HEADER MEMBRANE PROTEIN 27-JUL-17 5OLG TITLE STRUCTURE OF THE A2A-STAR2-BRIL562-ZM241385 COMPLEX AT 1.86A 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 PROTEINS, KEYWDS 3 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 2 22-MAR-23 5OLG 1 REMARK REVDAT 1 17-JAN-18 5OLG 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. 1.87 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) : 1.87 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.31 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7 REMARK 3 NUMBER OF REFLECTIONS : 41376 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.191 REMARK 3 R VALUE (WORKING SET) : 0.189 REMARK 3 FREE R VALUE : 0.224 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 3894 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 1.9320 - 1.8650 1.00 3701 200 0.4834 0.5144 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.250 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.670 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 24.36 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.73 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 : 0.012 3703 REMARK 3 ANGLE : 1.447 4946 REMARK 3 CHIRALITY : 0.070 551 REMARK 3 PLANARITY : 0.006 590 REMARK 3 DIHEDRAL : 16.617 2276 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' REMARK 3 ORIGIN FOR THE GROUP (A): -22.1678 -7.0563 17.6583 REMARK 3 T TENSOR REMARK 3 T11: 0.1778 T22: 0.1859 REMARK 3 T33: 0.1615 T12: -0.0024 REMARK 3 T13: 0.0031 T23: 0.0064 REMARK 3 L TENSOR REMARK 3 L11: 0.6759 L22: 0.6691 REMARK 3 L33: 0.8208 L12: 0.0955 REMARK 3 L13: 0.1973 L23: 0.0123 REMARK 3 S TENSOR REMARK 3 S11: 0.0198 S12: -0.0048 S13: -0.0381 REMARK 3 S21: -0.0743 S22: -0.0088 S23: -0.0320 REMARK 3 S31: 0.0917 S32: -0.0559 S33: -0.0000 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' REMARK 3 ORIGIN FOR THE GROUP (A): 0.1168 -54.5611 19.9519 REMARK 3 T TENSOR REMARK 3 T11: 0.4054 T22: 0.3022 REMARK 3 T33: 0.6749 T12: 0.0712 REMARK 3 T13: -0.0124 T23: -0.0261 REMARK 3 L TENSOR REMARK 3 L11: 0.0770 L22: 0.1943 REMARK 3 L33: 0.2107 L12: -0.0034 REMARK 3 L13: -0.0721 L23: -0.0953 REMARK 3 S TENSOR REMARK 3 S11: 0.0456 S12: -0.2658 S13: 0.3529 REMARK 3 S21: -0.2942 S22: 0.0507 S23: -0.1541 REMARK 3 S31: 0.1564 S32: 0.1043 S33: 0.0007 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 5OLG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-JUL-17. REMARK 100 THE DEPOSITION ID IS D_1200005995. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 17-MAY-17 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 : 42870 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850 REMARK 200 RESOLUTION RANGE LOW (A) : 46.530 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6 REMARK 200 DATA REDUNDANCY : 6.200 REMARK 200 R MERGE (I) : 0.15700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.89 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 6.40 REMARK 200 R MERGE FOR SHELL (I) : 2.19700 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL 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: 0.060-0.080 MM LONG PLATE-SHAPED CRYSTALS REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 41.75 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11 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, 0.5 MM THEOPHYLLINE. ZM241385 WAS REMARK 280 SUBSEQUENTLY ADDED TO MOTHERLIQUOR FOR THE SOAKING EXPERIMENT AT REMARK 280 A FINAL CONCENTRATION OF 0.005 MM., LIPIDIC CUBIC PHASE, REMARK 280 TEMPERATURE 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 69.80000 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 69.80000 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 19.72500 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 89.69650 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 19.72500 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 89.69650 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 69.80000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 19.72500 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 89.69650 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 69.80000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 19.72500 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 89.69650 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: 12190 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21210 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 26.0 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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 CG ARG A 293 C14 OLA A 1221 1.84 REMARK 500 O2 OLA A 1221 O HOH A 1301 2.06 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LEU A 58 -53.67 -120.22 REMARK 500 TYR A1101 -54.01 -129.07 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 A 208 -10.14 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 1214 REMARK 610 OLA A 1218 REMARK 610 OLA A 1222 REMARK 610 OLC A 1228 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 A1231 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 52 OD1 REMARK 620 2 SER A 91 OG 123.1 REMARK 620 3 HOH A1349 O 99.2 119.1 REMARK 620 4 HOH A1375 O 79.1 65.4 85.0 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZMA A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1202 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR 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 OLA 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 1210 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1211 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1212 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1213 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1214 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1215 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1216 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1217 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1218 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1219 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1220 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1221 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1222 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SCN A 1223 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SCN A 1224 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SCN A 1225 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SCN A 1226 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1227 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1228 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1229 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CIT A 1230 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 1231 DBREF 5OLG A 2 208 UNP P29274 AA2AR_HUMAN 2 208 DBREF 5OLG A 1001 1105 UNP P0ABE7 C562_ECOLX 23 127 DBREF 5OLG A 219 317 UNP P29274 AA2AR_HUMAN 219 317 SEQADV 5OLG ALA A -9 UNP P29274 EXPRESSION TAG SEQADV 5OLG ASP A -8 UNP P29274 EXPRESSION TAG SEQADV 5OLG TYR A -7 UNP P29274 EXPRESSION TAG SEQADV 5OLG LYS A -6 UNP P29274 EXPRESSION TAG SEQADV 5OLG ASP A -5 UNP P29274 EXPRESSION TAG SEQADV 5OLG ASP A -4 UNP P29274 EXPRESSION TAG SEQADV 5OLG ASP A -3 UNP P29274 EXPRESSION TAG SEQADV 5OLG ASP A -2 UNP P29274 EXPRESSION TAG SEQADV 5OLG GLY A -1 UNP P29274 EXPRESSION TAG SEQADV 5OLG ALA A 0 UNP P29274 EXPRESSION TAG SEQADV 5OLG PRO A 1 UNP P29274 EXPRESSION TAG SEQADV 5OLG LEU A 54 UNP P29274 ALA 54 ENGINEERED MUTATION SEQADV 5OLG ALA A 88 UNP P29274 THR 88 ENGINEERED MUTATION SEQADV 5OLG ALA A 107 UNP P29274 ARG 107 ENGINEERED MUTATION SEQADV 5OLG ALA A 122 UNP P29274 LYS 122 ENGINEERED MUTATION SEQADV 5OLG ALA A 154 UNP P29274 ASN 154 ENGINEERED MUTATION SEQADV 5OLG ALA A 202 UNP P29274 LEU 202 ENGINEERED MUTATION SEQADV 5OLG TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 5OLG ILE A 1102 UNP P0ABE7 HIS 124 CONFLICT SEQADV 5OLG LEU A 1106 UNP P0ABE7 LINKER SEQADV 5OLG ALA A 235 UNP P29274 LEU 235 ENGINEERED MUTATION SEQADV 5OLG ALA A 239 UNP P29274 VAL 239 ENGINEERED MUTATION SEQADV 5OLG ALA A 277 UNP P29274 SER 277 ENGINEERED MUTATION SEQADV 5OLG ALA A 318 UNP P29274 EXPRESSION TAG SEQADV 5OLG HIS A 319 UNP P29274 EXPRESSION TAG SEQADV 5OLG HIS A 320 UNP P29274 EXPRESSION TAG SEQADV 5OLG HIS A 321 UNP P29274 EXPRESSION TAG SEQADV 5OLG HIS A 322 UNP P29274 EXPRESSION TAG SEQADV 5OLG HIS A 323 UNP P29274 EXPRESSION TAG SEQADV 5OLG HIS A 324 UNP P29274 EXPRESSION TAG SEQADV 5OLG HIS A 325 UNP P29274 EXPRESSION TAG SEQADV 5OLG HIS A 326 UNP P29274 EXPRESSION TAG SEQADV 5OLG HIS A 327 UNP P29274 EXPRESSION TAG SEQADV 5OLG 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 ZMA A1201 25 HET CLR A1202 28 HET CLR A1203 28 HET CLR A1204 28 HET CLR A1205 28 HET OLA A1206 20 HET OLA A1207 20 HET OLA A1208 20 HET OLA A1209 20 HET OLA A1210 20 HET OLA A1211 20 HET OLA A1212 20 HET OLA A1213 20 HET OLA A1214 11 HET OLA A1215 20 HET OLA A1216 20 HET OLA A1217 20 HET OLA A1218 15 HET OLA A1219 20 HET OLA A1220 20 HET OLA A1221 20 HET OLA A1222 6 HET SCN A1223 3 HET SCN A1224 3 HET SCN A1225 3 HET SCN A1226 3 HET OLC A1227 25 HET OLC A1228 9 HET OLC A1229 25 HET CIT A1230 13 HET NA A1231 1 HETNAM ZMA 4-{2-[(7-AMINO-2-FURAN-2-YL[1,2,4]TRIAZOLO[1,5-A][1,3, HETNAM 2 ZMA 5]TRIAZIN-5-YL)AMINO]ETHYL}PHENOL HETNAM CLR CHOLESTEROL HETNAM OLA OLEIC ACID HETNAM SCN THIOCYANATE ION HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM CIT CITRIC ACID HETNAM NA SODIUM ION HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 ZMA C16 H15 N7 O2 FORMUL 3 CLR 4(C27 H46 O) FORMUL 7 OLA 17(C18 H34 O2) FORMUL 24 SCN 4(C N S 1-) FORMUL 28 OLC 3(C21 H40 O4) FORMUL 31 CIT C6 H8 O7 FORMUL 32 NA NA 1+ FORMUL 33 HOH *88(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 ILE A 108 VAL A 116 1 9 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 PHE A 180 1 8 HELIX 12 AB3 VAL A 186 LYS A 1019 1 42 HELIX 13 AB4 ASN A 1022 GLN A 1041 1 20 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 2.05 SSBOND 2 CYS A 74 CYS A 146 1555 1555 2.01 SSBOND 3 CYS A 77 CYS A 166 1555 1555 2.04 SSBOND 4 CYS A 259 CYS A 262 1555 1555 2.03 LINK OD1 ASP A 52 NA NA A1231 1555 1555 2.42 LINK OG SER A 91 NA NA A1231 1555 1555 2.57 LINK NA NA A1231 O HOH A1349 1555 1555 2.75 LINK NA NA A1231 O HOH A1375 1555 1555 2.93 SITE 1 AC1 14 LEU A 85 PHE A 168 GLU A 169 MET A 177 SITE 2 AC1 14 TRP A 246 LEU A 249 HIS A 250 ASN A 253 SITE 3 AC1 14 MET A 270 ILE A 274 HOH A1322 HOH A1356 SITE 4 AC1 14 HOH A1357 HOH A1373 SITE 1 AC2 9 ALA A 72 ALA A 73 GLY A 76 ILE A 80 SITE 2 AC2 9 CLR A1204 OLA A1207 OLA A1209 OLA A1211 SITE 3 AC2 9 HOH A1313 SITE 1 AC3 6 LEU A 247 CYS A 262 SER A 263 OLA A1208 SITE 2 AC3 6 OLA A1218 OLA A1219 SITE 1 AC4 7 PHE A 255 PHE A 258 CLR A1202 OLA A1207 SITE 2 AC4 7 OLA A1208 OLA A1209 HOH A1354 SITE 1 AC5 4 TRP A 268 OLA A1215 OLA A1218 OLC A1229 SITE 1 AC6 6 THR A 65 PHE A 70 CYS A 71 OLA A1207 SITE 2 AC6 6 OLA A1208 OLA A1220 SITE 1 AC7 12 LEU A 58 PRO A 61 THR A 65 PHE A 70 SITE 2 AC7 12 CYS A 71 GLN A 163 ASP A 261 CLR A1202 SITE 3 AC7 12 CLR A1204 OLA A1206 OLA A1208 HOH A1313 SITE 1 AC8 9 PHE A 255 ASP A 261 CYS A 262 CLR A1203 SITE 2 AC8 9 CLR A1204 OLA A1206 OLA A1207 OLA A1219 SITE 3 AC8 9 HOH A1377 SITE 1 AC9 6 PHE A 258 CLR A1202 CLR A1204 OLA A1210 SITE 2 AC9 6 OLA A1216 HOH A1313 SITE 1 AD1 4 VAL A 31 TRP A 32 ALA A 50 OLA A1209 SITE 1 AD2 6 TYR A 43 LEU A 54 LEU A 58 TRP A 129 SITE 2 AD2 6 CLR A1202 OLC A1227 SITE 1 AD3 7 MET A 140 LEU A 141 TYR A 179 ALA A 184 SITE 2 AD3 7 OLA A1216 OLC A1227 HOH A1320 SITE 1 AD4 5 TRP A 29 TRP A 32 LEU A 194 LYS A 233 SITE 2 AD4 5 ALA A 236 SITE 1 AD5 6 VAL A 40 PHE A 44 PHE A 93 LEU A 96 SITE 2 AD5 6 ASP A 101 VAL A 116 SITE 1 AD6 8 GLY A 5 SER A 6 LEU A 267 TYR A 271 SITE 2 AD6 8 VAL A 275 CLR A1205 OLC A1229 HOH A1306 SITE 1 AD7 6 TYR A 179 VAL A 188 LEU A 191 OLA A1209 SITE 2 AD7 6 OLA A1212 OLC A1228 SITE 1 AD8 4 SER A 7 LEU A 14 OLA A1220 HOH A1305 SITE 1 AD9 3 PRO A 266 CLR A1203 CLR A1205 SITE 1 AE1 3 CLR A1203 OLA A1208 OLA A1220 SITE 1 AE2 6 ILE A 10 LEU A 14 OLA A1206 OLA A1217 SITE 2 AE2 6 OLA A1219 HOH A1305 SITE 1 AE3 10 VAL A 45 ILE A 98 HIS A 230 ALA A 231 SITE 2 AE3 10 ALA A 235 TYR A 288 ARG A 291 ILE A 292 SITE 3 AE3 10 ARG A 293 HOH A1301 SITE 1 AE4 3 MET A 4 LEU A 19 PHE A 286 SITE 1 AE5 7 MET A 174 ASN A 175 LYS A1083 HOH A1348 SITE 2 AE5 7 HOH A1365 HOH A1379 HOH A1384 SITE 1 AE6 4 THR A 256 PHE A 257 HOH A1348 HOH A1384 SITE 1 AE7 4 PRO A 1 PRO A 2 ILE A 3 ARG A 300 SITE 1 AE8 4 GLY A 142 TRP A 143 ASN A 144 ASN A 175 SITE 1 AE9 5 ILE A 125 TRP A 129 PHE A 133 OLA A1211 SITE 2 AE9 5 OLA A1212 SITE 1 AF1 1 OLA A1216 SITE 1 AF2 8 VAL A 12 ILE A 16 THR A 279 VAL A 282 SITE 2 AF2 8 VAL A 283 PHE A 286 CLR A1205 OLA A1215 SITE 1 AF3 3 THR A 119 GLY A 123 ILE A 127 SITE 1 AF4 4 ASP A 52 SER A 91 HOH A1349 HOH A1375 CRYST1 39.450 179.393 139.600 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 0.025349 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005574 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007163 0.00000 ATOM 1 N GLY A -1 -21.046 24.590 1.506 1.00 69.07 N ANISOU 1 N GLY A -1 9712 7826 8704 -90 -407 998 N ATOM 2 CA GLY A -1 -21.783 23.697 2.394 1.00 68.27 C ANISOU 2 CA GLY A -1 9535 7783 8621 -22 -406 908 C ATOM 3 C GLY A -1 -23.006 23.047 1.759 1.00 64.23 C ANISOU 3 C GLY A -1 9017 7327 8060 38 -442 907 C ATOM 4 O GLY A -1 -24.085 23.641 1.728 1.00 62.33 O ANISOU 4 O GLY A -1 8796 7042 7844 105 -513 913 O ATOM 5 N ALA A 0 -22.822 21.828 1.251 1.00 63.58 N ANISOU 5 N ALA A 0 8906 7343 7909 13 -393 898 N ATOM 6 CA ALA A 0 -23.877 21.121 0.533 1.00 60.72 C ANISOU 6 CA ALA A 0 8540 7040 7490 55 -423 900 C ATOM 7 C ALA A 0 -25.083 20.877 1.439 1.00 58.63 C ANISOU 7 C ALA A 0 8217 6786 7273 139 -467 831 C ATOM 8 O ALA A 0 -24.913 20.606 2.634 1.00 58.44 O ANISOU 8 O ALA A 0 8135 6769 7300 153 -440 763 O ATOM 9 CB ALA A 0 -23.357 19.784 0.009 1.00 58.71 C ANISOU 9 CB ALA A 0 8261 6885 7162 12 -357 886 C ATOM 10 N PRO A 1 -26.307 20.951 0.907 1.00 54.37 N ANISOU 10 N PRO A 1 7689 6253 6718 195 -532 846 N ATOM 11 CA PRO A 1 -27.509 20.686 1.735 1.00 49.74 C ANISOU 11 CA PRO A 1 7037 5687 6175 275 -570 781 C ATOM 12 C PRO A 1 -27.345 19.404 2.533 1.00 51.12 C ANISOU 12 C PRO A 1 7135 5943 6346 265 -512 706 C ATOM 13 O PRO A 1 -27.008 18.343 1.974 1.00 52.35 O ANISOU 13 O PRO A 1 7284 6169 6439 223 -471 707 O ATOM 14 CB PRO A 1 -28.641 20.558 0.704 1.00 46.70 C ANISOU 14 CB PRO A 1 6670 5330 5743 312 -635 817 C ATOM 15 CG PRO A 1 -28.148 21.305 -0.533 1.00 47.38 C ANISOU 15 CG PRO A 1 6850 5369 5782 269 -654 912 C ATOM 16 CD PRO A 1 -26.630 21.286 -0.499 1.00 49.91 C ANISOU 16 CD PRO A 1 7194 5680 6090 185 -576 927 C ATOM 17 N PRO A 2 -27.537 19.462 3.856 1.00 52.59 N ANISOU 17 N PRO A 2 7266 6120 6596 301 -505 640 N ATOM 18 CA PRO A 2 -27.329 18.248 4.666 1.00 46.12 C ANISOU 18 CA PRO A 2 6378 5374 5772 287 -450 575 C ATOM 19 C PRO A 2 -28.203 17.080 4.245 1.00 37.94 C ANISOU 19 C PRO A 2 5305 4422 4689 302 -458 558 C ATOM 20 O PRO A 2 -27.784 15.928 4.402 1.00 39.26 O ANISOU 20 O PRO A 2 5441 4650 4827 267 -407 529 O ATOM 21 CB PRO A 2 -27.646 18.715 6.096 1.00 51.52 C ANISOU 21 CB PRO A 2 7016 6028 6529 334 -457 513 C ATOM 22 CG PRO A 2 -27.394 20.188 6.085 1.00 54.76 C ANISOU 22 CG PRO A 2 7483 6337 6985 345 -492 546 C ATOM 23 CD PRO A 2 -27.760 20.660 4.696 1.00 53.13 C ANISOU 23 CD PRO A 2 7340 6105 6741 347 -540 623 C ATOM 24 N ILE A 3 -29.399 17.329 3.707 1.00 37.17 N ANISOU 24 N ILE A 3 5210 4328 4585 351 -523 575 N ATOM 25 CA ILE A 3 -30.262 16.230 3.282 1.00 44.07 C ANISOU 25 CA ILE A 3 6048 5282 5415 359 -536 559 C ATOM 26 C ILE A 3 -29.629 15.346 2.187 1.00 44.48 C ANISOU 26 C ILE A 3 6137 5378 5384 296 -503 589 C ATOM 27 O ILE A 3 -30.033 14.191 2.021 1.00 40.42 O ANISOU 27 O ILE A 3 5592 4932 4833 287 -495 562 O ATOM 28 CB ILE A 3 -31.622 16.781 2.803 1.00 46.20 C ANISOU 28 CB ILE A 3 6315 5545 5693 423 -620 580 C ATOM 29 CG1 ILE A 3 -32.709 15.713 2.914 1.00 48.82 C ANISOU 29 CG1 ILE A 3 6578 5961 6010 444 -636 538 C ATOM 30 CG2 ILE A 3 -31.513 17.223 1.362 1.00 53.31 C ANISOU 30 CG2 ILE A 3 7295 6422 6538 402 -657 658 C ATOM 31 CD1 ILE A 3 -33.978 16.063 2.158 1.00 55.78 C ANISOU 31 CD1 ILE A 3 7458 6852 6884 494 -720 567 C ATOM 32 N MET A 4 -28.651 15.847 1.427 1.00 39.25 N ANISOU 32 N MET A 4 5543 4679 4690 252 -483 644 N ATOM 33 CA MET A 4 -28.100 15.016 0.352 1.00 39.61 C ANISOU 33 CA MET A 4 5624 4773 4652 197 -449 669 C ATOM 34 C MET A 4 -27.214 13.904 0.905 1.00 40.12 C ANISOU 34 C MET A 4 5652 4882 4711 158 -371 620 C ATOM 35 O MET A 4 -27.427 12.722 0.601 1.00 37.05 O ANISOU 35 O MET A 4 5245 4554 4277 146 -356 593 O ATOM 36 CB MET A 4 -27.332 15.875 -0.650 1.00 31.65 C ANISOU 36 CB MET A 4 4697 3721 3607 158 -446 744 C ATOM 37 CG MET A 4 -28.252 16.802 -1.382 1.00 31.56 C ANISOU 37 CG MET A 4 4731 3672 3588 195 -529 800 C ATOM 38 SD MET A 4 -27.383 17.885 -2.501 1.00 42.10 S ANISOU 38 SD MET A 4 6167 4948 4880 145 -530 897 S ATOM 39 CE MET A 4 -26.772 16.753 -3.786 1.00 42.36 C ANISOU 39 CE MET A 4 6237 5066 4793 79 -476 916 C ATOM 40 N GLY A 5 -26.186 14.267 1.695 1.00 33.79 N ANISOU 40 N GLY A 5 4839 4046 3953 137 -324 608 N ATOM 41 CA GLY A 5 -25.379 13.255 2.354 1.00 28.16 C ANISOU 41 CA GLY A 5 4084 3372 3244 109 -257 561 C ATOM 42 C GLY A 5 -26.199 12.439 3.326 1.00 34.33 C ANISOU 42 C GLY A 5 4799 4191 4055 144 -267 498 C ATOM 43 O GLY A 5 -25.964 11.235 3.500 1.00 31.73 O ANISOU 43 O GLY A 5 4441 3910 3705 126 -230 462 O ATOM 44 N ASER A 6 -27.169 13.083 3.979 0.57 33.76 N ANISOU 44 N ASER A 6 4700 4095 4031 195 -317 483 N ATOM 45 N BSER A 6 -27.196 13.060 3.953 0.43 33.61 N ANISOU 45 N BSER A 6 4682 4078 4011 195 -317 483 N ATOM 46 CA ASER A 6 -28.095 12.364 4.838 0.57 31.61 C ANISOU 46 CA ASER A 6 4363 3865 3782 227 -328 428 C ATOM 47 CA BSER A 6 -28.071 12.312 4.841 0.43 31.61 C ANISOU 47 CA BSER A 6 4362 3867 3781 226 -326 427 C ATOM 48 C ASER A 6 -28.812 11.262 4.067 0.57 30.28 C ANISOU 48 C ASER A 6 4188 3757 3558 220 -344 424 C ATOM 49 C BSER A 6 -28.861 11.255 4.079 0.43 30.24 C ANISOU 49 C BSER A 6 4182 3754 3554 222 -345 423 C ATOM 50 O ASER A 6 -28.892 10.128 4.539 0.57 31.78 O ANISOU 50 O ASER A 6 4338 3993 3743 208 -318 383 O ATOM 51 O BSER A 6 -29.053 10.144 4.577 0.43 31.81 O ANISOU 51 O BSER A 6 4337 3999 3749 213 -324 381 O ATOM 52 CB ASER A 6 -29.104 13.339 5.453 0.57 33.25 C ANISOU 52 CB ASER A 6 4546 4041 4045 288 -382 418 C ATOM 53 CB BSER A 6 -29.003 13.269 5.578 0.43 33.46 C ANISOU 53 CB BSER A 6 4569 4070 4075 285 -374 413 C ATOM 54 OG ASER A 6 -29.937 12.663 6.377 0.57 33.64 O ANISOU 54 OG ASER A 6 4527 4138 4118 316 -384 364 O ATOM 55 OG BSER A 6 -28.289 13.900 6.617 0.43 34.04 O ANISOU 55 OG BSER A 6 4634 4100 4200 286 -348 392 O ATOM 56 N SER A 7 -29.312 11.572 2.862 1.00 27.59 N ANISOU 56 N SER A 7 3891 3416 3175 224 -388 469 N ATOM 57 CA SER A 7 -30.073 10.592 2.087 1.00 29.32 C ANISOU 57 CA SER A 7 4108 3692 3339 217 -413 464 C ATOM 58 C SER A 7 -29.238 9.360 1.771 1.00 26.15 C ANISOU 58 C SER A 7 3720 3327 2890 166 -355 445 C ATOM 59 O SER A 7 -29.736 8.229 1.866 1.00 27.37 O ANISOU 59 O SER A 7 3844 3528 3027 159 -356 409 O ATOM 60 CB SER A 7 -30.575 11.223 0.787 1.00 36.20 C ANISOU 60 CB SER A 7 5036 4553 4166 225 -471 520 C ATOM 61 OG SER A 7 -31.543 12.205 1.092 1.00 43.77 O ANISOU 61 OG SER A 7 5973 5483 5173 282 -534 531 O ATOM 62 N VAL A 8 -27.966 9.565 1.414 1.00 23.16 N ANISOU 62 N VAL A 8 3384 2926 2490 132 -305 468 N ATOM 63 CA VAL A 8 -27.069 8.453 1.094 1.00 23.48 C ANISOU 63 CA VAL A 8 3436 2999 2487 90 -245 448 C ATOM 64 C VAL A 8 -26.879 7.576 2.324 1.00 27.70 C ANISOU 64 C VAL A 8 3911 3550 3066 91 -210 392 C ATOM 65 O VAL A 8 -27.082 6.359 2.280 1.00 24.33 O ANISOU 65 O VAL A 8 3470 3160 2615 80 -200 358 O ATOM 66 CB VAL A 8 -25.727 8.991 0.576 1.00 26.37 C ANISOU 66 CB VAL A 8 3847 3340 2832 56 -194 485 C ATOM 67 CG1 VAL A 8 -24.643 7.841 0.468 1.00 21.84 C ANISOU 67 CG1 VAL A 8 3271 2798 2228 21 -121 455 C ATOM 68 CG2 VAL A 8 -25.926 9.691 -0.775 1.00 30.15 C ANISOU 68 CG2 VAL A 8 4394 3810 3250 47 -227 546 C ATOM 69 N TYR A 9 -26.536 8.207 3.457 1.00 27.21 N ANISOU 69 N TYR A 9 3815 3456 3068 106 -197 382 N ATOM 70 CA TYR A 9 -26.293 7.490 4.696 1.00 23.46 C ANISOU 70 CA TYR A 9 3286 2994 2633 106 -165 334 C ATOM 71 C TYR A 9 -27.514 6.680 5.108 1.00 23.76 C ANISOU 71 C TYR A 9 3282 3070 2675 123 -198 300 C ATOM 72 O TYR A 9 -27.406 5.490 5.425 1.00 25.79 O ANISOU 72 O TYR A 9 3519 3355 2923 106 -174 268 O ATOM 73 CB TYR A 9 -25.889 8.503 5.787 1.00 25.76 C ANISOU 73 CB TYR A 9 3555 3244 2988 122 -159 331 C ATOM 74 CG TYR A 9 -25.976 7.923 7.182 1.00 24.65 C ANISOU 74 CG TYR A 9 3357 3120 2888 131 -144 283 C ATOM 75 CD1 TYR A 9 -25.113 6.889 7.575 1.00 22.23 C ANISOU 75 CD1 TYR A 9 3036 2833 2577 105 -96 259 C ATOM 76 CD2 TYR A 9 -26.928 8.365 8.086 1.00 22.70 C ANISOU 76 CD2 TYR A 9 3071 2872 2681 168 -176 261 C ATOM 77 CE1 TYR A 9 -25.188 6.311 8.844 1.00 23.03 C ANISOU 77 CE1 TYR A 9 3089 2950 2710 110 -85 221 C ATOM 78 CE2 TYR A 9 -27.004 7.783 9.377 1.00 23.76 C ANISOU 78 CE2 TYR A 9 3155 3028 2844 171 -158 219 C ATOM 79 CZ TYR A 9 -26.136 6.771 9.738 1.00 26.55 C ANISOU 79 CZ TYR A 9 3500 3399 3190 141 -115 202 C ATOM 80 OH TYR A 9 -26.190 6.203 11.015 1.00 28.99 O ANISOU 80 OH TYR A 9 3765 3728 3522 142 -101 166 O ATOM 81 N ILE A 10 -28.694 7.309 5.104 1.00 23.26 N ANISOU 81 N ILE A 10 3204 3007 2627 157 -254 308 N ATOM 82 CA ILE A 10 -29.914 6.628 5.547 1.00 24.11 C ANISOU 82 CA ILE A 10 3261 3156 2743 172 -284 277 C ATOM 83 C ILE A 10 -30.264 5.470 4.617 1.00 26.34 C ANISOU 83 C ILE A 10 3562 3477 2969 143 -295 273 C ATOM 84 O ILE A 10 -30.736 4.414 5.061 1.00 25.46 O ANISOU 84 O ILE A 10 3416 3400 2859 130 -293 240 O ATOM 85 CB ILE A 10 -31.079 7.647 5.632 1.00 24.71 C ANISOU 85 CB ILE A 10 3314 3226 2849 220 -343 288 C ATOM 86 CG1 ILE A 10 -30.845 8.633 6.790 1.00 27.62 C ANISOU 86 CG1 ILE A 10 3657 3559 3280 251 -332 275 C ATOM 87 CG2 ILE A 10 -32.476 6.962 5.716 1.00 24.93 C ANISOU 87 CG2 ILE A 10 3289 3307 2875 231 -384 266 C ATOM 88 CD1 ILE A 10 -31.785 9.828 6.724 1.00 28.72 C ANISOU 88 CD1 ILE A 10 3788 3676 3450 305 -388 290 C ATOM 89 N THR A 11 -30.133 5.681 3.311 1.00 24.79 N ANISOU 89 N THR A 11 3422 3276 2720 132 -311 307 N ATOM 90 CA THR A 11 -30.447 4.616 2.370 1.00 22.19 C ANISOU 90 CA THR A 11 3119 2982 2331 105 -324 299 C ATOM 91 C THR A 11 -29.553 3.418 2.600 1.00 22.39 C ANISOU 91 C THR A 11 3149 3015 2343 72 -266 266 C ATOM 92 O THR A 11 -30.012 2.274 2.546 1.00 23.43 O ANISOU 92 O THR A 11 3272 3175 2457 53 -274 237 O ATOM 93 CB THR A 11 -30.267 5.113 0.924 1.00 25.45 C ANISOU 93 CB THR A 11 3601 3388 2681 96 -344 342 C ATOM 94 OG1 THR A 11 -31.153 6.211 0.688 1.00 25.62 O ANISOU 94 OG1 THR A 11 3619 3399 2716 131 -406 376 O ATOM 95 CG2 THR A 11 -30.575 3.989 -0.109 1.00 22.33 C ANISOU 95 CG2 THR A 11 3239 3031 2214 66 -358 328 C ATOM 96 N VAL A 12 -28.255 3.666 2.814 1.00 21.99 N ANISOU 96 N VAL A 12 3116 2938 2302 64 -210 271 N ATOM 97 CA VAL A 12 -27.324 2.579 3.090 1.00 22.32 C ANISOU 97 CA VAL A 12 3158 2983 2339 41 -155 240 C ATOM 98 C VAL A 12 -27.700 1.877 4.392 1.00 21.48 C ANISOU 98 C VAL A 12 2995 2887 2282 44 -153 204 C ATOM 99 O VAL A 12 -27.703 0.644 4.466 1.00 20.98 O ANISOU 99 O VAL A 12 2929 2837 2205 26 -142 175 O ATOM 100 CB VAL A 12 -25.874 3.109 3.124 1.00 22.55 C ANISOU 100 CB VAL A 12 3205 2987 2377 34 -98 256 C ATOM 101 CG1 VAL A 12 -24.879 2.019 3.686 1.00 22.07 C ANISOU 101 CG1 VAL A 12 3129 2928 2328 21 -42 221 C ATOM 102 CG2 VAL A 12 -25.440 3.609 1.716 1.00 25.52 C ANISOU 102 CG2 VAL A 12 3644 3362 2692 20 -91 294 C ATOM 103 N GLU A 13 -28.040 2.646 5.436 1.00 21.55 N ANISOU 103 N GLU A 13 2959 2886 2343 68 -165 206 N ATOM 104 CA GLU A 13 -28.443 2.023 6.699 1.00 20.41 C ANISOU 104 CA GLU A 13 2761 2757 2238 69 -161 175 C ATOM 105 C GLU A 13 -29.664 1.132 6.487 1.00 21.13 C ANISOU 105 C GLU A 13 2835 2883 2311 57 -200 159 C ATOM 106 O GLU A 13 -29.735 0.009 7.009 1.00 22.98 O ANISOU 106 O GLU A 13 3051 3130 2549 35 -188 134 O ATOM 107 CB GLU A 13 -28.746 3.111 7.752 1.00 19.72 C ANISOU 107 CB GLU A 13 2632 2659 2203 100 -171 176 C ATOM 108 CG GLU A 13 -27.479 3.890 8.245 1.00 19.71 C ANISOU 108 CG GLU A 13 2641 2620 2229 104 -133 184 C ATOM 109 CD GLU A 13 -26.811 3.140 9.393 1.00 27.32 C ANISOU 109 CD GLU A 13 3576 3588 3217 91 -96 157 C ATOM 110 OE1 GLU A 13 -26.684 3.720 10.500 1.00 27.33 O ANISOU 110 OE1 GLU A 13 3547 3580 3258 106 -90 147 O ATOM 111 OE2 GLU A 13 -26.446 1.949 9.190 1.00 25.87 O ANISOU 111 OE2 GLU A 13 3402 3416 3012 68 -75 145 O ATOM 112 N LEU A 14 -30.630 1.606 5.717 1.00 21.12 N ANISOU 112 N LEU A 14 2838 2897 2290 68 -250 176 N ATOM 113 CA LEU A 14 -31.837 0.804 5.526 1.00 23.18 C ANISOU 113 CA LEU A 14 3075 3195 2536 53 -291 161 C ATOM 114 C LEU A 14 -31.531 -0.471 4.747 1.00 21.59 C ANISOU 114 C LEU A 14 2918 2998 2288 14 -283 146 C ATOM 115 O LEU A 14 -32.087 -1.535 5.046 1.00 22.39 O ANISOU 115 O LEU A 14 2998 3119 2391 -13 -293 122 O ATOM 116 CB LEU A 14 -32.914 1.632 4.820 1.00 26.37 C ANISOU 116 CB LEU A 14 3472 3616 2931 76 -353 184 C ATOM 117 CG LEU A 14 -33.423 2.797 5.689 1.00 33.93 C ANISOU 117 CG LEU A 14 4379 4571 3944 121 -367 191 C ATOM 118 CD1 LEU A 14 -34.445 3.645 4.952 1.00 34.78 C ANISOU 118 CD1 LEU A 14 4481 4689 4045 153 -431 215 C ATOM 119 CD2 LEU A 14 -33.980 2.300 7.009 1.00 35.86 C ANISOU 119 CD2 LEU A 14 4553 4843 4228 119 -355 159 C ATOM 120 N ALA A 15 -30.693 -0.373 3.707 1.00 23.52 N ANISOU 120 N ALA A 15 3224 3224 2487 8 -265 158 N ATOM 121 CA ALA A 15 -30.236 -1.564 3.009 1.00 21.33 C ANISOU 121 CA ALA A 15 2993 2946 2165 -22 -247 135 C ATOM 122 C ALA A 15 -29.583 -2.567 3.965 1.00 23.23 C ANISOU 122 C ALA A 15 3217 3172 2436 -35 -203 105 C ATOM 123 O ALA A 15 -29.841 -3.778 3.886 1.00 21.65 O ANISOU 123 O ALA A 15 3028 2977 2223 -62 -210 78 O ATOM 124 CB ALA A 15 -29.251 -1.166 1.911 1.00 22.56 C ANISOU 124 CB ALA A 15 3212 3088 2271 -21 -218 153 C ATOM 125 N ILE A 16 -28.725 -2.090 4.863 1.00 21.50 N ANISOU 125 N ILE A 16 2977 2935 2259 -18 -162 111 N ATOM 126 CA ILE A 16 -28.072 -3.006 5.799 1.00 20.36 C ANISOU 126 CA ILE A 16 2817 2776 2144 -27 -125 87 C ATOM 127 C ILE A 16 -29.105 -3.616 6.739 1.00 21.04 C ANISOU 127 C ILE A 16 2856 2880 2257 -42 -153 74 C ATOM 128 O ILE A 16 -29.058 -4.814 7.040 1.00 23.89 O ANISOU 128 O ILE A 16 3222 3234 2620 -65 -147 53 O ATOM 129 CB ILE A 16 -26.961 -2.265 6.576 1.00 20.84 C ANISOU 129 CB ILE A 16 2859 2816 2241 -7 -82 98 C ATOM 130 CG1 ILE A 16 -25.838 -1.861 5.608 1.00 26.03 C ANISOU 130 CG1 ILE A 16 3563 3460 2869 -3 -47 110 C ATOM 131 CG2 ILE A 16 -26.442 -3.112 7.803 1.00 25.07 C ANISOU 131 CG2 ILE A 16 3368 3342 2815 -13 -56 78 C ATOM 132 CD1 ILE A 16 -24.926 -0.843 6.177 1.00 21.42 C ANISOU 132 CD1 ILE A 16 2961 2859 2320 12 -17 128 C ATOM 133 N ALA A 17 -30.068 -2.808 7.198 1.00 21.90 N ANISOU 133 N ALA A 17 2919 3012 2389 -29 -184 86 N ATOM 134 CA ALA A 17 -31.086 -3.311 8.118 1.00 19.61 C ANISOU 134 CA ALA A 17 2578 2750 2125 -44 -205 76 C ATOM 135 C ALA A 17 -31.868 -4.467 7.500 1.00 23.50 C ANISOU 135 C ALA A 17 3083 3256 2588 -83 -238 62 C ATOM 136 O ALA A 17 -32.079 -5.499 8.143 1.00 25.43 O ANISOU 136 O ALA A 17 3314 3502 2846 -113 -235 48 O ATOM 137 CB ALA A 17 -32.004 -2.164 8.556 1.00 16.60 C ANISOU 137 CB ALA A 17 2143 2394 1768 -16 -231 88 C ATOM 138 N AVAL A 18 -32.289 -4.291 6.245 0.76 24.48 N ANISOU 138 N AVAL A 18 3239 3389 2673 -85 -272 67 N ATOM 139 N BVAL A 18 -32.257 -4.352 6.226 0.24 24.01 N ANISOU 139 N BVAL A 18 3182 3328 2612 -86 -271 66 N ATOM 140 CA AVAL A 18 -33.002 -5.322 5.493 0.76 23.54 C ANISOU 140 CA AVAL A 18 3141 3282 2520 -124 -310 51 C ATOM 141 CA BVAL A 18 -33.066 -5.422 5.636 0.24 23.64 C ANISOU 141 CA BVAL A 18 3148 3296 2537 -127 -310 50 C ATOM 142 C AVAL A 18 -32.210 -6.620 5.499 0.76 24.14 C ANISOU 142 C AVAL A 18 3262 3324 2586 -151 -280 26 C ATOM 143 C BVAL A 18 -32.232 -6.680 5.393 0.24 23.45 C ANISOU 143 C BVAL A 18 3179 3237 2495 -153 -282 25 C ATOM 144 O AVAL A 18 -32.713 -7.679 5.914 0.76 21.35 O ANISOU 144 O AVAL A 18 2898 2971 2243 -188 -294 11 O ATOM 145 O BVAL A 18 -32.744 -7.800 5.502 0.24 23.77 O ANISOU 145 O BVAL A 18 3221 3276 2534 -193 -302 7 O ATOM 146 CB AVAL A 18 -33.260 -4.824 4.063 0.76 22.05 C ANISOU 146 CB AVAL A 18 2995 3103 2281 -117 -345 62 C ATOM 147 CB BVAL A 18 -33.762 -4.943 4.348 0.24 23.10 C ANISOU 147 CB BVAL A 18 3101 3250 2427 -124 -360 61 C ATOM 148 CG1AVAL A 18 -33.747 -5.974 3.151 0.76 23.25 C ANISOU 148 CG1AVAL A 18 3186 3261 2388 -160 -381 39 C ATOM 149 CG1BVAL A 18 -32.747 -4.590 3.280 0.24 22.36 C ANISOU 149 CG1BVAL A 18 3079 3131 2288 -108 -338 67 C ATOM 150 CG2AVAL A 18 -34.280 -3.665 4.102 0.76 24.15 C ANISOU 150 CG2AVAL A 18 3210 3402 2563 -90 -389 87 C ATOM 151 CG2BVAL A 18 -34.743 -6.008 3.835 0.24 20.16 C ANISOU 151 CG2BVAL A 18 2733 2898 2030 -171 -409 42 C ATOM 152 N LEU A 19 -30.948 -6.533 5.070 1.00 22.32 N ANISOU 152 N LEU A 19 3079 3062 2338 -131 -238 23 N ATOM 153 CA LEU A 19 -30.097 -7.707 4.931 1.00 24.19 C ANISOU 153 CA LEU A 19 3363 3265 2565 -145 -208 -5 C ATOM 154 C LEU A 19 -29.803 -8.337 6.289 1.00 25.63 C ANISOU 154 C LEU A 19 3513 3429 2796 -152 -185 -9 C ATOM 155 O LEU A 19 -29.710 -9.564 6.397 1.00 24.91 O ANISOU 155 O LEU A 19 3447 3313 2707 -177 -186 -31 O ATOM 156 CB LEU A 19 -28.781 -7.341 4.215 1.00 22.10 C ANISOU 156 CB LEU A 19 3144 2980 2273 -117 -162 -6 C ATOM 157 CG LEU A 19 -29.002 -6.887 2.756 1.00 20.88 C ANISOU 157 CG LEU A 19 3035 2842 2055 -117 -182 -1 C ATOM 158 CD1 LEU A 19 -27.715 -6.211 2.196 1.00 21.64 C ANISOU 158 CD1 LEU A 19 3164 2929 2131 -90 -130 10 C ATOM 159 CD2 LEU A 19 -29.505 -8.056 1.853 1.00 24.81 C ANISOU 159 CD2 LEU A 19 3583 3338 2507 -150 -214 -35 C ATOM 160 N ALA A 20 -29.641 -7.518 7.328 1.00 22.03 N ANISOU 160 N ALA A 20 3008 2983 2380 -131 -167 11 N ATOM 161 CA ALA A 20 -29.357 -8.089 8.645 1.00 23.07 C ANISOU 161 CA ALA A 20 3112 3102 2552 -139 -147 9 C ATOM 162 C ALA A 20 -30.550 -8.900 9.147 1.00 25.67 C ANISOU 162 C ALA A 20 3415 3449 2890 -182 -183 7 C ATOM 163 O ALA A 20 -30.389 -9.990 9.711 1.00 24.01 O ANISOU 163 O ALA A 20 3215 3215 2692 -207 -178 -1 O ATOM 164 CB ALA A 20 -29.029 -6.976 9.639 1.00 18.81 C ANISOU 164 CB ALA A 20 2526 2575 2046 -109 -125 28 C ATOM 165 N ILE A 21 -31.757 -8.382 8.946 1.00 23.63 N ANISOU 165 N ILE A 21 3121 3233 2626 -191 -220 15 N ATOM 166 CA AILE A 21 -32.955 -9.077 9.401 0.87 24.84 C ANISOU 166 CA AILE A 21 3237 3412 2787 -236 -252 15 C ATOM 167 CA BILE A 21 -32.930 -9.100 9.431 0.13 24.62 C ANISOU 167 CA BILE A 21 3210 3384 2760 -237 -251 15 C ATOM 168 C ILE A 21 -33.135 -10.384 8.632 1.00 27.01 C ANISOU 168 C ILE A 21 3564 3661 3038 -280 -277 -5 C ATOM 169 O ILE A 21 -33.274 -11.474 9.216 1.00 27.18 O ANISOU 169 O ILE A 21 3590 3664 3074 -320 -280 -9 O ATOM 170 CB AILE A 21 -34.163 -8.135 9.273 0.87 22.78 C ANISOU 170 CB AILE A 21 2920 3207 2529 -229 -286 26 C ATOM 171 CB BILE A 21 -34.179 -8.196 9.429 0.13 23.29 C ANISOU 171 CB BILE A 21 2980 3272 2597 -231 -284 26 C ATOM 172 CG1AILE A 21 -34.052 -7.033 10.337 0.87 23.03 C ANISOU 172 CG1AILE A 21 2899 3259 2592 -189 -260 39 C ATOM 173 CG1BILE A 21 -35.400 -8.967 9.936 0.13 22.56 C ANISOU 173 CG1BILE A 21 2842 3214 2515 -284 -313 27 C ATOM 174 CG2AILE A 21 -35.477 -8.890 9.443 0.87 23.32 C ANISOU 174 CG2AILE A 21 2951 3311 2601 -282 -325 24 C ATOM 175 CG2BILE A 21 -34.462 -7.613 8.066 0.13 22.12 C ANISOU 175 CG2BILE A 21 2857 3133 2415 -215 -317 27 C ATOM 176 CD1AILE A 21 -34.921 -5.821 10.030 0.87 22.83 C ANISOU 176 CD1AILE A 21 2829 3274 2570 -158 -288 49 C ATOM 177 CD1BILE A 21 -36.688 -8.191 9.806 0.13 22.31 C ANISOU 177 CD1BILE A 21 2744 3244 2489 -278 -350 34 C ATOM 178 N LEU A 22 -33.071 -10.303 7.303 1.00 24.86 N ANISOU 178 N LEU A 22 3339 3382 2726 -274 -296 -18 N ATOM 179 CA LEU A 22 -33.325 -11.468 6.465 1.00 24.95 C ANISOU 179 CA LEU A 22 3402 3369 2707 -315 -325 -44 C ATOM 180 C LEU A 22 -32.362 -12.600 6.772 1.00 27.68 C ANISOU 180 C LEU A 22 3798 3656 3064 -322 -295 -62 C ATOM 181 O LEU A 22 -32.780 -13.746 6.972 1.00 29.98 O ANISOU 181 O LEU A 22 4105 3925 3363 -370 -318 -74 O ATOM 182 CB LEU A 22 -33.216 -11.089 4.983 1.00 24.75 C ANISOU 182 CB LEU A 22 3427 3347 2629 -299 -342 -56 C ATOM 183 CG LEU A 22 -34.361 -10.295 4.349 1.00 32.02 C ANISOU 183 CG LEU A 22 4316 4320 3529 -303 -394 -41 C ATOM 184 CD1 LEU A 22 -34.099 -10.043 2.839 1.00 33.11 C ANISOU 184 CD1 LEU A 22 4519 4457 3604 -290 -409 -52 C ATOM 185 CD2 LEU A 22 -35.660 -11.000 4.614 1.00 36.85 C ANISOU 185 CD2 LEU A 22 4889 4958 4154 -359 -444 -45 C ATOM 186 N GLY A 23 -31.057 -12.305 6.789 1.00 27.13 N ANISOU 186 N GLY A 23 3753 3559 2997 -277 -247 -65 N ATOM 187 CA GLY A 23 -30.086 -13.366 6.954 1.00 22.57 C ANISOU 187 CA GLY A 23 3223 2924 2429 -274 -221 -86 C ATOM 188 C GLY A 23 -30.151 -13.986 8.339 1.00 25.96 C ANISOU 188 C GLY A 23 3622 3336 2904 -295 -218 -70 C ATOM 189 O GLY A 23 -30.040 -15.206 8.498 1.00 24.44 O ANISOU 189 O GLY A 23 3468 3098 2722 -321 -227 -84 O ATOM 190 N ASN A 24 -30.300 -13.159 9.361 1.00 23.06 N ANISOU 190 N ASN A 24 3194 3005 2564 -284 -205 -41 N ATOM 191 CA ASN A 24 -30.338 -13.713 10.702 1.00 23.66 C ANISOU 191 CA ASN A 24 3244 3071 2675 -305 -199 -23 C ATOM 192 C ASN A 24 -31.679 -14.336 11.061 1.00 27.24 C ANISOU 192 C ASN A 24 3672 3546 3132 -369 -238 -13 C ATOM 193 O ASN A 24 -31.691 -15.276 11.859 1.00 25.82 O ANISOU 193 O ASN A 24 3501 3339 2972 -403 -241 -3 O ATOM 194 CB ASN A 24 -29.901 -12.649 11.700 1.00 19.12 C ANISOU 194 CB ASN A 24 2618 2525 2123 -270 -168 0 C ATOM 195 CG ASN A 24 -28.428 -12.392 11.557 1.00 20.61 C ANISOU 195 CG ASN A 24 2834 2681 2317 -219 -129 -8 C ATOM 196 OD1 ASN A 24 -27.601 -13.249 11.924 1.00 22.16 O ANISOU 196 OD1 ASN A 24 3059 2833 2530 -214 -116 -12 O ATOM 197 ND2 ASN A 24 -28.081 -11.264 10.950 1.00 22.01 N ANISOU 197 ND2 ASN A 24 3004 2878 2482 -183 -114 -8 N ATOM 198 N VAL A 25 -32.794 -13.902 10.454 1.00 23.45 N ANISOU 198 N VAL A 25 3164 3112 2633 -390 -271 -15 N ATOM 199 CA VAL A 25 -34.032 -14.688 10.589 1.00 28.99 C ANISOU 199 CA VAL A 25 3848 3831 3337 -459 -312 -10 C ATOM 200 C VAL A 25 -33.853 -16.075 9.980 1.00 30.13 C ANISOU 200 C VAL A 25 4066 3911 3472 -497 -334 -34 C ATOM 201 O VAL A 25 -34.312 -17.083 10.536 1.00 29.03 O ANISOU 201 O VAL A 25 3931 3751 3348 -554 -352 -25 O ATOM 202 CB VAL A 25 -35.228 -13.948 9.958 1.00 28.57 C ANISOU 202 CB VAL A 25 3747 3841 3267 -469 -347 -9 C ATOM 203 CG1 VAL A 25 -36.404 -14.911 9.687 1.00 27.08 C ANISOU 203 CG1 VAL A 25 3553 3662 3074 -545 -398 -14 C ATOM 204 CG2 VAL A 25 -35.674 -12.801 10.881 1.00 25.61 C ANISOU 204 CG2 VAL A 25 3289 3529 2913 -443 -330 15 C ATOM 205 N LEU A 26 -33.161 -16.157 8.847 1.00 27.31 N ANISOU 205 N LEU A 26 3772 3519 3087 -466 -332 -65 N ATOM 206 CA LEU A 26 -32.880 -17.452 8.237 1.00 28.72 C ANISOU 206 CA LEU A 26 4028 3629 3255 -492 -349 -96 C ATOM 207 C LEU A 26 -32.047 -18.355 9.159 1.00 25.93 C ANISOU 207 C LEU A 26 3703 3213 2936 -489 -326 -90 C ATOM 208 O LEU A 26 -32.281 -19.569 9.234 1.00 28.81 O ANISOU 208 O LEU A 26 4110 3526 3311 -537 -353 -98 O ATOM 209 CB LEU A 26 -32.170 -17.225 6.902 1.00 29.74 C ANISOU 209 CB LEU A 26 4215 3741 3343 -448 -339 -132 C ATOM 210 CG LEU A 26 -31.774 -18.485 6.133 1.00 38.82 C ANISOU 210 CG LEU A 26 5453 4821 4476 -462 -353 -177 C ATOM 211 CD1 LEU A 26 -33.030 -19.273 5.662 1.00 39.59 C ANISOU 211 CD1 LEU A 26 5567 4917 4559 -538 -417 -191 C ATOM 212 CD2 LEU A 26 -30.818 -18.168 4.940 1.00 36.64 C ANISOU 212 CD2 LEU A 26 5230 4533 4157 -406 -324 -213 C ATOM 213 N VAL A 27 -31.055 -17.794 9.845 1.00 21.93 N ANISOU 213 N VAL A 27 3178 2706 2449 -436 -281 -74 N ATOM 214 CA VAL A 27 -30.281 -18.566 10.820 1.00 26.30 C ANISOU 214 CA VAL A 27 3751 3206 3037 -430 -265 -62 C ATOM 215 C VAL A 27 -31.197 -19.131 11.906 1.00 26.70 C ANISOU 215 C VAL A 27 3771 3265 3109 -496 -288 -27 C ATOM 216 O VAL A 27 -31.097 -20.308 12.277 1.00 28.60 O ANISOU 216 O VAL A 27 4055 3445 3367 -529 -305 -23 O ATOM 217 CB VAL A 27 -29.165 -17.696 11.448 1.00 26.32 C ANISOU 217 CB VAL A 27 3724 3222 3056 -365 -217 -47 C ATOM 218 CG1 VAL A 27 -28.544 -18.388 12.702 1.00 25.04 C ANISOU 218 CG1 VAL A 27 3566 3019 2930 -365 -208 -22 C ATOM 219 CG2 VAL A 27 -28.057 -17.417 10.439 1.00 26.21 C ANISOU 219 CG2 VAL A 27 3748 3186 3026 -305 -188 -80 C ATOM 220 N CYS A 28 -32.042 -18.277 12.493 1.00 27.72 N ANISOU 220 N CYS A 28 3826 3470 3238 -514 -287 1 N ATOM 221 CA CYS A 28 -32.907 -18.729 13.585 1.00 28.30 C ANISOU 221 CA CYS A 28 3861 3564 3327 -578 -301 36 C ATOM 222 C CYS A 28 -33.884 -19.794 13.110 1.00 31.10 C ANISOU 222 C CYS A 28 4243 3897 3677 -656 -348 29 C ATOM 223 O CYS A 28 -34.175 -20.749 13.847 1.00 28.56 O ANISOU 223 O CYS A 28 3934 3546 3372 -713 -362 53 O ATOM 224 CB CYS A 28 -33.679 -17.553 14.177 1.00 28.46 C ANISOU 224 CB CYS A 28 3793 3676 3344 -576 -288 57 C ATOM 225 SG CYS A 28 -32.618 -16.365 15.006 1.00 28.77 S ANISOU 225 SG CYS A 28 3800 3738 3393 -499 -238 69 S ATOM 226 N ATRP A 29 -34.406 -19.641 11.883 0.55 29.96 N ANISOU 226 N ATRP A 29 4109 3766 3508 -663 -376 -2 N ATOM 227 N BTRP A 29 -34.437 -19.624 11.907 0.45 30.10 N ANISOU 227 N BTRP A 29 4125 3787 3526 -664 -376 -1 N ATOM 228 CA ATRP A 29 -35.349 -20.599 11.303 0.55 32.46 C ANISOU 228 CA ATRP A 29 4452 4063 3818 -739 -427 -15 C ATOM 229 CA BTRP A 29 -35.339 -20.632 11.362 0.45 32.59 C ANISOU 229 CA BTRP A 29 4469 4079 3836 -740 -426 -13 C ATOM 230 C ATRP A 29 -34.681 -21.946 11.028 0.55 33.48 C ANISOU 230 C ATRP A 29 4678 4089 3956 -753 -441 -37 C ATOM 231 C BTRP A 29 -34.621 -21.963 11.185 0.45 33.40 C ANISOU 231 C BTRP A 29 4666 4077 3949 -752 -438 -32 C ATOM 232 O ATRP A 29 -35.307 -22.998 11.191 0.55 35.20 O ANISOU 232 O ATRP A 29 4920 4271 4185 -829 -477 -29 O ATOM 233 O BTRP A 29 -35.142 -23.016 11.575 0.45 33.78 O ANISOU 233 O BTRP A 29 4735 4087 4013 -824 -467 -18 O ATOM 234 CB ATRP A 29 -35.950 -20.009 10.020 0.55 35.54 C ANISOU 234 CB ATRP A 29 4833 4495 4174 -733 -455 -44 C ATOM 235 CB BTRP A 29 -35.933 -20.157 10.037 0.45 35.71 C ANISOU 235 CB BTRP A 29 4862 4509 4198 -738 -457 -45 C ATOM 236 CG ATRP A 29 -37.279 -20.597 9.505 0.55 40.95 C ANISOU 236 CG ATRP A 29 5509 5200 4851 -817 -514 -51 C ATOM 237 CG BTRP A 29 -37.241 -19.447 10.199 0.45 40.44 C ANISOU 237 CG BTRP A 29 5371 5200 4795 -773 -477 -24 C ATOM 238 CD1ATRP A 29 -37.611 -20.831 8.197 0.55 46.73 C ANISOU 238 CD1ATRP A 29 6284 5921 5552 -833 -557 -89 C ATOM 239 CD1BTRP A 29 -37.482 -18.125 9.996 0.45 39.82 C ANISOU 239 CD1BTRP A 29 5232 5193 4705 -725 -466 -20 C ATOM 240 CD2ATRP A 29 -38.442 -20.965 10.278 0.55 45.49 C ANISOU 240 CD2ATRP A 29 6023 5815 5446 -899 -537 -18 C ATOM 241 CD2BTRP A 29 -38.490 -20.024 10.614 0.45 44.89 C ANISOU 241 CD2BTRP A 29 5890 5795 5371 -861 -512 -4 C ATOM 242 NE1ATRP A 29 -38.893 -21.336 8.109 0.55 46.86 N ANISOU 242 NE1ATRP A 29 6269 5965 5571 -919 -609 -83 N ATOM 243 NE1BTRP A 29 -38.800 -17.838 10.244 0.45 41.63 N ANISOU 243 NE1BTRP A 29 5381 5496 4941 -770 -493 -2 N ATOM 244 CE2ATRP A 29 -39.420 -21.430 9.371 0.55 47.10 C ANISOU 244 CE2ATRP A 29 6233 6027 5634 -962 -596 -39 C ATOM 245 CE2BTRP A 29 -39.440 -18.988 10.631 0.45 45.43 C ANISOU 245 CE2BTRP A 29 5866 5959 5437 -857 -519 9 C ATOM 246 CE3ATRP A 29 -38.745 -20.957 11.649 0.55 46.51 C ANISOU 246 CE3ATRP A 29 6092 5977 5602 -928 -512 27 C ATOM 247 CE3BTRP A 29 -38.895 -21.317 10.969 0.45 46.59 C ANISOU 247 CE3BTRP A 29 6134 5965 5603 -946 -539 6 C ATOM 248 CZ2ATRP A 29 -40.678 -21.887 9.793 0.55 48.91 C ANISOU 248 CZ2ATRP A 29 6406 6297 5879 -1055 -630 -15 C ATOM 249 CZ2BTRP A 29 -40.770 -19.201 10.988 0.45 45.32 C ANISOU 249 CZ2BTRP A 29 5780 6005 5434 -932 -548 28 C ATOM 250 CZ3ATRP A 29 -39.997 -21.411 12.063 0.55 46.63 C ANISOU 250 CZ3ATRP A 29 6054 6034 5629 -1019 -541 50 C ATOM 251 CZ3BTRP A 29 -40.215 -21.524 11.327 0.45 47.17 C ANISOU 251 CZ3BTRP A 29 6140 6096 5685 -1028 -568 30 C ATOM 252 CH2ATRP A 29 -40.942 -21.869 11.137 0.55 48.16 C ANISOU 252 CH2ATRP A 29 6250 6236 5812 -1082 -599 30 C ATOM 253 CH2BTRP A 29 -41.135 -20.472 11.331 0.45 46.76 C ANISOU 253 CH2BTRP A 29 5989 6148 5630 -1019 -571 39 C ATOM 254 N ALA A 30 -33.408 -21.932 10.620 1.00 31.73 N ANISOU 254 N ALA A 30 4510 3816 3731 -681 -413 -64 N ATOM 255 CA ALA A 30 -32.663 -23.171 10.411 1.00 32.59 C ANISOU 255 CA ALA A 30 4709 3823 3853 -678 -422 -88 C ATOM 256 C ALA A 30 -32.454 -23.931 11.728 1.00 34.31 C ANISOU 256 C ALA A 30 4931 3996 4109 -706 -420 -46 C ATOM 257 O ALA A 30 -32.600 -25.153 11.780 1.00 37.53 O ANISOU 257 O ALA A 30 5398 4329 4533 -754 -453 -48 O ATOM 258 CB ALA A 30 -31.317 -22.855 9.754 1.00 27.45 C ANISOU 258 CB ALA A 30 4097 3142 3191 -587 -384 -125 C ATOM 259 N VAL A 31 -32.088 -23.230 12.800 1.00 32.87 N ANISOU 259 N VAL A 31 4693 3856 3941 -676 -384 -7 N ATOM 260 CA VAL A 31 -31.868 -23.930 14.059 1.00 30.69 C ANISOU 260 CA VAL A 31 4425 3542 3694 -701 -384 37 C ATOM 261 C VAL A 31 -33.194 -24.454 14.609 1.00 36.02 C ANISOU 261 C VAL A 31 5074 4239 4371 -805 -417 73 C ATOM 262 O VAL A 31 -33.267 -25.576 15.135 1.00 33.06 O ANISOU 262 O VAL A 31 4745 3800 4017 -857 -441 97 O ATOM 263 CB VAL A 31 -31.147 -23.011 15.064 1.00 28.64 C ANISOU 263 CB VAL A 31 4113 3327 3443 -645 -340 67 C ATOM 264 CG1 VAL A 31 -31.048 -23.651 16.440 1.00 30.48 C ANISOU 264 CG1 VAL A 31 4349 3535 3697 -679 -343 120 C ATOM 265 CG2 VAL A 31 -29.773 -22.635 14.536 1.00 27.55 C ANISOU 265 CG2 VAL A 31 4001 3159 3307 -551 -310 34 C ATOM 266 N TRP A 32 -34.260 -23.656 14.500 1.00 32.97 N ANISOU 266 N TRP A 32 4613 3946 3967 -836 -418 79 N ATOM 267 CA TRP A 32 -35.563 -24.095 14.981 1.00 35.37 C ANISOU 267 CA TRP A 32 4879 4285 4273 -936 -445 112 C ATOM 268 C TRP A 32 -36.029 -25.365 14.266 1.00 39.47 C ANISOU 268 C TRP A 32 5468 4730 4797 -1007 -498 92 C ATOM 269 O TRP A 32 -36.588 -26.272 14.896 1.00 42.21 O ANISOU 269 O TRP A 32 5827 5050 5160 -1090 -521 128 O ATOM 270 CB TRP A 32 -36.585 -22.971 14.815 1.00 38.66 C ANISOU 270 CB TRP A 32 5201 4816 4671 -943 -440 112 C ATOM 271 CG TRP A 32 -38.015 -23.347 15.226 1.00 49.80 C ANISOU 271 CG TRP A 32 6557 6279 6085 -1047 -466 142 C ATOM 272 CD1 TRP A 32 -38.908 -24.114 14.518 1.00 54.73 C ANISOU 272 CD1 TRP A 32 7198 6887 6709 -1126 -516 129 C ATOM 273 CD2 TRP A 32 -38.705 -22.940 16.417 1.00 55.11 C ANISOU 273 CD2 TRP A 32 7144 7034 6759 -1082 -440 188 C ATOM 274 NE1 TRP A 32 -40.095 -24.228 15.208 1.00 51.49 N ANISOU 274 NE1 TRP A 32 6715 6545 6304 -1211 -523 167 N ATOM 275 CE2 TRP A 32 -39.997 -23.514 16.374 1.00 57.71 C ANISOU 275 CE2 TRP A 32 7439 7397 7092 -1184 -474 203 C ATOM 276 CE3 TRP A 32 -38.354 -22.153 17.522 1.00 57.74 C ANISOU 276 CE3 TRP A 32 7428 7420 7090 -1040 -391 215 C ATOM 277 CZ2 TRP A 32 -40.937 -23.320 17.397 1.00 62.22 C ANISOU 277 CZ2 TRP A 32 7923 8056 7663 -1243 -455 245 C ATOM 278 CZ3 TRP A 32 -39.294 -21.963 18.541 1.00 57.72 C ANISOU 278 CZ3 TRP A 32 7345 7502 7084 -1095 -373 253 C ATOM 279 CH2 TRP A 32 -40.566 -22.538 18.465 1.00 60.56 C ANISOU 279 CH2 TRP A 32 7667 7897 7447 -1194 -402 269 C ATOM 280 N LEU A 33 -35.779 -25.473 12.961 1.00 39.81 N ANISOU 280 N LEU A 33 5564 4736 4827 -977 -518 37 N ATOM 281 CA LEU A 33 -36.343 -26.560 12.177 1.00 42.05 C ANISOU 281 CA LEU A 33 5910 4958 5110 -1047 -573 10 C ATOM 282 C LEU A 33 -35.496 -27.831 12.172 1.00 45.19 C ANISOU 282 C LEU A 33 6415 5225 5530 -1043 -588 -4 C ATOM 283 O LEU A 33 -36.053 -28.931 12.067 1.00 48.33 O ANISOU 283 O LEU A 33 6862 5562 5941 -1124 -635 -4 O ATOM 284 CB LEU A 33 -36.566 -26.097 10.737 1.00 45.37 C ANISOU 284 CB LEU A 33 6340 5404 5496 -1022 -592 -47 C ATOM 285 CG LEU A 33 -37.649 -25.022 10.513 1.00 49.88 C ANISOU 285 CG LEU A 33 6813 6093 6046 -1041 -598 -37 C ATOM 286 CD1 LEU A 33 -37.607 -24.513 9.067 1.00 53.88 C ANISOU 286 CD1 LEU A 33 7343 6616 6514 -999 -615 -91 C ATOM 287 CD2 LEU A 33 -39.058 -25.486 10.872 1.00 45.95 C ANISOU 287 CD2 LEU A 33 6265 5635 5559 -1153 -639 -8 C ATOM 288 N ASN A 34 -34.176 -27.732 12.281 1.00 38.21 N ANISOU 288 N ASN A 34 5568 4296 4656 -951 -553 -17 N ATOM 289 CA ASN A 34 -33.302 -28.879 12.058 1.00 38.25 C ANISOU 289 CA ASN A 34 5676 4175 4682 -928 -568 -44 C ATOM 290 C ASN A 34 -32.690 -29.331 13.383 1.00 41.72 C ANISOU 290 C ASN A 34 6125 4570 5158 -921 -555 11 C ATOM 291 O ASN A 34 -31.855 -28.631 13.962 1.00 37.28 O ANISOU 291 O ASN A 34 5527 4038 4599 -849 -512 29 O ATOM 292 CB ASN A 34 -32.234 -28.537 11.023 1.00 35.61 C ANISOU 292 CB ASN A 34 5381 3818 4330 -827 -542 -107 C ATOM 293 CG ASN A 34 -31.278 -29.692 10.759 1.00 42.91 C ANISOU 293 CG ASN A 34 6408 4615 5279 -790 -554 -143 C ATOM 294 OD1 ASN A 34 -31.413 -30.791 11.342 1.00 41.76 O ANISOU 294 OD1 ASN A 34 6312 4386 5167 -840 -587 -118 O ATOM 295 ND2 ASN A 34 -30.309 -29.457 9.878 1.00 37.59 N ANISOU 295 ND2 ASN A 34 5767 3924 4590 -701 -525 -200 N ATOM 296 N SER A 35 -33.071 -30.531 13.845 1.00 39.97 N ANISOU 296 N SER A 35 5956 4270 4961 -998 -596 39 N ATOM 297 CA SER A 35 -32.567 -30.980 15.135 1.00 37.64 C ANISOU 297 CA SER A 35 5673 3933 4696 -998 -589 99 C ATOM 298 C SER A 35 -31.061 -31.283 15.088 1.00 40.07 C ANISOU 298 C SER A 35 6041 4156 5027 -893 -574 75 C ATOM 299 O SER A 35 -30.398 -31.211 16.133 1.00 39.06 O ANISOU 299 O SER A 35 5900 4024 4917 -859 -555 121 O ATOM 300 CB SER A 35 -33.367 -32.192 15.642 1.00 42.45 C ANISOU 300 CB SER A 35 6328 4477 5326 -1112 -639 142 C ATOM 301 OG SER A 35 -33.095 -33.334 14.854 1.00 43.95 O ANISOU 301 OG SER A 35 6623 4539 5535 -1116 -682 96 O ATOM 302 N ASN A 36 -30.488 -31.548 13.907 1.00 36.06 N ANISOU 302 N ASN A 36 5593 3591 4518 -835 -578 2 N ATOM 303 CA ASN A 36 -29.025 -31.644 13.846 1.00 43.00 C ANISOU 303 CA ASN A 36 6508 4412 5419 -723 -552 -25 C ATOM 304 C ASN A 36 -28.327 -30.308 14.116 1.00 42.94 C ANISOU 304 C ASN A 36 6418 4500 5396 -643 -495 -17 C ATOM 305 O ASN A 36 -27.106 -30.281 14.298 1.00 41.29 O ANISOU 305 O ASN A 36 6220 4259 5209 -556 -471 -26 O ATOM 306 CB ASN A 36 -28.565 -32.170 12.482 1.00 48.33 C ANISOU 306 CB ASN A 36 7260 5015 6089 -676 -561 -111 C ATOM 307 CG ASN A 36 -29.149 -33.539 12.149 1.00 52.56 C ANISOU 307 CG ASN A 36 7889 5440 6642 -749 -622 -128 C ATOM 308 OD1 ASN A 36 -29.515 -34.298 13.039 1.00 58.69 O ANISOU 308 OD1 ASN A 36 8690 6163 7448 -814 -656 -73 O ATOM 309 ND2 ASN A 36 -29.266 -33.837 10.868 1.00 49.07 N ANISOU 309 ND2 ASN A 36 7501 4965 6178 -743 -637 -205 N ATOM 310 N LEU A 37 -29.058 -29.200 14.132 1.00 37.14 N ANISOU 310 N LEU A 37 5601 3880 4628 -670 -474 -3 N ATOM 311 CA LEU A 37 -28.470 -27.916 14.448 1.00 34.26 C ANISOU 311 CA LEU A 37 5163 3603 4253 -603 -424 7 C ATOM 312 C LEU A 37 -28.782 -27.493 15.873 1.00 34.98 C ANISOU 312 C LEU A 37 5191 3751 4349 -637 -414 79 C ATOM 313 O LEU A 37 -28.342 -26.425 16.290 1.00 35.36 O ANISOU 313 O LEU A 37 5177 3869 4388 -589 -376 91 O ATOM 314 CB LEU A 37 -28.946 -26.840 13.442 1.00 34.05 C ANISOU 314 CB LEU A 37 5090 3662 4185 -594 -404 -30 C ATOM 315 CG LEU A 37 -28.413 -26.930 12.000 1.00 39.42 C ANISOU 315 CG LEU A 37 5821 4308 4847 -541 -398 -103 C ATOM 316 CD1 LEU A 37 -29.134 -25.945 11.071 1.00 37.06 C ANISOU 316 CD1 LEU A 37 5482 4097 4504 -552 -391 -128 C ATOM 317 CD2 LEU A 37 -26.894 -26.681 11.949 1.00 35.65 C ANISOU 317 CD2 LEU A 37 5352 3809 4385 -436 -355 -124 C ATOM 318 N GLN A 38 -29.508 -28.308 16.636 1.00 37.41 N ANISOU 318 N GLN A 38 5516 4030 4667 -721 -448 126 N ATOM 319 CA GLN A 38 -29.919 -27.929 17.994 1.00 39.00 C ANISOU 319 CA GLN A 38 5659 4296 4864 -763 -436 195 C ATOM 320 C GLN A 38 -28.917 -28.508 18.986 1.00 38.89 C ANISOU 320 C GLN A 38 5682 4216 4877 -728 -441 234 C ATOM 321 O GLN A 38 -29.023 -29.649 19.426 1.00 42.23 O ANISOU 321 O GLN A 38 6166 4558 5321 -776 -477 267 O ATOM 322 CB GLN A 38 -31.343 -28.380 18.285 1.00 36.15 C ANISOU 322 CB GLN A 38 5285 3959 4493 -880 -465 229 C ATOM 323 CG GLN A 38 -32.337 -27.709 17.351 1.00 39.26 C ANISOU 323 CG GLN A 38 5629 4428 4859 -908 -464 193 C ATOM 324 CD GLN A 38 -33.713 -28.369 17.362 1.00 44.53 C ANISOU 324 CD GLN A 38 6293 5103 5524 -1027 -501 214 C ATOM 325 OE1 GLN A 38 -33.968 -29.297 18.121 1.00 43.15 O ANISOU 325 OE1 GLN A 38 6151 4880 5364 -1095 -524 262 O ATOM 326 NE2 GLN A 38 -34.597 -27.885 16.512 1.00 45.13 N ANISOU 326 NE2 GLN A 38 6328 5239 5579 -1054 -509 183 N ATOM 327 N ASN A 39 -27.942 -27.691 19.344 1.00 38.05 N ANISOU 327 N ASN A 39 5539 4146 4772 -647 -406 233 N ATOM 328 CA ASN A 39 -26.920 -28.052 20.307 1.00 35.08 C ANISOU 328 CA ASN A 39 5184 3724 4419 -604 -410 270 C ATOM 329 C ASN A 39 -26.560 -26.759 21.009 1.00 35.14 C ANISOU 329 C ASN A 39 5113 3831 4409 -564 -370 287 C ATOM 330 O ASN A 39 -27.003 -25.669 20.613 1.00 33.50 O ANISOU 330 O ASN A 39 4843 3709 4175 -559 -340 263 O ATOM 331 CB ASN A 39 -25.712 -28.698 19.612 1.00 34.35 C ANISOU 331 CB ASN A 39 5155 3532 4362 -521 -419 226 C ATOM 332 CG ASN A 39 -25.254 -27.882 18.391 1.00 41.99 C ANISOU 332 CG ASN A 39 6100 4535 5321 -451 -384 156 C ATOM 333 OD1 ASN A 39 -24.873 -26.720 18.518 1.00 36.42 O ANISOU 333 OD1 ASN A 39 5328 3909 4601 -407 -346 152 O ATOM 334 ND2 ASN A 39 -25.325 -28.480 17.209 1.00 43.34 N ANISOU 334 ND2 ASN A 39 6326 4646 5494 -445 -396 100 N ATOM 335 N VAL A 40 -25.736 -26.873 22.044 1.00 34.37 N ANISOU 335 N VAL A 40 5017 3717 4324 -532 -373 327 N ATOM 336 CA VAL A 40 -25.469 -25.713 22.887 1.00 36.20 C ANISOU 336 CA VAL A 40 5178 4041 4535 -507 -342 347 C ATOM 337 C VAL A 40 -24.747 -24.636 22.099 1.00 35.63 C ANISOU 337 C VAL A 40 5066 4009 4465 -426 -305 293 C ATOM 338 O VAL A 40 -25.056 -23.444 22.232 1.00 34.12 O ANISOU 338 O VAL A 40 4809 3907 4249 -423 -275 287 O ATOM 339 CB VAL A 40 -24.670 -26.120 24.137 1.00 36.11 C ANISOU 339 CB VAL A 40 5184 4000 4535 -489 -360 401 C ATOM 340 CG1 VAL A 40 -23.952 -24.905 24.667 1.00 35.77 C ANISOU 340 CG1 VAL A 40 5077 4032 4480 -432 -329 399 C ATOM 341 CG2 VAL A 40 -25.606 -26.692 25.178 1.00 36.22 C ANISOU 341 CG2 VAL A 40 5212 4025 4527 -584 -381 468 C ATOM 342 N THR A 41 -23.773 -25.037 21.273 1.00 34.28 N ANISOU 342 N THR A 41 4933 3769 4324 -359 -307 252 N ATOM 343 CA THR A 41 -23.048 -24.070 20.455 1.00 33.23 C ANISOU 343 CA THR A 41 4764 3672 4191 -287 -270 203 C ATOM 344 C THR A 41 -24.006 -23.172 19.687 1.00 34.57 C ANISOU 344 C THR A 41 4896 3913 4328 -316 -248 175 C ATOM 345 O THR A 41 -23.906 -21.937 19.724 1.00 31.23 O ANISOU 345 O THR A 41 4414 3565 3889 -292 -217 168 O ATOM 346 CB THR A 41 -22.129 -24.780 19.466 1.00 34.89 C ANISOU 346 CB THR A 41 5025 3800 4431 -224 -273 156 C ATOM 347 OG1 THR A 41 -21.461 -25.872 20.118 1.00 37.66 O ANISOU 347 OG1 THR A 41 5425 4068 4818 -205 -305 183 O ATOM 348 CG2 THR A 41 -21.111 -23.781 18.933 1.00 32.29 C ANISOU 348 CG2 THR A 41 4651 3511 4105 -146 -230 119 C ATOM 349 N ASN A 42 -24.956 -23.788 18.995 1.00 30.67 N ANISOU 349 N ASN A 42 4436 3395 3824 -370 -268 160 N ATOM 350 CA ASN A 42 -25.878 -23.035 18.187 1.00 24.67 C ANISOU 350 CA ASN A 42 3643 2696 3033 -396 -256 134 C ATOM 351 C ASN A 42 -26.943 -22.290 19.002 1.00 26.66 C ANISOU 351 C ASN A 42 3831 