PHE A 332 15.101 46.350 126.590 1.00 32.37 C ANISOU 3169 CD1 PHE A 332 3702 4593 4003 171 36 294 C ATOM 3170 CD2 PHE A 332 14.669 46.765 124.279 1.00 35.79 C ANISOU 3170 CD2 PHE A 332 4177 5007 4415 117 81 337 C ATOM 3171 CE1 PHE A 332 14.123 45.365 126.601 1.00 35.24 C ANISOU 3171 CE1 PHE A 332 4024 5025 4342 184 37 342 C ATOM 3172 CE2 PHE A 332 13.685 45.771 124.281 1.00 35.66 C ANISOU 3172 CE2 PHE A 332 4127 5050 4372 121 53 376 C ATOM 3173 CZ PHE A 332 13.414 45.079 125.446 1.00 29.17 C ANISOU 3173 CZ PHE A 332 3252 4272 3559 150 36 385 C ATOM 3174 N ALA A 333 17.886 46.794 123.021 1.00 31.51 N ANISOU 3174 N ALA A 333 3626 4321 4025 18 195 306 N ATOM 3175 CA ALA A 333 17.857 45.807 121.949 1.00 31.36 C ANISOU 3175 CA ALA A 333 3646 4310 3959 14 246 325 C ATOM 3176 C ALA A 333 19.105 44.935 121.966 1.00 34.63 C ANISOU 3176 C ALA A 333 4018 4699 4439 -1 301 328 C ATOM 3177 O ALA A 333 19.018 43.708 121.844 1.00 32.62 O ANISOU 3177 O ALA A 333 3780 4467 4145 2 306 322 O ATOM 3178 CB ALA A 333 17.717 46.502 120.593 1.00 28.50 C ANISOU 3178 CB ALA A 333 3369 3908 3554 27 304 358 C ATOM 3179 N LEU A 334 20.280 45.558 122.099 1.00 31.26 N ANISOU 3179 N LEU A 334 3532 4219 4126 -18 341 350 N ATOM 3180 CA LEU A 334 21.532 44.817 122.032 1.00 35.84 C ANISOU 3180 CA LEU A 334 4051 4772 4793 -24 410 382 C ATOM 3181 C LEU A 334 21.721 43.935 123.260 1.00 38.54 C ANISOU 3181 C LEU A 334 4323 5154 5165 -36 338 346 C ATOM 3182 O LEU A 334 22.241 42.822 123.152 1.00 34.00 O ANISOU 3182 O LEU A 334 3733 4587 4600 -24 387 360 O ATOM 3183 CB LEU A 334 22.711 45.778 121.885 1.00 33.91 C ANISOU 3183 CB LEU A 334 3731 4454 4700 -47 459 442 C ATOM 3184 CG LEU A 334 22.788 46.604 120.594 1.00 41.30 C ANISOU 3184 CG LEU A 334 4725 5339 5629 -25 566 503 C ATOM 3185 CD1 LEU A 334 23.893 47.661 120.696 1.00 38.16 C ANISOU 3185 CD1 LEU A 334 4222 4861 5417 -65 587 574 C ATOM 3186 CD2 LEU A 334 22.990 45.718 119.365 1.00 39.50 C ANISOU 3186 CD2 LEU A 334 4583 5103 5323 37 707 547 C ATOM 3187 N CYS A 335 21.317 44.419 124.434 1.00 27.87 N ANISOU 3187 N CYS A 335 2949 3822 3819 -45 229 304 N ATOM 3188 CA CYS A 335 21.560 43.678 125.662 1.00 28.31 C ANISOU 3188 CA CYS A 335 2952 3907 3897 -44 160 274 C ATOM 3189 C CYS A 335 20.651 42.465 125.788 1.00 28.47 C ANISOU 3189 C CYS A 335 3006 3996 3817 -19 159 256 C ATOM 3190 O CYS A 335 21.060 41.447 126.354 1.00 29.06 O ANISOU 3190 O CYS A 335 3039 4090 3911 -16 152 250 O ATOM 3191 CB CYS A 335 21.347 44.582 126.874 1.00 26.77 C ANISOU 3191 CB CYS A 335 2766 3698 3708 -38 44 235 C ATOM 3192 SG CYS A 335 22.736 45.705 127.170 1.00 36.14 S ANISOU 3192 SG CYS A 335 3892 4777 5061 -92 -20 254 S ATOM 3193 N TRP A 336 19.411 42.572 125.316 1.00 25.04 N ANISOU 3193 N TRP A 336 2634 3593 3287 -4 155 256 N ATOM 3194 CA TRP A 336 18.446 41.504 125.507 1.00 25.55 C ANISOU 3194 CA TRP A 336 2712 3712 3284 8 130 257 C ATOM 3195 C TRP A 336 18.414 40.527 124.346 1.00 33.09 C ANISOU 3195 C TRP A 336 3723 4650 4198 -7 173 271 C ATOM 3196 O TRP A 336 17.857 39.439 124.492 1.00 30.53 O ANISOU 3196 O TRP A 336 3408 4350 3842 -11 142 274 O ATOM 3197 CB TRP A 336 17.046 42.080 125.717 1.00 22.64 C ANISOU 3197 CB TRP A 336 2364 3383 2857 32 85 272 C ATOM 3198 CG TRP A 336 16.864 42.560 127.091 1.00 27.99 C ANISOU 3198 CG TRP A 336 3017 4081 3537 77 44 260 C ATOM 3199 CD1 TRP A 336 17.107 43.815 127.559 1.00 28.43 C ANISOU 3199 CD1 TRP A 336 3099 4103 3601 101 22 239 C ATOM 3200 CD2 TRP A 336 16.461 41.773 128.213 1.00 30.39 C ANISOU 3200 CD2 TRP A 336 3290 4432 3826 115 21 269 C ATOM 3201 NE1 TRP A 336 16.844 43.867 128.909 1.00 34.19 N ANISOU 3201 NE1 TRP A 336 3838 4850 4302 163 -19 228 N ATOM 3202 CE2 TRP A 336 16.443 42.626 129.333 1.00 29.84 C ANISOU 3202 CE2 TRP A 336 3248 4355 3737 178 -9 251 C ATOM 3203 CE3 TRP A 336 16.098 40.424 128.376 1.00 28.69 C ANISOU 3203 CE3 TRP A 336 3039 4254 3608 108 23 295 C ATOM 3204 CZ2 TRP A 336 16.077 42.179 130.609 1.00 30.63 C ANISOU 3204 CZ2 TRP A 336 3348 4488 3801 249 -23 262 C ATOM 3205 CZ3 TRP A 336 15.724 39.986 129.635 1.00 32.88 C ANISOU 3205 CZ3 TRP A 336 3544 4823 4125 165 12 313 C ATOM 3206 CH2 TRP A 336 15.718 40.858 130.735 1.00 27.22 C ANISOU 3206 CH2 TRP A 336 2862 4105 3377 242 -3 299 C ATOM 3207 N LEU A 337 18.969 40.891 123.193 1.00 29.59 N ANISOU 3207 N LEU A 337 3336 4155 3751 -6 243 285 N ATOM 3208 CA LEU A 337 18.930 39.966 122.066 1.00 33.16 C ANISOU 3208 CA LEU A 337 3892 4573 4133 3 281 294 C ATOM 3209 C LEU A 337 19.601 38.633 122.389 1.00 36.31 C ANISOU 3209 C LEU A 337 4279 4967 4551 10 309 289 C ATOM 3210 O LEU A 337 19.013 37.586 122.066 1.00 29.26 O ANISOU 3210 O LEU A 337 3462 4064 3590 6 270 280 O ATOM 3211 CB LEU A 337 19.545 40.620 120.826 1.00 31.98 C ANISOU 3211 CB LEU A 337 3821 4363 3967 30 380 322 C ATOM 3212 CG LEU A 337 19.558 39.689 119.606 1.00 43.65 C ANISOU 3212 CG LEU A 337 5458 5786 5341 67 427 328 C ATOM 3213 CD1 LEU A 337 18.153 39.536 119.034 1.00 43.39 C ANISOU 3213 CD1 LEU A 337 5534 5752 5199 49 311 312 C ATOM 3214 CD2 LEU A 337 20.532 40.148 118.549 1.00 48.53 C ANISOU 3214 CD2 LEU A 337 6146 6339 5955 126 574 375 C ATOM 3215 N PRO A 338 20.794 38.585 123.013 1.00 31.58 N ANISOU 3215 N PRO A 338 3587 4364 4047 19 362 299 N ATOM 3216 CA PRO A 338 21.456 37.280 123.191 1.00 30.29 C ANISOU 3216 CA PRO A 338 3421 4191 3898 38 403 303 C ATOM 3217 C PRO A 338 20.642 36.267 123.985 1.00 31.93 C ANISOU 3217 C PRO A 338 3621 4440 4069 20 314 276 C ATOM 3218 O PRO A 338 20.649 35.078 123.643 1.00 35.14 O ANISOU 3218 O PRO A 338 4099 4820 4432 32 329 274 O ATOM 3219 CB PRO A 338 22.763 37.653 123.907 1.00 29.31 C ANISOU 3219 CB PRO A 338 3163 4064 3910 40 441 331 C ATOM 3220 CG PRO A 338 23.070 39.071 123.382 1.00 27.25 C ANISOU 3220 CG PRO A 338 2884 3770 3699 31 475 360 C ATOM 3221 CD PRO A 338 21.697 39.705 123.361 1.00 28.13 C ANISOU 3221 CD PRO A 338 3057 3912 3720 11 389 320 C ATOM 3222 N LEU A 339 19.951 36.686 125.042 1.00 25.99 N ANISOU 3222 N LEU A 339 2795 3745 3337 2 231 263 N ATOM 3223 CA LEU A 339 19.194 35.712 125.825 1.00 33.75 C ANISOU 3223 CA LEU A 339 3758 4766 4301 -4 168 261 C ATOM 3224 C LEU A 339 18.017 35.154 125.028 1.00 37.92 C ANISOU 3224 C LEU A 339 4370 5276 4760 -31 116 275 C ATOM 3225 O LEU A 339 17.720 33.952 125.108 1.00 32.49 O ANISOU 3225 O LEU A 339 3708 4576 4061 -44 85 282 O ATOM 3226 CB LEU A 339 18.726 36.337 127.136 1.00 26.38 C ANISOU 3226 CB LEU A 339 2744 3889 3391 10 114 261 C ATOM 3227 CG LEU A 339 17.812 35.516 128.033 1.00 31.19 C ANISOU 3227 CG LEU A 339 3320 4543 3988 21 69 285 C ATOM 3228 CD1 LEU A 339 18.524 34.188 128.407 1.00 28.93 C ANISOU 3228 CD1 LEU A 339 3021 4248 3725 25 90 280 C ATOM 3229 CD2 LEU A 339 17.470 36.331 129.270 1.00 28.26 C ANISOU 3229 CD2 LEU A 339 2904 4216 3618 69 43 290 C ATOM 3230 N HIS A 340 17.344 35.998 124.238 1.00 27.85 N ANISOU 3230 N HIS A 340 3145 3991 3447 -43 91 283 N ATOM 3231 CA HIS A 340 16.241 35.494 123.417 1.00 31.01 C ANISOU 3231 CA HIS A 340 3629 4362 3792 -76 9 302 C ATOM 3232 C HIS A 340 16.741 34.546 122.328 1.00 30.75 C ANISOU 3232 C HIS A 340 3750 4243 3693 -71 28 281 C ATOM 3233 O HIS A 340 16.121 33.502 122.071 1.00 31.00 O ANISOU 3233 O HIS A 340 3849 4234 3697 -103 -58 287 O ATOM 3234 CB HIS A 340 15.465 36.658 122.799 1.00 32.29 C ANISOU 3234 CB HIS A 340 3813 4530 3927 -82 -26 320 C ATOM 3235 CG HIS A 340 14.683 37.451 123.801 1.00 32.91 C ANISOU 3235 CG HIS A 340 3771 4682 4053 -72 -53 355 C ATOM 3236 ND1 HIS A 340 13.487 37.011 124.326 1.00 32.49 N ANISOU 3236 ND1 HIS A 340 3649 4665 4031 -88 -128 415 N ATOM 3237 CD2 HIS A 340 14.936 38.643 124.391 1.00 30.64 C ANISOU 3237 CD2 HIS A 340 3430 4426 3785 -37 -9 347 C ATOM 3238 CE1 HIS A 340 13.032 37.901 125.190 1.00 36.35 C ANISOU 3238 CE1 HIS A 340 4053 5211 4545 -46 -108 447 C ATOM 3239 NE2 HIS A 340 13.894 38.900 125.250 1.00 34.35 N ANISOU 3239 NE2 HIS A 340 3823 4952 4276 -15 -46 396 N ATOM 3240 N LEU A 341 17.845 34.902 121.662 1.00 27.37 N ANISOU 3240 N LEU A 341 3386 3775 3239 -25 140 265 N ATOM 3241 CA LEU A 341 18.418 34.009 120.665 1.00 28.01 C ANISOU 3241 CA LEU A 341 3637 3767 3240 14 191 253 C ATOM 3242 C LEU A 341 18.808 32.669 121.283 1.00 30.43 C ANISOU 3242 C LEU A 341 3930 4063 3569 18 196 246 C ATOM 3243 O LEU A 341 18.655 31.625 120.644 1.00 33.12 O ANISOU 3243 O LEU A 341 4428 4324 3832 27 161 232 O ATOM 3244 CB LEU A 341 19.635 34.649 120.003 1.00 31.94 C ANISOU 3244 CB LEU A 341 4170 4232 3733 84 349 269 C ATOM 3245 CG LEU A 341 19.341 35.854 119.101 1.00 48.99 C ANISOU 3245 CG LEU A 341 6394 6375 5846 96 363 281 C ATOM 3246 CD1 LEU A 341 20.607 36.331 118.418 1.00 53.46 C ANISOU 3246 CD1 LEU A 341 6993 6897 6421 175 542 320 C ATOM 3247 CD2 LEU A 341 18.280 35.513 118.076 1.00 49.95 C ANISOU 3247 CD2 LEU A 341 6706 6435 5836 87 252 263 C ATOM 3248 N ALA A 342 19.315 32.681 122.523 1.00 31.36 N ANISOU 3248 N ALA A 342 3879 4251 3787 16 229 253 N ATOM 3249 CA ALA A 342 19.684 31.428 123.180 1.00 33.43 C ANISOU 3249 CA ALA A 342 4121 4508 4074 24 235 251 C ATOM 3250 C ALA A 342 18.477 30.509 123.317 1.00 34.96 C ANISOU 3250 C ALA A 342 4355 4684 4244 -32 103 253 C ATOM 3251 O ALA A 342 18.546 29.316 122.985 1.00 32.88 O ANISOU 3251 O ALA A 342 4205 4349 3938 -27 86 245 O ATOM 3252 CB ALA A 342 20.319 31.708 124.551 1.00 25.00 C ANISOU 3252 CB ALA A 342 2871 3518 3110 31 266 261 C ATOM 3253 N ARG A 343 17.354 31.053 123.797 1.00 29.83 N ANISOU 3253 N ARG A 343 3614 4091 3630 -82 9 277 N ATOM 3254 CA ARG A 343 16.162 30.237 124.009 1.00 30.64 C ANISOU 3254 CA ARG A 343 3709 4179 3752 -141 -118 312 C ATOM 3255 C ARG A 343 15.526 29.818 122.685 1.00 37.13 C ANISOU 3255 C ARG A 343 4713 4897 4499 -180 -225 305 C ATOM 3256 O ARG A 343 15.003 28.698 122.575 1.00 35.77 O ANISOU 3256 O ARG A 343 4604 4658 4330 -226 -328 319 O ATOM 3257 CB ARG A 343 15.159 30.986 124.899 1.00 34.01 C ANISOU 3257 CB ARG A 343 3976 4696 4251 -162 -163 366 C ATOM 3258 CG ARG A 343 15.503 30.984 126.421 1.00 37.33 C ANISOU 3258 CG ARG A 343 4251 5198 4733 -121 -99 383 C ATOM 3259 CD ARG A 343 15.196 29.613 127.022 1.00 33.80 C ANISOU 3259 CD ARG A 343 3778 4737 4329 -141 -134 421 C ATOM 3260 NE ARG A 343 15.200 29.553 128.483 1.00 35.46 N ANISOU 3260 NE ARG A 343 3863 5022 4588 -95 -90 456 N ATOM 3261 CZ ARG A 343 16.185 29.033 129.222 1.00 33.54 C ANISOU 3261 CZ ARG A 343 3604 4791 4348 -51 -28 428 C ATOM 3262 NH1 ARG A 343 17.270 28.536 128.641 1.00 34.71 N ANISOU 3262 NH1 ARG A 343 3834 4887 4468 -45 12 373 N ATOM 3263 NH2 ARG A 343 16.089 29.012 130.548 1.00 33.50 N ANISOU 3263 NH2 ARG A 343 3509 4848 4371 1 -1 463 N ATOM 3264 N ILE A 344 15.595 30.681 121.667 1.00 31.16 N ANISOU 3264 N ILE A 344 4057 4113 3670 -160 -212 283 N ATOM 3265 CA ILE A 344 15.068 30.346 120.343 1.00 32.05 C ANISOU 3265 CA ILE A 344 4381 4112 3683 -181 -324 269 C ATOM 3266 C ILE A 344 15.900 29.256 119.677 1.00 32.47 C ANISOU 3266 C ILE A 344 4648 4052 3637 -129 -280 224 C ATOM 3267 O ILE A 344 15.367 28.420 118.933 1.00 35.23 O ANISOU 3267 O ILE A 344 5186 4284 3915 -158 -418 210 O ATOM 3268 CB ILE A 344 15.014 31.605 119.453 1.00 34.44 C ANISOU 3268 CB ILE A 344 4748 4417 3922 -152 -300 261 C ATOM 3269 CG1 ILE A 344 14.008 32.626 119.997 1.00 48.47 C ANISOU 3269 CG1 ILE A 344 6346 6288 5784 -198 -362 312 C ATOM 3270 CG2 ILE A 344 14.697 31.233 118.001 1.00 32.34 C ANISOU 3270 CG2 ILE A 344 4753 4016 3516 -145 -402 235 C ATOM 3271 CD1 ILE A 344 12.719 32.021 120.486 1.00 51.51 C ANISOU 3271 CD1 ILE A 344 6635 6680 6256 -282 -525 376 C ATOM 3272 N LEU A 345 17.227 29.291 119.864 1.00 34.35 N ANISOU 3272 N LEU A 345 4874 4311 3868 -44 -94 206 N ATOM 3273 CA LEU A 345 18.084 28.276 119.254 1.00 35.19 C ANISOU 3273 CA LEU A 345 5181 4311 3878 33 -18 179 C ATOM 3274 C LEU A 345 17.775 26.891 119.801 1.00 37.60 C ANISOU 3274 C LEU A 345 5503 4572 4212 -11 -110 177 C ATOM 3275 O LEU A 345 17.770 25.908 119.050 1.00 37.38 O ANISOU 3275 O LEU A 345 5714 4410 4079 13 -164 149 O ATOM 3276 CB LEU A 345 19.555 28.611 119.480 1.00 37.28 C ANISOU 3276 CB LEU A 345 5374 4619 4173 131 205 194 C ATOM 3277 CG LEU A 345 20.142 29.722 118.600 1.00 44.28 C ANISOU 3277 CG LEU A 345 6316 5498 5011 204 331 209 C ATOM 3278 CD1 LEU A 345 21.535 30.082 119.082 1.00 48.66 C ANISOU 3278 CD1 LEU A 345 6720 6107 5662 272 527 252 C ATOM 3279 CD2 LEU A 345 20.185 29.279 117.147 1.00 50.89 C ANISOU 3279 CD2 LEU A 345 7474 6194 5667 288 347 190 C ATOM 3280 N LYS A 346 17.530 26.787 121.111 1.00 29.37 N ANISOU 3280 N LYS A 346 4227 3629 3303 -65 -127 208 N ATOM 3281 CA LYS A 346 17.125 25.501 121.670 1.00 36.42 C ANISOU 3281 CA LYS A 346 5119 4480 4238 -114 -218 221 C ATOM 3282 C LYS A 346 15.808 25.041 121.058 1.00 41.59 C ANISOU 3282 C LYS A 346 5887 5038 4877 -210 -441 233 C ATOM 3283 O LYS A 346 15.686 23.896 120.612 1.00 41.62 O ANISOU 3283 O LYS A 346 6074 4909 4829 -226 -534 215 O ATOM 3284 CB LYS A 346 17.008 25.582 123.191 1.00 36.18 C ANISOU 3284 CB LYS A 346 4824 4577 4347 -142 -190 265 C ATOM 3285 CG LYS A 346 16.449 24.295 123.807 1.00 38.41 C ANISOU 3285 CG LYS A 346 5087 4819 4690 -197 -284 299 C ATOM 3286 CD LYS A 346 15.906 24.522 125.207 1.00 55.92 C ANISOU 3286 CD LYS A 346 7056 7157 7035 -227 -284 365 C ATOM 3287 CE LYS A 346 14.764 23.554 125.515 1.00 65.38 C ANISOU 3287 CE LYS A 346 8221 8305 8317 -314 -429 436 C ATOM 3288 NZ LYS A 346 15.086 22.165 125.073 1.00 62.47 N ANISOU 3288 NZ LYS A 346 8029 7801 7906 -324 -474 407 N ATOM 3289 N LEU A 347 14.814 25.935 121.009 1.00 39.14 N ANISOU 3289 N LEU A 347 5475 4780 4617 -274 -540 270 N ATOM 3290 CA LEU A 347 13.523 25.585 120.416 1.00 36.69 C ANISOU 3290 CA LEU A 347 5243 4377 4321 -375 -776 303 C ATOM 3291 C LEU A 347 13.680 25.066 118.995 1.00 42.39 C ANISOU 3291 C LEU A 347 6304 4924 4876 -351 -867 238 C ATOM 3292 O LEU A 347 12.989 24.121 118.593 1.00 48.81 O ANISOU 3292 O LEU A 347 7256 5603 5687 -426 -1070 244 O ATOM 3293 CB LEU A 347 12.593 26.802 120.410 1.00 39.88 C ANISOU 3293 CB LEU A 347 5499 4864 4787 -420 -838 357 C ATOM 3294 CG LEU A 347 11.702 27.058 121.623 1.00 43.91 C ANISOU 3294 CG LEU A 347 5719 5492 5473 -476 -860 461 C ATOM 3295 CD1 LEU A 347 11.058 28.428 121.500 1.00 45.20 C ANISOU 3295 CD1 LEU A 347 5775 5739 5662 -477 -867 501 C ATOM 3296 CD2 LEU A 347 10.636 25.975 121.731 1.00 46.23 C ANISOU 3296 CD2 LEU A 347 5986 5702 5876 -585 -1060 542 C ATOM 3297 N THR A 348 14.583 25.665 118.217 1.00 37.88 N ANISOU 3297 N THR A 348 5886 4341 4167 -241 -723 181 N ATOM 3298 CA THR A 348 14.640 25.351 116.797 1.00 42.54 C ANISOU 3298 CA THR A 348 6829 4763 4572 -192 -803 126 C ATOM 3299 C THR A 348 15.668 24.279 116.454 1.00 41.75 C ANISOU 3299 C THR A 348 6969 4548 4348 -86 -697 75 C ATOM 3300 O THR A 348 15.515 23.607 115.432 1.00 42.02 O ANISOU 3300 O THR A 348 7333 4403 4228 -58 -818 30 O ATOM 3301 CB THR A 348 14.929 26.616 115.987 1.00 44.67 