HEADER MEMBRANE PROTEIN 27-JUL-17 5OLH TITLE STRUCTURE OF THE A2A-STAR2-BRIL562-VIPADENANT COMPLEX AT 2.6A OBTAINED TITLE 2 FROM IN MESO SOAKING EXPERIMENTS. COMPND MOL_ID: 1; COMPND 2 MOLECULE: ADENOSINE RECEPTOR A2A,SOLUBLE CYTOCHROME B562,ADENOSINE COMPND 3 RECEPTOR A2A; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: CYTOCHROME B-562; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 562; SOURCE 5 GENE: ADORA2A, ADORA2, CYBC; SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: VIRUS KEYWDS G-PROTEIN COUPLED RECEPTOR, ADENOSINE 2A RECEPTOR, 7 TM INTEGRAL KEYWDS 2 MEMBRANE PROTEIN, THERMOSTABILIZING MUTATIONS, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR P.RUCKTOOA,R.K.Y.CHENG,E.SEGALA,T.GENG,J.C.ERREY,G.A.BROWN,R.COOKE, AUTHOR 2 F.H.MARSHALL,A.S.DORE REVDAT 1 17-JAN-18 5OLH 0 JRNL AUTH P.RUCKTOOA,R.K.Y.CHENG,E.SEGALA,T.GENG,J.C.ERREY,G.A.BROWN, JRNL AUTH 2 R.M.COOKE,F.H.MARSHALL,A.S.DORE JRNL TITL TOWARDS HIGH THROUGHPUT GPCR CRYSTALLOGRAPHY: IN MESO JRNL TITL 2 SOAKING OF ADENOSINE A2A RECEPTOR CRYSTALS. JRNL REF SCI REP V. 8 41 2018 JRNL REFN ESSN 2045-2322 JRNL PMID 29311713 JRNL DOI 10.1038/S41598-017-18570-W REMARK 2 REMARK 2 RESOLUTION. 2.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.12RC2_2821) 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) : 2.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.82 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.030 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9 REMARK 3 NUMBER OF REFLECTIONS : 29093 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.203 REMARK 3 R VALUE (WORKING SET) : 0.200 REMARK 3 FREE R VALUE : 0.249 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.170 REMARK 3 FREE R VALUE TEST SET COUNT : 1503 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 29.8188 - 5.7705 0.99 2546 135 0.1732 0.2167 REMARK 3 2 5.7705 - 4.5856 0.99 2529 146 0.1784 0.2885 REMARK 3 3 4.5856 - 4.0075 0.98 2491 133 0.1661 0.1985 REMARK 3 4 4.0075 - 3.6418 0.96 2486 134 0.1748 0.2097 REMARK 3 5 3.6418 - 3.3811 0.98 2481 156 0.1897 0.2133 REMARK 3 6 3.3811 - 3.1820 0.98 2514 117 0.2088 0.2484 REMARK 3 7 3.1820 - 3.0228 0.99 2518 152 0.2482 0.3562 REMARK 3 8 3.0228 - 2.8913 0.99 2562 110 0.2355 0.2399 REMARK 3 9 2.8913 - 2.7801 0.99 2532 140 0.2458 0.3031 REMARK 3 10 2.7801 - 2.6843 0.97 2474 145 0.2673 0.3240 REMARK 3 11 2.6843 - 2.6004 0.96 2457 135 0.2623 0.2722 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) : 0.320 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.440 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 31.80 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.21 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.003 3591 REMARK 3 ANGLE : 0.739 4778 REMARK 3 CHIRALITY : 0.042 528 REMARK 3 PLANARITY : 0.003 560 REMARK 3 DIHEDRAL : 12.955 2206 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN A AND (RESSEQ -1:208 OR RESSEQ 219:305 OR REMARK 3 RESSEQ 1201)) REMARK 3 ORIGIN FOR THE GROUP (A): -22.4758 -6.0286 18.1040 REMARK 3 T TENSOR REMARK 3 T11: 0.1490 T22: 0.2143 REMARK 3 T33: 0.1230 T12: -0.0104 REMARK 3 T13: 0.0107 T23: 0.0203 REMARK 3 L TENSOR REMARK 3 L11: 0.8781 L22: 1.7577 REMARK 3 L33: 1.3079 L12: 0.0860 REMARK 3 L13: 0.1822 L23: 0.0625 REMARK 3 S TENSOR REMARK 3 S11: 0.0047 S12: -0.0015 S13: -0.0576 REMARK 3 S21: -0.0948 S22: -0.0045 S23: -0.0332 REMARK 3 S31: 0.1201 S32: -0.0777 S33: -0.0001 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN A AND (RESSEQ 1001:1106)) REMARK 3 ORIGIN FOR THE GROUP (A): 0.0233 -54.0513 20.1672 REMARK 3 T TENSOR REMARK 3 T11: 0.5193 T22: 0.4042 REMARK 3 T33: 0.8319 T12: 0.0766 REMARK 3 T13: -0.0071 T23: -0.0412 REMARK 3 L TENSOR REMARK 3 L11: 0.6145 L22: 2.6109 REMARK 3 L33: 2.2925 L12: -0.0819 REMARK 3 L13: -0.2999 L23: -0.3085 REMARK 3 S TENSOR REMARK 3 S11: 0.1366 S12: -0.1312 S13: 0.4454 REMARK 3 S21: -0.3472 S22: 0.1490 S23: -0.1381 REMARK 3 S31: -0.0507 S32: 0.1765 S33: -0.2721 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 5OLH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JUL-17. REMARK 100 THE DEPOSITION ID IS D_1200006007. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-APR-16 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.3-5.4 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X06SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15853 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 REMARK 200 RESOLUTION RANGE LOW (A) : 29.820 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 200 DATA REDUNDANCY : 8.300 REMARK 200 R MERGE (I) : 0.24800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.72 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7 REMARK 200 DATA REDUNDANCY IN SHELL : 5.10 REMARK 200 R MERGE FOR SHELL (I) : 1.23200 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.800 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: 5MZJ REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.57 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTAL GROWTH: 0.L M TRI-SODIUM REMARK 280 CITRATE PH 5.3-5.4, 0.05 M SODIUM THIOCYANATE, 29-32% PEG400, 2% REMARK 280 (V/V) 2,5-HEXANEDIOL AND 0.5 MM THEOPHYLLINE VIPADENANT WAS REMARK 280 ADDED TO THE MOTHER LIQUOR TO A CONCENTRATION OF 0.005 MM FOR REMARK 280 THE SOAKING EXPERIMENTS., LIPIDIC CUBIC PHASE, TEMPERATURE REMARK 280 293.15K 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 70.57250 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 70.57250 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 19.70000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 89.66700 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 19.70000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 89.66700 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 70.57250 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 19.70000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 89.66700 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 70.57250 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 19.70000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 89.66700 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: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 8630 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21180 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 19.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A 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 ALA A -9 REMARK 465 ASP A -8 REMARK 465 TYR A -7 REMARK 465 LYS A -6 REMARK 465 ASP A -5 REMARK 465 ASP A -4 REMARK 465 ASP A -3 REMARK 465 ASP A -2 REMARK 465 ALA A 1043 REMARK 465 THR A 1044 REMARK 465 PRO A 1045 REMARK 465 PRO A 1046 REMARK 465 LYS A 1047 REMARK 465 LEU A 1048 REMARK 465 GLU A 1049 REMARK 465 ASP A 1050 REMARK 465 LYS A 1051 REMARK 465 SER A 1052 REMARK 465 PRO A 1053 REMARK 465 ASP A 1054 REMARK 465 SER A 1055 REMARK 465 HIS A 306 REMARK 465 VAL A 307 REMARK 465 LEU A 308 REMARK 465 ARG A 309 REMARK 465 GLN A 310 REMARK 465 GLN A 311 REMARK 465 GLU A 312 REMARK 465 PRO A 313 REMARK 465 PHE A 314 REMARK 465 LYS A 315 REMARK 465 ALA A 316 REMARK 465 ALA A 317 REMARK 465 ALA A 318 REMARK 465 HIS A 319 REMARK 465 HIS A 320 REMARK 465 HIS A 321 REMARK 465 HIS A 322 REMARK 465 HIS A 323 REMARK 465 HIS A 324 REMARK 465 HIS A 325 REMARK 465 HIS A 326 REMARK 465 HIS A 327 REMARK 465 HIS A 328 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 LYS A 150 89.62 -67.44 REMARK 500 TYR A1101 -51.98 -129.01 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 LEU A1106 -13.49 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 OLA A 1207 REMARK 610 OLA A 1208 REMARK 610 OLA A 1211 REMARK 610 OLA A 1212 REMARK 610 OLA A 1213 REMARK 610 OLA A 1214 REMARK 610 OLA A 1215 REMARK 610 OLA A 1216 REMARK 610 OLA A 1217 REMARK 610 OLA A 1218 REMARK 610 OLA A 1219 REMARK 610 OLC A 1220 REMARK 610 OLC A 1221 REMARK 610 OLC A 1222 REMARK 610 OLC A 1223 REMARK 610 OLC A 1224 REMARK 610 OLC A 1225 REMARK 610 OLC A 1226 REMARK 610 OLC A 1227 REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A1203 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 52 OD1 REMARK 620 2 SER A 91 OG 135.4 REMARK 620 3 HOH A1309 O 106.3 117.8 REMARK 620 N 1 2 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 9XT A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1202 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 1203 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1204 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1205 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1206 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1207 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1208 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1209 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1211 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1213 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1214 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1215 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1216 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1217 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1218 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1219 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1220 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1221 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1222 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1223 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1224 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1225 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1226 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1227 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1228 DBREF 5OLH A 2 208 UNP P29274 AA2AR_HUMAN 2 208 DBREF 5OLH A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128 DBREF 5OLH A 219 317 UNP P29274 AA2AR_HUMAN 219 317 SEQADV 5OLH ALA A -9 UNP P29274 EXPRESSION TAG SEQADV 5OLH ASP A -8 UNP P29274 EXPRESSION TAG SEQADV 5OLH TYR A -7 UNP P29274 EXPRESSION TAG SEQADV 5OLH LYS A -6 UNP P29274 EXPRESSION TAG SEQADV 5OLH ASP A -5 UNP P29274 EXPRESSION TAG SEQADV 5OLH ASP A -4 UNP P29274 EXPRESSION TAG SEQADV 5OLH ASP A -3 UNP P29274 EXPRESSION TAG SEQADV 5OLH ASP A -2 UNP P29274 EXPRESSION TAG SEQADV 5OLH GLY A -1 UNP P29274 EXPRESSION TAG SEQADV 5OLH ALA A 0 UNP P29274 EXPRESSION TAG SEQADV 5OLH PRO A 1 UNP P29274 EXPRESSION TAG SEQADV 5OLH LEU A 54 UNP P29274 ALA 54 ENGINEERED MUTATION SEQADV 5OLH ALA A 88 UNP P29274 THR 88 ENGINEERED MUTATION SEQADV 5OLH ALA A 107 UNP P29274 ARG 107 ENGINEERED MUTATION SEQADV 5OLH ALA A 122 UNP P29274 LYS 122 ENGINEERED MUTATION SEQADV 5OLH ALA A 154 UNP P29274 ASN 154 ENGINEERED MUTATION SEQADV 5OLH ALA A 202 UNP P29274 LEU 202 ENGINEERED MUTATION SEQADV 5OLH TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 5OLH ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 5OLH LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION SEQADV 5OLH ALA A 235 UNP P29274 LEU 235 ENGINEERED MUTATION SEQADV 5OLH ALA A 239 UNP P29274 VAL 239 ENGINEERED MUTATION SEQADV 5OLH ALA A 277 UNP P29274 SER 277 ENGINEERED MUTATION SEQADV 5OLH ALA A 318 UNP P29274 EXPRESSION TAG SEQADV 5OLH HIS A 319 UNP P29274 EXPRESSION TAG SEQADV 5OLH HIS A 320 UNP P29274 EXPRESSION TAG SEQADV 5OLH HIS A 321 UNP P29274 EXPRESSION TAG SEQADV 5OLH HIS A 322 UNP P29274 EXPRESSION TAG SEQADV 5OLH HIS A 323 UNP P29274 EXPRESSION TAG SEQADV 5OLH HIS A 324 UNP P29274 EXPRESSION TAG SEQADV 5OLH HIS A 325 UNP P29274 EXPRESSION TAG SEQADV 5OLH HIS A 326 UNP P29274 EXPRESSION TAG SEQADV 5OLH HIS A 327 UNP P29274 EXPRESSION TAG SEQADV 5OLH HIS A 328 UNP P29274 EXPRESSION TAG SEQRES 1 A 434 ALA ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO PRO ILE SEQRES 2 A 434 MET GLY SER SER VAL TYR ILE THR VAL GLU LEU ALA ILE SEQRES 3 A 434 ALA VAL LEU ALA ILE LEU GLY ASN VAL LEU VAL CYS TRP SEQRES 4 A 434 ALA VAL TRP LEU ASN SER ASN LEU GLN ASN VAL THR ASN SEQRES 5 A 434 TYR PHE VAL VAL SER LEU ALA ALA ALA ASP ILE LEU VAL SEQRES 6 A 434 GLY VAL LEU ALA ILE PRO PHE ALA ILE THR ILE SER THR SEQRES 7 A 434 GLY PHE CYS ALA ALA CYS HIS GLY CYS LEU PHE ILE ALA SEQRES 8 A 434 CYS PHE VAL LEU VAL LEU ALA GLN SER SER ILE PHE SER SEQRES 9 A 434 LEU LEU ALA ILE ALA ILE ASP ARG TYR ILE ALA ILE ALA SEQRES 10 A 434 ILE PRO LEU ARG TYR ASN GLY LEU VAL THR GLY THR ARG SEQRES 11 A 434 ALA ALA GLY ILE ILE ALA ILE CYS TRP VAL LEU SER PHE SEQRES 12 A 434 ALA ILE GLY LEU THR PRO MET LEU GLY TRP ASN ASN CYS SEQRES 13 A 434 GLY GLN PRO LYS GLU GLY LYS ALA HIS SER GLN GLY CYS SEQRES 14 A 434 GLY GLU GLY GLN VAL ALA CYS LEU PHE GLU ASP VAL VAL SEQRES 15 A 434 PRO MET ASN TYR MET VAL TYR PHE ASN PHE PHE ALA CYS SEQRES 16 A 434 VAL LEU VAL PRO LEU LEU LEU MET LEU GLY VAL TYR LEU SEQRES 17 A 434 ARG ILE PHE ALA ALA ALA ARG ARG GLN LEU ALA ASP LEU SEQRES 18 A 434 GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS VAL SEQRES 19 A 434 ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP ALA SEQRES 20 A 434 LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN LYS SEQRES 21 A 434 ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SER SEQRES 22 A 434 PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE LEU SEQRES 23 A 434 VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN GLU SEQRES 24 A 434 GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN LEU SEQRES 25 A 434 LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU GLU SEQRES 26 A 434 ARG ALA ARG SER THR LEU GLN LYS GLU VAL HIS ALA ALA SEQRES 27 A 434 LYS SER ALA ALA ILE ILE ALA GLY LEU PHE ALA LEU CYS SEQRES 28 A 434 TRP LEU PRO LEU HIS ILE ILE ASN CYS PHE THR PHE PHE SEQRES 29 A 434 CYS PRO ASP CYS SER HIS ALA PRO LEU TRP LEU MET TYR SEQRES 30 A 434 LEU ALA ILE VAL LEU ALA HIS THR ASN SER VAL VAL ASN SEQRES 31 A 434 PRO PHE ILE TYR ALA TYR ARG ILE ARG GLU PHE ARG GLN SEQRES 32 A 434 THR PHE ARG LYS ILE ILE ARG SER HIS VAL LEU ARG GLN SEQRES 33 A 434 GLN GLU PRO PHE LYS ALA ALA ALA HIS HIS HIS HIS HIS SEQRES 34 A 434 HIS HIS HIS HIS HIS HET 9XT A1201 24 HET OLA A1202 20 HET NA A1203 1 HET CLR A1204 28 HET CLR A1205 28 HET CLR A1206 28 HET OLA A1207 9 HET OLA A1208 18 HET OLA A1209 20 HET OLA A1210 20 HET OLA A1211 12 HET OLA A1212 8 HET OLA A1213 9 HET OLA A1214 19 HET OLA A1215 14 HET OLA A1216 10 HET OLA A1217 13 HET OLA A1218 12 HET OLA A1219 13 HET OLC A1220 16 HET OLC A1221 17 HET OLC A1222 17 HET OLC A1223 20 HET OLC A1224 24 HET OLC A1225 22 HET OLC A1226 20 HET OLC A1227 20 HET OLA A1228 20 HETNAM 9XT 3-[(4-AZANYL-3-METHYL-PHENYL)METHYL]-7-(FURAN-2-YL)-[1, HETNAM 2 9XT 2,3]TRIAZOLO[4,5-D]PYRIMIDIN-5-AMINE HETNAM OLA OLEIC ACID HETNAM NA SODIUM ION HETNAM CLR CHOLESTEROL HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 9XT C16 H15 N7 O FORMUL 3 OLA 15(C18 H34 O2) FORMUL 4 NA NA 1+ FORMUL 5 CLR 3(C27 H46 O) FORMUL 21 OLC 8(C21 H40 O4) FORMUL 30 HOH *29(H2 O) HELIX 1 AA1 PRO A 1 ASN A 34 1 34 HELIX 2 AA2 SER A 35 GLN A 38 5 4 HELIX 3 AA3 ASN A 39 LEU A 58 1 20 HELIX 4 AA4 LEU A 58 THR A 68 1 11 HELIX 5 AA5 CYS A 74 ILE A 108 1 35 HELIX 6 AA6 ARG A 111 VAL A 116 1 6 HELIX 7 AA7 THR A 117 LEU A 137 1 21 HELIX 8 AA8 THR A 138 GLY A 142 5 5 HELIX 9 AA9 LYS A 150 GLN A 157 1 8 HELIX 10 AB1 LEU A 167 VAL A 172 1 6 HELIX 11 AB2 PRO A 173 TYR A 179 1 7 HELIX 12 AB3 VAL A 186 LYS A 1019 1 42 HELIX 13 AB4 ASN A 1022 LYS A 1042 1 21 HELIX 14 AB5 GLU A 1057 GLU A 1081 1 25 HELIX 15 AB6 LYS A 1083 GLN A 1093 1 11 HELIX 16 AB7 GLN A 1093 TYR A 1101 1 9 HELIX 17 AB8 TYR A 1101 CYS A 259 1 47 HELIX 18 AB9 PRO A 266 ILE A 292 1 27 HELIX 19 AC1 ILE A 292 SER A 305 1 14 SHEET 1 AA1 2 CYS A 71 ALA A 73 0 SHEET 2 AA1 2 GLN A 163 ALA A 165 -1 O VAL A 164 N ALA A 72 SSBOND 1 CYS A 71 CYS A 159 1555 1555 2.04 SSBOND 2 CYS A 74 CYS A 146 1555 1555 2.03 SSBOND 3 CYS A 77 CYS A 166 1555 1555 2.03 SSBOND 4 CYS A 259 CYS A 262 1555 1555 2.03 LINK OD1 ASP A 52 NA NA A1203 1555 1555 2.44 LINK OG SER A 91 NA NA A1203 1555 1555 2.46 LINK NA NA A1203 O HOH A1309 1555 1555 2.95 SITE 1 AC1 15 TYR A 9 ALA A 63 ILE A 66 LEU A 85 SITE 2 AC1 15 PHE A 168 GLU A 169 MET A 177 TRP A 246 SITE 3 AC1 15 LEU A 249 HIS A 250 ASN A 253 TYR A 271 SITE 4 AC1 15 ILE A 274 HOH A1321 HOH A1322 SITE 1 AC2 3 PHE A 133 OLC A1224 OLC A1226 SITE 1 AC3 3 ASP A 52 SER A 91 HOH A1309 SITE 1 AC4 7 ALA A 72 ALA A 73 GLY A 76 CLR A1206 SITE 2 AC4 7 OLC A1220 OLC A1223 OLC A1224 SITE 1 AC5 4 PRO A 248 CYS A 262 SER A 263 OLC A1222 SITE 1 AC6 5 PHE A 255 CLR A1204 OLA A1219 OLC A1220 SITE 2 AC6 5 OLC A1223 SITE 1 AC7 5 PHE A 44 ALA A 97 ILE A 100 VAL A 116 SITE 2 AC7 5 ILE A 124 SITE 1 AC8 3 LEU A 267 VAL A 275 OLA A1217 SITE 1 AC9 5 LEU A 96 PRO A 189 LEU A 192 OLA A1215 SITE 2 AC9 5 OLC A1226 SITE 1 AD1 5 VAL A 8 LEU A 19 LEU A 22 LEU A 26 SITE 2 AD1 5 PHE A 286 SITE 1 AD2 1 OLC A1222 SITE 1 AD3 6 VAL A 25 TRP A 29 TRP A 32 PHE A 201 SITE 2 AD3 6 VAL A 229 LYS A 233 SITE 1 AD4 2 ILE A 127 OLA A1209 SITE 1 AD5 1 ILE A 287 SITE 1 AD6 2 PHE A 286 OLA A1208 SITE 1 AD7 2 ALA A 236 OLA A1219 SITE 1 AD8 5 TYR A 197 ALA A 236 ALA A 239 CLR A1206 SITE 2 AD8 5 OLA A1218 SITE 1 AD9 5 PHE A 183 PHE A 258 CLR A1204 CLR A1206 SITE 2 AD9 5 OLC A1221 SITE 1 AE1 3 TYR A 179 OLC A1220 OLC A1226 SITE 1 AE2 4 PHE A 255 CLR A1205 OLA A1213 OLC A1227 SITE 1 AE3 6 VAL A 57 PRO A 61 PHE A 70 CLR A1204 SITE 2 AE3 6 CLR A1206 OLC A1227 SITE 1 AE4 9 TYR A 43 LEU A 54 LEU A 58 PHE A 83 SITE 2 AE4 9 ILE A 125 TRP A 129 OLA A1202 CLR A1204 SITE 3 AE4 9 OLC A1225 SITE 1 AE5 6 CYS A 28 GLN A 38 TYR A 43 ALA A 50 SITE 2 AE5 6 ARG A 205 OLC A1224 SITE 1 AE6 9 HIS A 75 MET A 140 LEU A 141 GLY A 142 SITE 2 AE6 9 TYR A 179 ALA A 184 OLA A1202 OLA A1209 SITE 3 AE6 9 OLC A1221 SITE 1 AE7 3 THR A 65 OLC A1222 OLC A1223 SITE 1 AE8 1 THR A 11 CRYST1 39.400 179.334 141.145 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 0.025381 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005576 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007085 0.00000 ATOM 1 N GLY A -1 -20.983 24.862 1.337 1.00 91.02 N ANISOU 1 N GLY A -1 13681 10310 10593 -177 -268 1432 N ATOM 2 CA GLY A -1 -21.639 23.801 2.079 1.00 91.77 C ANISOU 2 CA GLY A -1 13595 10539 10733 -91 -304 1324 C ATOM 3 C GLY A -1 -22.893 23.261 1.413 1.00 89.56 C ANISOU 3 C GLY A -1 13342 10316 10370 17 -422 1330 C ATOM 4 O GLY A -1 -23.925 23.935 1.378 1.00 93.09 O ANISOU 4 O GLY A -1 13843 10693 10835 125 -562 1349 O ATOM 5 N ALA A 0 -22.797 22.037 0.895 1.00 80.52 N ANISOU 5 N ALA A 0 12158 9296 9140 -11 -370 1311 N ATOM 6 CA ALA A 0 -23.921 21.401 0.223 1.00 73.70 C ANISOU 6 CA ALA A 0 11315 8495 8193 73 -482 1311 C ATOM 7 C ALA A 0 -25.064 21.153 1.208 1.00 71.96 C ANISOU 7 C ALA A 0 10935 8325 8080 196 -593 1224 C ATOM 8 O ALA A 0 -24.833 21.001 2.412 1.00 70.69 O ANISOU 8 O ALA A 0 10626 8198 8035 199 -545 1144 O ATOM 9 CB ALA A 0 -23.483 20.081 -0.408 1.00 69.10 C ANISOU 9 CB ALA A 0 10715 8033 7507 9 -390 1292 C ATOM 10 N PRO A 1 -26.305 21.107 0.726 1.00 72.33 N ANISOU 10 N PRO A 1 11009 8381 8093 297 -741 1237 N ATOM 11 CA PRO A 1 -27.442 20.852 1.622 1.00 73.96 C ANISOU 11 CA PRO A 1 11051 8643 8406 413 -838 1155 C ATOM 12 C PRO A 1 -27.294 19.516 2.326 1.00 72.10 C ANISOU 12 C PRO A 1 10639 8551 8205 382 -758 1060 C ATOM 13 O PRO A 1 -26.916 18.510 1.707 1.00 70.48 O ANISOU 13 O PRO A 1 10447 8423 7909 316 -701 1060 O ATOM 14 CB PRO A 1 -28.656 20.858 0.677 1.00 73.23 C ANISOU 14 CB PRO A 1 11028 8550 8246 502 -1004 1198 C ATOM 15 CG PRO A 1 -28.097 20.715 -0.694 1.00 73.40 C ANISOU 15 CG PRO A 1 11182 8575 8131 408 -951 1258 C ATOM 16 CD PRO A 1 -26.743 21.347 -0.659 1.00 73.33 C ANISOU 16 CD PRO A 1 11265 8486 8111 304 -812 1303 C ATOM 17 N PRO A 2 -27.576 19.471 3.631 1.00 66.87 N ANISOU 17 N PRO A 2 9818 7920 7669 430 -750 977 N ATOM 18 CA PRO A 2 -27.322 18.240 4.393 1.00 63.91 C ANISOU 18 CA PRO A 2 9286 7669 7327 392 -666 893 C ATOM 19 C PRO A 2 -28.199 17.074 3.982 1.00 62.22 C ANISOU 19 C PRO A 2 9007 7564 7070 421 -726 865 C ATOM 20 O PRO A 2 -27.809 15.923 4.213 1.00 61.06 O ANISOU 20 O PRO A 2 8780 7509 6910 365 -649 819 O ATOM 21 CB PRO A 2 -27.600 18.659 5.845 1.00 62.85 C ANISOU 21 CB PRO A 2 9025 7528 7327 451 -664 821 C ATOM 22 CG PRO A 2 -27.588 20.167 5.832 1.00 64.43 C ANISOU 22 CG PRO A 2 9334 7586 7562 491 -711 866 C ATOM 23 CD PRO A 2 -28.089 20.554 4.483 1.00 65.96 C ANISOU 23 CD PRO A 2 9672 7724 7666 520 -809 955 C ATOM 24 N ILE A 3 -29.362 17.325 3.374 1.00 61.14 N ANISOU 24 N ILE A 3 8902 7416 6914 504 -869 892 N ATOM 25 CA ILE A 3 -30.276 16.235 3.055 1.00 62.79 C ANISOU 25 CA ILE A 3 9033 7728 7097 527 -941 859 C ATOM 26 C ILE A 3 -29.775 15.396 1.885 1.00 64.13 C ANISOU 26 C ILE A 3 9313 7931 7123 443 -911 893 C ATOM 27 O ILE A 3 -30.156 14.226 1.760 1.00 64.48 O ANISOU 27 O ILE A 3 9288 8068 7143 425 -925 849 O ATOM 28 CB ILE A 3 -31.687 16.788 2.780 1.00 64.42 C ANISOU 28 CB ILE A 3 9225 7914 7340 645 -1114 876 C ATOM 29 CG1 ILE A 3 -32.705 15.650 2.675 1.00 64.63 C ANISOU 29 CG1 ILE A 3 9130 8055 7373 666 -1190 828 C ATOM 30 CG2 ILE A 3 -31.692 17.629 1.523 1.00 66.58 C ANISOU 30 CG2 ILE A 3 9697 8087 7512 658 -1203 976 C ATOM 31 CD1 ILE A 3 -34.089 16.104 2.278 1.00 65.85 C ANISOU 31 CD1 ILE A 3 9258 8199 7562 777 -1372 846 C ATOM 32 N MET A 4 -28.917 15.952 1.027 1.00 61.41 N ANISOU 32 N MET A 4 9142 7511 6680 386 -865 967 N ATOM 33 CA MET A 4 -28.365 15.162 -0.069 1.00 58.10 C ANISOU 33 CA MET A 4 8835 7124 6115 306 -814 993 C ATOM 34 C MET A 4 -27.451 14.061 0.456 1.00 54.26 C ANISOU 34 C MET A 4 8255 6716 5645 229 -662 928 C ATOM 35 O MET A 4 -27.641 12.880 0.141 1.00 50.20 O ANISOU 35 O MET A 4 7714 6281 5080 206 -661 887 O ATOM 36 CB MET A 4 -27.620 16.068 -1.045 1.00 61.28 C ANISOU 36 CB MET A 4 9445 7427 6410 259 -779 1091 C ATOM 37 CG MET A 4 -28.496 17.129 -1.671 1.00 65.07 C ANISOU 37 CG MET A 4 9994 7834 6894 330 -916 1142 C ATOM 38 SD MET A 4 -27.614 18.065 -2.925 1.00 69.81 S ANISOU 38 SD MET A 4 10785 8344 7395 253 -839 1228 S ATOM 39 CE MET A 4 -27.263 16.776 -4.119 1.00 70.40 C ANISOU 39 CE MET A 4 10911 8514 7324 175 -770 1205 C ATOM 40 N GLY A 5 -26.453 14.429 1.264 1.00 53.87 N ANISOU 40 N GLY A 5 8158 6640 5669 188 -541 917 N ATOM 41 CA GLY A 5 -25.607 13.423 1.882 1.00 45.73 C ANISOU 41 CA GLY A 5 7023 5681 4673 128 -411 854 C ATOM 42 C GLY A 5 -26.351 12.559 2.882 1.00 39.41 C ANISOU 42 C GLY A 5 6049 4964 3962 171 -449 772 C ATOM 43 O GLY A 5 -26.010 11.388 3.070 1.00 33.03 O ANISOU 43 O GLY A 5 5176 4226 3148 133 -383 723 O ATOM 44 N SER A 6 -27.375 13.118 3.530 1.00 40.28 N ANISOU 44 N SER A 6 6085 5064 4157 253 -550 757 N ATOM 45 CA SER A 6 -28.165 12.349 4.484 1.00 39.02 C ANISOU 45 CA SER A 6 5760 4984 4080 291 -581 683 C ATOM 46 C SER A 6 -29.035 11.310 3.784 1.00 38.18 C ANISOU 46 C SER A 6 5644 4946 3916 296 -660 667 C ATOM 47 O SER A 6 -29.285 10.237 4.343 1.00 40.31 O ANISOU 47 O SER A 6 5801 5292 4222 281 -641 609 O ATOM 48 CB SER A 6 -29.021 13.301 5.327 1.00 43.73 C ANISOU 48 CB SER A 6 6281 5550 4782 381 -655 669 C ATOM 49 OG SER A 6 -29.726 12.624 6.352 1.00 50.48 O ANISOU 49 OG SER A 6 6973 6485 5720 413 -662 598 O ATOM 50 N SER A 7 -29.492 11.599 2.563 1.00 37.17 N ANISOU 50 N SER A 7 5642 4788 3695 311 -756 721 N ATOM 51 CA SER A 7 -30.328 10.647 1.837 1.00 32.64 C ANISOU 51 CA SER A 7 5071 4273 3059 309 -849 704 C ATOM 52 C SER A 7 -29.549 9.393 1.463 1.00 30.16 C ANISOU 52 C SER A 7 4791 4004 2667 225 -751 674 C ATOM 53 O SER A 7 -30.096 8.286 1.486 1.00 32.18 O ANISOU 53 O SER A 7 4979 4324 2923 211 -786 625 O ATOM 54 CB SER A 7 -30.907 11.305 0.586 1.00 37.03 C ANISOU 54 CB SER A 7 5774 4777 3519 344 -981 773 C ATOM 55 OG SER A 7 -31.700 12.430 0.922 1.00 38.46 O ANISOU 55 OG SER A 7 5918 4911 3782 435 -1084 798 O ATOM 56 N VAL A 8 -28.273 9.546 1.104 1.00 31.52 N ANISOU 56 N VAL A 8 5064 4138 2775 168 -626 702 N ATOM 57 CA VAL A 8 -27.446 8.380 0.818 1.00 27.79 C ANISOU 57 CA VAL A 8 4614 3705 2241 100 -517 666 C ATOM 58 C VAL A 8 -27.206 7.575 2.087 1.00 30.77 C ANISOU 58 C VAL A 8 4825 4135 2730 89 -445 598 C ATOM 59 O VAL A 8 -27.295 6.341 2.082 1.00 30.44 O ANISOU 59 O VAL A 8 4746 4144 2675 63 -431 548 O ATOM 60 CB VAL A 8 -26.123 8.807 0.162 1.00 26.77 C ANISOU 60 CB VAL A 8 4616 3526 2029 45 -390 713 C ATOM 61 CG1 VAL A 8 -25.206 7.602 -0.017 1.00 22.77 C ANISOU 61 CG1 VAL A 8 4111 3061 1480 -13 -262 667 C ATOM 62 CG2 VAL A 8 -26.397 9.467 -1.166 1.00 24.68 C ANISOU 62 CG2 VAL A 8 4537 3210 1629 48 -461 784 C ATOM 63 N TYR A 9 -26.896 8.256 3.192 1.00 33.78 N ANISOU 63 N TYR A 9 5115 4500 3220 108 -402 595 N ATOM 64 CA TYR A 9 -26.662 7.558 4.451 1.00 24.47 C ANISOU 64 CA TYR A 9 3791 3368 2139 100 -340 536 C ATOM 65 C TYR A 9 -27.906 6.795 4.894 1.00 22.03 C ANISOU 65 C TYR A 9 3376 3120 1875 128 -429 491 C ATOM 66 O TYR A 9 -27.823 5.621 5.271 1.00 21.41 O ANISOU 66 O TYR A 9 3235 3088 1811 97 -391 445 O ATOM 67 CB TYR A 9 -26.213 8.552 5.522 1.00 23.83 C ANISOU 67 CB TYR A 9 3648 3252 2153 118 -298 540 C ATOM 68 CG TYR A 9 -26.373 8.047 6.940 1.00 26.38 C ANISOU 68 CG TYR A 9 3822 3624 2577 130 -276 483 C ATOM 69 CD1 TYR A 9 -25.510 7.091 7.465 1.00 22.34 C ANISOU 69 CD1 TYR A 9 3260 3146 2084 85 -183 449 C ATOM 70 CD2 TYR A 9 -27.386 8.531 7.755 1.00 25.81 C ANISOU 70 CD2 TYR A 9 3663 3563 2579 190 -345 464 C ATOM 71 CE1 TYR A 9 -25.653 6.634 8.762 1.00 17.69 C ANISOU 71 CE1 TYR A 9 2552 2597 1574 93 -168 404 C ATOM 72 CE2 TYR A 9 -27.540 8.079 9.050 1.00 25.72 C ANISOU 72 CE2 TYR A 9 3530 3597 2645 196 -316 414 C ATOM 73 CZ TYR A 9 -26.674 7.130 9.548 1.00 20.20 C ANISOU 73 CZ TYR A 9 2796 2928 1952 145 -230 387 C ATOM 74 OH TYR A 9 -26.833 6.688 10.840 1.00 19.40 O ANISOU 74 OH TYR A 9 2589 2868 1916 150 -206 345 O ATOM 75 N ILE A 10 -29.076 7.441 4.825 1.00 22.81 N ANISOU 75 N ILE A 10 3452 3215 1999 187 -548 505 N ATOM 76 CA ILE A 10 -30.317 6.804 5.266 1.00 22.02 C ANISOU 76 CA ILE A 10 3233 3177 1957 211 -630 465 C ATOM 77 C ILE A 10 -30.636 5.590 4.405 1.00 25.80 C ANISOU 77 C ILE A 10 3751 3692 2360 166 -672 446 C ATOM 78 O ILE A 10 -31.014 4.530 4.918 1.00 29.87 O ANISOU 78 O ILE A 10 4174 4260 2916 139 -667 400 O ATOM 79 CB ILE A 10 -31.475 7.819 5.253 1.00 22.66 C ANISOU 79 CB ILE A 10 3279 3244 2086 292 -752 486 C ATOM 80 CG1 ILE A 10 -31.302 8.844 6.370 1.00 21.86 C ANISOU 80 CG1 ILE A 10 3114 3114 2080 341 -707 481 C ATOM 81 CG2 ILE A 10 -32.812 7.115 5.380 1.00 21.21 C ANISOU 81 CG2 ILE A 10 2979 3129 1951 309 -849 450 C ATOM 82 CD1 ILE A 10 -32.370 9.905 6.372 1.00 21.87 C ANISOU 82 CD1 ILE A 10 3085 3089 2135 434 -817 498 C ATOM 83 N THR A 11 -30.489 5.727 3.085 1.00 27.11 N ANISOU 83 N THR A 11 4067 3825 2410 152 -714 483 N ATOM 84 CA THR A 11 -30.779 4.618 2.179 1.00 28.76 C ANISOU 84 CA THR A 11 4338 4060 2531 108 -761 460 C ATOM 85 C THR A 11 -29.871 3.425 2.454 1.00 27.57 C ANISOU 85 C THR A 11 4182 3926 2368 48 -638 415 C ATOM 86 O THR A 11 -30.324 2.272 2.448 1.00 20.87 O ANISOU 86 O THR A 11 3297 3112 1520 15 -668 370 O ATOM 87 CB THR A 11 -30.632 5.080 0.730 1.00 30.18 C ANISOU 87 CB THR A 11 4705 4194 2569 105 -813 510 C ATOM 88 OG1 THR A 11 -31.462 6.227 0.509 1.00 26.28 O ANISOU 88 OG1 THR A 11 4219 3674 2093 170 -937 558 O ATOM 89 CG2 THR A 11 -31.039 3.972 -0.224 1.00 24.47 C ANISOU 89 CG2 THR A 11 4057 3494 1746 63 -880 480 C ATOM 90 N VAL A 12 -28.583 3.681 2.695 1.00 24.30 N ANISOU 90 N VAL A 12 3800 3483 1949 33 -503 426 N ATOM 91 CA VAL A 12 -27.665 2.599 3.033 1.00 25.22 C ANISOU 91 CA VAL A 12 3898 3612 2071 -10 -387 384 C ATOM 92 C VAL A 12 -28.045 1.977 4.372 1.00 25.86 C ANISOU 92 C VAL A 12 3821 3735 2270 -9 -381 342 C ATOM 93 O VAL A 12 -28.058 0.748 4.517 1.00 26.01 O ANISOU 93 O VAL A 12 3816 3775 2292 -42 -364 300 O ATOM 94 CB VAL A 12 -26.211 3.110 3.027 1.00 27.11 C ANISOU 94 CB VAL A 12 4187 3817 2297 -24 -250 408 C ATOM 95 CG1 VAL A 12 -25.263 2.045 3.560 1.00 18.67 C ANISOU 95 CG1 VAL A 12 3070 2763 1263 -53 -136 364 C ATOM 96 CG2 VAL A 12 -25.804 3.534 1.620 1.00 20.45 C ANISOU 96 CG2 VAL A 12 3514 2935 1319 -39 -236 449 C ATOM 97 N GLU A 13 -28.383 2.808 5.363 1.00 26.05 N ANISOU 97 N GLU A 13 3744 3766 2386 29 -395 354 N ATOM 98 CA GLU A 13 -28.782 2.286 6.668 1.00 22.74 C ANISOU 98 CA GLU A 13 3185 3389 2067 30 -384 318 C ATOM 99 C GLU A 13 -30.010 1.395 6.555 1.00 20.76 C ANISOU 99 C GLU A 13 2881 3181 1827 14 -474 290 C ATOM 100 O GLU A 13 -30.082 0.340 7.199 1.00 21.39 O ANISOU 100 O GLU A 13 2896 3287 1944 -21 -445 256 O ATOM 101 CB GLU A 13 -29.054 3.435 7.637 1.00 25.98 C ANISOU 101 CB GLU A 13 3514 3798 2559 80 -390 331 C ATOM 102 CG GLU A 13 -27.813 4.154 8.108 1.00 27.94 C ANISOU 102 CG GLU A 13 3784 4007 2824 82 -295 347 C ATOM 103 CD GLU A 13 -27.174 3.498 9.315 1.00 32.13 C ANISOU 103 CD GLU A 13 4234 4560 3413 60 -214 315 C ATOM 104 OE1 GLU A 13 -27.251 4.080 10.417 1.00 34.13 O ANISOU 104 OE1 GLU A 13 4416 4818 3733 86 -202 306 O ATOM 105 OE2 GLU A 13 -26.602 2.399 9.166 1.00 34.31 O ANISOU 105 OE2 GLU A 13 4526 4844 3665 21 -166 297 O ATOM 106 N LEU A 14 -30.986 1.801 5.740 1.00 21.14 N ANISOU 106 N LEU A 14 2956 3233 1845 35 -591 306 N ATOM 107 CA LEU A 14 -32.187 0.991 5.578 1.00 22.69 C ANISOU 107 CA LEU A 14 3092 3472 2060 12 -690 280 C ATOM 108 C LEU A 14 -31.881 -0.318 4.861 1.00 22.48 C ANISOU 108 C LEU A 14 3149 3436 1957 -53 -682 250 C ATOM 109 O LEU A 14 -32.444 -1.364 5.205 1.00 23.66 O ANISOU 109 O LEU A 14 3232 3615 2144 -97 -705 215 O ATOM 110 CB LEU A 14 -33.258 1.786 4.836 1.00 30.17 C ANISOU 110 CB LEU A 14 4045 4422 2995 56 -831 306 C ATOM 111 CG LEU A 14 -33.815 2.986 5.612 1.00 35.62 C ANISOU 111 CG LEU A 14 4633 5121 3781 131 -853 324 C ATOM 112 CD1 LEU A 14 -35.013 3.572 4.891 1.00 41.53 C ANISOU 112 CD1 LEU A 14 5367 5878 4534 179 -1010 345 C ATOM 113 CD2 LEU A 14 -34.178 2.603 7.051 1.00 29.91 C ANISOU 113 CD2 LEU A 14 3747 4449 3171 127 -794 288 C ATOM 114 N ALA A 15 -30.986 -0.285 3.870 1.00 21.67 N ANISOU 114 N ALA A 15 3197 3291 1746 -63 -644 262 N ATOM 115 CA ALA A 15 -30.592 -1.517 3.196 1.00 22.55 C ANISOU 115 CA ALA A 15 3400 3387 1780 -116 -621 225 C ATOM 116 C ALA A 15 -29.910 -2.477 4.162 1.00 22.47 C ANISOU 116 C ALA A 15 3329 3378 1831 -143 -512 191 C ATOM 117 O ALA A 15 -30.152 -3.690 4.119 1.00 25.50 O ANISOU 117 O ALA A 15 3715 3761 2212 -188 -527 151 O ATOM 118 CB ALA A 15 -29.673 -1.200 2.015 1.00 22.31 C ANISOU 118 CB ALA A 15 3543 3314 1621 -114 -575 244 C ATOM 119 N ILE A 16 -29.061 -1.952 5.047 1.00 21.50 N ANISOU 119 N ILE A 16 3154 3251 1765 -117 -412 208 N ATOM 120 CA ILE A 16 -28.384 -2.798 6.026 1.00 22.46 C ANISOU 120 CA ILE A 16 3217 3372 1946 -135 -320 183 C ATOM 121 C ILE A 16 -29.385 -3.367 7.024 1.00 21.60 C ANISOU 121 C ILE A 16 2984 3300 1922 -156 -366 166 C ATOM 122 O ILE A 16 -29.295 -4.537 7.416 1.00 25.76 O ANISOU 122 O ILE A 16 3497 3821 2470 -194 -340 138 O ATOM 123 CB ILE A 16 -27.265 -2.002 6.724 1.00 20.94 C ANISOU 123 CB ILE A 16 2996 3167 1792 -104 -220 206 C ATOM 124 CG1 ILE A 16 -26.167 -1.655 5.719 1.00 21.09 C ANISOU 124 CG1 ILE A 16 3133 3149 1730 -100 -151 220 C ATOM 125 CG2 ILE A 16 -26.701 -2.772 7.914 1.00 16.06 C ANISOU 125 CG2 ILE A 16 2302 2553 1246 -115 -149 186 C ATOM 126 CD1 ILE A 16 -25.129 -0.714 6.260 1.00 28.31 C ANISOU 126 CD1 ILE A 16 4021 4051 2686 -78 -67 248 C ATOM 127 N ALA A 17 -30.359 -2.553 7.441 1.00 20.94 N ANISOU 127 N ALA A 17 2812 3253 1891 -130 -431 184 N ATOM 128 CA ALA A 17 -31.373 -3.027 8.378 1.00 18.17 C ANISOU 128 CA ALA A 17 2335 2946 1623 -153 -463 169 C ATOM 129 C ALA A 17 -32.189 -4.167 7.782 1.00 25.60 C ANISOU 129 C ALA A 17 3288 3893 2546 -214 -540 142 C ATOM 130 O ALA A 17 -32.434 -5.177 8.451 1.00 29.00 O ANISOU 130 O ALA A 17 3666 4332 3021 -263 -520 122 O ATOM 131 CB ALA A 17 -32.283 -1.872 8.792 1.00 19.83 C ANISOU 131 CB ALA A 17 2448 3194 1891 -103 -515 188 C ATOM 132 N VAL A 18 -32.613 -4.027 6.524 1.00 28.67 N ANISOU 132 N VAL A 18 3755 4272 2866 -216 -633 141 N ATOM 133 CA VAL A 18 -33.365 -5.095 5.870 1.00 22.80 C ANISOU 133 CA VAL A 18 3036 3528 2098 -280 -720 109 C ATOM 134 C VAL A 18 -32.531 -6.369 5.807 1.00 22.13 C ANISOU 134 C VAL A 18 3037 3396 1977 -327 -649 76 C ATOM 135 O VAL A 18 -33.011 -7.462 6.129 1.00 19.93 O ANISOU 135 O VAL A 18 2723 3115 1735 -390 -669 50 O ATOM 136 CB VAL A 18 -33.829 -4.651 4.469 1.00 27.67 C ANISOU 136 CB VAL A 18 3748 4137 2628 -269 -839 115 C ATOM 137 CG1 VAL A 18 -34.412 -5.828 3.694 1.00 26.59 C ANISOU 137 CG1 VAL A 18 3668 3987 2447 -342 -929 74 C ATOM 138 CG2 VAL A 18 -34.852 -3.529 4.579 1.00 27.83 C ANISOU 138 CG2 VAL A 18 3667 4202 2706 -220 -932 145 C ATOM 139 N LEU A 19 -31.260 -6.247 5.408 1.00 19.25 N ANISOU 139 N LEU A 19 2782 2989 1544 -298 -561 77 N ATOM 140 CA LEU A 19 -30.423 -7.435 5.261 1.00 31.29 C ANISOU 140 CA LEU A 19 4391 4464 3036 -328 -492 41 C ATOM 141 C LEU A 19 -30.111 -8.073 6.611 1.00 30.01 C ANISOU 141 C LEU A 19 4139 4300 2965 -341 -418 40 C ATOM 142 O LEU A 19 -30.051 -9.303 6.721 1.00 28.49 O ANISOU 142 O LEU A 19 3975 4070 2778 -385 -409 10 O ATOM 143 CB LEU A 19 -29.136 -7.084 4.519 1.00 29.67 C ANISOU 143 CB LEU A 19 4306 4221 2745 -288 -406 43 C ATOM 144 CG LEU A 19 -29.309 -6.721 3.043 1.00 30.44 C ANISOU 144 CG LEU A 19 4538 4307 2721 -286 -467 40 C ATOM 145 CD1 LEU A 19 -27.980 -6.291 2.435 1.00 30.29 C ANISOU 145 CD1 LEU A 19 4626 4258 2625 -249 -354 48 C ATOM 146 CD2 LEU A 19 -29.911 -7.886 2.269 1.00 21.09 C ANISOU 146 CD2 LEU A 19 3438 3097 1479 -342 -548 -12 C ATOM 147 N ALA A 20 -29.905 -7.257 7.648 1.00 26.47 N ANISOU 147 N ALA A 20 3592 3883 2581 -303 -368 74 N ATOM 148 CA ALA A 20 -29.637 -7.800 8.978 1.00 29.24 C ANISOU 148 CA ALA A 20 3867 4235 3006 -315 -305 78 C ATOM 149 C ALA A 20 -30.841 -8.562 9.513 1.00 29.34 C ANISOU 149 C ALA A 20 3802 4271 3073 -378 -363 71 C ATOM 150 O ALA A 20 -30.687 -9.629 10.118 1.00 30.46 O ANISOU 150 O ALA A 20 3945 4385 3244 -418 -331 62 O ATOM 151 CB ALA A 20 -29.246 -6.678 9.941 1.00 16.25 C ANISOU 151 CB ALA A 20 2144 2622 1408 -263 -252 111 C ATOM 152 N ILE A 21 -32.045 -8.029 9.296 1.00 27.99 N ANISOU 152 N ILE A 21 3563 4150 2923 -389 -448 76 N ATOM 153 CA ILE A 21 -33.256 -8.686 9.779 1.00 27.02 C ANISOU 153 CA ILE A 21 3347 4058 2863 -456 -499 71 C ATOM 154 C ILE A 21 -33.486 -9.995 9.034 1.00 25.70 C ANISOU 154 C ILE A 21 3260 3842 2663 -531 -552 36 C ATOM 155 O ILE A 21 -33.682 -11.048 9.650 1.00 28.46 O ANISOU 155 O ILE A 21 3590 4171 3053 -595 -533 30 O ATOM 156 CB ILE A 21 -34.466 -7.744 9.648 1.00 27.31 C ANISOU 156 CB ILE A 21 3277 4162 2938 -439 -581 82 C ATOM 157 CG1 ILE A 21 -34.336 -6.563 10.612 1.00 21.64 C ANISOU 157 CG1 ILE A 21 2472 3484 2265 -369 -520 109 C ATOM 158 CG2 ILE A 21 -35.758 -8.500 9.898 1.00 19.93 C ANISOU 158 CG2 ILE A 21 2243 3261 2069 -519 -643 71 C ATOM 159 CD1 ILE A 21 -35.400 -5.502 10.414 1.00 18.98 C ANISOU 159 CD1 ILE A 21 2042 3203 1968 -327 -597 118 C ATOM 160 N LEU A 22 -33.455 -9.950 7.699 1.00 26.73 N ANISOU 160 N LEU A 22 3494 3948 2715 -526 -619 13 N ATOM 161 CA LEU A 22 -33.741 -11.143 6.905 1.00 26.95 C ANISOU 161 CA LEU A 22 3611 3925 2703 -598 -683 -29 C ATOM 162 C LEU A 22 -32.758 -12.265 7.216 1.00 26.84 C ANISOU 162 C LEU A 22 3683 3837 2679 -614 -597 -49 C ATOM 163 O LEU A 22 -33.162 -13.401 7.492 1.00 27.26 O ANISOU 163 O LEU A 22 3737 3854 2766 -690 -617 -67 O ATOM 164 CB LEU A 22 -33.708 -10.803 5.414 1.00 28.42 C ANISOU 164 CB LEU A 22 3920 4096 2783 -579 -759 -50 C ATOM 165 CG LEU A 22 -34.854 -9.960 4.855 1.00 30.87 C ANISOU 165 CG LEU A 22 4169 4464 3095 -576 -888 -36 C ATOM 166 CD1 LEU A 22 -34.631 -9.652 3.390 1.00 22.95 C ANISOU 166 CD1 LEU A 22 3321 3434 1965 -553 -955 -52 C ATOM 167 CD2 LEU A 22 -36.169 -10.681 5.058 1.00 31.91 C ANISOU 167 CD2 LEU A 22 4202 4622 3303 -664 -989 -53 C ATOM 168 N GLY A 23 -31.460 -11.961 7.181 1.00 19.77 N ANISOU 168 N GLY A 23 2855 2913 1743 -544 -501 -45 N ATOM 169 CA GLY A 23 -30.461 -13.000 7.359 1.00 19.64 C ANISOU 169 CA GLY A 23 2922 2822 1720 -543 -425 -68 C ATOM 170 C GLY A 23 -30.508 -13.644 8.729 1.00 21.25 C ANISOU 170 C GLY A 23 3047 3017 2011 -574 -383 -44 C ATOM 171 O GLY A 23 -30.378 -14.864 8.857 1.00 25.40 O ANISOU 171 O GLY A 23 3629 3474 2547 -616 -378 -66 O ATOM 172 N ASN A 24 -30.701 -12.844 9.771 1.00 19.32 N ANISOU 172 N ASN A 24 2681 2835 1823 -553 -354 0 N ATOM 173 CA ASN A 24 -30.669 -13.384 11.121 1.00 29.75 C ANISOU 173 CA ASN A 24 3943 4152 3211 -578 -306 27 C ATOM 174 C ASN A 24 -32.007 -13.956 11.568 1.00 36.31 C ANISOU 174 C ASN A 24 4698 5004 4093 -673 -360 35 C ATOM 175 O ASN A 24 -32.027 -14.817 12.454 1.00 34.98 O ANISOU 175 O ASN A 24 4522 4805 3963 -720 -329 52 O ATOM 176 CB ASN A 24 -30.179 -12.313 12.100 1.00 17.33 C ANISOU 176 CB ASN A 24 2289 2630 1665 -514 -242 66 C ATOM 177 CG ASN A 24 -28.718 -11.955 11.873 1.00 16.75 C ANISOU 177 CG ASN A 24 2279 2525 1560 -435 -177 62 C ATOM 178 OD1 ASN A 24 -27.822 -12.721 12.216 1.00 28.62 O ANISOU 178 OD1 ASN A 24 3830 3972 3072 -421 -130 59 O ATOM 179 ND2 ASN A 24 -28.476 -10.801 11.272 1.00 17.43 N ANISOU 179 ND2 ASN A 24 2364 2644 1614 -384 -175 64 N ATOM 180 N VAL A 25 -33.123 -13.521 10.977 1.00 35.73 N ANISOU 180 N VAL A 25 4568 4984 4025 -705 -443 26 N ATOM 181 CA VAL A 25 -34.369 -14.253 11.181 1.00 31.17 C ANISOU 181 CA VAL A 25 3925 4419 3501 -809 -502 24 C ATOM 182 C VAL A 25 -34.260 -15.640 10.557 1.00 32.49 C ANISOU 182 C VAL A 25 4213 4490 3642 -878 -540 -13 C ATOM 183 O VAL A 25 -34.785 -16.624 11.090 1.00 33.78 O ANISOU 183 O VAL A 25 4359 4622 3853 -970 -546 -6 O ATOM 184 CB VAL A 25 -35.566 -13.457 10.625 1.00 31.02 C ANISOU 184 CB VAL A 25 3807 4477 3501 -820 -595 19 C ATOM 185 CG1 VAL A 25 -36.802 -14.330 10.548 1.00 22.30 C ANISOU 185 CG1 VAL A 25 2645 3378 2452 -938 -672 7 C ATOM 186 CG2 VAL A 25 -35.855 -12.252 11.501 1.00 20.51 C ANISOU 186 CG2 VAL A 25 2342 3234 2218 -762 -550 54 C ATOM 187 N LEU A 26 -33.535 -15.744 9.440 1.00 31.07 N ANISOU 187 N LEU A 26 4166 4256 3384 -837 -557 -53 N ATOM 188 CA LEU A 26 -33.274 -17.047 8.836 1.00 29.20 C ANISOU 188 CA LEU A 26 4065 3915 3113 -886 -581 -98 C ATOM 189 C LEU A 26 -32.405 -17.917 9.739 1.00 30.73 C ANISOU 189 C LEU A 26 4304 4035 3337 -878 -494 -82 C ATOM 190 O LEU A 26 -32.584 -19.139 9.793 1.00 31.97 O ANISOU 190 O LEU A 26 4526 4109 3511 -950 -515 -99 O ATOM 191 CB LEU A 26 -32.606 -16.863 7.475 1.00 33.58 C ANISOU 191 CB LEU A 26 4756 4435 3567 -829 -599 -147 C ATOM 192 CG LEU A 26 -32.415 -18.123 6.632 1.00 40.12 C ANISOU 192 CG LEU A 26 5743 5157 4346 -873 -634 -209 C ATOM 193 CD1 LEU A 26 -33.766 -18.752 6.316 1.00 40.39 C ANISOU 193 CD1 LEU A 26 5757 5185 4406 -995 -758 -231 C ATOM 194 CD2 LEU A 26 -31.659 -17.798 5.353 1.00 43.30 C ANISOU 194 CD2 LEU A 26 6281 5536 4635 -804 -625 -255 C ATOM 195 N VAL A 27 -31.452 -17.308 10.448 1.00 29.96 N ANISOU 195 N VAL A 27 4179 3959 3246 -791 -404 -49 N ATOM 196 CA VAL A 27 -30.622 -18.062 11.385 1.00 27.38 C ANISOU 196 CA VAL A 27 3887 3566 2950 -775 -333 -27 C ATOM 197 C VAL A 27 -31.482 -18.651 12.498 1.00 25.76 C ANISOU 197 C VAL A 27 3611 3366 2810 -867 -339 15 C ATOM 198 O VAL A 27 -31.388 -19.842 12.817 1.00 23.76 O ANISOU 198 O VAL A 27 3429 3023 2577 -918 -337 18 O ATOM 199 CB VAL A 27 -29.499 -17.169 11.943 1.00 23.41 C ANISOU 199 CB VAL A 27 3351 3099 2446 -668 -251 1 C ATOM 200 CG1 VAL A 27 -28.777 -17.858 13.086 1.00 19.13 C ANISOU 200 CG1 VAL A 27 2822 2502 1942 -653 -196 35 C ATOM 201 CG2 VAL A 27 -28.518 -16.811 10.840 1.00 25.40 C ANISOU 201 CG2 VAL A 27 3686 3329 2636 -587 -227 -40 C ATOM 202 N CYS A 28 -32.344 -17.825 13.097 1.00 27.51 N ANISOU 202 N CYS A 28 3697 3689 3066 -891 -342 50 N ATOM 203 CA CYS A 28 -33.213 -18.306 14.167 1.00 26.01 C ANISOU 203 CA CYS A 28 3431 3516 2934 -984 -331 92 C ATOM 204 C CYS A 28 -34.196 -19.352 13.655 1.00 34.92 C ANISOU 204 C CYS A 28 4584 4598 4087 -1108 -405 69 C ATOM 205 O CYS A 28 -34.466 -20.344 14.343 1.00 39.19 O ANISOU 205 O CYS A 28 5143 5083 4663 -1193 -390 96 O ATOM 206 CB CYS A 28 -33.959 -17.133 14.802 1.00 26.87 C ANISOU 206 CB CYS A 28 3386 3750 3074 -973 -311 122 C ATOM 207 SG CYS A 28 -32.891 -15.810 15.413 1.00 25.41 S ANISOU 207 SG CYS A 28 3173 3618 2863 -839 -235 144 S ATOM 208 N ATRP A 29 -34.723 -19.160 12.443 0.45 36.46 N ANISOU 208 N ATRP A 29 4786 4806 4259 -1125 -491 21 N ATOM 209 N BTRP A 29 -34.759 -19.139 12.460 0.55 36.40 N ANISOU 209 N BTRP A 29 4774 4803 4254 -1126 -491 22 N ATOM 210 CA ATRP A 29 -35.676 -20.112 11.882 0.45 39.52 C ANISOU 210 CA ATRP A 29 5196 5149 4671 -1249 -579 -8 C ATOM 211 CA BTRP A 29 -35.669 -20.126 11.886 0.55 39.54 C ANISOU 211 CA BTRP A 29 5200 5151 4674 -1249 -579 -8 C ATOM 212 C ATRP A 29 -35.016 -21.447 11.548 0.45 35.91 C ANISOU 212 C ATRP A 29 4909 4546 4187 -1276 -585 -39 C ATOM 213 C BTRP A 29 -34.976 -21.467 11.687 0.55 35.72 C ANISOU 213 C BTRP A 29 4882 4522 4168 -1275 -575 -33 C ATOM 214 O ATRP A 29 -35.687 -22.485 11.550 0.45 38.44 O ANISOU 214 O ATRP A 29 5257 4804 4544 -1395 -632 -46 O ATOM 215 O BTRP A 29 -35.576 -22.524 11.912 0.55 37.80 O ANISOU 215 O BTRP A 29 5168 4722 4474 -1392 -606 -29 O ATOM 216 CB ATRP A 29 -36.340 -19.505 10.643 0.45 42.51 C ANISOU 216 CB ATRP A 29 5551 5580 5022 -1249 -684 -53 C ATOM 217 CB BTRP A 29 -36.233 -19.626 10.554 0.55 42.51 C ANISOU 217 CB BTRP A 29 5574 5564 5015 -1248 -685 -59 C ATOM 218 CG ATRP A 29 -37.500 -20.286 10.098 0.45 48.38 C ANISOU 218 CG ATRP A 29 6280 6301 5800 -1384 -794 -82 C ATOM 219 CG BTRP A 29 -37.513 -18.856 10.669 0.55 47.13 C ANISOU 219 CG BTRP A 29 5984 6266 5657 -1290 -738 -41 C ATOM 220 CD1ATRP A 29 -37.607 -20.824 8.850 0.45 51.35 C ANISOU 220 CD1ATRP A 29 6773 6612 6124 -1419 -895 -146 C ATOM 221 CD1BTRP A 29 -37.689 -17.527 10.435 0.55 48.12 C ANISOU 221 CD1BTRP A 29 6022 6489 5773 -1208 -752 -34 C ATOM 222 CD2ATRP A 29 -38.716 -20.614 10.781 0.45 52.04 C ANISOU 222 CD2ATRP A 29 6605 6808 6358 -1507 -814 -52 C ATOM 223 CD2BTRP A 29 -38.796 -19.372 11.041 0.55 49.81 C ANISOU 223 CD2BTRP A 29 6209 6634 6082 -1422 -784 -28 C ATOM 224 NE1ATRP A 29 -38.813 -21.465 8.710 0.45 53.81 N ANISOU 224 NE1ATRP A 29 7027 6922 6496 -1559 -990 -158 N ATOM 225 NE1BTRP A 29 -39.001 -17.177 10.638 0.55 50.24 N ANISOU 225 NE1BTRP A 29 6125 6846 6119 -1269 -806 -21 N ATOM 226 CE2ATRP A 29 -39.513 -21.352 9.882 0.45 54.86 C ANISOU 226 CE2ATRP A 29 6995 7123 6727 -1617 -938 -98 C ATOM 227 CE2BTRP A 29 -39.703 -18.292 11.012 0.55 52.80 C ANISOU 227 CE2BTRP A 29 6422 7135 6504 -1404 -822 -17 C ATOM 228 CE3ATRP A 29 -39.209 -20.356 12.063 0.45 53.18 C ANISOU 228 CE3ATRP A 29 6603 7026 6578 -1537 -734 9 C ATOM 229 CE3BTRP A 29 -39.268 -20.639 11.396 0.55 54.10 C ANISOU 229 CE3BTRP A 29 6773 7107 6674 -1557 -794 -23 C ATOM 230 CZ2ATRP A 29 -40.775 -21.836 10.225 0.45 56.92 C ANISOU 230 CZ2ATRP A 29 7131 7412 7082 -1762 -987 -84 C ATOM 231 CZ2BTRP A 29 -41.054 -18.441 11.323 0.55 54.11 C ANISOU 231 CZ2BTRP A 29 6427 7365 6767 -1511 -866 -5 C ATOM 232 CZ3ATRP A 29 -40.462 -20.838 12.402 0.45 55.42 C ANISOU 232 CZ3ATRP A 29 6767 7341 6949 -1676 -768 24 C ATOM 233 CZ3BTRP A 29 -40.610 -20.785 11.706 0.55 54.43 C ANISOU 233 CZ3BTRP A 29 6661 7212 6808 -1677 -835 -7 C ATOM 234 CH2ATRP A 29 -41.230 -21.569 11.486 0.45 56.25 C ANISOU 234 CH2ATRP A 29 6893 7404 7076 -1789 -895 -21 C ATOM 235 CH2BTRP A 29 -41.487 -19.692 11.667 0.55 55.98 C ANISOU 235 CH2BTRP A 29 6678 7540 7052 -1651 -869 0 C ATOM 236 N ALA A 30 -33.710 -21.446 11.265 1.00 33.77 N ANISOU 236 N ALA A 30 4752 4218 3862 -1167 -535 -59 N ATOM 237 CA ALA A 30 -32.999 -22.697 11.021 1.00 32.40 C ANISOU 237 CA ALA A 30 4738 3901 3670 -1172 -529 -91 C ATOM 238 C ALA A 30 -32.801 -23.480 12.313 1.00 36.02 C ANISOU 238 C ALA A 30 5200 4300 4184 -1207 -474 -33 C ATOM 239 O ALA A 30 -32.973 -24.704 12.337 1.00 35.88 O ANISOU 239 O ALA A 30 5275 4170 4188 -1287 -502 -42 O ATOM 240 CB ALA A 30 -31.653 -22.419 10.352 1.00 27.74 C ANISOU 240 CB ALA A 30 4249 3276 3014 -1037 -482 -131 C ATOM 241 N VAL A 31 -32.445 -22.787 13.398 1.00 34.96 N ANISOU 241 N VAL A 31 4978 4236 4069 -1152 -400 28 N ATOM 242 CA VAL A 31 -32.211 -23.451 14.676 1.00 37.73 C ANISOU 242 CA VAL A 31 5343 4537 4457 -1178 -348 92 C ATOM 243 C VAL A 31 -33.525 -23.907 15.294 1.00 38.00 C ANISOU 243 C VAL A 31 5306 4591 4543 -1329 -368 132 C ATOM 244 O VAL A 31 -33.566 -24.909 16.017 1.00 37.88 O ANISOU 244 O VAL A 31 5350 4489 4554 -1398 -352 173 O ATOM 245 CB VAL A 31 -31.432 -22.511 15.617 1.00 38.84 C ANISOU 245 CB VAL A 31 5418 4750 4591 -1074 -272 139 C ATOM 246 CG1 VAL A 31 -31.233 -23.146 16.985 1.00 33.42 C ANISOU 246 CG1 VAL A 31 4752 4018 3928 -1103 -228 210 C ATOM 247 CG2 VAL A 31 -30.089 -22.131 14.995 1.00 30.69 C ANISOU 247 CG2 VAL A 31 4448 3693 3519 -936 -249 100 C ATOM 248 N TRP A 32 -34.618 -23.191 15.022 1.00 36.30 N ANISOU 248 N TRP A 32 4960 4486 4346 -1383 -401 124 N ATOM 249 CA TRP A 32 -35.911 -23.583 15.573 1.00 39.29 C ANISOU 249 CA TRP A 32 5246 4896 4785 -1530 -412 159 C ATOM 250 C TRP A 32 -36.405 -24.890 14.960 1.00 42.34 C ANISOU 250 C TRP A 32 5728 5165 5196 -1655 -488 128 C ATOM 251 O TRP A 32 -36.990 -25.725 15.656 1.00 46.22 O ANISOU 251 O TRP A 32 6217 5612 5734 -1779 -474 172 O ATOM 252 CB TRP A 32 -36.933 -22.467 15.352 1.00 44.59 C ANISOU 252 CB TRP A 32 5743 5715 5483 -1542 -436 151 C ATOM 253 CG TRP A 32 -38.336 -22.848 15.730 1.00 52.65 C ANISOU 253 CG TRP A 32 6648 6779 6579 -1696 -454 176 C ATOM 254 CD1 TRP A 32 -39.255 -23.496 14.947 1.00 55.41 C ANISOU 254 CD1 TRP A 32 6987 7098 6968 -1817 -550 139 C ATOM 255 CD2 TRP A 32 -38.984 -22.598 16.982 1.00 57.62 C ANISOU 255 CD2 TRP A 32 7148 7491 7254 -1749 -369 239 C ATOM 256 NE1 TRP A 32 -40.428 -23.671 15.640 1.00 57.56 N ANISOU 256 NE1 TRP A 32 7119 7432 7320 -1947 -529 180 N ATOM 257 CE2 TRP A 32 -40.289 -23.126 16.890 1.00 60.80 C ANISOU 257 CE2 TRP A 32 7456 7914 7732 -1906 -410 241 C ATOM 258 CE3 TRP A 32 -38.587 -21.980 18.173 1.00 59.97 C ANISOU 258 CE3 TRP A 32 7405 7849 7533 -1683 -260 292 C ATOM 259 CZ2 TRP A 32 -41.199 -23.052 17.943 1.00 63.83 C ANISOU 259 CZ2 TRP A 32 7699 8380 8176 -1995 -332 296 C ATOM 260 CZ3 TRP A 32 -39.493 -21.910 19.218 1.00 63.63 C ANISOU 260 CZ3 TRP A 32 7745 8390 8042 -1768 -186 344 C ATOM 261 CH2 TRP A 32 -40.783 -22.443 19.096 1.00 64.45 C ANISOU 261 CH2 TRP A 32 7748 8516 8223 -1922 -215 346 C ATOM 262 N LEU A 33 -36.179 -25.089 13.663 1.00 42.72 N ANISOU 262 N LEU A 33 5869 5158 5206 -1630 -566 52 N ATOM 263 CA LEU A 33 -36.719 -26.256 12.970 1.00 44.62 C ANISOU 263 CA LEU A 33 6203 5287 5464 -1752 -653 9 C ATOM 264 C LEU A 33 -35.797 -27.467 13.084 1.00 44.22 C ANISOU 264 C LEU A 33 6341 5062 5397 -1738 -633 3 C ATOM 265 O LEU A 33 -36.212 -28.530 13.555 1.00 49.41 O ANISOU 265 O LEU A 33 7048 5625 6100 -1858 -643 32 O ATOM 266 CB LEU A 33 -36.971 -25.917 11.497 1.00 48.99 C ANISOU 266 CB LEU A 33 6781 5859 5972 -1736 -755 -75 C ATOM 267 CG LEU A 33 -38.012 -24.835 11.220 1.00 52.45 C ANISOU 267 CG LEU A 33 7042 6452 6435 -1758 -806 -74 C ATOM 268 CD1 LEU A 33 -38.067 -24.532 9.736 1.00 52.37 C ANISOU 268 CD1 LEU A 33 7095 6444 6359 -1726 -912 -154 C ATOM 269 CD2 LEU A 33 -39.380 -25.261 11.738 1.00 57.24 C ANISOU 269 CD2 LEU A 33 7519 7094 7138 -1927 -840 -41 C ATOM 270 N ASN A 34 -34.548 -27.320 12.654 1.00 41.64 N ANISOU 270 N ASN A 34 6119 4689 5011 -1592 -604 -33 N ATOM 271 CA ASN A 34 -33.622 -28.442 12.589 1.00 42.64 C ANISOU 271 CA ASN A 34 6427 4648 5126 -1556 -593 -54 C ATOM 272 C ASN A 34 -33.095 -28.766 13.983 1.00 48.11 C ANISOU 272 C ASN A 34 7123 5303 5852 -1535 -515 34 C ATOM 273 O ASN A 34 -32.453 -27.925 14.621 1.00 51.23 O ANISOU 273 O ASN A 34 7449 5781 6235 -1429 -447 74 O ATOM 274 CB ASN A 34 -32.477 -28.115 11.636 1.00 39.63 C ANISOU 274 CB ASN A 34 6137 4243 4676 -1402 -578 -125 C ATOM 275 CG ASN A 34 -31.639 -29.326 11.300 1.00 39.33 C ANISOU 275 CG ASN A 34 6291 4025 4630 -1364 -578 -171 C ATOM 276 OD1 ASN A 34 -31.946 -30.442 11.721 1.00 40.48 O ANISOU 276 OD1 ASN A 34 6513 4050 4819 -1457 -603 -151 O ATOM 277 ND2 ASN A 34 -30.579 -29.117 10.528 1.00 37.10 N ANISOU 277 ND2 ASN A 34 6086 3718 4292 -1227 -546 -233 N ATOM 278 N SER A 35 -33.358 -29.987 14.456 1.00 50.91 N ANISOU 278 N SER A 35 7569 5528 6247 -1638 -531 64 N ATOM 279 CA SER A 35 -32.896 -30.371 15.786 1.00 52.91 C ANISOU 279 CA SER A 35 7846 5734 6522 -1625 -468 154 C ATOM 280 C SER A 35 -31.400 -30.657 15.817 1.00 54.79 C ANISOU 280 C SER A 35 8204 5875 6737 -1463 -438 142 C ATOM 281 O SER A 35 -30.794 -30.599 16.893 1.00 59.24 O ANISOU 281 O SER A 35 8764 6438 7307 -1406 -387 215 O ATOM 282 CB SER A 35 -33.674 -31.588 16.293 1.00 53.65 C ANISOU 282 CB SER A 35 8006 5713 6664 -1794 -494 200 C ATOM 283 OG SER A 35 -33.420 -32.730 15.496 1.00 58.14 O ANISOU 283 OG SER A 35 8749 6104 7237 -1813 -557 137 O ATOM 284 N ASN A 36 -30.792 -30.963 14.669 1.00 50.85 N ANISOU 284 N ASN A 36 7812 5297 6214 -1387 -468 50 N ATOM 285 CA ASN A 36 -29.343 -31.116 14.614 1.00 46.21 C ANISOU 285 CA ASN A 36 7310 4634 5613 -1219 -430 29 C ATOM 286 C ASN A 36 -28.622 -29.805 14.879 1.00 46.20 C ANISOU 286 C ASN A 36 7186 4778 5588 -1089 -368 47 C ATOM 287 O ASN A 36 -27.432 -29.819 15.213 1.00 48.01 O ANISOU 287 O ASN A 36 7447 4971 5825 -957 -329 58 O ATOM 288 CB ASN A 36 -28.924 -31.668 13.255 1.00 47.13 C ANISOU 288 CB ASN A 36 7560 4646 5702 -1169 -462 -84 C ATOM 289 CG ASN A 36 -29.622 -32.963 12.923 1.00 48.23 C ANISOU 289 CG ASN A 36 7834 4630 5863 -1300 -532 -113 C ATOM 290 OD1 ASN A 36 -29.986 -33.727 13.817 1.00 51.33 O ANISOU 290 OD1 ASN A 36 8261 4940 6303 -1392 -544 -42 O ATOM 291 ND2 ASN A 36 -29.824 -33.216 11.635 1.00 46.39 N ANISOU 291 ND2 ASN A 36 7685 4351 5591 -1317 -581 -217 N ATOM 292 N LEU A 37 -29.309 -28.679 14.726 1.00 41.29 N ANISOU 292 N LEU A 37 6426 4316 4946 -1122 -365 49 N ATOM 293 CA LEU A 37 -28.751 -27.377 15.048 1.00 38.37 C ANISOU 293 CA LEU A 37 5938 4083 4557 -1017 -311 71 C ATOM 294 C LEU A 37 -29.051 -26.948 16.478 1.00 36.26 C ANISOU 294 C LEU A 37 5573 3894 4311 -1051 -275 168 C ATOM 295 O LEU A 37 -28.584 -25.890 16.900 1.00 32.45 O ANISOU 295 O LEU A 37 4998 3517 3815 -969 -233 190 O ATOM 296 CB LEU A 37 -29.280 -26.324 14.069 1.00 34.73 C ANISOU 296 CB LEU A 37 5394 3745 4058 -1019 -328 19 C ATOM 297 CG LEU A 37 -28.794 -26.438 12.622 1.00 37.08 C ANISOU 297 CG LEU A 37 5787 3994 4309 -958 -346 -77 C ATOM 298 CD1 LEU A 37 -29.530 -25.448 11.739 1.00 36.07 C ANISOU 298 CD1 LEU A 37 5584 3984 4138 -984 -381 -113 C ATOM 299 CD2 LEU A 37 -27.285 -26.217 12.540 1.00 35.10 C ANISOU 299 CD2 LEU A 37 5571 3719 4046 -797 -279 -95 C ATOM 300 N GLN A 38 -29.811 -27.741 17.231 1.00 36.89 N ANISOU 300 N GLN A 38 5676 3923 4419 -1174 -289 224 N ATOM 301 CA GLN A 38 -30.226 -27.363 18.582 1.00 35.32 C ANISOU 301 CA GLN A 38 5393 3802 4226 -1222 -246 315 C ATOM 302 C GLN A 38 -29.211 -27.910 19.577 1.00 36.89 C ANISOU 302 C GLN A 38 5678 3912 4426 -1152 -225 376 C ATOM 303 O GLN A 38 -29.363 -29.002 20.125 1.00 38.26 O ANISOU 303 O GLN A 38 5951 3969 4617 -1223 -239 424 O ATOM 304 CB GLN A 38 -31.635 -27.864 18.873 1.00 36.70 C ANISOU 304 CB GLN A 38 5535 3981 4428 -1401 -261 348 C ATOM 305 CG GLN A 38 -32.711 -27.171 18.048 1.00 37.07 C ANISOU 305 CG GLN A 38 5463 4141 4483 -1467 -290 298 C ATOM 306 CD GLN A 38 -34.069 -27.835 18.164 1.00 41.61 C ANISOU 306 CD GLN A 38 6006 4702 5101 -1651 -316 319 C ATOM 307 OE1 GLN A 38 -34.189 -28.957 18.655 1.00 47.21 O ANISOU 307 OE1 GLN A 38 6812 5293 5832 -1740 -319 362 O ATOM 308 NE2 GLN A 38 -35.103 -27.141 17.709 1.00 42.49 N ANISOU 308 NE2 GLN A 38 5980 4934 5232 -1711 -339 292 N ATOM 309 N ASN A 39 -28.156 -27.136 19.808 1.00 37.94 N ANISOU 309 N ASN A 39 5776 4098 4543 -1012 -197 376 N ATOM 310 CA ASN A 39 -27.169 -27.435 20.831 1.00 34.91 C ANISOU 310 CA ASN A 39 5448 3656 4159 -934 -187 438 C ATOM 311 C ASN A 39 -26.843 -26.139 21.554 1.00 38.29 C ANISOU 311 C ASN A 39 5761 4228 4561 -868 -148 467 C ATOM 312 O ASN A 39 -27.345 -25.067 21.205 1.00 37.11 O ANISOU 312 O ASN A 39 5497 4207 4397 -877 -126 437 O ATOM 313 CB ASN A 39 -25.917 -28.078 20.228 1.00 34.68 C ANISOU 313 CB ASN A 39 5521 3502 4155 -810 -210 391 C ATOM 314 CG ASN A 39 -25.368 -27.288 19.066 1.00 38.48 C ANISOU 314 CG ASN A 39 5947 4045 4629 -712 -194 303 C ATOM 315 OD1 ASN A 39 -24.596 -26.349 19.249 1.00 47.54 O ANISOU 315 OD1 ASN A 39 7017 5277 5771 -611 -166 304 O ATOM 316 ND2 ASN A 39 -25.772 -27.657 17.858 1.00 36.85 N ANISOU 316 ND2 ASN A 39 5788 3795 4419 -747 -214 228 N ATOM 317 N VAL A 40 -25.987 -26.238 22.570 1.00 40.40 N ANISOU 317 N VAL A 40 6063 4465 4821 -800 -147 526 N ATOM 318 CA VAL A 40 -25.700 -25.072 23.395 1.00 32.99 C ANISOU 318 CA VAL A 40 5031 3652 3853 -749 -118 557 C ATOM 319 C VAL A 40 -24.984 -24.002 22.584 1.00 31.58 C ANISOU 319 C VAL A 40 4767 3550 3682 -639 -108 488 C ATOM 320 O VAL A 40 -25.280 -22.808 22.711 1.00 33.23 O ANISOU 320 O VAL A 40 4870 3888 3869 -636 -79 480 O ATOM 321 CB VAL A 40 -24.896 -25.489 24.636 1.00 30.57 C ANISOU 321 CB VAL A 40 4796 3287 3533 -702 -138 634 C ATOM 322 CG1 VAL A 40 -24.435 -24.267 25.398 1.00 28.42 C ANISOU 322 CG1 VAL A 40 4437 3136 3227 -637 -120 651 C ATOM 323 CG2 VAL A 40 -25.747 -26.380 25.520 1.00 24.44 C ANISOU 323 CG2 VAL A 40 4100 2453 2732 -828 -134 713 C ATOM 324 N THR A 41 -24.047 -24.407 21.723 1.00 33.78 N ANISOU 324 N THR A 41 5092 3749 3993 -548 -125 436 N ATOM 325 CA THR A 41 -23.302 -23.433 20.931 1.00 33.40 C ANISOU 325 CA THR A 41 4970 3769 3952 -449 -104 375 C ATOM 326 C THR A 41 -24.239 -22.562 20.105 1.00 35.15 C ANISOU 326 C THR A 41 5114 4092 4148 -505 -84 330 C ATOM 327 O THR A 41 -24.073 -21.339 20.045 1.00 37.42 O ANISOU 327 O THR A 41 5309 4486 4422 -464 -61 318 O ATOM 328 CB THR A 41 -22.303 -24.146 20.022 1.00 34.84 C ANISOU 328 CB THR A 41 5222 3844 4171 -357 -111 319 C ATOM 329 OG1 THR A 41 -21.559 -25.102 20.787 1.00 41.78 O ANISOU 329 OG1 THR A 41 6181 4612 5083 -308 -142 364 O ATOM 330 CG2 THR A 41 -21.341 -23.141 19.402 1.00 34.75 C ANISOU 330 CG2 THR A 41 5131 3903 4169 -250 -76 271 C ATOM 331 N ASN A 42 -25.239 -23.174 19.475 1.00 35.12 N ANISOU 331 N ASN A 42 5149 4054 4140 -600 -101 307 N ATOM 332 CA ASN A 42 -26.177 -22.432 18.647 1.00 31.78 C ANISOU 332 CA ASN A 42 4656 3720 3697 -652 -101 265 C ATOM 333 C ASN A 42 -27.192 -21.640 19.458 1.00 26.09 C ANISOU 333 C ASN A 42 3832 3116 2965 -724 -85 309 C ATOM 334 O ASN A 42 -27.843 -20.752 18.899 1.00 27.73 O ANISOU 334 O ASN A 42 3959 3416 3162 -740 -85 280 O ATOM 335 CB ASN A 42 -26.896 -23.383 17.691 1.00 32.73 C ANISOU 335 CB ASN A 42 4853 3763 3821 -733 -139 221 C ATOM 336 CG ASN A 42 -25.968 -23.947 16.636 1.00 32.78 C ANISOU 336 CG ASN A 42 4957 3672 3827 -652 -145 154 C ATOM 337 OD1 ASN A 42 -24.889 -23.405 16.397 1.00 33.90 O ANISOU 337 OD1 ASN A 42 5081 3832 3966 -538 -112 133 O ATOM 338 ND2 ASN A 42 -26.385 -25.032 15.992 1.00 33.98 N ANISOU 338 ND2 ASN A 42 5211 3718 3982 -714 -182 118 N ATOM 339 N TYR A 43 -27.344 -21.928 20.753 1.00 25.53 N ANISOU 339 N TYR A 43 3767 3040 2892 -762 -70 378 N ATOM 340 CA TYR A 43 -28.190 -21.076 21.580 1.00 29.95 C ANISOU 340 CA TYR A 43 4227 3718 3435 -812 -37 414 C ATOM 341 C TYR A 43 -27.558 -19.702 21.763 1.00 27.82 C ANISOU 341 C TYR A 43 3879 3543 3148 -714 -14 403 C ATOM 342 O TYR A 43 -28.265 -18.689 21.808 1.00 27.87 O ANISOU 342 O TYR A 43 3787 3655 3146 -729 6 394 O ATOM 343 CB TYR A 43 -28.464 -21.738 22.929 1.00 35.52 C ANISOU 343 CB TYR A 43 4975 4394 4128 -879 -18 492 C ATOM 344 CG TYR A 43 -29.205 -23.049 22.811 1.00 45.18 C ANISOU 344 CG TYR A 43 6271 5523 5371 -996 -37 511 C ATOM 345 CD1 TYR A 43 -30.002 -23.319 21.702 1.00 53.31 C ANISOU 345 CD1 TYR A 43 7284 6543 6428 -1064 -66 459 C ATOM 346 CD2 TYR A 43 -29.104 -24.023 23.798 1.00 45.10 C ANISOU 346 CD2 TYR A 43 6357 5427 5351 -1044 -33 583 C ATOM 347 CE1 TYR A 43 -30.680 -24.518 21.579 1.00 53.51 C ANISOU 347 CE1 TYR A 43 7378 6476 6478 -1181 -90 473 C ATOM 348 CE2 TYR A 43 -29.782 -25.227 23.684 1.00 50.12 C ANISOU 348 CE2 TYR A 43 7067 5966 6010 -1161 -50 603 C ATOM 349 CZ TYR A 43 -30.567 -25.467 22.571 1.00 52.49 C ANISOU 349 CZ TYR A 43 7342 6258 6344 -1231 -79 545 C ATOM 350 OH TYR A 43 -31.242 -26.657 22.445 1.00 56.21 O ANISOU 350 OH TYR A 43 7888 6627 6843 -1357 -102 561 O ATOM 351 N PHE A 44 -26.228 -19.642 21.847 1.00 18.77 N ANISOU 351 N PHE A 44 2770 2356 2004 -611 -20 400 N ATOM 352 CA PHE A 44 -25.562 -18.345 21.808 1.00 22.76 C ANISOU 352 CA PHE A 44 3204 2940 2503 -524 -4 380 C ATOM 353 C PHE A 44 -25.568 -17.761 20.400 1.00 21.31 C ANISOU 353 C PHE A 44 2989 2784 2326 -494 -6 316 C ATOM 354 O PHE A 44 -25.588 -16.536 20.239 1.00 25.13 O ANISOU 354 O PHE A 44 3398 3352 2800 -460 9 300 O ATOM 355 CB PHE A 44 -24.135 -18.466 22.343 1.00 21.95 C ANISOU 355 CB PHE A 44 3138 2791 2412 -432 -14 398 C ATOM 356 CG PHE A 44 -24.063 -18.969 23.756 1.00 22.90 C ANISOU 356 CG PHE A 44 3303 2885 2513 -454 -23 467 C ATOM 357 CD1 PHE A 44 -24.371 -18.136 24.820 1.00 26.27 C ANISOU 357 CD1 PHE A 44 3682 3397 2901 -469 -4 499 C ATOM 358 CD2 PHE A 44 -23.694 -20.277 24.020 1.00 20.91 C ANISOU 358 CD2 PHE A 44 3151 2517 2275 -459 -53 499 C ATOM 359 CE1 PHE A 44 -24.314 -18.602 26.120 1.00 27.64 C ANISOU 359 CE1 PHE A 44 3914 3548 3039 -494 -12 564 C ATOM 360 CE2 PHE A 44 -23.631 -20.745 25.316 1.00 19.67 C ANISOU 360 CE2 PHE A 44 3051 2332 2090 -481 -67 570 C ATOM 361 CZ PHE A 44 -23.943 -19.910 26.366 1.00 19.41 C ANISOU 361 CZ PHE A 44 2976 2392 2008 -501 -45 604 C ATOM 362 N VAL A 45 -25.563 -18.617 19.375 1.00 23.78 N ANISOU 362 N VAL A 45 3369 3021 2648 -506 -26 279 N ATOM 363 CA VAL A 45 -25.698 -18.138 18.000 1.00 27.81 C ANISOU 363 CA VAL A 45 3868 3554 3146 -490 -32 220 C ATOM 364 C VAL A 45 -27.041 -17.446 17.808 1.00 27.35 C ANISOU 364 C VAL A 45 3733 3584 3075 -560 -46 216 C ATOM 365 O VAL A 45 -27.129 -16.400 17.153 1.00 29.74 O ANISOU 365 O VAL A 45 3986 3953 3363 -527 -45 191 O ATOM 366 CB VAL A 45 -25.513 -19.306 17.011 1.00 32.90 C ANISOU 366 CB VAL A 45 4616 4091 3791 -498 -53 176 C ATOM 367 CG1 VAL A 45 -25.932 -18.904 15.596 1.00 31.56 C ANISOU 367 CG1 VAL A 45 4453 3949 3591 -507 -68 117 C ATOM 368 CG2 VAL A 45 -24.074 -19.791 17.031 1.00 26.54 C ANISOU 368 CG2 VAL A 45 3869 3208 3008 -402 -31 168 C ATOM 369 N VAL A 46 -28.106 -18.014 18.381 1.00 29.92 N ANISOU 369 N VAL A 46 4046 3912 3412 -656 -58 245 N ATOM 370 CA VAL A 46 -29.426 -17.399 18.283 1.00 26.95 C ANISOU 370 CA VAL A 46 3576 3625 3040 -721 -70 243 C ATOM 371 C VAL A 46 -29.465 -16.085 19.054 1.00 23.14 C ANISOU 371 C VAL A 46 2997 3243 2551 -675 -33 264 C ATOM 372 O VAL A 46 -29.997 -15.080 18.566 1.00 19.99 O ANISOU 372 O VAL A 46 2525 2919 2152 -660 -43 242 O ATOM 373 CB VAL A 46 -30.507 -18.382 18.770 1.00 26.08 C ANISOU 373 CB VAL A 46 3466 3491 2953 -842 -80 271 C ATOM 374 CG1 VAL A 46 -31.836 -17.668 18.977 1.00 19.44 C ANISOU 374 CG1 VAL A 46 2497 2758 2130 -901 -76 277 C ATOM 375 CG2 VAL A 46 -30.664 -19.513 17.773 1.00 25.48 C ANISOU 375 CG2 VAL A 46 3480 3319 2883 -895 -132 235 C ATOM 376 N SER A 47 -28.901 -16.067 20.267 1.00 23.73 N ANISOU 376 N SER A 47 3080 3316 2619 -651 4 306 N ATOM 377 CA SER A 47 -28.802 -14.819 21.019 1.00 22.54 C ANISOU 377 CA SER A 47 2857 3250 2456 -602 37 317 C ATOM 378 C SER A 47 -28.021 -13.771 20.236 1.00 26.93 C ANISOU 378 C SER A 47 3398 3827 3008 -512 30 282 C ATOM 379 O SER A 47 -28.414 -12.599 20.186 1.00 28.22 O ANISOU 379 O SER A 47 3490 4064 3170 -488 37 270 O ATOM 380 CB SER A 47 -28.145 -15.075 22.376 1.00 24.10 C ANISOU 380 CB SER A 47 3092 3428 2635 -588 64 364 C ATOM 381 OG SER A 47 -27.962 -13.866 23.091 1.00 19.97 O ANISOU 381 OG SER A 47 2514 2979 2094 -538 91 367 O ATOM 382 N LEU A 48 -26.918 -14.185 19.607 1.00 26.96 N ANISOU 382 N LEU A 48 3469 3761 3012 -463 20 265 N ATOM 383 CA LEU A 48 -26.137 -13.278 18.773 1.00 21.30 C ANISOU 383 CA LEU A 48 2744 3058 2289 -389 24 234 C ATOM 384 C LEU A 48 -26.950 -12.777 17.585 1.00 23.20 C ANISOU 384 C LEU A 48 2964 3334 2518 -407 -1 201 C ATOM 385 O LEU A 48 -26.842 -11.606 17.199 1.00 25.34 O ANISOU 385 O LEU A 48 3197 3651 2780 -364 3 190 O ATOM 386 CB LEU A 48 -24.867 -13.985 18.298 1.00 17.49 C ANISOU 386 CB LEU A 48 2335 2496 1816 -339 30 219 C ATOM 387 CG LEU A 48 -23.897 -13.189 17.432 1.00 18.12 C ANISOU 387 CG LEU A 48 2411 2583 1893 -268 51 190 C ATOM 388 CD1 LEU A 48 -23.441 -11.937 18.159 1.00 14.43 C ANISOU 388 CD1 LEU A 48 1876 2173 1433 -227 67 209 C ATOM 389 CD2 LEU A 48 -22.706 -14.061 17.040 1.00 15.36 C ANISOU 389 CD2 LEU A 48 2122 2152 1560 -219 68 173 C ATOM 390 N ALA A 49 -27.774 -13.650 16.994 1.00 23.27 N ANISOU 390 N ALA A 49 3002 3315 2526 -472 -35 186 N ATOM 391 CA ALA A 49 -28.619 -13.235 15.878 1.00 16.24 C ANISOU 391 CA ALA A 49 2094 2457 1621 -493 -78 157 C ATOM 392 C ALA A 49 -29.756 -12.329 16.334 1.00 25.22 C ANISOU 392 C ALA A 49 3123 3684 2777 -514 -88 171 C ATOM 393 O ALA A 49 -30.180 -11.447 15.582 1.00 26.28 O ANISOU 393 O ALA A 49 3225 3860 2901 -492 -120 154 O ATOM 394 CB ALA A 49 -29.176 -14.458 15.150 1.00 17.08 C ANISOU 394 CB ALA A 49 2262 2504 1722 -564 -122 132 C ATOM 395 N ALA A 50 -30.268 -12.532 17.551 1.00 24.55 N ANISOU 395 N ALA A 50 2985 3627 2716 -554 -60 202 N ATOM 396 CA ALA A 50 -31.318 -11.654 18.058 1.00 24.88 C ANISOU 396 CA ALA A 50 2917 3757 2781 -564 -54 210 C ATOM 397 C ALA A 50 -30.804 -10.232 18.245 1.00 26.01 C ANISOU 397 C ALA A 50 3027 3941 2913 -476 -32 207 C ATOM 398 O ALA A 50 -31.535 -9.263 18.009 1.00 24.35 O ANISOU 398 O ALA A 50 2745 3789 2716 -454 -50 197 O ATOM 399 CB ALA A 50 -31.875 -12.200 19.370 1.00 16.92 C ANISOU 399 CB ALA A 50 1871 2768 1789 -625 -10 244 C ATOM 400 N ALA A 51 -29.548 -10.084 18.669 1.00 21.80 N ANISOU 400 N ALA A 51 2546 3376 2362 -425 0 216 N ATOM 401 CA ALA A 51 -28.982 -8.747 18.809 1.00 20.61 C ANISOU 401 CA ALA A 51 2373 3254 2205 -351 16 212 C ATOM 402 C ALA A 51 -28.783 -8.091 17.449 1.00 23.82 C ANISOU 402 C ALA A 51 2800 3652 2598 -314 -17 190 C ATOM 403 O ALA A 51 -28.945 -6.874 17.314 1.00 24.13 O ANISOU 403 O ALA A 51 2802 3725 2639 -271 -23 186 O ATOM 404 CB ALA A 51 -27.664 -8.807 19.581 1.00 15.41 C ANISOU 404 CB ALA A 51 1756 2561 1537 -315 48 227 C ATOM 405 N ASP A 52 -28.434 -8.882 16.429 1.00 29.54 N ANISOU 405 N ASP A 52 3595 4325 3305 -329 -38 175 N ATOM 406 CA ASP A 52 -28.328 -8.352 15.072 1.00 26.89 C ANISOU 406 CA ASP A 52 3296 3981 2939 -303 -68 156 C ATOM 407 C ASP A 52 -29.696 -7.974 14.510 1.00 26.90 C ANISOU 407 C ASP A 52 3250 4028 2944 -327 -130 148 C ATOM 408 O ASP A 52 -29.806 -6.990 13.768 1.00 20.09 O ANISOU 408 O ASP A 52 2390 3182 2063 -289 -159 146 O ATOM 409 CB ASP A 52 -27.623 -9.365 14.163 1.00 25.72 C ANISOU 409 CB ASP A 52 3245 3767 2761 -312 -67 136 C ATOM 410 CG ASP A 52 -26.124 -9.478 14.460 1.00 35.67 C ANISOU 410 CG ASP A 52 4541 4986 4025 -266 -8 139 C ATOM 411 OD1 ASP A 52 -25.548 -8.523 15.022 1.00 38.02 O ANISOU 411 OD1 ASP A 52 4801 5308 4338 -224 21 155 O ATOM 412 OD2 ASP A 52 -25.519 -10.521 14.122 1.00 44.27 O ANISOU 412 OD2 ASP A 52 5696 6017 5108 -269 7 124 O ATOM 413 N ILE A 53 -30.743 -8.730 14.858 1.00 20.63 N ANISOU 413 N ILE A 53 2409 3252 2177 -391 -155 148 N ATOM 414 CA ILE A 53 -32.101 -8.357 14.470 1.00 16.39 C ANISOU 414 CA ILE A 53 1797 2768 1664 -413 -217 142 C ATOM 415 C ILE A 53 -32.472 -7.009 15.080 1.00 25.38 C ANISOU 415 C ILE A 53 2848 3966 2830 -356 -202 152 C ATOM 416 O ILE A 53 -32.988 -6.118 14.394 1.00 25.68 O ANISOU 416 O ILE A 53 2859 4028 2869 -320 -254 147 O ATOM 417 CB ILE A 53 -33.096 -9.463 14.874 1.00 27.74 C ANISOU 417 CB ILE A 53 3186 4215 3138 -504 -234 142 C ATOM 418 CG1 ILE A 53 -32.844 -10.722 14.043 1.00 26.13 C ANISOU 418 CG1 ILE A 53 3083 3940 2905 -558 -269 123 C ATOM 419 CG2 ILE A 53 -34.538 -8.992 14.719 1.00 17.86 C ANISOU 419 CG2 ILE A 53 1819 3034 1933 -524 -290 137 C ATOM 420 CD1 ILE A 53 -33.673 -11.912 14.449 1.00 18.27 C ANISOU 420 CD1 ILE A 53 2059 2935 1948 -659 -283 126 C ATOM 421 N LEU A 54 -32.188 -6.831 16.376 1.00 15.81 N ANISOU 421 N LEU A 54 1599 2771 1636 -344 -133 166 N ATOM 422 CA LEU A 54 -32.511 -5.579 17.057 1.00 23.96 C ANISOU 422 CA LEU A 54 2559 3853 2692 -287 -110 168 C ATOM 423 C LEU A 54 -31.669 -4.410 16.558 1.00 23.57 C ANISOU 423 C LEU A 54 2558 3779 2618 -212 -116 167 C ATOM 424 O LEU A 54 -32.034 -3.253 16.794 1.00 26.66 O ANISOU 424 O LEU A 54 2901 4199 3029 -159 -119 163 O ATOM 425 CB LEU A 54 -32.343 -5.747 18.568 1.00 23.71 C ANISOU 425 CB LEU A 54 2500 3840 2668 -298 -35 179 C ATOM 426 CG LEU A 54 -33.389 -6.653 19.225 1.00 24.21 C ANISOU 426 CG LEU A 54 2497 3941 2760 -373 -15 187 C ATOM 427 CD1 LEU A 54 -33.084 -6.916 20.690 1.00 16.15 C ANISOU 427 CD1 LEU A 54 1482 2929 1724 -388 63 205 C ATOM 428 CD2 LEU A 54 -34.763 -6.035 19.071 1.00 23.32 C ANISOU 428 CD2 LEU A 54 2267 3897 2698 -366 -39 172 C ATOM 429 N VAL A 55 -30.553 -4.683 15.881 1.00 20.66 N ANISOU 429 N VAL A 55 2284 3356 2210 -208 -113 169 N ATOM 430 CA VAL A 55 -29.780 -3.615 15.259 1.00 19.04 C ANISOU 430 CA VAL A 55 2127 3125 1981 -152 -115 173 C ATOM 431 C VAL A 55 -30.562 -2.994 14.107 1.00 17.28 C ANISOU 431 C VAL A 55 1907 2912 1747 -133 -187 171 C ATOM 432 O VAL A 55 -30.616 -1.767 13.965 1.00 18.69 O ANISOU 432 O VAL A 55 2078 3093 1930 -80 -202 179 O ATOM 433 CB VAL A 55 -28.410 -4.151 14.802 1.00 20.00 C ANISOU 433 CB VAL A 55 2338 3192 2069 -156 -81 174 C ATOM 434 CG1 VAL A 55 -27.752 -3.190 13.822 1.00 14.10 C ANISOU 434 CG1 VAL A 55 1648 2419 1290 -117 -85 181 C ATOM 435 CG2 VAL A 55 -27.510 -4.372 16.006 1.00 15.37 C ANISOU 435 CG2 VAL A 55 1743 2596 1502 -152 -24 181 C ATOM 436 N GLY A 56 -31.187 -3.826 13.272 1.00 15.57 N ANISOU 436 N GLY A 56 1706 2695 1514 -177 -242 162 N ATOM 437 CA GLY A 56 -31.969 -3.299 12.170 1.00 23.92 C ANISOU 437 CA GLY A 56 2771 3762 2555 -161 -329 163 C ATOM 438 C GLY A 56 -33.310 -2.732 12.584 1.00 25.71 C ANISOU 438 C GLY A 56 2878 4046 2843 -142 -376 161 C ATOM 439 O GLY A 56 -33.799 -1.784 11.965 1.00 31.33 O ANISOU 439 O GLY A 56 3583 4766 3557 -94 -440 169 O ATOM 440 N VAL A 57 -33.920 -3.292 13.628 1.00 27.79 N ANISOU 440 N VAL A 57 3047 4351 3161 -177 -342 153 N ATOM 441 CA VAL A 57 -35.239 -2.839 14.051 1.00 28.44 C ANISOU 441 CA VAL A 57 2998 4496 3312 -161 -372 147 C ATOM 442 C VAL A 57 -35.137 -1.556 14.866 1.00 24.50 C ANISOU 442 C VAL A 57 2457 4012 2840 -81 -325 148 C ATOM 443 O VAL A 57 -35.951 -0.639 14.705 1.00 25.04 O ANISOU 443 O VAL A 57 2458 4107 2950 -23 -372 144 O ATOM 444 CB VAL A 57 -35.948 -3.960 14.836 1.00 39.51 C ANISOU 444 CB VAL A 57 4316 5937 4757 -240 -341 140 C ATOM 445 CG1 VAL A 57 -37.220 -3.444 15.496 1.00 38.71 C ANISOU 445 CG1 VAL A 57 4062 5911 4736 -220 -339 131 C ATOM 446 CG2 VAL A 57 -36.259 -5.136 13.918 1.00 36.21 C ANISOU 446 CG2 VAL A 57 3936 5500 4323 -321 -409 133 C ATOM 447 N LEU A 58 -34.137 -1.459 15.740 1.00 24.77 N ANISOU 447 N LEU A 58 2534 4024 2854 -73 -241 150 N ATOM 448 CA LEU A 58 -34.035 -0.351 16.682 1.00 22.20 C ANISOU 448 CA LEU A 58 2175 3709 2551 -8 -192 143 C ATOM 449 C LEU A 58 -32.762 0.466 16.522 1.00 23.31 C ANISOU 449 C LEU A 58 2415 3790 2653 34 -175 153 C ATOM 450 O LEU A 58 -32.838 1.690 16.372 1.00 25.25 O ANISOU 450 O LEU A 58 2663 4019 2910 100 -196 152 O ATOM 451 CB LEU A 58 -34.142 -0.885 18.119 1.00 22.97 C ANISOU 451 CB LEU A 58 2221 3843 2663 -40 -107 134 C ATOM 452 CG LEU A 58 -35.485 -1.522 18.488 1.00 26.15 C ANISOU 452 CG LEU A 58 2507 4314 3116 -83 -102 126 C ATOM 453 CD1 LEU A 58 -35.472 -1.985 19.938 1.00 22.77 C ANISOU 453 CD1 LEU A 58 2052 3916 2684 -117 -5 124 C ATOM 454 CD2 LEU A 58 -36.637 -0.553 18.242 1.00 27.30 C ANISOU 454 CD2 LEU A 58 2549 4502 3323 -18 -145 109 C ATOM 455 N ALA A 59 -31.588 -0.170 16.550 1.00 16.38 N ANISOU 455 N ALA A 59 1614 2876 1735 -4 -137 162 N ATOM 456 CA ALA A 59 -30.339 0.589 16.577 1.00 18.53 C ANISOU 456 CA ALA A 59 1958 3099 1984 27 -110 170 C ATOM 457 C ALA A 59 -30.172 1.455 15.330 1.00 20.55 C ANISOU 457 C ALA A 59 2273 3316 2219 60 -160 186 C ATOM 458 O ALA A 59 -29.763 2.617 15.429 1.00 23.72 O ANISOU 458 O ALA A 59 2700 3687 2627 105 -155 191 O ATOM 459 CB ALA A 59 -29.148 -0.355 16.738 1.00 15.07 C ANISOU 459 CB ALA A 59 1575 2632 1518 -17 -67 177 C ATOM 460 N ILE A 60 -30.481 0.914 14.154 1.00 18.60 N ANISOU 460 N ILE A 60 2060 3064 1942 37 -211 195 N ATOM 461 CA ILE A 60 -30.297 1.647 12.902 1.00 15.42 C ANISOU 461 CA ILE A 60 1736 2623 1501 62 -258 216 C ATOM 462 C ILE A 60 -31.321 2.775 12.788 1.00 16.22 C ANISOU 462 C ILE A 60 1793 2733 1635 124 -323 220 C ATOM 463 O ILE A 60 -30.945 3.894 12.414 1.00 16.91 O ANISOU 463 O ILE A 60 1937 2776 1711 166 -335 241 O ATOM 464 CB ILE A 60 -30.339 0.700 11.687 1.00 23.03 C ANISOU 464 CB ILE A 60 2764 3579 2409 18 -297 219 C ATOM 465 CG1 ILE A 60 -29.047 -0.128 11.632 1.00 21.67 C ANISOU 465 CG1 ILE A 60 2657 3377 2201 -21 -224 215 C ATOM 466 CG2 ILE A 60 -30.551 1.481 10.394 1.00 16.37 C ANISOU 466 CG2 ILE A 60 1996 2708 1517 46 -367 243 C ATOM 467 CD1 ILE A 60 -28.960 -1.099 10.476 1.00 15.54 C ANISOU 467 CD1 ILE A 60 1959 2583 1362 -60 -246 208 C ATOM 468 N PRO A 61 -32.607 2.563 13.095 1.00 20.06 N ANISOU 468 N PRO A 61 2178 3273 2169 134 -365 204 N ATOM 469 CA PRO A 61 -33.504 3.728 13.198 1.00 22.10 C ANISOU 469 CA PRO A 61 2380 3538 2478 211 -415 203 C ATOM 470 C PRO A 61 -33.079 4.730 14.270 1.00 24.62 C ANISOU 470 C PRO A 61 2689 3838 2829 261 -352 190 C ATOM 471 O PRO A 61 -33.255 5.940 14.074 1.00 20.78 O ANISOU 471 O PRO A 61 2221 3315 2360 330 -387 198 O ATOM 472 CB PRO A 61 -34.867 3.094 13.504 1.00 17.92 C ANISOU 472 CB PRO A 61 1721 3082 2006 200 -448 181 C ATOM 473 CG PRO A 61 -34.778 1.729 12.916 1.00 17.81 C ANISOU 473 CG PRO A 61 1736 3078 1952 114 -464 183 C ATOM 474 CD PRO A 61 -33.362 1.296 13.153 1.00 21.06 C ANISOU 474 CD PRO A 61 2242 3450 2312 76 -382 188 C ATOM 475 N PHE A 62 -32.509 4.270 15.390 1.00 22.20 N ANISOU 475 N PHE A 62 2363 3547 2525 229 -267 171 N ATOM 476 CA PHE A 62 -31.976 5.201 16.384 1.00 21.66 C ANISOU 476 CA PHE A 62 2305 3452 2473 268 -214 156 C ATOM 477 C PHE A 62 -30.800 5.996 15.825 1.00 21.30 C ANISOU 477 C PHE A 62 2369 3330 2395 274 -216 181 C ATOM 478 O PHE A 62 -30.706 7.209 16.045 1.00 25.15 O ANISOU 478 O PHE A 62 2881 3774 2902 327 -222 177 O ATOM 479 CB PHE A 62 -31.548 4.459 17.657 1.00 19.39 C ANISOU 479 CB PHE A 62 1990 3196 2181 226 -134 135 C ATOM 480 CG PHE A 62 -32.696 3.950 18.496 1.00 22.66 C ANISOU 480 CG PHE A 62 2297 3683 2631 224 -108 109 C ATOM 481 CD1 PHE A 62 -34.008 4.246 18.164 1.00 25.67 C ANISOU 481 CD1 PHE A 62 2593 4101 3061 266 -153 100 C ATOM 482 CD2 PHE A 62 -32.455 3.183 19.628 1.00 18.43 C ANISOU 482 CD2 PHE A 62 1743 3179 2081 180 -39 97 C ATOM 483 CE1 PHE A 62 -35.060 3.774 18.938 1.00 26.21 C ANISOU 483 CE1 PHE A 62 2548 4242 3169 257 -117 77 C ATOM 484 CE2 PHE A 62 -33.500 2.710 20.406 1.00 20.80 C ANISOU 484 CE2 PHE A 62 1949 3546 2408 168 -1 79 C ATOM 485 CZ PHE A 62 -34.805 3.005 20.062 1.00 24.24 C ANISOU 485 CZ PHE A 62 2289 4024 2898 205 -34 67 C ATOM 486 N ALA A 63 -29.892 5.330 15.102 1.00 19.84 N ANISOU 486 N ALA A 63 2252 3124 2162 218 -205 205 N ATOM 487 CA ALA A 63 -28.733 6.024 14.545 1.00 20.13 C ANISOU 487 CA ALA A 63 2384 3094 2170 211 -191 231 C ATOM 488 C ALA A 63 -29.147 7.065 13.509 1.00 18.77 C ANISOU 488 C ALA A 63 2268 2877 1987 256 -258 261 C ATOM 489 O ALA A 63 -28.561 8.152 13.449 1.00 20.75 O ANISOU 489 O ALA A 63 2577 3065 2240 275 -252 277 O ATOM 490 CB ALA A 63 -27.758 5.016 13.937 1.00 22.13 C ANISOU 490 CB ALA A 63 2688 3343 2378 148 -156 246 C ATOM 491 N ILE A 64 -30.152 6.752 12.684 1.00 22.50 N ANISOU 491 N ILE A 64 2727 3375 2446 270 -328 270 N ATOM 492 CA ILE A 64 -30.675 7.739 11.740 1.00 23.44 C ANISOU 492 CA ILE A 64 2901 3452 2555 321 -409 302 C ATOM 493 C ILE A 64 -31.252 8.930 12.490 1.00 27.92 C ANISOU 493 C ILE A 64 3423 3996 3188 401 -428 286 C ATOM 494 O ILE A 64 -31.091 10.085 12.077 1.00 32.98 O ANISOU 494 O ILE A 64 4137 4566 3827 443 -461 314 O ATOM 495 CB ILE A 64 -31.729 7.098 10.819 1.00 18.95 C ANISOU 495 CB ILE A 64 2312 2922 1965 321 -498 310 C ATOM 496 CG1 ILE A 64 -31.102 6.000 9.960 1.00 17.69 C ANISOU 496 CG1 ILE A 64 2224 2769 1727 246 -480 321 C ATOM 497 CG2 ILE A 64 -32.411 8.164 9.956 1.00 19.02 C ANISOU 497 CG2 ILE A 64 2367 2889 1970 389 -601 344 C ATOM 498 CD1 ILE A 64 -32.113 5.201 9.158 1.00 18.31 C ANISOU 498 CD1 ILE A 64 2285 2888 1783 231 -570 317 C ATOM 499 N THR A 65 -31.925 8.666 13.611 1.00 26.54 N ANISOU 499 N THR A 65 3135 3878 3072 424 -402 241 N ATOM 500 CA THR A 65 -32.564 9.729 14.379 1.00 23.31 C ANISOU 500 CA THR A 65 2676 3453 2726 508 -410 214 C ATOM 501 C THR A 65 -31.531 10.646 15.028 1.00 23.37 C ANISOU 501 C THR A 65 2754 3391 2734 513 -357 206 C ATOM 502 O THR A 65 -31.635 11.874 14.938 1.00 20.12 O ANISOU 502 O THR A 65 2388 2911 2347 576 -391 212 O ATOM 503 CB THR A 65 -33.481 9.115 15.437 1.00 24.39 C ANISOU 503 CB THR A 65 2678 3676 2914 520 -374 165 C ATOM 504 OG1 THR A 65 -34.460 8.288 14.794 1.00 25.38 O ANISOU 504 OG1 THR A 65 2732 3863 3049 506 -432 172 O ATOM 505 CG2 THR A 65 -34.184 10.201 16.230 1.00 24.17 C ANISOU 505 CG2 THR A 65 2597 3636 2950 617 -370 127 C ATOM 506 N ILE A 66 -30.520 10.068 15.686 1.00 23.94 N ANISOU 506 N ILE A 66 2838 3476 2784 446 -282 194 N ATOM 507 CA ILE A 66 -29.552 10.877 16.417 1.00 25.33 C ANISOU 507 CA ILE A 66 3065 3591 2966 442 -239 180 C ATOM 508 C ILE A 66 -28.549 11.564 15.505 1.00 30.48 C ANISOU 508 C ILE A 66 3831 4159 3592 413 -252 228 C ATOM 509 O ILE A 66 -27.812 12.447 15.963 1.00 31.16 O ANISOU 509 O ILE A 66 3966 4180 3694 410 -233 222 O ATOM 510 CB ILE A 66 -28.805 10.025 17.462 1.00 23.71 C ANISOU 510 CB ILE A 66 2831 3430 2749 382 -168 153 C ATOM 511 CG1 ILE A 66 -28.360 10.899 18.632 1.00 17.31 C ANISOU 511 CG1 ILE A 66 2038 2580 1960 402 -138 113 C ATOM 512 CG2 ILE A 66 -27.596 9.343 16.840 1.00 15.54 C ANISOU 512 CG2 ILE A 66 1845 2383 1675 303 -144 188 C ATOM 513 CD1 ILE A 66 -27.699 10.124 19.741 1.00 15.65 C ANISOU 513 CD1 ILE A 66 1803 2411 1732 351 -84 87 C ATOM 514 N SER A 67 -28.497 11.187 14.226 1.00 35.05 N ANISOU 514 N SER A 67 4455 4735 4126 386 -283 276 N ATOM 515 CA SER A 67 -27.654 11.909 13.280 1.00 37.30 C ANISOU 515 CA SER A 67 4854 4939 4378 359 -288 328 C ATOM 516 C SER A 67 -28.224 13.278 12.930 1.00 35.75 C ANISOU 516 C SER A 67 4716 4664 4204 431 -355 349 C ATOM 517 O SER A 67 -27.464 14.171 12.543 1.00 34.99 O ANISOU 517 O SER A 67 4716 4481 4098 410 -350 386 O ATOM 518 CB SER A 67 -27.463 11.087 12.006 1.00 31.46 C ANISOU 518 CB SER A 67 4162 4222 3571 311 -295 369 C ATOM 519 OG SER A 67 -28.690 10.944 11.313 1.00 31.21 O ANISOU 519 OG SER A 67 4118 4214 3525 359 -378 379 O ATOM 520 N THR A 68 -29.540 13.464 13.059 1.00 37.11 N ANISOU 520 N THR A 68 4829 4861 4412 514 -418 329 N ATOM 521 CA THR A 68 -30.169 14.746 12.761 1.00 38.82 C ANISOU 521 CA THR A 68 5093 4997 4659 600 -491 346 C ATOM 522 C THR A 68 -29.975 15.777 13.866 1.00 41.90 C ANISOU 522 C THR A 68 5487 5326 5108 643 -464 303 C ATOM 523 O THR A 68 -30.228 16.965 13.630 1.00 40.45 O ANISOU 523 O THR A 68 5371 5049 4950 707 -516 320 O ATOM 524 CB THR A 68 -31.673 14.566 12.514 1.00 40.87 C ANISOU 524 CB THR A 68 5268 5309 4951 684 -573 335 C ATOM 525 OG1 THR A 68 -32.324 14.214 13.743 1.00 46.47 O ANISOU 525 OG1 THR A 68 5846 6090 5720 719 -532 265 O ATOM 526 CG2 THR A 68 -31.936 13.478 11.477 1.00 34.17 C ANISOU 526 CG2 THR A 68 4415 4523 4044 637 -611 367 C ATOM 527 N GLY A 69 -29.542 15.357 15.053 1.00 38.54 N ANISOU 527 N GLY A 69 5002 4944 4698 610 -390 249 N ATOM 528 CA GLY A 69 -29.383 16.279 16.160 1.00 35.14 C ANISOU 528 CA GLY A 69 4582 4458 4311 648 -366 198 C ATOM 529 C GLY A 69 -30.671 16.888 16.665 1.00 36.39 C ANISOU 529 C GLY A 69 4684 4616 4527 769 -400 151 C ATOM 530 O GLY A 69 -30.671 18.042 17.098 1.00 40.41 O ANISOU 530 O GLY A 69 5247 5036 5073 826 -412 125 O ATOM 531 N PHE A 70 -31.773 16.141 16.621 1.00 30.89 N ANISOU 531 N PHE A 70 3877 4014 3846 809 -414 136 N ATOM 532 CA PHE A 70 -33.077 16.664 17.004 1.00 30.57 C ANISOU 532 CA PHE A 70 3759 3984 3871 930 -444 93 C ATOM 533 C PHE A 70 -33.117 17.027 18.491 1.00 29.90 C ANISOU 533 C PHE A 70 3642 3904 3815 966 -369 11 C ATOM 534 O PHE A 70 -32.341 16.524 19.307 1.00 28.11 O ANISOU 534 O PHE A 70 3421 3709 3552 892 -298 -15 O ATOM 535 CB PHE A 70 -34.169 15.639 16.704 1.00 34.12 C ANISOU 535 CB PHE A 70 4079 4549 4337 942 -465 94 C ATOM 536 CG PHE A 70 -34.176 14.481 17.657 1.00 39.73 C ANISOU 536 CG PHE A 70 4694 5369 5033 881 -376 51 C ATOM 537 CD1 PHE A 70 -33.111 13.599 17.697 1.00 37.72 C ANISOU 537 CD1 PHE A 70 4479 5137 4716 768 -329 71 C ATOM 538 CD2 PHE A 70 -35.241 14.278 18.518 1.00 46.74 C ANISOU 538 CD2 PHE A 70 5454 6333 5973 939 -337 -6 C ATOM 539 CE1 PHE A 70 -33.103 12.539 18.578 1.00 38.74 C ANISOU 539 CE1 PHE A 70 4535 5355 4830 714 -256 40 C ATOM 540 CE2 PHE A 70 -35.241 13.214 19.404 1.00 44.26 C ANISOU 540 CE2 PHE A 70 5067 6114 5638 876 -253 -37 C ATOM 541 CZ PHE A 70 -34.169 12.343 19.433 1.00 41.33 C ANISOU 541 CZ PHE A 70 4748 5755 5199 764 -218 -11 C ATOM 542 N CYS A 71 -34.057 17.903 18.834 1.00 29.14 N ANISOU 542 N CYS A 71 3513 3776 3782 1089 -390 -33 N ATOM 543 CA CYS A 71 -34.260 18.305 20.219 1.00 30.40 C ANISOU 543 CA CYS A 71 3647 3940 3965 1141 -316 -120 C ATOM 544 C CYS A 71 -34.909 17.180 21.017 1.00 32.62 C ANISOU 544 C CYS A 71 3790 4364 4241 1123 -239 -163 C ATOM 545 O CYS A 71 -35.836 16.520 20.541 1.00 38.49 O ANISOU 545 O CYS A 71 4420 5189 5014 1141 -260 -145 O ATOM 546 CB CYS A 71 -35.136 19.557 20.269 1.00 34.28 C ANISOU 546 CB CYS A 71 4141 4353 4530 1289 -357 -157 C ATOM 547 SG CYS A 71 -34.430 21.025 19.464 1.00 38.01 S ANISOU 547 SG CYS A 71 4796 4633 5012 1315 -447 -108 S ATOM 548 N ALA A 72 -34.427 16.966 22.241 1.00 31.01 N ANISOU 548 N ALA A 72 3599 4187 3999 1084 -152 -217 N ATOM 549 CA ALA A 72 -34.981 15.922 23.101 1.00 33.09 C ANISOU 549 CA ALA A 72 3749 4577 4246 1060 -67 -253 C ATOM 550 C ALA A 72 -34.495 16.114 24.532 1.00 38.00 C ANISOU 550 C ALA A 72 4422 5197 4821 1048 17 -323 C ATOM 551 O ALA A 72 -33.433 16.694 24.776 1.00 38.17 O ANISOU 551 O ALA A 72 4563 5131 4809 1014 3 -329 O ATOM 552 CB ALA A 72 -34.599 14.523 22.608 1.00 33.03 C ANISOU 552 CB ALA A 72 3708 4647 4195 942 -68 -194 C ATOM 553 N ALA A 73 -35.292 15.611 25.475 1.00 33.34 N ANISOU 553 N ALA A 73 3738 4703 4227 1070 105 -374 N ATOM 554 CA ALA A 73 -34.851 15.532 26.860 1.00 31.48 C ANISOU 554 CA ALA A 73 3554 4485 3922 1042 190 -434 C ATOM 555 C ALA A 73 -33.613 14.650 26.953 1.00 26.11 C ANISOU 555 C ALA A 73 2938 3817 3167 909 183 -388 C ATOM 556 O ALA A 73 -33.524 13.608 26.299 1.00 25.71 O ANISOU 556 O ALA A 73 2837 3820 3111 836 165 -325 O ATOM 557 CB ALA A 73 -35.964 14.979 27.748 1.00 30.10 C ANISOU 557 CB ALA A 73 3263 4426 3747 1075 296 -483 C ATOM 558 N CYS A 74 -32.656 15.071 27.781 1.00 25.05 N ANISOU 558 N CYS A 74 2913 3628 2976 879 193 -423 N ATOM 559 CA CYS A 74 -31.322 14.481 27.731 1.00 30.59 C ANISOU 559 CA CYS A 74 3682 4315 3626 765 162 -378 C ATOM 560 C CYS A 74 -31.350 12.983 28.024 1.00 31.19 C ANISOU 560 C CYS A 74 3695 4499 3656 686 206 -345 C ATOM 561 O CYS A 74 -30.693 12.198 27.330 1.00 30.87 O ANISOU 561 O CYS A 74 3651 4467 3611 609 170 -280 O ATOM 562 CB CYS A 74 -30.394 15.212 28.702 1.00 34.96 C ANISOU 562 CB CYS A 74 4353 4798 4132 751 158 -431 C ATOM 563 SG CYS A 74 -28.640 14.822 28.486 1.00 36.61 S ANISOU 563 SG CYS A 74 4637 4964 4310 625 96 -377 S ATOM 564 N HIS A 75 -32.111 12.560 29.035 1.00 32.33 N ANISOU 564 N HIS A 75 3794 4723 3765 704 291 -387 N ATOM 565 CA HIS A 75 -32.109 11.140 29.378 1.00 30.55 C ANISOU 565 CA HIS A 75 3527 4589 3493 621 334 -351 C ATOM 566 C HIS A 75 -32.791 10.297 28.310 1.00 25.31 C ANISOU 566 C HIS A 75 2755 3979 2883 601 318 -293 C ATOM 567 O HIS A 75 -32.378 9.157 28.068 1.00 23.50 O ANISOU 567 O HIS A 75 2517 3783 2630 517 309 -240 O ATOM 568 CB HIS A 75 -32.757 10.923 30.742 1.00 37.83 C ANISOU 568 CB HIS A 75 4439 5580 4354 637 437 -405 C ATOM 569 CG HIS A 75 -31.917 11.409 31.881 1.00 49.12 C ANISOU 569 CG HIS A 75 5994 6968 5700 627 445 -455 C ATOM 570 ND1 HIS A 75 -31.895 12.729 32.277 1.00 50.93 N ANISOU 570 ND1 HIS A 75 6291 7126 5932 704 440 -527 N ATOM 571 CD2 HIS A 75 -31.046 10.759 32.689 1.00 47.17 C ANISOU 571 CD2 HIS A 75 5823 6734 5365 550 444 -442 C ATOM 572 CE1 HIS A 75 -31.059 12.869 33.289 1.00 49.81 C ANISOU 572 CE1 HIS A 75 6262 6958 5703 668 437 -561 C ATOM 573 NE2 HIS A 75 -30.531 11.688 33.559 1.00 49.81 N ANISOU 573 NE2 HIS A 75 6268 7012 5648 577 436 -508 N ATOM 574 N GLY A 76 -33.828 10.828 27.662 1.00 25.87 N ANISOU 574 N GLY A 76 2746 4054 3028 679 307 -303 N ATOM 575 CA GLY A 76 -34.376 10.150 26.501 1.00 26.52 C ANISOU 575 CA GLY A 76 2741 4172 3163 657 263 -249 C ATOM 576 C GLY A 76 -33.391 10.111 25.348 1.00 29.90 C ANISOU 576 C GLY A 76 3236 4533 3593 612 174 -190 C ATOM 577 O GLY A 76 -33.271 9.098 24.655 1.00 29.72 O ANISOU 577 O GLY A 76 3186 4541 3565 545 149 -139 O ATOM 578 N CYS A 77 -32.668 11.215 25.131 1.00 24.98 N ANISOU 578 N CYS A 77 2703 3814 2973 646 129 -198 N ATOM 579 CA CYS A 77 -31.590 11.232 24.147 1.00 24.84 C ANISOU 579 CA CYS A 77 2758 3732 2949 594 62 -144 C ATOM 580 C CYS A 77 -30.508 10.221 24.488 1.00 25.90 C ANISOU 580 C CYS A 77 2927 3886 3028 495 81 -118 C ATOM 581 O CYS A 77 -29.881 9.646 23.590 1.00 25.06 O ANISOU 581 O CYS A 77 2836 3768 2917 439 47 -67 O ATOM 582 CB CYS A 77 -30.983 12.634 24.063 1.00 31.32 C ANISOU 582 CB CYS A 77 3673 4444 3785 636 24 -161 C ATOM 583 SG CYS A 77 -29.528 12.749 22.998 1.00 40.47 S ANISOU 583 SG CYS A 77 4923 5522 4933 561 -35 -95 S ATOM 584 N ALEU A 78 -30.289 9.975 25.778 0.08 22.42 N ANISOU 584 N ALEU A 78 2502 3474 2542 476 134 -155 N ATOM 585 N BLEU A 78 -30.258 10.005 25.780 0.92 23.28 N ANISOU 585 N BLEU A 78 2613 3580 2650 477 133 -155 N ATOM 586 CA ALEU A 78 -29.233 9.061 26.189 0.08 22.52 C ANISOU 586 CA ALEU A 78 2552 3499 2506 392 139 -130 C ATOM 587 CA BLEU A 78 -29.232 9.051 26.188 0.92 24.00 C ANISOU 587 CA BLEU A 78 2739 3687 2693 392 140 -130 C ATOM 588 C ALEU A 78 -29.591 7.612 25.887 0.08 19.97 C ANISOU 588 C ALEU A 78 2167 3247 2173 339 158 -89 C ATOM 589 C BLEU A 78 -29.595 7.635 25.773 0.92 18.64 C ANISOU 589 C BLEU A 78 1998 3076 2009 340 154 -87 C ATOM 590 O ALEU A 78 -28.694 6.782 25.702 0.08 20.53 O ANISOU 590 O ALEU A 78 2264 3313 2224 274 143 -52 O ATOM 591 O BLEU A 78 -28.716 6.851 25.397 0.92 15.46 O ANISOU 591 O BLEU A 78 1619 2664 1592 278 133 -46 O ATOM 592 CB ALEU A 78 -28.947 9.248 27.675 0.08 22.53 C ANISOU 592 CB ALEU A 78 2602 3509 2452 391 179 -179 C ATOM 593 CB BLEU A 78 -29.017 9.120 27.698 0.92 24.05 C ANISOU 593 CB BLEU A 78 2787 3710 2641 388 184 -177 C ATOM 594 CG ALEU A 78 -27.586 8.787 28.179 0.08 22.13 C ANISOU 594 CG ALEU A 78 2615 3438 2357 322 155 -163 C ATOM 595 CG BLEU A 78 -28.132 10.245 28.218 0.92 22.60 C ANISOU 595 CG BLEU A 78 2694 3447 2445 402 153 -216 C ATOM 596 CD1ALEU A 78 -26.484 9.295 27.266 0.08 21.85 C ANISOU 596 CD1ALEU A 78 2616 3326 2361 299 92 -134 C ATOM 597 CD1BLEU A 78 -28.032 10.169 29.729 0.92 17.72 C ANISOU 597 CD1BLEU A 78 2124 2856 1754 396 193 -264 C ATOM 598 CD2ALEU A 78 -27.405 9.317 29.577 0.08 24.42 C ANISOU 598 CD2ALEU A 78 2970 3721 2590 336 175 -221 C ATOM 599 CD2BLEU A 78 -26.755 10.159 27.572 0.92 21.54 C ANISOU 599 CD2BLEU A 78 2600 3258 2325 341 93 -171 C ATOM 600 N PHE A 79 -30.885 7.290 25.829 1.00 16.65 N ANISOU 600 N PHE A 79 1663 2889 1776 363 189 -96 N ATOM 601 CA PHE A 79 -31.291 5.923 25.528 1.00 16.40 C ANISOU 601 CA PHE A 79 1574 2916 1740 303 202 -59 C ATOM 602 C PHE A 79 -31.122 5.603 24.048 1.00 19.29 C ANISOU 602 C PHE A 79 1935 3257 2137 283 138 -15 C ATOM 603 O PHE A 79 -30.601 4.539 23.694 1.00 24.98 O ANISOU 603 O PHE A 79 2671 3982 2839 218 129 21 O ATOM 604 CB PHE A 79 -32.734 5.668 25.959 1.00 17.23 C ANISOU 604 CB PHE A 79 1580 3099 1868 325 258 -82 C ATOM 605 CG PHE A 79 -33.189 4.261 25.685 1.00 23.69 C ANISOU 605 CG PHE A 79 2341 3972 2687 251 270 -44 C ATOM 606 CD1 PHE A 79 -32.897 3.240 26.575 1.00 21.32 C ANISOU 606 CD1 PHE A 79 2067 3702 2333 182 320 -29 C ATOM 607 CD2 PHE A 79 -33.871 3.950 24.521 1.00 20.61 C ANISOU 607 CD2 PHE A 79 1885 3597 2350 246 221 -21 C ATOM 608 CE1 PHE A 79 -33.294 1.940 26.318 1.00 20.49 C ANISOU 608 CE1 PHE A 79 1920 3633 2232 109 328 7 C ATOM 609 CE2 PHE A 79 -34.268 2.650 24.259 1.00 19.79 C ANISOU 609 CE2 PHE A 79 1737 3533 2249 170 225 9 C ATOM 610 CZ PHE A 79 -33.980 1.646 25.157 1.00 19.68 C ANISOU 610 CZ PHE A 79 1748 3542 2186 101 281 24 C ATOM 611 N ILE A 80 -31.567 6.501 23.162 1.00 17.54 N ANISOU 611 N ILE A 80 1700 3006 1959 341 92 -16 N ATOM 612 CA ILE A 80 -31.373 6.242 21.740 1.00 28.23 C ANISOU 612 CA ILE A 80 3069 4333 3323 320 29 27 C ATOM 613 C ILE A 80 -29.898 6.293 21.367 1.00 23.57 C ANISOU 613 C ILE A 80 2571 3680 2704 281 14 52 C ATOM 614 O ILE A 80 -29.503 5.736 20.336 1.00 22.86 O ANISOU 614 O ILE A 80 2505 3577 2603 244 -14 88 O ATOM 615 CB ILE A 80 -32.166 7.222 20.854 1.00 31.62 C ANISOU 615 CB ILE A 80 3478 4739 3798 393 -28 27 C ATOM 616 CG1 ILE A 80 -31.510 8.596 20.866 1.00 38.67 C ANISOU 616 CG1 ILE A 80 4449 5549 4695 443 -46 17 C ATOM 617 CG2 ILE A 80 -33.623 7.309 21.287 1.00 31.24 C ANISOU 617 CG2 ILE A 80 3318 4754 3796 445 -11 -5 C ATOM 618 CD1 ILE A 80 -32.031 9.504 19.799 1.00 45.63 C ANISOU 618 CD1 ILE A 80 5342 6385 5611 506 -117 35 C ATOM 619 N ALA A 81 -29.067 6.944 22.186 1.00 25.10 N ANISOU 619 N ALA A 81 2816 3836 2884 288 33 32 N ATOM 620 CA ALA A 81 -27.634 6.989 21.919 1.00 22.69 C ANISOU 620 CA ALA A 81 2578 3478 2565 246 22 54 C ATOM 621 C ALA A 81 -26.939 5.704 22.345 1.00 22.42 C ANISOU 621 C ALA A 81 2543 3474 2503 183 46 69 C ATOM 622 O ALA A 81 -26.001 5.255 21.678 1.00 25.20 O ANISOU 622 O ALA A 81 2922 3801 2852 144 37 98 O ATOM 623 CB ALA A 81 -27.003 8.183 22.634 1.00 14.84 C ANISOU 623 CB ALA A 81 1635 2428 1575 269 20 25 C ATOM 624 N CYS A 82 -27.390 5.097 23.440 1.00 17.80 N ANISOU 624 N CYS A 82 1928 2939 1896 174 81 50 N ATOM 625 CA CYS A 82 -26.657 4.022 24.087 1.00 22.59 C ANISOU 625 CA CYS A 82 2549 3560 2472 122 97 64 C ATOM 626 C CYS A 82 -27.249 2.643 23.847 1.00 25.44 C ANISOU 626 C CYS A 82 2875 3966 2825 83 112 88 C ATOM 627 O CYS A 82 -26.603 1.650 24.197 1.00 24.65 O ANISOU 627 O CYS A 82 2796 3866 2706 42 118 107 O ATOM 628 CB CYS A 82 -26.577 4.269 25.600 1.00 19.92 C ANISOU 628 CB CYS A 82 2233 3238 2099 128 122 32 C ATOM 629 SG CYS A 82 -25.588 5.698 26.044 1.00 17.88 S ANISOU 629 SG CYS A 82 2034 2915 1845 153 93 0 S ATOM 630 N PHE A 83 -28.452 2.545 23.276 1.00 21.50 N ANISOU 630 N PHE A 83 2323 3501 2347 95 112 87 N ATOM 631 CA PHE A 83 -29.044 1.220 23.126 1.00 21.05 C ANISOU 631 CA PHE A 83 2232 3481 2285 46 123 107 C ATOM 632 C PHE A 83 -28.194 0.330 22.229 1.00 23.41 C ANISOU 632 C PHE A 83 2571 3744 2579 6 97 136 C ATOM 633 O PHE A 83 -28.127 -0.887 22.442 1.00 25.07 O ANISOU 633 O PHE A 83 2787 3962 2776 -41 109 153 O ATOM 634 CB PHE A 83 -30.468 1.314 22.588 1.00 15.34 C ANISOU 634 CB PHE A 83 1434 2800 1596 61 114 99 C ATOM 635 CG PHE A 83 -31.130 -0.021 22.441 1.00 21.93 C ANISOU 635 CG PHE A 83 2230 3671 2433 -1 121 116 C ATOM 636 CD1 PHE A 83 -31.522 -0.739 23.561 1.00 25.26 C ANISOU 636 CD1 PHE A 83 2628 4132 2836 -41 177 118 C ATOM 637 CD2 PHE A 83 -31.333 -0.573 21.189 1.00 25.90 C ANISOU 637 CD2 PHE A 83 2730 4161 2949 -27 72 133 C ATOM 638 CE1 PHE A 83 -32.120 -1.980 23.432 1.00 25.93 C ANISOU 638 CE1 PHE A 83 2683 4241 2929 -110 184 138 C ATOM 639 CE2 PHE A 83 -31.929 -1.811 21.052 1.00 28.84 C ANISOU 639 CE2 PHE A 83 3073 4556 3327 -92 72 145 C ATOM 640 CZ PHE A 83 -32.322 -2.519 22.176 1.00 24.97 C ANISOU 640 CZ PHE A 83 2555 4102 2829 -136 128 150 C ATOM 641 N VAL A 84 -27.514 0.920 21.245 1.00 14.88 N ANISOU 641 N VAL A 84 1526 2620 1508 26 68 143 N ATOM 642 CA VAL A 84 -26.630 0.137 20.392 1.00 14.83 C ANISOU 642 CA VAL A 84 1560 2581 1495 -5 59 164 C ATOM 643 C VAL A 84 -25.438 -0.395 21.187 1.00 18.79 C ANISOU 643 C VAL A 84 2090 3062 1989 -23 77 171 C ATOM 644 O VAL A 84 -24.876 -1.445 20.847 1.00 19.64 O ANISOU 644 O VAL A 84 2217 3151 2093 -49 80 186 O ATOM 645 CB VAL A 84 -26.204 0.984 19.180 1.00 15.33 C ANISOU 645 CB VAL A 84 1657 2605 1562 18 36 171 C ATOM 646 CG1 VAL A 84 -25.379 2.196 19.627 1.00 12.92 C ANISOU 646 CG1 VAL A 84 1372 2267 1269 45 42 165 C ATOM 647 CG2 VAL A 84 -25.461 0.128 18.150 1.00 12.82 C ANISOU 647 CG2 VAL A 84 1382 2260 1230 -10 39 187 C ATOM 648 N LEU A 85 -25.046 0.291 22.266 1.00 20.95 N ANISOU 648 N LEU A 85 2366 3336 2260 -6 84 158 N ATOM 649 CA LEU A 85 -23.991 -0.241 23.123 1.00 18.69 C ANISOU 649 CA LEU A 85 2102 3035 1965 -22 86 166 C ATOM 650 C LEU A 85 -24.456 -1.484 23.874 1.00 22.40 C ANISOU 650 C LEU A 85 2572 3530 2409 -54 99 180 C ATOM 651 O LEU A 85 -23.639 -2.355 24.192 1.00 28.28 O ANISOU 651 O LEU A 85 3341 4253 3150 -70 91 199 O ATOM 652 CB LEU A 85 -23.512 0.830 24.105 1.00 13.85 C ANISOU 652 CB LEU A 85 1501 2415 1348 -2 77 145 C ATOM 653 CG LEU A 85 -23.082 2.179 23.520 1.00 16.69 C ANISOU 653 CG LEU A 85 1868 2739 1735 22 63 133 C ATOM 654 CD1 LEU A 85 -22.727 3.160 24.630 1.00 13.08 C ANISOU 654 CD1 LEU A 85 1431 2269 1269 36 50 104 C ATOM 655 CD2 LEU A 85 -21.922 2.021 22.548 1.00 12.59 C ANISOU 655 CD2 LEU A 85 1356 2182 1247 7 58 154 C ATOM 656 N VAL A 86 -25.756 -1.587 24.160 1.00 19.70 N ANISOU 656 N VAL A 86 2201 3231 2052 -63 121 173 N ATOM 657 CA VAL A 86 -26.287 -2.796 24.784 1.00 13.41 C ANISOU 657 CA VAL A 86 1406 2456 1233 -106 141 193 C ATOM 658 C VAL A 86 -26.190 -3.974 23.824 1.00 18.31 C ANISOU 658 C VAL A 86 2038 3049 1870 -139 127 214 C ATOM 659 O VAL A 86 -25.748 -5.068 24.196 1.00 19.89 O ANISOU 659 O VAL A 86 2273 3224 2058 -167 125 237 O ATOM 660 CB VAL A 86 -27.739 -2.575 25.248 1.00 13.92 C ANISOU 660 CB VAL A 86 1421 2578 1289 -113 179 179 C ATOM 661 CG1 VAL A 86 -28.297 -3.856 25.856 1.00 14.34 C ANISOU 661 CG1 VAL A 86 1477 2651 1319 -174 208 206 C ATOM 662 CG2 VAL A 86 -27.821 -1.420 26.233 1.00 14.16 C ANISOU 662 CG2 VAL A 86 1452 2631 1298 -73 201 149 C ATOM 663 N LEU A 87 -26.608 -3.769 22.574 1.00 18.63 N ANISOU 663 N LEU A 87 2058 3087 1933 -133 111 205 N ATOM 664 CA LEU A 87 -26.542 -4.843 21.590 1.00 14.47 C ANISOU 664 CA LEU A 87 1554 2529 1413 -163 96 215 C ATOM 665 C LEU A 87 -25.096 -5.221 21.281 1.00 19.12 C ANISOU 665 C LEU A 87 2192 3065 2008 -147 90 222 C ATOM 666 O LEU A 87 -24.783 -6.405 21.112 1.00 19.30 O ANISOU 666 O LEU A 87 2248 3053 2031 -170 88 233 O ATOM 667 CB LEU A 87 -27.285 -4.430 20.321 1.00 15.34 C ANISOU 667 CB LEU A 87 1643 2650 1534 -157 71 201 C ATOM 668 CG LEU A 87 -28.711 -3.915 20.529 1.00 21.13 C ANISOU 668 CG LEU A 87 2308 3440 2281 -159 69 190 C ATOM 669 CD1 LEU A 87 -29.325 -3.449 19.221 1.00 13.90 C ANISOU 669 CD1 LEU A 87 1377 2528 1377 -144 24 181 C ATOM 670 CD2 LEU A 87 -29.585 -4.970 21.194 1.00 14.19 C ANISOU 670 CD2 LEU A 87 1398 2589 1403 -219 88 201 C ATOM 671 N ALA A 88 -24.197 -4.234 21.213 1.00 12.66 N ANISOU 671 N ALA A 88 1375 2235 1200 -109 89 214 N ATOM 672 CA ALA A 88 -22.787 -4.548 21.012 1.00 12.54 C ANISOU 672 CA ALA A 88 1384 2177 1203 -93 91 220 C ATOM 673 C ALA A 88 -22.227 -5.330 22.193 1.00 16.54 C ANISOU 673 C ALA A 88 1904 2671 1708 -99 83 237 C ATOM 674 O ALA A 88 -21.447 -6.272 22.010 1.00 17.32 O ANISOU 674 O ALA A 88 2026 2730 1825 -95 79 247 O ATOM 675 CB ALA A 88 -21.982 -3.269 20.782 1.00 12.38 C ANISOU 675 CB ALA A 88 1352 2150 1201 -64 93 211 C ATOM 676 N GLN A 89 -22.621 -4.962 23.415 1.00 16.26 N ANISOU 676 N GLN A 89 1863 2666 1649 -105 79 241 N ATOM 677 CA GLN A 89 -22.165 -5.705 24.585 1.00 19.43 C ANISOU 677 CA GLN A 89 2293 3055 2034 -113 64 264 C ATOM 678 C GLN A 89 -22.726 -7.118 24.587 1.00 19.78 C ANISOU 678 C GLN A 89 2368 3082 2066 -151 70 287 C ATOM 679 O GLN A 89 -22.015 -8.072 24.923 1.00 15.86 O ANISOU 679 O GLN A 89 1908 2543 1576 -149 50 311 O ATOM 680 CB GLN A 89 -22.559 -4.979 25.872 1.00 15.84 C ANISOU 680 CB GLN A 89 1841 2640 1538 -115 66 259 C ATOM 681 CG GLN A 89 -21.760 -5.430 27.080 1.00 23.39 C ANISOU 681 CG GLN A 89 2838 3578 2469 -114 34 282 C ATOM 682 CD GLN A 89 -20.270 -5.256 26.871 1.00 24.16 C ANISOU 682 CD GLN A 89 2926 3639 2614 -81 -9 280 C ATOM 683 OE1 GLN A 89 -19.822 -4.239 26.339 1.00 21.97 O ANISOU 683 OE1 GLN A 89 2615 3363 2370 -62 -10 255 O ATOM 684 NE2 GLN A 89 -19.494 -6.257 27.271 1.00 22.23 N ANISOU 684 NE2 GLN A 89 2710 3359 2379 -74 -44 309 N ATOM 685 N SER A 90 -23.999 -7.269 24.215 1.00 18.37 N ANISOU 685 N SER A 90 2172 2930 1876 -186 92 283 N ATOM 686 CA SER A 90 -24.599 -8.597 24.150 1.00 13.83 C ANISOU 686 CA SER A 90 1626 2334 1296 -235 96 304 C ATOM 687 C SER A 90 -23.877 -9.475 23.140 1.00 20.21 C ANISOU 687 C SER A 90 2468 3077 2132 -225 79 301 C ATOM 688 O SER A 90 -23.662 -10.669 23.384 1.00 23.54 O ANISOU 688 O SER A 90 2939 3450 2556 -244 69 324 O ATOM 689 CB SER A 90 -26.079 -8.483 23.801 1.00 14.03 C ANISOU 689 CB SER A 90 1608 2405 1318 -277 117 293 C ATOM 690 OG SER A 90 -26.717 -9.737 23.927 1.00 19.70 O ANISOU 690 OG SER A 90 2350 3104 2032 -341 122 317 O ATOM 691 N SER A 91 -23.489 -8.899 21.999 1.00 18.60 N ANISOU 691 N SER A 91 2248 2870 1950 -193 79 273 N ATOM 692 CA SER A 91 -22.727 -9.650 21.009 1.00 19.43 C ANISOU 692 CA SER A 91 2390 2917 2077 -175 77 262 C ATOM 693 C SER A 91 -21.414 -10.158 21.593 1.00 21.54 C ANISOU 693 C SER A 91 2677 3139 2369 -136 67 277 C ATOM 694 O SER A 91 -21.023 -11.308 21.360 1.00 24.94 O ANISOU 694 O SER A 91 3151 3510 2815 -131 61 281 O ATOM 695 CB SER A 91 -22.467 -8.777 19.781 1.00 13.30 C ANISOU 695 CB SER A 91 1597 2151 1305 -147 89 233 C ATOM 696 OG SER A 91 -23.683 -8.405 19.158 1.00 16.37 O ANISOU 696 OG SER A 91 1973 2575 1673 -177 82 222 O ATOM 697 N ILE A 92 -20.725 -9.316 22.364 1.00 22.30 N ANISOU 697 N ILE A 92 2741 3259 2473 -107 58 284 N ATOM 698 CA ILE A 92 -19.438 -9.706 22.931 1.00 21.31 C ANISOU 698 CA ILE A 92 2620 3096 2380 -67 33 299 C ATOM 699 C ILE A 92 -19.607 -10.872 23.894 1.00 21.65 C ANISOU 699 C ILE A 92 2716 3103 2405 -85 5 335 C ATOM 700 O ILE A 92 -18.841 -11.843 23.854 1.00 15.35 O ANISOU 700 O ILE A 92 1948 2245 1641 -55 -15 346 O ATOM 701 CB ILE A 92 -18.773 -8.494 23.607 1.00 20.99 C ANISOU 701 CB ILE A 92 2536 3092 2349 -44 16 296 C ATOM 702 CG1 ILE A 92 -18.357 -7.479 22.541 1.00 18.49 C ANISOU 702 CG1 ILE A 92 2176 2789 2061 -26 46 267 C ATOM 703 CG2 ILE A 92 -17.584 -8.925 24.444 1.00 18.74 C ANISOU 703 CG2 ILE A 92 2250 2775 2095 -9 -30 316 C ATOM 704 CD1 ILE A 92 -17.816 -6.202 23.098 1.00 26.08 C ANISOU 704 CD1 ILE A 92 3097 3777 3035 -16 30 261 C ATOM 705 N PHE A 93 -20.620 -10.808 24.761 1.00 21.48 N ANISOU 705 N PHE A 93 2712 3116 2332 -132 6 356 N ATOM 706 CA PHE A 93 -20.860 -11.919 25.677 1.00 19.85 C ANISOU 706 CA PHE A 93 2570 2874 2099 -162 -14 399 C ATOM 707 C PHE A 93 -21.172 -13.207 24.918 1.00 19.34 C ANISOU 707 C PHE A 93 2550 2744 2053 -185 -8 403 C ATOM 708 O PHE A 93 -20.665 -14.278 25.270 1.00 17.51 O ANISOU 708 O PHE A 93 2377 2444 1834 -174 -37 432 O ATOM 709 CB PHE A 93 -21.985 -11.568 26.653 1.00 21.65 C ANISOU 709 CB PHE A 93 2804 3159 2264 -216 8 418 C ATOM 710 CG PHE A 93 -21.610 -10.508 27.660 1.00 27.62 C ANISOU 710 CG PHE A 93 3545 3961 2987 -192 -6 416 C ATOM 711 CD1 PHE A 93 -20.322 -10.435 28.168 1.00 36.71 C ANISOU 711 CD1 PHE A 93 4709 5085 4155 -144 -60 426 C ATOM 712 CD2 PHE A 93 -22.544 -9.579 28.088 1.00 25.51 C ANISOU 712 CD2 PHE A 93 3251 3763 2679 -216 32 400 C ATOM 713 CE1 PHE A 93 -19.978 -9.462 29.089 1.00 31.03 C ANISOU 713 CE1 PHE A 93 3983 4403 3402 -129 -84 419 C ATOM 714 CE2 PHE A 93 -22.205 -8.606 29.008 1.00 25.54 C ANISOU 714 CE2 PHE A 93 3256 3801 2648 -194 19 390 C ATOM 715 CZ PHE A 93 -20.921 -8.548 29.510 1.00 27.05 C ANISOU 715 CZ PHE A 93 3468 3962 2847 -155 -43 399 C ATOM 716 N SER A 94 -21.991 -13.126 23.864 1.00 15.07 N ANISOU 716 N SER A 94 1991 2220 1516 -216 21 372 N ATOM 717 CA SER A 94 -22.291 -14.329 23.090 1.00 20.46 C ANISOU 717 CA SER A 94 2726 2836 2213 -244 20 366 C ATOM 718 C SER A 94 -21.038 -14.878 22.418 1.00 25.61 C ANISOU 718 C SER A 94 3404 3417 2911 -175 9 347 C ATOM 719 O SER A 94 -20.822 -16.095 22.395 1.00 30.76 O ANISOU 719 O SER A 94 4122 3986 3579 -174 -8 358 O ATOM 720 CB SER A 94 -23.382 -14.044 22.053 1.00 18.22 C ANISOU 720 CB SER A 94 2416 2587 1921 -289 39 332 C ATOM 721 OG SER A 94 -24.655 -13.872 22.663 1.00 17.38 O ANISOU 721 OG SER A 94 2283 2534 1787 -359 51 351 O ATOM 722 N LEU A 95 -20.196 -13.996 21.872 1.00 19.94 N ANISOU 722 N LEU A 95 2633 2726 2217 -117 23 317 N ATOM 723 CA LEU A 95 -18.971 -14.448 21.216 1.00 20.41 C ANISOU 723 CA LEU A 95 2701 2729 2327 -47 29 294 C ATOM 724 C LEU A 95 -18.008 -15.075 22.213 1.00 21.84 C ANISOU 724 C LEU A 95 2896 2860 2542 0 -12 329 C ATOM 725 O LEU A 95 -17.352 -16.077 21.905 1.00 23.83 O ANISOU 725 O LEU A 95 3186 3033 2834 45 -19 322 O ATOM 726 CB LEU A 95 -18.299 -13.282 20.492 1.00 20.11 C ANISOU 726 CB LEU A 95 2595 2738 2307 -7 63 261 C ATOM 727 CG LEU A 95 -18.986 -12.789 19.223 1.00 22.97 C ANISOU 727 CG LEU A 95 2961 3129 2638 -34 100 225 C ATOM 728 CD1 LEU A 95 -18.311 -11.532 18.699 1.00 22.84 C ANISOU 728 CD1 LEU A 95 2885 3158 2634 -2 132 207 C ATOM 729 CD2 LEU A 95 -18.963 -13.886 18.180 1.00 22.52 C ANISOU 729 CD2 LEU A 95 2971 3004 2582 -27 117 193 C ATOM 730 N LEU A 96 -17.893 -14.491 23.405 1.00 27.04 N ANISOU 730 N LEU A 96 3530 3561 3184 -4 -44 363 N ATOM 731 CA LEU A 96 -17.043 -15.089 24.425 1.00 24.84 C ANISOU 731 CA LEU A 96 3275 3236 2929 37 -102 403 C ATOM 732 C LEU A 96 -17.601 -16.427 24.896 1.00 22.33 C ANISOU 732 C LEU A 96 3054 2843 2586 3 -126 443 C ATOM 733 O LEU A 96 -16.831 -17.345 25.202 1.00 25.75 O ANISOU 733 O LEU A 96 3529 3199 3058 54 -169 466 O ATOM 734 CB LEU A 96 -16.878 -14.118 25.596 1.00 28.66 C ANISOU 734 CB LEU A 96 3724 3782 3382 32 -136 427 C ATOM 735 CG LEU A 96 -15.979 -14.548 26.758 1.00 30.56 C ANISOU 735 CG LEU A 96 3990 3988 3636 74 -214 471 C ATOM 736 CD1 LEU A 96 -14.606 -14.978 26.260 1.00 28.90 C ANISOU 736 CD1 LEU A 96 3735 3724 3520 162 -239 455 C ATOM 737 CD2 LEU A 96 -15.858 -13.424 27.774 1.00 23.73 C ANISOU 737 CD2 LEU A 96 3094 3190 2730 62 -247 480 C ATOM 738 N ALA A 97 -18.928 -16.567 24.940 1.00 17.36 N ANISOU 738 N ALA A 97 2461 2234 1902 -82 -101 454 N ATOM 739 CA ALA A 97 -19.520 -17.832 25.364 1.00 23.24 C ANISOU 739 CA ALA A 97 3300 2904 2625 -132 -118 496 C ATOM 740 C ALA A 97 -19.278 -18.929 24.338 1.00 22.25 C ANISOU 740 C ALA A 97 3226 2682 2547 -109 -115 468 C ATOM 741 O ALA A 97 -18.975 -20.072 24.703 1.00 22.14 O ANISOU 741 O ALA A 97 3292 2569 2549 -94 -152 501 O ATOM 742 CB ALA A 97 -21.015 -17.655 25.617 1.00 24.91 C ANISOU 742 CB ALA A 97 3518 3170 2778 -237 -82 510 C ATOM 743 N ILE A 98 -19.411 -18.601 23.051 1.00 17.89 N ANISOU 743 N ILE A 98 2638 2149 2011 -103 -74 406 N ATOM 744 CA ILE A 98 -19.164 -19.578 21.996 1.00 18.44 C ANISOU 744 CA ILE A 98 2764 2127 2115 -77 -66 366 C ATOM 745 C ILE A 98 -17.732 -20.092 22.067 1.00 22.39 C ANISOU 745 C ILE A 98 3270 2556 2680 33 -87 363 C ATOM 746 O ILE A 98 -17.486 -21.301 21.972 1.00 24.69 O ANISOU 746 O ILE A 98 3643 2737 3001 58 -109 366 O ATOM 747 CB ILE A 98 -19.482 -18.961 20.621 1.00 21.82 C ANISOU 747 CB ILE A 98 3155 2601 2534 -85 -18 300 C ATOM 748 CG1 ILE A 98 -20.987 -18.715 20.505 1.00 17.65 C ANISOU 748 CG1 ILE A 98 2627 2124 1954 -191 -13 304 C ATOM 749 CG2 ILE A 98 -18.971 -19.856 19.496 1.00 18.56 C ANISOU 749 CG2 ILE A 98 2804 2098 2151 -38 -2 247 C ATOM 750 CD1 ILE A 98 -21.385 -17.883 19.320 1.00 17.14 C ANISOU 750 CD1 ILE A 98 2521 2121 1870 -201 16 251 C ATOM 751 N ALA A 99 -16.765 -19.191 22.250 1.00 21.76 N ANISOU 751 N ALA A 99 3102 2534 2632 100 -85 357 N ATOM 752 CA ALA A 99 -15.374 -19.625 22.312 1.00 21.66 C ANISOU 752 CA ALA A 99 3070 2464 2697 208 -108 352 C ATOM 753 C ALA A 99 -15.130 -20.512 23.524 1.00 26.08 C ANISOU 753 C ALA A 99 3694 2949 3265 225 -186 418 C ATOM 754 O ALA A 99 -14.460 -21.546 23.418 1.00 29.34 O ANISOU 754 O ALA A 99 4154 3259 3735 296 -212 418 O ATOM 755 CB ALA A 99 -14.439 -18.415 22.330 1.00 21.87 C ANISOU 755 CB ALA A 99 2976 2574 2759 259 -95 337 C ATOM 756 N ILE A 100 -15.677 -20.133 24.681 1.00 26.13 N ANISOU 756 N ILE A 100 3714 3003 3212 164 -223 476 N ATOM 757 CA ILE A 100 -15.509 -20.947 25.881 1.00 24.64 C ANISOU 757 CA ILE A 100 3605 2745 3012 171 -300 549 C ATOM 758 C ILE A 100 -16.198 -22.294 25.715 1.00 23.09 C ANISOU 758 C ILE A 100 3533 2437 2803 127 -302 569 C ATOM 759 O ILE A 100 -15.676 -23.334 26.135 1.00 25.57 O ANISOU 759 O ILE A 100 3924 2641 3149 176 -359 606 O ATOM 760 CB ILE A 100 -16.030 -20.188 27.112 1.00 23.92 C ANISOU 760 CB ILE A 100 3513 2736 2841 107 -324 601 C ATOM 761 CG1 ILE A 100 -15.092 -19.017 27.422 1.00 24.16 C ANISOU 761 CG1 ILE A 100 3436 2848 2897 165 -348 584 C ATOM 762 CG2 ILE A 100 -16.171 -21.132 28.299 1.00 21.40 C ANISOU 762 CG2 ILE A 100 3310 2343 2480 86 -390 683 