3037 3261 -451 -250 170 C ATOM 352 O ASN A 42 -27.640 -21.452 18.423 1.00 28.45 O ANISOU 352 O ASN A 42 4018 3326 3466 -460 -238 150 O ATOM 353 CB ASN A 42 -26.525 -23.988 17.180 1.00 26.12 C ANISOU 353 CB ASN A 42 3885 2824 3214 -436 -286 104 C ATOM 354 CG ASN A 42 -25.579 -24.377 16.091 1.00 33.20 C ANISOU 354 CG ASN A 42 4834 3658 4122 -372 -279 49 C ATOM 355 OD1 ASN A 42 -24.533 -23.743 15.917 1.00 31.00 O ANISOU 355 OD1 ASN A 42 4534 3394 3849 -298 -246 32 O ATOM 356 ND2 ASN A 42 -25.937 -25.413 15.322 1.00 31.05 N ANISOU 356 ND2 ASN A 42 4629 3316 3852 -401 -309 20 N ATOM 357 N TYR A 43 -27.112 -22.547 20.309 1.00 24.50 N ANISOU 357 N TYR A 43 3546 2774 2989 -487 -258 222 N ATOM 358 CA TYR A 43 -27.984 -21.634 21.059 1.00 28.41 C ANISOU 358 CA TYR A 43 3972 3366 3458 -523 -241 246 C ATOM 359 C TYR A 43 -27.322 -20.260 21.225 1.00 26.47 C ANISOU 359 C TYR A 43 3673 3179 3206 -456 -205 232 C ATOM 360 O TYR A 43 -28.005 -19.225 21.200 1.00 25.11 O ANISOU 360 O TYR A 43 3444 3084 3014 -462 -187 224 O ATOM 361 CB TYR A 43 -28.366 -22.227 22.417 1.00 30.79 C ANISOU 361 CB TYR A 43 4274 3672 3752 -582 -253 305 C ATOM 362 CG TYR A 43 -29.035 -23.591 22.259 1.00 36.82 C ANISOU 362 CG TYR A 43 5093 4372 4524 -656 -291 324 C ATOM 363 CD1 TYR A 43 -29.751 -23.903 21.095 1.00 40.33 C ANISOU 363 CD1 TYR A 43 5554 4799 4970 -686 -307 289 C ATOM 364 CD2 TYR A 43 -28.938 -24.558 23.247 1.00 37.69 C ANISOU 364 CD2 TYR A 43 5243 4437 4640 -697 -313 378 C ATOM 365 CE1 TYR A 43 -30.345 -25.140 20.917 1.00 42.60 C ANISOU 365 CE1 TYR A 43 5895 5023 5267 -757 -345 303 C ATOM 366 CE2 TYR A 43 -29.539 -25.795 23.091 1.00 43.42 C ANISOU 366 CE2 TYR A 43 6024 5097 5377 -769 -350 397 C ATOM 367 CZ TYR A 43 -30.239 -26.085 21.918 1.00 45.22 C ANISOU 367 CZ TYR A 43 6267 5307 5609 -800 -365 357 C ATOM 368 OH TYR A 43 -30.828 -27.319 21.751 1.00 42.93 O ANISOU 368 OH TYR A 43 6034 4945 5331 -876 -405 374 O ATOM 369 N PHE A 44 -26.007 -20.240 21.374 1.00 21.49 N ANISOU 369 N PHE A 44 3059 2511 2595 -394 -198 227 N ATOM 370 CA PHE A 44 -25.274 -18.970 21.370 1.00 23.17 C ANISOU 370 CA PHE A 44 3227 2769 2807 -332 -168 209 C ATOM 371 C PHE A 44 -25.281 -18.349 19.990 1.00 20.63 C ANISOU 371 C PHE A 44 2900 2457 2482 -302 -152 162 C ATOM 372 O PHE A 44 -25.410 -17.127 19.856 1.00 21.66 O ANISOU 372 O PHE A 44 2984 2646 2600 -282 -129 150 O ATOM 373 CB PHE A 44 -23.848 -19.190 21.891 1.00 22.06 C ANISOU 373 CB PHE A 44 3102 2587 2691 -278 -168 218 C ATOM 374 CG PHE A 44 -23.810 -19.611 23.342 1.00 26.40 C ANISOU 374 CG PHE A 44 3653 3140 3237 -306 -186 269 C ATOM 375 CD1 PHE A 44 -24.122 -18.706 24.333 1.00 28.96 C ANISOU 375 CD1 PHE A 44 3927 3538 3536 -320 -171 288 C ATOM 376 CD2 PHE A 44 -23.481 -20.909 23.704 1.00 26.51 C ANISOU 376 CD2 PHE A 44 3723 3081 3270 -318 -217 297 C ATOM 377 CE1 PHE A 44 -24.112 -19.090 25.662 1.00 31.33 C ANISOU 377 CE1 PHE A 44 4233 3847 3823 -349 -186 335 C ATOM 378 CE2 PHE A 44 -23.468 -21.286 25.022 1.00 28.20 C ANISOU 378 CE2 PHE A 44 3942 3299 3475 -346 -236 349 C ATOM 379 CZ PHE A 44 -23.800 -20.390 25.998 1.00 29.86 C ANISOU 379 CZ PHE A 44 4103 3590 3653 -364 -219 369 C ATOM 380 N VAL A 45 -25.216 -19.179 18.948 1.00 25.14 N ANISOU 380 N VAL A 45 3523 2970 3061 -300 -165 136 N ATOM 381 CA VAL A 45 -25.354 -18.672 17.583 1.00 25.01 C ANISOU 381 CA VAL A 45 3507 2964 3030 -280 -153 94 C ATOM 382 C VAL A 45 -26.693 -17.951 17.397 1.00 24.10 C ANISOU 382 C VAL A 45 3351 2917 2888 -323 -156 96 C ATOM 383 O VAL A 45 -26.775 -16.907 16.736 1.00 21.74 O ANISOU 383 O VAL A 45 3024 2660 2575 -298 -139 76 O ATOM 384 CB VAL A 45 -25.201 -19.836 16.579 1.00 26.44 C ANISOU 384 CB VAL A 45 3758 3071 3218 -281 -171 64 C ATOM 385 CG1 VAL A 45 -25.803 -19.434 15.194 1.00 24.15 C ANISOU 385 CG1 VAL A 45 3474 2803 2898 -287 -169 25 C ATOM 386 CG2 VAL A 45 -23.734 -20.197 16.419 1.00 25.52 C ANISOU 386 CG2 VAL A 45 3670 2900 3127 -214 -156 46 C ATOM 387 N VAL A 46 -27.772 -18.515 17.950 1.00 25.88 N ANISOU 387 N VAL A 46 3572 3155 3108 -390 -179 121 N ATOM 388 CA VAL A 46 -29.085 -17.886 17.825 1.00 22.60 C ANISOU 388 CA VAL A 46 3107 2808 2671 -430 -184 123 C ATOM 389 C VAL A 46 -29.171 -16.613 18.674 1.00 24.67 C ANISOU 389 C VAL A 46 3302 3144 2927 -409 -158 137 C ATOM 390 O VAL A 46 -29.763 -15.619 18.247 1.00 23.66 O ANISOU 390 O VAL A 46 3133 3070 2787 -398 -151 123 O ATOM 391 CB VAL A 46 -30.185 -18.895 18.207 1.00 24.87 C ANISOU 391 CB VAL A 46 3403 3091 2956 -512 -214 147 C ATOM 392 CG1 VAL A 46 -31.540 -18.163 18.357 1.00 23.64 C ANISOU 392 CG1 VAL A 46 3177 3023 2783 -552 -214 154 C ATOM 393 CG2 VAL A 46 -30.246 -20.027 17.177 1.00 24.85 C ANISOU 393 CG2 VAL A 46 3468 3016 2958 -536 -244 123 C ATOM 394 N SER A 47 -28.595 -16.614 19.882 1.00 24.34 N ANISOU 394 N SER A 47 3252 3103 2892 -400 -146 164 N ATOM 395 CA SER A 47 -28.503 -15.356 20.643 1.00 23.68 C ANISOU 395 CA SER A 47 3113 3083 2802 -371 -121 168 C ATOM 396 C SER A 47 -27.773 -14.274 19.841 1.00 22.25 C ANISOU 396 C SER A 47 2924 2904 2626 -308 -102 138 C ATOM 397 O SER A 47 -28.196 -13.113 19.819 1.00 20.08 O ANISOU 397 O SER A 47 2604 2682 2343 -292 -90 129 O ATOM 398 CB SER A 47 -27.805 -15.582 21.994 1.00 24.96 C ANISOU 398 CB SER A 47 3277 3239 2968 -368 -115 198 C ATOM 399 OG SER A 47 -27.767 -14.377 22.779 1.00 25.05 O ANISOU 399 OG SER A 47 3238 3311 2969 -345 -93 198 O ATOM 400 N LEU A 48 -26.685 -14.644 19.162 1.00 21.44 N ANISOU 400 N LEU A 48 2864 2746 2538 -272 -100 123 N ATOM 401 CA LEU A 48 -25.955 -13.697 18.333 1.00 23.45 C ANISOU 401 CA LEU A 48 3112 3001 2794 -219 -80 98 C ATOM 402 C LEU A 48 -26.801 -13.231 17.148 1.00 21.17 C ANISOU 402 C LEU A 48 2821 2736 2488 -226 -85 78 C ATOM 403 O LEU A 48 -26.809 -12.035 16.814 1.00 21.46 O ANISOU 403 O LEU A 48 2830 2806 2519 -198 -72 69 O ATOM 404 CB LEU A 48 -24.641 -14.350 17.868 1.00 23.04 C ANISOU 404 CB LEU A 48 3105 2889 2762 -182 -72 85 C ATOM 405 CG LEU A 48 -23.655 -13.597 16.997 1.00 23.26 C ANISOU 405 CG LEU A 48 3133 2912 2793 -131 -46 62 C ATOM 406 CD1 LEU A 48 -23.165 -12.306 17.758 1.00 23.56 C ANISOU 406 CD1 LEU A 48 3122 2990 2839 -106 -27 73 C ATOM 407 CD2 LEU A 48 -22.425 -14.530 16.689 1.00 23.27 C ANISOU 407 CD2 LEU A 48 3173 2853 2815 -97 -39 50 C ATOM 408 N ALA A 49 -27.567 -14.148 16.533 1.00 23.28 N ANISOU 408 N ALA A 49 3117 2985 2745 -265 -110 71 N ATOM 409 CA ALA A 49 -28.435 -13.759 15.414 1.00 22.55 C ANISOU 409 CA ALA A 49 3020 2916 2630 -276 -124 53 C ATOM 410 C ALA A 49 -29.561 -12.842 15.889 1.00 23.77 C ANISOU 410 C ALA A 49 3112 3141 2779 -292 -129 66 C ATOM 411 O ALA A 49 -29.942 -11.902 15.183 1.00 21.61 O ANISOU 411 O ALA A 49 2819 2898 2494 -272 -131 55 O ATOM 412 CB ALA A 49 -29.003 -15.006 14.709 1.00 21.53 C ANISOU 412 CB ALA A 49 2936 2751 2492 -320 -154 42 C ATOM 413 N ALA A 50 -30.072 -13.077 17.100 1.00 21.30 N ANISOU 413 N ALA A 50 2767 2854 2472 -324 -129 88 N ATOM 414 CA ALA A 50 -31.097 -12.208 17.680 1.00 24.86 C ANISOU 414 CA ALA A 50 3152 3376 2918 -333 -127 96 C ATOM 415 C ALA A 50 -30.576 -10.794 17.898 1.00 22.85 C ANISOU 415 C ALA A 50 2869 3145 2668 -276 -103 89 C ATOM 416 O ALA A 50 -31.261 -9.818 17.591 1.00 22.48 O ANISOU 416 O ALA A 50 2785 3140 2618 -259 -106 81 O ATOM 417 CB ALA A 50 -31.587 -12.789 19.015 1.00 22.95 C ANISOU 417 CB ALA A 50 2886 3159 2677 -379 -124 122 C ATOM 418 N ALA A 51 -29.369 -10.669 18.458 1.00 21.49 N ANISOU 418 N ALA A 51 2713 2944 2506 -246 -83 92 N ATOM 419 CA ALA A 51 -28.737 -9.353 18.557 1.00 23.39 C ANISOU 419 CA ALA A 51 2936 3198 2755 -196 -63 84 C ATOM 420 C ALA A 51 -28.659 -8.672 17.183 1.00 22.40 C ANISOU 420 C ALA A 51 2824 3061 2624 -167 -67 68 C ATOM 421 O ALA A 51 -28.899 -7.468 17.068 1.00 23.14 O ANISOU 421 O ALA A 51 2891 3182 2720 -140 -63 63 O ATOM 422 CB ALA A 51 -27.342 -9.492 19.182 1.00 23.40 C ANISOU 422 CB ALA A 51 2957 3163 2770 -173 -46 90 C ATOM 423 N ASP A 52 -28.326 -9.429 16.131 1.00 19.76 N ANISOU 423 N ASP A 52 2536 2688 2282 -173 -74 60 N ATOM 424 CA ASP A 52 -28.151 -8.823 14.815 1.00 21.92 C ANISOU 424 CA ASP A 52 2831 2955 2544 -148 -75 48 C ATOM 425 C ASP A 52 -29.502 -8.465 14.181 1.00 23.73 C ANISOU 425 C ASP A 52 3039 3221 2757 -164 -104 46 C ATOM 426 O ASP A 52 -29.624 -7.423 13.515 1.00 23.27 O ANISOU 426 O ASP A 52 2974 3176 2690 -136 -107 44 O ATOM 427 CB ASP A 52 -27.307 -9.751 13.926 1.00 22.06 C ANISOU 427 CB ASP A 52 2906 2923 2553 -146 -70 35 C ATOM 428 CG ASP A 52 -25.826 -9.749 14.331 1.00 27.05 C ANISOU 428 CG ASP A 52 3548 3524 3204 -115 -39 35 C ATOM 429 OD1 ASP A 52 -25.390 -8.712 14.900 1.00 28.15 O ANISOU 429 OD1 ASP A 52 3658 3681 3358 -91 -23 44 O ATOM 430 OD2 ASP A 52 -25.110 -10.772 14.093 1.00 29.46 O ANISOU 430 OD2 ASP A 52 3892 3788 3515 -113 -33 26 O ATOM 431 N ILE A 53 -30.538 -9.281 14.423 1.00 25.23 N ANISOU 431 N ILE A 53 3215 3429 2942 -208 -127 49 N ATOM 432 CA ILE A 53 -31.898 -8.902 14.032 1.00 22.25 C ANISOU 432 CA ILE A 53 2801 3098 2555 -223 -156 48 C ATOM 433 C ILE A 53 -32.278 -7.576 14.685 1.00 24.20 C ANISOU 433 C ILE A 53 2990 3388 2815 -190 -147 53 C ATOM 434 O ILE A 53 -32.871 -6.691 14.050 1.00 22.50 O ANISOU 434 O ILE A 53 2756 3197 2596 -167 -165 51 O ATOM 435 CB ILE A 53 -32.900 -10.019 14.403 1.00 20.82 C ANISOU 435 CB ILE A 53 2604 2934 2373 -284 -179 53 C ATOM 436 CG1 ILE A 53 -32.626 -11.274 13.572 1.00 23.42 C ANISOU 436 CG1 ILE A 53 2997 3213 2690 -316 -196 43 C ATOM 437 CG2 ILE A 53 -34.353 -9.553 14.173 1.00 23.05 C ANISOU 437 CG2 ILE A 53 2830 3277 2652 -299 -208 54 C ATOM 438 CD1 ILE A 53 -33.509 -12.472 13.946 1.00 23.22 C ANISOU 438 CD1 ILE A 53 2966 3191 2666 -384 -220 51 C ATOM 439 N LEU A 54 -31.992 -7.440 15.981 1.00 22.38 N ANISOU 439 N LEU A 54 2734 3169 2599 -186 -123 58 N ATOM 440 CA LEU A 54 -32.301 -6.196 16.676 1.00 23.91 C ANISOU 440 CA LEU A 54 2878 3400 2805 -152 -112 56 C ATOM 441 C LEU A 54 -31.442 -5.030 16.207 1.00 23.29 C ANISOU 441 C LEU A 54 2821 3295 2734 -101 -102 51 C ATOM 442 O LEU A 54 -31.868 -3.885 16.363 1.00 20.66 O ANISOU 442 O LEU A 54 2455 2985 2411 -68 -105 46 O ATOM 443 CB LEU A 54 -32.154 -6.372 18.189 1.00 21.03 C ANISOU 443 CB LEU A 54 2489 3055 2447 -163 -88 60 C ATOM 444 CG LEU A 54 -33.232 -7.288 18.812 1.00 24.52 C ANISOU 444 CG LEU A 54 2897 3539 2881 -217 -94 69 C ATOM 445 CD1 LEU A 54 -32.902 -7.561 20.284 1.00 24.80 C ANISOU 445 CD1 LEU A 54 2920 3588 2914 -232 -69 79 C ATOM 446 CD2 LEU A 54 -34.619 -6.644 18.689 1.00 27.14 C ANISOU 446 CD2 LEU A 54 3166 3933 3215 -213 -108 61 C ATOM 447 N VAL A 55 -30.253 -5.272 15.651 1.00 20.74 N ANISOU 447 N VAL A 55 2548 2924 2408 -93 -90 53 N ATOM 448 CA VAL A 55 -29.538 -4.161 14.993 1.00 20.64 C ANISOU 448 CA VAL A 55 2555 2889 2399 -53 -83 53 C ATOM 449 C VAL A 55 -30.376 -3.622 13.835 1.00 23.22 C ANISOU 449 C VAL A 55 2883 3229 2712 -44 -112 55 C ATOM 450 O VAL A 55 -30.534 -2.394 13.658 1.00 21.15 O ANISOU 450 O VAL A 55 2609 2970 2457 -10 -118 58 O ATOM 451 CB VAL A 55 -28.128 -4.606 14.523 1.00 19.68 C ANISOU 451 CB VAL A 55 2482 2721 2274 -50 -60 54 C ATOM 452 CG1 VAL A 55 -27.494 -3.558 13.512 1.00 19.18 C ANISOU 452 CG1 VAL A 55 2443 2638 2205 -21 -54 59 C ATOM 453 CG2 VAL A 55 -27.215 -4.777 15.749 1.00 17.58 C ANISOU 453 CG2 VAL A 55 2207 2445 2029 -48 -36 55 C ATOM 454 N GLY A 56 -30.980 -4.530 13.069 1.00 23.45 N ANISOU 454 N GLY A 56 2928 3263 2719 -74 -135 54 N ATOM 455 CA GLY A 56 -31.780 -4.113 11.935 1.00 21.80 C ANISOU 455 CA GLY A 56 2722 3069 2492 -68 -169 57 C ATOM 456 C GLY A 56 -33.087 -3.455 12.349 1.00 23.30 C ANISOU 456 C GLY A 56 2850 3307 2696 -57 -195 57 C ATOM 457 O GLY A 56 -33.496 -2.451 11.774 1.00 24.72 O ANISOU 457 O GLY A 56 3021 3494 2875 -25 -217 64 O ATOM 458 N VAL A 57 -33.757 -4.011 13.344 1.00 19.43 N ANISOU 458 N VAL A 57 2314 2851 2218 -82 -192 52 N ATOM 459 CA VAL A 57 -35.097 -3.544 13.701 1.00 22.50 C ANISOU 459 CA VAL A 57 2634 3295 2619 -75 -213 49 C ATOM 460 C VAL A 57 -35.048 -2.264 14.555 1.00 23.32 C ANISOU 460 C VAL A 57 2702 3410 2748 -24 -195 43 C ATOM 461 O VAL A 57 -35.914 -1.375 14.439 1.00 24.97 O ANISOU 461 O VAL A 57 2870 3649 2970 10 -217 39 O ATOM 462 CB VAL A 57 -35.831 -4.701 14.418 1.00 27.90 C ANISOU 462 CB VAL A 57 3283 4016 3303 -129 -213 47 C ATOM 463 CG1 VAL A 57 -37.160 -4.219 15.045 1.00 37.32 C ANISOU 463 CG1 VAL A 57 4392 5278 4511 -122 -222 42 C ATOM 464 CG2 VAL A 57 -36.094 -5.834 13.426 1.00 29.22 C ANISOU 464 CG2 VAL A 57 3485 4170 3447 -178 -243 50 C ATOM 465 N LEU A 58 -34.069 -2.156 15.444 1.00 18.24 N ANISOU 465 N LEU A 58 2073 2743 2113 -17 -158 39 N ATOM 466 CA LEU A 58 -34.034 -1.055 16.415 1.00 21.80 C ANISOU 466 CA LEU A 58 2492 3205 2585 24 -140 26 C ATOM 467 C LEU A 58 -32.786 -0.190 16.301 1.00 23.99 C ANISOU 467 C LEU A 58 2814 3430 2872 56 -126 28 C ATOM 468 O LEU A 58 -32.896 1.041 16.199 1.00 21.27 O ANISOU 468 O LEU A 58 2463 3076 2545 100 -135 23 O ATOM 469 CB LEU A 58 -34.126 -1.586 17.865 1.00 24.85 C ANISOU 469 CB LEU A 58 2844 3624 2972 1 -111 17 C ATOM 470 CG LEU A 58 -35.498 -2.158 18.264 1.00 28.27 C ANISOU 470 CG LEU A 58 3216 4124 3401 -28 -119 14 C ATOM 471 CD1 LEU A 58 -35.472 -2.790 19.683 1.00 25.53 C ANISOU 471 CD1 LEU A 58 2846 3808 3045 -61 -86 12 C ATOM 472 CD2 LEU A 58 -36.557 -1.080 18.161 1.00 28.32 C ANISOU 472 CD2 LEU A 58 3167 4170 3424 18 -136 0 C ATOM 473 N ALA A 59 -31.586 -0.786 16.349 1.00 21.90 N ANISOU 473 N ALA A 59 2592 3128 2600 35 -104 35 N ATOM 474 CA ALA A 59 -30.404 0.070 16.419 1.00 18.33 C ANISOU 474 CA ALA A 59 2169 2634 2162 61 -87 36 C ATOM 475 C ALA A 59 -30.228 0.892 15.154 1.00 16.86 C ANISOU 475 C ALA A 59 2015 2417 1973 84 -104 49 C ATOM 476 O ALA A 59 -29.727 2.025 15.224 1.00 20.74 O ANISOU 476 O ALA A 59 2517 2881 2482 113 -101 50 O ATOM 477 CB ALA A 59 -29.120 -0.740 16.682 1.00 19.57 C ANISOU 477 CB ALA A 59 2359 2762 2315 37 -61 41 C ATOM 478 N ILE A 60 -30.572 0.347 13.991 1.00 19.81 N ANISOU 478 N ILE A 60 2411 2792 2324 68 -124 61 N ATOM 479 CA ILE A 60 -30.388 1.171 12.793 1.00 17.88 C ANISOU 479 CA ILE A 60 2202 2521 2071 88 -141 78 C ATOM 480 C ILE A 60 -31.431 2.282 12.719 1.00 20.56 C ANISOU 480 C ILE A 60 2511 2874 2425 126 -174 79 C ATOM 481 O ILE A 60 -31.062 3.422 12.408 1.00 19.62 O ANISOU 481 O ILE A 60 2414 2722 2318 155 -180 91 O ATOM 482 CB ILE A 60 -30.343 0.301 11.525 1.00 21.68 C ANISOU 482 CB ILE A 60 2724 2999 2516 61 -152 88 C ATOM 483 CG1 ILE A 60 -28.911 -0.325 11.448 1.00 22.76 C ANISOU 483 CG1 ILE A 60 2900 3104 2644 43 -112 88 C ATOM 484 CG2 ILE A 60 -30.625 1.127 10.259 1.00 24.06 C ANISOU 484 CG2 ILE A 60 3054 3290 2798 80 -182 109 C ATOM 485 CD1 ILE A 60 -28.750 -1.451 10.337 1.00 20.60 C ANISOU 485 CD1 ILE A 60 2670 2826 2332 15 -114 87 C ATOM 486 N PRO A 61 -32.722 2.023 12.924 1.00 21.72 N ANISOU 486 N PRO A 61 2611 3066 2574 128 -198 70 N ATOM 487 CA PRO A 61 -33.643 3.160 13.073 1.00 24.51 C ANISOU 487 CA PRO A 61 2927 3434 2952 175 -225 65 C ATOM 488 C PRO A 61 -33.180 4.174 14.127 1.00 21.17 C ANISOU 488 C PRO A 61 2494 2989 2561 210 -203 49 C ATOM 489 O PRO A 61 -33.336 5.381 13.913 1.00 21.84 O ANISOU 489 O PRO A 61 2583 3048 2666 254 -223 52 O ATOM 490 CB PRO A 61 -34.972 2.480 13.448 1.00 22.41 C ANISOU 490 CB PRO A 61 2597 3231 2686 163 -241 51 C ATOM 491 CG PRO A 61 -34.907 1.165 12.690 1.00 20.15 C ANISOU 491 CG PRO A 61 2339 2952 2367 109 -248 62 C ATOM 492 CD PRO A 61 -33.451 0.729 12.931 1.00 25.07 C ANISOU 492 CD PRO A 61 3012 3532 2982 88 -206 64 C ATOM 493 N PHE A 62 -32.616 3.720 15.254 1.00 20.80 N ANISOU 493 N PHE A 62 2436 2949 2518 191 -166 31 N ATOM 494 CA PHE A 62 -32.123 4.662 16.259 1.00 20.01 C ANISOU 494 CA PHE A 62 2331 2829 2444 219 -148 12 C ATOM 495 C PHE A 62 -30.953 5.484 15.723 1.00 20.75 C ANISOU 495 C PHE A 62 2480 2857 2546 227 -145 29 C ATOM 496 O PHE A 62 -30.850 6.688 16.009 1.00 19.38 O ANISOU 496 O PHE A 62 2312 2654 2399 263 -152 21 O ATOM 497 CB PHE A 62 -31.687 3.922 17.531 1.00 18.33 C ANISOU 497 CB PHE A 62 2101 2638 2225 191 -112 -6 C ATOM 498 CG PHE A 62 -32.832 3.363 18.383 1.00 17.98 C ANISOU 498 CG PHE A 62 1996 2660 2175 185 -107 -25 C ATOM 499 CD1 PHE A 62 -34.167 3.474 17.979 1.00 21.53 C ANISOU 499 CD1 PHE A 62 2403 3150 2629 202 -133 -28 C ATOM 500 CD2 PHE A 62 -32.539 2.695 19.589 1.00 20.69 C ANISOU 500 CD2 PHE A 62 2325 3030 2508 157 -77 -37 C ATOM 501 CE1 PHE A 62 -35.202 2.919 18.759 1.00 21.66 C ANISOU 501 CE1 PHE A 62 2356 3234 2639 190 -123 -44 C ATOM 502 CE2 PHE A 62 -33.532 2.160 20.388 1.00 21.95 C ANISOU 502 CE2 PHE A 62 2430 3252 2656 144 -67 -50 C ATOM 503 CZ PHE A 62 -34.894 2.282 19.966 1.00 22.03 C ANISOU 503 CZ PHE A 62 2392 3307 2672 159 -88 -54 C ATOM 504 N ALA A 63 -30.023 4.835 14.998 1.00 20.26 N ANISOU 504 N ALA A 63 2460 2775 2464 192 -133 52 N ATOM 505 CA ALA A 63 -28.864 5.546 14.451 1.00 19.12 C ANISOU 505 CA ALA A 63 2364 2576 2325 192 -125 71 C ATOM 506 C ALA A 63 -29.286 6.588 13.419 1.00 21.05 C ANISOU 506 C ALA A 63 2633 2793 2572 220 -158 94 C ATOM 507 O ALA A 63 -28.693 7.663 13.338 1.00 19.53 O ANISOU 507 O ALA A 63 2467 2553 2399 234 -160 105 O ATOM 508 CB ALA A 63 -27.888 4.567 13.802 1.00 18.92 C ANISOU 508 CB ALA A 63 2371 2543 2274 152 -101 88 C ATOM 509 N ILE A 64 -30.271 6.256 12.580 1.00 22.97 N ANISOU 509 N ILE A 64 2870 3062 2795 224 -188 106 N ATOM 510 CA ILE A 64 -30.794 7.229 11.630 1.00 21.65 C ANISOU 510 CA ILE A 64 2725 2872 2629 255 -229 130 C ATOM 511 C ILE A 64 -31.361 8.431 12.381 1.00 25.95 C ANISOU 511 C ILE A 64 3243 3400 3216 306 -248 113 C ATOM 512 O ILE A 64 -31.111 9.597 12.024 1.00 22.72 O ANISOU 512 O ILE A 64 2867 2939 2825 332 -266 131 O ATOM 513 CB ILE A 64 -31.862 6.564 10.731 1.00 21.00 C ANISOU 513 CB ILE A 64 2632 2830 2517 250 -264 141 C ATOM 514 CG1 ILE A 64 -31.191 5.543 9.785 1.00 23.48 C ANISOU 514 CG1 ILE A 64 2989 3146 2785 203 -248 158 C ATOM 515 CG2 ILE A 64 -32.727 7.629 10.000 1.00 22.02 C ANISOU 515 CG2 ILE A 64 2766 2946 2655 294 -317 162 C ATOM 516 CD1 ILE A 64 -32.190 4.572 9.090 1.00 23.48 C ANISOU 516 CD1 ILE A 64 2977 3192 2753 185 -278 157 C ATOM 517 N THR A 65 -32.120 8.165 13.441 1.00 21.80 N ANISOU 517 N THR A 65 2659 2918 2707 322 -242 76 N ATOM 518 CA THR A 65 -32.723 9.238 14.216 1.00 19.84 C ANISOU 518 CA THR A 65 2381 2661 2497 377 -256 50 C ATOM 519 C THR A 65 -31.663 10.165 14.818 1.00 20.38 C ANISOU 519 C THR A 65 2484 2670 2591 384 -237 41 C ATOM 520 O THR A 65 -31.746 11.393 14.695 1.00 22.28 O ANISOU 520 O THR A 65 2744 2860 2860 425 -263 43 O ATOM 521 CB THR A 65 -33.600 8.598 15.294 1.00 25.06 C ANISOU 521 CB THR A 65 2972 3390 3161 382 -240 11 C ATOM 522 OG1 THR A 65 -34.579 7.794 14.630 1.00 27.64 O ANISOU 522 OG1 THR A 65 3268 3767 3467 370 -263 23 O ATOM 523 CG2 THR A 65 -34.310 9.656 16.117 1.00 24.71 C ANISOU 523 CG2 THR A 65 2890 3346 3153 444 -249 -25 C ATOM 524 N ILE A 66 -30.644 9.594 15.455 1.00 23.04 N ANISOU 524 N ILE A 66 2828 3007 2918 343 -198 32 N ATOM 525 CA ILE A 66 -29.678 10.433 16.145 1.00 22.93 C ANISOU 525 CA ILE A 66 2839 2944 2929 346 -184 19 C ATOM 526 C ILE A 66 -28.778 11.178 15.173 1.00 23.54 C ANISOU 526 C ILE A 66 2977 2956 3013 333 -194 58 C ATOM 527 O ILE A 66 -28.223 12.227 15.540 1.00 23.26 O ANISOU 527 O ILE A 66 2965 2865 3006 344 -198 52 O ATOM 528 CB ILE A 66 -28.865 9.596 17.152 1.00 20.07 C ANISOU 528 CB ILE A 66 2464 2607 2557 307 -144 -2 C ATOM 529 CG1 ILE A 66 -28.315 10.524 18.228 1.00 33.46 C ANISOU 529 CG1 ILE A 66 4164 4269 4279 322 -137 -33 C ATOM 530 CG2 ILE A 66 -27.708 8.711 16.467 1.00 16.08 C ANISOU 530 CG2 ILE A 66 1989 2095 2027 254 -121 32 C ATOM 531 CD1 ILE A 66 -27.676 9.794 19.444 1.00 39.73 C ANISOU 531 CD1 ILE A 66 4939 5095 5062 292 -105 -58 C ATOM 532 N SER A 67 -28.637 10.690 13.930 1.00 22.81 N ANISOU 532 N SER A 67 2910 2865 2890 308 -199 99 N ATOM 533 CA SER A 67 -27.869 11.447 12.932 1.00 21.10 C ANISOU 533 CA SER A 67 2752 2592 2673 294 -207 142 C ATOM 534 C SER A 67 -28.532 12.793 12.630 1.00 25.12 C ANISOU 534 C SER A 67 3281 3053 3211 342 -253 153 C ATOM 535 O SER A 67 -27.863 13.701 12.118 1.00 24.90 O ANISOU 535 O SER A 67 3303 2963 3194 333 -262 185 O ATOM 536 CB SER A 67 -27.687 10.661 11.608 1.00 21.36 C ANISOU 536 CB SER A 67 2812 2644 2659 261 -203 181 C ATOM 537 OG SER A 67 -28.912 10.509 10.865 1.00 23.76 O ANISOU 537 OG SER A 67 3109 2975 2945 286 -242 192 O ATOM 538 N THR A 68 -29.823 12.957 12.937 1.00 23.81 N ANISOU 538 N THR A 68 3077 2912 3059 393 -282 129 N ATOM 539 CA THR A 68 -30.485 14.219 12.616 1.00 28.43 C ANISOU 539 CA THR A 68 3680 3448 3675 447 -330 140 C ATOM 540 C THR A 68 -30.214 15.300 13.658 1.00 29.36 C ANISOU 540 C THR A 68 3803 3512 3841 477 -330 104 C ATOM 541 O THR A 68 -30.468 16.473 13.392 1.00 29.66 O ANISOU 541 O THR A 68 3872 3488 3911 518 -368 116 O ATOM 542 CB THR A 68 -32.024 14.047 12.462 1.00 30.19 C ANISOU 542 CB THR A 68 3853 3718 3899 498 -366 127 C ATOM 543 OG1 THR A 68 -32.648 13.770 13.729 1.00 27.13 O ANISOU 543 OG1 THR A 68 3401 3378 3530 524 -348 69 O ATOM 544 CG2 THR A 68 -32.362 12.929 11.481 1.00 25.73 C ANISOU 544 CG2 THR A 68 3282 3208 3286 465 -371 156 C ATOM 545 N GLY A 69 -29.745 14.941 14.845 1.00 22.93 N ANISOU 545 N GLY A 69 2961 2719 3032 461 -292 61 N ATOM 546 CA GLY A 69 -29.561 15.950 15.876 1.00 22.98 C ANISOU 546 CA GLY A 69 2973 2679 3078 491 -295 19 C ATOM 547 C GLY A 69 -30.864 16.545 16.361 1.00 29.00 C ANISOU 547 C GLY A 69 3700 3450 3869 568 -322 -21 C ATOM 548 O GLY A 69 -30.872 17.674 16.861 1.00 30.09 O ANISOU 548 O GLY A 69 3858 3528 4046 608 -340 -49 O ATOM 549 N PHE A 70 -31.970 15.802 16.244 1.00 30.26 N ANISOU 549 N PHE A 70 3803 3682 4010 589 -326 -29 N ATOM 550 CA PHE A 70 -33.296 16.295 16.640 1.00 29.99 C ANISOU 550 CA PHE A 70 3722 3669 4003 666 -350 -67 C ATOM 551 C PHE A 70 -33.361 16.643 18.131 1.00 30.50 C ANISOU 551 C PHE A 70 3758 3744 4087 695 -323 -138 C ATOM 552 O PHE A 70 -32.735 15.997 18.963 1.00 29.57 O ANISOU 552 O PHE A 70 3629 3659 3946 651 -281 -159 O ATOM 553 CB PHE A 70 -34.364 15.244 16.292 1.00 27.37 C ANISOU 553 CB PHE A 70 3328 3428 3645 667 -352 -61 C ATOM 554 CG PHE A 70 -34.436 14.095 17.265 1.00 30.73 C ANISOU 554 CG PHE A 70 3699 3936 4043 631 -303 -95 C ATOM 555 CD1 PHE A 70 -33.382 13.194 17.400 1.00 29.65 C ANISOU 555 CD1 PHE A 70 3584 3809 3874 560 -267 -80 C ATOM 556 CD2 PHE A 70 -35.569 13.924 18.065 1.00 32.11 C ANISOU 556 CD2 PHE A 70 3799 4178 4224 672 -294 -141 C ATOM 557 CE1 PHE A 70 -33.450 12.167 18.300 1.00 31.88 C ANISOU 557 CE1 PHE A 70 3822 4159 4132 529 -228 -107 C ATOM 558 CE2 PHE A 70 -35.637 12.900 18.960 1.00 31.62 C ANISOU 558 CE2 PHE A 70 3691 4189 4133 635 -250 -166 C ATOM 559 CZ PHE A 70 -34.602 12.022 19.096 1.00 31.43 C ANISOU 559 CZ PHE A 70 3696 4169 4078 564 -219 -148 C ATOM 560 N CYS A 71 -34.152 17.677 18.468 1.00 28.91 N ANISOU 560 N CYS A 71 3544 3514 3925 774 -349 -175 N ATOM 561 CA CYS A 71 -34.378 18.067 19.865 1.00 30.90 C ANISOU 561 CA CYS A 71 3767 3781 4192 812 -325 -250 C ATOM 562 C CYS A 71 -35.006 16.926 20.664 1.00 31.51 C ANISOU 562 C CYS A 71 3765 3972 4233 798 -281 -282 C ATOM 563 O CYS A 71 -36.003 16.341 20.235 1.00 34.93 O ANISOU 563 O CYS A 71 4144 4471 4658 812 -288 -270 O ATOM 564 CB CYS A 71 -35.311 19.289 19.912 1.00 31.68 C ANISOU 564 CB CYS A 71 3859 3837 4341 910 -363 -284 C ATOM 565 SG CYS A 71 -34.645 20.758 19.156 1.00 38.86 S ANISOU 565 SG CYS A 71 4865 4601 5298 931 -418 -250 S ATOM 566 N ALA A 72 -34.434 16.604 21.829 1.00 25.32 N ANISOU 566 N ALA A 72 2978 3215 3428 767 -239 -322 N ATOM 567 CA ALA A 72 -34.933 15.502 22.639 1.00 23.74 C ANISOU 567 CA ALA A 72 2712 3120 3190 744 -196 -346 C ATOM 568 C ALA A 72 -34.625 15.740 24.112 1.00 31.86 C ANISOU 568 C ALA A 72 3736 4164 4205 750 -160 -411 C ATOM 569 O ALA A 72 -33.651 16.428 24.448 1.00 32.94 O ANISOU 569 O ALA A 72 3931 4231 4355 741 -166 -424 O ATOM 570 CB ALA A 72 -34.289 14.153 22.209 1.00 23.38 C ANISOU 570 CB ALA A 72 2671 3109 3103 658 -177 -294 C ATOM 571 N ALA A 73 -35.441 15.153 25.003 1.00 30.16 N ANISOU 571 N ALA A 73 3454 4044 3963 759 -124 -449 N ATOM 572 CA ALA A 73 -35.013 15.079 26.396 1.00 28.56 C ANISOU 572 CA ALA A 73 3251 3870 3729 743 -86 -500 C ATOM 573 C ALA A 73 -33.730 14.269 26.470 1.00 28.29 C ANISOU 573 C ALA A 73 3259 3825 3665 658 -74 -461 C ATOM 574 O ALA A 73 -33.554 13.263 25.767 1.00 25.38 O ANISOU 574 O ALA A 73 2885 3478 3280 606 -74 -405 O ATOM 575 CB ALA A 73 -36.099 14.465 27.294 1.00 30.86 C ANISOU 575 CB ALA A 73 3462 4275 3988 757 -44 -538 C ATOM 576 N CYS A 74 -32.798 14.734 27.291 1.00 28.86 N ANISOU 576 N CYS A 74 3374 3861 3731 644 -68 -492 N ATOM 577 CA CYS A 74 -31.456 14.187 27.213 1.00 32.34 C ANISOU 577 CA CYS A 74 3857 4273 4156 572 -67 -453 C ATOM 578 C CYS A 74 -31.422 12.701 27.563 1.00 28.96 C ANISOU 578 C CYS A 74 3396 3927 3679 513 -36 -426 C ATOM 579 O CYS A 74 -30.681 11.935 26.941 1.00 25.06 O ANISOU 579 O CYS A 74 2921 3421 3179 460 -40 -373 O ATOM 580 CB CYS A 74 -30.501 14.981 28.109 1.00 37.00 C ANISOU 580 CB CYS A 74 4494 4814 4750 567 -71 -495 C ATOM 581 SG CYS A 74 -28.767 14.457 27.829 1.00 36.57 S ANISOU 581 SG CYS A 74 4488 4717 4689 483 -79 -441 S ATOM 582 N HIS A 75 -32.220 12.256 28.545 1.00 25.11 N ANISOU 582 N HIS A 75 2859 3524 3156 522 -4 -461 N ATOM 583 CA HIS A 75 -32.153 10.834 28.886 1.00 28.41 C ANISOU 583 CA HIS A 75 3254 4013 3529 461 23 -430 C ATOM 584 C HIS A 75 -32.842 9.938 27.849 1.00 30.08 C ANISOU 584 C HIS A 75 3432 4255 3744 443 19 -380 C ATOM 585 O HIS A 75 -32.411 8.791 27.639 1.00 25.39 O ANISOU 585 O HIS A 75 2844 3677 3127 384 25 -336 O ATOM 586 CB HIS A 75 -32.699 10.616 30.295 1.00 30.20 C ANISOU 586 CB HIS A 75 3445 4321 3709 464 60 -478 C ATOM 587 CG HIS A 75 -31.814 11.224 31.341 1.00 37.48 C ANISOU 587 CG HIS A 75 4408 5217 4615 463 62 -520 C ATOM 588 ND1 HIS A 75 -31.897 12.557 31.707 1.00 40.93 N ANISOU 588 ND1 HIS A 75 4864 5612 5075 521 52 -581 N ATOM 589 CD2 HIS A 75 -30.782 10.704 32.044 1.00 35.69 C ANISOU 589 CD2 HIS A 75 4212 4994 4355 410 66 -509 C ATOM 590 CE1 HIS A 75 -30.971 12.820 32.610 1.00 37.55 C ANISOU 590 CE1 HIS A 75 4475 5166 4625 500 51 -608 C ATOM 591 NE2 HIS A 75 -30.275 11.716 32.822 1.00 37.48 N ANISOU 591 NE2 HIS A 75 4472 5187 4582 433 58 -564 N ATOM 592 N GLY A 76 -33.865 10.432 27.153 1.00 28.15 N ANISOU 592 N GLY A 76 3157 4012 3527 492 3 -386 N ATOM 593 CA GLY A 76 -34.385 9.668 26.020 1.00 25.64 C ANISOU 593 CA GLY A 76 2818 3711 3215 472 -11 -336 C ATOM 594 C GLY A 76 -33.368 9.566 24.898 1.00 25.90 C ANISOU 594 C GLY A 76 2908 3669 3263 442 -38 -286 C ATOM 595 O GLY A 76 -33.228 8.519 24.254 1.00 27.30 O ANISOU 595 O GLY A 76 3087 3859 3424 395 -39 -242 O ATOM 596 N CYS A 77 -32.658 10.658 24.643 1.00 26.29 N ANISOU 596 N CYS A 77 3007 3640 3342 468 -59 -293 N ATOM 597 CA CYS A 77 -31.590 10.667 23.659 1.00 28.83 C ANISOU 597 CA CYS A 77 3383 3893 3676 437 -78 -247 C ATOM 598 C CYS A 77 -30.508 9.638 24.012 1.00 23.87 C ANISOU 598 C CYS A 77 2774 3276 3020 371 -57 -225 C ATOM 599 O CYS A 77 -29.990 8.944 23.135 1.00 22.53 O ANISOU 599 O CYS A 77 2624 3091 2844 334 -61 -181 O ATOM 600 CB CYS A 77 -31.005 12.083 23.575 1.00 33.31 C ANISOU 600 CB CYS A 77 3998 4377 4280 470 -101 -263 C ATOM 601 SG CYS A 77 -29.558 12.229 22.490 1.00 32.04 S ANISOU 601 SG CYS A 77 3904 4135 4133 425 -117 -207 S ATOM 602 N ALEU A 78 -30.201 9.510 25.297 0.38 24.23 N ANISOU 602 N ALEU A 78 2812 3350 3046 360 -35 -257 N ATOM 603 N BLEU A 78 -30.169 9.520 25.299 0.62 24.07 N ANISOU 603 N BLEU A 78 2793 3328 3025 359 -35 -257 N ATOM 604 CA ALEU A 78 -29.177 8.580 25.733 0.38 23.72 C ANISOU 604 CA ALEU A 78 2763 3293 2956 304 -20 -237 C ATOM 605 CA BLEU A 78 -29.162 8.555 25.723 0.62 23.74 C ANISOU 605 CA BLEU A 78 2766 3296 2958 303 -20 -236 C ATOM 606 C ALEU A 78 -29.580 7.145 25.437 0.38 22.35 C ANISOU 606 C ALEU A 78 2565 3171 2756 266 -8 -203 C ATOM 607 C BLEU A 78 -29.588 7.144 25.381 0.62 21.89 C ANISOU 607 C BLEU A 78 2507 3111 2698 267 -9 -202 C ATOM 608 O ALEU A 78 -28.736 6.324 25.070 0.38 23.87 O ANISOU 608 O ALEU A 78 2780 3348 2941 225 -7 -169 O ATOM 609 O BLEU A 78 -28.766 6.330 24.955 0.62 24.41 O ANISOU 609 O BLEU A 78 2849 3415 3011 226 -8 -166 O ATOM 610 CB ALEU A 78 -28.923 8.777 27.228 0.38 23.10 C ANISOU 610 CB ALEU A 78 2680 3241 2855 303 -4 -280 C ATOM 611 CB BLEU A 78 -28.905 8.646 27.239 0.62 23.21 C ANISOU 611 CB BLEU A 78 2693 3259 2866 299 -2 -277 C ATOM 612 CG ALEU A 78 -27.635 8.254 27.831 0.38 20.13 C ANISOU 612 CG ALEU A 78 2329 2856 2462 257 0 -268 C ATOM 613 CG BLEU A 78 -28.080 9.771 27.850 0.62 20.67 C ANISOU 613 CG BLEU A 78 2405 2887 2560 313 -13 -312 C ATOM 614 CD1ALEU A 78 -26.377 8.784 27.096 0.38 18.10 C ANISOU 614 CD1ALEU A 78 2116 2523 2240 245 -20 -245 C ATOM 615 CD1BLEU A 78 -28.136 9.633 29.389 0.62 16.80 C ANISOU 615 CD1BLEU A 78 1902 2451 2030 308 6 -355 C ATOM 616 CD2ALEU A 78 -27.639 8.710 29.287 0.38 19.24 C ANISOU 616 CD2ALEU A 78 2213 2771 2324 268 10 -319 C ATOM 617 CD2BLEU A 78 -26.659 9.792 27.321 0.62 17.39 C ANISOU 617 CD2BLEU A 78 2031 2411 2165 278 -28 -278 C ATOM 618 N PHE A 79 -30.867 6.823 25.588 1.00 20.04 N ANISOU 618 N PHE A 79 2226 2939 2450 279 1 -214 N ATOM 619 CA PHE A 79 -31.313 5.466 25.312 1.00 24.40 C ANISOU 619 CA PHE A 79 2756 3536 2979 237 9 -182 C ATOM 620 C PHE A 79 -31.155 5.148 23.833 1.00 21.86 C ANISOU 620 C PHE A 79 2457 3176 2672 226 -13 -142 C ATOM 621 O PHE A 79 -30.656 4.088 23.462 1.00 21.57 O ANISOU 621 O PHE A 79 2438 3135 2622 183 -11 -111 O ATOM 622 CB PHE A 79 -32.782 5.246 25.743 1.00 23.36 C ANISOU 622 CB PHE A 79 2562 3482 2833 249 22 -201 C ATOM 623 CG PHE A 79 -33.244 3.848 25.471 1.00 27.05 C ANISOU 623 CG PHE A 79 3009 3991 3278 198 27 -167 C ATOM 624 CD1 PHE A 79 -32.818 2.797 26.294 1.00 29.14 C ANISOU 624 CD1 PHE A 79 3281 4281 3510 146 47 -152 C ATOM 625 CD2 PHE A 79 -34.023 3.554 24.373 1.00 24.39 C ANISOU 625 CD2 PHE A 79 2653 3662 2954 197 7 -147 C ATOM 626 CE1 PHE A 79 -33.204 1.486 26.044 1.00 27.73 C ANISOU 626 CE1 PHE A 79 3090 4131 3314 95 49 -119 C ATOM 627 CE2 PHE A 79 -34.417 2.249 24.112 1.00 29.41 C ANISOU 627 CE2 PHE A 79 3275 4329 3570 144 8 -117 C ATOM 628 CZ PHE A 79 -34.000 1.195 24.943 1.00 32.38 C ANISOU 628 CZ PHE A 79 3661 4726 3917 92 30 -103 C ATOM 629 N ILE A 80 -31.576 6.063 22.967 1.00 18.89 N ANISOU 629 N ILE A 80 2084 2771 2322 267 -36 -144 N ATOM 630 CA AILE A 80 -31.417 5.969 21.507 0.45 20.70 C ANISOU 630 CA AILE A 80 2342 2962 2562 261 -60 -107 C ATOM 631 CA BILE A 80 -31.399 5.690 21.575 0.55 20.70 C ANISOU 631 CA BILE A 80 2339 2970 2556 251 -56 -105 C ATOM 632 C ILE A 80 -29.950 5.793 21.125 1.00 21.06 C ANISOU 632 C ILE A 80 2440 2953 2608 231 -55 -83 C ATOM 633 O ILE A 80 -29.603 5.106 20.162 1.00 21.94 O ANISOU 633 O ILE A 80 2574 3051 2710 205 -60 -52 O ATOM 634 CB AILE A 80 -32.008 7.243 20.860 0.45 20.05 C ANISOU 634 CB AILE A 80 2259 2850 2508 317 -88 -115 C ATOM 635 CB BILE A 80 -32.304 6.472 20.620 0.55 20.11 C ANISOU 635 CB BILE A 80 2255 2886 2502 294 -87 -102 C ATOM 636 CG1AILE A 80 -33.539 7.290 20.998 0.45 21.60 C ANISOU 636 CG1AILE A 80 2395 3106 2708 349 -97 -134 C ATOM 637 CG1BILE A 80 -31.998 7.969 20.683 0.55 19.03 C ANISOU 637 CG1BILE A 80 2141 2694 2396 343 -100 -120 C ATOM 638 CG2AILE A 80 -31.558 7.425 19.410 0.45 19.65 C ANISOU 638 CG2AILE A 80 2254 2747 2464 312 -113 -75 C ATOM 639 CG2BILE A 80 -33.769 6.079 20.887 0.55 22.43 C ANISOU 639 CG2BILE A 80 2482 3252 2787 304 -88 -116 C ATOM 640 CD1AILE A 80 -34.270 6.313 20.080 0.45 22.21 C ANISOU 640 CD1AILE A 80 2450 3218 2769 321 -112 -105 C ATOM 641 CD1BILE A 80 -32.617 8.720 19.529 0.55 22.40 C ANISOU 641 CD1BILE A 80 2576 3093 2843 381 -138 -103 C ATOM 642 N ALA A 81 -29.076 6.496 21.833 1.00 19.04 N ANISOU 642 N ALA A 81 2204 2667 2365 238 -48 -100 N ATOM 643 CA ALA A 81 -27.655 6.421 21.514 1.00 20.52 C ANISOU 643 CA ALA A 81 2432 2808 2557 211 -43 -79 C ATOM 644 C ALA A 81 -27.005 5.131 22.014 1.00 22.65 C ANISOU 644 C ALA A 81 2700 3102 2805 168 -24 -68 C ATOM 645 O ALA A 81 -26.054 4.650 21.394 1.00 24.77 O ANISOU 645 O ALA A 81 2994 3344 3075 144 -19 -42 O ATOM 646 CB ALA A 81 -26.921 7.619 22.135 1.00 25.74 C ANISOU 646 CB ALA A 81 3112 3427 3242 227 -47 -101 C ATOM 647 N CYS A 82 -27.446 4.593 23.152 1.00 18.37 N ANISOU 647 N CYS A 82 2129 2607 2243 160 -12 -86 N ATOM 648 CA CYS A 82 -26.715 3.525 23.827 1.00 21.24 C ANISOU 648 CA CYS A 82 2497 2986 2589 123 1 -75 C ATOM 649 C CYS A 82 -27.299 2.148 23.578 1.00 22.43 C ANISOU 649 C CYS A 82 2635 3169 2717 93 6 -53 C ATOM 650 O CYS A 82 -26.655 1.160 23.915 1.00 20.93 O ANISOU 650 O CYS A 82 2457 2980 2516 63 12 -37 O ATOM 651 CB CYS A 82 -26.666 3.768 25.356 1.00 21.11 C ANISOU 651 CB CYS A 82 2466 2999 2557 124 10 -104 C ATOM 652 SG CYS A 82 -25.681 5.220 25.802 1.00 24.54 S ANISOU 652 SG CYS A 82 2922 3385 3016 146 1 -132 S ATOM 653 N PHE A 83 -28.525 2.043 23.056 1.00 19.80 N ANISOU 653 N PHE A 83 2279 2863 2379 100 -1 -53 N ATOM 654 CA PHE A 83 -29.090 0.703 22.914 1.00 18.64 C ANISOU 654 CA PHE A 83 2123 2748 2213 64 1 -34 C ATOM 655 C PHE A 83 -28.184 -0.199 22.052 1.00 20.54 C ANISOU 655 C PHE A 83 2403 2948 2455 39 -2 -7 C ATOM 656 O PHE A 83 -28.058 -1.405 22.318 1.00 21.29 O ANISOU 656 O PHE A 83 2504 3051 2535 5 2 9 O ATOM 657 CB PHE A 83 -30.519 0.773 22.317 1.00 18.95 C ANISOU 657 CB PHE A 83 2128 2822 2251 73 -11 -37 C ATOM 658 CG PHE A 83 -31.162 -0.571 22.210 1.00 23.34 C ANISOU 658 CG PHE A 83 2671 3409 2787 28 -12 -19 C ATOM 659 CD1 PHE A 83 -31.520 -1.293 23.387 1.00 26.90 C ANISOU 659 CD1 PHE A 83 3097 3906 3217 -3 5 -19 C ATOM 660 CD2 PHE A 83 -31.380 -1.156 20.964 1.00 21.03 C ANISOU 660 CD2 PHE A 83 2396 3099 2494 12 -31 -1 C ATOM 661 CE1 PHE A 83 -32.100 -2.568 23.306 1.00 22.94 C ANISOU 661 CE1 PHE A 83 2589 3429 2700 -53 3 2 C ATOM 662 CE2 PHE A 83 -31.975 -2.422 20.882 1.00 21.50 C ANISOU 662 CE2 PHE A 83 2447 3182 2538 -34 -35 14 C ATOM 663 CZ PHE A 83 -32.297 -3.138 22.026 1.00 19.81 C ANISOU 663 CZ PHE A 83 2211 3007 2309 -68 -19 17 C ATOM 664 N VAL A 84 -27.559 0.361 21.008 1.00 18.75 N ANISOU 664 N VAL A 84 2204 2678 2243 56 -9 0 N ATOM 665 CA VAL A 84 -26.685 -0.460 20.158 1.00 20.42 C ANISOU 665 CA VAL A 84 2450 2856 2453 37 -6 20 C ATOM 666 C VAL A 84 -25.513 -1.037 20.957 1.00 17.72 C ANISOU 666 C VAL A 84 2119 2500 2114 23 7 25 C ATOM 667 O VAL A 84 -25.017 -2.128 20.642 1.00 18.13 O ANISOU 667 O VAL A 84 2191 2538 2162 4 10 39 O ATOM 668 CB VAL A 84 -26.169 0.343 18.959 1.00 17.59 C ANISOU 668 CB VAL A 84 2119 2460 2106 56 -9 28 C ATOM 669 CG1 VAL A 84 -25.282 1.506 19.426 1.00 17.63 C ANISOU 669 CG1 VAL A 84 2126 2439 2132 75 -3 20 C ATOM 670 CG2 VAL A 84 -25.371 -0.594 17.938 1.00 17.20 C ANISOU 670 CG2 VAL A 84 2104 2384 2048 39 -1 44 C ATOM 671 N LEU A 85 -25.060 -0.324 22.000 1.00 17.99 N ANISOU 671 N LEU A 85 2141 2538 2156 34 11 12 N ATOM 672 CA LEU A 85 -24.008 -0.861 22.861 1.00 21.84 C ANISOU 672 CA LEU A 85 2634 3019 2645 20 17 18 C ATOM 673 C LEU A 85 -24.475 -2.102 23.618 1.00 21.33 C ANISOU 673 C LEU A 85 2563 2982 2558 -7 16 28 C ATOM 674 O LEU A 85 -23.649 -2.962 23.977 1.00 21.30 O ANISOU 674 O LEU A 85 2573 2965 2555 -21 15 43 O ATOM 675 CB LEU A 85 -23.569 0.210 23.863 1.00 20.74 C ANISOU 675 CB LEU A 85 2484 2883 2514 34 16 -2 C ATOM 676 CG LEU A 85 -23.189 1.536 23.199 1.00 20.33 C ANISOU 676 CG LEU A 85 2441 2798 2486 57 13 -11 C ATOM 677 CD1 LEU A 85 -22.797 2.551 24.282 1.00 20.77 C ANISOU 677 CD1 LEU A 85 2489 2853 2549 66 9 -36 C ATOM 678 CD2 LEU A 85 -22.028 1.335 22.185 1.00 18.60 C ANISOU 678 CD2 LEU A 85 2243 2541 2285 51 20 9 C ATOM 679 N VAL A 86 -25.767 -2.160 23.956 1.00 20.72 N ANISOU 679 N VAL A 86 2463 2947 2462 -16 15 22 N ATOM 680 CA VAL A 86 -26.331 -3.377 24.550 1.00 22.47 C ANISOU 680 CA VAL A 86 2680 3197 2662 -51 15 37 C ATOM 681 C VAL A 86 -26.187 -4.541 23.576 1.00 21.20 C ANISOU 681 C VAL A 86 2546 3004 2505 -71 8 58 C ATOM 682 O VAL A 86 -25.752 -5.641 23.946 1.00 19.41 O ANISOU 682 O VAL A 86 2338 2763 2273 -94 4 77 O ATOM 683 CB VAL A 86 -27.810 -3.158 24.929 1.00 20.95 C ANISOU 683 CB VAL A 86 2450 3060 2450 -58 20 26 C ATOM 684 CG1 VAL A 86 -28.407 -4.462 25.478 1.00 21.49 C ANISOU 684 CG1 VAL A 86 2513 3156 2495 -105 21 49 C ATOM 685 CG2 VAL A 86 -27.999 -1.953 25.889 1.00 19.28 C ANISOU 685 CG2 VAL A 86 2213 2879 2234 -31 30 -3 C ATOM 686 N LEU A 87 -26.536 -4.309 22.299 1.00 17.12 N ANISOU 686 N LEU A 87 2036 2472 1996 -60 3 54 N ATOM 687 CA LEU A 87 -26.500 -5.399 21.322 1.00 17.81 C ANISOU 687 CA LEU A 87 2153 2532 2082 -79 -5 66 C ATOM 688 C LEU A 87 -25.063 -5.824 21.016 1.00 19.18 C ANISOU 688 C LEU A 87 2360 2658 2271 -68 1 72 C ATOM 689 O LEU A 87 -24.790 -7.009 20.806 1.00 22.76 O ANISOU 689 O LEU A 87 2838 3086 2723 -85 -4 82 O ATOM 690 CB LEU A 87 -27.204 -4.976 20.021 1.00 19.76 C ANISOU 690 CB LEU A 87 2401 2779 2327 -69 -14 59 C ATOM 691 CG LEU A 87 -28.683 -4.531 20.155 1.00 21.11 C ANISOU 691 CG LEU A 87 2531 2999 2489 -74 -24 51 C ATOM 692 CD1 LEU A 87 -29.245 -4.091 18.750 1.00 18.28 C ANISOU 692 CD1 LEU A 87 2179 2635 2129 -60 -41 48 C ATOM 693 CD2 LEU A 87 -29.512 -5.642 20.797 1.00 21.47 C ANISOU 693 CD2 LEU A 87 2562 3075 2520 -119 -28 62 C ATOM 694 N ALA A 88 -24.145 -4.861 20.928 1.00 20.04 N ANISOU 694 N ALA A 88 2467 2753 2395 -39 11 65 N ATOM 695 CA ALA A 88 -22.748 -5.205 20.720 1.00 19.61 C ANISOU 695 CA ALA A 88 2432 2662 2358 -28 19 70 C ATOM 696 C ALA A 88 -22.213 -5.988 21.900 1.00 21.76 C ANISOU 696 C ALA A 88 2702 2933 2632 -38 13 81 C ATOM 697 O ALA A 88 -21.437 -6.936 21.725 1.00 19.39 O ANISOU 697 O ALA A 88 2422 2602 2342 -37 12 90 O ATOM 698 CB ALA A 88 -21.927 -3.923 20.521 1.00 16.72 C ANISOU 698 CB ALA A 88 2056 2287 2008 -3 30 62 C ATOM 699 N GLN A 89 -22.586 -5.579 23.121 1.00 19.37 N ANISOU 699 N GLN A 89 2378 2663 2319 -46 8 81 N ATOM 700 CA GLN A 89 -22.134 -6.301 24.310 1.00 17.63 C ANISOU 700 CA GLN A 89 2159 2446 2093 -60 -1 97 C ATOM 701 C GLN A 89 -22.694 -7.719 24.352 1.00 20.23 C ANISOU 701 C GLN A 89 2509 2767 2410 -90 -11 117 C ATOM 702 O GLN A 89 -21.979 -8.672 24.713 1.00 20.53 O ANISOU 702 O GLN A 89 2566 2778 2455 -93 -23 135 O ATOM 703 CB GLN A 89 -22.546 -5.552 25.575 1.00 16.02 C ANISOU 703 CB GLN A 89 1931 2286 1870 -65 -2 89 C ATOM 704 CG GLN A 89 -21.691 -6.022 26.769 1.00 21.32 C ANISOU 704 CG GLN A 89 2607 2957 2536 -72 -15 105 C ATOM 705 CD GLN A 89 -20.203 -5.752 26.528 1.00 22.42 C ANISOU 705 CD GLN A 89 2748 3064 2708 -46 -19 103 C ATOM 706 OE1 GLN A 89 -19.828 -4.688 26.017 1.00 23.46 O ANISOU 706 OE1 GLN A 89 2868 3188 2857 -27 -10 84 O ATOM 707 NE2 GLN A 89 -19.345 -6.736 26.869 1.00 20.28 N ANISOU 707 NE2 GLN A 89 2490 2770 2446 -46 -35 125 N ATOM 708 N SER A 90 -23.982 -7.877 24.016 1.00 21.27 N ANISOU 708 N SER A 90 2636 2922 2525 -112 -11 115 N ATOM 709 CA SER A 90 -24.548 -9.214 23.935 1.00 21.25 C ANISOU 709 CA SER A 90 2655 2906 2513 -148 -23 134 C ATOM 710 C SER A 90 -23.793 -10.055 22.912 1.00 21.50 C ANISOU 710 C SER A 90 2724 2879 2564 -136 -28 134 C ATOM 711 O SER A 90 -23.554 -11.251 23.139 1.00 20.69 O ANISOU 711 O SER A 90 2651 2744 2466 -152 -42 153 O ATOM 712 CB SER A 90 -26.039 -9.151 23.574 1.00 19.43 C ANISOU 712 CB SER A 90 2406 2711 2265 -175 -23 129 C ATOM 713 OG SER A 90 -26.578 -10.476 23.497 1.00 22.92 O ANISOU 713 OG SER A 90 2870 3138 2700 -218 -37 149 O ATOM 714 N SER A 91 -23.418 -9.450 21.779 1.00 20.43 N ANISOU 714 N SER A 91 2592 2729 2441 -107 -17 114 N ATOM 715 CA SER A 91 -22.698 -10.208 20.753 1.00 20.83 C ANISOU 715 CA SER A 91 2678 2731 2506 -92 -16 108 C ATOM 716 C SER A 91 -21.374 -10.703 21.288 1.00 20.51 C ANISOU 716 C SER A 91 2646 2658 2487 -70 -17 117 C ATOM 717 O SER A 91 -20.970 -11.843 21.027 1.00 22.00 O ANISOU 717 O SER A 91 2867 2804 2687 -67 -25 120 O ATOM 718 CB SER A 91 -22.439 -9.340 19.506 1.00 18.90 C ANISOU 718 CB SER A 91 2433 2484 2263 -65 1 87 C ATOM 719 OG SER A 91 -23.646 -8.955 18.922 1.00 21.44 O ANISOU 719 OG SER A 91 2750 2832 2565 -82 -5 80 O ATOM 720 N ILE A 92 -20.660 -9.827 21.996 1.00 20.98 N ANISOU 720 N ILE A 92 2677 2738 2556 -51 -10 118 N ATOM 721 CA ILE A 92 -19.389 -10.190 22.610 1.00 20.84 C ANISOU 721 CA ILE A 92 2658 2698 2561 -30 -17 128 C ATOM 722 C ILE A 92 -19.531 -11.384 23.559 1.00 20.51 C ANISOU 722 C ILE A 92 2637 2641 2515 -50 -42 155 C ATOM 723 O ILE A 92 -18.716 -12.313 23.529 1.00 21.36 O ANISOU 723 O ILE A 92 2765 2706 2644 -32 -53 164 O ATOM 724 CB ILE A 92 -18.807 -8.963 23.325 1.00 20.39 C ANISOU 724 CB ILE A 92 2566 2672 2511 -17 -12 125 C ATOM 725 CG1 ILE A 92 -18.178 -8.043 22.248 1.00 26.40 C ANISOU 725 CG1 ILE A 92 3315 3428 3288 8 12 105 C ATOM 726 CG2 ILE A 92 -17.741 -9.415 24.330 1.00 20.48 C ANISOU 726 CG2 ILE A 92 2571 2672 2537 -5 -30 142 C ATOM 727 CD1 ILE A 92 -18.011 -6.651 22.712 1.00 37.74 C ANISOU 727 CD1 ILE A 92 4722 4892 4726 11 16 98 C ATOM 728 N PHE A 93 -20.524 -11.353 24.448 1.00 20.67 N ANISOU 728 N PHE A 93 2651 2696 2508 -87 -52 171 N ATOM 729 CA PHE A 93 -20.752 -12.491 25.339 1.00 25.90 C ANISOU 729 CA PHE A 93 3337 3344 3159 -116 -75 203 C ATOM 730 C PHE A 93 -21.052 -13.761 24.552 1.00 25.68 C ANISOU 730 C PHE A 93 3351 3265 3141 -129 -86 207 C ATOM 731 O PHE A 93 -20.560 -14.845 24.895 1.00 21.63 O ANISOU 731 O PHE A 93 2870 2707 2642 -128 -108 229 O ATOM 732 CB PHE A 93 -21.913 -12.187 26.306 1.00 21.30 C ANISOU 732 CB PHE A 93 2737 2817 2539 -159 -75 216 C ATOM 733 CG PHE A 93 -21.560 -11.227 27.407 1.00 26.12 C ANISOU 733 CG PHE A 93 3318 3471 3134 -150 -73 216 C ATOM 734 CD1 PHE A 93 -20.358 -11.343 28.099 1.00 35.96 C ANISOU 734 CD1 PHE A 93 4567 4702 4393 -128 -90 229 C ATOM 735 CD2 PHE A 93 -22.407 -10.182 27.737 1.00 22.81 C ANISOU 735 CD2 PHE A 93 2867 3108 2690 -160 -56 198 C ATOM 736 CE1 PHE A 93 -20.042 -10.451 29.145 1.00 37.31 C ANISOU 736 CE1 PHE A 93 4715 4915 4547 -124 -92 225 C ATOM 737 CE2 PHE A 93 -22.090 -9.279 28.776 1.00 24.96 C ANISOU 737 CE2 PHE A 93 3118 3420 2947 -151 -54 190 C ATOM 738 CZ PHE A 93 -20.916 -9.407 29.468 1.00 30.09 C ANISOU 738 CZ PHE A 93 3775 4055 3605 -136 -73 203 C ATOM 739 N SER A 94 -21.864 -13.659 23.491 1.00 20.21 N ANISOU 739 N SER A 94 2663 2574 2441 -141 -75 186 N ATOM 740 CA SER A 94 -22.127 -14.870 22.705 1.00 24.89 C ANISOU 740 CA SER A 94 3301 3115 3042 -156 -88 185 C ATOM 741 C SER A 94 -20.855 -15.392 22.048 1.00 21.99 C ANISOU 741 C SER A 94 2959 2689 2706 -107 -86 170 C ATOM 742 O SER A 94 -20.624 -16.607 22.014 1.00 23.59 O ANISOU 742 O SER A 94 3204 2836 2924 -108 -106 178 O ATOM 743 CB SER A 94 -23.199 -14.609 21.647 1.00 23.28 C ANISOU 743 CB SER A 94 3096 2928 2822 -177 -80 162 C ATOM 744 OG SER A 94 -24.459 -14.407 22.291 1.00 27.46 O ANISOU 744 OG SER A 94 3601 3507 3326 -225 -85 178 O ATOM 745 N LEU A 95 -20.051 -14.496 21.477 1.00 20.93 N ANISOU 745 N LEU A 95 2801 2569 2584 -64 -62 146 N ATOM 746 CA LEU A 95 -18.810 -14.923 20.833 1.00 23.47 C ANISOU 746 CA LEU A 95 3137 2847 2935 -15 -53 128 C ATOM 747 C LEU A 95 -17.865 -15.567 21.833 1.00 22.68 C ANISOU 747 C LEU A 95 3038 2719 2861 6 -74 152 C ATOM 748 O LEU A 95 -17.216 -16.575 21.516 1.00 24.48 O ANISOU 748 O LEU A 95 3296 2891 3115 35 -84 147 O ATOM 749 CB LEU A 95 -18.104 -13.740 20.157 1.00 21.46 C ANISOU 749 CB LEU A 95 2848 2620 2686 19 -20 105 C ATOM 750 CG LEU A 95 -18.854 -13.178 18.948 1.00 24.93 C ANISOU 750 CG LEU A 95 3294 3077 3100 8 -1 81 C ATOM 751 CD1 LEU A 95 -18.325 -11.753 18.549 1.00 25.47 C ANISOU 751 CD1 LEU A 95 3325 3182 3169 29 28 70 C ATOM 752 CD2 LEU A 95 -18.756 -14.192 17.750 1.00 20.41 C ANISOU 752 CD2 LEU A 95 2769 2458 2528 21 4 55 C ATOM 753 N LEU A 96 -17.759 -15.001 23.043 1.00 20.64 N ANISOU 753 N LEU A 96 2748 2497 2595 -4 -85 177 N ATOM 754 CA LEU A 96 -16.874 -15.605 24.035 1.00 24.95 C ANISOU 754 CA LEU A 96 3297 3020 3162 15 -113 205 C ATOM 755 C LEU A 96 -17.399 -16.969 24.476 1.00 24.26 C ANISOU 755 C LEU A 96 3259 2886 3072 -14 -146 235 C ATOM 756 O LEU A 96 -16.618 -17.896 24.704 1.00 25.60 O ANISOU 756 O LEU A 96 3452 3003 3270 15 -170 249 O ATOM 757 CB LEU A 96 -16.707 -14.666 25.237 1.00 25.86 C ANISOU 757 CB LEU A 96 3373 3190 3264 5 -119 223 C ATOM 758 CG LEU A 96 -15.835 -15.164 26.406 1.00 32.30 C ANISOU 758 CG LEU A 96 4188 3993 4092 20 -155 256 C ATOM 759 CD1 LEU A 96 -14.405 -15.536 25.970 1.00 32.30 C ANISOU 759 CD1 LEU A 96 4177 3954 4141 80 -158 245 C ATOM 760 CD2 LEU A 96 -15.787 -14.136 27.572 1.00 31.05 C ANISOU 760 CD2 LEU A 96 3994 3894 3909 4 -161 267 C ATOM 761 N ALA A 97 -18.726 -17.122 24.565 1.00 23.89 N ANISOU 761 N ALA A 97 3229 2855 2993 -70 -148 245 N ATOM 762 CA ALA A 97 -19.320 -18.395 24.954 1.00 27.27 C ANISOU 762 CA ALA A 97 3707 3239 3417 -110 -179 277 C ATOM 763 C ALA A 97 -19.067 -19.474 23.902 1.00 27.32 C ANISOU 763 C ALA A 97 3762 3167 3452 -88 -187 256 C ATOM 764 O ALA A 97 -18.759 -20.619 24.244 1.00 26.44 O ANISOU 764 O ALA A 97 3694 2992 3360 -85 -219 280 O ATOM 765 CB ALA A 97 -20.828 -18.230 25.171 1.00 25.78 C ANISOU 765 CB ALA A 97 3514 3093 3188 -179 -174 289 C ATOM 766 N ILE A 98 -19.209 -19.124 22.615 1.00 26.90 N ANISOU 766 N ILE A 98 3707 3116 3399 -73 -160 211 N ATOM 767 CA ILE A 98 -18.926 -20.063 21.535 1.00 20.22 C ANISOU 767 CA ILE A 98 2908 2200 2575 -48 -162 181 C ATOM 768 C ILE A 98 -17.483 -20.541 21.616 1.00 24.56 C ANISOU 768 C ILE A 98 3462 2703 3167 21 -168 176 C ATOM 769 O ILE A 98 -17.204 -21.733 21.475 1.00 29.50 O ANISOU 769 O ILE A 98 4138 3254 3819 38 -192 175 O ATOM 770 CB ILE A 98 -19.253 -19.419 20.172 1.00 20.18 C ANISOU 770 CB ILE A 98 2894 2220 2554 -41 -129 134 C ATOM 771 CG1 ILE A 98 -20.780 -19.227 20.099 1.00 23.01 C ANISOU 771 CG1 ILE A 98 3253 2613 2876 -110 -136 141 C ATOM 772 CG2 ILE A 98 -18.700 -20.313 19.037 1.00 21.31 C ANISOU 772 CG2 ILE A 98 3085 2295 2717 -2 -126 93 C ATOM 773 CD1 ILE A 98 -21.363 -18.356 18.974 1.00 23.68 C ANISOU 773 CD1 ILE A 98 3321 2740 2935 -115 -111 107 C ATOM 774 N ALA A 99 -16.553 -19.630 21.903 1.00 25.93 N ANISOU 774 N ALA A 99 3583 2919 3352 62 -150 173 N ATOM 775 CA ALA A 99 -15.149 -20.018 21.975 1.00 24.59 C ANISOU 775 CA ALA A 99 3404 2714 3226 129 -155 168 C ATOM 776 C ALA A 99 -14.925 -20.990 23.133 1.00 27.41 C ANISOU 776 C ALA A 99 3788 3025 3601 127 -204 215 C ATOM 777 O ALA A 99 -14.273 -22.034 22.966 1.00 24.96 O ANISOU 777 O ALA A 99 3511 2644 3327 170 -225 211 O ATOM 778 CB ALA A 99 -14.265 -18.760 22.113 1.00 21.88 C ANISOU 778 CB ALA A 99 2992 2434 2890 161 -127 160 C ATOM 779 N ILE A 100 -15.459 -20.652 24.320 1.00 26.27 N ANISOU 779 N ILE A 100 3632 2921 3428 79 -225 260 N ATOM 780 CA ILE A 100 -15.292 -21.487 25.510 1.00 27.78 C ANISOU 780 CA ILE A 100 3851 3078 3627 70 -273 313 C ATOM 781 C ILE A 100 -15.947 -22.849 25.303 1.00 28.18 C ANISOU 781 C ILE A 100 3975 3048 3682 41 -302 327 C ATOM 782 O ILE A 100 -15.368 -23.892 25.644 1.00 27.85 O ANISOU 782 O ILE A 100 3973 2935 3674 69 -341 350 O ATOM 783 CB ILE A 100 -15.834 -20.745 26.756 1.00 26.73 C ANISOU 783 CB ILE A 100 3691 3016 3451 18 -281 353 C ATOM 784 CG1 ILE A 100 -14.901 -19.566 27.087 1.00 28.94 C ANISOU 784 CG1 ILE A 100 3906 3356 3736 56 -266 340 C ATOM 785 CG2 ILE A 100 -15.982 -21.694 27.980 1.00 27.58 C ANISOU 785 CG2 ILE A 100 3841 3091 3548 -13 -332 416 C ATOM 786 CD1 ILE A 100 -15.489 -18.548 28.070 1.00 32.90 C ANISOU 786 CD1 ILE A 100 4375 3935 4189 9 -261 359 C ATOM 787 N ASP A 101 -17.158 -22.858 24.727 1.00 25.32 N ANISOU 787 N ASP A 101 3634 2694 3291 -16 -286 314 N ATOM 788 CA ASP A 101 -17.825 -24.106 24.394 1.00 26.52 C ANISOU 788 CA ASP A 101 3856 2770 3450 -51 -313 321 C ATOM 789 C ASP A 101 -16.930 -25.005 23.540 1.00 32.48 C ANISOU 789 C ASP A 101 4651 3436 4254 18 -321 284 C ATOM 790 O ASP A 101 -16.767 -26.197 23.830 1.00 31.41 O ANISOU 790 O ASP A 101 4574 3215 4145 22 -363 308 O ATOM 791 CB ASP A 101 -19.135 -23.803 23.666 1.00 23.83 C ANISOU 791 CB ASP A 101 3518 2462 3075 -113 -290 298 C ATOM 792 CG ASP A 101 -19.867 -25.061 23.255 1.00 30.51 C ANISOU 792 CG ASP A 101 4436 3230 3928 -157 -320 301 C ATOM 793 OD1 ASP A 101 -20.396 -25.723 24.150 1.00 33.78 O ANISOU 793 OD1 ASP A 101 4880 3622 4333 -213 -352 354 O ATOM 794 OD2 ASP A 101 -19.868 -25.418 22.058 1.00 33.15 O ANISOU 794 OD2 ASP A 101 4800 3522 4275 -137 -311 251 O ATOM 795 N ARG A 102 -16.336 -24.448 22.481 1.00 29.44 N ANISOU 795 N ARG A 102 4236 3069 3880 73 -281 226 N ATOM 796 CA ARG A 102 -15.497 -25.281 21.622 1.00 27.43 C ANISOU 796 CA ARG A 102 4017 2737 3668 142 -282 184 C ATOM 797 C ARG A 102 -14.215 -25.718 22.339 1.00 27.02 C ANISOU 797 C ARG A 102 3955 2648 3663 211 -309 206 C ATOM 798 O ARG A 102 -13.731 -26.820 22.089 1.00 30.50 O ANISOU 798 O ARG A 102 4444 3000 4144 256 -334 194 O ATOM 799 CB ARG A 102 -15.164 -24.553 20.312 1.00 29.50 C ANISOU 799 CB ARG A 102 4248 3037 3924 181 -227 119 C ATOM 800 CG ARG A 102 -16.364 -24.320 19.339 1.00 33.73 C ANISOU 800 CG ARG A 102 4806 3593 4417 124 -208 88 C ATOM 801 CD ARG A 102 -16.990 -25.651 18.837 1.00 38.68 C ANISOU 801 CD ARG A 102 5518 4128 5049 99 -239 73 C ATOM 802 NE ARG A 102 -17.905 -26.247 19.825 1.00 39.49 N ANISOU 802 NE ARG A 102 5653 4207 5145 24 -285 131 N ATOM 803 CZ ARG A 102 -18.125 -27.548 19.977 1.00 42.71 C ANISOU 803 CZ ARG A 102 6133 4519 5574 6 -328 145 C ATOM 804 NH1 ARG A 102 -18.968 -27.987 20.915 1.00 39.36 N ANISOU 804 NH1 ARG A 102 5733 4084 5139 -70 -365 204 N ATOM 805 NH2 ARG A 102 -17.488 -28.415 19.198 1.00 48.80 N ANISOU 805 NH2 ARG A 102 6956 5207 6380 64 -334 99 N ATOM 806 N TYR A 103 -13.667 -24.884 23.233 1.00 28.36 N ANISOU 806 N TYR A 103 4063 2883 3831 222 -308 237 N ATOM 807 CA TYR A 103 -12.517 -25.311 24.022 1.00 30.94 C ANISOU 807 CA TYR A 103 4377 3178 4199 281 -344 265 C ATOM 808 C TYR A 103 -12.876 -26.488 24.937 1.00 33.23 C ANISOU 808 C TYR A 103 4735 3394 4497 252 -407 324 C ATOM 809 O TYR A 103 -12.116 -27.469 25.034 1.00 32.24 O ANISOU 809 O TYR A 103 4642 3188 4420 310 -443 330 O ATOM 810 CB TYR A 103 -11.944 -24.136 24.831 1.00 30.14 C ANISOU 810 CB TYR A 103 4198 3166 4088 287 -336 286 C ATOM 811 CG TYR A 103 -10.794 -24.572 25.717 1.00 33.87 C ANISOU 811 CG TYR A 103 4655 3613 4602 344 -381 320 C ATOM 812 CD1 TYR A 103 -9.586 -24.978 25.165 1.00 39.67 C ANISOU 812 CD1 TYR A 103 5370 4309 5394 435 -378 287 C ATOM 813 CD2 TYR A 103 -10.940 -24.665 27.093 1.00 40.36 C ANISOU 813 CD2 TYR A 103 5485 4445 5404 309 -429 386 C ATOM 814 CE1 TYR A 103 -8.536 -25.429 25.956 1.00 41.01 C ANISOU 814 CE1 TYR A 103 5522 4452 5606 492 -425 318 C ATOM 815 CE2 TYR A 103 -9.892 -25.125 27.905 1.00 39.80 C ANISOU 815 CE2 TYR A 103 5404 4347 5370 362 -479 421 C ATOM 816 CZ TYR A 103 -8.689 -25.495 27.324 1.00 42.84 C ANISOU 816 CZ TYR A 103 5764 4695 5819 455 -479 387 C ATOM 817 OH TYR A 103 -7.641 -25.966 28.107 1.00 42.55 O ANISOU 817 OH TYR A 103 5713 4632 5824 513 -533 421 O ATOM 818 N ILE A 104 -14.038 -26.430 25.591 1.00 34.39 N ANISOU 818 N ILE A 104 4905 3565 4598 163 -420 367 N ATOM 819 CA ILE A 104 -14.448 -27.540 26.460 1.00 35.10 C ANISOU 819 CA ILE A 104 5063 3586 4688 122 -478 430 C ATOM 820 C ILE A 104 -14.609 -28.812 25.640 1.00 36.42 C ANISOU 820 C ILE A 104 5308 3640 4890 135 -497 406 C ATOM 821 O ILE A 104 -14.212 -29.906 26.071 1.00 34.18 O ANISOU 821 O ILE A 104 5080 3266 4643 159 -549 439 O ATOM 822 CB ILE A 104 -15.748 -27.202 27.220 1.00 34.21 C ANISOU 822 CB ILE A 104 4954 3530 4514 17 -478 477 C ATOM 823 CG1 ILE A 104 -15.528 -26.080 28.238 1.00 35.85 C ANISOU 823 CG1 ILE A 104 5097 3839 4687 8 -469 504 C ATOM 824 CG2 ILE A 104 -16.319 -28.466 27.908 1.00 39.16 C ANISOU 824 CG2 ILE A 104 5661 4079 5139 -38 -532 540 C ATOM 825 CD1 ILE A 104 -16.837 -25.401 28.661 1.00 36.77 C ANISOU 825 CD1 ILE A 104 5196 4035 4739 -83 -444 523 C ATOM 826 N ALA A 105 -15.162 -28.679 24.432 1.00 33.58 N ANISOU 826 N ALA A 105 4957 3282 4521 122 -459 346 N ATOM 827 CA ALA A 105 -15.403 -29.842 23.583 1.00 31.68 C ANISOU 827 CA ALA A 105 4794 2935 4306 127 -476 315 C ATOM 828 C ALA A 105 -14.090 -30.507 23.168 1.00 34.83 C ANISOU 828 C ALA A 105 5207 3257 4768 237 -487 279 C ATOM 829 O ALA A 105 -13.994 -31.733 23.149 1.00 39.42 O ANISOU 829 O ALA A 105 5864 3727 5386 254 -531 286 O ATOM 830 CB ALA A 105 -16.215 -29.430 22.356 1.00 31.05 C ANISOU 830 CB ALA A 105 4713 2887 4196 94 -432 254 C ATOM 831 N ILE A 106 -13.049 -29.724 22.880 1.00 37.01 N ANISOU 831 N ILE A 106 5412 3591 5061 314 -450 244 N ATOM 832 CA ILE A 106 -11.804 -30.355 22.452 1.00 41.76 C ANISOU 832 CA ILE A 106 6018 4126 5724 422 -456 206 C ATOM 833 C ILE A 106 -10.891 -30.755 23.614 1.00 39.86 C ANISOU 833 C ILE A 106 5765 3855 5524 471 -509 263 C ATOM 834 O ILE A 106 -10.052 -31.659 23.458 1.00 35.76 O ANISOU 834 O ILE A 106 5274 3250 5063 553 -537 248 O ATOM 835 CB ILE A 106 -11.039 -29.454 21.468 1.00 41.57 C ANISOU 835 CB ILE A 106 5921 4171 5702 485 -389 137 C ATOM 836 CG1 ILE A 106 -10.027 -30.298 20.690 1.00 44.96 C ANISOU 836 CG1 ILE A 106 6371 4523 6190 590 -385 79 C ATOM 837 CG2 ILE A 106 -10.327 -28.282 22.200 1.00 36.04 C ANISOU 837 CG2 ILE A 106 5124 3572 4998 502 -373 165 C ATOM 838 CD1 ILE A 106 -9.422 -29.544 19.578 1.00 52.54 C ANISOU 838 CD1 ILE A 106 7272 5546 7144 641 -313 8 C ATOM 839 N ALA A 107 -11.044 -30.136 24.781 1.00 37.67 N ANISOU 839 N ALA A 107 5452 3644 5217 424 -528 328 N ATOM 840 CA ALA A 107 -10.167 -30.408 25.906 1.00 39.56 C ANISOU 840 CA ALA A 107 5676 3868 5487 467 -581 385 C ATOM 841 C ALA A 107 -10.707 -31.541 26.769 1.00 45.05 C ANISOU 841 C ALA A 107 6459 4473 6183 422 -652 456 C ATOM 842 O ALA A 107 -9.940 -32.389 27.242 1.00 46.31 O ANISOU 842 O ALA A 107 6647 4555 6392 482 -707 486 O ATOM 843 CB ALA A 107 -9.979 -29.140 26.750 1.00 40.11 C ANISOU 843 CB ALA A 107 5664 4056 5520 442 -568 416 C ATOM 844 N ILE A 108 -12.014 -31.592 26.977 1.00 39.35 N ANISOU 844 N ILE A 108 5781 3759 5410 316 -652 487 N ATOM 845 CA ILE A 108 -12.568 -32.665 27.789 1.00 44.98 C ANISOU 845 CA ILE A 108 6580 4389 6121 261 -716 560 C ATOM 846 C ILE A 108 -13.803 -33.240 27.115 1.00 40.65 C ANISOU 846 C ILE A 108 6101 3790 5553 182 -708 544 C ATOM 847 O ILE A 108 -14.903 -33.132 27.666 1.00 41.94 O ANISOU 847 O ILE A 108 6281 3989 5665 78 -711 592 O ATOM 848 CB ILE A 108 -12.881 -32.169 29.209 1.00 51.18 C ANISOU 848 CB ILE A 108 7343 5248 6853 195 -739 643 C ATOM 849 CG1 ILE A 108 -13.665 -30.867 29.189 1.00 46.28 C ANISOU 849 CG1 ILE A 108 6659 4758 6168 128 -679 626 C ATOM 850 CG2 ILE A 108 -11.601 -31.912 29.980 1.00 55.28 C ANISOU 850 CG2 ILE A 108 7814 5791 7399 274 -770 669 C ATOM 851 CD1 ILE A 108 -14.121 -30.467 30.581 1.00 47.15 C ANISOU 851 CD1 ILE A 108 6759 4937 6220 56 -699 703 C ATOM 852 N PRO A 109 -13.677 -33.881 25.947 1.00 42.00 N ANISOU 852 N PRO A 109 6314 3880 5764 227 -699 476 N ATOM 853 CA PRO A 109 -14.882 -34.363 25.248 1.00 42.24 C ANISOU 853 CA PRO A 109 6407 3868 5773 146 -693 455 C ATOM 854 C PRO A 109 -15.695 -35.372 26.056 1.00 49.70 C ANISOU 854 C PRO A 109 7437 4735 6712 58 -753 534 C ATOM 855 O PRO A 109 -16.905 -35.486 25.828 1.00 48.08 O ANISOU 855 O PRO A 109 7261 4535 6471 -42 -746 539 O ATOM 856 CB PRO A 109 -14.318 -34.996 23.967 1.00 42.31 C ANISOU 856 CB PRO A 109 6453 3790 5833 230 -683 369 C ATOM 857 CG PRO A 109 -12.914 -35.350 24.309 1.00 44.37 C ANISOU 857 CG PRO A 109 6701 4004 6154 345 -710 373 C ATOM 858 CD PRO A 109 -12.436 -34.289 25.266 1.00 42.98 C ANISOU 858 CD PRO A 109 6434 3943 5955 352 -699 418 C ATOM 859 N LEU A 110 -15.069 -36.093 27.000 1.00 55.50 N ANISOU 859 N LEU A 110 8210 5400 7478 89 -814 599 N ATOM 860 CA LEU A 110 -15.785 -37.107 27.775 1.00 59.54 C ANISOU 860 CA LEU A 110 8810 5829 7983 3 -875 681 C ATOM 861 C LEU A 110 -16.762 -36.480 28.770 1.00 58.58 C ANISOU 861 C LEU A 110 8658 5812 7787 -113 -863 754 C ATOM 862 O LEU A 110 -17.836 -37.034 29.022 1.00 60.22 O ANISOU 862 O LEU A 110 8921 5989 7969 -220 -882 799 O ATOM 863 CB LEU A 110 -14.786 -38.016 28.499 1.00 63.82 C ANISOU 863 CB LEU A 110 9402 6268 8580 76 -946 733 C ATOM 864 CG LEU A 110 -13.790 -38.812 27.637 1.00 64.30 C ANISOU 864 CG LEU A 110 9500 6208 8722 199 -966 667 C ATOM 865 CD1 LEU A 110 -12.675 -39.407 28.508 1.00 63.83 C ANISOU 865 CD1 LEU A 110 9460 6080 8713 284 -1033 724 C ATOM 866 CD2 LEU A 110 -14.478 -39.904 26.816 1.00 60.10 C ANISOU 866 CD2 LEU A 110 9071 5548 8215 161 -986 635 C ATOM 867 N ARG A 111 -16.423 -35.328 29.342 1.00 55.01 N ANISOU 867 N ARG A 111 8118 5485 7299 -96 -831 763 N ATOM 868 CA ARG A 111 -17.343 -34.640 30.238 1.00 57.84 C ANISOU 868 CA ARG A 111 8442 5952 7583 -199 -812 820 C ATOM 869 C ARG A 111 -18.107 -33.499 29.579 1.00 50.13 C ANISOU 869 C ARG A 111 7393 5091 6564 -238 -740 761 C ATOM 870 O ARG A 111 -18.869 -32.813 30.273 1.00 41.81 O ANISOU 870 O ARG A 111 6300 4137 5450 -314 -717 797 O ATOM 871 CB ARG A 111 -16.599 -34.100 31.453 1.00 65.46 C ANISOU 871 CB ARG A 111 9363 6982 8527 -168 -830 874 C ATOM 872 CG ARG A 111 -15.119 -34.217 31.350 1.00 74.33 C ANISOU 872 CG ARG A 111 10470 8061 9710 -41 -856 851 C ATOM 873 CD ARG A 111 -14.479 -33.875 32.672 1.00 83.72 C ANISOU 873 CD ARG A 111 11632 9303 10876 -26 -890 919 C ATOM 874 NE ARG A 111 -13.030 -34.016 32.599 1.00 90.74 N ANISOU 874 NE ARG A 111 12498 10151 11828 98 -921 900 N ATOM 875 CZ ARG A 111 -12.196 -33.712 33.586 1.00 93.60 C ANISOU 875 CZ ARG A 111 12827 10554 12185 137 -956 945 C ATOM 876 NH1 ARG A 111 -12.668 -33.241 34.738 1.00 95.56 N ANISOU 876 NH1 ARG A 111 13066 10883 12360 61 -964 1010 N ATOM 877 NH2 ARG A 111 -10.890 -33.881 33.416 1.00 92.85 N ANISOU 877 NH2 ARG A 111 12705 10420 12155 252 -984 922 N ATOM 878 N TYR A 112 -17.920 -33.271 28.271 1.00 44.98 N ANISOU 878 N TYR A 112 6723 4428 5940 -185 -704 673 N ATOM 879 CA TYR A 112 -18.591 -32.152 27.622 1.00 42.56 C ANISOU 879 CA TYR A 112 6349 4229 5594 -215 -641 620 C ATOM 880 C TYR A 112 -20.107 -32.253 27.779 1.00 44.33 C ANISOU 880 C TYR A 112 6589 4484 5772 -340 -635 651 C ATOM 881 O TYR A 112 -20.756 -31.321 28.277 1.00 42.65 O ANISOU 881 O TYR A 112 6316 4383 5505 -393 -601 668 O ATOM 882 CB TYR A 112 -18.205 -32.068 26.141 1.00 38.95 C ANISOU 882 CB TYR A 112 5886 3743 5170 -147 -610 526 C ATOM 883 CG TYR A 112 -18.960 -30.971 25.426 1.00 37.90 C ANISOU 883 CG TYR A 112 5692 3712 4995 -182 -551 477 C ATOM 884 CD1 TYR A 112 -18.512 -29.662 25.442 1.00 36.25 C ANISOU 884 CD1 TYR A 112 5398 3608 4768 -141 -506 453 C ATOM 885 CD2 TYR A 112 -20.134 -31.246 24.743 1.00 43.52 C ANISOU 885 CD2 TYR A 112 6434 4414 5689 -257 -545 457 C ATOM 886 CE1 TYR A 112 -19.220 -28.661 24.791 1.00 34.67 C ANISOU 886 CE1 TYR A 112 5147 3494 4531 -171 -458 413 C ATOM 887 CE2 TYR A 112 -20.851 -30.250 24.102 1.00 41.49 C ANISOU 887 CE2 TYR A 112 6120 4249 5393 -287 -498 417 C ATOM 888 CZ TYR A 112 -20.382 -28.955 24.137 1.00 34.20 C ANISOU 888 CZ TYR A 112 5116 3425 4453 -241 -455 396 C ATOM 889 OH TYR A 112 -21.096 -27.981 23.479 1.00 36.32 O ANISOU 889 OH TYR A 112 5335 3778 4688 -267 -413 358 O ATOM 890 N ASN A 113 -20.697 -33.384 27.367 1.00 46.02 N ANISOU 890 N ASN A 113 6883 4598 6006 -390 -667 656 N ATOM 891 CA ASN A 113 -22.158 -33.472 27.370 1.00 51.07 C ANISOU 891 CA ASN A 113 7529 5270 6605 -512 -660 678 C ATOM 892 C ASN A 113 -22.739 -33.390 28.784 1.00 51.78 C ANISOU 892 C ASN A 113 7608 5419 6646 -596 -669 770 C ATOM 893 O ASN A 113 -23.834 -32.847 28.972 1.00 54.63 O ANISOU 893 O ASN A 113 7925 5872 6959 -680 -637 782 O ATOM 894 CB ASN A 113 -22.618 -34.742 26.650 1.00 51.80 C ANISOU 894 CB ASN A 113 7714 5237 6733 -551 -699 665 C ATOM 895 CG ASN A 113 -22.605 -34.582 25.138 1.00 59.21 C ANISOU 895 CG ASN A 113 8648 6158 7689 -508 -673 566 C ATOM 896 OD1 ASN A 113 -22.680 -33.461 24.618 1.00 62.50 O ANISOU 896 OD1 ASN A 113 8990 6677 8081 -484 -622 517 O ATOM 897 ND2 ASN A 113 -22.514 -35.700 24.421 1.00 62.93 N ANISOU 897 ND2 ASN A 113 9206 6502 8204 -498 -710 536 N ATOM 898 N GLY A 114 -22.010 -33.867 29.791 1.00 49.79 N ANISOU 898 N GLY A 114 7390 5123 6403 -572 -710 834 N ATOM 899 CA GLY A 114 -22.487 -33.727 31.156 1.00 50.50 C ANISOU 899 CA GLY A 114 7470 5279 6438 -648 -715 921 C ATOM 900 C GLY A 114 -22.332 -32.328 31.716 1.00 50.87 C ANISOU 900 C GLY A 114 7423 5469 6436 -625 -668 911 C ATOM 901 O GLY A 114 -23.077 -31.932 32.620 1.00 53.50 O ANISOU 901 O GLY A 114 7727 5890 6708 -702 -650 960 O ATOM 902 N LEU A 115 -21.367 -31.562 31.202 1.00 44.62 N ANISOU 902 N LEU A 115 6581 4701 5669 -522 -647 848 N ATOM 903 CA LEU A 115 -21.056 -30.244 31.743 1.00 44.32 C ANISOU 903 CA LEU A 115 6461 4786 5594 -492 -609 837 C ATOM 904 C LEU A 115 -21.828 -29.130 31.036 1.00 44.73 C ANISOU 904 C LEU A 115 6440 4935 5618 -512 -547 775 C ATOM 905 O LEU A 115 -22.370 -28.235 31.697 1.00 45.57 O ANISOU 905 O LEU A 115 6492 5150 5671 -551 -514 788 O ATOM 906 CB LEU A 115 -19.546 -29.994 31.656 1.00 48.11 C ANISOU 906 CB LEU A 115 6923 5242 6116 -374 -623 810 C ATOM 907 CG LEU A 115 -18.996 -28.563 31.778 1.00 60.25 C ANISOU 907 CG LEU A 115 8371 6887 7634 -322 -583 771 C ATOM 908 CD1 LEU A 115 -19.406 -27.895 33.089 1.00 65.67 C ANISOU 908 CD1 LEU A 115 9026 7674 8252 -378 -575 822 C ATOM 909 CD2 LEU A 115 -17.469 -28.529 31.632 1.00 59.30 C ANISOU 909 CD2 LEU A 115 8237 6729 7567 -211 -604 748 C ATOM 910 N VAL A 116 -21.921 -29.190 29.708 1.00 37.49 N ANISOU 910 N VAL A 116 5526 3981 4736 -485 -531 709 N ATOM 911 CA VAL A 116 -22.498 -28.152 28.877 1.00 34.50 C ANISOU 911 CA VAL A 116 5085 3683 4340 -488 -478 646 C ATOM 912 C VAL A 116 -23.857 -28.671 28.421 1.00 42.66 C ANISOU 912 C VAL A 116 6142 4706 5360 -582 -478 649 C ATOM 913 O VAL A 116 -23.927 -29.542 27.554 1.00 49.41 O ANISOU 913 O VAL A 116 7052 5470 6250 -583 -500 625 O ATOM 914 CB VAL A 116 -21.574 -27.832 27.694 1.00 40.29 C ANISOU 914 CB VAL A 116 5805 4387 5117 -391 -462 571 C ATOM 915 CG1 VAL A 116 -22.018 -26.590 26.940 1.00 39.27 C ANISOU 915 CG1 VAL A 116 5607 4348 4966 -386 -409 513 C ATOM 916 CG2 VAL A 116 -20.144 -27.652 28.190 1.00 41.45 C ANISOU 916 CG2 VAL A 116 5939 4521 5289 -303 -476 578 C ATOM 917 N THR A 117 -24.946 -28.176 29.013 1.00 39.87 N ANISOU 917 N THR A 117 5746 4445 4956 -661 -454 677 N ATOM 918 CA THR A 117 -26.287 -28.629 28.668 1.00 37.59 C ANISOU 918 CA THR A 117 5468 4160 4654 -758 -453 685 C ATOM 919 C THR A 117 -27.102 -27.469 28.124 1.00 41.85 C ANISOU 919 C THR A 117 5928 4807 5168 -769 -405 636 C ATOM 920 O THR A 117 -26.784 -26.301 28.356 1.00 44.17 O ANISOU 920 O THR A 117 6159 5182 5442 -721 -371 615 O ATOM 921 CB THR A 117 -27.045 -29.223 29.875 1.00 41.94 C ANISOU 921 CB THR A 117 6040 4728 5169 -859 -469 769 C ATOM 922 OG1 THR A 117 -27.248 -28.183 30.838 1.00 42.62 O ANISOU 922 OG1 THR A 117 6056 4935 5201 -866 -431 788 O ATOM 923 CG2 THR A 117 -26.276 -30.415 30.528 1.00 42.76 C ANISOU 923 CG2 THR A 117 6230 4721 5296 -853 -524 831 C ATOM 924 N GLY A 118 -28.174 -27.806 27.406 1.00 39.17 N ANISOU 924 N GLY A 118 5591 4464 4828 -835 -407 621 N ATOM 925 CA GLY A 118 -29.069 -26.774 26.908 1.00 35.22 C ANISOU 925 CA GLY A 118 5013 4064 4303 -851 -368 581 C ATOM 926 C GLY A 118 -29.606 -25.891 28.018 1.00 36.01 C ANISOU 926 C GLY A 118 5044 4284 4356 -881 -332 612 C ATOM 927 O GLY A 118 -29.621 -24.666 27.901 1.00 36.95 O ANISOU 927 O GLY A 118 5096 4485 4459 -837 -296 575 O ATOM 928 N THR A 119 -30.046 -26.506 29.113 1.00 36.44 N ANISOU 928 N THR A 119 5116 4347 4385 -956 -342 681 N ATOM 929 CA THR A 119 -30.628 -25.776 30.237 1.00 37.25 C ANISOU 929 CA THR A 119 5156 4566 4434 -993 -306 712 C ATOM 930 C THR A 119 -29.653 -24.774 30.840 1.00 38.53 C ANISOU 930 C THR A 119 5288 4771 4579 -909 -286 699 C ATOM 931 O THR A 119 -30.040 -23.649 31.172 1.00 41.97 O ANISOU 931 O THR A 119 5654 5311 4983 -898 -245 677 O ATOM 932 CB THR A 119 -31.092 -26.776 31.307 1.00 41.44 C ANISOU 932 CB THR A 119 5725 5082 4937 -1088 -324 796 C ATOM 933 OG1 THR A 119 -32.341 -27.335 30.898 1.00 52.56 O ANISOU 933 OG1 THR A 119 7127 6498 6346 -1184 -327 806 O ATOM 934 CG2 THR A 119 -31.299 -26.098 32.633 1.00 45.07 C ANISOU 934 CG2 THR A 119 6138 5650 5336 -1108 -289 831 C ATOM 935 N ARG A 120 -28.386 -25.162 31.006 1.00 39.59 N ANISOU 935 N ARG A 120 5476 4829 4739 -849 -316 709 N ATOM 936 CA ARG A 120 -27.411 -24.215 31.534 1.00 36.90 C ANISOU 936 CA ARG A 120 5105 4528 4386 -772 -302 694 C ATOM 937 C ARG A 120 -27.060 -23.160 30.497 1.00 36.22 C ANISOU 937 C ARG A 120 4974 4463 4325 -696 -276 618 C ATOM 938 O ARG A 120 -26.762 -22.023 30.860 1.00 36.92 O ANISOU 938 O ARG A 120 5012 4621 4394 -654 -249 595 O ATOM 939 CB ARG A 120 -26.137 -24.937 31.990 1.00 37.88 C ANISOU 939 CB ARG A 120 5292 4566 4534 -727 -345 728 C ATOM 940 CG ARG A 120 -26.313 -25.857 33.218 1.00 40.51 C ANISOU 940 CG ARG A 120 5675 4883 4836 -796 -374 814 C ATOM 941 CD ARG A 120 -25.054 -26.708 33.519 1.00 38.30 C ANISOU 941 CD ARG A 120 5463 4500 4589 -746 -428 849 C ATOM 942 NE ARG A 120 -25.403 -27.823 34.404 1.00 47.69 N ANISOU 942 NE ARG A 120 6715 5649 5757 -823 -464 934 N ATOM 943 CZ ARG A 120 -24.632 -28.879 34.624 1.00 50.63 C ANISOU 943 CZ ARG A 120 7163 5914 6161 -804 -520 978 C ATOM 944 NH1 ARG A 120 -25.036 -29.843 35.447 1.00 55.70 N ANISOU 944 NH1 ARG A 120 7863 6521 6778 -883 -552 1061 N ATOM 945 NH2 ARG A 120 -23.461 -28.978 34.025 1.00 49.87 N ANISOU 945 NH2 ARG A 120 7082 5744 6121 -706 -544 941 N ATOM 946 N ALA A 121 -27.081 -23.518 29.213 1.00 33.08 N ANISOU 946 N ALA A 121 4597 4005 3968 -679 -285 579 N ATOM 947 CA ALA A 121 -26.804 -22.527 28.173 1.00 35.82 C ANISOU 947 CA ALA A 121 4905 4374 4332 -613 -260 511 C ATOM 948 C ALA A 121 -27.872 -21.435 28.157 1.00 35.83 C ANISOU 948 C ALA A 121 4832 4481 4300 -639 -222 489 C ATOM 949 O ALA A 121 -27.562 -20.244 28.026 1.00 33.23 O ANISOU 949 O ALA A 121 4456 4203 3967 -585 -196 452 O ATOM 950 CB ALA A 121 -26.702 -23.214 26.806 1.00 31.86 C ANISOU 950 CB ALA A 121 4445 3789 3870 -598 -279 475 C ATOM 951 N ALA A 122 -29.138 -21.817 28.299 1.00 33.72 N ANISOU 951 N ALA A 122 4553 4247 4013 -721 -220 511 N ATOM 952 CA ALA A 122 -30.187 -20.805 28.273 1.00 35.19 C ANISOU 952 CA ALA A 122 4663 4535 4172 -739 -185 488 C ATOM 953 C ALA A 122 -30.091 -19.865 29.479 1.00 36.57 C ANISOU 953 C ALA A 122 4792 4794 4308 -724 -155 499 C ATOM 954 O ALA A 122 -30.437 -18.686 29.366 1.00 34.72 O ANISOU 954 O ALA A 122 4497 4632 4062 -695 -124 462 O ATOM 955 CB ALA A 122 -31.564 -21.471 28.193 1.00 32.00 C ANISOU 955 CB ALA A 122 4248 4153 3756 -834 -190 511 C ATOM 956 N GLY A 123 -29.600 -20.349 30.630 1.00 36.76 N ANISOU 956 N GLY A 123 4848 4809 4311 -741 -166 548 N ATOM 957 CA GLY A 123 -29.440 -19.458 31.771 1.00 30.86 C ANISOU 957 CA GLY A 123 4063 4140 3521 -725 -140 553 C ATOM 958 C GLY A 123 -28.237 -18.540 31.620 1.00 29.24 C ANISOU 958 C GLY A 123 3851 3923 3334 -634 -138 514 C ATOM 959 O GLY A 123 -28.275 -17.377 32.020 1.00 29.85 O ANISOU 959 O GLY A 123 3881 4072 3390 -605 -110 486 O ATOM 960 N ILE A 124 -27.149 -19.053 31.049 1.00 27.64 N ANISOU 960 N ILE A 124 3695 3632 3174 -589 -168 511 N ATOM 961 CA ILE A 124 -26.035 -18.178 30.696 1.00 28.80 C ANISOU 961 CA ILE A 124 3828 3769 3346 -506 -164 470 C ATOM 962 C ILE A 124 -26.491 -17.113 29.706 1.00 27.08 C ANISOU 962 C ILE A 124 3562 3588 3139 -478 -135 413 C ATOM 963 O ILE A 124 -26.164 -15.932 29.861 1.00 29.02 O ANISOU 963 O ILE A 124 3770 3877 3378 -435 -115 383 O ATOM 964 CB ILE A 124 -24.874 -19.015 30.147 1.00 29.27 C ANISOU 964 CB ILE A 124 3941 3729 3452 -464 -198 474 C ATOM 965 CG1 ILE A 124 -24.332 -19.924 31.271 1.00 37.43 C ANISOU 965 CG1 ILE A 124 5019 4729 4474 -483 -232 534 C ATOM 966 CG2 ILE A 124 -23.805 -18.119 29.549 1.00 28.43 C ANISOU 966 CG2 ILE A 124 3812 3616 3376 -384 -188 428 C ATOM 967 CD1 ILE A 124 -23.301 -20.954 30.769 1.00 43.61 C ANISOU 967 CD1 ILE A 124 5858 5406 5307 -443 -270 543 C ATOM 968 N ILE A 125 -27.283 -17.501 28.702 1.00 24.14 N ANISOU 968 N ILE A 125 3194 3199 2782 -504 -135 400 N ATOM 969 CA ILE A 125 -27.733 -16.526 27.707 1.00 27.28 C ANISOU 969 CA ILE A 125 3549 3628 3187 -477 -114 350 C ATOM 970 C ILE A 125 -28.554 -15.425 28.380 1.00 23.41 C ANISOU 970 C ILE A 125 2997 3235 2665 -485 -84 340 C ATOM 971 O ILE A 125 -28.337 -14.229 28.144 1.00 22.85 O ANISOU 971 O ILE A 125 2892 3193 2597 -436 -66 303 O ATOM 972 CB ILE A 125 -28.506 -17.220 26.565 1.00 28.53 C ANISOU 972 CB ILE A 125 3724 3754 3362 -510 -127 341 C ATOM 973 CG1 ILE A 125 -27.531 -18.041 25.705 1.00 30.00 C ANISOU 973 CG1 ILE A 125 3971 3843 3584 -479 -151 332 C ATOM 974 CG2 ILE A 125 -29.226 -16.151 25.656 1.00 24.69 C ANISOU 974 CG2 ILE A 125 3188 3317 2876 -491 -108 297 C ATOM 975 CD1 ILE A 125 -28.207 -19.052 24.769 1.00 28.52 C ANISOU 975 CD1 ILE A 125 3820 3608 3409 -522 -173 328 C ATOM 976 N ALA A 126 -29.509 -15.811 29.233 1.00 26.78 N ANISOU 976 N ALA A 126 3407 3710 3057 -549 -76 371 N ATOM 977 CA ALA A 126 -30.331 -14.820 29.931 1.00 27.72 C ANISOU 977 CA ALA A 126 3465 3927 3142 -555 -43 357 C ATOM 978 C ALA A 126 -29.462 -13.877 30.771 1.00 26.12 C ANISOU 978 C ALA A 126 3253 3747 2923 -505 -31 343 C ATOM 979 O ALA A 126 -29.646 -12.644 30.765 1.00 26.04 O ANISOU 979 O ALA A 126 3200 3786 2909 -466 -8 303 O ATOM 980 CB ALA A 126 -31.360 -15.535 30.825 1.00 24.81 C ANISOU 980 CB ALA A 126 3084 3608 2735 -637 -34 400 C ATOM 981 N ILE A 127 -28.533 -14.453 31.528 1.00 27.01 N ANISOU 981 N ILE A 127 3408 3826 3027 -506 -50 377 N ATOM 982 CA ILE A 127 -27.633 -13.661 32.360 1.00 28.43 C ANISOU 982 CA ILE A 127 3586 4026 3192 -464 -47 366 C ATOM 983 C ILE A 127 -26.844 -12.686 31.511 1.00 25.87 C ANISOU 983 C ILE A 127 3249 3674 2906 -394 -46 319 C ATOM 984 O ILE A 127 -26.659 -11.521 31.875 1.00 23.71 O ANISOU 984 O ILE A 127 2946 3440 2622 -360 -30 287 O ATOM 985 CB ILE A 127 -26.709 -14.604 33.148 1.00 29.11 C ANISOU 985 CB ILE A 127 3723 4068 3269 -477 -79 415 C ATOM 986 CG1 ILE A 127 -27.520 -15.258 34.285 1.00 32.80 C ANISOU 986 CG1 ILE A 127 4197 4584 3682 -549 -73 463 C ATOM 987 CG2 ILE A 127 -25.490 -13.864 33.630 1.00 26.82 C ANISOU 987 CG2 ILE A 127 3434 3774 2981 -422 -89 398 C ATOM 988 CD1 ILE A 127 -26.811 -16.458 34.944 1.00 34.40 C ANISOU 988 CD1 ILE A 127 4462 4732 3878 -574 -112 525 C ATOM 989 N CYS A 128 -26.346 -13.154 30.372 1.00 23.86 N ANISOU 989 N CYS A 128 3021 3350 2696 -374 -63 314 N ATOM 990 CA CYS A 128 -25.528 -12.306 29.526 1.00 24.30 C ANISOU 990 CA CYS A 128 3068 3379 2786 -313 -60 275 C ATOM 991 C CYS A 128 -26.355 -11.164 28.930 1.00 24.69 C ANISOU 991 C CYS A 128 3073 3472 2835 -297 -35 235 C ATOM 992 O CYS A 128 -25.859 -10.041 28.813 1.00 21.65 O ANISOU 992 O CYS A 128 2670 3096 2460 -254 -26 204 O ATOM 993 CB CYS A 128 -24.864 -13.177 28.442 1.00 26.78 C ANISOU 993 CB CYS A 128 3422 3614 3141 -297 -79 278 C ATOM 994 SG CYS A 128 -23.482 -14.158 29.145 1.00 31.26 S ANISOU 994 SG CYS A 128 4033 4122 3721 -284 -112 315 S ATOM 995 N TRP A 129 -27.631 -11.408 28.609 1.00 22.53 N ANISOU 995 N TRP A 129 2782 3229 2551 -334 -27 236 N ATOM 996 CA TRP A 129 -28.463 -10.306 28.123 1.00 24.81 C ANISOU 996 CA TRP A 129 3024 3563 2840 -315 -8 200 C ATOM 997 C TRP A 129 -28.702 -9.261 29.215 1.00 24.00 C ANISOU 997 C TRP A 129 2884 3526 2709 -301 14 182 C ATOM 998 O TRP A 129 -28.698 -8.062 28.929 1.00 22.62 O ANISOU 998 O TRP A 129 2685 3366 2545 -258 24 146 O ATOM 999 CB TRP A 129 -29.791 -10.832 27.579 1.00 23.09 C ANISOU 999 CB TRP A 129 2787 3368 2617 -359 -8 206 C ATOM 1000 CG TRP A 129 -29.695 -11.240 26.148 1.00 23.86 C ANISOU 1000 CG TRP A 129 2910 3411 2745 -352 -26 198 C ATOM 1001 CD1 TRP A 129 -29.562 -12.512 25.635 1.00 23.11 C ANISOU 1001 CD1 TRP A 129 2860 3261 2661 -384 -48 219 C ATOM 1002 CD2 TRP A 129 -29.725 -10.354 25.031 1.00 22.92 C ANISOU 1002 CD2 TRP A 129 2778 3285 2644 -309 -25 165 C ATOM 1003 NE1 TRP A 129 -29.512 -12.458 24.259 1.00 27.08 N ANISOU 1003 NE1 TRP A 129 3377 3728 3184 -363 -58 196 N ATOM 1004 CE2 TRP A 129 -29.598 -11.149 23.861 1.00 24.38 C ANISOU 1004 CE2 TRP A 129 3001 3417 2847 -318 -45 166 C ATOM 1005 CE3 TRP A 129 -29.819 -8.957 24.911 1.00 21.81 C ANISOU 1005 CE3 TRP A 129 2603 3176 2508 -264 -12 135 C ATOM 1006 CZ2 TRP A 129 -29.580 -10.601 22.581 1.00 23.68 C ANISOU 1006 CZ2 TRP A 129 2915 3311 2771 -287 -49 141 C ATOM 1007 CZ3 TRP A 129 -29.821 -8.407 23.645 1.00 19.90 C ANISOU 1007 CZ3 TRP A 129 2363 2912 2284 -233 -19 115 C ATOM 1008 CH2 TRP A 129 -29.697 -9.235 22.485 1.00 23.38 C ANISOU 1008 CH2 TRP A 129 2842 3306 2735 -246 -37 119 C ATOM 1009 N VAL A 130 -28.924 -9.689 30.465 1.00 21.48 N ANISOU 1009 N VAL A 130 2564 3247 2352 -338 21 207 N ATOM 1010 CA VAL A 130 -29.061 -8.733 31.564 1.00 22.34 C ANISOU 1010 CA VAL A 130 2643 3417 2426 -323 42 185 C ATOM 1011 C VAL A 130 -27.775 -7.930 31.719 1.00 22.56 C ANISOU 1011 C VAL A 130 2690 3414 2469 -273 32 164 C ATOM 1012 O VAL A 130 -27.806 -6.700 31.814 1.00 23.44 O ANISOU 1012 O VAL A 130 2776 3548 2582 -235 45 124 O ATOM 1013 CB VAL A 130 -29.446 -9.439 32.888 1.00 25.89 C ANISOU 1013 CB VAL A 130 3098 3917 2824 -377 51 220 C ATOM 1014 CG1 VAL A 130 -29.378 -8.452 34.077 1.00 27.89 C ANISOU 1014 CG1 VAL A 130 3330 4231 3035 -357 72 193 C ATOM 1015 CG2 VAL A 130 -30.876 -10.070 32.832 1.00 25.04 C ANISOU 1015 CG2 VAL A 130 2958 3857 2697 -434 68 239 C ATOM 1016 N LEU A 131 -26.620 -8.613 31.747 1.00 20.91 N ANISOU 1016 N LEU A 131 2521 3148 2274 -272 6 191 N ATOM 1017 CA LEU A 131 -25.356 -7.912 31.888 1.00 20.79 C ANISOU 1017 CA LEU A 131 2517 3106 2277 -230 -6 173 C ATOM 1018 C LEU A 131 -25.128 -6.945 30.724 1.00 25.10 C ANISOU 1018 C LEU A 131 3049 3623 2864 -186 -1 137 C ATOM 1019 O LEU A 131 -24.567 -5.855 30.916 1.00 21.55 O ANISOU 1019 O LEU A 131 2590 3175 2422 -153 1 108 O ATOM 1020 CB LEU A 131 -24.188 -8.909 31.965 1.00 25.44 C ANISOU 1020 CB LEU A 131 3146 3639 2882 -232 -36 209 C ATOM 1021 CG LEU A 131 -24.219 -9.851 33.177 1.00 26.61 C ANISOU 1021 CG LEU A 131 3316 3806 2988 -274 -50 253 C ATOM 1022 CD1 LEU A 131 -23.064 -10.892 33.070 1.00 29.98 C ANISOU 1022 CD1 LEU A 131 3784 4166 3443 -267 -85 289 C ATOM 1023 CD2 LEU A 131 -24.114 -9.031 34.451 1.00 28.94 C ANISOU 1023 CD2 LEU A 131 3598 4158 3238 -272 -44 239 C ATOM 1024 N SER A 132 -25.575 -7.320 29.518 1.00 20.64 N ANISOU 1024 N SER A 132 2486 3032 2324 -187 0 139 N ATOM 1025 CA SER A 132 -25.403 -6.450 28.358 1.00 22.05 C ANISOU 1025 CA SER A 132 2657 3185 2536 -150 4 110 C ATOM 1026 C SER A 132 -26.213 -5.161 28.490 1.00 22.19 C ANISOU 1026 C SER A 132 2639 3246 2545 -129 21 75 C ATOM 1027 O SER A 132 -25.765 -4.099 28.040 1.00 20.36 O ANISOU 1027 O SER A 132 2404 2996 2337 -93 21 51 O ATOM 1028 CB SER A 132 -25.822 -7.185 27.083 1.00 21.44 C ANISOU 1028 CB SER A 132 2593 3077 2477 -160 0 120 C ATOM 1029 OG SER A 132 -24.991 -8.306 26.903 1.00 26.16 O ANISOU 1029 OG SER A 132 3227 3626 3087 -170 -15 145 O ATOM 1030 N PHE A 133 -27.451 -5.263 28.996 1.00 22.63 N ANISOU 1030 N PHE A 133 2666 3358 2572 -152 34 73 N ATOM 1031 CA PHE A 133 -28.227 -4.059 29.276 1.00 24.79 C ANISOU 1031 CA PHE A 133 2904 3678 2839 -126 51 36 C ATOM 1032 C PHE A 133 -27.540 -3.177 30.328 1.00 25.59 C ANISOU 1032 C PHE A 133 3007 3789 2926 -104 54 12 C ATOM 1033 O PHE A 133 -27.459 -1.959 30.162 1.00 22.48 O ANISOU 1033 O PHE A 133 2604 3388 2549 -64 57 -23 O ATOM 1034 CB PHE A 133 -29.649 -4.451 29.700 1.00 22.46 C ANISOU 1034 CB PHE A 133 2570 3449 2514 -157 68 40 C ATOM 1035 CG PHE A 133 -30.590 -4.597 28.546 1.00 27.24 C ANISOU 1035 CG PHE A 133 3154 4055 3140 -160 64 40 C ATOM 1036 CD1 PHE A 133 -31.291 -3.483 28.058 1.00 28.99 C ANISOU 1036 CD1 PHE A 133 3341 4296 3378 -119 69 6 C ATOM 1037 CD2 PHE A 133 -30.787 -5.833 27.936 1.00 26.93 C ANISOU 1037 CD2 PHE A 133 3133 3995 3105 -202 51 73 C ATOM 1038 CE1 PHE A 133 -32.182 -3.614 26.973 1.00 27.83 C ANISOU 1038 CE1 PHE A 133 3173 4153 3249 -121 58 9 C ATOM 1039 CE2 PHE A 133 -31.666 -5.979 26.836 1.00 26.69 C ANISOU 1039 CE2 PHE A 133 3084 3967 3091 -208 42 72 C ATOM 1040 CZ PHE A 133 -32.365 -4.846 26.349 1.00 27.35 C ANISOU 1040 CZ PHE A 133 3129 4076 3189 -167 44 41 C ATOM 1041 N ALA A 134 -27.021 -3.771 31.404 1.00 21.60 N ANISOU 1041 N ALA A 134 2519 3297 2390 -129 51 31 N ATOM 1042 CA ALA A 134 -26.356 -2.974 32.440 1.00 25.84 C ANISOU 1042 CA ALA A 134 3061 3847 2908 -112 49 7 C ATOM 1043 C ALA A 134 -25.096 -2.268 31.905 1.00 25.02 C ANISOU 1043 C ALA A 134 2977 3684 2847 -80 30 -6 C ATOM 1044 O ALA A 134 -24.886 -1.081 32.186 1.00 22.85 O ANISOU 1044 O ALA A 134 2697 3410 2577 -52 30 -44 O ATOM 1045 CB ALA A 134 -26.005 -3.865 33.649 1.00 24.73 C ANISOU 1045 CB ALA A 134 2940 3732 2723 -150 42 38 C ATOM 1046 N ILE A 135 -24.261 -2.972 31.128 1.00 22.09 N ANISOU 1046 N ILE A 135 2627 3261 2507 -85 14 24 N ATOM 1047 CA ILE A 135 -23.063 -2.372 30.531 1.00 21.44 C ANISOU 1047 CA ILE A 135 2555 3127 2464 -59 0 16 C ATOM 1048 C ILE A 135 -23.423 -1.315 29.467 1.00 22.22 C ANISOU 1048 C ILE A 135 2644 3206 2594 -30 9 -10 C ATOM 1049 O ILE A 135 -22.880 -0.203 29.455 1.00 20.34 O ANISOU 1049 O ILE A 135 2406 2948 2375 -8 5 -35 O ATOM 1050 CB ILE A 135 -22.158 -3.474 29.933 1.00 21.37 C ANISOU 1050 CB ILE A 135 2566 3074 2479 -68 -14 52 C ATOM 1051 CG1 ILE A 135 -21.475 -4.260 31.064 1.00 24.53 C ANISOU 1051 CG1 ILE A 135 2980 3483 2857 -87 -33 77 C ATOM 1052 CG2 ILE A 135 -21.119 -2.872 28.957 1.00 26.03 C ANISOU 1052 CG2 ILE A 135 3159 3616 3114 -43 -17 44 C ATOM 1053 CD1 ILE A 135 -21.000 -5.677 30.644 1.00 25.76 C ANISOU 1053 CD1 ILE A 135 3157 3602 3028 -99 -46 117 C ATOM 1054 N GLY A 136 -24.328 -1.641 28.551 1.00 18.83 N ANISOU 1054 N GLY A 136 2208 2778 2170 -31 18 -3 N ATOM 1055 CA GLY A 136 -24.573 -0.726 27.442 1.00 18.22 C ANISOU 1055 CA GLY A 136 2126 2675 2120 -4 20 -19 C ATOM 1056 C GLY A 136 -25.362 0.490 27.871 1.00 21.48 C ANISOU 1056 C GLY A 136 2519 3115 2529 22 27 -57 C ATOM 1057 O GLY A 136 -25.231 1.559 27.271 1.00 20.41 O ANISOU 1057 O GLY A 136 2386 2949 2419 50 22 -74 O ATOM 1058 N LEU A 137 -26.190 0.355 28.914 1.00 19.80 N ANISOU 1058 N LEU A 137 2284 2957 2281 13 38 -70 N ATOM 1059 CA LEU A 137 -26.963 1.507 29.393 1.00 19.20 C ANISOU 1059 CA LEU A 137 2186 2910 2199 45 47 -112 C ATOM 1060 C LEU A 137 -26.369 2.137 30.643 1.00 19.91 C ANISOU 1060 C LEU A 137 2286 3011 2270 50 47 -142 C ATOM 1061 O LEU A 137 -27.048 2.923 31.297 1.00 23.04 O ANISOU 1061 O LEU A 137 2664 3440 2651 74 59 -182 O ATOM 1062 CB LEU A 137 -28.422 1.124 29.669 1.00 20.17 C ANISOU 1062 CB LEU A 137 2271 3098 2296 37 66 -117 C ATOM 1063 CG LEU A 137 -29.143 0.519 28.450 1.00 17.97 C ANISOU 1063 CG LEU A 137 1980 2813 2034 28 62 -92 C ATOM 1064 CD1 LEU A 137 -30.603 0.209 28.820 1.00 25.09 C ANISOU 1064 CD1 LEU A 137 2834 3787 2912 18 80 -99 C ATOM 1065 CD2 LEU A 137 -29.004 1.354 27.141 1.00 21.35 C ANISOU 1065 CD2 LEU A 137 2419 3189 2503 64 45 -97 C ATOM 1066 N THR A 138 -25.127 1.794 30.999 1.00 20.18 N ANISOU 1066 N THR A 138 2344 3019 2303 31 32 -125 N ATOM 1067 CA THR A 138 -24.457 2.468 32.117 1.00 21.34 C ANISOU 1067 CA THR A 138 2502 3171 2434 35 24 -154 C ATOM 1068 C THR A 138 -24.507 3.996 32.008 1.00 20.38 C ANISOU 1068 C THR A 138 2383 3023 2336 73 20 -201 C ATOM 1069 O THR A 138 -24.680 4.653 33.049 1.00 20.55 O ANISOU 1069 O THR A 138 2405 3071 2332 84 23 -243 O ATOM 1070 CB THR A 138 -23.004 1.943 32.228 1.00 23.26 C ANISOU 1070 CB THR A 138 2767 3382 2688 12 1 -125 C ATOM 1071 OG1 THR A 138 -23.014 0.724 32.991 1.00 24.78 O ANISOU 1071 OG1 THR A 138 2962 3611 2841 -20 1 -94 O ATOM 1072 CG2 THR A 138 -22.094 2.923 32.939 1.00 22.70 C ANISOU 1072 CG2 THR A 138 2709 3295 2621 20 -18 -156 C ATOM 1073 N PRO A 139 -24.416 4.623 30.818 1.00 24.36 N ANISOU 1073 N PRO A 139 2892 3475 2887 94 13 -199 N ATOM 1074 CA PRO A 139 -24.597 6.083 30.777 1.00 21.29 C ANISOU 1074 CA PRO A 139 2510 3058 2522 131 7 -243 C ATOM 1075 C PRO A 139 -25.935 6.523 31.321 1.00 22.30 C ANISOU 1075 C PRO A 139 2613 3233 2627 163 25 -284 C ATOM 1076 O PRO A 139 -26.027 7.617 31.899 1.00 21.38 O ANISOU 1076 O PRO A 139 2504 3107 2512 192 21 -333 O ATOM 1077 CB PRO A 139 -24.446 6.419 29.279 1.00 20.61 C ANISOU 1077 CB PRO A 139 2433 2915 2483 143 -2 -218 C ATOM 1078 CG PRO A 139 -23.393 5.375 28.803 1.00 20.01 C ANISOU 1078 CG PRO A 139 2368 2824 2413 106 -6 -171 C ATOM 1079 CD PRO A 139 -23.877 4.108 29.547 1.00 19.52 C ANISOU 1079 CD PRO A 139 2289 2820 2307 83 7 -157 C ATOM 1080 N MET A 140 -26.976 5.692 31.198 1.00 21.16 N ANISOU 1080 N MET A 140 2438 3140 2461 156 44 -267 N ATOM 1081 CA MET A 140 -28.266 6.096 31.753 1.00 21.40 C ANISOU 1081 CA MET A 140 2436 3226 2471 187 66 -308 C ATOM 1082 C MET A 140 -28.278 6.083 33.278 1.00 24.69 C ANISOU 1082 C MET A 140 2849 3697 2833 177 82 -341 C ATOM 1083 O MET A 140 -29.201 6.649 33.874 1.00 22.29 O ANISOU 1083 O MET A 140 2521 3437 2510 209 103 -388 O ATOM 1084 CB MET A 140 -29.376 5.190 31.196 1.00 22.34 C ANISOU 1084 CB MET A 140 2515 3390 2582 175 81 -279 C ATOM 1085 CG MET A 140 -29.517 5.352 29.641 1.00 27.37 C ANISOU 1085 CG MET A 140 3155 3976 3266 191 62 -253 C ATOM 1086 SD MET A 140 -30.972 4.496 29.029 1.00 36.40 S ANISOU 1086 SD MET A 140 4250 5178 4404 182 74 -231 S ATOM 1087 CE MET A 140 -32.268 5.668 29.533 1.00 32.20 C ANISOU 1087 CE MET A 140 3670 4690 3875 245 88 -291 C ATOM 1088 N ALEU A 141 -27.294 5.456 33.927 0.61 25.15 N ANISOU 1088 N ALEU A 141 2933 3757 2866 137 73 -320 N ATOM 1089 N BLEU A 141 -27.289 5.454 33.915 0.39 24.95 N ANISOU 1089 N BLEU A 141 2908 3732 2841 137 73 -319 N ATOM 1090 CA ALEU A 141 -27.219 5.477 35.387 0.61 25.62 C ANISOU 1090 CA ALEU A 141 2998 3868 2868 125 84 -350 C ATOM 1091 CA BLEU A 141 -27.178 5.452 35.370 0.39 25.72 C ANISOU 1091 CA BLEU A 141 3012 3880 2882 124 83 -348 C ATOM 1092 C ALEU A 141 -26.516 6.720 35.917 0.61 28.05 C ANISOU 1092 C ALEU A 141 3336 4139 3184 150 65 -402 C ATOM 1093 C BLEU A 141 -26.380 6.639 35.895 0.39 27.31 C ANISOU 1093 C BLEU A 141 3244 4041 3091 145 62 -397 C ATOM 1094 O ALEU A 141 -26.426 6.893 37.146 0.61 29.07 O ANISOU 1094 O ALEU A 141 3475 4309 3262 144 71 -437 O ATOM 1095 O BLEU A 141 -26.083 6.683 37.099 0.39 28.67 O ANISOU 1095 O BLEU A 141 3430 4249 3213 132 63 -422 O ATOM 1096 CB ALEU A 141 -26.512 4.215 35.907 0.61 24.40 C ANISOU 1096 CB ALEU A 141 2859 3735 2678 71 76 -299 C ATOM 1097 CB BLEU A 141 -26.547 4.143 35.865 0.39 24.44 C ANISOU 1097 CB BLEU A 141 2863 3741 2684 69 77 -296 C ATOM 1098 CG ALEU A 141 -27.049 2.874 35.392 0.61 23.90 C ANISOU 1098 CG ALEU A 141 2776 3695 2609 38 88 -243 C ATOM 1099 CG BLEU A 141 -27.452 2.909 35.970 0.39 24.42 C ANISOU 1099 CG BLEU A 141 2833 3799 2646 37 102 -257 C ATOM 1100 CD1ALEU A 141 -26.265 1.733 36.025 0.61 24.82 C ANISOU 1100 CD1ALEU A 141 2915 3821 2692 -10 75 -197 C ATOM 1101 CD1BLEU A 141 -27.895 2.420 34.607 0.39 22.28 C ANISOU 1101 CD1BLEU A 141 2545 3500 2420 37 101 -222 C ATOM 1102 CD2ALEU A 141 -28.514 2.718 35.724 0.61 22.48 C ANISOU 1102 CD2ALEU A 141 2555 3589 2396 41 126 -258 C ATOM 1103 CD2BLEU A 141 -26.743 1.794 36.732 0.39 24.35 C ANISOU 1103 CD2BLEU A 141 2847 3808 2596 -13 91 -213 C ATOM 1104 N GLY A 142 -26.032 7.594 35.029 1.00 23.53 N ANISOU 1104 N GLY A 142 2780 3490 2670 174 42 -410 N ATOM 1105 CA GLY A 142 -25.470 8.865 35.460 1.00 23.34 C ANISOU 1105 CA GLY A 142 2785 3422 2660 196 22 -463 C ATOM 1106 C GLY A 142 -24.129 9.204 34.837 1.00 23.15 C ANISOU 1106 C GLY A 142 2791 3320 2684 177 -13 -439 C ATOM 1107 O GLY A 142 -23.674 10.344 34.942 1.00 24.73 O ANISOU 1107 O GLY A 142 3018 3469 2911 193 -34 -478 O ATOM 1108 N TRP A 143 -23.496 8.277 34.130 1.00 23.66 N ANISOU 1108 N TRP A 143 2853 3371 2766 144 -20 -378 N ATOM 1109 CA TRP A 143 -22.234 8.582 33.451 1.00 21.27 C ANISOU 1109 CA TRP A 143 2570 3001 2511 126 -47 -354 C ATOM 1110 C TRP A 143 -22.596 9.136 32.081 1.00 21.55 C ANISOU 1110 C TRP A 143 2606 2985 2597 151 -46 -341 C ATOM 1111 O TRP A 143 -22.489 8.464 31.047 1.00 20.89 O ANISOU 1111 O TRP A 143 2515 2890 2532 140 -40 -292 O ATOM 1112 CB TRP A 143 -21.357 7.349 33.348 1.00 20.45 C ANISOU 1112 CB TRP A 143 2461 2908 2401 86 -53 -299 C ATOM 1113 CG TRP A 143 -19.913 7.604 32.973 1.00 24.19 C ANISOU 1113 CG TRP A 143 2946 3329 2914 63 -80 -280 C ATOM 1114 CD1 TRP A 143 -19.312 8.811 32.621 1.00 20.96 C ANISOU 1114 CD1 TRP A 143 2554 2861 2548 67 -98 -301 C ATOM 1115 CD2 TRP A 143 -18.873 6.612 32.969 1.00 20.12 C ANISOU 1115 CD2 TRP A 143 2424 2820 2402 32 -91 -237 C ATOM 1116 NE1 TRP A 143 -17.955 8.587 32.394 1.00 21.71 N ANISOU 1116 NE1 TRP A 143 2647 2932 2670 35 -117 -271 N ATOM 1117 CE2 TRP A 143 -17.673 7.258 32.609 1.00 21.84 C ANISOU 1117 CE2 TRP A 143 2648 2989 2663 17 -113 -234 C ATOM 1118 CE3 TRP A 143 -18.850 5.241 33.263 1.00 21.53 C ANISOU 1118 CE3 TRP A 143 2593 3039 2551 15 -86 -200 C ATOM 1119 CZ2 TRP A 143 -16.461 6.573 32.506 1.00 24.83 C ANISOU 1119 CZ2 TRP A 143 3014 3363 3059 -8 -127 -198 C ATOM 1120 CZ3 TRP A 143 -17.637 4.547 33.161 1.00 22.65 C ANISOU 1120 CZ3 TRP A 143 2728 3167 2710 -7 -104 -164 C ATOM 1121 CH2 TRP A 143 -16.459 5.213 32.786 1.00 23.92 C ANISOU 1121 CH2 TRP A 143 2887 3286 2916 -16 -124 -164 C ATOM 1122 N ASN A 144 -23.034 10.389 32.082 1.00 21.20 N ANISOU 1122 N ASN A 144 2575 2908 2573 188 -52 -385 N ATOM 1123 CA ASN A 144 -23.497 11.019 30.851 1.00 23.98 C ANISOU 1123 CA ASN A 144 2931 3209 2969 217 -55 -374 C ATOM 1124 C ASN A 144 -23.147 12.504 30.884 1.00 25.87 C ANISOU 1124 C ASN A 144 3204 3379 3246 236 -80 -412 C ATOM 1125 O ASN A 144 -22.681 13.028 31.898 1.00 24.45 O ANISOU 1125 O ASN A 144 3041 3193 3054 230 -92 -455 O ATOM 1126 CB ASN A 144 -25.007 10.803 30.646 1.00 22.37 C ANISOU 1126 CB ASN A 144 2697 3050 2751 255 -33 -383 C ATOM 1127 CG ASN A 144 -25.849 11.368 31.781 1.00 23.70 C ANISOU 1127 CG ASN A 144 2855 3258 2892 292 -22 -448 C ATOM 1128 OD1 ASN A 144 -25.843 12.558 32.033 1.00 29.68 O ANISOU 1128 OD1 ASN A 144 3635 3971 3669 324 -36 -495 O ATOM 1129 ND2 ASN A 144 -26.620 10.504 32.445 1.00 22.63 N ANISOU 1129 ND2 ASN A 144 2686 3205 2708 287 6 -452 N ATOM 1130 N ASN A 145 -23.398 13.193 29.763 1.00 22.40 N ANISOU 1130 N ASN A 145 2778 2882 2850 259 -90 -396 N ATOM 1131 CA ASN A 145 -23.189 14.638 29.685 1.00 26.65 C ANISOU 1131 CA ASN A 145 3354 3343 3429 280 -116 -428 C ATOM 1132 C ASN A 145 -24.485 15.414 29.818 1.00 26.73 C ANISOU 1132 C ASN A 145 3362 3350 3446 347 -115 -476 C ATOM 1133 O ASN A 145 -24.523 16.583 29.438 1.00 28.83 O ANISOU 1133 O ASN A 145 3660 3542 3753 375 -139 -492 O ATOM 1134 CB ASN A 145 -22.519 15.057 28.359 1.00 28.05 C ANISOU 1134 CB ASN A 145 3557 3449 3653 260 -132 -376 C ATOM 1135 CG ASN A 145 -21.133 14.445 28.155 1.00 35.50 C ANISOU 1135 CG ASN A 145 4499 4390 4599 198 -132 -333 C ATOM 1136 OD1 ASN A 145 -20.390 14.232 29.096 1.00 33.82 O ANISOU 1136 OD1 ASN A 145 4284 4197 4370 169 -137 -351 O ATOM 1137 ND2 ASN A 145 -20.791 14.161 26.900 1.00 38.48 N ANISOU 1137 ND2 ASN A 145 4879 4747 4996 179 -127 -276 N ATOM 1138 N CYS A 146 -25.557 14.794 30.327 1.00 24.43 N ANISOU 1138 N CYS A 146 3030 3136 3115 374 -88 -496 N ATOM 1139 CA CYS A 146 -26.826 15.511 30.437 1.00 25.34 C ANISOU 1139 CA CYS A 146 3133 3256 3240 444 -84 -543 C ATOM 1140 C CYS A 146 -26.784 16.652 31.440 1.00 31.69 C ANISOU 1140 C CYS A 146 3966 4028 4048 476 -96 -620 C ATOM 1141 O CYS A 146 -27.557 17.622 31.307 1.00 30.72 O ANISOU 1141 O CYS A 146 3850 3869 3955 540 -106 -660 O ATOM 1142 CB CYS A 146 -27.937 14.524 30.801 1.00 32.51 C ANISOU 1142 CB CYS A 146 3984 4265 4105 457 -49 -547 C ATOM 1143 SG CYS A 146 -28.284 13.338 29.426 1.00 36.26 S ANISOU 1143 SG CYS A 146 4428 4766 4584 431 -43 -464 S ATOM 1144 N GLY A 147 -25.872 16.597 32.411 1.00 34.05 N ANISOU 1144 N GLY A 147 4285 4333 4320 437 -99 -644 N ATOM 1145 CA GLY A 147 -25.710 17.722 33.318 1.00 34.73 C ANISOU 1145 CA GLY A 147 4408 4380 4410 461 -116 -720 C ATOM 1146 C GLY A 147 -24.996 18.930 32.724 1.00 38.62 C ANISOU 1146 C GLY A 147 4955 4755 4965 460 -158 -720 C ATOM 1147 O GLY A 147 -24.944 19.969 33.382 1.00 43.29 O ANISOU 1147 O GLY A 147 5583 5298 5566 486 -177 -786 O ATOM 1148 N GLN A 148 -24.451 18.830 31.514 1.00 34.31 N ANISOU 1148 N GLN A 148 4418 4160 4457 428 -173 -648 N ATOM 1149 CA GLN A 148 -23.727 19.935 30.875 1.00 35.54 C ANISOU 1149 CA GLN A 148 4627 4206 4672 416 -212 -636 C ATOM 1150 C GLN A 148 -24.210 20.076 29.438 1.00 34.72 C ANISOU 1150 C GLN A 148 4524 4062 4607 438 -218 -578 C ATOM 1151 O GLN A 148 -23.468 19.830 28.482 1.00 36.34 O ANISOU 1151 O GLN A 148 4737 4240 4830 390 -224 -511 O ATOM 1152 CB GLN A 148 -22.217 19.699 30.923 1.00 47.60 C ANISOU 1152 CB GLN A 148 6169 5713 6202 335 -226 -602 C ATOM 1153 CG GLN A 148 -21.625 19.638 32.352 1.00 65.87 C ANISOU 1153 CG GLN A 148 8489 8061 8478 308 -231 -658 C ATOM 1154 CD GLN A 148 -21.272 21.022 32.933 1.00 77.05 C ANISOU 1154 CD GLN A 148 9960 9394 9923 315 -268 -722 C ATOM 1155 OE1 GLN A 148 -21.131 22.004 32.191 1.00 82.36 O ANISOU 1155 OE1 GLN A 148 10671 9970 10652 320 -295 -711 O ATOM 1156 NE2 GLN A 148 -21.124 21.097 34.265 1.00 76.13 N ANISOU 1156 NE2 GLN A 148 9851 9310 9764 312 -272 -790 N ATOM 1157 N PRO A 149 -25.478 20.413 29.250 1.00 33.93 N ANISOU 1157 N PRO A 149 4410 3967 4516 511 -215 -603 N ATOM 1158 CA PRO A 149 -26.026 20.438 27.893 1.00 32.10 C ANISOU 1158 CA PRO A 149 4175 3710 4313 533 -225 -545 C ATOM 1159 C PRO A 149 -25.364 21.550 27.089 1.00 33.70 C ANISOU 1159 C PRO A 149 4439 3794 4570 520 -265 -516 C ATOM 1160 O PRO A 149 -24.946 22.574 27.632 1.00 34.03 O ANISOU 1160 O PRO A 149 4526 3765 4639 524 -290 -560 O ATOM 1161 CB PRO A 149 -27.521 20.693 28.125 1.00 32.11 C ANISOU 1161 CB PRO A 149 4144 3743 4314 620 -218 -592 C ATOM 1162 CG PRO A 149 -27.582 21.431 29.404 1.00 34.33 C ANISOU 1162 CG PRO A 149 4442 4012 4590 652 -218 -681 C ATOM 1163 CD PRO A 149 -26.463 20.862 30.254 1.00 33.87 C ANISOU 1163 CD PRO A 149 4390 3986 4493 579 -205 -687 C ATOM 1164 N LYS A 150 -25.210 21.305 25.797 1.00 34.20 N ANISOU 1164 N LYS A 150 4508 3840 4648 497 -271 -439 N ATOM 1165 CA LYS A 150 -24.708 22.309 24.859 1.00 36.19 C ANISOU 1165 CA LYS A 150 4818 3985 4948 483 -307 -398 C ATOM 1166 C LYS A 150 -25.855 23.269 24.575 1.00 35.50 C ANISOU 1166 C LYS A 150 4749 3844 4896 568 -336 -421 C ATOM 1167 O LYS A 150 -26.634 23.088 23.631 1.00 33.44 O ANISOU 1167 O LYS A 150 4473 3594 4637 602 -343 -380 O ATOM 1168 CB LYS A 150 -24.209 21.666 23.571 1.00 32.94 C ANISOU 1168 CB LYS A 150 4405 3583 4529 431 -298 -309 C ATOM 1169 CG LYS A 150 -22.954 20.800 23.696 1.00 35.73 C ANISOU 1169 CG LYS A 150 4743 3976 4857 350 -272 -280 C ATOM 1170 CD LYS A 150 -22.058 21.015 22.508 1.00 38.29 C ANISOU 1170 CD LYS A 150 5100 4250 5201 294 -279 -206 C ATOM 1171 CE LYS A 150 -20.981 19.961 22.387 1.00 46.10 C ANISOU 1171 CE LYS A 150 6060 5294 6163 225 -247 -170 C ATOM 1172 NZ LYS A 150 -20.170 19.952 23.601 1.00 53.70 N ANISOU 1172 NZ LYS A 150 7013 6267 7125 193 -245 -215 N ATOM 1173 N GLU A 151 -25.956 24.313 25.402 1.00 37.47 N ANISOU 1173 N GLU A 151 5031 4032 5172 607 -358 -490 N ATOM 1174 CA GLU A 151 -27.144 25.161 25.367 1.00 40.96 C ANISOU 1174 CA GLU A 151 5481 4435 5647 703 -383 -530 C ATOM 1175 C GLU A 151 -27.165 26.077 24.149 1.00 36.51 C ANISOU 1175 C GLU A 151 4973 3763 5134 716 -429 -472 C ATOM 1176 O GLU A 151 -28.242 26.440 23.672 1.00 41.04 O ANISOU 1176 O GLU A 151 5540 4323 5730 793 -450 -471 O ATOM 1177 CB GLU A 151 -27.235 25.964 26.664 1.00 49.52 C ANISOU 1177 CB GLU A 151 6587 5487 6742 743 -390 -629 C ATOM 1178 CG GLU A 151 -28.632 26.059 27.186 1.00 57.80 C ANISOU 1178 CG GLU A 151 7592 6583 7787 844 -378 -696 C ATOM 1179 CD GLU A 151 -29.081 24.796 27.865 1.00 58.34 C ANISOU 1179 CD GLU A 151 7583 6793 7792 838 -324 -716 C ATOM 1180 OE1 GLU A 151 -29.904 24.058 27.294 1.00 60.61 O ANISOU 1180 OE1 GLU A 151 7814 7150 8064 859 -308 -681 O ATOM 1181 OE2 GLU A 151 -28.621 24.558 28.991 1.00 63.65 O ANISOU 1181 OE2 GLU A 151 8252 7505 8429 809 -301 -768 O ATOM 1182 N GLY A 152 -26.005 26.455 23.616 1.00 38.22 N ANISOU 1182 N GLY A 152 5244 3907 5370 642 -447 -419 N ATOM 1183 CA GLY A 152 -26.004 27.230 22.382 1.00 39.26 C ANISOU 1183 CA GLY A 152 5431 3945 5542 644 -488 -350 C ATOM 1184 C GLY A 152 -26.505 26.423 21.202 1.00 41.52 C ANISOU 1184 C GLY A 152 5685 4291 5802 645 -478 -276 C ATOM 1185 O GLY A 152 -27.252 26.925 20.359 1.00 41.71 O ANISOU 1185 O GLY A 152 5728 4270 5848 697 -513 -243 O ATOM 1186 N LYS A 153 -26.124 25.148 21.133 1.00 35.87 N ANISOU 1186 N LYS A 153 4919 3674 5036 591 -434 -250 N ATOM 1187 CA LYS A 153 -26.633 24.333 20.048 1.00 33.61 C ANISOU 1187 CA LYS A 153 4604 3446 4721 592 -426 -187 C ATOM 1188 C LYS A 153 -28.122 24.033 20.241 1.00 35.30 C ANISOU 1188 C LYS A 153 4763 3722 4927 679 -427 -225 C ATOM 1189 O LYS A 153 -28.884 23.978 19.266 1.00 35.76 O ANISOU 1189 O LYS A 153 4816 3786 4986 713 -449 -182 O ATOM 1190 CB LYS A 153 -25.782 23.069 19.955 1.00 34.44 C ANISOU 1190 CB LYS A 153 4675 3632 4778 512 -379 -156 C ATOM 1191 CG LYS A 153 -26.182 22.110 18.920 1.00 36.38 C ANISOU 1191 CG LYS A 153 4893 3941 4987 504 -366 -99 C ATOM 1192 CD LYS A 153 -25.312 20.865 19.023 1.00 39.76 C ANISOU 1192 CD LYS A 153 5288 4444 5373 432 -320 -82 C ATOM 1193 CE LYS A 153 -23.810 21.175 18.928 1.00 39.29 C ANISOU 1193 CE LYS A 153 5267 4336 5326 355 -312 -53 C ATOM 1194 NZ LYS A 153 -22.952 19.943 18.789 1.00 35.65 N ANISOU 1194 NZ LYS A 153 4772 3945 4826 292 -269 -27 N ATOM 1195 N ALA A 154 -28.561 23.868 21.487 1.00 36.70 N ANISOU 1195 N ALA A 154 4898 3948 5096 716 -405 -305 N ATOM 1196 CA ALA A 154 -29.978 23.629 21.735 1.00 35.82 C ANISOU 1196 CA ALA A 154 4728 3901 4980 798 -402 -345 C ATOM 1197 C ALA A 154 -30.812 24.855 21.345 1.00 34.19 C ANISOU 1197 C ALA A 154 4551 3611 4828 885 -453 -355 C ATOM 1198 O ALA A 154 -31.881 24.719 20.728 1.00 38.37 O ANISOU 1198 O ALA A 154 5045 4171 5361 941 -471 -337 O ATOM 1199 CB ALA A 154 -30.200 23.242 23.204 1.00 29.05 C ANISOU 1199 CB ALA A 154 3823 3115 4098 814 -363 -429 C ATOM 1200 N HIS A 155 -30.323 26.064 21.647 1.00 33.64 N ANISOU 1200 N HIS A 155 4549 3431 4803 897 -484 -381 N ATOM 1201 CA HIS A 155 -31.071 27.265 21.249 1.00 38.70 C ANISOU 1201 CA HIS A 155 5226 3978 5500 983 -539 -387 C ATOM 1202 C HIS A 155 -31.042 27.462 19.735 1.00 38.14 C ANISOU 1202 C HIS A 155 5195 3855 5441 967 -579 -288 C ATOM 1203 O HIS A 155 -32.066 27.796 19.134 1.00 39.46 O ANISOU 1203 O HIS A 155 5352 4010 5631 1042 -617 -273 O ATOM 1204 CB HIS A 155 -30.532 28.505 21.963 1.00 44.36 C ANISOU 1204 CB HIS A 155 6012 4580 6263 996 -564 -441 C ATOM 1205 CG HIS A 155 -30.645 28.442 23.456 1.00 55.87 C ANISOU 1205 CG HIS A 155 7438 6083 7706 1022 -529 -546 C ATOM 1206 ND1 HIS A 155 -31.666 27.776 24.099 1.00 59.58 N ANISOU 1206 ND1 HIS A 155 7825 6666 8147 1079 -493 -601 N ATOM 1207 CD2 HIS A 155 -29.854 28.947 24.432 1.00 58.45 C ANISOU 1207 CD2 HIS A 155 7805 6363 8039 993 -525 -604 C ATOM 1208 CE1 HIS A 155 -31.510 27.885 25.406 1.00 60.08 C ANISOU 1208 CE1 HIS A 155 7882 6750 8195 1087 -465 -688 C ATOM 1209 NE2 HIS A 155 -30.414 28.587 25.635 1.00 60.41 N ANISOU 1209 NE2 HIS A 155 8000 6696 8257 1036 -487 -694 N ATOM 1210 N SER A 156 -29.898 27.212 19.090 1.00 36.62 N ANISOU 1210 N SER A 156 5043 3641 5228 870 -572 -218 N ATOM 1211 CA SER A 156 -29.842 27.410 17.645 1.00 39.04 C ANISOU 1211 CA SER A 156 5393 3902 5537 850 -608 -122 C ATOM 1212 C SER A 156 -30.861 26.533 16.912 1.00 42.09 C ANISOU 1212 C SER A 156 5719 4382 5890 883 -607 -91 C ATOM 1213 O SER A 156 -31.460 26.971 15.921 1.00 41.80 O ANISOU 1213 O SER A 156 5707 4307 5870 922 -655 -40 O ATOM 1214 CB SER A 156 -28.412 27.180 17.135 1.00 39.27 C ANISOU 1214 CB SER A 156 5466 3910 5543 736 -588 -58 C ATOM 1215 OG SER A 156 -27.980 25.841 17.330 1.00 51.45 O ANISOU 1215 OG SER A 156 6952 5565 7032 677 -531 -57 O ATOM 1216 N GLN A 157 -31.117 25.325 17.402 1.00 40.71 N ANISOU 1216 N GLN A 157 5469 4328 5672 869 -558 -121 N ATOM 1217 CA GLN A 157 -32.098 24.444 16.780 1.00 41.79 C ANISOU 1217 CA GLN A 157 5545 4555 5778 894 -558 -97 C ATOM 1218 C GLN A 157 -33.513 24.649 17.284 1.00 39.37 C ANISOU 1218 C GLN A 157 5177 4285 5496 998 -573 -156 C ATOM 1219 O GLN A 157 -34.381 23.837 16.954 1.00 43.37 O ANISOU 1219 O GLN A 157 5619 4881 5978 1015 -569 -147 O ATOM 1220 CB GLN A 157 -31.750 22.981 17.038 1.00 41.92 C ANISOU 1220 CB GLN A 157 5507 4684 5736 827 -499 -98 C ATOM 1221 CG GLN A 157 -30.481 22.497 16.461 1.00 51.77 C ANISOU 1221 CG GLN A 157 6794 5923 6952 730 -476 -40 C ATOM 1222 CD GLN A 157 -30.467 20.999 16.493 1.00 53.31 C ANISOU 1222 CD GLN A 157 6932 6230 7094 685 -430 -37 C ATOM 1223 OE1 GLN A 157 -31.480 20.366 16.833 1.00 54.56 O ANISOU 1223 OE1 GLN A 157 7025 6467 7239 723 -422 -69 O ATOM 1224 NE2 GLN A 157 -29.339 20.417 16.155 1.00 56.79 N ANISOU 1224 NE2 GLN A 157 7395 6678 7504 604 -401 1 N ATOM 1225 N GLY A 158 -33.753 25.626 18.149 1.00 38.94 N ANISOU 1225 N GLY A 158 5134 4172 5488 1063 -586 -223 N ATOM 1226 CA GLY A 158 -35.089 25.826 18.672 1.00 33.86 C ANISOU 1226 CA GLY A 158 4425 3570 4869 1166 -595 -286 C ATOM 1227 C GLY A 158 -35.569 24.766 19.642 1.00 40.19 C ANISOU 1227 C GLY A 158 5135 4504 5632 1164 -535 -345 C ATOM 1228 O GLY A 158 -36.780 24.580 19.780 1.00 42.41 O ANISOU 1228 O GLY A 158 5342 4852 5921 1233 -536 -376 O ATOM 1229 N CYS A 159 -34.665 24.060 20.325 1.00 36.40 N ANISOU 1229 N CYS A 159 4655 4064 5112 1085 -483 -360 N ATOM 1230 CA CYS A 159 -35.102 23.060 21.288 1.00 37.12 C ANISOU 1230 CA CYS A 159 4665 4277 5163 1078 -427 -412 C ATOM 1231 C CYS A 159 -35.779 23.725 22.475 1.00 38.26 C ANISOU 1231 C CYS A 159 4779 4428 5331 1161 -415 -508 C ATOM 1232 O CYS A 159 -35.486 24.862 22.824 1.00 45.00 O ANISOU 1232 O CYS A 159 5689 5184 6224 1200 -439 -545 O ATOM 1233 CB CYS A 159 -33.928 22.207 21.779 1.00 36.58 C ANISOU 1233 CB CYS A 159 4610 4242 5047 978 -381 -403 C ATOM 1234 SG CYS A 159 -33.143 21.336 20.426 1.00 37.95 S ANISOU 1234 SG CYS A 159 4812 4419 5189 886 -386 -300 S ATOM 1235 N GLY A 160 -36.687 22.992 23.102 1.00 39.08 N ANISOU 1235 N GLY A 160 4793 4646 5408 1187 -377 -550 N ATOM 1236 CA GLY A 160 -37.391 23.479 24.265 1.00 42.36 C ANISOU 1236 CA GLY A 160 5169 5090 5835 1264 -353 -645 C ATOM 1237 C GLY A 160 -36.604 23.232 25.535 1.00 47.40 C ANISOU 1237 C GLY A 160 5822 5753 6433 1215 -304 -699 C ATOM 1238 O GLY A 160 -35.518 22.651 25.531 1.00 43.69 O ANISOU 1238 O GLY A 160 5388 5280 5930 1123 -289 -661 O ATOM 1239 N GLU A 161 -37.186 23.681 26.646 1.00 55.45 N ANISOU 1239 N GLU A 161 6811 6802 7455 1282 -278 -790 N ATOM 1240 CA GLU A 161 -36.533 23.576 27.942 1.00 60.58 C ANISOU 1240 CA GLU A 161 7479 7476 8064 1246 -236 -852 C ATOM 1241 C GLU A 161 -36.339 22.123 28.332 1.00 56.37 C ANISOU 1241 C GLU A 161 6895 7061 7461 1162 -184 -826 C ATOM 1242 O GLU A 161 -37.221 21.284 28.130 1.00 56.58 O ANISOU 1242 O GLU A 161 6844 7186 7468 1166 -161 -806 O ATOM 1243 CB GLU A 161 -37.352 24.300 29.010 1.00 71.74 C ANISOU 1243 CB GLU A 161 8862 8910 9487 1342 -215 -959 C ATOM 1244 CG GLU A 161 -37.388 25.803 28.810 1.00 79.50 C ANISOU 1244 CG GLU A 161 9909 9758 10539 1425 -267 -997 C ATOM 1245 CD GLU A 161 -36.017 26.360 28.486 1.00 84.18 C ANISOU 1245 CD GLU A 161 10608 10224 11151 1361 -307 -961 C ATOM 1246 OE1 GLU A 161 -35.182 26.474 29.411 1.00 85.29 O ANISOU 1246 OE1 GLU A 161 10791 10351 11265 1318 -289 -1006 O ATOM 1247 OE2 GLU A 161 -35.764 26.658 27.297 1.00 86.58 O ANISOU 1247 OE2 GLU A 161 10954 10448 11495 1348 -357 -885 O ATOM 1248 N GLY A 162 -35.168 21.831 28.902 1.00 56.12 N ANISOU 1248 N GLY A 162 6910 7017 7394 1085 -168 -824 N ATOM 1249 CA GLY A 162 -34.783 20.481 29.238 1.00 50.75 C ANISOU 1249 CA GLY A 162 6200 6431 6653 1000 -128 -791 C ATOM 1250 C GLY A 162 -34.346 19.638 28.062 1.00 51.51 C ANISOU 1250 C GLY A 162 6300 6524 6747 933 -143 -694 C ATOM 1251 O GLY A 162 -33.969 18.477 28.267 1.00 58.19 O ANISOU 1251 O GLY A 162 7126 7437 7545 862 -113 -663 O ATOM 1252 N GLN A 163 -34.390 20.169 26.837 1.00 45.40 N ANISOU 1252 N GLN A 163 5555 5674 6020 953 -189 -646 N ATOM 1253 CA GLN A 163 -34.035 19.382 25.662 1.00 40.71 C ANISOU 1253 CA GLN A 163 4967 5081 5420 893 -202 -558 C ATOM 1254 C GLN A 163 -32.638 19.753 25.166 1.00 37.84 C ANISOU 1254 C GLN A 163 4684 4622 5070 835 -226 -515 C ATOM 1255 O GLN A 163 -32.154 20.870 25.377 1.00 36.67 O ANISOU 1255 O GLN A 163 4592 4383 4956 856 -251 -542 O ATOM 1256 CB GLN A 163 -35.045 19.575 24.521 1.00 36.94 C ANISOU 1256 CB GLN A 163 4463 4598 4974 945 -237 -522 C ATOM 1257 CG GLN A 163 -36.450 19.001 24.752 1.00 31.77 C ANISOU 1257 CG GLN A 163 3714 4051 4306 989 -216 -547 C ATOM 1258 CD GLN A 163 -37.299 19.121 23.490 1.00 38.23 C ANISOU 1258 CD GLN A 163 4510 4861 5155 1029 -260 -500 C ATOM 1259 OE1 GLN A 163 -37.089 20.023 22.656 1.00 38.80 O ANISOU 1259 OE1 GLN A 163 4637 4836 5267 1058 -309 -472 O ATOM 1260 NE2 GLN A 163 -38.264 18.222 23.342 1.00 41.90 N ANISOU 1260 NE2 GLN A 163 4895 5426 5599 1027 -245 -490 N ATOM 1261 N VAL A 164 -32.013 18.798 24.475 1.00 29.28 N ANISOU 1261 N VAL A 164 3605 3559 3961 762 -219 -448 N ATOM 1262 CA VAL A 164 -30.726 18.975 23.813 1.00 31.44 C ANISOU 1262 CA VAL A 164 3943 3758 4245 702 -236 -396 C ATOM 1263 C VAL A 164 -30.884 18.553 22.354 1.00 28.55 C ANISOU 1263 C VAL A 164 3581 3389 3880 685 -255 -320 C ATOM 1264 O VAL A 164 -31.748 17.744 22.011 1.00 28.68 O ANISOU 1264 O VAL A 164 3545 3476 3874 694 -247 -305 O ATOM 1265 CB VAL A 164 -29.600 18.130 24.475 1.00 30.21 C ANISOU 1265 CB VAL A 164 3790 3636 4051 624 -203 -392 C ATOM 1266 CG1 VAL A 164 -29.451 18.436 25.937 1.00 33.25 C ANISOU 1266 CG1 VAL A 164 4172 4036 4424 635 -186 -465 C ATOM 1267 CG2 VAL A 164 -29.863 16.635 24.293 1.00 31.01 C ANISOU 1267 CG2 VAL A 164 3842 3832 4109 586 -173 -359 C ATOM 1268 N ALA A 165 -30.023 19.089 21.496 1.00 24.86 N ANISOU 1268 N ALA A 165 3174 2839 3432 654 -280 -271 N ATOM 1269 CA ALA A 165 -29.832 18.470 20.188 1.00 28.40 C ANISOU 1269 CA ALA A 165 3632 3294 3863 615 -286 -196 C ATOM 1270 C ALA A 165 -29.267 17.065 20.395 1.00 29.49 C ANISOU 1270 C ALA A 165 3742 3507 3956 548 -244 -182 C ATOM 1271 O ALA A 165 -28.209 16.902 21.017 1.00 29.95 O ANISOU 1271 O ALA A 165 3815 3559 4007 502 -223 -192 O ATOM 1272 CB ALA A 165 -28.881 19.308 19.319 1.00 28.87 C ANISOU 1272 CB ALA A 165 3764 3257 3948 585 -313 -146 C ATOM 1273 N CYS A 166 -29.957 16.045 19.893 1.00 25.40 