C ANISOU 3301 CB THR A 348 7164 5064 4744 -115 -706 111 C ATOM 3302 OG1 THR A 348 16.165 27.203 116.420 1.00 41.57 O ANISOU 3302 OG1 THR A 348 6647 4777 4370 -14 -431 114 O ATOM 3303 CG2 THR A 348 13.800 27.631 116.160 1.00 42.89 C ANISOU 3303 CG2 THR A 348 6749 4927 4620 -213 -835 161 C ATOM 3304 N LEU A 349 16.707 24.091 117.277 1.00 38.03 N ANISOU 3304 N LEU A 349 6355 4162 3934 -19 -483 84 N ATOM 3305 CA LEU A 349 17.795 23.184 116.931 1.00 42.79 C ANISOU 3305 CA LEU A 349 7170 4666 4422 109 -341 53 C ATOM 3306 C LEU A 349 17.831 21.899 117.741 1.00 43.55 C ANISOU 3306 C LEU A 349 7228 4729 4590 71 -380 58 C ATOM 3307 O LEU A 349 18.492 20.948 117.316 1.00 41.26 O ANISOU 3307 O LEU A 349 7175 4316 4186 168 -317 28 O ATOM 3308 CB LEU A 349 19.154 23.878 117.089 1.00 42.32 C ANISOU 3308 CB LEU A 349 7003 4706 4369 240 -47 75 C ATOM 3309 CG LEU A 349 19.432 25.075 116.183 1.00 49.90 C ANISOU 3309 CG LEU A 349 8034 5679 5247 316 53 81 C ATOM 3310 CD1 LEU A 349 20.841 25.585 116.425 1.00 45.80 C ANISOU 3310 CD1 LEU A 349 7385 5242 4777 435 337 129 C ATOM 3311 CD2 LEU A 349 19.230 24.674 114.727 1.00 52.23 C ANISOU 3311 CD2 LEU A 349 8742 5787 5317 397 -17 38 C ATOM 3312 N TYR A 350 17.164 21.844 118.889 1.00 41.51 N ANISOU 3312 N TYR A 350 6690 4573 4509 -51 -467 102 N ATOM 3313 CA TYR A 350 17.327 20.711 119.792 1.00 43.50 C ANISOU 3313 CA TYR A 350 6871 4816 4843 -72 -463 120 C ATOM 3314 C TYR A 350 16.475 19.525 119.344 1.00 44.24 C ANISOU 3314 C TYR A 350 7179 4727 4905 -155 -701 108 C ATOM 3315 O TYR A 350 15.258 19.649 119.176 1.00 44.00 O ANISOU 3315 O TYR A 350 7120 4661 4937 -284 -928 136 O ATOM 3316 CB TYR A 350 16.980 21.119 121.223 1.00 37.61 C ANISOU 3316 CB TYR A 350 5758 4244 4286 -147 -443 184 C ATOM 3317 CG TYR A 350 17.104 19.981 122.208 1.00 39.03 C ANISOU 3317 CG TYR A 350 5857 4420 4552 -165 -436 212 C ATOM 3318 CD1 TYR A 350 18.355 19.511 122.604 1.00 30.67 C ANISOU 3318 CD1 TYR A 350 4803 3382 3469 -55 -248 198 C ATOM 3319 CD2 TYR A 350 15.968 19.358 122.722 1.00 34.64 C ANISOU 3319 CD2 TYR A 350 5214 3835 4113 -289 -615 269 C ATOM 3320 CE1 TYR A 350 18.465 18.449 123.508 1.00 31.13 C ANISOU 3320 CE1 TYR A 350 4794 3434 3600 -65 -242 226 C ATOM 3321 CE2 TYR A 350 16.070 18.318 123.621 1.00 37.92 C ANISOU 3321 CE2 TYR A 350 5557 4242 4607 -301 -600 305 C ATOM 3322 CZ TYR A 350 17.318 17.864 124.008 1.00 34.32 C ANISOU 3322 CZ TYR A 350 5123 3809 4108 -187 -415 276 C ATOM 3323 OH TYR A 350 17.397 16.816 124.895 1.00 37.54 O ANISOU 3323 OH TYR A 350 5468 4206 4591 -196 -404 313 O ATOM 3324 N ASN A 351 17.124 18.374 119.146 1.00 42.38 N ANISOU 3324 N ASN A 351 7158 4365 4580 -81 -657 74 N ATOM 3325 CA ASN A 351 16.474 17.126 118.733 1.00 40.10 C ANISOU 3325 CA ASN A 351 7111 3873 4254 -150 -883 54 C ATOM 3326 C ASN A 351 16.719 16.105 119.831 1.00 38.06 C ANISOU 3326 C ASN A 351 6717 3633 4111 -169 -834 91 C ATOM 3327 O ASN A 351 17.828 15.568 119.949 1.00 37.33 O ANISOU 3327 O ASN A 351 6711 3526 3946 -38 -643 68 O ATOM 3328 CB ASN A 351 17.015 16.650 117.384 1.00 43.85 C ANISOU 3328 CB ASN A 351 8036 4144 4480 -20 -878 -26 C ATOM 3329 CG ASN A 351 16.493 15.266 116.961 1.00 51.96 C ANISOU 3329 CG ASN A 351 9367 4929 5447 -75 -1115 -59 C ATOM 3330 OD1 ASN A 351 15.760 14.579 117.687 1.00 50.05 O ANISOU 3330 OD1 ASN A 351 8983 4667 5369 -219 -1280 -12 O ATOM 3331 ND2 ASN A 351 16.884 14.858 115.760 1.00 54.61 N ANISOU 3331 ND2 ASN A 351 10141 5067 5540 50 -1131 -134 N ATOM 3332 N GLN A 352 15.676 15.830 120.618 1.00 40.56 N ANISOU 3332 N GLN A 352 6821 3978 4612 -324 -1000 162 N ATOM 3333 CA GLN A 352 15.783 14.951 121.772 1.00 43.14 C ANISOU 3333 CA GLN A 352 6983 4339 5067 -349 -954 216 C ATOM 3334 C GLN A 352 16.143 13.514 121.397 1.00 43.57 C ANISOU 3334 C GLN A 352 7334 4190 5031 -313 -1004 174 C ATOM 3335 O GLN A 352 16.529 12.748 122.285 1.00 42.20 O ANISOU 3335 O GLN A 352 7062 4042 4931 -293 -914 207 O ATOM 3336 CB GLN A 352 14.473 14.970 122.573 1.00 41.22 C ANISOU 3336 CB GLN A 352 6467 4150 5044 -516 -1123 325 C ATOM 3337 CG GLN A 352 13.248 14.430 121.836 1.00 49.24 C ANISOU 3337 CG GLN A 352 7631 4976 6103 -667 -1446 352 C ATOM 3338 CD GLN A 352 11.989 14.446 122.698 1.00 51.20 C ANISOU 3338 CD GLN A 352 7563 5287 6605 -821 -1582 498 C ATOM 3339 OE1 GLN A 352 11.754 15.386 123.453 1.00 55.99 O ANISOU 3339 OE1 GLN A 352 7874 6087 7312 -815 -1469 566 O ATOM 3340 NE2 GLN A 352 11.180 13.400 122.589 1.00 41.51 N ANISOU 3340 NE2 GLN A 352 6402 3885 5486 -951 -1821 559 N ATOM 3341 N ASN A 353 16.040 13.135 120.123 1.00 40.40 N ANISOU 3341 N ASN A 353 7311 3580 4461 -293 -1144 102 N ATOM 3342 CA ASN A 353 16.399 11.787 119.690 1.00 53.54 C ANISOU 3342 CA ASN A 353 9310 5023 6009 -240 -1195 53 C ATOM 3343 C ASN A 353 17.869 11.655 119.298 1.00 52.50 C ANISOU 3343 C ASN A 353 9383 4881 5685 -11 -912 -7 C ATOM 3344 O ASN A 353 18.320 10.547 119.011 1.00 48.14 O ANISOU 3344 O ASN A 353 9110 4158 5023 69 -902 -43 O ATOM 3345 CB ASN A 353 15.510 11.360 118.511 1.00 52.23 C ANISOU 3345 CB ASN A 353 9497 4604 5745 -326 -1520 6 C ATOM 3346 CG ASN A 353 14.042 11.261 118.894 1.00 59.65 C ANISOU 3346 CG ASN A 353 10235 5520 6912 -561 -1825 94 C ATOM 3347 OD1 ASN A 353 13.676 10.539 119.826 1.00 62.99 O ANISOU 3347 OD1 ASN A 353 10465 5950 7519 -657 -1871 173 O ATOM 3348 ND2 ASN A 353 13.197 12.002 118.189 1.00 62.15 N ANISOU 3348 ND2 ASN A 353 10577 5810 7226 -649 -2024 97 N ATOM 3349 N ASP A 354 18.623 12.750 119.276 1.00 50.47 N ANISOU 3349 N ASP A 354 8990 4793 5393 98 -680 -6 N ATOM 3350 CA ASP A 354 20.002 12.709 118.813 1.00 42.15 C ANISOU 3350 CA ASP A 354 8111 3726 4178 319 -405 -33 C ATOM 3351 C ASP A 354 20.917 12.300 119.961 1.00 36.41 C ANISOU 3351 C ASP A 354 7146 3126 3563 385 -189 19 C ATOM 3352 O ASP A 354 20.983 13.013 120.970 1.00 43.16 O ANISOU 3352 O ASP A 354 7626 4189 4582 332 -111 72 O ATOM 3353 CB ASP A 354 20.400 14.080 118.261 1.00 40.37 C ANISOU 3353 CB ASP A 354 7830 3614 3893 397 -262 -34 C ATOM 3354 CG ASP A 354 21.806 14.108 117.674 1.00 50.67 C ANISOU 3354 CG ASP A 354 9307 4898 5048 635 36 -32 C ATOM 3355 OD1 ASP A 354 22.082 15.046 116.910 1.00 58.27 O ANISOU 3355 OD1 ASP A 354 10334 5885 5920 716 132 -34 O ATOM 3356 OD2 ASP A 354 22.637 13.215 117.962 1.00 48.16 O ANISOU 3356 OD2 ASP A 354 9054 4537 4709 749 184 -15 O ATOM 3357 N PRO A 355 21.643 11.183 119.852 1.00 41.85 N ANISOU 3357 N PRO A 355 8053 3689 4161 509 -91 8 N ATOM 3358 CA PRO A 355 22.600 10.822 120.906 1.00 35.33 C ANISOU 3358 CA PRO A 355 7001 2985 3437 587 122 65 C ATOM 3359 C PRO A 355 23.779 11.776 121.018 1.00 33.56 C ANISOU 3359 C PRO A 355 6591 2931 3231 726 401 110 C ATOM 3360 O PRO A 355 24.556 11.643 121.966 1.00 46.60 O ANISOU 3360 O PRO A 355 8009 4705 4994 775 555 167 O ATOM 3361 CB PRO A 355 23.077 9.422 120.485 1.00 41.69 C ANISOU 3361 CB PRO A 355 8155 3580 4105 709 157 40 C ATOM 3362 CG PRO A 355 22.066 8.942 119.482 1.00 44.66 C ANISOU 3362 CG PRO A 355 8900 3720 4351 630 -119 -33 C ATOM 3363 CD PRO A 355 21.625 10.182 118.773 1.00 41.20 C ANISOU 3363 CD PRO A 355 8450 3335 3869 591 -179 -56 C ATOM 3364 N ASN A 356 23.961 12.711 120.088 1.00 34.59 N ANISOU 3364 N ASN A 356 6816 3064 3263 791 466 96 N ATOM 3365 CA ASN A 356 25.027 13.692 120.204 1.00 38.26 C ANISOU 3365 CA ASN A 356 7073 3686 3780 901 714 157 C ATOM 3366 C ASN A 356 24.520 15.047 120.670 1.00 38.86 C ANISOU 3366 C ASN A 356 6836 3939 3989 767 646 168 C ATOM 3367 O ASN A 356 25.283 16.008 120.663 1.00 38.56 O ANISOU 3367 O ASN A 356 6637 4015 3999 834 813 215 O ATOM 3368 CB ASN A 356 25.765 13.839 118.877 1.00 43.29 C ANISOU 3368 CB ASN A 356 8016 4207 4225 1100 891 161 C ATOM 3369 CG ASN A 356 26.481 12.561 118.464 1.00 60.22 C ANISOU 3369 CG ASN A 356 10468 6183 6230 1282 1019 168 C ATOM 3370 OD1 ASN A 356 26.901 11.762 119.306 1.00 58.59 O ANISOU 3370 OD1 ASN A 356 10149 6002 6112 1296 1072 201 O ATOM 3371 ND2 ASN A 356 26.625 12.365 117.158 1.00 68.90 N ANISOU 3371 ND2 ASN A 356 11978 7102 7098 1435 1074 139 N ATOM 3372 N ARG A 357 23.262 15.133 121.109 1.00 40.38 N ANISOU 3372 N ARG A 357 6932 4154 4256 582 408 139 N ATOM 3373 CA ARG A 357 22.634 16.413 121.401 1.00 37.51 C ANISOU 3373 CA ARG A 357 6330 3933 3990 468 332 146 C ATOM 3374 C ARG A 357 23.217 17.111 122.624 1.00 36.91 C ANISOU 3374 C ARG A 357 5884 4059 4080 460 449 201 C ATOM 3375 O ARG A 357 22.950 18.300 122.813 1.00 34.07 O ANISOU 3375 O ARG A 357 5344 3815 3785 403 431 209 O ATOM 3376 CB ARG A 357 21.128 16.236 121.599 1.00 30.53 C ANISOU 3376 CB ARG A 357 5427 3015 3159 287 60 128 C ATOM 3377 CG ARG A 357 20.738 15.531 122.893 1.00 31.96 C ANISOU 3377 CG ARG A 357 5402 3251 3489 198 -6 168 C ATOM 3378 CD ARG A 357 19.304 15.014 122.770 1.00 33.55 C ANISOU 3378 CD ARG A 357 5671 3347 3728 41 -273 170 C ATOM 3379 NE ARG A 357 18.794 14.367 123.979 1.00 31.42 N ANISOU 3379 NE ARG A 357 5199 3126 3615 -48 -336 231 N ATOM 3380 CZ ARG A 357 18.949 13.079 124.278 1.00 36.63 C ANISOU 3380 CZ ARG A 357 5954 3682 4282 -38 -351 240 C ATOM 3381 NH1 ARG A 357 19.628 12.269 123.476 1.00 34.34 N ANISOU 3381 NH1 ARG A 357 5971 3233 3844 64 -306 187 N ATOM 3382 NH2 ARG A 357 18.411 12.598 125.384 1.00 34.46 N ANISOU 3382 NH2 ARG A 357 5478 3458 4157 -119 -402 311 N ATOM 3383 N CYS A 358 23.989 16.422 123.461 1.00 34.15 N ANISOU 3383 N CYS A 358 5431 3748 3798 518 554 237 N ATOM 3384 CA CYS A 358 24.501 17.109 124.639 1.00 34.49 C ANISOU 3384 CA CYS A 358 5145 3968 3991 505 626 284 C ATOM 3385 C CYS A 358 25.626 18.095 124.305 1.00 38.97 C ANISOU 3385 C CYS A 358 5625 4603 4580 604 803 323 C ATOM 3386 O CYS A 358 25.946 18.952 125.141 1.00 32.55 O ANISOU 3386 O CYS A 358 4552 3926 3891 573 821 353 O ATOM 3387 CB CYS A 358 24.945 16.082 125.679 1.00 29.80 C ANISOU 3387 CB CYS A 358 4462 3393 3465 534 663 317 C ATOM 3388 SG CYS A 358 23.542 15.259 126.486 1.00 34.40 S ANISOU 3388 SG CYS A 358 5019 3952 4099 389 454 307 S ATOM 3389 N GLU A 359 26.227 18.012 123.110 1.00 28.57 N ANISOU 3389 N GLU A 359 4525 3183 3148 726 932 331 N ATOM 3390 CA GLU A 359 27.153 19.074 122.709 1.00 35.80 C ANISOU 3390 CA GLU A 359 5341 4157 4104 806 1096 388 C ATOM 3391 C GLU A 359 26.412 20.381 122.464 1.00 37.68 C ANISOU 3391 C GLU A 359 5509 4456 4354 706 998 357 C ATOM 3392 O GLU A 359 26.890 21.453 122.854 1.00 33.69 O ANISOU 3392 O GLU A 359 4779 4058 3965 691 1049 400 O ATOM 3393 CB GLU A 359 27.951 18.669 121.470 1.00 37.32 C ANISOU 3393 CB GLU A 359 5794 4221 4163 987 1287 424 C ATOM 3394 CG GLU A 359 28.909 17.505 121.754 1.00 45.53 C ANISOU 3394 CG GLU A 359 6871 5215 5213 1117 1433 481 C ATOM 3395 CD GLU A 359 29.872 17.225 120.618 1.00 58.42 C ANISOU 3395 CD GLU A 359 8728 6736 6733 1332 1675 550 C ATOM 3396 OE1 GLU A 359 30.084 18.118 119.768 1.00 59.87 O ANISOU 3396 OE1 GLU A 359 8957 6912 6878 1390 1772 583 O ATOM 3397 OE2 GLU A 359 30.419 16.100 120.590 1.00 59.76 O ANISOU 3397 OE2 GLU A 359 9035 6822 6850 1455 1779 579 O ATOM 3398 N LEU A 360 25.247 20.317 121.816 1.00 30.53 N ANISOU 3398 N LEU A 360 4793 3473 3336 635 843 290 N ATOM 3399 CA LEU A 360 24.413 21.506 121.699 1.00 29.82 C ANISOU 3399 CA LEU A 360 4618 3446 3265 531 731 265 C ATOM 3400 C LEU A 360 23.952 21.996 123.071 1.00 35.60 C ANISOU 3400 C LEU A 360 5055 4321 4150 413 631 270 C ATOM 3401 O LEU A 360 23.954 23.202 123.336 1.00 37.37 O ANISOU 3401 O LEU A 360 5112 4641 4445 376 633 283 O ATOM 3402 CB LEU A 360 23.211 21.222 120.807 1.00 29.80 C ANISOU 3402 CB LEU A 360 4867 3327 3130 472 558 203 C ATOM 3403 CG LEU A 360 22.182 22.356 120.767 1.00 33.19 C ANISOU 3403 CG LEU A 360 5196 3824 3592 356 419 186 C ATOM 3404 CD1 LEU A 360 22.768 23.618 120.132 1.00 31.99 C ANISOU 3404 CD1 LEU A 360 5018 3712 3424 421 551 209 C ATOM 3405 CD2 LEU A 360 20.920 21.911 120.032 1.00 39.76 C ANISOU 3405 CD2 LEU A 360 6247 4535 4325 277 206 140 C ATOM 3406 N LEU A 361 23.554 21.074 123.960 1.00 28.52 N ANISOU 3406 N LEU A 361 4107 3431 3296 363 546 265 N ATOM 3407 CA LEU A 361 23.096 21.486 125.280 1.00 25.94 C ANISOU 3407 CA LEU A 361 3533 3231 3091 278 467 279 C ATOM 3408 C LEU A 361 24.207 22.188 126.055 1.00 31.11 C ANISOU 3408 C LEU A 361 3978 3993 3849 328 577 316 C ATOM 3409 O LEU A 361 23.959 23.199 126.721 1.00 29.85 O ANISOU 3409 O LEU A 361 3652 3930 3758 277 528 318 O ATOM 3410 CB LEU A 361 22.563 20.284 126.060 1.00 28.82 C ANISOU 3410 CB LEU A 361 3893 3573 3483 237 384 285 C ATOM 3411 CG LEU A 361 21.209 19.715 125.623 1.00 34.31 C ANISOU 3411 CG LEU A 361 4721 4177 4138 142 213 268 C ATOM 3412 CD1 LEU A 361 20.831 18.484 126.464 1.00 28.33 C ANISOU 3412 CD1 LEU A 361 3938 3393 3435 107 153 296 C ATOM 3413 CD2 LEU A 361 20.109 20.805 125.677 1.00 27.35 C ANISOU 3413 CD2 LEU A 361 3732 3364 3296 47 100 276 C ATOM 3414 N SER A 362 25.446 21.690 125.945 1.00 28.66 N ANISOU 3414 N SER A 362 3680 3657 3554 430 720 353 N ATOM 3415 CA SER A 362 26.569 22.350 126.609 1.00 32.24 C ANISOU 3415 CA SER A 362 3925 4195 4129 470 804 406 C ATOM 3416 C SER A 362 26.829 23.741 126.033 1.00 28.64 C ANISOU 3416 C SER A 362 3413 3766 3703 463 843 421 C ATOM 3417 O SER A 362 27.214 24.657 126.768 1.00 28.43 O ANISOU 3417 O SER A 362 3195 3819 3788 433 817 443 O ATOM 3418 CB SER A 362 27.821 21.475 126.516 1.00 29.68 C ANISOU 3418 CB SER A 362 3618 3829 3831 587 955 467 C ATOM 3419 OG SER A 362 27.667 20.328 127.365 1.00 27.57 O ANISOU 3419 OG SER A 362 3347 3561 3567 585 909 459 O ATOM 3420 N PHE A 363 26.663 23.912 124.721 1.00 30.74 N ANISOU 3420 N PHE A 363 3858 3953 3868 498 900 413 N ATOM 3421 CA PHE A 363 26.830 25.237 124.126 1.00 30.57 C ANISOU 3421 CA PHE A 363 3795 3951 3871 493 940 433 C ATOM 3422 C PHE A 363 25.727 26.181 124.578 1.00 32.52 C ANISOU 3422 C PHE A 363 3965 4265 4128 377 782 380 C ATOM 3423 O PHE A 363 25.980 27.366 124.846 1.00 36.00 O ANISOU 3423 O PHE A 363 4263 4762 4653 348 777 398 O ATOM 3424 CB PHE A 363 26.849 25.117 122.602 1.00 33.68 C ANISOU 3424 CB PHE A 363 4434 4235 4126 577 1042 438 C ATOM 3425 CG PHE A 363 26.992 26.439 121.869 1.00 37.72 C ANISOU 3425 CG PHE A 363 4926 4755 4649 584 1100 466 C ATOM 3426 CD1 PHE A 363 28.175 27.158 121.920 1.00 45.45 C ANISOU 3426 CD1 PHE A 363 5737 5766 5766 634 1239 562 C ATOM 3427 CD2 PHE A 363 25.951 26.934 121.099 1.00 40.24 C ANISOU 3427 CD2 PHE A 363 5394 5041 4853 539 1011 410 C ATOM 3428 CE1 PHE A 363 28.318 28.362 121.217 1.00 47.40 C ANISOU 3428 CE1 PHE A 363 5967 6010 6034 641 1300 601 C ATOM 3429 CE2 PHE A 363 26.087 28.125 120.393 1.00 49.39 C ANISOU 3429 CE2 PHE A 363 6548 6203 6016 555 1073 440 C ATOM 3430 CZ PHE A 363 27.271 28.841 120.458 1.00 48.00 C ANISOU 3430 CZ PHE A 363 6206 6056 5975 606 1223 535 C ATOM 3431 N LEU A 364 24.495 25.673 124.661 1.00 30.97 N ANISOU 3431 N LEU A 364 3860 4053 3855 312 651 326 N ATOM 3432 CA LEU A 364 23.371 26.508 125.066 1.00 32.05 C ANISOU 3432 CA LEU A 364 3924 4251 4004 219 516 296 