HEADER SIGNALING PROTEIN 09-FEB-23 8CIC TITLE CRYSTAL STRUCTURE OF STABILIZED A2A ADENOSINE RECEPTOR A2AR-STAR2-BRIL TITLE 2 IN COMPLEX WITH CLINICAL CANDIDATE ETRUMADENANT COMPND MOL_ID: 1; COMPND 2 MOLECULE: ADENOSINE RECEPTOR A2A,SOLUBLE CYTOCHROME B562; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: CYTOCHROME B-562; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: ADORA2A, ADORA2, CYBC; SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111 KEYWDS G-PROTEIN COUPLED RECEPTOR, SIGNALING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR R.K.Y.CHENG,S.MARKOVIC-MUELLER,M.HENNIG REVDAT 2 14-JUN-23 8CIC 1 JRNL REVDAT 1 31-MAY-23 8CIC 0 JRNL AUTH T.CLAFF,J.G.SCHLEGEL,J.H.VOSS,V.J.VAASSEN,R.H.WEISSE, JRNL AUTH 2 R.K.Y.CHENG,S.MARKOVIC-MUELLER,D.BUCHER,N.STRATER,C.E.MULLER JRNL TITL CRYSTAL STRUCTURE OF ADENOSINE A 2A RECEPTOR IN COMPLEX WITH JRNL TITL 2 CLINICAL CANDIDATE ETRUMADENANT REVEALS UNPRECEDENTED JRNL TITL 3 ANTAGONIST INTERACTION. JRNL REF COMMUN CHEM V. 6 106 2023 JRNL REFN ESSN 2399-3669 JRNL PMID 37264098 JRNL DOI 10.1038/S42004-023-00894-6 REMARK 2 REMARK 2 RESOLUTION. 2.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.14 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.77 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.280 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 55857 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.192 REMARK 3 R VALUE (WORKING SET) : 0.190 REMARK 3 FREE R VALUE : 0.214 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080 REMARK 3 FREE R VALUE TEST SET COUNT : 2840 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 44.7730 - 5.7008 1.00 2658 135 0.1883 0.1762 REMARK 3 2 5.7008 - 4.5263 1.00 2666 156 0.1752 0.1679 REMARK 3 3 4.5263 - 3.9546 1.00 2624 145 0.1573 0.1804 REMARK 3 4 3.9546 - 3.5932 1.00 2623 154 0.1598 0.2114 REMARK 3 5 3.5932 - 3.3357 1.00 2698 125 0.1649 0.2017 REMARK 3 6 3.3357 - 3.1391 1.00 2645 173 0.1815 0.1975 REMARK 3 7 3.1391 - 2.9819 1.00 2632 139 0.1913 0.2596 REMARK 3 8 2.9819 - 2.8521 1.00 2670 126 0.1752 0.2051 REMARK 3 9 2.8521 - 2.7424 1.00 2693 128 0.1836 0.1890 REMARK 3 10 2.7424 - 2.6477 1.00 2629 127 0.1947 0.2327 REMARK 3 11 2.6477 - 2.5650 1.00 2699 128 0.1951 0.2164 REMARK 3 12 2.5650 - 2.4916 1.00 2618 152 0.2142 0.2514 REMARK 3 13 2.4916 - 2.4261 1.00 2635 151 0.2340 0.2957 REMARK 3 14 2.4261 - 2.3669 1.00 2662 171 0.2345 0.2573 REMARK 3 15 2.3669 - 2.3131 1.00 2615 138 0.2463 0.2663 REMARK 3 16 2.3131 - 2.2638 1.00 2680 146 0.2523 0.2907 REMARK 3 17 2.2638 - 2.2186 1.00 2642 149 0.2569 0.3213 REMARK 3 18 2.2186 - 2.1767 1.00 2613 136 0.2720 0.3076 REMARK 3 19 2.1767 - 2.1378 1.00 2693 152 0.2971 0.3401 REMARK 3 20 2.1378 - 2.1020 0.99 2622 109 0.3085 0.3766 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.260 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.090 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.003 3631 REMARK 3 ANGLE : 0.549 4860 REMARK 3 CHIRALITY : 0.036 545 REMARK 3 PLANARITY : 0.003 574 REMARK 3 DIHEDRAL : 15.801 1988 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID -1 THROUGH 208 ) REMARK 3 ORIGIN FOR THE GROUP (A): -23.9494 -5.4505 21.0380 REMARK 3 T TENSOR REMARK 3 T11: 0.2008 T22: 0.2541 REMARK 3 T33: 0.1819 T12: -0.0220 REMARK 3 T13: 0.0231 T23: 0.0194 REMARK 3 L TENSOR REMARK 3 L11: 1.2773 L22: 2.3399 REMARK 3 L33: 1.3498 L12: -0.1284 REMARK 3 L13: 0.3202 L23: 0.3987 REMARK 3 S TENSOR REMARK 3 S11: -0.0183 S12: -0.0918 S13: -0.0172 REMARK 3 S21: -0.0221 S22: 0.0114 S23: 0.0105 REMARK 3 S31: 0.1183 S32: -0.1129 S33: 0.0076 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1001 THROUGH 1106 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.0603 -54.7794 20.1953 REMARK 3 T TENSOR REMARK 3 T11: 0.5715 T22: 0.4054 REMARK 3 T33: 1.0174 T12: 0.0987 REMARK 3 T13: 0.0308 T23: -0.0653 REMARK 3 L TENSOR REMARK 3 L11: 0.7354 L22: 4.0666 REMARK 3 L33: 7.3562 L12: -0.1795 REMARK 3 L13: 1.9527 L23: -3.4260 REMARK 3 S TENSOR REMARK 3 S11: 0.1809 S12: -0.2344 S13: 0.8718 REMARK 3 S21: -0.5755 S22: 0.0091 S23: -0.3833 REMARK 3 S31: -0.0005 S32: -0.1308 S33: -0.2327 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 219 THROUGH 305 ) REMARK 3 ORIGIN FOR THE GROUP (A): -17.7070 -10.9516 10.9742 REMARK 3 T TENSOR REMARK 3 T11: 0.2611 T22: 0.2501 REMARK 3 T33: 0.2131 T12: 0.0225 REMARK 3 T13: 0.0286 T23: -0.0024 REMARK 3 L TENSOR REMARK 3 L11: 1.2913 L22: 3.3589 REMARK 3 L33: 1.5005 L12: 0.4328 REMARK 3 L13: 0.2772 L23: -0.2003 REMARK 3 S TENSOR REMARK 3 S11: -0.0293 S12: 0.1058 S13: -0.1956 REMARK 3 S21: -0.4410 S22: 0.0596 S23: -0.0404 REMARK 3 S31: 0.2998 S32: 0.0215 S33: -0.0220 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 8CIC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-FEB-23. REMARK 100 THE DEPOSITION ID IS D_1292128566. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 29-NOV-18 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X10SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.99997 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS BUILT 20161205 REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.3 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55857 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100 REMARK 200 RESOLUTION RANGE LOW (A) : 46.860 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 13.20 REMARK 200 R MERGE (I) : 0.17200 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : 13.40 REMARK 200 R MERGE FOR SHELL (I) : 2.17700 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> 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 2.8.2 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.32 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE PH 5.0, 50 MM REMARK 280 SODIUM THIOCYANATE, 3 % (V/V) 2-METHYL-2,4-PENTANEDIOL (MPD), 21- REMARK 280 32 % (W/V) PEG400, AND 2 MM THEOPHYLLINE, LIPIDIC CUBIC PHASE, REMARK 280 TEMPERATURE 294K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.28650 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.28650 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 19.68000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 89.54550 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 19.68000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 89.54550 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 70.28650 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 19.68000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 89.54550 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 70.28650 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 19.68000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 89.54550 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: 9040 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20930 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 21.0 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 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 PRO A 1056 REMARK 465 GLU A 1057 REMARK 465 MET A 1058 REMARK 465 LYS A 1059 REMARK 465 HIS A 306 REMARK 465 VAL A 307 REMARK 465 LEU A 308 REMARK 465 ARG A 309 REMARK 465 GLN A 310 REMARK 465 GLN A 311 REMARK 465 GLU A 312 REMARK 465 PRO A 313 REMARK 465 PHE A 314 REMARK 465 LYS A 315 REMARK 465 ALA A 316 REMARK 465 ALA A 317 REMARK 465 ALA A 318 REMARK 465 HIS A 319 REMARK 465 HIS A 320 REMARK 465 HIS A 321 REMARK 465 HIS A 322 REMARK 465 HIS A 323 REMARK 465 HIS A 324 REMARK 465 HIS A 325 REMARK 465 HIS A 326 REMARK 465 HIS A 327 REMARK 465 HIS A 328 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LEU A 58 -50.25 -120.86 REMARK 500 VAL A 186 -55.16 -120.31 REMARK 500 TYR A1101 -61.52 -124.76 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 1208 REMARK 610 OLA A 1209 REMARK 610 OLA A 1210 REMARK 610 OLA A 1211 REMARK 610 OLA A 1212 REMARK 610 OLA A 1213 REMARK 610 OLA A 1214 REMARK 610 OLA A 1215 REMARK 610 OLA A 1216 REMARK 610 OLA A 1217 REMARK 610 OLA A 1218 REMARK 610 OLA A 1219 REMARK 610 OLA A 1221 REMARK 610 OLB A 1222 REMARK 610 OLB A 1223 REMARK 610 OLB A 1224 REMARK 610 OLC A 1226 REMARK 610 OLC A 1227 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 A1201 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 52 OD1 REMARK 620 2 SER A 91 OG 129.6 REMARK 620 3 HOH A1332 O 86.2 115.0 REMARK 620 4 HOH A1334 O 99.6 125.1 87.4 REMARK 620 5 HOH A1365 O 94.9 71.0 171.0 83.6 REMARK 620 N 1 2 3 4 DBREF 8CIC A 2 208 UNP P29274 AA2AR_HUMAN 2 208 DBREF 8CIC A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128 DBREF 8CIC A 219 317 UNP P29274 AA2AR_HUMAN 219 317 SEQADV 8CIC ASP A -8 UNP P29274 EXPRESSION TAG SEQADV 8CIC TYR A -7 UNP P29274 EXPRESSION TAG SEQADV 8CIC LYS A -6 UNP P29274 EXPRESSION TAG SEQADV 8CIC ASP A -5 UNP P29274 EXPRESSION TAG SEQADV 8CIC ASP A -4 UNP P29274 EXPRESSION TAG SEQADV 8CIC ASP A -3 UNP P29274 EXPRESSION TAG SEQADV 8CIC ASP A -2 UNP P29274 EXPRESSION TAG SEQADV 8CIC GLY A -1 UNP P29274 EXPRESSION TAG SEQADV 8CIC ALA A 0 UNP P29274 EXPRESSION TAG SEQADV 8CIC PRO A 1 UNP P29274 EXPRESSION TAG SEQADV 8CIC LEU A 54 UNP P29274 ALA 54 ENGINEERED MUTATION SEQADV 8CIC ALA A 88 UNP P29274 THR 88 ENGINEERED MUTATION SEQADV 8CIC ALA A 107 UNP P29274 ARG 107 ENGINEERED MUTATION SEQADV 8CIC ALA A 122 UNP P29274 LYS 122 ENGINEERED MUTATION SEQADV 8CIC ALA A 154 UNP P29274 ASN 154 ENGINEERED MUTATION SEQADV 8CIC ALA A 202 UNP P29274 LEU 202 ENGINEERED MUTATION SEQADV 8CIC TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 8CIC ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 8CIC LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION SEQADV 8CIC ALA A 235 UNP P29274 LEU 235 ENGINEERED MUTATION SEQADV 8CIC ALA A 239 UNP P29274 VAL 239 ENGINEERED MUTATION SEQADV 8CIC ALA A 318 UNP P29274 EXPRESSION TAG SEQADV 8CIC HIS A 319 UNP P29274 EXPRESSION TAG SEQADV 8CIC HIS A 320 UNP P29274 EXPRESSION TAG SEQADV 8CIC HIS A 321 UNP P29274 EXPRESSION TAG SEQADV 8CIC HIS A 322 UNP P29274 EXPRESSION TAG SEQADV 8CIC HIS A 323 UNP P29274 EXPRESSION TAG SEQADV 8CIC HIS A 324 UNP P29274 EXPRESSION TAG SEQADV 8CIC HIS A 325 UNP P29274 EXPRESSION TAG SEQADV 8CIC HIS A 326 UNP P29274 EXPRESSION TAG SEQADV 8CIC HIS A 327 UNP P29274 EXPRESSION TAG SEQADV 8CIC HIS A 328 UNP P29274 EXPRESSION TAG SEQRES 1 A 433 ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO PRO ILE MET SEQRES 2 A 433 GLY SER SER VAL TYR ILE THR VAL GLU LEU ALA ILE ALA SEQRES 3 A 433 VAL LEU ALA ILE LEU GLY ASN VAL LEU VAL CYS TRP ALA SEQRES 4 A 433 VAL TRP LEU ASN SER ASN LEU GLN ASN VAL THR ASN TYR SEQRES 5 A 433 PHE VAL VAL SER LEU ALA ALA ALA ASP ILE LEU VAL GLY SEQRES 6 A 433 VAL LEU ALA ILE PRO PHE ALA ILE THR ILE SER THR GLY SEQRES 7 A 433 PHE CYS ALA ALA CYS HIS GLY CYS LEU PHE ILE ALA CYS SEQRES 8 A 433 PHE VAL LEU VAL LEU ALA GLN SER SER ILE PHE SER LEU SEQRES 9 A 433 LEU ALA ILE ALA ILE ASP ARG TYR ILE ALA ILE ALA ILE SEQRES 10 A 433 PRO LEU ARG TYR ASN GLY LEU VAL THR GLY THR ARG ALA SEQRES 11 A 433 ALA GLY ILE ILE ALA ILE CYS TRP VAL LEU SER PHE ALA SEQRES 12 A 433 ILE GLY LEU THR PRO MET LEU GLY TRP ASN ASN CYS GLY SEQRES 13 A 433 GLN PRO LYS GLU GLY LYS ALA HIS SER GLN GLY CYS GLY SEQRES 14 A 433 GLU GLY GLN VAL ALA CYS LEU PHE GLU ASP VAL VAL PRO SEQRES 15 A 433 MET ASN TYR MET VAL TYR PHE ASN PHE PHE ALA CYS VAL SEQRES 16 A 433 LEU VAL PRO LEU LEU LEU MET LEU GLY VAL TYR LEU ARG SEQRES 17 A 433 ILE PHE ALA ALA ALA ARG ARG GLN LEU ALA ASP LEU GLU SEQRES 18 A 433 ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS VAL ILE SEQRES 19 A 433 GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP ALA LEU SEQRES 20 A 433 THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN LYS ALA SEQRES 21 A 433 THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SER PRO SEQRES 22 A 433 GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE LEU VAL SEQRES 23 A 433 GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN GLU GLY SEQRES 24 A 433 LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN LEU LYS SEQRES 25 A 433 THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU GLU ARG SEQRES 26 A 433 ALA ARG SER THR LEU GLN LYS GLU VAL HIS ALA ALA LYS SEQRES 27 A 433 SER ALA ALA ILE ILE ALA GLY LEU PHE ALA LEU CYS TRP SEQRES 28 A 433 LEU PRO LEU HIS ILE ILE ASN CYS PHE THR PHE PHE CYS SEQRES 29 A 433 PRO ASP CYS SER HIS ALA PRO LEU TRP LEU MET TYR LEU SEQRES 30 A 433 ALA ILE VAL LEU SER HIS THR ASN SER VAL VAL ASN PRO SEQRES 31 A 433 PHE ILE TYR ALA TYR ARG ILE ARG GLU PHE ARG GLN THR SEQRES 32 A 433 PHE ARG LYS ILE ILE ARG SER HIS VAL LEU ARG GLN GLN SEQRES 33 A 433 GLU PRO PHE LYS ALA ALA ALA HIS HIS HIS HIS HIS HIS SEQRES 34 A 433 HIS HIS HIS HIS HET NA A1201 1 HET U30 A1202 32 HET CLR A1203 28 HET CLR A1204 28 HET CLR A1205 28 HET CLR A1206 28 HET OLA A1207 20 HET OLA A1208 15 HET OLA A1209 9 HET OLA A1210 19 HET OLA A1211 10 HET OLA A1212 17 HET OLA A1213 8 HET OLA A1214 7 HET OLA A1215 16 HET OLA A1216 11 HET OLA A1217 12 HET OLA A1218 8 HET OLA A1219 12 HET OLA A1220 20 HET OLA A1221 14 HET OLB A1222 22 HET OLB A1223 19 HET OLB A1224 18 HET OLC A1225 25 HET OLC A1226 19 HET OLC A1227 21 HET OLC A1228 17 HET OLC A1229 25 HETNAM NA SODIUM ION HETNAM U30 3-[2-AZANYL-6-[1-[[6-(2-OXIDANYLPROPAN-2-YL)PYRIDIN-2- HETNAM 2 U30 YL]METHYL]-1,2,3-TRIAZOL-4-YL]PYRIMIDIN-4-YL]-2- HETNAM 3 U30 METHYL-BENZENECARBONITRILE HETNAM CLR CHOLESTEROL HETNAM OLA OLEIC ACID HETNAM OLB (2S)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 NA NA 1+ FORMUL 3 U30 C23 H22 N8 O FORMUL 4 CLR 4(C27 H46 O) FORMUL 8 OLA 15(C18 H34 O2) FORMUL 23 OLB 3(C21 H40 O4) FORMUL 26 OLC 5(C21 H40 O4) FORMUL 31 HOH *126(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 LYS A 1042 1 21 HELIX 14 AB5 PHE A 1061 GLU A 1081 1 21 HELIX 15 AB6 LYS A 1083 TYR A 1101 1 19 HELIX 16 AB7 TYR A 1101 CYS A 259 1 47 HELIX 17 AB8 PRO A 266 ILE A 292 1 27 HELIX 18 AB9 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 2.03 SSBOND 2 CYS A 74 CYS A 146 1555 1555 2.03 SSBOND 3 CYS A 77 CYS A 166 1555 1555 2.03 SSBOND 4 CYS A 259 CYS A 262 1555 1555 2.03 LINK OD1 ASP A 52 NA NA A1201 1555 1555 2.44 LINK OG SER A 91 NA NA A1201 1555 1555 2.45 LINK NA NA A1201 O HOH A1332 1555 1555 2.36 LINK NA NA A1201 O HOH A1334 1555 1555 2.61 LINK NA NA A1201 O HOH A1365 1555 1555 2.44 CRYST1 39.360 179.091 140.573 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 0.025407 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005584 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007114 0.00000 ATOM 1 N GLY A -1 -20.264 24.003 1.241 1.00100.21 N ANISOU 1 N GLY A -1 15514 10449 12112 -595 112 1998 N ATOM 2 CA GLY A -1 -21.113 23.266 2.158 1.00 97.82 C ANISOU 2 CA GLY A -1 15096 10227 11845 -483 -32 1875 C ATOM 3 C GLY A -1 -22.382 22.747 1.514 1.00 97.81 C ANISOU 3 C GLY A -1 15200 10290 11673 -340 -212 1876 C ATOM 4 O GLY A -1 -23.431 23.384 1.598 1.00 97.35 O ANISOU 4 O GLY A -1 15187 10150 11651 -214 -431 1868 O ATOM 5 N ALA A 0 -22.283 21.581 0.877 1.00 95.96 N ANISOU 5 N ALA A 0 14978 10213 11271 -354 -124 1867 N ATOM 6 CA ALA A 0 -23.420 20.998 0.182 1.00 92.84 C ANISOU 6 CA ALA A 0 14663 9897 10715 -231 -289 1852 C ATOM 7 C ALA A 0 -24.574 20.768 1.157 1.00 84.86 C ANISOU 7 C ALA A 0 13483 8938 9823 -91 -499 1722 C ATOM 8 O ALA A 0 -24.346 20.537 2.350 1.00 83.36 O ANISOU 8 O ALA A 0 13046 8823 9806 -99 -454 1598 O ATOM 9 CB ALA A 0 -23.024 19.681 -0.482 1.00 93.20 C ANISOU 9 CB ALA A 0 14711 10110 10590 -278 -147 1831 C ATOM 10 N PRO A 1 -25.817 20.861 0.685 1.00 81.24 N ANISOU 10 N PRO A 1 13121 8456 9290 42 -727 1729 N ATOM 11 CA PRO A 1 -26.974 20.669 1.572 1.00 76.68 C ANISOU 11 CA PRO A 1 12337 7949 8848 180 -914 1587 C ATOM 12 C PRO A 1 -26.857 19.372 2.350 1.00 73.92 C ANISOU 12 C PRO A 1 11738 7805 8543 159 -819 1445 C ATOM 13 O PRO A 1 -26.598 18.308 1.768 1.00 69.45 O ANISOU 13 O PRO A 1 11205 7351 7833 113 -732 1449 O ATOM 14 CB PRO A 1 -28.159 20.627 0.597 1.00 75.43 C ANISOU 14 CB PRO A 1 12344 7767 8550 300 -1140 1630 C ATOM 15 CG PRO A 1 -27.709 21.436 -0.569 1.00 74.67 C ANISOU 15 CG PRO A 1 12468 7567 8337 244 -1086 1760 C ATOM 16 CD PRO A 1 -26.222 21.223 -0.686 1.00 77.32 C ANISOU 16 CD PRO A 1 12831 7919 8628 74 -801 1819 C ATOM 17 N PRO A 2 -27.024 19.426 3.674 1.00 72.19 N ANISOU 17 N PRO A 2 11278 7633 8517 193 -831 1319 N ATOM 18 CA PRO A 2 -26.793 18.222 4.490 1.00 65.02 C ANISOU 18 CA PRO A 2 10144 6907 7651 161 -726 1198 C ATOM 19 C PRO A 2 -27.701 17.059 4.135 1.00 57.22 C ANISOU 19 C PRO A 2 9118 6057 6568 223 -814 1142 C ATOM 20 O PRO A 2 -27.303 15.902 4.320 1.00 53.40 O ANISOU 20 O PRO A 2 8535 5706 6047 169 -699 1088 O ATOM 21 CB PRO A 2 -27.039 18.715 5.925 1.00 65.35 C ANISOU 21 CB PRO A 2 9978 6950 7902 211 -766 1082 C ATOM 22 CG PRO A 2 -27.013 20.218 5.847 1.00 68.20 C ANISOU 22 CG PRO A 2 10460 7113 8339 234 -840 1150 C ATOM 23 CD PRO A 2 -27.491 20.565 4.480 1.00 69.85 C ANISOU 23 CD PRO A 2 10916 7224 8398 271 -950 1278 C ATOM 24 N ILE A 3 -28.909 17.327 3.631 1.00 57.96 N ANISOU 24 N ILE A 3 9281 6113 6630 337 -1025 1149 N ATOM 25 CA ILE A 3 -29.844 16.251 3.324 1.00 61.96 C ANISOU 25 CA ILE A 3 9733 6742 7068 395 -1129 1086 C ATOM 26 C ILE A 3 -29.333 15.349 2.207 1.00 59.45 C ANISOU 26 C ILE A 3 9576 6473 6540 321 -1044 1148 C ATOM 27 O ILE A 3 -29.814 14.221 2.057 1.00 57.18 O ANISOU 27 O ILE A 3 9223 6304 6198 335 -1079 1081 O ATOM 28 CB ILE A 3 -31.226 16.837 2.971 1.00 62.73 C ANISOU 28 CB ILE A 3 9870 6775 7191 537 -1390 1081 C ATOM 29 CG1 ILE A 3 -32.311 15.760 3.058 1.00 61.90 C ANISOU 29 CG1 ILE A 3 9614 6808 7095 599 -1505 974 C ATOM 30 CG2 ILE A 3 -31.197 17.451 1.590 1.00 68.99 C ANISOU 30 CG2 ILE A 3 10966 7434 7813 548 -1478 1226 C ATOM 31 CD1 ILE A 3 -33.632 16.166 2.440 1.00 64.54 C ANISOU 31 CD1 ILE A 3 10004 7088 7429 732 -1773 975 C ATOM 32 N MET A 4 -28.352 15.808 1.426 1.00 56.80 N ANISOU 32 N MET A 4 9449 6048 6086 240 -923 1272 N ATOM 33 CA MET A 4 -27.864 15.001 0.312 1.00 55.26 C ANISOU 33 CA MET A 4 9424 5896 5674 177 -831 1328 C ATOM 34 C MET A 4 -26.968 13.877 0.819 1.00 54.11 C ANISOU 34 C MET A 4 9127 5883 5549 87 -621 1255 C ATOM 35 O MET A 4 -27.223 12.697 0.555 1.00 55.08 O ANISOU 35 O MET A 4 9221 6116 5590 91 -626 1193 O ATOM 36 CB MET A 4 -27.130 15.880 -0.703 1.00 53.92 C ANISOU 36 CB MET A 4 9534 5587 5365 118 -753 1488 C ATOM 37 CG MET A 4 -28.030 16.897 -1.386 1.00 51.69 C ANISOU 37 CG MET A 4 9432 5172 5034 213 -974 1568 C ATOM 38 SD MET A 4 -27.183 17.858 -2.653 1.00 61.67 S ANISOU 38 SD MET A 4 10923 6333 6175 128 -838 1703 S ATOM 39 CE MET A 4 -26.807 16.580 -3.851 1.00 62.05 C ANISOU 39 CE MET A 4 11071 6518 5988 74 -716 1688 C ATOM 40 N GLY A 5 -25.904 14.230 1.545 1.00 51.80 N ANISOU 40 N GLY A 5 8739 5572 5372 5 -446 1257 N ATOM 41 CA GLY A 5 -25.082 13.210 2.170 1.00 45.44 C ANISOU 41 CA GLY A 5 7765 4886 4616 -65 -271 1179 C ATOM 42 C GLY A 5 -25.854 12.402 3.194 1.00 46.21 C ANISOU 42 C GLY A 5 7631 5100 4827 -5 -358 1045 C ATOM 43 O GLY A 5 -25.553 11.226 3.424 1.00 41.52 O ANISOU 43 O GLY A 5 6939 4617 4220 -37 -272 978 O ATOM 44 N ASER A 6 -26.858 13.021 3.822 1.00 45.31 N ANISOU 44 N ASER A 6 7430 4957 4828 82 -524 1004 N ATOM 45 CA ASER A 6 -27.721 12.301 4.752 1.00 45.71 C ANISOU 45 CA ASER A 6 7269 5118 4981 139 -606 882 C ATOM 46 C ASER A 6 -28.559 11.255 4.028 1.00 41.64 C ANISOU 46 C ASER A 6 6790 4678 4353 174 -706 853 C ATOM 47 O ASER A 6 -28.769 10.154 4.548 1.00 44.36 O ANISOU 47 O ASER A 6 6990 5135 4731 164 -682 767 O ATOM 48 CB ASER A 6 -28.619 13.291 5.496 1.00 50.52 C ANISOU 48 CB ASER A 6 7786 5673 5736 231 -751 844 C ATOM 49 OG ASER A 6 -29.545 12.624 6.331 1.00 60.30 O ANISOU 49 OG ASER A 6 8826 7020 7067 286 -822 730 O ATOM 50 N SER A 7 -29.046 11.585 2.827 1.00 40.47 N ANISOU 50 N SER A 7 6845 4463 4071 213 -826 925 N ATOM 51 CA SER A 7 -29.817 10.629 2.036 1.00 43.55 C ANISOU 51 CA SER A 7 7291 4913 4343 244 -940 895 C ATOM 52 C SER A 7 -29.003 9.380 1.727 1.00 38.52 C ANISOU 52 C SER A 7 6676 4360 3601 161 -779 874 C ATOM 53 O SER A 7 -29.520 8.259 1.805 1.00 39.93 O ANISOU 53 O SER A 7 6767 4628 3776 167 -823 793 O ATOM 54 CB SER A 7 -30.309 11.285 0.748 1.00 48.18 C ANISOU 54 CB SER A 7 8128 5400 4780 298 -1094 988 C ATOM 55 OG SER A 7 -31.194 12.353 1.036 1.00 57.39 O ANISOU 55 OG SER A 7 9260 6487 6058 393 -1272 994 O ATOM 56 N VAL A 8 -27.728 9.553 1.373 1.00 35.93 N ANISOU 56 N VAL A 8 6459 3997 3196 83 -589 944 N ATOM 57 CA VAL A 8 -26.867 8.408 1.086 1.00 35.63 C ANISOU 57 CA VAL A 8 6435 4032 3069 12 -422 918 C ATOM 58 C VAL A 8 -26.684 7.569 2.344 1.00 35.15 C ANISOU 58 C VAL A 8 6122 4068 3164 -9 -349 815 C ATOM 59 O VAL A 8 -26.818 6.340 2.317 1.00 37.28 O ANISOU 59 O VAL A 8 6343 4417 3403 -18 -340 746 O ATOM 60 CB VAL A 8 -25.519 8.877 0.510 1.00 38.72 C ANISOU 60 CB VAL A 8 6973 4367 3373 -67 -218 1011 C ATOM 61 CG1 VAL A 8 -24.541 7.717 0.429 1.00 41.44 C ANISOU 61 CG1 VAL A 8 7281 4792 3671 -131 -27 965 C ATOM 62 CG2 VAL A 8 -25.723 9.485 -0.861 1.00 40.49 C ANISOU 62 CG2 VAL A 8 7483 4504 3398 -51 -281 1118 C ATOM 63 N TYR A 9 -26.352 8.223 3.460 1.00 36.31 N ANISOU 63 N TYR A 9 6120 4201 3474 -18 -301 804 N ATOM 64 CA TYR A 9 -26.179 7.515 4.725 1.00 30.46 C ANISOU 64 CA TYR A 9 5156 3546 2872 -34 -241 714 C ATOM 65 C TYR A 9 -27.431 6.733 5.098 1.00 29.34 C ANISOU 65 C TYR A 9 4902 3478 2770 17 -382 632 C ATOM 66 O TYR A 9 -27.355 5.554 5.464 1.00 30.42 O ANISOU 66 O TYR A 9 4947 3693 2920 -8 -334 569 O ATOM 67 CB TYR A 9 -25.847 8.512 5.831 1.00 37.14 C ANISOU 67 CB TYR A 9 5883 4354 3874 -35 -211 711 C ATOM 68 CG TYR A 9 -25.968 7.925 7.218 1.00 33.46 C ANISOU 68 CG TYR A 9 5200 3974 3541 -30 -195 617 C ATOM 69 CD1 TYR A 9 -25.153 6.882 7.633 1.00 31.91 C ANISOU 69 CD1 TYR A 9 4925 3846 3354 -82 -70 578 C ATOM 70 CD2 TYR A 9 -26.938 8.390 8.096 1.00 32.43 C ANISOU 70 CD2 TYR A 9 4950 3853 3520 32 -308 566 C ATOM 71 CE1 TYR A 9 -25.279 6.342 8.899 1.00 31.35 C ANISOU 71 CE1 TYR A 9 4677 3845 3387 -76 -62 503 C ATOM 72 CE2 TYR A 9 -27.077 7.853 9.358 1.00 33.06 C ANISOU 72 CE2 TYR A 9 4850 4012 3700 34 -284 486 C ATOM 73 CZ TYR A 9 -26.249 6.828 9.754 1.00 34.20 C ANISOU 73 CZ TYR A 9 4936 4220 3840 -22 -165 460 C ATOM 74 OH TYR A 9 -26.384 6.301 11.018 1.00 35.28 O ANISOU 74 OH TYR A 9 4915 4428 4060 -19 -146 391 O ATOM 75 N ILE A 10 -28.596 7.378 5.015 1.00 31.63 N ANISOU 75 N ILE A 10 5191 3736 3090 89 -556 630 N ATOM 76 CA ILE A 10 -29.836 6.728 5.421 1.00 36.08 C ANISOU 76 CA ILE A 10 5620 4368 3720 134 -687 549 C ATOM 77 C ILE A 10 -30.159 5.562 4.497 1.00 36.70 C ANISOU 77 C ILE A 10 5780 4486 3677 119 -734 528 C ATOM 78 O ILE A 10 -30.573 4.489 4.953 1.00 35.09 O ANISOU 78 O ILE A 10 5453 4358 3522 101 -741 455 O ATOM 79 CB ILE A 10 -30.983 7.755 5.471 1.00 38.20 C ANISOU 79 CB ILE A 10 5863 4588 4061 224 -866 548 C ATOM 80 CG1 ILE A 10 -30.748 8.756 6.604 1.00 39.43 C ANISOU 80 CG1 ILE A 10 5907 4716 4359 243 -818 537 C ATOM 81 CG2 ILE A 10 -32.325 7.057 5.633 1.00 33.42 C ANISOU 81 CG2 ILE A 10 5129 4052 3517 266 -1009 466 C ATOM 82 CD1 ILE A 10 -31.758 9.878 6.647 1.00 39.07 C ANISOU 82 CD1 ILE A 10 5845 4605 4392 341 -983 535 C ATOM 83 N THR A 11 -29.971 5.747 3.189 1.00 39.78 N ANISOU 83 N THR A 11 6391 4820 3903 121 -767 592 N ATOM 84 CA THR A 11 -30.259 4.671 2.247 1.00 35.65 C ANISOU 84 CA THR A 11 5970 4328 3249 111 -821 563 C ATOM 85 C THR A 11 -29.360 3.465 2.495 1.00 32.86 C ANISOU 85 C THR A 11 5575 4034 2878 41 -650 521 C ATOM 86 O THR A 11 -29.823 2.319 2.463 1.00 33.45 O ANISOU 86 O THR A 11 5600 4160 2951 30 -696 451 O ATOM 87 CB THR A 11 -30.093 5.175 0.813 1.00 34.48 C ANISOU 87 CB THR A 11 6094 4105 2902 128 -868 646 C ATOM 88 OG1 THR A 11 -30.941 6.311 0.604 1.00 36.23 O ANISOU 88 OG1 THR A 11 6360 4259 3147 202 -1045 689 O ATOM 89 CG2 THR A 11 -30.467 4.089 -0.180 1.00 34.55 C ANISOU 89 CG2 THR A 11 6222 4143 2764 126 -946 604 C ATOM 90 N VAL A 12 -28.069 3.704 2.742 1.00 33.41 N ANISOU 90 N VAL A 12 5657 4090 2945 -5 -458 561 N ATOM 91 CA VAL A 12 -27.149 2.607 3.035 1.00 29.43 C ANISOU 91 CA VAL A 12 5101 3637 2445 -59 -299 518 C ATOM 92 C VAL A 12 -27.549 1.900 4.325 1.00 33.27 C ANISOU 92 C VAL A 12 5364 4188 3089 -65 -312 442 C ATOM 93 O VAL A 12 -27.542 0.665 4.402 1.00 31.68 O ANISOU 93 O VAL A 12 5125 4030 2884 -88 -290 384 O ATOM 94 CB VAL A 12 -25.700 3.129 3.090 1.00 26.75 C ANISOU 94 CB VAL A 12 4795 3269 2101 -104 -101 573 C ATOM 95 CG1 VAL A 12 -24.782 2.097 3.726 1.00 31.06 C ANISOU 95 CG1 VAL A 12 5227 3868 2707 -145 48 518 C ATOM 96 CG2 VAL A 12 -25.218 3.486 1.692 1.00 29.95 C ANISOU 96 CG2 VAL A 12 5440 3621 2319 -116 -48 644 C ATOM 97 N GLU A 13 -27.901 2.673 5.359 1.00 31.33 N ANISOU 97 N GLU A 13 4978 3945 2979 -43 -344 441 N ATOM 98 CA GLU A 13 -28.310 2.086 6.634 1.00 27.63 C ANISOU 98 CA GLU A 13 4311 3540 2647 -49 -346 376 C ATOM 99 C GLU A 13 -29.535 1.199 6.477 1.00 24.84 C ANISOU 99 C GLU A 13 3911 3225 2302 -40 -477 319 C ATOM 100 O GLU A 13 -29.586 0.093 7.028 1.00 30.39 O ANISOU 100 O GLU A 13 4523 3975 3050 -74 -442 270 O ATOM 101 CB GLU A 13 -28.606 3.188 7.651 1.00 34.89 C ANISOU 101 CB GLU A 13 5113 4453 3691 -17 -371 379 C ATOM 102 CG GLU A 13 -27.393 3.906 8.179 1.00 35.65 C ANISOU 102 CG GLU A 13 5202 4519 3825 -40 -241 413 C ATOM 103 CD GLU A 13 -26.729 3.178 9.330 1.00 39.42 C ANISOU 103 CD GLU A 13 5547 5052 4379 -75 -134 370 C ATOM 104 OE1 GLU A 13 -26.596 3.789 10.410 1.00 39.46 O ANISOU 104 OE1 GLU A 13 5449 5063 4482 -64 -115 355 O ATOM 105 OE2 GLU A 13 -26.337 2.005 9.160 1.00 39.24 O ANISOU 105 OE2 GLU A 13 5532 5061 4316 -107 -76 350 O ATOM 106 N LEU A 14 -30.535 1.672 5.733 1.00 29.85 N ANISOU 106 N LEU A 14 4606 3834 2902 6 -636 325 N ATOM 107 CA LEU A 14 -31.738 0.879 5.522 1.00 32.26 C ANISOU 107 CA LEU A 14 4857 4172 3231 12 -778 265 C ATOM 108 C LEU A 14 -31.425 -0.409 4.772 1.00 33.37 C ANISOU 108 C LEU A 14 5096 4317 3265 -33 -755 237 C ATOM 109 O LEU A 14 -31.980 -1.468 5.086 1.00 33.69 O ANISOU 109 O LEU A 14 5043 4394 3364 -65 -790 176 O ATOM 110 CB LEU A 14 -32.784 1.708 4.777 1.00 34.25 C ANISOU 110 CB LEU A 14 5164 4385 3463 79 -970 278 C ATOM 111 CG LEU A 14 -33.341 2.877 5.598 1.00 39.82 C ANISOU 111 CG LEU A 14 5742 5085 4303 136 -1017 282 C ATOM 112 CD1 LEU A 14 -34.248 3.759 4.750 1.00 40.08 C ANISOU 112 CD1 LEU A 14 5855 5063 4311 216 -1214 302 C ATOM 113 CD2 LEU A 14 -34.062 2.384 6.850 1.00 43.09 C ANISOU 113 CD2 LEU A 14 5917 5573 4880 123 -1004 209 C ATOM 114 N ALA A 15 -30.542 -0.337 3.773 1.00 32.70 N ANISOU 114 N ALA A 15 5206 4193 3027 -37 -692 279 N ATOM 115 CA ALA A 15 -30.124 -1.547 3.072 1.00 31.66 C ANISOU 115 CA ALA A 15 5178 4063 2789 -72 -651 242 C ATOM 116 C ALA A 15 -29.455 -2.533 4.022 1.00 30.80 C ANISOU 116 C ALA A 15 4947 3989 2767 -120 -511 205 C ATOM 117 O ALA A 15 -29.699 -3.743 3.945 1.00 32.43 O ANISOU 117 O ALA A 15 5141 4206 2975 -148 -534 145 O ATOM 118 CB ALA A 15 -29.184 -1.184 1.922 1.00 32.82 C ANISOU 118 CB ALA A 15 5550 4166 2754 -66 -570 296 C ATOM 119 N ILE A 16 -28.603 -2.037 4.922 1.00 28.94 N ANISOU 119 N ILE A 16 4627 3764 2606 -128 -376 238 N ATOM 120 CA ILE A 16 -27.934 -2.918 5.874 1.00 29.69 C ANISOU 120 CA ILE A 16 4612 3886 2782 -163 -258 208 C ATOM 121 C ILE A 16 -28.944 -3.529 6.837 1.00 28.78 C ANISOU 121 C ILE A 16 4336 3810 2790 -181 -333 163 C ATOM 122 O ILE A 16 -28.865 -4.719 7.169 1.00 27.58 O ANISOU 122 O ILE A 16 4145 3667 2666 -216 -304 125 O ATOM 123 CB ILE A 16 -26.831 -2.149 6.621 1.00 28.19 C ANISOU 123 CB ILE A 16 4368 3697 2647 -165 -121 250 C ATOM 124 CG1 ILE A 16 -25.712 -1.767 5.656 1.00 30.67 C ANISOU 124 CG1 ILE A 16 4831 3974 2850 -166 -13 290 C ATOM 125 CG2 ILE A 16 -26.282 -2.977 7.777 1.00 28.49 C ANISOU 125 CG2 ILE A 16 4278 3765 2783 -190 -34 220 C ATOM 126 CD1 ILE A 16 -24.763 -0.766 6.230 1.00 34.90 C ANISOU 126 CD1 ILE A 16 5317 4496 3447 -173 95 336 C ATOM 127 N ALA A 17 -29.908 -2.726 7.298 1.00 30.50 N ANISOU 127 N ALA A 17 4458 4045 3083 -157 -425 168 N ATOM 128 CA ALA A 17 -30.905 -3.225 8.241 1.00 27.96 C ANISOU 128 CA ALA A 17 3972 3767 2883 -178 -476 128 C ATOM 129 C ALA A 17 -31.721 -4.355 7.631 1.00 28.98 C ANISOU 129 C ALA A 17 4119 3893 3001 -211 -577 77 C ATOM 130 O ALA A 17 -32.003 -5.358 8.297 1.00 33.28 O ANISOU 130 O ALA A 17 4571 4456 3618 -260 -556 46 O ATOM 131 CB ALA A 17 -31.819 -2.086 8.693 1.00 24.58 C ANISOU 131 CB ALA A 17 3444 3359 2538 -134 -556 132 C ATOM 132 N AVAL A 18 -32.106 -4.209 6.361 1.00 30.81 N ANISOU 132 N AVAL A 18 4478 4092 3136 -186 -693 70 N ATOM 133 CA AVAL A 18 -32.880 -5.246 5.684 1.00 31.71 C ANISOU 133 CA AVAL A 18 4622 4194 3234 -216 -811 12 C ATOM 134 C AVAL A 18 -32.084 -6.543 5.613 1.00 30.42 C ANISOU 134 C AVAL A 18 4521 4009 3028 -264 -715 -15 C ATOM 135 O AVAL A 18 -32.598 -7.627 5.915 1.00 29.12 O ANISOU 135 O AVAL A 18 4288 3843 2934 -317 -748 -61 O ATOM 136 CB AVAL A 18 -33.302 -4.768 4.282 1.00 35.57 C ANISOU 136 CB AVAL A 18 5268 4647 3598 -171 -960 11 C ATOM 137 CG1AVAL A 18 -33.872 -5.923 3.472 1.00 36.19 C ANISOU 137 CG1AVAL A 18 5413 4704 3634 -204 -1078 -59 C ATOM 138 CG2AVAL A 18 -34.312 -3.637 4.392 1.00 36.53 C ANISOU 138 CG2AVAL A 18 5306 4781 3793 -119 -1092 24 C ATOM 139 N LEU A 19 -30.811 -6.450 5.222 1.00 30.08 N ANISOU 139 N LEU A 19 4605 3944 2880 -246 -593 14 N ATOM 140 CA LEU A 19 -29.998 -7.653 5.068 1.00 27.95 C ANISOU 140 CA LEU A 19 4401 3647 2571 -274 -503 -20 C ATOM 141 C LEU A 19 -29.690 -8.292 6.417 1.00 30.30 C ANISOU 141 C LEU A 19 4555 3962 2997 -311 -408 -18 C ATOM 142 O LEU A 19 -29.636 -9.522 6.530 1.00 32.54 O ANISOU 142 O LEU A 19 4840 4218 3305 -348 -399 -59 O ATOM 143 CB LEU A 19 -28.705 -7.316 4.326 1.00 25.65 C ANISOU 143 CB LEU A 19 4262 3335 2148 -242 -381 6 C ATOM 144 CG LEU A 19 -28.860 -6.890 2.863 1.00 32.06 C ANISOU 144 CG LEU A 19 5268 4122 2792 -210 -455 7 C ATOM 145 CD1 LEU A 19 -27.572 -6.264 2.350 1.00 36.20 C ANISOU 145 CD1 LEU A 19 5912 4636 3207 -186 -300 55 C ATOM 146 CD2 LEU A 19 -29.278 -8.069 1.995 1.00 36.49 C ANISOU 146 CD2 LEU A 19 5937 4652 3277 -224 -546 -72 C ATOM 147 N ALA A 20 -29.482 -7.473 7.450 1.00 30.93 N ANISOU 147 N ALA A 20 4521 4079 3153 -300 -344 27 N ATOM 148 CA ALA A 20 -29.217 -8.012 8.780 1.00 28.93 C ANISOU 148 CA ALA A 20 4146 3844 3004 -330 -263 35 C ATOM 149 C ALA A 20 -30.417 -8.784 9.316 1.00 34.34 C ANISOU 149 C ALA A 20 4727 4539 3782 -384 -341 6 C ATOM 150 O ALA A 20 -30.261 -9.851 9.921 1.00 31.63 O ANISOU 150 O ALA A 20 4354 4177 3486 -427 -299 -3 O ATOM 151 CB ALA A 20 -28.835 -6.883 9.736 1.00 28.04 C ANISOU 151 CB ALA A 20 3945 3769 2940 -303 -196 80 C ATOM 152 N ILE A 21 -31.623 -8.251 9.113 1.00 30.63 N ANISOU 152 N ILE A 21 4197 4094 3348 -384 -455 -7 N ATOM 153 CA ILE A 21 -32.832 -8.937 9.561 1.00 31.77 C ANISOU 153 CA ILE A 21 4223 4251 3597 -444 -526 -39 C ATOM 154 C ILE A 21 -33.028 -10.244 8.799 1.00 33.08 C ANISOU 154 C ILE A 21 4469 4360 3741 -493 -590 -88 C ATOM 155 O ILE A 21 -33.225 -11.305 9.401 1.00 34.54 O ANISOU 155 O ILE A 21 4601 4524 3999 -560 -564 -99 O ATOM 156 CB ILE A 21 -34.054 -8.011 9.426 1.00 34.46 C ANISOU 156 CB ILE A 21 4468 4631 3994 -421 -641 -52 C ATOM 157 CG1 ILE A 21 -33.909 -6.806 10.358 1.00 32.51 C ANISOU 157 CG1 ILE A 21 4131 4434 3788 -375 -570 -14 C ATOM 158 CG2 ILE A 21 -35.338 -8.771 9.730 1.00 36.58 C ANISOU 158 CG2 ILE A 21 4604 4912 4384 -491 -717 -95 C ATOM 159 CD1 ILE A 21 -34.870 -5.678 10.054 1.00 33.89 C ANISOU 159 CD1 ILE A 21 4245 4633 4001 -322 -683 -26 C ATOM 160 N LEU A 22 -32.976 -10.188 7.465 1.00 32.02 N ANISOU 160 N LEU A 22 4475 4191 3499 -462 -676 -119 N ATOM 161 CA LEU A 22 -33.283 -11.365 6.654 1.00 31.32 C ANISOU 161 CA LEU A 22 4471 4045 3385 -504 -763 -182 C ATOM 162 C LEU A 22 -32.304 -12.502 6.922 1.00 34.36 C ANISOU 162 C LEU A 22 4919 4378 3757 -528 -653 -189 C ATOM 163 O LEU A 22 -32.709 -13.657 7.098 1.00 38.69 O ANISOU 163 O LEU A 22 5446 4880 4373 -594 -686 -225 O ATOM 164 CB LEU A 22 -33.274 -10.995 5.172 1.00 35.60 C ANISOU 164 CB LEU A 22 5182 4563 3782 -452 -866 -213 C ATOM 165 CG LEU A 22 -34.410 -10.108 4.665 1.00 38.29 C ANISOU 165 CG LEU A 22 5486 4931 4132 -425 -1032 -221 C ATOM 166 CD1 LEU A 22 -34.195 -9.768 3.199 1.00 39.79 C ANISOU 166 CD1 LEU A 22 5886 5090 4142 -369 -1120 -238 C ATOM 167 CD2 LEU A 22 -35.744 -10.803 4.869 1.00 42.89 C ANISOU 167 CD2 LEU A 22 5932 5511 4854 -494 -1165 -278 C ATOM 168 N GLY A 23 -31.007 -12.194 6.954 1.00 31.60 N ANISOU 168 N GLY A 23 4644 4028 3333 -476 -525 -157 N ATOM 169 CA GLY A 23 -30.017 -13.246 7.110 1.00 32.73 C ANISOU 169 CA GLY A 23 4850 4119 3468 -481 -430 -172 C ATOM 170 C GLY A 23 -30.075 -13.909 8.472 1.00 31.60 C ANISOU 170 C GLY A 23 4588 3970 3451 -532 -376 -142 C ATOM 171 O GLY A 23 -29.941 -15.131 8.584 1.00 33.35 O ANISOU 171 O GLY A 23 4843 4124 3706 -568 -372 -169 O ATOM 172 N ASN A 24 -30.271 -13.117 9.524 1.00 32.50 N ANISOU 172 N ASN A 24 4573 4146 3627 -534 -333 -86 N ATOM 173 CA ASN A 24 -30.236 -13.666 10.873 1.00 33.31 C ANISOU 173 CA ASN A 24 4583 4249 3823 -577 -267 -47 C ATOM 174 C ASN A 24 -31.563 -14.302 11.271 1.00 31.65 C ANISOU 174 C ASN A 24 4282 4033 3712 -667 -336 -58 C ATOM 175 O ASN A 24 -31.576 -15.220 12.100 1.00 33.47 O ANISOU 175 O ASN A 24 4485 4227 4005 -723 -294 -35 O ATOM 176 CB ASN A 24 -29.834 -12.571 11.859 1.00 29.87 C ANISOU 176 CB ASN A 24 4064 3884 3401 -539 -186 9 C ATOM 177 CG ASN A 24 -28.365 -12.208 11.747 1.00 31.26 C ANISOU 177 CG ASN A 24 4310 4053 3516 -470 -99 23 C ATOM 178 OD1 ASN A 24 -27.491 -12.992 12.116 1.00 28.69 O ANISOU 178 OD1 ASN A 24 4016 3684 3199 -462 -40 28 O ATOM 179 ND2 ASN A 24 -28.085 -11.030 11.204 1.00 27.63 N ANISOU 179 ND2 ASN A 24 3871 3628 3001 -420 -92 30 N ATOM 180 N VAL A 25 -32.681 -13.827 10.716 1.00 31.98 N ANISOU 180 N VAL A 25 4271 4106 3775 -684 -441 -89 N ATOM 181 CA VAL A 25 -33.923 -14.592 10.801 1.00 36.66 C ANISOU 181 CA VAL A 25 4782 4677 4470 -777 -521 -118 C ATOM 182 C VAL A 25 -33.728 -15.976 10.196 1.00 36.89 C ANISOU 182 C VAL A 25 4922 4602 4491 -822 -564 -163 C ATOM 183 O VAL A 25 -34.207 -16.982 10.735 1.00 36.63 O ANISOU 183 O VAL A 25 4845 4521 4553 -913 -562 -160 O ATOM 184 CB VAL A 25 -35.076 -13.825 10.125 1.00 38.60 C ANISOU 184 CB VAL A 25 4957 4968 4742 -771 -652 -158 C ATOM 185 CG1 VAL A 25 -36.227 -14.761 9.792 1.00 36.95 C ANISOU 185 CG1 VAL A 25 4692 4715 4630 -866 -767 -214 C ATOM 186 CG2 VAL A 25 -35.565 -12.707 11.033 1.00 36.46 C ANISOU 186 CG2 VAL A 25 4532 4789 4532 -750 -606 -120 C ATOM 187 N LEU A 26 -33.015 -16.048 9.068 1.00 38.54 N ANISOU 187 N LEU A 26 5286 4771 4587 -761 -595 -207 N ATOM 188 CA LEU A 26 -32.751 -17.334 8.430 1.00 34.47 C ANISOU 188 CA LEU A 26 4893 4151 4054 -788 -634 -265 C ATOM 189 C LEU A 26 -31.930 -18.242 9.337 1.00 33.20 C ANISOU 189 C LEU A 26 4750 3931 3934 -804 -525 -226 C ATOM 190 O LEU A 26 -32.160 -19.456 9.386 1.00 35.25 O ANISOU 190 O LEU A 26 5042 4097 4255 -870 -558 -252 O ATOM 191 CB LEU A 26 -32.033 -17.112 7.098 1.00 36.90 C ANISOU 191 CB LEU A 26 5369 4440 4210 -705 -659 -319 C ATOM 192 CG LEU A 26 -31.847 -18.310 6.167 1.00 51.04 C ANISOU 192 CG LEU A 26 7309 6126 5956 -715 -720 -405 C ATOM 193 CD1 LEU A 26 -33.190 -18.855 5.709 1.00 58.45 C ANISOU 193 CD1 LEU A 26 8219 7027 6963 -799 -889 -468 C ATOM 194 CD2 LEU A 26 -30.978 -17.929 4.977 1.00 49.17 C ANISOU 194 CD2 LEU A 26 7241 5891 5549 -621 -699 -447 C ATOM 195 N VAL A 27 -30.958 -17.672 10.053 1.00 30.86 N ANISOU 195 N VAL A 27 4438 3678 3609 -743 -405 -166 N ATOM 196 CA VAL A 27 -30.191 -18.447 11.025 1.00 34.46 C ANISOU 196 CA VAL A 27 4904 4083 4107 -748 -317 -122 C ATOM 197 C VAL A 27 -31.116 -19.022 12.090 1.00 34.37 C ANISOU 197 C VAL A 27 4793 4057 4209 -854 -319 -75 C ATOM 198 O VAL A 27 -31.076 -20.220 12.394 1.00 35.56 O ANISOU 198 O VAL A 27 4989 4109 4412 -907 -321 -69 O ATOM 199 CB VAL A 27 -29.080 -17.581 11.647 1.00 33.15 C ANISOU 199 CB VAL A 27 4717 3978 3899 -665 -209 -69 C ATOM 200 CG1 VAL A 27 -28.526 -18.248 12.896 1.00 31.46 C ANISOU 200 CG1 VAL A 27 4487 3726 3740 -677 -140 -10 C ATOM 201 CG2 VAL A 27 -27.973 -17.337 10.636 1.00 33.63 C ANISOU 201 CG2 VAL A 27 4887 4027 3864 -574 -178 -114 C ATOM 202 N CYS A 28 -31.961 -18.168 12.675 1.00 33.06 N ANISOU 202 N CYS A 28 4494 3984 4082 -885 -312 -40 N ATOM 203 CA CYS A 28 -32.845 -18.608 13.749 1.00 37.61 C ANISOU 203 CA CYS A 28 4965 4563 4760 -989 -285 10 C ATOM 204 C CYS A 28 -33.845 -19.641 13.250 1.00 41.07 C ANISOU 204 C CYS A 28 5398 4921 5284 -1096 -377 -36 C ATOM 205 O CYS A 28 -34.161 -20.604 13.960 1.00 42.67 O ANISOU 205 O CYS A 28 5589 5058 5565 -1190 -348 2 O ATOM 206 CB CYS A 28 -33.572 -17.405 14.350 1.00 37.87 C ANISOU 206 CB CYS A 28 4851 4720 4818 -988 -255 37 C ATOM 207 SG CYS A 28 -32.492 -16.224 15.191 1.00 39.94 S ANISOU 207 SG CYS A 28 5108 5068 5001 -882 -147 92 S ATOM 208 N ATRP A 29 -34.358 -19.444 12.032 0.50 40.20 N ANISOU 208 N ATRP A 29 5302 4810 5160 -1087 -496 -117 N ATOM 209 N BTRP A 29 -34.357 -19.471 12.030 0.50 40.20 N ANISOU 209 N BTRP A 29 5304 4808 5160 -1089 -496 -117 N ATOM 210 CA ATRP A 29 -35.280 -20.400 11.428 0.50 42.39 C ANISOU 210 CA ATRP A 29 5580 5006 5520 -1186 -609 -179 C ATOM 211 CA BTRP A 29 -35.303 -20.457 11.521 0.50 42.42 C ANISOU 211 CA BTRP A 29 5578 5007 5532 -1194 -603 -174 C ATOM 212 C ATRP A 29 -34.605 -21.746 11.205 0.50 42.33 C ANISOU 212 C ATRP A 29 5721 4857 5507 -1204 -614 -199 C ATOM 213 C BTRP A 29 -34.614 -21.771 11.175 0.50 42.36 C ANISOU 213 C BTRP A 29 5727 4858 5511 -1205 -617 -201 C ATOM 214 O ATRP A 29 -35.220 -22.801 11.403 0.50 41.31 O ANISOU 214 O ATRP A 29 5580 4635 5482 -1317 -649 -204 O ATOM 215 O BTRP A 29 -35.240 -22.833 11.257 0.50 41.86 O ANISOU 215 O BTRP A 29 5658 4699 5549 -1316 -664 -216 O ATOM 216 CB ATRP A 29 -35.805 -19.829 10.108 0.50 45.31 C ANISOU 216 CB ATRP A 29 5964 5406 5847 -1148 -751 -266 C ATOM 217 CB BTRP A 29 -36.055 -19.909 10.307 0.50 45.72 C ANISOU 217 CB BTRP A 29 5979 5459 5933 -1176 -750 -259 C ATOM 218 CG ATRP A 29 -37.064 -20.458 9.593 0.50 49.93 C ANISOU 218 CG ATRP A 29 6486 5943 6542 -1254 -892 -333 C ATOM 219 CG BTRP A 29 -37.547 -19.975 10.474 0.50 50.30 C ANISOU 219 CG BTRP A 29 6390 6063 6660 -1286 -827 -279 C ATOM 220 CD1ATRP A 29 -37.735 -21.516 10.130 0.50 54.23 C ANISOU 220 CD1ATRP A 29 6967 6413 7226 -1388 -895 -326 C ATOM 221 CD1BTRP A 29 -38.290 -21.080 10.778 0.50 54.01 C ANISOU 221 CD1BTRP A 29 6805 6452 7265 -1422 -852 -288 C ATOM 222 CD2ATRP A 29 -37.810 -20.056 8.436 0.50 51.73 C ANISOU 222 CD2ATRP A 29 6710 6189 6755 -1237 -1060 -419 C ATOM 223 CD2BTRP A 29 -38.476 -18.892 10.344 0.50 50.99 C ANISOU 223 CD2BTRP A 29 6329 6255 6788 -1269 -888 -297 C ATOM 224 NE1ATRP A 29 -38.850 -21.801 9.378 0.50 56.13 N ANISOU 224 NE1ATRP A 29 7147 6626 7554 -1461 -1054 -409 N ATOM 225 NE1BTRP A 29 -39.623 -20.750 10.849 0.50 56.03 N ANISOU 225 NE1BTRP A 29 6874 6766 7650 -1497 -917 -313 N ATOM 226 CE2ATRP A 29 -38.918 -20.919 8.332 0.50 53.03 C ANISOU 226 CE2ATRP A 29 6791 6291 7065 -1365 -1167 -470 C ATOM 227 CE2BTRP A 29 -39.763 -19.413 10.585 0.50 54.98 C ANISOU 227 CE2BTRP A 29 6679 6747 7463 -1397 -945 -322 C ATOM 228 CE3ATRP A 29 -37.646 -19.050 7.479 0.50 54.72 C ANISOU 228 CE3ATRP A 29 7154 6627 7010 -1129 -1137 -454 C ATOM 229 CE3BTRP A 29 -38.345 -17.533 10.047 0.50 47.55 C ANISOU 229 CE3BTRP A 29 5878 5916 6273 -1158 -902 -295 C ATOM 230 CZ2ATRP A 29 -39.857 -20.809 7.309 0.50 54.24 C ANISOU 230 CZ2ATRP A 29 6916 6442 7249 -1382 -1360 -564 C ATOM 231 CZ2BTRP A 29 -40.910 -18.623 10.538 0.50 57.10 C ANISOU 231 CZ2BTRP A 29 6763 7104 7828 -1408 -1017 -352 C ATOM 232 CZ3ATRP A 29 -38.580 -18.943 6.463 0.50 54.55 C ANISOU 232 CZ3ATRP A 29 7123 6601 7002 -1141 -1327 -538 C ATOM 233 CZ3BTRP A 29 -39.483 -16.750 10.002 0.50 49.48 C ANISOU 233 CZ3BTRP A 29 5957 6238 6605 -1164 -982 -320 C ATOM 234 CH2ATRP A 29 -39.670 -19.817 6.387 0.50 54.54 C ANISOU 234 CH2ATRP A 29 7030 6541 7153 -1263 -1444 -596 C ATOM 235 CH2BTRP A 29 -40.749 -17.297 10.246 0.50 55.33 C ANISOU 235 CH2BTRP A 29 6532 6972 7521 -1284 -1039 -352 C ATOM 236 N ALA A 30 -33.333 -21.727 10.800 1.00 40.14 N ANISOU 236 N ALA A 30 5580 4554 5119 -1095 -575 -212 N ATOM 237 CA ALA A 30 -32.605 -22.967 10.549 1.00 37.34 C ANISOU 237 CA ALA A 30 5368 4061 4759 -1089 -579 -243 C ATOM 238 C ALA A 30 -32.419 -23.762 11.837 1.00 40.26 C ANISOU 238 C ALA A 30 5721 4365 5211 -1149 -498 -155 C ATOM 239 O ALA A 30 -32.628 -24.980 11.865 1.00 42.02 O ANISOU 239 O ALA A 30 6004 4456 5508 -1224 -537 -168 O ATOM 240 CB ALA A 30 -31.254 -22.659 9.903 1.00 31.43 C ANISOU 240 CB ALA A 30 4742 3317 3882 -950 -533 -277 C ATOM 241 N VAL A 31 -32.014 -23.085 12.914 1.00 40.09 N ANISOU 241 N VAL A 31 5633 4427 5173 -1115 -391 -65 N ATOM 242 CA VAL A 31 -31.803 -23.765 14.189 1.00 40.33 C ANISOU 242 CA VAL A 31 5666 4402 5255 -1164 -316 29 C ATOM 243 C VAL A 31 -33.117 -24.324 14.720 1.00 41.67 C ANISOU 243 C VAL A 31 5750 4542 5541 -1323 -330 65 C ATOM 244 O VAL A 31 -33.171 -25.452 15.225 1.00 40.49 O ANISOU 244 O VAL A 31 5658 4270 5456 -1401 -321 108 O ATOM 245 CB VAL A 31 -31.136 -22.813 15.199 1.00 38.89 C ANISOU 245 CB VAL A 31 5433 4327 5015 -1090 -212 109 C ATOM 246 CG1 VAL A 31 -30.954 -23.504 16.542 1.00 37.35 C ANISOU 246 CG1 VAL A 31 5259 4076 4854 -1138 -145 211 C ATOM 247 CG2 VAL A 31 -29.797 -22.327 14.660 1.00 34.62 C ANISOU 247 CG2 VAL A 31 4966 3805 4383 -946 -195 71 C ATOM 248 N TRP A 32 -34.193 -23.537 14.626 1.00 42.47 N ANISOU 248 N TRP A 32 5708 4749 5678 -1374 -348 49 N ATOM 249 CA TRP A 32 -35.502 -24.000 15.080 1.00 45.56 C ANISOU 249 CA TRP A 32 5987 5126 6199 -1530 -352 72 C ATOM 250 C TRP A 32 -35.942 -25.259 14.340 1.00 48.39 C ANISOU 250 C TRP A 32 6412 5331 6643 -1624 -459 10 C ATOM 251 O TRP A 32 -36.518 -26.171 14.944 1.00 47.50 O ANISOU 251 O TRP A 32 6280 5131 6636 -1759 -435 59 O ATOM 252 CB TRP A 32 -36.538 -22.886 14.910 1.00 49.31 C ANISOU 252 CB TRP A 32 6287 5741 6708 -1545 -374 41 C ATOM 253 CG TRP A 32 -37.952 -23.292 15.250 1.00 60.33 C ANISOU 253 CG TRP A 32 7533 7132 8256 -1705 -380 46 C ATOM 254 CD1 TRP A 32 -38.800 -24.042 14.486 1.00 61.38 C ANISOU 254 CD1 TRP A 32 7640 7182 8501 -1808 -499 -27 C ATOM 255 CD2 TRP A 32 -38.678 -22.963 16.444 1.00 67.95 C ANISOU 255 CD2 TRP A 32 8350 8183 9287 -1784 -257 121 C ATOM 256 NE1 TRP A 32 -40.003 -24.204 15.130 1.00 66.18 N ANISOU 256 NE1 TRP A 32 8076 7817 9254 -1952 -456 2 N ATOM 257 CE2 TRP A 32 -39.954 -23.551 16.334 1.00 69.45 C ANISOU 257 CE2 TRP A 32 8414 8337 9638 -1939 -297 93 C ATOM 258 CE3 TRP A 32 -38.370 -22.232 17.596 1.00 70.24 C ANISOU 258 CE3 TRP A 32 8602 8575 9513 -1740 -114 203 C ATOM 259 CZ2 TRP A 32 -40.922 -23.428 17.330 1.00 73.82 C ANISOU 259 CZ2 TRP A 32 8797 8959 10292 -2051 -181 148 C ATOM 260 CZ3 TRP A 32 -39.334 -22.112 18.585 1.00 73.16 C ANISOU 260 CZ3 TRP A 32 8820 9012 9964 -1844 -4 254 C ATOM 261 CH2 TRP A 32 -40.593 -22.707 18.445 1.00 73.97 C ANISOU 261 CH2 TRP A 32 8793 9083 10230 -1999 -29 228 C ATOM 262 N LEU A 33 -35.682 -25.329 13.033 1.00 48.67 N ANISOU 262 N LEU A 33 6535 5328 6632 -1560 -575 -98 N ATOM 263 CA LEU A 33 -36.236 -26.411 12.226 1.00 50.59 C ANISOU 263 CA LEU A 33 6832 5433 6957 -1649 -700 -180 C ATOM 264 C LEU A 33 -35.406 -27.687 12.283 1.00 53.02 C ANISOU 264 C LEU A 33 7312 5566 7265 -1645 -695 -175 C ATOM 265 O LEU A 33 -35.970 -28.784 12.228 1.00 58.10 O ANISOU 265 O LEU A 33 7982 6072 8021 -1767 -754 -192 O ATOM 266 CB LEU A 33 -36.379 -25.972 10.769 1.00 54.19 C ANISOU 266 CB LEU A 33 7325 5917 7347 -1581 -839 -307 C ATOM 267 CG LEU A 33 -37.511 -25.006 10.421 1.00 59.80 C ANISOU 267 CG LEU A 33 7873 6752 8097 -1609 -913 -343 C ATOM 268 CD1 LEU A 33 -37.495 -24.716 8.928 1.00 63.11 C ANISOU 268 CD1 LEU A 33 8383 7173 8422 -1531 -1064 -463 C ATOM 269 CD2 LEU A 33 -38.857 -25.565 10.856 1.00 60.45 C ANISOU 269 CD2 LEU A 33 7801 6801 8366 -1785 -949 -336 C ATOM 270 N ASN A 34 -34.086 -27.578 12.390 1.00 48.04 N ANISOU 270 N ASN A 34 6796 4931 6528 -1510 -631 -154 N ATOM 271 CA ASN A 34 -33.191 -28.716 12.218 1.00 47.17 C ANISOU 271 CA ASN A 34 6855 4654 6412 -1469 -646 -177 C ATOM 272 C ASN A 34 -32.640 -29.122 13.578 1.00 48.78 C ANISOU 272 C ASN A 34 7082 4812 6641 -1477 -540 -46 C ATOM 273 O ASN A 34 -31.922 -28.347 14.219 1.00 46.14 O ANISOU 273 O ASN A 34 6722 4581 6230 -1385 -450 19 O ATOM 274 CB ASN A 34 -32.058 -28.366 11.250 1.00 45.87 C ANISOU 274 CB ASN A 34 6802 4509 6119 -1301 -657 -264 C ATOM 275 CG ASN A 34 -31.183 -29.561 10.906 1.00 51.33 C ANISOU 275 CG ASN A 34 7663 5025 6815 -1246 -682 -317 C ATOM 276 OD1 ASN A 34 -31.302 -30.632 11.501 1.00 53.52 O ANISOU 276 OD1 ASN A 34 7988 5159 7189 -1323 -691 -272 O ATOM 277 ND2 ASN A 34 -30.293 -29.379 9.937 1.00 47.26 N ANISOU 277 ND2 ASN A 34 7245 4518 6195 -1111 -688 -413 N ATOM 278 N ASER A 35 -32.974 -30.342 14.011 1.00 49.75 N ANISOU 278 N ASER A 35 7262 4772 6867 -1590 -559 -6 N ATOM 279 CA ASER A 35 -32.477 -30.845 15.286 1.00 49.05 C ANISOU 279 CA ASER A 35 7227 4618 6793 -1601 -473 126 C ATOM 280 C ASER A 35 -30.982 -31.132 15.248 1.00 47.72 C ANISOU 280 C ASER A 35 7196 4380 6553 -1436 -466 115 C ATOM 281 O ASER A 35 -30.348 -31.180 16.308 1.00 48.41 O ANISOU 281 O ASER A 35 7316 4461 6617 -1396 -398 223 O ATOM 282 CB ASER A 35 -33.240 -32.105 15.695 1.00 52.11 C ANISOU 282 CB ASER A 35 7655 4831 7313 -1772 -499 176 C ATOM 283 OG ASER A 35 -32.957 -33.182 14.820 1.00 56.58 O ANISOU 283 OG ASER A 35 8361 5212 7926 -1760 -606 79 O ATOM 284 N ASN A 36 -30.404 -31.323 14.059 1.00 43.38 N ANISOU 284 N ASN A 36 6729 3783 5969 -1336 -534 -15 N ATOM 285 CA ASN A 36 -28.954 -31.446 13.952 1.00 46.69 C ANISOU 285 CA ASN A 36 7249 4164 6328 -1165 -513 -41 C ATOM 286 C ASN A 36 -28.246 -30.139 14.279 1.00 46.62 C ANISOU 286 C ASN A 36 7155 4340 6219 -1050 -427 -7 C ATOM 287 O ASN A 36 -27.039 -30.148 14.540 1.00 49.01 O ANISOU 287 O ASN A 36 7506 4627 6489 -920 -392 3 O ATOM 288 CB ASN A 36 -28.565 -31.910 12.549 1.00 54.62 C ANISOU 288 CB ASN A 36 8356 5086 7310 -1088 -587 -200 C ATOM 289 CG ASN A 36 -29.007 -33.329 12.260 1.00 62.17 C ANISOU 289 CG ASN A 36 9425 5825 8370 -1176 -681 -244 C ATOM 290 OD1 ASN A 36 -29.238 -34.118 13.177 1.00 69.24 O ANISOU 290 OD1 ASN A 36 10353 6600 9355 -1263 -679 -145 O ATOM 291 ND2 ASN A 36 -29.128 -33.662 10.981 1.00 61.01 N ANISOU 291 ND2 ASN A 36 9352 5622 8207 -1156 -764 -394 N ATOM 292 N LEU A 37 -28.968 -29.021 14.272 1.00 44.40 N ANISOU 292 N LEU A 37 6745 4225 5901 -1095 -399 7 N ATOM 293 CA LEU A 37 -28.411 -27.722 14.617 1.00 45.20 C ANISOU 293 CA LEU A 37 6761 4495 5917 -1002 -323 40 C ATOM 294 C LEU A 37 -28.750 -27.306 16.038 1.00 44.15 C ANISOU 294 C LEU A 37 6546 4435 5793 -1061 -253 173 C ATOM 295 O LEU A 37 -28.344 -26.223 16.467 1.00 43.00 O ANISOU 295 O LEU A 37 6329 4424 5583 -994 -193 205 O ATOM 296 CB LEU A 37 -28.903 -26.650 13.637 1.00 40.83 C ANISOU 296 CB LEU A 37 6132 4076 5305 -991 -342 -37 C ATOM 297 CG LEU A 37 -28.375 -26.731 12.204 1.00 44.02 C ANISOU 297 CG LEU A 37 6626 4450 5649 -902 -388 -167 C ATOM 298 CD1 LEU A 37 -29.137 -25.775 11.301 1.00 41.60 C ANISOU 298 CD1 LEU A 37 6261 4259 5287 -920 -430 -225 C ATOM 299 CD2 LEU A 37 -26.882 -26.435 12.169 1.00 38.46 C ANISOU 299 CD2 LEU A 37 5965 3766 4882 -749 -317 -179 C ATOM 300 N GLN A 38 -29.490 -28.132 16.776 1.00 41.80 N ANISOU 300 N GLN A 38 6262 4048 5570 -1190 -253 249 N ATOM 301 CA GLN A 38 -29.933 -27.776 18.122 1.00 43.75 C ANISOU 301 CA GLN A 38 6443 4368 5813 -1260 -173 375 C ATOM 302 C GLN A 38 -28.928 -28.352 19.111 1.00 48.11 C ANISOU 302 C GLN A 38 7104 4833 6342 -1196 -150 465 C ATOM 303 O GLN A 38 -29.062 -29.477 19.594 1.00 53.30 O ANISOU 303 O GLN A 38 7858 5340 7054 -1268 -165 529 O ATOM 304 CB GLN A 38 -31.350 -28.276 18.372 1.00 40.54 C ANISOU 304 CB GLN A 38 5981 3926 5498 -1445 -169 411 C ATOM 305 CG GLN A 38 -32.383 -27.611 17.474 1.00 46.57 C ANISOU 305 CG GLN A 38 6614 4787 6293 -1499 -207 322 C ATOM 306 CD GLN A 38 -33.724 -28.315 17.488 1.00 52.97 C ANISOU 306 CD GLN A 38 7367 5532 7228 -1683 -230 330 C ATOM 307 OE1 GLN A 38 -33.934 -29.267 18.239 1.00 56.23 O ANISOU 307 OE1 GLN A 38 7836 5827 7700 -1785 -197 416 O ATOM 308 NE2 GLN A 38 -34.644 -27.846 16.651 1.00 52.76 N ANISOU 308 NE2 GLN A 38 7227 5574 7246 -1729 -291 242 N ATOM 309 N ASN A 39 -27.905 -27.557 19.410 1.00 52.14 N ANISOU 309 N ASN A 39 7601 5434 6775 -1061 -120 470 N ATOM 310 CA ASN A 39 -26.891 -27.882 20.398 1.00 48.54 C ANISOU 310 CA ASN A 39 7230 4923 6290 -981 -112 551 C ATOM 311 C ASN A 39 -26.537 -26.601 21.137 1.00 45.40 C ANISOU 311 C ASN A 39 6746 4695 5808 -917 -53 589 C ATOM 312 O ASN A 39 -26.955 -25.506 20.749 1.00 42.05 O ANISOU 312 O ASN A 39 6208 4415 5356 -920 -20 542 O ATOM 313 CB ASN A 39 -25.650 -28.511 19.749 1.00 48.79 C ANISOU 313 CB ASN A 39 7356 4840 6344 -845 -175 479 C ATOM 314 CG ASN A 39 -25.156 -27.724 18.549 1.00 52.44 C ANISOU 314 CG ASN A 39 7755 5391 6778 -747 -174 352 C ATOM 315 OD1 ASN A 39 -24.715 -26.581 18.679 1.00 56.23 O ANISOU 315 OD1 ASN A 39 8150 6013 7200 -678 -131 347 O ATOM 316 ND2 ASN A 39 -25.225 -28.335 17.371 1.00 51.69 N ANISOU 316 ND2 ASN A 39 7712 5209 6719 -743 -221 249 N ATOM 317 N VAL A 40 -25.772 -26.741 22.222 1.00 49.18 N ANISOU 317 N VAL A 40 7289 5149 6247 -857 -50 673 N ATOM 318 CA VAL A 40 -25.480 -25.585 23.067 1.00 45.28 C ANISOU 318 CA VAL A 40 6726 4805 5671 -806 -2 712 C ATOM 319 C VAL A 40 -24.735 -24.516 22.276 1.00 41.35 C ANISOU 319 C VAL A 40 6140 4413 5158 -690 -6 610 C ATOM 320 O VAL A 40 -25.024 -23.319 22.400 1.00 44.15 O ANISOU 320 O VAL A 40 6393 4914 5468 -691 40 598 O ATOM 321 CB VAL A 40 -24.689 -26.020 24.314 1.00 44.49 C ANISOU 321 CB VAL A 40 6733 4644 5528 -750 -26 812 C ATOM 322 CG1 VAL A 40 -24.083 -24.809 24.998 1.00 43.09 C ANISOU 322 CG1 VAL A 40 6490 4610 5271 -663 -6 817 C ATOM 323 CG2 VAL A 40 -25.590 -26.786 25.269 1.00 40.18 C ANISOU 323 CG2 VAL A 40 6271 4031 4967 -885 10 935 C ATOM 324 N THR A 41 -23.760 -24.930 21.459 1.00 38.34 N ANISOU 324 N THR A 41 5797 3954 4816 -590 -54 536 N ATOM 325 CA THR A 41 -22.997 -23.978 20.656 1.00 39.55 C ANISOU 325 CA THR A 41 5873 4198 4957 -488 -41 444 C ATOM 326 C THR A 41 -23.910 -23.074 19.838 1.00 38.70 C ANISOU 326 C THR A 41 5676 4201 4828 -548 -5 390 C ATOM 327 O THR A 41 -23.703 -21.857 19.771 1.00 38.65 O ANISOU 327 O THR A 41 5584 4318 4782 -507 29 368 O ATOM 328 CB THR A 41 -22.033 -24.722 19.730 1.00 43.10 C ANISOU 328 CB THR A 41 6380 4538 5458 -393 -78 360 C ATOM 329 OG1 THR A 41 -21.618 -25.947 20.347 1.00 47.65 O ANISOU 329 OG1 THR A 41 7064 4962 6078 -371 -133 411 O ATOM 330 CG2 THR A 41 -20.810 -23.867 19.430 1.00 43.29 C ANISOU 330 CG2 THR A 41 6334 4638 5475 -265 -55 301 C ATOM 331 N ASN A 42 -24.933 -23.656 19.212 1.00 37.70 N ANISOU 331 N ASN A 42 5569 4024 4732 -646 -23 368 N ATOM 332 CA ASN A 42 -25.827 -22.909 18.340 1.00 34.58 C ANISOU 332 CA ASN A 42 5097 3718 4324 -696 -16 310 C ATOM 333 C ASN A 42 -26.884 -22.107 19.090 1.00 33.21 C ANISOU 333 C ASN A 42 4825 3658 4134 -780 25 366 C ATOM 334 O ASN A 42 -27.496 -21.214 18.494 1.00 34.61 O ANISOU 334 O ASN A 42 4921 3930 4299 -794 28 322 O ATOM 335 CB ASN A 42 -26.501 -23.858 17.351 1.00 33.22 C ANISOU 335 CB ASN A 42 4980 3443 4199 -764 -72 250 C ATOM 336 CG ASN A 42 -25.569 -24.286 16.233 1.00 38.05 C ANISOU 336 CG ASN A 42 5671 3981 4806 -668 -101 154 C ATOM 337 OD1 ASN A 42 -24.507 -23.697 16.037 1.00 35.02 O ANISOU 337 OD1 ASN A 42 5275 3645 4386 -556 -68 125 O ATOM 338 ND2 ASN A 42 -25.960 -25.319 15.498 1.00 38.83 N ANISOU 338 ND2 ASN A 42 5849 3960 4946 -713 -158 99 N ATOM 339 N TYR A 43 -27.125 -22.399 20.370 1.00 33.78 N ANISOU 339 N TYR A 43 4909 3723 4203 -830 58 462 N ATOM 340 CA TYR A 43 -27.977 -21.510 21.155 1.00 37.29 C ANISOU 340 CA TYR A 43 5257 4292 4621 -887 118 506 C ATOM 341 C TYR A 43 -27.316 -20.152 21.348 1.00 33.82 C ANISOU 341 C TYR A 43 4754 3973 4121 -787 142 486 C ATOM 342 O TYR A 43 -27.995 -19.118 21.339 1.00 33.16 O ANISOU 342 O TYR A 43 4571 4002 4025 -804 171 468 O ATOM 343 CB TYR A 43 -28.315 -22.151 22.501 1.00 37.14 C ANISOU 343 CB TYR A 43 5285 4236 4591 -962 162 615 C ATOM 344 CG TYR A 43 -28.968 -23.507 22.370 1.00 45.58 C ANISOU 344 CG TYR A 43 6419 5169 5729 -1076 143 645 C ATOM 345 CD1 TYR A 43 -29.735 -23.823 21.254 1.00 48.95 C ANISOU 345 CD1 TYR A 43 6807 5560 6230 -1143 100 573 C ATOM 346 CD2 TYR A 43 -28.830 -24.468 23.362 1.00 45.27 C ANISOU 346 CD2 TYR A 43 6489 5029 5682 -1120 158 748 C ATOM 347 CE1 TYR A 43 -30.337 -25.056 21.126 1.00 52.80 C ANISOU 347 CE1 TYR A 43 7352 5915 6795 -1255 75 593 C ATOM 348 CE2 TYR A 43 -29.431 -25.707 23.242 1.00 51.17 C ANISOU 348 CE2 TYR A 43 7302 5637 6502 -1233 141 780 C ATOM 349 CZ TYR A 43 -30.183 -25.994 22.122 1.00 55.58 C ANISOU 349 CZ TYR A 43 7808 6161 7147 -1304 100 698 C ATOM 350 OH TYR A 43 -30.786 -27.223 21.991 1.00 60.84 O ANISOU 350 OH TYR A 43 8537 6681 7901 -1425 75 723 O ATOM 351 N PHE A 44 -25.994 -20.133 21.525 1.00 30.04 N ANISOU 351 N PHE A 44 4328 3469 3619 -680 125 485 N ATOM 352 CA PHE A 44 -25.276 -18.864 21.555 1.00 31.14 C ANISOU 352 CA PHE A 44 4405 3707 3719 -589 140 454 C ATOM 353 C PHE A 44 -25.260 -18.214 20.176 1.00 31.34 C ANISOU 353 C PHE A 44 4385 3768 3755 -559 130 368 C ATOM 354 O PHE A 44 -25.306 -16.983 20.061 1.00 29.85 O ANISOU 354 O PHE A 44 4123 3677 3541 -531 150 346 O ATOM 355 CB PHE A 44 -23.856 -19.075 22.077 1.00 27.72 C ANISOU 355 CB PHE A 44 4024 3230 3278 -489 116 469 C ATOM 356 CG PHE A 44 -23.802 -19.496 23.518 1.00 33.99 C ANISOU 356 CG PHE A 44 4875 4005 4036 -503 114 560 C ATOM 357 CD1 PHE A 44 -24.121 -18.601 24.525 1.00 40.10 C ANISOU 357 CD1 PHE A 44 5607 4881 4747 -514 151 596 C ATOM 358 CD2 PHE A 44 -23.435 -20.785 23.865 1.00 30.86 C ANISOU 358 CD2 PHE A 44 4587 3479 3658 -502 73 608 C ATOM 359 CE1 PHE A 44 -24.075 -18.983 25.852 1.00 44.17 C ANISOU 359 CE1 PHE A 44 6196 5382 5205 -526 152 681 C ATOM 360 CE2 PHE A 44 -23.388 -21.174 25.192 1.00 35.20 C ANISOU 360 CE2 PHE A 44 5213 4005 4158 -514 67 703 C ATOM 361 CZ PHE A 44 -23.707 -20.270 26.187 1.00 36.38 C ANISOU 361 CZ PHE A 44 5327 4267 4229 -528 109 740 C ATOM 362 N VAL A 45 -25.176 -19.029 19.120 1.00 33.03 N ANISOU 362 N VAL A 45 4657 3896 3999 -561 96 319 N ATOM 363 CA VAL A 45 -25.300 -18.521 17.755 1.00 31.62 C ANISOU 363 CA VAL A 45 4463 3744 3809 -543 84 241 C ATOM 364 C VAL A 45 -26.648 -17.838 17.550 1.00 29.08 C ANISOU 364 C VAL A 45 4065 3500 3485 -617 76 236 C ATOM 365 O VAL A 45 -26.735 -16.786 16.903 1.00 27.20 O ANISOU 365 O VAL A 45 3785 3334 3218 -586 75 200 O ATOM 366 CB VAL A 45 -25.085 -19.665 16.744 1.00 32.30 C ANISOU 366 CB VAL A 45 4641 3715 3916 -539 45 185 C ATOM 367 CG1 VAL A 45 -25.549 -19.252 15.353 1.00 32.95 C ANISOU 367 CG1 VAL A 45 4728 3823 3968 -545 21 109 C ATOM 368 CG2 VAL A 45 -23.622 -20.092 16.725 1.00 25.96 C ANISOU 368 CG2 VAL A 45 3891 2850 3122 -437 59 166 C ATOM 369 N VAL A 46 -27.716 -18.410 18.112 1.00 31.84 N ANISOU 369 N VAL A 46 4393 3834 3872 -715 70 275 N ATOM 370 CA VAL A 46 -29.034 -17.793 17.991 1.00 32.58 C ANISOU 370 CA VAL A 46 4391 4004 3986 -783 63 264 C ATOM 371 C VAL A 46 -29.103 -16.502 18.795 1.00 32.74 C ANISOU 371 C VAL A 46 4322 4141 3976 -750 114 291 C ATOM 372 O VAL A 46 -29.645 -15.494 18.326 1.00 29.10 O ANISOU 372 O VAL A 46 3789 3754 3513 -736 99 256 O ATOM 373 CB VAL A 46 -30.130 -18.788 18.412 1.00 35.44 C ANISOU 373 CB VAL A 46 4737 4315 4414 -906 58 296 C ATOM 374 CG1 VAL A 46 -31.460 -18.071 18.606 1.00 36.72 C ANISOU 374 CG1 VAL A 46 4766 4574 4614 -971 71 292 C ATOM 375 CG2 VAL A 46 -30.267 -19.887 17.373 1.00 31.94 C ANISOU 375 CG2 VAL A 46 4371 3757 4010 -944 -15 245 C ATOM 376 N SER A 47 -28.563 -16.508 20.017 1.00 29.88 N ANISOU 376 N SER A 47 3974 3791 3589 -731 165 350 N ATOM 377 CA ASER A 47 -28.497 -15.276 20.797 1.00 29.47 C ANISOU 377 CA ASER A 47 3854 3842 3500 -689 208 363 C ATOM 378 C SER A 47 -27.737 -14.192 20.042 1.00 31.13 C ANISOU 378 C SER A 47 4052 4089 3686 -598 188 314 C ATOM 379 O SER A 47 -28.120 -13.016 20.070 1.00 28.37 O ANISOU 379 O SER A 47 3630 3819 3329 -577 197 295 O ATOM 380 CB ASER A 47 -27.843 -15.549 22.153 1.00 30.07 C ANISOU 380 CB ASER A 47 3978 3911 3535 -671 246 428 C ATOM 381 OG ASER A 47 -27.786 -14.371 22.942 1.00 32.96 O ANISOU 381 OG ASER A 47 4288 4374 3860 -630 282 430 O ATOM 382 N LEU A 48 -26.665 -14.578 19.349 1.00 29.36 N ANISOU 382 N LEU A 48 3899 3802 3456 -545 168 291 N ATOM 383 CA LEU A 48 -25.906 -13.632 18.538 1.00 27.18 C ANISOU 383 CA LEU A 48 3618 3551 3158 -472 166 249 C ATOM 384 C LEU A 48 -26.719 -13.136 17.348 1.00 28.15 C ANISOU 384 C LEU A 48 3724 3695 3275 -490 132 206 C ATOM 385 O LEU A 48 -26.671 -11.947 17.007 1.00 26.87 O ANISOU 385 O LEU A 48 3529 3587 3095 -452 133 190 O ATOM 386 CB LEU A 48 -24.608 -14.291 18.067 1.00 28.99 C ANISOU 386 CB LEU A 48 3919 3706 3389 -415 168 230 C ATOM 387 CG LEU A 48 -23.618 -13.464 17.249 1.00 34.34 C ANISOU 387 CG LEU A 48 4597 4401 4050 -346 192 191 C ATOM 388 CD1 LEU A 48 -23.167 -12.241 18.018 1.00 28.43 C ANISOU 388 CD1 LEU A 48 3781 3720 3301 -311 216 209 C ATOM 389 CD2 LEU A 48 -22.428 -14.319 16.850 1.00 39.81 C ANISOU 389 CD2 LEU A 48 5347 5019 4761 -294 206 165 C ATOM 390 N ALA A 49 -27.474 -14.028 16.705 1.00 29.82 N ANISOU 390 N ALA A 49 3965 3859 3506 -546 89 185 N ATOM 391 CA ALA A 49 -28.351 -13.607 15.618 1.00 30.55 C ANISOU 391 CA ALA A 49 4046 3971 3593 -563 31 142 C ATOM 392 C ALA A 49 -29.478 -12.708 16.110 1.00 29.09 C ANISOU 392 C ALA A 49 3749 3868 3437 -590 22 152 C ATOM 393 O ALA A 49 -29.895 -11.795 15.390 1.00 27.22 O ANISOU 393 O ALA A 49 3489 3667 3186 -564 -21 125 O ATOM 394 CB ALA A 49 -28.923 -14.832 14.902 1.00 30.68 C ANISOU 394 CB ALA A 49 4115 3911 3631 -623 -27 110 C ATOM 395 N ALA A 50 -29.983 -12.949 17.323 1.00 29.45 N ANISOU 395 N ALA A 50 3729 3940 3521 -638 63 191 N ATOM 396 CA ALA A 50 -31.009 -12.075 17.885 1.00 28.72 C ANISOU 396 CA ALA A 50 3520 3931 3461 -653 74 191 C ATOM 397 C ALA A 50 -30.482 -10.659 18.083 1.00 30.61 C ANISOU 397 C ALA A 50 3736 4229 3664 -571 94 188 C ATOM 398 O ALA A 50 -31.185 -9.681 17.798 1.00 30.22 O ANISOU 398 O ALA A 50 3619 4228 3634 -549 63 162 O ATOM 399 CB ALA A 50 -31.523 -12.648 19.206 1.00 26.47 C ANISOU 399 CB ALA A 50 3187 3664 3205 -721 142 237 C ATOM 400 N ALA A 51 -29.248 -10.528 18.576 1.00 31.30 N ANISOU 400 N ALA A 51 3876 4305 3711 -522 138 211 N ATOM 401 CA ALA A 51 -28.638 -9.208 18.696 1.00 28.92 C ANISOU 401 CA ALA A 51 3559 4043 3387 -451 151 203 C ATOM 402 C ALA A 51 -28.538 -8.522 17.340 1.00 28.13 C ANISOU 402 C ALA A 51 3490 3927 3270 -415 102 173 C ATOM 403 O ALA A 51 -28.768 -7.312 17.227 1.00 29.47 O ANISOU 403 O ALA A 51 3623 4133 3443 -378 87 162 O ATOM 404 CB ALA A 51 -27.257 -9.323 19.339 1.00 28.45 C ANISOU 404 CB ALA A 51 3547 3961 3301 -411 190 225 C ATOM 405 N ASP A 52 -28.190 -9.279 16.298 1.00 27.05 N ANISOU 405 N ASP A 52 3435 3734 3111 -423 78 160 N ATOM 406 CA ASP A 52 -28.032 -8.687 14.975 1.00 23.70 C ANISOU 406 CA ASP A 52 3068 3293 2646 -390 40 138 C ATOM 407 C ASP A 52 -29.379 -8.333 14.356 1.00 25.52 C ANISOU 407 C ASP A 52 3263 3544 2890 -407 -45 115 C ATOM 408 O ASP A 52 -29.477 -7.353 13.608 1.00 27.89 O ANISOU 408 O ASP A 52 3587 3850 3160 -368 -85 109 O ATOM 409 CB ASP A 52 -27.243 -9.635 14.072 1.00 29.07 C ANISOU 409 CB ASP A 52 3854 3908 3285 -388 49 121 C ATOM 410 CG ASP A 52 -25.773 -9.706 14.450 1.00 37.88 C ANISOU 410 CG ASP A 52 4993 5004 4395 -348 126 134 C ATOM 411 OD1 ASP A 52 -25.238 -8.696 14.957 1.00 35.63 O ANISOU 411 OD1 ASP A 52 4668 4752 4119 -316 160 151 O ATOM 412 OD2 ASP A 52 -25.152 -10.771 14.248 1.00 38.04 O ANISOU 412 OD2 ASP A 52 5070 4972 4413 -348 145 121 O ATOM 413 N ILE A 53 -30.419 -9.123 14.635 1.00 27.80 N ANISOU 413 N ILE A 53 3496 3838 3231 -467 -78 103 N ATOM 414 CA ILE A 53 -31.767 -8.750 14.213 1.00 27.84 C ANISOU 414 CA ILE A 53 3430 3870 3277 -483 -166 75 C ATOM 415 C ILE A 53 -32.169 -7.415 14.830 1.00 28.12 C ANISOU 415 C ILE A 53 3371 3967 3344 -438 -156 80 C ATOM 416 O ILE A 53 -32.756 -6.555 14.162 1.00 30.27 O ANISOU 416 O ILE A 53 3628 4250 3621 -400 -235 60 O ATOM 417 CB ILE A 53 -32.773 -9.863 14.569 1.00 29.31 C ANISOU 417 CB ILE A 53 3547 4051 3537 -569 -185 62 C ATOM 418 CG1 ILE A 53 -32.530 -11.108 13.715 1.00 27.44 C ANISOU 418 CG1 ILE A 53 3414 3736 3275 -608 -227 42 C ATOM 419 CG2 ILE A 53 -34.202 -9.376 14.368 1.00 29.88 C ANISOU 419 CG2 ILE A 53 3502 4166 3685 -583 -267 28 C ATOM 420 CD1 ILE A 53 -33.311 -12.325 14.184 1.00 29.17 C ANISOU 420 CD1 ILE A 53 3581 3929 3575 -706 -231 39 C ATOM 421 N LEU A 54 -31.850 -7.215 16.113 1.00 25.95 N ANISOU 421 N LEU A 54 3043 3729 3086 -435 -68 102 N ATOM 422 CA LEU A 54 -32.199 -5.969 16.786 1.00 28.32 C ANISOU 422 CA LEU A 54 3261 4085 3416 -388 -52 95 C ATOM 423 C LEU A 54 -31.348 -4.789 16.335 1.00 28.29 C ANISOU 423 C LEU A 54 3321 4061 3367 -316 -62 102 C ATOM 424 O LEU A 54 -31.784 -3.642 16.482 1.00 30.70 O ANISOU 424 O LEU A 54 3574 4391 3700 -268 -87 87 O ATOM 425 CB LEU A 54 -32.081 -6.132 18.303 1.00 26.98 C ANISOU 425 CB LEU A 54 3035 3958 3258 -406 44 112 C ATOM 426 CG LEU A 54 -33.040 -7.113 18.971 1.00 31.27 C ANISOU 426 CG LEU A 54 3503 4529 3851 -485 80 115 C ATOM 427 CD1 LEU A 54 -32.681 -7.306 20.434 1.00 27.98 C ANISOU 427 CD1 LEU A 54 3078 4145 3407 -499 183 146 C ATOM 428 CD2 LEU A 54 -34.460 -6.595 18.837 1.00 33.02 C ANISOU 428 CD2 LEU A 54 3593 4799 4154 -488 39 73 C ATOM 429 N VAL A 55 -30.148 -5.030 15.803 1.00 27.34 N ANISOU 429 N VAL A 55 3308 3894 3187 -308 -38 123 N ATOM 430 CA VAL A 55 -29.419 -3.953 15.140 1.00 22.70 C ANISOU 430 CA VAL A 55 2785 3277 2561 -256 -46 134 C ATOM 431 C VAL A 55 -30.219 -3.430 13.955 1.00 24.10 C ANISOU 431 C VAL A 55 2996 3438 2724 -234 -146 124 C ATOM 432 O VAL A 55 -30.318 -2.216 13.736 1.00 28.31 O ANISOU 432 O VAL A 55 3534 3964 3259 -186 -179 130 O ATOM 433 CB VAL A 55 -28.018 -4.431 14.715 1.00 25.01 C ANISOU 433 CB VAL A 55 3175 3527 2802 -259 12 153 C ATOM 434 CG1 VAL A 55 -27.380 -3.437 13.751 1.00 19.86 C ANISOU 434 CG1 VAL A 55 2602 2839 2104 -223 10 169 C ATOM 435 CG2 VAL A 55 -27.132 -4.629 15.939 1.00 22.49 C ANISOU 435 CG2 VAL A 55 2818 3220 2505 -259 88 163 C ATOM 436 N GLY A 56 -30.817 -4.337 13.182 1.00 24.69 N ANISOU 436 N GLY A 56 3100 3499 2783 -268 -207 106 N ATOM 437 CA GLY A 56 -31.604 -3.917 12.036 1.00 29.33 C ANISOU 437 CA GLY A 56 3728 4068 3348 -244 -324 93 C ATOM 438 C GLY A 56 -32.912 -3.263 12.437 1.00 30.15 C ANISOU 438 C GLY A 56 3703 4212 3541 -221 -400 67 C ATOM 439 O GLY A 56 -33.314 -2.249 11.858 1.00 33.51 O ANISOU 439 O GLY A 56 4147 4622 3962 -166 -484 67 O ATOM 440 N VAL A 57 -33.596 -3.834 13.428 1.00 31.27 N ANISOU 440 N VAL A 57 3714 4402 3767 -263 -367 44 N ATOM 441 CA VAL A 57 -34.919 -3.346 13.800 1.00 30.39 C ANISOU 441 CA VAL A 57 3457 4336 3755 -245 -426 7 C ATOM 442 C VAL A 57 -34.834 -2.079 14.646 1.00 28.79 C ANISOU 442 C VAL A 57 3194 4160 3584 -181 -381 6 C ATOM 443 O VAL A 57 -35.655 -1.168 14.492 1.00 28.61 O ANISOU 443 O VAL A 57 3105 4147 3620 -122 -459 -21 O ATOM 444 CB VAL A 57 -35.697 -4.463 14.523 1.00 34.06 C ANISOU 444 CB VAL A 57 3803 4841 4298 -326 -389 -16 C ATOM 445 CG1 VAL A 57 -36.942 -3.907 15.201 1.00 36.09 C ANISOU 445 CG1 VAL A 57 3880 5160 4671 -309 -401 -57 C ATOM 446 CG2 VAL A 57 -36.065 -5.572 13.548 1.00 34.65 C ANISOU 446 CG2 VAL A 57 3923 4877 4366 -384 -475 -33 C ATOM 447 N LEU A 58 -33.847 -1.981 15.539 1.00 24.93 N ANISOU 447 N LEU A 58 2729 3679 3063 -184 -267 30 N ATOM 448 CA LEU A 58 -33.803 -0.871 16.486 1.00 26.78 C ANISOU 448 CA LEU A 58 2903 3940 3331 -129 -223 16 C ATOM 449 C LEU A 58 -32.548 -0.017 16.399 1.00 29.48 C ANISOU 449 C LEU A 58 3350 4235 3617 -90 -195 47 C ATOM 450 O LEU A 58 -32.655 1.213 16.320 1.00 29.39 O ANISOU 450 O LEU A 58 3338 4201 3629 -26 -235 37 O ATOM 451 CB LEU A 58 -33.968 -1.395 17.923 1.00 31.27 C ANISOU 451 CB LEU A 58 3380 4573 3927 -166 -114 3 C ATOM 452 CG LEU A 58 -35.346 -1.960 18.268 1.00 32.81 C ANISOU 452 CG LEU A 58 3436 4825 4204 -205 -115 -33 C ATOM 453 CD1 LEU A 58 -35.356 -2.515 19.681 1.00 33.44 C ANISOU 453 CD1 LEU A 58 3460 4963 4283 -251 14 -29 C ATOM 454 CD2 LEU A 58 -36.413 -0.891 18.100 1.00 31.13 C ANISOU 454 CD2 LEU A 58 3118 4634 4077 -134 -188 -84 C ATOM 455 N ALA A 59 -31.354 -0.622 16.413 1.00 25.14 N ANISOU 455 N ALA A 59 2883 3662 3007 -126 -129 81 N ATOM 456 CA ALA A 59 -30.138 0.182 16.524 1.00 26.76 C ANISOU 456 CA ALA A 59 3155 3829 3184 -100 -89 103 C ATOM 457 C ALA A 59 -29.920 1.053 15.292 1.00 31.04 C ANISOU 457 C ALA A 59 3791 4307 3697 -67 -150 128 C ATOM 458 O ALA A 59 -29.451 2.192 15.409 1.00 29.59 O ANISOU 458 O ALA A 59 3629 4087 3526 -31 -146 136 O ATOM 459 CB ALA A 59 -28.928 -0.723 16.761 1.00 23.52 C ANISOU 459 CB ALA A 59 2795 3409 2732 -142 -11 127 C ATOM 460 N ILE A 60 -30.250 0.549 14.107 1.00 27.07 N ANISOU 460 N ILE A 60 3354 3781 3149 -81 -209 142 N ATOM 461 CA ILE A 60 -30.020 1.311 12.882 1.00 25.61 C ANISOU 461 CA ILE A 60 3289 3533 2910 -53 -263 176 C ATOM 462 C ILE A 60 -31.050 2.437 12.798 1.00 24.69 C ANISOU 462 C ILE A 60 3133 3403 2844 11 -367 163 C ATOM 463 O ILE A 60 -30.672 3.577 12.490 1.00 27.71 O ANISOU 463 O ILE A 60 3582 3727 3219 48 -383 193 O ATOM 464 CB ILE A 60 -30.022 0.402 11.640 1.00 30.72 C ANISOU 464 CB ILE A 60 4040 4159 3471 -82 -298 189 C ATOM 465 CG1 ILE A 60 -28.709 -0.386 11.577 1.00 29.93 C ANISOU 465 CG1 ILE A 60 4003 4050 3320 -125 -184 206 C ATOM 466 CG2 ILE A 60 -30.235 1.218 10.375 1.00 26.85 C ANISOU 466 CG2 ILE A 60 3673 3612 2916 -45 -387 222 C ATOM 467 CD1 ILE A 60 -28.629 -1.364 10.430 1.00 31.80 C ANISOU 467 CD1 ILE A 60 4348 4267 3469 -150 -201 204 C ATOM 468 N PRO A 61 -32.348 2.187 13.044 1.00 27.00 N ANISOU 468 N PRO A 61 3316 3741 3202 27 -439 117 N ATOM 469 CA PRO A 61 -33.278 3.322 13.177 1.00 27.11 C ANISOU 469 CA PRO A 61 3265 3746 3291 102 -529 91 C ATOM 470 C PRO A 61 -32.850 4.336 14.226 1.00 26.57 C ANISOU 470 C PRO A 61 3153 3671 3272 139 -465 78 C ATOM 471 O PRO A 61 -33.018 5.544 14.016 1.00 24.87 O ANISOU 471 O PRO A 61 2965 3399 3085 205 -528 82 O ATOM 472 CB PRO A 61 -34.596 2.635 13.556 1.00 28.13 C ANISOU 472 CB PRO A 61 3243 3945 3501 95 -572 33 C ATOM 473 CG PRO A 61 -34.526 1.340 12.853 1.00 29.41 C ANISOU 473 CG PRO A 61 3459 4112 3603 26 -583 45 C ATOM 474 CD PRO A 61 -33.085 0.909 12.993 1.00 29.30 C ANISOU 474 CD PRO A 61 3546 4081 3508 -21 -461 87 C ATOM 475 N PHE A 62 -32.302 3.878 15.356 1.00 26.29 N ANISOU 475 N PHE A 62 3060 3684 3245 101 -350 61 N ATOM 476 CA PHE A 62 -31.827 4.812 16.372 1.00 25.66 C ANISOU 476 CA PHE A 62 2951 3596 3202 134 -298 39 C ATOM 477 C PHE A 62 -30.645 5.629 15.866 1.00 29.75 C ANISOU 477 C PHE A 62 3592 4027 3684 135 -288 89 C ATOM 478 O PHE A 62 -30.562 6.835 16.127 1.00 28.80 O ANISOU 478 O PHE A 62 3480 3857 3608 184 -312 77 O ATOM 479 CB PHE A 62 -31.432 4.061 17.646 1.00 24.01 C ANISOU 479 CB PHE A 62 2678 3457 2989 92 -189 15 C ATOM 480 CG PHE A 62 -32.595 3.486 18.413 1.00 24.77 C ANISOU 480 CG PHE A 62 2643 3636 3130 89 -171 -34 C ATOM 481 CD1 PHE A 62 -33.900 3.696 18.001 1.00 29.15 C ANISOU 481 CD1 PHE A 62 3120 4208 3750 127 -250 -67 C ATOM 482 CD2 PHE A 62 -32.373 2.728 19.552 1.00 22.62 C ANISOU 482 CD2 PHE A 62 2329 3427 2840 47 -74 -46 C ATOM 483 CE1 PHE A 62 -34.962 3.162 18.711 1.00 33.59 C ANISOU 483 CE1 PHE A 62 3544 4851 4368 114 -216 -114 C ATOM 484 CE2 PHE A 62 -33.429 2.190 20.265 1.00 27.45 C ANISOU 484 CE2 PHE A 62 2826 4115 3487 32 -36 -83 C ATOM 485 CZ PHE A 62 -34.725 2.408 19.844 1.00 31.84 C ANISOU 485 CZ PHE A 62 3287 4692 4120 62 -99 -119 C ATOM 486 N ALA A 63 -29.721 4.991 15.139 1.00 24.43 N ANISOU 486 N ALA A 63 3015 3331 2938 79 -247 141 N ATOM 487 CA ALA A 63 -28.563 5.707 14.610 1.00 22.78 C ANISOU 487 CA ALA A 63 2913 3042 2700 65 -215 191 C ATOM 488 C ALA A 63 -28.977 6.755 13.585 1.00 28.07 C ANISOU 488 C ALA A 63 3675 3630 3360 109 -308 229 C ATOM 489 O ALA A 63 -28.439 7.869 13.575 1.00 29.51 O ANISOU 489 O ALA A 63 3908 3737 3567 123 -305 253 O ATOM 490 CB ALA A 63 -27.569 4.721 13.996 1.00 24.94 C ANISOU 490 CB ALA A 63 3258 3317 2901 1 -140 230 C ATOM 491 N ILE A 64 -29.920 6.409 12.708 1.00 29.20 N ANISOU 491 N ILE A 64 3847 3780 3468 130 -399 236 N ATOM 492 CA ILE A 64 -30.466 7.381 11.763 1.00 27.02 C ANISOU 492 CA ILE A 64 3663 3425 3178 185 -514 272 C ATOM 493 C ILE A 64 -31.080 8.560 12.510 1.00 30.91 C ANISOU 493 C ILE A 64 4078 3889 3776 261 -574 231 C ATOM 494 O ILE A 64 -30.854 9.726 12.164 1.00 29.19 O ANISOU 494 O ILE A 64 3948 3573 3570 295 -615 270 O ATOM 495 CB ILE A 64 -31.486 6.704 10.829 1.00 26.56 C ANISOU 495 CB ILE A 64 3629 3391 3074 201 -626 269 C ATOM 496 CG1 ILE A 64 -30.780 5.707 9.909 1.00 27.23 C ANISOU 496 CG1 ILE A 64 3831 3480 3036 134 -573 310 C ATOM 497 CG2 ILE A 64 -32.244 7.745 10.013 1.00 25.05 C ANISOU 497 CG2 ILE A 64 3514 3122 2883 279 -777 296 C ATOM 498 CD1 ILE A 64 -31.725 4.803 9.145 1.00 27.76 C ANISOU 498 CD1 ILE A 64 3908 3579 3059 137 -677 287 C ATOM 499 N THR A 65 -31.877 8.267 13.540 1.00 28.12 N ANISOU 499 N THR A 65 3566 3616 3503 289 -573 152 N ATOM 500 CA THR A 65 -32.546 9.317 14.304 1.00 30.93 C ANISOU 500 CA THR A 65 3835 3954 3962 372 -621 95 C ATOM 501 C THR A 65 -31.542 10.273 14.939 1.00 31.77 C ANISOU 501 C THR A 65 3981 3996 4093 370 -558 98 C ATOM 502 O THR A 65 -31.668 11.498 14.817 1.00 32.53 O ANISOU 502 O THR A 65 4121 3999 4238 431 -625 101 O ATOM 503 CB THR A 65 -33.434 8.685 15.378 1.00 31.59 C ANISOU 503 CB THR A 65 3741 4151 4111 385 -588 8 C ATOM 504 OG1 THR A 65 -34.359 7.781 14.761 1.00 33.47 O ANISOU 504 OG1 THR A 65 3933 4441 4344 374 -651 3 O ATOM 505 CG2 THR A 65 -34.206 9.749 16.125 1.00 30.90 C ANISOU 505 CG2 THR A 65 3559 4053 4130 481 -630 -65 C ATOM 506 N AILE A 66 -30.532 9.729 15.624 0.50 35.15 N ANISOU 506 N AILE A 66 4394 4464 4495 301 -440 95 N ATOM 507 N BILE A 66 -30.535 9.728 15.623 0.50 35.14 N ANISOU 507 N BILE A 66 4394 4464 4494 301 -440 95 N ATOM 508 CA AILE A 66 -29.566 10.566 16.334 0.50 38.40 C ANISOU 508 CA AILE A 66 4825 4822 4943 293 -389 84 C ATOM 509 CA BILE A 66 -29.569 10.562 16.327 0.50 38.39 C ANISOU 509 CA BILE A 66 4825 4821 4942 293 -389 85 C ATOM 510 C AILE A 66 -28.550 11.207 15.399 0.50 39.06 C ANISOU 510 C AILE A 66 5051 4792 4998 252 -383 169 C ATOM 511 C BILE A 66 -28.641 11.289 15.364 0.50 39.16 C ANISOU 511 C BILE A 66 5065 4799 5013 259 -393 168 C ATOM 512 O AILE A 66 -27.791 12.085 15.829 0.50 41.04 O ANISOU 512 O AILE A 66 5325 4973 5298 242 -360 164 O ATOM 513 O BILE A 66 -28.049 12.313 15.728 0.50 41.51 O ANISOU 513 O BILE A 66 5391 5016 5366 263 -388 164 O ATOM 514 CB AILE A 66 -28.895 9.727 17.441 0.50 41.07 C ANISOU 514 CB AILE A 66 5091 5246 5267 241 -283 46 C ATOM 515 CB BILE A 66 -28.807 9.685 17.336 0.50 40.93 C ANISOU 515 CB BILE A 66 5084 5225 5244 234 -281 55 C ATOM 516 CG1AILE A 66 -28.141 10.617 18.434 0.50 44.08 C ANISOU 516 CG1AILE A 66 5462 5585 5701 249 -256 4 C ATOM 517 CG1BILE A 66 -29.804 9.109 18.339 0.50 42.87 C ANISOU 517 CG1BILE A 66 5201 5578 5510 266 -269 -21 C ATOM 518 CG2AILE A 66 -27.978 8.677 16.845 0.50 39.65 C ANISOU 518 CG2AILE A 66 4966 5086 5015 157 -216 107 C ATOM 519 CG2BILE A 66 -27.728 10.469 18.067 0.50 43.56 C ANISOU 519 CG2BILE A 66 5432 5503 5616 219 -241 37 C ATOM 520 CD1AILE A 66 -27.634 9.883 19.650 0.50 43.73 C ANISOU 520 CD1AILE A 66 5349 5626 5639 218 -180 -44 C ATOM 521 CD1BILE A 66 -29.214 8.113 19.258 0.50 47.56 C ANISOU 521 CD1BILE A 66 5752 6251 6067 212 -176 -38 C ATOM 522 N SER A 67 -28.526 10.813 14.123 1.00 34.30 N ANISOU 522 N SER A 67 4549 4167 4316 224 -401 243 N ATOM 523 CA SER A 67 -27.712 11.526 13.146 1.00 37.09 C ANISOU 523 CA SER A 67 5052 4408 4633 188 -391 331 C ATOM 524 C SER A 67 -28.304 12.885 12.796 1.00 40.77 C ANISOU 524 C SER A 67 5587 4758 5144 260 -504 352 C ATOM 525 O SER A 67 -27.590 13.739 12.261 1.00 41.27 O ANISOU 525 O SER A 67 5769 4708 5203 230 -490 422 O ATOM 526 CB SER A 67 -27.550 10.689 11.876 1.00 32.43 C ANISOU 526 CB SER A 67 4568 3832 3923 144 -373 401 C ATOM 527 OG SER A 67 -28.718 10.739 11.074 1.00 33.80 O ANISOU 527 OG SER A 67 4791 3994 4059 206 -502 415 O ATOM 528 N THR A 68 -29.589 13.104 13.083 1.00 38.00 N ANISOU 528 N THR A 68 5162 4431 4846 354 -613 293 N ATOM 529 CA THR A 68 -30.246 14.363 12.756 1.00 38.97 C ANISOU 529 CA THR A 68 5343 4439 5024 441 -738 305 C ATOM 530 C THR A 68 -30.030 15.439 13.812 1.00 38.61 C ANISOU 530 C THR A 68 5247 4331 5091 478 -732 244 C ATOM 531 O THR A 68 -30.293 16.614 13.536 1.00 41.22 O ANISOU 531 O THR A 68 5653 4534 5474 539 -824 263 O ATOM 532 CB THR A 68 -31.749 14.143 12.564 1.00 39.36 C ANISOU 532 CB THR A 68 5319 4538 5099 536 -868 258 C ATOM 533 OG1 THR A 68 -32.361 13.872 13.830 1.00 36.83 O ANISOU 533 OG1 THR A 68 4811 4317 4865 576 -840 143 O ATOM 534 CG2 THR A 68 -32.005 12.973 11.625 1.00 34.45 C ANISOU 534 CG2 THR A 68 4733 3985 4370 496 -883 298 C ATOM 535 N GLY A 69 -29.567 15.074 15.005 1.00 36.93 N ANISOU 535 N GLY A 69 4922 4196 4913 446 -637 169 N ATOM 536 CA GLY A 69 -29.418 16.049 16.066 1.00 35.62 C ANISOU 536 CA GLY A 69 4711 3978 4845 487 -640 93 C ATOM 537 C GLY A 69 -30.717 16.616 16.589 1.00 39.21 C ANISOU 537 C GLY A 69 5080 4438 5382 615 -734 1 C ATOM 538 O GLY A 69 -30.720 17.719 17.139 1.00 38.28 O ANISOU 538 O GLY A 69 4967 4229 5348 672 -772 -51 O ATOM 539 N PHE A 70 -31.822 15.888 16.438 1.00 36.14 N ANISOU 539 N PHE A 70 4603 4149 4981 661 -770 -27 N ATOM 540 CA PHE A 70 -33.136 16.405 16.794 1.00 39.66 C ANISOU 540 CA PHE A 70 4949 4601 5518 789 -860 -115 C ATOM 541 C PHE A 70 -33.226 16.710 18.289 1.00 37.69 C ANISOU 541 C PHE A 70 4585 4401 5333 831 -795 -240 C ATOM 542 O PHE A 70 -32.504 16.149 19.117 1.00 39.18 O ANISOU 542 O PHE A 70 4742 4665 5479 760 -682 -265 O ATOM 543 CB PHE A 70 -34.226 15.402 16.420 1.00 39.25 C ANISOU 543 CB PHE A 70 4799 4664 5451 808 -895 -127 C ATOM 544 CG PHE A 70 -34.328 14.243 17.369 1.00 41.02 C ANISOU 544 CG PHE A 70 4885 5049 5652 756 -773 -188 C ATOM 545 CD1 PHE A 70 -33.301 13.320 17.475 1.00 38.50 C ANISOU 545 CD1 PHE A 70 4605 4781 5240 640 -663 -140 C ATOM 546 CD2 PHE A 70 -35.445 14.088 18.170 1.00 44.31 C ANISOU 546 CD2 PHE A 70 5135 5559 6142 825 -763 -293 C ATOM 547 CE1 PHE A 70 -33.391 12.262 18.358 1.00 39.20 C ANISOU 547 CE1 PHE A 70 4586 5004 5304 595 -560 -187 C ATOM 548 CE2 PHE A 70 -35.540 13.032 19.055 1.00 40.04 C ANISOU 548 CE2 PHE A 70 4484 5158 5572 769 -642 -338 C ATOM 549 CZ PHE A 70 -34.513 12.116 19.147 1.00 39.90 C ANISOU 549 CZ PHE A 70 4524 5182 5455 655 -547 -280 C ATOM 550 N CYS A 71 -34.132 17.625 18.623 1.00 40.44 N ANISOU 550 N CYS A 71 4878 4703 5783 956 -873 -323 N ATOM 551 CA CYS A 71 -34.338 18.026 20.008 1.00 42.95 C ANISOU 551 CA CYS A 71 5098 5062 6158 1016 -816 -456 C ATOM 552 C CYS A 71 -34.982 16.896 20.803 1.00 40.43 C ANISOU 552 C CYS A 71 4620 4930 5810 1003 -714 -525 C ATOM 553 O CYS A 71 -35.977 16.307 20.370 1.00 36.70 O ANISOU 553 O CYS A 71 4056 4530 5357 1029 -744 -525 O ATOM 554 CB CYS A 71 -35.220 19.267 20.073 1.00 46.66 C ANISOU 554 CB CYS A 71 5545 5432 6750 1165 -926 -534 C ATOM 555 SG CYS A 71 -34.511 20.775 19.400 1.00 52.19 S ANISOU 555 SG CYS A 71 6438 5889 7504 1189 -1043 -468 S ATOM 556 N ALA A 72 -34.415 16.590 21.966 1.00 33.63 N ANISOU 556 N ALA A 72 3733 4143 4903 960 -598 -582 N ATOM 557 CA ALA A 72 -34.895 15.481 22.775 1.00 32.86 C ANISOU 557 CA ALA A 72 3511 4214 4759 931 -485 -631 C ATOM 558 C ALA A 72 -34.546 15.744 24.231 1.00 38.61 C ANISOU 558 C ALA A 72 4222 4986 5462 948 -394 -733 C ATOM 559 O ALA A 72 -33.531 16.377 24.533 1.00 40.00 O ANISOU 559 O ALA A 72 4497 5077 5624 929 -406 -737 O ATOM 560 CB ALA A 72 -34.297 14.145 22.319 1.00 35.64 C ANISOU 560 CB ALA A 72 3893 4636 5012 802 -429 -528 C ATOM 561 N ALA A 73 -35.404 15.264 25.131 1.00 38.08 N ANISOU 561 N ALA A 73 4030 5050 5387 981 -303 -819 N ATOM 562 CA ALA A 73 -35.016 15.158 26.530 1.00 38.39 C ANISOU 562 CA ALA A 73 4071 5162 5353 972 -195 -899 C ATOM 563 C ALA A 73 -33.733 14.346 26.626 1.00 33.11 C ANISOU 563 C ALA A 73 3496 4510 4575 847 -155 -813 C ATOM 564 O ALA A 73 -33.608 13.292 25.995 1.00 33.20 O ANISOU 564 O ALA A 73 3504 4566 4546 762 -138 -717 O ATOM 565 CB ALA A 73 -36.131 14.504 27.347 1.00 39.76 C ANISOU 565 CB ALA A 73 4103 5490 5513 999 -78 -975 C ATOM 566 N CYS A 74 -32.775 14.845 27.412 1.00 36.83 N ANISOU 566 N CYS A 74 4048 4939 5006 841 -150 -856 N ATOM 567 CA CYS A 74 -31.422 14.301 27.343 1.00 39.01 C ANISOU 567 CA CYS A 74 4412 5197 5212 734 -146 -776 C ATOM 568 C CYS A 74 -31.382 12.824 27.710 1.00 35.22 C ANISOU 568 C CYS A 74 3903 4851 4630 656 -51 -728 C ATOM 569 O CYS A 74 -30.638 12.048 27.098 1.00 35.06 O ANISOU 569 O CYS A 74 3922 4824 4577 568 -55 -628 O ATOM 570 CB CYS A 74 -30.477 15.090 28.249 1.00 44.38 C ANISOU 570 CB CYS A 74 5169 5817 5879 746 -169 -849 C ATOM 571 SG CYS A 74 -28.750 14.597 28.034 1.00 47.09 S ANISOU 571 SG CYS A 74 5598 6115 6180 623 -188 -757 S ATOM 572 N HIS A 75 -32.173 12.409 28.701 1.00 34.41 N ANISOU 572 N HIS A 75 3735 4865 4476 686 40 -796 N ATOM 573 CA HIS A 75 -32.125 11.010 29.109 1.00 37.55 C ANISOU 573 CA HIS A 75 4119 5375 4772 606 132 -743 C ATOM 574 C HIS A 75 -32.827 10.100 28.109 1.00 39.07 C ANISOU 574 C HIS A 75 4241 5604 4999 558 142 -661 C ATOM 575 O HIS A 75 -32.447 8.931 27.969 1.00 34.78 O ANISOU 575 O HIS A 75 3719 5103 4395 471 178 -581 O ATOM 576 CB HIS A 75 -32.728 10.860 30.504 1.00 39.04 C ANISOU 576 CB HIS A 75 4276 5674 4882 643 241 -834 C ATOM 577 CG HIS A 75 -31.890 11.474 31.581 1.00 44.93 C ANISOU 577 CG HIS A 75 5117 6398 5558 673 229 -909 C ATOM 578 ND1 HIS A 75 -30.852 10.803 32.190 1.00 44.31 N ANISOU 578 ND1 HIS A 75 5126 6342 5369 609 237 -870 N ATOM 579 CD2 HIS A 75 -31.922 12.706 32.142 1.00 45.55 C ANISOU 579 CD2 HIS A 75 5218 6425 5662 763 195 -1026 C ATOM 580 CE1 HIS A 75 -30.288 11.590 33.088 1.00 45.72 C ANISOU 580 CE1 HIS A 75 5376 6490 5506 656 203 -961 C ATOM 581 NE2 HIS A 75 -30.919 12.751 33.079 1.00 47.02 N ANISOU 581 NE2 HIS A 75 5507 6609 5751 747 181 -1059 N ATOM 582 N GLY A 76 -33.843 10.605 27.409 1.00 37.33 N ANISOU 582 N GLY A 76 3942 5363 4880 618 98 -684 N ATOM 583 CA GLY A 76 -34.382 9.861 26.283 1.00 36.34 C ANISOU 583 CA GLY A 76 3766 5247 4794 573 69 -607 C ATOM 584 C GLY A 76 -33.378 9.731 25.156 1.00 33.86 C ANISOU 584 C GLY A 76 3555 4840 4469 515 -11 -505 C ATOM 585 O GLY A 76 -33.253 8.669 24.539 1.00 35.74 O ANISOU 585 O GLY A 76 3801 5103 4675 438 -2 -427 O ATOM 586 N CYS A 77 -32.664 10.820 24.863 1.00 31.72 N ANISOU 586 N CYS A 77 3365 4457 4230 550 -85 -508 N ATOM 587 CA CYS A 77 -31.585 10.771 23.885 1.00 35.60 C ANISOU 587 CA CYS A 77 3958 4861 4707 488 -135 -414 C ATOM 588 C CYS A 77 -30.535 9.742 24.286 1.00 34.10 C ANISOU 588 C CYS A 77 3810 4715 4431 398 -69 -368 C ATOM 589 O CYS A 77 -29.958 9.061 23.428 1.00 28.75 O ANISOU 589 O CYS A 77 3178 4018 3728 332 -75 -285 O ATOM 590 CB CYS A 77 -30.959 12.155 23.742 1.00 37.43 C ANISOU 590 CB CYS A 77 4265 4965 4993 530 -205 -432 C ATOM 591 SG CYS A 77 -29.561 12.225 22.619 1.00 42.23 S ANISOU 591 SG CYS A 77 4993 5462 5589 446 -239 -320 S ATOM 592 N ALEU A 78 -30.265 9.633 25.591 1.00 35.07 N ANISOU 592 N ALEU A 78 3925 4894 4505 402 -11 -426 N ATOM 593 CA ALEU A 78 -29.285 8.670 26.080 1.00 32.73 C ANISOU 593 CA ALEU A 78 3670 4637 4130 331 35 -387 C ATOM 594 C ALEU A 78 -29.661 7.248 25.693 1.00 29.23 C ANISOU 594 C ALEU A 78 3199 4262 3644 269 82 -321 C ATOM 595 O ALEU A 78 -28.797 6.458 25.292 1.00 30.21 O ANISOU 595 O ALEU A 78 3369 4372 3736 206 86 -254 O ATOM 596 CB ALEU A 78 -29.157 8.780 27.598 1.00 32.49 C ANISOU 596 CB ALEU A 78 3644 4663 4038 358 79 -465 C ATOM 597 CG ALEU A 78 -27.936 9.478 28.190 1.00 34.08 C ANISOU 597 CG ALEU A 78 3914 4803 4234 363 34 -502 C ATOM 598 CD1ALEU A 78 -27.997 9.387 29.706 1.00 32.17 C ANISOU 598 CD1ALEU A 78 3687 4636 3901 393 78 -580 C ATOM 599 CD2ALEU A 78 -26.649 8.869 27.653 1.00 31.08 C ANISOU 599 CD2ALEU A 78 3578 4381 3849 288 13 -422 C ATOM 600 N PHE A 79 -30.945 6.901 25.809 1.00 30.89 N ANISOU 600 N PHE A 79 3328 4544 3866 285 119 -344 N ATOM 601 CA PHE A 79 -31.356 5.524 25.562 1.00 30.18 C ANISOU 601 CA PHE A 79 3208 4515 3744 217 165 -288 C ATOM 602 C PHE A 79 -31.160 5.140 24.101 1.00 27.33 C ANISOU 602 C PHE A 79 2877 4097 3410 178 104 -216 C ATOM 603 O PHE A 79 -30.632 4.063 23.800 1.00 32.03 O ANISOU 603 O PHE A 79 3511 4696 3962 112 124 -156 O ATOM 604 CB PHE A 79 -32.811 5.310 25.979 1.00 31.65 C ANISOU 604 CB PHE A 79 3282 4787 3958 235 221 -335 C ATOM 605 CG PHE A 79 -33.292 3.906 25.757 1.00 36.31 C ANISOU 605 CG PHE A 79 3836 5431 4531 154 268 -280 C ATOM 606 CD1 PHE A 79 -32.939 2.893 26.632 1.00 36.48 C ANISOU 606 CD1 PHE A 79 3892 5502 4466 93 351 -249 C ATOM 607 CD2 PHE A 79 -34.072 3.591 24.656 1.00 35.30 C ANISOU 607 CD2 PHE A 79 3649 5291 4471 137 216 -259 C ATOM 608 CE1 PHE A 79 -33.368 1.597 26.424 1.00 38.85 C ANISOU 608 CE1 PHE A 79 4169 5835 4759 12 391 -196 C ATOM 609 CE2 PHE A 79 -34.503 2.297 24.441 1.00 37.32 C ANISOU 609 CE2 PHE A 79 3874 5586 4722 55 250 -215 C ATOM 610 CZ PHE A 79 -34.151 1.298 25.326 1.00 38.78 C ANISOU 610 CZ PHE A 79 4092 5813 4829 -10 342 -182 C ATOM 611 N AILE A 80 -31.584 6.005 23.174 1.00 29.77 N ANISOU 611 N AILE A 80 3180 4348 3785 225 27 -222 N ATOM 612 CA AILE A 80 -31.398 5.689 21.763 1.00 29.79 C ANISOU 612 CA AILE A 80 3234 4295 3790 192 -32 -154 C ATOM 613 C AILE A 80 -29.929 5.742 21.373 1.00 25.99 C ANISOU 613 C AILE A 80 2858 3746 3271 155 -32 -102 C ATOM 614 O AILE A 80 -29.530 5.103 20.394 1.00 31.84 O ANISOU 614 O AILE A 80 3653 4461 3984 110 -42 -43 O ATOM 615 CB AILE A 80 -32.223 6.618 20.853 1.00 34.28 C ANISOU 615 CB AILE A 80 3788 4812 4426 257 -128 -166 C ATOM 616 CG1AILE A 80 -31.821 8.080 21.039 1.00 40.34 C ANISOU 616 CG1AILE A 80 4597 5500 5232 322 -167 -196 C ATOM 617 CG2AILE A 80 -33.695 6.448 21.120 1.00 35.47 C ANISOU 617 CG2AILE A 80 3809 5033 4634 291 -133 -221 C ATOM 618 CD1AILE A 80 -32.525 9.020 20.082 1.00 45.96 C ANISOU 618 CD1AILE A 80 5319 6138 6006 390 -276 -194 C ATOM 619 N ALA A 81 -29.106 6.483 22.118 1.00 23.07 N ANISOU 619 N ALA A 81 2514 3347 2906 174 -19 -130 N ATOM 620 CA ALA A 81 -27.674 6.475 21.846 1.00 25.86 C ANISOU 620 CA ALA A 81 2940 3643 3243 131 -10 -88 C ATOM 621 C ALA A 81 -27.033 5.191 22.347 1.00 26.95 C ANISOU 621 C ALA A 81 3079 3834 3326 77 47 -66 C ATOM 622 O ALA A 81 -26.140 4.638 21.695 1.00 30.27 O ANISOU 622 O ALA A 81 3544 4225 3732 33 61 -16 O ATOM 623 CB ALA A 81 -27.006 7.691 22.486 1.00 21.58 C ANISOU 623 CB ALA A 81 2415 3044 2740 163 -30 -133 C ATOM 624 N CYS A 82 -27.480 4.698 23.503 1.00 26.91 N ANISOU 624 N CYS A 82 3031 3906 3288 84 85 -102 N ATOM 625 CA CYS A 82 -26.782 3.632 24.204 1.00 27.27 C ANISOU 625 CA CYS A 82 3094 3988 3278 44 127 -83 C ATOM 626 C CYS A 82 -27.320 2.240 23.910 1.00 26.72 C ANISOU 626 C CYS A 82 3016 3962 3175 -3 160 -39 C ATOM 627 O CYS A 82 -26.640 1.263 24.238 1.00 24.41 O ANISOU 627 O CYS A 82 2754 3677 2843 -38 184 -8 O ATOM 628 CB CYS A 82 -26.824 3.875 25.718 1.00 26.78 C ANISOU 628 CB CYS A 82 3022 3976 3177 74 149 -140 C ATOM 629 SG CYS A 82 -25.854 5.297 26.257 1.00 31.10 S ANISOU 629 SG CYS A 82 3596 4462 3759 117 97 -200 S ATOM 630 N PHE A 83 -28.521 2.115 23.332 1.00 25.64 N ANISOU 630 N PHE A 83 2834 3847 3061 -5 154 -39 N ATOM 631 CA PHE A 83 -29.092 0.782 23.149 1.00 27.33 C ANISOU 631 CA PHE A 83 3034 4098 3255 -59 183 -6 C ATOM 632 C PHE A 83 -28.179 -0.104 22.311 1.00 26.10 C ANISOU 632 C PHE A 83 2944 3893 3078 -101 174 47 C ATOM 633 O PHE A 83 -28.083 -1.314 22.551 1.00 29.41 O ANISOU 633 O PHE A 83 3380 4326 3467 -146 204 76 O ATOM 634 CB PHE A 83 -30.477 0.856 22.509 1.00 29.67 C ANISOU 634 CB PHE A 83 3261 4415 3599 -55 157 -22 C ATOM 635 CG PHE A 83 -31.143 -0.484 22.393 1.00 34.65 C ANISOU 635 CG PHE A 83 3863 5078 4225 -121 183 4 C ATOM 636 CD1 PHE A 83 -31.537 -1.171 23.529 1.00 36.81 C ANISOU 636 CD1 PHE A 83 4101 5412 4472 -156 261 3 C ATOM 637 CD2 PHE A 83 -31.331 -1.079 21.154 1.00 31.94 C ANISOU 637 CD2 PHE A 83 3542 4699 3895 -153 131 31 C ATOM 638 CE1 PHE A 83 -32.136 -2.417 23.436 1.00 33.12 C ANISOU 638 CE1 PHE A 83 3611 4962 4010 -229 288 33 C ATOM 639 CE2 PHE A 83 -31.928 -2.328 21.052 1.00 34.08 C ANISOU 639 CE2 PHE A 83 3790 4988 4173 -221 147 49 C ATOM 640 CZ PHE A 83 -32.332 -2.997 22.196 1.00 34.21 C ANISOU 640 CZ PHE A 83 3761 5057 4179 -262 227 52 C ATOM 641 N VAL A 84 -27.512 0.476 21.312 1.00 27.59 N ANISOU 641 N VAL A 84 3179 4021 3284 -88 138 61 N ATOM 642 CA VAL A 84 -26.619 -0.310 20.466 1.00 24.36 C ANISOU 642 CA VAL A 84 2832 3569 2855 -121 145 101 C ATOM 643 C VAL A 84 -25.468 -0.874 21.291 1.00 25.25 C ANISOU 643 C VAL A 84 2963 3681 2951 -130 179 109 C ATOM 644 O VAL A 84 -24.917 -1.933 20.965 1.00 27.29 O ANISOU 644 O VAL A 84 3255 3920 3194 -157 195 135 O ATOM 645 CB VAL A 84 -26.132 0.535 19.272 1.00 24.08 C ANISOU 645 CB VAL A 84 2847 3472 2832 -107 119 116 C ATOM 646 CG1 VAL A 84 -25.293 1.698 19.750 1.00 22.92 C ANISOU 646 CG1 VAL A 84 2698 3294 2716 -80 121 100 C ATOM 647 CG2 VAL A 84 -25.363 -0.330 18.277 1.00 25.87 C ANISOU 647 CG2 VAL A 84 3139 3662 3029 -139 141 149 C ATOM 648 N LEU A 85 -25.095 -0.188 22.378 1.00 25.04 N ANISOU 648 N LEU A 85 2916 3670 2930 -102 179 80 N ATOM 649 CA LEU A 85 -24.043 -0.700 23.251 1.00 26.13 C ANISOU 649 CA LEU A 85 3070 3807 3051 -103 188 83 C ATOM 650 C LEU A 85 -24.477 -1.982 23.946 1.00 25.02 C ANISOU 650 C LEU A 85 2941 3705 2861 -128 212 107 C ATOM 651 O LEU A 85 -23.641 -2.847 24.229 1.00 27.65 O ANISOU 651 O LEU A 85 3306 4019 3180 -136 211 130 O ATOM 652 CB LEU A 85 -23.681 0.347 24.308 1.00 25.21 C ANISOU 652 CB LEU A 85 2937 3700 2941 -66 168 38 C ATOM 653 CG LEU A 85 -23.274 1.767 23.903 1.00 32.01 C ANISOU 653 CG LEU A 85 3788 4513 3860 -43 140 10 C ATOM 654 CD1 LEU A 85 -23.028 2.606 25.143 1.00 30.35 C ANISOU 654 CD1 LEU A 85 3568 4315 3649 -8 112 -47 C ATOM 655 CD2 LEU A 85 -22.021 1.739 23.061 1.00 37.90 C ANISOU 655 CD2 LEU A 85 4548 5199 4653 -64 143 34 C ATOM 656 N VAL A 86 -25.774 -2.116 24.230 1.00 24.53 N ANISOU 656 N VAL A 86 2850 3691 2779 -143 234 103 N ATOM 657 CA VAL A 86 -26.304 -3.361 24.781 1.00 22.75 C ANISOU 657 CA VAL A 86 2637 3493 2513 -185 269 135 C ATOM 658 C VAL A 86 -26.131 -4.498 23.782 1.00 27.26 C ANISOU 658 C VAL A 86 3241 4018 3100 -225 261 173 C ATOM 659 O VAL A 86 -25.691 -5.599 24.133 1.00 26.94 O ANISOU 659 O VAL A 86 3246 3955 3035 -247 269 208 O ATOM 660 CB VAL A 86 -27.778 -3.184 25.185 1.00 23.08 C ANISOU 660 CB VAL A 86 2618 3598 2552 -200 308 117 C ATOM 661 CG1 VAL A 86 -28.335 -4.485 25.745 1.00 24.48 C ANISOU 661 CG1 VAL A 86 2810 3797 2694 -261 358 159 C ATOM 662 CG2 VAL A 86 -27.920 -2.053 26.193 1.00 20.72 C ANISOU 662 CG2 VAL A 86 2295 3343 2233 -150 321 66 C ATOM 663 N LEU A 87 -26.479 -4.243 22.519 1.00 23.81 N ANISOU 663 N LEU A 87 2792 3558 2698 -230 239 165 N ATOM 664 CA LEU A 87 -26.406 -5.284 21.499 1.00 25.44 C ANISOU 664 CA LEU A 87 3038 3719 2909 -264 229 187 C ATOM 665 C LEU A 87 -24.965 -5.685 21.211 1.00 28.60 C ANISOU 665 C LEU A 87 3492 4066 3307 -246 230 198 C ATOM 666 O LEU A 87 -24.671 -6.874 21.038 1.00 30.76 O ANISOU 666 O LEU A 87 3808 4304 3576 -267 234 218 O ATOM 667 CB LEU A 87 -27.095 -4.806 20.223 1.00 23.00 C ANISOU 667 CB LEU A 87 2719 3400 2621 -265 193 171 C ATOM 668 CG LEU A 87 -28.568 -4.419 20.383 1.00 24.57 C ANISOU 668 CG LEU A 87 2843 3648 2846 -275 179 150 C ATOM 669 CD1 LEU A 87 -29.175 -4.041 19.041 1.00 24.94 C ANISOU 669 CD1 LEU A 87 2892 3673 2910 -268 117 136 C ATOM 670 CD2 LEU A 87 -29.355 -5.547 21.042 1.00 20.57 C ANISOU 670 CD2 LEU A 87 2306 3168 2343 -335 211 165 C ATOM 671 N ALA A 88 -24.054 -4.711 21.143 1.00 25.26 N ANISOU 671 N ALA A 88 3063 3632 2901 -206 227 182 N ATOM 672 CA ALA A 88 -22.648 -5.046 20.948 1.00 24.64 C ANISOU 672 CA ALA A 88 3010 3511 2842 -188 235 185 C ATOM 673 C ALA A 88 -22.124 -5.867 22.117 1.00 25.77 C ANISOU 673 C ALA A 88 3163 3654 2975 -179 227 199 C ATOM 674 O ALA A 88 -21.352 -6.815 21.927 1.00 25.25 O ANISOU 674 O ALA A 88 3126 3545 2923 -172 226 209 O ATOM 675 CB ALA A 88 -21.824 -3.773 20.764 1.00 20.28 C ANISOU 675 CB ALA A 88 2433 2947 2326 -160 237 165 C ATOM 676 N GLN A 89 -22.528 -5.512 23.339 1.00 24.41 N ANISOU 676 N GLN A 89 2976 3526 2774 -173 217 198 N ATOM 677 CA GLN A 89 -22.037 -6.227 24.510 1.00 22.89 C ANISOU 677 CA GLN A 89 2815 3332 2550 -161 199 218 C ATOM 678 C GLN A 89 -22.569 -7.654 24.530 1.00 28.45 C ANISOU 678 C GLN A 89 3568 4015 3228 -201 213 262 C ATOM 679 O GLN A 89 -21.835 -8.593 24.860 1.00 31.03 O ANISOU 679 O GLN A 89 3941 4297 3553 -187 189 286 O ATOM 680 CB GLN A 89 -22.424 -5.485 25.788 1.00 20.22 C ANISOU 680 CB GLN A 89 2469 3050 2165 -147 194 203 C ATOM 681 CG GLN A 89 -21.583 -5.889 26.982 1.00 24.63 C ANISOU 681 CG GLN A 89 3072 3603 2685 -116 152 214 C ATOM 682 CD GLN A 89 -20.101 -5.676 26.725 1.00 29.29 C ANISOU 682 CD GLN A 89 3639 4147 3343 -74 101 190 C ATOM 683 OE1 GLN A 89 -19.691 -4.621 26.239 1.00 31.99 O ANISOU 683 OE1 GLN A 89 3928 4485 3742 -61 97 149 O ATOM 684 NE2 GLN A 89 -19.292 -6.685 27.037 1.00 29.70 N ANISOU 684 NE2 GLN A 89 3727 4158 3399 -52 61 214 N ATOM 685 N SER A 90 -23.852 -7.829 24.198 1.00 25.43 N ANISOU 685 N SER A 90 3174 3656 2834 -250 242 271 N ATOM 686 CA SER A 90 -24.421 -9.170 24.102 1.00 28.69 C ANISOU 686 CA SER A 90 3627 4036 3238 -303 254 310 C ATOM 687 C SER A 90 -23.681 -9.999 23.063 1.00 27.62 C ANISOU 687 C SER A 90 3531 3824 3140 -295 234 307 C ATOM 688 O SER A 90 -23.434 -11.194 23.270 1.00 29.96 O ANISOU 688 O SER A 90 3885 4064 3434 -308 223 339 O ATOM 689 CB SER A 90 -25.909 -9.084 23.766 1.00 29.60 C ANISOU 689 CB SER A 90 3697 4189 3361 -360 282 305 C ATOM 690 OG SER A 90 -26.483 -10.375 23.671 1.00 30.66 O ANISOU 690 OG SER A 90 3865 4284 3501 -425 292 340 O ATOM 691 N SER A 91 -23.330 -9.384 21.931 1.00 27.22 N ANISOU 691 N SER A 91 3459 3766 3119 -272 232 270 N ATOM 692 CA SER A 91 -22.563 -10.087 20.908 1.00 27.05 C ANISOU 692 CA SER A 91 3476 3679 3123 -256 229 256 C ATOM 693 C SER A 91 -21.226 -10.559 21.465 1.00 28.65 C ANISOU 693 C SER A 91 3695 3842 3349 -205 215 261 C ATOM 694 O SER A 91 -20.805 -11.697 21.230 1.00 30.96 O ANISOU 694 O SER A 91 4035 4069 3659 -197 205 266 O ATOM 695 CB SER A 91 -22.351 -9.178 19.697 1.00 28.81 C ANISOU 695 CB SER A 91 3682 3909 3355 -240 244 221 C ATOM 696 OG SER A 91 -23.581 -8.880 19.056 1.00 30.45 O ANISOU 696 OG SER A 91 3885 4140 3544 -278 233 215 O ATOM 697 N ILE A 92 -20.542 -9.682 22.204 1.00 26.48 N ANISOU 697 N ILE A 92 3379 3599 3083 -167 203 252 N ATOM 698 CA AILE A 92 -19.260 -10.028 22.812 1.00 23.76 C ANISOU 698 CA AILE A 92 3034 3221 2773 -112 170 250 C ATOM 699 C ILE A 92 -19.411 -11.237 23.728 1.00 26.12 C ANISOU 699 C ILE A 92 3400 3484 3040 -116 133 297 C ATOM 700 O ILE A 92 -18.598 -12.169 23.698 1.00 28.77 O ANISOU 700 O ILE A 92 3765 3753 3412 -78 104 300 O ATOM 701 CB AILE A 92 -18.688 -8.817 23.571 1.00 29.10 C ANISOU 701 CB AILE A 92 3655 3942 3462 -81 146 229 C ATOM 702 CG1AILE A 92 -18.111 -7.790 22.596 1.00 32.88 C ANISOU 702 CG1AILE A 92 4073 4424 3997 -73 181 188 C ATOM 703 CG2AILE A 92 -17.634 -9.261 24.573 1.00 26.59 C ANISOU 703 CG2AILE A 92 3342 3597 3163 -28 81 233 C ATOM 704 CD1AILE A 92 -16.806 -8.225 21.976 1.00 45.34 C ANISOU 704 CD1AILE A 92 5623 5953 5651 -35 194 162 C ATOM 705 N PHE A 93 -20.461 -11.238 24.553 1.00 23.35 N ANISOU 705 N PHE A 93 3076 3171 2623 -161 140 335 N ATOM 706 CA PHE A 93 -20.681 -12.350 25.473 1.00 28.06 C ANISOU 706 CA PHE A 93 3754 3731 3177 -177 117 394 C ATOM 707 C PHE A 93 -20.973 -13.642 24.720 1.00 32.73 C ANISOU 707 C PHE A 93 4398 4243 3796 -211 124 413 C ATOM 708 O PHE A 93 -20.486 -14.713 25.102 1.00 31.31 O ANISOU 708 O PHE A 93 4287 3986 3622 -191 84 447 O ATOM 709 CB PHE A 93 -21.824 -12.012 26.431 1.00 27.72 C ANISOU 709 CB PHE A 93 3723 3754 3054 -229 151 428 C ATOM 710 CG PHE A 93 -21.436 -11.052 27.519 1.00 37.29 C ANISOU 710 CG PHE A 93 4925 5026 4218 -186 128 415 C ATOM 711 CD1 PHE A 93 -20.172 -11.097 28.084 1.00 47.71 C ANISOU 711 CD1 PHE A 93 6266 6315 5546 -116 52 409 C ATOM 712 CD2 PHE A 93 -22.330 -10.094 27.969 1.00 37.34 C ANISOU 712 CD2 PHE A 93 4896 5115 4178 -210 173 398 C ATOM 713 CE1 PHE A 93 -19.811 -10.211 29.083 1.00 50.85 C ANISOU 713 CE1 PHE A 93 6661 6763 5898 -77 14 387 C ATOM 714 CE2 PHE A 93 -21.975 -9.204 28.967 1.00 39.08 C ANISOU 714 CE2 PHE A 93 5117 5384 4348 -167 147 374 C ATOM 715 CZ PHE A 93 -20.714 -9.263 29.525 1.00 44.00 C ANISOU 715 CZ PHE A 93 5772 5975 4972 -103 64 369 C ATOM 716 N SER A 94 -21.771 -13.565 23.652 1.00 30.18 N ANISOU 716 N SER A 94 4048 3928 3490 -260 162 388 N ATOM 717 CA SER A 94 -22.052 -14.757 22.858 1.00 31.01 C ANISOU 717 CA SER A 94 4206 3952 3624 -293 159 390 C ATOM 718 C SER A 94 -20.784 -15.295 22.208 1.00 31.98 C ANISOU 718 C SER A 94 4351 4002 3800 -220 134 354 C ATOM 719 O SER A 94 -20.555 -16.510 22.190 1.00 33.33 O ANISOU 719 O SER A 94 4590 4080 3993 -214 107 370 O ATOM 720 CB SER A 94 -23.110 -14.446 21.799 1.00 28.99 C ANISOU 720 CB SER A 94 3916 3725 3373 -350 185 358 C ATOM 721 OG SER A 94 -24.363 -14.159 22.398 1.00 33.22 O ANISOU 721 OG SER A 94 4420 4319 3882 -419 209 388 O ATOM 722 N LEU A 95 -19.953 -14.406 21.657 1.00 27.81 N ANISOU 722 N LEU A 95 3761 3507 3298 -166 150 303 N ATOM 723 CA LEU A 95 -18.725 -14.846 21.002 1.00 30.14 C ANISOU 723 CA LEU A 95 4055 3743 3653 -95 148 258 C ATOM 724 C LEU A 95 -17.774 -15.498 21.998 1.00 29.95 C ANISOU 724 C LEU A 95 4050 3666 3662 -32 89 282 C ATOM 725 O LEU A 95 -17.127 -16.504 21.685 1.00 29.03 O ANISOU 725 O LEU A 95 3969 3464 3596 15 68 264 O ATOM 726 CB LEU A 95 -18.049 -13.665 20.305 1.00 29.90 C ANISOU 726 CB LEU A 95 3948 3767 3648 -64 192 208 C ATOM 727 CG LEU A 95 -18.759 -13.110 19.070 1.00 31.62 C ANISOU 727 CG LEU A 95 4168 4015 3832 -107 242 181 C ATOM 728 CD1 LEU A 95 -18.201 -11.747 18.692 1.00 27.76 C ANISOU 728 CD1 LEU A 95 3611 3581 3356 -88 284 156 C ATOM 729 CD2 LEU A 95 -18.646 -14.085 17.908 1.00 27.99 C ANISOU 729 CD2 LEU A 95 3770 3489 3377 -98 263 142 C ATOM 730 N LEU A 96 -17.672 -14.931 23.202 1.00 31.42 N ANISOU 730 N LEU A 96 4219 3900 3821 -23 52 316 N ATOM 731 CA LEU A 96 -16.822 -15.522 24.231 1.00 33.81 C ANISOU 731 CA LEU A 96 4553 4152 4140 41 -27 344 C ATOM 732 C LEU A 96 -17.344 -16.890 24.652 1.00 35.38 C ANISOU 732 C LEU A 96 4869 4265 4309 14 -60 408 C ATOM 733 O LEU A 96 -16.562 -17.827 24.852 1.00 38.71 O ANISOU 733 O LEU A 96 5335 4595 4777 78 -122 416 O ATOM 734 CB LEU A 96 -16.730 -14.585 25.435 1.00 33.40 C ANISOU 734 CB LEU A 96 4478 4173 4040 50 -65 365 C ATOM 735 CG LEU A 96 -15.868 -15.048 26.612 1.00 34.66 C ANISOU 735 CG LEU A 96 4680 4291 4199 120 -170 394 C ATOM 736 CD1 LEU A 96 -14.460 -15.391 26.148 1.00 32.44 C ANISOU 736 CD1 LEU A 96 4337 3949 4038 214 -216 339 C ATOM 737 CD2 LEU A 96 -15.834 -13.984 27.703 1.00 33.94 C ANISOU 737 CD2 LEU A 96 4570 4280 4046 126 -206 397 C ATOM 738 N ALA A 97 -18.665 -17.019 24.801 1.00 30.31 N ANISOU 738 N ALA A 97 4273 3644 3601 -81 -20 455 N ATOM 739 CA ALA A 97 -19.250 -18.301 25.179 1.00 32.25 C ANISOU 739 CA ALA A 97 4629 3800 3824 -128 -39 523 C ATOM 740 C ALA A 97 -18.980 -19.362 24.120 1.00 33.49 C ANISOU 740 C ALA A 97 4822 3848 4055 -111 -48 486 C ATOM 741 O ALA A 97 -18.667 -20.512 24.450 1.00 35.82 O ANISOU 741 O ALA A 97 5207 4030 4372 -86 -102 523 O ATOM 742 CB ALA A 97 -20.752 -18.143 25.412 1.00 29.37 C ANISOU 742 CB ALA A 97 4276 3488 3396 -244 23 567 C ATOM 743 N ILE A 98 -19.114 -18.998 22.841 1.00 33.39 N ANISOU 743 N ILE A 98 4752 3861 4074 -120 1 412 N ATOM 744 CA ILE A 98 -18.857 -19.950 21.763 1.00 30.15 C ANISOU 744 CA ILE A 98 4383 3353 3721 -99 -1 361 C ATOM 745 C ILE A 98 -17.417 -20.441 21.823 1.00 33.42 C ANISOU 745 C ILE A 98 4796 3695 4205 21 -46 328 C ATOM 746 O ILE A 98 -17.147 -21.637 21.652 1.00 35.70 O ANISOU 746 O ILE A 98 5162 3862 4540 53 -85 324 O ATOM 747 CB ILE A 98 -19.191 -19.322 20.396 1.00 26.67 C ANISOU 747 CB ILE A 98 3891 2966 3276 -122 60 286 C ATOM 748 CG1 ILE A 98 -20.704 -19.135 20.254 1.00 29.28 C ANISOU 748 CG1 ILE A 98 4228 3338 3558 -236 80 312 C ATOM 749 CG2 ILE A 98 -18.648 -20.179 19.260 1.00 27.47 C ANISOU 749 CG2 ILE A 98 4035 2975 3426 -73 64 212 C ATOM 750 CD1 ILE A 98 -21.107 -18.279 19.078 1.00 29.77 C ANISOU 750 CD1 ILE A 98 4241 3470 3600 -255 120 251 C ATOM 751 N ALA A 99 -16.471 -19.529 22.067 1.00 31.89 N ANISOU 751 N ALA A 99 4511 3570 4035 91 -47 300 N ATOM 752 CA ALA A 99 -15.070 -19.926 22.159 1.00 33.33 C ANISOU 752 CA ALA A 99 4664 3693 4307 209 -94 261 C ATOM 753 C ALA A 99 -14.862 -20.889 23.321 1.00 35.17 C ANISOU 753 C ALA A 99 4988 3832 4542 245 -199 333 C ATOM 754 O ALA A 99 -14.181 -21.912 23.183 1.00 37.43 O ANISOU 754 O ALA A 99 5315 4005 4902 323 -250 313 O ATOM 755 CB ALA A 99 -14.182 -18.691 22.311 1.00 25.15 C ANISOU 755 CB ALA A 99 3500 2753 3305 259 -81 221 C ATOM 756 N ILE A 100 -15.436 -20.567 24.484 1.00 33.96 N ANISOU 756 N ILE A 100 4877 3723 4304 195 -231 418 N ATOM 757 CA ILE A 100 -15.244 -21.399 25.667 1.00 34.69 C ANISOU 757 CA ILE A 100 5077 3731 4373 226 -332 501 C ATOM 758 C ILE A 100 -15.902 -22.759 25.468 1.00 36.90 C ANISOU 758 C ILE A 100 5488 3880 4653 177 -339 549 C ATOM 759 O ILE A 100 -15.348 -23.796 25.853 1.00 35.29 O ANISOU 759 O ILE A 100 5371 3549 4490 243 -427 580 O ATOM 760 CB ILE A 100 -15.782 -20.679 26.918 1.00 31.50 C ANISOU 760 CB ILE A 100 4701 3415 3854 175 -344 577 C ATOM 761 CG1 ILE A 100 -14.876 -19.502 27.285 1.00 33.65 C ANISOU 761 CG1 ILE A 100 4862 3782 4144 246 -378 526 C ATOM 762 CG2 ILE A 100 -15.906 -21.643 28.090 1.00 27.64 C ANISOU 762 CG2 ILE A 100 4367 2834 3301 176 -427 685 C ATOM 763 CD1 ILE A 100 -15.455 -18.591 28.346 1.00 33.63 C ANISOU 763 CD1 ILE A 100 4875 3880 4022 196 -374 573 C ATOM 764 N ASP A 101 -17.090 -22.775 24.856 1.00 35.69 N ANISOU 764 N ASP A 101 5349 3748 4465 62 -257 552 N ATOM 765 CA ASP A 101 -17.779 -24.029 24.564 1.00 37.19 C ANISOU 765 CA ASP A 101 5651 3809 4669 -2 -262 586 C ATOM 766 C ASP A 101 -16.922 -24.950 23.702 1.00 35.33 C ANISOU 766 C ASP A 101 5437 3448 4539 93 -301 511 C ATOM 767 O ASP A 101 -16.809 -26.151 23.977 1.00 36.09 O ANISOU 767 O ASP A 101 5649 3393 4670 112 -368 552 O ATOM 768 CB ASP A 101 -19.118 -23.733 23.883 1.00 40.43 C ANISOU 768 CB ASP A 101 6036 4279 5046 -133 -175 575 C ATOM 769 CG ASP A 101 -19.842 -24.987 23.443 1.00 43.93 C ANISOU 769 CG ASP A 101 6580 4588 5523 -209 -184 592 C ATOM 770 OD1 ASP A 101 -20.447 -25.657 24.304 1.00 46.78 O ANISOU 770 OD1 ASP A 101 7038 4883 5854 -284 -200 694 O ATOM 771 OD2 ASP A 101 -19.813 -25.298 22.234 1.00 45.71 O ANISOU 771 OD2 ASP A 101 6794 4771 5802 -198 -173 502 O ATOM 772 N ARG A 102 -16.315 -24.406 22.644 1.00 31.81 N ANISOU 772 N ARG A 102 4887 3056 4144 154 -255 399 N ATOM 773 CA ARG A 102 -15.464 -25.224 21.785 1.00 36.27 C ANISOU 773 CA ARG A 102 5463 3513 4807 253 -272 311 C ATOM 774 C ARG A 102 -14.201 -25.686 22.501 1.00 38.74 C ANISOU 774 C ARG A 102 5777 3748 5195 391 -369 317 C ATOM 775 O ARG A 102 -13.689 -26.772 22.206 1.00 40.12 O ANISOU 775 O ARG A 102 6012 3782 5451 468 -418 283 O ATOM 776 CB ARG A 102 -15.111 -24.466 20.505 1.00 36.98 C ANISOU 776 CB ARG A 102 5445 3690 4916 281 -179 194 C ATOM 777 CG ARG A 102 -16.306 -24.122 19.611 1.00 42.83 C ANISOU 777 CG ARG A 102 6198 4488 5589 163 -106 174 C ATOM 778 CD ARG A 102 -16.989 -25.375 19.047 1.00 48.13 C ANISOU 778 CD ARG A 102 6989 5023 6274 115 -130 159 C ATOM 779 NE ARG A 102 -17.892 -26.018 20.000 1.00 47.86 N ANISOU 779 NE ARG A 102 7046 4922 6216 21 -184 269 N ATOM 780 CZ ARG A 102 -18.037 -27.334 20.124 1.00 48.15 C ANISOU 780 CZ ARG A 102 7203 4794 6298 12 -245 293 C ATOM 781 NH1 ARG A 102 -17.334 -28.156 19.358 1.00 57.39 N ANISOU 781 NH1 ARG A 102 8415 5848 7541 103 -267 204 N ATOM 782 NH2 ARG A 102 -18.882 -27.830 21.019 1.00 42.30 N ANISOU 782 NH2 ARG A 102 6543 3999 5531 -90 -277 406 N ATOM 783 N TYR A 103 -13.683 -24.886 23.435 1.00 36.32 N ANISOU 783 N TYR A 103 5405 3527 4869 429 -407 354 N ATOM 784 CA TYR A 103 -12.527 -25.326 24.210 1.00 39.77 C ANISOU 784 CA TYR A 103 5845 3889 5377 561 -526 365 C ATOM 785 C TYR A 103 -12.881 -26.499 25.115 1.00 43.04 C ANISOU 785 C TYR A 103 6436 4157 5761 551 -629 476 C ATOM 786 O TYR A 103 -12.110 -27.460 25.222 1.00 44.98 O ANISOU 786 O TYR A 103 6732 4264 6095 661 -725 465 O ATOM 787 CB TYR A 103 -11.952 -24.169 25.026 1.00 40.65 C ANISOU 787 CB TYR A 103 5854 4124 5469 595 -559 375 C ATOM 788 CG TYR A 103 -10.812 -24.597 25.921 1.00 46.94 C ANISOU 788 CG TYR A 103 6654 4846 6334 730 -709 389 C ATOM 789 CD1 TYR A 103 -9.549 -24.838 25.397 1.00 43.01 C ANISOU 789 CD1 TYR A 103 6048 4304 5992 867 -740 287 C ATOM 790 CD2 TYR A 103 -10.999 -24.766 27.287 1.00 52.49 C ANISOU 790 CD2 TYR A 103 7472 5524 6948 724 -820 503 C ATOM 791 CE1 TYR A 103 -8.501 -25.230 26.208 1.00 49.71 C ANISOU 791 CE1 TYR A 103 6887 5082 6920 1000 -895 294 C ATOM 792 CE2 TYR A 103 -9.957 -25.162 28.107 1.00 53.41 C ANISOU 792 CE2 TYR A 103 7605 5568 7123 855 -980 517 C ATOM 793 CZ TYR A 103 -8.710 -25.390 27.562 1.00 55.00 C ANISOU 793 CZ TYR A 103 7682 5723 7494 996 -1025 411 C ATOM 794 OH TYR A 103 -7.672 -25.790 28.373 1.00 59.21 O ANISOU 794 OH TYR A 103 8218 6180 8100 1135 -1201 419 O ATOM 795 N ILE A 104 -14.032 -26.434 25.789 1.00 42.83 N ANISOU 795 N ILE A 104 6504 4155 5613 421 -609 584 N ATOM 796 CA ILE A 104 -14.469 -27.550 26.625 1.00 44.74 C ANISOU 796 CA ILE A 104 6928 4255 5815 387 -685 704 C ATOM 797 C ILE A 104 -14.627 -28.812 25.787 1.00 40.63 C ANISOU 797 C ILE A 104 6491 3566 5379 387 -690 672 C ATOM 798 O ILE A 104 -14.249 -29.911 26.213 1.00 44.13 O ANISOU 798 O ILE A 104 7060 3841 5867 449 -794 721 O ATOM 799 CB ILE A 104 -15.775 -27.191 27.358 1.00 45.75 C ANISOU 799 CB ILE A 104 7125 4456 5802 228 -621 815 C ATOM 800 CG1 ILE A 104 -15.573 -25.966 28.252 1.00 42.79 C ANISOU 800 CG1 ILE A 104 6683 4238 5338 242 -625 838 C ATOM 801 CG2 ILE A 104 -16.274 -28.374 28.174 1.00 48.83 C ANISOU 801 CG2 ILE A 104 