C ATOM 763 CD1 ILE A 100 -15.561 -18.121 28.539 1.00 23.97 C ANISOU 763 CD1 ILE A 100 3411 2908 2789 109 -366 618 C ATOM 764 N ASP A 101 -17.372 -22.297 25.088 1.00 24.33 N ANISOU 764 N ASP A 101 3711 2614 2918 33 -246 544 N ATOM 765 CA ASP A 101 -18.069 -23.548 24.834 1.00 24.05 C ANISOU 765 CA ASP A 101 3791 2471 2877 -24 -249 556 C ATOM 766 C ASP A 101 -17.239 -24.476 23.954 1.00 28.19 C ANISOU 766 C ASP A 101 4358 2878 3476 68 -256 509 C ATOM 767 O ASP A 101 -17.180 -25.688 24.198 1.00 33.86 O ANISOU 767 O ASP A 101 5186 3467 4214 75 -296 540 O ATOM 768 CB ASP A 101 -19.418 -23.260 24.187 1.00 23.62 C ANISOU 768 CB ASP A 101 3726 2472 2777 -138 -194 526 C ATOM 769 CG ASP A 101 -20.127 -24.514 23.767 1.00 27.49 C ANISOU 769 CG ASP A 101 4326 2851 3270 -205 -199 526 C ATOM 770 OD1 ASP A 101 -20.738 -25.168 24.638 1.00 25.56 O ANISOU 770 OD1 ASP A 101 4158 2558 2994 -283 -222 594 O ATOM 771 OD2 ASP A 101 -20.050 -24.857 22.571 1.00 30.08 O ANISOU 771 OD2 ASP A 101 4671 3132 3628 -184 -180 457 O ATOM 772 N ARG A 102 -16.588 -23.926 22.925 1.00 25.10 N ANISOU 772 N ARG A 102 3885 2525 3126 140 -211 434 N ATOM 773 CA ARG A 102 -15.762 -24.754 22.054 1.00 24.19 C ANISOU 773 CA ARG A 102 3804 2306 3080 237 -201 380 C ATOM 774 C ARG A 102 -14.513 -25.255 22.770 1.00 27.48 C ANISOU 774 C ARG A 102 4218 2652 3570 356 -262 414 C ATOM 775 O ARG A 102 -14.035 -26.359 22.480 1.00 30.97 O ANISOU 775 O ARG A 102 4735 2964 4067 427 -279 398 O ATOM 776 CB ARG A 102 -15.384 -23.977 20.793 1.00 26.08 C ANISOU 776 CB ARG A 102 3959 2615 3335 279 -124 294 C ATOM 777 CG ARG A 102 -16.532 -23.747 19.810 1.00 29.56 C ANISOU 777 CG ARG A 102 4427 3092 3711 181 -76 248 C ATOM 778 CD ARG A 102 -17.057 -25.059 19.232 1.00 37.17 C ANISOU 778 CD ARG A 102 5526 3927 4672 149 -85 220 C ATOM 779 NE ARG A 102 -18.043 -25.687 20.108 1.00 47.36 N ANISOU 779 NE ARG A 102 6893 5171 5929 45 -137 288 N ATOM 780 CZ ARG A 102 -18.310 -26.989 20.131 1.00 53.57 C ANISOU 780 CZ ARG A 102 7806 5818 6729 21 -171 297 C ATOM 781 NH1 ARG A 102 -19.223 -27.463 20.967 1.00 55.10 N ANISOU 781 NH1 ARG A 102 8063 5981 6892 -88 -208 366 N ATOM 782 NH2 ARG A 102 -17.659 -27.818 19.325 1.00 59.40 N ANISOU 782 NH2 ARG A 102 8613 6442 7512 104 -161 235 N ATOM 783 N TYR A 103 -13.978 -24.472 23.709 1.00 23.57 N ANISOU 783 N TYR A 103 3641 2235 3078 383 -301 459 N ATOM 784 CA TYR A 103 -12.823 -24.934 24.469 1.00 29.27 C ANISOU 784 CA TYR A 103 4356 2893 3870 493 -380 499 C ATOM 785 C TYR A 103 -13.186 -26.103 25.375 1.00 33.34 C ANISOU 785 C TYR A 103 5018 3288 4362 468 -458 577 C ATOM 786 O TYR A 103 -12.408 -27.054 25.512 1.00 34.72 O ANISOU 786 O TYR A 103 5242 3342 4606 567 -513 591 O ATOM 787 CB TYR A 103 -12.232 -23.787 25.282 1.00 28.08 C ANISOU 787 CB TYR A 103 4091 2856 3719 513 -417 527 C ATOM 788 CG TYR A 103 -11.078 -24.211 26.154 1.00 29.64 C ANISOU 788 CG TYR A 103 4278 2999 3987 620 -519 574 C ATOM 789 CD1 TYR A 103 -9.844 -24.516 25.601 1.00 32.77 C ANISOU 789 CD1 TYR A 103 4598 3351 4504 755 -521 529 C ATOM 790 CD2 TYR A 103 -11.223 -24.309 27.530 1.00 33.25 C ANISOU 790 CD2 TYR A 103 4798 3447 4388 590 -615 662 C ATOM 791 CE1 TYR A 103 -8.786 -24.908 26.394 1.00 37.43 C ANISOU 791 CE1 TYR A 103 5164 3890 5169 860 -626 571 C ATOM 792 CE2 TYR A 103 -10.173 -24.697 28.331 1.00 36.21 C ANISOU 792 CE2 TYR A 103 5167 3769 4822 690 -726 708 C ATOM 793 CZ TYR A 103 -8.956 -24.996 27.760 1.00 40.61 C ANISOU 793 CZ TYR A 103 5637 4283 5512 827 -737 663 C ATOM 794 OH TYR A 103 -7.905 -25.382 28.560 1.00 52.25 O ANISOU 794 OH TYR A 103 7092 5704 7056 934 -859 709 O ATOM 795 N ILE A 104 -14.362 -26.054 26.002 1.00 34.48 N ANISOU 795 N ILE A 104 5233 3458 4410 337 -460 631 N ATOM 796 CA ILE A 104 -14.794 -27.172 26.834 1.00 36.48 C ANISOU 796 CA ILE A 104 5636 3593 4630 294 -521 713 C ATOM 797 C ILE A 104 -14.997 -28.419 25.983 1.00 34.23 C ANISOU 797 C ILE A 104 5458 3160 4387 301 -506 678 C ATOM 798 O ILE A 104 -14.663 -29.535 26.401 1.00 33.99 O ANISOU 798 O ILE A 104 5540 2985 4388 346 -572 724 O ATOM 799 CB ILE A 104 -16.068 -26.799 27.612 1.00 32.47 C ANISOU 799 CB ILE A 104 5169 3157 4010 142 -503 772 C ATOM 800 CG1 ILE A 104 -15.817 -25.548 28.452 1.00 27.81 C ANISOU 800 CG1 ILE A 104 4485 2705 3375 145 -518 796 C ATOM 801 CG2 ILE A 104 -16.503 -27.947 28.504 1.00 33.18 C ANISOU 801 CG2 ILE A 104 5421 3125 4061 86 -557 865 C ATOM 802 CD1 ILE A 104 -17.063 -24.972 29.072 1.00 27.39 C ANISOU 802 CD1 ILE A 104 4446 2746 3215 8 -474 832 C ATOM 803 N ALA A 105 -15.526 -28.252 24.769 1.00 31.82 N ANISOU 803 N ALA A 105 5128 2882 4082 260 -426 595 N ATOM 804 CA ALA A 105 -15.804 -29.410 23.928 1.00 32.90 C ANISOU 804 CA ALA A 105 5377 2877 4247 254 -413 553 C ATOM 805 C ALA A 105 -14.528 -30.102 23.473 1.00 38.14 C ANISOU 805 C ALA A 105 6051 3428 5011 419 -434 509 C ATOM 806 O ALA A 105 -14.538 -31.313 23.221 1.00 45.00 O ANISOU 806 O ALA A 105 7048 4137 5913 440 -457 501 O ATOM 807 CB ALA A 105 -16.637 -28.995 22.717 1.00 31.26 C ANISOU 807 CB ALA A 105 5139 2732 4005 175 -333 470 C ATOM 808 N ILE A 106 -13.424 -29.365 23.367 1.00 38.86 N ANISOU 808 N ILE A 106 6008 3597 5159 536 -423 478 N ATOM 809 CA ILE A 106 -12.186 -29.942 22.863 1.00 39.95 C ANISOU 809 CA ILE A 106 6129 3645 5406 700 -427 426 C ATOM 810 C ILE A 106 -11.196 -30.287 23.971 1.00 43.87 C ANISOU 810 C ILE A 106 6616 4086 5967 809 -531 499 C ATOM 811 O ILE A 106 -10.337 -31.159 23.764 1.00 45.03 O ANISOU 811 O ILE A 106 6793 4108 6209 942 -560 477 O ATOM 812 CB ILE A 106 -11.531 -29.003 21.830 1.00 40.64 C ANISOU 812 CB ILE A 106 6067 3844 5531 766 -335 333 C ATOM 813 CG1 ILE A 106 -10.653 -29.801 20.873 1.00 42.20 C ANISOU 813 CG1 ILE A 106 6281 3933 5820 905 -293 249 C ATOM 814 CG2 ILE A 106 -10.711 -27.928 22.518 1.00 38.73 C ANISOU 814 CG2 ILE A 106 5668 3726 5320 816 -361 365 C ATOM 815 CD1 ILE A 106 -10.295 -29.033 19.632 1.00 43.87 C ANISOU 815 CD1 ILE A 106 6389 4240 6041 937 -176 149 C ATOM 816 N ALA A 107 -11.294 -29.648 25.137 1.00 44.54 N ANISOU 816 N ALA A 107 6667 4255 6002 761 -593 583 N ATOM 817 CA ALA A 107 -10.383 -29.932 26.237 1.00 46.37 C ANISOU 817 CA ALA A 107 6897 4439 6283 858 -710 658 C ATOM 818 C ALA A 107 -10.893 -31.047 27.141 1.00 50.90 C ANISOU 818 C ALA A 107 7657 4870 6812 813 -797 756 C ATOM 819 O ALA A 107 -10.104 -31.882 27.594 1.00 57.21 O ANISOU 819 O ALA A 107 8511 5546 7681 927 -890 795 O ATOM 820 CB ALA A 107 -10.138 -28.666 27.061 1.00 44.64 C ANISOU 820 CB ALA A 107 6557 4377 6026 834 -743 696 C ATOM 821 N ILE A 108 -12.194 -31.081 27.413 1.00 47.37 N ANISOU 821 N ILE A 108 7307 4437 6253 649 -769 797 N ATOM 822 CA ILE A 108 -12.778 -32.124 28.255 1.00 46.67 C ANISOU 822 CA ILE A 108 7404 4216 6114 582 -836 896 C ATOM 823 C ILE A 108 -14.038 -32.673 27.596 1.00 48.67 C ANISOU 823 C ILE A 108 7759 4414 6320 443 -763 872 C ATOM 824 O ILE A 108 -15.146 -32.484 28.121 1.00 48.01 O ANISOU 824 O ILE A 108 7725 4380 6138 288 -740 927 O ATOM 825 CB ILE A 108 -13.076 -31.594 29.665 1.00 44.00 C ANISOU 825 CB ILE A 108 7086 3957 5674 507 -894 1002 C ATOM 826 CG1 ILE A 108 -13.691 -30.195 29.592 1.00 40.49 C ANISOU 826 CG1 ILE A 108 6516 3713 5157 410 -813 969 C ATOM 827 CG2 ILE A 108 -11.809 -31.579 30.502 1.00 43.10 C ANISOU 827 CG2 ILE A 108 6942 3824 5611 648 -1016 1052 C ATOM 828 CD1 ILE A 108 -14.130 -29.659 30.935 1.00 40.38 C ANISOU 828 CD1 ILE A 108 6535 3779 5028 325 -850 1061 C ATOM 829 N PRO A 109 -13.922 -33.375 26.465 1.00 49.57 N ANISOU 829 N PRO A 109 7909 4423 6502 491 -726 788 N ATOM 830 CA PRO A 109 -15.131 -33.837 25.764 1.00 50.51 C ANISOU 830 CA PRO A 109 8118 4496 6577 352 -665 754 C ATOM 831 C PRO A 109 -15.893 -34.914 26.513 1.00 60.02 C ANISOU 831 C PRO A 109 9507 5558 7739 244 -717 851 C ATOM 832 O PRO A 109 -17.096 -35.073 26.275 1.00 59.06 O ANISOU 832 O PRO A 109 9439 5439 7562 84 -672 852 O ATOM 833 CB PRO A 109 -14.582 -34.367 24.435 1.00 45.49 C ANISOU 833 CB PRO A 109 7488 3769 6027 458 -626 638 C ATOM 834 CG PRO A 109 -13.188 -34.803 24.765 1.00 46.25 C ANISOU 834 CG PRO A 109 7574 3777 6221 648 -694 649 C ATOM 835 CD PRO A 109 -12.686 -33.849 25.817 1.00 47.24 C ANISOU 835 CD PRO A 109 7584 4037 6328 676 -741 720 C ATOM 836 N LEU A 110 -15.235 -35.651 27.411 1.00 70.79 N ANISOU 836 N LEU A 110 10969 6797 9130 323 -813 937 N ATOM 837 CA LEU A 110 -15.912 -36.726 28.129 1.00 75.28 C ANISOU 837 CA LEU A 110 11732 7215 9657 220 -863 1038 C ATOM 838 C LEU A 110 -16.955 -36.177 29.095 1.00 72.94 C ANISOU 838 C LEU A 110 11442 7033 9239 44 -839 1130 C ATOM 839 O LEU A 110 -18.016 -36.785 29.284 1.00 73.38 O ANISOU 839 O LEU A 110 11615 7022 9245 -113 -818 1180 O ATOM 840 CB LEU A 110 -14.885 -37.585 28.870 1.00 76.85 C ANISOU 840 CB LEU A 110 12035 7253 9911 361 -982 1112 C ATOM 841 CG LEU A 110 -13.816 -38.259 28.004 1.00 78.37 C ANISOU 841 CG LEU A 110 12227 7315 10236 549 -1005 1024 C ATOM 842 CD1 LEU A 110 -12.829 -39.043 28.857 1.00 80.70 C ANISOU 842 CD1 LEU A 110 12542 7535 10585 676 -1098 1082 C ATOM 843 CD2 LEU A 110 -14.459 -39.160 26.962 1.00 79.14 C ANISOU 843 CD2 LEU A 110 12430 7281 10359 487 -952 948 C ATOM 844 N ARG A 111 -16.679 -35.029 29.710 1.00 71.25 N ANISOU 844 N ARG A 111 11102 6992 8978 66 -836 1151 N ATOM 845 CA ARG A 111 -17.589 -34.412 30.666 1.00 71.11 C ANISOU 845 CA ARG A 111 11083 7094 8841 -81 -805 1229 C ATOM 846 C ARG A 111 -18.198 -33.121 30.128 1.00 65.91 C ANISOU 846 C ARG A 111 10254 6639 8149 -148 -705 1152 C ATOM 847 O ARG A 111 -18.596 -32.247 30.900 1.00 65.59 O ANISOU 847 O ARG A 111 10159 6737 8024 -213 -680 1193 O ATOM 848 CB ARG A 111 -16.874 -34.156 31.991 1.00 76.00 C ANISOU 848 CB ARG A 111 11728 7738 9412 -15 -893 1327 C ATOM 849 CG ARG A 111 -15.476 -33.595 31.842 1.00 81.31 C ANISOU 849 CG ARG A 111 12275 8456 10163 175 -953 1276 C ATOM 850 CD ARG A 111 -14.796 -33.469 33.194 1.00 88.32 C ANISOU 850 CD ARG A 111 13208 9348 11001 233 -1064 1378 C ATOM 851 NE ARG A 111 -13.383 -33.127 33.061 1.00 93.92 N ANISOU 851 NE ARG A 111 13802 10074 11809 419 -1141 1335 N ATOM 852 CZ ARG A 111 -12.560 -32.930 34.086 1.00 99.62 C ANISOU 852 CZ ARG A 111 14512 10824 12516 498 -1246 1393 C ATOM 853 NH1 ARG A 111 -13.007 -33.040 35.331 1.00102.00 N ANISOU 853 NH1 ARG A 111 14896 11164 12698 405 -1262 1476 N ATOM 854 NH2 ARG A 111 -11.288 -32.622 33.865 1.00101.45 N ANISOU 854 NH2 ARG A 111 14623 11068 12855 663 -1317 1349 N ATOM 855 N TYR A 112 -18.281 -32.992 28.803 1.00 63.85 N ANISOU 855 N TYR A 112 9917 6392 7950 -130 -650 1039 N ATOM 856 CA TYR A 112 -18.874 -31.795 28.217 1.00 59.33 C ANISOU 856 CA TYR A 112 9194 6001 7349 -189 -564 967 C ATOM 857 C TYR A 112 -20.391 -31.800 28.372 1.00 65.10 C ANISOU 857 C TYR A 112 9951 6776 8008 -383 -503 998 C ATOM 858 O TYR A 112 -20.985 -30.797 28.784 1.00 65.76 O ANISOU 858 O TYR A 112 9942 7016 8029 -452 -454 1010 O ATOM 859 CB TYR A 112 -18.480 -31.682 26.744 1.00 54.10 C ANISOU 859 CB TYR A 112 8457 5335 6763 -110 -527 842 C ATOM 860 CG TYR A 112 -19.219 -30.593 25.997 1.00 46.67 C ANISOU 860 CG TYR A 112 7387 4556 5790 -182 -444 771 C ATOM 861 CD1 TYR A 112 -18.806 -29.270 26.069 1.00 45.01 C ANISOU 861 CD1 TYR A 112 7030 4505 5568 -129 -419 746 C ATOM 862 CD2 TYR A 112 -20.335 -30.888 25.225 1.00 45.97 C ANISOU 862 CD2 TYR A 112 7326 4453 5688 -304 -401 730 C ATOM 863 CE1 TYR A 112 -19.483 -28.272 25.393 1.00 44.79 C ANISOU 863 CE1 TYR A 112 6893 4613 5512 -189 -351 686 C ATOM 864 CE2 TYR A 112 -21.020 -29.897 24.550 1.00 43.36 C ANISOU 864 CE2 TYR A 112 6879 4267 5331 -363 -340 670 C ATOM 865 CZ TYR A 112 -20.589 -28.592 24.634 1.00 43.38 C ANISOU 865 CZ TYR A 112 6743 4420 5318 -302 -314 650 C ATOM 866 OH TYR A 112 -21.266 -27.604 23.956 1.00 43.72 O ANISOU 866 OH TYR A 112 6679 4595 5336 -354 -260 594 O ATOM 867 N ASN A 113 -21.036 -32.925 28.045 1.00 68.56 N ANISOU 867 N ASN A 113 10512 7075 8463 -472 -505 1009 N ATOM 868 CA ASN A 113 -22.495 -32.986 28.077 1.00 70.81 C ANISOU 868 CA ASN A 113 10805 7399 8699 -663 -447 1030 C ATOM 869 C ASN A 113 -23.034 -32.828 29.494 1.00 69.57 C ANISOU 869 C ASN A 113 10685 7295 8453 -761 -433 1148 C ATOM 870 O ASN A 113 -24.087 -32.214 29.699 1.00 68.32 O ANISOU 870 O ASN A 113 10452 7264 8244 -887 -361 1156 O ATOM 871 CB ASN A 113 -22.982 -34.300 27.466 1.00 76.50 C ANISOU 871 CB ASN A 113 11660 7942 9464 -741 -465 1020 C ATOM 872 CG ASN A 113 -22.718 -34.385 25.974 1.00 79.19 C ANISOU 872 CG ASN A 113 11967 8250 9873 -674 -460 890 C ATOM 873 OD1 ASN A 113 -22.680 -33.369 25.278 1.00 78.06 O ANISOU 873 OD1 ASN A 113 11683 8247 9729 -635 -419 810 O ATOM 874 ND2 ASN A 113 -22.537 -35.604 25.476 1.00 81.69 N ANISOU 874 ND2 ASN A 113 12424 8373 10241 -661 -502 870 N ATOM 875 N GLY A 114 -22.331 -33.381 30.485 1.00 70.50 N ANISOU 875 N GLY A 114 10921 7317 8548 -704 -500 1240 N ATOM 876 CA GLY A 114 -22.760 -33.218 31.861 1.00 72.56 C ANISOU 876 CA GLY A 114 11235 7628 8706 -789 -487 1353 C ATOM 877 C GLY A 114 -22.504 -31.834 32.413 1.00 71.48 C ANISOU 877 C GLY A 114 10969 7680 8509 -739 -463 1342 C ATOM 878 O GLY A 114 -23.230 -31.377 33.301 1.00 76.64 O ANISOU 878 O GLY A 114 11620 8431 9069 -840 -408 1401 O ATOM 879 N LEU A 115 -21.479 -31.150 31.904 1.00 66.94 N ANISOU 879 N LEU A 115 10289 7157 7989 -586 -498 1267 N ATOM 880 CA LEU A 115 -21.145 -29.801 32.349 1.00 60.77 C ANISOU 880 CA LEU A 115 9383 6544 7162 -533 -484 1247 C ATOM 881 C LEU A 115 -21.935 -28.739 31.590 1.00 56.68 C ANISOU 881 C LEU A 115 8708 6182 6647 -589 -390 1160 C ATOM 882 O LEU A 115 -22.619 -27.917 32.206 1.00 56.56 O ANISOU 882 O LEU A 115 8639 6295 6555 -663 -331 1178 O ATOM 883 CB LEU A 115 -19.636 -29.559 32.203 1.00 58.10 C ANISOU 883 CB LEU A 115 9000 6186 6888 -348 -569 1213 C ATOM 884 CG LEU A 115 -19.081 -28.128 32.227 1.00 54.23 C ANISOU 884 CG LEU A 115 8355 5857 6393 -272 -561 1158 C ATOM 885 CD1 LEU A 115 -19.427 -27.402 33.510 1.00 54.56 C ANISOU 885 CD1 LEU A 115 8408 6004 6316 -331 -554 1222 C ATOM 886 CD2 LEU A 115 -17.575 -28.134 32.014 1.00 54.23 C ANISOU 886 CD2 LEU A 115 8313 5812 6480 -100 -649 1129 C ATOM 887 N VAL A 116 -21.858 -28.747 30.262 1.00 53.69 N ANISOU 887 N VAL A 116 8261 5789 6351 -553 -374 1065 N ATOM 888 CA VAL A 116 -22.484 -27.729 29.426 1.00 50.08 C ANISOU 888 CA VAL A 116 7658 5468 5902 -587 -303 980 C ATOM 889 C VAL A 116 -23.839 -28.272 28.983 1.00 54.50 C ANISOU 889 C VAL A 116 8241 6008 6460 -740 -251 978 C ATOM 890 O VAL A 116 -23.925 -29.093 28.066 1.00 57.41 O ANISOU 890 O VAL A 116 8658 6269 6885 -753 -266 938 O ATOM 891 CB VAL A 116 -21.603 -27.356 28.231 1.00 43.80 C ANISOU 891 CB VAL A 116 6779 4678 5185 -462 -316 881 C ATOM 892 CG1 VAL A 116 -22.218 -26.201 27.463 1.00 35.06 C ANISOU 892 CG1 VAL A 116 5531 3716 4073 -494 -250 806 C ATOM 893 CG2 VAL A 116 -20.198 -27.006 28.698 1.00 42.84 C ANISOU 893 CG2 VAL A 116 6635 4558 5084 -315 -375 891 C ATOM 894 N THR A 117 -24.902 -27.805 29.632 1.00 53.66 N ANISOU 894 N THR A 117 8097 6003 6290 -858 -188 1016 N ATOM 895 CA THR A 117 -26.261 -28.251 29.366 1.00 51.11 C ANISOU 895 CA THR A 117 7773 5677 5968 -1018 -135 1022 C ATOM 896 C THR A 117 -27.084 -27.109 28.785 1.00 48.71 C ANISOU 896 C THR A 117 7305 5535 5669 -1055 -73 952 C ATOM 897 O THR A 117 -26.709 -25.936 28.856 1.00 50.99 O ANISOU 897 O THR A 117 7495 5941 5939 -973 -59 918 O ATOM 898 CB THR A 117 -26.920 -28.782 30.645 1.00 48.54 C ANISOU 898 CB THR A 117 7541 5330 5571 -1139 -103 1134 C ATOM 899 OG1 THR A 117 -26.940 -27.747 31.633 1.00 49.49 O ANISOU 899 OG1 THR A 117 7604 5587 5612 -1123 -61 1162 O ATOM 900 CG2 THR A 117 -26.152 -29.980 31.189 1.00 45.06 C ANISOU 900 CG2 THR A 117 7281 4713 5127 -1106 -176 1211 C ATOM 901 N GLY A 118 -28.231 -27.469 28.205 1.00 47.55 N ANISOU 901 N GLY A 118 7128 5387 5550 -1181 -42 933 N ATOM 902 CA GLY A 118 -29.076 -26.470 27.576 1.00 43.89 C ANISOU 902 CA GLY A 118 6509 5067 5101 -1215 3 867 C ATOM 903 C GLY A 118 -29.722 -25.517 28.560 1.00 44.44 C ANISOU 903 C GLY A 118 6490 5283 5113 -1256 78 902 C ATOM 904 O GLY A 118 -29.902 -24.335 28.254 1.00 46.11 O ANISOU 904 O GLY A 118 6572 5622 5325 -1210 104 847 O ATOM 905 N THR A 119 -30.075 -26.007 29.751 1.00 47.80 N ANISOU 905 N THR A 119 6991 5690 5484 -1339 117 993 N ATOM 906 CA THR A 119 -30.790 -25.170 30.710 1.00 48.82 C ANISOU 906 CA THR A 119 7043 5957 5550 -1388 205 1022 C ATOM 907 C THR A 119 -29.867 -24.137 31.341 1.00 46.77 C ANISOU 907 C THR A 119 6771 5769 5231 -1256 197 1015 C ATOM 908 O THR A 119 -30.278 -22.995 31.584 1.00 43.47 O ANISOU 908 O THR A 119 6242 5487 4787 -1241 254 984 O ATOM 909 CB THR A 119 -31.432 -26.040 31.788 1.00 56.58 C ANISOU 909 CB THR A 119 8123 6894 6479 -1523 259 1124 C ATOM 910 OG1 THR A 119 -32.191 -27.085 31.168 1.00 62.55 O ANISOU 910 OG1 THR A 119 8902 7563 7301 -1651 253 1131 O ATOM 911 CG2 THR A 119 -32.355 -25.205 32.657 1.00 58.35 C ANISOU 911 CG2 THR A 119 8255 7270 6644 -1587 371 1143 C ATOM 912 N ARG A 120 -28.619 -24.522 31.622 1.00 48.35 N ANISOU 912 N ARG A 120 7081 5875 5414 -1160 122 1043 N ATOM 913 CA ARG A 120 -27.645 -23.569 32.143 1.00 47.46 C ANISOU 913 CA ARG A 120 6952 5822 5258 -1036 96 1031 C ATOM 914 C ARG A 120 -27.287 -22.515 31.104 1.00 50.41 C ANISOU 914 C ARG A 120 7195 6268 5689 -940 81 932 C ATOM 915 O ARG A 120 -26.948 -21.383 31.464 1.00 55.24 O ANISOU 915 O ARG A 120 7745 6975 6268 -873 91 906 O ATOM 916 CB ARG A 120 -26.384 -24.301 32.608 1.00 50.02 C ANISOU 916 CB ARG A 120 7414 6023 5569 -954 5 1082 C ATOM 917 CG ARG A 120 -26.610 -25.312 33.726 1.00 54.11 C ANISOU 917 CG ARG A 120 8087 6458 6016 -1038 7 1193 C ATOM 918 CD ARG A 120 -25.367 -26.164 33.956 1.00 55.56 C ANISOU 918 CD ARG A 120 8402 6496 6210 -947 -102 1239 C ATOM 919 NE ARG A 120 -25.620 -27.288 34.854 1.00 59.52 N ANISOU 919 NE ARG A 120 9071 6891 6653 -1032 -110 1349 N ATOM 920 CZ ARG A 120 -24.750 -28.264 35.094 1.00 61.76 C ANISOU 920 CZ ARG A 120 9494 7024 6949 -974 -205 1406 C ATOM 921 NH1 ARG A 120 -25.064 -29.246 35.928 1.00 63.13 N ANISOU 921 NH1 ARG A 120 9783 7120 7084 -1036 -202 1480 N ATOM 922 NH2 ARG A 120 -23.566 -28.264 34.498 1.00 63.66 N ANISOU 922 NH2 ARG A 120 9712 7209 7265 -827 -295 1357 N ATOM 923 N ALA A 121 -27.354 -22.866 29.816 1.00 46.72 N ANISOU 923 N ALA A 121 6696 5755 5303 -937 56 876 N ATOM 924 CA ALA A 121 -27.045 -21.899 28.767 1.00 37.52 C ANISOU 924 CA ALA A 121 5419 4653 4183 -854 46 788 C ATOM 925 C ALA A 121 -28.098 -20.802 28.698 1.00 35.21 C ANISOU 925 C ALA A 121 4998 4502 3880 -898 112 753 C ATOM 926 O ALA A 121 -27.761 -19.623 28.540 1.00 31.52 O ANISOU 926 O ALA A 121 4449 4117 3409 -820 117 708 O ATOM 927 CB ALA A 121 -26.925 -22.603 27.417 1.00 36.13 C ANISOU 927 CB ALA A 121 5259 4390 4078 -847 8 738 C ATOM 928 N ALA A 122 -29.377 -21.171 28.806 1.00 31.96 N ANISOU 928 N ALA A 122 4560 4114 3468 -1021 163 773 N ATOM 929 CA ALA A 122 -30.435 -20.168 28.771 1.00 26.99 C ANISOU 929 CA ALA A 122 3796 3619 2840 -1058 227 740 C ATOM 930 C ALA A 122 -30.340 -19.222 29.957 1.00 30.50 C ANISOU 930 C ALA A 122 4222 4154 3212 -1021 278 760 C ATOM 931 O ALA A 122 -30.665 -18.034 29.833 1.00 33.13 O ANISOU 931 O ALA A 122 4448 4592 3548 -981 309 712 O ATOM 932 CB ALA A 122 -31.806 -20.843 28.737 1.00 25.52 C ANISOU 932 CB ALA A 122 3578 3440 2679 -1204 273 763 C ATOM 933 N GLY A 123 -29.898 -19.726 31.112 1.00 29.49 N ANISOU 933 N GLY A 123 4208 3983 3015 -1033 282 830 N ATOM 934 CA GLY A 123 -29.698 -18.854 32.256 1.00 29.31 C ANISOU 934 CA GLY A 123 4190 4037 2908 -994 320 844 C ATOM 935 C GLY A 123 -28.536 -17.902 32.055 1.00 28.82 C ANISOU 935 C GLY A 123 4109 3991 2850 -860 260 796 C ATOM 936 O GLY A 123 -28.621 -16.722 32.405 1.00 29.66 O ANISOU 936 O GLY A 123 4153 4191 2925 -818 293 761 O ATOM 937 N ILE A 124 -27.437 -18.401 31.484 1.00 29.41 N ANISOU 937 N ILE A 124 4235 3973 2967 -793 175 793 N ATOM 938 CA ILE A 124 -26.295 -17.546 31.174 1.00 29.44 C ANISOU 938 CA ILE A 124 4205 3988 2991 -674 121 746 C ATOM 939 C ILE A 124 -26.694 -16.462 30.179 1.00 31.35 C ANISOU 939 C ILE A 124 4319 4310 3282 -646 146 669 C ATOM 940 O ILE A 124 -26.299 -15.299 30.318 1.00 31.77 O ANISOU 940 O ILE A 124 4322 4425 3324 -581 144 634 O ATOM 941 CB ILE A 124 -25.122 -18.396 30.652 1.00 28.58 C ANISOU 941 CB ILE A 124 4161 3763 2933 -611 38 754 C ATOM 942 CG1 ILE A 124 -24.563 -19.269 31.772 1.00 32.13 C ANISOU 942 CG1 ILE A 124 4742 4137 3330 -614 -5 834 C ATOM 943 CG2 ILE A 124 -24.022 -17.517 30.085 1.00 25.90 C ANISOU 943 CG2 ILE A 124 3761 3444 2638 -500 -5 699 C ATOM 944 CD1 ILE A 124 -23.422 -20.149 31.331 1.00 37.43 C ANISOU 944 CD1 ILE A 124 5473 4688 4060 -542 -88 843 C ATOM 945 N ILE A 125 -27.493 -16.821 29.170 1.00 29.33 N ANISOU 945 N ILE A 125 4016 4049 3081 -698 162 644 N ATOM 946 CA ILE A 125 -27.912 -15.843 28.168 1.00 26.95 C ANISOU 946 CA ILE A 125 3603 3816 2822 -671 174 577 C ATOM 947 C ILE A 125 -28.762 -14.755 28.809 1.00 28.61 C ANISOU 947 C ILE A 125 3734 4138 2999 -684 237 564 C ATOM 948 O ILE A 125 -28.580 -13.561 28.536 1.00 24.43 O ANISOU 948 O ILE A 125 3140 3665 2478 -618 236 518 O ATOM 949 CB ILE A 125 -28.651 -16.545 27.014 1.00 25.25 C ANISOU 949 CB ILE A 125 3365 3568 2662 -732 165 556 C ATOM 950 CG1 ILE A 125 -27.670 -17.408 26.217 1.00 26.41 C ANISOU 950 CG1 ILE A 125 3588 3604 2844 -692 105 548 C ATOM 951 CG2 ILE A 125 -29.345 -15.530 26.118 1.00 18.19 C ANISOU 951 CG2 ILE A 125 2356 2755 1801 -719 176 498 C ATOM 952 CD1 ILE A 125 -28.327 -18.335 25.220 1.00 19.11 C ANISOU 952 CD1 ILE A 125 2679 2624 1960 -762 88 531 C ATOM 953 N ALA A 126 -29.695 -15.148 29.681 1.00 31.42 N ANISOU 953 N ALA A 126 4098 4523 3316 -769 299 604 N ATOM 954 CA ALA A 126 -30.489 -14.166 30.412 1.00 29.84 C ANISOU 954 CA ALA A 126 3829 4430 3079 -776 373 590 C ATOM 955 C ALA A 126 -29.601 -13.233 31.229 1.00 27.55 C ANISOU 955 C ALA A 126 3577 4164 2729 -692 363 579 C ATOM 956 O ALA A 126 -29.822 -12.018 31.257 1.00 26.31 O ANISOU 956 O ALA A 126 3349 4078 2570 -643 389 532 O ATOM 957 CB ALA A 126 -31.497 -14.878 31.314 1.00 20.90 C ANISOU 957 CB ALA A 126 2715 3318 1906 -886 453 642 C ATOM 958 N ILE A 127 -28.579 -13.784 31.887 1.00 23.58 N ANISOU 958 N ILE A 127 3186 3595 2179 -673 317 623 N ATOM 959 CA ILE A 127 -27.696 -12.971 32.717 1.00 26.22 C ANISOU 959 CA ILE A 127 3562 3947 2455 -602 292 615 C ATOM 960 C ILE A 127 -26.898 -11.993 31.860 1.00 24.86 C ANISOU 960 C ILE A 127 3327 3778 2341 -511 238 555 C ATOM 961 O ILE A 127 -26.757 -10.814 32.210 1.00 21.96 O ANISOU 961 O ILE A 127 2931 3463 1949 -464 247 516 O ATOM 962 CB ILE A 127 -26.783 -13.882 33.559 1.00 31.44 C ANISOU 962 CB ILE A 127 4355 4531 3060 -603 236 680 C ATOM 963 CG1 ILE A 127 -27.613 -14.607 34.627 1.00 30.67 C ANISOU 963 CG1 ILE A 127 4333 4442 2878 -696 304 745 C ATOM 964 CG2 ILE A 127 -25.644 -13.084 34.186 1.00 26.96 C ANISOU 964 CG2 ILE A 127 3822 3968 2452 -521 175 665 C ATOM 965 CD1 ILE A 127 -26.872 -15.706 35.373 1.00 28.70 C ANISOU 965 CD1 ILE A 127 4228 4101 2575 -710 244 824 C ATOM 966 N CYS A 128 -26.383 -12.456 30.717 1.00 22.48 N ANISOU 966 N CYS A 128 3011 3418 2114 -489 188 544 N ATOM 967 CA CYS A 128 -25.573 -11.591 29.860 1.00 25.92 C ANISOU 967 CA CYS A 128 3394 3853 2602 -411 147 494 C ATOM 968 C CYS A 128 -26.391 -10.461 29.253 1.00 25.84 C ANISOU 968 C CYS A 128 3287 3914 2616 -401 187 441 C ATOM 969 O CYS A 128 -25.863 -9.364 29.035 1.00 26.00 O ANISOU 969 O CYS A 128 3274 3955 2650 -341 169 404 O ATOM 970 CB CYS A 128 -24.916 -12.413 28.754 1.00 28.85 C ANISOU 970 CB CYS A 128 3777 4147 3039 -393 101 493 C ATOM 971 SG CYS A 128 -23.743 -13.623 29.359 1.00 30.35 S ANISOU 971 SG CYS A 128 4072 4239 3220 -373 38 548 S ATOM 972 N TRP A 129 -27.670 -10.704 28.966 1.00 24.80 N ANISOU 972 N TRP A 129 3108 3818 2496 -460 235 440 N ATOM 973 CA TRP A 129 -28.516 -9.622 28.479 1.00 25.11 C ANISOU 973 CA TRP A 129 3051 3927 2562 -443 266 393 C ATOM 974 C TRP A 129 -28.747 -8.579 29.564 1.00 23.70 C ANISOU 974 C TRP A 129 2863 3811 2332 -416 311 376 C ATOM 975 O TRP A 129 -28.732 -7.373 29.287 1.00 20.50 O ANISOU 975 O TRP A 129 2409 3437 1944 -359 308 331 O ATOM 976 CB TRP A 129 -29.839 -10.183 27.956 1.00 25.88 C ANISOU 976 CB TRP A 129 3089 4050 2694 -514 298 395 C ATOM 977 CG TRP A 129 -29.757 -10.619 26.526 1.00 27.32 C ANISOU 977 CG TRP A 129 3257 4189 2935 -517 246 380 C ATOM 978 CD1 TRP A 129 -29.600 -11.895 26.058 1.00 26.96 C ANISOU 978 CD1 TRP A 129 3265 4074 2906 -565 218 403 C ATOM 979 CD2 TRP A 129 -29.805 -9.772 25.373 1.00 26.39 C ANISOU 979 CD2 TRP A 129 3083 4087 2857 -468 216 336 C ATOM 980 NE1 TRP A 129 -29.558 -11.892 24.684 1.00 28.11 N ANISOU 980 NE1 TRP A 129 3391 4195 3093 -550 175 370 N ATOM 981 CE2 TRP A 129 -29.681 -10.601 24.239 1.00 27.30 C ANISOU 981 CE2 TRP A 129 3222 4146 3002 -492 172 333 C ATOM 982 CE3 TRP A 129 -29.940 -8.392 25.189 1.00 23.85 C ANISOU 982 CE3 TRP A 129 2702 3814 2545 -407 219 300 C ATOM 983 CZ2 TRP A 129 -29.693 -10.096 22.939 1.00 26.45 C ANISOU 983 CZ2 TRP A 129 3087 4038 2923 -459 134 298 C ATOM 984 CZ3 TRP A 129 -29.953 -7.891 23.896 1.00 24.01 C ANISOU 984 CZ3 TRP A 129 2693 3828 2600 -374 178 271 C ATOM 985 CH2 TRP A 129 -29.828 -8.741 22.789 1.00 25.20 C ANISOU 985 CH2 TRP A 129 2873 3930 2770 -401 136 272 C ATOM 986 N VAL A 130 -28.939 -9.020 30.811 1.00 23.28 N ANISOU 986 N VAL A 130 2866 3771 2209 -456 352 410 N ATOM 987 CA VAL A 130 -29.084 -8.072 31.913 1.00 19.89 C ANISOU 987 CA VAL A 130 2448 3396 1713 -429 397 389 C ATOM 988 C VAL A 130 -27.801 -7.267 32.092 1.00 20.15 C ANISOU 988 C VAL A 130 2525 3399 1730 -356 331 366 C ATOM 989 O VAL A 130 -27.839 -6.040 32.241 1.00 22.40 O ANISOU 989 O VAL A 130 2781 3718 2010 -306 342 317 O ATOM 990 CB VAL A 130 -29.490 -8.807 33.204 1.00 22.56 C ANISOU 990 CB VAL A 130 2859 3750 1963 -494 456 437 C ATOM 991 CG1 VAL A 130 -29.486 -7.853 34.382 1.00 21.57 C ANISOU 991 CG1 VAL A 130 2771 3673 1750 -460 499 410 C ATOM 992 CG2 VAL A 130 -30.869 -9.436 33.041 1.00 22.89 C ANISOU 992 CG2 VAL A 130 2835 3831 2030 -574 535 454 C ATOM 993 N LEU A 131 -26.645 -7.938 32.050 1.00 19.76 N ANISOU 993 N LEU A 131 2541 3284 1684 -348 259 398 N ATOM 994 CA LEU A 131 -25.372 -7.228 32.153 1.00 19.40 C ANISOU 994 CA LEU A 131 2520 3211 1642 -286 190 378 C ATOM 995 C LEU A 131 -25.137 -6.303 30.967 1.00 18.46 C ANISOU 995 C LEU A 131 2323 3090 1602 -239 170 331 C ATOM 996 O LEU A 131 -24.520 -5.243 31.123 1.00 19.59 O ANISOU 996 O LEU A 131 2462 3235 1745 -194 143 297 O ATOM 997 CB LEU A 131 -24.217 -8.220 32.270 1.00 16.51 C ANISOU 997 CB LEU A 131 2219 2774 1281 -283 116 423 C ATOM 998 CG LEU A 131 -24.205 -9.091 33.519 1.00 18.49 C ANISOU 998 CG LEU A 131 2572 3011 1445 -321 112 480 C ATOM 999 CD1 LEU A 131 -22.934 -9.927 33.564 1.00 20.50 C ANISOU 999 CD1 LEU A 131 2882 3188 1720 -296 20 520 C ATOM 1000 CD2 LEU A 131 -24.333 -8.231 34.760 1.00 17.96 C ANISOU 1000 CD2 LEU A 131 2550 2993 1282 -315 132 462 C ATOM 1001 N SER A 132 -25.609 -6.685 29.778 1.00 22.47 N ANISOU 1001 N SER A 132 2777 3590 2171 -252 181 329 N ATOM 1002 CA SER A 132 -25.426 -5.837 28.605 1.00 19.27 C ANISOU 1002 CA SER A 132 2313 3181 1827 -211 163 291 C ATOM 1003 C SER A 132 -26.210 -4.536 28.736 1.00 20.96 C ANISOU 1003 C SER A 132 2479 3448 2035 -185 199 249 C ATOM 1004 O SER A 132 -25.710 -3.464 28.374 1.00 23.65 O ANISOU 1004 O SER A 132 2806 3779 2400 -140 175 218 O ATOM 1005 CB SER A 132 -25.835 -6.598 27.345 1.00 15.36 C ANISOU 1005 CB SER A 132 1788 2666 1381 -236 162 299 C ATOM 1006 OG SER A 132 -25.041 -7.760 27.176 1.00 16.71 O ANISOU 1006 OG SER A 132 2009 2778 1563 -248 130 330 O ATOM 1007 N PHE A 133 -27.439 -4.609 29.256 1.00 18.67 N ANISOU 1007 N PHE A 133 2164 3211 1719 -213 259 246 N ATOM 1008 CA PHE A 133 -28.206 -3.394 29.511 1.00 20.88 C ANISOU 1008 CA PHE A 133 2399 3540 1996 -176 299 201 C ATOM 1009 C PHE A 133 -27.518 -2.517 30.552 1.00 21.84 C ANISOU 1009 C PHE A 133 2578 3657 2063 -140 291 176 C ATOM 1010 O PHE A 133 -27.388 -1.303 30.363 1.00 21.58 O ANISOU 1010 O PHE A 133 2530 3620 2051 -89 279 134 O ATOM 1011 CB PHE A 133 -29.625 -3.749 29.959 1.00 19.22 C ANISOU 1011 CB PHE A 133 2140 3391 1771 -215 376 204 C ATOM 1012 CG PHE A 133 -30.587 -3.956 28.822 1.00 24.69 C ANISOU 1012 CG PHE A 133 2742 4104 2536 -230 378 201 C ATOM 1013 CD1 PHE A 133 -31.321 -2.895 28.316 1.00 25.70 C ANISOU 1013 CD1 PHE A 133 2792 4265 2709 -180 385 159 C ATOM 1014 CD2 PHE A 133 -30.766 -5.211 28.263 1.00 25.11 C ANISOU 1014 CD2 PHE A 133 2793 4138 2611 -294 363 238 C ATOM 1015 CE1 PHE A 133 -32.212 -3.080 27.272 1.00 25.58 C ANISOU 1015 CE1 PHE A 133 2693 4269 2758 -192 370 158 C ATOM 1016 CE2 PHE A 133 -31.656 -5.402 27.216 1.00 24.88 C ANISOU 1016 CE2 PHE A 133 2684 4125 2643 -314 351 232 C ATOM 1017 CZ PHE A 133 -32.379 -4.334 26.720 1.00 24.78 C ANISOU 1017 CZ PHE A 133 2589 4152 2673 -263 350 193 C ATOM 1018 N ALA A 134 -27.052 -3.121 31.651 1.00 24.85 N ANISOU 1018 N ALA A 134 3035 4032 2374 -167 290 203 N ATOM 1019 CA ALA A 134 -26.397 -2.354 32.709 1.00 22.04 C ANISOU 1019 CA ALA A 134 2747 3671 1955 -139 271 177 C ATOM 1020 C ALA A 134 -25.118 -1.691 32.212 1.00 23.54 C ANISOU 1020 C ALA A 134 2944 3809 2190 -103 188 161 C ATOM 1021 O ALA A 134 -24.842 -0.532 32.545 1.00 23.27 O ANISOU 1021 O ALA A 134 2925 3770 2146 -67 173 116 O ATOM 1022 CB ALA A 134 -26.099 -3.262 33.902 1.00 17.01 C ANISOU 1022 CB ALA A 134 2202 3033 1228 -180 269 219 C ATOM 1023 N ILE A 135 -24.319 -2.414 31.426 1.00 21.58 N ANISOU 1023 N ILE A 135 2685 3519 1995 -113 138 196 N ATOM 1024 CA ILE A 135 -23.085 -1.845 30.892 1.00 16.04 C ANISOU 1024 CA ILE A 135 1975 2773 1347 -85 72 184 C ATOM 1025 C ILE A 135 -23.397 -0.772 29.859 1.00 20.31 C ANISOU 1025 C ILE A 135 2459 3312 1946 -55 86 149 C ATOM 1026 O ILE A 135 -22.869 0.345 29.917 1.00 14.37 O ANISOU 1026 O ILE A 135 1713 2539 1208 -30 59 116 O ATOM 1027 CB ILE A 135 -22.200 -2.949 30.287 1.00 17.65 C ANISOU 1027 CB ILE A 135 2176 2936 1596 -97 30 226 C ATOM 1028 CG1 ILE A 135 -21.626 -3.850 31.381 1.00 17.46 C ANISOU 1028 CG1 ILE A 135 2218 2896 1518 -113 -9 264 C ATOM 1029 CG2 ILE A 135 -21.099 -2.337 29.431 1.00 14.07 C ANISOU 1029 CG2 ILE A 135 1686 2445 1215 -71 -12 212 C ATOM 1030 CD1 ILE A 135 -20.851 -5.031 30.847 1.00 14.92 C ANISOU 1030 CD1 ILE A 135 1895 2528 1244 -115 -47 304 C ATOM 1031 N GLY A 136 -24.254 -1.103 28.889 1.00 22.67 N ANISOU 1031 N GLY A 136 2710 3626 2280 -61 120 157 N ATOM 1032 CA GLY A 136 -24.519 -0.188 27.794 1.00 19.39 C ANISOU 1032 CA GLY A 136 2250 3202 1916 -33 121 134 C ATOM 1033 C GLY A 136 -25.306 1.037 28.206 1.00 21.47 C ANISOU 1033 C GLY A 136 2503 3487 2167 3 148 90 C ATOM 1034 O GLY A 136 -25.135 2.111 27.619 1.00 21.97 O ANISOU 1034 O GLY A 136 2558 3523 2266 36 129 68 O ATOM 1035 N LEU A 137 -26.175 0.905 29.209 1.00 17.72 N ANISOU 1035 N LEU A 137 2034 3058 1641 0 196 77 N ATOM 1036 CA LEU A 137 -26.962 2.032 29.689 1.00 17.81 C ANISOU 1036 CA LEU A 137 2035 3092 1640 44 232 27 C ATOM 1037 C LEU A 137 -26.380 2.644 30.954 1.00 19.27 C ANISOU 1037 C LEU A 137 2295 3266 1762 55 225 -5 C ATOM 1038 O LEU A 137 -27.082 3.372 31.663 1.00 30.78 O ANISOU 1038 O LEU A 137 3762 4747 3186 88 270 -51 O ATOM 1039 CB LEU A 137 -28.419 1.617 29.916 1.00 21.01 C ANISOU 1039 CB LEU A 137 2384 3562 2036 37 305 24 C ATOM 1040 CG LEU A 137 -29.177 1.085 28.694 1.00 16.24 C ANISOU 1040 CG LEU A 137 1701 2974 1495 24 303 48 C ATOM 1041 CD1 LEU A 137 -30.621 0.798 29.053 1.00 18.20 C ANISOU 1041 CD1 LEU A 137 1878 3291 1744 15 375 39 C ATOM 1042 CD2 LEU A 137 -29.087 2.038 27.512 1.00 15.21 C ANISOU 1042 CD2 LEU A 137 1545 2807 1427 71 256 34 C ATOM 1043 N THR A 138 -25.112 2.359 31.251 1.00 15.49 N ANISOU 1043 N THR A 138 1867 2750 1267 31 165 14 N ATOM 1044 CA THR A 138 -24.448 3.026 32.368 1.00 22.40 C ANISOU 1044 CA THR A 138 2818 3608 2086 39 135 -20 C ATOM 1045 C THR A 138 -24.498 4.550 32.275 1.00 21.57 C ANISOU 1045 C THR A 138 2721 3470 2005 85 127 -79 C ATOM 1046 O THR A 138 -24.669 5.191 33.327 1.00 23.91 O ANISOU 1046 O THR A 138 3077 3770 2237 104 141 -128 O ATOM 1047 CB THR A 138 -23.000 2.526 32.488 1.00 21.81 C ANISOU 1047 CB THR A 138 2775 3495 2018 9 53 12 C ATOM 1048 OG1 THR A 138 -22.998 1.164 32.936 1.00 20.76 O ANISOU 1048 OG1 THR A 138 2662 3384 1841 -26 58 61 O ATOM 1049 CG2 THR A 138 -22.212 3.368 33.474 1.00 16.32 C ANISOU 1049 CG2 THR A 138 2149 2772 1279 14 -2 -28 C ATOM 1050 N PRO A 139 -24.364 5.190 31.103 1.00 21.38 N ANISOU 1050 N PRO A 139 2654 3408 2062 104 105 -79 N ATOM 1051 CA PRO A 139 -24.551 6.649 31.065 1.00 16.13 C ANISOU 1051 CA PRO A 139 2007 2703 1417 151 101 -133 C ATOM 1052 C PRO A 139 -25.878 7.110 31.625 1.00 16.83 C ANISOU 1052 C PRO A 139 2091 2829 1473 201 172 -181 C ATOM 1053 O PRO A 139 -25.951 8.196 32.212 1.00 22.83 O ANISOU 1053 O PRO A 139 2902 3559 2214 240 173 -240 O ATOM 1054 CB PRO A 139 -24.416 6.973 29.572 1.00 15.56 C ANISOU 1054 CB PRO A 139 1887 2593 1431 158 79 -105 C ATOM 1055 CG PRO A 139 -23.442 5.963 29.094 1.00 14.95 C ANISOU 1055 CG PRO A 139 1793 2514 1373 106 47 -52 C ATOM 1056 CD PRO A 139 -23.801 4.696 29.828 1.00 15.00 C ANISOU 1056 CD PRO A 139 1799 2577 1323 82 75 -31 C ATOM 1057 N MET A 140 -26.934 6.314 31.481 1.00 20.46 N ANISOU 1057 N MET A 140 2490 3353 1930 201 233 -160 N ATOM 1058 CA MET A 140 -28.214 6.691 32.062 1.00 18.25 C ANISOU 1058 CA MET A 140 2187 3119 1626 249 313 -206 C ATOM 1059 C MET A 140 -28.220 6.611 33.584 1.00 24.15 C ANISOU 1059 C MET A 140 3011 3896 2269 240 357 -242 C ATOM 1060 O MET A 140 -29.136 7.158 34.207 1.00 27.26 O ANISOU 1060 O MET A 140 3404 4321 2634 289 431 -296 O ATOM 1061 CB MET A 140 -29.325 5.819 31.482 1.00 18.46 C ANISOU 1061 CB MET A 140 2116 3211 1689 239 365 -172 C ATOM 1062 CG MET A 140 -29.431 5.919 29.968 1.00 23.72 C ANISOU 1062 CG MET A 140 2717 3851 2445 250 317 -142 C ATOM 1063 SD MET A 140 -30.914 5.116 29.343 1.00 25.16 S ANISOU 1063 SD MET A 140 2777 4108 2673 245 365 -118 S ATOM 1064 CE MET A 140 -32.167 6.260 29.910 1.00 25.86 C ANISOU 1064 CE MET A 140 2818 4227 2780 337 432 -190 C ATOM 1065 N LEU A 141 -27.228 5.961 34.195 1.00 22.28 N ANISOU 1065 N LEU A 141 2844 3651 1972 185 314 -213 N ATOM 1066 CA LEU A 141 -27.135 5.905 35.648 1.00 22.61 C ANISOU 1066 CA LEU A 141 2980 3714 1897 174 341 -243 C ATOM 1067 C LEU A 141 -26.445 7.124 36.240 1.00 26.29 C ANISOU 1067 C LEU A 141 3536 4121 2331 203 289 -309 C ATOM 1068 O LEU A 141 -26.292 7.191 37.464 1.00 28.26 O ANISOU 1068 O LEU A 141 3882 4381 2473 195 298 -343 O ATOM 1069 CB LEU A 141 -26.393 4.641 36.092 1.00 23.18 C ANISOU 1069 CB LEU A 141 3095 3798 1913 105 303 -179 C ATOM 1070 CG LEU A 141 -26.939 3.298 35.601 1.00 25.46 C ANISOU 1070 CG LEU A 141 3317 4132 2225 62 344 -110 C ATOM 1071 CD1 LEU A 141 -26.206 2.161 36.289 1.00 24.72 C ANISOU 1071 CD1 LEU A 141 3294 4038 2060 5 306 -54 C ATOM 1072 CD2 LEU A 141 -28.434 3.193 35.833 1.00 27.77 C ANISOU 1072 CD2 LEU A 141 3557 4494 2502 75 464 -127 C ATOM 1073 N GLY A 142 -26.023 8.078 35.414 1.00 19.29 N ANISOU 1073 N GLY A 142 2630 3168 1531 230 232 -328 N ATOM 1074 CA GLY A 142 -25.444 9.300 35.932 1.00 19.88 C ANISOU 1074 CA GLY A 142 2792 3177 1586 253 183 -395 C ATOM 1075 C GLY A 142 -24.152 9.703 35.253 1.00 19.30 C ANISOU 1075 C GLY A 142 2721 3028 1585 219 75 -374 C ATOM 1076 O GLY A 142 -23.727 10.858 35.351 1.00 19.95 O ANISOU 1076 O GLY A 142 2856 3039 1684 235 30 -425 O ATOM 1077 N TRP A 143 -23.509 8.761 34.563 1.00 18.43 N ANISOU 1077 N TRP A 143 2555 2928 1519 170 37 -300 N ATOM 1078 CA TRP A 143 -22.239 9.033 33.889 1.00 17.97 C ANISOU 1078 CA TRP A 143 2484 2808 1535 133 -51 -275 C ATOM 1079 C TRP A 143 -22.535 9.617 32.506 1.00 18.75 C ANISOU 1079 C TRP A 143 2520 2871 1732 158 -37 -259 C ATOM 1080 O TRP A 143 -22.415 8.961 31.470 1.00 21.26 O ANISOU 1080 O TRP A 143 2771 3202 2105 140 -34 -201 O ATOM 1081 CB TRP A 143 -21.398 7.764 33.808 1.00 25.37 C ANISOU 1081 CB TRP A 143 3392 3772 2476 80 -91 -208 C ATOM 1082 CG TRP A 143 -19.951 7.999 33.464 1.00 23.87 C ANISOU 1082 CG TRP A 143 3190 3528 2350 39 -182 -192 C ATOM 1083 CD1 TRP A 143 -19.365 9.189 33.132 1.00 21.09 C ANISOU 1083 CD1 TRP A 143 2849 3107 2056 32 -226 -222 C ATOM 1084 CD2 TRP A 143 -18.906 7.017 33.427 1.00 21.16 C ANISOU 1084 CD2 TRP A 143 2816 3194 2029 -2 -238 -140 C ATOM 1085 NE1 TRP A 143 -18.024 9.007 32.895 1.00 17.46 N ANISOU 1085 NE1 TRP A 143 2358 2621 1655 -18 -300 -193 N ATOM 1086 CE2 TRP A 143 -17.718 7.683 33.063 1.00 17.16 C ANISOU 1086 CE2 TRP A 143 2290 2632 1599 -33 -309 -144 C ATOM 1087 CE3 TRP A 143 -18.861 5.638 33.666 1.00 16.83 C ANISOU 1087 CE3 TRP A 143 2256 2691 1449 -15 -235 -90 C ATOM 1088 CZ2 TRP A 143 -16.500 7.020 32.932 1.00 17.10 C ANISOU 1088 CZ2 TRP A 143 2234 2621 1642 -69 -373 -104 C ATOM 1089 CZ3 TRP A 143 -17.650 4.979 33.534 1.00 16.75 C ANISOU 1089 CZ3 TRP A 143 2211 2668 1485 -44 -305 -50 C ATOM 1090 CH2 TRP A 143 -16.484 5.672 33.173 1.00 16.90 C ANISOU 1090 CH2 TRP A 143 2195 2639 1585 -67 -371 -60 C ATOM 1091 N ASN A 144 -22.939 10.888 32.506 1.00 18.04 N ANISOU 1091 N ASN A 144 2466 2730 1658 204 -31 -314 N ATOM 1092 CA ASN A 144 -23.345 11.563 31.280 1.00 23.69 C ANISOU 1092 CA ASN A 144 3141 3404 2455 237 -22 -301 C ATOM 1093 C ASN A 144 -23.011 13.047 31.389 1.00 21.74 C ANISOU 1093 C ASN A 144 2964 3060 2234 256 -62 -354 C ATOM 1094 O ASN A 144 -22.524 13.523 32.418 1.00 24.40 O ANISOU 1094 O ASN A 144 3378 3368 2526 243 -96 -407 O ATOM 1095 CB ASN A 144 -24.837 11.343 31.000 1.00 17.82 C ANISOU 1095 CB ASN A 144 2343 2715 1711 300 54 -304 C ATOM 1096 CG ASN A 144 -25.728 11.824 32.140 1.00 18.79 C ANISOU 1096 CG ASN A 144 2507 2859 1772 358 109 -379 C ATOM 1097 OD1 ASN A 144 -25.834 13.021 32.389 1.00 19.51 O ANISOU 1097 OD1 ASN A 144 2654 2886 1872 404 99 -439 O ATOM 1098 ND2 ASN A 144 -26.385 10.892 32.822 1.00 18.92 N ANISOU 1098 ND2 ASN A 144 2500 2961 1726 354 173 -377 N ATOM 1099 N ASN A 145 -23.283 13.785 30.311 1.00 18.59 N ANISOU 1099 N ASN A 145 2548 2607 1907 285 -65 -338 N ATOM 1100 CA ASN A 145 -23.070 15.227 30.277 1.00 23.77 C ANISOU 1100 CA ASN A 145 3277 3157 2598 306 -102 -381 C ATOM 1101 C ASN A 145 -24.375 16.013 30.337 1.00 27.37 C ANISOU 1101 C ASN A 145 3749 3595 3058 408 -60 -432 C ATOM 1102 O ASN A 145 -24.404 17.183 29.944 1.00 29.49 O ANISOU 1102 O ASN A 145 4067 3766 3374 441 -88 -452 O ATOM 1103 CB ASN A 145 -22.277 15.625 29.032 1.00 22.45 C ANISOU 1103 CB ASN A 145 3099 2921 2509 260 -144 -322 C ATOM 1104 CG ASN A 145 -20.871 15.075 29.041 1.00 26.61 C ANISOU 1104 CG ASN A 145 3608 3453 3048 164 -187 -285 C ATOM 1105 OD1 ASN A 145 -20.240 14.973 30.091 1.00 37.19 O ANISOU 1105 OD1 ASN A 145 4980 4800 4351 129 -221 -321 O ATOM 1106 ND2 ASN A 145 -20.376 14.702 27.871 1.00 29.84 N ANISOU 1106 ND2 ASN A 145 3966 3863 3509 123 -185 -215 N ATOM 1107 N CYS A 146 -25.455 15.399 30.829 1.00 27.83 N ANISOU 1107 N CYS A 146 3762 3740 3072 460 9 -453 N ATOM 1108 CA CYS A 146 -26.722 16.116 30.935 1.00 29.14 C ANISOU 1108 CA CYS A 146 3923 3897 3251 566 57 -506 C ATOM 1109 C CYS A 146 -26.628 17.285 31.908 1.00 35.95 C ANISOU 1109 C CYS A 146 4894 4680 4084 607 49 -600 C ATOM 1110 O CYS A 146 -27.308 18.303 31.723 1.00 37.05 O ANISOU 1110 O CYS A 146 5057 4756 4266 694 57 -643 O ATOM 1111 CB CYS A 146 -27.831 15.159 31.364 1.00 31.52 C ANISOU 1111 CB CYS A 146 4144 4317 3513 598 142 -511 C ATOM 1112 SG CYS A 146 -28.143 13.833 30.188 1.00 37.20 S ANISOU 1112 SG CYS A 146 4742 5120 4272 558 149 -413 S ATOM 1113 N GLY A 147 -25.791 17.163 32.941 1.00 37.34 N ANISOU 1113 N GLY A 147 5144 4855 4189 548 26 -634 N ATOM 1114 CA GLY A 147 -25.606 18.252 33.884 1.00 40.82 C ANISOU 1114 CA GLY A 147 5704 5214 4592 575 7 -728 C ATOM 1115 C GLY A 147 -24.996 19.500 33.282 1.00 44.76 C ANISOU 1115 C GLY A 147 6269 5572 5166 569 -69 -736 C ATOM 1116 O GLY A 147 -25.229 20.599 33.798 1.00 45.67 O ANISOU 1116 O GLY A 147 6477 5601 5275 626 -74 -819 O ATOM 1117 N GLN A 148 -24.230 19.363 32.197 1.00 48.08 N ANISOU 1117 N GLN A 148 6648 5962 5656 500 -123 -652 N ATOM 1118 CA GLN A 148 -23.603 20.497 31.520 1.00 49.57 C ANISOU 1118 CA GLN A 148 6898 6017 5920 477 -189 -642 C ATOM 1119 C GLN A 148 -24.062 20.546 30.066 1.00 38.23 C ANISOU 1119 C GLN A 148 5399 4567 4561 507 -182 -564 C ATOM 1120 O GLN A 148 -23.282 20.256 29.150 1.00 34.93 O ANISOU 1120 O GLN A 148 4948 4140 4184 430 -212 -484 O ATOM 1121 CB GLN A 148 -22.079 20.424 31.594 1.00 57.77 C ANISOU 1121 CB GLN A 148 7961 7020 6969 351 -264 -615 C ATOM 1122 CG GLN A 148 -21.519 20.108 32.971 1.00 66.18 C ANISOU 1122 CG GLN A 148 9075 8120 7950 308 -290 -675 C ATOM 1123 CD GLN A 148 -21.420 18.617 33.225 1.00 68.16 C ANISOU 1123 CD GLN A 148 9243 8505 8147 275 -263 -629 C ATOM 1124 OE1 GLN A 148 -21.536 17.811 32.301 1.00 68.74 O ANISOU 1124 OE1 GLN A 148 9221 8639 8260 265 -234 -549 O ATOM 1125 NE2 GLN A 148 -21.212 18.242 34.482 1.00 69.79 N ANISOU 1125 NE2 GLN A 148 9499 8755 8261 258 -275 -678 N ATOM 1126 N PRO A 149 -25.315 20.926 29.819 1.00 35.91 N ANISOU 1126 N PRO A 149 5088 4269 4288 621 -142 -585 N ATOM 1127 CA PRO A 149 -25.823 20.930 28.444 1.00 30.06 C ANISOU 1127 CA PRO A 149 4291 3519 3611 655 -148 -509 C ATOM 1128 C PRO A 149 -25.294 22.107 27.639 1.00 32.50 C ANISOU 1128 C PRO A 149 4684 3680 3983 639 -212 -480 C ATOM 1129 O PRO A 149 -25.177 23.230 28.137 1.00 34.50 O ANISOU 1129 O PRO A 149 5039 3820 4249 666 -240 -543 O ATOM 1130 CB PRO A 149 -27.340 21.033 28.636 1.00 29.22 C ANISOU 1130 CB PRO A 149 4136 3455 3510 788 -95 -555 C ATOM 1131 CG PRO A 149 -27.488 21.795 29.906 1.00 28.85 C ANISOU 1131 CG PRO A 149 4175 3361 3427 840 -75 -665 C ATOM 1132 CD PRO A 149 -26.344 21.357 30.783 1.00 33.77 C ANISOU 1132 CD PRO A 149 4845 4005 3981 729 -90 -682 C ATOM 1133 N LYS A 150 -24.972 21.833 26.375 1.00 34.91 N ANISOU 1133 N LYS A 150 4958 3984 4324 591 -232 -384 N ATOM 1134 CA LYS A 150 -24.598 22.885 25.440 1.00 36.24 C ANISOU 1134 CA LYS A 150 5205 4016 4548 577 -283 -338 C ATOM 1135 C LYS A 150 -25.806 23.767 25.155 1.00 42.36 C ANISOU 1135 C LYS A 150 6013 4723 5360 713 -295 -361 C ATOM 1136 O LYS A 150 -26.568 23.508 24.218 1.00 40.81 O ANISOU 1136 O LYS A 150 5764 4560 5182 768 -297 -306 O ATOM 1137 CB LYS A 150 -24.039 22.291 24.144 1.00 37.88 C ANISOU 1137 CB LYS A 150 5373 4251 4768 498 -288 -230 C ATOM 1138 CG LYS A 150 -22.747 21.505 24.328 1.00 38.02 C ANISOU 1138 CG LYS A 150 5355 4322 4767 368 -279 -204 C ATOM 1139 CD LYS A 150 -22.104 21.183 22.994 1.00 42.57 C ANISOU 1139 CD LYS A 150 5914 4897 5362 293 -276 -104 C ATOM 1140 CE LYS A 150 -20.869 20.310 23.169 1.00 44.66 C ANISOU 1140 CE LYS A 150 6123 5227 5620 179 -259 -83 C ATOM 1141 NZ LYS A 150 -19.837 20.954 24.017 1.00 49.13 N ANISOU 1141 NZ LYS A 150 6735 5723 6209 106 -293 -127 N ATOM 1142 N GLU A 151 -25.980 24.814 25.966 1.00 54.57 N ANISOU 1142 N GLU A 151 7648 6169 6917 772 -308 -446 N ATOM 1143 CA GLU A 151 -27.172 25.647 25.871 1.00 56.85 C ANISOU 1143 CA GLU A 151 7961 6393 7247 921 -315 -485 C ATOM 1144 C GLU A 151 -27.178 26.493 24.606 1.00 51.00 C ANISOU 1144 C GLU A 151 7287 5525 6564 938 -378 -406 C ATOM 1145 O GLU A 151 -28.250 26.837 24.099 1.00 52.60 O ANISOU 1145 O GLU A 151 7472 5707 6806 1060 -394 -397 O ATOM 1146 CB GLU A 151 -27.279 26.540 27.105 1.00 66.18 C ANISOU 1146 CB GLU A 151 9233 7493 8420 979 -308 -605 C ATOM 1147 CG GLU A 151 -28.660 26.573 27.729 1.00 76.20 C ANISOU 1147 CG GLU A 151 10449 8815 9688 1135 -251 -687 C ATOM 1148 CD GLU A 151 -29.131 25.202 28.179 1.00 79.90 C ANISOU 1148 CD GLU A 151 10781 9475 10103 1127 -175 -692 C ATOM 1149 OE1 GLU A 151 -29.651 24.437 27.337 1.00 81.62 O ANISOU 1149 OE1 GLU A 151 10888 9783 10340 1136 -168 -618 O ATOM 1150 OE2 GLU A 151 -28.978 24.888 29.379 1.00 82.57 O ANISOU 1150 OE2 GLU A 151 11130 9868 10374 1108 -125 -767 O ATOM 1151 N GLY A 152 -26.002 26.843 24.086 1.00 47.94 N ANISOU 1151 N GLY A 152 6977 5052 6186 816 -416 -346 N ATOM 1152 CA GLY A 152 -25.958 27.590 22.842 1.00 46.05 C ANISOU 1152 CA GLY A 152 6814 4694 5990 817 -469 -258 C ATOM 1153 C GLY A 152 -26.454 26.775 21.665 1.00 41.63 C ANISOU 1153 C GLY A 152 6171 4229 5418 830 -468 -164 C ATOM 1154 O GLY A 152 -27.217 27.272 20.831 1.00 38.51 O ANISOU 1154 O GLY A 152 5805 3775 5052 919 -512 -120 O ATOM 1155 N LYS A 153 -26.039 25.509 21.585 1.00 39.08 N ANISOU 1155 N LYS A 153 5748 4048 5051 746 -424 -134 N ATOM 1156 CA LYS A 153 -26.497 24.652 20.497 1.00 36.34 C ANISOU 1156 CA LYS A 153 5329 3795 4686 753 -423 -54 C ATOM 1157 C LYS A 153 -27.982 24.338 20.623 1.00 38.63 C ANISOU 1157 C LYS A 153 5528 4163 4987 893 -423 -90 C ATOM 1158 O LYS A 153 -28.667 24.172 19.606 1.00 40.78 O ANISOU 1158 O LYS A 153 5775 4453 5265 941 -459 -29 O ATOM 1159 CB LYS A 153 -25.672 23.366 20.466 1.00 31.21 C ANISOU 1159 CB LYS A 153 4599 3269 3990 634 -374 -25 C ATOM 1160 CG LYS A 153 -25.935 22.484 19.266 1.00 32.04 C ANISOU 1160 CG LYS A 153 4652 3455 4068 618 -373 58 C ATOM 1161 CD LYS A 153 -25.015 21.274 19.259 1.00 34.53 C ANISOU 1161 CD LYS A 153 4902 3874 4345 504 -322 81 C ATOM 1162 CE LYS A 153 -23.552 21.688 19.279 1.00 33.78 C ANISOU 1162 CE LYS A 153 4869 3707 4260 384 -311 103 C ATOM 1163 NZ LYS A 153 -22.640 20.508 19.186 1.00 34.62 N ANISOU 1163 NZ LYS A 153 4903 3912 4340 284 -263 128 N ATOM 1164 N ALA A 154 -28.499 24.269 21.854 1.00 35.29 N ANISOU 1164 N ALA A 154 5056 3787 4567 957 -383 -189 N ATOM 1165 CA ALA A 154 -29.914 23.964 22.047 1.00 36.99 C ANISOU 1165 CA ALA A 154 5168 4085 4803 1085 -368 -229 C ATOM 1166 C ALA A 154 -30.795 25.125 21.607 1.00 42.94 C ANISOU 1166 C ALA A 154 5971 4724 5621 1223 -428 -232 C ATOM 1167 O ALA A 154 -31.823 24.919 20.952 1.00 43.59 O ANISOU 1167 O ALA A 154 5977 4851 5733 1309 -459 -203 O ATOM 1168 CB ALA A 154 -30.180 23.609 23.510 1.00 25.56 C ANISOU 1168 CB ALA A 154 3664 2716 3331 1111 -293 -333 C ATOM 1169 N HIS A 155 -30.411 26.354 21.961 1.00 46.32 N ANISOU 1169 N HIS A 155 6527 4997 6075 1246 -454 -269 N ATOM 1170 CA HIS A 155 -31.194 27.518 21.562 1.00 50.05 C ANISOU 1170 CA HIS A 155 7063 5340 6615 1383 -518 -272 C ATOM 1171 C HIS A 155 -31.094 27.780 20.068 1.00 48.97 C ANISOU 1171 C HIS A 155 6987 5133 6487 1364 -601 -150 C ATOM 1172 O HIS A 155 -32.062 28.243 19.456 1.00 50.56 O ANISOU 1172 O HIS A 155 7183 5292 6737 1489 -664 -126 O ATOM 1173 CB HIS A 155 -30.745 28.747 22.349 1.00 57.43 C ANISOU 1173 CB HIS A 155 8136 6115 7571 1404 -525 -346 C ATOM 1174 CG HIS A 155 -31.089 28.681 23.802 1.00 63.63 C ANISOU 1174 CG HIS A 155 8880 6952 8343 1460 -450 -477 C ATOM 1175 ND1 HIS A 155 -32.375 28.467 24.248 1.00 66.44 N ANISOU 1175 ND1 HIS A 155 9123 7394 8727 1603 -408 -542 N ATOM 1176 CD2 HIS A 155 -30.319 28.795 24.909 1.00 65.16 C ANISOU 1176 CD2 HIS A 155 9135 7129 8495 1390 -410 -554 C ATOM 1177 CE1 HIS A 155 -32.383 28.453 25.569 1.00 69.06 C ANISOU 1177 CE1 HIS A 155 9456 7759 9027 1619 -333 -654 C ATOM 1178 NE2 HIS A 155 -31.148 28.647 25.995 1.00 66.86 N ANISOU 1178 NE2 HIS A 155 9287 7416 8700 1492 -340 -664 N ATOM 1179 N SER A 156 -29.943 27.487 19.462 1.00 52.20 N ANISOU 1179 N SER A 156 7454 5531 6849 1212 -601 -71 N ATOM 1180 CA SER A 156 -29.793 27.691 18.028 1.00 54.33 C ANISOU 1180 CA SER A 156 7794 5739 7108 1182 -667 48 C ATOM 1181 C SER A 156 -30.690 26.764 17.217 1.00 53.98 C ANISOU 1181 C SER A 156 7639 5823 7048 1228 -691 97 C ATOM 1182 O SER A 156 -30.926 27.031 16.035 1.00 60.08 O ANISOU 1182 O SER A 156 8471 6543 7814 1248 -764 186 O ATOM 1183 CB SER A 156 -28.333 27.497 17.620 1.00 58.46 C ANISOU 1183 CB SER A 156 8390 6239 7584 1002 -640 114 C ATOM 1184 OG SER A 156 -27.889 26.193 17.946 1.00 65.06 O ANISOU 1184 OG SER A 156 9112 7235 8373 912 -570 101 O ATOM 1185 N GLN A 157 -31.193 25.689 17.820 1.00 50.05 N ANISOU 1185 N GLN A 157 6989 5487 6541 1241 -636 42 N ATOM 1186 CA GLN A 157 -32.106 24.776 17.147 1.00 49.58 C ANISOU 1186 CA GLN A 157 6812 5551 6474 1280 -661 77 C ATOM 1187 C GLN A 157 -33.528 24.863 17.688 1.00 48.33 C ANISOU 1187 C GLN A 157 6536 5444 6385 1438 -670 6 C ATOM 1188 O GLN A 157 -34.354 23.998 17.378 1.00 47.83 O ANISOU 1188 O GLN A 157 6343 5503 6326 1466 -680 15 O ATOM 1189 CB GLN A 157 -31.591 23.342 17.252 1.00 53.85 C ANISOU 1189 CB GLN A 157 7266 6243 6954 1158 -592 85 C ATOM 1190 CG GLN A 157 -30.242 23.127 16.597 1.00 60.05 C ANISOU 1190 CG GLN A 157 8143 6996 7678 1010 -577 158 C ATOM 1191 CD GLN A 157 -29.821 21.677 16.641 1.00 66.49 C ANISOU 1191 CD GLN A 157 8867 7955 8440 910 -516 164 C ATOM 1192 OE1 GLN A 157 -30.630 20.798 16.938 1.00 69.40 O ANISOU 1192 OE1 GLN A 157 9113 8444 8813 946 -499 131 O ATOM 1193 NE2 GLN A 157 -28.549 21.415 16.353 1.00 67.59 N ANISOU 1193 NE2 GLN A 157 9063 8080 8536 782 -480 206 N ATOM 1194 N GLY A 158 -33.835 25.884 18.484 1.00 48.43 N ANISOU 1194 N GLY A 158 6585 5363 6453 1540 -664 -69 N ATOM 1195 CA GLY A 158 -35.187 26.070 18.967 1.00 46.59 C ANISOU 1195 CA GLY A 158 6238 5170 6295 1702 -665 -140 C ATOM 1196 C GLY A 158 -35.656 25.036 19.959 1.00 51.55 C ANISOU 1196 C GLY A 158 6705 5967 6915 1696 -563 -217 C ATOM 1197 O GLY A 158 -36.865 24.862 20.130 1.00 61.56 O ANISOU 1197 O GLY A 158 7836 7310 8243 1809 -559 -256 O ATOM 1198 N CYS A 159 -34.734 24.341 20.621 1.00 46.16 N ANISOU 1198 N CYS A 159 6032 5346 6162 1565 -483 -236 N ATOM 1199 CA CYS A 159 -35.123 23.333 21.595 1.00 41.85 C ANISOU 1199 CA CYS A 159 5352 4954 5596 1548 -384 -301 C ATOM 1200 C CYS A 159 -35.807 23.988 22.785 1.00 42.90 C ANISOU 1200 C CYS A 159 5458 5071 5770 1671 -321 -415 C ATOM 1201 O CYS A 159 -35.447 25.091 23.201 1.00 44.23 O ANISOU 1201 O CYS A 159 5749 5106 5951 1715 -330 -461 O ATOM 1202 CB CYS A 159 -33.908 22.535 22.068 1.00 41.32 C ANISOU 1202 CB CYS A 159 5321 4936 5443 1388 -324 -294 C ATOM 1203 SG CYS A 159 -32.999 21.665 20.764 1.00 44.84 S ANISOU 1203 SG CYS A 159 5794 5408 5835 1241 -371 -172 S ATOM 1204 N GLY A 160 -36.803 23.302 23.328 1.00 44.13 N ANISOU 1204 N GLY A 160 5457 5363 5948 1723 -252 -464 N ATOM 1205 CA GLY A 160 -37.518 23.800 24.479 1.00 49.27 C ANISOU 1205 CA GLY A 160 6068 6021 6631 1839 -170 -577 C ATOM 1206 C GLY A 160 -36.678 23.717 25.737 1.00 52.97 C ANISOU 1206 C GLY A 160 6620 6491 7014 1763 -79 -647 C ATOM 1207 O GLY A 160 -35.569 23.183 25.762 1.00 51.93 O ANISOU 1207 O GLY A 160 6556 6369 6807 1619 -81 -607 O ATOM 1208 N GLU A 161 -37.235 24.264 26.812 1.00 61.82 N ANISOU 1208 N GLU A 161 7736 7604 8147 1867 0 -757 N ATOM 1209 CA GLU A 161 -36.573 24.202 28.104 1.00 64.46 C ANISOU 1209 CA GLU A 161 8154 7947 8390 