C ATOM 3433 C LEU A 364 23.538 27.001 126.497 1.00 30.72 C ANISOU 3433 C LEU A 364 3544 4184 3944 191 475 307 C ATOM 3434 O LEU A 364 23.152 28.128 126.815 1.00 28.75 O ANISOU 3434 O LEU A 364 3210 3989 3724 152 423 299 O ATOM 3435 CB LEU A 364 22.064 25.736 124.921 1.00 32.93 C ANISOU 3435 CB LEU A 364 4148 4318 4046 157 386 267 C ATOM 3436 CG LEU A 364 21.667 25.401 123.486 1.00 35.78 C ANISOU 3436 CG LEU A 364 4751 4561 4280 170 366 243 C ATOM 3437 CD1 LEU A 364 20.454 24.488 123.504 1.00 39.93 C ANISOU 3437 CD1 LEU A 364 5364 5030 4777 93 204 229 C ATOM 3438 CD2 LEU A 364 21.388 26.681 122.705 1.00 36.95 C ANISOU 3438 CD2 LEU A 364 4923 4720 4396 159 363 237 C ATOM 3439 N LEU A 365 24.121 26.179 127.369 1.00 24.89 N ANISOU 3439 N LEU A 365 2738 3465 3256 221 496 324 N ATOM 3440 CA LEU A 365 24.395 26.631 128.732 1.00 26.58 C ANISOU 3440 CA LEU A 365 2782 3761 3556 212 448 333 C ATOM 3441 C LEU A 365 25.273 27.876 128.729 1.00 29.72 C ANISOU 3441 C LEU A 365 3076 4181 4035 219 476 352 C ATOM 3442 O LEU A 365 25.026 28.816 129.494 1.00 26.87 O ANISOU 3442 O LEU A 365 2631 3870 3707 188 395 337 O ATOM 3443 CB LEU A 365 25.061 25.524 129.545 1.00 20.75 C ANISOU 3443 CB LEU A 365 2000 3028 2855 257 474 356 C ATOM 3444 CG LEU A 365 24.149 24.354 129.942 1.00 23.96 C ANISOU 3444 CG LEU A 365 2471 3422 3212 240 423 347 C ATOM 3445 CD1 LEU A 365 24.976 23.163 130.488 1.00 20.79 C ANISOU 3445 CD1 LEU A 365 2054 3006 2838 299 476 374 C ATOM 3446 CD2 LEU A 365 23.119 24.810 130.967 1.00 23.55 C ANISOU 3446 CD2 LEU A 365 2344 3438 3164 200 323 342 C ATOM 3447 N VAL A 366 26.296 27.903 127.872 1.00 26.08 N ANISOU 3447 N VAL A 366 2627 3674 3610 265 594 396 N ATOM 3448 CA VAL A 366 27.167 29.074 127.785 1.00 28.46 C ANISOU 3448 CA VAL A 366 2813 3982 4019 263 623 438 C ATOM 3449 C VAL A 366 26.387 30.285 127.288 1.00 30.82 C ANISOU 3449 C VAL A 366 3148 4285 4278 213 577 405 C ATOM 3450 O VAL A 366 26.446 31.365 127.886 1.00 30.77 O ANISOU 3450 O VAL A 366 3044 4308 4337 174 501 399 O ATOM 3451 CB VAL A 366 28.379 28.777 126.892 1.00 29.21 C ANISOU 3451 CB VAL A 366 2908 4021 4170 340 790 522 C ATOM 3452 CG1 VAL A 366 29.095 30.075 126.499 1.00 29.37 C ANISOU 3452 CG1 VAL A 366 2822 4032 4307 330 832 585 C ATOM 3453 CG2 VAL A 366 29.346 27.829 127.634 1.00 35.16 C ANISOU 3453 CG2 VAL A 366 3566 4783 5010 390 823 574 C ATOM 3454 N LEU A 367 25.638 30.124 126.191 1.00 27.94 N ANISOU 3454 N LEU A 367 2939 3880 3798 217 611 383 N ATOM 3455 CA LEU A 367 24.851 31.242 125.673 1.00 33.34 C ANISOU 3455 CA LEU A 367 3660 4567 4439 175 566 357 C ATOM 3456 C LEU A 367 23.860 31.746 126.717 1.00 36.47 C ANISOU 3456 C LEU A 367 3997 5029 4832 118 428 314 C ATOM 3457 O LEU A 367 23.614 32.957 126.823 1.00 28.22 O ANISOU 3457 O LEU A 367 2911 4003 3808 90 385 305 O ATOM 3458 CB LEU A 367 24.102 30.835 124.407 1.00 31.66 C ANISOU 3458 CB LEU A 367 3642 4295 4092 188 589 337 C ATOM 3459 CG LEU A 367 24.837 30.351 123.160 1.00 44.61 C ANISOU 3459 CG LEU A 367 5422 5852 5677 274 736 375 C ATOM 3460 CD1 LEU A 367 23.820 30.146 122.048 1.00 49.01 C ANISOU 3460 CD1 LEU A 367 6198 6345 6079 272 693 334 C ATOM 3461 CD2 LEU A 367 25.901 31.345 122.737 1.00 47.98 C ANISOU 3461 CD2 LEU A 367 5765 6270 6196 314 860 446 C ATOM 3462 N ASP A 368 23.272 30.828 127.487 1.00 28.57 N ANISOU 3462 N ASP A 368 2999 4056 3802 111 368 296 N ATOM 3463 CA ASP A 368 22.271 31.212 128.480 1.00 25.49 C ANISOU 3463 CA ASP A 368 2562 3723 3399 84 265 276 C ATOM 3464 C ASP A 368 22.891 32.089 129.564 1.00 27.71 C ANISOU 3464 C ASP A 368 2738 4040 3751 95 224 273 C ATOM 3465 O ASP A 368 22.334 33.136 129.927 1.00 26.66 O ANISOU 3465 O ASP A 368 2595 3930 3606 84 167 257 O ATOM 3466 CB ASP A 368 21.629 29.963 129.113 1.00 26.52 C ANISOU 3466 CB ASP A 368 2705 3868 3502 86 231 282 C ATOM 3467 CG ASP A 368 20.788 29.138 128.128 1.00 37.12 C ANISOU 3467 CG ASP A 368 4165 5159 4779 57 219 285 C ATOM 3468 OD1 ASP A 368 20.460 29.620 127.017 1.00 31.42 O ANISOU 3468 OD1 ASP A 368 3527 4399 4013 37 218 276 O ATOM 3469 OD2 ASP A 368 20.474 27.964 128.467 1.00 36.28 O ANISOU 3469 OD2 ASP A 368 4078 5039 4668 54 198 298 O ATOM 3470 N TYR A 369 24.035 31.664 130.112 1.00 23.71 N ANISOU 3470 N TYR A 369 2164 3529 3318 119 241 290 N ATOM 3471 CA TYR A 369 24.665 32.443 131.176 1.00 23.87 C ANISOU 3471 CA TYR A 369 2100 3563 3408 123 162 285 C ATOM 3472 C TYR A 369 25.185 33.772 130.644 1.00 27.92 C ANISOU 3472 C TYR A 369 2579 4041 3988 93 158 295 C ATOM 3473 O TYR A 369 25.082 34.804 131.323 1.00 28.40 O ANISOU 3473 O TYR A 369 2628 4101 4062 81 62 271 O ATOM 3474 CB TYR A 369 25.778 31.620 131.838 1.00 23.82 C ANISOU 3474 CB TYR A 369 2021 3554 3478 152 164 314 C ATOM 3475 CG TYR A 369 25.198 30.703 132.870 1.00 27.20 C ANISOU 3475 CG TYR A 369 2473 4021 3841 186 123 297 C ATOM 3476 CD1 TYR A 369 24.856 31.186 134.136 1.00 24.64 C ANISOU 3476 CD1 TYR A 369 2152 3725 3485 211 19 272 C ATOM 3477 CD2 TYR A 369 24.919 29.372 132.568 1.00 25.62 C ANISOU 3477 CD2 TYR A 369 2314 3820 3600 203 191 311 C ATOM 3478 CE1 TYR A 369 24.262 30.357 135.084 1.00 28.00 C ANISOU 3478 CE1 TYR A 369 2608 4187 3845 259 4 273 C ATOM 3479 CE2 TYR A 369 24.333 28.535 133.512 1.00 22.69 C ANISOU 3479 CE2 TYR A 369 1960 3481 3182 232 162 311 C ATOM 3480 CZ TYR A 369 24.006 29.024 134.760 1.00 28.81 C ANISOU 3480 CZ TYR A 369 2723 4293 3930 264 78 298 C ATOM 3481 OH TYR A 369 23.412 28.190 135.686 1.00 26.82 O ANISOU 3481 OH TYR A 369 2490 4071 3629 309 72 314 O ATOM 3482 N ILE A 370 25.723 33.777 129.419 1.00 28.12 N ANISOU 3482 N ILE A 370 2607 4027 4051 89 265 335 N ATOM 3483 CA ILE A 370 26.044 35.049 128.775 1.00 29.25 C ANISOU 3483 CA ILE A 370 2726 4134 4253 60 278 357 C ATOM 3484 C ILE A 370 24.792 35.907 128.658 1.00 33.24 C ANISOU 3484 C ILE A 370 3312 4657 4662 39 225 307 C ATOM 3485 O ILE A 370 24.805 37.100 128.987 1.00 31.96 O ANISOU 3485 O ILE A 370 3128 4480 4537 16 155 295 O ATOM 3486 CB ILE A 370 26.695 34.817 127.401 1.00 28.12 C ANISOU 3486 CB ILE A 370 2600 3945 4140 86 434 422 C ATOM 3487 CG1 ILE A 370 28.088 34.196 127.568 1.00 27.29 C ANISOU 3487 CG1 ILE A 370 2382 3818 4167 118 499 501 C ATOM 3488 CG2 ILE A 370 26.779 36.147 126.602 1.00 30.09 C ANISOU 3488 CG2 ILE A 370 2847 4157 4429 62 464 449 C ATOM 3489 CD1 ILE A 370 28.752 33.889 126.241 1.00 27.65 C ANISOU 3489 CD1 ILE A 370 2459 3815 4231 177 687 584 C ATOM 3490 N GLY A 371 23.693 35.307 128.200 1.00 26.64 N ANISOU 3490 N GLY A 371 2569 3843 3710 48 247 284 N ATOM 3491 CA GLY A 371 22.461 36.054 127.994 1.00 22.45 C ANISOU 3491 CA GLY A 371 2098 3330 3100 33 205 259 C ATOM 3492 C GLY A 371 21.948 36.709 129.264 1.00 31.72 C ANISOU 3492 C GLY A 371 3250 4540 4264 44 106 232 C ATOM 3493 O GLY A 371 21.462 37.841 129.231 1.00 29.63 O ANISOU 3493 O GLY A 371 3009 4271 3979 40 73 221 O ATOM 3494 N ILE A 372 22.034 35.996 130.395 1.00 29.22 N ANISOU 3494 N ILE A 372 2905 4251 3945 72 65 225 N ATOM 3495 CA ILE A 372 21.663 36.563 131.691 1.00 26.64 C ANISOU 3495 CA ILE A 372 2588 3945 3587 111 -21 202 C ATOM 3496 C ILE A 372 22.542 37.762 132.023 1.00 26.60 C ANISOU 3496 C ILE A 372 2569 3889 3649 97 -92 183 C ATOM 3497 O ILE A 372 22.056 38.788 132.517 1.00 26.48 O ANISOU 3497 O ILE A 372 2610 3862 3590 121 -154 158 O ATOM 3498 CB ILE A 372 21.742 35.486 132.794 1.00 29.49 C ANISOU 3498 CB ILE A 372 2935 4337 3932 155 -42 205 C ATOM 3499 CG1 ILE A 372 20.489 34.620 132.797 1.00 25.90 C ANISOU 3499 CG1 ILE A 372 2504 3929 3410 175 -2 234 C ATOM 3500 CG2 ILE A 372 21.898 36.121 134.187 1.00 29.12 C ANISOU 3500 CG2 ILE A 372 2920 4284 3860 210 -140 178 C ATOM 3501 CD1 ILE A 372 19.228 35.357 133.164 1.00 33.15 C ANISOU 3501 CD1 ILE A 372 3459 4875 4260 216 -15 251 C ATOM 3502 N ASN A 373 23.852 37.655 131.771 1.00 23.92 N ANISOU 3502 N ASN A 373 2154 3508 3425 61 -90 204 N ATOM 3503 CA ASN A 373 24.749 38.773 132.072 1.00 27.47 C ANISOU 3503 CA ASN A 373 2570 3893 3975 29 -182 203 C ATOM 3504 C ASN A 373 24.463 39.980 131.180 1.00 32.56 C ANISOU 3504 C ASN A 373 3241 4502 4629 -4 -157 208 C ATOM 3505 O ASN A 373 24.558 41.130 131.631 1.00 31.72 O ANISOU 3505 O ASN A 373 3165 4342 4544 -16 -258 185 O ATOM 3506 CB ASN A 373 26.209 38.330 131.923 1.00 24.12 C ANISOU 3506 CB ASN A 373 2024 3433 3708 -4 -173 259 C ATOM 3507 CG ASN A 373 26.758 37.700 133.193 1.00 34.29 C ANISOU 3507 CG ASN A 373 3283 4725 5018 21 -278 249 C ATOM 3508 OD1 ASN A 373 26.100 37.694 134.242 1.00 39.60 O ANISOU 3508 OD1 ASN A 373 4046 5419 5582 69 -362 195 O ATOM 3509 ND2 ASN A 373 27.969 37.179 133.109 1.00 29.59 N ANISOU 3509 ND2 ASN A 373 2570 4108 4565 1 -267 312 N ATOM 3510 N MET A 374 24.102 39.744 129.911 1.00 26.37 N ANISOU 3510 N MET A 374 2465 3734 3819 -14 -32 235 N ATOM 3511 CA MET A 374 23.845 40.861 129.006 1.00 28.80 C ANISOU 3511 CA MET A 374 2804 4008 4131 -37 0 246 C ATOM 3512 C MET A 374 22.529 41.542 129.341 1.00 26.66 C ANISOU 3512 C MET A 374 2627 3763 3740 -8 -46 202 C ATOM 3513 O MET A 374 22.420 42.778 129.286 1.00 29.56 O ANISOU 3513 O MET A 374 3028 4087 4117 -18 -87 193 O ATOM 3514 CB MET A 374 23.859 40.369 127.557 1.00 24.68 C ANISOU 3514 CB MET A 374 2294 3488 3596 -38 142 288 C ATOM 3515 CG MET A 374 25.230 39.871 127.101 1.00 28.63 C ANISOU 3515 CG MET A 374 2705 3951 4223 -44 225 357 C ATOM 3516 SD MET A 374 26.479 41.185 127.153 1.00 44.47 S ANISOU 3516 SD MET A 374 4595 5873 6428 -96 186 422 S ATOM 3517 CE MET A 374 27.358 40.866 128.683 1.00 49.63 C ANISOU 3517 CE MET A 374 5148 6516 7195 -117 33 415 C ATOM 3518 N ALA A 375 21.514 40.749 129.684 1.00 21.99 N ANISOU 3518 N ALA A 375 2073 3236 3044 33 -36 189 N ATOM 3519 CA ALA A 375 20.236 41.319 130.078 1.00 25.61 C ANISOU 3519 CA ALA A 375 2601 3725 3404 79 -62 176 C ATOM 3520 C ALA A 375 20.393 42.199 131.313 1.00 33.76 C ANISOU 3520 C ALA A 375 3683 4722 4423 121 -162 140 C ATOM 3521 O ALA A 375 19.837 43.300 131.376 1.00 29.22 O ANISOU 3521 O ALA A 375 3177 4124 3803 149 -185 129 O ATOM 3522 CB ALA A 375 19.226 40.194 130.328 1.00 24.25 C ANISOU 3522 CB ALA A 375 2430 3622 3161 114 -33 196 C ATOM 3523 N SER A 376 21.157 41.733 132.299 1.00 27.05 N ANISOU 3523 N SER A 376 2816 3858 3603 133 -229 121 N ATOM 3524 CA SER A 376 21.404 42.523 133.497 1.00 35.26 C ANISOU 3524 CA SER A 376 3938 4841 4616 178 -353 79 C ATOM 3525 C SER A 376 22.333 43.701 133.221 1.00 37.51 C ANISOU 3525 C SER A 376 4220 5027 5006 111 -439 67 C ATOM 3526 O SER A 376 22.299 44.693 133.954 1.00 32.29 O ANISOU 3526 O SER A 376 3667 4296 4307 144 -550 27 O ATOM 3527 CB SER A 376 22.004 41.637 134.594 1.00 39.62 C ANISOU 3527 CB SER A 376 4483 5400 5172 208 -420 66 C ATOM 3528 OG SER A 376 21.098 40.634 135.001 1.00 48.41 O ANISOU 3528 OG SER A 376 5609 6595 6191 279 -346 86 O ATOM 3529 N LEU A 377 23.185 43.599 132.198 1.00 30.41 N ANISOU 3529 N LEU A 377 3206 4107 4240 26 -389 108 N ATOM 3530 CA LEU A 377 23.984 44.747 131.805 1.00 37.53 C ANISOU 3530 CA LEU A 377 4082 4912 5266 -43 -449 124 C ATOM 3531 C LEU A 377 23.097 45.894 131.319 1.00 38.81 C ANISOU 3531 C LEU A 377 4337 5055 5355 -25 -423 110 C ATOM 3532 O LEU A 377 23.451 47.061 131.494 1.00 33.26 O ANISOU 3532 O LEU A 377 3678 4255 4704 -53 -521 97 O ATOM 3533 CB LEU A 377 24.989 44.339 130.729 1.00 29.59 C ANISOU 3533 CB LEU A 377 2930 3897 4415 -112 -354 201 C ATOM 3534 CG LEU A 377 25.859 45.493 130.203 1.00 34.78 C ANISOU 3534 CG LEU A 377 3527 4451 5235 -187 -390 251 C ATOM 3535 CD1 LEU A 377 26.820 45.982 131.287 1.00 33.56 C ANISOU 3535 CD1 LEU A 377 3348 4199 5205 -233 -595 244 C ATOM 3536 CD2 LEU A 377 26.598 45.102 128.936 1.00 42.87 C ANISOU 3536 CD2 LEU A 377 4427 5480 6382 -220 -232 349 C ATOM 3537 N ASN A 378 21.943 45.584 130.715 1.00 35.13 N ANISOU 3537 N ASN A 378 3901 4670 4776 19 -306 117 N ATOM 3538 CA ASN A 378 21.002 46.635 130.349 1.00 33.15 C ANISOU 3538 CA ASN A 378 3738 4408 4448 51 -284 111 C ATOM 3539 C ASN A 378 20.568 47.424 131.574 1.00 42.24 C ANISOU 3539 C ASN A 378 5024 5515 5510 126 -392 61 C ATOM 3540 O ASN A 378 20.547 48.667 131.555 1.00 35.55 O ANISOU 3540 O ASN A 378 4257 4586 4664 127 -445 45 O ATOM 3541 CB ASN A 378 19.780 46.044 129.648 1.00 24.54 C ANISOU 3541 CB ASN A 378 2649 3414 3261 87 -169 138 C ATOM 3542 CG ASN A 378 18.752 47.109 129.265 1.00 30.60 C ANISOU 3542 CG ASN A 378 3495 4178 3955 128 -146 146 C ATOM 3543 OD1 ASN A 378 17.557 46.851 129.246 1.00 33.51 O ANISOU 3543 OD1 ASN A 378 3883 4614 4234 185 -101 170 O ATOM 3544 ND2 ASN A 378 19.223 48.313 128.973 1.00 33.92 N ANISOU 3544 ND2 ASN A 378 3948 4513 4427 97 -180 139 N ATOM 3545 N SER A 379 20.186 46.713 132.641 1.00 34.75 N ANISOU 3545 N SER A 379 4120 4611 4472 204 -416 41 N ATOM 3546 CA SER A 379 19.760 47.383 133.864 1.00 43.67 C ANISOU 3546 CA SER A 379 5414 5691 5486 310 -502 -2 C ATOM 3547 C SER A 379 20.888 48.238 134.412 1.00 43.27 C ANISOU 3547 C SER A 379 5429 5502 5508 263 -679 -51 C ATOM 3548 O SER A 379 20.669 49.361 134.882 1.00 37.80 O ANISOU 3548 O SER A 379 4895 4718 4750 314 -762 -89 O ATOM 3549 CB SER A 379 19.316 46.353 134.905 1.00 45.75 C ANISOU 3549 CB SER A 379 5709 6022 5651 407 -485 0 C ATOM 3550 OG SER A 379 18.487 45.349 134.330 1.00 41.93 O ANISOU 3550 OG SER A 379 5124 5656 5154 413 -346 60 O ATOM 3551 N CYS A 380 22.112 47.731 134.311 1.00 39.72 N ANISOU 3551 N CYS A 380 4859 5027 5208 162 -743 -41 N ATOM 3552 CA CYS A 380 23.287 48.464 134.758 1.00 38.07 C ANISOU 3552 CA CYS A 380 4670 4678 5118 90 -935 -65 C ATOM 3553 C CYS A 380 23.624 49.625 133.825 1.00 39.19 C ANISOU 3553 C CYS A 380 4779 4734 5379 2 -943 -37 C ATOM 3554 O CYS A 380 24.184 50.630 134.273 1.00 46.11 O ANISOU 3554 O CYS A 380 5737 5468 6313 -36 -1117 -64 O ATOM 3555 CB CYS A 380 24.446 47.468 134.877 1.00 37.95 C ANISOU 3555 CB CYS A 380 4498 4675 5248 15 -979 -32 C ATOM 3556 SG CYS A 380 26.062 48.225 135.173 1.00 49.89 S ANISOU 3556 SG CYS A 380 5949 6017 6989 -112 -1217 -14 S ATOM 3557 N ALA A 381 23.272 49.521 132.537 1.00 37.98 N ANISOU 3557 N ALA A 381 4522 4653 5256 -29 -766 17 N ATOM 3558 CA ALA A 381 23.672 50.500 131.525 1.00 32.60 C ANISOU 3558 CA ALA A 381 3789 3898 4700 -111 -743 63 C ATOM 3559 C ALA A 381 22.784 51.734 131.476 1.00 39.70 C ANISOU 3559 C ALA A 381 4845 4747 5491 -57 -751 30 C ATOM 3560 O ALA A 381 23.247 52.799 131.044 1.00 42.01 O ANISOU 3560 O ALA A 381 5140 4930 5890 -123 -802 51 O ATOM 3561 CB ALA A 381 23.664 49.872 130.127 1.00 32.32 C ANISOU 3561 CB ALA A 381 3611 3951 4717 -145 -545 137 C ATOM 3562 N ASN A 382 21.515 51.613 131.867 1.00 33.67 N ANISOU 3562 N ASN A 382 4202 4059 4534 64 -690 -5 N ATOM 3563 CA ASN A 382 20.607 52.753 131.761 1.00 34.22 C ANISOU 3563 CA ASN A 382 4415 4089 4498 134 -672 -21 C ATOM 3564 C ASN A 382 21.102 53.973 132.524 1.00 34.49 C ANISOU 3564 C ASN A 382 4606 3950 4547 130 -859 -73 C ATOM 3565 O ASN A 382 21.075 55.073 131.949 1.00 38.98 O ANISOU 3565 O