N ANISOU 1273 N CYS A 166 3183 3058 3409 544 -235 -160 N ATOM 1274 CA CYS A 166 -29.596 14.670 20.241 1.00 26.03 C ANISOU 1274 CA CYS A 166 3232 3209 3448 490 -197 -155 C ATOM 1275 C CYS A 166 -28.490 14.213 19.302 1.00 29.63 C ANISOU 1275 C CYS A 166 3727 3640 3890 430 -192 -98 C ATOM 1276 O CYS A 166 -28.760 13.823 18.164 1.00 30.89 O ANISOU 1276 O CYS A 166 3893 3807 4036 421 -203 -55 O ATOM 1277 CB CYS A 166 -30.808 13.750 20.156 1.00 30.60 C ANISOU 1277 CB CYS A 166 3753 3870 4004 506 -191 -158 C ATOM 1278 SG CYS A 166 -30.399 12.071 20.643 1.00 31.95 S ANISOU 1278 SG CYS A 166 3894 4118 4128 440 -149 -151 S ATOM 1279 N LEU A 167 -27.241 14.273 19.786 1.00 26.87 N ANISOU 1279 N LEU A 167 3401 3265 3544 388 -174 -101 N ATOM 1280 CA LEU A 167 -26.037 13.951 19.033 1.00 23.00 C ANISOU 1280 CA LEU A 167 2942 2751 3045 331 -163 -54 C ATOM 1281 C LEU A 167 -25.154 13.081 19.906 1.00 21.61 C ANISOU 1281 C LEU A 167 2746 2611 2852 289 -131 -69 C ATOM 1282 O LEU A 167 -24.896 13.432 21.068 1.00 23.17 O ANISOU 1282 O LEU A 167 2938 2807 3059 293 -129 -110 O ATOM 1283 CB LEU A 167 -25.288 15.220 18.611 1.00 25.35 C ANISOU 1283 CB LEU A 167 3293 2962 3377 324 -184 -34 C ATOM 1284 CG LEU A 167 -26.124 16.072 17.638 1.00 30.43 C ANISOU 1284 CG LEU A 167 3963 3561 4036 366 -221 -9 C ATOM 1285 CD1 LEU A 167 -25.537 17.449 17.487 1.00 30.61 C ANISOU 1285 CD1 LEU A 167 4040 3491 4098 365 -247 2 C ATOM 1286 CD2 LEU A 167 -26.190 15.340 16.306 1.00 30.64 C ANISOU 1286 CD2 LEU A 167 3997 3613 4031 343 -218 47 C ATOM 1287 N PHE A 168 -24.686 11.965 19.332 1.00 22.73 N ANISOU 1287 N PHE A 168 2883 2786 2968 250 -110 -36 N ATOM 1288 CA PHE A 168 -23.980 10.939 20.095 1.00 22.20 C ANISOU 1288 CA PHE A 168 2793 2759 2883 216 -84 -46 C ATOM 1289 C PHE A 168 -22.880 11.535 20.967 1.00 22.35 C ANISOU 1289 C PHE A 168 2822 2747 2922 196 -83 -65 C ATOM 1290 O PHE A 168 -22.858 11.320 22.195 1.00 22.48 O ANISOU 1290 O PHE A 168 2818 2793 2932 197 -78 -101 O ATOM 1291 CB PHE A 168 -23.398 9.872 19.145 1.00 23.53 C ANISOU 1291 CB PHE A 168 2966 2944 3030 180 -64 -5 C ATOM 1292 CG PHE A 168 -22.785 8.686 19.878 1.00 21.70 C ANISOU 1292 CG PHE A 168 2710 2753 2782 152 -41 -13 C ATOM 1293 CD1 PHE A 168 -21.458 8.728 20.337 1.00 21.43 C ANISOU 1293 CD1 PHE A 168 2679 2703 2761 123 -31 -12 C ATOM 1294 CD2 PHE A 168 -23.537 7.577 20.150 1.00 24.56 C ANISOU 1294 CD2 PHE A 168 3047 3167 3118 154 -34 -20 C ATOM 1295 CE1 PHE A 168 -20.902 7.638 21.040 1.00 20.38 C ANISOU 1295 CE1 PHE A 168 2524 2606 2615 102 -16 -17 C ATOM 1296 CE2 PHE A 168 -22.984 6.482 20.848 1.00 26.51 C ANISOU 1296 CE2 PHE A 168 3277 3444 3350 129 -18 -23 C ATOM 1297 CZ PHE A 168 -21.662 6.527 21.291 1.00 20.25 C ANISOU 1297 CZ PHE A 168 2488 2635 2571 107 -10 -21 C ATOM 1298 N GLU A 169 -21.958 12.286 20.354 1.00 19.45 N ANISOU 1298 N GLU A 169 2486 2324 2579 173 -88 -39 N ATOM 1299 CA GLU A 169 -20.793 12.755 21.107 1.00 20.38 C ANISOU 1299 CA GLU A 169 2611 2416 2718 143 -89 -53 C ATOM 1300 C GLU A 169 -21.118 13.914 22.040 1.00 23.62 C ANISOU 1300 C GLU A 169 3034 2790 3151 170 -113 -100 C ATOM 1301 O GLU A 169 -20.266 14.306 22.842 1.00 25.12 O ANISOU 1301 O GLU A 169 3228 2962 3355 146 -119 -121 O ATOM 1302 CB GLU A 169 -19.649 13.158 20.168 1.00 22.84 C ANISOU 1302 CB GLU A 169 2946 2684 3048 102 -84 -10 C ATOM 1303 CG GLU A 169 -19.058 11.942 19.434 1.00 20.29 C ANISOU 1303 CG GLU A 169 2606 2401 2701 74 -53 26 C ATOM 1304 CD GLU A 169 -17.752 12.230 18.690 1.00 22.74 C ANISOU 1304 CD GLU A 169 2928 2683 3027 28 -38 64 C ATOM 1305 OE1 GLU A 169 -17.113 13.293 18.941 1.00 25.14 O ANISOU 1305 OE1 GLU A 169 3249 2940 3364 7 -52 62 O ATOM 1306 OE2 GLU A 169 -17.372 11.371 17.854 1.00 23.49 O ANISOU 1306 OE2 GLU A 169 3017 2807 3103 12 -11 93 O ATOM 1307 N ASP A 170 -22.309 14.468 21.956 1.00 21.54 N ANISOU 1307 N ASP A 170 2777 2517 2892 220 -130 -118 N ATOM 1308 CA ASP A 170 -22.702 15.474 22.940 1.00 23.45 C ANISOU 1308 CA ASP A 170 3028 2730 3153 254 -150 -173 C ATOM 1309 C ASP A 170 -23.245 14.836 24.218 1.00 25.03 C ANISOU 1309 C ASP A 170 3190 2998 3322 271 -135 -223 C ATOM 1310 O ASP A 170 -23.141 15.438 25.290 1.00 29.74 O ANISOU 1310 O ASP A 170 3794 3583 3923 282 -143 -273 O ATOM 1311 CB ASP A 170 -23.781 16.416 22.385 1.00 22.74 C ANISOU 1311 CB ASP A 170 2957 2597 3084 310 -175 -177 C ATOM 1312 CG ASP A 170 -23.258 17.358 21.269 1.00 31.56 C ANISOU 1312 CG ASP A 170 4125 3632 4234 294 -198 -131 C ATOM 1313 OD1 ASP A 170 -22.041 17.357 20.958 1.00 30.49 O ANISOU 1313 OD1 ASP A 170 4006 3472 4105 237 -190 -99 O ATOM 1314 OD2 ASP A 170 -24.087 18.134 20.716 1.00 31.74 O ANISOU 1314 OD2 ASP A 170 4169 3613 4277 339 -225 -126 O ATOM 1315 N VAL A 171 -23.873 13.663 24.144 1.00 22.41 N ANISOU 1315 N VAL A 171 2822 2736 2957 274 -114 -211 N ATOM 1316 CA VAL A 171 -24.508 13.110 25.331 1.00 23.99 C ANISOU 1316 CA VAL A 171 2988 3002 3125 290 -99 -254 C ATOM 1317 C VAL A 171 -23.726 11.940 25.943 1.00 21.41 C ANISOU 1317 C VAL A 171 2644 2723 2768 243 -79 -242 C ATOM 1318 O VAL A 171 -23.761 11.768 27.164 1.00 26.28 O ANISOU 1318 O VAL A 171 3247 3377 3360 242 -73 -279 O ATOM 1319 CB VAL A 171 -25.974 12.713 25.067 1.00 25.40 C ANISOU 1319 CB VAL A 171 3133 3230 3289 330 -91 -258 C ATOM 1320 CG1 VAL A 171 -26.765 13.956 24.600 1.00 25.57 C ANISOU 1320 CG1 VAL A 171 3169 3202 3344 386 -116 -274 C ATOM 1321 CG2 VAL A 171 -26.081 11.540 24.062 1.00 18.23 C ANISOU 1321 CG2 VAL A 171 2210 2352 2363 303 -81 -205 C ATOM 1322 N VAL A 172 -23.014 11.143 25.158 1.00 20.18 N ANISOU 1322 N VAL A 172 2489 2568 2611 206 -71 -193 N ATOM 1323 CA VAL A 172 -22.311 9.965 25.670 1.00 18.72 C ANISOU 1323 CA VAL A 172 2288 2425 2402 169 -57 -180 C ATOM 1324 C VAL A 172 -20.873 10.393 25.965 1.00 21.99 C ANISOU 1324 C VAL A 172 2717 2802 2836 136 -67 -178 C ATOM 1325 O VAL A 172 -20.183 10.854 25.044 1.00 22.84 O ANISOU 1325 O VAL A 172 2843 2863 2973 120 -71 -150 O ATOM 1326 CB VAL A 172 -22.349 8.783 24.682 1.00 22.12 C ANISOU 1326 CB VAL A 172 2708 2876 2820 152 -42 -134 C ATOM 1327 CG1 VAL A 172 -21.661 7.567 25.310 1.00 20.61 C ANISOU 1327 CG1 VAL A 172 2502 2723 2607 120 -30 -123 C ATOM 1328 CG2 VAL A 172 -23.807 8.443 24.274 1.00 21.78 C ANISOU 1328 CG2 VAL A 172 2649 2867 2761 179 -38 -134 C ATOM 1329 N PRO A 173 -20.398 10.291 27.213 1.00 27.64 N ANISOU 1329 N PRO A 173 3425 3539 3536 122 -72 -206 N ATOM 1330 CA PRO A 173 -19.017 10.715 27.503 1.00 21.93 C ANISOU 1330 CA PRO A 173 2712 2784 2835 88 -88 -205 C ATOM 1331 C PRO A 173 -18.011 9.843 26.784 1.00 21.15 C ANISOU 1331 C PRO A 173 2600 2689 2746 55 -77 -156 C ATOM 1332 O PRO A 173 -18.152 8.613 26.737 1.00 19.72 O ANISOU 1332 O PRO A 173 2402 2550 2542 53 -62 -136 O ATOM 1333 CB PRO A 173 -18.886 10.534 29.026 1.00 22.47 C ANISOU 1333 CB PRO A 173 2773 2892 2873 82 -97 -243 C ATOM 1334 CG PRO A 173 -20.304 10.458 29.542 1.00 26.42 C ANISOU 1334 CG PRO A 173 3266 3432 3340 120 -85 -275 C ATOM 1335 CD PRO A 173 -21.067 9.754 28.414 1.00 24.88 C ANISOU 1335 CD PRO A 173 3058 3250 3145 132 -65 -237 C ATOM 1336 N MET A 174 -16.963 10.489 26.258 1.00 18.70 N ANISOU 1336 N MET A 174 2299 2333 2471 29 -84 -140 N ATOM 1337 CA MET A 174 -15.944 9.746 25.526 1.00 23.22 C ANISOU 1337 CA MET A 174 2855 2912 3056 1 -69 -97 C ATOM 1338 C MET A 174 -15.043 8.945 26.470 1.00 21.59 C ANISOU 1338 C MET A 174 2621 2741 2842 -19 -77 -99 C ATOM 1339 O MET A 174 -14.547 7.884 26.082 1.00 20.78 O ANISOU 1339 O MET A 174 2498 2660 2736 -26 -61 -70 O ATOM 1340 CB MET A 174 -15.123 10.711 24.662 1.00 23.42 C ANISOU 1340 CB MET A 174 2894 2884 3121 -24 -71 -76 C ATOM 1341 CG MET A 174 -14.443 10.065 23.479 1.00 27.78 C ANISOU 1341 CG MET A 174 3433 3441 3680 -42 -43 -30 C ATOM 1342 SD MET A 174 -15.568 9.164 22.360 1.00 26.19 S ANISOU 1342 SD MET A 174 3241 3262 3448 -11 -18 -6 S ATOM 1343 CE MET A 174 -16.006 10.450 21.170 1.00 27.65 C ANISOU 1343 CE MET A 174 3466 3390 3648 -8 -21 13 C ATOM 1344 N ASN A 175 -14.888 9.369 27.739 1.00 18.92 N ANISOU 1344 N ASN A 175 2283 2409 2494 -25 -102 -135 N ATOM 1345 CA ASN A 175 -14.136 8.508 28.652 1.00 19.86 C ANISOU 1345 CA ASN A 175 2378 2568 2599 -41 -114 -133 C ATOM 1346 C ASN A 175 -14.888 7.200 28.911 1.00 18.23 C ANISOU 1346 C ASN A 175 2164 2410 2352 -22 -100 -122 C ATOM 1347 O ASN A 175 -14.267 6.137 29.006 1.00 19.60 O ANISOU 1347 O ASN A 175 2318 2607 2523 -31 -99 -97 O ATOM 1348 CB ASN A 175 -13.760 9.226 29.968 1.00 20.78 C ANISOU 1348 CB ASN A 175 2501 2686 2709 -55 -148 -174 C ATOM 1349 CG ASN A 175 -14.945 9.924 30.683 1.00 25.83 C ANISOU 1349 CG ASN A 175 3168 3327 3319 -28 -153 -223 C ATOM 1350 OD1 ASN A 175 -16.134 9.669 30.433 1.00 23.44 O ANISOU 1350 OD1 ASN A 175 2872 3040 2995 3 -132 -226 O ATOM 1351 ND2 ASN A 175 -14.594 10.821 31.592 1.00 24.53 N ANISOU 1351 ND2 ASN A 175 3018 3147 3155 -40 -182 -264 N ATOM 1352 N TYR A 176 -16.221 7.241 28.999 1.00 17.45 N ANISOU 1352 N TYR A 176 2080 2325 2227 3 -89 -140 N ATOM 1353 CA TYR A 176 -16.975 5.979 29.035 1.00 17.33 C ANISOU 1353 CA TYR A 176 2056 2352 2178 13 -72 -122 C ATOM 1354 C TYR A 176 -16.725 5.158 27.761 1.00 21.13 C ANISOU 1354 C TYR A 176 2531 2821 2676 11 -53 -81 C ATOM 1355 O TYR A 176 -16.520 3.928 27.806 1.00 16.22 O ANISOU 1355 O TYR A 176 1900 2221 2042 6 -48 -57 O ATOM 1356 CB TYR A 176 -18.499 6.246 29.193 1.00 17.47 C ANISOU 1356 CB TYR A 176 2082 2389 2168 39 -61 -147 C ATOM 1357 CG TYR A 176 -19.323 5.002 28.810 1.00 19.61 C ANISOU 1357 CG TYR A 176 2344 2693 2416 43 -41 -121 C ATOM 1358 CD1 TYR A 176 -19.625 4.014 29.781 1.00 20.70 C ANISOU 1358 CD1 TYR A 176 2474 2879 2513 32 -41 -117 C ATOM 1359 CD2 TYR A 176 -19.799 4.824 27.500 1.00 16.89 C ANISOU 1359 CD2 TYR A 176 2001 2331 2086 53 -27 -99 C ATOM 1360 CE1 TYR A 176 -20.336 2.850 29.457 1.00 18.41 C ANISOU 1360 CE1 TYR A 176 2178 2613 2204 28 -26 -90 C ATOM 1361 CE2 TYR A 176 -20.502 3.651 27.145 1.00 17.69 C ANISOU 1361 CE2 TYR A 176 2096 2459 2167 50 -14 -77 C ATOM 1362 CZ TYR A 176 -20.759 2.663 28.129 1.00 20.49 C ANISOU 1362 CZ TYR A 176 2443 2857 2487 36 -14 -72 C ATOM 1363 OH TYR A 176 -21.444 1.508 27.770 1.00 23.04 O ANISOU 1363 OH TYR A 176 2763 3200 2793 27 -4 -49 O ATOM 1364 N MET A 177 -16.790 5.818 26.600 1.00 16.51 N ANISOU 1364 N MET A 177 1956 2201 2117 17 -42 -72 N ATOM 1365 CA MET A 177 -16.667 5.065 25.351 1.00 20.55 C ANISOU 1365 CA MET A 177 2467 2706 2636 17 -21 -38 C ATOM 1366 C MET A 177 -15.303 4.399 25.225 1.00 18.41 C ANISOU 1366 C MET A 177 2177 2434 2383 0 -18 -16 C ATOM 1367 O MET A 177 -15.201 3.287 24.695 1.00 17.16 O ANISOU 1367 O MET A 177 2015 2286 2219 4 -3 5 O ATOM 1368 CB MET A 177 -16.933 5.963 24.142 1.00 18.43 C ANISOU 1368 CB MET A 177 2217 2402 2386 23 -12 -30 C ATOM 1369 CG MET A 177 -18.418 6.323 23.977 1.00 20.67 C ANISOU 1369 CG MET A 177 2514 2690 2652 49 -13 -44 C ATOM 1370 SD MET A 177 -19.498 4.898 23.862 1.00 20.64 S ANISOU 1370 SD MET A 177 2501 2730 2612 58 -2 -35 S ATOM 1371 CE MET A 177 -18.860 4.119 22.381 1.00 22.10 C ANISOU 1371 CE MET A 177 2695 2899 2804 47 17 2 C ATOM 1372 N VAL A 178 -14.248 5.071 25.659 1.00 18.41 N ANISOU 1372 N VAL A 178 2165 2421 2409 -18 -32 -22 N ATOM 1373 CA VAL A 178 -12.895 4.538 25.450 1.00 19.54 C ANISOU 1373 CA VAL A 178 2282 2567 2577 -32 -28 -1 C ATOM 1374 C VAL A 178 -12.465 3.579 26.571 1.00 18.51 C ANISOU 1374 C VAL A 178 2132 2466 2434 -31 -49 -1 C ATOM 1375 O VAL A 178 -12.009 2.464 26.300 1.00 19.40 O ANISOU 1375 O VAL A 178 2231 2590 2551 -23 -41 20 O ATOM 1376 CB VAL A 178 -11.895 5.696 25.306 1.00 18.21 C ANISOU 1376 CB VAL A 178 2102 2372 2445 -57 -35 -3 C ATOM 1377 CG1 VAL A 178 -10.433 5.149 25.402 1.00 20.32 C ANISOU 1377 CG1 VAL A 178 2326 2653 2740 -72 -37 13 C ATOM 1378 CG2 VAL A 178 -12.156 6.419 23.988 1.00 22.97 C ANISOU 1378 CG2 VAL A 178 2725 2943 3060 -60 -11 11 C ATOM 1379 N TYR A 179 -12.522 4.020 27.832 1.00 20.45 N ANISOU 1379 N TYR A 179 2380 2725 2666 -39 -78 -24 N ATOM 1380 CA TYR A 179 -12.015 3.194 28.941 1.00 21.17 C ANISOU 1380 CA TYR A 179 2456 2846 2742 -42 -105 -20 C ATOM 1381 C TYR A 179 -12.970 2.074 29.309 1.00 20.54 C ANISOU 1381 C TYR A 179 2391 2790 2621 -28 -100 -10 C ATOM 1382 O TYR A 179 -12.546 0.937 29.531 1.00 21.96 O ANISOU 1382 O TYR A 179 2562 2982 2799 -24 -109 13 O ATOM 1383 CB TYR A 179 -11.786 4.027 30.183 1.00 21.95 C ANISOU 1383 CB TYR A 179 2556 2954 2830 -58 -139 -49 C ATOM 1384 CG TYR A 179 -10.636 4.986 30.082 1.00 21.68 C ANISOU 1384 CG TYR A 179 2502 2897 2837 -82 -155 -56 C ATOM 1385 CD1 TYR A 179 -9.430 4.593 29.537 1.00 22.57 C ANISOU 1385 CD1 TYR A 179 2578 3008 2990 -90 -152 -30 C ATOM 1386 CD2 TYR A 179 -10.764 6.294 30.545 1.00 24.21 C ANISOU 1386 CD2 TYR A 179 2840 3200 3160 -96 -173 -91 C ATOM 1387 CE1 TYR A 179 -8.369 5.483 29.460 1.00 26.28 C ANISOU 1387 CE1 TYR A 179 3024 3463 3500 -119 -166 -34 C ATOM 1388 CE2 TYR A 179 -9.701 7.188 30.491 1.00 25.71 C ANISOU 1388 CE2 TYR A 179 3012 3365 3389 -126 -191 -96 C ATOM 1389 CZ TYR A 179 -8.508 6.761 29.943 1.00 26.27 C ANISOU 1389 CZ TYR A 179 3042 3440 3500 -140 -187 -65 C ATOM 1390 OH TYR A 179 -7.440 7.633 29.877 1.00 29.84 O ANISOU 1390 OH TYR A 179 3471 3874 3994 -176 -204 -68 O ATOM 1391 N PHE A 180 -14.255 2.386 29.416 1.00 20.29 N ANISOU 1391 N PHE A 180 2382 2768 2560 -21 -90 -28 N ATOM 1392 CA PHE A 180 -15.202 1.398 29.921 1.00 22.14 C ANISOU 1392 CA PHE A 180 2627 3031 2752 -17 -87 -20 C ATOM 1393 C PHE A 180 -15.732 0.560 28.769 1.00 20.29 C ANISOU 1393 C PHE A 180 2399 2786 2523 -8 -61 3 C ATOM 1394 O PHE A 180 -15.592 -0.664 28.763 1.00 24.35 O ANISOU 1394 O PHE A 180 2915 3304 3033 -8 -63 28 O ATOM 1395 CB PHE A 180 -16.324 2.132 30.685 1.00 21.36 C ANISOU 1395 CB PHE A 180 2542 2956 2617 -15 -86 -53 C ATOM 1396 CG PHE A 180 -17.271 1.213 31.468 1.00 22.85 C ANISOU 1396 CG PHE A 180 2738 3188 2757 -20 -83 -45 C ATOM 1397 CD1 PHE A 180 -18.358 0.578 30.834 1.00 17.24 C ANISOU 1397 CD1 PHE A 180 2031 2486 2035 -16 -59 -32 C ATOM 1398 CD2 PHE A 180 -17.115 1.061 32.854 1.00 25.30 C ANISOU 1398 CD2 PHE A 180 3052 3533 3029 -33 -104 -52 C ATOM 1399 CE1 PHE A 180 -19.272 -0.210 31.563 1.00 23.17 C ANISOU 1399 CE1 PHE A 180 2785 3277 2740 -28 -54 -23 C ATOM 1400 CE2 PHE A 180 -18.025 0.277 33.612 1.00 24.41 C ANISOU 1400 CE2 PHE A 180 2947 3464 2864 -44 -97 -42 C ATOM 1401 CZ PHE A 180 -19.094 -0.394 32.949 1.00 23.08 C ANISOU 1401 CZ PHE A 180 2779 3303 2690 -43 -71 -26 C ATOM 1402 N ASN A 181 -16.309 1.206 27.753 1.00 22.00 N ANISOU 1402 N ASN A 181 2623 2984 2752 1 -41 -5 N ATOM 1403 CA ASN A 181 -16.884 0.405 26.701 1.00 19.40 C ANISOU 1403 CA ASN A 181 2303 2648 2421 8 -21 13 C ATOM 1404 C ASN A 181 -15.792 -0.290 25.892 1.00 23.51 C ANISOU 1404 C ASN A 181 2817 3147 2969 10 -13 35 C ATOM 1405 O ASN A 181 -15.788 -1.521 25.792 1.00 24.78 O ANISOU 1405 O ASN A 181 2984 3308 3123 12 -12 53 O ATOM 1406 CB ASN A 181 -17.808 1.232 25.805 1.00 23.20 C ANISOU 1406 CB ASN A 181 2793 3118 2902 18 -6 2 C ATOM 1407 CG ASN A 181 -18.655 0.333 24.901 1.00 24.95 C ANISOU 1407 CG ASN A 181 3026 3343 3111 21 7 17 C ATOM 1408 OD1 ASN A 181 -18.252 0.013 23.765 1.00 26.48 O ANISOU 1408 OD1 ASN A 181 3228 3515 3319 23 20 31 O ATOM 1409 ND2 ASN A 181 -19.798 -0.128 25.419 1.00 23.18 N ANISOU 1409 ND2 ASN A 181 2801 3148 2857 17 5 13 N ATOM 1410 N PHE A 182 -14.808 0.456 25.374 1.00 18.41 N ANISOU 1410 N PHE A 182 2159 2480 2354 9 -7 34 N ATOM 1411 CA PHE A 182 -13.848 -0.182 24.481 1.00 21.20 C ANISOU 1411 CA PHE A 182 2502 2820 2733 15 9 52 C ATOM 1412 C PHE A 182 -12.824 -1.048 25.235 1.00 21.28 C ANISOU 1412 C PHE A 182 2491 2838 2757 19 -9 63 C ATOM 1413 O PHE A 182 -12.749 -2.259 25.025 1.00 22.69 O ANISOU 1413 O PHE A 182 2675 3013 2934 31 -6 76 O ATOM 1414 CB PHE A 182 -13.128 0.890 23.638 1.00 19.67 C ANISOU 1414 CB PHE A 182 2299 2608 2568 8 26 51 C ATOM 1415 CG PHE A 182 -12.127 0.324 22.648 1.00 21.76 C ANISOU 1415 CG PHE A 182 2547 2865 2854 15 51 66 C ATOM 1416 CD1 PHE A 182 -12.373 -0.900 21.999 1.00 22.42 C ANISOU 1416 CD1 PHE A 182 2645 2947 2926 32 67 74 C ATOM 1417 CD2 PHE A 182 -10.959 1.033 22.326 1.00 22.88 C ANISOU 1417 CD2 PHE A 182 2661 3002 3029 2 62 71 C ATOM 1418 CE1 PHE A 182 -11.471 -1.424 21.065 1.00 18.36 C ANISOU 1418 CE1 PHE A 182 2118 2429 2430 43 95 81 C ATOM 1419 CE2 PHE A 182 -10.033 0.521 21.408 1.00 26.24 C ANISOU 1419 CE2 PHE A 182 3067 3429 3473 10 92 82 C ATOM 1420 CZ PHE A 182 -10.298 -0.730 20.757 1.00 22.19 C ANISOU 1420 CZ PHE A 182 2570 2916 2945 34 111 85 C ATOM 1421 N PHE A 183 -11.996 -0.442 26.089 1.00 19.77 N ANISOU 1421 N PHE A 183 2277 2655 2581 8 -31 57 N ATOM 1422 CA PHE A 183 -10.900 -1.199 26.706 1.00 19.12 C ANISOU 1422 CA PHE A 183 2168 2580 2517 14 -53 70 C ATOM 1423 C PHE A 183 -11.420 -2.357 27.557 1.00 22.25 C ANISOU 1423 C PHE A 183 2583 2988 2884 21 -75 83 C ATOM 1424 O PHE A 183 -11.021 -3.520 27.364 1.00 23.20 O ANISOU 1424 O PHE A 183 2701 3099 3016 39 -77 101 O ATOM 1425 CB PHE A 183 -10.023 -0.275 27.579 1.00 20.37 C ANISOU 1425 CB PHE A 183 2299 2749 2692 -3 -81 60 C ATOM 1426 CG PHE A 183 -9.182 0.709 26.813 1.00 25.63 C ANISOU 1426 CG PHE A 183 2939 3402 3396 -16 -64 56 C ATOM 1427 CD1 PHE A 183 -9.155 0.716 25.428 1.00 29.59 C ANISOU 1427 CD1 PHE A 183 3442 3888 3912 -10 -23 63 C ATOM 1428 CD2 PHE A 183 -8.345 1.607 27.502 1.00 24.84 C ANISOU 1428 CD2 PHE A 183 2814 3308 3318 -39 -92 46 C ATOM 1429 CE1 PHE A 183 -8.328 1.625 24.716 1.00 28.71 C ANISOU 1429 CE1 PHE A 183 3307 3768 3833 -28 -5 65 C ATOM 1430 CE2 PHE A 183 -7.546 2.505 26.798 1.00 25.84 C ANISOU 1430 CE2 PHE A 183 2915 3422 3481 -59 -76 46 C ATOM 1431 CZ PHE A 183 -7.564 2.518 25.394 1.00 24.14 C ANISOU 1431 CZ PHE A 183 2702 3193 3278 -54 -30 58 C ATOM 1432 N ALA A 184 -12.329 -2.063 28.494 1.00 20.13 N ANISOU 1432 N ALA A 184 2333 2738 2577 7 -90 73 N ATOM 1433 CA ALA A 184 -12.781 -3.072 29.456 1.00 22.40 C ANISOU 1433 CA ALA A 184 2638 3042 2830 4 -112 90 C ATOM 1434 C ALA A 184 -13.766 -4.053 28.837 1.00 24.95 C ANISOU 1434 C ALA A 184 2987 3354 3137 8 -93 103 C ATOM 1435 O ALA A 184 -13.658 -5.263 29.057 1.00 23.44 O ANISOU 1435 O ALA A 184 2809 3155 2944 12 -106 127 O ATOM 1436 CB ALA A 184 -13.430 -2.400 30.680 1.00 21.38 C ANISOU 1436 CB ALA A 184 2520 2946 2660 -15 -129 73 C ATOM 1437 N CYS A 185 -14.785 -3.548 28.129 1.00 22.57 N ANISOU 1437 N CYS A 185 2698 3053 2824 4 -66 88 N ATOM 1438 CA CYS A 185 -15.927 -4.386 27.751 1.00 19.24 C ANISOU 1438 CA CYS A 185 2301 2631 2380 -2 -55 98 C ATOM 1439 C CYS A 185 -15.820 -4.997 26.353 1.00 19.74 C ANISOU 1439 C CYS A 185 2373 2662 2465 12 -34 103 C ATOM 1440 O CYS A 185 -16.524 -5.977 26.068 1.00 21.19 O ANISOU 1440 O CYS A 185 2579 2838 2635 6 -32 114 O ATOM 1441 CB CYS A 185 -17.224 -3.574 27.869 1.00 22.36 C ANISOU 1441 CB CYS A 185 2699 3051 2746 -13 -43 78 C ATOM 1442 SG CYS A 185 -17.580 -3.255 29.643 1.00 27.92 S ANISOU 1442 SG CYS A 185 3401 3801 3408 -30 -63 70 S ATOM 1443 N VAL A 186 -14.929 -4.493 25.508 1.00 19.81 N ANISOU 1443 N VAL A 186 2368 2654 2506 27 -19 95 N ATOM 1444 CA VAL A 186 -14.764 -5.030 24.162 1.00 21.39 C ANISOU 1444 CA VAL A 186 2579 2830 2721 41 5 96 C ATOM 1445 C VAL A 186 -13.372 -5.623 23.952 1.00 25.03 C ANISOU 1445 C VAL A 186 3022 3274 3216 63 6 103 C ATOM 1446 O VAL A 186 -13.213 -6.796 23.576 1.00 24.57 O ANISOU 1446 O VAL A 186 2978 3193 3164 79 8 110 O ATOM 1447 CB VAL A 186 -15.054 -3.936 23.116 1.00 25.24 C ANISOU 1447 CB VAL A 186 3066 3315 3209 40 30 82 C ATOM 1448 CG1 VAL A 186 -14.704 -4.428 21.709 1.00 20.29 C ANISOU 1448 CG1 VAL A 186 2450 2668 2591 54 57 82 C ATOM 1449 CG2 VAL A 186 -16.552 -3.539 23.179 1.00 24.43 C ANISOU 1449 CG2 VAL A 186 2980 3228 3075 27 27 75 C ATOM 1450 N LEU A 187 -12.351 -4.810 24.172 1.00 22.16 N ANISOU 1450 N LEU A 187 2624 2918 2878 66 5 99 N ATOM 1451 CA LEU A 187 -10.996 -5.244 23.865 1.00 22.27 C ANISOU 1451 CA LEU A 187 2609 2923 2929 88 11 104 C ATOM 1452 C LEU A 187 -10.572 -6.419 24.742 1.00 20.81 C ANISOU 1452 C LEU A 187 2424 2731 2753 105 -21 120 C ATOM 1453 O LEU A 187 -10.036 -7.422 24.256 1.00 25.35 O ANISOU 1453 O LEU A 187 2998 3284 3348 133 -15 123 O ATOM 1454 CB LEU A 187 -10.057 -4.042 24.021 1.00 26.83 C ANISOU 1454 CB LEU A 187 3146 3515 3532 78 13 98 C ATOM 1455 CG LEU A 187 -8.688 -4.121 23.388 1.00 33.87 C ANISOU 1455 CG LEU A 187 3996 4407 4465 96 33 99 C ATOM 1456 CD1 LEU A 187 -8.893 -4.510 21.918 1.00 36.08 C ANISOU 1456 CD1 LEU A 187 4296 4674 4739 110 78 93 C ATOM 1457 CD2 LEU A 187 -7.979 -2.753 23.521 1.00 33.00 C ANISOU 1457 CD2 LEU A 187 3850 4312 4376 71 34 95 C ATOM 1458 N VAL A 188 -10.782 -6.318 26.041 1.00 22.01 N ANISOU 1458 N VAL A 188 2576 2899 2888 89 -57 130 N ATOM 1459 CA VAL A 188 -10.390 -7.413 26.933 1.00 23.38 C ANISOU 1459 CA VAL A 188 2754 3066 3066 102 -94 152 C ATOM 1460 C VAL A 188 -11.125 -8.711 26.602 1.00 27.62 C ANISOU 1460 C VAL A 188 3334 3572 3589 109 -93 164 C ATOM 1461 O VAL A 188 -10.460 -9.747 26.450 1.00 26.06 O ANISOU 1461 O VAL A 188 3137 3346 3418 139 -103 174 O ATOM 1462 CB VAL A 188 -10.545 -6.974 28.406 1.00 22.41 C ANISOU 1462 CB VAL A 188 2628 2971 2915 78 -133 161 C ATOM 1463 CG1 VAL A 188 -10.602 -8.193 29.343 1.00 25.86 C ANISOU 1463 CG1 VAL A 188 3088 3400 3336 81 -171 192 C ATOM 1464 CG2 VAL A 188 -9.375 -6.056 28.782 1.00 23.36 C ANISOU 1464 CG2 VAL A 188 2702 3111 3063 78 -147 152 C ATOM 1465 N PRO A 189 -12.454 -8.727 26.422 1.00 24.39 N ANISOU 1465 N PRO A 189 2959 3165 3143 83 -81 161 N ATOM 1466 CA PRO A 189 -13.075 -9.980 25.943 1.00 25.71 C ANISOU 1466 CA PRO A 189 3166 3298 3303 86 -80 170 C ATOM 1467 C PRO A 189 -12.542 -10.461 24.601 1.00 24.79 C ANISOU 1467 C PRO A 189 3053 3149 3216 118 -53 154 C ATOM 1468 O PRO A 189 -12.370 -11.675 24.420 1.00 22.62 O ANISOU 1468 O PRO A 189 2802 2836 2955 137 -64 161 O ATOM 1469 CB PRO A 189 -14.584 -9.633 25.874 1.00 23.36 C ANISOU 1469 CB PRO A 189 2892 3021 2965 49 -69 165 C ATOM 1470 CG PRO A 189 -14.754 -8.552 26.895 1.00 24.11 C ANISOU 1470 CG PRO A 189 2965 3158 3038 31 -78 163 C ATOM 1471 CD PRO A 189 -13.480 -7.705 26.745 1.00 17.72 C ANISOU 1471 CD PRO A 189 2118 2353 2263 52 -74 150 C ATOM 1472 N LEU A 190 -12.225 -9.563 23.661 1.00 19.48 N ANISOU 1472 N LEU A 190 2359 2490 2554 125 -18 131 N ATOM 1473 CA LEU A 190 -11.721 -10.045 22.386 1.00 20.76 C ANISOU 1473 CA LEU A 190 2525 2627 2736 155 12 114 C ATOM 1474 C LEU A 190 -10.337 -10.667 22.556 1.00 24.01 C ANISOU 1474 C LEU A 190 2908 3024 3190 196 5 117 C ATOM 1475 O LEU A 190 -10.034 -11.713 21.972 1.00 21.99 O ANISOU 1475 O LEU A 190 2671 2734 2952 228 11 109 O ATOM 1476 CB LEU A 190 -11.690 -8.910 21.367 1.00 19.83 C ANISOU 1476 CB LEU A 190 2392 2530 2613 148 52 95 C ATOM 1477 CG LEU A 190 -13.101 -8.485 20.869 1.00 25.23 C ANISOU 1477 CG LEU A 190 3109 3221 3257 118 60 90 C ATOM 1478 CD1 LEU A 190 -12.864 -7.218 20.016 1.00 24.81 C ANISOU 1478 CD1 LEU A 190 3038 3187 3203 114 92 79 C ATOM 1479 CD2 LEU A 190 -13.721 -9.591 19.979 1.00 24.92 C ANISOU 1479 CD2 LEU A 190 3115 3152 3203 124 67 80 C ATOM 1480 N LEU A 191 -9.511 -10.081 23.407 1.00 21.61 N ANISOU 1480 N LEU A 191 2560 2745 2907 198 -14 127 N ATOM 1481 CA LEU A 191 -8.214 -10.702 23.656 1.00 25.91 C ANISOU 1481 CA LEU A 191 3070 3279 3496 240 -28 133 C ATOM 1482 C LEU A 191 -8.353 -12.031 24.389 1.00 27.97 C ANISOU 1482 C LEU A 191 3364 3504 3760 256 -71 155 C ATOM 1483 O LEU A 191 -7.555 -12.951 24.145 1.00 27.74 O ANISOU 1483 O LEU A 191 3328 3445 3768 303 -76 153 O ATOM 1484 CB LEU A 191 -7.330 -9.730 24.435 1.00 21.12 C ANISOU 1484 CB LEU A 191 2407 2711 2909 232 -45 140 C ATOM 1485 CG LEU A 191 -6.970 -8.439 23.664 1.00 29.53 C ANISOU 1485 CG LEU A 191 3436 3804 3980 216 -4 121 C ATOM 1486 CD1 LEU A 191 -6.376 -7.434 24.638 1.00 28.27 C ANISOU 1486 CD1 LEU A 191 3233 3677 3832 193 -31 129 C ATOM 1487 CD2 LEU A 191 -5.983 -8.700 22.500 1.00 31.09 C ANISOU 1487 CD2 LEU A 191 3600 4000 4213 252 40 104 C ATOM 1488 N LEU A 192 -9.343 -12.157 25.298 1.00 24.63 N ANISOU 1488 N LEU A 192 2977 3081 3299 220 -102 177 N ATOM 1489 CA LEU A 192 -9.619 -13.443 25.938 1.00 23.76 C ANISOU 1489 CA LEU A 192 2908 2932 3186 225 -142 204 C ATOM 1490 C LEU A 192 -10.022 -14.494 24.914 1.00 28.61 C ANISOU 1490 C LEU A 192 3568 3495 3807 242 -124 190 C ATOM 1491 O LEU A 192 -9.592 -15.649 24.990 1.00 30.70 O ANISOU 1491 O LEU A 192 3853 3712 4098 276 -148 200 O ATOM 1492 CB LEU A 192 -10.731 -13.294 26.971 1.00 26.47 C ANISOU 1492 CB LEU A 192 3282 3296 3481 173 -167 229 C ATOM 1493 CG LEU A 192 -10.351 -12.526 28.234 1.00 34.32 C ANISOU 1493 CG LEU A 192 4245 4334 4462 157 -196 245 C ATOM 1494 CD1 LEU A 192 -11.601 -12.338 29.035 1.00 39.61 C ANISOU 1494 CD1 LEU A 192 4946 5028 5077 106 -206 261 C ATOM 1495 CD2 LEU A 192 -9.322 -13.314 29.007 1.00 37.47 C ANISOU 1495 CD2 LEU A 192 4634 4714 4890 190 -244 274 C ATOM 1496 N MET A 193 -10.904 -14.120 23.982 1.00 27.89 N ANISOU 1496 N MET A 193 3496 3410 3689 218 -88 167 N ATOM 1497 CA MET A 193 -11.295 -15.001 22.886 1.00 28.56 C ANISOU 1497 CA MET A 193 3625 3451 3775 231 -69 147 C ATOM 1498 C MET A 193 -10.092 -15.457 22.089 1.00 27.46 C ANISOU 1498 C MET A 193 3467 3287 3679 292 -49 121 C ATOM 1499 O MET A 193 -10.002 -16.629 21.706 1.00 30.59 O ANISOU 1499 O MET A 193 3901 3629 4092 322 -57 112 O ATOM 1500 CB MET A 193 -12.242 -14.277 21.926 1.00 29.04 C ANISOU 1500 CB MET A 193 3697 3534 3801 200 -33 123 C ATOM 1501 CG MET A 193 -13.671 -14.261 22.334 1.00 34.49 C ANISOU 1501 CG MET A 193 4420 4234 4452 146 -48 139 C ATOM 1502 SD MET A 193 -14.523 -13.202 21.123 1.00 34.20 S ANISOU 1502 SD MET A 193 4382 4231 4383 123 -7 110 S ATOM 1503 CE MET A 193 -15.271 -11.994 22.235 1.00 29.13 C ANISOU 1503 CE MET A 193 3711 3643 3713 81 -19 129 C ATOM 1504 N LEU A 194 -9.198 -14.519 21.766 1.00 26.18 N ANISOU 1504 N LEU A 194 3248 3165 3535 310 -19 106 N ATOM 1505 CA LEU A 194 -7.978 -14.861 21.051 1.00 30.27 C ANISOU 1505 CA LEU A 194 3734 3673 4094 369 7 82 C ATOM 1506 C LEU A 194 -7.190 -15.909 21.819 1.00 26.22 C ANISOU 1506 C LEU A 194 3215 3123 3623 415 -36 99 C ATOM 1507 O LEU A 194 -6.689 -16.872 21.240 1.00 27.95 O ANISOU 1507 O LEU A 194 3448 3300 3872 467 -28 78 O ATOM 1508 CB LEU A 194 -7.138 -13.597 20.836 1.00 28.48 C ANISOU 1508 CB LEU A 194 3439 3503 3880 368 40 74 C ATOM 1509 CG LEU A 194 -5.753 -13.832 20.239 1.00 30.51 C ANISOU 1509 CG LEU A 194 3645 3766 4184 426 69 52 C ATOM 1510 CD1 LEU A 194 -5.888 -14.498 18.884 1.00 31.37 C ANISOU 1510 CD1 LEU A 194 3789 3847 4283 455 114 14 C ATOM 1511 CD2 LEU A 194 -4.994 -12.514 20.121 1.00 32.33 C ANISOU 1511 CD2 LEU A 194 3804 4054 4424 411 99 51 C ATOM 1512 N GLY A 195 -7.062 -15.723 23.134 1.00 27.88 N ANISOU 1512 N GLY A 195 3408 3348 3837 398 -83 136 N ATOM 1513 CA GLY A 195 -6.350 -16.700 23.948 1.00 27.49 C ANISOU 1513 CA GLY A 195 3356 3263 3825 440 -133 160 C ATOM 1514 C GLY A 195 -7.043 -18.052 23.982 1.00 30.23 C ANISOU 1514 C GLY A 195 3780 3539 4167 445 -162 172 C ATOM 1515 O GLY A 195 -6.386 -19.098 23.892 1.00 32.67 O ANISOU 1515 O GLY A 195 4100 3796 4519 502 -181 169 O ATOM 1516 N VAL A 196 -8.378 -18.057 24.051 1.00 24.75 N ANISOU 1516 N VAL A 196 3140 2838 3425 385 -164 182 N ATOM 1517 CA VAL A 196 -9.106 -19.325 24.015 1.00 25.35 C ANISOU 1517 CA VAL A 196 3292 2846 3496 378 -190 193 C ATOM 1518 C VAL A 196 -8.909 -20.034 22.677 1.00 29.55 C ANISOU 1518 C VAL A 196 3850 3329 4050 422 -157 146 C ATOM 1519 O VAL A 196 -8.751 -21.256 22.646 1.00 28.12 O ANISOU 1519 O VAL A 196 3713 3075 3896 456 -185 147 O ATOM 1520 CB VAL A 196 -10.604 -19.129 24.332 1.00 25.27 C ANISOU 1520 CB VAL A 196 3323 2848 3429 300 -195 213 C ATOM 1521 CG1 VAL A 196 -11.402 -20.410 24.094 1.00 24.48 C ANISOU 1521 CG1 VAL A 196 3301 2677 3326 284 -216 220 C ATOM 1522 CG2 VAL A 196 -10.783 -18.655 25.778 1.00 27.20 C ANISOU 1522 CG2 VAL A 196 3551 3133 3649 262 -231 259 C ATOM 1523 N TYR A 197 -8.949 -19.296 21.549 1.00 26.67 N ANISOU 1523 N TYR A 197 3464 2999 3670 422 -100 104 N ATOM 1524 CA TYR A 197 -8.768 -19.952 20.246 1.00 26.65 C ANISOU 1524 CA TYR A 197 3489 2956 3679 463 -66 55 C ATOM 1525 C TYR A 197 -7.351 -20.500 20.104 1.00 28.29 C ANISOU 1525 C TYR A 197 3662 3142 3945 547 -63 36 C ATOM 1526 O TYR A 197 -7.156 -21.589 19.545 1.00 30.78 O ANISOU 1526 O TYR A 197 4019 3393 4284 594 -64 8 O ATOM 1527 CB TYR A 197 -9.114 -18.994 19.077 1.00 26.51 C ANISOU 1527 CB TYR A 197 3459 2989 3626 440 -6 18 C ATOM 1528 CG TYR A 197 -10.615 -18.931 18.837 1.00 26.75 C ANISOU 1528 CG TYR A 197 3544 3015 3604 373 -12 22 C ATOM 1529 CD1 TYR A 197 -11.308 -20.082 18.460 1.00 29.66 C ANISOU 1529 CD1 TYR A 197 3985 3319 3966 366 -31 10 C ATOM 1530 CD2 TYR A 197 -11.354 -17.765 19.073 1.00 28.46 C ANISOU 1530 CD2 TYR A 197 3739 3291 3783 317 -3 39 C ATOM 1531 CE1 TYR A 197 -12.681 -20.093 18.303 1.00 29.65 C ANISOU 1531 CE1 TYR A 197 4028 3316 3923 301 -42 16 C ATOM 1532 CE2 TYR A 197 -12.749 -17.768 18.915 1.00 26.87 C ANISOU 1532 CE2 TYR A 197 3581 3089 3540 260 -13 44 C ATOM 1533 CZ TYR A 197 -13.405 -18.932 18.523 1.00 28.24 C ANISOU 1533 CZ TYR A 197 3820 3203 3707 250 -32 34 C ATOM 1534 OH TYR A 197 -14.791 -18.985 18.376 1.00 29.99 O ANISOU 1534 OH TYR A 197 4078 3426 3891 189 -44 40 O ATOM 1535 N LEU A 198 -6.350 -19.781 20.626 1.00 27.56 N ANISOU 1535 N LEU A 198 3492 3100 3879 569 -61 49 N ATOM 1536 CA LEU A 198 -4.985 -20.315 20.634 1.00 30.00 C ANISOU 1536 CA LEU A 198 3756 3393 4250 651 -64 36 C ATOM 1537 C LEU A 198 -4.916 -21.630 21.395 1.00 31.50 C ANISOU 1537 C LEU A 198 3992 3505 4473 685 -129 63 C ATOM 1538 O LEU A 198 -4.304 -22.609 20.936 1.00 30.54 O ANISOU 1538 O LEU A 198 3884 3328 4394 756 -130 35 O ATOM 1539 CB LEU A 198 -4.028 -19.288 21.263 1.00 35.87 C ANISOU 1539 CB LEU A 198 4406 4208 5014 655 -64 55 C ATOM 1540 CG LEU A 198 -3.815 -18.106 20.320 1.00 45.16 C ANISOU 1540 CG LEU A 198 5534 5453 6173 637 5 24 C ATOM 1541 CD1 LEU A 198 -2.935 -17.020 20.956 1.00 48.79 C ANISOU 1541 CD1 LEU A 198 5905 5981 6653 628 2 44 C ATOM 1542 CD2 LEU A 198 -3.225 -18.610 19.007 1.00 49.46 C ANISOU 1542 CD2 LEU A 198 6073 5983 6736 697 61 -30 C ATOM 1543 N ARG A 199 -5.526 -21.666 22.582 1.00 30.74 N ANISOU 1543 N ARG A 199 3922 3401 4356 635 -185 118 N ATOM 1544 CA ARG A 199 -5.614 -22.913 23.337 1.00 33.64 C ANISOU 1544 CA ARG A 199 4346 3690 4746 654 -250 153 C ATOM 1545 C ARG A 199 -6.351 -24.014 22.562 1.00 30.76 C ANISOU 1545 C ARG A 199 4070 3242 4377 655 -248 127 C ATOM 1546 O ARG A 199 -5.959 -25.175 22.629 1.00 34.89 O ANISOU 1546 O ARG A 199 4630 3684 4942 709 -283 128 O ATOM 1547 CB ARG A 199 -6.292 -22.655 24.681 1.00 35.33 C ANISOU 1547 CB ARG A 199 4577 3923 4923 585 -301 217 C ATOM 1548 CG ARG A 199 -5.450 -21.776 25.615 1.00 39.90 C ANISOU 1548 CG ARG A 199 5077 4570 5511 591 -321 244 C ATOM 1549 CD ARG A 199 -6.063 -21.767 27.011 1.00 51.64 C ANISOU 1549 CD ARG A 199 6594 6065 6961 533 -378 307 C ATOM 1550 NE ARG A 199 -5.310 -20.896 27.906 1.00 62.77 N ANISOU 1550 NE ARG A 199 7935 7542 8373 533 -400 328 N ATOM 1551 CZ ARG A 199 -4.261 -21.282 28.632 1.00 68.59 C ANISOU 1551 CZ ARG A 199 8641 8270 9152 584 -452 355 C ATOM 1552 NH1 ARG A 199 -3.837 -22.541 28.583 1.00 69.45 N ANISOU 1552 NH1 ARG A 199 8783 8301 9306 644 -488 366 N ATOM 1553 NH2 ARG A 199 -3.631 -20.405 29.410 1.00 68.27 N ANISOU 1553 NH2 ARG A 199 8537 8295 9108 576 -472 371 N ATOM 1554 N ILE A 200 -7.427 -23.687 21.835 1.00 30.24 N ANISOU 1554 N ILE A 200 4040 3188 4261 597 -212 105 N ATOM 1555 CA ILE A 200 -8.125 -24.730 21.066 1.00 26.42 C ANISOU 1555 CA ILE A 200 3640 2626 3772 594 -213 77 C ATOM 1556 C ILE A 200 -7.217 -25.313 19.983 1.00 25.73 C ANISOU 1556 C ILE A 200 3550 2499 3726 682 -180 14 C ATOM 1557 O ILE A 200 -7.092 -26.537 19.831 1.00 29.20 O ANISOU 1557 O ILE A 200 4047 2847 4199 725 -209 0 O ATOM 1558 CB ILE A 200 -9.417 -24.177 20.433 1.00 28.34 C ANISOU 1558 CB ILE A 200 3912 2900 3953 515 -182 62 C ATOM 1559 CG1 ILE A 200 -10.502 -23.901 21.474 1.00 30.74 C ANISOU 1559 CG1 ILE A 200 4234 3226 4217 429 -217 121 C ATOM 1560 CG2 ILE A 200 -9.933 -25.192 19.425 1.00 28.61 C ANISOU 1560 CG2 ILE A 200 4025 2859 3986 521 -177 19 C ATOM 1561 CD1 ILE A 200 -11.711 -23.081 20.900 1.00 28.73 C ANISOU 1561 CD1 ILE A 200 3986 3026 3906 356 -183 106 C ATOM 1562 N PHE A 201 -6.611 -24.445 19.175 1.00 30.36 N ANISOU 1562 N PHE A 201 4073 3154 4309 708 -117 -28 N ATOM 1563 CA PHE A 201 -5.755 -24.935 18.098 1.00 31.12 C ANISOU 1563 CA PHE A 201 4162 3227 4437 791 -75 -93 C ATOM 1564 C PHE A 201 -4.516 -25.661 18.633 1.00 31.43 C ANISOU 1564 C PHE A 201 4167 3226 4548 882 -107 -88 C ATOM 1565 O PHE A 201 -4.089 -26.665 18.052 1.00 31.13 O ANISOU 1565 O PHE A 201 4162 3119 4546 954 -104 -132 O ATOM 1566 CB PHE A 201 -5.395 -23.769 17.184 1.00 32.13 C ANISOU 1566 CB PHE A 201 4224 3445 4537 789 1 -130 C ATOM 1567 CG PHE A 201 -6.589 -23.218 16.437 1.00 30.77 C ANISOU 1567 CG PHE A 201 4095 3299 4296 714 31 -144 C ATOM 1568 CD1 PHE A 201 -7.354 -24.053 15.631 1.00 30.63 C ANISOU 1568 CD1 PHE A 201 4163 3219 4255 705 31 -181 C ATOM 1569 CD2 PHE A 201 -6.958 -21.904 16.562 1.00 30.43 C ANISOU 1569 CD2 PHE A 201 4010 3337 4215 653 52 -120 C ATOM 1570 CE1 PHE A 201 -8.461 -23.580 14.946 1.00 32.95 C ANISOU 1570 CE1 PHE A 201 4494 3539 4487 637 51 -192 C ATOM 1571 CE2 PHE A 201 -8.062 -21.414 15.890 1.00 32.41 C ANISOU 1571 CE2 PHE A 201 4298 3609 4406 590 73 -130 C ATOM 1572 CZ PHE A 201 -8.821 -22.257 15.079 1.00 33.60 C ANISOU 1572 CZ PHE A 201 4530 3705 4533 581 71 -165 C ATOM 1573 N ALA A 202 -3.954 -25.207 19.763 1.00 30.23 N ANISOU 1573 N ALA A 202 3954 3113 4420 883 -142 -36 N ATOM 1574 CA ALA A 202 -2.840 -25.946 20.365 1.00 34.56 C ANISOU 1574 CA ALA A 202 4472 3621 5039 969 -185 -23 C ATOM 1575 C ALA A 202 -3.292 -27.315 20.879 1.00 36.34 C ANISOU 1575 C ALA A 202 4791 3731 5285 980 -255 4 C ATOM 1576 O ALA A 202 -2.569 -28.305 20.727 1.00 41.41 O ANISOU 1576 O ALA A 202 5445 4303 5985 1068 -275 -19 O ATOM 1577 CB ALA A 202 -2.204 -25.150 21.506 1.00 30.86 C ANISOU 1577 CB ALA A 202 3921 3220 4585 959 -216 30 C ATOM 1578 N ALA A 203 -4.475 -27.398 21.504 1.00 33.91 N ANISOU 1578 N ALA A 203 4550 3401 4933 892 -294 52 N ATOM 1579 CA ALA A 203 -4.936 -28.697 22.000 1.00 35.89 C ANISOU 1579 CA ALA A 203 4895 3541 5202 892 -362 84 C ATOM 1580 C ALA A 203 -5.195 -29.664 20.849 1.00 35.59 C ANISOU 1580 C ALA A 203 4931 3417 5176 926 -342 20 C ATOM 1581 O ALA A 203 -4.910 -30.861 20.955 1.00 45.17 O ANISOU 1581 O ALA A 203 6199 4526 6437 982 -387 19 O ATOM 1582 CB ALA A 203 -6.198 -28.527 22.842 1.00 34.66 C ANISOU 1582 CB ALA A 203 4789 3392 4990 781 -398 147 C ATOM 1583 N ALA A 204 -5.754 -29.165 19.753 1.00 33.14 N ANISOU 1583 N ALA A 204 4627 3144 4820 892 -278 -33 N ATOM 1584 CA ALA A 204 -5.953 -29.990 18.571 1.00 35.93 C ANISOU 1584 CA ALA A 204 5048 3427 5178 924 -254 -103 C ATOM 1585 C ALA A 204 -4.622 -30.494 18.025 1.00 39.22 C ANISOU 1585 C ALA A 204 5429 3815 5657 1049 -231 -160 C ATOM 1586 O ALA A 204 -4.482 -31.672 17.680 1.00 38.17 O ANISOU 1586 O ALA A 204 5363 3578 5561 1107 -254 -195 O ATOM 1587 CB ALA A 204 -6.686 -29.189 17.501 1.00 34.04 C ANISOU 1587 CB ALA A 204 4809 3253 4873 867 -188 -148 C ATOM 1588 N ARG A 205 -3.645 -29.598 17.899 1.00 38.78 N ANISOU 1588 N ARG A 205 5268 3854 5614 1092 -183 -174 N ATOM 1589 CA ARG A 205 -2.368 -29.992 17.320 1.00 43.60 C ANISOU 1589 CA ARG A 205 5830 4454 6282 1210 -151 -233 C ATOM 1590 C ARG A 205 -1.683 -31.043 18.184 1.00 41.93 C ANISOU 1590 C ARG A 205 5630 4154 6146 1288 -226 -203 C ATOM 1591 O ARG A 205 -1.083 -32.001 17.670 1.00 44.46 O ANISOU 1591 O ARG A 205 5975 4401 6518 1384 -224 -256 O ATOM 1592 CB ARG A 205 -1.482 -28.759 17.152 1.00 48.89 C ANISOU 1592 CB ARG A 205 6376 5250 6950 1226 -90 -241 C ATOM 1593 CG ARG A 205 -0.166 -29.028 16.467 1.00 60.33 C ANISOU 1593 CG ARG A 205 7758 6710 8453 1342 -43 -305 C ATOM 1594 CD ARG A 205 0.787 -27.903 16.777 1.00 68.04 C ANISOU 1594 CD ARG A 205 8604 7802 9445 1350 -12 -285 C ATOM 1595 NE ARG A 205 0.990 -27.800 18.215 1.00 69.24 N ANISOU 1595 NE ARG A 205 8726 7954 9629 1335 -90 -205 N ATOM 1596 CZ ARG A 205 1.107 -26.659 18.881 1.00 67.01 C ANISOU 1596 CZ ARG A 205 8371 7762 9328 1278 -93 -158 C ATOM 1597 NH1 ARG A 205 1.036 -25.500 18.241 1.00 61.14 N ANISOU 1597 NH1 ARG A 205 7579 7111 8540 1228 -22 -177 N ATOM 1598 NH2 ARG A 205 1.276 -26.685 20.197 1.00 69.65 N ANISOU 1598 NH2 ARG A 205 8689 8090 9687 1267 -170 -89 N ATOM 1599 N ARG A 206 -1.771 -30.877 19.504 1.00 41.57 N ANISOU 1599 N ARG A 206 5571 4115 6108 1249 -292 -118 N ATOM 1600 CA ARG A 206 -1.164 -31.819 20.431 1.00 39.71 C ANISOU 1600 CA ARG A 206 5350 3799 5940 1315 -372 -76 C ATOM 1601 C ARG A 206 -1.853 -33.178 20.367 1.00 40.09 C ANISOU 1601 C ARG A 206 5527 3705 6001 1316 -424 -77 C ATOM 1602 O ARG A 206 -1.198 -34.216 20.475 1.00 43.48 O ANISOU 1602 O ARG A 206 5982 4041 6499 1410 -467 -87 O ATOM 1603 CB ARG A 206 -1.226 -31.245 21.842 1.00 43.12 C ANISOU 1603 CB ARG A 206 5745 4280 6359 1258 -430 17 C ATOM 1604 CG ARG A 206 -0.965 -32.248 22.932 1.00 58.38 C ANISOU 1604 CG ARG A 206 7721 6121 8341 1294 -527 80 C ATOM 1605 CD ARG A 206 -0.981 -31.570 24.288 1.00 74.59 C ANISOU 1605 CD ARG A 206 9733 8238 10370 1236 -578 167 C ATOM 1606 NE ARG A 206 -0.198 -32.317 25.270 1.00 87.48 N ANISOU 1606 NE ARG A 206 11363 9813 12063 1304 -664 220 N ATOM 1607 CZ ARG A 206 0.471 -31.759 26.276 1.00 90.87 C ANISOU 1607 CZ ARG A 206 11716 10309 12501 1310 -704 273 C ATOM 1608 NH1 ARG A 206 0.456 -30.440 26.428 1.00 89.40 N ANISOU 1608 NH1 ARG A 206 11452 10246 12270 1250 -663 276 N ATOM 1609 NH2 ARG A 206 1.162 -32.518 27.124 1.00 93.17 N ANISOU 1609 NH2 ARG A 206 12012 10542 12846 1376 -789 322 N ATOM 1610 N GLN A 207 -3.174 -33.194 20.204 1.00 37.31 N ANISOU 1610 N GLN A 207 5257 3332 5588 1213 -425 -66 N ATOM 1611 CA GLN A 207 -3.881 -34.467 20.224 1.00 37.86 C ANISOU 1611 CA GLN A 207 5452 3265 5670 1199 -480 -59 C ATOM 1612 C GLN A 207 -3.667 -35.232 18.927 1.00 33.58 C ANISOU 1612 C GLN A 207 4957 2650 5151 1273 -443 -157 C ATOM 1613 O GLN A 207 -3.561 -36.460 18.939 1.00 40.12 O ANISOU 1613 O GLN A 207 5865 3350 6030 1326 -493 -168 O ATOM 1614 CB GLN A 207 -5.364 -34.232 20.503 1.00 41.01 C ANISOU 1614 CB GLN A 207 5914 3672 5997 1060 -494 -13 C ATOM 1615 CG GLN A 207 -5.634 -33.743 21.920 1.00 38.39 C ANISOU 1615 CG GLN A 207 5556 3387 5643 991 -544 87 C ATOM 1616 CD GLN A 207 -7.114 -33.520 22.182 1.00 42.39 C ANISOU 1616 CD GLN A 207 6118 3908 6080 856 -551 128 C ATOM 1617 OE1 GLN A 207 -7.966 -34.163 21.565 1.00 47.60 O ANISOU 1617 OE1 GLN A 207 6862 4498 6724 815 -553 102 O ATOM 1618 NE2 GLN A 207 -7.427 -32.595 23.083 1.00 39.77 N ANISOU 1618 NE2 GLN A 207 5737 3669 5706 788 -555 189 N ATOM 1619 N LEU A 208 -3.558 -34.528 17.805 1.00 39.74 N ANISOU 1619 N LEU A 208 5693 3511 5898 1281 -356 -231 N ATOM 1620 CA LEU A 208 -3.254 -35.183 16.538 1.00 36.66 C ANISOU 1620 CA LEU A 208 5340 3065 5523 1357 -312 -332 C ATOM 1621 C LEU A 208 -1.827 -35.741 16.555 1.00 38.66 C ANISOU 1621 C LEU A 208 5543 3285 5862 1503 -315 -366 C ATOM 1622 O LEU A 208 -1.600 -36.909 16.222 1.00 43.86 O ANISOU 1622 O LEU A 208 6272 3824 6568 1580 -341 -411 O ATOM 1623 CB LEU A 208 -3.448 -34.209 15.372 1.00 36.27 C ANISOU 1623 CB LEU A 208 5251 3123 5408 1327 -217 -395 C ATOM 1624 CG LEU A 208 -4.907 -33.938 14.959 1.00 45.24 C ANISOU 1624 CG LEU A 208 6458 4267 6464 1203 -211 -392 C ATOM 1625 CD1 LEU A 208 -5.049 -32.649 14.150 1.00 49.63 C ANISOU 1625 CD1 LEU A 208 6949 4954 6953 1161 -127 -422 C ATOM 1626 CD2 LEU A 208 -5.495 -35.120 14.158 1.00 47.80 C ANISOU 1626 CD2 LEU A 208 6906 4470 6787 1209 -228 -454 C ATOM 1627 N ALA A1001 -0.873 -35.062 17.322 1.00 48.58 N ANISOU 1627 N ALA A1001 4494 3761 10203 351 467 -962 N ATOM 1628 CA ALA A1001 0.509 -35.505 17.378 1.00 48.00 C ANISOU 1628 CA ALA A1001 4403 3715 10119 380 516 -987 C ATOM 1629 C ALA A1001 0.583 -36.746 18.245 1.00 55.37 C ANISOU 1629 C ALA A1001 5334 4771 10933 401 455 -989 C ATOM 1630 O ALA A1001 1.334 -37.674 17.936 1.00 55.83 O ANISOU 1630 O ALA A1001 5460 4835 10918 431 470 -948 O ATOM 1631 CB ALA A1001 1.421 -34.426 17.907 1.00 41.39 C ANISOU 1631 CB ALA A1001 3419 2896 9411 372 580 -1098 C ATOM 1632 N ASP A1002 -0.231 -36.769 19.309 1.00 54.68 N ANISOU 1632 N ASP A1002 5174 4778 10824 385 388 -1034 N ATOM 1633 CA ASP A1002 -0.304 -37.948 20.168 1.00 55.30 C ANISOU 1633 CA ASP A1002 5252 4974 10785 402 323 -1034 C ATOM 1634 C ASP A1002 -0.873 -39.152 19.431 1.00 56.74 C ANISOU 1634 C ASP A1002 5600 5124 10835 416 277 -913 C ATOM 1635 O ASP A1002 -0.418 -40.282 19.637 1.00 56.05 O ANISOU 1635 O ASP A1002 5555 5093 10647 443 258 -888 O ATOM 1636 CB ASP A1002 -1.152 -37.660 21.404 1.00 56.87 C ANISOU 1636 CB ASP A1002 5344 5273 10993 380 260 -1103 C ATOM 1637 CG ASP A1002 -0.543 -36.617 22.281 1.00 67.14 C ANISOU 1637 CG ASP A1002 6478 6623 12408 368 299 -1227 C ATOM 1638 OD1 ASP A1002 0.617 -36.245 22.018 1.00 66.21 O ANISOU 1638 OD1 ASP A1002 6325 6477 12355 380 370 -1262 O ATOM 1639 OD2 ASP A1002 -1.230 -36.149 23.222 1.00 77.94 O ANISOU 1639 OD2 ASP A1002 7752 8058 13805 347 259 -1290 O ATOM 1640 N LEU A1003 -1.904 -38.951 18.612 1.00 50.82 N ANISOU 1640 N LEU A1003 4942 4286 10080 396 256 -838 N ATOM 1641 CA LEU A1003 -2.446 -40.088 17.881 1.00 52.83 C ANISOU 1641 CA LEU A1003 5358 4506 10208 406 213 -722 C ATOM 1642 C LEU A1003 -1.394 -40.681 16.957 1.00 51.37 C ANISOU 1642 C LEU A1003 5273 4259 9988 437 269 -667 C ATOM 1643 O LEU A1003 -1.207 -41.906 16.905 1.00 52.69 O ANISOU 1643 O LEU A1003 5525 4459 10038 461 242 -614 O ATOM 1644 CB LEU A1003 -3.681 -39.668 17.093 1.00 56.19 C ANISOU 1644 CB LEU A1003 5863 4840 10645 377 186 -652 C ATOM 1645 CG LEU A1003 -4.959 -39.594 17.911 1.00 55.82 C ANISOU 1645 CG LEU A1003 5768 4862 10579 352 107 -668 C ATOM 1646 CD1 LEU A1003 -5.942 -38.745 17.178 1.00 57.88 C ANISOU 1646 CD1 LEU A1003 6066 5027 10900 323 105 -627 C ATOM 1647 CD2 LEU A1003 -5.511 -40.989 18.099 1.00 60.85 C ANISOU 1647 CD2 LEU A1003 6497 5558 11066 361 30 -601 C ATOM 1648 N GLU A1004 -0.690 -39.816 16.228 1.00 53.27 N ANISOU 1648 N GLU A1004 5503 4408 10329 437 350 -680 N ATOM 1649 CA GLU A1004 0.351 -40.270 15.317 1.00 60.93 C ANISOU 1649 CA GLU A1004 6563 5312 11277 467 412 -630 C ATOM 1650 C GLU A1004 1.514 -40.913 16.071 1.00 62.67 C ANISOU 1650 C GLU A1004 6720 5629 11465 500 430 -682 C ATOM 1651 O GLU A1004 2.125 -41.867 15.579 1.00 62.46 O ANISOU 1651 O GLU A1004 6788 5587 11356 531 445 -624 O ATOM 1652 CB GLU A1004 0.839 -39.094 14.472 1.00 70.11 C ANISOU 1652 CB GLU A1004 7711 6361 12566 458 496 -642 C ATOM 1653 CG GLU A1004 1.732 -39.482 13.300 1.00 75.19 C ANISOU 1653 CG GLU A1004 8468 6911 13189 486 562 -573 C ATOM 1654 CD GLU A1004 1.104 -40.539 12.399 1.00 77.53 C ANISOU 1654 CD GLU A1004 8947 7152 13360 494 522 -450 C ATOM 1655 OE1 GLU A1004 1.837 -41.466 11.999 1.00 79.13 O ANISOU 1655 OE1 GLU A1004 9233 7347 13487 527 543 -403 O ATOM 1656 OE2 GLU A1004 -0.111 -40.451 12.098 1.00 77.21 O ANISOU 1656 OE2 GLU A1004 8965 7075 13296 469 470 -399 O ATOM 1657 N ASP A1005 1.836 -40.402 17.265 1.00 64.48 N ANISOU 1657 N ASP A1005 6788 5957 11755 493 428 -792 N ATOM 1658 CA ASP A1005 2.916 -40.985 18.055 1.00 62.44 C ANISOU 1658 CA ASP A1005 6459 5797 11466 523 440 -846 C ATOM 1659 C ASP A1005 2.560 -42.388 18.521 1.00 62.76 C ANISOU 1659 C ASP A1005 6563 5921 11359 542 368 -801 C ATOM 1660 O ASP A1005 3.378 -43.307 18.407 1.00 59.40 O ANISOU 1660 O ASP A1005 6188 5519 10864 577 384 -773 O ATOM 1661 CB ASP A1005 3.246 -40.106 19.258 1.00 65.64 C ANISOU 1661 CB ASP A1005 6680 6292 11969 508 448 -974 C ATOM 1662 CG ASP A1005 3.997 -38.845 18.874 1.00 73.33 C ANISOU 1662 CG ASP A1005 7580 7195 13086 497 533 -1028 C ATOM 1663 OD1 ASP A1005 4.435 -38.737 17.705 1.00 75.84 O ANISOU 1663 OD1 ASP A1005 7988 7403 13426 507 592 -969 O ATOM 1664 OD2 ASP A1005 4.144 -37.957 19.748 1.00 74.74 O ANISOU 1664 OD2 ASP A1005 7613 7428 13355 478 541 -1131 O ATOM 1665 N ASN A1006 1.351 -42.568 19.073 1.00 61.06 N ANISOU 1665 N ASN A1006 6346 5756 11098 520 288 -795 N ATOM 1666 CA ASN A1006 0.952 -43.897 19.520 1.00 63.38 C ANISOU 1666 CA ASN A1006 6703 6128 11251 536 218 -751 C ATOM 1667 C ASN A1006 1.015 -44.893 18.365 1.00 55.51 C ANISOU 1667 C ASN A1006 5886 5051 10154 557 224 -633 C ATOM 1668 O ASN A1006 1.515 -46.013 18.522 1.00 52.11 O ANISOU 1668 O ASN A1006 5505 4670 9625 589 212 -605 O ATOM 1669 CB ASN A1006 -0.452 -43.854 20.132 1.00 70.53 C ANISOU 1669 CB ASN A1006 7590 7082 12128 505 134 -753 C ATOM 1670 CG ASN A1006 -0.450 -43.578 21.644 1.00 76.59 C ANISOU 1670 CG ASN A1006 8194 7982 12923 498 102 -863 C ATOM 1671 OD1 ASN A1006 0.465 -43.969 22.372 1.00 80.26 O ANISOU 1671 OD1 ASN A1006 8590 8533 13371 523 114 -917 O ATOM 1672 ND2 ASN A1006 -1.505 -42.920 22.119 1.00 74.79 N ANISOU 1672 ND2 ASN A1006 7908 7773 12736 466 60 -894 N ATOM 1673 N TRP A1007 0.547 -44.474 17.186 1.00 50.18 N ANISOU 1673 N TRP A1007 5310 4251 9507 542 245 -564 N ATOM 1674 CA TRP A1007 0.577 -45.313 15.992 1.00 44.67 C ANISOU 1674 CA TRP A1007 4787 3463 8722 559 254 -450 C ATOM 1675 C TRP A1007 2.002 -45.715 15.625 1.00 45.42 C ANISOU 1675 C TRP A1007 4905 3542 8811 599 326 -447 C ATOM 1676 O TRP A1007 2.297 -46.904 15.435 1.00 49.71 O ANISOU 1676 O TRP A1007 5545 4101 9242 628 314 -388 O ATOM 1677 CB TRP A1007 -0.093 -44.556 14.846 1.00 46.87 C ANISOU 1677 CB TRP A1007 5144 3608 9055 532 273 -393 C ATOM 1678 CG TRP A1007 -0.136 -45.282 13.544 1.00 52.56 C ANISOU 1678 CG TRP A1007 6048 4226 9696 545 285 -276 C ATOM 1679 CD1 TRP A1007 0.589 -44.994 12.422 1.00 54.68 C ANISOU 1679 CD1 TRP A1007 6387 4384 10006 559 362 -237 C ATOM 1680 CD2 TRP A1007 -0.964 -46.408 13.211 1.00 48.50 C ANISOU 1680 CD2 TRP A1007 5674 3707 9046 544 217 -181 C ATOM 1681 NE1 TRP A1007 0.269 -45.876 11.421 1.00 51.69 N ANISOU 1681 NE1 TRP A1007 6185 3932 9525 567 346 -125 N ATOM 1682 CE2 TRP A1007 -0.681 -46.751 11.879 1.00 47.67 C ANISOU 1682 CE2 TRP A1007 5721 3485 8906 558 258 -89 C ATOM 1683 CE3 TRP A1007 -1.924 -47.157 13.916 1.00 50.12 C ANISOU 1683 CE3 TRP A1007 5891 3995 9157 533 127 -166 C ATOM 1684 CZ2 TRP A1007 -1.316 -47.813 11.229 1.00 53.54 C ANISOU 1684 CZ2 TRP A1007 6629 4192 9522 559 210 16 C ATOM 1685 CZ3 TRP A1007 -2.556 -48.209 13.273 1.00 52.63 C ANISOU 1685 CZ3 TRP A1007 6370 4277 9350 533 80 -60 C ATOM 1686 CH2 TRP A1007 -2.250 -48.530 11.942 1.00 54.95 C ANISOU 1686 CH2 TRP A1007 6815 4453 9610 546 121 29 C ATOM 1687 N GLU A1008 2.904 -44.737 15.527 1.00 45.89 N ANISOU 1687 N GLU A1008 4875 3571 8991 601 403 -509 N ATOM 1688 CA GLU A1008 4.290 -45.033 15.175 1.00 54.49 C ANISOU 1688 CA GLU A1008 5976 4644 10085 639 476 -509 C ATOM 1689 C GLU A1008 4.959 -45.909 16.226 1.00 55.27 C ANISOU 1689 C GLU A1008 6011 4871 10116 669 455 -552 C ATOM 1690 O GLU A1008 5.761 -46.784 15.890 1.00 54.23 O ANISOU 1690 O GLU A1008 5949 4737 9917 707 482 -509 O ATOM 1691 CB GLU A1008 5.078 -43.737 14.984 1.00 59.01 C ANISOU 1691 CB GLU A1008 6447 5168 10808 631 558 -576 C ATOM 1692 CG GLU A1008 4.629 -42.918 13.794 1.00 69.07 C ANISOU 1692 CG GLU A1008 7795 6300 12147 608 594 -526 C ATOM 1693 CD GLU A1008 5.221 -41.522 13.801 1.00 83.31 C ANISOU 1693 CD GLU A1008 9479 8069 14106 593 664 -606 C ATOM 1694 OE1 GLU A1008 6.147 -41.272 14.609 1.00 87.51 O ANISOU 1694 OE1 GLU A1008 9882 8676 14690 604 694 -693 O ATOM 1695 OE2 GLU A1008 4.758 -40.672 13.007 1.00 89.29 O ANISOU 1695 OE2 GLU A1008 10270 8722 14933 570 689 -582 O ATOM 1696 N THR A1009 4.654 -45.676 17.502 1.00 55.53 N ANISOU 1696 N THR A1009 5912 5019 10169 654 408 -637 N ATOM 1697 CA THR A1009 5.183 -46.531 18.559 1.00 55.56 C ANISOU 1697 CA THR A1009 5856 5152 10103 681 379 -677 C ATOM 1698 C THR A1009 4.700 -47.964 18.392 1.00 53.09 C ANISOU 1698 C THR A1009 5680 4857 9634 701 322 -587 C ATOM 1699 O THR A1009 5.464 -48.921 18.582 1.00 51.25 O ANISOU 1699 O THR A1009 5474 4674 9326 739 330 -572 O ATOM 1700 CB THR A1009 4.769 -45.975 19.922 1.00 59.75 C ANISOU 1700 CB THR A1009 6228 5794 10680 657 333 -779 C ATOM 1701 OG1 THR A1009 5.335 -44.665 20.079 1.00 65.77 O ANISOU 1701 OG1 THR A1009 6863 6540 11588 641 392 -866 O ATOM 1702 CG2 THR A1009 5.260 -46.874 21.050 1.00 53.39 C ANISOU 1702 CG2 THR A1009 5361 5127 9799 685 299 -820 C ATOM 1703 N LEU A1010 3.434 -48.132 18.024 1.00 45.85 N ANISOU 1703 N LEU A1010 4854 3900 8667 675 264 -524 N ATOM 1704 CA LEU A1010 2.935 -49.465 17.745 1.00 45.05 C ANISOU 1704 CA LEU A1010 4895 3803 8419 689 212 -432 C ATOM 1705 C LEU A1010 3.744 -50.122 16.625 1.00 45.36 C ANISOU 1705 C LEU A1010 5070 3756 8409 724 269 -351 C ATOM 1706 O LEU A1010 4.217 -51.261 16.757 1.00 41.71 O ANISOU 1706 O LEU A1010 4665 3338 7845 759 261 -318 O ATOM 1707 CB LEU A1010 1.451 -49.387 17.388 1.00 43.29 C ANISOU 1707 CB LEU A1010 4749 3534 8166 652 148 -375 C ATOM 1708 CG LEU A1010 0.843 -50.765 17.210 1.00 48.68 C ANISOU 1708 CG LEU A1010 5571 4230 8694 662 85 -285 C ATOM 1709 CD1 LEU A1010 1.030 -51.480 18.516 1.00 51.38 C ANISOU 1709 CD1 LEU A1010 5832 4716 8974 679 40 -338 C ATOM 1710 CD2 LEU A1010 -0.636 -50.631 16.857 1.00 51.87 C ANISOU 1710 CD2 LEU A1010 6045 4590 9075 621 21 -230 C ATOM 1711 N ASN A1011 3.959 -49.399 15.532 1.00 44.30 N ANISOU 1711 N ASN A1011 4984 3500 8349 717 331 -322 N ATOM 1712 CA ASN A1011 4.606 -50.016 14.381 1.00 46.39 C ANISOU 1712 CA ASN A1011 5391 3673 8563 747 383 -237 C ATOM 1713 C ASN A1011 6.106 -50.177 14.584 1.00 45.76 C ANISOU 1713 C ASN A1011 5252 3628 8508 789 453 -277 C ATOM 1714 O ASN A1011 6.686 -51.146 14.091 1.00 45.00 O ANISOU 1714 O ASN A1011 5261 3511 8327 826 475 -214 O ATOM 1715 CB ASN A1011 4.304 -49.210 13.120 1.00 48.69 C ANISOU 1715 CB ASN A1011 5759 3821 8921 725 425 -187 C ATOM 1716 CG ASN A1011 2.886 -49.465 12.606 1.00 53.79 C ANISOU 1716 CG ASN A1011 6523 4415 9502 694 356 -108 C ATOM 1717 OD1 ASN A1011 2.395 -50.597 12.641 1.00 55.75 O ANISOU 1717 OD1 ASN A1011 6869 4691 9623 702 299 -47 O ATOM 1718 ND2 ASN A1011 2.228 -48.421 12.140 1.00 57.13 N ANISOU 1718 ND2 ASN A1011 6933 4763 10010 659 362 -109 N ATOM 1719 N ASP A1012 6.744 -49.262 15.306 1.00 46.08 N ANISOU 1719 N ASP A1012 5128 3721 8660 784 487 -380 N ATOM 1720 CA ASP A1012 8.160 -49.437 15.587 1.00 47.93 C ANISOU 1720 CA ASP A1012 5296 3998 8916 823 548 -421 C ATOM 1721 C ASP A1012 8.393 -50.603 16.528 1.00 45.68 C ANISOU 1721 C ASP A1012 4996 3837 8524 853 502 -430 C ATOM 1722 O ASP A1012 9.358 -51.355 16.366 1.00 42.36 O ANISOU 1722 O ASP A1012 4614 3428 8054 896 540 -405 O ATOM 1723 CB ASP A1012 8.735 -48.158 16.159 1.00 49.50 C ANISOU 1723 CB ASP A1012 5320 4225 9261 807 592 -530 C ATOM 1724 CG ASP A1012 8.620 -47.026 15.188 1.00 58.42 C ANISOU 1724 CG ASP A1012 6469 5231 10499 782 646 -520 C ATOM 1725 OD1 ASP A1012 8.338 -47.330 14.011 1.00 65.79 O ANISOU 1725 OD1 ASP A1012 7553 6054 11389 785 661 -424 O ATOM 1726 OD2 ASP A1012 8.762 -45.857 15.590 1.00 58.45 O ANISOU 1726 OD2 ASP A1012 6340 5243 10625 757 671 -604 O ATOM 1727 N ASN A1013 7.526 -50.784 17.515 1.00 46.27 N ANISOU 1727 N ASN A1013 5016 4004 8559 833 422 -464 N ATOM 1728 CA ASN A1013 7.789 -51.870 18.450 1.00 47.20 C ANISOU 1728 CA ASN A1013 5113 4243 8578 862 380 -477 C ATOM 1729 C ASN A1013 7.504 -53.233 17.827 1.00 41.34 C ANISOU 1729 C ASN A1013 4549 3470 7690 887 352 -367 C ATOM 1730 O ASN A1013 8.168 -54.215 18.172 1.00 39.54 O ANISOU 1730 O ASN A1013 4338 3304 7381 927 354 -356 O ATOM 1731 CB ASN A1013 7.007 -51.643 19.736 1.00 52.55 C ANISOU 1731 CB ASN A1013 5673 5033 9260 835 305 -551 C ATOM 1732 CG ASN A1013 7.755 -50.741 20.700 1.00 50.00 C ANISOU 1732 CG ASN A1013 5160 4789 9049 831 334 -671 C ATOM 1733 OD1 ASN A1013 8.967 -50.841 20.838 1.00 54.53 O ANISOU 1733 OD1 ASN A1013 5683 5391 9645 863 388 -701 O ATOM 1734 ND2 ASN A1013 7.044 -49.874 21.361 1.00 48.48 N ANISOU 1734 ND2 ASN A1013 4865 4632 8925 792 300 -738 N ATOM 1735 N LEU A1014 6.576 -53.307 16.874 1.00 41.54 N ANISOU 1735 N LEU A1014 4709 3395 7679 864 332 -284 N ATOM 1736 CA LEU A1014 6.430 -54.534 16.105 1.00 44.46 C ANISOU 1736 CA LEU A1014 5259 3716 7918 888 319 -176 C ATOM 1737 C LEU A1014 7.747 -54.923 15.437 1.00 45.73 C ANISOU 1737 C LEU A1014 5473 3830 8072 935 402 -145 C ATOM 1738 O LEU A1014 8.132 -56.105 15.437 1.00 42.67 O ANISOU 1738 O LEU A1014 5167 3472 7575 972 396 -97 O ATOM 1739 CB LEU A1014 5.313 -54.372 15.074 1.00 45.35 C ANISOU 1739 CB LEU A1014 5503 3715 8013 853 294 -95 C ATOM 1740 CG LEU A1014 3.901 -54.508 15.642 1.00 48.58 C ANISOU 1740 CG LEU A1014 5912 4173 8374 815 197 -91 C ATOM 1741 CD1 LEU A1014 2.873 -54.056 14.625 1.00 46.70 C ANISOU 1741 CD1 LEU A1014 5775 3819 8150 778 182 -25 C ATOM 1742 CD2 LEU A1014 3.647 -55.961 16.063 1.00 50.86 C ANISOU 1742 CD2 LEU A1014 6281 4533 8512 837 137 -44 C ATOM 1743 N LYS A1015 8.468 -53.940 14.891 1.00 47.01 N ANISOU 1743 N LYS A1015 5588 3922 8350 934 480 -172 N ATOM 1744 CA LYS A1015 9.743 -54.231 14.238 1.00 46.70 C ANISOU 1744 CA LYS A1015 5593 3837 8314 978 564 -144 C ATOM 1745 C LYS A1015 10.811 -54.603 15.250 1.00 46.66 C ANISOU 1745 C LYS A1015 5472 3951 8306 1016 581 -210 C ATOM 1746 O LYS A1015 11.639 -55.478 14.984 1.00 49.72 O ANISOU 1746 O LYS A1015 5925 4338 8626 1062 616 -168 O ATOM 1747 CB LYS A1015 10.201 -53.028 13.419 1.00 48.53 C ANISOU 1747 CB LYS A1015 5799 3965 8677 966 643 -159 C ATOM 1748 CG LYS A1015 9.239 -52.648 12.337 1.00 56.10 C ANISOU 1748 CG LYS A1015 6875 4799 9641 932 634 -90 C ATOM 1749 CD LYS A1015 9.511 -51.251 11.806 1.00 61.63 C ANISOU 1749 CD LYS A1015 7511 5417 10488 910 699 -128 C ATOM 1750 CE LYS A1015 8.682 -50.981 10.550 1.00 68.12 C ANISOU 1750 CE LYS A1015 8474 6102 11306 884 700 -45 C ATOM 1751 NZ LYS A1015 8.979 -51.979 9.464 1.00 70.87 N ANISOU 1751 NZ LYS A1015 9006 6368 11554 917 727 63 N ATOM 1752 N VAL A1016 10.837 -53.924 16.402 1.00 47.78 N ANISOU 1752 N VAL A1016 5440 4193 8522 997 559 -314 N ATOM 1753 CA VAL A1016 11.721 -54.349 17.489 1.00 49.15 C ANISOU 1753 CA VAL A1016 5501 4493 8681 1030 560 -378 C ATOM 1754 C VAL A1016 11.528 -55.841 17.760 1.00 47.74 C ANISOU 1754 C VAL A1016 5420 4373 8347 1061 509 -319 C ATOM 1755 O VAL A1016 12.480 -56.627 17.724 1.00 44.42 O ANISOU 1755 O VAL A1016 5027 3975 7873 1109 545 -296 O ATOM 1756 CB VAL A1016 11.472 -53.506 18.758 1.00 44.44 C ANISOU 1756 CB VAL A1016 4719 4000 8165 998 522 -493 C ATOM 1757 CG1 VAL A1016 12.334 -54.006 19.908 1.00 46.29 C ANISOU 1757 CG1 VAL A1016 4841 4371 8375 1031 517 -556 C ATOM 1758 CG2 VAL A1016 11.766 -52.085 18.510 1.00 45.28 C ANISOU 1758 CG2 VAL A1016 4730 4051 8422 971 577 -552 C ATOM 1759 N ILE A1017 10.276 -56.257 17.989 1.00 45.92 N ANISOU 1759 N ILE A1017 5248 4161 8041 1035 426 -289 N ATOM 1760 CA ILE A1017 9.987 -57.663 18.282 1.00 45.88 C ANISOU 1760 CA ILE A1017 5336 4212 7886 1060 372 -234 C ATOM 1761 C ILE A1017 10.474 -58.569 17.154 1.00 47.37 C ANISOU 1761 C ILE A1017 5695 4310 7992 1098 417 -131 C ATOM 1762 O ILE A1017 11.050 -59.640 17.404 1.00 44.13 O ANISOU 1762 O ILE A1017 5324 3952 7490 1142 419 -105 O ATOM 1763 CB ILE A1017 8.481 -57.867 18.550 1.00 42.11 C ANISOU 1763 CB ILE A1017 4903 3750 7348 1019 279 -211 C ATOM 1764 CG1 ILE A1017 8.087 -57.303 19.919 1.00 38.88 C ANISOU 1764 CG1 ILE A1017 4323 3460 6989 994 227 -313 C ATOM 1765 CG2 ILE A1017 8.126 -59.369 18.469 1.00 38.48 C ANISOU 1765 CG2 ILE A1017 4586 3308 6726 1044 232 -127 C ATOM 1766 CD1 ILE A1017 6.636 -56.908 20.010 1.00 39.52 C ANISOU 1766 CD1 ILE A1017 4415 3527 7072 943 157 -307 C ATOM 1767 N GLU A1018 10.245 -58.160 15.897 1.00 51.07 N ANISOU 1767 N GLU A1018 6270 4643 8490 1083 454 -69 N ATOM 1768 CA GLU A1018 10.573 -59.012 14.756 1.00 48.62 C ANISOU 1768 CA GLU A1018 6139 4239 8097 1115 492 34 C ATOM 1769 C GLU A1018 12.061 -59.274 14.655 1.00 56.25 C ANISOU 1769 C GLU A1018 7080 5215 9079 1169 574 26 C ATOM 1770 O GLU A1018 12.468 -60.338 14.181 1.00 61.94 O ANISOU 1770 O GLU A1018 7925 5912 9700 1209 593 98 O ATOM 1771 CB GLU A1018 10.085 -58.382 13.459 1.00 49.32 C ANISOU 1771 CB GLU A1018 6331 4180 8228 1086 520 92 C ATOM 1772 CG GLU A1018 8.663 -58.697 13.099 1.00 45.78 C ANISOU 1772 CG GLU A1018 5999 3690 7706 1049 445 156 C ATOM 1773 CD GLU A1018 8.059 -57.622 12.250 1.00 57.63 C ANISOU 1773 CD GLU A1018 7523 5080 9294 1007 460 170 C ATOM 1774 OE1 GLU A1018 8.815 -56.724 11.805 1.00 61.88 O ANISOU 1774 OE1 GLU A1018 8008 5562 9942 1011 537 141 O ATOM 1775 OE2 GLU A1018 6.826 -57.657 12.041 1.00 61.69 O ANISOU 1775 OE2 GLU A1018 8105 5564 9769 969 396 210 O ATOM 1776 N LYS A1019 12.898 -58.333 15.080 1.00 60.20 N ANISOU 1776 N LYS A1019 7425 5749 9701 1171 624 -60 N ATOM 1777 CA LYS A1019 14.336 -58.564 15.008 1.00 62.79 C ANISOU 1777 CA LYS A1019 7721 6090 10047 1222 702 -68 C ATOM 1778 C LYS A1019 14.987 -58.674 16.380 1.00 58.47 C ANISOU 1778 C LYS A1019 7011 5692 9514 1241 687 -157 C ATOM 1779 O LYS A1019 16.210 -58.554 16.491 1.00 53.21 O ANISOU 1779 O LYS A1019 6272 5050 8897 1276 752 -189 O ATOM 1780 CB LYS A1019 15.019 -57.479 14.178 1.00 67.24 C ANISOU 1780 CB LYS A1019 8255 6554 10737 1216 790 -81 C ATOM 1781 CG LYS A1019 14.866 -56.081 14.692 1.00 71.00 C ANISOU 1781 CG LYS A1019 8570 7053 11354 1173 790 -178 C ATOM 1782 CD LYS A1019 15.015 -55.116 13.528 1.00 78.00 C ANISOU 1782 CD LYS A1019 9495 7802 12337 1156 859 -155 C ATOM 1783 CE LYS A1019 14.253 -55.615 12.297 1.00 81.35 C ANISOU 1783 CE LYS A1019 10123 8105 12682 1150 850 -43 C ATOM 1784 NZ LYS A1019 14.304 -54.626 11.178 1.00 85.87 N ANISOU 1784 NZ LYS A1019 10733 8545 13351 1130 913 -22 N ATOM 1785 N ALA A1020 14.199 -58.904 17.427 1.00 60.76 N ANISOU 1785 N ALA A1020 7242 6083 9761 1221 603 -197 N ATOM 1786 CA ALA A1020 14.788 -59.281 18.700 1.00 64.07 C ANISOU 1786 CA ALA A1020 7535 6646 10164 1246 582 -265 C ATOM 1787 C ALA A1020 15.514 -60.617 18.551 1.00 64.74 C ANISOU 1787 C ALA A1020 7714 6751 10133 1306 602 -201 C ATOM 1788 O ALA A1020 15.237 -61.409 17.647 1.00 58.22 O ANISOU 1788 O ALA A1020 7061 5844 9216 1321 606 -104 O ATOM 1789 CB ALA A1020 13.718 -59.377 19.783 1.00 61.24 C ANISOU 1789 CB ALA A1020 7116 6385 9767 1213 485 -308 C ATOM 1790 N ASP A1021 16.465 -60.867 19.444 1.00 79.58 N ANISOU 1790 N ASP A1021 9479 8739 12017 1341 617 -257 N ATOM 1791 CA ASP A1021 17.171 -62.143 19.409 1.00 86.92 C ANISOU 1791 CA ASP A1021 10488 9699 12839 1400 634 -201 C ATOM 1792 C ASP A1021 17.122 -62.867 20.749 1.00 85.25 C ANISOU 1792 C ASP A1021 10197 9637 12555 1416 571 -245 C ATOM 1793 O ASP A1021 17.913 -63.787 20.976 1.00 86.53 O ANISOU 1793 O ASP A1021 10378 9851 12648 1469 590 -223 O ATOM 1794 CB ASP A1021 18.617 -61.955 18.941 1.00 98.85 C ANISOU 1794 CB ASP A1021 11967 11179 14411 1442 733 -203 C ATOM 1795 CG ASP A1021 19.481 -61.256 19.965 1.00105.14 C ANISOU 1795 CG ASP A1021 12560 12081 15308 1446 752 -311 C ATOM 1796 OD1 ASP A1021 18.997 -60.283 20.590 1.00103.85 O ANISOU 1796 OD1 ASP A1021 12274 11956 15230 1399 718 -391 O ATOM 1797 OD2 ASP A1021 20.647 -61.692 20.141 1.00108.30 O ANISOU 1797 OD2 ASP A1021 12924 12527 15700 1496 800 -314 O ATOM 1798 N ASN A1022 16.200 -62.483 21.632 1.00 76.56 N ANISOU 1798 N ASN A1022 9014 8607 11468 1374 496 -304 N ATOM 1799 CA ASN A1022 15.965 -63.213 22.871 1.00 69.16 C ANISOU 1799 CA ASN A1022 8019 7806 10452 1385 426 -338 C ATOM 1800 C ASN A1022 14.586 -62.862 23.411 1.00 66.25 C ANISOU 1800 C ASN A1022 7625 7467 10080 1330 341 -367 C ATOM 1801 O ASN A1022 13.951 -61.886 22.990 1.00 58.75 O ANISOU 1801 O ASN A1022 6665 6446 9210 1284 340 -381 O ATOM 1802 CB ASN A1022 17.034 -62.910 23.925 1.00 65.10 C ANISOU 1802 CB ASN A1022 7324 7410 10000 1408 448 -431 C ATOM 1803 CG ASN A1022 17.139 -61.440 24.227 1.00 61.81 C ANISOU 1803 CG ASN A1022 6752 6998 9734 1366 467 -526 C ATOM 1804 OD1 ASN A1022 16.273 -60.867 24.882 1.00 59.19 O ANISOU 1804 OD1 ASN A1022 6347 6708 9435 1322 409 -582 O ATOM 1805 ND2 ASN A1022 18.205 -60.814 23.741 1.00 63.91 N ANISOU 1805 ND2 ASN A1022 6970 7219 10095 1381 550 -544 N ATOM 1806 N ALA A1023 14.153 -63.657 24.395 1.00 60.08 N ANISOU 1806 N ALA A1023 6827 6795 9208 1338 271 -379 N ATOM 1807 CA ALA A1023 12.844 -63.446 24.998 1.00 55.86 C ANISOU 1807 CA ALA A1023 6267 6298 8657 1290 187 -405 C ATOM 1808 C ALA A1023 12.751 -62.089 25.692 1.00 57.32 C ANISOU 1808 C ALA A1023 6277 6527 8977 1249 182 -513 C ATOM 1809 O ALA A1023 11.683 -61.473 25.690 1.00 59.07 O ANISOU 1809 O ALA A1023 6493 6721 9231 1200 140 -526 O ATOM 1810 CB ALA A1023 12.527 -64.586 25.970 1.00 52.68 C ANISOU 1810 CB ALA A1023 5873 6011 8132 1310 118 -400 C ATOM 1811 N ALA A1024 13.853 -61.589 26.260 1.00 58.00 N ANISOU 1811 N ALA A1024 6220 6676 9143 1267 226 -591 N ATOM 1812 CA ALA A1024 13.776 -60.376 27.074 1.00 57.27 C ANISOU 1812 CA ALA A1024 5953 6639 9168 1229 215 -700 C ATOM 1813 C ALA A1024 13.517 -59.134 26.234 1.00 59.21 C ANISOU 1813 C ALA A1024 6195 6770 9532 1188 255 -708 C ATOM 1814 O ALA A1024 12.848 -58.202 26.699 1.00 54.86 O ANISOU 1814 O ALA A1024 5554 6236 9055 1143 224 -772 O ATOM 1815 CB ALA A1024 15.055 -60.191 27.884 1.00 59.14 C ANISOU 1815 CB ALA A1024 6039 6973 9457 1259 252 -779 C ATOM 1816 N GLN A1025 14.046 -59.087 25.010 1.00 57.76 N ANISOU 1816 N GLN A1025 6107 6470 9369 1204 325 -645 N ATOM 1817 CA GLN A1025 13.788 -57.932 24.156 1.00 52.28 C ANISOU 1817 CA GLN A1025 5418 5661 8784 1167 364 -647 C ATOM 1818 C GLN A1025 12.340 -57.919 23.691 1.00 48.93 C ANISOU 1818 C GLN A1025 5100 5171 8321 1126 308 -594 C ATOM 1819 O GLN A1025 11.669 -56.882 23.740 1.00 52.96 O ANISOU 1819 O GLN A1025 5551 5654 8916 1080 293 -637 O ATOM 1820 CB GLN A1025 14.748 -57.936 22.969 1.00 53.20 C ANISOU 1820 CB GLN A1025 5614 5672 8927 1197 454 -591 C ATOM 1821 CG GLN A1025 16.191 -57.874 23.419 1.00 59.42 C ANISOU 1821 CG GLN A1025 6290 6525 9763 1235 511 -645 C ATOM 1822 CD GLN A1025 17.183 -58.012 22.296 1.00 61.21 C ANISOU 1822 CD GLN A1025 6598 6656 10005 1271 600 -584 C ATOM 1823 OE1 GLN A1025 18.374 -58.157 22.543 1.00 67.53 O ANISOU 1823 OE1 GLN A1025 7331 7502 10826 1309 649 -609 O ATOM 1824 NE2 GLN A1025 16.707 -57.961 21.056 1.00 58.35 N ANISOU 1824 NE2 GLN A1025 6379 6159 9633 1260 622 -504 N ATOM 1825 N VAL A1026 11.834 -59.069 23.247 1.00 48.88 N ANISOU 1825 N VAL A1026 5249 5138 8185 1143 275 -501 N ATOM 1826 CA VAL A1026 10.410 -59.166 22.937 1.00 46.42 C ANISOU 1826 CA VAL A1026 5033 4780 7825 1104 211 -451 C ATOM 1827 C VAL A1026 9.589 -58.685 24.121 1.00 49.61 C ANISOU 1827 C VAL A1026 5312 5282 8256 1067 140 -531 C ATOM 1828 O VAL A1026 8.661 -57.877 23.965 1.00 50.55 O ANISOU 1828 O VAL A1026 5418 5357 8431 1021 115 -544 O ATOM 1829 CB VAL A1026 10.038 -60.606 22.545 1.00 48.31 C ANISOU 1829 CB VAL A1026 5442 5006 7909 1130 177 -350 C ATOM 1830 CG1 VAL A1026 8.551 -60.686 22.237 1.00 42.55 C ANISOU 1830 CG1 VAL A1026 4807 4230 7132 1086 108 -299 C ATOM 1831 CG2 VAL A1026 10.904 -61.083 21.352 1.00 44.81 C ANISOU 1831 CG2 VAL A1026 5125 4461 7438 1169 252 -270 C ATOM 1832 N LYS A1027 9.944 -59.148 25.331 1.00 51.07 N ANISOU 1832 N LYS A1027 5399 5601 8404 1088 109 -589 N ATOM 1833 CA LYS A1027 9.185 -58.774 26.529 1.00 59.45 C ANISOU 1833 CA LYS A1027 6342 6764 9482 1056 41 -665 C ATOM 1834 C LYS A1027 9.161 -57.264 26.730 1.00 58.04 C ANISOU 1834 C LYS A1027 6028 6571 9453 1017 64 -753 C ATOM 1835 O LYS A1027 8.111 -56.688 27.043 1.00 52.52 O ANISOU 1835 O LYS A1027 5294 5876 8783 974 16 -779 O ATOM 1836 CB LYS A1027 9.751 -59.446 27.785 1.00 60.84 C ANISOU 1836 CB LYS A1027 6426 7086 9604 1088 14 -719 C ATOM 1837 CG LYS A1027 9.174 -58.820 29.071 1.00 60.44 C ANISOU 1837 CG LYS A1027 6224 7142 9599 1055 -43 -817 C ATOM 1838 CD LYS A1027 9.731 -59.404 30.360 1.00 65.05 C ANISOU 1838 CD LYS A1027 6706 7873 10135 1085 -70 -876 C ATOM 1839 CE LYS A1027 8.874 -58.937 31.545 1.00 69.93 C ANISOU 1839 CE LYS A1027 7210 8587 10775 1049 -138 -955 C ATOM 1840 NZ LYS A1027 9.211 -59.604 32.836 1.00 69.88 N ANISOU 1840 NZ LYS A1027 7119 8728 10706 1075 -178 -1006 N ATOM 1841 N ASP A1028 10.307 -56.606 26.557 1.00 62.94 N ANISOU 1841 N ASP A1028 6570 7174 10169 1031 139 -797 N ATOM 1842 CA ASP A1028 10.359 -55.171 26.810 1.00 62.75 C ANISOU 1842 CA ASP A1028 6410 7142 10288 994 163 -886 C ATOM 1843 C ASP A1028 9.528 -54.397 25.793 1.00 54.96 C ANISOU 1843 C ASP A1028 5498 6027 9359 954 174 -845 C ATOM 1844 O ASP A1028 8.831 -53.448 26.160 1.00 54.46 O ANISOU 1844 O ASP A1028 5354 5967 9370 912 150 -901 O ATOM 1845 CB ASP A1028 11.814 -54.697 26.821 1.00 73.88 C ANISOU 1845 CB ASP A1028 7726 8562 11785 1018 242 -939 C ATOM 1846 CG ASP A1028 12.595 -55.236 28.023 1.00 83.44 C ANISOU 1846 CG ASP A1028 8828 9915 12960 1050 226 -1000 C ATOM 1847 OD1 ASP A1028 12.090 -55.129 29.164 1.00 86.90 O ANISOU 1847 OD1 ASP A1028 9170 10456 13391 1032 166 -1066 O ATOM 1848 OD2 ASP A1028 13.707 -55.774 27.832 1.00 85.79 O ANISOU 1848 OD2 ASP A1028 9139 10224 13235 1094 274 -981 O ATOM 1849 N ALA A1029 9.579 -54.783 24.513 1.00 49.13 N ANISOU 1849 N ALA A1029 4911 5172 8584 968 209 -748 N ATOM 1850 CA ALA A1029 8.788 -54.069 23.513 1.00 46.28 C ANISOU 1850 CA ALA A1029 4624 4686 8274 931 218 -706 C ATOM 1851 C ALA A1029 7.290 -54.284 23.731 1.00 46.08 C ANISOU 1851 C ALA A1029 4649 4671 8188 897 133 -677 C ATOM 1852 O ALA A1029 6.492 -53.351 23.584 1.00 49.53 O ANISOU 1852 O ALA A1029 5059 5063 8698 855 120 -696 O ATOM 1853 CB ALA A1029 9.196 -54.497 22.104 1.00 40.12 C ANISOU 1853 CB ALA A1029 4000 3782 7461 955 274 -606 C ATOM 1854 N LEU A1030 6.890 -55.504 24.084 1.00 46.18 N ANISOU 1854 N LEU A1030 4735 4743 8070 915 75 -630 N ATOM 1855 CA LEU A1030 5.470 -55.784 24.336 1.00 48.24 C ANISOU 1855 CA LEU A1030 5044 5020 8267 883 -9 -601 C ATOM 1856 C LEU A1030 4.959 -55.083 25.589 1.00 44.06 C ANISOU 1856 C LEU A1030 4356 4591 7794 853 -55 -701 C ATOM 1857 O LEU A1030 3.785 -54.683 25.650 1.00 44.24 O ANISOU 1857 O LEU A1030 4384 4598 7828 814 -104 -697 O ATOM 1858 CB LEU A1030 5.243 -57.293 24.491 1.00 47.82 C ANISOU 1858 CB LEU A1030 5100 5014 8058 911 -58 -532 C ATOM 1859 CG LEU A1030 5.420 -58.229 23.298 1.00 48.43 C ANISOU 1859 CG LEU A1030 5362 4997 8044 937 -34 -418 C ATOM 1860 CD1 LEU A1030 5.575 -59.673 23.822 1.00 36.84 C ANISOU 1860 CD1 LEU A1030 3950 3612 6436 974 -73 -383 C ATOM 1861 CD2 LEU A1030 4.233 -58.110 22.319 1.00 39.79 C ANISOU 1861 CD2 LEU A1030 4396 3792 6930 900 -63 -338 C ATOM 1862 N THR A1031 5.806 -54.977 26.615 1.00 50.77 N ANISOU 1862 N THR A1031 5069 5547 8675 872 -43 -788 N ATOM 1863 CA THR A1031 5.438 -54.231 27.813 1.00 50.64 C ANISOU 1863 CA THR A1031 4896 5625 8722 845 -79 -890 C ATOM 1864 C THR A1031 5.023 -52.815 27.451 1.00 46.20 C ANISOU 1864 C THR A1031 4277 4987 8289 802 -54 -928 C ATOM 1865 O THR A1031 3.974 -52.334 27.891 1.00 47.41 O ANISOU 1865 O THR A1031 4390 5159 8463 766 -104 -955 O ATOM 1866 CB THR A1031 6.608 -54.222 28.792 1.00 56.66 C ANISOU 1866 CB THR A1031 5522 6495 9511 873 -54 -978 C ATOM 1867 OG1 THR A1031 6.884 -55.566 29.204 1.00 57.94 O ANISOU 1867 OG1 THR A1031 5735 6734 9546 912 -85 -942 O ATOM 1868 CG2 THR A1031 6.291 -53.364 30.009 1.00 54.48 C ANISOU 1868 CG2 THR A1031 5081 6312 9308 843 -86 -1089 C ATOM 1869 N LYS A1032 5.836 -52.140 26.629 1.00 48.16 N ANISOU 1869 N LYS A1032 4526 5148 8626 807 25 -929 N ATOM 1870 CA LYS A1032 5.508 -50.791 26.172 1.00 50.00 C ANISOU 1870 CA LYS A1032 4715 5297 8984 769 56 -959 C ATOM 1871 C LYS A1032 4.236 -50.787 25.342 1.00 51.50 C ANISOU 1871 C LYS A1032 5028 5395 9145 740 22 -877 C ATOM 1872 O LYS A1032 3.354 -49.938 25.535 1.00 57.56 O ANISOU 1872 O LYS A1032 5746 6150 9974 701 -4 -909 O ATOM 1873 CB LYS A1032 6.660 -50.216 25.349 1.00 54.50 C ANISOU 1873 CB LYS A1032 5280 5785 9641 783 149 -963 C ATOM 1874 CG LYS A1032 7.920 -49.871 26.130 1.00 61.61 C ANISOU 1874 CG LYS A1032 6036 6767 10607 802 192 -1057 C ATOM 1875 CD LYS A1032 9.048 -49.578 25.147 1.00 65.86 C ANISOU 1875 CD LYS A1032 6604 7215 11205 822 283 -1035 C ATOM 1876 CE LYS A1032 10.223 -48.870 25.793 1.00 68.00 C ANISOU 1876 CE LYS A1032 6716 7544 11575 829 334 -1136 C ATOM 1877 NZ LYS A1032 11.149 -48.373 24.741 1.00 68.17 N ANISOU 1877 NZ LYS A1032 6767 7462 11674 839 424 -1113 N ATOM 1878 N MET A1033 4.133 -51.712 24.383 1.00 48.93 N ANISOU 1878 N MET A1033 4865 4999 8725 759 22 -770 N ATOM 1879 CA MET A1033 2.937 -51.746 23.552 1.00 41.50 C ANISOU 1879 CA MET A1033 4047 3969 7752 731 -13 -688 C ATOM 1880 C MET A1033 1.690 -51.907 24.408 1.00 41.17 C ANISOU 1880 C MET A1033 3975 4002 7664 704 -101 -702 C ATOM 1881 O MET A1033 0.656 -51.294 24.128 1.00 41.95 O ANISOU 1881 O MET A1033 4089 4051 7799 666 -127 -687 O ATOM 1882 CB MET A1033 3.032 -52.864 22.513 1.00 46.94 C ANISOU 1882 CB MET A1033 4918 4587 8331 757 -6 -572 C ATOM 1883 CG MET A1033 4.145 -52.673 21.519 1.00 50.40 C ANISOU 1883 CG MET A1033 5402 4934 8815 782 83 -546 C ATOM 1884 SD MET A1033 4.488 -54.213 20.633 1.00 53.03 S ANISOU 1884 SD MET A1033 5929 5221 9001 824 89 -426 S ATOM 1885 CE MET A1033 3.044 -54.297 19.581 1.00 49.94 C ANISOU 1885 CE MET A1033 5697 4717 8562 787 44 -323 C ATOM 1886 N ARG A1034 1.767 -52.714 25.466 1.00 44.61 N ANISOU 1886 N ARG A1034 4368 4561 8022 722 -147 -731 N ATOM 1887 CA ARG A1034 0.581 -52.918 26.290 1.00 45.18 C ANISOU 1887 CA ARG A1034 4414 4707 8046 697 -231 -742 C ATOM 1888 C ARG A1034 0.151 -51.620 26.973 1.00 49.93 C ANISOU 1888 C ARG A1034 4870 5337 8765 662 -236 -836 C ATOM 1889 O ARG A1034 -1.035 -51.287 26.990 1.00 52.67 O ANISOU 1889 O ARG A1034 5227 5667 9119 627 -283 -821 O ATOM 1890 CB ARG A1034 0.827 -54.014 27.323 1.00 41.48 C ANISOU 1890 CB ARG A1034 3921 4366 7474 726 -275 -760 C ATOM 1891 CG ARG A1034 -0.453 -54.415 28.057 1.00 39.32 C ANISOU 1891 CG ARG A1034 3648 4161 7131 703 -365 -753 C ATOM 1892 CD ARG A1034 -0.179 -55.433 29.133 1.00 42.88 C ANISOU 1892 CD ARG A1034 4065 4741 7486 731 -406 -777 C ATOM 1893 NE ARG A1034 -1.443 -55.994 29.589 1.00 53.39 N ANISOU 1893 NE ARG A1034 5433 6119 8733 711 -490 -745 N ATOM 1894 CZ ARG A1034 -2.140 -55.534 30.618 1.00 60.95 C ANISOU 1894 CZ ARG A1034 6282 7157 9719 687 -537 -812 C ATOM 1895 NH1 ARG A1034 -1.683 -54.507 31.318 1.00 65.94 N ANISOU 1895 NH1 ARG A1034 6760 7834 10460 679 -508 -917 N ATOM 1896 NH2 ARG A1034 -3.290 -56.106 30.947 1.00 65.03 N ANISOU 1896 NH2 ARG A1034 6844 7709 10154 669 -611 -773 N ATOM 1897 N ALA A1035 1.108 -50.868 27.520 1.00 53.63 N ANISOU 1897 N ALA A1035 5203 5846 9329 669 -188 -931 N ATOM 1898 CA ALA A1035 0.798 -49.593 28.164 1.00 52.02 C ANISOU 1898 CA ALA A1035 4857 5665 9242 635 -186 -1025 C ATOM 1899 C ALA A1035 0.183 -48.604 27.180 1.00 52.04 C ANISOU 1899 C ALA A1035 4901 5543 9330 603 -160 -995 C ATOM 1900 O ALA A1035 -0.822 -47.954 27.484 1.00 52.85 O ANISOU 1900 O ALA A1035 4960 5647 9473 569 -196 -1018 O ATOM 1901 CB ALA A1035 2.068 -49.009 28.799 1.00 47.62 C ANISOU 1901 CB ALA A1035 4159 5164 8770 650 -131 -1127 C ATOM 1902 N ALA A1036 0.775 -48.485 25.988 1.00 51.81 N ANISOU 1902 N ALA A1036 4955 5403 9328 613 -98 -941 N ATOM 1903 CA ALA A1036 0.250 -47.585 24.965 1.00 49.33 C ANISOU 1903 CA ALA A1036 4689 4962 9091 585 -69 -905 C ATOM 1904 C ALA A1036 -1.148 -47.996 24.506 1.00 57.58 C ANISOU 1904 C ALA A1036 5849 5965 10064 563 -134 -819 C ATOM 1905 O ALA A1036 -2.007 -47.138 24.264 1.00 58.48 O ANISOU 1905 O ALA A1036 5950 6027 10243 529 -143 -819 O ATOM 1906 CB ALA A1036 1.204 -47.545 23.771 1.00 48.92 C ANISOU 1906 CB ALA A1036 4717 4804 9066 606 9 -857 C ATOM 1907 N ALA A1037 -1.389 -49.300 24.340 1.00 56.75 N ANISOU 1907 N ALA A1037 5860 5878 9825 581 -177 -740 N ATOM 1908 CA ALA A1037 -2.712 -49.722 23.892 1.00 56.42 C ANISOU 1908 CA ALA A1037 5929 5797 9712 558 -240 -655 C ATOM 1909 C ALA A1037 -3.774 -49.366 24.926 1.00 55.42 C ANISOU 1909 C ALA A1037 5709 5751 9597 529 -306 -706 C ATOM 1910 O ALA A1037 -4.830 -48.830 24.578 1.00 56.11 O ANISOU 1910 O ALA A1037 5819 5785 9714 496 -332 -678 O ATOM 1911 CB ALA A1037 -2.717 -51.217 23.590 1.00 54.05 C ANISOU 1911 CB ALA A1037 5767 5507 9262 584 -273 -566 C ATOM 1912 N LEU A1038 -3.497 -49.637 26.207 1.00 59.31 N ANISOU 1912 N LEU A1038 6094 6373 10069 541 -332 -782 N ATOM 1913 CA LEU A1038 -4.376 -49.198 27.289 1.00 63.55 C ANISOU 1913 CA LEU A1038 6524 6993 10629 515 -387 -844 C ATOM 1914 C LEU A1038 -4.514 -47.685 27.312 1.00 63.65 C ANISOU 1914 C LEU A1038 6432 6965 10787 487 -350 -913 C ATOM 1915 O LEU A1038 -5.603 -47.154 27.543 1.00 59.04 O ANISOU 1915 O LEU A1038 5820 6381 10233 456 -389 -920 O ATOM 1916 CB LEU A1038 -3.834 -49.686 28.630 1.00 63.66 C ANISOU 1916 CB LEU A1038 6435 7149 10605 537 -409 -921 C ATOM 1917 CG LEU A1038 -4.023 -51.164 28.930 1.00 64.16 C ANISOU 1917 CG LEU A1038 6581 7279 10519 559 -465 -864 C ATOM 1918 CD1 LEU A1038 -3.639 -51.431 30.364 1.00 64.01 C ANISOU 1918 CD1 LEU A1038 6438 7403 10478 575 -491 -952 C ATOM 1919 CD2 LEU A1038 -5.472 -51.537 28.678 1.00 67.28 C ANISOU 1919 CD2 LEU A1038 7065 7651 10847 532 -535 -789 C ATOM 1920 N ASP A1039 -3.406 -46.979 27.109 1.00 70.07 N ANISOU 1920 N ASP A1039 7183 7746 11693 497 -275 -966 N ATOM 1921 CA ASP A1039 -3.450 -45.528 27.015 1.00 72.48 C ANISOU 1921 CA ASP A1039 7399 8000 12140 471 -232 -1028 C ATOM 1922 C ASP A1039 -4.391 -45.092 25.902 1.00 73.30 C ANISOU 1922 C ASP A1039 7600 7982 12268 445 -233 -949 C ATOM 1923 O ASP A1039 -5.294 -44.279 26.118 1.00 80.34 O ANISOU 1923 O ASP A1039 8442 8865 13221 415 -254 -973 O ATOM 1924 CB ASP A1039 -2.037 -44.998 26.782 1.00 78.33 C ANISOU 1924 CB ASP A1039 8084 8713 12964 489 -147 -1080 C ATOM 1925 CG ASP A1039 -1.895 -43.543 27.136 1.00 85.99 C ANISOU 1925 CG ASP A1039 8920 9674 14079 465 -107 -1176 C ATOM 1926 OD1 ASP A1039 -2.205 -43.187 28.293 1.00 88.46 O ANISOU 1926 OD1 ASP A1039 9114 10080 14416 452 -139 -1258 O ATOM 1927 OD2 ASP A1039 -1.462 -42.759 26.261 1.00 89.51 O ANISOU 1927 OD2 ASP A1039 9380 10018 14613 459 -41 -1169 O ATOM 1928 N ALA A1040 -4.209 -45.644 24.701 1.00 71.78 N ANISOU 1928 N ALA A1040 7551 7696 12026 458 -212 -852 N ATOM 1929 CA ALA A1040 -5.095 -45.322 23.589 1.00 69.40 C ANISOU 1929 CA ALA A1040 7354 7277 11737 434 -217 -769 C ATOM 1930 C ALA A1040 -6.530 -45.788 23.832 1.00 70.10 C ANISOU 1930 C ALA A1040 7489 7395 11750 412 -303 -719 C ATOM 1931 O ALA A1040 -7.462 -45.226 23.243 1.00 70.66 O ANISOU 1931 O ALA A1040 7599 7392 11857 384 -316 -677 O ATOM 1932 CB ALA A1040 -4.553 -45.934 22.290 1.00 63.32 C ANISOU 1932 CB ALA A1040 6734 6407 10918 454 -179 -675 C ATOM 1933 N GLN A1041 -6.732 -46.796 24.685 1.00 68.56 N ANISOU 1933 N GLN A1041 7291 7306 11451 424 -363 -720 N ATOM 1934 CA GLN A1041 -8.073 -47.308 24.954 1.00 71.06 C ANISOU 1934 CA GLN A1041 7652 7657 11691 403 -447 -671 C ATOM 1935 C GLN A1041 -8.916 -46.330 25.754 1.00 77.84 C ANISOU 1935 C GLN A1041 8390 8558 12629 374 -473 -739 C ATOM 1936 O GLN A1041 -10.096 -46.608 26.000 1.00 78.97 O ANISOU 1936 O GLN A1041 8556 8727 12721 354 -540 -703 O ATOM 1937 CB GLN A1041 -7.997 -48.650 25.693 1.00 66.72 C ANISOU 1937 CB GLN A1041 7127 7213 11011 425 -500 -659 C ATOM 1938 CG GLN A1041 -9.278 -49.471 25.632 1.00 65.91 C ANISOU 1938 CG GLN A1041 7120 7122 10802 408 -582 -576 C ATOM 1939 CD GLN A1041 -9.118 -50.883 26.169 1.00 72.42 C ANISOU 1939 CD GLN A1041 7992 8033 11490 432 -628 -550 C ATOM 1940 OE1 GLN A1041 -8.275 -51.149 27.031 1.00 72.86 O ANISOU 1940 OE1 GLN A1041 7967 8179 11537 458 -615 -619 O ATOM 1941 NE2 GLN A1041 -9.935 -51.802 25.657 1.00 76.85 N ANISOU 1941 NE2 GLN A1041 8687 8568 11945 424 -682 -450 N ATOM 1942 N LYS A1042 -8.343 -45.208 26.167 1.00 78.54 N ANISOU 1942 N LYS A1042 8349 8653 12838 370 -421 -836 N ATOM 1943 CA LYS A1042 -9.094 -44.183 26.866 1.00 78.35 C ANISOU 1943 CA LYS A1042 8210 8659 12899 342 -437 -903 C ATOM 1944 C LYS A1042 -9.397 -43.024 25.918 1.00 80.28 C ANISOU 1944 C LYS A1042 8469 8782 13252 320 -393 -885 C ATOM 1945 O LYS A1042 -10.559 -42.709 25.649 1.00 80.79 O ANISOU 1945 O LYS A1042 8563 8808 13325 294 -429 -842 O ATOM 1946 CB LYS A1042 -8.310 -43.694 28.077 1.00 80.41 C ANISOU 1946 CB LYS A1042 8312 9019 13222 351 -414 -1029 C ATOM 1947 CG LYS A1042 -7.929 -44.782 29.072 1.00 81.14 C ANISOU 1947 CG LYS A1042 8380 9238 13214 376 -454 -1054 C ATOM 1948 CD LYS A1042 -6.893 -44.245 30.052 1.00 83.96 C ANISOU 1948 CD LYS A1042 8588 9673 13640 387 -415 -1176 C ATOM 1949 CE LYS A1042 -6.720 -45.139 31.261 1.00 84.58 C ANISOU 1949 CE LYS A1042 8615 9891 13631 406 -463 -1216 C ATOM 1950 NZ LYS A1042 -5.889 -44.452 32.295 1.00 85.29 N ANISOU 1950 NZ LYS A1042 8547 10059 13800 410 -431 -1341 N ATOM 1951 N PRO A1056 -22.295 -48.717 17.956 1.00 84.11 N ANISOU 1951 N PRO A1056 10315 8721 12923 66 -1057 342 N ATOM 1952 CA PRO A1056 -22.062 -49.542 16.765 1.00 84.45 C ANISOU 1952 CA PRO A1056 10530 8678 12879 67 -1057 441 C ATOM 1953 C PRO A1056 -20.602 -49.492 16.293 1.00 84.51 C ANISOU 1953 C PRO A1056 10562 8635 12912 101 -972 412 C ATOM 1954 O PRO A1056 -19.946 -50.541 16.205 1.00 76.56 O ANISOU 1954 O PRO A1056 9635 7644 11811 121 -971 435 O ATOM 1955 CB PRO A1056 -23.018 -48.930 15.742 1.00 83.50 C ANISOU 1955 CB PRO A1056 10473 8456 12796 35 -1072 519 C ATOM 1956 CG PRO A1056 -24.175 -48.487 16.581 1.00 82.79 C ANISOU 1956 CG PRO A1056 10281 8436 12740 11 -1128 496 C ATOM 1957 CD PRO A1056 -23.555 -47.959 17.856 1.00 84.25 C ANISOU 1957 CD PRO A1056 10299 8716 12995 33 -1094 369 C ATOM 1958 N GLU A1057 -20.102 -48.289 15.989 1.00 88.18 N ANISOU 1958 N GLU A1057 10960 9040 13504 106 -902 362 N ATOM 1959 CA GLU A1057 -18.662 -48.124 15.813 1.00 91.91 C ANISOU 1959 CA GLU A1057 11418 9488 14017 140 -819 311 C ATOM 1960 C GLU A1057 -17.926 -48.225 17.145 1.00 95.29 C ANISOU 1960 C GLU A1057 11714 10035 14457 164 -806 204 C ATOM 1961 O GLU A1057 -16.754 -48.617 17.172 1.00 97.73 O ANISOU 1961 O GLU A1057 12032 10354 14748 195 -759 175 O ATOM 1962 CB GLU A1057 -18.347 -46.784 15.146 1.00 95.63 C ANISOU 1962 CB GLU A1057 11849 9862 14622 137 -747 286 C ATOM 1963 CG GLU A1057 -18.456 -46.757 13.630 1.00 96.47 C ANISOU 1963 CG GLU A1057 12103 9833 14718 128 -728 385 C ATOM 1964 CD GLU A1057 -17.922 -45.455 13.037 1.00 98.57 C ANISOU 1964 CD GLU A1057 12323 10010 15120 131 -646 349 C ATOM 1965 OE1 GLU A1057 -17.152 -44.746 13.724 1.00 97.67 O ANISOU 1965 OE1 GLU A1057 12079 9935 15096 148 -593 247 O ATOM 1966 OE2 GLU A1057 -18.269 -45.137 11.880 1.00 99.75 O ANISOU 1966 OE2 GLU A1057 12567 10048 15285 117 -635 423 O ATOM 1967 N MET A1058 -18.590 -47.875 18.255 1.00 97.02 N ANISOU 1967 N MET A1058 11812 10347 14706 152 -846 144 N ATOM 1968 CA MET A1058 -17.974 -48.004 19.575 1.00101.83 C ANISOU 1968 CA MET A1058 12295 11075 15319 173 -840 43 C ATOM 1969 C MET A1058 -17.830 -49.461 19.999 1.00100.46 C ANISOU 1969 C MET A1058 12186 10977 15005 188 -888 73 C ATOM 1970 O MET A1058 -16.891 -49.808 20.727 1.00 98.64 O ANISOU 1970 O MET A1058 11899 10821 14761 217 -864 8 O ATOM 1971 CB MET A1058 -18.791 -47.242 20.619 1.00108.10 C ANISOU 1971 CB MET A1058 12949 11944 16180 155 -872 -24 C ATOM 1972 CG MET A1058 -18.373 -45.797 20.794 1.00114.33 C ANISOU 1972 CG MET A1058 13612 12709 17120 155 -806 -112 C ATOM 1973 SD MET A1058 -16.652 -45.667 21.317 1.00118.95 S ANISOU 1973 SD MET A1058 14112 13334 17749 193 -727 -216 S ATOM 1974 CE MET A1058 -16.679 -46.648 22.817 1.00118.73 C ANISOU 1974 CE MET A1058 14015 13467 17629 206 -787 -268 C ATOM 1975 N LYS A1059 -18.757 -50.319 19.576 1.00 99.12 N ANISOU 1975 N LYS A1059 12134 10794 14732 169 -955 171 N ATOM 1976 CA LYS A1059 -18.629 -51.737 19.879 1.00 94.54 C ANISOU 1976 CA LYS A1059 11630 10277 14015 182 -998 207 C ATOM 1977 C LYS A1059 -17.448 -52.350 19.132 1.00 88.37 C ANISOU 1977 C LYS A1059 10948 9439 13188 213 -945 236 C ATOM 1978 O LYS A1059 -16.680 -53.125 19.711 1.00 86.38 O ANISOU 1978 O LYS A1059 10687 9256 12875 242 -939 205 O ATOM 1979 CB LYS A1059 -19.936 -52.462 19.543 1.00 95.27 C ANISOU 1979 CB LYS A1059 11828 10360 14011 151 -1082 307 C ATOM 1980 CG LYS A1059 -21.184 -51.790 20.124 1.00 98.17 C ANISOU 1980 CG LYS A1059 12106 10767 14429 119 -1133 291 C ATOM 1981 CD LYS A1059 -22.482 -52.472 19.656 1.00 98.25 C ANISOU 1981 CD LYS A1059 12228 10757 14348 85 -1214 399 C ATOM 1982 CE LYS A1059 -23.698 -51.567 19.824 1.00 94.63 C ANISOU 1982 CE LYS A1059 11697 10296 13961 52 -1248 399 C ATOM 1983 NZ LYS A1059 -23.866 -51.137 21.237 1.00 96.68 N ANISOU 1983 NZ LYS A1059 11793 10671 14269 57 -1261 300 N ATOM 1984 N ASP A1060 -17.276 -51.998 17.850 1.00 85.94 N ANISOU 1984 N ASP A1060 10736 9007 12911 208 -904 294 N ATOM 1985 CA ASP A1060 -16.186 -52.567 17.057 1.00 85.69 C ANISOU 1985 CA ASP A1060 10807 8914 12836 237 -851 328 C ATOM 1986 C ASP A1060 -14.821 -52.058 17.511 1.00 81.60 C ANISOU 1986 C ASP A1060 10183 8423 12398 271 -773 230 C ATOM 1987 O ASP A1060 -13.842 -52.810 17.476 1.00 80.43 O ANISOU 1987 O ASP A1060 10080 8289 12193 304 -743 231 O ATOM 1988 CB ASP A1060 -16.384 -52.266 15.569 1.00 88.36 C ANISOU 1988 CB ASP A1060 11273 9110 13191 222 -827 415 C ATOM 1989 CG ASP A1060 -17.560 -53.015 14.966 1.00 90.59 C ANISOU 1989 CG ASP A1060 11691 9359 13371 191 -903 525 C ATOM 1990 OD1 ASP A1060 -18.241 -53.757 15.706 1.00 91.10 O ANISOU 1990 OD1 ASP A1060 11751 9510 13355 180 -974 535 O ATOM 1991 OD2 ASP A1060 -17.804 -52.859 13.748 1.00 91.46 O ANISOU 1991 OD2 ASP A1060 11914 9355 13482 176 -891 603 O ATOM 1992 N PHE A1061 -14.730 -50.797 17.934 1.00 78.46 N ANISOU 1992 N PHE A1061 9646 8033 12130 265 -737 147 N ATOM 1993 CA PHE A1061 -13.449 -50.274 18.396 1.00 78.16 C ANISOU 1993 CA PHE A1061 9501 8024 12171 295 -664 51 C ATOM 1994 C PHE A1061 -13.109 -50.759 19.795 1.00 72.81 C ANISOU 1994 C PHE A1061 8719 7486 11459 313 -688 -27 C ATOM 1995 O PHE A1061 -11.927 -50.951 20.102 1.00 68.66 O ANISOU 1995 O PHE A1061 8155 6995 10939 346 -640 -77 O ATOM 1996 CB PHE A1061 -13.446 -48.744 18.339 1.00 81.88 C ANISOU 1996 CB PHE A1061 9864 8451 12795 281 -615 -11 C ATOM 1997 CG PHE A1061 -13.339 -48.198 16.941 1.00 84.48 C ANISOU 1997 CG PHE A1061 10286 8639 13174 274 -566 50 C ATOM 1998 CD1 PHE A1061 -12.608 -48.880 15.977 1.00 83.90 C ANISOU 1998 CD1 PHE A1061 10343 8494 13040 295 -531 114 C ATOM 1999 CD2 PHE A1061 -13.982 -47.019 16.582 1.00 86.28 C ANISOU 1999 CD2 PHE A1061 10473 8803 13505 247 -555 45 C ATOM 2000 CE1 PHE A1061 -12.511 -48.396 14.689 1.00 86.12 C ANISOU 2000 CE1 PHE A1061 10713 8645 13364 289 -486 171 C ATOM 2001 CE2 PHE A1061 -13.892 -46.529 15.290 1.00 84.45 C ANISOU 2001 CE2 PHE A1061 10329 8441 13316 241 -510 102 C ATOM 2002 CZ PHE A1061 -13.152 -47.217 14.344 1.00 84.03 C ANISOU 2002 CZ PHE A1061 10406 8319 13202 262 -476 165 C ATOM 2003 N ARG A1062 -14.117 -50.951 20.651 1.00 69.24 N ANISOU 2003 N ARG A1062 8219 7117 10973 294 -761 -37 N ATOM 2004 CA ARG A1062 -13.873 -51.610 21.928 1.00 67.60 C ANISOU 2004 CA ARG A1062 7933 7042 10709 311 -792 -96 C ATOM 2005 C ARG A1062 -13.485 -53.065 21.709 1.00 59.31 C ANISOU 2005 C ARG A1062 7006 6008 9520 335 -812 -32 C ATOM 2006 O ARG A1062 -12.567 -53.573 22.365 1.00 60.46 O ANISOU 2006 O ARG A1062 7110 6227 9635 366 -794 -81 O ATOM 2007 CB ARG A1062 -15.100 -51.497 22.833 1.00 78.25 C ANISOU 2007 CB ARG A1062 9210 8470 12050 284 -865 -115 C ATOM 2008 CG ARG A1062 -15.098 -52.438 24.039 1.00 88.09 C ANISOU 2008 CG ARG A1062 10414 9850 13207 299 -915 -148 C ATOM 2009 CD ARG A1062 -15.818 -51.820 25.244 1.00 97.15 C ANISOU 2009 CD ARG A1062 11416 11090 14406 281 -952 -225 C ATOM 2010 NE ARG A1062 -15.138 -50.615 25.725 1.00104.17 N ANISOU 2010 NE ARG A1062 12160 11992 15426 288 -892 -332 N ATOM 2011 CZ ARG A1062 -14.034 -50.621 26.474 1.00106.22 C ANISOU 2011 CZ ARG A1062 12331 12321 15706 317 -854 -417 C ATOM 2012 NH1 ARG A1062 -13.478 -51.772 26.832 1.00106.59 N ANISOU 2012 NH1 ARG A1062 12417 12432 15650 344 -870 -407 N ATOM 2013 NH2 ARG A1062 -13.481 -49.476 26.861 1.00105.82 N ANISOU 2013 NH2 ARG A1062 12153 12277 15779 319 -801 -512 N ATOM 2014 N HIS A1063 -14.149 -53.741 20.765 1.00 47.39 N ANISOU 2014 N HIS A1063 5651 4428 7927 319 -848 78 N ATOM 2015 CA HIS A1063 -13.734 -55.095 20.414 1.00 49.35 C ANISOU 2015 CA HIS A1063 6030 4675 8046 341 -859 145 C ATOM 2016 C HIS A1063 -12.319 -55.102 19.847 1.00 49.80 C ANISOU 2016 C HIS A1063 6116 4681 8126 378 -776 133 C ATOM 2017 O HIS A1063 -11.539 -56.020 20.131 1.00 48.49 O ANISOU 2017 O HIS A1063 5978 4561 7885 410 -767 130 O ATOM 2018 CB HIS A1063 -14.714 -55.724 19.418 1.00 46.82 C ANISOU 2018 CB HIS A1063 5873 4277 7638 314 -909 266 C ATOM 2019 CG HIS A1063 -14.466 -57.184 19.160 1.00 46.73 C ANISOU 2019 CG HIS A1063 5999 4273 7484 333 -933 336 C ATOM 2020 ND1 HIS A1063 -14.283 -58.105 20.175 1.00 46.91 N ANISOU 2020 ND1 HIS A1063 5992 4409 7424 352 -967 308 N ATOM 2021 CD2 HIS A1063 -14.383 -57.883 18.001 1.00 46.75 C ANISOU 2021 CD2 HIS A1063 6171 4183 7409 334 -927 434 C ATOM 2022 CE1 HIS A1063 -14.103 -59.308 19.651 1.00 46.88 C ANISOU 2022 CE1 HIS A1063 6133 4381 7299 365 -981 386 C ATOM 2023 NE2 HIS A1063 -14.154 -59.201 18.334 1.00 46.99 N ANISOU 2023 NE2 HIS A1063 6270 4270 7313 355 -956 462 N ATOM 2024 N GLY A1064 -11.977 -54.090 19.039 1.00 43.83 N ANISOU 2024 N GLY A1064 5353 3826 7474 373 -713 127 N ATOM 2025 CA GLY A1064 -10.647 -54.021 18.454 1.00 42.48 C ANISOU 2025 CA GLY A1064 5208 3601 7333 406 -631 117 C ATOM 2026 C GLY A1064 -9.565 -53.929 19.508 1.00 40.58 C ANISOU 2026 C GLY A1064 4833 3457 7129 439 -594 14 C ATOM 2027 O GLY A1064 -8.586 -54.677 19.480 1.00 43.53 O ANISOU 2027 O GLY A1064 5245 3847 7447 474 -564 18 O ATOM 2028 N PHE A1065 -9.750 -53.045 20.481 1.00 40.31 N ANISOU 2028 N PHE A1065 4640 3492 7183 427 -599 -80 N ATOM 2029 CA PHE A1065 -8.722 -52.863 21.501 1.00 47.37 C ANISOU 2029 CA PHE A1065 5398 4479 8120 454 -564 -183 C ATOM 2030 C PHE A1065 -8.663 -54.057 22.452 1.00 49.49 C ANISOU 2030 C PHE A1065 5664 4865 8274 474 -615 -190 C ATOM 2031 O PHE A1065 -7.576 -54.442 22.900 1.00 48.12 O ANISOU 2031 O PHE A1065 5451 4747 8086 510 -581 -233 O ATOM 2032 CB PHE A1065 -8.969 -51.552 22.256 1.00 47.45 C ANISOU 2032 CB PHE A1065 5243 4527 8258 433 -556 -281 C ATOM 2033 CG PHE A1065 -8.338 -50.346 21.594 1.00 46.31 C ANISOU 2033 CG PHE A1065 5058 4293 8245 431 -475 -314 C ATOM 2034 CD1 PHE A1065 -6.966 -50.174 21.615 1.00 41.69 C ANISOU 2034 CD1 PHE A1065 4426 3709 7705 462 -403 -366 C ATOM 2035 CD2 PHE A1065 -9.122 -49.397 20.942 1.00 52.22 C ANISOU 2035 CD2 PHE A1065 5817 4954 9070 399 -472 -291 C ATOM 2036 CE1 PHE A1065 -6.395 -49.087 21.004 1.00 48.11 C ANISOU 2036 CE1 PHE A1065 5203 4439 8637 459 -330 -394 C ATOM 2037 CE2 PHE A1065 -8.551 -48.298 20.329 1.00 48.91 C ANISOU 2037 CE2 PHE A1065 5363 4451 8769 397 -398 -319 C ATOM 2038 CZ PHE A1065 -7.190 -48.149 20.352 1.00 48.48 C ANISOU 2038 CZ PHE A1065 5264 4399 8759 427 -327 -371 C ATOM 2039 N ASP A1066 -9.821 -54.662 22.751 1.00 47.32 N ANISOU 2039 N ASP A1066 5433 4629 7917 453 -696 -145 N ATOM 2040 CA ASP A1066 -9.868 -55.913 23.513 1.00 44.41 C ANISOU 2040 CA ASP A1066 5089 4361 7426 470 -748 -134 C ATOM 2041 C ASP A1066 -9.022 -56.997 22.865 1.00 43.64 C ANISOU 2041 C ASP A1066 5119 4229 7234 505 -721 -72 C ATOM 2042 O ASP A1066 -8.240 -57.676 23.545 1.00 48.25 O ANISOU 2042 O ASP A1066 5670 4893 7768 538 -714 -106 O ATOM 2043 CB ASP A1066 -11.309 -56.410 23.641 1.00 49.07 C ANISOU 2043 CB ASP A1066 5736 4970 7939 437 -836 -74 C ATOM 2044 CG ASP A1066 -12.104 -55.658 24.678 1.00 60.02 C ANISOU 2044 CG ASP A1066 6982 6434 9388 412 -875 -146 C ATOM 2045 OD1 ASP A1066 -11.515 -54.886 25.470 1.00 65.86 O ANISOU 2045 OD1 ASP A1066 7576 7230 10217 422 -841 -248 O ATOM 2046 OD2 ASP A1066 -13.340 -55.836 24.689 1.00 67.73 O ANISOU 2046 OD2 ASP A1066 7997 7414 10325 381 -941 -98 O ATOM 2047 N ILE A1067 -9.183 -57.201 21.555 1.00 35.90 N ANISOU 2047 N ILE A1067 4285 3129 6225 497 -707 22 N ATOM 2048 CA ILE A1067 -8.338 -58.167 20.863 1.00 36.61 C ANISOU 2048 CA ILE A1067 4501 3178 6233 531 -673 82 C ATOM 2049 C ILE A1067 -6.869 -57.773 21.002 1.00 39.43 C ANISOU 2049 C ILE A1067 4777 3543 6659 569 -590 12 C ATOM 2050 O ILE A1067 -6.013 -58.600 21.345 1.00 40.95 O ANISOU 2050 O ILE A1067 4981 3790 6789 607 -575 4 O ATOM 2051 CB ILE A1067 -8.739 -58.301 19.385 1.00 39.35 C ANISOU 2051 CB ILE A1067 5014 3387 6550 515 -666 189 C ATOM 2052 CG1 ILE A1067 -10.200 -58.744 19.237 1.00 48.60 C ANISOU 2052 CG1 ILE A1067 6269 4551 7646 475 -751 262 C ATOM 2053 CG2 ILE A1067 -7.784 -59.285 18.654 1.00 38.03 C ANISOU 2053 CG2 ILE A1067 4978 3173 6299 553 -624 249 C ATOM 2054 CD1 ILE A1067 -10.751 -58.609 17.788 1.00 49.62 C ANISOU 2054 CD1 ILE A1067 6544 4541 7769 450 -747 361 C ATOM 2055 N LEU A1068 -6.566 -56.498 20.760 1.00 38.95 N ANISOU 2055 N LEU A1068 4633 3434 6733 559 -536 -39 N ATOM 2056 CA LEU A1068 -5.180 -56.048 20.719 1.00 36.65 C ANISOU 2056 CA LEU A1068 4275 3134 6515 592 -453 -97 C ATOM 2057 C LEU A1068 -4.496 -56.274 22.058 1.00 37.12 C ANISOU 2057 C LEU A1068 4203 3328 6572 618 -456 -188 C ATOM 2058 O LEU A1068 -3.380 -56.804 22.115 1.00 38.50 O ANISOU 2058 O LEU A1068 4383 3526 6719 658 -414 -198 O ATOM 2059 CB LEU A1068 -5.121 -54.565 20.331 1.00 36.12 C ANISOU 2059 CB LEU A1068 4130 2998 6597 570 -402 -142 C ATOM 2060 CG LEU A1068 -3.686 -54.168 20.004 1.00 35.60 C ANISOU 2060 CG LEU A1068 4028 2898 6602 602 -310 -181 C ATOM 2061 CD1 LEU A1068 -3.407 -54.654 18.601 1.00 36.69 C ANISOU 2061 CD1 LEU A1068 4335 2915 6691 615 -274 -80 C ATOM 2062 CD2 LEU A1068 -3.468 -52.650 20.107 1.00 35.93 C ANISOU 2062 CD2 LEU A1068 3937 2914 6800 584 -262 -262 C ATOM 2063 N VAL A1069 -5.156 -55.886 23.154 1.00 38.02 N ANISOU 2063 N VAL A1069 4197 3535 6714 597 -505 -254 N ATOM 2064 CA VAL A1069 -4.572 -56.111 24.474 1.00 40.44 C ANISOU 2064 CA VAL A1069 4378 3974 7013 620 -514 -341 C ATOM 2065 C VAL A1069 -4.449 -57.600 24.748 1.00 36.48 C ANISOU 2065 C VAL A1069 3961 3532 6366 648 -551 -292 C ATOM 2066 O VAL A1069 -3.420 -58.072 25.247 1.00 39.51 O ANISOU 2066 O VAL A1069 4305 3980 6726 686 -524 -328 O ATOM 2067 CB VAL A1069 -5.395 -55.396 25.567 1.00 41.83 C ANISOU 2067 CB VAL A1069 4416 4232 7244 589 -561 -418 C ATOM 2068 CG1 VAL A1069 -4.733 -55.567 26.938 1.00 36.42 C ANISOU 2068 CG1 VAL A1069 3596 3684 6558 613 -567 -513 C ATOM 2069 CG2 VAL A1069 -5.502 -53.928 25.241 1.00 47.37 C ANISOU 2069 CG2 VAL A1069 5042 4868 8090 562 -520 -463 C ATOM 2070 N GLY A1070 -5.492 -58.366 24.413 1.00 36.75 N ANISOU 2070 N GLY A1070 4115 3546 6301 630 -614 -207 N ATOM 2071 CA GLY A1070 -5.419 -59.804 24.576 1.00 35.83 C ANISOU 2071 CA GLY A1070 4095 3476 6043 655 -649 -152 C ATOM 2072 C GLY A1070 -4.239 -60.419 23.839 1.00 40.64 C ANISOU 2072 C GLY A1070 4794 4033 6614 697 -587 -112 C ATOM 2073 O GLY A1070 -3.535 -61.278 24.371 1.00 42.49 O ANISOU 2073 O GLY A1070 5025 4340 6779 734 -584 -123 O ATOM 2074 N GLN A1071 -4.021 -60.003 22.592 1.00 39.21 N ANISOU 2074 N GLN A1071 4696 3725 6475 692 -535 -62 N ATOM 2075 CA GLN A1071 -2.935 -60.574 21.797 1.00 34.63 C ANISOU 2075 CA GLN A1071 4212 3086 5858 732 -473 -16 C ATOM 2076 C GLN A1071 -1.570 -60.156 22.325 1.00 37.66 C ANISOU 2076 C GLN A1071 4471 3522 6318 768 -406 -103 C ATOM 2077 O GLN A1071 -0.627 -60.954 22.314 1.00 36.31 O ANISOU 2077 O GLN A1071 4338 3371 6087 811 -375 -88 O ATOM 2078 CB GLN A1071 -3.093 -60.142 20.341 1.00 39.25 C ANISOU 2078 CB GLN A1071 4913 3522 6478 716 -435 56 C ATOM 2079 CG GLN A1071 -4.260 -60.824 19.622 1.00 40.06 C ANISOU 2079 CG GLN A1071 5176 3564 6482 688 -495 161 C ATOM 2080 CD GLN A1071 -4.508 -60.241 18.260 1.00 43.05 C ANISOU 2080 CD GLN A1071 5651 3799 6906 666 -462 223 C ATOM 2081 OE1 GLN A1071 -4.512 -59.010 18.097 1.00 39.57 O ANISOU 2081 OE1 GLN A1071 5127 3319 6589 648 -429 178 O ATOM 2082 NE2 GLN A1071 -4.722 -61.109 17.267 1.00 34.36 N ANISOU 2082 NE2 GLN A1071 4730 2619 5707 669 -470 328 N ATOM 2083 N ILE A1072 -1.430 -58.901 22.774 1.00 37.94 N ANISOU 2083 N ILE A1072 4357 3575 6483 751 -382 -192 N ATOM 2084 CA ILE A1072 -0.203 -58.508 23.458 1.00 36.79 C ANISOU 2084 CA ILE A1072 4077 3496 6407 781 -328 -283 C ATOM 2085 C ILE A1072 0.020 -59.401 24.676 1.00 37.90 C ANISOU 2085 C ILE A1072 4161 3774 6465 807 -370 -320 C ATOM 2086 O ILE A1072 1.116 -59.931 24.881 1.00 40.61 O ANISOU 2086 O ILE A1072 4492 4157 6781 850 -333 -334 O ATOM 2087 CB ILE A1072 -0.261 -57.009 23.821 1.00 37.70 C ANISOU 2087 CB ILE A1072 4041 3613 6671 752 -306 -374 C ATOM 2088 CG1 ILE A1072 -0.218 -56.158 22.545 1.00 36.69 C ANISOU 2088 CG1 ILE A1072 3970 3343 6627 735 -249 -337 C ATOM 2089 CG2 ILE A1072 0.878 -56.628 24.767 1.00 39.39 C ANISOU 2089 CG2 ILE A1072 4098 3918 6951 777 -266 -479 C ATOM 2090 CD1 ILE A1072 -0.598 -54.719 22.753 1.00 36.13 C ANISOU 2090 CD1 ILE A1072 3780 3257 6691 699 -239 -408 C ATOM 2091 N ASP A1073 -1.038 -59.636 25.467 1.00 38.85 N ANISOU 2091 N ASP A1073 4254 3967 6539 782 -449 -330 N ATOM 2092 CA ASP A1073 -0.929 -60.506 26.641 1.00 42.64 C ANISOU 2092 CA ASP A1073 4686 4580 6937 805 -494 -362 C ATOM 2093 C ASP A1073 -0.514 -61.932 26.272 1.00 40.71 C ANISOU 2093 C ASP A1073 4578 4332 6559 843 -495 -282 C ATOM 2094 O ASP A1073 0.288 -62.541 26.987 1.00 40.98 O ANISOU 2094 O ASP A1073 4566 4454 6551 882 -488 -315 O ATOM 2095 CB ASP A1073 -2.261 -60.547 27.413 1.00 46.86 C ANISOU 2095 CB ASP A1073 5188 5179 7438 769 -580 -373 C ATOM 2096 CG ASP A1073 -2.545 -59.274 28.213 1.00 50.79 C ANISOU 2096 CG ASP A1073 5516 5724 8056 740 -585 -474 C ATOM 2097 OD1 ASP A1073 -1.644 -58.421 28.416 1.00 51.19 O ANISOU 2097 OD1 ASP A1073 5456 5783 8212 750 -527 -551 O ATOM 2098 OD2 ASP A1073 -3.707 -59.127 28.639 1.00 52.62 O ANISOU 2098 OD2 ASP A1073 5730 5984 8278 706 -647 -476 O ATOM 2099 N ASP A1074 -1.088 -62.513 25.198 1.00 38.02 N ANISOU 2099 N ASP A1074 4407 3894 6145 834 -508 -176 N ATOM 2100 CA ASP A1074 -0.658 -63.855 24.779 1.00 37.98 C ANISOU 2100 CA ASP A1074 4540 3877 6014 871 -504 -98 C ATOM 2101 C ASP A1074 0.831 -63.869 24.479 1.00 36.98 C ANISOU 2101 C ASP A1074 4399 3732 5919 918 -420 -115 C ATOM 2102 O ASP A1074 1.553 -64.824 24.829 1.00 34.98 O ANISOU 2102 O ASP A1074 4167 3537 5588 961 -412 -107 O ATOM 2103 CB ASP A1074 -1.407 -64.336 23.522 1.00 38.58 C ANISOU 2103 CB ASP A1074 4804 3833 6021 851 -520 17 C ATOM 2104 CG ASP A1074 -2.910 -64.428 23.702 1.00 41.12 C ANISOU 2104 CG ASP A1074 5159 4165 6301 805 -605 48 C ATOM 2105 OD1 ASP A1074 -3.381 -64.433 24.855 1.00 46.72 O ANISOU 2105 OD1 ASP A1074 5766 4983 7003 794 -658 -8 O ATOM 2106 OD2 ASP A1074 -3.627 -64.517 22.677 1.00 38.96 O ANISOU 2106 OD2 ASP A1074 5015 3790 5999 779 -619 131 O ATOM 2107 N ALA A1075 1.294 -62.843 23.762 1.00 36.44 N ANISOU 2107 N ALA A1075 4304 3579 5963 910 -355 -132 N ATOM 2108 CA ALA A1075 2.696 -62.813 23.354 1.00 41.92 C ANISOU 2108 CA ALA A1075 4992 4245 6693 953 -271 -141 C ATOM 2109 C ALA A1075 3.614 -62.590 24.552 1.00 41.21 C ANISOU 2109 C ALA A1075 4733 4276 6650 979 -254 -244 C ATOM 2110 O ALA A1075 4.734 -63.114 24.589 1.00 39.30 O ANISOU 2110 O ALA A1075 4492 4058 6383 1026 -208 -245 O ATOM 2111 CB ALA A1075 2.908 -61.727 22.292 1.00 39.91 C ANISOU 2111 CB ALA A1075 4748 3866 6549 935 -207 -134 C ATOM 2112 N LEU A1076 3.150 -61.825 25.535 1.00 38.83 N ANISOU 2112 N LEU A1076 4287 4051 6415 950 -290 -329 N ATOM 2113 CA LEU A1076 3.929 -61.598 26.750 1.00 41.83 C ANISOU 2113 CA LEU A1076 4502 4553 6837 971 -281 -430 C ATOM 2114 C LEU A1076 4.093 -62.877 27.560 1.00 40.56 C ANISOU 2114 C LEU A1076 4359 4500 6553 1006 -323 -420 C ATOM 2115 O LEU A1076 5.181 -63.167 28.065 1.00 44.64 O ANISOU 2115 O LEU A1076 4811 5083 7066 1046 -290 -459 O ATOM 2116 CB LEU A1076 3.252 -60.513 27.593 1.00 49.12 C ANISOU 2116 CB LEU A1076 5280 5530 7853 928 -316 -519 C ATOM 2117 CG LEU A1076 3.804 -59.098 27.480 1.00 52.61 C ANISOU 2117 CG LEU A1076 5604 5937 8449 913 -256 -594 C ATOM 2118 CD1 LEU A1076 2.879 -58.141 28.196 1.00 56.24 C ANISOU 2118 CD1 LEU A1076 5952 6436 8982 867 -300 -663 C ATOM 2119 CD2 LEU A1076 5.215 -59.032 28.076 1.00 49.96 C ANISOU 2119 CD2 LEU A1076 5156 5673 8154 951 -204 -664 C ATOM 2120 N LYS A1077 3.020 -63.650 27.716 1.00 41.93 N ANISOU 2120 N LYS A1077 4615 4692 6624 990 -395 -368 N ATOM 2121 CA LYS A1077 3.148 -64.911 28.429 1.00 42.32 C ANISOU 2121 CA LYS A1077 4693 4837 6551 1023 -434 -351 C ATOM 2122 C LYS A1077 4.162 -65.829 27.743 1.00 45.68 C ANISOU 2122 C LYS A1077 5227 5221 6908 1074 -381 -287 C ATOM 2123 O LYS A1077 4.973 -66.489 28.411 1.00 42.26 O ANISOU 2123 O LYS A1077 4753 4875 6428 1117 -372 -311 O ATOM 2124 CB LYS A1077 1.786 -65.587 28.536 1.00 42.31 C ANISOU 2124 CB LYS A1077 4781 4844 6450 995 -517 -294 C ATOM 2125 CG LYS A1077 1.801 -66.756 29.479 1.00 48.39 C ANISOU 2125 CG LYS A1077 5553 5727 7103 1023 -565 -293 C ATOM 2126 CD LYS A1077 0.538 -67.585 29.398 1.00 59.34 C ANISOU 2126 CD LYS A1077 7058 7109 8379 999 -641 -220 C ATOM 2127 CE LYS A1077 0.876 -69.066 29.107 1.00 67.45 C ANISOU 2127 CE LYS A1077 8227 8135 9265 1040 -644 -138 C ATOM 2128 NZ LYS A1077 1.520 -69.285 27.749 1.00 69.32 N ANISOU 2128 NZ LYS A1077 8597 8248 9493 1061 -578 -62 N ATOM 2129 N LEU A1078 4.122 -65.904 26.406 1.00 42.77 N ANISOU 2129 N LEU A1078 5000 4722 6530 1072 -346 -204 N ATOM 2130 CA LEU A1078 5.064 -66.771 25.702 1.00 40.92 C ANISOU 2130 CA LEU A1078 4875 4442 6230 1121 -293 -139 C ATOM 2131 C LEU A1078 6.487 -66.282 25.894 1.00 41.19 C ANISOU 2131 C LEU A1078 4799 4503 6349 1157 -217 -203 C ATOM 2132 O LEU A1078 7.404 -67.081 26.150 1.00 41.13 O ANISOU 2132 O LEU A1078 4799 4544 6284 1207 -191 -196 O ATOM 2133 CB LEU A1078 4.711 -66.844 24.217 1.00 35.99 C ANISOU 2133 CB LEU A1078 4420 3667 5586 1107 -268 -41 C ATOM 2134 CG LEU A1078 3.479 -67.700 23.942 1.00 41.16 C ANISOU 2134 CG LEU A1078 5218 4298 6124 1083 -340 41 C ATOM 2135 CD1 LEU A1078 2.945 -67.350 22.545 1.00 43.51 C ANISOU 2135 CD1 LEU A1078 5647 4446 6439 1053 -323 118 C ATOM 2136 CD2 LEU A1078 3.808 -69.231 24.081 1.00 35.01 C ANISOU 2136 CD2 LEU A1078 4544 3559 5198 1127 -354 100 C ATOM 2137 N ALA A1079 6.683 -64.967 25.787 1.00 40.04 N ANISOU 2137 N ALA A1079 4548 4325 6340 1132 -180 -265 N ATOM 2138 CA ALA A1079 7.994 -64.372 26.033 1.00 45.18 C ANISOU 2138 CA ALA A1079 5077 5005 7084 1160 -110 -334 C ATOM 2139 C ALA A1079 8.504 -64.710 27.432 1.00 53.33 C ANISOU 2139 C ALA A1079 5978 6189 8096 1186 -135 -410 C ATOM 2140 O ALA A1079 9.660 -65.118 27.605 1.00 58.55 O ANISOU 2140 O ALA A1079 6611 6890 8746 1233 -90 -421 O ATOM 2141 CB ALA A1079 7.913 -62.856 25.839 1.00 42.35 C ANISOU 2141 CB ALA A1079 4617 4597 6875 1120 -80 -396 C ATOM 2142 N ASN A1080 7.653 -64.546 28.450 1.00 51.65 N ANISOU 2142 N ASN A1080 5683 6065 7878 1156 -206 -462 N ATOM 2143 CA ASN A1080 8.086 -64.793 29.818 1.00 49.24 C ANISOU 2143 CA ASN A1080 5246 5906 7558 1177 -232 -539 C ATOM 2144 C ASN A1080 8.390 -66.270 30.077 1.00 49.63 C ANISOU 2144 C ASN A1080 5378 6012 7467 1225 -251 -486 C ATOM 2145 O ASN A1080 9.171 -66.571 30.978 1.00 49.33 O ANISOU 2145 O ASN A1080 5246 6081 7417 1259 -247 -538 O ATOM 2146 CB ASN A1080 7.038 -64.252 30.791 1.00 51.75 C ANISOU 2146 CB ASN A1080 5465 6296 7902 1133 -303 -604 C ATOM 2147 CG ASN A1080 7.081 -62.726 30.904 1.00 53.87 C ANISOU 2147 CG ASN A1080 5600 6547 8323 1096 -276 -689 C ATOM 2148 OD1 ASN A1080 8.140 -62.123 30.763 1.00 64.07 O ANISOU 2148 OD1 ASN A1080 6817 7826 9701 1111 -210 -732 O ATOM 2149 ND2 ASN A1080 5.939 -62.104 31.158 1.00 51.04 N ANISOU 2149 ND2 ASN A1080 5209 6186 7997 1047 -325 -712 N ATOM 2150 N GLU A1081 7.814 -67.189 29.300 1.00 47.35 N ANISOU 2150 N GLU A1081 5265 5655 7073 1229 -271 -383 N ATOM 2151 CA GLU A1081 8.200 -68.598 29.292 1.00 47.27 C ANISOU 2151 CA GLU A1081 5358 5673 6931 1277 -275 -319 C ATOM 2152 C GLU A1081 9.464 -68.867 28.486 1.00 52.56 C ANISOU 2152 C GLU A1081 6083 6283 7607 1325 -190 -280 C ATOM 2153 O GLU A1081 9.821 -70.039 28.301 1.00 50.15 O ANISOU 2153 O GLU A1081 5881 5981 7192 1368 -184 -217 O ATOM 2154 CB GLU A1081 7.062 -69.460 28.731 1.00 45.54 C ANISOU 2154 CB GLU A1081 5309 5396 6596 1259 -328 -222 C ATOM 2155 CG GLU A1081 5.895 -69.583 29.656 1.00 52.21 C ANISOU 2155 CG GLU A1081 6115 6322 7401 1224 -417 -248 C ATOM 2156 CD GLU A1081 4.646 -70.062 28.960 1.00 64.47 C ANISOU 2156 CD GLU A1081 7823 7799 8876 1191 -467 -159 C ATOM 2157 OE1 GLU A1081 4.627 -70.115 27.708 1.00 66.32 O ANISOU 2157 OE1 GLU A1081 8188 7908 9103 1187 -432 -84 O ATOM 2158 OE2 GLU A1081 3.668 -70.379 29.671 1.00 71.86 O ANISOU 2158 OE2 GLU A1081 8747 8798 9756 1166 -542 -165 O ATOM 2159 N GLY A1082 10.124 -67.820 27.984 1.00 55.34 N ANISOU 2159 N GLY A1082 6372 6576 8081 1320 -124 -315 N ATOM 2160 CA GLY A1082 11.331 -67.969 27.195 1.00 55.92 C ANISOU 2160 CA GLY A1082 6489 6587 8170 1363 -39 -281 C ATOM 2161 C GLY A1082 11.149 -68.513 25.795 1.00 56.77 C ANISOU 2161 C GLY A1082 6793 6559 8217 1371 -10 -169 C ATOM 2162 O GLY A1082 12.105 -69.033 25.222 1.00 62.49 O ANISOU 2162 O GLY A1082 7582 7246 8914 1417 52 -125 O ATOM 2163 N LYS A1083 9.954 -68.414 25.214 1.00 46.03 N ANISOU 2163 N LYS A1083 5532 5124 6835 1326 -51 -120 N ATOM 2164 CA LYS A1083 9.690 -69.010 23.910 1.00 42.47 C ANISOU 2164 CA LYS A1083 5276 4546 6313 1330 -32 -10 C ATOM 2165 C LYS A1083 9.698 -67.896 22.866 1.00 45.21 C ANISOU 2165 C LYS A1083 5636 4771 6771 1301 20 -4 C ATOM 2166 O LYS A1083 8.654 -67.408 22.427 1.00 44.05 O ANISOU 2166 O LYS A1083 5532 4559 6644 1252 -14 16 O ATOM 2167 CB LYS A1083 8.373 -69.780 23.936 1.00 40.89 C ANISOU 2167 CB LYS A1083 5190 4345 6001 1303 -115 49 C ATOM 2168 CG LYS A1083 8.211 -70.706 25.134 1.00 44.38 C ANISOU 2168 CG LYS A1083 5594 4920 6348 1322 -176 28 C ATOM 2169 CD LYS A1083 6.849 -71.382 25.110 1.00 50.71 C ANISOU 2169 CD LYS A1083 6508 5714 7047 1288 -258 87 C ATOM 2170 CE LYS A1083 6.679 -72.378 26.251 1.00 49.98 C ANISOU 2170 CE LYS A1083 6390 5748 6852 1309 -317 73 C ATOM 2171 NZ LYS A1083 5.431 -73.172 26.027 1.00 47.21 N ANISOU 2171 NZ LYS A1083 6177 5372 6390 1281 -388 148 N ATOM 2172 N VAL A1084 10.907 -67.500 22.451 1.00 41.23 N ANISOU 2172 N VAL A1084 5094 4232 6338 1333 104 -20 N ATOM 2173 CA VAL A1084 11.046 -66.310 21.609 1.00 44.06 C ANISOU 2173 CA VAL A1084 5434 4488 6819 1307 159 -31 C ATOM 2174 C VAL A1084 10.297 -66.473 20.289 1.00 44.28 C ANISOU 2174 C VAL A1084 5644 4377 6806 1285 159 67 C ATOM 2175 O VAL A1084 9.555 -65.579 19.871 1.00 44.64 O ANISOU 2175 O VAL A1084 5685 4357 