7713 4693 6148 174 -678 949 C ATOM 802 CD1 ILE A 104 -16.864 -25.377 28.781 1.00 44.73 C ANISOU 802 CD1 ILE A 104 6954 4590 5453 94 -529 912 C ATOM 803 N ALA A 105 -15.185 -28.675 24.583 1.00 40.31 N ANISOU 803 N ALA A 105 6395 3561 5361 321 -589 587 N ATOM 804 CA ALA A 105 -15.416 -29.836 23.730 1.00 41.39 C ANISOU 804 CA ALA A 105 6617 3540 5571 312 -594 542 C ATOM 805 C ALA A 105 -14.108 -30.482 23.286 1.00 45.83 C ANISOU 805 C ALA A 105 7163 3990 6259 489 -663 447 C ATOM 806 O ALA A 105 -14.028 -31.710 23.166 1.00 51.98 O ANISOU 806 O ALA A 105 8063 4583 7105 523 -729 449 O ATOM 807 CB ALA A 105 -16.251 -29.432 22.515 1.00 39.40 C ANISOU 807 CB ALA A 105 6304 3366 5302 213 -483 458 C ATOM 808 N ILE A 106 -13.073 -29.679 23.036 1.00 45.65 N ANISOU 808 N ILE A 106 6990 4073 6283 602 -645 359 N ATOM 809 CA ILE A 106 -11.806 -30.249 22.587 1.00 48.35 C ANISOU 809 CA ILE A 106 7288 4320 6761 775 -695 256 C ATOM 810 C ILE A 106 -10.941 -30.711 23.757 1.00 51.47 C ANISOU 810 C ILE A 106 7725 4623 7207 895 -849 325 C ATOM 811 O ILE A 106 -10.133 -31.633 23.602 1.00 52.05 O ANISOU 811 O ILE A 106 7827 4549 7400 1030 -930 274 O ATOM 812 CB ILE A 106 -11.056 -29.249 21.688 1.00 51.08 C ANISOU 812 CB ILE A 106 7444 4811 7152 838 -592 123 C ATOM 813 CG1 ILE A 106 -9.991 -29.975 20.865 1.00 56.93 C ANISOU 813 CG1 ILE A 106 8144 5450 8036 993 -594 -10 C ATOM 814 CG2 ILE A 106 -10.425 -28.135 22.511 1.00 50.10 C ANISOU 814 CG2 ILE A 106 7194 4825 7019 874 -618 153 C ATOM 815 CD1 ILE A 106 -9.746 -29.351 19.516 1.00 62.26 C ANISOU 815 CD1 ILE A 106 8702 6231 8723 1000 -441 -147 C ATOM 816 N ALA A 107 -11.083 -30.103 24.935 1.00 49.29 N ANISOU 816 N ALA A 107 7462 4426 6842 857 -901 435 N ATOM 817 CA ALA A 107 -10.144 -30.378 26.016 1.00 52.70 C ANISOU 817 CA ALA A 107 7920 4790 7313 987 -1062 487 C ATOM 818 C ALA A 107 -10.644 -31.454 26.967 1.00 59.09 C ANISOU 818 C ALA A 107 8956 5432 8064 955 -1174 635 C ATOM 819 O ALA A 107 -9.837 -32.236 27.482 1.00 61.51 O ANISOU 819 O ALA A 107 9331 5595 8445 1090 -1324 657 O ATOM 820 CB ALA A 107 -9.846 -29.098 26.804 1.00 49.71 C ANISOU 820 CB ALA A 107 7434 4585 6868 985 -1077 512 C ATOM 821 N ILE A 108 -11.949 -31.519 27.212 1.00 58.55 N ANISOU 821 N ILE A 108 9005 5373 7869 780 -1104 739 N ATOM 822 CA ILE A 108 -12.520 -32.579 28.040 1.00 57.42 C ANISOU 822 CA ILE A 108 9087 5062 7668 724 -1183 888 C ATOM 823 C ILE A 108 -13.774 -33.127 27.364 1.00 57.17 C ANISOU 823 C ILE A 108 9134 4970 7618 559 -1076 905 C ATOM 824 O ILE A 108 -14.881 -32.983 27.906 1.00 57.44 O ANISOU 824 O ILE A 108 9246 5045 7533 397 -1013 1017 O ATOM 825 CB ILE A 108 -12.818 -32.070 29.460 1.00 60.47 C ANISOU 825 CB ILE A 108 9556 5524 7896 670 -1225 1034 C ATOM 826 CG1 ILE A 108 -13.501 -30.699 29.414 1.00 59.29 C ANISOU 826 CG1 ILE A 108 9278 5606 7642 554 -1085 1015 C ATOM 827 CG2 ILE A 108 -11.540 -32.001 30.282 1.00 64.33 C ANISOU 827 CG2 ILE A 108 10037 5990 8416 849 -1397 1040 C ATOM 828 CD1 ILE A 108 -14.099 -30.270 30.735 1.00 61.73 C ANISOU 828 CD1 ILE A 108 9691 5988 7775 468 -1088 1156 C ATOM 829 N PRO A 109 -13.659 -33.761 26.192 1.00 59.22 N ANISOU 829 N PRO A 109 9373 5133 7994 592 -1052 790 N ATOM 830 CA PRO A 109 -14.867 -34.249 25.503 1.00 60.40 C ANISOU 830 CA PRO A 109 9590 5227 8132 430 -964 791 C ATOM 831 C PRO A 109 -15.650 -35.299 26.276 1.00 65.70 C ANISOU 831 C PRO A 109 10474 5722 8767 320 -1014 948 C ATOM 832 O PRO A 109 -16.850 -35.459 26.023 1.00 58.21 O ANISOU 832 O PRO A 109 9565 4769 7783 144 -931 984 O ATOM 833 CB PRO A 109 -14.315 -34.830 24.193 1.00 58.10 C ANISOU 833 CB PRO A 109 9259 4841 7976 531 -963 627 C ATOM 834 CG PRO A 109 -12.871 -35.104 24.474 1.00 59.54 C ANISOU 834 CG PRO A 109 9414 4951 8256 745 -1077 583 C ATOM 835 CD PRO A 109 -12.436 -34.033 25.417 1.00 58.83 C ANISOU 835 CD PRO A 109 9232 5027 8092 777 -1097 642 C ATOM 836 N LEU A 110 -15.018 -36.018 27.209 1.00 78.12 N ANISOU 836 N LEU A 110 12185 7146 10351 415 -1150 1045 N ATOM 837 CA LEU A 110 -15.727 -37.074 27.927 1.00 88.66 C ANISOU 837 CA LEU A 110 13743 8293 11652 307 -1195 1205 C ATOM 838 C LEU A 110 -16.749 -36.516 28.909 1.00 87.31 C ANISOU 838 C LEU A 110 13620 8239 11315 132 -1111 1358 C ATOM 839 O LEU A 110 -17.733 -37.194 29.226 1.00 89.55 O ANISOU 839 O LEU A 110 14044 8415 11565 -29 -1074 1475 O ATOM 840 CB LEU A 110 -14.730 -37.996 28.630 1.00 96.72 C ANISOU 840 CB LEU A 110 14912 9111 12726 469 -1376 1270 C ATOM 841 CG LEU A 110 -13.867 -38.829 27.676 1.00102.32 C ANISOU 841 CG LEU A 110 15592 9672 13615 628 -1447 1120 C ATOM 842 CD1 LEU A 110 -12.385 -38.526 27.818 1.00105.16 C ANISOU 842 CD1 LEU A 110 15842 10064 14049 865 -1558 1037 C ATOM 843 CD2 LEU A 110 -14.132 -40.312 27.889 1.00106.16 C ANISOU 843 CD2 LEU A 110 16224 9969 14145 587 -1489 1180 C ATOM 844 N ARG A 111 -16.542 -35.294 29.399 1.00 83.23 N ANISOU 844 N ARG A 111 12987 7938 10699 157 -1075 1356 N ATOM 845 CA ARG A 111 -17.447 -34.686 30.367 1.00 80.94 C ANISOU 845 CA ARG A 111 12736 7774 10245 10 -988 1486 C ATOM 846 C ARG A 111 -18.149 -33.456 29.809 1.00 68.64 C ANISOU 846 C ARG A 111 10983 6449 8647 -86 -836 1401 C ATOM 847 O ARG A 111 -18.849 -32.764 30.557 1.00 64.04 O ANISOU 847 O ARG A 111 10398 6000 7934 -190 -753 1482 O ATOM 848 CB ARG A 111 -16.706 -34.343 31.664 1.00 87.61 C ANISOU 848 CB ARG A 111 13656 8655 10978 114 -1091 1580 C ATOM 849 CG ARG A 111 -15.332 -33.735 31.480 1.00 92.52 C ANISOU 849 CG ARG A 111 14138 9348 11667 321 -1194 1458 C ATOM 850 CD ARG A 111 -14.658 -33.537 32.830 1.00101.32 C ANISOU 850 CD ARG A 111 15354 10473 12672 417 -1325 1559 C ATOM 851 NE ARG A 111 -13.203 -33.600 32.737 1.00107.38 N ANISOU 851 NE ARG A 111 16052 11193 13557 637 -1490 1469 N ATOM 852 CZ ARG A 111 -12.383 -33.508 33.780 1.00111.40 C ANISOU 852 CZ ARG A 111 16630 11688 14008 760 -1650 1527 C ATOM 853 NH1 ARG A 111 -12.873 -33.346 35.001 1.00113.37 N ANISOU 853 NH1 ARG A 111 16995 12012 14070 675 -1631 1652 N ATOM 854 NH2 ARG A 111 -11.071 -33.577 33.601 1.00112.45 N ANISOU 854 NH2 ARG A 111 16661 11786 14279 957 -1792 1425 N ATOM 855 N TYR A 112 -17.966 -33.157 28.520 1.00 64.70 N ANISOU 855 N TYR A 112 10330 5999 8253 -48 -798 1240 N ATOM 856 CA TYR A 112 -18.632 -32.012 27.907 1.00 60.23 C ANISOU 856 CA TYR A 112 9591 5639 7655 -132 -667 1160 C ATOM 857 C TYR A 112 -20.144 -32.111 28.077 1.00 64.33 C ANISOU 857 C TYR A 112 10148 6179 8117 -344 -558 1243 C ATOM 858 O TYR A 112 -20.785 -31.196 28.609 1.00 63.62 O ANISOU 858 O TYR A 112 9995 6252 7924 -426 -469 1285 O ATOM 859 CB TYR A 112 -18.253 -31.914 26.427 1.00 54.28 C ANISOU 859 CB TYR A 112 8712 4896 7015 -66 -650 987 C ATOM 860 CG TYR A 112 -19.010 -30.848 25.661 1.00 51.78 C ANISOU 860 CG TYR A 112 8240 4763 6669 -157 -528 907 C ATOM 861 CD1 TYR A 112 -18.544 -29.542 25.612 1.00 49.87 C ANISOU 861 CD1 TYR A 112 7851 4708 6389 -93 -491 846 C ATOM 862 CD2 TYR A 112 -20.183 -31.149 24.978 1.00 53.70 C ANISOU 862 CD2 TYR A 112 8487 4985 6931 -305 -462 892 C ATOM 863 CE1 TYR A 112 -19.225 -28.562 24.914 1.00 49.37 C ANISOU 863 CE1 TYR A 112 7659 4799 6299 -168 -391 780 C ATOM 864 CE2 TYR A 112 -20.873 -30.176 24.277 1.00 52.98 C ANISOU 864 CE2 TYR A 112 8259 5056 6816 -376 -371 820 C ATOM 865 CZ TYR A 112 -20.389 -28.884 24.248 1.00 50.60 C ANISOU 865 CZ TYR A 112 7824 4932 6468 -304 -335 768 C ATOM 866 OH TYR A 112 -21.068 -27.911 23.552 1.00 44.37 O ANISOU 866 OH TYR A 112 6912 4292 5654 -368 -254 703 O ATOM 867 N ASN A 113 -20.735 -33.217 27.609 1.00 66.13 N ANISOU 867 N ASN A 113 10467 6237 8421 -435 -562 1259 N ATOM 868 CA ASN A 113 -22.191 -33.326 27.576 1.00 69.97 C ANISOU 868 CA ASN A 113 10955 6741 8891 -644 -455 1312 C ATOM 869 C ASN A 113 -22.794 -33.238 28.972 1.00 69.11 C ANISOU 869 C ASN A 113 10938 6667 8655 -750 -399 1484 C ATOM 870 O ASN A 113 -23.914 -32.740 29.132 1.00 71.42 O ANISOU 870 O ASN A 113 11160 7076 8902 -900 -277 1514 O ATOM 871 CB ASN A 113 -22.607 -34.635 26.903 1.00 72.09 C ANISOU 871 CB ASN A 113 11322 6793 9277 -720 -492 1301 C ATOM 872 CG ASN A 113 -22.479 -34.582 25.394 1.00 73.62 C ANISOU 872 CG ASN A 113 11409 6992 9572 -673 -503 1120 C ATOM 873 OD1 ASN A 113 -22.645 -33.527 24.782 1.00 72.08 O ANISOU 873 OD1 ASN A 113 11054 6981 9353 -667 -440 1024 O ATOM 874 ND2 ASN A 113 -22.186 -35.724 24.784 1.00 77.46 N ANISOU 874 ND2 ASN A 113 11996 7269 10164 -638 -583 1072 N ATOM 875 N GLY A 114 -22.077 -33.715 29.993 1.00 66.55 N ANISOU 875 N GLY A 114 10773 6244 8270 -669 -485 1595 N ATOM 876 CA GLY A 114 -22.567 -33.571 31.351 1.00 69.00 C ANISOU 876 CA GLY A 114 11190 6598 8430 -756 -427 1757 C ATOM 877 C GLY A 114 -22.328 -32.204 31.951 1.00 69.23 C ANISOU 877 C GLY A 114 11117 6854 8331 -695 -387 1738 C ATOM 878 O GLY A 114 -23.063 -31.799 32.858 1.00 73.65 O ANISOU 878 O GLY A 114 11711 7511 8762 -800 -286 1835 O ATOM 879 N LEU A 115 -21.318 -31.484 31.464 1.00 63.86 N ANISOU 879 N LEU A 115 10314 6260 7690 -532 -459 1611 N ATOM 880 CA LEU A 115 -20.997 -30.160 31.979 1.00 62.21 C ANISOU 880 CA LEU A 115 10005 6255 7378 -467 -437 1578 C ATOM 881 C LEU A 115 -21.780 -29.074 31.256 1.00 59.19 C ANISOU 881 C LEU A 115 9422 6057 7010 -545 -308 1477 C ATOM 882 O LEU A 115 -22.288 -28.145 31.892 1.00 61.98 O ANISOU 882 O LEU A 115 9728 6568 7254 -594 -223 1501 O ATOM 883 CB LEU A 115 -19.492 -29.896 31.851 1.00 67.69 C ANISOU 883 CB LEU A 115 10655 6943 8120 -259 -579 1494 C ATOM 884 CG LEU A 115 -18.980 -28.463 32.029 1.00 71.57 C ANISOU 884 CG LEU A 115 10999 7635 8559 -177 -574 1413 C ATOM 885 CD1 LEU A 115 -19.387 -27.882 33.373 1.00 74.19 C ANISOU 885 CD1 LEU A 115 11410 8069 8708 -225 -538 1517 C ATOM 886 CD2 LEU A 115 -17.468 -28.415 31.857 1.00 71.73 C ANISOU 886 CD2 LEU A 115 10973 7618 8662 18 -721 1333 C ATOM 887 N VAL A 116 -21.893 -29.184 29.939 1.00 51.96 N ANISOU 887 N VAL A 116 8399 5121 6223 -551 -297 1362 N ATOM 888 CA VAL A 116 -22.430 -28.126 29.096 1.00 49.07 C ANISOU 888 CA VAL A 116 7844 4919 5881 -590 -208 1250 C ATOM 889 C VAL A 116 -23.783 -28.615 28.595 1.00 54.16 C ANISOU 889 C VAL A 116 8477 5528 6575 -765 -121 1265 C ATOM 890 O VAL A 116 -23.861 -29.405 27.647 1.00 57.12 O ANISOU 890 O VAL A 116 8864 5781 7057 -784 -155 1212 O ATOM 891 CB VAL A 116 -21.485 -27.782 27.940 1.00 48.09 C ANISOU 891 CB VAL A 116 7609 4810 5852 -458 -263 1103 C ATOM 892 CG1 VAL A 116 -21.997 -26.581 27.179 1.00 43.57 C ANISOU 892 CG1 VAL A 116 6863 4410 5281 -492 -177 1005 C ATOM 893 CG2 VAL A 116 -20.081 -27.522 28.465 1.00 53.05 C ANISOU 893 CG2 VAL A 116 8250 5441 6467 -289 -363 1092 C ATOM 894 N THR A 117 -24.854 -28.148 29.228 1.00 54.59 N ANISOU 894 N THR A 117 8499 5687 6555 -892 -9 1328 N ATOM 895 CA THR A 117 -26.204 -28.595 28.928 1.00 52.18 C ANISOU 895 CA THR A 117 8168 5356 6303 -1071 78 1353 C ATOM 896 C THR A 117 -27.029 -27.436 28.385 1.00 50.22 C ANISOU 896 C THR A 117 7724 5291 6064 -1121 165 1263 C ATOM 897 O THR A 117 -26.693 -26.263 28.568 1.00 49.01 O ANISOU 897 O THR A 117 7484 5291 5846 -1038 181 1217 O ATOM 898 CB THR A 117 -26.891 -29.189 30.166 1.00 57.96 C ANISOU 898 CB THR A 117 9030 6036 6956 -1199 152 1516 C ATOM 899 OG1 THR A 117 -27.065 -28.169 31.157 1.00 60.46 O ANISOU 899 OG1 THR A 117 9313 6523 7135 -1193 235 1555 O ATOM 900 CG2 THR A 117 -26.053 -30.318 30.751 1.00 60.80 C ANISOU 900 CG2 THR A 117 9603 6201 7296 -1141 51 1617 C ATOM 901 N GLY A 118 -28.117 -27.788 27.697 1.00 52.69 N ANISOU 901 N GLY A 118 7971 5579 6469 -1256 208 1235 N ATOM 902 CA GLY A 118 -28.989 -26.770 27.136 1.00 48.04 C ANISOU 902 CA GLY A 118 7197 5150 5906 -1304 274 1150 C ATOM 903 C GLY A 118 -29.600 -25.872 28.195 1.00 47.80 C ANISOU 903 C GLY A 118 7107 5278 5779 -1348 391 1206 C ATOM 904 O GLY A 118 -29.717 -24.659 28.001 1.00 50.14 O ANISOU 904 O GLY A 118 7270 5730 6050 -1297 419 1131 O ATOM 905 N THR A 119 -29.999 -26.454 29.330 1.00 50.61 N ANISOU 905 N THR A 119 7567 5590 6073 -1442 465 1337 N ATOM 906 CA THR A 119 -30.601 -25.658 30.396 1.00 54.64 C ANISOU 906 CA THR A 119 8035 6249 6476 -1485 594 1389 C ATOM 907 C THR A 119 -29.592 -24.689 31.000 1.00 52.55 C ANISOU 907 C THR A 119 7797 6086 6084 -1326 559 1372 C ATOM 908 O THR A 119 -29.934 -23.543 31.314 1.00 53.15 O ANISOU 908 O THR A 119 7766 6324 6103 -1306 630 1329 O ATOM 909 CB THR A 119 -31.172 -26.576 31.478 1.00 57.76 C ANISOU 909 CB THR A 119 8565 6563 6818 -1622 689 1543 C ATOM 910 OG1 THR A 119 -32.093 -27.500 30.886 1.00 60.48 O ANISOU 910 OG1 THR A 119 8877 6800 7303 -1781 715 1554 O ATOM 911 CG2 THR A 119 -31.895 -25.765 32.542 1.00 58.50 C ANISOU 911 CG2 THR A 119 8611 6820 6797 -1675 847 1586 C ATOM 912 N ARG A 120 -28.343 -25.128 31.166 1.00 51.47 N ANISOU 912 N ARG A 120 7795 5850 5911 -1209 442 1397 N ATOM 913 CA ARG A 120 -27.309 -24.232 31.673 1.00 51.79 C ANISOU 913 CA ARG A 120 7849 5976 5852 -1058 386 1369 C ATOM 914 C ARG A 120 -26.966 -23.157 30.651 1.00 53.15 C ANISOU 914 C ARG A 120 7854 6249 6091 -966 347 1224 C ATOM 915 O ARG A 120 -26.720 -22.002 31.017 1.00 55.85 O ANISOU 915 O ARG A 120 8132 6723 6365 -896 362 1180 O ATOM 916 CB ARG A 120 -26.063 -25.026 32.066 1.00 52.33 C ANISOU 916 CB ARG A 120 8088 5904 5889 -953 257 1427 C ATOM 917 CG ARG A 120 -26.243 -25.876 33.314 1.00 54.28 C ANISOU 917 CG ARG A 120 8533 6066 6026 -1018 283 1586 C ATOM 918 CD ARG A 120 -25.027 -26.752 33.572 1.00 52.92 C ANISOU 918 CD ARG A 120 8529 5732 5847 -907 130 1639 C ATOM 919 NE ARG A 120 -25.293 -27.762 34.592 1.00 57.44 N ANISOU 919 NE ARG A 120 9313 6184 6329 -985 148 1804 N ATOM 920 CZ ARG A 120 -24.516 -28.815 34.822 1.00 60.85 C ANISOU 920 CZ ARG A 120 9919 6433 6770 -924 22 1879 C ATOM 921 NH1 ARG A 120 -24.837 -29.683 35.771 1.00 66.60 N ANISOU 921 NH1 ARG A 120 10806 7075 7426 -986 51 2013 N ATOM 922 NH2 ARG A 120 -23.417 -29.000 34.103 1.00 61.27 N ANISOU 922 NH2 ARG A 120 9942 6409 6927 -779 -124 1792 N ATOM 923 N ALA A 121 -26.932 -23.521 29.366 1.00 49.11 N ANISOU 923 N ALA A 121 7283 5671 5705 -966 297 1148 N ATOM 924 CA ALA A 121 -26.697 -22.530 28.321 1.00 42.71 C ANISOU 924 CA ALA A 121 6328 4950 4948 -893 273 1020 C ATOM 925 C ALA A 121 -27.769 -21.447 28.329 1.00 39.15 C ANISOU 925 C ALA A 121 5735 4654 4485 -954 369 982 C ATOM 926 O ALA A 121 -27.458 -20.258 28.193 1.00 39.35 O ANISOU 926 O ALA A 121 5673 4792 4487 -874 366 913 O ATOM 927 CB ALA A 121 -26.640 -23.212 26.955 1.00 40.32 C ANISOU 927 CB ALA A 121 6010 4545 4764 -899 215 952 C ATOM 928 N ALA A 122 -29.037 -21.837 28.484 1.00 39.84 N ANISOU 928 N ALA A 122 5792 4745 4600 -1095 454 1023 N ATOM 929 CA ALA A 122 -30.114 -20.854 28.446 1.00 41.32 C ANISOU 929 CA ALA A 122 5826 5075 4798 -1148 543 976 C ATOM 930 C ALA A 122 -30.026 -19.892 29.625 1.00 45.68 C ANISOU 930 C ALA A 122 6378 5752 5227 -1102 611 1000 C ATOM 931 O ALA A 122 -30.325 -18.701 29.485 1.00 42.14 O ANISOU 931 O ALA A 122 5807 5428 4776 -1063 639 926 O ATOM 932 CB ALA A 122 -31.470 -21.560 28.428 1.00 36.30 C ANISOU 932 CB ALA A 122 5145 4411 4235 -1315 623 1015 C ATOM 933 N GLY A 123 -29.618 -20.392 30.793 1.00 43.81 N ANISOU 933 N GLY A 123 6288 5475 4882 -1101 629 1100 N ATOM 934 CA GLY A 123 -29.412 -19.513 31.932 1.00 38.18 C ANISOU 934 CA GLY A 123 5602 4872 4032 -1044 676 1114 C ATOM 935 C GLY A 123 -28.268 -18.541 31.719 1.00 40.04 C ANISOU 935 C GLY A 123 5813 5154 4248 -892 577 1034 C ATOM 936 O GLY A 123 -28.373 -17.360 32.063 1.00 45.08 O ANISOU 936 O GLY A 123 6379 5913 4836 -845 611 979 O ATOM 937 N ILE A 124 -27.156 -19.026 31.160 1.00 36.88 N ANISOU 937 N ILE A 124 5468 4652 3893 -813 455 1022 N ATOM 938 CA ILE A 124 -26.024 -18.153 30.859 1.00 35.46 C ANISOU 938 CA ILE A 124 5247 4506 3719 -679 366 943 C ATOM 939 C ILE A 124 -26.436 -17.061 29.880 1.00 34.43 C ANISOU 939 C ILE A 124 4953 4467 3662 -669 389 837 C ATOM 940 O ILE A 124 -26.079 -15.888 30.050 1.00 34.86 O ANISOU 940 O ILE A 124 4949 4609 3687 -597 380 780 O ATOM 941 CB ILE A 124 -24.840 -18.982 30.326 1.00 37.09 C ANISOU 941 CB ILE A 124 5523 4583 3986 -605 248 943 C ATOM 942 CG1 ILE A 124 -24.291 -19.891 31.428 1.00 44.88 C ANISOU 942 CG1 ILE A 124 6681 5481 4889 -586 199 1047 C ATOM 943 CG2 ILE A 124 -23.747 -18.075 29.783 1.00 33.77 C ANISOU 943 CG2 ILE A 124 5023 4200 3606 -484 175 849 C ATOM 944 CD1 ILE A 124 -23.437 -21.028 30.913 1.00 49.65 C ANISOU 944 CD1 ILE A 124 7364 5930 5573 -538 98 1062 C ATOM 945 N ILE A 125 -27.185 -17.428 28.835 1.00 35.67 N ANISOU 945 N ILE A 125 5042 4596 3916 -739 409 810 N ATOM 946 CA ILE A 125 -27.644 -16.441 27.858 1.00 37.46 C ANISOU 946 CA ILE A 125 5127 4899 4206 -730 418 718 C ATOM 947 C ILE A 125 -28.508 -15.378 28.525 1.00 33.05 C ANISOU 947 C ILE A 125 4485 4470 3602 -749 502 701 C ATOM 948 O ILE A 125 -28.359 -14.179 28.257 1.00 31.90 O ANISOU 948 O ILE A 125 4260 4400 3462 -683 490 631 O ATOM 949 CB ILE A 125 -28.395 -17.142 26.709 1.00 39.07 C ANISOU 949 CB ILE A 125 5290 5044 4510 -809 411 697 C ATOM 950 CG1 ILE A 125 -27.434 -18.007 25.892 1.00 40.74 C ANISOU 950 CG1 ILE A 125 5578 5133 4766 -765 326 684 C ATOM 951 CG2 ILE A 125 -29.095 -16.122 25.820 1.00 34.98 C ANISOU 951 CG2 ILE A 125 4636 4611 4045 -808 418 613 C ATOM 952 CD1 ILE A 125 -28.127 -18.970 24.956 1.00 39.10 C ANISOU 952 CD1 ILE A 125 5373 4841 4642 -850 309 672 C ATOM 953 N ALA A 126 -29.422 -15.799 29.405 1.00 36.01 N ANISOU 953 N ALA A 126 4880 4869 3935 -839 595 763 N ATOM 954 CA ALA A 126 -30.255 -14.842 30.129 1.00 36.02 C ANISOU 954 CA ALA A 126 4803 4995 3889 -852 693 741 C ATOM 955 C ALA A 126 -29.402 -13.905 30.976 1.00 38.06 C ANISOU 955 C ALA A 126 5108 5312 4042 -746 671 721 C ATOM 956 O ALA A 126 -29.606 -12.686 30.976 1.00 32.97 O ANISOU 956 O ALA A 126 4373 4757 3396 -696 687 647 O ATOM 957 CB ALA A 126 -31.274 -15.584 30.995 1.00 34.17 C ANISOU 957 CB ALA A 126 4595 4769 3619 -972 815 820 C ATOM 958 N ILE A 127 -28.443 -14.468 31.715 1.00 37.28 N ANISOU 958 N ILE A 127 5153 5155 3856 -709 622 783 N ATOM 959 CA ILE A 127 -27.561 -13.665 32.557 1.00 35.47 C ANISOU 959 CA ILE A 127 4979 4971 3528 -609 578 761 C ATOM 960 C ILE A 127 -26.772 -12.675 31.709 1.00 31.26 C ANISOU 960 C ILE A 127 4358 4449 3069 -516 490 666 C ATOM 961 O ILE A 127 -26.622 -11.502 32.072 1.00 32.47 O ANISOU 961 O ILE A 127 4470 4677 3188 -457 488 605 O ATOM 962 CB ILE A 127 -26.630 -14.582 33.373 1.00 36.79 C ANISOU 962 CB ILE A 127 5318 5054 3605 -582 512 846 C ATOM 963 CG1 ILE A 127 -27.418 -15.304 34.466 1.00 38.40 C ANISOU 963 CG1 ILE A 127 5632 5264 3696 -672 616 947 C ATOM 964 CG2 ILE A 127 -25.489 -13.787 33.983 1.00 34.60 C ANISOU 964 CG2 ILE A 127 5082 4804 3259 -465 418 805 C ATOM 965 CD1 ILE A 127 -26.620 -16.363 35.196 1.00 37.67 C ANISOU 965 CD1 ILE A 127 5728 5068 3516 -655 544 1049 C ATOM 966 N CYS A 128 -26.265 -13.131 30.561 1.00 29.88 N ANISOU 966 N CYS A 128 4160 4196 2997 -505 423 652 N ATOM 967 CA CYS A 128 -25.442 -12.273 29.714 1.00 29.95 C ANISOU 967 CA CYS A 128 4098 4208 3074 -426 354 573 C ATOM 968 C CYS A 128 -26.249 -11.118 29.131 1.00 30.65 C ANISOU 968 C CYS A 128 4063 4376 3207 -432 397 503 C ATOM 969 O CYS A 128 -25.725 -10.010 28.969 1.00 28.66 O ANISOU 969 O CYS A 128 3763 4156 2969 -366 363 443 O ATOM 970 CB CYS A 128 -24.797 -13.099 28.605 1.00 34.27 C ANISOU 970 CB CYS A 128 4657 4657 3708 -417 294 573 C ATOM 971 SG CYS A 128 -23.474 -14.188 29.186 1.00 39.17 S ANISOU 971 SG CYS A 128 5404 5173 4304 -362 207 629 S ATOM 972 N TRP A 129 -27.521 -11.356 28.797 1.00 29.46 N ANISOU 972 N TRP A 129 3854 4249 3089 -511 464 509 N ATOM 973 CA TRP A 129 -28.357 -10.266 28.303 1.00 30.74 C ANISOU 973 CA TRP A 129 3897 4485 3299 -508 494 442 C ATOM 974 C TRP A 129 -28.609 -9.228 29.390 1.00 27.15 C ANISOU 974 C TRP A 129 3423 4119 2774 -470 542 412 C ATOM 975 O TRP A 129 -28.610 -8.022 29.114 1.00 29.29 O ANISOU 975 O TRP A 129 3626 4431 3073 -415 524 344 O ATOM 976 CB TRP A 129 -29.675 -10.807 27.749 1.00 30.27 C ANISOU 976 CB TRP A 129 3766 4429 3304 -599 542 450 C ATOM 977 CG TRP A 129 -29.577 -11.209 26.311 1.00 31.98 C ANISOU 977 CG TRP A 129 3966 4580 3606 -610 475 430 C ATOM 978 CD1 TRP A 129 -29.434 -12.471 25.815 1.00 33.80 C ANISOU 978 CD1 TRP A 129 4256 4722 3866 -661 448 467 C ATOM 979 CD2 TRP A 129 -29.597 -10.331 25.179 1.00 31.14 C ANISOU 979 CD2 TRP A 129 3792 4485 3556 -566 423 365 C ATOM 980 NE1 TRP A 129 -29.372 -12.433 24.441 1.00 33.62 N ANISOU 980 NE1 TRP A 129 4206 4661 3905 -648 386 421 N ATOM 981 CE2 TRP A 129 -29.469 -11.130 24.028 1.00 33.12 C ANISOU 981 CE2 TRP A 129 4071 4660 3854 -592 371 365 C ATOM 982 CE3 TRP A 129 -29.715 -8.946 25.029 1.00 27.77 C ANISOU 982 CE3 TRP A 129 3297 4117 3139 -505 413 309 C ATOM 983 CZ2 TRP A 129 -29.454 -10.589 22.742 1.00 32.14 C ANISOU 983 CZ2 TRP A 129 3917 4525 3770 -561 314 314 C ATOM 984 CZ3 TRP A 129 -29.701 -8.411 23.753 1.00 28.32 C ANISOU 984 CZ3 TRP A 129 3335 4167 3259 -477 353 268 C ATOM 985 CH2 TRP A 129 -29.573 -9.231 22.626 1.00 31.64 C ANISOU 985 CH2 TRP A 129 3792 4519 3709 -505 307 273 C ATOM 986 N VAL A 130 -28.832 -9.674 30.627 1.00 27.02 N ANISOU 986 N VAL A 130 3478 4130 2660 -499 606 461 N ATOM 987 CA VAL A 130 -29.007 -8.739 31.736 1.00 29.90 C ANISOU 987 CA VAL A 130 3847 4578 2934 -457 655 426 C ATOM 988 C VAL A 130 -27.738 -7.920 31.941 1.00 32.78 C ANISOU 988 C VAL A 130 4253 4931 3270 -359 558 382 C ATOM 989 O VAL A 130 -27.786 -6.695 32.107 1.00 33.39 O ANISOU 989 O VAL A 130 4279 5059 3347 -303 554 307 O ATOM 990 CB VAL A 130 -29.404 -9.493 33.019 1.00 35.51 C ANISOU 990 CB VAL A 130 4656 5314 3522 -511 745 498 C ATOM 991 CG1 VAL A 130 -29.385 -8.555 34.218 1.00 33.02 C ANISOU 991 CG1 VAL A 130 4379 5081 3086 -453 786 455 C ATOM 992 CG2 VAL A 130 -30.778 -10.127 32.861 1.00 33.05 C ANISOU 992 CG2 VAL A 130 4274 5026 3258 -620 861 531 C ATOM 993 N LEU A 131 -26.579 -8.585 31.925 1.00 31.13 N ANISOU 993 N LEU A 131 4131 4648 3051 -335 472 423 N ATOM 994 CA ALEU A 131 -25.317 -7.872 32.078 1.00 29.50 C ANISOU 994 CA ALEU A 131 3944 4423 2841 -249 373 378 C ATOM 995 C LEU A 131 -25.056 -6.928 30.911 1.00 33.29 C ANISOU 995 C LEU A 131 4319 4893 3438 -217 335 309 C ATOM 996 O LEU A 131 -24.427 -5.879 31.092 1.00 30.79 O ANISOU 996 O LEU A 131 3983 4588 3129 -157 285 250 O ATOM 997 CB ALEU A 131 -24.166 -8.866 32.220 1.00 26.11 C ANISOU 997 CB ALEU A 131 3609 3913 2400 -228 287 433 C ATOM 998 CG ALEU A 131 -24.163 -9.737 33.476 1.00 36.27 C ANISOU 998 CG ALEU A 131 5034 5192 3555 -243 295 510 C ATOM 999 CD1ALEU A 131 -22.966 -10.678 33.474 1.00 41.79 C ANISOU 999 CD1ALEU A 131 5814 5796 4270 -205 186 557 C ATOM 1000 CD2ALEU A 131 -24.168 -8.872 34.727 1.00 38.08 C ANISOU 1000 CD2ALEU A 131 5313 5495 3659 -200 299 474 C ATOM 1001 N ASER A 132 -25.525 -7.280 29.712 1.00 29.12 N ANISOU 1001 N ASER A 132 3732 4337 2995 -258 353 318 N ATOM 1002 CA ASER A 132 -25.341 -6.401 28.562 1.00 25.62 C ANISOU 1002 CA ASER A 132 3210 3881 2644 -231 322 264 C ATOM 1003 C ASER A 132 -26.161 -5.126 28.704 1.00 27.95 C ANISOU 1003 C ASER A 132 3434 4241 2945 -212 354 204 C ATOM 1004 O ASER A 132 -25.713 -4.046 28.298 1.00 29.27 O ANISOU 1004 O ASER A 132 3566 4399 3158 -166 314 154 O ATOM 1005 CB ASER A 132 -25.706 -7.139 27.276 1.00 27.32 C ANISOU 1005 CB ASER A 132 3401 4052 2928 -278 326 286 C ATOM 1006 OG ASER A 132 -24.851 -8.248 27.078 1.00 25.45 O ANISOU 1006 OG ASER A 132 3230 3745 2697 -281 292 327 O ATOM 1007 N PHE A 133 -27.366 -5.229 29.270 1.00 24.42 N ANISOU 1007 N PHE A 133 2962 3854 2461 -246 431 207 N ATOM 1008 CA PHE A 133 -28.148 -4.028 29.546 1.00 29.41 C ANISOU 1008 CA PHE A 133 3524 4548 3100 -213 465 140 C ATOM 1009 C PHE A 133 -27.459 -3.161 30.593 1.00 30.14 C ANISOU 1009 C PHE A 133 3665 4662 3126 -148 440 94 C ATOM 1010 O PHE A 133 -27.427 -1.932 30.466 1.00 28.95 O ANISOU 1010 O PHE A 133 3471 4517 3013 -96 413 26 O ATOM 1011 CB PHE A 133 -29.564 -4.406 29.982 1.00 26.69 C ANISOU 1011 CB PHE A 133 3130 4269 2740 -265 567 148 C ATOM 1012 CG PHE A 133 -30.516 -4.589 28.835 1.00 29.75 C ANISOU 1012 CG PHE A 133 3421 4652 3233 -307 571 145 C ATOM 1013 CD1 PHE A 133 -31.181 -3.500 28.295 1.00 27.77 C ANISOU 1013 CD1 PHE A 133 3073 4425 3055 -264 555 78 C ATOM 1014 CD2 PHE A 133 -30.736 -5.843 28.287 1.00 29.15 C ANISOU 1014 CD2 PHE A 133 3357 4536 3184 -383 575 204 C ATOM 1015 CE1 PHE A 133 -32.054 -3.658 27.234 1.00 32.12 C ANISOU 1015 CE1 PHE A 133 3538 4968 3699 -295 536 73 C ATOM 1016 CE2 PHE A 133 -31.609 -6.010 27.226 1.00 27.30 C ANISOU 1016 CE2 PHE A 133 3036 4294 3043 -420 559 193 C ATOM 1017 CZ PHE A 133 -32.269 -4.916 26.698 1.00 32.78 C ANISOU 1017 CZ PHE A 133 3632 5018 3805 -375 536 127 C ATOM 1018 N ALA A 134 -26.909 -3.783 31.640 1.00 28.60 N ANISOU 1018 N ALA A 134 3566 4471 2829 -150 440 130 N ATOM 1019 CA ALA A 134 -26.259 -3.013 32.695 1.00 30.23 C ANISOU 1019 CA ALA A 134 3830 4697 2958 -88 401 80 C ATOM 1020 C ALA A 134 -25.023 -2.294 32.166 1.00 29.88 C ANISOU 1020 C ALA A 134 3772 4591 2990 -40 291 41 C ATOM 1021 O ALA A 134 -24.797 -1.120 32.480 1.00 32.48 O ANISOU 1021 O ALA A 134 4087 4928 3327 10 257 -34 O ATOM 1022 CB ALA A 134 -25.895 -3.925 33.866 1.00 29.05 C ANISOU 1022 CB ALA A 134 3805 4557 2675 -98 405 136 C ATOM 1023 N ILE A 135 -24.214 -2.985 31.360 1.00 28.94 N ANISOU 1023 N ILE A 135 3655 4408 2935 -57 241 87 N ATOM 1024 CA ILE A 135 -23.018 -2.372 30.792 1.00 29.81 C ANISOU 1024 CA ILE A 135 3737 4460 3130 -24 156 55 C ATOM 1025 C ILE A 135 -23.391 -1.301 29.773 1.00 28.33 C ANISOU 1025 C ILE A 135 3469 4260 3036 -20 168 12 C ATOM 1026 O ILE A 135 -22.890 -0.171 29.821 1.00 28.34 O ANISOU 1026 O ILE A 135 3448 4241 3079 15 123 -45 O ATOM 1027 CB ILE A 135 -22.110 -3.448 30.169 1.00 28.88 C ANISOU 1027 CB ILE A 135 3636 4281 3057 -39 120 110 C ATOM 1028 CG1 ILE A 135 -21.425 -4.269 31.261 1.00 31.32 C ANISOU 1028 CG1 ILE A 135 4032 4581 3286 -20 68 142 C ATOM 1029 CG2 ILE A 135 -21.082 -2.813 29.238 1.00 28.22 C ANISOU 1029 CG2 ILE A 135 3494 4143 3087 -21 72 78 C ATOM 1030 CD1 ILE A 135 -20.746 -5.523 30.743 1.00 33.20 C ANISOU 1030 CD1 ILE A 135 4292 4757 3564 -30 40 200 C ATOM 1031 N GLY A 136 -24.275 -1.641 28.833 1.00 26.95 N ANISOU 1031 N GLY A 136 3255 4089 2897 -56 218 41 N ATOM 1032 CA GLY A 136 -24.578 -0.721 27.751 1.00 26.20 C ANISOU 1032 CA GLY A 136 3101 3969 2884 -49 212 14 C ATOM 1033 C GLY A 136 -25.378 0.494 28.175 1.00 29.77 C ANISOU 1033 C GLY A 136 3518 4457 3339 -11 223 -50 C ATOM 1034 O GLY A 136 -25.262 1.560 27.561 1.00 27.75 O ANISOU 1034 O GLY A 136 3233 4161 3149 14 191 -83 O ATOM 1035 N LEU A 137 -26.195 0.363 29.218 1.00 26.66 N ANISOU 1035 N LEU A 137 3127 4130 2872 -5 275 -69 N ATOM 1036 CA LEU A 137 -26.979 1.483 29.719 1.00 28.56 C ANISOU 1036 CA LEU A 137 3331 4407 3112 42 296 -144 C ATOM 1037 C LEU A 137 -26.370 2.127 30.958 1.00 24.92 C ANISOU 1037 C LEU A 137 2925 3959 2584 89 270 -204 C ATOM 1038 O LEU A 137 -27.044 2.919 31.623 1.00 28.48 O ANISOU 1038 O LEU A 137 3361 4450 3009 133 300 -275 O ATOM 1039 CB LEU A 137 -28.414 1.040 30.008 1.00 27.07 C ANISOU 1039 CB LEU A 137 3094 4295 2898 21 388 -143 C ATOM 1040 CG LEU A 137 -29.180 0.461 28.814 1.00 26.38 C ANISOU 1040 CG LEU A 137 2941 4197 2884 -25 399 -100 C ATOM 1041 CD1 LEU A 137 -30.600 0.091 29.211 1.00 28.28 C ANISOU 1041 CD1 LEU A 137 3112 4516 3119 -50 491 -110 C ATOM 1042 CD2 LEU A 137 -29.172 1.427 27.630 1.00 23.17 C ANISOU 1042 CD2 LEU A 137 2495 3733 2574 9 330 -123 C ATOM 1043 N THR A 138 -25.129 1.783 31.299 1.00 25.80 N ANISOU 1043 N THR A 138 3098 4037 2669 85 209 -184 N ATOM 1044 CA THR A 138 -24.438 2.457 32.396 1.00 24.80 C ANISOU 1044 CA THR A 138 3025 3910 2488 132 154 -249 C ATOM 1045 C THR A 138 -24.483 3.982 32.305 1.00 26.49 C ANISOU 1045 C THR A 138 3206 4091 2770 180 116 -339 C ATOM 1046 O THR A 138 -24.635 4.626 33.358 1.00 28.47 O ANISOU 1046 O THR A 138 3494 4371 2954 227 111 -417 O ATOM 1047 CB THR A 138 -22.988 1.949 32.470 1.00 26.50 C ANISOU 1047 CB THR A 138 3281 4076 2712 123 67 -218 C ATOM 1048 OG1 THR A 138 -22.949 0.720 33.205 1.00 30.48 O ANISOU 1048 OG1 THR A 138 3858 4617 3107 106 84 -161 O ATOM 1049 CG2 THR A 138 -22.076 2.962 33.154 1.00 24.31 C ANISOU 1049 CG2 THR A 138 3026 3766 2444 167 -28 -300 C ATOM 1050 N PRO A 139 -24.382 4.618 31.128 1.00 27.01 N ANISOU 1050 N PRO A 139 3215 4091 2957 173 90 -335 N ATOM 1051 CA PRO A 139 -24.562 6.079 31.081 1.00 26.91 C ANISOU 1051 CA PRO A 139 3181 4035 3008 221 56 -415 C ATOM 1052 C PRO A 139 -25.894 6.556 31.632 1.00 27.87 C ANISOU 1052 C PRO A 139 3281 4216 3091 270 118 -479 C ATOM 1053 O PRO A 139 -25.966 7.668 32.171 1.00 27.14 O ANISOU 1053 O PRO A 139 3201 4104 3009 327 88 -571 O ATOM 1054 CB PRO A 139 -24.413 6.387 29.585 1.00 26.20 C ANISOU 1054 CB PRO A 139 3048 3869 3036 193 38 -367 C ATOM 1055 CG PRO A 139 -23.435 5.356 29.139 1.00 25.10 C ANISOU 1055 CG PRO A 139 2921 3715 2899 139 29 -292 C ATOM 1056 CD PRO A 139 -23.960 4.115 29.807 1.00 23.98 C ANISOU 1056 CD PRO A 139 2802 3657 2653 126 83 -259 C ATOM 1057 N AMET A 140 -26.954 5.755 31.510 0.70 25.93 N ANISOU 1057 N AMET A 140 3000 4042 2811 251 204 -440 N ATOM 1058 N BMET A 140 -26.948 5.755 31.515 0.30 25.91 N ANISOU 1058 N BMET A 140 2998 4040 2809 251 204 -440 N ATOM 1059 CA AMET A 140 -28.241 6.157 32.061 0.70 26.53 C ANISOU 1059 CA AMET A 140 3034 4185 2863 297 279 -506 C ATOM 1060 CA BMET A 140 -28.260 6.123 32.038 0.30 26.96 C ANISOU 1060 CA BMET A 140 3086 4240 2917 295 280 -503 C ATOM 1061 C AMET A 140 -28.249 6.116 33.583 0.70 29.83 C ANISOU 1061 C AMET A 140 3519 4671 3144 326 323 -565 C ATOM 1062 C BMET A 140 -28.239 6.195 33.561 0.30 29.19 C ANISOU 1062 C BMET A 140 3436 4586 3069 330 319 -569 C ATOM 1063 O AMET A 140 -29.154 6.686 34.201 0.70 29.65 O ANISOU 1063 O AMET A 140 3471 4700 3095 380 387 -646 O ATOM 1064 O BMET A 140 -29.102 6.820 34.174 0.30 29.95 O ANISOU 1064 O BMET A 140 3509 4729 3141 386 377 -654 O ATOM 1065 CB AMET A 140 -29.355 5.272 31.498 0.70 27.13 C ANISOU 1065 CB AMET A 140 3036 4316 2955 256 358 -448 C ATOM 1066 CB BMET A 140 -29.322 5.123 31.577 0.30 27.39 C ANISOU 1066 CB BMET A 140 3075 4356 2976 249 365 -441 C ATOM 1067 CG AMET A 140 -29.416 5.257 29.980 0.70 28.93 C ANISOU 1067 CG AMET A 140 3215 4481 3297 231 307 -393 C ATOM 1068 CG BMET A 140 -29.418 4.959 30.069 0.30 29.03 C ANISOU 1068 CG BMET A 140 3232 4507 3291 217 321 -380 C ATOM 1069 SD AMET A 140 -30.936 4.535 29.335 0.70 33.50 S ANISOU 1069 SD AMET A 140 3687 5120 3922 200 374 -363 S ATOM 1070 SD BMET A 140 -30.104 6.412 29.256 0.30 28.97 S ANISOU 1070 SD BMET A 140 3157 4443 3410 290 266 -443 S ATOM 1071 CE AMET A 140 -32.122 5.788 29.805 0.70 29.84 C ANISOU 1071 CE AMET A 140 3137 4690 3510 295 403 -479 C ATOM 1072 CE BMET A 140 -31.677 6.548 30.102 0.30 31.39 C ANISOU 1072 CE BMET A 140 3371 4852 3703 338 368 -524 C ATOM 1073 N ALEU A 141 -27.265 5.460 34.198 1.00 29.53 N ANISOU 1073 N ALEU A 141 3568 4634 3016 298 289 -529 N ATOM 1074 CA ALEU A 141 -27.126 5.470 35.648 1.00 32.27 C ANISOU 1074 CA ALEU A 141 4009 5037 3215 331 307 -583 C ATOM 1075 C ALEU A 141 -26.421 6.719 36.162 1.00 34.75 C ANISOU 1075 C ALEU A 141 4368 5298 3538 395 209 -692 C ATOM 1076 O ALEU A 141 -26.253 6.859 37.380 1.00 36.41 O ANISOU 1076 O ALEU A 141 4669 5547 3616 431 205 -754 O ATOM 1077 CB ALEU A 141 -26.377 4.220 36.121 1.00 36.03 C ANISOU 1077 CB ALEU A 141 4574 5530 3587 282 291 -497 C ATOM 1078 CG ALEU A 141 -26.965 2.866 35.716 1.00 41.82 C ANISOU 1078 CG ALEU A 141 5284 6301 4303 211 379 -386 C ATOM 1079 CD1ALEU A 141 -26.293 1.741 36.486 1.00 43.70 C ANISOU 1079 CD1ALEU A 141 5638 6552 4414 181 362 -314 C ATOM 1080 CD2ALEU A 141 -28.470 2.835 35.921 1.00 39.18 C ANISOU 1080 CD2ALEU A 141 4890 6050 3946 206 523 -405 C ATOM 1081 N GLY A 142 -25.999 7.615 35.272 1.00 27.10 N ANISOU 1081 N GLY A 142 3347 4234 2715 404 128 -714 N ATOM 1082 CA GLY A 142 -25.458 8.896 35.681 1.00 29.87 C ANISOU 1082 CA GLY A 142 3729 4518 3101 459 37 -823 C ATOM 1083 C GLY A 142 -24.131 9.258 35.046 1.00 29.50 C ANISOU 1083 C GLY A 142 3677 4362 3168 424 -86 -803 C ATOM 1084 O GLY A 142 -23.676 10.400 35.162 1.00 31.55 O ANISOU 1084 O GLY A 142 3948 4543 3496 455 -167 -886 O ATOM 1085 N TRP A 143 -23.497 8.302 34.366 1.00 27.83 N ANISOU 1085 N TRP A 143 3446 4140 2987 360 -95 -696 N ATOM 1086 CA TRP A 143 -22.230 8.564 33.685 1.00 24.77 C ANISOU 1086 CA TRP A 143 3036 3657 2719 320 -188 -672 C ATOM 1087 C TRP A 143 -22.560 9.105 32.297 1.00 28.10 C ANISOU 1087 C TRP A 143 3392 4012 3275 299 -165 -633 C ATOM 1088 O TRP A 143 -22.464 8.416 31.280 1.00 28.94 O ANISOU 1088 O TRP A 143 3462 4110 3422 250 -132 -540 O ATOM 1089 CB TRP A 143 -21.373 7.306 33.628 1.00 23.48 C ANISOU 1089 CB TRP A 143 2881 3512 2527 273 -205 -588 C ATOM 1090 CG TRP A 143 -19.940 7.567 33.259 1.00 28.11 C ANISOU 1090 CG TRP A 143 3439 4014 3229 241 -302 -588 C ATOM 1091 CD1 TRP A 143 -19.391 8.763 32.898 1.00 29.05 C ANISOU 1091 CD1 TRP A 143 3525 4040 3474 235 -362 -641 C ATOM 1092 CD2 TRP A 143 -18.869 6.613 33.242 1.00 25.93 C ANISOU 1092 CD2 TRP A 143 3156 3734 2964 211 -347 -535 C ATOM 1093 NE1 TRP A 143 -18.048 8.610 32.645 1.00 25.45 N ANISOU 1093 NE1 TRP A 143 3030 3529 3111 193 -431 -624 N ATOM 1094 CE2 TRP A 143 -17.704 7.300 32.849 1.00 25.04 C ANISOU 1094 CE2 TRP A 143 2988 3533 2993 185 -426 -564 C ATOM 1095 CE3 TRP A 143 -18.784 5.244 33.515 1.00 25.61 C ANISOU 1095 CE3 TRP A 143 3147 3748 2835 204 -330 -467 C ATOM 1096 CZ2 TRP A 143 -16.468 6.665 32.724 1.00 23.45 C ANISOU 1096 CZ2 TRP A 143 2746 3307 2855 159 -484 -535 C ATOM 1097 CZ3 TRP A 143 -17.556 4.615 33.389 1.00 24.01 C ANISOU 1097 CZ3 TRP A 143 2920 3513 2691 187 -398 -436 C ATOM 1098 CH2 TRP A 143 -16.416 5.325 32.997 1.00 24.55 C ANISOU 1098 CH2 TRP A 143 2916 3502 2908 167 -473 -475 C ATOM 1099 N ASN A 144 -22.943 10.379 32.267 1.00 29.01 N ANISOU 1099 N ASN A 144 3502 4070 3451 342 -190 -708 N ATOM 1100 CA ASN A 144 -23.432 11.016 31.053 1.00 26.09 C ANISOU 1100 CA ASN A 144 3089 3632 3191 339 -177 -676 C ATOM 1101 C ASN A 144 -23.160 12.511 31.134 1.00 30.08 C ANISOU 1101 C ASN A 144 3611 4027 3789 371 -252 -760 C ATOM 1102 O ASN A 144 -22.760 13.034 32.177 1.00 31.85 O ANISOU 1102 O ASN A 144 3875 4240 3987 402 -307 -856 O ATOM 1103 CB ASN A 144 -24.921 10.713 30.841 1.00 25.55 C ANISOU 1103 CB ASN A 144 2987 3637 3084 375 -94 -664 C ATOM 1104 CG ASN A 144 -25.806 11.289 31.938 1.00 31.12 C ANISOU 1104 CG ASN A 144 3702 4393 3729 456 -68 -777 C ATOM 1105 OD1 ASN A 144 -25.827 12.497 32.178 1.00 35.92 O ANISOU 1105 OD1 ASN A 144 4325 4930 4391 510 -119 -866 O ATOM 1106 ND2 ASN A 144 -26.541 10.414 32.616 1.00 30.35 N ANISOU 1106 ND2 ASN A 144 3599 4413 3520 463 19 -775 N ATOM 1107 N ASN A 145 -23.384 13.201 30.015 1.00 27.06 N ANISOU 1107 N ASN A 145 3211 3555 3513 364 -261 -722 N ATOM 1108 CA ASN A 145 -23.187 14.642 29.952 1.00 28.54 C ANISOU 1108 CA ASN A 145 3423 3616 3804 389 -332 -787 C ATOM 1109 C ASN A 145 -24.494 15.421 30.045 1.00 34.35 C ANISOU 1109 C ASN A 145 4156 4344 4551 483 -324 -854 C ATOM 1110 O ASN A 145 -24.548 16.577 29.614 1.00 36.77 O ANISOU 1110 O ASN A 145 4483 4527 4960 507 -380 -879 O ATOM 1111 CB ASN A 145 -22.455 15.019 28.663 1.00 29.51 C ANISOU 1111 CB ASN A 145 3546 3623 4044 317 -354 -697 C ATOM 1112 CG ASN A 145 -21.073 14.409 28.575 1.00 35.74 C ANISOU 1112 CG ASN A 145 4319 4407 4853 230 -360 -649 C ATOM 1113 OD1 ASN A 145 -20.397 14.227 29.587 1.00 41.97 O ANISOU 1113 OD1 ASN A 145 5108 5225 5613 228 -402 -712 O ATOM 1114 ND2 ASN A 145 -20.642 14.095 27.358 1.00 40.76 N ANISOU 1114 ND2 ASN A 145 4942 5006 5538 162 -323 -542 N ATOM 1115 N CYS A 146 -25.552 14.816 30.591 1.00 34.91 N ANISOU 1115 N CYS A 146 4199 4538 4527 535 -254 -883 N ATOM 1116 CA CYS A 146 -26.827 15.524 30.654 1.00 37.03 C ANISOU 1116 CA CYS A 146 4441 4805 4823 631 -239 -954 C ATOM 1117 C CYS A 146 -26.781 16.661 31.665 1.00 39.29 C ANISOU 1117 C CYS A 146 4771 5037 5121 707 -289 -1100 C ATOM 1118 O CYS A 146 -27.540 17.629 31.543 1.00 39.75 O ANISOU 1118 O CYS A 146 4819 5032 5251 790 -312 -1167 O ATOM 1119 CB CYS A 146 -27.965 14.554 30.975 1.00 42.37 C ANISOU 1119 CB CYS A 146 5057 5631 5408 657 -136 -949 C ATOM 1120 SG CYS A 146 -28.309 13.406 29.623 1.00 44.38 S ANISOU 1120 SG CYS A 146 5258 5926 5677 585 -97 -797 S ATOM 1121 N GLY A 147 -25.902 16.563 32.666 1.00 40.39 N ANISOU 1121 N GLY A 147 4961 5194 5190 686 -316 -1156 N ATOM 1122 CA GLY A 147 -25.732 17.649 33.613 1.00 42.80 C ANISOU 1122 CA GLY A 147 5323 5436 5503 751 -379 -1302 C ATOM 1123 C GLY A 147 -25.098 18.891 33.025 1.00 44.79 C ANISOU 1123 C GLY A 147 5604 5503 5911 737 -487 -1318 C ATOM 1124 O GLY A 147 -25.236 19.975 33.602 1.00 52.01 O ANISOU 1124 O GLY A 147 6560 6338 6864 808 -543 -1445 O ATOM 1125 N GLN A 148 -24.403 18.763 31.895 1.00 45.08 N ANISOU 1125 N GLN A 148 5626 5464 6038 646 -511 -1193 N ATOM 1126 CA GLN A 148 -23.716 19.889 31.259 1.00 48.73 C ANISOU 1126 CA GLN A 148 6121 5743 6652 609 -599 -1184 C ATOM 1127 C GLN A 148 -24.145 20.012 29.801 1.00 48.29 C ANISOU 1127 C GLN A 148 6050 5621 6675 589 -580 -1060 C ATOM 1128 O GLN A 148 -23.337 19.832 28.884 1.00 49.16 O ANISOU 1128 O GLN A 148 6163 5674 6841 491 -581 -947 O ATOM 1129 CB GLN A 148 -22.199 19.734 31.368 1.00 60.31 C ANISOU 1129 CB GLN A 148 7594 7164 8155 502 -650 -1160 C ATOM 1130 CG GLN A 148 -21.696 19.223 32.712 1.00 74.47 C ANISOU 1130 CG GLN A 148 9403 9054 9840 511 -675 -1251 C ATOM 1131 CD GLN A 148 -21.579 17.711 32.762 1.00 84.10 C ANISOU 1131 CD GLN A 148 10587 10426 10941 473 -602 -1164 C ATOM 1132 OE1 GLN A 148 -21.139 17.078 31.802 1.00 84.64 O ANISOU 1132 OE1 GLN A 148 10614 10495 11050 396 -567 -1040 O ATOM 1133 NE2 GLN A 148 -21.970 17.124 33.888 1.00 88.76 N ANISOU 1133 NE2 GLN A 148 11203 11141 11380 527 -575 -1230 N ATOM 1134 N PRO A 149 -25.422 20.305 29.547 1.00 46.48 N ANISOU 1134 N PRO A 149 5807 5403 6453 684 -563 -1079 N ATOM 1135 CA PRO A 149 -25.897 20.363 28.161 1.00 42.68 C ANISOU 1135 CA PRO A 149 5322 4865 6031 675 -562 -960 C ATOM 1136 C PRO A 149 -25.220 21.481 27.382 1.00 45.32 C ANISOU 1136 C PRO A 149 5726 4998 6494 631 -640 -914 C ATOM 1137 O PRO A 149 -24.842 22.516 27.936 1.00 48.90 O ANISOU 1137 O PRO A 149 6224 5335 7021 651 -708 -1006 O ATOM 1138 CB PRO A 149 -27.399 20.623 28.315 1.00 38.84 C ANISOU 1138 CB PRO A 149 4794 4420 5541 806 -552 -1030 C ATOM 1139 CG PRO A 149 -27.507 21.345 29.615 1.00 41.76 C ANISOU 1139 CG PRO A 149 5181 4780 5907 887 -574 -1197 C ATOM 1140 CD PRO A 149 -26.479 20.693 30.499 1.00 44.66 C ANISOU 1140 CD PRO A 149 5562 5224 6184 811 -550 -1220 C ATOM 1141 N LYS A 150 -25.072 21.264 26.077 1.00 41.48 N ANISOU 1141 N LYS A 150 5261 4468 6032 567 -627 -770 N ATOM 1142 CA LYS A 150 -24.636 22.320 25.166 1.00 42.30 C ANISOU 1142 CA LYS A 150 5447 4377 6247 528 -687 -702 C ATOM 1143 C LYS A 150 -25.834 23.222 24.898 1.00 43.09 C ANISOU 1143 C LYS A 150 5579 4392 6403 653 -755 -737 C ATOM 1144 O LYS A 150 -26.631 22.988 23.989 1.00 42.87 O ANISOU 1144 O LYS A 150 5554 4379 6356 690 -758 -657 O ATOM 1145 CB LYS A 150 -24.057 21.725 23.889 1.00 42.95 C ANISOU 1145 CB LYS A 150 5555 4453 6312 419 -637 -537 C ATOM 1146 CG LYS A 150 -22.797 20.914 24.141 1.00 44.99 C ANISOU 1146 CG LYS A 150 5772 4779 6543 302 -574 -512 C ATOM 1147 CD LYS A 150 -21.944 20.759 22.894 1.00 48.62 C ANISOU 1147 CD LYS A 150 6273 5174 7028 185 -526 -366 C ATOM 1148 CE LYS A 150 -20.835 19.748 23.133 1.00 55.02 C ANISOU 1148 CE LYS A 150 7016 6080 7808 90 -456 -349 C ATOM 1149 NZ LYS A 150 -20.077 19.432 21.892 1.00 61.85 N ANISOU 1149 NZ LYS A 150 7909 6908 8682 -16 -381 -213 N ATOM 1150 N GLU A 151 -25.960 24.276 25.709 1.00 47.62 N ANISOU 1150 N GLU A 151 6176 4869 7048 727 -822 -867 N ATOM 1151 CA GLU A 151 -27.134 25.139 25.633 1.00 54.96 C ANISOU 1151 CA GLU A 151 7121 5721 8039 869 -890 -928 C ATOM 1152 C GLU A 151 -27.169 25.955 24.347 1.00 53.71 C ANISOU 1152 C GLU A 151 7062 5375 7970 858 -964 -808 C ATOM 1153 O GLU A 151 -28.252 26.209 23.809 1.00 53.81 O ANISOU 1153 O GLU A 151 7077 5363 8005 964 -1013 -794 O ATOM 1154 CB GLU A 151 -27.187 26.056 26.855 1.00 64.60 C ANISOU 1154 CB GLU A 151 8353 6879 9313 953 -940 -1109 C ATOM 1155 CG GLU A 151 -28.550 26.108 27.530 1.00 75.99 C ANISOU 1155 CG GLU A 151 9726 8413 10733 1118 -930 -1241 C ATOM 1156 CD GLU A 151 -28.998 24.757 28.060 1.00 81.12 C ANISOU 1156 CD GLU A 151 10271 9306 11245 1118 -815 -1256 C ATOM 1157 OE1 GLU A 151 -29.602 23.981 27.288 1.00 83.53 O ANISOU 1157 OE1 GLU A 151 10523 9700 11516 1112 -777 -1157 O ATOM 1158 OE2 GLU A 151 -28.745 24.469 29.249 1.00 84.91 O ANISOU 1158 OE2 GLU A 151 10731 9883 11649 1121 -768 -1365 O ATOM 1159 N GLY A 152 -26.007 26.366 23.835 1.00 49.04 N ANISOU 1159 N GLY A 152 6553 4649 7432 731 -973 -719 N ATOM 1160 CA GLY A 152 -25.994 27.140 22.604 1.00 48.88 C ANISOU 1160 CA GLY A 152 6649 4442 7479 709 -1032 -589 C ATOM 1161 C GLY A 152 -26.470 26.331 21.415 1.00 51.28 C ANISOU 1161 C GLY A 152 6963 4826 7695 696 -999 -444 C ATOM 1162 O GLY A 152 -27.174 26.847 20.542 1.00 57.20 O ANISOU 1162 O GLY A 152 7790 5474 8470 762 -1074 -375 O ATOM 1163 N LYS A 153 -26.096 25.052 21.364 1.00 43.62 N ANISOU 1163 N LYS A 153 5923 4031 6620 617 -898 -400 N ATOM 1164 CA LYS A 153 -26.578 24.186 20.295 1.00 43.23 C ANISOU 1164 CA LYS A 153 5880 4068 6477 607 -868 -281 C ATOM 1165 C LYS A 153 -28.072 23.924 20.439 1.00 42.92 C ANISOU 1165 C LYS A 153 5767 4124 6415 755 -915 -347 C ATOM 1166 O LYS A 153 -28.805 23.903 19.443 1.00 41.20 O ANISOU 1166 O LYS A 153 5592 3882 6179 801 -971 -266 O ATOM 1167 CB LYS A 153 -25.801 22.870 20.302 1.00 44.88 C ANISOU 1167 CB LYS A 153 6027 4434 6590 493 -750 -235 C ATOM 1168 CG LYS A 153 -25.997 22.017 19.062 1.00 45.25 C ANISOU 1168 CG LYS A 153 6110 4541 6542 454 -714 -101 C ATOM 1169 CD LYS A 153 -25.195 20.729 19.158 1.00 45.99 C ANISOU 1169 CD LYS A 153 6140 4781 6554 351 -599 -73 C ATOM 1170 CE LYS A 153 -23.703 21.005 19.244 1.00 50.91 C ANISOU 1170 CE LYS A 153 6786 5328 7229 225 -542 -44 C ATOM 1171 NZ LYS A 153 -22.897 19.786 18.959 1.00 52.62 N ANISOU 1171 NZ LYS A 153 6961 5660 7372 127 -433 12 N ATOM 1172 N ALA A 154 -28.538 23.716 21.674 1.00 43.61 N ANISOU 1172 N ALA A 154 5742 4323 6504 828 -893 -495 N ATOM 1173 CA ALA A 154 -29.964 23.521 21.914 1.00 44.82 C ANISOU 1173 CA ALA A 154 5803 4571 6658 967 -922 -574 C ATOM 1174 C ALA A 154 -30.773 24.756 21.531 1.00 49.12 C ANISOU 1174 C ALA A 154 6402 4951 7311 1095 -1050 -597 C ATOM 1175 O ALA A 154 -31.828 24.643 20.895 1.00 48.38 O ANISOU 1175 O ALA A 154 6279 4877 7226 1182 -1110 -573 O ATOM 1176 CB ALA A 154 -30.202 23.156 23.380 1.00 41.65 C ANISOU 1176 CB ALA A 154 5287 4309 6230 1012 -853 -729 C ATOM 1177 N HIS A 155 -30.298 25.946 21.912 1.00 50.99 N ANISOU 1177 N HIS A 155 6717 5018 7641 1112 -1106 -650 N ATOM 1178 CA HIS A 155 -31.025 27.167 21.576 1.00 55.90 C ANISOU 1178 CA HIS A 155 7402 5462 8376 1241 -1238 -674 C ATOM 1179 C HIS A 155 -31.026 27.421 20.073 1.00 51.33 C ANISOU 1179 C HIS A 155 6954 4753 7796 1211 -1316 -497 C ATOM 1180 O HIS A 155 -32.016 27.918 19.525 1.00 57.21 O ANISOU 1180 O HIS A 155 7720 5423 8595 1337 -1431 -489 O ATOM 1181 CB HIS A 155 -30.437 28.363 22.326 1.00 62.24 C ANISOU 1181 CB HIS A 155 8273 6097 9280 1254 -1280 -770 C ATOM 1182 CG HIS A 155 -30.784 28.394 23.782 1.00 70.14 C ANISOU 1182 CG HIS A 155 9167 7195 10289 1342 -1241 -971 C ATOM 1183 ND1 HIS A 155 -32.077 28.545 24.234 1.00 76.14 N ANISOU 1183 ND1 HIS A 155 9830 8015 11086 1513 -1265 -1097 N ATOM 1184 CD2 HIS A 155 -30.007 28.309 24.888 1.00 74.39 C ANISOU 1184 CD2 HIS A 155 9684 7780 10798 1285 -1179 -1071 C ATOM 1185 CE1 HIS A 155 -32.083 28.542 25.555 1.00 78.22 C ANISOU 1185 CE1 HIS A 155 10027 8363 11330 1555 -1204 -1264 C ATOM 1186 NE2 HIS A 155 -30.840 28.400 25.977 1.00 74.65 N ANISOU 1186 NE2 HIS A 155 9628 7904 10832 1421 -1160 -1251 N ATOM 1187 N SER A 156 -29.928 27.090 19.389 1.00 48.54 N ANISOU 1187 N SER A 156 6691 4372 7379 1050 -1258 -356 N ATOM 1188 CA SER A 156 -29.851 27.355 17.956 1.00 51.12 C ANISOU 1188 CA SER A 156 7169 4572 7681 1012 -1318 -181 C ATOM 1189 C SER A 156 -30.842 26.502 17.176 1.00 53.56 C ANISOU 1189 C SER A 156 7438 5005 7907 1071 -1349 -127 C ATOM 1190 O SER A 156 -31.316 26.920 16.113 1.00 54.91 O ANISOU 1190 O SER A 156 7723 5065 8074 1119 -1458 -26 O ATOM 1191 CB SER A 156 -28.432 27.111 17.445 1.00 48.43 C ANISOU 1191 CB SER A 156 6919 4195 7286 821 -1218 -53 C ATOM 1192 OG SER A 156 -28.056 25.755 17.605 1.00 56.38 O ANISOU 1192 OG SER A 156 7824 5410 8186 737 -1093 -47 O ATOM 1193 N AGLN A 157 -31.167 25.316 17.683 1.00 54.05 N ANISOU 1193 N AGLN A 157 7346 5288 7901 1066 -1264 -191 N ATOM 1194 CA AGLN A 157 -32.100 24.415 17.025 1.00 56.40 C ANISOU 1194 CA AGLN A 157 7587 5712 8131 1110 -1292 -155 C ATOM 1195 C AGLN A 157 -33.528 24.569 17.529 1.00 55.29 C ANISOU 1195 C AGLN A 157 7308 5628 8073 1281 -1372 -285 C ATOM 1196 O AGLN A 157 -34.394 23.777 17.148 1.00 55.70 O ANISOU 1196 O AGLN A 157 7273 5801 8090 1320 -1395 -282 O ATOM 1197 CB AGLN A 157 -31.647 22.965 17.202 1.00 59.45 C ANISOU 1197 CB AGLN A 157 7887 6297 8403 996 -1153 -140 C ATOM 1198 CG AGLN A 157 -30.265 22.674 16.647 1.00 68.74 C ANISOU 1198 CG AGLN A 157 9176 7439 9502 832 -1063 -17 C ATOM 1199 CD AGLN A 157 -30.011 21.190 16.497 1.00 77.51 C ANISOU 1199 CD AGLN A 157 10222 8731 10498 744 -956 16 C ATOM 1200 OE1AGLN A 157 -30.940 20.387 16.554 1.00 81.43 O ANISOU 1200 OE1AGLN A 157 10616 9360 10964 797 -967 -25 O ATOM 1201 NE2AGLN A 157 -28.751 20.817 16.305 1.00 81.63 N ANISOU 1201 NE2AGLN A 157 10796 9252 10966 608 -852 86 N ATOM 1202 N GLY A 158 -33.795 25.563 18.372 1.00 54.56 N ANISOU 1202 N GLY A 158 7186 5449 8095 1384 -1413 -408 N ATOM 1203 CA GLY A 158 -35.146 25.741 18.859 1.00 54.50 C ANISOU 1203 CA GLY A 158 7034 5496 8176 1554 -1475 -542 C ATOM 1204 C GLY A 158 -35.603 24.692 19.841 1.00 53.71 C ANISOU 1204 C GLY A 158 6737 5629 8040 1554 -1348 -656 C ATOM 1205 O GLY A 158 -36.809 24.485 19.995 1.00 59.43 O ANISOU 1205 O GLY A 158 7318 6441 8821 1668 -1378 -739 O ATOM 1206 N CYS A 159 -34.673 24.019 20.512 1.00 48.74 N ANISOU 1206 N CYS A 159 6096 5099 7323 1428 -1207 -661 N ATOM 1207 CA CYS A 159 -35.045 22.975 21.453 1.00 51.24 C ANISOU 1207 CA CYS A 159 6250 5631 7588 1416 -1080 -753 C ATOM 1208 C CYS A 159 -35.798 23.560 22.639 1.00 53.59 C ANISOU 1208 C CYS A 159 6438 5957 7969 1552 -1062 -936 C ATOM 1209 O CYS A 159 -35.614 24.721 23.013 1.00 53.45 O ANISOU 1209 O CYS A 159 6485 5794 8029 1623 -1118 -1006 O ATOM 1210 CB CYS A 159 -33.819 22.210 21.946 1.00 49.93 C ANISOU 1210 CB CYS A 159 6115 5544 7312 1263 -952 -718 C ATOM 1211 SG CYS A 159 -32.992 21.269 20.656 1.00 49.62 S ANISOU 1211 SG CYS A 159 6171 5517 7166 1106 -933 -525 S ATOM 1212 N GLY A 160 -36.651 22.734 23.237 1.00 55.50 N ANISOU 1212 N GLY A 160 6512 6383 8192 1585 -973 -1017 N ATOM 1213 CA GLY A 160 -37.432 23.163 24.372 1.00 54.51 C ANISOU 1213 CA GLY A 160 6269 6311 8131 1712 -926 -1195 C ATOM 1214 C GLY A 160 -36.631 23.110 25.653 1.00 59.89 C ANISOU 1214 C GLY A 160 6979 7046 8731 1660 -806 -1279 C ATOM 1215 O GLY A 160 -35.457 22.740 25.682 1.00 60.02 O ANISOU 1215 O GLY A 160 7093 7057 8656 1527 -769 -1201 O ATOM 1216 N GLU A 161 -37.288 23.493 26.742 1.00 66.81 N ANISOU 1216 N GLU A 161 7766 7977 9642 1773 -746 -1448 N ATOM 1217 CA GLU A 161 -36.611 23.515 28.028 1.00 75.22 C ANISOU 1217 CA GLU A 161 8871 9092 10618 1743 -645 -1545 C ATOM 1218 C GLU A 161 -36.349 22.090 28.499 1.00 70.07 C ANISOU 1218 C GLU A 161 8169 8636 9818 1619 -500 -1499 C ATOM 1219 O GLU A 161 -37.213 21.215 28.391 1.00 69.85 O ANISOU 1219 O GLU A 161 8011 8751 9780 1618 -429 -1484 O ATOM 1220 CB GLU A 161 -37.467 24.262 29.054 1.00 90.13 C ANISOU 1220 CB GLU A 161 10682 10996 12567 1905 -608 -1746 C ATOM 1221 CG GLU A 161 -37.248 25.787 29.164 1.00102.83 C ANISOU 1221 CG GLU A 161 12394 12392 14285 2013 -729 -1837 C ATOM 1222 CD GLU A 161 -35.807 26.277 29.020 1.00110.88 C ANISOU 1222 CD GLU A 161 13595 13255 15278 1906 -804 -1768 C ATOM 1223 OE1 GLU A 161 -34.841 25.515 29.235 1.00112.72 O ANISOU 1223 OE1 GLU A 161 13877 13561 15391 1760 -741 -1695 O ATOM 1224 OE2 GLU A 161 -35.649 27.464 28.665 1.00115.43 O ANISOU 1224 OE2 GLU A 161 14265 13624 15969 1969 -932 -1785 O ATOM 1225 N GLY A 162 -35.148 21.852 29.025 1.00 66.48 N ANISOU 1225 N GLY A 162 7817 8184 9259 1515 -465 -1475 N ATOM 1226 CA GLY A 162 -34.765 20.504 29.387 1.00 56.16 C ANISOU 1226 CA GLY A 162 6487 7038 7813 1395 -349 -1412 C ATOM 1227 C GLY A 162 -34.370 19.611 28.230 1.00 55.57 C ANISOU 1227 C GLY A 162 6427 6971 7716 1275 -373 -1237 C ATOM 1228 O GLY A 162 -34.116 18.420 28.452 1.00 59.99 O ANISOU 1228 O GLY A 162 6964 7659 8171 1179 -283 -1180 O ATOM 1229 N GLN A 163 -34.306 20.137 27.010 1.00 51.64 N ANISOU 1229 N GLN A 163 5978 6337 7305 1279 -491 -1149 N ATOM 1230 CA GLN A 163 -33.933 19.363 25.835 1.00 48.16 C ANISOU 1230 CA GLN A 163 5568 5896 6834 1173 -515 -989 C ATOM 1231 C GLN A 163 -32.546 19.737 25.330 1.00 44.61 C ANISOU 1231 C GLN A 163 5262 5314 6375 1079 -567 -897 C ATOM 1232 O GLN A 163 -32.056 20.849 25.549 1.00 49.53 O ANISOU 1232 O GLN A 163 5962 5799 7057 1110 -628 -943 O ATOM 1233 CB GLN A 163 -34.939 19.565 24.698 1.00 46.95 C ANISOU 1233 CB GLN A 163 5373 5698 6770 1241 -609 -943 C ATOM 1234 CG GLN A 163 -36.334 19.050 24.977 1.00 47.53 C ANISOU 1234 CG GLN A 163 5277 5908 6876 1316 -562 -1016 C ATOM 1235 CD GLN A 163 -37.209 19.091 23.739 1.00 49.78 C ANISOU 1235 CD GLN A 163 5521 6151 7243 1366 -677 -956 C ATOM 1236 OE1 GLN A 163 -37.082 19.990 22.905 1.00 51.13 O ANISOU 1236 OE1 GLN A 163 5788 6163 7475 1412 -810 -909 O ATOM 1237 NE2 GLN A 163 -38.098 18.114 23.608 1.00 51.38 N ANISOU 1237 NE2 GLN A 163 5588 6490 7446 1354 -634 -955 N ATOM 1238 N VAL A 164 -31.920 18.776 24.652 1.00 35.71 N ANISOU 1238 N VAL A 164 4163 4228 5178 961 -536 -772 N ATOM 1239 CA VAL A 164 -30.637 18.956 23.991 1.00 36.96 C ANISOU 1239 CA VAL A 164 4437 4278 5329 859 -564 -669 C ATOM 1240 C VAL A 164 -30.785 18.519 22.541 1.00 35.55 C ANISOU 1240 C VAL A 164 4295 4076 5138 816 -599 -533 C ATOM 1241 O VAL A 164 -31.704 17.780 22.179 1.00 32.92 O ANISOU 1241 O VAL A 164 3889 3838 4781 840 -592 -517 O ATOM 1242 CB VAL A 164 -29.509 18.150 24.671 1.00 35.60 C ANISOU 1242 CB VAL A 164 4270 4183 5071 753 -480 -660 C ATOM 1243 CG1 VAL A 164 -29.321 18.601 26.104 1.00 39.74 C ANISOU 1243 CG1 VAL A 164 4782 4727 5590 797 -462 -797 C ATOM 1244 CG2 VAL A 164 -29.811 16.659 24.611 1.00 34.03 C ANISOU 1244 CG2 VAL A 164 4005 4146 4781 703 -399 -612 C ATOM 1245 N ALA A 165 -29.868 18.993 21.703 1.00 35.43 N ANISOU 1245 N ALA A 165 4395 3930 5137 749 -636 -436 N ATOM 1246 CA ALA A 165 -29.684 18.384 20.393 1.00 38.88 C ANISOU 1246 CA ALA A 165 4891 4361 5520 680 -638 -300 C ATOM 1247 C ALA A 165 -29.142 16.975 20.591 1.00 39.29 C ANISOU 1247 C ALA A 165 4895 4554 5477 584 -534 -271 C ATOM 1248 O ALA A 165 -28.065 16.794 21.170 1.00 36.92 O ANISOU 1248 O ALA A 165 4603 4264 5161 513 -474 -280 O ATOM 1249 CB ALA A 165 -28.736 19.222 19.540 1.00 39.56 C ANISOU 1249 CB ALA A 165 5118 