ASN A 382 5216 4437 5156 99 -863 -61 O ATOM 3566 CB ASN A 382 19.197 52.355 132.206 1.00 31.42 C ANISOU 3566 CB ASN A 382 4147 3841 3951 280 -575 -25 C ATOM 3567 CG ASN A 382 18.540 51.380 131.252 1.00 35.29 C ANISOU 3567 CG ASN A 382 4497 4477 4436 270 -410 35 C ATOM 3568 OD1 ASN A 382 18.840 51.365 130.056 1.00 31.84 O ANISOU 3568 OD1 ASN A 382 3953 4053 4090 184 -344 74 O ATOM 3569 ND2 ASN A 382 17.633 50.567 131.773 1.00 32.33 N ANISOU 3569 ND2 ASN A 382 4130 4201 3954 364 -348 51 N ATOM 3570 N PRO A 383 21.551 53.878 133.783 1.00 38.48 N ANISOU 3570 N PRO A 383 5222 4380 5017 160 -1028 -132 N ATOM 3571 CA PRO A 383 22.103 55.084 134.423 1.00 41.95 C ANISOU 3571 CA PRO A 383 5833 4625 5483 140 -1243 -184 C ATOM 3572 C PRO A 383 23.299 55.640 133.678 1.00 45.22 C ANISOU 3572 C PRO A 383 6099 4931 6152 -38 -1330 -134 C ATOM 3573 O PRO A 383 23.477 56.862 133.635 1.00 41.72 O ANISOU 3573 O PRO A 383 5762 4337 5752 -73 -1440 -147 O ATOM 3574 CB PRO A 383 22.490 54.605 135.834 1.00 38.74 C ANISOU 3574 CB PRO A 383 5551 4167 5001 195 -1417 -249 C ATOM 3575 CG PRO A 383 21.718 53.365 136.059 1.00 40.22 C ANISOU 3575 CG PRO A 383 5692 4531 5059 300 -1252 -235 C ATOM 3576 CD PRO A 383 21.583 52.722 134.703 1.00 34.77 C ANISOU 3576 CD PRO A 383 4753 3981 4476 219 -1050 -155 C ATOM 3577 N ILE A 384 24.122 54.774 133.080 1.00 43.20 N ANISOU 3577 N ILE A 384 5601 4741 6072 -144 -1273 -64 N ATOM 3578 CA ILE A 384 25.315 55.244 132.381 1.00 45.29 C ANISOU 3578 CA ILE A 384 5698 4905 6605 -302 -1332 18 C ATOM 3579 C ILE A 384 24.928 55.999 131.115 1.00 41.00 C ANISOU 3579 C ILE A 384 5115 4367 6095 -322 -1172 76 C ATOM 3580 O ILE A 384 25.483 57.061 130.812 1.00 41.31 O ANISOU 3580 O ILE A 384 5151 4264 6283 -408 -1260 114 O ATOM 3581 CB ILE A 384 26.255 54.059 132.085 1.00 51.36 C ANISOU 3581 CB ILE A 384 6225 5751 7540 -377 -1279 95 C ATOM 3582 CG1 ILE A 384 26.668 53.373 133.393 1.00 46.53 C ANISOU 3582 CG1 ILE A 384 5661 5122 6896 -356 -1458 38 C ATOM 3583 CG2 ILE A 384 27.494 54.531 131.307 1.00 51.11 C ANISOU 3583 CG2 ILE A 384 5993 5618 7808 -525 -1304 216 C ATOM 3584 CD1 ILE A 384 27.491 52.095 133.206 1.00 41.01 C ANISOU 3584 CD1 ILE A 384 4738 4511 6333 -405 -1395 111 C ATOM 3585 N ALA A 385 23.954 55.480 130.371 1.00 35.02 N ANISOU 3585 N ALA A 385 4337 3766 5204 -244 -949 88 N ATOM 3586 CA ALA A 385 23.488 56.179 129.183 1.00 40.35 C ANISOU 3586 CA ALA A 385 4999 4450 5881 -246 -803 138 C ATOM 3587 C ALA A 385 22.972 57.575 129.530 1.00 38.13 C ANISOU 3587 C ALA A 385 4918 4046 5525 -206 -900 89 C ATOM 3588 O ALA A 385 23.284 58.545 128.833 1.00 36.64 O ANISOU 3588 O ALA A 385 4712 3761 5449 -269 -895 139 O ATOM 3589 CB ALA A 385 22.411 55.348 128.484 1.00 38.53 C ANISOU 3589 CB ALA A 385 4745 4397 5496 -161 -594 147 C ATOM 3590 N LEU A 386 22.190 57.700 130.612 1.00 38.83 N ANISOU 3590 N LEU A 386 5208 4128 5419 -89 -978 -1 N ATOM 3591 CA LEU A 386 21.687 59.017 131.007 1.00 46.47 C ANISOU 3591 CA LEU A 386 6400 4966 6292 -26 -1065 -51 C ATOM 3592 C LEU A 386 22.826 59.945 131.408 1.00 46.15 C ANISOU 3592 C LEU A 386 6408 4705 6422 -143 -1303 -61 C ATOM 3593 O LEU A 386 22.792 61.147 131.108 1.00 48.12 O ANISOU 3593 O LEU A 386 6751 4825 6706 -164 -1348 -55 O ATOM 3594 CB LEU A 386 20.686 58.887 132.154 1.00 47.62 C ANISOU 3594 CB LEU A 386 6764 5141 6188 149 -1086 -130 C ATOM 3595 CG LEU A 386 19.393 58.118 131.861 1.00 50.23 C ANISOU 3595 CG LEU A 386 7059 5670 6358 274 -868 -102 C ATOM 3596 CD1 LEU A 386 18.652 57.840 133.158 1.00 51.51 C ANISOU 3596 CD1 LEU A 386 7408 5850 6314 444 -893 -156 C ATOM 3597 CD2 LEU A 386 18.510 58.883 130.895 1.00 43.04 C ANISOU 3597 CD2 LEU A 386 6163 4789 5403 316 -726 -57 C ATOM 3598 N TYR A 387 23.842 59.406 132.089 1.00 42.92 N ANISOU 3598 N TYR A 387 5932 4243 6132 -223 -1470 -70 N ATOM 3599 CA TYR A 387 24.996 60.213 132.473 1.00 46.88 C ANISOU 3599 CA TYR A 387 6450 4526 6836 -356 -1731 -62 C ATOM 3600 C TYR A 387 25.689 60.800 131.250 1.00 45.65 C ANISOU 3600 C TYR A 387 6094 4314 6938 -498 -1664 61 C ATOM 3601 O TYR A 387 26.132 61.950 131.273 1.00 46.23 O ANISOU 3601 O TYR A 387 6238 4194 7134 -578 -1822 74 O ATOM 3602 CB TYR A 387 25.978 59.369 133.299 1.00 46.88 C ANISOU 3602 CB TYR A 387 6365 4503 6943 -423 -1908 -68 C ATOM 3603 CG TYR A 387 27.310 60.054 133.584 1.00 52.59 C ANISOU 3603 CG TYR A 387 7037 5006 7940 -592 -2193 -25 C ATOM 3604 CD1 TYR A 387 28.391 59.906 132.721 1.00 57.24 C ANISOU 3604 CD1 TYR A 387 7317 5584 8847 -752 -2155 121 C ATOM 3605 CD2 TYR A 387 27.483 60.846 134.712 1.00 52.68 C ANISOU 3605 CD2 TYR A 387 7313 4807 7896 -587 -2504 -120 C ATOM 3606 CE1 TYR A 387 29.600 60.532 132.973 1.00 59.99 C ANISOU 3606 CE1 TYR A 387 7585 5725 9482 -916 -2421 188 C ATOM 3607 CE2 TYR A 387 28.691 61.475 134.972 1.00 57.69 C ANISOU 3607 CE2 TYR A 387 7897 5222 8800 -758 -2801 -73 C ATOM 3608 CZ TYR A 387 29.746 61.312 134.101 1.00 63.80 C ANISOU 3608 CZ TYR A 387 8325 5996 9921 -930 -2759 89 C ATOM 3609 OH TYR A 387 30.951 61.936 134.350 1.00 71.87 O ANISOU 3609 OH TYR A 387 9261 6807 11237 -1099 -3045 166 O ATOM 3610 N LEU A 388 25.800 60.025 130.173 1.00 47.25 N ANISOU 3610 N LEU A 388 6060 4672 7222 -525 -1431 157 N ATOM 3611 CA LEU A 388 26.553 60.462 129.004 1.00 51.17 C ANISOU 3611 CA LEU A 388 6357 5119 7966 -642 -1340 295 C ATOM 3612 C LEU A 388 25.739 61.329 128.058 1.00 58.78 C ANISOU 3612 C LEU A 388 7397 6090 8846 -591 -1178 314 C ATOM 3613 O LEU A 388 26.315 62.121 127.303 1.00 65.48 O ANISOU 3613 O LEU A 388 8157 6834 9888 -681 -1158 416 O ATOM 3614 CB LEU A 388 27.079 59.250 128.236 1.00 51.68 C ANISOU 3614 CB LEU A 388 6164 5331 8140 -669 -1149 397 C ATOM 3615 CG LEU A 388 27.992 58.295 129.005 1.00 53.36 C ANISOU 3615 CG LEU A 388 6254 5550 8469 -723 -1275 408 C ATOM 3616 CD1 LEU A 388 28.283 57.067 128.163 1.00 51.89 C ANISOU 3616 CD1 LEU A 388 5857 5524 8333 -710 -1040 500 C ATOM 3617 CD2 LEU A 388 29.277 59.007 129.404 1.00 58.05 C ANISOU 3617 CD2 LEU A 388 6756 5938 9362 -876 -1521 484 C ATOM 3618 N VAL A 389 24.418 61.197 128.083 1.00 56.04 N ANISOU 3618 N VAL A 389 7204 5863 8227 -447 -1062 234 N ATOM 3619 CA VAL A 389 23.552 61.826 127.094 1.00 55.83 C ANISOU 3619 CA VAL A 389 7228 5878 8107 -384 -885 261 C ATOM 3620 C VAL A 389 22.945 63.112 127.645 1.00 53.09 C ANISOU 3620 C VAL A 389 7130 5394 7650 -326 -1004 189 C ATOM 3621 O VAL A 389 22.747 64.086 126.910 1.00 62.70 O ANISOU 3621 O VAL A 389 8382 6544 8898 -333 -943 234 O ATOM 3622 CB VAL A 389 22.463 60.825 126.651 1.00 62.83 C ANISOU 3622 CB VAL A 389 8098 6984 8790 -268 -679 245 C ATOM 3623 CG1 VAL A 389 21.148 61.501 126.522 1.00 66.31 C ANISOU 3623 CG1 VAL A 389 8710 7453 9030 -146 -609 206 C ATOM 3624 CG2 VAL A 389 22.841 60.174 125.336 1.00 60.54 C ANISOU 3624 CG2 VAL A 389 7612 6791 8601 -312 -484 352 C ATOM 3625 N SER A 390 22.655 63.137 128.942 1.00 48.93 N ANISOU 3625 N SER A 390 6794 4813 6982 -255 -1169 80 N ATOM 3626 CA SER A 390 21.938 64.246 129.561 1.00 56.80 C ANISOU 3626 CA SER A 390 8074 5687 7819 -153 -1262 2 C ATOM 3627 C SER A 390 22.891 65.073 130.422 1.00 60.07 C ANISOU 3627 C SER A 390 8619 5848 8358 -248 -1563 -40 C ATOM 3628 O SER A 390 23.470 64.557 131.384 1.00 58.88 O ANISOU 3628 O SER A 390 8494 5652 8226 -275 -1744 -90 O ATOM 3629 CB SER A 390 20.770 63.733 130.401 1.00 57.52 C ANISOU 3629 CB SER A 390 8335 5892 7627 37 -1207 -80 C ATOM 3630 OG SER A 390 20.253 64.773 131.214 1.00 60.74 O ANISOU 3630 OG SER A 390 9049 6152 7879 150 -1321 -156 O ATOM 3631 N LYS A 391 23.043 66.358 130.083 1.00 53.28 N ANISOU 3631 N LYS A 391 7850 4812 7580 -297 -1633 -18 N ATOM 3632 CA LYS A 391 23.889 67.233 130.890 1.00 58.83 C ANISOU 3632 CA LYS A 391 8704 5245 8403 -393 -1952 -59 C ATOM 3633 C LYS A 391 23.351 67.362 132.312 1.00 55.63 C ANISOU 3633 C LYS A 391 8643 4755 7737 -244 -2125 -205 C ATOM 3634 O LYS A 391 24.122 67.408 133.276 1.00 57.98 O ANISOU 3634 O LYS A 391 9045 4890 8095 -308 -2412 -261 O ATOM 3635 CB LYS A 391 24.003 68.613 130.233 1.00 62.70 C ANISOU 3635 CB LYS A 391 9251 5560 9011 -459 -1978 -7 C ATOM 3636 N ARG A 392 22.026 67.415 132.459 1.00 54.33 N ANISOU 3636 N ARG A 392 8662 4696 7283 -34 -1952 -258 N ATOM 3637 CA ARG A 392 21.413 67.522 133.780 1.00 55.09 C ANISOU 3637 CA ARG A 392 9103 4723 7104 152 -2063 -378 C ATOM 3638 C ARG A 392 21.745 66.309 134.642 1.00 56.71 C ANISOU 3638 C ARG A 392 9265 5016 7268 167 -2137 -419 C ATOM 3639 O ARG A 392 22.096 66.442 135.821 1.00 50.82 O ANISOU 3639 O ARG A 392 8762 4111 6438 204 -2386 -511 O ATOM 3640 CB ARG A 392 19.901 67.677 133.623 1.00 66.72 C ANISOU 3640 CB ARG A 392 10709 6330 8310 380 -1805 -381 C ATOM 3641 CG ARG A 392 19.163 68.154 134.856 1.00 77.70 C ANISOU 3641 CG ARG A 392 12505 7610 9406 609 -1880 -480 C ATOM 3642 CD ARG A 392 17.939 68.953 134.429 1.00 83.06 C ANISOU 3642 CD ARG A 392 13320 8318 9919 783 -1673 -451 C ATOM 3643 NE ARG A 392 17.456 68.511 133.120 1.00 89.33 N ANISOU 3643 NE ARG A 392 13793 9342 10808 736 -1405 -340 N ATOM 3644 CZ ARG A 392 16.563 69.167 132.383 1.00 92.76 C ANISOU 3644 CZ ARG A 392 14244 9821 11180 825 -1224 -283 C ATOM 3645 NH1 ARG A 392 16.192 68.681 131.204 1.00 89.88 N ANISOU 3645 NH1 ARG A 392 13595 9656 10900 773 -1013 -187 N ATOM 3646 NH2 ARG A 392 16.044 70.308 132.820 1.00 97.07 N ANISOU 3646 NH2 ARG A 392 15105 10204 11572 971 -1260 -322 N ATOM 3647 N PHE A 393 21.633 65.107 134.069 1.00 47.28 N ANISOU 3647 N PHE A 393 7780 4063 6120 144 -1930 -354 N ATOM 3648 CA PHE A 393 21.964 63.920 134.844 1.00 48.53 C ANISOU 3648 CA PHE A 393 7883 4308 6250 155 -1989 -384 C ATOM 3649 C PHE A 393 23.461 63.823 135.084 1.00 48.96 C ANISOU 3649 C PHE A 393 7817 4221 6565 -49 -2255 -372 C ATOM 3650 O PHE A 393 23.888 63.454 136.182 1.00 51.31 O ANISOU 3650 O PHE A 393 8240 4445 6812 -30 -2462 -440 O ATOM 3651 CB PHE A 393 21.437 62.659 134.148 1.00 44.39 C ANISOU 3651 CB PHE A 393 7093 4063 5710 183 -1706 -316 C ATOM 3652 CG PHE A 393 19.990 62.395 134.419 1.00 43.53 C ANISOU 3652 CG PHE A 393 7115 4095 5328 405 -1506 -332 C ATOM 3653 CD1 PHE A 393 19.578 61.978 135.672 1.00 48.94 C ANISOU 3653 CD1 PHE A 393 8007 4782 5806 567 -1556 -398 C ATOM 3654 CD2 PHE A 393 19.040 62.573 133.432 1.00 47.09 C ANISOU 3654 CD2 PHE A 393 7483 4672 5737 459 -1269 -267 C ATOM 3655 CE1 PHE A 393 18.237 61.739 135.934 1.00 50.72 C ANISOU 3655 CE1 PHE A 393 8332 5135 5803 781 -1353 -382 C ATOM 3656 CE2 PHE A 393 17.700 62.336 133.687 1.00 48.25 C ANISOU 3656 CE2 PHE A 393 7722 4944 5665 660 -1092 -255 C ATOM 3657 CZ PHE A 393 17.297 61.925 134.939 1.00 46.66 C ANISOU 3657 CZ PHE A 393 7707 4746 5276 822 -1124 -305 C ATOM 3658 N LYS A 394 24.269 64.153 134.072 1.00 52.76 N ANISOU 3658 N LYS A 394 8054 4661 7333 -238 -2252 -272 N ATOM 3659 CA LYS A 394 25.720 64.110 134.224 1.00 54.17 C ANISOU 3659 CA LYS A 394 8074 4701 7807 -440 -2496 -223 C ATOM 3660 C LYS A 394 26.162 64.912 135.440 1.00 57.65 C ANISOU 3660 C LYS A 394 8818 4868 8217 -453 -2873 -322 C ATOM 3661 O LYS A 394 26.937 64.428 136.274 1.00 54.13 O ANISOU 3661 O LYS A 394 8374 4353 7840 -511 -3108 -349 O ATOM 3662 CB LYS A 394 26.404 64.636 132.961 1.00 61.45 C ANISOU 3662 CB LYS A 394 8735 5581 9033 -613 -2424 -83 C ATOM 3663 CG LYS A 394 27.921 64.683 133.075 1.00 68.03 C ANISOU 3663 CG LYS A 394 9373 6257 10218 -827 -2671 5 C ATOM 3664 CD LYS A 394 28.585 65.231 131.822 1.00 67.94 C ANISOU 3664 CD LYS A 394 9098 6199 10517 -980 -2570 172 C ATOM 3665 CE LYS A 394 30.091 65.319 132.014 1.00 73.53 C ANISOU 3665 CE LYS A 394 9597 6736 11604 -1191 -2828 286 C ATOM 3666 NZ LYS A 394 30.775 65.925 130.840 1.00 82.89 N ANISOU 3666 NZ LYS A 394 10521 7903 13072 -1300 -2692 474 N ATOM 3667 N ASN A 395 25.652 66.137 135.572 1.00 59.80 N ANISOU 3667 N ASN A 395 9373 4975 8372 -388 -2945 -380 N ATOM 3668 CA ASN A 395 26.013 66.953 136.725 1.00 70.00 C ANISOU 3668 CA ASN A 395 11009 5984 9602 -383 -3316 -485 C ATOM 3669 C ASN A 395 25.405 66.413 138.013 1.00 74.93 C ANISOU 3669 C ASN A 395 11931 6649 9889 -166 -3362 -609 C ATOM 3670 O ASN A 395 26.038 66.485 139.075 1.00 74.78 O ANISOU 3670 O ASN A 395 12030 6552 9833 -156 -3607 -626 O ATOM 3671 CB ASN A 395 25.591 68.398 136.486 1.00 72.75 C ANISOU 3671 CB ASN A 395 11566 6192 9883 -340 -3326 -494 C ATOM 3672 CG ASN A 395 26.430 69.071 135.419 1.00 80.54 C ANISOU 3672 CG ASN A 395 12271 7111 11219 -560 -3336 -356 C ATOM 3673 OD1 ASN A 395 27.657 68.946 135.411 1.00 88.50 O ANISOU 3673 OD1 ASN A 395 13031 8094 12500 -732 -3489 -258 O ATOM 3674 ND2 ASN A 395 25.775 69.768 134.500 1.00 77.60 N ANISOU 3674 ND2 ASN A 395 11927 6716 10842 -538 -3154 -329 N ATOM 3675 N ALA A 396 24.194 65.854 137.940 1.00 73.80 N ANISOU 3675 N ALA A 396 11839 6715 9488 38 -3058 -633 N ATOM 3676 CA ALA A 396 23.573 65.287 139.132 1.00 73.93 C ANISOU 3676 CA ALA A 396 12128 6772 9192 258 -3067 -730 C ATOM 3677 C ALA A 396 24.373 64.107 139.670 1.00 72.47 C ANISOU 3677 C ALA A 396 11783 6655 9099 182 -3186 -727 C ATOM 3678 O ALA A 396 24.569 63.984 140.884 1.00 80.27 O ANISOU 3678 O ALA A 396 13014 7551 9935 276 -3385 -797 O ATOM 3679 CB ALA A 396 22.140 64.868 138.824 1.00 75.89 C ANISOU 3679 CB ALA A 396 12374 7259 9201 475 -2684 -705 C ATOM 3680 N PHE A 397 24.835 63.221 138.783 1.00 71.80 N ANISOU 3680 N PHE A 397 11276 6757 9248 34 -3030 -620 N ATOM 3681 CA PHE A 397 25.689 62.120 139.222 1.00 65.26 C ANISOU 3681 CA PHE A 397 10271 5986 8538 -51 -3143 -602 C ATOM 3682 C PHE A 397 27.001 62.633 139.806 1.00 71.76 C ANISOU 3682 C PHE A 397 11131 6566 9567 -214 -3540 -604 C ATOM 3683 O PHE A 397 27.552 62.014 140.722 1.00 65.55 O ANISOU 3683 O PHE A 397 10362 5783 8759 -190 -3679 -606 O ATOM 3684 CB PHE A 397 25.985 61.172 138.063 1.00 53.81 C ANISOU 3684 CB PHE A 397 8373 4761 7310 -174 -2892 -475 C ATOM 3685 CG PHE A 397 24.865 60.211 137.727 1.00 46.69 C ANISOU 3685 CG PHE A 397 7394 4132 6215 -20 -2539 -460 C ATOM 3686 CD1 PHE A 397 24.121 60.365 136.557 1.00 48.63 C ANISOU 3686 CD1 PHE A 397 7505 4512 6461 -4 -2253 -396 C ATOM 3687 CD2 PHE A 397 24.591 59.127 138.545 1.00 49.13 C ANISOU 3687 CD2 PHE A 397 7750 4556 6362 99 -2506 -500 C ATOM 3688 CE1 PHE A 397 23.107 59.460 136.218 1.00 46.31 C ANISOU 3688 CE1 PHE A 397 7124 4454 6016 119 -1961 -372 C ATOM 3689 CE2 PHE A 397 23.575 58.207 138.208 1.00 47.36 C ANISOU 3689 CE2 PHE A 397 7428 4572 5993 223 -2194 -469 C ATOM 3690 CZ PHE A 397 22.834 58.382 137.052 1.00 43.82 C ANISOU 3690 CZ PHE A 397 6846 4246 5556 227 -1935 -405 C ATOM 3691 N LYS A 398 27.514 63.756 139.286 1.00 73.52 N ANISOU 3691 N LYS A 398 11302 6648 9983 -343 -3635 -536 N ATOM 3692 CA LYS A 398 28.765 64.321 139.793 1.00 78.94 C ANISOU 3692 CA LYS A 398 11947 7178 10866 -461 -3924 -461 C ATOM 3693 C LYS A 398 28.617 64.771 141.241 1.00 86.82 C ANISOU 3693 C LYS A 398 13352 8036 11598 -294 -4148 -550 C ATOM 3694 O LYS A 398 29.459 64.456 142.090 1.00 93.20 