1807 87 -834 C ATOM 1210 C GLU A 161 -36.479 22.762 28.585 1.00 56.38 C ANISOU 1210 C GLU A 161 7038 7093 7292 1693 167 -816 C ATOM 1211 O GLU A 161 -37.435 21.988 28.478 1.00 55.58 O ANISOU 1211 O GLU A 161 6778 7119 7222 1719 214 -804 O ATOM 1212 CB GLU A 161 -37.320 25.054 29.127 1.00 77.87 C ANISOU 1212 CB GLU A 161 9866 9611 10112 1954 165 -962 C ATOM 1213 CG GLU A 161 -37.132 26.544 28.926 1.00 91.03 C ANISOU 1213 CG GLU A 161 11676 11081 11832 2050 91 -998 C ATOM 1214 CD GLU A 161 -35.681 26.966 29.063 1.00 99.72 C ANISOU 1214 CD GLU A 161 12964 12061 12863 1927 35 -985 C ATOM 1215 OE1 GLU A 161 -34.934 26.308 29.819 1.00101.73 O ANISOU 1215 OE1 GLU A 161 13250 12381 13020 1806 84 -1001 O ATOM 1216 OE2 GLU A 161 -35.285 27.955 28.410 1.00103.23 O ANISOU 1216 OE2 GLU A 161 13524 12344 13356 1948 -62 -956 O ATOM 1217 N GLY A 162 -35.313 22.403 29.116 1.00 49.82 N ANISOU 1217 N GLY A 162 6307 6257 6367 1564 175 -811 N ATOM 1218 CA GLY A 162 -35.053 21.051 29.552 1.00 48.07 C ANISOU 1218 CA GLY A 162 6023 6173 6068 1449 235 -784 C ATOM 1219 C GLY A 162 -34.585 20.115 28.466 1.00 43.88 C ANISOU 1219 C GLY A 162 5444 5686 5540 1340 172 -669 C ATOM 1220 O GLY A 162 -34.241 18.964 28.770 1.00 43.66 O ANISOU 1220 O GLY A 162 5380 5758 5451 1237 210 -640 O ATOM 1221 N GLN A 163 -34.558 20.564 27.216 1.00 40.85 N ANISOU 1221 N GLN A 163 5070 5228 5223 1361 76 -604 N ATOM 1222 CA GLN A 163 -34.132 19.757 26.083 1.00 37.59 C ANISOU 1222 CA GLN A 163 4626 4848 4809 1266 15 -499 C ATOM 1223 C GLN A 163 -32.728 20.149 25.639 1.00 34.47 C ANISOU 1223 C GLN A 163 4367 4346 4385 1173 -51 -452 C ATOM 1224 O GLN A 163 -32.237 21.244 25.930 1.00 42.13 O ANISOU 1224 O GLN A 163 5452 5195 5362 1197 -76 -489 O ATOM 1225 CB GLN A 163 -35.104 19.913 24.912 1.00 38.50 C ANISOU 1225 CB GLN A 163 4659 4963 5006 1347 -49 -451 C ATOM 1226 CG GLN A 163 -36.470 19.300 25.135 1.00 40.89 C ANISOU 1226 CG GLN A 163 4792 5392 5352 1414 6 -479 C ATOM 1227 CD GLN A 163 -37.349 19.410 23.907 1.00 44.53 C ANISOU 1227 CD GLN A 163 5170 5853 5895 1484 -82 -426 C ATOM 1228 OE1 GLN A 163 -37.086 20.214 23.011 1.00 44.13 O ANISOU 1228 OE1 GLN A 163 5206 5691 5873 1517 -179 -382 O ATOM 1229 NE2 GLN A 163 -38.397 18.597 23.855 1.00 52.02 N ANISOU 1229 NE2 GLN A 163 5956 6927 6883 1501 -53 -426 N ATOM 1230 N VAL A 164 -32.081 19.230 24.924 1.00 25.30 N ANISOU 1230 N VAL A 164 3188 3229 3195 1064 -75 -372 N ATOM 1231 CA VAL A 164 -30.789 19.481 24.303 1.00 24.74 C ANISOU 1231 CA VAL A 164 3219 3073 3107 971 -129 -315 C ATOM 1232 C VAL A 164 -30.860 19.044 22.848 1.00 26.06 C ANISOU 1232 C VAL A 164 3358 3253 3292 943 -183 -220 C ATOM 1233 O VAL A 164 -31.777 18.333 22.429 1.00 25.81 O ANISOU 1233 O VAL A 164 3223 3310 3274 973 -181 -201 O ATOM 1234 CB VAL A 164 -29.631 18.748 25.016 1.00 21.70 C ANISOU 1234 CB VAL A 164 2859 2728 2657 850 -96 -318 C ATOM 1235 CG1 VAL A 164 -29.555 19.159 26.472 1.00 22.45 C ANISOU 1235 CG1 VAL A 164 3000 2812 2719 873 -51 -412 C ATOM 1236 CG2 VAL A 164 -29.790 17.249 24.884 1.00 20.72 C ANISOU 1236 CG2 VAL A 164 2635 2736 2502 792 -60 -280 C ATOM 1237 N ALA A 165 -29.879 19.492 22.070 1.00 24.83 N ANISOU 1237 N ALA A 165 3297 3007 3132 880 -231 -163 N ATOM 1238 CA ALA A 165 -29.656 18.915 20.750 1.00 27.14 C ANISOU 1238 CA ALA A 165 3581 3318 3412 824 -267 -73 C ATOM 1239 C ALA A 165 -29.082 17.522 20.945 1.00 31.42 C ANISOU 1239 C ALA A 165 4065 3969 3906 724 -219 -58 C ATOM 1240 O ALA A 165 -27.996 17.360 21.512 1.00 33.00 O ANISOU 1240 O ALA A 165 4299 4159 4080 644 -191 -68 O ATOM 1241 CB ALA A 165 -28.718 19.789 19.924 1.00 22.55 C ANISOU 1241 CB ALA A 165 3124 2611 2834 777 -313 -15 C ATOM 1242 N CYS A 166 -29.821 16.512 20.511 1.00 31.81 N ANISOU 1242 N CYS A 166 4023 4116 3948 729 -214 -36 N ATOM 1243 CA CYS A 166 -29.436 15.128 20.777 1.00 31.83 C ANISOU 1243 CA CYS A 166 3967 4219 3909 645 -168 -28 C ATOM 1244 C CYS A 166 -28.283 14.743 19.858 1.00 28.07 C ANISOU 1244 C CYS A 166 3544 3717 3403 551 -180 38 C ATOM 1245 O CYS A 166 -28.486 14.365 18.701 1.00 23.59 O ANISOU 1245 O CYS A 166 2975 3161 2825 540 -211 91 O ATOM 1246 CB CYS A 166 -30.625 14.197 20.595 1.00 35.98 C ANISOU 1246 CB CYS A 166 4382 4847 4442 675 -162 -27 C ATOM 1247 SG CYS A 166 -30.288 12.516 21.129 1.00 41.73 S ANISOU 1247 SG CYS A 166 5046 5686 5124 580 -102 -25 S ATOM 1248 N LEU A 167 -27.060 14.849 20.380 1.00 24.20 N ANISOU 1248 N LEU A 167 3101 3193 2900 484 -156 30 N ATOM 1249 CA LEU A 167 -25.845 14.448 19.686 1.00 24.71 C ANISOU 1249 CA LEU A 167 3200 3243 2946 392 -150 83 C ATOM 1250 C LEU A 167 -25.050 13.521 20.595 1.00 28.82 C ANISOU 1250 C LEU A 167 3682 3821 3447 328 -108 60 C ATOM 1251 O LEU A 167 -24.916 13.785 21.794 1.00 33.77 O ANISOU 1251 O LEU A 167 4311 4446 4074 335 -98 8 O ATOM 1252 CB LEU A 167 -24.996 15.664 19.296 1.00 25.80 C ANISOU 1252 CB LEU A 167 3433 3264 3105 367 -172 106 C ATOM 1253 CG LEU A 167 -25.598 16.610 18.250 1.00 25.15 C ANISOU 1253 CG LEU A 167 3414 3105 3035 421 -221 147 C ATOM 1254 CD1 LEU A 167 -24.657 17.767 17.971 1.00 30.26 C ANISOU 1254 CD1 LEU A 167 4164 3630 3702 378 -235 173 C ATOM 1255 CD2 LEU A 167 -25.920 15.858 16.967 1.00 22.48 C ANISOU 1255 CD2 LEU A 167 3065 2812 2664 409 -233 207 C ATOM 1256 N PHE A 168 -24.532 12.434 20.015 1.00 27.19 N ANISOU 1256 N PHE A 168 3448 3662 3219 269 -89 99 N ATOM 1257 CA PHE A 168 -23.869 11.390 20.795 1.00 22.06 C ANISOU 1257 CA PHE A 168 2758 3071 2555 219 -58 85 C ATOM 1258 C PHE A 168 -22.722 11.956 21.623 1.00 23.27 C ANISOU 1258 C PHE A 168 2942 3177 2724 178 -62 62 C ATOM 1259 O PHE A 168 -22.683 11.796 22.848 1.00 24.80 O ANISOU 1259 O PHE A 168 3123 3396 2904 181 -59 18 O ATOM 1260 CB PHE A 168 -23.358 10.293 19.861 1.00 19.12 C ANISOU 1260 CB PHE A 168 2366 2733 2167 168 -39 131 C ATOM 1261 CG PHE A 168 -22.811 9.081 20.569 1.00 14.24 C ANISOU 1261 CG PHE A 168 1703 2171 1536 129 -14 121 C ATOM 1262 CD1 PHE A 168 -21.501 9.056 21.034 1.00 14.17 C ANISOU 1262 CD1 PHE A 168 1697 2142 1544 81 -9 120 C ATOM 1263 CD2 PHE A 168 -23.599 7.951 20.742 1.00 17.44 C ANISOU 1263 CD2 PHE A 168 2063 2646 1917 138 -1 117 C ATOM 1264 CE1 PHE A 168 -20.994 7.935 21.682 1.00 16.65 C ANISOU 1264 CE1 PHE A 168 1974 2503 1849 54 3 116 C ATOM 1265 CE2 PHE A 168 -23.098 6.819 21.385 1.00 17.09 C ANISOU 1265 CE2 PHE A 168 1990 2642 1860 104 17 115 C ATOM 1266 CZ PHE A 168 -21.793 6.812 21.855 1.00 13.48 C ANISOU 1266 CZ PHE A 168 1542 2163 1418 67 16 115 C ATOM 1267 N GLU A 169 -21.768 12.618 20.968 1.00 22.36 N ANISOU 1267 N GLU A 169 2868 2993 2634 134 -70 93 N ATOM 1268 CA GLU A 169 -20.594 13.088 21.693 1.00 23.56 C ANISOU 1268 CA GLU A 169 3037 3104 2813 82 -81 73 C ATOM 1269 C GLU A 169 -20.898 14.264 22.608 1.00 26.35 C ANISOU 1269 C GLU A 169 3441 3395 3174 116 -113 19 C ATOM 1270 O GLU A 169 -20.027 14.658 23.390 1.00 29.85 O ANISOU 1270 O GLU A 169 3902 3805 3633 73 -134 -9 O ATOM 1271 CB GLU A 169 -19.482 13.443 20.710 1.00 24.71 C ANISOU 1271 CB GLU A 169 3202 3196 2991 14 -70 124 C ATOM 1272 CG GLU A 169 -19.038 12.244 19.891 1.00 28.55 C ANISOU 1272 CG GLU A 169 3641 3740 3466 -19 -29 166 C ATOM 1273 CD GLU A 169 -17.755 12.485 19.129 1.00 35.38 C ANISOU 1273 CD GLU A 169 4509 4566 4367 -93 0 207 C ATOM 1274 OE1 GLU A 169 -17.045 13.468 19.438 1.00 37.29 O ANISOU 1274 OE1 GLU A 169 4774 4742 4651 -134 -17 201 O ATOM 1275 OE2 GLU A 169 -17.459 11.683 18.218 1.00 34.33 O ANISOU 1275 OE2 GLU A 169 4355 4469 4221 -112 44 243 O ATOM 1276 N ASP A 170 -22.111 14.812 22.542 1.00 32.05 N ANISOU 1276 N ASP A 170 4186 4102 3888 195 -119 0 N ATOM 1277 CA ASP A 170 -22.515 15.846 23.483 1.00 29.12 C ANISOU 1277 CA ASP A 170 3864 3677 3522 244 -140 -64 C ATOM 1278 C ASP A 170 -23.054 15.259 24.781 1.00 25.27 C ANISOU 1278 C ASP A 170 3344 3265 2992 277 -119 -124 C ATOM 1279 O ASP A 170 -22.898 15.873 25.840 1.00 30.48 O ANISOU 1279 O ASP A 170 4051 3891 3641 286 -133 -184 O ATOM 1280 CB ASP A 170 -23.572 16.755 22.849 1.00 27.83 C ANISOU 1280 CB ASP A 170 3737 3458 3378 327 -156 -60 C ATOM 1281 CG ASP A 170 -22.989 17.730 21.843 1.00 30.44 C ANISOU 1281 CG ASP A 170 4141 3681 3744 295 -185 -11 C ATOM 1282 OD1 ASP A 170 -21.763 17.710 21.630 1.00 32.48 O ANISOU 1282 OD1 ASP A 170 4412 3912 4015 203 -183 19 O ATOM 1283 OD2 ASP A 170 -23.762 18.523 21.266 1.00 34.42 O ANISOU 1283 OD2 ASP A 170 4689 4125 4266 362 -211 1 O ATOM 1284 N VAL A 171 -23.676 14.082 24.734 1.00 16.97 N ANISOU 1284 N VAL A 171 2224 2311 1913 290 -86 -109 N ATOM 1285 CA VAL A 171 -24.364 13.565 25.913 1.00 22.59 C ANISOU 1285 CA VAL A 171 2909 3094 2580 323 -54 -159 C ATOM 1286 C VAL A 171 -23.604 12.389 26.520 1.00 24.25 C ANISOU 1286 C VAL A 171 3094 3366 2754 257 -46 -147 C ATOM 1287 O VAL A 171 -23.619 12.186 27.742 1.00 18.05 O ANISOU 1287 O VAL A 171 2326 2611 1921 258 -36 -190 O ATOM 1288 CB VAL A 171 -25.813 13.178 25.568 1.00 23.77 C ANISOU 1288 CB VAL A 171 2997 3304 2730 390 -22 -157 C ATOM 1289 CG1 VAL A 171 -26.615 14.428 25.197 1.00 23.92 C ANISOU 1289 CG1 VAL A 171 3042 3257 2788 474 -39 -180 C ATOM 1290 CG2 VAL A 171 -25.852 12.172 24.442 1.00 18.45 C ANISOU 1290 CG2 VAL A 171 2269 2675 2064 356 -21 -91 C ATOM 1291 N VAL A 172 -22.926 11.615 25.683 1.00 15.85 N ANISOU 1291 N VAL A 172 1997 2318 1707 204 -51 -88 N ATOM 1292 CA VAL A 172 -22.156 10.459 26.134 1.00 19.52 C ANISOU 1292 CA VAL A 172 2435 2833 2150 150 -50 -70 C ATOM 1293 C VAL A 172 -20.729 10.915 26.397 1.00 22.11 C ANISOU 1293 C VAL A 172 2791 3107 2504 94 -93 -73 C ATOM 1294 O VAL A 172 -20.073 11.415 25.471 1.00 31.69 O ANISOU 1294 O VAL A 172 4007 4268 3767 65 -103 -42 O ATOM 1295 CB VAL A 172 -22.180 9.327 25.103 1.00 21.43 C ANISOU 1295 CB VAL A 172 2624 3116 2401 128 -29 -14 C ATOM 1296 CG1 VAL A 172 -21.369 8.145 25.604 1.00 14.38 C ANISOU 1296 CG1 VAL A 172 1709 2263 1493 83 -32 2 C ATOM 1297 CG2 VAL A 172 -23.614 8.910 24.800 1.00 18.38 C ANISOU 1297 CG2 VAL A 172 2204 2781 1999 174 2 -13 C ATOM 1298 N PRO A 173 -20.209 10.763 27.615 1.00 28.73 N ANISOU 1298 N PRO A 173 3649 3956 3311 73 -120 -105 N ATOM 1299 CA PRO A 173 -18.846 11.221 27.898 1.00 20.97 C ANISOU 1299 CA PRO A 173 2681 2923 2362 16 -175 -110 C ATOM 1300 C PRO A 173 -17.820 10.364 27.176 1.00 15.76 C ANISOU 1300 C PRO A 173 1957 2281 1749 -34 -177 -55 C ATOM 1301 O PRO A 173 -17.973 9.148 27.048 1.00 22.14 O ANISOU 1301 O PRO A 173 2725 3148 2538 -28 -153 -26 O ATOM 1302 CB PRO A 173 -18.723 11.073 29.421 1.00 18.62 C ANISOU 1302 CB PRO A 173 2425 2647 2002 15 -209 -158 C ATOM 1303 CG PRO A 173 -20.131 10.931 29.916 1.00 25.11 C ANISOU 1303 CG PRO A 173 3269 3514 2757 78 -157 -188 C ATOM 1304 CD PRO A 173 -20.879 10.245 28.818 1.00 26.02 C ANISOU 1304 CD PRO A 173 3323 3670 2895 99 -103 -140 C ATOM 1305 N MET A 174 -16.758 11.013 26.705 1.00 16.08 N ANISOU 1305 N MET A 174 1989 2266 1854 -84 -202 -42 N ATOM 1306 CA MET A 174 -15.755 10.295 25.936 1.00 15.83 C ANISOU 1306 CA MET A 174 1888 2251 1876 -126 -189 7 C ATOM 1307 C MET A 174 -14.873 9.416 26.815 1.00 15.93 C ANISOU 1307 C MET A 174 1860 2301 1893 -150 -234 4 C ATOM 1308 O MET A 174 -14.334 8.416 26.326 1.00 17.01 O ANISOU 1308 O MET A 174 1934 2471 2058 -158 -215 41 O ATOM 1309 CB MET A 174 -14.913 11.287 25.134 1.00 16.31 C ANISOU 1309 CB MET A 174 1944 2243 2009 -179 -189 25 C ATOM 1310 CG MET A 174 -14.356 10.708 23.855 1.00 36.28 C ANISOU 1310 CG MET A 174 4417 4788 4581 -204 -133 81 C ATOM 1311 SD MET A 174 -15.595 9.839 22.867 1.00 41.77 S ANISOU 1311 SD MET A 174 5121 5530 5218 -145 -68 110 S ATOM 1312 CE MET A 174 -16.695 11.182 22.430 1.00 50.11 C ANISOU 1312 CE MET A 174 6261 6528 6253 -112 -68 103 C ATOM 1313 N ASN A 175 -14.721 9.750 28.101 1.00 22.58 N ANISOU 1313 N ASN A 175 2741 3135 2702 -155 -298 -40 N ATOM 1314 CA ASN A 175 -13.977 8.864 28.994 1.00 24.53 C ANISOU 1314 CA ASN A 175 2961 3420 2941 -169 -355 -38 C ATOM 1315 C ASN A 175 -14.741 7.573 29.263 1.00 23.92 C ANISOU 1315 C ASN A 175 2887 3405 2796 -126 -324 -19 C ATOM 1316 O ASN A 175 -14.121 6.525 29.469 1.00 19.16 O ANISOU 1316 O ASN A 175 2244 2832 2205 -131 -349 9 O ATOM 1317 CB ASN A 175 -13.627 9.570 30.311 1.00 24.28 C ANISOU 1317 CB ASN A 175 2987 3360 2876 -189 -442 -91 C ATOM 1318 CG ASN A 175 -14.841 10.156 31.023 1.00 29.65 C ANISOU 1318 CG ASN A 175 3765 4036 3464 -146 -423 -141 C ATOM 1319 OD1 ASN A 175 -15.982 9.769 30.775 1.00 35.76 O ANISOU 1319 OD1 ASN A 175 4551 4844 4191 -98 -353 -133 O ATOM 1320 ND2 ASN A 175 -14.587 11.098 31.922 1.00 27.97 N ANISOU 1320 ND2 ASN A 175 3620 3779 3228 -165 -487 -198 N ATOM 1321 N TYR A 176 -16.076 7.621 29.260 1.00 21.66 N ANISOU 1321 N TYR A 176 2645 3138 2446 -85 -270 -31 N ATOM 1322 CA TYR A 176 -16.842 6.383 29.332 1.00 15.60 C ANISOU 1322 CA TYR A 176 1872 2427 1628 -58 -229 -6 C ATOM 1323 C TYR A 176 -16.601 5.531 28.092 1.00 17.01 C ANISOU 1323 C TYR A 176 1986 2617 1860 -61 -189 43 C ATOM 1324 O TYR A 176 -16.349 4.324 28.195 1.00 17.00 O ANISOU 1324 O TYR A 176 1962 2643 1854 -61 -193 72 O ATOM 1325 CB TYR A 176 -18.337 6.676 29.506 1.00 16.25 C ANISOU 1325 CB TYR A 176 1994 2531 1648 -17 -174 -31 C ATOM 1326 CG TYR A 176 -19.206 5.467 29.193 1.00 16.40 C ANISOU 1326 CG TYR A 176 1989 2603 1638 -2 -121 2 C ATOM 1327 CD1 TYR A 176 -19.472 4.501 30.162 1.00 17.25 C ANISOU 1327 CD1 TYR A 176 2121 2752 1680 -4 -121 10 C ATOM 1328 CD2 TYR A 176 -19.736 5.277 27.916 1.00 14.23 C ANISOU 1328 CD2 TYR A 176 1674 2332 1400 9 -75 27 C ATOM 1329 CE1 TYR A 176 -20.252 3.386 29.866 1.00 16.38 C ANISOU 1329 CE1 TYR A 176 1990 2682 1551 -2 -73 42 C ATOM 1330 CE2 TYR A 176 -20.504 4.171 27.615 1.00 13.89 C ANISOU 1330 CE2 TYR A 176 1610 2331 1336 14 -36 54 C ATOM 1331 CZ TYR A 176 -20.761 3.231 28.588 1.00 14.04 C ANISOU 1331 CZ TYR A 176 1648 2388 1300 6 -33 61 C ATOM 1332 OH TYR A 176 -21.530 2.136 28.276 1.00 15.48 O ANISOU 1332 OH TYR A 176 1810 2604 1466 0 5 89 O ATOM 1333 N MET A 177 -16.667 6.152 26.908 1.00 14.53 N ANISOU 1333 N MET A 177 1654 2275 1592 -64 -153 52 N ATOM 1334 CA MET A 177 -16.534 5.409 25.658 1.00 14.10 C ANISOU 1334 CA MET A 177 1555 2230 1572 -66 -106 92 C ATOM 1335 C MET A 177 -15.171 4.740 25.543 1.00 19.50 C ANISOU 1335 C MET A 177 2182 2911 2314 -90 -126 114 C ATOM 1336 O MET A 177 -15.063 3.623 25.024 1.00 19.67 O ANISOU 1336 O MET A 177 2177 2954 2345 -80 -98 140 O ATOM 1337 CB MET A 177 -16.761 6.338 24.467 1.00 14.06 C ANISOU 1337 CB MET A 177 1557 2190 1594 -68 -71 100 C ATOM 1338 CG MET A 177 -18.191 6.798 24.297 1.00 20.08 C ANISOU 1338 CG MET A 177 2360 2958 2312 -30 -50 87 C ATOM 1339 SD MET A 177 -19.351 5.420 24.244 1.00 15.21 S ANISOU 1339 SD MET A 177 1729 2405 1644 -3 -18 99 S ATOM 1340 CE MET A 177 -18.806 4.547 22.777 1.00 13.12 C ANISOU 1340 CE MET A 177 1436 2139 1410 -21 16 142 C ATOM 1341 N VAL A 178 -14.121 5.406 26.010 1.00 18.59 N ANISOU 1341 N VAL A 178 2048 2770 2247 -121 -176 101 N ATOM 1342 CA VAL A 178 -12.768 4.891 25.848 1.00 17.89 C ANISOU 1342 CA VAL A 178 1883 2680 2234 -142 -195 120 C ATOM 1343 C VAL A 178 -12.380 3.966 26.994 1.00 18.75 C ANISOU 1343 C VAL A 178 1985 2812 2326 -127 -263 120 C ATOM 1344 O VAL A 178 -11.976 2.822 26.769 1.00 19.67 O ANISOU 1344 O VAL A 178 2061 2945 2468 -108 -255 145 O ATOM 1345 CB VAL A 178 -11.777 6.066 25.703 1.00 19.89 C ANISOU 1345 CB VAL A 178 2104 2892 2562 -192 -218 110 C ATOM 1346 CG1 VAL A 178 -10.347 5.565 25.739 1.00 16.41 C ANISOU 1346 CG1 VAL A 178 1566 2458 2211 -213 -248 124 C ATOM 1347 CG2 VAL A 178 -12.046 6.811 24.417 1.00 19.48 C ANISOU 1347 CG2 VAL A 178 2063 2812 2526 -208 -144 125 C ATOM 1348 N TYR A 179 -12.500 4.431 28.239 1.00 15.80 N ANISOU 1348 N TYR A 179 1662 2437 1906 -134 -333 92 N ATOM 1349 CA TYR A 179 -12.023 3.636 29.368 1.00 25.56 C ANISOU 1349 CA TYR A 179 2902 3690 3118 -125 -412 97 C ATOM 1350 C TYR A 179 -12.988 2.512 29.712 1.00 25.99 C ANISOU 1350 C TYR A 179 3009 3776 3089 -90 -385 117 C ATOM 1351 O TYR A 179 -12.590 1.347 29.813 1.00 27.01 O ANISOU 1351 O TYR A 179 3117 3914 3232 -72 -405 148 O ATOM 1352 CB TYR A 179 -11.811 4.525 30.590 1.00 16.94 C ANISOU 1352 CB TYR A 179 1863 2583 1989 -148 -499 57 C ATOM 1353 CG TYR A 179 -10.601 5.422 30.505 1.00 21.66 C ANISOU 1353 CG TYR A 179 2401 3147 2681 -195 -557 41 C ATOM 1354 CD1 TYR A 179 -9.380 4.943 30.040 1.00 18.00 C ANISOU 1354 CD1 TYR A 179 1828 2685 2326 -207 -579 68 C ATOM 1355 CD2 TYR A 179 -10.681 6.752 30.893 1.00 18.98 C ANISOU 1355 CD2 TYR A 179 2112 2771 2329 -228 -588 -3 C ATOM 1356 CE1 TYR A 179 -8.268 5.768 29.974 1.00 21.22 C ANISOU 1356 CE1 TYR A 179 2166 3066 2830 -260 -629 54 C ATOM 1357 CE2 TYR A 179 -9.581 7.582 30.827 1.00 27.38 C ANISOU 1357 CE2 TYR A 179 3121 3797 3483 -284 -645 -17 C ATOM 1358 CZ TYR A 179 -8.380 7.089 30.369 1.00 28.92 C ANISOU 1358 CZ TYR A 179 3197 4003 3790 -304 -664 14 C ATOM 1359 OH TYR A 179 -7.295 7.929 30.309 1.00 27.53 O ANISOU 1359 OH TYR A 179 2954 3793 3713 -369 -716 0 O ATOM 1360 N PHE A 180 -14.260 2.847 29.908 1.00 26.09 N ANISOU 1360 N PHE A 180 3089 3802 3022 -81 -340 99 N ATOM 1361 CA PHE A 180 -15.226 1.857 30.361 1.00 22.73 C ANISOU 1361 CA PHE A 180 2712 3409 2516 -61 -312 117 C ATOM 1362 C PHE A 180 -15.675 0.965 29.210 1.00 19.26 C ANISOU 1362 C PHE A 180 2238 2978 2104 -49 -241 148 C ATOM 1363 O PHE A 180 -15.539 -0.261 29.267 1.00 23.75 O ANISOU 1363 O PHE A 180 2804 3550 2669 -40 -247 181 O ATOM 1364 CB PHE A 180 -16.423 2.560 31.008 1.00 22.96 C ANISOU 1364 CB PHE A 180 2811 3455 2458 -56 -281 81 C ATOM 1365 CG PHE A 180 -17.285 1.653 31.839 1.00 21.38 C ANISOU 1365 CG PHE A 180 2668 3291 2165 -49 -260 97 C ATOM 1366 CD1 PHE A 180 -18.294 0.905 31.255 1.00 17.18 C ANISOU 1366 CD1 PHE A 180 2123 2784 1622 -43 -186 120 C ATOM 1367 CD2 PHE A 180 -17.097 1.559 33.209 1.00 23.65 C ANISOU 1367 CD2 PHE A 180 3026 3587 2373 -56 -315 89 C ATOM 1368 CE1 PHE A 180 -19.086 0.072 32.015 1.00 16.76 C ANISOU 1368 CE1 PHE A 180 2118 2762 1489 -49 -160 139 C ATOM 1369 CE2 PHE A 180 -17.892 0.732 33.976 1.00 22.95 C ANISOU 1369 CE2 PHE A 180 2998 3531 2192 -58 -285 110 C ATOM 1370 CZ PHE A 180 -18.885 -0.016 33.377 1.00 15.96 C ANISOU 1370 CZ PHE A 180 2091 2668 1305 -57 -203 136 C ATOM 1371 N ASN A 181 -16.214 1.566 28.152 1.00 20.74 N ANISOU 1371 N ASN A 181 2406 3161 2314 -47 -181 138 N ATOM 1372 CA ASN A 181 -16.801 0.762 27.088 1.00 26.84 C ANISOU 1372 CA ASN A 181 3162 3942 3095 -38 -121 162 C ATOM 1373 C ASN A 181 -15.727 0.029 26.292 1.00 28.37 C ANISOU 1373 C ASN A 181 3304 4116 3359 -36 -119 185 C ATOM 1374 O ASN A 181 -15.735 -1.205 26.208 1.00 35.24 O ANISOU 1374 O ASN A 181 4176 4987 4225 -25 -114 208 O ATOM 1375 CB ASN A 181 -17.660 1.633 26.174 1.00 21.00 C ANISOU 1375 CB ASN A 181 2422 3201 2354 -34 -71 147 C ATOM 1376 CG ASN A 181 -18.576 0.809 25.299 1.00 18.79 C ANISOU 1376 CG ASN A 181 2140 2939 2059 -28 -23 165 C ATOM 1377 OD1 ASN A 181 -18.328 0.638 24.106 1.00 26.96 O ANISOU 1377 OD1 ASN A 181 3155 3959 3128 -29 4 177 O ATOM 1378 ND2 ASN A 181 -19.629 0.262 25.899 1.00 17.58 N ANISOU 1378 ND2 ASN A 181 2010 2817 1853 -27 -11 165 N ATOM 1379 N PHE A 182 -14.779 0.769 25.714 1.00 20.38 N ANISOU 1379 N PHE A 182 2247 3083 2414 -46 -120 179 N ATOM 1380 CA PHE A 182 -13.809 0.144 24.821 1.00 20.01 C ANISOU 1380 CA PHE A 182 2143 3023 2438 -40 -95 196 C ATOM 1381 C PHE A 182 -12.813 -0.723 25.591 1.00 14.55 C ANISOU 1381 C PHE A 182 1417 2327 1783 -25 -155 208 C ATOM 1382 O PHE A 182 -12.750 -1.940 25.390 1.00 23.73 O ANISOU 1382 O PHE A 182 2579 3486 2953 1 -144 226 O ATOM 1383 CB PHE A 182 -13.085 1.211 24.001 1.00 17.54 C ANISOU 1383 CB PHE A 182 1787 2691 2187 -64 -67 189 C ATOM 1384 CG PHE A 182 -12.103 0.651 23.011 1.00 21.51 C ANISOU 1384 CG PHE A 182 2227 3186 2760 -58 -20 202 C ATOM 1385 CD1 PHE A 182 -12.343 -0.563 22.381 1.00 21.85 C ANISOU 1385 CD1 PHE A 182 2280 3233 2790 -29 22 213 C ATOM 1386 CD2 PHE A 182 -10.930 1.330 22.722 1.00 21.79 C ANISOU 1386 CD2 PHE A 182 2193 3209 2877 -85 -13 201 C ATOM 1387 CE1 PHE A 182 -11.440 -1.077 21.470 1.00 26.43 C ANISOU 1387 CE1 PHE A 182 2808 3804 3431 -15 76 217 C ATOM 1388 CE2 PHE A 182 -10.022 0.819 21.813 1.00 22.49 C ANISOU 1388 CE2 PHE A 182 2217 3297 3033 -77 47 210 C ATOM 1389 CZ PHE A 182 -10.278 -0.385 21.186 1.00 24.83 C ANISOU 1389 CZ PHE A 182 2529 3596 3309 -37 94 215 C ATOM 1390 N PHE A 183 -12.026 -0.113 26.480 1.00 17.81 N ANISOU 1390 N PHE A 183 1807 2735 2223 -39 -227 198 N ATOM 1391 CA PHE A 183 -10.929 -0.836 27.124 1.00 22.97 C ANISOU 1391 CA PHE A 183 2415 3384 2929 -20 -299 211 C ATOM 1392 C PHE A 183 -11.445 -1.968 28.007 1.00 22.13 C ANISOU 1392 C PHE A 183 2374 3281 2754 5 -340 233 C ATOM 1393 O PHE A 183 -11.037 -3.124 27.854 1.00 20.91 O ANISOU 1393 O PHE A 183 2200 3112 2632 39 -346 256 O ATOM 1394 CB PHE A 183 -10.065 0.127 27.945 1.00 23.21 C ANISOU 1394 CB PHE A 183 2413 3409 2996 -49 -384 193 C ATOM 1395 CG PHE A 183 -9.155 1.000 27.116 1.00 28.30 C ANISOU 1395 CG PHE A 183 2970 4042 3741 -80 -355 182 C ATOM 1396 CD1 PHE A 183 -9.060 0.834 25.744 1.00 25.53 C ANISOU 1396 CD1 PHE A 183 2576 3689 3435 -75 -253 192 C ATOM 1397 CD2 PHE A 183 -8.384 1.983 27.718 1.00 33.10 C ANISOU 1397 CD2 PHE A 183 3543 4640 4393 -121 -428 163 C ATOM 1398 CE1 PHE A 183 -8.218 1.637 24.988 1.00 22.01 C ANISOU 1398 CE1 PHE A 183 2055 3234 3075 -112 -214 188 C ATOM 1399 CE2 PHE A 183 -7.544 2.789 26.966 1.00 30.09 C ANISOU 1399 CE2 PHE A 183 3078 4245 4108 -162 -396 158 C ATOM 1400 CZ PHE A 183 -7.462 2.612 25.600 1.00 17.60 C ANISOU 1400 CZ PHE A 183 1454 2663 2569 -158 -283 173 C ATOM 1401 N ALA A 184 -12.354 -1.655 28.934 1.00 21.17 N ANISOU 1401 N ALA A 184 2334 3174 2535 -10 -362 226 N ATOM 1402 CA ALA A 184 -12.807 -2.643 29.910 1.00 21.36 C ANISOU 1402 CA ALA A 184 2430 3201 2483 3 -400 252 C ATOM 1403 C ALA A 184 -13.774 -3.659 29.304 1.00 23.60 C ANISOU 1403 C ALA A 184 2747 3485 2735 11 -326 274 C ATOM 1404 O ALA A 184 -13.590 -4.869 29.465 1.00 21.66 O ANISOU 1404 O ALA A 184 2519 3218 2492 32 -347 306 O ATOM 1405 CB ALA A 184 -13.458 -1.938 31.102 1.00 22.24 C ANISOU 1405 CB ALA A 184 2622 3333 2495 -20 -432 233 C ATOM 1406 N CYS A 185 -14.809 -3.189 28.605 1.00 23.59 N ANISOU 1406 N CYS A 185 2755 3501 2706 -5 -249 256 N ATOM 1407 CA CYS A 185 -15.934 -4.035 28.221 1.00 24.94 C ANISOU 1407 CA CYS A 185 2964 3678 2834 -11 -191 272 C ATOM 1408 C CYS A 185 -15.870 -4.565 26.792 1.00 19.21 C ANISOU 1408 C CYS A 185 2202 2933 2163 0 -136 273 C ATOM 1409 O CYS A 185 -16.674 -5.433 26.440 1.00 17.68 O ANISOU 1409 O CYS A 185 2040 2736 1943 -8 -102 286 O ATOM 1410 CB CYS A 185 -17.252 -3.271 28.409 1.00 27.20 C ANISOU 1410 CB CYS A 185 3281 4000 3053 -33 -146 251 C ATOM 1411 SG CYS A 185 -17.565 -2.745 30.104 1.00 27.76 S ANISOU 1411 SG CYS A 185 3418 4096 3034 -45 -187 241 S ATOM 1412 N VAL A 186 -14.959 -4.071 25.957 1.00 20.65 N ANISOU 1412 N VAL A 186 2324 3104 2419 13 -124 259 N ATOM 1413 CA VAL A 186 -14.821 -4.530 24.580 1.00 18.39 C ANISOU 1413 CA VAL A 186 2014 2801 2173 25 -65 256 C ATOM 1414 C VAL A 186 -13.442 -5.133 24.329 1.00 19.31 C ANISOU 1414 C VAL A 186 2076 2888 2372 59 -78 261 C ATOM 1415 O VAL A 186 -13.325 -6.262 23.847 1.00 21.21 O ANISOU 1415 O VAL A 186 2327 3101 2630 85 -58 268 O ATOM 1416 CB VAL A 186 -15.112 -3.391 23.574 1.00 22.09 C ANISOU 1416 CB VAL A 186 2465 3282 2645 8 -13 236 C ATOM 1417 CG1 VAL A 186 -14.764 -3.819 22.153 1.00 22.94 C ANISOU 1417 CG1 VAL A 186 2557 3372 2787 20 48 232 C ATOM 1418 CG2 VAL A 186 -16.572 -2.961 23.659 1.00 17.27 C ANISOU 1418 CG2 VAL A 186 1900 2697 1965 -12 2 229 C ATOM 1419 N LEU A 187 -12.384 -4.398 24.671 1.00 14.79 N ANISOU 1419 N LEU A 187 1442 2321 1858 61 -113 255 N ATOM 1420 CA LEU A 187 -11.037 -4.822 24.308 1.00 18.88 C ANISOU 1420 CA LEU A 187 1881 2819 2473 95 -115 255 C ATOM 1421 C LEU A 187 -10.583 -6.012 25.146 1.00 20.26 C ANISOU 1421 C LEU A 187 2063 2968 2665 137 -186 278 C ATOM 1422 O LEU A 187 -10.045 -6.989 24.612 1.00 23.89 O ANISOU 1422 O LEU A 187 2498 3398 3179 182 -164 280 O ATOM 1423 CB LEU A 187 -10.069 -3.651 24.459 1.00 18.46 C ANISOU 1423 CB LEU A 187 1749 2779 2485 73 -139 243 C ATOM 1424 CG LEU A 187 -8.673 -3.840 23.874 1.00 22.48 C ANISOU 1424 CG LEU A 187 2149 3281 3112 99 -117 239 C ATOM 1425 CD1 LEU A 187 -8.764 -4.228 22.405 1.00 24.73 C ANISOU 1425 CD1 LEU A 187 2433 3558 3406 113 -1 229 C ATOM 1426 CD2 LEU A 187 -7.864 -2.560 24.045 1.00 22.72 C ANISOU 1426 CD2 LEU A 187 2104 3325 3204 57 -139 228 C ATOM 1427 N VAL A 188 -10.784 -5.948 26.461 1.00 20.03 N ANISOU 1427 N VAL A 188 2077 2946 2588 126 -271 295 N ATOM 1428 CA VAL A 188 -10.371 -7.057 27.324 1.00 22.59 C ANISOU 1428 CA VAL A 188 2425 3241 2918 164 -350 325 C ATOM 1429 C VAL A 188 -11.106 -8.348 26.975 1.00 19.82 C ANISOU 1429 C VAL A 188 2146 2855 2530 181 -312 344 C ATOM 1430 O VAL A 188 -10.438 -9.382 26.801 1.00 19.47 O ANISOU 1430 O VAL A 188 2086 2767 2546 234 -329 356 O ATOM 1431 CB VAL A 188 -10.505 -6.654 28.803 1.00 21.69 C ANISOU 1431 CB VAL A 188 2363 3143 2737 142 -447 340 C ATOM 1432 CG1 VAL A 188 -10.390 -7.865 29.714 1.00 17.75 C ANISOU 1432 CG1 VAL A 188 1926 2608 2209 174 -525 383 C ATOM 1433 CG2 VAL A 188 -9.441 -5.623 29.159 1.00 21.44 C ANISOU 1433 CG2 VAL A 188 2249 3128 2768 134 -511 321 C ATOM 1434 N PRO A 189 -12.440 -8.371 26.827 1.00 20.11 N ANISOU 1434 N PRO A 189 2257 2903 2479 140 -261 345 N ATOM 1435 CA PRO A 189 -13.089 -9.618 26.372 1.00 25.18 C ANISOU 1435 CA PRO A 189 2962 3507 3101 146 -226 359 C ATOM 1436 C PRO A 189 -12.598 -10.116 25.022 1.00 25.65 C ANISOU 1436 C PRO A 189 2981 3534 3229 182 -164 334 C ATOM 1437 O PRO A 189 -12.442 -11.329 24.840 1.00 24.63 O ANISOU 1437 O PRO A 189 2886 3350 3123 217 -168 345 O ATOM 1438 CB PRO A 189 -14.575 -9.239 26.325 1.00 15.31 C ANISOU 1438 CB PRO A 189 1766 2291 1761 86 -178 355 C ATOM 1439 CG PRO A 189 -14.707 -8.175 27.333 1.00 16.80 C ANISOU 1439 CG PRO A 189 1955 2524 1905 62 -215 354 C ATOM 1440 CD PRO A 189 -13.444 -7.366 27.221 1.00 19.07 C ANISOU 1440 CD PRO A 189 2161 2818 2268 88 -245 334 C ATOM 1441 N LEU A 190 -12.359 -9.222 24.060 1.00 24.27 N ANISOU 1441 N LEU A 190 2746 3389 3085 176 -103 301 N ATOM 1442 CA LEU A 190 -11.849 -9.671 22.769 1.00 21.93 C ANISOU 1442 CA LEU A 190 2421 3067 2843 210 -32 275 C ATOM 1443 C LEU A 190 -10.465 -10.289 22.915 1.00 27.10 C ANISOU 1443 C LEU A 190 3010 3689 3598 280 -61 276 C ATOM 1444 O LEU A 190 -10.148 -11.281 22.248 1.00 30.69 O ANISOU 1444 O LEU A 190 3475 4097 4091 328 -25 262 O ATOM 1445 CB LEU A 190 -11.834 -8.512 21.771 1.00 20.16 C ANISOU 1445 CB LEU A 190 2155 2883 2622 184 40 247 C ATOM 1446 CG LEU A 190 -13.208 -8.126 21.202 1.00 17.79 C ANISOU 1446 CG LEU A 190 1921 2603 2235 134 79 240 C ATOM 1447 CD1 LEU A 190 -13.131 -6.833 20.396 1.00 14.57 C ANISOU 1447 CD1 LEU A 190 1480 2229 1827 109 130 223 C ATOM 1448 CD2 LEU A 190 -13.779 -9.251 20.348 1.00 14.91 C ANISOU 1448 CD2 LEU A 190 1622 2202 1843 141 117 228 C ATOM 1449 N LEU A 191 -9.634 -9.734 23.801 1.00 24.29 N ANISOU 1449 N LEU A 191 2586 3353 3290 289 -131 289 N ATOM 1450 CA LEU A 191 -8.341 -10.353 24.075 1.00 18.54 C ANISOU 1450 CA LEU A 191 1783 2594 2666 360 -178 294 C ATOM 1451 C LEU A 191 -8.506 -11.685 24.797 1.00 20.00 C ANISOU 1451 C LEU A 191 2045 2719 2835 401 -249 327 C ATOM 1452 O LEU A 191 -7.697 -12.598 24.599 1.00 20.38 O ANISOU 1452 O LEU A 191 2060 2718 2964 477 -260 325 O ATOM 1453 CB LEU A 191 -7.458 -9.402 24.884 1.00 22.12 C ANISOU 1453 CB LEU A 191 2145 3085 3174 351 -254 301 C ATOM 1454 CG LEU A 191 -7.031 -8.095 24.205 1.00 26.46 C ANISOU 1454 CG LEU A 191 2605 3682 3765 310 -191 272 C ATOM 1455 CD1 LEU A 191 -6.183 -7.237 25.142 1.00 23.54 C ANISOU 1455 CD1 LEU A 191 2155 3340 3451 293 -286 278 C ATOM 1456 CD2 LEU A 191 -6.283 -8.363 22.905 1.00 22.87 C ANISOU 1456 CD2 LEU A 191 2073 3221 3397 349 -84 244 C ATOM 1457 N LEU A 192 -9.551 -11.823 25.618 1.00 23.64 N ANISOU 1457 N LEU A 192 2610 3178 3193 354 -292 359 N ATOM 1458 CA LEU A 192 -9.844 -13.113 26.238 1.00 26.94 C ANISOU 1458 CA LEU A 192 3123 3532 3583 379 -348 398 C ATOM 1459 C LEU A 192 -10.303 -14.137 25.204 1.00 32.04 C ANISOU 1459 C LEU A 192 3823 4120 4229 394 -273 380 C ATOM 1460 O LEU A 192 -9.925 -15.311 25.282 1.00 32.84 O ANISOU 1460 O LEU A 192 3961 4146 4371 453 -305 395 O ATOM 1461 CB LEU A 192 -10.898 -12.952 27.335 1.00 26.19 C ANISOU 1461 CB LEU A 192 3125 3456 3369 312 -392 436 C ATOM 1462 CG LEU A 192 -10.473 -12.209 28.607 1.00 25.93 C ANISOU 1462 CG LEU A 192 3078 3461 3314 302 -488 458 C ATOM 1463 CD1 LEU A 192 -11.633 -12.078 29.586 1.00 23.17 C ANISOU 1463 CD1 LEU A 192 2837 3133 2834 235 -503 488 C ATOM 1464 CD2 LEU A 192 -9.307 -12.913 29.263 1.00 27.05 C ANISOU 1464 CD2 LEU A 192 3197 3555 3526 375 -596 488 C ATOM 1465 N MET A 193 -11.123 -13.722 24.232 1.00 32.41 N ANISOU 1465 N MET A 193 3887 4197 4232 345 -182 347 N ATOM 1466 CA MET A 193 -11.491 -14.639 23.156 1.00 35.44 C ANISOU 1466 CA MET A 193 4324 4526 4615 358 -116 320 C ATOM 1467 C MET A 193 -10.259 -15.100 22.397 1.00 36.29 C ANISOU 1467 C MET A 193 4366 4595 4827 447 -81 286 C ATOM 1468 O MET A 193 -10.123 -16.287 22.076 1.00 44.34 O ANISOU 1468 O MET A 193 5438 5536 5874 497 -76 278 O ATOM 1469 CB MET A 193 -12.475 -13.983 22.185 1.00 36.08 C ANISOU 1469 CB MET A 193 4423 4653 4633 294 -35 288 C ATOM 1470 CG MET A 193 -13.795 -13.562 22.786 1.00 36.39 C ANISOU 1470 CG MET A 193 4515 4731 4579 211 -54 313 C ATOM 1471 SD MET A 193 -14.848 -12.742 21.573 1.00 38.25 S ANISOU 1471 SD MET A 193 4756 5018 4758 152 25 276 S ATOM 1472 CE MET A 193 -15.864 -11.741 22.658 1.00 37.53 C ANISOU 1472 CE MET A 193 4665 4997 4597 86 -8 304 C ATOM 1473 N LEU A 194 -9.352 -14.168 22.097 1.00 31.21 N ANISOU 1473 N LEU A 194 3606 4005 4246 468 -52 264 N ATOM 1474 CA LEU A 194 -8.126 -14.524 21.395 1.00 27.29 C ANISOU 1474 CA LEU A 194 3026 3485 3859 553 -5 230 C ATOM 1475 C LEU A 194 -7.349 -15.586 22.160 1.00 27.51 C ANISOU 1475 C LEU A 194 3045 3443 3963 639 -91 254 C ATOM 1476 O LEU A 194 -6.865 -16.558 21.569 1.00 31.67 O ANISOU 1476 O LEU A 194 3577 3905 4550 717 -56 227 O ATOM 1477 CB LEU A 194 -7.273 -13.273 21.176 1.00 27.71 C ANISOU 1477 CB LEU A 194 2946 3612 3972 544 28 214 C ATOM 1478 CG LEU A 194 -5.934 -13.465 20.462 1.00 30.73 C ANISOU 1478 CG LEU A 194 3211 3987 4478 624 93 178 C ATOM 1479 CD1 LEU A 194 -6.155 -13.972 19.051 1.00 30.25 C ANISOU 1479 CD1 LEU A 194 3203 3899 4393 644 220 129 C ATOM 1480 CD2 LEU A 194 -5.132 -12.173 20.456 1.00 31.32 C ANISOU 1480 CD2 LEU A 194 3149 4136 4616 595 111 175 C ATOM 1481 N GLY A 195 -7.245 -15.432 23.483 1.00 25.00 N ANISOU 1481 N GLY A 195 2725 3135 3641 630 -209 305 N ATOM 1482 CA GLY A 195 -6.531 -16.410 24.283 1.00 22.26 C ANISOU 1482 CA GLY A 195 2379 2720 3360 712 -310 337 C ATOM 1483 C GLY A 195 -7.239 -17.745 24.374 1.00 27.26 C ANISOU 1483 C GLY A 195 3158 3256 3944 725 -328 359 C ATOM 1484 O GLY A 195 -6.587 -18.790 24.458 1.00 29.80 O ANISOU 1484 O GLY A 195 3488 3494 4341 817 -369 365 O ATOM 1485 N VAL A 196 -8.574 -17.736 24.368 1.00 23.45 N ANISOU 1485 N VAL A 196 2789 2778 3343 633 -302 372 N ATOM 1486 CA VAL A 196 -9.318 -18.993 24.365 1.00 25.32 C ANISOU 1486 CA VAL A 196 3164 2920 3536 626 -311 391 C ATOM 1487 C VAL A 196 -9.099 -19.735 23.052 1.00 29.07 C ANISOU 1487 C VAL A 196 3651 3333 4062 682 -224 330 C ATOM 1488 O VAL A 196 -8.854 -20.947 23.042 1.00 27.10 O ANISOU 1488 O VAL A 196 3468 2976 3853 747 -251 334 O ATOM 1489 CB VAL A 196 -10.813 -18.735 24.635 1.00 23.67 C ANISOU 1489 CB VAL A 196 3052 2743 3200 505 -296 415 C ATOM 1490 CG1 VAL A 196 -11.619 -20.008 24.434 1.00 22.31 C ANISOU 1490 CG1 VAL A 196 3014 2472 2990 482 -291 427 C ATOM 1491 CG2 VAL A 196 -11.019 -18.202 26.044 1.00 24.61 C ANISOU 1491 CG2 VAL A 196 3183 2907 3259 461 -381 475 C ATOM 1492 N TYR A 197 -9.164 -19.023 21.925 1.00 26.16 N ANISOU 1492 N TYR A 197 3229 3023 3687 660 -118 272 N ATOM 1493 CA TYR A 197 -8.947 -19.674 20.637 1.00 27.53 C ANISOU 1493 CA TYR A 197 3425 3142 3892 712 -27 207 C ATOM 1494 C TYR A 197 -7.522 -20.201 20.511 1.00 33.03 C ANISOU 1494 C TYR A 197 4037 3793 4721 844 -25 183 C ATOM 1495 O TYR A 197 -7.306 -21.280 19.948 1.00 38.22 O ANISOU 1495 O TYR A 197 4752 4355 5416 915 4 148 O ATOM 1496 CB TYR A 197 -9.282 -18.716 19.493 1.00 24.68 C ANISOU 1496 CB TYR A 197 3032 2862 3485 658 82 157 C ATOM 1497 CG TYR A 197 -10.767 -18.595 19.242 1.00 26.83 C ANISOU 1497 CG TYR A 197 3408 3148 3639 550 93 161 C ATOM 1498 CD1 TYR A 197 -11.519 -19.708 18.887 1.00 20.95 C ANISOU 1498 CD1 TYR A 197 2791 2317 2854 532 91 148 C ATOM 1499 CD2 TYR A 197 -11.420 -17.370 19.354 1.00 23.36 C ANISOU 1499 CD2 TYR A 197 2936 2805 3136 466 100 176 C ATOM 1500 CE1 TYR A 197 -12.879 -19.610 18.658 1.00 22.49 C ANISOU 1500 CE1 TYR A 197 3064 2528 2952 428 93 151 C ATOM 1501 CE2 TYR A 197 -12.786 -17.263 19.125 1.00 21.77 C ANISOU 1501 CE2 TYR A 197 2813 2620 2838 374 105 179 C ATOM 1502 CZ TYR A 197 -13.507 -18.388 18.779 1.00 25.62 C ANISOU 1502 CZ TYR A 197 3414 3029 3293 353 100 167 C ATOM 1503 OH TYR A 197 -14.859 -18.298 18.553 1.00 31.34 O ANISOU 1503 OH TYR A 197 4201 3773 3935 258 99 170 O ATOM 1504 N LEU A 198 -6.537 -19.470 21.042 1.00 31.99 N ANISOU 1504 N LEU A 198 3764 3722 4667 881 -60 199 N ATOM 1505 CA LEU A 198 -5.165 -19.970 21.016 1.00 33.70 C ANISOU 1505 CA LEU A 198 3878 3900 5026 1012 -70 180 C ATOM 1506 C LEU A 198 -5.038 -21.264 21.809 1.00 35.73 C ANISOU 1506 C LEU A 198 4218 4041 5319 1085 -179 220 C ATOM 1507 O LEU A 198 -4.309 -22.179 21.409 1.00 37.25 O ANISOU 1507 O LEU A 198 4397 4151 5605 1200 -162 187 O ATOM 1508 CB LEU A 198 -4.203 -18.915 21.558 1.00 34.17 C ANISOU 1508 CB LEU A 198 3768 4051 5166 1021 -108 197 C ATOM 1509 CG LEU A 198 -3.980 -17.701 20.661 1.00 38.57 C ANISOU 1509 CG LEU A 198 4221 4708 5725 972 10 153 C ATOM 1510 CD1 LEU A 198 -2.972 -16.761 21.294 1.00 39.90 C ANISOU 1510 CD1 LEU A 198 4222 4951 5987 978 -44 172 C ATOM 1511 CD2 LEU A 198 -3.528 -18.136 19.271 1.00 39.52 C ANISOU 1511 CD2 LEU A 198 4321 4804 5892 1037 156 80 C ATOM 1512 N AARG A 199 -5.742 -21.361 22.938 0.49 35.06 N ANISOU 1512 N AARG A 199 4224 3941 5155 1021 -289 292 N ATOM 1513 N BARG A 199 -5.735 -21.355 22.944 0.51 35.07 N ANISOU 1513 N BARG A 199 4225 3943 5158 1022 -290 293 N ATOM 1514 CA AARG A 199 -5.721 -22.597 23.711 0.49 36.96 C ANISOU 1514 CA AARG A 199 4569 4062 5412 1078 -395 342 C ATOM 1515 CA BARG A 199 -5.732 -22.591 23.717 0.51 36.94 C ANISOU 1515 CA BARG A 199 4567 4060 5408 1076 -395 343 C ATOM 1516 C AARG A 199 -6.512 -23.702 23.022 0.49 34.62 C ANISOU 1516 C AARG A 199 4428 3658 5070 1068 -343 318 C ATOM 1517 C BARG A 199 -6.498 -23.698 23.004 0.51 34.64 C ANISOU 1517 C BARG A 199 4428 3660 5074 1069 -341 316 C ATOM 1518 O AARG A 199 -6.200 -24.885 23.196 0.49 36.82 O ANISOU 1518 O AARG A 199 4778 3810 5401 1152 -394 330 O ATOM 1519 O BARG A 199 -6.153 -24.877 23.144 0.51 36.74 O ANISOU 1519 O BARG A 199 4761 3801 5396 1157 -389 326 O ATOM 1520 CB AARG A 199 -6.262 -22.344 25.119 0.49 35.80 C ANISOU 1520 CB AARG A 199 4486 3936 5180 1003 -517 430 C ATOM 1521 CB BARG A 199 -6.321 -22.340 25.106 0.51 35.71 C ANISOU 1521 CB BARG A 199 4480 3925 5163 997 -514 430 C ATOM 1522 CG AARG A 199 -5.418 -21.380 25.941 0.49 39.17 C ANISOU 1522 CG AARG A 199 4779 4451 5652 1019 -597 455 C ATOM 1523 CG BARG A 199 -5.485 -21.417 25.980 0.51 39.12 C ANISOU 1523 CG BARG A 199 4784 4441 5640 1015 -600 459 C ATOM 1524 CD AARG A 199 -5.986 -21.195 27.339 0.49 40.79 C ANISOU 1524 CD AARG A 199 5073 4670 5754 947 -714 537 C ATOM 1525 CD BARG A 199 -6.247 -20.986 27.226 0.51 40.55 C ANISOU 1525 CD BARG A 199 5049 4660 5699 917 -689 530 C ATOM 1526 NE AARG A 199 -5.178 -20.282 28.144 0.49 42.18 N ANISOU 1526 NE AARG A 199 5135 4924 5967 959 -804 556 N ATOM 1527 NE BARG A 199 -6.715 -22.122 28.016 0.51 42.39 N ANISOU 1527 NE BARG A 199 5442 4787 5878 918 -774 599 N ATOM 1528 CZ AARG A 199 -4.159 -20.663 28.907 0.49 48.67 C ANISOU 1528 CZ AARG A 199 5912 5709 6873 1052 -936 592 C ATOM 1529 CZ BARG A 199 -6.049 -22.647 29.039 0.51 45.02 C ANISOU 1529 CZ BARG A 199 5798 5062 6244 987 -914 660 C ATOM 1530 NH1AARG A 199 -3.819 -21.943 28.971 0.49 52.70 N ANISOU 1530 NH1AARG A 199 6483 6098 7441 1149 -989 616 N ATOM 1531 NH1BARG A 199 -4.879 -22.139 29.402 0.51 49.62 N ANISOU 1531 NH1BARG A 199 6242 5690 6922 1061 -991 657 N ATOM 1532 NH2AARG A 199 -3.479 -19.764 29.606 0.49 50.24 N ANISOU 1532 NH2AARG A 199 6005 5983 7100 1049 -1023 603 N ATOM 1533 NH2BARG A 199 -6.553 -23.679 29.701 0.51 46.28 N ANISOU 1533 NH2BARG A 199 6122 5119 6344 978 -981 728 N ATOM 1534 N ILE A 200 -7.530 -23.340 22.237 1.00 30.91 N ANISOU 1534 N ILE A 200 4012 3227 4505 966 -250 282 N ATOM 1535 CA ILE A 200 -8.292 -24.341 21.494 1.00 31.60 C ANISOU 1535 CA ILE A 200 4243 3215 4548 946 -203 249 C ATOM 1536 C ILE A 200 -7.430 -24.971 20.408 1.00 32.21 C ANISOU 1536 C ILE A 200 4295 3226 4718 1067 -124 167 C ATOM 1537 O ILE A 200 -7.368 -26.198 20.273 1.00 33.81 O ANISOU 1537 O ILE A 200 4600 3294 4954 1130 -144 155 O ATOM 1538 CB ILE A 200 -9.565 -23.716 20.896 1.00 29.38 C ANISOU 1538 CB ILE A 200 4011 3004 4148 810 -134 229 C ATOM 1539 CG1 ILE A 200 -10.616 -23.494 21.982 1.00 29.88 C ANISOU 1539 CG1 ILE A 200 4139 3096 4119 694 -207 307 C ATOM 1540 CG2 ILE A 200 -10.110 -24.587 19.770 1.00 25.85 C ANISOU 1540 CG2 ILE A 200 3679 2469 3674 801 -67 166 C ATOM 1541 CD1 ILE A 200 -11.899 -22.878 21.464 1.00 28.87 C ANISOU 1541 CD1 ILE A 200 4043 3038 3887 566 -149 290 C ATOM 1542 N PHE A 201 -6.762 -24.138 19.608 1.00 31.11 N ANISOU 1542 N PHE A 201 4024 3177 4620 1100 -27 109 N ATOM 1543 CA PHE A 201 -5.958 -24.660 18.509 1.00 35.06 C ANISOU 1543 CA PHE A 201 4496 3627 5198 1212 73 24 C ATOM 1544 C PHE A 201 -4.707 -25.362 19.016 1.00 40.58 C ANISOU 1544 C PHE A 201 5121 4254 6045 1367 15 32 C ATOM 1545 O PHE A 201 -4.219 -26.299 18.372 1.00 41.38 O ANISOU 1545 O PHE A 201 5256 4255 6211 1476 64 -28 O ATOM 1546 CB PHE A 201 -5.597 -23.528 17.548 1.00 33.70 C ANISOU 1546 CB PHE A 201 4206 3576 5022 1194 201 -32 C ATOM 1547 CG PHE A 201 -6.787 -22.918 16.864 1.00 26.51 C ANISOU 1547 CG PHE A 201 3376 2723 3971 1061 260 -48 C ATOM 1548 CD1 PHE A 201 -7.712 -23.719 16.214 1.00 26.57 C ANISOU 1548 CD1 PHE A 201 3548 2651 3898 1021 282 -83 C ATOM 1549 CD2 PHE A 201 -6.991 -21.549 16.888 1.00 25.32 C ANISOU 1549 CD2 PHE A 201 3142 2703 3776 976 283 -28 C ATOM 1550 CE1 PHE A 201 -8.812 -23.163 15.589 1.00 27.85 C ANISOU 1550 CE1 PHE A 201 3776 2867 3937 903 321 -97 C ATOM 1551 CE2 PHE A 201 -8.090 -20.987 16.268 1.00 27.47 C ANISOU 1551 CE2 PHE A 201 3486 3024 3926 864 326 -39 C ATOM 1552 CZ PHE A 201 -9.002 -21.794 15.617 1.00 28.57 C ANISOU 1552 CZ PHE A 201 3778 3090 3987 829 342 -73 C ATOM 1553 N ALA A 202 -4.178 -24.931 20.162 1.00 42.36 N ANISOU 1553 N ALA A 202 5247 4523 6323 1382 -94 101 N ATOM 1554 CA ALA A 202 -3.045 -25.634 20.752 1.00 40.50 C ANISOU 1554 CA ALA A 202 4945 4214 6230 1530 -179 119 C ATOM 1555 C ALA A 202 -3.467 -26.998 21.285 1.00 36.11 C ANISOU 1555 C ALA A 202 4564 3497 5660 1565 -276 159 C ATOM 1556 O ALA A 202 -2.708 -27.969 21.194 1.00 39.70 O ANISOU 1556 O ALA A 202 5020 3841 6225 1707 -297 137 O ATOM 1557 CB ALA A 202 -2.420 -24.785 21.859 1.00 31.44 C ANISOU 1557 CB ALA A 202 3657 3158 5131 1526 -288 184 C ATOM 1558 N ALA A 203 -4.678 -27.090 21.839 1.00 36.73 N ANISOU 1558 N ALA A 203 4791 3558 5608 1436 -332 219 N ATOM 1559 CA ALA A 203 -5.162 -28.363 22.360 1.00 35.87 C ANISOU 1559 CA ALA A 203 4861 3291 5476 1446 -420 267 C ATOM 1560 C ALA A 203 -5.433 -29.352 21.235 1.00 37.26 C ANISOU 1560 C ALA A 203 5153 3347 5656 1483 -332 187 C ATOM 1561 O ALA A 203 -5.117 -30.541 21.358 1.00 41.54 O ANISOU 1561 O ALA A 203 5786 3735 6262 1581 -383 190 O ATOM 1562 CB ALA A 203 -6.422 -28.141 23.197 1.00 31.13 C ANISOU 1562 CB ALA A 203 4379 2716 4735 1285 -482 349 C ATOM 1563 N ALA A 204 -6.019 -28.878 20.132 1.00 36.05 N ANISOU 1563 N ALA A 204 5009 3258 5431 1406 -204 115 N ATOM 1564 CA ALA A 204 -6.289 -29.753 18.996 1.00 32.77 C ANISOU 1564 CA ALA A 204 4711 2735 5004 1433 -119 28 C ATOM 1565 C ALA A 204 -4.999 -30.250 18.359 1.00 40.23 C ANISOU 1565 C ALA A 204 5578 3621 6086 1617 -58 -50 C ATOM 1566 O ALA A 204 -4.873 -31.440 18.046 1.00 45.60 O ANISOU 1566 O ALA A 204 6373 4144 6809 1703 -61 -89 O ATOM 1567 CB ALA A 204 -7.142 -29.021 17.963 1.00 33.01 C ANISOU 1567 CB ALA A 204 4759 2862 4923 1312 -6 -30 C ATOM 1568 N ARG A 205 -4.037 -29.350 18.148 1.00 41.91 N ANISOU 1568 N ARG A 205 5594 3957 6374 1679 4 -77 N ATOM 1569 CA ARG A 205 -2.762 -29.746 17.561 1.00 53.39 C ANISOU 1569 CA ARG A 205 6945 5373 7970 1856 75 -152 C ATOM 1570 C ARG A 205 -2.060 -30.792 18.419 1.00 58.09 C ANISOU 1570 C ARG A 205 7553 5831 8689 1999 -51 -109 C ATOM 1571 O ARG A 205 -1.454 -31.734 17.894 1.00 61.32 O ANISOU 1571 O ARG A 205 7988 6120 9189 2143 -10 -176 O ATOM 1572 CB ARG A 205 -1.875 -28.515 17.375 1.00 59.73 C ANISOU 1572 CB ARG A 205 7517 6341 8837 1876 149 -168 C ATOM 1573 CG ARG A 205 -0.426 -28.824 17.044 1.00 68.06 C ANISOU 1573 CG ARG A 205 8415 7377 10067 2062 206 -227 C ATOM 1574 CD ARG A 205 0.446 -27.602 17.262 1.00 72.21 C ANISOU 1574 CD ARG A 205 8701 8064 10673 2062 228 -210 C ATOM 1575 NE ARG A 205 0.340 -27.089 18.627 1.00 75.41 N ANISOU 1575 NE ARG A 205 9060 8517 11074 1998 59 -102 N ATOM 1576 CZ ARG A 205 0.885 -25.950 19.042 1.00 77.39 C ANISOU 1576 CZ ARG A 205 9130 8905 11371 1962 40 -71 C ATOM 1577 NH1 ARG A 205 1.577 -25.198 18.199 1.00 80.83 N ANISOU 1577 NH1 ARG A 205 9404 9442 11865 1977 184 -133 N ATOM 1578 NH2 ARG A 205 0.739 -25.559 20.301 1.00 76.64 N ANISOU 1578 NH2 ARG A 205 9021 8841 11258 1905 -121 22 N ATOM 1579 N ARG A 206 -2.147 -30.654 19.744 1.00 55.51 N ANISOU 1579 N ARG A 206 7217 5512 8361 1963 -208 2 N ATOM 1580 CA ARG A 206 -1.484 -31.602 20.634 1.00 56.87 C ANISOU 1580 CA ARG A 206 7409 5555 8643 2097 -349 57 C ATOM 1581 C ARG A 206 -2.171 -32.961 20.609 1.00 54.64 C ANISOU 1581 C ARG A 206 7365 5075 8320 2102 -391 63 C ATOM 1582 O ARG A 206 -1.504 -34.001 20.651 1.00 57.78 O ANISOU 1582 O ARG A 206 7798 5326 8830 2258 -435 47 O ATOM 1583 CB ARG A 206 -1.450 -31.046 22.056 1.00 61.89 C ANISOU 1583 CB ARG A 206 7995 6257 9265 2044 -508 176 C ATOM 1584 CG ARG A 206 -0.561 -31.826 23.006 1.00 73.22 C ANISOU 1584 CG ARG A 206 9412 7584 10825 2194 -666 237 C ATOM 1585 CD ARG A 206 -0.629 -31.256 24.412 1.00 80.40 C ANISOU 1585 CD ARG A 206 10299 8560 11688 2125 -827 355 C ATOM 1586 NE ARG A 206 0.510 -31.673 25.226 1.00 88.90 N ANISOU 1586 NE ARG A 206 11288 9601 12888 2261 -958 405 N ATOM 1587 CZ ARG A 206 0.685 -31.329 26.498 1.00 94.39 C ANISOU 1587 CZ ARG A 206 11965 10355 13545 2217 -1102 505 C ATOM 1588 NH1 ARG A 206 -0.212 -30.564 27.107 1.00 94.68 N ANISOU 1588 NH1 ARG A 206 12068 10452 13456 2079 -1159 563 N ATOM 1589 NH2 ARG A 206 1.755 -31.751 27.161 1.00 97.76 N ANISOU 1589 NH2 ARG A 206 12313 10778 14052 2312 -1188 545 N ATOM 1590 N GLN A 207 -3.504 -32.974 20.541 1.00 49.73 N ANISOU 1590 N GLN A 207 6906 4445 7545 1932 -381 85 N ATOM 1591 CA GLN A 207 -4.233 -34.237 20.555 1.00 47.76 C ANISOU 1591 CA GLN A 207 6885 4006 7253 1911 -427 97 C ATOM 1592 C GLN A 207 -4.022 -35.027 19.271 1.00 45.68 C ANISOU 1592 C GLN A 207 6692 3633 7033 2005 -312 -29 C ATOM 1593 O GLN A 207 -3.983 -36.264 19.304 1.00 42.08 O ANISOU 1593 O GLN A 207 6382 2984 6622 2083 -362 -35 O ATOM 1594 CB GLN A 207 -5.721 -33.976 20.791 1.00 37.78 C ANISOU 1594 CB GLN A 207 5753 2778 5824 1695 -439 150 C ATOM 1595 CG GLN A 207 -6.019 -33.441 22.182 1.00 45.27 C ANISOU 1595 CG GLN A 207 6682 3799 6720 1606 -559 279 C ATOM 1596 CD GLN A 207 -7.484 -33.124 22.394 1.00 43.19 C ANISOU 1596 CD GLN A 207 6524 3584 6300 1397 -553 325 C ATOM 1597 OE1 GLN A 207 -8.357 -33.688 21.733 1.00 46.19 O ANISOU 1597 OE1 GLN A 207 7040 3888 6621 1318 -504 285 O ATOM 1598 NE2 GLN A 207 -7.763 -32.211 23.320 1.00 38.77 N ANISOU 1598 NE2 GLN A 207 5900 3153 5677 1308 -603 404 N ATOM 1599 N LEU A 208 -3.882 -34.342 18.141 1.00 43.56 N ANISOU 1599 N LEU A 208 6331 3475 6746 1999 -159 -130 N ATOM 1600 CA LEU A 208 -3.608 -35.010 16.874 1.00 47.72 C ANISOU 1600 CA LEU A 208 6919 3911 7303 2094 -35 -260 C ATOM 1601 C LEU A 208 -2.214 -35.629 16.862 1.00 47.48 C ANISOU 1601 C LEU A 208 6793 3796 7452 2326 -32 -302 C ATOM 1602 O LEU A 208 -2.028 -36.735 16.358 1.00 47.14 O ANISOU 1602 O LEU A 208 6870 3583 7456 2435 -8 -372 O ATOM 1603 CB LEU A 208 -3.756 -34.031 15.710 1.00 52.62 C ANISOU 1603 CB LEU A 208 7461 4684 7847 2028 129 -348 C ATOM 1604 CG LEU A 208 -5.182 -33.803 15.210 1.00 56.99 C ANISOU 1604 CG LEU A 208 8161 5264 8228 1833 156 -357 C ATOM 1605 CD1 LEU A 208 -5.225 -32.617 14.267 1.00 58.52 C ANISOU 1605 CD1 LEU A 208 8250 5633 8350 1771 293 -417 C ATOM 1606 CD2 LEU A 208 -5.699 -35.054 14.519 1.00 59.78 C ANISOU 1606 CD2 LEU A 208 8735 5432 8547 1843 170 -430 C ATOM 1607 N ALA A1001 -1.282 -34.870 17.485 1.00 67.65 N ANISOU 1607 N ALA A1001 8893 4376 12434 401 1673 -424 N ATOM 1608 CA ALA A1001 0.105 -35.229 17.760 1.00 66.36 C ANISOU 1608 CA ALA A1001 8619 4314 12280 212 1714 -579 C ATOM 1609 C ALA A1001 0.182 -36.485 18.621 1.00 63.99 C ANISOU 1609 C ALA A1001 8106 4277 11929 226 1558 -658 C ATOM 1610 O ALA A1001 0.998 -37.368 18.366 1.00 64.69 O ANISOU 1610 O ALA A1001 8097 4507 11974 156 1521 -685 O ATOM 1611 CB ALA A1001 0.833 -34.077 18.434 1.00 65.12 C ANISOU 1611 CB ALA A1001 8501 4020 12223 60 1861 -745 C ATOM 1612 N ASP A1002 -0.673 -36.559 19.645 1.00 63.07 N ANISOU 1612 N ASP A1002 7928 4220 11816 325 1479 -691 N ATOM 1613 CA ASP A1002 -0.704 -37.745 20.496 1.00 61.32 C ANISOU 1613 CA ASP A1002 7529 4235 11535 349 1333 -754 C ATOM 1614 C ASP A1002 -1.251 -38.950 19.743 1.00 58.13 C ANISOU 1614 C ASP A1002 7093 3956 11035 451 1198 -597 C ATOM 1615 O ASP A1002 -0.816 -40.083 19.974 1.00 61.03 O ANISOU 1615 O ASP A1002 7343 4508 11336 427 1101 -637 O ATOM 1616 CB ASP A1002 -1.537 -37.477 21.749 1.00 66.40 C ANISOU 1616 CB ASP A1002 8139 4892 12198 432 1306 -819 C ATOM 1617 CG ASP A1002 -0.993 -36.332 22.577 1.00 72.43 C ANISOU 1617 CG ASP A1002 8957 5527 13035 325 1428 -990 C ATOM 1618 OD1 ASP A1002 0.231 -36.090 22.530 1.00 74.49 O ANISOU 1618 OD1 ASP A1002 9202 5775 13328 152 1485 -1106 O ATOM 1619 OD2 ASP A1002 -1.791 -35.672 23.275 1.00 75.04 O ANISOU 1619 OD2 ASP A1002 9349 5767 13395 411 1469 -1009 O ATOM 1620 N LEU A1003 -2.215 -38.731 18.847 1.00 58.38 N ANISOU 1620 N LEU A1003 7239 3887 11055 566 1182 -417 N ATOM 1621 CA LEU A1003 -2.733 -39.837 18.051 1.00 57.25 C ANISOU 1621 CA LEU A1003 7091 3847 10815 644 1043 -266 C ATOM 1622 C LEU A1003 -1.690 -40.351 17.073 1.00 64.59 C ANISOU 1622 C LEU A1003 8068 4793 11680 552 1071 -253 C ATOM 1623 O LEU A1003 -1.644 -41.554 16.794 1.00 63.00 O ANISOU 1623 O LEU A1003 7822 4733 11383 570 958 -210 O ATOM 1624 CB LEU A1003 -3.991 -39.406 17.303 1.00 63.02 C ANISOU 1624 CB LEU A1003 7932 4460 11551 784 1004 -76 C ATOM 1625 CG LEU A1003 -5.226 -39.147 18.163 1.00 63.08 C ANISOU 1625 CG LEU A1003 7865 4484 11618 914 958 -49 C ATOM 1626 CD1 LEU A1003 -6.332 -38.551 17.319 1.00 64.11 C ANISOU 1626 CD1 LEU A1003 8103 4481 11775 1052 934 143 C ATOM 1627 CD2 LEU A1003 -5.688 -40.434 18.824 1.00 56.51 C ANISOU 1627 CD2 LEU A1003 6871 3873 10728 947 805 -52 C ATOM 1628 N GLU A1004 -0.849 -39.464 16.546 1.00 67.30 N ANISOU 1628 N GLU A1004 8511 4988 12073 454 1233 -288 N ATOM 1629 CA GLU A1004 0.213 -39.887 15.646 1.00 69.99 C ANISOU 1629 CA GLU A1004 8891 5340 12364 364 1297 -282 C ATOM 1630 C GLU A1004 1.406 -40.473 16.389 1.00 67.23 C ANISOU 1630 C GLU A1004 8362 5150 12032 251 1310 -452 C ATOM 1631 O GLU A1004 2.134 -41.287 15.814 1.00 68.67 O ANISOU 1631 O GLU A1004 8524 5416 12152 220 1313 -440 O ATOM 1632 CB GLU A1004 0.664 -38.711 14.776 1.00 78.03 C ANISOU 1632 CB GLU A1004 10084 6132 13430 293 1482 -246 C ATOM 1633 CG GLU A1004 1.452 -39.112 13.538 1.00 84.76 C ANISOU 1633 CG GLU A1004 11037 6960 14209 240 1560 -177 C ATOM 1634 CD GLU A1004 0.703 -40.097 12.657 1.00 88.45 C ANISOU 1634 CD GLU A1004 11598 7476 14531 362 1415 -10 C ATOM 1635 OE1 GLU A1004 0.989 -41.311 12.741 1.00 88.88 O ANISOU 1635 OE1 GLU A1004 11558 7704 14510 370 1323 -31 O ATOM 1636 OE2 GLU A1004 -0.177 -39.660 11.885 1.00 91.02 O ANISOU 1636 OE2 GLU A1004 12102 7664 14816 451 1385 143 O ATOM 1637 N ASP A1005 1.618 -40.090 17.651 1.00 65.16 N ANISOU 1637 N ASP A1005 7976 4932 11848 198 1313 -608 N ATOM 1638 CA ASP A1005 2.725 -40.658 18.414 1.00 64.37 C ANISOU 1638 CA ASP A1005 7696 4996 11764 99 1295 -768 C ATOM 1639 C ASP A1005 2.425 -42.091 18.834 1.00 60.17 C ANISOU 1639 C ASP A1005 7057 4674 11130 191 1121 -755 C ATOM 1640 O ASP A1005 3.253 -42.989 18.645 1.00 57.55 O ANISOU 1640 O ASP A1005 6644 4469 10754 164 1098 -782 O ATOM 1641 CB ASP A1005 3.030 -39.787 19.633 1.00 70.05 C ANISOU 1641 CB ASP A1005 8345 5689 12582 8 1335 -941 C ATOM 1642 CG ASP A1005 3.777 -38.517 19.270 1.00 77.26 C ANISOU 1642 CG ASP A1005 9336 6419 13602 -139 1519 -996 C ATOM 1643 OD1 ASP A1005 4.075 -38.319 18.072 1.00 78.82 O ANISOU 1643 OD1 ASP A1005 9637 6513 13797 -165 1626 -896 O ATOM 1644 OD2 ASP A1005 4.067 -37.715 20.184 1.00 80.48 O ANISOU 1644 OD2 ASP A1005 9715 6777 14088 -235 1559 -1140 O ATOM 1645 N ASN A1006 1.241 -42.324 19.407 1.00 59.28 N ANISOU 1645 N ASN A1006 6945 4596 10981 302 1007 -709 N ATOM 1646 CA ASN A1006 0.876 -43.675 19.818 1.00 58.91 C ANISOU 1646 CA ASN A1006 6815 4734 10836 380 847 -688 C ATOM 1647 C ASN A1006 0.797 -44.614 18.621 1.00 56.58 C ANISOU 1647 C ASN A1006 6598 4463 10436 429 796 -545 C ATOM 1648 O ASN A1006 1.189 -45.783 18.714 1.00 52.24 O ANISOU 1648 O ASN A1006 5987 4057 9804 443 714 -562 O ATOM 1649 CB ASN A1006 -0.448 -43.650 20.583 1.00 60.26 C ANISOU 1649 CB ASN A1006 6977 4919 11001 481 761 -650 C ATOM 1650 CG ASN A1006 -0.294 -43.097 21.987 1.00 63.71 C ANISOU 1650 CG ASN A1006 7333 5377 11496 443 786 -814 C ATOM 1651 OD1 ASN A1006 0.738 -43.289 22.627 1.00 65.84 O ANISOU 1651 OD1 ASN A1006 7510 5735 11770 355 784 -960 O ATOM 1652 ND2 ASN A1006 -1.318 -42.408 22.471 1.00 54.12 N ANISOU 1652 ND2 ASN A1006 6159 4081 10325 513 807 -790 N ATOM 1653 N TRP A1007 0.304 -44.117 17.483 1.00 57.74 N ANISOU 1653 N TRP A1007 6903 4461 10576 459 843 -405 N ATOM 1654 CA TRP A1007 0.256 -44.929 16.271 1.00 57.00 C ANISOU 1654 CA TRP A1007 6923 4367 10368 497 799 -271 C ATOM 1655 C TRP A1007 1.657 -45.296 15.797 1.00 61.30 C ANISOU 1655 C TRP A1007 7454 4945 10892 419 901 -334 C ATOM 