6921 1237 148 61 O ATOM 2176 CB VAL A1084 12.525 -66.004 21.356 1.00 50.97 C ANISOU 2176 CB VAL A1084 6251 5351 7765 1350 252 -56 C ATOM 2177 CG1 VAL A1084 12.657 -64.641 20.712 1.00 48.64 C ANISOU 2177 CG1 VAL A1084 5902 4969 7610 1319 304 -87 C ATOM 2178 CG2 VAL A1084 13.295 -66.088 22.649 1.00 57.52 C ANISOU 2178 CG2 VAL A1084 6921 6323 8611 1378 248 -140 C ATOM 2179 N LYS A1085 10.541 -67.581 19.577 1.00 43.83 N ANISOU 2179 N LYS A1085 5747 4266 6639 1320 178 159 N ATOM 2180 CA LYS A1085 9.903 -67.780 18.278 1.00 40.89 C ANISOU 2180 CA LYS A1085 5555 3759 6222 1301 182 255 C ATOM 2181 C LYS A1085 8.387 -67.771 18.401 1.00 36.69 C ANISOU 2181 C LYS A1085 5066 3224 5652 1246 93 274 C ATOM 2182 O LYS A1085 7.690 -67.145 17.596 1.00 42.08 O ANISOU 2182 O LYS A1085 5805 3809 6375 1206 90 304 O ATOM 2183 CB LYS A1085 10.360 -69.099 17.666 1.00 40.25 C ANISOU 2183 CB LYS A1085 5639 3639 6016 1349 207 347 C ATOM 2184 CG LYS A1085 11.802 -69.126 17.204 1.00 44.98 C ANISOU 2184 CG LYS A1085 6235 4207 6649 1404 304 352 C ATOM 2185 CD LYS A1085 11.995 -68.257 15.975 1.00 46.68 C ANISOU 2185 CD LYS A1085 6499 4286 6952 1388 370 379 C ATOM 2186 CE LYS A1085 13.367 -68.551 15.328 1.00 51.00 C ANISOU 2186 CE LYS A1085 7088 4785 7504 1447 467 410 C ATOM 2187 NZ LYS A1085 13.513 -67.705 14.108 1.00 53.90 N ANISOU 2187 NZ LYS A1085 7509 5017 7954 1431 530 439 N ATOM 2188 N GLU A1086 7.862 -68.464 19.408 1.00 37.31 N ANISOU 2188 N GLU A1086 5117 3409 5650 1245 20 258 N ATOM 2189 CA GLU A1086 6.422 -68.501 19.604 1.00 41.39 C ANISOU 2189 CA GLU A1086 5667 3932 6126 1194 -66 275 C ATOM 2190 C GLU A1086 5.902 -67.111 19.934 1.00 42.88 C ANISOU 2190 C GLU A1086 5719 4129 6446 1145 -81 199 C ATOM 2191 O GLU A1086 4.844 -66.705 19.436 1.00 40.09 O ANISOU 2191 O GLU A1086 5419 3710 6104 1098 -117 230 O ATOM 2192 CB GLU A1086 6.076 -69.503 20.709 1.00 43.23 C ANISOU 2192 CB GLU A1086 5883 4287 6254 1206 -136 265 C ATOM 2193 CG GLU A1086 4.906 -70.380 20.372 1.00 54.59 C ANISOU 2193 CG GLU A1086 7475 5694 7572 1181 -205 349 C ATOM 2194 CD GLU A1086 4.933 -71.713 21.104 1.00 60.50 C ANISOU 2194 CD GLU A1086 8264 6535 8189 1212 -247 369 C ATOM 2195 OE1 GLU A1086 5.573 -72.672 20.598 1.00 66.64 O ANISOU 2195 OE1 GLU A1086 9158 7279 8881 1256 -211 432 O ATOM 2196 OE2 GLU A1086 4.312 -71.800 22.184 1.00 56.03 O ANISOU 2196 OE2 GLU A1086 7613 6073 7605 1195 -314 323 O ATOM 2197 N ALA A1087 6.668 -66.358 20.733 1.00 36.24 N ANISOU 2197 N ALA A1087 4703 3363 5704 1156 -50 101 N ATOM 2198 CA ALA A1087 6.291 -64.996 21.097 1.00 41.90 C ANISOU 2198 CA ALA A1087 5279 4089 6551 1113 -57 22 C ATOM 2199 C ALA A1087 6.285 -64.077 19.877 1.00 43.15 C ANISOU 2199 C ALA A1087 5486 4110 6797 1091 -3 50 C ATOM 2200 O ALA A1087 5.346 -63.291 19.689 1.00 36.32 O ANISOU 2200 O ALA A1087 4608 3205 5988 1043 -34 43 O ATOM 2201 CB ALA A1087 7.244 -64.473 22.180 1.00 38.22 C ANISOU 2201 CB ALA A1087 4624 3733 6167 1135 -30 -86 C ATOM 2202 N GLN A1088 7.315 -64.179 19.025 1.00 40.42 N ANISOU 2202 N GLN A1088 5203 3691 6465 1127 77 86 N ATOM 2203 CA GLN A1088 7.356 -63.375 17.800 1.00 40.26 C ANISOU 2203 CA GLN A1088 5241 3535 6521 1110 132 119 C ATOM 2204 C GLN A1088 6.212 -63.728 16.847 1.00 42.67 C ANISOU 2204 C GLN A1088 5717 3740 6755 1078 91 216 C ATOM 2205 O GLN A1088 5.619 -62.837 16.224 1.00 46.29 O ANISOU 2205 O GLN A1088 6186 4117 7285 1038 94 223 O ATOM 2206 CB GLN A1088 8.704 -63.549 17.089 1.00 38.65 C ANISOU 2206 CB GLN A1088 5078 3275 6332 1159 226 144 C ATOM 2207 CG GLN A1088 9.888 -62.984 17.850 1.00 39.35 C ANISOU 2207 CG GLN A1088 4995 3442 6515 1185 277 50 C ATOM 2208 CD GLN A1088 11.209 -63.392 17.228 1.00 40.47 C ANISOU 2208 CD GLN A1088 5187 3543 6649 1240 364 84 C ATOM 2209 OE1 GLN A1088 11.444 -64.568 16.986 1.00 41.24 O ANISOU 2209 OE1 GLN A1088 5401 3637 6631 1277 364 151 O ATOM 2210 NE2 GLN A1088 12.056 -62.419 16.935 1.00 38.50 N ANISOU 2210 NE2 GLN A1088 4852 3254 6520 1244 438 40 N ATOM 2211 N ALA A1089 5.903 -65.016 16.690 1.00 39.70 N ANISOU 2211 N ALA A1089 5478 3367 6238 1094 55 292 N ATOM 2212 CA ALA A1089 4.773 -65.365 15.839 1.00 40.54 C ANISOU 2212 CA ALA A1089 5744 3386 6274 1060 9 381 C ATOM 2213 C ALA A1089 3.465 -64.845 16.428 1.00 39.41 C ANISOU 2213 C ALA A1089 5535 3283 6154 1005 -72 349 C ATOM 2214 O ALA A1089 2.600 -64.363 15.690 1.00 41.09 O ANISOU 2214 O ALA A1089 5814 3410 6390 964 -90 390 O ATOM 2215 CB ALA A1089 4.705 -66.878 15.619 1.00 37.08 C ANISOU 2215 CB ALA A1089 5463 2948 5677 1088 -16 466 C ATOM 2216 N ALA A1090 3.313 -64.906 17.758 1.00 37.69 N ANISOU 2216 N ALA A1090 5188 3198 5936 1004 -120 277 N ATOM 2217 CA ALA A1090 2.093 -64.379 18.379 1.00 40.34 C ANISOU 2217 CA ALA A1090 5452 3577 6298 953 -195 242 C ATOM 2218 C ALA A1090 1.965 -62.886 18.147 1.00 44.11 C ANISOU 2218 C ALA A1090 5831 4005 6923 920 -165 190 C ATOM 2219 O ALA A1090 0.853 -62.373 17.950 1.00 38.71 O ANISOU 2219 O ALA A1090 5160 3286 6263 873 -210 203 O ATOM 2220 CB ALA A1090 2.082 -64.667 19.881 1.00 39.13 C ANISOU 2220 CB ALA A1090 5167 3577 6123 962 -243 167 C ATOM 2221 N ALA A1091 3.100 -62.173 18.180 1.00 35.95 N ANISOU 2221 N ALA A1091 4699 2970 5990 944 -89 129 N ATOM 2222 CA ALA A1091 3.084 -60.732 17.977 1.00 43.71 C ANISOU 2222 CA ALA A1091 5583 3906 7117 914 -54 74 C ATOM 2223 C ALA A1091 2.747 -60.393 16.542 1.00 42.64 C ANISOU 2223 C ALA A1091 5580 3621 7001 895 -24 153 C ATOM 2224 O ALA A1091 2.145 -59.353 16.283 1.00 39.31 O ANISOU 2224 O ALA A1091 5118 3150 6667 856 -28 134 O ATOM 2225 CB ALA A1091 4.429 -60.121 18.362 1.00 36.89 C ANISOU 2225 CB ALA A1091 4586 3079 6351 945 20 -7 C ATOM 2226 N GLU A1092 3.100 -61.266 15.600 1.00 44.40 N ANISOU 2226 N GLU A1092 5963 3770 7137 922 3 242 N ATOM 2227 CA GLU A1092 2.742 -61.001 14.208 1.00 46.90 C ANISOU 2227 CA GLU A1092 6416 3943 7463 903 29 321 C ATOM 2228 C GLU A1092 1.223 -60.957 14.020 1.00 42.75 C ANISOU 2228 C GLU A1092 5953 3389 6902 852 -51 366 C ATOM 2229 O GLU A1092 0.723 -60.235 13.146 1.00 43.88 O ANISOU 2229 O GLU A1092 6143 3431 7100 821 -40 398 O ATOM 2230 CB GLU A1092 3.404 -62.050 13.307 1.00 54.49 C ANISOU 2230 CB GLU A1092 7541 4836 8326 944 70 408 C ATOM 2231 CG GLU A1092 3.802 -61.558 11.913 1.00 63.71 C ANISOU 2231 CG GLU A1092 8804 5860 9543 946 144 461 C ATOM 2232 CD GLU A1092 4.812 -60.414 11.913 1.00 66.80 C ANISOU 2232 CD GLU A1092 9065 6237 10079 959 226 387 C ATOM 2233 OE1 GLU A1092 5.373 -60.064 12.975 1.00 68.67 O ANISOU 2233 OE1 GLU A1092 9141 6578 10375 971 234 295 O ATOM 2234 OE2 GLU A1092 5.046 -59.850 10.827 1.00 69.85 O ANISOU 2234 OE2 GLU A1092 9513 6508 10520 955 284 422 O ATOM 2235 N GLN A1093 0.472 -61.645 14.881 1.00 38.64 N ANISOU 2235 N GLN A1093 5422 2961 6299 841 -132 363 N ATOM 2236 CA GLN A1093 -0.986 -61.624 14.797 1.00 44.91 C ANISOU 2236 CA GLN A1093 6266 3740 7059 792 -212 402 C ATOM 2237 C GLN A1093 -1.558 -60.248 15.069 1.00 50.01 C ANISOU 2237 C GLN A1093 6783 4385 7833 751 -220 338 C ATOM 2238 O GLN A1093 -2.673 -59.952 14.608 1.00 49.63 O ANISOU 2238 O GLN A1093 6789 4282 7785 709 -264 382 O ATOM 2239 CB GLN A1093 -1.598 -62.635 15.774 1.00 44.68 C ANISOU 2239 CB GLN A1093 6237 3821 6920 790 -294 405 C ATOM 2240 CG GLN A1093 -0.989 -64.012 15.673 1.00 55.00 C ANISOU 2240 CG GLN A1093 7653 5144 8099 833 -286 458 C ATOM 2241 CD GLN A1093 -1.092 -64.576 14.286 1.00 58.81 C ANISOU 2241 CD GLN A1093 8336 5500 8511 834 -268 568 C ATOM 2242 OE1 GLN A1093 -2.141 -64.490 13.658 1.00 61.86 O ANISOU 2242 OE1 GLN A1093 8810 5819 8875 794 -310 627 O ATOM 2243 NE2 GLN A1093 0.001 -65.146 13.789 1.00 62.95 N ANISOU 2243 NE2 GLN A1093 8931 5989 8999 881 -203 597 N ATOM 2244 N LEU A1094 -0.809 -59.414 15.806 1.00 45.74 N ANISOU 2244 N LEU A1094 6076 3904 7401 763 -179 238 N ATOM 2245 CA LEU A1094 -1.202 -58.037 16.054 1.00 42.92 C ANISOU 2245 CA LEU A1094 5591 3541 7175 729 -175 170 C ATOM 2246 C LEU A1094 -1.421 -57.270 14.763 1.00 43.87 C ANISOU 2246 C LEU A1094 5789 3520 7360 707 -135 220 C ATOM 2247 O LEU A1094 -2.212 -56.323 14.744 1.00 43.15 O ANISOU 2247 O LEU A1094 5644 3404 7346 668 -155 199 O ATOM 2248 CB LEU A1094 -0.141 -57.329 16.901 1.00 44.51 C ANISOU 2248 CB LEU A1094 5617 3815 7479 750 -123 60 C ATOM 2249 CG LEU A1094 -0.008 -57.786 18.360 1.00 45.65 C ANISOU 2249 CG LEU A1094 5646 4112 7589 765 -165 -12 C ATOM 2250 CD1 LEU A1094 1.264 -57.225 18.971 1.00 43.62 C ANISOU 2250 CD1 LEU A1094 5243 3909 7421 793 -101 -106 C ATOM 2251 CD2 LEU A1094 -1.231 -57.357 19.165 1.00 47.62 C ANISOU 2251 CD2 LEU A1094 5815 4422 7856 722 -241 -49 C ATOM 2252 N LYS A1095 -0.739 -57.649 13.677 1.00 47.82 N ANISOU 2252 N LYS A1095 6414 3926 7831 732 -78 286 N ATOM 2253 CA LYS A1095 -0.924 -56.925 12.420 1.00 52.26 C ANISOU 2253 CA LYS A1095 7053 4351 8452 713 -38 335 C ATOM 2254 C LYS A1095 -2.341 -57.076 11.891 1.00 50.69 C ANISOU 2254 C LYS A1095 6961 4099 8199 670 -108 410 C ATOM 2255 O LYS A1095 -2.873 -56.153 11.261 1.00 53.30 O ANISOU 2255 O LYS A1095 7296 4349 8606 639 -99 423 O ATOM 2256 CB LYS A1095 0.090 -57.393 11.380 1.00 55.01 C ANISOU 2256 CB LYS A1095 7521 4612 8769 751 37 393 C ATOM 2257 CG LYS A1095 1.486 -56.896 11.672 1.00 55.51 C ANISOU 2257 CG LYS A1095 7471 4700 8921 786 120 319 C ATOM 2258 CD LYS A1095 2.491 -57.449 10.708 1.00 58.59 C ANISOU 2258 CD LYS A1095 7979 5011 9272 827 192 378 C ATOM 2259 CE LYS A1095 3.869 -56.887 11.012 1.00 66.02 C ANISOU 2259 CE LYS A1095 8798 5978 10309 861 275 303 C ATOM 2260 NZ LYS A1095 4.928 -57.667 10.307 1.00 72.61 N ANISOU 2260 NZ LYS A1095 9738 6763 11086 909 339 357 N ATOM 2261 N THR A1096 -2.978 -58.214 12.157 1.00 50.12 N ANISOU 2261 N THR A1096 6971 4073 7998 667 -179 461 N ATOM 2262 CA THR A1096 -4.344 -58.408 11.693 1.00 49.17 C ANISOU 2262 CA THR A1096 6952 3909 7822 625 -250 535 C ATOM 2263 C THR A1096 -5.276 -57.447 12.406 1.00 45.77 C ANISOU 2263 C THR A1096 6390 3527 7475 585 -296 475 C ATOM 2264 O THR A1096 -6.114 -56.785 11.783 1.00 46.29 O ANISOU 2264 O THR A1096 6487 3519 7583 548 -312 508 O ATOM 2265 CB THR A1096 -4.767 -59.861 11.926 1.00 52.32 C ANISOU 2265 CB THR A1096 7458 4356 8064 631 -315 595 C ATOM 2266 OG1 THR A1096 -3.884 -60.726 11.205 1.00 55.96 O ANISOU 2266 OG1 THR A1096 8047 4765 8450 670 -267 652 O ATOM 2267 CG2 THR A1096 -6.201 -60.093 11.481 1.00 48.27 C ANISOU 2267 CG2 THR A1096 7047 3803 7490 585 -393 672 C ATOM 2268 N THR A1097 -5.109 -57.331 13.717 1.00 44.51 N ANISOU 2268 N THR A1097 6080 3490 7341 592 -315 386 N ATOM 2269 CA THR A1097 -5.928 -56.413 14.494 1.00 42.71 C ANISOU 2269 CA THR A1097 5717 3316 7194 557 -355 321 C ATOM 2270 C THR A1097 -5.649 -54.963 14.101 1.00 44.45 C ANISOU 2270 C THR A1097 5855 3470 7565 545 -293 274 C ATOM 2271 O THR A1097 -6.576 -54.154 13.974 1.00 43.05 O ANISOU 2271 O THR A1097 5648 3261 7448 508 -320 274 O ATOM 2272 CB THR A1097 -5.650 -56.654 15.972 1.00 41.02 C ANISOU 2272 CB THR A1097 5364 3248 6972 573 -381 234 C ATOM 2273 OG1 THR A1097 -5.685 -58.067 16.211 1.00 47.99 O ANISOU 2273 OG1 THR A1097 6339 4183 7713 592 -424 283 O ATOM 2274 CG2 THR A1097 -6.664 -55.955 16.841 1.00 41.30 C ANISOU 2274 CG2 THR A1097 5281 3349 7062 537 -438 179 C ATOM 2275 N ARG A1098 -4.379 -54.625 13.879 1.00 48.23 N ANISOU 2275 N ARG A1098 6298 3922 8105 577 -209 237 N ATOM 2276 CA ARG A1098 -4.025 -53.254 13.512 1.00 47.26 C ANISOU 2276 CA ARG A1098 6095 3736 8127 568 -145 189 C ATOM 2277 C ARG A1098 -4.704 -52.844 12.213 1.00 49.38 C ANISOU 2277 C ARG A1098 6480 3869 8411 540 -140 271 C ATOM 2278 O ARG A1098 -5.238 -51.735 12.107 1.00 53.98 O ANISOU 2278 O ARG A1098 7000 4416 9093 511 -136 245 O ATOM 2279 CB ARG A1098 -2.504 -53.128 13.394 1.00 44.55 C ANISOU 2279 CB ARG A1098 5713 3382 7831 609 -55 148 C ATOM 2280 CG ARG A1098 -1.994 -51.727 13.154 1.00 50.66 C ANISOU 2280 CG ARG A1098 6388 4103 8757 601 16 87 C ATOM 2281 CD ARG A1098 -0.597 -51.796 12.593 1.00 53.47 C ANISOU 2281 CD ARG A1098 6768 4412 9137 641 105 87 C ATOM 2282 NE ARG A1098 -0.554 -52.698 11.442 1.00 55.46 N ANISOU 2282 NE ARG A1098 7209 4574 9290 656 115 198 N ATOM 2283 CZ ARG A1098 0.551 -53.052 10.803 1.00 52.50 C ANISOU 2283 CZ ARG A1098 6897 4149 8901 693 185 224 C ATOM 2284 NH1 ARG A1098 1.728 -52.593 11.210 1.00 55.89 N ANISOU 2284 NH1 ARG A1098 7213 4613 9411 719 251 149 N ATOM 2285 NH2 ARG A1098 0.476 -53.868 9.764 1.00 57.00 N ANISOU 2285 NH2 ARG A1098 7644 4636 9377 704 188 327 N ATOM 2286 N ASN A1099 -4.737 -53.751 11.236 1.00 50.79 N ANISOU 2286 N ASN A1099 6834 3976 8489 550 -142 372 N ATOM 2287 CA ASN A1099 -5.338 -53.464 9.937 1.00 54.78 C ANISOU 2287 CA ASN A1099 7466 4350 8997 526 -138 457 C ATOM 2288 C ASN A1099 -6.855 -53.388 10.025 1.00 57.76 C ANISOU 2288 C ASN A1099 7864 4733 9349 480 -224 493 C ATOM 2289 O ASN A1099 -7.471 -52.497 9.434 1.00 64.17 O ANISOU 2289 O ASN A1099 8680 5470 10232 451 -221 510 O ATOM 2290 CB ASN A1099 -4.921 -54.535 8.921 1.00 57.53 C ANISOU 2290 CB ASN A1099 7998 4625 9237 550 -118 553 C ATOM 2291 CG ASN A1099 -3.426 -54.556 8.674 1.00 59.74 C ANISOU 2291 CG ASN A1099 8268 4882 9547 595 -26 527 C ATOM 2292 OD1 ASN A1099 -2.680 -53.760 9.240 1.00 60.66 O ANISOU 2292 OD1 ASN A1099 8241 5038 9769 608 24 438 O ATOM 2293 ND2 ASN A1099 -2.978 -55.483 7.838 1.00 59.53 N ANISOU 2293 ND2 ASN A1099 8396 4795 9428 620 -3 606 N ATOM 2294 N ALA A1100 -7.477 -54.307 10.756 1.00 57.84 N ANISOU 2294 N ALA A1100 7886 4832 9259 474 -301 505 N ATOM 2295 CA ALA A1100 -8.928 -54.400 10.767 1.00 55.61 C ANISOU 2295 CA ALA A1100 7642 4554 8935 432 -386 553 C ATOM 2296 C ALA A1100 -9.602 -53.450 11.744 1.00 60.11 C ANISOU 2296 C ALA A1100 8048 5194 9595 406 -418 473 C ATOM 2297 O ALA A1100 -10.766 -53.105 11.523 1.00 62.36 O ANISOU 2297 O ALA A1100 8352 5452 9889 368 -469 509 O ATOM 2298 CB ALA A1100 -9.370 -55.824 11.083 1.00 53.00 C ANISOU 2298 CB ALA A1100 7403 4282 8452 434 -457 607 C ATOM 2299 N TYR A1101 -8.918 -53.009 12.806 1.00 56.59 N ANISOU 2299 N TYR A1101 7445 4839 9219 424 -391 367 N ATOM 2300 CA TYR A1101 -9.582 -52.173 13.807 1.00 53.97 C ANISOU 2300 CA TYR A1101 6960 4581 8965 400 -425 291 C ATOM 2301 C TYR A1101 -8.826 -50.881 14.139 1.00 50.44 C ANISOU 2301 C TYR A1101 6363 4136 8668 407 -354 191 C ATOM 2302 O TYR A1101 -9.401 -49.792 14.096 1.00 50.67 O ANISOU 2302 O TYR A1101 6326 4134 8794 380 -352 165 O ATOM 2303 CB TYR A1101 -9.802 -52.961 15.105 1.00 50.70 C ANISOU 2303 CB TYR A1101 6481 4306 8476 406 -486 251 C ATOM 2304 CG TYR A1101 -10.687 -54.188 14.996 1.00 53.29 C ANISOU 2304 CG TYR A1101 6935 4652 8662 394 -567 339 C ATOM 2305 CD1 TYR A1101 -10.143 -55.436 14.704 1.00 54.68 C ANISOU 2305 CD1 TYR A1101 7229 4827 8720 421 -566 393 C ATOM 2306 CD2 TYR A1101 -12.058 -54.111 15.230 1.00 55.86 C ANISOU 2306 CD2 TYR A1101 7258 4997 8969 355 -643 365 C ATOM 2307 CE1 TYR A1101 -10.936 -56.569 14.623 1.00 55.04 C ANISOU 2307 CE1 TYR A1101 7390 4890 8634 409 -638 471 C ATOM 2308 CE2 TYR A1101 -12.871 -55.249 15.151 1.00 57.75 C ANISOU 2308 CE2 TYR A1101 7611 5255 9076 341 -718 445 C ATOM 2309 CZ TYR A1101 -12.299 -56.471 14.841 1.00 61.47 C ANISOU 2309 CZ TYR A1101 8201 5722 9432 368 -715 497 C ATOM 2310 OH TYR A1101 -13.087 -57.603 14.759 1.00 67.20 O ANISOU 2310 OH TYR A1101 9042 6464 10027 353 -788 576 O ATOM 2311 N ILE A1102 -7.553 -51.001 14.513 1.00 44.45 N ANISOU 2311 N ILE A1102 5547 3415 7926 443 -297 133 N ATOM 2312 CA ILE A1102 -6.830 -49.878 15.092 1.00 41.92 C ANISOU 2312 CA ILE A1102 5066 3123 7739 449 -239 25 C ATOM 2313 C ILE A1102 -6.649 -48.775 14.066 1.00 46.77 C ANISOU 2313 C ILE A1102 5695 3614 8462 438 -174 36 C ATOM 2314 O ILE A1102 -6.740 -47.586 14.389 1.00 48.82 O ANISOU 2314 O ILE A1102 5836 3874 8841 422 -151 -33 O ATOM 2315 CB ILE A1102 -5.474 -50.348 15.647 1.00 46.07 C ANISOU 2315 CB ILE A1102 5540 3715 8251 491 -194 -30 C ATOM 2316 CG1 ILE A1102 -5.641 -51.659 16.445 1.00 49.53 C ANISOU 2316 CG1 ILE A1102 6002 4259 8558 506 -258 -17 C ATOM 2317 CG2 ILE A1102 -4.866 -49.267 16.493 1.00 46.93 C ANISOU 2317 CG2 ILE A1102 5467 3878 8486 493 -152 -149 C ATOM 2318 CD1 ILE A1102 -6.596 -51.570 17.685 1.00 47.59 C ANISOU 2318 CD1 ILE A1102 5650 4126 8306 482 -335 -69 C ATOM 2319 N GLN A1103 -6.385 -49.145 12.816 1.00 47.23 N ANISOU 2319 N GLN A1103 5900 3565 8480 448 -142 122 N ATOM 2320 CA GLN A1103 -6.238 -48.131 11.782 1.00 52.73 C ANISOU 2320 CA GLN A1103 6620 4139 9275 438 -80 139 C ATOM 2321 C GLN A1103 -7.546 -47.377 11.560 1.00 46.96 C ANISOU 2321 C GLN A1103 5885 3368 8589 395 -124 162 C ATOM 2322 O GLN A1103 -7.538 -46.165 11.320 1.00 46.50 O ANISOU 2322 O GLN A1103 5759 3256 8651 381 -81 125 O ATOM 2323 CB GLN A1103 -5.755 -48.775 10.486 1.00 58.97 C ANISOU 2323 CB GLN A1103 7580 4824 10000 457 -43 234 C ATOM 2324 CG GLN A1103 -5.210 -47.769 9.501 1.00 66.77 C ANISOU 2324 CG GLN A1103 8578 5695 11095 458 40 236 C ATOM 2325 CD GLN A1103 -4.876 -48.396 8.171 1.00 72.03 C ANISOU 2325 CD GLN A1103 9424 6321 11623 463 70 328 C ATOM 2326 OE1 GLN A1103 -4.079 -49.339 8.098 1.00 76.10 O ANISOU 2326 OE1 GLN A1103 10000 6835 12077 499 90 351 O ATOM 2327 NE2 GLN A1103 -5.494 -47.888 7.105 1.00 71.22 N ANISOU 2327 NE2 GLN A1103 9409 6194 11458 429 71 378 N ATOM 2328 N LYS A1104 -8.680 -48.078 11.642 1.00 43.57 N ANISOU 2328 N LYS A1104 5526 2964 8064 375 -208 222 N ATOM 2329 CA LYS A1104 -9.964 -47.412 11.493 1.00 49.06 C ANISOU 2329 CA LYS A1104 6212 3629 8798 335 -255 245 C ATOM 2330 C LYS A1104 -10.222 -46.453 12.646 1.00 45.77 C ANISOU 2330 C LYS A1104 5614 3295 8481 321 -263 140 C ATOM 2331 O LYS A1104 -10.767 -45.357 12.441 1.00 50.36 O ANISOU 2331 O LYS A1104 6145 3828 9160 297 -253 125 O ATOM 2332 CB LYS A1104 -11.082 -48.446 11.383 1.00 50.07 C ANISOU 2332 CB LYS A1104 6454 3775 8798 316 -345 333 C ATOM 2333 CG LYS A1104 -11.051 -49.243 10.093 1.00 60.14 C ANISOU 2333 CG LYS A1104 7920 4950 9981 320 -342 446 C ATOM 2334 CD LYS A1104 -12.043 -50.397 10.150 1.00 68.86 C ANISOU 2334 CD LYS A1104 9127 6089 10948 304 -433 524 C ATOM 2335 CE LYS A1104 -11.911 -51.338 8.956 1.00 73.58 C ANISOU 2335 CE LYS A1104 9918 6648 11392 307 -418 620 C ATOM 2336 NZ LYS A1104 -10.701 -52.195 9.050 1.00 74.61 N ANISOU 2336 NZ LYS A1104 10085 6773 11491 351 -384 618 N ATOM 2337 N TYR A1105 -9.842 -46.847 13.865 1.00 41.60 N ANISOU 2337 N TYR A1105 4987 2889 7930 337 -280 67 N ATOM 2338 CA TYR A1105 -9.954 -45.939 15.002 1.00 46.79 C ANISOU 2338 CA TYR A1105 5467 3627 8683 327 -282 -40 C ATOM 2339 C TYR A1105 -9.076 -44.708 14.804 1.00 47.78 C ANISOU 2339 C TYR A1105 5504 3702 8950 333 -193 -110 C ATOM 2340 O TYR A1105 -9.514 -43.582 15.038 1.00 48.62 O ANISOU 2340 O TYR A1105 5515 3797 9160 311 -185 -158 O ATOM 2341 CB TYR A1105 -9.595 -46.653 16.307 1.00 51.15 C ANISOU 2341 CB TYR A1105 5938 4319 9179 345 -313 -104 C ATOM 2342 CG TYR A1105 -9.455 -45.695 17.473 1.00 63.42 C ANISOU 2342 CG TYR A1105 7306 5954 10837 340 -301 -224 C ATOM 2343 CD1 TYR A1105 -10.580 -45.098 18.043 1.00 70.16 C ANISOU 2343 CD1 TYR A1105 8087 6843 11730 309 -350 -249 C ATOM 2344 CD2 TYR A1105 -8.202 -45.361 17.992 1.00 67.52 C ANISOU 2344 CD2 TYR A1105 7724 6514 11418 364 -239 -313 C ATOM 2345 CE1 TYR A1105 -10.468 -44.201 19.105 1.00 69.72 C ANISOU 2345 CE1 TYR A1105 7863 6857 11769 304 -338 -360 C ATOM 2346 CE2 TYR A1105 -8.080 -44.458 19.057 1.00 70.88 C ANISOU 2346 CE2 TYR A1105 7980 7012 11940 357 -228 -425 C ATOM 2347 CZ TYR A1105 -9.221 -43.889 19.608 1.00 72.22 C ANISOU 2347 CZ TYR A1105 8083 7213 12143 326 -278 -448 C ATOM 2348 OH TYR A1105 -9.129 -43.004 20.659 1.00 76.86 O ANISOU 2348 OH TYR A1105 8509 7871 12823 319 -267 -557 O ATOM 2349 N LEU A1106 -7.841 -44.901 14.361 1.00 49.07 N ANISOU 2349 N LEU A1106 5697 3830 9118 363 -126 -113 N ATOM 2350 CA LEU A1106 -6.934 -43.776 14.140 1.00 44.11 C ANISOU 2350 CA LEU A1106 4988 3151 8621 369 -38 -177 C ATOM 2351 C LEU A1106 -7.517 -42.810 13.096 1.00 46.44 C ANISOU 2351 C LEU A1106 5329 3322 8994 344 -14 -133 C ATOM 2352 O LEU A1106 -7.443 -41.575 13.246 1.00 47.86 O ANISOU 2352 O LEU A1106 5405 3480 9300 331 26 -199 O ATOM 2353 CB LEU A1106 -5.546 -44.289 13.701 1.00 44.67 C ANISOU 2353 CB LEU A1106 5106 3198 8669 407 28 -171 C ATOM 2354 CG LEU A1106 -4.597 -43.277 13.027 1.00 53.24 C ANISOU 2354 CG LEU A1106 6161 4194 9874 414 125 -201 C ATOM 2355 CD1 LEU A1106 -3.921 -42.351 14.049 1.00 52.96 C ANISOU 2355 CD1 LEU A1106 5941 4229 9952 415 164 -328 C ATOM 2356 CD2 LEU A1106 -3.556 -43.957 12.133 1.00 56.53 C ANISOU 2356 CD2 LEU A1106 6688 4548 10241 447 180 -146 C ATOM 2357 N GLU A 219 -8.194 -43.407 12.061 1.00 48.46 N ANISOU 2357 N GLU A 219 7800 3585 7030 1253 -547 -703 N ATOM 2358 CA GLU A 219 -8.593 -42.489 10.993 1.00 47.40 C ANISOU 2358 CA GLU A 219 7627 3574 6809 1209 -466 -765 C ATOM 2359 C GLU A 219 -9.804 -41.695 11.450 1.00 45.64 C ANISOU 2359 C GLU A 219 7385 3436 6520 1053 -479 -682 C ATOM 2360 O GLU A 219 -9.891 -40.489 11.198 1.00 43.53 O ANISOU 2360 O GLU A 219 7029 3317 6195 1019 -417 -676 O ATOM 2361 CB GLU A 219 -8.898 -43.242 9.699 1.00 50.01 C ANISOU 2361 CB GLU A 219 8062 3822 7117 1226 -453 -883 C ATOM 2362 CG GLU A 219 -7.662 -43.679 8.956 1.00 59.85 C ANISOU 2362 CG GLU A 219 9280 5061 8401 1371 -396 -979 C ATOM 2363 CD GLU A 219 -7.917 -44.865 8.042 1.00 69.74 C ANISOU 2363 CD GLU A 219 10626 6219 9654 1370 -401 -1062 C ATOM 2364 OE1 GLU A 219 -9.048 -45.398 8.044 1.00 75.12 O ANISOU 2364 OE1 GLU A 219 11401 6826 10313 1260 -459 -1044 O ATOM 2365 OE2 GLU A 219 -6.985 -45.271 7.323 1.00 73.27 O ANISOU 2365 OE2 GLU A 219 11049 6666 10123 1476 -346 -1146 O ATOM 2366 N ARG A 220 -10.717 -42.378 12.154 1.00 45.23 N ANISOU 2366 N ARG A 220 7415 3290 6482 959 -560 -615 N ATOM 2367 CA ARG A 220 -11.877 -41.705 12.717 1.00 46.43 C ANISOU 2367 CA ARG A 220 7546 3518 6579 812 -576 -530 C ATOM 2368 C ARG A 220 -11.474 -40.659 13.748 1.00 44.12 C ANISOU 2368 C ARG A 220 7134 3346 6283 810 -558 -442 C ATOM 2369 O ARG A 220 -12.035 -39.564 13.769 1.00 43.98 O ANISOU 2369 O ARG A 220 7050 3457 6204 734 -521 -413 O ATOM 2370 CB ARG A 220 -12.837 -42.716 13.328 1.00 55.95 C ANISOU 2370 CB ARG A 220 8859 4595 7804 716 -665 -472 C ATOM 2371 CG ARG A 220 -13.949 -43.127 12.391 1.00 71.60 C ANISOU 2371 CG ARG A 220 10930 6533 9742 627 -677 -529 C ATOM 2372 CD ARG A 220 -13.425 -44.006 11.268 1.00 85.59 C ANISOU 2372 CD ARG A 220 12784 8199 11538 723 -669 -651 C ATOM 2373 NE ARG A 220 -14.498 -44.648 10.510 1.00 94.71 N ANISOU 2373 NE ARG A 220 14047 9278 12661 633 -702 -700 N ATOM 2374 CZ ARG A 220 -15.259 -45.637 10.978 1.00101.71 C ANISOU 2374 CZ ARG A 220 15015 10056 13574 545 -777 -653 C ATOM 2375 NH1 ARG A 220 -15.078 -46.093 12.213 1.00103.67 N ANISOU 2375 NH1 ARG A 220 15260 10254 13877 537 -827 -553 N ATOM 2376 NH2 ARG A 220 -16.211 -46.168 10.216 1.00103.67 N ANISOU 2376 NH2 ARG A 220 15334 10268 13788 458 -796 -698 N ATOM 2377 N ALA A 221 -10.516 -40.976 14.625 1.00 41.40 N ANISOU 2377 N ALA A 221 6763 2960 6005 892 -588 -398 N ATOM 2378 CA ALA A 221 -10.117 -39.998 15.634 1.00 37.54 C ANISOU 2378 CA ALA A 221 6165 2585 5513 888 -577 -316 C ATOM 2379 C ALA A 221 -9.502 -38.759 14.990 1.00 37.06 C ANISOU 2379 C ALA A 221 5992 2672 5417 934 -486 -364 C ATOM 2380 O ALA A 221 -9.756 -37.631 15.424 1.00 36.26 O ANISOU 2380 O ALA A 221 5810 2694 5273 874 -460 -313 O ATOM 2381 CB ALA A 221 -9.135 -40.616 16.627 1.00 39.22 C ANISOU 2381 CB ALA A 221 6373 2724 5805 975 -631 -265 C ATOM 2382 N ARG A 222 -8.681 -38.961 13.959 1.00 36.37 N ANISOU 2382 N ARG A 222 5900 2573 5348 1040 -437 -463 N ATOM 2383 CA ARG A 222 -8.078 -37.862 13.218 1.00 38.83 C ANISOU 2383 CA ARG A 222 6112 3019 5623 1082 -347 -514 C ATOM 2384 C ARG A 222 -9.152 -37.018 12.547 1.00 40.79 C ANISOU 2384 C ARG A 222 6359 3356 5782 974 -307 -526 C ATOM 2385 O ARG A 222 -9.140 -35.784 12.625 1.00 39.93 O ANISOU 2385 O ARG A 222 6159 3379 5633 942 -261 -499 O ATOM 2386 CB ARG A 222 -7.113 -38.443 12.187 1.00 43.79 C ANISOU 2386 CB ARG A 222 6753 3601 6284 1211 -304 -623 C ATOM 2387 CG ARG A 222 -6.237 -37.472 11.436 1.00 52.95 C ANISOU 2387 CG ARG A 222 7809 4890 7420 1275 -209 -678 C ATOM 2388 CD ARG A 222 -5.381 -38.257 10.431 1.00 62.74 C ANISOU 2388 CD ARG A 222 9078 6068 8692 1401 -171 -790 C ATOM 2389 NE ARG A 222 -4.367 -39.094 11.081 1.00 71.34 N ANISOU 2389 NE ARG A 222 10159 7069 9878 1516 -213 -783 N ATOM 2390 CZ ARG A 222 -3.774 -40.143 10.512 1.00 77.78 C ANISOU 2390 CZ ARG A 222 11030 7781 10743 1627 -213 -867 C ATOM 2391 NH1 ARG A 222 -4.109 -40.521 9.283 1.00 77.23 N ANISOU 2391 NH1 ARG A 222 11035 7680 10630 1634 -174 -968 N ATOM 2392 NH2 ARG A 222 -2.853 -40.827 11.183 1.00 82.28 N ANISOU 2392 NH2 ARG A 222 11583 8276 11404 1733 -256 -851 N ATOM 2393 N SER A 223 -10.099 -37.677 11.884 1.00 40.65 N ANISOU 2393 N SER A 223 6443 3266 5736 917 -329 -566 N ATOM 2394 CA SER A 223 -11.126 -36.952 11.154 1.00 36.58 C ANISOU 2394 CA SER A 223 5930 2831 5137 820 -297 -583 C ATOM 2395 C SER A 223 -12.053 -36.197 12.097 1.00 36.41 C ANISOU 2395 C SER A 223 5870 2880 5085 704 -324 -484 C ATOM 2396 O SER A 223 -12.547 -35.118 11.749 1.00 38.44 O ANISOU 2396 O SER A 223 6074 3250 5280 648 -282 -480 O ATOM 2397 CB SER A 223 -11.895 -37.933 10.282 1.00 46.26 C ANISOU 2397 CB SER A 223 7277 3955 6346 787 -325 -649 C ATOM 2398 OG SER A 223 -13.280 -37.649 10.303 1.00 56.23 O ANISOU 2398 OG SER A 223 8567 5246 7553 653 -352 -612 O ATOM 2399 N THR A 224 -12.284 -36.721 13.302 1.00 36.99 N ANISOU 2399 N THR A 224 5966 2890 5199 670 -391 -403 N ATOM 2400 CA THR A 224 -13.071 -35.966 14.276 1.00 36.78 C ANISOU 2400 CA THR A 224 5894 2940 5141 568 -409 -310 C ATOM 2401 C THR A 224 -12.336 -34.702 14.721 1.00 35.07 C ANISOU 2401 C THR A 224 5557 2852 4917 603 -361 -279 C ATOM 2402 O THR A 224 -12.927 -33.624 14.750 1.00 33.01 O ANISOU 2402 O THR A 224 5241 2698 4603 536 -332 -255 O ATOM 2403 CB THR A 224 -13.414 -36.852 15.468 1.00 39.30 C ANISOU 2403 CB THR A 224 6268 3164 5500 525 -489 -229 C ATOM 2404 OG1 THR A 224 -14.341 -37.857 15.052 1.00 46.06 O ANISOU 2404 OG1 THR A 224 7233 3915 6352 462 -533 -250 O ATOM 2405 CG2 THR A 224 -14.022 -36.047 16.580 1.00 38.76 C ANISOU 2405 CG2 THR A 224 6142 3183 5402 437 -501 -134 C ATOM 2406 N LEU A 225 -11.027 -34.808 15.008 1.00 38.47 N ANISOU 2406 N LEU A 225 5944 3272 5402 710 -352 -286 N ATOM 2407 CA LEU A 225 -10.227 -33.638 15.364 1.00 36.86 C ANISOU 2407 CA LEU A 225 5624 3185 5195 747 -308 -264 C ATOM 2408 C LEU A 225 -10.141 -32.638 14.218 1.00 38.39 C ANISOU 2408 C LEU A 225 5767 3481 5338 753 -227 -326 C ATOM 2409 O LEU A 225 -10.114 -31.423 14.446 1.00 37.29 O ANISOU 2409 O LEU A 225 5546 3454 5169 724 -192 -297 O ATOM 2410 CB LEU A 225 -8.820 -34.063 15.782 1.00 43.80 C ANISOU 2410 CB LEU A 225 6467 4027 6147 865 -317 -267 C ATOM 2411 CG LEU A 225 -8.694 -34.758 17.137 1.00 48.04 C ANISOU 2411 CG LEU A 225 7028 4490 6733 865 -397 -185 C ATOM 2412 CD1 LEU A 225 -7.326 -35.370 17.259 1.00 46.93 C ANISOU 2412 CD1 LEU A 225 6866 4294 6669 996 -409 -207 C ATOM 2413 CD2 LEU A 225 -8.934 -33.754 18.264 1.00 51.35 C ANISOU 2413 CD2 LEU A 225 7378 5008 7126 798 -407 -99 C ATOM 2414 N GLN A 226 -10.068 -33.120 12.979 1.00 40.71 N ANISOU 2414 N GLN A 226 6111 3737 5621 792 -196 -413 N ATOM 2415 CA GLN A 226 -9.954 -32.178 11.873 1.00 42.82 C ANISOU 2415 CA GLN A 226 6333 4104 5834 797 -118 -469 C ATOM 2416 C GLN A 226 -11.256 -31.417 11.671 1.00 40.91 C ANISOU 2416 C GLN A 226 6098 3925 5520 682 -117 -444 C ATOM 2417 O GLN A 226 -11.232 -30.241 11.282 1.00 34.60 O ANISOU 2417 O GLN A 226 5235 3235 4678 665 -64 -445 O ATOM 2418 CB GLN A 226 -9.516 -32.906 10.594 1.00 44.86 C ANISOU 2418 CB GLN A 226 6646 4309 6091 871 -84 -571 C ATOM 2419 CG GLN A 226 -8.019 -33.174 10.588 1.00 52.49 C ANISOU 2419 CG GLN A 226 7561 5264 7118 999 -53 -606 C ATOM 2420 CD GLN A 226 -7.576 -34.225 9.570 1.00 63.71 C ANISOU 2420 CD GLN A 226 9051 6601 8556 1084 -35 -706 C ATOM 2421 OE1 GLN A 226 -8.401 -34.885 8.932 1.00 67.66 O ANISOU 2421 OE1 GLN A 226 9650 7032 9024 1045 -56 -749 O ATOM 2422 NE2 GLN A 226 -6.262 -34.387 9.424 1.00 66.72 N ANISOU 2422 NE2 GLN A 226 9377 6986 8985 1202 3 -747 N ATOM 2423 N LYS A 227 -12.394 -32.050 11.980 1.00 44.22 N ANISOU 2423 N LYS A 227 6592 4281 5930 601 -176 -416 N ATOM 2424 CA LYS A 227 -13.665 -31.330 11.958 1.00 38.60 C ANISOU 2424 CA LYS A 227 5876 3633 5158 491 -181 -383 C ATOM 2425 C LYS A 227 -13.748 -30.299 13.078 1.00 34.11 C ANISOU 2425 C LYS A 227 5223 3151 4586 452 -182 -302 C ATOM 2426 O LYS A 227 -14.324 -29.224 12.884 1.00 34.82 O ANISOU 2426 O LYS A 227 5269 3334 4627 399 -155 -288 O ATOM 2427 CB LYS A 227 -14.835 -32.309 12.043 1.00 37.88 C ANISOU 2427 CB LYS A 227 5878 3453 5062 412 -244 -373 C ATOM 2428 CG LYS A 227 -15.010 -33.139 10.788 1.00 43.94 C ANISOU 2428 CG LYS A 227 6732 4149 5813 429 -242 -461 C ATOM 2429 CD LYS A 227 -16.121 -34.173 10.945 1.00 50.93 C ANISOU 2429 CD LYS A 227 7711 4937 6702 346 -312 -448 C ATOM 2430 CE LYS A 227 -16.229 -35.043 9.683 1.00 59.59 C ANISOU 2430 CE LYS A 227 8901 5955 7785 367 -314 -543 C ATOM 2431 NZ LYS A 227 -17.099 -36.247 9.882 1.00 66.99 N ANISOU 2431 NZ LYS A 227 9939 6771 8742 298 -389 -535 N ATOM 2432 N GLU A 228 -13.208 -30.601 14.261 1.00 34.17 N ANISOU 2432 N GLU A 228 5212 3128 4645 477 -217 -246 N ATOM 2433 CA GLU A 228 -13.221 -29.604 15.337 1.00 32.40 C ANISOU 2433 CA GLU A 228 4910 2988 4414 444 -217 -175 C ATOM 2434 C GLU A 228 -12.339 -28.413 14.993 1.00 33.57 C ANISOU 2434 C GLU A 228 4966 3235 4552 494 -154 -195 C ATOM 2435 O GLU A 228 -12.692 -27.268 15.317 1.00 30.64 O ANISOU 2435 O GLU A 228 4538 2956 4149 447 -136 -161 O ATOM 2436 CB GLU A 228 -12.790 -30.216 16.686 1.00 33.65 C ANISOU 2436 CB GLU A 228 5071 3092 4623 460 -272 -110 C ATOM 2437 CG GLU A 228 -13.833 -31.151 17.291 1.00 40.95 C ANISOU 2437 CG GLU A 228 6075 3938 5548 383 -336 -64 C ATOM 2438 CD GLU A 228 -13.404 -31.756 18.637 1.00 44.99 C ANISOU 2438 CD GLU A 228 6596 4396 6104 397 -393 6 C ATOM 2439 OE1 GLU A 228 -12.901 -32.903 18.628 1.00 40.94 O ANISOU 2439 OE1 GLU A 228 6142 3773 5640 451 -430 -5 O ATOM 2440 OE2 GLU A 228 -13.587 -31.095 19.696 1.00 43.09 O ANISOU 2440 OE2 GLU A 228 6306 4221 5845 354 -404 73 O ATOM 2441 N VAL A 229 -11.183 -28.657 14.350 1.00 33.22 N ANISOU 2441 N VAL A 229 4908 3176 4539 589 -119 -250 N ATOM 2442 CA VAL A 229 -10.331 -27.550 13.902 1.00 35.88 C ANISOU 2442 CA VAL A 229 5159 3609 4866 631 -54 -271 C ATOM 2443 C VAL A 229 -11.073 -26.684 12.889 1.00 36.02 C ANISOU 2443 C VAL A 229 5176 3696 4815 578 -9 -300 C ATOM 2444 O VAL A 229 -11.063 -25.449 12.977 1.00 34.73 O ANISOU 2444 O VAL A 229 4947 3625 4625 551 22 -276 O ATOM 2445 CB VAL A 229 -9.011 -28.073 13.312 1.00 36.35 C ANISOU 2445 CB VAL A 229 5203 3639 4969 741 -20 -330 C ATOM 2446 CG1 VAL A 229 -8.224 -26.915 12.703 1.00 32.61 C ANISOU 2446 CG1 VAL A 229 4643 3271 4477 772 54 -355 C ATOM 2447 CG2 VAL A 229 -8.188 -28.761 14.369 1.00 33.81 C ANISOU 2447 CG2 VAL A 229 4866 3260 4719 801 -67 -296 C ATOM 2448 N HIS A 230 -11.719 -27.324 11.906 1.00 34.14 N ANISOU 2448 N HIS A 230 5014 3411 4546 562 -9 -351 N ATOM 2449 CA HIS A 230 -12.487 -26.587 10.908 1.00 37.19 C ANISOU 2449 CA HIS A 230 5408 3859 4863 510 24 -376 C ATOM 2450 C HIS A 230 -13.617 -25.782 11.553 1.00 36.24 C ANISOU 2450 C HIS A 230 5268 3792 4712 417 -2 -314 C ATOM 2451 O HIS A 230 -13.850 -24.621 11.189 1.00 33.68 O ANISOU 2451 O HIS A 230 4899 3552 4345 389 32 -308 O ATOM 2452 CB HIS A 230 -13.035 -27.567 9.867 1.00 45.91 C ANISOU 2452 CB HIS A 230 6608 4894 5943 505 14 -440 C ATOM 2453 CG HIS A 230 -13.688 -26.904 8.690 1.00 58.82 C ANISOU 2453 CG HIS A 230 8255 6589 7503 464 48 -475 C ATOM 2454 ND1 HIS A 230 -15.041 -26.639 8.639 1.00 61.43 N ANISOU 2454 ND1 HIS A 230 8612 6938 7791 373 15 -451 N ATOM 2455 CD2 HIS A 230 -13.174 -26.457 7.519 1.00 61.44 C ANISOU 2455 CD2 HIS A 230 8578 6970 7796 502 110 -531 C ATOM 2456 CE1 HIS A 230 -15.331 -26.051 7.491 1.00 61.52 C ANISOU 2456 CE1 HIS A 230 8630 7004 7740 359 50 -489 C ATOM 2457 NE2 HIS A 230 -14.216 -25.922 6.797 1.00 62.11 N ANISOU 2457 NE2 HIS A 230 8688 7100 7813 434 109 -536 N ATOM 2458 N ALA A 231 -14.352 -26.396 12.490 1.00 36.67 N ANISOU 2458 N ALA A 231 5354 3795 4783 367 -62 -268 N ATOM 2459 CA ALA A 231 -15.429 -25.687 13.179 1.00 37.19 C ANISOU 2459 CA ALA A 231 5396 3914 4822 281 -85 -211 C ATOM 2460 C ALA A 231 -14.892 -24.528 14.025 1.00 35.86 C ANISOU 2460 C ALA A 231 5139 3825 4662 291 -65 -166 C ATOM 2461 O ALA A 231 -15.491 -23.447 14.065 1.00 31.73 O ANISOU 2461 O ALA A 231 4576 3376 4102 245 -50 -145 O ATOM 2462 CB ALA A 231 -16.223 -26.667 14.044 1.00 35.97 C ANISOU 2462 CB ALA A 231 5294 3689 4686 227 -149 -170 C ATOM 2463 N ALA A 232 -13.764 -24.731 14.716 1.00 31.30 N ANISOU 2463 N ALA A 232 4530 3229 4133 352 -67 -151 N ATOM 2464 CA ALA A 232 -13.223 -23.635 15.511 1.00 30.96 C ANISOU 2464 CA ALA A 232 4406 3261 4098 358 -52 -111 C ATOM 2465 C ALA A 232 -12.710 -22.509 14.621 1.00 30.67 C ANISOU 2465 C ALA A 232 4317 3299 4038 381 10 -144 C ATOM 2466 O ALA A 232 -12.815 -21.337 14.993 1.00 31.53 O ANISOU 2466 O ALA A 232 4371 3480 4130 353 24 -115 O ATOM 2467 CB ALA A 232 -12.115 -24.125 16.441 1.00 29.06 C ANISOU 2467 CB ALA A 232 4140 2985 3915 417 -75 -87 C ATOM 2468 N LYS A 233 -12.192 -22.834 13.428 1.00 29.62 N ANISOU 2468 N LYS A 233 4204 3151 3901 429 49 -203 N ATOM 2469 CA LYS A 233 -11.760 -21.774 12.531 1.00 29.98 C ANISOU 2469 CA LYS A 233 4205 3270 3917 443 110 -229 C ATOM 2470 C LYS A 233 -12.951 -20.942 12.060 1.00 29.31 C ANISOU 2470 C LYS A 233 4132 3232 3771 371 114 -221 C ATOM 2471 O LYS A 233 -12.858 -19.713 11.950 1.00 29.36 O ANISOU 2471 O LYS A 233 4087 3310 3757 356 144 -206 O ATOM 2472 CB LYS A 233 -10.998 -22.357 11.340 1.00 33.21 C ANISOU 2472 CB LYS A 233 4638 3656 4326 508 153 -297 C ATOM 2473 CG LYS A 233 -9.559 -22.693 11.691 1.00 44.77 C ANISOU 2473 CG LYS A 233 6054 5107 5850 591 169 -306 C ATOM 2474 CD LYS A 233 -8.695 -23.056 10.487 1.00 47.97 C ANISOU 2474 CD LYS A 233 6463 5510 6252 660 228 -377 C ATOM 2475 CE LYS A 233 -7.252 -23.342 10.918 1.00 46.46 C ANISOU 2475 CE LYS A 233 6210 5315 6128 745 242 -383 C ATOM 2476 NZ LYS A 233 -6.544 -24.192 9.897 1.00 50.45 N ANISOU 2476 NZ LYS A 233 6741 5787 6642 825 284 -459 N ATOM 2477 N SER A 234 -14.085 -21.601 11.791 1.00 29.73 N ANISOU 2477 N SER A 234 4251 3245 3799 326 80 -229 N ATOM 2478 CA SER A 234 -15.281 -20.887 11.372 1.00 27.61 C ANISOU 2478 CA SER A 234 3992 3022 3478 260 76 -220 C ATOM 2479 C SER A 234 -15.753 -19.921 12.447 1.00 31.03 C ANISOU 2479 C SER A 234 4371 3506 3912 216 59 -162 C ATOM 2480 O SER A 234 -16.046 -18.752 12.158 1.00 30.22 O ANISOU 2480 O SER A 234 4235 3467 3780 195 80 -152 O ATOM 2481 CB SER A 234 -16.372 -21.884 11.015 1.00 27.05 C ANISOU 2481 CB SER A 234 3996 2895 3387 217 35 -238 C ATOM 2482 OG SER A 234 -15.920 -22.654 9.928 1.00 32.16 O ANISOU 2482 OG SER A 234 4695 3499 4026 259 55 -300 O ATOM 2483 N ALA A 235 -15.835 -20.395 13.696 1.00 30.59 N ANISOU 2483 N ALA A 235 4310 3421 3890 204 20 -123 N ATOM 2484 CA ALA A 235 -16.229 -19.538 14.798 1.00 30.23 C ANISOU 2484 CA ALA A 235 4216 3424 3844 167 5 -72 C ATOM 2485 C ALA A 235 -15.225 -18.401 14.996 1.00 29.68 C ANISOU 2485 C ALA A 235 4078 3410 3787 202 41 -64 C ATOM 2486 O ALA A 235 -15.610 -17.241 15.255 1.00 25.75 O ANISOU 2486 O ALA A 235 3543 2972 3271 173 49 -43 O ATOM 2487 CB ALA A 235 -16.396 -20.387 16.065 1.00 27.33 C ANISOU 2487 CB ALA A 235 3864 3013 3506 150 -42 -32 C ATOM 2488 N ALA A 236 -13.932 -18.700 14.849 1.00 27.82 N ANISOU 2488 N ALA A 236 3827 3158 3586 264 62 -83 N ATOM 2489 CA ALA A 236 -12.914 -17.651 14.971 1.00 27.56 C ANISOU 2489 CA ALA A 236 3725 3178 3567 293 96 -77 C ATOM 2490 C ALA A 236 -13.021 -16.610 13.860 1.00 24.73 C ANISOU 2490 C ALA A 236 3354 2871 3170 283 142 -98 C ATOM 2491 O ALA A 236 -12.713 -15.431 14.097 1.00 25.89 O ANISOU 2491 O ALA A 236 3450 3070 3317 274 160 -79 O ATOM 2492 CB ALA A 236 -11.490 -18.249 14.974 1.00 28.20 C ANISOU 2492 CB ALA A 236 3784 3233 3696 364 111 -95 C ATOM 2493 N ILE A 237 -13.401 -17.020 12.644 1.00 22.73 N ANISOU 2493 N ILE A 237 3149 2602 2884 283 160 -136 N ATOM 2494 CA ILE A 237 -13.585 -16.040 11.571 1.00 23.45 C ANISOU 2494 CA ILE A 237 3236 2744 2931 269 199 -150 C ATOM 2495 C ILE A 237 -14.689 -15.059 11.953 1.00 25.63 C ANISOU 2495 C ILE A 237 3500 3057 3181 212 176 -115 C ATOM 2496 O ILE A 237 -14.554 -13.841 11.788 1.00 25.56 O ANISOU 2496 O ILE A 237 3456 3096 3160 202 199 -101 O ATOM 2497 CB ILE A 237 -13.903 -16.734 10.248 1.00 25.87 C ANISOU 2497 CB ILE A 237 3604 3026 3198 275 214 -197 C ATOM 2498 CG1 ILE A 237 -12.649 -17.437 9.680 1.00 28.72 C ANISOU 2498 CG1 ILE A 237 3967 3365 3580 342 253 -240 C ATOM 2499 CG2 ILE A 237 -14.489 -15.710 9.216 1.00 26.83 C ANISOU 2499 CG2 ILE A 237 3733 3199 3261 243 237 -200 C ATOM 2500 CD1 ILE A 237 -12.998 -18.532 8.670 1.00 32.79 C ANISOU 2500 CD1 ILE A 237 4557 3833 4067 354 253 -293 C ATOM 2501 N ILE A 238 -15.775 -15.576 12.520 1.00 21.71 N ANISOU 2501 N ILE A 238 3031 2537 2680 174 130 -100 N ATOM 2502 CA ILE A 238 -16.860 -14.705 12.959 1.00 26.07 C ANISOU 2502 CA ILE A 238 3567 3127 3211 125 109 -70 C ATOM 2503 C ILE A 238 -16.404 -13.744 14.053 1.00 24.93 C ANISOU 2503 C ILE A 238 3364 3017 3093 127 111 -37 C ATOM 2504 O ILE A 238 -16.745 -12.551 14.023 1.00 25.14 O ANISOU 2504 O ILE A 238 3364 3086 3103 109 118 -24 O ATOM 2505 CB ILE A 238 -18.059 -15.566 13.382 1.00 28.13 C ANISOU 2505 CB ILE A 238 3864 3359 3465 83 64 -61 C ATOM 2506 CG1 ILE A 238 -18.579 -16.255 12.096 1.00 34.60 C ANISOU 2506 CG1 ILE A 238 4742 4153 4252 75 62 -99 C ATOM 2507 CG2 ILE A 238 -19.102 -14.711 14.096 1.00 25.10 C ANISOU 2507 CG2 ILE A 238 3450 3020 3069 39 43 -29 C ATOM 2508 CD1 ILE A 238 -19.990 -16.638 12.128 1.00 41.42 C ANISOU 2508 CD1 ILE A 238 5632 5012 5094 19 22 -92 C ATOM 2509 N ALA A 239 -15.634 -14.230 15.032 1.00 22.33 N ANISOU 2509 N ALA A 239 3015 2666 2802 149 99 -24 N ATOM 2510 CA ALA A 239 -15.118 -13.327 16.064 1.00 24.35 C ANISOU 2510 CA ALA A 239 3217 2955 3079 151 98 3 C ATOM 2511 C ALA A 239 -14.158 -12.297 15.472 1.00 21.79 C ANISOU 2511 C ALA A 239 2855 2664 2760 173 139 -6 C ATOM 2512 O ALA A 239 -14.181 -11.120 15.855 1.00 24.07 O ANISOU 2512 O ALA A 239 3108 2989 3047 157 143 11 O ATOM 2513 CB ALA A 239 -14.436 -14.114 17.189 1.00 21.74 C ANISOU 2513 CB ALA A 239 2876 2597 2787 171 72 20 C ATOM 2514 N GLY A 240 -13.339 -12.708 14.510 1.00 23.97 N ANISOU 2514 N GLY A 240 3138 2929 3042 209 173 -34 N ATOM 2515 CA GLY A 240 -12.414 -11.772 13.896 1.00 26.23 C ANISOU 2515 CA GLY A 240 3387 3250 3330 225 218 -40 C ATOM 2516 C GLY A 240 -13.134 -10.718 13.069 1.00 27.27 C ANISOU 2516 C GLY A 240 3530 3412 3418 192 234 -37 C ATOM 2517 O GLY A 240 -12.700 -9.574 12.996 1.00 22.99 O ANISOU 2517 O GLY A 240 2953 2903 2879 184 255 -24 O ATOM 2518 N LEU A 241 -14.237 -11.091 12.431 1.00 21.95 N ANISOU 2518 N LEU A 241 2907 2728 2707 172 221 -48 N ATOM 2519 CA LEU A 241 -14.965 -10.124 11.630 1.00 22.42 C ANISOU 2519 CA LEU A 241 2978 2814 2724 145 229 -43 C ATOM 2520 C LEU A 241 -15.711 -9.124 12.504 1.00 19.30 C ANISOU 2520 C LEU A 241 2559 2440 2333 115 200 -13 C ATOM 2521 O LEU A 241 -15.874 -7.968 12.122 1.00 22.31 O ANISOU 2521 O LEU A 241 2931 2847 2700 102 210 0 O ATOM 2522 CB LEU A 241 -15.953 -10.842 10.721 1.00 23.32 C ANISOU 2522 CB LEU A 241 3151 2913 2796 132 216 -64 C ATOM 2523 CG LEU A 241 -15.290 -11.526 9.532 1.00 27.47 C ANISOU 2523 CG LEU A 241 3709 3428 3302 160 252 -101 C ATOM 2524 CD1 LEU A 241 -16.362 -12.334 8.857 1.00 29.80 C ANISOU 2524 CD1 LEU A 241 4063 3700 3558 141 226 -123 C ATOM 2525 CD2 LEU A 241 -14.644 -10.510 8.569 1.00 28.61 C ANISOU 2525 CD2 LEU A 241 3840 3610 3420 165 301 -99 C ATOM 2526 N PHE A 242 -16.221 -9.563 13.649 1.00 21.51 N ANISOU 2526 N PHE A 242 2832 2708 2631 104 164 -1 N ATOM 2527 CA PHE A 242 -16.753 -8.616 14.619 1.00 25.91 C ANISOU 2527 CA PHE A 242 3360 3289 3195 83 143 22 C ATOM 2528 C PHE A 242 -15.691 -7.576 14.979 1.00 25.47 C ANISOU 2528 C PHE A 242 3261 3250 3164 94 162 32 C ATOM 2529 O PHE A 242 -15.940 -6.365 14.931 1.00 19.60 O ANISOU 2529 O PHE A 242 2505 2527 2415 81 164 43 O ATOM 2530 CB PHE A 242 -17.270 -9.368 15.863 1.00 21.83 C ANISOU 2530 CB PHE A 242 2842 2761 2690 70 107 33 C ATOM 2531 CG PHE A 242 -17.852 -8.445 16.928 1.00 21.54 C ANISOU 2531 CG PHE A 242 2776 2753 2656 50 89 51 C ATOM 2532 CD1 PHE A 242 -17.026 -7.758 17.787 1.00 18.36 C ANISOU 2532 CD1 PHE A 242 2337 2363 2278 59 91 60 C ATOM 2533 CD2 PHE A 242 -19.223 -8.243 17.024 1.00 20.15 C ANISOU 2533 CD2 PHE A 242 2606 2594 2455 23 69 55 C ATOM 2534 CE1 PHE A 242 -17.543 -6.833 18.733 1.00 23.49 C ANISOU 2534 CE1 PHE A 242 2964 3038 2925 44 76 70 C ATOM 2535 CE2 PHE A 242 -19.749 -7.347 17.976 1.00 23.18 C ANISOU 2535 CE2 PHE A 242 2961 3007 2840 12 57 65 C ATOM 2536 CZ PHE A 242 -18.909 -6.653 18.828 1.00 22.91 C ANISOU 2536 CZ PHE A 242 2897 2981 2826 22 61 70 C ATOM 2537 N ALA A 243 -14.484 -8.032 15.305 1.00 20.96 N ANISOU 2537 N ALA A 243 2669 2670 2625 119 175 29 N ATOM 2538 CA ALA A 243 -13.398 -7.104 15.640 1.00 19.09 C ANISOU 2538 CA ALA A 243 2386 2452 2417 125 191 38 C ATOM 2539 C ALA A 243 -13.074 -6.183 14.470 1.00 18.53 C ANISOU 2539 C ALA A 243 2314 2397 2329 120 229 37 C ATOM 2540 O ALA A 243 -12.932 -4.973 14.646 1.00 24.86 O ANISOU 2540 O ALA A 243 3094 3214 3137 103 231 51 O ATOM 2541 CB ALA A 243 -12.143 -7.899 16.058 1.00 21.61 C ANISOU 2541 CB ALA A 243 2677 2760 2773 156 197 34 C ATOM 2542 N LEU A 244 -13.024 -6.720 13.251 1.00 22.47 N ANISOU 2542 N LEU A 244 2843 2892 2803 131 257 21 N ATOM 2543 CA ALEU A 244 -12.671 -5.900 12.095 0.52 23.17 C ANISOU 2543 CA ALEU A 244 2935 3000 2869 124 296 23 C ATOM 2544 CA BLEU A 244 -12.659 -5.881 12.115 0.48 23.07 C ANISOU 2544 CA BLEU A 244 2922 2988 2857 124 296 23 C ATOM 2545 C LEU A 244 -13.731 -4.834 11.820 1.00 25.16 C ANISOU 2545 C LEU A 244 3209 3259 3092 95 279 41 C ATOM 2546 O LEU A 244 -13.404 -3.714 11.436 1.00 22.36 O ANISOU 2546 O LEU A 244 2844 2918 2734 80 296 58 O ATOM 2547 CB ALEU A 244 -12.475 -6.788 10.859 0.52 22.43 C ANISOU 2547 CB ALEU A 244 2875 2902 2744 144 330 -3 C ATOM 2548 CB BLEU A 244 -12.396 -6.735 10.874 0.48 22.45 C ANISOU 2548 CB BLEU A 244 2874 2906 2749 144 331 -2 C ATOM 2549 CG ALEU A 244 -12.372 -6.136 9.475 0.52 22.52 C ANISOU 2549 CG ALEU A 244 2909 2937 2713 133 369 -1 C ATOM 2550 CG BLEU A 244 -10.938 -7.096 10.581 0.48 24.18 C ANISOU 2550 CG BLEU A 244 3059 3136 2992 174 378 -16 C ATOM 2551 CD1ALEU A 244 -11.191 -5.180 9.430 0.52 24.87 C ANISOU 2551 CD1ALEU A 244 3158 3259 3032 127 407 16 C ATOM 2552 CD1BLEU A 244 -10.876 -8.283 9.618 0.48 23.45 C ANISOU 2552 CD1BLEU A 244 3005 3031 2873 203 402 -53 C ATOM 2553 CD2ALEU A 244 -12.239 -7.166 8.342 0.52 21.79 C ANISOU 2553 CD2ALEU A 244 2854 2840 2583 155 400 -35 C ATOM 2554 CD2BLEU A 244 -10.206 -5.908 9.987 0.48 26.63 C ANISOU 2554 CD2BLEU A 244 3342 3479 3297 156 419 1 C ATOM 2555 N CYS A 245 -15.013 -5.179 11.967 1.00 20.71 N ANISOU 2555 N CYS A 245 2675 2687 2508 86 244 38 N ATOM 2556 CA CYS A 245 -16.053 -4.201 11.671 1.00 21.09 C ANISOU 2556 CA CYS A 245 2740 2744 2531 65 224 53 C ATOM 2557 C CYS A 245 -16.214 -3.137 12.758 1.00 21.64 C ANISOU 2557 C CYS A 245 2777 2816 2628 56 202 69 C ATOM 2558 O CYS A 245 -16.625 -2.019 12.443 1.00 21.12 O ANISOU 2558 O CYS A 245 2718 2754 2553 45 196 84 O ATOM 2559 CB CYS A 245 -17.402 -4.893 11.477 1.00 20.91 C ANISOU 2559 CB CYS A 245 2750 2717 2480 58 192 43 C ATOM 2560 SG CYS A 245 -17.464 -5.971 10.017 1.00 25.76 S ANISOU 2560 SG CYS A 245 3415 3323 3048 64 210 19 S ATOM 2561 N TRP A 246 -15.956 -3.467 14.028 1.00 19.15 N ANISOU 2561 N TRP A 246 2433 2497 2344 60 186 66 N ATOM 2562 CA TRP A 246 -16.162 -2.511 15.125 1.00 19.87 C ANISOU 2562 CA TRP A 246 2499 2593 2456 51 163 75 C ATOM 2563 C TRP A 246 -14.911 -1.732 15.490 1.00 21.56 C ANISOU 2563 C TRP A 246 2680 2808 2703 49 179 82 C ATOM 2564 O TRP A 246 -15.033 -0.633 16.034 1.00 19.33 O ANISOU 2564 O TRP A 246 2387 2526 2434 38 164 88 O ATOM 2565 CB TRP A 246 -16.632 -3.214 16.416 1.00 20.86 C ANISOU 2565 CB TRP A 246 2613 2722 2591 51 135 69 C ATOM 2566 CG TRP A 246 -18.074 -3.606 16.330 1.00 21.66 C ANISOU 2566 CG TRP A 246 2736 2829 2666 43 113 66 C ATOM 2567 CD1 TRP A 246 -18.592 -4.818 15.958 1.00 23.58 C ANISOU 2567 CD1 TRP A 246 3003 3065 2891 40 107 59 C ATOM 2568 CD2 TRP A 246 -19.176 -2.735 16.558 1.00 23.31 C ANISOU 2568 CD2 TRP A 246 2941 3051 2864 35 93 68 C ATOM 2569 NE1 TRP A 246 -19.992 -4.753 15.973 1.00 23.35 N ANISOU 2569 NE1 TRP A 246 2981 3049 2840 25 84 59 N ATOM 2570 CE2 TRP A 246 -20.360 -3.474 16.325 1.00 23.50 C ANISOU 2570 CE2 TRP A 246 2982 3084 2865 26 77 64 C ATOM 2571 CE3 TRP A 246 -19.279 -1.396 16.967 1.00 20.93 C ANISOU 2571 CE3 TRP A 246 2625 2754 2574 37 87 70 C ATOM 2572 CZ2 TRP A 246 -21.627 -2.916 16.496 1.00 23.33 C ANISOU 2572 CZ2 TRP A 246 2952 3081 2831 21 56 63 C ATOM 2573 CZ3 TRP A 246 -20.551 -0.832 17.107 1.00 22.13 C ANISOU 2573 CZ3 TRP A 246 2775 2918 2714 38 66 67 C ATOM 2574 CH2 TRP A 246 -21.705 -1.602 16.884 1.00 23.23 C ANISOU 2574 CH2 TRP A 246 2922 3073 2831 31 52 64 C ATOM 2575 N LEU A 247 -13.711 -2.283 15.265 1.00 22.29 N ANISOU 2575 N LEU A 247 2754 2901 2812 59 205 80 N ATOM 2576 CA LEU A 247 -12.501 -1.560 15.686 1.00 22.59 C ANISOU 2576 CA LEU A 247 2752 2946 2886 52 216 87 C ATOM 2577 C LEU A 247 -12.348 -0.169 15.087 1.00 21.38 C ANISOU 2577 C LEU A 247 2602 2792 2732 30 230 103 C ATOM 2578 O LEU A 247 -11.869 0.731 15.808 1.00 21.90 O ANISOU 2578 O LEU A 247 2641 2854 2825 15 218 109 O ATOM 2579 CB LEU A 247 -11.236 -2.386 15.369 1.00 22.59 C ANISOU 2579 CB LEU A 247 2726 2953 2905 71 247 81 C ATOM 2580 CG LEU A 247 -10.884 -3.447 16.430 1.00 27.39 C ANISOU 2580 CG LEU A 247 3313 3557 3538 92 224 73 C ATOM 2581 CD1 LEU A 247 -9.754 -4.391 15.942 1.00 29.06 C ANISOU 2581 CD1 LEU A 247 3502 3771 3768 122 255 63 C ATOM 2582 CD2 LEU A 247 -10.467 -2.767 17.736 1.00 27.99 C ANISOU 2582 CD2 LEU A 247 3352 3638 3643 79 194 81 C ATOM 2583 N PRO A 248 -12.631 0.073 13.797 1.00 21.86 N ANISOU 2583 N PRO A 248 2693 2852 2761 25 253 112 N ATOM 2584 CA PRO A 248 -12.458 1.440 13.268 1.00 20.24 C ANISOU 2584 CA PRO A 248 2495 2640 2555 0 262 134 C ATOM 2585 C PRO A 248 -13.178 2.489 14.079 1.00 21.43 C ANISOU 2585 C PRO A 248 2651 2773 2720 -10 223 138 C ATOM 2586 O PRO A 248 -12.594 3.537 14.393 1.00 22.73 O ANISOU 2586 O PRO A 248 2799 2926 2910 -30 220 149 O ATOM 2587 CB PRO A 248 -13.027 1.324 11.838 1.00 22.59 C ANISOU 2587 CB PRO A 248 2838 2942 2805 0 282 142 C ATOM 2588 CG PRO A 248 -12.675 -0.051 11.444 1.00 20.54 C ANISOU 2588 CG PRO A 248 2577 2697 2532 21 307 122 C ATOM 2589 CD PRO A 248 -13.055 -0.845 12.720 1.00 22.78 C ANISOU 2589 CD PRO A 248 2844 2973 2838 38 271 103 C ATOM 2590 N LEU A 249 -14.429 2.227 14.456 1.00 19.15 N ANISOU 2590 N LEU A 249 2382 2482 2414 4 192 127 N ATOM 2591 CA LEU A 249 -15.176 3.193 15.257 1.00 22.62 C ANISOU 2591 CA LEU A 249 2823 2907 2865 3 156 123 C ATOM 2592 C LEU A 249 -14.540 3.411 16.637 1.00 21.10 C ANISOU 2592 C LEU A 249 2596 2714 2708 -2 141 111 C ATOM 2593 O LEU A 249 -14.438 4.549 17.108 1.00 21.81 O ANISOU 2593 O LEU A 249 2682 2785 2817 -13 126 111 O ATOM 2594 CB LEU A 249 -16.618 2.711 15.379 1.00 23.29 C ANISOU 2594 CB LEU A 249 2926 3000 2925 20 132 112 C ATOM 2595 CG LEU A 249 -17.769 3.644 15.796 1.00 27.72 C ANISOU 2595 CG LEU A 249 3495 3551 3486 29 99 107 C ATOM 2596 CD1 LEU A 249 -17.766 4.967 15.070 1.00 27.06 C ANISOU 2596 CD1 LEU A 249 3434 3440 3406 23 96 126 C ATOM 2597 CD2 LEU A 249 -19.117 2.920 15.601 1.00 24.82 C ANISOU 2597 CD2 LEU A 249 3139 3202 3090 42 83 99 C ATOM 2598 N HIS A 250 -14.147 2.330 17.319 1.00 21.42 N ANISOU 2598 N HIS A 250 2613 2772 2754 7 141 99 N ATOM 2599 CA HIS A 250 -13.470 2.464 18.613 1.00 19.92 C ANISOU 2599 CA HIS A 250 2391 2586 2592 1 124 89 C ATOM 2600 C HIS A 250 -12.161 3.210 18.483 1.00 20.90 C ANISOU 2600 C HIS A 250 2489 2703 2748 -20 137 100 C ATOM 2601 O HIS A 250 -11.782 3.984 19.361 1.00 21.18 O ANISOU 2601 O HIS A 250 2509 2732 2807 -35 116 93 O ATOM 2602 CB HIS A 250 -13.194 1.082 19.209 1.00 20.03 C ANISOU 2602 CB HIS A 250 2388 2617 2606 16 120 83 C ATOM 2603 CG HIS A 250 -14.423 0.373 19.686 1.00 18.44 C ANISOU 2603 CG HIS A 250 2206 2423 2377 26 101 74 C ATOM 2604 ND1 HIS A 250 -15.177 0.813 20.753 1.00 20.76 N ANISOU 2604 ND1 HIS A 250 2500 2725 2665 24 74 62 N ATOM 2605 CD2 HIS A 250 -15.011 -0.767 19.250 1.00 22.01 C ANISOU 2605 CD2 HIS A 250 2676 2878 2808 37 106 74 C ATOM 2606 CE1 HIS A 250 -16.164 -0.041 20.976 1.00 21.84 C ANISOU 2606 CE1 HIS A 250 2648 2873 2776 30 66 59 C ATOM 2607 NE2 HIS A 250 -16.106 -0.993 20.053 1.00 20.08 N ANISOU 2607 NE2 HIS A 250 2439 2644 2545 35 82 67 N ATOM 2608 N ILE A 251 -11.424 2.948 17.414 1.00 18.28 N ANISOU 2608 N ILE A 251 2151 2377 2417 -24 174 114 N ATOM 2609 CA ILE A 251 -10.139 3.597 17.242 1.00 18.18 C ANISOU 2609 CA ILE A 251 2107 2366 2436 -49 192 127 C ATOM 2610 C ILE A 251 -10.325 5.092 16.972 1.00 19.11 C ANISOU 2610 C ILE A 251 2246 2456 2559 -78 184 140 C ATOM 2611 O ILE A 251 -9.593 5.931 17.501 1.00 19.24 O ANISOU 2611 O ILE A 251 2240 2462 2608 -106 173 143 O ATOM 2612 CB ILE A 251 -9.366 2.892 16.109 1.00 20.34 C ANISOU 2612 CB ILE A 251 2367 2658 2702 -44 240 137 C ATOM 2613 CG1 ILE A 251 -8.922 1.483 16.549 1.00 21.90 C ANISOU 2613 CG1 ILE A 251 2537 2875 2909 -13 242 121 C ATOM 2614 CG2 ILE A 251 -8.203 3.792 15.604 1.00 19.64 C ANISOU 2614 CG2 ILE A 251 2250 2574 2639 -79 268 157 C ATOM 2615 CD1 ILE A 251 -8.393 0.628 15.388 1.00 23.18 C ANISOU 2615 CD1 ILE A 251 2696 3054 3058 4 290 120 C ATOM 2616 N ILE A 252 -11.317 5.455 16.176 1.00 17.19 N ANISOU 2616 N ILE A 252 2048 2197 2288 -73 185 150 N ATOM 2617 CA ILE A 252 -11.580 6.881 15.981 1.00 18.38 C ANISOU 2617 CA ILE A 252 2225 2313 2447 -95 170 164 C ATOM 2618 C ILE A 252 -11.939 7.550 17.313 1.00 19.53 C ANISOU 2618 C ILE A 252 2368 2438 2614 -93 127 140 C ATOM 2619 O ILE A 252 -11.479 8.664 17.619 1.00 20.05 O ANISOU 2619 O ILE A 252 2434 2476 2709 -121 112 144 O ATOM 2620 CB ILE A 252 -12.696 7.069 14.928 1.00 18.46 C ANISOU 2620 CB ILE A 252 2284 2310 2419 -82 171 179 C ATOM 2621 CG1 ILE A 252 -12.200 6.722 13.520 1.00 21.62 C ANISOU 2621 CG1 ILE A 252 2695 2727 2793 -94 216 205 C ATOM 2622 CG2 ILE A 252 -13.231 8.503 14.931 1.00 18.92 C ANISOU 2622 CG2 ILE A 252 2375 2325 2489 -92 142 190 C ATOM 2623 CD1 ILE A 252 -13.366 6.581 12.499 1.00 23.88 C ANISOU 2623 CD1 ILE A 252 3029 3011 3032 -77 212 215 C ATOM 2624 N ASN A 253 -12.770 6.888 18.120 1.00 20.19 N ANISOU 2624 N ASN A 253 2451 2537 2683 -64 106 115 N ATOM 2625 CA ASN A 253 -13.094 7.427 19.439 1.00 20.10 C ANISOU 2625 CA ASN A 253 2436 2516 2686 -60 70 87 C ATOM 2626 C ASN A 253 -11.825 7.614 20.263 1.00 21.73 C ANISOU 2626 C ASN A 253 2606 2726 2924 -86 62 81 C ATOM 2627 O ASN A 253 -11.668 8.626 20.960 1.00 19.92 O ANISOU 2627 O ASN A 253 2381 2473 2716 -103 35 67 O ATOM 2628 CB ASN A 253 -14.079 6.503 20.167 1.00 16.95 C ANISOU 2628 CB ASN A 253 2036 2144 2260 -30 