O ANISOU 3694 O LYS A 398 14167 8778 12468 -316 -4361 -524 O ATOM 3695 CB LYS A 398 29.212 65.498 138.922 1.00 76.30 C ANISOU 3695 CB LYS A 398 11495 6729 10767 -611 -3961 -369 C ATOM 3696 CG LYS A 398 29.665 65.144 137.511 1.00 79.98 C ANISOU 3696 CG LYS A 398 11533 7302 11555 -788 -3762 -232 C ATOM 3697 CD LYS A 398 30.992 64.408 137.488 1.00 85.54 C ANISOU 3697 CD LYS A 398 11896 8050 12557 -928 -3839 -95 C ATOM 3698 CE LYS A 398 31.654 64.541 136.123 1.00 85.48 C ANISOU 3698 CE LYS A 398 11500 8085 12892 -1093 -3675 83 C ATOM 3699 NZ LYS A 398 31.869 65.972 135.749 1.00 83.70 N ANISOU 3699 NZ LYS A 398 11327 7699 12777 -1161 -3767 133 N ATOM 3700 N SER A 399 27.552 65.524 141.538 1.00 83.47 N ANISOU 3700 N SER A 399 13279 7558 10878 -114 -4091 -643 N ATOM 3701 CA SER A 399 27.326 65.978 142.907 1.00 84.20 C ANISOU 3701 CA SER A 399 13786 7515 10692 75 -4272 -714 C ATOM 3702 C SER A 399 27.146 64.801 143.858 1.00 89.45 C ANISOU 3702 C SER A 399 14537 8270 11178 221 -4242 -758 C ATOM 3703 O SER A 399 27.667 64.814 144.980 1.00 98.85 O ANISOU 3703 O SER A 399 15916 9335 12309 278 -4471 -765 O ATOM 3704 CB SER A 399 26.107 66.895 142.967 1.00 78.21 C ANISOU 3704 CB SER A 399 13365 6717 9633 271 -4147 -784 C ATOM 3705 OG SER A 399 26.180 67.913 141.986 1.00 78.83 O ANISOU 3705 OG SER A 399 13349 6730 9874 140 -4132 -746 O ATOM 3706 N ALA A 400 26.422 63.766 143.420 1.00 79.59 N ANISOU 3706 N ALA A 400 13156 7233 9851 283 -3964 -784 N ATOM 3707 CA ALA A 400 26.089 62.664 144.314 1.00 80.78 C ANISOU 3707 CA ALA A 400 13406 7484 9804 448 -3896 -826 C ATOM 3708 C ALA A 400 27.276 61.741 144.556 1.00 90.32 C ANISOU 3708 C ALA A 400 14359 8713 11245 295 -4043 -773 C ATOM 3709 O ALA A 400 27.364 61.122 145.622 1.00 94.27 O ANISOU 3709 O ALA A 400 15006 9202 11610 415 -4107 -800 O ATOM 3710 CB ALA A 400 24.915 61.864 143.748 1.00 81.21 C ANISOU 3710 CB ALA A 400 13393 7765 9698 566 -3556 -861 C ATOM 3711 N LEU A 401 28.189 61.630 143.593 1.00 94.40 N ANISOU 3711 N LEU A 401 14495 9260 12113 46 -4077 -683 N ATOM 3712 CA LEU A 401 29.247 60.626 143.636 1.00 98.43 C ANISOU 3712 CA LEU A 401 14707 9833 12861 -91 -4145 -608 C ATOM 3713 C LEU A 401 30.645 61.202 143.802 1.00112.63 C ANISOU 3713 C LEU A 401 16391 11453 14952 -263 -4430 -507 C ATOM 3714 O LEU A 401 31.471 60.605 144.498 1.00112.85 O ANISOU 3714 O LEU A 401 16367 11445 15066 -289 -4578 -472 O ATOM 3715 CB LEU A 401 29.205 59.770 142.368 1.00 89.53 C ANISOU 3715 CB LEU A 401 13184 8919 11916 -216 -3902 -549 C ATOM 3716 CG LEU A 401 27.911 58.979 142.186 1.00 80.99 C ANISOU 3716 CG LEU A 401 12167 8036 10569 -59 -3635 -633 C ATOM 3717 CD1 LEU A 401 28.005 58.049 140.990 1.00 77.98 C ANISOU 3717 CD1 LEU A 401 11377 7868 10384 -182 -3406 -548 C ATOM 3718 CD2 LEU A 401 27.609 58.209 143.455 1.00 77.98 C ANISOU 3718 CD2 LEU A 401 12005 7692 9931 133 -3653 -698 C ATOM 3719 N CYS A 402 30.940 62.340 143.178 1.00118.08 N ANISOU 3719 N CYS A 402 17035 12027 15802 -377 -4510 -452 N ATOM 3720 CA CYS A 402 32.262 62.948 143.256 1.00125.30 C ANISOU 3720 CA CYS A 402 17821 12775 17014 -542 -4778 -336 C ATOM 3721 C CYS A 402 32.398 63.897 144.439 1.00130.66 C ANISOU 3721 C CYS A 402 18894 13212 17541 -450 -5091 -388 C ATOM 3722 O CYS A 402 33.393 64.625 144.523 1.00137.61 O ANISOU 3722 O CYS A 402 19718 13920 18646 -578 -5347 -298 O ATOM 3723 CB CYS A 402 32.576 63.689 141.952 1.00126.91 C ANISOU 3723 CB CYS A 402 17754 12976 17490 -713 -4700 -229 C ATOM 3724 SG CYS A 402 32.579 62.611 140.495 1.00125.69 S ANISOU 3724 SG CYS A 402 17127 13079 17550 -826 -4341 -134 S ATOM 3725 N CYS A 403 31.435 63.898 145.355 1.00128.19 N ANISOU 3725 N CYS A 403 18977 12876 16855 -223 -5073 -518 N ATOM 3726 CA CYS A 403 31.491 64.785 146.549 1.00128.12 C ANISOU 3726 CA CYS A 403 19392 12626 16662 -102 -5362 -567 C ATOM 3727 C CYS A 403 30.912 64.051 147.764 1.00125.27 C ANISOU 3727 C CYS A 403 19341 12275 15980 133 -5335 -662 C ATOM 3728 O CYS A 403 31.077 62.815 147.813 1.00122.43 O ANISOU 3728 O CYS A 403 18787 12063 15668 122 -5218 -655 O ATOM 3729 CB CYS A 403 30.728 66.082 146.305 1.00127.53 C ANISOU 3729 CB CYS A 403 19569 12462 16425 -30 -5349 -614 C ATOM 3730 SG CYS A 403 31.451 67.118 145.006 1.00127.93 S ANISOU 3730 SG CYS A 403 19304 12455 16848 -295 -5412 -500 S TER 3731 CYS A 403 ATOM 3732 N CYS B 1 13.604 27.224 132.368 1.00 42.12 N ANISOU 3732 N CYS B 1 4621 4707 6675 1567 -1014 -893 N ATOM 3733 CA CYS B 1 14.108 26.102 131.524 1.00 43.52 C ANISOU 3733 CA CYS B 1 5020 4966 6548 1278 -953 -499 C ATOM 3734 C CYS B 1 13.046 24.994 131.462 1.00 44.22 C ANISOU 3734 C CYS B 1 4777 5314 6711 1228 -776 -557 C ATOM 3735 O CYS B 1 12.501 24.650 132.530 1.00 44.56 O ANISOU 3735 O CYS B 1 4526 5651 6756 1241 -440 -801 O ATOM 3736 CB CYS B 1 15.416 25.558 132.086 1.00 35.35 C ANISOU 3736 CB CYS B 1 4227 4102 5101 1075 -647 -358 C ATOM 3737 SG CYS B 1 16.271 24.394 130.993 1.00 38.26 S ANISOU 3737 SG CYS B 1 4848 4513 5176 763 -660 -11 S ATOM 3738 N THR B 2 12.753 24.446 130.287 1.00 43.84 N ANISOU 3738 N THR B 2 4756 5209 6693 1125 -970 -365 N ATOM 3739 CA THR B 2 11.740 23.405 130.178 1.00 49.09 C ANISOU 3739 CA THR B 2 5090 6099 7462 1052 -805 -455 C ATOM 3740 C THR B 2 12.175 22.349 129.170 1.00 45.86 C ANISOU 3740 C THR B 2 4832 5712 6881 794 -824 -182 C ATOM 3741 O THR B 2 13.103 22.549 128.383 1.00 44.06 O ANISOU 3741 O THR B 2 4914 5360 6468 686 -1025 32 O ATOM 3742 CB THR B 2 10.382 23.985 129.777 1.00 65.22 C ANISOU 3742 CB THR B 2 6781 8092 9909 1306 -1098 -735 C ATOM 3743 OG1 THR B 2 9.368 22.989 129.956 1.00 75.59 O ANISOU 3743 OG1 THR B 2 7702 9705 11314 1203 -832 -926 O ATOM 3744 CG2 THR B 2 10.409 24.410 128.325 1.00 67.37 C ANISOU 3744 CG2 THR B 2 7251 8103 10243 1342 -1618 -504 C ATOM 3745 N CYS B 3 11.471 21.215 129.198 1.00 47.59 N ANISOU 3745 N CYS B 3 4793 6116 7171 660 -603 -244 N ATOM 3746 CA CYS B 3 11.736 20.087 128.315 1.00 40.62 C ANISOU 3746 CA CYS B 3 3956 5263 6216 426 -599 -94 C ATOM 3747 C CYS B 3 10.419 19.489 127.842 1.00 46.60 C ANISOU 3747 C CYS B 3 4326 6149 7231 398 -600 -274 C ATOM 3748 O CYS B 3 9.413 19.533 128.553 1.00 44.38 O ANISOU 3748 O CYS B 3 3732 6004 7126 466 -428 -510 O ATOM 3749 CB CYS B 3 12.565 19.006 129.035 1.00 45.39 C ANISOU 3749 CB CYS B 3 4706 5900 6639 223 -272 40 C ATOM 3750 SG CYS B 3 14.171 19.623 129.602 1.00 49.23 S ANISOU 3750 SG CYS B 3 5594 6299 6813 265 -273 178 S ATOM 3751 N PHE B 4 10.453 18.896 126.640 1.00 52.08 N ANISOU 3751 N PHE B 4 5002 6859 7925 263 -770 -219 N ATOM 3752 CA PHE B 4 9.263 18.262 126.069 1.00 56.01 C ANISOU 3752 CA PHE B 4 5115 7503 8663 216 -785 -421 C ATOM 3753 C PHE B 4 8.722 17.148 126.970 1.00 46.43 C ANISOU 3753 C PHE B 4 3681 6389 7570 19 -343 -528 C ATOM 3754 O PHE B 4 7.508 17.047 127.181 1.00 44.49 O ANISOU 3754 O PHE B 4 3056 6310 7539 30 -239 -793 O ATOM 3755 CB PHE B 4 9.581 17.710 124.670 1.00 59.60 C ANISOU 3755 CB PHE B 4 5593 8013 9039 50 -1004 -368 C ATOM 3756 CG PHE B 4 8.363 17.269 123.890 1.00 64.05 C ANISOU 3756 CG PHE B 4 5750 8756 9831 38 -1113 -605 C ATOM 3757 CD1 PHE B 4 7.600 18.196 123.191 1.00 67.33 C ANISOU 3757 CD1 PHE B 4 6034 9225 10323 264 -1529 -682 C ATOM 3758 CD2 PHE B 4 7.985 15.936 123.851 1.00 60.82 C ANISOU 3758 CD2 PHE B 4 5090 8433 9584 -196 -840 -759 C ATOM 3759 CE1 PHE B 4 6.486 17.806 122.478 1.00 67.90 C ANISOU 3759 CE1 PHE B 4 5702 9501 10595 278 -1657 -938 C ATOM 3760 CE2 PHE B 4 6.860 15.537 123.135 1.00 65.85 C ANISOU 3760 CE2 PHE B 4 5317 9268 10437 -222 -925 -1033 C ATOM 3761 CZ PHE B 4 6.115 16.472 122.448 1.00 69.86 C ANISOU 3761 CZ PHE B 4 5666 9895 10982 25 -1328 -1138 C ATOM 3762 N THR B 5 9.600 16.300 127.508 1.00 39.94 N ANISOU 3762 N THR B 5 3092 5468 6616 -184 -103 -331 N ATOM 3763 CA THR B 5 9.149 15.185 128.330 1.00 44.43 C ANISOU 3763 CA THR B 5 3541 6066 7274 -445 264 -326 C ATOM 3764 C THR B 5 10.150 14.921 129.448 1.00 41.61 C ANISOU 3764 C THR B 5 3529 5590 6690 -530 455 -52 C ATOM 3765 O THR B 5 11.355 15.091 129.267 1.00 40.78 O ANISOU 3765 O THR B 5 3727 5341 6428 -441 302 98 O ATOM 3766 CB THR B 5 8.956 13.905 127.496 1.00 42.93 C ANISOU 3766 CB THR B 5 3215 5805 7292 -680 267 -374 C ATOM 3767 OG1 THR B 5 8.810 12.785 128.373 1.00 47.26 O ANISOU 3767 OG1 THR B 5 3791 6254 7912 -983 586 -251 O ATOM 3768 CG2 THR B 5 10.172 13.662 126.605 1.00 41.79 C ANISOU 3768 CG2 THR B 5 3303 5511 7063 -664 27 -282 C ATOM 3769 N TYR B 6 9.620 14.491 130.603 1.00 49.33 N ANISOU 3769 N TYR B 6 4441 6677 7624 -736 786 -8 N ATOM 3770 CA TYR B 6 10.445 14.013 131.716 1.00 57.72 C ANISOU 3770 CA TYR B 6 5834 7648 8450 -883 951 306 C ATOM 3771 C TYR B 6 11.403 12.907 131.295 1.00 49.42 C ANISOU 3771 C TYR B 6 5044 6247 7488 -979 808 534 C ATOM 3772 O TYR B 6 12.488 12.781 131.867 1.00 53.39 O ANISOU 3772 O TYR B 6 5870 6607 7807 -933 753 760 O ATOM 3773 CB TYR B 6 9.566 13.466 132.850 1.00 71.38 C ANISOU 3773 CB TYR B 6 7439 9587 10097 -1237 1327 356 C ATOM 3774 CG TYR B 6 8.885 14.495 133.716 1.00 83.39 C ANISOU 3774 CG TYR B 6 8719 11525 11441 -1180 1531 99 C ATOM 3775 CD1 TYR B 6 9.621 15.337 134.540 1.00 87.99 C ANISOU 3775 CD1 TYR B 6 9490 12215 11727 -1007 1538 151 C ATOM 3776 CD2 TYR B 6 7.499 14.602 133.739 1.00 87.57 C ANISOU 3776 CD2 TYR B 6 8777 12376 12119 -1308 1722 -277 C ATOM 3777 CE1 TYR B 6 8.991 16.279 135.348 1.00 92.43 C ANISOU 3777 CE1 TYR B 6 9768 13182 12169 -951 1722 -184 C ATOM 3778 CE2 TYR B 6 6.865 15.537 134.541 1.00 92.85 C ANISOU 3778 CE2 TYR B 6 9141 13464 12672 -1243 1898 -637 C ATOM 3779 CZ TYR B 6 7.614 16.374 135.344 1.00 94.33 C ANISOU 3779 CZ TYR B 6 9515 13740 12586 -1063 1896 -597 C ATOM 3780 OH TYR B 6 6.985 17.308 136.144 1.00 94.69 O ANISOU 3780 OH TYR B 6 9199 14222 12557 -991 2066 -1050 O ATOM 3781 N LYS B 7 11.004 12.069 130.333 1.00 45.77 N ANISOU 3781 N LYS B 7 4405 5651 7333 -1103 732 420 N ATOM 3782 CA LYS B 7 11.833 10.938 129.936 1.00 52.36 C ANISOU 3782 CA LYS B 7 5410 6134 8352 -1189 579 528 C ATOM 3783 C LYS B 7 13.103 11.364 129.204 1.00 44.28 C ANISOU 3783 C LYS B 7 4532 5056 7238 -934 290 438 C ATOM 3784 O LYS B 7 13.996 10.531 129.020 1.00 39.42 O ANISOU 3784 O LYS B 7 4046 4175 6759 -947 137 456 O ATOM 3785 CB LYS B 7 11.032 9.960 129.062 1.00 61.52 C ANISOU 3785 CB LYS B 7 6277 7199 9899 -1398 582 332 C ATOM 3786 CG LYS B 7 9.529 9.848 129.375 1.00 66.43 C ANISOU 3786 CG LYS B 7 6594 8035 10613 -1645 868 233 C ATOM 3787 CD LYS B 7 9.201 9.663 130.861 1.00 71.68 C ANISOU 3787 CD LYS B 7 7416 8749 11071 -1919 1177 523 C ATOM 3788 CE LYS B 7 7.720 9.993 131.136 1.00 77.40 C ANISOU 3788 CE LYS B 7 7735 9883 11789 -2111 1478 262 C ATOM 3789 NZ LYS B 7 7.368 10.039 132.588 1.00 75.74 N ANISOU 3789 NZ LYS B 7 7612 9905 11260 -2417 1819 457 N ATOM 3790 N ASP B 8 13.206 12.628 128.782 1.00 38.66 N ANISOU 3790 N ASP B 8 3790 4579 6320 -727 194 317 N ATOM 3791 CA ASP B 8 14.450 13.163 128.213 1.00 38.31 C ANISOU 3791 CA ASP B 8 3914 4546 6097 -574 -31 252 C ATOM 3792 C ASP B 8 15.317 13.657 129.368 1.00 36.72 C ANISOU 3792 C ASP B 8 4011 4315 5626 -455 29 440 C ATOM 3793 O ASP B 8 15.385 14.847 129.693 1.00 32.87 O ANISOU 3793 O ASP B 8 3596 3976 4917 -315 43 447 O ATOM 3794 CB ASP B 8 14.153 14.267 127.206 1.00 32.26 C ANISOU 3794 CB ASP B 8 3035 4001 5223 -481 -198 103 C ATOM 3795 CG ASP B 8 15.404 14.846 126.572 1.00 33.82 C ANISOU 3795 CG ASP B 8 3413 4264 5174 -442 -399 45 C ATOM 3796 OD1 ASP B 8 16.530 14.437 126.933 1.00 31.12 O ANISOU 3796 OD1 ASP B 8 3234 3829 4762 -438 -400 43 O ATOM 3797 OD2 ASP B 8 15.261 15.730 125.695 1.00 35.85 O ANISOU 3797 OD2 ASP B 8 3649 4677 5296 -435 -581 -2 O ATOM 3798 N LYS B 9 16.005 12.708 129.994 1.00 32.64 N ANISOU 3798 N LYS B 9 4142 3133 5128 -15 242 550 N ATOM 3799 CA LYS B 9 16.785 13.016 131.184 1.00 42.34 C ANISOU 3799 CA LYS B 9 5322 4463 6304 56 303 698 C ATOM 3800 C LYS B 9 17.961 13.931 130.885 1.00 36.00 C ANISOU 3800 C LYS B 9 4499 3770 5410 203 341 624 C ATOM 3801 O LYS B 9 18.432 14.619 131.794 1.00 32.48 O ANISOU 3801 O LYS B 9 3992 3459 4890 243 351 716 O ATOM 3802 CB LYS B 9 17.276 11.720 131.848 1.00 33.81 C ANISOU 3802 CB LYS B 9 4315 3181 5348 73 276 829 C ATOM 3803 CG LYS B 9 16.147 10.815 132.319 1.00 37.04 C ANISOU 3803 CG LYS B 9 4750 3467 5858 -100 271 941 C ATOM 3804 CD LYS B 9 16.685 9.697 133.193 1.00 40.73 C ANISOU 3804 CD LYS B 9 5330 3742 6405 -80 242 1116 C ATOM 3805 CE LYS B 9 15.582 9.040 134.012 1.00 44.92 C ANISOU 3805 CE LYS B 9 5894 4186 6988 -277 298 1287 C ATOM 3806 NZ LYS B 9 16.183 8.006 134.907 1.00 51.51 N ANISOU 3806 NZ LYS B 9 6896 4817 7857 -247 252 1483 N ATOM 3807 N GLU B 10 18.442 13.957 129.640 1.00 36.79 N ANISOU 3807 N GLU B 10 4668 3801 5511 274 372 457 N ATOM 3808 CA GLU B 10 19.533 14.866 129.301 1.00 36.43 C ANISOU 3808 CA GLU B 10 4586 3847 5407 390 459 389 C ATOM 3809 C GLU B 10 19.049 16.307 129.278 1.00 36.73 C ANISOU 3809 C GLU B 10 4582 4097 5278 347 464 368 C ATOM 3810 O GLU B 10 19.741 17.210 129.754 1.00 32.59 O ANISOU 3810 O GLU B 10 3973 3698 4712 396 498 403 O ATOM 3811 CB GLU B 10 20.150 14.469 127.958 1.00 30.94 C ANISOU 3811 CB GLU B 10 4020 2997 4739 469 558 217 C ATOM 3812 CG GLU B 10 20.506 12.960 127.871 1.00 32.98 C ANISOU 3812 CG GLU B 10 4346 3003 5182 522 554 209 C ATOM 3813 CD GLU B 10 21.738 12.598 128.708 1.00 39.49 C ANISOU 3813 CD GLU B 10 5025 3777 6204 651 571 310 C ATOM 3814 OE1 GLU B 10 22.327 13.520 129.329 1.00 33.72 O ANISOU 3814 OE1 GLU B 10 4143 3208 5461 687 571 377 O ATOM 3815 OE2 GLU B 10 22.117 11.402 128.743 1.00 39.68 O ANISOU 3815 OE2 GLU B 10 5087 3580 6409 720 554 319 O ATOM 3816 N CYS B 11 17.850 16.535 128.751 1.00 34.60 N ANISOU 3816 N CYS B 11 4360 3849 4937 256 403 312 N ATOM 3817 CA CYS B 11 17.288 17.875 128.779 1.00 32.44 C ANISOU 3817 CA CYS B 11 4038 3751 4536 230 386 299 C ATOM 3818 C CYS B 11 17.012 18.320 130.211 1.00 31.44 C ANISOU 3818 C CYS B 11 3777 3765 4402 201 398 439 C ATOM 3819 O CYS B 11 17.278 19.471 130.569 1.00 29.13 O ANISOU 3819 O CYS B 11 3446 3613 4010 235 426 445 O ATOM 3820 CB CYS B 11 16.011 17.925 127.954 1.00 30.28 C ANISOU 3820 CB CYS B 11 3817 3439 4247 150 267 216 C ATOM 3821 SG CYS B 11 15.317 19.599 127.899 1.00 41.30 S ANISOU 3821 SG CYS B 11 5153 5015 5526 151 222 192 S ATOM 3822 N VAL B 12 16.496 17.417 131.051 1.00 31.19 N ANISOU 3822 N VAL B 12 3711 3678 4460 133 390 551 N ATOM 3823 CA VAL B 12 16.219 17.772 132.443 1.00 33.49 C ANISOU 3823 CA VAL B 12 3949 4081 4694 100 440 686 C ATOM 3824 C VAL B 12 17.514 18.068 133.190 1.00 32.58 C ANISOU 3824 C VAL B 12 3867 4007 4506 192 428 751 C ATOM 3825 O VAL B 12 17.575 18.986 134.018 1.00 31.44 O ANISOU 3825 O VAL B 12 3721 3992 4234 201 443 793 O ATOM 3826 CB VAL B 12 15.402 16.657 133.126 1.00 40.48 C ANISOU 3826 CB VAL B 12 4834 4865 5682 -11 470 807 C ATOM 3827 CG1 VAL B 12 15.305 16.888 134.643 1.00 33.89 C ANISOU 3827 CG1 VAL B 12 4033 4112 4731 -38 561 963 