4278 5636 619 -673 -204 C ATOM 1250 N CYS A 166 -29.880 15.976 20.114 1.00 39.05 N ANISOU 1250 N CYS A 166 4817 4626 5394 585 -522 -239 N ATOM 1251 CA CYS A 166 -29.552 14.585 20.419 1.00 35.94 C ANISOU 1251 CA CYS A 166 4370 4367 4919 510 -428 -225 C ATOM 1252 C CYS A 166 -28.448 14.116 19.482 1.00 36.05 C ANISOU 1252 C CYS A 166 4474 4343 4879 406 -394 -115 C ATOM 1253 O CYS A 166 -28.701 13.738 18.335 1.00 35.61 O ANISOU 1253 O CYS A 166 4469 4277 4784 389 -418 -37 O ATOM 1254 CB CYS A 166 -30.782 13.695 20.312 1.00 37.55 C ANISOU 1254 CB CYS A 166 4483 4686 5101 543 -428 -242 C ATOM 1255 SG CYS A 166 -30.428 11.997 20.794 1.00 41.76 S ANISOU 1255 SG CYS A 166 4960 5366 5542 452 -316 -227 S ATOM 1256 N LEU A 167 -27.214 14.157 19.977 1.00 30.27 N ANISOU 1256 N LEU A 167 3761 3591 4150 341 -340 -117 N ATOM 1257 CA LEU A 167 -26.028 13.736 19.247 1.00 30.84 C ANISOU 1257 CA LEU A 167 3895 3633 4189 242 -286 -29 C ATOM 1258 C LEU A 167 -25.209 12.819 20.139 1.00 30.78 C ANISOU 1258 C LEU A 167 3826 3716 4153 190 -212 -61 C ATOM 1259 O LEU A 167 -25.028 13.114 21.326 1.00 30.32 O ANISOU 1259 O LEU A 167 3721 3675 4122 212 -215 -143 O ATOM 1260 CB LEU A 167 -25.191 14.939 18.804 1.00 30.25 C ANISOU 1260 CB LEU A 167 3908 3407 4179 210 -306 11 C ATOM 1261 CG LEU A 167 -25.836 15.865 17.773 1.00 33.31 C ANISOU 1261 CG LEU A 167 4391 3679 4585 253 -385 69 C ATOM 1262 CD1 LEU A 167 -25.032 17.144 17.629 1.00 36.91 C ANISOU 1262 CD1 LEU A 167 4929 3975 5121 220 -403 96 C ATOM 1263 CD2 LEU A 167 -25.949 15.152 16.434 1.00 29.78 C ANISOU 1263 CD2 LEU A 167 4017 3250 4048 217 -369 172 C ATOM 1264 N PHE A 168 -24.743 11.699 19.573 1.00 30.41 N ANISOU 1264 N PHE A 168 3786 3722 4046 128 -153 -1 N ATOM 1265 CA PHE A 168 -24.076 10.668 20.365 1.00 26.71 C ANISOU 1265 CA PHE A 168 3261 3341 3548 90 -94 -26 C ATOM 1266 C PHE A 168 -22.965 11.256 21.224 1.00 30.38 C ANISOU 1266 C PHE A 168 3708 3763 4072 66 -94 -71 C ATOM 1267 O PHE A 168 -22.930 11.048 22.442 1.00 29.23 O ANISOU 1267 O PHE A 168 3514 3675 3916 90 -100 -142 O ATOM 1268 CB PHE A 168 -23.516 9.570 19.456 1.00 29.38 C ANISOU 1268 CB PHE A 168 3625 3706 3833 27 -35 47 C ATOM 1269 CG PHE A 168 -22.972 8.383 20.208 1.00 23.80 C ANISOU 1269 CG PHE A 168 2863 3084 3095 1 12 26 C ATOM 1270 CD1 PHE A 168 -21.643 8.354 20.613 1.00 25.53 C ANISOU 1270 CD1 PHE A 168 3063 3283 3355 -40 40 18 C ATOM 1271 CD2 PHE A 168 -23.785 7.306 20.519 1.00 28.07 C ANISOU 1271 CD2 PHE A 168 3371 3717 3576 17 21 16 C ATOM 1272 CE1 PHE A 168 -21.135 7.272 21.311 1.00 26.53 C ANISOU 1272 CE1 PHE A 168 3146 3478 3454 -52 65 0 C ATOM 1273 CE2 PHE A 168 -23.284 6.217 21.217 1.00 29.94 C ANISOU 1273 CE2 PHE A 168 3576 4018 3782 -5 57 6 C ATOM 1274 CZ PHE A 168 -21.957 6.201 21.614 1.00 28.69 C ANISOU 1274 CZ PHE A 168 3407 3836 3656 -34 73 -1 C ATOM 1275 N GLU A 169 -22.040 11.988 20.607 1.00 28.40 N ANISOU 1275 N GLU A 169 3501 3408 3882 16 -87 -30 N ATOM 1276 CA GLU A 169 -20.873 12.440 21.350 1.00 26.91 C ANISOU 1276 CA GLU A 169 3281 3177 3767 -22 -90 -74 C ATOM 1277 C GLU A 169 -21.181 13.608 22.281 1.00 29.66 C ANISOU 1277 C GLU A 169 3627 3471 4172 30 -164 -161 C ATOM 1278 O GLU A 169 -20.323 13.972 23.092 1.00 35.60 O ANISOU 1278 O GLU A 169 4350 4195 4981 8 -188 -219 O ATOM 1279 CB GLU A 169 -19.755 12.816 20.371 1.00 26.51 C ANISOU 1279 CB GLU A 169 3264 3033 3777 -107 -43 -2 C ATOM 1280 CG GLU A 169 -19.236 11.626 19.569 1.00 29.11 C ANISOU 1280 CG GLU A 169 3587 3419 4053 -157 43 64 C ATOM 1281 CD GLU A 169 -17.995 11.946 18.755 1.00 37.89 C ANISOU 1281 CD GLU A 169 4713 4453 5232 -245 116 122 C ATOM 1282 OE1 GLU A 169 -17.437 13.050 18.913 1.00 41.02 O ANISOU 1282 OE1 GLU A 169 5110 4749 5726 -281 97 111 O ATOM 1283 OE2 GLU A 169 -17.578 11.089 17.949 1.00 37.95 O ANISOU 1283 OE2 GLU A 169 4728 4495 5195 -282 198 175 O ATOM 1284 N ASP A 170 -22.372 14.204 22.186 1.00 31.47 N ANISOU 1284 N ASP A 170 3884 3680 4394 103 -209 -180 N ATOM 1285 CA ASP A 170 -22.767 15.231 23.147 1.00 33.76 C ANISOU 1285 CA ASP A 170 4170 3927 4731 170 -274 -280 C ATOM 1286 C ASP A 170 -23.321 14.649 24.444 1.00 29.43 C ANISOU 1286 C ASP A 170 3564 3502 4116 229 -270 -374 C ATOM 1287 O ASP A 170 -23.245 15.309 25.485 1.00 33.38 O ANISOU 1287 O ASP A 170 4061 3984 4639 268 -311 -473 O ATOM 1288 CB ASP A 170 -23.791 16.193 22.538 1.00 36.99 C ANISOU 1288 CB ASP A 170 4628 4252 5176 236 -329 -271 C ATOM 1289 CG ASP A 170 -23.192 17.083 21.465 1.00 41.74 C ANISOU 1289 CG ASP A 170 5312 4699 5846 182 -346 -188 C ATOM 1290 OD1 ASP A 170 -21.959 17.033 21.270 1.00 40.20 O ANISOU 1290 OD1 ASP A 170 5124 4465 5687 87 -305 -149 O ATOM 1291 OD2 ASP A 170 -23.949 17.855 20.838 1.00 38.45 O ANISOU 1291 OD2 ASP A 170 4956 4198 5456 234 -401 -162 O ATOM 1292 N VAL A 171 -23.884 13.440 24.418 1.00 25.61 N ANISOU 1292 N VAL A 171 3046 3141 3545 233 -219 -346 N ATOM 1293 CA VAL A 171 -24.516 12.886 25.605 1.00 31.00 C ANISOU 1293 CA VAL A 171 3685 3938 4155 283 -199 -421 C ATOM 1294 C VAL A 171 -23.732 11.729 26.218 1.00 28.06 C ANISOU 1294 C VAL A 171 3296 3649 3716 233 -161 -409 C ATOM 1295 O VAL A 171 -23.779 11.554 27.442 1.00 30.16 O ANISOU 1295 O VAL A 171 3555 3978 3925 264 -161 -481 O ATOM 1296 CB VAL A 171 -25.972 12.457 25.312 1.00 34.97 C ANISOU 1296 CB VAL A 171 4152 4515 4621 334 -173 -413 C ATOM 1297 CG1 VAL A 171 -26.787 13.646 24.822 1.00 38.29 C ANISOU 1297 CG1 VAL A 171 4583 4850 5115 403 -231 -438 C ATOM 1298 CG2 VAL A 171 -26.015 11.316 24.298 1.00 28.19 C ANISOU 1298 CG2 VAL A 171 3289 3698 3722 277 -135 -312 C ATOM 1299 N VAL A 172 -23.019 10.937 25.426 1.00 28.03 N ANISOU 1299 N VAL A 172 3294 3645 3710 165 -131 -324 N ATOM 1300 CA VAL A 172 -22.265 9.798 25.940 1.00 27.74 C ANISOU 1300 CA VAL A 172 3243 3677 3622 128 -105 -309 C ATOM 1301 C VAL A 172 -20.837 10.266 26.204 1.00 29.89 C ANISOU 1301 C VAL A 172 3512 3880 3966 89 -145 -331 C ATOM 1302 O VAL A 172 -20.178 10.753 25.272 1.00 26.77 O ANISOU 1302 O VAL A 172 3121 3398 3652 41 -141 -287 O ATOM 1303 CB VAL A 172 -22.282 8.614 24.965 1.00 28.38 C ANISOU 1303 CB VAL A 172 3320 3793 3670 84 -50 -219 C ATOM 1304 CG1 VAL A 172 -21.613 7.402 25.596 1.00 26.98 C ANISOU 1304 CG1 VAL A 172 3131 3681 3442 60 -32 -209 C ATOM 1305 CG2 VAL A 172 -23.712 8.279 24.560 1.00 25.55 C ANISOU 1305 CG2 VAL A 172 2955 3486 3267 113 -27 -201 C ATOM 1306 N PRO A 173 -20.329 10.147 27.431 1.00 31.58 N ANISOU 1306 N PRO A 173 3720 4127 4152 105 -185 -397 N ATOM 1307 CA PRO A 173 -18.971 10.626 27.711 1.00 28.46 C ANISOU 1307 CA PRO A 173 3307 3663 3843 68 -242 -430 C ATOM 1308 C PRO A 173 -17.944 9.775 26.984 1.00 27.38 C ANISOU 1308 C PRO A 173 3132 3523 3749 4 -207 -357 C ATOM 1309 O PRO A 173 -18.098 8.558 26.858 1.00 27.12 O ANISOU 1309 O PRO A 173 3096 3563 3646 4 -164 -310 O ATOM 1310 CB PRO A 173 -18.844 10.481 29.234 1.00 24.74 C ANISOU 1310 CB PRO A 173 2852 3248 3301 112 -303 -517 C ATOM 1311 CG PRO A 173 -20.247 10.392 29.732 1.00 28.36 C ANISOU 1311 CG PRO A 173 3343 3781 3650 176 -266 -544 C ATOM 1312 CD PRO A 173 -21.006 9.682 28.650 1.00 25.25 C ANISOU 1312 CD PRO A 173 2934 3421 3240 158 -185 -452 C ATOM 1313 N AMET A 174 -16.878 10.420 26.512 0.70 25.59 N ANISOU 1313 N AMET A 174 2872 3207 3645 -51 -221 -354 N ATOM 1314 N BMET A 174 -16.889 10.435 26.498 0.30 25.61 N ANISOU 1314 N BMET A 174 2875 3208 3648 -51 -221 -353 N ATOM 1315 CA AMET A 174 -15.872 9.671 25.769 0.70 24.70 C ANISOU 1315 CA AMET A 174 2710 3091 3585 -108 -171 -294 C ATOM 1316 CA BMET A 174 -15.839 9.722 25.778 0.30 25.11 C ANISOU 1316 CA BMET A 174 2760 3139 3642 -109 -173 -296 C ATOM 1317 C AMET A 174 -14.967 8.853 26.686 0.70 23.97 C ANISOU 1317 C AMET A 174 2567 3046 3493 -99 -224 -332 C ATOM 1318 C BMET A 174 -15.022 8.831 26.702 0.30 24.13 C ANISOU 1318 C BMET A 174 2592 3070 3508 -96 -224 -331 C ATOM 1319 O AMET A 174 -14.402 7.846 26.245 0.70 25.91 O ANISOU 1319 O AMET A 174 2777 3320 3747 -117 -181 -286 O ATOM 1320 O BMET A 174 -14.565 7.763 26.281 0.30 24.30 O ANISOU 1320 O BMET A 174 2582 3126 3523 -110 -179 -284 O ATOM 1321 CB AMET A 174 -15.044 10.615 24.895 0.70 28.45 C ANISOU 1321 CB AMET A 174 3158 3456 4197 -180 -146 -270 C ATOM 1322 CB BMET A 174 -14.922 10.711 25.058 0.30 28.28 C ANISOU 1322 CB BMET A 174 3129 3428 4187 -180 -160 -283 C ATOM 1323 CG AMET A 174 -14.378 9.918 23.720 0.70 30.52 C ANISOU 1323 CG AMET A 174 3389 3717 4492 -236 -46 -190 C ATOM 1324 CG BMET A 174 -15.587 11.443 23.913 0.30 29.42 C ANISOU 1324 CG BMET A 174 3334 3507 4337 -201 -103 -220 C ATOM 1325 SD AMET A 174 -15.546 9.067 22.638 0.70 32.12 S ANISOU 1325 SD AMET A 174 3667 3976 4561 -214 40 -102 S ATOM 1326 SD BMET A 174 -16.156 10.335 22.613 0.30 35.87 S ANISOU 1326 SD BMET A 174 4189 4382 5057 -205 3 -115 S ATOM 1327 CE AMET A 174 -15.971 10.374 21.490 0.70 34.97 C ANISOU 1327 CE AMET A 174 4099 4230 4956 -249 73 -48 C ATOM 1328 CE BMET A 174 -14.594 9.692 22.025 0.30 33.90 C ANISOU 1328 CE BMET A 174 3863 4123 4894 -280 79 -83 C ATOM 1329 N ASN A 175 -14.822 9.248 27.955 1.00 24.74 N ANISOU 1329 N ASN A 175 2672 3150 3578 -63 -324 -418 N ATOM 1330 CA ASN A 175 -14.060 8.417 28.885 1.00 27.13 C ANISOU 1330 CA ASN A 175 2947 3500 3859 -41 -395 -451 C ATOM 1331 C ASN A 175 -14.789 7.106 29.157 1.00 24.34 C ANISOU 1331 C ASN A 175 2645 3243 3358 1 -358 -405 C ATOM 1332 O ASN A 175 -14.151 6.060 29.328 1.00 27.25 O ANISOU 1332 O ASN A 175 2990 3643 3721 7 -376 -383 O ATOM 1333 CB ASN A 175 -13.754 9.170 30.186 1.00 29.96 C ANISOU 1333 CB ASN A 175 3322 3841 4221 -10 -522 -558 C ATOM 1334 CG ASN A 175 -14.972 9.835 30.798 1.00 32.98 C ANISOU 1334 CG ASN A 175 3791 4243 4497 42 -528 -607 C ATOM 1335 OD1 ASN A 175 -16.111 9.471 30.513 1.00 35.50 O ANISOU 1335 OD1 ASN A 175 4154 4615 4719 67 -447 -562 O ATOM 1336 ND2 ASN A 175 -14.728 10.813 31.666 1.00 32.04 N ANISOU 1336 ND2 ASN A 175 3691 4079 4403 61 -628 -709 N ATOM 1337 N TYR A 176 -16.124 7.143 29.214 1.00 21.37 N ANISOU 1337 N TYR A 176 2334 2912 2876 31 -311 -393 N ATOM 1338 CA TYR A 176 -16.885 5.897 29.220 1.00 21.11 C ANISOU 1338 CA TYR A 176 2338 2958 2725 49 -254 -335 C ATOM 1339 C TYR A 176 -16.590 5.072 27.974 1.00 27.23 C ANISOU 1339 C TYR A 176 3080 3722 3545 9 -181 -253 C ATOM 1340 O TYR A 176 -16.300 3.873 28.062 1.00 25.78 O ANISOU 1340 O TYR A 176 2899 3572 3326 13 -175 -217 O ATOM 1341 CB TYR A 176 -18.388 6.178 29.315 1.00 22.52 C ANISOU 1341 CB TYR A 176 2563 3179 2814 78 -203 -339 C ATOM 1342 CG TYR A 176 -19.223 4.944 29.034 1.00 26.19 C ANISOU 1342 CG TYR A 176 3049 3712 3191 74 -130 -269 C ATOM 1343 CD1 TYR A 176 -19.496 4.017 30.032 1.00 27.11 C ANISOU 1343 CD1 TYR A 176 3211 3897 3194 95 -132 -264 C ATOM 1344 CD2 TYR A 176 -19.716 4.693 27.756 1.00 20.35 C ANISOU 1344 CD2 TYR A 176 2293 2959 2480 44 -63 -208 C ATOM 1345 CE1 TYR A 176 -20.243 2.882 29.765 1.00 21.72 C ANISOU 1345 CE1 TYR A 176 2546 3262 2445 79 -65 -198 C ATOM 1346 CE2 TYR A 176 -20.459 3.563 27.482 1.00 23.31 C ANISOU 1346 CE2 TYR A 176 2684 3386 2788 34 -8 -152 C ATOM 1347 CZ TYR A 176 -20.720 2.660 28.488 1.00 24.35 C ANISOU 1347 CZ TYR A 176 2850 3579 2824 47 -6 -148 C ATOM 1348 OH TYR A 176 -21.468 1.536 28.218 1.00 33.32 O ANISOU 1348 OH TYR A 176 4001 4754 3905 26 50 -91 O ATOM 1349 N MET A 177 -16.682 5.699 26.798 1.00 27.84 N ANISOU 1349 N MET A 177 3139 3747 3693 -27 -126 -224 N ATOM 1350 CA MET A 177 -16.545 4.955 25.549 1.00 25.28 C ANISOU 1350 CA MET A 177 2804 3416 3385 -61 -47 -152 C ATOM 1351 C MET A 177 -15.159 4.339 25.405 1.00 24.57 C ANISOU 1351 C MET A 177 2653 3307 3375 -81 -50 -148 C ATOM 1352 O MET A 177 -15.020 3.232 24.874 1.00 26.46 O ANISOU 1352 O MET A 177 2891 3567 3593 -83 -3 -104 O ATOM 1353 CB MET A 177 -16.851 5.869 24.361 1.00 20.26 C ANISOU 1353 CB MET A 177 2180 2722 2796 -94 4 -121 C ATOM 1354 CG MET A 177 -18.320 6.217 24.197 1.00 20.78 C ANISOU 1354 CG MET A 177 2297 2808 2789 -66 13 -112 C ATOM 1355 SD MET A 177 -19.354 4.746 24.058 1.00 25.61 S ANISOU 1355 SD MET A 177 2937 3507 3288 -51 54 -69 S ATOM 1356 CE MET A 177 -18.765 4.061 22.511 1.00 24.42 C ANISOU 1356 CE MET A 177 2794 3324 3162 -97 123 0 C ATOM 1357 N VAL A 178 -14.124 5.033 25.870 1.00 22.43 N ANISOU 1357 N VAL A 178 2323 2993 3206 -93 -109 -199 N ATOM 1358 CA VAL A 178 -12.753 4.554 25.691 1.00 25.57 C ANISOU 1358 CA VAL A 178 2635 3369 3711 -111 -113 -205 C ATOM 1359 C VAL A 178 -12.323 3.624 26.820 1.00 24.74 C ANISOU 1359 C VAL A 178 2522 3306 3572 -59 -206 -234 C ATOM 1360 O VAL A 178 -11.901 2.491 26.575 1.00 25.30 O ANISOU 1360 O VAL A 178 2573 3394 3647 -43 -186 -206 O ATOM 1361 CB VAL A 178 -11.792 5.752 25.540 1.00 24.04 C ANISOU 1361 CB VAL A 178 2364 3101 3671 -161 -130 -245 C ATOM 1362 CG1 VAL A 178 -10.349 5.278 25.547 1.00 22.57 C ANISOU 1362 CG1 VAL A 178 2061 2899 3615 -175 -147 -269 C ATOM 1363 CG2 VAL A 178 -12.098 6.505 24.256 1.00 24.55 C ANISOU 1363 CG2 VAL A 178 2451 3113 3765 -218 -25 -194 C ATOM 1364 N TYR A 179 -12.426 4.069 28.077 1.00 25.95 N ANISOU 1364 N TYR A 179 2703 3472 3684 -26 -313 -293 N ATOM 1365 CA TYR A 179 -11.886 3.278 29.181 1.00 27.83 C ANISOU 1365 CA TYR A 179 2947 3740 3888 25 -421 -319 C ATOM 1366 C TYR A 179 -12.816 2.141 29.575 1.00 25.95 C ANISOU 1366 C TYR A 179 2809 3565 3488 63 -400 -268 C ATOM 1367 O TYR A 179 -12.362 1.010 29.788 1.00 31.62 O ANISOU 1367 O TYR A 179 3530 4292 4191 92 -431 -242 O ATOM 1368 CB TYR A 179 -11.607 4.151 30.408 1.00 25.09 C ANISOU 1368 CB TYR A 179 2612 3383 3539 48 -552 -406 C ATOM 1369 CG TYR A 179 -10.471 5.136 30.275 1.00 28.59 C ANISOU 1369 CG TYR A 179 2945 3756 4163 8 -609 -469 C ATOM 1370 CD1 TYR A 179 -9.263 4.761 29.698 1.00 32.11 C ANISOU 1370 CD1 TYR A 179 3268 4170 4764 -17 -602 -464 C ATOM 1371 CD2 TYR A 179 -10.585 6.428 30.771 1.00 28.75 C ANISOU 1371 CD2 TYR A 179 2979 3737 4206 -4 -669 -540 C ATOM 1372 CE1 TYR A 179 -8.213 5.655 29.592 1.00 31.44 C ANISOU 1372 CE1 TYR A 179 3066 4019 4860 -66 -646 -523 C ATOM 1373 CE2 TYR A 179 -9.541 7.327 30.671 1.00 29.76 C ANISOU 1373 CE2 TYR A 179 3005 3790 4513 -53 -725 -598 C ATOM 1374 CZ TYR A 179 -8.357 6.935 30.080 1.00 32.27 C ANISOU 1374 CZ TYR A 179 3190 4080 4990 -89 -711 -587 C ATOM 1375 OH TYR A 179 -7.313 7.828 29.984 1.00 35.50 O ANISOU 1375 OH TYR A 179 3481 4414 5593 -149 -758 -646 O ATOM 1376 N PHE A 180 -14.113 2.416 29.675 1.00 25.85 N ANISOU 1376 N PHE A 180 2873 3588 3362 63 -349 -253 N ATOM 1377 CA PHE A 180 -15.047 1.425 30.190 1.00 29.88 C ANISOU 1377 CA PHE A 180 3473 4157 3722 88 -325 -209 C ATOM 1378 C PHE A 180 -15.528 0.517 29.063 1.00 28.16 C ANISOU 1378 C PHE A 180 3255 3942 3501 61 -222 -134 C ATOM 1379 O PHE A 180 -15.379 -0.707 29.137 1.00 33.12 O ANISOU 1379 O PHE A 180 3911 4579 4096 73 -224 -90 O ATOM 1380 CB PHE A 180 -16.217 2.143 30.877 1.00 28.17 C ANISOU 1380 CB PHE A 180 3321 3982 3398 102 -311 -240 C ATOM 1381 CG PHE A 180 -17.123 1.238 31.667 1.00 30.70 C ANISOU 1381 CG PHE A 180 3733 4369 3563 122 -286 -203 C ATOM 1382 CD1 PHE A 180 -18.163 0.558 31.053 1.00 26.70 C ANISOU 1382 CD1 PHE A 180 3243 3891 3011 95 -185 -140 C ATOM 1383 CD2 PHE A 180 -16.950 1.091 33.035 1.00 35.40 C ANISOU 1383 CD2 PHE A 180 4403 4994 4052 162 -364 -233 C ATOM 1384 CE1 PHE A 180 -19.005 -0.266 31.784 1.00 31.98 C ANISOU 1384 CE1 PHE A 180 3988 4615 3547 99 -149 -103 C ATOM 1385 CE2 PHE A 180 -17.787 0.268 33.772 1.00 33.25 C ANISOU 1385 CE2 PHE A 180 4227 4779 3627 171 -324 -190 C ATOM 1386 CZ PHE A 180 -18.816 -0.411 33.144 1.00 27.91 C ANISOU 1386 CZ PHE A 180 3553 4130 2922 134 -210 -123 C ATOM 1387 N ASN A 181 -16.108 1.104 28.014 1.00 23.88 N ANISOU 1387 N ASN A 181 2692 3387 2993 26 -142 -120 N ATOM 1388 CA ASN A 181 -16.670 0.295 26.937 1.00 28.03 C ANISOU 1388 CA ASN A 181 3231 3917 3501 1 -56 -58 C ATOM 1389 C ASN A 181 -15.580 -0.377 26.109 1.00 33.07 C ANISOU 1389 C ASN A 181 3822 4515 4227 -9 -36 -39 C ATOM 1390 O ASN A 181 -15.585 -1.602 25.940 1.00 36.72 O ANISOU 1390 O ASN A 181 4310 4981 4659 -1 -20 -2 O ATOM 1391 CB ASN A 181 -17.579 1.137 26.045 1.00 26.70 C ANISOU 1391 CB ASN A 181 3065 3743 3337 -24 4 -50 C ATOM 1392 CG ASN A 181 -18.401 0.285 25.102 1.00 30.62 C ANISOU 1392 CG ASN A 181 3590 4253 3790 -45 71 4 C ATOM 1393 OD1 ASN A 181 -17.997 0.029 23.969 1.00 33.62 O ANISOU 1393 OD1 ASN A 181 3960 4600 4214 -68 115 30 O ATOM 1394 ND2 ASN A 181 -19.548 -0.186 25.577 1.00 27.78 N ANISOU 1394 ND2 ASN A 181 3268 3943 3345 -41 82 18 N ATOM 1395 N PHE A 182 -14.628 0.403 25.591 1.00 26.53 N ANISOU 1395 N PHE A 182 2924 3644 3514 -27 -31 -66 N ATOM 1396 CA PHE A 182 -13.642 -0.167 24.677 1.00 26.53 C ANISOU 1396 CA PHE A 182 2868 3610 3601 -39 18 -53 C ATOM 1397 C PHE A 182 -12.633 -1.021 25.433 1.00 28.18 C ANISOU 1397 C PHE A 182 3038 3815 3854 5 -57 -74 C ATOM 1398 O PHE A 182 -12.546 -2.235 25.213 1.00 31.76 O ANISOU 1398 O PHE A 182 3511 4268 4287 28 -42 -47 O ATOM 1399 CB PHE A 182 -12.944 0.945 23.887 1.00 27.32 C ANISOU 1399 CB PHE A 182 2901 3664 3815 -82 65 -70 C ATOM 1400 CG PHE A 182 -11.980 0.438 22.841 1.00 31.82 C ANISOU 1400 CG PHE A 182 3412 4207 4472 -99 148 -59 C ATOM 1401 CD1 PHE A 182 -12.232 -0.746 22.164 1.00 30.78 C ANISOU 1401 CD1 PHE A 182 3321 4088 4285 -84 207 -26 C ATOM 1402 CD2 PHE A 182 -10.839 1.158 22.519 1.00 30.49 C ANISOU 1402 CD2 PHE A 182 3144 3997 4442 -134 175 -87 C ATOM 1403 CE1 PHE A 182 -11.356 -1.215 21.199 1.00 26.09 C ANISOU 1403 CE1 PHE A 182 2678 3472 3763 -92 294 -27 C ATOM 1404 CE2 PHE A 182 -9.956 0.697 21.552 1.00 32.46 C ANISOU 1404 CE2 PHE A 182 3331 4229 4772 -149 274 -82 C ATOM 1405 CZ PHE A 182 -10.217 -0.492 20.890 1.00 32.87 C ANISOU 1405 CZ PHE A 182 3433 4299 4757 -123 335 -55 C ATOM 1406 N PHE A 183 -11.844 -0.406 26.317 1.00 25.92 N ANISOU 1406 N PHE A 183 2696 3517 3634 20 -152 -127 N ATOM 1407 CA PHE A 183 -10.744 -1.140 26.936 1.00 28.07 C ANISOU 1407 CA PHE A 183 2916 3778 3973 67 -241 -153 C ATOM 1408 C PHE A 183 -11.268 -2.295 27.784 1.00 27.82 C ANISOU 1408 C PHE A 183 2984 3773 3814 117 -301 -118 C ATOM 1409 O PHE A 183 -10.868 -3.450 27.597 1.00 28.64 O ANISOU 1409 O PHE A 183 3086 3859 3935 150 -304 -95 O ATOM 1410 CB PHE A 183 -9.880 -0.202 27.785 1.00 25.30 C ANISOU 1410 CB PHE A 183 2492 3409 3713 73 -353 -224 C ATOM 1411 CG PHE A 183 -9.015 0.739 26.982 1.00 30.59 C ANISOU 1411 CG PHE A 183 3039 4036 4550 19 -300 -257 C ATOM 1412 CD1 PHE A 183 -9.031 0.721 25.597 1.00 32.91 C ANISOU 1412 CD1 PHE A 183 3306 4314 4885 -27 -152 -219 C ATOM 1413 CD2 PHE A 183 -8.171 1.632 27.623 1.00 32.82 C ANISOU 1413 CD2 PHE A 183 3236 4289 4945 9 -400 -327 C ATOM 1414 CE1 PHE A 183 -8.230 1.583 24.867 1.00 32.25 C ANISOU 1414 CE1 PHE A 183 3119 4188 4947 -86 -86 -240 C ATOM 1415 CE2 PHE A 183 -7.367 2.495 26.898 1.00 37.04 C ANISOU 1415 CE2 PHE A 183 3652 4776 5645 -55 -342 -353 C ATOM 1416 CZ PHE A 183 -7.398 2.470 25.518 1.00 32.77 C ANISOU 1416 CZ PHE A 183 3090 4221 5139 -105 -176 -304 C ATOM 1417 N ALA A 184 -12.175 -2.001 28.720 1.00 26.93 N ANISOU 1417 N ALA A 184 2963 3698 3573 123 -342 -114 N ATOM 1418 CA ALA A 184 -12.605 -3.012 29.681 1.00 29.00 C ANISOU 1418 CA ALA A 184 3329 3981 3707 162 -400 -77 C ATOM 1419 C ALA A 184 -13.596 -4.006 29.081 1.00 30.47 C ANISOU 1419 C ALA A 184 3586 4178 3814 140 -303 -6 C ATOM 1420 O ALA A 184 -13.450 -5.219 29.261 1.00 29.05 O ANISOU 1420 O ALA A 184 3452 3978 3606 167 -328 34 O ATOM 1421 CB ALA A 184 -13.208 -2.336 30.915 1.00 23.17 C ANISOU 1421 CB ALA A 184 2667 3284 2851 174 -460 -103 C ATOM 1422 N CYS A 185 -14.611 -3.515 28.365 1.00 25.88 N ANISOU 1422 N CYS A 185 3013 3619 3201 93 -203 8 N ATOM 1423 CA CYS A 185 -15.743 -4.351 27.979 1.00 27.19 C ANISOU 1423 CA CYS A 185 3248 3802 3283 66 -129 66 C ATOM 1424 C CYS A 185 -15.637 -4.944 26.579 1.00 28.67 C ANISOU 1424 C CYS A 185 3407 3954 3532 44 -54 88 C ATOM 1425 O CYS A 185 -16.408 -5.854 26.253 1.00 28.09 O ANISOU 1425 O CYS A 185 3390 3879 3403 24 -12 131 O ATOM 1426 CB CYS A 185 -17.050 -3.554 28.095 1.00 28.20 C ANISOU 1426 CB CYS A 185 3402 3979 3335 34 -78 64 C ATOM 1427 SG CYS A 185 -17.501 -3.146 29.798 1.00 34.83 S ANISOU 1427 SG CYS A 185 4309 4871 4054 61 -136 42 S ATOM 1428 N VAL A 186 -14.717 -4.465 25.746 1.00 26.71 N ANISOU 1428 N VAL A 186 3078 3676 3394 43 -31 56 N ATOM 1429 CA VAL A 186 -14.603 -4.957 24.378 1.00 28.00 C ANISOU 1429 CA VAL A 186 3229 3812 3600 25 53 69 C ATOM 1430 C VAL A 186 -13.216 -5.543 24.166 1.00 29.09 C ANISOU 1430 C VAL A 186 3302 3907 3844 65 38 44 C ATOM 1431 O VAL A 186 -13.073 -6.704 23.767 1.00 32.51 O ANISOU 1431 O VAL A 186 3761 4311 4279 86 55 59 O ATOM 1432 CB VAL A 186 -14.891 -3.843 23.354 1.00 30.63 C ANISOU 1432 CB VAL A 186 3536 4147 3955 -18 127 60 C ATOM 1433 CG1 VAL A 186 -14.537 -4.310 21.952 1.00 24.79 C ANISOU 1433 CG1 VAL A 186 2791 3378 3251 -31 214 67 C ATOM 1434 CG2 VAL A 186 -16.349 -3.421 23.424 1.00 26.60 C ANISOU 1434 CG2 VAL A 186 3083 3673 3350 -45 139 82 C ATOM 1435 N ALEU A 187 -12.186 -4.742 24.440 1.00 28.94 N ANISOU 1435 N ALEU A 187 3191 3881 3925 76 3 -1 N ATOM 1436 CA ALEU A 187 -10.819 -5.158 24.146 1.00 30.19 C ANISOU 1436 CA ALEU A 187 3252 4003 4214 112 -1 -36 C ATOM 1437 C ALEU A 187 -10.413 -6.358 24.994 1.00 30.13 C ANISOU 1437 C ALEU A 187 3269 3974 4205 180 -102 -31 C ATOM 1438 O ALEU A 187 -9.854 -7.335 24.481 1.00 33.68 O ANISOU 1438 O ALEU A 187 3698 4387 4711 218 -79 -37 O ATOM 1439 CB ALEU A 187 -9.871 -3.981 24.368 1.00 33.25 C ANISOU 1439 CB ALEU A 187 3525 4386 4723 98 -28 -88 C ATOM 1440 CG ALEU A 187 -8.684 -3.856 23.419 1.00 43.90 C ANISOU 1440 CG ALEU A 187 4748 5707 6225 89 54 -124 C ATOM 1441 CD1ALEU A 187 -9.129 -4.096 21.986 1.00 46.28 C ANISOU 1441 CD1ALEU A 187 5095 6005 6484 54 206 -94 C ATOM 1442 CD2ALEU A 187 -8.041 -2.483 23.559 1.00 44.19 C ANISOU 1442 CD2ALEU A 187 4683 5735 6371 44 44 -164 C ATOM 1443 N VAL A 188 -10.689 -6.303 26.299 1.00 27.64 N ANISOU 1443 N VAL A 188 3008 3676 3817 202 -215 -21 N ATOM 1444 CA VAL A 188 -10.319 -7.411 27.183 1.00 30.68 C ANISOU 1444 CA VAL A 188 3441 4033 4184 269 -325 -4 C ATOM 1445 C VAL A 188 -11.031 -8.708 26.813 1.00 30.79 C ANISOU 1445 C VAL A 188 3558 4020 4122 271 -280 54 C ATOM 1446 O VAL A 188 -10.358 -9.747 26.716 1.00 32.76 O ANISOU 1446 O VAL A 188 3800 4215 4431 328 -317 53 O ATOM 1447 CB VAL A 188 -10.533 -7.009 28.656 1.00 31.93 C ANISOU 1447 CB VAL A 188 3662 4219 4251 287 -448 -1 C ATOM 1448 CG1 VAL A 188 -10.465 -8.233 29.553 1.00 37.28 C ANISOU 1448 CG1 VAL A 188 4440 4864 4859 347 -551 44 C ATOM 1449 CG2 VAL A 188 -9.490 -5.991 29.076 1.00 27.44 C ANISOU 1449 CG2 VAL A 188 2980 3652 3793 304 -533 -74 C ATOM 1450 N PRO A 189 -12.354 -8.735 26.598 1.00 33.17 N ANISOU 1450 N PRO A 189 3949 4348 4306 213 -209 100 N ATOM 1451 CA PRO A 189 -12.973 -9.994 26.146 1.00 33.37 C ANISOU 1451 CA PRO A 189 4060 4336 4283 204 -169 147 C ATOM 1452 C PRO A 189 -12.444 -10.499 24.813 1.00 31.62 C ANISOU 1452 C PRO A 189 3789 4073 4154 216 -93 117 C ATOM 1453 O PRO A 189 -12.286 -11.714 24.644 1.00 32.21 O ANISOU 1453 O PRO A 189 3910 4087 4241 251 -108 131 O ATOM 1454 CB PRO A 189 -14.461 -9.635 26.060 1.00 33.61 C ANISOU 1454 CB PRO A 189 4156 4414 4199 130 -102 184 C ATOM 1455 CG PRO A 189 -14.638 -8.538 27.040 1.00 29.47 C ANISOU 1455 CG PRO A 189 3623 3946 3629 125 -144 171 C ATOM 1456 CD PRO A 189 -13.378 -7.728 26.941 1.00 25.89 C ANISOU 1456 CD PRO A 189 3059 3487 3292 159 -181 109 C ATOM 1457 N LEU A 190 -12.178 -9.609 23.854 1.00 28.57 N ANISOU 1457 N LEU A 190 3321 3710 3824 189 -8 77 N ATOM 1458 CA LEU A 190 -11.618 -10.053 22.581 1.00 26.72 C ANISOU 1458 CA LEU A 190 3047 3441 3663 203 79 43 C ATOM 1459 C LEU A 190 -10.242 -10.680 22.768 1.00 32.29 C ANISOU 1459 C LEU A 190 3673 4101 4496 285 31 1 C ATOM 1460 O LEU A 190 -9.922 -11.691 22.132 1.00 30.68 O ANISOU 1460 O LEU A 190 3481 3846 4329 325 64 -17 O ATOM 1461 CB LEU A 190 -11.551 -8.887 21.596 1.00 27.62 C ANISOU 1461 CB LEU A 190 3102 3591 3803 153 183 18 C ATOM 1462 CG LEU A 190 -12.893 -8.403 21.041 1.00 32.62 C ANISOU 1462 CG LEU A 190 3814 4256 4324 84 238 53 C ATOM 1463 CD1 LEU A 190 -12.712 -7.125 20.238 1.00 37.62 C ANISOU 1463 CD1 LEU A 190 4397 4912 4984 43 318 37 C ATOM 1464 CD2 LEU A 190 -13.537 -9.490 20.195 1.00 29.66 C ANISOU 1464 CD2 LEU A 190 3527 3851 3890 77 282 66 C ATOM 1465 N LEU A 191 -9.410 -10.091 23.630 1.00 31.19 N ANISOU 1465 N LEU A 191 3446 3973 4431 316 -55 -25 N ATOM 1466 CA LEU A 191 -8.106 -10.685 23.903 1.00 32.77 C ANISOU 1466 CA LEU A 191 3554 4128 4768 404 -125 -71 C ATOM 1467 C LEU A 191 -8.255 -12.031 24.602 1.00 33.74 C ANISOU 1467 C LEU A 191 3780 4192 4846 468 -230 -32 C ATOM 1468 O LEU A 191 -7.492 -12.967 24.332 1.00 36.37 O ANISOU 1468 O LEU A 191 4080 4465 5275 543 -248 -62 O ATOM 1469 CB LEU A 191 -7.253 -9.725 24.730 1.00 33.97 C ANISOU 1469 CB LEU A 191 3592 4305 5011 418 -217 -110 C ATOM 1470 CG LEU A 191 -6.832 -8.446 23.999 1.00 38.82 C ANISOU 1470 CG LEU A 191 4084 4955 5711 357 -113 -153 C ATOM 1471 CD1 LEU A 191 -6.127 -7.479 24.940 1.00 40.48 C ANISOU 1471 CD1 LEU A 191 4194 5181 6005 360 -225 -193 C ATOM 1472 CD2 LEU A 191 -5.954 -8.772 22.801 1.00 40.44 C ANISOU 1472 CD2 LEU A 191 4182 5139 6046 375 11 -202 C ATOM 1473 N LEU A 192 -9.228 -12.143 25.513 1.00 31.47 N ANISOU 1473 N LEU A 192 3622 3917 4419 439 -296 35 N ATOM 1474 CA LEU A 192 -9.537 -13.435 26.120 1.00 29.76 C ANISOU 1474 CA LEU A 192 3531 3635 4140 479 -377 91 C ATOM 1475 C LEU A 192 -9.979 -14.452 25.074 1.00 29.96 C ANISOU 1475 C LEU A 192 3616 3606 4160 469 -288 99 C ATOM 1476 O LEU A 192 -9.576 -15.620 25.126 1.00 34.62 O ANISOU 1476 O LEU A 192 4248 4112 4794 536 -342 104 O ATOM 1477 CB LEU A 192 -10.613 -13.273 27.192 1.00 32.87 C ANISOU 1477 CB LEU A 192 4053 4062 4372 430 -424 165 C ATOM 1478 CG LEU A 192 -10.228 -12.505 28.457 1.00 37.20 C ANISOU 1478 CG LEU A 192 4589 4651 4894 455 -543 160 C ATOM 1479 CD1 LEU A 192 -11.436 -12.341 29.363 1.00 40.76 C ANISOU 1479 CD1 LEU A 192 5176 5144 5167 398 -546 228 C ATOM 1480 CD2 LEU A 192 -9.108 -13.226 29.187 1.00 40.63 C ANISOU 1480 CD2 LEU A 192 5017 5020 5401 561 -699 151 C ATOM 1481 N MET A 193 -10.812 -14.028 24.118 1.00 31.28 N ANISOU 1481 N MET A 193 3797 3814 4275 389 -162 98 N ATOM 1482 CA MET A 193 -11.214 -14.919 23.033 1.00 35.48 C ANISOU 1482 CA MET A 193 4386 4295 4799 377 -82 91 C ATOM 1483 C MET A 193 -9.999 -15.423 22.268 1.00 33.37 C ANISOU 1483 C MET A 193 4034 3977 4667 460 -52 16 C ATOM 1484 O MET A 193 -9.888 -16.617 21.963 1.00 35.85 O ANISOU 1484 O MET A 193 4407 4208 5007 507 -65 7 O ATOM 1485 CB MET A 193 -12.160 -14.192 22.078 1.00 39.17 C ANISOU 1485 CB MET A 193 4866 4822 5196 287 33 90 C ATOM 1486 CG MET A 193 -13.591 -14.055 22.546 1.00 44.88 C ANISOU 1486 CG MET A 193 5681 5578 5793 206 25 156 C ATOM 1487 SD MET A 193 -14.547 -13.172 21.299 1.00 44.93 S ANISOU 1487 SD MET A 193 5683 5645 5743 123 139 140 S ATOM 1488 CE MET A 193 -15.458 -12.014 22.315 1.00 41.78 C ANISOU 1488 CE MET A 193 5279 5330 5266 68 111 183 C ATOM 1489 N LEU A 194 -9.080 -14.513 21.937 1.00 31.39 N ANISOU 1489 N LEU A 194 3641 3772 4512 476 -6 -43 N ATOM 1490 CA LEU A 194 -7.854 -14.899 21.249 1.00 35.09 C ANISOU 1490 CA LEU A 194 4002 4205 5125 555 40 -123 C ATOM 1491 C LEU A 194 -7.088 -15.951 22.039 1.00 33.46 C ANISOU 1491 C LEU A 194 3789 3917 5006 665 -95 -131 C ATOM 1492 O LEU A 194 -6.611 -16.940 21.473 1.00 36.82 O ANISOU 1492 O LEU A 194 4214 4272 5504 737 -73 -177 O ATOM 1493 CB LEU A 194 -6.986 -13.663 21.010 1.00 31.66 C ANISOU 1493 CB LEU A 194 3404 3835 4790 541 101 -173 C ATOM 1494 CG LEU A 194 -5.607 -13.865 20.387 1.00 39.64 C ANISOU 1494 CG LEU A 194 4261 4825 5975 615 164 -263 C ATOM 1495 CD1 LEU A 194 -5.733 -14.555 19.041 1.00 44.61 C ANISOU 1495 CD1 LEU A 194 4941 5426 6581 623 308 -301 C ATOM 1496 CD2 LEU A 194 -4.896 -12.530 20.243 1.00 40.66 C ANISOU 1496 CD2 LEU A 194 4233 5018 6198 572 227 -298 C ATOM 1497 N GLY A 195 -6.957 -15.751 23.351 1.00 35.90 N ANISOU 1497 N GLY A 195 4102 4231 5307 686 -241 -91 N ATOM 1498 CA GLY A 195 -6.282 -16.738 24.177 1.00 35.80 C ANISOU 1498 CA GLY A 195 4105 4134 5362 795 -393 -86 C ATOM 1499 C GLY A 195 -6.975 -18.088 24.188 1.00 34.17 C ANISOU 1499 C GLY A 195 4071 3833 5081 810 -424 -32 C ATOM 1500 O GLY A 195 -6.319 -19.132 24.136 1.00 36.35 O ANISOU 1500 O GLY A 195 4349 4013 5451 911 -483 -60 O ATOM 1501 N VAL A 196 -8.308 -18.089 24.262 1.00 32.28 N ANISOU 1501 N VAL A 196 3970 3611 4683 709 -387 43 N ATOM 1502 CA VAL A 196 -9.058 -19.344 24.205 1.00 35.56 C ANISOU 1502 CA VAL A 196 4546 3931 5034 699 -403 97 C ATOM 1503 C VAL A 196 -8.837 -20.052 22.873 1.00 35.97 C ANISOU 1503 C VAL A 196 4584 3924 5158 730 -306 23 C ATOM 1504 O VAL A 196 -8.601 -21.265 22.828 1.00 32.84 O ANISOU 1504 O VAL A 196 4258 3411 4810 800 -360 18 O ATOM 1505 CB VAL A 196 -10.555 -19.089 24.465 1.00 33.86 C ANISOU 1505 CB VAL A 196 4451 3760 4655 572 -363 181 C ATOM 1506 CG1 VAL A 196 -11.342 -20.379 24.322 1.00 35.55 C ANISOU 1506 CG1 VAL A 196 4818 3870 4821 544 -370 232 C ATOM 1507 CG2 VAL A 196 -10.760 -18.503 25.851 1.00 34.21 C ANISOU 1507 CG2 VAL A 196 4527 3856 4616 553 -455 248 C ATOM 1508 N TYR A 197 -8.912 -19.308 21.766 1.00 34.68 N ANISOU 1508 N TYR A 197 4346 3836 4997 682 -163 -36 N ATOM 1509 CA TYR A 197 -8.710 -19.924 20.458 1.00 36.91 C ANISOU 1509 CA TYR A 197 4629 4071 5323 711 -60 -114 C ATOM 1510 C TYR A 197 -7.295 -20.468 20.305 1.00 42.65 C ANISOU 1510 C TYR A 197 5249 4738 6218 849 -81 -199 C ATOM 1511 O TYR A 197 -7.096 -21.540 19.722 1.00 43.96 O ANISOU 1511 O TYR A 197 5465 4809 6430 914 -67 -248 O ATOM 1512 CB TYR A 197 -9.047 -18.932 19.346 1.00 35.96 C ANISOU 1512 CB TYR A 197 4464 4047 5152 632 94 -151 C ATOM 1513 CG TYR A 197 -10.534 -18.854 19.100 1.00 36.88 C ANISOU 1513 CG TYR A 197 4708 4185 5121 518 120 -92 C ATOM 1514 CD1 TYR A 197 -11.236 -19.961 18.639 1.00 36.88 C ANISOU 1514 CD1 TYR A 197 4838 4099 5077 502 114 -90 C ATOM 1515 CD2 TYR A 197 -11.243 -17.687 19.353 1.00 37.23 C ANISOU 1515 CD2 TYR A 197 4736 4327 5082 427 140 -44 C ATOM 1516 CE1 TYR A 197 -12.597 -19.902 18.415 1.00 37.66 C ANISOU 1516 CE1 TYR A 197 5033 4217 5060 394 128 -43 C ATOM 1517 CE2 TYR A 197 -12.607 -17.621 19.139 1.00 38.28 C ANISOU 1517 CE2 TYR A 197 4966 4480 5098 330 157 2 C ATOM 1518 CZ TYR A 197 -13.276 -18.730 18.667 1.00 41.46 C ANISOU 1518 CZ TYR A 197 5483 4804 5467 312 150 3 C ATOM 1519 OH TYR A 197 -14.634 -18.668 18.461 1.00 42.11 O ANISOU 1519 OH TYR A 197 5642 4906 5451 212 158 43 O ATOM 1520 N LEU A 198 -6.296 -19.741 20.812 1.00 39.84 N ANISOU 1520 N LEU A 198 4738 4433 5965 897 -117 -226 N ATOM 1521 CA LEU A 198 -4.935 -20.269 20.809 1.00 38.66 C ANISOU 1521 CA LEU A 198 4465 4228 5997 1036 -157 -309 C ATOM 1522 C LEU A 198 -4.861 -21.587 21.569 1.00 37.68 C ANISOU 1522 C LEU A 198 4448 3969 5899 1130 -320 -274 C ATOM 1523 O LEU A 198 -4.200 -22.534 21.124 1.00 38.11 O ANISOU 1523 O LEU A 198 4482 3932 6067 1240 -323 -345 O ATOM 1524 CB LEU A 198 -3.966 -19.245 21.400 1.00 42.46 C ANISOU 1524 CB LEU A 198 4761 4784 6590 1060 -200 -336 C ATOM 1525 CG LEU A 198 -3.733 -17.994 20.549 1.00 46.63 C ANISOU 1525 CG LEU A 198 5156 5421 7139 984 -30 -385 C ATOM 1526 CD1 LEU A 198 -2.850 -16.998 21.283 1.00 45.46 C ANISOU 1526 CD1 LEU A 198 4833 5332 7107 995 -98 -405 C ATOM 1527 CD2 LEU A 198 -3.126 -18.370 19.205 1.00 46.80 C ANISOU 1527 CD2 LEU A 198 5106 5429 7247 1030 138 -486 C ATOM 1528 N ARG A 199 -5.529 -21.664 22.722 1.00 38.42 N ANISOU 1528 N ARG A 199 4663 4046 5888 1090 -453 -164 N ATOM 1529 CA ARG A 199 -5.545 -22.901 23.495 1.00 44.01 C ANISOU 1529 CA ARG A 199 5505 4618 6600 1165 -609 -108 C ATOM 1530 C ARG A 199 -6.270 -24.016 22.750 1.00 44.12 C ANISOU 1530 C ARG A 199 5667 4527 6568 1145 -554 -105 C ATOM 1531 O ARG A 199 -5.855 -25.180 22.813 1.00 47.78 O ANISOU 1531 O ARG A 199 6189 4853 7112 1248 -637 -120 O ATOM 1532 CB ARG A 199 -6.190 -22.655 24.859 1.00 45.21 C ANISOU 1532 CB ARG A 199 5771 4786 6619 1108 -735 16 C ATOM 1533 CG ARG A 199 -5.381 -21.751 25.775 1.00 48.97 C ANISOU 1533 CG ARG A 199 6127 5336 7145 1152 -840 8 C ATOM 1534 CD ARG A 199 -6.053 -21.594 27.130 1.00 60.51 C ANISOU 1534 CD ARG A 199 7732 6808 8450 1102 -961 127 C ATOM 1535 NE ARG A 199 -5.139 -21.054 28.132 1.00 74.09 N ANISOU 1535 NE ARG A 199 9367 8558 10224 1178 -1116 114 N ATOM 1536 CZ ARG A 199 -4.289 -21.787 28.842 1.00 87.47 C ANISOU 1536 CZ ARG A 199 11077 10157 12001 1311 -1301 118 C ATOM 1537 NH1 ARG A 199 -4.235 -23.100 28.665 1.00 93.05 N ANISOU 1537 NH1 ARG A 199 11885 10724 12747 1384 -1347 138 N ATOM 1538 NH2 ARG A 199 -3.494 -21.209 29.732 1.00 91.40 N ANISOU 1538 NH2 ARG A 199 11493 10690 12544 1374 -1452 98 N ATOM 1539 N ILE A 200 -7.360 -23.686 22.050 1.00 40.71 N ANISOU 1539 N ILE A 200 5301 4151 6015 1015 -427 -87 N ATOM 1540 CA ILE A 200 -8.086 -24.693 21.276 1.00 37.26 C ANISOU 1540 CA ILE A 200 5001 3618 5539 985 -380 -96 C ATOM 1541 C ILE A 200 -7.182 -25.300 20.210 1.00 36.57 C ANISOU 1541 C ILE A 200 4846 3467 5581 1099 -314 -228 C ATOM 1542 O ILE A 200 -7.059 -26.526 20.096 1.00 38.17 O ANISOU 1542 O ILE A 200 5141 3524 5838 1173 -373 -248 O ATOM 1543 CB ILE A 200 -9.352 -24.081 20.650 1.00 34.83 C ANISOU 1543 CB ILE A 200 4747 3397 5090 831 -263 -70 C ATOM 1544 CG1 ILE A 200 -10.398 -23.787 21.724 1.00 34.39 C ANISOU 1544 CG1 ILE A 200 4783 3374 4909 723 -326 60 C ATOM 1545 CG2 ILE A 200 -9.927 -25.013 19.591 1.00 34.80 C ANISOU 1545 CG2 ILE A 200 4852 3304 5067 808 -204 -116 C ATOM 1546 CD1 ILE A 200 -11.558 -22.952 21.228 1.00 34.18 C ANISOU 1546 CD1 ILE A 200 4766 3455 4765 583 -221 80 C ATOM 1547 N PHE A 201 -6.537 -24.447 19.411 1.00 40.27 N ANISOU 1547 N PHE A 201 5158 4041 6102 1114 -185 -320 N ATOM 1548 CA PHE A 201 -5.720 -24.935 18.305 1.00 41.42 C ANISOU 1548 CA PHE A 201 5236 4145 6355 1213 -85 -453 C ATOM 1549 C PHE A 201 -4.475 -25.659 18.801 1.00 39.47 C ANISOU 1549 C PHE A 201 4902 3803 6291 1384 -192 -507 C ATOM 1550 O PHE A 201 -4.035 -26.630 18.176 1.00 44.77 O ANISOU 1550 O PHE A 201 5592 4370 7048 1486 -171 -597 O ATOM 1551 CB PHE A 201 -5.338 -23.776 17.386 1.00 43.78 C ANISOU 1551 CB PHE A 201 5393 4586 6656 1175 93 -524 C ATOM 1552 CG PHE A 201 -6.504 -23.184 16.647 1.00 42.65 C ANISOU 1552 CG PHE A 201 5345 4518 6342 1031 201 -492 C ATOM 1553 CD1 PHE A 201 -7.396 -23.998 15.968 1.00 45.52 C ANISOU 1553 CD1 PHE A 201 5875 4809 6614 992 220 -502 C ATOM 1554 CD2 PHE A 201 -6.720 -21.816 16.646 1.00 43.36 C ANISOU 1554 CD2 PHE A 201 5361 4743 6370 936 269 -456 C ATOM 1555 CE1 PHE A 201 -8.475 -23.460 15.291 1.00 47.29 C ANISOU 1555 CE1 PHE A 201 6180 5099 6687 867 298 -477 C ATOM 1556 CE2 PHE A 201 -7.798 -21.271 15.972 1.00 46.47 C ANISOU 1556 CE2 PHE A 201 5844 5200 6614 815 351 -426 C ATOM 1557 CZ PHE A 201 -8.676 -22.095 15.293 1.00 46.41 C ANISOU 1557 CZ PHE A 201 5993 5125 6516 783 362 -437 C ATOM 1558 N ALA A 202 -3.897 -25.203 19.914 1.00 42.93 N ANISOU 1558 N ALA A 202 5246 4272 6793 1422 -316 -460 N ATOM 1559 CA ALA A 202 -2.770 -25.914 20.506 1.00 47.67 C ANISOU 1559 CA ALA A 202 5771 4773 7568 1590 -457 -501 C ATOM 1560 C ALA A 202 -3.196 -27.274 21.042 1.00 50.89 C ANISOU 1560 C ALA A 202 6378 5005 7953 1641 -608 -436 C ATOM 1561 O ALA A 202 -2.450 -28.253 20.929 1.00 50.54 O ANISOU 1561 O ALA A 202 6321 4833 8050 1789 -673 -505 O ATOM 1562 CB ALA A 202 -2.139 -25.072 21.614 1.00 42.49 C ANISOU 1562 CB ALA A 202 4985 4191 6969 1611 -578 -462 C ATOM 1563 N ALA A 203 -4.390 -27.355 21.635 1.00 51.72 N ANISOU 1563 N ALA A 203 6668 5094 7890 1519 -662 -304 N ATOM 1564 CA ALA A 203 -4.880 -28.641 22.121 1.00 50.06 C ANISOU 1564 CA ALA A 203 6662 4708 7651 1542 -790 -229 C ATOM 1565 C ALA A 203 -5.139 -29.603 20.970 1.00 51.51 C ANISOU 1565 C ALA A 203 6929 4783 7860 1560 -702 -312 C ATOM 1566 O ALA A 203 -4.800 -30.788 21.059 1.00 53.37 O ANISOU 1566 O ALA A 203 7247 4846 8185 1671 -802 -331 O ATOM 1567 CB ALA A 203 -6.148 -28.441 22.950 1.00 45.89 C ANISOU 1567 CB ALA A 203 6299 4202 6937 1387 -834 -71 C ATOM 1568 N ALA A 204 -5.732 -29.113 19.878 1.00 52.12 N ANISOU 1568 N ALA A 204 6994 4952 7856 1458 -526 -366 N ATOM 1569 CA ALA A 204 -5.931 -29.957 18.705 1.00 47.35 C ANISOU 1569 CA ALA A 204 6469 4256 7268 1480 -441 -465 C ATOM 1570 C ALA A 204 -4.602 -30.448 18.149 1.00 49.77 C ANISOU 1570 C ALA A 204 6652 4503 7755 1666 -416 -614 C ATOM 1571 O ALA A 204 -4.460 -31.627 17.804 1.00 51.26 O ANISOU 1571 O ALA A 204 6934 4529 8013 1758 -456 -675 O ATOM 1572 CB ALA A 204 -6.707 -29.192 17.636 1.00 45.29 C ANISOU 1572 CB ALA A 204 6207 4123 6879 1346 -265 -500 C ATOM 1573 N ARG A 205 -3.619 -29.550 18.044 1.00 53.00 N ANISOU 1573 N ARG A 205 6845 5039 8254 1724 -346 -681 N ATOM 1574 CA ARG A 205 -2.314 -29.934 17.519 1.00 59.92 C ANISOU 1574 CA ARG A 205 7570 5877 9321 1901 -303 -831 C ATOM 1575 C ARG A 205 -1.660 -30.996 18.392 1.00 57.48 C ANISOU 1575 C ARG A 205 7285 5396 9159 2061 -509 -820 C ATOM 1576 O ARG A 205 -1.053 -31.944 17.881 1.00 59.06 O ANISOU 1576 O ARG A 205 7480 5472 9487 2206 -509 -934 O ATOM 1577 CB ARG A 205 -1.415 -28.703 17.410 1.00 67.41 C ANISOU 1577 CB ARG A 205 8268 6995 10349 1911 -200 -885 C ATOM 1578 CG ARG A 205 0.018 -29.006 17.010 1.00 77.78 C ANISOU 1578 CG ARG A 205 9381 8283 11887 2093 -156 -1038 C ATOM 1579 CD ARG A 205 0.876 -27.757 17.105 1.00 86.70 C ANISOU 1579 CD ARG A 205 10257 9575 13112 2083 -78 -1071 C ATOM 1580 NE ARG A 205 0.733 -27.113 18.408 1.00 95.05 N ANISOU 1580 NE ARG A 205 11297 10676 14143 2027 -250 -943 N ATOM 1581 CZ ARG A 205 1.310 -25.964 18.742 1.00102.11 C ANISOU 1581 CZ ARG A 205 11998 11700 15101 1994 -230 -944 C ATOM 1582 NH1 ARG A 205 2.078 -25.328 17.869 1.00105.47 N ANISOU 1582 NH1 ARG A 205 12222 12224 15629 2002 -37 -1057 N ATOM 1583 NH2 ARG A 205 1.122 -25.450 19.951 1.00103.74 N ANISOU 1583 NH2 ARG A 205 12217 11935 15266 1948 -400 -834 N ATOM 1584 N ARG A 206 -1.767 -30.851 19.715 1.00 53.58 N ANISOU 1584 N ARG A 206 6827 4888 8643 2045 -691 -686 N ATOM 1585 CA ARG A 206 -1.166 -31.831 20.612 1.00 57.30 C ANISOU 1585 CA ARG A 206 7343 5190 9238 2199 -910 -658 C ATOM 1586 C ARG A 206 -1.867 -33.180 20.508 1.00 56.79 C ANISOU 1586 C ARG A 206 7524 4922 9132 2205 -979 -622 C ATOM 1587 O ARG A 206 -1.210 -34.228 20.515 1.00 60.04 O ANISOU 1587 O ARG A 206 7957 5165 9691 2371 -1079 -684 O ATOM 1588 CB ARG A 206 -1.196 -31.316 22.050 1.00 60.84 C ANISOU 1588 CB ARG A 206 7803 5677 9636 2168 -1087 -516 C ATOM 1589 CG ARG A 206 -0.689 -32.322 23.068 1.00 77.21 C ANISOU 1589 CG ARG A 206 9964 7570 11804 2317 -1336 -460 C ATOM 1590 CD ARG A 206 -0.589 -31.720 24.459 1.00 90.44 C ANISOU 1590 CD ARG A 206 11641 9299 13422 2300 -1510 -335 C ATOM 1591 NE ARG A 206 0.071 -32.632 25.389 1.00104.91 N ANISOU 1591 NE ARG A 206 13539 10998 15325 2429 -1730 -287 N ATOM 1592 CZ ARG A 206 0.405 -32.319 26.637 1.00111.18 C ANISOU 1592 CZ ARG A 206 14338 11832 16074 2437 -1901 -195 C ATOM 1593 NH1 ARG A 206 0.143 -31.110 27.113 1.00111.69 N ANISOU 1593 NH1 ARG A 206 14346 12033 16059 2361 -1906 -151 N ATOM 1594 NH2 ARG A 206 1.003 -33.215 27.409 1.00113.78 N ANISOU 1594 NH2 ARG A 206 14733 12064 16432 2523 -2070 -152 N ATOM 1595 N GLN A 207 -3.199 -33.177 20.402 1.00 51.84 N ANISOU 1595 N GLN A 207 7078 4300 8319 2026 -929 -527 N ATOM 1596 CA GLN A 207 -3.929 -34.441 20.372 1.00 49.84 C ANISOU 1596 CA GLN A 207 7060 3845 8031 2008 -1002 -481 C ATOM 1597 C GLN A 207 -3.673 -35.192 19.072 1.00 49.39 C ANISOU 1597 C GLN A 207 7009 3697 8059 2092 -897 -650 C ATOM 1598 O GLN A 207 -3.567 -36.424 19.073 1.00 56.19 O ANISOU 1598 O GLN A 207 7999 4349 9003 2188 -998 -672 O ATOM 1599 CB GLN A 207 -5.423 -34.195 20.574 1.00 47.81 C ANISOU 1599 CB GLN A 207 6967 3627 7571 1786 -968 -345 C ATOM 1600 CG GLN A 207 -5.774 -33.576 21.915 1.00 51.65 C ANISOU 1600 CG GLN A 207 7483 4186 7956 1703 -1070 -176 C ATOM 1601 CD GLN A 207 -7.268 -33.432 22.120 1.00 57.76 C ANISOU 1601 CD GLN A 207 8412 4988 8547 1491 -1027 -49 C ATOM 1602 OE1 GLN A 207 -8.066 -34.089 21.452 1.00 65.39 O ANISOU 1602 OE1 GLN A 207 9502 5866 9479 1413 -975 -64 O ATOM 1603 NE2 GLN A 207 -7.656 -32.563 23.046 1.00 52.42 N ANISOU 1603 NE2 GLN A 207 7724 4435 7758 1397 -1048 68 N ATOM 1604 N LEU A 208 -3.578 -34.470 17.952 1.00 46.92 N ANISOU 1604 N LEU A 208 6573 3535 7721 2058 -694 -770 N ATOM 1605 CA LEU A 208 -3.243 -35.119 16.690 1.00 53.76 C ANISOU 1605 CA LEU A 208 7440 4331 8655 2150 -580 -946 C ATOM 1606 C LEU A 208 -1.834 -35.696 16.738 1.00 54.93 C ANISOU 1606 C LEU A 208 7454 4387 9029 2387 -636 -1066 C ATOM 1607 O LEU A 208 -1.594 -36.812 16.262 1.00 60.28 O ANISOU 1607 O LEU A 208 8213 4905 9786 2494 -654 -1158 O ATOM 1608 CB LEU A 208 -3.380 -34.124 15.537 1.00 56.91 C ANISOU 1608 CB LEU A 208 7740 4924 8961 2065 -347 -1037 C ATOM 1609 CG LEU A 208 -4.805 -33.761 15.113 1.00 64.67 C ANISOU 1609 CG LEU A 208 8869 5970 9734 1855 -278 -967 C ATOM 1610 CD1 LEU A 208 -4.790 -32.633 14.093 1.00 67.56 C ANISOU 1610 CD1 LEU A 208 9123 6536 10012 1787 -67 -1042 C ATOM 1611 CD2 LEU A 208 -5.518 -34.981 14.550 1.00 65.57 C ANISOU 1611 CD2 LEU A 208 9197 5900 9817 1841 -314 -1008 C ATOM 1612 N ALA A1001 -0.886 -34.938 17.296 1.00 91.84 N ANISOU 1612 N ALA A1001 14054 4550 16293 1874 -278 -916 N ATOM 1613 CA ALA A1001 0.470 -35.445 17.471 1.00 90.53 C ANISOU 1613 CA ALA A1001 13661 4393 16342 1361 -336 -876 C ATOM 1614 C ALA A1001 0.486 -36.680 18.364 1.00 87.20 C ANISOU 1614 C ALA A1001 12811 4353 15967 1414 -248 -1008 C ATOM 1615 O ALA A1001 1.220 -37.639 18.098 1.00 84.43 O ANISOU 1615 O ALA A1001 12062 4217 15801 1128 -161 -896 O ATOM 1616 CB ALA A1001 1.371 -34.353 18.048 1.00 94.72 C ANISOU 1616 CB ALA A1001 14638 4474 16878 1055 -571 -944 C ATOM 1617 N ASP A1002 -0.312 -36.668 19.437 1.00 87.77 N ANISOU 1617 N ASP A1002 12977 4517 15856 1798 -247 -1234 N ATOM 1618 CA ASP A1002 -0.382 -37.824 20.327 1.00 88.23 C ANISOU 1618 CA ASP A1002 12651 4949 15924 1857 -169 -1363 C ATOM 1619 C ASP A1002 -0.933 -39.050 19.610 1.00 83.60 C ANISOU 1619 C ASP A1002 11587 4799 15379 1932 19 -1203 C ATOM 1620 O ASP A1002 -0.484 -40.175 19.857 1.00 83.20 O ANISOU 1620 O ASP A1002 11178 5012 15423 1757 84 -1204 O ATOM 1621 CB ASP A1002 -1.234 -37.491 21.553 1.00 93.30 C ANISOU 1621 CB ASP A1002 13515 5616 16319 2298 -176 -1605 C ATOM 1622 CG ASP A1002 -0.582 -36.459 22.454 1.00104.38 C ANISOU 1622 CG ASP A1002 15440 6582 17637 2179 -371 -1784 C ATOM 1623 OD1 ASP A1002 0.657 -36.312 22.393 1.00107.57 O ANISOU 1623 OD1 ASP A1002 15892 6760 18218 1674 -541 -1735 O ATOM 1624 OD2 ASP A1002 -1.307 -35.791 23.221 1.00110.74 O ANISOU 1624 OD2 ASP A1002 16600 7277 18199 2580 -343 -1945 O ATOM 1625 N LEU A1003 -1.917 -38.856 18.727 1.00 81.04 N ANISOU 1625 N LEU A1003 11287 4535 14969 2187 88 -1055 N ATOM 1626 CA LEU A1003 -2.431 -39.973 17.939 1.00 79.24 C ANISOU 1626 CA LEU A1003 10686 4658 14762 2199 215 -863 C ATOM 1627 C LEU A1003 -1.346 -40.553 17.043 1.00 78.73 C ANISOU 1627 C LEU A1003 10490 4570 14854 1777 270 -691 C ATOM 1628 O LEU A1003 -1.164 -41.775 16.980 1.00 72.86 O ANISOU 1628 O LEU A1003 9449 4098 14135 1674 362 -633 O ATOM 1629 CB LEU A1003 -3.636 -39.527 17.110 1.00 82.39 C ANISOU 1629 CB LEU A1003 11172 5070 15063 2514 229 -704 C ATOM 1630 CG LEU A1003 -4.943 -39.289 17.868 1.00 84.22 C ANISOU 1630 CG LEU A1003 11375 5486 15138 3035 245 -785 C ATOM 1631 CD1 LEU A1003 -5.944 -38.555 16.991 1.00 83.18 C ANISOU 1631 CD1 LEU A1003 11387 5276 14943 3339 229 -608 C ATOM 1632 CD2 LEU A1003 -5.522 -40.609 18.357 1.00 81.67 C ANISOU 1632 CD2 LEU A1003 10587 5638 14806 3115 322 -752 C ATOM 1633 N GLU A1004 -0.616 -39.687 16.337 1.00 85.29 N ANISOU 1633 N GLU A1004 11562 5075 15771 1550 223 -590 N ATOM 1634 CA GLU A1004 0.424 -40.164 15.433 1.00 91.93 C ANISOU 1634 CA GLU A1004 12267 5910 16753 1198 320 -385 C ATOM 1635 C GLU A1004 1.589 -40.785 16.193 1.00 87.93 C ANISOU 1635 C GLU A1004 11525 5466 16420 941 342 -452 C ATOM 1636 O GLU A1004 2.198 -41.745 15.710 1.00 85.39 O ANISOU 1636 O GLU A1004 10960 5309 16177 798 493 -306 O ATOM 1637 CB GLU A1004 0.917 -39.018 14.549 1.00102.49 C ANISOU 1637 CB GLU A1004 13901 6894 18147 1005 258 -236 C ATOM 1638 CG GLU A1004 1.640 -39.464 13.286 1.00109.75 C ANISOU 1638 CG GLU A1004 14705 7848 19146 754 415 45 C ATOM 1639 CD GLU A1004 0.880 -40.533 12.525 1.00113.70 C ANISOU 1639 CD GLU A1004 15074 8637 19488 929 554 158 C ATOM 1640 OE1 GLU A1004 1.488 -41.572 12.191 1.00113.64 O ANISOU 1640 OE1 GLU A1004 14866 8803 19507 818 716 274 O ATOM 1641 OE2 GLU A1004 -0.323 -40.332 12.255 1.00115.79 O ANISOU 1641 OE2 GLU A1004 15462 8933 19598 1181 488 153 O ATOM 1642 N ASP A1005 1.909 -40.260 17.379 1.00 85.50 N ANISOU 1642 N ASP A1005 11317 5013 16157 898 187 -662 N ATOM 1643 CA ASP A1005 2.984 -40.840 18.178 1.00 81.55 C ANISOU 1643 CA ASP A1005 10582 4580 15825 640 167 -720 C ATOM 1644 C ASP A1005 2.627 -42.244 18.649 1.00 78.91 C ANISOU 1644 C ASP A1005 9927 4698 15355 790 282 -798 C ATOM 1645 O ASP A1005 3.477 -43.142 18.649 1.00 76.10 O ANISOU 1645 O ASP A1005 9302 4582 15030 601 365 -707 O ATOM 1646 CB ASP A1005 3.299 -39.939 19.371 1.00 88.17 C ANISOU 1646 CB ASP A1005 11681 5141 16680 551 -78 -932 C ATOM 1647 CG ASP A1005 4.201 -38.780 19.002 1.00 98.64 C ANISOU 1647 CG ASP A1005 13270 6072 18136 187 -249 -784 C ATOM 1648 OD1 ASP A1005 5.024 -38.937 18.076 1.00101.35 O ANISOU 1648 OD1 ASP A1005 13414 6453 18642 -105 -152 -499 O ATOM 1649 OD2 ASP A1005 4.089 -37.711 19.639 1.00103.81 O ANISOU 1649 OD2 ASP A1005 14358 6417 18667 192 -478 -927 O ATOM 1650 N ASN A1006 1.373 -42.452 19.056 1.00 76.54 N ANISOU 1650 N ASN A1006 9654 4535 14892 1137 282 -939 N ATOM 1651 CA ASN A1006 0.949 -43.779 19.482 1.00 76.10 C ANISOU 1651 CA ASN A1006 9322 4908 14684 1239 353 -980 C ATOM 1652 C ASN A1006 0.886 -44.747 18.307 1.00 73.08 C ANISOU 1652 C ASN A1006 8809 4721 14236 1197 492 -738 C ATOM 1653 O ASN A1006 1.153 -45.942 18.474 1.00 67.73 O ANISOU 1653 O ASN A1006 7943 4329 13463 1134 542 -716 O ATOM 1654 CB ASN A1006 -0.407 -43.695 20.183 1.00 81.98 C ANISOU 1654 CB ASN A1006 10096 5793 15261 1604 318 -1127 C ATOM 1655 CG ASN A1006 -0.279 -43.578 21.690 1.00 86.24 C ANISOU 1655 CG ASN A1006 10660 6361 15745 1655 225 -1399 C ATOM 1656 OD1 ASN A1006 0.667 -44.094 22.287 1.00 91.23 O ANISOU 1656 OD1 ASN A1006 11174 7064 16424 1406 183 -1468 O ATOM 1657 ND2 ASN A1006 -1.229 -42.891 22.313 1.00 82.85 N ANISOU 1657 ND2 ASN A1006 10402 5879 15199 2008 196 -1543 N ATOM 1658 N TRP A1007 0.531 -44.250 17.120 1.00 73.39 N ANISOU 1658 N TRP A1007 9007 4581 14299 1240 539 -556 N ATOM 1659 CA TRP A1007 0.542 -45.085 15.923 1.00 69.87 C ANISOU 1659 CA TRP A1007 8540 4246 13760 1189 658 -317 C ATOM 1660 C TRP A1007 1.957 -45.529 15.571 1.00 69.14 C ANISOU 1660 C TRP A1007 8358 4172 13742 951 786 -203 C ATOM 1661 O TRP A1007 2.191 -46.706 15.270 1.00 68.81 O ANISOU 1661 O TRP A1007 8239 4350 13555 949 882 -113 O ATOM 1662 CB TRP A1007 -0.095 -44.325 14.758 1.00 73.83 C ANISOU 1662 CB TRP A1007 9266 4531 14254 1266 659 -146 C ATOM 1663 CG TRP A1007 -0.120 -45.083 13.466 1.00 76.53 C ANISOU 1663 CG TRP A1007 9684 4924 14470 1215 762 103 C ATOM 1664 CD1 TRP A1007 0.628 -44.826 12.354 1.00 79.22 C ANISOU 1664 CD1 TRP A1007 10164 5110 14827 1067 879 294 C ATOM 1665 CD2 TRP A1007 -0.940 -46.214 13.145 1.00 77.30 C ANISOU 1665 CD2 TRP A1007 9775 5244 14351 1298 734 207 C ATOM 1666 NE1 TRP A1007 0.329 -45.729 11.363 1.00 80.29 N ANISOU 1666 NE1 TRP A1007 10422 5332 14753 1093 944 482 N ATOM 1667 CE2 TRP A1007 -0.631 -46.591 11.823 1.00 78.08 C ANISOU 1667 CE2 TRP A1007 10078 5239 14350 1218 836 438 C ATOM 1668 CE3 TRP A1007 -1.904 -46.945 13.847 1.00 75.37 C ANISOU 1668 CE3 TRP A1007 9393 5298 13947 1406 614 150 C ATOM 1669 CZ2 TRP A1007 -1.251 -47.667 11.188 1.00 75.43 C ANISOU 1669 CZ2 TRP A1007 9883 5032 13747 1234 787 597 C ATOM 1670 CZ3 TRP A1007 -2.517 -48.014 13.215 1.00 73.23 C ANISOU 1670 CZ3 TRP A1007 9204 5187 13431 1378 551 339 C ATOM 1671 CH2 TRP A1007 -2.188 -48.364 11.899 1.00 74.15 C ANISOU 1671 CH2 TRP A1007 9594 5140 13439 1289 620 551 C ATOM 1672 N GLU A1008 2.915 -44.598 15.599 1.00 71.69 N ANISOU 1672 N GLU A1008 8700 4271 14268 756 779 -177 N ATOM 1673 CA GLU A1008 4.301 -44.953 15.306 1.00 76.24 C ANISOU 1673 CA GLU A1008 9106 4933 14929 536 913 -8 C ATOM 1674 C GLU A1008 4.872 -45.899 16.355 1.00 73.34 C ANISOU 1674 C GLU A1008 8480 4852 14534 504 901 -127 C ATOM 1675 O GLU A1008 5.565 -46.863 16.012 1.00 73.25 O ANISOU 1675 O GLU A1008 8321 5058 14451 503 1060 12 O ATOM 1676 CB GLU A1008 5.162 -43.693 15.203 1.00 84.15 C ANISOU 1676 CB GLU A1008 10154 5661 16156 268 850 92 C ATOM 1677 CG GLU A1008 4.735 -42.727 14.113 1.00 95.71 C ANISOU 1677 CG GLU A1008 11898 6815 17650 269 855 233 C ATOM 1678 CD GLU A1008 5.437 -41.389 14.219 1.00109.11 C ANISOU 1678 CD GLU A1008 13717 8194 19546 -26 704 299 C ATOM 1679 OE1 GLU A1008 6.476 -41.316 14.908 1.00114.41 O ANISOU 1679 OE1 GLU A1008 14198 8931 20341 -291 632 327 O ATOM 1680 OE2 GLU A1008 4.950 -40.411 13.615 1.00114.61 O ANISOU 1680 OE2 GLU A1008 14716 8565 20265 -12 627 341 O ATOM 1681 N THR A1009 4.594 -45.639 17.636 1.00 72.96 N ANISOU 1681 N THR A1009 8408 4797 14518 507 717 -380 N ATOM 1682 CA THR A1009 5.081 -46.520 18.694 1.00 74.34 C ANISOU 1682 CA THR A1009 8359 5230 14658 466 676 -505 C ATOM 1683 C THR A1009 4.582 -47.945 18.493 1.00 72.44 C ANISOU 1683 C THR A1009 8067 5279 14179 649 770 -494 C ATOM 1684 O THR A1009 5.325 -48.911 18.707 1.00 69.58 O ANISOU 1684 O THR A1009 7539 5132 13767 619 833 -453 O ATOM 1685 CB THR A1009 4.653 -45.981 20.061 1.00 76.93 C ANISOU 1685 CB THR A1009 8754 5474 15000 481 464 -791 C ATOM 1686 OG1 THR A1009 5.388 -44.788 20.357 1.00 86.89 O ANISOU 1686 OG1 THR A1009 10116 6441 16457 243 324 -788 O ATOM 1687 CG2 THR A1009 4.910 -47.008 21.156 1.00 72.76 C ANISOU 1687 CG2 THR A1009 8027 5229 14388 471 412 -937 C ATOM 1688 N LEU A1010 3.325 -48.095 18.073 1.00 70.27 N ANISOU 1688 N LEU A1010 7952 5007 13739 832 754 -504 N ATOM 1689 CA LEU A1010 2.785 -49.421 17.793 1.00 65.60 C ANISOU 1689 CA LEU A1010 7387 4649 12889 944 780 -449 C ATOM 1690 C LEU A1010 3.571 -50.110 16.682 1.00 64.54 C ANISOU 1690 C LEU A1010 7322 4527 12672 937 964 -219 C ATOM 1691 O LEU A1010 3.988 -51.266 16.823 1.00 66.65 O ANISOU 1691 O LEU A1010 7564 4979 12780 976 1003 -202 O ATOM 1692 CB LEU A1010 1.306 -49.303 17.422 1.00 68.31 C ANISOU 1692 CB LEU A1010 7873 4991 13092 1086 697 -420 C ATOM 1693 CG LEU A1010 0.588 -50.511 16.815 1.00 68.86 C ANISOU 1693 CG LEU A1010 8063 5230 12871 1134 664 -275 C ATOM 1694 CD1 LEU A1010 0.693 -51.718 17.722 1.00 69.24 C ANISOU 1694 CD1 LEU A1010 8012 5545 12749 1105 584 -378 C ATOM 1695 CD2 LEU A1010 -0.870 -50.181 16.530 1.00 71.24 C ANISOU 1695 CD2 LEU A1010 8426 5557 13084 1234 546 -196 C ATOM 1696 N ASN A1011 3.779 -49.413 15.561 1.00 63.88 N ANISOU 1696 N ASN A1011 7364 4238 12667 916 1085 -35 N ATOM 1697 CA ASN A1011 4.424 -50.035 14.409 1.00 64.53 C ANISOU 1697 CA ASN A1011 7568 4330 12619 969 1296 202 C ATOM 1698 C ASN A1011 5.925 -50.205 14.620 1.00 64.93 C ANISOU 1698 C ASN A1011 7369 4509 12793 907 