1656 O TRP A1007 1.906 -46.440 15.397 1.00 58.39 O ANISOU 1656 O TRP A1007 7102 4669 10416 451 839 -298 O ATOM 1657 CB TRP A1007 -0.508 -44.184 15.177 1.00 54.22 C ANISOU 1657 CB TRP A1007 6757 3834 10009 541 829 -113 C ATOM 1658 CG TRP A1007 -0.458 -44.833 13.824 1.00 57.75 C ANISOU 1658 CG TRP A1007 7369 4245 10329 564 804 19 C ATOM 1659 CD1 TRP A1007 0.326 -44.468 12.768 1.00 57.63 C ANISOU 1659 CD1 TRP A1007 7494 4112 10289 512 949 51 C ATOM 1660 CD2 TRP A1007 -1.233 -45.954 13.377 1.00 58.65 C ANISOU 1660 CD2 TRP A1007 7544 4430 10311 637 629 137 C ATOM 1661 NE1 TRP A1007 0.088 -45.291 11.694 1.00 55.17 N ANISOU 1661 NE1 TRP A1007 7342 3791 9828 559 875 180 N ATOM 1662 CE2 TRP A1007 -0.863 -46.213 12.043 1.00 58.89 C ANISOU 1662 CE2 TRP A1007 7769 4375 10231 631 670 232 C ATOM 1663 CE3 TRP A1007 -2.201 -46.766 13.978 1.00 57.62 C ANISOU 1663 CE3 TRP A1007 7330 4420 10142 699 446 171 C ATOM 1664 CZ2 TRP A1007 -1.426 -47.248 11.299 1.00 58.61 C ANISOU 1664 CZ2 TRP A1007 7860 4368 10042 681 521 352 C ATOM 1665 CZ3 TRP A1007 -2.760 -47.792 13.238 1.00 56.97 C ANISOU 1665 CZ3 TRP A1007 7354 4369 9921 738 298 294 C ATOM 1666 CH2 TRP A1007 -2.372 -48.024 11.913 1.00 57.62 C ANISOU 1666 CH2 TRP A1007 7643 4361 9888 728 329 380 C ATOM 1667 N GLU A1008 2.587 -44.341 15.839 1.00 66.07 N ANISOU 1667 N GLU A1008 8028 5472 11603 314 1066 -428 N ATOM 1668 CA GLU A1008 3.965 -44.648 15.476 1.00 70.28 C ANISOU 1668 CA GLU A1008 8504 6052 12145 235 1178 -494 C ATOM 1669 C GLU A1008 4.655 -45.476 16.551 1.00 71.68 C ANISOU 1669 C GLU A1008 8471 6434 12332 223 1100 -633 C ATOM 1670 O GLU A1008 5.501 -46.316 16.231 1.00 73.88 O ANISOU 1670 O GLU A1008 8699 6806 12566 226 1120 -647 O ATOM 1671 CB GLU A1008 4.738 -43.359 15.209 1.00 75.70 C ANISOU 1671 CB GLU A1008 9209 6595 12956 108 1378 -549 C ATOM 1672 CG GLU A1008 4.323 -42.661 13.924 1.00 80.79 C ANISOU 1672 CG GLU A1008 10093 7034 13571 121 1483 -401 C ATOM 1673 CD GLU A1008 4.989 -41.313 13.746 1.00 87.03 C ANISOU 1673 CD GLU A1008 10919 7660 14486 -11 1686 -455 C ATOM 1674 OE1 GLU A1008 5.827 -40.947 14.597 1.00 90.04 O ANISOU 1674 OE1 GLU A1008 11128 8098 14983 -128 1741 -613 O ATOM 1675 OE2 GLU A1008 4.671 -40.619 12.756 1.00 89.56 O ANISOU 1675 OE2 GLU A1008 11451 7792 14785 -4 1784 -338 O ATOM 1676 N THR A1009 4.309 -45.259 17.822 1.00 71.16 N ANISOU 1676 N THR A1009 8291 6432 12316 218 1013 -732 N ATOM 1677 CA THR A1009 4.849 -46.101 18.885 1.00 66.87 C ANISOU 1677 CA THR A1009 7571 6081 11757 223 912 -853 C ATOM 1678 C THR A1009 4.415 -47.549 18.704 1.00 63.48 C ANISOU 1678 C THR A1009 7173 5766 11182 339 775 -769 C ATOM 1679 O THR A1009 5.193 -48.478 18.956 1.00 64.15 O ANISOU 1679 O THR A1009 7159 5988 11225 357 735 -825 O ATOM 1680 CB THR A1009 4.404 -45.574 20.250 1.00 64.43 C ANISOU 1680 CB THR A1009 7183 5797 11501 206 845 -962 C ATOM 1681 OG1 THR A1009 4.929 -44.255 20.445 1.00 64.81 O ANISOU 1681 OG1 THR A1009 7213 5732 11678 82 972 -1057 O ATOM 1682 CG2 THR A1009 4.897 -46.484 21.367 1.00 63.23 C ANISOU 1682 CG2 THR A1009 6875 5841 11310 221 722 -1078 C ATOM 1683 N LEU A1010 3.181 -47.760 18.252 1.00 62.79 N ANISOU 1683 N LEU A1010 7223 5618 11017 419 699 -632 N ATOM 1684 CA LEU A1010 2.694 -49.115 18.022 1.00 50.55 C ANISOU 1684 CA LEU A1010 5727 4156 9324 509 564 -545 C ATOM 1685 C LEU A1010 3.478 -49.798 16.906 1.00 50.84 C ANISOU 1685 C LEU A1010 5848 4188 9283 520 626 -491 C ATOM 1686 O LEU A1010 3.916 -50.943 17.054 1.00 50.34 O ANISOU 1686 O LEU A1010 5751 4241 9135 567 565 -512 O ATOM 1687 CB LEU A1010 1.203 -49.075 17.697 1.00 50.02 C ANISOU 1687 CB LEU A1010 5778 4017 9210 571 470 -404 C ATOM 1688 CG LEU A1010 0.482 -50.414 17.580 1.00 59.57 C ANISOU 1688 CG LEU A1010 7045 5310 10280 644 310 -312 C ATOM 1689 CD1 LEU A1010 0.267 -51.020 18.954 1.00 59.32 C ANISOU 1689 CD1 LEU A1010 6880 5422 10238 666 207 -399 C ATOM 1690 CD2 LEU A1010 -0.837 -50.233 16.853 1.00 59.20 C ANISOU 1690 CD2 LEU A1010 7126 5166 10201 683 235 -150 C ATOM 1691 N ASN A1011 3.681 -49.099 15.787 1.00 54.44 N ANISOU 1691 N ASN A1011 6427 4499 9759 484 759 -422 N ATOM 1692 CA ASN A1011 4.356 -49.671 14.625 1.00 55.71 C ANISOU 1692 CA ASN A1011 6705 4630 9834 500 845 -359 C ATOM 1693 C ASN A1011 5.857 -49.823 14.829 1.00 55.52 C ANISOU 1693 C ASN A1011 6525 4692 9876 457 969 -477 C ATOM 1694 O ASN A1011 6.451 -50.778 14.314 1.00 53.89 O ANISOU 1694 O ASN A1011 6356 4539 9582 510 995 -455 O ATOM 1695 CB ASN A1011 4.101 -48.813 13.386 1.00 58.29 C ANISOU 1695 CB ASN A1011 7228 4764 10154 474 959 -245 C ATOM 1696 CG ASN A1011 2.649 -48.814 12.975 1.00 60.82 C ANISOU 1696 CG ASN A1011 7710 5006 10394 535 819 -103 C ATOM 1697 OD1 ASN A1011 1.942 -49.803 13.160 1.00 61.19 O ANISOU 1697 OD1 ASN A1011 7778 5132 10339 598 651 -55 O ATOM 1698 ND2 ASN A1011 2.193 -47.701 12.407 1.00 63.36 N ANISOU 1698 ND2 ASN A1011 8145 5166 10762 514 886 -31 N ATOM 1699 N ASP A1012 6.493 -48.892 15.543 1.00 57.62 N ANISOU 1699 N ASP A1012 6622 4973 10299 362 1049 -601 N ATOM 1700 CA ASP A1012 7.929 -49.008 15.766 1.00 63.16 C ANISOU 1700 CA ASP A1012 7141 5772 11085 310 1154 -713 C ATOM 1701 C ASP A1012 8.251 -50.194 16.664 1.00 65.19 C ANISOU 1701 C ASP A1012 7254 6224 11290 387 1013 -785 C ATOM 1702 O ASP A1012 9.194 -50.946 16.392 1.00 70.45 O ANISOU 1702 O ASP A1012 7855 6975 11936 429 1065 -802 O ATOM 1703 CB ASP A1012 8.478 -47.716 16.365 1.00 68.33 C ANISOU 1703 CB ASP A1012 7652 6392 11918 169 1248 -832 C ATOM 1704 CG ASP A1012 8.351 -46.539 15.419 1.00 73.80 C ANISOU 1704 CG ASP A1012 8496 6880 12665 89 1418 -762 C ATOM 1705 OD1 ASP A1012 7.945 -46.750 14.256 1.00 74.92 O ANISOU 1705 OD1 ASP A1012 8847 6917 12704 146 1467 -622 O ATOM 1706 OD2 ASP A1012 8.647 -45.401 15.841 1.00 77.69 O ANISOU 1706 OD2 ASP A1012 8917 7307 13294 -34 1498 -847 O ATOM 1707 N ASN A1013 7.478 -50.383 17.736 1.00 63.94 N ANISOU 1707 N ASN A1013 7054 6133 11107 417 843 -824 N ATOM 1708 CA ASN A1013 7.727 -51.514 18.621 1.00 63.63 C ANISOU 1708 CA ASN A1013 6906 6267 11003 495 703 -886 C ATOM 1709 C ASN A1013 7.435 -52.842 17.934 1.00 60.65 C ANISOU 1709 C ASN A1013 6679 5908 10458 615 646 -776 C ATOM 1710 O ASN A1013 7.999 -53.871 18.322 1.00 61.13 O ANISOU 1710 O ASN A1013 6669 6095 10461 690 586 -815 O ATOM 1711 CB ASN A1013 6.900 -51.380 19.897 1.00 67.12 C ANISOU 1711 CB ASN A1013 7301 6759 11444 496 553 -944 C ATOM 1712 CG ASN A1013 7.468 -50.356 20.858 1.00 73.01 C ANISOU 1712 CG ASN A1013 7878 7529 12332 388 581 -1094 C ATOM 1713 OD1 ASN A1013 8.685 -50.223 20.993 1.00 76.31 O ANISOU 1713 OD1 ASN A1013 8139 8017 12838 332 641 -1189 O ATOM 1714 ND2 ASN A1013 6.587 -49.628 21.537 1.00 73.49 N ANISOU 1714 ND2 ASN A1013 7971 7533 12420 358 537 -1117 N ATOM 1715 N LEU A1014 6.561 -52.846 16.924 1.00 58.46 N ANISOU 1715 N LEU A1014 6619 5501 10094 635 656 -638 N ATOM 1716 CA LEU A1014 6.353 -54.060 16.140 1.00 55.27 C ANISOU 1716 CA LEU A1014 6389 5091 9521 730 612 -535 C ATOM 1717 C LEU A1014 7.623 -54.456 15.399 1.00 57.16 C ANISOU 1717 C LEU A1014 6622 5344 9754 760 765 -546 C ATOM 1718 O LEU A1014 7.971 -55.641 15.336 1.00 58.44 O ANISOU 1718 O LEU A1014 6820 5577 9809 857 728 -537 O ATOM 1719 CB LEU A1014 5.196 -53.869 15.159 1.00 55.74 C ANISOU 1719 CB LEU A1014 6684 5000 9493 728 582 -387 C ATOM 1720 CG LEU A1014 3.777 -53.958 15.725 1.00 54.55 C ANISOU 1720 CG LEU A1014 6568 4854 9306 738 403 -336 C ATOM 1721 CD1 LEU A1014 2.743 -53.722 14.635 1.00 55.31 C ANISOU 1721 CD1 LEU A1014 6879 4807 9330 737 371 -183 C ATOM 1722 CD2 LEU A1014 3.555 -55.306 16.386 1.00 53.86 C ANISOU 1722 CD2 LEU A1014 6473 4886 9105 808 252 -347 C ATOM 1723 N LYS A1015 8.333 -53.476 14.832 1.00 57.23 N ANISOU 1723 N LYS A1015 6588 5280 9877 681 953 -564 N ATOM 1724 CA LYS A1015 9.597 -53.771 14.166 1.00 56.92 C ANISOU 1724 CA LYS A1015 6510 5261 9856 705 1129 -577 C ATOM 1725 C LYS A1015 10.642 -54.257 15.162 1.00 54.99 C ANISOU 1725 C LYS A1015 5997 5204 9695 738 1102 -705 C ATOM 1726 O LYS A1015 11.435 -55.151 14.847 1.00 55.65 O ANISOU 1726 O LYS A1015 6062 5352 9730 833 1162 -701 O ATOM 1727 CB LYS A1015 10.104 -52.534 13.426 1.00 56.01 C ANISOU 1727 CB LYS A1015 6395 5024 9861 593 1345 -570 C ATOM 1728 CG LYS A1015 9.100 -51.932 12.462 1.00 64.46 C ANISOU 1728 CG LYS A1015 7733 5903 10856 564 1367 -442 C ATOM 1729 CD LYS A1015 9.652 -50.677 11.804 1.00 66.25 C ANISOU 1729 CD LYS A1015 7968 6003 11202 450 1590 -439 C ATOM 1730 CE LYS A1015 8.589 -49.981 10.966 1.00 67.55 C ANISOU 1730 CE LYS A1015 8396 5973 11295 430 1588 -313 C ATOM 1731 NZ LYS A1015 8.086 -50.855 9.870 1.00 68.39 N ANISOU 1731 NZ LYS A1015 8787 6005 11191 528 1555 -177 N ATOM 1732 N VAL A1016 10.653 -53.684 16.369 1.00 54.81 N ANISOU 1732 N VAL A1016 5772 5265 9789 668 1010 -816 N ATOM 1733 CA VAL A1016 11.616 -54.092 17.390 1.00 66.15 C ANISOU 1733 CA VAL A1016 6950 6883 11300 694 952 -940 C ATOM 1734 C VAL A1016 11.428 -55.561 17.748 1.00 70.39 C ANISOU 1734 C VAL A1016 7546 7519 11682 850 804 -917 C ATOM 1735 O VAL A1016 12.402 -56.306 17.913 1.00 73.91 O ANISOU 1735 O VAL A1016 7865 8083 12133 938 819 -957 O ATOM 1736 CB VAL A1016 11.493 -53.189 18.633 1.00 63.88 C ANISOU 1736 CB VAL A1016 6491 6645 11135 584 856 -1061 C ATOM 1737 CG1 VAL A1016 12.449 -53.650 19.724 1.00 56.12 C ANISOU 1737 CG1 VAL A1016 5256 5855 10211 613 762 -1187 C ATOM 1738 CG2 VAL A1016 11.748 -51.731 18.271 1.00 56.55 C ANISOU 1738 CG2 VAL A1016 5521 5603 10362 422 1013 -1089 C ATOM 1739 N ILE A1017 10.174 -56.000 17.870 1.00 69.72 N ANISOU 1739 N ILE A1017 7648 7383 11457 888 662 -847 N ATOM 1740 CA ILE A1017 9.899 -57.387 18.230 1.00 69.49 C ANISOU 1740 CA ILE A1017 7703 7429 11271 1020 520 -820 C ATOM 1741 C ILE A1017 10.344 -58.330 17.118 1.00 72.31 C ANISOU 1741 C ILE A1017 8216 7745 11514 1128 618 -736 C ATOM 1742 O ILE A1017 10.846 -59.429 17.381 1.00 73.53 O ANISOU 1742 O ILE A1017 8358 7989 11592 1253 573 -751 O ATOM 1743 CB ILE A1017 8.404 -57.559 18.560 1.00 65.37 C ANISOU 1743 CB ILE A1017 7341 6854 10643 1010 362 -757 C ATOM 1744 CG1 ILE A1017 8.026 -56.714 19.779 1.00 60.65 C ANISOU 1744 CG1 ILE A1017 6591 6305 10149 927 278 -850 C ATOM 1745 CG2 ILE A1017 8.068 -59.023 18.807 1.00 65.94 C ANISOU 1745 CG2 ILE A1017 7535 6976 10541 1128 229 -715 C ATOM 1746 CD1 ILE A1017 6.544 -56.673 20.062 1.00 54.80 C ANISOU 1746 CD1 ILE A1017 5977 5504 9338 908 161 -783 C ATOM 1747 N GLU A1018 10.183 -57.910 15.861 1.00 73.17 N ANISOU 1747 N GLU A1018 8491 7708 11601 1090 758 -647 N ATOM 1748 CA GLU A1018 10.496 -58.789 14.738 1.00 74.44 C ANISOU 1748 CA GLU A1018 8855 7804 11626 1191 858 -562 C ATOM 1749 C GLU A1018 11.989 -59.082 14.660 1.00 78.65 C ANISOU 1749 C GLU A1018 9211 8433 12240 1267 1013 -622 C ATOM 1750 O GLU A1018 12.396 -60.234 14.472 1.00 79.70 O ANISOU 1750 O GLU A1018 9420 8600 12261 1411 1019 -601 O ATOM 1751 CB GLU A1018 10.001 -58.165 13.436 1.00 74.31 C ANISOU 1751 CB GLU A1018 9066 7606 11564 1125 974 -456 C ATOM 1752 CG GLU A1018 8.494 -58.072 13.347 1.00 74.55 C ANISOU 1752 CG GLU A1018 9290 7541 11494 1078 810 -371 C ATOM 1753 CD GLU A1018 8.035 -57.307 12.131 1.00 77.70 C ANISOU 1753 CD GLU A1018 9893 7766 11864 1012 908 -269 C ATOM 1754 OE1 GLU A1018 8.895 -56.756 11.414 1.00 81.49 O ANISOU 1754 OE1 GLU A1018 10364 8192 12407 989 1119 -272 O ATOM 1755 OE2 GLU A1018 6.812 -57.256 11.892 1.00 78.17 O ANISOU 1755 OE2 GLU A1018 10120 7743 11838 984 774 -183 O ATOM 1756 N LYS A1019 12.823 -58.052 14.800 1.00 80.50 N ANISOU 1756 N LYS A1019 9205 8708 12673 1174 1143 -697 N ATOM 1757 CA LYS A1019 14.269 -58.208 14.710 1.00 83.96 C ANISOU 1757 CA LYS A1019 9429 9249 13225 1229 1302 -752 C ATOM 1758 C LYS A1019 14.928 -58.313 16.081 1.00 84.52 C ANISOU 1758 C LYS A1019 9179 9518 13418 1245 1173 -878 C ATOM 1759 O LYS A1019 16.095 -57.943 16.241 1.00 86.71 O ANISOU 1759 O LYS A1019 9183 9896 13867 1221 1281 -950 O ATOM 1760 CB LYS A1019 14.876 -57.061 13.905 1.00 86.90 C ANISOU 1760 CB LYS A1019 9735 9540 13743 1105 1544 -747 C ATOM 1761 CG LYS A1019 14.472 -55.682 14.383 1.00 87.19 C ANISOU 1761 CG LYS A1019 9671 9539 13920 918 1511 -800 C ATOM 1762 CD LYS A1019 14.579 -54.669 13.257 1.00 89.56 C ANISOU 1762 CD LYS A1019 10078 9675 14274 806 1740 -741 C ATOM 1763 CE LYS A1019 13.743 -55.094 12.057 1.00 88.88 C ANISOU 1763 CE LYS A1019 10372 9418 13979 872 1776 -597 C ATOM 1764 NZ LYS A1019 13.881 -54.145 10.917 1.00 91.01 N ANISOU 1764 NZ LYS A1019 10777 9522 14282 776 2005 -530 N ATOM 1765 N ALA A1020 14.201 -58.812 17.076 1.00 84.46 N ANISOU 1765 N ALA A1020 9198 9568 13323 1282 941 -904 N ATOM 1766 CA ALA A1020 14.795 -59.110 18.367 1.00 88.87 C ANISOU 1766 CA ALA A1020 9504 10312 13952 1326 798 -1014 C ATOM 1767 C ALA A1020 15.445 -60.489 18.338 1.00102.97 C ANISOU 1767 C ALA A1020 11298 12183 15641 1533 786 -993 C ATOM 1768 O ALA A1020 15.213 -61.296 17.433 1.00 97.98 O ANISOU 1768 O ALA A1020 10914 11457 14859 1640 858 -895 O ATOM 1769 CB ALA A1020 13.749 -59.038 19.478 1.00 81.24 C ANISOU 1769 CB ALA A1020 8580 9363 12924 1280 571 -1050 C ATOM 1770 N ASP A1021 16.274 -60.758 19.346 1.00125.76 N ANISOU 1770 N ASP A1021 13924 15247 18611 1595 688 -1087 N ATOM 1771 CA ASP A1021 16.992 -62.022 19.416 1.00132.26 C ANISOU 1771 CA ASP A1021 14726 16165 19364 1810 673 -1072 C ATOM 1772 C ASP A1021 16.842 -62.754 20.740 1.00125.07 C ANISOU 1772 C ASP A1021 13771 15377 18375 1904 424 -1127 C ATOM 1773 O ASP A1021 17.236 -63.923 20.817 1.00131.66 O ANISOU 1773 O ASP A1021 14652 16263 19109 2101 390 -1100 O ATOM 1774 CB ASP A1021 18.488 -61.807 19.140 1.00141.73 C ANISOU 1774 CB ASP A1021 15620 17477 20754 1850 840 -1114 C ATOM 1775 CG ASP A1021 19.149 -60.926 20.178 1.00148.79 C ANISOU 1775 CG ASP A1021 16151 18527 21856 1726 746 -1243 C ATOM 1776 OD1 ASP A1021 18.454 -60.065 20.759 1.00149.96 O ANISOU 1776 OD1 ASP A1021 16307 18640 22031 1556 640 -1294 O ATOM 1777 OD2 ASP A1021 20.364 -61.097 20.416 1.00153.26 O ANISOU 1777 OD2 ASP A1021 16425 19248 22559 1801 777 -1291 O ATOM 1778 N ASN A1022 16.293 -62.122 21.775 1.00106.88 N ANISOU 1778 N ASN A1022 11397 13110 16102 1779 259 -1200 N ATOM 1779 CA ASN A1022 16.109 -62.774 23.063 1.00 92.18 C ANISOU 1779 CA ASN A1022 9520 11355 14151 1859 28 -1251 C ATOM 1780 C ASN A1022 14.727 -62.437 23.603 1.00 84.48 C ANISOU 1780 C ASN A1022 8724 10294 13079 1744 -95 -1246 C ATOM 1781 O ASN A1022 14.007 -61.598 23.057 1.00 83.86 O ANISOU 1781 O ASN A1022 8735 10094 13033 1602 -14 -1214 O ATOM 1782 CB ASN A1022 17.194 -62.362 24.065 1.00 85.43 C ANISOU 1782 CB ASN A1022 8315 10687 13457 1845 -64 -1376 C ATOM 1783 CG ASN A1022 17.260 -60.866 24.266 1.00 78.38 C ANISOU 1783 CG ASN A1022 7245 9791 12746 1615 -30 -1461 C ATOM 1784 OD1 ASN A1022 16.615 -60.319 25.160 1.00 75.06 O ANISOU 1784 OD1 ASN A1022 6843 9366 12309 1506 -165 -1524 O ATOM 1785 ND2 ASN A1022 18.039 -60.191 23.428 1.00 77.35 N ANISOU 1785 ND2 ASN A1022 6955 9650 12786 1541 166 -1463 N ATOM 1786 N ALA A1023 14.365 -63.104 24.698 1.00 80.90 N ANISOU 1786 N ALA A1023 8323 9907 12509 1816 -288 -1273 N ATOM 1787 CA ALA A1023 13.059 -62.906 25.311 1.00 76.56 C ANISOU 1787 CA ALA A1023 7936 9290 11862 1726 -399 -1264 C ATOM 1788 C ALA A1023 12.953 -61.609 26.099 1.00 77.17 C ANISOU 1788 C ALA A1023 7851 9400 12072 1557 -442 -1370 C ATOM 1789 O ALA A1023 11.844 -61.245 26.507 1.00 80.13 O ANISOU 1789 O ALA A1023 8349 9704 12393 1472 -495 -1361 O ATOM 1790 CB ALA A1023 12.725 -64.082 26.233 1.00 75.88 C ANISOU 1790 CB ALA A1023 7978 9255 11597 1857 -573 -1255 C ATOM 1791 N ALA A1024 14.061 -60.903 26.335 1.00 75.66 N ANISOU 1791 N ALA A1024 7389 9308 12052 1504 -419 -1469 N ATOM 1792 CA ALA A1024 13.971 -59.669 27.109 1.00 74.03 C ANISOU 1792 CA ALA A1024 7054 9117 11958 1334 -465 -1578 C ATOM 1793 C ALA A1024 13.671 -58.465 26.225 1.00 75.50 C ANISOU 1793 C ALA A1024 7247 9169 12268 1171 -292 -1558 C ATOM 1794 O ALA A1024 13.014 -57.521 26.677 1.00 75.96 O ANISOU 1794 O ALA A1024 7335 9166 12362 1038 -310 -1603 O ATOM 1795 CB ALA A1024 15.262 -59.442 27.898 1.00 73.41 C ANISOU 1795 CB ALA A1024 6684 9207 12000 1330 -554 -1704 C ATOM 1796 N GLN A1025 14.133 -58.482 24.971 1.00 71.46 N ANISOU 1796 N GLN A1025 6730 8605 11817 1186 -115 -1487 N ATOM 1797 CA GLN A1025 13.843 -57.382 24.056 1.00 68.40 C ANISOU 1797 CA GLN A1025 6381 8077 11530 1041 56 -1454 C ATOM 1798 C GLN A1025 12.376 -57.373 23.645 1.00 65.03 C ANISOU 1798 C GLN A1025 6232 7497 10980 1026 59 -1352 C ATOM 1799 O GLN A1025 11.776 -56.304 23.482 1.00 63.10 O ANISOU 1799 O GLN A1025 6030 7144 10800 896 117 -1352 O ATOM 1800 CB GLN A1025 14.741 -57.478 22.825 1.00 71.48 C ANISOU 1800 CB GLN A1025 6712 8449 11997 1072 254 -1400 C ATOM 1801 CG GLN A1025 16.215 -57.312 23.123 1.00 76.72 C ANISOU 1801 CG GLN A1025 7058 9264 12827 1064 280 -1495 C ATOM 1802 CD GLN A1025 17.070 -57.444 21.882 1.00 82.53 C ANISOU 1802 CD GLN A1025 7739 9980 13639 1106 504 -1431 C ATOM 1803 OE1 GLN A1025 16.574 -57.776 20.805 1.00 83.77 O ANISOU 1803 OE1 GLN A1025 8128 10006 13695 1158 629 -1316 O ATOM 1804 NE2 GLN A1025 18.365 -57.185 22.025 1.00 85.80 N ANISOU 1804 NE2 GLN A1025 7846 10524 14231 1079 558 -1505 N ATOM 1805 N VAL A1026 11.787 -58.554 23.457 1.00 63.62 N ANISOU 1805 N VAL A1026 6243 7303 10627 1157 -5 -1261 N ATOM 1806 CA VAL A1026 10.370 -58.630 23.124 1.00 62.17 C ANISOU 1806 CA VAL A1026 6301 6991 10330 1138 -29 -1160 C ATOM 1807 C VAL A1026 9.525 -58.116 24.281 1.00 64.70 C ANISOU 1807 C VAL A1026 6613 7322 10648 1068 -149 -1218 C ATOM 1808 O VAL A1026 8.532 -57.409 24.077 1.00 67.07 O ANISOU 1808 O VAL A1026 7008 7513 10963 986 -121 -1174 O ATOM 1809 CB VAL A1026 9.993 -60.072 22.740 1.00 63.74 C ANISOU 1809 CB VAL A1026 6700 7176 10342 1279 -83 -1060 C ATOM 1810 CG1 VAL A1026 8.537 -60.150 22.313 1.00 63.16 C ANISOU 1810 CG1 VAL A1026 6858 6974 10164 1241 -115 -950 C ATOM 1811 CG2 VAL A1026 10.913 -60.579 21.637 1.00 65.54 C ANISOU 1811 CG2 VAL A1026 6945 7391 10566 1364 53 -1013 C ATOM 1812 N LYS A1027 9.914 -58.448 25.515 1.00 66.16 N ANISOU 1812 N LYS A1027 6691 7635 10811 1108 -281 -1315 N ATOM 1813 CA LYS A1027 9.161 -57.990 26.678 1.00 67.73 C ANISOU 1813 CA LYS A1027 6901 7843 10992 1050 -383 -1377 C ATOM 1814 C LYS A1027 9.216 -56.474 26.812 1.00 74.62 C ANISOU 1814 C LYS A1027 7671 8661 12022 897 -308 -1456 C ATOM 1815 O LYS A1027 8.226 -55.842 27.200 1.00 73.05 O ANISOU 1815 O LYS A1027 7551 8387 11820 836 -314 -1454 O ATOM 1816 CB LYS A1027 9.692 -58.661 27.945 1.00 66.35 C ANISOU 1816 CB LYS A1027 6648 7815 10747 1127 -540 -1468 C ATOM 1817 CG LYS A1027 9.026 -58.185 29.229 1.00 66.10 C ANISOU 1817 CG LYS A1027 6638 7795 10683 1071 -637 -1545 C ATOM 1818 CD LYS A1027 9.639 -58.841 30.455 1.00 68.02 C ANISOU 1818 CD LYS A1027 6821 8180 10843 1151 -799 -1635 C ATOM 1819 CE LYS A1027 9.027 -58.293 31.737 1.00 69.77 C ANISOU 1819 CE LYS A1027 7083 8403 11023 1089 -881 -1721 C ATOM 1820 NZ LYS A1027 9.607 -58.925 32.957 1.00 71.07 N ANISOU 1820 NZ LYS A1027 7217 8700 11086 1168 -1051 -1807 N ATOM 1821 N ASP A1028 10.363 -55.871 26.492 1.00 83.39 N ANISOU 1821 N ASP A1028 8607 9803 13276 834 -227 -1524 N ATOM 1822 CA ASP A1028 10.493 -54.423 26.613 1.00 88.91 C ANISOU 1822 CA ASP A1028 9221 10437 14125 675 -152 -1605 C ATOM 1823 C ASP A1028 9.589 -53.698 25.622 1.00 83.60 C ANISOU 1823 C ASP A1028 8695 9587 13481 615 -15 -1504 C ATOM 1824 O ASP A1028 8.952 -52.699 25.973 1.00 93.03 O ANISOU 1824 O ASP A1028 9930 10693 14724 526 6 -1535 O ATOM 1825 CB ASP A1028 11.952 -54.008 26.421 1.00 95.91 C ANISOU 1825 CB ASP A1028 9879 11398 15165 608 -90 -1690 C ATOM 1826 CG ASP A1028 12.809 -54.305 27.640 1.00102.67 C ANISOU 1826 CG ASP A1028 10557 12426 16028 625 -251 -1821 C ATOM 1827 OD1 ASP A1028 12.359 -54.015 28.769 1.00104.82 O ANISOU 1827 OD1 ASP A1028 10863 12713 16253 589 -373 -1902 O ATOM 1828 OD2 ASP A1028 13.930 -54.829 27.470 1.00105.80 O ANISOU 1828 OD2 ASP A1028 10784 12941 16475 681 -257 -1840 O ATOM 1829 N ALA A1029 9.511 -54.190 24.384 1.00 74.69 N ANISOU 1829 N ALA A1029 7665 8399 12315 672 75 -1380 N ATOM 1830 CA ALA A1029 8.667 -53.535 23.390 1.00 66.78 C ANISOU 1830 CA ALA A1029 6815 7230 11329 624 187 -1274 C ATOM 1831 C ALA A1029 7.187 -53.728 23.702 1.00 59.86 C ANISOU 1831 C ALA A1029 6097 6298 10349 662 98 -1200 C ATOM 1832 O ALA A1029 6.386 -52.803 23.532 1.00 58.53 O ANISOU 1832 O ALA A1029 5997 6012 10230 602 148 -1167 O ATOM 1833 CB ALA A1029 8.998 -54.058 21.994 1.00 51.76 C ANISOU 1833 CB ALA A1029 4998 5277 9391 676 298 -1163 C ATOM 1834 N LEU A1030 6.805 -54.920 24.167 1.00 54.60 N ANISOU 1834 N LEU A1030 5488 5712 9544 764 -29 -1169 N ATOM 1835 CA LEU A1030 5.404 -55.176 24.488 1.00 53.96 C ANISOU 1835 CA LEU A1030 5538 5591 9374 792 -109 -1094 C ATOM 1836 C LEU A1030 4.944 -54.391 25.709 1.00 56.31 C ANISOU 1836 C LEU A1030 5779 5898 9718 740 -146 -1187 C ATOM 1837 O LEU A1030 3.771 -54.007 25.789 1.00 55.18 O ANISOU 1837 O LEU A1030 5716 5678 9571 730 -144 -1127 O ATOM 1838 CB LEU A1030 5.179 -56.669 24.718 1.00 52.07 C ANISOU 1838 CB LEU A1030 5380 5430 8973 899 -226 -1043 C ATOM 1839 CG LEU A1030 5.274 -57.574 23.492 1.00 50.80 C ANISOU 1839 CG LEU A1030 5347 5230 8725 961 -200 -928 C ATOM 1840 CD1 LEU A1030 5.416 -59.019 23.938 1.00 48.95 C ANISOU 1840 CD1 LEU A1030 5170 5086 8343 1068 -310 -919 C ATOM 1841 CD2 LEU A1030 4.051 -57.396 22.607 1.00 46.39 C ANISOU 1841 CD2 LEU A1030 4948 4544 8136 932 -185 -790 C ATOM 1842 N THR A1031 5.839 -54.155 26.673 1.00 59.55 N ANISOU 1842 N THR A1031 6056 6401 10171 711 -183 -1333 N ATOM 1843 CA THR A1031 5.468 -53.361 27.840 1.00 61.42 C ANISOU 1843 CA THR A1031 6267 6632 10438 657 -212 -1433 C ATOM 1844 C THR A1031 5.187 -51.912 27.458 1.00 62.64 C ANISOU 1844 C THR A1031 6430 6647 10725 556 -86 -1443 C ATOM 1845 O THR A1031 4.380 -51.243 28.115 1.00 61.33 O ANISOU 1845 O THR A1031 6312 6421 10571 535 -77 -1468 O ATOM 1846 CB THR A1031 6.568 -53.433 28.901 1.00 66.52 C ANISOU 1846 CB THR A1031 6779 7406 11089 640 -299 -1589 C ATOM 1847 OG1 THR A1031 6.927 -54.803 29.125 1.00 71.01 O ANISOU 1847 OG1 THR A1031 7347 8097 11536 752 -409 -1568 O ATOM 1848 CG2 THR A1031 6.088 -52.830 30.213 1.00 66.18 C ANISOU 1848 CG2 THR A1031 6759 7359 11027 601 -349 -1691 C ATOM 1849 N LYS A1032 5.828 -51.418 26.395 1.00 63.84 N ANISOU 1849 N LYS A1032 6548 6734 10973 501 25 -1419 N ATOM 1850 CA LYS A1032 5.536 -50.077 25.903 1.00 64.76 C ANISOU 1850 CA LYS A1032 6703 6696 11206 412 154 -1409 C ATOM 1851 C LYS A1032 4.220 -50.036 25.137 1.00 62.26 C ANISOU 1851 C LYS A1032 6537 6264 10854 466 187 -1250 C ATOM 1852 O LYS A1032 3.447 -49.081 25.275 1.00 62.65 O ANISOU 1852 O LYS A1032 6643 6203 10959 441 241 -1239 O ATOM 1853 CB LYS A1032 6.677 -49.579 25.015 1.00 67.52 C ANISOU 1853 CB LYS A1032 6977 7011 11665 328 273 -1430 C ATOM 1854 CG LYS A1032 8.020 -49.469 25.721 1.00 70.90 C ANISOU 1854 CG LYS A1032 7221 7555 12164 253 243 -1587 C ATOM 1855 CD LYS A1032 9.085 -48.920 24.785 1.00 71.27 C ANISOU 1855 CD LYS A1032 7182 7561 12339 157 386 -1596 C ATOM 1856 CE LYS A1032 10.421 -48.772 25.490 1.00 72.74 C ANISOU 1856 CE LYS A1032 7150 7871 12616 69 346 -1750 C ATOM 1857 NZ LYS A1032 11.458 -48.205 24.584 1.00 73.51 N ANISOU 1857 NZ LYS A1032 7144 7930 12857 -39 506 -1756 N ATOM 1858 N MET A1033 3.951 -51.060 24.323 1.00 59.68 N ANISOU 1858 N MET A1033 6281 5960 10435 543 152 -1125 N ATOM 1859 CA MET A1033 2.719 -51.076 23.542 1.00 57.40 C ANISOU 1859 CA MET A1033 6128 5572 10111 587 156 -969 C ATOM 1860 C MET A1033 1.499 -51.231 24.437 1.00 56.09 C ANISOU 1860 C MET A1033 5985 5426 9900 634 74 -946 C ATOM 1861 O MET A1033 0.459 -50.613 24.185 1.00 57.80 O ANISOU 1861 O MET A1033 6260 5544 10156 644 104 -864 O ATOM 1862 CB MET A1033 2.769 -52.196 22.506 1.00 59.20 C ANISOU 1862 CB MET A1033 6443 5818 10234 645 122 -852 C ATOM 1863 CG MET A1033 3.968 -52.119 21.588 1.00 63.09 C ANISOU 1863 CG MET A1033 6920 6290 10762 614 227 -865 C ATOM 1864 SD MET A1033 4.210 -53.611 20.605 1.00 66.93 S ANISOU 1864 SD MET A1033 7519 6814 11099 701 188 -760 S ATOM 1865 CE MET A1033 2.804 -53.516 19.504 1.00 67.42 C ANISOU 1865 CE MET A1033 7786 6732 11097 715 167 -577 C ATOM 1866 N ARG A1034 1.606 -52.051 25.487 1.00 55.12 N ANISOU 1866 N ARG A1034 5818 5430 9697 669 -25 -1014 N ATOM 1867 CA ARG A1034 0.479 -52.223 26.398 1.00 56.45 C ANISOU 1867 CA ARG A1034 6010 5621 9820 710 -82 -996 C ATOM 1868 C ARG A1034 0.146 -50.917 27.109 1.00 59.93 C ANISOU 1868 C ARG A1034 6426 5985 10357 672 -3 -1074 C ATOM 1869 O ARG A1034 -1.027 -50.615 27.356 1.00 57.58 O ANISOU 1869 O ARG A1034 6164 5639 10074 707 13 -1010 O ATOM 1870 CB ARG A1034 0.779 -53.322 27.415 1.00 55.07 C ANISOU 1870 CB ARG A1034 5812 5585 9528 752 -191 -1061 C ATOM 1871 CG ARG A1034 -0.449 -53.770 28.188 1.00 58.40 C ANISOU 1871 CG ARG A1034 6279 6031 9878 797 -242 -1009 C ATOM 1872 CD ARG A1034 -0.110 -54.779 29.267 1.00 62.34 C ANISOU 1872 CD ARG A1034 6778 6655 10252 836 -340 -1080 C ATOM 1873 NE ARG A1034 -1.304 -55.475 29.739 1.00 67.00 N ANISOU 1873 NE ARG A1034 7432 7266 10760 876 -382 -994 N ATOM 1874 CZ ARG A1034 -2.132 -55.002 30.664 1.00 70.46 C ANISOU 1874 CZ ARG A1034 7872 7691 11211 880 -343 -1016 C ATOM 1875 NH1 ARG A1034 -1.899 -53.823 31.225 1.00 73.46 N ANISOU 1875 NH1 ARG A1034 8215 8026 11672 851 -268 -1127 N ATOM 1876 NH2 ARG A1034 -3.195 -55.707 31.028 1.00 71.88 N ANISOU 1876 NH2 ARG A1034 8095 7894 11321 910 -370 -927 N ATOM 1877 N ALA A1035 1.169 -50.128 27.444 1.00 61.30 N ANISOU 1877 N ALA A1035 6541 6147 10604 598 49 -1213 N ATOM 1878 CA ALA A1035 0.924 -48.821 28.041 1.00 61.44 C ANISOU 1878 CA ALA A1035 6568 6067 10711 552 133 -1295 C ATOM 1879 C ALA A1035 0.341 -47.852 27.019 1.00 62.36 C ANISOU 1879 C ALA A1035 6747 6021 10925 544 245 -1193 C ATOM 1880 O ALA A1035 -0.540 -47.050 27.349 1.00 63.97 O ANISOU 1880 O ALA A1035 6997 6131 11176 569 306 -1177 O ATOM 1881 CB ALA A1035 2.217 -48.267 28.638 1.00 63.62 C ANISOU 1881 CB ALA A1035 6768 6370 11035 454 143 -1473 C ATOM 1882 N ALA A1036 0.815 -47.917 25.770 1.00 60.78 N ANISOU 1882 N ALA A1036 6561 5780 10751 520 280 -1117 N ATOM 1883 CA ALA A1036 0.303 -47.027 24.731 1.00 58.17 C ANISOU 1883 CA ALA A1036 6315 5290 10499 518 379 -1011 C ATOM 1884 C ALA A1036 -1.087 -47.437 24.268 1.00 58.61 C ANISOU 1884 C ALA A1036 6434 5323 10512 616 327 -840 C ATOM 1885 O ALA A1036 -1.874 -46.582 23.847 1.00 60.35 O ANISOU 1885 O ALA A1036 6714 5417 10800 644 389 -759 O ATOM 1886 CB ALA A1036 1.263 -46.994 23.543 1.00 50.77 C ANISOU 1886 CB ALA A1036 5392 4312 9586 461 441 -982 C ATOM 1887 N ALA A1037 -1.404 -48.733 24.321 1.00 57.87 N ANISOU 1887 N ALA A1037 6328 5348 10311 666 209 -780 N ATOM 1888 CA ALA A1037 -2.747 -49.179 23.970 1.00 57.01 C ANISOU 1888 CA ALA A1037 6260 5233 10168 739 142 -622 C ATOM 1889 C ALA A1037 -3.761 -48.713 25.006 1.00 62.82 C ANISOU 1889 C ALA A1037 6958 5964 10947 786 161 -635 C ATOM 1890 O ALA A1037 -4.806 -48.153 24.658 1.00 65.03 O ANISOU 1890 O ALA A1037 7257 6161 11290 837 187 -526 O ATOM 1891 CB ALA A1037 -2.780 -50.700 23.829 1.00 54.83 C ANISOU 1891 CB ALA A1037 5995 5077 9762 763 16 -565 C ATOM 1892 N LEU A1038 -3.467 -48.938 26.291 1.00 65.88 N ANISOU 1892 N LEU A1038 7295 6438 11297 778 150 -766 N ATOM 1893 CA LEU A1038 -4.357 -48.468 27.346 1.00 70.92 C ANISOU 1893 CA LEU A1038 7915 7065 11966 825 194 -793 C ATOM 1894 C LEU A1038 -4.435 -46.949 27.373 1.00 74.08 C ANISOU 1894 C LEU A1038 8347 7315 12486 820 327 -837 C ATOM 1895 O LEU A1038 -5.487 -46.388 27.701 1.00 74.07 O ANISOU 1895 O LEU A1038 8350 7254 12540 890 387 -786 O ATOM 1896 CB LEU A1038 -3.896 -48.998 28.704 1.00 72.84 C ANISOU 1896 CB LEU A1038 8133 7421 12123 812 155 -934 C ATOM 1897 CG LEU A1038 -3.934 -50.515 28.887 1.00 74.36 C ANISOU 1897 CG LEU A1038 8316 7753 12186 832 31 -892 C ATOM 1898 CD1 LEU A1038 -3.480 -50.893 30.288 1.00 74.18 C ANISOU 1898 CD1 LEU A1038 8288 7823 12073 828 -1 -1035 C ATOM 1899 CD2 LEU A1038 -5.327 -51.058 28.602 1.00 76.75 C ANISOU 1899 CD2 LEU A1038 8616 8066 12480 888 -2 -725 C ATOM 1900 N ASP A1039 -3.337 -46.271 27.037 1.00 74.36 N ANISOU 1900 N ASP A1039 8405 7283 12565 738 383 -929 N ATOM 1901 CA ASP A1039 -3.370 -44.818 26.935 1.00 77.64 C ANISOU 1901 CA ASP A1039 8878 7531 13091 721 515 -964 C ATOM 1902 C ASP A1039 -4.241 -44.374 25.768 1.00 76.62 C ANISOU 1902 C ASP A1039 8799 7286 13026 787 550 -786 C ATOM 1903 O ASP A1039 -4.971 -43.381 25.872 1.00 79.14 O ANISOU 1903 O ASP A1039 9162 7481 13425 845 641 -756 O ATOM 1904 CB ASP A1039 -1.947 -44.277 26.794 1.00 81.55 C ANISOU 1904 CB ASP A1039 9378 7986 13621 595 563 -1098 C ATOM 1905 CG ASP A1039 -1.890 -42.764 26.813 1.00 85.75 C ANISOU 1905 CG ASP A1039 9990 8334 14259 555 704 -1156 C ATOM 1906 OD1 ASP A1039 -2.405 -42.129 25.869 1.00 87.55 O ANISOU 1906 OD1 ASP A1039 10288 8426 14550 594 773 -1036 O ATOM 1907 OD2 ASP A1039 -1.330 -42.207 27.781 1.00 87.95 O ANISOU 1907 OD2 ASP A1039 10275 8594 14549 483 739 -1322 O ATOM 1908 N ALA A1040 -4.182 -45.098 24.650 1.00 72.14 N ANISOU 1908 N ALA A1040 8241 6752 12418 786 474 -666 N ATOM 1909 CA ALA A1040 -5.023 -44.769 23.506 1.00 70.58 C ANISOU 1909 CA ALA A1040 8103 6454 12261 849 476 -488 C ATOM 1910 C ALA A1040 -6.472 -45.190 23.718 1.00 70.43 C ANISOU 1910 C ALA A1040 8032 6485 12242 956 404 -359 C ATOM 1911 O ALA A1040 -7.375 -44.600 23.115 1.00 69.90 O ANISOU 1911 O ALA A1040 7992 6324 12243 1032 420 -228 O ATOM 1912 CB ALA A1040 -4.469 -45.418 22.238 1.00 69.45 C ANISOU 1912 CB ALA A1040 8012 6321 12054 808 417 -407 C ATOM 1913 N GLN A1041 -6.716 -46.194 24.564 1.00 70.77 N ANISOU 1913 N GLN A1041 7998 6676 12215 964 327 -389 N ATOM 1914 CA GLN A1041 -8.084 -46.610 24.848 1.00 71.52 C ANISOU 1914 CA GLN A1041 8025 6828 12322 1049 274 -270 C ATOM 1915 C GLN A1041 -8.856 -45.545 25.615 1.00 77.25 C ANISOU 1915 C GLN A1041 8725 7475 13151 1132 397 -288 C ATOM 1916 O GLN A1041 -10.091 -45.545 25.577 1.00 82.54 O ANISOU 1916 O GLN A1041 9330 8153 13878 1223 383 -158 O ATOM 1917 CB GLN A1041 -8.084 -47.928 25.629 1.00 69.85 C ANISOU 1917 CB GLN A1041 7756 6781 12003 1026 182 -306 C ATOM 1918 CG GLN A1041 -9.426 -48.654 25.659 1.00 69.35 C ANISOU 1918 CG GLN A1041 7618 6793 11938 1080 102 -158 C ATOM 1919 CD GLN A1041 -9.334 -50.028 26.308 1.00 70.19 C ANISOU 1919 CD GLN A1041 7701 7045 11923 1042 12 -187 C ATOM 1920 OE1 GLN A1041 -8.301 -50.392 26.870 1.00 69.84 O ANISOU 1920 OE1 GLN A1041 7690 7049 11795 995 11 -325 O ATOM 1921 NE2 GLN A1041 -10.416 -50.797 26.230 1.00 70.54 N ANISOU 1921 NE2 GLN A1041 7686 7157 11958 1059 -70 -54 N ATOM 1922 N LYS A1042 -8.162 -44.636 26.293 1.00 76.24 N ANISOU 1922 N LYS A1042 8647 7269 13053 1104 517 -445 N ATOM 1923 CA LYS A1042 -8.816 -43.558 27.023 1.00 77.66 C ANISOU 1923 CA LYS A1042 8840 7349 13320 1186 653 -476 C ATOM 1924 C LYS A1042 -9.177 -42.411 26.083 1.00 76.83 C ANISOU 1924 C LYS A1042 8800 7068 13323 1246 727 -378 C ATOM 1925 O LYS A1042 -10.310 -41.927 26.083 1.00 77.37 O ANISOU 1925 O LYS A1042 8838 7083 13475 1372 774 -270 O ATOM 1926 CB LYS A1042 -7.918 -43.050 28.155 1.00 79.64 C ANISOU 1926 CB LYS A1042 9147 7572 13541 1120 741 -692 C ATOM 1927 CG LYS A1042 -7.592 -44.094 29.216 1.00 79.76 C ANISOU 1927 CG LYS A1042 9116 7750 13440 1079 671 -794 C ATOM 1928 CD LYS A1042 -6.724 -43.504 30.320 1.00 80.96 C ANISOU 1928 CD LYS A1042 9336 7866 13557 1012 739 -1007 C ATOM 1929 CE LYS A1042 -6.362 -44.546 31.370 1.00 80.08 C ANISOU 1929 CE LYS A1042 9197 7914 13316 979 654 -1104 C ATOM 1930 NZ LYS A1042 -5.497 -43.973 32.441 1.00 80.66 N ANISOU 1930 NZ LYS A1042 9345 7956 13346 908 694 -1313 N ATOM 1931 N PRO A1056 -22.876 -48.460 18.326 1.00117.11 N ANISOU 1931 N PRO A1056 12478 13030 18987 1657 -1186 1958 N ATOM 1932 CA PRO A1056 -22.511 -48.987 17.007 1.00118.54 C ANISOU 1932 CA PRO A1056 12857 13168 19013 1550 -1419 2021 C ATOM 1933 C PRO A1056 -21.002 -49.039 16.793 1.00121.02 C ANISOU 1933 C PRO A1056 13468 13374 19139 1478 -1332 1856 C ATOM 1934 O PRO A1056 -20.416 -50.121 16.767 1.00119.50 O ANISOU 1934 O PRO A1056 13385 13229 18792 1329 -1398 1786 O ATOM 1935 CB PRO A1056 -23.163 -47.994 16.043 1.00118.78 C ANISOU 1935 CB PRO A1056 12872 13113 19145 1694 -1519 2185 C ATOM 1936 CG PRO A1056 -24.329 -47.462 16.799 1.00119.80 C ANISOU 1936 CG PRO A1056 12691 13321 19508 1838 -1436 2271 C ATOM 1937 CD PRO A1056 -23.882 -47.388 18.232 1.00118.59 C ANISOU 1937 CD PRO A1056 12488 13190 19379 1850 -1156 2094 C ATOM 1938 N GLU A1057 -20.381 -47.870 16.636 1.00127.45 N ANISOU 1938 N GLU A1057 14411 14041 19972 1584 -1181 1798 N ATOM 1939 CA GLU A1057 -18.935 -47.823 16.460 1.00131.04 C ANISOU 1939 CA GLU A1057 15118 14397 20274 1517 -1078 1643 C ATOM 1940 C GLU A1057 -18.198 -47.914 17.790 1.00132.99 C ANISOU 1940 C GLU A1057 15334 14682 20514 1488 -867 1445 C ATOM 1941 O GLU A1057 -17.059 -48.393 17.828 1.00133.06 O ANISOU 1941 O GLU A1057 15495 14680 20384 1389 -827 1313 O ATOM 1942 CB GLU A1057 -18.534 -46.548 15.718 1.00135.22 C ANISOU 1942 CB GLU A1057 15810 14745 20823 1620 -1001 1662 C ATOM 1943 CG GLU A1057 -19.059 -46.469 14.293 1.00139.06 C ANISOU 1943 CG GLU A1057 16393 15172 21271 1643 -1219 1848 C ATOM 1944 CD GLU A1057 -18.643 -45.192 13.590 1.00141.58 C ANISOU 1944 CD GLU A1057 16897 15297 21599 1747 -1125 1869 C ATOM 1945 OE1 GLU A1057 -18.010 -44.334 14.241 1.00141.55 O ANISOU 1945 OE1 GLU A1057 16928 15206 21650 1798 -889 1741 O ATOM 1946 OE2 GLU A1057 -18.947 -45.045 12.388 1.00143.13 O ANISOU 1946 OE2 GLU A1057 17220 15422 21742 1773 -1291 2014 O ATOM 1947 N MET A1058 -18.823 -47.466 18.882 1.00134.60 N ANISOU 1947 N MET A1058 15347 14932 20861 1579 -731 1424 N ATOM 1948 CA MET A1058 -18.210 -47.589 20.200 1.00133.40 C ANISOU 1948 CA MET A1058 15175 14821 20688 1551 -547 1240 C ATOM 1949 C MET A1058 -18.114 -49.037 20.659 1.00131.03 C ANISOU 1949 C MET A1058 14841 14666 20280 1414 -634 1200 C ATOM 1950 O MET A1058 -17.279 -49.351 21.514 1.00129.33 O ANISOU 1950 O MET A1058 14680 14476 19984 1362 -525 1038 O ATOM 1951 CB MET A1058 -18.994 -46.772 21.228 1.00135.40 C ANISOU 1951 CB MET A1058 15257 15080 21110 1691 -375 1238 C ATOM 1952 CG MET A1058 -18.844 -45.269 21.077 1.00136.60 C ANISOU 1952 CG MET A1058 15485 15064 21354 1831 -228 1223 C ATOM 1953 SD MET A1058 -17.153 -44.710 21.361 1.00135.17 S ANISOU 1953 SD MET A1058 15544 14753 21062 1763 -61 992 S ATOM 1954 CE MET A1058 -16.876 -45.296 23.031 1.00134.15 C ANISOU 1954 CE MET A1058 15336 14741 20894 1710 69 815 C ATOM 1955 N LYS A1059 -18.952 -49.922 20.117 1.00130.71 N ANISOU 1955 N LYS A1059 14718 14715 20230 1353 -834 1347 N ATOM 1956 CA LYS A1059 -18.874 -51.335 20.461 1.00128.53 C ANISOU 1956 CA LYS A1059 14440 14556 19839 1213 -924 1319 C ATOM 1957 C LYS A1059 -17.786 -52.050 19.670 1.00127.48 C ANISOU 1957 C LYS A1059 14544 14381 19511 1102 -1024 1262 C ATOM 1958 O LYS A1059 -17.155 -52.976 20.192 1.00127.31 O ANISOU 1958 O LYS A1059 14588 14415 19369 1014 -1011 1159 O ATOM 1959 CB LYS A1059 -20.230 -52.005 20.226 1.00127.64 C ANISOU 1959 CB LYS A1059 14144 14552 19803 1173 -1096 1496 C ATOM 1960 CG LYS A1059 -21.411 -51.204 20.758 1.00127.35 C ANISOU 1960 CG LYS A1059 13851 14552 19984 1306 -1009 1590 C ATOM 1961 CD LYS A1059 -22.733 -51.900 20.477 1.00127.19 C ANISOU 1961 CD LYS A1059 13621 14651 20053 1250 -1193 1773 C ATOM 1962 CE LYS A1059 -23.909 -50.993 20.803 1.00128.40 C ANISOU 1962 CE LYS A1059 13508 14835 20443 1409 -1113 1889 C ATOM 1963 NZ LYS A1059 -23.839 -50.483 22.199 1.00127.84 N ANISOU 1963 NZ LYS A1059 13357 14773 20445 1506 -827 1770 N ATOM 1964 N ASP A1060 -17.547 -51.634 18.422 1.00127.04 N ANISOU 1964 N ASP A1060 14629 14222 19418 1115 -1113 1330 N ATOM 1965 CA ASP A1060 -16.501 -52.247 17.610 1.00125.17 C ANISOU 1965 CA ASP A1060 14631 13933 18996 1025 -1182 1281 C ATOM 1966 C ASP A1060 -15.116 -51.726 17.969 1.00121.10 C ANISOU 1966 C ASP A1060 14234 13346 18433 1044 -989 1103 C ATOM 1967 O ASP A1060 -14.122 -52.432 17.764 1.00118.78 O ANISOU 1967 O ASP A1060 14089 13050 17993 969 -996 1018 O ATOM 1968 CB ASP A1060 -16.775 -52.005 16.124 1.00127.93 C ANISOU 1968 CB ASP A1060 15107 14192 19307 1030 -1342 1425 C ATOM 1969 CG ASP A1060 -18.108 -52.569 15.676 1.00130.70 C ANISOU 1969 CG ASP A1060 15343 14618 19697 993 -1571 1604 C ATOM 1970 OD1 ASP A1060 -18.534 -53.604 16.230 1.00130.76 O ANISOU 1970 OD1 ASP A1060 15255 14742 19685 902 -1640 1608 O ATOM 1971 OD2 ASP A1060 -18.730 -51.975 14.770 1.00132.43 O ANISOU 1971 OD2 ASP A1060 15570 14780 19969 1050 -1686 1744 O ATOM 1972 N PHE A1061 -15.027 -50.501 18.490 1.00121.08 N ANISOU 1972 N PHE A1061 14169 13282 18555 1142 -818 1045 N ATOM 1973 CA PHE A1061 -13.737 -49.962 18.906 1.00119.48 C ANISOU 1973 CA PHE A1061 14060 13016 18323 1141 -642 871 C ATOM 1974 C PHE A1061 -13.331 -50.482 20.278 1.00122.51 C ANISOU 1974 C PHE A1061 14366 13501 18682 1108 -552 721 C ATOM 1975 O PHE A1061 -12.145 -50.726 20.524 1.00122.86 O ANISOU 1975 O PHE A1061 14499 13545 18638 1057 -489 582 O ATOM 1976 CB PHE A1061 -13.776 -48.435 18.901 1.00115.80 C ANISOU 1976 CB PHE A1061 13590 12423 17987 1244 -498 863 C ATOM 1977 CG PHE A1061 -13.658 -47.834 17.531 1.00111.24 C ANISOU 1977 CG PHE A1061 13163 11711 17391 1266 -546 963 C ATOM 1978 CD1 PHE A1061 -12.981 -48.504 16.525 1.00108.20 C ANISOU 1978 CD1 PHE A1061 12951 11303 16858 1183 -638 981 C ATOM 1979 CD2 PHE A1061 -14.222 -46.602 17.248 1.00110.50 C ANISOU 1979 CD2 PHE A1061 13059 11506 17421 1380 -490 1043 C ATOM 1980 CE1 PHE A1061 -12.869 -47.958 15.264 1.00107.25 C ANISOU 1980 CE1 PHE A1061 12996 11051 16704 1204 -672 1076 C ATOM 1981 CE2 PHE A1061 -14.113 -46.051 15.988 1.00109.58 C ANISOU 1981 CE2 PHE A1061 13105 11257 17275 1405 -534 1141 C ATOM 1982 CZ PHE A1061 -13.435 -46.731 14.996 1.00108.43 C ANISOU 1982 CZ PHE A1061 13137 11090 16972 1312 -625 1157 C ATOM 1983 N ARG A1062 -14.295 -50.648 21.187 1.00126.72 N ANISOU 1983 N ARG A1062 14733 14121 19294 1141 -541 751 N ATOM 1984 CA ARG A1062 -13.989 -51.285 22.462 1.00128.15 C ANISOU 1984 CA ARG A1062 14865 14400 19424 1106 -474 625 C ATOM 1985 C ARG A1062 -13.563 -52.733 22.255 1.00119.74 C ANISOU 1985 C ARG A1062 13883 13414 18199 1000 -604 618 C ATOM 1986 O ARG A1062 -12.664 -53.228 22.944 1.00124.50 O ANISOU 1986 O ARG A1062 14538 14059 18709 965 -556 481 O ATOM 1987 CB ARG A1062 -15.195 -51.200 23.399 1.00135.32 C ANISOU 1987 CB ARG A1062 15590 15380 20445 1163 -424 678 C ATOM 1988 CG ARG A1062 -15.053 -52.029 24.667 1.00140.47 C ANISOU 1988 CG ARG A1062 16208 16138 21025 1120 -374 577 C ATOM 1989 CD ARG A1062 -15.969 -51.522 25.766 1.00146.28 C ANISOU 1989 CD ARG A1062 16792 16907 21880 1203 -236 581 C ATOM 1990 NE ARG A1062 -15.611 -50.167 26.172 1.00150.19 N ANISOU 1990 NE ARG A1062 17312 17299 22453 1298 -65 483 N ATOM 1991 CZ ARG A1062 -14.646 -49.879 27.040 1.00152.07 C ANISOU 1991 CZ ARG A1062 17639 17514 22628 1290 50 301 C ATOM 1992 NH1 ARG A1062 -13.940 -50.855 27.597 1.00151.77 N ANISOU 1992 NH1 ARG A1062 17662 17555 22448 1208 10 202 N ATOM 1993 NH2 ARG A1062 -14.386 -48.617 27.351 1.00153.37 N ANISOU 1993 NH2 ARG A1062 17838 17570 22866 1363 197 217 N ATOM 1994 N HIS A1063 -14.186 -53.422 21.294 1.00106.73 N ANISOU 1994 N HIS A1063 12260 11779 16512 952 -777 764 N ATOM 1995 CA HIS A1063 -13.767 -54.780 20.963 1.00 93.94 C ANISOU 1995 CA HIS A1063 10759 10206 14727 853 -901 762 C ATOM 1996 C HIS A1063 -12.375 -54.801 20.344 1.00 79.35 C ANISOU 1996 C HIS A1063 9095 8288 12766 836 -872 669 C ATOM 1997 O HIS A1063 -11.603 -55.734 20.591 1.00 77.51 O ANISOU 1997 O HIS A1063 8949 8097 12404 790 -886 587 O ATOM 1998 CB HIS A1063 -14.785 -55.427 20.019 1.00 93.08 C ANISOU 1998 CB HIS A1063 10653 10111 14602 794 -1101 941 C ATOM 1999 CG HIS A1063 -14.493 -56.861 19.695 1.00 92.36 C ANISOU 1999 CG HIS A1063 10703 10054 14337 687 -1232 947 C ATOM 2000 ND1 HIS A1063 -14.369 -57.835 20.663 1.00 92.34 N ANISOU 2000 ND1 HIS A1063 10688 10136 14262 639 -1215 878 N ATOM 2001 CD2 HIS A1063 -14.311 -57.488 18.508 1.00 92.20 C ANISOU 2001 CD2 HIS A1063 10863 9981 14189 624 -1379 1014 C ATOM 2002 CE1 HIS A1063 -14.119 -58.998 20.087 1.00 91.38 C ANISOU 2002 CE1 HIS A1063 10729 10009 13982 553 -1343 903 C ATOM 2003 NE2 HIS A1063 -14.080 -58.815 18.779 1.00 91.46 N ANISOU 2003 NE2 HIS A1063 10861 9936 13954 541 -1443 983 N ATOM 2004 N GLY A1064 -12.035 -53.785 19.548 1.00 70.33 N ANISOU 2004 N GLY A1064 8013 7038 11672 879 -823 683 N ATOM 2005 CA GLY A1064 -10.724 -53.756 18.921 1.00 61.01 C ANISOU 2005 CA GLY A1064 6995 5790 10397 859 -774 602 C ATOM 2006 C GLY A1064 -9.596 -53.579 19.921 1.00 56.43 C ANISOU 2006 C GLY A1064 6386 5241 9816 865 -627 417 C ATOM 2007 O GLY A1064 -8.544 -54.214 19.802 1.00 55.77 O ANISOU 2007 O GLY A1064 6393 5174 9623 833 -619 337 O ATOM 2008 N PHE A1065 -9.794 -52.713 20.918 1.00 53.58 N ANISOU 2008 N PHE A1065 5900 4887 9572 911 -513 346 N ATOM 2009 CA PHE A1065 -8.773 -52.525 21.939 1.00 54.59 C ANISOU 2009 CA PHE A1065 6000 5047 9694 907 -396 166 C ATOM 2010 C PHE A1065 -8.738 -53.678 22.932 1.00 58.07 C ANISOU 2010 C PHE A1065 6407 5614 10043 884 -445 108 C ATOM 2011 O PHE A1065 -7.697 -53.921 23.553 1.00 57.08 O ANISOU 2011 O PHE A1065 6296 5530 9860 871 -402 -30 O ATOM 2012 CB PHE A1065 -8.991 -51.204 22.673 1.00 56.02 C ANISOU 2012 CB PHE A1065 6096 5175 10012 959 -258 104 C ATOM 2013 CG PHE A1065 -8.473 -50.008 21.928 1.00 56.54 C ANISOU 2013 CG PHE A1065 6227 5106 10150 968 -166 93 C ATOM 2014 CD1 PHE A1065 -7.131 -49.670 21.986 1.00 55.11 C ANISOU 2014 CD1 PHE A1065 6095 4894 9952 923 -77 -46 C ATOM 2015 CD2 PHE A1065 -9.326 -49.219 21.175 1.00 56.45 C ANISOU 2015 CD2 PHE A1065 6226 4996 10225 1022 -168 225 C ATOM 2016 CE1 PHE A1065 -6.647 -48.569 21.303 1.00 55.15 C ANISOU 2016 CE1 PHE A1065 6167 4765 10024 916 22 -54 C ATOM 2017 CE2 PHE A1065 -8.849 -48.116 20.490 1.00 56.47 C ANISOU 2017 CE2 PHE A1065 6313 4859 10284 1031 -75 219 C ATOM 2018 CZ PHE A1065 -7.508 -47.790 20.555 1.00 55.47 C ANISOU 2018 CZ PHE A1065 6244 4694 10138 970 28 78 C ATOM 2019 N ASP A1066 -9.853 -54.392 23.103 1.00 61.83 N ANISOU 2019 N ASP A1066 6837 6151 10506 877 -537 214 N ATOM 2020 CA ASP A1066 -9.816 -55.617 23.895 1.00 62.34 C ANISOU 2020 CA ASP A1066 6907 6318 10460 845 -591 177 C ATOM 2021 C ASP A1066 -8.994 -56.691 23.195 1.00 54.75 C ANISOU 2021 C ASP A1066 6090 5364 9350 802 -682 173 C ATOM 2022 O ASP A1066 -8.304 -57.481 23.851 1.00 56.14 O ANISOU 2022 O ASP A1066 6303 5603 9424 797 -686 82 O ATOM 2023 CB ASP A1066 -11.235 -56.118 24.167 1.00 74.78 C ANISOU 2023 CB ASP A1066 8397 7948 12067 829 -660 303 C ATOM 2024 CG ASP A1066 -12.007 -55.211 25.103 1.00 85.37 C ANISOU 2024 CG ASP A1066 9591 9299 13544 888 -542 292 C ATOM 2025 OD1 ASP A1066 -11.369 -54.524 25.930 1.00 88.63 O ANISOU 2025 OD1 ASP A1066 9995 9701 13980 929 -417 153 O ATOM 2026 OD2 ASP A1066 -13.252 -55.182 25.010 1.00 89.61 O ANISOU 2026 OD2 ASP A1066 10025 9857 14168 895 -576 423 O ATOM 2027 N ILE A1067 -9.056 -56.737 21.864 1.00 46.34 N ANISOU 2027 N ILE A1067 5119 4228 8260 782 -752 274 N ATOM 2028 CA ILE A1067 -8.214 -57.662 21.114 1.00 44.96 C ANISOU 2028 CA ILE A1067 5106 4039 7939 755 -812 267 C ATOM 2029 C ILE A1067 -6.763 -57.203 21.148 1.00 58.43 C ANISOU 2029 C ILE A1067 6834 5725 9643 785 -695 130 C ATOM 2030 O ILE A1067 -5.847 -58.008 21.351 1.00 56.82 O ANISOU 2030 O ILE A1067 6690 5564 9335 791 -698 53 O ATOM 2031 CB ILE A1067 -8.721 -57.801 19.667 1.00 52.48 C ANISOU 2031 CB ILE A1067 6178 4910 8853 723 -918 413 C ATOM 2032 CG1 ILE A1067 -10.144 -58.359 19.637 1.00 54.56 C ANISOU 2032 CG1 ILE A1067 6400 5207 9122 674 -1059 550 C ATOM 2033 CG2 ILE A1067 -7.798 -58.698 18.867 1.00 45.16 C ANISOU 2033 CG2 ILE A1067 5443 3949 7765 707 -953 399 C ATOM 2034 CD1 ILE A1067 -10.758 -58.355 18.255 1.00 46.80 C ANISOU 2034 CD1 ILE A1067 5522 4146 8112 640 -1188 699 C ATOM 2035 N LEU A1068 -6.532 -55.904 20.948 1.00 45.07 N ANISOU 2035 N LEU A1068 5091 3965 8069 804 -591 100 N ATOM 2036 CA LEU A1068 -5.170 -55.384 20.913 1.00 45.04 C ANISOU 2036 CA LEU A1068 5093 3938 8083 811 -476 -24 C ATOM 2037 C LEU A1068 -4.455 -55.613 22.239 1.00 46.67 C ANISOU 2037 C LEU A1068 5210 4242 8279 822 -437 -177 C ATOM 2038 O LEU A1068 -3.350 -56.166 22.273 1.00 51.50 O ANISOU 2038 O LEU A1068 5850 4897 8822 827 -427 -257 O ATOM 2039 CB LEU A1068 -5.189 -53.897 20.565 1.00 47.89 C ANISOU 2039 CB LEU A1068 5420 4197 8579 816 -368 -25 C ATOM 2040 CG LEU A1068 -3.810 -53.244 20.494 1.00 49.74 C ANISOU 2040 CG LEU A1068 5649 4397 8852 798 -238 -149 C ATOM 2041 CD1 LEU A1068 -3.027 -53.792 19.312 1.00 46.00 C ANISOU 2041 CD1 LEU A1068 5307 3886 8286 786 -236 -111 C ATOM 2042 CD2 LEU A1068 -3.938 -51.735 20.411 1.00 52.73 C ANISOU 2042 CD2 LEU A1068 5995 4668 9370 794 -125 -161 C ATOM 2043 N VAL A1069 -5.069 -55.190 23.345 1.00 44.80 N ANISOU 2043 N VAL A1069 4870 4044 8108 833 -415 -217 N ATOM 2044 CA VAL A1069 -4.436 -55.378 24.647 1.00 49.37 C ANISOU 2044 CA VAL A1069 5386 4711 8662 844 -390 -362 C ATOM 2045 C VAL A1069 -4.340 -56.860 24.984 1.00 44.08 C ANISOU 2045 C VAL A1069 4773 4131 7844 854 -492 -354 C ATOM 2046 O VAL A1069 -3.339 -57.317 25.549 1.00 46.80 O ANISOU 2046 O VAL A1069 5115 4541 8125 871 -497 -463 O ATOM 2047 CB VAL A1069 -5.194 -54.589 25.731 1.00 50.60 C ANISOU 2047 CB VAL A1069 5452 4870 8903 859 -332 -401 C ATOM 2048 CG1 VAL A1069 -4.599 -54.857 27.105 1.00 49.92 C ANISOU 2048 CG1 VAL A1069 5332 4873 8761 868 -324 -547 C ATOM 2049 CG2 VAL A1069 -5.153 -53.099 25.422 1.00 51.19 C ANISOU 2049 CG2 VAL A1069 5494 4838 9116 856 -221 -423 C ATOM 2050 N GLY A1070 -5.363 -57.638 24.621 1.00 43.91 N ANISOU 2050 N GLY A1070 4807 4110 7766 841 -581 -222 N ATOM 2051 CA GLY A1070 -5.322 -59.069 24.883 1.00 46.82 C ANISOU 2051 CA GLY A1070 5259 4542 7988 841 -674 -205 C ATOM 2052 C GLY A1070 -4.179 -59.763 24.167 1.00 46.89 C ANISOU 2052 C GLY A1070 5375 4544 7898 861 -696 -232 C ATOM 2053 O GLY A1070 -3.443 -60.552 24.764 1.00 49.26 O ANISOU 2053 O GLY A1070 5704 4910 8104 897 -719 -307 O ATOM 2054 N GLN A1071 -4.013 -59.477 22.873 1.00 47.09 N ANISOU 2054 N GLN A1071 5467 4486 7938 847 -684 -167 N ATOM 2055 CA GLN A1071 -2.929 -60.094 22.115 1.00 43.43 C ANISOU 2055 CA GLN A1071 5112 4006 7384 875 -677 -186 C ATOM 2056 C GLN A1071 -1.561 -59.661 22.624 1.00 44.11 C ANISOU 2056 C GLN A1071 5101 4142 7518 914 -585 -334 C ATOM 2057 O GLN A1071 -0.608 -60.446 22.570 1.00 45.00 O ANISOU 2057 O GLN A1071 5260 4292 7545 962 -589 -379 O ATOM 2058 CB GLN A1071 -3.062 -59.757 20.635 1.00 43.75 C ANISOU 2058 CB GLN A1071 5259 3937 7429 851 -664 -86 C ATOM 2059 CG GLN A1071 -4.246 -60.394 19.955 1.00 45.38 C ANISOU 2059 CG GLN A1071 5588 4096 7559 807 -788 63 C ATOM 2060 CD GLN A1071 -4.444 -59.854 18.559 1.00 47.77 C ANISOU 2060 CD GLN A1071 5993 4285 7871 785 -783 160 C ATOM 2061 OE1 GLN A1071 -3.966 -58.767 18.233 1.00 50.44 O ANISOU 2061 OE1 GLN A1071 6281 4575 8307 796 -675 128 O ATOM 2062 NE2 GLN A1071 -5.144 -60.610 17.721 1.00 46.29 N ANISOU 2062 NE2 GLN A1071 5966 4047 7575 746 -905 281 N ATOM 2063 N ILE A1072 -1.437 -58.423 23.107 1.00 43.88 N ANISOU 2063 N ILE A1072 4937 4109 7625 893 -504 -408 N ATOM 2064 CA ILE A1072 -0.181 -57.994 23.714 1.00 44.26 C ANISOU 2064 CA ILE A1072 4875 4214 7726 908 -437 -556 C ATOM 2065 C ILE A1072 0.103 -58.811 24.966 1.00 48.60 C ANISOU 2065 C ILE A1072 5394 4879 8194 951 -509 -639 C ATOM 2066 O ILE A1072 1.246 -59.207 25.226 1.00 44.43 O ANISOU 2066 O ILE A1072 4828 4418 7635 993 -511 -726 O ATOM 2067 CB ILE A1072 -0.220 -56.483 24.011 1.00 47.53 C ANISOU 2067 CB ILE A1072 5179 4583 8295 860 -343 -620 C ATOM 2068 CG1 ILE A1072 -0.269 -55.692 22.704 1.00 47.29 C ANISOU 2068 CG1 ILE A1072 5200 4432 8337 827 -262 -542 C ATOM 2069 CG2 ILE A1072 0.982 -56.062 24.852 1.00 45.30 C ANISOU 2069 CG2 ILE A1072 4774 4371 8066 853 -302 -784 C ATOM 2070 CD1 ILE A1072 -0.470 -54.210 22.891 1.00 45.64 C ANISOU 2070 CD1 ILE A1072 4918 4149 8272 784 -167 -582 C ATOM 2071 N ASP A1073 -0.940 -59.093 25.752 1.00 48.49 N ANISOU 2071 N ASP A1073 5394 4888 8141 946 -567 -607 N ATOM 2072 CA ASP A1073 -0.777 -59.924 26.940 1.00 49.33 C ANISOU 2072 CA ASP A1073 5506 5090 8147 988 -635 -671 C ATOM 2073 C ASP A1073 -0.355 -61.342 26.572 1.00 48.44 C ANISOU 2073 C ASP A1073 5515 5003 7887 1043 -709 -629 C ATOM 2074 O ASP A1073 0.504 -61.929 27.241 1.00 45.78 O ANISOU 2074 O ASP A1073 5170 4744 7481 1106 -746 -711 O ATOM 2075 CB ASP A1073 -2.074 -59.938 27.749 1.00 54.58 C ANISOU 2075 CB ASP A1073 6177 5761 8800 966 -657 -627 C ATOM 2076 CG ASP A1073 -2.424 -58.574 28.311 1.00 58.36 C ANISOU 2076 CG ASP A1073 6549 6215 9411 936 -573 -687 C ATOM 2077 OD1 ASP A1073 -1.503 -57.750 28.493 1.00 60.51 O ANISOU 2077 OD1 ASP A1073 6746 6490 9756 929 -521 -801 O ATOM 2078 OD2 ASP A1073 -3.620 -58.325 28.576 1.00 60.47 O ANISOU 2078 OD2 ASP A1073 6806 6457 9713 918 -555 -618 O ATOM 2079 N ASP A1074 -0.952 -61.912 25.520 1.00 50.02 N ANISOU 2079 N ASP A1074 5841 5133 8033 1025 -737 -500 N ATOM 2080 CA ASP A1074 -0.545 -63.238 25.061 1.00 44.17 C ANISOU 2080 CA ASP A1074 5250 4390 7144 1078 -795 -459 C ATOM 2081 C ASP A1074 0.942 -63.269 24.742 1.00 43.71 C ANISOU 2081 C ASP A1074 5155 4360 7092 1150 -742 -540 C ATOM 2082 O ASP A1074 1.670 -64.160 25.195 1.00 50.67 O ANISOU 2082 O ASP A1074 6072 5303 7879 1235 -781 -586 O ATOM 2083 CB ASP A1074 -1.353 -63.653 23.828 1.00 43.09 C ANISOU 2083 CB ASP A1074 5263 4154 6954 1030 -829 -316 C ATOM 2084 CG ASP A1074 -2.833 -63.806 24.114 1.00 55.66 C ANISOU 2084 CG ASP A1074 6876 5731 8540 955 -898 -222 C ATOM 2085 OD1 ASP A1074 -3.270 -63.486 25.241 1.00 55.69 O ANISOU 2085 OD1 ASP A1074 6776 5793 8590 945 -891 -265 O ATOM 2086 OD2 ASP A1074 -3.563 -64.250 23.201 1.00 54.97 O ANISOU 2086 OD2 ASP A1074 6911 5572 8401 904 -958 -103 O ATOM 2087 N ALA A1075 1.414 -62.297 23.960 1.00 43.98 N ANISOU 2087 N ALA A1075 5117 4351 7241 1123 -647 -554 N ATOM 2088 CA ALA A1075 2.826 -62.251 23.608 1.00 53.57 C ANISOU 2088 CA ALA A1075 6272 5597 8487 1181 -575 -626 C ATOM 2089 C ALA A1075 3.708 -61.921 24.806 1.00 52.88 C ANISOU 2089 C ALA A1075 6004 5625 8461 1211 -582 -769 C ATOM 2090 O ALA A1075 4.879 -62.313 24.823 1.00 45.86 O ANISOU 2090 O ALA A1075 5059 4800 7564 1287 -568 -828 O ATOM 2091 CB ALA A1075 3.051 -61.238 22.485 1.00 48.99 C ANISOU 2091 CB ALA A1075 5666 4931 8016 1127 -457 -599 C ATOM 2092 N LEU A1076 3.170 -61.222 25.811 1.00 52.87 N ANISOU 2092 N LEU A1076 5917 5654 8518 1157 -608 -824 N ATOM 2093 CA LEU A1076 3.954 -60.906 27.001 1.00 51.62 C ANISOU 2093 CA LEU A1076 