C ATOM 3828 CG2 VAL B 12 14.010 16.576 132.504 1.00 34.38 C ANISOU 3828 CG2 VAL B 12 3960 4067 5036 -119 461 740 C ATOM 3829 N TYR B 13 18.569 17.299 132.917 1.00 29.71 N ANISOU 3829 N TYR B 13 3528 3515 4244 264 386 751 N ATOM 3830 CA TYR B 13 19.852 17.604 133.535 1.00 27.53 C ANISOU 3830 CA TYR B 13 3230 3258 3972 357 327 800 C ATOM 3831 C TYR B 13 20.371 18.958 133.069 1.00 32.66 C ANISOU 3831 C TYR B 13 3816 4034 4561 398 357 696 C ATOM 3832 O TYR B 13 20.947 19.722 133.857 1.00 28.94 O ANISOU 3832 O TYR B 13 3321 3645 4032 421 295 739 O ATOM 3833 CB TYR B 13 20.864 16.504 133.226 1.00 31.03 C ANISOU 3833 CB TYR B 13 3660 3516 4614 446 286 804 C ATOM 3834 CG TYR B 13 22.180 16.725 133.918 1.00 30.42 C ANISOU 3834 CG TYR B 13 3509 3430 4619 545 175 863 C ATOM 3835 CD1 TYR B 13 22.336 16.409 135.258 1.00 39.61 C ANISOU 3835 CD1 TYR B 13 4748 4568 5734 544 19 1030 C ATOM 3836 CD2 TYR B 13 23.265 17.265 133.239 1.00 35.55 C ANISOU 3836 CD2 TYR B 13 4022 4082 5403 630 219 757 C ATOM 3837 CE1 TYR B 13 23.545 16.606 135.903 1.00 44.30 C ANISOU 3837 CE1 TYR B 13 5275 5132 6424 635 -160 1084 C ATOM 3838 CE2 TYR B 13 24.481 17.463 133.877 1.00 33.44 C ANISOU 3838 CE2 TYR B 13 3630 3789 5286 712 83 807 C ATOM 3839 CZ TYR B 13 24.610 17.137 135.210 1.00 38.74 C ANISOU 3839 CZ TYR B 13 4370 4431 5918 717 -140 968 C ATOM 3840 OH TYR B 13 25.813 17.322 135.864 1.00 40.88 O ANISOU 3840 OH TYR B 13 4522 4654 6355 799 -351 1018 O ATOM 3841 N TYR B 14 20.190 19.268 131.783 1.00 29.14 N ANISOU 3841 N TYR B 14 3376 3581 4116 399 438 560 N ATOM 3842 CA TYR B 14 20.566 20.585 131.289 1.00 30.96 C ANISOU 3842 CA TYR B 14 3584 3909 4270 418 486 476 C ATOM 3843 C TYR B 14 19.825 21.691 132.043 1.00 31.30 C ANISOU 3843 C TYR B 14 3628 4104 4159 372 453 509 C ATOM 3844 O TYR B 14 20.434 22.694 132.443 1.00 32.80 O ANISOU 3844 O TYR B 14 3791 4370 4304 391 434 506 O ATOM 3845 CB TYR B 14 20.303 20.648 129.786 1.00 32.27 C ANISOU 3845 CB TYR B 14 3842 4015 4402 415 570 344 C ATOM 3846 CG TYR B 14 19.970 22.017 129.215 1.00 36.53 C ANISOU 3846 CG TYR B 14 4436 4649 4795 395 594 276 C ATOM 3847 CD1 TYR B 14 18.653 22.373 128.943 1.00 31.81 C ANISOU 3847 CD1 TYR B 14 3895 4092 4101 347 520 250 C ATOM 3848 CD2 TYR B 14 20.981 22.923 128.888 1.00 30.87 C ANISOU 3848 CD2 TYR B 14 3706 3952 4072 424 684 239 C ATOM 3849 CE1 TYR B 14 18.346 23.616 128.395 1.00 34.89 C ANISOU 3849 CE1 TYR B 14 4352 4536 4367 346 509 195 C ATOM 3850 CE2 TYR B 14 20.689 24.158 128.341 1.00 31.68 C ANISOU 3850 CE2 TYR B 14 3895 4108 4034 402 703 190 C ATOM 3851 CZ TYR B 14 19.370 24.503 128.100 1.00 38.47 C ANISOU 3851 CZ TYR B 14 4838 5003 4776 373 603 171 C ATOM 3852 OH TYR B 14 19.080 25.729 127.543 1.00 43.25 O ANISOU 3852 OH TYR B 14 5547 5634 5253 367 589 131 O ATOM 3853 N CYS B 15 18.512 21.522 132.259 1.00 26.16 N ANISOU 3853 N CYS B 15 2999 3483 3457 311 453 531 N ATOM 3854 CA CYS B 15 17.759 22.516 133.027 1.00 29.68 C ANISOU 3854 CA CYS B 15 3436 4056 3785 286 467 551 C ATOM 3855 C CYS B 15 18.274 22.613 134.452 1.00 32.71 C ANISOU 3855 C CYS B 15 3861 4481 4087 294 440 655 C ATOM 3856 O CYS B 15 18.216 23.678 135.068 1.00 34.67 O ANISOU 3856 O CYS B 15 4142 4820 4210 302 442 643 O ATOM 3857 CB CYS B 15 16.267 22.176 133.024 1.00 23.87 C ANISOU 3857 CB CYS B 15 2660 3320 3089 220 504 558 C ATOM 3858 SG CYS B 15 15.492 22.541 131.430 1.00 34.46 S ANISOU 3858 SG CYS B 15 3986 4624 4482 216 440 421 S ATOM 3859 N HIS B 16 18.787 21.511 134.985 1.00 30.57 N ANISOU 3859 N HIS B 16 3621 4120 3873 296 389 754 N ATOM 3860 CA HIS B 16 19.387 21.528 136.308 1.00 31.21 C ANISOU 3860 CA HIS B 16 3797 4207 3854 310 299 862 C ATOM 3861 C HIS B 16 20.637 22.404 136.354 1.00 31.08 C ANISOU 3861 C HIS B 16 3739 4215 3852 367 178 815 C ATOM 3862 O HIS B 16 20.885 23.059 137.370 1.00 33.54 O ANISOU 3862 O HIS B 16 4151 4575 4020 366 87 850 O ATOM 3863 CB HIS B 16 19.693 20.089 136.724 1.00 30.69 C ANISOU 3863 CB HIS B 16 3787 4001 3874 311 233 986 C ATOM 3864 CG HIS B 16 20.461 19.966 137.998 1.00 36.43 C ANISOU 3864 CG HIS B 16 4649 4690 4503 339 68 1111 C ATOM 3865 ND1 HIS B 16 19.918 20.276 139.227 1.00 43.92 N ANISOU 3865 ND1 HIS B 16 5803 5688 5197 289 89 1200 N ATOM 3866 CD2 HIS B 16 21.717 19.524 138.239 1.00 38.18 C ANISOU 3866 CD2 HIS B 16 4849 4806 4851 415 -138 1162 C ATOM 3867 CE1 HIS B 16 20.813 20.042 140.171 1.00 44.50 C ANISOU 3867 CE1 HIS B 16 6024 5686 5198 328 -131 1305 C ATOM 3868 NE2 HIS B 16 21.915 19.594 139.598 1.00 44.17 N ANISOU 3868 NE2 HIS B 16 5820 5550 5413 408 -295 1286 N ATOM 3869 N LEU B 17 21.427 22.436 135.276 1.00 26.92 N ANISOU 3869 N LEU B 17 3082 3644 3501 409 187 731 N ATOM 3870 CA LEU B 17 22.606 23.300 135.209 1.00 32.87 C ANISOU 3870 CA LEU B 17 3747 4407 4337 441 110 682 C ATOM 3871 C LEU B 17 22.295 24.708 134.719 1.00 30.53 C ANISOU 3871 C LEU B 17 3457 4205 3939 410 191 582 C ATOM 3872 O LEU B 17 23.137 25.604 134.880 1.00 28.73 O ANISOU 3872 O LEU B 17 3178 3987 3752 407 121 551 O ATOM 3873 CB LEU B 17 23.686 22.693 134.290 1.00 26.02 C ANISOU 3873 CB LEU B 17 2722 3425 3739 499 147 640 C ATOM 3874 CG LEU B 17 24.245 21.315 134.683 1.00 29.34 C ANISOU 3874 CG LEU B 17 3104 3710 4335 561 43 729 C ATOM 3875 CD1 LEU B 17 25.463 20.943 133.807 1.00 29.65 C ANISOU 3875 CD1 LEU B 17 2945 3629 4691 641 113 660 C ATOM 3876 CD2 LEU B 17 24.597 21.265 136.172 1.00 31.57 C ANISOU 3876 CD2 LEU B 17 3457 3983 4555 568 -211 856 C ATOM 3877 N ASP B 18 21.111 24.924 134.154 1.00 25.69 N ANISOU 3877 N ASP B 18 2900 3640 3221 385 307 535 N ATOM 3878 CA ASP B 18 20.821 26.097 133.346 1.00 26.79 C ANISOU 3878 CA ASP B 18 3054 3823 3303 375 376 440 C ATOM 3879 C ASP B 18 20.482 27.305 134.218 1.00 24.17 C ANISOU 3879 C ASP B 18 2790 3573 2822 365 332 429 C ATOM 3880 O ASP B 18 20.184 27.182 135.410 1.00 26.26 O ANISOU 3880 O ASP B 18 3123 3872 2981 361 285 486 O ATOM 3881 CB ASP B 18 19.647 25.806 132.414 1.00 25.67 C ANISOU 3881 CB ASP B 18 2948 3673 3133 366 451 395 C ATOM 3882 CG ASP B 18 19.564 26.787 131.268 1.00 31.84 C ANISOU 3882 CG ASP B 18 3785 4444 3870 369 492 306 C ATOM 3883 OD1 ASP B 18 20.631 27.344 130.883 1.00 26.81 O ANISOU 3883 OD1 ASP B 18 3143 3776 3268 368 531 280 O ATOM 3884 OD2 ASP B 18 18.440 27.004 130.773 1.00 24.86 O ANISOU 3884 OD2 ASP B 18 2946 3567 2932 368 477 269 O ATOM 3885 N ILE B 19 20.486 28.483 133.584 1.00 28.84 N ANISOU 3885 N ILE B 19 3400 4174 3382 362 362 352 N ATOM 3886 CA ILE B 19 20.008 29.701 134.238 1.00 23.63 C ANISOU 3886 CA ILE B 19 2823 3566 2588 366 337 316 C ATOM 3887 C ILE B 19 18.569 29.506 134.714 1.00 29.24 C ANISOU 3887 C ILE B 19 3567 4331 3211 388 402 323 C ATOM 3888 O ILE B 19 17.815 28.667 134.198 1.00 28.10 O ANISOU 3888 O ILE B 19 3367 4178 3132 386 454 340 O ATOM 3889 CB ILE B 19 20.071 30.906 133.284 1.00 25.83 C ANISOU 3889 CB ILE B 19 3135 3814 2864 363 365 241 C ATOM 3890 CG1 ILE B 19 19.119 30.674 132.097 1.00 23.84 C ANISOU 3890 CG1 ILE B 19 2903 3541 2614 385 424 213 C ATOM 3891 CG2 ILE B 19 21.505 31.189 132.836 1.00 22.99 C ANISOU 3891 CG2 ILE B 19 2721 3389 2625 318 360 235 C ATOM 3892 CD1 ILE B 19 19.060 31.818 131.073 1.00 27.54 C ANISOU 3892 CD1 ILE B 19 3472 3952 3040 388 432 158 C ATOM 3893 N ILE B 20 18.176 30.319 135.687 1.00 26.31 N ANISOU 3893 N ILE B 20 3285 3999 2711 406 411 300 N ATOM 3894 CA ILE B 20 16.765 30.508 136.004 1.00 29.72 C ANISOU 3894 CA ILE B 20 3719 4471 3105 440 532 275 C ATOM 3895 C ILE B 20 16.244 31.601 135.073 1.00 36.81 C ANISOU 3895 C ILE B 20 4588 5346 4053 488 524 185 C ATOM 3896 O ILE B 20 16.651 32.766 135.171 1.00 30.92 O ANISOU 3896 O ILE B 20 3930 4578 3242 508 479 128 O ATOM 3897 CB ILE B 20 16.540 30.882 137.472 1.00 36.04 C ANISOU 3897 CB ILE B 20 4667 5301 3724 453 595 278 C ATOM 3898 CG1 ILE B 20 17.093 29.810 138.403 1.00 41.07 C ANISOU 3898 CG1 ILE B 20 5398 5933 4273 406 559 388 C ATOM 3899 CG2 ILE B 20 15.056 31.012 137.735 1.00 42.97 C ANISOU 3899 CG2 ILE B 20 5495 6207 4623 493 791 246 C ATOM 3900 CD1 ILE B 20 16.489 28.420 138.165 1.00 43.35 C ANISOU 3900 CD1 ILE B 20 5584 6215 4673 371 651 477 C ATOM 3901 N TRP B 21 15.368 31.217 134.153 1.00 34.26 N ANISOU 3901 N TRP B 21 4160 5006 3852 502 535 175 N ATOM 3902 CA TRP B 21 14.740 32.148 133.219 1.00 37.30 C ANISOU 3902 CA TRP B 21 4538 5345 4291 559 477 104 C ATOM 3903 C TRP B 21 13.596 31.427 132.520 1.00 40.33 C ANISOU 3903 C TRP B 21 4787 5706 4830 566 448 105 C ATOM 3904 O TRP B 21 13.793 30.291 132.094 1.00 35.10 O ANISOU 3904 O TRP B 21 4098 5028 4211 507 427 147 O ATOM 3905 CB TRP B 21 15.737 32.655 132.176 1.00 30.22 C ANISOU 3905 CB TRP B 21 3750 4382 3352 536 389 92 C ATOM 3906 CG TRP B 21 15.095 33.447 131.066 1.00 32.24 C ANISOU 3906 CG TRP B 21 4062 4558 3630 588 297 46 C ATOM 3907 CD1 TRP B 21 14.843 33.017 129.795 1.00 32.80 C ANISOU 3907 CD1 TRP B 21 4179 4561 3724 579 208 48 C ATOM 3908 CD2 TRP B 21 14.617 34.798 131.134 1.00 31.60 C ANISOU 3908 CD2 TRP B 21 4038 4432 3538 664 254 -7 C ATOM 3909 NE1 TRP B 21 14.244 34.012 129.070 1.00 30.79 N ANISOU 3909 NE1 TRP B 21 4018 4221 3462 643 88 13 N ATOM 3910 CE2 TRP B 21 14.092 35.117 129.867 1.00 33.95 C ANISOU 3910 CE2 TRP B 21 4408 4631 3861 701 118 -19 C ATOM 3911 CE3 TRP B 21 14.591 35.768 132.140 1.00 33.93 C ANISOU 3911 CE3 TRP B 21 4362 4738 3792 710 306 -52 C ATOM 3912 CZ2 TRP B 21 13.538 36.369 129.578 1.00 29.25 C ANISOU 3912 CZ2 TRP B 21 3889 3944 3279 791 19 -59 C ATOM 3913 CZ3 TRP B 21 14.034 37.006 131.853 1.00 32.13 C ANISOU 3913 CZ3 TRP B 21 4199 4421 3586 800 238 -109 C ATOM 3914 CH2 TRP B 21 13.512 37.294 130.584 1.00 29.97 C ANISOU 3914 CH2 TRP B 21 3973 4047 3367 843 91 -105 C ATOM 3915 OXT TRP B 21 12.494 31.956 132.362 1.00 33.96 O ANISOU 3915 OXT TRP B 21 3891 4878 4135 632 427 57 O TER 3916 TRP B 21 HETATM 3917 C18 OLC A1201 34.062 48.966 144.836 1.00 92.85 C HETATM 3918 C10 OLC A1201 34.509 44.878 142.412 1.00 83.21 C HETATM 3919 C9 OLC A1201 34.118 43.617 142.241 1.00 79.59 C HETATM 3920 C17 OLC A1201 32.955 49.693 144.101 1.00 92.38 C HETATM 3921 C11 OLC A1201 34.675 45.821 141.243 1.00 82.34 C HETATM 3922 C8 OLC A1201 33.834 43.074 140.861 1.00 75.16 C HETATM 3923 C24 OLC A1201 34.585 30.116 141.100 1.00 75.25 C HETATM 3924 C16 OLC A1201 33.508 50.769 143.169 1.00 90.70 C HETATM 3925 C12 OLC A1201 34.085 47.164 141.654 1.00 84.43 C HETATM 3926 C7 OLC A1201 34.853 41.986 140.550 1.00 72.06 C HETATM 3927 C15 OLC A1201 34.339 50.163 142.040 1.00 89.87 C HETATM 3928 C13 OLC A1201 34.080 48.177 140.517 1.00 86.59 C HETATM 3929 C6 OLC A1201 34.982 41.014 141.720 1.00 66.18 C HETATM 3930 C14 OLC A1201 33.460 49.486 140.994 1.00 87.07 C HETATM 3931 C5 OLC A1201 35.610 39.715 141.242 1.00 70.21 C HETATM 3932 C4 OLC A1201 35.076 38.504 141.999 1.00 70.30 C HETATM 3933 C3 OLC A1201 35.581 37.251 141.299 1.00 72.67 C HETATM 3934 C2 OLC A1201 35.055 35.968 141.923 1.00 74.07 C HETATM 3935 C21 OLC A1201 34.432 32.553 140.513 1.00 71.87 C HETATM 3936 C1 OLC A1201 35.309 34.848 140.940 1.00 76.64 C HETATM 3937 C22 OLC A1201 35.201 31.259 140.311 1.00 75.83 C HETATM 3938 O19 OLC A1201 35.617 35.110 139.790 1.00 76.57 O HETATM 3939 O25 OLC A1201 34.947 28.888 140.451 1.00 76.52 O HETATM 3940 O23 OLC A1201 35.123 30.908 138.930 1.00 85.79 O HETATM 3941 O20 OLC A1201 35.181 33.450 141.330 1.00 79.78 O HETATM 3942 C18 OLC A1202 13.021 36.944 147.052 1.00 67.80 C HETATM 3943 C10 OLC A1202 21.193 33.364 146.618 1.00 64.49 C HETATM 3944 C9 OLC A1202 22.500 33.252 146.384 1.00 68.51 C HETATM 3945 C17 OLC A1202 14.316 37.689 146.800 1.00 69.28 C HETATM 3946 C11 OLC A1202 20.424 34.653 146.467 1.00 67.79 C HETATM 3947 C8 OLC A1202 23.396 34.394 145.958 1.00 70.28 C HETATM 3948 C24 OLC A1202 31.566 25.686 144.961 1.00 84.57 C HETATM 3949 C16 OLC A1202 15.436 36.722 146.426 1.00 73.65 C HETATM 3950 C12 OLC A1202 19.026 34.273 145.993 1.00 69.70 C HETATM 3951 C7 OLC A1202 24.843 33.902 146.017 1.00 69.27 C HETATM 3952 C15 OLC A1202 16.796 37.409 146.492 1.00 74.30 C HETATM 3953 C13 OLC A1202 17.946 35.174 146.585 1.00 75.27 C HETATM 3954 C6 OLC A1202 25.864 34.816 145.335 1.00 60.64 C HETATM 3955 C14 OLC A1202 17.882 36.528 145.884 1.00 74.85 C HETATM 3956 C5 OLC A1202 27.110 34.002 145.001 1.00 59.96 C HETATM 3957 C4 OLC A1202 27.375 32.936 146.063 1.00 61.96 C HETATM 3958 C3 OLC A1202 28.220 31.780 145.536 1.00 63.91 C HETATM 3959 C2 OLC A1202 28.347 30.635 146.542 1.00 68.32 C HETATM 3960 C21 OLC A1202 30.288 27.566 145.954 1.00 80.40 C HETATM 3961 C1 OLC A1202 28.588 29.365 145.758 1.00 78.40 C HETATM 3962 C22 OLC A1202 30.223 26.089 145.560 1.00 84.95 C HETATM 3963 O19 OLC A1202 28.430 29.401 144.553 1.00 90.00 O HETATM 3964 O25 OLC A1202 31.572 24.268 144.766 1.00 85.26 O HETATM 3965 O23 OLC A1202 29.957 25.240 146.685 1.00 88.66 O HETATM 3966 O20 OLC A1202 29.031 28.111 146.364 1.00 74.53 O HETATM 3967 C18 OLC A1203 -1.828 38.404 141.298 1.00 71.73 C HETATM 3968 C10 OLC A1203 0.919 44.546 142.231 1.00 71.28 C HETATM 3969 C9 OLC A1203 1.625 45.509 142.815 1.00 71.12 C HETATM 3970 C17 OLC A1203 -3.271 38.777 141.039 1.00 70.84 C HETATM 3971 C11 OLC A1203 0.704 43.237 142.948 1.00 75.79 C HETATM 3972 C8 OLC A1203 1.843 46.825 142.109 1.00 70.73 C HETATM 3973 C24 OLC A1203 6.418 56.425 141.800 1.00 73.65 C HETATM 3974 C16 OLC A1203 -3.380 40.246 140.654 1.00 75.61 C HETATM 3975 C12 OLC A1203 -0.782 43.095 143.256 1.00 75.47 C HETATM 3976 C7 OLC A1203 1.020 47.904 142.810 1.00 74.25 C HETATM 3977 C15 OLC A1203 -2.791 41.153 141.730 1.00 76.65 C HETATM 3978 C13 OLC A1203 -1.612 43.351 142.005 1.00 72.57 C HETATM 3979 C6 OLC A1203 1.407 49.302 142.339 1.00 70.72 C HETATM 3980 C14 OLC A1203 -1.742 42.097 141.151 1.00 75.72 C HETATM 3981 C5 OLC A1203 2.786 49.693 142.857 1.00 67.84 C HETATM 3982 C4 OLC A1203 3.323 50.885 142.081 1.00 60.11 C HETATM 3983 C3 OLC A1203 4.786 51.173 142.397 1.00 54.87 C HETATM 3984 C2 OLC A1203 5.285 52.180 141.369 1.00 59.71 C HETATM 3985 C21 OLC A1203 8.168 54.683 141.523 1.00 74.31 C HETATM 3986 C1 OLC A1203 6.652 52.724 141.690 1.00 68.77 C HETATM 3987 C22 OLC A1203 7.830 56.149 141.297 1.00 72.42 C HETATM 3988 O19 OLC A1203 7.338 52.247 142.574 1.00 77.55 O HETATM 3989 O25 OLC A1203 6.268 57.821 142.082 1.00 79.92 O HETATM 3990 O23 OLC A1203 8.755 56.943 142.040 1.00 75.25 O HETATM 3991 O20 OLC A1203 7.160 53.861 140.945 1.00 75.42 O HETATM 3992 C18 OLC A1204 7.303 43.216 141.004 1.00 64.61 C HETATM 3993 C10 OLC A1204 1.000 39.779 144.432 1.00 82.79 C HETATM 3994 C9 OLC A1204 0.462 38.733 143.808 1.00 80.84 C HETATM 3995 C17 OLC A1204 7.532 43.550 142.458 1.00 65.32 C HETATM 3996 C11 OLC A1204 2.446 39.792 144.876 1.00 81.52 C HETATM 3997 C8 OLC A1204 1.260 37.481 143.523 1.00 80.34 C HETATM 3998 C24 OLC A1204 0.893 24.185 142.337 1.00 90.94 C HETATM 3999 C16 OLC A1204 6.347 43.107 143.303 1.00 63.09 C HETATM 4000 C12 OLC A1204 2.864 41.234 145.148 1.00 76.58 C HETATM 