1459 291 C ATOM 1699 O ASN A1011 6.509 -51.199 14.174 1.00 64.46 O ANISOU 1699 O ASN A1011 7353 4590 12551 1045 1629 420 O ATOM 1700 CB ASN A1011 4.148 -49.213 13.150 1.00 63.48 C ANISOU 1700 CB ASN A1011 7652 3950 12517 960 1377 386 C ATOM 1701 CG ASN A1011 2.705 -49.310 12.700 1.00 70.89 C ANISOU 1701 CG ASN A1011 8844 4810 13281 1050 1232 387 C ATOM 1702 OD1 ASN A1011 2.091 -50.373 12.776 1.00 68.09 O ANISOU 1702 OD1 ASN A1011 8601 4597 12674 1123 1143 376 O ATOM 1703 ND2 ASN A1011 2.153 -48.196 12.230 1.00 74.57 N ANISOU 1703 ND2 ASN A1011 9408 5054 13873 1028 1181 429 N ATOM 1704 N ASP A1012 6.568 -49.241 15.286 1.00 67.04 N ANISOU 1704 N ASP A1012 7395 4730 13348 710 1398 250 N ATOM 1705 CA ASP A1012 7.988 -49.369 15.605 1.00 69.56 C ANISOU 1705 CA ASP A1012 7398 5224 13810 603 1504 380 C ATOM 1706 C ASP A1012 8.254 -50.598 16.465 1.00 68.35 C ANISOU 1706 C ASP A1012 7108 5334 13527 714 1474 262 C ATOM 1707 O ASP A1012 9.145 -51.401 16.165 1.00 66.27 O ANISOU 1707 O ASP A1012 6728 5273 13179 840 1667 434 O ATOM 1708 CB ASP A1012 8.492 -48.106 16.304 1.00 73.89 C ANISOU 1708 CB ASP A1012 7770 5640 14666 299 1337 354 C ATOM 1709 CG ASP A1012 8.502 -46.898 15.391 1.00 81.50 C ANISOU 1709 CG ASP A1012 8869 6339 15757 156 1369 528 C ATOM 1710 OD1 ASP A1012 8.505 -47.085 14.156 1.00 83.48 O ANISOU 1710 OD1 ASP A1012 9242 6582 15897 272 1591 740 O ATOM 1711 OD2 ASP A1012 8.511 -45.761 15.908 1.00 85.85 O ANISOU 1711 OD2 ASP A1012 9458 6665 16496 -72 1159 455 O ATOM 1712 N ASN A1013 7.491 -50.755 17.547 1.00 67.74 N ANISOU 1712 N ASN A1013 7054 5267 13415 696 1242 -19 N ATOM 1713 CA ASN A1013 7.745 -51.848 18.478 1.00 69.51 C ANISOU 1713 CA ASN A1013 7158 5726 13528 757 1174 -143 C ATOM 1714 C ASN A1013 7.443 -53.206 17.856 1.00 65.22 C ANISOU 1714 C ASN A1013 6847 5289 12643 1004 1275 -82 C ATOM 1715 O ASN A1013 8.051 -54.209 18.246 1.00 64.03 O ANISOU 1715 O ASN A1013 6624 5326 12379 1106 1304 -79 O ATOM 1716 CB ASN A1013 6.929 -51.644 19.751 1.00 71.34 C ANISOU 1716 CB ASN A1013 7389 5943 13773 678 913 -444 C ATOM 1717 CG ASN A1013 7.648 -50.781 20.771 1.00 74.35 C ANISOU 1717 CG ASN A1013 7557 6274 14420 444 772 -531 C ATOM 1718 OD1 ASN A1013 8.872 -50.823 20.885 1.00 77.56 O ANISOU 1718 OD1 ASN A1013 7715 6782 14972 323 819 -379 O ATOM 1719 ND2 ASN A1013 6.887 -49.986 21.516 1.00 71.47 N ANISOU 1719 ND2 ASN A1013 7303 5753 14098 389 589 -750 N ATOM 1720 N LEU A1014 6.506 -53.267 16.905 1.00 65.44 N ANISOU 1720 N LEU A1014 7199 5179 12485 1098 1298 -24 N ATOM 1721 CA LEU A1014 6.311 -54.501 16.149 1.00 67.54 C ANISOU 1721 CA LEU A1014 7796 5477 12391 1305 1373 80 C ATOM 1722 C LEU A1014 7.574 -54.884 15.388 1.00 72.54 C ANISOU 1722 C LEU A1014 8414 6174 12975 1485 1672 311 C ATOM 1723 O LEU A1014 7.949 -56.062 15.346 1.00 73.32 O ANISOU 1723 O LEU A1014 8669 6378 12810 1699 1735 345 O ATOM 1724 CB LEU A1014 5.131 -54.354 15.188 1.00 68.66 C ANISOU 1724 CB LEU A1014 8295 5432 12360 1321 1314 149 C ATOM 1725 CG LEU A1014 3.729 -54.481 15.784 1.00 74.18 C ANISOU 1725 CG LEU A1014 9065 6162 12959 1233 1029 2 C ATOM 1726 CD1 LEU A1014 2.678 -54.083 14.761 1.00 77.87 C ANISOU 1726 CD1 LEU A1014 9798 6458 13331 1225 976 137 C ATOM 1727 CD2 LEU A1014 3.491 -55.900 16.275 1.00 73.54 C ANISOU 1727 CD2 LEU A1014 9145 6234 12564 1273 879 -54 C ATOM 1728 N LYS A1015 8.238 -53.903 14.772 1.00 74.32 N ANISOU 1728 N LYS A1015 8466 6344 13427 1422 1863 494 N ATOM 1729 CA LYS A1015 9.491 -54.181 14.076 1.00 74.36 C ANISOU 1729 CA LYS A1015 8368 6486 13399 1607 2189 769 C ATOM 1730 C LYS A1015 10.560 -54.665 15.046 1.00 71.55 C ANISOU 1730 C LYS A1015 7619 6415 13152 1640 2209 772 C ATOM 1731 O LYS A1015 11.326 -55.583 14.730 1.00 73.01 O ANISOU 1731 O LYS A1015 7828 6773 13140 1944 2428 927 O ATOM 1732 CB LYS A1015 9.970 -52.935 13.330 1.00 81.54 C ANISOU 1732 CB LYS A1015 9110 7317 14556 1454 2355 995 C ATOM 1733 CG LYS A1015 9.029 -52.455 12.238 1.00 88.31 C ANISOU 1733 CG LYS A1015 10365 7890 15299 1449 2362 1035 C ATOM 1734 CD LYS A1015 9.499 -51.130 11.656 1.00 97.18 C ANISOU 1734 CD LYS A1015 11314 8917 16691 1242 2473 1240 C ATOM 1735 CE LYS A1015 8.576 -50.646 10.548 1.00101.63 C ANISOU 1735 CE LYS A1015 12287 9187 17139 1244 2470 1288 C ATOM 1736 NZ LYS A1015 8.762 -51.425 9.293 1.00105.28 N ANISOU 1736 NZ LYS A1015 13106 9643 17252 1534 2752 1502 N ATOM 1737 N VAL A1016 10.631 -54.050 16.229 1.00 69.95 N ANISOU 1737 N VAL A1016 7081 6254 13242 1352 1978 613 N ATOM 1738 CA VAL A1016 11.593 -54.466 17.247 1.00 74.19 C ANISOU 1738 CA VAL A1016 7241 7049 13900 1331 1934 614 C ATOM 1739 C VAL A1016 11.397 -55.934 17.606 1.00 70.85 C ANISOU 1739 C VAL A1016 7041 6728 13149 1605 1892 481 C ATOM 1740 O VAL A1016 12.366 -56.692 17.739 1.00 69.34 O ANISOU 1740 O VAL A1016 6685 6766 12894 1821 2030 616 O ATOM 1741 CB VAL A1016 11.476 -53.558 18.486 1.00 67.28 C ANISOU 1741 CB VAL A1016 6115 6118 13331 955 1628 418 C ATOM 1742 CG1 VAL A1016 12.292 -54.114 19.645 1.00 73.65 C ANISOU 1742 CG1 VAL A1016 6599 7164 14219 912 1513 379 C ATOM 1743 CG2 VAL A1016 11.911 -52.143 18.150 1.00 69.87 C ANISOU 1743 CG2 VAL A1016 6252 6333 13964 668 1644 597 C ATOM 1744 N ILE A1017 10.141 -56.357 17.770 1.00 68.22 N ANISOU 1744 N ILE A1017 7086 6239 12595 1599 1686 244 N ATOM 1745 CA ILE A1017 9.853 -57.746 18.120 1.00 66.59 C ANISOU 1745 CA ILE A1017 7161 6093 12048 1794 1581 127 C ATOM 1746 C ILE A1017 10.286 -58.685 17.002 1.00 67.73 C ANISOU 1746 C ILE A1017 7661 6228 11846 2187 1839 334 C ATOM 1747 O ILE A1017 10.849 -59.758 17.255 1.00 71.18 O ANISOU 1747 O ILE A1017 8186 6788 12071 2444 1876 351 O ATOM 1748 CB ILE A1017 8.358 -57.909 18.449 1.00 59.86 C ANISOU 1748 CB ILE A1017 6611 5103 11028 1646 1291 -98 C ATOM 1749 CG1 ILE A1017 8.012 -57.164 19.738 1.00 58.86 C ANISOU 1749 CG1 ILE A1017 6163 5024 11176 1357 1061 -322 C ATOM 1750 CG2 ILE A1017 7.989 -59.382 18.573 1.00 57.69 C ANISOU 1750 CG2 ILE A1017 6734 4850 10338 1807 1157 -158 C ATOM 1751 CD1 ILE A1017 6.530 -57.018 19.974 1.00 59.61 C ANISOU 1751 CD1 ILE A1017 6450 5039 11161 1232 840 -479 C ATOM 1752 N GLU A1018 10.033 -58.298 15.749 1.00 69.35 N ANISOU 1752 N GLU A1018 8122 6269 11960 2267 2021 495 N ATOM 1753 CA GLU A1018 10.356 -59.166 14.620 1.00 72.77 C ANISOU 1753 CA GLU A1018 9008 6642 11999 2670 2271 685 C ATOM 1754 C GLU A1018 11.848 -59.471 14.550 1.00 82.83 C ANISOU 1754 C GLU A1018 9975 8188 13311 2992 2603 911 C ATOM 1755 O GLU A1018 12.240 -60.613 14.282 1.00 86.72 O ANISOU 1755 O GLU A1018 10805 8712 13435 3405 2727 972 O ATOM 1756 CB GLU A1018 9.873 -58.533 13.317 1.00 74.06 C ANISOU 1756 CB GLU A1018 9463 6582 12094 2660 2409 830 C ATOM 1757 CG GLU A1018 8.365 -58.530 13.167 1.00 77.40 C ANISOU 1757 CG GLU A1018 10294 6752 12363 2445 2093 679 C ATOM 1758 CD GLU A1018 7.905 -57.823 11.911 1.00 88.22 C ANISOU 1758 CD GLU A1018 11920 7899 13700 2411 2204 834 C ATOM 1759 OE1 GLU A1018 8.757 -57.507 11.056 1.00 94.82 O ANISOU 1759 OE1 GLU A1018 12722 8756 14551 2596 2549 1058 O ATOM 1760 OE2 GLU A1018 6.688 -57.584 11.779 1.00 89.73 O ANISOU 1760 OE2 GLU A1018 12330 7918 13845 2202 1947 757 O ATOM 1761 N LYS A1019 12.698 -58.471 14.783 1.00 86.19 N ANISOU 1761 N LYS A1019 9774 8816 14156 2818 2737 1065 N ATOM 1762 CA LYS A1019 14.138 -58.660 14.693 1.00 89.16 C ANISOU 1762 CA LYS A1019 9743 9528 14605 3094 3059 1363 C ATOM 1763 C LYS A1019 14.799 -58.771 16.062 1.00 85.64 C ANISOU 1763 C LYS A1019 8771 9344 14424 2947 2878 1300 C ATOM 1764 O LYS A1019 16.017 -58.596 16.173 1.00 88.90 O ANISOU 1764 O LYS A1019 8651 10088 15037 3026 3079 1589 O ATOM 1765 CB LYS A1019 14.775 -57.526 13.888 1.00 96.42 C ANISOU 1765 CB LYS A1019 10307 10546 15781 2983 3340 1690 C ATOM 1766 CG LYS A1019 14.415 -56.132 14.370 1.00 98.59 C ANISOU 1766 CG LYS A1019 10257 10712 16489 2411 3089 1604 C ATOM 1767 CD LYS A1019 15.097 -55.064 13.529 1.00107.06 C ANISOU 1767 CD LYS A1019 11025 11874 17781 2280 3345 1965 C ATOM 1768 CE LYS A1019 14.895 -55.318 12.042 1.00111.12 C ANISOU 1768 CE LYS A1019 12003 12263 17953 2624 3679 2134 C ATOM 1769 NZ LYS A1019 15.578 -54.296 11.201 1.00116.73 N ANISOU 1769 NZ LYS A1019 12411 13085 18855 2490 3945 2514 N ATOM 1770 N ALA A1020 14.022 -59.055 17.104 1.00 83.13 N ANISOU 1770 N ALA A1020 8574 8907 14104 2724 2499 958 N ATOM 1771 CA ALA A1020 14.603 -59.386 18.395 1.00 84.72 C ANISOU 1771 CA ALA A1020 8396 9327 14467 2638 2313 877 C ATOM 1772 C ALA A1020 15.282 -60.750 18.329 1.00 87.84 C ANISOU 1772 C ALA A1020 8947 9891 14536 3153 2472 977 C ATOM 1773 O ALA A1020 14.927 -61.606 17.513 1.00 84.00 O ANISOU 1773 O ALA A1020 9050 9250 13617 3532 2600 976 O ATOM 1774 CB ALA A1020 13.531 -59.378 19.485 1.00 76.94 C ANISOU 1774 CB ALA A1020 7558 8170 13507 2299 1892 490 C ATOM 1775 N ASP A1021 16.272 -60.951 19.198 1.00 92.80 N ANISOU 1775 N ASP A1021 9084 10820 15355 3173 2441 1074 N ATOM 1776 CA ASP A1021 16.990 -62.215 19.245 1.00101.77 C ANISOU 1776 CA ASP A1021 10325 12140 16204 3699 2582 1179 C ATOM 1777 C ASP A1021 16.911 -62.918 20.592 1.00 99.55 C ANISOU 1777 C ASP A1021 10024 11890 15910 3593 2223 928 C ATOM 1778 O ASP A1021 17.482 -64.005 20.736 1.00105.64 O ANISOU 1778 O ASP A1021 10916 12790 16434 4031 2292 991 O ATOM 1779 CB ASP A1021 18.463 -62.000 18.869 1.00115.33 C ANISOU 1779 CB ASP A1021 11437 14282 18103 3975 2960 1644 C ATOM 1780 CG ASP A1021 18.632 -61.040 17.708 1.00122.14 C ANISOU 1780 CG ASP A1021 12160 15167 19079 3934 3282 1928 C ATOM 1781 OD1 ASP A1021 18.943 -59.855 17.959 1.00122.86 O ANISOU 1781 OD1 ASP A1021 11704 15372 19607 3458 3209 2068 O ATOM 1782 OD2 ASP A1021 18.441 -61.462 16.549 1.00124.36 O ANISOU 1782 OD2 ASP A1021 12932 15327 18993 4358 3584 2013 O ATOM 1783 N ASN A1022 16.225 -62.343 21.578 1.00 93.91 N ANISOU 1783 N ASN A1022 9197 11057 15427 3061 1852 649 N ATOM 1784 CA ASN A1022 15.986 -63.032 22.837 1.00 86.14 C ANISOU 1784 CA ASN A1022 8282 10068 14379 2940 1500 384 C ATOM 1785 C ASN A1022 14.615 -62.639 23.369 1.00 78.20 C ANISOU 1785 C ASN A1022 7542 8799 13371 2506 1174 31 C ATOM 1786 O ASN A1022 13.993 -61.680 22.904 1.00 76.70 O ANISOU 1786 O ASN A1022 7367 8462 13315 2274 1204 5 O ATOM 1787 CB ASN A1022 17.082 -62.724 23.864 1.00 85.26 C ANISOU 1787 CB ASN A1022 7503 10258 14635 2767 1398 512 C ATOM 1788 CG ASN A1022 17.230 -61.241 24.133 1.00 83.71 C ANISOU 1788 CG ASN A1022 6828 10082 14898 2254 1318 580 C ATOM 1789 OD1 ASN A1022 16.394 -60.632 24.800 1.00 80.54 O ANISOU 1789 OD1 ASN A1022 6524 9473 14603 1839 1035 295 O ATOM 1790 ND2 ASN A1022 18.300 -60.650 23.614 1.00 86.08 N ANISOU 1790 ND2 ASN A1022 6628 10634 15445 2288 1563 981 N ATOM 1791 N ALA A1023 14.146 -63.406 24.356 1.00 73.20 N ANISOU 1791 N ALA A1023 7114 8129 12568 2421 866 -221 N ATOM 1792 CA ALA A1023 12.812 -63.184 24.901 1.00 69.25 C ANISOU 1792 CA ALA A1023 6857 7446 12007 2066 577 -521 C ATOM 1793 C ALA A1023 12.716 -61.865 25.657 1.00 68.97 C ANISOU 1793 C ALA A1023 6403 7421 12382 1633 451 -620 C ATOM 1794 O ALA A1023 11.637 -61.265 25.713 1.00 68.47 O ANISOU 1794 O ALA A1023 6483 7208 12325 1404 344 -787 O ATOM 1795 CB ALA A1023 12.417 -64.347 25.812 1.00 67.47 C ANISOU 1795 CB ALA A1023 6928 7220 11489 2065 283 -725 C ATOM 1796 N ALA A1024 13.821 -61.401 26.247 1.00 70.34 N ANISOU 1796 N ALA A1024 6085 7766 12877 1522 443 -502 N ATOM 1797 CA ALA A1024 13.778 -60.157 27.009 1.00 70.37 C ANISOU 1797 CA ALA A1024 5795 7719 13224 1094 270 -596 C ATOM 1798 C ALA A1024 13.529 -58.956 26.105 1.00 70.43 C ANISOU 1798 C ALA A1024 5767 7584 13410 983 435 -487 C ATOM 1799 O ALA A1024 12.838 -58.009 26.500 1.00 73.82 O ANISOU 1799 O ALA A1024 6244 7841 13962 701 287 -663 O ATOM 1800 CB ALA A1024 15.076 -59.978 27.796 1.00 74.71 C ANISOU 1800 CB ALA A1024 5858 8474 14056 956 173 -437 C ATOM 1801 N GLN A1025 14.084 -58.972 24.890 1.00 70.20 N ANISOU 1801 N GLN A1025 5680 7618 13374 1229 750 -192 N ATOM 1802 CA GLN A1025 13.827 -57.883 23.952 1.00 67.96 C ANISOU 1802 CA GLN A1025 5403 7187 13231 1128 907 -76 C ATOM 1803 C GLN A1025 12.372 -57.877 23.504 1.00 71.03 C ANISOU 1803 C GLN A1025 6265 7333 13391 1155 873 -293 C ATOM 1804 O GLN A1025 11.755 -56.811 23.391 1.00 69.82 O ANISOU 1804 O GLN A1025 6149 6998 13381 941 820 -367 O ATOM 1805 CB GLN A1025 14.761 -57.986 22.748 1.00 68.97 C ANISOU 1805 CB GLN A1025 5372 7472 13362 1410 1275 311 C ATOM 1806 CG GLN A1025 16.224 -57.749 23.078 1.00 79.62 C ANISOU 1806 CG GLN A1025 6133 9124 14994 1338 1327 630 C ATOM 1807 CD GLN A1025 17.133 -57.997 21.892 1.00 87.39 C ANISOU 1807 CD GLN A1025 6940 10341 15924 1704 1744 1048 C ATOM 1808 OE1 GLN A1025 16.703 -58.524 20.866 1.00 88.10 O ANISOU 1808 OE1 GLN A1025 7430 10336 15709 2068 1991 1060 O ATOM 1809 NE2 GLN A1025 18.397 -57.616 22.026 1.00 97.45 N ANISOU 1809 NE2 GLN A1025 7617 11934 17475 1607 1819 1421 N ATOM 1810 N VAL A1026 11.813 -59.059 23.234 1.00 71.50 N ANISOU 1810 N VAL A1026 6705 7381 13080 1415 882 -370 N ATOM 1811 CA VAL A1026 10.394 -59.158 22.904 1.00 67.46 C ANISOU 1811 CA VAL A1026 6612 6685 12336 1390 787 -531 C ATOM 1812 C VAL A1026 9.547 -58.624 24.052 1.00 68.31 C ANISOU 1812 C VAL A1026 6659 6753 12542 1092 509 -804 C ATOM 1813 O VAL A1026 8.573 -57.892 23.837 1.00 68.64 O ANISOU 1813 O VAL A1026 6811 6661 12610 984 471 -880 O ATOM 1814 CB VAL A1026 10.030 -60.612 22.551 1.00 62.57 C ANISOU 1814 CB VAL A1026 6442 6058 11272 1655 763 -537 C ATOM 1815 CG1 VAL A1026 8.543 -60.740 22.275 1.00 56.76 C ANISOU 1815 CG1 VAL A1026 6098 5172 10296 1553 603 -647 C ATOM 1816 CG2 VAL A1026 10.838 -61.082 21.353 1.00 65.02 C ANISOU 1816 CG2 VAL A1026 6898 6375 11432 2027 1076 -270 C ATOM 1817 N LYS A1027 9.901 -58.987 25.288 1.00 71.77 N ANISOU 1817 N LYS A1027 6936 7315 13018 987 320 -945 N ATOM 1818 CA LYS A1027 9.138 -58.531 26.446 1.00 77.84 C ANISOU 1818 CA LYS A1027 7683 8059 13834 747 79 -1205 C ATOM 1819 C LYS A1027 9.168 -57.011 26.551 1.00 78.66 C ANISOU 1819 C LYS A1027 7618 8018 14250 550 82 -1228 C ATOM 1820 O LYS A1027 8.135 -56.372 26.783 1.00 75.47 O ANISOU 1820 O LYS A1027 7342 7509 13824 480 6 -1382 O ATOM 1821 CB LYS A1027 9.691 -59.164 27.724 1.00 83.29 C ANISOU 1821 CB LYS A1027 8240 8892 14513 665 -119 -1328 C ATOM 1822 CG LYS A1027 9.102 -58.580 28.999 1.00 87.28 C ANISOU 1822 CG LYS A1027 8715 9371 15077 425 -345 -1587 C ATOM 1823 CD LYS A1027 9.655 -59.264 30.237 1.00 89.21 C ANISOU 1823 CD LYS A1027 8866 9746 15286 333 -552 -1701 C ATOM 1824 CE LYS A1027 8.909 -58.819 31.485 1.00 88.99 C ANISOU 1824 CE LYS A1027 8900 9691 15220 139 -759 -1970 C ATOM 1825 NZ LYS A1027 9.366 -59.552 32.698 1.00 89.91 N ANISOU 1825 NZ LYS A1027 8972 9926 15264 37 -978 -2087 N ATOM 1826 N ASP A1028 10.357 -56.420 26.404 1.00 83.11 N ANISOU 1826 N ASP A1028 7904 8585 15090 462 154 -1051 N ATOM 1827 CA ASP A1028 10.497 -54.970 26.496 1.00 85.70 C ANISOU 1827 CA ASP A1028 8133 8732 15696 227 105 -1043 C ATOM 1828 C ASP A1028 9.562 -54.261 25.522 1.00 76.14 C ANISOU 1828 C ASP A1028 7145 7331 14455 299 229 -1030 C ATOM 1829 O ASP A1028 8.846 -53.327 25.899 1.00 77.98 O ANISOU 1829 O ASP A1028 7507 7382 14739 198 118 -1194 O ATOM 1830 CB ASP A1028 11.950 -54.566 26.245 1.00 97.06 C ANISOU 1830 CB ASP A1028 9223 10248 17409 97 170 -748 C ATOM 1831 CG ASP A1028 12.770 -54.512 27.521 1.00106.59 C ANISOU 1831 CG ASP A1028 10195 11535 18768 -152 -85 -787 C ATOM 1832 OD1 ASP A1028 12.709 -53.482 28.224 1.00111.25 O ANISOU 1832 OD1 ASP A1028 10834 11929 19506 -443 -307 -901 O ATOM 1833 OD2 ASP A1028 13.474 -55.499 27.820 1.00109.33 O ANISOU 1833 OD2 ASP A1028 10352 12120 19068 -48 -81 -699 O ATOM 1834 N ALA A1029 9.562 -54.690 24.257 1.00 69.88 N ANISOU 1834 N ALA A1029 6431 6564 13555 500 460 -831 N ATOM 1835 CA ALA A1029 8.740 -54.015 23.258 1.00 67.07 C ANISOU 1835 CA ALA A1029 6284 6022 13178 554 567 -785 C ATOM 1836 C ALA A1029 7.254 -54.245 23.510 1.00 63.91 C ANISOU 1836 C ALA A1029 6138 5592 12554 627 452 -989 C ATOM 1837 O ALA A1029 6.437 -53.345 23.284 1.00 66.89 O ANISOU 1837 O ALA A1029 6628 5809 12978 612 434 -1040 O ATOM 1838 CB ALA A1029 9.128 -54.483 21.857 1.00 63.91 C ANISOU 1838 CB ALA A1029 5954 5652 12679 754 835 -513 C ATOM 1839 N LEU A1030 6.882 -55.439 23.979 1.00 59.40 N ANISOU 1839 N LEU A1030 5651 5188 11730 707 363 -1079 N ATOM 1840 CA LEU A1030 5.469 -55.722 24.221 1.00 59.69 C ANISOU 1840 CA LEU A1030 5873 5267 11540 738 241 -1203 C ATOM 1841 C LEU A1030 4.934 -54.907 25.391 1.00 58.83 C ANISOU 1841 C LEU A1030 5679 5146 11526 639 98 -1429 C ATOM 1842 O LEU A1030 3.795 -54.425 25.350 1.00 57.89 O ANISOU 1842 O LEU A1030 5648 5008 11340 697 75 -1474 O ATOM 1843 CB LEU A1030 5.253 -57.214 24.469 1.00 58.84 C ANISOU 1843 CB LEU A1030 5902 5337 11118 792 141 -1213 C ATOM 1844 CG LEU A1030 5.340 -58.173 23.284 1.00 55.36 C ANISOU 1844 CG LEU A1030 5734 4868 10433 947 237 -1012 C ATOM 1845 CD1 LEU A1030 5.539 -59.587 23.788 1.00 52.80 C ANISOU 1845 CD1 LEU A1030 5554 4675 9831 988 104 -1047 C ATOM 1846 CD2 LEU A1030 4.081 -58.076 22.439 1.00 52.53 C ANISOU 1846 CD2 LEU A1030 5618 4437 9904 955 208 -915 C ATOM 1847 N ATHR A1031 5.735 -54.753 26.448 1.00 62.30 N ANISOU 1847 N ATHR A1031 5968 5603 12100 514 -2 -1555 N ATOM 1848 CA ATHR A1031 5.302 -53.961 27.595 1.00 67.07 C ANISOU 1848 CA ATHR A1031 6582 6151 12752 444 -140 -1782 C ATOM 1849 C ATHR A1031 5.089 -52.504 27.205 1.00 66.33 C ANISOU 1849 C ATHR A1031 6574 5790 12837 450 -94 -1780 C ATOM 1850 O ATHR A1031 4.145 -51.858 27.676 1.00 64.13 O ANISOU 1850 O ATHR A1031 6420 5456 12489 547 -136 -1926 O ATOM 1851 CB ATHR A1031 6.323 -54.070 28.728 1.00 73.01 C ANISOU 1851 CB ATHR A1031 7206 6926 13607 270 -289 -1890 C ATOM 1852 OG1ATHR A1031 7.634 -53.794 28.218 1.00 85.16 O ANISOU 1852 OG1ATHR A1031 8580 8387 15390 155 -235 -1699 O ATOM 1853 CG2ATHR A1031 6.303 -55.465 29.334 1.00 65.62 C ANISOU 1853 CG2ATHR A1031 6241 6242 12451 286 -376 -1944 C ATOM 1854 N LYS A1032 5.957 -51.970 26.343 1.00 66.78 N ANISOU 1854 N LYS A1032 6579 5690 13106 367 -2 -1596 N ATOM 1855 CA LYS A1032 5.756 -50.617 25.839 1.00 73.25 C ANISOU 1855 CA LYS A1032 7529 6225 14076 355 24 -1566 C ATOM 1856 C LYS A1032 4.525 -50.535 24.947 1.00 73.92 C ANISOU 1856 C LYS A1032 7758 6301 14027 572 138 -1511 C ATOM 1857 O LYS A1032 3.849 -49.501 24.916 1.00 78.80 O ANISOU 1857 O LYS A1032 8536 6727 14676 659 118 -1578 O ATOM 1858 CB LYS A1032 6.999 -50.153 25.080 1.00 78.59 C ANISOU 1858 CB LYS A1032 8084 6783 14993 174 92 -1327 C ATOM 1859 CG LYS A1032 8.207 -49.906 25.967 1.00 81.92 C ANISOU 1859 CG LYS A1032 8346 7185 15594 -101 -76 -1324 C ATOM 1860 CD LYS A1032 9.432 -49.545 25.145 1.00 85.31 C ANISOU 1860 CD LYS A1032 8567 7596 16251 -290 9 -1000 C ATOM 1861 CE LYS A1032 10.578 -49.099 26.037 1.00 91.93 C ANISOU 1861 CE LYS A1032 9240 8401 17288 -635 -222 -943 C ATOM 1862 NZ LYS A1032 11.795 -48.759 25.250 1.00 97.58 N ANISOU 1862 NZ LYS A1032 9671 9178 18228 -848 -141 -552 N ATOM 1863 N MET A1033 4.223 -51.611 24.216 1.00 68.62 N ANISOU 1863 N MET A1033 7068 5816 13188 666 233 -1376 N ATOM 1864 CA MET A1033 3.009 -51.643 23.407 1.00 65.20 C ANISOU 1864 CA MET A1033 6768 5401 12604 825 287 -1288 C ATOM 1865 C MET A1033 1.762 -51.685 24.281 1.00 61.58 C ANISOU 1865 C MET A1033 6316 5106 11975 941 184 -1437 C ATOM 1866 O MET A1033 0.747 -51.057 23.954 1.00 59.01 O ANISOU 1866 O MET A1033 6059 4744 11616 1088 203 -1403 O ATOM 1867 CB MET A1033 3.043 -52.846 22.467 1.00 67.92 C ANISOU 1867 CB MET A1033 7173 5869 12763 859 360 -1095 C ATOM 1868 CG MET A1033 4.020 -52.693 21.323 1.00 71.95 C ANISOU 1868 CG MET A1033 7713 6232 13392 842 532 -891 C ATOM 1869 SD MET A1033 4.107 -54.148 20.266 1.00 73.04 S ANISOU 1869 SD MET A1033 8052 6467 13233 954 625 -687 S ATOM 1870 CE MET A1033 2.455 -54.151 19.588 1.00 71.37 C ANISOU 1870 CE MET A1033 8077 6229 12812 1006 529 -608 C ATOM 1871 N ARG A1034 1.815 -52.425 25.391 1.00 60.53 N ANISOU 1871 N ARG A1034 6095 5180 11722 891 82 -1579 N ATOM 1872 CA ARG A1034 0.627 -52.603 26.220 1.00 62.69 C ANISOU 1872 CA ARG A1034 6339 5687 11794 1002 10 -1675 C ATOM 1873 C ARG A1034 0.230 -51.303 26.909 1.00 69.50 C ANISOU 1873 C ARG A1034 7265 6406 12735 1151 15 -1847 C ATOM 1874 O ARG A1034 -0.950 -50.934 26.928 1.00 76.44 O ANISOU 1874 O ARG A1034 8146 7399 13499 1366 51 -1819 O ATOM 1875 CB ARG A1034 0.867 -53.701 27.255 1.00 57.03 C ANISOU 1875 CB ARG A1034 5539 5209 10919 891 -106 -1781 C ATOM 1876 CG ARG A1034 -0.404 -54.180 27.928 1.00 59.42 C ANISOU 1876 CG ARG A1034 5778 5841 10958 967 -172 -1790 C ATOM 1877 CD ARG A1034 -0.111 -55.136 29.069 1.00 63.57 C ANISOU 1877 CD ARG A1034 6251 6570 11333 836 -301 -1918 C ATOM 1878 NE ARG A1034 -1.331 -55.774 29.554 1.00 73.96 N ANISOU 1878 NE ARG A1034 7483 8254 12362 856 -371 -1846 N ATOM 1879 CZ ARG A1034 -2.167 -55.216 30.424 1.00 81.54 C ANISOU 1879 CZ ARG A1034 8359 9390 13232 1014 -333 -1934 C ATOM 1880 NH1 ARG A1034 -1.917 -54.005 30.905 1.00 86.51 N ANISOU 1880 NH1 ARG A1034 9063 9793 14012 1180 -246 -2133 N ATOM 1881 NH2 ARG A1034 -3.255 -55.866 30.812 1.00 83.12 N ANISOU 1881 NH2 ARG A1034 8424 9994 13164 1010 -388 -1800 N ATOM 1882 N ALA A1035 1.205 -50.597 27.488 1.00 71.58 N ANISOU 1882 N ALA A1035 7605 6418 13173 1049 -34 -2004 N ATOM 1883 CA ALA A1035 0.923 -49.298 28.089 1.00 70.44 C ANISOU 1883 CA ALA A1035 7657 6037 13069 1195 -60 -2174 C ATOM 1884 C ALA A1035 0.436 -48.291 27.057 1.00 72.61 C ANISOU 1884 C ALA A1035 8070 6085 13436 1355 27 -2058 C ATOM 1885 O ALA A1035 -0.401 -47.437 27.370 1.00 75.91 O ANISOU 1885 O ALA A1035 8647 6422 13775 1631 49 -2148 O ATOM 1886 CB ALA A1035 2.166 -48.767 28.803 1.00 69.01 C ANISOU 1886 CB ALA A1035 7590 5583 13050 966 -198 -2316 C ATOM 1887 N ALA A1036 0.944 -48.374 25.825 1.00 71.23 N ANISOU 1887 N ALA A1036 7855 5804 13404 1220 87 -1852 N ATOM 1888 CA ALA A1036 0.493 -47.466 24.776 1.00 70.89 C ANISOU 1888 CA ALA A1036 7954 5539 13443 1347 157 -1724 C ATOM 1889 C ALA A1036 -0.914 -47.815 24.308 1.00 75.22 C ANISOU 1889 C ALA A1036 8425 6343 13812 1595 226 -1596 C ATOM 1890 O ALA A1036 -1.711 -46.921 24.002 1.00 76.92 O ANISOU 1890 O ALA A1036 8759 6442 14024 1836 258 -1568 O ATOM 1891 CB ALA A1036 1.472 -47.492 23.604 1.00 66.09 C ANISOU 1891 CB ALA A1036 7327 4770 13014 1123 215 -1521 C ATOM 1892 N ALA A1037 -1.232 -49.110 24.236 1.00 73.81 N ANISOU 1892 N ALA A1037 8061 6510 13472 1528 221 -1489 N ATOM 1893 CA ALA A1037 -2.562 -49.528 23.802 1.00 72.23 C ANISOU 1893 CA ALA A1037 7765 6592 13089 1681 229 -1302 C ATOM 1894 C ALA A1037 -3.636 -49.018 24.754 1.00 76.33 C ANISOU 1894 C ALA A1037 8216 7302 13483 1979 240 -1397 C ATOM 1895 O ALA A1037 -4.673 -48.502 24.321 1.00 75.63 O ANISOU 1895 O ALA A1037 8099 7286 13351 2224 283 -1254 O ATOM 1896 CB ALA A1037 -2.622 -51.051 23.685 1.00 68.76 C ANISOU 1896 CB ALA A1037 7210 6453 12461 1493 159 -1170 C ATOM 1897 N LEU A1038 -3.407 -49.159 26.062 1.00 81.05 N ANISOU 1897 N LEU A1038 8789 8002 14006 1991 212 -1621 N ATOM 1898 CA LEU A1038 -4.346 -48.613 27.036 1.00 87.31 C ANISOU 1898 CA LEU A1038 9561 8967 14645 2332 264 -1726 C ATOM 1899 C LEU A1038 -4.404 -47.092 26.975 1.00 97.72 C ANISOU 1899 C LEU A1038 11165 9899 16067 2623 321 -1844 C ATOM 1900 O LEU A1038 -5.459 -46.502 27.237 1.00100.81 O ANISOU 1900 O LEU A1038 11553 10422 16326 3027 411 -1819 O ATOM 1901 CB LEU A1038 -3.966 -49.075 28.442 1.00 85.59 C ANISOU 1901 CB LEU A1038 9328 8885 14307 2262 215 -1956 C ATOM 1902 CG LEU A1038 -3.834 -50.587 28.629 1.00 83.76 C ANISOU 1902 CG LEU A1038 8877 8996 13951 1970 126 -1866 C ATOM 1903 CD1 LEU A1038 -3.573 -50.931 30.087 1.00 83.21 C ANISOU 1903 CD1 LEU A1038 8808 9061 13746 1936 75 -2096 C ATOM 1904 CD2 LEU A1038 -5.085 -51.288 28.131 1.00 85.97 C ANISOU 1904 CD2 LEU A1038 8912 9710 14044 2018 127 -1558 C ATOM 1905 N ASP A1039 -3.287 -46.441 26.640 1.00102.95 N ANISOU 1905 N ASP A1039 12080 10093 16944 2431 263 -1947 N ATOM 1906 CA ASP A1039 -3.285 -44.986 26.531 1.00111.26 C ANISOU 1906 CA ASP A1039 13486 10712 18076 2653 263 -2046 C ATOM 1907 C ASP A1039 -4.115 -44.521 25.341 1.00108.97 C ANISOU 1907 C ASP A1039 13182 10398 17824 2863 337 -1816 C ATOM 1908 O ASP A1039 -4.777 -43.478 25.406 1.00116.82 O ANISOU 1908 O ASP A1039 14394 11229 18764 3250 378 -1857 O ATOM 1909 CB ASP A1039 -1.850 -44.471 26.421 1.00119.72 C ANISOU 1909 CB ASP A1039 14801 11322 19366 2300 137 -2144 C ATOM 1910 CG ASP A1039 -1.732 -42.997 26.753 1.00131.81 C ANISOU 1910 CG ASP A1039 16810 12361 20911 2471 54 -2313 C ATOM 1911 OD1 ASP A1039 -1.799 -42.649 27.950 1.00137.20 O ANISOU 1911 OD1 ASP A1039 17728 12963 21438 2632 -2 -2549 O ATOM 1912 OD2 ASP A1039 -1.572 -42.185 25.816 1.00135.78 O ANISOU 1912 OD2 ASP A1039 17509 12549 21533 2433 32 -2197 O ATOM 1913 N ALA A1040 -4.090 -45.282 24.246 1.00101.47 N ANISOU 1913 N ALA A1040 12021 9590 16943 2634 346 -1567 N ATOM 1914 CA ALA A1040 -4.921 -44.988 23.085 1.00 98.75 C ANISOU 1914 CA ALA A1040 11647 9258 16616 2790 388 -1314 C ATOM 1915 C ALA A1040 -6.371 -45.416 23.263 1.00 99.86 C ANISOU 1915 C ALA A1040 11500 9892 16552 3082 434 -1134 C ATOM 1916 O ALA A1040 -7.234 -44.957 22.507 1.00 99.55 O ANISOU 1916 O ALA A1040 11433 9882 16511 3306 458 -925 O ATOM 1917 CB ALA A1040 -4.340 -45.659 21.839 1.00 92.99 C ANISOU 1917 CB ALA A1040 10869 8472 15993 2433 367 -1106 C ATOM 1918 N GLN A1041 -6.661 -46.280 24.238 1.00 99.08 N ANISOU 1918 N GLN A1041 11165 10203 16278 3070 436 -1175 N ATOM 1919 CA GLN A1041 -8.044 -46.671 24.485 1.00102.73 C ANISOU 1919 CA GLN A1041 11299 11200 16533 3323 476 -951 C ATOM 1920 C GLN A1041 -8.813 -45.607 25.258 1.00107.76 C ANISOU 1920 C GLN A1041 11997 11880 17066 3886 610 -1053 C ATOM 1921 O GLN A1041 -10.035 -45.501 25.104 1.00112.24 O ANISOU 1921 O GLN A1041 12308 12822 17517 4212 678 -793 O ATOM 1922 CB GLN A1041 -8.082 -48.001 25.240 1.00100.75 C ANISOU 1922 CB GLN A1041 10785 11386 16107 3078 417 -928 C ATOM 1923 CG GLN A1041 -9.455 -48.650 25.307 1.00104.36 C ANISOU 1923 CG GLN A1041 10842 12461 16348 3180 405 -586 C ATOM 1924 CD GLN A1041 -9.414 -50.033 25.926 1.00105.61 C ANISOU 1924 CD GLN A1041 10799 13002 16327 2844 294 -534 C ATOM 1925 OE1 GLN A1041 -8.475 -50.376 26.646 1.00105.89 O ANISOU 1925 OE1 GLN A1041 10972 12889 16372 2669 273 -814 O ATOM 1926 NE2 GLN A1041 -10.433 -50.837 25.647 1.00106.81 N ANISOU 1926 NE2 GLN A1041 10633 13644 16305 2728 189 -149 N ATOM 1927 N LYS A1042 -8.130 -44.819 26.081 1.00105.76 N ANISOU 1927 N LYS A1042 12098 11256 16831 4022 639 -1401 N ATOM 1928 CA LYS A1042 -8.781 -43.753 26.834 1.00107.62 C ANISOU 1928 CA LYS A1042 12531 11442 16916 4613 768 -1535 C ATOM 1929 C LYS A1042 -9.326 -42.671 25.904 1.00108.07 C ANISOU 1929 C LYS A1042 12760 11249 17054 4959 804 -1400 C ATOM 1930 O LYS A1042 -10.537 -42.543 25.726 1.00109.21 O ANISOU 1930 O LYS A1042 12642 11771 17082 5370 914 -1149 O ATOM 1931 CB LYS A1042 -7.815 -43.142 27.849 1.00109.16 C ANISOU 1931 CB LYS A1042 13197 11188 17092 4609 723 -1940 C ATOM 1932 CG LYS A1042 -7.395 -44.102 28.950 1.00108.55 C ANISOU 1932 CG LYS A1042 12976 11373 16897 4362 694 -2088 C ATOM 1933 CD LYS A1042 -6.492 -43.424 29.965 1.00111.82 C ANISOU 1933 CD LYS A1042 13895 11320 17273 4357 613 -2464 C ATOM 1934 CE LYS A1042 -6.147 -44.365 31.109 1.00109.87 C ANISOU 1934 CE LYS A1042 13509 11348 16889 4142 579 -2605 C ATOM 1935 NZ LYS A1042 -5.326 -43.692 32.153 1.00111.92 N ANISOU 1935 NZ LYS A1042 14293 11151 17081 4132 466 -2955 N ATOM 1936 N ASP A1060 -17.404 -51.903 18.501 1.00123.54 N ANISOU 1936 N ASP A1060 11498 17355 18085 1941 -1126 3365 N ATOM 1937 CA ASP A1060 -16.314 -52.381 17.658 1.00123.28 C ANISOU 1937 CA ASP A1060 12092 16679 18071 1560 -1254 3131 C ATOM 1938 C ASP A1060 -14.997 -51.704 18.024 1.00120.67 C ANISOU 1938 C ASP A1060 12104 15803 17943 1829 -929 2503 C ATOM 1939 O ASP A1060 -13.922 -52.275 17.836 1.00116.85 O ANISOU 1939 O ASP A1060 12032 14923 17442 1556 -957 2238 O ATOM 1940 CB ASP A1060 -16.634 -52.140 16.181 1.00126.59 C ANISOU 1940 CB ASP A1060 12740 16824 18536 1420 -1457 3440 C ATOM 1941 CG ASP A1060 -18.105 -52.329 15.866 1.00134.96 C ANISOU 1941 CG ASP A1060 13337 18467 19474 1308 -1736 4104 C ATOM 1942 OD1 ASP A1060 -18.674 -53.359 16.283 1.00137.67 O ANISOU 1942 OD1 ASP A1060 13435 19293 19579 936 -1993 4438 O ATOM 1943 OD2 ASP A1060 -18.692 -51.445 15.208 1.00139.10 O ANISOU 1943 OD2 ASP A1060 13733 18980 20137 1577 -1716 4320 O ATOM 1944 N PHE A1061 -15.088 -50.476 18.540 1.00120.39 N ANISOU 1944 N PHE A1061 11911 15749 18081 2373 -636 2294 N ATOM 1945 CA PHE A1061 -13.922 -49.837 19.141 1.00114.38 C ANISOU 1945 CA PHE A1061 11431 14547 17479 2597 -371 1731 C ATOM 1946 C PHE A1061 -13.413 -50.632 20.337 1.00110.35 C ANISOU 1946 C PHE A1061 10863 14222 16845 2448 -337 1488 C ATOM 1947 O PHE A1061 -12.223 -50.959 20.419 1.00106.15 O ANISOU 1947 O PHE A1061 10659 13310 16365 2242 -314 1158 O ATOM 1948 CB PHE A1061 -14.266 -48.399 19.542 1.00117.02 C ANISOU 1948 CB PHE A1061 11672 14839 17952 3215 -118 1592 C ATOM 1949 CG PHE A1061 -13.356 -47.818 20.594 1.00114.52 C ANISOU 1949 CG PHE A1061 11556 14244 17711 3460 113 1072 C ATOM 1950 CD1 PHE A1061 -12.202 -47.143 20.233 1.00110.99 C ANISOU 1950 CD1 PHE A1061 11561 13149 17461 3437 184 723 C ATOM 1951 CD2 PHE A1061 -13.676 -47.911 21.942 1.00115.96 C ANISOU 1951 CD2 PHE A1061 11485 14822 17751 3702 244 964 C ATOM 1952 CE1 PHE A1061 -11.370 -46.601 21.196 1.00110.32 C ANISOU 1952 CE1 PHE A1061 11682 12800 17436 3602 335 289 C ATOM 1953 CE2 PHE A1061 -12.846 -47.371 22.907 1.00114.47 C ANISOU 1953 CE2 PHE A1061 11544 14342 17606 3901 415 496 C ATOM 1954 CZ PHE A1061 -11.693 -46.714 22.533 1.00111.55 C ANISOU 1954 CZ PHE A1061 11635 13308 17439 3833 439 164 C ATOM 1955 N ARG A1062 -14.303 -50.946 21.282 1.00113.46 N ANISOU 1955 N ARG A1062 10818 15225 17067 2562 -328 1672 N ATOM 1956 CA ARG A1062 -13.886 -51.676 22.475 1.00111.60 C ANISOU 1956 CA ARG A1062 10523 15183 16695 2431 -299 1451 C ATOM 1957 C ARG A1062 -13.401 -53.076 22.126 1.00100.63 C ANISOU 1957 C ARG A1062 9341 13733 15161 1834 -579 1530 C ATOM 1958 O ARG A1062 -12.425 -53.566 22.705 1.00 94.34 O ANISOU 1958 O ARG A1062 8758 12739 14349 1682 -556 1197 O ATOM 1959 CB ARG A1062 -15.033 -51.736 23.484 1.00122.37 C ANISOU 1959 CB ARG A1062 11357 17267 17874 2674 -225 1700 C ATOM 1960 CG ARG A1062 -14.787 -52.687 24.645 1.00127.75 C ANISOU 1960 CG ARG A1062 11944 18237 18360 2448 -257 1577 C ATOM 1961 CD ARG A1062 -15.602 -52.304 25.868 1.00135.87 C ANISOU 1961 CD ARG A1062 12545 19836 19245 2886 -27 1634 C ATOM 1962 NE ARG A1062 -15.137 -51.051 26.455 1.00139.64 N ANISOU 1962 NE ARG A1062 13236 19971 19849 3457 295 1187 N ATOM 1963 CZ ARG A1062 -14.089 -50.951 27.268 1.00138.30 C ANISOU 1963 CZ ARG A1062 13395 19440 19711 3470 392 689 C ATOM 1964 NH1 ARG A1062 -13.392 -52.031 27.592 1.00135.78 N ANISOU 1964 NH1 ARG A1062 13187 19080 19324 2985 223 568 N ATOM 1965 NH2 ARG A1062 -13.735 -49.770 27.757 1.00139.25 N ANISOU 1965 NH2 ARG A1062 13769 19223 19916 3961 630 326 N ATOM 1966 N HIS A1063 -14.072 -53.734 21.178 1.00 95.39 N ANISOU 1966 N HIS A1063 8657 13216 14370 1499 -867 1983 N ATOM 1967 CA HIS A1063 -13.650 -55.068 20.767 1.00 87.08 C ANISOU 1967 CA HIS A1063 7923 12042 13123 956 -1167 2072 C ATOM 1968 C HIS A1063 -12.246 -55.045 20.175 1.00 75.89 C ANISOU 1968 C HIS A1063 7048 9951 11837 900 -1085 1692 C ATOM 1969 O HIS A1063 -11.415 -55.899 20.503 1.00 70.52 O ANISOU 1969 O HIS A1063 6618 9124 11053 678 -1143 1490 O ATOM 1970 CB HIS A1063 -14.649 -55.652 19.767 1.00 89.80 C ANISOU 1970 CB HIS A1063 8237 12595 13289 606 -1528 2646 C ATOM 1971 CG HIS A1063 -14.449 -57.110 19.492 1.00 91.54 C ANISOU 1971 CG HIS A1063 8811 12758 13213 42 -1899 2804 C ATOM 1972 ND1 HIS A1063 -14.405 -58.057 20.494 1.00 90.82 N ANISOU 1972 ND1 HIS A1063 8637 12960 12910 -189 -2012 2776 N ATOM 1973 CD2 HIS A1063 -14.288 -57.786 18.330 1.00 91.67 C ANISOU 1973 CD2 HIS A1063 9331 12427 13074 -322 -2196 2992 C ATOM 1974 CE1 HIS A1063 -14.222 -59.252 19.960 1.00 89.95 C ANISOU 1974 CE1 HIS A1063 8979 12670 12528 -670 -2378 2937 C ATOM 1975 NE2 HIS A1063 -14.148 -59.115 18.648 1.00 90.23 N ANISOU 1975 NE2 HIS A1063 9395 12309 12579 -746 -2491 3067 N ATOM 1976 N GLY A1064 -11.963 -54.071 19.306 1.00 75.51 N ANISOU 1976 N GLY A1064 7171 9510 12009 1113 -944 1617 N ATOM 1977 CA GLY A1064 -10.640 -53.987 18.705 1.00 63.14 C ANISOU 1977 CA GLY A1064 6062 7361 10567 1070 -838 1315 C ATOM 1978 C GLY A1064 -9.527 -53.855 19.727 1.00 61.28 C ANISOU 1978 C GLY A1064 5852 6982 10449 1188 -628 858 C ATOM 1979 O GLY A1064 -8.498 -54.528 19.632 1.00 62.39 O ANISOU 1979 O GLY A1064 6280 6877 10550 1007 -640 691 O ATOM 1980 N PHE A1065 -9.713 -52.981 20.720 1.00 62.53 N ANISOU 1980 N PHE A1065 5736 7288 10734 1512 -440 665 N ATOM 1981 CA PHE A1065 -8.688 -52.832 21.748 1.00 63.65 C ANISOU 1981 CA PHE A1065 5926 7285 10971 1588 -287 251 C ATOM 1982 C PHE A1065 -8.659 -54.021 22.698 1.00 65.91 C ANISOU 1982 C PHE A1065 6112 7892 11037 1364 -412 224 C ATOM 1983 O PHE A1065 -7.597 -54.346 23.242 1.00 64.56 O ANISOU 1983 O PHE A1065 6082 7545 10905 1278 -373 -62 O ATOM 1984 CB PHE A1065 -8.890 -51.530 22.523 1.00 64.60 C ANISOU 1984 CB PHE A1065 5905 7400 11241 2006 -79 43 C ATOM 1985 CG PHE A1065 -8.299 -50.326 21.846 1.00 68.41 C ANISOU 1985 CG PHE A1065 6631 7384 11976 2180 51 -103 C ATOM 1986 CD1 PHE A1065 -6.939 -50.074 21.922 1.00 67.36 C ANISOU 1986 CD1 PHE A1065 6745 6838 12010 2080 122 -397 C ATOM 1987 CD2 PHE A1065 -9.099 -49.447 21.133 1.00 74.26 C ANISOU 1987 CD2 PHE A1065 7344 8086 12784 2425 82 88 C ATOM 1988 CE1 PHE A1065 -6.385 -48.970 21.300 1.00 70.48 C ANISOU 1988 CE1 PHE A1065 7364 6791 12625 2181 212 -488 C ATOM 1989 CE2 PHE A1065 -8.551 -48.340 20.508 1.00 74.62 C ANISOU 1989 CE2 PHE A1065 7654 7653 13046 2555 174 -37 C ATOM 1990 CZ PHE A1065 -7.193 -48.100 20.593 1.00 73.98 C ANISOU 1990 CZ PHE A1065 7827 7163 13119 2413 234 -321 C ATOM 1991 N ASP A1066 -9.802 -54.678 22.917 1.00 70.75 N ANISOU 1991 N ASP A1066 6472 8991 11418 1247 -581 547 N ATOM 1992 CA ASP A1066 -9.805 -55.881 23.744 1.00 74.01 C ANISOU 1992 CA ASP A1066 6830 9699 11590 974 -744 563 C ATOM 1993 C ASP A1066 -8.984 -56.988 23.096 1.00 66.90 C ANISOU 1993 C ASP A1066 6342 8506 10573 624 -933 560 C ATOM 1994 O ASP A1066 -8.202 -57.668 23.772 1.00 66.24 O ANISOU 1994 O ASP A1066 6380 8368 10421 506 -961 339 O ATOM 1995 CB ASP A1066 -11.239 -56.346 23.997 1.00 88.07 C ANISOU 1995 CB ASP A1066 8243 12087 13134 867 -916 993 C ATOM 1996 CG ASP A1066 -11.925 -55.548 25.088 1.00 99.43 C ANISOU 1996 CG ASP A1066 9256 13927 14596 1254 -691 948 C ATOM 1997 OD1 ASP A1066 -11.217 -55.007 25.964 1.00101.95 O ANISOU 1997 OD1 ASP A1066 9636 14075 15026 1496 -477 537 O ATOM 1998 OD2 ASP A1066 -13.171 -55.464 25.072 1.00104.93 O ANISOU 1998 OD2 ASP A1066 9569 15118 15181 1325 -735 1345 O ATOM 1999 N ILE A1067 -9.157 -57.190 21.788 1.00 59.15 N ANISOU 1999 N ILE A1067 5610 7323 9541 481 -1068 812 N ATOM 2000 CA ILE A1067 -8.310 -58.130 21.058 1.00 61.11 C ANISOU 2000 CA ILE A1067 6346 7222 9653 249 -1200 793 C ATOM 2001 C ILE A1067 -6.850 -57.706 21.148 1.00 54.72 C ANISOU 2001 C ILE A1067 5698 6017 9075 436 -937 398 C ATOM 2002 O ILE A1067 -5.961 -58.527 21.403 1.00 53.29 O ANISOU 2002 O ILE A1067 5740 5712 8795 338 -971 247 O ATOM 2003 CB ILE A1067 -8.769 -58.255 19.594 1.00 57.52 C ANISOU 2003 CB ILE A1067 6184 6579 9093 112 -1366 1126 C ATOM 2004 CG1 ILE A1067 -10.259 -58.587 19.520 1.00 59.98 C ANISOU 2004 CG1 ILE A1067 6264 7327 9198 -109 -1662 1583 C ATOM 2005 CG2 ILE A1067 -7.940 -59.290 18.864 1.00 60.96 C ANISOU 2005 CG2 ILE A1067 7202 6650 9308 -74 -1495 1114 C ATOM 2006 CD1 ILE A1067 -10.861 -58.374 18.150 1.00 61.50 C ANISOU 2006 CD1 ILE A1067 6650 7365 9351 -202 -1815 1928 C ATOM 2007 N LEU A1068 -6.584 -56.414 20.938 1.00 55.10 N ANISOU 2007 N LEU A1068 5637 5872 9427 700 -690 257 N ATOM 2008 CA LEU A1068 -5.206 -55.939 20.866 1.00 53.94 C ANISOU 2008 CA LEU A1068 5630 5356 9510 817 -472 -32 C ATOM 2009 C LEU A1068 -4.476 -56.171 22.182 1.00 53.00 C ANISOU 2009 C LEU A1068 5381 5326 9432 824 -425 -328 C ATOM 2010 O LEU A1068 -3.377 -56.737 22.204 1.00 52.40 O ANISOU 2010 O LEU A1068 5472 5084 9353 759 -399 -453 O ATOM 2011 CB LEU A1068 -5.180 -54.457 20.493 1.00 55.08 C ANISOU 2011 CB LEU A1068 5691 5288 9948 1051 -274 -99 C ATOM 2012 CG LEU A1068 -3.798 -53.901 20.152 1.00 54.51 C ANISOU 2012 CG LEU A1068 5771 4828 10111 1102 -82 -292 C ATOM 2013 CD1 LEU A1068 -3.330 -54.451 18.814 1.00 54.03 C ANISOU 2013 CD1 LEU A1068 6039 4535 9954 1003 -79 -113 C ATOM 2014 CD2 LEU A1068 -3.795 -52.379 20.148 1.00 56.02 C ANISOU 2014 CD2 LEU A1068 5882 4827 10577 1301 64 -398 C ATOM 2015 N VAL A1069 -5.072 -55.731 23.292 1.00 53.89 N ANISOU 2015 N VAL A1069 5201 5707 9568 928 -406 -428 N ATOM 2016 CA VAL A1069 -4.446 -55.918 24.597 1.00 56.76 C ANISOU 2016 CA VAL A1069 5468 6149 9949 922 -383 -706 C ATOM 2017 C VAL A1069 -4.320 -57.402 24.919 1.00 54.85 C ANISOU 2017 C VAL A1069 5328 6077 9435 673 -584 -649 C ATOM 2018 O VAL A1069 -3.298 -57.853 25.451 1.00 53.14 O ANISOU 2018 O VAL A1069 5191 5758 9241 617 -583 -848 O ATOM 2019 CB VAL A1069 -5.235 -55.162 25.682 1.00 62.56 C ANISOU 2019 CB VAL A1069 5932 7143 10695 1124 -313 -802 C ATOM 2020 CG1 VAL A1069 -4.645 -55.433 27.060 1.00 54.54 C ANISOU 2020 CG1 VAL A1069 4866 6207 9650 1091 -320 -1079 C ATOM 2021 CG2 VAL A1069 -5.239 -53.671 25.384 1.00 61.96 C ANISOU 2021 CG2 VAL A1069 5864 6814 10865 1403 -132 -891 C ATOM 2022 N GLY A1070 -5.357 -58.182 24.603 1.00 53.91 N ANISOU 2022 N GLY A1070 5222 6216 9046 505 -789 -352 N ATOM 2023 CA GLY A1070 -5.286 -59.616 24.834 1.00 51.74 C ANISOU 2023 CA GLY A1070 5135 6054 8468 235 -1035 -271 C ATOM 2024 C GLY A1070 -4.191 -60.288 24.027 1.00 51.94 C ANISOU 2024 C GLY A1070 5578 5710 8449 191 -1054 -309 C ATOM 2025 O GLY A1070 -3.493 -61.174 24.526 1.00 49.82 O ANISOU 2025 O GLY A1070 5467 5410 8052 110 -1140 -429 O ATOM 2026 N GLN A1071 -4.029 -59.881 22.765 1.00 50.73 N ANISOU 2026 N GLN A1071 5620 5277 8378 274 -962 -197 N ATOM 2027 CA GLN A1071 -2.985 -60.474 21.935 1.00 50.14 C ANISOU 2027 CA GLN A1071 5952 4868 8231 305 -924 -210 C ATOM 2028 C GLN A1071 -1.599 -60.049 22.403 1.00 49.42 C ANISOU 2028 C GLN A1071 5741 4625 8410 481 -680 -494 C ATOM 2029 O GLN A1071 -0.631 -60.798 22.231 1.00 52.38 O ANISOU 2029 O GLN A1071 6357 4857 8689 526 -660 -538 O ATOM 2030 CB GLN A1071 -3.195 -60.103 20.468 1.00 50.91 C ANISOU 2030 CB GLN A1071 6295 4720 8327 353 -872 -1 C ATOM 2031 CG GLN A1071 -4.395 -60.768 19.820 1.00 55.34 C ANISOU 2031 CG GLN A1071 7096 5369 8561 122 -1183 338 C ATOM 2032 CD GLN A1071 -4.649 -60.263 18.414 1.00 57.25 C ANISOU 2032 CD GLN A1071 7566 5362 8823 168 -1138 540 C ATOM 2033 OE1 GLN A1071 -4.455 -59.084 18.122 1.00 53.00 O ANISOU 2033 OE1 GLN A1071 6816 4721 8601 355 -890 463 O ATOM 2034 NE2 GLN A1071 -5.088 -61.155 17.534 1.00 53.93 N ANISOU 2034 NE2 GLN A1071 7631 4815 8044 -23 -1407 808 N ATOM 2035 N ILE A1072 -1.487 -58.855 22.987 1.00 49.90 N ANISOU 2035 N ILE A1072 5453 4714 8790 588 -511 -663 N ATOM 2036 CA ILE A1072 -0.231 -58.444 23.606 1.00 49.70 C ANISOU 2036 CA ILE A1072 5288 4582 9016 673 -355 -901 C ATOM 2037 C ILE A1072 0.042 -59.287 24.845 1.00 51.45 C ANISOU 2037 C ILE A1072 5448 4990 9111 578 -495 -1053 C ATOM 2038 O ILE A1072 1.175 -59.729 25.076 1.00 48.42 O ANISOU 2038 O ILE A1072 5104 4525 8768 604 -460 -1146 O ATOM 2039 CB ILE A1072 -0.254 -56.939 23.930 1.00 52.56 C ANISOU 2039 CB ILE A1072 5398 4872 9700 773 -205 -1031 C ATOM 2040 CG1 ILE A1072 -0.262 -56.119 22.639 1.00 51.01 C ANISOU 2040 CG1 ILE A1072 5300 4435 9647 861 -62 -886 C ATOM 2041 CG2 ILE A1072 0.941 -56.556 24.788 1.00 50.42 C ANISOU 2041 CG2 ILE A1072 4984 4519 9655 772 -136 -1255 C ATOM 2042 CD1 ILE A1072 -0.542 -54.648 22.849 1.00 52.29 C ANISOU 2042 CD1 ILE A1072 5307 4498 10061 965 33 -979 C ATOM 2043 N ASP A1073 -0.989 -59.525 25.660 1.00 50.59 N ANISOU 2043 N ASP A1073 5221 5160 8840 476 -653 -1053 N ATOM 2044 CA ASP A1073 -0.825 -60.384 26.829 1.00 52.69 C ANISOU 2044 CA ASP A1073 5459 5614 8947 357 -809 -1177 C ATOM 2045 C ASP A1073 -0.433 -61.800 26.423 1.00 52.57 C ANISOU 2045 C ASP A1073 5792 5536 8645 263 -976 -1072 C ATOM 2046 O ASP A1073 0.403 -62.429 27.083 1.00 51.97 O ANISOU 2046 O ASP A1073 5763 5451 8534 253 -1029 -1210 O ATOM 2047 CB ASP A1073 -2.112 -60.400 27.656 1.00 55.15 C ANISOU 2047 CB ASP A1073 5579 6282 9095 263 -931 -1130 C ATOM 2048 CG ASP A1073 -2.414 -59.058 28.294 1.00 64.96 C ANISOU 2048 CG ASP A1073 6538 7578 10565 437 -756 -1282 C ATOM 2049 OD1 ASP A1073 -1.474 -58.256 28.477 1.00 66.81 O ANISOU 2049 OD1 ASP A1073 6746 7570 11069 547 -613 -1487 O ATOM 2050 OD2 ASP A1073 -3.594 -58.806 28.615 1.00 70.44 O ANISOU 2050 OD2 ASP A1073 7054 8563 11148 469 -771 -1172 O ATOM 2051 N ASP A1074 -1.042 -62.329 25.357 1.00 52.81 N ANISOU 2051 N ASP A1074 6117 5506 8441 200 -1086 -822 N ATOM 2052 CA ASP A1074 -0.666 -63.657 24.879 1.00 47.99 C ANISOU 2052 CA ASP A1074 5973 4758 7502 149 -1259 -722 C ATOM 2053 C ASP A1074 0.824 -63.713 24.562 1.00 47.96 C ANISOU 2053 C ASP A1074 6077 4508 7636 394 -1048 -842 C ATOM 2054 O ASP A1074 1.530 -64.636 24.984 1.00 47.96 O ANISOU 2054 O ASP A1074 6258 4484 7483 430 -1135 -915 O ATOM 2055 CB ASP A1074 -1.486 -64.030 23.643 1.00 48.83 C ANISOU 2055 CB ASP A1074 6450 4759 7346 53 -1406 -426 C ATOM 2056 CG ASP A1074 -2.953 -64.245 23.955 1.00 58.62 C ANISOU 2056 CG ASP A1074 7585 6304 8385 -240 -1682 -216 C ATOM 2057 OD1 ASP A1074 -3.304 -64.337 25.150 1.00 59.75 O ANISOU 2057 OD1 ASP A1074 7432 6749 8519 -357 -1765 -299 O ATOM 2058 OD2 ASP A1074 -3.754 -64.333 23.000 1.00 55.46 O ANISOU 2058 OD2 ASP A1074 7391 5859 7823 -360 -1822 62 O ATOM 2059 N ALA A1075 1.317 -62.726 23.810 1.00 50.68 N ANISOU 2059 N ALA A1075 6300 4692 8265 569 -772 -834 N ATOM 2060 CA ALA A1075 2.722 -62.719 23.418 1.00 53.53 C ANISOU 2060 CA ALA A1075 6694 4884 8762 802 -544 -871 C ATOM 2061 C ALA A1075 3.626 -62.457 24.617 1.00 54.95 C ANISOU 2061 C ALA A1075 6503 5178 9196 810 -494 -1079 C ATOM 2062 O ALA A1075 4.729 -63.008 24.702 1.00 49.34 O ANISOU 2062 O ALA A1075 5833 4436 8476 958 -430 -1094 O ATOM 2063 CB ALA A1075 2.957 -61.680 22.322 1.00 49.59 C ANISOU 2063 CB ALA A1075 6134 4214 8495 931 -279 -769 C ATOM 2064 N ALEU A1076 3.172 -61.624 25.557 0.50 54.12 N ANISOU 2064 N ALEU A1076 6057 5206 9299 673 -529 -1225 N ATOM 2065 N BLEU A1076 3.179 -61.603 25.544 0.50 54.14 N ANISOU 2065 N BLEU A1076 6058 5207 9308 675 -525 -1224 N ATOM 2066 CA ALEU A1076 3.976 -61.336 26.741 0.50 55.81 C ANISOU 2066 CA ALEU A1076 5978 5497 9731 638 -530 -1421 C ATOM 2067 CA BLEU A1076 3.956 -61.332 26.750 0.50 55.80 C ANISOU 2067 CA BLEU A1076 5977 5498 9728 635 -532 -1422 C ATOM 2068 C ALEU A1076 4.144 -62.576 27.611 0.50 55.45 C ANISOU 2068 C ALEU A1076 6054 5578 9436 572 -745 -1496 C ATOM 2069 C BLEU A1076 4.153 -62.595 27.575 0.50 55.47 C ANISOU 2069 C BLEU A1076 6066 5576 9433 577 -743 -1490 C ATOM 2070 O ALEU A1076 5.215 -62.793 28.191 0.50 55.94 O ANISOU 2070 O ALEU A1076 5997 5648 9608 617 -739 -1578 O ATOM 2071 O BLEU A1076 5.250 -62.846 28.089 0.50 55.94 O ANISOU 2071 O BLEU A1076 6019 5638 9597 633 -730 -1563 O ATOM 2072 CB ALEU A1076 3.340 -60.198 27.540 0.50 56.00 C ANISOU 2072 CB ALEU A1076 5737 5591 9949 537 -536 -1567 C ATOM 2073 CB BLEU A1076 3.265 -60.255 27.587 0.50 56.01 C ANISOU 2073 CB BLEU A1076 5745 5607 9928 529 -551 -1569 C ATOM 2074 CG ALEU A1076 4.119 -59.689 28.753 0.50 55.89 C ANISOU 2074 CG ALEU A1076 5483 5594 10160 471 -563 -1772 C ATOM 2075 CG BLEU A1076 3.598 -58.795 27.289 0.50 56.48 C ANISOU 2075 CG BLEU A1076 5621 5503 10338 581 -368 -1595 C ATOM 2076 CD1ALEU A1076 5.442 -59.071 28.325 0.50 56.59 C ANISOU 2076 CD1ALEU A1076 5427 5516 10556 523 -409 -1719 C ATOM 2077 CD1BLEU A1076 2.555 -57.877 27.905 0.50 57.22 C ANISOU 2077 CD1BLEU A1076 5614 5658 10471 559 -396 -1708 C ATOM 2078 CD2ALEU A1076 3.286 -58.691 29.542 0.50 56.38 C ANISOU 2078 CD2ALEU A1076 5425 5703 10294 425 -584 -1922 C ATOM 2079 CD2BLEU A1076 4.983 -58.457 27.817 0.50 57.31 C ANISOU 2079 CD2BLEU A1076 5539 5535 10703 550 -331 -1677 C ATOM 2080 N LYS A1077 3.099 -63.401 27.715 1.00 55.16 N ANISOU 2080 N LYS A1077 6251 5649 9057 443 -961 -1439 N ATOM 2081 CA LYS A1077 3.208 -64.641 28.477 1.00 56.58 C ANISOU 2081 CA LYS A1077 6619 5924 8957 354 -1201 -1489 C ATOM 2082 C LYS A1077 4.202 -65.598 27.830 1.00 57.05 C ANISOU 2082 C LYS A1077 7009 5810 8858 562 -1181 -1408 C ATOM 2083 O LYS A1077 4.993 -66.247 28.524 1.00 59.15 O ANISOU 2083 O LYS A1077 7288 6103 9083 613 -1261 -1498 O ATOM 2084 CB LYS A1077 1.837 -65.300 28.610 1.00 58.68 C ANISOU 2084 CB LYS A1077 7079 6348 8870 121 -1463 -1377 C ATOM 2085 CG LYS A1077 1.880 -66.641 29.315 1.00 65.28 C ANISOU 2085 CG LYS A1077 8184 7253 9365 -16 -1756 -1396 C ATOM 2086 CD LYS A1077 0.493 -67.134 29.668 1.00 70.42 C ANISOU 2086 CD LYS A1077 8912 8139 9704 -328 -2033 -1259 C ATOM 2087 CE LYS A1077 0.562 -68.507 30.309 1.00 73.03 C ANISOU 2087 CE LYS A1077 9577 8503 9667 -500 -2361 -1255 C ATOM 2088 NZ LYS A1077 1.173 -69.511 29.395 1.00 75.14 N ANISOU 2088 NZ LYS A1077 10424 8456 9668 -359 -2462 -1160 N ATOM 2089 N LEU A1078 4.171 -65.700 26.500 1.00 55.97 N ANISOU 2089 N LEU A1078 7166 5491 8608 717 -1068 -1231 N ATOM 2090 CA LEU A1078 5.137 -66.541 25.801 1.00 55.18 C ANISOU 2090 CA LEU A1078 7422 5219 8325 1011 -988 -1143 C ATOM 2091 C LEU A1078 6.552 -66.009 25.982 1.00 55.21 C ANISOU 2091 C LEU A1078 7039 5253 8684 1238 -719 -1188 C ATOM 2092 O LEU A1078 7.494 -66.784 26.186 1.00 56.89 O ANISOU 2092 O LEU A1078 7350 5467 8800 1453 -713 -1184 O ATOM 2093 CB LEU A1078 4.775 -66.622 24.319 1.00 50.53 C ANISOU 2093 CB LEU A1078 7249 4417 7534 1137 -899 -941 C ATOM 2094 CG LEU A1078 3.455 -67.325 23.998 1.00 51.67 C ANISOU 2094 CG LEU A1078 7858 4507 7266 888 -1227 -818 C ATOM 2095 CD1 LEU A1078 3.080 -67.131 22.537 1.00 51.23 C ANISOU 2095 CD1 LEU A1078 8155 4231 7081 975 -1135 -617 C ATOM 2096 CD2 LEU A1078 3.539 -68.809 24.343 1.00 51.13 C ANISOU 2096 CD2 LEU A1078 8318 4364 6745 877 -1532 -814 C ATOM 2097 N ALA A1079 6.722 -64.688 25.886 1.00 55.44 N ANISOU 2097 N ALA A1079 6638 5312 9115 1192 -512 -1200 N ATOM 2098 CA ALA A1079 8.028 -64.077 26.112 1.00 61.25 C ANISOU 2098 CA ALA A1079 6957 6105 10211 1310 -308 -1193 C ATOM 2099 C ALA A1079 8.574 -64.436 27.490 1.00 64.31 C ANISOU 2099 C ALA A1079 7126 6639 10669 1211 -488 -1343 C ATOM 2100 O ALA A1079 9.737 -64.833 27.627 1.00 67.50 O ANISOU 2100 O ALA A1079 7406 7105 11135 1401 -417 -1275 O ATOM 2101 CB ALA A1079 7.931 -62.560 25.946 1.00 58.89 C ANISOU 2101 CB ALA A1079 6299 5781 10296 1173 -157 -1195 C ATOM 2102 N ASN A1080 7.744 -64.299 28.528 1.00 62.92 N ANISOU 2102 N ASN A1080 6892 6541 10475 930 -716 -1528 N ATOM 2103 CA ASN A1080 8.179 -64.587 29.890 1.00 65.86 C ANISOU 2103 CA ASN A1080 7090 7036 10898 801 -907 -1685 C ATOM 2104 C ASN A1080 8.499 -66.060 30.105 1.00 65.81 C ANISOU 2104 C ASN A1080 7398 7049 10556 931 -1071 -1669 C ATOM 2105 O ASN A1080 9.236 -66.391 31.041 1.00 67.16 O ANISOU 2105 O ASN A1080 7416 7307 10793 913 -1188 -1745 O ATOM 2106 CB ASN A1080 7.113 -64.138 30.892 1.00 67.58 C ANISOU 2106 CB ASN A1080 7235 7339 11104 513 -1082 -1873 C ATOM 2107 CG ASN A1080 6.964 -62.631 30.947 1.00 73.26 C ANISOU 2107 CG ASN A1080 7668 8012 12157 422 -949 -1930 C ATOM 2108 OD1 ASN A1080 7.951 -61.898 30.921 1.00 77.09 O ANISOU 2108 OD1 ASN A1080 7902 8435 12954 439 -841 -1898 O ATOM 2109 ND2 ASN A1080 5.724 -62.160 31.028 1.00 73.63 N ANISOU 2109 ND2 ASN A1080 7760 8093 12123 326 -973 -1987 N ATOM 2110 N GLU A1081 7.970 -66.949 29.268 1.00 64.59 N ANISOU 2110 N GLU A1081 7725 6790 10027 1054 -1112 -1564 N ATOM 2111 CA GLU A1081 8.363 -68.351 29.289 1.00 63.37 C ANISOU 2111 CA GLU A1081 7987 6580 9511 1242 -1262 -1528 C ATOM 2112 C GLU A1081 9.616 -68.628 28.470 1.00 65.13 C ANISOU 2112 C GLU A1081 8251 6738 9758 1694 -1001 -1365 C ATOM 2113 O GLU A1081 10.017 -69.792 28.360 1.00 67.11 O ANISOU 2113 O GLU A1081 8911 6911 9677 1956 -1086 -1320 O ATOM 2114 CB GLU A1081 7.215 -69.230 28.784 1.00 65.62 C ANISOU 2114 CB GLU A1081 8870 6741 9320 1142 -1484 -1467 C ATOM 2115 CG GLU A1081 6.003 -69.264 29.702 1.00 69.32 C ANISOU 2115 CG GLU A1081 9306 7354 9679 715 -1776 -1566 C ATOM 2116 CD GLU A1081 4.761 -69.791 29.009 1.00 77.77 C ANISOU 2116 CD GLU A1081 10840 8346 10362 539 -1974 -1417 C ATOM 2117 OE1 GLU A1081 4.828 -70.067 27.793 1.00 81.42 O ANISOU 2117 OE1 GLU A1081 11697 8594 10646 742 -1891 -1264 O ATOM 2118 OE2 GLU A1081 3.718 -69.932 29.680 1.00 79.33 O ANISOU 2118 OE2 GLU A1081 11011 8712 10420 190 -2219 -1426 O ATOM 2119 N GLY A1082 10.240 -67.600 27.899 1.00 64.29 N ANISOU 2119 N GLY A1082 7747 6670 10009 1806 -686 -1257 N ATOM 2120 CA GLY A1082 11.422 -67.802 27.085 1.00 63.33 C ANISOU 2120 CA GLY A1082 7595 6558 9911 2253 -391 -1048 C ATOM 2121 C GLY A1082 11.163 -68.414 25.729 1.00 59.58 C ANISOU 2121 C GLY A1082 7713 5877 9048 2580 -249 -904 C ATOM 2122 O GLY A1082 12.088 -68.950 25.115 1.00 64.49 O ANISOU 2122 O GLY A1082 8477 6495 9531 3049 -28 -739 O ATOM 2123 N LYS A1083 9.926 -68.344 25.238 1.00 56.94 N ANISOU 2123 N LYS A1083 7740 5378 8517 2360 -372 -939 N ATOM 2124 CA LYS A1083 9.562 -68.890 23.932 1.00 61.49 C ANISOU 2124 CA LYS A1083 8961 5709 8693 2602 -298 -798 C ATOM 2125 C LYS A1083 9.552 -67.740 22.929 1.00 62.16 C ANISOU 2125 C LYS A1083 8805 5771 9040 2625 21 -669 C ATOM 2126 O LYS A1083 8.519 -67.137 22.637 1.00 66.48 O ANISOU 2126 O LYS A1083 9379 6247 9633 2330 -61 -688 O ATOM 2127 CB LYS A1083 8.215 -69.601 23.998 1.00 62.53 C ANISOU 2127 CB LYS A1083 9661 5681 8418 2298 -693 -859 C ATOM 2128 CG LYS A1083 8.098 -70.622 25.116 1.00 62.07 C ANISOU 2128 CG LYS A1083 9797 5663 8125 2163 -1055 -988 C ATOM 2129 CD LYS A1083 6.722 -71.265 25.119 1.00 63.67 C ANISOU 2129 CD LYS A1083 10524 5744 7923 1793 -1463 -978 C ATOM 2130 CE LYS A1083 6.600 -72.309 26.215 1.00 64.59 C ANISOU 2130 CE LYS A1083 10867 5897 7775 1625 -1843 -1083 C ATOM 2131 NZ LYS A1083 5.258 -72.955 26.211 1.00 63.05 N ANISOU 2131 NZ LYS A1083 11164 5622 7172 1207 -2271 -1009 N ATOM 2132 N VAL A1084 10.737 -67.435 22.398 1.00 60.97 N ANISOU 2132 N VAL A1084 8397 5707 9062 2990 390 -507 N ATOM 2133 CA VAL A1084 10.905 -66.238 21.577 1.00 61.67 C ANISOU 2133 CA VAL A1084 8156 5816 9461 2975 699 -368 C ATOM 2134 C VAL A1084 10.148 -66.382 20.262 1.00 61.44 C ANISOU 2134 C VAL A1084 8730 5518 9099 3071 758 -268 C ATOM 2135 O VAL A1084 9.300 -65.548 19.921 1.00 59.81 O ANISOU 2135 O VAL A1084 8459 5234 9034 2778 720 -281 O ATOM 2136 CB VAL A1084 12.397 -65.958 21.331 1.00 69.53 C ANISOU 2136 CB VAL A1084 8704 7026 10690 3327 1074 -153 C ATOM 2137 CG1 VAL A1084 12.585 -64.571 20.732 1.00 67.18 C ANISOU 2137 CG1 VAL A1084 7957 6784 10783 3179 1330 -11 C ATOM 2138 CG2 VAL A1084 13.187 -66.112 22.622 1.00 74.76 C ANISOU 2138 CG2 VAL A1084 8882 7937 11587 3266 951 -217 C ATOM 2139 N LYS A1085 10.465 -67.429 19.494 1.00 63.84 N ANISOU 2139 N LYS A1085 9661 5658 8937 3506 848 -156 N ATOM 2140 CA LYS A1085 9.798 -67.651 