57 65 C ATOM 2629 CG ASN A 253 -15.483 6.601 19.618 1.00 17.11 C ANISOU 2629 CG ASN A 253 2087 2160 2255 -7 52 65 C ATOM 2630 OD1 ASN A 253 -15.868 7.610 18.953 1.00 19.95 O ANISOU 2630 OD1 ASN A 253 2474 2489 2619 -7 47 75 O ATOM 2631 ND2 ASN A 253 -16.289 5.587 19.917 1.00 16.38 N ANISOU 2631 ND2 ASN A 253 1991 2097 2137 12 50 54 N ATOM 2632 N CYS A 254 -10.885 6.662 20.172 1.00 18.09 N ANISOU 2632 N CYS A 254 2109 2294 2469 -90 82 90 N ATOM 2633 CA CYS A 254 -9.596 6.867 20.843 1.00 20.42 C ANISOU 2633 CA CYS A 254 2362 2596 2799 -116 72 88 C ATOM 2634 C CYS A 254 -8.867 8.129 20.360 1.00 20.83 C ANISOU 2634 C CYS A 254 2413 2620 2881 -158 77 105 C ATOM 2635 O CYS A 254 -8.328 8.885 21.171 1.00 21.96 O ANISOU 2635 O CYS A 254 2543 2749 3052 -185 49 93 O ATOM 2636 CB CYS A 254 -8.691 5.637 20.655 1.00 22.72 C ANISOU 2636 CB CYS A 254 2611 2923 3097 -106 95 97 C ATOM 2637 SG CYS A 254 -9.234 4.174 21.582 1.00 23.02 S ANISOU 2637 SG CYS A 254 2646 2987 3112 -67 76 81 S ATOM 2638 N PHE A 255 -8.832 8.383 19.049 1.00 19.63 N ANISOU 2638 N PHE A 255 2278 2458 2723 -169 112 133 N ATOM 2639 CA PHE A 255 -8.198 9.627 18.577 1.00 22.83 C ANISOU 2639 CA PHE A 255 2687 2832 3155 -216 116 155 C ATOM 2640 C PHE A 255 -8.924 10.863 19.108 1.00 24.28 C ANISOU 2640 C PHE A 255 2914 2964 3346 -223 75 142 C ATOM 2641 O PHE A 255 -8.289 11.816 19.593 1.00 23.43 O ANISOU 2641 O PHE A 255 2800 2829 3273 -261 53 138 O ATOM 2642 CB PHE A 255 -8.144 9.684 17.043 1.00 20.05 C ANISOU 2642 CB PHE A 255 2355 2481 2784 -227 161 193 C ATOM 2643 CG PHE A 255 -6.974 8.945 16.451 1.00 19.35 C ANISOU 2643 CG PHE A 255 2215 2435 2701 -240 207 208 C ATOM 2644 CD1 PHE A 255 -5.752 9.601 16.265 1.00 18.79 C ANISOU 2644 CD1 PHE A 255 2107 2368 2664 -291 224 230 C ATOM 2645 CD2 PHE A 255 -7.086 7.588 16.118 1.00 22.69 C ANISOU 2645 CD2 PHE A 255 2625 2896 3098 -200 234 199 C ATOM 2646 CE1 PHE A 255 -4.635 8.901 15.743 1.00 27.55 C ANISOU 2646 CE1 PHE A 255 3160 3526 3782 -299 271 241 C ATOM 2647 CE2 PHE A 255 -5.980 6.879 15.576 1.00 25.77 C ANISOU 2647 CE2 PHE A 255 2966 3327 3496 -203 279 208 C ATOM 2648 CZ PHE A 255 -4.750 7.540 15.418 1.00 24.96 C ANISOU 2648 CZ PHE A 255 2819 3235 3428 -251 299 227 C ATOM 2649 N THR A 256 -10.253 10.889 18.972 1.00 20.60 N ANISOU 2649 N THR A 256 2492 2483 2852 -186 64 132 N ATOM 2650 CA THR A 256 -11.027 12.004 19.489 1.00 19.23 C ANISOU 2650 CA THR A 256 2358 2261 2687 -180 26 113 C ATOM 2651 C THR A 256 -10.688 12.256 20.947 1.00 24.67 C ANISOU 2651 C THR A 256 3028 2949 3397 -187 -9 74 C ATOM 2652 O THR A 256 -10.461 13.398 21.338 1.00 23.43 O ANISOU 2652 O THR A 256 2888 2747 3267 -212 -37 63 O ATOM 2653 CB THR A 256 -12.521 11.716 19.344 1.00 18.82 C ANISOU 2653 CB THR A 256 2338 2212 2602 -129 18 100 C ATOM 2654 OG1 THR A 256 -12.811 11.527 17.958 1.00 22.83 O ANISOU 2654 OG1 THR A 256 2866 2719 3088 -126 45 137 O ATOM 2655 CG2 THR A 256 -13.374 12.874 19.892 1.00 19.85 C ANISOU 2655 CG2 THR A 256 2505 2293 2744 -113 -20 75 C ATOM 2656 N PHE A 257 -10.610 11.188 21.750 1.00 19.69 N ANISOU 2656 N PHE A 257 2364 2367 2751 -168 -11 53 N ATOM 2657 CA PHE A 257 -10.426 11.311 23.201 1.00 23.13 C ANISOU 2657 CA PHE A 257 2787 2810 3193 -170 -47 15 C ATOM 2658 C PHE A 257 -8.977 11.626 23.585 1.00 26.96 C ANISOU 2658 C PHE A 257 3234 3296 3715 -218 -59 19 C ATOM 2659 O PHE A 257 -8.715 12.533 24.380 1.00 24.41 O ANISOU 2659 O PHE A 257 2920 2945 3411 -241 -94 -6 O ATOM 2660 CB PHE A 257 -10.880 10.013 23.872 1.00 22.06 C ANISOU 2660 CB PHE A 257 2633 2725 3024 -135 -46 0 C ATOM 2661 CG PHE A 257 -10.735 10.023 25.367 1.00 24.84 C ANISOU 2661 CG PHE A 257 2974 3093 3371 -137 -82 -37 C ATOM 2662 CD1 PHE A 257 -11.543 10.838 26.161 1.00 24.81 C ANISOU 2662 CD1 PHE A 257 3002 3068 3355 -124 -108 -76 C ATOM 2663 CD2 PHE A 257 -9.785 9.203 25.981 1.00 25.27 C ANISOU 2663 CD2 PHE A 257 2986 3185 3429 -148 -90 -33 C ATOM 2664 CE1 PHE A 257 -11.403 10.835 27.580 1.00 26.52 C ANISOU 2664 CE1 PHE A 257 3213 3306 3557 -127 -140 -112 C ATOM 2665 CE2 PHE A 257 -9.635 9.176 27.396 1.00 28.77 C ANISOU 2665 CE2 PHE A 257 3423 3648 3859 -151 -127 -63 C ATOM 2666 CZ PHE A 257 -10.434 10.019 28.191 1.00 28.81 C ANISOU 2666 CZ PHE A 257 3464 3635 3847 -143 -152 -104 C ATOM 2667 N PHE A 258 -8.029 10.892 23.039 1.00 21.67 N ANISOU 2667 N PHE A 258 2521 2659 3056 -232 -31 47 N ATOM 2668 CA PHE A 258 -6.646 11.010 23.485 1.00 24.07 C ANISOU 2668 CA PHE A 258 2773 2976 3395 -274 -43 51 C ATOM 2669 C PHE A 258 -5.890 12.114 22.775 1.00 27.15 C ANISOU 2669 C PHE A 258 3162 3331 3822 -328 -34 76 C ATOM 2670 O PHE A 258 -4.827 12.530 23.256 1.00 27.29 O ANISOU 2670 O PHE A 258 3143 3351 3875 -373 -54 73 O ATOM 2671 CB PHE A 258 -5.904 9.678 23.251 1.00 20.29 C ANISOU 2671 CB PHE A 258 2240 2553 2917 -259 -16 68 C ATOM 2672 CG PHE A 258 -6.285 8.596 24.198 1.00 23.65 C ANISOU 2672 CG PHE A 258 2658 3012 3316 -219 -36 48 C ATOM 2673 CD1 PHE A 258 -6.166 8.800 25.579 1.00 25.72 C ANISOU 2673 CD1 PHE A 258 2915 3279 3577 -226 -84 18 C ATOM 2674 CD2 PHE A 258 -6.718 7.341 23.715 1.00 18.49 C ANISOU 2674 CD2 PHE A 258 2004 2384 2637 -178 -7 59 C ATOM 2675 CE1 PHE A 258 -6.498 7.788 26.480 1.00 20.39 C ANISOU 2675 CE1 PHE A 258 2236 2637 2873 -194 -103 5 C ATOM 2676 CE2 PHE A 258 -7.065 6.308 24.602 1.00 20.95 C ANISOU 2676 CE2 PHE A 258 2313 2723 2925 -146 -27 45 C ATOM 2677 CZ PHE A 258 -6.954 6.532 25.996 1.00 22.55 C ANISOU 2677 CZ PHE A 258 2511 2934 3125 -155 -74 21 C ATOM 2678 N CYS A 259 -6.394 12.605 21.641 1.00 24.27 N ANISOU 2678 N CYS A 259 2837 2934 3450 -331 -7 102 N ATOM 2679 CA CYS A 259 -5.689 13.630 20.864 1.00 29.57 C ANISOU 2679 CA CYS A 259 3511 3571 4152 -389 5 135 C ATOM 2680 C CYS A 259 -6.604 14.822 20.622 1.00 28.58 C ANISOU 2680 C CYS A 259 3459 3376 4026 -390 -17 135 C ATOM 2681 O CYS A 259 -7.020 15.076 19.487 1.00 24.46 O ANISOU 2681 O CYS A 259 2971 2833 3490 -389 9 169 O ATOM 2682 CB CYS A 259 -5.161 13.080 19.535 1.00 30.02 C ANISOU 2682 CB CYS A 259 3542 3661 4201 -399 64 179 C ATOM 2683 SG CYS A 259 -4.027 14.338 18.745 1.00 36.01 S ANISOU 2683 SG CYS A 259 4291 4389 5001 -487 81 225 S ATOM 2684 N PRO A 260 -6.906 15.594 21.671 1.00 29.24 N ANISOU 2684 N PRO A 260 3568 3419 4124 -392 -66 95 N ATOM 2685 CA PRO A 260 -7.705 16.821 21.497 1.00 35.86 C ANISOU 2685 CA PRO A 260 4474 4180 4969 -390 -91 91 C ATOM 2686 C PRO A 260 -7.029 17.880 20.639 1.00 36.63 C ANISOU 2686 C PRO A 260 4591 4226 5100 -454 -86 135 C ATOM 2687 O PRO A 260 -7.706 18.836 20.248 1.00 39.00 O ANISOU 2687 O PRO A 260 4953 4458 5406 -450 -103 144 O ATOM 2688 CB PRO A 260 -7.870 17.340 22.939 1.00 39.67 C ANISOU 2688 CB PRO A 260 4970 4640 5463 -384 -143 32 C ATOM 2689 CG PRO A 260 -6.597 16.845 23.628 1.00 35.86 C ANISOU 2689 CG PRO A 260 4422 4205 4997 -424 -150 25 C ATOM 2690 CD PRO A 260 -6.384 15.462 23.048 1.00 30.62 C ANISOU 2690 CD PRO A 260 3710 3614 4310 -400 -103 54 C ATOM 2691 N ASP A 261 -5.720 17.771 20.392 1.00 32.56 N ANISOU 2691 N ASP A 261 4023 3739 4610 -514 -65 164 N ATOM 2692 CA ASP A 261 -5.013 18.653 19.463 1.00 32.12 C ANISOU 2692 CA ASP A 261 3978 3646 4582 -583 -49 215 C ATOM 2693 C ASP A 261 -5.150 18.229 18.003 1.00 32.95 C ANISOU 2693 C ASP A 261 4089 3775 4656 -578 8 270 C ATOM 2694 O ASP A 261 -4.715 18.974 17.117 1.00 32.32 O ANISOU 2694 O ASP A 261 4028 3664 4588 -634 25 320 O ATOM 2695 CB ASP A 261 -3.527 18.713 19.799 1.00 36.40 C ANISOU 2695 CB ASP A 261 4450 4215 5163 -653 -48 223 C ATOM 2696 CG ASP A 261 -3.266 19.349 21.132 1.00 52.98 C ANISOU 2696 CG ASP A 261 6552 6283 7296 -676 -109 175 C ATOM 2697 OD1 ASP A 261 -4.160 20.074 21.619 1.00 56.99 O ANISOU 2697 OD1 ASP A 261 7127 6726 7802 -651 -150 142 O ATOM 2698 OD2 ASP A 261 -2.168 19.124 21.693 1.00 59.26 O ANISOU 2698 OD2 ASP A 261 7281 7118 8118 -717 -118 167 O ATOM 2699 N CYS A 262 -5.679 17.037 17.735 1.00 30.38 N ANISOU 2699 N CYS A 262 3748 3507 4288 -518 37 263 N ATOM 2700 CA CYS A 262 -5.895 16.554 16.372 1.00 31.18 C ANISOU 2700 CA CYS A 262 3860 3634 4351 -508 89 307 C ATOM 2701 C CYS A 262 -7.277 16.984 15.906 1.00 32.91 C ANISOU 2701 C CYS A 262 4157 3806 4543 -465 70 312 C ATOM 2702 O CYS A 262 -8.237 16.928 16.675 1.00 29.34 O ANISOU 2702 O CYS A 262 3727 3337 4085 -413 34 270 O ATOM 2703 CB CYS A 262 -5.826 15.022 16.302 1.00 31.64 C ANISOU 2703 CB CYS A 262 3869 3773 4379 -462 126 292 C ATOM 2704 SG CYS A 262 -4.233 14.205 16.732 1.00 40.64 S ANISOU 2704 SG CYS A 262 4907 4985 5548 -492 153 286 S ATOM 2705 N SER A 263 -7.385 17.384 14.642 1.00 26.03 N ANISOU 2705 N SER A 263 3323 2915 3651 -487 94 365 N ATOM 2706 CA SER A 263 -8.705 17.648 14.089 1.00 28.87 C ANISOU 2706 CA SER A 263 3750 3238 3980 -440 76 375 C ATOM 2707 C SER A 263 -9.599 16.415 14.201 1.00 23.09 C ANISOU 2707 C SER A 263 3005 2560 3208 -369 84 342 C ATOM 2708 O SER A 263 -9.147 15.276 14.014 1.00 25.61 O ANISOU 2708 O SER A 263 3277 2946 3506 -362 124 338 O ATOM 2709 CB SER A 263 -8.573 18.079 12.627 1.00 37.10 C ANISOU 2709 CB SER A 263 4832 4268 4997 -477 106 443 C ATOM 2710 OG SER A 263 -8.008 19.384 12.569 1.00 46.17 O ANISOU 2710 OG SER A 263 6008 5349 6185 -542 86 476 O ATOM 2711 N HIS A 264 -10.885 16.639 14.504 1.00 25.13 N ANISOU 2711 N HIS A 264 3304 2787 3458 -315 45 318 N ATOM 2712 CA HIS A 264 -11.810 15.514 14.631 1.00 26.83 C ANISOU 2712 CA HIS A 264 3507 3051 3637 -253 50 289 C ATOM 2713 C HIS A 264 -11.880 14.750 13.303 1.00 27.27 C ANISOU 2713 C HIS A 264 3569 3149 3645 -251 92 326 C ATOM 2714 O HIS A 264 -11.888 15.361 12.236 1.00 30.06 O ANISOU 2714 O HIS A 264 3962 3476 3982 -274 100 374 O ATOM 2715 CB HIS A 264 -13.208 16.028 15.013 1.00 25.69 C ANISOU 2715 CB HIS A 264 3403 2866 3491 -200 4 264 C ATOM 2716 CG HIS A 264 -14.130 14.964 15.536 1.00 27.65 C ANISOU 2716 CG HIS A 264 3628 3164 3713 -143 1 223 C ATOM 2717 ND1 HIS A 264 -14.618 13.942 14.743 1.00 25.04 N ANISOU 2717 ND1 HIS A 264 3294 2881 3340 -121 26 237 N ATOM 2718 CD2 HIS A 264 -14.649 14.763 16.775 1.00 25.01 C ANISOU 2718 CD2 HIS A 264 3276 2841 3388 -109 -22 171 C ATOM 2719 CE1 HIS A 264 -15.399 13.166 15.470 1.00 23.35 C ANISOU 2719 CE1 HIS A 264 3059 2700 3112 -79 16 197 C ATOM 2720 NE2 HIS A 264 -15.434 13.640 16.704 1.00 25.05 N ANISOU 2720 NE2 HIS A 264 3263 2897 3356 -71 -10 158 N ATOM 2721 N ALA A 265 -11.950 13.414 13.364 1.00 23.51 N ANISOU 2721 N ALA A 265 3058 2735 3142 -223 117 304 N ATOM 2722 CA ALA A 265 -12.237 12.612 12.174 1.00 22.11 C ANISOU 2722 CA ALA A 265 2893 2595 2913 -210 150 327 C ATOM 2723 C ALA A 265 -13.391 13.282 11.442 1.00 22.97 C ANISOU 2723 C ALA A 265 3062 2666 2999 -190 121 351 C ATOM 2724 O ALA A 265 -14.333 13.748 12.092 1.00 24.03 O ANISOU 2724 O ALA A 265 3213 2768 3149 -156 76 328 O ATOM 2725 CB ALA A 265 -12.624 11.160 12.514 1.00 25.89 C ANISOU 2725 CB ALA A 265 3342 3127 3369 -169 161 290 C ATOM 2726 N PRO A 266 -13.328 13.403 10.118 1.00 25.76 N ANISOU 2726 N PRO A 266 3450 3024 3315 -210 143 397 N ATOM 2727 CA PRO A 266 -14.391 14.106 9.382 1.00 27.16 C ANISOU 2727 CA PRO A 266 3688 3162 3470 -191 109 426 C ATOM 2728 C PRO A 266 -15.704 13.330 9.416 1.00 25.63 C ANISOU 2728 C PRO A 266 3496 2994 3247 -133 85 397 C ATOM 2729 O PRO A 266 -15.753 12.123 9.642 1.00 21.93 O ANISOU 2729 O PRO A 266 2994 2577 2761 -115 105 366 O ATOM 2730 CB PRO A 266 -13.855 14.222 7.946 1.00 28.56 C ANISOU 2730 CB PRO A 266 3897 3353 3603 -232 146 484 C ATOM 2731 CG PRO A 266 -12.797 13.200 7.820 1.00 29.96 C ANISOU 2731 CG PRO A 266 4025 3591 3765 -254 206 472 C ATOM 2732 CD PRO A 266 -12.255 12.891 9.250 1.00 27.46 C ANISOU 2732 CD PRO A 266 3648 3281 3503 -248 203 424 C ATOM 2733 N LEU A 267 -16.778 14.060 9.186 1.00 24.34 N ANISOU 2733 N LEU A 267 3374 2792 3083 -105 39 410 N ATOM 2734 CA LEU A 267 -18.106 13.471 9.267 1.00 30.41 C ANISOU 2734 CA LEU A 267 4140 3584 3831 -51 10 383 C ATOM 2735 C LEU A 267 -18.254 12.261 8.342 1.00 25.75 C ANISOU 2735 C LEU A 267 3550 3052 3182 -51 38 389 C ATOM 2736 O LEU A 267 -18.869 11.251 8.722 1.00 24.18 O ANISOU 2736 O LEU A 267 3324 2893 2972 -22 35 352 O ATOM 2737 CB LEU A 267 -19.140 14.539 8.918 1.00 43.20 C ANISOU 2737 CB LEU A 267 5804 5152 5457 -22 -44 406 C ATOM 2738 CG LEU A 267 -20.589 14.174 9.138 1.00 57.26 C ANISOU 2738 CG LEU A 267 7574 6951 7230 36 -82 377 C ATOM 2739 CD1 LEU A 267 -20.800 14.246 10.627 1.00 63.78 C ANISOU 2739 CD1 LEU A 267 8360 7772 8102 63 -93 322 C ATOM 2740 CD2 LEU A 267 -21.482 15.156 8.399 1.00 61.91 C ANISOU 2740 CD2 LEU A 267 8212 7496 7816 63 -132 414 C ATOM 2741 N TRP A 268 -17.729 12.344 7.118 1.00 26.70 N ANISOU 2741 N TRP A 268 3704 3180 3262 -84 64 434 N ATOM 2742 CA TRP A 268 -17.931 11.216 6.207 1.00 27.21 C ANISOU 2742 CA TRP A 268 3776 3298 3266 -80 88 433 C ATOM 2743 C TRP A 268 -17.269 9.951 6.742 1.00 25.37 C ANISOU 2743 C TRP A 268 3493 3111 3036 -82 131 391 C ATOM 2744 O TRP A 268 -17.795 8.846 6.559 1.00 21.55 O ANISOU 2744 O TRP A 268 3003 2664 2521 -61 133 365 O ATOM 2745 CB TRP A 268 -17.422 11.550 4.816 1.00 22.13 C ANISOU 2745 CB TRP A 268 3179 2658 2571 -118 114 487 C ATOM 2746 CG TRP A 268 -15.914 11.756 4.706 1.00 26.64 C ANISOU 2746 CG TRP A 268 3735 3234 3153 -169 171 507 C ATOM 2747 CD1 TRP A 268 -15.248 12.952 4.703 1.00 29.20 C ANISOU 2747 CD1 TRP A 268 4075 3513 3506 -208 172 547 C ATOM 2748 CD2 TRP A 268 -14.912 10.741 4.574 1.00 27.12 C ANISOU 2748 CD2 TRP A 268 3759 3347 3197 -186 234 486 C ATOM 2749 NE1 TRP A 268 -13.896 12.740 4.589 1.00 26.12 N ANISOU 2749 NE1 TRP A 268 3654 3151 3118 -252 233 554 N ATOM 2750 CE2 TRP A 268 -13.663 11.393 4.500 1.00 29.14 C ANISOU 2750 CE2 TRP A 268 4003 3595 3473 -235 272 516 C ATOM 2751 CE3 TRP A 268 -14.949 9.337 4.518 1.00 28.20 C ANISOU 2751 CE3 TRP A 268 3873 3535 3307 -162 259 445 C ATOM 2752 CZ2 TRP A 268 -12.463 10.697 4.362 1.00 29.75 C ANISOU 2752 CZ2 TRP A 268 4038 3719 3545 -258 337 505 C ATOM 2753 CZ3 TRP A 268 -13.752 8.648 4.398 1.00 33.06 C ANISOU 2753 CZ3 TRP A 268 4454 4189 3919 -181 322 432 C ATOM 2754 CH2 TRP A 268 -12.527 9.331 4.318 1.00 32.47 C ANISOU 2754 CH2 TRP A 268 4360 4112 3865 -227 361 462 C ATOM 2755 N LEU A 269 -16.137 10.093 7.426 1.00 22.35 N ANISOU 2755 N LEU A 269 3075 2723 2693 -106 160 383 N ATOM 2756 CA LEU A 269 -15.487 8.921 8.010 1.00 20.80 C ANISOU 2756 CA LEU A 269 2831 2567 2505 -103 194 345 C ATOM 2757 C LEU A 269 -16.245 8.392 9.220 1.00 20.09 C ANISOU 2757 C LEU A 269 2711 2480 2442 -67 162 300 C ATOM 2758 O LEU A 269 -16.293 7.176 9.434 1.00 23.78 O ANISOU 2758 O LEU A 269 3156 2981 2897 -51 175 271 O ATOM 2759 CB LEU A 269 -14.045 9.269 8.399 1.00 21.07 C ANISOU 2759 CB LEU A 269 2830 2598 2576 -139 230 352 C ATOM 2760 CG LEU A 269 -13.228 8.127 8.971 1.00 23.19 C ANISOU 2760 CG LEU A 269 3045 2906 2859 -133 263 317 C ATOM 2761 CD1 LEU A 269 -13.136 6.966 7.949 1.00 27.49 C ANISOU 2761 CD1 LEU A 269 3600 3494 3351 -124 303 312 C ATOM 2762 CD2 LEU A 269 -11.804 8.653 9.392 1.00 21.60 C ANISOU 2762 CD2 LEU A 269 2803 2702 2701 -172 290 328 C ATOM 2763 N MET A 270 -16.783 9.277 10.070 1.00 23.03 N ANISOU 2763 N MET A 270 3081 2817 2851 -54 121 293 N ATOM 2764 CA MET A 270 -17.639 8.809 11.162 1.00 22.52 C ANISOU 2764 CA MET A 270 2991 2762 2802 -20 92 251 C ATOM 2765 C MET A 270 -18.753 7.909 10.638 1.00 21.57 C ANISOU 2765 C MET A 270 2883 2673 2642 5 80 243 C ATOM 2766 O MET A 270 -19.040 6.844 11.201 1.00 22.04 O ANISOU 2766 O MET A 270 2915 2761 2697 18 83 213 O ATOM 2767 CB MET A 270 -18.281 9.990 11.926 1.00 18.55 C ANISOU 2767 CB MET A 270 2494 2218 2334 -2 50 244 C ATOM 2768 CG MET A 270 -17.291 11.017 12.575 1.00 21.92 C ANISOU 2768 CG MET A 270 2916 2606 2807 -29 50 247 C ATOM 2769 SD MET A 270 -16.041 10.189 13.614 1.00 23.08 S ANISOU 2769 SD MET A 270 3008 2784 2976 -50 81 218 S ATOM 2770 CE MET A 270 -17.009 9.262 14.816 1.00 20.57 C ANISOU 2770 CE MET A 270 2662 2500 2655 -10 61 170 C ATOM 2771 N TYR A 271 -19.441 8.360 9.599 1.00 19.10 N ANISOU 2771 N TYR A 271 2608 2349 2299 10 61 270 N ATOM 2772 CA TYR A 271 -20.598 7.604 9.134 1.00 19.57 C ANISOU 2772 CA TYR A 271 2676 2436 2322 32 40 261 C ATOM 2773 C TYR A 271 -20.163 6.365 8.380 1.00 19.66 C ANISOU 2773 C TYR A 271 2694 2484 2292 17 75 257 C ATOM 2774 O TYR A 271 -20.840 5.336 8.440 1.00 24.36 O ANISOU 2774 O TYR A 271 3280 3105 2869 29 66 233 O ATOM 2775 CB TYR A 271 -21.522 8.529 8.317 1.00 21.47 C ANISOU 2775 CB TYR A 271 2955 2655 2547 46 -1 292 C ATOM 2776 CG TYR A 271 -22.293 9.390 9.313 1.00 27.74 C ANISOU 2776 CG TYR A 271 3731 3423 3387 78 -41 276 C ATOM 2777 CD1 TYR A 271 -23.341 8.847 10.056 1.00 30.70 C ANISOU 2777 CD1 TYR A 271 4070 3825 3769 107 -63 240 C ATOM 2778 CD2 TYR A 271 -21.917 10.704 9.594 1.00 31.12 C ANISOU 2778 CD2 TYR A 271 4174 3799 3851 77 -52 292 C ATOM 2779 CE1 TYR A 271 -24.006 9.597 11.026 1.00 27.53 C ANISOU 2779 CE1 TYR A 271 3647 3407 3408 140 -91 219 C ATOM 2780 CE2 TYR A 271 -22.588 11.460 10.561 1.00 32.62 C ANISOU 2780 CE2 TYR A 271 4348 3964 4083 111 -86 268 C ATOM 2781 CZ TYR A 271 -23.625 10.892 11.277 1.00 33.54 C ANISOU 2781 CZ TYR A 271 4426 4114 4203 144 -103 229 C ATOM 2782 OH TYR A 271 -24.290 11.624 12.248 1.00 30.11 O ANISOU 2782 OH TYR A 271 3973 3661 3806 181 -130 200 O ATOM 2783 N LEU A 272 -19.010 6.420 7.719 1.00 20.09 N ANISOU 2783 N LEU A 272 2762 2539 2333 -10 117 277 N ATOM 2784 CA LEU A 272 -18.480 5.204 7.130 1.00 21.25 C ANISOU 2784 CA LEU A 272 2911 2719 2445 -18 156 263 C ATOM 2785 C LEU A 272 -18.190 4.174 8.216 1.00 23.03 C ANISOU 2785 C LEU A 272 3092 2958 2700 -7 167 223 C ATOM 2786 O LEU A 272 -18.532 3.000 8.072 1.00 21.59 O ANISOU 2786 O LEU A 272 2912 2796 2495 2 169 200 O ATOM 2787 CB LEU A 272 -17.222 5.533 6.327 1.00 24.03 C ANISOU 2787 CB LEU A 272 3275 3074 2780 -47 206 290 C ATOM 2788 CG LEU A 272 -16.571 4.343 5.641 1.00 31.80 C ANISOU 2788 CG LEU A 272 4262 4093 3728 -50 253 272 C ATOM 2789 CD1 LEU A 272 -17.591 3.698 4.668 1.00 35.22 C ANISOU 2789 CD1 LEU A 272 4739 4544 4100 -40 233 266 C ATOM 2790 CD2 LEU A 272 -15.271 4.827 4.901 1.00 31.68 C ANISOU 2790 CD2 LEU A 272 4250 4088 3699 -81 309 300 C ATOM 2791 N ALA A 273 -17.574 4.600 9.323 1.00 21.00 N ANISOU 2791 N ALA A 273 2800 2687 2493 -10 170 217 N ATOM 2792 CA ALA A 273 -17.274 3.638 10.394 1.00 21.14 C ANISOU 2792 CA ALA A 273 2778 2717 2536 0 175 185 C ATOM 2793 C ALA A 273 -18.544 3.106 11.053 1.00 18.96 C ANISOU 2793 C ALA A 273 2496 2448 2258 20 138 163 C ATOM 2794 O ALA A 273 -18.603 1.931 11.470 1.00 18.22 O ANISOU 2794 O ALA A 273 2389 2370 2163 26 141 140 O ATOM 2795 CB ALA A 273 -16.363 4.279 11.439 1.00 18.41 C ANISOU 2795 CB ALA A 273 2398 2358 2240 -9 180 183 C ATOM 2796 N ILE A 274 -19.559 3.960 11.202 1.00 20.45 N ANISOU 2796 N ILE A 274 2693 2627 2451 30 102 169 N ATOM 2797 CA ILE A 274 -20.836 3.497 11.751 1.00 18.33 C ANISOU 2797 CA ILE A 274 2413 2373 2179 46 69 149 C ATOM 2798 C ILE A 274 -21.470 2.466 10.827 1.00 18.27 C ANISOU 2798 C ILE A 274 2426 2386 2129 44 66 146 C ATOM 2799 O ILE A 274 -22.001 1.447 11.272 1.00 21.45 O ANISOU 2799 O ILE A 274 2815 2806 2528 45 57 126 O ATOM 2800 CB ILE A 274 -21.775 4.697 11.973 1.00 19.67 C ANISOU 2800 CB ILE A 274 2582 2528 2362 64 33 155 C ATOM 2801 CG1 ILE A 274 -21.290 5.570 13.143 1.00 20.62 C ANISOU 2801 CG1 ILE A 274 2681 2628 2526 67 31 146 C ATOM 2802 CG2 ILE A 274 -23.253 4.227 12.157 1.00 18.33 C ANISOU 2802 CG2 ILE A 274 2400 2384 2180 80 1 140 C ATOM 2803 CD1 ILE A 274 -21.963 6.956 13.145 1.00 20.22 C ANISOU 2803 CD1 ILE A 274 2643 2549 2492 87 -1 153 C ATOM 2804 N AVAL A 275 -21.461 2.750 9.526 0.43 21.11 N ANISOU 2804 N AVAL A 275 2824 2743 2455 38 69 168 N ATOM 2805 N BVAL A 275 -21.465 2.719 9.517 0.57 21.24 N ANISOU 2805 N BVAL A 275 2840 2760 2470 38 69 167 N ATOM 2806 CA AVAL A 275 -22.048 1.826 8.565 0.43 21.28 C ANISOU 2806 CA AVAL A 275 2872 2783 2431 34 62 162 C ATOM 2807 CA BVAL A 275 -22.134 1.736 8.668 0.57 21.11 C ANISOU 2807 CA BVAL A 275 2847 2763 2411 35 60 159 C ATOM 2808 C AVAL A 275 -21.312 0.496 8.597 0.43 20.90 C ANISOU 2808 C AVAL A 275 2822 2743 2375 27 95 139 C ATOM 2809 C BVAL A 275 -21.314 0.457 8.588 0.57 20.89 C ANISOU 2809 C BVAL A 275 2822 2743 2374 27 95 138 C ATOM 2810 O AVAL A 275 -21.931 -0.575 8.561 0.43 19.83 O ANISOU 2810 O AVAL A 275 2692 2619 2225 25 81 119 O ATOM 2811 O BVAL A 275 -21.885 -0.631 8.454 0.57 19.96 O ANISOU 2811 O BVAL A 275 2711 2635 2236 24 84 119 O ATOM 2812 CB AVAL A 275 -22.044 2.456 7.158 0.43 22.85 C ANISOU 2812 CB AVAL A 275 3117 2979 2588 28 61 192 C ATOM 2813 CB BVAL A 275 -22.467 2.281 7.257 0.57 22.88 C ANISOU 2813 CB BVAL A 275 3116 2987 2590 31 48 186 C ATOM 2814 CG1AVAL A 275 -22.180 1.392 6.087 0.43 20.39 C ANISOU 2814 CG1AVAL A 275 2838 2687 2222 18 69 181 C ATOM 2815 CG1BVAL A 275 -23.446 3.456 7.347 0.57 21.07 C ANISOU 2815 CG1BVAL A 275 2885 2748 2374 47 3 206 C ATOM 2816 CG2AVAL A 275 -23.164 3.507 7.042 0.43 22.71 C ANISOU 2816 CG2AVAL A 275 3104 2954 2573 42 12 212 C ATOM 2817 CG2BVAL A 275 -21.201 2.646 6.457 0.57 21.03 C ANISOU 2817 CG2BVAL A 275 2908 2746 2338 16 92 207 C ATOM 2818 N LEU A 276 -19.981 0.546 8.695 1.00 21.66 N ANISOU 2818 N LEU A 276 2911 2832 2488 23 136 141 N ATOM 2819 CA LEU A 276 -19.174 -0.682 8.723 1.00 24.95 C ANISOU 2819 CA LEU A 276 3323 3253 2903 24 168 118 C ATOM 2820 C LEU A 276 -19.497 -1.546 9.959 1.00 18.47 C ANISOU 2820 C LEU A 276 2474 2431 2113 30 150 97 C ATOM 2821 O LEU A 276 -19.623 -2.769 9.866 1.00 19.81 O ANISOU 2821 O LEU A 276 2655 2601 2271 31 150 76 O ATOM 2822 CB LEU A 276 -17.685 -0.323 8.702 1.00 21.90 C ANISOU 2822 CB LEU A 276 2920 2864 2536 21 213 127 C ATOM 2823 CG LEU A 276 -16.729 -1.514 8.917 1.00 27.63 C ANISOU 2823 CG LEU A 276 3630 3593 3275 32 245 102 C ATOM 2824 CD1 LEU A 276 -16.849 -2.604 7.778 1.00 25.82 C ANISOU 2824 CD1 LEU A 276 3442 3371 2998 37 262 81 C ATOM 2825 CD2 LEU A 276 -15.296 -1.017 9.056 1.00 24.85 C ANISOU 2825 CD2 LEU A 276 3246 3244 2951 29 285 112 C ATOM 2826 N ALA A 277 -19.590 -0.922 11.128 1.00 18.91 N ANISOU 2826 N ALA A 277 2497 2484 2206 33 134 101 N ATOM 2827 CA ALA A 277 -20.028 -1.629 12.320 1.00 18.49 C ANISOU 2827 CA ALA A 277 2419 2434 2172 34 115 86 C ATOM 2828 C ALA A 277 -21.392 -2.300 12.084 1.00 18.79 C ANISOU 2828 C ALA A 277 2471 2483 2184 28 85 78 C ATOM 2829 O ALA A 277 -21.582 -3.477 12.411 1.00 20.82 O ANISOU 2829 O ALA A 277 2730 2740 2440 21 80 64 O ATOM 2830 CB ALA A 277 -20.100 -0.646 13.515 1.00 16.47 C ANISOU 2830 CB ALA A 277 2131 2178 1949 37 101 90 C ATOM 2831 N HIS A 278 -22.344 -1.573 11.494 1.00 18.36 N ANISOU 2831 N HIS A 278 2427 2438 2112 28 62 87 N ATOM 2832 CA HIS A 278 -23.662 -2.183 11.242 1.00 20.24 C ANISOU 2832 CA HIS A 278 2670 2692 2328 19 30 80 C ATOM 2833 C HIS A 278 -23.568 -3.376 10.271 1.00 21.08 C ANISOU 2833 C HIS A 278 2815 2794 2401 7 36 68 C ATOM 2834 O HIS A 278 -24.299 -4.364 10.424 1.00 21.32 O ANISOU 2834 O HIS A 278 2847 2830 2425 -8 16 55 O ATOM 2835 CB HIS A 278 -24.628 -1.113 10.716 1.00 19.79 C ANISOU 2835 CB HIS A 278 2615 2646 2259 27 1 94 C ATOM 2836 CG HIS A 278 -24.972 -0.070 11.729 1.00 19.13 C ANISOU 2836 CG HIS A 278 2495 2565 2209 43 -11 97 C ATOM 2837 ND1 HIS A 278 -25.575 1.118 11.402 1.00 22.36 N ANISOU 2837 ND1 HIS A 278 2904 2973 2620 60 -34 111 N ATOM 2838 CD2 HIS A 278 -24.837 -0.064 13.084 1.00 24.20 C ANISOU 2838 CD2 HIS A 278 3102 3211 2880 46 -5 86 C ATOM 2839 CE1 HIS A 278 -25.782 1.827 12.505 1.00 25.71 C ANISOU 2839 CE1 HIS A 278 3295 3398 3077 76 -40 103 C ATOM 2840 NE2 HIS A 278 -25.335 1.133 13.541 1.00 21.87 N ANISOU 2840 NE2 HIS A 278 2788 2918 2605 65 -21 88 N ATOM 2841 N ATHR A 279 -22.675 -3.298 9.282 0.57 21.06 N ANISOU 2841 N ATHR A 279 2843 2782 2378 12 65 70 N ATOM 2842 N BTHR A 279 -22.674 -3.312 9.268 0.43 21.27 N ANISOU 2842 N BTHR A 279 2869 2808 2403 11 65 70 N ATOM 2843 CA ATHR A 279 -22.529 -4.350 8.279 0.57 22.14 C ANISOU 2843 CA ATHR A 279 3021 2914 2478 5 74 52 C ATOM 2844 CA BTHR A 279 -22.605 -4.400 8.286 0.43 21.80 C ANISOU 2844 CA BTHR A 279 2978 2871 2433 4 72 51 C ATOM 2845 C ATHR A 279 -22.153 -5.682 8.910 0.57 22.42 C ANISOU 2845 C ATHR A 279 3054 2933 2532 3 83 29 C ATOM 2846 C BTHR A 279 -22.165 -5.708 8.917 0.43 22.44 C ANISOU 2846 C BTHR A 279 3057 2935 2535 3 82 28 C ATOM 2847 O ATHR A 279 -22.452 -6.732 8.342 0.57 23.45 O ANISOU 2847 O ATHR A 279 3217 3054 2638 -6 74 8 O ATOM 2848 O BTHR A 279 -22.380 -6.767 8.326 0.43 23.63 O ANISOU 2848 O BTHR A 279 3240 3076 2661 -5 77 7 O ATOM 2849 CB ATHR A 279 -21.463 -3.930 7.241 0.57 21.14 C ANISOU 2849 CB ATHR A 279 2921 2786 2326 12 114 58 C ATOM 2850 CB BTHR A 279 -21.631 -4.120 7.113 0.43 21.48 C ANISOU 2850 CB BTHR A 279 2970 2829 2362 10 110 54 C ATOM 2851 OG1ATHR A 279 -21.876 -2.733 6.594 0.57 24.49 O ANISOU 2851 OG1ATHR A 279 3356 3220 2728 10 101 84 O ATOM 2852 OG1BTHR A 279 -20.282 -3.995 7.589 0.43 19.64 O ANISOU 2852 OG1BTHR A 279 2715 2587 2160 23 152 55 O ATOM 2853 CG2ATHR A 279 -21.244 -4.972 6.177 0.57 17.44 C ANISOU 2853 CG2ATHR A 279 2498 2315 1815 10 130 32 C ATOM 2854 CG2BTHR A 279 -22.031 -2.911 6.307 0.43 23.61 C ANISOU 2854 CG2BTHR A 279 3256 3112 2604 8 97 81 C ATOM 2855 N ASN A 280 -21.534 -5.663 10.087 1.00 20.91 N ANISOU 2855 N ASN A 280 2828 2734 2384 12 94 33 N ATOM 2856 CA ASN A 280 -21.222 -6.910 10.773 1.00 23.36 C ANISOU 2856 CA ASN A 280 3137 3025 2714 12 95 17 C ATOM 2857 C ASN A 280 -22.476 -7.742 11.044 1.00 23.91 C ANISOU 2857 C ASN A 280 3215 3095 2776 -13 57 12 C ATOM 2858 O ASN A 280 -22.403 -8.974 11.100 1.00 24.44 O ANISOU 2858 O ASN A 280 3304 3138 2844 -20 52 -4 O ATOM 2859 CB ASN A 280 -20.524 -6.662 12.098 1.00 19.82 C ANISOU 2859 CB ASN A 280 2649 2574 2309 21 103 28 C ATOM 2860 CG ASN A 280 -20.021 -7.982 12.709 1.00 25.67 C ANISOU 2860 CG ASN A 280 3394 3290 3070 26 104 17 C ATOM 2861 OD1 ASN A 280 -19.185 -8.678 12.110 1.00 28.70 O ANISOU 2861 OD1 ASN A 280 3799 3654 3453 43 126 0 O ATOM 2862 ND2 ASN A 280 -20.574 -8.360 13.830 1.00 21.67 N ANISOU 2862 ND2 ASN A 280 2871 2783 2579 11 78 25 N ATOM 2863 N SER A 281 -23.620 -7.086 11.233 1.00 18.91 N ANISOU 2863 N SER A 281 2561 2487 2135 -27 29 24 N ATOM 2864 CA SER A 281 -24.878 -7.791 11.470 1.00 24.85 C ANISOU 2864 CA SER A 281 3312 3249 2881 -57 -7 20 C ATOM 2865 C SER A 281 -25.387 -8.517 10.229 1.00 24.34 C ANISOU 2865 C SER A 281 3292 3177 2779 -73 -24 4 C ATOM 2866 O SER A 281 -26.389 -9.216 10.321 1.00 27.08 O ANISOU 2866 O SER A 281 3640 3529 3120 -104 -56 -1 O ATOM 2867 CB SER A 281 -25.938 -6.798 11.991 1.00 21.09 C ANISOU 2867 CB SER A 281 2793 2809 2410 -61 -29 35 C ATOM 2868 OG SER A 281 -25.573 -6.388 13.324 1.00 23.11 O ANISOU 2868 OG SER A 281 3012 3071 2698 -52 -17 44 O ATOM 2869 N VAL A 282 -24.728 -8.357 9.079 1.00 24.00 N ANISOU 2869 N VAL A 282 3286 3126 2709 -57 -4 -6 N ATOM 2870 CA VAL A 282 -25.106 -9.008 7.823 1.00 23.61 C ANISOU 2870 CA VAL A 282 3285 3070 2615 -71 -18 -27 C ATOM 2871 C VAL A 282 -24.259 -10.254 7.609 1.00 26.60 C ANISOU 2871 C VAL A 282 3703 3410 2994 -65 3 -56 C ATOM 2872 O VAL A 282 -24.720 -11.210 6.977 1.00 27.53 O ANISOU 2872 O VAL A 282 3862 3511 3087 -84 -18 -80 O ATOM 2873 CB VAL A 282 -24.946 -8.050 6.617 1.00 22.23 C ANISOU 2873 CB VAL A 282 3133 2914 2400 -58 -9 -20 C ATOM 2874 CG1 VAL A 282 -25.332 -8.750 5.273 1.00 24.01 C ANISOU 2874 CG1 VAL A 282 3416 3137 2570 -74 -26 -45 C ATOM 2875 CG2 VAL A 282 -25.810 -6.794 6.825 1.00 23.78 C ANISOU 2875 CG2 VAL A 282 3293 3142 2602 -58 -36 9 C ATOM 2876 N VAL A 283 -23.011 -10.259 8.114 1.00 22.15 N ANISOU 2876 N VAL A 283 3127 2829 2459 -36 42 -56 N ATOM 2877 CA VAL A 283 -22.044 -11.225 7.563 1.00 24.00 C ANISOU 2877 CA VAL A 283 3401 3030 2688 -16 71 -88 C ATOM 2878 C VAL A 283 -22.153 -12.652 8.137 1.00 26.43 C ANISOU 2878 C VAL A 283 3729 3295 3020 -25 51 -105 C ATOM 2879 O VAL A 283 -21.888 -13.618 7.409 1.00 26.62 O ANISOU 2879 O VAL A 283 3802 3287 3027 -18 56 -140 O ATOM 2880 CB VAL A 283 -20.588 -10.726 7.692 1.00 25.98 C ANISOU 2880 CB VAL A 283 3629 3282 2959 22 121 -84 C ATOM 2881 CG1 VAL A 283 -20.396 -9.378 7.004 1.00 30.71 C ANISOU 2881 CG1 VAL A 283 4219 3918 3533 26 143 -65 C ATOM 2882 CG2 VAL A 283 -20.157 -10.625 9.130 1.00 24.30 C ANISOU 2882 CG2 VAL A 283 3369 3063 2801 30 121 -63 C ATOM 2883 N ASN A 284 -22.532 -12.850 9.396 1.00 23.55 N ANISOU 2883 N ASN A 284 3333 2925 2692 -42 29 -83 N ATOM 2884 CA ASN A 284 -22.496 -14.216 9.943 1.00 26.86 C ANISOU 2884 CA ASN A 284 3776 3295 3134 -51 11 -93 C ATOM 2885 C ASN A 284 -23.329 -15.236 9.170 1.00 27.86 C ANISOU 2885 C ASN A 284 3957 3395 3234 -83 -21 -120 C ATOM 2886 O ASN A 284 -22.808 -16.336 8.931 1.00 28.04 O ANISOU 2886 O ASN A 284 4024 3366 3265 -70 -18 -148 O ATOM 2887 CB ASN A 284 -22.883 -14.230 11.436 1.00 25.66 C ANISOU 2887 CB ASN A 284 3584 3149 3018 -72 -9 -59 C ATOM 2888 CG ASN A 284 -21.952 -13.334 12.263 1.00 35.84 C ANISOU 2888 CG ASN A 284 4825 4458 4334 -40 18 -38 C ATOM 2889 OD1 ASN A 284 -20.873 -12.935 11.787 1.00 32.45 O ANISOU 2889 OD1 ASN A 284 4394 4029 3908 -2 53 -49 O ATOM 2890 ND2 ASN A 284 -22.352 -13.016 13.482 1.00 36.30 N ANISOU 2890 ND2 ASN A 284 4846 4536 4411 -57 4 -10 N ATOM 2891 N PRO A 285 -24.561 -14.957 8.717 1.00 26.35 N ANISOU 2891 N PRO A 285 3766 3233 3013 -122 -53 -117 N ATOM 2892 CA PRO A 285 -25.258 -15.957 7.883 1.00 25.23 C ANISOU 2892 CA PRO A 285 3680 3064 2843 -155 -86 -147 C ATOM 2893 C PRO A 285 -24.444 -16.430 6.688 1.00 27.44 C ANISOU 2893 C PRO A 285 4019 3314 3093 -123 -61 -193 C ATOM 2894 O PRO A 285 -24.548 -17.591 6.301 1.00 31.58 O ANISOU 2894 O PRO A 285 4597 3790 3610 -136 -80 -226 O ATOM 2895 CB PRO A 285 -26.521 -15.205 7.430 1.00 25.76 C ANISOU 2895 CB PRO A 285 3725 3184 2878 -190 -118 -134 C ATOM 2896 CG PRO A 285 -26.795 -14.278 8.583 1.00 26.60 C ANISOU 2896 CG PRO A 285 3762 3331 3015 -190 -114 -93 C ATOM 2897 CD PRO A 285 -25.430 -13.802 9.018 1.00 26.68 C ANISOU 2897 CD PRO A 285 3757 3332 3049 -140 -67 -86 C ATOM 2898 N PHE A 286 -23.658 -15.548 6.082 1.00 26.85 N ANISOU 2898 N PHE A 286 3936 3269 2997 -84 -19 -196 N ATOM 2899 CA PHE A 286 -22.823 -15.935 4.938 1.00 31.33 C ANISOU 2899 CA PHE A 286 4555 3819 3530 -51 14 -240 C ATOM 2900 C PHE A 286 -21.702 -16.861 5.356 1.00 30.60 C ANISOU 2900 C PHE A 286 4475 3673 3477 -11 41 -263 C ATOM 2901 O PHE A 286 -21.406 -17.847 4.657 1.00 30.90 O ANISOU 2901 O PHE A 286 4571 3669 3499 3 46 -311 O ATOM 2902 CB PHE A 286 -22.272 -14.680 4.250 1.00 37.04 C ANISOU 2902 CB PHE A 286 5259 4592 4220 -26 55 -229 C ATOM 2903 CG PHE A 286 -23.295 -14.009 3.425 1.00 34.85 C ANISOU 2903 CG PHE A 286 4994 4356 3890 -58 25 -219 C ATOM 2904 CD1 PHE A 286 -23.520 -14.438 2.123 1.00 36.54 C ANISOU 2904 CD1 PHE A 286 5271 4569 4043 -66 18 -257 C ATOM 2905 CD2 PHE A 286 -24.121 -13.052 3.982 1.00 38.60 C ANISOU 2905 CD2 PHE A 286 5421 4868 4379 -79 -2 -176 C ATOM 2906 CE1 PHE A 286 -24.520 -13.868 1.359 1.00 38.94 C ANISOU 2906 CE1 PHE A 286 5587 4911 4296 -96 -19 -246 C ATOM 2907 CE2 PHE A 286 -25.134 -12.475 3.232 1.00 40.42 C ANISOU 2907 CE2 PHE A 286 5658 5133 4565 -105 -38 -166 C ATOM 2908 CZ PHE A 286 -25.338 -12.889 1.913 1.00 33.83 C ANISOU 2908 CZ PHE A 286 4887 4300 3668 -115 -49 -199 C ATOM 2909 N ILE A 287 -21.078 -16.583 6.501 1.00 28.61 N ANISOU 2909 N ILE A 287 4173 3421 3278 9 57 -232 N ATOM 2910 CA ILE A 287 -20.021 -17.485 6.957 1.00 32.05 C ANISOU 2910 CA ILE A 287 4617 3804 3755 51 75 -250 C ATOM 2911 C ILE A 287 -20.596 -18.868 7.251 1.00 31.63 C ANISOU 2911 C ILE A 287 4612 3685 3719 26 30 -266 C ATOM 2912 O ILE A 287 -20.013 -19.889 6.858 1.00 34.99 O ANISOU 2912 O ILE A 287 5085 4056 4152 57 38 -307 O ATOM 2913 CB ILE A 287 -19.299 -16.887 8.175 1.00 33.58 C ANISOU 2913 CB ILE A 287 4745 4014 3999 72 91 -210 C ATOM 2914 CG1 ILE A 287 -18.823 -15.468 7.864 1.00 33.28 C ANISOU 2914 CG1 ILE A 287 4662 4037 3944 87 131 -192 C ATOM 2915 CG2 ILE A 287 -18.138 -17.763 8.574 1.00 31.66 C ANISOU 2915 CG2 ILE A 287 4506 3722 3800 122 108 -227 C ATOM 2916 CD1 ILE A 287 -17.718 -15.395 6.858 1.00 36.07 C ANISOU 2916 CD1 ILE A 287 5027 4399 4278 131 185 -226 C ATOM 2917 N TYR A 288 -21.765 -18.931 7.920 1.00 31.17 N ANISOU 2917 N TYR A 288 4544 3631 3667 -31 -17 -234 N ATOM 2918 CA TYR A 288 -22.370 -20.236 8.200 1.00 33.08 C ANISOU 2918 CA TYR A 288 4833 3809 3925 -67 -62 -243 C ATOM 2919 C TYR A 288 -22.686 -20.970 6.908 1.00 34.29 C ANISOU 2919 C TYR A 288 5059 3931 4038 -76 -75 -298 C ATOM 2920 O TYR A 288 -22.425 -22.171 6.795 1.00 35.73 O ANISOU 2920 O TYR A 288 5298 4041 4237 -67 -88 -331 O ATOM 2921 CB TYR A 288 -23.648 -20.112 9.045 1.00 31.41 C ANISOU 2921 CB TYR A 288 4593 3621 3721 -134 -106 -199 C ATOM 2922 CG TYR A 288 -23.462 -19.407 10.361 1.00 30.95 C ANISOU 2922 CG TYR A 288 4468 3597 3696 -130 -96 -148 C ATOM 2923 CD1 TYR A 288 -22.384 -19.699 11.189 1.00 34.93 C ANISOU 2923 CD1 TYR A 288 4961 4068 4240 -89 -79 -135 C ATOM 2924 CD2 TYR A 288 -24.365 -18.435 10.770 1.00 28.09 C ANISOU 2924 CD2 TYR A 288 4053 3299 3321 -165 -105 -114 C ATOM 2925 CE1 TYR A 288 -22.216 -19.040 12.425 1.00 41.48 C ANISOU 2925 CE1 TYR A 288 5733 4932 5095 -88 -74 -90 C ATOM 2926 CE2 TYR A 288 -24.208 -17.766 11.972 1.00 27.40 C ANISOU 2926 CE2 TYR A 288 3909 3244 3259 -160 -96 -74 C ATOM 2927 CZ TYR A 288 -23.131 -18.062 12.794 1.00 34.22 C ANISOU 2927 CZ TYR A 288 4766 4077 4158 -124 -80 -62 C ATOM 2928 OH TYR A 288 -22.998 -17.369 13.979 1.00 29.25 O ANISOU 2928 OH TYR A 288 4083 3483 3547 -122 -74 -24 O ATOM 2929 N ALA A 289 -23.252 -20.253 5.923 1.00 32.65 N ANISOU 2929 N ALA A 289 4854 3776 3776 -94 -74 -310 N ATOM 2930 CA ALA A 289 -23.627 -20.864 4.654 1.00 33.73 C ANISOU 2930 CA ALA A 289 5061 3892 3863 -108 -90 -363 C ATOM 2931 C ALA A 289 -22.403 -21.393 3.919 1.00 37.88 C ANISOU 2931 C ALA A 289 5633 4381 4381 -44 -46 -419 C ATOM 2932 O ALA A 289 -22.439 -22.496 3.365 1.00 35.07 O ANISOU 2932 O ALA A 289 5347 3965 4015 -45 -63 -469 O ATOM 2933 CB ALA A 289 -24.365 -19.859 3.771 1.00 30.73 C ANISOU 2933 CB ALA A 289 4669 3583 3424 -133 -97 -358 C ATOM 2934 N TYR A 290 -21.308 -20.619 3.914 1.00 35.84 N ANISOU 2934 N TYR A 290 5333 4157 4126 12 13 -411 N ATOM 2935 CA TYR A 290 -20.110 -21.017 3.181 1.00 38.05 C ANISOU 2935 CA TYR A 290 5645 4418 4396 76 64 -464 C ATOM 2936 C TYR A 290 -19.288 -22.073 3.917 1.00 38.43 C ANISOU 2936 C TYR A 290 5703 4391 4508 120 67 -479 C ATOM 2937 O TYR A 290 -18.607 -22.876 3.267 1.00 38.86 O ANISOU 2937 O TYR A 290 5806 4403 4557 166 90 -538 O ATOM 2938 CB TYR A 290 -19.253 -19.782 2.857 1.00 42.87 C ANISOU 2938 CB TYR A 290 6204 5099 4987 113 127 -448 C ATOM 2939 CG TYR A 290 -19.686 -19.101 1.572 1.00 50.54 C ANISOU 2939 CG TYR A 290 7202 6125 5877 93 137 -463 C ATOM 2940 CD1 TYR A 290 -19.238 -19.562 0.334 1.00 53.05 C ANISOU 2940 CD1 TYR A 290 7578 6438 6140 120 169 -526 C ATOM 2941 CD2 TYR A 290 -20.571 -18.028 1.588 1.00 57.47 C ANISOU 2941 CD2 TYR A 290 8048 7058 6731 48 113 -416 C ATOM 2942 CE1 TYR A 290 -19.645 -18.969 -0.844 1.00 54.99 C ANISOU 2942 CE1 TYR A 290 7854 6734 6304 99 175 -536 C ATOM 2943 CE2 TYR A 290 -20.986 -17.420 0.410 1.00 59.67 C ANISOU 2943 CE2 TYR A 290 8355 7384 6934 30 115 -425 C ATOM 2944 CZ TYR A 290 -20.516 -17.900 -0.802 1.00 61.91 C ANISOU 2944 CZ TYR A 290 8700 7663 7158 53 146 -483 C ATOM 2945 OH TYR A 290 -20.916 -17.312 -1.980 1.00 70.28 O ANISOU 2945 OH TYR A 290 9794 8773 8137 34 146 -489 O ATOM 2946 N ARG A 291 -19.366 -22.158 5.241 1.00 34.76 N ANISOU 2946 N ARG A 291 5199 3907 4103 108 42 -430 N ATOM 2947 CA ARG A 291 -18.433 -23.026 5.957 1.00 38.59 C ANISOU 2947 CA ARG A 291 5686 4326 4648 158 46 -436 C ATOM 2948 C ARG A 291 -19.066 -24.190 6.712 1.00 41.11 C ANISOU 2948 C ARG A 291 6047 4565 5006 122 -15 -425 C ATOM 2949 O ARG A 291 -18.327 -25.059 7.187 1.00 42.46 O ANISOU 2949 O ARG A 291 6237 4669 5227 167 -19 -435 O ATOM 2950 CB ARG A 291 -17.576 -22.208 6.944 1.00 39.98 C ANISOU 2950 CB ARG A 291 5780 4543 4868 191 75 -388 C ATOM 2951 CG ARG A 291 -16.619 -21.206 6.268 1.00 39.44 C ANISOU 2951 CG ARG A 291 5669 4542 4776 236 142 -401 C ATOM 2952 CD ARG A 291 -15.521 -20.777 7.206 1.00 38.81 C ANISOU 2952 CD ARG A 291 5518 4477 4750 280 168 -369 C ATOM 2953 NE ARG A 291 -14.963 -21.927 7.928 1.00 46.02 N ANISOU 2953 NE ARG A 291 6447 5316 5723 319 146 -376 N ATOM 2954 CZ ARG A 291 -13.757 -22.460 7.701 1.00 48.47 C ANISOU 2954 CZ ARG A 291 6753 5600 6062 394 180 -414 C ATOM 2955 NH1 ARG A 291 -12.961 -21.943 6.776 1.00 42.59 N ANISOU 2955 NH1 ARG A 291 5987 4904 5291 434 244 -448 N ATOM 2956 NH2 ARG A 291 -13.337 -23.505 8.416 1.00 49.61 N ANISOU 2956 NH2 ARG A 291 6914 5671 6264 429 151 -415 N ATOM 2957 N ILE A 292 -20.386 -24.254 6.833 1.00 37.39 N ANISOU 2957 N ILE A 292 5593 4097 4516 44 -64 -402 N ATOM 2958 CA ILE A 292 -21.038 -25.245 7.672 1.00 35.36 C ANISOU 2958 CA ILE A 292 5366 3772 4296 -3 -121 -378 C ATOM 2959 C ILE A 292 -22.096 -25.945 6.829 1.00 37.44 C ANISOU 2959 C ILE A 292 5699 4002 4523 -61 -163 -415 C ATOM 2960 O ILE A 292 -23.207 -25.429 6.658 1.00 34.96 O ANISOU 2960 O ILE A 292 5368 3740 4176 -126 -187 -395 O ATOM 2961 CB ILE A 292 -21.657 -24.633 8.929 1.00 37.61 C ANISOU 2961 CB ILE A 292 5588 4102 4602 -52 -141 -303 C ATOM 2962 CG1 ILE A 292 -20.614 -23.783 9.670 1.00 44.12 C ANISOU 2962 CG1 ILE A 292 6342 4970 5453 4 -100 -271 C ATOM 2963 CG2 ILE A 292 -22.234 -25.755 9.814 1.00 35.11 C ANISOU 2963 CG2 ILE A 292 5307 3711 4321 -101 -195 -274 C ATOM 2964 CD1 ILE A 292 -21.123 -23.078 10.939 1.00 45.18 C ANISOU 2964 CD1 ILE A 292 6412 5152 5602 -37 -114 -202 C ATOM 2965 N ARG A 293 -21.770 -27.151 6.348 1.00 39.81 N ANISOU 2965 N ARG A 293 6079 4212 4834 -38 -177 -469 N ATOM 2966 CA ARG A 293 -22.658 -27.889 5.451 1.00 44.60 C ANISOU 2966 CA ARG A 293 6762 4779 5406 -90 -218 -516 C ATOM 2967 C ARG A 293 -24.082 -27.982 5.997 1.00 38.34 C ANISOU 2967 C ARG A 293 5960 3995 4614 -193 -278 -468 C ATOM 2968 O ARG A 293 -25.060 -27.787 5.265 1.00 39.42 O ANISOU 2968 O ARG A 293 6108 4166 4703 -250 -304 -484 O ATOM 2969 CB ARG A 293 -22.112 -29.302 5.212 1.00 58.54 C ANISOU 2969 CB ARG A 293 8614 6426 7201 -54 -234 -572 C ATOM 2970 CG ARG A 293 -20.603 -29.481 4.958 1.00 78.07 C ANISOU 2970 CG ARG A 293 11094 8873 9696 57 -179 -616 C ATOM 2971 CD ARG A 293 -20.511 -30.814 4.171 1.00 85.67 C ANISOU 2971 CD ARG A 293 12164 9730 10658 75 -202 -697 C ATOM 2972 NE ARG A 293 -19.249 -31.526 4.326 1.00 89.78 N ANISOU 2972 NE ARG A 293 12706 10178 11229 172 -177 -732 N ATOM 2973 CZ ARG A 293 -18.408 -31.770 3.327 1.00 95.56 C ANISOU 2973 CZ ARG A 293 13472 10897 11939 250 -131 -814 C ATOM 2974 NH1 ARG A 293 -18.709 -31.368 2.098 1.00 96.03 N ANISOU 2974 NH1 ARG A 293 13556 11011 11921 237 -107 -867 N ATOM 2975 NH2 ARG A 293 -17.271 -32.418 3.557 1.00 99.22 N ANISOU 2975 NH2 ARG A 293 13947 11296 12457 342 -110 -843 N ATOM 2976 N GLU A 294 -24.222 -28.299 7.282 1.00 39.82 N ANISOU 2976 N GLU A 294 6123 4153 4852 -220 -301 -409 N ATOM 2977 CA GLU A 294 -25.552 -28.519 7.843 1.00 40.57 C ANISOU 2977 CA GLU A 294 6210 4254 4951 -321 -354 -364 C ATOM 2978 C GLU A 294 -26.419 -27.257 7.777 1.00 42.80 C ANISOU 2978 C GLU A 294 6416 4652 5195 -362 -348 -332 C ATOM 2979 O GLU A 294 -27.635 -27.345 7.556 1.00 42.39 O ANISOU 2979 O GLU A 294 6365 4620 5122 -441 -389 -325 O ATOM 2980 CB GLU A 294 -25.410 -29.013 9.282 1.00 39.50 C ANISOU 2980 CB GLU A 294 6061 4074 4872 -335 -372 -301 C ATOM 2981 CG GLU A 294 -26.684 -29.519 9.873 1.00 42.50 C ANISOU 2981 CG GLU A 294 6446 4443 5261 -442 -426 -258 C ATOM 2982 CD GLU A 294 -27.116 -30.818 9.265 1.00 50.89 C ANISOU 2982 CD GLU A 294 7603 5404 6327 -486 -476 -300 C ATOM 2983 OE1 GLU A 294 -26.233 -31.605 8.868 1.00 56.34 O ANISOU 2983 OE1 GLU A 294 8364 6005 7037 -426 -474 -348 O ATOM 2984 OE2 GLU A 294 -28.338 -31.046 9.167 1.00 55.00 O ANISOU 2984 OE2 GLU A 294 8128 5937 6833 -581 -519 -287 O ATOM 2985 N PHE A 295 -25.818 -26.073 7.983 1.00 37.37 N ANISOU 2985 N PHE A 295 5661 4039 4501 -309 -298 -311 N ATOM 2986 CA PHE A 295 -26.554 -24.824 7.793 1.00 35.41 C ANISOU 2986 CA PHE A 295 5345 3893 4215 -335 -291 -288 C ATOM 2987 C PHE A 295 -26.873 -24.602 6.323 1.00 36.18 C ANISOU 2987 C PHE A 295 5477 4014 4254 -336 -294 -341 C ATOM 2988 O PHE A 295 -28.024 -24.336 5.957 1.00 33.23 O ANISOU 2988 O PHE A 295 5090 3684 3851 -397 -329 -335 O ATOM 2989 CB PHE A 295 -25.749 -23.619 8.315 1.00 33.00 C ANISOU 2989 CB PHE A 295 4969 3651 3919 -276 -239 -257 C ATOM 2990 CG PHE A 295 -26.010 -23.277 9.759 1.00 31.94 C ANISOU 2990 CG PHE A 295 4773 3545 3819 -300 -243 -192 C ATOM 2991 CD1 PHE A 295 -27.203 -22.669 10.134 1.00 30.51 C ANISOU 2991 CD1 PHE A 295 4539 3429 3625 -361 -263 -156 C ATOM 2992 CD2 PHE A 295 -25.054 -23.545 10.734 1.00 31.35 C ANISOU 2992 CD2 PHE A 295 4690 3434 3787 -260 -226 -169 C ATOM 2993 CE1 PHE A 295 -27.461 -22.349 11.465 1.00 32.33 C ANISOU 2993 CE1 PHE A 295 4713 3690 3880 -383 -262 -101 C ATOM 2994 CE2 PHE A 295 -25.301 -23.224 12.093 1.00 34.34 C ANISOU 2994 CE2 PHE A 295 5015 3843 4190 -285 -230 -109 C ATOM 2995 CZ PHE A 295 -26.508 -22.623 12.446 1.00 32.30 C ANISOU 2995 CZ PHE A 295 4707 3651 3913 -347 -246 -77 C ATOM 2996 N ARG A 296 -25.843 -24.647 5.473 1.00 39.63 N ANISOU 2996 N ARG A 296 5954 4432 4672 -268 -256 -392 N ATOM 2997 CA ARG A 296 -26.036 -24.480 4.038 1.00 37.83 C ANISOU 2997 CA ARG A 296 5767 4227 4379 -266 -255 -445 C ATOM 2998 C ARG A 296 -27.188 -25.343 3.524 1.00 38.98 C ANISOU 2998 C ARG A 296 5969 4337 4504 -342 -321 -471 C ATOM 2999 O ARG A 296 -28.070 -24.862 2.803 1.00 38.26 O ANISOU 2999 O ARG A 296 5872 4301 4365 -383 -347 -476 O ATOM 3000 CB ARG A 296 -24.724 -24.813 3.326 1.00 39.75 C ANISOU 3000 CB ARG A 296 6059 4433 4612 -186 -206 -502 C ATOM 3001 CG ARG A 296 -24.791 -24.804 1.830 1.00 47.03 C ANISOU 3001 CG ARG A 296 7037 5370 5461 -179 -201 -565 C ATOM 3002 CD ARG A 296 -23.381 -24.808 1.231 1.00 48.05 C ANISOU 3002 CD ARG A 296 7189 5491 5578 -91 -133 -612 C ATOM 3003 NE ARG A 296 -22.637 -26.048 1.441 1.00 43.73 N ANISOU 3003 NE ARG A 296 6694 4846 5073 -49 -129 -655 N ATOM 3004 CZ ARG A 296 -21.564 -26.172 2.216 1.00 42.33 C ANISOU 3004 CZ ARG A 296 6487 4643 4955 13 -93 -641 C ATOM 3005 NH1 ARG A 296 -20.953 -27.349 2.321 1.00 41.99 N ANISOU 3005 NH1 ARG A 296 6497 4506 4950 53 -97 -683 N ATOM 3006 NH2 ARG A 296 -21.108 -25.131 2.914 1.00 41.48 N ANISOU 3006 NH2 ARG A 296 6293 4597 4868 34 -58 -585 N ATOM 3007 N GLN A 297 -27.220 -26.622 3.927 1.00 38.48 N ANISOU 3007 N GLN A 297 5960 4182 4481 -365 -353 -484 N ATOM 3008 CA GLN A 297 -28.263 -27.512 3.431 1.00 41.78 C ANISOU 3008 CA GLN A 297 6436 4557 4882 -443 -418 -512 C ATOM 3009 C GLN A 297 -29.628 -27.120 3.980 1.00 40.72 C ANISOU 3009 C GLN A 297 6240 4481 4752 -531 -462 -456 C ATOM 3010 O GLN A 297 -30.637 -27.169 3.264 1.00 39.47 O ANISOU 3010 O GLN A 297 6094 4347 4556 -592 -508 -473 O ATOM 3011 CB GLN A 297 -27.915 -28.974 3.774 1.00 44.20 C ANISOU 3011 CB GLN A 297 6819 4740 5235 -446 -442 -537 C ATOM 3012 CG GLN A 297 -26.655 -29.495 3.060 1.00 47.85 C ANISOU 3012 CG GLN A 297 7351 5140 5691 -357 -404 -609 C ATOM 3013 CD GLN A 297 -26.240 -30.917 3.481 1.00 58.49 C ANISOU 3013 CD GLN A 297 8773 6356 7093 -347 -429 -631 C ATOM 3014 OE1 GLN A 297 -26.402 -31.322 4.641 1.00 61.24 O ANISOU 3014 OE1 GLN A 297 9105 6666 7499 -378 -453 -575 O ATOM 3015 NE2 GLN A 297 -25.684 -31.670 2.532 1.00 56.74 N ANISOU 3015 NE2 GLN A 297 8638 6067 6853 -302 -424 -715 N ATOM 3016 N THR A 298 -29.687 -26.734 5.252 1.00 37.34 N ANISOU 3016 N THR A 298 5741 4079 4368 -539 -450 -389 N ATOM 3017 CA THR A 298 -30.963 -26.300 5.798 1.00 37.08 C ANISOU 3017 CA THR A 298 5639 4111 4337 -617 -483 -337 C ATOM 3018 C THR A 298 -31.416 -24.992 5.160 1.00 36.63 C ANISOU 3018 C THR A 298 5525 4158 4234 -606 -473 -333 C ATOM 3019 O THR A 298 -32.603 -24.819 4.873 1.00 36.68 O ANISOU 3019 O THR A 298 5505 4211 4221 -670 -517 -324 O ATOM 3020 CB THR A 298 -30.846 -26.157 7.304 1.00 34.50 C ANISOU 3020 CB THR A 298 5254 3792 4061 -621 -465 -271 C ATOM 3021 OG1 THR A 298 -30.243 -27.339 7.825 1.00 38.80 O ANISOU 3021 OG1 THR A 298 5861 4235 4648 -617 -473 -274 O ATOM 3022 CG2 THR A 298 -32.203 -25.965 7.923 1.00 34.76 C ANISOU 3022 CG2 THR A 298 5223 3882 4100 -708 -500 -222 C ATOM 3023 N PHE A 299 -30.484 -24.057 4.941 1.00 38.51 N ANISOU 3023 N PHE A 299 5743 4433 4457 -526 -419 -336 N ATOM 3024 CA PHE A 299 -30.809 -22.840 4.198 1.00 33.91 C ANISOU 3024 CA PHE A 299 5121 3937 3827 -511 -411 -334 C ATOM 3025 C PHE A 299 -31.404 -23.186 2.836 1.00 38.80 C ANISOU 3025 C PHE A 299 5799 4555 4390 -543 -453 -384 C ATOM 3026 O PHE A 299 -32.445 -22.642 2.445 1.00 38.40 O ANISOU 3026 O PHE A 299 5712 4566 4310 -584 -491 -371 O ATOM 3027 CB PHE A 299 -29.565 -21.960 4.012 1.00 35.07 C ANISOU 3027 CB PHE A 299 5255 4106 3963 -424 -345 -337 C ATOM 3028 CG PHE A 299 -29.040 -21.318 5.309 1.00 35.20 C ANISOU 3028 CG PHE A 299 5203 4144 4029 -392 -306 -285 C ATOM 3029 CD1 PHE A 299 -29.741 -21.422 6.494 1.00 31.25 C ANISOU 3029 CD1 PHE A 299 4653 3654 3568 -439 -328 -238 C ATOM 3030 CD2 PHE A 299 -27.814 -20.638 5.321 1.00 34.76 C ANISOU 3030 CD2 PHE A 299 5134 4100 3975 -318 -248 -285 C ATOM 3031 CE1 PHE A 299 -29.246 -20.838 7.670 1.00 31.23 C ANISOU 3031 CE1 PHE A 299 4592 3672 3602 -410 -294 -195 C ATOM 3032 CE2 PHE A 299 -27.321 -20.064 6.484 1.00 32.30 C ANISOU 3032 CE2 PHE A 299 4762 3806 3705 -292 -218 -241 C ATOM 3033 CZ PHE A 299 -28.044 -20.165 7.656 1.00 29.69 C ANISOU 3033 CZ PHE A 299 4387 3485 3410 -337 -242 -198 C ATOM 3034 N AARG A 300 -30.748 -24.086 2.100 0.54 42.19 N ANISOU 3034 N AARG A 300 6317 4914 4800 -522 -449 -444 N ATOM 3035 N BARG A 300 -30.759 -24.096 2.104 0.46 42.36 N ANISOU 3035 N BARG A 300 6339 4935 4822 -522 -450 -444 N ATOM 3036 CA AARG A 300 -31.256 -24.493 0.788 0.54 46.80 C ANISOU 3036 CA AARG A 300 6968 5492 5324 -552 -490 -500 C ATOM 3037 CA BARG A 300 -31.267 -24.471 0.785 0.46 46.69 C ANISOU 3037 CA BARG A 300 6952 5480 5309 -552 -491 -499 C ATOM 3038 C AARG A 300 -32.681 -25.025 0.889 0.54 45.20 C ANISOU 3038 C AARG A 300 6757 5290 5128 -650 -567 -489 C ATOM 3039 C BARG A 300 -32.677 -25.043 0.873 0.46 45.28 C ANISOU 3039 C BARG A 300 6768 5298 5137 -651 -568 -490 C ATOM 3040 O AARG A 300 -33.550 -24.670 0.085 0.54 45.35 O ANISOU 3040 O AARG A 300 6769 5361 5099 -688 -610 -498 O ATOM 3041 O BARG A 300 -33.535 -24.729 0.040 0.46 45.26 O ANISOU 3041 O BARG A 300 6764 5346 5087 -689 -611 -502 O ATOM 3042 CB AARG A 300 -30.338 -25.551 0.161 0.54 51.25 C ANISOU 3042 CB AARG A 300 7631 5967 5875 -515 -474 -571 C ATOM 3043 CB BARG A 300 -30.321 -25.474 0.117 0.46 51.27 C ANISOU 3043 CB BARG A 300 7631 5974 5874 -512 -472 -571 C ATOM 3044 CG AARG A 300 -29.136 -24.995 -0.600 0.54 54.51 C ANISOU 3044 CG AARG A 300 8065 6399 6245 -427 -407 -605 C ATOM 3045 CG BARG A 300 -28.956 -24.896 -0.240 0.46 53.93 C ANISOU 3045 CG BARG A 300 7974 6326 6192 -417 -395 -589 C ATOM 3046 CD AARG A 300 -28.513 -26.052 -1.525 0.54 56.97 C ANISOU 3046 CD AARG A 300 8482 6637 6526 -400 -401 -690 C ATOM 3047 CD BARG A 300 -28.183 -25.813 -1.183 0.46 56.84 C ANISOU 3047 CD BARG A 300 8442 6628 6528 -378 -378 -672 C ATOM 3048 NE AARG A 300 -27.652 -26.994 -0.810 0.54 58.24 N ANISOU 3048 NE AARG A 300 8672 6706 6751 -362 -379 -705 N ATOM 3049 NE BARG A 300 -27.022 -25.143 -1.766 0.46 57.22 N ANISOU 3049 NE BARG A 300 8489 6711 6540 -296 -304 -693 N ATOM 3050 CZ AARG A 300 -26.321 -26.945 -0.805 0.54 57.82 C ANISOU 3050 CZ AARG A 300 8623 6636 6709 -275 -311 -726 C ATOM 3051 CZ BARG A 300 -27.091 -24.298 -2.788 0.46 58.22 C ANISOU 3051 CZ BARG A 300 8618 6910 6591 -287 -290 -703 C ATOM 3052 NH1AARG A 300 -25.678 -25.999 -1.486 0.54 56.83 N ANISOU 3052 NH1AARG A 300 8478 6580 6534 -222 -255 -734 N ATOM 3053 NH1BARG A 300 -28.263 -24.012 -3.335 0.46 56.90 N ANISOU 3053 NH1BARG A 300 8453 6787 6378 -350 -349 -695 N ATOM 3054 NH2AARG A 300 -25.633 -27.846 -0.120 0.54 56.61 N ANISOU 3054 NH2AARG A 300 8494 6396 6618 -241 -302 -736 N ATOM 3055 NH2BARG A 300 -25.991 -23.732 -3.258 0.46 62.45 N ANISOU 3055 NH2BARG A 300 9152 7477 7097 -218 -218 -718 N ATOM 3056 N LYS A 301 -32.940 -25.879 1.880 1.00 44.74 N ANISOU 3056 N LYS A 301 6695 5176 5129 -696 -588 -466 N ATOM 3057 CA LYS A 301 -34.270 -26.475 2.004 1.00 47.42 C ANISOU 3057 CA LYS A 301 7027 5514 5479 -798 -659 -455 C ATOM 3058 C LYS A 301 -35.321 -25.430 2.353 1.00 43.09 C ANISOU 3058 C LYS A 301 6371 5071 4928 -833 -676 -400 C ATOM 3059 O LYS A 301 -36.421 -25.447 1.795 1.00 44.39 O ANISOU 3059 O LYS A 301 6524 5274 5068 -897 -734 -406 O ATOM 3060 CB LYS A 301 -34.260 -27.592 3.045 1.00 53.00 C ANISOU 3060 CB LYS A 301 7753 6135 6248 -841 -672 -435 C ATOM 3061 CG LYS A 301 -33.642 -28.883 2.549 1.00 63.49 C ANISOU 3061 CG LYS A 301 9197 7346 7579 -833 -685 -498 C ATOM 3062 CD LYS A 301 -33.692 -29.962 3.617 1.00 69.80 C ANISOU 3062 CD LYS A 301 10020 8059 8444 -880 -705 -468 C ATOM 3063 CE LYS A 301 -32.870 -31.171 3.212 1.00 74.88 C ANISOU 3063 CE LYS A 301 10778 8574 9098 -849 -711 -530 C ATOM 3064 NZ LYS A 301 -32.466 -31.987 4.399 1.00 77.32 N ANISOU 3064 NZ LYS A 301 11104 8798 9476 -855 -709 -491 N ATOM 3065 N ILE A 302 -35.004 -24.519 3.278 1.00 37.11 N ANISOU 3065 N ILE A 302 5537 4363 4200 -791 -627 -348 N ATOM 3066 CA ILE A 302 -35.917 -23.430 3.618 1.00 42.20 C ANISOU 3066 CA ILE A 302 6080 5109 4845 -809 -637 -300 C ATOM 3067 C ILE A 302 -36.209 -22.558 2.402 1.00 46.87 C ANISOU 3067 C ILE A 302 6669 5763 5377 -786 -654 -321 C ATOM 3068 O ILE A 302 -37.359 -22.167 2.152 1.00 44.99 O ANISOU 3068 O ILE A 302 6378 5589 5125 -832 -702 -306 O ATOM 3069 CB ILE A 302 -35.334 -22.576 4.754 1.00 44.48 C ANISOU 3069 CB ILE A 302 6300 5430 5169 -755 -577 -251 C ATOM 3070 CG1 ILE A 302 -35.203 -23.394 6.030 1.00 46.34 C ANISOU 3070 CG1 ILE A 302 6531 5615 5460 -786 -567 -221 C ATOM 3071 CG2 ILE A 302 -36.218 -21.398 4.990 1.00 41.93 C ANISOU 3071 CG2 ILE A 302 5879 5208 4844 -760 -584 -212 C ATOM 3072 CD1 ILE A 302 -34.497 -22.651 7.133 1.00 37.58 C ANISOU 3072 CD1 ILE A 302 5368 4530 4381 -731 -510 -179 C ATOM 3073 N ILE A 303 -35.162 -22.174 1.671 1.00 46.80 N ANISOU 3073 N ILE A 303 6709 5743 5330 -712 -613 -351 N ATOM 3074 CA ILE A 303 -35.376 -21.297 0.526 1.00 48.05 C ANISOU 3074 CA ILE A 303 6869 5961 5425 -690 -627 -364 C ATOM 3075 C ILE A 303 -36.175 -22.026 -0.562 1.00 51.52 C ANISOU 3075 C ILE A 303 7367 6390 5818 -751 -697 -409 C ATOM 3076 O ILE A 303 -37.000 -21.414 -1.246 1.00 48.29 O ANISOU 3076 O ILE A 303 6932 6046 5371 -770 -742 -402 O ATOM 3077 CB ILE A 303 -34.022 -20.751 0.016 1.00 44.43 C ANISOU 3077 CB ILE A 303 6451 5494 4936 -603 -561 -382 C ATOM 3078 CG1 ILE A 303 -33.369 -19.858 1.076 1.00 44.04 C ANISOU 3078 CG1 ILE A 303 6333 5467 4932 -550 -501 -334 C ATOM 3079 CG2 ILE A 303 -34.172 -19.972 -1.294 1.00 42.22 C ANISOU 3079 CG2 ILE A 303 6194 5268 4581 -584 -576 -397 C ATOM 3080 CD1 ILE A 303 -31.820 -19.860 1.026 1.00 45.45 C ANISOU 3080 CD1 ILE A 303 6554 5606 5110 -476 -430 -354 C ATOM 3081 N ARG A 304 -35.996 -23.340 -0.715 1.00 56.10 N ANISOU 3081 N ARG A 304 8026 6887 6404 -784 -715 -454 N ATOM 3082 CA ARG A 304 -36.730 -24.016 -1.786 1.00 61.76 