4001 C7 OLC A1204 0.337 36.268 143.564 1.00 76.12 C HETATM 4002 C15 OLC A1204 6.240 41.587 143.289 1.00 68.25 C HETATM 4003 C13 OLC A1204 3.866 41.732 144.115 1.00 71.47 C HETATM 4004 C6 OLC A1204 1.120 34.964 143.441 1.00 76.54 C HETATM 4005 C14 OLC A1204 5.232 41.090 144.320 1.00 70.38 C HETATM 4006 C5 OLC A1204 0.405 33.965 142.534 1.00 73.70 C HETATM 4007 C4 OLC A1204 -0.194 32.804 143.319 1.00 74.73 C HETATM 4008 C3 OLC A1204 0.746 31.603 143.398 1.00 76.85 C HETATM 4009 C2 OLC A1204 0.291 30.487 142.462 1.00 81.50 C HETATM 4010 C21 OLC A1204 1.009 26.665 142.640 1.00 89.94 C HETATM 4011 C1 OLC A1204 0.856 29.157 142.906 1.00 85.43 C HETATM 4012 C22 OLC A1204 0.276 25.523 141.940 1.00 92.44 C HETATM 4013 O19 OLC A1204 1.664 29.104 143.817 1.00 85.84 O HETATM 4014 O25 OLC A1204 0.665 23.951 143.732 1.00 90.06 O HETATM 4015 O23 OLC A1204 -1.103 25.532 142.326 1.00 93.33 O HETATM 4016 O20 OLC A1204 0.441 27.919 142.255 1.00 87.98 O HETATM 4017 C18 OLC A1205 25.372 41.939 120.420 1.00 63.29 C HETATM 4018 C10 OLC A1205 25.677 33.621 118.896 1.00 73.57 C HETATM 4019 C9 OLC A1205 25.930 32.572 118.116 1.00 71.90 C HETATM 4020 C17 OLC A1205 24.094 41.170 120.173 1.00 64.42 C HETATM 4021 C11 OLC A1205 24.367 33.751 119.635 1.00 78.13 C HETATM 4022 C8 OLC A1205 24.912 31.473 117.907 1.00 70.07 C HETATM 4023 C24 OLC A1205 21.382 20.896 114.927 1.00 81.28 C HETATM 4024 C16 OLC A1205 24.277 40.118 119.079 1.00 70.81 C HETATM 4025 C12 OLC A1205 23.772 35.140 119.413 1.00 83.93 C HETATM 4026 C7 OLC A1205 25.028 30.973 116.473 1.00 67.68 C HETATM 4027 C15 OLC A1205 24.943 38.844 119.595 1.00 76.57 C HETATM 4028 C13 OLC A1205 24.703 36.304 119.753 1.00 84.25 C HETATM 4029 C6 OLC A1205 24.319 29.640 116.264 1.00 64.51 C HETATM 4030 C14 OLC A1205 24.124 37.613 119.209 1.00 80.45 C HETATM 4031 C5 OLC A1205 25.195 28.465 116.687 1.00 64.20 C HETATM 4032 C4 OLC A1205 24.567 27.157 116.219 1.00 65.43 C HETATM 4033 C3 OLC A1205 25.340 25.941 116.717 1.00 70.33 C HETATM 4034 C2 OLC A1205 24.843 24.689 116.006 1.00 75.70 C HETATM 4035 C21 OLC A1205 23.358 22.212 115.649 1.00 82.20 C HETATM 4036 C1 OLC A1205 25.174 23.460 116.819 1.00 85.83 C HETATM 4037 C22 OLC A1205 22.443 21.048 116.009 1.00 81.52 C HETATM 4038 O19 OLC A1205 25.979 23.500 117.742 1.00 89.81 O HETATM 4039 O25 OLC A1205 20.348 20.017 115.388 1.00 82.34 O HETATM 4040 O23 OLC A1205 23.210 19.841 116.110 1.00 84.36 O HETATM 4041 O20 OLC A1205 24.499 22.210 116.507 1.00 85.56 O HETATM 4042 C18 OLC A1206 15.188 49.070 113.712 1.00 71.16 C HETATM 4043 C10 OLC A1206 11.599 42.552 115.628 1.00 69.53 C HETATM 4044 C9 OLC A1206 12.756 41.914 115.471 1.00 73.05 C HETATM 4045 C17 OLC A1206 14.071 48.551 114.592 1.00 72.32 C HETATM 4046 C11 OLC A1206 11.569 43.974 116.127 1.00 63.89 C HETATM 4047 C8 OLC A1206 14.067 42.586 115.802 1.00 73.95 C HETATM 4048 C24 OLC A1206 13.145 31.594 113.470 1.00109.37 C HETATM 4049 C16 OLC A1206 12.775 48.413 113.800 1.00 68.75 C HETATM 4050 C12 OLC A1206 10.351 44.678 115.543 1.00 64.47 C HETATM 4051 C7 OLC A1206 15.121 41.503 115.994 1.00 76.19 C HETATM 4052 C15 OLC A1206 11.595 48.205 114.740 1.00 67.89 C HETATM 4053 C13 OLC A1206 10.747 45.853 114.659 1.00 64.23 C HETATM 4054 C6 OLC A1206 15.116 40.555 114.799 1.00 80.63 C HETATM 4055 C14 OLC A1206 11.630 46.838 115.411 1.00 67.72 C HETATM 4056 C5 OLC A1206 16.334 39.640 114.798 1.00 78.98 C HETATM 4057 C4 OLC A1206 16.313 38.707 116.001 1.00 80.60 C HETATM 4058 C3 OLC A1206 16.339 37.245 115.569 1.00 81.32 C HETATM 4059 C2 OLC A1206 14.989 36.804 115.017 1.00 84.96 C HETATM 4060 C21 OLC A1206 13.933 33.913 113.045 1.00104.27 C HETATM 4061 C1 OLC A1206 14.997 35.304 114.822 1.00 90.64 C HETATM 4062 C22 OLC A1206 12.773 32.937 112.855 1.00109.63 C HETATM 4063 O19 OLC A1206 15.992 34.650 115.096 1.00 90.74 O HETATM 4064 O25 OLC A1206 13.382 31.770 114.870 1.00109.12 O HETATM 4065 O23 OLC A1206 11.583 33.431 113.483 1.00113.29 O HETATM 4066 O20 OLC A1206 13.827 34.628 114.277 1.00 96.81 O HETATM 4067 C18 OLC A1207 31.312 47.172 124.607 1.00 84.76 C HETATM 4068 C10 OLC A1207 32.056 38.335 122.752 1.00 90.96 C HETATM 4069 C9 OLC A1207 32.057 37.250 121.976 1.00 85.35 C HETATM 4070 C17 OLC A1207 31.569 45.907 123.812 1.00 88.83 C HETATM 4071 C11 OLC A1207 33.281 39.180 123.024 1.00 94.21 C HETATM 4072 C8 OLC A1207 33.290 36.717 121.283 1.00 81.96 C HETATM 4073 C24 OLC A1207 32.290 24.360 120.608 1.00 80.54 C HETATM 4074 C16 OLC A1207 31.863 44.722 124.729 1.00 88.88 C HETATM 4075 C12 OLC A1207 32.828 40.620 123.268 1.00 95.72 C HETATM 4076 C7 OLC A1207 33.155 35.199 121.186 1.00 80.20 C HETATM 4077 C15 OLC A1207 32.594 43.605 123.989 1.00 89.03 C HETATM 4078 C13 OLC A1207 33.750 41.366 124.230 1.00 93.36 C HETATM 4079 C6 OLC A1207 33.631 34.661 119.839 1.00 79.87 C HETATM 4080 C14 OLC A1207 33.013 42.494 124.948 1.00 89.86 C HETATM 4081 C5 OLC A1207 32.866 33.399 119.441 1.00 78.32 C HETATM 4082 C4 OLC A1207 32.663 32.484 120.643 1.00 77.82 C HETATM 4083 C3 OLC A1207 31.811 31.266 120.300 1.00 77.87 C HETATM 4084 C2 OLC A1207 32.503 30.412 119.250 1.00 79.15 C HETATM 4085 C21 OLC A1207 32.741 26.723 120.031 1.00 77.24 C HETATM 4086 C1 OLC A1207 32.033 28.977 119.344 1.00 81.25 C HETATM 4087 C22 OLC A1207 31.930 25.804 120.931 1.00 82.75 C HETATM 4088 O19 OLC A1207 31.264 28.525 118.515 1.00 86.13 O HETATM 4089 O25 OLC A1207 31.947 23.520 121.713 1.00 80.10 O HETATM 4090 O23 OLC A1207 32.221 26.093 122.303 1.00 91.42 O HETATM 4091 O20 OLC A1207 32.500 28.082 120.388 1.00 79.89 O HETATM 4092 C18 OLC A1208 43.011 32.442 132.459 1.00 60.38 C HETATM 4093 C10 OLC A1208 37.452 37.521 127.437 1.00 77.20 C HETATM 4094 C9 OLC A1208 36.785 37.185 126.324 1.00 72.09 C HETATM 4095 C17 OLC A1208 41.623 33.013 132.248 1.00 60.40 C HETATM 4096 C11 OLC A1208 38.036 36.465 128.358 1.00 79.79 C HETATM 4097 C8 OLC A1208 36.588 35.732 125.937 1.00 66.86 C HETATM 4098 C24 OLC A1208 31.948 24.336 126.618 1.00 80.72 C HETATM 4099 C16 OLC A1208 41.247 33.068 130.769 1.00 55.07 C HETATM 4100 C12 OLC A1208 39.515 36.696 128.689 1.00 73.36 C HETATM 4101 C7 OLC A1208 35.317 35.513 125.119 1.00 59.71 C HETATM 4102 C15 OLC A1208 42.098 34.059 129.978 1.00 56.75 C HETATM 4103 C13 OLC A1208 40.240 35.353 128.835 1.00 64.89 C HETATM 4104 C6 OLC A1208 34.321 34.619 125.854 1.00 55.50 C HETATM 4105 C14 OLC A1208 41.417 35.417 129.804 1.00 61.20 C HETATM 4106 C5 OLC A1208 33.380 33.896 124.889 1.00 57.06 C HETATM 4107 C4 OLC A1208 32.572 32.824 125.627 1.00 67.01 C HETATM 4108 C3 OLC A1208 32.423 31.514 124.843 1.00 71.55 C HETATM 4109 C2 OLC A1208 32.543 30.291 125.757 1.00 70.21 C HETATM 4110 C21 OLC A1208 31.831 26.611 125.602 1.00 78.24 C HETATM 4111 C1 OLC A1208 32.313 28.984 125.020 1.00 72.82 C HETATM 4112 C22 OLC A1208 32.528 25.260 125.555 1.00 82.55 C HETATM 4113 O19 OLC A1208 31.745 28.970 123.941 1.00 74.56 O HETATM 4114 O25 OLC A1208 31.724 23.030 126.068 1.00 83.70 O HETATM 4115 O23 OLC A1208 32.273 24.671 124.278 1.00 92.27 O HETATM 4116 O20 OLC A1208 32.740 27.711 125.598 1.00 74.97 O HETATM 4117 C10 OLC A1209 1.447 34.140 128.379 1.00 53.18 C HETATM 4118 C9 OLC A1209 1.099 35.005 129.323 1.00 55.57 C HETATM 4119 C11 OLC A1209 0.405 33.381 127.613 1.00 55.02 C HETATM 4120 C8 OLC A1209 -0.341 35.249 129.683 1.00 52.69 C HETATM 4121 C24 OLC A1209 -3.959 27.240 135.617 1.00 96.26 C HETATM 4122 C12 OLC A1209 0.944 33.103 126.215 1.00 51.53 C HETATM 4123 C7 OLC A1209 -0.372 35.929 131.046 1.00 49.02 C HETATM 4124 C13 OLC A1209 2.040 32.048 126.249 1.00 52.78 C HETATM 4125 C6 OLC A1209 -1.663 35.625 131.796 1.00 57.54 C HETATM 4126 C5 OLC A1209 -1.585 36.170 133.215 1.00 60.65 C HETATM 4127 C4 OLC A1209 -2.796 35.774 134.053 1.00 65.33 C HETATM 4128 C3 OLC A1209 -2.589 34.441 134.764 1.00 72.60 C HETATM 4129 C2 OLC A1209 -3.203 33.266 134.005 1.00 78.68 C HETATM 4130 C21 OLC A1209 -3.418 29.625 135.078 1.00 99.08 C HETATM 4131 C1 OLC A1209 -3.369 32.118 134.974 1.00 87.40 C HETATM 4132 C22 OLC A1209 -4.537 28.617 135.300 1.00100.10 C HETATM 4133 O19 OLC A1209 -2.998 32.246 136.128 1.00 88.19 O HETATM 4134 O25 OLC A1209 -3.574 27.141 136.994 1.00 93.48 O HETATM 4135 O23 OLC A1209 -5.325 29.070 136.405 1.00106.30 O HETATM 4136 O20 OLC A1209 -3.952 30.847 134.563 1.00 95.12 O HETATM 4137 C18 OLC A1210 25.751 42.765 123.976 1.00 69.85 C HETATM 4138 C10 OLC A1210 26.902 50.222 127.434 1.00 67.92 C HETATM 4139 C9 OLC A1210 26.768 51.194 128.334 1.00 63.83 C HETATM 4140 C17 OLC A1210 25.990 44.245 123.749 1.00 72.98 C HETATM 4141 C11 OLC A1210 26.751 48.768 127.803 1.00 65.64 C HETATM 4142 C8 OLC A1210 26.925 52.610 127.845 1.00 60.76 C HETATM 4143 C24 OLC A1210 26.547 63.318 121.893 1.00102.44 C HETATM 4144 C16 OLC A1210 26.977 44.800 124.770 1.00 70.39 C HETATM 4145 C12 OLC A1210 25.577 48.197 127.016 1.00 63.35 C HETATM 4146 C7 OLC A1210 25.688 52.898 127.006 1.00 64.55 C HETATM 4147 C15 OLC A1210 27.072 46.321 124.730 1.00 65.36 C HETATM 4148 C13 OLC A1210 25.785 48.339 125.513 1.00 57.82 C HETATM 4149 C6 OLC A1210 25.497 54.384 126.731 1.00 66.37 C HETATM 4150 C14 OLC A1210 25.702 46.981 124.818 1.00 56.45 C HETATM 4151 C5 OLC A1210 26.446 54.892 125.654 1.00 71.26 C HETATM 4152 C4 OLC A1210 26.017 56.288 125.220 1.00 81.82 C HETATM 4153 C3 OLC A1210 26.980 56.879 124.199 1.00 88.75 C HETATM 4154 C2 OLC A1210 27.406 58.294 124.583 1.00 94.51 C HETATM 4155 C21 OLC A1210 25.740 61.644 123.545 1.00100.93 C HETATM 4156 C1 OLC A1210 26.380 59.301 124.116 1.00101.16 C HETATM 4157 C22 OLC A1210 26.362 63.024 123.378 1.00 99.06 C HETATM 4158 O19 OLC A1210 25.258 58.942 123.800 1.00105.70 O HETATM 4159 O25 OLC A1210 27.179 62.204 121.250 1.00103.57 O HETATM 4160 O23 OLC A1210 25.491 64.003 123.955 1.00 98.53 O HETATM 4161 O20 OLC A1210 26.716 60.715 124.021 1.00102.66 O HETATM 4162 C10 OLC A1211 5.206 40.899 117.451 1.00 77.22 C HETATM 4163 C9 OLC A1211 5.595 39.858 116.716 1.00 80.29 C HETATM 4164 C11 OLC A1211 5.760 42.278 117.176 1.00 76.73 C HETATM 4165 C8 OLC A1211 6.608 40.041 115.609 1.00 82.80 C HETATM 4166 C24 OLC A1211 8.450 29.192 114.060 1.00 91.48 C HETATM 4167 C12 OLC A1211 4.779 43.330 117.680 1.00 74.03 C HETATM 4168 C7 OLC A1211 7.632 38.917 115.681 1.00 78.90 C HETATM 4169 C6 OLC A1211 6.934 37.587 115.455 1.00 77.95 C HETATM 4170 C5 OLC A1211 7.075 36.663 116.656 1.00 81.15 C HETATM 4171 C4 OLC A1211 6.029 35.559 116.557 1.00 87.75 C HETATM 4172 C3 OLC A1211 6.309 34.418 117.527 1.00 95.22 C HETATM 4173 C2 OLC A1211 5.542 33.157 117.134 1.00 98.97 C HETATM 4174 C21 OLC A1211 7.098 29.993 115.967 1.00 96.92 C HETATM 4175 C1 OLC A1211 6.359 32.354 116.148 1.00101.11 C HETATM 4176 C22 OLC A1211 7.097 29.075 114.752 1.00 94.08 C HETATM 4177 O19 OLC A1211 7.315 32.857 115.578 1.00104.05 O HETATM 4178 O25 OLC A1211 8.867 30.564 114.068 1.00 91.51 O HETATM 4179 O23 OLC A1211 6.890 27.721 115.173 1.00 93.01 O HETATM 4180 O20 OLC A1211 6.048 30.955 115.888 1.00 98.05 O HETATM 4181 C10 OLC A1212 2.537 39.217 122.501 1.00 74.39 C HETATM 4182 C9 OLC A1212 2.576 37.896 122.361 1.00 74.81 C HETATM 4183 C11 OLC A1212 1.494 40.024 121.768 1.00 73.99 C HETATM 4184 C8 OLC A1212 1.592 37.170 121.471 1.00 73.65 C HETATM 4185 C24 OLC A1212 6.473 25.469 119.642 1.00 95.38 C HETATM 4186 C12 OLC A1212 0.832 40.986 122.745 1.00 72.14 C HETATM 4187 C7 OLC A1212 2.256 35.952 120.826 1.00 70.93 C HETATM 4188 C6 OLC A1212 2.497 34.830 121.834 1.00 66.81 C HETATM 4189 C5 OLC A1212 3.399 33.738 121.265 1.00 61.64 C HETATM 4190 C4 OLC A1212 2.596 32.588 120.660 1.00 65.17 C HETATM 4191 C3 OLC A1212 3.505 31.503 120.085 1.00 74.18 C HETATM 4192 C2 OLC A1212 2.713 30.256 119.698 1.00 81.15 C HETATM 4193 C21 OLC A1212 4.319 26.778 119.531 1.00 96.13 C HETATM 4194 C1 OLC A1212 3.621 29.159 119.181 1.00 90.68 C HETATM 4195 C22 OLC A1212 5.759 26.671 119.034 1.00 99.62 C HETATM 4196 O19 OLC A1212 3.960 29.141 118.008 1.00 94.79 O HETATM 4197 O25 OLC A1212 7.852 25.503 119.247 1.00 91.02 O HETATM 4198 O23 OLC A1212 5.748 26.528 117.608 1.00106.19 O HETATM 4199 O20 OLC A1212 4.089 28.089 120.053 1.00 93.62 O HETATM 4200 C1 CIT A1213 27.986 81.978 90.370 1.00 97.87 C HETATM 4201 O1 CIT A1213 28.246 80.827 89.961 1.00 95.47 O HETATM 4202 O2 CIT A1213 28.704 82.478 91.264 1.00 98.39 O HETATM 4203 C2 CIT A1213 26.837 82.769 89.784 1.00100.12 C HETATM 4204 C3 CIT A1213 25.514 81.999 89.740 1.00103.09 C HETATM 4205 O7 CIT A1213 25.586 81.068 88.629 1.00 99.66 O HETATM 4206 C4 CIT A1213 25.124 81.172 90.972 1.00 99.78 C HETATM 4207 C5 CIT A1213 25.468 81.786 92.310 1.00101.03 C HETATM 4208 O3 CIT A1213 25.434 83.025 92.504 1.00101.16 O HETATM 4209 O4 CIT A1213 25.788 81.038 93.261 1.00 99.88 O HETATM 4210 C6 CIT A1213 24.402 82.993 89.443 1.00111.21 C HETATM 4211 O5 CIT A1213 24.101 83.264 88.260 1.00115.01 O HETATM 4212 O6 CIT A1213 23.794 83.572 90.371 1.00113.52 O HETATM 4213 O HOH A1301 17.919 19.746 146.821 1.00 52.97 O HETATM 4214 O HOH A1302 -11.082 91.269 112.746 1.00 55.28 O HETATM 4215 O HOH A1303 27.196 83.627 93.994 1.00 61.94 O HETATM 4216 O HOH A1304 9.986 79.359 119.195 1.00 59.94 O HETATM 4217 O HOH A1305 30.606 84.057 105.366 1.00 59.11 O HETATM 4218 O HOH A1306 9.066 26.631 126.667 1.00 56.50 O HETATM 4219 O HOH A1307 11.410 27.982 149.213 1.00 57.07 O HETATM 4220 O HOH A1308 3.876 57.882 128.870 1.00 48.53 O HETATM 4221 O HOH A1309 16.322 46.470 133.795 1.00 41.11 O HETATM 4222 O HOH A1310 21.695 66.385 107.457 1.00 42.36 O HETATM 4223 O HOH A1311 9.668 90.560 111.617 1.00 48.27 O HETATM 4224 O HOH A1312 4.030 81.579 107.733 1.00 25.73 O HETATM 4225 O HOH A1313 30.080 7.126 120.854 1.00 28.64 O HETATM 4226 O HOH A1314 19.127 20.448 143.890 1.00 44.51 O HETATM 4227 O HOH A1315 7.110 34.492 131.290 1.00 44.24 O HETATM 4228 O HOH A1316 2.445 75.014 93.294 1.00 58.39 O HETATM 4229 O HOH A1317 17.361 50.526 127.815 1.00 44.61 O HETATM 4230 O HOH A1318 13.407 80.376 117.160 1.00 46.14 O HETATM 4231 O HOH A1319 -4.021 85.999 101.966 1.00 58.45 O HETATM 4232 O HOH A1320 12.690 30.464 129.208 1.00 45.86 O HETATM 4233 O HOH A1321 15.299 75.575 118.308 1.00 50.50 O HETATM 4234 O HOH A1322 3.454 23.294 140.749 1.00 53.50 O HETATM 4235 O HOH A1323 6.522 75.769 90.990 1.00 51.34 O HETATM 4236 O HOH A1324 3.130 77.028 119.100 1.00 47.68 O HETATM 4237 O HOH A1325 25.325 13.424 128.962 1.00 36.59 O HETATM 4238 O HOH A1326 28.360 34.121 136.678 1.00 40.97 O HETATM 4239 O HOH A1327 25.271 34.787 133.928 1.00 34.53 O HETATM 4240 O HOH A1328 30.840 80.740 102.416 1.00 51.35 O HETATM 4241 O HOH A1329 32.361 62.960 132.402 1.00 74.46 O HETATM 4242 O HOH A1330 4.163 70.745 114.005 1.00 55.17 O HETATM 4243 O HOH A1331 20.715 38.864 126.679 1.00 24.58 O HETATM 4244 O HOH A1332 23.427 6.889 123.369 1.00 35.42 O HETATM 4245 O HOH A1333 9.296 67.641 129.907 1.00 58.33 O HETATM 4246 O HOH A1334 8.663 89.465 106.781 1.00 53.42 O HETATM 4247 O HOH A1335 7.988 81.633 