18.214 1.00 68.84 C ANISOU 2140 CA LYS A1085 10976 5989 9191 3606 874 -48 C ATOM 2141 C LYS A1085 8.280 -67.677 18.359 1.00 61.78 C ANISOU 2141 C LYS A1085 10376 4937 8162 3114 455 -152 C ATOM 2142 O LYS A1085 7.564 -67.077 17.549 1.00 61.26 O ANISOU 2142 O LYS A1085 10429 4738 8107 2954 473 -71 O ATOM 2143 CB LYS A1085 10.304 -68.947 17.580 1.00 67.86 C ANISOU 2143 CB LYS A1085 11624 5665 8494 4152 947 47 C ATOM 2144 CG LYS A1085 11.770 -68.893 17.184 1.00 71.53 C ANISOU 2144 CG LYS A1085 11739 6401 9037 4605 1403 227 C ATOM 2145 CD LYS A1085 11.961 -68.112 15.892 1.00 73.25 C ANISOU 2145 CD LYS A1085 11912 6619 9299 4703 1766 429 C ATOM 2146 CE LYS A1085 13.383 -68.238 15.370 1.00 82.26 C ANISOU 2146 CE LYS A1085 12821 8048 10384 5169 2204 660 C ATOM 2147 NZ LYS A1085 13.481 -67.919 13.919 1.00 87.29 N ANISOU 2147 NZ LYS A1085 13746 8621 10800 5340 2516 865 N ATOM 2148 N GLU A1086 7.770 -68.376 19.378 1.00 62.92 N ANISOU 2148 N GLU A1086 10621 5118 8168 2868 71 -300 N ATOM 2149 CA GLU A1086 6.324 -68.427 19.581 1.00 63.94 C ANISOU 2149 CA GLU A1086 10948 5182 8166 2387 -328 -339 C ATOM 2150 C GLU A1086 5.772 -67.057 19.956 1.00 60.80 C ANISOU 2150 C GLU A1086 9852 4981 8269 2039 -278 -396 C ATOM 2151 O GLU A1086 4.656 -66.700 19.559 1.00 54.99 O ANISOU 2151 O GLU A1086 9219 4185 7489 1763 -433 -329 O ATOM 2152 CB GLU A1086 5.966 -69.460 20.648 1.00 68.05 C ANISOU 2152 CB GLU A1086 11680 5745 8430 2189 -734 -455 C ATOM 2153 CG GLU A1086 4.489 -69.830 20.646 1.00 74.46 C ANISOU 2153 CG GLU A1086 12861 6481 8951 1729 -1176 -394 C ATOM 2154 CD GLU A1086 4.157 -70.966 21.589 1.00 81.89 C ANISOU 2154 CD GLU A1086 14107 7445 9564 1520 -1598 -460 C ATOM 2155 OE1 GLU A1086 5.069 -71.752 21.922 1.00 85.27 O ANISOU 2155 OE1 GLU A1086 14760 7810 9829 1827 -1577 -535 O ATOM 2156 OE2 GLU A1086 2.981 -71.072 21.995 1.00 84.86 O ANISOU 2156 OE2 GLU A1086 14486 7921 9838 1053 -1953 -410 O ATOM 2157 N ALA A1087 6.539 -66.277 20.722 1.00 55.35 N ANISOU 2157 N ALA A1087 8477 4516 8038 2053 -82 -502 N ATOM 2158 CA ALA A1087 6.099 -64.935 21.088 1.00 61.08 C ANISOU 2158 CA ALA A1087 8626 5374 9208 1774 -33 -570 C ATOM 2159 C ALA A1087 6.089 -64.013 19.877 1.00 61.50 C ANISOU 2159 C ALA A1087 8664 5297 9404 1860 233 -419 C ATOM 2160 O ALA A1087 5.173 -63.199 19.717 1.00 53.42 O ANISOU 2160 O ALA A1087 7515 4260 8523 1629 170 -416 O ATOM 2161 CB ALA A1087 6.993 -64.366 22.190 1.00 57.98 C ANISOU 2161 CB ALA A1087 7613 5194 9221 1747 61 -705 C ATOM 2162 N GLN A1088 7.105 -64.122 19.017 1.00 62.28 N ANISOU 2162 N GLN A1088 8885 5320 9459 2214 542 -277 N ATOM 2163 CA GLN A1088 7.144 -63.301 17.812 1.00 63.11 C ANISOU 2163 CA GLN A1088 9017 5298 9662 2300 805 -112 C ATOM 2164 C GLN A1088 6.008 -63.658 16.860 1.00 61.74 C ANISOU 2164 C GLN A1088 9460 4879 9121 2222 632 -17 C ATOM 2165 O GLN A1088 5.436 -62.775 16.210 1.00 61.27 O ANISOU 2165 O GLN A1088 9343 4734 9203 2087 680 59 O ATOM 2166 CB GLN A1088 8.494 -63.469 17.114 1.00 60.78 C ANISOU 2166 CB GLN A1088 8731 5024 9338 2731 1193 58 C ATOM 2167 CG GLN A1088 9.681 -62.949 17.908 1.00 61.67 C ANISOU 2167 CG GLN A1088 8154 5415 9865 2766 1371 56 C ATOM 2168 CD GLN A1088 11.008 -63.333 17.281 1.00 65.26 C ANISOU 2168 CD GLN A1088 8594 5972 10229 3240 1747 282 C ATOM 2169 OE1 GLN A1088 11.324 -64.516 17.148 1.00 66.74 O ANISOU 2169 OE1 GLN A1088 9215 6119 10023 3602 1763 308 O ATOM 2170 NE2 GLN A1088 11.792 -62.334 16.894 1.00 67.11 N ANISOU 2170 NE2 GLN A1088 8342 6350 10807 3253 2050 469 N ATOM 2171 N ALA A1089 5.669 -64.945 16.762 1.00 58.11 N ANISOU 2171 N ALA A1089 9624 4283 8171 2286 394 -1 N ATOM 2172 CA ALA A1089 4.525 -65.340 15.948 1.00 61.63 C ANISOU 2172 CA ALA A1089 10684 4491 8241 2123 133 120 C ATOM 2173 C ALA A1089 3.218 -64.824 16.538 1.00 61.29 C ANISOU 2173 C ALA A1089 10340 4583 8365 1661 -177 81 C ATOM 2174 O ALA A1089 2.351 -64.336 15.804 1.00 64.23 O ANISOU 2174 O ALA A1089 10828 4855 8722 1496 -254 215 O ATOM 2175 CB ALA A1089 4.484 -66.861 15.801 1.00 59.77 C ANISOU 2175 CB ALA A1089 11244 4053 7413 2252 -115 157 C ATOM 2176 N ALA A1090 3.054 -64.940 17.860 1.00 55.12 N ANISOU 2176 N ALA A1090 9175 4045 7724 1471 -351 -81 N ATOM 2177 CA ALA A1090 1.882 -64.366 18.516 1.00 53.11 C ANISOU 2177 CA ALA A1090 8551 3987 7643 1106 -573 -109 C ATOM 2178 C ALA A1090 1.783 -62.869 18.257 1.00 57.88 C ANISOU 2178 C ALA A1090 8675 4631 8688 1101 -333 -116 C ATOM 2179 O ALA A1090 0.684 -62.334 18.071 1.00 58.41 O ANISOU 2179 O ALA A1090 8651 4742 8799 904 -464 -25 O ATOM 2180 CB ALA A1090 1.927 -64.651 20.017 1.00 51.54 C ANISOU 2180 CB ALA A1090 8000 4048 7534 970 -721 -299 C ATOM 2181 N ALA A1091 2.924 -62.176 18.244 1.00 58.44 N ANISOU 2181 N ALA A1091 8434 4693 9077 1311 3 -194 N ATOM 2182 CA ALA A1091 2.906 -60.729 18.070 1.00 57.22 C ANISOU 2182 CA ALA A1091 7867 4542 9333 1279 197 -206 C ATOM 2183 C ALA A1091 2.579 -60.348 16.633 1.00 61.28 C ANISOU 2183 C ALA A1091 8688 4830 9764 1337 299 -3 C ATOM 2184 O ALA A1091 2.074 -59.248 16.384 1.00 62.10 O ANISOU 2184 O ALA A1091 8574 4909 10114 1250 343 23 O ATOM 2185 CB ALA A1091 4.247 -60.129 18.490 1.00 53.23 C ANISOU 2185 CB ALA A1091 6954 4097 9174 1410 466 -298 C ATOM 2186 N GLU A1092 2.879 -61.229 15.676 1.00 64.40 N ANISOU 2186 N GLU A1092 9635 5038 9796 1508 337 140 N ATOM 2187 CA GLU A1092 2.516 -60.964 14.289 1.00 70.33 C ANISOU 2187 CA GLU A1092 10769 5548 10405 1550 402 340 C ATOM 2188 C GLU A1092 1.003 -60.901 14.110 1.00 66.04 C ANISOU 2188 C GLU A1092 10363 4988 9739 1260 62 444 C ATOM 2189 O GLU A1092 0.513 -60.223 13.200 1.00 63.80 O ANISOU 2189 O GLU A1092 10172 4565 9505 1219 93 587 O ATOM 2190 CB GLU A1092 3.121 -62.033 13.379 1.00 79.29 C ANISOU 2190 CB GLU A1092 12567 6465 11094 1826 492 462 C ATOM 2191 CG GLU A1092 3.384 -61.559 11.963 1.00 90.46 C ANISOU 2191 CG GLU A1092 14275 7647 12448 2000 751 645 C ATOM 2192 CD GLU A1092 4.599 -60.656 11.878 1.00 98.60 C ANISOU 2192 CD GLU A1092 14823 8785 13857 2203 1189 644 C ATOM 2193 OE1 GLU A1092 5.587 -60.923 12.595 1.00103.18 O ANISOU 2193 OE1 GLU A1092 15106 9552 14547 2365 1340 560 O ATOM 2194 OE2 GLU A1092 4.567 -59.681 11.099 1.00102.30 O ANISOU 2194 OE2 GLU A1092 15204 9159 14508 2176 1359 754 O ATOM 2195 N GLN A1093 0.252 -61.607 14.962 1.00 63.96 N ANISOU 2195 N GLN A1093 10099 4893 9312 1047 -271 408 N ATOM 2196 CA GLN A1093 -1.206 -61.542 14.917 1.00 64.46 C ANISOU 2196 CA GLN A1093 10172 5043 9278 750 -604 564 C ATOM 2197 C GLN A1093 -1.713 -60.127 15.162 1.00 66.07 C ANISOU 2197 C GLN A1093 9801 5392 9911 712 -492 529 C ATOM 2198 O GLN A1093 -2.787 -59.758 14.672 1.00 68.79 O ANISOU 2198 O GLN A1093 10157 5751 10230 568 -656 720 O ATOM 2199 CB GLN A1093 -1.805 -62.508 15.939 1.00 67.50 C ANISOU 2199 CB GLN A1093 10557 5654 9437 520 -951 548 C ATOM 2200 CG GLN A1093 -1.296 -63.935 15.808 1.00 77.39 C ANISOU 2200 CG GLN A1093 12435 6732 10238 568 -1101 562 C ATOM 2201 CD GLN A1093 -1.582 -64.534 14.445 1.00 86.98 C ANISOU 2201 CD GLN A1093 14426 7598 11025 552 -1258 805 C ATOM 2202 OE1 GLN A1093 -2.706 -64.947 14.160 1.00 93.25 O ANISOU 2202 OE1 GLN A1093 15498 8385 11549 225 -1654 1038 O ATOM 2203 NE2 GLN A1093 -0.562 -64.585 13.595 1.00 89.79 N ANISOU 2203 NE2 GLN A1093 15143 7676 11297 901 -954 780 N ATOM 2204 N LEU A1094 -0.964 -59.334 15.936 1.00 62.57 N ANISOU 2204 N LEU A1094 8883 5046 9844 839 -242 301 N ATOM 2205 CA LEU A1094 -1.337 -57.949 16.212 1.00 60.52 C ANISOU 2205 CA LEU A1094 8172 4860 9963 848 -135 238 C ATOM 2206 C LEU A1094 -1.591 -57.159 14.936 1.00 64.95 C ANISOU 2206 C LEU A1094 8895 5190 10594 893 -39 412 C ATOM 2207 O LEU A1094 -2.400 -56.224 14.935 1.00 69.10 O ANISOU 2207 O LEU A1094 9189 5764 11299 870 -75 455 O ATOM 2208 CB LEU A1094 -0.243 -57.280 17.045 1.00 58.68 C ANISOU 2208 CB LEU A1094 7567 4659 10069 960 100 -9 C ATOM 2209 CG LEU A1094 -0.108 -57.836 18.463 1.00 56.75 C ANISOU 2209 CG LEU A1094 7098 4657 9807 901 -12 -201 C ATOM 2210 CD1 LEU A1094 1.194 -57.397 19.095 1.00 58.43 C ANISOU 2210 CD1 LEU A1094 7052 4851 10299 987 189 -391 C ATOM 2211 CD2 LEU A1094 -1.279 -57.381 19.307 1.00 54.25 C ANISOU 2211 CD2 LEU A1094 6490 4575 9547 810 -166 -243 C ATOM 2212 N LYS A1095 -0.911 -57.513 13.842 1.00 63.53 N ANISOU 2212 N LYS A1095 9126 4758 10255 989 93 521 N ATOM 2213 CA LYS A1095 -1.055 -56.751 12.606 1.00 68.95 C ANISOU 2213 CA LYS A1095 9992 5207 10999 1029 202 685 C ATOM 2214 C LYS A1095 -2.451 -56.919 12.021 1.00 70.99 C ANISOU 2214 C LYS A1095 10474 5452 11046 856 -107 919 C ATOM 2215 O LYS A1095 -3.015 -55.968 11.467 1.00 72.86 O ANISOU 2215 O LYS A1095 10625 5610 11447 845 -99 1025 O ATOM 2216 CB LYS A1095 0.011 -57.171 11.596 1.00 75.19 C ANISOU 2216 CB LYS A1095 11195 5761 11615 1202 440 765 C ATOM 2217 CG LYS A1095 1.409 -56.707 11.958 1.00 82.36 C ANISOU 2217 CG LYS A1095 11782 6710 12801 1366 781 631 C ATOM 2218 CD LYS A1095 2.430 -57.175 10.940 1.00 89.04 C ANISOU 2218 CD LYS A1095 13002 7394 13436 1594 1055 763 C ATOM 2219 CE LYS A1095 3.786 -56.552 11.212 1.00 93.58 C ANISOU 2219 CE LYS A1095 13158 8069 14330 1718 1395 718 C ATOM 2220 NZ LYS A1095 4.838 -57.093 10.309 1.00 99.44 N ANISOU 2220 NZ LYS A1095 14197 8743 14843 2005 1709 881 N ATOM 2221 N THR A1096 -3.018 -58.124 12.118 1.00 71.28 N ANISOU 2221 N THR A1096 10813 5559 10710 700 -409 1031 N ATOM 2222 CA THR A1096 -4.394 -58.323 11.677 1.00 71.64 C ANISOU 2222 CA THR A1096 11009 5655 10557 463 -767 1310 C ATOM 2223 C THR A1096 -5.348 -57.431 12.464 1.00 65.29 C ANISOU 2223 C THR A1096 9588 5173 10047 415 -834 1312 C ATOM 2224 O THR A1096 -6.261 -56.824 11.890 1.00 63.74 O ANISOU 2224 O THR A1096 9329 4984 9906 358 -947 1526 O ATOM 2225 CB THR A1096 -4.785 -59.794 11.826 1.00 74.25 C ANISOU 2225 CB THR A1096 11755 6029 10430 244 -1128 1439 C ATOM 2226 OG1 THR A1096 -3.953 -60.599 10.982 1.00 78.26 O ANISOU 2226 OG1 THR A1096 12947 6184 10603 360 -1063 1452 O ATOM 2227 CG2 THR A1096 -6.243 -60.005 11.443 1.00 74.55 C ANISOU 2227 CG2 THR A1096 11884 6174 10267 -78 -1556 1793 C ATOM 2228 N THR A1097 -5.148 -57.336 13.781 1.00 63.30 N ANISOU 2228 N THR A1097 8895 5188 9968 470 -758 1082 N ATOM 2229 CA THR A1097 -5.985 -56.464 14.601 1.00 61.94 C ANISOU 2229 CA THR A1097 8174 5319 10041 512 -768 1058 C ATOM 2230 C THR A1097 -5.741 -54.996 14.269 1.00 63.14 C ANISOU 2230 C THR A1097 8147 5294 10551 733 -508 961 C ATOM 2231 O THR A1097 -6.686 -54.199 14.217 1.00 58.51 O ANISOU 2231 O THR A1097 7324 4822 10083 796 -559 1084 O ATOM 2232 CB THR A1097 -5.723 -56.725 16.085 1.00 60.24 C ANISOU 2232 CB THR A1097 7620 5383 9886 536 -734 814 C ATOM 2233 OG1 THR A1097 -5.834 -58.128 16.353 1.00 59.97 O ANISOU 2233 OG1 THR A1097 7818 5466 9500 317 -987 899 O ATOM 2234 CG2 THR A1097 -6.725 -55.967 16.947 1.00 56.48 C ANISOU 2234 CG2 THR A1097 6640 5254 9565 615 -753 826 C ATOM 2235 N ARG A1098 -4.477 -54.624 14.049 1.00 62.01 N ANISOU 2235 N ARG A1098 8109 4881 10570 854 -239 767 N ATOM 2236 CA ARG A1098 -4.147 -53.249 13.683 1.00 68.99 C ANISOU 2236 CA ARG A1098 8888 5553 11770 1006 -25 696 C ATOM 2237 C ARG A1098 -4.833 -52.835 12.387 1.00 73.76 C ANISOU 2237 C ARG A1098 9728 5973 12325 985 -100 964 C ATOM 2238 O ARG A1098 -5.375 -51.727 12.290 1.00 72.56 O ANISOU 2238 O ARG A1098 9406 5786 12377 1094 -79 990 O ATOM 2239 CB ARG A1098 -2.630 -53.097 13.578 1.00 67.95 C ANISOU 2239 CB ARG A1098 8834 5209 11776 1066 241 530 C ATOM 2240 CG ARG A1098 -2.150 -51.696 13.254 1.00 70.61 C ANISOU 2240 CG ARG A1098 9083 5316 12431 1154 432 473 C ATOM 2241 CD ARG A1098 -0.798 -51.753 12.565 1.00 73.42 C ANISOU 2241 CD ARG A1098 9608 5468 12819 1157 669 496 C ATOM 2242 NE ARG A1098 -0.813 -52.615 11.387 1.00 77.02 N ANISOU 2242 NE ARG A1098 10488 5810 12967 1148 670 710 N ATOM 2243 CZ ARG A1098 0.278 -53.112 10.815 1.00 81.12 C ANISOU 2243 CZ ARG A1098 11212 6232 13376 1214 880 763 C ATOM 2244 NH1 ARG A1098 1.475 -52.841 11.318 1.00 81.21 N ANISOU 2244 NH1 ARG A1098 10964 6297 13595 1258 1094 651 N ATOM 2245 NH2 ARG A1098 0.174 -53.889 9.746 1.00 83.72 N ANISOU 2245 NH2 ARG A1098 12020 6421 13367 1246 870 951 N ATOM 2246 N ASN A1099 -4.819 -53.707 11.378 1.00 76.17 N ANISOU 2246 N ASN A1099 10476 6131 12336 862 -201 1165 N ATOM 2247 CA ASN A1099 -5.411 -53.356 10.091 1.00 78.36 C ANISOU 2247 CA ASN A1099 11039 6196 12539 817 -291 1430 C ATOM 2248 C ASN A1099 -6.932 -53.307 10.184 1.00 77.92 C ANISOU 2248 C ASN A1099 10795 6390 12422 717 -602 1674 C ATOM 2249 O ASN A1099 -7.566 -52.373 9.681 1.00 83.05 O ANISOU 2249 O ASN A1099 11355 6980 13221 786 -626 1809 O ATOM 2250 CB ASN A1099 -4.965 -54.349 9.017 1.00 83.04 C ANISOU 2250 CB ASN A1099 12242 6535 12775 727 -327 1577 C ATOM 2251 CG ASN A1099 -3.459 -54.397 8.855 1.00 85.56 C ANISOU 2251 CG ASN A1099 12701 6670 13139 884 23 1399 C ATOM 2252 OD1 ASN A1099 -2.750 -53.475 9.259 1.00 85.56 O ANISOU 2252 OD1 ASN A1099 12369 6665 13474 1002 275 1222 O ATOM 2253 ND2 ASN A1099 -2.962 -55.474 8.259 1.00 85.79 N ANISOU 2253 ND2 ASN A1099 13240 6550 12808 893 27 1472 N ATOM 2254 N ALA A1100 -7.535 -54.310 10.826 1.00 76.68 N ANISOU 2254 N ALA A1100 10560 6535 12039 551 -852 1765 N ATOM 2255 CA ALA A1100 -8.988 -54.431 10.839 1.00 75.64 C ANISOU 2255 CA ALA A1100 10232 6705 11801 402 -1179 2095 C ATOM 2256 C ALA A1100 -9.651 -53.463 11.812 1.00 77.61 C ANISOU 2256 C ALA A1100 9859 7297 12331 621 -1091 2030 C ATOM 2257 O ALA A1100 -10.804 -53.074 11.595 1.00 77.76 O ANISOU 2257 O ALA A1100 9650 7529 12365 626 -1259 2324 O ATOM 2258 CB ALA A1100 -9.392 -55.866 11.178 1.00 75.62 C ANISOU 2258 CB ALA A1100 10381 6919 11430 98 -1507 2261 C ATOM 2259 N TYR A1101 -8.960 -53.068 12.882 1.00 79.22 N ANISOU 2259 N TYR A1101 9803 7562 12737 820 -837 1672 N ATOM 2260 CA TYR A1101 -9.572 -52.267 13.938 1.00 78.88 C ANISOU 2260 CA TYR A1101 9251 7837 12882 1065 -753 1586 C ATOM 2261 C TYR A1101 -8.817 -50.972 14.207 1.00 73.55 C ANISOU 2261 C TYR A1101 8527 6893 12526 1363 -451 1259 C ATOM 2262 O TYR A1101 -9.390 -49.889 14.045 1.00 67.17 O ANISOU 2262 O TYR A1101 7590 6057 11876 1600 -402 1314 O ATOM 2263 CB TYR A1101 -9.681 -53.088 15.232 1.00 82.40 C ANISOU 2263 CB TYR A1101 9437 8674 13197 989 -812 1492 C ATOM 2264 CG TYR A1101 -10.595 -54.289 15.145 1.00 85.82 C ANISOU 2264 CG TYR A1101 9864 9438 13305 663 -1162 1858 C ATOM 2265 CD1 TYR A1101 -11.967 -54.155 15.317 1.00 88.09 C ANISOU 2265 CD1 TYR A1101 9759 10173 13539 662 -1336 2211 C ATOM 2266 CD2 TYR A1101 -10.085 -55.559 14.908 1.00 85.02 C ANISOU 2266 CD2 TYR A1101 10160 9212 12932 358 -1334 1878 C ATOM 2267 CE1 TYR A1101 -12.807 -55.250 15.246 1.00 90.25 C ANISOU 2267 CE1 TYR A1101 10010 10772 13508 290 -1705 2605 C ATOM 2268 CE2 TYR A1101 -10.918 -56.661 14.835 1.00 85.90 C ANISOU 2268 CE2 TYR A1101 10342 9582 12713 6 -1715 2230 C ATOM 2269 CZ TYR A1101 -12.277 -56.500 15.004 1.00 89.18 C ANISOU 2269 CZ TYR A1101 10337 10453 13094 -65 -1915 2606 C ATOM 2270 OH TYR A1101 -13.109 -57.594 14.933 1.00 90.75 O ANISOU 2270 OH TYR A1101 10590 10932 12958 -487 -2340 3014 O ATOM 2271 N ILE A1102 -7.551 -51.051 14.625 1.00 70.53 N ANISOU 2271 N ILE A1102 8256 6310 12230 1352 -273 945 N ATOM 2272 CA ILE A1102 -6.872 -49.898 15.215 1.00 69.19 C ANISOU 2272 CA ILE A1102 7999 5953 12338 1572 -53 640 C ATOM 2273 C ILE A1102 -6.756 -48.754 14.216 1.00 71.41 C ANISOU 2273 C ILE A1102 8471 5863 12797 1677 30 695 C ATOM 2274 O ILE A1102 -6.940 -47.583 14.571 1.00 73.28 O ANISOU 2274 O ILE A1102 8627 6002 13213 1917 104 578 O ATOM 2275 CB ILE A1102 -5.493 -50.312 15.761 1.00 67.04 C ANISOU 2275 CB ILE A1102 7796 5563 12114 1468 74 369 C ATOM 2276 CG1 ILE A1102 -5.616 -51.584 16.601 1.00 68.12 C ANISOU 2276 CG1 ILE A1102 7815 6035 12033 1334 -44 346 C ATOM 2277 CG2 ILE A1102 -4.881 -49.183 16.579 1.00 62.96 C ANISOU 2277 CG2 ILE A1102 7181 4891 11850 1631 221 79 C ATOM 2278 CD1 ILE A1102 -6.523 -51.431 17.808 1.00 67.44 C ANISOU 2278 CD1 ILE A1102 7381 6322 11919 1471 -98 294 C ATOM 2279 N GLN A1103 -6.447 -49.066 12.955 1.00 71.04 N ANISOU 2279 N GLN A1103 8732 5582 12677 1511 11 872 N ATOM 2280 CA GLN A1103 -6.298 -48.009 11.960 1.00 75.25 C ANISOU 2280 CA GLN A1103 9470 5756 13364 1578 86 939 C ATOM 2281 C GLN A1103 -7.613 -47.284 11.704 1.00 70.79 C ANISOU 2281 C GLN A1103 8794 5274 12829 1762 -43 1135 C ATOM 2282 O GLN A1103 -7.610 -46.077 11.436 1.00 69.44 O ANISOU 2282 O GLN A1103 8694 4848 12842 1935 25 1090 O ATOM 2283 CB GLN A1103 -5.744 -48.586 10.657 1.00 83.07 C ANISOU 2283 CB GLN A1103 10839 6507 14215 1380 104 1111 C ATOM 2284 CG GLN A1103 -5.367 -47.534 9.625 1.00 91.46 C ANISOU 2284 CG GLN A1103 12136 7184 15432 1409 213 1171 C ATOM 2285 CD GLN A1103 -4.830 -48.138 8.341 1.00 97.80 C ANISOU 2285 CD GLN A1103 13340 7771 16049 1251 264 1352 C ATOM 2286 OE1 GLN A1103 -4.082 -49.115 8.365 1.00101.84 O ANISOU 2286 OE1 GLN A1103 13969 8326 16400 1167 346 1314 O ATOM 2287 NE2 GLN A1103 -5.209 -47.555 7.209 1.00 99.63 N ANISOU 2287 NE2 GLN A1103 13817 7780 16258 1236 217 1544 N ATOM 2288 N LYS A1104 -8.740 -47.996 11.777 1.00 70.91 N ANISOU 2288 N LYS A1104 8634 5652 12657 1723 -244 1381 N ATOM 2289 CA LYS A1104 -10.035 -47.341 11.621 1.00 76.03 C ANISOU 2289 CA LYS A1104 9081 6473 13335 1932 -362 1618 C ATOM 2290 C LYS A1104 -10.299 -46.355 12.753 1.00 77.99 C ANISOU 2290 C LYS A1104 9050 6843 13741 2323 -226 1401 C ATOM 2291 O LYS A1104 -10.837 -45.265 12.522 1.00 79.96 O ANISOU 2291 O LYS A1104 9290 6984 14107 2617 -205 1456 O ATOM 2292 CB LYS A1104 -11.145 -48.388 11.538 1.00 80.39 C ANISOU 2292 CB LYS A1104 9448 7456 13641 1750 -632 1984 C ATOM 2293 CG LYS A1104 -11.017 -49.313 10.338 1.00 89.15 C ANISOU 2293 CG LYS A1104 10957 8381 14535 1377 -825 2228 C ATOM 2294 CD LYS A1104 -12.133 -50.343 10.299 1.00 96.32 C ANISOU 2294 CD LYS A1104 11725 9696 15178 1127 -1167 2625 C ATOM 2295 CE LYS A1104 -12.000 -51.251 9.085 1.00 96.99 C ANISOU 2295 CE LYS A1104 12340 9516 14994 754 -1401 2862 C ATOM 2296 NZ LYS A1104 -10.740 -52.043 9.112 1.00 93.44 N ANISOU 2296 NZ LYS A1104 12280 8807 14416 628 -1269 2589 N ATOM 2297 N TYR A1105 -9.938 -46.722 13.985 1.00 74.68 N ANISOU 2297 N TYR A1105 8448 6628 13297 2354 -139 1155 N ATOM 2298 CA TYR A1105 -10.085 -45.795 15.104 1.00 77.32 C ANISOU 2298 CA TYR A1105 8622 7021 13735 2739 -2 914 C ATOM 2299 C TYR A1105 -9.191 -44.573 14.933 1.00 73.18 C ANISOU 2299 C TYR A1105 8424 5960 13423 2856 125 652 C ATOM 2300 O TYR A1105 -9.627 -43.437 15.152 1.00 78.23 O ANISOU 2300 O TYR A1105 9107 6477 14139 3225 170 591 O ATOM 2301 CB TYR A1105 -9.776 -46.503 16.424 1.00 82.33 C ANISOU 2301 CB TYR A1105 9060 7942 14278 2695 47 699 C ATOM 2302 CG TYR A1105 -9.746 -45.562 17.608 1.00 93.24 C ANISOU 2302 CG TYR A1105 10395 9304 15730 3077 194 404 C ATOM 2303 CD1 TYR A1105 -10.883 -44.865 17.995 1.00102.44 C ANISOU 2303 CD1 TYR A1105 11364 10711 16848 3532 235 510 C ATOM 2304 CD2 TYR A1105 -8.577 -45.363 18.333 1.00 94.23 C ANISOU 2304 CD2 TYR A1105 10699 9161 15944 3002 281 39 C ATOM 2305 CE1 TYR A1105 -10.858 -43.997 19.073 1.00106.27 C ANISOU 2305 CE1 TYR A1105 11909 11131 17338 3936 375 229 C ATOM 2306 CE2 TYR A1105 -8.543 -44.500 19.414 1.00 97.04 C ANISOU 2306 CE2 TYR A1105 11113 9438 16319 3332 375 -232 C ATOM 2307 CZ TYR A1105 -9.686 -43.820 19.780 1.00104.37 C ANISOU 2307 CZ TYR A1105 11923 10569 17166 3816 428 -152 C ATOM 2308 OH TYR A1105 -9.659 -42.960 20.855 1.00109.12 O ANISOU 2308 OH TYR A1105 12679 11052 17730 4197 527 -432 O ATOM 2309 N LEU A1106 -7.926 -44.794 14.565 1.00 70.56 N ANISOU 2309 N LEU A1106 8332 5312 13166 2550 176 515 N ATOM 2310 CA LEU A1106 -7.004 -43.687 14.326 1.00 73.94 C ANISOU 2310 CA LEU A1106 9057 5249 13790 2559 260 333 C ATOM 2311 C LEU A1106 -7.566 -42.700 13.309 1.00 74.81 C ANISOU 2311 C LEU A1106 9361 5091 13970 2716 214 511 C ATOM 2312 O LEU A1106 -7.556 -41.484 13.533 1.00 76.45 O ANISOU 2312 O LEU A1106 9751 5024 14272 2950 229 375 O ATOM 2313 CB LEU A1106 -5.652 -44.231 13.860 1.00 73.98 C ANISOU 2313 CB LEU A1106 9210 5060 13841 2185 328 288 C ATOM 2314 CG LEU A1106 -4.727 -43.241 13.148 1.00 82.54 C ANISOU 2314 CG LEU A1106 10590 5701 15068 2064 386 259 C ATOM 2315 CD1 LEU A1106 -3.993 -42.365 14.151 1.00 83.02 C ANISOU 2315 CD1 LEU A1106 10724 5627 15191 2074 397 -21 C ATOM 2316 CD2 LEU A1106 -3.743 -43.977 12.251 1.00 82.58 C ANISOU 2316 CD2 LEU A1106 10697 5657 15024 1742 471 379 C ATOM 2317 N GLU A 219 -8.057 -43.211 12.178 1.00 63.00 N ANISOU 2317 N GLU A 219 10203 3351 10383 2030 174 -719 N ATOM 2318 CA GLU A 219 -8.570 -42.334 11.131 1.00 63.22 C ANISOU 2318 CA GLU A 219 10309 3546 10165 1942 269 -871 C ATOM 2319 C GLU A 219 -9.836 -41.608 11.573 1.00 64.79 C ANISOU 2319 C GLU A 219 10598 3881 10137 1723 163 -750 C ATOM 2320 O GLU A 219 -10.031 -40.434 11.234 1.00 63.58 O ANISOU 2320 O GLU A 219 10404 3932 9824 1682 230 -781 O ATOM 2321 CB GLU A 219 -8.826 -43.139 9.857 1.00 69.41 C ANISOU 2321 CB GLU A 219 11301 4194 10879 1914 354 -1084 C ATOM 2322 CG GLU A 219 -7.556 -43.616 9.169 1.00 78.68 C ANISOU 2322 CG GLU A 219 12390 5282 12222 2138 485 -1253 C ATOM 2323 CD GLU A 219 -7.814 -44.719 8.163 1.00 87.14 C ANISOU 2323 CD GLU A 219 13689 6156 13263 2115 535 -1432 C ATOM 2324 OE1 GLU A 219 -8.995 -45.045 7.926 1.00 89.96 O ANISOU 2324 OE1 GLU A 219 14266 6460 13453 1914 463 -1430 O ATOM 2325 OE2 GLU A 219 -6.834 -45.263 7.610 1.00 92.49 O ANISOU 2325 OE2 GLU A 219 14328 6736 14077 2300 631 -1577 O ATOM 2326 N ARG A 220 -10.708 -42.282 12.327 1.00 63.77 N ANISOU 2326 N ARG A 220 10587 3648 9994 1577 -5 -610 N ATOM 2327 CA ARG A 220 -11.924 -41.620 12.793 1.00 62.62 C ANISOU 2327 CA ARG A 220 10502 3631 9659 1361 -125 -496 C ATOM 2328 C ARG A 220 -11.614 -40.566 13.847 1.00 58.57 C ANISOU 2328 C ARG A 220 9802 3300 9153 1400 -175 -332 C ATOM 2329 O ARG A 220 -12.212 -39.483 13.843 1.00 56.99 O ANISOU 2329 O ARG A 220 9572 3291 8792 1291 -177 -310 O ATOM 2330 CB ARG A 220 -12.911 -42.650 13.340 1.00 69.74 C ANISOU 2330 CB ARG A 220 11555 4384 10559 1182 -285 -387 C ATOM 2331 CG ARG A 220 -13.791 -43.290 12.281 1.00 81.10 C ANISOU 2331 CG ARG A 220 13204 5717 11895 1037 -284 -533 C ATOM 2332 CD ARG A 220 -14.734 -44.312 12.894 1.00 92.56 C ANISOU 2332 CD ARG A 220 14775 7026 13366 856 -440 -411 C ATOM 2333 NE ARG A 220 -15.426 -45.101 11.880 1.00102.29 N ANISOU 2333 NE ARG A 220 16201 8126 14538 740 -450 -555 N ATOM 2334 CZ ARG A 220 -16.217 -46.135 12.150 1.00109.99 C ANISOU 2334 CZ ARG A 220 17298 8950 15542 587 -567 -491 C ATOM 2335 NH1 ARG A 220 -16.416 -46.509 13.406 1.00112.64 N ANISOU 2335 NH1 ARG A 220 17589 9253 15957 530 -670 -282 N ATOM 2336 NH2 ARG A 220 -16.808 -46.797 11.164 1.00113.39 N ANISOU 2336 NH2 ARG A 220 17901 9267 15914 485 -583 -632 N ATOM 2337 N ALA A 221 -10.691 -40.865 14.765 1.00 54.86 N ANISOU 2337 N ALA A 221 9192 2787 8866 1542 -220 -212 N ATOM 2338 CA ALA A 221 -10.296 -39.874 15.761 1.00 56.86 C ANISOU 2338 CA ALA A 221 9261 3217 9127 1584 -284 -62 C ATOM 2339 C ALA A 221 -9.668 -38.655 15.098 1.00 53.56 C ANISOU 2339 C ALA A 221 8689 2986 8674 1692 -131 -176 C ATOM 2340 O ALA A 221 -9.965 -37.513 15.468 1.00 55.28 O ANISOU 2340 O ALA A 221 8767 3469 8766 1591 -138 -104 O ATOM 2341 CB ALA A 221 -9.333 -40.496 16.771 1.00 56.91 C ANISOU 2341 CB ALA A 221 9154 3143 9327 1719 -361 81 C ATOM 2342 N ARG A 222 -8.783 -38.885 14.124 1.00 56.80 N ANISOU 2342 N ARG A 222 9056 3334 9190 1854 42 -346 N ATOM 2343 CA ARG A 222 -8.198 -37.786 13.363 1.00 57.95 C ANISOU 2343 CA ARG A 222 9067 3662 9288 1938 223 -464 C ATOM 2344 C ARG A 222 -9.269 -36.976 12.643 1.00 58.30 C ANISOU 2344 C ARG A 222 9212 3878 9061 1745 280 -532 C ATOM 2345 O ARG A 222 -9.219 -35.741 12.629 1.00 55.29 O ANISOU 2345 O ARG A 222 8670 3752 8585 1703 335 -512 O ATOM 2346 CB ARG A 222 -7.183 -38.335 12.363 1.00 65.28 C ANISOU 2346 CB ARG A 222 9946 4512 10345 2099 368 -654 C ATOM 2347 CG ARG A 222 -6.434 -37.278 11.573 1.00 65.83 C ANISOU 2347 CG ARG A 222 9860 4789 10361 2179 566 -767 C ATOM 2348 CD ARG A 222 -5.487 -37.936 10.584 1.00 74.62 C ANISOU 2348 CD ARG A 222 10969 5823 11559 2330 705 -951 C ATOM 2349 NE ARG A 222 -4.637 -38.935 11.229 1.00 80.65 N ANISOU 2349 NE ARG A 222 11674 6425 12546 2500 586 -902 N ATOM 2350 CZ ARG A 222 -3.908 -39.831 10.573 1.00 87.73 C ANISOU 2350 CZ ARG A 222 12608 7184 13540 2645 661 -1041 C ATOM 2351 NH1 ARG A 222 -3.928 -39.864 9.248 1.00 89.58 N ANISOU 2351 NH1 ARG A 222 12936 7428 13673 2628 860 -1238 N ATOM 2352 NH2 ARG A 222 -3.165 -40.703 11.241 1.00 90.41 N ANISOU 2352 NH2 ARG A 222 12924 7381 14049 2811 544 -971 N ATOM 2353 N SER A 223 -10.250 -37.656 12.044 1.00 60.47 N ANISOU 2353 N SER A 223 9737 4021 9217 1612 248 -609 N ATOM 2354 CA SER A 223 -11.292 -36.954 11.301 1.00 57.21 C ANISOU 2354 CA SER A 223 9408 3767 8562 1417 271 -673 C ATOM 2355 C SER A 223 -12.163 -36.110 12.223 1.00 53.55 C ANISOU 2355 C SER A 223 8820 3529 7996 1234 138 -499 C ATOM 2356 O SER A 223 -12.604 -35.020 11.843 1.00 53.61 O ANISOU 2356 O SER A 223 8762 3758 7851 1136 182 -518 O ATOM 2357 CB SER A 223 -12.145 -37.958 10.525 1.00 61.79 C ANISOU 2357 CB SER A 223 10284 4133 9061 1308 230 -784 C ATOM 2358 OG SER A 223 -13.338 -37.357 10.054 1.00 67.22 O ANISOU 2358 OG SER A 223 11040 4964 9536 1088 179 -798 O ATOM 2359 N THR A 224 -12.420 -36.596 13.439 1.00 51.84 N ANISOU 2359 N THR A 224 8582 3254 7862 1186 -18 -328 N ATOM 2360 CA THR A 224 -13.184 -35.810 14.403 1.00 48.58 C ANISOU 2360 CA THR A 224 8053 3049 7355 1025 -118 -163 C ATOM 2361 C THR A 224 -12.410 -34.575 14.847 1.00 45.09 C ANISOU 2361 C THR A 224 7371 2841 6921 1113 -63 -112 C ATOM 2362 O THR A 224 -12.973 -33.476 14.927 1.00 44.07 O ANISOU 2362 O THR A 224 7147 2939 6658 999 -53 -80 O ATOM 2363 CB THR A 224 -13.560 -36.674 15.608 1.00 49.27 C ANISOU 2363 CB THR A 224 8201 3004 7517 957 -279 9 C ATOM 2364 OG1 THR A 224 -14.470 -37.700 15.194 1.00 56.30 O ANISOU 2364 OG1 THR A 224 9309 3698 8386 829 -339 -29 O ATOM 2365 CG2 THR A 224 -14.220 -35.830 16.688 1.00 47.13 C ANISOU 2365 CG2 THR A 224 7808 2950 7150 811 -351 177 C ATOM 2366 N LEU A 225 -11.116 -34.736 15.139 1.00 48.84 N ANISOU 2366 N LEU A 225 7738 3253 7567 1317 -33 -104 N ATOM 2367 CA LEU A 225 -10.297 -33.595 15.535 1.00 48.81 C ANISOU 2367 CA LEU A 225 7500 3454 7593 1400 8 -60 C ATOM 2368 C LEU A 225 -10.217 -32.557 14.421 1.00 51.64 C ANISOU 2368 C LEU A 225 7799 3982 7841 1397 177 -198 C ATOM 2369 O LEU A 225 -10.274 -31.350 14.684 1.00 53.20 O ANISOU 2369 O LEU A 225 7851 4406 7956 1342 188 -151 O ATOM 2370 CB LEU A 225 -8.901 -34.076 15.930 1.00 54.63 C ANISOU 2370 CB LEU A 225 8126 4063 8569 1624 0 -36 C ATOM 2371 CG LEU A 225 -8.668 -34.284 17.427 1.00 58.96 C ANISOU 2371 CG LEU A 225 8610 4589 9204 1632 -194 165 C ATOM 2372 CD1 LEU A 225 -7.415 -35.111 17.664 1.00 62.13 C ANISOU 2372 CD1 LEU A 225 8949 4785 9871 1857 -232 178 C ATOM 2373 CD2 LEU A 225 -8.577 -32.950 18.144 1.00 61.32 C ANISOU 2373 CD2 LEU A 225 8728 5150 9420 1574 -229 260 C ATOM 2374 N GLN A 226 -10.076 -33.006 13.171 1.00 55.29 N ANISOU 2374 N GLN A 226 8389 4329 8291 1453 311 -370 N ATOM 2375 CA GLN A 226 -9.977 -32.069 12.056 1.00 55.86 C ANISOU 2375 CA GLN A 226 8440 4545 8240 1446 477 -498 C ATOM 2376 C GLN A 226 -11.273 -31.290 11.868 1.00 53.86 C ANISOU 2376 C GLN A 226 8239 4460 7766 1230 419 -476 C ATOM 2377 O GLN A 226 -11.242 -30.116 11.482 1.00 48.44 O ANISOU 2377 O GLN A 226 7458 3967 6979 1199 496 -498 O ATOM 2378 CB GLN A 226 -9.602 -32.813 10.776 1.00 62.25 C ANISOU 2378 CB GLN A 226 9421 5173 9058 1543 635 -690 C ATOM 2379 CG GLN A 226 -8.193 -33.385 10.795 1.00 75.25 C ANISOU 2379 CG GLN A 226 10972 6675 10945 1784 744 -736 C ATOM 2380 CD GLN A 226 -7.908 -34.285 9.610 1.00 86.98 C ANISOU 2380 CD GLN A 226 12653 7958 12439 1875 897 -931 C ATOM 2381 OE1 GLN A 226 -8.820 -34.693 8.891 1.00 89.96 O ANISOU 2381 OE1 GLN A 226 13278 8257 12648 1752 882 -1020 O ATOM 2382 NE2 GLN A 226 -6.635 -34.606 9.404 1.00 90.83 N ANISOU 2382 NE2 GLN A 226 12981 8429 13101 2044 992 -991 N ATOM 2383 N LYS A 227 -12.415 -31.927 12.136 1.00 52.89 N ANISOU 2383 N LYS A 227 8258 4256 7583 1080 283 -427 N ATOM 2384 CA LYS A 227 -13.696 -31.232 12.077 1.00 46.66 C ANISOU 2384 CA LYS A 227 7486 3618 6626 877 211 -389 C ATOM 2385 C LYS A 227 -13.813 -30.212 13.201 1.00 43.89 C ANISOU 2385 C LYS A 227 6933 3477 6267 830 154 -238 C ATOM 2386 O LYS A 227 -14.397 -29.137 13.017 1.00 47.51 O ANISOU 2386 O LYS A 227 7325 4122 6607 732 163 -231 O ATOM 2387 CB LYS A 227 -14.841 -32.242 12.138 1.00 46.73 C ANISOU 2387 CB LYS A 227 7673 3474 6610 727 83 -367 C ATOM 2388 CG LYS A 227 -14.972 -33.097 10.889 1.00 56.83 C ANISOU 2388 CG LYS A 227 9186 4560 7847 728 121 -533 C ATOM 2389 CD LYS A 227 -16.159 -34.041 10.978 1.00 64.68 C ANISOU 2389 CD LYS A 227 10345 5405 8826 556 -27 -503 C ATOM 2390 CE LYS A 227 -16.284 -34.882 9.717 1.00 74.79 C ANISOU 2390 CE LYS A 227 11884 6481 10052 550 -4 -679 C ATOM 2391 NZ LYS A 227 -17.382 -35.881 9.815 1.00 80.64 N ANISOU 2391 NZ LYS A 227 12786 7050 10802 377 -163 -650 N ATOM 2392 N GLU A 228 -13.268 -30.536 14.375 1.00 43.75 N ANISOU 2392 N GLU A 228 6830 3421 6372 900 87 -118 N ATOM 2393 CA GLU A 228 -13.246 -29.581 15.477 1.00 44.51 C ANISOU 2393 CA GLU A 228 6757 3703 6451 868 36 14 C ATOM 2394 C GLU A 228 -12.358 -28.383 15.155 1.00 44.26 C ANISOU 2394 C GLU A 228 6560 3838 6420 963 141 -32 C ATOM 2395 O GLU A 228 -12.713 -27.242 15.473 1.00 41.17 O ANISOU 2395 O GLU A 228 6066 3640 5939 887 135 15 O ATOM 2396 CB GLU A 228 -12.782 -30.273 16.758 1.00 48.28 C ANISOU 2396 CB GLU A 228 7216 4079 7047 924 -75 151 C ATOM 2397 CG GLU A 228 -13.916 -30.867 17.579 1.00 54.77 C ANISOU 2397 CG GLU A 228 8144 4847 7817 762 -190 270 C ATOM 2398 CD GLU A 228 -13.432 -31.525 18.854 1.00 57.88 C ANISOU 2398 CD GLU A 228 8549 5138 8305 811 -306 417 C ATOM 2399 OE1 GLU A 228 -12.846 -32.624 18.773 1.00 57.39 O ANISOU 2399 OE1 GLU A 228 8570 4861 8375 917 -341 406 O ATOM 2400 OE2 GLU A 228 -13.642 -30.943 19.939 1.00 58.66 O ANISOU 2400 OE2 GLU A 228 8585 5362 8340 744 -365 544 O ATOM 2401 N VAL A 229 -11.194 -28.620 14.544 1.00 44.55 N ANISOU 2401 N VAL A 229 6564 3795 6567 1129 245 -123 N ATOM 2402 CA VAL A 229 -10.361 -27.507 14.096 1.00 41.26 C ANISOU 2402 CA VAL A 229 5994 3528 6157 1205 367 -174 C ATOM 2403 C VAL A 229 -11.122 -26.643 13.099 1.00 39.98 C ANISOU 2403 C VAL A 229 5888 3495 5810 1091 443 -255 C ATOM 2404 O VAL A 229 -11.090 -25.408 13.173 1.00 41.81 O ANISOU 2404 O VAL A 229 5997 3909 5978 1055 469 -229 O ATOM 2405 CB VAL A 229 -9.046 -28.030 13.488 1.00 45.35 C ANISOU 2405 CB VAL A 229 6473 3920 6840 1400 497 -271 C ATOM 2406 CG1 VAL A 229 -8.228 -26.883 12.911 1.00 41.89 C ANISOU 2406 CG1 VAL A 229 5878 3632 6405 1459 649 -328 C ATOM 2407 CG2 VAL A 229 -8.249 -28.794 14.518 1.00 51.96 C ANISOU 2407 CG2 VAL A 229 7228 4631 7883 1523 394 -176 C ATOM 2408 N HIS A 230 -11.817 -27.278 12.151 1.00 42.32 N ANISOU 2408 N HIS A 230 6379 3685 6017 1030 466 -353 N ATOM 2409 CA HIS A 230 -12.543 -26.524 11.133 1.00 45.09 C ANISOU 2409 CA HIS A 230 6806 4138 6189 921 513 -428 C ATOM 2410 C HIS A 230 -13.657 -25.692 11.753 1.00 44.37 C ANISOU 2410 C HIS A 230 6649 4204 6004 765 395 -324 C ATOM 2411 O HIS A 230 -13.884 -24.544 11.354 1.00 44.50 O ANISOU 2411 O HIS A 230 6611 4376 5922 714 430 -334 O ATOM 2412 CB HIS A 230 -13.108 -27.474 10.078 1.00 54.02 C ANISOU 2412 CB HIS A 230 8180 5103 7242 875 521 -546 C ATOM 2413 CG HIS A 230 -13.628 -26.780 8.858 1.00 63.95 C ANISOU 2413 CG HIS A 230 9545 6438 8315 788 573 -640 C ATOM 2414 ND1 HIS A 230 -14.953 -26.427 8.712 1.00 65.99 N ANISOU 2414 ND1 HIS A 230 9860 6762 8450 614 445 -607 N ATOM 2415 CD2 HIS A 230 -13.004 -26.374 7.727 1.00 67.57 C ANISOU 2415 CD2 HIS A 230 10069 6913 8691 848 734 -758 C ATOM 2416 CE1 HIS A 230 -15.121 -25.832 7.545 1.00 65.94 C ANISOU 2416 CE1 HIS A 230 9958 6805 8291 572 501 -697 C ATOM 2417 NE2 HIS A 230 -13.954 -25.788 6.927 1.00 67.01 N ANISOU 2417 NE2 HIS A 230 10114 6913 8433 707 684 -789 N ATOM 2418 N ALA A 231 -14.363 -26.257 12.735 1.00 41.92 N ANISOU 2418 N ALA A 231 6348 3851 5730 688 266 -221 N ATOM 2419 CA ALA A 231 -15.437 -25.520 13.392 1.00 40.67 C ANISOU 2419 CA ALA A 231 6118 3834 5500 546 180 -125 C ATOM 2420 C ALA A 231 -14.889 -24.396 14.260 1.00 44.86 C ANISOU 2420 C ALA A 231 6463 4532 6049 590 195 -45 C ATOM 2421 O ALA A 231 -15.490 -23.318 14.339 1.00 44.03 O ANISOU 2421 O ALA A 231 6284 4580 5863 510 187 -19 O ATOM 2422 CB ALA A 231 -16.293 -26.473 14.223 1.00 39.45 C ANISOU 2422 CB ALA A 231 6028 3579 5381 449 66 -34 C ATOM 2423 N ALA A 232 -13.753 -24.626 14.923 1.00 44.02 N ANISOU 2423 N ALA A 232 6281 4389 6056 716 205 -7 N ATOM 2424 CA ALA A 232 -13.153 -23.561 15.719 1.00 42.43 C ANISOU 2424 CA ALA A 232 5912 4335 5873 753 202 62 C ATOM 2425 C ALA A 232 -12.650 -22.428 14.834 1.00 41.15 C ANISOU 2425 C ALA A 232 5672 4293 5672 789 312 -17 C ATOM 2426 O ALA A 232 -12.725 -21.255 15.219 1.00 42.52 O ANISOU 2426 O ALA A 232 5740 4618 5799 751 306 25 O ATOM 2427 CB ALA A 232 -12.018 -24.120 16.575 1.00 37.83 C ANISOU 2427 CB ALA A 232 5266 3670 5436 878 158 124 C ATOM 2428 N LYS A 233 -12.126 -22.754 13.649 1.00 41.68 N ANISOU 2428 N LYS A 233 5801 4284 5751 859 423 -131 N ATOM 2429 CA LYS A 233 -11.718 -21.707 12.718 1.00 42.86 C ANISOU 2429 CA LYS A 233 5905 4539 5841 874 543 -202 C ATOM 2430 C LYS A 233 -12.915 -20.886 12.256 1.00 40.04 C ANISOU 2430 C LYS A 233 5603 4288 5322 734 510 -206 C ATOM 2431 O LYS A 233 -12.829 -19.657 12.149 1.00 35.57 O ANISOU 2431 O LYS A 233 4949 3858 4707 711 542 -194 O ATOM 2432 CB LYS A 233 -10.977 -22.310 11.525 1.00 49.77 C ANISOU 2432 CB LYS A 233 6869 5301 6742 970 690 -328 C ATOM 2433 CG LYS A 233 -9.594 -22.839 11.870 1.00 59.18 C ANISOU 2433 CG LYS A 233 7947 6409 8129 1134 753 -330 C ATOM 2434 CD LYS A 233 -8.817 -23.240 10.627 1.00 64.11 C ANISOU 2434 CD LYS A 233 8640 6940 8779 1236 947 -467 C ATOM 2435 CE LYS A 233 -7.416 -23.717 10.983 1.00 65.01 C ANISOU 2435 CE LYS A 233 8601 6972 9129 1412 1017 -466 C ATOM 2436 NZ LYS A 233 -6.693 -24.272 9.806 1.00 69.57 N ANISOU 2436 NZ LYS A 233 9254 7434 9747 1523 1232 -610 N ATOM 2437 N SER A 234 -14.041 -21.549 11.975 1.00 39.37 N ANISOU 2437 N SER A 234 5658 4132 5169 637 437 -221 N ATOM 2438 CA SER A 234 -15.240 -20.826 11.559 1.00 35.82 C ANISOU 2438 CA SER A 234 5243 3771 4597 505 380 -217 C ATOM 2439 C SER A 234 -15.704 -19.871 12.649 1.00 40.62 C ANISOU 2439 C SER A 234 5703 4520 5211 453 317 -112 C ATOM 2440 O SER A 234 -16.051 -18.717 12.374 1.00 42.58 O ANISOU 2440 O SER A 234 5899 4886 5392 408 321 -109 O ATOM 2441 CB SER A 234 -16.353 -21.812 11.201 1.00 34.56 C ANISOU 2441 CB SER A 234 5236 3497 4400 405 290 -239 C ATOM 2442 OG SER A 234 -15.952 -22.677 10.153 1.00 40.17 O ANISOU 2442 OG SER A 234 6113 4065 5084 450 349 -351 O ATOM 2443 N ALA A 235 -15.725 -20.344 13.895 1.00 37.12 N ANISOU 2443 N ALA A 235 5207 4055 4842 456 258 -26 N ATOM 2444 CA ALA A 235 -16.109 -19.485 15.009 1.00 35.82 C ANISOU 2444 CA ALA A 235 4925 4014 4669 411 215 65 C ATOM 2445 C ALA A 235 -15.124 -18.336 15.176 1.00 36.05 C ANISOU 2445 C ALA A 235 4834 4152 4710 484 268 67 C ATOM 2446 O ALA A 235 -15.522 -17.201 15.464 1.00 30.22 O ANISOU 2446 O ALA A 235 4023 3535 3926 439 260 95 O ATOM 2447 CB ALA A 235 -16.214 -20.307 16.293 1.00 33.43 C ANISOU 2447 CB ALA A 235 4628 3652 4423 400 150 157 C ATOM 2448 N ALA A 236 -13.829 -18.616 15.006 1.00 36.73 N ANISOU 2448 N ALA A 236 4892 4190 4874 598 323 38 N ATOM 2449 CA ALA A 236 -12.819 -17.571 15.140 1.00 36.62 C ANISOU 2449 CA ALA A 236 4749 4269 4896 660 370 42 C ATOM 2450 C ALA A 236 -12.956 -16.519 14.046 1.00 35.47 C ANISOU 2450 C ALA A 236 4605 4205 4667 627 447 -18 C ATOM 2451 O ALA A 236 -12.698 -15.333 14.285 1.00 34.48 O ANISOU 2451 O ALA A 236 4383 4187 4532 619 456 6 O ATOM 2452 CB ALA A 236 -11.421 -18.190 15.118 1.00 33.02 C ANISOU 2452 CB ALA A 236 4241 3731 4575 790 417 24 C ATOM 2453 N ILE A 237 -13.339 -16.933 12.835 1.00 31.42 N ANISOU 2453 N ILE A 237 4217 3633 4087 605 496 -95 N ATOM 2454 CA ILE A 237 -13.574 -15.968 11.763 1.00 33.64 C ANISOU 2454 CA ILE A 237 4535 3982 4264 561 551 -141 C ATOM 2455 C ILE A 237 -14.678 -14.997 12.159 1.00 34.18 C ANISOU 2455 C ILE A 237 4566 4152 4271 465 461 -87 C ATOM 2456 O ILE A 237 -14.577 -13.788 11.920 1.00 34.09 O ANISOU 2456 O ILE A 237 4502 4230 4221 450 485 -80 O ATOM 2457 CB ILE A 237 -13.893 -16.692 10.441 1.00 35.97 C ANISOU 2457 CB ILE A 237 5012 4181 4473 541 593 -232 C ATOM 2458 CG1 ILE A 237 -12.657 -17.428 9.924 1.00 34.55 C ANISOU 2458 CG1 ILE A 237 4863 3909 4358 654 729 -304 C ATOM 2459 CG2 ILE A 237 -14.402 -15.709 9.397 1.00 35.63 C ANISOU 2459 CG2 ILE A 237 5040 4202 4294 469 604 -260 C ATOM 2460 CD1 ILE A 237 -12.944 -18.387 8.794 1.00 35.75 C ANISOU 2460 CD1 ILE A 237 5224 3935 4426 644 769 -404 C ATOM 2461 N AILE A 238 -15.746 -15.511 12.776 1.00 30.42 N ANISOU 2461 N AILE A 238 4109 3654 3795 400 365 -45 N ATOM 2462 CA AILE A 238 -16.833 -14.651 13.235 1.00 30.93 C ANISOU 2462 CA AILE A 238 4118 3807 3829 320 296 5 C ATOM 2463 C AILE A 238 -16.321 -13.641 14.254 1.00 35.05 C ANISOU 2463 C AILE A 238 4510 4424 4382 351 307 56 C ATOM 2464 O AILE A 238 -16.659 -12.452 14.198 1.00 32.17 O ANISOU 2464 O AILE A 238 4095 4142 3985 323 302 65 O ATOM 2465 CB AILE A 238 -17.978 -15.501 13.817 1.00 36.40 C ANISOU 2465 CB AILE A 238 4836 4453 4542 245 217 45 C ATOM 2466 CG1AILE A 238 -18.531 -16.465 12.765 1.00 43.35 C ANISOU 2466 CG1AILE A 238 5853 5228 5391 198 183 -10 C ATOM 2467 CG2AILE A 238 -19.086 -14.605 14.354 1.00 30.98 C ANISOU 2467 CG2AILE A 238 4065 3857 3849 173 173 94 C ATOM 2468 CD1AILE A 238 -19.619 -15.870 11.907 1.00 49.07 C ANISOU 2468 CD1AILE A 238 6605 5984 6057 111 118 -27 C ATOM 2469 N ALA A 239 -15.497 -14.098 15.201 1.00 36.20 N ANISOU 2469 N ALA A 239 4612 4549 4595 409 309 90 N ATOM 2470 CA ALA A 239 -14.970 -13.194 16.218 1.00 33.30 C ANISOU 2470 CA ALA A 239 4143 4260 4249 431 297 136 C ATOM 2471 C ALA A 239 -14.012 -12.176 15.612 1.00 31.61 C ANISOU 2471 C ALA A 239 3867 4097 4046 472 356 104 C ATOM 2472 O ALA A 239 -14.022 -11.000 15.997 1.00 31.71 O ANISOU 2472 O ALA A 239 3817 4190 4042 452 345 123 O ATOM 2473 CB ALA A 239 -14.279 -13.991 17.324 1.00 31.16 C ANISOU 2473 CB ALA A 239 3856 3941 4044 479 255 186 C ATOM 2474 N GLY A 240 -13.176 -12.605 14.665 1.00 30.56 N ANISOU 2474 N GLY A 240 3755 3912 3943 527 432 53 N ATOM 2475 CA GLY A 240 -12.257 -11.674 14.032 1.00 30.72 C ANISOU 2475 CA GLY A 240 3716 3978 3979 554 512 27 C ATOM 2476 C GLY A 240 -12.969 -10.642 13.177 1.00 33.58 C ANISOU 2476 C GLY A 240 4126 4395 4239 487 528 9 C ATOM 2477 O GLY A 240 -12.548 -9.484 13.107 1.00 31.72 O ANISOU 2477 O GLY A 240 3828 4220 4003 478 553 20 O ATOM 2478 N LEU A 241 -14.057 -11.046 12.516 1.00 29.45 N ANISOU 2478 N LEU A 241 3716 3840 3634 435 499 -14 N ATOM 2479 CA LEU A 241 -14.825 -10.098 11.715 1.00 28.78 C ANISOU 2479 CA LEU A 241 3681 3795 3458 372 480 -20 C ATOM 2480 C LEU A 241 -15.548 -9.083 12.588 1.00 29.52 C ANISOU 2480 C LEU A 241 3692 3962 3563 335 404 31 C ATOM 2481 O LEU A 241 -15.701 -7.923 12.186 1.00 32.36 O ANISOU 2481 O LEU A 241 4043 4365 3888 309 401 39 O ATOM 2482 CB LEU A 241 -15.817 -10.841 10.820 1.00 33.58 C ANISOU 2482 CB LEU A 241 4427 4341 3990 320 435 -54 C ATOM 2483 CG LEU A 241 -15.190 -11.549 9.616 1.00 39.52 C ANISOU 2483 CG LEU A 241 5311 5019 4685 345 526 -126 C ATOM 2484 CD1 LEU A 241 -16.207 -12.438 8.920 1.00 42.84 C ANISOU 2484 CD1 LEU A 241 5882 5362 5033 286 451 -161 C ATOM 2485 CD2 LEU A 241 -14.595 -10.539 8.647 1.00 40.11 C ANISOU 2485 CD2 LEU A 241 5423 5130 4685 341 614 -143 C ATOM 2486 N PHE A 242 -16.012 -9.498 13.769 1.00 28.47 N ANISOU 2486 N PHE A 242 3510 3833 3474 331 351 66 N ATOM 2487 CA PHE A 242 -16.562 -8.538 14.720 1.00 26.50 C ANISOU 2487 CA PHE A 242 3186 3648 3234 308 310 104 C ATOM 2488 C PHE A 242 -15.518 -7.486 15.074 1.00 26.65 C ANISOU 2488 C PHE A 242 3137 3714 3277 340 338 111 C ATOM 2489 O PHE A 242 -15.806 -6.283 15.088 1.00 26.32 O ANISOU 2489 O PHE A 242 3066 3714 3220 320 326 118 O ATOM 2490 CB PHE A 242 -17.054 -9.267 15.974 1.00 23.60 C ANISOU 2490 CB PHE A 242 2801 3273 2895 298 276 140 C ATOM 2491 CG PHE A 242 -17.653 -8.356 17.013 1.00 26.47 C ANISOU 2491 CG PHE A 242 3107 3696 3256 276 260 168 C ATOM 2492 CD1 PHE A 242 -16.851 -7.700 17.935 1.00 26.68 C ANISOU 2492 CD1 PHE A 242 3094 3758 3287 305 262 182 C ATOM 2493 CD2 PHE A 242 -19.024 -8.162 17.070 1.00 25.16 C ANISOU 2493 CD2 PHE A 242 2927 3544 3090 227 242 177 C ATOM 2494 CE1 PHE A 242 -17.404 -6.857 18.885 1.00 29.92 C ANISOU 2494 CE1 PHE A 242 3479 4211 3677 286 258 194 C ATOM 2495 CE2 PHE A 242 -19.584 -7.325 18.021 1.00 25.87 C ANISOU 2495 CE2 PHE A 242 2966 3681 3183 218 255 192 C ATOM 2496 CZ PHE A 242 -18.772 -6.671 18.931 1.00 29.00 C ANISOU 2496 CZ PHE A 242 3352 4108 3560 248 268 195 C ATOM 2497 N ALA A 243 -14.297 -7.932 15.379 1.00 26.92 N ANISOU 2497 N ALA A 243 3135 3730 3363 390 368 112 N ATOM 2498 CA ALA A 243 -13.227 -7.001 15.717 1.00 28.67 C ANISOU 2498 CA ALA A 243 3277 3989 3630 411 381 122 C ATOM 2499 C ALA A 243 -12.906 -6.082 14.545 1.00 28.83 C ANISOU 2499 C ALA A 243 3304 4024 3626 394 444 101 C ATOM 2500 O ALA A 243 -12.690 -4.879 14.730 1.00 32.70 O ANISOU 2500 O ALA A 243 3751 4551 4122 373 434 114 O ATOM 2501 CB ALA A 243 -11.983 -7.773 16.156 1.00 25.96 C ANISOU 2501 CB ALA A 243 2875 3611 3375 470 389 132 C ATOM 2502 N ALEU A 244 -12.878 -6.630 13.328 0.50 29.61 N ANISOU 2502 N ALEU A 244 3477 4085 3687 397 511 68 N ATOM 2503 N BLEU A 244 -12.869 -6.630 13.327 0.50 29.61 N ANISOU 2503 N BLEU A 244 3477 4086 3688 397 511 68 N ATOM 2504 CA ALEU A 244 -12.544 -5.821 12.160 0.50 31.40 C ANISOU 2504 CA ALEU A 244 3742 4321 3868 373 583 53 C ATOM 2505 CA BLEU A 244 -12.545 -5.812 12.162 0.50 31.40 C ANISOU 2505 CA BLEU A 244 3741 4321 3868 373 583 54 C ATOM 2506 C ALEU A 244 -13.605 -4.758 11.898 0.50 30.41 C ANISOU 2506 C ALEU A 244 3661 4221 3671 316 517 72 C ATOM 2507 C BLEU A 244 -13.605 -4.746 11.919 0.50 30.37 C ANISOU 2507 C BLEU A 244 3655 4217 3669 316 516 73 C ATOM 2508 O ALEU A 244 -13.282 -3.643 11.474 0.50 31.39 O ANISOU 2508 O ALEU A 244 3782 4364 3781 291 542 87 O ATOM 2509 O BLEU A 244 -13.283 -3.621 11.521 0.50 31.33 O ANISOU 2509 O BLEU A 244 3771 4358 3776 291 539 88 O ATOM 2510 CB ALEU A 244 -12.370 -6.719 10.936 0.50 34.26 C ANISOU 2510 CB ALEU A 244 4211 4629 4175 385 671 6 C ATOM 2511 CB BLEU A 244 -12.390 -6.692 10.922 0.50 34.26 C ANISOU 2511 CB BLEU A 244 4213 4630 4174 383 670 7 C ATOM 2512 CG ALEU A 244 -12.008 -6.033 9.617 0.50 33.92 C ANISOU 2512 CG ALEU A 244 4249 4586 4052 352 768 -9 C ATOM 2513 CG BLEU A 244 -11.140 -7.564 10.813 0.50 36.64 C ANISOU 2513 CG BLEU A 244 4472 4893 4558 452 780 -24 C ATOM 2514 CD1ALEU A 244 -10.639 -5.378 9.709 0.50 37.28 C ANISOU 2514 CD1ALEU A 244 4560 5038 4567 372 872 5 C ATOM 2515 CD1BLEU A 244 -11.160 -8.343 9.509 0.50 37.44 C ANISOU 2515 CD1BLEU A 244 4720 4933 4574 457 878 -85 C ATOM 2516 CD2ALEU A 244 -12.059 -7.024 8.464 0.50 33.46 C ANISOU 2516 CD2ALEU A 244 4343 4464 3905 358 845 -67 C ATOM 2517 CD2BLEU A 244 -9.884 -6.714 10.913 0.50 39.94 C ANISOU 2517 CD2BLEU A 244 4763 5347 5066 466 858 -4 C ATOM 2518 N CYS A 245 -14.875 -5.080 12.151 1.00 26.26 N ANISOU 2518 N CYS A 245 3170 3689 3118 296 432 77 N ATOM 2519 CA CYS A 245 -15.950 -4.135 11.878 1.00 27.41 C ANISOU 2519 CA CYS A 245 3340 3849 3227 254 361 95 C ATOM 2520 C CYS A 245 -16.090 -3.077 12.964 1.00 29.43 C ANISOU 2520 C CYS A 245 3505 4143 3535 259 325 119 C ATOM 2521 O CYS A 245 -16.496 -1.948 12.667 1.00 29.41 O ANISOU 2521 O CYS A 245 3509 4145 3521 239 293 134 O ATOM 2522 CB CYS A 245 -17.274 -4.881 11.701 1.00 28.90 C ANISOU 2522 CB CYS A 245 3575 4012 3395 227 285 92 C ATOM 2523 SG CYS A 245 -17.364 -5.890 10.204 1.00 35.94 S ANISOU 2523 SG CYS A 245 4623 4840 4192 200 294 55 S ATOM 2524 N TRP A 246 -15.770 -3.408 14.215 1.00 26.44 N ANISOU 2524 N TRP A 246 3059 3782 3206 285 325 123 N ATOM 2525 CA TRP A 246 -15.967 -2.460 15.304 1.00 27.12 C ANISOU 2525 CA TRP A 246 3089 3896 3319 286 292 133 C ATOM 2526 C TRP A 246 -14.726 -1.652 15.655 1.00 30.69 C ANISOU 2526 C TRP A 246 3496 4360 3803 292 309 137 C ATOM 2527 O TRP A 246 -14.860 -0.549 16.196 1.00 28.66 O ANISOU 2527 O TRP A 246 3222 4112 3555 282 280 138 O ATOM 2528 CB TRP A 246 -16.464 -3.180 16.561 1.00 28.88 C ANISOU 2528 CB TRP A 246 3292 4128 3552 295 273 139 C ATOM 2529 CG TRP A 246 -17.913 -3.533 16.479 1.00 29.94 C ANISOU 2529 CG TRP A 246 3438 4257 3682 274 253 141 C ATOM 2530 CD1 TRP A 246 -18.445 -4.727 16.093 1.00 27.05 C ANISOU 2530 CD1 TRP A 246 3102 3865 3312 258 245 144 C ATOM 2531 CD2 TRP A 246 -19.021 -2.658 16.718 1.00 27.74 C ANISOU 2531 CD2 TRP A 246 3128 3988 3422 266 234 141 C ATOM 2532 NE1 TRP A 246 -19.817 -4.662 16.117 1.00 31.53 N ANISOU 2532 NE1 TRP A 246 3646 4432 3902 231 217 151 N ATOM 2533 CE2 TRP A 246 -20.196 -3.401 16.494 1.00 30.20 C ANISOU 2533 CE2 TRP A 246 3431 4287 3755 242 216 149 C ATOM 2534 CE3 TRP A 246 -19.133 -1.324 17.119 1.00 24.77 C ANISOU 2534 CE3 TRP A 246 2727 3623 3062 278 232 132 C ATOM 2535 CZ2 TRP A 246 -21.465 -2.855 16.654 1.00 25.16 C ANISOU 2535 CZ2 TRP A 246 2737 3653 3170 235 200 153 C ATOM 2536 CZ3 TRP A 246 -20.394 -0.784 17.277 1.00 23.43 C ANISOU 2536 CZ3 TRP A 246 2518 3450 2936 281 224 128 C ATOM 2537 CH2 TRP A 246 -21.543 -1.547 17.045 1.00 21.42 C ANISOU 2537 CH2 TRP A 246 2232 3188 2717 262 210 141 C ATOM 2538 N LEU A 247 -13.526 -2.166 15.382 1.00 29.18 N ANISOU 2538 N LEU A 247 3280 4163 3644 307 353 137 N ATOM 2539 CA LEU A 247 -12.318 -1.451 15.791 1.00 30.11 C ANISOU 2539 CA LEU A 247 3327 4290 3822 305 356 147 C ATOM 2540 C LEU A 247 -12.202 -0.050 15.197 1.00 28.97 C ANISOU 2540 C LEU A 247 3190 4144 3672 265 368 154 C ATOM 2541 O LEU A 247 -11.746 0.851 15.922 1.00 29.88 O ANISOU 2541 O LEU A 247 3264 4263 3827 247 327 160 O ATOM 2542 CB LEU A 247 -11.071 -2.283 15.464 1.00 27.55 C ANISOU 2542 CB LEU A 247 2948 3953 3566 335 415 147 C ATOM 2543 CG LEU A 247 -10.679 -3.311 16.527 1.00 34.04 C ANISOU 2543 CG LEU A 247 3727 4766 4439 376 364 157 C ATOM 2544 CD1 LEU A 247 -9.658 -4.298 15.982 1.00 34.25 C ANISOU 2544 CD1 LEU A 247 3703 4763 4546 425 433 151 C ATOM 2545 CD2 LEU A 247 -10.153 -2.610 17.776 1.00 36.72 C ANISOU 2545 CD2 LEU A 247 4010 5121 4818 362 273 177 C ATOM 2546 N PRO A 248 -12.561 0.210 13.929 1.00 30.12 N ANISOU 2546 N PRO A 248 3403 4276 3767 243 411 158 N ATOM 2547 CA PRO A 248 -12.383 1.576 13.410 1.00 28.05 C ANISOU 2547 CA PRO A 248 3158 3999 3500 200 415 178 C ATOM 2548 C PRO A 248 -13.118 2.620 14.233 1.00 28.14 C ANISOU 2548 C PRO A 248 3169 4003 3520 195 330 177 C ATOM 2549 O PRO A 248 -12.548 3.676 14.531 1.00 31.05 O ANISOU 2549 O PRO A 248 3512 4358 3929 167 315 186 O ATOM 2550 CB PRO A 248 -12.931 1.468 11.982 1.00 28.72 C ANISOU 2550 CB PRO A 248 3351 4063 3498 179 449 186 C ATOM 2551 CG PRO A 248 -12.580 0.076 11.601 1.00 27.54 C ANISOU 2551 CG PRO A 248 3213 3917 3333 207 517 162 C ATOM 2552 CD PRO A 248 -12.941 -0.708 12.838 1.00 22.96 C ANISOU 2552 CD PRO A 248 2573 3353 2798 248 457 146 C ATOM 2553 N LEU A 249 -14.372 2.351 14.609 1.00 25.16 N ANISOU 2553 N LEU A 249 2816 3628 3117 219 283 164 N ATOM 2554 CA LEU A 249 -15.125 3.302 15.420 1.00 27.27 C ANISOU 2554 CA LEU A 249 3079 3881 3401 228 228 152 C ATOM 2555 C LEU A 249 -14.471 3.504 16.781 1.00 28.24 C ANISOU 2555 C LEU A 249 3162 4015 3551 232 210 131 C ATOM 2556 O LEU A 249 -14.365 4.636 17.266 1.00 30.97 O ANISOU 2556 O LEU A 249 3516 4334 3916 219 179 119 O ATOM 2557 CB LEU A 249 -16.565 2.823 15.599 1.00 27.81 C ANISOU 2557 CB LEU A 249 3154 3953 3458 256 204 141 C ATOM 2558 CG LEU A 249 -17.696 3.567 14.888 1.00 31.51 C ANISOU 2558 CG LEU A 249 3648 4386 3938 259 158 155 C ATOM 2559 CD1 LEU A 249 -19.040 3.057 15.392 1.00 29.91 C ANISOU 2559 CD1 LEU A 249 3407 4193 3765 287 142 141 C ATOM 2560 CD2 LEU A 249 -17.578 5.072 15.084 1.00 28.22 C ANISOU 2560 CD2 LEU A 249 3240 3928 3555 259 133 154 C ATOM 2561 N HIS A 250 -14.023 2.415 17.412 1.00 25.36 N ANISOU 2561 N HIS A 250 2770 3679 3186 246 216 128 N ATOM 2562 CA HIS A 250 -13.329 2.532 18.691 1.00 25.94 C ANISOU 2562 CA HIS A 250 2824 3759 3273 242 173 117 C ATOM 2563 C HIS A 250 -12.029 3.313 18.555 1.00 24.55 C ANISOU 2563 C HIS A 250 2603 3567 3156 206 153 129 C ATOM 2564 O HIS A 250 -11.708 4.148 19.408 1.00 27.75 O ANISOU 2564 O HIS A 250 3018 3954 3572 182 93 113 O ATOM 2565 CB HIS A 250 -13.045 1.144 19.265 1.00 27.03 C ANISOU 2565 CB HIS A 250 2948 3919 3405 265 167 127 C ATOM 2566 CG HIS A 250 -14.252 0.441 19.802 1.00 26.08 C ANISOU 2566 CG HIS A 250 2871 3808 3229 284 179 119 C ATOM 2567 ND1 HIS A 250 -14.929 0.877 20.921 1.00 25.21 N ANISOU 2567 ND1 HIS A 250 2805 3700 3073 282 166 97 N ATOM 2568 CD2 HIS A 250 -14.893 -0.677 19.385 1.00 26.77 C ANISOU 2568 CD2 HIS A 250 2967 3900 3304 298 210 130 C ATOM 2569 CE1 HIS A 250 -15.936 0.058 21.170 1.00 27.30 C ANISOU 2569 CE1 HIS A 250 3090 3976 3308 292 201 101 C ATOM 2570 NE2 HIS A 250 -15.940 -0.890 20.249 1.00 26.62 N ANISOU 2570 NE2 HIS A 250 2979 3889 3245 298 217 122 N ATOM 2571 N ILE A 251 -11.257 3.038 17.502 1.00 22.39 N ANISOU 2571 N ILE A 251 2286 3297 2926 194 208 154 N ATOM 2572 CA ILE A 251 -10.001 3.751 17.289 1.00 25.41 C ANISOU 2572 CA ILE A 251 2603 3665 3389 150 210 173 C ATOM 2573 C ILE A 251 -10.257 5.239 17.086 1.00 24.00 C ANISOU 2573 C ILE A 251 2468 3446 3203 104 189 174 C ATOM 2574 O ILE A 251 -9.535 6.086 17.626 1.00 29.75 O ANISOU 2574 O ILE A 251 3167 4149 3987 60 134 174 O ATOM 2575 CB ILE A 251 -9.229 3.131 16.109 1.00 29.10 C ANISOU 2575 CB ILE A 251 3019 4141 3897 150 314 196 C ATOM 2576 CG1 ILE A 251 -8.766 1.715 16.467 1.00 31.84 C ANISOU 2576 CG1 ILE A 251 3307 4506 4283 202 322 193 C ATOM 2577 CG2 ILE A 251 -8.037 3.997 15.727 1.00 31.47 C ANISOU 2577 CG2 ILE A 251 3242 4425 4290 90 346 223 C ATOM 2578 CD1 ILE A 251 -8.158 0.955 15.307 1.00 33.96 C ANISOU 2578 CD1 ILE A 251 3542 4775 4585 221 448 198 C ATOM 2579 N ILE A 252 -11.282 5.582 16.302 1.00 23.89 N ANISOU 2579 N ILE A 252 2529 3416 3132 113 216 176 N ATOM 2580 CA ILE A 252 -11.647 6.988 16.125 1.00 25.82 C ANISOU 2580 CA ILE A 252 2826 3606 3378 82 183 180 C ATOM 2581 C ILE A 252 -11.979 7.632 17.467 1.00 26.96 C ANISOU 2581 C ILE A 252 2993 3726 3526 93 106 136 C ATOM 2582 O ILE A 252 -11.550 8.755 17.756 1.00 29.45 O ANISOU 2582 O ILE A 252 3323 3990 3878 51 62 130 O ATOM 2583 CB ILE A 252 -12.813 7.119 15.129 1.00 26.37 C ANISOU 2583 CB ILE A 252 2971 3657 3393 102 198 196 C ATOM 2584 CG1 ILE A 252 -12.353 6.742 13.718 1.00 27.14 C ANISOU 2584 CG1 ILE A 252 3091 3762 3461 71 273 239 C ATOM 2585 CG2 ILE A 252 -13.393 8.525 15.157 1.00 23.16 C ANISOU 2585 CG2 ILE A 252 2619 3180 3001 94 143 197 C ATOM 2586 CD1 ILE A 252 -13.484 6.582 12.734 1.00 29.25 C ANISOU 2586 CD1 ILE A 252 3445 4014 3655 87 261 256 C ATOM 2587 N ASN A 253 -12.762 6.940 18.301 1.00 25.52 N ANISOU 2587 N ASN A 253 2826 3572 3298 144 96 101 N ATOM 2588 CA ASN A 253 -13.048 7.460 