5614 5600 8399 1174 -636 -964 C ATOM 2094 C LEU A1076 4.214 -62.147 27.844 1.00 51.53 C ANISOU 2094 C LEU A1076 5661 5676 8241 1273 -747 -986 C ATOM 2095 O LEU A1076 5.341 -62.365 28.304 1.00 55.00 O ANISOU 2095 O LEU A1076 6007 6208 8681 1339 -780 -1075 O ATOM 2096 CB LEU A1076 3.240 -59.842 27.831 1.00 45.55 C ANISOU 2096 CB LEU A1076 4779 4818 7710 1094 -624 -1016 C ATOM 2097 CG LEU A1076 3.850 -58.445 27.769 1.00 48.05 C ANISOU 2097 CG LEU A1076 4951 5115 8191 1019 -536 -1108 C ATOM 2098 CD1 LEU A1076 3.077 -57.483 28.649 1.00 47.82 C ANISOU 2098 CD1 LEU A1076 4897 5058 8216 956 -521 -1158 C ATOM 2099 CD2 LEU A1076 5.313 -58.499 28.182 1.00 48.44 C ANISOU 2099 CD2 LEU A1076 4866 5269 8271 1046 -559 -1231 C ATOM 2100 N LYS A1077 3.185 -62.967 28.069 1.00 51.50 N ANISOU 2100 N LYS A1077 5810 5644 8113 1283 -809 -901 N ATOM 2101 CA LYS A1077 3.377 -64.196 28.832 1.00 53.06 C ANISOU 2101 CA LYS A1077 6100 5904 8155 1377 -907 -909 C ATOM 2102 C LYS A1077 4.349 -65.135 28.126 1.00 55.29 C ANISOU 2102 C LYS A1077 6439 6196 8371 1485 -912 -887 C ATOM 2103 O LYS A1077 5.203 -65.755 28.770 1.00 56.21 O ANISOU 2103 O LYS A1077 6535 6398 8425 1591 -974 -948 O ATOM 2104 CB LYS A1077 2.032 -64.886 29.069 1.00 51.93 C ANISOU 2104 CB LYS A1077 6119 5711 7901 1344 -953 -809 C ATOM 2105 CG LYS A1077 2.137 -66.190 29.848 1.00 57.78 C ANISOU 2105 CG LYS A1077 6993 6494 8468 1433 -1045 -805 C ATOM 2106 CD LYS A1077 0.770 -66.800 30.112 1.00 63.24 C ANISOU 2106 CD LYS A1077 7833 7133 9064 1373 -1075 -705 C ATOM 2107 CE LYS A1077 0.896 -68.144 30.807 1.00 68.51 C ANISOU 2107 CE LYS A1077 8664 7822 9547 1458 -1156 -692 C ATOM 2108 NZ LYS A1077 1.517 -69.172 29.922 1.00 73.28 N ANISOU 2108 NZ LYS A1077 9401 8383 10057 1542 -1179 -642 N ATOM 2109 N LEU A1078 4.240 -65.248 26.799 1.00 56.79 N ANISOU 2109 N LEU A1078 6711 6297 8569 1470 -845 -799 N ATOM 2110 CA LEU A1078 5.177 -66.079 26.050 1.00 56.14 C ANISOU 2110 CA LEU A1078 6695 6210 8425 1581 -820 -779 C ATOM 2111 C LEU A1078 6.600 -65.557 26.169 1.00 57.24 C ANISOU 2111 C LEU A1078 6623 6443 8682 1638 -770 -885 C ATOM 2112 O LEU A1078 7.553 -66.343 26.144 1.00 47.99 O ANISOU 2112 O LEU A1078 5452 5324 7459 1771 -779 -902 O ATOM 2113 CB LEU A1078 4.761 -66.146 24.583 1.00 45.74 C ANISOU 2113 CB LEU A1078 5520 4767 7091 1540 -747 -670 C ATOM 2114 CG LEU A1078 3.407 -66.790 24.301 1.00 48.27 C ANISOU 2114 CG LEU A1078 6053 4994 7292 1477 -814 -553 C ATOM 2115 CD1 LEU A1078 3.009 -66.562 22.852 1.00 50.71 C ANISOU 2115 CD1 LEU A1078 6477 5183 7607 1416 -754 -458 C ATOM 2116 CD2 LEU A1078 3.449 -68.274 24.622 1.00 45.21 C ANISOU 2116 CD2 LEU A1078 5852 4604 6721 1572 -894 -522 C ATOM 2117 N ALA A1079 6.759 -64.238 26.299 1.00 56.68 N ANISOU 2117 N ALA A1079 6369 6393 8774 1540 -715 -955 N ATOM 2118 CA ALA A1079 8.079 -63.643 26.466 1.00 60.97 C ANISOU 2118 CA ALA A1079 6686 7029 9449 1561 -673 -1061 C ATOM 2119 C ALA A1079 8.638 -63.900 27.860 1.00 63.26 C ANISOU 2119 C ALA A1079 6871 7454 9712 1624 -800 -1166 C ATOM 2120 O ALA A1079 9.837 -64.163 28.013 1.00 69.31 O ANISOU 2120 O ALA A1079 7502 8319 10513 1716 -816 -1225 O ATOM 2121 CB ALA A1079 8.016 -62.141 26.183 1.00 57.54 C ANISOU 2121 CB ALA A1079 6119 6556 9190 1417 -577 -1103 C ATOM 2122 N ASN A1080 7.788 -63.826 28.886 1.00 61.57 N ANISOU 2122 N ASN A1080 6714 7245 9433 1580 -889 -1187 N ATOM 2123 CA ASN A1080 8.236 -64.108 30.243 1.00 62.31 C ANISOU 2123 CA ASN A1080 6750 7455 9470 1642 -1020 -1280 C ATOM 2124 C ASN A1080 8.638 -65.565 30.427 1.00 65.80 C ANISOU 2124 C ASN A1080 7307 7939 9754 1810 -1104 -1240 C ATOM 2125 O ASN A1080 9.423 -65.869 31.332 1.00 65.89 O ANISOU 2125 O ASN A1080 7239 8064 9733 1899 -1211 -1317 O ATOM 2126 CB ASN A1080 7.143 -63.738 31.247 1.00 60.06 C ANISOU 2126 CB ASN A1080 6541 7148 9133 1561 -1070 -1300 C ATOM 2127 CG ASN A1080 6.810 -62.254 31.232 1.00 59.05 C ANISOU 2127 CG ASN A1080 6302 6977 9158 1414 -992 -1354 C ATOM 2128 OD1 ASN A1080 7.692 -61.405 31.084 1.00 58.63 O ANISOU 2128 OD1 ASN A1080 6072 6959 9245 1366 -955 -1438 O ATOM 2129 ND2 ASN A1080 5.528 -61.935 31.386 1.00 57.64 N ANISOU 2129 ND2 ASN A1080 6226 6718 8958 1341 -960 -1303 N ATOM 2130 N GLU A1081 8.123 -66.468 29.595 1.00 69.29 N ANISOU 2130 N GLU A1081 7947 8289 10092 1857 -1065 -1122 N ATOM 2131 CA GLU A1081 8.496 -67.875 29.655 1.00 74.24 C ANISOU 2131 CA GLU A1081 8716 8928 10562 2022 -1127 -1076 C ATOM 2132 C GLU A1081 9.777 -68.178 28.890 1.00 77.11 C ANISOU 2132 C GLU A1081 8982 9333 10984 2147 -1065 -1082 C ATOM 2133 O GLU A1081 10.238 -69.324 28.919 1.00 84.36 O ANISOU 2133 O GLU A1081 10005 10264 11782 2311 -1106 -1049 O ATOM 2134 CB GLU A1081 7.358 -68.746 29.114 1.00 78.91 C ANISOU 2134 CB GLU A1081 9586 9389 11007 2004 -1115 -949 C ATOM 2135 CG GLU A1081 6.070 -68.660 29.916 1.00 83.87 C ANISOU 2135 CG GLU A1081 10314 9984 11568 1899 -1171 -927 C ATOM 2136 CD GLU A1081 4.919 -69.395 29.254 1.00 89.17 C ANISOU 2136 CD GLU A1081 11224 10528 12129 1845 -1157 -798 C ATOM 2137 OE1 GLU A1081 5.006 -69.675 28.040 1.00 90.67 O ANISOU 2137 OE1 GLU A1081 11497 10639 12315 1855 -1095 -729 O ATOM 2138 OE2 GLU A1081 3.926 -69.695 29.950 1.00 92.49 O ANISOU 2138 OE2 GLU A1081 11752 10925 12463 1788 -1208 -763 O ATOM 2139 N GLY A1082 10.358 -67.190 28.213 1.00 72.62 N ANISOU 2139 N GLY A1082 8220 8779 10593 2079 -956 -1119 N ATOM 2140 CA GLY A1082 11.549 -67.400 27.420 1.00 70.49 C ANISOU 2140 CA GLY A1082 7842 8546 10396 2188 -864 -1119 C ATOM 2141 C GLY A1082 11.305 -67.862 25.999 1.00 65.66 C ANISOU 2141 C GLY A1082 7416 7800 9731 2212 -728 -1009 C ATOM 2142 O GLY A1082 12.274 -68.039 25.250 1.00 67.81 O ANISOU 2142 O GLY A1082 7617 8089 10060 2309 -620 -1001 O ATOM 2143 N LYS A1083 10.049 -68.061 25.604 1.00 59.83 N ANISOU 2143 N LYS A1083 6915 6931 8887 2127 -730 -923 N ATOM 2144 CA LYS A1083 9.711 -68.499 24.250 1.00 59.34 C ANISOU 2144 CA LYS A1083 7066 6729 8752 2132 -625 -817 C ATOM 2145 C LYS A1083 9.713 -67.282 23.334 1.00 58.72 C ANISOU 2145 C LYS A1083 6884 6600 8826 2001 -488 -814 C ATOM 2146 O LYS A1083 8.673 -66.683 23.056 1.00 56.83 O ANISOU 2146 O LYS A1083 6717 6277 8598 1859 -488 -771 O ATOM 2147 CB LYS A1083 8.359 -69.200 24.238 1.00 58.48 C ANISOU 2147 CB LYS A1083 7238 6508 8473 2078 -706 -726 C ATOM 2148 CG LYS A1083 8.218 -70.291 25.281 1.00 58.48 C ANISOU 2148 CG LYS A1083 7351 6547 8323 2177 -841 -730 C ATOM 2149 CD LYS A1083 6.823 -70.881 25.262 1.00 58.49 C ANISOU 2149 CD LYS A1083 7608 6437 8179 2086 -910 -639 C ATOM 2150 CE LYS A1083 6.657 -71.929 26.343 1.00 58.31 C ANISOU 2150 CE LYS A1083 7710 6442 8004 2171 -1030 -640 C ATOM 2151 NZ LYS A1083 5.298 -72.536 26.290 1.00 58.12 N ANISOU 2151 NZ LYS A1083 7930 6306 7847 2065 -1086 -546 N ATOM 2152 N VAL A1084 10.901 -66.922 22.843 1.00 60.93 N ANISOU 2152 N VAL A1084 6993 6931 9228 2055 -365 -854 N ATOM 2153 CA VAL A1084 11.038 -65.711 22.038 1.00 61.54 C ANISOU 2153 CA VAL A1084 6962 6963 9459 1930 -221 -859 C ATOM 2154 C VAL A1084 10.405 -65.897 20.664 1.00 63.89 C ANISOU 2154 C VAL A1084 7520 7093 9663 1899 -122 -744 C ATOM 2155 O VAL A1084 9.728 -64.996 20.153 1.00 68.86 O ANISOU 2155 O VAL A1084 8178 7637 10347 1759 -79 -711 O ATOM 2156 CB VAL A1084 12.520 -65.305 21.934 1.00 61.06 C ANISOU 2156 CB VAL A1084 6630 7008 9560 1986 -108 -933 C ATOM 2157 CG1 VAL A1084 13.376 -66.500 21.530 1.00 67.70 C ANISOU 2157 CG1 VAL A1084 7536 7872 10317 2193 -55 -899 C ATOM 2158 CG2 VAL A1084 12.691 -64.157 20.948 1.00 57.70 C ANISOU 2158 CG2 VAL A1084 6136 6511 9276 1859 70 -922 C ATOM 2159 N LYS A1085 10.608 -67.063 20.043 1.00 61.21 N ANISOU 2159 N LYS A1085 7389 6695 9172 2034 -91 -679 N ATOM 2160 CA LYS A1085 10.022 -67.312 18.730 1.00 58.08 C ANISOU 2160 CA LYS A1085 7276 6131 8662 2005 -13 -572 C ATOM 2161 C LYS A1085 8.501 -67.329 18.797 1.00 49.74 C ANISOU 2161 C LYS A1085 6404 4985 7509 1877 -148 -506 C ATOM 2162 O LYS A1085 7.826 -66.814 17.897 1.00 54.22 O ANISOU 2162 O LYS A1085 7094 5440 8069 1772 -108 -437 O ATOM 2163 CB LYS A1085 10.547 -68.629 18.159 1.00 57.78 C ANISOU 2163 CB LYS A1085 7450 6041 8463 2183 40 -526 C ATOM 2164 CG LYS A1085 11.940 -68.544 17.552 1.00 60.15 C ANISOU 2164 CG LYS A1085 7622 6380 8854 2303 239 -553 C ATOM 2165 CD LYS A1085 11.931 -67.753 16.255 1.00 61.75 C ANISOU 2165 CD LYS A1085 7895 6467 9098 2212 417 -504 C ATOM 2166 CE LYS A1085 13.290 -67.794 15.575 1.00 65.25 C ANISOU 2166 CE LYS A1085 8241 6936 9615 2340 644 -518 C ATOM 2167 NZ LYS A1085 13.271 -67.114 14.249 1.00 66.14 N ANISOU 2167 NZ LYS A1085 8476 6916 9738 2258 835 -460 N ATOM 2168 N GLU A1086 7.939 -67.918 19.854 1.00 51.46 N ANISOU 2168 N GLU A1086 6643 5255 7655 1887 -308 -519 N ATOM 2169 CA GLU A1086 6.487 -67.943 19.989 1.00 53.84 C ANISOU 2169 CA GLU A1086 7086 5487 7885 1762 -429 -454 C ATOM 2170 C GLU A1086 5.941 -66.570 20.355 1.00 54.07 C ANISOU 2170 C GLU A1086 6923 5545 8077 1618 -435 -484 C ATOM 2171 O GLU A1086 4.784 -66.262 20.047 1.00 53.71 O ANISOU 2171 O GLU A1086 6971 5422 8016 1505 -484 -413 O ATOM 2172 CB GLU A1086 6.072 -68.987 21.029 1.00 60.32 C ANISOU 2172 CB GLU A1086 7992 6348 8580 1812 -575 -456 C ATOM 2173 CG GLU A1086 4.588 -69.340 21.008 1.00 65.11 C ANISOU 2173 CG GLU A1086 8787 6869 9084 1694 -689 -367 C ATOM 2174 CD GLU A1086 4.242 -70.508 21.920 1.00 69.07 C ANISOU 2174 CD GLU A1086 9414 7389 9442 1744 -809 -359 C ATOM 2175 OE1 GLU A1086 5.173 -71.133 22.475 1.00 70.70 O ANISOU 2175 OE1 GLU A1086 9596 7661 9605 1892 -809 -415 O ATOM 2176 OE2 GLU A1086 3.036 -70.800 22.080 1.00 69.43 O ANISOU 2176 OE2 GLU A1086 9579 7382 9419 1636 -903 -293 O ATOM 2177 N ALA A1087 6.756 -65.731 21.000 1.00 52.55 N ANISOU 2177 N ALA A1087 6463 5461 8043 1621 -387 -589 N ATOM 2178 CA ALA A1087 6.319 -64.378 21.325 1.00 50.03 C ANISOU 2178 CA ALA A1087 5980 5153 7877 1489 -375 -626 C ATOM 2179 C ALA A1087 6.289 -63.495 20.083 1.00 50.16 C ANISOU 2179 C ALA A1087 6026 5063 7969 1414 -244 -575 C ATOM 2180 O ALA A1087 5.362 -62.696 19.904 1.00 46.66 O ANISOU 2180 O ALA A1087 5598 4555 7576 1306 -256 -534 O ATOM 2181 CB ALA A1087 7.230 -63.775 22.394 1.00 50.45 C ANISOU 2181 CB ALA A1087 5764 5343 8064 1502 -374 -760 C ATOM 2182 N GLN A1088 7.292 -63.626 19.214 1.00 51.55 N ANISOU 2182 N GLN A1088 6217 5218 8152 1479 -111 -572 N ATOM 2183 CA GLN A1088 7.304 -62.844 17.982 1.00 53.26 C ANISOU 2183 CA GLN A1088 6497 5322 8419 1413 28 -517 C ATOM 2184 C GLN A1088 6.142 -63.221 17.073 1.00 52.16 C ANISOU 2184 C GLN A1088 6642 5042 8136 1373 -28 -388 C ATOM 2185 O GLN A1088 5.556 -62.354 16.414 1.00 47.93 O ANISOU 2185 O GLN A1088 6152 4413 7644 1280 7 -332 O ATOM 2186 CB GLN A1088 8.635 -63.032 17.260 1.00 50.09 C ANISOU 2186 CB GLN A1088 6065 4927 8040 1502 198 -536 C ATOM 2187 CG GLN A1088 9.810 -62.511 18.045 1.00 52.89 C ANISOU 2187 CG GLN A1088 6106 5424 8567 1517 254 -659 C ATOM 2188 CD GLN A1088 11.134 -62.885 17.425 1.00 60.10 C ANISOU 2188 CD GLN A1088 6963 6366 9505 1627 417 -672 C ATOM 2189 OE1 GLN A1088 11.224 -63.833 16.643 1.00 62.31 O ANISOU 2189 OE1 GLN A1088 7457 6577 9640 1734 468 -601 O ATOM 2190 NE2 GLN A1088 12.178 -62.139 17.770 1.00 62.12 N ANISOU 2190 NE2 GLN A1088 6931 6722 9949 1599 506 -763 N ATOM 2191 N ALA A1089 5.792 -64.509 17.023 1.00 49.70 N ANISOU 2191 N ALA A1089 6529 4707 7647 1441 -124 -337 N ATOM 2192 CA ALA A1089 4.671 -64.933 16.192 1.00 47.45 C ANISOU 2192 CA ALA A1089 6515 4292 7220 1386 -203 -216 C ATOM 2193 C ALA A1089 3.349 -64.425 16.749 1.00 49.17 C ANISOU 2193 C ALA A1089 6681 4515 7486 1270 -339 -183 C ATOM 2194 O ALA A1089 2.443 -64.069 15.988 1.00 50.71 O ANISOU 2194 O ALA A1089 6997 4612 7658 1189 -377 -90 O ATOM 2195 CB ALA A1089 4.651 -66.455 16.068 1.00 47.64 C ANISOU 2195 CB ALA A1089 6773 4285 7043 1474 -273 -178 C ATOM 2196 N ALA A1090 3.216 -64.387 18.076 1.00 49.13 N ANISOU 2196 N ALA A1090 6498 4623 7544 1269 -412 -254 N ATOM 2197 CA ALA A1090 2.001 -63.848 18.674 1.00 47.79 C ANISOU 2197 CA ALA A1090 6259 4465 7436 1172 -511 -227 C ATOM 2198 C ALA A1090 1.892 -62.346 18.453 1.00 49.55 C ANISOU 2198 C ALA A1090 6341 4659 7825 1100 -428 -239 C ATOM 2199 O ALA A1090 0.784 -61.824 18.290 1.00 48.22 O ANISOU 2199 O ALA A1090 6190 4440 7692 1024 -484 -167 O ATOM 2200 CB ALA A1090 1.960 -64.172 20.168 1.00 48.14 C ANISOU 2200 CB ALA A1090 6171 4629 7493 1197 -587 -306 C ATOM 2201 N ALA A1091 3.025 -61.640 18.440 1.00 53.30 N ANISOU 2201 N ALA A1091 6676 5165 8410 1122 -295 -326 N ATOM 2202 CA ALA A1091 3.016 -60.206 18.178 1.00 53.74 C ANISOU 2202 CA ALA A1091 6625 5175 8620 1048 -199 -340 C ATOM 2203 C ALA A1091 2.707 -59.890 16.723 1.00 59.24 C ANISOU 2203 C ALA A1091 7502 5730 9279 1017 -141 -229 C ATOM 2204 O ALA A1091 2.319 -58.758 16.416 1.00 63.47 O ANISOU 2204 O ALA A1091 8003 6198 9915 953 -94 -203 O ATOM 2205 CB ALA A1091 4.358 -59.589 18.569 1.00 51.00 C ANISOU 2205 CB ALA A1091 6079 4899 8402 1061 -74 -465 C ATOM 2206 N GLU A1092 2.876 -60.861 15.822 1.00 60.07 N ANISOU 2206 N GLU A1092 7818 5777 9229 1066 -143 -162 N ATOM 2207 CA GLU A1092 2.531 -60.649 14.422 1.00 60.66 C ANISOU 2207 CA GLU A1092 8106 5709 9234 1037 -106 -51 C ATOM 2208 C GLU A1092 1.024 -60.639 14.202 1.00 53.42 C ANISOU 2208 C GLU A1092 7298 4732 8268 971 -268 61 C ATOM 2209 O GLU A1092 0.555 -60.046 13.225 1.00 52.47 O ANISOU 2209 O GLU A1092 7298 4500 8139 930 -258 151 O ATOM 2210 CB GLU A1092 3.188 -61.725 13.555 1.00 68.48 C ANISOU 2210 CB GLU A1092 9313 6649 10058 1113 -55 -21 C ATOM 2211 CG GLU A1092 3.509 -61.276 12.139 1.00 77.15 C ANISOU 2211 CG GLU A1092 10591 7611 11113 1105 81 46 C ATOM 2212 CD GLU A1092 4.622 -60.241 12.088 1.00 83.60 C ANISOU 2212 CD GLU A1092 11230 8444 12092 1102 291 -30 C ATOM 2213 OE1 GLU A1092 5.384 -60.129 13.072 1.00 85.63 O ANISOU 2213 OE1 GLU A1092 11239 8827 12469 1126 333 -143 O ATOM 2214 OE2 GLU A1092 4.735 -59.538 11.062 1.00 86.28 O ANISOU 2214 OE2 GLU A1092 11683 8667 12434 1069 410 26 O ATOM 2215 N GLN A1093 0.257 -61.277 15.090 1.00 50.83 N ANISOU 2215 N GLN A1093 6925 4477 7911 961 -417 63 N ATOM 2216 CA GLN A1093 -1.196 -61.180 15.031 1.00 51.99 C ANISOU 2216 CA GLN A1093 7111 4591 8052 891 -567 166 C ATOM 2217 C GLN A1093 -1.690 -59.770 15.320 1.00 51.14 C ANISOU 2217 C GLN A1093 6831 4478 8121 851 -532 165 C ATOM 2218 O GLN A1093 -2.845 -59.458 15.016 1.00 50.63 O ANISOU 2218 O GLN A1093 6794 4369 8074 805 -631 267 O ATOM 2219 CB GLN A1093 -1.833 -62.157 16.023 1.00 55.44 C ANISOU 2219 CB GLN A1093 7516 5114 8434 884 -704 161 C ATOM 2220 CG GLN A1093 -1.397 -63.601 15.853 1.00 62.69 C ANISOU 2220 CG GLN A1093 8621 6029 9171 930 -745 160 C ATOM 2221 CD GLN A1093 -1.898 -64.214 14.562 1.00 72.12 C ANISOU 2221 CD GLN A1093 10097 7098 10206 893 -825 278 C ATOM 2222 OE1 GLN A1093 -3.024 -64.708 14.495 1.00 77.71 O ANISOU 2222 OE1 GLN A1093 10889 7786 10853 818 -983 366 O ATOM 2223 NE2 GLN A1093 -1.063 -64.186 13.528 1.00 74.49 N ANISOU 2223 NE2 GLN A1093 10551 7314 10437 939 -714 282 N ATOM 2224 N LEU A1094 -0.847 -58.917 15.906 1.00 53.34 N ANISOU 2224 N LEU A1094 6933 4800 8534 867 -396 54 N ATOM 2225 CA LEU A1094 -1.261 -57.549 16.195 1.00 55.45 C ANISOU 2225 CA LEU A1094 7061 5043 8964 831 -348 44 C ATOM 2226 C LEU A1094 -1.496 -56.750 14.921 1.00 59.55 C ANISOU 2226 C LEU A1094 7709 5422 9493 809 -299 143 C ATOM 2227 O LEU A1094 -2.305 -55.815 14.920 1.00 64.25 O ANISOU 2227 O LEU A1094 8257 5971 10185 788 -316 194 O ATOM 2228 CB LEU A1094 -0.215 -56.857 17.068 1.00 54.72 C ANISOU 2228 CB LEU A1094 6778 5016 8998 837 -219 -106 C ATOM 2229 CG LEU A1094 -0.090 -57.381 18.498 1.00 52.32 C ANISOU 2229 CG LEU A1094 6330 4848 8701 858 -276 -208 C ATOM 2230 CD1 LEU A1094 1.187 -56.873 19.145 1.00 52.79 C ANISOU 2230 CD1 LEU A1094 6232 4972 8856 862 -165 -357 C ATOM 2231 CD2 LEU A1094 -1.299 -56.969 19.311 1.00 50.27 C ANISOU 2231 CD2 LEU A1094 5987 4609 8506 835 -351 -185 C ATOM 2232 N LYS A1095 -0.810 -57.100 13.829 1.00 60.67 N ANISOU 2232 N LYS A1095 8030 5492 9531 823 -234 174 N ATOM 2233 CA LYS A1095 -1.002 -56.375 12.579 1.00 60.87 C ANISOU 2233 CA LYS A1095 8213 5373 9541 804 -185 273 C ATOM 2234 C LYS A1095 -2.414 -56.547 12.034 1.00 62.41 C ANISOU 2234 C LYS A1095 8533 5512 9667 783 -369 419 C ATOM 2235 O LYS A1095 -2.963 -55.613 11.438 1.00 65.22 O ANISOU 2235 O LYS A1095 8935 5774 10074 771 -369 501 O ATOM 2236 CB LYS A1095 0.026 -56.827 11.548 1.00 61.18 C ANISOU 2236 CB LYS A1095 8438 5347 9462 829 -66 276 C ATOM 2237 CG LYS A1095 1.444 -56.446 11.909 1.00 62.24 C ANISOU 2237 CG LYS A1095 8426 5527 9696 843 135 148 C ATOM 2238 CD LYS A1095 2.416 -56.911 10.848 1.00 63.53 C ANISOU 2238 CD LYS A1095 8768 5623 9746 878 273 163 C ATOM 2239 CE LYS A1095 3.818 -56.423 11.149 1.00 65.93 C ANISOU 2239 CE LYS A1095 8894 5977 10178 881 482 46 C ATOM 2240 NZ LYS A1095 4.781 -56.859 10.101 1.00 68.67 N ANISOU 2240 NZ LYS A1095 9404 6261 10427 926 647 66 N ATOM 2241 N THR A1096 -3.017 -57.722 12.229 1.00 61.48 N ANISOU 2241 N THR A1096 8472 5449 9438 777 -532 457 N ATOM 2242 CA THR A1096 -4.401 -57.915 11.811 1.00 62.38 C ANISOU 2242 CA THR A1096 8666 5530 9506 740 -727 595 C ATOM 2243 C THR A1096 -5.338 -57.002 12.593 1.00 62.96 C ANISOU 2243 C THR A1096 8519 5648 9756 733 -766 611 C ATOM 2244 O THR A1096 -6.222 -56.356 12.016 1.00 65.22 O ANISOU 2244 O THR A1096 8834 5867 10081 725 -841 724 O ATOM 2245 CB THR A1096 -4.806 -59.379 11.984 1.00 61.57 C ANISOU 2245 CB THR A1096 8654 5481 9260 715 -882 619 C ATOM 2246 OG1 THR A1096 -3.879 -60.218 11.283 1.00 65.14 O ANISOU 2246 OG1 THR A1096 9325 5881 9546 740 -825 597 O ATOM 2247 CG2 THR A1096 -6.205 -59.610 11.434 1.00 61.66 C ANISOU 2247 CG2 THR A1096 8750 5455 9222 655 -1096 767 C ATOM 2248 N THR A1097 -5.154 -56.931 13.916 1.00 58.61 N ANISOU 2248 N THR A1097 7753 5208 9310 745 -714 502 N ATOM 2249 CA THR A1097 -5.979 -56.052 14.739 1.00 54.90 C ANISOU 2249 CA THR A1097 7082 4774 9003 752 -721 505 C ATOM 2250 C THR A1097 -5.750 -54.588 14.390 1.00 55.55 C ANISOU 2250 C THR A1097 7139 4760 9207 773 -590 502 C ATOM 2251 O THR A1097 -6.687 -53.782 14.440 1.00 56.61 O ANISOU 2251 O THR A1097 7201 4863 9446 791 -623 573 O ATOM 2252 CB THR A1097 -5.688 -56.296 16.222 1.00 51.17 C ANISOU 2252 CB THR A1097 6427 4427 8590 762 -676 376 C ATOM 2253 OG1 THR A1097 -5.814 -57.694 16.510 1.00 51.94 O ANISOU 2253 OG1 THR A1097 6577 4598 8559 744 -786 381 O ATOM 2254 CG2 THR A1097 -6.655 -55.517 17.104 1.00 46.39 C ANISOU 2254 CG2 THR A1097 5636 3856 8133 774 -681 386 C ATOM 2255 N ARG A1098 -4.518 -54.233 14.022 1.00 56.40 N ANISOU 2255 N ARG A1098 7307 4817 9307 775 -434 424 N ATOM 2256 CA ARG A1098 -4.202 -52.850 13.680 1.00 59.23 C ANISOU 2256 CA ARG A1098 7662 5069 9776 779 -292 414 C ATOM 2257 C ARG A1098 -4.940 -52.410 12.422 1.00 62.27 C ANISOU 2257 C ARG A1098 8219 5322 10118 790 -356 574 C ATOM 2258 O ARG A1098 -5.549 -51.334 12.390 1.00 61.42 O ANISOU 2258 O ARG A1098 8070 5146 10120 814 -339 625 O ATOM 2259 CB ARG A1098 -2.694 -52.694 13.496 1.00 48.88 C ANISOU 2259 CB ARG A1098 6375 3737 8459 762 -111 304 C ATOM 2260 CG ARG A1098 -2.269 -51.305 13.072 1.00 56.18 C ANISOU 2260 CG ARG A1098 7319 4537 9489 745 52 294 C ATOM 2261 CD ARG A1098 -0.832 -51.292 12.589 1.00 50.33 C ANISOU 2261 CD ARG A1098 6630 3766 8726 716 226 219 C ATOM 2262 NE ARG A1098 -0.643 -52.143 11.418 1.00 54.98 N ANISOU 2262 NE ARG A1098 7440 4308 9144 732 203 306 N ATOM 2263 CZ ARG A1098 0.544 -52.477 10.923 1.00 56.22 C ANISOU 2263 CZ ARG A1098 7661 4454 9246 726 343 259 C ATOM 2264 NH1 ARG A1098 1.653 -52.032 11.500 1.00 56.97 N ANISOU 2264 NH1 ARG A1098 7590 4597 9460 695 503 128 N ATOM 2265 NH2 ARG A1098 0.622 -53.261 9.855 1.00 58.13 N ANISOU 2265 NH2 ARG A1098 8133 4638 9317 750 323 343 N ATOM 2266 N ASN A1099 -4.898 -53.233 11.373 1.00 66.97 N ANISOU 2266 N ASN A1099 9024 5874 10546 778 -435 655 N ATOM 2267 CA ASN A1099 -5.501 -52.861 10.099 1.00 70.32 C ANISOU 2267 CA ASN A1099 9650 6167 10902 786 -507 805 C ATOM 2268 C ASN A1099 -7.022 -52.900 10.134 1.00 76.51 C ANISOU 2268 C ASN A1099 10381 6976 11715 797 -722 934 C ATOM 2269 O ASN A1099 -7.664 -52.229 9.319 1.00 83.91 O ANISOU 2269 O ASN A1099 11415 7810 12655 821 -783 1057 O ATOM 2270 CB ASN A1099 -4.985 -53.781 8.993 1.00 69.24 C ANISOU 2270 CB ASN A1099 9779 5972 10558 768 -528 847 C ATOM 2271 CG ASN A1099 -3.474 -53.808 8.920 1.00 67.60 C ANISOU 2271 CG ASN A1099 9606 5750 10330 768 -305 729 C ATOM 2272 OD1 ASN A1099 -2.806 -52.883 9.378 1.00 66.57 O ANISOU 2272 OD1 ASN A1099 9343 5613 10339 766 -131 641 O ATOM 2273 ND2 ASN A1099 -2.926 -54.869 8.344 1.00 67.32 N ANISOU 2273 ND2 ASN A1099 9748 5707 10124 768 -306 729 N ATOM 2274 N ALA A1100 -7.613 -53.661 11.053 1.00 75.06 N ANISOU 2274 N ALA A1100 10039 6924 11554 781 -835 914 N ATOM 2275 CA ALA A1100 -9.059 -53.841 11.080 1.00 73.86 C ANISOU 2275 CA ALA A1100 9816 6813 11434 778 -1041 1041 C ATOM 2276 C ALA A1100 -9.764 -52.968 12.105 1.00 73.68 C ANISOU 2276 C ALA A1100 9538 6845 11615 826 -1004 1029 C ATOM 2277 O ALA A1100 -10.942 -52.647 11.918 1.00 74.63 O ANISOU 2277 O ALA A1100 9591 6962 11802 852 -1133 1155 O ATOM 2278 CB ALA A1100 -9.403 -55.309 11.355 1.00 72.36 C ANISOU 2278 CB ALA A1100 9636 6724 11133 717 -1195 1048 C ATOM 2279 N TYR A1101 -9.083 -52.573 13.180 1.00 72.30 N ANISOU 2279 N TYR A1101 9219 6716 11535 841 -834 882 N ATOM 2280 CA TYR A1101 -9.736 -51.829 14.249 1.00 71.17 C ANISOU 2280 CA TYR A1101 8854 6622 11566 889 -787 857 C ATOM 2281 C TYR A1101 -8.973 -50.561 14.607 1.00 67.64 C ANISOU 2281 C TYR A1101 8373 6098 11229 924 -577 751 C ATOM 2282 O TYR A1101 -9.554 -49.472 14.648 1.00 69.38 O ANISOU 2282 O TYR A1101 8540 6249 11572 985 -534 799 O ATOM 2283 CB TYR A1101 -9.886 -52.707 15.494 1.00 74.20 C ANISOU 2283 CB TYR A1101 9084 7155 11955 863 -812 777 C ATOM 2284 CG TYR A1101 -10.802 -53.896 15.319 1.00 77.21 C ANISOU 2284 CG TYR A1101 9470 7613 12254 815 -1014 882 C ATOM 2285 CD1 TYR A1101 -12.163 -53.789 15.572 1.00 80.16 C ANISOU 2285 CD1 TYR A1101 9695 8035 12727 832 -1121 994 C ATOM 2286 CD2 TYR A1101 -10.305 -55.129 14.913 1.00 78.25 C ANISOU 2286 CD2 TYR A1101 9753 7765 12214 752 -1092 870 C ATOM 2287 CE1 TYR A1101 -13.007 -54.873 15.420 1.00 82.46 C ANISOU 2287 CE1 TYR A1101 9979 8397 12954 765 -1309 1091 C ATOM 2288 CE2 TYR A1101 -11.141 -56.221 14.758 1.00 79.96 C ANISOU 2288 CE2 TYR A1101 9993 8038 12352 690 -1279 963 C ATOM 2289 CZ TYR A1101 -12.491 -56.086 15.014 1.00 82.55 C ANISOU 2289 CZ TYR A1101 10162 8417 12786 687 -1391 1072 C ATOM 2290 OH TYR A1101 -13.331 -57.166 14.863 1.00 83.75 O ANISOU 2290 OH TYR A1101 10325 8626 12871 603 -1579 1165 O ATOM 2291 N ILE A1102 -7.673 -50.696 14.874 1.00 63.15 N ANISOU 2291 N ILE A1102 7835 5539 10622 884 -447 609 N ATOM 2292 CA ILE A1102 -6.909 -49.578 15.419 1.00 58.37 C ANISOU 2292 CA ILE A1102 7171 4880 10129 890 -256 485 C ATOM 2293 C ILE A1102 -6.714 -48.491 14.371 1.00 58.62 C ANISOU 2293 C ILE A1102 7345 4742 10188 904 -169 550 C ATOM 2294 O ILE A1102 -6.768 -47.294 14.680 1.00 59.14 O ANISOU 2294 O ILE A1102 7371 4723 10376 933 -55 520 O ATOM 2295 CB ILE A1102 -5.563 -50.074 15.976 1.00 55.73 C ANISOU 2295 CB ILE A1102 6807 4616 9752 836 -162 321 C ATOM 2296 CG1 ILE A1102 -5.781 -51.238 16.947 1.00 48.24 C ANISOU 2296 CG1 ILE A1102 5753 3825 8751 831 -261 273 C ATOM 2297 CG2 ILE A1102 -4.814 -48.927 16.641 1.00 54.89 C ANISOU 2297 CG2 ILE A1102 6623 4464 9769 820 15 186 C ATOM 2298 CD1 ILE A1102 -6.706 -50.924 18.103 1.00 48.21 C ANISOU 2298 CD1 ILE A1102 5588 3882 8849 865 -279 258 C ATOM 2299 N GLN A1103 -6.479 -48.884 13.118 1.00 57.61 N ANISOU 2299 N GLN A1103 7408 4547 9935 886 -214 638 N ATOM 2300 CA GLN A1103 -6.310 -47.899 12.057 1.00 58.52 C ANISOU 2300 CA GLN A1103 7691 4490 10053 901 -131 712 C ATOM 2301 C GLN A1103 -7.594 -47.117 11.808 1.00 58.50 C ANISOU 2301 C GLN A1103 7684 4415 10128 981 -218 852 C ATOM 2302 O GLN A1103 -7.539 -45.952 11.399 1.00 58.43 O ANISOU 2302 O GLN A1103 7757 4261 10183 1014 -113 884 O ATOM 2303 CB GLN A1103 -5.844 -48.588 10.776 1.00 60.57 C ANISOU 2303 CB GLN A1103 8180 4695 10138 870 -166 782 C ATOM 2304 CG GLN A1103 -5.432 -47.639 9.667 1.00 62.04 C ANISOU 2304 CG GLN A1103 8571 4698 10304 873 -44 843 C ATOM 2305 CD GLN A1103 -5.051 -48.367 8.392 1.00 63.93 C ANISOU 2305 CD GLN A1103 9063 4878 10349 851 -78 919 C ATOM 2306 OE1 GLN A1103 -4.718 -49.556 8.413 1.00 61.96 O ANISOU 2306 OE1 GLN A1103 8830 4722 9988 823 -135 884 O ATOM 2307 NE2 GLN A1103 -5.105 -47.657 7.269 1.00 66.93 N ANISOU 2307 NE2 GLN A1103 9663 5091 10675 870 -37 1026 N ATOM 2308 N LYS A1104 -8.754 -47.729 12.056 1.00 60.43 N ANISOU 2308 N LYS A1104 7830 4757 10375 1015 -406 941 N ATOM 2309 CA LYS A1104 -10.015 -47.020 11.864 1.00 69.20 C ANISOU 2309 CA LYS A1104 8898 5819 11577 1105 -498 1081 C ATOM 2310 C LYS A1104 -10.266 -46.017 12.985 1.00 70.96 C ANISOU 2310 C LYS A1104 8945 6037 11981 1167 -366 1007 C ATOM 2311 O LYS A1104 -10.774 -44.918 12.736 1.00 73.45 O ANISOU 2311 O LYS A1104 9284 6236 12388 1253 -325 1082 O ATOM 2312 CB LYS A1104 -11.166 -48.018 11.768 1.00 76.11 C ANISOU 2312 CB LYS A1104 9700 6809 12411 1108 -740 1202 C ATOM 2313 CG LYS A1104 -11.074 -48.955 10.576 1.00 81.67 C ANISOU 2313 CG LYS A1104 10614 7494 12924 1049 -894 1291 C ATOM 2314 CD LYS A1104 -11.437 -48.244 9.282 1.00 85.24 C ANISOU 2314 CD LYS A1104 11262 7793 13332 1100 -958 1442 C ATOM 2315 CE LYS A1104 -11.296 -49.177 8.090 1.00 87.20 C ANISOU 2315 CE LYS A1104 11757 8008 13366 1037 -1105 1521 C ATOM 2316 NZ LYS A1104 -12.019 -50.461 8.302 1.00 87.51 N ANISOU 2316 NZ LYS A1104 11716 8187 13345 978 -1323 1561 N ATOM 2317 N TYR A1105 -9.919 -46.378 14.225 1.00 67.57 N ANISOU 2317 N TYR A1105 8357 5724 11593 1132 -298 862 N ATOM 2318 CA TYR A1105 -10.101 -45.457 15.344 1.00 65.83 C ANISOU 2318 CA TYR A1105 7998 5491 11523 1186 -164 775 C ATOM 2319 C TYR A1105 -9.271 -44.192 15.161 1.00 61.88 C ANISOU 2319 C TYR A1105 7609 4825 11076 1181 30 702 C ATOM 2320 O TYR A1105 -9.750 -43.083 15.428 1.00 62.22 O ANISOU 2320 O TYR A1105 7635 4769 11237 1262 115 720 O ATOM 2321 CB TYR A1105 -9.738 -46.145 16.662 1.00 68.97 C ANISOU 2321 CB TYR A1105 8247 6038 11921 1136 -131 623 C ATOM 2322 CG TYR A1105 -9.727 -45.213 17.859 1.00 75.97 C ANISOU 2322 CG TYR A1105 9030 6902 12934 1175 24 505 C ATOM 2323 CD1 TYR A1105 -10.904 -44.896 18.527 1.00 81.49 C ANISOU 2323 CD1 TYR A1105 9597 7630 13737 1273 13 562 C ATOM 2324 CD2 TYR A1105 -8.540 -44.646 18.318 1.00 78.84 C ANISOU 2324 CD2 TYR A1105 9430 7212 13312 1112 183 337 C ATOM 2325 CE1 TYR A1105 -10.901 -44.044 19.618 1.00 82.70 C ANISOU 2325 CE1 TYR A1105 9687 7748 13989 1316 166 451 C ATOM 2326 CE2 TYR A1105 -8.529 -43.789 19.408 1.00 81.50 C ANISOU 2326 CE2 TYR A1105 9703 7515 13748 1138 314 223 C ATOM 2327 CZ TYR A1105 -9.713 -43.493 20.055 1.00 83.99 C ANISOU 2327 CZ TYR A1105 9916 7848 14149 1244 310 278 C ATOM 2328 OH TYR A1105 -9.714 -42.644 21.141 1.00 85.21 O ANISOU 2328 OH TYR A1105 10035 7954 14386 1277 452 162 O ATOM 2329 N LEU A1106 -8.027 -44.339 14.718 1.00 57.22 N ANISOU 2329 N LEU A1106 7135 4199 10408 1087 112 620 N ATOM 2330 CA LEU A1106 -7.155 -43.198 14.476 1.00 60.87 C ANISOU 2330 CA LEU A1106 7707 4502 10920 1053 302 551 C ATOM 2331 C LEU A1106 -7.706 -42.308 13.368 1.00 67.57 C ANISOU 2331 C LEU A1106 8723 5172 11778 1127 303 709 C ATOM 2332 O LEU A1106 -7.841 -41.099 13.545 1.00 68.98 O ANISOU 2332 O LEU A1106 8934 5214 12059 1174 423 701 O ATOM 2333 CB LEU A1106 -5.742 -43.668 14.119 1.00 60.78 C ANISOU 2333 CB LEU A1106 7766 4505 10823 936 384 452 C ATOM 2334 CG LEU A1106 -4.914 -42.721 13.244 1.00 62.84 C ANISOU 2334 CG LEU A1106 8203 4583 11089 888 549 453 C ATOM 2335 CD1 LEU A1106 -3.567 -42.420 13.881 1.00 63.47 C ANISOU 2335 CD1 LEU A1106 8218 4674 11225 773 722 264 C ATOM 2336 CD2 LEU A1106 -4.725 -43.309 11.851 1.00 63.42 C ANISOU 2336 CD2 LEU A1106 8465 4614 11016 877 495 574 C ATOM 2337 N GLU A 219 -8.482 -42.857 12.447 1.00 61.76 N ANISOU 2337 N GLU A 219 10221 4513 8733 1752 -21 -706 N ATOM 2338 CA GLU A 219 -8.924 -41.999 11.356 1.00 60.56 C ANISOU 2338 CA GLU A 219 10069 4479 8461 1686 84 -801 C ATOM 2339 C GLU A 219 -10.213 -41.266 11.712 1.00 57.18 C ANISOU 2339 C GLU A 219 9699 4117 7912 1486 25 -726 C ATOM 2340 O GLU A 219 -10.426 -40.135 11.280 1.00 56.19 O ANISOU 2340 O GLU A 219 9489 4154 7707 1436 94 -747 O ATOM 2341 CB GLU A 219 -9.111 -42.818 10.080 1.00 65.43 C ANISOU 2341 CB GLU A 219 10817 5010 9032 1677 149 -942 C ATOM 2342 CG GLU A 219 -7.814 -43.384 9.532 1.00 70.97 C ANISOU 2342 CG GLU A 219 11448 5669 9846 1877 238 -1038 C ATOM 2343 CD GLU A 219 -8.035 -44.347 8.386 1.00 75.95 C ANISOU 2343 CD GLU A 219 12232 6192 10434 1866 284 -1171 C ATOM 2344 OE1 GLU A 219 -9.107 -44.279 7.749 1.00 76.73 O ANISOU 2344 OE1 GLU A 219 12462 6297 10396 1710 276 -1211 O ATOM 2345 OE2 GLU A 219 -7.137 -45.177 8.127 1.00 79.15 O ANISOU 2345 OE2 GLU A 219 12624 6504 10945 2013 322 -1237 O ATOM 2346 N ARG A 220 -11.074 -41.912 12.503 1.00 56.81 N ANISOU 2346 N ARG A 220 9766 3968 7853 1355 -96 -632 N ATOM 2347 CA ARG A 220 -12.266 -41.224 12.987 1.00 60.12 C ANISOU 2347 CA ARG A 220 10202 4466 8175 1156 -153 -546 C ATOM 2348 C ARG A 220 -11.905 -40.175 14.030 1.00 55.68 C ANISOU 2348 C ARG A 220 9432 4085 7639 1164 -172 -426 C ATOM 2349 O ARG A 220 -12.491 -39.085 14.051 1.00 54.20 O ANISOU 2349 O ARG A 220 9133 4088 7372 1041 -150 -392 O ATOM 2350 CB ARG A 220 -13.266 -42.226 13.562 1.00 70.39 C ANISOU 2350 CB ARG A 220 11662 5622 9462 1002 -265 -474 C ATOM 2351 CG ARG A 220 -13.746 -43.276 12.577 1.00 81.10 C ANISOU 2351 CG ARG A 220 13167 6860 10788 945 -256 -578 C ATOM 2352 CD ARG A 220 -14.961 -44.006 13.129 1.00 90.06 C ANISOU 2352 CD ARG A 220 14425 7904 11891 744 -358 -498 C ATOM 2353 NE ARG A 220 -15.027 -45.396 12.685 1.00 96.78 N ANISOU 2353 NE ARG A 220 15413 8586 12773 747 -382 -557 N ATOM 2354 CZ ARG A 220 -15.790 -45.835 11.689 1.00102.37 C ANISOU 2354 CZ ARG A 220 16230 9252 13415 639 -375 -653 C ATOM 2355 NH1 ARG A 220 -16.566 -44.991 11.022 1.00102.40 N ANISOU 2355 NH1 ARG A 220 16218 9374 13315 519 -350 -698 N ATOM 2356 NH2 ARG A 220 -15.778 -47.122 11.364 1.00106.03 N ANISOU 2356 NH2 ARG A 220 16818 9553 13914 652 -401 -702 N ATOM 2357 N ALA A 221 -10.946 -40.486 14.906 1.00 53.28 N ANISOU 2357 N ALA A 221 9077 3720 7445 1310 -221 -361 N ATOM 2358 CA ALA A 221 -10.492 -39.505 15.885 1.00 48.81 C ANISOU 2358 CA ALA A 221 8318 3319 6906 1330 -247 -257 C ATOM 2359 C ALA A 221 -9.777 -38.344 15.207 1.00 47.16 C ANISOU 2359 C ALA A 221 7913 3305 6701 1406 -130 -326 C ATOM 2360 O ALA A 221 -9.893 -37.193 15.644 1.00 46.30 O ANISOU 2360 O ALA A 221 7653 3383 6555 1338 -125 -265 O ATOM 2361 CB ALA A 221 -9.580 -40.173 16.913 1.00 47.89 C ANISOU 2361 CB ALA A 221 8204 3082 6911 1479 -340 -179 C ATOM 2362 N ARG A 222 -9.028 -38.630 14.142 1.00 48.48 N ANISOU 2362 N ARG A 222 8085 3425 6910 1546 -30 -455 N ATOM 2363 CA ARG A 222 -8.419 -37.564 13.358 1.00 47.42 C ANISOU 2363 CA ARG A 222 7784 3469 6766 1601 100 -527 C ATOM 2364 C ARG A 222 -9.480 -36.733 12.649 1.00 46.59 C ANISOU 2364 C ARG A 222 7690 3499 6513 1422 152 -554 C ATOM 2365 O ARG A 222 -9.358 -35.508 12.555 1.00 46.29 O ANISOU 2365 O ARG A 222 7494 3652 6443 1390 208 -539 O ATOM 2366 CB ARG A 222 -7.436 -38.165 12.357 1.00 50.17 C ANISOU 2366 CB ARG A 222 8156 3724 7184 1788 208 -663 C ATOM 2367 CG ARG A 222 -6.880 -37.196 11.334 1.00 53.04 C ANISOU 2367 CG ARG A 222 8382 4251 7519 1833 367 -753 C ATOM 2368 CD ARG A 222 -5.728 -37.849 10.600 1.00 57.83 C ANISOU 2368 CD ARG A 222 8988 4762 8223 2045 472 -872 C ATOM 2369 NE ARG A 222 -4.639 -38.172 11.518 1.00 63.39 N ANISOU 2369 NE ARG A 222 9553 5433 9098 2194 412 -813 N ATOM 2370 CZ ARG A 222 -3.831 -39.217 11.385 1.00 70.77 C ANISOU 2370 CZ ARG A 222 10476 6258 10154 2318 415 -862 C ATOM 2371 NH1 ARG A 222 -3.995 -40.060 10.374 1.00 72.75 N ANISOU 2371 NH1 ARG A 222 10860 6413 10370 2318 479 -977 N ATOM 2372 NH2 ARG A 222 -2.866 -39.428 12.270 1.00 72.67 N ANISOU 2372 NH2 ARG A 222 10576 6483 10553 2439 349 -797 N ATOM 2373 N SER A 223 -10.537 -37.381 12.159 1.00 51.58 N ANISOU 2373 N SER A 223 8508 4029 7059 1302 124 -591 N ATOM 2374 CA SER A 223 -11.592 -36.654 11.462 1.00 52.97 C ANISOU 2374 CA SER A 223 8701 4325 7100 1135 156 -618 C ATOM 2375 C SER A 223 -12.392 -35.782 12.424 1.00 49.96 C ANISOU 2375 C SER A 223 8223 4083 6676 983 84 -491 C ATOM 2376 O SER A 223 -12.747 -34.646 12.090 1.00 54.24 O ANISOU 2376 O SER A 223 8664 4798 7145 906 129 -490 O ATOM 2377 CB SER A 223 -12.505 -37.640 10.732 1.00 60.56 C ANISOU 2377 CB SER A 223 9884 5132 7992 1045 128 -691 C ATOM 2378 OG SER A 223 -13.500 -36.965 9.987 1.00 66.32 O ANISOU 2378 OG SER A 223 10629 5976 8595 892 148 -723 O ATOM 2379 N THR A 224 -12.676 -36.290 13.625 1.00 47.86 N ANISOU 2379 N THR A 224 7992 3740 6452 941 -25 -383 N ATOM 2380 CA THR A 224 -13.433 -35.506 14.598 1.00 45.71 C ANISOU 2380 CA THR A 224 7637 3596 6135 802 -84 -265 C ATOM 2381 C THR A 224 -12.665 -34.257 15.024 1.00 42.26 C ANISOU 2381 C THR A 224 6991 3341 5726 867 -47 -225 C ATOM 2382 O THR A 224 -13.246 -33.170 15.119 1.00 43.00 O ANISOU 2382 O THR A 224 6991 3597 5752 762 -34 -192 O ATOM 2383 CB THR A 224 -13.783 -36.376 15.810 1.00 36.06 C ANISOU 2383 CB THR A 224 6510 2243 4947 755 -198 -157 C ATOM 2384 OG1 THR A 224 -14.478 -37.552 15.371 1.00 37.33 O ANISOU 2384 OG1 THR A 224 6869 2224 5089 687 -232 -198 O ATOM 2385 CG2 THR A 224 -14.670 -35.615 16.788 1.00 34.61 C ANISOU 2385 CG2 THR A 224 6257 2190 4704 600 -246 -43 C ATOM 2386 N LEU A 225 -11.356 -34.388 15.272 1.00 42.62 N ANISOU 2386 N LEU A 225 6959 3359 5877 1042 -34 -231 N ATOM 2387 CA LEU A 225 -10.553 -33.226 15.652 1.00 39.56 C ANISOU 2387 CA LEU A 225 6368 3136 5527 1103 -3 -198 C ATOM 2388 C LEU A 225 -10.458 -32.219 14.514 1.00 39.47 C ANISOU 2388 C LEU A 225 6267 3267 5463 1093 119 -282 C ATOM 2389 O LEU A 225 -10.453 -31.006 14.750 1.00 35.14 O ANISOU 2389 O LEU A 225 5580 2884 4889 1047 138 -243 O ATOM 2390 CB LEU A 225 -9.155 -33.666 16.087 1.00 39.77 C ANISOU 2390 CB LEU A 225 6326 3094 5692 1295 -20 -194 C ATOM 2391 CG LEU A 225 -9.042 -34.286 17.478 1.00 41.04 C ANISOU 2391 CG LEU A 225 6526 3161 5908 1316 -157 -80 C ATOM 2392 CD1 LEU A 225 -7.673 -34.920 17.690 1.00 40.27 C ANISOU 2392 CD1 LEU A 225 6381 2965 5956 1525 -179 -95 C ATOM 2393 CD2 LEU A 225 -9.318 -33.235 18.538 1.00 40.02 C ANISOU 2393 CD2 LEU A 225 6285 3184 5737 1223 -214 26 C ATOM 2394 N GLN A 226 -10.367 -32.702 13.274 1.00 40.42 N ANISOU 2394 N GLN A 226 6476 3321 5561 1137 203 -396 N ATOM 2395 CA GLN A 226 -10.349 -31.793 12.137 1.00 33.51 C ANISOU 2395 CA GLN A 226 5545 2573 4615 1117 320 -472 C ATOM 2396 C GLN A 226 -11.668 -31.043 12.001 1.00 37.76 C ANISOU 2396 C GLN A 226 6105 3214 5028 933 294 -441 C ATOM 2397 O GLN A 226 -11.672 -29.867 11.619 1.00 39.03 O ANISOU 2397 O GLN A 226 6161 3528 5141 897 354 -444 O ATOM 2398 CB GLN A 226 -10.027 -32.564 10.860 1.00 57.90 C ANISOU 2398 CB GLN A 226 8752 5556 7690 1200 412 -604 C ATOM 2399 CG GLN A 226 -8.579 -33.009 10.770 1.00 62.20 C ANISOU 2399 CG GLN A 226 9229 6041 8363 1403 479 -654 C ATOM 2400 CD GLN A 226 -8.330 -33.929 9.592 1.00 71.44 C ANISOU 2400 CD GLN A 226 10543 7082 9518 1490 566 -788 C ATOM 2401 OE1 GLN A 226 -9.235 -34.200 8.802 1.00 78.19 O ANISOU 2401 OE1 GLN A 226 11555 7896 10257 1392 572 -846 O ATOM 2402 NE2 GLN A 226 -7.099 -34.417 9.467 1.00 72.83 N ANISOU 2402 NE2 GLN A 226 10666 7193 9812 1677 632 -842 N ATOM 2403 N LYS A 227 -12.790 -31.692 12.319 1.00 38.03 N ANISOU 2403 N LYS A 227 6268 3167 5016 814 205 -408 N ATOM 2404 CA LYS A 227 -14.069 -30.990 12.304 1.00 36.79 C ANISOU 2404 CA LYS A 227 6110 3112 4758 641 172 -372 C ATOM 2405 C LYS A 227 -14.161 -29.968 13.428 1.00 42.27 C ANISOU 2405 C LYS A 227 6655 3941 5463 595 133 -264 C ATOM 2406 O LYS A 227 -14.772 -28.907 13.250 1.00 42.29 O ANISOU 2406 O LYS A 227 6589 4082 5399 505 148 -249 O ATOM 2407 CB LYS A 227 -15.222 -31.988 12.398 1.00 36.55 C ANISOU 2407 CB LYS A 227 6241 2956 4689 521 88 -363 C ATOM 2408 CG LYS A 227 -15.336 -32.902 11.194 1.00 42.58 C ANISOU 2408 CG LYS A 227 7169 3592 5419 538 118 -479 C ATOM 2409 CD LYS A 227 -16.510 -33.849 11.322 1.00 50.57 C ANISOU 2409 CD LYS A 227 8333 4481 6400 401 26 -467 C ATOM 2410 CE LYS A 227 -16.604 -34.755 10.106 1.00 59.71 C ANISOU 2410 CE LYS A 227 9666 5503 7519 416 47 -592 C ATOM 2411 NZ LYS A 227 -17.741 -35.710 10.208 1.00 67.26 N ANISOU 2411 NZ LYS A 227 10773 6330 8454 272 -48 -583 N ATOM 2412 N GLU A 228 -13.568 -30.265 14.588 1.00 45.55 N ANISOU 2412 N GLU A 228 7029 4316 5962 658 77 -190 N ATOM 2413 CA GLU A 228 -13.588 -29.309 15.690 1.00 42.89 C ANISOU 2413 CA GLU A 228 6563 4103 5630 620 37 -94 C ATOM 2414 C GLU A 228 -12.707 -28.102 15.400 1.00 37.60 C ANISOU 2414 C GLU A 228 5730 3573 4982 691 111 -115 C ATOM 2415 O GLU A 228 -13.033 -26.986 15.817 1.00 32.95 O ANISOU 2415 O GLU A 228 5044 3118 4356 623 105 -68 O ATOM 2416 CB GLU A 228 -13.150 -29.991 16.986 1.00 48.22 C ANISOU 2416 CB GLU A 228 7254 4689 6377 671 -51 -9 C ATOM 2417 CG GLU A 228 -14.223 -30.851 17.631 1.00 54.99 C ANISOU 2417 CG GLU A 228 8250 5447 7197 555 -132 52 C ATOM 2418 CD GLU A 228 -13.756 -31.490 18.926 1.00 64.96 C ANISOU 2418 CD GLU A 228 9543 6622 8518 606 -221 145 C ATOM 2419 OE1 GLU A 228 -12.902 -32.400 18.870 1.00 68.55 O ANISOU 2419 OE1 GLU A 228 10051 6941 9053 734 -240 124 O ATOM 2420 OE2 GLU A 228 -14.237 -31.073 20.002 1.00 70.33 O ANISOU 2420 OE2 GLU A 228 10196 7366 9161 524 -273 239 O ATOM 2421 N VAL A 229 -11.591 -28.303 14.697 1.00 40.56 N ANISOU 2421 N VAL A 229 6074 3917 5419 825 185 -187 N ATOM 2422 CA VAL A 229 -10.754 -27.179 14.292 1.00 38.05 C ANISOU 2422 CA VAL A 229 5604 3730 5124 881 270 -212 C ATOM 2423 C VAL A 229 -11.498 -26.299 13.295 1.00 35.82 C ANISOU 2423 C VAL A 229 5329 3549 4731 783 337 -252 C ATOM 2424 O VAL A 229 -11.516 -25.069 13.421 1.00 35.31 O ANISOU 2424 O VAL A 229 5153 3619 4643 740 356 -221 O ATOM 2425 CB VAL A 229 -9.420 -27.688 13.716 1.00 36.98 C ANISOU 2425 CB VAL A 229 5432 3533 5085 1046 347 -284 C ATOM 2426 CG1 VAL A 229 -8.598 -26.535 13.166 1.00 29.11 C ANISOU 2426 CG1 VAL A 229 4281 2673 4108 1087 454 -314 C ATOM 2427 CG2 VAL A 229 -8.644 -28.423 14.784 1.00 30.39 C ANISOU 2427 CG2 VAL A 229 4568 2609 4369 1151 264 -233 C ATOM 2428 N HIS A 230 -12.128 -26.917 12.294 1.00 32.96 N ANISOU 2428 N HIS A 230 5107 3118 4299 747 364 -322 N ATOM 2429 CA HIS A 230 -12.900 -26.145 11.327 1.00 37.27 C ANISOU 2429 CA HIS A 230 5677 3752 4732 653 409 -358 C ATOM 2430 C HIS A 230 -14.029 -25.378 12.008 1.00 34.97 C ANISOU 2430 C HIS A 230 5349 3552 4386 517 333 -280 C ATOM 2431 O HIS A 230 -14.294 -24.218 11.669 1.00 39.56 O ANISOU 2431 O HIS A 230 5862 4255 4913 468 365 -273 O ATOM 2432 CB HIS A 230 -13.452 -27.066 10.239 1.00 45.16 C ANISOU 2432 CB HIS A 230 6849 4648 5662 631 425 -445 C ATOM 2433 CG HIS A 230 -14.312 -26.364 9.233 1.00 52.04 C ANISOU 2433 CG HIS A 230 7764 5600 6410 533 450 -481 C ATOM 2434 ND1 HIS A 230 -13.795 -25.731 8.124 1.00 53.98 N ANISOU 2434 ND1 HIS A 230 7997 5911 6604 575 559 -543 N ATOM 2435 CD2 HIS A 230 -15.653 -26.185 9.177 1.00 52.30 C ANISOU 2435 CD2 HIS A 230 7849 5661 6363 395 376 -458 C ATOM 2436 CE1 HIS A 230 -14.780 -25.199 7.423 1.00 53.16 C ANISOU 2436 CE1 HIS A 230 7948 5864 6385 470 541 -556 C ATOM 2437 NE2 HIS A 230 -15.918 -25.458 8.042 1.00 53.06 N ANISOU 2437 NE2 HIS A 230 7968 5833 6361 363 428 -507 N ATOM 2438 N ALA A 231 -14.702 -26.008 12.976 1.00 25.86 N ANISOU 2438 N ALA A 231 4242 2337 3246 457 237 -219 N ATOM 2439 CA ALA A 231 -15.790 -25.334 13.677 1.00 27.47 C ANISOU 2439 CA ALA A 231 4407 2626 3403 332 176 -147 C ATOM 2440 C ALA A 231 -15.270 -24.178 14.521 1.00 30.58 C ANISOU 2440 C ALA A 231 4650 3139 3829 355 179 -85 C ATOM 2441 O ALA A 231 -15.897 -23.113 14.581 1.00 31.96 O ANISOU 2441 O ALA A 231 4763 3427 3954 281 178 -60 O ATOM 2442 CB ALA A 231 -16.555 -26.333 14.544 1.00 24.69 C ANISOU 2442 CB ALA A 231 4143 2178 3060 262 88 -95 C ATOM 2443 N ALA A 232 -14.124 -24.368 15.179 1.00 33.71 N ANISOU 2443 N ALA A 232 4987 3508 4314 460 175 -63 N ATOM 2444 CA ALA A 232 -13.518 -23.287 15.948 1.00 32.98 C ANISOU 2444 CA ALA A 232 4752 3521 4257 485 171 -13 C ATOM 2445 C ALA A 232 -13.022 -22.170 15.037 1.00 39.19 C ANISOU 2445 C ALA A 232 5450 4410 5031 508 262 -58 C ATOM 2446 O ALA A 232 -13.102 -20.989 15.397 1.00 40.41 O ANISOU 2446 O ALA A 232 5510 4673 5169 468 260 -22 O ATOM 2447 CB ALA A 232 -12.374 -23.828 16.805 1.00 26.89 C ANISOU 2447 CB ALA A 232 3939 2691 3589 595 133 18 C ATOM 2448 N LYS A 233 -12.498 -22.521 13.858 1.00 35.45 N ANISOU 2448 N LYS A 233 5011 3897 4559 570 345 -136 N ATOM 2449 CA LYS A 233 -12.055 -21.494 12.921 1.00 35.48 C ANISOU 2449 CA LYS A 233 4948 3994 4539 582 443 -175 C ATOM 2450 C LYS A 233 -13.227 -20.654 12.435 1.00 30.26 C ANISOU 2450 C LYS A 233 4320 3410 3768 467 438 -170 C ATOM 2451 O LYS A 233 -13.115 -19.429 12.315 1.00 29.84 O ANISOU 2451 O LYS A 233 4182 3458 3696 443 471 -152 O ATOM 2452 CB LYS A 233 -11.324 -22.133 11.741 1.00 37.42 C ANISOU 2452 CB LYS A 233 5245 4178 4794 670 543 -264 C ATOM 2453 CG LYS A 233 -9.903 -22.570 12.060 1.00 45.01 C ANISOU 2453 CG LYS A 233 6120 5099 5884 805 577 -276 C ATOM 2454 CD LYS A 233 -9.234 -23.232 10.862 1.00 48.34 C ANISOU 2454 CD LYS A 233 6597 5458 6312 896 692 -373 C ATOM 2455 CE LYS A 233 -7.780 -23.575 11.158 1.00 50.62 C ANISOU 2455 CE LYS A 233 6770 5719 6743 1040 734 -388 C ATOM 2456 NZ LYS A 233 -7.150 -24.353 10.050 1.00 53.04 N ANISOU 2456 NZ LYS A 233 7138 5953 7063 1142 851 -489 N ATOM 2457 N SER A 234 -14.364 -21.295 12.161 1.00 26.31 N ANISOU 2457 N SER A 234 3938 2858 3199 394 391 -183 N ATOM 2458 CA SER A 234 -15.549 -20.556 11.744 1.00 25.16 C ANISOU 2458 CA SER A 234 3816 2784 2960 287 370 -175 C ATOM 2459 C SER A 234 -16.012 -19.595 12.834 1.00 27.02 C ANISOU 2459 C SER A 234 3954 3109 3205 231 315 -98 C ATOM 2460 O SER A 234 -16.395 -18.455 12.547 1.00 28.80 O ANISOU 2460 O SER A 234 4133 3426 3384 189 328 -87 O ATOM 2461 CB SER A 234 -16.662 -21.534 11.370 1.00 25.81 C ANISOU 2461 CB SER A 234 4031 2788 2987 216 315 -202 C ATOM 2462 OG SER A 234 -16.240 -22.399 10.327 1.00 28.24 O ANISOU 2462 OG SER A 234 4444 3007 3277 269 366 -283 O ATOM 2463 N ALA A 235 -15.968 -20.032 14.095 1.00 23.29 N ANISOU 2463 N ALA A 235 3456 2605 2786 234 254 -44 N ATOM 2464 CA ALA A 235 -16.388 -19.165 15.191 1.00 23.96 C ANISOU 2464 CA ALA A 235 3461 2772 2871 184 207 24 C ATOM 2465 C ALA A 235 -15.403 -18.023 15.405 1.00 22.36 C ANISOU 2465 C ALA A 235 3141 2648 2709 236 244 37 C ATOM 2466 O ALA A 235 -15.809 -16.893 15.701 1.00 19.14 O ANISOU 2466 O ALA A 235 2673 2328 2273 191 235 65 O ATOM 2467 CB ALA A 235 -16.551 -19.983 16.469 1.00 23.62 C ANISOU 2467 CB ALA A 235 3441 2670 2862 173 136 79 C ATOM 2468 N ALA A 236 -14.104 -18.294 15.260 1.00 21.44 N ANISOU 2468 N ALA A 236 2986 2499 2662 331 285 15 N ATOM 2469 CA ALA A 236 -13.106 -17.237 15.389 1.00 25.38 C ANISOU 2469 CA ALA A 236 3363 3070 3210 373 322 23 C ATOM 2470 C ALA A 236 -13.220 -16.213 14.266 1.00 29.37 C ANISOU 2470 C ALA A 236 3855 3644 3661 345 398 -8 C ATOM 2471 O ALA A 236 -12.869 -15.043 14.462 1.00 29.88 O ANISOU 2471 O ALA A 236 3831 3783 3739 334 414 14 O ATOM 2472 CB ALA A 236 -11.700 -17.839 15.422 1.00 20.20 C ANISOU 2472 CB ALA A 236 2657 2363 2654 483 352 3 C ATOM 2473 N ILE A 237 -13.698 -16.628 13.089 1.00 25.67 N ANISOU 2473 N ILE A 237 3483 3146 3127 329 442 -58 N ATOM 2474 CA ILE A 237 -13.938 -15.678 12.006 1.00 24.72 C ANISOU 2474 CA ILE A 237 3373 3085 2934 295 502 -80 C ATOM 2475 C ILE A 237 -15.063 -14.719 12.378 1.00 22.28 C ANISOU 2475 C ILE A 237 3052 2843 2571 210 441 -37 C ATOM 2476 O ILE A 237 -15.008 -13.522 12.068 1.00 19.69 O ANISOU 2476 O ILE A 237 2681 2582 2220 190 470 -24 O ATOM 2477 CB ILE A 237 -14.240 -16.428 10.696 1.00 22.23 C ANISOU 2477 CB ILE A 237 3183 2716 2547 297 548 -145 C ATOM 2478 CG1 ILE A 237 -12.977 -17.115 10.173 1.00 21.00 C ANISOU 2478 CG1 ILE A 237 3025 2507 2445 395 639 -197 C ATOM 2479 CG2 ILE A 237 -14.795 -15.479 9.646 1.00 23.02 C ANISOU 2479 CG2 ILE A 237 3322 2876 2549 245 580 -156 C ATOM 2480 CD1 ILE A 237 -13.226 -18.030 8.985 1.00 21.84 C ANISOU 2480 CD1 ILE A 237 3273 2544 2480 407 682 -271 C ATOM 2481 N ILE A 238 -16.093 -15.228 13.059 1.00 29.66 N ANISOU 2481 N ILE A 238 4024 3758 3489 160 360 -13 N ATOM 2482 CA ILE A 238 -17.202 -14.386 13.501 1.00 29.09 C ANISOU 2482 CA ILE A 238 3928 3750 3376 87 307 24 C ATOM 2483 C ILE A 238 -16.711 -13.325 14.478 1.00 28.34 C ANISOU 2483 C ILE A 238 3728 3715 3325 98 298 67 C ATOM 2484 O ILE A 238 -17.036 -12.138 14.351 1.00 29.39 O ANISOU 2484 O ILE A 238 3826 3911 3431 71 302 81 O ATOM 2485 CB ILE A 238 -18.311 -15.250 14.128 1.00 25.63 C ANISOU 2485 CB ILE A 238 3538 3278 2924 31 235 42 C ATOM 2486 CG1 ILE A 238 -18.806 -16.301 13.130 1.00 29.45 C ANISOU 2486 CG1 ILE A 238 4131 3693 3365 10 233 -6 C ATOM 2487 CG2 ILE A 238 -19.453 -14.374 14.627 1.00 21.05 C ANISOU 2487 CG2 ILE A 238 2917 2770 2311 -37 190 77 C ATOM 2488 CD1 ILE A 238 -19.592 -15.737 11.985 1.00 31.49 C ANISOU 2488 CD1 ILE A 238 4429 3990 3546 -34 234 -34 C ATOM 2489 N ALA A 239 -15.931 -13.740 15.479 1.00 29.99 N ANISOU 2489 N ALA A 239 3893 3899 3602 140 278 89 N ATOM 2490 CA ALA A 239 -15.440 -12.788 16.468 1.00 28.89 C ANISOU 2490 CA ALA A 239 3662 3811 3502 147 257 126 C ATOM 2491 C ALA A 239 -14.385 -11.859 15.878 1.00 23.59 C ANISOU 2491 C ALA A 239 2923 3174 2865 180 321 111 C ATOM 2492 O ALA A 239 -14.246 -10.716 16.331 1.00 22.70 O ANISOU 2492 O ALA A 239 2748 3114 2762 162 310 133 O ATOM 2493 CB ALA A 239 -14.886 -13.532 17.682 1.00 36.23 C ANISOU 2493 CB ALA A 239 4575 4702 4489 182 204 155 C ATOM 2494 N GLY A 240 -13.649 -12.320 14.865 1.00 17.93 N ANISOU 2494 N GLY A 240 2222 2426 2165 225 392 71 N ATOM 2495 CA GLY A 240 -12.672 -11.455 14.219 1.00 18.20 C ANISOU 2495 CA GLY A 240 2192 2496 2229 247 470 59 C ATOM 2496 C GLY A 240 -13.315 -10.359 13.389 1.00 23.37 C ANISOU 2496 C GLY A 240 2877 3197 2806 192 501 60 C ATOM 2497 O GLY A 240 -12.873 -9.208 13.418 1.00 21.57 O ANISOU 2497 O GLY A 240 2586 3012 2597 177 524 78 O ATOM 2498 N LEU A 241 -14.360 -10.703 12.629 1.00 21.08 N ANISOU 2498 N LEU A 241 2686 2893 2430 160 494 42 N ATOM 2499 CA LEU A 241 -15.070 -9.698 11.844 1.00 21.26 C ANISOU 2499 CA LEU A 241 2748 2956 2375 113 504 48 C ATOM 2500 C LEU A 241 -15.761 -8.680 12.739 1.00 22.12 C ANISOU 2500 C LEU A 241 2811 3110 2485 74 436 89 C ATOM 2501 O LEU A 241 -15.823 -7.497 12.393 1.00 17.40 O ANISOU 2501 O LEU A 241 2201 2545 1864 52 451 105 O ATOM 2502 CB LEU A 241 -16.084 -10.370 10.921 1.00 27.91 C ANISOU 2502 CB LEU A 241 3704 3772 3129 88 489 19 C ATOM 2503 CG LEU A 241 -15.494 -11.222 9.795 1.00 32.84 C ANISOU 2503 CG LEU A 241 4402 4351 3725 124 566 -34 C ATOM 2504 CD1 LEU A 241 -16.561 -12.102 9.155 1.00 30.99 C ANISOU 2504 CD1 LEU A 241 4284 4078 3413 94 522 -66 C ATOM 2505 CD2 LEU A 241 -14.818 -10.342 8.751 1.00 25.32 C ANISOU 2505 CD2 LEU A 241 3458 3428 2736 130 661 -40 C ATOM 2506 N PHE A 242 -16.279 -9.120 13.889 1.00 22.00 N ANISOU 2506 N PHE A 242 2776 3090 2493 65 365 107 N ATOM 2507 CA PHE A 242 -16.858 -8.188 14.848 1.00 23.41 C ANISOU 2507 CA PHE A 242 2909 3311 2674 36 312 139 C ATOM 2508 C PHE A 242 -15.846 -7.124 15.256 1.00 25.02 C ANISOU 2508 C PHE A 242 3037 3539 2930 50 332 154 C ATOM 2509 O PHE A 242 -16.150 -5.925 15.255 1.00 22.45 O ANISOU 2509 O PHE A 242 2697 3245 2588 26 325 168 O ATOM 2510 CB PHE A 242 -17.365 -8.946 16.074 1.00 19.11 C ANISOU 2510 CB PHE A 242 2361 2757 2145 26 250 156 C ATOM 2511 CG PHE A 242 -17.947 -8.059 17.126 1.00 19.07 C ANISOU 2511 CG PHE A 242 2315 2795 2135 2 206 182 C ATOM 2512 CD1 PHE A 242 -19.299 -7.767 17.130 1.00 19.24 C ANISOU 2512 CD1 PHE A 242 2355 2846 2109 -37 178 186 C ATOM 2513 CD2 PHE A 242 -17.141 -7.508 18.110 1.00 16.48 C ANISOU 2513 CD2 PHE A 242 1930 2481 1853 19 191 198 C ATOM 2514 CE1 PHE A 242 -19.839 -6.943 18.100 1.00 21.11 C ANISOU 2514 CE1 PHE A 242 2556 3123 2343 -52 149 203 C ATOM 2515 CE2 PHE A 242 -17.672 -6.679 19.080 1.00 18.64 C ANISOU 2515 CE2 PHE A 242 2180 2791 2113 -1 154 214 C ATOM 2516 CZ PHE A 242 -19.020 -6.395 19.076 1.00 17.33 C ANISOU 2516 CZ PHE A 242 2035 2652 1897 -33 140 215 C ATOM 2517 N ALA A 243 -14.632 -7.550 15.617 1.00 14.69 N ANISOU 2517 N ALA A 243 1677 2212 1693 88 352 151 N ATOM 2518 CA ALA A 243 -13.589 -6.590 15.959 1.00 14.82 C ANISOU 2518 CA ALA A 243 1610 2249 1770 94 367 163 C ATOM 2519 C ALA A 243 -13.259 -5.696 14.773 1.00 26.33 C ANISOU 2519 C ALA A 243 3073 3720 3210 77 443 157 C ATOM 2520 O ALA A 243 -13.151 -4.473 14.918 1.00 24.35 O ANISOU 2520 O ALA A 243 2793 3491 2967 49 440 175 O ATOM 2521 CB ALA A 243 -12.336 -7.324 16.443 1.00 15.42 C ANISOU 2521 CB ALA A 243 1620 2303 1935 143 370 158 C ATOM 2522 N LEU A 244 -13.107 -6.289 13.587 1.00 27.39 N ANISOU 2522 N LEU A 244 3258 3836 3313 93 514 133 N ATOM 2523 CA LEU A 244 -12.793 -5.509 12.397 1.00 26.99 C ANISOU 2523 CA LEU A 244 3231 3796 3228 74 596 132 C ATOM 2524 C LEU A 244 -13.846 -4.436 12.140 1.00 24.57 C ANISOU 2524 C LEU A 244 2979 3509 2850 29 560 155 C ATOM 2525 O LEU A 244 -13.513 -3.314 11.741 1.00 22.99 O ANISOU 2525 O LEU A 244 2771 3319 2647 3 596 175 O ATOM 2526 CB LEU A 244 -12.663 -6.441 11.191 1.00 35.68 C ANISOU 2526 CB LEU A 244 4404 4872 4282 99 672 95 C ATOM 2527 CG LEU A 244 -11.985 -5.905 9.929 1.00 44.19 C ANISOU 2527 CG LEU A 244 5504 5957 5328 91 787 89 C ATOM 2528 CD1 LEU A 244 -10.517 -5.622 10.194 1.00 47.96 C ANISOU 2528 CD1 LEU A 244 5862 6447 5914 109 857 92 C ATOM 2529 CD2 LEU A 244 -12.142 -6.889 8.780 1.00 45.55 C ANISOU 2529 CD2 LEU A 244 5780 6102 5424 115 847 46 C ATOM 2530 N CYS A 245 -15.120 -4.752 12.391 1.00 14.95 N ANISOU 2530 N CYS A 245 1810 2290 1578 19 487 155 N ATOM 2531 CA CYS A 245 -16.199 -3.817 12.087 1.00 18.32 C ANISOU 2531 CA CYS A 245 2284 2735 1944 -12 446 173 C ATOM 2532 C CYS A 245 -16.368 -2.737 13.148 1.00 17.89 C ANISOU 2532 C CYS A 245 2173 2698 1928 -25 395 197 C ATOM 2533 O CYS A 245 -16.862 -1.646 12.837 1.00 16.98 O ANISOU 2533 O CYS A 245 2082 2588 1781 -42 380 215 O ATOM 2534 CB CYS A 245 -17.518 -4.569 11.916 1.00 15.14 C ANISOU 2534 CB CYS A 245 1941 2330 1481 -20 388 160 C ATOM 2535 SG CYS A 245 -17.635 -5.468 10.368 1.00 27.29 S ANISOU 2535 SG CYS A 245 3587 3843 2940 -19 432 128 S ATOM 2536 N TRP A 246 -15.987 -3.015 14.394 1.00 18.44 N ANISOU 