95.851 1.00 54.45 O HETATM 4248 O HOH A1336 7.674 87.501 110.214 1.00 36.84 O HETATM 4249 O HOH A1337 22.336 66.820 97.360 1.00 48.39 O HETATM 4250 O HOH A1338 5.988 40.827 133.435 1.00 29.56 O HETATM 4251 O HOH A1339 -2.541 74.709 122.125 1.00 47.53 O HETATM 4252 O HOH A1340 13.310 41.345 126.595 1.00 38.16 O HETATM 4253 O HOH A1341 -0.482 95.029 101.730 1.00 43.08 O HETATM 4254 O HOH A1342 17.424 87.431 109.718 1.00 38.42 O HETATM 4255 O HOH A1343 -1.165 87.121 120.427 1.00 24.09 O HETATM 4256 O HOH A1344 5.276 62.967 113.734 1.00 38.31 O HETATM 4257 O HOH A1345 18.574 28.235 125.712 1.00 30.75 O HETATM 4258 O HOH A1346 25.174 84.795 110.894 1.00 50.52 O HETATM 4259 O HOH A1347 29.122 14.086 121.836 1.00 51.44 O HETATM 4260 O HOH A1348 28.537 88.640 98.446 1.00 57.82 O HETATM 4261 O HOH A1349 23.045 75.345 110.750 1.00 38.41 O HETATM 4262 O HOH A1350 29.301 24.575 128.516 1.00 31.13 O HETATM 4263 O HOH A1351 1.247 75.036 127.056 1.00 49.02 O HETATM 4264 O HOH A1352 5.802 72.877 113.599 1.00 50.27 O HETATM 4265 O HOH A1353 10.798 85.586 117.760 1.00 57.81 O HETATM 4266 O HOH A1354 -7.613 79.314 115.880 1.00 39.06 O HETATM 4267 O HOH A1355 24.371 81.543 114.063 1.00 51.39 O HETATM 4268 O HOH A1356 0.433 72.540 111.902 1.00 48.74 O HETATM 4269 O HOH A1357 21.868 68.831 123.096 1.00 42.24 O HETATM 4270 O HOH A1358 32.903 71.243 98.125 1.00 61.49 O HETATM 4271 O HOH A1359 18.890 36.428 142.762 1.00 32.44 O HETATM 4272 O HOH A1360 16.975 37.875 133.735 1.00 37.08 O HETATM 4273 O HOH A1361 28.177 18.536 134.530 1.00 41.80 O HETATM 4274 O HOH A1362 22.100 69.305 113.977 1.00 45.54 O HETATM 4275 O HOH A1363 25.163 25.100 136.734 1.00 33.68 O HETATM 4276 O HOH A1364 15.872 48.937 129.917 1.00 56.38 O HETATM 4277 O HOH A1365 2.694 95.944 113.727 1.00 29.67 O HETATM 4278 O HOH A1366 16.276 81.606 119.428 1.00 47.12 O HETATM 4279 O HOH A1367 31.538 25.801 129.286 1.00 34.97 O HETATM 4280 O HOH A1368 11.503 27.428 128.171 1.00 51.19 O HETATM 4281 O HOH A1369 -0.705 73.603 109.622 1.00 46.26 O HETATM 4282 O HOH A1370 5.423 89.441 103.325 1.00 47.23 O HETATM 4283 O HOH A1371 2.013 68.615 116.316 1.00 63.63 O HETATM 4284 O HOH A1372 25.264 7.831 129.162 1.00 33.59 O HETATM 4285 O HOH A1373 12.712 34.164 124.010 1.00 31.57 O HETATM 4286 O HOH A1374 14.017 27.367 124.828 1.00 39.61 O HETATM 4287 O HOH A1375 28.413 80.381 106.863 1.00 53.20 O HETATM 4288 O HOH A1376 24.440 51.645 136.872 1.00 47.56 O HETATM 4289 O HOH A1377 13.309 85.899 116.190 1.00 55.26 O HETATM 4290 O HOH A1378 10.165 59.030 121.656 1.00 29.07 O HETATM 4291 O HOH A1379 0.742 71.181 107.721 1.00 62.90 O HETATM 4292 O HOH A1380 26.318 11.365 130.974 1.00 52.58 O HETATM 4293 O HOH A1381 -7.206 87.998 118.440 1.00 36.58 O HETATM 4294 O HOH A1382 23.855 84.251 113.569 1.00 51.55 O HETATM 4295 O HOH A1383 -6.518 94.435 118.635 1.00 42.21 O HETATM 4296 O HOH A1384 19.981 68.519 115.734 1.00 55.02 O HETATM 4297 O HOH A1385 29.336 21.339 134.580 1.00 41.33 O HETATM 4298 O HOH A1386 8.047 77.379 96.256 1.00 46.47 O HETATM 4299 O HOH A1387 5.235 36.710 131.176 1.00 35.75 O HETATM 4300 O HOH A1388 31.510 16.119 123.213 1.00 60.39 O HETATM 4301 O HOH A1389 -11.472 85.637 118.389 1.00 48.96 O HETATM 4302 O HOH A1390 0.224 23.333 136.183 1.00 57.23 O HETATM 4303 O HOH A1391 24.066 11.893 115.867 1.00 53.60 O HETATM 4304 O HOH A1392 19.866 17.570 143.858 1.00 40.82 O HETATM 4305 O HOH A1393 3.100 82.178 110.236 1.00 26.14 O HETATM 4306 O HOH A1394 8.278 84.871 104.037 1.00 46.19 O HETATM 4307 O HOH A1395 28.525 16.351 124.718 1.00 43.69 O HETATM 4308 O HOH A1396 19.998 18.406 118.828 1.00 43.40 O HETATM 4309 O HOH A1397 22.101 86.873 94.887 1.00 54.93 O HETATM 4310 O HOH A1398 13.332 17.401 119.974 1.00 51.79 O HETATM 4311 O HOH A1399 24.197 87.358 92.952 1.00 54.62 O HETATM 4312 O AHOH A1400 38.250 25.045 131.795 1.00 39.62 O HETATM 4313 O HOH A1401 13.172 21.635 120.080 1.00 60.41 O HETATM 4314 O HOH A1402 11.078 84.982 93.206 1.00 53.98 O HETATM 4315 O HOH A1403 -5.013 78.500 110.029 1.00 56.88 O HETATM 4316 O HOH A1404 4.823 89.290 118.016 1.00 44.25 O HETATM 4317 O HOH A1405 8.789 28.042 124.449 1.00 38.99 O HETATM 4318 O HOH A1406 17.575 82.469 103.028 1.00 38.14 O HETATM 4319 O HOH A1407 2.173 75.546 96.271 1.00 67.61 O HETATM 4320 O HOH A1408 23.147 64.496 102.209 1.00 60.81 O HETATM 4321 O HOH A1409 25.179 68.358 118.304 1.00 69.25 O HETATM 4322 O HOH A1410 4.858 71.593 107.204 1.00 45.40 O HETATM 4323 O HOH A1411 9.952 22.864 149.263 1.00 68.28 O HETATM 4324 O HOH A1412 4.727 79.340 100.809 1.00 44.03 O HETATM 4325 O HOH A1413 12.943 68.861 105.308 1.00 43.37 O HETATM 4326 O HOH A1414 9.328 14.466 140.545 1.00 51.32 O HETATM 4327 O HOH A1415 23.149 66.538 117.684 1.00 74.09 O HETATM 4328 O HOH A1416 3.170 84.151 102.432 1.00 43.49 O HETATM 4329 O HOH A1417 8.889 83.521 92.546 1.00 66.07 O HETATM 4330 O HOH A1418 -3.889 79.141 112.123 1.00 38.24 O HETATM 4331 O HOH A1419 4.509 64.590 127.979 1.00 42.12 O HETATM 4332 O HOH A1420 0.529 82.833 121.907 1.00 25.56 O HETATM 4333 O HOH A1421 19.123 84.872 91.926 1.00 64.84 O HETATM 4334 O HOH A1422 17.776 23.168 139.802 1.00 41.82 O HETATM 4335 O HOH A1423 22.602 66.419 123.003 1.00 51.75 O HETATM 4336 O HOH A1424 16.090 88.385 106.171 1.00 44.33 O HETATM 4337 O HOH A1425 26.170 14.561 131.605 1.00 34.96 O HETATM 4338 O HOH A1426 -1.375 95.141 113.965 1.00 54.30 O HETATM 4339 O HOH A1427 -8.488 100.065 105.710 1.00 50.12 O HETATM 4340 O HOH A1428 26.769 14.320 123.274 1.00 49.62 O HETATM 4341 O HOH A1429 12.361 87.499 104.654 1.00 50.62 O HETATM 4342 O HOH A1430 -1.527 101.056 108.113 1.00 63.38 O HETATM 4343 O HOH A1431 13.901 88.967 107.782 1.00 52.10 O HETATM 4344 O HOH A1432 -0.371 80.106 121.453 1.00 25.61 O HETATM 4345 O HOH A1433 0.290 69.992 117.395 1.00 51.26 O HETATM 4346 O HOH A1434 15.766 25.916 135.215 1.00 59.18 O HETATM 4347 O HOH A1435 19.414 61.033 117.610 1.00 62.35 O HETATM 4348 O HOH A1436 9.902 88.143 116.663 1.00 69.76 O HETATM 4349 O HOH A1437 5.435 65.113 112.072 1.00 51.18 O HETATM 4350 O HOH A1438 -5.414 101.290 105.967 1.00 56.58 O HETATM 4351 O HOH A1439 9.118 11.953 140.838 1.00 68.87 O HETATM 4352 O HOH A1440 11.372 67.958 131.162 1.00 70.31 O HETATM 4353 O HOH A1441 23.474 70.525 121.362 1.00 47.35 O HETATM 4354 O HOH A1442 4.184 91.442 116.468 1.00 51.07 O HETATM 4355 O HOH A1443 21.331 85.211 91.783 1.00 69.83 O HETATM 4356 O HOH A1444 -12.118 93.670 108.425 1.00 61.77 O HETATM 4357 O HOH A1445 -3.224 94.362 115.431 1.00 55.42 O HETATM 4358 O HOH A1446 18.402 86.669 114.864 1.00 66.76 O HETATM 4359 O HOH A1447 21.325 81.402 117.008 1.00 61.78 O HETATM 4360 O HOH A1448 28.537 8.616 118.549 1.00 53.28 O HETATM 4361 O HOH A1449 21.313 84.221 115.654 1.00 66.48 O HETATM 4362 O HOH A1450 11.153 88.459 107.007 1.00 60.00 O HETATM 4363 O HOH A1451 7.040 71.382 108.246 1.00 53.01 O HETATM 4364 O HOH A1452 5.135 82.239 102.716 1.00 64.08 O HETATM 4365 O HOH A1453 21.756 88.807 91.675 1.00 71.25 O HETATM 4366 O HOH A1454 7.619 88.606 104.412 1.00 62.39 O HETATM 4367 O HOH A1455 -11.566 93.763 111.677 1.00 65.40 O HETATM 4368 O HOH A1456 26.206 81.891 111.620 1.00 71.98 O HETATM 4369 O HOH A1457 25.330 72.228 122.566 1.00 60.54 O HETATM 4370 O HOH A1458 29.450 82.109 104.399 1.00 60.05 O HETATM 4371 O HOH A1459 14.152 82.829 118.326 1.00 45.62 O HETATM 4372 O HOH A1460 21.831 4.946 122.840 1.00 50.91 O HETATM 4373 O HOH A1461 2.967 90.037 119.902 1.00 44.32 O HETATM 4374 O HOH A1462 -4.796 102.075 108.188 1.00 66.22 O HETATM 4375 O HOH A1463 18.247 89.099 107.510 1.00 42.62 O HETATM 4376 O HOH A1464 6.781 80.683 100.729 1.00 72.11 O HETATM 4377 O HOH A1465 6.793 79.405 97.491 1.00 65.51 O HETATM 4378 O HOH A1466 19.009 82.623 118.675 1.00 75.54 O HETATM 4379 O HOH B 101 15.200 27.980 134.158 1.00 34.64 O HETATM 4380 O HOH B 102 12.878 16.741 125.481 1.00 37.66 O HETATM 4381 O HOH B 103 19.882 10.223 129.496 1.00 60.76 O HETATM 4382 O HOH B 104 11.568 28.275 130.920 1.00 40.72 O HETATM 4383 O HOH B 105 14.637 7.995 129.845 1.00 56.17 O HETATM 4384 O HOH B 106 13.058 33.535 126.505 1.00 37.11 O HETATM 4385 O HOH B 107 13.687 25.928 127.961 1.00 50.29 O HETATM 4386 O HOH B 108 12.943 19.749 125.300 1.00 56.15 O HETATM 4387 O HOH B 109 17.446 10.627 127.970 1.00 44.66 O CONECT 33 3388 CONECT 679 1300 CONECT 1300 679 CONECT 3388 33 CONECT 3737 3858 CONECT 3750 3821 CONECT 3821 3750 CONECT 3858 3737 CONECT 3917 3920 CONECT 3918 3919 3921 CONECT 3919 3918 3922 CONECT 3920 3917 3924 CONECT 3921 3918 3925 CONECT 3922 3919 3926 CONECT 3923 3937 3939 CONECT 3924 3920 3927 CONECT 3925 3921 3928 CONECT 3926 3922 3929 CONECT 3927 3924 3930 CONECT 3928 3925 3930 CONECT 3929 3926 3931 CONECT 3930 3927 3928 CONECT 3931 3929 3932 CONECT 3932 3931 3933 CONECT 3933 3932 3934 CONECT 3934 3933 3936 CONECT 3935 3937 3941 CONECT 3936 3934 3938 3941 CONECT 3937 3923 3935 3940 CONECT 3938 3936 CONECT 3939 3923 CONECT 3940 3937 CONECT 3941 3935 3936 CONECT 3942 3945 CONECT 3943 3944 3946 CONECT 3944 3943 3947 CONECT 3945 3942 3949 CONECT 3946 3943 3950 CONECT 3947 3944 3951 CONECT 3948 3962 3964 CONECT 3949 3945 3952 CONECT 3950 3946 3953 CONECT 3951 3947 3954 CONECT 3952 3949 3955 CONECT 3953 3950 3955 CONECT 3954 3951 3956 CONECT 3955 3952 3953 CONECT 3956 3954 3957 CONECT 3957 3956 3958 CONECT 3958 3957 3959 CONECT 3959 3958 3961 CONECT 3960 3962 3966 CONECT 3961 3959 3963 3966 CONECT 3962 3948 3960 3965 CONECT 3963 3961 CONECT 3964 3948 CONECT 3965 3962 CONECT 3966 3960 3961 CONECT 3967 3970 CONECT 3968 3969 3971 CONECT 3969 3968 3972 CONECT 3970 3967 3974 CONECT 3971 3968 3975 CONECT 3972 3969 3976 CONECT 3973 3987 3989 CONECT 3974 3970 3977 CONECT 3975 3971 3978 CONECT 3976 3972 3979 CONECT 3977 3974 3980 CONECT 3978 3975 3980 CONECT 3979 3976 3981 CONECT 3980 3977 3978 CONECT 3981 3979 3982 CONECT 3982 3981 3983 CONECT 3983 3982 3984 CONECT 3984 3983 3986 CONECT 3985 3987 3991 CONECT 3986 3984 3988 3991 CONECT 3987 3973 3985 3990 CONECT 3988 3986 CONECT 3989 3973 CONECT 3990 3987 CONECT 3991 3985 3986 CONECT 3992 3995 CONECT 3993 3994 3996 CONECT 3994 3993 3997 CONECT 3995 3992 3999 CONECT 3996 3993 4000 CONECT 3997 3994 4001 CONECT 3998 4012 4014 CONECT 3999 3995 4002 CONECT 4000 3996 4003 CONECT 4001 3997 4004 CONECT 4002 3999 4005 CONECT 4003 4000 4005 CONECT 4004 4001 4006 CONECT 4005 4002 4003 CONECT 4006 4004 4007 CONECT 4007 4006 4008 CONECT 4008 4007 4009 CONECT 4009 4008 4011 CONECT 4010 4012 4016 CONECT 4011 4009 4013 4016 CONECT 4012 3998 4010 4015 CONECT 4013 4011 CONECT 4014 3998 CONECT 4015 4012 CONECT 4016 4010 4011 CONECT 4017 4020 CONECT 4018 4019 4021 CONECT 4019 4018 4022 CONECT 4020 4017 4024 CONECT 4021 4018 4025 CONECT 4022 4019 4026 CONECT 4023 4037 4039 CONECT 4024 4020 4027 CONECT 4025 4021 4028 CONECT 4026 4022 4029 CONECT 4027 4024 4030 CONECT 4028 4025 4030 CONECT 4029 4026 4031 CONECT 4030 4027 4028 CONECT 4031 4029 4032 CONECT 4032 4031 4033 CONECT 4033 4032 4034 CONECT 4034 4033 4036 CONECT 4035 4037 4041 CONECT 4036 4034 4038 4041 CONECT 4037 4023 4035 4040 CONECT 4038 4036 CONECT 4039 4023 CONECT 4040 4037 CONECT 4041 4035 4036 CONECT 4042 4045 CONECT 4043 4044 4046 CONECT 4044 4043 4047 CONECT 4045 4042 4049 CONECT 4046 4043 4050 CONECT 4047 4044 4051 CONECT 4048 4062 4064 CONECT 4049 4045 4052 CONECT 4050 4046 4053 CONECT 4051 4047 4054 CONECT 4052 4049 4055 CONECT 4053 4050 4055 CONECT 4054 4051 4056 CONECT 4055 4052 4053 CONECT 4056 4054 4057 CONECT 4057 4056 4058 CONECT 4058 4057 4059 CONECT 4059 4058 4061 CONECT 4060 4062 4066 CONECT 4061 4059 4063 4066 CONECT 4062 4048 4060 4065 CONECT 4063 4061 CONECT 4064 4048 CONECT 4065 4062 CONECT 4066 4060 4061 CONECT 4067 4070 CONECT 4068 4069 4071 CONECT 4069 4068 4072 CONECT 4070 4067 4074 CONECT 4071 4068 4075 CONECT 4072 4069 4076 CONECT 4073 4087 4089 CONECT 4074 4070 4077 CONECT 4075 4071 4078 CONECT 4076 4072 4079 CONECT 4077 4074 4080 CONECT 4078 4075 4080 CONECT 4079 4076 4081 CONECT 4080 4077 4078 CONECT 4081 4079 4082 CONECT 4082 4081 4083 CONECT 4083 4082 4084 CONECT 4084 4083 4086 CONECT 4085 4087 4091 CONECT 4086 4084 4088 4091 CONECT 4087 4073 4085 4090 CONECT 4088 4086 CONECT 4089 4073 CONECT 4090 4087 CONECT 4091 4085 4086 CONECT 4092 4095 CONECT 4093 4094 4096 CONECT 4094 4093 4097 CONECT 4095 4092 4099 CONECT 4096 4093 4100 CONECT 4097 4094 4101 CONECT 4098 4112 4114 CONECT 4099 4095 4102 CONECT 4100 4096 4103 CONECT 4101 4097 4104 CONECT 4102 4099 4105 CONECT 4103 4100 4105 CONECT 4104 4101 4106 CONECT 4105 4102 4103 CONECT 4106 4104 4107 CONECT 4107 4106 4108 CONECT 4108 4107 4109 CONECT 4109 4108 4111 CONECT 4110 4112 4116 CONECT 4111 4109 4113 4116 CONECT 4112 4098 4110 4115 CONECT 4113 4111 CONECT 4114 4098 CONECT 4115 4112 CONECT 4116 4110 4111 CONECT 4117 4118 4119 CONECT 4118 4117 4120 CONECT 4119 4117 4122 CONECT 4120 4118 4123 CONECT 4121 4132 4134 CONECT 4122 4119 4124 CONECT 4123 4120 4125 CONECT 4124 4122 CONECT 4125 4123 4126 CONECT 4126 4125 4127 CONECT 4127 4126 4128 CONECT 4128 4127 4129 CONECT 4129 4128 4131 CONECT 4130 4132 4136 CONECT 4131 4129 4133 4136 CONECT 4132 4121 4130 4135 CONECT 4133 4131 CONECT 4134 4121 CONECT 4135 4132 CONECT 4136 4130 4131 CONECT 4137 4140 CONECT 4138 4139 4141 CONECT 4139 4138 4142 CONECT 4140 4137 4144 CONECT 4141 4138 4145 CONECT 4142 4139 4146 CONECT 4143 4157 4159 CONECT 4144 4140 4147 CONECT 4145 4141 4148 CONECT 4146 4142 4149 CONECT 4147 4144 4150 CONECT 4148 4145 4150 CONECT 4149 4146 4151 CONECT 4150 4147 4148 CONECT 4151 4149 4152 CONECT 4152 4151 4153 CONECT 4153 4152 4154 CONECT 4154 4153 4156 CONECT 4155 4157 4161 CONECT 4156 4154 4158 4161 CONECT 4157 4143 4155 4160 CONECT 4158 4156 CONECT 4159 4143 CONECT 4160 4157 CONECT 4161 4155 4156 CONECT 4162 4163 4164 CONECT 4163 4162 4165 CONECT 4164 4162 4167 CONECT 4165 4163 4168 CONECT 4166 4176 4178 CONECT 4167 4164 CONECT 4168 4165 4169 CONECT 4169 4168 4170 CONECT 4170 4169 4171 CONECT 4171 4170 4172 CONECT 4172 4171 4173 CONECT 4173 4172 4175 CONECT 4174 4176 4180 CONECT 4175 4173 4177 4180 CONECT 4176 4166 4174 4179 CONECT 4177 4175 CONECT 4178 4166 CONECT 4179 4176 CONECT 4180 4174 4175 CONECT 4181 4182 4183 CONECT 4182 4181 4184 CONECT 4183 4181 4186 CONECT 4184 4182 4187 CONECT 4185 4195 4197 CONECT 4186 4183 CONECT 4187 4184 4188 CONECT 4188 4187 4189 CONECT 4189 4188 4190 CONECT 4190 4189 4191 CONECT 4191 4190 4192 CONECT 4192 4191 4194 CONECT 4193 4195 4199 CONECT 4194 4192 4196 4199 CONECT 4195 4185 4193 4198 CONECT 4196 4194 CONECT 4197 4185 CONECT 4198 4195 CONECT 4199 4193 4194 CONECT 4200 4201 4202 4203 CONECT 4201 4200 CONECT 4202 4200 CONECT 4203 4200 4204 CONECT 4204 4203 4205 4206 4210 CONECT 4205 4204 CONECT 4206 4204 4207 CONECT 4207 4206 4208 4209 CONECT 4208 4207 CONECT 4209 4207 CONECT 4210 4204 4211 4212 CONECT 4211 4210 CONECT 4212 4210 MASTER 438 0 13 21 5 0 21 6 4382 2 304 41 END