19.636 1.00 27.79 C ANISOU 2588 CA ASN A 253 3157 3837 3564 154 45 51 C ATOM 2589 C ASN A 253 -11.769 7.693 20.431 1.00 29.85 C ANISOU 2589 C ASN A 253 3398 4089 3853 104 -24 46 C ATOM 2590 O ASN A 253 -11.671 8.661 21.193 1.00 30.99 O ANISOU 2590 O ASN A 253 3598 4183 3993 79 -82 8 O ATOM 2591 CB ASN A 253 -13.989 6.522 20.393 1.00 25.31 C ANISOU 2591 CB ASN A 253 2864 3562 3190 204 70 24 C ATOM 2592 CG ASN A 253 -15.418 6.590 19.883 1.00 26.53 C ANISOU 2592 CG ASN A 253 3030 3708 3341 249 115 18 C ATOM 2593 OD1 ASN A 253 -15.807 7.549 19.215 1.00 32.32 O ANISOU 2593 OD1 ASN A 253 3777 4393 4111 252 107 22 O ATOM 2594 ND2 ASN A 253 -16.214 5.580 20.215 1.00 27.79 N ANISOU 2594 ND2 ASN A 253 3181 3907 3470 280 153 13 N ATOM 2595 N CYS A 254 -10.776 6.817 20.264 1.00 24.34 N ANISOU 2595 N CYS A 254 2620 3432 3196 89 -26 82 N ATOM 2596 CA CYS A 254 -9.510 7.003 20.964 1.00 25.90 C ANISOU 2596 CA CYS A 254 2771 3618 3452 39 -114 88 C ATOM 2597 C CYS A 254 -8.802 8.272 20.501 1.00 22.29 C ANISOU 2597 C CYS A 254 2289 3107 3073 -32 -136 101 C ATOM 2598 O CYS A 254 -8.232 9.005 21.319 1.00 27.83 O ANISOU 2598 O CYS A 254 3008 3767 3800 -84 -237 81 O ATOM 2599 CB CYS A 254 -8.620 5.776 20.770 1.00 26.58 C ANISOU 2599 CB CYS A 254 2751 3750 3600 53 -105 129 C ATOM 2600 SG CYS A 254 -9.166 4.313 21.684 1.00 28.57 S ANISOU 2600 SG CYS A 254 3045 4041 3770 116 -126 122 S ATOM 2601 N PHE A 255 -8.819 8.546 19.193 1.00 23.80 N ANISOU 2601 N PHE A 255 2455 3293 3297 -46 -47 138 N ATOM 2602 CA PHE A 255 -8.227 9.786 18.697 1.00 25.32 C ANISOU 2602 CA PHE A 255 2639 3425 3558 -123 -56 162 C ATOM 2603 C PHE A 255 -8.968 10.999 19.240 1.00 26.27 C ANISOU 2603 C PHE A 255 2875 3468 3637 -129 -120 117 C ATOM 2604 O PHE A 255 -8.342 11.986 19.647 1.00 31.19 O ANISOU 2604 O PHE A 255 3509 4027 4314 -199 -195 109 O ATOM 2605 CB PHE A 255 -8.205 9.794 17.167 1.00 22.89 C ANISOU 2605 CB PHE A 255 2316 3121 3259 -138 61 216 C ATOM 2606 CG PHE A 255 -7.012 9.093 16.581 1.00 26.66 C ANISOU 2606 CG PHE A 255 2667 3641 3821 -166 138 258 C ATOM 2607 CD1 PHE A 255 -5.837 9.786 16.345 1.00 27.86 C ANISOU 2607 CD1 PHE A 255 2733 3764 4090 -256 146 296 C ATOM 2608 CD2 PHE A 255 -7.060 7.740 16.278 1.00 26.96 C ANISOU 2608 CD2 PHE A 255 2667 3741 3837 -103 208 257 C ATOM 2609 CE1 PHE A 255 -4.733 9.148 15.814 1.00 33.42 C ANISOU 2609 CE1 PHE A 255 3298 4505 4896 -275 239 332 C ATOM 2610 CE2 PHE A 255 -5.958 7.095 15.746 1.00 30.47 C ANISOU 2610 CE2 PHE A 255 2990 4214 4375 -114 295 287 C ATOM 2611 CZ PHE A 255 -4.793 7.799 15.514 1.00 33.09 C ANISOU 2611 CZ PHE A 255 3220 4522 4832 -197 319 324 C ATOM 2612 N THR A 256 -10.303 10.950 19.240 1.00 25.11 N ANISOU 2612 N THR A 256 2810 3319 3412 -57 -90 86 N ATOM 2613 CA THR A 256 -11.084 12.074 19.744 1.00 26.65 C ANISOU 2613 CA THR A 256 3108 3432 3585 -42 -131 35 C ATOM 2614 C THR A 256 -10.755 12.336 21.207 1.00 29.18 C ANISOU 2614 C THR A 256 3480 3728 3881 -60 -218 -31 C ATOM 2615 O THR A 256 -10.628 13.491 21.633 1.00 32.70 O ANISOU 2615 O THR A 256 3997 4083 4343 -97 -279 -68 O ATOM 2616 CB THR A 256 -12.578 11.794 19.573 1.00 29.25 C ANISOU 2616 CB THR A 256 3480 3772 3861 49 -78 13 C ATOM 2617 OG1 THR A 256 -12.882 11.643 18.181 1.00 33.54 O ANISOU 2617 OG1 THR A 256 4002 4325 4418 54 -28 76 O ATOM 2618 CG2 THR A 256 -13.409 12.934 20.151 1.00 23.48 C ANISOU 2618 CG2 THR A 256 2841 2949 3130 84 -103 -49 C ATOM 2619 N PHE A 257 -10.602 11.266 21.987 1.00 25.28 N ANISOU 2619 N PHE A 257 2965 3302 3336 -38 -232 -44 N ATOM 2620 CA PHE A 257 -10.423 11.368 23.429 1.00 27.92 C ANISOU 2620 CA PHE A 257 3383 3617 3606 -52 -319 -105 C ATOM 2621 C PHE A 257 -8.985 11.724 23.789 1.00 31.11 C ANISOU 2621 C PHE A 257 3746 3994 4082 -148 -445 -87 C ATOM 2622 O PHE A 257 -8.744 12.655 24.565 1.00 31.77 O ANISOU 2622 O PHE A 257 3923 4000 4148 -197 -539 -138 O ATOM 2623 CB PHE A 257 -10.834 10.051 24.090 1.00 24.72 C ANISOU 2623 CB PHE A 257 2988 3290 3114 1 -294 -110 C ATOM 2624 CG PHE A 257 -10.717 10.053 25.586 1.00 27.83 C ANISOU 2624 CG PHE A 257 3501 3667 3407 -17 -378 -165 C ATOM 2625 CD1 PHE A 257 -11.539 10.856 26.361 1.00 25.43 C ANISOU 2625 CD1 PHE A 257 3344 3303 3013 4 -356 -250 C ATOM 2626 CD2 PHE A 257 -9.796 9.235 26.218 1.00 28.06 C ANISOU 2626 CD2 PHE A 257 3505 3731 3425 -50 -479 -133 C ATOM 2627 CE1 PHE A 257 -11.433 10.852 27.740 1.00 28.37 C ANISOU 2627 CE1 PHE A 257 3862 3656 3262 -19 -425 -307 C ATOM 2628 CE2 PHE A 257 -9.684 9.225 27.594 1.00 30.71 C ANISOU 2628 CE2 PHE A 257 3980 4046 3643 -75 -575 -177 C ATOM 2629 CZ PHE A 257 -10.506 10.035 28.358 1.00 32.99 C ANISOU 2629 CZ PHE A 257 4441 4279 3816 -64 -543 -266 C ATOM 2630 N PHE A 258 -8.018 10.990 23.234 1.00 30.31 N ANISOU 2630 N PHE A 258 3500 3946 4069 -175 -448 -17 N ATOM 2631 CA PHE A 258 -6.625 11.130 23.641 1.00 28.37 C ANISOU 2631 CA PHE A 258 3174 3684 3922 -260 -575 9 C ATOM 2632 C PHE A 258 -5.893 12.258 22.922 1.00 31.14 C ANISOU 2632 C PHE A 258 3465 3970 4398 -352 -586 40 C ATOM 2633 O PHE A 258 -4.844 12.696 23.406 1.00 34.08 O ANISOU 2633 O PHE A 258 3788 4302 4858 -441 -714 48 O ATOM 2634 CB PHE A 258 -5.874 9.817 23.400 1.00 28.86 C ANISOU 2634 CB PHE A 258 3086 3825 4056 -239 -566 70 C ATOM 2635 CG PHE A 258 -6.240 8.718 24.358 1.00 32.96 C ANISOU 2635 CG PHE A 258 3664 4388 4472 -179 -610 54 C ATOM 2636 CD1 PHE A 258 -6.091 8.888 25.724 1.00 30.03 C ANISOU 2636 CD1 PHE A 258 3405 3985 4021 -210 -761 16 C ATOM 2637 CD2 PHE A 258 -6.717 7.504 23.885 1.00 30.40 C ANISOU 2637 CD2 PHE A 258 3299 4129 4121 -101 -505 80 C ATOM 2638 CE1 PHE A 258 -6.424 7.873 26.605 1.00 31.70 C ANISOU 2638 CE1 PHE A 258 3692 4232 4120 -164 -798 13 C ATOM 2639 CE2 PHE A 258 -7.050 6.484 24.759 1.00 30.77 C ANISOU 2639 CE2 PHE A 258 3409 4208 4077 -55 -544 76 C ATOM 2640 CZ PHE A 258 -6.903 6.668 26.122 1.00 33.19 C ANISOU 2640 CZ PHE A 258 3829 4484 4296 -87 -687 47 C ATOM 2641 N CYS A 259 -6.410 12.737 21.789 1.00 34.58 N ANISOU 2641 N CYS A 259 3905 4387 4845 -340 -466 63 N ATOM 2642 CA CYS A 259 -5.755 13.772 20.989 1.00 38.46 C ANISOU 2642 CA CYS A 259 4352 4814 5447 -433 -455 108 C ATOM 2643 C CYS A 259 -6.675 14.971 20.777 1.00 39.01 C ANISOU 2643 C CYS A 259 4569 4788 5467 -428 -443 75 C ATOM 2644 O CYS A 259 -7.193 15.180 19.671 1.00 32.64 O ANISOU 2644 O CYS A 259 3775 3972 4654 -407 -342 117 O ATOM 2645 CB CYS A 259 -5.268 13.241 19.642 1.00 43.77 C ANISOU 2645 CB CYS A 259 4893 5543 6195 -443 -318 190 C ATOM 2646 SG CYS A 259 -4.125 14.413 18.860 1.00 50.33 S ANISOU 2646 SG CYS A 259 5643 6298 7181 -590 -306 259 S ATOM 2647 N PRO A 260 -6.906 15.779 21.817 1.00 42.73 N ANISOU 2647 N PRO A 260 5162 5175 5897 -443 -550 0 N ATOM 2648 CA PRO A 260 -7.728 16.985 21.632 1.00 43.41 C ANISOU 2648 CA PRO A 260 5383 5149 5963 -429 -541 -35 C ATOM 2649 C PRO A 260 -7.064 18.038 20.758 1.00 46.15 C ANISOU 2649 C PRO A 260 5707 5407 6423 -535 -549 30 C ATOM 2650 O PRO A 260 -7.747 18.977 20.328 1.00 48.21 O ANISOU 2650 O PRO A 260 6069 5570 6680 -519 -531 26 O ATOM 2651 CB PRO A 260 -7.926 17.496 23.063 1.00 46.33 C ANISOU 2651 CB PRO A 260 5894 5447 6263 -428 -651 -143 C ATOM 2652 CG PRO A 260 -6.710 17.024 23.792 1.00 45.96 C ANISOU 2652 CG PRO A 260 5774 5439 6249 -511 -771 -133 C ATOM 2653 CD PRO A 260 -6.368 15.683 23.187 1.00 43.67 C ANISOU 2653 CD PRO A 260 5317 5283 5991 -479 -694 -56 C ATOM 2654 N ASP A 261 -5.761 17.917 20.489 1.00 41.43 N ANISOU 2654 N ASP A 261 4973 4833 5936 -643 -572 95 N ATOM 2655 CA ASP A 261 -5.093 18.761 19.507 1.00 46.37 C ANISOU 2655 CA ASP A 261 5556 5391 6672 -754 -540 177 C ATOM 2656 C ASP A 261 -5.290 18.273 18.078 1.00 39.61 C ANISOU 2656 C ASP A 261 4646 4599 5805 -728 -375 264 C ATOM 2657 O ASP A 261 -4.952 19.002 17.140 1.00 39.46 O ANISOU 2657 O ASP A 261 4632 4519 5842 -812 -323 339 O ATOM 2658 CB ASP A 261 -3.595 18.845 19.814 1.00 52.57 C ANISOU 2658 CB ASP A 261 6196 6173 7603 -889 -621 212 C ATOM 2659 CG ASP A 261 -3.308 19.540 21.129 1.00 68.75 C ANISOU 2659 CG ASP A 261 8328 8129 9663 -948 -813 132 C ATOM 2660 OD1 ASP A 261 -4.161 20.334 21.580 1.00 73.64 O ANISOU 2660 OD1 ASP A 261 9134 8650 10197 -911 -859 58 O ATOM 2661 OD2 ASP A 261 -2.233 19.289 21.714 1.00 75.81 O ANISOU 2661 OD2 ASP A 261 9106 9045 10655 -1030 -924 142 O ATOM 2662 N CYS A 262 -5.813 17.065 17.892 1.00 37.94 N ANISOU 2662 N CYS A 262 4400 4502 5515 -623 -295 257 N ATOM 2663 CA CYS A 262 -6.101 16.536 16.567 1.00 38.07 C ANISOU 2663 CA CYS A 262 4399 4575 5492 -593 -150 325 C ATOM 2664 C CYS A 262 -7.484 16.986 16.120 1.00 36.85 C ANISOU 2664 C CYS A 262 4395 4366 5241 -516 -141 316 C ATOM 2665 O CYS A 262 -8.418 17.059 16.924 1.00 34.05 O ANISOU 2665 O CYS A 262 4114 3990 4832 -430 -203 241 O ATOM 2666 CB CYS A 262 -6.041 15.006 16.558 1.00 41.23 C ANISOU 2666 CB CYS A 262 4701 5107 5859 -517 -80 318 C ATOM 2667 SG CYS A 262 -4.430 14.235 16.860 1.00 50.08 S ANISOU 2667 SG CYS A 262 5608 6298 7121 -580 -73 344 S ATOM 2668 N ASER A 263 -7.609 17.289 14.831 1.00 33.52 N ANISOU 2668 N ASER A 263 4018 3919 4800 -547 -62 397 N ATOM 2669 CA ASER A 263 -8.925 17.539 14.265 1.00 39.15 C ANISOU 2669 CA ASER A 263 4856 4589 5430 -467 -67 405 C ATOM 2670 C ASER A 263 -9.776 16.282 14.375 1.00 37.39 C ANISOU 2670 C ASER A 263 4609 4473 5126 -350 -35 363 C ATOM 2671 O ASER A 263 -9.287 15.167 14.181 1.00 35.63 O ANISOU 2671 O ASER A 263 4299 4354 4885 -347 40 371 O ATOM 2672 CB ASER A 263 -8.807 17.968 12.801 1.00 47.42 C ANISOU 2672 CB ASER A 263 5972 5596 6452 -535 3 513 C ATOM 2673 OG ASER A 263 -8.049 19.158 12.674 1.00 59.49 O ANISOU 2673 OG ASER A 263 7528 7015 8060 -656 -21 562 O ATOM 2674 N HIS A 264 -11.049 16.467 14.718 1.00 34.81 N ANISOU 2674 N HIS A 264 4351 4109 4764 -252 -89 316 N ATOM 2675 CA HIS A 264 -11.990 15.355 14.743 1.00 34.71 C ANISOU 2675 CA HIS A 264 4318 4184 4687 -151 -62 286 C ATOM 2676 C HIS A 264 -11.976 14.632 13.403 1.00 35.78 C ANISOU 2676 C HIS A 264 4458 4375 4761 -167 11 360 C ATOM 2677 O HIS A 264 -11.835 15.258 12.349 1.00 39.33 O ANISOU 2677 O HIS A 264 4980 4767 5195 -225 23 435 O ATOM 2678 CB HIS A 264 -13.401 15.843 15.073 1.00 34.21 C ANISOU 2678 CB HIS A 264 4316 4056 4625 -54 -120 244 C ATOM 2679 CG HIS A 264 -14.315 14.758 15.554 1.00 36.20 C ANISOU 2679 CG HIS A 264 4521 4393 4838 41 -96 192 C ATOM 2680 ND1 HIS A 264 -14.759 13.740 14.737 1.00 36.95 N ANISOU 2680 ND1 HIS A 264 4593 4562 4883 66 -60 230 N ATOM 2681 CD2 HIS A 264 -14.858 14.525 16.773 1.00 35.33 C ANISOU 2681 CD2 HIS A 264 4394 4301 4728 107 -98 107 C ATOM 2682 CE1 HIS A 264 -15.542 12.931 15.428 1.00 35.88 C ANISOU 2682 CE1 HIS A 264 4413 4484 4734 140 -47 176 C ATOM 2683 NE2 HIS A 264 -15.618 13.385 16.667 1.00 35.52 N ANISOU 2683 NE2 HIS A 264 4371 4410 4716 166 -60 104 N ATOM 2684 N ALA A 265 -12.078 13.306 13.454 1.00 31.97 N ANISOU 2684 N ALA A 265 3916 3997 4234 -123 62 337 N ATOM 2685 CA ALA A 265 -12.263 12.528 12.239 1.00 32.82 C ANISOU 2685 CA ALA A 265 4056 4150 4264 -124 125 386 C ATOM 2686 C ALA A 265 -13.350 13.166 11.375 1.00 34.69 C ANISOU 2686 C ALA A 265 4406 4312 4460 -104 62 432 C ATOM 2687 O ALA A 265 -14.400 13.569 11.895 1.00 33.74 O ANISOU 2687 O ALA A 265 4295 4148 4375 -34 -21 399 O ATOM 2688 CB ALA A 265 -12.639 11.084 12.579 1.00 31.11 C ANISOU 2688 CB ALA A 265 3782 4028 4012 -56 154 340 C ATOM 2689 N PRO A 266 -13.139 13.267 10.065 1.00 36.15 N ANISOU 2689 N PRO A 266 4682 4478 4575 -163 99 508 N ATOM 2690 CA PRO A 266 -14.111 13.955 9.209 1.00 37.96 C ANISOU 2690 CA PRO A 266 5037 4622 4765 -154 8 568 C ATOM 2691 C PRO A 266 -15.435 13.215 9.120 1.00 37.48 C ANISOU 2691 C PRO A 266 4975 4588 4676 -66 -65 544 C ATOM 2692 O PRO A 266 -15.553 12.029 9.437 1.00 36.09 O ANISOU 2692 O PRO A 266 4730 4503 4480 -29 -23 494 O ATOM 2693 CB PRO A 266 -13.414 14.008 7.845 1.00 37.59 C ANISOU 2693 CB PRO A 266 5103 4565 4615 -253 86 654 C ATOM 2694 CG PRO A 266 -12.402 12.919 7.882 1.00 40.00 C ANISOU 2694 CG PRO A 266 5326 4974 4897 -278 232 621 C ATOM 2695 CD PRO A 266 -11.977 12.768 9.310 1.00 39.48 C ANISOU 2695 CD PRO A 266 5102 4948 4949 -242 230 545 C ATOM 2696 N ALEU A 267 -16.446 13.960 8.671 1.00 36.38 N ANISOU 2696 N ALEU A 267 4910 4359 4554 -35 -186 587 N ATOM 2697 CA ALEU A 267 -17.811 13.448 8.648 1.00 35.00 C ANISOU 2697 CA ALEU A 267 4708 4192 4398 49 -280 571 C ATOM 2698 C ALEU A 267 -17.936 12.218 7.756 1.00 37.64 C ANISOU 2698 C ALEU A 267 5091 4598 4613 24 -261 588 C ATOM 2699 O ALEU A 267 -18.643 11.264 8.101 1.00 39.40 O ANISOU 2699 O ALEU A 267 5237 4878 4853 77 -278 541 O ATOM 2700 CB ALEU A 267 -18.759 14.553 8.187 1.00 41.30 C ANISOU 2700 CB ALEU A 267 5574 4864 5254 82 -428 630 C ATOM 2701 CG ALEU A 267 -20.223 14.161 8.030 1.00 48.88 C ANISOU 2701 CG ALEU A 267 6490 5815 6267 164 -550 630 C ATOM 2702 CD1ALEU A 267 -20.716 13.507 9.302 1.00 50.23 C ANISOU 2702 CD1ALEU A 267 6495 6057 6532 245 -496 529 C ATOM 2703 CD2ALEU A 267 -21.084 15.361 7.666 1.00 49.37 C ANISOU 2703 CD2ALEU A 267 6598 5736 6423 210 -706 691 C ATOM 2704 N TRP A 268 -17.258 12.219 6.605 1.00 37.33 N ANISOU 2704 N TRP A 268 5189 4550 4447 -63 -218 653 N ATOM 2705 CA TRP A 268 -17.347 11.076 5.703 1.00 36.34 C ANISOU 2705 CA TRP A 268 5143 4477 4187 -90 -194 659 C ATOM 2706 C TRP A 268 -16.757 9.822 6.337 1.00 37.72 C ANISOU 2706 C TRP A 268 5209 4759 4365 -72 -63 577 C ATOM 2707 O TRP A 268 -17.242 8.713 6.088 1.00 36.00 O ANISOU 2707 O TRP A 268 4999 4583 4094 -53 -76 548 O ATOM 2708 CB TRP A 268 -16.663 11.388 4.370 1.00 34.52 C ANISOU 2708 CB TRP A 268 5105 4209 3802 -191 -143 739 C ATOM 2709 CG TRP A 268 -15.184 11.564 4.456 1.00 35.92 C ANISOU 2709 CG TRP A 268 5262 4416 3970 -258 42 738 C ATOM 2710 CD1 TRP A 268 -14.503 12.738 4.584 1.00 38.22 C ANISOU 2710 CD1 TRP A 268 5557 4647 4316 -311 71 784 C ATOM 2711 CD2 TRP A 268 -14.195 10.530 4.392 1.00 37.50 C ANISOU 2711 CD2 TRP A 268 5422 4703 4123 -281 221 690 C ATOM 2712 NE1 TRP A 268 -13.150 12.498 4.618 1.00 36.99 N ANISOU 2712 NE1 TRP A 268 5351 4543 4159 -373 256 772 N ATOM 2713 CE2 TRP A 268 -12.935 11.149 4.502 1.00 37.77 C ANISOU 2713 CE2 TRP A 268 5417 4732 4202 -348 353 714 C ATOM 2714 CE3 TRP A 268 -14.253 9.138 4.260 1.00 37.10 C ANISOU 2714 CE3 TRP A 268 5361 4723 4013 -250 279 630 C ATOM 2715 CZ2 TRP A 268 -11.743 10.427 4.483 1.00 41.73 C ANISOU 2715 CZ2 TRP A 268 5847 5303 4705 -375 544 680 C ATOM 2716 CZ3 TRP A 268 -13.069 8.422 4.243 1.00 41.11 C ANISOU 2716 CZ3 TRP A 268 5818 5292 4512 -271 469 592 C ATOM 2717 CH2 TRP A 268 -11.831 9.068 4.354 1.00 42.03 C ANISOU 2717 CH2 TRP A 268 5874 5406 4688 -329 601 618 C ATOM 2718 N LEU A 269 -15.719 9.976 7.164 1.00 34.09 N ANISOU 2718 N LEU A 269 4648 4332 3972 -80 46 543 N ATOM 2719 CA LEU A 269 -15.103 8.820 7.808 1.00 32.67 C ANISOU 2719 CA LEU A 269 4362 4242 3809 -58 152 476 C ATOM 2720 C LEU A 269 -15.974 8.326 8.955 1.00 33.27 C ANISOU 2720 C LEU A 269 4323 4350 3970 23 87 415 C ATOM 2721 O LEU A 269 -16.071 7.116 9.193 1.00 30.00 O ANISOU 2721 O LEU A 269 3865 3994 3540 51 121 373 O ATOM 2722 CB LEU A 269 -13.698 9.167 8.298 1.00 30.37 C ANISOU 2722 CB LEU A 269 3994 3969 3577 -99 265 469 C ATOM 2723 CG LEU A 269 -12.926 8.026 8.964 1.00 33.84 C ANISOU 2723 CG LEU A 269 4316 4488 4055 -73 360 411 C ATOM 2724 CD1 LEU A 269 -12.739 6.861 7.998 1.00 37.45 C ANISOU 2724 CD1 LEU A 269 4840 4979 4411 -80 452 405 C ATOM 2725 CD2 LEU A 269 -11.583 8.518 9.475 1.00 31.03 C ANISOU 2725 CD2 LEU A 269 3863 4137 3788 -118 434 415 C ATOM 2726 N MET A 270 -16.600 9.255 9.680 1.00 30.50 N ANISOU 2726 N MET A 270 3927 3952 3707 62 5 409 N ATOM 2727 CA MET A 270 -17.587 8.883 10.687 1.00 26.71 C ANISOU 2727 CA MET A 270 3353 3494 3301 137 -40 355 C ATOM 2728 C MET A 270 -18.672 8.007 10.080 1.00 28.39 C ANISOU 2728 C MET A 270 3583 3721 3483 158 -102 364 C ATOM 2729 O MET A 270 -19.056 6.989 10.665 1.00 31.85 O ANISOU 2729 O MET A 270 3949 4213 3939 188 -81 321 O ATOM 2730 CB MET A 270 -18.179 10.119 11.366 1.00 29.08 C ANISOU 2730 CB MET A 270 3625 3724 3700 180 -106 345 C ATOM 2731 CG MET A 270 -17.149 10.968 12.087 1.00 33.64 C ANISOU 2731 CG MET A 270 4193 4278 4312 152 -63 326 C ATOM 2732 SD MET A 270 -16.266 9.967 13.308 1.00 35.32 S ANISOU 2732 SD MET A 270 4313 4586 4522 153 26 259 S ATOM 2733 CE MET A 270 -17.614 9.381 14.334 1.00 34.56 C ANISOU 2733 CE MET A 270 4151 4518 4462 240 9 198 C ATOM 2734 N TYR A 271 -19.190 8.381 8.904 1.00 28.87 N ANISOU 2734 N TYR A 271 3747 3725 3496 133 -193 425 N ATOM 2735 CA TYR A 271 -20.322 7.617 8.409 1.00 31.16 C ANISOU 2735 CA TYR A 271 4045 4019 3778 148 -287 432 C ATOM 2736 C TYR A 271 -19.867 6.266 7.884 1.00 30.64 C ANISOU 2736 C TYR A 271 4034 4008 3599 108 -222 412 C ATOM 2737 O TYR A 271 -20.610 5.284 7.977 1.00 33.21 O ANISOU 2737 O TYR A 271 4320 4359 3939 123 -261 388 O ATOM 2738 CB TYR A 271 -20.962 8.289 7.189 1.00 35.98 C ANISOU 2738 CB TYR A 271 4776 4547 4348 122 -431 510 C ATOM 2739 CG TYR A 271 -21.839 9.510 7.316 1.00 39.96 C ANISOU 2739 CG TYR A 271 5245 4963 4974 172 -558 548 C ATOM 2740 CD1 TYR A 271 -23.130 9.432 7.807 1.00 38.69 C ANISOU 2740 CD1 TYR A 271 4955 4789 4956 243 -650 531 C ATOM 2741 CD2 TYR A 271 -21.437 10.709 6.745 1.00 48.51 C ANISOU 2741 CD2 TYR A 271 6439 5964 6029 142 -597 612 C ATOM 2742 CE1 TYR A 271 -23.950 10.553 7.847 1.00 40.25 C ANISOU 2742 CE1 TYR A 271 5113 4893 5286 301 -766 565 C ATOM 2743 CE2 TYR A 271 -22.247 11.821 6.764 1.00 51.77 C ANISOU 2743 CE2 TYR A 271 6833 6277 6559 193 -727 652 C ATOM 2744 CZ TYR A 271 -23.498 11.745 7.318 1.00 47.43 C ANISOU 2744 CZ TYR A 271 6140 5714 6167 281 -811 625 C ATOM 2745 OH TYR A 271 -24.290 12.871 7.345 1.00 46.41 O ANISOU 2745 OH TYR A 271 5979 5474 6180 347 -933 661 O ATOM 2746 N LEU A 272 -18.652 6.196 7.335 1.00 29.58 N ANISOU 2746 N LEU A 272 3988 3887 3364 57 -114 420 N ATOM 2747 CA LEU A 272 -18.073 4.909 6.965 1.00 32.01 C ANISOU 2747 CA LEU A 272 4338 4241 3583 35 -19 385 C ATOM 2748 C LEU A 272 -17.841 4.004 8.169 1.00 30.96 C ANISOU 2748 C LEU A 272 4065 4170 3530 82 51 323 C ATOM 2749 O LEU A 272 -18.122 2.801 8.110 1.00 32.83 O ANISOU 2749 O LEU A 272 4306 4428 3741 89 56 291 O ATOM 2750 CB LEU A 272 -16.770 5.137 6.199 1.00 37.46 C ANISOU 2750 CB LEU A 272 5128 4929 4177 -21 111 405 C ATOM 2751 CG LEU A 272 -16.047 3.894 5.682 1.00 49.69 C ANISOU 2751 CG LEU A 272 6735 6511 5636 -36 239 364 C ATOM 2752 CD1 LEU A 272 -16.924 3.148 4.686 1.00 54.76 C ANISOU 2752 CD1 LEU A 272 7526 7123 6156 -59 152 362 C ATOM 2753 CD2 LEU A 272 -14.720 4.280 5.045 1.00 49.57 C ANISOU 2753 CD2 LEU A 272 6782 6494 5560 -87 399 384 C ATOM 2754 N ALA A 273 -17.328 4.561 9.272 1.00 27.15 N ANISOU 2754 N ALA A 273 3473 3706 3136 108 95 307 N ATOM 2755 CA ALA A 273 -17.067 3.734 10.448 1.00 26.80 C ANISOU 2755 CA ALA A 273 3319 3714 3150 146 147 258 C ATOM 2756 C ALA A 273 -18.348 3.273 11.127 1.00 26.78 C ANISOU 2756 C ALA A 273 3253 3719 3202 184 77 238 C ATOM 2757 O ALA A 273 -18.402 2.156 11.654 1.00 29.91 O ANISOU 2757 O ALA A 273 3609 4149 3605 199 107 209 O ATOM 2758 CB ALA A 273 -16.189 4.495 11.439 1.00 25.30 C ANISOU 2758 CB ALA A 273 3052 3533 3026 152 189 248 C ATOM 2759 N ILE A 274 -19.381 4.114 11.125 1.00 26.79 N ANISOU 2759 N ILE A 274 3240 3685 3255 201 -12 257 N ATOM 2760 CA ILE A 274 -20.668 3.719 11.688 1.00 28.70 C ANISOU 2760 CA ILE A 274 3401 3932 3573 234 -64 243 C ATOM 2761 C ILE A 274 -21.307 2.636 10.830 1.00 30.10 C ANISOU 2761 C ILE A 274 3622 4107 3710 205 -122 254 C ATOM 2762 O ILE A 274 -21.778 1.610 11.334 1.00 29.78 O ANISOU 2762 O ILE A 274 3526 4093 3698 209 -109 232 O ATOM 2763 CB ILE A 274 -21.584 4.947 11.841 1.00 27.66 C ANISOU 2763 CB ILE A 274 3226 3750 3534 271 -139 259 C ATOM 2764 CG1 ILE A 274 -21.044 5.866 12.939 1.00 26.24 C ANISOU 2764 CG1 ILE A 274 3006 3566 3396 301 -76 227 C ATOM 2765 CG2 ILE A 274 -23.009 4.518 12.151 1.00 27.98 C ANISOU 2765 CG2 ILE A 274 3168 3790 3673 300 -192 253 C ATOM 2766 CD1 ILE A 274 -21.590 7.274 12.884 1.00 27.15 C ANISOU 2766 CD1 ILE A 274 3118 3607 3590 336 -139 242 C ATOM 2767 N AVAL A 275 -21.323 2.855 9.514 1.00 28.71 N ANISOU 2767 N AVAL A 275 3563 3890 3456 167 -191 290 N ATOM 2768 CA AVAL A 275 -21.920 1.897 8.589 1.00 30.36 C ANISOU 2768 CA AVAL A 275 3846 4082 3606 127 -269 297 C ATOM 2769 C AVAL A 275 -21.175 0.567 8.637 1.00 28.82 C ANISOU 2769 C AVAL A 275 3690 3919 3341 112 -169 254 C ATOM 2770 O AVAL A 275 -21.789 -0.506 8.586 1.00 31.80 O ANISOU 2770 O AVAL A 275 4064 4293 3725 96 -208 237 O ATOM 2771 CB AVAL A 275 -21.949 2.498 7.170 1.00 35.62 C ANISOU 2771 CB AVAL A 275 4672 4693 4170 82 -362 347 C ATOM 2772 CG1AVAL A 275 -22.019 1.414 6.113 1.00 39.83 C ANISOU 2772 CG1AVAL A 275 5350 5208 4576 27 -400 337 C ATOM 2773 CG2AVAL A 275 -23.123 3.462 7.033 1.00 35.20 C ANISOU 2773 CG2AVAL A 275 4571 4587 4216 102 -522 397 C ATOM 2774 N LEU A 276 -19.844 0.615 8.749 1.00 27.43 N ANISOU 2774 N LEU A 276 3541 3767 3117 117 -41 237 N ATOM 2775 CA LEU A 276 -19.060 -0.615 8.835 1.00 27.80 C ANISOU 2775 CA LEU A 276 3607 3832 3123 120 58 196 C ATOM 2776 C LEU A 276 -19.434 -1.431 10.066 1.00 27.80 C ANISOU 2776 C LEU A 276 3491 3860 3212 151 67 172 C ATOM 2777 O LEU A 276 -19.577 -2.657 9.984 1.00 25.73 O ANISOU 2777 O LEU A 276 3256 3587 2932 142 72 149 O ATOM 2778 CB LEU A 276 -17.567 -0.294 8.854 1.00 25.47 C ANISOU 2778 CB LEU A 276 3317 3556 2806 128 190 188 C ATOM 2779 CG LEU A 276 -16.659 -1.517 9.002 1.00 26.11 C ANISOU 2779 CG LEU A 276 3394 3648 2880 149 298 146 C ATOM 2780 CD1 LEU A 276 -16.845 -2.490 7.845 1.00 23.98 C ANISOU 2780 CD1 LEU A 276 3270 3338 2504 123 304 120 C ATOM 2781 CD2 LEU A 276 -15.201 -1.100 9.131 1.00 29.26 C ANISOU 2781 CD2 LEU A 276 3749 4067 3304 161 420 146 C ATOM 2782 N SER A 277 -19.590 -0.773 11.218 1.00 24.11 N ANISOU 2782 N SER A 277 2911 3421 2830 182 73 178 N ATOM 2783 CA SER A 277 -19.969 -1.498 12.426 1.00 24.09 C ANISOU 2783 CA SER A 277 2820 3443 2890 202 93 163 C ATOM 2784 C SER A 277 -21.327 -2.166 12.259 1.00 23.81 C ANISOU 2784 C SER A 277 2766 3389 2890 178 16 170 C ATOM 2785 O SER A 277 -21.557 -3.263 12.779 1.00 28.98 O ANISOU 2785 O SER A 277 3399 4048 3565 170 36 161 O ATOM 2786 CB SER A 277 -19.983 -0.550 13.627 1.00 21.01 C ANISOU 2786 CB SER A 277 2344 3078 2560 234 115 161 C ATOM 2787 OG SER A 277 -21.123 0.295 13.595 1.00 25.70 O ANISOU 2787 OG SER A 277 2896 3655 3214 242 54 174 O ATOM 2788 N HIS A 278 -22.239 -1.521 11.527 1.00 24.42 N ANISOU 2788 N HIS A 278 2848 3439 2990 162 -82 193 N ATOM 2789 CA HIS A 278 -23.557 -2.104 11.303 1.00 24.40 C ANISOU 2789 CA HIS A 278 2807 3415 3049 131 -176 206 C ATOM 2790 C HIS A 278 -23.496 -3.282 10.339 1.00 28.53 C ANISOU 2790 C HIS A 278 3446 3903 3490 80 -220 194 C ATOM 2791 O HIS A 278 -24.295 -4.216 10.458 1.00 29.46 O ANISOU 2791 O HIS A 278 3532 4005 3658 45 -267 194 O ATOM 2792 CB HIS A 278 -24.512 -1.034 10.775 1.00 27.60 C ANISOU 2792 CB HIS A 278 3176 3791 3521 135 -293 240 C ATOM 2793 CG HIS A 278 -24.826 0.035 11.773 1.00 30.94 C ANISOU 2793 CG HIS A 278 3476 4231 4049 191 -250 241 C ATOM 2794 ND1 HIS A 278 -25.357 1.256 11.415 1.00 32.86 N ANISOU 2794 ND1 HIS A 278 3691 4437 4357 219 -331 268 N ATOM 2795 CD2 HIS A 278 -24.667 0.074 13.117 1.00 32.62 C ANISOU 2795 CD2 HIS A 278 3607 4483 4305 227 -135 214 C ATOM 2796 CE1 HIS A 278 -25.521 1.996 12.497 1.00 33.78 C ANISOU 2796 CE1 HIS A 278 3708 4567 4561 275 -256 249 C ATOM 2797 NE2 HIS A 278 -25.109 1.303 13.543 1.00 32.31 N ANISOU 2797 NE2 HIS A 278 3495 4429 4351 276 -135 214 N ATOM 2798 N ATHR A 279 -22.563 -3.253 9.383 0.50 28.14 N ANISOU 2798 N ATHR A 279 3539 3835 3317 70 -198 182 N ATOM 2799 N BTHR A 279 -22.563 -3.255 9.382 0.50 28.12 N ANISOU 2799 N BTHR A 279 3537 3833 3315 70 -198 182 N ATOM 2800 CA ATHR A 279 -22.441 -4.339 8.417 0.50 30.13 C ANISOU 2800 CA ATHR A 279 3934 4043 3472 26 -223 155 C ATOM 2801 CA BTHR A 279 -22.443 -4.346 8.419 0.50 30.13 C ANISOU 2801 CA BTHR A 279 3934 4043 3472 26 -223 155 C ATOM 2802 C ATHR A 279 -22.061 -5.657 9.082 0.50 29.26 C ANISOU 2802 C ATHR A 279 3807 3932 3380 35 -142 120 C ATOM 2803 C BTHR A 279 -22.052 -5.659 9.079 0.50 29.27 C ANISOU 2803 C BTHR A 279 3809 3932 3380 35 -141 120 C ATOM 2804 O ATHR A 279 -22.327 -6.724 8.517 0.50 30.81 O ANISOU 2804 O ATHR A 279 4095 4076 3535 -5 -185 95 O ATOM 2805 O BTHR A 279 -22.275 -6.723 8.492 0.50 30.89 O ANISOU 2805 O BTHR A 279 4110 4087 3540 -4 -181 94 O ATOM 2806 CB ATHR A 279 -21.416 -3.957 7.340 0.50 30.68 C ANISOU 2806 CB ATHR A 279 4162 4095 3399 20 -170 144 C ATOM 2807 CB BTHR A 279 -21.416 -4.002 7.338 0.50 30.70 C ANISOU 2807 CB BTHR A 279 4166 4097 3401 19 -169 143 C ATOM 2808 OG1ATHR A 279 -21.765 -2.684 6.779 0.50 29.99 O ANISOU 2808 OG1ATHR A 279 4100 4000 3294 7 -253 190 O ATOM 2809 OG1BTHR A 279 -20.118 -3.874 7.931 0.50 27.57 O ANISOU 2809 OG1BTHR A 279 3729 3738 3008 68 -12 125 O ATOM 2810 CG2ATHR A 279 -21.383 -4.986 6.217 0.50 29.80 C ANISOU 2810 CG2ATHR A 279 4234 3926 3163 -28 -195 106 C ATOM 2811 CG2BTHR A 279 -21.781 -2.706 6.642 0.50 30.05 C ANISOU 2811 CG2BTHR A 279 4127 4003 3289 2 -260 190 C ATOM 2812 N ASN A 280 -21.467 -5.611 10.279 1.00 28.12 N ANISOU 2812 N ASN A 280 3560 3831 3293 84 -41 120 N ATOM 2813 CA ASN A 280 -21.140 -6.843 10.990 1.00 28.84 C ANISOU 2813 CA ASN A 280 3638 3911 3409 95 17 102 C ATOM 2814 C ASN A 280 -22.383 -7.679 11.262 1.00 27.41 C ANISOU 2814 C ASN A 280 3420 3703 3293 44 -60 115 C ATOM 2815 O ASN A 280 -22.298 -8.909 11.351 1.00 28.20 O ANISOU 2815 O ASN A 280 3567 3759 3390 27 -49 99 O ATOM 2816 CB ASN A 280 -20.420 -6.527 12.299 1.00 30.58 C ANISOU 2816 CB ASN A 280 3761 4180 3677 147 104 112 C ATOM 2817 CG ASN A 280 -19.975 -7.778 13.032 1.00 35.67 C ANISOU 2817 CG ASN A 280 4407 4804 4342 162 150 106 C ATOM 2818 OD1 ASN A 280 -19.071 -8.483 12.586 1.00 43.68 O ANISOU 2818 OD1 ASN A 280 5492 5782 5323 186 195 78 O ATOM 2819 ND2 ASN A 280 -20.608 -8.058 14.167 1.00 32.71 N ANISOU 2819 ND2 ASN A 280 3960 4445 4023 150 146 134 N ATOM 2820 N SER A 281 -23.542 -7.035 11.401 1.00 23.29 N ANISOU 2820 N SER A 281 2805 3198 2846 19 -137 146 N ATOM 2821 CA SER A 281 -24.777 -7.773 11.630 1.00 30.68 C ANISOU 2821 CA SER A 281 3677 4108 3871 -40 -207 166 C ATOM 2822 C SER A 281 -25.283 -8.475 10.376 1.00 32.07 C ANISOU 2822 C SER A 281 3965 4213 4007 -109 -334 151 C ATOM 2823 O SER A 281 -26.290 -9.188 10.453 1.00 30.95 O ANISOU 2823 O SER A 281 3775 4038 3948 -173 -411 167 O ATOM 2824 CB SER A 281 -25.854 -6.827 12.165 1.00 26.89 C ANISOU 2824 CB SER A 281 3038 3665 3513 -36 -237 201 C ATOM 2825 OG SER A 281 -25.516 -6.353 13.460 1.00 31.87 O ANISOU 2825 OG SER A 281 3585 4351 4173 15 -114 205 O ATOM 2826 N VAL A 282 -24.622 -8.286 9.234 1.00 37.92 N ANISOU 2826 N VAL A 282 4860 4926 4620 -105 -357 122 N ATOM 2827 CA VAL A 282 -25.000 -8.940 7.985 1.00 30.63 C ANISOU 2827 CA VAL A 282 4093 3928 3619 -174 -479 98 C ATOM 2828 C VAL A 282 -24.177 -10.206 7.765 1.00 33.84 C ANISOU 2828 C VAL A 282 4640 4276 3940 -172 -402 40 C ATOM 2829 O VAL A 282 -24.648 -11.165 7.143 1.00 36.01 O ANISOU 2829 O VAL A 282 5024 4473 4186 -238 -493 13 O ATOM 2830 CB VAL A 282 -24.845 -7.965 6.799 1.00 28.08 C ANISOU 2830 CB VAL A 282 3888 3596 3183 -179 -549 102 C ATOM 2831 CG1 VAL A 282 -25.174 -8.649 5.477 1.00 30.08 C ANISOU 2831 CG1 VAL A 282 4347 3765 3318 -257 -680 72 C ATOM 2832 CG2 VAL A 282 -25.722 -6.736 7.002 1.00 27.56 C ANISOU 2832 CG2 VAL A 282 3681 3567 3224 -172 -644 163 C ATOM 2833 N VAL A 283 -22.954 -10.234 8.300 1.00 30.06 N ANISOU 2833 N VAL A 283 4157 3827 3438 -96 -243 20 N ATOM 2834 CA VAL A 283 -21.944 -11.134 7.745 1.00 32.09 C ANISOU 2834 CA VAL A 283 4569 4023 3600 -71 -157 -43 C ATOM 2835 C VAL A 283 -22.044 -12.557 8.295 1.00 32.51 C ANISOU 2835 C VAL A 283 4630 4011 3712 -82 -149 -61 C ATOM 2836 O VAL A 283 -21.727 -13.514 7.579 1.00 34.33 O ANISOU 2836 O VAL A 283 5020 4152 3873 -92 -140 -121 O ATOM 2837 CB VAL A 283 -20.534 -10.555 7.968 1.00 35.46 C ANISOU 2837 CB VAL A 283 4974 4499 4000 16 2 -55 C ATOM 2838 CG1 VAL A 283 -20.406 -9.200 7.293 1.00 40.97 C ANISOU 2838 CG1 VAL A 283 5695 5242 4628 12 -5 -36 C ATOM 2839 CG2 VAL A 283 -20.219 -10.447 9.452 1.00 34.52 C ANISOU 2839 CG2 VAL A 283 4683 4436 3996 68 64 -16 C ATOM 2840 N ASN A 284 -22.458 -12.736 9.554 1.00 30.95 N ANISOU 2840 N ASN A 284 4281 3844 3633 -82 -143 -11 N ATOM 2841 CA ASN A 284 -22.458 -14.079 10.138 1.00 39.09 C ANISOU 2841 CA ASN A 284 5331 4804 4716 -94 -129 -14 C ATOM 2842 C ASN A 284 -23.268 -15.101 9.344 1.00 39.86 C ANISOU 2842 C ASN A 284 5551 4796 4799 -184 -244 -45 C ATOM 2843 O ASN A 284 -22.765 -16.220 9.142 1.00 39.20 O ANISOU 2843 O ASN A 284 5588 4616 4690 -172 -213 -92 O ATOM 2844 CB ASN A 284 -22.926 -14.016 11.597 1.00 41.72 C ANISOU 2844 CB ASN A 284 5501 5191 5160 -100 -107 56 C ATOM 2845 CG ASN A 284 -21.994 -13.202 12.473 1.00 44.81 C ANISOU 2845 CG ASN A 284 5806 5665 5555 -14 -4 77 C ATOM 2846 OD1 ASN A 284 -20.903 -12.817 12.049 1.00 38.83 O ANISOU 2846 OD1 ASN A 284 5091 4920 4741 53 58 43 O ATOM 2847 ND2 ASN A 284 -22.415 -12.943 13.703 1.00 46.56 N ANISOU 2847 ND2 ASN A 284 5909 5940 5841 -21 19 132 N ATOM 2848 N PRO A 285 -24.503 -14.821 8.896 1.00 31.25 N ANISOU 2848 N PRO A 285 4432 3705 3735 -276 -386 -22 N ATOM 2849 CA PRO A 285 -25.219 -15.821 8.082 1.00 35.81 C ANISOU 2849 CA PRO A 285 5141 4170 4296 -374 -519 -56 C ATOM 2850 C PRO A 285 -24.431 -16.316 6.880 1.00 38.80 C ANISOU 2850 C PRO A 285 5765 4460 4516 -355 -503 -149 C ATOM 2851 O PRO A 285 -24.556 -17.488 6.501 1.00 41.74 O ANISOU 2851 O PRO A 285 6277 4714 4868 -403 -549 -198 O ATOM 2852 CB PRO A 285 -26.488 -15.072 7.656 1.00 36.28 C ANISOU 2852 CB PRO A 285 5118 4262 4407 -457 -684 -13 C ATOM 2853 CG PRO A 285 -26.719 -14.102 8.757 1.00 34.93 C ANISOU 2853 CG PRO A 285 4719 4205 4347 -412 -613 56 C ATOM 2854 CD PRO A 285 -25.350 -13.642 9.162 1.00 31.55 C ANISOU 2854 CD PRO A 285 4310 3833 3844 -296 -444 37 C ATOM 2855 N PHE A 286 -23.617 -15.452 6.269 1.00 37.53 N ANISOU 2855 N PHE A 286 5670 4349 4240 -290 -426 -178 N ATOM 2856 CA PHE A 286 -22.791 -15.875 5.143 1.00 40.79 C ANISOU 2856 CA PHE A 286 6321 4684 4493 -266 -366 -271 C ATOM 2857 C PHE A 286 -21.661 -16.794 5.587 1.00 40.01 C ANISOU 2857 C PHE A 286 6253 4530 4418 -174 -201 -320 C ATOM 2858 O PHE A 286 -21.334 -17.762 4.890 1.00 39.36 O ANISOU 2858 O PHE A 286 6365 4330 4260 -174 -177 -405 O ATOM 2859 CB PHE A 286 -22.248 -14.651 4.407 1.00 47.26 C ANISOU 2859 CB PHE A 286 7193 5573 5191 -232 -313 -274 C ATOM 2860 CG PHE A 286 -23.282 -13.947 3.583 1.00 52.19 C ANISOU 2860 CG PHE A 286 7874 6204 5751 -325 -502 -244 C ATOM 2861 CD1 PHE A 286 -24.020 -12.903 4.113 1.00 51.02 C ANISOU 2861 CD1 PHE A 286 7531 6145 5710 -338 -588 -156 C ATOM 2862 CD2 PHE A 286 -23.526 -14.343 2.277 1.00 53.37 C ANISOU 2862 CD2 PHE A 286 8282 6260 5735 -398 -602 -304 C ATOM 2863 CE1 PHE A 286 -24.981 -12.263 3.355 1.00 51.68 C ANISOU 2863 CE1 PHE A 286 7653 6223 5759 -414 -782 -120 C ATOM 2864 CE2 PHE A 286 -24.483 -13.706 1.512 1.00 56.29 C ANISOU 2864 CE2 PHE A 286 8712 6627 6048 -486 -809 -265 C ATOM 2865 CZ PHE A 286 -25.213 -12.666 2.052 1.00 53.77 C ANISOU 2865 CZ PHE A 286 8175 6396 5861 -491 -905 -169 C ATOM 2866 N ILE A 287 -21.049 -16.506 6.738 1.00 39.55 N ANISOU 2866 N ILE A 287 6014 4546 4466 -92 -93 -270 N ATOM 2867 CA ILE A 287 -19.981 -17.365 7.243 1.00 42.22 C ANISOU 2867 CA ILE A 287 6358 4828 4855 2 37 -301 C ATOM 2868 C ILE A 287 -20.516 -18.759 7.543 1.00 41.81 C ANISOU 2868 C ILE A 287 6368 4652 4867 -45 -35 -310 C ATOM 2869 O ILE A 287 -19.872 -19.768 7.227 1.00 46.59 O ANISOU 2869 O ILE A 287 7104 5140 5459 4 28 -381 O ATOM 2870 CB ILE A 287 -19.317 -16.732 8.478 1.00 42.11 C ANISOU 2870 CB ILE A 287 6140 4917 4942 83 123 -232 C ATOM 2871 CG1 ILE A 287 -18.856 -15.308 8.166 1.00 40.25 C ANISOU 2871 CG1 ILE A 287 5847 4793 4653 113 181 -221 C ATOM 2872 CG2 ILE A 287 -18.148 -17.587 8.949 1.00 38.93 C ANISOU 2872 CG2 ILE A 287 5737 4448 4606 187 235 -257 C ATOM 2873 CD1 ILE A 287 -17.825 -15.234 7.065 1.00 44.62 C ANISOU 2873 CD1 ILE A 287 6533 5315 5104 166 305 -299 C ATOM 2874 N TYR A 288 -21.700 -18.841 8.155 1.00 39.85 N ANISOU 2874 N TYR A 288 6024 4420 4698 -141 -160 -239 N ATOM 2875 CA TYR A 288 -22.291 -20.145 8.436 1.00 43.70 C ANISOU 2875 CA TYR A 288 6567 4785 5253 -208 -236 -236 C ATOM 2876 C TYR A 288 -22.609 -20.884 7.144 1.00 46.60 C ANISOU 2876 C TYR A 288 7165 5019 5523 -275 -321 -330 C ATOM 2877 O TYR A 288 -22.389 -22.097 7.041 1.00 46.98 O ANISOU 2877 O TYR A 288 7344 4923 5583 -272 -316 -381 O ATOM 2878 CB TYR A 288 -23.563 -19.984 9.270 1.00 41.53 C ANISOU 2878 CB TYR A 288 6130 4562 5088 -313 -337 -139 C ATOM 2879 CG TYR A 288 -23.373 -19.239 10.569 1.00 42.45 C ANISOU 2879 CG TYR A 288 6047 4804 5279 -260 -254 -53 C ATOM 2880 CD1 TYR A 288 -22.301 -19.515 11.405 1.00 46.10 C ANISOU 2880 CD1 TYR A 288 6486 5264 5764 -159 -142 -37 C ATOM 2881 CD2 TYR A 288 -24.274 -18.257 10.960 1.00 40.49 C ANISOU 2881 CD2 TYR A 288 5639 4666 5079 -311 -296 10 C ATOM 2882 CE1 TYR A 288 -22.135 -18.839 12.601 1.00 46.90 C ANISOU 2882 CE1 TYR A 288 6434 5472 5912 -121 -85 38 C ATOM 2883 CE2 TYR A 288 -24.112 -17.570 12.146 1.00 37.51 C ANISOU 2883 CE2 TYR A 288 5107 4394 4752 -265 -213 76 C ATOM 2884 CZ TYR A 288 -23.044 -17.866 12.965 1.00 40.26 C ANISOU 2884 CZ TYR A 288 5459 4740 5099 -176 -112 89 C ATOM 2885 OH TYR A 288 -22.879 -17.171 14.142 1.00 35.44 O ANISOU 2885 OH TYR A 288 4722 4227 4516 -140 -46 150 O ATOM 2886 N ALA A 289 -23.134 -20.166 6.148 1.00 46.64 N ANISOU 2886 N ALA A 289 7237 5059 5425 -337 -411 -354 N ATOM 2887 CA ALA A 289 -23.504 -20.797 4.886 1.00 45.14 C ANISOU 2887 CA ALA A 289 7294 4742 5116 -417 -518 -443 C ATOM 2888 C ALA A 289 -22.281 -21.335 4.153 1.00 48.53 C ANISOU 2888 C ALA A 289 7938 5079 5423 -319 -366 -561 C ATOM 2889 O ALA A 289 -22.316 -22.442 3.606 1.00 50.01 O ANISOU 2889 O ALA A 289 8328 5109 5565 -350 -398 -646 O ATOM 2890 CB ALA A 289 -24.265 -19.807 4.005 1.00 36.85 C ANISOU 2890 CB ALA A 289 6275 3753 3972 -498 -659 -429 C ATOM 2891 N TYR A 290 -21.190 -20.568 4.134 1.00 47.38 N ANISOU 2891 N TYR A 290 7747 5021 5233 -201 -191 -572 N ATOM 2892 CA TYR A 290 -20.006 -20.974 3.388 1.00 54.69 C ANISOU 2892 CA TYR A 290 8854 5870 6056 -103 -16 -685 C ATOM 2893 C TYR A 290 -19.152 -21.996 4.126 1.00 55.10 C ANISOU 2893 C TYR A 290 8864 5833 6237 8 107 -708 C ATOM 2894 O TYR A 290 -18.384 -22.719 3.481 1.00 51.49 O ANISOU 2894 O TYR A 290 8582 5257 5723 78 227 -819 O ATOM 2895 CB TYR A 290 -19.146 -19.747 3.071 1.00 56.41 C ANISOU 2895 CB TYR A 290 9021 6213 6199 -28 132 -680 C ATOM 2896 CG TYR A 290 -19.588 -18.972 1.852 1.00 68.82 C ANISOU 2896 CG TYR A 290 10763 7811 7574 -112 62 -704 C ATOM 2897 CD1 TYR A 290 -19.371 -19.466 0.572 1.00 78.21 C ANISOU 2897 CD1 TYR A 290 12257 8889 8572 -135 100 -822 C ATOM 2898 CD2 TYR A 290 -20.223 -17.744 1.981 1.00 73.34 C ANISOU 2898 CD2 TYR A 290 11207 8511 8148 -168 -46 -609 C ATOM 2899 CE1 TYR A 290 -19.773 -18.757 -0.544 1.00 84.36 C ANISOU 2899 CE1 TYR A 290 13220 9685 9148 -220 21 -835 C ATOM 2900 CE2 TYR A 290 -20.630 -17.029 0.873 1.00 79.33 C ANISOU 2900 CE2 TYR A 290 12130 9283 8731 -244 -132 -617 C ATOM 2901 CZ TYR A 290 -20.402 -17.539 -0.387 1.00 85.83 C ANISOU 2901 CZ TYR A 290 13267 9996 9348 -274 -105 -725 C ATOM 2902 OH TYR A 290 -20.808 -16.828 -1.493 1.00 90.05 O ANISOU 2902 OH TYR A 290 13993 10538 9685 -359 -205 -725 O ATOM 2903 N ARG A 291 -19.266 -22.080 5.452 1.00 51.44 N ANISOU 2903 N ARG A 291 8186 5417 5942 27 81 -607 N ATOM 2904 CA ARG A 291 -18.343 -22.879 6.244 1.00 50.25 C ANISOU 2904 CA ARG A 291 7976 5196 5920 145 187 -607 C ATOM 2905 C ARG A 291 -18.977 -24.053 6.978 1.00 48.15 C ANISOU 2905 C ARG A 291 7719 4810 5765 90 76 -566 C ATOM 2906 O ARG A 291 -18.240 -24.934 7.436 1.00 47.09 O ANISOU 2906 O ARG A 291 7597 4571 5726 185 144 -580 O ATOM 2907 CB ARG A 291 -17.608 -21.992 7.260 1.00 48.42 C ANISOU 2907 CB ARG A 291 7503 5110 5785 236 274 -519 C ATOM 2908 CG ARG A 291 -16.629 -21.028 6.614 1.00 44.25 C ANISOU 2908 CG ARG A 291 6960 4669 5185 316 425 -563 C ATOM 2909 CD ARG A 291 -15.553 -20.585 7.585 1.00 46.31 C ANISOU 2909 CD ARG A 291 7011 5009 5574 433 526 -504 C ATOM 2910 NE ARG A 291 -14.930 -21.723 8.253 1.00 52.07 N ANISOU 2910 NE ARG A 291 7721 5622 6442 525 553 -505 N ATOM 2911 CZ ARG A 291 -13.747 -22.227 7.919 1.00 52.63 C ANISOU 2911 CZ ARG A 291 7816 5608 6571 655 700 -578 C ATOM 2912 NH1 ARG A 291 -13.057 -21.695 6.920 1.00 50.85 N ANISOU 2912 NH1 ARG A 291 7640 5412 6268 701 854 -659 N ATOM 2913 NH2 ARG A 291 -13.255 -23.265 8.581 1.00 55.86 N ANISOU 2913 NH2 ARG A 291 8201 5899 7123 741 697 -567 N ATOM 2914 N ILE A 292 -20.300 -24.104 7.109 1.00 46.88 N ANISOU 2914 N ILE A 292 7547 4656 5611 -60 -91 -512 N ATOM 2915 CA ILE A 292 -20.969 -25.135 7.899 1.00 48.99 C ANISOU 2915 CA ILE A 292 7801 4821 5993 -133 -189 -452 C ATOM 2916 C ILE A 292 -22.016 -25.785 7.004 1.00 50.49 C ANISOU 2916 C ILE A 292 8169 4889 6126 -280 -342 -509 C ATOM 2917 O ILE A 292 -23.067 -25.193 6.731 1.00 46.16 O ANISOU 2917 O ILE A 292 7573 4414 5551 -403 -470 -473 O ATOM 2918 CB ILE A 292 -21.607 -24.571 9.173 1.00 50.15 C ANISOU 2918 CB ILE A 292 7715 5099 6241 -187 -232 -309 C ATOM 2919 CG1 ILE A 292 -20.616 -23.672 9.919 1.00 49.84 C ANISOU 2919 CG1 ILE A 292 7514 5198 6225 -57 -105 -261 C ATOM 2920 CG2 ILE A 292 -22.084 -25.702 10.075 1.00 47.77 C ANISOU 2920 CG2 ILE A 292 7410 4683 6056 -250 -293 -239 C ATOM 2921 CD1 ILE A 292 -21.144 -23.135 11.230 1.00 46.73 C ANISOU 2921 CD1 ILE A 292 6924 4923 5910 -99 -128 -132 C ATOM 2922 N ARG A 293 -21.718 -26.999 6.531 1.00 53.99 N ANISOU 2922 N ARG A 293 8820 5136 6557 -265 -339 -602 N ATOM 2923 CA ARG A 293 -22.601 -27.709 5.609 1.00 58.84 C ANISOU 2923 CA ARG A 293 9644 5607 7105 -404 -493 -675 C ATOM 2924 C ARG A 293 -24.022 -27.823 6.152 1.00 54.83 C ANISOU 2924 C ARG A 293 9018 5115 6701 -585 -678 -566 C ATOM 2925 O ARG A 293 -24.994 -27.640 5.409 1.00 52.17 O ANISOU 2925 O ARG A 293 8741 4771 6309 -723 -840 -584 O ATOM 2926 CB ARG A 293 -22.012 -29.086 5.297 1.00 66.29 C ANISOU 2926 CB ARG A 293 10812 6319 8056 -348 -448 -780 C ATOM 2927 CG ARG A 293 -22.699 -29.828 4.167 1.00 75.95 C ANISOU 2927 CG ARG A 293 12311 7371 9174 -475 -590 -892 C ATOM 2928 CD ARG A 293 -22.130 -31.231 4.005 1.00 85.70 C ANISOU 2928 CD ARG A 293 13761 8359 10440 -412 -540 -994 C ATOM 2929 NE ARG A 293 -20.866 -31.217 3.267 1.00 96.29 N ANISOU 2929 NE ARG A 293 15252 9658 11677 -238 -335 -1133 N ATOM 2930 CZ ARG A 293 -19.661 -31.187 3.831 1.00102.32 C ANISOU 2930 CZ ARG A 293 15900 10446 12532 -47 -140 -1125 C ATOM 2931 NH1 ARG A 293 -18.575 -31.173 3.071 1.00105.98 N ANISOU 2931 NH1 ARG A 293 16490 10867 12912 101 56 -1258 N ATOM 2932 NH2 ARG A 293 -19.538 -31.173 5.151 1.00101.76 N ANISOU 2932 NH2 ARG A 293 15589 10439 12636 -6 -139 -983 N ATOM 2933 N GLU A 294 -24.165 -28.133 7.445 1.00 52.51 N ANISOU 2933 N GLU A 294 8556 4836 6561 -590 -659 -449 N ATOM 2934 CA GLU A 294 -25.496 -28.337 8.013 1.00 52.49 C ANISOU 2934 CA GLU A 294 8433 4837 6673 -764 -801 -344 C ATOM 2935 C GLU A 294 -26.329 -27.062 7.946 1.00 49.44 C ANISOU 2935 C GLU A 294 7862 4639 6283 -834 -866 -284 C ATOM 2936 O GLU A 294 -27.545 -27.119 7.734 1.00 49.10 O ANISOU 2936 O GLU A 294 7773 4582 6300 -996 -1026 -249 O ATOM 2937 CB GLU A 294 -25.385 -28.833 9.454 1.00 57.63 C ANISOU 2937 CB GLU A 294 8955 5479 7463 -748 -735 -225 C ATOM 2938 CG GLU A 294 -26.660 -29.471 9.990 1.00 65.46 C ANISOU 2938 CG GLU A 294 9882 6407 8583 -938 -856 -130 C ATOM 2939 CD GLU A 294 -26.982 -30.796 9.328 1.00 73.25 C ANISOU 2939 CD GLU A 294 11094 7155 9584 -1038 -977 -201 C ATOM 2940 OE1 GLU A 294 -26.038 -31.557 9.026 1.00 77.04 O ANISOU 2940 OE1 GLU A 294 11766 7486 10018 -930 -921 -289 O ATOM 2941 OE2 GLU A 294 -28.179 -31.077 9.111 1.00 76.53 O ANISOU 2941 OE2 GLU A 294 11487 7523 10067 -1225 -1131 -172 O ATOM 2942 N PHE A 295 -25.694 -25.902 8.127 1.00 42.73 N ANISOU 2942 N PHE A 295 6896 3957 5382 -716 -749 -269 N ATOM 2943 CA PHE A 295 -26.402 -24.641 7.934 1.00 42.28 C ANISOU 2943 CA PHE A 295 6689 4060 5315 -763 -811 -226 C ATOM 2944 C PHE A 295 -26.727 -24.437 6.461 1.00 45.83 C ANISOU 2944 C PHE A 295 7314 4466 5634 -823 -943 -319 C ATOM 2945 O PHE A 295 -27.871 -24.137 6.101 1.00 47.84 O ANISOU 2945 O PHE A 295 7510 4739 5928 -953 -1115 -285 O ATOM 2946 CB PHE A 295 -25.573 -23.475 8.474 1.00 41.52 C ANISOU 2946 CB PHE A 295 6452 4135 5191 -623 -656 -193 C ATOM 2947 CG PHE A 295 -25.890 -23.112 9.897 1.00 43.39 C ANISOU 2947 CG PHE A 295 6455 4477 5552 -625 -597 -72 C ATOM 2948 CD1 PHE A 295 -27.121 -22.571 10.228 1.00 40.29 C ANISOU 2948 CD1 PHE A 295 5888 4166 5253 -733 -676 6 C ATOM 2949 CD2 PHE A 295 -24.956 -23.304 10.903 1.00 45.68 C ANISOU 2949 CD2 PHE A 295 6707 4782 5868 -518 -461 -36 C ATOM 2950 CE1 PHE A 295 -27.420 -22.234 11.535 1.00 40.39 C ANISOU 2950 CE1 PHE A 295 5707 4273 5365 -736 -594 107 C ATOM 2951 CE2 PHE A 295 -25.249 -22.969 12.213 1.00 46.64 C ANISOU 2951 CE2 PHE A 295 6652 4997 6073 -529 -406 72 C ATOM 2952 CZ PHE A 295 -26.482 -22.433 12.528 1.00 41.78 C ANISOU 2952 CZ PHE A 295 5879 4463 5532 -637 -459 139 C ATOM 2953 N ARG A 296 -25.715 -24.573 5.600 1.00 47.58 N ANISOU 2953 N ARG A 296 7751 4627 5700 -727 -862 -433 N ATOM 2954 CA ARG A 296 -25.893 -24.342 4.170 1.00 49.48 C ANISOU 2954 CA ARG A 296 8204 4825 5771 -778 -966 -526 C ATOM 2955 C ARG A 296 -27.017 -25.199 3.604 1.00 49.26 C ANISOU 2955 C ARG A 296 8303 4652 5762 -954 -1197 -550 C ATOM 2956 O ARG A 296 -27.828 -24.721 2.804 1.00 53.74 O ANISOU 2956 O ARG A 296 8913 5234 6271 -1060 -1381 -551 O ATOM 2957 CB ARG A 296 -24.581 -24.616 3.440 1.00 49.67 C ANISOU 2957 CB ARG A 296 8459 4778 5635 -649 -801 -654 C ATOM 2958 CG ARG A 296 -24.636 -24.425 1.937 1.00 54.92 C ANISOU 2958 CG ARG A 296 9396 5388 6082 -697 -876 -761 C ATOM 2959 CD ARG A 296 -23.239 -24.447 1.338 1.00 55.18 C ANISOU 2959 CD ARG A 296 9608 5391 5967 -550 -647 -875 C ATOM 2960 NE ARG A 296 -22.563 -25.727 1.526 1.00 52.82 N ANISOU 2960 NE ARG A 296 9427 4928 5715 -476 -537 -957 N ATOM 2961 CZ ARG A 296 -21.579 -25.927 2.398 1.00 54.40 C ANISOU 2961 CZ ARG A 296 9488 5146 6036 -328 -349 -935 C ATOM 2962 NH1 ARG A 296 -21.011 -27.120 2.498 1.00 58.26 N ANISOU 2962 NH1 ARG A 296 10095 5464 6577 -259 -270 -1010 N ATOM 2963 NH2 ARG A 296 -21.158 -24.929 3.165 1.00 53.56 N ANISOU 2963 NH2 ARG A 296 9130 5216 6003 -250 -253 -840 N ATOM 2964 N GLN A 297 -27.091 -26.465 4.020 1.00 49.56 N ANISOU 2964 N GLN A 297 8401 4539 5891 -994 -1207 -562 N ATOM 2965 CA GLN A 297 -28.134 -27.349 3.509 1.00 52.49 C ANISOU 2965 CA GLN A 297 8896 4755 6294 -1174 -1433 -586 C ATOM 2966 C GLN A 297 -29.501 -26.949 4.045 1.00 48.99 C ANISOU 2966 C GLN A 297 8189 4396 6030 -1322 -1597 -455 C ATOM 2967 O GLN A 297 -30.505 -27.026 3.327 1.00 48.39 O ANISOU 2967 O GLN A 297 8162 4263 5960 -1476 -1831 -462 O ATOM 2968 CB GLN A 297 -27.816 -28.799 3.869 1.00 58.71 C ANISOU 2968 CB GLN A 297 9816 5348 7145 -1175 -1392 -627 C ATOM 2969 CG GLN A 297 -26.621 -29.373 3.124 1.00 68.05 C ANISOU 2969 CG GLN A 297 11293 6399 8165 -1047 -1260 -781 C ATOM 2970 CD GLN A 297 -26.273 -30.778 3.577 1.00 77.68 C ANISOU 2970 CD GLN A 297 12624 7417 9476 -1027 -1215 -813 C ATOM 2971 OE1 GLN A 297 -26.649 -31.201 4.670 1.00 80.30 O ANISOU 2971 OE1 GLN A 297 12784 7739 9987 -1071 -1226 -699 O ATOM 2972 NE2 GLN A 297 -25.547 -31.508 2.737 1.00 79.05 N ANISOU 2972 NE2 GLN A 297 13095 7417 9522 -959 -1155 -969 N ATOM 2973 N THR A 298 -29.561 -26.523 5.308 1.00 47.01 N ANISOU 2973 N THR A 298 7656 4275 5931 -1277 -1477 -336 N ATOM 2974 CA THR A 298 -30.830 -26.087 5.878 1.00 47.96 C ANISOU 2974 CA THR A 298 7503 4484 6235 -1402 -1588 -214 C ATOM 2975 C THR A 298 -31.280 -24.772 5.253 1.00 47.02 C ANISOU 2975 C THR A 298 7292 4500 6074 -1403 -1687 -199 C ATOM 2976 O THR A 298 -32.472 -24.584 4.983 1.00 47.36 O ANISOU 2976 O THR A 298 7221 4544 6228 -1542 -1888 -150 O ATOM 2977 CB THR A 298 -30.712 -25.952 7.396 1.00 48.04 C ANISOU 2977 CB THR A 298 7271 4594 6387 -1346 -1407 -101 C ATOM 2978 OG1 THR A 298 -30.148 -27.153 7.940 1.00 48.99 O ANISOU 2978 OG1 THR A 298 7508 4580 6527 -1327 -1319 -110 O ATOM 2979 CG2 THR A 298 -32.084 -25.722 8.017 1.00 45.63 C ANISOU 2979 CG2 THR A 298 6693 4351 6291 -1489 -1493 18 C ATOM 2980 N PHE A 299 -30.342 -23.844 5.036 1.00 48.00 N ANISOU 2980 N PHE A 299 7453 4732 6055 -1252 -1553 -233 N ATOM 2981 CA PHE A 299 -30.656 -22.622 4.300 1.00 49.85 C ANISOU 2981 CA PHE A 299 7655 5068 6220 -1249 -1654 -226 C ATOM 2982 C PHE A 299 -31.272 -22.940 2.943 1.00 57.38 C ANISOU 2982 C PHE A 299 8831 5901 7072 -1378 -1912 -292 C ATOM 2983 O PHE A 299 -32.277 -22.338 2.550 1.00 58.87 O ANISOU 2983 O PHE A 299 8915 6125 7327 -1471 -2118 -239 O ATOM 2984 CB PHE A 299 -29.400 -21.763 4.124 1.00 45.42 C ANISOU 2984 CB PHE A 299 7163 4602 5491 -1079 -1465 -269 C ATOM 2985 CG PHE A 299 -28.878 -21.161 5.402 1.00 43.56 C ANISOU 2985 CG PHE A 299 6695 4504 5350 -960 -1256 -196 C ATOM 2986 CD1 PHE A 299 -29.638 -21.171 6.560 1.00 43.03 C ANISOU 2986 CD1 PHE A 299 6371 4492 5485 -1007 -1245 -94 C ATOM 2987 CD2 PHE A 299 -27.625 -20.569 5.434 1.00 40.91 C ANISOU 2987 CD2 PHE A 299 6404 4241 4899 -809 -1068 -231 C ATOM 2988 CE1 PHE A 299 -29.154 -20.612 7.728 1.00 41.63 C ANISOU 2988 CE1 PHE A 299 6017 4435 5368 -904 -1059 -34 C ATOM 2989 CE2 PHE A 299 -27.136 -20.008 6.598 1.00 39.45 C ANISOU 2989 CE2 PHE A 299 6022 4174 4794 -710 -902 -168 C ATOM 2990 CZ PHE A 299 -27.902 -20.029 7.746 1.00 41.97 C ANISOU 2990 CZ PHE A 299 6115 4542 5289 -757 -902 -72 C ATOM 2991 N AARG A 300 -30.682 -23.892 2.214 0.50 60.78 N ANISOU 2991 N AARG A 300 9575 6179 7342 -1384 -1910 -410 N ATOM 2992 N BARG A 300 -30.676 -23.886 2.211 0.50 60.77 N ANISOU 2992 N BARG A 300 9574 6178 7339 -1383 -1910 -410 N ATOM 2993 CA AARG A 300 -31.213 -24.257 0.903 0.50 65.84 C ANISOU 2993 CA AARG A 300 10477 6688 7851 -1513 -2159 -486 C ATOM 2994 CA BARG A 300 -31.211 -24.268 0.906 0.50 65.85 C ANISOU 2994 CA BARG A 300 10479 6688 7852 -1513 -2158 -486 C ATOM 2995 C AARG A 300 -32.640 -24.784 1.009 0.50 65.26 C ANISOU 2995 C AARG A 300 10276 6540 7979 -1709 -2424 -421 C ATOM 2996 C BARG A 300 -32.646 -24.763 1.025 0.50 65.24 C ANISOU 2996 C BARG A 300 10267 6542 7980 -1708 -2423 -418 C ATOM 2997 O AARG A 300 -33.505 -24.417 0.205 0.50 64.62 O ANISOU 2997 O AARG A 300 10219 6448 7887 -1819 -2681 -403 O ATOM 2998 O BARG A 300 -33.521 -24.362 0.248 0.50 64.63 O ANISOU 2998 O BARG A 300 10203 6456 7896 -1818 -2680 -398 O ATOM 2999 CB AARG A 300 -30.313 -25.298 0.236 0.50 71.82 C ANISOU 2999 CB AARG A 300 11597 7277 8414 -1479 -2077 -635 C ATOM 3000 CB BARG A 300 -30.338 -25.349 0.267 0.50 71.86 C ANISOU 3000 CB BARG A 300 11598 7277 8427 -1483 -2080 -634 C ATOM 3001 CG AARG A 300 -28.959 -24.778 -0.222 0.50 74.65 C ANISOU 3001 CG AARG A 300 12125 7687 8552 -1308 -1845 -719 C ATOM 3002 CG BARG A 300 -28.936 -24.918 -0.117 0.50 74.71 C ANISOU 3002 CG BARG A 300 12127 7684 8577 -1307 -1833 -720 C ATOM 3003 CD AARG A 300 -28.318 -25.752 -1.202 0.50 80.35 C ANISOU 3003 CD AARG A 300 13244 8222 9063 -1304 -1812 -883 C ATOM 3004 CD BARG A 300 -28.251 -26.033 -0.891 0.50 80.09 C ANISOU 3004 CD BARG A 300 13175 8171 9085 -1292 -1778 -879 C ATOM 3005 NE AARG A 300 -26.973 -25.347 -1.601 0.50 82.26 N ANISOU 3005 NE AARG A 300 13631 8506 9117 -1137 -1551 -967 N ATOM 3006 NE BARG A 300 -26.803 -25.872 -0.956 0.50 81.19 N ANISOU 3006 NE BARG A 300 13412 8340 9097 -1104 -1479 -956 N ATOM 3007 CZ AARG A 300 -25.857 -25.901 -1.138 0.50 81.74 C ANISOU 3007 CZ AARG A 300 13584 8401 9074 -991 -1293 -1024 C ATOM 3008 CZ BARG A 300 -26.171 -25.152 -1.876 0.50 82.77 C ANISOU 3008 CZ BARG A 300 13791 8587 9071 -1043 -1393 -1021 C ATOM 3009 NH1AARG A 300 -24.676 -25.469 -1.558 0.50 82.28 N ANISOU 3009 NH1AARG A 300 13759 8511 8990 -849 -1058 -1096 N ATOM 3010 NH1BARG A 300 -24.849 -25.069 -1.858 0.50 82.31 N ANISOU 3010 NH1BARG A 300 13785 8552 8938 -876 -1104 -1086 N ATOM 3011 NH2AARG A 300 -25.921 -26.893 -0.260 0.50 79.58 N ANISOU 3011 NH2AARG A 300 13215 8038 8983 -989 -1272 -1004 N ATOM 3012 NH2BARG A 300 -26.858 -24.512 -2.812 0.50 83.70 N ANISOU 3012 NH2BARG A 300 14032 8725 9047 -1154 -1599 -1014 N ATOM 3013 N LYS A 301 -32.906 -25.642 1.996 1.00 64.25 N ANISOU 3013 N LYS A 301 10005 6363 8045 -1753 -2364 -372 N ATOM 3014 CA LYS A 301 -34.242 -26.213 2.141 1.00 64.77 C ANISOU 3014 CA LYS A 301 9933 6350 8325 -1952 -2594 -305 C ATOM 3015 C LYS A 301 -35.268 -25.144 2.495 1.00 59.19 C ANISOU 3015 C LYS A 301 8878 5797 7816 -1996 -2695 -178 C ATOM 3016 O LYS A 301 -36.400 -25.175 1.998 1.00 62.29 O ANISOU 3016 O LYS A 301 9174 6184 8309 -2091 -2898 -126 O ATOM 3017 CB LYS A 301 -34.227 -27.317 3.198 1.00 67.12 C ANISOU 3017 CB LYS A 301 10154 6567 8783 -1985 -2471 -269 C ATOM 3018 CG LYS A 301 -33.545 -28.599 2.745 1.00 78.51 C ANISOU 3018 CG LYS A 301 11941 7802 10090 -1989 -2454 -392 C ATOM 3019 CD LYS A 301 -33.731 -29.710 3.764 1.00 87.03 C ANISOU 3019 CD LYS A 301 12938 8778 11353 -2054 -2384 -334 C ATOM 3020 CE LYS A 301 -32.939 -30.950 3.384 1.00 91.56 C ANISOU 3020 CE LYS A 301 13829 9161 11797 -2003 -2320 -451 C ATOM 3021 NZ LYS A 301 -32.982 -31.984 4.456 1.00 94.43 N ANISOU 3021 NZ LYS A 301 14127 9421 12332 -2048 -2237 -384 N ATOM 3022 N ILE A 302 -34.897 -24.197 3.359 1.00 53.31 N ANISOU 3022 N ILE A 302 7905 5228 7123 -1855 -2479 -110 N ATOM 3023 CA ILE A 302 -35.817 -23.122 3.720 1.00 58.23 C ANISOU 3023 CA ILE A 302 8197 5990 7936 -1872 -2546 0 C ATOM 3024 C ILE A 302 -36.122 -22.256 2.504 1.00 61.73 C ANISOU 3024 C ILE A 302 8736 6448 8269 -1888 -2778 -21 C ATOM 3025 O ILE A 302 -37.281 -21.923 2.227 1.00 62.14 O ANISOU 3025 O ILE A 302 8609 6521 8481 -1962 -2970 53 O ATOM 3026 CB ILE A 302 -35.239 -22.284 4.874 1.00 54.24 C ANISOU 3026 CB ILE A 302 7479 5656 7474 -1709 -2255 58 C ATOM 3027 CG1 ILE A 302 -35.184 -23.104 6.164 1.00 52.82 C ANISOU 3027 CG1 ILE A 302 7177 5463 7431 -1722 -2065 108 C ATOM 3028 CG2 ILE A 302 -36.063 -21.028 5.076 1.00 51.33 C ANISOU 3028 CG2 ILE A 302 6814 5423 7267 -1696 -2315 148 C ATOM 3029 CD1 ILE A 302 -34.264 -22.518 7.213 1.00 49.49 C ANISOU 3029 CD1 ILE A 302 6663 5173 6967 -1552 -1773 134 C ATOM 3030 N ILE A 303 -35.081 -21.884 1.757 1.00 64.65 N ANISOU 3030 N ILE A 303 9382 6824 8359 -1779 -2711 -108 N ATOM 3031 CA ILE A 303 -35.256 -21.008 0.602 1.00 69.30 C ANISOU 3031 CA ILE A 303 10101 7426 8804 -1788 -2911 -122 C ATOM 3032 C ILE A 303 -36.048 -21.713 -0.493 1.00 75.92 C ANISOU 3032 C ILE A 303 11095 8152 9598 -1881 -3124 -130 C ATOM 3033 O ILE A 303 -37.006 -21.157 -1.042 1.00 79.15 O ANISOU 3033 O ILE A 303 11399 8587 10086 -1912 -3313 -53 O ATOM 3034 CB ILE A 303 -33.891 -20.509 0.095 1.00 63.60 C ANISOU 3034 CB ILE A 303 9639 6744 7784 -1638 -2720 -204 C ATOM 3035 CG1 ILE A 303 -33.244 -19.601 1.145 1.00 60.43 C ANISOU 3035 CG1 ILE A 303 9001 6510 7449 -1471 -2438 -147 C ATOM 3036 CG2 ILE A 303 -34.048 -19.774 -1.226 1.00 63.54 C ANISOU 3036 