C ANISOU 3082 CA ARG A 304 8803 7592 7073 -844 -786 -502 C ATOM 3083 C ARG A 304 -38.188 -24.246 -1.407 1.00 64.72 C ANISOU 3083 C ARG A 304 9115 8000 7474 -939 -857 -473 C ATOM 3084 O ARG A 304 -39.088 -23.984 -2.209 1.00 70.64 O ANISOU 3084 O ARG A 304 9854 8804 8182 -977 -918 -481 O ATOM 3085 CB ARG A 304 -36.053 -25.332 -2.174 1.00 60.10 C ANISOU 3085 CB ARG A 304 8705 7276 6855 -846 -784 -569 C ATOM 3086 CG ARG A 304 -34.787 -25.123 -2.996 1.00 63.60 C ANISOU 3086 CG ARG A 304 9217 7701 7246 -759 -725 -616 C ATOM 3087 CD ARG A 304 -34.052 -26.427 -3.291 1.00 72.49 C ANISOU 3087 CD ARG A 304 10450 8719 8373 -749 -717 -685 C ATOM 3088 NE ARG A 304 -32.652 -26.167 -3.640 1.00 79.05 N ANISOU 3088 NE ARG A 304 11318 9537 9181 -652 -638 -715 N ATOM 3089 CZ ARG A 304 -31.724 -27.111 -3.791 1.00 82.46 C ANISOU 3089 CZ ARG A 304 11829 9881 9620 -612 -609 -773 C ATOM 3090 NH1 ARG A 304 -30.475 -26.780 -4.102 1.00 79.89 N ANISOU 3090 NH1 ARG A 304 11522 9557 9274 -524 -533 -797 N ATOM 3091 NH2 ARG A 304 -32.042 -28.388 -3.625 1.00 84.71 N ANISOU 3091 NH2 ARG A 304 12174 10074 9937 -662 -655 -807 N ATOM 3092 N SER A 305 -38.444 -24.713 -0.192 1.00 65.17 N ANISOU 3092 N SER A 305 9129 8033 7601 -979 -853 -436 N ATOM 3093 CA SER A 305 -39.812 -24.991 0.246 1.00 70.98 C ANISOU 3093 CA SER A 305 9799 8804 8367 -1075 -914 -406 C ATOM 3094 C SER A 305 -40.679 -23.730 0.307 1.00 74.32 C ANISOU 3094 C SER A 305 10111 9344 8784 -1070 -928 -361 C ATOM 3095 O SER A 305 -40.172 -22.614 0.428 1.00 75.83 O ANISOU 3095 O SER A 305 10263 9580 8967 -992 -879 -337 O ATOM 3096 CB SER A 305 -39.802 -25.680 1.614 1.00 70.93 C ANISOU 3096 CB SER A 305 9767 8751 8431 -1114 -894 -368 C ATOM 3097 OG SER A 305 -39.156 -26.941 1.544 1.00 72.56 O ANISOU 3097 OG SER A 305 10078 8842 8648 -1127 -896 -409 O TER 3098 SER A 305 HETATM 3099 C1 ZMA A1201 -19.301 12.839 15.528 1.00 32.42 C ANISOU 3099 C1 ZMA A1201 4233 3870 4214 56 -49 151 C HETATM 3100 C2 ZMA A1201 -18.967 14.175 15.696 1.00 35.79 C ANISOU 3100 C2 ZMA A1201 4687 4234 4677 47 -70 156 C HETATM 3101 C3 ZMA A1201 -19.830 15.190 15.222 1.00 51.59 C ANISOU 3101 C3 ZMA A1201 6728 6186 6689 78 -105 169 C HETATM 3102 O4 ZMA A1201 -19.504 16.508 15.397 1.00 55.85 O ANISOU 3102 O4 ZMA A1201 7300 6653 7267 69 -130 173 O HETATM 3103 C5 ZMA A1201 -21.039 14.876 14.586 1.00 48.35 C ANISOU 3103 C5 ZMA A1201 6321 5796 6252 118 -120 177 C HETATM 3104 C6 ZMA A1201 -21.355 13.529 14.400 1.00 48.38 C ANISOU 3104 C6 ZMA A1201 6295 5869 6219 120 -98 172 C HETATM 3105 C7 ZMA A1201 -20.483 12.519 14.845 1.00 36.52 C ANISOU 3105 C7 ZMA A1201 4761 4408 4707 89 -62 160 C HETATM 3106 C8 ZMA A1201 -20.905 11.091 14.657 1.00 25.90 C ANISOU 3106 C8 ZMA A1201 3390 3125 3325 95 -44 153 C HETATM 3107 C9 ZMA A1201 -21.996 10.924 15.724 1.00 21.63 C ANISOU 3107 C9 ZMA A1201 2820 2608 2790 134 -63 109 C HETATM 3108 N10 ZMA A1201 -22.348 9.533 15.926 1.00 18.76 N ANISOU 3108 N10 ZMA A1201 2427 2303 2399 132 -47 96 N HETATM 3109 C11 ZMA A1201 -21.525 8.673 16.581 1.00 18.38 C ANISOU 3109 C11 ZMA A1201 2356 2280 2349 109 -22 84 C HETATM 3110 N12 ZMA A1201 -21.912 7.380 16.751 1.00 17.72 N ANISOU 3110 N12 ZMA A1201 2251 2241 2240 108 -12 75 N HETATM 3111 N13 ZMA A1201 -20.307 9.088 17.053 1.00 22.27 N ANISOU 3111 N13 ZMA A1201 2847 2749 2864 85 -11 83 N HETATM 3112 C14 ZMA A1201 -19.476 8.243 17.718 1.00 20.04 C ANISOU 3112 C14 ZMA A1201 2540 2492 2582 65 8 73 C HETATM 3113 N15 ZMA A1201 -18.265 8.678 18.145 1.00 19.95 N ANISOU 3113 N15 ZMA A1201 2523 2461 2596 40 15 73 N HETATM 3114 N16 ZMA A1201 -19.869 6.969 17.892 1.00 22.18 N ANISOU 3114 N16 ZMA A1201 2794 2806 2830 69 17 65 N HETATM 3115 N17 ZMA A1201 -19.151 5.972 18.535 1.00 21.63 N ANISOU 3115 N17 ZMA A1201 2701 2760 2758 55 32 58 N HETATM 3116 C18 ZMA A1201 -21.059 6.556 17.431 1.00 19.59 C ANISOU 3116 C18 ZMA A1201 2468 2496 2478 88 8 66 C HETATM 3117 N19 ZMA A1201 -21.223 5.243 17.745 1.00 18.60 N ANISOU 3117 N19 ZMA A1201 2326 2408 2334 82 18 58 N HETATM 3118 C20 ZMA A1201 -20.057 4.949 18.407 1.00 20.03 C ANISOU 3118 C20 ZMA A1201 2495 2588 2529 65 32 55 C HETATM 3119 C21 ZMA A1201 -19.738 3.611 18.928 1.00 18.51 C ANISOU 3119 C21 ZMA A1201 2285 2421 2325 55 43 51 C HETATM 3120 C22 ZMA A1201 -20.646 2.580 19.169 1.00 17.58 C ANISOU 3120 C22 ZMA A1201 2161 2334 2186 58 38 44 C HETATM 3121 C23 ZMA A1201 -19.807 1.559 19.643 1.00 22.07 C ANISOU 3121 C23 ZMA A1201 2721 2909 2756 46 48 47 C HETATM 3122 C24 ZMA A1201 -18.480 1.996 19.664 1.00 20.28 C ANISOU 3122 C24 ZMA A1201 2488 2663 2553 39 58 52 C HETATM 3123 O25 ZMA A1201 -18.436 3.314 19.228 1.00 21.75 O ANISOU 3123 O25 ZMA A1201 2685 2828 2752 41 56 55 O HETATM 3124 C1 CLR A1202 -38.211 10.669 21.820 1.00 27.15 C HETATM 3125 C2 CLR A1202 -37.963 12.153 22.103 1.00 30.32 C HETATM 3126 C3 CLR A1202 -38.181 12.478 23.588 1.00 30.25 C HETATM 3127 C4 CLR A1202 -37.272 11.633 24.475 1.00 27.95 C HETATM 3128 C5 CLR A1202 -37.617 10.184 24.209 1.00 29.59 C HETATM 3129 C6 CLR A1202 -37.995 9.421 25.248 1.00 32.43 C HETATM 3130 C7 CLR A1202 -38.116 7.909 25.176 1.00 34.53 C HETATM 3131 C8 CLR A1202 -37.815 7.360 23.764 1.00 29.83 C HETATM 3132 C9 CLR A1202 -38.176 8.318 22.641 1.00 23.47 C HETATM 3133 C10 CLR A1202 -37.513 9.686 22.781 1.00 26.85 C HETATM 3134 C11 CLR A1202 -37.914 7.662 21.263 1.00 25.19 C HETATM 3135 C12 CLR A1202 -38.764 6.385 21.115 1.00 23.03 C HETATM 3136 C13 CLR A1202 -38.337 5.396 22.203 1.00 24.32 C HETATM 3137 C14 CLR A1202 -38.600 6.067 23.537 1.00 29.87 C HETATM 3138 C15 CLR A1202 -38.354 4.959 24.563 1.00 30.66 C HETATM 3139 C16 CLR A1202 -38.918 3.711 23.860 1.00 26.59 C HETATM 3140 C17 CLR A1202 -39.114 4.091 22.376 1.00 25.12 C HETATM 3141 C18 CLR A1202 -36.853 5.002 22.067 1.00 24.02 C HETATM 3142 C19 CLR A1202 -36.015 9.566 22.399 1.00 27.52 C HETATM 3143 C20 CLR A1202 -38.812 2.923 21.451 1.00 22.68 C HETATM 3144 C21 CLR A1202 -38.955 3.249 19.966 1.00 25.57 C HETATM 3145 C22 CLR A1202 -39.739 1.761 21.817 1.00 29.25 C HETATM 3146 C23 CLR A1202 -39.499 0.490 20.992 1.00 33.39 C HETATM 3147 C24 CLR A1202 -40.389 -0.613 21.549 1.00 43.60 C HETATM 3148 C25 CLR A1202 -40.009 -1.949 20.910 1.00 53.79 C HETATM 3149 C26 CLR A1202 -40.087 -3.077 21.919 1.00 56.12 C HETATM 3150 C27 CLR A1202 -40.835 -2.270 19.663 1.00 49.80 C HETATM 3151 O1 CLR A1202 -37.877 13.849 23.821 1.00 28.75 O HETATM 3152 C1 CLR A1203 -8.141 10.815 13.372 1.00 30.03 C HETATM 3153 C2 CLR A1203 -8.194 12.345 13.367 1.00 30.79 C HETATM 3154 C3 CLR A1203 -6.822 12.959 13.031 1.00 32.17 C HETATM 3155 C4 CLR A1203 -6.377 12.481 11.664 1.00 25.06 C HETATM 3156 C5 CLR A1203 -6.424 10.977 11.596 1.00 29.71 C HETATM 3157 C6 CLR A1203 -5.345 10.327 11.130 1.00 29.28 C HETATM 3158 C7 CLR A1203 -5.306 8.826 10.934 1.00 28.91 C HETATM 3159 C8 CLR A1203 -6.690 8.178 10.961 1.00 29.81 C HETATM 3160 C9 CLR A1203 -7.480 8.730 12.145 1.00 26.61 C HETATM 3161 C10 CLR A1203 -7.692 10.247 12.028 1.00 29.38 C HETATM 3162 C11 CLR A1203 -8.794 7.943 12.301 1.00 27.05 C HETATM 3163 C12 CLR A1203 -8.529 6.440 12.495 1.00 22.64 C HETATM 3164 C13 CLR A1203 -7.846 5.880 11.250 1.00 27.12 C HETATM 3165 C14 CLR A1203 -6.537 6.655 11.141 1.00 31.96 C HETATM 3166 C15 CLR A1203 -5.643 5.861 10.184 1.00 27.95 C HETATM 3167 C16 CLR A1203 -6.105 4.416 10.387 1.00 27.58 C HETATM 3168 C17 CLR A1203 -7.362 4.437 11.301 1.00 25.18 C HETATM 3169 C18 CLR A1203 -8.720 6.100 10.011 1.00 27.83 C HETATM 3170 C19 CLR A1203 -8.735 10.521 10.935 1.00 27.59 C HETATM 3171 C20 CLR A1203 -8.351 3.304 10.961 1.00 26.46 C HETATM 3172 C21 CLR A1203 -9.577 3.321 11.868 1.00 29.50 C HETATM 3173 C22 CLR A1203 -7.664 1.965 11.185 1.00 26.41 C HETATM 3174 C23 CLR A1203 -8.475 0.704 10.891 1.00 27.99 C HETATM 3175 C24 CLR A1203 -7.629 -0.502 11.317 1.00 35.28 C HETATM 3176 C25 CLR A1203 -8.291 -1.879 11.190 1.00 43.60 C HETATM 3177 C26 CLR A1203 -9.225 -2.166 12.350 1.00 36.05 C HETATM 3178 C27 CLR A1203 -8.994 -2.077 9.855 1.00 50.42 C HETATM 3179 O1 CLR A1203 -6.923 14.392 13.006 1.00 32.11 O HETATM 3180 C1 CLR A1204 -3.097 8.095 21.211 1.00 24.44 C HETATM 3181 C2 CLR A1204 -2.923 9.622 21.166 1.00 24.63 C HETATM 3182 C3 CLR A1204 -1.931 9.992 20.065 1.00 25.23 C HETATM 3183 C4 CLR A1204 -2.451 9.477 18.710 1.00 24.57 C HETATM 3184 C5 CLR A1204 -2.687 7.999 18.769 1.00 21.39 C HETATM 3185 C6 CLR A1204 -2.123 7.184 17.839 1.00 27.64 C HETATM 3186 C7 CLR A1204 -2.419 5.702 17.681 1.00 26.79 C HETATM 3187 C8 CLR A1204 -3.571 5.271 18.593 1.00 24.17 C HETATM 3188 C9 CLR A1204 -3.485 5.957 19.964 1.00 21.89 C HETATM 3189 C10 CLR A1204 -3.572 7.485 19.877 1.00 23.39 C HETATM 3190 C11 CLR A1204 -4.556 5.420 20.919 1.00 26.23 C HETATM 3191 C12 CLR A1204 -4.617 3.901 21.012 1.00 26.52 C HETATM 3192 C13 CLR A1204 -4.708 3.232 19.639 1.00 27.61 C HETATM 3193 C14 CLR A1204 -3.541 3.753 18.801 1.00 26.05 C HETATM 3194 C15 CLR A1204 -3.583 2.889 17.534 1.00 28.62 C HETATM 3195 C16 CLR A1204 -4.097 1.529 18.006 1.00 25.92 C HETATM 3196 C17 CLR A1204 -4.456 1.725 19.493 1.00 28.18 C HETATM 3197 C18 CLR A1204 -6.088 3.575 19.007 1.00 22.86 C HETATM 3198 C19 CLR A1204 -5.004 7.955 19.559 1.00 23.04 C HETATM 3199 C20 CLR A1204 -5.574 0.743 19.891 1.00 29.65 C HETATM 3200 C21 CLR A1204 -5.990 0.844 21.368 1.00 26.94 C HETATM 3201 C22 CLR A1204 -5.091 -0.692 19.614 1.00 34.69 C HETATM 3202 C23 CLR A1204 -6.234 -1.701 19.542 1.00 41.40 C HETATM 3203 C24 CLR A1204 -5.737 -3.057 20.029 1.00 52.49 C HETATM 3204 C25 CLR A1204 -5.123 -3.869 18.910 1.00 55.95 C HETATM 3205 C26 CLR A1204 -4.871 -5.285 19.395 1.00 59.64 C HETATM 3206 C27 CLR A1204 -6.051 -3.858 17.712 1.00 59.48 C HETATM 3207 O1 CLR A1204 -1.880 11.409 20.013 1.00 24.64 O HETATM 3208 C1 CLR A1205 -17.316 11.644 1.385 0.67 52.99 C HETATM 3209 C2 CLR A1205 -17.340 13.149 1.168 0.67 53.67 C HETATM 3210 C3 CLR A1205 -16.006 13.761 1.547 0.67 51.17 C HETATM 3211 C4 CLR A1205 -14.940 13.236 0.599 0.67 50.24 C HETATM 3212 C5 CLR A1205 -14.928 11.723 0.636 0.67 55.31 C HETATM 3213 C6 CLR A1205 -13.733 11.102 0.692 0.67 56.55 C HETATM 3214 C7 CLR A1205 -13.550 9.603 0.685 0.67 56.37 C HETATM 3215 C8 CLR A1205 -14.856 8.874 0.402 0.67 59.75 C HETATM 3216 C9 CLR A1205 -16.041 9.544 1.094 0.67 58.21 C HETATM 3217 C10 CLR A1205 -16.235 10.957 0.568 0.67 57.54 C HETATM 3218 C11 CLR A1205 -17.338 8.734 0.958 0.67 58.24 C HETATM 3219 C12 CLR A1205 -17.167 7.255 1.318 0.67 61.44 C HETATM 3220 C13 CLR A1205 -16.006 6.638 0.545 0.67 66.74 C HETATM 3221 C14 CLR A1205 -14.769 7.435 0.898 0.67 66.29 C HETATM 3222 C15 CLR A1205 -13.599 6.592 0.410 0.67 67.94 C HETATM 3223 C16 CLR A1205 -14.072 5.167 0.690 0.67 67.83 C HETATM 3224 C17 CLR A1205 -15.586 5.217 0.921 0.67 69.46 C HETATM 3225 C18 CLR A1205 -16.245 6.728 -0.964 0.67 70.16 C HETATM 3226 C19 CLR A1205 -16.704 10.893 -0.883 0.67 63.43 C HETATM 3227 C20 CLR A1205 -16.261 4.069 0.172 0.67 74.91 C HETATM 3228 C21 CLR A1205 -17.770 3.988 0.378 0.67 76.95 C HETATM 3229 C22 CLR A1205 -15.633 2.741 0.582 0.67 76.69 C HETATM 3230 C23 CLR A1205 -16.480 1.580 0.066 0.67 78.25 C HETATM 3231 C24 CLR A1205 -15.873 0.217 0.382 0.67 78.62 C HETATM 3232 C25 CLR A1205 -16.401 -0.826 -0.599 0.67 78.15 C HETATM 3233 C26 CLR A1205 -15.683 -2.168 -0.447 0.67 77.39 C HETATM 3234 C27 CLR A1205 -17.907 -0.976 -0.438 0.67 77.95 C HETATM 3235 O1 CLR A1205 -16.116 15.187 1.451 0.67 52.83 O HETATM 3236 C1 OLA A1206 3.493 18.699 15.656 1.00 66.00 C HETATM 3237 O1 OLA A1206 2.679 18.295 16.514 1.00 67.44 O HETATM 3238 O2 OLA A1206 4.406 19.506 15.958 1.00 67.14 O HETATM 3239 C2 OLA A1206 3.358 18.200 14.214 1.00 61.41 C HETATM 3240 C3 OLA A1206 2.555 16.896 14.157 1.00 56.53 C HETATM 3241 C4 OLA A1206 3.230 15.784 13.336 1.00 52.04 C HETATM 3242 C5 OLA A1206 2.510 14.444 13.543 1.00 43.93 C HETATM 3243 C6 OLA A1206 3.186 13.317 12.765 1.00 42.06 C HETATM 3244 C7 OLA A1206 2.598 11.942 13.097 1.00 40.59 C HETATM 3245 C8 OLA A1206 3.350 10.837 12.361 1.00 38.19 C HETATM 3246 C9 OLA A1206 2.643 9.506 12.442 1.00 38.60 C HETATM 3247 C10 OLA A1206 3.115 8.492 11.716 1.00 40.82 C HETATM 3248 C11 OLA A1206 2.470 7.124 11.756 1.00 36.84 C HETATM 3249 C12 OLA A1206 3.331 6.153 10.958 1.00 37.90 C HETATM 3250 C13 OLA A1206 2.738 4.756 10.970 1.00 46.89 C HETATM 3251 C14 OLA A1206 2.291 4.306 9.592 1.00 54.83 C HETATM 3252 C15 OLA A1206 1.114 3.353 9.744 1.00 56.52 C HETATM 3253 C16 OLA A1206 1.478 2.099 10.530 1.00 57.20 C HETATM 3254 C17 OLA A1206 0.218 1.298 10.854 1.00 60.55 C HETATM 3255 C18 OLA A1206 0.547 -0.076 11.409 1.00 59.15 C HETATM 3256 C1 OLA A1207 0.342 16.786 19.609 1.00 72.81 C HETATM 3257 O1 OLA A1207 -0.168 16.715 20.757 1.00 76.13 O HETATM 3258 O2 OLA A1207 0.495 17.874 19.005 1.00 78.62 O HETATM 3259 C2 OLA A1207 0.794 15.513 18.918 1.00 57.24 C HETATM 3260 C3 OLA A1207 -0.140 15.191 17.768 1.00 47.24 C HETATM 3261 C4 OLA A1207 0.367 14.007 16.984 1.00 37.46 C HETATM 3262 C5 OLA A1207 0.368 12.749 17.829 1.00 37.28 C HETATM 3263 C6 OLA A1207 0.863 11.684 16.857 1.00 36.48 C HETATM 3264 C7 OLA A1207 1.388 10.471 17.595 1.00 36.60 C HETATM 3265 C8 OLA A1207 1.381 9.298 16.638 1.00 31.68 C HETATM 3266 C9 OLA A1207 1.831 8.045 17.317 1.00 32.14 C HETATM 3267 C10 OLA A1207 1.901 7.032 16.479 1.00 38.10 C HETATM 3268 C11 OLA A1207 2.358 5.683 16.927 1.00 41.18 C HETATM 3269 C12 OLA A1207 1.344 4.750 16.348 1.00 44.70 C HETATM 3270 C13 OLA A1207 1.914 3.998 15.196 1.00 41.18 C HETATM 3271 C14 OLA A1207 0.929 2.901 14.849 1.00 46.31 C HETATM 3272 C15 OLA A1207 0.743 1.902 15.982 1.00 50.97 C HETATM 3273 C16 OLA A1207 0.103 0.619 15.444 1.00 50.53 C HETATM 3274 C17 OLA A1207 -0.351 -0.294 16.585 1.00 51.79 C HETATM 3275 C18 OLA A1207 -1.031 -1.548 16.069 1.00 53.61 C HETATM 3276 C1 OLA A1208 -1.431 17.841 15.075 1.00 70.99 C HETATM 3277 O1 OLA A1208 -0.560 17.904 15.969 1.00 76.83 O HETATM 3278 O2 OLA A1208 -2.331 18.704 14.920 1.00 70.92 O HETATM 3279 C2 OLA A1208 -1.378 16.655 14.143 1.00 64.86 C HETATM 3280 C3 OLA A1208 -2.791 16.127 13.970 1.00 60.45 C HETATM 3281 C4 OLA A1208 -2.817 14.791 13.246 1.00 52.93 C HETATM 3282 C5 OLA A1208 -1.976 13.798 14.016 1.00 47.76 C HETATM 3283 C6 OLA A1208 -1.846 12.565 13.153 1.00 44.55 C HETATM 3284 C7 OLA A1208 -2.153 11.289 13.909 1.00 37.24 C HETATM 3285 C8 OLA A1208 -1.513 10.175 13.111 1.00 40.31 C HETATM 3286 C9 OLA A1208 -1.830 8.834 13.677 1.00 42.64 C HETATM 3287 C10 OLA A1208 -1.358 7.764 13.044 1.00 46.66 C HETATM 3288 C11 OLA A1208 -1.647 6.384 13.567 1.00 42.18 C HETATM 3289 C12 OLA A1208 -1.999 5.468 12.410 1.00 40.81 C HETATM 3290 C13 OLA A1208 -2.372 4.102 12.965 1.00 44.15 C HETATM 3291 C14 OLA A1208 -3.861 3.986 13.207 1.00 42.07 C HETATM 3292 C15 OLA A1208 -4.187 2.782 14.071 1.00 44.53 C HETATM 3293 C16 OLA A1208 -4.014 1.449 13.358 1.00 44.81 C HETATM 3294 C17 OLA A1208 -3.975 0.352 14.394 1.00 45.04 C HETATM 3295 C18 OLA A1208 -4.486 -0.962 13.849 1.00 50.03 C HETATM 3296 C1 OLA A1209 -1.879 12.212 25.914 1.00 49.53 C HETATM 3297 O1 OLA A1209 -1.413 11.946 27.036 1.00 55.51 O HETATM 3298 O2 OLA A1209 -1.899 13.363 25.425 1.00 47.14 O HETATM 3299 C2 OLA A1209 -2.418 11.040 25.138 1.00 43.32 C HETATM 3300 C3 OLA A1209 -2.179 9.781 25.937 1.00 30.90 C HETATM 3301 C4 OLA A1209 -2.551 8.626 25.039 1.00 28.59 C HETATM 3302 C5 OLA A1209 -2.730 7.359 25.851 1.00 33.00 C HETATM 3303 C6 OLA A1209 -3.131 6.263 24.880 1.00 29.45 C HETATM 3304 C7 OLA A1209 -3.272 4.893 25.534 1.00 35.57 C HETATM 3305 C8 OLA A1209 -3.478 3.816 24.483 1.00 40.36 C HETATM 3306 C9 OLA A1209 -3.285 2.460 25.106 1.00 43.51 C HETATM 3307 C10 OLA A1209 -3.686 1.334 24.526 1.00 46.94 C HETATM 3308 C11 OLA A1209 -3.406 0.063 25.293 1.00 52.96 C HETATM 3309 C12 OLA A1209 -4.064 -1.158 24.670 1.00 59.97 C HETATM 3310 C13 OLA A1209 -3.323 -2.392 25.188 1.00 66.46 C HETATM 3311 C14 OLA A1209 -3.870 -3.714 24.663 1.00 70.24 C HETATM 3312 C15 OLA A1209 -3.715 -3.840 23.152 1.00 74.96 C HETATM 3313 C16 OLA A1209 -3.414 -5.283 22.741 1.00 79.47 C HETATM 3314 C17 OLA A1209 -2.317 -5.926 23.596 1.00 77.80 C HETATM 3315 C18 OLA A1209 -1.854 -7.238 23.003 1.00 73.47 C HETATM 3316 C1 OLA A1210 -34.124 -21.952 18.542 1.00 63.91 C HETATM 3317 O1 OLA A1210 -34.245 -22.989 19.246 1.00 64.51 O HETATM 3318 O2 OLA A1210 -33.476 -21.887 17.485 1.00 66.06 O HETATM 3319 C2 OLA A1210 -34.797 -20.668 18.925 1.00 61.20 C HETATM 3320 C3 OLA A1210 -34.996 -19.979 17.592 1.00 53.84 C HETATM 3321 C4 OLA A1210 -35.870 -18.749 17.756 1.00 53.06 C HETATM 3322 C5 OLA A1210 -35.224 -17.715 18.661 1.00 49.34 C HETATM 3323 C6 OLA A1210 -35.509 -16.347 18.067 1.00 52.39 C HETATM 3324 C7 OLA A1210 -35.392 -15.276 19.130 1.00 57.25 C HETATM 3325 C8 OLA A1210 -34.793 -14.011 18.535 1.00 57.37 C HETATM 3326 C9 OLA A1210 -35.744 -13.378 17.565 1.00 57.11 C HETATM 3327 C10 OLA A1210 -35.925 -12.055 17.553 1.00 61.56 C HETATM 3328 C11 OLA A1210 -35.189 -11.116 18.475 1.00 63.33 C HETATM 3329 C12 OLA A1210 -36.134 -10.528 19.528 1.00 70.08 C HETATM 3330 C13 OLA A1210 -37.392 -9.887 18.938 1.00 73.93 C HETATM 3331 C14 OLA A1210 -38.516 -9.708 19.968 1.00 75.80 C HETATM 3332 C15 OLA A1210 -39.796 -9.194 19.292 1.00 79.70 C HETATM 3333 C16 OLA A1210 -41.079 -9.436 20.099 1.00 80.64 C HETATM 3334 C17 OLA A1210 -42.320 -8.807 19.455 1.00 78.21 C HETATM 3335 C18 OLA A1210 -42.793 -9.578 18.239 1.00 77.17 C HETATM 3336 C1 OLA A1211 -31.980 -21.137 23.275 1.00 67.61 C HETATM 3337 O1 OLA A1211 -32.277 -22.014 24.129 1.00 69.30 O HETATM 3338 O2 OLA A1211 -31.787 -21.383 22.062 1.00 72.64 O HETATM 3339 C2 OLA A1211 -31.841 -19.699 23.704 1.00 62.77 C HETATM 3340 C3 OLA A1211 -31.276 -18.894 22.546 1.00 52.91 C HETATM 3341 C4 OLA A1211 -32.306 -17.856 22.146 1.00 48.36 C HETATM 3342 C5 OLA A1211 -31.813 -16.475 22.514 1.00 42.37 C HETATM 3343 C6 OLA A1211 -32.817 -15.403 22.107 1.00 49.07 C HETATM 3344 C7 OLA A1211 -32.330 -14.104 22.724 1.00 47.57 C HETATM 3345 C8 OLA A1211 -33.189 -12.912 22.386 1.00 49.44 C HETATM 3346 C9 OLA A1211 -33.925 -12.660 23.657 1.00 58.01 C HETATM 3347 C10 OLA A1211 -33.992 -11.455 24.201 1.00 56.26 C HETATM 3348 C11 OLA A1211 -33.399 -10.219 23.595 1.00 44.09 C HETATM 3349 C12 OLA A1211 -33.769 -9.111 24.576 1.00 45.91 C HETATM 3350 C13 OLA A1211 -33.652 -7.722 23.969 1.00 51.08 C HETATM 3351 C14 OLA A1211 -34.944 -7.360 23.248 1.00 60.65 C HETATM 3352 C15 OLA A1211 -35.263 -5.877 23.415 1.00 61.80 C HETATM 3353 C16 OLA A1211 -36.513 -5.502 22.639 1.00 59.01 C HETATM 3354 C17 OLA A1211 -36.971 -4.123 23.085 1.00 60.88 C HETATM 3355 C18 OLA A1211 -35.825 -3.147 23.276 1.00 60.58 C HETATM 3356 C1 OLA A1212 -7.414 6.877 33.526 1.00 52.75 C HETATM 3357 O1 OLA A1212 -6.183 6.961 33.683 1.00 56.51 O HETATM 3358 O2 OLA A1212 -8.155 7.889 33.506 1.00 56.69 O HETATM 3359 C2 OLA A1212 -8.028 5.508 33.381 1.00 46.81 C HETATM 3360 C3 OLA A1212 -7.094 4.510 32.689 1.00 43.55 C HETATM 3361 C4 OLA A1212 -7.598 3.107 32.984 1.00 44.77 C HETATM 3362 C5 OLA A1212 -7.624 2.109 31.836 1.00 49.25 C HETATM 3363 C6 OLA A1212 -8.368 0.873 32.343 1.00 50.62 C HETATM 3364 C7 OLA A1212 -8.789 -0.120 31.271 1.00 45.98 C HETATM 3365 C8 OLA A1212 -9.660 -1.233 31.839 1.00 44.88 C HETATM 3366 C9 OLA A1212 -9.206 -2.554 31.269 1.00 53.18 C HETATM 3367 C10 OLA A1212 -9.362 -3.727 31.911 1.00 59.62 C HETATM 3368 C11 OLA A1212 -10.039 -3.895 33.262 1.00 58.79 C HETATM 3369 C12 OLA A1212 -10.625 -5.312 33.401 1.00 53.50 C HETATM 3370 C13 OLA A1212 -12.081 -5.352 32.956 1.00 48.26 C HETATM 3371 C14 OLA A1212 -12.648 -6.745 32.718 1.00 51.94 C HETATM 3372 C15 OLA A1212 -14.074 -6.649 32.161 1.00 56.61 C HETATM 3373 C16 OLA A1212 -14.575 -7.982 31.593 1.00 59.30 C HETATM 3374 C17 OLA A1212 -15.639 -7.844 30.496 1.00 55.46 C HETATM 3375 C18 OLA A1212 -16.937 -7.223 30.966 1.00 51.69 C HETATM 3376 C1 OLA A1213 -4.188 -24.274 13.008 1.00 61.10 C HETATM 3377 O1 OLA A1213 -3.466 -24.816 13.887 1.00 62.28 O HETATM 3378 O2 OLA A1213 -4.606 -24.906 12.007 1.00 60.99 O HETATM 3379 C2 OLA A1213 -4.611 -22.822 13.118 1.00 55.73 C HETATM 3380 C3 OLA A1213 -3.796 -21.947 14.080 1.00 57.27 C HETATM 3381 C4 OLA A1213 -4.232 -20.484 13.862 1.00 61.85 C HETATM 3382 C5 OLA A1213 -3.941 -19.516 15.019 1.00 66.85 C HETATM 3383 C6 OLA A1213 -4.760 -18.205 14.964 1.00 67.91 C HETATM 3384 C7 OLA A1213 -5.968 -18.197 15.918 1.00 66.64 C HETATM 3385 C8 OLA A1213 -6.580 -16.816 16.199 1.00 62.69 C HETATM 3386 C9 OLA A1213 -7.811 -16.549 15.354 1.00 61.86 C HETATM 3387 C10 OLA A1213 -8.879 -15.835 15.743 1.00 60.69 C HETATM 3388 C11 OLA A1213 -9.032 -15.162 17.093 1.00 55.84 C HETATM 3389 C12 OLA A1213 -10.392 -14.467 17.231 1.00 50.52 C HETATM 3390 C13 OLA A1213 -10.371 -12.948 17.037 1.00 52.72 C HETATM 3391 C14 OLA A1213 -9.932 -12.125 18.244 1.00 48.39 C HETATM 3392 C15 OLA A1213 -9.610 -10.695 17.819 1.00 46.78 C HETATM 3393 C16 OLA A1213 -8.564 -10.017 18.715 1.00 50.98 C HETATM 3394 C17 OLA A1213 -8.219 -8.606 18.229 1.00 51.49 C HETATM 3395 C18 OLA A1213 -8.328 -7.558 19.331 1.00 46.54 C HETATM 3396 C1 OLA A1214 -20.879 -23.244 27.634 1.00 64.56 C HETATM 3397 O1 OLA A1214 -21.276 -23.589 26.504 1.00 72.19 O HETATM 3398 O2 OLA A1214 -21.355 -23.682 28.710 1.00 70.31 O HETATM 3399 C2 OLA A1214 -19.765 -22.245 27.669 1.00 50.72 C HETATM 3400 C3 OLA A1214 -20.280 -21.014 28.362 1.00 47.87 C HETATM 3401 C4 OLA A1214 -19.539 -20.833 29.667 1.00 51.89 C HETATM 3402 C5 OLA A1214 -18.838 -19.493 29.611 1.00 49.98 C HETATM 3403 C6 OLA A1214 -19.805 -18.386 29.261 1.00 44.50 C HETATM 3404 C7 OLA A1214 -18.983 -17.144 28.964 1.00 49.18 C HETATM 3405 C8 OLA A1214 -19.788 -15.866 29.070 1.00 49.72 C HETATM 3406 C9 OLA A1214 -19.183 -14.944 28.052 1.00 49.60 C HETATM 3407 C1 OLA A1215 -25.467 13.158 8.324 1.00 71.07 C HETATM 3408 O1 OLA A1215 -24.988 14.137 8.933 1.00 74.89 O HETATM 3409 O2 OLA A1215 -26.701 12.983 8.221 1.00 75.80 O HETATM 3410 C2 OLA A1215 -24.534 12.146 7.694 1.00 65.81 C HETATM 3411 C3 OLA A1215 -23.472 12.845 6.854 1.00 62.61 C HETATM 3412 C4 OLA A1215 -23.368 12.243 5.460 1.00 63.40 C HETATM 3413 C5 OLA A1215 -22.594 10.941 5.475 1.00 62.44 C HETATM 3414 C6 OLA A1215 -22.489 10.400 4.061 1.00 60.96 C HETATM 3415 C7 OLA A1215 -21.183 9.639 3.941 1.00 56.93 C HETATM 3416 C8 OLA A1215 -21.401 8.267 3.336 1.00 58.09 C HETATM 3417 C9 OLA A1215 -21.314 7.195 4.403 1.00 59.57 C HETATM 3418 C10 OLA A1215 -21.793 5.959 4.206 1.00 58.43 C HETATM 3419 C11 OLA A1215 -22.473 5.539 2.923 1.00 56.13 C HETATM 3420 C12 OLA A1215 -21.479 5.092 1.852 1.00 54.73 C HETATM 3421 C13 OLA A1215 -20.561 4.028 2.409 1.00 55.92 C HETATM 3422 C14 OLA A1215 -20.787 2.660 1.779 1.00 57.48 C HETATM 3423 C15 OLA A1215 -20.397 1.645 2.844 1.00 62.13 C HETATM 3424 C16 OLA A1215 -20.744 0.210 2.480 1.00 66.38 C HETATM 3425 C17 OLA A1215 -20.416 -0.710 3.655 1.00 66.73 C HETATM 3426 C18 OLA A1215 -18.951 -0.620 4.045 1.00 63.57 C HETATM 3427 C1 OLA A1216 -4.532 10.375 29.777 1.00 77.44 C HETATM 3428 O1 OLA A1216 -3.556 11.035 30.198 1.00 79.14 O HETATM 3429 O2 OLA A1216 -5.511 10.873 29.162 1.00 80.74 O HETATM 3430 C2 OLA A1216 -4.538 8.890 30.021 1.00 67.98 C HETATM 3431 C3 OLA A1216 -3.233 8.419 30.635 1.00 62.36 C HETATM 3432 C4 OLA A1216 -3.014 6.981 30.193 1.00 60.88 C HETATM 3433 C5 OLA A1216 -4.350 6.273 30.257 1.00 61.64 C HETATM 3434 C6 OLA A1216 -4.379 5.029 29.400 1.00 58.43 C HETATM 3435 C7 OLA A1216 -4.023 3.828 30.247 1.00 57.95 C HETATM 3436 C8 OLA A1216 -4.138 2.604 29.362 1.00 62.58 C HETATM 3437 C9 OLA A1216 -3.264 1.517 29.938 1.00 73.43 C HETATM 3438 C10 OLA A1216 -3.484 0.260 29.590 1.00 79.72 C HETATM 3439 C11 OLA A1216 -4.600 0.023 28.615 1.00 86.09 C HETATM 3440 C12 OLA A1216 -5.842 -0.408 29.387 1.00 91.17 C HETATM 3441 C13 OLA A1216 -5.584 -1.608 30.293 1.00 91.74 C HETATM 3442 C14 OLA A1216 -6.177 -2.855 29.653 1.00 89.72 C HETATM 3443 C15 OLA A1216 -5.419 -3.186 28.374 1.00 86.00 C HETATM 3444 C16 OLA A1216 -6.347 -3.211 27.177 1.00 82.54 C HETATM 3445 C17 OLA A1216 -6.651 -4.654 26.797 1.00 84.96 C HETATM 3446 C18 OLA A1216 -5.873 -5.663 27.621 1.00 86.90 C HETATM 3447 C1 OLA A1217 -34.214 10.808 3.141 0.64 56.93 C HETATM 3448 O1 OLA A1217 -35.225 10.643 3.848 0.64 58.08 O HETATM 3449 O2 OLA A1217 -33.654 11.920 3.029 0.64 57.91 O HETATM 3450 C2 OLA A1217 -33.663 9.610 2.399 0.64 53.50 C HETATM 3451 C3 OLA A1217 -34.800 8.613 2.237 0.64 51.98 C HETATM 3452 C4 OLA A1217 -34.619 7.713 1.014 0.64 53.26 C HETATM 3453 C5 OLA A1217 -35.363 6.393 1.243 0.64 53.75 C HETATM 3454 C6 OLA A1217 -34.782 5.228 0.440 0.64 55.04 C HETATM 3455 C7 OLA A1217 -34.958 3.884 1.157 0.64 57.14 C HETATM 3456 C8 OLA A1217 -34.078 2.779 0.561 0.64 59.52 C HETATM 3457 C9 OLA A1217 -33.963 1.594 1.507 0.64 60.71 C HETATM 3458 C10 OLA A1217 -33.722 0.340 1.089 0.64 60.00 C HETATM 3459 C11 OLA A1217 -33.529 0.012 -0.376 0.64 60.30 C HETATM 3460 C12 OLA A1217 -33.342 -1.499 -0.521 0.64 60.76 C HETATM 3461 C13 OLA A1217 -34.652 -2.292 -0.382 0.64 59.50 C HETATM 3462 C14 OLA A1217 -34.448 -3.758 -0.781 0.64 57.48 C HETATM 3463 C15 OLA A1217 -35.679 -4.647 -0.595 0.64 55.16 C HETATM 3464 C16 OLA A1217 -35.343 -6.124 -0.821 0.64 53.97 C HETATM 3465 C17 OLA A1217 -34.644 -6.369 -2.161 0.64 53.32 C HETATM 3466 C18 OLA A1217 -34.241 -7.825 -2.345 0.64 53.10 C HETATM 3467 C1 OLA A1218 -7.915 14.734 9.267 1.00 68.82 C HETATM 3468 O1 OLA A1218 -6.777 15.180 9.599 1.00 75.81 O HETATM 3469 O2 OLA A1218 -8.881 14.688 10.080 1.00 61.40 O HETATM 3470 C2 OLA A1218 -8.118 14.255 7.833 1.00 60.39 C HETATM 3471 C3 OLA A1218 -8.895 12.945 7.817 1.00 57.02 C HETATM 3472 C4 OLA A1218 -8.546 12.088 6.608 1.00 58.28 C HETATM 3473 C5 OLA A1218 -8.190 10.662 7.018 1.00 54.88 C HETATM 3474 C6 OLA A1218 -8.825 9.643 6.083 1.00 52.92 C HETATM 3475 C7 OLA A1218 -8.442 8.208 6.443 1.00 54.14 C HETATM 3476 C8 OLA A1218 -9.313 7.304 5.580 1.00 59.51 C HETATM 3477 C9 OLA A1218 -8.861 5.862 5.541 1.00 65.19 C HETATM 3478 C10 OLA A1218 -9.698 4.936 5.062 1.00 65.30 C HETATM 3479 C11 OLA A1218 -11.077 5.328 4.571 1.00 63.78 C HETATM 3480 C12 OLA A1218 -11.374 4.772 3.179 1.00 62.32 C HETATM 3481 C13 OLA A1218 -11.235 3.256 3.111 1.00 64.06 C HETATM 3482 C1 OLA A1219 -0.549 13.663 9.633 1.00 84.32 C HETATM 3483 O1 OLA A1219 -1.118 14.624 10.198 1.00 88.73 O HETATM 3484 O2 OLA A1219 0.693 13.578 9.526 1.00 88.97 O HETATM 3485 C2 OLA A1219 -1.399 12.564 9.042 1.00 75.65 C HETATM 3486 C3 OLA A1219 -0.748 11.198 9.241 1.00 70.96 C HETATM 3487 C4 OLA A1219 -1.756 10.141 8.810 1.00 66.95 C HETATM 3488 C5 OLA A1219 -1.162 8.745 8.781 1.00 62.36 C HETATM 3489 C6 OLA A1219 -2.173 7.820 8.123 1.00 58.79 C HETATM 3490 C7 OLA A1219 -1.722 6.363 8.169 1.00 61.87 C HETATM 3491 C8 OLA A1219 -2.823 5.430 7.668 1.00 65.44 C HETATM 3492 C9 OLA A1219 -2.181 4.137 7.235 1.00 72.53 C HETATM 3493 C10 OLA A1219 -2.585 2.926 7.620 1.00 74.63 C HETATM 3494 C11 OLA A1219 -3.756 2.705 8.538 1.00 75.25 C HETATM 3495 C12 OLA A1219 -4.334 1.300 8.354 1.00 75.83 C HETATM 3496 C13 OLA A1219 -3.475 0.247 9.051 1.00 74.94 C HETATM 3497 C14 OLA A1219 -4.211 -1.080 9.228 1.00 75.62 C HETATM 3498 C15 OLA A1219 -4.514 -1.763 7.892 1.00 80.29 C HETATM 3499 C16 OLA A1219 -5.446 -2.975 8.038 1.00 80.32 C HETATM 3500 C17 OLA A1219 -6.111 -3.369 6.717 1.00 76.42 C HETATM 3501 C18 OLA A1219 -7.078 -4.524 6.890 1.00 73.41 C HETATM 3502 C1 OLA A1220 4.751 13.106 8.104 1.00 74.56 C HETATM 3503 O1 OLA A1220 3.664 13.621 8.462 1.00 75.53 O HETATM 3504 O2 OLA A1220 5.749 13.791 7.768 1.00 76.11 O HETATM 3505 C2 OLA A1220 4.881 11.597 8.071 1.00 69.53 C HETATM 3506 C3 OLA A1220 3.681 10.902 8.704 1.00 64.68 C HETATM 3507 C4 OLA A1220 2.844 10.188 7.656 1.00 61.67 C HETATM 3508 C5 OLA A1220 3.363 8.802 7.281 1.00 57.85 C HETATM 3509 C6 OLA A1220 2.536 8.306 6.098 1.00 57.58 C HETATM 3510 C7 OLA A1220 2.775 6.844 5.768 1.00 58.17 C HETATM 3511 C8 OLA A1220 1.495 6.033 5.913 1.00 61.00 C HETATM 3512 C9 OLA A1220 1.646 4.729 5.167 1.00 64.72 C HETATM 3513 C10 OLA A1220 0.896 3.662 5.447 1.00 67.41 C HETATM 3514 C11 OLA A1220 1.120 2.398 4.641 1.00 66.61 C HETATM 3515 C12 OLA A1220 0.255 1.239 5.126 1.00 64.20 C HETATM 3516 C13 OLA A1220 0.580 0.791 6.543 1.00 66.55 C HETATM 3517 C14 OLA A1220 1.894 0.015 6.633 1.00 69.42 C HETATM 3518 C15 OLA A1220 2.115 -0.475 8.068 1.00 68.73 C HETATM 3519 C16 OLA A1220 3.449 -1.174 8.308 1.00 63.67 C HETATM 3520 C17 OLA A1220 3.158 -2.619 8.661 1.00 63.29 C HETATM 3521 C18 OLA A1220 2.403 -3.289 7.535 1.00 63.73 C HETATM 3522 C1 OLA A1221 -20.186 -19.135 15.699 1.00 65.27 C HETATM 3523 O1 OLA A1221 -21.169 -18.385 15.516 1.00 68.36 O HETATM 3524 O2 OLA A1221 -19.040 -18.655 15.760 1.00 68.94 O HETATM 3525 C2 OLA A1221 -20.369 -20.638 15.887 1.00 63.61 C HETATM 3526 C3 OLA A1221 -20.042 -21.469 14.659 1.00 58.47 C HETATM 3527 C4 OLA A1221 -19.523 -22.821 15.131 1.00 62.46 C HETATM 3528 C5 OLA A1221 -18.674 -23.497 14.061 1.00 61.85 C HETATM 3529 C6 OLA A1221 -19.296 -24.826 13.629 1.00 66.71 C HETATM 3530 C7 OLA A1221 -18.743 -25.218 12.263 1.00 67.78 C HETATM 3531 C8 OLA A1221 -19.070 -26.637 11.820 1.00 66.40 C HETATM 3532 C9 OLA A1221 -17.975 -27.036 10.861 1.00 64.76 C HETATM 3533 C10 OLA A1221 -18.226 -27.818 9.818 1.00 66.86 C HETATM 3534 C11 OLA A1221 -19.624 -28.299 9.544 1.00 64.15 C HETATM 3535 C12 OLA A1221 -19.685 -28.945 8.172 1.00 59.17 C HETATM 3536 C13 OLA A1221 -18.944 -28.173 7.093 1.00 53.86 C HETATM 3537 C14 OLA A1221 -19.041 -28.918 5.759 1.00 60.60 C HETATM 3538 C15 OLA A1221 -17.593 -29.240 5.337 1.00 66.15 C HETATM 3539 C16 OLA A1221 -16.915 -30.196 6.320 1.00 63.91 C HETATM 3540 C17 OLA A1221 -15.486 -29.756 6.638 1.00 61.55 C HETATM 3541 C18 OLA A1221 -15.080 -30.226 8.019 1.00 54.53 C HETATM 3542 C1 OLA A1222 -29.302 12.454 -2.961 1.00 61.06 C HETATM 3543 O1 OLA A1222 -28.928 11.356 -3.446 1.00 62.73 O HETATM 3544 O2 OLA A1222 -28.480 13.347 -2.674 1.00 69.63 O HETATM 3545 C2 OLA A1222 -30.770 12.729 -2.685 1.00 48.95 C HETATM 3546 C3 OLA A1222 -31.000 14.213 -2.432 1.00 43.52 C HETATM 3547 C4 OLA A1222 -32.463 14.510 -2.118 1.00 46.62 C HETATM 3548 S SCN A1223 -14.070 13.838 26.517 1.00 60.81 S HETATM 3549 C SCN A1223 -14.788 12.822 27.699 1.00 52.22 C HETATM 3550 N SCN A1223 -15.273 12.148 28.508 1.00 29.19 N HETATM 3551 S SCN A1224 -10.197 14.785 25.306 1.00 58.80 S HETATM 3552 C SCN A1224 -11.063 15.100 23.876 1.00 50.02 C HETATM 3553 N SCN A1224 -11.650 15.308 22.903 1.00 46.55 N HETATM 3554 S SCN A1225 -30.766 20.202 3.557 1.00 62.70 S HETATM 3555 C SCN A1225 -31.220 21.710 2.964 1.00 48.54 C HETATM 3556 N SCN A1225 -31.539 22.731 2.571 1.00 37.86 N HETATM 3557 S SCN A1226 -19.849 12.158 33.051 1.00 77.95 S HETATM 3558 C SCN A1226 -18.193 12.061 32.747 1.00 68.61 C HETATM 3559 N SCN A1226 -17.061 11.998 32.544 1.00 64.49 N HETATM 3560 C18 OLC A1227 -33.945 5.314 32.896 1.00 53.49 C HETATM 3561 C10 OLC A1227 -31.004 -3.853 33.530 1.00 55.28 C HETATM 3562 C9 OLC A1227 -31.899 -4.798 33.165 1.00 56.89 C HETATM 3563 C17 OLC A1227 -33.858 3.813 32.700 1.00 55.86 C HETATM 3564 C11 OLC A1227 -30.499 -2.720 32.656 1.00 54.96 C HETATM 3565 C8 OLC A1227 -32.596 -4.932 31.826 1.00 55.77 C HETATM 3566 C24 OLC A1227 -34.445 -17.219 27.125 1.00 72.02 C HETATM 3567 C16 OLC A1227 -32.573 3.209 33.261 1.00 56.41 C HETATM 3568 C12 OLC A1227 -30.280 -1.382 33.370 1.00 50.25 C HETATM 3569 C7 OLC A1227 -33.059 -6.374 31.599 1.00 55.71 C HETATM 3570 C15 OLC A1227 -32.409 1.785 32.735 1.00 56.08 C HETATM 3571 C13 OLC A1227 -31.272 -0.394 32.769 1.00 52.50 C HETATM 3572 C6 OLC A1227 -33.515 -6.609 30.149 1.00 56.36 C HETATM 3573 C14 OLC A1227 -31.099 1.083 33.106 1.00 51.20 C HETATM 3574 C5 OLC A1227 -34.152 -7.981 29.887 1.00 57.97 C HETATM 3575 C4 OLC A1227 -33.195 -9.044 29.343 1.00 57.47 C HETATM 3576 C3 OLC A1227 -33.960 -10.241 28.766 1.00 58.67 C HETATM 3577 C2 OLC A1227 -33.125 -11.523 28.669 1.00 62.48 C HETATM 3578 C21 OLC A1227 -33.849 -14.820 26.714 1.00 63.26 C HETATM 3579 C1 OLC A1227 -33.772 -12.546 27.751 1.00 67.92 C HETATM 3580 C22 OLC A1227 -33.335 -16.181 27.158 1.00 67.33 C HETATM 3581 O19 OLC A1227 -34.882 -12.337 27.297 1.00 73.62 O HETATM 3582 O25 OLC A1227 -33.846 -18.516 27.235 1.00 77.52 O HETATM 3583 O23 OLC A1227 -32.349 -16.627 26.239 1.00 73.94 O HETATM 3584 O20 OLC A1227 -33.112 -13.797 27.374 1.00 63.13 O HETATM 3585 C24 OLC A1228 -36.089 6.328 28.110 1.00 60.56 C HETATM 3586 C2 OLC A1228 -39.455 1.050 28.593 1.00 72.19 C HETATM 3587 C21 OLC A1228 -36.935 3.976 28.080 1.00 73.45 C HETATM 3588 C1 OLC A1228 -38.306 1.864 28.039 1.00 74.63 C HETATM 3589 C22 OLC A1228 -36.771 5.239 28.935 1.00 69.65 C HETATM 3590 O19 OLC A1228 -37.578 1.406 27.171 1.00 73.22 O HETATM 3591 O25 OLC A1228 -36.258 7.614 28.721 1.00 61.98 O HETATM 3592 O23 OLC A1228 -38.045 5.691 29.427 1.00 70.99 O HETATM 3593 O20 OLC A1228 -38.053 3.208 28.546 1.00 75.16 O HETATM 3594 C18 OLC A1229 -22.232 -8.579 3.416 0.46 47.50 C HETATM 3595 C10 OLC A1229 -23.637 -0.702 0.220 0.46 51.49 C HETATM 3596 C9 OLC A1229 -23.754 0.624 0.064 0.46 51.48 C HETATM 3597 C17 OLC A1229 -21.761 -7.539 2.427 0.46 46.57 C HETATM 3598 C11 OLC A1229 -23.755 -1.373 1.580 0.46 49.92 C HETATM 3599 C8 OLC A1229 -23.635 1.287 -1.301 0.46 50.16 C HETATM 3600 C24 OLC A1229 -21.679 12.596 0.314 0.46 49.03 C HETATM 3601 C16 OLC A1229 -21.916 -6.133 2.990 0.46 45.38 C HETATM 3602 C12 OLC A1229 -24.944 -2.336 1.592 0.46 48.27 C HETATM 3603 C7 OLC A1229 -24.818 2.215 -1.581 0.46 48.38 C HETATM 3604 C15 OLC A1229 -23.350 -5.608 2.932 0.46 44.69 C HETATM 3605 C13 OLC A1229 -24.741 -3.539 2.515 0.46 46.58 C HETATM 3606 C6 OLC A1229 -24.460 3.304 -2.595 0.46 46.84 C HETATM 3607 C14 OLC A1229 -23.384 -4.209 2.321 0.46 45.30 C HETATM 3608 C5 OLC A1229 -23.616 4.424 -1.995 0.46 45.48 C HETATM 3609 C4 OLC A1229 -23.099 5.394 -3.057 0.46 44.89 C HETATM 3610 C3 OLC A1229 -22.630 6.713 -2.439 0.46 45.86 C HETATM 3611 C2 OLC A1229 -21.540 7.426 -3.236 0.46 45.82 C HETATM 3612 C21 OLC A1229 -21.645 10.794 -1.369 0.46 47.07 C HETATM 3613 C1 OLC A1229 -21.549 8.913 -2.920 0.46 48.05 C HETATM 3614 C22 OLC A1229 -20.921 11.374 -0.169 0.46 48.03 C HETATM 3615 O19 OLC A1229 -21.863 9.730 -3.767 0.46 48.50 O HETATM 3616 O25 OLC A1229 -20.945 13.223 1.369 0.46 53.73 O HETATM 3617 O23 OLC A1229 -20.889 10.398 0.872 0.46 51.63 O HETATM 3618 O20 OLC A1229 -21.205 9.460 -1.616 0.46 48.91 O HETATM 3619 C1 CIT A1230 -27.039 -20.811 35.111 1.00 92.15 C HETATM 3620 O1 CIT A1230 -25.879 -21.254 34.968 1.00 91.53 O HETATM 3621 O2 CIT A1230 -27.215 -19.897 35.943 1.00 91.88 O HETATM 3622 C2 CIT A1230 -28.174 -21.371 34.279 1.00 93.97 C HETATM 3623 C3 CIT A1230 -29.472 -21.652 35.042 1.00 97.67 C HETATM 3624 O7 CIT A1230 -30.237 -22.577 34.224 1.00 95.25 O HETATM 3625 C4 CIT A1230 -29.225 -22.346 36.374 1.00100.74 C HETATM 3626 C5 CIT A1230 -29.960 -23.668 36.370 1.00101.85 C HETATM 3627 O3 CIT A1230 -29.463 -24.684 35.834 1.00102.11 O HETATM 3628 O4 CIT A1230 -31.083 -23.752 36.912 1.00102.08 O HETATM 3629 C6 CIT A1230 -30.308 -20.385 35.274 1.00101.21 C HETATM 3630 O5 CIT A1230 -31.541 -20.390 35.038 1.00103.20 O HETATM 3631 O6 CIT A1230 -29.810 -19.314 35.692 1.00100.95 O HETATM 3632 NA NA A1231 -23.463 -8.712 16.369 1.00 40.50 NA HETATM 3633 O HOH A1301 -17.935 -17.348 16.900 1.00 60.45 O HETATM 3634 O HOH A1302 3.742 -73.026 23.944 1.00 50.47 O HETATM 3635 O HOH A1303 1.698 -46.568 20.889 1.00 53.70 O HETATM 3636 O HOH A1304 -19.260 -35.619 26.597 1.00 48.73 O HETATM 3637 O HOH A1305 6.402 13.757 5.373 1.00 67.80 O HETATM 3638 O HOH A1306 -29.032 12.237 8.667 1.00 39.50 O HETATM 3639 O HOH A1307 -4.595 -37.658 20.914 1.00 45.13 O HETATM 3640 O HOH A1308 -16.131 14.942 20.596 1.00 44.11 O HETATM 3641 O HOH A1309 -26.194 18.509 22.140 1.00 26.01 O HETATM 3642 O HOH A1310 -4.340 -63.514 27.060 1.00 46.35 O HETATM 3643 O HOH A1311 -2.878 -64.431 20.210 1.00 42.64 O HETATM 3644 O HOH A1312 -26.125 -11.941 25.579 1.00 29.36 O HETATM 3645 O HOH A1313 -40.127 14.960 23.195 1.00 54.95 O HETATM 3646 O HOH A1314 -20.994 16.348 18.818 1.00 36.49 O HETATM 3647 O HOH A1315 -25.126 -16.065 14.689 1.00 27.59 O HETATM 3648 O HOH A1316 -16.350 -16.987 18.999 1.00 27.98 O HETATM 3649 O HOH A1317 0.458 -67.178 25.227 1.00 41.17 O HETATM 3650 O HOH A1318 -15.004 10.081 17.835 1.00 19.58 O HETATM 3651 O HOH A1319 -26.052 7.608 13.326 1.00 21.01 O HETATM 3652 O HOH A1320 -10.372 9.066 34.344 1.00 48.38 O HETATM 3653 O HOH A1321 -22.720 -28.199 21.395 1.00 47.71 O HETATM 3654 O HOH A1322 -17.230 17.006 16.666 1.00 38.66 O HETATM 3655 O HOH A1323 -0.879 -62.701 19.941 1.00 36.59 O HETATM 3656 O HOH A1324 -27.869 2.828 16.956 1.00 19.79 O HETATM 3657 O HOH A1325 2.867 -68.347 18.710 1.00 44.14 O HETATM 3658 O HOH A1326 -25.452 -13.445 13.499 1.00 26.50 O HETATM 3659 O HOH A1327 -18.108 12.894 23.570 1.00 29.34 O HETATM 3660 O HOH A1328 -23.525 -4.767 13.953 1.00 22.37 O HETATM 3661 O HOH A1329 -18.715 10.263 22.870 1.00 31.80 O HETATM 3662 O HOH A1330 -14.390 -57.651 22.828 1.00 50.73 O HETATM 3663 O HOH A1331 -16.340 0.653 12.645 1.00 22.43 O HETATM 3664 O HOH A1332 -25.407 2.408 15.914 1.00 24.81 O HETATM 3665 O HOH A1333 -18.968 -11.416 12.944 1.00 26.35 O HETATM 3666 O HOH A1334 -13.003 -33.434 21.280 1.00 44.71 O HETATM 3667 O HOH A1335 -19.570 -1.559 21.994 1.00 24.29 O HETATM 3668 O HOH A1336 -25.776 -14.591 24.654 1.00 34.54 O HETATM 3669 O HOH A1337 -23.773 15.111 33.283 1.00 38.78 O HETATM 3670 O HOH A1338 -24.879 16.683 2.327 1.00 41.70 O HETATM 3671 O HOH A1339 9.182 -70.379 20.827 1.00 43.66 O HETATM 3672 O HOH A1340 -25.689 5.255 18.762 1.00 24.80 O HETATM 3673 O HOH A1341 -14.403 -27.000 17.429 1.00 29.37 O HETATM 3674 O HOH A1342 -23.966 -11.200 11.366 1.00 31.41 O HETATM 3675 O HOH A1343 -25.851 -12.207 21.448 1.00 28.41 O HETATM 3676 O HOH A1344 7.256 -60.795 15.366 1.00 45.28 O HETATM 3677 O HOH A1345 -20.916 -2.657 24.197 1.00 24.07 O HETATM 3678 O HOH A1346 -28.834 2.518 19.589 1.00 19.26 O HETATM 3679 O HOH A1347 -28.125 5.373 17.828 1.00 24.17 O HETATM 3680 O HOH A1348 -13.616 13.566 23.854 1.00 33.69 O HETATM 3681 O HOH A1349 -22.113 -6.555 15.325 1.00 28.29 O HETATM 3682 O HOH A1350 -12.542 -36.023 28.221 1.00 49.21 O HETATM 3683 O HOH A1351 15.010 -55.589 18.375 1.00 45.45 O HETATM 3684 O HOH A1352 -11.160 12.157 15.762 1.00 23.79 O HETATM 3685 O HOH A1353 -34.015 13.717 30.245 1.00 43.28 O HETATM 3686 O HOH A1354 -2.207 13.315 22.082 1.00 31.35 O HETATM 3687 O HOH A1355 -16.390 16.792 8.548 1.00 37.66 O HETATM 3688 O HOH A1356 -23.717 4.051 17.063 1.00 28.19 O HETATM 3689 O HOH A1357 -24.833 9.902 14.452 1.00 25.93 O HETATM 3690 O HOH A1358 -29.810 17.907 29.584 1.00 46.06 O HETATM 3691 O HOH A1359 -4.314 -63.853 17.988 1.00 45.53 O HETATM 3692 O HOH A1360 -27.790 20.706 22.522 1.00 27.05 O HETATM 3693 O HOH A1361 -18.215 -2.940 19.922 1.00 25.12 O HETATM 3694 O HOH A1362 -27.491 -11.694 6.379 1.00 38.87 O HETATM 3695 O HOH A1363 -25.884 18.700 24.776 1.00 28.42 O HETATM 3696 O HOH A1364 -3.655 16.198 21.650 1.00 37.80 O HETATM 3697 O HOH A1365 -17.507 13.553 29.695 1.00 39.78 O HETATM 3698 O HOH A1366 -15.289 3.515 21.799 1.00 20.98 O HETATM 3699 O HOH A1367 -21.960 13.786 17.861 1.00 25.59 O HETATM 3700 O HOH A1368 -13.956 -28.167 19.514 1.00 37.51 O HETATM 3701 O HOH A1369 -31.350 21.434 28.131 1.00 48.12 O HETATM 3702 O HOH A1370 -18.098 16.056 19.106 1.00 37.97 O HETATM 3703 O HOH A1371 -25.447 11.781 16.499 1.00 24.02 O HETATM 3704 O HOH A1372 -25.717 16.859 26.746 1.00 39.62 O HETATM 3705 O HOH A1373 -24.519 6.418 15.725 1.00 32.82 O HETATM 3706 O HOH A1374 -20.770 -11.184 15.211 1.00 38.73 O HETATM 3707 O HOH A1375 -25.150 -6.701 17.666 1.00 42.41 O HETATM 3708 O HOH A1376 -17.479 15.131 6.052 1.00 33.12 O HETATM 3709 O HOH A1377 -4.987 17.845 12.908 1.00 49.35 O HETATM 3710 O HOH A1378 -5.211 -31.218 24.568 1.00 55.05 O HETATM 3711 O HOH A1379 -17.413 13.474 26.193 1.00 30.40 O HETATM 3712 O HOH A1380 -5.747 -61.359 28.389 1.00 45.45 O HETATM 3713 O HOH A1381 -11.774 19.600 14.406 1.00 38.41 O HETATM 3714 O HOH A1382 -11.410 10.674 32.218 1.00 32.87 O HETATM 3715 O HOH A1383 -9.046 13.649 16.900 1.00 31.43 O HETATM 3716 O HOH A1384 8.269 -75.121 27.518 1.00 43.49 O HETATM 3717 O HOH A1385 -31.395 16.322 31.422 1.00 56.38 O HETATM 3718 O HOH A1386 4.121 -75.648 22.668 1.00 38.55 O HETATM 3719 O HOH A1387 8.660 -62.140 13.473 1.00 47.25 O HETATM 3720 O HOH A1388 15.398 -53.415 17.091 1.00 52.09 O CONECT 429 3632 CONECT 565 1234 CONECT 581 1143 CONECT 601 1278 CONECT 719 3632 CONECT 1143 581 CONECT 1234 565 CONECT 1278 601 CONECT 2683 2704 CONECT 2704 2683 CONECT 3099 3100 3105 CONECT 3100 3099 3101 CONECT 3101 3100 3102 3103 CONECT 3102 3101 CONECT 3103 3101 3104 CONECT 3104 3103 3105 CONECT 3105 3099 3104 3106 CONECT 3106 3105 3107 CONECT 3107 3106 3108 CONECT 3108 3107 3109 CONECT 3109 3108 3110 3111 CONECT 3110 3109 3116 CONECT 3111 3109 3112 CONECT 3112 3111 3113 3114 CONECT 3113 3112 CONECT 3114 3112 3115 3116 CONECT 3115 3114 3118 CONECT 3116 3110 3114 3117 CONECT 3117 3116 3118 CONECT 3118 3115 3117 3119 CONECT 3119 3118 3120 3123 CONECT 3120 3119 3121 CONECT 3121 3120 3122 CONECT 3122 3121 3123 CONECT 3123 3119 3122 CONECT 3124 3125 3133 CONECT 3125 3124 3126 CONECT 3126 3125 3127 3151 CONECT 3127 3126 3128 CONECT 3128 3127 3129 3133 CONECT 3129 3128 3130 CONECT 3130 3129 3131 CONECT 3131 3130 3132 3137 CONECT 3132 3131 3133 3134 CONECT 3133 3124 3128 3132 3142 CONECT 3134 3132 3135 CONECT 3135 3134 3136 CONECT 3136 3135 3137 3140 3141 CONECT 3137 3131 3136 3138 CONECT 3138 3137 3139 CONECT 3139 3138 3140 CONECT 3140 3136 3139 3143 CONECT 3141 3136 CONECT 3142 3133 CONECT 3143 3140 3144 3145 CONECT 3144 3143 CONECT 3145 3143 3146 CONECT 3146 3145 3147 CONECT 3147 3146 3148 CONECT 3148 3147 3149 3150 CONECT 3149 3148 CONECT 3150 3148 CONECT 3151 3126 CONECT 3152 3153 3161 CONECT 3153 3152 3154 CONECT 3154 3153 3155 3179 CONECT 3155 3154 3156 CONECT 3156 3155 3157 3161 CONECT 3157 3156 3158 CONECT 3158 3157 3159 CONECT 3159 3158 3160 3165 CONECT 3160 3159 3161 3162 CONECT 3161 3152 3156 3160 3170 CONECT 3162 3160 3163 CONECT 3163 3162 3164 CONECT 3164 3163 3165 3168 3169 CONECT 3165 3159 3164 3166 CONECT 3166 3165 3167 CONECT 3167 3166 3168 CONECT 3168 3164 3167 3171 CONECT 3169 3164 CONECT 3170 3161 CONECT 3171 3168 3172 3173 CONECT 3172 3171 CONECT 3173 3171 3174 CONECT 3174 3173 3175 CONECT 3175 3174 3176 CONECT 3176 3175 3177 3178 CONECT 3177 3176 CONECT 3178 3176 CONECT 3179 3154 CONECT 3180 3181 3189 CONECT 3181 3180 3182 CONECT 3182 3181 3183 3207 CONECT 3183 3182 3184 CONECT 3184 3183 3185 3189 CONECT 3185 3184 3186 CONECT 3186 3185 3187 CONECT 3187 3186 3188 3193 CONECT 3188 3187 3189 3190 CONECT 3189 3180 3184 3188 3198 CONECT 3190 3188 3191 CONECT 3191 3190 3192 CONECT 3192 3191 3193 3196 3197 CONECT 3193 3187 3192 3194 CONECT 3194 3193 3195 CONECT 3195 3194 3196 CONECT 3196 3192 3195 3199 CONECT 3197 3192 CONECT 3198 3189 CONECT 3199 3196 3200 3201 CONECT 3200 3199 CONECT 3201 3199 3202 CONECT 3202 3201 3203 CONECT 3203 3202 3204 CONECT 3204 3203 3205 3206 CONECT 3205 3204 CONECT 3206 3204 CONECT 3207 3182 CONECT 3208 3209 3217 CONECT 3209 3208 3210 CONECT 3210 3209 3211 3235 CONECT 3211 3210 3212 CONECT 3212 3211 3213 3217 CONECT 3213 3212 3214 CONECT 3214 3213 3215 CONECT 3215 3214 3216 3221 CONECT 3216 3215 3217 3218 CONECT 3217 3208 3212 3216 3226 CONECT 3218 3216 3219 CONECT 3219 3218 3220 CONECT 3220 3219 3221 3224 3225 CONECT 3221 3215 3220 3222 CONECT 3222 3221 3223 CONECT 3223 3222 3224 CONECT 3224 3220 3223 3227 CONECT 3225 3220 CONECT 3226 3217 CONECT 3227 3224 3228 3229 CONECT 3228 3227 CONECT 3229 3227 3230 CONECT 3230 3229 3231 CONECT 3231 3230 3232 CONECT 3232 3231 3233 3234 CONECT 3233 3232 CONECT 3234 3232 CONECT 3235 3210 CONECT 3236 3237 3238 3239 CONECT 3237 3236 CONECT 3238 3236 CONECT 3239 3236 3240 CONECT 3240 3239 3241 CONECT 3241 3240 3242 CONECT 3242 3241 3243 CONECT 3243 3242 3244 CONECT 3244 3243 3245 CONECT 3245 3244 3246 CONECT 3246 3245 3247 CONECT 3247 3246 3248 CONECT 3248 3247 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 CONECT 3256 3257 3258 3259 CONECT 3257 3256 CONECT 3258 3256 CONECT 3259 3256 3260 CONECT 3260 3259 3261 CONECT 3261 3260 3262 CONECT 3262 3261 3263 CONECT 3263 3262 3264 CONECT 3264 3263 3265 CONECT 3265 3264 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 3274 CONECT 3274 3273 3275 CONECT 3275 3274 CONECT 3276 3277 3278 3279 CONECT 3277 3276 CONECT 3278 3276 CONECT 3279 3276 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 3293 CONECT 3293 3292 3294 CONECT 3294 3293 3295 CONECT 3295 3294 CONECT 3296 3297 3298 3299 CONECT 3297 3296 CONECT 3298 3296 CONECT 3299 3296 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 3307 CONECT 3307 3306 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 CONECT 3316 3317 3318 3319 CONECT 3317 3316 CONECT 3318 3316 CONECT 3319 3316 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 3330 CONECT 3330 3329 3331 CONECT 3331 3330 3332 CONECT 3332 3331 3333 CONECT 3333 3332 3334 CONECT 3334 3333 3335 CONECT 3335 3334 CONECT 3336 3337 3338 3339 CONECT 3337 3336 CONECT 3338 3336 CONECT 3339 3336 3340 CONECT 3340 3339 3341 CONECT 3341 3340 3342 CONECT 3342 3341 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 3355 CONECT 3355 3354 CONECT 3356 3357 3358 3359 CONECT 3357 3356 CONECT 3358 3356 CONECT 3359 3356 3360 CONECT 3360 3359 3361 CONECT 3361 3360 3362 CONECT 3362 3361 3363 CONECT 3363 3362 3364 CONECT 3364 3363 3365 CONECT 3365 3364 3366 CONECT 3366 3365 3367 CONECT 3367 3366 3368 CONECT 3368 3367 3369 CONECT 3369 3368 3370 CONECT 3370 3369 3371 CONECT 3371 3370 3372 CONECT 3372 3371 3373 CONECT 3373 3372 3374 CONECT 3374 3373 3375 CONECT 3375 3374 CONECT 3376 3377 3378 3379 CONECT 3377 3376 CONECT 3378 3376 CONECT 3379 3376 3380 CONECT 3380 3379 3381 CONECT 3381 3380 3382 CONECT 3382 3381 3383 CONECT 3383 3382 3384 CONECT 3384 3383 3385 CONECT 3385 3384 3386 CONECT 3386 3385 3387 CONECT 3387 3386 3388 CONECT 3388 3387 3389 CONECT 3389 3388 3390 CONECT 3390 3389 3391 CONECT 3391 3390 3392 CONECT 3392 3391 3393 CONECT 3393 3392 3394 CONECT 3394 3393 3395 CONECT 3395 3394 CONECT 3396 3397 3398 3399 CONECT 3397 3396 CONECT 3398 3396 CONECT 3399 3396 3400 CONECT 3400 3399 3401 CONECT 3401 3400 3402 CONECT 3402 3401 3403 CONECT 3403 3402 3404 CONECT 3404 3403 3405 CONECT 3405 3404 3406 CONECT 3406 3405 CONECT 3407 3408 3409 3410 CONECT 3408 3407 CONECT 3409 3407 CONECT 3410 3407 3411 CONECT 3411 3410 3412 CONECT 3412 3411 3413 CONECT 3413 3412 3414 CONECT 3414 3413 3415 CONECT 3415 3414 3416 CONECT 3416 3415 3417 CONECT 3417 3416 3418 CONECT 3418 3417 3419 CONECT 3419 3418 3420 CONECT 3420 3419 3421 CONECT 3421 3420 3422 CONECT 3422 3421 3423 CONECT 3423 3422 3424 CONECT 3424 3423 3425 CONECT 3425 3424 3426 CONECT 3426 3425 CONECT 3427 3428 3429 3430 CONECT 3428 3427 CONECT 3429 3427 CONECT 3430 3427 3431 CONECT 3431 3430 3432 CONECT 3432 3431 3433 CONECT 3433 3432 3434 CONECT 3434 3433 3435 CONECT 3435 3434 3436 CONECT 3436 3435 3437 CONECT 3437 3436 3438 CONECT 3438 3437 3439 CONECT 3439 3438 3440 CONECT 3440 3439 3441 CONECT 3441 3440 3442 CONECT 3442 3441 3443 CONECT 3443 3442 3444 CONECT 3444 3443 3445 CONECT 3445 3444 3446 CONECT 3446 3445 CONECT 3447 3448 3449 3450 CONECT 3448 3447 CONECT 3449 3447 CONECT 3450 3447 3451 CONECT 3451 3450 3452 CONECT 3452 3451 3453 CONECT 3453 3452 3454 CONECT 3454 3453 3455 CONECT 3455 3454 3456 CONECT 3456 3455 3457 CONECT 3457 3456 3458 CONECT 3458 3457 3459 CONECT 3459 3458 3460 CONECT 3460 3459 3461 CONECT 3461 3460 3462 CONECT 3462 3461 3463 CONECT 3463 3462 3464 CONECT 3464 3463 3465 CONECT 3465 3464 3466 CONECT 3466 3465 CONECT 3467 3468 3469 3470 CONECT 3468 3467 CONECT 3469 3467 CONECT 3470 3467 3471 CONECT 3471 3470 3472 CONECT 3472 3471 3473 CONECT 3473 3472 3474 CONECT 3474 3473 3475 CONECT 3475 3474 3476 CONECT 3476 3475 3477 CONECT 3477 3476 3478 CONECT 3478 3477 3479 CONECT 3479 3478 3480 CONECT 3480 3479 3481 CONECT 3481 3480 CONECT 3482 3483 3484 3485 CONECT 3483 3482 CONECT 3484 3482 CONECT 3485 3482 3486 CONECT 3486 3485 3487 CONECT 3487 3486 3488 CONECT 3488 3487 3489 CONECT 3489 3488 3490 CONECT 3490 3489 3491 CONECT 3491 3490 3492 CONECT 3492 3491 3493 CONECT 3493 3492 3494 CONECT 3494 3493 3495 CONECT 3495 3494 3496 CONECT 3496 3495 3497 CONECT 3497 3496 3498 CONECT 3498 3497 3499 CONECT 3499 3498 3500 CONECT 3500 3499 3501 CONECT 3501 3500 CONECT 3502 3503 3504 3505 CONECT 3503 3502 CONECT 3504 3502 CONECT 3505 3502 3506 CONECT 3506 3505 3507 CONECT 3507 3506 3508 CONECT 3508 3507 3509 CONECT 3509 3508 3510 CONECT 3510 3509 3511 CONECT 3511 3510 3512 CONECT 3512 3511 3513 CONECT 3513 3512 3514 CONECT 3514 3513 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 CONECT 3522 3523 3524 3525 CONECT 3523 3522 CONECT 3524 3522 CONECT 3525 3522 3526 CONECT 3526 3525 3527 CONECT 3527 3526 3528 CONECT 3528 3527 3529 CONECT 3529 3528 3530 CONECT 3530 3529 3531 CONECT 3531 3530 3532 CONECT 3532 3531 3533 CONECT 3533 3532 3534 CONECT 3534 3533 3535 CONECT 3535 3534 3536 CONECT 3536 3535 3537 CONECT 3537 3536 3538 CONECT 3538 3537 3539 CONECT 3539 3538 3540 CONECT 3540 3539 3541 CONECT 3541 3540 CONECT 3542 3543 3544 3545 CONECT 3543 3542 CONECT 3544 3542 CONECT 3545 3542 3546 CONECT 3546 3545 3547 CONECT 3547 3546 CONECT 3548 3549 CONECT 3549 3548 3550 CONECT 3550 3549 CONECT 3551 3552 CONECT 3552 3551 3553 CONECT 3553 3552 CONECT 3554 3555 CONECT 3555 3554 3556 CONECT 3556 3555 CONECT 3557 3558 CONECT 3558 3557 3559 CONECT 3559 3558 CONECT 3560 3563 CONECT 3561 3562 3564 CONECT 3562 3561 3565 CONECT 3563 3560 3567 CONECT 3564 3561 3568 CONECT 3565 3562 3569 CONECT 3566 3580 3582 CONECT 3567 3563 3570 CONECT 3568 3564 3571 CONECT 3569 3565 3572 CONECT 3570 3567 3573 CONECT 3571 3568 3573 CONECT 3572 3569 3574 CONECT 3573 3570 3571 CONECT 3574 3572 3575 CONECT 3575 3574 3576 CONECT 3576 3575 3577 CONECT 3577 3576 3579 CONECT 3578 3580 3584 CONECT 3579 3577 3581 3584 CONECT 3580 3566 3578 3583 CONECT 3581 3579 CONECT 3582 3566 CONECT 3583 3580 CONECT 3584 3578 3579 CONECT 3585 3589 3591 CONECT 3586 3588 CONECT 3587 3589 3593 CONECT 3588 3586 3590 3593 CONECT 3589 3585 3587 3592 CONECT 3590 3588 CONECT 3591 3585 CONECT 3592 3589 CONECT 3593 3587 3588 CONECT 3594 3597 CONECT 3595 3596 3598 CONECT 3596 3595 3599 CONECT 3597 3594 3601 CONECT 3598 3595 3602 CONECT 3599 3596 3603 CONECT 3600 3614 3616 CONECT 3601 3597 3604 CONECT 3602 3598 3605 CONECT 3603 3599 3606 CONECT 3604 3601 3607 CONECT 3605 3602 3607 CONECT 3606 3603 3608 CONECT 3607 3604 3605 CONECT 3608 3606 3609 CONECT 3609 3608 3610 CONECT 3610 3609 3611 CONECT 3611 3610 3613 CONECT 3612 3614 3618 CONECT 3613 3611 3615 3618 CONECT 3614 3600 3612 3617 CONECT 3615 3613 CONECT 3616 3600 CONECT 3617 3614 CONECT 3618 3612 3613 CONECT 3619 3620 3621 3622 CONECT 3620 3619 CONECT 3621 3619 CONECT 3622 3619 3623 CONECT 3623 3622 3624 3625 3629 CONECT 3624 3623 CONECT 3625 3623 3626 CONECT 3626 3625 3627 3628 CONECT 3627 3626 CONECT 3628 3626 CONECT 3629 3623 3630 3631 CONECT 3630 3629 CONECT 3631 3629 CONECT 3632 429 719 3681 3707 CONECT 3681 3632 CONECT 3707 3632 MASTER 485 0 31 19 2 0 56 6 3636 1 546 34 END