2536 N TRP A 246 2176 2772 2059 -14 363 197 N ATOM 2537 CA TRP A 246 -16.219 -2.074 15.481 1.00 16.07 C ANISOU 2537 CA TRP A 246 1836 2486 1783 -24 310 210 C ATOM 2538 C TRP A 246 -14.980 -1.307 15.898 1.00 14.40 C ANISOU 2538 C TRP A 246 1561 2270 1640 -31 328 218 C ATOM 2539 O TRP A 246 -15.116 -0.209 16.449 1.00 16.01 O ANISOU 2539 O TRP A 246 1753 2478 1854 -47 295 227 O ATOM 2540 CB TRP A 246 -16.777 -2.798 16.709 1.00 14.84 C ANISOU 2540 CB TRP A 246 1665 2342 1633 -16 251 207 C ATOM 2541 CG TRP A 246 -18.219 -3.130 16.591 1.00 18.49 C ANISOU 2541 CG TRP A 246 2170 2816 2038 -27 219 204 C ATOM 2542 CD1 TRP A 246 -18.755 -4.335 16.256 1.00 18.44 C ANISOU 2542 CD1 TRP A 246 2199 2801 2005 -29 216 195 C ATOM 2543 CD2 TRP A 246 -19.322 -2.243 16.810 1.00 17.94 C ANISOU 2543 CD2 TRP A 246 2107 2770 1940 -36 185 209 C ATOM 2544 NE1 TRP A 246 -20.129 -4.256 16.260 1.00 17.82 N ANISOU 2544 NE1 TRP A 246 2139 2744 1887 -48 179 195 N ATOM 2545 CE2 TRP A 246 -20.499 -2.980 16.591 1.00 12.66 C ANISOU 2545 CE2 TRP A 246 1464 2114 1234 -47 162 203 C ATOM 2546 CE3 TRP A 246 -19.426 -0.897 17.171 1.00 14.63 C ANISOU 2546 CE3 TRP A 246 1672 2357 1529 -35 169 214 C ATOM 2547 CZ2 TRP A 246 -21.763 -2.418 16.719 1.00 15.48 C ANISOU 2547 CZ2 TRP A 246 1815 2498 1568 -52 127 204 C ATOM 2548 CZ3 TRP A 246 -20.682 -0.341 17.296 1.00 13.13 C ANISOU 2548 CZ3 TRP A 246 1490 2187 1311 -32 136 212 C ATOM 2549 CH2 TRP A 246 -21.835 -1.101 17.075 1.00 13.66 C ANISOU 2549 CH2 TRP A 246 1567 2275 1348 -38 117 207 C ATOM 2550 N LEU A 247 -13.791 -1.857 15.658 1.00 17.90 N ANISOU 2550 N LEU A 247 1960 2705 2136 -17 376 212 N ATOM 2551 CA LEU A 247 -12.568 -1.177 16.075 1.00 15.74 C ANISOU 2551 CA LEU A 247 1606 2430 1943 -29 388 218 C ATOM 2552 C LEU A 247 -12.391 0.208 15.464 1.00 19.03 C ANISOU 2552 C LEU A 247 2034 2841 2356 -70 423 235 C ATOM 2553 O LEU A 247 -11.946 1.111 16.193 1.00 23.22 O ANISOU 2553 O LEU A 247 2519 3367 2936 -95 388 242 O ATOM 2554 CB LEU A 247 -11.352 -2.055 15.768 1.00 16.08 C ANISOU 2554 CB LEU A 247 1588 2468 2052 -1 444 206 C ATOM 2555 CG LEU A 247 -11.035 -3.087 16.845 1.00 21.97 C ANISOU 2555 CG LEU A 247 2290 3211 2847 38 384 198 C ATOM 2556 CD1 LEU A 247 -9.972 -4.054 16.348 1.00 21.06 C ANISOU 2556 CD1 LEU A 247 2124 3083 2794 82 445 182 C ATOM 2557 CD2 LEU A 247 -10.589 -2.392 18.125 1.00 22.24 C ANISOU 2557 CD2 LEU A 247 2260 3254 2934 22 306 209 C ATOM 2558 N PRO A 248 -12.685 0.452 14.179 1.00 19.50 N ANISOU 2558 N PRO A 248 2160 2893 2357 -83 485 244 N ATOM 2559 CA PRO A 248 -12.528 1.823 13.666 1.00 22.19 C ANISOU 2559 CA PRO A 248 2523 3218 2692 -126 512 270 C ATOM 2560 C PRO A 248 -13.303 2.850 14.472 1.00 19.75 C ANISOU 2560 C PRO A 248 2233 2898 2374 -138 429 278 C ATOM 2561 O PRO A 248 -12.767 3.918 14.789 1.00 18.22 O ANISOU 2561 O PRO A 248 2014 2684 2226 -172 422 290 O ATOM 2562 CB PRO A 248 -13.038 1.709 12.223 1.00 17.70 C ANISOU 2562 CB PRO A 248 2052 2643 2032 -128 569 280 C ATOM 2563 CG PRO A 248 -12.740 0.307 11.850 1.00 15.90 C ANISOU 2563 CG PRO A 248 1816 2426 1798 -94 615 252 C ATOM 2564 CD PRO A 248 -13.051 -0.481 13.096 1.00 18.97 C ANISOU 2564 CD PRO A 248 2157 2825 2224 -63 535 233 C ATOM 2565 N LEU A 249 -14.545 2.538 14.843 1.00 22.10 N ANISOU 2565 N LEU A 249 2571 3206 2619 -110 367 268 N ATOM 2566 CA LEU A 249 -15.319 3.443 15.684 1.00 23.65 C ANISOU 2566 CA LEU A 249 2781 3396 2811 -109 297 267 C ATOM 2567 C LEU A 249 -14.640 3.664 17.034 1.00 20.19 C ANISOU 2567 C LEU A 249 2275 2958 2437 -117 255 252 C ATOM 2568 O LEU A 249 -14.576 4.796 17.527 1.00 18.38 O ANISOU 2568 O LEU A 249 2049 2706 2229 -136 224 252 O ATOM 2569 CB LEU A 249 -16.731 2.888 15.863 1.00 30.35 C ANISOU 2569 CB LEU A 249 3664 4267 3601 -78 252 255 C ATOM 2570 CG LEU A 249 -17.882 3.867 16.089 1.00 36.76 C ANISOU 2570 CG LEU A 249 4511 5072 4384 -65 201 256 C ATOM 2571 CD1 LEU A 249 -17.784 5.061 15.153 1.00 35.77 C ANISOU 2571 CD1 LEU A 249 4438 4907 4247 -81 218 283 C ATOM 2572 CD2 LEU A 249 -19.205 3.143 15.891 1.00 31.67 C ANISOU 2572 CD2 LEU A 249 3888 4457 3689 -41 174 248 C ATOM 2573 N HIS A 250 -14.106 2.598 17.638 1.00 16.61 N ANISOU 2573 N HIS A 250 1770 2526 2016 -102 248 239 N ATOM 2574 CA HIS A 250 -13.420 2.742 18.920 1.00 17.81 C ANISOU 2574 CA HIS A 250 1864 2679 2222 -108 194 227 C ATOM 2575 C HIS A 250 -12.103 3.494 18.775 1.00 24.83 C ANISOU 2575 C HIS A 250 2695 3549 3190 -147 215 234 C ATOM 2576 O HIS A 250 -11.721 4.261 19.668 1.00 26.23 O ANISOU 2576 O HIS A 250 2848 3713 3404 -171 161 225 O ATOM 2577 CB HIS A 250 -13.172 1.371 19.543 1.00 14.07 C ANISOU 2577 CB HIS A 250 1358 2227 1763 -77 172 220 C ATOM 2578 CG HIS A 250 -14.406 0.722 20.076 1.00 20.02 C ANISOU 2578 CG HIS A 250 2159 2997 2449 -54 138 214 C ATOM 2579 ND1 HIS A 250 -15.105 1.228 21.151 1.00 19.48 N ANISOU 2579 ND1 HIS A 250 2113 2938 2349 -55 84 204 N ATOM 2580 CD2 HIS A 250 -15.065 -0.395 19.689 1.00 18.68 C ANISOU 2580 CD2 HIS A 250 2020 2837 2241 -35 155 215 C ATOM 2581 CE1 HIS A 250 -16.146 0.453 21.399 1.00 22.13 C ANISOU 2581 CE1 HIS A 250 2482 3294 2633 -39 76 203 C ATOM 2582 NE2 HIS A 250 -16.143 -0.540 20.528 1.00 18.92 N ANISOU 2582 NE2 HIS A 250 2080 2884 2223 -30 113 211 N ATOM 2583 N ILE A 251 -11.388 3.274 17.669 1.00 23.50 N ANISOU 2583 N ILE A 251 2502 3378 3047 -159 297 248 N ATOM 2584 CA ILE A 251 -10.114 3.957 17.464 1.00 26.10 C ANISOU 2584 CA ILE A 251 2762 3694 3460 -205 332 258 C ATOM 2585 C ILE A 251 -10.334 5.456 17.288 1.00 24.59 C ANISOU 2585 C ILE A 251 2619 3464 3259 -255 326 273 C ATOM 2586 O ILE A 251 -9.592 6.275 17.845 1.00 26.40 O ANISOU 2586 O ILE A 251 2802 3673 3556 -301 295 271 O ATOM 2587 CB ILE A 251 -9.365 3.340 16.266 1.00 26.66 C ANISOU 2587 CB ILE A 251 2801 3775 3552 -204 441 267 C ATOM 2588 CG1 ILE A 251 -8.965 1.897 16.574 1.00 24.07 C ANISOU 2588 CG1 ILE A 251 2417 3473 3257 -149 439 248 C ATOM 2589 CG2 ILE A 251 -8.133 4.161 15.909 1.00 17.63 C ANISOU 2589 CG2 ILE A 251 1584 2620 2494 -264 498 283 C ATOM 2590 CD1 ILE A 251 -8.330 1.182 15.413 1.00 26.94 C ANISOU 2590 CD1 ILE A 251 2759 3845 3634 -132 552 245 C ATOM 2591 N ILE A 252 -11.357 5.837 16.520 1.00 15.99 N ANISOU 2591 N ILE A 252 1627 2360 2089 -248 346 288 N ATOM 2592 CA ILE A 252 -11.663 7.252 16.334 1.00 19.52 C ANISOU 2592 CA ILE A 252 2134 2758 2524 -284 333 305 C ATOM 2593 C ILE A 252 -11.984 7.911 17.670 1.00 19.72 C ANISOU 2593 C ILE A 252 2160 2765 2566 -281 237 278 C ATOM 2594 O ILE A 252 -11.541 9.031 17.947 1.00 20.79 O ANISOU 2594 O ILE A 252 2300 2856 2745 -328 215 281 O ATOM 2595 CB ILE A 252 -12.816 7.424 15.327 1.00 19.19 C ANISOU 2595 CB ILE A 252 2197 2704 2389 -260 352 326 C ATOM 2596 CG1 ILE A 252 -12.409 6.889 13.955 1.00 16.41 C ANISOU 2596 CG1 ILE A 252 1863 2364 2007 -272 450 351 C ATOM 2597 CG2 ILE A 252 -13.225 8.885 15.231 1.00 16.34 C ANISOU 2597 CG2 ILE A 252 1907 2283 2018 -284 323 345 C ATOM 2598 CD1 ILE A 252 -13.533 6.867 12.950 1.00 20.87 C ANISOU 2598 CD1 ILE A 252 2535 2923 2471 -246 455 369 C ATOM 2599 N ASN A 253 -12.758 7.230 18.519 1.00 21.00 N ANISOU 2599 N ASN A 253 2328 2960 2692 -231 183 251 N ATOM 2600 CA ASN A 253 -13.037 7.773 19.844 1.00 15.35 C ANISOU 2600 CA ASN A 253 1620 2233 1980 -225 102 220 C ATOM 2601 C ASN A 253 -11.761 7.961 20.648 1.00 18.66 C ANISOU 2601 C ASN A 253 1967 2645 2479 -268 64 207 C ATOM 2602 O ASN A 253 -11.660 8.908 21.435 1.00 21.24 O ANISOU 2602 O ASN A 253 2312 2936 2822 -292 6 185 O ATOM 2603 CB ASN A 253 -14.002 6.867 20.602 1.00 14.70 C ANISOU 2603 CB ASN A 253 1551 2194 1841 -171 67 198 C ATOM 2604 CG ASN A 253 -15.401 6.904 20.037 1.00 18.44 C ANISOU 2604 CG ASN A 253 2088 2674 2246 -132 81 203 C ATOM 2605 OD1 ASN A 253 -15.787 7.865 19.368 1.00 14.50 O ANISOU 2605 OD1 ASN A 253 1637 2136 1735 -137 92 216 O ATOM 2606 ND2 ASN A 253 -16.180 5.862 20.313 1.00 13.80 N ANISOU 2606 ND2 ASN A 253 1498 2129 1615 -97 76 195 N ATOM 2607 N CYS A 254 -10.779 7.075 20.466 1.00 16.15 N ANISOU 2607 N CYS A 254 1565 2357 2213 -275 92 216 N ATOM 2608 CA CYS A 254 -9.506 7.247 21.153 1.00 16.87 C ANISOU 2608 CA CYS A 254 1569 2444 2395 -315 49 206 C ATOM 2609 C CYS A 254 -8.800 8.515 20.692 1.00 17.67 C ANISOU 2609 C CYS A 254 1659 2497 2559 -391 71 219 C ATOM 2610 O CYS A 254 -8.234 9.247 21.512 1.00 22.38 O ANISOU 2610 O CYS A 254 2232 3067 3207 -435 1 200 O ATOM 2611 CB CYS A 254 -8.614 6.026 20.936 1.00 18.72 C ANISOU 2611 CB CYS A 254 1708 2720 2686 -296 80 214 C ATOM 2612 SG CYS A 254 -9.124 4.552 21.837 1.00 18.29 S ANISOU 2612 SG CYS A 254 1661 2707 2583 -222 23 200 S ATOM 2613 N PHE A 255 -8.829 8.798 19.386 1.00 17.83 N ANISOU 2613 N PHE A 255 1704 2501 2569 -412 165 253 N ATOM 2614 CA PHE A 255 -8.205 10.022 18.889 1.00 25.46 C ANISOU 2614 CA PHE A 255 2673 3414 3588 -492 196 275 C ATOM 2615 C PHE A 255 -8.945 11.259 19.381 1.00 22.28 C ANISOU 2615 C PHE A 255 2369 2946 3150 -505 130 262 C ATOM 2616 O PHE A 255 -8.318 12.261 19.741 1.00 23.10 O ANISOU 2616 O PHE A 255 2463 2998 3316 -573 94 257 O ATOM 2617 CB PHE A 255 -8.145 10.008 17.361 1.00 24.88 C ANISOU 2617 CB PHE A 255 2626 3337 3492 -509 317 320 C ATOM 2618 CG PHE A 255 -6.985 9.234 16.809 1.00 25.83 C ANISOU 2618 CG PHE A 255 2633 3500 3681 -527 401 331 C ATOM 2619 CD1 PHE A 255 -5.745 9.835 16.658 1.00 21.38 C ANISOU 2619 CD1 PHE A 255 1981 2921 3222 -611 440 346 C ATOM 2620 CD2 PHE A 255 -7.133 7.904 16.443 1.00 25.34 C ANISOU 2620 CD2 PHE A 255 2550 3492 3587 -461 445 324 C ATOM 2621 CE1 PHE A 255 -4.674 9.126 16.152 1.00 22.34 C ANISOU 2621 CE1 PHE A 255 1983 3087 3418 -621 528 352 C ATOM 2622 CE2 PHE A 255 -6.067 7.187 15.935 1.00 22.96 C ANISOU 2622 CE2 PHE A 255 2144 3226 3354 -465 529 327 C ATOM 2623 CZ PHE A 255 -4.833 7.799 15.787 1.00 21.82 C ANISOU 2623 CZ PHE A 255 1900 3074 3317 -542 575 341 C ATOM 2624 N THR A 256 -10.279 11.206 19.398 1.00 17.91 N ANISOU 2624 N THR A 256 1909 2393 2505 -439 112 254 N ATOM 2625 CA THR A 256 -11.069 12.309 19.936 1.00 23.10 C ANISOU 2625 CA THR A 256 2657 2990 3131 -431 50 232 C ATOM 2626 C THR A 256 -10.721 12.578 21.393 1.00 23.42 C ANISOU 2626 C THR A 256 2675 3022 3203 -443 -44 182 C ATOM 2627 O THR A 256 -10.581 13.736 21.804 1.00 23.94 O ANISOU 2627 O THR A 256 2785 3018 3293 -484 -90 164 O ATOM 2628 CB THR A 256 -12.561 11.995 19.808 1.00 22.32 C ANISOU 2628 CB THR A 256 2631 2910 2938 -347 47 226 C ATOM 2629 OG1 THR A 256 -12.917 11.869 18.425 1.00 22.35 O ANISOU 2629 OG1 THR A 256 2672 2914 2905 -339 118 272 O ATOM 2630 CG2 THR A 256 -13.388 13.092 20.450 1.00 17.31 C ANISOU 2630 CG2 THR A 256 2080 2218 2279 -323 -13 195 C ATOM 2631 N PHE A 257 -10.573 11.517 22.185 1.00 21.17 N ANISOU 2631 N PHE A 257 2331 2801 2910 -411 -78 159 N ATOM 2632 CA PHE A 257 -10.384 11.659 23.624 1.00 25.32 C ANISOU 2632 CA PHE A 257 2856 3325 3439 -413 -175 110 C ATOM 2633 C PHE A 257 -8.931 11.957 23.971 1.00 30.01 C ANISOU 2633 C PHE A 257 3364 3903 4134 -491 -219 107 C ATOM 2634 O PHE A 257 -8.644 12.889 24.728 1.00 30.57 O ANISOU 2634 O PHE A 257 3464 3923 4228 -535 -293 73 O ATOM 2635 CB PHE A 257 -10.856 10.385 24.330 1.00 23.66 C ANISOU 2635 CB PHE A 257 2632 3186 3172 -347 -197 96 C ATOM 2636 CG PHE A 257 -10.664 10.398 25.824 1.00 24.86 C ANISOU 2636 CG PHE A 257 2795 3344 3306 -347 -297 51 C ATOM 2637 CD1 PHE A 257 -11.420 11.235 26.629 1.00 24.04 C ANISOU 2637 CD1 PHE A 257 2785 3205 3143 -332 -340 7 C ATOM 2638 CD2 PHE A 257 -9.751 9.544 26.424 1.00 24.67 C ANISOU 2638 CD2 PHE A 257 2694 3360 3321 -355 -348 53 C ATOM 2639 CE1 PHE A 257 -11.255 11.237 28.001 1.00 18.30 C ANISOU 2639 CE1 PHE A 257 2086 2485 2382 -332 -429 -38 C ATOM 2640 CE2 PHE A 257 -9.580 9.540 27.799 1.00 18.43 C ANISOU 2640 CE2 PHE A 257 1928 2574 2500 -355 -449 15 C ATOM 2641 CZ PHE A 257 -10.337 10.387 28.586 1.00 20.47 C ANISOU 2641 CZ PHE A 257 2292 2800 2686 -347 -487 -31 C ATOM 2642 N PHE A 258 -8.002 11.179 23.420 1.00 31.21 N ANISOU 2642 N PHE A 258 3408 4097 4353 -510 -175 137 N ATOM 2643 CA PHE A 258 -6.615 11.260 23.846 1.00 22.67 C ANISOU 2643 CA PHE A 258 2216 3017 3380 -575 -225 131 C ATOM 2644 C PHE A 258 -5.851 12.396 23.186 1.00 27.24 C ANISOU 2644 C PHE A 258 2770 3537 4044 -673 -190 151 C ATOM 2645 O PHE A 258 -4.834 12.832 23.731 1.00 27.52 O ANISOU 2645 O PHE A 258 2732 3555 4171 -744 -256 136 O ATOM 2646 CB PHE A 258 -5.911 9.932 23.573 1.00 20.17 C ANISOU 2646 CB PHE A 258 1782 2769 3113 -545 -191 151 C ATOM 2647 CG PHE A 258 -6.244 8.859 24.570 1.00 19.96 C ANISOU 2647 CG PHE A 258 1760 2790 3033 -472 -263 131 C ATOM 2648 CD1 PHE A 258 -6.103 9.093 25.932 1.00 22.66 C ANISOU 2648 CD1 PHE A 258 2122 3124 3363 -481 -390 94 C ATOM 2649 CD2 PHE A 258 -6.703 7.620 24.149 1.00 19.02 C ANISOU 2649 CD2 PHE A 258 1639 2717 2871 -401 -207 149 C ATOM 2650 CE1 PHE A 258 -6.406 8.108 26.855 1.00 19.70 C ANISOU 2650 CE1 PHE A 258 1767 2790 2930 -419 -454 83 C ATOM 2651 CE2 PHE A 258 -7.010 6.632 25.066 1.00 18.54 C ANISOU 2651 CE2 PHE A 258 1594 2691 2761 -343 -272 137 C ATOM 2652 CZ PHE A 258 -6.865 6.878 26.422 1.00 18.95 C ANISOU 2652 CZ PHE A 258 1667 2736 2796 -352 -394 108 C ATOM 2653 N CYS A 259 -6.305 12.889 22.032 1.00 32.02 N ANISOU 2653 N CYS A 259 3435 4107 4622 -684 -94 188 N ATOM 2654 CA CYS A 259 -5.628 13.970 21.319 1.00 35.87 C ANISOU 2654 CA CYS A 259 3916 4532 5182 -784 -47 218 C ATOM 2655 C CYS A 259 -6.605 15.121 21.103 1.00 37.06 C ANISOU 2655 C CYS A 259 4218 4597 5265 -785 -53 221 C ATOM 2656 O CYS A 259 -7.221 15.235 20.033 1.00 40.93 O ANISOU 2656 O CYS A 259 4778 5073 5702 -764 30 262 O ATOM 2657 CB CYS A 259 -5.053 13.498 19.984 1.00 38.65 C ANISOU 2657 CB CYS A 259 4197 4918 5570 -807 88 272 C ATOM 2658 SG CYS A 259 -4.084 14.784 19.173 1.00 51.15 S ANISOU 2658 SG CYS A 259 5760 6428 7247 -947 156 316 S ATOM 2659 N PRO A 260 -6.771 15.997 22.096 1.00 36.16 N ANISOU 2659 N PRO A 260 4166 4422 5152 -804 -154 176 N ATOM 2660 CA PRO A 260 -7.610 17.186 21.889 1.00 39.11 C ANISOU 2660 CA PRO A 260 4682 4698 5479 -803 -161 176 C ATOM 2661 C PRO A 260 -6.982 18.219 20.963 1.00 45.69 C ANISOU 2661 C PRO A 260 5534 5449 6378 -907 -107 226 C ATOM 2662 O PRO A 260 -7.681 19.151 20.541 1.00 44.58 O ANISOU 2662 O PRO A 260 5519 5221 6198 -901 -99 243 O ATOM 2663 CB PRO A 260 -7.785 17.741 23.308 1.00 38.84 C ANISOU 2663 CB PRO A 260 4699 4624 5434 -797 -284 102 C ATOM 2664 CG PRO A 260 -6.566 17.289 24.031 1.00 38.55 C ANISOU 2664 CG PRO A 260 4537 4631 5479 -856 -345 81 C ATOM 2665 CD PRO A 260 -6.236 15.929 23.466 1.00 37.78 C ANISOU 2665 CD PRO A 260 4323 4638 5392 -821 -272 119 C ATOM 2666 N ASP A 261 -5.691 18.092 20.648 1.00 48.42 N ANISOU 2666 N ASP A 261 5758 5815 6825 -1002 -68 253 N ATOM 2667 CA ASP A 261 -5.038 18.968 19.684 1.00 49.78 C ANISOU 2667 CA ASP A 261 5936 5917 7059 -1112 6 311 C ATOM 2668 C ASP A 261 -5.182 18.483 18.247 1.00 46.46 C ANISOU 2668 C ASP A 261 5523 5535 6596 -1096 148 381 C ATOM 2669 O ASP A 261 -5.010 19.283 17.320 1.00 45.95 O ANISOU 2669 O ASP A 261 5519 5402 6539 -1169 218 439 O ATOM 2670 CB ASP A 261 -3.551 19.116 20.023 1.00 59.54 C ANISOU 2670 CB ASP A 261 7025 7160 8435 -1233 -12 307 C ATOM 2671 CG ASP A 261 -3.318 19.866 21.325 1.00 67.99 C ANISOU 2671 CG ASP A 261 8114 8168 9551 -1278 -159 242 C ATOM 2672 OD1 ASP A 261 -4.207 20.646 21.730 1.00 70.96 O ANISOU 2672 OD1 ASP A 261 8641 8461 9860 -1244 -221 212 O ATOM 2673 OD2 ASP A 261 -2.244 19.679 21.939 1.00 69.78 O ANISOU 2673 OD2 ASP A 261 8206 8427 9881 -1344 -216 218 O ATOM 2674 N CYS A 262 -5.475 17.201 18.039 1.00 43.74 N ANISOU 2674 N CYS A 262 5127 5292 6201 -1007 189 377 N ATOM 2675 CA CYS A 262 -5.791 16.714 16.704 1.00 41.90 C ANISOU 2675 CA CYS A 262 4928 5092 5902 -978 312 432 C ATOM 2676 C CYS A 262 -7.174 17.202 16.293 1.00 38.32 C ANISOU 2676 C CYS A 262 4643 4583 5334 -911 296 448 C ATOM 2677 O CYS A 262 -8.080 17.313 17.122 1.00 37.27 O ANISOU 2677 O CYS A 262 4568 4436 5158 -839 202 403 O ATOM 2678 CB CYS A 262 -5.751 15.185 16.661 1.00 48.83 C ANISOU 2678 CB CYS A 262 5712 6083 6760 -899 349 415 C ATOM 2679 SG CYS A 262 -4.206 14.393 17.184 1.00 55.95 S ANISOU 2679 SG CYS A 262 6400 7060 7800 -943 356 392 S ATOM 2680 N SER A 263 -7.336 17.510 15.009 1.00 39.35 N ANISOU 2680 N SER A 263 4853 4683 5415 -934 387 514 N ATOM 2681 CA SER A 263 -8.666 17.826 14.508 1.00 38.10 C ANISOU 2681 CA SER A 263 4846 4484 5148 -858 367 534 C ATOM 2682 C SER A 263 -9.542 16.585 14.590 1.00 34.55 C ANISOU 2682 C SER A 263 4379 4127 4622 -742 355 503 C ATOM 2683 O SER A 263 -9.075 15.463 14.379 1.00 34.70 O ANISOU 2683 O SER A 263 4305 4233 4646 -731 413 497 O ATOM 2684 CB SER A 263 -8.603 18.334 13.067 1.00 43.70 C ANISOU 2684 CB SER A 263 5651 5144 5809 -909 463 618 C ATOM 2685 OG SER A 263 -7.881 19.549 12.981 1.00 51.29 O ANISOU 2685 OG SER A 263 6644 6006 6839 -1024 474 653 O ATOM 2686 N HIS A 264 -10.813 16.787 14.924 1.00 32.09 N ANISOU 2686 N HIS A 264 4153 3794 4246 -655 279 480 N ATOM 2687 CA HIS A 264 -11.739 15.667 15.007 1.00 28.12 C ANISOU 2687 CA HIS A 264 3637 3373 3673 -554 264 453 C ATOM 2688 C HIS A 264 -11.821 14.962 13.659 1.00 28.70 C ANISOU 2688 C HIS A 264 3734 3489 3680 -546 354 501 C ATOM 2689 O HIS A 264 -11.701 15.587 12.601 1.00 33.75 O ANISOU 2689 O HIS A 264 4456 4078 4290 -589 407 560 O ATOM 2690 CB HIS A 264 -13.122 16.155 15.443 1.00 25.61 C ANISOU 2690 CB HIS A 264 3406 3020 3305 -469 180 428 C ATOM 2691 CG HIS A 264 -14.051 15.061 15.868 1.00 25.39 C ANISOU 2691 CG HIS A 264 3344 3078 3227 -377 152 388 C ATOM 2692 ND1 HIS A 264 -14.563 14.132 14.987 1.00 25.90 N ANISOU 2692 ND1 HIS A 264 3414 3200 3225 -338 193 411 N ATOM 2693 CD2 HIS A 264 -14.573 14.756 17.080 1.00 23.77 C ANISOU 2693 CD2 HIS A 264 3104 2905 3023 -323 90 328 C ATOM 2694 CE1 HIS A 264 -15.353 13.297 15.639 1.00 22.97 C ANISOU 2694 CE1 HIS A 264 3007 2893 2828 -269 156 368 C ATOM 2695 NE2 HIS A 264 -15.379 13.655 16.910 1.00 23.92 N ANISOU 2695 NE2 HIS A 264 3102 3001 2986 -258 99 320 N ATOM 2696 N ALA A 265 -11.993 13.646 13.703 1.00 25.85 N ANISOU 2696 N ALA A 265 3311 3218 3292 -494 371 475 N ATOM 2697 CA ALA A 265 -12.153 12.885 12.476 1.00 25.22 C ANISOU 2697 CA ALA A 265 3264 3179 3139 -479 448 507 C ATOM 2698 C ALA A 265 -13.290 13.480 11.648 1.00 26.10 C ANISOU 2698 C ALA A 265 3513 3244 3160 -443 420 545 C ATOM 2699 O ALA A 265 -14.310 13.901 12.211 1.00 25.09 O ANISOU 2699 O ALA A 265 3423 3091 3018 -385 330 524 O ATOM 2700 CB ALA A 265 -12.437 11.416 12.790 1.00 20.33 C ANISOU 2700 CB ALA A 265 2577 2647 2500 -415 444 465 C ATOM 2701 N PRO A 266 -13.143 13.563 10.327 1.00 22.96 N ANISOU 2701 N PRO A 266 3194 2832 2697 -473 493 600 N ATOM 2702 CA PRO A 266 -14.176 14.213 9.515 1.00 25.54 C ANISOU 2702 CA PRO A 266 3661 3106 2937 -441 452 644 C ATOM 2703 C PRO A 266 -15.509 13.494 9.631 1.00 24.78 C ANISOU 2703 C PRO A 266 3574 3057 2782 -344 375 611 C ATOM 2704 O PRO A 266 -15.576 12.298 9.925 1.00 25.70 O ANISOU 2704 O PRO A 266 3615 3252 2897 -313 384 569 O ATOM 2705 CB PRO A 266 -13.615 14.135 8.089 1.00 21.39 C ANISOU 2705 CB PRO A 266 3210 2577 2341 -496 559 705 C ATOM 2706 CG PRO A 266 -12.588 13.060 8.130 1.00 32.02 C ANISOU 2706 CG PRO A 266 4442 4000 3725 -525 656 675 C ATOM 2707 CD PRO A 266 -12.015 13.082 9.514 1.00 27.79 C ANISOU 2707 CD PRO A 266 3773 3475 3312 -536 619 625 C ATOM 2708 N LEU A 267 -16.581 14.251 9.398 1.00 26.60 N ANISOU 2708 N LEU A 267 3898 3235 2972 -296 295 633 N ATOM 2709 CA LEU A 267 -17.924 13.708 9.561 1.00 24.38 C ANISOU 2709 CA LEU A 267 3613 2997 2652 -205 213 602 C ATOM 2710 C LEU A 267 -18.170 12.531 8.623 1.00 28.44 C ANISOU 2710 C LEU A 267 4144 3579 3083 -194 245 607 C ATOM 2711 O LEU A 267 -18.822 11.552 9.007 1.00 35.92 O ANISOU 2711 O LEU A 267 5031 4592 4024 -147 212 562 O ATOM 2712 CB LEU A 267 -18.961 14.805 9.332 1.00 25.88 C ANISOU 2712 CB LEU A 267 3899 3114 2821 -153 124 631 C ATOM 2713 CG LEU A 267 -20.377 14.434 9.766 1.00 29.67 C ANISOU 2713 CG LEU A 267 4344 3635 3293 -57 32 590 C ATOM 2714 CD1 LEU A 267 -20.433 14.292 11.278 1.00 28.73 C ANISOU 2714 CD1 LEU A 267 4117 3546 3255 -32 14 521 C ATOM 2715 CD2 LEU A 267 -21.394 15.449 9.270 1.00 29.02 C ANISOU 2715 CD2 LEU A 267 4358 3481 3186 4 -56 627 C ATOM 2716 N TRP A 268 -17.652 12.600 7.391 1.00 27.93 N ANISOU 2716 N TRP A 268 4169 3496 2949 -242 313 660 N ATOM 2717 CA TRP A 268 -17.857 11.493 6.460 1.00 29.35 C ANISOU 2717 CA TRP A 268 4381 3732 3037 -233 345 658 C ATOM 2718 C TRP A 268 -17.164 10.225 6.936 1.00 32.11 C ANISOU 2718 C TRP A 268 4618 4155 3427 -243 413 603 C ATOM 2719 O TRP A 268 -17.671 9.121 6.709 1.00 34.10 O ANISOU 2719 O TRP A 268 4861 4460 3633 -210 400 572 O ATOM 2720 CB TRP A 268 -17.377 11.866 5.054 1.00 28.58 C ANISOU 2720 CB TRP A 268 4416 3599 2844 -284 417 724 C ATOM 2721 CG TRP A 268 -15.897 12.129 4.928 1.00 27.16 C ANISOU 2721 CG TRP A 268 4212 3403 2704 -370 549 746 C ATOM 2722 CD1 TRP A 268 -15.278 13.343 4.979 1.00 25.74 C ANISOU 2722 CD1 TRP A 268 4063 3150 2568 -429 576 794 C ATOM 2723 CD2 TRP A 268 -14.861 11.160 4.707 1.00 21.57 C ANISOU 2723 CD2 TRP A 268 3439 2754 2004 -406 672 721 C ATOM 2724 NE1 TRP A 268 -13.922 13.191 4.817 1.00 24.46 N ANISOU 2724 NE1 TRP A 268 3847 3003 2445 -508 710 802 N ATOM 2725 CE2 TRP A 268 -13.640 11.862 4.650 1.00 22.39 C ANISOU 2725 CE2 TRP A 268 3522 2824 2164 -488 772 756 C ATOM 2726 CE3 TRP A 268 -14.846 9.770 4.564 1.00 21.10 C ANISOU 2726 CE3 TRP A 268 3334 2766 1916 -375 706 670 C ATOM 2727 CZ2 TRP A 268 -12.417 11.221 4.449 1.00 26.83 C ANISOU 2727 CZ2 TRP A 268 4005 3430 2759 -535 909 740 C ATOM 2728 CZ3 TRP A 268 -13.632 9.134 4.370 1.00 26.94 C ANISOU 2728 CZ3 TRP A 268 4010 3542 2686 -414 839 653 C ATOM 2729 CH2 TRP A 268 -12.434 9.861 4.310 1.00 27.91 C ANISOU 2729 CH2 TRP A 268 4099 3638 2868 -490 941 687 C ATOM 2730 N LEU A 269 -16.012 10.359 7.596 1.00 31.11 N ANISOU 2730 N LEU A 269 4404 4026 3388 -289 478 592 N ATOM 2731 CA LEU A 269 -15.371 9.195 8.193 1.00 26.98 C ANISOU 2731 CA LEU A 269 3766 3566 2918 -287 524 541 C ATOM 2732 C LEU A 269 -16.186 8.657 9.362 1.00 24.74 C ANISOU 2732 C LEU A 269 3408 3318 2675 -229 433 489 C ATOM 2733 O LEU A 269 -16.230 7.441 9.581 1.00 16.90 O ANISOU 2733 O LEU A 269 2363 2378 1681 -205 441 451 O ATOM 2734 CB LEU A 269 -13.955 9.556 8.640 1.00 27.47 C ANISOU 2734 CB LEU A 269 3745 3617 3076 -349 599 544 C ATOM 2735 CG LEU A 269 -13.059 8.433 9.151 1.00 23.41 C ANISOU 2735 CG LEU A 269 3108 3161 2627 -348 654 499 C ATOM 2736 CD1 LEU A 269 -12.931 7.350 8.100 1.00 24.89 C ANISOU 2736 CD1 LEU A 269 3331 3386 2741 -334 735 493 C ATOM 2737 CD2 LEU A 269 -11.697 8.990 9.517 1.00 19.19 C ANISOU 2737 CD2 LEU A 269 2487 2609 2193 -414 715 510 C ATOM 2738 N MET A 270 -16.840 9.543 10.116 1.00 21.51 N ANISOU 2738 N MET A 270 3000 2877 2298 -206 350 487 N ATOM 2739 CA MET A 270 -17.747 9.092 11.167 1.00 23.48 C ANISOU 2739 CA MET A 270 3190 3161 2569 -151 273 441 C ATOM 2740 C MET A 270 -18.902 8.296 10.577 1.00 23.89 C ANISOU 2740 C MET A 270 3277 3250 2549 -107 233 434 C ATOM 2741 O MET A 270 -19.247 7.218 11.073 1.00 27.48 O ANISOU 2741 O MET A 270 3673 3757 3010 -85 220 397 O ATOM 2742 CB MET A 270 -18.269 10.291 11.959 1.00 25.89 C ANISOU 2742 CB MET A 270 3504 3419 2914 -129 203 437 C ATOM 2743 CG MET A 270 -17.190 11.078 12.675 1.00 29.79 C ANISOU 2743 CG MET A 270 3964 3871 3484 -178 224 434 C ATOM 2744 SD MET A 270 -16.326 10.062 13.878 1.00 35.07 S ANISOU 2744 SD MET A 270 4506 4599 4218 -192 243 384 S ATOM 2745 CE MET A 270 -17.704 9.398 14.810 1.00 31.90 C ANISOU 2745 CE MET A 270 4078 4249 3794 -117 171 338 C ATOM 2746 N TYR A 271 -19.513 8.820 9.511 1.00 27.46 N ANISOU 2746 N TYR A 271 3828 3672 2932 -97 207 473 N ATOM 2747 CA TYR A 271 -20.594 8.104 8.843 1.00 24.67 C ANISOU 2747 CA TYR A 271 3512 3353 2510 -63 157 468 C ATOM 2748 C TYR A 271 -20.118 6.756 8.313 1.00 24.14 C ANISOU 2748 C TYR A 271 3441 3329 2402 -85 219 448 C ATOM 2749 O TYR A 271 -20.849 5.760 8.381 1.00 24.62 O ANISOU 2749 O TYR A 271 3478 3431 2444 -62 181 416 O ATOM 2750 CB TYR A 271 -21.165 8.963 7.714 1.00 21.03 C ANISOU 2750 CB TYR A 271 3171 2845 1976 -52 112 520 C ATOM 2751 CG TYR A 271 -22.216 9.957 8.170 1.00 27.87 C ANISOU 2751 CG TYR A 271 4037 3679 2874 3 13 526 C ATOM 2752 CD1 TYR A 271 -21.862 11.128 8.827 1.00 33.04 C ANISOU 2752 CD1 TYR A 271 4688 4275 3591 2 13 536 C ATOM 2753 CD2 TYR A 271 -23.563 9.720 7.945 1.00 28.06 C ANISOU 2753 CD2 TYR A 271 4061 3729 2872 57 -81 517 C ATOM 2754 CE1 TYR A 271 -22.821 12.033 9.242 1.00 30.52 C ANISOU 2754 CE1 TYR A 271 4373 3920 3304 64 -73 535 C ATOM 2755 CE2 TYR A 271 -24.529 10.618 8.355 1.00 25.15 C ANISOU 2755 CE2 TYR A 271 3680 3333 2543 119 -167 519 C ATOM 2756 CZ TYR A 271 -24.154 11.775 9.002 1.00 25.30 C ANISOU 2756 CZ TYR A 271 3703 3289 2620 127 -159 526 C ATOM 2757 OH TYR A 271 -25.118 12.673 9.416 1.00 25.75 O ANISOU 2757 OH TYR A 271 3752 3313 2720 199 -240 521 O ATOM 2758 N LEU A 272 -18.888 6.704 7.797 1.00 21.64 N ANISOU 2758 N LEU A 272 3146 3000 2077 -129 319 463 N ATOM 2759 CA LEU A 272 -18.350 5.452 7.276 1.00 21.01 C ANISOU 2759 CA LEU A 272 3066 2955 1964 -142 390 438 C ATOM 2760 C LEU A 272 -18.137 4.432 8.389 1.00 23.05 C ANISOU 2760 C LEU A 272 3210 3251 2296 -126 391 389 C ATOM 2761 O LEU A 272 -18.466 3.251 8.226 1.00 24.04 O ANISOU 2761 O LEU A 272 3336 3406 2394 -111 386 357 O ATOM 2762 CB LEU A 272 -17.043 5.727 6.537 1.00 28.73 C ANISOU 2762 CB LEU A 272 4076 3912 2928 -189 510 465 C ATOM 2763 CG LEU A 272 -16.737 4.821 5.352 1.00 36.22 C ANISOU 2763 CG LEU A 272 5098 4877 3785 -198 587 456 C ATOM 2764 CD1 LEU A 272 -17.858 4.912 4.329 1.00 35.90 C ANISOU 2764 CD1 LEU A 272 5190 4826 3624 -184 517 476 C ATOM 2765 CD2 LEU A 272 -15.405 5.213 4.732 1.00 37.83 C ANISOU 2765 CD2 LEU A 272 5319 5066 3989 -247 723 483 C ATOM 2766 N ALA A 273 -17.591 4.867 9.528 1.00 15.92 N ANISOU 2766 N ALA A 273 2220 2344 1485 -131 391 382 N ATOM 2767 CA ALA A 273 -17.398 3.959 10.656 1.00 21.54 C ANISOU 2767 CA ALA A 273 2835 3088 2260 -115 380 342 C ATOM 2768 C ALA A 273 -18.726 3.426 11.176 1.00 25.53 C ANISOU 2768 C ALA A 273 3332 3621 2749 -81 296 319 C ATOM 2769 O ALA A 273 -18.847 2.234 11.482 1.00 21.25 O ANISOU 2769 O ALA A 273 2759 3106 2211 -71 294 292 O ATOM 2770 CB ALA A 273 -16.639 4.667 11.778 1.00 15.13 C ANISOU 2770 CB ALA A 273 1947 2265 1538 -130 377 341 C ATOM 2771 N ILE A 274 -19.732 4.300 11.287 1.00 17.91 N ANISOU 2771 N ILE A 274 2389 2645 1770 -63 228 332 N ATOM 2772 CA ILE A 274 -21.046 3.893 11.781 1.00 16.21 C ANISOU 2772 CA ILE A 274 2149 2462 1549 -33 156 311 C ATOM 2773 C ILE A 274 -21.651 2.829 10.870 1.00 19.43 C ANISOU 2773 C ILE A 274 2599 2890 1894 -35 143 303 C ATOM 2774 O ILE A 274 -22.159 1.801 11.332 1.00 19.56 O ANISOU 2774 O ILE A 274 2577 2937 1919 -32 122 276 O ATOM 2775 CB ILE A 274 -21.964 5.124 11.910 1.00 20.51 C ANISOU 2775 CB ILE A 274 2710 2988 2097 -4 91 326 C ATOM 2776 CG1 ILE A 274 -21.540 5.999 13.096 1.00 22.85 C ANISOU 2776 CG1 ILE A 274 2959 3264 2458 1 93 317 C ATOM 2777 CG2 ILE A 274 -23.434 4.713 12.007 1.00 19.43 C ANISOU 2777 CG2 ILE A 274 2550 2887 1946 27 21 309 C ATOM 2778 CD1 ILE A 274 -21.899 5.430 14.460 1.00 13.85 C ANISOU 2778 CD1 ILE A 274 1741 2165 1355 16 76 279 C ATOM 2779 N VAL A 275 -21.601 3.062 9.558 1.00 18.09 N ANISOU 2779 N VAL A 275 2519 2699 1655 -44 154 326 N ATOM 2780 CA VAL A 275 -22.150 2.101 8.606 1.00 23.72 C ANISOU 2780 CA VAL A 275 3290 3425 2296 -50 134 313 C ATOM 2781 C VAL A 275 -21.390 0.780 8.677 1.00 20.70 C ANISOU 2781 C VAL A 275 2891 3052 1921 -64 199 281 C ATOM 2782 O VAL A 275 -21.992 -0.301 8.668 1.00 17.76 O ANISOU 2782 O VAL A 275 2518 2696 1535 -66 167 252 O ATOM 2783 CB VAL A 275 -22.135 2.702 7.188 1.00 32.85 C ANISOU 2783 CB VAL A 275 4566 4553 3363 -58 136 347 C ATOM 2784 CG1 VAL A 275 -22.354 1.626 6.142 1.00 31.04 C ANISOU 2784 CG1 VAL A 275 4415 4333 3048 -71 136 326 C ATOM 2785 CG2 VAL A 275 -23.189 3.794 7.067 1.00 23.68 C ANISOU 2785 CG2 VAL A 275 3426 3380 2192 -31 42 377 C ATOM 2786 N LEU A 276 -20.059 0.844 8.771 1.00 18.48 N ANISOU 2786 N LEU A 276 2594 2757 1672 -74 288 283 N ATOM 2787 CA LEU A 276 -19.263 -0.378 8.853 1.00 20.32 C ANISOU 2787 CA LEU A 276 2804 2993 1923 -75 349 251 C ATOM 2788 C LEU A 276 -19.640 -1.208 10.078 1.00 23.71 C ANISOU 2788 C LEU A 276 3155 3441 2413 -64 306 227 C ATOM 2789 O LEU A 276 -19.750 -2.439 9.994 1.00 24.74 O ANISOU 2789 O LEU A 276 3298 3570 2533 -62 307 199 O ATOM 2790 CB LEU A 276 -17.773 -0.030 8.871 1.00 23.55 C ANISOU 2790 CB LEU A 276 3180 3390 2378 -83 447 261 C ATOM 2791 CG LEU A 276 -16.801 -1.203 9.023 1.00 27.20 C ANISOU 2791 CG LEU A 276 3601 3852 2880 -70 514 228 C ATOM 2792 CD1 LEU A 276 -16.875 -2.120 7.807 1.00 21.83 C ANISOU 2792 CD1 LEU A 276 3015 3162 2117 -66 556 202 C ATOM 2793 CD2 LEU A 276 -15.367 -0.722 9.269 1.00 19.01 C ANISOU 2793 CD2 LEU A 276 2494 2811 1917 -78 596 239 C ATOM 2794 N ALA A 277 -19.861 -0.551 11.221 1.00 14.15 N ANISOU 2794 N ALA A 277 1876 2243 1259 -58 267 238 N ATOM 2795 CA ALA A 277 -20.263 -1.269 12.427 1.00 13.67 C ANISOU 2795 CA ALA A 277 1752 2200 1241 -52 230 221 C ATOM 2796 C ALA A 277 -21.622 -1.939 12.254 1.00 23.60 C ANISOU 2796 C ALA A 277 3030 3475 2462 -59 170 209 C ATOM 2797 O ALA A 277 -21.824 -3.071 12.709 1.00 30.46 O ANISOU 2797 O ALA A 277 3883 4347 3344 -67 161 192 O ATOM 2798 CB ALA A 277 -20.286 -0.316 13.622 1.00 13.31 C ANISOU 2798 CB ALA A 277 1647 2165 1247 -45 204 230 C ATOM 2799 N HIS A 278 -22.569 -1.253 11.608 1.00 19.41 N ANISOU 2799 N HIS A 278 2532 2953 1892 -57 123 220 N ATOM 2800 CA HIS A 278 -23.880 -1.845 11.359 1.00 18.65 C ANISOU 2800 CA HIS A 278 2442 2876 1769 -68 57 208 C ATOM 2801 C HIS A 278 -23.792 -3.023 10.400 1.00 19.44 C ANISOU 2801 C HIS A 278 2611 2958 1818 -89 66 186 C ATOM 2802 O HIS A 278 -24.541 -3.995 10.550 1.00 18.95 O ANISOU 2802 O HIS A 278 2539 2904 1757 -112 27 167 O ATOM 2803 CB HIS A 278 -24.839 -0.789 10.808 1.00 19.56 C ANISOU 2803 CB HIS A 278 2573 3000 1858 -54 -6 226 C ATOM 2804 CG HIS A 278 -25.134 0.315 11.772 1.00 23.54 C ANISOU 2804 CG HIS A 278 3013 3518 2415 -26 -21 237 C ATOM 2805 ND1 HIS A 278 -25.716 1.504 11.390 1.00 25.57 N ANISOU 2805 ND1 HIS A 278 3285 3768 2663 2 -67 257 N ATOM 2806 CD2 HIS A 278 -24.934 0.406 13.108 1.00 24.26 C ANISOU 2806 CD2 HIS A 278 3035 3622 2561 -19 0 229 C ATOM 2807 CE1 HIS A 278 -25.856 2.282 12.448 1.00 29.64 C ANISOU 2807 CE1 HIS A 278 3741 4289 3231 28 -68 255 C ATOM 2808 NE2 HIS A 278 -25.391 1.639 13.503 1.00 26.67 N ANISOU 2808 NE2 HIS A 278 3316 3929 2890 13 -26 237 N ATOM 2809 N THR A 279 -22.886 -2.954 9.418 1.00 17.63 N ANISOU 2809 N THR A 279 2454 2702 1544 -86 121 187 N ATOM 2810 CA THR A 279 -22.742 -4.031 8.439 1.00 21.16 C ANISOU 2810 CA THR A 279 2983 3125 1930 -100 139 158 C ATOM 2811 C THR A 279 -22.439 -5.367 9.106 1.00 21.61 C ANISOU 2811 C THR A 279 3011 3168 2031 -105 160 129 C ATOM 2812 O THR A 279 -22.835 -6.421 8.593 1.00 23.02 O ANISOU 2812 O THR A 279 3245 3326 2174 -123 138 99 O ATOM 2813 CB THR A 279 -21.646 -3.670 7.429 1.00 20.75 C ANISOU 2813 CB THR A 279 3005 3051 1828 -91 223 162 C ATOM 2814 OG1 THR A 279 -22.106 -2.610 6.580 1.00 28.55 O ANISOU 2814 OG1 THR A 279 4055 4041 2750 -94 189 192 O ATOM 2815 CG2 THR A 279 -21.272 -4.865 6.567 1.00 22.18 C ANISOU 2815 CG2 THR A 279 3269 3204 1953 -95 265 121 C ATOM 2816 N ASN A 280 -21.756 -5.343 10.253 1.00 20.33 N ANISOU 2816 N ASN A 280 2771 3009 1944 -89 193 138 N ATOM 2817 CA ASN A 280 -21.439 -6.579 10.959 1.00 25.83 C ANISOU 2817 CA ASN A 280 3447 3684 2683 -89 205 120 C ATOM 2818 C ASN A 280 -22.687 -7.405 11.238 1.00 23.30 C ANISOU 2818 C ASN A 280 3128 3366 2357 -124 136 110 C ATOM 2819 O ASN A 280 -22.621 -8.639 11.267 1.00 23.27 O ANISOU 2819 O ASN A 280 3156 3327 2358 -135 137 88 O ATOM 2820 CB ASN A 280 -20.719 -6.267 12.270 1.00 24.91 C ANISOU 2820 CB ASN A 280 3246 3577 2642 -70 225 139 C ATOM 2821 CG ASN A 280 -20.277 -7.510 12.989 1.00 27.03 C ANISOU 2821 CG ASN A 280 3502 3816 2952 -62 232 128 C ATOM 2822 OD1 ASN A 280 -19.338 -8.180 12.566 1.00 35.90 O ANISOU 2822 OD1 ASN A 280 4650 4904 4086 -37 281 109 O ATOM 2823 ND2 ASN A 280 -20.950 -7.832 14.081 1.00 26.83 N ANISOU 2823 ND2 ASN A 280 3440 3803 2950 -81 186 142 N ATOM 2824 N SER A 281 -23.829 -6.747 11.430 1.00 17.74 N ANISOU 2824 N SER A 281 2390 2703 1649 -143 75 125 N ATOM 2825 CA SER A 281 -25.076 -7.444 11.693 1.00 19.55 C ANISOU 2825 CA SER A 281 2602 2944 1883 -185 12 118 C ATOM 2826 C SER A 281 -25.591 -8.207 10.481 1.00 23.08 C ANISOU 2826 C SER A 281 3131 3365 2272 -215 -27 89 C ATOM 2827 O SER A 281 -26.590 -8.927 10.595 1.00 26.38 O ANISOU 2827 O SER A 281 3539 3787 2699 -262 -82 79 O ATOM 2828 CB SER A 281 -26.112 -6.435 12.195 1.00 17.63 C ANISOU 2828 CB SER A 281 2284 2755 1660 -186 -34 139 C ATOM 2829 OG SER A 281 -25.799 -6.042 13.522 1.00 20.39 O ANISOU 2829 OG SER A 281 2565 3124 2060 -169 -3 157 O ATOM 2830 N VAL A 282 -24.931 -8.087 9.329 1.00 17.77 N ANISOU 2830 N VAL A 282 2545 2667 1539 -196 3 73 N ATOM 2831 CA VAL A 282 -25.325 -8.810 8.128 1.00 20.19 C ANISOU 2831 CA VAL A 282 2952 2944 1774 -222 -33 38 C ATOM 2832 C VAL A 282 -24.426 -10.011 7.846 1.00 23.12 C ANISOU 2832 C VAL A 282 3397 3254 2135 -215 27 -1 C ATOM 2833 O VAL A 282 -24.912 -11.018 7.320 1.00 26.47 O ANISOU 2833 O VAL A 282 3890 3641 2526 -250 -13 -37 O ATOM 2834 CB VAL A 282 -25.349 -7.861 6.908 1.00 17.88 C ANISOU 2834 CB VAL A 282 2731 2664 1400 -208 -45 44 C ATOM 2835 CG1 VAL A 282 -25.842 -8.580 5.662 1.00 19.08 C ANISOU 2835 CG1 VAL A 282 3000 2788 1463 -239 -97 5 C ATOM 2836 CG2 VAL A 282 -26.230 -6.641 7.174 1.00 16.74 C ANISOU 2836 CG2 VAL A 282 2516 2569 1274 -203 -110 82 C ATOM 2837 N VAL A 283 -23.144 -9.958 8.228 1.00 25.42 N ANISOU 2837 N VAL A 283 3668 3529 2461 -169 116 4 N ATOM 2838 CA VAL A 283 -22.172 -10.923 7.711 1.00 30.66 C ANISOU 2838 CA VAL A 283 4407 4135 3110 -142 185 -37 C ATOM 2839 C VAL A 283 -22.251 -12.281 8.393 1.00 38.25 C ANISOU 2839 C VAL A 283 5369 5044 4121 -155 167 -56 C ATOM 2840 O VAL A 283 -21.821 -13.275 7.800 1.00 49.19 O ANISOU 2840 O VAL A 283 6840 6368 5484 -141 197 -102 O ATOM 2841 CB VAL A 283 -20.737 -10.384 7.846 1.00 31.61 C ANISOU 2841 CB VAL A 283 4489 4258 3263 -86 287 -26 C ATOM 2842 CG1 VAL A 283 -20.574 -9.129 7.023 1.00 32.40 C ANISOU 2842 CG1 VAL A 283 4611 4394 3304 -82 315 -7 C ATOM 2843 CG2 VAL A 283 -20.412 -10.106 9.310 1.00 35.60 C ANISOU 2843 CG2 VAL A 283 4877 4785 3865 -72 284 12 C ATOM 2844 N ASN A 284 -22.775 -12.357 9.622 1.00 34.43 N ANISOU 2844 N ASN A 284 4802 4578 3701 -179 124 -22 N ATOM 2845 CA ASN A 284 -22.808 -13.633 10.337 1.00 39.58 C ANISOU 2845 CA ASN A 284 5464 5174 4399 -194 110 -29 C ATOM 2846 C ASN A 284 -23.622 -14.709 9.616 1.00 43.25 C ANISOU 2846 C ASN A 284 6023 5587 4824 -248 57 -70 C ATOM 2847 O ASN A 284 -23.119 -15.840 9.478 1.00 41.58 O ANISOU 2847 O ASN A 284 5882 5296 4621 -233 78 -103 O ATOM 2848 CB ASN A 284 -23.290 -13.398 11.776 1.00 41.47 C ANISOU 2848 CB ASN A 284 5607 5451 4699 -219 79 21 C ATOM 2849 CG ASN A 284 -22.246 -12.677 12.633 1.00 39.77 C ANISOU 2849 CG ASN A 284 5319 5262 4531 -163 128 52 C ATOM 2850 OD1 ASN A 284 -21.285 -12.110 12.119 1.00 41.53 O ANISOU 2850 OD1 ASN A 284 5541 5490 4749 -114 182 42 O ATOM 2851 ND2 ASN A 284 -22.429 -12.716 13.944 1.00 38.02 N ANISOU 2851 ND2 ASN A 284 5038 5055 4354 -175 109 89 N ATOM 2852 N PRO A 285 -24.842 -14.450 9.123 1.00 35.56 N ANISOU 2852 N PRO A 285 5055 4646 3810 -308 -17 -73 N ATOM 2853 CA PRO A 285 -25.556 -15.494 8.365 1.00 33.37 C ANISOU 2853 CA PRO A 285 4873 4313 3493 -366 -76 -119 C ATOM 2854 C PRO A 285 -24.811 -15.992 7.133 1.00 38.67 C ANISOU 2854 C PRO A 285 5677 4924 4093 -329 -36 -180 C ATOM 2855 O PRO A 285 -25.054 -17.126 6.703 1.00 35.67 O ANISOU 2855 O PRO A 285 5392 4469 3693 -363 -66 -226 O ATOM 2856 CB PRO A 285 -26.872 -14.807 7.978 1.00 30.98 C ANISOU 2856 CB PRO A 285 4534 4077 3162 -422 -165 -108 C ATOM 2857 CG PRO A 285 -27.077 -13.789 9.031 1.00 30.16 C ANISOU 2857 CG PRO A 285 4297 4048 3115 -408 -155 -51 C ATOM 2858 CD PRO A 285 -25.704 -13.279 9.359 1.00 29.62 C ANISOU 2858 CD PRO A 285 4216 3979 3060 -329 -61 -36 C ATOM 2859 N PHE A 286 -23.913 -15.194 6.549 1.00 41.87 N ANISOU 2859 N PHE A 286 6098 5354 4458 -266 37 -183 N ATOM 2860 CA PHE A 286 -23.154 -15.680 5.400 1.00 45.00 C ANISOU 2860 CA PHE A 286 6621 5696 4781 -228 96 -244 C ATOM 2861 C PHE A 286 -22.023 -16.612 5.807 1.00 51.02 C ANISOU 2861 C PHE A 286 7398 6387 5602 -168 177 -269 C ATOM 2862 O PHE A 286 -21.681 -17.527 5.048 1.00 51.03 O ANISOU 2862 O PHE A 286 7516 6313 5561 -149 206 -334 O ATOM 2863 CB PHE A 286 -22.607 -14.506 4.589 1.00 43.05 C ANISOU 2863 CB PHE A 286 6389 5501 4466 -189 157 -236 C ATOM 2864 CG PHE A 286 -23.648 -13.824 3.771 1.00 45.86 C ANISOU 2864 CG PHE A 286 6788 5901 4735 -237 71 -229 C ATOM 2865 CD1 PHE A 286 -23.949 -14.278 2.499 1.00 46.46 C ANISOU 2865 CD1 PHE A 286 7012 5943 4699 -258 41 -284 C ATOM 2866 CD2 PHE A 286 -24.356 -12.754 4.287 1.00 46.16 C ANISOU 2866 CD2 PHE A 286 6724 6010 4804 -257 13 -171 C ATOM 2867 CE1 PHE A 286 -24.923 -13.666 1.748 1.00 48.08 C ANISOU 2867 CE1 PHE A 286 7259 6186 4823 -301 -56 -275 C ATOM 2868 CE2 PHE A 286 -25.332 -12.137 3.540 1.00 48.09 C ANISOU 2868 CE2 PHE A 286 7004 6291 4979 -291 -78 -162 C ATOM 2869 CZ PHE A 286 -25.618 -12.596 2.269 1.00 48.05 C ANISOU 2869 CZ PHE A 286 7142 6253 4861 -315 -118 -212 C ATOM 2870 N ILE A 287 -21.439 -16.410 6.990 1.00 48.28 N ANISOU 2870 N ILE A 287 6939 6055 5349 -133 210 -223 N ATOM 2871 CA ILE A 287 -20.360 -17.286 7.429 1.00 47.41 C ANISOU 2871 CA ILE A 287 6834 5877 5305 -68 272 -241 C ATOM 2872 C ILE A 287 -20.896 -18.673 7.753 1.00 47.08 C ANISOU 2872 C ILE A 287 6858 5744 5288 -105 211 -262 C ATOM 2873 O ILE A 287 -20.261 -19.687 7.441 1.00 52.33 O ANISOU 2873 O ILE A 287 7603 6317 5961 -59 249 -312 O ATOM 2874 CB ILE A 287 -19.624 -16.668 8.628 1.00 46.03 C ANISOU 2874 CB ILE A 287 6525 5745 5220 -25 302 -182 C ATOM 2875 CG1 ILE A 287 -19.179 -15.245 8.297 1.00 45.28 C ANISOU 2875 CG1 ILE A 287 6368 5733 5103 -4 354 -159 C ATOM 2876 CG2 ILE A 287 -18.426 -17.520 9.012 1.00 44.94 C ANISOU 2876 CG2 ILE A 287 6384 5537 5155 54 359 -200 C ATOM 2877 CD1 ILE A 287 -18.300 -15.165 7.075 1.00 45.79 C ANISOU 2877 CD1 ILE A 287 6499 5785 5113 44 451 -208 C ATOM 2878 N TYR A 288 -22.074 -18.744 8.378 1.00 43.53 N ANISOU 2878 N TYR A 288 6376 5312 4853 -189 122 -225 N ATOM 2879 CA TYR A 288 -22.678 -20.042 8.663 1.00 41.44 C ANISOU 2879 CA TYR A 288 6177 4958 4611 -244 62 -240 C ATOM 2880 C TYR A 288 -23.056 -20.774 7.383 1.00 38.52 C ANISOU 2880 C TYR A 288 5951 4521 4165 -274 36 -317 C ATOM 2881 O TYR A 288 -22.983 -22.005 7.331 1.00 48.57 O ANISOU 2881 O TYR A 288 7318 5685 5453 -280 23 -356 O ATOM 2882 CB TYR A 288 -23.906 -19.866 9.552 1.00 43.91 C ANISOU 2882 CB TYR A 288 6412 5317 4953 -338 -16 -183 C ATOM 2883 CG TYR A 288 -23.633 -19.088 10.817 1.00 47.28 C ANISOU 2883 CG TYR A 288 6712 5814 5439 -314 7 -111 C ATOM 2884 CD1 TYR A 288 -22.455 -19.271 11.528 1.00 48.86 C ANISOU 2884 CD1 TYR A 288 6889 5983 5694 -235 60 -92 C ATOM 2885 CD2 TYR A 288 -24.550 -18.161 11.293 1.00 48.25 C ANISOU 2885 CD2 TYR A 288 6738 6032 5564 -365 -29 -68 C ATOM 2886 CE1 TYR A 288 -22.201 -18.557 12.683 1.00 50.39 C ANISOU 2886 CE1 TYR A 288 6976 6238 5931 -216 70 -31 C ATOM 2887 CE2 TYR A 288 -24.306 -17.443 12.444 1.00 49.41 C ANISOU 2887 CE2 TYR A 288 6782 6237 5754 -342 -7 -11 C ATOM 2888 CZ TYR A 288 -23.131 -17.644 13.137 1.00 51.50 C ANISOU 2888 CZ TYR A 288 7036 6469 6062 -272 39 7 C ATOM 2889 OH TYR A 288 -22.891 -16.929 14.288 1.00 52.26 O ANISOU 2889 OH TYR A 288 7041 6622 6193 -253 50 59 O ATOM 2890 N ALA A 289 -23.451 -20.036 6.343 1.00 33.38 N ANISOU 2890 N ALA A 289 5330 3927 3426 -293 22 -342 N ATOM 2891 CA ALA A 289 -23.851 -20.669 5.091 1.00 37.57 C ANISOU 2891 CA ALA A 289 6009 4400 3867 -326 -14 -419 C ATOM 2892 C ALA A 289 -22.651 -21.234 4.343 1.00 43.09 C ANISOU 2892 C ALA A 289 6818 5024 4530 -236 85 -489 C ATOM 2893 O ALA A 289 -22.726 -22.332 3.781 1.00 53.14 O ANISOU 2893 O ALA A 289 8224 6195 5771 -247 67 -558 O ATOM 2894 CB ALA A 289 -24.602 -19.670 4.211 1.00 30.98 C ANISOU 2894 CB ALA A 289 5180 3650 2942 -367 -66 -418 C ATOM 2895 N TYR A 290 -21.541 -20.500 4.319 1.00 42.91 N ANISOU 2895 N TYR A 290 6741 5048 4515 -146 192 -475 N ATOM 2896 CA TYR A 290 -20.373 -20.948 3.576 1.00 48.86 C ANISOU 2896 CA TYR A 290 7581 5744 5239 -55 304 -543 C ATOM 2897 C TYR A 290 -19.510 -21.928 4.359 1.00 48.37 C ANISOU 2897 C TYR A 290 7500 5594 5285 16 348 -551 C ATOM 2898 O TYR A 290 -18.713 -22.650 3.749 1.00 50.82 O ANISOU 2898 O TYR A 290 7902 5827 5581 90 425 -623 O ATOM 2899 CB TYR A 290 -19.529 -19.744 3.147 1.00 59.76 C ANISOU 2899 CB TYR A 290 8906 7214 6587 3 408 -525 C ATOM 2900 CG TYR A 290 -20.100 -18.993 1.966 1.00 70.56 C ANISOU 2900 CG TYR A 290 10356 8635 7817 -41 390 -541 C ATOM 2901 CD1 TYR A 290 -19.826 -19.398 0.666 1.00 77.07 C ANISOU 2901 CD1 TYR A 290 11341 9416 8525 -20 443 -623 C ATOM 2902 CD2 TYR A 290 -20.915 -17.883 2.149 1.00 74.61 C ANISOU 2902 CD2 TYR A 290 10795 9239 8314 -99 316 -476 C ATOM 2903 CE1 TYR A 290 -20.347 -18.716 -0.421 1.00 79.81 C ANISOU 2903 CE1 TYR A 290 11780 9811 8734 -61 417 -633 C ATOM 2904 CE2 TYR A 290 -21.443 -17.195 1.071 1.00 77.55 C ANISOU 2904 CE2 TYR A 290 11250 9655 8561 -135 286 -484 C ATOM 2905 CZ TYR A 290 -21.156 -17.615 -0.213 1.00 80.81 C ANISOU 2905 CZ TYR A 290 11829 10025 8850 -118 333 -560 C ATOM 2906 OH TYR A 290 -21.678 -16.935 -1.290 1.00 83.15 O ANISOU 2906 OH TYR A 290 12222 10362 9010 -154 294 -563 O ATOM 2907 N ARG A 291 -19.658 -21.992 5.685 1.00 44.07 N ANISOU 2907 N ARG A 291 6848 5054 4842 0 301 -481 N ATOM 2908 CA ARG A 291 -18.756 -22.788 6.504 1.00 43.45 C ANISOU 2908 CA ARG A 291 6742 4899 4868 78 336 -475 C ATOM 2909 C ARG A 291 -19.419 -23.918 7.283 1.00 40.26 C ANISOU 2909 C ARG A 291 6383 4398 4516 23 245 -457 C ATOM 2910 O ARG A 291 -18.708 -24.818 7.745 1.00 38.32 O ANISOU 2910 O ARG A 291 6161 4056 4342 91 264 -466 O ATOM 2911 CB ARG A 291 -17.995 -21.884 7.486 1.00 40.99 C ANISOU 2911 CB ARG A 291 6267 4670 4637 130 375 -402 C ATOM 2912 CG ARG A 291 -17.139 -20.826 6.797 1.00 43.88 C ANISOU 2912 CG ARG A 291 6582 5118 4972 188 478 -415 C ATOM 2913 CD ARG A 291 -16.141 -20.204 7.759 1.00 43.01 C ANISOU 2913 CD ARG A 291 6320 5060 4963 252 520 -359 C ATOM 2914 NE ARG A 291 -15.236 -21.207 8.308 1.00 45.58 N ANISOU 2914 NE ARG A 291 6637 5296 5384 339 540 -373 N ATOM 2915 CZ ARG A 291 -14.095 -21.574 7.735 1.00 47.22 C ANISOU 2915 CZ ARG A 291 6853 5465 5621 441 641 -430 C ATOM 2916 NH1 ARG A 291 -13.715 -21.013 6.594 1.00 47.73 N ANISOU 2916 NH1 ARG A 291 6943 5576 5618 460 741 -477 N ATOM 2917 NH2 ARG A 291 -13.333 -22.500 8.306 1.00 46.35 N ANISOU 2917 NH2 ARG A 291 6729 5270 5610 527 644 -438 N ATOM 2918 N ILE A 292 -20.739 -23.916 7.442 1.00 38.38 N ANISOU 2918 N ILE A 292 6156 4179 4250 -97 148 -430 N ATOM 2919 CA ILE A 292 -21.432 -24.948 8.208 1.00 41.52 C ANISOU 2919 CA ILE A 292 6591 4488 4697 -168 67 -405 C ATOM 2920 C ILE A 292 -22.449 -25.624 7.299 1.00 47.62 C ANISOU 2920 C ILE A 292 7493 5198 5401 -263 -3 -467 C ATOM 2921 O ILE A 292 -23.417 -24.989 6.862 1.00 46.24 O ANISOU 2921 O ILE A 292 7297 5104 5169 -347 -57 -463 O ATOM 2922 CB ILE A 292 -22.107 -24.372 9.460 1.00 38.12 C ANISOU 2922 CB ILE A 292 6032 4138 4313 -237 18 -307 C ATOM 2923 CG1 ILE A 292 -21.078 -23.623 10.305 1.00 36.52 C ANISOU 2923 CG1 ILE A 292 5709 3999 4167 -145 78 -253 C ATOM 2924 CG2 ILE A 292 -22.755 -25.482 10.274 1.00 37.34 C ANISOU 2924 CG2 ILE A 292 5980 3945 4264 -314 -50 -274 C ATOM 2925 CD1 ILE A 292 -21.655 -22.991 11.541 1.00 34.16 C ANISOU 2925 CD1 ILE A 292 5294 3782 3902 -201 40 -164 C ATOM 2926 N ARG A 293 -22.235 -26.915 7.026 1.00 56.85 N ANISOU 2926 N ARG A 293 8798 6220 6581 -249 -11 -525 N ATOM 2927 CA ARG A 293 -23.119 -27.637 6.115 1.00 63.31 C ANISOU 2927 CA ARG A 293 9758 6965 7334 -339 -83 -595 C ATOM 2928 C ARG A 293 -24.531 -27.744 6.675 1.00 55.22 C ANISOU 2928 C ARG A 293 8691 5961 6331 -493 -193 -541 C ATOM 2929 O ARG A 293 -25.509 -27.672 5.922 1.00 54.68 O ANISOU 2929 O ARG A 293 8663 5913 6200 -589 -267 -576 O ATOM 2930 CB ARG A 293 -22.564 -29.033 5.828 1.00 72.77 C ANISOU 2930 CB ARG A 293 11114 7986 8551 -289 -68 -668 C ATOM 2931 CG ARG A 293 -21.119 -29.064 5.369 1.00 83.66 C ANISOU 2931 CG ARG A 293 12523 9334 9929 -126 52 -724 C ATOM 2932 CD ARG A 293 -20.700 -30.476 4.985 1.00 92.92 C ANISOU 2932 CD ARG A 293 13866 10323 11116 -76 60 -809 C ATOM 2933 NE ARG A 293 -19.291 -30.547 4.607 1.00100.32 N ANISOU 2933 NE ARG A 293 14815 11231 12069 91 185 -865 N ATOM 2934 CZ ARG A 293 -18.692 -31.644 4.152 1.00106.71 C ANISOU 2934 CZ ARG A 293 15766 11889 12891 174 222 -953 C ATOM 2935 NH1 ARG A 293 -19.380 -32.769 4.015 1.00109.63 N ANISOU 2935 NH1 ARG A 293 16289 12112 13254 99 137 -996 N ATOM 2936 NH2 ARG A 293 -17.405 -31.617 3.833 1.00108.48 N ANISOU 2936 NH2 ARG A 293 15974 12104 13138 330 347 -1002 N ATOM 2937 N GLU A 294 -24.661 -27.926 7.989 1.00 49.91 N ANISOU 2937 N GLU A 294 7935 5283 5746 -521 -207 -455 N ATOM 2938 CA GLU A 294 -25.985 -28.114 8.567 1.00 48.70 C ANISOU 2938 CA GLU A 294 7739 5145 5620 -671 -295 -403 C ATOM 2939 C GLU A 294 -26.812 -26.839 8.479 1.00 47.04 C ANISOU 2939 C GLU A 294 7395 5100 5378 -727 -321 -369 C ATOM 2940 O GLU A 294 -28.023 -26.895 8.236 1.00 46.26 O ANISOU 2940 O GLU A 294 7284 5025 5268 -850 -404 -372 O ATOM 2941 CB GLU A 294 -25.869 -28.582 10.015 1.00 50.31 C ANISOU 2941 CB GLU A 294 7897 5307 5912 -684 -289 -315 C ATOM 2942 CG GLU A 294 -27.140 -29.220 10.550 1.00 54.39 C ANISOU 2942 CG GLU A 294 8416 5787 6462 -846 -367 -273 C ATOM 2943 CD GLU A 294 -27.423 -30.573 9.925 1.00 60.17 C ANISOU 2943 CD GLU A 294 9319 6351 7192 -910 -424 -340 C ATOM 2944 OE1 GLU A 294 -26.480 -31.191 9.388 1.00 63.88 O ANISOU 2944 OE1 GLU A 294 9913 6709 7649 -808 -392 -405 O ATOM 2945 OE2 GLU A 294 -28.590 -31.019 9.971 1.00 61.88 O ANISOU 2945 OE2 GLU A 294 9543 6545 7422 -1062 -499 -329 O ATOM 2946 N PHE A 295 -26.180 -25.679 8.672 1.00 43.58 N ANISOU 2946 N PHE A 295 6852 4774 4932 -637 -256 -338 N ATOM 2947 CA PHE A 295 -26.898 -24.425 8.477 1.00 42.32 C ANISOU 2947 CA PHE A 295 6581 4760 4739 -673 -280 -313 C ATOM 2948 C PHE A 295 -27.258 -24.222 7.012 1.00 41.81 C ANISOU 2948 C PHE A 295 6599 4706 4580 -690 -322 -389 C ATOM 2949 O PHE A 295 -28.392 -23.847 6.689 1.00 39.63 O ANISOU 2949 O PHE A 295 6282 4492 4282 -780 -405 -386 O ATOM 2950 CB PHE A 295 -26.063 -23.249 8.983 1.00 37.54 C ANISOU 2950 CB PHE A 295 5863 4254 4146 -573 -201 -266 C ATOM 2951 CG PHE A 295 -26.368 -22.853 10.396 1.00 35.25 C ANISOU 2951 CG PHE A 295 5444 4027 3923 -600 -199 -178 C ATOM 2952 CD1 PHE A 295 -27.526 -22.154 10.698 1.00 33.03 C ANISOU 2952 CD1 PHE A 295 5058 3845 3647 -682 -245 -140 C ATOM 2953 CD2 PHE A 295 -25.488 -23.161 11.421 1.00 33.15 C ANISOU 2953 CD2 PHE A 295 5162 3722 3713 -539 -150 -135 C ATOM 2954 CE1 PHE A 295 -27.809 -21.781 11.996 1.00 32.81 C ANISOU 2954 CE1 PHE A 295 4919 3875 3671 -705 -230 -65 C ATOM 2955 CE2 PHE A 295 -25.763 -22.789 12.723 1.00 32.39 C ANISOU 2955 CE2 PHE A 295 4964 3683 3662 -565 -147 -57 C ATOM 2956 CZ PHE A 295 -26.927 -22.099 13.011 1.00 34.01 C ANISOU 2956 CZ PHE A 295 5072 3987 3863 -649 -181 -24 C ATOM 2957 N ARG A 296 -26.305 -24.476 6.114 1.00 41.23 N ANISOU 2957 N ARG A 296 6643 4574 4450 -603 -266 -458 N ATOM 2958 CA ARG A 296 -26.520 -24.212 4.697 1.00 41.04 C ANISOU 2958 CA ARG A 296 6716 4564 4315 -609 -294 -530 C ATOM 2959 C ARG A 296 -27.643 -25.076 4.140 1.00 42.53 C ANISOU 2959 C ARG A 296 7000 4684 4476 -730 -413 -579 C ATOM 2960 O ARG A 296 -28.528 -24.584 3.430 1.00 43.72 O ANISOU 2960 O ARG A 296 7150 4897 4566 -795 -498 -593 O ATOM 2961 CB ARG A 296 -25.219 -24.449 3.934 1.00 42.04 C ANISOU 2961 CB ARG A 296 6957 4631 4387 -491 -191 -598 C ATOM 2962 CG ARG A 296 -25.378 -24.454 2.436 1.00 39.91 C ANISOU 2962 CG ARG A 296 6832 4346 3985 -498 -212 -684 C ATOM 2963 CD ARG A 296 -24.028 -24.441 1.741 1.00 39.83 C ANISOU 2963 CD ARG A 296 6907 4308 3920 -372 -79 -741 C ATOM 2964 NE ARG A 296 -23.267 -25.672 1.926 1.00 40.32 N ANISOU 2964 NE ARG A 296 7055 4232 4031 -313 -26 -793 N ATOM 2965 CZ ARG A 296 -22.247 -25.804 2.767 1.00 43.86 C ANISOU 2965 CZ ARG A 296 7428 4661 4577 -219 63 -760 C ATOM 2966 NH1 ARG A 296 -21.608 -26.962 2.862 1.00 45.68 N ANISOU 2966 NH1 ARG A 296 7747 4756 4852 -159 99 -811 N ATOM 2967 NH2 ARG A 296 -21.864 -24.778 3.514 1.00 43.35 N ANISOU 2967 NH2 ARG A 296 7200 4704 4567 -182 108 -678 N ATOM 2968 N GLN A 297 -27.626 -26.373 4.459 1.00 41.88 N ANISOU 2968 N GLN A 297 7003 4469 4442 -765 -430 -603 N ATOM 2969 CA GLN A 297 -28.676 -27.268 3.984 1.00 44.13 C ANISOU 2969 CA GLN A 297 7381 4675 4710 -893 -547 -651 C ATOM 2970 C GLN A 297 -30.032 -26.893 4.560 1.00 41.68 C ANISOU 2970 C GLN A 297 6929 4451 4455 -1024 -643 -585 C ATOM 2971 O GLN A 297 -31.057 -27.053 3.887 1.00 42.40 O ANISOU 2971 O GLN A 297 7051 4546 4514 -1129 -757 -622 O ATOM 2972 CB GLN A 297 -28.328 -28.717 4.333 1.00 52.08 C ANISOU 2972 CB GLN A 297 8507 5511 5771 -902 -540 -681 C ATOM 2973 CG GLN A 297 -27.135 -29.263 3.564 1.00 61.97 C ANISOU 2973 CG GLN A 297 9921 6659 6967 -780 -459 -770 C ATOM 2974 CD GLN A 297 -26.717 -30.644 4.028 1.00 72.22 C ANISOU 2974 CD GLN A 297 11326 7781 8333 -769 -448 -791 C ATOM 2975 OE1 GLN A 297 -27.228 -31.159 5.023 1.00 75.09 O ANISOU 2975 OE1 GLN A 297 11643 8102 8786 -850 -492 -726 O ATOM 2976 NE2 GLN A 297 -25.781 -31.252 3.307 1.00 78.72 N ANISOU 2976 NE2 GLN A 297 12300 8497 9112 -665 -385 -882 N ATOM 2977 N THR A 298 -30.063 -26.395 5.796 1.00 40.64 N ANISOU 2977 N THR A 298 6640 4393 4408 -1018 -600 -492 N ATOM 2978 CA THR A 298 -31.325 -25.945 6.372 1.00 40.07 C ANISOU 2978 CA THR A 298 6417 4417 4391 -1130 -670 -431 C ATOM 2979 C THR A 298 -31.783 -24.644 5.727 1.00 46.69 C ANISOU 2979 C THR A 298 7171 5393 5174 -1113 -707 -429 C ATOM 2980 O THR A 298 -32.984 -24.433 5.530 1.00 47.28 O ANISOU 2980 O THR A 298 7174 5526 5262 -1212 -808 -424 O ATOM 2981 CB THR A 298 -31.187 -25.773 7.885 1.00 36.00 C ANISOU 2981 CB THR A 298 5774 3939 3967 -1122 -602 -336 C ATOM 2982 OG1 THR A 298 -30.619 -26.959 8.453 1.00 33.23 O ANISOU 2982 OG1 THR A 298 5519 3450 3658 -1120 -568 -332 O ATOM 2983 CG2 THR A 298 -32.549 -25.526 8.514 1.00 32.31 C ANISOU 2983 CG2 THR A 298 5161 3554 3562 -1249 -663 -280 C ATOM 2984 N PHE A 299 -30.837 -23.762 5.392 1.00 54.84 N ANISOU 2984 N PHE A 299 8209 6478 6149 -987 -629 -432 N ATOM 2985 CA PHE A 299 -31.187 -22.522 4.706 1.00 52.46 C ANISOU 2985 CA PHE A 299 7853 6292 5786 -964 -664 -429 C ATOM 2986 C PHE A 299 -31.852 -22.805 3.364 1.00 51.25 C ANISOU 2986 C PHE A 299 7817 6112 5544 -1025 -779 -502 C ATOM 2987 O PHE A 299 -32.861 -22.181 3.020 1.00 50.85 O ANISOU 2987 O PHE A 299 7694 6144 5484 -1080 -879 -490 O ATOM 2988 CB PHE A 299 -29.941 -21.654 4.514 1.00 48.75 C ANISOU 2988 CB PHE A 299 7395 5861 5267 -827 -552 -422 C ATOM 2989 CG PHE A 299 -29.439 -21.003 5.779 1.00 44.09 C ANISOU 2989 CG PHE A 299 6664 5331 4757 -770 -466 -344 C ATOM 2990 CD1 PHE A 299 -30.210 -20.994 6.931 1.00 44.40 C ANISOU 2990 CD1 PHE A 299 6572 5411 4887 -836 -490 -282 C ATOM 2991 CD2 PHE A 299 -28.199 -20.382 5.806 1.00 41.67 C ANISOU 2991 CD2 PHE A 299 6359 5045 4431 -655 -358 -335 C ATOM 2992 CE1 PHE A 299 -29.747 -20.385 8.092 1.00 36.78 C ANISOU 2992 CE1 PHE A 299 5494 4500 3981 -784 -414 -216 C ATOM 2993 CE2 PHE A 299 -27.733 -19.771 6.962 1.00 35.65 C ANISOU 2993 CE2 PHE A 299 5472 4335 3738 -607 -292 -268 C ATOM 2994 CZ PHE A 299 -28.509 -19.777 8.105 1.00 33.60 C ANISOU 2994 CZ PHE A 299 5098 4111 3557 -670 -323 -211 C ATOM 2995 N ARG A 300 -31.309 -23.757 2.599 1.00 54.68 N ANISOU 2995 N ARG A 300 8435 6429 5913 -1013 -771 -582 N ATOM 2996 CA ARG A 300 -31.884 -24.081 1.295 1.00 56.99 C ANISOU 2996 CA ARG A 300 8863 6686 6104 -1072 -883 -661 C ATOM 2997 C ARG A 300 -33.297 -24.634 1.428 1.00 50.05 C ANISOU 2997 C ARG A 300 7933 5798 5287 -1225 -1030 -661 C ATOM 2998 O ARG A 300 -34.193 -24.260 0.662 1.00 43.53 O ANISOU 2998 O ARG A 300 7103 5025 4412 -1285 -1156 -680 O ATOM 2999 CB ARG A 300 -30.989 -25.077 0.558 1.00 67.56 C ANISOU 2999 CB ARG A 300 10415 7890 7366 -1026 -831 -753 C ATOM 3000 CG ARG A 300 -29.697 -24.476 0.032 1.00 75.28 C ANISOU 3000 CG ARG A 300 11459 8886 8256 -883 -699 -772 C ATOM 3001 CD ARG A 300 -29.003 -25.424 -0.931 1.00 82.79 C ANISOU 3001 CD ARG A 300 12633 9712 9113 -844 -661 -881 C ATOM 3002 NE ARG A 300 -28.360 -26.539 -0.241 1.00 88.89 N ANISOU 3002 NE ARG A 300 13441 10360 9971 -816 -592 -898 N ATOM 3003 CZ ARG A 300 -27.050 -26.636 -0.039 1.00 86.54 C ANISOU 3003 CZ ARG A 300 13166 10028 9689 -689 -445 -907 C ATOM 3004 NH1 ARG A 300 -26.235 -25.685 -0.483 1.00 84.46 N ANISOU 3004 NH1 ARG A 300 12886 9844 9358 -589 -343 -902 N ATOM 3005 NH2 ARG A 300 -26.553 -27.689 0.600 1.00 85.80 N ANISOU 3005 NH2 ARG A 300 13107 9814 9679 -664 -404 -919 N ATOM 3006 N LYS A 301 -33.518 -25.528 2.394 1.00 49.86 N ANISOU 3006 N LYS A 301 7867 5707 5371 -1295 -1020 -635 N ATOM 3007 CA LYS A 301 -34.844 -26.110 2.565 1.00 49.70 C ANISOU 3007 CA LYS A 301 7789 5674 5420 -1454 -1149 -632 C ATOM 3008 C LYS A 301 -35.863 -25.071 3.014 1.00 46.67 C ANISOU 3008 C LYS A 301 7190 5444 5100 -1496 -1203 -562 C ATOM 3009 O LYS A 301 -37.054 -25.208 2.716 1.00 49.23 O ANISOU 3009 O LYS A 301 7458 5794 5455 -1615 -1336 -573 O ATOM 3010 CB LYS A 301 -34.787 -27.268 3.561 1.00 55.38 C ANISOU 3010 CB LYS A 301 8519 6284 6240 -1519 -1109 -609 C ATOM 3011 CG LYS A 301 -33.928 -28.430 3.092 1.00 62.42 C ANISOU 3011 CG LYS A 301 9629 7005 7083 -1486 -1077 -687 C ATOM 3012 CD LYS A 301 -33.902 -29.552 4.111 1.00 69.79 C ANISOU 3012 CD LYS A 301 10577 7822 8119 -1549 -1047 -654 C ATOM 3013 CE LYS A 301 -33.088 -30.732 3.602 1.00 76.57 C ANISOU 3013 CE LYS A 301 11661 8497 8935 -1510 -1025 -738 C ATOM 3014 NZ LYS A 301 -33.048 -31.845 4.593 1.00 81.37 N ANISOU 3014 NZ LYS A 301 12298 8976 9643 -1569 -1003 -699 N ATOM 3015 N ILE A 302 -35.425 -24.031 3.724 1.00 45.81 N ANISOU 3015 N ILE A 302 6955 5435 5018 -1401 -1104 -492 N ATOM 3016 CA ILE A 302 -36.352 -22.982 4.135 1.00 47.48 C ANISOU 3016 CA ILE A 302 6965 5788 5288 -1423 -1147 -432 C ATOM 3017 C ILE A 302 -36.692 -22.081 2.957 1.00 53.90 C ANISOU 3017 C ILE A 302 7798 6672 6011 -1389 -1243 -461 C ATOM 3018 O ILE A 302 -37.843 -21.658 2.790 1.00 55.08 O ANISOU 3018 O ILE A 302 7831 6899 6199 -1455 -1359 -448 O ATOM 3019 CB ILE A 302 -35.767 -22.177 5.307 1.00 41.47 C ANISOU 3019 CB ILE A 302 6077 5099 4580 -1332 -1013 -354 C ATOM 3020 CG1 ILE A 302 -35.622 -23.059 6.544 1.00 43.22 C ANISOU 3020 CG1 ILE A 302 6272 5259 4892 -1381 -939 -313 C ATOM 3021 CG2 ILE A 302 -36.647 -20.981 5.615 1.00 35.95 C ANISOU 3021 CG2 ILE A 302 5187 4543 3930 -1332 -1050 -302 C ATOM 3022 CD1 ILE A 302 -34.804 -22.425 7.640 1.00 42.23 C ANISOU 3022 CD1 ILE A 302 6069 5179 4796 -1283 -807 -248 C ATOM 3023 N ILE A 303 -35.700 -21.775 2.123 1.00 59.18 N ANISOU 3023 N ILE A 303 8614 7314 6559 -1286 -1196 -498 N ATOM 3024 CA ILE A 303 -35.921 -20.862 1.008 1.00 65.41 C ANISOU 3024 CA ILE A 303 9443 8165 7244 -1247 -1278 -516 C ATOM 3025 C ILE A 303 -36.730 -21.542 -0.092 1.00 66.18 C ANISOU 3025 C ILE A 303 9653 8213 7278 -1346 -1443 -589 C ATOM 3026 O ILE A 303 -37.650 -20.943 -0.664 1.00 64.53 O ANISOU 3026 O ILE A 303 9391 8077 7052 -1379 -1580 -585 O ATOM 3027 CB ILE A 303 -34.569 -20.331 0.499 1.00 63.36 C ANISOU 3027 CB ILE A 303 9307 7893 6873 -1114 -1158 -528 C ATOM 3028 CG1 ILE A 303 -33.879 -19.535 1.613 1.00 64.27 C ANISOU 3028 CG1 ILE A 303 9289 8068 7061 -1026 -1018 -453 C ATOM 3029 CG2 ILE A 303 -34.761 -19.463 -0.725 1.00 62.14 C ANISOU 3029 CG2 ILE A 303 9229 7790 6593 -1080 -1240 -545 C ATOM 3030 CD1 ILE A 303 -32.381 -19.415 1.460 1.00 65.70 C ANISOU 3030 CD1 ILE A 303 9574 8210 7178 -913 -871 -466 C ATOM 3031 N ARG A 304 -36.418 -22.808 -0.391 1.00 70.08 N ANISOU 3031 N ARG A 304 10306 8579 7741 -1395 -1442 -658 N ATOM 3032 CA ARG A 304 -37.178 -23.544 -1.398 1.00 77.09 C ANISOU 3032 CA ARG A 304 11288 9413 8590 -1475 -1578 -723 C ATOM 3033 C ARG A 304 -38.637 -23.709 -0.987 1.00 86.29 C ANISOU 3033 C ARG A 304 12267 10630 9891 -1592 -1696 -690 C ATOM 3034 O ARG A 304 -39.545 -23.507 -1.802 1.00 94.75 O ANISOU 3034 O ARG A 304 13303 11745 10953 -1612 -1816 -702 O ATOM 3035 CB ARG A 304 -36.538 -24.911 -1.649 1.00 77.45 C ANISOU 3035 CB ARG A 304 11519 9304 8604 -1489 -1528 -797 C ATOM 3036 CG ARG A 304 -35.179 -24.854 -2.327 1.00 79.08 C ANISOU 3036 CG ARG A 304 11916 9457 8673 -1365 -1412 -847 C ATOM 3037 CD ARG A 304 -34.545 -26.236 -2.402 1.00 83.61 C ANISOU 3037 CD ARG A 304 12654 9874 9241 -1369 -1354 -918 C ATOM 3038 NE ARG A 304 -33.190 -26.182 -2.947 1.00 88.25 N ANISOU 3038 NE ARG A 304 13400 10416 9716 -1240 -1220 -966 N ATOM 3039 CZ ARG A 304 -32.359 -27.218 -2.990 1.00 93.08 C ANISOU 3039 CZ ARG A 304 14153 10896 10318 -1201 -1134 -1028 C ATOM 3040 NH1 ARG A 304 -31.144 -27.074 -3.504 1.00 94.71 N ANISOU 3040 NH1 ARG A 304 14477 11078 10431 -1074 -1001 -1069 N ATOM 3041 NH2 ARG A 304 -32.740 -28.397 -2.518 1.00 95.18 N ANISOU 3041 NH2 ARG A 304 14437 11053 10674 -1285 -1177 -1045 N ATOM 3042 N SER A 305 -38.883 -24.075 0.265 1.00 87.93 N ANISOU 3042 N SER A 305 12350 10834 10225 -1669 -1660 -646 N ATOM 3043 CA SER A 305 -40.246 -24.257 0.746 1.00 90.49 C ANISOU 3043 CA SER A 305 12482 11212 10689 -1781 -1745 -610 C ATOM 3044 C SER A 305 -40.898 -22.914 1.064 1.00 91.05 C ANISOU 3044 C SER A 305 12344 11439 10813 -1746 -1776 -546 C ATOM 3045 O SER A 305 -40.922 -22.483 2.218 1.00 90.69 O ANISOU 3045 O SER A 305 12150 11456 10852 -1757 -1708 -483 O ATOM 3046 CB SER A 305 -40.262 -25.157 1.982 1.00 90.56 C ANISOU 3046 CB SER A 305 12439 11158 10812 -1877 -1675 -579 C ATOM 3047 OG SER A 305 -39.673 -26.416 1.702 1.00 91.72 O ANISOU 3047 OG SER A 305 12782 11148 10919 -1900 -1650 -637 O TER 3048 SER A 305 HETATM 3049 N1 9XT A1201 -24.351 8.628 11.401 1.00 26.40 N ANISOU 3049 N1 9XT A1201 3554 3634 2844 112 -91 381 N HETATM 3050 N3 9XT A1201 -23.309 5.957 17.608 1.00 32.29 N ANISOU 3050 N3 9XT A1201 3962 4551 3754 78 21 205 N HETATM 3051 C4 9XT A1201 -23.767 8.488 15.521 1.00 22.81 C ANISOU 3051 C4 9XT A1201 2892 3233 2541 123 -36 263 C HETATM 3052 C5 9XT A1201 -24.839 7.824 14.951 1.00 24.53 C ANISOU 3052 C5 9XT A1201 3096 3494 2732 144 -66 266 C HETATM 3053 C6 9XT A1201 -25.037 7.862 13.585 1.00 25.24 C ANISOU 3053 C6 9XT A1201 3247 3566 2778 142 -90 302 C HETATM 3054 C7 9XT A1201 -24.160 8.580 12.782 1.00 26.42 C ANISOU 3054 C7 9XT A1201 3477 3655 2907 116 -69 341 C HETATM 3055 C8 9XT A1201 -23.563 8.441 17.013 1.00 14.33 C ANISOU 3055 C8 9XT A1201 1766 2179 1501 125 -22 221 C HETATM 3056 C10 9XT A1201 -19.957 5.571 18.749 1.00 16.80 C ANISOU 3056 C10 9XT A1201 1971 2553 1857 -7 79 204 C HETATM 3057 C13 9XT A1201 -19.589 4.205 19.143 1.00 17.42 C ANISOU 3057 C13 9XT A1201 2015 2668 1936 -18 91 201 C HETATM 3058 C15 9XT A1201 -19.657 2.044 19.628 1.00 18.53 C ANISOU 3058 C15 9XT A1201 2125 2857 2061 -22 100 198 C HETATM 3059 C1 9XT A1201 -22.145 10.032 12.480 1.00 26.09 C ANISOU 3059 C1 9XT A1201 3522 3506 2886 50 3 387 C HETATM 3060 C11 9XT A1201 -19.338 7.772 18.482 1.00 16.96 C ANISOU 3060 C11 9XT A1201 2044 2484 1915 -21 66 214 C HETATM 3061 C12 9XT A1201 -21.511 7.226 17.909 1.00 25.87 C ANISOU 3061 C12 9XT A1201 3183 3662 2984 44 40 212 C HETATM 3062 C14 9XT A1201 -20.434 3.138 19.221 1.00 12.68 C ANISOU 3062 C14 9XT A1201 1407 2106 1306 -8 89 197 C HETATM 3063 C16 9XT A1201 -18.387 2.488 19.780 1.00 22.70 C ANISOU 3063 C16 9XT A1201 2636 3359 2630 -36 105 201 C HETATM 3064 C2 9XT A1201 -23.090 9.253 13.355 1.00 25.34 C ANISOU 3064 C2 9XT A1201 3346 3476 2807 90 -29 341 C HETATM 3065 C3 9XT A1201 -22.897 9.210 14.723 1.00 25.54 C ANISOU 3065 C3 9XT A1201 3305 3519 2880 93 -19 300 C HETATM 3066 C9 9XT A1201 -21.254 5.890 18.270 1.00 23.52 C ANISOU 3066 C9 9XT A1201 2846 3411 2680 26 59 205 C HETATM 3067 N2 9XT A1201 -22.817 7.264 17.479 1.00 27.23 N ANISOU 3067 N2 9XT A1201 3362 3852 3133 83 14 213 N HETATM 3068 N4 9XT A1201 -22.381 5.187 18.064 1.00 19.85 N ANISOU 3068 N4 9XT A1201 2369 2987 2187 46 48 202 N HETATM 3069 N5 9XT A1201 -19.049 6.534 18.833 1.00 15.04 N ANISOU 3069 N5 9XT A1201 1758 2286 1669 -29 79 208 N HETATM 3070 N6 9XT A1201 -20.532 8.120 18.035 1.00 13.98 N ANISOU 3070 N6 9XT A1201 1697 2106 1509 19 46 218 N HETATM 3071 N7 9XT A1201 -18.340 8.726 18.593 1.00 14.32 N ANISOU 3071 N7 9XT A1201 1721 2098 1623 -57 67 219 N HETATM 3072 O1 9XT A1201 -18.347 3.795 19.484 1.00 16.34 O ANISOU 3072 O1 9XT A1201 1848 2525 1834 -40 103 202 O HETATM 3073 C1 OLA A1202 -30.390 -0.064 33.631 1.00 50.64 C HETATM 3074 O1 OLA A1202 -30.994 0.956 33.232 1.00 50.63 O HETATM 3075 O2 OLA A1202 -29.150 -0.020 33.769 1.00 53.23 O HETATM 3076 C2 OLA A1202 -31.146 -1.328 33.953 1.00 47.63 C HETATM 3077 C3 OLA A1202 -30.295 -2.540 33.598 1.00 47.30 C HETATM 3078 C4 OLA A1202 -31.140 -3.812 33.553 1.00 49.64 C HETATM 3079 C5 OLA A1202 -32.509 -3.559 32.927 1.00 48.41 C HETATM 3080 C6 OLA A1202 -33.278 -4.863 32.748 1.00 48.76 C HETATM 3081 C7 OLA A1202 -33.388 -5.222 31.271 1.00 48.35 C HETATM 3082 C8 OLA A1202 -33.865 -6.657 31.081 1.00 49.44 C HETATM 3083 C9 OLA A1202 -33.297 -7.183 29.785 1.00 50.14 C HETATM 3084 C10 OLA A1202 -33.743 -8.477 29.250 1.00 48.24 C HETATM 3085 C11 OLA A1202 -34.122 -9.578 30.206 1.00 48.32 C HETATM 3086 C12 OLA A1202 -34.628 -10.766 29.401 1.00 47.28 C HETATM 3087 C13 OLA A1202 -33.460 -11.617 28.923 1.00 45.11 C HETATM 3088 C14 OLA A1202 -33.602 -11.924 27.440 1.00 42.96 C HETATM 3089 C15 OLA A1202 -32.937 -13.248 27.077 1.00 40.43 C HETATM 3090 C16 OLA A1202 -33.902 -14.412 27.261 1.00 36.13 C HETATM 3091 C17 OLA A1202 -33.190 -15.750 27.106 1.00 37.29 C HETATM 3092 C18 OLA A1202 -34.189 -16.882 26.886 1.00 36.43 C HETATM 3093 NA NA A1203 -23.925 -7.938 16.753 1.00 54.73 NA HETATM 3094 C1 CLR A1204 -38.261 11.164 22.341 1.00 35.68 C HETATM 3095 C2 CLR A1204 -37.847 12.606 22.594 1.00 34.07 C HETATM 3096 C3 CLR A1204 -38.113 12.983 24.047 1.00 33.16 C HETATM 3097 C4 CLR A1204 -37.257 12.109 24.950 1.00 33.58 C HETATM 3098 C5 CLR A1204 -37.506 10.654 24.639 1.00 31.73 C HETATM 3099 C6 CLR A1204 -37.729 9.824 25.667 1.00 31.83 C HETATM 3100 C7 CLR A1204 -38.127 8.380 25.498 1.00 30.94 C HETATM 3101 C8 CLR A1204 -37.688 7.831 24.153 1.00 29.64 C HETATM 3102 C9 CLR A1204 -38.084 8.797 23.047 1.00 32.73 C HETATM 3103 C10 CLR A1204 -37.469 10.187 23.205 1.00 32.11 C HETATM 3104 C11 CLR A1204 -37.798 8.189 21.670 1.00 30.99 C HETATM 3105 C12 CLR A1204 -38.548 6.871 21.477 1.00 32.89 C HETATM 3106 C13 CLR A1204 -38.153 5.883 22.567 1.00 31.52 C HETATM 3107 C14 CLR A1204 -38.424 6.521 23.913 1.00 32.93 C HETATM 3108 C15 CLR A1204 -38.207 5.390 24.906 1.00 30.05 C HETATM 3109 C16 CLR A1204 -38.799 4.192 24.164 1.00 28.69 C HETATM 3110 C17 CLR A1204 -38.980 4.604 22.697 1.00 33.57 C HETATM 3111 C18 CLR A1204 -36.676 5.524 22.464 1.00 29.27 C HETATM 3112 C19 CLR A1204 -36.009 10.175 22.777 1.00 31.32 C HETATM 3113 C20 CLR A1204 -38.679 3.426 21.763 1.00 35.14 C HETATM 3114 C21 CLR A1204 -39.036 3.674 20.302 1.00 36.25 C HETATM 3115 C22 CLR A1204 -39.432 2.208 22.290 1.00 40.18 C HETATM 3116 C23 CLR A1204 -39.444 1.006 21.352 1.00 44.83 C HETATM 3117 C24 CLR A1204 -39.958 -0.198 22.135 1.00 54.41 C HETATM 3118 C25 CLR A1204 -40.120 -1.435 21.266 1.00 62.44 C HETATM 3119 C26 CLR A1204 -40.447 -2.653 22.121 1.00 67.16 C HETATM 3120 C27 CLR A1204 -41.201 -1.212 20.218 1.00 66.44 C HETATM 3121 O1 CLR A1204 -37.760 14.351 24.268 1.00 33.21 O HETATM 3122 C1 CLR A1205 -8.148 10.991 13.678 1.00 30.40 C HETATM 3123 C2 CLR A1205 -8.210 12.513 13.654 1.00 29.39 C HETATM 3124 C3 CLR A1205 -6.839 13.101 13.353 1.00 33.04 C HETATM 3125 C4 CLR A1205 -6.410 12.639 11.968 1.00 35.04 C HETATM 3126 C5 CLR A1205 -6.439 11.130 11.918 1.00 32.33 C HETATM 3127 C6 CLR A1205 -5.351 10.474 11.486 1.00 33.00 C HETATM 3128 C7 CLR A1205 -5.279 8.973 11.350 1.00 34.10 C HETATM 3129 C8 CLR A1205 -6.668 8.353 11.337 1.00 31.75 C HETATM 3130 C9 CLR A1205 -7.504 8.924 12.476 1.00 30.00 C HETATM 3131 C10 CLR A1205 -7.705 10.427 12.336 1.00 29.85 C HETATM 3132 C11 CLR A1205 -8.849 8.204 12.596 1.00 27.89 C HETATM 3133 C12 CLR A1205 -8.679 6.690 12.743 1.00 31.56 C HETATM 3134 C13 CLR A1205 -7.895 6.145 11.559 1.00 36.69 C HETATM 3135 C14 CLR A1205 -6.554 6.849 11.531 1.00 34.73 C HETATM 3136 C15 CLR A1205 -5.729 6.070 10.515 1.00 34.33 C HETATM 3137 C16 CLR A1205 -6.186 4.630 10.747 1.00 37.01 C HETATM 3138 C17 CLR A1205 -7.452 4.684 11.611 1.00 36.69 C HETATM 3139 C18 CLR A1205 -8.659 6.406 10.262 1.00 33.97 C HETATM 3140 C19 CLR A1205 -8.748 10.718 11.264 1.00 27.27 C HETATM 3141 C20 CLR A1205 -8.451 3.618 11.161 1.00 32.62 C HETATM 3142 C21 CLR A1205 -9.638 3.458 12.104 1.00 32.96 C HETATM 3143 C22 CLR A1205 -7.704 2.297 11.008 1.00 34.00 C HETATM 3144 C23 CLR A1205 -8.578 1.060 11.179 1.00 30.54 C HETATM 3145 C24 CLR A1205 -7.679 -0.155 11.364 1.00 34.38 C HETATM 3146 C25 CLR A1205 -8.464 -1.458 11.449 1.00 33.80 C HETATM 3147 C26 CLR A1205 -9.523 -1.391 12.541 1.00 29.55 C HETATM 3148 C27 CLR A1205 -9.077 -1.809 10.100 1.00 41.96 C HETATM 3149 O1 CLR A1205 -6.909 14.530 13.378 1.00 35.87 O HETATM 3150 C1 CLR A1206 -3.051 8.526 21.464 1.00 31.89 C HETATM 3151 C2 CLR A1206 -2.873 10.035 21.360 1.00 31.39 C HETATM 3152 C3 CLR A1206 -1.831 10.384 20.309 1.00 30.91 C HETATM 3153 C4 CLR A1206 -2.313 9.890 18.949 1.00 26.80 C HETATM 3154 C5 CLR A1206 -2.631 8.416 19.030 1.00 26.57 C HETATM 3155 C6 CLR A1206 -2.120 7.607 18.084 1.00 25.68 C HETATM 3156 C7 CLR A1206 -2.255 6.103 18.095 1.00 23.82 C HETATM 3157 C8 CLR A1206 -3.456 5.678 18.925 1.00 28.17 C HETATM 3158 C9 CLR A1206 -3.437 6.389 20.277 1.00 27.24 C HETATM 3159 C10 CLR A1206 -3.517 7.911 20.151 1.00 25.06 C HETATM 3160 C11 CLR A1206 -4.517 5.851 21.218 1.00 26.28 C HETATM 3161 C12 CLR A1206 -4.495 4.324 21.348 1.00 32.81 C HETATM 3162 C13 CLR A1206 -4.592 3.676 19.972 1.00 41.20 C HETATM 3163 C14 CLR A1206 -3.416 4.174 19.157 1.00 33.98 C HETATM 3164 C15 CLR A1206 -3.396 3.268 17.933 1.00 32.26 C HETATM 3165 C16 CLR A1206 -3.852 1.915 18.485 1.00 32.73 C HETATM 3166 C17 CLR A1206 -4.407 2.163 19.891 1.00 36.97 C HETATM 3167 C18 CLR A1206 -5.909 4.046 19.287 1.00 35.51 C HETATM 3168 C19 CLR A1206 -4.951 8.354 19.879 1.00 20.36 C HETATM 3169 C20 CLR A1206 -5.644 1.306 20.161 1.00 34.57 C HETATM 3170 C21 CLR A1206 -5.995 1.225 21.644 1.00 29.43 C HETATM 3171 C22 CLR A1206 -5.435 -0.097 19.603 1.00 40.89 C HETATM 3172 C23 CLR A1206 -6.553 -1.037 20.038 1.00 43.13 C HETATM 3173 C24 CLR A1206 -5.989 -2.332 20.613 1.00 48.78 C HETATM 3174 C25 CLR A1206 -5.303 -3.171 19.540 1.00 50.64 C HETATM 3175 C26 CLR A1206 -4.527 -4.321 20.169 1.00 52.70 C HETATM 3176 C27 CLR A1206 -6.312 -3.695 18.527 1.00 49.58 C HETATM 3177 O1 CLR A1206 -1.663 11.803 20.282 1.00 34.15 O HETATM 3178 C1 OLA A1207 -20.373 -21.907 28.457 1.00 59.30 C HETATM 3179 O1 OLA A1207 -20.873 -21.381 27.441 1.00 61.75 O HETATM 3180 O2 OLA A1207 -20.503 -23.139 28.624 1.00 62.35 O HETATM 3181 C2 OLA A1207 -19.623 -21.069 29.465 1.00 54.91 C HETATM 3182 C3 OLA A1207 -20.294 -19.708 29.605 1.00 49.36 C HETATM 3183 C4 OLA A1207 -19.284 -18.572 29.514 1.00 44.70 C HETATM 3184 C5 OLA A1207 -19.889 -17.274 30.035 1.00 41.68 C HETATM 3185 C6 OLA A1207 -19.255 -16.059 29.370 1.00 39.14 C HETATM 3186 C7 OLA A1207 -20.301 -14.983 29.110 1.00 36.81 C HETATM 3187 C1 OLA A1208 -22.188 13.349 5.226 1.00 64.18 C HETATM 3188 O1 OLA A1208 -23.403 13.644 5.211 1.00 66.41 O HETATM 3189 O2 OLA A1208 -21.450 13.861 6.095 1.00 65.62 O HETATM 3190 C2 OLA A1208 -21.615 12.390 4.210 1.00 59.72 C HETATM 3191 C3 OLA A1208 -22.034 10.966 4.553 1.00 54.53 C HETATM 3192 C4 OLA A1208 -21.930 10.064 3.330 1.00 50.85 C HETATM 3193 C5 OLA A1208 -22.763 8.804 3.513 1.00 47.96 C HETATM 3194 C6 OLA A1208 -22.048 7.594 2.925 1.00 44.76 C HETATM 3195 C7 OLA A1208 -22.563 6.303 3.546 1.00 40.23 C HETATM 3196 C8 OLA A1208 -21.589 5.155 3.308 1.00 45.46 C HETATM 3197 C9 OLA A1208 -21.500 4.857 1.829 1.00 49.88 C HETATM 3198 C10 OLA A1208 -21.235 3.484 1.380 1.00 55.52 C HETATM 3199 C11 OLA A1208 -20.260 2.617 2.141 1.00 61.98 C HETATM 3200 C12 OLA A1208 -20.522 1.148 1.827 1.00 68.18 C HETATM 3201 C13 OLA A1208 -19.538 0.240 2.558 1.00 74.79 C HETATM 3202 C14 OLA A1208 -20.004 -0.065 3.978 1.00 71.06 C HETATM 3203 C15 OLA A1208 -18.876 -0.648 4.824 1.00 67.44 C HETATM 3204 C16 OLA A1208 -18.365 -1.956 4.231 1.00 66.04 C HETATM 3205 C1 OLA A1209 -28.382 -20.055 40.390 1.00 75.64 C HETATM 3206 O1 OLA A1209 -27.231 -20.540 40.469 1.00 76.48 O HETATM 3207 O2 OLA A1209 -29.345 -20.826 40.180 1.00 77.43 O HETATM 3208 C2 OLA A1209 -28.614 -18.568 40.560 1.00 72.48 C HETATM 3209 C3 OLA A1209 -27.283 -17.825 40.621 1.00 66.89 C HETATM 3210 C4 OLA A1209 -27.172 -16.751 39.545 1.00 60.61 C HETATM 3211 C5 OLA A1209 -25.720 -16.308 39.402 1.00 56.30 C HETATM 3212 C6 OLA A1209 -25.613 -14.896 38.842 1.00 54.34 C HETATM 3213 C7 OLA A1209 -24.177 -14.596 38.433 1.00 56.68 C HETATM 3214 C8 OLA A1209 -23.953 -13.101 38.230 1.00 59.07 C HETATM 3215 C9 OLA A1209 -24.422 -12.349 39.450 1.00 64.30 C HETATM 3216 C10 OLA A1209 -24.592 -10.890 39.400 1.00 67.17 C HETATM 3217 C11 OLA A1209 -23.555 -10.021 38.734 1.00 67.92 C HETATM 3218 C12 OLA A1209 -24.055 -8.581 38.720 1.00 68.28 C HETATM 3219 C13 OLA A1209 -23.414 -7.744 39.823 1.00 65.91 C HETATM 3220 C14 OLA A1209 -22.340 -6.824 39.251 1.00 62.02 C HETATM 3221 C15 OLA A1209 -22.952 -5.732 38.377 1.00 57.07 C HETATM 3222 C16 OLA A1209 -21.911 -5.095 37.461 1.00 53.05 C HETATM 3223 C17 OLA A1209 -22.500 -3.948 36.645 1.00 44.08 C HETATM 3224 C18 OLA A1209 -21.514 -3.465 35.589 1.00 36.16 C HETATM 3225 C1 OLA A1210 -8.060 14.968 8.427 1.00 61.72 C HETATM 3226 O1 OLA A1210 -7.985 16.005 7.732 1.00 64.91 O HETATM 3227 O2 OLA A1210 -8.411 15.063 9.624 1.00 61.37 O HETATM 3228 C2 OLA A1210 -7.733 13.623 7.823 1.00 58.58 C HETATM 3229 C3 OLA A1210 -8.973 13.077 7.127 1.00 53.68 C HETATM 3230 C4 OLA A1210 -9.187 11.603 7.451 1.00 49.18 C HETATM 3231 C5 OLA A1210 -8.131 10.735 6.779 1.00 47.42 C HETATM 3232 C6 OLA A1210 -8.761 9.483 6.180 1.00 46.05 C HETATM 3233 C7 OLA A1210 -8.137 8.220 6.765 1.00 47.60 C HETATM 3234 C8 OLA A1210 -8.310 7.041 5.814 1.00 51.87 C HETATM 3235 C9 OLA A1210 -9.611 6.333 6.107 1.00 54.22 C HETATM 3236 C10 OLA A1210 -10.192 5.419 5.111 1.00 57.71 C HETATM 3237 C11 OLA A1210 -10.692 5.984 3.801 1.00 62.19 C HETATM 3238 C12 OLA A1210 -10.921 4.874 2.782 1.00 65.31 C HETATM 3239 C13 OLA A1210 -11.894 3.825 3.304 1.00 66.56 C HETATM 3240 C14 OLA A1210 -12.112 2.730 2.265 1.00 68.26 C HETATM 3241 C15 OLA A1210 -10.909 1.799 2.158 1.00 69.32 C HETATM 3242 C16 OLA A1210 -10.881 0.787 3.299 1.00 67.72 C HETATM 3243 C17 OLA A1210 -9.594 -0.030 3.281 1.00 67.58 C HETATM 3244 C18 OLA A1210 -9.349 -0.653 1.910 1.00 67.46 C HETATM 3245 C1 OLA A1211 -36.172 -15.199 5.409 1.00 69.03 C HETATM 3246 O1 OLA A1211 -35.958 -14.089 5.943 1.00 68.75 O HETATM 3247 O2 OLA A1211 -36.397 -16.190 6.138 1.00 70.02 O HETATM 3248 C2 OLA A1211 -36.161 -15.337 3.905 1.00 66.58 C HETATM 3249 C3 OLA A1211 -35.012 -14.523 3.318 1.00 61.62 C HETATM 3250 C4 OLA A1211 -34.041 -15.423 2.563 1.00 58.08 C HETATM 3251 C5 OLA A1211 -33.010 -14.609 1.792 1.00 55.24 C HETATM 3252 C6 OLA A1211 -31.674 -14.586 2.520 1.00 46.39 C HETATM 3253 C7 OLA A1211 -31.442 -13.226 3.160 1.00 39.39 C HETATM 3254 C8 OLA A1211 -29.957 -13.003 3.401 1.00 37.95 C HETATM 3255 C9 OLA A1211 -29.756 -11.584 3.865 1.00 40.10 C HETATM 3256 C10 OLA A1211 -28.446 -10.940 3.702 1.00 44.36 C HETATM 3257 C1 OLA A1212 -15.478 13.065 1.071 1.00 75.84 C HETATM 3258 O1 OLA A1212 -14.373 13.655 1.055 1.00 76.85 O HETATM 3259 O2 OLA A1212 -16.527 13.741 1.164 1.00 75.59 O HETATM 3260 C2 OLA A1212 -15.547 11.558 0.986 1.00 73.18 C HETATM 3261 C3 OLA A1212 -16.918 11.092 1.463 1.00 69.65 C HETATM 3262 C4 OLA A1212 -17.551 10.129 0.467 1.00 66.32 C HETATM 3263 C5 OLA A1212 -16.746 8.837 0.388 1.00 62.25 C HETATM 3264 C6 OLA A1212 -17.263 7.818 1.394 1.00 56.98 C HETATM 3265 C1 OLA A1213 -42.489 0.055 10.089 1.00 56.88 C HETATM 3266 C2 OLA A1213 -43.203 0.914 9.051 1.00 58.18 C HETATM 3267 C3 OLA A1213 -42.402 2.166 8.704 1.00 56.92 C HETATM 3268 C4 OLA A1213 -43.229 3.049 7.796 1.00 57.67 C HETATM 3269 C5 OLA A1213 -42.730 4.371 7.390 1.00 56.36 C HETATM 3270 C6 OLA A1213 -41.837 5.156 8.324 1.00 55.09 C HETATM 3271 C7 OLA A1213 -41.847 6.633 7.942 1.00 57.49 C HETATM 3272 C8 OLA A1213 -41.058 7.461 8.950 1.00 57.29 C HETATM 3273 C9 OLA A1213 -41.450 8.932 8.884 1.00 60.03 C HETATM 3274 C1 OLA A1214 -43.970 -24.282 13.350 1.00 67.00 C HETATM 3275 O1 OLA A1214 -44.702 -25.013 12.648 1.00 68.29 O HETATM 3276 O2 OLA A1214 -43.183 -24.809 14.168 1.00 66.80 O HETATM 3277 C2 OLA A1214 -44.035 -22.783 13.209 1.00 63.95 C HETATM 3278 C3 OLA A1214 -43.330 -22.146 14.398 1.00 62.09 C HETATM 3279 C4 OLA A1214 -43.838 -20.729 14.619 1.00 63.01 C HETATM 3280 C5 OLA A1214 -43.130 -20.082 15.802 1.00 63.94 C HETATM 3281 C6 OLA A1214 -41.845 -19.385 15.368 1.00 63.60 C HETATM 3282 C7 OLA A1214 -40.734 -19.575 16.395 1.00 64.12 C HETATM 3283 C8 OLA A1214 -39.742 -18.419 16.334 1.00 62.14 C HETATM 3284 C9 OLA A1214 -38.838 -18.595 15.136 1.00 61.84 C HETATM 3285 C10 OLA A1214 -37.936 -17.506 14.736 1.00 61.03 C HETATM 3286 C11 OLA A1214 -38.503 -16.128 14.498 1.00 62.42 C HETATM 3287 C12 OLA A1214 -37.399 -15.086 14.621 1.00 61.87 C HETATM 3288 C13 OLA A1214 -37.854 -13.769 14.007 1.00 63.51 C HETATM 3289 C14 OLA A1214 -38.059 -12.674 15.046 1.00 62.62 C HETATM 3290 C15 OLA A1214 -38.696 -11.449 14.395 1.00 61.73 C HETATM 3291 C16 OLA A1214 -38.507 -10.193 15.239 1.00 58.88 C HETATM 3292 C17 OLA A1214 -39.297 -9.026 14.656 1.00 58.19 C HETATM 3293 C1 OLA A1215 -28.286 -20.470 35.598 1.00 71.57 C HETATM 3294 O1 OLA A1215 -27.255 -20.000 35.065 1.00 69.51 O HETATM 3295 O2 OLA A1215 -28.757 -21.544 35.157 1.00 71.81 O HETATM 3296 C2 OLA A1215 -28.940 -19.764 36.768 1.00 73.18 C HETATM 3297 C3 OLA A1215 -30.235 -19.070 36.355 1.00 74.12 C HETATM 3298 C4 OLA A1215 -30.404 -17.753 37.106 1.00 73.84 C HETATM 3299 C5 OLA A1215 -30.360 -16.560 36.159 1.00 71.51 C HETATM 3300 C6 OLA A1215 -31.757 -16.001 35.910 1.00 70.64 C HETATM 3301 C7 OLA A1215 -31.747 -14.494 35.661 1.00 69.41 C HETATM 3302 C8 OLA A1215 -30.689 -13.753 36.478 1.00 67.17 C HETATM 3303 C9 OLA A1215 -30.660 -12.302 36.047 1.00 64.29 C HETATM 3304 C10 OLA A1215 -29.442 -11.476 36.152 1.00 62.31 C HETATM 3305 C11 OLA A1215 -28.583 -11.493 37.396 1.00 55.64 C HETATM 3306 C12 OLA A1215 -27.398 -10.546 37.229 1.00 49.69 C HETATM 3307 C3 OLA A1216 -17.533 -15.867 3.346 1.00 59.84 C HETATM 3308 C4 OLA A1216 -18.415 -14.715 2.881 1.00 59.81 C HETATM 3309 C5 OLA A1216 -18.358 -13.546 3.858 1.00 60.02 C HETATM 3310 C6 OLA A1216 -17.329 -12.512 3.418 1.00 61.38 C HETATM 3311 C7 OLA A1216 -17.961 -11.128 3.323 1.00 61.90 C HETATM 3312 C8 OLA A1216 -17.593 -10.239 4.508 1.00 60.35 C HETATM 3313 C9 OLA A1216 -16.293 -9.522 4.229 1.00 59.61 C HETATM 3314 C10 OLA A1216 -15.913 -8.350 5.033 1.00 57.50 C HETATM 3315 C11 OLA A1216 -16.969 -7.340 5.426 1.00 55.49 C HETATM 3316 C12 OLA A1216 -16.316 -6.095 6.019 1.00 54.19 C HETATM 3317 C6 OLA A1217 -21.009 -12.786 1.048 1.00 69.00 C HETATM 3318 C7 OLA A1217 -21.645 -11.477 0.593 1.00 66.33 C HETATM 3319 C8 OLA A1217 -21.228 -10.306 1.480 1.00 61.98 C HETATM 3320 C9 OLA A1217 -22.022 -10.290 2.767 1.00 56.79 C HETATM 3321 C10 OLA A1217 -22.417 -9.000 3.356 1.00 55.94 C HETATM 3322 C11 OLA A1217 -21.456 -7.834 3.363 1.00 54.90 C HETATM 3323 C12 OLA A1217 -22.165 -6.574 2.874 1.00 56.09 C HETATM 3324 C13 OLA A1217 -23.428 -6.286 3.678 1.00 59.06 C HETATM 3325 C14 OLA A1217 -23.813 -4.812 3.602 1.00 59.88 C HETATM 3326 C15 OLA A1217 -24.516 -4.485 2.291 1.00 61.95 C HETATM 3327 C16 OLA A1217 -24.733 -2.983 2.162 1.00 64.16 C HETATM 3328 C17 OLA A1217 -23.419 -2.287 1.830 1.00 66.26 C HETATM 3329 C18 OLA A1217 -23.599 -0.778 1.730 1.00 68.03 C HETATM 3330 C1 OLA A1218 -8.160 -18.560 12.867 1.00 51.63 C HETATM 3331 C2 OLA A1218 -9.258 -17.666 12.338 1.00 52.67 C HETATM 3332 C3 OLA A1218 -8.736 -16.242 12.170 1.00 55.04 C HETATM 3333 C4 OLA A1218 -9.677 -15.199 12.771 1.00 57.92 C HETATM 3334 C5 OLA A1218 -9.320 -13.793 12.292 1.00 62.98 C HETATM 3335 C6 OLA A1218 -10.226 -13.339 11.149 1.00 62.51 C HETATM 3336 C7 OLA A1218 -10.013 -11.871 10.784 1.00 61.96 C HETATM 3337 C8 OLA A1218 -9.693 -11.015 12.005 1.00 60.28 C HETATM 3338 C9 OLA A1218 -9.166 -9.674 11.555 1.00 59.55 C HETATM 3339 C10 OLA A1218 -8.515 -8.776 12.519 1.00 59.48 C HETATM 3340 C11 OLA A1218 -9.181 -8.448 13.833 1.00 53.76 C HETATM 3341 C12 OLA A1218 -8.275 -7.514 14.627 1.00 51.16 C HETATM 3342 C6 OLA A1219 -5.798 -16.626 15.591 1.00 61.27 C HETATM 3343 C7 OLA A1219 -6.921 -17.419 16.247 1.00 60.61 C HETATM 3344 C8 OLA A1219 -7.933 -16.498 16.920 1.00 59.61 C HETATM 3345 C9 OLA A1219 -8.306 -15.368 15.993 1.00 57.59 C HETATM 3346 C10 OLA A1219 -9.183 -14.282 16.461 1.00 56.44 C HETATM 3347 C11 OLA A1219 -10.455 -14.599 17.211 1.00 53.58 C HETATM 3348 C12 OLA A1219 -11.221 -13.311 17.491 1.00 52.15 C HETATM 3349 C13 OLA A1219 -10.442 -12.389 18.419 1.00 47.94 C HETATM 3350 C14 OLA A1219 -10.065 -11.082 17.734 1.00 43.12 C HETATM 3351 C15 OLA A1219 -9.112 -10.313 18.637 1.00 44.68 C HETATM 3352 C16 OLA A1219 -9.010 -8.849 18.239 1.00 44.42 C HETATM 3353 C17 OLA A1219 -8.277 -8.063 19.319 1.00 44.22 C HETATM 3354 C18 OLA A1219 -8.459 -6.568 19.098 1.00 45.77 C HETATM 3355 C9 OLC A1220 -3.799 -2.039 25.115 1.00 54.48 C HETATM 3356 C8 OLC A1220 -4.152 -0.701 24.509 1.00 53.69 C HETATM 3357 C24 OLC A1220 -1.566 12.618 26.786 1.00 53.95 C HETATM 3358 C7 OLC A1220 -3.698 0.429 25.427 1.00 50.01 C HETATM 3359 C6 OLC A1220 -3.954 1.782 24.773 1.00 48.12 C HETATM 3360 C5 OLC A1220 -3.449 2.933 25.638 1.00 44.54 C HETATM 3361 C4 OLC A1220 -3.617 4.273 24.928 1.00 42.06 C HETATM 3362 C3 OLC A1220 -3.148 5.426 25.809 1.00 38.98 C HETATM 3363 C2 OLC A1220 -3.132 6.755 25.056 1.00 39.04 C HETATM 3364 C21 OLC A1220 -1.980 10.192 26.437 1.00 48.65 C HETATM 3365 C1 OLC A1220 -2.617 7.836 25.978 1.00 42.81 C HETATM 3366 C22 OLC A1220 -2.279 11.593 25.917 1.00 57.13 C HETATM 3367 O19 OLC A1220 -2.288 7.567 27.118 1.00 49.99 O HETATM 3368 O25 OLC A1220 -1.760 13.908 26.199 1.00 51.95 O HETATM 3369 O23 OLC A1220 -1.820 11.731 24.567 1.00 71.75 O HETATM 3370 O20 OLC A1220 -2.503 9.216 25.538 1.00 45.10 O HETATM 3371 C10 OLC A1221 -6.535 -3.604 27.555 1.00 55.07 C HETATM 3372 C9 OLC A1221 -6.368 -2.741 28.552 1.00 56.65 C HETATM 3373 C8 OLC A1221 -5.164 -1.834 28.554 1.00 62.82 C HETATM 3374 C24 OLC A1221 -4.333 11.082 29.137 1.00 68.95 C HETATM 3375 C7 OLC A1221 -5.604 -0.411 28.874 1.00 67.26 C HETATM 3376 C6 OLC A1221 -4.405 0.519 29.030 1.00 63.82 C HETATM 3377 C5 OLC A1221 -4.866 1.879 29.533 1.00 59.44 C HETATM 3378 C4 OLC A1221 -3.729 2.890 29.623 1.00 59.29 C HETATM 3379 C3 OLC A1221 -4.270 4.196 30.191 1.00 57.72 C HETATM 3380 C2 OLC A1221 -3.266 5.340 30.123 1.00 61.30 C HETATM 3381 C21 OLC A1221 -4.154 9.078 30.624 1.00 67.53 C HETATM 3382 C1 OLC A1221 -4.017 6.619 30.411 1.00 65.24 C HETATM 3383 C22 OLC A1221 -3.442 10.331 30.125 1.00 70.74 C HETATM 3384 O19 OLC A1221 -5.214 6.582 30.643 1.00 70.00 O HETATM 3385 O25 OLC A1221 -5.618 11.362 29.710 1.00 67.00 O HETATM 3386 O23 OLC A1221 -3.133 11.177 31.237 1.00 78.86 O HETATM 3387 O20 OLC A1221 -3.355 7.914 30.411 1.00 65.66 O HETATM 3388 C10 OLC A1222 -41.608 4.614 13.712 1.00 44.05 C HETATM 3389 C9 OLC A1222 -41.094 5.687 13.112 1.00 46.20 C HETATM 3390 C11 OLC A1222 -43.069 4.566 14.090 1.00 41.40 C HETATM 3391 C8 OLC A1222 -41.957 6.886 12.795 1.00 51.81 C HETATM 3392 C12 OLC A1222 -43.734 3.318 13.516 1.00 40.02 C HETATM 3393 C7 OLC A1222 -41.079 8.113 12.566 1.00 50.46 C HETATM 3394 C15 OLC A1222 -43.732 -0.439 14.449 1.00 34.66 C HETATM 3395 C13 OLC A1222 -43.291 2.038 14.219 1.00 36.83 C HETATM 3396 C6 OLC A1222 -40.481 8.633 13.866 1.00 48.26 C HETATM 3397 C14 OLC A1222 -44.164 0.864 13.786 1.00 36.79 C HETATM 3398 C5 OLC A1222 -41.215 9.881 14.347 1.00 45.90 C HETATM 3399 C4 OLC A1222 -40.808 11.110 13.545 1.00 45.40 C HETATM 3400 C3 OLC A1222 -41.675 12.316 13.893 1.00 49.04 C HETATM 3401 C2 OLC A1222 -40.829 13.578 14.031 1.00 52.22 C HETATM 3402 C1 OLC A1222 -41.721 14.793 13.929 1.00 60.04 C HETATM 3403 O19 OLC A1222 -42.870 14.685 13.531 1.00 62.87 O HETATM 3404 O20 OLC A1222 -41.224 16.110 14.308 1.00 62.17 O HETATM 3405 C18 OLC A1223 -41.338 -4.654 15.446 1.00 68.85 C HETATM 3406 C10 OLC A1223 -37.721 4.112 15.067 1.00 43.38 C HETATM 3407 C9 OLC A1223 -37.625 5.344 15.559 1.00 35.73 C HETATM 3408 C17 OLC A1223 -41.270 -3.143 15.380 1.00 69.38 C HETATM 3409 C11 OLC A1223 -38.186 2.969 15.934 1.00 47.81 C HETATM 3410 C8 OLC A1223 -37.974 5.618 16.998 1.00 32.80 C HETATM 3411 C16 OLC A1223 -40.623 -2.562 16.633 1.00 68.16 C HETATM 3412 C12 OLC A1223 -39.026 1.999 15.112 1.00 52.46 C HETATM 3413 C7 OLC A1223 -37.195 6.835 17.478 1.00 31.16 C HETATM 3414 C15 OLC A1223 -40.800 -1.048 16.712 1.00 66.94 C HETATM 3415 C13 OLC A1223 -39.933 1.196 16.037 1.00 58.25 C HETATM 3416 C6 OLC A1223 -37.703 8.097 16.790 1.00 31.72 C HETATM 3417 C14 OLC A1223 -39.938 -0.293 15.704 1.00 64.49 C HETATM 3418 C5 OLC A1223 -37.544 9.312 17.696 1.00 30.27 C HETATM 3419 C4 OLC A1223 -38.045 10.565 16.988 1.00 35.56 C HETATM 3420 C3 OLC A1223 -38.176 11.745 17.945 1.00 36.18 C HETATM 3421 C2 OLC A1223 -38.638 12.994 17.204 1.00 39.86 C HETATM 3422 C1 OLC A1223 -39.061 14.039 18.206 1.00 41.37 C HETATM 3423 O19 OLC A1223 -39.159 13.752 19.381 1.00 49.32 O HETATM 3424 O20 OLC A1223 -39.354 15.396 17.788 1.00 41.09 O HETATM 3425 C10 OLC A1224 -33.747 -7.856 25.152 1.00 50.55 C HETATM 3426 C9 OLC A1224 -33.546 -9.169 25.234 1.00 48.67 C HETATM 3427 C17 OLC A1224 -37.438 -0.716 24.712 1.00 60.49 C HETATM 3428 C11 OLC A1224 -34.545 -7.269 24.014 1.00 54.68 C HETATM 3429 C8 OLC A1224 -34.095 -10.119 24.195 1.00 46.36 C HETATM 3430 C24 OLC A1224 -32.112 -23.013 25.369 1.00 70.16 C HETATM 3431 C16 OLC A1224 -36.443 -1.481 23.846 1.00 59.71 C HETATM 3432 C12 OLC A1224 -35.031 -5.871 24.382 1.00 57.68 C HETATM 3433 C7 OLC A1224 -33.046 -11.187 23.906 1.00 43.75 C HETATM 3434 C15 OLC A1224 -36.559 -2.985 24.069 1.00 60.38 C HETATM 3435 C13 OLC A1224 -35.825 -5.255 23.234 1.00 61.20 C HETATM 3436 C6 OLC A1224 -33.630 -12.404 23.199 1.00 36.94 C HETATM 3437 C14 OLC A1224 -35.622 -3.746 23.140 1.00 59.83 C HETATM 3438 C5 OLC A1224 -32.577 -13.503 23.106 1.00 34.89 C HETATM 3439 C4 OLC A1224 -33.191 -14.810 22.619 1.00 35.87 C HETATM 3440 C3 OLC A1224 -32.275 -15.994 22.912 1.00 37.30 C HETATM 3441 C2 OLC A1224 -33.033 -17.313 22.787 1.00 45.79 C HETATM 3442 C21 OLC A1224 -32.002 -20.739 24.308 1.00 60.18 C HETATM 3443 C1 OLC A1224 -32.174 -18.437 23.312 1.00 53.99 C HETATM 3444 C22 OLC A1224 -32.816 -22.028 24.438 1.00 65.56 C HETATM 3445 O19 OLC A1224 -31.006 -18.228 23.566 1.00 65.57 O HETATM 3446 O25 OLC A1224 -32.904 -24.200 25.526 1.00 72.06 O HETATM 3447 O23 OLC A1224 -34.114 -21.730 24.964 1.00 67.39 O HETATM 3448 O20 OLC A1224 -32.720 -19.767 23.541 1.00 56.69 O HETATM 3449 C10 OLC A1225 -35.599 -9.724 19.361 1.00 63.49 C HETATM 3450 C9 OLC A1225 -35.396 -10.945 18.871 1.00 61.69 C HETATM 3451 C11 OLC A1225 -36.967 -9.303 19.850 1.00 65.34 C HETATM 3452 C8 OLC A1225 -36.537 -11.930 18.786 1.00 61.07 C HETATM 3453 C24 OLC A1225 -34.709 -24.765 20.021 1.00 73.58 C HETATM 3454 C12 OLC A1225 -36.948 -9.151 21.370 1.00 65.77 C HETATM 3455 C7 OLC A1225 -36.045 -13.223 18.151 1.00 57.33 C HETATM 3456 C15 OLC A1225 -39.306 -6.185 22.112 1.00 64.35 C HETATM 3457 C13 OLC A1225 -38.192 -8.437 21.892 1.00 66.18 C HETATM 3458 C6 OLC A1225 -35.122 -13.950 19.121 1.00 53.73 C HETATM 3459 C14 OLC A1225 -38.275 -7.012 21.353 1.00 64.47 C HETATM 3460 C5 OLC A1225 -34.780 -15.346 18.622 1.00 52.84 C HETATM 3461 C4 OLC A1225 -36.026 -16.219 18.528 1.00 54.32 C HETATM 3462 C3 OLC A1225 -35.673 -17.635 18.084 1.00 57.48 C HETATM 3463 C2 OLC A1225 -35.569 -18.582 19.274 1.00 62.04 C HETATM 3464 C21 OLC A1225 -34.673 -22.359 19.314 1.00 70.86 C HETATM 3465 C1 OLC A1225 -35.065 -19.937 18.829 1.00 65.38 C HETATM 3466 C22 OLC A1225 -34.734 -23.318 20.498 1.00 74.54 C HETATM 3467 O19 OLC A1225 -34.700 -20.123 17.682 1.00 69.07 O HETATM 3468 O25 OLC A1225 -34.873 -25.640 21.145 1.00 72.34 O HETATM 3469 O23 OLC A1225 -33.602 -23.082 21.341 1.00 80.92 O HETATM 3470 O20 OLC A1225 -35.009 -21.047 19.766 1.00 67.68 O HETATM 3471 C18 OLC A1226 -26.404 -6.175 37.320 1.00 25.53 C HETATM 3472 C10 OLC A1226 -31.869 0.507 38.321 1.00 56.63 C HETATM 3473 C9 OLC A1226 -32.375 1.735 38.334 1.00 59.42 C HETATM 3474 C17 OLC A1226 -27.890 -5.951 37.482 1.00 31.50 C HETATM 3475 C11 OLC A1226 -30.429 0.264 37.955 1.00 54.11 C HETATM 3476 C8 OLC A1226 -31.541 2.939 37.970 1.00 54.80 C HETATM 3477 C16 OLC A1226 -28.311 -4.566 37.002 1.00 36.54 C HETATM 3478 C12 OLC A1226 -29.907 -0.849 38.853 1.00 55.02 C HETATM 3479 C7 OLC A1226 -32.435 3.907 37.205 1.00 51.75 C HETATM 3480 C15 OLC A1226 -29.753 -4.281 37.416 1.00 44.27 C HETATM 3481 C13 OLC A1226 -29.174 -1.915 38.043 1.00 55.12 C HETATM 3482 C6 OLC A1226 -31.814 5.291 37.052 1.00 50.17 C HETATM 3483 C14 OLC A1226 -30.126 -2.810 37.259 1.00 52.95 C HETATM 3484 C5 OLC A1226 -32.842 6.237 36.443 1.00 49.96 C HETATM 3485 C4 OLC A1226 -32.218 7.546 35.976 1.00 53.00 C HETATM 3486 C3 OLC A1226 -32.021 8.504 37.142 1.00 60.69 C HETATM 3487 C2 OLC A1226 -31.327 9.792 36.711 1.00 69.07 C HETATM 3488 C1 OLC A1226 -29.843 9.550 36.550 1.00 77.49 C HETATM 3489 O19 OLC A1226 -29.357 8.455 36.778 1.00 78.84 O HETATM 3490 O20 OLC A1226 -28.967 10.629 36.118 1.00 85.53 O HETATM 3491 C18 OLC A1227 -39.531 -3.881 11.952 1.00 62.01 C HETATM 3492 C10 OLC A1227 -37.226 5.229 10.864 1.00 46.50 C HETATM 3493 C9 OLC A1227 -37.298 6.555 10.832 1.00 43.54 C HETATM 3494 C17 OLC A1227 -39.970 -2.437 12.061 1.00 62.46 C HETATM 3495 C11 OLC A1227 -38.083 4.425 9.916 1.00 52.93 C HETATM 3496 C8 OLC A1227 -36.463 7.398 11.763 1.00 38.74 C HETATM 3497 C16 OLC A1227 -38.796 -1.495 11.828 1.00 62.23 C HETATM 3498 C12 OLC A1227 -37.717 2.954 10.028 1.00 57.48 C HETATM 3499 C7 OLC A1227 -36.733 8.865 11.455 1.00 41.29 C HETATM 3500 C15 OLC A1227 -39.227 -0.034 11.859 1.00 63.13 C HETATM 3501 C13 OLC A1227 -38.544 2.284 11.120 1.00 63.82 C HETATM 3502 C6 OLC A1227 -35.911 9.761 12.369 1.00 44.06 C HETATM 3503 C14 OLC A1227 -38.107 0.837 11.303 1.00 63.70 C HETATM 3504 C5 OLC A1227 -36.527 11.144 12.533 1.00 46.86 C HETATM 3505 C4 OLC A1227 -35.562 12.031 13.310 1.00 51.75 C HETATM 3506 C3 OLC A1227 -36.247 13.279 13.849 1.00 58.10 C HETATM 3507 C2 OLC A1227 -36.812 14.107 12.705 1.00 67.00 C HETATM 3508 C1 OLC A1227 -36.852 15.560 13.115 1.00 74.36 C HETATM 3509 O19 OLC A1227 -37.911 16.092 13.411 1.00 78.65 O HETATM 3510 O20 OLC A1227 -35.626 16.344 13.148 1.00 74.60 O HETATM 3511 C1 OLA A1228 -34.980 9.447 1.876 0.62 63.30 C HETATM 3512 O1 OLA A1228 -35.745 9.714 0.922 0.62 63.98 O HETATM 3513 O2 OLA A1228 -34.411 10.383 2.479 0.62 62.50 O HETATM 3514 C2 OLA A1228 -34.749 8.015 2.297 0.62 63.11 C HETATM 3515 C3 OLA A1228 -34.766 7.108 1.071 0.62 63.43 C HETATM 3516 C4 OLA A1228 -35.731 5.949 1.283 0.62 63.57 C HETATM 3517 C5 OLA A1228 -35.612 4.905 0.179 0.62 64.33 C HETATM 3518 C6 OLA A1228 -35.709 3.493 0.749 0.62 63.73 C HETATM 3519 C7 OLA A1228 -34.427 2.700 0.519 0.62 63.71 C HETATM 3520 C8 OLA A1228 -34.706 1.201 0.520 0.62 62.79 C HETATM 3521 C9 OLA A1228 -33.540 0.455 -0.086 0.62 63.35 C HETATM 3522 C10 OLA A1228 -33.713 -0.938 -0.523 0.62 63.23 C HETATM 3523 C11 OLA A1228 -34.523 -1.899 0.316 0.62 62.66 C HETATM 3524 C12 OLA A1228 -34.781 -3.181 -0.471 0.62 64.31 C HETATM 3525 C13 OLA A1228 -35.732 -4.107 0.282 0.62 63.60 C HETATM 3526 C14 OLA A1228 -35.498 -5.574 -0.067 0.62 63.68 C HETATM 3527 C15 OLA A1228 -35.320 -5.771 -1.568 0.62 64.75 C HETATM 3528 C16 OLA A1228 -35.483 -7.237 -1.953 0.62 65.83 C HETATM 3529 C17 OLA A1228 -34.688 -8.148 -1.026 0.62 64.33 C HETATM 3530 C18 OLA A1228 -34.715 -9.584 -1.536 0.62 64.51 C HETATM 3531 O HOH A1301 -16.679 0.752 12.900 1.00 26.13 O HETATM 3532 O HOH A1302 -18.021 -2.121 20.243 1.00 25.47 O HETATM 3533 O HOH A1303 -15.196 3.554 22.149 1.00 22.82 O HETATM 3534 O HOH A1304 -23.852 -4.601 14.296 1.00 16.45 O HETATM 3535 O HOH A1305 -15.310 10.214 18.397 1.00 22.00 O HETATM 3536 O HOH A1306 -22.624 -27.262 21.730 1.00 41.54 O HETATM 3537 O HOH A1307 -19.740 -1.292 23.055 1.00 34.64 O HETATM 3538 O HOH A1308 -16.484 -16.408 19.451 1.00 20.12 O HETATM 3539 O HOH A1309 -22.101 -5.966 15.544 1.00 27.40 O HETATM 3540 O HOH A1310 -28.361 6.023 17.950 1.00 23.89 O HETATM 3541 O HOH A1311 -11.491 12.271 15.966 1.00 42.00 O HETATM 3542 O HOH A1312 -19.138 -10.806 13.155 1.00 20.85 O HETATM 3543 O AHOH A1313 -25.753 -13.752 25.132 0.53 0.00 O HETATM 3544 O BHOH A1313 -26.161 -11.780 25.754 0.47 0.00 O HETATM 3545 O HOH A1314 -28.016 12.337 8.455 1.00 29.75 O HETATM 3546 O HOH A1315 -27.983 3.641 17.268 1.00 17.72 O HETATM 3547 O HOH A1316 -24.791 16.728 2.001 1.00 45.06 O HETATM 3548 O HOH A1317 -18.255 -17.144 17.029 1.00 38.83 O HETATM 3549 O HOH A1318 -28.894 3.036 19.943 1.00 18.11 O HETATM 3550 O HOH A1319 -15.006 12.453 28.852 1.00 21.14 O HETATM 3551 O HOH A1320 -26.220 -11.610 21.871 1.00 18.03 O HETATM 3552 O HOH A1321 -26.028 5.765 18.748 1.00 29.47 O HETATM 3553 O HOH A1322 -20.402 10.940 17.030 1.00 31.79 O HETATM 3554 O HOH A1323 -22.045 13.265 18.052 1.00 19.96 O HETATM 3555 O HOH A1324 -24.723 12.284 16.992 1.00 21.13 O HETATM 3556 O HOH A1325 -33.822 14.785 30.931 1.00 45.38 O HETATM 3557 O HOH A1326 -9.189 13.814 17.097 1.00 33.10 O HETATM 3558 O HOH A1327 -19.537 -28.201 8.116 1.00 46.32 O HETATM 3559 O HOH A1328 -25.573 3.417 16.209 1.00 35.72 O HETATM 3560 O HOH A1329 -23.374 13.135 14.767 1.00 37.80 O CONECT 411 3093 CONECT 547 1203 CONECT 563 1112 CONECT 583 1247 CONECT 696 3093 CONECT 1112 563 CONECT 1203 547 CONECT 1247 583 CONECT 2658 2679 CONECT 2679 2658 CONECT 3049 3054 CONECT 3050 3067 3068 CONECT 3051 3052 3055 3065 CONECT 3052 3051 3053 CONECT 3053 3052 3054 CONECT 3054 3049 3053 3064 CONECT 3055 3051 3067 CONECT 3056 3057 3066 3069 CONECT 3057 3056 3062 3072 CONECT 3058 3062 3063 CONECT 3059 3064 CONECT 3060 3069 3070 3071 CONECT 3061 3066 3067 3070 CONECT 3062 3057 3058 CONECT 3063 3058 3072 CONECT 3064 3054 3059 3065 CONECT 3065 3051 3064 CONECT 3066 3056 3061 3068 CONECT 3067 3050 3055 3061 CONECT 3068 3050 3066 CONECT 3069 3056 3060 CONECT 3070 3060 3061 CONECT 3071 3060 CONECT 3072 3057 3063 CONECT 3073 3074 3075 3076 CONECT 3074 3073 CONECT 3075 3073 CONECT 3076 3073 3077 CONECT 3077 3076 3078 CONECT 3078 3077 3079 CONECT 3079 3078 3080 CONECT 3080 3079 3081 CONECT 3081 3080 3082 CONECT 3082 3081 3083 CONECT 3083 3082 3084 CONECT 3084 3083 3085 CONECT 3085 3084 3086 CONECT 3086 3085 3087 CONECT 3087 3086 3088 CONECT 3088 3087 3089 CONECT 3089 3088 3090 CONECT 3090 3089 3091 CONECT 3091 3090 3092 CONECT 3092 3091 CONECT 3093 411 696 3539 CONECT 3094 3095 3103 CONECT 3095 3094 3096 CONECT 3096 3095 3097 3121 CONECT 3097 3096 3098 CONECT 3098 3097 3099 3103 CONECT 3099 3098 3100 CONECT 3100 3099 3101 CONECT 3101 3100 3102 3107 CONECT 3102 3101 3103 3104 CONECT 3103 3094 3098 3102 3112 CONECT 3104 3102 3105 CONECT 3105 3104 3106 CONECT 3106 3105 3107 3110 3111 CONECT 3107 3101 3106 3108 CONECT 3108 3107 3109 CONECT 3109 3108 3110 CONECT 3110 3106 3109 3113 CONECT 3111 3106 CONECT 3112 3103 CONECT 3113 3110 3114 3115 CONECT 3114 3113 CONECT 3115 3113 3116 CONECT 3116 3115 3117 CONECT 3117 3116 3118 CONECT 3118 3117 3119 3120 CONECT 3119 3118 CONECT 3120 3118 CONECT 3121 3096 CONECT 3122 3123 3131 CONECT 3123 3122 3124 CONECT 3124 3123 3125 3149 CONECT 3125 3124 3126 CONECT 3126 3125 3127 3131 CONECT 3127 3126 3128 CONECT 3128 3127 3129 CONECT 3129 3128 3130 3135 CONECT 3130 3129 3131 3132 CONECT 3131 3122 3126 3130 3140 CONECT 3132 3130 3133 CONECT 3133 3132 3134 CONECT 3134 3133 3135 3138 3139 CONECT 3135 3129 3134 3136 CONECT 3136 3135 3137 CONECT 3137 3136 3138 CONECT 3138 3134 3137 3141 CONECT 3139 3134 CONECT 3140 3131 CONECT 3141 3138 3142 3143 CONECT 3142 3141 CONECT 3143 3141 3144 CONECT 3144 3143 3145 CONECT 3145 3144 3146 CONECT 3146 3145 3147 3148 CONECT 3147 3146 CONECT 3148 3146 CONECT 3149 3124 CONECT 3150 3151 3159 CONECT 3151 3150 3152 CONECT 3152 3151 3153 3177 CONECT 3153 3152 3154 CONECT 3154 3153 3155 3159 CONECT 3155 3154 3156 CONECT 3156 3155 3157 CONECT 3157 3156 3158 3163 CONECT 3158 3157 3159 3160 CONECT 3159 3150 3154 3158 3168 CONECT 3160 3158 3161 CONECT 3161 3160 3162 CONECT 3162 3161 3163 3166 3167 CONECT 3163 3157 3162 3164 CONECT 3164 3163 3165 CONECT 3165 3164 3166 CONECT 3166 3162 3165 3169 CONECT 3167 3162 CONECT 3168 3159 CONECT 3169 3166 3170 3171 CONECT 3170 3169 CONECT 3171 3169 3172 CONECT 3172 3171 3173 CONECT 3173 3172 3174 CONECT 3174 3173 3175 3176 CONECT 3175 3174 CONECT 3176 3174 CONECT 3177 3152 CONECT 3178 3179 3180 3181 CONECT 3179 3178 CONECT 3180 3178 CONECT 3181 3178 3182 CONECT 3182 3181 3183 CONECT 3183 3182 3184 CONECT 3184 3183 3185 CONECT 3185 3184 3186 CONECT 3186 3185 CONECT 3187 3188 3189 3190 CONECT 3188 3187 CONECT 3189 3187 CONECT 3190 3187 3191 CONECT 3191 3190 3192 CONECT 3192 3191 3193 CONECT 3193 3192 3194 CONECT 3194 3193 3195 CONECT 3195 3194 3196 CONECT 3196 3195 3197 CONECT 3197 3196 3198 CONECT 3198 3197 3199 CONECT 3199 3198 3200 CONECT 3200 3199 3201 CONECT 3201 3200 3202 CONECT 3202 3201 3203 CONECT 3203 3202 3204 CONECT 3204 3203 CONECT 3205 3206 3207 3208 CONECT 3206 3205 CONECT 3207 3205 CONECT 3208 3205 3209 CONECT 3209 3208 3210 CONECT 3210 3209 3211 CONECT 3211 3210 3212 CONECT 3212 3211 3213 CONECT 3213 3212 3214 CONECT 3214 3213 3215 CONECT 3215 3214 3216 CONECT 3216 3215 3217 CONECT 3217 3216 3218 CONECT 3218 3217 3219 CONECT 3219 3218 3220 CONECT 3220 3219 3221 CONECT 3221 3220 3222 CONECT 3222 3221 3223 CONECT 3223 3222 3224 CONECT 3224 3223 CONECT 3225 3226 3227 3228 CONECT 3226 3225 CONECT 3227 3225 CONECT 3228 3225 3229 CONECT 3229 3228 3230 CONECT 3230 3229 3231 CONECT 3231 3230 3232 CONECT 3232 3231 3233 CONECT 3233 3232 3234 CONECT 3234 3233 3235 CONECT 3235 3234 3236 CONECT 3236 3235 3237 CONECT 3237 3236 3238 CONECT 3238 3237 3239 CONECT 3239 3238 3240 CONECT 3240 3239 3241 CONECT 3241 3240 3242 CONECT 3242 3241 3243 CONECT 3243 3242 3244 CONECT 3244 3243 CONECT 3245 3246 3247 3248 CONECT 3246 3245 CONECT 3247 3245 CONECT 3248 3245 3249 CONECT 3249 3248 3250 CONECT 3250 3249 3251 CONECT 3251 3250 3252 CONECT 3252 3251 3253 CONECT 3253 3252 3254 CONECT 3254 3253 3255 CONECT 3255 3254 3256 CONECT 3256 3255 CONECT 3257 3258 3259 3260 CONECT 3258 3257 CONECT 3259 3257 CONECT 3260 3257 3261 CONECT 3261 3260 3262 CONECT 3262 3261 3263 CONECT 3263 3262 3264 CONECT 3264 3263 CONECT 3265 3266 CONECT 3266 3265 3267 CONECT 3267 3266 3268 CONECT 3268 3267 3269 CONECT 3269 3268 3270 CONECT 3270 3269 3271 CONECT 3271 3270 3272 CONECT 3272 3271 3273 CONECT 3273 3272 CONECT 3274 3275 3276 3277 CONECT 3275 3274 CONECT 3276 3274 CONECT 3277 3274 3278 CONECT 3278 3277 3279 CONECT 3279 3278 3280 CONECT 3280 3279 3281 CONECT 3281 3280 3282 CONECT 3282 3281 3283 CONECT 3283 3282 3284 CONECT 3284 3283 3285 CONECT 3285 3284 3286 CONECT 3286 3285 3287 CONECT 3287 3286 3288 CONECT 3288 3287 3289 CONECT 3289 3288 3290 CONECT 3290 3289 3291 CONECT 3291 3290 3292 CONECT 3292 3291 CONECT 3293 3294 3295 3296 CONECT 3294 3293 CONECT 3295 3293 CONECT 3296 3293 3297 CONECT 3297 3296 3298 CONECT 3298 3297 3299 CONECT 3299 3298 3300 CONECT 3300 3299 3301 CONECT 3301 3300 3302 CONECT 3302 3301 3303 CONECT 3303 3302 3304 CONECT 3304 3303 3305 CONECT 3305 3304 3306 CONECT 3306 3305 CONECT 3307 3308 CONECT 3308 3307 3309 CONECT 3309 3308 3310 CONECT 3310 3309 3311 CONECT 3311 3310 3312 CONECT 3312 3311 3313 CONECT 3313 3312 3314 CONECT 3314 3313 3315 CONECT 3315 3314 3316 CONECT 3316 3315 CONECT 3317 3318 CONECT 3318 3317 3319 CONECT 3319 3318 3320 CONECT 3320 3319 3321 CONECT 3321 3320 3322 CONECT 3322 3321 3323 CONECT 3323 3322 3324 CONECT 3324 3323 3325 CONECT 3325 3324 3326 CONECT 3326 3325 3327 CONECT 3327 3326 3328 CONECT 3328 3327 3329 CONECT 3329 3328 CONECT 3330 3331 CONECT 3331 3330 3332 CONECT 3332 3331 3333 CONECT 3333 3332 3334 CONECT 3334 3333 3335 CONECT 3335 3334 3336 CONECT 3336 3335 3337 CONECT 3337 3336 3338 CONECT 3338 3337 3339 CONECT 3339 3338 3340 CONECT 3340 3339 3341 CONECT 3341 3340 CONECT 3342 3343 CONECT 3343 3342 3344 CONECT 3344 3343 3345 CONECT 3345 3344 3346 CONECT 3346 3345 3347 CONECT 3347 3346 3348 CONECT 3348 3347 3349 CONECT 3349 3348 3350 CONECT 3350 3349 3351 CONECT 3351 3350 3352 CONECT 3352 3351 3353 CONECT 3353 3352 3354 CONECT 3354 3353 CONECT 3355 3356 CONECT 3356 3355 3358 CONECT 3357 3366 3368 CONECT 3358 3356 3359 CONECT 3359 3358 3360 CONECT 3360 3359 3361 CONECT 3361 3360 3362 CONECT 3362 3361 3363 CONECT 3363 3362 3365 CONECT 3364 3366 3370 CONECT 3365 3363 3367 3370 CONECT 3366 3357 3364 3369 CONECT 3367 3365 CONECT 3368 3357 CONECT 3369 3366 CONECT 3370 3364 3365 CONECT 3371 3372 CONECT 3372 3371 3373 CONECT 3373 3372 3375 CONECT 3374 3383 3385 CONECT 3375 3373 3376 CONECT 3376 3375 3377 CONECT 3377 3376 3378 CONECT 3378 3377 3379 CONECT 3379 3378 3380 CONECT 3380 3379 3382 CONECT 3381 3383 3387 CONECT 3382 3380 3384 3387 CONECT 3383 3374 3381 3386 CONECT 3384 3382 CONECT 3385 3374 CONECT 3386 3383 CONECT 3387 3381 3382 CONECT 3388 3389 3390 CONECT 3389 3388 3391 CONECT 3390 3388 3392 CONECT 3391 3389 3393 CONECT 3392 3390 3395 CONECT 3393 3391 3396 CONECT 3394 3397 CONECT 3395 3392 3397 CONECT 3396 3393 3398 CONECT 3397 3394 3395 CONECT 3398 3396 3399 CONECT 3399 3398 3400 CONECT 3400 3399 3401 CONECT 3401 3400 3402 CONECT 3402 3401 3403 3404 CONECT 3403 3402 CONECT 3404 3402 CONECT 3405 3408 CONECT 3406 3407 3409 CONECT 3407 3406 3410 CONECT 3408 3405 3411 CONECT 3409 3406 3412 CONECT 3410 3407 3413 CONECT 3411 3408 3414 CONECT 3412 3409 3415 CONECT 3413 3410 3416 CONECT 3414 3411 3417 CONECT 3415 3412 3417 CONECT 3416 3413 3418 CONECT 3417 3414 3415 CONECT 3418 3416 3419 CONECT 3419 3418 3420 CONECT 3420 3419 3421 CONECT 3421 3420 3422 CONECT 3422 3421 3423 3424 CONECT 3423 3422 CONECT 3424 3422 CONECT 3425 3426 3428 CONECT 3426 3425 3429 CONECT 3427 3431 CONECT 3428 3425 3432 CONECT 3429 3426 3433 CONECT 3430 3444 3446 CONECT 3431 3427 3434 CONECT 3432 3428 3435 CONECT 3433 3429 3436 CONECT 3434 3431 3437 CONECT 3435 3432 3437 CONECT 3436 3433 3438 CONECT 3437 3434 3435 CONECT 3438 3436 3439 CONECT 3439 3438 3440 CONECT 3440 3439 3441 CONECT 3441 3440 3443 CONECT 3442 3444 3448 CONECT 3443 3441 3445 3448 CONECT 3444 3430 3442 3447 CONECT 3445 3443 CONECT 3446 3430 CONECT 3447 3444 CONECT 3448 3442 3443 CONECT 3449 3450 3451 CONECT 3450 3449 3452 CONECT 3451 3449 3454 CONECT 3452 3450 3455 CONECT 3453 3466 3468 CONECT 3454 3451 3457 CONECT 3455 3452 3458 CONECT 3456 3459 CONECT 3457 3454 3459 CONECT 3458 3455 3460 CONECT 3459 3456 3457 CONECT 3460 3458 3461 CONECT 3461 3460 3462 CONECT 3462 3461 3463 CONECT 3463 3462 3465 CONECT 3464 3466 3470 CONECT 3465 3463 3467 3470 CONECT 3466 3453 3464 3469 CONECT 3467 3465 CONECT 3468 3453 CONECT 3469 3466 CONECT 3470 3464 3465 CONECT 3471 3474 CONECT 3472 3473 3475 CONECT 3473 3472 3476 CONECT 3474 3471 3477 CONECT 3475 3472 3478 CONECT 3476 3473 3479 CONECT 3477 3474 3480 CONECT 3478 3475 3481 CONECT 3479 3476 3482 CONECT 3480 3477 3483 CONECT 3481 3478 3483 CONECT 3482 3479 3484 CONECT 3483 3480 3481 CONECT 3484 3482 3485 CONECT 3485 3484 3486 CONECT 3486 3485 3487 CONECT 3487 3486 3488 CONECT 3488 3487 3489 3490 CONECT 3489 3488 CONECT 3490 3488 CONECT 3491 3494 CONECT 3492 3493 3495 CONECT 3493 3492 3496 CONECT 3494 3491 3497 CONECT 3495 3492 3498 CONECT 3496 3493 3499 CONECT 3497 3494 3500 CONECT 3498 3495 3501 CONECT 3499 3496 3502 CONECT 3500 3497 3503 CONECT 3501 3498 3503 CONECT 3502 3499 3504 CONECT 3503 3500 3501 CONECT 3504 3502 3505 CONECT 3505 3504 3506 CONECT 3506 3505 3507 CONECT 3507 3506 3508 CONECT 3508 3507 3509 3510 CONECT 3509 3508 CONECT 3510 3508 CONECT 3511 3512 3513 3514 CONECT 3512 3511 CONECT 3513 3511 CONECT 3514 3511 3515 CONECT 3515 3514 3516 CONECT 3516 3515 3517 CONECT 3517 3516 3518 CONECT 3518 3517 3519 CONECT 3519 3518 3520 CONECT 3520 3519 3521 CONECT 3521 3520 3522 CONECT 3522 3521 3523 CONECT 3523 3522 3524 CONECT 3524 3523 3525 CONECT 3525 3524 3526 CONECT 3526 3525 3527 CONECT 3527 3526 3528 CONECT 3528 3527 3529 CONECT 3529 3528 3530 CONECT 3530 3529 CONECT 3539 3093 MASTER 479 0 28 19 2 0 43 6 3525 1 493 34 END