CG2 ILE A 303 9829 6729 7587 -1653 -2909 -214 C ATOM 3037 CD1 ILE A 303 -31.731 -19.619 1.139 1.00 60.66 C ANISOU 3037 CD1 ILE A 303 9223 6559 7266 -1324 -2162 -230 C ATOM 3038 N ARG A 304 -35.650 -22.941 -0.839 1.00 80.79 N ANISOU 3038 N ARG A 304 11972 8632 10091 -1920 -3097 -223 N ATOM 3039 CA ARG A 304 -36.350 -23.684 -1.885 1.00 88.79 C ANISOU 3039 CA ARG A 304 13158 9530 11049 -2013 -3300 -238 C ATOM 3040 C ARG A 304 -37.824 -23.856 -1.542 1.00 91.82 C ANISOU 3040 C ARG A 304 13236 9918 11735 -2126 -3482 -122 C ATOM 3041 O ARG A 304 -38.704 -23.528 -2.346 1.00 95.98 O ANISOU 3041 O ARG A 304 13749 10434 12287 -2174 -3700 -69 O ATOM 3042 CB ARG A 304 -35.686 -25.044 -2.106 1.00 91.76 C ANISOU 3042 CB ARG A 304 13824 9756 11284 -2030 -3215 -356 C ATOM 3043 CG ARG A 304 -34.361 -24.983 -2.851 1.00 96.37 C ANISOU 3043 CG ARG A 304 14765 10309 11544 -1920 -3057 -483 C ATOM 3044 CD ARG A 304 -33.666 -26.338 -2.847 1.00103.35 C ANISOU 3044 CD ARG A 304 15881 11044 12341 -1910 -2930 -599 C ATOM 3045 NE ARG A 304 -32.322 -26.270 -3.414 1.00108.60 N ANISOU 3045 NE ARG A 304 16841 11689 12732 -1781 -2721 -721 N ATOM 3046 CZ ARG A 304 -31.431 -27.253 -3.341 1.00112.55 C ANISOU 3046 CZ ARG A 304 17535 12077 13154 -1718 -2541 -833 C ATOM 3047 NH1 ARG A 304 -30.230 -27.104 -3.884 1.00112.75 N ANISOU 3047 NH1 ARG A 304 17793 12097 12951 -1590 -2330 -938 N ATOM 3048 NH2 ARG A 304 -31.739 -28.386 -2.726 1.00113.89 N ANISOU 3048 NH2 ARG A 304 17652 12136 13485 -1779 -2561 -834 N ATOM 3049 N SER A 305 -38.114 -24.371 -0.352 1.00 91.04 N ANISOU 3049 N SER A 305 12891 9829 11872 -2170 -3385 -78 N ATOM 3050 CA SER A 305 -39.495 -24.532 0.090 1.00 95.26 C ANISOU 3050 CA SER A 305 13106 10378 12712 -2270 -3507 33 C ATOM 3051 C SER A 305 -40.125 -23.177 0.394 1.00 97.08 C ANISOU 3051 C SER A 305 13018 10755 13114 -2216 -3533 137 C ATOM 3052 O SER A 305 -40.688 -22.968 1.469 1.00 99.42 O ANISOU 3052 O SER A 305 12971 11130 13673 -2226 -3438 221 O ATOM 3053 CB SER A 305 -39.566 -25.434 1.325 1.00 96.21 C ANISOU 3053 CB SER A 305 13061 10471 13022 -2329 -3353 59 C ATOM 3054 OG SER A 305 -38.914 -26.671 1.094 1.00 98.90 O ANISOU 3054 OG SER A 305 13700 10665 13213 -2361 -3314 -39 O TER 3055 SER A 305 HETATM 3056 NA NA A1201 -23.517 -8.378 16.660 1.00 51.17 NA HETATM 3057 N1 U30 A1202 -19.043 5.993 18.729 1.00 27.77 N HETATM 3058 N3 U30 A1202 -20.544 7.594 17.506 1.00 27.27 N HETATM 3059 C4 U30 A1202 -19.611 3.637 18.969 1.00 26.50 C HETATM 3060 C5 U30 A1202 -19.952 5.018 18.470 1.00 25.95 C HETATM 3061 C6 U30 A1202 -19.388 7.265 18.233 1.00 26.49 C HETATM 3062 C7 U30 A1202 -21.389 6.545 17.285 1.00 25.87 C HETATM 3063 C8 U30 A1202 -22.613 6.802 16.537 1.00 28.53 C HETATM 3064 C10 U30 A1202 -25.267 8.478 14.682 1.00 36.43 C HETATM 3065 C13 U30 A1202 -24.174 9.502 11.309 1.00 34.83 C HETATM 3066 C15 U30 A1202 -23.519 11.217 12.875 1.00 40.32 C HETATM 3067 C17 U30 A1202 -21.316 12.430 13.396 1.00 38.91 C HETATM 3068 C20 U30 A1202 -18.262 3.295 18.993 1.00 24.27 C HETATM 3069 C21 U30 A1202 -17.832 2.045 19.418 1.00 27.47 C HETATM 3070 C22 U30 A1202 -18.742 1.077 19.829 1.00 25.30 C HETATM 3071 N U30 A1202 -21.902 -0.292 20.534 1.00 31.49 N HETATM 3072 C U30 A1202 -21.078 0.468 20.204 1.00 34.67 C HETATM 3073 O U30 A1202 -23.468 13.164 14.180 1.00 47.13 O HETATM 3074 C1 U30 A1202 -20.089 1.393 19.806 1.00 31.83 C HETATM 3075 C11 U30 A1202 -24.650 9.359 13.647 1.00 34.75 C HETATM 3076 C12 U30 A1202 -24.721 8.802 12.368 1.00 35.40 C HETATM 3077 C14 U30 A1202 -23.561 10.727 11.553 1.00 36.03 C HETATM 3078 C16 U30 A1202 -22.834 12.568 13.094 1.00 41.65 C HETATM 3079 C18 U30 A1202 -23.004 13.492 11.886 1.00 41.96 C HETATM 3080 C19 U30 A1202 -21.105 5.273 17.734 1.00 27.03 C HETATM 3081 C2 U30 A1202 -20.547 2.648 19.381 1.00 31.09 C HETATM 3082 C3 U30 A1202 -22.023 2.818 19.423 1.00 33.54 C HETATM 3083 C9 U30 A1202 -23.162 7.962 15.992 1.00 27.33 C HETATM 3084 N2 U30 A1202 -18.488 8.281 18.495 1.00 25.32 N HETATM 3085 N4 U30 A1202 -24.382 7.549 15.393 1.00 30.76 N HETATM 3086 N5 U30 A1202 -24.052 10.536 13.914 1.00 38.49 N HETATM 3087 N6 U30 A1202 -24.529 6.210 15.574 1.00 32.48 N HETATM 3088 N7 U30 A1202 -23.533 5.764 16.229 1.00 34.22 N HETATM 3089 C1 CLR A1203 -37.070 8.821 28.527 1.00123.08 C HETATM 3090 C2 CLR A1203 -36.777 10.301 28.869 1.00123.24 C HETATM 3091 C3 CLR A1203 -37.277 10.727 30.224 1.00123.79 C HETATM 3092 C4 CLR A1203 -36.910 9.704 31.314 1.00125.20 C HETATM 3093 C5 CLR A1203 -37.250 8.293 30.907 1.00125.10 C HETATM 3094 C6 CLR A1203 -38.061 7.575 31.703 1.00125.32 C HETATM 3095 C7 CLR A1203 -38.551 6.178 31.383 1.00124.16 C HETATM 3096 C8 CLR A1203 -37.620 5.493 30.393 1.00122.03 C HETATM 3097 C9 CLR A1203 -37.260 6.408 29.219 1.00120.51 C HETATM 3098 C10 CLR A1203 -36.690 7.792 29.594 1.00122.59 C HETATM 3099 C11 CLR A1203 -36.398 5.601 28.242 1.00117.40 C HETATM 3100 C12 CLR A1203 -36.995 4.244 27.824 1.00116.89 C HETATM 3101 C13 CLR A1203 -37.533 3.371 28.930 1.00117.68 C HETATM 3102 C14 CLR A1203 -38.349 4.301 29.818 1.00119.60 C HETATM 3103 C15 CLR A1203 -39.018 3.364 30.812 1.00118.21 C HETATM 3104 C16 CLR A1203 -39.403 2.199 29.909 1.00116.96 C HETATM 3105 C17 CLR A1203 -38.590 2.292 28.615 1.00115.38 C HETATM 3106 C18 CLR A1203 -36.350 2.688 29.674 1.00118.53 C HETATM 3107 C19 CLR A1203 -35.142 7.757 29.719 1.00122.34 C HETATM 3108 C20 CLR A1203 -38.189 0.883 28.149 1.00111.26 C HETATM 3109 C21 CLR A1203 -37.945 0.820 26.642 1.00110.00 C HETATM 3110 C22 CLR A1203 -39.280 -0.144 28.537 1.00109.48 C HETATM 3111 C23 CLR A1203 -39.141 -1.560 27.956 1.00107.98 C HETATM 3112 C24 CLR A1203 -40.480 -2.016 27.367 1.00106.34 C HETATM 3113 C25 CLR A1203 -41.106 -3.250 28.037 1.00104.50 C HETATM 3114 C26 CLR A1203 -40.772 -3.344 29.525 1.00103.92 C HETATM 3115 C27 CLR A1203 -40.738 -4.554 27.332 1.00102.77 C HETATM 3116 O1 CLR A1203 -36.689 11.990 30.577 1.00122.75 O HETATM 3117 C1 CLR A1204 -38.117 10.822 21.899 1.00 35.50 C HETATM 3118 C2 CLR A1204 -37.915 12.316 22.241 1.00 38.47 C HETATM 3119 C3 CLR A1204 -38.152 12.624 23.696 1.00 37.47 C HETATM 3120 C4 CLR A1204 -37.331 11.689 24.600 1.00 34.76 C HETATM 3121 C5 CLR A1204 -37.569 10.242 24.259 1.00 38.47 C HETATM 3122 C6 CLR A1204 -37.918 9.404 25.248 1.00 39.24 C HETATM 3123 C7 CLR A1204 -38.050 7.895 25.124 1.00 39.44 C HETATM 3124 C8 CLR A1204 -37.689 7.398 23.730 1.00 38.68 C HETATM 3125 C9 CLR A1204 -38.067 8.420 22.649 1.00 37.45 C HETATM 3126 C10 CLR A1204 -37.423 9.807 22.818 1.00 37.86 C HETATM 3127 C11 CLR A1204 -37.851 7.806 21.265 1.00 34.41 C HETATM 3128 C12 CLR A1204 -38.509 6.429 21.092 1.00 34.81 C HETATM 3129 C13 CLR A1204 -38.169 5.419 22.157 1.00 36.11 C HETATM 3130 C14 CLR A1204 -38.463 6.119 23.477 1.00 35.26 C HETATM 3131 C15 CLR A1204 -38.321 5.013 24.516 1.00 35.66 C HETATM 3132 C16 CLR A1204 -38.867 3.795 23.776 1.00 36.45 C HETATM 3133 C17 CLR A1204 -39.008 4.139 22.292 1.00 37.98 C HETATM 3134 C18 CLR A1204 -36.688 4.979 22.035 1.00 35.17 C HETATM 3135 C19 CLR A1204 -35.905 9.766 22.486 1.00 35.59 C HETATM 3136 C20 CLR A1204 -38.694 2.899 21.439 1.00 38.29 C HETATM 3137 C21 CLR A1204 -38.917 3.111 19.940 1.00 39.60 C HETATM 3138 C22 CLR A1204 -39.547 1.702 21.912 1.00 43.36 C HETATM 3139 C23 CLR A1204 -39.417 0.429 21.065 1.00 47.09 C HETATM 3140 C24 CLR A1204 -39.816 -0.785 21.906 1.00 56.14 C HETATM 3141 C25 CLR A1204 -40.012 -2.072 21.095 1.00 64.28 C HETATM 3142 C26 CLR A1204 -40.097 -3.294 22.007 1.00 64.58 C HETATM 3143 C27 CLR A1204 -41.260 -2.001 20.220 1.00 70.71 C HETATM 3144 O1 CLR A1204 -37.766 13.979 23.981 1.00 40.80 O HETATM 3145 C1 CLR A1205 -8.290 10.796 13.369 1.00 43.26 C HETATM 3146 C2 CLR A1205 -8.274 12.333 13.487 1.00 45.56 C HETATM 3147 C3 CLR A1205 -6.915 12.926 13.221 1.00 44.57 C HETATM 3148 C4 CLR A1205 -6.309 12.416 11.900 1.00 42.63 C HETATM 3149 C5 CLR A1205 -6.407 10.918 11.738 1.00 43.95 C HETATM 3150 C6 CLR A1205 -5.321 10.243 11.312 1.00 40.29 C HETATM 3151 C7 CLR A1205 -5.285 8.751 11.021 1.00 41.78 C HETATM 3152 C8 CLR A1205 -6.681 8.135 11.043 1.00 41.88 C HETATM 3153 C9 CLR A1205 -7.511 8.735 12.185 1.00 39.32 C HETATM 3154 C10 CLR A1205 -7.726 10.246 12.056 1.00 42.83 C HETATM 3155 C11 CLR A1205 -8.819 7.965 12.367 1.00 37.82 C HETATM 3156 C12 CLR A1205 -8.641 6.444 12.416 1.00 39.94 C HETATM 3157 C13 CLR A1205 -7.866 5.861 11.265 1.00 42.56 C HETATM 3158 C14 CLR A1205 -6.556 6.637 11.244 1.00 46.33 C HETATM 3159 C15 CLR A1205 -5.688 5.883 10.241 1.00 45.18 C HETATM 3160 C16 CLR A1205 -6.151 4.438 10.401 1.00 46.82 C HETATM 3161 C17 CLR A1205 -7.349 4.414 11.349 1.00 44.93 C HETATM 3162 C18 CLR A1205 -8.681 6.020 9.949 1.00 43.08 C HETATM 3163 C19 CLR A1205 -8.715 10.570 10.900 1.00 43.25 C HETATM 3164 C20 CLR A1205 -8.256 3.214 11.030 1.00 42.17 C HETATM 3165 C21 CLR A1205 -9.463 3.107 11.962 1.00 38.60 C HETATM 3166 C22 CLR A1205 -7.464 1.890 11.107 1.00 42.04 C HETATM 3167 C23 CLR A1205 -8.331 0.628 11.221 1.00 45.70 C HETATM 3168 C24 CLR A1205 -7.464 -0.610 11.465 1.00 54.15 C HETATM 3169 C25 CLR A1205 -8.185 -1.941 11.202 1.00 58.68 C HETATM 3170 C26 CLR A1205 -9.065 -2.344 12.382 1.00 55.47 C HETATM 3171 C27 CLR A1205 -9.020 -1.902 9.924 1.00 62.98 C HETATM 3172 O1 CLR A1205 -7.023 14.357 13.139 1.00 39.35 O HETATM 3173 C1 CLR A1206 -3.183 8.359 21.346 1.00 34.09 C HETATM 3174 C2 CLR A1206 -2.916 9.879 21.315 1.00 31.47 C HETATM 3175 C3 CLR A1206 -1.930 10.262 20.245 1.00 32.69 C HETATM 3176 C4 CLR A1206 -2.343 9.710 18.867 1.00 33.99 C HETATM 3177 C5 CLR A1206 -2.660 8.236 18.908 1.00 32.82 C HETATM 3178 C6 CLR A1206 -2.116 7.430 17.974 1.00 34.25 C HETATM 3179 C7 CLR A1206 -2.361 5.933 17.866 1.00 37.63 C HETATM 3180 C8 CLR A1206 -3.533 5.497 18.740 1.00 37.36 C HETATM 3181 C9 CLR A1206 -3.494 6.215 20.096 1.00 36.12 C HETATM 3182 C10 CLR A1206 -3.583 7.742 20.000 1.00 34.36 C HETATM 3183 C11 CLR A1206 -4.538 5.635 21.052 1.00 31.16 C HETATM 3184 C12 CLR A1206 -4.547 4.104 21.107 1.00 30.73 C HETATM 3185 C13 CLR A1206 -4.635 3.430 19.768 1.00 34.65 C HETATM 3186 C14 CLR A1206 -3.469 3.999 18.972 1.00 32.00 C HETATM 3187 C15 CLR A1206 -3.371 3.106 17.738 1.00 34.26 C HETATM 3188 C16 CLR A1206 -3.911 1.761 18.220 1.00 36.33 C HETATM 3189 C17 CLR A1206 -4.379 1.920 19.666 1.00 36.79 C HETATM 3190 C18 CLR A1206 -6.016 3.726 19.119 1.00 27.54 C HETATM 3191 C19 CLR A1206 -5.029 8.190 19.647 1.00 31.70 C HETATM 3192 C20 CLR A1206 -5.506 0.927 19.999 1.00 41.38 C HETATM 3193 C21 CLR A1206 -5.826 0.870 21.495 1.00 36.47 C HETATM 3194 C22 CLR A1206 -5.169 -0.501 19.515 1.00 49.97 C HETATM 3195 C23 CLR A1206 -6.179 -1.567 19.970 1.00 56.71 C HETATM 3196 C24 CLR A1206 -5.469 -2.859 20.380 1.00 61.64 C HETATM 3197 C25 CLR A1206 -5.087 -3.759 19.197 1.00 62.95 C HETATM 3198 C26 CLR A1206 -4.624 -5.135 19.671 1.00 62.98 C HETATM 3199 C27 CLR A1206 -6.234 -3.912 18.199 1.00 62.29 C HETATM 3200 O1 CLR A1206 -1.850 11.694 20.157 1.00 33.23 O HETATM 3201 C1 OLA A1207 -36.068 15.330 12.888 1.00 82.69 C HETATM 3202 O1 OLA A1207 -35.327 16.287 12.531 1.00 86.01 O HETATM 3203 O2 OLA A1207 -36.868 15.535 13.815 1.00 85.26 O HETATM 3204 C2 OLA A1207 -35.998 13.970 12.223 1.00 74.83 C HETATM 3205 C3 OLA A1207 -36.751 12.902 13.023 1.00 66.54 C HETATM 3206 C4 OLA A1207 -35.976 11.598 13.179 1.00 60.26 C HETATM 3207 C5 OLA A1207 -36.155 10.639 12.019 1.00 54.11 C HETATM 3208 C6 OLA A1207 -36.619 9.240 12.404 1.00 49.11 C HETATM 3209 C7 OLA A1207 -35.947 8.168 11.549 1.00 49.17 C HETATM 3210 C8 OLA A1207 -36.595 6.795 11.606 1.00 51.82 C HETATM 3211 C9 OLA A1207 -35.792 5.841 10.732 1.00 58.09 C HETATM 3212 C10 OLA A1207 -36.264 4.744 10.096 1.00 63.31 C HETATM 3213 C11 OLA A1207 -37.706 4.288 10.163 1.00 66.57 C HETATM 3214 C12 OLA A1207 -37.828 2.757 10.043 1.00 69.85 C HETATM 3215 C13 OLA A1207 -38.547 2.100 11.240 1.00 71.87 C HETATM 3216 C14 OLA A1207 -39.123 0.711 10.917 1.00 73.74 C HETATM 3217 C15 OLA A1207 -38.918 -0.327 12.038 1.00 72.85 C HETATM 3218 C16 OLA A1207 -38.695 -1.758 11.515 1.00 70.39 C HETATM 3219 C17 OLA A1207 -39.693 -2.782 12.078 1.00 68.67 C HETATM 3220 C18 OLA A1207 -39.835 -4.021 11.181 1.00 68.01 C HETATM 3221 C1 OLA A1208 -8.188 14.697 8.104 1.00 83.47 C HETATM 3222 O1 OLA A1208 -7.969 15.547 7.198 1.00 86.73 O HETATM 3223 O2 OLA A1208 -7.917 15.017 9.273 1.00 87.09 O HETATM 3224 C2 OLA A1208 -8.759 13.327 7.797 1.00 76.77 C HETATM 3225 C3 OLA A1208 -7.657 12.297 7.538 1.00 73.17 C HETATM 3226 C4 OLA A1208 -8.061 11.219 6.539 1.00 70.59 C HETATM 3227 C5 OLA A1208 -7.578 9.833 6.916 1.00 65.60 C HETATM 3228 C6 OLA A1208 -8.368 8.694 6.285 1.00 62.87 C HETATM 3229 C7 OLA A1208 -7.615 7.368 6.355 1.00 64.03 C HETATM 3230 C8 OLA A1208 -8.501 6.136 6.313 1.00 67.19 C HETATM 3231 C9 OLA A1208 -8.248 5.390 5.011 1.00 69.05 C HETATM 3232 C10 OLA A1208 -9.194 4.958 4.146 1.00 70.43 C HETATM 3233 C11 OLA A1208 -10.681 5.158 4.351 1.00 70.16 C HETATM 3234 C12 OLA A1208 -11.497 3.964 3.817 1.00 68.71 C HETATM 3235 C13 OLA A1208 -11.117 3.549 2.381 1.00 68.75 C HETATM 3236 C1 OLA A1209 -20.188 -22.320 28.192 1.00 69.74 C HETATM 3237 O1 OLA A1209 -20.544 -22.015 27.021 1.00 72.80 O HETATM 3238 O2 OLA A1209 -20.205 -23.522 28.503 1.00 74.94 O HETATM 3239 C2 OLA A1209 -19.751 -21.273 29.199 1.00 64.20 C HETATM 3240 C3 OLA A1209 -20.164 -19.862 28.775 1.00 59.66 C HETATM 3241 C4 OLA A1209 -19.364 -18.766 29.468 1.00 53.41 C HETATM 3242 C5 OLA A1209 -20.013 -17.398 29.388 1.00 50.35 C HETATM 3243 C6 OLA A1209 -19.125 -16.300 28.816 1.00 49.02 C HETATM 3244 C7 OLA A1209 -19.631 -14.911 29.192 1.00 49.08 C HETATM 3245 C1 OLA A1210 -43.614 -24.406 13.118 1.00 73.01 C HETATM 3246 O1 OLA A1210 -44.017 -25.133 12.169 1.00 76.12 O HETATM 3247 O2 OLA A1210 -42.780 -24.887 13.903 1.00 74.97 O HETATM 3248 C2 OLA A1210 -44.116 -22.989 13.311 1.00 67.74 C HETATM 3249 C3 OLA A1210 -43.229 -22.208 14.283 1.00 67.48 C HETATM 3250 C4 OLA A1210 -43.638 -20.750 14.456 1.00 71.89 C HETATM 3251 C5 OLA A1210 -42.606 -19.931 15.204 1.00 75.02 C HETATM 3252 C6 OLA A1210 -41.215 -20.550 15.242 1.00 74.90 C HETATM 3253 C7 OLA A1210 -40.276 -19.786 16.172 1.00 74.92 C HETATM 3254 C8 OLA A1210 -39.588 -18.587 15.543 1.00 73.84 C HETATM 3255 C9 OLA A1210 -38.226 -19.016 15.018 1.00 72.42 C HETATM 3256 C10 OLA A1210 -37.452 -18.306 14.167 1.00 72.13 C HETATM 3257 C11 OLA A1210 -37.843 -16.955 13.606 1.00 71.58 C HETATM 3258 C12 OLA A1210 -37.345 -15.794 14.489 1.00 69.34 C HETATM 3259 C13 OLA A1210 -37.382 -14.427 13.778 1.00 69.37 C HETATM 3260 C14 OLA A1210 -37.672 -13.252 14.726 1.00 72.37 C HETATM 3261 C15 OLA A1210 -38.231 -12.004 14.013 1.00 73.00 C HETATM 3262 C16 OLA A1210 -38.001 -10.696 14.792 1.00 71.35 C HETATM 3263 C17 OLA A1210 -38.300 -9.431 13.971 1.00 67.77 C HETATM 3264 C9 OLA A1211 -6.899 -17.146 16.444 1.00 62.34 C HETATM 3265 C10 OLA A1211 -8.076 -16.563 16.124 1.00 63.87 C HETATM 3266 C11 OLA A1211 -8.466 -15.166 16.562 1.00 61.46 C HETATM 3267 C12 OLA A1211 -9.958 -15.074 16.937 1.00 55.69 C HETATM 3268 C13 OLA A1211 -10.261 -14.002 18.003 1.00 53.18 C HETATM 3269 C14 OLA A1211 -10.224 -12.569 17.448 1.00 54.09 C HETATM 3270 C15 OLA A1211 -9.915 -11.500 18.514 1.00 51.60 C HETATM 3271 C16 OLA A1211 -9.262 -10.232 17.936 1.00 50.99 C HETATM 3272 C17 OLA A1211 -8.179 -9.628 18.846 1.00 50.53 C HETATM 3273 C18 OLA A1211 -8.139 -8.094 18.780 1.00 51.74 C HETATM 3274 C1 OLA A1212 -21.186 12.967 1.854 1.00 87.22 C HETATM 3275 O1 OLA A1212 -21.819 13.785 1.167 1.00 88.74 O HETATM 3276 O2 OLA A1212 -20.752 13.351 2.975 1.00 87.78 O HETATM 3277 C2 OLA A1212 -20.955 11.558 1.346 1.00 81.16 C HETATM 3278 C3 OLA A1212 -20.811 10.553 2.491 1.00 76.62 C HETATM 3279 C4 OLA A1212 -20.883 9.100 2.040 1.00 73.13 C HETATM 3280 C5 OLA A1212 -21.702 8.218 2.963 1.00 68.87 C HETATM 3281 C6 OLA A1212 -20.927 7.086 3.626 1.00 67.56 C HETATM 3282 C7 OLA A1212 -21.620 5.738 3.440 1.00 63.76 C HETATM 3283 C8 OLA A1212 -21.300 5.033 2.135 1.00 63.32 C HETATM 3284 C9 OLA A1212 -20.813 3.623 2.441 1.00 62.74 C HETATM 3285 C10 OLA A1212 -20.677 2.626 1.539 1.00 63.38 C HETATM 3286 C11 OLA A1212 -20.187 1.238 1.893 1.00 68.53 C HETATM 3287 C12 OLA A1212 -21.254 0.159 1.623 1.00 73.70 C HETATM 3288 C13 OLA A1212 -21.202 -1.028 2.607 1.00 73.91 C HETATM 3289 C14 OLA A1212 -19.793 -1.302 3.156 1.00 74.28 C HETATM 3290 C15 OLA A1212 -19.472 -0.549 4.462 1.00 71.70 C HETATM 3291 C9 OLA A1213 -20.589 -11.274 3.063 1.00 54.61 C HETATM 3292 C10 OLA A1213 -21.450 -10.247 3.254 1.00 55.23 C HETATM 3293 C11 OLA A1213 -21.124 -8.813 2.899 1.00 56.31 C HETATM 3294 C12 OLA A1213 -22.141 -7.823 3.496 1.00 53.79 C HETATM 3295 C13 OLA A1213 -22.061 -6.415 2.873 1.00 52.91 C HETATM 3296 C14 OLA A1213 -23.361 -5.605 3.015 1.00 47.82 C HETATM 3297 C15 OLA A1213 -23.226 -4.138 2.565 1.00 48.52 C HETATM 3298 C16 OLA A1213 -24.568 -3.492 2.177 1.00 50.57 C HETATM 3299 C1 OLA A1214 -11.180 -13.228 8.413 1.00 64.09 C HETATM 3300 C2 OLA A1214 -10.915 -11.888 9.072 1.00 64.56 C HETATM 3301 C3 OLA A1214 -10.201 -12.042 10.418 1.00 65.54 C HETATM 3302 C4 OLA A1214 -9.227 -10.909 10.722 1.00 66.51 C HETATM 3303 C5 OLA A1214 -9.052 -10.632 12.203 1.00 66.04 C HETATM 3304 C6 OLA A1214 -8.267 -9.369 12.530 1.00 66.05 C HETATM 3305 C7 OLA A1214 -8.822 -8.655 13.760 1.00 66.10 C HETATM 3306 C1 OLA A1215 -34.968 11.208 34.274 1.00 94.70 C HETATM 3307 O1 OLA A1215 -35.641 12.003 33.598 1.00 96.28 O HETATM 3308 O2 OLA A1215 -33.946 11.658 34.859 1.00 96.19 O HETATM 3309 C2 OLA A1215 -35.377 9.752 34.379 1.00 89.68 C HETATM 3310 C3 OLA A1215 -34.414 8.829 33.628 1.00 85.12 C HETATM 3311 C4 OLA A1215 -34.887 7.382 33.558 1.00 81.37 C HETATM 3312 C5 OLA A1215 -33.831 6.428 33.035 1.00 75.89 C HETATM 3313 C6 OLA A1215 -34.157 4.949 33.196 1.00 68.92 C HETATM 3314 C7 OLA A1215 -33.003 4.077 32.710 1.00 65.92 C HETATM 3315 C8 OLA A1215 -33.181 2.584 32.916 1.00 63.74 C HETATM 3316 C9 OLA A1215 -31.799 1.953 33.008 1.00 59.44 C HETATM 3317 C10 OLA A1215 -31.530 0.644 33.208 1.00 54.70 C HETATM 3318 C11 OLA A1215 -30.123 0.094 33.287 1.00 55.98 C HETATM 3319 C12 OLA A1215 -30.040 -1.153 34.187 1.00 58.19 C HETATM 3320 C13 OLA A1215 -29.894 -2.468 33.397 1.00 59.38 C HETATM 3321 C14 OLA A1215 -30.671 -3.637 34.022 1.00 62.06 C HETATM 3322 C3 OLA A1216 -40.492 10.954 9.001 1.00 67.92 C HETATM 3323 C4 OLA A1216 -40.356 9.445 9.164 1.00 66.78 C HETATM 3324 C5 OLA A1216 -41.341 8.647 8.331 1.00 67.72 C HETATM 3325 C6 OLA A1216 -41.144 7.138 8.390 1.00 67.94 C HETATM 3326 C7 OLA A1216 -42.169 6.384 7.545 1.00 66.15 C HETATM 3327 C8 OLA A1216 -41.857 4.912 7.340 1.00 68.95 C HETATM 3328 C9 OLA A1216 -43.158 4.142 7.156 1.00 72.05 C HETATM 3329 C10 OLA A1216 -43.474 2.972 7.757 1.00 72.04 C HETATM 3330 C11 OLA A1216 -42.554 2.252 8.720 1.00 70.45 C HETATM 3331 C12 OLA A1216 -42.622 0.722 8.549 1.00 69.03 C HETATM 3332 C13 OLA A1216 -42.942 -0.032 9.856 1.00 64.93 C HETATM 3333 C5 OLA A1217 -33.423 -16.581 26.950 1.00 58.82 C HETATM 3334 C6 OLA A1217 -33.458 -15.123 26.506 1.00 57.71 C HETATM 3335 C7 OLA A1217 -32.947 -14.184 27.599 1.00 58.72 C HETATM 3336 C8 OLA A1217 -33.464 -12.752 27.567 1.00 63.64 C HETATM 3337 C9 OLA A1217 -33.739 -12.333 29.007 1.00 66.67 C HETATM 3338 C10 OLA A1217 -33.774 -11.094 29.562 1.00 65.78 C HETATM 3339 C11 OLA A1217 -33.546 -9.764 28.874 1.00 60.70 C HETATM 3340 C12 OLA A1217 -34.187 -8.612 29.681 1.00 63.72 C HETATM 3341 C13 OLA A1217 -33.229 -7.454 30.034 1.00 64.64 C HETATM 3342 C14 OLA A1217 -33.290 -7.022 31.511 1.00 65.46 C HETATM 3343 C15 OLA A1217 -33.799 -5.583 31.732 1.00 65.04 C HETATM 3344 C16 OLA A1217 -32.677 -4.532 31.779 1.00 62.56 C HETATM 3345 C1 OLA A1218 -16.061 13.865 1.037 1.00 75.64 C HETATM 3346 O1 OLA A1218 -17.222 13.459 0.865 1.00 77.99 O HETATM 3347 O2 OLA A1218 -15.905 15.072 1.371 1.00 76.75 O HETATM 3348 C2 OLA A1218 -14.885 12.927 0.848 1.00 72.39 C HETATM 3349 C3 OLA A1218 -15.211 11.779 -0.111 1.00 72.49 C HETATM 3350 C4 OLA A1218 -15.978 10.638 0.547 1.00 70.55 C HETATM 3351 C5 OLA A1218 -15.358 9.275 0.310 1.00 65.74 C HETATM 3352 C6 OLA A1218 -16.318 8.102 0.452 1.00 62.57 C HETATM 3353 C1 OLA A1219 -36.168 -15.655 5.118 1.00 82.43 C HETATM 3354 O1 OLA A1219 -36.951 -16.585 5.362 1.00 83.20 O HETATM 3355 O2 OLA A1219 -35.593 -15.099 6.094 1.00 82.49 O HETATM 3356 C2 OLA A1219 -35.923 -15.218 3.687 1.00 81.07 C HETATM 3357 C3 OLA A1219 -34.492 -14.712 3.484 1.00 78.78 C HETATM 3358 C4 OLA A1219 -33.759 -15.407 2.343 1.00 74.87 C HETATM 3359 C5 OLA A1219 -32.777 -14.505 1.622 1.00 68.69 C HETATM 3360 C6 OLA A1219 -31.345 -14.581 2.134 1.00 63.17 C HETATM 3361 C7 OLA A1219 -30.933 -13.298 2.850 1.00 59.09 C HETATM 3362 C8 OLA A1219 -29.436 -13.114 3.011 1.00 56.79 C HETATM 3363 C9 OLA A1219 -29.147 -11.644 3.278 1.00 57.83 C HETATM 3364 C10 OLA A1219 -28.090 -11.162 3.970 1.00 61.46 C HETATM 3365 C1 OLA A1220 -27.722 -20.723 39.892 1.00 85.94 C HETATM 3366 O1 OLA A1220 -27.022 -21.764 39.761 1.00 86.95 O HETATM 3367 O2 OLA A1220 -28.745 -20.798 40.592 1.00 86.55 O HETATM 3368 C2 OLA A1220 -27.345 -19.414 39.225 1.00 84.44 C HETATM 3369 C3 OLA A1220 -28.107 -18.225 39.818 1.00 82.15 C HETATM 3370 C4 OLA A1220 -27.722 -16.887 39.197 1.00 78.28 C HETATM 3371 C5 OLA A1220 -26.333 -16.419 39.583 1.00 75.51 C HETATM 3372 C6 OLA A1220 -25.568 -15.687 38.487 1.00 74.74 C HETATM 3373 C7 OLA A1220 -24.441 -14.833 39.062 1.00 75.86 C HETATM 3374 C8 OLA A1220 -23.872 -13.786 38.120 1.00 77.69 C HETATM 3375 C9 OLA A1220 -23.828 -12.449 38.848 1.00 79.91 C HETATM 3376 C10 OLA A1220 -24.691 -11.425 38.666 1.00 79.36 C HETATM 3377 C11 OLA A1220 -24.618 -10.109 39.412 1.00 77.45 C HETATM 3378 C12 OLA A1220 -23.207 -9.491 39.390 1.00 74.53 C HETATM 3379 C13 OLA A1220 -23.177 -8.024 39.867 1.00 70.69 C HETATM 3380 C14 OLA A1220 -22.252 -7.129 39.027 1.00 69.49 C HETATM 3381 C15 OLA A1220 -22.981 -6.353 37.912 1.00 66.00 C HETATM 3382 C16 OLA A1220 -22.027 -5.681 36.908 1.00 62.54 C HETATM 3383 C17 OLA A1220 -22.360 -4.204 36.643 1.00 61.71 C HETATM 3384 C18 OLA A1220 -21.528 -3.610 35.497 1.00 60.98 C HETATM 3385 C1 OLA A1221 -28.668 -21.196 35.033 1.00 83.08 C HETATM 3386 O1 OLA A1221 -27.498 -21.419 34.681 1.00 81.62 O HETATM 3387 O2 OLA A1221 -29.499 -22.143 34.948 1.00 83.35 O HETATM 3388 C2 OLA A1221 -29.061 -19.824 35.544 1.00 82.50 C HETATM 3389 C3 OLA A1221 -30.555 -19.542 35.360 1.00 81.85 C HETATM 3390 C4 OLA A1221 -31.017 -18.250 36.025 1.00 80.66 C HETATM 3391 C5 OLA A1221 -31.011 -17.052 35.096 1.00 81.23 C HETATM 3392 C6 OLA A1221 -31.810 -15.852 35.588 1.00 79.81 C HETATM 3393 C7 OLA A1221 -31.015 -14.552 35.471 1.00 77.31 C HETATM 3394 C8 OLA A1221 -30.656 -13.901 36.795 1.00 76.20 C HETATM 3395 C9 OLA A1221 -30.003 -12.551 36.529 1.00 74.67 C HETATM 3396 C10 OLA A1221 -28.846 -12.116 37.078 1.00 74.55 C HETATM 3397 C11 OLA A1221 -28.236 -10.761 36.783 1.00 73.42 C HETATM 3398 C12 OLA A1221 -26.764 -10.872 36.343 1.00 69.46 C HETATM 3399 C1 OLB A1222 -31.951 6.707 36.579 1.00 71.68 C HETATM 3400 C2 OLB A1222 -33.086 5.654 36.543 1.00 69.50 C HETATM 3401 C3 OLB A1222 -32.530 4.185 36.346 1.00 66.66 C HETATM 3402 C4 OLB A1222 -31.636 3.609 37.504 1.00 62.58 C HETATM 3403 C5 OLB A1222 -32.270 2.464 38.364 1.00 62.54 C HETATM 3404 O19 OLB A1222 -30.789 6.489 36.557 1.00 74.75 O HETATM 3405 O20 OLB A1222 -32.347 8.050 36.641 1.00 73.73 O HETATM 3406 C21 OLB A1222 -31.239 8.965 36.819 1.00 77.95 C HETATM 3407 C22 OLB A1222 -31.773 10.435 36.929 1.00 84.44 C HETATM 3408 O23 OLB A1222 -33.158 10.339 37.011 1.00 89.11 O HETATM 3409 C24 OLB A1222 -31.266 11.055 38.282 1.00 83.87 C HETATM 3410 O25 OLB A1222 -31.930 10.333 39.285 1.00 80.38 O HETATM 3411 C6 OLB A1222 -31.886 0.994 37.975 1.00 60.08 C HETATM 3412 C7 OLB A1222 -30.597 0.422 38.657 1.00 56.81 C HETATM 3413 C8 OLB A1222 -30.169 -1.018 38.223 1.00 59.37 C HETATM 3414 C9 OLB A1222 -30.491 -2.186 39.132 1.00 66.08 C HETATM 3415 C10 OLB A1222 -30.509 -3.486 38.768 1.00 71.69 C HETATM 3416 C11 OLB A1222 -30.209 -4.030 37.382 1.00 72.15 C HETATM 3417 C12 OLB A1222 -28.746 -3.948 36.818 1.00 68.70 C HETATM 3418 C13 OLB A1222 -28.029 -5.313 36.542 1.00 61.37 C HETATM 3419 C14 OLB A1222 -27.153 -5.873 37.710 1.00 57.77 C HETATM 3420 C15 OLB A1222 -26.272 -7.124 37.380 1.00 61.55 C HETATM 3421 C1 OLB A1223 -1.643 12.524 26.255 1.00 61.46 C HETATM 3422 C2 OLB A1223 -2.729 11.493 25.877 1.00 51.83 C HETATM 3423 C3 OLB A1223 -2.103 10.166 25.306 1.00 42.48 C HETATM 3424 C4 OLB A1223 -2.446 8.841 26.065 1.00 38.88 C HETATM 3425 C5 OLB A1223 -2.662 7.590 25.149 1.00 38.65 C HETATM 3426 O19 OLB A1223 -0.680 12.322 26.909 1.00 69.57 O HETATM 3427 O20 OLB A1223 -1.821 13.817 25.750 1.00 68.20 O HETATM 3428 C21 OLB A1223 -1.384 14.871 26.642 1.00 74.78 C HETATM 3429 C22 OLB A1223 -1.293 16.209 25.824 1.00 79.16 C HETATM 3430 O23 OLB A1223 0.039 16.341 25.459 1.00 78.85 O HETATM 3431 C24 OLB A1223 -2.122 16.054 24.494 1.00 79.88 C HETATM 3432 O25 OLB A1223 -3.326 16.740 24.718 1.00 80.12 O HETATM 3433 C6 OLB A1223 -3.100 6.267 25.856 1.00 44.53 C HETATM 3434 C7 OLB A1223 -3.641 5.143 24.910 1.00 50.22 C HETATM 3435 C8 OLB A1223 -3.608 3.680 25.474 1.00 52.54 C HETATM 3436 C9 OLB A1223 -2.683 2.669 24.830 1.00 55.50 C HETATM 3437 C10 OLB A1223 -2.863 1.333 24.821 1.00 59.74 C HETATM 3438 C11 OLB A1223 -4.025 0.597 25.453 1.00 63.41 C HETATM 3439 C12 OLB A1223 -4.289 -0.902 25.060 1.00 63.86 C HETATM 3440 C1 OLB A1224 -34.324 -21.056 18.073 1.00 71.15 C HETATM 3441 C2 OLB A1224 -35.608 -20.193 18.063 1.00 66.38 C HETATM 3442 C3 OLB A1224 -35.320 -18.693 17.692 1.00 64.84 C HETATM 3443 C4 OLB A1224 -36.103 -17.615 18.519 1.00 63.09 C HETATM 3444 C5 OLB A1224 -35.223 -16.545 19.251 1.00 61.80 C HETATM 3445 O19 OLB A1224 -33.506 -21.119 17.222 1.00 74.23 O HETATM 3446 O20 OLB A1224 -34.119 -21.823 19.227 1.00 75.74 O HETATM 3447 C21 OLB A1224 -33.918 -23.235 18.990 1.00 80.62 C HETATM 3448 C22 OLB A1224 -34.090 -23.991 20.356 1.00 86.51 C HETATM 3449 O23 OLB A1224 -35.446 -23.934 20.657 1.00 90.06 O HETATM 3450 C24 OLB A1224 -33.727 -25.505 20.159 1.00 89.66 C HETATM 3451 O25 OLB A1224 -33.889 -26.088 21.423 1.00 90.32 O HETATM 3452 C6 OLB A1224 -34.666 -15.394 18.363 1.00 59.35 C HETATM 3453 C7 OLB A1224 -35.739 -14.454 17.728 1.00 59.69 C HETATM 3454 C8 OLB A1224 -35.390 -12.935 17.703 1.00 58.18 C HETATM 3455 C9 OLB A1224 -35.730 -12.081 18.901 1.00 61.35 C HETATM 3456 C10 OLB A1224 -35.506 -10.761 18.964 1.00 62.26 C HETATM 3457 C11 OLB A1224 -34.889 -9.965 17.845 1.00 62.18 C HETATM 3458 C18 OLC A1225 -39.898 -5.342 18.061 1.00 81.56 C HETATM 3459 C10 OLC A1225 -38.401 3.132 14.678 1.00 58.84 C HETATM 3460 C9 OLC A1225 -37.919 4.414 14.845 1.00 53.92 C HETATM 3461 C17 OLC A1225 -39.774 -3.904 17.525 1.00 82.19 C HETATM 3462 C11 OLC A1225 -38.106 2.023 15.652 1.00 59.20 C HETATM 3463 C8 OLC A1225 -37.057 4.803 16.012 1.00 48.05 C HETATM 3464 C24 OLC A1225 -39.190 16.250 20.246 1.00 80.97 C HETATM 3465 C16 OLC A1225 -40.714 -3.562 16.332 1.00 81.20 C HETATM 3466 C12 OLC A1225 -38.851 0.667 15.421 1.00 62.52 C HETATM 3467 C7 OLC A1225 -36.824 6.333 16.227 1.00 53.45 C HETATM 3468 C15 OLC A1225 -40.558 -2.117 15.768 1.00 78.41 C HETATM 3469 C13 OLC A1225 -40.132 0.452 16.299 1.00 69.71 C HETATM 3470 C6 OLC A1225 -37.769 7.004 17.282 1.00 52.11 C HETATM 3471 C14 OLC A1225 -40.331 -1.001 16.846 1.00 74.98 C HETATM 3472 C5 OLC A1225 -37.399 8.469 17.685 1.00 47.65 C HETATM 3473 C4 OLC A1225 -38.080 9.609 16.861 1.00 49.28 C HETATM 3474 C3 OLC A1225 -37.771 11.052 17.362 1.00 53.50 C HETATM 3475 C2 OLC A1225 -38.541 12.234 16.681 1.00 59.04 C HETATM 3476 C21 OLC A1225 -40.006 15.443 17.947 1.00 68.86 C HETATM 3477 C1 OLC A1225 -39.028 13.257 17.655 1.00 60.32 C HETATM 3478 C22 OLC A1225 -39.191 16.607 18.676 1.00 77.73 C HETATM 3479 O19 OLC A1225 -39.448 13.047 18.790 1.00 62.44 O HETATM 3480 O25 OLC A1225 -39.331 17.502 20.862 1.00 80.97 O HETATM 3481 O23 OLC A1225 -37.903 16.515 18.239 1.00 77.46 O HETATM 3482 O20 OLC A1225 -39.029 14.644 17.289 1.00 61.67 O HETATM 3483 C10 OLC A1226 -32.793 -10.566 23.393 1.00 53.61 C HETATM 3484 C9 OLC A1226 -32.548 -11.827 22.876 1.00 51.34 C HETATM 3485 C11 OLC A1226 -33.885 -10.239 24.377 1.00 52.04 C HETATM 3486 C8 OLC A1226 -33.333 -13.065 23.216 1.00 48.18 C HETATM 3487 C24 OLC A1226 -32.206 -25.940 25.831 1.00 83.65 C HETATM 3488 C12 OLC A1226 -34.017 -8.721 24.786 1.00 47.88 C HETATM 3489 C7 OLC A1226 -33.056 -14.320 22.305 1.00 47.15 C HETATM 3490 C6 OLC A1226 -33.004 -15.701 23.057 1.00 52.01 C HETATM 3491 C5 OLC A1226 -31.748 -16.593 22.750 1.00 48.89 C HETATM 3492 C4 OLC A1226 -32.039 -18.020 22.175 1.00 52.13 C HETATM 3493 C3 OLC A1226 -31.382 -19.213 22.941 1.00 59.30 C HETATM 3494 C2 OLC A1226 -32.327 -20.062 23.866 1.00 69.71 C HETATM 3495 C21 OLC A1226 -32.070 -23.647 24.690 1.00 81.17 C HETATM 3496 C1 OLC A1226 -32.282 -21.524 23.562 1.00 79.54 C HETATM 3497 C22 OLC A1226 -33.095 -24.748 25.220 1.00 84.91 C HETATM 3498 O19 OLC A1226 -31.802 -22.046 22.562 1.00 85.84 O HETATM 3499 O25 OLC A1226 -33.122 -26.670 26.601 1.00 82.30 O HETATM 3500 O23 OLC A1226 -33.775 -24.180 26.254 1.00 88.32 O HETATM 3501 O20 OLC A1226 -32.841 -22.467 24.489 1.00 80.03 O HETATM 3502 C10 OLC A1227 -43.511 3.196 14.020 1.00 62.50 C HETATM 3503 C9 OLC A1227 -42.947 4.243 13.317 1.00 61.36 C HETATM 3504 C11 OLC A1227 -42.794 1.893 14.263 1.00 63.14 C HETATM 3505 C8 OLC A1227 -41.564 4.176 12.725 1.00 64.33 C HETATM 3506 C24 OLC A1227 -41.911 18.056 14.407 1.00 83.42 C HETATM 3507 C12 OLC A1227 -43.312 0.636 13.482 1.00 63.46 C HETATM 3508 C7 OLC A1227 -40.943 5.527 12.226 1.00 65.05 C HETATM 3509 C13 OLC A1227 -44.241 -0.324 14.311 1.00 67.91 C HETATM 3510 C6 OLC A1227 -40.792 6.647 13.320 1.00 62.94 C HETATM 3511 C14 OLC A1227 -43.871 -1.850 14.258 1.00 70.08 C HETATM 3512 C5 OLC A1227 -41.344 8.057 12.915 1.00 65.52 C HETATM 3513 C4 OLC A1227 -40.697 9.296 13.626 1.00 64.22 C HETATM 3514 C3 OLC A1227 -41.231 10.692 13.157 1.00 62.39 C HETATM 3515 C2 OLC A1227 -40.951 11.914 14.096 1.00 66.88 C HETATM 3516 C21 OLC A1227 -42.009 15.554 13.827 1.00 80.81 C HETATM 3517 C1 OLC A1227 -41.613 13.175 13.643 1.00 74.12 C HETATM 3518 C22 OLC A1227 -41.024 16.811 13.912 1.00 83.70 C HETATM 3519 O19 OLC A1227 -42.481 13.282 12.781 1.00 80.22 O HETATM 3520 O25 OLC A1227 -41.424 18.308 15.696 1.00 83.19 O HETATM 3521 O23 OLC A1227 -40.125 16.538 14.899 1.00 84.08 O HETATM 3522 O20 OLC A1227 -41.234 14.427 14.234 1.00 78.73 O HETATM 3523 C10 OLC A1228 -4.491 0.380 29.435 1.00 73.60 C HETATM 3524 C9 OLC A1228 -4.281 1.747 29.484 1.00 74.06 C HETATM 3525 C8 OLC A1228 -3.780 2.460 30.717 1.00 74.65 C HETATM 3526 C24 OLC A1228 -6.936 14.213 28.174 1.00 86.59 C HETATM 3527 C7 OLC A1228 -3.235 3.924 30.525 1.00 73.33 C HETATM 3528 C6 OLC A1228 -4.121 4.879 29.639 1.00 71.40 C HETATM 3529 C5 OLC A1228 -3.637 6.379 29.563 1.00 70.61 C HETATM 3530 C4 OLC A1228 -4.069 7.311 30.753 1.00 70.43 C HETATM 3531 C3 OLC A1228 -3.290 8.666 30.893 1.00 71.17 C HETATM 3532 C2 OLC A1228 -3.334 9.649 29.666 1.00 76.36 C HETATM 3533 C21 OLC A1228 -5.588 12.024 28.239 1.00 86.79 C HETATM 3534 C1 OLC A1228 -4.253 10.819 29.859 1.00 84.03 C HETATM 3535 C22 OLC A1228 -7.033 12.644 28.521 1.00 84.83 C HETATM 3536 O19 OLC A1228 -4.084 11.774 30.615 1.00 87.30 O HETATM 3537 O25 OLC A1228 -6.505 14.225 26.840 1.00 86.50 O HETATM 3538 O23 OLC A1228 -7.880 12.084 27.613 1.00 81.47 O HETATM 3539 O20 OLC A1228 -5.474 10.895 29.107 1.00 87.41 O HETATM 3540 C18 OLC A1229 -33.895 2.232 -0.303 1.00 65.33 C HETATM 3541 C10 OLC A1229 -34.626 10.723 2.778 1.00 76.10 C HETATM 3542 C9 OLC A1229 -34.626 11.941 3.434 1.00 78.54 C HETATM 3543 C17 OLC A1229 -34.523 3.199 0.718 1.00 63.62 C HETATM 3544 C11 OLC A1229 -33.488 9.736 2.865 1.00 72.82 C HETATM 3545 C8 OLC A1229 -33.484 12.409 4.300 1.00 80.85 C HETATM 3546 C24 OLC A1229 -25.796 16.477 12.377 1.00 92.70 C HETATM 3547 C16 OLC A1229 -35.035 4.539 0.116 1.00 62.82 C HETATM 3548 C12 OLC A1229 -33.744 8.318 2.240 1.00 69.44 C HETATM 3549 C7 OLC A1229 -33.840 13.431 5.437 1.00 82.75 C HETATM 3550 C15 OLC A1229 -34.989 5.769 1.081 1.00 65.84 C HETATM 3551 C13 OLC A1229 -34.318 8.324 0.776 1.00 68.00 C HETATM 3552 C6 OLC A1229 -32.837 13.460 6.650 1.00 83.95 C HETATM 3553 C14 OLC A1229 -35.312 7.160 0.430 1.00 68.11 C HETATM 3554 C5 OLC A1229 -33.361 14.167 7.954 1.00 85.27 C HETATM 3555 C4 OLC A1229 -32.532 15.406 8.451 1.00 86.81 C HETATM 3556 C3 OLC A1229 -30.970 15.243 8.448 1.00 87.51 C HETATM 3557 C2 OLC A1229 -30.164 16.146 9.452 1.00 89.46 C HETATM 3558 C21 OLC A1229 -27.488 17.551 10.761 1.00 96.09 C HETATM 3559 C1 OLC A1229 -28.725 16.330 9.079 1.00 93.37 C HETATM 3560 C22 OLC A1229 -27.237 17.188 12.298 1.00 94.45 C HETATM 3561 O19 OLC A1229 -28.272 16.510 7.951 1.00 92.29 O HETATM 3562 O25 OLC A1229 -24.903 17.555 12.352 1.00 92.21 O HETATM 3563 O23 OLC A1229 -27.141 18.371 12.967 1.00 94.94 O HETATM 3564 O20 OLC A1229 -27.718 16.306 10.103 1.00 96.62 O HETATM 3565 O HOH A1301 -26.263 13.127 8.400 1.00 50.16 O HETATM 3566 O HOH A1302 1.572 -46.816 20.509 1.00 70.26 O HETATM 3567 O HOH A1303 -27.327 19.586 14.861 1.00 73.29 O HETATM 3568 O HOH A1304 -18.357 12.869 23.884 1.00 40.82 O HETATM 3569 O HOH A1305 5.190 -73.371 20.032 1.00 67.88 O HETATM 3570 O HOH A1306 -16.493 14.796 20.425 1.00 44.11 O HETATM 3571 O HOH A1307 -15.262 10.159 17.978 1.00 25.69 O HETATM 3572 O HOH A1308 -28.881 12.408 8.731 1.00 47.77 O HETATM 3573 O HOH A1309 -23.760 -10.936 11.511 1.00 36.55 O HETATM 3574 O HOH A1310 -25.334 -13.219 13.722 1.00 31.57 O HETATM 3575 O HOH A1311 -24.570 16.832 1.987 1.00 48.49 O HETATM 3576 O HOH A1312 -22.668 -28.088 21.586 1.00 54.05 O HETATM 3577 O HOH A1313 -24.199 -30.682 25.475 1.00 68.40 O HETATM 3578 O HOH A1314 -9.658 15.167 19.048 1.00 53.42 O HETATM 3579 O HOH A1315 -25.776 13.662 10.480 1.00 57.09 O HETATM 3580 O HOH A1316 -31.070 21.984 27.863 1.00 66.76 O HETATM 3581 O HOH A1317 -31.066 8.348 32.840 1.00 57.63 O HETATM 3582 O HOH A1318 -17.640 -17.256 16.947 1.00 42.99 O HETATM 3583 O HOH A1319 -20.805 16.532 18.998 1.00 47.92 O HETATM 3584 O HOH A1320 -23.645 15.170 33.494 1.00 49.61 O HETATM 3585 O HOH A1321 -16.195 -16.724 19.227 1.00 32.48 O HETATM 3586 O HOH A1322 -28.402 2.798 19.882 1.00 36.32 O HETATM 3587 O HOH A1323 -25.841 -12.097 21.736 1.00 29.17 O HETATM 3588 O HOH A1324 -33.795 14.188 34.187 1.00 67.68 O HETATM 3589 O HOH A1325 -19.357 -35.594 26.798 1.00 51.23 O HETATM 3590 O HOH A1326 -26.173 -11.875 25.808 1.00 38.31 O HETATM 3591 O HOH A1327 -18.759 -11.316 13.066 1.00 33.33 O HETATM 3592 O HOH A1328 -13.180 -33.517 21.240 1.00 51.38 O HETATM 3593 O HOH A1329 -10.943 -33.630 22.058 1.00 58.74 O HETATM 3594 O HOH A1330 -16.126 16.597 8.723 1.00 68.19 O HETATM 3595 O HOH A1331 7.510 -72.799 21.835 1.00 66.76 O HETATM 3596 O HOH A1332 -22.191 -9.845 15.369 1.00 46.94 O HETATM 3597 O HOH A1333 -16.293 0.717 12.758 1.00 28.94 O HETATM 3598 O HOH A1334 -22.184 -6.410 15.573 1.00 35.00 O HETATM 3599 O HOH A1335 -25.074 -15.767 14.790 1.00 35.89 O HETATM 3600 O HOH A1336 -0.983 -62.657 20.158 1.00 41.93 O HETATM 3601 O HOH A1337 -14.504 -26.950 17.488 1.00 35.68 O HETATM 3602 O HOH A1338 -26.120 18.437 22.360 1.00 33.21 O HETATM 3603 O HOH A1339 -2.857 -64.549 20.447 1.00 55.21 O HETATM 3604 O HOH A1340 -10.208 14.801 25.362 1.00 49.93 O HETATM 3605 O HOH A1341 -18.963 12.175 15.865 1.00 61.66 O HETATM 3606 O HOH A1342 -20.532 18.708 18.123 1.00 61.28 O HETATM 3607 O HOH A1343 5.523 -75.631 26.749 1.00 46.48 O HETATM 3608 O HOH A1344 -2.365 13.586 22.090 1.00 40.15 O HETATM 3609 O HOH A1345 -25.784 -14.368 24.848 1.00 51.42 O HETATM 3610 O HOH A1346 -8.736 -53.074 26.072 1.00 88.88 O HETATM 3611 O HOH A1347 -23.500 -4.624 14.252 1.00 25.76 O HETATM 3612 O HOH A1348 -22.037 -29.021 8.986 1.00 50.69 O HETATM 3613 O HOH A1349 -27.441 2.879 17.195 1.00 31.09 O HETATM 3614 O HOH A1350 -11.407 11.996 15.848 1.00 30.74 O HETATM 3615 O HOH A1351 -19.246 -1.704 22.183 1.00 29.96 O HETATM 3616 O HOH A1352 -32.531 23.598 25.683 1.00 70.47 O HETATM 3617 O HOH A1353 -18.788 9.959 22.983 1.00 49.07 O HETATM 3618 O HOH A1354 -27.432 -11.353 7.005 1.00 47.50 O HETATM 3619 O HOH A1355 -11.510 15.353 23.540 1.00 48.54 O HETATM 3620 O HOH A1356 -15.137 3.456 22.018 1.00 26.90 O HETATM 3621 O HOH A1357 -13.321 17.473 11.447 1.00 54.91 O HETATM 3622 O HOH A1358 -12.018 19.094 15.028 1.00 54.42 O HETATM 3623 O HOH A1359 -13.787 -27.879 19.614 1.00 52.40 O HETATM 3624 O HOH A1360 -22.336 12.285 17.814 1.00 34.91 O HETATM 3625 O HOH A1361 -20.552 -11.415 15.178 1.00 41.27 O HETATM 3626 O HOH A1362 -20.640 10.263 16.572 1.00 28.66 O HETATM 3627 O HOH A1363 -18.038 -2.784 20.121 1.00 30.13 O HETATM 3628 O HOH A1364 -25.770 18.741 24.982 1.00 32.05 O HETATM 3629 O HOH A1365 -24.696 -6.580 17.817 1.00 49.32 O HETATM 3630 O HOH A1366 9.133 -70.339 20.917 1.00 38.03 O HETATM 3631 O HOH A1367 3.316 -72.934 24.118 1.00 45.71 O HETATM 3632 O HOH A1368 -22.735 1.130 15.790 1.00 62.19 O HETATM 3633 O HOH A1369 -25.622 16.917 26.996 1.00 45.00 O HETATM 3634 O HOH A1370 -29.798 17.973 29.838 1.00 51.61 O HETATM 3635 O HOH A1371 -24.532 11.456 16.710 1.00 35.56 O HETATM 3636 O HOH A1372 -21.249 -27.744 18.111 1.00 64.53 O HETATM 3637 O HOH A1373 -27.626 20.602 22.688 1.00 34.37 O HETATM 3638 O HOH A1374 -20.756 -2.614 24.411 1.00 29.11 O HETATM 3639 O HOH A1375 -32.639 -33.103 10.776 1.00 80.84 O HETATM 3640 O HOH A1376 -4.306 -63.907 18.061 1.00 56.19 O HETATM 3641 O HOH A1377 2.286 -68.255 18.833 1.00 61.96 O HETATM 3642 O HOH A1378 -21.406 -33.185 22.145 1.00 61.20 O HETATM 3643 O HOH A1379 -19.594 -30.675 20.839 1.00 61.40 O HETATM 3644 O HOH A1380 14.188 -64.971 16.597 1.00 64.18 O HETATM 3645 O HOH A1381 -21.923 22.955 27.959 1.00 57.52 O HETATM 3646 O HOH A1382 -17.451 13.990 29.546 1.00 60.81 O HETATM 3647 O HOH A1383 15.029 -55.701 18.573 1.00 64.26 O HETATM 3648 O HOH A1384 -4.178 -25.763 25.185 1.00 47.51 O HETATM 3649 O HOH A1385 -5.335 17.144 12.917 1.00 63.35 O HETATM 3650 O HOH A1386 -28.552 9.503 35.340 1.00 63.58 O HETATM 3651 O HOH A1387 -36.088 18.587 16.574 1.00 56.30 O HETATM 3652 O HOH A1388 -3.586 16.217 21.649 1.00 42.29 O HETATM 3653 O HOH A1389 -25.174 12.999 35.203 1.00 61.04 O HETATM 3654 O HOH A1390 -25.207 -29.575 23.034 1.00 51.69 O HETATM 3655 O HOH A1391 -24.585 2.925 16.150 1.00 39.43 O HETATM 3656 O HOH A1392 -34.301 13.872 30.506 1.00 53.77 O HETATM 3657 O HOH A1393 -23.709 19.726 16.021 1.00 69.02 O HETATM 3658 O HOH A1394 0.816 -72.666 23.438 1.00 65.12 O HETATM 3659 O HOH A1395 -9.281 13.386 16.671 1.00 42.72 O HETATM 3660 O HOH A1396 -29.732 28.870 28.803 1.00 64.90 O HETATM 3661 O HOH A1397 -10.805 14.485 4.932 1.00 57.37 O HETATM 3662 O HOH A1398 -18.894 -28.262 6.432 1.00 72.43 O HETATM 3663 O HOH A1399 -17.326 13.566 26.337 1.00 37.29 O HETATM 3664 O HOH A1400 -37.211 17.739 28.586 1.00 61.15 O HETATM 3665 O HOH A1401 -15.176 12.326 28.701 1.00 34.10 O HETATM 3666 O HOH A1402 -12.343 -35.613 28.922 1.00 57.02 O HETATM 3667 O HOH A1403 14.512 -64.901 14.270 1.00 79.08 O HETATM 3668 O HOH A1404 -20.870 11.967 35.114 1.00 63.92 O HETATM 3669 O HOH A1405 -19.655 12.626 32.926 1.00 60.84 O HETATM 3670 O HOH A1406 -16.513 15.070 5.300 1.00 47.56 O HETATM 3671 O HOH A1407 -5.122 -31.229 24.538 1.00 58.42 O HETATM 3672 O HOH A1408 -27.978 11.688 35.219 1.00 85.74 O HETATM 3673 O HOH A1409 -17.394 12.228 32.846 1.00 57.15 O HETATM 3674 O HOH A1410 5.814 -73.343 29.393 1.00 60.24 O HETATM 3675 O HOH A1411 -12.992 13.331 30.506 1.00 70.07 O HETATM 3676 O HOH A1412 -19.590 -28.526 8.542 1.00 56.52 O HETATM 3677 O HOH A1413 1.506 -73.141 19.825 1.00 66.40 O HETATM 3678 O HOH A1414 -35.777 -34.740 13.889 1.00 70.18 O HETATM 3679 O HOH A1415 -31.310 15.892 31.821 1.00 62.70 O HETATM 3680 O HOH A1416 -17.382 15.186 12.381 1.00 56.37 O HETATM 3681 O HOH A1417 -11.379 10.721 32.393 1.00 45.60 O HETATM 3682 O HOH A1418 4.172 -75.109 22.774 1.00 56.19 O HETATM 3683 O HOH A1419 -31.173 20.266 29.332 1.00 68.77 O HETATM 3684 O HOH A1420 6.296 -75.800 24.232 1.00 43.20 O HETATM 3685 O HOH A1421 -28.883 15.115 35.053 1.00 77.28 O HETATM 3686 O HOH A1422 -11.697 16.298 18.575 1.00 55.26 O HETATM 3687 O HOH A1423 -18.093 16.258 16.803 1.00 72.09 O HETATM 3688 O HOH A1424 -18.855 14.807 15.191 1.00 66.89 O HETATM 3689 O HOH A1425 -16.116 17.097 11.850 1.00 68.05 O HETATM 3690 O HOH A1426 -21.515 14.608 17.262 1.00 44.33 O CONECT 411 3056 CONECT 555 1211 CONECT 571 1120 CONECT 591 1255 CONECT 696 3056 CONECT 1120 571 CONECT 1211 555 CONECT 1255 591 CONECT 2646 2667 CONECT 2667 2646 CONECT 3056 411 696 3596 3598 CONECT 3056 3629 CONECT 3057 3060 3061 CONECT 3058 3061 3062 CONECT 3059 3060 3068 3081 CONECT 3060 3057 3059 3080 CONECT 3061 3057 3058 3084 CONECT 3062 3058 3063 3080 CONECT 3063 3062 3083 3088 CONECT 3064 3075 3085 CONECT 3065 3076 3077 CONECT 3066 3077 3078 3086 CONECT 3067 3078 CONECT 3068 3059 3069 CONECT 3069 3068 3070 CONECT 3070 3069 3074 CONECT 3071 3072 CONECT 3072 3071 3074 CONECT 3073 3078 CONECT 3074 3070 3072 3081 CONECT 3075 3064 3076 3086 CONECT 3076 3065 3075 CONECT 3077 3065 3066 CONECT 3078 3066 3067 3073 3079 CONECT 3079 3078 CONECT 3080 3060 3062 CONECT 3081 3059 3074 3082 CONECT 3082 3081 CONECT 3083 3063 3085 CONECT 3084 3061 CONECT 3085 3064 3083 3087 CONECT 3086 3066 3075 CONECT 3087 3085 3088 CONECT 3088 3063 3087 CONECT 3089 3090 3098 CONECT 3090 3089 3091 CONECT 3091 3090 3092 3116 CONECT 3092 3091 3093 CONECT 3093 3092 3094 3098 CONECT 3094 3093 3095 CONECT 3095 3094 3096 CONECT 3096 3095 3097 3102 CONECT 3097 3096 3098 3099 CONECT 3098 3089 3093 3097 3107 CONECT 3099 3097 3100 CONECT 3100 3099 3101 CONECT 3101 3100 3102 3105 3106 CONECT 3102 3096 3101 3103 CONECT 3103 3102 3104 CONECT 3104 3103 3105 CONECT 3105 3101 3104 3108 CONECT 3106 3101 CONECT 3107 3098 CONECT 3108 3105 3109 3110 CONECT 3109 3108 CONECT 3110 3108 3111 CONECT 3111 3110 3112 CONECT 3112 3111 3113 CONECT 3113 3112 3114 3115 CONECT 3114 3113 CONECT 3115 3113 CONECT 3116 3091 CONECT 3117 3118 3126 CONECT 3118 3117 3119 CONECT 3119 3118 3120 3144 CONECT 3120 3119 3121 CONECT 3121 3120 3122 3126 CONECT 3122 3121 3123 CONECT 3123 3122 3124 CONECT 3124 3123 3125 3130 CONECT 3125 3124 3126 3127 CONECT 3126 3117 3121 3125 3135 CONECT 3127 3125 3128 CONECT 3128 3127 3129 CONECT 3129 3128 3130 3133 3134 CONECT 3130 3124 3129 3131 CONECT 3131 3130 3132 CONECT 3132 3131 3133 CONECT 3133 3129 3132 3136 CONECT 3134 3129 CONECT 3135 3126 CONECT 3136 3133 3137 3138 CONECT 3137 3136 CONECT 3138 3136 3139 CONECT 3139 3138 3140 CONECT 3140 3139 3141 CONECT 3141 3140 3142 3143 CONECT 3142 3141 CONECT 3143 3141 CONECT 3144 3119 CONECT 3145 3146 3154 CONECT 3146 3145 3147 CONECT 3147 3146 3148 3172 CONECT 3148 3147 3149 CONECT 3149 3148 3150 3154 CONECT 3150 3149 3151 CONECT 3151 3150 3152 CONECT 3152 3151 3153 3158 CONECT 3153 3152 3154 3155 CONECT 3154 3145 3149 3153 3163 CONECT 3155 3153 3156 CONECT 3156 3155 3157 CONECT 3157 3156 3158 3161 3162 CONECT 3158 3152 3157 3159 CONECT 3159 3158 3160 CONECT 3160 3159 3161 CONECT 3161 3157 3160 3164 CONECT 3162 3157 CONECT 3163 3154 CONECT 3164 3161 3165 3166 CONECT 3165 3164 CONECT 3166 3164 3167 CONECT 3167 3166 3168 CONECT 3168 3167 3169 CONECT 3169 3168 3170 3171 CONECT 3170 3169 CONECT 3171 3169 CONECT 3172 3147 CONECT 3173 3174 3182 CONECT 3174 3173 3175 CONECT 3175 3174 3176 3200 CONECT 3176 3175 3177 CONECT 3177 3176 3178 3182 CONECT 3178 3177 3179 CONECT 3179 3178 3180 CONECT 3180 3179 3181 3186 CONECT 3181 3180 3182 3183 CONECT 3182 3173 3177 3181 3191 CONECT 3183 3181 3184 CONECT 3184 3183 3185 CONECT 3185 3184 3186 3189 3190 CONECT 3186 3180 3185 3187 CONECT 3187 3186 3188 CONECT 3188 3187 3189 CONECT 3189 3185 3188 3192 CONECT 3190 3185 CONECT 3191 3182 CONECT 3192 3189 3193 3194 CONECT 3193 3192 CONECT 3194 3192 3195 CONECT 3195 3194 3196 CONECT 3196 3195 3197 CONECT 3197 3196 3198 3199 CONECT 3198 3197 CONECT 3199 3197 CONECT 3200 3175 CONECT 3201 3202 3203 3204 CONECT 3202 3201 CONECT 3203 3201 CONECT 3204 3201 3205 CONECT 3205 3204 3206 CONECT 3206 3205 3207 CONECT 3207 3206 3208 CONECT 3208 3207 3209 CONECT 3209 3208 3210 CONECT 3210 3209 3211 CONECT 3211 3210 3212 CONECT 3212 3211 3213 CONECT 3213 3212 3214 CONECT 3214 3213 3215 CONECT 3215 3214 3216 CONECT 3216 3215 3217 CONECT 3217 3216 3218 CONECT 3218 3217 3219 CONECT 3219 3218 3220 CONECT 3220 3219 CONECT 3221 3222 3223 3224 CONECT 3222 3221 CONECT 3223 3221 CONECT 3224 3221 3225 CONECT 3225 3224 3226 CONECT 3226 3225 3227 CONECT 3227 3226 3228 CONECT 3228 3227 3229 CONECT 3229 3228 3230 CONECT 3230 3229 3231 CONECT 3231 3230 3232 CONECT 3232 3231 3233 CONECT 3233 3232 3234 CONECT 3234 3233 3235 CONECT 3235 3234 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 CONECT 3245 3246 3247 3248 CONECT 3246 3245 CONECT 3247 3245 CONECT 3248 3245 3249 CONECT 3249 3248 3250 CONECT 3250 3249 3251 CONECT 3251 3250 3252 CONECT 3252 3251 3253 CONECT 3253 3252 3254 CONECT 3254 3253 3255 CONECT 3255 3254 3256 CONECT 3256 3255 3257 CONECT 3257 3256 3258 CONECT 3258 3257 3259 CONECT 3259 3258 3260 CONECT 3260 3259 3261 CONECT 3261 3260 3262 CONECT 3262 3261 3263 CONECT 3263 3262 CONECT 3264 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 CONECT 3274 3275 3276 3277 CONECT 3275 3274 CONECT 3276 3274 CONECT 3277 3274 3278 CONECT 3278 3277 3279 CONECT 3279 3278 3280 CONECT 3280 3279 3281 CONECT 3281 3280 3282 CONECT 3282 3281 3283 CONECT 3283 3282 3284 CONECT 3284 3283 3285 CONECT 3285 3284 3286 CONECT 3286 3285 3287 CONECT 3287 3286 3288 CONECT 3288 3287 3289 CONECT 3289 3288 3290 CONECT 3290 3289 CONECT 3291 3292 CONECT 3292 3291 3293 CONECT 3293 3292 3294 CONECT 3294 3293 3295 CONECT 3295 3294 3296 CONECT 3296 3295 3297 CONECT 3297 3296 3298 CONECT 3298 3297 CONECT 3299 3300 CONECT 3300 3299 3301 CONECT 3301 3300 3302 CONECT 3302 3301 3303 CONECT 3303 3302 3304 CONECT 3304 3303 3305 CONECT 3305 3304 CONECT 3306 3307 3308 3309 CONECT 3307 3306 CONECT 3308 3306 CONECT 3309 3306 3310 CONECT 3310 3309 3311 CONECT 3311 3310 3312 CONECT 3312 3311 3313 CONECT 3313 3312 3314 CONECT 3314 3313 3315 CONECT 3315 3314 3316 CONECT 3316 3315 3317 CONECT 3317 3316 3318 CONECT 3318 3317 3319 CONECT 3319 3318 3320 CONECT 3320 3319 3321 CONECT 3321 3320 CONECT 3322 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 CONECT 3333 3334 CONECT 3334 3333 3335 CONECT 3335 3334 3336 CONECT 3336 3335 3337 CONECT 3337 3336 3338 CONECT 3338 3337 3339 CONECT 3339 3338 3340 CONECT 3340 3339 3341 CONECT 3341 3340 3342 CONECT 3342 3341 3343 CONECT 3343 3342 3344 CONECT 3344 3343 CONECT 3345 3346 3347 3348 CONECT 3346 3345 CONECT 3347 3345 CONECT 3348 3345 3349 CONECT 3349 3348 3350 CONECT 3350 3349 3351 CONECT 3351 3350 3352 CONECT 3352 3351 CONECT 3353 3354 3355 3356 CONECT 3354 3353 CONECT 3355 3353 CONECT 3356 3353 3357 CONECT 3357 3356 3358 CONECT 3358 3357 3359 CONECT 3359 3358 3360 CONECT 3360 3359 3361 CONECT 3361 3360 3362 CONECT 3362 3361 3363 CONECT 3363 3362 3364 CONECT 3364 3363 CONECT 3365 3366 3367 3368 CONECT 3366 3365 CONECT 3367 3365 CONECT 3368 3365 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 3376 CONECT 3376 3375 3377 CONECT 3377 3376 3378 CONECT 3378 3377 3379 CONECT 3379 3378 3380 CONECT 3380 3379 3381 CONECT 3381 3380 3382 CONECT 3382 3381 3383 CONECT 3383 3382 3384 CONECT 3384 3383 CONECT 3385 3386 3387 3388 CONECT 3386 3385 CONECT 3387 3385 CONECT 3388 3385 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 3396 CONECT 3396 3395 3397 CONECT 3397 3396 3398 CONECT 3398 3397 CONECT 3399 3400 3404 3405 CONECT 3400 3399 3401 CONECT 3401 3400 3402 CONECT 3402 3401 3403 CONECT 3403 3402 3411 CONECT 3404 3399 CONECT 3405 3399 3406 CONECT 3406 3405 3407 CONECT 3407 3406 3408 3409 CONECT 3408 3407 CONECT 3409 3407 3410 CONECT 3410 3409 CONECT 3411 3403 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 CONECT 3421 3422 3426 3427 CONECT 3422 3421 3423 CONECT 3423 3422 3424 CONECT 3424 3423 3425 CONECT 3425 3424 3433 CONECT 3426 3421 CONECT 3427 3421 3428 CONECT 3428 3427 3429 CONECT 3429 3428 3430 3431 CONECT 3430 3429 CONECT 3431 3429 3432 CONECT 3432 3431 CONECT 3433 3425 3434 CONECT 3434 3433 3435 CONECT 3435 3434 3436 CONECT 3436 3435 3437 CONECT 3437 3436 3438 CONECT 3438 3437 3439 CONECT 3439 3438 CONECT 3440 3441 3445 3446 CONECT 3441 3440 3442 CONECT 3442 3441 3443 CONECT 3443 3442 3444 CONECT 3444 3443 3452 CONECT 3445 3440 CONECT 3446 3440 3447 CONECT 3447 3446 3448 CONECT 3448 3447 3449 3450 CONECT 3449 3448 CONECT 3450 3448 3451 CONECT 3451 3450 CONECT 3452 3444 3453 CONECT 3453 3452 3454 CONECT 3454 3453 3455 CONECT 3455 3454 3456 CONECT 3456 3455 3457 CONECT 3457 3456 CONECT 3458 3461 CONECT 3459 3460 3462 CONECT 3460 3459 3463 CONECT 3461 3458 3465 CONECT 3462 3459 3466 CONECT 3463 3460 3467 CONECT 3464 3478 3480 CONECT 3465 3461 3468 CONECT 3466 3462 3469 CONECT 3467 3463 3470 CONECT 3468 3465 3471 CONECT 3469 3466 3471 CONECT 3470 3467 3472 CONECT 3471 3468 3469 CONECT 3472 3470 3473 CONECT 3473 3472 3474 CONECT 3474 3473 3475 CONECT 3475 3474 3477 CONECT 3476 3478 3482 CONECT 3477 3475 3479 3482 CONECT 3478 3464 3476 3481 CONECT 3479 3477 CONECT 3480 3464 CONECT 3481 3478 CONECT 3482 3476 3477 CONECT 3483 3484 3485 CONECT 3484 3483 3486 CONECT 3485 3483 3488 CONECT 3486 3484 3489 CONECT 3487 3497 3499 CONECT 3488 3485 CONECT 3489 3486 3490 CONECT 3490 3489 3491 CONECT 3491 3490 3492 CONECT 3492 3491 3493 CONECT 3493 3492 3494 CONECT 3494 3493 3496 CONECT 3495 3497 3501 CONECT 3496 3494 3498 3501 CONECT 3497 3487 3495 3500 CONECT 3498 3496 CONECT 3499 3487 CONECT 3500 3497 CONECT 3501 3495 3496 CONECT 3502 3503 3504 CONECT 3503 3502 3505 CONECT 3504 3502 3507 CONECT 3505 3503 3508 CONECT 3506 3518 3520 CONECT 3507 3504 3509 CONECT 3508 3505 3510 CONECT 3509 3507 3511 CONECT 3510 3508 3512 CONECT 3511 3509 CONECT 3512 3510 3513 CONECT 3513 3512 3514 CONECT 3514 3513 3515 CONECT 3515 3514 3517 CONECT 3516 3518 3522 CONECT 3517 3515 3519 3522 CONECT 3518 3506 3516 3521 CONECT 3519 3517 CONECT 3520 3506 CONECT 3521 3518 CONECT 3522 3516 3517 CONECT 3523 3524 CONECT 3524 3523 3525 CONECT 3525 3524 3527 CONECT 3526 3535 3537 CONECT 3527 3525 3528 CONECT 3528 3527 3529 CONECT 3529 3528 3530 CONECT 3530 3529 3531 CONECT 3531 3530 3532 CONECT 3532 3531 3534 CONECT 3533 3535 3539 CONECT 3534 3532 3536 3539 CONECT 3535 3526 3533 3538 CONECT 3536 3534 CONECT 3537 3526 CONECT 3538 3535 CONECT 3539 3533 3534 CONECT 3540 3543 CONECT 3541 3542 3544 CONECT 3542 3541 3545 CONECT 3543 3540 3547 CONECT 3544 3541 3548 CONECT 3545 3542 3549 CONECT 3546 3560 3562 CONECT 3547 3543 3550 CONECT 3548 3544 3551 CONECT 3549 3545 3552 CONECT 3550 3547 3553 CONECT 3551 3548 3553 CONECT 3552 3549 3554 CONECT 3553 3550 3551 CONECT 3554 3552 3555 CONECT 3555 3554 3556 CONECT 3556 3555 3557 CONECT 3557 3556 3559 CONECT 3558 3560 3564 CONECT 3559 3557 3561 3564 CONECT 3560 3546 3558 3563 CONECT 3561 3559 CONECT 3562 3546 CONECT 3563 3560 CONECT 3564 3558 3559 CONECT 3596 3056 CONECT 3598 3056 CONECT 3629 3056 MASTER 387 0 29 18 2 0 0 6 3617 1 523 34 END